data_9BY3
# 
_entry.id   9BY3 
# 
_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   9BY3         pdb_00009by3 10.2210/pdb9by3/pdb 
WWPDB D_1000284361 ?            ?                   
EMDB  EMD-45019    ?            ?                   
# 
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                        9BY3 
_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 3 model for product condition of Bacillus subtilis ribonucleotide reductase complex' EMD-45019 '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                   9BY3 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BY3 
_struct.title                        'Class 3 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        9BY3 
_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 9BY3 A 1  ? 700 ? P50620 1 ? 700 ? 1 700 
2 1 9BY3 B 1  ? 700 ? P50620 1 ? 700 ? 1 700 
3 2 9BY3 C 22 ? 350 ? P50621 1 ? 329 ? 1 329 
4 2 9BY3 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 9BY3 MET C 1  ? UNP P50621 ? ? 'initiating methionine' -20 1  
3 9BY3 GLY C 2  ? UNP P50621 ? ? 'expression tag'        -19 2  
3 9BY3 SER C 3  ? UNP P50621 ? ? 'expression tag'        -18 3  
3 9BY3 SER C 4  ? UNP P50621 ? ? 'expression tag'        -17 4  
3 9BY3 HIS C 5  ? UNP P50621 ? ? 'expression tag'        -16 5  
3 9BY3 HIS C 6  ? UNP P50621 ? ? 'expression tag'        -15 6  
3 9BY3 HIS C 7  ? UNP P50621 ? ? 'expression tag'        -14 7  
3 9BY3 HIS C 8  ? UNP P50621 ? ? 'expression tag'        -13 8  
3 9BY3 HIS C 9  ? UNP P50621 ? ? 'expression tag'        -12 9  
3 9BY3 HIS C 10 ? UNP P50621 ? ? 'expression tag'        -11 10 
3 9BY3 SER C 11 ? UNP P50621 ? ? 'expression tag'        -10 11 
3 9BY3 SER C 12 ? UNP P50621 ? ? 'expression tag'        -9  12 
3 9BY3 GLY C 13 ? UNP P50621 ? ? 'expression tag'        -8  13 
3 9BY3 LEU C 14 ? UNP P50621 ? ? 'expression tag'        -7  14 
3 9BY3 VAL C 15 ? UNP P50621 ? ? 'expression tag'        -6  15 
3 9BY3 PRO C 16 ? UNP P50621 ? ? 'expression tag'        -5  16 
3 9BY3 ARG C 17 ? UNP P50621 ? ? 'expression tag'        -4  17 
3 9BY3 GLY C 18 ? UNP P50621 ? ? 'expression tag'        -3  18 
3 9BY3 SER C 19 ? UNP P50621 ? ? 'expression tag'        -2  19 
3 9BY3 HIS C 20 ? UNP P50621 ? ? 'expression tag'        -1  20 
3 9BY3 MET C 21 ? UNP P50621 ? ? 'expression tag'        0   21 
4 9BY3 MET D 1  ? UNP P50621 ? ? 'initiating methionine' -20 22 
4 9BY3 GLY D 2  ? UNP P50621 ? ? 'expression tag'        -19 23 
4 9BY3 SER D 3  ? UNP P50621 ? ? 'expression tag'        -18 24 
4 9BY3 SER D 4  ? UNP P50621 ? ? 'expression tag'        -17 25 
4 9BY3 HIS D 5  ? UNP P50621 ? ? 'expression tag'        -16 26 
4 9BY3 HIS D 6  ? UNP P50621 ? ? 'expression tag'        -15 27 
4 9BY3 HIS D 7  ? UNP P50621 ? ? 'expression tag'        -14 28 
4 9BY3 HIS D 8  ? UNP P50621 ? ? 'expression tag'        -13 29 
4 9BY3 HIS D 9  ? UNP P50621 ? ? 'expression tag'        -12 30 
4 9BY3 HIS D 10 ? UNP P50621 ? ? 'expression tag'        -11 31 
4 9BY3 SER D 11 ? UNP P50621 ? ? 'expression tag'        -10 32 
4 9BY3 SER D 12 ? UNP P50621 ? ? 'expression tag'        -9  33 
4 9BY3 GLY D 13 ? UNP P50621 ? ? 'expression tag'        -8  34 
4 9BY3 LEU D 14 ? UNP P50621 ? ? 'expression tag'        -7  35 
4 9BY3 VAL D 15 ? UNP P50621 ? ? 'expression tag'        -6  36 
4 9BY3 PRO D 16 ? UNP P50621 ? ? 'expression tag'        -5  37 
4 9BY3 ARG D 17 ? UNP P50621 ? ? 'expression tag'        -4  38 
4 9BY3 GLY D 18 ? UNP P50621 ? ? 'expression tag'        -3  39 
4 9BY3 SER D 19 ? UNP P50621 ? ? 'expression tag'        -2  40 
4 9BY3 HIS D 20 ? UNP P50621 ? ? 'expression tag'        -1  41 
4 9BY3 MET D 21 ? UNP P50621 ? ? 'expression tag'        0   42 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 7   ? ASN A 14  ? PRO A 7   ASN A 14  1 ? 8  
HELX_P HELX_P2  AA2 GLU A 15  ? MET A 17  ? GLU A 15  MET A 17  5 ? 3  
HELX_P HELX_P3  AA3 ASP A 27  ? TYR A 40  ? ASP A 27  TYR A 40  1 ? 14 
HELX_P HELX_P4  AA4 TYR A 40  ? THR A 45  ? TYR A 40  THR A 45  1 ? 6  
HELX_P HELX_P5  AA5 ASN A 50  ? ASN A 61  ? ASN A 50  ASN A 61  1 ? 12 
HELX_P HELX_P6  AA6 GLU A 65  ? SER A 70  ? GLU A 65  SER A 70  1 ? 6  
HELX_P HELX_P7  AA7 SER A 73  ? LYS A 87  ? SER A 73  LYS A 87  1 ? 15 
HELX_P HELX_P8  AA8 SER A 93  ? TYR A 104 ? SER A 93  TYR A 104 1 ? 12 
HELX_P HELX_P9  AA9 ARG A 117 ? ASN A 131 ? ARG A 117 ASN A 131 1 ? 15 
HELX_P HELX_P10 AB1 ASP A 133 ? ASN A 146 ? ASP A 133 ASN A 146 1 ? 14 
HELX_P HELX_P11 AB2 SER A 152 ? ALA A 159 ? SER A 152 ALA A 159 1 ? 8  
HELX_P HELX_P12 AB3 SER A 178 ? LEU A 195 ? SER A 178 LEU A 195 1 ? 18 
HELX_P HELX_P13 AB4 GLY A 222 ? ALA A 237 ? GLY A 222 ALA A 237 1 ? 16 
HELX_P HELX_P14 AB5 ASP A 238 ? GLN A 242 ? ASP A 238 GLN A 242 5 ? 5  
HELX_P HELX_P15 AB6 ASP A 257 ? THR A 264 ? ASP A 257 THR A 264 1 ? 8  
HELX_P HELX_P16 AB7 PRO A 285 ? GLU A 294 ? PRO A 285 GLU A 294 1 ? 10 
HELX_P HELX_P17 AB8 TYR A 302 ? GLY A 311 ? TYR A 302 GLY A 311 1 ? 10 
HELX_P HELX_P18 AB9 HIS A 313 ? MET A 317 ? HIS A 313 MET A 317 5 ? 5  
HELX_P HELX_P19 AC1 ASP A 318 ? ASN A 329 ? ASP A 318 ASN A 329 1 ? 12 
HELX_P HELX_P20 AC2 ASN A 338 ? GLY A 354 ? ASN A 338 GLY A 354 1 ? 17 
HELX_P HELX_P21 AC3 GLN A 361 ? LYS A 366 ? GLN A 361 LYS A 366 1 ? 6  
HELX_P HELX_P22 AC4 ILE A 416 ? LYS A 423 ? ILE A 416 LYS A 423 1 ? 8  
HELX_P HELX_P23 AC5 SER A 424 ? THR A 443 ? SER A 424 THR A 443 1 ? 20 
HELX_P HELX_P24 AC6 ALA A 448 ? LYS A 459 ? ALA A 448 LYS A 459 1 ? 12 
HELX_P HELX_P25 AC7 ASN A 467 ? GLN A 474 ? ASN A 467 GLN A 474 1 ? 8  
HELX_P HELX_P26 AC8 SER A 481 ? GLY A 511 ? SER A 481 GLY A 511 1 ? 31 
HELX_P HELX_P27 AC9 SER A 520 ? GLY A 525 ? SER A 520 GLY A 525 1 ? 6  
HELX_P HELX_P28 AD1 PHE A 528 ? THR A 534 ? PHE A 528 THR A 534 1 ? 7  
HELX_P HELX_P29 AD2 TYR A 540 ? PHE A 547 ? TYR A 540 PHE A 547 1 ? 8  
HELX_P HELX_P30 AD3 THR A 554 ? GLY A 569 ? THR A 554 GLY A 569 1 ? 16 
HELX_P HELX_P31 AD4 SER A 583 ? GLN A 588 ? SER A 583 GLN A 588 1 ? 6  
HELX_P HELX_P32 AD5 GLU A 628 ? MET A 632 ? GLU A 628 MET A 632 5 ? 5  
HELX_P HELX_P33 AD6 ASP A 633 ? GLN A 646 ? ASP A 633 GLN A 646 1 ? 14 
HELX_P HELX_P34 AD7 THR A 663 ? ARG A 677 ? THR A 663 ARG A 677 1 ? 15 
HELX_P HELX_P35 AD8 PRO B 7   ? GLU B 15  ? PRO B 7   GLU B 15  1 ? 9  
HELX_P HELX_P36 AD9 ASP B 27  ? THR B 45  ? ASP B 27  THR B 45  1 ? 19 
HELX_P HELX_P37 AE1 ASN B 50  ? ASN B 61  ? ASN B 50  ASN B 61  1 ? 12 
HELX_P HELX_P38 AE2 GLU B 65  ? SER B 70  ? GLU B 65  SER B 70  1 ? 6  
HELX_P HELX_P39 AE3 SER B 73  ? LYS B 87  ? SER B 73  LYS B 87  1 ? 15 
HELX_P HELX_P40 AE4 SER B 93  ? TYR B 104 ? SER B 93  TYR B 104 1 ? 12 
HELX_P HELX_P41 AE5 ARG B 117 ? ASN B 131 ? ARG B 117 ASN B 131 1 ? 15 
HELX_P HELX_P42 AE6 ASP B 133 ? ASN B 146 ? ASP B 133 ASN B 146 1 ? 14 
HELX_P HELX_P43 AE7 SER B 152 ? ALA B 159 ? SER B 152 ALA B 159 1 ? 8  
HELX_P HELX_P44 AE8 SER B 178 ? LEU B 195 ? SER B 178 LEU B 195 1 ? 18 
HELX_P HELX_P45 AE9 GLY B 222 ? ALA B 237 ? GLY B 222 ALA B 237 1 ? 16 
HELX_P HELX_P46 AF1 ASP B 257 ? THR B 264 ? ASP B 257 THR B 264 1 ? 8  
HELX_P HELX_P47 AF2 PRO B 285 ? GLU B 294 ? PRO B 285 GLU B 294 1 ? 10 
HELX_P HELX_P48 AF3 TYR B 302 ? GLY B 311 ? TYR B 302 GLY B 311 1 ? 10 
HELX_P HELX_P49 AF4 HIS B 313 ? MET B 317 ? HIS B 313 MET B 317 5 ? 5  
HELX_P HELX_P50 AF5 ASP B 318 ? ASN B 329 ? ASP B 318 ASN B 329 1 ? 12 
HELX_P HELX_P51 AF6 ASN B 338 ? GLY B 354 ? ASN B 338 GLY B 354 1 ? 17 
HELX_P HELX_P52 AF7 GLN B 361 ? LYS B 366 ? GLN B 361 LYS B 366 1 ? 6  
HELX_P HELX_P53 AF8 ILE B 416 ? LYS B 423 ? ILE B 416 LYS B 423 1 ? 8  
HELX_P HELX_P54 AF9 SER B 424 ? THR B 443 ? SER B 424 THR B 443 1 ? 20 
HELX_P HELX_P55 AG1 ALA B 448 ? LYS B 459 ? ALA B 448 LYS B 459 1 ? 12 
HELX_P HELX_P56 AG2 ASN B 467 ? GLN B 474 ? ASN B 467 GLN B 474 1 ? 8  
HELX_P HELX_P57 AG3 SER B 481 ? GLY B 511 ? SER B 481 GLY B 511 1 ? 31 
HELX_P HELX_P58 AG4 SER B 520 ? GLY B 525 ? SER B 520 GLY B 525 1 ? 6  
HELX_P HELX_P59 AG5 PHE B 528 ? THR B 534 ? PHE B 528 THR B 534 1 ? 7  
HELX_P HELX_P60 AG6 TYR B 540 ? PHE B 547 ? TYR B 540 PHE B 547 1 ? 8  
HELX_P HELX_P61 AG7 THR B 554 ? GLY B 569 ? THR B 554 GLY B 569 1 ? 16 
HELX_P HELX_P62 AG8 SER B 583 ? GLN B 588 ? SER B 583 GLN B 588 1 ? 6  
HELX_P HELX_P63 AG9 ASP B 633 ? GLN B 646 ? ASP B 633 GLN B 646 1 ? 14 
HELX_P HELX_P64 AH1 THR B 663 ? ARG B 677 ? THR B 663 ARG B 677 1 ? 15 
HELX_P HELX_P65 AH2 PHE C 38  ? GLN C 49  ? PHE C 17  GLN C 28  1 ? 12 
HELX_P HELX_P66 AH3 LEU C 52  ? ILE C 56  ? LEU C 31  ILE C 35  5 ? 5  
HELX_P HELX_P67 AH4 LEU C 58  ? GLY C 60  ? LEU C 37  GLY C 39  5 ? 3  
HELX_P HELX_P68 AH5 ASP C 61  ? TYR C 67  ? ASP C 40  TYR C 46  1 ? 7  
HELX_P HELX_P69 AH6 GLY C 69  ? THR C 93  ? GLY C 48  THR C 72  1 ? 25 
HELX_P HELX_P70 AH7 THR C 93  ? VAL C 102 ? THR C 72  VAL C 81  1 ? 10 
HELX_P HELX_P71 AH8 GLY C 104 ? VAL C 121 ? GLY C 83  VAL C 100 1 ? 18 
HELX_P HELX_P72 AH9 VAL C 121 ? ALA C 134 ? VAL C 100 ALA C 113 1 ? 14 
HELX_P HELX_P73 AI1 PRO C 135 ? ASN C 149 ? PRO C 114 ASN C 128 1 ? 15 
HELX_P HELX_P74 AI2 ASN C 149 ? ALA C 165 ? ASN C 128 ALA C 144 1 ? 17 
HELX_P HELX_P75 AI3 ASP C 170 ? PHE C 187 ? ASP C 149 PHE C 166 1 ? 18 
HELX_P HELX_P76 AI4 PHE C 189 ? GLY C 201 ? PHE C 168 GLY C 180 1 ? 13 
HELX_P HELX_P77 AI5 LEU C 205 ? ASN C 235 ? LEU C 184 ASN C 214 1 ? 31 
HELX_P HELX_P78 AI6 THR C 238 ? ASP C 269 ? THR C 217 ASP C 248 1 ? 32 
HELX_P HELX_P79 AI7 GLN C 270 ? GLY C 272 ? GLN C 249 GLY C 251 5 ? 3  
HELX_P HELX_P80 AI8 LEU C 273 ? LEU C 292 ? LEU C 252 LEU C 271 1 ? 20 
HELX_P HELX_P81 AI9 ASN C 304 ? GLY C 310 ? ASN C 283 GLY C 289 1 ? 7  
HELX_P HELX_P82 AJ1 LYS C 337 ? TYR C 342 ? LYS C 316 TYR C 321 5 ? 6  
HELX_P HELX_P83 AJ2 PHE D 38  ? GLN D 49  ? PHE D 17  GLN D 28  1 ? 12 
HELX_P HELX_P84 AJ3 LEU D 52  ? ILE D 56  ? LEU D 31  ILE D 35  5 ? 5  
HELX_P HELX_P85 AJ4 LEU D 58  ? GLY D 60  ? LEU D 37  GLY D 39  5 ? 3  
HELX_P HELX_P86 AJ5 ASP D 61  ? LYS D 66  ? ASP D 40  LYS D 45  1 ? 6  
HELX_P HELX_P87 AJ6 GLY D 69  ? THR D 93  ? GLY D 48  THR D 72  1 ? 25 
HELX_P HELX_P88 AJ7 THR D 93  ? VAL D 102 ? THR D 72  VAL D 81  1 ? 10 
HELX_P HELX_P89 AJ8 GLY D 104 ? VAL D 121 ? GLY D 83  VAL D 100 1 ? 18 
HELX_P HELX_P90 AJ9 VAL D 121 ? ALA D 134 ? VAL D 100 ALA D 113 1 ? 14 
HELX_P HELX_P91 AK1 PRO D 135 ? ASN D 149 ? PRO D 114 ASN D 128 1 ? 15 
HELX_P HELX_P92 AK2 ASN D 149 ? ALA D 165 ? ASN D 128 ALA D 144 1 ? 17 
HELX_P HELX_P93 AK3 ASP D 170 ? PHE D 187 ? ASP D 149 PHE D 166 1 ? 18 
HELX_P HELX_P94 AK4 PHE D 189 ? GLY D 201 ? PHE D 168 GLY D 180 1 ? 13 
HELX_P HELX_P95 AK5 LEU D 205 ? ASN D 235 ? LEU D 184 ASN D 214 1 ? 31 
HELX_P HELX_P96 AK6 THR D 238 ? ASP D 269 ? THR D 217 ASP D 248 1 ? 32 
HELX_P HELX_P97 AK7 GLN D 270 ? GLY D 272 ? GLN D 249 GLY D 251 5 ? 3  
HELX_P HELX_P98 AK8 LEU D 273 ? LEU D 292 ? LEU D 252 LEU D 271 1 ? 20 
HELX_P HELX_P99 AK9 ASN D 304 ? LEU D 311 ? ASN D 283 LEU D 290 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? E TTP .   O2A ? ? ? 1_555 F MG . MG ? ? A TTP 801 A MG 802 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
metalc2  metalc ? ? E TTP .   O2B ? ? ? 1_555 F MG . MG ? ? A TTP 801 A MG 802 1_555 ? ? ? ? ? ? ? 2.471 ? ? 
metalc3  metalc ? ? E TTP .   O1G ? ? ? 1_555 F MG . MG ? ? A TTP 801 A MG 802 1_555 ? ? ? ? ? ? ? 2.484 ? ? 
metalc4  metalc ? ? I TTP .   O2A ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.343 ? ? 
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 ? ? ? ? ? ? ? 2.031 ? ? 
metalc7  metalc ? ? C GLU 118 OE2 ? ? ? 1_555 M MN . MN ? ? C GLU 97  C MN 401 1_555 ? ? ? ? ? ? ? 1.960 ? ? 
metalc8  metalc ? ? C GLU 118 OE1 ? ? ? 1_555 N MN . MN ? ? C GLU 97  C MN 402 1_555 ? ? ? ? ? ? ? 2.112 ? ? 
metalc9  metalc ? ? C HIS 122 ND1 ? ? ? 1_555 N MN . MN ? ? C HIS 101 C MN 402 1_555 ? ? ? ? ? ? ? 2.176 ? ? 
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 ? ? ? ? ? ? ? 1.966 ? ? 
metalc12 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 M MN . MN ? ? C GLU 198 C MN 401 1_555 ? ? ? ? ? ? ? 2.172 ? ? 
metalc13 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 N MN . MN ? ? C GLU 198 C MN 402 1_555 ? ? ? ? ? ? ? 2.711 ? ? 
metalc14 metalc ? ? C GLU 219 OE2 ? ? ? 1_555 N MN . MN ? ? C GLU 198 C MN 402 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc15 metalc ? ? C HIS 222 ND1 ? ? ? 1_555 M MN . MN ? ? C HIS 201 C MN 401 1_555 ? ? ? ? ? ? ? 2.409 ? ? 
metalc16 metalc ? ? D ASP 87  OD1 ? ? ? 1_555 P MN . MN ? ? D ASP 66  D MN 402 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc17 metalc ? ? D ASP 87  OD2 ? ? ? 1_555 P MN . MN ? ? D ASP 66  D MN 402 1_555 ? ? ? ? ? ? ? 2.156 ? ? 
metalc18 metalc ? ? D GLU 118 OE2 ? ? ? 1_555 O MN . MN ? ? D GLU 97  D MN 401 1_555 ? ? ? ? ? ? ? 1.912 ? ? 
metalc19 metalc ? ? D GLU 118 OE1 ? ? ? 1_555 P MN . MN ? ? D GLU 97  D MN 402 1_555 ? ? ? ? ? ? ? 1.990 ? ? 
metalc20 metalc ? ? D HIS 122 ND1 ? ? ? 1_555 P MN . MN ? ? D HIS 101 D MN 402 1_555 ? ? ? ? ? ? ? 2.147 ? ? 
metalc21 metalc ? ? D GLU 185 OE1 ? ? ? 1_555 O MN . MN ? ? D GLU 164 D MN 401 1_555 ? ? ? ? ? ? ? 2.303 ? ? 
metalc22 metalc ? ? D GLU 185 OE2 ? ? ? 1_555 O MN . MN ? ? D GLU 164 D MN 401 1_555 ? ? ? ? ? ? ? 2.317 ? ? 
metalc23 metalc ? ? D GLU 219 OE1 ? ? ? 1_555 O MN . MN ? ? D GLU 198 D MN 401 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc24 metalc ? ? D GLU 219 OE2 ? ? ? 1_555 P MN . MN ? ? D GLU 198 D MN 402 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
metalc25 metalc ? ? D HIS 222 ND1 ? ? ? 1_555 O MN . MN ? ? D HIS 201 D MN 401 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O2A ? E TTP .   ? A TTP 801 ? 1_555 MG ? F MG . ? A MG 802 ? 1_555 O2B ? E TTP .   ? A TTP 801 ? 1_555 72.0  ? 
2  O2A ? E TTP .   ? A TTP 801 ? 1_555 MG ? F MG . ? A MG 802 ? 1_555 O1G ? E TTP .   ? A TTP 801 ? 1_555 88.8  ? 
3  O2B ? E TTP .   ? A TTP 801 ? 1_555 MG ? F MG . ? A MG 802 ? 1_555 O1G ? E TTP .   ? A TTP 801 ? 1_555 68.1  ? 
4  O2A ? I TTP .   ? B TTP 801 ? 1_555 MG ? J MG . ? B MG 802 ? 1_555 O3G ? I TTP .   ? B TTP 801 ? 1_555 102.3 ? 
5  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE1 ? C GLU 118 ? C GLU 97  ? 1_555 89.6  ? 
6  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 120.6 ? 
7  OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 90.1  ? 
8  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 138.3 ? 
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_555 137.8 ? 
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_555 103.9 ? 
24 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 98.4  ? 
25 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 58.6  ? 
26 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 93.4  ? 
27 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 119.5 ? 
28 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 165.7 ? 
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_555 107.0 ? 
30 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 93.8  ? 
31 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 90.2  ? 
32 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 111.3 ? 
33 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 122.1 ? 
34 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 96.5  ? 
35 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 153.3 ? 
36 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 99.7  ? 
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_555 121.6 ? 
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_555 136.8 ? 
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 1.24  
2 TYR 355 B . ? TYR 355 B PRO 356 B ? PRO 356 B 1 -0.37 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 6 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 149 ? PRO A 151 ? TYR A 149 PRO A 151 
AA1 2 ASN A 410 ? ASN A 415 ? ASN A 410 ASN A 415 
AA1 3 ILE A 461 ? MET A 466 ? ILE A 461 MET A 466 
AA2 1 ILE A 407 ? SER A 408 ? ILE A 407 SER A 408 
AA2 2 CYS A 170 ? GLU A 174 ? CYS A 170 GLU A 174 
AA2 3 GLY A 198 ? ASN A 202 ? GLY A 198 ASN A 202 
AA2 4 GLY A 247 ? ASN A 252 ? GLY A 247 ASN A 252 
AA2 5 LEU A 278 ? ILE A 284 ? LEU A 278 ILE A 284 
AA2 6 TYR A 357 ? PHE A 360 ? TYR A 357 PHE A 360 
AA2 7 THR A 681 ? ILE A 682 ? THR A 681 ILE A 682 
AA3 1 ALA A 298 ? PHE A 301 ? ALA A 298 PHE A 301 
AA3 2 LYS A 334 ? ILE A 337 ? LYS A 334 ILE A 337 
AA4 1 ILE A 601 ? TYR A 606 ? ILE A 601 TYR A 606 
AA4 2 SER A 609 ? PRO A 614 ? SER A 609 PRO A 614 
AA5 1 THR A 655 ? LEU A 658 ? THR A 655 LEU A 658 
AA5 2 TYR A 684 ? THR A 687 ? TYR A 684 THR A 687 
AA6 1 TYR B 149 ? PRO B 151 ? TYR B 149 PRO B 151 
AA6 2 ASN B 410 ? ASN B 415 ? ASN B 410 ASN B 415 
AA6 3 ILE B 461 ? MET B 466 ? ILE B 461 MET B 466 
AA7 1 CYS B 170 ? GLU B 174 ? CYS B 170 GLU B 174 
AA7 2 GLY B 198 ? ASN B 202 ? GLY B 198 ASN B 202 
AA7 3 GLY B 247 ? ASN B 252 ? GLY B 247 ASN B 252 
AA7 4 LEU B 278 ? ILE B 284 ? LEU B 278 ILE B 284 
AA7 5 TYR B 357 ? PHE B 360 ? TYR B 357 PHE B 360 
AA7 6 THR B 681 ? ILE B 682 ? THR B 681 ILE B 682 
AA8 1 ALA B 298 ? PHE B 301 ? ALA B 298 PHE B 301 
AA8 2 LYS B 334 ? ILE B 337 ? LYS B 334 ILE B 337 
AA9 1 ILE B 601 ? TYR B 606 ? ILE B 601 TYR B 606 
AA9 2 SER B 609 ? PRO B 614 ? SER B 609 PRO B 614 
AB1 1 THR B 655 ? LEU B 658 ? THR B 655 LEU B 658 
AB1 2 TYR B 684 ? THR B 687 ? TYR B 684 THR B 687 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLN A 150 ? N GLN A 150 O SER A 413 ? O SER A 413 
AA1 2 3 N GLY A 412 ? N GLY A 412 O GLY A 464 ? O GLY A 464 
AA2 1 2 O ILE A 407 ? O ILE A 407 N LEU A 172 ? N LEU A 172 
AA2 2 3 N LEU A 173 ? N LEU A 173 O SER A 200 ? O SER A 200 
AA2 3 4 N LEU A 201 ? N LEU A 201 O ALA A 248 ? O ALA A 248 
AA2 4 5 N GLY A 247 ? N GLY A 247 O SER A 279 ? O SER A 279 
AA2 5 6 N VAL A 282 ? N VAL A 282 O TYR A 357 ? O TYR A 357 
AA2 6 7 N ILE A 358 ? N ILE A 358 O ILE A 682 ? O ILE A 682 
AA3 1 2 N VAL A 300 ? N VAL A 300 O GLU A 335 ? O GLU A 335 
AA4 1 2 N GLU A 602 ? N GLU A 602 O TYR A 613 ? O TYR A 613 
AA5 1 2 N LEU A 656 ? N LEU A 656 O TYR A 684 ? O TYR A 684 
AA6 1 2 N GLN B 150 ? N GLN B 150 O SER B 413 ? O SER B 413 
AA6 2 3 N GLY B 412 ? N GLY B 412 O GLY B 464 ? O GLY B 464 
AA7 1 2 N LEU B 173 ? N LEU B 173 O SER B 200 ? O SER B 200 
AA7 2 3 N LEU B 201 ? N LEU B 201 O TYR B 250 ? O TYR B 250 
AA7 3 4 N GLY B 247 ? N GLY B 247 O SER B 279 ? O SER B 279 
AA7 4 5 N VAL B 282 ? N VAL B 282 O TYR B 357 ? O TYR B 357 
AA7 5 6 N ILE B 358 ? N ILE B 358 O ILE B 682 ? O ILE B 682 
AA8 1 2 N ALA B 298 ? N ALA B 298 O ILE B 337 ? O ILE B 337 
AA9 1 2 N ARG B 604 ? N ARG B 604 O THR B 611 ? O THR B 611 
AB1 1 2 N LEU B 656 ? N LEU B 656 O TYR B 684 ? O TYR B 684 
# 
_pdbx_entry_details.entry_id                   9BY3 
_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 ? ? 72.05   -7.42   
2  1 SER A 593 ? ? 59.63   -154.82 
3  1 SER A 653 ? ? -68.94  99.32   
4  1 ASP B 215 ? ? 79.70   -0.92   
5  1 ASP B 238 ? ? -95.44  31.32   
6  1 SER B 408 ? ? -160.48 113.47  
7  1 SER B 593 ? ? 58.51   -151.24 
8  1 THR C 72  ? ? -128.00 -59.08  
9  1 ASP C 148 ? ? 58.10   15.67   
10 1 PHE C 166 ? ? -125.64 -60.85  
11 1 THR D 72  ? ? -128.16 -58.51  
12 1 PHE D 166 ? ? -144.22 -61.12  
13 1 THR D 311 ? ? -168.72 115.97  
14 1 ASP D 317 ? ? 61.70   167.61  
15 1 ASP D 318 ? ? 67.23   -4.16   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BY3 
_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                    9BY3 
_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                  3.57 
_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               56000 
_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                        9BY3 
_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              9BY3 
_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                9BY3 
_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              9BY3 
_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           9BY3 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              'Class 3 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                    9BY3 
_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   ? 103.628 117.527 98.889  1.00 63.04 ?  6   VAL A N     1 
ATOM   2     C  CA    . VAL A 1 6   ? 104.939 118.015 98.484  1.00 62.74 ?  6   VAL A CA    1 
ATOM   3     C  C     . VAL A 1 6   ? 104.771 119.168 97.494  1.00 63.36 ?  6   VAL A C     1 
ATOM   4     O  O     . VAL A 1 6   ? 103.866 119.149 96.655  1.00 63.20 ?  6   VAL A O     1 
ATOM   5     C  CB    . VAL A 1 6   ? 105.801 116.863 97.897  1.00 64.24 ?  6   VAL A CB    1 
ATOM   6     C  CG1   . VAL A 1 6   ? 105.532 116.658 96.409  1.00 62.93 ?  6   VAL A CG1   1 
ATOM   7     C  CG2   . VAL A 1 6   ? 107.278 117.107 98.152  1.00 61.49 ?  6   VAL A CG2   1 
ATOM   8     N  N     . PRO A 1 7   ? 105.604 120.201 97.625  1.00 58.77 ?  7   PRO A N     1 
ATOM   9     C  CA    . PRO A 1 7   ? 105.569 121.295 96.650  1.00 54.02 ?  7   PRO A CA    1 
ATOM   10    C  C     . PRO A 1 7   ? 105.928 120.800 95.259  1.00 56.48 ?  7   PRO A C     1 
ATOM   11    O  O     . PRO A 1 7   ? 106.750 119.898 95.088  1.00 60.50 ?  7   PRO A O     1 
ATOM   12    C  CB    . PRO A 1 7   ? 106.616 122.278 97.183  1.00 55.37 ?  7   PRO A CB    1 
ATOM   13    C  CG    . PRO A 1 7   ? 106.674 121.999 98.642  1.00 57.08 ?  7   PRO A CG    1 
ATOM   14    C  CD    . PRO A 1 7   ? 106.469 120.517 98.774  1.00 57.20 ?  7   PRO A CD    1 
ATOM   15    N  N     . LYS A 1 8   ? 105.290 121.401 94.254  1.00 58.03 ?  8   LYS A N     1 
ATOM   16    C  CA    . LYS A 1 8   ? 105.535 120.986 92.877  1.00 56.12 ?  8   LYS A CA    1 
ATOM   17    C  C     . LYS A 1 8   ? 106.963 121.293 92.452  1.00 57.08 ?  8   LYS A C     1 
ATOM   18    O  O     . LYS A 1 8   ? 107.587 120.508 91.727  1.00 57.57 ?  8   LYS A O     1 
ATOM   19    C  CB    . LYS A 1 8   ? 104.540 121.665 91.936  1.00 55.64 ?  8   LYS A CB    1 
ATOM   20    C  CG    . LYS A 1 8   ? 104.378 120.955 90.603  1.00 56.25 ?  8   LYS A CG    1 
ATOM   21    C  CD    . LYS A 1 8   ? 104.138 121.940 89.475  1.00 57.80 ?  8   LYS A CD    1 
ATOM   22    C  CE    . LYS A 1 8   ? 104.331 121.282 88.120  1.00 57.13 ?  8   LYS A CE    1 
ATOM   23    N  NZ    . LYS A 1 8   ? 104.854 122.240 87.109  1.00 58.95 1  8   LYS A NZ    1 
ATOM   24    N  N     . TRP A 1 9   ? 107.499 122.433 92.892  1.00 57.42 ?  9   TRP A N     1 
ATOM   25    C  CA    . TRP A 1 9   ? 108.824 122.840 92.442  1.00 52.16 ?  9   TRP A CA    1 
ATOM   26    C  C     . TRP A 1 9   ? 109.914 121.957 93.035  1.00 54.06 ?  9   TRP A C     1 
ATOM   27    O  O     . TRP A 1 9   ? 110.885 121.624 92.346  1.00 57.94 ?  9   TRP A O     1 
ATOM   28    C  CB    . TRP A 1 9   ? 109.069 124.310 92.774  1.00 53.77 ?  9   TRP A CB    1 
ATOM   29    C  CG    . TRP A 1 9   ? 108.769 124.698 94.181  1.00 50.50 ?  9   TRP A CG    1 
ATOM   30    C  CD1   . TRP A 1 9   ? 109.615 124.633 95.242  1.00 51.38 ?  9   TRP A CD1   1 
ATOM   31    C  CD2   . TRP A 1 9   ? 107.538 125.227 94.681  1.00 51.33 ?  9   TRP A CD2   1 
ATOM   32    N  NE1   . TRP A 1 9   ? 108.989 125.081 96.378  1.00 52.90 ?  9   TRP A NE1   1 
ATOM   33    C  CE2   . TRP A 1 9   ? 107.711 125.455 96.060  1.00 52.26 ?  9   TRP A CE2   1 
ATOM   34    C  CE3   . TRP A 1 9   ? 106.305 125.529 94.098  1.00 51.69 ?  9   TRP A CE3   1 
ATOM   35    C  CZ2   . TRP A 1 9   ? 106.699 125.967 96.864  1.00 52.47 ?  9   TRP A CZ2   1 
ATOM   36    C  CZ3   . TRP A 1 9   ? 105.303 126.037 94.896  1.00 55.31 ?  9   TRP A CZ3   1 
ATOM   37    C  CH2   . TRP A 1 9   ? 105.505 126.253 96.264  1.00 54.90 ?  9   TRP A CH2   1 
ATOM   38    N  N     . ILE A 1 10  ? 109.781 121.557 94.303  1.00 54.45 ?  10  ILE A N     1 
ATOM   39    C  CA    . ILE A 1 10  ? 110.775 120.646 94.862  1.00 57.23 ?  10  ILE A CA    1 
ATOM   40    C  C     . ILE A 1 10  ? 110.575 119.224 94.359  1.00 55.75 ?  10  ILE A C     1 
ATOM   41    O  O     . ILE A 1 10  ? 111.528 118.435 94.366  1.00 59.01 ?  10  ILE A O     1 
ATOM   42    C  CB    . ILE A 1 10  ? 110.789 120.643 96.402  1.00 56.46 ?  10  ILE A CB    1 
ATOM   43    C  CG1   . ILE A 1 10  ? 109.811 119.615 96.967  1.00 58.14 ?  10  ILE A CG1   1 
ATOM   44    C  CG2   . ILE A 1 10  ? 110.499 122.020 96.958  1.00 55.14 ?  10  ILE A CG2   1 
ATOM   45    C  CD1   . ILE A 1 10  ? 110.023 119.341 98.435  1.00 58.28 ?  10  ILE A CD1   1 
ATOM   46    N  N     . GLN A 1 11  ? 109.365 118.871 93.924  1.00 57.10 ?  11  GLN A N     1 
ATOM   47    C  CA    . GLN A 1 11  ? 109.178 117.585 93.263  1.00 57.23 ?  11  GLN A CA    1 
ATOM   48    C  C     . GLN A 1 11  ? 109.875 117.566 91.909  1.00 56.41 ?  11  GLN A C     1 
ATOM   49    O  O     . GLN A 1 11  ? 110.522 116.577 91.551  1.00 58.51 ?  11  GLN A O     1 
ATOM   50    C  CB    . GLN A 1 11  ? 107.686 117.284 93.117  1.00 59.25 ?  11  GLN A CB    1 
ATOM   51    C  CG    . GLN A 1 11  ? 107.367 116.153 92.159  1.00 60.60 ?  11  GLN A CG    1 
ATOM   52    C  CD    . GLN A 1 11  ? 106.576 116.622 90.957  1.00 61.60 ?  11  GLN A CD    1 
ATOM   53    O  OE1   . GLN A 1 11  ? 105.593 117.349 91.093  1.00 60.15 ?  11  GLN A OE1   1 
ATOM   54    N  NE2   . GLN A 1 11  ? 107.004 116.211 89.769  1.00 60.38 ?  11  GLN A NE2   1 
ATOM   55    N  N     . LEU A 1 12  ? 109.761 118.659 91.151  1.00 56.36 ?  12  LEU A N     1 
ATOM   56    C  CA    . LEU A 1 12  ? 110.486 118.774 89.888  1.00 55.06 ?  12  LEU A CA    1 
ATOM   57    C  C     . LEU A 1 12  ? 111.991 118.817 90.118  1.00 57.48 ?  12  LEU A C     1 
ATOM   58    O  O     . LEU A 1 12  ? 112.763 118.262 89.327  1.00 59.89 ?  12  LEU A O     1 
ATOM   59    C  CB    . LEU A 1 12  ? 110.028 120.021 89.136  1.00 55.96 ?  12  LEU A CB    1 
ATOM   60    C  CG    . LEU A 1 12  ? 108.918 119.848 88.100  1.00 56.90 ?  12  LEU A CG    1 
ATOM   61    C  CD1   . LEU A 1 12  ? 108.169 121.155 87.910  1.00 55.45 ?  12  LEU A CD1   1 
ATOM   62    C  CD2   . LEU A 1 12  ? 109.492 119.359 86.782  1.00 57.52 ?  12  LEU A CD2   1 
ATOM   63    N  N     . ASN A 1 13  ? 112.427 119.482 91.190  1.00 56.01 ?  13  ASN A N     1 
ATOM   64    C  CA    . ASN A 1 13  ? 113.850 119.583 91.484  1.00 52.82 ?  13  ASN A CA    1 
ATOM   65    C  C     . ASN A 1 13  ? 114.442 118.235 91.873  1.00 54.86 ?  13  ASN A C     1 
ATOM   66    O  O     . ASN A 1 13  ? 115.638 118.003 91.668  1.00 60.62 ?  13  ASN A O     1 
ATOM   67    C  CB    . ASN A 1 13  ? 114.077 120.610 92.595  1.00 56.25 ?  13  ASN A CB    1 
ATOM   68    C  CG    . ASN A 1 13  ? 115.527 120.699 93.021  1.00 56.13 ?  13  ASN A CG    1 
ATOM   69    O  OD1   . ASN A 1 13  ? 115.915 120.162 94.058  1.00 54.72 ?  13  ASN A OD1   1 
ATOM   70    N  ND2   . ASN A 1 13  ? 116.337 121.382 92.222  1.00 55.92 ?  13  ASN A ND2   1 
ATOM   71    N  N     . ASN A 1 14  ? 113.629 117.339 92.431  1.00 57.72 ?  14  ASN A N     1 
ATOM   72    C  CA    . ASN A 1 14  ? 114.100 116.008 92.784  1.00 58.51 ?  14  ASN A CA    1 
ATOM   73    C  C     . ASN A 1 14  ? 114.176 115.071 91.587  1.00 57.77 ?  14  ASN A C     1 
ATOM   74    O  O     . ASN A 1 14  ? 114.752 113.986 91.708  1.00 60.03 ?  14  ASN A O     1 
ATOM   75    C  CB    . ASN A 1 14  ? 113.200 115.398 93.861  1.00 56.46 ?  14  ASN A CB    1 
ATOM   76    C  CG    . ASN A 1 14  ? 113.466 115.975 95.235  1.00 58.69 ?  14  ASN A CG    1 
ATOM   77    O  OD1   . ASN A 1 14  ? 113.808 117.148 95.372  1.00 60.90 ?  14  ASN A OD1   1 
ATOM   78    N  ND2   . ASN A 1 14  ? 113.308 115.151 96.264  1.00 59.30 ?  14  ASN A ND2   1 
ATOM   79    N  N     . GLU A 1 15  ? 113.616 115.458 90.442  1.00 57.87 ?  15  GLU A N     1 
ATOM   80    C  CA    . GLU A 1 15  ? 113.727 114.661 89.228  1.00 59.07 ?  15  GLU A CA    1 
ATOM   81    C  C     . GLU A 1 15  ? 115.090 114.793 88.562  1.00 61.72 ?  15  GLU A C     1 
ATOM   82    O  O     . GLU A 1 15  ? 115.337 114.116 87.559  1.00 63.52 ?  15  GLU A O     1 
ATOM   83    C  CB    . GLU A 1 15  ? 112.626 115.046 88.235  1.00 59.34 ?  15  GLU A CB    1 
ATOM   84    C  CG    . GLU A 1 15  ? 111.251 115.183 88.863  1.00 60.15 ?  15  GLU A CG    1 
ATOM   85    C  CD    . GLU A 1 15  ? 110.132 115.159 87.841  1.00 63.73 ?  15  GLU A CD    1 
ATOM   86    O  OE1   . GLU A 1 15  ? 110.427 115.236 86.632  1.00 63.57 ?  15  GLU A OE1   1 
ATOM   87    O  OE2   . GLU A 1 15  ? 108.956 115.065 88.250  1.00 63.84 -1 15  GLU A OE2   1 
ATOM   88    N  N     . ILE A 1 16  ? 115.965 115.655 89.083  1.00 59.98 ?  16  ILE A N     1 
ATOM   89    C  CA    . ILE A 1 16  ? 117.329 115.733 88.569  1.00 59.72 ?  16  ILE A CA    1 
ATOM   90    C  C     . ILE A 1 16  ? 118.065 114.424 88.819  1.00 59.78 ?  16  ILE A C     1 
ATOM   91    O  O     . ILE A 1 16  ? 118.778 113.916 87.945  1.00 61.09 ?  16  ILE A O     1 
ATOM   92    C  CB    . ILE A 1 16  ? 118.071 116.927 89.198  1.00 58.93 ?  16  ILE A CB    1 
ATOM   93    C  CG1   . ILE A 1 16  ? 117.352 118.237 88.880  1.00 57.54 ?  16  ILE A CG1   1 
ATOM   94    C  CG2   . ILE A 1 16  ? 119.513 116.981 88.714  1.00 59.58 ?  16  ILE A CG2   1 
ATOM   95    C  CD1   . ILE A 1 16  ? 117.853 119.415 89.682  1.00 56.90 ?  16  ILE A CD1   1 
ATOM   96    N  N     . MET A 1 17  ? 117.896 113.853 90.012  1.00 60.50 ?  17  MET A N     1 
ATOM   97    C  CA    . MET A 1 17  ? 118.604 112.635 90.378  1.00 61.98 ?  17  MET A CA    1 
ATOM   98    C  C     . MET A 1 17  ? 118.020 111.390 89.728  1.00 62.80 ?  17  MET A C     1 
ATOM   99    O  O     . MET A 1 17  ? 118.710 110.367 89.656  1.00 63.98 ?  17  MET A O     1 
ATOM   100   C  CB    . MET A 1 17  ? 118.602 112.468 91.896  1.00 61.29 ?  17  MET A CB    1 
ATOM   101   C  CG    . MET A 1 17  ? 119.070 113.703 92.631  1.00 61.55 ?  17  MET A CG    1 
ATOM   102   S  SD    . MET A 1 17  ? 120.610 114.371 91.973  1.00 68.12 ?  17  MET A SD    1 
ATOM   103   C  CE    . MET A 1 17  ? 121.813 113.385 92.860  1.00 61.05 ?  17  MET A CE    1 
ATOM   104   N  N     . ILE A 1 18  ? 116.776 111.443 89.258  1.00 62.62 ?  18  ILE A N     1 
ATOM   105   C  CA    . ILE A 1 18  ? 116.203 110.315 88.529  1.00 64.44 ?  18  ILE A CA    1 
ATOM   106   C  C     . ILE A 1 18  ? 116.934 110.219 87.194  1.00 65.28 ?  18  ILE A C     1 
ATOM   107   O  O     . ILE A 1 18  ? 116.745 111.056 86.307  1.00 66.44 ?  18  ILE A O     1 
ATOM   108   C  CB    . ILE A 1 18  ? 114.686 110.458 88.332  1.00 65.30 ?  18  ILE A CB    1 
ATOM   109   C  CG1   . ILE A 1 18  ? 113.880 110.210 89.625  1.00 64.60 ?  18  ILE A CG1   1 
ATOM   110   C  CG2   . ILE A 1 18  ? 114.195 109.501 87.251  1.00 64.87 ?  18  ILE A CG2   1 
ATOM   111   C  CD1   . ILE A 1 18  ? 114.341 110.903 90.893  1.00 64.07 ?  18  ILE A CD1   1 
ATOM   112   N  N     . GLN A 1 19  ? 117.787 109.208 87.058  1.00 68.96 ?  19  GLN A N     1 
ATOM   113   C  CA    . GLN A 1 19  ? 118.648 109.086 85.889  1.00 70.00 ?  19  GLN A CA    1 
ATOM   114   C  C     . GLN A 1 19  ? 117.856 108.505 84.726  1.00 69.78 ?  19  GLN A C     1 
ATOM   115   O  O     . GLN A 1 19  ? 117.424 107.349 84.774  1.00 71.76 ?  19  GLN A O     1 
ATOM   116   C  CB    . GLN A 1 19  ? 119.859 108.215 86.210  1.00 72.02 ?  19  GLN A CB    1 
ATOM   117   C  CG    . GLN A 1 19  ? 120.833 108.853 87.189  1.00 70.29 ?  19  GLN A CG    1 
ATOM   118   C  CD    . GLN A 1 19  ? 122.052 107.991 87.450  1.00 71.59 ?  19  GLN A CD    1 
ATOM   119   O  OE1   . GLN A 1 19  ? 122.179 106.894 86.908  1.00 71.28 ?  19  GLN A OE1   1 
ATOM   120   N  NE2   . GLN A 1 19  ? 122.957 108.485 88.288  1.00 71.39 ?  19  GLN A NE2   1 
ATOM   121   N  N     . LYS A 1 20  ? 117.666 109.308 83.684  1.00 71.28 ?  20  LYS A N     1 
ATOM   122   C  CA    . LYS A 1 20  ? 116.978 108.889 82.472  1.00 73.11 ?  20  LYS A CA    1 
ATOM   123   C  C     . LYS A 1 20  ? 118.012 108.719 81.368  1.00 73.64 ?  20  LYS A C     1 
ATOM   124   O  O     . LYS A 1 20  ? 118.763 109.655 81.072  1.00 73.55 ?  20  LYS A O     1 
ATOM   125   C  CB    . LYS A 1 20  ? 115.909 109.904 82.069  1.00 71.82 ?  20  LYS A CB    1 
ATOM   126   C  CG    . LYS A 1 20  ? 115.304 109.658 80.698  1.00 72.49 ?  20  LYS A CG    1 
ATOM   127   C  CD    . LYS A 1 20  ? 115.122 110.958 79.934  1.00 73.53 ?  20  LYS A CD    1 
ATOM   128   C  CE    . LYS A 1 20  ? 116.392 111.792 79.951  1.00 73.84 ?  20  LYS A CE    1 
ATOM   129   N  NZ    . LYS A 1 20  ? 117.531 111.082 79.308  1.00 73.93 1  20  LYS A NZ    1 
ATOM   130   N  N     . ASP A 1 21  ? 118.047 107.527 80.770  1.00 72.18 ?  21  ASP A N     1 
ATOM   131   C  CA    . ASP A 1 21  ? 119.024 107.185 79.735  1.00 73.50 ?  21  ASP A CA    1 
ATOM   132   C  C     . ASP A 1 21  ? 120.455 107.330 80.252  1.00 74.05 ?  21  ASP A C     1 
ATOM   133   O  O     . ASP A 1 21  ? 121.361 107.736 79.523  1.00 72.09 ?  21  ASP A O     1 
ATOM   134   C  CB    . ASP A 1 21  ? 118.814 108.025 78.472  1.00 73.43 ?  21  ASP A CB    1 
ATOM   135   C  CG    . ASP A 1 21  ? 117.357 108.101 78.061  1.00 74.57 ?  21  ASP A CG    1 
ATOM   136   O  OD1   . ASP A 1 21  ? 116.645 107.084 78.193  1.00 72.61 ?  21  ASP A OD1   1 
ATOM   137   O  OD2   . ASP A 1 21  ? 116.924 109.181 77.606  1.00 74.27 -1 21  ASP A OD2   1 
ATOM   138   N  N     . GLY A 1 22  ? 120.657 106.993 81.524  1.00 73.98 ?  22  GLY A N     1 
ATOM   139   C  CA    . GLY A 1 22  ? 121.980 107.011 82.114  1.00 74.01 ?  22  GLY A CA    1 
ATOM   140   C  C     . GLY A 1 22  ? 122.532 108.380 82.438  1.00 73.96 ?  22  GLY A C     1 
ATOM   141   O  O     . GLY A 1 22  ? 123.725 108.489 82.742  1.00 72.73 ?  22  GLY A O     1 
ATOM   142   N  N     . LYS A 1 23  ? 121.712 109.427 82.388  1.00 70.77 ?  23  LYS A N     1 
ATOM   143   C  CA    . LYS A 1 23  ? 122.164 110.784 82.646  1.00 68.48 ?  23  LYS A CA    1 
ATOM   144   C  C     . LYS A 1 23  ? 121.237 111.465 83.640  1.00 69.58 ?  23  LYS A C     1 
ATOM   145   O  O     . LYS A 1 23  ? 120.036 111.184 83.687  1.00 70.55 ?  23  LYS A O     1 
ATOM   146   C  CB    . LYS A 1 23  ? 122.220 111.615 81.357  1.00 68.39 ?  23  LYS A CB    1 
ATOM   147   C  CG    . LYS A 1 23  ? 123.296 111.193 80.374  1.00 68.46 ?  23  LYS A CG    1 
ATOM   148   C  CD    . LYS A 1 23  ? 123.320 112.129 79.177  1.00 68.57 ?  23  LYS A CD    1 
ATOM   149   C  CE    . LYS A 1 23  ? 124.308 111.668 78.124  1.00 68.95 ?  23  LYS A CE    1 
ATOM   150   N  NZ    . LYS A 1 23  ? 124.281 112.553 76.926  1.00 67.63 1  23  LYS A NZ    1 
ATOM   151   N  N     . PHE A 1 24  ? 121.809 112.364 84.436  1.00 63.30 ?  24  PHE A N     1 
ATOM   152   C  CA    . PHE A 1 24  ? 121.005 113.203 85.313  1.00 60.09 ?  24  PHE A CA    1 
ATOM   153   C  C     . PHE A 1 24  ? 120.139 114.143 84.485  1.00 60.84 ?  24  PHE A C     1 
ATOM   154   O  O     . PHE A 1 24  ? 120.573 114.670 83.458  1.00 59.40 ?  24  PHE A O     1 
ATOM   155   C  CB    . PHE A 1 24  ? 121.900 114.014 86.250  1.00 58.54 ?  24  PHE A CB    1 
ATOM   156   C  CG    . PHE A 1 24  ? 122.558 113.197 87.320  1.00 59.92 ?  24  PHE A CG    1 
ATOM   157   C  CD1   . PHE A 1 24  ? 121.886 112.896 88.491  1.00 60.45 ?  24  PHE A CD1   1 
ATOM   158   C  CD2   . PHE A 1 24  ? 123.853 112.737 87.158  1.00 59.89 ?  24  PHE A CD2   1 
ATOM   159   C  CE1   . PHE A 1 24  ? 122.492 112.147 89.479  1.00 60.18 ?  24  PHE A CE1   1 
ATOM   160   C  CE2   . PHE A 1 24  ? 124.463 111.988 88.144  1.00 59.21 ?  24  PHE A CE2   1 
ATOM   161   C  CZ    . PHE A 1 24  ? 123.782 111.693 89.305  1.00 60.10 ?  24  PHE A CZ    1 
ATOM   162   N  N     . GLN A 1 25  ? 118.903 114.350 84.938  1.00 61.85 ?  25  GLN A N     1 
ATOM   163   C  CA    . GLN A 1 25  ? 117.976 115.253 84.257  1.00 59.76 ?  25  GLN A CA    1 
ATOM   164   C  C     . GLN A 1 25  ? 118.222 116.665 84.779  1.00 60.95 ?  25  GLN A C     1 
ATOM   165   O  O     . GLN A 1 25  ? 117.520 117.178 85.652  1.00 61.19 ?  25  GLN A O     1 
ATOM   166   C  CB    . GLN A 1 25  ? 116.536 114.805 84.468  1.00 61.01 ?  25  GLN A CB    1 
ATOM   167   C  CG    . GLN A 1 25  ? 116.251 113.395 83.985  1.00 61.65 ?  25  GLN A CG    1 
ATOM   168   C  CD    . GLN A 1 25  ? 114.796 113.009 84.145  1.00 62.47 ?  25  GLN A CD    1 
ATOM   169   O  OE1   . GLN A 1 25  ? 113.977 113.251 83.260  1.00 62.18 ?  25  GLN A OE1   1 
ATOM   170   N  NE2   . GLN A 1 25  ? 114.466 112.402 85.280  1.00 60.78 ?  25  GLN A NE2   1 
ATOM   171   N  N     . PHE A 1 26  ? 119.254 117.301 84.220  1.00 57.38 ?  26  PHE A N     1 
ATOM   172   C  CA    . PHE A 1 26  ? 119.644 118.629 84.677  1.00 55.95 ?  26  PHE A CA    1 
ATOM   173   C  C     . PHE A 1 26  ? 118.628 119.689 84.274  1.00 57.41 ?  26  PHE A C     1 
ATOM   174   O  O     . PHE A 1 26  ? 118.485 120.702 84.968  1.00 56.88 ?  26  PHE A O     1 
ATOM   175   C  CB    . PHE A 1 26  ? 121.028 118.985 84.133  1.00 53.29 ?  26  PHE A CB    1 
ATOM   176   C  CG    . PHE A 1 26  ? 122.140 118.186 84.745  1.00 54.17 ?  26  PHE A CG    1 
ATOM   177   C  CD1   . PHE A 1 26  ? 122.321 118.162 86.117  1.00 54.44 ?  26  PHE A CD1   1 
ATOM   178   C  CD2   . PHE A 1 26  ? 123.004 117.455 83.949  1.00 55.39 ?  26  PHE A CD2   1 
ATOM   179   C  CE1   . PHE A 1 26  ? 123.343 117.426 86.682  1.00 53.11 ?  26  PHE A CE1   1 
ATOM   180   C  CE2   . PHE A 1 26  ? 124.027 116.718 84.510  1.00 54.08 ?  26  PHE A CE2   1 
ATOM   181   C  CZ    . PHE A 1 26  ? 124.196 116.704 85.878  1.00 51.66 ?  26  PHE A CZ    1 
ATOM   182   N  N     . ASP A 1 27  ? 117.916 119.480 83.165  1.00 62.63 ?  27  ASP A N     1 
ATOM   183   C  CA    . ASP A 1 27  ? 116.925 120.445 82.707  1.00 61.91 ?  27  ASP A CA    1 
ATOM   184   C  C     . ASP A 1 27  ? 115.719 120.543 83.631  1.00 62.06 ?  27  ASP A C     1 
ATOM   185   O  O     . ASP A 1 27  ? 114.918 121.471 83.476  1.00 62.82 ?  27  ASP A O     1 
ATOM   186   C  CB    . ASP A 1 27  ? 116.459 120.091 81.294  1.00 61.74 ?  27  ASP A CB    1 
ATOM   187   C  CG    . ASP A 1 27  ? 116.439 121.291 80.369  1.00 65.25 ?  27  ASP A CG    1 
ATOM   188   O  OD1   . ASP A 1 27  ? 116.429 121.095 79.135  1.00 66.74 ?  27  ASP A OD1   1 
ATOM   189   O  OD2   . ASP A 1 27  ? 116.434 122.433 80.875  1.00 65.33 -1 27  ASP A OD2   1 
ATOM   190   N  N     . LYS A 1 28  ? 115.566 119.613 84.576  1.00 58.49 ?  28  LYS A N     1 
ATOM   191   C  CA    . LYS A 1 28  ? 114.451 119.689 85.512  1.00 59.07 ?  28  LYS A CA    1 
ATOM   192   C  C     . LYS A 1 28  ? 114.561 120.904 86.423  1.00 59.76 ?  28  LYS A C     1 
ATOM   193   O  O     . LYS A 1 28  ? 113.539 121.413 86.898  1.00 62.05 ?  28  LYS A O     1 
ATOM   194   C  CB    . LYS A 1 28  ? 114.376 118.411 86.347  1.00 58.92 ?  28  LYS A CB    1 
ATOM   195   C  CG    . LYS A 1 28  ? 114.022 117.175 85.546  1.00 60.16 ?  28  LYS A CG    1 
ATOM   196   C  CD    . LYS A 1 28  ? 112.562 117.184 85.136  1.00 61.07 ?  28  LYS A CD    1 
ATOM   197   C  CE    . LYS A 1 28  ? 112.273 116.101 84.113  1.00 60.92 ?  28  LYS A CE    1 
ATOM   198   N  NZ    . LYS A 1 28  ? 110.821 116.007 83.804  1.00 61.66 1  28  LYS A NZ    1 
ATOM   199   N  N     . ASP A 1 29  ? 115.782 121.382 86.679  1.00 56.42 ?  29  ASP A N     1 
ATOM   200   C  CA    . ASP A 1 29  ? 115.954 122.530 87.561  1.00 54.47 ?  29  ASP A CA    1 
ATOM   201   C  C     . ASP A 1 29  ? 115.410 123.807 86.935  1.00 53.46 ?  29  ASP A C     1 
ATOM   202   O  O     . ASP A 1 29  ? 114.960 124.704 87.658  1.00 55.08 ?  29  ASP A O     1 
ATOM   203   C  CB    . ASP A 1 29  ? 117.428 122.698 87.923  1.00 52.84 ?  29  ASP A CB    1 
ATOM   204   C  CG    . ASP A 1 29  ? 117.637 122.933 89.403  1.00 56.37 ?  29  ASP A CG    1 
ATOM   205   O  OD1   . ASP A 1 29  ? 116.761 122.534 90.197  1.00 56.68 ?  29  ASP A OD1   1 
ATOM   206   O  OD2   . ASP A 1 29  ? 118.680 123.509 89.775  1.00 55.59 -1 29  ASP A OD2   1 
ATOM   207   N  N     . LYS A 1 30  ? 115.452 123.918 85.607  1.00 54.13 ?  30  LYS A N     1 
ATOM   208   C  CA    . LYS A 1 30  ? 114.791 125.034 84.939  1.00 56.39 ?  30  LYS A CA    1 
ATOM   209   C  C     . LYS A 1 30  ? 113.281 124.949 85.117  1.00 55.12 ?  30  LYS A C     1 
ATOM   210   O  O     . LYS A 1 30  ? 112.623 125.945 85.449  1.00 59.35 ?  30  LYS A O     1 
ATOM   211   C  CB    . LYS A 1 30  ? 115.164 125.052 83.458  1.00 55.60 ?  30  LYS A CB    1 
ATOM   212   C  CG    . LYS A 1 30  ? 114.571 126.213 82.679  1.00 57.24 ?  30  LYS A CG    1 
ATOM   213   C  CD    . LYS A 1 30  ? 115.567 126.767 81.674  1.00 57.04 ?  30  LYS A CD    1 
ATOM   214   C  CE    . LYS A 1 30  ? 115.000 127.968 80.938  1.00 57.35 ?  30  LYS A CE    1 
ATOM   215   N  NZ    . LYS A 1 30  ? 114.480 127.597 79.593  1.00 56.39 1  30  LYS A NZ    1 
ATOM   216   N  N     . GLU A 1 31  ? 112.715 123.758 84.920  1.00 52.94 ?  31  GLU A N     1 
ATOM   217   C  CA    . GLU A 1 31  ? 111.302 123.557 85.213  1.00 53.56 ?  31  GLU A CA    1 
ATOM   218   C  C     . GLU A 1 31  ? 111.026 123.739 86.698  1.00 54.66 ?  31  GLU A C     1 
ATOM   219   O  O     . GLU A 1 31  ? 109.974 124.260 87.082  1.00 56.52 ?  31  GLU A O     1 
ATOM   220   C  CB    . GLU A 1 31  ? 110.860 122.171 84.748  1.00 55.25 ?  31  GLU A CB    1 
ATOM   221   C  CG    . GLU A 1 31  ? 110.387 122.119 83.307  1.00 56.83 ?  31  GLU A CG    1 
ATOM   222   C  CD    . GLU A 1 31  ? 110.676 120.786 82.647  1.00 60.89 ?  31  GLU A CD    1 
ATOM   223   O  OE1   . GLU A 1 31  ? 111.392 119.964 83.256  1.00 60.98 ?  31  GLU A OE1   1 
ATOM   224   O  OE2   . GLU A 1 31  ? 110.189 120.560 81.520  1.00 58.42 -1 31  GLU A OE2   1 
ATOM   225   N  N     . ALA A 1 32  ? 111.967 123.323 87.548  1.00 50.02 ?  32  ALA A N     1 
ATOM   226   C  CA    . ALA A 1 32  ? 111.786 123.486 88.986  1.00 49.58 ?  32  ALA A CA    1 
ATOM   227   C  C     . ALA A 1 32  ? 111.682 124.955 89.368  1.00 52.01 ?  32  ALA A C     1 
ATOM   228   O  O     . ALA A 1 32  ? 110.795 125.338 90.136  1.00 51.91 ?  32  ALA A O     1 
ATOM   229   C  CB    . ALA A 1 32  ? 112.932 122.816 89.742  1.00 48.80 ?  32  ALA A CB    1 
ATOM   230   N  N     . VAL A 1 33  ? 112.563 125.800 88.828  1.00 53.52 ?  33  VAL A N     1 
ATOM   231   C  CA    . VAL A 1 33  ? 112.523 127.218 89.174  1.00 52.03 ?  33  VAL A CA    1 
ATOM   232   C  C     . VAL A 1 33  ? 111.317 127.897 88.531  1.00 52.95 ?  33  VAL A C     1 
ATOM   233   O  O     . VAL A 1 33  ? 110.712 128.800 89.122  1.00 54.60 ?  33  VAL A O     1 
ATOM   234   C  CB    . VAL A 1 33  ? 113.851 127.909 88.804  1.00 49.44 ?  33  VAL A CB    1 
ATOM   235   C  CG1   . VAL A 1 33  ? 114.003 128.066 87.302  1.00 51.09 ?  33  VAL A CG1   1 
ATOM   236   C  CG2   . VAL A 1 33  ? 113.956 129.257 89.495  1.00 49.46 ?  33  VAL A CG2   1 
ATOM   237   N  N     . HIS A 1 34  ? 110.940 127.472 87.322  1.00 50.73 ?  34  HIS A N     1 
ATOM   238   C  CA    . HIS A 1 34  ? 109.755 128.035 86.681  1.00 50.74 ?  34  HIS A CA    1 
ATOM   239   C  C     . HIS A 1 34  ? 108.508 127.746 87.511  1.00 52.66 ?  34  HIS A C     1 
ATOM   240   O  O     . HIS A 1 34  ? 107.681 128.638 87.752  1.00 53.04 ?  34  HIS A O     1 
ATOM   241   C  CB    . HIS A 1 34  ? 109.629 127.472 85.263  1.00 53.19 ?  34  HIS A CB    1 
ATOM   242   C  CG    . HIS A 1 34  ? 108.539 128.093 84.440  1.00 55.22 ?  34  HIS A CG    1 
ATOM   243   N  ND1   . HIS A 1 34  ? 107.304 128.426 84.952  1.00 54.82 ?  34  HIS A ND1   1 
ATOM   244   C  CD2   . HIS A 1 34  ? 108.509 128.442 83.133  1.00 54.74 ?  34  HIS A CD2   1 
ATOM   245   C  CE1   . HIS A 1 34  ? 106.558 128.949 83.995  1.00 55.21 ?  34  HIS A CE1   1 
ATOM   246   N  NE2   . HIS A 1 34  ? 107.268 128.973 82.882  1.00 55.54 ?  34  HIS A NE2   1 
ATOM   247   N  N     . SER A 1 35  ? 108.365 126.499 87.969  1.00 54.59 ?  35  SER A N     1 
ATOM   248   C  CA    . SER A 1 35  ? 107.246 126.143 88.831  1.00 51.97 ?  35  SER A CA    1 
ATOM   249   C  C     . SER A 1 35  ? 107.327 126.872 90.165  1.00 52.12 ?  35  SER A C     1 
ATOM   250   O  O     . SER A 1 35  ? 106.307 127.341 90.682  1.00 54.74 ?  35  SER A O     1 
ATOM   251   C  CB    . SER A 1 35  ? 107.211 124.631 89.050  1.00 51.86 ?  35  SER A CB    1 
ATOM   252   O  OG    . SER A 1 35  ? 106.423 124.303 90.180  1.00 54.09 ?  35  SER A OG    1 
ATOM   253   N  N     . TYR A 1 36  ? 108.530 126.978 90.734  1.00 51.70 ?  36  TYR A N     1 
ATOM   254   C  CA    . TYR A 1 36  ? 108.710 127.706 91.983  1.00 51.33 ?  36  TYR A CA    1 
ATOM   255   C  C     . TYR A 1 36  ? 108.166 129.116 91.863  1.00 48.41 ?  36  TYR A C     1 
ATOM   256   O  O     . TYR A 1 36  ? 107.361 129.556 92.689  1.00 48.38 ?  36  TYR A O     1 
ATOM   257   C  CB    . TYR A 1 36  ? 110.191 127.730 92.362  1.00 47.92 ?  36  TYR A CB    1 
ATOM   258   C  CG    . TYR A 1 36  ? 110.507 128.546 93.595  1.00 49.41 ?  36  TYR A CG    1 
ATOM   259   C  CD1   . TYR A 1 36  ? 109.951 128.228 94.825  1.00 47.81 ?  36  TYR A CD1   1 
ATOM   260   C  CD2   . TYR A 1 36  ? 111.371 129.630 93.528  1.00 48.66 ?  36  TYR A CD2   1 
ATOM   261   C  CE1   . TYR A 1 36  ? 110.244 128.967 95.952  1.00 46.14 ?  36  TYR A CE1   1 
ATOM   262   C  CE2   . TYR A 1 36  ? 111.668 130.377 94.648  1.00 46.68 ?  36  TYR A CE2   1 
ATOM   263   C  CZ    . TYR A 1 36  ? 111.102 130.040 95.857  1.00 48.10 ?  36  TYR A CZ    1 
ATOM   264   O  OH    . TYR A 1 36  ? 111.397 130.783 96.977  1.00 50.06 ?  36  TYR A OH    1 
ATOM   265   N  N     . PHE A 1 37  ? 108.549 129.819 90.799  1.00 52.38 ?  37  PHE A N     1 
ATOM   266   C  CA    . PHE A 1 37  ? 108.052 131.173 90.607  1.00 52.15 ?  37  PHE A CA    1 
ATOM   267   C  C     . PHE A 1 37  ? 106.542 131.177 90.428  1.00 53.54 ?  37  PHE A C     1 
ATOM   268   O  O     . PHE A 1 37  ? 105.817 131.688 91.288  1.00 56.56 ?  37  PHE A O     1 
ATOM   269   C  CB    . PHE A 1 37  ? 108.757 131.837 89.428  1.00 54.60 ?  37  PHE A CB    1 
ATOM   270   C  CG    . PHE A 1 37  ? 110.032 132.513 89.814  1.00 53.80 ?  37  PHE A CG    1 
ATOM   271   C  CD1   . PHE A 1 37  ? 110.012 133.782 90.363  1.00 51.23 ?  37  PHE A CD1   1 
ATOM   272   C  CD2   . PHE A 1 37  ? 111.245 131.871 89.664  1.00 53.12 ?  37  PHE A CD2   1 
ATOM   273   C  CE1   . PHE A 1 37  ? 111.180 134.405 90.735  1.00 52.41 ?  37  PHE A CE1   1 
ATOM   274   C  CE2   . PHE A 1 37  ? 112.414 132.490 90.033  1.00 52.36 ?  37  PHE A CE2   1 
ATOM   275   C  CZ    . PHE A 1 37  ? 112.382 133.756 90.572  1.00 52.98 ?  37  PHE A CZ    1 
ATOM   276   N  N     . VAL A 1 38  ? 106.047 130.527 89.370  1.00 56.41 ?  38  VAL A N     1 
ATOM   277   C  CA    . VAL A 1 38  ? 104.634 130.642 89.019  1.00 55.88 ?  38  VAL A CA    1 
ATOM   278   C  C     . VAL A 1 38  ? 103.695 129.974 90.012  1.00 55.62 ?  38  VAL A C     1 
ATOM   279   O  O     . VAL A 1 38  ? 102.474 130.069 89.843  1.00 57.68 ?  38  VAL A O     1 
ATOM   280   C  CB    . VAL A 1 38  ? 104.359 130.067 87.615  1.00 54.03 ?  38  VAL A CB    1 
ATOM   281   C  CG1   . VAL A 1 38  ? 105.294 130.696 86.599  1.00 55.29 ?  38  VAL A CG1   1 
ATOM   282   C  CG2   . VAL A 1 38  ? 104.486 128.553 87.622  1.00 52.16 ?  38  VAL A CG2   1 
ATOM   283   N  N     . ASP A 1 39  ? 104.212 129.303 91.044  1.00 54.34 ?  39  ASP A N     1 
ATOM   284   C  CA    . ASP A 1 39  ? 103.348 128.704 92.048  1.00 53.08 ?  39  ASP A CA    1 
ATOM   285   C  C     . ASP A 1 39  ? 103.547 129.244 93.456  1.00 57.49 ?  39  ASP A C     1 
ATOM   286   O  O     . ASP A 1 39  ? 102.641 129.091 94.281  1.00 61.79 ?  39  ASP A O     1 
ATOM   287   C  CB    . ASP A 1 39  ? 103.538 127.179 92.077  1.00 55.36 ?  39  ASP A CB    1 
ATOM   288   C  CG    . ASP A 1 39  ? 103.263 126.532 90.733  1.00 58.49 ?  39  ASP A CG    1 
ATOM   289   O  OD1   . ASP A 1 39  ? 102.424 127.063 89.977  1.00 59.03 ?  39  ASP A OD1   1 
ATOM   290   O  OD2   . ASP A 1 39  ? 103.882 125.490 90.434  1.00 58.25 -1 39  ASP A OD2   1 
ATOM   291   N  N     . TYR A 1 40  ? 104.689 129.857 93.763  1.00 56.20 ?  40  TYR A N     1 
ATOM   292   C  CA    . TYR A 1 40  ? 104.918 130.442 95.076  1.00 55.34 ?  40  TYR A CA    1 
ATOM   293   C  C     . TYR A 1 40  ? 105.219 131.930 95.011  1.00 59.10 ?  40  TYR A C     1 
ATOM   294   O  O     . TYR A 1 40  ? 104.624 132.712 95.759  1.00 61.95 ?  40  TYR A O     1 
ATOM   295   C  CB    . TYR A 1 40  ? 106.071 129.708 95.778  1.00 54.12 ?  40  TYR A CB    1 
ATOM   296   C  CG    . TYR A 1 40  ? 106.214 130.047 97.242  1.00 54.91 ?  40  TYR A CG    1 
ATOM   297   C  CD1   . TYR A 1 40  ? 105.190 129.785 98.139  1.00 55.80 ?  40  TYR A CD1   1 
ATOM   298   C  CD2   . TYR A 1 40  ? 107.375 130.633 97.725  1.00 55.91 ?  40  TYR A CD2   1 
ATOM   299   C  CE1   . TYR A 1 40  ? 105.318 130.095 99.479  1.00 57.94 ?  40  TYR A CE1   1 
ATOM   300   C  CE2   . TYR A 1 40  ? 107.513 130.946 99.061  1.00 58.46 ?  40  TYR A CE2   1 
ATOM   301   C  CZ    . TYR A 1 40  ? 106.482 130.677 99.933  1.00 60.69 ?  40  TYR A CZ    1 
ATOM   302   O  OH    . TYR A 1 40  ? 106.615 130.988 101.266 1.00 61.32 ?  40  TYR A OH    1 
ATOM   303   N  N     . ILE A 1 41  ? 106.118 132.347 94.119  1.00 55.06 ?  41  ILE A N     1 
ATOM   304   C  CA    . ILE A 1 41  ? 106.706 133.677 94.230  1.00 54.10 ?  41  ILE A CA    1 
ATOM   305   C  C     . ILE A 1 41  ? 105.748 134.736 93.706  1.00 53.77 ?  41  ILE A C     1 
ATOM   306   O  O     . ILE A 1 41  ? 105.465 135.726 94.388  1.00 56.11 ?  41  ILE A O     1 
ATOM   307   C  CB    . ILE A 1 41  ? 108.058 133.723 93.495  1.00 53.23 ?  41  ILE A CB    1 
ATOM   308   C  CG1   . ILE A 1 41  ? 109.068 132.799 94.178  1.00 51.97 ?  41  ILE A CG1   1 
ATOM   309   C  CG2   . ILE A 1 41  ? 108.592 135.143 93.452  1.00 52.91 ?  41  ILE A CG2   1 
ATOM   310   C  CD1   . ILE A 1 41  ? 109.359 133.162 95.609  1.00 49.09 ?  41  ILE A CD1   1 
ATOM   311   N  N     . ASN A 1 42  ? 105.232 134.543 92.490  1.00 55.14 ?  42  ASN A N     1 
ATOM   312   C  CA    . ASN A 1 42  ? 104.276 135.496 91.939  1.00 57.04 ?  42  ASN A CA    1 
ATOM   313   C  C     . ASN A 1 42  ? 103.001 135.548 92.770  1.00 60.67 ?  42  ASN A C     1 
ATOM   314   O  O     . ASN A 1 42  ? 102.332 136.586 92.816  1.00 60.98 ?  42  ASN A O     1 
ATOM   315   C  CB    . ASN A 1 42  ? 103.959 135.137 90.488  1.00 56.57 ?  42  ASN A CB    1 
ATOM   316   C  CG    . ASN A 1 42  ? 105.195 135.117 89.610  1.00 57.49 ?  42  ASN A CG    1 
ATOM   317   O  OD1   . ASN A 1 42  ? 106.245 135.632 89.988  1.00 61.31 ?  42  ASN A OD1   1 
ATOM   318   N  ND2   . ASN A 1 42  ? 105.074 134.521 88.431  1.00 57.43 ?  42  ASN A ND2   1 
ATOM   319   N  N     . GLN A 1 43  ? 102.649 134.443 93.428  1.00 62.95 ?  43  GLN A N     1 
ATOM   320   C  CA    . GLN A 1 43  ? 101.483 134.442 94.304  1.00 61.34 ?  43  GLN A CA    1 
ATOM   321   C  C     . GLN A 1 43  ? 101.752 135.219 95.586  1.00 59.55 ?  43  GLN A C     1 
ATOM   322   O  O     . GLN A 1 43  ? 100.906 136.002 96.034  1.00 62.85 ?  43  GLN A O     1 
ATOM   323   C  CB    . GLN A 1 43  ? 101.067 133.006 94.623  1.00 60.93 ?  43  GLN A CB    1 
ATOM   324   C  CG    . GLN A 1 43  ? 101.246 132.026 93.470  1.00 61.60 ?  43  GLN A CG    1 
ATOM   325   C  CD    . GLN A 1 43  ? 100.199 132.188 92.383  1.00 64.24 ?  43  GLN A CD    1 
ATOM   326   O  OE1   . GLN A 1 43  ? 100.155 133.206 91.691  1.00 62.89 ?  43  GLN A OE1   1 
ATOM   327   N  NE2   . GLN A 1 43  ? 99.352  131.178 92.225  1.00 62.68 ?  43  GLN A NE2   1 
ATOM   328   N  N     . ASN A 1 44  ? 102.923 135.022 96.189  1.00 54.88 ?  44  ASN A N     1 
ATOM   329   C  CA    . ASN A 1 44  ? 103.267 135.652 97.456  1.00 56.20 ?  44  ASN A CA    1 
ATOM   330   C  C     . ASN A 1 44  ? 103.901 137.027 97.292  1.00 56.44 ?  44  ASN A C     1 
ATOM   331   O  O     . ASN A 1 44  ? 104.269 137.645 98.296  1.00 57.09 ?  44  ASN A O     1 
ATOM   332   C  CB    . ASN A 1 44  ? 104.210 134.746 98.255  1.00 56.48 ?  44  ASN A CB    1 
ATOM   333   C  CG    . ASN A 1 44  ? 103.492 133.566 98.880  1.00 59.38 ?  44  ASN A CG    1 
ATOM   334   O  OD1   . ASN A 1 44  ? 103.128 133.599 100.055 1.00 60.88 ?  44  ASN A OD1   1 
ATOM   335   N  ND2   . ASN A 1 44  ? 103.284 132.516 98.095  1.00 58.08 ?  44  ASN A ND2   1 
ATOM   336   N  N     . THR A 1 45  ? 104.043 137.518 96.066  1.00 58.13 ?  45  THR A N     1 
ATOM   337   C  CA    . THR A 1 45  ? 104.632 138.826 95.822  1.00 59.07 ?  45  THR A CA    1 
ATOM   338   C  C     . THR A 1 45  ? 103.567 139.908 95.929  1.00 59.02 ?  45  THR A C     1 
ATOM   339   O  O     . THR A 1 45  ? 102.521 139.826 95.277  1.00 60.05 ?  45  THR A O     1 
ATOM   340   C  CB    . THR A 1 45  ? 105.288 138.880 94.443  1.00 58.07 ?  45  THR A CB    1 
ATOM   341   O  OG1   . THR A 1 45  ? 106.346 137.916 94.379  1.00 59.58 ?  45  THR A OG1   1 
ATOM   342   C  CG2   . THR A 1 45  ? 105.852 140.265 94.174  1.00 55.65 ?  45  THR A CG2   1 
ATOM   343   N  N     . VAL A 1 46  ? 103.836 140.919 96.754  1.00 60.32 ?  46  VAL A N     1 
ATOM   344   C  CA    . VAL A 1 46  ? 102.969 142.090 96.814  1.00 60.71 ?  46  VAL A CA    1 
ATOM   345   C  C     . VAL A 1 46  ? 103.212 142.933 95.570  1.00 60.62 ?  46  VAL A C     1 
ATOM   346   O  O     . VAL A 1 46  ? 104.347 143.338 95.290  1.00 62.72 ?  46  VAL A O     1 
ATOM   347   C  CB    . VAL A 1 46  ? 103.223 142.899 98.091  1.00 60.03 ?  46  VAL A CB    1 
ATOM   348   C  CG1   . VAL A 1 46  ? 102.180 143.991 98.241  1.00 60.24 ?  46  VAL A CG1   1 
ATOM   349   C  CG2   . VAL A 1 46  ? 103.225 141.991 99.303  1.00 59.25 ?  46  VAL A CG2   1 
ATOM   350   N  N     . PHE A 1 47  ? 102.150 143.203 94.819  1.00 64.09 ?  47  PHE A N     1 
ATOM   351   C  CA    . PHE A 1 47  ? 102.235 143.988 93.597  1.00 66.23 ?  47  PHE A CA    1 
ATOM   352   C  C     . PHE A 1 47  ? 101.438 145.270 93.768  1.00 67.45 ?  47  PHE A C     1 
ATOM   353   O  O     . PHE A 1 47  ? 100.290 145.239 94.221  1.00 67.74 ?  47  PHE A O     1 
ATOM   354   C  CB    . PHE A 1 47  ? 101.724 143.197 92.390  1.00 67.11 ?  47  PHE A CB    1 
ATOM   355   C  CG    . PHE A 1 47  ? 101.858 143.933 91.086  1.00 68.09 ?  47  PHE A CG    1 
ATOM   356   C  CD1   . PHE A 1 47  ? 103.064 143.946 90.404  1.00 67.12 ?  47  PHE A CD1   1 
ATOM   357   C  CD2   . PHE A 1 47  ? 100.778 144.605 90.540  1.00 66.60 ?  47  PHE A CD2   1 
ATOM   358   C  CE1   . PHE A 1 47  ? 103.191 144.620 89.206  1.00 67.08 ?  47  PHE A CE1   1 
ATOM   359   C  CE2   . PHE A 1 47  ? 100.899 145.281 89.340  1.00 67.40 ?  47  PHE A CE2   1 
ATOM   360   C  CZ    . PHE A 1 47  ? 102.107 145.289 88.672  1.00 68.47 ?  47  PHE A CZ    1 
ATOM   361   N  N     . PHE A 1 48  ? 102.053 146.390 93.409  1.00 66.92 ?  48  PHE A N     1 
ATOM   362   C  CA    . PHE A 1 48  ? 101.445 147.705 93.518  1.00 64.94 ?  48  PHE A CA    1 
ATOM   363   C  C     . PHE A 1 48  ? 101.082 148.215 92.131  1.00 65.55 ?  48  PHE A C     1 
ATOM   364   O  O     . PHE A 1 48  ? 101.614 147.754 91.118  1.00 67.21 ?  48  PHE A O     1 
ATOM   365   C  CB    . PHE A 1 48  ? 102.385 148.691 94.220  1.00 63.60 ?  48  PHE A CB    1 
ATOM   366   C  CG    . PHE A 1 48  ? 102.833 148.240 95.585  1.00 63.28 ?  48  PHE A CG    1 
ATOM   367   C  CD1   . PHE A 1 48  ? 102.327 148.836 96.725  1.00 64.12 ?  48  PHE A CD1   1 
ATOM   368   C  CD2   . PHE A 1 48  ? 103.779 147.237 95.726  1.00 63.11 ?  48  PHE A CD2   1 
ATOM   369   C  CE1   . PHE A 1 48  ? 102.739 148.427 97.976  1.00 65.24 ?  48  PHE A CE1   1 
ATOM   370   C  CE2   . PHE A 1 48  ? 104.194 146.826 96.975  1.00 63.83 ?  48  PHE A CE2   1 
ATOM   371   C  CZ    . PHE A 1 48  ? 103.674 147.421 98.099  1.00 64.21 ?  48  PHE A CZ    1 
ATOM   372   N  N     . HIS A 1 49  ? 100.156 149.176 92.096  1.00 68.07 ?  49  HIS A N     1 
ATOM   373   C  CA    . HIS A 1 49  ? 99.695  149.707 90.816  1.00 70.19 ?  49  HIS A CA    1 
ATOM   374   C  C     . HIS A 1 49  ? 100.835 150.356 90.043  1.00 69.96 ?  49  HIS A C     1 
ATOM   375   O  O     . HIS A 1 49  ? 100.962 150.159 88.829  1.00 70.21 ?  49  HIS A O     1 
ATOM   376   C  CB    . HIS A 1 49  ? 98.557  150.702 91.039  1.00 69.80 ?  49  HIS A CB    1 
ATOM   377   C  CG    . HIS A 1 49  ? 97.396  150.132 91.793  1.00 71.45 ?  49  HIS A CG    1 
ATOM   378   N  ND1   . HIS A 1 49  ? 97.432  149.895 93.150  1.00 71.84 ?  49  HIS A ND1   1 
ATOM   379   C  CD2   . HIS A 1 49  ? 96.165  149.752 91.377  1.00 70.55 ?  49  HIS A CD2   1 
ATOM   380   C  CE1   . HIS A 1 49  ? 96.273  149.393 93.538  1.00 69.89 ?  49  HIS A CE1   1 
ATOM   381   N  NE2   . HIS A 1 49  ? 95.487  149.295 92.482  1.00 71.70 ?  49  HIS A NE2   1 
ATOM   382   N  N     . ASN A 1 50  ? 101.674 151.130 90.727  1.00 67.49 ?  50  ASN A N     1 
ATOM   383   C  CA    . ASN A 1 50  ? 102.842 151.738 90.111  1.00 66.95 ?  50  ASN A CA    1 
ATOM   384   C  C     . ASN A 1 50  ? 103.994 151.715 91.104  1.00 65.92 ?  50  ASN A C     1 
ATOM   385   O  O     . ASN A 1 50  ? 103.808 151.473 92.298  1.00 67.91 ?  50  ASN A O     1 
ATOM   386   C  CB    . ASN A 1 50  ? 102.559 153.173 89.638  1.00 66.30 ?  50  ASN A CB    1 
ATOM   387   C  CG    . ASN A 1 50  ? 101.984 154.050 90.732  1.00 66.97 ?  50  ASN A CG    1 
ATOM   388   O  OD1   . ASN A 1 50  ? 101.866 153.634 91.884  1.00 66.48 ?  50  ASN A OD1   1 
ATOM   389   N  ND2   . ASN A 1 50  ? 101.623 155.276 90.375  1.00 66.32 ?  50  ASN A ND2   1 
ATOM   390   N  N     . LEU A 1 51  ? 105.202 151.959 90.587  1.00 60.19 ?  51  LEU A N     1 
ATOM   391   C  CA    . LEU A 1 51  ? 106.387 151.948 91.437  1.00 60.44 ?  51  LEU A CA    1 
ATOM   392   C  C     . LEU A 1 51  ? 106.326 153.037 92.502  1.00 62.18 ?  51  LEU A C     1 
ATOM   393   O  O     . LEU A 1 51  ? 106.908 152.879 93.581  1.00 64.40 ?  51  LEU A O     1 
ATOM   394   C  CB    . LEU A 1 51  ? 107.644 152.107 90.582  1.00 61.12 ?  51  LEU A CB    1 
ATOM   395   C  CG    . LEU A 1 51  ? 108.985 152.153 91.318  1.00 58.98 ?  51  LEU A CG    1 
ATOM   396   C  CD1   . LEU A 1 51  ? 109.254 150.837 92.024  1.00 58.21 ?  51  LEU A CD1   1 
ATOM   397   C  CD2   . LEU A 1 51  ? 110.111 152.501 90.362  1.00 58.63 ?  51  LEU A CD2   1 
ATOM   398   N  N     . LYS A 1 52  ? 105.637 154.146 92.219  1.00 62.24 ?  52  LYS A N     1 
ATOM   399   C  CA    . LYS A 1 52  ? 105.521 155.216 93.205  1.00 60.33 ?  52  LYS A CA    1 
ATOM   400   C  C     . LYS A 1 52  ? 104.792 154.740 94.453  1.00 61.87 ?  52  LYS A C     1 
ATOM   401   O  O     . LYS A 1 52  ? 105.225 155.017 95.578  1.00 61.87 ?  52  LYS A O     1 
ATOM   402   C  CB    . LYS A 1 52  ? 104.806 156.419 92.592  1.00 59.33 ?  52  LYS A CB    1 
ATOM   403   C  CG    . LYS A 1 52  ? 105.094 157.736 93.292  1.00 62.17 ?  52  LYS A CG    1 
ATOM   404   C  CD    . LYS A 1 52  ? 104.986 158.905 92.328  1.00 63.90 ?  52  LYS A CD    1 
ATOM   405   C  CE    . LYS A 1 52  ? 105.877 160.061 92.753  1.00 63.03 ?  52  LYS A CE    1 
ATOM   406   N  NZ    . LYS A 1 52  ? 106.118 160.068 94.222  1.00 61.51 1  52  LYS A NZ    1 
ATOM   407   N  N     . GLU A 1 53  ? 103.686 154.015 94.272  1.00 65.07 ?  53  GLU A N     1 
ATOM   408   C  CA    . GLU A 1 53  ? 102.961 153.476 95.416  1.00 65.62 ?  53  GLU A CA    1 
ATOM   409   C  C     . GLU A 1 53  ? 103.820 152.481 96.184  1.00 64.75 ?  53  GLU A C     1 
ATOM   410   O  O     . GLU A 1 53  ? 103.808 152.466 97.419  1.00 65.93 ?  53  GLU A O     1 
ATOM   411   C  CB    . GLU A 1 53  ? 101.659 152.823 94.951  1.00 65.41 ?  53  GLU A CB    1 
ATOM   412   C  CG    . GLU A 1 53  ? 100.959 151.987 96.009  1.00 67.11 ?  53  GLU A CG    1 
ATOM   413   C  CD    . GLU A 1 53  ? 99.707  151.313 95.481  1.00 69.03 ?  53  GLU A CD    1 
ATOM   414   O  OE1   . GLU A 1 53  ? 99.245  151.689 94.383  1.00 69.01 ?  53  GLU A OE1   1 
ATOM   415   O  OE2   . GLU A 1 53  ? 99.185  150.407 96.163  1.00 68.53 -1 53  GLU A OE2   1 
ATOM   416   N  N     . LYS A 1 54  ? 104.582 151.653 95.468  1.00 60.53 ?  54  LYS A N     1 
ATOM   417   C  CA    . LYS A 1 54  ? 105.457 150.686 96.124  1.00 62.09 ?  54  LYS A CA    1 
ATOM   418   C  C     . LYS A 1 54  ? 106.505 151.382 96.981  1.00 58.42 ?  54  LYS A C     1 
ATOM   419   O  O     . LYS A 1 54  ? 106.718 151.018 98.145  1.00 60.89 ?  54  LYS A O     1 
ATOM   420   C  CB    . LYS A 1 54  ? 106.126 149.801 95.073  1.00 61.73 ?  54  LYS A CB    1 
ATOM   421   C  CG    . LYS A 1 54  ? 107.208 148.895 95.625  1.00 59.32 ?  54  LYS A CG    1 
ATOM   422   C  CD    . LYS A 1 54  ? 107.523 147.769 94.662  1.00 59.69 ?  54  LYS A CD    1 
ATOM   423   C  CE    . LYS A 1 54  ? 108.435 146.740 95.299  1.00 60.84 ?  54  LYS A CE    1 
ATOM   424   N  NZ    . LYS A 1 54  ? 108.363 145.429 94.600  1.00 61.90 1  54  LYS A NZ    1 
ATOM   425   N  N     . LEU A 1 55  ? 107.172 152.392 96.420  1.00 56.48 ?  55  LEU A N     1 
ATOM   426   C  CA    . LEU A 1 55  ? 108.215 153.090 97.163  1.00 58.32 ?  55  LEU A CA    1 
ATOM   427   C  C     . LEU A 1 55  ? 107.634 153.858 98.343  1.00 61.53 ?  55  LEU A C     1 
ATOM   428   O  O     . LEU A 1 55  ? 108.232 153.882 99.425  1.00 63.78 ?  55  LEU A O     1 
ATOM   429   C  CB    . LEU A 1 55  ? 108.987 154.024 96.234  1.00 59.39 ?  55  LEU A CB    1 
ATOM   430   C  CG    . LEU A 1 55  ? 109.851 153.317 95.190  1.00 59.74 ?  55  LEU A CG    1 
ATOM   431   C  CD1   . LEU A 1 55  ? 110.501 154.326 94.267  1.00 59.60 ?  55  LEU A CD1   1 
ATOM   432   C  CD2   . LEU A 1 55  ? 110.899 152.444 95.861  1.00 59.41 ?  55  LEU A CD2   1 
ATOM   433   N  N     . ASP A 1 56  ? 106.472 154.490 98.158  1.00 65.92 ?  56  ASP A N     1 
ATOM   434   C  CA    . ASP A 1 56  ? 105.831 155.183 99.269  1.00 64.75 ?  56  ASP A CA    1 
ATOM   435   C  C     . ASP A 1 56  ? 105.452 154.209 100.377 1.00 64.19 ?  56  ASP A C     1 
ATOM   436   O  O     . ASP A 1 56  ? 105.654 154.496 101.562 1.00 65.16 ?  56  ASP A O     1 
ATOM   437   C  CB    . ASP A 1 56  ? 104.602 155.942 98.771  1.00 65.50 ?  56  ASP A CB    1 
ATOM   438   C  CG    . ASP A 1 56  ? 104.965 157.165 97.953  1.00 68.31 ?  56  ASP A CG    1 
ATOM   439   O  OD1   . ASP A 1 56  ? 106.096 157.671 98.107  1.00 67.57 ?  56  ASP A OD1   1 
ATOM   440   O  OD2   . ASP A 1 56  ? 104.120 157.622 97.154  1.00 67.50 -1 56  ASP A OD2   1 
ATOM   441   N  N     . TYR A 1 57  ? 104.915 153.045 100.007 1.00 59.50 ?  57  TYR A N     1 
ATOM   442   C  CA    . TYR A 1 57  ? 104.550 152.036 100.993 1.00 62.04 ?  57  TYR A CA    1 
ATOM   443   C  C     . TYR A 1 57  ? 105.773 151.545 101.754 1.00 61.86 ?  57  TYR A C     1 
ATOM   444   O  O     . TYR A 1 57  ? 105.717 151.340 102.973 1.00 63.68 ?  57  TYR A O     1 
ATOM   445   C  CB    . TYR A 1 57  ? 103.855 150.868 100.292 1.00 61.52 ?  57  TYR A CB    1 
ATOM   446   C  CG    . TYR A 1 57  ? 103.596 149.666 101.168 1.00 62.14 ?  57  TYR A CG    1 
ATOM   447   C  CD1   . TYR A 1 57  ? 102.535 149.649 102.060 1.00 62.07 ?  57  TYR A CD1   1 
ATOM   448   C  CD2   . TYR A 1 57  ? 104.428 148.556 101.120 1.00 63.16 ?  57  TYR A CD2   1 
ATOM   449   C  CE1   . TYR A 1 57  ? 102.293 148.549 102.857 1.00 62.91 ?  57  TYR A CE1   1 
ATOM   450   C  CE2   . TYR A 1 57  ? 104.199 147.458 101.920 1.00 63.73 ?  57  TYR A CE2   1 
ATOM   451   C  CZ    . TYR A 1 57  ? 103.132 147.460 102.789 1.00 63.36 ?  57  TYR A CZ    1 
ATOM   452   O  OH    . TYR A 1 57  ? 102.901 146.366 103.588 1.00 62.05 ?  57  TYR A OH    1 
ATOM   453   N  N     . LEU A 1 58  ? 106.889 151.342 101.050 1.00 56.04 ?  58  LEU A N     1 
ATOM   454   C  CA    . LEU A 1 58  ? 108.084 150.816 101.700 1.00 54.62 ?  58  LEU A CA    1 
ATOM   455   C  C     . LEU A 1 58  ? 108.738 151.858 102.599 1.00 55.12 ?  58  LEU A C     1 
ATOM   456   O  O     . LEU A 1 58  ? 109.248 151.524 103.674 1.00 58.06 ?  58  LEU A O     1 
ATOM   457   C  CB    . LEU A 1 58  ? 109.070 150.312 100.648 1.00 56.32 ?  58  LEU A CB    1 
ATOM   458   C  CG    . LEU A 1 58  ? 108.603 149.080 99.871  1.00 56.27 ?  58  LEU A CG    1 
ATOM   459   C  CD1   . LEU A 1 58  ? 109.371 148.940 98.572  1.00 55.04 ?  58  LEU A CD1   1 
ATOM   460   C  CD2   . LEU A 1 58  ? 108.741 147.828 100.713 1.00 56.23 ?  58  LEU A CD2   1 
ATOM   461   N  N     . VAL A 1 59  ? 108.743 153.124 102.178 1.00 60.11 ?  59  VAL A N     1 
ATOM   462   C  CA    . VAL A 1 59  ? 109.338 154.172 103.001 1.00 62.24 ?  59  VAL A CA    1 
ATOM   463   C  C     . VAL A 1 59  ? 108.481 154.439 104.232 1.00 64.10 ?  59  VAL A C     1 
ATOM   464   O  O     . VAL A 1 59  ? 108.993 154.562 105.351 1.00 63.20 ?  59  VAL A O     1 
ATOM   465   C  CB    . VAL A 1 59  ? 109.553 155.451 102.172 1.00 62.74 ?  59  VAL A CB    1 
ATOM   466   C  CG1   . VAL A 1 59  ? 109.990 156.597 103.067 1.00 60.59 ?  59  VAL A CG1   1 
ATOM   467   C  CG2   . VAL A 1 59  ? 110.586 155.207 101.083 1.00 62.18 ?  59  VAL A CG2   1 
ATOM   468   N  N     . GLU A 1 60  ? 107.160 154.531 104.046 1.00 64.88 ?  60  GLU A N     1 
ATOM   469   C  CA    . GLU A 1 60  ? 106.277 154.888 105.152 1.00 64.28 ?  60  GLU A CA    1 
ATOM   470   C  C     . GLU A 1 60  ? 106.261 153.816 106.234 1.00 65.21 ?  60  GLU A C     1 
ATOM   471   O  O     . GLU A 1 60  ? 106.233 154.136 107.429 1.00 67.47 ?  60  GLU A O     1 
ATOM   472   C  CB    . GLU A 1 60  ? 104.864 155.147 104.628 1.00 64.16 ?  60  GLU A CB    1 
ATOM   473   C  CG    . GLU A 1 60  ? 104.725 156.444 103.845 1.00 65.72 ?  60  GLU A CG    1 
ATOM   474   C  CD    . GLU A 1 60  ? 103.530 156.441 102.910 1.00 69.17 ?  60  GLU A CD    1 
ATOM   475   O  OE1   . GLU A 1 60  ? 102.691 155.522 103.017 1.00 68.12 ?  60  GLU A OE1   1 
ATOM   476   O  OE2   . GLU A 1 60  ? 103.431 157.356 102.065 1.00 67.57 -1 60  GLU A OE2   1 
ATOM   477   N  N     . ASN A 1 61  ? 106.278 152.542 105.845 1.00 59.25 ?  61  ASN A N     1 
ATOM   478   C  CA    . ASN A 1 61  ? 106.203 151.451 106.809 1.00 60.01 ?  61  ASN A CA    1 
ATOM   479   C  C     . ASN A 1 61  ? 107.567 150.982 107.292 1.00 61.33 ?  61  ASN A C     1 
ATOM   480   O  O     . ASN A 1 61  ? 107.702 149.809 107.665 1.00 64.86 ?  61  ASN A O     1 
ATOM   481   C  CB    . ASN A 1 61  ? 105.422 150.275 106.224 1.00 60.81 ?  61  ASN A CB    1 
ATOM   482   C  CG    . ASN A 1 61  ? 104.062 150.686 105.709 1.00 62.46 ?  61  ASN A CG    1 
ATOM   483   O  OD1   . ASN A 1 61  ? 103.769 151.872 105.577 1.00 63.19 ?  61  ASN A OD1   1 
ATOM   484   N  ND2   . ASN A 1 61  ? 103.208 149.708 105.458 1.00 61.88 ?  61  ASN A ND2   1 
ATOM   485   N  N     . GLN A 1 62  ? 108.568 151.862 107.280 1.00 57.49 ?  62  GLN A N     1 
ATOM   486   C  CA    . GLN A 1 62  ? 109.864 151.608 107.908 1.00 58.44 ?  62  GLN A CA    1 
ATOM   487   C  C     . GLN A 1 62  ? 110.598 150.434 107.267 1.00 57.89 ?  62  GLN A C     1 
ATOM   488   O  O     . GLN A 1 62  ? 111.367 149.733 107.930 1.00 58.51 ?  62  GLN A O     1 
ATOM   489   C  CB    . GLN A 1 62  ? 109.709 151.375 109.414 1.00 58.21 ?  62  GLN A CB    1 
ATOM   490   C  CG    . GLN A 1 62  ? 109.019 152.508 110.161 1.00 57.65 ?  62  GLN A CG    1 
ATOM   491   C  CD    . GLN A 1 62  ? 109.642 153.862 109.891 1.00 60.19 ?  62  GLN A CD    1 
ATOM   492   O  OE1   . GLN A 1 62  ? 110.613 154.254 110.538 1.00 59.91 ?  62  GLN A OE1   1 
ATOM   493   N  NE2   . GLN A 1 62  ? 109.089 154.583 108.923 1.00 58.82 ?  62  GLN A NE2   1 
ATOM   494   N  N     . TYR A 1 63  ? 110.368 150.203 105.974 1.00 55.04 ?  63  TYR A N     1 
ATOM   495   C  CA    . TYR A 1 63  ? 111.106 149.170 105.258 1.00 53.55 ?  63  TYR A CA    1 
ATOM   496   C  C     . TYR A 1 63  ? 112.366 149.719 104.604 1.00 53.47 ?  63  TYR A C     1 
ATOM   497   O  O     . TYR A 1 63  ? 113.411 149.060 104.626 1.00 52.88 ?  63  TYR A O     1 
ATOM   498   C  CB    . TYR A 1 63  ? 110.215 148.516 104.198 1.00 52.78 ?  63  TYR A CB    1 
ATOM   499   C  CG    . TYR A 1 63  ? 109.166 147.591 104.766 1.00 53.89 ?  63  TYR A CG    1 
ATOM   500   C  CD1   . TYR A 1 63  ? 109.512 146.572 105.641 1.00 52.87 ?  63  TYR A CD1   1 
ATOM   501   C  CD2   . TYR A 1 63  ? 107.829 147.735 104.423 1.00 55.05 ?  63  TYR A CD2   1 
ATOM   502   C  CE1   . TYR A 1 63  ? 108.556 145.725 106.163 1.00 53.91 ?  63  TYR A CE1   1 
ATOM   503   C  CE2   . TYR A 1 63  ? 106.866 146.893 104.939 1.00 55.36 ?  63  TYR A CE2   1 
ATOM   504   C  CZ    . TYR A 1 63  ? 107.235 145.890 105.808 1.00 56.36 ?  63  TYR A CZ    1 
ATOM   505   O  OH    . TYR A 1 63  ? 106.277 145.049 106.323 1.00 55.76 ?  63  TYR A OH    1 
ATOM   506   N  N     . TYR A 1 64  ? 112.287 150.912 104.029 1.00 49.94 ?  64  TYR A N     1 
ATOM   507   C  CA    . TYR A 1 64  ? 113.410 151.552 103.365 1.00 48.26 ?  64  TYR A CA    1 
ATOM   508   C  C     . TYR A 1 64  ? 113.866 152.769 104.157 1.00 50.88 ?  64  TYR A C     1 
ATOM   509   O  O     . TYR A 1 64  ? 113.258 153.157 105.157 1.00 53.87 ?  64  TYR A O     1 
ATOM   510   C  CB    . TYR A 1 64  ? 113.035 151.968 101.939 1.00 47.96 ?  64  TYR A CB    1 
ATOM   511   C  CG    . TYR A 1 64  ? 113.062 150.839 100.940 1.00 50.04 ?  64  TYR A CG    1 
ATOM   512   C  CD1   . TYR A 1 64  ? 113.502 149.574 101.302 1.00 48.97 ?  64  TYR A CD1   1 
ATOM   513   C  CD2   . TYR A 1 64  ? 112.648 151.039 99.633  1.00 49.89 ?  64  TYR A CD2   1 
ATOM   514   C  CE1   . TYR A 1 64  ? 113.525 148.541 100.391 1.00 45.60 ?  64  TYR A CE1   1 
ATOM   515   C  CE2   . TYR A 1 64  ? 112.670 150.015 98.716  1.00 48.10 ?  64  TYR A CE2   1 
ATOM   516   C  CZ    . TYR A 1 64  ? 113.108 148.768 99.099  1.00 47.41 ?  64  TYR A CZ    1 
ATOM   517   O  OH    . TYR A 1 64  ? 113.127 147.747 98.181  1.00 50.79 ?  64  TYR A OH    1 
ATOM   518   N  N     . GLU A 1 65  ? 114.952 153.372 103.691 1.00 53.79 ?  65  GLU A N     1 
ATOM   519   C  CA    . GLU A 1 65  ? 115.448 154.627 104.237 1.00 52.12 ?  65  GLU A CA    1 
ATOM   520   C  C     . GLU A 1 65  ? 115.083 155.759 103.288 1.00 55.07 ?  65  GLU A C     1 
ATOM   521   O  O     . GLU A 1 65  ? 115.300 155.654 102.077 1.00 56.78 ?  65  GLU A O     1 
ATOM   522   C  CB    . GLU A 1 65  ? 116.961 154.578 104.452 1.00 52.60 ?  65  GLU A CB    1 
ATOM   523   C  CG    . GLU A 1 65  ? 117.438 153.372 105.238 1.00 51.39 ?  65  GLU A CG    1 
ATOM   524   C  CD    . GLU A 1 65  ? 118.949 153.295 105.323 1.00 55.09 ?  65  GLU A CD    1 
ATOM   525   O  OE1   . GLU A 1 65  ? 119.621 153.667 104.338 1.00 57.01 ?  65  GLU A OE1   1 
ATOM   526   O  OE2   . GLU A 1 65  ? 119.464 152.866 106.377 1.00 54.12 -1 65  GLU A OE2   1 
ATOM   527   N  N     . GLU A 1 66  ? 114.521 156.833 103.840 1.00 58.01 ?  66  GLU A N     1 
ATOM   528   C  CA    . GLU A 1 66  ? 114.113 157.965 103.017 1.00 56.33 ?  66  GLU A CA    1 
ATOM   529   C  C     . GLU A 1 66  ? 115.300 158.784 102.530 1.00 56.91 ?  66  GLU A C     1 
ATOM   530   O  O     . GLU A 1 66  ? 115.226 159.375 101.447 1.00 57.92 ?  66  GLU A O     1 
ATOM   531   C  CB    . GLU A 1 66  ? 113.144 158.851 103.804 1.00 57.09 ?  66  GLU A CB    1 
ATOM   532   C  CG    . GLU A 1 66  ? 112.718 160.135 103.104 1.00 59.42 ?  66  GLU A CG    1 
ATOM   533   C  CD    . GLU A 1 66  ? 111.795 159.887 101.924 1.00 61.01 ?  66  GLU A CD    1 
ATOM   534   O  OE1   . GLU A 1 66  ? 110.596 160.225 102.028 1.00 58.42 ?  66  GLU A OE1   1 
ATOM   535   O  OE2   . GLU A 1 66  ? 112.266 159.369 100.890 1.00 62.31 -1 66  GLU A OE2   1 
ATOM   536   N  N     . GLU A 1 67  ? 116.393 158.821 103.296 1.00 58.05 ?  67  GLU A N     1 
ATOM   537   C  CA    . GLU A 1 67  ? 117.496 159.725 102.987 1.00 56.47 ?  67  GLU A CA    1 
ATOM   538   C  C     . GLU A 1 67  ? 118.138 159.398 101.644 1.00 57.31 ?  67  GLU A C     1 
ATOM   539   O  O     . GLU A 1 67  ? 118.398 160.299 100.837 1.00 57.76 ?  67  GLU A O     1 
ATOM   540   C  CB    . GLU A 1 67  ? 118.536 159.678 104.107 1.00 56.92 ?  67  GLU A CB    1 
ATOM   541   C  CG    . GLU A 1 67  ? 118.632 158.333 104.807 1.00 58.91 ?  67  GLU A CG    1 
ATOM   542   C  CD    . GLU A 1 67  ? 117.835 158.289 106.095 1.00 59.42 ?  67  GLU A CD    1 
ATOM   543   O  OE1   . GLU A 1 67  ? 116.588 158.283 106.027 1.00 57.57 ?  67  GLU A OE1   1 
ATOM   544   O  OE2   . GLU A 1 67  ? 118.456 158.265 107.179 1.00 62.17 -1 67  GLU A OE2   1 
ATOM   545   N  N     . PHE A 1 68  ? 118.404 158.118 101.381 1.00 54.61 ?  68  PHE A N     1 
ATOM   546   C  CA    . PHE A 1 68  ? 119.087 157.762 100.142 1.00 52.02 ?  68  PHE A CA    1 
ATOM   547   C  C     . PHE A 1 68  ? 118.154 157.816 98.940  1.00 51.81 ?  68  PHE A C     1 
ATOM   548   O  O     . PHE A 1 68  ? 118.604 158.111 97.827  1.00 55.05 ?  68  PHE A O     1 
ATOM   549   C  CB    . PHE A 1 68  ? 119.735 156.379 100.270 1.00 51.38 ?  68  PHE A CB    1 
ATOM   550   C  CG    . PHE A 1 68  ? 118.847 155.238 99.859  1.00 50.85 ?  68  PHE A CG    1 
ATOM   551   C  CD1   . PHE A 1 68  ? 117.934 154.701 100.746 1.00 51.28 ?  68  PHE A CD1   1 
ATOM   552   C  CD2   . PHE A 1 68  ? 118.950 154.684 98.594  1.00 48.03 ?  68  PHE A CD2   1 
ATOM   553   C  CE1   . PHE A 1 68  ? 117.123 153.648 100.371 1.00 48.97 ?  68  PHE A CE1   1 
ATOM   554   C  CE2   . PHE A 1 68  ? 118.144 153.631 98.216  1.00 46.98 ?  68  PHE A CE2   1 
ATOM   555   C  CZ    . PHE A 1 68  ? 117.232 153.111 99.107  1.00 48.15 ?  68  PHE A CZ    1 
ATOM   556   N  N     . LEU A 1 69  ? 116.864 157.543 99.137  1.00 50.98 ?  69  LEU A N     1 
ATOM   557   C  CA    . LEU A 1 69  ? 115.909 157.652 98.041  1.00 53.18 ?  69  LEU A CA    1 
ATOM   558   C  C     . LEU A 1 69  ? 115.559 159.097 97.722  1.00 53.68 ?  69  LEU A C     1 
ATOM   559   O  O     . LEU A 1 69  ? 115.025 159.369 96.641  1.00 54.19 ?  69  LEU A O     1 
ATOM   560   C  CB    . LEU A 1 69  ? 114.635 156.873 98.370  1.00 54.09 ?  69  LEU A CB    1 
ATOM   561   C  CG    . LEU A 1 69  ? 114.699 155.357 98.186  1.00 52.44 ?  69  LEU A CG    1 
ATOM   562   C  CD1   . LEU A 1 69  ? 113.479 154.688 98.796  1.00 51.87 ?  69  LEU A CD1   1 
ATOM   563   C  CD2   . LEU A 1 69  ? 114.830 155.001 96.717  1.00 50.13 ?  69  LEU A CD2   1 
ATOM   564   N  N     . SER A 1 70  ? 115.847 160.029 98.631  1.00 55.83 ?  70  SER A N     1 
ATOM   565   C  CA    . SER A 1 70  ? 115.527 161.434 98.419  1.00 54.06 ?  70  SER A CA    1 
ATOM   566   C  C     . SER A 1 70  ? 116.541 162.152 97.542  1.00 53.45 ?  70  SER A C     1 
ATOM   567   O  O     . SER A 1 70  ? 116.288 163.294 97.144  1.00 56.79 ?  70  SER A O     1 
ATOM   568   C  CB    . SER A 1 70  ? 115.414 162.156 99.764  1.00 54.37 ?  70  SER A CB    1 
ATOM   569   O  OG    . SER A 1 70  ? 116.682 162.289 100.378 1.00 54.27 ?  70  SER A OG    1 
ATOM   570   N  N     . LEU A 1 71  ? 117.674 161.523 97.232  1.00 50.47 ?  71  LEU A N     1 
ATOM   571   C  CA    . LEU A 1 71  ? 118.671 162.137 96.366  1.00 50.14 ?  71  LEU A CA    1 
ATOM   572   C  C     . LEU A 1 71  ? 118.337 161.998 94.889  1.00 50.99 ?  71  LEU A C     1 
ATOM   573   O  O     . LEU A 1 71  ? 119.032 162.588 94.055  1.00 50.24 ?  71  LEU A O     1 
ATOM   574   C  CB    . LEU A 1 71  ? 120.052 161.533 96.637  1.00 48.19 ?  71  LEU A CB    1 
ATOM   575   C  CG    . LEU A 1 71  ? 120.389 161.252 98.101  1.00 49.88 ?  71  LEU A CG    1 
ATOM   576   C  CD1   . LEU A 1 71  ? 121.394 160.123 98.208  1.00 51.77 ?  71  LEU A CD1   1 
ATOM   577   C  CD2   . LEU A 1 71  ? 120.916 162.508 98.771  1.00 51.24 ?  71  LEU A CD2   1 
ATOM   578   N  N     . TYR A 1 72  ? 117.299 161.239 94.546  1.00 48.11 ?  72  TYR A N     1 
ATOM   579   C  CA    . TYR A 1 72  ? 116.869 161.059 93.170  1.00 50.38 ?  72  TYR A CA    1 
ATOM   580   C  C     . TYR A 1 72  ? 115.433 161.533 93.015  1.00 52.50 ?  72  TYR A C     1 
ATOM   581   O  O     . TYR A 1 72  ? 114.588 161.275 93.878  1.00 52.67 ?  72  TYR A O     1 
ATOM   582   C  CB    . TYR A 1 72  ? 116.951 159.591 92.732  1.00 48.01 ?  72  TYR A CB    1 
ATOM   583   C  CG    . TYR A 1 72  ? 118.237 158.881 93.073  1.00 47.76 ?  72  TYR A CG    1 
ATOM   584   C  CD1   . TYR A 1 72  ? 118.417 158.289 94.316  1.00 46.66 ?  72  TYR A CD1   1 
ATOM   585   C  CD2   . TYR A 1 72  ? 119.258 158.770 92.141  1.00 46.11 ?  72  TYR A CD2   1 
ATOM   586   C  CE1   . TYR A 1 72  ? 119.583 157.630 94.628  1.00 44.18 ?  72  TYR A CE1   1 
ATOM   587   C  CE2   . TYR A 1 72  ? 120.427 158.109 92.443  1.00 42.59 ?  72  TYR A CE2   1 
ATOM   588   C  CZ    . TYR A 1 72  ? 120.584 157.543 93.688  1.00 44.18 ?  72  TYR A CZ    1 
ATOM   589   O  OH    . TYR A 1 72  ? 121.750 156.883 93.994  1.00 49.45 ?  72  TYR A OH    1 
ATOM   590   N  N     . SER A 1 73  ? 115.159 162.225 91.913  1.00 55.03 ?  73  SER A N     1 
ATOM   591   C  CA    . SER A 1 73  ? 113.779 162.443 91.513  1.00 56.45 ?  73  SER A CA    1 
ATOM   592   C  C     . SER A 1 73  ? 113.159 161.109 91.114  1.00 57.84 ?  73  SER A C     1 
ATOM   593   O  O     . SER A 1 73  ? 113.848 160.199 90.648  1.00 58.76 ?  73  SER A O     1 
ATOM   594   C  CB    . SER A 1 73  ? 113.701 163.434 90.353  1.00 57.18 ?  73  SER A CB    1 
ATOM   595   O  OG    . SER A 1 73  ? 113.900 162.784 89.111  1.00 57.54 ?  73  SER A OG    1 
ATOM   596   N  N     . PHE A 1 74  ? 111.843 160.989 91.313  1.00 58.15 ?  74  PHE A N     1 
ATOM   597   C  CA    . PHE A 1 74  ? 111.194 159.710 91.051  1.00 55.90 ?  74  PHE A CA    1 
ATOM   598   C  C     . PHE A 1 74  ? 111.322 159.271 89.600  1.00 58.32 ?  74  PHE A C     1 
ATOM   599   O  O     . PHE A 1 74  ? 111.248 158.070 89.325  1.00 60.17 ?  74  PHE A O     1 
ATOM   600   C  CB    . PHE A 1 74  ? 109.716 159.747 91.433  1.00 58.40 ?  74  PHE A CB    1 
ATOM   601   C  CG    . PHE A 1 74  ? 109.021 158.438 91.207  1.00 58.85 ?  74  PHE A CG    1 
ATOM   602   C  CD1   . PHE A 1 74  ? 109.255 157.363 92.045  1.00 57.77 ?  74  PHE A CD1   1 
ATOM   603   C  CD2   . PHE A 1 74  ? 108.167 158.271 90.129  1.00 58.58 ?  74  PHE A CD2   1 
ATOM   604   C  CE1   . PHE A 1 74  ? 108.636 156.151 91.825  1.00 59.26 ?  74  PHE A CE1   1 
ATOM   605   C  CE2   . PHE A 1 74  ? 107.544 157.062 89.906  1.00 59.84 ?  74  PHE A CE2   1 
ATOM   606   C  CZ    . PHE A 1 74  ? 107.780 156.002 90.752  1.00 61.18 ?  74  PHE A CZ    1 
ATOM   607   N  N     . GLU A 1 75  ? 111.513 160.203 88.665  1.00 61.63 ?  75  GLU A N     1 
ATOM   608   C  CA    . GLU A 1 75  ? 111.763 159.799 87.287  1.00 61.08 ?  75  GLU A CA    1 
ATOM   609   C  C     . GLU A 1 75  ? 113.075 159.031 87.176  1.00 62.99 ?  75  GLU A C     1 
ATOM   610   O  O     . GLU A 1 75  ? 113.167 158.044 86.439  1.00 62.51 ?  75  GLU A O     1 
ATOM   611   C  CB    . GLU A 1 75  ? 111.766 161.022 86.372  1.00 60.87 ?  75  GLU A CB    1 
ATOM   612   C  CG    . GLU A 1 75  ? 110.384 161.612 86.144  1.00 62.72 ?  75  GLU A CG    1 
ATOM   613   C  CD    . GLU A 1 75  ? 109.362 160.565 85.743  1.00 65.19 ?  75  GLU A CD    1 
ATOM   614   O  OE1   . GLU A 1 75  ? 109.556 159.911 84.696  1.00 65.33 ?  75  GLU A OE1   1 
ATOM   615   O  OE2   . GLU A 1 75  ? 108.366 160.393 86.475  1.00 64.89 -1 75  GLU A OE2   1 
ATOM   616   N  N     . ASP A 1 76  ? 114.097 159.462 87.917  1.00 58.05 ?  76  ASP A N     1 
ATOM   617   C  CA    . ASP A 1 76  ? 115.374 158.754 87.910  1.00 55.77 ?  76  ASP A CA    1 
ATOM   618   C  C     . ASP A 1 76  ? 115.252 157.370 88.539  1.00 55.43 ?  76  ASP A C     1 
ATOM   619   O  O     . ASP A 1 76  ? 115.826 156.399 88.032  1.00 60.04 ?  76  ASP A O     1 
ATOM   620   C  CB    . ASP A 1 76  ? 116.428 159.584 88.636  1.00 57.42 ?  76  ASP A CB    1 
ATOM   621   C  CG    . ASP A 1 76  ? 116.635 160.944 88.001  1.00 60.39 ?  76  ASP A CG    1 
ATOM   622   O  OD1   . ASP A 1 76  ? 116.612 161.028 86.755  1.00 59.97 ?  76  ASP A OD1   1 
ATOM   623   O  OD2   . ASP A 1 76  ? 116.821 161.928 88.746  1.00 59.16 -1 76  ASP A OD2   1 
ATOM   624   N  N     . ILE A 1 77  ? 114.518 157.261 89.648  1.00 51.09 ?  77  ILE A N     1 
ATOM   625   C  CA    . ILE A 1 77  ? 114.305 155.958 90.274  1.00 51.47 ?  77  ILE A CA    1 
ATOM   626   C  C     . ILE A 1 77  ? 113.534 155.042 89.334  1.00 51.41 ?  77  ILE A C     1 
ATOM   627   O  O     . ILE A 1 77  ? 113.823 153.842 89.230  1.00 53.07 ?  77  ILE A O     1 
ATOM   628   C  CB    . ILE A 1 77  ? 113.580 156.123 91.621  1.00 52.51 ?  77  ILE A CB    1 
ATOM   629   C  CG1   . ILE A 1 77  ? 114.276 157.182 92.473  1.00 52.79 ?  77  ILE A CG1   1 
ATOM   630   C  CG2   . ILE A 1 77  ? 113.521 154.795 92.355  1.00 51.51 ?  77  ILE A CG2   1 
ATOM   631   C  CD1   . ILE A 1 77  ? 113.857 157.175 93.924  1.00 52.94 ?  77  ILE A CD1   1 
ATOM   632   N  N     . LYS A 1 78  ? 112.535 155.592 88.644  1.00 54.77 ?  78  LYS A N     1 
ATOM   633   C  CA    . LYS A 1 78  ? 111.790 154.821 87.659  1.00 54.72 ?  78  LYS A CA    1 
ATOM   634   C  C     . LYS A 1 78  ? 112.699 154.341 86.538  1.00 54.66 ?  78  LYS A C     1 
ATOM   635   O  O     . LYS A 1 78  ? 112.597 153.193 86.100  1.00 57.65 ?  78  LYS A O     1 
ATOM   636   C  CB    . LYS A 1 78  ? 110.644 155.663 87.101  1.00 57.81 ?  78  LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 78  ? 109.402 154.874 86.730  1.00 56.70 ?  78  LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 78  ? 108.384 155.764 86.040  1.00 56.73 ?  78  LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 78  ? 107.589 154.995 85.003  1.00 57.73 ?  78  LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 78  ? 106.156 154.874 85.388  1.00 57.58 1  78  LYS A NZ    1 
ATOM   641   N  N     . GLU A 1 79  ? 113.597 155.207 86.061  1.00 55.66 ?  79  GLU A N     1 
ATOM   642   C  CA    . GLU A 1 79  ? 114.542 154.805 85.023  1.00 55.52 ?  79  GLU A CA    1 
ATOM   643   C  C     . GLU A 1 79  ? 115.452 153.685 85.510  1.00 52.99 ?  79  GLU A C     1 
ATOM   644   O  O     . GLU A 1 79  ? 115.744 152.742 84.765  1.00 55.14 ?  79  GLU A O     1 
ATOM   645   C  CB    . GLU A 1 79  ? 115.373 156.008 84.577  1.00 56.06 ?  79  GLU A CB    1 
ATOM   646   C  CG    . GLU A 1 79  ? 114.637 156.989 83.685  1.00 56.91 ?  79  GLU A CG    1 
ATOM   647   C  CD    . GLU A 1 79  ? 115.507 158.158 83.271  1.00 60.38 ?  79  GLU A CD    1 
ATOM   648   O  OE1   . GLU A 1 79  ? 116.539 157.926 82.609  1.00 60.58 ?  79  GLU A OE1   1 
ATOM   649   O  OE2   . GLU A 1 79  ? 115.164 159.309 83.613  1.00 61.84 -1 79  GLU A OE2   1 
ATOM   650   N  N     . VAL A 1 80  ? 115.912 153.776 86.757  1.00 45.61 ?  80  VAL A N     1 
ATOM   651   C  CA    . VAL A 1 80  ? 116.758 152.726 87.322  1.00 43.99 ?  80  VAL A CA    1 
ATOM   652   C  C     . VAL A 1 80  ? 116.003 151.403 87.380  1.00 48.77 ?  80  VAL A C     1 
ATOM   653   O  O     . VAL A 1 80  ? 116.533 150.346 87.008  1.00 49.84 ?  80  VAL A O     1 
ATOM   654   C  CB    . VAL A 1 80  ? 117.268 153.155 88.711  1.00 43.52 ?  80  VAL A CB    1 
ATOM   655   C  CG1   . VAL A 1 80  ? 117.835 151.971 89.466  1.00 45.04 ?  80  VAL A CG1   1 
ATOM   656   C  CG2   . VAL A 1 80  ? 118.310 154.249 88.572  1.00 44.18 ?  80  VAL A CG2   1 
ATOM   657   N  N     . PHE A 1 81  ? 114.749 151.441 87.836  1.00 48.14 ?  81  PHE A N     1 
ATOM   658   C  CA    . PHE A 1 81  ? 113.958 150.218 87.923  1.00 44.30 ?  81  PHE A CA    1 
ATOM   659   C  C     . PHE A 1 81  ? 113.656 149.648 86.541  1.00 47.34 ?  81  PHE A C     1 
ATOM   660   O  O     . PHE A 1 81  ? 113.615 148.425 86.364  1.00 49.22 ?  81  PHE A O     1 
ATOM   661   C  CB    . PHE A 1 81  ? 112.671 150.481 88.699  1.00 44.78 ?  81  PHE A CB    1 
ATOM   662   C  CG    . PHE A 1 81  ? 112.798 150.246 90.177  1.00 44.53 ?  81  PHE A CG    1 
ATOM   663   C  CD1   . PHE A 1 81  ? 113.410 151.184 90.989  1.00 45.67 ?  81  PHE A CD1   1 
ATOM   664   C  CD2   . PHE A 1 81  ? 112.304 149.090 90.753  1.00 46.79 ?  81  PHE A CD2   1 
ATOM   665   C  CE1   . PHE A 1 81  ? 113.528 150.973 92.349  1.00 45.99 ?  81  PHE A CE1   1 
ATOM   666   C  CE2   . PHE A 1 81  ? 112.420 148.874 92.112  1.00 45.17 ?  81  PHE A CE2   1 
ATOM   667   C  CZ    . PHE A 1 81  ? 113.033 149.816 92.910  1.00 43.40 ?  81  PHE A CZ    1 
ATOM   668   N  N     . LYS A 1 82  ? 113.434 150.514 85.548  1.00 47.06 ?  82  LYS A N     1 
ATOM   669   C  CA    . LYS A 1 82  ? 113.288 150.037 84.175  1.00 50.44 ?  82  LYS A CA    1 
ATOM   670   C  C     . LYS A 1 82  ? 114.561 149.355 83.698  1.00 50.45 ?  82  LYS A C     1 
ATOM   671   O  O     . LYS A 1 82  ? 114.506 148.312 83.039  1.00 52.83 ?  82  LYS A O     1 
ATOM   672   C  CB    . LYS A 1 82  ? 112.929 151.187 83.232  1.00 51.75 ?  82  LYS A CB    1 
ATOM   673   C  CG    . LYS A 1 82  ? 111.649 151.938 83.556  1.00 53.41 ?  82  LYS A CG    1 
ATOM   674   C  CD    . LYS A 1 82  ? 110.446 151.022 83.574  1.00 53.59 ?  82  LYS A CD    1 
ATOM   675   C  CE    . LYS A 1 82  ? 109.366 151.522 82.631  1.00 54.29 ?  82  LYS A CE    1 
ATOM   676   N  NZ    . LYS A 1 82  ? 109.897 151.758 81.259  1.00 52.75 1  82  LYS A NZ    1 
ATOM   677   N  N     . THR A 1 83  ? 115.717 149.936 84.022  1.00 43.33 ?  83  THR A N     1 
ATOM   678   C  CA    . THR A 1 83  ? 116.985 149.324 83.639  1.00 45.07 ?  83  THR A CA    1 
ATOM   679   C  C     . THR A 1 83  ? 117.137 147.945 84.267  1.00 46.81 ?  83  THR A C     1 
ATOM   680   O  O     . THR A 1 83  ? 117.621 147.009 83.620  1.00 47.75 ?  83  THR A O     1 
ATOM   681   C  CB    . THR A 1 83  ? 118.148 150.233 84.040  1.00 46.72 ?  83  THR A CB    1 
ATOM   682   O  OG1   . THR A 1 83  ? 117.942 151.539 83.492  1.00 50.88 ?  83  THR A OG1   1 
ATOM   683   C  CG2   . THR A 1 83  ? 119.461 149.681 83.518  1.00 46.24 ?  83  THR A CG2   1 
ATOM   684   N  N     . ALA A 1 84  ? 116.728 147.800 85.529  1.00 46.18 ?  84  ALA A N     1 
ATOM   685   C  CA    . ALA A 1 84  ? 116.790 146.490 86.172  1.00 41.53 ?  84  ALA A CA    1 
ATOM   686   C  C     . ALA A 1 84  ? 115.858 145.491 85.500  1.00 42.96 ?  84  ALA A C     1 
ATOM   687   O  O     . ALA A 1 84  ? 116.247 144.347 85.240  1.00 47.86 ?  84  ALA A O     1 
ATOM   688   C  CB    . ALA A 1 84  ? 116.454 146.617 87.656  1.00 43.85 ?  84  ALA A CB    1 
ATOM   689   N  N     . TYR A 1 85  ? 114.624 145.904 85.207  1.00 47.92 ?  85  TYR A N     1 
ATOM   690   C  CA    . TYR A 1 85  ? 113.645 144.992 84.632  1.00 47.31 ?  85  TYR A CA    1 
ATOM   691   C  C     . TYR A 1 85  ? 113.812 144.805 83.130  1.00 46.51 ?  85  TYR A C     1 
ATOM   692   O  O     . TYR A 1 85  ? 113.254 143.853 82.576  1.00 49.04 ?  85  TYR A O     1 
ATOM   693   C  CB    . TYR A 1 85  ? 112.228 145.483 84.936  1.00 47.59 ?  85  TYR A CB    1 
ATOM   694   C  CG    . TYR A 1 85  ? 111.754 145.155 86.334  1.00 48.42 ?  85  TYR A CG    1 
ATOM   695   C  CD1   . TYR A 1 85  ? 111.999 146.019 87.392  1.00 47.29 ?  85  TYR A CD1   1 
ATOM   696   C  CD2   . TYR A 1 85  ? 111.066 143.980 86.596  1.00 46.70 ?  85  TYR A CD2   1 
ATOM   697   C  CE1   . TYR A 1 85  ? 111.569 145.724 88.669  1.00 46.62 ?  85  TYR A CE1   1 
ATOM   698   C  CE2   . TYR A 1 85  ? 110.632 143.675 87.869  1.00 46.81 ?  85  TYR A CE2   1 
ATOM   699   C  CZ    . TYR A 1 85  ? 110.887 144.550 88.901  1.00 47.28 ?  85  TYR A CZ    1 
ATOM   700   O  OH    . TYR A 1 85  ? 110.456 144.249 90.172  1.00 49.55 ?  85  TYR A OH    1 
ATOM   701   N  N     . ALA A 1 86  ? 114.560 145.685 82.459  1.00 45.11 ?  86  ALA A N     1 
ATOM   702   C  CA    . ALA A 1 86  ? 114.777 145.522 81.026  1.00 44.63 ?  86  ALA A CA    1 
ATOM   703   C  C     . ALA A 1 86  ? 115.613 144.287 80.720  1.00 47.07 ?  86  ALA A C     1 
ATOM   704   O  O     . ALA A 1 86  ? 115.463 143.688 79.650  1.00 48.77 ?  86  ALA A O     1 
ATOM   705   C  CB    . ALA A 1 86  ? 115.448 146.766 80.444  1.00 44.19 ?  86  ALA A CB    1 
ATOM   706   N  N     . LYS A 1 87  ? 116.498 143.899 81.640  1.00 46.25 ?  87  LYS A N     1 
ATOM   707   C  CA    . LYS A 1 87  ? 117.314 142.710 81.429  1.00 45.97 ?  87  LYS A CA    1 
ATOM   708   C  C     . LYS A 1 87  ? 116.462 141.448 81.389  1.00 45.92 ?  87  LYS A C     1 
ATOM   709   O  O     . LYS A 1 87  ? 116.819 140.480 80.707  1.00 45.76 ?  87  LYS A O     1 
ATOM   710   C  CB    . LYS A 1 87  ? 118.380 142.615 82.524  1.00 42.62 ?  87  LYS A CB    1 
ATOM   711   C  CG    . LYS A 1 87  ? 118.962 141.228 82.746  1.00 44.03 ?  87  LYS A CG    1 
ATOM   712   C  CD    . LYS A 1 87  ? 120.328 141.084 82.097  1.00 45.15 ?  87  LYS A CD    1 
ATOM   713   C  CE    . LYS A 1 87  ? 120.941 139.730 82.411  1.00 45.16 ?  87  LYS A CE    1 
ATOM   714   N  NZ    . LYS A 1 87  ? 122.280 139.565 81.784  1.00 42.00 1  87  LYS A NZ    1 
ATOM   715   N  N     . LYS A 1 88  ? 115.321 141.454 82.080  1.00 48.62 ?  88  LYS A N     1 
ATOM   716   C  CA    . LYS A 1 88  ? 114.468 140.276 82.219  1.00 47.59 ?  88  LYS A CA    1 
ATOM   717   C  C     . LYS A 1 88  ? 115.270 139.095 82.756  1.00 43.20 ?  88  LYS A C     1 
ATOM   718   O  O     . LYS A 1 88  ? 115.312 138.014 82.166  1.00 46.03 ?  88  LYS A O     1 
ATOM   719   C  CB    . LYS A 1 88  ? 113.786 139.925 80.894  1.00 49.47 ?  88  LYS A CB    1 
ATOM   720   C  CG    . LYS A 1 88  ? 112.480 140.665 80.651  1.00 49.24 ?  88  LYS A CG    1 
ATOM   721   C  CD    . LYS A 1 88  ? 112.057 140.593 79.191  1.00 47.96 ?  88  LYS A CD    1 
ATOM   722   C  CE    . LYS A 1 88  ? 113.252 140.659 78.255  1.00 49.54 ?  88  LYS A CE    1 
ATOM   723   N  NZ    . LYS A 1 88  ? 112.838 140.610 76.826  1.00 47.96 1  88  LYS A NZ    1 
ATOM   724   N  N     . PHE A 1 89  ? 115.927 139.322 83.891  1.00 42.48 ?  89  PHE A N     1 
ATOM   725   C  CA    . PHE A 1 89  ? 116.763 138.296 84.493  1.00 38.98 ?  89  PHE A CA    1 
ATOM   726   C  C     . PHE A 1 89  ? 115.919 137.109 84.933  1.00 41.01 ?  89  PHE A C     1 
ATOM   727   O  O     . PHE A 1 89  ? 114.842 137.269 85.511  1.00 44.65 ?  89  PHE A O     1 
ATOM   728   C  CB    . PHE A 1 89  ? 117.531 138.870 85.685  1.00 35.95 ?  89  PHE A CB    1 
ATOM   729   C  CG    . PHE A 1 89  ? 118.228 137.832 86.517  1.00 37.82 ?  89  PHE A CG    1 
ATOM   730   C  CD1   . PHE A 1 89  ? 119.490 137.385 86.173  1.00 35.27 ?  89  PHE A CD1   1 
ATOM   731   C  CD2   . PHE A 1 89  ? 117.622 137.303 87.644  1.00 35.78 ?  89  PHE A CD2   1 
ATOM   732   C  CE1   . PHE A 1 89  ? 120.132 136.432 86.932  1.00 37.73 ?  89  PHE A CE1   1 
ATOM   733   C  CE2   . PHE A 1 89  ? 118.260 136.349 88.406  1.00 35.76 ?  89  PHE A CE2   1 
ATOM   734   C  CZ    . PHE A 1 89  ? 119.515 135.913 88.051  1.00 38.16 ?  89  PHE A CZ    1 
ATOM   735   N  N     . ARG A 1 90  ? 116.419 135.908 84.657  1.00 41.13 ?  90  ARG A N     1 
ATOM   736   C  CA    . ARG A 1 90  ? 115.775 134.674 85.076  1.00 40.95 ?  90  ARG A CA    1 
ATOM   737   C  C     . ARG A 1 90  ? 116.784 133.828 85.833  1.00 41.23 ?  90  ARG A C     1 
ATOM   738   O  O     . ARG A 1 90  ? 117.905 133.621 85.358  1.00 43.62 ?  90  ARG A O     1 
ATOM   739   C  CB    . ARG A 1 90  ? 115.220 133.897 83.879  1.00 42.51 ?  90  ARG A CB    1 
ATOM   740   C  CG    . ARG A 1 90  ? 114.258 134.692 83.016  1.00 42.59 ?  90  ARG A CG    1 
ATOM   741   C  CD    . ARG A 1 90  ? 112.847 134.642 83.574  1.00 45.13 ?  90  ARG A CD    1 
ATOM   742   N  NE    . ARG A 1 90  ? 111.966 135.590 82.904  1.00 45.28 ?  90  ARG A NE    1 
ATOM   743   C  CZ    . ARG A 1 90  ? 111.749 136.833 83.315  1.00 47.41 ?  90  ARG A CZ    1 
ATOM   744   N  NH1   . ARG A 1 90  ? 112.318 137.307 84.410  1.00 46.93 1  90  ARG A NH1   1 
ATOM   745   N  NH2   . ARG A 1 90  ? 110.939 137.617 82.610  1.00 44.82 ?  90  ARG A NH2   1 
ATOM   746   N  N     . PHE A 1 91  ? 116.390 133.353 87.004  1.00 36.44 ?  91  PHE A N     1 
ATOM   747   C  CA    . PHE A 1 91  ? 117.251 132.468 87.773  1.00 36.22 ?  91  PHE A CA    1 
ATOM   748   C  C     . PHE A 1 91  ? 117.419 131.149 87.028  1.00 42.87 ?  91  PHE A C     1 
ATOM   749   O  O     . PHE A 1 91  ? 116.421 130.542 86.621  1.00 45.07 ?  91  PHE A O     1 
ATOM   750   C  CB    . PHE A 1 91  ? 116.663 132.229 89.159  1.00 35.20 ?  91  PHE A CB    1 
ATOM   751   C  CG    . PHE A 1 91  ? 116.765 133.416 90.073  1.00 39.44 ?  91  PHE A CG    1 
ATOM   752   C  CD1   . PHE A 1 91  ? 117.916 133.648 90.805  1.00 42.42 ?  91  PHE A CD1   1 
ATOM   753   C  CD2   . PHE A 1 91  ? 115.712 134.303 90.198  1.00 39.20 ?  91  PHE A CD2   1 
ATOM   754   C  CE1   . PHE A 1 91  ? 118.013 134.737 91.646  1.00 38.91 ?  91  PHE A CE1   1 
ATOM   755   C  CE2   . PHE A 1 91  ? 115.802 135.395 91.037  1.00 39.18 ?  91  PHE A CE2   1 
ATOM   756   C  CZ    . PHE A 1 91  ? 116.953 135.612 91.762  1.00 38.29 ?  91  PHE A CZ    1 
ATOM   757   N  N     . PRO A 1 92  ? 118.651 130.676 86.823  1.00 41.57 ?  92  PRO A N     1 
ATOM   758   C  CA    . PRO A 1 92  ? 118.840 129.446 86.042  1.00 37.12 ?  92  PRO A CA    1 
ATOM   759   C  C     . PRO A 1 92  ? 118.525 128.178 86.810  1.00 38.04 ?  92  PRO A C     1 
ATOM   760   O  O     . PRO A 1 92  ? 118.359 127.123 86.183  1.00 40.67 ?  92  PRO A O     1 
ATOM   761   C  CB    . PRO A 1 92  ? 120.324 129.506 85.666  1.00 38.47 ?  92  PRO A CB    1 
ATOM   762   C  CG    . PRO A 1 92  ? 120.950 130.227 86.810  1.00 39.59 ?  92  PRO A CG    1 
ATOM   763   C  CD    . PRO A 1 92  ? 119.927 131.210 87.331  1.00 40.78 ?  92  PRO A CD    1 
ATOM   764   N  N     . SER A 1 93  ? 118.435 128.242 88.135  1.00 39.30 ?  93  SER A N     1 
ATOM   765   C  CA    . SER A 1 93  ? 118.222 127.062 88.954  1.00 42.91 ?  93  SER A CA    1 
ATOM   766   C  C     . SER A 1 93  ? 117.250 127.400 90.073  1.00 44.00 ?  93  SER A C     1 
ATOM   767   O  O     . SER A 1 93  ? 117.051 128.565 90.421  1.00 46.31 ?  93  SER A O     1 
ATOM   768   C  CB    . SER A 1 93  ? 119.542 126.538 89.534  1.00 41.29 ?  93  SER A CB    1 
ATOM   769   O  OG    . SER A 1 93  ? 119.974 127.336 90.621  1.00 40.49 ?  93  SER A OG    1 
ATOM   770   N  N     . PHE A 1 94  ? 116.636 126.355 90.632  1.00 41.93 ?  94  PHE A N     1 
ATOM   771   C  CA    . PHE A 1 94  ? 115.711 126.556 91.741  1.00 42.32 ?  94  PHE A CA    1 
ATOM   772   C  C     . PHE A 1 94  ? 116.433 127.071 92.979  1.00 43.88 ?  94  PHE A C     1 
ATOM   773   O  O     . PHE A 1 94  ? 115.884 127.886 93.727  1.00 46.67 ?  94  PHE A O     1 
ATOM   774   C  CB    . PHE A 1 94  ? 114.966 125.261 92.057  1.00 41.55 ?  94  PHE A CB    1 
ATOM   775   C  CG    . PHE A 1 94  ? 114.325 125.253 93.414  1.00 43.53 ?  94  PHE A CG    1 
ATOM   776   C  CD1   . PHE A 1 94  ? 113.225 126.049 93.677  1.00 44.19 ?  94  PHE A CD1   1 
ATOM   777   C  CD2   . PHE A 1 94  ? 114.823 124.454 94.427  1.00 44.94 ?  94  PHE A CD2   1 
ATOM   778   C  CE1   . PHE A 1 94  ? 112.638 126.051 94.924  1.00 43.92 ?  94  PHE A CE1   1 
ATOM   779   C  CE2   . PHE A 1 94  ? 114.237 124.451 95.677  1.00 46.60 ?  94  PHE A CE2   1 
ATOM   780   C  CZ    . PHE A 1 94  ? 113.143 125.251 95.925  1.00 44.64 ?  94  PHE A CZ    1 
ATOM   781   N  N     . MET A 1 95  ? 117.657 126.596 93.221  1.00 41.38 ?  95  MET A N     1 
ATOM   782   C  CA    . MET A 1 95  ? 118.381 127.001 94.421  1.00 36.23 ?  95  MET A CA    1 
ATOM   783   C  C     . MET A 1 95  ? 118.687 128.491 94.420  1.00 39.46 ?  95  MET A C     1 
ATOM   784   O  O     . MET A 1 95  ? 118.626 129.138 95.468  1.00 45.02 ?  95  MET A O     1 
ATOM   785   C  CB    . MET A 1 95  ? 119.671 126.195 94.562  1.00 42.26 ?  95  MET A CB    1 
ATOM   786   C  CG    . MET A 1 95  ? 120.086 125.825 95.995  1.00 44.32 ?  95  MET A CG    1 
ATOM   787   S  SD    . MET A 1 95  ? 118.838 125.554 97.280  1.00 53.46 ?  95  MET A SD    1 
ATOM   788   C  CE    . MET A 1 95  ? 117.672 124.452 96.483  1.00 45.67 ?  95  MET A CE    1 
ATOM   789   N  N     . SER A 1 96  ? 119.027 129.055 93.260  1.00 35.10 ?  96  SER A N     1 
ATOM   790   C  CA    . SER A 1 96  ? 119.335 130.480 93.195  1.00 33.05 ?  96  SER A CA    1 
ATOM   791   C  C     . SER A 1 96  ? 118.153 131.319 93.665  1.00 34.07 ?  96  SER A C     1 
ATOM   792   O  O     . SER A 1 96  ? 118.278 132.144 94.582  1.00 34.98 ?  96  SER A O     1 
ATOM   793   C  CB    . SER A 1 96  ? 119.723 130.855 91.767  1.00 35.24 ?  96  SER A CB    1 
ATOM   794   O  OG    . SER A 1 96  ? 120.488 129.828 91.165  1.00 38.59 ?  96  SER A OG    1 
ATOM   795   N  N     . ALA A 1 97  ? 116.986 131.093 93.061  1.00 40.03 ?  97  ALA A N     1 
ATOM   796   C  CA    . ALA A 1 97  ? 115.796 131.855 93.418  1.00 37.07 ?  97  ALA A CA    1 
ATOM   797   C  C     . ALA A 1 97  ? 115.354 131.556 94.843  1.00 37.56 ?  97  ALA A C     1 
ATOM   798   O  O     . ALA A 1 97  ? 114.921 132.459 95.564  1.00 45.57 ?  97  ALA A O     1 
ATOM   799   C  CB    . ALA A 1 97  ? 114.671 131.553 92.434  1.00 36.46 ?  97  ALA A CB    1 
ATOM   800   N  N     . PHE A 1 98  ? 115.440 130.292 95.260  1.00 33.25 ?  98  PHE A N     1 
ATOM   801   C  CA    . PHE A 1 98  ? 115.031 129.932 96.610  1.00 35.49 ?  98  PHE A CA    1 
ATOM   802   C  C     . PHE A 1 98  ? 115.894 130.638 97.645  1.00 37.06 ?  98  PHE A C     1 
ATOM   803   O  O     . PHE A 1 98  ? 115.381 131.215 98.610  1.00 45.07 ?  98  PHE A O     1 
ATOM   804   C  CB    . PHE A 1 98  ? 115.100 128.417 96.792  1.00 40.98 ?  98  PHE A CB    1 
ATOM   805   C  CG    . PHE A 1 98  ? 114.923 127.972 98.214  1.00 42.29 ?  98  PHE A CG    1 
ATOM   806   C  CD1   . PHE A 1 98  ? 113.660 127.903 98.776  1.00 41.66 ?  98  PHE A CD1   1 
ATOM   807   C  CD2   . PHE A 1 98  ? 116.016 127.631 98.990  1.00 42.38 ?  98  PHE A CD2   1 
ATOM   808   C  CE1   . PHE A 1 98  ? 113.493 127.501 100.082 1.00 41.14 ?  98  PHE A CE1   1 
ATOM   809   C  CE2   . PHE A 1 98  ? 115.854 127.228 100.298 1.00 42.94 ?  98  PHE A CE2   1 
ATOM   810   C  CZ    . PHE A 1 98  ? 114.590 127.162 100.844 1.00 42.27 ?  98  PHE A CZ    1 
ATOM   811   N  N     . LYS A 1 99  ? 117.213 130.613 97.450  1.00 39.01 ?  99  LYS A N     1 
ATOM   812   C  CA    . LYS A 1 99  ? 118.113 131.279 98.380  1.00 38.77 ?  99  LYS A CA    1 
ATOM   813   C  C     . LYS A 1 99  ? 117.874 132.779 98.394  1.00 39.03 ?  99  LYS A C     1 
ATOM   814   O  O     . LYS A 1 99  ? 117.849 133.395 99.465  1.00 41.24 ?  99  LYS A O     1 
ATOM   815   C  CB    . LYS A 1 99  ? 119.565 130.966 98.022  1.00 38.86 ?  99  LYS A CB    1 
ATOM   816   C  CG    . LYS A 1 99  ? 119.991 129.550 98.367  1.00 41.35 ?  99  LYS A CG    1 
ATOM   817   C  CD    . LYS A 1 99  ? 119.592 129.180 99.783  1.00 43.43 ?  99  LYS A CD    1 
ATOM   818   C  CE    . LYS A 1 99  ? 120.745 128.537 100.529 1.00 41.25 ?  99  LYS A CE    1 
ATOM   819   N  NZ    . LYS A 1 99  ? 120.640 128.759 101.996 1.00 42.13 1  99  LYS A NZ    1 
ATOM   820   N  N     . PHE A 1 100 ? 117.670 133.389 97.221  1.00 34.65 ?  100 PHE A N     1 
ATOM   821   C  CA    . PHE A 1 100 ? 117.411 134.824 97.209  1.00 34.54 ?  100 PHE A CA    1 
ATOM   822   C  C     . PHE A 1 100 ? 116.129 135.158 97.961  1.00 36.68 ?  100 PHE A C     1 
ATOM   823   O  O     . PHE A 1 100 ? 116.131 135.994 98.870  1.00 42.14 ?  100 PHE A O     1 
ATOM   824   C  CB    . PHE A 1 100 ? 117.331 135.364 95.785  1.00 36.23 ?  100 PHE A CB    1 
ATOM   825   C  CG    . PHE A 1 100 ? 116.932 136.808 95.735  1.00 36.68 ?  100 PHE A CG    1 
ATOM   826   C  CD1   . PHE A 1 100 ? 117.825 137.794 96.116  1.00 37.98 ?  100 PHE A CD1   1 
ATOM   827   C  CD2   . PHE A 1 100 ? 115.655 137.179 95.353  1.00 36.45 ?  100 PHE A CD2   1 
ATOM   828   C  CE1   . PHE A 1 100 ? 117.461 139.122 96.097  1.00 38.96 ?  100 PHE A CE1   1 
ATOM   829   C  CE2   . PHE A 1 100 ? 115.286 138.506 95.331  1.00 39.45 ?  100 PHE A CE2   1 
ATOM   830   C  CZ    . PHE A 1 100 ? 116.190 139.479 95.704  1.00 39.03 ?  100 PHE A CZ    1 
ATOM   831   N  N     . TYR A 1 101 ? 115.026 134.499 97.613  1.00 41.22 ?  101 TYR A N     1 
ATOM   832   C  CA    . TYR A 1 101 ? 113.739 134.842 98.199  1.00 38.44 ?  101 TYR A CA    1 
ATOM   833   C  C     . TYR A 1 101 ? 113.576 134.328 99.621  1.00 40.02 ?  101 TYR A C     1 
ATOM   834   O  O     . TYR A 1 101 ? 112.578 134.660 100.268 1.00 46.64 ?  101 TYR A O     1 
ATOM   835   C  CB    . TYR A 1 101 ? 112.607 134.327 97.308  1.00 38.76 ?  101 TYR A CB    1 
ATOM   836   C  CG    . TYR A 1 101 ? 112.459 135.131 96.037  1.00 36.64 ?  101 TYR A CG    1 
ATOM   837   C  CD1   . TYR A 1 101 ? 111.947 136.420 96.066  1.00 39.62 ?  101 TYR A CD1   1 
ATOM   838   C  CD2   . TYR A 1 101 ? 112.855 134.613 94.814  1.00 35.22 ?  101 TYR A CD2   1 
ATOM   839   C  CE1   . TYR A 1 101 ? 111.820 137.164 94.910  1.00 39.29 ?  101 TYR A CE1   1 
ATOM   840   C  CE2   . TYR A 1 101 ? 112.734 135.348 93.654  1.00 39.50 ?  101 TYR A CE2   1 
ATOM   841   C  CZ    . TYR A 1 101 ? 112.216 136.623 93.707  1.00 41.13 ?  101 TYR A CZ    1 
ATOM   842   O  OH    . TYR A 1 101 ? 112.094 137.359 92.552  1.00 39.45 ?  101 TYR A OH    1 
ATOM   843   N  N     . ASN A 1 102 ? 114.520 133.534 100.123 1.00 40.55 ?  102 ASN A N     1 
ATOM   844   C  CA    . ASN A 1 102 ? 114.499 133.124 101.518 1.00 41.46 ?  102 ASN A CA    1 
ATOM   845   C  C     . ASN A 1 102 ? 115.472 133.897 102.397 1.00 43.05 ?  102 ASN A C     1 
ATOM   846   O  O     . ASN A 1 102 ? 115.242 133.988 103.608 1.00 45.65 ?  102 ASN A O     1 
ATOM   847   C  CB    . ASN A 1 102 ? 114.808 131.626 101.634 1.00 42.60 ?  102 ASN A CB    1 
ATOM   848   C  CG    . ASN A 1 102 ? 113.557 130.771 101.644 1.00 44.82 ?  102 ASN A CG    1 
ATOM   849   O  OD1   . ASN A 1 102 ? 112.657 130.958 100.826 1.00 46.40 ?  102 ASN A OD1   1 
ATOM   850   N  ND2   . ASN A 1 102 ? 113.493 129.829 102.576 1.00 44.73 ?  102 ASN A ND2   1 
ATOM   851   N  N     . ASP A 1 103 ? 116.543 134.454 101.835 1.00 43.44 ?  103 ASP A N     1 
ATOM   852   C  CA    . ASP A 1 103 ? 117.565 135.122 102.632 1.00 41.09 ?  103 ASP A CA    1 
ATOM   853   C  C     . ASP A 1 103 ? 117.658 136.620 102.394 1.00 41.31 ?  103 ASP A C     1 
ATOM   854   O  O     . ASP A 1 103 ? 117.869 137.373 103.345 1.00 47.96 ?  103 ASP A O     1 
ATOM   855   C  CB    . ASP A 1 103 ? 118.936 134.493 102.358 1.00 44.45 ?  103 ASP A CB    1 
ATOM   856   C  CG    . ASP A 1 103 ? 119.028 133.059 102.838 1.00 46.42 ?  103 ASP A CG    1 
ATOM   857   O  OD1   . ASP A 1 103 ? 118.017 132.532 103.347 1.00 47.25 ?  103 ASP A OD1   1 
ATOM   858   O  OD2   . ASP A 1 103 ? 120.113 132.456 102.705 1.00 48.74 -1 103 ASP A OD2   1 
ATOM   859   N  N     . TYR A 1 104 ? 117.508 137.082 101.150 1.00 31.26 ?  104 TYR A N     1 
ATOM   860   C  CA    . TYR A 1 104 ? 117.785 138.469 100.811 1.00 37.51 ?  104 TYR A CA    1 
ATOM   861   C  C     . TYR A 1 104 ? 116.568 139.257 100.353 1.00 39.68 ?  104 TYR A C     1 
ATOM   862   O  O     . TYR A 1 104 ? 116.583 140.487 100.455 1.00 44.70 ?  104 TYR A O     1 
ATOM   863   C  CB    . TYR A 1 104 ? 118.859 138.540 99.715  1.00 36.23 ?  104 TYR A CB    1 
ATOM   864   C  CG    . TYR A 1 104 ? 120.130 137.810 100.076 1.00 39.20 ?  104 TYR A CG    1 
ATOM   865   C  CD1   . TYR A 1 104 ? 121.117 138.429 100.828 1.00 34.99 ?  104 TYR A CD1   1 
ATOM   866   C  CD2   . TYR A 1 104 ? 120.337 136.498 99.674  1.00 34.27 ?  104 TYR A CD2   1 
ATOM   867   C  CE1   . TYR A 1 104 ? 122.276 137.765 101.166 1.00 36.30 ?  104 TYR A CE1   1 
ATOM   868   C  CE2   . TYR A 1 104 ? 121.494 135.824 100.008 1.00 34.79 ?  104 TYR A CE2   1 
ATOM   869   C  CZ    . TYR A 1 104 ? 122.461 136.463 100.755 1.00 39.47 ?  104 TYR A CZ    1 
ATOM   870   O  OH    . TYR A 1 104 ? 123.616 135.799 101.091 1.00 37.58 ?  104 TYR A OH    1 
ATOM   871   N  N     . ALA A 1 105 ? 115.529 138.597 99.852  1.00 39.31 ?  105 ALA A N     1 
ATOM   872   C  CA    . ALA A 1 105 ? 114.345 139.318 99.406  1.00 40.02 ?  105 ALA A CA    1 
ATOM   873   C  C     . ALA A 1 105 ? 113.613 139.926 100.595 1.00 43.24 ?  105 ALA A C     1 
ATOM   874   O  O     . ALA A 1 105 ? 113.436 139.281 101.632 1.00 41.64 ?  105 ALA A O     1 
ATOM   875   C  CB    . ALA A 1 105 ? 113.410 138.391 98.634  1.00 37.86 ?  105 ALA A CB    1 
ATOM   876   N  N     . LEU A 1 106 ? 113.196 141.178 100.442 1.00 47.41 ?  106 LEU A N     1 
ATOM   877   C  CA    . LEU A 1 106 ? 112.457 141.852 101.499 1.00 45.87 ?  106 LEU A CA    1 
ATOM   878   C  C     . LEU A 1 106 ? 111.078 141.227 101.666 1.00 47.88 ?  106 LEU A C     1 
ATOM   879   O  O     . LEU A 1 106 ? 110.374 140.959 100.690 1.00 46.17 ?  106 LEU A O     1 
ATOM   880   C  CB    . LEU A 1 106 ? 112.325 143.342 101.192 1.00 46.17 ?  106 LEU A CB    1 
ATOM   881   C  CG    . LEU A 1 106 ? 111.697 144.214 102.279 1.00 44.92 ?  106 LEU A CG    1 
ATOM   882   C  CD1   . LEU A 1 106 ? 112.605 144.298 103.492 1.00 43.99 ?  106 LEU A CD1   1 
ATOM   883   C  CD2   . LEU A 1 106 ? 111.405 145.598 101.739 1.00 45.17 ?  106 LEU A CD2   1 
ATOM   884   N  N     . LYS A 1 107 ? 110.697 141.000 102.917 1.00 54.76 ?  107 LYS A N     1 
ATOM   885   C  CA    . LYS A 1 107 ? 109.406 140.430 103.257 1.00 53.91 ?  107 LYS A CA    1 
ATOM   886   C  C     . LYS A 1 107 ? 108.669 141.366 104.204 1.00 54.18 ?  107 LYS A C     1 
ATOM   887   O  O     . LYS A 1 107 ? 109.268 142.233 104.845 1.00 54.39 ?  107 LYS A O     1 
ATOM   888   C  CB    . LYS A 1 107 ? 109.560 139.044 103.899 1.00 51.79 ?  107 LYS A CB    1 
ATOM   889   C  CG    . LYS A 1 107 ? 109.969 137.956 102.925 1.00 50.81 ?  107 LYS A CG    1 
ATOM   890   C  CD    . LYS A 1 107 ? 110.255 136.651 103.645 1.00 55.44 ?  107 LYS A CD    1 
ATOM   891   C  CE    . LYS A 1 107 ? 110.623 135.553 102.663 1.00 54.96 ?  107 LYS A CE    1 
ATOM   892   N  NZ    . LYS A 1 107 ? 111.227 134.373 103.344 1.00 51.84 1  107 LYS A NZ    1 
ATOM   893   N  N     . THR A 1 108 ? 107.353 141.187 104.276 1.00 60.48 ?  108 THR A N     1 
ATOM   894   C  CA    . THR A 1 108 ? 106.536 141.994 105.164 1.00 61.10 ?  108 THR A CA    1 
ATOM   895   C  C     . THR A 1 108 ? 106.940 141.754 106.619 1.00 62.03 ?  108 THR A C     1 
ATOM   896   O  O     . THR A 1 108 ? 107.674 140.820 106.946 1.00 60.42 ?  108 THR A O     1 
ATOM   897   C  CB    . THR A 1 108 ? 105.055 141.682 104.959 1.00 60.24 ?  108 THR A CB    1 
ATOM   898   O  OG1   . THR A 1 108 ? 104.876 140.267 104.831 1.00 62.28 ?  108 THR A OG1   1 
ATOM   899   C  CG2   . THR A 1 108 ? 104.537 142.367 103.704 1.00 59.01 ?  108 THR A CG2   1 
ATOM   900   N  N     . ASN A 1 109 ? 106.442 142.624 107.502 1.00 63.53 ?  109 ASN A N     1 
ATOM   901   C  CA    . ASN A 1 109 ? 106.867 142.594 108.898 1.00 62.62 ?  109 ASN A CA    1 
ATOM   902   C  C     . ASN A 1 109 ? 106.526 141.272 109.573 1.00 64.06 ?  109 ASN A C     1 
ATOM   903   O  O     . ASN A 1 109 ? 107.199 140.875 110.531 1.00 65.05 ?  109 ASN A O     1 
ATOM   904   C  CB    . ASN A 1 109 ? 106.236 143.758 109.660 1.00 62.62 ?  109 ASN A CB    1 
ATOM   905   C  CG    . ASN A 1 109 ? 106.997 145.053 109.472 1.00 62.85 ?  109 ASN A CG    1 
ATOM   906   O  OD1   . ASN A 1 109 ? 108.219 145.053 109.337 1.00 64.74 ?  109 ASN A OD1   1 
ATOM   907   N  ND2   . ASN A 1 109 ? 106.275 146.167 109.459 1.00 63.04 ?  109 ASN A ND2   1 
ATOM   908   N  N     . ASP A 1 110 ? 105.496 140.578 109.095 1.00 68.70 ?  110 ASP A N     1 
ATOM   909   C  CA    . ASP A 1 110 ? 105.110 139.283 109.633 1.00 67.94 ?  110 ASP A CA    1 
ATOM   910   C  C     . ASP A 1 110 ? 105.744 138.122 108.877 1.00 68.31 ?  110 ASP A C     1 
ATOM   911   O  O     . ASP A 1 110 ? 105.372 136.968 109.112 1.00 69.86 ?  110 ASP A O     1 
ATOM   912   C  CB    . ASP A 1 110 ? 103.586 139.142 109.628 1.00 67.40 ?  110 ASP A CB    1 
ATOM   913   C  CG    . ASP A 1 110 ? 102.956 139.689 108.364 1.00 68.90 ?  110 ASP A CG    1 
ATOM   914   O  OD1   . ASP A 1 110 ? 103.586 140.539 107.704 1.00 69.20 ?  110 ASP A OD1   1 
ATOM   915   O  OD2   . ASP A 1 110 ? 101.828 139.270 108.032 1.00 70.98 -1 110 ASP A OD2   1 
ATOM   916   N  N     . LYS A 1 111 ? 106.692 138.405 107.979 1.00 66.46 ?  111 LYS A N     1 
ATOM   917   C  CA    . LYS A 1 111 ? 107.360 137.380 107.173 1.00 65.58 ?  111 LYS A CA    1 
ATOM   918   C  C     . LYS A 1 111 ? 106.350 136.553 106.382 1.00 65.91 ?  111 LYS A C     1 
ATOM   919   O  O     . LYS A 1 111 ? 106.488 135.337 106.241 1.00 67.92 ?  111 LYS A O     1 
ATOM   920   C  CB    . LYS A 1 111 ? 108.241 136.472 108.038 1.00 65.10 ?  111 LYS A CB    1 
ATOM   921   C  CG    . LYS A 1 111 ? 109.405 137.165 108.739 1.00 65.13 ?  111 LYS A CG    1 
ATOM   922   C  CD    . LYS A 1 111 ? 109.972 138.315 107.923 1.00 66.65 ?  111 LYS A CD    1 
ATOM   923   C  CE    . LYS A 1 111 ? 109.983 139.605 108.727 1.00 66.83 ?  111 LYS A CE    1 
ATOM   924   N  NZ    . LYS A 1 111 ? 110.479 140.757 107.925 1.00 64.70 1  111 LYS A NZ    1 
ATOM   925   N  N     . LYS A 1 112 ? 105.323 137.220 105.857 1.00 64.63 ?  112 LYS A N     1 
ATOM   926   C  CA    . LYS A 1 112 ? 104.218 136.546 105.186 1.00 66.88 ?  112 LYS A CA    1 
ATOM   927   C  C     . LYS A 1 112 ? 104.314 136.621 103.668 1.00 66.69 ?  112 LYS A C     1 
ATOM   928   O  O     . LYS A 1 112 ? 104.270 135.590 102.993 1.00 68.00 ?  112 LYS A O     1 
ATOM   929   C  CB    . LYS A 1 112 ? 102.885 137.141 105.655 1.00 66.48 ?  112 LYS A CB    1 
ATOM   930   C  CG    . LYS A 1 112 ? 101.672 136.293 105.311 1.00 67.80 ?  112 LYS A CG    1 
ATOM   931   C  CD    . LYS A 1 112 ? 101.656 134.997 106.108 1.00 68.20 ?  112 LYS A CD    1 
ATOM   932   C  CE    . LYS A 1 112 ? 101.812 135.255 107.601 1.00 68.46 ?  112 LYS A CE    1 
ATOM   933   N  NZ    . LYS A 1 112 ? 100.806 136.227 108.111 1.00 66.80 1  112 LYS A NZ    1 
ATOM   934   N  N     . LYS A 1 113 ? 104.444 137.822 103.119 1.00 59.74 ?  113 LYS A N     1 
ATOM   935   C  CA    . LYS A 1 113 ? 104.496 138.038 101.682 1.00 57.63 ?  113 LYS A CA    1 
ATOM   936   C  C     . LYS A 1 113 ? 105.875 138.562 101.287 1.00 57.10 ?  113 LYS A C     1 
ATOM   937   O  O     . LYS A 1 113 ? 106.747 138.791 102.128 1.00 58.08 ?  113 LYS A O     1 
ATOM   938   C  CB    . LYS A 1 113 ? 103.389 139.000 101.247 1.00 58.63 ?  113 LYS A CB    1 
ATOM   939   C  CG    . LYS A 1 113 ? 101.986 138.431 101.379 1.00 58.57 ?  113 LYS A CG    1 
ATOM   940   C  CD    . LYS A 1 113 ? 101.697 137.416 100.287 1.00 61.20 ?  113 LYS A CD    1 
ATOM   941   C  CE    . LYS A 1 113 ? 100.276 136.888 100.382 1.00 59.99 ?  113 LYS A CE    1 
ATOM   942   N  NZ    . LYS A 1 113 ? 100.008 135.841 99.358  1.00 58.80 1  113 LYS A NZ    1 
ATOM   943   N  N     . ILE A 1 114 ? 106.061 138.754 99.985  1.00 53.70 ?  114 ILE A N     1 
ATOM   944   C  CA    . ILE A 1 114 ? 107.339 139.166 99.414  1.00 52.40 ?  114 ILE A CA    1 
ATOM   945   C  C     . ILE A 1 114 ? 107.170 140.561 98.828  1.00 50.13 ?  114 ILE A C     1 
ATOM   946   O  O     . ILE A 1 114 ? 106.281 140.790 97.998  1.00 52.75 ?  114 ILE A O     1 
ATOM   947   C  CB    . ILE A 1 114 ? 107.828 138.174 98.348  1.00 52.98 ?  114 ILE A CB    1 
ATOM   948   C  CG1   . ILE A 1 114 ? 108.346 136.895 99.009  1.00 51.59 ?  114 ILE A CG1   1 
ATOM   949   C  CG2   . ILE A 1 114 ? 108.910 138.798 97.485  1.00 52.71 ?  114 ILE A CG2   1 
ATOM   950   C  CD1   . ILE A 1 114 ? 108.413 135.715 98.072  1.00 51.35 ?  114 ILE A CD1   1 
ATOM   951   N  N     . LEU A 1 115 ? 108.019 141.490 99.260  1.00 49.22 ?  115 LEU A N     1 
ATOM   952   C  CA    . LEU A 1 115 ? 107.977 142.868 98.787  1.00 51.09 ?  115 LEU A CA    1 
ATOM   953   C  C     . LEU A 1 115 ? 108.954 143.140 97.653  1.00 51.90 ?  115 LEU A C     1 
ATOM   954   O  O     . LEU A 1 115 ? 108.623 143.881 96.724  1.00 52.05 ?  115 LEU A O     1 
ATOM   955   C  CB    . LEU A 1 115 ? 108.263 143.834 99.941  1.00 50.85 ?  115 LEU A CB    1 
ATOM   956   C  CG    . LEU A 1 115 ? 107.214 143.875 101.049 1.00 49.79 ?  115 LEU A CG    1 
ATOM   957   C  CD1   . LEU A 1 115 ? 107.842 144.298 102.364 1.00 50.56 ?  115 LEU A CD1   1 
ATOM   958   C  CD2   . LEU A 1 115 ? 106.082 144.806 100.661 1.00 50.74 ?  115 LEU A CD2   1 
ATOM   959   N  N     . GLU A 1 116 ? 110.146 142.556 97.705  1.00 49.12 ?  116 GLU A N     1 
ATOM   960   C  CA    . GLU A 1 116 ? 111.199 142.820 96.735  1.00 45.80 ?  116 GLU A CA    1 
ATOM   961   C  C     . GLU A 1 116 ? 111.390 141.618 95.824  1.00 46.41 ?  116 GLU A C     1 
ATOM   962   O  O     . GLU A 1 116 ? 111.446 140.478 96.295  1.00 50.13 ?  116 GLU A O     1 
ATOM   963   C  CB    . GLU A 1 116 ? 112.519 143.144 97.434  1.00 44.75 ?  116 GLU A CB    1 
ATOM   964   C  CG    . GLU A 1 116 ? 112.816 144.620 97.567  1.00 44.63 ?  116 GLU A CG    1 
ATOM   965   C  CD    . GLU A 1 116 ? 114.060 144.882 98.386  1.00 47.03 ?  116 GLU A CD    1 
ATOM   966   O  OE1   . GLU A 1 116 ? 114.553 143.936 99.033  1.00 46.08 ?  116 GLU A OE1   1 
ATOM   967   O  OE2   . GLU A 1 116 ? 114.547 146.031 98.382  1.00 48.24 -1 116 GLU A OE2   1 
ATOM   968   N  N     . ARG A 1 117 ? 111.487 141.876 94.525  1.00 42.37 ?  117 ARG A N     1 
ATOM   969   C  CA    . ARG A 1 117 ? 111.984 140.889 93.583  1.00 42.21 ?  117 ARG A CA    1 
ATOM   970   C  C     . ARG A 1 117 ? 113.504 141.030 93.503  1.00 43.77 ?  117 ARG A C     1 
ATOM   971   O  O     . ARG A 1 117 ? 114.114 141.811 94.236  1.00 47.51 ?  117 ARG A O     1 
ATOM   972   C  CB    . ARG A 1 117 ? 111.313 141.061 92.221  1.00 42.43 ?  117 ARG A CB    1 
ATOM   973   C  CG    . ARG A 1 117 ? 109.794 141.072 92.266  1.00 44.77 ?  117 ARG A CG    1 
ATOM   974   C  CD    . ARG A 1 117 ? 109.252 139.876 93.034  1.00 49.50 ?  117 ARG A CD    1 
ATOM   975   N  NE    . ARG A 1 117 ? 109.347 138.637 92.272  1.00 47.61 ?  117 ARG A NE    1 
ATOM   976   C  CZ    . ARG A 1 117 ? 108.528 138.296 91.285  1.00 47.19 ?  117 ARG A CZ    1 
ATOM   977   N  NH1   . ARG A 1 117 ? 107.529 139.080 90.914  1.00 48.28 1  117 ARG A NH1   1 
ATOM   978   N  NH2   . ARG A 1 117 ? 108.715 137.139 90.658  1.00 47.65 ?  117 ARG A NH2   1 
ATOM   979   N  N     . TYR A 1 118 ? 114.139 140.263 92.616  1.00 42.19 ?  118 TYR A N     1 
ATOM   980   C  CA    . TYR A 1 118 ? 115.573 140.424 92.411  1.00 36.17 ?  118 TYR A CA    1 
ATOM   981   C  C     . TYR A 1 118 ? 115.887 141.792 91.821  1.00 37.76 ?  118 TYR A C     1 
ATOM   982   O  O     . TYR A 1 118 ? 116.841 142.460 92.241  1.00 40.66 ?  118 TYR A O     1 
ATOM   983   C  CB    . TYR A 1 118 ? 116.097 139.309 91.507  1.00 36.88 ?  118 TYR A CB    1 
ATOM   984   C  CG    . TYR A 1 118 ? 117.596 139.145 91.521  1.00 36.73 ?  118 TYR A CG    1 
ATOM   985   C  CD1   . TYR A 1 118 ? 118.282 138.960 92.713  1.00 36.21 ?  118 TYR A CD1   1 
ATOM   986   C  CD2   . TYR A 1 118 ? 118.326 139.170 90.344  1.00 36.96 ?  118 TYR A CD2   1 
ATOM   987   C  CE1   . TYR A 1 118 ? 119.650 138.807 92.729  1.00 35.71 ?  118 TYR A CE1   1 
ATOM   988   C  CE2   . TYR A 1 118 ? 119.693 139.013 90.349  1.00 31.19 ?  118 TYR A CE2   1 
ATOM   989   C  CZ    . TYR A 1 118 ? 120.352 138.833 91.544  1.00 35.72 ?  118 TYR A CZ    1 
ATOM   990   O  OH    . TYR A 1 118 ? 121.718 138.682 91.552  1.00 45.66 ?  118 TYR A OH    1 
ATOM   991   N  N     . GLU A 1 119 ? 115.077 142.234 90.856  1.00 41.38 ?  119 GLU A N     1 
ATOM   992   C  CA    . GLU A 1 119 ? 115.290 143.536 90.238  1.00 38.57 ?  119 GLU A CA    1 
ATOM   993   C  C     . GLU A 1 119 ? 115.084 144.668 91.236  1.00 40.41 ?  119 GLU A C     1 
ATOM   994   O  O     . GLU A 1 119 ? 115.816 145.661 91.208  1.00 43.54 ?  119 GLU A O     1 
ATOM   995   C  CB    . GLU A 1 119 ? 114.363 143.702 89.036  1.00 40.57 ?  119 GLU A CB    1 
ATOM   996   C  CG    . GLU A 1 119 ? 114.818 142.952 87.801  1.00 41.16 ?  119 GLU A CG    1 
ATOM   997   C  CD    . GLU A 1 119 ? 114.245 141.552 87.719  1.00 43.69 ?  119 GLU A CD    1 
ATOM   998   O  OE1   . GLU A 1 119 ? 113.822 141.015 88.764  1.00 43.92 ?  119 GLU A OE1   1 
ATOM   999   O  OE2   . GLU A 1 119 ? 114.224 140.985 86.607  1.00 44.72 -1 119 GLU A OE2   1 
ATOM   1000  N  N     . ASP A 1 120 ? 114.096 144.540 92.124  1.00 42.16 ?  120 ASP A N     1 
ATOM   1001  C  CA    . ASP A 1 120 ? 113.861 145.582 93.119  1.00 38.20 ?  120 ASP A CA    1 
ATOM   1002  C  C     . ASP A 1 120 ? 115.039 145.704 94.076  1.00 38.64 ?  120 ASP A C     1 
ATOM   1003  O  O     . ASP A 1 120 ? 115.510 146.812 94.361  1.00 45.44 ?  120 ASP A O     1 
ATOM   1004  C  CB    . ASP A 1 120 ? 112.573 145.292 93.891  1.00 42.51 ?  120 ASP A CB    1 
ATOM   1005  C  CG    . ASP A 1 120 ? 111.394 145.042 92.980  1.00 47.73 ?  120 ASP A CG    1 
ATOM   1006  O  OD1   . ASP A 1 120 ? 111.309 145.700 91.922  1.00 46.98 ?  120 ASP A OD1   1 
ATOM   1007  O  OD2   . ASP A 1 120 ? 110.549 144.188 93.318  1.00 51.12 -1 120 ASP A OD2   1 
ATOM   1008  N  N     . ARG A 1 121 ? 115.528 144.571 94.584  1.00 33.43 ?  121 ARG A N     1 
ATOM   1009  C  CA    . ARG A 1 121 ? 116.677 144.593 95.482  1.00 32.95 ?  121 ARG A CA    1 
ATOM   1010  C  C     . ARG A 1 121 ? 117.906 145.160 94.787  1.00 34.25 ?  121 ARG A C     1 
ATOM   1011  O  O     . ARG A 1 121 ? 118.636 145.973 95.367  1.00 41.31 ?  121 ARG A O     1 
ATOM   1012  C  CB    . ARG A 1 121 ? 116.960 143.185 96.005  1.00 34.34 ?  121 ARG A CB    1 
ATOM   1013  C  CG    . ARG A 1 121 ? 118.119 143.101 96.982  1.00 32.95 ?  121 ARG A CG    1 
ATOM   1014  C  CD    . ARG A 1 121 ? 117.642 143.254 98.413  1.00 33.48 ?  121 ARG A CD    1 
ATOM   1015  N  NE    . ARG A 1 121 ? 118.512 144.126 99.192  1.00 38.02 ?  121 ARG A NE    1 
ATOM   1016  C  CZ    . ARG A 1 121 ? 118.238 145.389 99.488  1.00 37.23 ?  121 ARG A CZ    1 
ATOM   1017  N  NH1   . ARG A 1 121 ? 117.124 145.969 99.077  1.00 36.19 1  121 ARG A NH1   1 
ATOM   1018  N  NH2   . ARG A 1 121 ? 119.105 146.087 100.215 1.00 34.72 ?  121 ARG A NH2   1 
ATOM   1019  N  N     . ILE A 1 122 ? 118.145 144.752 93.539  1.00 33.17 ?  122 ILE A N     1 
ATOM   1020  C  CA    . ILE A 1 122 ? 119.308 145.247 92.812  1.00 29.12 ?  122 ILE A CA    1 
ATOM   1021  C  C     . ILE A 1 122 ? 119.195 146.746 92.567  1.00 30.95 ?  122 ILE A C     1 
ATOM   1022  O  O     . ILE A 1 122 ? 120.174 147.484 92.714  1.00 36.66 ?  122 ILE A O     1 
ATOM   1023  C  CB    . ILE A 1 122 ? 119.491 144.459 91.503  1.00 32.31 ?  122 ILE A CB    1 
ATOM   1024  C  CG1   . ILE A 1 122 ? 120.227 143.151 91.787  1.00 27.19 ?  122 ILE A CG1   1 
ATOM   1025  C  CG2   . ILE A 1 122 ? 120.248 145.282 90.470  1.00 33.57 ?  122 ILE A CG2   1 
ATOM   1026  C  CD1   . ILE A 1 122 ? 120.536 142.360 90.559  1.00 33.73 ?  122 ILE A CD1   1 
ATOM   1027  N  N     . SER A 1 123 ? 118.003 147.224 92.199  1.00 34.94 ?  123 SER A N     1 
ATOM   1028  C  CA    . SER A 1 123 ? 117.815 148.652 91.968  1.00 32.04 ?  123 SER A CA    1 
ATOM   1029  C  C     . SER A 1 123 ? 118.021 149.452 93.245  1.00 31.85 ?  123 SER A C     1 
ATOM   1030  O  O     . SER A 1 123 ? 118.619 150.533 93.218  1.00 39.19 ?  123 SER A O     1 
ATOM   1031  C  CB    . SER A 1 123 ? 116.419 148.911 91.403  1.00 34.60 ?  123 SER A CB    1 
ATOM   1032  O  OG    . SER A 1 123 ? 116.064 147.925 90.456  1.00 39.38 ?  123 SER A OG    1 
ATOM   1033  N  N     . ILE A 1 124 ? 117.520 148.946 94.374  1.00 31.75 ?  124 ILE A N     1 
ATOM   1034  C  CA    . ILE A 1 124 ? 117.707 149.652 95.637  1.00 34.84 ?  124 ILE A CA    1 
ATOM   1035  C  C     . ILE A 1 124 ? 119.183 149.695 96.015  1.00 36.09 ?  124 ILE A C     1 
ATOM   1036  O  O     . ILE A 1 124 ? 119.696 150.736 96.443  1.00 39.49 ?  124 ILE A O     1 
ATOM   1037  C  CB    . ILE A 1 124 ? 116.848 149.010 96.739  1.00 38.69 ?  124 ILE A CB    1 
ATOM   1038  C  CG1   . ILE A 1 124 ? 115.367 149.266 96.460  1.00 39.24 ?  124 ILE A CG1   1 
ATOM   1039  C  CG2   . ILE A 1 124 ? 117.230 149.550 98.103  1.00 33.39 ?  124 ILE A CG2   1 
ATOM   1040  C  CD1   . ILE A 1 124 ? 115.054 150.706 96.110  1.00 37.19 ?  124 ILE A CD1   1 
ATOM   1041  N  N     . VAL A 1 125 ? 119.891 148.575 95.851  1.00 32.10 ?  125 VAL A N     1 
ATOM   1042  C  CA    . VAL A 1 125 ? 121.319 148.547 96.155  1.00 29.01 ?  125 VAL A CA    1 
ATOM   1043  C  C     . VAL A 1 125 ? 122.082 149.500 95.240  1.00 28.32 ?  125 VAL A C     1 
ATOM   1044  O  O     . VAL A 1 125 ? 123.017 150.183 95.671  1.00 39.80 ?  125 VAL A O     1 
ATOM   1045  C  CB    . VAL A 1 125 ? 121.854 147.105 96.059  1.00 33.53 ?  125 VAL A CB    1 
ATOM   1046  C  CG1   . VAL A 1 125 ? 123.359 147.082 96.193  1.00 30.75 ?  125 VAL A CG1   1 
ATOM   1047  C  CG2   . VAL A 1 125 ? 121.228 146.240 97.135  1.00 28.67 ?  125 VAL A CG2   1 
ATOM   1048  N  N     . ALA A 1 126 ? 121.680 149.579 93.972  1.00 26.22 ?  126 ALA A N     1 
ATOM   1049  C  CA    . ALA A 1 126 ? 122.359 150.459 93.027  1.00 26.65 ?  126 ALA A CA    1 
ATOM   1050  C  C     . ALA A 1 126 ? 122.115 151.926 93.351  1.00 34.15 ?  126 ALA A C     1 
ATOM   1051  O  O     . ALA A 1 126 ? 123.038 152.745 93.275  1.00 39.43 ?  126 ALA A O     1 
ATOM   1052  C  CB    . ALA A 1 126 ? 121.899 150.148 91.608  1.00 29.39 ?  126 ALA A CB    1 
ATOM   1053  N  N     . LEU A 1 127 ? 120.877 152.280 93.700  1.00 36.11 ?  127 LEU A N     1 
ATOM   1054  C  CA    . LEU A 1 127 ? 120.583 153.654 94.089  1.00 32.17 ?  127 LEU A CA    1 
ATOM   1055  C  C     . LEU A 1 127 ? 121.286 154.022 95.387  1.00 30.19 ?  127 LEU A C     1 
ATOM   1056  O  O     . LEU A 1 127 ? 121.673 155.181 95.574  1.00 35.16 ?  127 LEU A O     1 
ATOM   1057  C  CB    . LEU A 1 127 ? 119.074 153.852 94.219  1.00 33.59 ?  127 LEU A CB    1 
ATOM   1058  C  CG    . LEU A 1 127 ? 118.276 153.794 92.915  1.00 34.25 ?  127 LEU A CG    1 
ATOM   1059  C  CD1   . LEU A 1 127 ? 116.838 153.395 93.185  1.00 36.24 ?  127 LEU A CD1   1 
ATOM   1060  C  CD2   . LEU A 1 127 ? 118.333 155.121 92.183  1.00 34.84 ?  127 LEU A CD2   1 
ATOM   1061  N  N     . PHE A 1 128 ? 121.448 153.058 96.295  1.00 32.75 ?  128 PHE A N     1 
ATOM   1062  C  CA    . PHE A 1 128 ? 122.242 153.292 97.494  1.00 32.86 ?  128 PHE A CA    1 
ATOM   1063  C  C     . PHE A 1 128 ? 123.708 153.532 97.147  1.00 30.93 ?  128 PHE A C     1 
ATOM   1064  O  O     . PHE A 1 128 ? 124.344 154.432 97.706  1.00 38.78 ?  128 PHE A O     1 
ATOM   1065  C  CB    . PHE A 1 128 ? 122.094 152.105 98.445  1.00 30.53 ?  128 PHE A CB    1 
ATOM   1066  C  CG    . PHE A 1 128 ? 122.967 152.184 99.662  1.00 35.69 ?  128 PHE A CG    1 
ATOM   1067  C  CD1   . PHE A 1 128 ? 122.545 152.870 100.786 1.00 37.91 ?  128 PHE A CD1   1 
ATOM   1068  C  CD2   . PHE A 1 128 ? 124.201 151.559 99.688  1.00 33.56 ?  128 PHE A CD2   1 
ATOM   1069  C  CE1   . PHE A 1 128 ? 123.343 152.941 101.909 1.00 38.80 ?  128 PHE A CE1   1 
ATOM   1070  C  CE2   . PHE A 1 128 ? 125.003 151.631 100.804 1.00 33.60 ?  128 PHE A CE2   1 
ATOM   1071  C  CZ    . PHE A 1 128 ? 124.573 152.319 101.917 1.00 35.48 ?  128 PHE A CZ    1 
ATOM   1072  N  N     . PHE A 1 129 ? 124.258 152.735 96.228  1.00 28.02 ?  129 PHE A N     1 
ATOM   1073  C  CA    . PHE A 1 129 ? 125.660 152.884 95.848  1.00 25.55 ?  129 PHE A CA    1 
ATOM   1074  C  C     . PHE A 1 129 ? 125.920 154.217 95.159  1.00 29.30 ?  129 PHE A C     1 
ATOM   1075  O  O     . PHE A 1 129 ? 126.923 154.881 95.439  1.00 33.20 ?  129 PHE A O     1 
ATOM   1076  C  CB    . PHE A 1 129 ? 126.084 151.739 94.929  1.00 26.16 ?  129 PHE A CB    1 
ATOM   1077  C  CG    . PHE A 1 129 ? 126.311 150.439 95.636  1.00 25.05 ?  129 PHE A CG    1 
ATOM   1078  C  CD1   . PHE A 1 129 ? 126.468 150.396 97.007  1.00 27.59 ?  129 PHE A CD1   1 
ATOM   1079  C  CD2   . PHE A 1 129 ? 126.382 149.258 94.919  1.00 26.52 ?  129 PHE A CD2   1 
ATOM   1080  C  CE1   . PHE A 1 129 ? 126.678 149.197 97.653  1.00 24.89 ?  129 PHE A CE1   1 
ATOM   1081  C  CE2   . PHE A 1 129 ? 126.598 148.058 95.559  1.00 26.00 ?  129 PHE A CE2   1 
ATOM   1082  C  CZ    . PHE A 1 129 ? 126.745 148.029 96.928  1.00 27.59 ?  129 PHE A CZ    1 
ATOM   1083  N  N     . ALA A 1 130 ? 125.030 154.620 94.251  1.00 35.43 ?  130 ALA A N     1 
ATOM   1084  C  CA    . ALA A 1 130 ? 125.307 155.777 93.406  1.00 35.20 ?  130 ALA A CA    1 
ATOM   1085  C  C     . ALA A 1 130 ? 125.277 157.083 94.188  1.00 42.34 ?  130 ALA A C     1 
ATOM   1086  O  O     . ALA A 1 130 ? 125.985 158.030 93.829  1.00 47.09 ?  130 ALA A O     1 
ATOM   1087  C  CB    . ALA A 1 130 ? 124.311 155.828 92.253  1.00 34.43 ?  130 ALA A CB    1 
ATOM   1088  N  N     . ASN A 1 131 ? 124.462 157.157 95.242  1.00 42.79 ?  131 ASN A N     1 
ATOM   1089  C  CA    . ASN A 1 131 ? 124.402 158.324 96.123  1.00 43.74 ?  131 ASN A CA    1 
ATOM   1090  C  C     . ASN A 1 131 ? 124.024 159.590 95.350  1.00 43.29 ?  131 ASN A C     1 
ATOM   1091  O  O     . ASN A 1 131 ? 124.705 160.615 95.416  1.00 47.94 ?  131 ASN A O     1 
ATOM   1092  C  CB    . ASN A 1 131 ? 125.725 158.509 96.872  1.00 43.48 ?  131 ASN A CB    1 
ATOM   1093  C  CG    . ASN A 1 131 ? 125.585 159.392 98.094  1.00 48.16 ?  131 ASN A CG    1 
ATOM   1094  O  OD1   . ASN A 1 131 ? 124.636 159.257 98.867  1.00 44.83 ?  131 ASN A OD1   1 
ATOM   1095  N  ND2   . ASN A 1 131 ? 126.533 160.301 98.277  1.00 46.49 ?  131 ASN A ND2   1 
ATOM   1096  N  N     . GLY A 1 132 ? 122.920 159.510 94.610  1.00 41.46 ?  132 GLY A N     1 
ATOM   1097  C  CA    . GLY A 1 132 ? 122.371 160.643 93.902  1.00 41.96 ?  132 GLY A CA    1 
ATOM   1098  C  C     . GLY A 1 132 ? 122.624 160.658 92.408  1.00 44.87 ?  132 GLY A C     1 
ATOM   1099  O  O     . GLY A 1 132 ? 121.958 161.414 91.693  1.00 49.08 ?  132 GLY A O     1 
ATOM   1100  N  N     . ASP A 1 133 ? 123.556 159.847 91.915  1.00 47.04 ?  133 ASP A N     1 
ATOM   1101  C  CA    . ASP A 1 133 ? 123.895 159.825 90.498  1.00 46.05 ?  133 ASP A CA    1 
ATOM   1102  C  C     . ASP A 1 133 ? 122.998 158.827 89.774  1.00 49.14 ?  133 ASP A C     1 
ATOM   1103  O  O     . ASP A 1 133 ? 122.980 157.641 90.114  1.00 49.71 ?  133 ASP A O     1 
ATOM   1104  C  CB    . ASP A 1 133 ? 125.368 159.468 90.304  1.00 48.23 ?  133 ASP A CB    1 
ATOM   1105  C  CG    . ASP A 1 133 ? 125.926 159.979 88.990  1.00 53.27 ?  133 ASP A CG    1 
ATOM   1106  O  OD1   . ASP A 1 133 ? 125.140 160.171 88.038  1.00 52.24 ?  133 ASP A OD1   1 
ATOM   1107  O  OD2   . ASP A 1 133 ? 127.154 160.190 88.909  1.00 52.57 -1 133 ASP A OD2   1 
ATOM   1108  N  N     . THR A 1 134 ? 122.255 159.309 88.777  1.00 48.73 ?  134 THR A N     1 
ATOM   1109  C  CA    . THR A 1 134 ? 121.350 158.428 88.043  1.00 47.99 ?  134 THR A CA    1 
ATOM   1110  C  C     . THR A 1 134 ? 122.112 157.510 87.095  1.00 49.88 ?  134 THR A C     1 
ATOM   1111  O  O     . THR A 1 134 ? 121.826 156.309 87.019  1.00 51.80 ?  134 THR A O     1 
ATOM   1112  C  CB    . THR A 1 134 ? 120.328 159.263 87.275  1.00 52.41 ?  134 THR A CB    1 
ATOM   1113  O  OG1   . THR A 1 134 ? 119.491 159.956 88.207  1.00 53.72 ?  134 THR A OG1   1 
ATOM   1114  C  CG2   . THR A 1 134 ? 119.461 158.374 86.396  1.00 51.31 ?  134 THR A CG2   1 
ATOM   1115  N  N     . GLU A 1 135 ? 123.089 158.057 86.366  1.00 47.24 ?  135 GLU A N     1 
ATOM   1116  C  CA    . GLU A 1 135 ? 123.865 157.243 85.437  1.00 47.75 ?  135 GLU A CA    1 
ATOM   1117  C  C     . GLU A 1 135 ? 124.688 156.196 86.175  1.00 48.60 ?  135 GLU A C     1 
ATOM   1118  O  O     . GLU A 1 135 ? 124.799 155.052 85.720  1.00 51.03 ?  135 GLU A O     1 
ATOM   1119  C  CB    . GLU A 1 135 ? 124.767 158.136 84.588  1.00 49.48 ?  135 GLU A CB    1 
ATOM   1120  C  CG    . GLU A 1 135 ? 124.011 159.141 83.739  1.00 48.79 ?  135 GLU A CG    1 
ATOM   1121  C  CD    . GLU A 1 135 ? 122.900 158.499 82.933  1.00 54.08 ?  135 GLU A CD    1 
ATOM   1122  O  OE1   . GLU A 1 135 ? 123.197 157.596 82.124  1.00 54.31 ?  135 GLU A OE1   1 
ATOM   1123  O  OE2   . GLU A 1 135 ? 121.729 158.896 83.112  1.00 55.23 -1 135 GLU A OE2   1 
ATOM   1124  N  N     . LYS A 1 136 ? 125.276 156.569 87.313  1.00 40.59 ?  136 LYS A N     1 
ATOM   1125  C  CA    . LYS A 1 136 ? 126.012 155.600 88.115  1.00 40.58 ?  136 LYS A CA    1 
ATOM   1126  C  C     . LYS A 1 136 ? 125.083 154.524 88.662  1.00 41.54 ?  136 LYS A C     1 
ATOM   1127  O  O     . LYS A 1 136 ? 125.461 153.350 88.744  1.00 44.71 ?  136 LYS A O     1 
ATOM   1128  C  CB    . LYS A 1 136 ? 126.747 156.312 89.250  1.00 45.00 ?  136 LYS A CB    1 
ATOM   1129  C  CG    . LYS A 1 136 ? 127.904 155.526 89.835  1.00 42.10 ?  136 LYS A CG    1 
ATOM   1130  C  CD    . LYS A 1 136 ? 129.111 155.565 88.919  1.00 43.50 ?  136 LYS A CD    1 
ATOM   1131  C  CE    . LYS A 1 136 ? 130.393 155.282 89.682  1.00 46.23 ?  136 LYS A CE    1 
ATOM   1132  N  NZ    . LYS A 1 136 ? 131.593 155.477 88.825  1.00 47.84 1  136 LYS A NZ    1 
ATOM   1133  N  N     . ALA A 1 137 ? 123.863 154.906 89.045  1.00 39.31 ?  137 ALA A N     1 
ATOM   1134  C  CA    . ALA A 1 137 ? 122.891 153.918 89.503  1.00 34.47 ?  137 ALA A CA    1 
ATOM   1135  C  C     . ALA A 1 137 ? 122.534 152.942 88.391  1.00 36.75 ?  137 ALA A C     1 
ATOM   1136  O  O     . ALA A 1 137 ? 122.409 151.736 88.630  1.00 39.98 ?  137 ALA A O     1 
ATOM   1137  C  CB    . ALA A 1 137 ? 121.640 154.617 90.032  1.00 36.06 ?  137 ALA A CB    1 
ATOM   1138  N  N     . LYS A 1 138 ? 122.366 153.446 87.166  1.00 40.72 ?  138 LYS A N     1 
ATOM   1139  C  CA    . LYS A 1 138 ? 122.106 152.561 86.034  1.00 40.87 ?  138 LYS A CA    1 
ATOM   1140  C  C     . LYS A 1 138 ? 123.295 151.649 85.757  1.00 41.41 ?  138 LYS A C     1 
ATOM   1141  O  O     . LYS A 1 138 ? 123.117 150.476 85.412  1.00 43.37 ?  138 LYS A O     1 
ATOM   1142  C  CB    . LYS A 1 138 ? 121.755 153.383 84.794  1.00 45.21 ?  138 LYS A CB    1 
ATOM   1143  C  CG    . LYS A 1 138 ? 120.341 153.935 84.798  1.00 44.02 ?  138 LYS A CG    1 
ATOM   1144  C  CD    . LYS A 1 138 ? 120.237 155.187 83.949  1.00 43.87 ?  138 LYS A CD    1 
ATOM   1145  C  CE    . LYS A 1 138 ? 119.976 154.843 82.493  1.00 47.11 ?  138 LYS A CE    1 
ATOM   1146  N  NZ    . LYS A 1 138 ? 119.996 156.051 81.626  1.00 48.97 1  138 LYS A NZ    1 
ATOM   1147  N  N     . GLU A 1 139 ? 124.515 152.173 85.895  1.00 40.08 ?  139 GLU A N     1 
ATOM   1148  C  CA    . GLU A 1 139 ? 125.703 151.343 85.720  1.00 36.52 ?  139 GLU A CA    1 
ATOM   1149  C  C     . GLU A 1 139 ? 125.758 150.229 86.760  1.00 34.97 ?  139 GLU A C     1 
ATOM   1150  O  O     . GLU A 1 139 ? 126.080 149.081 86.435  1.00 40.47 ?  139 GLU A O     1 
ATOM   1151  C  CB    . GLU A 1 139 ? 126.961 152.208 85.795  1.00 38.10 ?  139 GLU A CB    1 
ATOM   1152  C  CG    . GLU A 1 139 ? 127.326 152.889 84.489  1.00 41.30 ?  139 GLU A CG    1 
ATOM   1153  C  CD    . GLU A 1 139 ? 128.452 153.890 84.651  1.00 48.31 ?  139 GLU A CD    1 
ATOM   1154  O  OE1   . GLU A 1 139 ? 128.517 154.548 85.710  1.00 45.67 ?  139 GLU A OE1   1 
ATOM   1155  O  OE2   . GLU A 1 139 ? 129.272 154.023 83.719  1.00 48.32 -1 139 GLU A OE2   1 
ATOM   1156  N  N     . TYR A 1 140 ? 125.449 150.550 88.017  1.00 32.51 ?  140 TYR A N     1 
ATOM   1157  C  CA    . TYR A 1 140 ? 125.417 149.530 89.062  1.00 30.56 ?  140 TYR A CA    1 
ATOM   1158  C  C     . TYR A 1 140 ? 124.322 148.504 88.796  1.00 33.75 ?  140 TYR A C     1 
ATOM   1159  O  O     . TYR A 1 140 ? 124.506 147.307 89.045  1.00 34.13 ?  140 TYR A O     1 
ATOM   1160  C  CB    . TYR A 1 140 ? 125.206 150.179 90.427  1.00 32.61 ?  140 TYR A CB    1 
ATOM   1161  C  CG    . TYR A 1 140 ? 126.425 150.839 91.017  1.00 32.42 ?  140 TYR A CG    1 
ATOM   1162  C  CD1   . TYR A 1 140 ? 127.597 150.126 91.226  1.00 34.45 ?  140 TYR A CD1   1 
ATOM   1163  C  CD2   . TYR A 1 140 ? 126.398 152.175 91.383  1.00 33.15 ?  140 TYR A CD2   1 
ATOM   1164  C  CE1   . TYR A 1 140 ? 128.707 150.732 91.774  1.00 34.20 ?  140 TYR A CE1   1 
ATOM   1165  C  CE2   . TYR A 1 140 ? 127.500 152.787 91.927  1.00 35.74 ?  140 TYR A CE2   1 
ATOM   1166  C  CZ    . TYR A 1 140 ? 128.651 152.065 92.121  1.00 30.78 ?  140 TYR A CZ    1 
ATOM   1167  O  OH    . TYR A 1 140 ? 129.745 152.686 92.668  1.00 33.69 ?  140 TYR A OH    1 
ATOM   1168  N  N     . VAL A 1 141 ? 123.167 148.963 88.308  1.00 33.86 ?  141 VAL A N     1 
ATOM   1169  C  CA    . VAL A 1 141 ? 122.086 148.048 87.955  1.00 33.00 ?  141 VAL A CA    1 
ATOM   1170  C  C     . VAL A 1 141 ? 122.537 147.088 86.867  1.00 35.02 ?  141 VAL A C     1 
ATOM   1171  O  O     . VAL A 1 141 ? 122.292 145.881 86.945  1.00 39.42 ?  141 VAL A O     1 
ATOM   1172  C  CB    . VAL A 1 141 ? 120.835 148.835 87.526  1.00 36.37 ?  141 VAL A CB    1 
ATOM   1173  C  CG1   . VAL A 1 141 ? 119.933 147.963 86.692  1.00 36.42 ?  141 VAL A CG1   1 
ATOM   1174  C  CG2   . VAL A 1 141 ? 120.086 149.320 88.736  1.00 35.34 ?  141 VAL A CG2   1 
ATOM   1175  N  N     . ASN A 1 142 ? 123.202 147.606 85.834  1.00 35.68 ?  142 ASN A N     1 
ATOM   1176  C  CA    . ASN A 1 142 ? 123.709 146.739 84.778  1.00 31.75 ?  142 ASN A CA    1 
ATOM   1177  C  C     . ASN A 1 142 ? 124.745 145.765 85.321  1.00 33.91 ?  142 ASN A C     1 
ATOM   1178  O  O     . ASN A 1 142 ? 124.773 144.594 84.931  1.00 40.10 ?  142 ASN A O     1 
ATOM   1179  C  CB    . ASN A 1 142 ? 124.301 147.578 83.649  1.00 32.37 ?  142 ASN A CB    1 
ATOM   1180  C  CG    . ASN A 1 142 ? 123.244 148.126 82.719  1.00 38.00 ?  142 ASN A CG    1 
ATOM   1181  O  OD1   . ASN A 1 142 ? 122.348 147.403 82.286  1.00 37.20 ?  142 ASN A OD1   1 
ATOM   1182  N  ND2   . ASN A 1 142 ? 123.338 149.413 82.410  1.00 36.90 ?  142 ASN A ND2   1 
ATOM   1183  N  N     . LEU A 1 143 ? 125.607 146.236 86.224  1.00 34.59 ?  143 LEU A N     1 
ATOM   1184  C  CA    . LEU A 1 143 ? 126.647 145.381 86.782  1.00 27.88 ?  143 LEU A CA    1 
ATOM   1185  C  C     . LEU A 1 143 ? 126.059 144.227 87.587  1.00 29.22 ?  143 LEU A C     1 
ATOM   1186  O  O     . LEU A 1 143 ? 126.529 143.089 87.486  1.00 29.56 ?  143 LEU A O     1 
ATOM   1187  C  CB    . LEU A 1 143 ? 127.586 146.217 87.650  1.00 27.94 ?  143 LEU A CB    1 
ATOM   1188  C  CG    . LEU A 1 143 ? 129.010 145.701 87.826  1.00 32.99 ?  143 LEU A CG    1 
ATOM   1189  C  CD1   . LEU A 1 143 ? 129.794 145.919 86.550  1.00 33.82 ?  143 LEU A CD1   1 
ATOM   1190  C  CD2   . LEU A 1 143 ? 129.668 146.414 88.985  1.00 28.96 ?  143 LEU A CD2   1 
ATOM   1191  N  N     . MET A 1 144 ? 125.036 144.500 88.398  1.00 33.23 ?  144 MET A N     1 
ATOM   1192  C  CA    . MET A 1 144 ? 124.507 143.456 89.270  1.00 27.56 ?  144 MET A CA    1 
ATOM   1193  C  C     . MET A 1 144 ? 123.468 142.582 88.573  1.00 28.03 ?  144 MET A C     1 
ATOM   1194  O  O     . MET A 1 144 ? 123.373 141.386 88.866  1.00 31.91 ?  144 MET A O     1 
ATOM   1195  C  CB    . MET A 1 144 ? 123.923 144.068 90.541  1.00 28.77 ?  144 MET A CB    1 
ATOM   1196  C  CG    . MET A 1 144 ? 124.921 144.878 91.350  1.00 30.13 ?  144 MET A CG    1 
ATOM   1197  S  SD    . MET A 1 144 ? 124.244 145.426 92.924  1.00 44.79 ?  144 MET A SD    1 
ATOM   1198  C  CE    . MET A 1 144 ? 123.496 146.974 92.444  1.00 33.81 ?  144 MET A CE    1 
ATOM   1199  N  N     . ILE A 1 145 ? 122.669 143.153 87.669  1.00 28.21 ?  145 ILE A N     1 
ATOM   1200  C  CA    . ILE A 1 145 ? 121.682 142.353 86.948  1.00 30.79 ?  145 ILE A CA    1 
ATOM   1201  C  C     . ILE A 1 145 ? 122.368 141.427 85.951  1.00 33.87 ?  145 ILE A C     1 
ATOM   1202  O  O     . ILE A 1 145 ? 121.883 140.319 85.689  1.00 37.32 ?  145 ILE A O     1 
ATOM   1203  C  CB    . ILE A 1 145 ? 120.627 143.257 86.279  1.00 31.53 ?  145 ILE A CB    1 
ATOM   1204  C  CG1   . ILE A 1 145 ? 119.298 142.512 86.149  1.00 30.46 ?  145 ILE A CG1   1 
ATOM   1205  C  CG2   . ILE A 1 145 ? 121.087 143.750 84.914  1.00 30.98 ?  145 ILE A CG2   1 
ATOM   1206  C  CD1   . ILE A 1 145 ? 118.632 142.202 87.467  1.00 28.31 ?  145 ILE A CD1   1 
ATOM   1207  N  N     . ASN A 1 146 ? 123.496 141.852 85.379  1.00 29.04 ?  146 ASN A N     1 
ATOM   1208  C  CA    . ASN A 1 146 ? 124.338 140.936 84.625  1.00 27.56 ?  146 ASN A CA    1 
ATOM   1209  C  C     . ASN A 1 146 ? 125.085 139.978 85.538  1.00 29.54 ?  146 ASN A C     1 
ATOM   1210  O  O     . ASN A 1 146 ? 125.725 139.047 85.042  1.00 36.63 ?  146 ASN A O     1 
ATOM   1211  C  CB    . ASN A 1 146 ? 125.338 141.708 83.764  1.00 29.11 ?  146 ASN A CB    1 
ATOM   1212  C  CG    . ASN A 1 146 ? 124.664 142.553 82.704  1.00 33.00 ?  146 ASN A CG    1 
ATOM   1213  O  OD1   . ASN A 1 146 ? 123.495 142.349 82.383  1.00 34.73 ?  146 ASN A OD1   1 
ATOM   1214  N  ND2   . ASN A 1 146 ? 125.401 143.508 82.153  1.00 35.28 ?  146 ASN A ND2   1 
ATOM   1215  N  N     . GLN A 1 147 ? 125.014 140.200 86.851  1.00 28.22 ?  147 GLN A N     1 
ATOM   1216  C  CA    . GLN A 1 147 ? 125.676 139.370 87.851  1.00 24.26 ?  147 GLN A CA    1 
ATOM   1217  C  C     . GLN A 1 147 ? 127.182 139.333 87.640  1.00 27.66 ?  147 GLN A C     1 
ATOM   1218  O  O     . GLN A 1 147 ? 127.828 138.318 87.887  1.00 34.10 ?  147 GLN A O     1 
ATOM   1219  C  CB    . GLN A 1 147 ? 125.087 137.957 87.876  1.00 24.18 ?  147 GLN A CB    1 
ATOM   1220  C  CG    . GLN A 1 147 ? 123.647 137.916 88.358  1.00 23.63 ?  147 GLN A CG    1 
ATOM   1221  C  CD    . GLN A 1 147 ? 123.206 136.534 88.775  1.00 27.67 ?  147 GLN A CD    1 
ATOM   1222  O  OE1   . GLN A 1 147 ? 122.554 136.362 89.804  1.00 31.18 ?  147 GLN A OE1   1 
ATOM   1223  N  NE2   . GLN A 1 147 ? 123.550 135.537 87.972  1.00 35.38 ?  147 GLN A NE2   1 
ATOM   1224  N  N     . GLU A 1 148 ? 127.749 140.443 87.161  1.00 26.16 ?  148 GLU A N     1 
ATOM   1225  C  CA    . GLU A 1 148 ? 129.197 140.569 87.066  1.00 22.83 ?  148 GLU A CA    1 
ATOM   1226  C  C     . GLU A 1 148 ? 129.827 140.860 88.420  1.00 26.73 ?  148 GLU A C     1 
ATOM   1227  O  O     . GLU A 1 148 ? 130.947 140.412 88.690  1.00 28.77 ?  148 GLU A O     1 
ATOM   1228  C  CB    . GLU A 1 148 ? 129.562 141.668 86.071  1.00 21.54 ?  148 GLU A CB    1 
ATOM   1229  C  CG    . GLU A 1 148 ? 129.033 141.431 84.672  1.00 25.93 ?  148 GLU A CG    1 
ATOM   1230  C  CD    . GLU A 1 148 ? 129.185 142.643 83.780  1.00 32.88 ?  148 GLU A CD    1 
ATOM   1231  O  OE1   . GLU A 1 148 ? 128.262 143.482 83.751  1.00 33.79 ?  148 GLU A OE1   1 
ATOM   1232  O  OE2   . GLU A 1 148 ? 130.232 142.760 83.110  1.00 36.84 -1 148 GLU A OE2   1 
ATOM   1233  N  N     . TYR A 1 149 ? 129.132 141.605 89.273  1.00 24.71 ?  149 TYR A N     1 
ATOM   1234  C  CA    . TYR A 1 149 ? 129.596 141.916 90.616  1.00 19.22 ?  149 TYR A CA    1 
ATOM   1235  C  C     . TYR A 1 149 ? 128.477 141.643 91.605  1.00 22.08 ?  149 TYR A C     1 
ATOM   1236  O  O     . TYR A 1 149 ? 127.311 141.942 91.335  1.00 27.63 ?  149 TYR A O     1 
ATOM   1237  C  CB    . TYR A 1 149 ? 130.051 143.374 90.724  1.00 19.77 ?  149 TYR A CB    1 
ATOM   1238  C  CG    . TYR A 1 149 ? 130.254 143.859 92.141  1.00 24.10 ?  149 TYR A CG    1 
ATOM   1239  C  CD1   . TYR A 1 149 ? 131.261 143.335 92.938  1.00 16.11 ?  149 TYR A CD1   1 
ATOM   1240  C  CD2   . TYR A 1 149 ? 129.438 144.842 92.679  1.00 21.98 ?  149 TYR A CD2   1 
ATOM   1241  C  CE1   . TYR A 1 149 ? 131.449 143.779 94.230  1.00 16.16 ?  149 TYR A CE1   1 
ATOM   1242  C  CE2   . TYR A 1 149 ? 129.616 145.289 93.969  1.00 21.75 ?  149 TYR A CE2   1 
ATOM   1243  C  CZ    . TYR A 1 149 ? 130.624 144.756 94.740  1.00 18.88 ?  149 TYR A CZ    1 
ATOM   1244  O  OH    . TYR A 1 149 ? 130.805 145.200 96.027  1.00 21.26 ?  149 TYR A OH    1 
ATOM   1245  N  N     . GLN A 1 150 ? 128.835 141.069 92.744  1.00 18.57 ?  150 GLN A N     1 
ATOM   1246  C  CA    . GLN A 1 150 ? 127.874 140.768 93.801  1.00 14.00 ?  150 GLN A CA    1 
ATOM   1247  C  C     . GLN A 1 150 ? 128.329 141.395 95.107  1.00 16.18 ?  150 GLN A C     1 
ATOM   1248  O  O     . GLN A 1 150 ? 129.371 140.988 95.656  1.00 23.41 ?  150 GLN A O     1 
ATOM   1249  C  CB    . GLN A 1 150 ? 127.712 139.257 93.962  1.00 19.28 ?  150 GLN A CB    1 
ATOM   1250  C  CG    . GLN A 1 150 ? 126.964 138.825 95.209  1.00 21.38 ?  150 GLN A CG    1 
ATOM   1251  C  CD    . GLN A 1 150 ? 125.534 139.317 95.239  1.00 16.86 ?  150 GLN A CD    1 
ATOM   1252  O  OE1   . GLN A 1 150 ? 124.704 138.897 94.435  1.00 29.61 ?  150 GLN A OE1   1 
ATOM   1253  N  NE2   . GLN A 1 150 ? 125.236 140.209 96.172  1.00 14.13 ?  150 GLN A NE2   1 
ATOM   1254  N  N     . PRO A 1 151 ? 127.610 142.383 95.635  1.00 25.42 ?  151 PRO A N     1 
ATOM   1255  C  CA    . PRO A 1 151 ? 127.928 142.888 96.973  1.00 16.72 ?  151 PRO A CA    1 
ATOM   1256  C  C     . PRO A 1 151 ? 127.757 141.794 98.016  1.00 18.06 ?  151 PRO A C     1 
ATOM   1257  O  O     . PRO A 1 151 ? 126.961 140.869 97.853  1.00 24.62 ?  151 PRO A O     1 
ATOM   1258  C  CB    . PRO A 1 151 ? 126.919 144.022 97.177  1.00 15.05 ?  151 PRO A CB    1 
ATOM   1259  C  CG    . PRO A 1 151 ? 126.485 144.403 95.802  1.00 20.42 ?  151 PRO A CG    1 
ATOM   1260  C  CD    . PRO A 1 151 ? 126.528 143.148 94.995  1.00 22.10 ?  151 PRO A CD    1 
ATOM   1261  N  N     . SER A 1 152 ? 128.532 141.904 99.091  1.00 20.26 ?  152 SER A N     1 
ATOM   1262  C  CA    . SER A 1 152 ? 128.513 140.891 100.134 1.00 16.72 ?  152 SER A CA    1 
ATOM   1263  C  C     . SER A 1 152 ? 127.123 140.769 100.752 1.00 23.77 ?  152 SER A C     1 
ATOM   1264  O  O     . SER A 1 152 ? 126.251 141.621 100.568 1.00 26.90 ?  152 SER A O     1 
ATOM   1265  C  CB    . SER A 1 152 ? 129.537 141.223 101.217 1.00 25.81 ?  152 SER A CB    1 
ATOM   1266  O  OG    . SER A 1 152 ? 129.138 142.358 101.961 1.00 28.95 ?  152 SER A OG    1 
ATOM   1267  N  N     . THR A 1 153 ? 126.925 139.678 101.490 1.00 30.12 ?  153 THR A N     1 
ATOM   1268  C  CA    . THR A 1 153 ? 125.647 139.431 102.157 1.00 23.96 ?  153 THR A CA    1 
ATOM   1269  C  C     . THR A 1 153 ? 125.186 140.591 103.031 1.00 30.26 ?  153 THR A C     1 
ATOM   1270  O  O     . THR A 1 153 ? 124.007 140.967 102.936 1.00 27.34 ?  153 THR A O     1 
ATOM   1271  C  CB    . THR A 1 153 ? 125.741 138.126 102.962 1.00 23.09 ?  153 THR A CB    1 
ATOM   1272  O  OG1   . THR A 1 153 ? 125.780 137.011 102.064 1.00 35.60 ?  153 THR A OG1   1 
ATOM   1273  C  CG2   . THR A 1 153 ? 124.552 137.974 103.897 1.00 24.13 ?  153 THR A CG2   1 
ATOM   1274  N  N     . PRO A 1 154 ? 126.027 141.207 103.874 1.00 29.45 ?  154 PRO A N     1 
ATOM   1275  C  CA    . PRO A 1 154 ? 125.542 142.376 104.632 1.00 21.01 ?  154 PRO A CA    1 
ATOM   1276  C  C     . PRO A 1 154 ? 125.100 143.527 103.744 1.00 22.76 ?  154 PRO A C     1 
ATOM   1277  O  O     . PRO A 1 154 ? 124.009 144.076 103.940 1.00 30.56 ?  154 PRO A O     1 
ATOM   1278  C  CB    . PRO A 1 154 ? 126.750 142.752 105.498 1.00 23.98 ?  154 PRO A CB    1 
ATOM   1279  C  CG    . PRO A 1 154 ? 127.557 141.527 105.576 1.00 21.87 ?  154 PRO A CG    1 
ATOM   1280  C  CD    . PRO A 1 154 ? 127.400 140.848 104.267 1.00 22.33 ?  154 PRO A CD    1 
ATOM   1281  N  N     . THR A 1 155 ? 125.920 143.903 102.762 1.00 22.52 ?  155 THR A N     1 
ATOM   1282  C  CA    . THR A 1 155 ? 125.570 145.020 101.891 1.00 22.76 ?  155 THR A CA    1 
ATOM   1283  C  C     . THR A 1 155 ? 124.351 144.693 101.037 1.00 25.20 ?  155 THR A C     1 
ATOM   1284  O  O     . THR A 1 155 ? 123.395 145.472 100.984 1.00 25.43 ?  155 THR A O     1 
ATOM   1285  C  CB    . THR A 1 155 ? 126.760 145.390 101.007 1.00 21.27 ?  155 THR A CB    1 
ATOM   1286  O  OG1   . THR A 1 155 ? 127.889 145.703 101.829 1.00 27.97 ?  155 THR A OG1   1 
ATOM   1287  C  CG2   . THR A 1 155 ? 126.426 146.591 100.145 1.00 16.40 ?  155 THR A CG2   1 
ATOM   1288  N  N     . PHE A 1 156 ? 124.363 143.537 100.372 1.00 27.54 ?  156 PHE A N     1 
ATOM   1289  C  CA    . PHE A 1 156 ? 123.247 143.172 99.505  1.00 25.07 ?  156 PHE A CA    1 
ATOM   1290  C  C     . PHE A 1 156 ? 121.954 143.017 100.296 1.00 27.98 ?  156 PHE A C     1 
ATOM   1291  O  O     . PHE A 1 156 ? 120.867 143.312 99.790  1.00 29.53 ?  156 PHE A O     1 
ATOM   1292  C  CB    . PHE A 1 156 ? 123.572 141.881 98.753  1.00 25.40 ?  156 PHE A CB    1 
ATOM   1293  C  CG    . PHE A 1 156 ? 122.692 141.634 97.564  1.00 27.47 ?  156 PHE A CG    1 
ATOM   1294  C  CD1   . PHE A 1 156 ? 122.598 142.570 96.549  1.00 24.32 ?  156 PHE A CD1   1 
ATOM   1295  C  CD2   . PHE A 1 156 ? 121.961 140.464 97.459  1.00 26.19 ?  156 PHE A CD2   1 
ATOM   1296  C  CE1   . PHE A 1 156 ? 121.790 142.344 95.453  1.00 28.99 ?  156 PHE A CE1   1 
ATOM   1297  C  CE2   . PHE A 1 156 ? 121.152 140.232 96.367  1.00 24.92 ?  156 PHE A CE2   1 
ATOM   1298  C  CZ    . PHE A 1 156 ? 121.068 141.174 95.363  1.00 29.97 ?  156 PHE A CZ    1 
ATOM   1299  N  N     . LEU A 1 157 ? 122.055 142.556 101.542 1.00 31.66 ?  157 LEU A N     1 
ATOM   1300  C  CA    . LEU A 1 157 ? 120.874 142.337 102.367 1.00 28.13 ?  157 LEU A CA    1 
ATOM   1301  C  C     . LEU A 1 157 ? 120.339 143.623 102.983 1.00 29.68 ?  157 LEU A C     1 
ATOM   1302  O  O     . LEU A 1 157 ? 119.125 143.757 103.154 1.00 37.88 ?  157 LEU A O     1 
ATOM   1303  C  CB    . LEU A 1 157 ? 121.197 141.322 103.466 1.00 31.34 ?  157 LEU A CB    1 
ATOM   1304  C  CG    . LEU A 1 157 ? 120.101 140.995 104.480 1.00 31.00 ?  157 LEU A CG    1 
ATOM   1305  C  CD1   . LEU A 1 157 ? 118.896 140.396 103.788 1.00 29.27 ?  157 LEU A CD1   1 
ATOM   1306  C  CD2   . LEU A 1 157 ? 120.628 140.054 105.548 1.00 28.33 ?  157 LEU A CD2   1 
ATOM   1307  N  N     . ASN A 1 158 ? 121.208 144.574 103.317 1.00 32.61 ?  158 ASN A N     1 
ATOM   1308  C  CA    . ASN A 1 158 ? 120.810 145.718 104.123 1.00 26.65 ?  158 ASN A CA    1 
ATOM   1309  C  C     . ASN A 1 158 ? 120.888 147.053 103.393 1.00 31.48 ?  158 ASN A C     1 
ATOM   1310  O  O     . ASN A 1 158 ? 120.501 148.072 103.970 1.00 38.42 ?  158 ASN A O     1 
ATOM   1311  C  CB    . ASN A 1 158 ? 121.666 145.779 105.392 1.00 29.21 ?  158 ASN A CB    1 
ATOM   1312  C  CG    . ASN A 1 158 ? 121.639 144.482 106.175 1.00 36.03 ?  158 ASN A CG    1 
ATOM   1313  O  OD1   . ASN A 1 158 ? 120.600 143.836 106.291 1.00 38.85 ?  158 ASN A OD1   1 
ATOM   1314  N  ND2   . ASN A 1 158 ? 122.788 144.093 106.712 1.00 32.53 ?  158 ASN A ND2   1 
ATOM   1315  N  N     . ALA A 1 159 ? 121.370 147.085 102.151 1.00 33.82 ?  159 ALA A N     1 
ATOM   1316  C  CA    . ALA A 1 159 ? 121.506 148.356 101.448 1.00 29.94 ?  159 ALA A CA    1 
ATOM   1317  C  C     . ALA A 1 159 ? 120.148 149.006 101.217 1.00 36.52 ?  159 ALA A C     1 
ATOM   1318  O  O     . ALA A 1 159 ? 119.320 148.482 100.466 1.00 42.82 ?  159 ALA A O     1 
ATOM   1319  C  CB    . ALA A 1 159 ? 122.228 148.170 100.114 1.00 34.55 ?  159 ALA A CB    1 
ATOM   1320  N  N     . GLY A 1 160 ? 119.915 150.147 101.860 1.00 43.17 ?  160 GLY A N     1 
ATOM   1321  C  CA    . GLY A 1 160 ? 118.679 150.879 101.695 1.00 40.60 ?  160 GLY A CA    1 
ATOM   1322  C  C     . GLY A 1 160 ? 117.543 150.471 102.603 1.00 44.10 ?  160 GLY A C     1 
ATOM   1323  O  O     . GLY A 1 160 ? 116.426 150.968 102.424 1.00 45.10 ?  160 GLY A O     1 
ATOM   1324  N  N     . ARG A 1 161 ? 117.783 149.587 103.566 1.00 44.10 ?  161 ARG A N     1 
ATOM   1325  C  CA    . ARG A 1 161 ? 116.758 149.154 104.504 1.00 43.77 ?  161 ARG A CA    1 
ATOM   1326  C  C     . ARG A 1 161 ? 116.878 149.933 105.805 1.00 45.82 ?  161 ARG A C     1 
ATOM   1327  O  O     . ARG A 1 161 ? 117.986 150.231 106.262 1.00 48.53 ?  161 ARG A O     1 
ATOM   1328  C  CB    . ARG A 1 161 ? 116.865 147.653 104.775 1.00 41.51 ?  161 ARG A CB    1 
ATOM   1329  C  CG    . ARG A 1 161 ? 116.601 146.793 103.553 1.00 42.22 ?  161 ARG A CG    1 
ATOM   1330  C  CD    . ARG A 1 161 ? 116.363 145.342 103.927 1.00 41.57 ?  161 ARG A CD    1 
ATOM   1331  N  NE    . ARG A 1 161 ? 116.371 144.478 102.753 1.00 45.49 ?  161 ARG A NE    1 
ATOM   1332  C  CZ    . ARG A 1 161 ? 116.238 143.159 102.789 1.00 45.46 ?  161 ARG A CZ    1 
ATOM   1333  N  NH1   . ARG A 1 161 ? 116.078 142.511 103.932 1.00 43.98 1  161 ARG A NH1   1 
ATOM   1334  N  NH2   . ARG A 1 161 ? 116.271 142.473 101.651 1.00 42.72 ?  161 ARG A NH2   1 
ATOM   1335  N  N     . LYS A 1 162 ? 115.730 150.269 106.398 1.00 53.82 ?  162 LYS A N     1 
ATOM   1336  C  CA    . LYS A 1 162 ? 115.732 151.067 107.620 1.00 52.61 ?  162 LYS A CA    1 
ATOM   1337  C  C     . LYS A 1 162 ? 116.195 150.244 108.817 1.00 54.80 ?  162 LYS A C     1 
ATOM   1338  O  O     . LYS A 1 162 ? 117.218 150.553 109.438 1.00 55.62 ?  162 LYS A O     1 
ATOM   1339  C  CB    . LYS A 1 162 ? 114.338 151.641 107.873 1.00 52.45 ?  162 LYS A CB    1 
ATOM   1340  C  CG    . LYS A 1 162 ? 114.337 153.071 108.383 1.00 55.20 ?  162 LYS A CG    1 
ATOM   1341  C  CD    . LYS A 1 162 ? 112.959 153.699 108.266 1.00 55.29 ?  162 LYS A CD    1 
ATOM   1342  C  CE    . LYS A 1 162 ? 113.040 155.216 108.264 1.00 54.69 ?  162 LYS A CE    1 
ATOM   1343  N  NZ    . LYS A 1 162 ? 114.256 155.706 108.970 1.00 55.20 1  162 LYS A NZ    1 
ATOM   1344  N  N     . ARG A 1 163 ? 115.453 149.192 109.152 1.00 57.23 ?  163 ARG A N     1 
ATOM   1345  C  CA    . ARG A 1 163 ? 115.795 148.330 110.282 1.00 57.25 ?  163 ARG A CA    1 
ATOM   1346  C  C     . ARG A 1 163 ? 116.793 147.271 109.819 1.00 58.83 ?  163 ARG A C     1 
ATOM   1347  O  O     . ARG A 1 163 ? 116.459 146.118 109.544 1.00 57.95 ?  163 ARG A O     1 
ATOM   1348  C  CB    . ARG A 1 163 ? 114.533 147.710 110.874 1.00 60.18 ?  163 ARG A CB    1 
ATOM   1349  C  CG    . ARG A 1 163 ? 113.567 148.734 111.450 1.00 58.41 ?  163 ARG A CG    1 
ATOM   1350  C  CD    . ARG A 1 163 ? 112.211 148.117 111.738 1.00 58.40 ?  163 ARG A CD    1 
ATOM   1351  N  NE    . ARG A 1 163 ? 111.546 147.686 110.516 1.00 60.59 ?  163 ARG A NE    1 
ATOM   1352  C  CZ    . ARG A 1 163 ? 110.433 146.967 110.482 1.00 62.32 ?  163 ARG A CZ    1 
ATOM   1353  N  NH1   . ARG A 1 163 ? 109.822 146.588 111.592 1.00 61.42 1  163 ARG A NH1   1 
ATOM   1354  N  NH2   . ARG A 1 163 ? 109.919 146.621 109.305 1.00 59.59 ?  163 ARG A NH2   1 
ATOM   1355  N  N     . ARG A 1 164 ? 118.046 147.702 109.739 1.00 53.64 ?  164 ARG A N     1 
ATOM   1356  C  CA    . ARG A 1 164 ? 119.119 146.923 109.149 1.00 50.73 ?  164 ARG A CA    1 
ATOM   1357  C  C     . ARG A 1 164 ? 120.311 146.854 110.092 1.00 51.26 ?  164 ARG A C     1 
ATOM   1358  O  O     . ARG A 1 164 ? 120.476 147.686 110.988 1.00 52.65 ?  164 ARG A O     1 
ATOM   1359  C  CB    . ARG A 1 164 ? 119.568 147.531 107.815 1.00 49.66 ?  164 ARG A CB    1 
ATOM   1360  C  CG    . ARG A 1 164 ? 120.332 148.840 107.976 1.00 46.69 ?  164 ARG A CG    1 
ATOM   1361  C  CD    . ARG A 1 164 ? 121.227 149.109 106.784 1.00 49.28 ?  164 ARG A CD    1 
ATOM   1362  N  NE    . ARG A 1 164 ? 122.030 150.316 106.943 1.00 50.57 ?  164 ARG A NE    1 
ATOM   1363  C  CZ    . ARG A 1 164 ? 122.255 151.194 105.976 1.00 51.84 ?  164 ARG A CZ    1 
ATOM   1364  N  NH1   . ARG A 1 164 ? 121.739 151.039 104.767 1.00 47.62 1  164 ARG A NH1   1 
ATOM   1365  N  NH2   . ARG A 1 164 ? 123.017 152.255 106.227 1.00 50.81 ?  164 ARG A NH2   1 
ATOM   1366  N  N     . GLY A 1 165 ? 121.142 145.839 109.878 1.00 45.41 ?  165 GLY A N     1 
ATOM   1367  C  CA    . GLY A 1 165 ? 122.448 145.781 110.493 1.00 42.70 ?  165 GLY A CA    1 
ATOM   1368  C  C     . GLY A 1 165 ? 123.456 146.582 109.692 1.00 47.81 ?  165 GLY A C     1 
ATOM   1369  O  O     . GLY A 1 165 ? 123.123 147.309 108.754 1.00 44.98 ?  165 GLY A O     1 
ATOM   1370  N  N     . GLU A 1 166 ? 124.719 146.442 110.076 1.00 45.86 ?  166 GLU A N     1 
ATOM   1371  C  CA    . GLU A 1 166 ? 125.772 147.137 109.357 1.00 39.66 ?  166 GLU A CA    1 
ATOM   1372  C  C     . GLU A 1 166 ? 126.061 146.444 108.029 1.00 37.91 ?  166 GLU A C     1 
ATOM   1373  O  O     . GLU A 1 166 ? 125.768 145.261 107.835 1.00 38.58 ?  166 GLU A O     1 
ATOM   1374  C  CB    . GLU A 1 166 ? 127.045 147.212 110.200 1.00 37.81 ?  166 GLU A CB    1 
ATOM   1375  C  CG    . GLU A 1 166 ? 126.992 148.252 111.307 1.00 41.94 ?  166 GLU A CG    1 
ATOM   1376  C  CD    . GLU A 1 166 ? 126.772 149.661 110.786 1.00 47.92 ?  166 GLU A CD    1 
ATOM   1377  O  OE1   . GLU A 1 166 ? 127.204 149.959 109.653 1.00 46.33 ?  166 GLU A OE1   1 
ATOM   1378  O  OE2   . GLU A 1 166 ? 126.165 150.473 111.515 1.00 45.41 -1 166 GLU A OE2   1 
ATOM   1379  N  N     . LEU A 1 167 ? 126.642 147.206 107.104 1.00 33.25 ?  167 LEU A N     1 
ATOM   1380  C  CA    . LEU A 1 167 ? 127.047 146.661 105.815 1.00 25.75 ?  167 LEU A CA    1 
ATOM   1381  C  C     . LEU A 1 167 ? 128.384 145.940 105.880 1.00 30.06 ?  167 LEU A C     1 
ATOM   1382  O  O     . LEU A 1 167 ? 128.779 145.310 104.894 1.00 32.58 ?  167 LEU A O     1 
ATOM   1383  C  CB    . LEU A 1 167 ? 127.114 147.775 104.769 1.00 27.51 ?  167 LEU A CB    1 
ATOM   1384  C  CG    . LEU A 1 167 ? 125.828 148.542 104.458 1.00 28.18 ?  167 LEU A CG    1 
ATOM   1385  C  CD1   . LEU A 1 167 ? 125.921 149.174 103.087 1.00 31.34 ?  167 LEU A CD1   1 
ATOM   1386  C  CD2   . LEU A 1 167 ? 124.616 147.638 104.537 1.00 28.89 ?  167 LEU A CD2   1 
ATOM   1387  N  N     . VAL A 1 168 ? 129.084 146.021 107.006 1.00 33.17 ?  168 VAL A N     1 
ATOM   1388  C  CA    . VAL A 1 168 ? 130.335 145.310 107.229 1.00 26.44 ?  168 VAL A CA    1 
ATOM   1389  C  C     . VAL A 1 168 ? 130.093 144.248 108.291 1.00 30.61 ?  168 VAL A C     1 
ATOM   1390  O  O     . VAL A 1 168 ? 129.454 144.517 109.315 1.00 36.41 ?  168 VAL A O     1 
ATOM   1391  C  CB    . VAL A 1 168 ? 131.461 146.272 107.657 1.00 26.26 ?  168 VAL A CB    1 
ATOM   1392  C  CG1   . VAL A 1 168 ? 132.767 145.522 107.834 1.00 29.07 ?  168 VAL A CG1   1 
ATOM   1393  C  CG2   . VAL A 1 168 ? 131.617 147.387 106.639 1.00 31.34 ?  168 VAL A CG2   1 
ATOM   1394  N  N     . SER A 1 169 ? 130.596 143.041 108.048 1.00 29.13 ?  169 SER A N     1 
ATOM   1395  C  CA    . SER A 1 169 ? 130.416 141.940 108.981 1.00 30.02 ?  169 SER A CA    1 
ATOM   1396  C  C     . SER A 1 169 ? 131.720 141.328 109.468 1.00 25.74 ?  169 SER A C     1 
ATOM   1397  O  O     . SER A 1 169 ? 131.680 140.425 110.310 1.00 31.17 ?  169 SER A O     1 
ATOM   1398  C  CB    . SER A 1 169 ? 129.547 140.841 108.356 1.00 33.72 ?  169 SER A CB    1 
ATOM   1399  O  OG    . SER A 1 169 ? 128.181 141.034 108.681 1.00 37.71 ?  169 SER A OG    1 
ATOM   1400  N  N     . CYS A 1 170 ? 132.866 141.776 108.971 1.00 28.39 ?  170 CYS A N     1 
ATOM   1401  C  CA    . CYS A 1 170 ? 134.156 141.291 109.438 1.00 26.92 ?  170 CYS A CA    1 
ATOM   1402  C  C     . CYS A 1 170 ? 134.844 142.407 110.210 1.00 25.20 ?  170 CYS A C     1 
ATOM   1403  O  O     . CYS A 1 170 ? 135.030 143.510 109.685 1.00 27.42 ?  170 CYS A O     1 
ATOM   1404  C  CB    . CYS A 1 170 ? 135.022 140.798 108.274 1.00 33.70 ?  170 CYS A CB    1 
ATOM   1405  S  SG    . CYS A 1 170 ? 135.583 142.051 107.094 1.00 51.33 ?  170 CYS A SG    1 
ATOM   1406  N  N     . PHE A 1 171 ? 135.190 142.128 111.463 1.00 22.44 ?  171 PHE A N     1 
ATOM   1407  C  CA    . PHE A 1 171 ? 135.897 143.066 112.318 1.00 16.13 ?  171 PHE A CA    1 
ATOM   1408  C  C     . PHE A 1 171 ? 137.056 142.351 112.992 1.00 16.35 ?  171 PHE A C     1 
ATOM   1409  O  O     . PHE A 1 171 ? 136.939 141.183 113.372 1.00 27.33 ?  171 PHE A O     1 
ATOM   1410  C  CB    . PHE A 1 171 ? 134.971 143.677 113.375 1.00 17.63 ?  171 PHE A CB    1 
ATOM   1411  C  CG    . PHE A 1 171 ? 133.746 144.324 112.803 1.00 17.41 ?  171 PHE A CG    1 
ATOM   1412  C  CD1   . PHE A 1 171 ? 133.804 145.603 112.281 1.00 16.60 ?  171 PHE A CD1   1 
ATOM   1413  C  CD2   . PHE A 1 171 ? 132.535 143.654 112.789 1.00 16.10 ?  171 PHE A CD2   1 
ATOM   1414  C  CE1   . PHE A 1 171 ? 132.682 146.200 111.754 1.00 15.99 ?  171 PHE A CE1   1 
ATOM   1415  C  CE2   . PHE A 1 171 ? 131.411 144.248 112.263 1.00 16.69 ?  171 PHE A CE2   1 
ATOM   1416  C  CZ    . PHE A 1 171 ? 131.483 145.521 111.746 1.00 14.78 ?  171 PHE A CZ    1 
ATOM   1417  N  N     . LEU A 1 172 ? 138.173 143.057 113.130 1.00 17.80 ?  172 LEU A N     1 
ATOM   1418  C  CA    . LEU A 1 172 ? 139.374 142.526 113.757 1.00 7.46  ?  172 LEU A CA    1 
ATOM   1419  C  C     . LEU A 1 172 ? 139.775 143.463 114.884 1.00 13.17 ?  172 LEU A C     1 
ATOM   1420  O  O     . LEU A 1 172 ? 139.949 144.663 114.660 1.00 17.99 ?  172 LEU A O     1 
ATOM   1421  C  CB    . LEU A 1 172 ? 140.519 142.387 112.747 1.00 12.46 ?  172 LEU A CB    1 
ATOM   1422  C  CG    . LEU A 1 172 ? 140.421 141.316 111.659 1.00 7.26  ?  172 LEU A CG    1 
ATOM   1423  C  CD1   . LEU A 1 172 ? 139.527 141.775 110.520 1.00 11.37 ?  172 LEU A CD1   1 
ATOM   1424  C  CD2   . LEU A 1 172 ? 141.802 140.973 111.142 1.00 11.04 ?  172 LEU A CD2   1 
ATOM   1425  N  N     . LEU A 1 173 ? 139.923 142.917 116.087 1.00 22.03 ?  173 LEU A N     1 
ATOM   1426  C  CA    . LEU A 1 173 ? 140.213 143.708 117.274 1.00 9.24  ?  173 LEU A CA    1 
ATOM   1427  C  C     . LEU A 1 173 ? 141.548 143.295 117.874 1.00 16.79 ?  173 LEU A C     1 
ATOM   1428  O  O     . LEU A 1 173 ? 141.836 142.103 118.012 1.00 26.59 ?  173 LEU A O     1 
ATOM   1429  C  CB    . LEU A 1 173 ? 139.119 143.552 118.332 1.00 14.56 ?  173 LEU A CB    1 
ATOM   1430  C  CG    . LEU A 1 173 ? 137.664 143.784 117.929 1.00 16.55 ?  173 LEU A CG    1 
ATOM   1431  C  CD1   . LEU A 1 173 ? 136.777 143.662 119.153 1.00 20.59 ?  173 LEU A CD1   1 
ATOM   1432  C  CD2   . LEU A 1 173 ? 137.482 145.134 117.261 1.00 15.88 ?  173 LEU A CD2   1 
ATOM   1433  N  N     . GLU A 1 174 ? 142.355 144.286 118.232 1.00 23.22 ?  174 GLU A N     1 
ATOM   1434  C  CA    . GLU A 1 174 ? 143.585 144.069 118.980 1.00 19.58 ?  174 GLU A CA    1 
ATOM   1435  C  C     . GLU A 1 174 ? 143.299 144.310 120.456 1.00 17.36 ?  174 GLU A C     1 
ATOM   1436  O  O     . GLU A 1 174 ? 142.774 145.365 120.825 1.00 29.19 ?  174 GLU A O     1 
ATOM   1437  C  CB    . GLU A 1 174 ? 144.698 144.994 118.490 1.00 22.04 ?  174 GLU A CB    1 
ATOM   1438  C  CG    . GLU A 1 174 ? 145.238 144.654 117.120 1.00 20.41 ?  174 GLU A CG    1 
ATOM   1439  C  CD    . GLU A 1 174 ? 146.715 144.325 117.148 1.00 19.96 ?  174 GLU A CD    1 
ATOM   1440  O  OE1   . GLU A 1 174 ? 147.534 145.265 117.139 1.00 22.11 ?  174 GLU A OE1   1 
ATOM   1441  O  OE2   . GLU A 1 174 ? 147.057 143.126 117.177 1.00 32.00 -1 174 GLU A OE2   1 
ATOM   1442  N  N     . VAL A 1 175 ? 143.642 143.338 121.295 1.00 18.09 ?  175 VAL A N     1 
ATOM   1443  C  CA    . VAL A 1 175 ? 143.397 143.415 122.730 1.00 21.78 ?  175 VAL A CA    1 
ATOM   1444  C  C     . VAL A 1 175 ? 144.722 143.679 123.430 1.00 19.70 ?  175 VAL A C     1 
ATOM   1445  O  O     . VAL A 1 175 ? 145.675 142.904 123.285 1.00 21.46 ?  175 VAL A O     1 
ATOM   1446  C  CB    . VAL A 1 175 ? 142.741 142.130 123.258 1.00 21.89 ?  175 VAL A CB    1 
ATOM   1447  C  CG1   . VAL A 1 175 ? 142.090 142.381 124.608 1.00 15.48 ?  175 VAL A CG1   1 
ATOM   1448  C  CG2   . VAL A 1 175 ? 141.727 141.602 122.259 1.00 17.38 ?  175 VAL A CG2   1 
ATOM   1449  N  N     . ASN A 1 176 ? 144.785 144.769 124.188 1.00 15.24 ?  176 ASN A N     1 
ATOM   1450  C  CA    . ASN A 1 176 ? 145.975 145.086 124.958 1.00 18.20 ?  176 ASN A CA    1 
ATOM   1451  C  C     . ASN A 1 176 ? 145.988 144.303 126.267 1.00 21.81 ?  176 ASN A C     1 
ATOM   1452  O  O     . ASN A 1 176 ? 144.968 143.780 126.722 1.00 21.13 ?  176 ASN A O     1 
ATOM   1453  C  CB    . ASN A 1 176 ? 146.052 146.587 125.237 1.00 18.41 ?  176 ASN A CB    1 
ATOM   1454  C  CG    . ASN A 1 176 ? 147.456 147.127 125.126 1.00 23.52 ?  176 ASN A CG    1 
ATOM   1455  O  OD1   . ASN A 1 176 ? 148.429 146.387 125.254 1.00 27.38 ?  176 ASN A OD1   1 
ATOM   1456  N  ND2   . ASN A 1 176 ? 147.571 148.425 124.879 1.00 21.82 ?  176 ASN A ND2   1 
ATOM   1457  N  N     . ASP A 1 177 ? 147.170 144.237 126.880 1.00 29.34 ?  177 ASP A N     1 
ATOM   1458  C  CA    . ASP A 1 177 ? 147.386 143.419 128.073 1.00 22.42 ?  177 ASP A CA    1 
ATOM   1459  C  C     . ASP A 1 177 ? 146.980 144.200 129.325 1.00 22.88 ?  177 ASP A C     1 
ATOM   1460  O  O     . ASP A 1 177 ? 147.801 144.620 130.140 1.00 27.43 ?  177 ASP A O     1 
ATOM   1461  C  CB    . ASP A 1 177 ? 148.838 142.964 128.141 1.00 21.20 ?  177 ASP A CB    1 
ATOM   1462  C  CG    . ASP A 1 177 ? 149.075 141.931 129.219 1.00 27.82 ?  177 ASP A CG    1 
ATOM   1463  O  OD1   . ASP A 1 177 ? 148.171 141.105 129.459 1.00 30.56 ?  177 ASP A OD1   1 
ATOM   1464  O  OD2   . ASP A 1 177 ? 150.168 141.941 129.821 1.00 29.71 -1 177 ASP A OD2   1 
ATOM   1465  N  N     . SER A 1 178 ? 145.671 144.384 129.465 1.00 22.26 ?  178 SER A N     1 
ATOM   1466  C  CA    . SER A 1 178 ? 145.126 145.061 130.633 1.00 18.11 ?  178 SER A CA    1 
ATOM   1467  C  C     . SER A 1 178 ? 143.683 144.624 130.828 1.00 20.63 ?  178 SER A C     1 
ATOM   1468  O  O     . SER A 1 178 ? 143.018 144.183 129.889 1.00 29.47 ?  178 SER A O     1 
ATOM   1469  C  CB    . SER A 1 178 ? 145.221 146.583 130.497 1.00 19.31 ?  178 SER A CB    1 
ATOM   1470  O  OG    . SER A 1 178 ? 144.007 147.131 130.023 1.00 25.10 ?  178 SER A OG    1 
ATOM   1471  N  N     . LEU A 1 179 ? 143.208 144.752 132.069 1.00 27.75 ?  179 LEU A N     1 
ATOM   1472  C  CA    . LEU A 1 179 ? 141.819 144.418 132.366 1.00 20.46 ?  179 LEU A CA    1 
ATOM   1473  C  C     . LEU A 1 179 ? 140.865 145.430 131.748 1.00 22.67 ?  179 LEU A C     1 
ATOM   1474  O  O     . LEU A 1 179 ? 139.764 145.069 131.319 1.00 27.44 ?  179 LEU A O     1 
ATOM   1475  C  CB    . LEU A 1 179 ? 141.604 144.338 133.877 1.00 23.33 ?  179 LEU A CB    1 
ATOM   1476  C  CG    . LEU A 1 179 ? 140.250 143.794 134.335 1.00 22.04 ?  179 LEU A CG    1 
ATOM   1477  C  CD1   . LEU A 1 179 ? 140.144 142.307 134.045 1.00 24.32 ?  179 LEU A CD1   1 
ATOM   1478  C  CD2   . LEU A 1 179 ? 140.030 144.078 135.809 1.00 21.57 ?  179 LEU A CD2   1 
ATOM   1479  N  N     . ASN A 1 180 ? 141.262 146.705 131.708 1.00 23.10 ?  180 ASN A N     1 
ATOM   1480  C  CA    . ASN A 1 180 ? 140.449 147.707 131.027 1.00 21.89 ?  180 ASN A CA    1 
ATOM   1481  C  C     . ASN A 1 180 ? 140.304 147.372 129.550 1.00 26.71 ?  180 ASN A C     1 
ATOM   1482  O  O     . ASN A 1 180 ? 139.206 147.453 128.988 1.00 30.16 ?  180 ASN A O     1 
ATOM   1483  C  CB    . ASN A 1 180 ? 141.071 149.091 131.198 1.00 22.57 ?  180 ASN A CB    1 
ATOM   1484  C  CG    . ASN A 1 180 ? 140.717 149.733 132.520 1.00 27.08 ?  180 ASN A CG    1 
ATOM   1485  O  OD1   . ASN A 1 180 ? 139.693 149.418 133.124 1.00 33.00 ?  180 ASN A OD1   1 
ATOM   1486  N  ND2   . ASN A 1 180 ? 141.566 150.645 132.977 1.00 27.92 ?  180 ASN A ND2   1 
ATOM   1487  N  N     . ASP A 1 181 ? 141.404 146.970 128.913 1.00 25.42 ?  181 ASP A N     1 
ATOM   1488  C  CA    . ASP A 1 181 ? 141.359 146.618 127.501 1.00 16.89 ?  181 ASP A CA    1 
ATOM   1489  C  C     . ASP A 1 181 ? 140.598 145.322 127.264 1.00 20.98 ?  181 ASP A C     1 
ATOM   1490  O  O     . ASP A 1 181 ? 139.925 145.187 126.241 1.00 25.91 ?  181 ASP A O     1 
ATOM   1491  C  CB    . ASP A 1 181 ? 142.776 146.526 126.945 1.00 20.00 ?  181 ASP A CB    1 
ATOM   1492  C  CG    . ASP A 1 181 ? 143.408 147.888 126.748 1.00 32.71 ?  181 ASP A CG    1 
ATOM   1493  O  OD1   . ASP A 1 181 ? 143.070 148.562 125.754 1.00 36.80 ?  181 ASP A OD1   1 
ATOM   1494  O  OD2   . ASP A 1 181 ? 144.244 148.288 127.586 1.00 30.19 -1 181 ASP A OD2   1 
ATOM   1495  N  N     . ILE A 1 182 ? 140.673 144.367 128.191 1.00 21.36 ?  182 ILE A N     1 
ATOM   1496  C  CA    . ILE A 1 182 ? 139.905 143.133 128.041 1.00 21.47 ?  182 ILE A CA    1 
ATOM   1497  C  C     . ILE A 1 182 ? 138.412 143.410 128.183 1.00 18.86 ?  182 ILE A C     1 
ATOM   1498  O  O     . ILE A 1 182 ? 137.592 142.876 127.425 1.00 24.47 ?  182 ILE A O     1 
ATOM   1499  C  CB    . ILE A 1 182 ? 140.394 142.081 129.053 1.00 24.51 ?  182 ILE A CB    1 
ATOM   1500  C  CG1   . ILE A 1 182 ? 141.747 141.523 128.614 1.00 20.55 ?  182 ILE A CG1   1 
ATOM   1501  C  CG2   . ILE A 1 182 ? 139.379 140.957 129.201 1.00 26.74 ?  182 ILE A CG2   1 
ATOM   1502  C  CD1   . ILE A 1 182 ? 142.437 140.708 129.668 1.00 22.39 ?  182 ILE A CD1   1 
ATOM   1503  N  N     . SER A 1 183 ? 138.037 144.252 129.149 1.00 22.49 ?  183 SER A N     1 
ATOM   1504  C  CA    . SER A 1 183 ? 136.638 144.636 129.296 1.00 21.31 ?  183 SER A CA    1 
ATOM   1505  C  C     . SER A 1 183 ? 136.140 145.380 128.065 1.00 24.12 ?  183 SER A C     1 
ATOM   1506  O  O     . SER A 1 183 ? 135.026 145.129 127.586 1.00 30.09 ?  183 SER A O     1 
ATOM   1507  C  CB    . SER A 1 183 ? 136.461 145.497 130.545 1.00 21.24 ?  183 SER A CB    1 
ATOM   1508  O  OG    . SER A 1 183 ? 137.073 144.900 131.673 1.00 32.18 ?  183 SER A OG    1 
ATOM   1509  N  N     . ARG A 1 184 ? 136.951 146.298 127.537 1.00 23.49 ?  184 ARG A N     1 
ATOM   1510  C  CA    . ARG A 1 184 ? 136.563 147.001 126.321 1.00 23.99 ?  184 ARG A CA    1 
ATOM   1511  C  C     . ARG A 1 184 ? 136.472 146.057 125.132 1.00 28.93 ?  184 ARG A C     1 
ATOM   1512  O  O     . ARG A 1 184 ? 135.611 146.239 124.270 1.00 33.36 ?  184 ARG A O     1 
ATOM   1513  C  CB    . ARG A 1 184 ? 137.542 148.132 126.026 1.00 23.38 ?  184 ARG A CB    1 
ATOM   1514  C  CG    . ARG A 1 184 ? 136.943 149.241 125.185 1.00 27.12 ?  184 ARG A CG    1 
ATOM   1515  C  CD    . ARG A 1 184 ? 136.384 150.346 126.056 1.00 31.20 ?  184 ARG A CD    1 
ATOM   1516  N  NE    . ARG A 1 184 ? 134.947 150.506 125.873 1.00 31.34 ?  184 ARG A NE    1 
ATOM   1517  C  CZ    . ARG A 1 184 ? 134.215 151.428 126.483 1.00 35.55 ?  184 ARG A CZ    1 
ATOM   1518  N  NH1   . ARG A 1 184 ? 134.755 152.294 127.323 1.00 33.29 1  184 ARG A NH1   1 
ATOM   1519  N  NH2   . ARG A 1 184 ? 132.908 151.482 126.243 1.00 29.20 ?  184 ARG A NH2   1 
ATOM   1520  N  N     . ALA A 1 185 ? 137.346 145.052 125.063 1.00 28.47 ?  185 ALA A N     1 
ATOM   1521  C  CA    . ALA A 1 185 ? 137.263 144.069 123.991 1.00 15.38 ?  185 ALA A CA    1 
ATOM   1522  C  C     . ALA A 1 185 ? 135.972 143.272 124.078 1.00 21.04 ?  185 ALA A C     1 
ATOM   1523  O  O     . ALA A 1 185 ? 135.320 143.026 123.060 1.00 25.07 ?  185 ALA A O     1 
ATOM   1524  C  CB    . ALA A 1 185 ? 138.473 143.139 124.035 1.00 17.48 ?  185 ALA A CB    1 
ATOM   1525  N  N     . ILE A 1 186 ? 135.582 142.866 125.288 1.00 24.51 ?  186 ILE A N     1 
ATOM   1526  C  CA    . ILE A 1 186 ? 134.319 142.152 125.461 1.00 20.17 ?  186 ILE A CA    1 
ATOM   1527  C  C     . ILE A 1 186 ? 133.148 143.037 125.051 1.00 20.92 ?  186 ILE A C     1 
ATOM   1528  O  O     . ILE A 1 186 ? 132.232 142.598 124.340 1.00 27.02 ?  186 ILE A O     1 
ATOM   1529  C  CB    . ILE A 1 186 ? 134.174 141.669 126.917 1.00 27.30 ?  186 ILE A CB    1 
ATOM   1530  C  CG1   . ILE A 1 186 ? 135.164 140.545 127.213 1.00 24.05 ?  186 ILE A CG1   1 
ATOM   1531  C  CG2   . ILE A 1 186 ? 132.750 141.210 127.194 1.00 27.00 ?  186 ILE A CG2   1 
ATOM   1532  C  CD1   . ILE A 1 186 ? 135.375 140.311 128.691 1.00 25.30 ?  186 ILE A CD1   1 
ATOM   1533  N  N     . ASP A 1 187 ? 133.165 144.299 125.486 1.00 27.48 ?  187 ASP A N     1 
ATOM   1534  C  CA    . ASP A 1 187 ? 132.085 145.221 125.153 1.00 23.22 ?  187 ASP A CA    1 
ATOM   1535  C  C     . ASP A 1 187 ? 131.986 145.433 123.648 1.00 27.24 ?  187 ASP A C     1 
ATOM   1536  O  O     . ASP A 1 187 ? 130.895 145.368 123.073 1.00 32.57 ?  187 ASP A O     1 
ATOM   1537  C  CB    . ASP A 1 187 ? 132.299 146.552 125.873 1.00 22.13 ?  187 ASP A CB    1 
ATOM   1538  C  CG    . ASP A 1 187 ? 131.452 147.670 125.299 1.00 34.84 ?  187 ASP A CG    1 
ATOM   1539  O  OD1   . ASP A 1 187 ? 130.221 147.493 125.185 1.00 36.41 ?  187 ASP A OD1   1 
ATOM   1540  O  OD2   . ASP A 1 187 ? 132.018 148.730 124.958 1.00 37.56 -1 187 ASP A OD2   1 
ATOM   1541  N  N     . ILE A 1 188 ? 133.122 145.678 122.993 1.00 25.83 ?  188 ILE A N     1 
ATOM   1542  C  CA    . ILE A 1 188 ? 133.125 145.934 121.556 1.00 22.68 ?  188 ILE A CA    1 
ATOM   1543  C  C     . ILE A 1 188 ? 132.728 144.681 120.790 1.00 22.53 ?  188 ILE A C     1 
ATOM   1544  O  O     . ILE A 1 188 ? 132.035 144.758 119.770 1.00 28.19 ?  188 ILE A O     1 
ATOM   1545  C  CB    . ILE A 1 188 ? 134.502 146.464 121.115 1.00 25.08 ?  188 ILE A CB    1 
ATOM   1546  C  CG1   . ILE A 1 188 ? 134.744 147.861 121.685 1.00 23.81 ?  188 ILE A CG1   1 
ATOM   1547  C  CG2   . ILE A 1 188 ? 134.608 146.511 119.605 1.00 21.04 ?  188 ILE A CG2   1 
ATOM   1548  C  CD1   . ILE A 1 188 ? 136.097 148.425 121.346 1.00 23.99 ?  188 ILE A CD1   1 
ATOM   1549  N  N     . SER A 1 189 ? 133.153 143.510 121.266 1.00 24.80 ?  189 SER A N     1 
ATOM   1550  C  CA    . SER A 1 189 ? 132.754 142.264 120.626 1.00 14.85 ?  189 SER A CA    1 
ATOM   1551  C  C     . SER A 1 189 ? 131.247 142.074 120.695 1.00 21.48 ?  189 SER A C     1 
ATOM   1552  O  O     . SER A 1 189 ? 130.621 141.689 119.702 1.00 28.50 ?  189 SER A O     1 
ATOM   1553  C  CB    . SER A 1 189 ? 133.474 141.085 121.281 1.00 20.15 ?  189 SER A CB    1 
ATOM   1554  O  OG    . SER A 1 189 ? 134.869 141.315 121.349 1.00 24.99 ?  189 SER A OG    1 
ATOM   1555  N  N     . MET A 1 190 ? 130.643 142.347 121.853 1.00 24.96 ?  190 MET A N     1 
ATOM   1556  C  CA    . MET A 1 190 ? 129.191 142.240 121.951 1.00 25.46 ?  190 MET A CA    1 
ATOM   1557  C  C     . MET A 1 190 ? 128.493 143.288 121.091 1.00 24.52 ?  190 MET A C     1 
ATOM   1558  O  O     . MET A 1 190 ? 127.464 142.999 120.471 1.00 25.65 ?  190 MET A O     1 
ATOM   1559  C  CB    . MET A 1 190 ? 128.739 142.347 123.407 1.00 24.20 ?  190 MET A CB    1 
ATOM   1560  C  CG    . MET A 1 190 ? 128.903 141.054 124.189 1.00 25.61 ?  190 MET A CG    1 
ATOM   1561  S  SD    . MET A 1 190 ? 128.693 141.226 125.969 1.00 39.39 ?  190 MET A SD    1 
ATOM   1562  C  CE    . MET A 1 190 ? 128.904 142.987 126.174 1.00 30.50 ?  190 MET A CE    1 
ATOM   1563  N  N     . GLN A 1 191 ? 129.034 144.507 121.037 1.00 20.97 ?  191 GLN A N     1 
ATOM   1564  C  CA    . GLN A 1 191 ? 128.427 145.548 120.210 1.00 27.46 ?  191 GLN A CA    1 
ATOM   1565  C  C     . GLN A 1 191 ? 128.461 145.179 118.732 1.00 26.57 ?  191 GLN A C     1 
ATOM   1566  O  O     . GLN A 1 191 ? 127.480 145.388 118.010 1.00 30.30 ?  191 GLN A O     1 
ATOM   1567  C  CB    . GLN A 1 191 ? 129.128 146.888 120.438 1.00 28.45 ?  191 GLN A CB    1 
ATOM   1568  C  CG    . GLN A 1 191 ? 128.992 147.442 121.843 1.00 26.96 ?  191 GLN A CG    1 
ATOM   1569  C  CD    . GLN A 1 191 ? 127.576 147.858 122.182 1.00 29.87 ?  191 GLN A CD    1 
ATOM   1570  O  OE1   . GLN A 1 191 ? 127.171 147.825 123.342 1.00 30.00 ?  191 GLN A OE1   1 
ATOM   1571  N  NE2   . GLN A 1 191 ? 126.817 148.267 121.171 1.00 30.62 ?  191 GLN A NE2   1 
ATOM   1572  N  N     . LEU A 1 192 ? 129.585 144.635 118.262 1.00 26.64 ?  192 LEU A N     1 
ATOM   1573  C  CA    . LEU A 1 192 ? 129.713 144.288 116.852 1.00 21.91 ?  192 LEU A CA    1 
ATOM   1574  C  C     . LEU A 1 192 ? 128.953 143.016 116.502 1.00 24.46 ?  192 LEU A C     1 
ATOM   1575  O  O     . LEU A 1 192 ? 128.414 142.910 115.396 1.00 33.12 ?  192 LEU A O     1 
ATOM   1576  C  CB    . LEU A 1 192 ? 131.188 144.145 116.477 1.00 21.31 ?  192 LEU A CB    1 
ATOM   1577  C  CG    . LEU A 1 192 ? 132.025 145.425 116.518 1.00 20.35 ?  192 LEU A CG    1 
ATOM   1578  C  CD1   . LEU A 1 192 ? 133.504 145.104 116.404 1.00 20.92 ?  192 LEU A CD1   1 
ATOM   1579  C  CD2   . LEU A 1 192 ? 131.599 146.388 115.425 1.00 18.19 ?  192 LEU A CD2   1 
ATOM   1580  N  N     . SER A 1 193 ? 128.899 142.046 117.418 1.00 29.05 ?  193 SER A N     1 
ATOM   1581  C  CA    . SER A 1 193 ? 128.071 140.865 117.202 1.00 26.96 ?  193 SER A CA    1 
ATOM   1582  C  C     . SER A 1 193 ? 126.595 141.232 117.187 1.00 30.56 ?  193 SER A C     1 
ATOM   1583  O  O     . SER A 1 193 ? 125.803 140.619 116.463 1.00 34.58 ?  193 SER A O     1 
ATOM   1584  C  CB    . SER A 1 193 ? 128.362 139.823 118.280 1.00 28.66 ?  193 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 193 ? 127.595 138.650 118.078 1.00 37.95 ?  193 SER A OG    1 
ATOM   1586  N  N     . LYS A 1 194 ? 126.206 142.227 117.988 1.00 33.77 ?  194 LYS A N     1 
ATOM   1587  C  CA    . LYS A 1 194 ? 124.836 142.725 117.955 1.00 31.64 ?  194 LYS A CA    1 
ATOM   1588  C  C     . LYS A 1 194 ? 124.501 143.310 116.590 1.00 36.17 ?  194 LYS A C     1 
ATOM   1589  O  O     . LYS A 1 194 ? 123.380 143.147 116.093 1.00 39.77 ?  194 LYS A O     1 
ATOM   1590  C  CB    . LYS A 1 194 ? 124.646 143.763 119.060 1.00 29.29 ?  194 LYS A CB    1 
ATOM   1591  C  CG    . LYS A 1 194 ? 123.454 144.678 118.883 1.00 33.70 ?  194 LYS A CG    1 
ATOM   1592  C  CD    . LYS A 1 194 ? 123.557 145.881 119.803 1.00 36.36 ?  194 LYS A CD    1 
ATOM   1593  C  CE    . LYS A 1 194 ? 122.232 146.616 119.908 1.00 34.10 ?  194 LYS A CE    1 
ATOM   1594  N  NZ    . LYS A 1 194 ? 122.321 147.778 120.833 1.00 34.07 1  194 LYS A NZ    1 
ATOM   1595  N  N     . LEU A 1 195 ? 125.464 143.986 115.963 1.00 34.21 ?  195 LEU A N     1 
ATOM   1596  C  CA    . LEU A 1 195 ? 125.278 144.507 114.616 1.00 31.80 ?  195 LEU A CA    1 
ATOM   1597  C  C     . LEU A 1 195 ? 125.245 143.411 113.560 1.00 34.40 ?  195 LEU A C     1 
ATOM   1598  O  O     . LEU A 1 195 ? 124.922 143.700 112.403 1.00 38.44 ?  195 LEU A O     1 
ATOM   1599  C  CB    . LEU A 1 195 ? 126.387 145.504 114.280 1.00 33.76 ?  195 LEU A CB    1 
ATOM   1600  C  CG    . LEU A 1 195 ? 126.458 146.748 115.164 1.00 34.19 ?  195 LEU A CG    1 
ATOM   1601  C  CD1   . LEU A 1 195 ? 127.717 147.541 114.860 1.00 30.68 ?  195 LEU A CD1   1 
ATOM   1602  C  CD2   . LEU A 1 195 ? 125.217 147.604 114.980 1.00 36.49 ?  195 LEU A CD2   1 
ATOM   1603  N  N     . GLY A 1 196 ? 125.573 142.175 113.925 1.00 31.78 ?  196 GLY A N     1 
ATOM   1604  C  CA    . GLY A 1 196 ? 125.571 141.066 112.997 1.00 30.65 ?  196 GLY A CA    1 
ATOM   1605  C  C     . GLY A 1 196 ? 126.925 140.696 112.439 1.00 35.94 ?  196 GLY A C     1 
ATOM   1606  O  O     . GLY A 1 196 ? 127.013 139.741 111.659 1.00 40.43 ?  196 GLY A O     1 
ATOM   1607  N  N     . GLY A 1 197 ? 127.979 141.413 112.811 1.00 30.13 ?  197 GLY A N     1 
ATOM   1608  C  CA    . GLY A 1 197 ? 129.294 141.156 112.271 1.00 24.75 ?  197 GLY A CA    1 
ATOM   1609  C  C     . GLY A 1 197 ? 130.046 140.061 113.007 1.00 24.86 ?  197 GLY A C     1 
ATOM   1610  O  O     . GLY A 1 197 ? 129.820 139.807 114.186 1.00 30.82 ?  197 GLY A O     1 
ATOM   1611  N  N     . GLY A 1 198 ? 130.950 139.408 112.280 1.00 20.05 ?  198 GLY A N     1 
ATOM   1612  C  CA    . GLY A 1 198 ? 131.868 138.458 112.877 1.00 17.92 ?  198 GLY A CA    1 
ATOM   1613  C  C     . GLY A 1 198 ? 133.101 139.185 113.372 1.00 16.53 ?  198 GLY A C     1 
ATOM   1614  O  O     . GLY A 1 198 ? 133.671 140.014 112.659 1.00 22.13 ?  198 GLY A O     1 
ATOM   1615  N  N     . VAL A 1 199 ? 133.510 138.873 114.597 1.00 20.68 ?  199 VAL A N     1 
ATOM   1616  C  CA    . VAL A 1 199 ? 134.574 139.597 115.279 1.00 16.18 ?  199 VAL A CA    1 
ATOM   1617  C  C     . VAL A 1 199 ? 135.751 138.659 115.493 1.00 11.98 ?  199 VAL A C     1 
ATOM   1618  O  O     . VAL A 1 199 ? 135.584 137.551 116.013 1.00 15.18 ?  199 VAL A O     1 
ATOM   1619  C  CB    . VAL A 1 199 ? 134.093 140.179 116.621 1.00 14.84 ?  199 VAL A CB    1 
ATOM   1620  C  CG1   . VAL A 1 199 ? 135.156 141.075 117.219 1.00 14.75 ?  199 VAL A CG1   1 
ATOM   1621  C  CG2   . VAL A 1 199 ? 132.795 140.937 116.431 1.00 18.84 ?  199 VAL A CG2   1 
ATOM   1622  N  N     . SER A 1 200 ? 136.936 139.105 115.094 1.00 16.69 ?  200 SER A N     1 
ATOM   1623  C  CA    . SER A 1 200 ? 138.178 138.401 115.364 1.00 7.23  ?  200 SER A CA    1 
ATOM   1624  C  C     . SER A 1 200 ? 139.007 139.217 116.343 1.00 12.61 ?  200 SER A C     1 
ATOM   1625  O  O     . SER A 1 200 ? 139.066 140.446 116.248 1.00 19.88 ?  200 SER A O     1 
ATOM   1626  C  CB    . SER A 1 200 ? 138.969 138.161 114.079 1.00 14.12 ?  200 SER A CB    1 
ATOM   1627  O  OG    . SER A 1 200 ? 139.904 137.113 114.247 1.00 19.62 ?  200 SER A OG    1 
ATOM   1628  N  N     . LEU A 1 201 ? 139.642 138.533 117.287 1.00 18.50 ?  201 LEU A N     1 
ATOM   1629  C  CA    . LEU A 1 201 ? 140.428 139.187 118.320 1.00 10.78 ?  201 LEU A CA    1 
ATOM   1630  C  C     . LEU A 1 201 ? 141.827 138.594 118.363 1.00 10.09 ?  201 LEU A C     1 
ATOM   1631  O  O     . LEU A 1 201 ? 141.997 137.374 118.298 1.00 15.23 ?  201 LEU A O     1 
ATOM   1632  C  CB    . LEU A 1 201 ? 139.763 139.053 119.695 1.00 14.87 ?  201 LEU A CB    1 
ATOM   1633  C  CG    . LEU A 1 201 ? 138.366 139.663 119.824 1.00 15.59 ?  201 LEU A CG    1 
ATOM   1634  C  CD1   . LEU A 1 201 ? 137.308 138.574 119.885 1.00 20.18 ?  201 LEU A CD1   1 
ATOM   1635  C  CD2   . LEU A 1 201 ? 138.284 140.564 121.040 1.00 12.72 ?  201 LEU A CD2   1 
ATOM   1636  N  N     . ASN A 1 202 ? 142.823 139.468 118.468 1.00 10.92 ?  202 ASN A N     1 
ATOM   1637  C  CA    . ASN A 1 202 ? 144.202 139.053 118.679 1.00 8.56  ?  202 ASN A CA    1 
ATOM   1638  C  C     . ASN A 1 202 ? 144.457 138.953 120.177 1.00 18.53 ?  202 ASN A C     1 
ATOM   1639  O  O     . ASN A 1 202 ? 144.296 139.937 120.906 1.00 29.15 ?  202 ASN A O     1 
ATOM   1640  C  CB    . ASN A 1 202 ? 145.172 140.039 118.033 1.00 9.92  ?  202 ASN A CB    1 
ATOM   1641  C  CG    . ASN A 1 202 ? 146.560 139.461 117.861 1.00 12.50 ?  202 ASN A CG    1 
ATOM   1642  O  OD1   . ASN A 1 202 ? 146.729 138.250 117.739 1.00 17.38 ?  202 ASN A OD1   1 
ATOM   1643  N  ND2   . ASN A 1 202 ? 147.563 140.328 117.850 1.00 10.64 ?  202 ASN A ND2   1 
ATOM   1644  N  N     . LEU A 1 203 ? 144.854 137.766 120.635 1.00 13.46 ?  203 LEU A N     1 
ATOM   1645  C  CA    . LEU A 1 203 ? 145.108 137.523 122.047 1.00 11.52 ?  203 LEU A CA    1 
ATOM   1646  C  C     . LEU A 1 203 ? 146.594 137.358 122.345 1.00 13.48 ?  203 LEU A C     1 
ATOM   1647  O  O     . LEU A 1 203 ? 146.958 136.883 123.424 1.00 21.45 ?  203 LEU A O     1 
ATOM   1648  C  CB    . LEU A 1 203 ? 144.330 136.294 122.517 1.00 17.29 ?  203 LEU A CB    1 
ATOM   1649  C  CG    . LEU A 1 203 ? 142.808 136.348 122.373 1.00 16.61 ?  203 LEU A CG    1 
ATOM   1650  C  CD1   . LEU A 1 203 ? 142.161 135.268 123.218 1.00 17.98 ?  203 LEU A CD1   1 
ATOM   1651  C  CD2   . LEU A 1 203 ? 142.265 137.717 122.752 1.00 13.98 ?  203 LEU A CD2   1 
ATOM   1652  N  N     . SER A 1 204 ? 147.460 137.750 121.410 1.00 12.80 ?  204 SER A N     1 
ATOM   1653  C  CA    . SER A 1 204 ? 148.893 137.548 121.586 1.00 15.21 ?  204 SER A CA    1 
ATOM   1654  C  C     . SER A 1 204 ? 149.502 138.537 122.571 1.00 20.30 ?  204 SER A C     1 
ATOM   1655  O  O     . SER A 1 204 ? 150.447 138.186 123.285 1.00 27.24 ?  204 SER A O     1 
ATOM   1656  C  CB    . SER A 1 204 ? 149.603 137.647 120.239 1.00 15.24 ?  204 SER A CB    1 
ATOM   1657  O  OG    . SER A 1 204 ? 149.024 136.764 119.296 1.00 22.85 ?  204 SER A OG    1 
ATOM   1658  N  N     . LYS A 1 205 ? 148.991 139.769 122.621 1.00 19.51 ?  205 LYS A N     1 
ATOM   1659  C  CA    . LYS A 1 205 ? 149.523 140.749 123.560 1.00 16.00 ?  205 LYS A CA    1 
ATOM   1660  C  C     . LYS A 1 205 ? 149.163 140.425 125.000 1.00 18.09 ?  205 LYS A C     1 
ATOM   1661  O  O     . LYS A 1 205 ? 149.828 140.918 125.915 1.00 22.70 ?  205 LYS A O     1 
ATOM   1662  C  CB    . LYS A 1 205 ? 149.029 142.150 123.206 1.00 16.09 ?  205 LYS A CB    1 
ATOM   1663  C  CG    . LYS A 1 205 ? 149.628 142.705 121.934 1.00 18.07 ?  205 LYS A CG    1 
ATOM   1664  C  CD    . LYS A 1 205 ? 149.138 144.110 121.659 1.00 23.59 ?  205 LYS A CD    1 
ATOM   1665  C  CE    . LYS A 1 205 ? 149.889 144.730 120.496 1.00 26.62 ?  205 LYS A CE    1 
ATOM   1666  N  NZ    . LYS A 1 205 ? 149.698 143.962 119.238 1.00 19.06 1  205 LYS A NZ    1 
ATOM   1667  N  N     . LEU A 1 206 ? 148.134 139.611 125.219 1.00 17.87 ?  206 LEU A N     1 
ATOM   1668  C  CA    . LEU A 1 206 ? 147.759 139.217 126.568 1.00 12.12 ?  206 LEU A CA    1 
ATOM   1669  C  C     . LEU A 1 206 ? 148.834 138.326 127.171 1.00 17.25 ?  206 LEU A C     1 
ATOM   1670  O  O     . LEU A 1 206 ? 149.338 137.411 126.512 1.00 21.62 ?  206 LEU A O     1 
ATOM   1671  C  CB    . LEU A 1 206 ? 146.419 138.488 126.549 1.00 19.76 ?  206 LEU A CB    1 
ATOM   1672  C  CG    . LEU A 1 206 ? 145.217 139.317 126.103 1.00 20.73 ?  206 LEU A CG    1 
ATOM   1673  C  CD1   . LEU A 1 206 ? 143.962 138.471 126.122 1.00 16.80 ?  206 LEU A CD1   1 
ATOM   1674  C  CD2   . LEU A 1 206 ? 145.060 140.539 126.986 1.00 23.23 ?  206 LEU A CD2   1 
ATOM   1675  N  N     . ARG A 1 207 ? 149.184 138.589 128.427 1.00 24.80 ?  207 ARG A N     1 
ATOM   1676  C  CA    . ARG A 1 207 ? 150.218 137.804 129.081 1.00 22.16 ?  207 ARG A CA    1 
ATOM   1677  C  C     . ARG A 1 207 ? 149.707 136.405 129.404 1.00 27.34 ?  207 ARG A C     1 
ATOM   1678  O  O     . ARG A 1 207 ? 148.508 136.179 129.586 1.00 27.88 ?  207 ARG A O     1 
ATOM   1679  C  CB    . ARG A 1 207 ? 150.710 138.505 130.344 1.00 22.25 ?  207 ARG A CB    1 
ATOM   1680  C  CG    . ARG A 1 207 ? 149.701 138.613 131.463 1.00 23.35 ?  207 ARG A CG    1 
ATOM   1681  C  CD    . ARG A 1 207 ? 150.234 139.519 132.556 1.00 26.39 ?  207 ARG A CD    1 
ATOM   1682  N  NE    . ARG A 1 207 ? 150.283 140.911 132.128 1.00 28.94 ?  207 ARG A NE    1 
ATOM   1683  C  CZ    . ARG A 1 207 ? 150.301 141.949 132.951 1.00 24.31 ?  207 ARG A CZ    1 
ATOM   1684  N  NH1   . ARG A 1 207 ? 150.302 141.790 134.263 1.00 28.75 1  207 ARG A NH1   1 
ATOM   1685  N  NH2   . ARG A 1 207 ? 150.316 143.178 132.445 1.00 20.66 ?  207 ARG A NH2   1 
ATOM   1686  N  N     . ALA A 1 208 ? 150.639 135.461 129.470 1.00 33.04 ?  208 ALA A N     1 
ATOM   1687  C  CA    . ALA A 1 208 ? 150.308 134.052 129.564 1.00 24.77 ?  208 ALA A CA    1 
ATOM   1688  C  C     . ALA A 1 208 ? 149.857 133.682 130.975 1.00 31.73 ?  208 ALA A C     1 
ATOM   1689  O  O     . ALA A 1 208 ? 149.871 134.495 131.902 1.00 36.14 ?  208 ALA A O     1 
ATOM   1690  C  CB    . ALA A 1 208 ? 151.505 133.202 129.148 1.00 25.67 ?  208 ALA A CB    1 
ATOM   1691  N  N     . LYS A 1 209 ? 149.436 132.430 131.124 1.00 32.25 ?  209 LYS A N     1 
ATOM   1692  C  CA    . LYS A 1 209 ? 149.027 131.920 132.424 1.00 29.35 ?  209 LYS A CA    1 
ATOM   1693  C  C     . LYS A 1 209 ? 150.226 131.817 133.357 1.00 33.86 ?  209 LYS A C     1 
ATOM   1694  O  O     . LYS A 1 209 ? 151.303 131.360 132.963 1.00 34.76 ?  209 LYS A O     1 
ATOM   1695  C  CB    . LYS A 1 209 ? 148.361 130.553 132.269 1.00 29.71 ?  209 LYS A CB    1 
ATOM   1696  C  CG    . LYS A 1 209 ? 147.426 130.181 133.403 1.00 32.21 ?  209 LYS A CG    1 
ATOM   1697  C  CD    . LYS A 1 209 ? 147.103 128.696 133.385 1.00 31.43 ?  209 LYS A CD    1 
ATOM   1698  C  CE    . LYS A 1 209 ? 148.340 127.862 133.097 1.00 35.68 ?  209 LYS A CE    1 
ATOM   1699  N  NZ    . LYS A 1 209 ? 147.991 126.474 132.685 1.00 36.68 1  209 LYS A NZ    1 
ATOM   1700  N  N     . GLY A 1 210 ? 150.032 132.245 134.601 1.00 35.89 ?  210 GLY A N     1 
ATOM   1701  C  CA    . GLY A 1 210 ? 151.109 132.227 135.568 1.00 34.31 ?  210 GLY A CA    1 
ATOM   1702  C  C     . GLY A 1 210 ? 152.007 133.439 135.549 1.00 36.82 ?  210 GLY A C     1 
ATOM   1703  O  O     . GLY A 1 210 ? 153.128 133.373 136.062 1.00 38.71 ?  210 GLY A O     1 
ATOM   1704  N  N     . GLU A 1 211 ? 151.557 134.544 134.968 1.00 37.12 ?  211 GLU A N     1 
ATOM   1705  C  CA    . GLU A 1 211 ? 152.302 135.792 134.986 1.00 33.53 ?  211 GLU A CA    1 
ATOM   1706  C  C     . GLU A 1 211 ? 151.783 136.696 136.097 1.00 36.61 ?  211 GLU A C     1 
ATOM   1707  O  O     . GLU A 1 211 ? 150.669 136.531 136.599 1.00 37.11 ?  211 GLU A O     1 
ATOM   1708  C  CB    . GLU A 1 211 ? 152.209 136.503 133.635 1.00 32.02 ?  211 GLU A CB    1 
ATOM   1709  C  CG    . GLU A 1 211 ? 152.751 135.686 132.482 1.00 32.88 ?  211 GLU A CG    1 
ATOM   1710  C  CD    . GLU A 1 211 ? 153.707 136.471 131.612 1.00 37.46 ?  211 GLU A CD    1 
ATOM   1711  O  OE1   . GLU A 1 211 ? 154.821 136.777 132.083 1.00 41.10 ?  211 GLU A OE1   1 
ATOM   1712  O  OE2   . GLU A 1 211 ? 153.353 136.771 130.453 1.00 30.94 -1 211 GLU A OE2   1 
ATOM   1713  N  N     . ALA A 1 212 ? 152.612 137.661 136.479 1.00 34.70 ?  212 ALA A N     1 
ATOM   1714  C  CA    . ALA A 1 212 ? 152.295 138.534 137.598 1.00 31.46 ?  212 ALA A CA    1 
ATOM   1715  C  C     . ALA A 1 212 ? 151.343 139.647 137.180 1.00 36.01 ?  212 ALA A C     1 
ATOM   1716  O  O     . ALA A 1 212 ? 151.414 140.162 136.061 1.00 39.23 ?  212 ALA A O     1 
ATOM   1717  C  CB    . ALA A 1 212 ? 153.573 139.138 138.180 1.00 35.89 ?  212 ALA A CB    1 
ATOM   1718  N  N     . ILE A 1 213 ? 150.446 140.010 138.089 1.00 34.91 ?  213 ILE A N     1 
ATOM   1719  C  CA    . ILE A 1 213 ? 149.588 141.183 137.937 1.00 33.44 ?  213 ILE A CA    1 
ATOM   1720  C  C     . ILE A 1 213 ? 149.953 142.126 139.076 1.00 35.43 ?  213 ILE A C     1 
ATOM   1721  O  O     . ILE A 1 213 ? 149.413 142.025 140.180 1.00 40.52 ?  213 ILE A O     1 
ATOM   1722  C  CB    . ILE A 1 213 ? 148.098 140.835 137.962 1.00 35.77 ?  213 ILE A CB    1 
ATOM   1723  C  CG1   . ILE A 1 213 ? 147.801 139.636 137.065 1.00 37.06 ?  213 ILE A CG1   1 
ATOM   1724  C  CG2   . ILE A 1 213 ? 147.269 142.034 137.537 1.00 32.96 ?  213 ILE A CG2   1 
ATOM   1725  C  CD1   . ILE A 1 213 ? 146.458 139.006 137.338 1.00 30.23 ?  213 ILE A CD1   1 
ATOM   1726  N  N     . LYS A 1 214 ? 150.862 143.066 138.808 1.00 41.20 ?  214 LYS A N     1 
ATOM   1727  C  CA    . LYS A 1 214 ? 151.350 144.015 139.808 1.00 40.66 ?  214 LYS A CA    1 
ATOM   1728  C  C     . LYS A 1 214 ? 152.000 143.279 140.985 1.00 44.42 ?  214 LYS A C     1 
ATOM   1729  O  O     . LYS A 1 214 ? 151.493 143.248 142.106 1.00 46.37 ?  214 LYS A O     1 
ATOM   1730  C  CB    . LYS A 1 214 ? 150.227 144.947 140.278 1.00 39.51 ?  214 LYS A CB    1 
ATOM   1731  C  CG    . LYS A 1 214 ? 150.397 146.389 139.837 1.00 42.74 ?  214 LYS A CG    1 
ATOM   1732  C  CD    . LYS A 1 214 ? 149.244 147.256 140.312 1.00 42.94 ?  214 LYS A CD    1 
ATOM   1733  C  CE    . LYS A 1 214 ? 149.170 148.547 139.515 1.00 45.18 ?  214 LYS A CE    1 
ATOM   1734  N  NZ    . LYS A 1 214 ? 147.806 149.143 139.540 1.00 43.21 1  214 LYS A NZ    1 
ATOM   1735  N  N     . ASP A 1 215 ? 153.119 142.633 140.658 1.00 45.21 ?  215 ASP A N     1 
ATOM   1736  C  CA    . ASP A 1 215 ? 154.090 142.035 141.576 1.00 50.42 ?  215 ASP A CA    1 
ATOM   1737  C  C     . ASP A 1 215 ? 153.523 140.906 142.435 1.00 50.21 ?  215 ASP A C     1 
ATOM   1738  O  O     . ASP A 1 215 ? 154.172 140.494 143.404 1.00 52.51 ?  215 ASP A O     1 
ATOM   1739  C  CB    . ASP A 1 215 ? 154.772 143.098 142.463 1.00 49.52 ?  215 ASP A CB    1 
ATOM   1740  C  CG    . ASP A 1 215 ? 153.874 143.632 143.570 1.00 52.69 ?  215 ASP A CG    1 
ATOM   1741  O  OD1   . ASP A 1 215 ? 153.607 142.906 144.549 1.00 51.32 ?  215 ASP A OD1   1 
ATOM   1742  O  OD2   . ASP A 1 215 ? 153.438 144.798 143.461 1.00 51.14 -1 215 ASP A OD2   1 
ATOM   1743  N  N     . VAL A 1 216 ? 152.350 140.373 142.109 1.00 43.00 ?  216 VAL A N     1 
ATOM   1744  C  CA    . VAL A 1 216 ? 151.884 139.117 142.689 1.00 45.82 ?  216 VAL A CA    1 
ATOM   1745  C  C     . VAL A 1 216 ? 151.913 138.059 141.591 1.00 47.78 ?  216 VAL A C     1 
ATOM   1746  O  O     . VAL A 1 216 ? 151.238 138.194 140.564 1.00 50.41 ?  216 VAL A O     1 
ATOM   1747  C  CB    . VAL A 1 216 ? 150.488 139.252 143.323 1.00 45.53 ?  216 VAL A CB    1 
ATOM   1748  C  CG1   . VAL A 1 216 ? 149.515 139.917 142.385 1.00 44.93 ?  216 VAL A CG1   1 
ATOM   1749  C  CG2   . VAL A 1 216 ? 149.965 137.887 143.737 1.00 45.66 ?  216 VAL A CG2   1 
ATOM   1750  N  N     . GLU A 1 217 ? 152.702 137.014 141.805 1.00 48.05 ?  217 GLU A N     1 
ATOM   1751  C  CA    . GLU A 1 217 ? 153.056 136.074 140.754 1.00 46.87 ?  217 GLU A CA    1 
ATOM   1752  C  C     . GLU A 1 217 ? 152.014 134.970 140.616 1.00 48.29 ?  217 GLU A C     1 
ATOM   1753  O  O     . GLU A 1 217 ? 151.204 134.726 141.514 1.00 49.42 ?  217 GLU A O     1 
ATOM   1754  C  CB    . GLU A 1 217 ? 154.431 135.466 141.033 1.00 48.30 ?  217 GLU A CB    1 
ATOM   1755  C  CG    . GLU A 1 217 ? 155.432 136.464 141.591 1.00 49.23 ?  217 GLU A CG    1 
ATOM   1756  C  CD    . GLU A 1 217 ? 156.313 137.067 140.517 1.00 51.51 ?  217 GLU A CD    1 
ATOM   1757  O  OE1   . GLU A 1 217 ? 156.808 136.309 139.657 1.00 53.39 ?  217 GLU A OE1   1 
ATOM   1758  O  OE2   . GLU A 1 217 ? 156.505 138.301 140.529 1.00 49.38 -1 217 GLU A OE2   1 
ATOM   1759  N  N     . ASN A 1 218 ? 152.053 134.298 139.462 1.00 45.48 ?  218 ASN A N     1 
ATOM   1760  C  CA    . ASN A 1 218 ? 151.128 133.211 139.138 1.00 43.90 ?  218 ASN A CA    1 
ATOM   1761  C  C     . ASN A 1 218 ? 149.679 133.661 139.291 1.00 47.78 ?  218 ASN A C     1 
ATOM   1762  O  O     . ASN A 1 218 ? 148.813 132.913 139.748 1.00 49.11 ?  218 ASN A O     1 
ATOM   1763  C  CB    . ASN A 1 218 ? 151.413 131.974 139.989 1.00 45.70 ?  218 ASN A CB    1 
ATOM   1764  C  CG    . ASN A 1 218 ? 152.589 131.173 139.471 1.00 48.95 ?  218 ASN A CG    1 
ATOM   1765  O  OD1   . ASN A 1 218 ? 152.429 130.292 138.627 1.00 48.93 ?  218 ASN A OD1   1 
ATOM   1766  N  ND2   . ASN A 1 218 ? 153.780 131.480 139.970 1.00 46.74 ?  218 ASN A ND2   1 
ATOM   1767  N  N     . ALA A 1 219 ? 149.413 134.905 138.899 1.00 40.88 ?  219 ALA A N     1 
ATOM   1768  C  CA    . ALA A 1 219 ? 148.109 135.518 139.098 1.00 38.59 ?  219 ALA A CA    1 
ATOM   1769  C  C     . ALA A 1 219 ? 147.259 135.558 137.839 1.00 40.39 ?  219 ALA A C     1 
ATOM   1770  O  O     . ALA A 1 219 ? 146.029 135.509 137.936 1.00 41.10 ?  219 ALA A O     1 
ATOM   1771  C  CB    . ALA A 1 219 ? 148.282 136.942 139.634 1.00 37.28 ?  219 ALA A CB    1 
ATOM   1772  N  N     . THR A 1 220 ? 147.880 135.639 136.667 1.00 37.47 ?  220 THR A N     1 
ATOM   1773  C  CA    . THR A 1 220 ? 147.137 135.768 135.423 1.00 34.68 ?  220 THR A CA    1 
ATOM   1774  C  C     . THR A 1 220 ? 146.577 134.415 135.002 1.00 35.72 ?  220 THR A C     1 
ATOM   1775  O  O     . THR A 1 220 ? 147.261 133.391 135.082 1.00 37.02 ?  220 THR A O     1 
ATOM   1776  C  CB    . THR A 1 220 ? 148.043 136.340 134.330 1.00 33.58 ?  220 THR A CB    1 
ATOM   1777  O  OG1   . THR A 1 220 ? 148.302 137.722 134.602 1.00 36.06 ?  220 THR A OG1   1 
ATOM   1778  C  CG2   . THR A 1 220 ? 147.376 136.247 132.975 1.00 35.48 ?  220 THR A CG2   1 
ATOM   1779  N  N     . LYS A 1 221 ? 145.321 134.415 134.559 1.00 37.24 ?  221 LYS A N     1 
ATOM   1780  C  CA    . LYS A 1 221 ? 144.660 133.197 134.108 1.00 32.88 ?  221 LYS A CA    1 
ATOM   1781  C  C     . LYS A 1 221 ? 145.013 132.826 132.675 1.00 38.04 ?  221 LYS A C     1 
ATOM   1782  O  O     . LYS A 1 221 ? 144.557 131.783 132.192 1.00 43.49 ?  221 LYS A O     1 
ATOM   1783  C  CB    . LYS A 1 221 ? 143.142 133.337 134.234 1.00 33.02 ?  221 LYS A CB    1 
ATOM   1784  C  CG    . LYS A 1 221 ? 142.679 133.985 135.520 1.00 37.07 ?  221 LYS A CG    1 
ATOM   1785  C  CD    . LYS A 1 221 ? 141.183 133.820 135.700 1.00 36.66 ?  221 LYS A CD    1 
ATOM   1786  C  CE    . LYS A 1 221 ? 140.830 132.437 136.212 1.00 35.69 ?  221 LYS A CE    1 
ATOM   1787  N  NZ    . LYS A 1 221 ? 141.630 132.069 137.409 1.00 37.36 1  221 LYS A NZ    1 
ATOM   1788  N  N     . GLY A 1 222 ? 145.800 133.644 131.991 1.00 32.91 ?  222 GLY A N     1 
ATOM   1789  C  CA    . GLY A 1 222 ? 146.187 133.361 130.630 1.00 30.90 ?  222 GLY A CA    1 
ATOM   1790  C  C     . GLY A 1 222 ? 145.146 133.806 129.623 1.00 30.75 ?  222 GLY A C     1 
ATOM   1791  O  O     . GLY A 1 222 ? 144.157 134.471 129.942 1.00 31.07 ?  222 GLY A O     1 
ATOM   1792  N  N     . VAL A 1 223 ? 145.387 133.421 128.370 1.00 31.96 ?  223 VAL A N     1 
ATOM   1793  C  CA    . VAL A 1 223 ? 144.465 133.785 127.301 1.00 26.30 ?  223 VAL A CA    1 
ATOM   1794  C  C     . VAL A 1 223 ? 143.205 132.934 127.312 1.00 22.89 ?  223 VAL A C     1 
ATOM   1795  O  O     . VAL A 1 223 ? 142.218 133.307 126.674 1.00 31.06 ?  223 VAL A O     1 
ATOM   1796  C  CB    . VAL A 1 223 ? 145.141 133.689 125.921 1.00 25.90 ?  223 VAL A CB    1 
ATOM   1797  C  CG1   . VAL A 1 223 ? 146.475 134.412 125.930 1.00 25.11 ?  223 VAL A CG1   1 
ATOM   1798  C  CG2   . VAL A 1 223 ? 145.311 132.238 125.502 1.00 26.84 ?  223 VAL A CG2   1 
ATOM   1799  N  N     . VAL A 1 224 ? 143.206 131.803 128.018 1.00 25.50 ?  224 VAL A N     1 
ATOM   1800  C  CA    . VAL A 1 224 ? 142.030 130.938 128.027 1.00 25.72 ?  224 VAL A CA    1 
ATOM   1801  C  C     . VAL A 1 224 ? 140.899 131.540 128.858 1.00 27.40 ?  224 VAL A C     1 
ATOM   1802  O  O     . VAL A 1 224 ? 139.721 131.353 128.534 1.00 30.19 ?  224 VAL A O     1 
ATOM   1803  C  CB    . VAL A 1 224 ? 142.414 129.531 128.515 1.00 32.71 ?  224 VAL A CB    1 
ATOM   1804  C  CG1   . VAL A 1 224 ? 141.199 128.621 128.545 1.00 31.81 ?  224 VAL A CG1   1 
ATOM   1805  C  CG2   . VAL A 1 224 ? 143.486 128.947 127.615 1.00 29.46 ?  224 VAL A CG2   1 
ATOM   1806  N  N     . GLY A 1 225 ? 141.217 132.271 129.927 1.00 24.18 ?  225 GLY A N     1 
ATOM   1807  C  CA    . GLY A 1 225 ? 140.174 132.967 130.663 1.00 21.73 ?  225 GLY A CA    1 
ATOM   1808  C  C     . GLY A 1 225 ? 139.505 134.048 129.836 1.00 22.30 ?  225 GLY A C     1 
ATOM   1809  O  O     . GLY A 1 225 ? 138.275 134.179 129.837 1.00 31.46 ?  225 GLY A O     1 
ATOM   1810  N  N     . VAL A 1 226 ? 140.304 134.830 129.108 1.00 19.34 ?  226 VAL A N     1 
ATOM   1811  C  CA    . VAL A 1 226 ? 139.749 135.808 128.179 1.00 20.35 ?  226 VAL A CA    1 
ATOM   1812  C  C     . VAL A 1 226 ? 138.976 135.109 127.075 1.00 24.85 ?  226 VAL A C     1 
ATOM   1813  O  O     . VAL A 1 226 ? 137.975 135.633 126.578 1.00 26.82 ?  226 VAL A O     1 
ATOM   1814  C  CB    . VAL A 1 226 ? 140.874 136.695 127.612 1.00 18.19 ?  226 VAL A CB    1 
ATOM   1815  C  CG1   . VAL A 1 226 ? 140.293 137.833 126.786 1.00 25.76 ?  226 VAL A CG1   1 
ATOM   1816  C  CG2   . VAL A 1 226 ? 141.735 137.227 128.737 1.00 20.82 ?  226 VAL A CG2   1 
ATOM   1817  N  N     . MET A 1 227 ? 139.427 133.922 126.671 1.00 28.39 ?  227 MET A N     1 
ATOM   1818  C  CA    . MET A 1 227 ? 138.713 133.147 125.664 1.00 22.22 ?  227 MET A CA    1 
ATOM   1819  C  C     . MET A 1 227 ? 137.332 132.744 126.157 1.00 22.95 ?  227 MET A C     1 
ATOM   1820  O  O     . MET A 1 227 ? 136.355 132.812 125.408 1.00 29.97 ?  227 MET A O     1 
ATOM   1821  C  CB    . MET A 1 227 ? 139.535 131.913 125.295 1.00 19.68 ?  227 MET A CB    1 
ATOM   1822  C  CG    . MET A 1 227 ? 140.598 132.164 124.249 1.00 17.85 ?  227 MET A CG    1 
ATOM   1823  S  SD    . MET A 1 227 ? 141.272 130.635 123.586 1.00 33.28 ?  227 MET A SD    1 
ATOM   1824  C  CE    . MET A 1 227 ? 139.969 130.163 122.465 1.00 29.81 ?  227 MET A CE    1 
ATOM   1825  N  N     . LYS A 1 228 ? 137.234 132.313 127.416 1.00 26.79 ?  228 LYS A N     1 
ATOM   1826  C  CA    . LYS A 1 228 ? 135.933 131.978 127.991 1.00 23.10 ?  228 LYS A CA    1 
ATOM   1827  C  C     . LYS A 1 228 ? 135.045 133.212 128.100 1.00 24.38 ?  228 LYS A C     1 
ATOM   1828  O  O     . LYS A 1 228 ? 133.841 133.150 127.808 1.00 26.05 ?  228 LYS A O     1 
ATOM   1829  C  CB    . LYS A 1 228 ? 136.113 131.329 129.363 1.00 23.32 ?  228 LYS A CB    1 
ATOM   1830  C  CG    . LYS A 1 228 ? 136.893 130.029 129.337 1.00 29.04 ?  228 LYS A CG    1 
ATOM   1831  C  CD    . LYS A 1 228 ? 136.960 129.403 130.718 1.00 36.78 ?  228 LYS A CD    1 
ATOM   1832  C  CE    . LYS A 1 228 ? 138.093 129.992 131.542 1.00 36.15 ?  228 LYS A CE    1 
ATOM   1833  N  NZ    . LYS A 1 228 ? 139.252 129.063 131.642 1.00 30.76 1  228 LYS A NZ    1 
ATOM   1834  N  N     . LEU A 1 229 ? 135.624 134.339 128.523 1.00 24.46 ?  229 LEU A N     1 
ATOM   1835  C  CA    . LEU A 1 229 ? 134.871 135.588 128.573 1.00 21.84 ?  229 LEU A CA    1 
ATOM   1836  C  C     . LEU A 1 229 ? 134.309 135.944 127.202 1.00 21.51 ?  229 LEU A C     1 
ATOM   1837  O  O     . LEU A 1 229 ? 133.129 136.286 127.069 1.00 22.24 ?  229 LEU A O     1 
ATOM   1838  C  CB    . LEU A 1 229 ? 135.762 136.718 129.083 1.00 24.43 ?  229 LEU A CB    1 
ATOM   1839  C  CG    . LEU A 1 229 ? 136.145 136.769 130.560 1.00 23.02 ?  229 LEU A CG    1 
ATOM   1840  C  CD1   . LEU A 1 229 ? 137.287 137.746 130.736 1.00 24.40 ?  229 LEU A CD1   1 
ATOM   1841  C  CD2   . LEU A 1 229 ? 134.959 137.171 131.414 1.00 18.49 ?  229 LEU A CD2   1 
ATOM   1842  N  N     . LEU A 1 230 ? 135.147 135.863 126.168 1.00 26.92 ?  230 LEU A N     1 
ATOM   1843  C  CA    . LEU A 1 230 ? 134.716 136.201 124.816 1.00 18.66 ?  230 LEU A CA    1 
ATOM   1844  C  C     . LEU A 1 230 ? 133.690 135.205 124.295 1.00 17.88 ?  230 LEU A C     1 
ATOM   1845  O  O     . LEU A 1 230 ? 132.753 135.586 123.587 1.00 29.69 ?  230 LEU A O     1 
ATOM   1846  C  CB    . LEU A 1 230 ? 135.923 136.264 123.883 1.00 20.57 ?  230 LEU A CB    1 
ATOM   1847  C  CG    . LEU A 1 230 ? 136.832 137.479 124.052 1.00 27.78 ?  230 LEU A CG    1 
ATOM   1848  C  CD1   . LEU A 1 230 ? 138.170 137.240 123.374 1.00 28.12 ?  230 LEU A CD1   1 
ATOM   1849  C  CD2   . LEU A 1 230 ? 136.157 138.727 123.507 1.00 21.05 ?  230 LEU A CD2   1 
ATOM   1850  N  N     . ASP A 1 231 ? 133.856 133.925 124.625 1.00 20.37 ?  231 ASP A N     1 
ATOM   1851  C  CA    . ASP A 1 231 ? 132.898 132.918 124.190 1.00 24.19 ?  231 ASP A CA    1 
ATOM   1852  C  C     . ASP A 1 231 ? 131.521 133.183 124.779 1.00 28.73 ?  231 ASP A C     1 
ATOM   1853  O  O     . ASP A 1 231 ? 130.509 133.101 124.073 1.00 33.36 ?  231 ASP A O     1 
ATOM   1854  C  CB    . ASP A 1 231 ? 133.399 131.527 124.577 1.00 27.44 ?  231 ASP A CB    1 
ATOM   1855  C  CG    . ASP A 1 231 ? 132.450 130.427 124.157 1.00 35.91 ?  231 ASP A CG    1 
ATOM   1856  O  OD1   . ASP A 1 231 ? 132.303 130.201 122.939 1.00 39.62 ?  231 ASP A OD1   1 
ATOM   1857  O  OD2   . ASP A 1 231 ? 131.854 129.784 125.045 1.00 38.47 -1 231 ASP A OD2   1 
ATOM   1858  N  N     . ASN A 1 232 ? 131.459 133.529 126.066 1.00 29.49 ?  232 ASN A N     1 
ATOM   1859  C  CA    . ASN A 1 232 ? 130.164 133.861 126.653 1.00 27.94 ?  232 ASN A CA    1 
ATOM   1860  C  C     . ASN A 1 232 ? 129.628 135.192 126.144 1.00 28.52 ?  232 ASN A C     1 
ATOM   1861  O  O     . ASN A 1 232 ? 128.409 135.358 126.025 1.00 33.99 ?  232 ASN A O     1 
ATOM   1862  C  CB    . ASN A 1 232 ? 130.250 133.865 128.174 1.00 29.32 ?  232 ASN A CB    1 
ATOM   1863  C  CG    . ASN A 1 232 ? 130.103 132.483 128.755 1.00 36.30 ?  232 ASN A CG    1 
ATOM   1864  O  OD1   . ASN A 1 232 ? 130.991 131.642 128.625 1.00 38.87 ?  232 ASN A OD1   1 
ATOM   1865  N  ND2   . ASN A 1 232 ? 128.968 132.231 129.397 1.00 33.39 ?  232 ASN A ND2   1 
ATOM   1866  N  N     . ALA A 1 233 ? 130.509 136.144 125.835 1.00 25.87 ?  233 ALA A N     1 
ATOM   1867  C  CA    . ALA A 1 233 ? 130.057 137.402 125.254 1.00 17.88 ?  233 ALA A CA    1 
ATOM   1868  C  C     . ALA A 1 233 ? 129.430 137.180 123.884 1.00 30.07 ?  233 ALA A C     1 
ATOM   1869  O  O     . ALA A 1 233 ? 128.441 137.832 123.530 1.00 36.37 ?  233 ALA A O     1 
ATOM   1870  C  CB    . ALA A 1 233 ? 131.222 138.385 125.162 1.00 23.66 ?  233 ALA A CB    1 
ATOM   1871  N  N     . PHE A 1 234 ? 129.998 136.266 123.096 1.00 32.09 ?  234 PHE A N     1 
ATOM   1872  C  CA    . PHE A 1 234 ? 129.443 135.958 121.784 1.00 25.48 ?  234 PHE A CA    1 
ATOM   1873  C  C     . PHE A 1 234 ? 128.192 135.098 121.882 1.00 23.30 ?  234 PHE A C     1 
ATOM   1874  O  O     . PHE A 1 234 ? 127.297 135.218 121.039 1.00 29.86 ?  234 PHE A O     1 
ATOM   1875  C  CB    . PHE A 1 234 ? 130.501 135.276 120.918 1.00 24.96 ?  234 PHE A CB    1 
ATOM   1876  C  CG    . PHE A 1 234 ? 131.519 136.225 120.355 1.00 24.03 ?  234 PHE A CG    1 
ATOM   1877  C  CD1   . PHE A 1 234 ? 131.128 137.292 119.568 1.00 27.38 ?  234 PHE A CD1   1 
ATOM   1878  C  CD2   . PHE A 1 234 ? 132.864 136.059 120.625 1.00 23.01 ?  234 PHE A CD2   1 
ATOM   1879  C  CE1   . PHE A 1 234 ? 132.061 138.170 119.057 1.00 26.14 ?  234 PHE A CE1   1 
ATOM   1880  C  CE2   . PHE A 1 234 ? 133.800 136.936 120.121 1.00 24.47 ?  234 PHE A CE2   1 
ATOM   1881  C  CZ    . PHE A 1 234 ? 133.398 137.991 119.334 1.00 26.41 ?  234 PHE A CZ    1 
ATOM   1882  N  N     . ARG A 1 235 ? 128.108 134.226 122.887 1.00 31.26 ?  235 ARG A N     1 
ATOM   1883  C  CA    . ARG A 1 235 ? 126.859 133.512 123.128 1.00 26.90 ?  235 ARG A CA    1 
ATOM   1884  C  C     . ARG A 1 235 ? 125.742 134.459 123.540 1.00 32.93 ?  235 ARG A C     1 
ATOM   1885  O  O     . ARG A 1 235 ? 124.585 134.250 123.159 1.00 39.75 ?  235 ARG A O     1 
ATOM   1886  C  CB    . ARG A 1 235 ? 127.051 132.433 124.191 1.00 23.83 ?  235 ARG A CB    1 
ATOM   1887  C  CG    . ARG A 1 235 ? 126.953 131.025 123.647 1.00 35.16 ?  235 ARG A CG    1 
ATOM   1888  C  CD    . ARG A 1 235 ? 126.636 130.016 124.745 1.00 37.47 ?  235 ARG A CD    1 
ATOM   1889  N  NE    . ARG A 1 235 ? 127.539 130.086 125.890 1.00 36.06 ?  235 ARG A NE    1 
ATOM   1890  C  CZ    . ARG A 1 235 ? 128.851 129.906 125.836 1.00 36.85 ?  235 ARG A CZ    1 
ATOM   1891  N  NH1   . ARG A 1 235 ? 129.463 129.589 124.706 1.00 35.35 1  235 ARG A NH1   1 
ATOM   1892  N  NH2   . ARG A 1 235 ? 129.569 130.025 126.950 1.00 33.99 ?  235 ARG A NH2   1 
ATOM   1893  N  N     . TYR A 1 236 ? 126.058 135.491 124.322 1.00 29.33 ?  236 TYR A N     1 
ATOM   1894  C  CA    . TYR A 1 236 ? 125.029 136.433 124.744 1.00 27.39 ?  236 TYR A CA    1 
ATOM   1895  C  C     . TYR A 1 236 ? 124.521 137.260 123.569 1.00 26.88 ?  236 TYR A C     1 
ATOM   1896  O  O     . TYR A 1 236 ? 123.309 137.400 123.373 1.00 32.69 ?  236 TYR A O     1 
ATOM   1897  C  CB    . TYR A 1 236 ? 125.568 137.345 125.844 1.00 28.09 ?  236 TYR A CB    1 
ATOM   1898  C  CG    . TYR A 1 236 ? 124.527 138.286 126.391 1.00 29.84 ?  236 TYR A CG    1 
ATOM   1899  C  CD1   . TYR A 1 236 ? 123.509 137.817 127.208 1.00 26.03 ?  236 TYR A CD1   1 
ATOM   1900  C  CD2   . TYR A 1 236 ? 124.548 139.638 126.078 1.00 29.81 ?  236 TYR A CD2   1 
ATOM   1901  C  CE1   . TYR A 1 236 ? 122.553 138.664 127.706 1.00 30.09 ?  236 TYR A CE1   1 
ATOM   1902  C  CE2   . TYR A 1 236 ? 123.591 140.495 126.575 1.00 23.27 ?  236 TYR A CE2   1 
ATOM   1903  C  CZ    . TYR A 1 236 ? 122.597 140.000 127.390 1.00 24.22 ?  236 TYR A CZ    1 
ATOM   1904  O  OH    . TYR A 1 236 ? 121.635 140.838 127.894 1.00 29.49 ?  236 TYR A OH    1 
ATOM   1905  N  N     . ALA A 1 237 ? 125.434 137.818 122.775 1.00 30.76 ?  237 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 237 ? 125.063 138.640 121.624 1.00 33.92 ?  237 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 237 ? 124.934 137.727 120.408 1.00 38.01 ?  237 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 237 ? 125.868 137.530 119.629 1.00 37.56 ?  237 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 237 ? 126.082 139.749 121.402 1.00 31.93 ?  237 ALA A CB    1 
ATOM   1910  N  N     . ASP A 1 238 ? 123.742 137.156 120.255 1.00 54.09 ?  238 ASP A N     1 
ATOM   1911  C  CA    . ASP A 1 238 ? 123.479 136.169 119.218 1.00 57.14 ?  238 ASP A CA    1 
ATOM   1912  C  C     . ASP A 1 238 ? 122.374 136.579 118.254 1.00 59.65 ?  238 ASP A C     1 
ATOM   1913  O  O     . ASP A 1 238 ? 122.076 135.818 117.326 1.00 62.01 ?  238 ASP A O     1 
ATOM   1914  C  CB    . ASP A 1 238 ? 123.129 134.821 119.856 1.00 56.12 ?  238 ASP A CB    1 
ATOM   1915  C  CG    . ASP A 1 238 ? 121.901 134.898 120.738 1.00 59.17 ?  238 ASP A CG    1 
ATOM   1916  O  OD1   . ASP A 1 238 ? 121.541 136.014 121.167 1.00 58.79 ?  238 ASP A OD1   1 
ATOM   1917  O  OD2   . ASP A 1 238 ? 121.292 133.840 121.003 1.00 61.73 -1 238 ASP A OD2   1 
ATOM   1918  N  N     . GLN A 1 239 ? 121.759 137.748 118.444 1.00 61.84 ?  239 GLN A N     1 
ATOM   1919  C  CA    . GLN A 1 239 ? 120.743 138.280 117.535 1.00 63.57 ?  239 GLN A CA    1 
ATOM   1920  C  C     . GLN A 1 239 ? 119.590 137.285 117.362 1.00 64.40 ?  239 GLN A C     1 
ATOM   1921  O  O     . GLN A 1 239 ? 119.393 136.698 116.295 1.00 64.50 ?  239 GLN A O     1 
ATOM   1922  C  CB    . GLN A 1 239 ? 121.353 138.637 116.174 1.00 62.58 ?  239 GLN A CB    1 
ATOM   1923  C  CG    . GLN A 1 239 ? 122.741 139.242 116.232 1.00 60.47 ?  239 GLN A CG    1 
ATOM   1924  C  CD    . GLN A 1 239 ? 123.494 139.043 114.934 1.00 63.61 ?  239 GLN A CD    1 
ATOM   1925  O  OE1   . GLN A 1 239 ? 124.652 138.625 114.930 1.00 63.04 ?  239 GLN A OE1   1 
ATOM   1926  N  NE2   . GLN A 1 239 ? 122.837 139.340 113.820 1.00 62.96 ?  239 GLN A NE2   1 
ATOM   1927  N  N     . MET A 1 240 ? 118.869 137.075 118.469 1.00 72.88 ?  240 MET A N     1 
ATOM   1928  C  CA    . MET A 1 240 ? 117.738 136.149 118.542 1.00 74.86 ?  240 MET A CA    1 
ATOM   1929  C  C     . MET A 1 240 ? 118.186 134.692 118.507 1.00 74.66 ?  240 MET A C     1 
ATOM   1930  O  O     . MET A 1 240 ? 117.377 133.783 118.718 1.00 76.79 ?  240 MET A O     1 
ATOM   1931  C  CB    . MET A 1 240 ? 116.738 136.404 117.404 1.00 75.37 ?  240 MET A CB    1 
ATOM   1932  C  CG    . MET A 1 240 ? 115.356 135.811 117.620 1.00 74.25 ?  240 MET A CG    1 
ATOM   1933  S  SD    . MET A 1 240 ? 113.989 136.928 117.293 1.00 82.10 ?  240 MET A SD    1 
ATOM   1934  C  CE    . MET A 1 240 ? 112.616 135.785 117.443 1.00 74.95 ?  240 MET A CE    1 
ATOM   1935  N  N     . GLY A 1 241 ? 119.471 134.455 118.267 1.00 73.27 ?  241 GLY A N     1 
ATOM   1936  C  CA    . GLY A 1 241 ? 119.950 133.113 118.032 1.00 72.70 ?  241 GLY A CA    1 
ATOM   1937  C  C     . GLY A 1 241 ? 119.737 132.612 116.621 1.00 75.66 ?  241 GLY A C     1 
ATOM   1938  O  O     . GLY A 1 241 ? 120.138 131.480 116.318 1.00 74.83 ?  241 GLY A O     1 
ATOM   1939  N  N     . GLN A 1 242 ? 119.112 133.413 115.753 1.00 79.13 ?  242 GLN A N     1 
ATOM   1940  C  CA    . GLN A 1 242 ? 118.963 133.027 114.353 1.00 78.63 ?  242 GLN A CA    1 
ATOM   1941  C  C     . GLN A 1 242 ? 120.325 132.805 113.712 1.00 80.35 ?  242 GLN A C     1 
ATOM   1942  O  O     . GLN A 1 242 ? 120.554 131.799 113.032 1.00 79.65 ?  242 GLN A O     1 
ATOM   1943  C  CB    . GLN A 1 242 ? 118.183 134.103 113.596 1.00 77.99 ?  242 GLN A CB    1 
ATOM   1944  C  CG    . GLN A 1 242 ? 116.675 134.035 113.768 1.00 79.49 ?  242 GLN A CG    1 
ATOM   1945  C  CD    . GLN A 1 242 ? 115.938 134.892 112.756 1.00 79.66 ?  242 GLN A CD    1 
ATOM   1946  O  OE1   . GLN A 1 242 ? 116.552 135.522 111.895 1.00 78.67 ?  242 GLN A OE1   1 
ATOM   1947  N  NE2   . GLN A 1 242 ? 114.614 134.922 112.857 1.00 79.18 ?  242 GLN A NE2   1 
ATOM   1948  N  N     . ARG A 1 243 ? 121.246 133.743 113.926 1.00 67.57 ?  243 ARG A N     1 
ATOM   1949  C  CA    . ARG A 1 243 ? 122.657 133.569 113.608 1.00 64.53 ?  243 ARG A CA    1 
ATOM   1950  C  C     . ARG A 1 243 ? 123.433 133.898 114.874 1.00 65.13 ?  243 ARG A C     1 
ATOM   1951  O  O     . ARG A 1 243 ? 123.663 135.074 115.174 1.00 64.19 ?  243 ARG A O     1 
ATOM   1952  C  CB    . ARG A 1 243 ? 123.090 134.467 112.448 1.00 63.99 ?  243 ARG A CB    1 
ATOM   1953  C  CG    . ARG A 1 243 ? 124.503 134.195 111.958 1.00 65.11 ?  243 ARG A CG    1 
ATOM   1954  C  CD    . ARG A 1 243 ? 125.302 135.481 111.828 1.00 63.87 ?  243 ARG A CD    1 
ATOM   1955  N  NE    . ARG A 1 243 ? 125.621 136.050 113.131 1.00 65.64 ?  243 ARG A NE    1 
ATOM   1956  C  CZ    . ARG A 1 243 ? 126.698 136.781 113.388 1.00 62.31 ?  243 ARG A CZ    1 
ATOM   1957  N  NH1   . ARG A 1 243 ? 127.592 137.047 112.449 1.00 61.32 1  243 ARG A NH1   1 
ATOM   1958  N  NH2   . ARG A 1 243 ? 126.883 137.254 114.616 1.00 59.64 ?  243 ARG A NH2   1 
ATOM   1959  N  N     . GLN A 1 244 ? 123.829 132.863 115.614 1.00 62.49 ?  244 GLN A N     1 
ATOM   1960  C  CA    . GLN A 1 244 ? 124.484 133.069 116.897 1.00 60.92 ?  244 GLN A CA    1 
ATOM   1961  C  C     . GLN A 1 244 ? 125.793 133.827 116.718 1.00 61.50 ?  244 GLN A C     1 
ATOM   1962  O  O     . GLN A 1 244 ? 126.407 133.811 115.646 1.00 59.07 ?  244 GLN A O     1 
ATOM   1963  C  CB    . GLN A 1 244 ? 124.740 131.727 117.589 1.00 59.61 ?  244 GLN A CB    1 
ATOM   1964  C  CG    . GLN A 1 244 ? 125.991 131.001 117.122 1.00 61.35 ?  244 GLN A CG    1 
ATOM   1965  C  CD    . GLN A 1 244 ? 125.878 130.494 115.698 1.00 63.43 ?  244 GLN A CD    1 
ATOM   1966  O  OE1   . GLN A 1 244 ? 124.778 130.269 115.192 1.00 62.60 ?  244 GLN A OE1   1 
ATOM   1967  N  NE2   . GLN A 1 244 ? 127.018 130.314 115.040 1.00 60.79 ?  244 GLN A NE2   1 
ATOM   1968  N  N     . GLY A 1 245 ? 126.208 134.516 117.779 1.00 51.77 ?  245 GLY A N     1 
ATOM   1969  C  CA    . GLY A 1 245 ? 127.416 135.314 117.737 1.00 44.75 ?  245 GLY A CA    1 
ATOM   1970  C  C     . GLY A 1 245 ? 128.640 134.498 117.388 1.00 44.79 ?  245 GLY A C     1 
ATOM   1971  O  O     . GLY A 1 245 ? 128.941 133.496 118.044 1.00 45.23 ?  245 GLY A O     1 
ATOM   1972  N  N     . SER A 1 246 ? 129.354 134.918 116.349 1.00 39.42 ?  246 SER A N     1 
ATOM   1973  C  CA    . SER A 1 246 ? 130.524 134.209 115.856 1.00 34.17 ?  246 SER A CA    1 
ATOM   1974  C  C     . SER A 1 246 ? 131.767 135.035 116.140 1.00 31.18 ?  246 SER A C     1 
ATOM   1975  O  O     . SER A 1 246 ? 131.858 136.196 115.725 1.00 27.05 ?  246 SER A O     1 
ATOM   1976  C  CB    . SER A 1 246 ? 130.403 133.926 114.359 1.00 31.85 ?  246 SER A CB    1 
ATOM   1977  O  OG    . SER A 1 246 ? 129.398 132.963 114.102 1.00 41.80 ?  246 SER A OG    1 
ATOM   1978  N  N     . GLY A 1 247 ? 132.721 134.434 116.846 1.00 24.77 ?  247 GLY A N     1 
ATOM   1979  C  CA    . GLY A 1 247 ? 133.966 135.096 117.148 1.00 11.06 ?  247 GLY A CA    1 
ATOM   1980  C  C     . GLY A 1 247 ? 135.145 134.213 116.790 1.00 15.76 ?  247 GLY A C     1 
ATOM   1981  O  O     . GLY A 1 247 ? 135.031 132.993 116.683 1.00 22.75 ?  247 GLY A O     1 
ATOM   1982  N  N     . ALA A 1 248 ? 136.285 134.863 116.593 1.00 19.37 ?  248 ALA A N     1 
ATOM   1983  C  CA    . ALA A 1 248 ? 137.542 134.181 116.347 1.00 16.42 ?  248 ALA A CA    1 
ATOM   1984  C  C     . ALA A 1 248 ? 138.606 134.764 117.261 1.00 12.25 ?  248 ALA A C     1 
ATOM   1985  O  O     . ALA A 1 248 ? 138.643 135.974 117.491 1.00 20.81 ?  248 ALA A O     1 
ATOM   1986  C  CB    . ALA A 1 248 ? 137.981 134.303 114.884 1.00 9.18  ?  248 ALA A CB    1 
ATOM   1987  N  N     . ALA A 1 249 ? 139.458 133.896 117.789 1.00 17.17 ?  249 ALA A N     1 
ATOM   1988  C  CA    . ALA A 1 249 ? 140.600 134.304 118.590 1.00 11.41 ?  249 ALA A CA    1 
ATOM   1989  C  C     . ALA A 1 249 ? 141.872 133.867 117.885 1.00 10.22 ?  249 ALA A C     1 
ATOM   1990  O  O     . ALA A 1 249 ? 141.942 132.765 117.338 1.00 19.58 ?  249 ALA A O     1 
ATOM   1991  C  CB    . ALA A 1 249 ? 140.541 133.707 119.997 1.00 13.14 ?  249 ALA A CB    1 
ATOM   1992  N  N     . TYR A 1 250 ? 142.872 134.737 117.886 1.00 11.19 ?  250 TYR A N     1 
ATOM   1993  C  CA    . TYR A 1 250 ? 144.146 134.444 117.254 1.00 7.84  ?  250 TYR A CA    1 
ATOM   1994  C  C     . TYR A 1 250 ? 145.260 134.540 118.281 1.00 8.84  ?  250 TYR A C     1 
ATOM   1995  O  O     . TYR A 1 250 ? 145.283 135.458 119.106 1.00 13.20 ?  250 TYR A O     1 
ATOM   1996  C  CB    . TYR A 1 250 ? 144.421 135.392 116.086 1.00 10.59 ?  250 TYR A CB    1 
ATOM   1997  C  CG    . TYR A 1 250 ? 143.787 134.953 114.788 1.00 19.08 ?  250 TYR A CG    1 
ATOM   1998  C  CD1   . TYR A 1 250 ? 142.436 135.159 114.550 1.00 8.70  ?  250 TYR A CD1   1 
ATOM   1999  C  CD2   . TYR A 1 250 ? 144.535 134.317 113.806 1.00 12.91 ?  250 TYR A CD2   1 
ATOM   2000  C  CE1   . TYR A 1 250 ? 141.852 134.755 113.371 1.00 0.00  ?  250 TYR A CE1   1 
ATOM   2001  C  CE2   . TYR A 1 250 ? 143.957 133.911 112.623 1.00 7.59  ?  250 TYR A CE2   1 
ATOM   2002  C  CZ    . TYR A 1 250 ? 142.615 134.132 112.412 1.00 7.54  ?  250 TYR A CZ    1 
ATOM   2003  O  OH    . TYR A 1 250 ? 142.028 133.731 111.235 1.00 22.46 ?  250 TYR A OH    1 
ATOM   2004  N  N     . LEU A 1 251 ? 146.175 133.581 118.230 1.00 10.93 ?  251 LEU A N     1 
ATOM   2005  C  CA    . LEU A 1 251 ? 147.332 133.554 119.108 1.00 12.86 ?  251 LEU A CA    1 
ATOM   2006  C  C     . LEU A 1 251 ? 148.576 133.247 118.296 1.00 11.61 ?  251 LEU A C     1 
ATOM   2007  O  O     . LEU A 1 251 ? 148.565 132.363 117.435 1.00 17.27 ?  251 LEU A O     1 
ATOM   2008  C  CB    . LEU A 1 251 ? 147.168 132.513 120.216 1.00 18.54 ?  251 LEU A CB    1 
ATOM   2009  C  CG    . LEU A 1 251 ? 147.928 132.816 121.506 1.00 14.33 ?  251 LEU A CG    1 
ATOM   2010  C  CD1   . LEU A 1 251 ? 147.206 133.879 122.305 1.00 16.35 ?  251 LEU A CD1   1 
ATOM   2011  C  CD2   . LEU A 1 251 ? 148.108 131.559 122.326 1.00 13.33 ?  251 LEU A CD2   1 
ATOM   2012  N  N     . ASN A 1 252 ? 149.645 133.990 118.563 1.00 12.05 ?  252 ASN A N     1 
ATOM   2013  C  CA    . ASN A 1 252 ? 150.933 133.677 117.966 1.00 12.86 ?  252 ASN A CA    1 
ATOM   2014  C  C     . ASN A 1 252 ? 151.436 132.343 118.501 1.00 17.68 ?  252 ASN A C     1 
ATOM   2015  O  O     . ASN A 1 252 ? 151.262 132.021 119.678 1.00 23.42 ?  252 ASN A O     1 
ATOM   2016  C  CB    . ASN A 1 252 ? 151.939 134.788 118.261 1.00 15.86 ?  252 ASN A CB    1 
ATOM   2017  C  CG    . ASN A 1 252 ? 153.191 134.679 117.418 1.00 20.25 ?  252 ASN A CG    1 
ATOM   2018  O  OD1   . ASN A 1 252 ? 154.153 134.018 117.801 1.00 25.80 ?  252 ASN A OD1   1 
ATOM   2019  N  ND2   . ASN A 1 252 ? 153.182 135.324 116.260 1.00 15.68 ?  252 ASN A ND2   1 
ATOM   2020  N  N     . ILE A 1 253 ? 152.060 131.558 117.619 1.00 15.99 ?  253 ILE A N     1 
ATOM   2021  C  CA    . ILE A 1 253 ? 152.512 130.225 117.999 1.00 14.48 ?  253 ILE A CA    1 
ATOM   2022  C  C     . ILE A 1 253 ? 153.602 130.277 119.063 1.00 19.81 ?  253 ILE A C     1 
ATOM   2023  O  O     . ILE A 1 253 ? 153.834 129.280 119.755 1.00 23.62 ?  253 ILE A O     1 
ATOM   2024  C  CB    . ILE A 1 253 ? 152.984 129.456 116.749 1.00 17.64 ?  253 ILE A CB    1 
ATOM   2025  C  CG1   . ILE A 1 253 ? 153.036 127.954 117.030 1.00 19.79 ?  253 ILE A CG1   1 
ATOM   2026  C  CG2   . ILE A 1 253 ? 154.335 129.969 116.276 1.00 14.47 ?  253 ILE A CG2   1 
ATOM   2027  C  CD1   . ILE A 1 253 ? 152.515 127.106 115.900 1.00 16.32 ?  253 ILE A CD1   1 
ATOM   2028  N  N     . PHE A 1 254 ? 154.268 131.417 119.225 1.00 23.04 ?  254 PHE A N     1 
ATOM   2029  C  CA    . PHE A 1 254 ? 155.309 131.577 120.230 1.00 20.04 ?  254 PHE A CA    1 
ATOM   2030  C  C     . PHE A 1 254 ? 154.775 132.092 121.558 1.00 19.83 ?  254 PHE A C     1 
ATOM   2031  O  O     . PHE A 1 254 ? 155.559 132.304 122.487 1.00 29.11 ?  254 PHE A O     1 
ATOM   2032  C  CB    . PHE A 1 254 ? 156.402 132.512 119.706 1.00 23.31 ?  254 PHE A CB    1 
ATOM   2033  C  CG    . PHE A 1 254 ? 157.360 131.847 118.764 1.00 23.76 ?  254 PHE A CG    1 
ATOM   2034  C  CD1   . PHE A 1 254 ? 158.217 130.859 119.212 1.00 25.73 ?  254 PHE A CD1   1 
ATOM   2035  C  CD2   . PHE A 1 254 ? 157.391 132.197 117.426 1.00 24.41 ?  254 PHE A CD2   1 
ATOM   2036  C  CE1   . PHE A 1 254 ? 159.097 130.242 118.347 1.00 24.63 ?  254 PHE A CE1   1 
ATOM   2037  C  CE2   . PHE A 1 254 ? 158.269 131.581 116.557 1.00 28.73 ?  254 PHE A CE2   1 
ATOM   2038  C  CZ    . PHE A 1 254 ? 159.124 130.603 117.019 1.00 26.32 ?  254 PHE A CZ    1 
ATOM   2039  N  N     . HIS A 1 255 ? 153.468 132.309 121.664 1.00 22.21 ?  255 HIS A N     1 
ATOM   2040  C  CA    . HIS A 1 255 ? 152.851 132.596 122.950 1.00 22.02 ?  255 HIS A CA    1 
ATOM   2041  C  C     . HIS A 1 255 ? 152.936 131.366 123.843 1.00 23.79 ?  255 HIS A C     1 
ATOM   2042  O  O     . HIS A 1 255 ? 152.797 130.233 123.379 1.00 27.87 ?  255 HIS A O     1 
ATOM   2043  C  CB    . HIS A 1 255 ? 151.393 133.007 122.748 1.00 23.90 ?  255 HIS A CB    1 
ATOM   2044  C  CG    . HIS A 1 255 ? 150.806 133.766 123.898 1.00 19.97 ?  255 HIS A CG    1 
ATOM   2045  N  ND1   . HIS A 1 255 ? 150.426 133.160 125.075 1.00 16.34 ?  255 HIS A ND1   1 
ATOM   2046  C  CD2   . HIS A 1 255 ? 150.504 135.078 124.036 1.00 17.37 ?  255 HIS A CD2   1 
ATOM   2047  C  CE1   . HIS A 1 255 ? 149.933 134.069 125.897 1.00 17.98 ?  255 HIS A CE1   1 
ATOM   2048  N  NE2   . HIS A 1 255 ? 149.967 135.241 125.290 1.00 17.01 ?  255 HIS A NE2   1 
ATOM   2049  N  N     . ARG A 1 256 ? 153.181 131.592 125.135 1.00 23.57 ?  256 ARG A N     1 
ATOM   2050  C  CA    . ARG A 1 256 ? 153.300 130.473 126.064 1.00 26.08 ?  256 ARG A CA    1 
ATOM   2051  C  C     . ARG A 1 256 ? 151.995 129.696 126.183 1.00 25.39 ?  256 ARG A C     1 
ATOM   2052  O  O     . ARG A 1 256 ? 152.013 128.476 126.375 1.00 31.14 ?  256 ARG A O     1 
ATOM   2053  C  CB    . ARG A 1 256 ? 153.744 130.975 127.436 1.00 28.03 ?  256 ARG A CB    1 
ATOM   2054  C  CG    . ARG A 1 256 ? 153.997 129.870 128.437 1.00 29.43 ?  256 ARG A CG    1 
ATOM   2055  C  CD    . ARG A 1 256 ? 153.071 129.981 129.633 1.00 29.65 ?  256 ARG A CD    1 
ATOM   2056  N  NE    . ARG A 1 256 ? 151.803 129.295 129.424 1.00 31.35 ?  256 ARG A NE    1 
ATOM   2057  C  CZ    . ARG A 1 256 ? 151.551 128.055 129.814 1.00 34.72 ?  256 ARG A CZ    1 
ATOM   2058  N  NH1   . ARG A 1 256 ? 152.465 127.328 130.436 1.00 33.44 1  256 ARG A NH1   1 
ATOM   2059  N  NH2   . ARG A 1 256 ? 150.354 127.529 129.575 1.00 30.56 ?  256 ARG A NH2   1 
ATOM   2060  N  N     . ASP A 1 257 ? 150.859 130.378 126.063 1.00 23.03 ?  257 ASP A N     1 
ATOM   2061  C  CA    . ASP A 1 257 ? 149.550 129.756 126.191 1.00 19.77 ?  257 ASP A CA    1 
ATOM   2062  C  C     . ASP A 1 257 ? 149.103 129.030 124.933 1.00 23.50 ?  257 ASP A C     1 
ATOM   2063  O  O     . ASP A 1 257 ? 147.915 128.715 124.824 1.00 29.98 ?  257 ASP A O     1 
ATOM   2064  C  CB    . ASP A 1 257 ? 148.501 130.807 126.561 1.00 25.21 ?  257 ASP A CB    1 
ATOM   2065  C  CG    . ASP A 1 257 ? 148.608 131.260 127.997 1.00 31.90 ?  257 ASP A CG    1 
ATOM   2066  O  OD1   . ASP A 1 257 ? 149.324 130.606 128.783 1.00 32.69 ?  257 ASP A OD1   1 
ATOM   2067  O  OD2   . ASP A 1 257 ? 147.968 132.270 128.340 1.00 32.98 -1 257 ASP A OD2   1 
ATOM   2068  N  N     . ILE A 1 258 ? 150.007 128.755 123.990 1.00 24.69 ?  258 ILE A N     1 
ATOM   2069  C  CA    . ILE A 1 258 ? 149.589 128.200 122.706 1.00 21.61 ?  258 ILE A CA    1 
ATOM   2070  C  C     . ILE A 1 258 ? 148.994 126.808 122.884 1.00 20.20 ?  258 ILE A C     1 
ATOM   2071  O  O     . ILE A 1 258 ? 148.013 126.452 122.222 1.00 27.04 ?  258 ILE A O     1 
ATOM   2072  C  CB    . ILE A 1 258 ? 150.764 128.204 121.707 1.00 24.23 ?  258 ILE A CB    1 
ATOM   2073  C  CG1   . ILE A 1 258 ? 150.297 127.732 120.328 1.00 22.62 ?  258 ILE A CG1   1 
ATOM   2074  C  CG2   . ILE A 1 258 ? 151.930 127.362 122.212 1.00 17.77 ?  258 ILE A CG2   1 
ATOM   2075  C  CD1   . ILE A 1 258 ? 149.284 128.648 119.679 1.00 17.72 ?  258 ILE A CD1   1 
ATOM   2076  N  N     . ASN A 1 259 ? 149.564 126.001 123.781 1.00 31.20 ?  259 ASN A N     1 
ATOM   2077  C  CA    . ASN A 1 259 ? 149.044 124.654 123.987 1.00 25.53 ?  259 ASN A CA    1 
ATOM   2078  C  C     . ASN A 1 259 ? 147.680 124.684 124.665 1.00 29.96 ?  259 ASN A C     1 
ATOM   2079  O  O     . ASN A 1 259 ? 146.778 123.931 124.285 1.00 34.90 ?  259 ASN A O     1 
ATOM   2080  C  CB    . ASN A 1 259 ? 150.040 123.831 124.798 1.00 30.04 ?  259 ASN A CB    1 
ATOM   2081  C  CG    . ASN A 1 259 ? 151.332 123.583 124.048 1.00 34.90 ?  259 ASN A CG    1 
ATOM   2082  O  OD1   . ASN A 1 259 ? 151.351 122.887 123.036 1.00 34.38 ?  259 ASN A OD1   1 
ATOM   2083  N  ND2   . ASN A 1 259 ? 152.422 124.158 124.542 1.00 36.03 ?  259 ASN A ND2   1 
ATOM   2084  N  N     . ASP A 1 260 ? 147.508 125.547 125.670 1.00 29.27 ?  260 ASP A N     1 
ATOM   2085  C  CA    . ASP A 1 260 ? 146.191 125.720 126.270 1.00 25.18 ?  260 ASP A CA    1 
ATOM   2086  C  C     . ASP A 1 260 ? 145.219 126.369 125.296 1.00 26.78 ?  260 ASP A C     1 
ATOM   2087  O  O     . ASP A 1 260 ? 144.019 126.077 125.330 1.00 35.48 ?  260 ASP A O     1 
ATOM   2088  C  CB    . ASP A 1 260 ? 146.297 126.553 127.546 1.00 27.48 ?  260 ASP A CB    1 
ATOM   2089  C  CG    . ASP A 1 260 ? 147.427 126.099 128.447 1.00 39.93 ?  260 ASP A CG    1 
ATOM   2090  O  OD1   . ASP A 1 260 ? 147.571 124.877 128.656 1.00 37.41 ?  260 ASP A OD1   1 
ATOM   2091  O  OD2   . ASP A 1 260 ? 148.175 126.968 128.944 1.00 39.68 -1 260 ASP A OD2   1 
ATOM   2092  N  N     . PHE A 1 261 ? 145.717 127.260 124.436 1.00 31.54 ?  261 PHE A N     1 
ATOM   2093  C  CA    . PHE A 1 261 ? 144.884 127.865 123.403 1.00 22.38 ?  261 PHE A CA    1 
ATOM   2094  C  C     . PHE A 1 261 ? 144.345 126.806 122.452 1.00 21.58 ?  261 PHE A C     1 
ATOM   2095  O  O     . PHE A 1 261 ? 143.173 126.848 122.061 1.00 24.08 ?  261 PHE A O     1 
ATOM   2096  C  CB    . PHE A 1 261 ? 145.702 128.918 122.653 1.00 15.65 ?  261 PHE A CB    1 
ATOM   2097  C  CG    . PHE A 1 261 ? 144.983 129.568 121.506 1.00 22.10 ?  261 PHE A CG    1 
ATOM   2098  C  CD1   . PHE A 1 261 ? 144.139 130.641 121.724 1.00 20.48 ?  261 PHE A CD1   1 
ATOM   2099  C  CD2   . PHE A 1 261 ? 145.190 129.139 120.208 1.00 24.42 ?  261 PHE A CD2   1 
ATOM   2100  C  CE1   . PHE A 1 261 ? 143.491 131.252 120.674 1.00 14.82 ?  261 PHE A CE1   1 
ATOM   2101  C  CE2   . PHE A 1 261 ? 144.543 129.749 119.154 1.00 20.16 ?  261 PHE A CE2   1 
ATOM   2102  C  CZ    . PHE A 1 261 ? 143.695 130.808 119.389 1.00 14.38 ?  261 PHE A CZ    1 
ATOM   2103  N  N     . LEU A 1 262 ? 145.188 125.844 122.073 1.00 26.28 ?  262 LEU A N     1 
ATOM   2104  C  CA    . LEU A 1 262 ? 144.759 124.760 121.198 1.00 22.74 ?  262 LEU A CA    1 
ATOM   2105  C  C     . LEU A 1 262 ? 143.911 123.727 121.927 1.00 30.54 ?  262 LEU A C     1 
ATOM   2106  O  O     . LEU A 1 262 ? 143.050 123.093 121.306 1.00 34.37 ?  262 LEU A O     1 
ATOM   2107  C  CB    . LEU A 1 262 ? 145.975 124.080 120.570 1.00 26.69 ?  262 LEU A CB    1 
ATOM   2108  C  CG    . LEU A 1 262 ? 146.848 124.952 119.672 1.00 23.46 ?  262 LEU A CG    1 
ATOM   2109  C  CD1   . LEU A 1 262 ? 148.105 124.202 119.278 1.00 24.29 ?  262 LEU A CD1   1 
ATOM   2110  C  CD2   . LEU A 1 262 ? 146.077 125.402 118.447 1.00 22.16 ?  262 LEU A CD2   1 
ATOM   2111  N  N     . ASP A 1 263 ? 144.134 123.536 123.228 1.00 38.57 ?  263 ASP A N     1 
ATOM   2112  C  CA    . ASP A 1 263 ? 143.371 122.553 123.988 1.00 30.89 ?  263 ASP A CA    1 
ATOM   2113  C  C     . ASP A 1 263 ? 141.914 122.948 124.175 1.00 32.35 ?  263 ASP A C     1 
ATOM   2114  O  O     . ASP A 1 263 ? 141.113 122.105 124.593 1.00 41.94 ?  263 ASP A O     1 
ATOM   2115  C  CB    . ASP A 1 263 ? 144.016 122.319 125.353 1.00 33.94 ?  263 ASP A CB    1 
ATOM   2116  C  CG    . ASP A 1 263 ? 145.304 121.528 125.264 1.00 40.92 ?  263 ASP A CG    1 
ATOM   2117  O  OD1   . ASP A 1 263 ? 145.540 120.894 124.214 1.00 37.88 ?  263 ASP A OD1   1 
ATOM   2118  O  OD2   . ASP A 1 263 ? 146.079 121.541 126.242 1.00 42.51 -1 263 ASP A OD2   1 
ATOM   2119  N  N     . THR A 1 264 ? 141.550 124.199 123.889 1.00 37.53 ?  264 THR A N     1 
ATOM   2120  C  CA    . THR A 1 264 ? 140.153 124.608 123.955 1.00 36.65 ?  264 THR A CA    1 
ATOM   2121  C  C     . THR A 1 264 ? 139.311 123.996 122.845 1.00 38.27 ?  264 THR A C     1 
ATOM   2122  O  O     . THR A 1 264 ? 138.080 124.045 122.928 1.00 42.43 ?  264 THR A O     1 
ATOM   2123  C  CB    . THR A 1 264 ? 140.046 126.134 123.895 1.00 37.79 ?  264 THR A CB    1 
ATOM   2124  O  OG1   . THR A 1 264 ? 140.607 126.609 122.665 1.00 41.67 ?  264 THR A OG1   1 
ATOM   2125  C  CG2   . THR A 1 264 ? 140.788 126.766 125.060 1.00 33.19 ?  264 THR A CG2   1 
ATOM   2126  N  N     . LYS A 1 265 ? 139.937 123.422 121.819 1.00 34.74 ?  265 LYS A N     1 
ATOM   2127  C  CA    . LYS A 1 265 ? 139.224 122.822 120.702 1.00 38.69 ?  265 LYS A CA    1 
ATOM   2128  C  C     . LYS A 1 265 ? 139.280 121.302 120.701 1.00 38.10 ?  265 LYS A C     1 
ATOM   2129  O  O     . LYS A 1 265 ? 138.672 120.676 119.826 1.00 42.13 ?  265 LYS A O     1 
ATOM   2130  C  CB    . LYS A 1 265 ? 139.776 123.355 119.376 1.00 37.22 ?  265 LYS A CB    1 
ATOM   2131  C  CG    . LYS A 1 265 ? 139.262 124.729 119.006 1.00 37.99 ?  265 LYS A CG    1 
ATOM   2132  C  CD    . LYS A 1 265 ? 137.775 124.840 119.261 1.00 38.69 ?  265 LYS A CD    1 
ATOM   2133  C  CE    . LYS A 1 265 ? 137.247 126.180 118.807 1.00 36.61 ?  265 LYS A CE    1 
ATOM   2134  N  NZ    . LYS A 1 265 ? 135.867 126.421 119.304 1.00 42.06 1  265 LYS A NZ    1 
ATOM   2135  N  N     . LYS A 1 266 ? 139.990 120.693 121.645 1.00 40.85 ?  266 LYS A N     1 
ATOM   2136  C  CA    . LYS A 1 266 ? 140.021 119.242 121.728 1.00 45.78 ?  266 LYS A CA    1 
ATOM   2137  C  C     . LYS A 1 266 ? 138.649 118.702 122.113 1.00 51.25 ?  266 LYS A C     1 
ATOM   2138  O  O     . LYS A 1 266 ? 137.900 119.321 122.874 1.00 51.79 ?  266 LYS A O     1 
ATOM   2139  C  CB    . LYS A 1 266 ? 141.071 118.784 122.739 1.00 44.22 ?  266 LYS A CB    1 
ATOM   2140  C  CG    . LYS A 1 266 ? 142.487 118.771 122.192 1.00 46.23 ?  266 LYS A CG    1 
ATOM   2141  C  CD    . LYS A 1 266 ? 143.481 118.284 123.231 1.00 48.71 ?  266 LYS A CD    1 
ATOM   2142  C  CE    . LYS A 1 266 ? 144.833 117.991 122.601 1.00 49.28 ?  266 LYS A CE    1 
ATOM   2143  N  NZ    . LYS A 1 266 ? 145.915 117.883 123.619 1.00 47.87 1  266 LYS A NZ    1 
ATOM   2144  N  N     . ILE A 1 267 ? 138.318 117.532 121.564 1.00 54.28 ?  267 ILE A N     1 
ATOM   2145  C  CA    . ILE A 1 267 ? 137.027 116.914 121.853 1.00 55.14 ?  267 ILE A CA    1 
ATOM   2146  C  C     . ILE A 1 267 ? 136.934 116.527 123.324 1.00 57.07 ?  267 ILE A C     1 
ATOM   2147  O  O     . ILE A 1 267 ? 135.861 116.605 123.932 1.00 54.69 ?  267 ILE A O     1 
ATOM   2148  C  CB    . ILE A 1 267 ? 136.798 115.707 120.926 1.00 55.54 ?  267 ILE A CB    1 
ATOM   2149  C  CG1   . ILE A 1 267 ? 138.071 114.862 120.825 1.00 57.04 ?  267 ILE A CG1   1 
ATOM   2150  C  CG2   . ILE A 1 267 ? 136.346 116.170 119.551 1.00 55.23 ?  267 ILE A CG2   1 
ATOM   2151  C  CD1   . ILE A 1 267 ? 137.914 113.618 119.983 1.00 55.54 ?  267 ILE A CD1   1 
ATOM   2152  N  N     . SER A 1 268 ? 138.051 116.111 123.919 1.00 60.16 ?  268 SER A N     1 
ATOM   2153  C  CA    . SER A 1 268 ? 138.099 115.723 125.322 1.00 61.20 ?  268 SER A CA    1 
ATOM   2154  C  C     . SER A 1 268 ? 138.292 116.908 126.265 1.00 63.52 ?  268 SER A C     1 
ATOM   2155  O  O     . SER A 1 268 ? 138.681 116.704 127.422 1.00 63.03 ?  268 SER A O     1 
ATOM   2156  C  CB    . SER A 1 268 ? 139.213 114.698 125.543 1.00 63.43 ?  268 SER A CB    1 
ATOM   2157  O  OG    . SER A 1 268 ? 140.456 115.187 125.070 1.00 62.04 ?  268 SER A OG    1 
ATOM   2158  N  N     . ALA A 1 269 ? 138.035 118.131 125.808 1.00 67.34 ?  269 ALA A N     1 
ATOM   2159  C  CA    . ALA A 1 269 ? 138.222 119.299 126.658 1.00 66.38 ?  269 ALA A CA    1 
ATOM   2160  C  C     . ALA A 1 269 ? 137.095 119.414 127.675 1.00 67.63 ?  269 ALA A C     1 
ATOM   2161  O  O     . ALA A 1 269 ? 135.935 119.114 127.382 1.00 65.73 ?  269 ALA A O     1 
ATOM   2162  C  CB    . ALA A 1 269 ? 138.297 120.568 125.809 1.00 63.69 ?  269 ALA A CB    1 
ATOM   2163  N  N     . ASP A 1 270 ? 137.445 119.856 128.880 1.00 75.07 ?  270 ASP A N     1 
ATOM   2164  C  CA    . ASP A 1 270 ? 136.462 120.019 129.939 1.00 75.00 ?  270 ASP A CA    1 
ATOM   2165  C  C     . ASP A 1 270 ? 135.616 121.267 129.700 1.00 74.74 ?  270 ASP A C     1 
ATOM   2166  O  O     . ASP A 1 270 ? 135.980 122.165 128.937 1.00 75.33 ?  270 ASP A O     1 
ATOM   2167  C  CB    . ASP A 1 270 ? 137.153 120.102 131.301 1.00 75.61 ?  270 ASP A CB    1 
ATOM   2168  C  CG    . ASP A 1 270 ? 136.233 119.727 132.447 1.00 77.85 ?  270 ASP A CG    1 
ATOM   2169  O  OD1   . ASP A 1 270 ? 135.211 120.417 132.644 1.00 77.52 ?  270 ASP A OD1   1 
ATOM   2170  O  OD2   . ASP A 1 270 ? 136.532 118.739 133.152 1.00 76.02 -1 270 ASP A OD2   1 
ATOM   2171  N  N     . GLU A 1 271 ? 134.463 121.311 130.372 1.00 75.70 ?  271 GLU A N     1 
ATOM   2172  C  CA    . GLU A 1 271 ? 133.551 122.439 130.222 1.00 76.74 ?  271 GLU A CA    1 
ATOM   2173  C  C     . GLU A 1 271 ? 134.125 123.735 130.781 1.00 76.23 ?  271 GLU A C     1 
ATOM   2174  O  O     . GLU A 1 271 ? 133.670 124.816 130.392 1.00 75.27 ?  271 GLU A O     1 
ATOM   2175  C  CB    . GLU A 1 271 ? 132.216 122.127 130.899 1.00 75.14 ?  271 GLU A CB    1 
ATOM   2176  C  CG    . GLU A 1 271 ? 131.484 120.938 130.301 1.00 75.56 ?  271 GLU A CG    1 
ATOM   2177  C  CD    . GLU A 1 271 ? 131.091 121.166 128.854 1.00 76.58 ?  271 GLU A CD    1 
ATOM   2178  O  OE1   . GLU A 1 271 ? 130.673 122.295 128.520 1.00 76.79 ?  271 GLU A OE1   1 
ATOM   2179  O  OE2   . GLU A 1 271 ? 131.204 120.217 128.049 1.00 75.92 -1 271 GLU A OE2   1 
ATOM   2180  N  N     . ASP A 1 272 ? 135.106 123.655 131.678 1.00 74.59 ?  272 ASP A N     1 
ATOM   2181  C  CA    . ASP A 1 272 ? 135.739 124.845 132.230 1.00 75.23 ?  272 ASP A CA    1 
ATOM   2182  C  C     . ASP A 1 272 ? 136.863 125.379 131.352 1.00 73.89 ?  272 ASP A C     1 
ATOM   2183  O  O     . ASP A 1 272 ? 137.467 126.399 131.700 1.00 71.80 ?  272 ASP A O     1 
ATOM   2184  C  CB    . ASP A 1 272 ? 136.282 124.553 133.632 1.00 74.63 ?  272 ASP A CB    1 
ATOM   2185  C  CG    . ASP A 1 272 ? 135.216 124.660 134.705 1.00 76.48 ?  272 ASP A CG    1 
ATOM   2186  O  OD1   . ASP A 1 272 ? 134.143 125.234 134.425 1.00 76.29 ?  272 ASP A OD1   1 
ATOM   2187  O  OD2   . ASP A 1 272 ? 135.455 124.174 135.830 1.00 74.73 -1 272 ASP A OD2   1 
ATOM   2188  N  N     . VAL A 1 273 ? 137.162 124.715 130.235 1.00 64.46 ?  273 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 273 ? 138.219 125.124 129.320 1.00 63.69 ?  273 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 273 ? 137.688 125.310 127.902 1.00 61.79 ?  273 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 273 ? 138.007 126.295 127.231 1.00 62.73 ?  273 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 273 ? 139.395 124.120 129.334 1.00 64.13 ?  273 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 273 ? 140.316 124.351 128.147 1.00 60.73 ?  273 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 273 ? 140.164 124.225 130.641 1.00 62.17 ?  273 VAL A CG2   1 
ATOM   2195  N  N     . ARG A 1 274 ? 136.865 124.372 127.436 1.00 58.79 ?  274 ARG A N     1 
ATOM   2196  C  CA    . ARG A 1 274 ? 136.435 124.363 126.044 1.00 56.27 ?  274 ARG A CA    1 
ATOM   2197  C  C     . ARG A 1 274 ? 135.594 125.590 125.711 1.00 56.31 ?  274 ARG A C     1 
ATOM   2198  O  O     . ARG A 1 274 ? 134.728 126.004 126.488 1.00 59.27 ?  274 ARG A O     1 
ATOM   2199  C  CB    . ARG A 1 274 ? 135.645 123.086 125.752 1.00 58.56 ?  274 ARG A CB    1 
ATOM   2200  C  CG    . ARG A 1 274 ? 134.487 123.265 124.783 1.00 56.98 ?  274 ARG A CG    1 
ATOM   2201  C  CD    . ARG A 1 274 ? 133.923 121.924 124.334 1.00 57.29 ?  274 ARG A CD    1 
ATOM   2202  N  NE    . ARG A 1 274 ? 134.820 121.185 123.450 1.00 60.77 ?  274 ARG A NE    1 
ATOM   2203  C  CZ    . ARG A 1 274 ? 135.264 121.614 122.275 1.00 60.46 ?  274 ARG A CZ    1 
ATOM   2204  N  NH1   . ARG A 1 274 ? 134.879 122.773 121.765 1.00 59.29 1  274 ARG A NH1   1 
ATOM   2205  N  NH2   . ARG A 1 274 ? 136.105 120.850 121.583 1.00 56.10 ?  274 ARG A NH2   1 
ATOM   2206  N  N     . VAL A 1 275 ? 135.861 126.172 124.544 1.00 47.22 ?  275 VAL A N     1 
ATOM   2207  C  CA    . VAL A 1 275 ? 135.061 127.252 123.982 1.00 47.42 ?  275 VAL A CA    1 
ATOM   2208  C  C     . VAL A 1 275 ? 134.360 126.716 122.742 1.00 47.78 ?  275 VAL A C     1 
ATOM   2209  O  O     . VAL A 1 275 ? 134.953 125.968 121.956 1.00 49.68 ?  275 VAL A O     1 
ATOM   2210  C  CB    . VAL A 1 275 ? 135.916 128.490 123.645 1.00 45.57 ?  275 VAL A CB    1 
ATOM   2211  C  CG1   . VAL A 1 275 ? 136.415 129.149 124.919 1.00 42.16 ?  275 VAL A CG1   1 
ATOM   2212  C  CG2   . VAL A 1 275 ? 137.081 128.109 122.755 1.00 46.32 ?  275 VAL A CG2   1 
ATOM   2213  N  N     . LYS A 1 276 ? 133.092 127.078 122.580 1.00 47.35 ?  276 LYS A N     1 
ATOM   2214  C  CA    . LYS A 1 276 ? 132.256 126.518 121.524 1.00 48.92 ?  276 LYS A CA    1 
ATOM   2215  C  C     . LYS A 1 276 ? 131.940 127.497 120.407 1.00 45.86 ?  276 LYS A C     1 
ATOM   2216  O  O     . LYS A 1 276 ? 131.965 127.114 119.235 1.00 51.39 ?  276 LYS A O     1 
ATOM   2217  C  CB    . LYS A 1 276 ? 130.946 125.994 122.125 1.00 49.48 ?  276 LYS A CB    1 
ATOM   2218  C  CG    . LYS A 1 276 ? 131.148 124.847 123.104 1.00 50.86 ?  276 LYS A CG    1 
ATOM   2219  C  CD    . LYS A 1 276 ? 129.851 124.442 123.780 1.00 51.93 ?  276 LYS A CD    1 
ATOM   2220  C  CE    . LYS A 1 276 ? 130.081 123.295 124.753 1.00 52.38 ?  276 LYS A CE    1 
ATOM   2221  N  NZ    . LYS A 1 276 ? 128.923 123.096 125.668 1.00 54.84 1  276 LYS A NZ    1 
ATOM   2222  N  N     . THR A 1 277 ? 131.644 128.753 120.731 1.00 37.03 ?  277 THR A N     1 
ATOM   2223  C  CA    . THR A 1 277 ? 131.278 129.755 119.740 1.00 38.81 ?  277 THR A CA    1 
ATOM   2224  C  C     . THR A 1 277 ? 132.471 130.557 119.241 1.00 40.67 ?  277 THR A C     1 
ATOM   2225  O  O     . THR A 1 277 ? 132.289 131.501 118.465 1.00 39.52 ?  277 THR A O     1 
ATOM   2226  C  CB    . THR A 1 277 ? 130.224 130.703 120.314 1.00 39.99 ?  277 THR A CB    1 
ATOM   2227  O  OG1   . THR A 1 277 ? 130.873 131.792 120.984 1.00 38.24 ?  277 THR A OG1   1 
ATOM   2228  C  CG2   . THR A 1 277 ? 129.340 129.968 121.298 1.00 38.90 ?  277 THR A CG2   1 
ATOM   2229  N  N     . LEU A 1 278 ? 133.682 130.206 119.662 1.00 36.61 ?  278 LEU A N     1 
ATOM   2230  C  CA    . LEU A 1 278 ? 134.880 130.976 119.350 1.00 30.45 ?  278 LEU A CA    1 
ATOM   2231  C  C     . LEU A 1 278 ? 135.792 130.139 118.465 1.00 24.23 ?  278 LEU A C     1 
ATOM   2232  O  O     . LEU A 1 278 ? 136.372 129.153 118.925 1.00 32.43 ?  278 LEU A O     1 
ATOM   2233  C  CB    . LEU A 1 278 ? 135.601 131.400 120.629 1.00 30.01 ?  278 LEU A CB    1 
ATOM   2234  C  CG    . LEU A 1 278 ? 136.495 132.636 120.545 1.00 28.95 ?  278 LEU A CG    1 
ATOM   2235  C  CD1   . LEU A 1 278 ? 135.662 133.895 120.427 1.00 23.64 ?  278 LEU A CD1   1 
ATOM   2236  C  CD2   . LEU A 1 278 ? 137.399 132.711 121.757 1.00 26.19 ?  278 LEU A CD2   1 
ATOM   2237  N  N     . SER A 1 279 ? 135.916 130.534 117.201 1.00 24.49 ?  279 SER A N     1 
ATOM   2238  C  CA    . SER A 1 279 ? 136.928 129.955 116.333 1.00 15.83 ?  279 SER A CA    1 
ATOM   2239  C  C     . SER A 1 279 ? 138.310 130.392 116.800 1.00 17.60 ?  279 SER A C     1 
ATOM   2240  O  O     . SER A 1 279 ? 138.472 131.401 117.488 1.00 28.53 ?  279 SER A O     1 
ATOM   2241  C  CB    . SER A 1 279 ? 136.703 130.379 114.883 1.00 18.86 ?  279 SER A CB    1 
ATOM   2242  O  OG    . SER A 1 279 ? 135.404 130.028 114.441 1.00 26.41 ?  279 SER A OG    1 
ATOM   2243  N  N     . ILE A 1 280 ? 139.321 129.612 116.433 1.00 15.31 ?  280 ILE A N     1 
ATOM   2244  C  CA    . ILE A 1 280 ? 140.687 129.885 116.859 1.00 16.70 ?  280 ILE A CA    1 
ATOM   2245  C  C     . ILE A 1 280 ? 141.601 129.885 115.643 1.00 15.46 ?  280 ILE A C     1 
ATOM   2246  O  O     . ILE A 1 280 ? 141.426 129.085 114.718 1.00 20.73 ?  280 ILE A O     1 
ATOM   2247  C  CB    . ILE A 1 280 ? 141.177 128.878 117.921 1.00 17.82 ?  280 ILE A CB    1 
ATOM   2248  C  CG1   . ILE A 1 280 ? 141.178 127.449 117.384 1.00 23.63 ?  280 ILE A CG1   1 
ATOM   2249  C  CG2   . ILE A 1 280 ? 140.326 128.966 119.166 1.00 18.85 ?  280 ILE A CG2   1 
ATOM   2250  C  CD1   . ILE A 1 280 ? 142.163 126.550 118.092 1.00 18.27 ?  280 ILE A CD1   1 
ATOM   2251  N  N     . GLY A 1 281 ? 142.551 130.808 115.637 1.00 9.44  ?  281 GLY A N     1 
ATOM   2252  C  CA    . GLY A 1 281 ? 143.583 130.832 114.622 1.00 4.46  ?  281 GLY A CA    1 
ATOM   2253  C  C     . GLY A 1 281 ? 144.946 130.941 115.268 1.00 11.28 ?  281 GLY A C     1 
ATOM   2254  O  O     . GLY A 1 281 ? 145.102 131.503 116.350 1.00 21.39 ?  281 GLY A O     1 
ATOM   2255  N  N     . VAL A 1 282 ? 145.941 130.379 114.590 1.00 18.47 ?  282 VAL A N     1 
ATOM   2256  C  CA    . VAL A 1 282 ? 147.317 130.384 115.067 1.00 16.31 ?  282 VAL A CA    1 
ATOM   2257  C  C     . VAL A 1 282 ? 148.174 131.119 114.050 1.00 14.87 ?  282 VAL A C     1 
ATOM   2258  O  O     . VAL A 1 282 ? 148.151 130.794 112.858 1.00 19.62 ?  282 VAL A O     1 
ATOM   2259  C  CB    . VAL A 1 282 ? 147.847 128.958 115.306 1.00 12.54 ?  282 VAL A CB    1 
ATOM   2260  C  CG1   . VAL A 1 282 ? 149.346 128.980 115.516 1.00 19.43 ?  282 VAL A CG1   1 
ATOM   2261  C  CG2   . VAL A 1 282 ? 147.166 128.348 116.509 1.00 20.97 ?  282 VAL A CG2   1 
ATOM   2262  N  N     . VAL A 1 283 ? 148.924 132.107 114.521 1.00 12.30 ?  283 VAL A N     1 
ATOM   2263  C  CA    . VAL A 1 283 ? 149.825 132.885 113.685 1.00 8.37  ?  283 VAL A CA    1 
ATOM   2264  C  C     . VAL A 1 283 ? 151.211 132.267 113.796 1.00 13.12 ?  283 VAL A C     1 
ATOM   2265  O  O     . VAL A 1 283 ? 151.781 132.194 114.890 1.00 25.22 ?  283 VAL A O     1 
ATOM   2266  C  CB    . VAL A 1 283 ? 149.833 134.362 114.101 1.00 9.54  ?  283 VAL A CB    1 
ATOM   2267  C  CG1   . VAL A 1 283 ? 150.605 135.196 113.099 1.00 12.39 ?  283 VAL A CG1   1 
ATOM   2268  C  CG2   . VAL A 1 283 ? 148.411 134.864 114.240 1.00 9.73  ?  283 VAL A CG2   1 
ATOM   2269  N  N     . ILE A 1 284 ? 151.749 131.817 112.668 1.00 15.63 ?  284 ILE A N     1 
ATOM   2270  C  CA    . ILE A 1 284 ? 153.019 131.097 112.657 1.00 15.39 ?  284 ILE A CA    1 
ATOM   2271  C  C     . ILE A 1 284 ? 154.068 131.899 111.897 1.00 21.61 ?  284 ILE A C     1 
ATOM   2272  O  O     . ILE A 1 284 ? 153.997 132.000 110.664 1.00 21.50 ?  284 ILE A O     1 
ATOM   2273  C  CB    . ILE A 1 284 ? 152.857 129.694 112.053 1.00 15.46 ?  284 ILE A CB    1 
ATOM   2274  C  CG1   . ILE A 1 284 ? 151.694 128.960 112.719 1.00 12.76 ?  284 ILE A CG1   1 
ATOM   2275  C  CG2   . ILE A 1 284 ? 154.143 128.904 112.199 1.00 16.89 ?  284 ILE A CG2   1 
ATOM   2276  C  CD1   . ILE A 1 284 ? 151.510 127.545 112.237 1.00 16.53 ?  284 ILE A CD1   1 
ATOM   2277  N  N     . PRO A 1 285 ? 155.045 132.486 112.580 1.00 25.53 ?  285 PRO A N     1 
ATOM   2278  C  CA    . PRO A 1 285 ? 156.159 133.122 111.873 1.00 25.30 ?  285 PRO A CA    1 
ATOM   2279  C  C     . PRO A 1 285 ? 157.054 132.087 111.208 1.00 25.79 ?  285 PRO A C     1 
ATOM   2280  O  O     . PRO A 1 285 ? 157.046 130.902 111.547 1.00 25.01 ?  285 PRO A O     1 
ATOM   2281  C  CB    . PRO A 1 285 ? 156.907 133.870 112.982 1.00 26.35 ?  285 PRO A CB    1 
ATOM   2282  C  CG    . PRO A 1 285 ? 155.928 133.973 114.110 1.00 23.82 ?  285 PRO A CG    1 
ATOM   2283  C  CD    . PRO A 1 285 ? 155.102 132.734 114.028 1.00 19.89 ?  285 PRO A CD    1 
ATOM   2284  N  N     . ASP A 1 286 ? 157.834 132.560 110.233 1.00 31.22 ?  286 ASP A N     1 
ATOM   2285  C  CA    . ASP A 1 286 ? 158.789 131.694 109.553 1.00 25.97 ?  286 ASP A CA    1 
ATOM   2286  C  C     . ASP A 1 286 ? 159.792 131.078 110.518 1.00 34.55 ?  286 ASP A C     1 
ATOM   2287  O  O     . ASP A 1 286 ? 160.355 130.018 110.220 1.00 35.11 ?  286 ASP A O     1 
ATOM   2288  C  CB    . ASP A 1 286 ? 159.529 132.477 108.468 1.00 27.60 ?  286 ASP A CB    1 
ATOM   2289  C  CG    . ASP A 1 286 ? 158.979 132.216 107.083 1.00 38.61 ?  286 ASP A CG    1 
ATOM   2290  O  OD1   . ASP A 1 286 ? 157.745 132.094 106.943 1.00 42.79 ?  286 ASP A OD1   1 
ATOM   2291  O  OD2   . ASP A 1 286 ? 159.782 132.137 106.130 1.00 42.45 -1 286 ASP A OD2   1 
ATOM   2292  N  N     . LYS A 1 287 ? 160.027 131.721 111.665 1.00 32.80 ?  287 LYS A N     1 
ATOM   2293  C  CA    . LYS A 1 287 ? 160.949 131.174 112.654 1.00 27.94 ?  287 LYS A CA    1 
ATOM   2294  C  C     . LYS A 1 287 ? 160.473 129.823 113.171 1.00 27.59 ?  287 LYS A C     1 
ATOM   2295  O  O     . LYS A 1 287 ? 161.277 128.902 113.341 1.00 35.74 ?  287 LYS A O     1 
ATOM   2296  C  CB    . LYS A 1 287 ? 161.121 132.159 113.810 1.00 28.97 ?  287 LYS A CB    1 
ATOM   2297  C  CG    . LYS A 1 287 ? 162.240 131.794 114.768 1.00 27.77 ?  287 LYS A CG    1 
ATOM   2298  C  CD    . LYS A 1 287 ? 163.541 131.578 114.018 1.00 31.66 ?  287 LYS A CD    1 
ATOM   2299  C  CE    . LYS A 1 287 ? 164.681 131.261 114.964 1.00 32.61 ?  287 LYS A CE    1 
ATOM   2300  N  NZ    . LYS A 1 287 ? 165.988 131.228 114.257 1.00 33.85 1  287 LYS A NZ    1 
ATOM   2301  N  N     . PHE A 1 288 ? 159.172 129.688 113.438 1.00 27.34 ?  288 PHE A N     1 
ATOM   2302  C  CA    . PHE A 1 288 ? 158.652 128.418 113.934 1.00 22.62 ?  288 PHE A CA    1 
ATOM   2303  C  C     . PHE A 1 288 ? 158.803 127.311 112.898 1.00 25.80 ?  288 PHE A C     1 
ATOM   2304  O  O     . PHE A 1 288 ? 159.173 126.181 113.238 1.00 34.63 ?  288 PHE A O     1 
ATOM   2305  C  CB    . PHE A 1 288 ? 157.188 128.569 114.340 1.00 24.92 ?  288 PHE A CB    1 
ATOM   2306  C  CG    . PHE A 1 288 ? 156.617 127.351 115.003 1.00 27.45 ?  288 PHE A CG    1 
ATOM   2307  C  CD1   . PHE A 1 288 ? 156.786 127.143 116.361 1.00 23.19 ?  288 PHE A CD1   1 
ATOM   2308  C  CD2   . PHE A 1 288 ? 155.918 126.409 114.269 1.00 26.73 ?  288 PHE A CD2   1 
ATOM   2309  C  CE1   . PHE A 1 288 ? 156.267 126.024 116.972 1.00 27.14 ?  288 PHE A CE1   1 
ATOM   2310  C  CE2   . PHE A 1 288 ? 155.397 125.287 114.876 1.00 24.01 ?  288 PHE A CE2   1 
ATOM   2311  C  CZ    . PHE A 1 288 ? 155.572 125.096 116.228 1.00 27.79 ?  288 PHE A CZ    1 
ATOM   2312  N  N     . VAL A 1 289 ? 158.511 127.614 111.632 1.00 32.00 ?  289 VAL A N     1 
ATOM   2313  C  CA    . VAL A 1 289 ? 158.652 126.615 110.578 1.00 29.47 ?  289 VAL A CA    1 
ATOM   2314  C  C     . VAL A 1 289 ? 160.113 126.222 110.413 1.00 30.02 ?  289 VAL A C     1 
ATOM   2315  O  O     . VAL A 1 289 ? 160.435 125.050 110.188 1.00 35.14 ?  289 VAL A O     1 
ATOM   2316  C  CB    . VAL A 1 289 ? 158.050 127.140 109.262 1.00 30.34 ?  289 VAL A CB    1 
ATOM   2317  C  CG1   . VAL A 1 289 ? 158.220 126.119 108.151 1.00 30.45 ?  289 VAL A CG1   1 
ATOM   2318  C  CG2   . VAL A 1 289 ? 156.584 127.488 109.455 1.00 23.88 ?  289 VAL A CG2   1 
ATOM   2319  N  N     . GLU A 1 290 ? 161.021 127.195 110.525 1.00 37.54 ?  290 GLU A N     1 
ATOM   2320  C  CA    . GLU A 1 290 ? 162.445 126.887 110.452 1.00 34.55 ?  290 GLU A CA    1 
ATOM   2321  C  C     . GLU A 1 290 ? 162.882 126.005 111.618 1.00 35.20 ?  290 GLU A C     1 
ATOM   2322  O  O     . GLU A 1 290 ? 163.650 125.055 111.432 1.00 41.82 ?  290 GLU A O     1 
ATOM   2323  C  CB    . GLU A 1 290 ? 163.256 128.183 110.415 1.00 34.45 ?  290 GLU A CB    1 
ATOM   2324  C  CG    . GLU A 1 290 ? 164.606 128.104 111.104 1.00 39.30 ?  290 GLU A CG    1 
ATOM   2325  C  CD    . GLU A 1 290 ? 165.350 129.424 111.078 1.00 45.41 ?  290 GLU A CD    1 
ATOM   2326  O  OE1   . GLU A 1 290 ? 164.685 130.482 111.069 1.00 46.66 ?  290 GLU A OE1   1 
ATOM   2327  O  OE2   . GLU A 1 290 ? 166.598 129.406 111.068 1.00 43.61 -1 290 GLU A OE2   1 
ATOM   2328  N  N     . LEU A 1 291 ? 162.399 126.303 112.826 1.00 28.22 ?  291 LEU A N     1 
ATOM   2329  C  CA    . LEU A 1 291 ? 162.758 125.504 113.994 1.00 26.89 ?  291 LEU A CA    1 
ATOM   2330  C  C     . LEU A 1 291 ? 162.238 124.079 113.871 1.00 35.32 ?  291 LEU A C     1 
ATOM   2331  O  O     . LEU A 1 291 ? 162.938 123.123 114.221 1.00 38.89 ?  291 LEU A O     1 
ATOM   2332  C  CB    . LEU A 1 291 ? 162.219 126.159 115.265 1.00 31.08 ?  291 LEU A CB    1 
ATOM   2333  C  CG    . LEU A 1 291 ? 162.903 127.445 115.727 1.00 33.94 ?  291 LEU A CG    1 
ATOM   2334  C  CD1   . LEU A 1 291 ? 162.044 128.168 116.749 1.00 28.25 ?  291 LEU A CD1   1 
ATOM   2335  C  CD2   . LEU A 1 291 ? 164.277 127.150 116.290 1.00 31.72 ?  291 LEU A CD2   1 
ATOM   2336  N  N     . ALA A 1 292 ? 161.004 123.918 113.389 1.00 37.20 ?  292 ALA A N     1 
ATOM   2337  C  CA    . ALA A 1 292 ? 160.458 122.579 113.192 1.00 30.50 ?  292 ALA A CA    1 
ATOM   2338  C  C     . ALA A 1 292 ? 161.199 121.838 112.084 1.00 32.10 ?  292 ALA A C     1 
ATOM   2339  O  O     . ALA A 1 292 ? 161.396 120.622 112.168 1.00 35.83 ?  292 ALA A O     1 
ATOM   2340  C  CB    . ALA A 1 292 ? 158.965 122.662 112.882 1.00 26.04 ?  292 ALA A CB    1 
ATOM   2341  N  N     . ARG A 1 293 ? 161.612 122.558 111.039 1.00 32.95 ?  293 ARG A N     1 
ATOM   2342  C  CA    . ARG A 1 293 ? 162.333 121.933 109.936 1.00 33.13 ?  293 ARG A CA    1 
ATOM   2343  C  C     . ARG A 1 293 ? 163.668 121.364 110.396 1.00 39.16 ?  293 ARG A C     1 
ATOM   2344  O  O     . ARG A 1 293 ? 164.057 120.264 109.986 1.00 41.45 ?  293 ARG A O     1 
ATOM   2345  C  CB    . ARG A 1 293 ? 162.536 122.948 108.812 1.00 34.94 ?  293 ARG A CB    1 
ATOM   2346  C  CG    . ARG A 1 293 ? 163.400 122.460 107.665 1.00 35.23 ?  293 ARG A CG    1 
ATOM   2347  C  CD    . ARG A 1 293 ? 163.819 123.617 106.782 1.00 37.62 ?  293 ARG A CD    1 
ATOM   2348  N  NE    . ARG A 1 293 ? 162.694 124.494 106.477 1.00 42.26 ?  293 ARG A NE    1 
ATOM   2349  C  CZ    . ARG A 1 293 ? 162.720 125.814 106.598 1.00 40.70 ?  293 ARG A CZ    1 
ATOM   2350  N  NH1   . ARG A 1 293 ? 163.801 126.449 107.018 1.00 41.69 1  293 ARG A NH1   1 
ATOM   2351  N  NH2   . ARG A 1 293 ? 161.632 126.514 106.289 1.00 35.59 ?  293 ARG A NH2   1 
ATOM   2352  N  N     . GLU A 1 294 ? 164.382 122.095 111.247 1.00 44.74 ?  294 GLU A N     1 
ATOM   2353  C  CA    . GLU A 1 294 ? 165.671 121.648 111.757 1.00 43.18 ?  294 GLU A CA    1 
ATOM   2354  C  C     . GLU A 1 294 ? 165.543 120.708 112.947 1.00 44.44 ?  294 GLU A C     1 
ATOM   2355  O  O     . GLU A 1 294 ? 166.568 120.239 113.453 1.00 48.04 ?  294 GLU A O     1 
ATOM   2356  C  CB    . GLU A 1 294 ? 166.528 122.857 112.143 1.00 41.64 ?  294 GLU A CB    1 
ATOM   2357  C  CG    . GLU A 1 294 ? 166.643 123.905 111.048 1.00 43.84 ?  294 GLU A CG    1 
ATOM   2358  C  CD    . GLU A 1 294 ? 166.961 125.283 111.592 1.00 52.67 ?  294 GLU A CD    1 
ATOM   2359  O  OE1   . GLU A 1 294 ? 166.520 125.595 112.718 1.00 50.44 ?  294 GLU A OE1   1 
ATOM   2360  O  OE2   . GLU A 1 294 ? 167.650 126.056 110.894 1.00 51.67 -1 294 GLU A OE2   1 
ATOM   2361  N  N     . ASP A 1 295 ? 164.318 120.431 113.400 1.00 44.22 ?  295 ASP A N     1 
ATOM   2362  C  CA    . ASP A 1 295 ? 164.062 119.564 114.551 1.00 43.82 ?  295 ASP A CA    1 
ATOM   2363  C  C     . ASP A 1 295 ? 164.746 120.084 115.810 1.00 48.16 ?  295 ASP A C     1 
ATOM   2364  O  O     . ASP A 1 295 ? 165.094 119.312 116.707 1.00 51.21 ?  295 ASP A O     1 
ATOM   2365  C  CB    . ASP A 1 295 ? 164.481 118.119 114.270 1.00 46.89 ?  295 ASP A CB    1 
ATOM   2366  C  CG    . ASP A 1 295 ? 163.537 117.108 114.890 1.00 51.48 ?  295 ASP A CG    1 
ATOM   2367  O  OD1   . ASP A 1 295 ? 162.797 117.477 115.825 1.00 49.59 ?  295 ASP A OD1   1 
ATOM   2368  O  OD2   . ASP A 1 295 ? 163.531 115.942 114.439 1.00 50.75 -1 295 ASP A OD2   1 
ATOM   2369  N  N     . LYS A 1 296 ? 164.943 121.396 115.886 1.00 45.61 ?  296 LYS A N     1 
ATOM   2370  C  CA    . LYS A 1 296 ? 165.565 122.010 117.044 1.00 45.38 ?  296 LYS A CA    1 
ATOM   2371  C  C     . LYS A 1 296 ? 164.536 122.208 118.153 1.00 44.84 ?  296 LYS A C     1 
ATOM   2372  O  O     . LYS A 1 296 ? 163.336 121.998 117.971 1.00 45.52 ?  296 LYS A O     1 
ATOM   2373  C  CB    . LYS A 1 296 ? 166.212 123.339 116.659 1.00 45.77 ?  296 LYS A CB    1 
ATOM   2374  C  CG    . LYS A 1 296 ? 167.408 123.188 115.736 1.00 45.88 ?  296 LYS A CG    1 
ATOM   2375  C  CD    . LYS A 1 296 ? 168.046 124.529 115.424 1.00 46.45 ?  296 LYS A CD    1 
ATOM   2376  C  CE    . LYS A 1 296 ? 169.387 124.347 114.731 1.00 45.56 ?  296 LYS A CE    1 
ATOM   2377  N  NZ    . LYS A 1 296 ? 169.908 125.627 114.177 1.00 46.99 1  296 LYS A NZ    1 
ATOM   2378  N  N     . ALA A 1 297 ? 165.023 122.609 119.323 1.00 46.02 ?  297 ALA A N     1 
ATOM   2379  C  CA    . ALA A 1 297 ? 164.150 122.864 120.461 1.00 44.58 ?  297 ALA A CA    1 
ATOM   2380  C  C     . ALA A 1 297 ? 163.664 124.307 120.413 1.00 44.70 ?  297 ALA A C     1 
ATOM   2381  O  O     . ALA A 1 297 ? 164.457 125.241 120.566 1.00 46.57 ?  297 ALA A O     1 
ATOM   2382  C  CB    . ALA A 1 297 ? 164.883 122.585 121.769 1.00 44.33 ?  297 ALA A CB    1 
ATOM   2383  N  N     . ALA A 1 298 ? 162.366 124.486 120.198 1.00 38.12 ?  298 ALA A N     1 
ATOM   2384  C  CA    . ALA A 1 298 ? 161.773 125.811 120.170 1.00 36.96 ?  298 ALA A CA    1 
ATOM   2385  C  C     . ALA A 1 298 ? 161.354 126.232 121.574 1.00 35.89 ?  298 ALA A C     1 
ATOM   2386  O  O     . ALA A 1 298 ? 161.274 125.422 122.499 1.00 36.72 ?  298 ALA A O     1 
ATOM   2387  C  CB    . ALA A 1 298 ? 160.577 125.846 119.220 1.00 36.58 ?  298 ALA A CB    1 
ATOM   2388  N  N     . TYR A 1 299 ? 161.085 127.525 121.728 1.00 35.49 ?  299 TYR A N     1 
ATOM   2389  C  CA    . TYR A 1 299 ? 160.677 128.087 123.006 1.00 28.47 ?  299 TYR A CA    1 
ATOM   2390  C  C     . TYR A 1 299 ? 159.454 128.965 122.804 1.00 31.38 ?  299 TYR A C     1 
ATOM   2391  O  O     . TYR A 1 299 ? 159.437 129.813 121.908 1.00 40.14 ?  299 TYR A O     1 
ATOM   2392  C  CB    . TYR A 1 299 ? 161.806 128.906 123.637 1.00 34.24 ?  299 TYR A CB    1 
ATOM   2393  C  CG    . TYR A 1 299 ? 162.837 128.076 124.361 1.00 37.70 ?  299 TYR A CG    1 
ATOM   2394  C  CD1   . TYR A 1 299 ? 162.649 127.702 125.681 1.00 35.43 ?  299 TYR A CD1   1 
ATOM   2395  C  CD2   . TYR A 1 299 ? 164.006 127.681 123.726 1.00 37.20 ?  299 TYR A CD2   1 
ATOM   2396  C  CE1   . TYR A 1 299 ? 163.589 126.950 126.349 1.00 35.26 ?  299 TYR A CE1   1 
ATOM   2397  C  CE2   . TYR A 1 299 ? 164.952 126.926 124.385 1.00 37.25 ?  299 TYR A CE2   1 
ATOM   2398  C  CZ    . TYR A 1 299 ? 164.739 126.564 125.697 1.00 40.47 ?  299 TYR A CZ    1 
ATOM   2399  O  OH    . TYR A 1 299 ? 165.677 125.812 126.364 1.00 45.23 ?  299 TYR A OH    1 
ATOM   2400  N  N     . VAL A 1 300 ? 158.439 128.758 123.625 1.00 31.06 ?  300 VAL A N     1 
ATOM   2401  C  CA    . VAL A 1 300 ? 157.330 129.697 123.730 1.00 24.27 ?  300 VAL A CA    1 
ATOM   2402  C  C     . VAL A 1 300 ? 157.646 130.656 124.866 1.00 29.18 ?  300 VAL A C     1 
ATOM   2403  O  O     . VAL A 1 300 ? 158.328 130.303 125.831 1.00 29.35 ?  300 VAL A O     1 
ATOM   2404  C  CB    . VAL A 1 300 ? 155.986 128.973 123.948 1.00 26.12 ?  300 VAL A CB    1 
ATOM   2405  C  CG1   . VAL A 1 300 ? 155.586 128.215 122.694 1.00 29.40 ?  300 VAL A CG1   1 
ATOM   2406  C  CG2   . VAL A 1 300 ? 156.069 128.038 125.139 1.00 29.28 ?  300 VAL A CG2   1 
ATOM   2407  N  N     . PHE A 1 301 ? 157.157 131.884 124.754 1.00 27.32 ?  301 PHE A N     1 
ATOM   2408  C  CA    . PHE A 1 301 ? 157.583 132.956 125.637 1.00 25.15 ?  301 PHE A CA    1 
ATOM   2409  C  C     . PHE A 1 301 ? 156.409 133.534 126.410 1.00 25.22 ?  301 PHE A C     1 
ATOM   2410  O  O     . PHE A 1 301 ? 155.259 133.485 125.962 1.00 31.04 ?  301 PHE A O     1 
ATOM   2411  C  CB    . PHE A 1 301 ? 158.278 134.068 124.849 1.00 27.97 ?  301 PHE A CB    1 
ATOM   2412  C  CG    . PHE A 1 301 ? 159.433 133.586 124.025 1.00 31.39 ?  301 PHE A CG    1 
ATOM   2413  C  CD1   . PHE A 1 301 ? 160.666 133.360 124.608 1.00 29.04 ?  301 PHE A CD1   1 
ATOM   2414  C  CD2   . PHE A 1 301 ? 159.283 133.349 122.672 1.00 26.23 ?  301 PHE A CD2   1 
ATOM   2415  C  CE1   . PHE A 1 301 ? 161.728 132.910 123.857 1.00 31.76 ?  301 PHE A CE1   1 
ATOM   2416  C  CE2   . PHE A 1 301 ? 160.342 132.901 121.917 1.00 28.48 ?  301 PHE A CE2   1 
ATOM   2417  C  CZ    . PHE A 1 301 ? 161.567 132.682 122.511 1.00 32.52 ?  301 PHE A CZ    1 
ATOM   2418  N  N     . TYR A 1 302 ? 156.719 134.074 127.586 1.00 26.97 ?  302 TYR A N     1 
ATOM   2419  C  CA    . TYR A 1 302 ? 155.744 134.793 128.390 1.00 27.45 ?  302 TYR A CA    1 
ATOM   2420  C  C     . TYR A 1 302 ? 155.708 136.232 127.900 1.00 30.56 ?  302 TYR A C     1 
ATOM   2421  O  O     . TYR A 1 302 ? 156.717 136.942 128.029 1.00 29.62 ?  302 TYR A O     1 
ATOM   2422  C  CB    . TYR A 1 302 ? 156.116 134.736 129.863 1.00 28.30 ?  302 TYR A CB    1 
ATOM   2423  C  CG    . TYR A 1 302 ? 155.925 133.376 130.499 1.00 26.25 ?  302 TYR A CG    1 
ATOM   2424  C  CD1   . TYR A 1 302 ? 156.770 132.320 130.192 1.00 27.65 ?  302 TYR A CD1   1 
ATOM   2425  C  CD2   . TYR A 1 302 ? 154.907 133.154 131.413 1.00 27.48 ?  302 TYR A CD2   1 
ATOM   2426  C  CE1   . TYR A 1 302 ? 156.601 131.081 130.769 1.00 30.31 ?  302 TYR A CE1   1 
ATOM   2427  C  CE2   . TYR A 1 302 ? 154.733 131.919 132.000 1.00 30.14 ?  302 TYR A CE2   1 
ATOM   2428  C  CZ    . TYR A 1 302 ? 155.583 130.886 131.675 1.00 33.71 ?  302 TYR A CZ    1 
ATOM   2429  O  OH    . TYR A 1 302 ? 155.411 129.651 132.256 1.00 37.78 ?  302 TYR A OH    1 
ATOM   2430  N  N     . PRO A 1 303 ? 154.597 136.701 127.330 1.00 29.03 ?  303 PRO A N     1 
ATOM   2431  C  CA    . PRO A 1 303 ? 154.595 138.036 126.707 1.00 24.96 ?  303 PRO A CA    1 
ATOM   2432  C  C     . PRO A 1 303 ? 154.900 139.170 127.667 1.00 27.56 ?  303 PRO A C     1 
ATOM   2433  O  O     . PRO A 1 303 ? 155.522 140.159 127.260 1.00 30.61 ?  303 PRO A O     1 
ATOM   2434  C  CB    . PRO A 1 303 ? 153.172 138.153 126.141 1.00 24.83 ?  303 PRO A CB    1 
ATOM   2435  C  CG    . PRO A 1 303 ? 152.679 136.761 126.050 1.00 24.18 ?  303 PRO A CG    1 
ATOM   2436  C  CD    . PRO A 1 303 ? 153.306 136.016 127.174 1.00 25.44 ?  303 PRO A CD    1 
ATOM   2437  N  N     . HIS A 1 304 ? 154.473 139.068 128.928 1.00 32.27 ?  304 HIS A N     1 
ATOM   2438  C  CA    . HIS A 1 304 ? 154.694 140.168 129.858 1.00 27.96 ?  304 HIS A CA    1 
ATOM   2439  C  C     . HIS A 1 304 ? 156.168 140.346 130.180 1.00 32.41 ?  304 HIS A C     1 
ATOM   2440  O  O     . HIS A 1 304 ? 156.625 141.478 130.358 1.00 40.50 ?  304 HIS A O     1 
ATOM   2441  C  CB    . HIS A 1 304 ? 153.899 139.958 131.143 1.00 29.89 ?  304 HIS A CB    1 
ATOM   2442  C  CG    . HIS A 1 304 ? 153.785 141.192 131.981 1.00 32.74 ?  304 HIS A CG    1 
ATOM   2443  N  ND1   . HIS A 1 304 ? 153.523 142.432 131.442 1.00 31.93 ?  304 HIS A ND1   1 
ATOM   2444  C  CD2   . HIS A 1 304 ? 153.907 141.380 133.315 1.00 35.88 ?  304 HIS A CD2   1 
ATOM   2445  C  CE1   . HIS A 1 304 ? 153.484 143.331 132.408 1.00 33.55 ?  304 HIS A CE1   1 
ATOM   2446  N  NE2   . HIS A 1 304 ? 153.712 142.719 133.555 1.00 34.35 ?  304 HIS A NE2   1 
ATOM   2447  N  N     . THR A 1 305 ? 156.925 139.252 130.263 1.00 25.74 ?  305 THR A N     1 
ATOM   2448  C  CA    . THR A 1 305 ? 158.362 139.371 130.484 1.00 29.41 ?  305 THR A CA    1 
ATOM   2449  C  C     . THR A 1 305 ? 159.039 140.087 129.322 1.00 28.69 ?  305 THR A C     1 
ATOM   2450  O  O     . THR A 1 305 ? 159.905 140.945 129.532 1.00 37.07 ?  305 THR A O     1 
ATOM   2451  C  CB    . THR A 1 305 ? 158.975 137.988 130.695 1.00 33.48 ?  305 THR A CB    1 
ATOM   2452  O  OG1   . THR A 1 305 ? 158.832 137.214 129.498 1.00 32.73 ?  305 THR A OG1   1 
ATOM   2453  C  CG2   . THR A 1 305 ? 158.278 137.276 131.838 1.00 30.50 ?  305 THR A CG2   1 
ATOM   2454  N  N     . ILE A 1 306 ? 158.647 139.758 128.090 1.00 32.69 ?  306 ILE A N     1 
ATOM   2455  C  CA    . ILE A 1 306 ? 159.210 140.433 126.925 1.00 28.02 ?  306 ILE A CA    1 
ATOM   2456  C  C     . ILE A 1 306 ? 158.836 141.909 126.930 1.00 29.49 ?  306 ILE A C     1 
ATOM   2457  O  O     . ILE A 1 306 ? 159.666 142.774 126.630 1.00 35.55 ?  306 ILE A O     1 
ATOM   2458  C  CB    . ILE A 1 306 ? 158.751 139.735 125.632 1.00 30.36 ?  306 ILE A CB    1 
ATOM   2459  C  CG1   . ILE A 1 306 ? 159.407 138.361 125.511 1.00 28.05 ?  306 ILE A CG1   1 
ATOM   2460  C  CG2   . ILE A 1 306 ? 159.078 140.583 124.414 1.00 30.85 ?  306 ILE A CG2   1 
ATOM   2461  C  CD1   . ILE A 1 306 ? 158.903 137.555 124.350 1.00 31.24 ?  306 ILE A CD1   1 
ATOM   2462  N  N     . TYR A 1 307 ? 157.583 142.223 127.264 1.00 33.59 ?  307 TYR A N     1 
ATOM   2463  C  CA    . TYR A 1 307 ? 157.161 143.620 127.298 1.00 31.54 ?  307 TYR A CA    1 
ATOM   2464  C  C     . TYR A 1 307 ? 157.909 144.400 128.371 1.00 35.23 ?  307 TYR A C     1 
ATOM   2465  O  O     . TYR A 1 307 ? 158.299 145.552 128.150 1.00 36.72 ?  307 TYR A O     1 
ATOM   2466  C  CB    . TYR A 1 307 ? 155.652 143.708 127.521 1.00 29.33 ?  307 TYR A CB    1 
ATOM   2467  C  CG    . TYR A 1 307 ? 155.117 145.119 127.475 1.00 33.59 ?  307 TYR A CG    1 
ATOM   2468  C  CD1   . TYR A 1 307 ? 154.822 145.728 126.265 1.00 29.32 ?  307 TYR A CD1   1 
ATOM   2469  C  CD2   . TYR A 1 307 ? 154.908 145.841 128.641 1.00 34.47 ?  307 TYR A CD2   1 
ATOM   2470  C  CE1   . TYR A 1 307 ? 154.335 147.017 126.216 1.00 33.46 ?  307 TYR A CE1   1 
ATOM   2471  C  CE2   . TYR A 1 307 ? 154.422 147.132 128.602 1.00 34.77 ?  307 TYR A CE2   1 
ATOM   2472  C  CZ    . TYR A 1 307 ? 154.137 147.714 127.386 1.00 35.97 ?  307 TYR A CZ    1 
ATOM   2473  O  OH    . TYR A 1 307 ? 153.652 148.999 127.342 1.00 38.80 ?  307 TYR A OH    1 
ATOM   2474  N  N     . LYS A 1 308 ? 158.109 143.796 129.544 1.00 35.92 ?  308 LYS A N     1 
ATOM   2475  C  CA    . LYS A 1 308 ? 158.852 144.462 130.608 1.00 33.02 ?  308 LYS A CA    1 
ATOM   2476  C  C     . LYS A 1 308 ? 160.310 144.669 130.220 1.00 32.74 ?  308 LYS A C     1 
ATOM   2477  O  O     . LYS A 1 308 ? 160.889 145.725 130.496 1.00 39.07 ?  308 LYS A O     1 
ATOM   2478  C  CB    . LYS A 1 308 ? 158.752 143.651 131.900 1.00 34.34 ?  308 LYS A CB    1 
ATOM   2479  C  CG    . LYS A 1 308 ? 157.392 143.717 132.571 1.00 34.02 ?  308 LYS A CG    1 
ATOM   2480  C  CD    . LYS A 1 308 ? 157.408 143.024 133.922 1.00 34.74 ?  308 LYS A CD    1 
ATOM   2481  C  CE    . LYS A 1 308 ? 157.936 141.603 133.814 1.00 38.99 ?  308 LYS A CE    1 
ATOM   2482  N  NZ    . LYS A 1 308 ? 156.924 140.598 134.238 1.00 36.46 1  308 LYS A NZ    1 
ATOM   2483  N  N     . GLU A 1 309 ? 160.918 143.672 129.577 1.00 30.34 ?  309 GLU A N     1 
ATOM   2484  C  CA    . GLU A 1 309 ? 162.338 143.753 129.258 1.00 35.08 ?  309 GLU A CA    1 
ATOM   2485  C  C     . GLU A 1 309 ? 162.616 144.707 128.101 1.00 36.49 ?  309 GLU A C     1 
ATOM   2486  O  O     . GLU A 1 309 ? 163.599 145.454 128.136 1.00 39.85 ?  309 GLU A O     1 
ATOM   2487  C  CB    . GLU A 1 309 ? 162.874 142.357 128.939 1.00 32.16 ?  309 GLU A CB    1 
ATOM   2488  C  CG    . GLU A 1 309 ? 164.281 142.343 128.380 1.00 36.68 ?  309 GLU A CG    1 
ATOM   2489  C  CD    . GLU A 1 309 ? 165.329 142.674 129.418 1.00 43.34 ?  309 GLU A CD    1 
ATOM   2490  O  OE1   . GLU A 1 309 ? 164.997 142.679 130.621 1.00 44.25 ?  309 GLU A OE1   1 
ATOM   2491  O  OE2   . GLU A 1 309 ? 166.488 142.931 129.031 1.00 42.50 -1 309 GLU A OE2   1 
ATOM   2492  N  N     . TYR A 1 310 ? 161.765 144.704 127.076 1.00 34.65 ?  310 TYR A N     1 
ATOM   2493  C  CA    . TYR A 1 310 ? 162.039 145.431 125.846 1.00 35.73 ?  310 TYR A CA    1 
ATOM   2494  C  C     . TYR A 1 310 ? 161.137 146.636 125.625 1.00 33.98 ?  310 TYR A C     1 
ATOM   2495  O  O     . TYR A 1 310 ? 161.439 147.457 124.753 1.00 35.70 ?  310 TYR A O     1 
ATOM   2496  C  CB    . TYR A 1 310 ? 161.917 144.486 124.642 1.00 34.26 ?  310 TYR A CB    1 
ATOM   2497  C  CG    . TYR A 1 310 ? 162.948 143.383 124.637 1.00 34.23 ?  310 TYR A CG    1 
ATOM   2498  C  CD1   . TYR A 1 310 ? 164.205 143.585 124.089 1.00 33.53 ?  310 TYR A CD1   1 
ATOM   2499  C  CD2   . TYR A 1 310 ? 162.666 142.143 125.190 1.00 32.13 ?  310 TYR A CD2   1 
ATOM   2500  C  CE1   . TYR A 1 310 ? 165.150 142.582 124.085 1.00 36.62 ?  310 TYR A CE1   1 
ATOM   2501  C  CE2   . TYR A 1 310 ? 163.604 141.134 125.193 1.00 33.39 ?  310 TYR A CE2   1 
ATOM   2502  C  CZ    . TYR A 1 310 ? 164.845 141.359 124.639 1.00 36.69 ?  310 TYR A CZ    1 
ATOM   2503  O  OH    . TYR A 1 310 ? 165.783 140.357 124.639 1.00 35.81 ?  310 TYR A OH    1 
ATOM   2504  N  N     . GLY A 1 311 ? 160.050 146.767 126.377 1.00 31.00 ?  311 GLY A N     1 
ATOM   2505  C  CA    . GLY A 1 311 ? 159.134 147.870 126.188 1.00 32.53 ?  311 GLY A CA    1 
ATOM   2506  C  C     . GLY A 1 311 ? 158.165 147.706 125.041 1.00 35.66 ?  311 GLY A C     1 
ATOM   2507  O  O     . GLY A 1 311 ? 157.360 148.613 124.798 1.00 39.25 ?  311 GLY A O     1 
ATOM   2508  N  N     . GLN A 1 312 ? 158.215 146.584 124.327 1.00 36.16 ?  312 GLN A N     1 
ATOM   2509  C  CA    . GLN A 1 312 ? 157.315 146.309 123.220 1.00 32.63 ?  312 GLN A CA    1 
ATOM   2510  C  C     . GLN A 1 312 ? 156.677 144.944 123.421 1.00 33.64 ?  312 GLN A C     1 
ATOM   2511  O  O     . GLN A 1 312 ? 157.250 144.063 124.064 1.00 38.49 ?  312 GLN A O     1 
ATOM   2512  C  CB    . GLN A 1 312 ? 158.045 146.340 121.872 1.00 32.24 ?  312 GLN A CB    1 
ATOM   2513  C  CG    . GLN A 1 312 ? 158.730 147.654 121.556 1.00 35.80 ?  312 GLN A CG    1 
ATOM   2514  C  CD    . GLN A 1 312 ? 160.021 147.464 120.786 1.00 40.31 ?  312 GLN A CD    1 
ATOM   2515  O  OE1   . GLN A 1 312 ? 160.036 147.515 119.556 1.00 39.60 ?  312 GLN A OE1   1 
ATOM   2516  N  NE2   . GLN A 1 312 ? 161.113 147.240 121.507 1.00 37.60 ?  312 GLN A NE2   1 
ATOM   2517  N  N     . HIS A 1 313 ? 155.480 144.780 122.865 1.00 30.44 ?  313 HIS A N     1 
ATOM   2518  C  CA    . HIS A 1 313 ? 154.823 143.485 122.890 1.00 28.09 ?  313 HIS A CA    1 
ATOM   2519  C  C     . HIS A 1 313 ? 155.576 142.496 122.005 1.00 32.02 ?  313 HIS A C     1 
ATOM   2520  O  O     . HIS A 1 313 ? 156.279 142.872 121.064 1.00 32.61 ?  313 HIS A O     1 
ATOM   2521  C  CB    . HIS A 1 313 ? 153.373 143.610 122.429 1.00 25.78 ?  313 HIS A CB    1 
ATOM   2522  C  CG    . HIS A 1 313 ? 152.525 144.460 123.325 1.00 31.16 ?  313 HIS A CG    1 
ATOM   2523  N  ND1   . HIS A 1 313 ? 152.053 144.018 124.541 1.00 29.95 ?  313 HIS A ND1   1 
ATOM   2524  C  CD2   . HIS A 1 313 ? 152.064 145.724 123.179 1.00 30.97 ?  313 HIS A CD2   1 
ATOM   2525  C  CE1   . HIS A 1 313 ? 151.337 144.973 125.106 1.00 29.39 ?  313 HIS A CE1   1 
ATOM   2526  N  NE2   . HIS A 1 313 ? 151.328 146.018 124.301 1.00 31.94 ?  313 HIS A NE2   1 
ATOM   2527  N  N     . MET A 1 314 ? 155.431 141.210 122.331 1.00 35.83 ?  314 MET A N     1 
ATOM   2528  C  CA    . MET A 1 314 ? 156.134 140.178 121.576 1.00 29.72 ?  314 MET A CA    1 
ATOM   2529  C  C     . MET A 1 314 ? 155.672 140.138 120.125 1.00 35.52 ?  314 MET A C     1 
ATOM   2530  O  O     . MET A 1 314 ? 156.493 140.015 119.209 1.00 38.07 ?  314 MET A O     1 
ATOM   2531  C  CB    . MET A 1 314 ? 155.937 138.814 122.234 1.00 27.22 ?  314 MET A CB    1 
ATOM   2532  C  CG    . MET A 1 314 ? 156.564 137.670 121.459 1.00 32.36 ?  314 MET A CG    1 
ATOM   2533  S  SD    . MET A 1 314 ? 156.338 136.047 122.209 1.00 41.78 ?  314 MET A SD    1 
ATOM   2534  C  CE    . MET A 1 314 ? 154.985 136.371 123.330 1.00 30.24 ?  314 MET A CE    1 
ATOM   2535  N  N     . ASP A 1 315 ? 154.363 140.243 119.893 1.00 33.93 ?  315 ASP A N     1 
ATOM   2536  C  CA    . ASP A 1 315 ? 153.843 140.183 118.534 1.00 38.13 ?  315 ASP A CA    1 
ATOM   2537  C  C     . ASP A 1 315 ? 154.091 141.462 117.748 1.00 31.39 ?  315 ASP A C     1 
ATOM   2538  O  O     . ASP A 1 315 ? 153.903 141.465 116.528 1.00 39.47 ?  315 ASP A O     1 
ATOM   2539  C  CB    . ASP A 1 315 ? 152.344 139.871 118.550 1.00 31.26 ?  315 ASP A CB    1 
ATOM   2540  C  CG    . ASP A 1 315 ? 151.566 140.804 119.445 1.00 35.74 ?  315 ASP A CG    1 
ATOM   2541  O  OD1   . ASP A 1 315 ? 152.158 141.328 120.410 1.00 39.29 ?  315 ASP A OD1   1 
ATOM   2542  O  OD2   . ASP A 1 315 ? 150.363 141.015 119.183 1.00 32.58 -1 315 ASP A OD2   1 
ATOM   2543  N  N     . GLU A 1 316 ? 154.504 142.539 118.409 1.00 24.36 ?  316 GLU A N     1 
ATOM   2544  C  CA    . GLU A 1 316 ? 154.916 143.754 117.721 1.00 28.82 ?  316 GLU A CA    1 
ATOM   2545  C  C     . GLU A 1 316 ? 156.380 143.723 117.308 1.00 33.83 ?  316 GLU A C     1 
ATOM   2546  O  O     . GLU A 1 316 ? 156.853 144.681 116.687 1.00 32.98 ?  316 GLU A O     1 
ATOM   2547  C  CB    . GLU A 1 316 ? 154.657 144.976 118.606 1.00 31.77 ?  316 GLU A CB    1 
ATOM   2548  C  CG    . GLU A 1 316 ? 153.192 145.222 118.906 1.00 31.04 ?  316 GLU A CG    1 
ATOM   2549  C  CD    . GLU A 1 316 ? 152.521 146.086 117.859 1.00 38.93 ?  316 GLU A CD    1 
ATOM   2550  O  OE1   . GLU A 1 316 ? 151.377 146.528 118.093 1.00 41.23 ?  316 GLU A OE1   1 
ATOM   2551  O  OE2   . GLU A 1 316 ? 153.139 146.327 116.801 1.00 41.62 -1 316 GLU A OE2   1 
ATOM   2552  N  N     . MET A 1 317 ? 157.101 142.658 117.638 1.00 39.09 ?  317 MET A N     1 
ATOM   2553  C  CA    . MET A 1 317 ? 158.513 142.518 117.325 1.00 35.78 ?  317 MET A CA    1 
ATOM   2554  C  C     . MET A 1 317 ? 158.713 141.428 116.282 1.00 34.44 ?  317 MET A C     1 
ATOM   2555  O  O     . MET A 1 317 ? 157.865 140.553 116.094 1.00 36.95 ?  317 MET A O     1 
ATOM   2556  C  CB    . MET A 1 317 ? 159.322 142.193 118.586 1.00 34.12 ?  317 MET A CB    1 
ATOM   2557  C  CG    . MET A 1 317 ? 159.228 143.246 119.674 1.00 34.36 ?  317 MET A CG    1 
ATOM   2558  S  SD    . MET A 1 317 ? 160.070 142.762 121.189 1.00 44.92 ?  317 MET A SD    1 
ATOM   2559  C  CE    . MET A 1 317 ? 161.563 143.738 121.071 1.00 38.89 ?  317 MET A CE    1 
ATOM   2560  N  N     . ASP A 1 318 ? 159.855 141.494 115.604 1.00 41.30 ?  318 ASP A N     1 
ATOM   2561  C  CA    . ASP A 1 318 ? 160.200 140.511 114.584 1.00 38.66 ?  318 ASP A CA    1 
ATOM   2562  C  C     . ASP A 1 318 ? 160.774 139.279 115.267 1.00 37.96 ?  318 ASP A C     1 
ATOM   2563  O  O     . ASP A 1 318 ? 161.861 139.334 115.850 1.00 41.69 ?  318 ASP A O     1 
ATOM   2564  C  CB    . ASP A 1 318 ? 161.195 141.102 113.590 1.00 36.96 ?  318 ASP A CB    1 
ATOM   2565  C  CG    . ASP A 1 318 ? 161.323 140.269 112.332 1.00 46.58 ?  318 ASP A CG    1 
ATOM   2566  O  OD1   . ASP A 1 318 ? 160.358 139.557 111.985 1.00 43.51 ?  318 ASP A OD1   1 
ATOM   2567  O  OD2   . ASP A 1 318 ? 162.392 140.326 111.689 1.00 49.50 -1 318 ASP A OD2   1 
ATOM   2568  N  N     . MET A 1 319 ? 160.047 138.163 115.200 1.00 34.59 ?  319 MET A N     1 
ATOM   2569  C  CA    . MET A 1 319 ? 160.519 136.949 115.853 1.00 35.93 ?  319 MET A CA    1 
ATOM   2570  C  C     . MET A 1 319 ? 161.732 136.361 115.146 1.00 33.84 ?  319 MET A C     1 
ATOM   2571  O  O     . MET A 1 319 ? 162.613 135.800 115.803 1.00 37.29 ?  319 MET A O     1 
ATOM   2572  C  CB    . MET A 1 319 ? 159.396 135.917 115.933 1.00 33.86 ?  319 MET A CB    1 
ATOM   2573  C  CG    . MET A 1 319 ? 159.718 134.746 116.841 1.00 35.19 ?  319 MET A CG    1 
ATOM   2574  S  SD    . MET A 1 319 ? 160.063 135.245 118.538 1.00 43.77 ?  319 MET A SD    1 
ATOM   2575  C  CE    . MET A 1 319 ? 158.407 135.514 119.156 1.00 36.00 ?  319 MET A CE    1 
ATOM   2576  N  N     . ASN A 1 320 ? 161.808 136.493 113.822 1.00 39.08 ?  320 ASN A N     1 
ATOM   2577  C  CA    . ASN A 1 320 ? 162.951 135.961 113.090 1.00 40.11 ?  320 ASN A CA    1 
ATOM   2578  C  C     . ASN A 1 320 ? 164.249 136.679 113.435 1.00 41.59 ?  320 ASN A C     1 
ATOM   2579  O  O     . ASN A 1 320 ? 165.328 136.157 113.134 1.00 41.30 ?  320 ASN A O     1 
ATOM   2580  C  CB    . ASN A 1 320 ? 162.689 136.038 111.586 1.00 42.00 ?  320 ASN A CB    1 
ATOM   2581  C  CG    . ASN A 1 320 ? 161.700 134.992 111.118 1.00 43.63 ?  320 ASN A CG    1 
ATOM   2582  O  OD1   . ASN A 1 320 ? 160.497 135.243 111.051 1.00 38.11 ?  320 ASN A OD1   1 
ATOM   2583  N  ND2   . ASN A 1 320 ? 162.204 133.808 110.788 1.00 40.53 ?  320 ASN A ND2   1 
ATOM   2584  N  N     . GLU A 1 321 ? 164.174 137.858 114.054 1.00 42.57 ?  321 GLU A N     1 
ATOM   2585  C  CA    . GLU A 1 321 ? 165.361 138.585 114.476 1.00 41.38 ?  321 GLU A CA    1 
ATOM   2586  C  C     . GLU A 1 321 ? 165.499 138.713 115.985 1.00 43.34 ?  321 GLU A C     1 
ATOM   2587  O  O     . GLU A 1 321 ? 166.590 139.038 116.461 1.00 46.03 ?  321 GLU A O     1 
ATOM   2588  C  CB    . GLU A 1 321 ? 165.377 139.988 113.848 1.00 41.68 ?  321 GLU A CB    1 
ATOM   2589  C  CG    . GLU A 1 321 ? 164.851 141.089 114.754 1.00 44.45 ?  321 GLU A CG    1 
ATOM   2590  C  CD    . GLU A 1 321 ? 164.505 142.358 114.000 1.00 47.32 ?  321 GLU A CD    1 
ATOM   2591  O  OE1   . GLU A 1 321 ? 164.369 142.297 112.761 1.00 47.11 ?  321 GLU A OE1   1 
ATOM   2592  O  OE2   . GLU A 1 321 ? 164.367 143.416 114.651 1.00 43.73 -1 321 GLU A OE2   1 
ATOM   2593  N  N     . MET A 1 322 ? 164.436 138.456 116.748 1.00 40.61 ?  322 MET A N     1 
ATOM   2594  C  CA    . MET A 1 322 ? 164.465 138.606 118.196 1.00 38.13 ?  322 MET A CA    1 
ATOM   2595  C  C     . MET A 1 322 ? 164.274 137.299 118.952 1.00 35.74 ?  322 MET A C     1 
ATOM   2596  O  O     . MET A 1 322 ? 164.300 137.316 120.184 1.00 41.25 ?  322 MET A O     1 
ATOM   2597  C  CB    . MET A 1 322 ? 163.401 139.612 118.652 1.00 37.48 ?  322 MET A CB    1 
ATOM   2598  C  CG    . MET A 1 322 ? 163.540 140.997 118.049 1.00 38.97 ?  322 MET A CG    1 
ATOM   2599  S  SD    . MET A 1 322 ? 164.714 142.057 118.917 1.00 48.56 ?  322 MET A SD    1 
ATOM   2600  C  CE    . MET A 1 322 ? 164.512 141.499 120.603 1.00 39.49 ?  322 MET A CE    1 
ATOM   2601  N  N     . TYR A 1 323 ? 164.068 136.175 118.262 1.00 33.93 ?  323 TYR A N     1 
ATOM   2602  C  CA    . TYR A 1 323 ? 163.864 134.909 118.961 1.00 32.83 ?  323 TYR A CA    1 
ATOM   2603  C  C     . TYR A 1 323 ? 165.106 134.513 119.748 1.00 36.92 ?  323 TYR A C     1 
ATOM   2604  O  O     . TYR A 1 323 ? 165.016 134.100 120.911 1.00 39.12 ?  323 TYR A O     1 
ATOM   2605  C  CB    . TYR A 1 323 ? 163.485 133.813 117.965 1.00 33.05 ?  323 TYR A CB    1 
ATOM   2606  C  CG    . TYR A 1 323 ? 163.457 132.425 118.565 1.00 34.69 ?  323 TYR A CG    1 
ATOM   2607  C  CD1   . TYR A 1 323 ? 162.336 131.961 119.235 1.00 33.75 ?  323 TYR A CD1   1 
ATOM   2608  C  CD2   . TYR A 1 323 ? 164.553 131.579 118.461 1.00 32.20 ?  323 TYR A CD2   1 
ATOM   2609  C  CE1   . TYR A 1 323 ? 162.307 130.696 119.787 1.00 32.07 ?  323 TYR A CE1   1 
ATOM   2610  C  CE2   . TYR A 1 323 ? 164.534 130.316 119.010 1.00 32.37 ?  323 TYR A CE2   1 
ATOM   2611  C  CZ    . TYR A 1 323 ? 163.409 129.879 119.671 1.00 31.69 ?  323 TYR A CZ    1 
ATOM   2612  O  OH    . TYR A 1 323 ? 163.388 128.620 120.217 1.00 31.64 ?  323 TYR A OH    1 
ATOM   2613  N  N     . ASP A 1 324 ? 166.279 134.633 119.126 1.00 38.72 ?  324 ASP A N     1 
ATOM   2614  C  CA    . ASP A 1 324 ? 167.519 134.290 119.809 1.00 35.27 ?  324 ASP A CA    1 
ATOM   2615  C  C     . ASP A 1 324 ? 167.790 135.240 120.968 1.00 40.31 ?  324 ASP A C     1 
ATOM   2616  O  O     . ASP A 1 324 ? 168.305 134.823 122.010 1.00 47.00 ?  324 ASP A O     1 
ATOM   2617  C  CB    . ASP A 1 324 ? 168.681 134.300 118.819 1.00 41.26 ?  324 ASP A CB    1 
ATOM   2618  C  CG    . ASP A 1 324 ? 168.553 133.220 117.765 1.00 44.72 ?  324 ASP A CG    1 
ATOM   2619  O  OD1   . ASP A 1 324 ? 168.342 132.047 118.136 1.00 41.76 ?  324 ASP A OD1   1 
ATOM   2620  O  OD2   . ASP A 1 324 ? 168.662 133.544 116.564 1.00 44.08 -1 324 ASP A OD2   1 
ATOM   2621  N  N     . LYS A 1 325 ? 167.457 136.521 120.802 1.00 38.81 ?  325 LYS A N     1 
ATOM   2622  C  CA    . LYS A 1 325 ? 167.612 137.472 121.897 1.00 35.53 ?  325 LYS A CA    1 
ATOM   2623  C  C     . LYS A 1 325 ? 166.685 137.133 123.058 1.00 38.86 ?  325 LYS A C     1 
ATOM   2624  O  O     . LYS A 1 325 ? 167.081 137.233 124.223 1.00 43.73 ?  325 LYS A O     1 
ATOM   2625  C  CB    . LYS A 1 325 ? 167.359 138.892 121.393 1.00 37.33 ?  325 LYS A CB    1 
ATOM   2626  C  CG    . LYS A 1 325 ? 168.363 139.359 120.356 1.00 37.87 ?  325 LYS A CG    1 
ATOM   2627  C  CD    . LYS A 1 325 ? 168.033 140.749 119.851 1.00 41.16 ?  325 LYS A CD    1 
ATOM   2628  C  CE    . LYS A 1 325 ? 168.990 141.176 118.751 1.00 42.11 ?  325 LYS A CE    1 
ATOM   2629  N  NZ    . LYS A 1 325 ? 168.492 142.366 118.010 1.00 43.60 1  325 LYS A NZ    1 
ATOM   2630  N  N     . PHE A 1 326 ? 165.445 136.736 122.760 1.00 39.16 ?  326 PHE A N     1 
ATOM   2631  C  CA    . PHE A 1 326 ? 164.524 136.315 123.810 1.00 33.41 ?  326 PHE A CA    1 
ATOM   2632  C  C     . PHE A 1 326 ? 165.043 135.080 124.530 1.00 36.37 ?  326 PHE A C     1 
ATOM   2633  O  O     . PHE A 1 326 ? 164.953 134.982 125.760 1.00 40.55 ?  326 PHE A O     1 
ATOM   2634  C  CB    . PHE A 1 326 ? 163.140 136.030 123.223 1.00 32.69 ?  326 PHE A CB    1 
ATOM   2635  C  CG    . PHE A 1 326 ? 162.454 137.235 122.648 1.00 35.56 ?  326 PHE A CG    1 
ATOM   2636  C  CD1   . PHE A 1 326 ? 162.855 138.514 122.987 1.00 35.09 ?  326 PHE A CD1   1 
ATOM   2637  C  CD2   . PHE A 1 326 ? 161.400 137.079 121.765 1.00 34.20 ?  326 PHE A CD2   1 
ATOM   2638  C  CE1   . PHE A 1 326 ? 162.217 139.614 122.453 1.00 33.20 ?  326 PHE A CE1   1 
ATOM   2639  C  CE2   . PHE A 1 326 ? 160.760 138.176 121.230 1.00 37.15 ?  326 PHE A CE2   1 
ATOM   2640  C  CZ    . PHE A 1 326 ? 161.170 139.445 121.575 1.00 38.91 ?  326 PHE A CZ    1 
ATOM   2641  N  N     . VAL A 1 327 ? 165.576 134.116 123.777 1.00 39.05 ?  327 VAL A N     1 
ATOM   2642  C  CA    . VAL A 1 327 ? 166.083 132.889 124.385 1.00 38.24 ?  327 VAL A CA    1 
ATOM   2643  C  C     . VAL A 1 327 ? 167.293 133.184 125.261 1.00 40.04 ?  327 VAL A C     1 
ATOM   2644  O  O     . VAL A 1 327 ? 167.410 132.666 126.378 1.00 45.64 ?  327 VAL A O     1 
ATOM   2645  C  CB    . VAL A 1 327 ? 166.405 131.853 123.293 1.00 36.91 ?  327 VAL A CB    1 
ATOM   2646  C  CG1   . VAL A 1 327 ? 167.197 130.693 123.871 1.00 40.92 ?  327 VAL A CG1   1 
ATOM   2647  C  CG2   . VAL A 1 327 ? 165.126 131.354 122.650 1.00 33.27 ?  327 VAL A CG2   1 
ATOM   2648  N  N     . ASP A 1 328 ? 168.206 134.027 124.778 1.00 38.45 ?  328 ASP A N     1 
ATOM   2649  C  CA    . ASP A 1 328 ? 169.411 134.355 125.528 1.00 36.87 ?  328 ASP A CA    1 
ATOM   2650  C  C     . ASP A 1 328 ? 169.148 135.305 126.687 1.00 40.52 ?  328 ASP A C     1 
ATOM   2651  O  O     . ASP A 1 328 ? 169.981 135.394 127.596 1.00 45.52 ?  328 ASP A O     1 
ATOM   2652  C  CB    . ASP A 1 328 ? 170.457 134.971 124.596 1.00 38.98 ?  328 ASP A CB    1 
ATOM   2653  C  CG    . ASP A 1 328 ? 170.919 134.006 123.526 1.00 44.83 ?  328 ASP A CG    1 
ATOM   2654  O  OD1   . ASP A 1 328 ? 170.745 132.784 123.711 1.00 48.01 ?  328 ASP A OD1   1 
ATOM   2655  O  OD2   . ASP A 1 328 ? 171.458 134.470 122.498 1.00 44.15 -1 328 ASP A OD2   1 
ATOM   2656  N  N     . ASN A 1 329 ? 168.025 136.012 126.679 1.00 41.66 ?  329 ASN A N     1 
ATOM   2657  C  CA    . ASN A 1 329 ? 167.733 136.976 127.733 1.00 38.80 ?  329 ASN A CA    1 
ATOM   2658  C  C     . ASN A 1 329 ? 167.310 136.246 129.000 1.00 42.53 ?  329 ASN A C     1 
ATOM   2659  O  O     . ASN A 1 329 ? 166.317 135.510 128.975 1.00 42.49 ?  329 ASN A O     1 
ATOM   2660  C  CB    . ASN A 1 329 ? 166.638 137.934 127.287 1.00 33.89 ?  329 ASN A CB    1 
ATOM   2661  C  CG    . ASN A 1 329 ? 166.618 139.216 128.092 1.00 40.78 ?  329 ASN A CG    1 
ATOM   2662  O  OD1   . ASN A 1 329 ? 166.553 139.191 129.319 1.00 45.18 ?  329 ASN A OD1   1 
ATOM   2663  N  ND2   . ASN A 1 329 ? 166.684 140.347 127.402 1.00 41.09 ?  329 ASN A ND2   1 
ATOM   2664  N  N     . PRO A 1 330 ? 168.024 136.412 130.117 1.00 44.27 ?  330 PRO A N     1 
ATOM   2665  C  CA    . PRO A 1 330 ? 167.587 135.756 131.358 1.00 40.96 ?  330 PRO A CA    1 
ATOM   2666  C  C     . PRO A 1 330 ? 166.318 136.351 131.939 1.00 39.46 ?  330 PRO A C     1 
ATOM   2667  O  O     . PRO A 1 330 ? 165.558 135.631 132.598 1.00 40.15 ?  330 PRO A O     1 
ATOM   2668  C  CB    . PRO A 1 330 ? 168.785 135.953 132.297 1.00 39.08 ?  330 PRO A CB    1 
ATOM   2669  C  CG    . PRO A 1 330 ? 169.463 137.170 131.780 1.00 36.96 ?  330 PRO A CG    1 
ATOM   2670  C  CD    . PRO A 1 330 ? 169.291 137.140 130.290 1.00 38.41 ?  330 PRO A CD    1 
ATOM   2671  N  N     . ARG A 1 331 ? 166.062 137.640 131.715 1.00 38.41 ?  331 ARG A N     1 
ATOM   2672  C  CA    . ARG A 1 331 ? 164.882 138.289 132.270 1.00 40.80 ?  331 ARG A CA    1 
ATOM   2673  C  C     . ARG A 1 331 ? 163.611 137.963 131.500 1.00 41.59 ?  331 ARG A C     1 
ATOM   2674  O  O     . ARG A 1 331 ? 162.515 138.243 131.999 1.00 40.35 ?  331 ARG A O     1 
ATOM   2675  C  CB    . ARG A 1 331 ? 165.092 139.804 132.313 1.00 39.81 ?  331 ARG A CB    1 
ATOM   2676  C  CG    . ARG A 1 331 ? 166.055 140.254 133.400 1.00 40.33 ?  331 ARG A CG    1 
ATOM   2677  C  CD    . ARG A 1 331 ? 166.678 141.599 133.071 1.00 42.11 ?  331 ARG A CD    1 
ATOM   2678  N  NE    . ARG A 1 331 ? 167.293 141.609 131.749 1.00 41.88 ?  331 ARG A NE    1 
ATOM   2679  C  CZ    . ARG A 1 331 ? 168.463 141.058 131.461 1.00 43.13 ?  331 ARG A CZ    1 
ATOM   2680  N  NH1   . ARG A 1 331 ? 169.189 140.452 132.386 1.00 42.61 1  331 ARG A NH1   1 
ATOM   2681  N  NH2   . ARG A 1 331 ? 168.920 141.120 130.213 1.00 43.39 ?  331 ARG A NH2   1 
ATOM   2682  N  N     . VAL A 1 332 ? 163.727 137.388 130.311 1.00 37.30 ?  332 VAL A N     1 
ATOM   2683  C  CA    . VAL A 1 332 ? 162.579 136.887 129.569 1.00 32.98 ?  332 VAL A CA    1 
ATOM   2684  C  C     . VAL A 1 332 ? 162.297 135.467 130.038 1.00 37.43 ?  332 VAL A C     1 
ATOM   2685  O  O     . VAL A 1 332 ? 163.215 134.646 130.142 1.00 38.83 ?  332 VAL A O     1 
ATOM   2686  C  CB    . VAL A 1 332 ? 162.838 136.931 128.054 1.00 33.47 ?  332 VAL A CB    1 
ATOM   2687  C  CG1   . VAL A 1 332 ? 161.756 136.177 127.302 1.00 33.96 ?  332 VAL A CG1   1 
ATOM   2688  C  CG2   . VAL A 1 332 ? 162.921 138.369 127.572 1.00 34.85 ?  332 VAL A CG2   1 
ATOM   2689  N  N     . LYS A 1 333 ? 161.037 135.181 130.350 1.00 35.97 ?  333 LYS A N     1 
ATOM   2690  C  CA    . LYS A 1 333 ? 160.635 133.844 130.764 1.00 29.96 ?  333 LYS A CA    1 
ATOM   2691  C  C     . LYS A 1 333 ? 160.170 133.058 129.546 1.00 32.69 ?  333 LYS A C     1 
ATOM   2692  O  O     . LYS A 1 333 ? 159.338 133.537 128.770 1.00 35.64 ?  333 LYS A O     1 
ATOM   2693  C  CB    . LYS A 1 333 ? 159.528 133.907 131.815 1.00 28.38 ?  333 LYS A CB    1 
ATOM   2694  C  CG    . LYS A 1 333 ? 159.411 132.655 132.665 1.00 34.79 ?  333 LYS A CG    1 
ATOM   2695  C  CD    . LYS A 1 333 ? 158.220 132.734 133.602 1.00 35.04 ?  333 LYS A CD    1 
ATOM   2696  C  CE    . LYS A 1 333 ? 157.961 131.397 134.279 1.00 37.13 ?  333 LYS A CE    1 
ATOM   2697  N  NZ    . LYS A 1 333 ? 156.789 131.450 135.197 1.00 37.74 1  333 LYS A NZ    1 
ATOM   2698  N  N     . LYS A 1 334 ? 160.714 131.857 129.380 1.00 38.85 ?  334 LYS A N     1 
ATOM   2699  C  CA    . LYS A 1 334 ? 160.417 131.030 128.223 1.00 34.29 ?  334 LYS A CA    1 
ATOM   2700  C  C     . LYS A 1 334 ? 160.175 129.596 128.668 1.00 36.06 ?  334 LYS A C     1 
ATOM   2701  O  O     . LYS A 1 334 ? 160.677 129.157 129.705 1.00 39.70 ?  334 LYS A O     1 
ATOM   2702  C  CB    . LYS A 1 334 ? 161.554 131.076 127.194 1.00 32.87 ?  334 LYS A CB    1 
ATOM   2703  C  CG    . LYS A 1 334 ? 162.841 130.430 127.665 1.00 35.31 ?  334 LYS A CG    1 
ATOM   2704  C  CD    . LYS A 1 334 ? 164.053 131.260 127.294 1.00 35.92 ?  334 LYS A CD    1 
ATOM   2705  C  CE    . LYS A 1 334 ? 164.016 132.613 127.969 1.00 38.84 ?  334 LYS A CE    1 
ATOM   2706  N  NZ    . LYS A 1 334 ? 165.302 133.345 127.835 1.00 39.45 1  334 LYS A NZ    1 
ATOM   2707  N  N     . GLU A 1 335 ? 159.386 128.875 127.877 1.00 38.00 ?  335 GLU A N     1 
ATOM   2708  C  CA    . GLU A 1 335 ? 159.092 127.471 128.115 1.00 36.54 ?  335 GLU A CA    1 
ATOM   2709  C  C     . GLU A 1 335 ? 159.516 126.650 126.907 1.00 36.29 ?  335 GLU A C     1 
ATOM   2710  O  O     . GLU A 1 335 ? 159.256 127.032 125.762 1.00 40.84 ?  335 GLU A O     1 
ATOM   2711  C  CB    . GLU A 1 335 ? 157.604 127.251 128.400 1.00 36.06 ?  335 GLU A CB    1 
ATOM   2712  C  CG    . GLU A 1 335 ? 157.334 126.292 129.545 1.00 38.94 ?  335 GLU A CG    1 
ATOM   2713  C  CD    . GLU A 1 335 ? 156.064 126.623 130.301 1.00 44.57 ?  335 GLU A CD    1 
ATOM   2714  O  OE1   . GLU A 1 335 ? 155.991 126.306 131.507 1.00 44.53 ?  335 GLU A OE1   1 
ATOM   2715  O  OE2   . GLU A 1 335 ? 155.137 127.193 129.691 1.00 42.08 -1 335 GLU A OE2   1 
ATOM   2716  N  N     . LYS A 1 336 ? 160.170 125.522 127.167 1.00 37.35 ?  336 LYS A N     1 
ATOM   2717  C  CA    . LYS A 1 336 ? 160.667 124.664 126.103 1.00 32.44 ?  336 LYS A CA    1 
ATOM   2718  C  C     . LYS A 1 336 ? 159.526 123.855 125.499 1.00 37.58 ?  336 LYS A C     1 
ATOM   2719  O  O     . LYS A 1 336 ? 158.733 123.246 126.222 1.00 40.53 ?  336 LYS A O     1 
ATOM   2720  C  CB    . LYS A 1 336 ? 161.750 123.732 126.643 1.00 38.26 ?  336 LYS A CB    1 
ATOM   2721  C  CG    . LYS A 1 336 ? 162.645 123.118 125.584 1.00 43.11 ?  336 LYS A CG    1 
ATOM   2722  C  CD    . LYS A 1 336 ? 163.598 122.114 126.212 1.00 41.37 ?  336 LYS A CD    1 
ATOM   2723  C  CE    . LYS A 1 336 ? 164.790 121.834 125.315 1.00 41.46 ?  336 LYS A CE    1 
ATOM   2724  N  NZ    . LYS A 1 336 ? 164.603 120.597 124.509 1.00 42.28 1  336 LYS A NZ    1 
ATOM   2725  N  N     . ILE A 1 337 ? 159.446 123.856 124.168 1.00 34.86 ?  337 ILE A N     1 
ATOM   2726  C  CA    . ILE A 1 337 ? 158.457 123.079 123.437 1.00 30.93 ?  337 ILE A CA    1 
ATOM   2727  C  C     . ILE A 1 337 ? 159.150 122.380 122.276 1.00 34.73 ?  337 ILE A C     1 
ATOM   2728  O  O     . ILE A 1 337 ? 160.260 122.738 121.877 1.00 42.14 ?  337 ILE A O     1 
ATOM   2729  C  CB    . ILE A 1 337 ? 157.288 123.942 122.914 1.00 32.72 ?  337 ILE A CB    1 
ATOM   2730  C  CG1   . ILE A 1 337 ? 157.816 125.083 122.045 1.00 35.14 ?  337 ILE A CG1   1 
ATOM   2731  C  CG2   . ILE A 1 337 ? 156.456 124.478 124.067 1.00 36.24 ?  337 ILE A CG2   1 
ATOM   2732  C  CD1   . ILE A 1 337 ? 157.010 125.315 120.793 1.00 32.24 ?  337 ILE A CD1   1 
ATOM   2733  N  N     . ASN A 1 338 ? 158.476 121.367 121.736 1.00 36.42 ?  338 ASN A N     1 
ATOM   2734  C  CA    . ASN A 1 338 ? 158.947 120.701 120.532 1.00 31.75 ?  338 ASN A CA    1 
ATOM   2735  C  C     . ASN A 1 338 ? 158.159 121.238 119.349 1.00 33.43 ?  338 ASN A C     1 
ATOM   2736  O  O     . ASN A 1 338 ? 156.952 120.973 119.252 1.00 36.67 ?  338 ASN A O     1 
ATOM   2737  C  CB    . ASN A 1 338 ? 158.780 119.189 120.645 1.00 33.95 ?  338 ASN A CB    1 
ATOM   2738  C  CG    . ASN A 1 338 ? 159.488 118.441 119.535 1.00 36.09 ?  338 ASN A CG    1 
ATOM   2739  O  OD1   . ASN A 1 338 ? 158.853 117.925 118.616 1.00 38.24 ?  338 ASN A OD1   1 
ATOM   2740  N  ND2   . ASN A 1 338 ? 160.811 118.380 119.612 1.00 35.46 ?  338 ASN A ND2   1 
ATOM   2741  N  N     . PRO A 1 339 ? 158.777 122.000 118.444 1.00 35.15 ?  339 PRO A N     1 
ATOM   2742  C  CA    . PRO A 1 339 ? 158.012 122.585 117.332 1.00 29.42 ?  339 PRO A CA    1 
ATOM   2743  C  C     . PRO A 1 339 ? 157.363 121.555 116.425 1.00 32.59 ?  339 PRO A C     1 
ATOM   2744  O  O     . PRO A 1 339 ? 156.258 121.797 115.926 1.00 37.75 ?  339 PRO A O     1 
ATOM   2745  C  CB    . PRO A 1 339 ? 159.063 123.416 116.584 1.00 33.56 ?  339 PRO A CB    1 
ATOM   2746  C  CG    . PRO A 1 339 ? 160.370 122.816 116.967 1.00 36.27 ?  339 PRO A CG    1 
ATOM   2747  C  CD    . PRO A 1 339 ? 160.209 122.333 118.372 1.00 36.81 ?  339 PRO A CD    1 
ATOM   2748  N  N     . ARG A 1 340 ? 158.010 120.411 116.196 1.00 35.29 ?  340 ARG A N     1 
ATOM   2749  C  CA    . ARG A 1 340 ? 157.392 119.373 115.377 1.00 28.41 ?  340 ARG A CA    1 
ATOM   2750  C  C     . ARG A 1 340 ? 156.207 118.741 116.093 1.00 30.40 ?  340 ARG A C     1 
ATOM   2751  O  O     . ARG A 1 340 ? 155.201 118.404 115.460 1.00 37.55 ?  340 ARG A O     1 
ATOM   2752  C  CB    . ARG A 1 340 ? 158.424 118.313 114.998 1.00 28.21 ?  340 ARG A CB    1 
ATOM   2753  C  CG    . ARG A 1 340 ? 159.375 118.762 113.911 1.00 29.17 ?  340 ARG A CG    1 
ATOM   2754  C  CD    . ARG A 1 340 ? 160.012 117.582 113.207 1.00 33.78 ?  340 ARG A CD    1 
ATOM   2755  N  NE    . ARG A 1 340 ? 161.058 118.013 112.288 1.00 35.44 ?  340 ARG A NE    1 
ATOM   2756  C  CZ    . ARG A 1 340 ? 161.787 117.193 111.547 1.00 32.17 ?  340 ARG A CZ    1 
ATOM   2757  N  NH1   . ARG A 1 340 ? 161.613 115.883 111.590 1.00 30.86 1  340 ARG A NH1   1 
ATOM   2758  N  NH2   . ARG A 1 340 ? 162.715 117.699 110.741 1.00 33.45 ?  340 ARG A NH2   1 
ATOM   2759  N  N     . LYS A 1 341 ? 156.305 118.573 117.413 1.00 32.09 ?  341 LYS A N     1 
ATOM   2760  C  CA    . LYS A 1 341 ? 155.159 118.089 118.175 1.00 30.76 ?  341 LYS A CA    1 
ATOM   2761  C  C     . LYS A 1 341 ? 154.009 119.084 118.117 1.00 33.23 ?  341 LYS A C     1 
ATOM   2762  O  O     . LYS A 1 341 ? 152.843 118.690 118.016 1.00 36.39 ?  341 LYS A O     1 
ATOM   2763  C  CB    . LYS A 1 341 ? 155.566 117.819 119.622 1.00 35.55 ?  341 LYS A CB    1 
ATOM   2764  C  CG    . LYS A 1 341 ? 155.478 116.360 120.026 1.00 35.82 ?  341 LYS A CG    1 
ATOM   2765  C  CD    . LYS A 1 341 ? 156.236 115.476 119.050 1.00 38.75 ?  341 LYS A CD    1 
ATOM   2766  C  CE    . LYS A 1 341 ? 156.266 114.032 119.524 1.00 41.67 ?  341 LYS A CE    1 
ATOM   2767  N  NZ    . LYS A 1 341 ? 157.343 113.802 120.525 1.00 36.89 1  341 LYS A NZ    1 
ATOM   2768  N  N     . LEU A 1 342 ? 154.318 120.381 118.175 1.00 30.62 ?  342 LEU A N     1 
ATOM   2769  C  CA    . LEU A 1 342 ? 153.279 121.396 118.045 1.00 27.32 ?  342 LEU A CA    1 
ATOM   2770  C  C     . LEU A 1 342 ? 152.643 121.362 116.660 1.00 29.90 ?  342 LEU A C     1 
ATOM   2771  O  O     . LEU A 1 342 ? 151.427 121.527 116.527 1.00 33.99 ?  342 LEU A O     1 
ATOM   2772  C  CB    . LEU A 1 342 ? 153.859 122.779 118.340 1.00 31.11 ?  342 LEU A CB    1 
ATOM   2773  C  CG    . LEU A 1 342 ? 152.863 123.907 118.615 1.00 30.19 ?  342 LEU A CG    1 
ATOM   2774  C  CD1   . LEU A 1 342 ? 151.706 123.403 119.457 1.00 28.04 ?  342 LEU A CD1   1 
ATOM   2775  C  CD2   . LEU A 1 342 ? 153.556 125.069 119.303 1.00 26.81 ?  342 LEU A CD2   1 
ATOM   2776  N  N     . LEU A 1 343 ? 153.450 121.151 115.617 1.00 31.54 ?  343 LEU A N     1 
ATOM   2777  C  CA    . LEU A 1 343 ? 152.906 121.036 114.268 1.00 25.59 ?  343 LEU A CA    1 
ATOM   2778  C  C     . LEU A 1 343 ? 151.998 119.818 114.138 1.00 26.60 ?  343 LEU A C     1 
ATOM   2779  O  O     . LEU A 1 343 ? 150.929 119.890 113.519 1.00 37.59 ?  343 LEU A O     1 
ATOM   2780  C  CB    . LEU A 1 343 ? 154.044 120.963 113.251 1.00 30.44 ?  343 LEU A CB    1 
ATOM   2781  C  CG    . LEU A 1 343 ? 154.374 122.237 112.477 1.00 29.59 ?  343 LEU A CG    1 
ATOM   2782  C  CD1   . LEU A 1 343 ? 155.392 121.942 111.392 1.00 25.32 ?  343 LEU A CD1   1 
ATOM   2783  C  CD2   . LEU A 1 343 ? 153.115 122.847 111.885 1.00 33.56 ?  343 LEU A CD2   1 
ATOM   2784  N  N     . GLU A 1 344 ? 152.416 118.686 114.706 1.00 33.26 ?  344 GLU A N     1 
ATOM   2785  C  CA    . GLU A 1 344 ? 151.582 117.490 114.678 1.00 33.22 ?  344 GLU A CA    1 
ATOM   2786  C  C     . GLU A 1 344 ? 150.287 117.707 115.449 1.00 31.00 ?  344 GLU A C     1 
ATOM   2787  O  O     . GLU A 1 344 ? 149.225 117.228 115.038 1.00 34.27 ?  344 GLU A O     1 
ATOM   2788  C  CB    . GLU A 1 344 ? 152.355 116.298 115.241 1.00 30.91 ?  344 GLU A CB    1 
ATOM   2789  C  CG    . GLU A 1 344 ? 153.537 115.869 114.385 1.00 34.30 ?  344 GLU A CG    1 
ATOM   2790  C  CD    . GLU A 1 344 ? 154.616 115.164 115.184 1.00 41.97 ?  344 GLU A CD    1 
ATOM   2791  O  OE1   . GLU A 1 344 ? 154.346 114.781 116.342 1.00 44.43 ?  344 GLU A OE1   1 
ATOM   2792  O  OE2   . GLU A 1 344 ? 155.734 114.994 114.655 1.00 38.74 -1 344 GLU A OE2   1 
ATOM   2793  N  N     . LYS A 1 345 ? 150.358 118.418 116.576 1.00 29.36 ?  345 LYS A N     1 
ATOM   2794  C  CA    . LYS A 1 345 ? 149.147 118.740 117.325 1.00 28.66 ?  345 LYS A CA    1 
ATOM   2795  C  C     . LYS A 1 345 ? 148.222 119.637 116.514 1.00 31.02 ?  345 LYS A C     1 
ATOM   2796  O  O     . LYS A 1 345 ? 147.000 119.459 116.537 1.00 36.42 ?  345 LYS A O     1 
ATOM   2797  C  CB    . LYS A 1 345 ? 149.513 119.402 118.653 1.00 29.68 ?  345 LYS A CB    1 
ATOM   2798  C  CG    . LYS A 1 345 ? 148.315 119.882 119.451 1.00 30.37 ?  345 LYS A CG    1 
ATOM   2799  C  CD    . LYS A 1 345 ? 148.716 120.312 120.847 1.00 32.15 ?  345 LYS A CD    1 
ATOM   2800  C  CE    . LYS A 1 345 ? 147.509 120.759 121.651 1.00 36.64 ?  345 LYS A CE    1 
ATOM   2801  N  NZ    . LYS A 1 345 ? 147.866 121.073 123.060 1.00 33.99 1  345 LYS A NZ    1 
ATOM   2802  N  N     . LEU A 1 346 ? 148.788 120.610 115.798 1.00 30.76 ?  346 LEU A N     1 
ATOM   2803  C  CA    . LEU A 1 346 ? 147.983 121.451 114.917 1.00 25.94 ?  346 LEU A CA    1 
ATOM   2804  C  C     . LEU A 1 346 ? 147.282 120.612 113.858 1.00 28.41 ?  346 LEU A C     1 
ATOM   2805  O  O     . LEU A 1 346 ? 146.085 120.785 113.601 1.00 29.87 ?  346 LEU A O     1 
ATOM   2806  C  CB    . LEU A 1 346 ? 148.861 122.513 114.253 1.00 27.27 ?  346 LEU A CB    1 
ATOM   2807  C  CG    . LEU A 1 346 ? 149.456 123.628 115.112 1.00 29.07 ?  346 LEU A CG    1 
ATOM   2808  C  CD1   . LEU A 1 346 ? 150.432 124.451 114.293 1.00 29.73 ?  346 LEU A CD1   1 
ATOM   2809  C  CD2   . LEU A 1 346 ? 148.367 124.506 115.676 1.00 29.79 ?  346 LEU A CD2   1 
ATOM   2810  N  N     . ALA A 1 347 ? 148.018 119.691 113.233 1.00 30.42 ?  347 ALA A N     1 
ATOM   2811  C  CA    . ALA A 1 347 ? 147.425 118.843 112.203 1.00 26.76 ?  347 ALA A CA    1 
ATOM   2812  C  C     . ALA A 1 347 ? 146.321 117.964 112.776 1.00 32.78 ?  347 ALA A C     1 
ATOM   2813  O  O     . ALA A 1 347 ? 145.260 117.809 112.161 1.00 34.48 ?  347 ALA A O     1 
ATOM   2814  C  CB    . ALA A 1 347 ? 148.503 117.985 111.543 1.00 28.67 ?  347 ALA A CB    1 
ATOM   2815  N  N     . MET A 1 348 ? 146.553 117.381 113.953 1.00 35.83 ?  348 MET A N     1 
ATOM   2816  C  CA    . MET A 1 348 ? 145.541 116.539 114.583 1.00 34.31 ?  348 MET A CA    1 
ATOM   2817  C  C     . MET A 1 348 ? 144.295 117.342 114.937 1.00 34.62 ?  348 MET A C     1 
ATOM   2818  O  O     . MET A 1 348 ? 143.167 116.873 114.744 1.00 39.98 ?  348 MET A O     1 
ATOM   2819  C  CB    . MET A 1 348 ? 146.126 115.869 115.826 1.00 35.33 ?  348 MET A CB    1 
ATOM   2820  C  CG    . MET A 1 348 ? 145.109 115.155 116.694 1.00 42.25 ?  348 MET A CG    1 
ATOM   2821  S  SD    . MET A 1 348 ? 144.913 115.934 118.309 1.00 54.03 ?  348 MET A SD    1 
ATOM   2822  C  CE    . MET A 1 348 ? 146.594 115.871 118.920 1.00 37.83 ?  348 MET A CE    1 
ATOM   2823  N  N     . LEU A 1 349 ? 144.482 118.556 115.456 1.00 30.71 ?  349 LEU A N     1 
ATOM   2824  C  CA    . LEU A 1 349 ? 143.346 119.398 115.813 1.00 28.89 ?  349 LEU A CA    1 
ATOM   2825  C  C     . LEU A 1 349 ? 142.559 119.818 114.579 1.00 24.96 ?  349 LEU A C     1 
ATOM   2826  O  O     . LEU A 1 349 ? 141.328 119.893 114.622 1.00 29.91 ?  349 LEU A O     1 
ATOM   2827  C  CB    . LEU A 1 349 ? 143.828 120.621 116.590 1.00 31.98 ?  349 LEU A CB    1 
ATOM   2828  C  CG    . LEU A 1 349 ? 142.833 121.227 117.579 1.00 32.78 ?  349 LEU A CG    1 
ATOM   2829  C  CD1   . LEU A 1 349 ? 142.591 120.280 118.741 1.00 35.13 ?  349 LEU A CD1   1 
ATOM   2830  C  CD2   . LEU A 1 349 ? 143.324 122.577 118.072 1.00 28.86 ?  349 LEU A CD2   1 
ATOM   2831  N  N     . ARG A 1 350 ? 143.249 120.112 113.474 1.00 27.26 ?  350 ARG A N     1 
ATOM   2832  C  CA    . ARG A 1 350 ? 142.537 120.449 112.245 1.00 26.52 ?  350 ARG A CA    1 
ATOM   2833  C  C     . ARG A 1 350 ? 141.813 119.241 111.669 1.00 31.57 ?  350 ARG A C     1 
ATOM   2834  O  O     . ARG A 1 350 ? 140.730 119.386 111.092 1.00 35.26 ?  350 ARG A O     1 
ATOM   2835  C  CB    . ARG A 1 350 ? 143.500 121.034 111.212 1.00 24.25 ?  350 ARG A CB    1 
ATOM   2836  C  CG    . ARG A 1 350 ? 144.231 122.279 111.675 1.00 27.97 ?  350 ARG A CG    1 
ATOM   2837  C  CD    . ARG A 1 350 ? 144.930 122.971 110.523 1.00 29.70 ?  350 ARG A CD    1 
ATOM   2838  N  NE    . ARG A 1 350 ? 144.087 124.010 109.945 1.00 36.09 ?  350 ARG A NE    1 
ATOM   2839  C  CZ    . ARG A 1 350 ? 143.950 124.230 108.647 1.00 34.03 ?  350 ARG A CZ    1 
ATOM   2840  N  NH1   . ARG A 1 350 ? 144.590 123.500 107.750 1.00 30.09 1  350 ARG A NH1   1 
ATOM   2841  N  NH2   . ARG A 1 350 ? 143.143 125.206 108.237 1.00 30.10 ?  350 ARG A NH2   1 
ATOM   2842  N  N     . SER A 1 351 ? 142.396 118.048 111.801 1.00 35.31 ?  351 SER A N     1 
ATOM   2843  C  CA    . SER A 1 351 ? 141.717 116.840 111.348 1.00 32.15 ?  351 SER A CA    1 
ATOM   2844  C  C     . SER A 1 351 ? 140.459 116.572 112.162 1.00 37.40 ?  351 SER A C     1 
ATOM   2845  O  O     . SER A 1 351 ? 139.420 116.199 111.607 1.00 43.54 ?  351 SER A O     1 
ATOM   2846  C  CB    . SER A 1 351 ? 142.667 115.646 111.425 1.00 34.90 ?  351 SER A CB    1 
ATOM   2847  O  OG    . SER A 1 351 ? 143.717 115.767 110.482 1.00 45.11 ?  351 SER A OG    1 
ATOM   2848  N  N     . GLU A 1 352 ? 140.531 116.753 113.480 1.00 34.86 ?  352 GLU A N     1 
ATOM   2849  C  CA    . GLU A 1 352 ? 139.416 116.400 114.347 1.00 32.54 ?  352 GLU A CA    1 
ATOM   2850  C  C     . GLU A 1 352 ? 138.361 117.494 114.465 1.00 37.94 ?  352 GLU A C     1 
ATOM   2851  O  O     . GLU A 1 352 ? 137.208 117.185 114.784 1.00 46.70 ?  352 GLU A O     1 
ATOM   2852  C  CB    . GLU A 1 352 ? 139.932 116.030 115.743 1.00 38.24 ?  352 GLU A CB    1 
ATOM   2853  C  CG    . GLU A 1 352 ? 140.020 117.188 116.720 1.00 41.92 ?  352 GLU A CG    1 
ATOM   2854  C  CD    . GLU A 1 352 ? 140.578 116.773 118.065 1.00 45.83 ?  352 GLU A CD    1 
ATOM   2855  O  OE1   . GLU A 1 352 ? 141.613 116.075 118.092 1.00 43.39 ?  352 GLU A OE1   1 
ATOM   2856  O  OE2   . GLU A 1 352 ? 139.980 117.142 119.098 1.00 46.21 -1 352 GLU A OE2   1 
ATOM   2857  N  N     . SER A 1 353 ? 138.714 118.757 114.222 1.00 35.27 ?  353 SER A N     1 
ATOM   2858  C  CA    . SER A 1 353 ? 137.759 119.847 114.378 1.00 36.63 ?  353 SER A CA    1 
ATOM   2859  C  C     . SER A 1 353 ? 137.806 120.898 113.280 1.00 32.80 ?  353 SER A C     1 
ATOM   2860  O  O     . SER A 1 353 ? 136.877 121.709 113.206 1.00 32.09 ?  353 SER A O     1 
ATOM   2861  C  CB    . SER A 1 353 ? 137.969 120.544 115.730 1.00 35.94 ?  353 SER A CB    1 
ATOM   2862  O  OG    . SER A 1 353 ? 139.253 121.137 115.804 1.00 33.36 ?  353 SER A OG    1 
ATOM   2863  N  N     . GLY A 1 354 ? 138.833 120.927 112.434 1.00 25.10 ?  354 GLY A N     1 
ATOM   2864  C  CA    . GLY A 1 354 ? 138.990 121.975 111.452 1.00 27.40 ?  354 GLY A CA    1 
ATOM   2865  C  C     . GLY A 1 354 ? 139.728 123.200 111.945 1.00 23.52 ?  354 GLY A C     1 
ATOM   2866  O  O     . GLY A 1 354 ? 140.029 124.088 111.139 1.00 29.14 ?  354 GLY A O     1 
ATOM   2867  N  N     . TYR A 1 355 ? 140.037 123.271 113.236 1.00 22.42 ?  355 TYR A N     1 
ATOM   2868  C  CA    . TYR A 1 355 ? 140.724 124.368 113.888 1.00 16.59 ?  355 TYR A CA    1 
ATOM   2869  C  C     . TYR A 1 355 ? 142.137 123.951 114.278 1.00 22.01 ?  355 TYR A C     1 
ATOM   2870  O  O     . TYR A 1 355 ? 142.400 122.765 114.485 1.00 27.95 ?  355 TYR A O     1 
ATOM   2871  C  CB    . TYR A 1 355 ? 139.963 124.823 115.139 1.00 23.87 ?  355 TYR A CB    1 
ATOM   2872  C  CG    . TYR A 1 355 ? 138.625 125.452 114.840 1.00 28.43 ?  355 TYR A CG    1 
ATOM   2873  C  CD1   . TYR A 1 355 ? 138.523 126.532 113.975 1.00 21.92 ?  355 TYR A CD1   1 
ATOM   2874  C  CD2   . TYR A 1 355 ? 137.463 124.965 115.420 1.00 30.32 ?  355 TYR A CD2   1 
ATOM   2875  C  CE1   . TYR A 1 355 ? 137.304 127.107 113.697 1.00 28.77 ?  355 TYR A CE1   1 
ATOM   2876  C  CE2   . TYR A 1 355 ? 136.239 125.536 115.148 1.00 26.19 ?  355 TYR A CE2   1 
ATOM   2877  C  CZ    . TYR A 1 355 ? 136.164 126.607 114.287 1.00 29.94 ?  355 TYR A CZ    1 
ATOM   2878  O  OH    . TYR A 1 355 ? 134.945 127.179 114.014 1.00 31.97 ?  355 TYR A OH    1 
ATOM   2879  N  N     . PRO A 1 356 ? 143.075 124.896 114.398 1.00 30.72 ?  356 PRO A N     1 
ATOM   2880  C  CA    . PRO A 1 356 ? 142.948 126.346 114.228 1.00 15.39 ?  356 PRO A CA    1 
ATOM   2881  C  C     . PRO A 1 356 ? 143.092 126.813 112.788 1.00 15.29 ?  356 PRO A C     1 
ATOM   2882  O  O     . PRO A 1 356 ? 143.542 126.070 111.922 1.00 24.86 ?  356 PRO A O     1 
ATOM   2883  C  CB    . PRO A 1 356 ? 144.092 126.877 115.092 1.00 17.74 ?  356 PRO A CB    1 
ATOM   2884  C  CG    . PRO A 1 356 ? 145.164 125.852 114.896 1.00 22.45 ?  356 PRO A CG    1 
ATOM   2885  C  CD    . PRO A 1 356 ? 144.445 124.525 114.795 1.00 19.53 ?  356 PRO A CD    1 
ATOM   2886  N  N     . TYR A 1 357 ? 142.693 128.050 112.508 1.00 24.77 ?  357 TYR A N     1 
ATOM   2887  C  CA    . TYR A 1 357 ? 143.129 128.707 111.288 1.00 12.22 ?  357 TYR A CA    1 
ATOM   2888  C  C     . TYR A 1 357 ? 144.634 128.916 111.355 1.00 13.71 ?  357 TYR A C     1 
ATOM   2889  O  O     . TYR A 1 357 ? 145.186 129.202 112.418 1.00 26.45 ?  357 TYR A O     1 
ATOM   2890  C  CB    . TYR A 1 357 ? 142.424 130.053 111.113 1.00 13.47 ?  357 TYR A CB    1 
ATOM   2891  C  CG    . TYR A 1 357 ? 140.921 130.016 111.255 1.00 15.80 ?  357 TYR A CG    1 
ATOM   2892  C  CD1   . TYR A 1 357 ? 140.197 128.890 110.905 1.00 17.54 ?  357 TYR A CD1   1 
ATOM   2893  C  CD2   . TYR A 1 357 ? 140.225 131.116 111.732 1.00 18.09 ?  357 TYR A CD2   1 
ATOM   2894  C  CE1   . TYR A 1 357 ? 138.825 128.854 111.027 1.00 20.23 ?  357 TYR A CE1   1 
ATOM   2895  C  CE2   . TYR A 1 357 ? 138.854 131.090 111.859 1.00 15.86 ?  357 TYR A CE2   1 
ATOM   2896  C  CZ    . TYR A 1 357 ? 138.158 129.957 111.504 1.00 19.73 ?  357 TYR A CZ    1 
ATOM   2897  O  OH    . TYR A 1 357 ? 136.789 129.925 111.627 1.00 28.22 ?  357 TYR A OH    1 
ATOM   2898  N  N     . ILE A 1 358 ? 145.306 128.762 110.221 1.00 16.22 ?  358 ILE A N     1 
ATOM   2899  C  CA    . ILE A 1 358 ? 146.755 128.899 110.153 1.00 22.30 ?  358 ILE A CA    1 
ATOM   2900  C  C     . ILE A 1 358 ? 147.075 130.159 109.365 1.00 18.25 ?  358 ILE A C     1 
ATOM   2901  O  O     . ILE A 1 358 ? 146.687 130.283 108.198 1.00 20.96 ?  358 ILE A O     1 
ATOM   2902  C  CB    . ILE A 1 358 ? 147.419 127.669 109.517 1.00 22.40 ?  358 ILE A CB    1 
ATOM   2903  C  CG1   . ILE A 1 358 ? 147.037 126.394 110.272 1.00 19.24 ?  358 ILE A CG1   1 
ATOM   2904  C  CG2   . ILE A 1 358 ? 148.928 127.841 109.481 1.00 16.40 ?  358 ILE A CG2   1 
ATOM   2905  C  CD1   . ILE A 1 358 ? 147.259 126.474 111.760 1.00 19.28 ?  358 ILE A CD1   1 
ATOM   2906  N  N     . MET A 1 359 ? 147.778 131.089 110.000 1.00 15.72 ?  359 MET A N     1 
ATOM   2907  C  CA    . MET A 1 359 ? 148.289 132.281 109.338 1.00 9.17  ?  359 MET A CA    1 
ATOM   2908  C  C     . MET A 1 359 ? 149.806 132.202 109.303 1.00 11.86 ?  359 MET A C     1 
ATOM   2909  O  O     . MET A 1 359 ? 150.450 132.123 110.352 1.00 21.73 ?  359 MET A O     1 
ATOM   2910  C  CB    . MET A 1 359 ? 147.838 133.555 110.051 1.00 11.58 ?  359 MET A CB    1 
ATOM   2911  C  CG    . MET A 1 359 ? 148.191 134.819 109.291 1.00 12.28 ?  359 MET A CG    1 
ATOM   2912  S  SD    . MET A 1 359 ? 147.865 136.328 110.209 1.00 30.94 ?  359 MET A SD    1 
ATOM   2913  C  CE    . MET A 1 359 ? 149.453 137.138 110.102 1.00 9.99  ?  359 MET A CE    1 
ATOM   2914  N  N     . PHE A 1 360 ? 150.371 132.227 108.102 1.00 12.36 ?  360 PHE A N     1 
ATOM   2915  C  CA    . PHE A 1 360 ? 151.820 132.246 107.927 1.00 10.56 ?  360 PHE A CA    1 
ATOM   2916  C  C     . PHE A 1 360 ? 152.251 133.705 107.926 1.00 14.38 ?  360 PHE A C     1 
ATOM   2917  O  O     . PHE A 1 360 ? 152.160 134.392 106.907 1.00 20.45 ?  360 PHE A O     1 
ATOM   2918  C  CB    . PHE A 1 360 ? 152.213 131.518 106.649 1.00 14.32 ?  360 PHE A CB    1 
ATOM   2919  C  CG    . PHE A 1 360 ? 151.865 130.058 106.665 1.00 19.70 ?  360 PHE A CG    1 
ATOM   2920  C  CD1   . PHE A 1 360 ? 152.379 129.222 107.640 1.00 19.15 ?  360 PHE A CD1   1 
ATOM   2921  C  CD2   . PHE A 1 360 ? 151.006 129.528 105.720 1.00 14.52 ?  360 PHE A CD2   1 
ATOM   2922  C  CE1   . PHE A 1 360 ? 152.055 127.883 107.663 1.00 19.62 ?  360 PHE A CE1   1 
ATOM   2923  C  CE2   . PHE A 1 360 ? 150.679 128.191 105.739 1.00 15.20 ?  360 PHE A CE2   1 
ATOM   2924  C  CZ    . PHE A 1 360 ? 151.202 127.367 106.711 1.00 17.18 ?  360 PHE A CZ    1 
ATOM   2925  N  N     . GLN A 1 361 ? 152.730 134.172 109.082 1.00 17.83 ?  361 GLN A N     1 
ATOM   2926  C  CA    . GLN A 1 361 ? 152.904 135.604 109.308 1.00 10.93 ?  361 GLN A CA    1 
ATOM   2927  C  C     . GLN A 1 361 ? 153.919 136.211 108.348 1.00 17.63 ?  361 GLN A C     1 
ATOM   2928  O  O     . GLN A 1 361 ? 153.708 137.312 107.828 1.00 22.44 ?  361 GLN A O     1 
ATOM   2929  C  CB    . GLN A 1 361 ? 153.317 135.844 110.759 1.00 19.39 ?  361 GLN A CB    1 
ATOM   2930  C  CG    . GLN A 1 361 ? 153.935 137.199 111.029 1.00 22.88 ?  361 GLN A CG    1 
ATOM   2931  C  CD    . GLN A 1 361 ? 153.323 137.874 112.237 1.00 22.79 ?  361 GLN A CD    1 
ATOM   2932  O  OE1   . GLN A 1 361 ? 153.225 137.281 113.308 1.00 24.42 ?  361 GLN A OE1   1 
ATOM   2933  N  NE2   . GLN A 1 361 ? 152.902 139.121 112.068 1.00 23.32 ?  361 GLN A NE2   1 
ATOM   2934  N  N     . ASP A 1 362 ? 155.028 135.515 108.100 1.00 25.25 ?  362 ASP A N     1 
ATOM   2935  C  CA    . ASP A 1 362 ? 156.031 136.045 107.186 1.00 18.40 ?  362 ASP A CA    1 
ATOM   2936  C  C     . ASP A 1 362 ? 155.596 135.954 105.731 1.00 17.69 ?  362 ASP A C     1 
ATOM   2937  O  O     . ASP A 1 362 ? 156.115 136.702 104.897 1.00 28.33 ?  362 ASP A O     1 
ATOM   2938  C  CB    . ASP A 1 362 ? 157.362 135.324 107.383 1.00 24.85 ?  362 ASP A CB    1 
ATOM   2939  C  CG    . ASP A 1 362 ? 157.964 135.585 108.747 1.00 31.03 ?  362 ASP A CG    1 
ATOM   2940  O  OD1   . ASP A 1 362 ? 157.324 135.238 109.759 1.00 29.17 ?  362 ASP A OD1   1 
ATOM   2941  O  OD2   . ASP A 1 362 ? 159.076 136.149 108.804 1.00 33.69 -1 362 ASP A OD2   1 
ATOM   2942  N  N     . ASN A 1 363 ? 154.668 135.053 105.406 1.00 24.62 ?  363 ASN A N     1 
ATOM   2943  C  CA    . ASN A 1 363 ? 154.088 135.049 104.067 1.00 14.12 ?  363 ASN A CA    1 
ATOM   2944  C  C     . ASN A 1 363 ? 153.194 136.262 103.861 1.00 18.06 ?  363 ASN A C     1 
ATOM   2945  O  O     . ASN A 1 363 ? 153.130 136.817 102.758 1.00 28.52 ?  363 ASN A O     1 
ATOM   2946  C  CB    . ASN A 1 363 ? 153.301 133.759 103.840 1.00 12.26 ?  363 ASN A CB    1 
ATOM   2947  C  CG    . ASN A 1 363 ? 154.179 132.612 103.396 1.00 18.23 ?  363 ASN A CG    1 
ATOM   2948  O  OD1   . ASN A 1 363 ? 155.320 132.811 102.988 1.00 21.41 ?  363 ASN A OD1   1 
ATOM   2949  N  ND2   . ASN A 1 363 ? 153.650 131.398 103.477 1.00 20.23 ?  363 ASN A ND2   1 
ATOM   2950  N  N     . VAL A 1 364 ? 152.490 136.681 104.911 1.00 14.61 ?  364 VAL A N     1 
ATOM   2951  C  CA    . VAL A 1 364 ? 151.645 137.865 104.824 1.00 9.24  ?  364 VAL A CA    1 
ATOM   2952  C  C     . VAL A 1 364 ? 152.492 139.128 104.739 1.00 16.15 ?  364 VAL A C     1 
ATOM   2953  O  O     . VAL A 1 364 ? 152.201 140.035 103.952 1.00 19.34 ?  364 VAL A O     1 
ATOM   2954  C  CB    . VAL A 1 364 ? 150.680 137.915 106.021 1.00 1.23  ?  364 VAL A CB    1 
ATOM   2955  C  CG1   . VAL A 1 364 ? 149.721 139.076 105.875 1.00 9.60  ?  364 VAL A CG1   1 
ATOM   2956  C  CG2   . VAL A 1 364 ? 149.933 136.606 106.151 1.00 6.84  ?  364 VAL A CG2   1 
ATOM   2957  N  N     . ASN A 1 365 ? 153.553 139.207 105.541 1.00 22.21 ?  365 ASN A N     1 
ATOM   2958  C  CA    . ASN A 1 365 ? 154.257 140.463 105.747 1.00 11.29 ?  365 ASN A CA    1 
ATOM   2959  C  C     . ASN A 1 365 ? 155.406 140.694 104.779 1.00 14.01 ?  365 ASN A C     1 
ATOM   2960  O  O     . ASN A 1 365 ? 155.878 141.831 104.670 1.00 23.15 ?  365 ASN A O     1 
ATOM   2961  C  CB    . ASN A 1 365 ? 154.783 140.538 107.182 1.00 17.60 ?  365 ASN A CB    1 
ATOM   2962  C  CG    . ASN A 1 365 ? 153.702 140.904 108.172 1.00 16.59 ?  365 ASN A CG    1 
ATOM   2963  O  OD1   . ASN A 1 365 ? 153.011 141.907 108.008 1.00 22.15 ?  365 ASN A OD1   1 
ATOM   2964  N  ND2   . ASN A 1 365 ? 153.545 140.090 109.205 1.00 15.77 ?  365 ASN A ND2   1 
ATOM   2965  N  N     . LYS A 1 366 ? 155.873 139.661 104.076 1.00 19.65 ?  366 LYS A N     1 
ATOM   2966  C  CA    . LYS A 1 366 ? 156.905 139.881 103.072 1.00 22.10 ?  366 LYS A CA    1 
ATOM   2967  C  C     . LYS A 1 366 ? 156.356 140.586 101.841 1.00 24.85 ?  366 LYS A C     1 
ATOM   2968  O  O     . LYS A 1 366 ? 157.125 141.204 101.097 1.00 30.20 ?  366 LYS A O     1 
ATOM   2969  C  CB    . LYS A 1 366 ? 157.557 138.555 102.677 1.00 18.14 ?  366 LYS A CB    1 
ATOM   2970  C  CG    . LYS A 1 366 ? 156.670 137.631 101.865 1.00 27.92 ?  366 LYS A CG    1 
ATOM   2971  C  CD    . LYS A 1 366 ? 157.501 136.644 101.063 1.00 29.61 ?  366 LYS A CD    1 
ATOM   2972  C  CE    . LYS A 1 366 ? 157.993 135.498 101.933 1.00 24.39 ?  366 LYS A CE    1 
ATOM   2973  N  NZ    . LYS A 1 366 ? 159.180 134.826 101.337 1.00 31.12 1  366 LYS A NZ    1 
ATOM   2974  N  N     . VAL A 1 367 ? 155.045 140.512 101.618 1.00 24.91 ?  367 VAL A N     1 
ATOM   2975  C  CA    . VAL A 1 367 ? 154.377 141.219 100.535 1.00 13.81 ?  367 VAL A CA    1 
ATOM   2976  C  C     . VAL A 1 367 ? 153.424 142.287 101.043 1.00 21.55 ?  367 VAL A C     1 
ATOM   2977  O  O     . VAL A 1 367 ? 152.768 142.950 100.234 1.00 26.26 ?  367 VAL A O     1 
ATOM   2978  C  CB    . VAL A 1 367 ? 153.632 140.238 99.607  1.00 16.64 ?  367 VAL A CB    1 
ATOM   2979  C  CG1   . VAL A 1 367 ? 154.609 139.544 98.680  1.00 22.54 ?  367 VAL A CG1   1 
ATOM   2980  C  CG2   . VAL A 1 367 ? 152.872 139.219 100.428 1.00 13.91 ?  367 VAL A CG2   1 
ATOM   2981  N  N     . HIS A 1 368 ? 153.325 142.469 102.358 1.00 21.75 ?  368 HIS A N     1 
ATOM   2982  C  CA    . HIS A 1 368 ? 152.428 143.464 102.927 1.00 9.89  ?  368 HIS A CA    1 
ATOM   2983  C  C     . HIS A 1 368 ? 152.872 144.867 102.531 1.00 14.33 ?  368 HIS A C     1 
ATOM   2984  O  O     . HIS A 1 368 ? 154.050 145.214 102.648 1.00 24.79 ?  368 HIS A O     1 
ATOM   2985  C  CB    . HIS A 1 368 ? 152.392 143.322 104.445 1.00 8.77  ?  368 HIS A CB    1 
ATOM   2986  C  CG    . HIS A 1 368 ? 151.451 144.267 105.122 1.00 10.72 ?  368 HIS A CG    1 
ATOM   2987  N  ND1   . HIS A 1 368 ? 151.665 144.738 106.399 1.00 18.69 ?  368 HIS A ND1   1 
ATOM   2988  C  CD2   . HIS A 1 368 ? 150.290 144.823 104.706 1.00 6.90  ?  368 HIS A CD2   1 
ATOM   2989  C  CE1   . HIS A 1 368 ? 150.677 145.545 106.739 1.00 16.05 ?  368 HIS A CE1   1 
ATOM   2990  N  NE2   . HIS A 1 368 ? 149.830 145.614 105.729 1.00 10.79 ?  368 HIS A NE2   1 
ATOM   2991  N  N     . ALA A 1 369 ? 151.920 145.673 102.064 1.00 18.19 ?  369 ALA A N     1 
ATOM   2992  C  CA    . ALA A 1 369 ? 152.236 146.990 101.529 1.00 9.05  ?  369 ALA A CA    1 
ATOM   2993  C  C     . ALA A 1 369 ? 152.307 148.074 102.595 1.00 20.16 ?  369 ALA A C     1 
ATOM   2994  O  O     . ALA A 1 369 ? 152.817 149.163 102.314 1.00 24.96 ?  369 ALA A O     1 
ATOM   2995  C  CB    . ALA A 1 369 ? 151.202 147.384 100.474 1.00 14.58 ?  369 ALA A CB    1 
ATOM   2996  N  N     . ASN A 1 370 ? 151.822 147.809 103.803 1.00 19.06 ?  370 ASN A N     1 
ATOM   2997  C  CA    . ASN A 1 370 ? 151.716 148.822 104.847 1.00 9.80  ?  370 ASN A CA    1 
ATOM   2998  C  C     . ASN A 1 370 ? 152.394 148.352 106.122 1.00 8.58  ?  370 ASN A C     1 
ATOM   2999  O  O     . ASN A 1 370 ? 151.854 148.470 107.224 1.00 18.09 ?  370 ASN A O     1 
ATOM   3000  C  CB    . ASN A 1 370 ? 150.257 149.176 105.113 1.00 10.11 ?  370 ASN A CB    1 
ATOM   3001  C  CG    . ASN A 1 370 ? 149.553 149.698 103.882 1.00 12.97 ?  370 ASN A CG    1 
ATOM   3002  O  OD1   . ASN A 1 370 ? 149.979 150.682 103.282 1.00 28.26 ?  370 ASN A OD1   1 
ATOM   3003  N  ND2   . ASN A 1 370 ? 148.468 149.041 103.497 1.00 13.93 ?  370 ASN A ND2   1 
ATOM   3004  N  N     . ASN A 1 371 ? 153.603 147.805 105.989 1.00 17.89 ?  371 ASN A N     1 
ATOM   3005  C  CA    . ASN A 1 371 ? 154.359 147.401 107.168 1.00 11.60 ?  371 ASN A CA    1 
ATOM   3006  C  C     . ASN A 1 371 ? 154.836 148.595 107.982 1.00 19.41 ?  371 ASN A C     1 
ATOM   3007  O  O     . ASN A 1 371 ? 155.133 148.439 109.170 1.00 22.71 ?  371 ASN A O     1 
ATOM   3008  C  CB    . ASN A 1 371 ? 155.556 146.542 106.763 1.00 6.17  ?  371 ASN A CB    1 
ATOM   3009  C  CG    . ASN A 1 371 ? 155.191 145.088 106.572 1.00 15.84 ?  371 ASN A CG    1 
ATOM   3010  O  OD1   . ASN A 1 371 ? 154.205 144.606 107.124 1.00 23.36 ?  371 ASN A OD1   1 
ATOM   3011  N  ND2   . ASN A 1 371 ? 155.988 144.379 105.785 1.00 18.12 ?  371 ASN A ND2   1 
ATOM   3012  N  N     . HIS A 1 372 ? 154.921 149.776 107.367 1.00 20.00 ?  372 HIS A N     1 
ATOM   3013  C  CA    . HIS A 1 372 ? 155.276 150.979 108.112 1.00 17.08 ?  372 HIS A CA    1 
ATOM   3014  C  C     . HIS A 1 372 ? 154.221 151.307 109.161 1.00 20.55 ?  372 HIS A C     1 
ATOM   3015  O  O     . HIS A 1 372 ? 154.555 151.706 110.282 1.00 30.06 ?  372 HIS A O     1 
ATOM   3016  C  CB    . HIS A 1 372 ? 155.466 152.152 107.151 1.00 18.82 ?  372 HIS A CB    1 
ATOM   3017  C  CG    . HIS A 1 372 ? 154.201 152.597 106.488 1.00 19.92 ?  372 HIS A CG    1 
ATOM   3018  N  ND1   . HIS A 1 372 ? 153.469 151.777 105.658 1.00 19.60 ?  372 HIS A ND1   1 
ATOM   3019  C  CD2   . HIS A 1 372 ? 153.531 153.772 106.542 1.00 23.20 ?  372 HIS A CD2   1 
ATOM   3020  C  CE1   . HIS A 1 372 ? 152.406 152.428 105.224 1.00 18.35 ?  372 HIS A CE1   1 
ATOM   3021  N  NE2   . HIS A 1 372 ? 152.420 153.640 105.745 1.00 23.99 ?  372 HIS A NE2   1 
ATOM   3022  N  N     . ILE A 1 373 ? 152.942 151.159 108.812 1.00 14.86 ?  373 ILE A N     1 
ATOM   3023  C  CA    . ILE A 1 373 ? 151.881 151.344 109.793 1.00 16.32 ?  373 ILE A CA    1 
ATOM   3024  C  C     . ILE A 1 373 ? 151.973 150.276 110.873 1.00 19.30 ?  373 ILE A C     1 
ATOM   3025  O  O     . ILE A 1 373 ? 152.002 150.578 112.071 1.00 29.97 ?  373 ILE A O     1 
ATOM   3026  C  CB    . ILE A 1 373 ? 150.505 151.329 109.103 1.00 17.88 ?  373 ILE A CB    1 
ATOM   3027  C  CG1   . ILE A 1 373 ? 150.406 152.457 108.077 1.00 16.77 ?  373 ILE A CG1   1 
ATOM   3028  C  CG2   . ILE A 1 373 ? 149.388 151.437 110.129 1.00 17.56 ?  373 ILE A CG2   1 
ATOM   3029  C  CD1   . ILE A 1 373 ? 149.222 152.334 107.149 1.00 13.85 ?  373 ILE A CD1   1 
ATOM   3030  N  N     . SER A 1 374 ? 152.049 149.014 110.460 1.00 20.52 ?  374 SER A N     1 
ATOM   3031  C  CA    . SER A 1 374 ? 152.133 147.868 111.353 1.00 12.72 ?  374 SER A CA    1 
ATOM   3032  C  C     . SER A 1 374 ? 152.270 146.617 110.501 1.00 15.89 ?  374 SER A C     1 
ATOM   3033  O  O     . SER A 1 374 ? 151.932 146.615 109.315 1.00 16.80 ?  374 SER A O     1 
ATOM   3034  C  CB    . SER A 1 374 ? 150.905 147.754 112.258 1.00 17.29 ?  374 SER A CB    1 
ATOM   3035  O  OG    . SER A 1 374 ? 151.071 146.724 113.211 1.00 25.82 ?  374 SER A OG    1 
ATOM   3036  N  N     . LYS A 1 375 ? 152.769 145.556 111.118 1.00 22.63 ?  375 LYS A N     1 
ATOM   3037  C  CA    . LYS A 1 375 ? 152.737 144.246 110.491 1.00 15.46 ?  375 LYS A CA    1 
ATOM   3038  C  C     . LYS A 1 375 ? 151.389 143.585 110.741 1.00 14.23 ?  375 LYS A C     1 
ATOM   3039  O  O     . LYS A 1 375 ? 150.713 143.862 111.736 1.00 25.63 ?  375 LYS A O     1 
ATOM   3040  C  CB    . LYS A 1 375 ? 153.858 143.358 111.029 1.00 11.70 ?  375 LYS A CB    1 
ATOM   3041  C  CG    . LYS A 1 375 ? 155.234 143.978 110.944 1.00 19.34 ?  375 LYS A CG    1 
ATOM   3042  C  CD    . LYS A 1 375 ? 156.108 143.218 109.970 1.00 19.61 ?  375 LYS A CD    1 
ATOM   3043  C  CE    . LYS A 1 375 ? 157.411 143.945 109.706 1.00 20.30 ?  375 LYS A CE    1 
ATOM   3044  N  NZ    . LYS A 1 375 ? 158.131 143.366 108.540 1.00 25.16 1  375 LYS A NZ    1 
ATOM   3045  N  N     . VAL A 1 376 ? 150.994 142.711 109.820 1.00 11.48 ?  376 VAL A N     1 
ATOM   3046  C  CA    . VAL A 1 376 ? 149.774 141.941 110.019 1.00 17.46 ?  376 VAL A CA    1 
ATOM   3047  C  C     . VAL A 1 376 ? 150.045 140.881 111.077 1.00 14.05 ?  376 VAL A C     1 
ATOM   3048  O  O     . VAL A 1 376 ? 150.948 140.050 110.928 1.00 20.12 ?  376 VAL A O     1 
ATOM   3049  C  CB    . VAL A 1 376 ? 149.298 141.312 108.704 1.00 12.52 ?  376 VAL A CB    1 
ATOM   3050  C  CG1   . VAL A 1 376 ? 147.989 140.577 108.918 1.00 13.55 ?  376 VAL A CG1   1 
ATOM   3051  C  CG2   . VAL A 1 376 ? 149.148 142.375 107.635 1.00 3.43  ?  376 VAL A CG2   1 
ATOM   3052  N  N     . LYS A 1 377 ? 149.268 140.912 112.159 1.00 17.05 ?  377 LYS A N     1 
ATOM   3053  C  CA    . LYS A 1 377 ? 149.475 140.001 113.273 1.00 10.87 ?  377 LYS A CA    1 
ATOM   3054  C  C     . LYS A 1 377 ? 148.401 138.939 113.406 1.00 11.62 ?  377 LYS A C     1 
ATOM   3055  O  O     . LYS A 1 377 ? 148.618 137.962 114.126 1.00 27.28 ?  377 LYS A O     1 
ATOM   3056  C  CB    . LYS A 1 377 ? 149.557 140.776 114.595 1.00 13.24 ?  377 LYS A CB    1 
ATOM   3057  C  CG    . LYS A 1 377 ? 150.457 141.990 114.560 1.00 11.59 ?  377 LYS A CG    1 
ATOM   3058  C  CD    . LYS A 1 377 ? 150.013 142.998 115.596 1.00 22.02 ?  377 LYS A CD    1 
ATOM   3059  C  CE    . LYS A 1 377 ? 150.248 144.413 115.130 1.00 18.69 ?  377 LYS A CE    1 
ATOM   3060  N  NZ    . LYS A 1 377 ? 149.556 145.396 116.006 1.00 20.26 1  377 LYS A NZ    1 
ATOM   3061  N  N     . PHE A 1 378 ? 147.256 139.106 112.753 1.00 13.99 ?  378 PHE A N     1 
ATOM   3062  C  CA    . PHE A 1 378 ? 146.192 138.117 112.825 1.00 7.50  ?  378 PHE A CA    1 
ATOM   3063  C  C     . PHE A 1 378 ? 145.224 138.353 111.678 1.00 10.29 ?  378 PHE A C     1 
ATOM   3064  O  O     . PHE A 1 378 ? 145.241 139.403 111.032 1.00 18.96 ?  378 PHE A O     1 
ATOM   3065  C  CB    . PHE A 1 378 ? 145.468 138.150 114.181 1.00 6.96  ?  378 PHE A CB    1 
ATOM   3066  C  CG    . PHE A 1 378 ? 144.638 139.383 114.421 1.00 6.75  ?  378 PHE A CG    1 
ATOM   3067  C  CD1   . PHE A 1 378 ? 145.173 140.651 114.268 1.00 10.61 ?  378 PHE A CD1   1 
ATOM   3068  C  CD2   . PHE A 1 378 ? 143.324 139.267 114.836 1.00 4.93  ?  378 PHE A CD2   1 
ATOM   3069  C  CE1   . PHE A 1 378 ? 144.410 141.772 114.505 1.00 8.34  ?  378 PHE A CE1   1 
ATOM   3070  C  CE2   . PHE A 1 378 ? 142.558 140.385 115.075 1.00 10.30 ?  378 PHE A CE2   1 
ATOM   3071  C  CZ    . PHE A 1 378 ? 143.103 141.638 114.910 1.00 8.75  ?  378 PHE A CZ    1 
ATOM   3072  N  N     . SER A 1 379 ? 144.389 137.354 111.428 1.00 5.32  ?  379 SER A N     1 
ATOM   3073  C  CA    . SER A 1 379 ? 143.388 137.397 110.377 1.00 7.81  ?  379 SER A CA    1 
ATOM   3074  C  C     . SER A 1 379 ? 142.004 137.525 111.003 1.00 8.33  ?  379 SER A C     1 
ATOM   3075  O  O     . SER A 1 379 ? 141.859 137.690 112.218 1.00 16.72 ?  379 SER A O     1 
ATOM   3076  C  CB    . SER A 1 379 ? 143.504 136.160 109.484 1.00 13.39 ?  379 SER A CB    1 
ATOM   3077  O  OG    . SER A 1 379 ? 143.089 136.454 108.165 1.00 14.39 ?  379 SER A OG    1 
ATOM   3078  N  N     . ASN A 1 380 ? 140.978 137.464 110.163 1.00 8.33  ?  380 ASN A N     1 
ATOM   3079  C  CA    . ASN A 1 380 ? 139.604 137.625 110.601 1.00 7.79  ?  380 ASN A CA    1 
ATOM   3080  C  C     . ASN A 1 380 ? 138.975 136.261 110.877 1.00 16.69 ?  380 ASN A C     1 
ATOM   3081  O  O     . ASN A 1 380 ? 139.646 135.225 110.879 1.00 19.66 ?  380 ASN A O     1 
ATOM   3082  C  CB    . ASN A 1 380 ? 138.812 138.419 109.563 1.00 10.47 ?  380 ASN A CB    1 
ATOM   3083  C  CG    . ASN A 1 380 ? 138.697 137.699 108.240 1.00 7.14  ?  380 ASN A CG    1 
ATOM   3084  O  OD1   . ASN A 1 380 ? 139.656 137.098 107.762 1.00 18.25 ?  380 ASN A OD1   1 
ATOM   3085  N  ND2   . ASN A 1 380 ? 137.519 137.759 107.639 1.00 14.30 ?  380 ASN A ND2   1 
ATOM   3086  N  N     . LEU A 1 381 ? 137.665 136.261 111.126 1.00 17.42 ?  381 LEU A N     1 
ATOM   3087  C  CA    . LEU A 1 381 ? 136.951 135.014 111.373 1.00 10.98 ?  381 LEU A CA    1 
ATOM   3088  C  C     . LEU A 1 381 ? 136.926 134.127 110.135 1.00 10.10 ?  381 LEU A C     1 
ATOM   3089  O  O     . LEU A 1 381 ? 136.914 132.897 110.256 1.00 20.39 ?  381 LEU A O     1 
ATOM   3090  C  CB    . LEU A 1 381 ? 135.531 135.322 111.851 1.00 12.55 ?  381 LEU A CB    1 
ATOM   3091  C  CG    . LEU A 1 381 ? 134.530 134.176 111.989 1.00 14.65 ?  381 LEU A CG    1 
ATOM   3092  C  CD1   . LEU A 1 381 ? 134.872 133.289 113.171 1.00 16.28 ?  381 LEU A CD1   1 
ATOM   3093  C  CD2   . LEU A 1 381 ? 133.128 134.731 112.120 1.00 17.94 ?  381 LEU A CD2   1 
ATOM   3094  N  N     . CYS A 1 382 ? 136.919 134.721 108.946 1.00 18.94 ?  382 CYS A N     1 
ATOM   3095  C  CA    . CYS A 1 382 ? 136.970 133.968 107.703 1.00 13.00 ?  382 CYS A CA    1 
ATOM   3096  C  C     . CYS A 1 382 ? 138.392 133.750 107.205 1.00 7.71  ?  382 CYS A C     1 
ATOM   3097  O  O     . CYS A 1 382 ? 138.578 133.106 106.169 1.00 17.19 ?  382 CYS A O     1 
ATOM   3098  C  CB    . CYS A 1 382 ? 136.139 134.671 106.626 1.00 20.13 ?  382 CYS A CB    1 
ATOM   3099  S  SG    . CYS A 1 382 ? 134.433 135.008 107.111 1.00 26.50 ?  382 CYS A SG    1 
ATOM   3100  N  N     . SER A 1 383 ? 139.390 134.280 107.916 1.00 15.62 ?  383 SER A N     1 
ATOM   3101  C  CA    . SER A 1 383 ? 140.802 133.985 107.668 1.00 10.49 ?  383 SER A CA    1 
ATOM   3102  C  C     . SER A 1 383 ? 141.260 134.474 106.295 1.00 12.80 ?  383 SER A C     1 
ATOM   3103  O  O     . SER A 1 383 ? 142.059 133.823 105.621 1.00 26.33 ?  383 SER A O     1 
ATOM   3104  C  CB    . SER A 1 383 ? 141.085 132.490 107.836 1.00 16.56 ?  383 SER A CB    1 
ATOM   3105  O  OG    . SER A 1 383 ? 142.463 132.205 107.685 1.00 24.81 ?  383 SER A OG    1 
ATOM   3106  N  N     . GLU A 1 384 ? 140.756 135.632 105.871 1.00 14.02 ?  384 GLU A N     1 
ATOM   3107  C  CA    . GLU A 1 384 ? 141.222 136.223 104.622 1.00 5.78  ?  384 GLU A CA    1 
ATOM   3108  C  C     . GLU A 1 384 ? 141.531 137.711 104.710 1.00 14.42 ?  384 GLU A C     1 
ATOM   3109  O  O     . GLU A 1 384 ? 142.196 138.228 103.810 1.00 20.38 ?  384 GLU A O     1 
ATOM   3110  C  CB    . GLU A 1 384 ? 140.203 135.978 103.495 1.00 9.03  ?  384 GLU A CB    1 
ATOM   3111  C  CG    . GLU A 1 384 ? 139.371 137.176 103.066 1.00 10.86 ?  384 GLU A CG    1 
ATOM   3112  C  CD    . GLU A 1 384 ? 138.236 137.480 104.016 1.00 21.19 ?  384 GLU A CD    1 
ATOM   3113  O  OE1   . GLU A 1 384 ? 137.861 136.585 104.798 1.00 14.47 ?  384 GLU A OE1   1 
ATOM   3114  O  OE2   . GLU A 1 384 ? 137.705 138.606 103.965 1.00 27.61 -1 384 GLU A OE2   1 
ATOM   3115  N  N     . VAL A 1 385 ? 141.101 138.410 105.754 1.00 17.24 ?  385 VAL A N     1 
ATOM   3116  C  CA    . VAL A 1 385 ? 141.426 139.821 105.927 1.00 5.14  ?  385 VAL A CA    1 
ATOM   3117  C  C     . VAL A 1 385 ? 142.801 139.915 106.574 1.00 15.31 ?  385 VAL A C     1 
ATOM   3118  O  O     . VAL A 1 385 ? 143.015 139.398 107.674 1.00 23.18 ?  385 VAL A O     1 
ATOM   3119  C  CB    . VAL A 1 385 ? 140.368 140.538 106.776 1.00 7.09  ?  385 VAL A CB    1 
ATOM   3120  C  CG1   . VAL A 1 385 ? 140.809 141.951 107.058 1.00 8.27  ?  385 VAL A CG1   1 
ATOM   3121  C  CG2   . VAL A 1 385 ? 139.036 140.536 106.068 1.00 7.56  ?  385 VAL A CG2   1 
ATOM   3122  N  N     . LEU A 1 386 ? 143.733 140.577 105.889 1.00 16.57 ?  386 LEU A N     1 
ATOM   3123  C  CA    . LEU A 1 386 ? 145.125 140.683 106.327 1.00 2.61  ?  386 LEU A CA    1 
ATOM   3124  C  C     . LEU A 1 386 ? 145.556 142.138 106.189 1.00 5.27  ?  386 LEU A C     1 
ATOM   3125  O  O     . LEU A 1 386 ? 146.059 142.550 105.142 1.00 11.88 ?  386 LEU A O     1 
ATOM   3126  C  CB    . LEU A 1 386 ? 146.015 139.748 105.523 1.00 2.13  ?  386 LEU A CB    1 
ATOM   3127  C  CG    . LEU A 1 386 ? 145.759 138.263 105.775 1.00 6.65  ?  386 LEU A CG    1 
ATOM   3128  C  CD1   . LEU A 1 386 ? 146.612 137.425 104.865 1.00 10.46 ?  386 LEU A CD1   1 
ATOM   3129  C  CD2   . LEU A 1 386 ? 146.028 137.919 107.227 1.00 13.82 ?  386 LEU A CD2   1 
ATOM   3130  N  N     . GLN A 1 387 ? 145.365 142.909 107.255 1.00 14.61 ?  387 GLN A N     1 
ATOM   3131  C  CA    . GLN A 1 387 ? 145.638 144.336 107.255 1.00 10.55 ?  387 GLN A CA    1 
ATOM   3132  C  C     . GLN A 1 387 ? 146.425 144.714 108.501 1.00 12.82 ?  387 GLN A C     1 
ATOM   3133  O  O     . GLN A 1 387 ? 146.426 143.999 109.505 1.00 25.68 ?  387 GLN A O     1 
ATOM   3134  C  CB    . GLN A 1 387 ? 144.340 145.152 107.189 1.00 3.94  ?  387 GLN A CB    1 
ATOM   3135  C  CG    . GLN A 1 387 ? 143.440 144.784 106.030 1.00 7.66  ?  387 GLN A CG    1 
ATOM   3136  C  CD    . GLN A 1 387 ? 142.207 145.644 105.961 1.00 9.54  ?  387 GLN A CD    1 
ATOM   3137  O  OE1   . GLN A 1 387 ? 142.128 146.685 106.609 1.00 26.99 ?  387 GLN A OE1   1 
ATOM   3138  N  NE2   . GLN A 1 387 ? 141.229 145.217 105.175 1.00 13.40 ?  387 GLN A NE2   1 
ATOM   3139  N  N     . ALA A 1 388 ? 147.110 145.851 108.417 1.00 12.69 ?  388 ALA A N     1 
ATOM   3140  C  CA    . ALA A 1 388 ? 147.857 146.363 109.556 1.00 10.57 ?  388 ALA A CA    1 
ATOM   3141  C  C     . ALA A 1 388 ? 146.907 146.871 110.633 1.00 13.36 ?  388 ALA A C     1 
ATOM   3142  O  O     . ALA A 1 388 ? 145.895 147.512 110.341 1.00 25.27 ?  388 ALA A O     1 
ATOM   3143  C  CB    . ALA A 1 388 ? 148.794 147.484 109.114 1.00 11.56 ?  388 ALA A CB    1 
ATOM   3144  N  N     . SER A 1 389 ? 147.235 146.576 111.887 1.00 19.36 ?  389 SER A N     1 
ATOM   3145  C  CA    . SER A 1 389 ? 146.445 147.020 113.023 1.00 13.85 ?  389 SER A CA    1 
ATOM   3146  C  C     . SER A 1 389 ? 147.358 147.595 114.092 1.00 15.70 ?  389 SER A C     1 
ATOM   3147  O  O     . SER A 1 389 ? 148.499 147.157 114.262 1.00 23.18 ?  389 SER A O     1 
ATOM   3148  C  CB    . SER A 1 389 ? 145.612 145.879 113.621 1.00 14.60 ?  389 SER A CB    1 
ATOM   3149  O  OG    . SER A 1 389 ? 146.416 144.747 113.899 1.00 25.24 ?  389 SER A OG    1 
ATOM   3150  N  N     . GLN A 1 390 ? 146.842 148.582 114.816 1.00 17.82 ?  390 GLN A N     1 
ATOM   3151  C  CA    . GLN A 1 390 ? 147.524 149.167 115.961 1.00 14.43 ?  390 GLN A CA    1 
ATOM   3152  C  C     . GLN A 1 390 ? 146.629 149.016 117.179 1.00 14.63 ?  390 GLN A C     1 
ATOM   3153  O  O     . GLN A 1 390 ? 145.451 149.382 117.136 1.00 27.28 ?  390 GLN A O     1 
ATOM   3154  C  CB    . GLN A 1 390 ? 147.858 150.639 115.715 1.00 17.79 ?  390 GLN A CB    1 
ATOM   3155  C  CG    . GLN A 1 390 ? 148.887 150.857 114.624 1.00 17.56 ?  390 GLN A CG    1 
ATOM   3156  C  CD    . GLN A 1 390 ? 149.053 152.315 114.260 1.00 22.86 ?  390 GLN A CD    1 
ATOM   3157  O  OE1   . GLN A 1 390 ? 148.287 153.170 114.704 1.00 31.19 ?  390 GLN A OE1   1 
ATOM   3158  N  NE2   . GLN A 1 390 ? 150.061 152.611 113.450 1.00 21.59 ?  390 GLN A NE2   1 
ATOM   3159  N  N     . VAL A 1 391 ? 147.185 148.469 118.260 1.00 23.96 ?  391 VAL A N     1 
ATOM   3160  C  CA    . VAL A 1 391 ? 146.387 148.193 119.446 1.00 24.92 ?  391 VAL A CA    1 
ATOM   3161  C  C     . VAL A 1 391 ? 145.991 149.500 120.125 1.00 25.86 ?  391 VAL A C     1 
ATOM   3162  O  O     . VAL A 1 391 ? 146.725 150.497 120.100 1.00 26.45 ?  391 VAL A O     1 
ATOM   3163  C  CB    . VAL A 1 391 ? 147.147 147.261 120.409 1.00 15.46 ?  391 VAL A CB    1 
ATOM   3164  C  CG1   . VAL A 1 391 ? 148.216 148.021 121.176 1.00 21.40 ?  391 VAL A CG1   1 
ATOM   3165  C  CG2   . VAL A 1 391 ? 146.183 146.578 121.362 1.00 16.26 ?  391 VAL A CG2   1 
ATOM   3166  N  N     . SER A 1 392 ? 144.801 149.504 120.712 1.00 28.22 ?  392 SER A N     1 
ATOM   3167  C  CA    . SER A 1 392 ? 144.317 150.644 121.469 1.00 18.16 ?  392 SER A CA    1 
ATOM   3168  C  C     . SER A 1 392 ? 144.731 150.520 122.930 1.00 27.95 ?  392 SER A C     1 
ATOM   3169  O  O     . SER A 1 392 ? 145.050 149.437 123.424 1.00 36.07 ?  392 SER A O     1 
ATOM   3170  C  CB    . SER A 1 392 ? 142.797 150.761 121.363 1.00 24.73 ?  392 SER A CB    1 
ATOM   3171  O  OG    . SER A 1 392 ? 142.396 151.041 120.034 1.00 33.95 ?  392 SER A OG    1 
ATOM   3172  N  N     . SER A 1 393 ? 144.726 151.654 123.621 1.00 33.60 ?  393 SER A N     1 
ATOM   3173  C  CA    . SER A 1 393 ? 145.053 151.716 125.042 1.00 31.95 ?  393 SER A CA    1 
ATOM   3174  C  C     . SER A 1 393 ? 143.837 152.289 125.762 1.00 32.73 ?  393 SER A C     1 
ATOM   3175  O  O     . SER A 1 393 ? 143.750 153.497 125.993 1.00 34.99 ?  393 SER A O     1 
ATOM   3176  C  CB    . SER A 1 393 ? 146.304 152.552 125.286 1.00 31.84 ?  393 SER A CB    1 
ATOM   3177  O  OG    . SER A 1 393 ? 147.062 152.032 126.363 1.00 39.31 ?  393 SER A OG    1 
ATOM   3178  N  N     . TYR A 1 394 ? 142.899 151.415 126.112 1.00 34.05 ?  394 TYR A N     1 
ATOM   3179  C  CA    . TYR A 1 394 ? 141.710 151.828 126.845 1.00 31.62 ?  394 TYR A CA    1 
ATOM   3180  C  C     . TYR A 1 394 ? 142.065 151.973 128.318 1.00 35.26 ?  394 TYR A C     1 
ATOM   3181  O  O     . TYR A 1 394 ? 142.446 150.996 128.972 1.00 37.43 ?  394 TYR A O     1 
ATOM   3182  C  CB    . TYR A 1 394 ? 140.581 150.822 126.645 1.00 28.57 ?  394 TYR A CB    1 
ATOM   3183  C  CG    . TYR A 1 394 ? 140.117 150.715 125.210 1.00 30.05 ?  394 TYR A CG    1 
ATOM   3184  C  CD1   . TYR A 1 394 ? 139.391 151.740 124.619 1.00 31.16 ?  394 TYR A CD1   1 
ATOM   3185  C  CD2   . TYR A 1 394 ? 140.411 149.595 124.447 1.00 31.12 ?  394 TYR A CD2   1 
ATOM   3186  C  CE1   . TYR A 1 394 ? 138.968 151.649 123.310 1.00 33.30 ?  394 TYR A CE1   1 
ATOM   3187  C  CE2   . TYR A 1 394 ? 139.991 149.495 123.138 1.00 30.57 ?  394 TYR A CE2   1 
ATOM   3188  C  CZ    . TYR A 1 394 ? 139.271 150.524 122.574 1.00 37.78 ?  394 TYR A CZ    1 
ATOM   3189  O  OH    . TYR A 1 394 ? 138.853 150.427 121.267 1.00 39.81 ?  394 TYR A OH    1 
ATOM   3190  N  N     . THR A 1 395 ? 141.947 153.188 128.834 1.00 34.33 ?  395 THR A N     1 
ATOM   3191  C  CA    . THR A 1 395 ? 142.381 153.531 130.175 1.00 36.56 ?  395 THR A CA    1 
ATOM   3192  C  C     . THR A 1 395 ? 141.184 153.543 131.124 1.00 37.82 ?  395 THR A C     1 
ATOM   3193  O  O     . THR A 1 395 ? 140.082 153.104 130.779 1.00 34.94 ?  395 THR A O     1 
ATOM   3194  C  CB    . THR A 1 395 ? 143.106 154.876 130.150 1.00 35.93 ?  395 THR A CB    1 
ATOM   3195  O  OG1   . THR A 1 395 ? 142.231 155.880 129.621 1.00 37.71 ?  395 THR A OG1   1 
ATOM   3196  C  CG2   . THR A 1 395 ? 144.342 154.788 129.273 1.00 34.69 ?  395 THR A CG2   1 
ATOM   3197  N  N     . ASP A 1 396 ? 141.405 154.033 132.342 1.00 39.46 ?  396 ASP A N     1 
ATOM   3198  C  CA    . ASP A 1 396 ? 140.338 154.135 133.323 1.00 35.04 ?  396 ASP A CA    1 
ATOM   3199  C  C     . ASP A 1 396 ? 139.227 155.053 132.816 1.00 37.72 ?  396 ASP A C     1 
ATOM   3200  O  O     . ASP A 1 396 ? 139.364 155.751 131.810 1.00 43.75 ?  396 ASP A O     1 
ATOM   3201  C  CB    . ASP A 1 396 ? 140.883 154.646 134.656 1.00 37.84 ?  396 ASP A CB    1 
ATOM   3202  C  CG    . ASP A 1 396 ? 141.885 153.695 135.279 1.00 43.06 ?  396 ASP A CG    1 
ATOM   3203  O  OD1   . ASP A 1 396 ? 141.568 152.494 135.406 1.00 40.24 ?  396 ASP A OD1   1 
ATOM   3204  O  OD2   . ASP A 1 396 ? 142.988 154.149 135.647 1.00 44.39 -1 396 ASP A OD2   1 
ATOM   3205  N  N     . TYR A 1 397 ? 138.105 155.038 133.540 1.00 35.15 ?  397 TYR A N     1 
ATOM   3206  C  CA    . TYR A 1 397 ? 136.932 155.792 133.108 1.00 35.34 ?  397 TYR A CA    1 
ATOM   3207  C  C     . TYR A 1 397 ? 137.229 157.283 133.018 1.00 36.99 ?  397 TYR A C     1 
ATOM   3208  O  O     . TYR A 1 397 ? 136.809 157.951 132.065 1.00 41.13 ?  397 TYR A O     1 
ATOM   3209  C  CB    . TYR A 1 397 ? 135.765 155.535 134.062 1.00 30.96 ?  397 TYR A CB    1 
ATOM   3210  C  CG    . TYR A 1 397 ? 134.486 156.232 133.660 1.00 33.12 ?  397 TYR A CG    1 
ATOM   3211  C  CD1   . TYR A 1 397 ? 133.604 155.640 132.768 1.00 33.56 ?  397 TYR A CD1   1 
ATOM   3212  C  CD2   . TYR A 1 397 ? 134.165 157.483 134.170 1.00 34.28 ?  397 TYR A CD2   1 
ATOM   3213  C  CE1   . TYR A 1 397 ? 132.437 156.275 132.395 1.00 29.73 ?  397 TYR A CE1   1 
ATOM   3214  C  CE2   . TYR A 1 397 ? 133.002 158.123 133.802 1.00 33.91 ?  397 TYR A CE2   1 
ATOM   3215  C  CZ    . TYR A 1 397 ? 132.142 157.515 132.917 1.00 34.95 ?  397 TYR A CZ    1 
ATOM   3216  O  OH    . TYR A 1 397 ? 130.980 158.152 132.550 1.00 39.62 ?  397 TYR A OH    1 
ATOM   3217  N  N     . ASP A 1 398 ? 137.951 157.823 133.996 1.00 40.12 ?  398 ASP A N     1 
ATOM   3218  C  CA    . ASP A 1 398 ? 138.232 159.251 134.038 1.00 39.48 ?  398 ASP A CA    1 
ATOM   3219  C  C     . ASP A 1 398 ? 139.289 159.688 133.033 1.00 45.32 ?  398 ASP A C     1 
ATOM   3220  O  O     . ASP A 1 398 ? 139.383 160.885 132.743 1.00 46.74 ?  398 ASP A O     1 
ATOM   3221  C  CB    . ASP A 1 398 ? 138.673 159.652 135.448 1.00 43.35 ?  398 ASP A CB    1 
ATOM   3222  C  CG    . ASP A 1 398 ? 139.553 158.603 136.102 1.00 46.91 ?  398 ASP A CG    1 
ATOM   3223  O  OD1   . ASP A 1 398 ? 139.047 157.500 136.392 1.00 43.86 ?  398 ASP A OD1   1 
ATOM   3224  O  OD2   . ASP A 1 398 ? 140.750 158.881 136.326 1.00 45.84 -1 398 ASP A OD2   1 
ATOM   3225  N  N     . GLU A 1 399 ? 140.077 158.763 132.497 1.00 46.09 ?  399 GLU A N     1 
ATOM   3226  C  CA    . GLU A 1 399 ? 141.187 159.095 131.617 1.00 42.81 ?  399 GLU A CA    1 
ATOM   3227  C  C     . GLU A 1 399 ? 140.795 158.929 130.154 1.00 45.49 ?  399 GLU A C     1 
ATOM   3228  O  O     . GLU A 1 399 ? 139.869 158.190 129.808 1.00 45.00 ?  399 GLU A O     1 
ATOM   3229  C  CB    . GLU A 1 399 ? 142.404 158.223 131.929 1.00 42.35 ?  399 GLU A CB    1 
ATOM   3230  C  CG    . GLU A 1 399 ? 142.486 157.762 133.370 1.00 44.59 ?  399 GLU A CG    1 
ATOM   3231  C  CD    . GLU A 1 399 ? 143.843 157.190 133.720 1.00 50.14 ?  399 GLU A CD    1 
ATOM   3232  O  OE1   . GLU A 1 399 ? 144.125 156.039 133.322 1.00 46.87 ?  399 GLU A OE1   1 
ATOM   3233  O  OE2   . GLU A 1 399 ? 144.629 157.889 134.393 1.00 49.31 -1 399 GLU A OE2   1 
ATOM   3234  N  N     . GLU A 1 400 ? 141.520 159.637 129.292 1.00 43.20 ?  400 GLU A N     1 
ATOM   3235  C  CA    . GLU A 1 400 ? 141.308 159.527 127.857 1.00 40.44 ?  400 GLU A CA    1 
ATOM   3236  C  C     . GLU A 1 400 ? 141.934 158.245 127.322 1.00 41.95 ?  400 GLU A C     1 
ATOM   3237  O  O     . GLU A 1 400 ? 142.988 157.807 127.785 1.00 41.73 ?  400 GLU A O     1 
ATOM   3238  C  CB    . GLU A 1 400 ? 141.901 160.739 127.138 1.00 40.61 ?  400 GLU A CB    1 
ATOM   3239  C  CG    . GLU A 1 400 ? 141.063 161.999 127.248 1.00 44.10 ?  400 GLU A CG    1 
ATOM   3240  C  CD    . GLU A 1 400 ? 140.078 162.146 126.105 1.00 49.46 ?  400 GLU A CD    1 
ATOM   3241  O  OE1   . GLU A 1 400 ? 138.993 162.723 126.323 1.00 45.54 ?  400 GLU A OE1   1 
ATOM   3242  O  OE2   . GLU A 1 400 ? 140.388 161.683 124.988 1.00 49.57 -1 400 GLU A OE2   1 
ATOM   3243  N  N     . ASP A 1 401 ? 141.273 157.643 126.337 1.00 39.60 ?  401 ASP A N     1 
ATOM   3244  C  CA    . ASP A 1 401 ? 141.750 156.412 125.728 1.00 36.96 ?  401 ASP A CA    1 
ATOM   3245  C  C     . ASP A 1 401 ? 142.591 156.718 124.498 1.00 37.21 ?  401 ASP A C     1 
ATOM   3246  O  O     . ASP A 1 401 ? 142.294 157.647 123.742 1.00 39.03 ?  401 ASP A O     1 
ATOM   3247  C  CB    . ASP A 1 401 ? 140.579 155.510 125.340 1.00 35.70 ?  401 ASP A CB    1 
ATOM   3248  C  CG    . ASP A 1 401 ? 139.685 155.175 126.514 1.00 39.29 ?  401 ASP A CG    1 
ATOM   3249  O  OD1   . ASP A 1 401 ? 140.188 155.140 127.656 1.00 41.78 ?  401 ASP A OD1   1 
ATOM   3250  O  OD2   . ASP A 1 401 ? 138.479 154.943 126.295 1.00 40.69 -1 401 ASP A OD2   1 
ATOM   3251  N  N     . GLU A 1 402 ? 143.647 155.932 124.306 1.00 33.55 ?  402 GLU A N     1 
ATOM   3252  C  CA    . GLU A 1 402 ? 144.461 155.999 123.097 1.00 32.92 ?  402 GLU A CA    1 
ATOM   3253  C  C     . GLU A 1 402 ? 143.876 155.024 122.084 1.00 31.86 ?  402 GLU A C     1 
ATOM   3254  O  O     . GLU A 1 402 ? 144.037 153.807 122.218 1.00 39.81 ?  402 GLU A O     1 
ATOM   3255  C  CB    . GLU A 1 402 ? 145.919 155.670 123.402 1.00 36.93 ?  402 GLU A CB    1 
ATOM   3256  C  CG    . GLU A 1 402 ? 146.603 156.664 124.322 1.00 36.37 ?  402 GLU A CG    1 
ATOM   3257  C  CD    . GLU A 1 402 ? 147.442 155.989 125.389 1.00 43.09 ?  402 GLU A CD    1 
ATOM   3258  O  OE1   . GLU A 1 402 ? 148.622 155.683 125.116 1.00 43.53 ?  402 GLU A OE1   1 
ATOM   3259  O  OE2   . GLU A 1 402 ? 146.921 155.766 126.502 1.00 43.84 -1 402 GLU A OE2   1 
ATOM   3260  N  N     . ILE A 1 403 ? 143.197 155.554 121.076 1.00 29.35 ?  403 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 403 ? 142.493 154.737 120.095 1.00 30.38 ?  403 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 403 ? 143.469 154.306 119.009 1.00 29.83 ?  403 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 403 ? 144.152 155.142 118.407 1.00 31.37 ?  403 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 403 ? 141.303 155.506 119.497 1.00 27.23 ?  403 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 403 ? 140.274 155.823 120.586 1.00 30.31 ?  403 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 403 ? 140.670 154.716 118.368 1.00 22.57 ?  403 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 403 ? 139.913 154.638 121.453 1.00 30.63 ?  403 ILE A CD1   1 
ATOM   3268  N  N     . GLY A 1 404 ? 143.533 153.000 118.760 1.00 24.83 ?  404 GLY A N     1 
ATOM   3269  C  CA    . GLY A 1 404 ? 144.386 152.464 117.719 1.00 15.92 ?  404 GLY A CA    1 
ATOM   3270  C  C     . GLY A 1 404 ? 143.660 152.255 116.408 1.00 22.98 ?  404 GLY A C     1 
ATOM   3271  O  O     . GLY A 1 404 ? 142.767 153.030 116.055 1.00 33.56 ?  404 GLY A O     1 
ATOM   3272  N  N     . LEU A 1 405 ? 144.033 151.209 115.671 1.00 21.63 ?  405 LEU A N     1 
ATOM   3273  C  CA    . LEU A 1 405 ? 143.428 150.894 114.381 1.00 8.88  ?  405 LEU A CA    1 
ATOM   3274  C  C     . LEU A 1 405 ? 142.947 149.450 114.409 1.00 15.28 ?  405 LEU A C     1 
ATOM   3275  O  O     . LEU A 1 405 ? 143.760 148.523 114.446 1.00 16.33 ?  405 LEU A O     1 
ATOM   3276  C  CB    . LEU A 1 405 ? 144.420 151.109 113.237 1.00 18.00 ?  405 LEU A CB    1 
ATOM   3277  C  CG    . LEU A 1 405 ? 144.954 152.523 113.012 1.00 17.66 ?  405 LEU A CG    1 
ATOM   3278  C  CD1   . LEU A 1 405 ? 146.073 152.503 111.987 1.00 18.80 ?  405 LEU A CD1   1 
ATOM   3279  C  CD2   . LEU A 1 405 ? 143.846 153.462 112.579 1.00 16.03 ?  405 LEU A CD2   1 
ATOM   3280  N  N     . ASP A 1 406 ? 141.632 149.261 114.386 1.00 23.95 ?  406 ASP A N     1 
ATOM   3281  C  CA    . ASP A 1 406 ? 141.030 147.937 114.324 1.00 12.97 ?  406 ASP A CA    1 
ATOM   3282  C  C     . ASP A 1 406 ? 140.486 147.690 112.924 1.00 17.53 ?  406 ASP A C     1 
ATOM   3283  O  O     . ASP A 1 406 ? 139.796 148.539 112.353 1.00 31.72 ?  406 ASP A O     1 
ATOM   3284  C  CB    . ASP A 1 406 ? 139.916 147.789 115.359 1.00 16.10 ?  406 ASP A CB    1 
ATOM   3285  C  CG    . ASP A 1 406 ? 140.442 147.420 116.734 1.00 30.19 ?  406 ASP A CG    1 
ATOM   3286  O  OD1   . ASP A 1 406 ? 141.649 147.126 116.857 1.00 30.73 ?  406 ASP A OD1   1 
ATOM   3287  O  OD2   . ASP A 1 406 ? 139.649 147.431 117.697 1.00 30.34 -1 406 ASP A OD2   1 
ATOM   3288  N  N     . ILE A 1 407 ? 140.778 146.518 112.387 1.00 23.30 ?  407 ILE A N     1 
ATOM   3289  C  CA    . ILE A 1 407 ? 140.561 146.249 110.972 1.00 17.70 ?  407 ILE A CA    1 
ATOM   3290  C  C     . ILE A 1 407 ? 139.086 145.980 110.701 1.00 18.01 ?  407 ILE A C     1 
ATOM   3291  O  O     . ILE A 1 407 ? 138.391 145.339 111.498 1.00 21.33 ?  407 ILE A O     1 
ATOM   3292  C  CB    . ILE A 1 407 ? 141.432 145.065 110.519 1.00 13.02 ?  407 ILE A CB    1 
ATOM   3293  C  CG1   . ILE A 1 407 ? 142.908 145.351 110.785 1.00 2.81  ?  407 ILE A CG1   1 
ATOM   3294  C  CG2   . ILE A 1 407 ? 141.212 144.772 109.062 1.00 16.48 ?  407 ILE A CG2   1 
ATOM   3295  C  CD1   . ILE A 1 407 ? 143.670 144.142 111.240 1.00 18.29 ?  407 ILE A CD1   1 
ATOM   3296  N  N     . SER A 1 408 ? 138.611 146.481 109.563 1.00 27.38 ?  408 SER A N     1 
ATOM   3297  C  CA    . SER A 1 408 ? 137.314 146.126 109.007 1.00 20.37 ?  408 SER A CA    1 
ATOM   3298  C  C     . SER A 1 408 ? 137.312 146.536 107.542 1.00 24.30 ?  408 SER A C     1 
ATOM   3299  O  O     . SER A 1 408 ? 137.759 147.635 107.204 1.00 36.21 ?  408 SER A O     1 
ATOM   3300  C  CB    . SER A 1 408 ? 136.165 146.807 109.759 1.00 21.57 ?  408 SER A CB    1 
ATOM   3301  O  OG    . SER A 1 408 ? 135.836 148.055 109.176 1.00 28.81 ?  408 SER A OG    1 
ATOM   3302  N  N     . CYS A 1 409 ? 136.825 145.651 106.678 1.00 20.11 ?  409 CYS A N     1 
ATOM   3303  C  CA    . CYS A 1 409 ? 136.736 145.947 105.257 1.00 26.27 ?  409 CYS A CA    1 
ATOM   3304  C  C     . CYS A 1 409 ? 135.393 145.480 104.715 1.00 26.33 ?  409 CYS A C     1 
ATOM   3305  O  O     . CYS A 1 409 ? 134.785 144.534 105.219 1.00 24.50 ?  409 CYS A O     1 
ATOM   3306  C  CB    . CYS A 1 409 ? 137.887 145.306 104.464 1.00 22.59 ?  409 CYS A CB    1 
ATOM   3307  S  SG    . CYS A 1 409 ? 137.781 143.519 104.247 1.00 39.49 ?  409 CYS A SG    1 
ATOM   3308  N  N     . ASN A 1 410 ? 134.935 146.171 103.676 1.00 22.83 ?  410 ASN A N     1 
ATOM   3309  C  CA    . ASN A 1 410 ? 133.693 145.830 103.004 1.00 18.43 ?  410 ASN A CA    1 
ATOM   3310  C  C     . ASN A 1 410 ? 133.981 144.807 101.919 1.00 20.75 ?  410 ASN A C     1 
ATOM   3311  O  O     . ASN A 1 410 ? 134.933 144.961 101.147 1.00 22.15 ?  410 ASN A O     1 
ATOM   3312  C  CB    . ASN A 1 410 ? 133.042 147.068 102.393 1.00 22.82 ?  410 ASN A CB    1 
ATOM   3313  C  CG    . ASN A 1 410 ? 133.729 148.342 102.806 1.00 30.14 ?  410 ASN A CG    1 
ATOM   3314  O  OD1   . ASN A 1 410 ? 134.214 148.469 103.929 1.00 31.24 ?  410 ASN A OD1   1 
ATOM   3315  N  ND2   . ASN A 1 410 ? 133.788 149.297 101.891 1.00 28.88 ?  410 ASN A ND2   1 
ATOM   3316  N  N     . LEU A 1 411 ? 133.156 143.773 101.857 1.00 17.79 ?  411 LEU A N     1 
ATOM   3317  C  CA    . LEU A 1 411 ? 133.374 142.658 100.954 1.00 12.06 ?  411 LEU A CA    1 
ATOM   3318  C  C     . LEU A 1 411 ? 132.537 142.820 99.693  1.00 13.10 ?  411 LEU A C     1 
ATOM   3319  O  O     . LEU A 1 411 ? 131.449 143.399 99.712  1.00 19.18 ?  411 LEU A O     1 
ATOM   3320  C  CB    . LEU A 1 411 ? 133.031 141.338 101.644 1.00 21.93 ?  411 LEU A CB    1 
ATOM   3321  C  CG    . LEU A 1 411 ? 133.757 141.029 102.951 1.00 14.94 ?  411 LEU A CG    1 
ATOM   3322  C  CD1   . LEU A 1 411 ? 133.688 139.551 103.237 1.00 20.54 ?  411 LEU A CD1   1 
ATOM   3323  C  CD2   . LEU A 1 411 ? 135.202 141.477 102.882 1.00 19.17 ?  411 LEU A CD2   1 
ATOM   3324  N  N     . GLY A 1 412 ? 133.067 142.302 98.591  1.00 21.24 ?  412 GLY A N     1 
ATOM   3325  C  CA    . GLY A 1 412 ? 132.364 142.276 97.327  1.00 10.26 ?  412 GLY A CA    1 
ATOM   3326  C  C     . GLY A 1 412 ? 133.062 141.339 96.370  1.00 11.55 ?  412 GLY A C     1 
ATOM   3327  O  O     . GLY A 1 412 ? 134.294 141.318 96.318  1.00 25.53 ?  412 GLY A O     1 
ATOM   3328  N  N     . SER A 1 413 ? 132.305 140.556 95.611  1.00 15.23 ?  413 SER A N     1 
ATOM   3329  C  CA    . SER A 1 413 ? 132.872 139.517 94.764  1.00 9.33  ?  413 SER A CA    1 
ATOM   3330  C  C     . SER A 1 413 ? 132.559 139.791 93.303  1.00 15.97 ?  413 SER A C     1 
ATOM   3331  O  O     . SER A 1 413 ? 131.413 140.090 92.954  1.00 24.07 ?  413 SER A O     1 
ATOM   3332  C  CB    . SER A 1 413 ? 132.343 138.140 95.159  1.00 10.90 ?  413 SER A CB    1 
ATOM   3333  O  OG    . SER A 1 413 ? 132.874 137.739 96.406  1.00 29.53 ?  413 SER A OG    1 
ATOM   3334  N  N     . LEU A 1 414 ? 133.579 139.689 92.459  1.00 20.43 ?  414 LEU A N     1 
ATOM   3335  C  CA    . LEU A 1 414 ? 133.367 139.603 91.024  1.00 13.30 ?  414 LEU A CA    1 
ATOM   3336  C  C     . LEU A 1 414 ? 132.959 138.185 90.657  1.00 21.18 ?  414 LEU A C     1 
ATOM   3337  O  O     . LEU A 1 414 ? 133.485 137.213 91.205  1.00 21.96 ?  414 LEU A O     1 
ATOM   3338  C  CB    . LEU A 1 414 ? 134.634 139.986 90.262  1.00 14.83 ?  414 LEU A CB    1 
ATOM   3339  C  CG    . LEU A 1 414 ? 135.395 141.237 90.691  1.00 19.22 ?  414 LEU A CG    1 
ATOM   3340  C  CD1   . LEU A 1 414 ? 136.708 141.312 89.938  1.00 24.86 ?  414 LEU A CD1   1 
ATOM   3341  C  CD2   . LEU A 1 414 ? 134.561 142.477 90.440  1.00 24.81 ?  414 LEU A CD2   1 
ATOM   3342  N  N     . ASN A 1 415 ? 132.019 138.065 89.730  1.00 28.22 ?  415 ASN A N     1 
ATOM   3343  C  CA    . ASN A 1 415 ? 131.672 136.772 89.156  1.00 25.19 ?  415 ASN A CA    1 
ATOM   3344  C  C     . ASN A 1 415 ? 132.573 136.552 87.949  1.00 27.36 ?  415 ASN A C     1 
ATOM   3345  O  O     . ASN A 1 415 ? 132.388 137.186 86.907  1.00 29.83 ?  415 ASN A O     1 
ATOM   3346  C  CB    . ASN A 1 415 ? 130.197 136.723 88.774  1.00 20.33 ?  415 ASN A CB    1 
ATOM   3347  C  CG    . ASN A 1 415 ? 129.680 135.311 88.613  1.00 23.73 ?  415 ASN A CG    1 
ATOM   3348  O  OD1   . ASN A 1 415 ? 130.278 134.495 87.915  1.00 32.26 ?  415 ASN A OD1   1 
ATOM   3349  N  ND2   . ASN A 1 415 ? 128.562 135.015 89.259  1.00 30.02 ?  415 ASN A ND2   1 
ATOM   3350  N  N     . ILE A 1 416 ? 133.550 135.656 88.096  1.00 19.85 ?  416 ILE A N     1 
ATOM   3351  C  CA    . ILE A 1 416 ? 134.565 135.476 87.062  1.00 22.02 ?  416 ILE A CA    1 
ATOM   3352  C  C     . ILE A 1 416 ? 133.926 135.035 85.752  1.00 28.81 ?  416 ILE A C     1 
ATOM   3353  O  O     . ILE A 1 416 ? 134.312 135.495 84.671  1.00 26.69 ?  416 ILE A O     1 
ATOM   3354  C  CB    . ILE A 1 416 ? 135.640 134.481 87.538  1.00 24.02 ?  416 ILE A CB    1 
ATOM   3355  C  CG1   . ILE A 1 416 ? 136.419 135.072 88.714  1.00 21.73 ?  416 ILE A CG1   1 
ATOM   3356  C  CG2   . ILE A 1 416 ? 136.586 134.130 86.409  1.00 15.94 ?  416 ILE A CG2   1 
ATOM   3357  C  CD1   . ILE A 1 416 ? 137.334 134.091 89.402  1.00 19.62 ?  416 ILE A CD1   1 
ATOM   3358  N  N     . LEU A 1 417 ? 132.929 134.151 85.825  1.00 23.98 ?  417 LEU A N     1 
ATOM   3359  C  CA    . LEU A 1 417 ? 132.276 133.670 84.611  1.00 27.03 ?  417 LEU A CA    1 
ATOM   3360  C  C     . LEU A 1 417 ? 131.577 134.803 83.870  1.00 28.59 ?  417 LEU A C     1 
ATOM   3361  O  O     . LEU A 1 417 ? 131.759 134.974 82.659  1.00 36.05 ?  417 LEU A O     1 
ATOM   3362  C  CB    . LEU A 1 417 ? 131.283 132.563 84.959  1.00 27.64 ?  417 LEU A CB    1 
ATOM   3363  C  CG    . LEU A 1 417 ? 130.739 131.740 83.792  1.00 25.66 ?  417 LEU A CG    1 
ATOM   3364  C  CD1   . LEU A 1 417 ? 130.716 130.277 84.164  1.00 26.86 ?  417 LEU A CD1   1 
ATOM   3365  C  CD2   . LEU A 1 417 ? 129.350 132.211 83.406  1.00 32.99 ?  417 LEU A CD2   1 
ATOM   3366  N  N     . ASN A 1 418 ? 130.773 135.593 84.583  1.00 30.17 ?  418 ASN A N     1 
ATOM   3367  C  CA    . ASN A 1 418 ? 130.013 136.655 83.935  1.00 30.26 ?  418 ASN A CA    1 
ATOM   3368  C  C     . ASN A 1 418 ? 130.891 137.838 83.557  1.00 29.72 ?  418 ASN A C     1 
ATOM   3369  O  O     . ASN A 1 418 ? 130.627 138.503 82.549  1.00 32.38 ?  418 ASN A O     1 
ATOM   3370  C  CB    . ASN A 1 418 ? 128.873 137.111 84.845  1.00 26.41 ?  418 ASN A CB    1 
ATOM   3371  C  CG    . ASN A 1 418 ? 127.810 136.050 85.018  1.00 31.04 ?  418 ASN A CG    1 
ATOM   3372  O  OD1   . ASN A 1 418 ? 127.493 135.317 84.082  1.00 36.97 ?  418 ASN A OD1   1 
ATOM   3373  N  ND2   . ASN A 1 418 ? 127.253 135.956 86.218  1.00 32.23 ?  418 ASN A ND2   1 
ATOM   3374  N  N     . VAL A 1 419 ? 131.926 138.119 84.349  1.00 29.60 ?  419 VAL A N     1 
ATOM   3375  C  CA    . VAL A 1 419 ? 132.870 139.173 83.992  1.00 28.99 ?  419 VAL A CA    1 
ATOM   3376  C  C     . VAL A 1 419 ? 133.636 138.796 82.731  1.00 31.93 ?  419 VAL A C     1 
ATOM   3377  O  O     . VAL A 1 419 ? 133.833 139.625 81.835  1.00 35.55 ?  419 VAL A O     1 
ATOM   3378  C  CB    . VAL A 1 419 ? 133.814 139.458 85.175  1.00 27.28 ?  419 VAL A CB    1 
ATOM   3379  C  CG1   . VAL A 1 419 ? 135.057 140.170 84.707  1.00 31.92 ?  419 VAL A CG1   1 
ATOM   3380  C  CG2   . VAL A 1 419 ? 133.103 140.279 86.229  1.00 27.21 ?  419 VAL A CG2   1 
ATOM   3381  N  N     . MET A 1 420 ? 134.071 137.537 82.635  1.00 37.60 ?  420 MET A N     1 
ATOM   3382  C  CA    . MET A 1 420 ? 134.809 137.087 81.461  1.00 31.13 ?  420 MET A CA    1 
ATOM   3383  C  C     . MET A 1 420 ? 133.911 136.981 80.236  1.00 29.91 ?  420 MET A C     1 
ATOM   3384  O  O     . MET A 1 420 ? 134.364 137.239 79.115  1.00 35.71 ?  420 MET A O     1 
ATOM   3385  C  CB    . MET A 1 420 ? 135.475 135.744 81.749  1.00 32.87 ?  420 MET A CB    1 
ATOM   3386  C  CG    . MET A 1 420 ? 136.753 135.854 82.559  1.00 30.68 ?  420 MET A CG    1 
ATOM   3387  S  SD    . MET A 1 420 ? 137.971 136.915 81.769  1.00 39.19 ?  420 MET A SD    1 
ATOM   3388  C  CE    . MET A 1 420 ? 138.688 135.777 80.589  1.00 30.33 ?  420 MET A CE    1 
ATOM   3389  N  N     . GLU A 1 421 ? 132.646 136.598 80.424  1.00 38.79 ?  421 GLU A N     1 
ATOM   3390  C  CA    . GLU A 1 421 ? 131.712 136.547 79.305  1.00 37.01 ?  421 GLU A CA    1 
ATOM   3391  C  C     . GLU A 1 421 ? 131.471 137.934 78.725  1.00 41.48 ?  421 GLU A C     1 
ATOM   3392  O  O     . GLU A 1 421 ? 131.406 138.102 77.501  1.00 43.64 ?  421 GLU A O     1 
ATOM   3393  C  CB    . GLU A 1 421 ? 130.393 135.921 79.755  1.00 35.64 ?  421 GLU A CB    1 
ATOM   3394  C  CG    . GLU A 1 421 ? 130.347 134.407 79.645  1.00 40.90 ?  421 GLU A CG    1 
ATOM   3395  C  CD    . GLU A 1 421 ? 129.017 133.835 80.094  1.00 46.28 ?  421 GLU A CD    1 
ATOM   3396  O  OE1   . GLU A 1 421 ? 128.238 134.575 80.731  1.00 45.01 ?  421 GLU A OE1   1 
ATOM   3397  O  OE2   . GLU A 1 421 ? 128.750 132.648 79.811  1.00 45.47 -1 421 GLU A OE2   1 
ATOM   3398  N  N     . HIS A 1 422 ? 131.338 138.940 79.587  1.00 37.78 ?  422 HIS A N     1 
ATOM   3399  C  CA    . HIS A 1 422 ? 131.086 140.306 79.152  1.00 34.71 ?  422 HIS A CA    1 
ATOM   3400  C  C     . HIS A 1 422 ? 132.354 141.047 78.755  1.00 39.06 ?  422 HIS A C     1 
ATOM   3401  O  O     . HIS A 1 422 ? 132.255 142.181 78.273  1.00 39.00 ?  422 HIS A O     1 
ATOM   3402  C  CB    . HIS A 1 422 ? 130.366 141.081 80.258  1.00 34.38 ?  422 HIS A CB    1 
ATOM   3403  C  CG    . HIS A 1 422 ? 128.993 140.570 80.558  1.00 36.59 ?  422 HIS A CG    1 
ATOM   3404  N  ND1   . HIS A 1 422 ? 128.755 139.586 81.492  1.00 36.17 ?  422 HIS A ND1   1 
ATOM   3405  C  CD2   . HIS A 1 422 ? 127.783 140.907 80.052  1.00 38.64 ?  422 HIS A CD2   1 
ATOM   3406  C  CE1   . HIS A 1 422 ? 127.459 139.336 81.547  1.00 39.68 ?  422 HIS A CE1   1 
ATOM   3407  N  NE2   . HIS A 1 422 ? 126.847 140.124 80.682  1.00 41.23 ?  422 HIS A NE2   1 
ATOM   3408  N  N     . LYS A 1 423 ? 133.526 140.438 78.938  1.00 42.93 ?  423 LYS A N     1 
ATOM   3409  C  CA    . LYS A 1 423 ? 134.810 141.076 78.649  1.00 43.56 ?  423 LYS A CA    1 
ATOM   3410  C  C     . LYS A 1 423 ? 134.909 142.430 79.346  1.00 43.41 ?  423 LYS A C     1 
ATOM   3411  O  O     . LYS A 1 423 ? 135.283 143.443 78.751  1.00 46.66 ?  423 LYS A O     1 
ATOM   3412  C  CB    . LYS A 1 423 ? 135.029 141.217 77.143  1.00 40.83 ?  423 LYS A CB    1 
ATOM   3413  C  CG    . LYS A 1 423 ? 134.788 139.942 76.358  1.00 42.34 ?  423 LYS A CG    1 
ATOM   3414  C  CD    . LYS A 1 423 ? 136.068 139.141 76.212  1.00 46.49 ?  423 LYS A CD    1 
ATOM   3415  C  CE    . LYS A 1 423 ? 135.780 137.687 75.879  1.00 46.50 ?  423 LYS A CE    1 
ATOM   3416  N  NZ    . LYS A 1 423 ? 135.609 136.856 77.102  1.00 44.64 1  423 LYS A NZ    1 
ATOM   3417  N  N     . SER A 1 424 ? 134.566 142.439 80.629  1.00 33.13 ?  424 SER A N     1 
ATOM   3418  C  CA    . SER A 1 424 ? 134.403 143.670 81.394  1.00 32.99 ?  424 SER A CA    1 
ATOM   3419  C  C     . SER A 1 424 ? 135.135 143.584 82.722  1.00 36.41 ?  424 SER A C     1 
ATOM   3420  O  O     . SER A 1 424 ? 134.583 143.891 83.779  1.00 39.49 ?  424 SER A O     1 
ATOM   3421  C  CB    . SER A 1 424 ? 132.926 143.967 81.625  1.00 35.65 ?  424 SER A CB    1 
ATOM   3422  O  OG    . SER A 1 424 ? 132.376 143.073 82.575  1.00 32.10 ?  424 SER A OG    1 
ATOM   3423  N  N     . ILE A 1 425 ? 136.399 143.158 82.694  1.00 34.09 ?  425 ILE A N     1 
ATOM   3424  C  CA    . ILE A 1 425 ? 137.188 143.137 83.923  1.00 28.18 ?  425 ILE A CA    1 
ATOM   3425  C  C     . ILE A 1 425 ? 137.395 144.555 84.439  1.00 31.11 ?  425 ILE A C     1 
ATOM   3426  O  O     . ILE A 1 425 ? 137.181 144.842 85.622  1.00 36.98 ?  425 ILE A O     1 
ATOM   3427  C  CB    . ILE A 1 425 ? 138.528 142.415 83.697  1.00 32.28 ?  425 ILE A CB    1 
ATOM   3428  C  CG1   . ILE A 1 425 ? 138.321 140.901 83.682  1.00 33.29 ?  425 ILE A CG1   1 
ATOM   3429  C  CG2   . ILE A 1 425 ? 139.531 142.795 84.775  1.00 28.28 ?  425 ILE A CG2   1 
ATOM   3430  C  CD1   . ILE A 1 425 ? 139.566 140.111 83.392  1.00 32.74 ?  425 ILE A CD1   1 
ATOM   3431  N  N     . GLU A 1 426 ? 137.787 145.470 83.551  1.00 28.74 ?  426 GLU A N     1 
ATOM   3432  C  CA    . GLU A 1 426 ? 138.103 146.832 83.969  1.00 27.28 ?  426 GLU A CA    1 
ATOM   3433  C  C     . GLU A 1 426 ? 136.884 147.537 84.549  1.00 30.36 ?  426 GLU A C     1 
ATOM   3434  O  O     . GLU A 1 426 ? 136.933 148.076 85.662  1.00 37.14 ?  426 GLU A O     1 
ATOM   3435  C  CB    . GLU A 1 426 ? 138.660 147.618 82.784  1.00 29.43 ?  426 GLU A CB    1 
ATOM   3436  C  CG    . GLU A 1 426 ? 138.654 149.121 82.980  1.00 33.41 ?  426 GLU A CG    1 
ATOM   3437  C  CD    . GLU A 1 426 ? 139.359 149.855 81.859  1.00 39.47 ?  426 GLU A CD    1 
ATOM   3438  O  OE1   . GLU A 1 426 ? 139.635 149.225 80.817  1.00 38.35 ?  426 GLU A OE1   1 
ATOM   3439  O  OE2   . GLU A 1 426 ? 139.636 151.061 82.021  1.00 38.54 -1 426 GLU A OE2   1 
ATOM   3440  N  N     . LYS A 1 427 ? 135.776 147.544 83.805  1.00 32.91 ?  427 LYS A N     1 
ATOM   3441  C  CA    . LYS A 1 427 ? 134.589 148.265 84.248  1.00 28.97 ?  427 LYS A CA    1 
ATOM   3442  C  C     . LYS A 1 427 ? 134.014 147.655 85.517  1.00 30.16 ?  427 LYS A C     1 
ATOM   3443  O  O     . LYS A 1 427 ? 133.625 148.381 86.438  1.00 36.77 ?  427 LYS A O     1 
ATOM   3444  C  CB    . LYS A 1 427 ? 133.513 148.320 83.150  1.00 34.40 ?  427 LYS A CB    1 
ATOM   3445  C  CG    . LYS A 1 427 ? 133.851 148.964 81.770  1.00 38.16 ?  427 LYS A CG    1 
ATOM   3446  C  CD    . LYS A 1 427 ? 135.157 148.577 81.063  1.00 38.84 ?  427 LYS A CD    1 
ATOM   3447  C  CE    . LYS A 1 427 ? 135.285 147.074 80.854  1.00 34.59 ?  427 LYS A CE    1 
ATOM   3448  N  NZ    . LYS A 1 427 ? 136.584 146.699 80.230  1.00 35.02 1  427 LYS A NZ    1 
ATOM   3449  N  N     . THR A 1 428 ? 133.951 146.323 85.586  1.00 29.14 ?  428 THR A N     1 
ATOM   3450  C  CA    . THR A 1 428 ? 133.433 145.678 86.786  1.00 22.10 ?  428 THR A CA    1 
ATOM   3451  C  C     . THR A 1 428 ? 134.309 145.974 87.993  1.00 28.69 ?  428 THR A C     1 
ATOM   3452  O  O     . THR A 1 428 ? 133.796 146.282 89.074  1.00 31.20 ?  428 THR A O     1 
ATOM   3453  C  CB    . THR A 1 428 ? 133.313 144.170 86.580  1.00 24.52 ?  428 THR A CB    1 
ATOM   3454  O  OG1   . THR A 1 428 ? 132.700 143.905 85.314  1.00 28.64 ?  428 THR A OG1   1 
ATOM   3455  C  CG2   . THR A 1 428 ? 132.470 143.560 87.680  1.00 25.65 ?  428 THR A CG2   1 
ATOM   3456  N  N     . VAL A 1 429 ? 135.631 145.894 87.831  1.00 28.73 ?  429 VAL A N     1 
ATOM   3457  C  CA    . VAL A 1 429 ? 136.527 146.141 88.956  1.00 22.63 ?  429 VAL A CA    1 
ATOM   3458  C  C     . VAL A 1 429 ? 136.400 147.581 89.432  1.00 23.97 ?  429 VAL A C     1 
ATOM   3459  O  O     . VAL A 1 429 ? 136.331 147.844 90.636  1.00 30.65 ?  429 VAL A O     1 
ATOM   3460  C  CB    . VAL A 1 429 ? 137.980 145.793 88.578  1.00 24.00 ?  429 VAL A CB    1 
ATOM   3461  C  CG1   . VAL A 1 429 ? 138.942 146.402 89.574  1.00 19.09 ?  429 VAL A CG1   1 
ATOM   3462  C  CG2   . VAL A 1 429 ? 138.169 144.290 88.537  1.00 23.11 ?  429 VAL A CG2   1 
ATOM   3463  N  N     . LYS A 1 430 ? 136.341 148.534 88.499  1.00 24.20 ?  430 LYS A N     1 
ATOM   3464  C  CA    . LYS A 1 430 ? 136.256 149.936 88.897  1.00 23.38 ?  430 LYS A CA    1 
ATOM   3465  C  C     . LYS A 1 430 ? 134.918 150.254 89.558  1.00 23.32 ?  430 LYS A C     1 
ATOM   3466  O  O     . LYS A 1 430 ? 134.875 150.959 90.574  1.00 31.57 ?  430 LYS A O     1 
ATOM   3467  C  CB    . LYS A 1 430 ? 136.502 150.836 87.688  1.00 24.45 ?  430 LYS A CB    1 
ATOM   3468  C  CG    . LYS A 1 430 ? 137.912 150.715 87.135  1.00 26.85 ?  430 LYS A CG    1 
ATOM   3469  C  CD    . LYS A 1 430 ? 138.287 151.901 86.273  1.00 29.76 ?  430 LYS A CD    1 
ATOM   3470  C  CE    . LYS A 1 430 ? 139.732 151.799 85.819  1.00 29.64 ?  430 LYS A CE    1 
ATOM   3471  N  NZ    . LYS A 1 430 ? 140.126 152.943 84.955  1.00 33.48 1  430 LYS A NZ    1 
ATOM   3472  N  N     . LEU A 1 431 ? 133.815 149.741 89.007  1.00 24.92 ?  431 LEU A N     1 
ATOM   3473  C  CA    . LEU A 1 431 ? 132.509 149.992 89.609  1.00 20.54 ?  431 LEU A CA    1 
ATOM   3474  C  C     . LEU A 1 431 ? 132.388 149.326 90.974  1.00 22.83 ?  431 LEU A C     1 
ATOM   3475  O  O     . LEU A 1 431 ? 131.809 149.902 91.903  1.00 28.68 ?  431 LEU A O     1 
ATOM   3476  C  CB    . LEU A 1 431 ? 131.403 149.508 88.674  1.00 27.17 ?  431 LEU A CB    1 
ATOM   3477  C  CG    . LEU A 1 431 ? 130.712 150.557 87.804  1.00 30.22 ?  431 LEU A CG    1 
ATOM   3478  C  CD1   . LEU A 1 431 ? 129.602 149.915 86.993  1.00 29.53 ?  431 LEU A CD1   1 
ATOM   3479  C  CD2   . LEU A 1 431 ? 130.171 151.692 88.653  1.00 31.29 ?  431 LEU A CD2   1 
ATOM   3480  N  N     . ALA A 1 432 ? 132.920 148.109 91.116  1.00 24.46 ?  432 ALA A N     1 
ATOM   3481  C  CA    . ALA A 1 432 ? 132.917 147.440 92.410  1.00 15.27 ?  432 ALA A CA    1 
ATOM   3482  C  C     . ALA A 1 432 ? 133.772 148.191 93.418  1.00 26.11 ?  432 ALA A C     1 
ATOM   3483  O  O     . ALA A 1 432 ? 133.419 148.278 94.598  1.00 28.99 ?  432 ALA A O     1 
ATOM   3484  C  CB    . ALA A 1 432 ? 133.410 146.003 92.255  1.00 21.06 ?  432 ALA A CB    1 
ATOM   3485  N  N     . THR A 1 433 ? 134.906 148.734 92.972  1.00 28.03 ?  433 THR A N     1 
ATOM   3486  C  CA    . THR A 1 433 ? 135.736 149.547 93.852  1.00 21.24 ?  433 THR A CA    1 
ATOM   3487  C  C     . THR A 1 433 ? 134.987 150.787 94.313  1.00 23.51 ?  433 THR A C     1 
ATOM   3488  O  O     . THR A 1 433 ? 135.053 151.159 95.489  1.00 34.90 ?  433 THR A O     1 
ATOM   3489  C  CB    . THR A 1 433 ? 137.030 149.934 93.138  1.00 27.47 ?  433 THR A CB    1 
ATOM   3490  O  OG1   . THR A 1 433 ? 137.746 148.749 92.766  1.00 29.32 ?  433 THR A OG1   1 
ATOM   3491  C  CG2   . THR A 1 433 ? 137.907 150.784 94.042  1.00 24.32 ?  433 THR A CG2   1 
ATOM   3492  N  N     . ASP A 1 434 ? 134.263 151.438 93.401  1.00 22.85 ?  434 ASP A N     1 
ATOM   3493  C  CA    . ASP A 1 434 ? 133.468 152.602 93.780  1.00 22.59 ?  434 ASP A CA    1 
ATOM   3494  C  C     . ASP A 1 434 ? 132.385 152.232 94.788  1.00 20.26 ?  434 ASP A C     1 
ATOM   3495  O  O     . ASP A 1 434 ? 132.165 152.951 95.769  1.00 24.84 ?  434 ASP A O     1 
ATOM   3496  C  CB    . ASP A 1 434 ? 132.845 153.239 92.539  1.00 24.86 ?  434 ASP A CB    1 
ATOM   3497  C  CG    . ASP A 1 434 ? 133.882 153.797 91.590  1.00 31.71 ?  434 ASP A CG    1 
ATOM   3498  O  OD1   . ASP A 1 434 ? 135.001 154.106 92.046  1.00 35.06 ?  434 ASP A OD1   1 
ATOM   3499  O  OD2   . ASP A 1 434 ? 133.576 153.931 90.386  1.00 33.12 -1 434 ASP A OD2   1 
ATOM   3500  N  N     . SER A 1 435 ? 131.694 151.113 94.559  1.00 22.09 ?  435 SER A N     1 
ATOM   3501  C  CA    . SER A 1 435 ? 130.640 150.689 95.477  1.00 20.46 ?  435 SER A CA    1 
ATOM   3502  C  C     . SER A 1 435 ? 131.203 150.352 96.853  1.00 23.29 ?  435 SER A C     1 
ATOM   3503  O  O     . SER A 1 435 ? 130.616 150.717 97.879  1.00 29.51 ?  435 SER A O     1 
ATOM   3504  C  CB    . SER A 1 435 ? 129.889 149.493 94.894  1.00 23.10 ?  435 SER A CB    1 
ATOM   3505  O  OG    . SER A 1 435 ? 130.656 148.309 95.000  1.00 20.02 ?  435 SER A OG    1 
ATOM   3506  N  N     . LEU A 1 436 ? 132.345 149.664 96.896  1.00 19.07 ?  436 LEU A N     1 
ATOM   3507  C  CA    . LEU A 1 436 ? 132.963 149.331 98.174  1.00 10.90 ?  436 LEU A CA    1 
ATOM   3508  C  C     . LEU A 1 436 ? 133.470 150.579 98.883  1.00 17.35 ?  436 LEU A C     1 
ATOM   3509  O  O     . LEU A 1 436 ? 133.395 150.674 100.113 1.00 21.46 ?  436 LEU A O     1 
ATOM   3510  C  CB    . LEU A 1 436 ? 134.093 148.327 97.958  1.00 22.54 ?  436 LEU A CB    1 
ATOM   3511  C  CG    . LEU A 1 436 ? 133.664 146.921 97.536  1.00 19.18 ?  436 LEU A CG    1 
ATOM   3512  C  CD1   . LEU A 1 436 ? 134.854 146.113 97.046  1.00 10.93 ?  436 LEU A CD1   1 
ATOM   3513  C  CD2   . LEU A 1 436 ? 132.966 146.207 98.676  1.00 20.99 ?  436 LEU A CD2   1 
ATOM   3514  N  N     . THR A 1 437 ? 133.985 151.549 98.125  1.00 23.18 ?  437 THR A N     1 
ATOM   3515  C  CA    . THR A 1 437 ? 134.379 152.825 98.712  1.00 21.46 ?  437 THR A CA    1 
ATOM   3516  C  C     . THR A 1 437 ? 133.183 153.538 99.325  1.00 24.16 ?  437 THR A C     1 
ATOM   3517  O  O     . THR A 1 437 ? 133.282 154.108 100.418 1.00 35.32 ?  437 THR A O     1 
ATOM   3518  C  CB    . THR A 1 437 ? 135.036 153.704 97.651  1.00 19.83 ?  437 THR A CB    1 
ATOM   3519  O  OG1   . THR A 1 437 ? 136.023 152.944 96.945  1.00 21.94 ?  437 THR A OG1   1 
ATOM   3520  C  CG2   . THR A 1 437 ? 135.693 154.912 98.289  1.00 22.56 ?  437 THR A CG2   1 
ATOM   3521  N  N     . HIS A 1 438 ? 132.043 153.522 98.633  1.00 21.99 ?  438 HIS A N     1 
ATOM   3522  C  CA    . HIS A 1 438 ? 130.841 154.140 99.181  1.00 23.39 ?  438 HIS A CA    1 
ATOM   3523  C  C     . HIS A 1 438 ? 130.386 153.431 100.449 1.00 23.90 ?  438 HIS A C     1 
ATOM   3524  O  O     . HIS A 1 438 ? 129.975 154.079 101.420 1.00 31.71 ?  438 HIS A O     1 
ATOM   3525  C  CB    . HIS A 1 438 ? 129.727 154.144 98.137  1.00 26.69 ?  438 HIS A CB    1 
ATOM   3526  C  CG    . HIS A 1 438 ? 128.427 154.678 98.650  1.00 27.28 ?  438 HIS A CG    1 
ATOM   3527  N  ND1   . HIS A 1 438 ? 128.157 156.027 98.729  1.00 27.32 ?  438 HIS A ND1   1 
ATOM   3528  C  CD2   . HIS A 1 438 ? 127.324 154.047 99.116  1.00 28.60 ?  438 HIS A CD2   1 
ATOM   3529  C  CE1   . HIS A 1 438 ? 126.944 156.204 99.220  1.00 31.76 ?  438 HIS A CE1   1 
ATOM   3530  N  NE2   . HIS A 1 438 ? 126.417 155.017 99.463  1.00 31.05 ?  438 HIS A NE2   1 
ATOM   3531  N  N     . VAL A 1 439 ? 130.446 152.097 100.460 1.00 25.03 ?  439 VAL A N     1 
ATOM   3532  C  CA    . VAL A 1 439 ? 130.060 151.351 101.656 1.00 20.09 ?  439 VAL A CA    1 
ATOM   3533  C  C     . VAL A 1 439 ? 130.991 151.684 102.815 1.00 27.11 ?  439 VAL A C     1 
ATOM   3534  O  O     . VAL A 1 439 ? 130.555 151.815 103.964 1.00 36.62 ?  439 VAL A O     1 
ATOM   3535  C  CB    . VAL A 1 439 ? 130.033 149.839 101.362 1.00 23.14 ?  439 VAL A CB    1 
ATOM   3536  C  CG1   . VAL A 1 439 ? 129.761 149.057 102.631 1.00 24.30 ?  439 VAL A CG1   1 
ATOM   3537  C  CG2   . VAL A 1 439 ? 128.980 149.525 100.323 1.00 25.36 ?  439 VAL A CG2   1 
ATOM   3538  N  N     . SER A 1 440 ? 132.287 151.826 102.533 1.00 25.44 ?  440 SER A N     1 
ATOM   3539  C  CA    . SER A 1 440 ? 133.234 152.228 103.568 1.00 20.24 ?  440 SER A CA    1 
ATOM   3540  C  C     . SER A 1 440 ? 132.919 153.623 104.091 1.00 26.38 ?  440 SER A C     1 
ATOM   3541  O  O     . SER A 1 440 ? 132.990 153.874 105.299 1.00 34.05 ?  440 SER A O     1 
ATOM   3542  C  CB    . SER A 1 440 ? 134.661 152.171 103.024 1.00 25.82 ?  440 SER A CB    1 
ATOM   3543  O  OG    . SER A 1 440 ? 135.612 152.203 104.073 1.00 30.51 ?  440 SER A OG    1 
ATOM   3544  N  N     . GLU A 1 441 ? 132.574 154.546 103.192 1.00 29.54 ?  441 GLU A N     1 
ATOM   3545  C  CA    . GLU A 1 441 ? 132.320 155.923 103.597 1.00 21.89 ?  441 GLU A CA    1 
ATOM   3546  C  C     . GLU A 1 441 ? 131.031 156.059 104.397 1.00 31.00 ?  441 GLU A C     1 
ATOM   3547  O  O     . GLU A 1 441 ? 130.944 156.913 105.285 1.00 40.06 ?  441 GLU A O     1 
ATOM   3548  C  CB    . GLU A 1 441 ? 132.278 156.828 102.369 1.00 22.46 ?  441 GLU A CB    1 
ATOM   3549  C  CG    . GLU A 1 441 ? 133.642 157.113 101.771 1.00 28.54 ?  441 GLU A CG    1 
ATOM   3550  C  CD    . GLU A 1 441 ? 133.558 157.901 100.482 1.00 38.58 ?  441 GLU A CD    1 
ATOM   3551  O  OE1   . GLU A 1 441 ? 133.146 157.323 99.453  1.00 38.78 ?  441 GLU A OE1   1 
ATOM   3552  O  OE2   . GLU A 1 441 ? 133.903 159.101 100.493 1.00 37.83 -1 441 GLU A OE2   1 
ATOM   3553  N  N     . THR A 1 442 ? 130.023 155.241 104.104 1.00 32.28 ?  442 THR A N     1 
ATOM   3554  C  CA    . THR A 1 442 ? 128.746 155.328 104.800 1.00 31.30 ?  442 THR A CA    1 
ATOM   3555  C  C     . THR A 1 442 ? 128.696 154.490 106.070 1.00 32.40 ?  442 THR A C     1 
ATOM   3556  O  O     . THR A 1 442 ? 127.675 154.504 106.763 1.00 38.71 ?  442 THR A O     1 
ATOM   3557  C  CB    . THR A 1 442 ? 127.598 154.912 103.873 1.00 30.83 ?  442 THR A CB    1 
ATOM   3558  O  OG1   . THR A 1 442 ? 127.761 153.541 103.489 1.00 30.72 ?  442 THR A OG1   1 
ATOM   3559  C  CG2   . THR A 1 442 ? 127.571 155.789 102.635 1.00 30.57 ?  442 THR A CG2   1 
ATOM   3560  N  N     . THR A 1 443 ? 129.762 153.765 106.392 1.00 31.71 ?  443 THR A N     1 
ATOM   3561  C  CA    . THR A 1 443 ? 129.816 152.977 107.614 1.00 34.28 ?  443 THR A CA    1 
ATOM   3562  C  C     . THR A 1 443 ? 130.359 153.833 108.751 1.00 37.40 ?  443 THR A C     1 
ATOM   3563  O  O     . THR A 1 443 ? 131.401 154.478 108.605 1.00 39.22 ?  443 THR A O     1 
ATOM   3564  C  CB    . THR A 1 443 ? 130.687 151.736 107.422 1.00 33.99 ?  443 THR A CB    1 
ATOM   3565  O  OG1   . THR A 1 443 ? 130.086 150.874 106.448 1.00 38.06 ?  443 THR A OG1   1 
ATOM   3566  C  CG2   . THR A 1 443 ? 130.833 150.981 108.732 1.00 30.56 ?  443 THR A CG2   1 
ATOM   3567  N  N     . ASP A 1 444 ? 129.647 153.840 109.876 1.00 42.90 ?  444 ASP A N     1 
ATOM   3568  C  CA    . ASP A 1 444 ? 130.060 154.602 111.056 1.00 42.22 ?  444 ASP A CA    1 
ATOM   3569  C  C     . ASP A 1 444 ? 129.695 153.788 112.293 1.00 41.14 ?  444 ASP A C     1 
ATOM   3570  O  O     . ASP A 1 444 ? 128.543 153.799 112.733 1.00 42.24 ?  444 ASP A O     1 
ATOM   3571  C  CB    . ASP A 1 444 ? 129.407 155.979 111.082 1.00 43.39 ?  444 ASP A CB    1 
ATOM   3572  C  CG    . ASP A 1 444 ? 130.313 157.039 111.672 1.00 46.17 ?  444 ASP A CG    1 
ATOM   3573  O  OD1   . ASP A 1 444 ? 130.689 156.907 112.855 1.00 45.39 ?  444 ASP A OD1   1 
ATOM   3574  O  OD2   . ASP A 1 444 ? 130.650 158.003 110.954 1.00 47.95 -1 444 ASP A OD2   1 
ATOM   3575  N  N     . ILE A 1 445 ? 130.679 153.089 112.849 1.00 38.07 ?  445 ILE A N     1 
ATOM   3576  C  CA    . ILE A 1 445 ? 130.486 152.281 114.047 1.00 40.95 ?  445 ILE A CA    1 
ATOM   3577  C  C     . ILE A 1 445 ? 130.749 153.179 115.251 1.00 44.55 ?  445 ILE A C     1 
ATOM   3578  O  O     . ILE A 1 445 ? 131.889 153.569 115.509 1.00 44.52 ?  445 ILE A O     1 
ATOM   3579  C  CB    . ILE A 1 445 ? 131.407 151.055 114.055 1.00 39.74 ?  445 ILE A CB    1 
ATOM   3580  C  CG1   . ILE A 1 445 ? 131.320 150.319 112.715 1.00 37.73 ?  445 ILE A CG1   1 
ATOM   3581  C  CG2   . ILE A 1 445 ? 131.055 150.134 115.210 1.00 39.98 ?  445 ILE A CG2   1 
ATOM   3582  C  CD1   . ILE A 1 445 ? 130.250 149.252 112.658 1.00 37.05 ?  445 ILE A CD1   1 
ATOM   3583  N  N     . ARG A 1 446 ? 129.692 153.503 115.995 1.00 47.24 ?  446 ARG A N     1 
ATOM   3584  C  CA    . ARG A 1 446 ? 129.773 154.461 117.089 1.00 50.94 ?  446 ARG A CA    1 
ATOM   3585  C  C     . ARG A 1 446 ? 129.953 153.791 118.446 1.00 49.67 ?  446 ARG A C     1 
ATOM   3586  O  O     . ARG A 1 446 ? 129.783 154.445 119.481 1.00 45.92 ?  446 ARG A O     1 
ATOM   3587  C  CB    . ARG A 1 446 ? 128.535 155.360 117.092 1.00 47.16 ?  446 ARG A CB    1 
ATOM   3588  C  CG    . ARG A 1 446 ? 127.217 154.610 116.998 1.00 46.72 ?  446 ARG A CG    1 
ATOM   3589  C  CD    . ARG A 1 446 ? 126.078 155.531 116.577 1.00 50.06 ?  446 ARG A CD    1 
ATOM   3590  N  NE    . ARG A 1 446 ? 126.316 156.143 115.274 1.00 52.22 ?  446 ARG A NE    1 
ATOM   3591  C  CZ    . ARG A 1 446 ? 126.754 157.381 115.090 1.00 52.70 ?  446 ARG A CZ    1 
ATOM   3592  N  NH1   . ARG A 1 446 ? 126.999 158.187 116.109 1.00 49.54 1  446 ARG A NH1   1 
ATOM   3593  N  NH2   . ARG A 1 446 ? 126.951 157.822 113.851 1.00 51.25 ?  446 ARG A NH2   1 
ATOM   3594  N  N     . ASN A 1 447 ? 130.293 152.502 118.464 1.00 39.92 ?  447 ASN A N     1 
ATOM   3595  C  CA    . ASN A 1 447 ? 130.614 151.810 119.702 1.00 34.85 ?  447 ASN A CA    1 
ATOM   3596  C  C     . ASN A 1 447 ? 131.924 151.041 119.627 1.00 35.19 ?  447 ASN A C     1 
ATOM   3597  O  O     . ASN A 1 447 ? 132.300 150.393 120.609 1.00 36.74 ?  447 ASN A O     1 
ATOM   3598  C  CB    . ASN A 1 447 ? 129.479 150.854 120.096 1.00 34.46 ?  447 ASN A CB    1 
ATOM   3599  C  CG    . ASN A 1 447 ? 128.732 151.321 121.326 1.00 33.05 ?  447 ASN A CG    1 
ATOM   3600  O  OD1   . ASN A 1 447 ? 129.334 151.611 122.359 1.00 37.76 ?  447 ASN A OD1   1 
ATOM   3601  N  ND2   . ASN A 1 447 ? 127.413 151.407 121.220 1.00 34.04 ?  447 ASN A ND2   1 
ATOM   3602  N  N     . ALA A 1 448 ? 132.624 151.090 118.495 1.00 38.72 ?  448 ALA A N     1 
ATOM   3603  C  CA    . ALA A 1 448 ? 133.955 150.510 118.333 1.00 33.62 ?  448 ALA A CA    1 
ATOM   3604  C  C     . ALA A 1 448 ? 134.866 151.628 117.852 1.00 33.26 ?  448 ALA A C     1 
ATOM   3605  O  O     . ALA A 1 448 ? 134.988 151.864 116.640 1.00 33.62 ?  448 ALA A O     1 
ATOM   3606  C  CB    . ALA A 1 448 ? 133.938 149.337 117.355 1.00 29.25 ?  448 ALA A CB    1 
ATOM   3607  N  N     . PRO A 1 449 ? 135.508 152.360 118.768 1.00 30.75 ?  449 PRO A N     1 
ATOM   3608  C  CA    . PRO A 1 449 ? 136.273 153.548 118.351 1.00 27.60 ?  449 PRO A CA    1 
ATOM   3609  C  C     . PRO A 1 449 ? 137.408 153.242 117.391 1.00 29.34 ?  449 PRO A C     1 
ATOM   3610  O  O     . PRO A 1 449 ? 137.640 154.008 116.448 1.00 29.06 ?  449 PRO A O     1 
ATOM   3611  C  CB    . PRO A 1 449 ? 136.798 154.111 119.680 1.00 27.90 ?  449 PRO A CB    1 
ATOM   3612  C  CG    . PRO A 1 449 ? 136.033 153.408 120.748 1.00 31.86 ?  449 PRO A CG    1 
ATOM   3613  C  CD    . PRO A 1 449 ? 135.642 152.088 120.206 1.00 30.43 ?  449 PRO A CD    1 
ATOM   3614  N  N     . ALA A 1 450 ? 138.118 152.132 117.600 1.00 31.60 ?  450 ALA A N     1 
ATOM   3615  C  CA    . ALA A 1 450 ? 139.243 151.808 116.734 1.00 23.57 ?  450 ALA A CA    1 
ATOM   3616  C  C     . ALA A 1 450 ? 138.775 151.337 115.365 1.00 25.16 ?  450 ALA A C     1 
ATOM   3617  O  O     . ALA A 1 450 ? 139.416 151.647 114.355 1.00 27.25 ?  450 ALA A O     1 
ATOM   3618  C  CB    . ALA A 1 450 ? 140.128 150.755 117.396 1.00 24.69 ?  450 ALA A CB    1 
ATOM   3619  N  N     . VAL A 1 451 ? 137.661 150.606 115.310 1.00 30.39 ?  451 VAL A N     1 
ATOM   3620  C  CA    . VAL A 1 451 ? 137.083 150.218 114.027 1.00 23.44 ?  451 VAL A CA    1 
ATOM   3621  C  C     . VAL A 1 451 ? 136.688 151.457 113.234 1.00 24.66 ?  451 VAL A C     1 
ATOM   3622  O  O     . VAL A 1 451 ? 136.974 151.568 112.037 1.00 30.89 ?  451 VAL A O     1 
ATOM   3623  C  CB    . VAL A 1 451 ? 135.884 149.276 114.242 1.00 25.62 ?  451 VAL A CB    1 
ATOM   3624  C  CG1   . VAL A 1 451 ? 135.033 149.193 112.988 1.00 26.43 ?  451 VAL A CG1   1 
ATOM   3625  C  CG2   . VAL A 1 451 ? 136.363 147.898 114.655 1.00 25.40 ?  451 VAL A CG2   1 
ATOM   3626  N  N     . ARG A 1 452 ? 136.037 152.413 113.897 1.00 24.67 ?  452 ARG A N     1 
ATOM   3627  C  CA    . ARG A 1 452 ? 135.639 153.652 113.235 1.00 25.38 ?  452 ARG A CA    1 
ATOM   3628  C  C     . ARG A 1 452 ? 136.855 154.431 112.748 1.00 26.48 ?  452 ARG A C     1 
ATOM   3629  O  O     . ARG A 1 452 ? 136.885 154.915 111.608 1.00 31.93 ?  452 ARG A O     1 
ATOM   3630  C  CB    . ARG A 1 452 ? 134.805 154.498 114.198 1.00 26.48 ?  452 ARG A CB    1 
ATOM   3631  C  CG    . ARG A 1 452 ? 133.767 155.385 113.540 1.00 29.65 ?  452 ARG A CG    1 
ATOM   3632  C  CD    . ARG A 1 452 ? 133.949 156.830 113.964 1.00 28.18 ?  452 ARG A CD    1 
ATOM   3633  N  NE    . ARG A 1 452 ? 133.554 157.053 115.349 1.00 37.09 ?  452 ARG A NE    1 
ATOM   3634  C  CZ    . ARG A 1 452 ? 132.361 157.490 115.729 1.00 39.49 ?  452 ARG A CZ    1 
ATOM   3635  N  NH1   . ARG A 1 452 ? 131.414 157.767 114.848 1.00 35.94 1  452 ARG A NH1   1 
ATOM   3636  N  NH2   . ARG A 1 452 ? 132.115 157.657 117.025 1.00 36.35 ?  452 ARG A NH2   1 
ATOM   3637  N  N     . ARG A 1 453 ? 137.875 154.558 113.600 1.00 27.41 ?  453 ARG A N     1 
ATOM   3638  C  CA    . ARG A 1 453 ? 139.060 155.324 113.225 1.00 24.98 ?  453 ARG A CA    1 
ATOM   3639  C  C     . ARG A 1 453 ? 139.788 154.676 112.055 1.00 30.87 ?  453 ARG A C     1 
ATOM   3640  O  O     . ARG A 1 453 ? 140.215 155.367 111.124 1.00 35.58 ?  453 ARG A O     1 
ATOM   3641  C  CB    . ARG A 1 453 ? 139.996 155.470 114.424 1.00 26.76 ?  453 ARG A CB    1 
ATOM   3642  C  CG    . ARG A 1 453 ? 141.121 156.463 114.204 1.00 30.43 ?  453 ARG A CG    1 
ATOM   3643  C  CD    . ARG A 1 453 ? 142.261 156.244 115.180 1.00 27.05 ?  453 ARG A CD    1 
ATOM   3644  N  NE    . ARG A 1 453 ? 143.523 156.748 114.654 1.00 29.09 ?  453 ARG A NE    1 
ATOM   3645  C  CZ    . ARG A 1 453 ? 144.711 156.229 114.929 1.00 30.96 ?  453 ARG A CZ    1 
ATOM   3646  N  NH1   . ARG A 1 453 ? 144.841 155.191 115.738 1.00 31.00 1  453 ARG A NH1   1 
ATOM   3647  N  NH2   . ARG A 1 453 ? 145.796 156.764 114.379 1.00 30.21 ?  453 ARG A NH2   1 
ATOM   3648  N  N     . ALA A 1 454 ? 139.931 153.350 112.080 1.00 26.81 ?  454 ALA A N     1 
ATOM   3649  C  CA    . ALA A 1 454 ? 140.618 152.665 110.994 1.00 20.64 ?  454 ALA A CA    1 
ATOM   3650  C  C     . ALA A 1 454 ? 139.797 152.673 109.714 1.00 19.20 ?  454 ALA A C     1 
ATOM   3651  O  O     . ALA A 1 454 ? 140.366 152.696 108.621 1.00 25.25 ?  454 ALA A O     1 
ATOM   3652  C  CB    . ALA A 1 454 ? 140.958 151.235 111.403 1.00 23.13 ?  454 ALA A CB    1 
ATOM   3653  N  N     . ASN A 1 455 ? 138.468 152.654 109.820 1.00 23.57 ?  455 ASN A N     1 
ATOM   3654  C  CA    . ASN A 1 455 ? 137.644 152.779 108.625 1.00 23.02 ?  455 ASN A CA    1 
ATOM   3655  C  C     . ASN A 1 455 ? 137.795 154.158 107.999 1.00 26.24 ?  455 ASN A C     1 
ATOM   3656  O  O     . ASN A 1 455 ? 137.836 154.286 106.770 1.00 32.44 ?  455 ASN A O     1 
ATOM   3657  C  CB    . ASN A 1 455 ? 136.181 152.497 108.963 1.00 21.33 ?  455 ASN A CB    1 
ATOM   3658  C  CG    . ASN A 1 455 ? 135.290 152.516 107.740 1.00 27.83 ?  455 ASN A CG    1 
ATOM   3659  O  OD1   . ASN A 1 455 ? 135.444 151.698 106.834 1.00 34.90 ?  455 ASN A OD1   1 
ATOM   3660  N  ND2   . ASN A 1 455 ? 134.351 153.452 107.705 1.00 26.61 ?  455 ASN A ND2   1 
ATOM   3661  N  N     . LYS A 1 456 ? 137.874 155.202 108.826 1.00 29.69 ?  456 LYS A N     1 
ATOM   3662  C  CA    . LYS A 1 456 ? 138.055 156.544 108.283 1.00 26.25 ?  456 LYS A CA    1 
ATOM   3663  C  C     . LYS A 1 456 ? 139.457 156.739 107.716 1.00 27.17 ?  456 LYS A C     1 
ATOM   3664  O  O     . LYS A 1 456 ? 139.632 157.432 106.708 1.00 31.74 ?  456 LYS A O     1 
ATOM   3665  C  CB    . LYS A 1 456 ? 137.759 157.594 109.353 1.00 26.62 ?  456 LYS A CB    1 
ATOM   3666  C  CG    . LYS A 1 456 ? 136.359 157.515 109.927 1.00 29.67 ?  456 LYS A CG    1 
ATOM   3667  C  CD    . LYS A 1 456 ? 136.018 158.760 110.723 1.00 34.00 ?  456 LYS A CD    1 
ATOM   3668  C  CE    . LYS A 1 456 ? 134.532 158.830 111.026 1.00 32.56 ?  456 LYS A CE    1 
ATOM   3669  N  NZ    . LYS A 1 456 ? 133.707 158.444 109.849 1.00 33.57 1  456 LYS A NZ    1 
ATOM   3670  N  N     . ALA A 1 457 ? 140.468 156.138 108.342 1.00 26.25 ?  457 ALA A N     1 
ATOM   3671  C  CA    . ALA A 1 457 ? 141.852 156.397 107.965 1.00 22.46 ?  457 ALA A CA    1 
ATOM   3672  C  C     . ALA A 1 457 ? 142.343 155.489 106.841 1.00 27.03 ?  457 ALA A C     1 
ATOM   3673  O  O     . ALA A 1 457 ? 142.856 155.972 105.829 1.00 31.58 ?  457 ALA A O     1 
ATOM   3674  C  CB    . ALA A 1 457 ? 142.760 156.251 109.189 1.00 22.61 ?  457 ALA A CB    1 
ATOM   3675  N  N     . MET A 1 458 ? 142.198 154.175 107.007 1.00 29.41 ?  458 MET A N     1 
ATOM   3676  C  CA    . MET A 1 458 ? 142.722 153.223 106.035 1.00 19.45 ?  458 MET A CA    1 
ATOM   3677  C  C     . MET A 1 458 ? 141.873 153.167 104.773 1.00 21.76 ?  458 MET A C     1 
ATOM   3678  O  O     . MET A 1 458 ? 142.411 153.002 103.673 1.00 29.94 ?  458 MET A O     1 
ATOM   3679  C  CB    . MET A 1 458 ? 142.815 151.834 106.667 1.00 22.04 ?  458 MET A CB    1 
ATOM   3680  C  CG    . MET A 1 458 ? 143.493 151.814 108.022 1.00 22.23 ?  458 MET A CG    1 
ATOM   3681  S  SD    . MET A 1 458 ? 145.232 152.265 107.917 1.00 33.05 ?  458 MET A SD    1 
ATOM   3682  C  CE    . MET A 1 458 ? 145.989 150.644 107.854 1.00 25.27 ?  458 MET A CE    1 
ATOM   3683  N  N     . LYS A 1 459 ? 140.552 153.295 104.912 1.00 17.12 ?  459 LYS A N     1 
ATOM   3684  C  CA    . LYS A 1 459 ? 139.622 153.187 103.786 1.00 21.91 ?  459 LYS A CA    1 
ATOM   3685  C  C     . LYS A 1 459 ? 139.803 151.864 103.044 1.00 17.93 ?  459 LYS A C     1 
ATOM   3686  O  O     . LYS A 1 459 ? 139.794 151.814 101.814 1.00 25.40 ?  459 LYS A O     1 
ATOM   3687  C  CB    . LYS A 1 459 ? 139.770 154.372 102.829 1.00 21.80 ?  459 LYS A CB    1 
ATOM   3688  C  CG    . LYS A 1 459 ? 139.751 155.725 103.512 1.00 24.86 ?  459 LYS A CG    1 
ATOM   3689  C  CD    . LYS A 1 459 ? 140.677 156.700 102.814 1.00 25.02 ?  459 LYS A CD    1 
ATOM   3690  C  CE    . LYS A 1 459 ? 140.675 158.050 103.504 1.00 28.55 ?  459 LYS A CE    1 
ATOM   3691  N  NZ    . LYS A 1 459 ? 141.702 158.958 102.927 1.00 31.75 1  459 LYS A NZ    1 
ATOM   3692  N  N     . SER A 1 460 ? 139.969 150.785 103.802 1.00 20.38 ?  460 SER A N     1 
ATOM   3693  C  CA    . SER A 1 460 ? 140.229 149.475 103.222 1.00 14.03 ?  460 SER A CA    1 
ATOM   3694  C  C     . SER A 1 460 ? 138.946 148.850 102.695 1.00 20.49 ?  460 SER A C     1 
ATOM   3695  O  O     . SER A 1 460 ? 137.884 148.954 103.314 1.00 29.78 ?  460 SER A O     1 
ATOM   3696  C  CB    . SER A 1 460 ? 140.866 148.549 104.256 1.00 8.71  ?  460 SER A CB    1 
ATOM   3697  O  OG    . SER A 1 460 ? 141.953 149.180 104.907 1.00 30.12 ?  460 SER A OG    1 
ATOM   3698  N  N     . ILE A 1 461 ? 139.055 148.193 101.542 1.00 13.07 ?  461 ILE A N     1 
ATOM   3699  C  CA    . ILE A 1 461 ? 137.953 147.453 100.947 1.00 14.90 ?  461 ILE A CA    1 
ATOM   3700  C  C     . ILE A 1 461 ? 138.456 146.063 100.594 1.00 15.17 ?  461 ILE A C     1 
ATOM   3701  O  O     . ILE A 1 461 ? 139.657 145.824 100.465 1.00 22.96 ?  461 ILE A O     1 
ATOM   3702  C  CB    . ILE A 1 461 ? 137.380 148.152 99.695  1.00 14.02 ?  461 ILE A CB    1 
ATOM   3703  C  CG1   . ILE A 1 461 ? 138.458 148.285 98.620  1.00 7.16  ?  461 ILE A CG1   1 
ATOM   3704  C  CG2   . ILE A 1 461 ? 136.810 149.514 100.057 1.00 14.31 ?  461 ILE A CG2   1 
ATOM   3705  C  CD1   . ILE A 1 461 ? 137.984 148.957 97.361  1.00 7.09  ?  461 ILE A CD1   1 
ATOM   3706  N  N     . GLY A 1 462 ? 137.517 145.133 100.461 1.00 16.88 ?  462 GLY A N     1 
ATOM   3707  C  CA    . GLY A 1 462 ? 137.867 143.815 99.977  1.00 8.05  ?  462 GLY A CA    1 
ATOM   3708  C  C     . GLY A 1 462 ? 137.080 143.426 98.747  1.00 5.76  ?  462 GLY A C     1 
ATOM   3709  O  O     . GLY A 1 462 ? 135.873 143.188 98.830  1.00 24.60 ?  462 GLY A O     1 
ATOM   3710  N  N     . LEU A 1 463 ? 137.751 143.344 97.605  1.00 13.49 ?  463 LEU A N     1 
ATOM   3711  C  CA    . LEU A 1 463 ? 137.119 142.949 96.353  1.00 11.99 ?  463 LEU A CA    1 
ATOM   3712  C  C     . LEU A 1 463 ? 137.579 141.538 96.014  1.00 15.77 ?  463 LEU A C     1 
ATOM   3713  O  O     . LEU A 1 463 ? 138.722 141.333 95.595  1.00 27.78 ?  463 LEU A O     1 
ATOM   3714  C  CB    . LEU A 1 463 ? 137.458 143.929 95.232  1.00 18.12 ?  463 LEU A CB    1 
ATOM   3715  C  CG    . LEU A 1 463 ? 136.873 143.606 93.854  1.00 17.19 ?  463 LEU A CG    1 
ATOM   3716  C  CD1   . LEU A 1 463 ? 135.377 143.366 93.948  1.00 7.19  ?  463 LEU A CD1   1 
ATOM   3717  C  CD2   . LEU A 1 463 ? 137.179 144.716 92.863  1.00 15.33 ?  463 LEU A CD2   1 
ATOM   3718  N  N     . GLY A 1 464 ? 136.689 140.567 96.202  1.00 17.43 ?  464 GLY A N     1 
ATOM   3719  C  CA    . GLY A 1 464 ? 136.980 139.182 95.916  1.00 11.70 ?  464 GLY A CA    1 
ATOM   3720  C  C     . GLY A 1 464 ? 136.425 138.739 94.576  1.00 11.76 ?  464 GLY A C     1 
ATOM   3721  O  O     . GLY A 1 464 ? 135.938 139.532 93.768  1.00 18.98 ?  464 GLY A O     1 
ATOM   3722  N  N     . ALA A 1 465 ? 136.514 137.435 94.343  1.00 14.71 ?  465 ALA A N     1 
ATOM   3723  C  CA    . ALA A 1 465 ? 135.971 136.826 93.144  1.00 11.19 ?  465 ALA A CA    1 
ATOM   3724  C  C     . ALA A 1 465 ? 135.397 135.465 93.500  1.00 16.81 ?  465 ALA A C     1 
ATOM   3725  O  O     . ALA A 1 465 ? 135.772 134.854 94.502  1.00 29.03 ?  465 ALA A O     1 
ATOM   3726  C  CB    . ALA A 1 465 ? 137.035 136.693 92.047  1.00 15.71 ?  465 ALA A CB    1 
ATOM   3727  N  N     . MET A 1 466 ? 134.464 135.002 92.672  1.00 22.27 ?  466 MET A N     1 
ATOM   3728  C  CA    . MET A 1 466 ? 133.910 133.663 92.795  1.00 21.62 ?  466 MET A CA    1 
ATOM   3729  C  C     . MET A 1 466 ? 133.727 133.089 91.398  1.00 19.91 ?  466 MET A C     1 
ATOM   3730  O  O     . MET A 1 466 ? 134.035 133.737 90.393  1.00 23.91 ?  466 MET A O     1 
ATOM   3731  C  CB    . MET A 1 466 ? 132.582 133.655 93.556  1.00 26.40 ?  466 MET A CB    1 
ATOM   3732  C  CG    . MET A 1 466 ? 131.577 134.683 93.086  1.00 27.60 ?  466 MET A CG    1 
ATOM   3733  S  SD    . MET A 1 466 ? 130.049 134.567 94.028  1.00 40.18 ?  466 MET A SD    1 
ATOM   3734  C  CE    . MET A 1 466 ? 129.518 136.267 94.007  1.00 26.82 ?  466 MET A CE    1 
ATOM   3735  N  N     . ASN A 1 467 ? 133.217 131.857 91.347  1.00 20.36 ?  467 ASN A N     1 
ATOM   3736  C  CA    . ASN A 1 467 ? 132.946 131.152 90.095  1.00 20.74 ?  467 ASN A CA    1 
ATOM   3737  C  C     . ASN A 1 467 ? 134.219 130.890 89.298  1.00 21.97 ?  467 ASN A C     1 
ATOM   3738  O  O     . ASN A 1 467 ? 134.182 130.787 88.072  1.00 27.77 ?  467 ASN A O     1 
ATOM   3739  C  CB    . ASN A 1 467 ? 131.927 131.905 89.234  1.00 21.02 ?  467 ASN A CB    1 
ATOM   3740  C  CG    . ASN A 1 467 ? 130.880 130.992 88.641  1.00 26.60 ?  467 ASN A CG    1 
ATOM   3741  O  OD1   . ASN A 1 467 ? 130.824 129.806 88.959  1.00 30.58 ?  467 ASN A OD1   1 
ATOM   3742  N  ND2   . ASN A 1 467 ? 130.035 131.543 87.784  1.00 28.87 ?  467 ASN A ND2   1 
ATOM   3743  N  N     . LEU A 1 468 ? 135.360 130.788 89.981  1.00 17.20 ?  468 LEU A N     1 
ATOM   3744  C  CA    . LEU A 1 468 ? 136.589 130.413 89.292  1.00 18.24 ?  468 LEU A CA    1 
ATOM   3745  C  C     . LEU A 1 468 ? 136.509 128.980 88.785  1.00 22.11 ?  468 LEU A C     1 
ATOM   3746  O  O     . LEU A 1 468 ? 136.762 128.711 87.604  1.00 24.19 ?  468 LEU A O     1 
ATOM   3747  C  CB    . LEU A 1 468 ? 137.791 130.588 90.220  1.00 22.48 ?  468 LEU A CB    1 
ATOM   3748  C  CG    . LEU A 1 468 ? 139.101 129.987 89.704  1.00 20.24 ?  468 LEU A CG    1 
ATOM   3749  C  CD1   . LEU A 1 468 ? 139.670 130.820 88.571  1.00 17.75 ?  468 LEU A CD1   1 
ATOM   3750  C  CD2   . LEU A 1 468 ? 140.114 129.833 90.819  1.00 14.67 ?  468 LEU A CD2   1 
ATOM   3751  N  N     . HIS A 1 469 ? 136.140 128.046 89.664  1.00 25.00 ?  469 HIS A N     1 
ATOM   3752  C  CA    . HIS A 1 469 ? 135.997 126.660 89.241  1.00 15.91 ?  469 HIS A CA    1 
ATOM   3753  C  C     . HIS A 1 469 ? 134.836 126.500 88.273  1.00 25.43 ?  469 HIS A C     1 
ATOM   3754  O  O     . HIS A 1 469 ? 134.919 125.708 87.331  1.00 35.75 ?  469 HIS A O     1 
ATOM   3755  C  CB    . HIS A 1 469 ? 135.813 125.745 90.450  1.00 20.66 ?  469 HIS A CB    1 
ATOM   3756  C  CG    . HIS A 1 469 ? 135.941 124.289 90.125  1.00 24.47 ?  469 HIS A CG    1 
ATOM   3757  N  ND1   . HIS A 1 469 ? 135.663 123.295 91.037  1.00 30.41 ?  469 HIS A ND1   1 
ATOM   3758  C  CD2   . HIS A 1 469 ? 136.325 123.660 88.990  1.00 25.57 ?  469 HIS A CD2   1 
ATOM   3759  C  CE1   . HIS A 1 469 ? 135.863 122.117 90.475  1.00 26.91 ?  469 HIS A CE1   1 
ATOM   3760  N  NE2   . HIS A 1 469 ? 136.265 122.310 89.233  1.00 23.55 ?  469 HIS A NE2   1 
ATOM   3761  N  N     . GLY A 1 470 ? 133.745 127.234 88.488  1.00 23.18 ?  470 GLY A N     1 
ATOM   3762  C  CA    . GLY A 1 470 ? 132.639 127.176 87.545  1.00 18.91 ?  470 GLY A CA    1 
ATOM   3763  C  C     . GLY A 1 470 ? 133.039 127.646 86.161  1.00 13.76 ?  470 GLY A C     1 
ATOM   3764  O  O     . GLY A 1 470 ? 132.712 127.010 85.155  1.00 30.84 ?  470 GLY A O     1 
ATOM   3765  N  N     . TYR A 1 471 ? 133.769 128.761 86.095  1.00 17.80 ?  471 TYR A N     1 
ATOM   3766  C  CA    . TYR A 1 471 ? 134.229 129.273 84.810  1.00 20.66 ?  471 TYR A CA    1 
ATOM   3767  C  C     . TYR A 1 471 ? 135.192 128.301 84.140  1.00 26.74 ?  471 TYR A C     1 
ATOM   3768  O  O     . TYR A 1 471 ? 135.110 128.076 82.929  1.00 30.29 ?  471 TYR A O     1 
ATOM   3769  C  CB    . TYR A 1 471 ? 134.894 130.637 84.994  1.00 21.83 ?  471 TYR A CB    1 
ATOM   3770  C  CG    . TYR A 1 471 ? 135.505 131.189 83.729  1.00 25.96 ?  471 TYR A CG    1 
ATOM   3771  C  CD1   . TYR A 1 471 ? 134.709 131.746 82.740  1.00 25.94 ?  471 TYR A CD1   1 
ATOM   3772  C  CD2   . TYR A 1 471 ? 136.875 131.140 83.518  1.00 20.53 ?  471 TYR A CD2   1 
ATOM   3773  C  CE1   . TYR A 1 471 ? 135.260 132.248 81.580  1.00 26.67 ?  471 TYR A CE1   1 
ATOM   3774  C  CE2   . TYR A 1 471 ? 137.435 131.636 82.360  1.00 20.47 ?  471 TYR A CE2   1 
ATOM   3775  C  CZ    . TYR A 1 471 ? 136.623 132.189 81.396  1.00 28.50 ?  471 TYR A CZ    1 
ATOM   3776  O  OH    . TYR A 1 471 ? 137.178 132.686 80.241  1.00 31.36 ?  471 TYR A OH    1 
ATOM   3777  N  N     . LEU A 1 472 ? 136.116 127.721 84.910  1.00 22.56 ?  472 LEU A N     1 
ATOM   3778  C  CA    . LEU A 1 472 ? 137.085 126.800 84.322  1.00 21.54 ?  472 LEU A CA    1 
ATOM   3779  C  C     . LEU A 1 472 ? 136.418 125.515 83.844  1.00 26.87 ?  472 LEU A C     1 
ATOM   3780  O  O     . LEU A 1 472 ? 136.729 125.017 82.757  1.00 31.87 ?  472 LEU A O     1 
ATOM   3781  C  CB    . LEU A 1 472 ? 138.190 126.489 85.330  1.00 27.45 ?  472 LEU A CB    1 
ATOM   3782  C  CG    . LEU A 1 472 ? 139.086 127.659 85.741  1.00 29.85 ?  472 LEU A CG    1 
ATOM   3783  C  CD1   . LEU A 1 472 ? 139.858 127.313 86.999  1.00 22.43 ?  472 LEU A CD1   1 
ATOM   3784  C  CD2   . LEU A 1 472 ? 140.028 128.049 84.615  1.00 22.59 ?  472 LEU A CD2   1 
ATOM   3785  N  N     . ALA A 1 473 ? 135.502 124.962 84.643  1.00 28.89 ?  473 ALA A N     1 
ATOM   3786  C  CA    . ALA A 1 473 ? 134.829 123.726 84.267  1.00 25.05 ?  473 ALA A CA    1 
ATOM   3787  C  C     . ALA A 1 473 ? 133.898 123.939 83.081  1.00 32.50 ?  473 ALA A C     1 
ATOM   3788  O  O     . ALA A 1 473 ? 133.751 123.049 82.236  1.00 40.07 ?  473 ALA A O     1 
ATOM   3789  C  CB    . ALA A 1 473 ? 134.059 123.170 85.464  1.00 26.38 ?  473 ALA A CB    1 
ATOM   3790  N  N     . GLN A 1 474 ? 133.261 125.106 83.000  1.00 28.34 ?  474 GLN A N     1 
ATOM   3791  C  CA    . GLN A 1 474 ? 132.413 125.410 81.858  1.00 25.63 ?  474 GLN A CA    1 
ATOM   3792  C  C     . GLN A 1 474 ? 133.210 125.821 80.628  1.00 24.52 ?  474 GLN A C     1 
ATOM   3793  O  O     . GLN A 1 474 ? 132.616 126.019 79.564  1.00 35.27 ?  474 GLN A O     1 
ATOM   3794  C  CB    . GLN A 1 474 ? 131.412 126.508 82.223  1.00 27.87 ?  474 GLN A CB    1 
ATOM   3795  C  CG    . GLN A 1 474 ? 130.258 126.008 83.071  1.00 31.27 ?  474 GLN A CG    1 
ATOM   3796  C  CD    . GLN A 1 474 ? 129.449 127.132 83.677  1.00 30.88 ?  474 GLN A CD    1 
ATOM   3797  O  OE1   . GLN A 1 474 ? 128.763 127.869 82.971  1.00 33.25 ?  474 GLN A OE1   1 
ATOM   3798  N  NE2   . GLN A 1 474 ? 129.522 127.269 84.995  1.00 31.70 ?  474 GLN A NE2   1 
ATOM   3799  N  N     . ASN A 1 475 ? 134.529 125.959 80.749  1.00 30.94 ?  475 ASN A N     1 
ATOM   3800  C  CA    . ASN A 1 475 ? 135.400 126.248 79.619  1.00 32.64 ?  475 ASN A CA    1 
ATOM   3801  C  C     . ASN A 1 475 ? 136.346 125.096 79.308  1.00 33.12 ?  475 ASN A C     1 
ATOM   3802  O  O     . ASN A 1 475 ? 137.313 125.285 78.563  1.00 36.54 ?  475 ASN A O     1 
ATOM   3803  C  CB    . ASN A 1 475 ? 136.197 127.527 79.879  1.00 34.58 ?  475 ASN A CB    1 
ATOM   3804  C  CG    . ASN A 1 475 ? 135.357 128.777 79.727  1.00 30.33 ?  475 ASN A CG    1 
ATOM   3805  O  OD1   . ASN A 1 475 ? 135.310 129.379 78.656  1.00 35.59 ?  475 ASN A OD1   1 
ATOM   3806  N  ND2   . ASN A 1 475 ? 134.680 129.167 80.798  1.00 25.96 ?  475 ASN A ND2   1 
ATOM   3807  N  N     . GLY A 1 476 ? 136.092 123.914 79.859  1.00 29.91 ?  476 GLY A N     1 
ATOM   3808  C  CA    . GLY A 1 476 ? 136.930 122.756 79.603  1.00 30.17 ?  476 GLY A CA    1 
ATOM   3809  C  C     . GLY A 1 476 ? 138.338 122.859 80.146  1.00 34.66 ?  476 GLY A C     1 
ATOM   3810  O  O     . GLY A 1 476 ? 139.289 122.445 79.471  1.00 36.43 ?  476 GLY A O     1 
ATOM   3811  N  N     . ILE A 1 477 ? 138.499 123.403 81.349  1.00 31.37 ?  477 ILE A N     1 
ATOM   3812  C  CA    . ILE A 1 477 ? 139.801 123.536 81.989  1.00 28.71 ?  477 ILE A CA    1 
ATOM   3813  C  C     . ILE A 1 477 ? 139.733 122.878 83.359  1.00 31.58 ?  477 ILE A C     1 
ATOM   3814  O  O     . ILE A 1 477 ? 138.848 123.194 84.160  1.00 35.25 ?  477 ILE A O     1 
ATOM   3815  C  CB    . ILE A 1 477 ? 140.229 125.010 82.120  1.00 28.00 ?  477 ILE A CB    1 
ATOM   3816  C  CG1   . ILE A 1 477 ? 140.231 125.692 80.751  1.00 30.91 ?  477 ILE A CG1   1 
ATOM   3817  C  CG2   . ILE A 1 477 ? 141.599 125.107 82.760  1.00 31.37 ?  477 ILE A CG2   1 
ATOM   3818  C  CD1   . ILE A 1 477 ? 140.170 127.198 80.822  1.00 32.68 ?  477 ILE A CD1   1 
ATOM   3819  N  N     . ALA A 1 478 ? 140.662 121.963 83.623  1.00 31.56 ?  478 ALA A N     1 
ATOM   3820  C  CA    . ALA A 1 478 ? 140.736 121.332 84.932  1.00 26.59 ?  478 ALA A CA    1 
ATOM   3821  C  C     . ALA A 1 478 ? 141.283 122.314 85.958  1.00 33.48 ?  478 ALA A C     1 
ATOM   3822  O  O     . ALA A 1 478 ? 142.162 123.123 85.657  1.00 35.57 ?  478 ALA A O     1 
ATOM   3823  C  CB    . ALA A 1 478 ? 141.615 120.085 84.874  1.00 28.38 ?  478 ALA A CB    1 
ATOM   3824  N  N     . TYR A 1 479 ? 140.756 122.235 87.183  1.00 31.35 ?  479 TYR A N     1 
ATOM   3825  C  CA    . TYR A 1 479 ? 141.185 123.151 88.235  1.00 22.61 ?  479 TYR A CA    1 
ATOM   3826  C  C     . TYR A 1 479 ? 142.666 122.982 88.546  1.00 30.04 ?  479 TYR A C     1 
ATOM   3827  O  O     . TYR A 1 479 ? 143.374 123.967 88.782  1.00 39.24 ?  479 TYR A O     1 
ATOM   3828  C  CB    . TYR A 1 479 ? 140.341 122.931 89.491  1.00 21.64 ?  479 TYR A CB    1 
ATOM   3829  C  CG    . TYR A 1 479 ? 140.526 123.984 90.560  1.00 27.42 ?  479 TYR A CG    1 
ATOM   3830  C  CD1   . TYR A 1 479 ? 139.741 125.127 90.573  1.00 23.50 ?  479 TYR A CD1   1 
ATOM   3831  C  CD2   . TYR A 1 479 ? 141.476 123.829 91.561  1.00 28.82 ?  479 TYR A CD2   1 
ATOM   3832  C  CE1   . TYR A 1 479 ? 139.899 126.089 91.546  1.00 24.74 ?  479 TYR A CE1   1 
ATOM   3833  C  CE2   . TYR A 1 479 ? 141.642 124.789 92.538  1.00 26.82 ?  479 TYR A CE2   1 
ATOM   3834  C  CZ    . TYR A 1 479 ? 140.851 125.916 92.526  1.00 30.44 ?  479 TYR A CZ    1 
ATOM   3835  O  OH    . TYR A 1 479 ? 141.011 126.875 93.498  1.00 31.19 ?  479 TYR A OH    1 
ATOM   3836  N  N     . GLU A 1 480 ? 143.152 121.741 88.554  1.00 34.75 ?  480 GLU A N     1 
ATOM   3837  C  CA    . GLU A 1 480 ? 144.553 121.470 88.838  1.00 30.47 ?  480 GLU A CA    1 
ATOM   3838  C  C     . GLU A 1 480 ? 145.465 121.708 87.645  1.00 32.31 ?  480 GLU A C     1 
ATOM   3839  O  O     . GLU A 1 480 ? 146.689 121.675 87.811  1.00 38.83 ?  480 GLU A O     1 
ATOM   3840  C  CB    . GLU A 1 480 ? 144.726 120.024 89.302  1.00 35.32 ?  480 GLU A CB    1 
ATOM   3841  C  CG    . GLU A 1 480 ? 143.921 119.645 90.519  1.00 33.17 ?  480 GLU A CG    1 
ATOM   3842  C  CD    . GLU A 1 480 ? 143.608 118.166 90.544  1.00 41.41 ?  480 GLU A CD    1 
ATOM   3843  O  OE1   . GLU A 1 480 ? 142.586 117.764 89.949  1.00 41.14 ?  480 GLU A OE1   1 
ATOM   3844  O  OE2   . GLU A 1 480 ? 144.385 117.401 91.152  1.00 42.62 -1 480 GLU A OE2   1 
ATOM   3845  N  N     . SER A 1 481 ? 144.911 121.936 86.461  1.00 33.54 ?  481 SER A N     1 
ATOM   3846  C  CA    . SER A 1 481 ? 145.727 122.053 85.266  1.00 32.41 ?  481 SER A CA    1 
ATOM   3847  C  C     . SER A 1 481 ? 146.559 123.335 85.299  1.00 34.48 ?  481 SER A C     1 
ATOM   3848  O  O     . SER A 1 481 ? 146.163 124.329 85.911  1.00 37.49 ?  481 SER A O     1 
ATOM   3849  C  CB    . SER A 1 481 ? 144.849 122.035 84.020  1.00 32.23 ?  481 SER A CB    1 
ATOM   3850  O  OG    . SER A 1 481 ? 144.305 123.316 83.762  1.00 36.70 ?  481 SER A OG    1 
ATOM   3851  N  N     . PRO A 1 482 ? 147.731 123.327 84.659  1.00 39.26 ?  482 PRO A N     1 
ATOM   3852  C  CA    . PRO A 1 482 ? 148.512 124.570 84.555  1.00 35.92 ?  482 PRO A CA    1 
ATOM   3853  C  C     . PRO A 1 482 ? 147.788 125.675 83.808  1.00 35.70 ?  482 PRO A C     1 
ATOM   3854  O  O     . PRO A 1 482 ? 148.048 126.856 84.066  1.00 39.30 ?  482 PRO A O     1 
ATOM   3855  C  CB    . PRO A 1 482 ? 149.781 124.124 83.814  1.00 35.33 ?  482 PRO A CB    1 
ATOM   3856  C  CG    . PRO A 1 482 ? 149.863 122.656 84.043  1.00 36.84 ?  482 PRO A CG    1 
ATOM   3857  C  CD    . PRO A 1 482 ? 148.450 122.173 84.096  1.00 40.09 ?  482 PRO A CD    1 
ATOM   3858  N  N     . GLU A 1 483 ? 146.893 125.326 82.881  1.00 37.21 ?  483 GLU A N     1 
ATOM   3859  C  CA    . GLU A 1 483 ? 146.128 126.343 82.166  1.00 36.11 ?  483 GLU A CA    1 
ATOM   3860  C  C     . GLU A 1 483 ? 145.201 127.100 83.109  1.00 33.32 ?  483 GLU A C     1 
ATOM   3861  O  O     . GLU A 1 483 ? 144.993 128.308 82.948  1.00 36.83 ?  483 GLU A O     1 
ATOM   3862  C  CB    . GLU A 1 483 ? 145.332 125.698 81.032  1.00 38.31 ?  483 GLU A CB    1 
ATOM   3863  C  CG    . GLU A 1 483 ? 146.191 125.185 79.892  1.00 40.47 ?  483 GLU A CG    1 
ATOM   3864  C  CD    . GLU A 1 483 ? 146.613 123.743 80.089  1.00 43.75 ?  483 GLU A CD    1 
ATOM   3865  O  OE1   . GLU A 1 483 ? 146.335 123.185 81.170  1.00 41.03 ?  483 GLU A OE1   1 
ATOM   3866  O  OE2   . GLU A 1 483 ? 147.228 123.168 79.168  1.00 43.14 -1 483 GLU A OE2   1 
ATOM   3867  N  N     . ALA A 1 484 ? 144.632 126.405 84.095  1.00 27.96 ?  484 ALA A N     1 
ATOM   3868  C  CA    . ALA A 1 484 ? 143.793 127.074 85.082  1.00 28.48 ?  484 ALA A CA    1 
ATOM   3869  C  C     . ALA A 1 484 ? 144.591 128.088 85.888  1.00 29.73 ?  484 ALA A C     1 
ATOM   3870  O  O     . ALA A 1 484 ? 144.126 129.207 86.130  1.00 31.79 ?  484 ALA A O     1 
ATOM   3871  C  CB    . ALA A 1 484 ? 143.149 126.046 86.008  1.00 27.81 ?  484 ALA A CB    1 
ATOM   3872  N  N     . ARG A 1 485 ? 145.798 127.711 86.315  1.00 30.89 ?  485 ARG A N     1 
ATOM   3873  C  CA    . ARG A 1 485 ? 146.645 128.645 87.046  1.00 24.15 ?  485 ARG A CA    1 
ATOM   3874  C  C     . ARG A 1 485 ? 147.100 129.797 86.163  1.00 25.15 ?  485 ARG A C     1 
ATOM   3875  O  O     . ARG A 1 485 ? 147.238 130.923 86.644  1.00 35.58 ?  485 ARG A O     1 
ATOM   3876  C  CB    . ARG A 1 485 ? 147.848 127.913 87.637  1.00 27.04 ?  485 ARG A CB    1 
ATOM   3877  C  CG    . ARG A 1 485 ? 147.497 127.023 88.812  1.00 26.39 ?  485 ARG A CG    1 
ATOM   3878  C  CD    . ARG A 1 485 ? 148.741 126.494 89.494  1.00 28.57 ?  485 ARG A CD    1 
ATOM   3879  N  NE    . ARG A 1 485 ? 149.552 125.681 88.597  1.00 31.77 ?  485 ARG A NE    1 
ATOM   3880  C  CZ    . ARG A 1 485 ? 149.336 124.398 88.348  1.00 32.64 ?  485 ARG A CZ    1 
ATOM   3881  N  NH1   . ARG A 1 485 ? 148.334 123.743 88.912  1.00 30.58 1  485 ARG A NH1   1 
ATOM   3882  N  NH2   . ARG A 1 485 ? 150.147 123.754 87.514  1.00 29.50 ?  485 ARG A NH2   1 
ATOM   3883  N  N     . ASP A 1 486 ? 147.329 129.538 84.876  1.00 30.78 ?  486 ASP A N     1 
ATOM   3884  C  CA    . ASP A 1 486 ? 147.660 130.611 83.942  1.00 29.20 ?  486 ASP A CA    1 
ATOM   3885  C  C     . ASP A 1 486 ? 146.513 131.608 83.824  1.00 29.58 ?  486 ASP A C     1 
ATOM   3886  O  O     . ASP A 1 486 ? 146.723 132.831 83.857  1.00 36.63 ?  486 ASP A O     1 
ATOM   3887  C  CB    . ASP A 1 486 ? 148.002 130.008 82.580  1.00 33.34 ?  486 ASP A CB    1 
ATOM   3888  C  CG    . ASP A 1 486 ? 148.516 131.032 81.600  1.00 40.71 ?  486 ASP A CG    1 
ATOM   3889  O  OD1   . ASP A 1 486 ? 149.478 131.753 81.936  1.00 42.51 ?  486 ASP A OD1   1 
ATOM   3890  O  OD2   . ASP A 1 486 ? 147.959 131.110 80.487  1.00 39.27 -1 486 ASP A OD2   1 
ATOM   3891  N  N     . PHE A 1 487 ? 145.285 131.099 83.696  1.00 30.32 ?  487 PHE A N     1 
ATOM   3892  C  CA    . PHE A 1 487 ? 144.131 131.985 83.643  1.00 25.86 ?  487 PHE A CA    1 
ATOM   3893  C  C     . PHE A 1 487 ? 143.985 132.773 84.932  1.00 25.25 ?  487 PHE A C     1 
ATOM   3894  O  O     . PHE A 1 487 ? 143.692 133.970 84.901  1.00 31.24 ?  487 PHE A O     1 
ATOM   3895  C  CB    . PHE A 1 487 ? 142.844 131.212 83.373  1.00 26.95 ?  487 PHE A CB    1 
ATOM   3896  C  CG    . PHE A 1 487 ? 141.610 131.987 83.739  1.00 29.75 ?  487 PHE A CG    1 
ATOM   3897  C  CD1   . PHE A 1 487 ? 141.163 133.015 82.928  1.00 26.34 ?  487 PHE A CD1   1 
ATOM   3898  C  CD2   . PHE A 1 487 ? 140.922 131.719 84.911  1.00 26.22 ?  487 PHE A CD2   1 
ATOM   3899  C  CE1   . PHE A 1 487 ? 140.048 133.747 83.265  1.00 26.84 ?  487 PHE A CE1   1 
ATOM   3900  C  CE2   . PHE A 1 487 ? 139.804 132.451 85.252  1.00 25.28 ?  487 PHE A CE2   1 
ATOM   3901  C  CZ    . PHE A 1 487 ? 139.368 133.466 84.427  1.00 28.34 ?  487 PHE A CZ    1 
ATOM   3902  N  N     . ALA A 1 488 ? 144.145 132.109 86.078  1.00 25.81 ?  488 ALA A N     1 
ATOM   3903  C  CA    . ALA A 1 488 ? 144.024 132.807 87.352  1.00 20.51 ?  488 ALA A CA    1 
ATOM   3904  C  C     . ALA A 1 488 ? 145.081 133.895 87.476  1.00 27.80 ?  488 ALA A C     1 
ATOM   3905  O  O     . ALA A 1 488 ? 144.788 135.009 87.924  1.00 34.78 ?  488 ALA A O     1 
ATOM   3906  C  CB    . ALA A 1 488 ? 144.131 131.814 88.506  1.00 18.44 ?  488 ALA A CB    1 
ATOM   3907  N  N     . ASN A 1 489 ? 146.313 133.596 87.059  1.00 28.19 ?  489 ASN A N     1 
ATOM   3908  C  CA    . ASN A 1 489 ? 147.378 134.587 87.077  1.00 20.94 ?  489 ASN A CA    1 
ATOM   3909  C  C     . ASN A 1 489 ? 146.995 135.815 86.264  1.00 20.93 ?  489 ASN A C     1 
ATOM   3910  O  O     . ASN A 1 489 ? 147.026 136.941 86.770  1.00 30.25 ?  489 ASN A O     1 
ATOM   3911  C  CB    . ASN A 1 489 ? 148.666 133.963 86.539  1.00 22.28 ?  489 ASN A CB    1 
ATOM   3912  C  CG    . ASN A 1 489 ? 149.905 134.711 86.972  1.00 30.45 ?  489 ASN A CG    1 
ATOM   3913  O  OD1   . ASN A 1 489 ? 150.047 135.080 88.135  1.00 36.75 ?  489 ASN A OD1   1 
ATOM   3914  N  ND2   . ASN A 1 489 ? 150.819 134.928 86.035  1.00 28.71 ?  489 ASN A ND2   1 
ATOM   3915  N  N     . THR A 1 490 ? 146.599 135.611 85.004  1.00 26.43 ?  490 THR A N     1 
ATOM   3916  C  CA    . THR A 1 490 ? 146.266 136.752 84.155  1.00 24.41 ?  490 THR A CA    1 
ATOM   3917  C  C     . THR A 1 490 ? 145.052 137.508 84.684  1.00 26.18 ?  490 THR A C     1 
ATOM   3918  O  O     . THR A 1 490 ? 145.061 138.744 84.757  1.00 27.97 ?  490 THR A O     1 
ATOM   3919  C  CB    . THR A 1 490 ? 146.022 136.289 82.720  1.00 26.36 ?  490 THR A CB    1 
ATOM   3920  O  OG1   . THR A 1 490 ? 147.145 135.523 82.272  1.00 31.50 ?  490 THR A OG1   1 
ATOM   3921  C  CG2   . THR A 1 490 ? 145.832 137.486 81.801  1.00 25.93 ?  490 THR A CG2   1 
ATOM   3922  N  N     . PHE A 1 491 ? 144.004 136.781 85.073  1.00 21.58 ?  491 PHE A N     1 
ATOM   3923  C  CA    . PHE A 1 491 ? 142.764 137.406 85.512  1.00 18.72 ?  491 PHE A CA    1 
ATOM   3924  C  C     . PHE A 1 491 ? 142.984 138.245 86.762  1.00 25.92 ?  491 PHE A C     1 
ATOM   3925  O  O     . PHE A 1 491 ? 142.542 139.396 86.836  1.00 28.50 ?  491 PHE A O     1 
ATOM   3926  C  CB    . PHE A 1 491 ? 141.705 136.333 85.768  1.00 24.90 ?  491 PHE A CB    1 
ATOM   3927  C  CG    . PHE A 1 491 ? 140.411 136.871 86.304  1.00 22.44 ?  491 PHE A CG    1 
ATOM   3928  C  CD1   . PHE A 1 491 ? 139.436 137.341 85.444  1.00 18.33 ?  491 PHE A CD1   1 
ATOM   3929  C  CD2   . PHE A 1 491 ? 140.170 136.910 87.667  1.00 18.60 ?  491 PHE A CD2   1 
ATOM   3930  C  CE1   . PHE A 1 491 ? 138.248 137.840 85.930  1.00 15.30 ?  491 PHE A CE1   1 
ATOM   3931  C  CE2   . PHE A 1 491 ? 138.987 137.412 88.157  1.00 18.33 ?  491 PHE A CE2   1 
ATOM   3932  C  CZ    . PHE A 1 491 ? 138.023 137.876 87.287  1.00 19.82 ?  491 PHE A CZ    1 
ATOM   3933  N  N     . PHE A 1 492 ? 143.671 137.687 87.757  1.00 20.75 ?  492 PHE A N     1 
ATOM   3934  C  CA    . PHE A 1 492 ? 143.851 138.417 88.999  1.00 13.53 ?  492 PHE A CA    1 
ATOM   3935  C  C     . PHE A 1 492 ? 144.932 139.481 88.899  1.00 12.28 ?  492 PHE A C     1 
ATOM   3936  O  O     . PHE A 1 492 ? 144.855 140.476 89.622  1.00 22.08 ?  492 PHE A O     1 
ATOM   3937  C  CB    . PHE A 1 492 ? 144.130 137.438 90.137  1.00 20.06 ?  492 PHE A CB    1 
ATOM   3938  C  CG    . PHE A 1 492 ? 142.911 136.687 90.578  1.00 16.34 ?  492 PHE A CG    1 
ATOM   3939  C  CD1   . PHE A 1 492 ? 141.965 137.293 91.385  1.00 15.80 ?  492 PHE A CD1   1 
ATOM   3940  C  CD2   . PHE A 1 492 ? 142.686 135.391 90.150  1.00 21.73 ?  492 PHE A CD2   1 
ATOM   3941  C  CE1   . PHE A 1 492 ? 140.834 136.611 91.779  1.00 14.75 ?  492 PHE A CE1   1 
ATOM   3942  C  CE2   . PHE A 1 492 ? 141.556 134.705 90.540  1.00 16.11 ?  492 PHE A CE2   1 
ATOM   3943  C  CZ    . PHE A 1 492 ? 140.631 135.314 91.355  1.00 15.69 ?  492 PHE A CZ    1 
ATOM   3944  N  N     . MET A 1 493 ? 145.901 139.337 87.991  1.00 13.10 ?  493 MET A N     1 
ATOM   3945  C  CA    . MET A 1 493 ? 146.784 140.460 87.706  1.00 22.63 ?  493 MET A CA    1 
ATOM   3946  C  C     . MET A 1 493 ? 145.995 141.615 87.109  1.00 18.41 ?  493 MET A C     1 
ATOM   3947  O  O     . MET A 1 493 ? 146.218 142.776 87.464  1.00 28.96 ?  493 MET A O     1 
ATOM   3948  C  CB    . MET A 1 493 ? 147.917 140.024 86.773  1.00 25.38 ?  493 MET A CB    1 
ATOM   3949  C  CG    . MET A 1 493 ? 148.701 141.158 86.096  1.00 20.10 ?  493 MET A CG    1 
ATOM   3950  S  SD    . MET A 1 493 ? 147.952 141.905 84.634  1.00 34.53 ?  493 MET A SD    1 
ATOM   3951  C  CE    . MET A 1 493 ? 147.926 140.507 83.522  1.00 28.29 ?  493 MET A CE    1 
ATOM   3952  N  N     . MET A 1 494 ? 145.063 141.314 86.201  1.00 22.19 ?  494 MET A N     1 
ATOM   3953  C  CA    . MET A 1 494 ? 144.251 142.371 85.608  1.00 17.81 ?  494 MET A CA    1 
ATOM   3954  C  C     . MET A 1 494 ? 143.345 143.016 86.650  1.00 19.45 ?  494 MET A C     1 
ATOM   3955  O  O     . MET A 1 494 ? 143.163 144.241 86.659  1.00 32.12 ?  494 MET A O     1 
ATOM   3956  C  CB    . MET A 1 494 ? 143.427 141.807 84.450  1.00 24.00 ?  494 MET A CB    1 
ATOM   3957  C  CG    . MET A 1 494 ? 144.165 141.827 83.128  1.00 23.09 ?  494 MET A CG    1 
ATOM   3958  S  SD    . MET A 1 494 ? 143.387 140.891 81.803  1.00 41.86 ?  494 MET A SD    1 
ATOM   3959  C  CE    . MET A 1 494 ? 141.937 141.893 81.504  1.00 27.84 ?  494 MET A CE    1 
ATOM   3960  N  N     . VAL A 1 495 ? 142.767 142.200 87.534  1.00 22.31 ?  495 VAL A N     1 
ATOM   3961  C  CA    . VAL A 1 495 ? 141.934 142.726 88.609  1.00 13.04 ?  495 VAL A CA    1 
ATOM   3962  C  C     . VAL A 1 495 ? 142.749 143.636 89.518  1.00 19.56 ?  495 VAL A C     1 
ATOM   3963  O  O     . VAL A 1 495 ? 142.294 144.716 89.904  1.00 26.90 ?  495 VAL A O     1 
ATOM   3964  C  CB    . VAL A 1 495 ? 141.286 141.571 89.396  1.00 15.82 ?  495 VAL A CB    1 
ATOM   3965  C  CG1   . VAL A 1 495 ? 140.687 142.076 90.698  1.00 11.99 ?  495 VAL A CG1   1 
ATOM   3966  C  CG2   . VAL A 1 495 ? 140.230 140.886 88.553  1.00 18.51 ?  495 VAL A CG2   1 
ATOM   3967  N  N     . ASN A 1 496 ? 143.967 143.214 89.872  1.00 23.48 ?  496 ASN A N     1 
ATOM   3968  C  CA    . ASN A 1 496 ? 144.837 144.056 90.686  1.00 15.17 ?  496 ASN A CA    1 
ATOM   3969  C  C     . ASN A 1 496 ? 145.179 145.353 89.968  1.00 17.85 ?  496 ASN A C     1 
ATOM   3970  O  O     . ASN A 1 496 ? 145.165 146.429 90.575  1.00 23.80 ?  496 ASN A O     1 
ATOM   3971  C  CB    . ASN A 1 496 ? 146.110 143.292 91.048  1.00 19.22 ?  496 ASN A CB    1 
ATOM   3972  C  CG    . ASN A 1 496 ? 146.839 143.898 92.226  1.00 18.58 ?  496 ASN A CG    1 
ATOM   3973  O  OD1   . ASN A 1 496 ? 146.219 144.412 93.153  1.00 25.12 ?  496 ASN A OD1   1 
ATOM   3974  N  ND2   . ASN A 1 496 ? 148.163 143.841 92.195  1.00 18.92 ?  496 ASN A ND2   1 
ATOM   3975  N  N     . PHE A 1 497 ? 145.484 145.271 88.671  1.00 21.05 ?  497 PHE A N     1 
ATOM   3976  C  CA    . PHE A 1 497 ? 145.814 146.461 87.897  1.00 15.64 ?  497 PHE A CA    1 
ATOM   3977  C  C     . PHE A 1 497 ? 144.672 147.463 87.924  1.00 24.19 ?  497 PHE A C     1 
ATOM   3978  O  O     . PHE A 1 497 ? 144.874 148.649 88.205  1.00 28.93 ?  497 PHE A O     1 
ATOM   3979  C  CB    . PHE A 1 497 ? 146.142 146.068 86.456  1.00 17.27 ?  497 PHE A CB    1 
ATOM   3980  C  CG    . PHE A 1 497 ? 146.500 147.230 85.574  1.00 19.90 ?  497 PHE A CG    1 
ATOM   3981  C  CD1   . PHE A 1 497 ? 147.808 147.669 85.483  1.00 23.61 ?  497 PHE A CD1   1 
ATOM   3982  C  CD2   . PHE A 1 497 ? 145.528 147.880 84.833  1.00 21.10 ?  497 PHE A CD2   1 
ATOM   3983  C  CE1   . PHE A 1 497 ? 148.138 148.736 84.672  1.00 24.21 ?  497 PHE A CE1   1 
ATOM   3984  C  CE2   . PHE A 1 497 ? 145.854 148.947 84.023  1.00 22.95 ?  497 PHE A CE2   1 
ATOM   3985  C  CZ    . PHE A 1 497 ? 147.159 149.374 83.942  1.00 24.69 ?  497 PHE A CZ    1 
ATOM   3986  N  N     . TYR A 1 498 ? 143.455 146.997 87.654  1.00 26.98 ?  498 TYR A N     1 
ATOM   3987  C  CA    . TYR A 1 498 ? 142.334 147.921 87.574  1.00 18.45 ?  498 TYR A CA    1 
ATOM   3988  C  C     . TYR A 1 498 ? 141.874 148.391 88.948  1.00 22.85 ?  498 TYR A C     1 
ATOM   3989  O  O     . TYR A 1 498 ? 141.392 149.518 89.073  1.00 25.76 ?  498 TYR A O     1 
ATOM   3990  C  CB    . TYR A 1 498 ? 141.193 147.286 86.784  1.00 19.95 ?  498 TYR A CB    1 
ATOM   3991  C  CG    . TYR A 1 498 ? 141.519 147.194 85.314  1.00 24.72 ?  498 TYR A CG    1 
ATOM   3992  C  CD1   . TYR A 1 498 ? 141.794 148.337 84.578  1.00 24.50 ?  498 TYR A CD1   1 
ATOM   3993  C  CD2   . TYR A 1 498 ? 141.577 145.969 84.667  1.00 26.25 ?  498 TYR A CD2   1 
ATOM   3994  C  CE1   . TYR A 1 498 ? 142.105 148.265 83.239  1.00 25.80 ?  498 TYR A CE1   1 
ATOM   3995  C  CE2   . TYR A 1 498 ? 141.885 145.887 83.327  1.00 24.86 ?  498 TYR A CE2   1 
ATOM   3996  C  CZ    . TYR A 1 498 ? 142.148 147.039 82.617  1.00 30.37 ?  498 TYR A CZ    1 
ATOM   3997  O  OH    . TYR A 1 498 ? 142.457 146.967 81.279  1.00 32.57 ?  498 TYR A OH    1 
ATOM   3998  N  N     . SER A 1 499 ? 142.052 147.580 89.993  1.00 23.88 ?  499 SER A N     1 
ATOM   3999  C  CA    . SER A 1 499 ? 141.747 148.051 91.339  1.00 15.88 ?  499 SER A CA    1 
ATOM   4000  C  C     . SER A 1 499 ? 142.734 149.123 91.782  1.00 19.19 ?  499 SER A C     1 
ATOM   4001  O  O     . SER A 1 499 ? 142.339 150.120 92.395  1.00 30.15 ?  499 SER A O     1 
ATOM   4002  C  CB    . SER A 1 499 ? 141.740 146.882 92.322  1.00 15.23 ?  499 SER A CB    1 
ATOM   4003  O  OG    . SER A 1 499 ? 143.049 146.400 92.564  1.00 23.12 ?  499 SER A OG    1 
ATOM   4004  N  N     . ILE A 1 500 ? 144.021 148.943 91.472  1.00 17.80 ?  500 ILE A N     1 
ATOM   4005  C  CA    . ILE A 1 500 ? 145.011 149.971 91.782  1.00 19.65 ?  500 ILE A CA    1 
ATOM   4006  C  C     . ILE A 1 500 ? 144.726 151.235 90.984  1.00 18.17 ?  500 ILE A C     1 
ATOM   4007  O  O     . ILE A 1 500 ? 144.831 152.352 91.504  1.00 28.08 ?  500 ILE A O     1 
ATOM   4008  C  CB    . ILE A 1 500 ? 146.433 149.441 91.521  1.00 22.99 ?  500 ILE A CB    1 
ATOM   4009  C  CG1   . ILE A 1 500 ? 146.794 148.353 92.527  1.00 19.08 ?  500 ILE A CG1   1 
ATOM   4010  C  CG2   . ILE A 1 500 ? 147.446 150.562 91.604  1.00 20.01 ?  500 ILE A CG2   1 
ATOM   4011  C  CD1   . ILE A 1 500 ? 147.963 147.516 92.104  1.00 19.14 ?  500 ILE A CD1   1 
ATOM   4012  N  N     . GLN A 1 501 ? 144.357 151.080 89.711  1.00 24.23 ?  501 GLN A N     1 
ATOM   4013  C  CA    . GLN A 1 501 ? 144.024 152.237 88.887  1.00 22.16 ?  501 GLN A CA    1 
ATOM   4014  C  C     . GLN A 1 501 ? 142.820 152.986 89.442  1.00 28.31 ?  501 GLN A C     1 
ATOM   4015  O  O     . GLN A 1 501 ? 142.826 154.219 89.508  1.00 35.38 ?  501 GLN A O     1 
ATOM   4016  C  CB    . GLN A 1 501 ? 143.762 151.794 87.449  1.00 24.46 ?  501 GLN A CB    1 
ATOM   4017  C  CG    . GLN A 1 501 ? 144.244 152.777 86.405  1.00 25.08 ?  501 GLN A CG    1 
ATOM   4018  C  CD    . GLN A 1 501 ? 143.960 152.310 84.996  1.00 29.25 ?  501 GLN A CD    1 
ATOM   4019  O  OE1   . GLN A 1 501 ? 142.807 152.109 84.617  1.00 28.56 ?  501 GLN A OE1   1 
ATOM   4020  N  NE2   . GLN A 1 501 ? 145.012 152.130 84.210  1.00 33.56 ?  501 GLN A NE2   1 
ATOM   4021  N  N     . ARG A 1 502 ? 141.777 152.260 89.848  1.00 29.65 ?  502 ARG A N     1 
ATOM   4022  C  CA    . ARG A 1 502 ? 140.601 152.911 90.411  1.00 20.32 ?  502 ARG A CA    1 
ATOM   4023  C  C     . ARG A 1 502 ? 140.921 153.583 91.739  1.00 18.03 ?  502 ARG A C     1 
ATOM   4024  O  O     . ARG A 1 502 ? 140.422 154.676 92.019  1.00 30.49 ?  502 ARG A O     1 
ATOM   4025  C  CB    . ARG A 1 502 ? 139.467 151.901 90.577  1.00 24.31 ?  502 ARG A CB    1 
ATOM   4026  C  CG    . ARG A 1 502 ? 138.114 152.540 90.824  1.00 26.79 ?  502 ARG A CG    1 
ATOM   4027  C  CD    . ARG A 1 502 ? 137.819 153.626 89.809  1.00 27.43 ?  502 ARG A CD    1 
ATOM   4028  N  NE    . ARG A 1 502 ? 136.716 154.477 90.238  1.00 25.88 ?  502 ARG A NE    1 
ATOM   4029  C  CZ    . ARG A 1 502 ? 136.657 155.785 90.038  1.00 28.77 ?  502 ARG A CZ    1 
ATOM   4030  N  NH1   . ARG A 1 502 ? 137.624 156.431 89.408  1.00 32.34 1  502 ARG A NH1   1 
ATOM   4031  N  NH2   . ARG A 1 502 ? 135.604 156.463 90.483  1.00 30.22 ?  502 ARG A NH2   1 
ATOM   4032  N  N     . SER A 1 503 ? 141.744 152.946 92.574  1.00 18.39 ?  503 SER A N     1 
ATOM   4033  C  CA    . SER A 1 503 ? 142.132 153.562 93.839  1.00 23.96 ?  503 SER A CA    1 
ATOM   4034  C  C     . SER A 1 503 ? 142.915 154.847 93.605  1.00 24.98 ?  503 SER A C     1 
ATOM   4035  O  O     . SER A 1 503 ? 142.685 155.857 94.279  1.00 27.44 ?  503 SER A O     1 
ATOM   4036  C  CB    . SER A 1 503 ? 142.950 152.572 94.668  1.00 18.45 ?  503 SER A CB    1 
ATOM   4037  O  OG    . SER A 1 503 ? 142.895 152.890 96.045  1.00 22.93 ?  503 SER A OG    1 
ATOM   4038  N  N     . ALA A 1 504 ? 143.835 154.831 92.637  1.00 27.15 ?  504 ALA A N     1 
ATOM   4039  C  CA    . ALA A 1 504 ? 144.598 156.032 92.315  1.00 25.35 ?  504 ALA A CA    1 
ATOM   4040  C  C     . ALA A 1 504 ? 143.702 157.123 91.741  1.00 30.07 ?  504 ALA A C     1 
ATOM   4041  O  O     . ALA A 1 504 ? 143.878 158.305 92.054  1.00 37.59 ?  504 ALA A O     1 
ATOM   4042  C  CB    . ALA A 1 504 ? 145.723 155.688 91.342  1.00 27.51 ?  504 ALA A CB    1 
ATOM   4043  N  N     . GLU A 1 505 ? 142.736 156.749 90.900  1.00 28.85 ?  505 GLU A N     1 
ATOM   4044  C  CA    . GLU A 1 505 ? 141.810 157.731 90.349  1.00 28.97 ?  505 GLU A CA    1 
ATOM   4045  C  C     . GLU A 1 505 ? 140.928 158.336 91.436  1.00 30.69 ?  505 GLU A C     1 
ATOM   4046  O  O     . GLU A 1 505 ? 140.648 159.538 91.415  1.00 35.21 ?  505 GLU A O     1 
ATOM   4047  C  CB    . GLU A 1 505 ? 140.954 157.090 89.259  1.00 29.45 ?  505 GLU A CB    1 
ATOM   4048  C  CG    . GLU A 1 505 ? 141.709 156.798 87.975  1.00 32.55 ?  505 GLU A CG    1 
ATOM   4049  C  CD    . GLU A 1 505 ? 141.079 155.679 87.170  1.00 35.89 ?  505 GLU A CD    1 
ATOM   4050  O  OE1   . GLU A 1 505 ? 140.016 155.172 87.581  1.00 36.53 ?  505 GLU A OE1   1 
ATOM   4051  O  OE2   . GLU A 1 505 ? 141.648 155.309 86.122  1.00 39.44 -1 505 GLU A OE2   1 
ATOM   4052  N  N     . ILE A 1 506 ? 140.478 157.517 92.387  1.00 28.29 ?  506 ILE A N     1 
ATOM   4053  C  CA    . ILE A 1 506 ? 139.685 158.031 93.500  1.00 25.45 ?  506 ILE A CA    1 
ATOM   4054  C  C     . ILE A 1 506 ? 140.520 158.971 94.359  1.00 28.32 ?  506 ILE A C     1 
ATOM   4055  O  O     . ILE A 1 506 ? 140.040 160.021 94.798  1.00 37.79 ?  506 ILE A O     1 
ATOM   4056  C  CB    . ILE A 1 506 ? 139.107 156.867 94.325  1.00 25.65 ?  506 ILE A CB    1 
ATOM   4057  C  CG1   . ILE A 1 506 ? 138.047 156.117 93.519  1.00 28.37 ?  506 ILE A CG1   1 
ATOM   4058  C  CG2   . ILE A 1 506 ? 138.508 157.372 95.623  1.00 27.04 ?  506 ILE A CG2   1 
ATOM   4059  C  CD1   . ILE A 1 506 ? 137.677 154.777 94.106  1.00 22.37 ?  506 ILE A CD1   1 
ATOM   4060  N  N     . ALA A 1 507 ? 141.781 158.613 94.610  1.00 30.87 ?  507 ALA A N     1 
ATOM   4061  C  CA    . ALA A 1 507 ? 142.662 159.499 95.366  1.00 28.95 ?  507 ALA A CA    1 
ATOM   4062  C  C     . ALA A 1 507 ? 142.879 160.818 94.634  1.00 30.76 ?  507 ALA A C     1 
ATOM   4063  O  O     . ALA A 1 507 ? 142.909 161.884 95.258  1.00 33.56 ?  507 ALA A O     1 
ATOM   4064  C  CB    . ALA A 1 507 ? 143.997 158.804 95.635  1.00 25.37 ?  507 ALA A CB    1 
ATOM   4065  N  N     . LYS A 1 508 ? 143.043 160.764 93.311  1.00 36.54 ?  508 LYS A N     1 
ATOM   4066  C  CA    . LYS A 1 508 ? 143.210 161.984 92.528  1.00 33.53 ?  508 LYS A CA    1 
ATOM   4067  C  C     . LYS A 1 508 ? 141.955 162.849 92.564  1.00 38.04 ?  508 LYS A C     1 
ATOM   4068  O  O     . LYS A 1 508 ? 142.044 164.074 92.699  1.00 44.21 ?  508 LYS A O     1 
ATOM   4069  C  CB    . LYS A 1 508 ? 143.570 161.630 91.086  1.00 36.70 ?  508 LYS A CB    1 
ATOM   4070  C  CG    . LYS A 1 508 ? 143.555 162.813 90.134  1.00 40.47 ?  508 LYS A CG    1 
ATOM   4071  C  CD    . LYS A 1 508 ? 143.556 162.356 88.687  1.00 38.88 ?  508 LYS A CD    1 
ATOM   4072  C  CE    . LYS A 1 508 ? 143.801 163.520 87.743  1.00 39.18 ?  508 LYS A CE    1 
ATOM   4073  N  NZ    . LYS A 1 508 ? 144.623 163.120 86.572  1.00 42.23 1  508 LYS A NZ    1 
ATOM   4074  N  N     . GLU A 1 509 ? 140.781 162.230 92.443  1.00 36.02 ?  509 GLU A N     1 
ATOM   4075  C  CA    . GLU A 1 509 ? 139.535 162.990 92.419  1.00 36.32 ?  509 GLU A CA    1 
ATOM   4076  C  C     . GLU A 1 509 ? 139.246 163.616 93.777  1.00 39.00 ?  509 GLU A C     1 
ATOM   4077  O  O     . GLU A 1 509 ? 138.933 164.809 93.870  1.00 43.38 ?  509 GLU A O     1 
ATOM   4078  C  CB    . GLU A 1 509 ? 138.381 162.087 91.986  1.00 36.42 ?  509 GLU A CB    1 
ATOM   4079  C  CG    . GLU A 1 509 ? 138.374 161.754 90.503  1.00 42.34 ?  509 GLU A CG    1 
ATOM   4080  C  CD    . GLU A 1 509 ? 137.597 160.488 90.194  1.00 44.67 ?  509 GLU A CD    1 
ATOM   4081  O  OE1   . GLU A 1 509 ? 136.948 159.948 91.114  1.00 42.56 ?  509 GLU A OE1   1 
ATOM   4082  O  OE2   . GLU A 1 509 ? 137.633 160.036 89.030  1.00 42.61 -1 509 GLU A OE2   1 
ATOM   4083  N  N     . LYS A 1 510 ? 139.345 162.825 94.845  1.00 35.73 ?  510 LYS A N     1 
ATOM   4084  C  CA    . LYS A 1 510 ? 139.084 163.320 96.189  1.00 31.94 ?  510 LYS A CA    1 
ATOM   4085  C  C     . LYS A 1 510 ? 140.265 164.072 96.783  1.00 34.00 ?  510 LYS A C     1 
ATOM   4086  O  O     . LYS A 1 510 ? 140.118 164.677 97.850  1.00 39.30 ?  510 LYS A O     1 
ATOM   4087  C  CB    . LYS A 1 510 ? 138.697 162.157 97.104  1.00 30.48 ?  510 LYS A CB    1 
ATOM   4088  C  CG    . LYS A 1 510 ? 137.589 161.289 96.539  1.00 33.39 ?  510 LYS A CG    1 
ATOM   4089  C  CD    . LYS A 1 510 ? 136.973 160.397 97.599  1.00 33.07 ?  510 LYS A CD    1 
ATOM   4090  C  CE    . LYS A 1 510 ? 135.849 159.564 97.010  1.00 35.82 ?  510 LYS A CE    1 
ATOM   4091  N  NZ    . LYS A 1 510 ? 134.798 159.250 98.009  1.00 34.70 1  510 LYS A NZ    1 
ATOM   4092  N  N     . GLY A 1 511 ? 141.423 164.047 96.128  1.00 37.13 ?  511 GLY A N     1 
ATOM   4093  C  CA    . GLY A 1 511 ? 142.581 164.766 96.615  1.00 37.04 ?  511 GLY A CA    1 
ATOM   4094  C  C     . GLY A 1 511 ? 143.175 164.237 97.897  1.00 40.69 ?  511 GLY A C     1 
ATOM   4095  O  O     . GLY A 1 511 ? 144.031 164.903 98.486  1.00 42.75 ?  511 GLY A O     1 
ATOM   4096  N  N     . GLU A 1 512 ? 142.752 163.060 98.353  1.00 34.12 ?  512 GLU A N     1 
ATOM   4097  C  CA    . GLU A 1 512 ? 143.249 162.484 99.591  1.00 29.43 ?  512 GLU A CA    1 
ATOM   4098  C  C     . GLU A 1 512 ? 143.583 161.014 99.385  1.00 29.65 ?  512 GLU A C     1 
ATOM   4099  O  O     . GLU A 1 512 ? 142.935 160.312 98.606  1.00 33.10 ?  512 GLU A O     1 
ATOM   4100  C  CB    . GLU A 1 512 ? 142.229 162.633 100.729 1.00 31.02 ?  512 GLU A CB    1 
ATOM   4101  C  CG    . GLU A 1 512 ? 140.887 161.979 100.459 1.00 31.59 ?  512 GLU A CG    1 
ATOM   4102  C  CD    . GLU A 1 512 ? 140.194 161.540 101.732 1.00 35.46 ?  512 GLU A CD    1 
ATOM   4103  O  OE1   . GLU A 1 512 ? 140.899 161.221 102.710 1.00 35.24 ?  512 GLU A OE1   1 
ATOM   4104  O  OE2   . GLU A 1 512 ? 138.945 161.515 101.754 1.00 34.76 -1 512 GLU A OE2   1 
ATOM   4105  N  N     . THR A 1 513 ? 144.611 160.563 100.090 1.00 29.89 ?  513 THR A N     1 
ATOM   4106  C  CA    . THR A 1 513 ? 145.027 159.170 100.124 1.00 25.22 ?  513 THR A CA    1 
ATOM   4107  C  C     . THR A 1 513 ? 144.691 158.583 101.491 1.00 27.22 ?  513 THR A C     1 
ATOM   4108  O  O     . THR A 1 513 ? 144.210 159.277 102.390 1.00 36.88 ?  513 THR A O     1 
ATOM   4109  C  CB    . THR A 1 513 ? 146.522 159.048 99.822  1.00 24.19 ?  513 THR A CB    1 
ATOM   4110  O  OG1   . THR A 1 513 ? 147.267 159.793 100.791 1.00 28.55 ?  513 THR A OG1   1 
ATOM   4111  C  CG2   . THR A 1 513 ? 146.830 159.586 98.438  1.00 23.90 ?  513 THR A CG2   1 
ATOM   4112  N  N     . PHE A 1 514 ? 144.945 157.287 101.649 1.00 23.27 ?  514 PHE A N     1 
ATOM   4113  C  CA    . PHE A 1 514 ? 144.743 156.684 102.954 1.00 25.13 ?  514 PHE A CA    1 
ATOM   4114  C  C     . PHE A 1 514 ? 145.853 157.115 103.907 1.00 25.64 ?  514 PHE A C     1 
ATOM   4115  O  O     . PHE A 1 514 ? 146.951 157.495 103.492 1.00 28.15 ?  514 PHE A O     1 
ATOM   4116  C  CB    . PHE A 1 514 ? 144.661 155.158 102.851 1.00 18.28 ?  514 PHE A CB    1 
ATOM   4117  C  CG    . PHE A 1 514 ? 145.948 154.490 102.456 1.00 19.11 ?  514 PHE A CG    1 
ATOM   4118  C  CD1   . PHE A 1 514 ? 146.258 154.289 101.124 1.00 17.86 ?  514 PHE A CD1   1 
ATOM   4119  C  CD2   . PHE A 1 514 ? 146.831 154.031 103.419 1.00 22.51 ?  514 PHE A CD2   1 
ATOM   4120  C  CE1   . PHE A 1 514 ? 147.431 153.661 100.761 1.00 18.86 ?  514 PHE A CE1   1 
ATOM   4121  C  CE2   . PHE A 1 514 ? 148.003 153.404 103.060 1.00 17.63 ?  514 PHE A CE2   1 
ATOM   4122  C  CZ    . PHE A 1 514 ? 148.304 153.220 101.730 1.00 18.53 ?  514 PHE A CZ    1 
ATOM   4123  N  N     . ASP A 1 515 ? 145.544 157.075 105.200 1.00 29.13 ?  515 ASP A N     1 
ATOM   4124  C  CA    . ASP A 1 515 ? 146.472 157.574 106.207 1.00 27.15 ?  515 ASP A CA    1 
ATOM   4125  C  C     . ASP A 1 515 ? 147.783 156.801 106.167 1.00 29.36 ?  515 ASP A C     1 
ATOM   4126  O  O     . ASP A 1 515 ? 147.799 155.571 106.065 1.00 35.37 ?  515 ASP A O     1 
ATOM   4127  C  CB    . ASP A 1 515 ? 145.846 157.479 107.596 1.00 30.15 ?  515 ASP A CB    1 
ATOM   4128  C  CG    . ASP A 1 515 ? 144.938 158.652 107.905 1.00 38.05 ?  515 ASP A CG    1 
ATOM   4129  O  OD1   . ASP A 1 515 ? 144.447 159.294 106.953 1.00 36.62 ?  515 ASP A OD1   1 
ATOM   4130  O  OD2   . ASP A 1 515 ? 144.712 158.929 109.102 1.00 38.93 -1 515 ASP A OD2   1 
ATOM   4131  N  N     . GLN A 1 516 ? 148.889 157.542 106.254 1.00 27.50 ?  516 GLN A N     1 
ATOM   4132  C  CA    . GLN A 1 516 ? 150.237 156.980 106.175 1.00 28.05 ?  516 GLN A CA    1 
ATOM   4133  C  C     . GLN A 1 516 ? 150.460 156.251 104.852 1.00 25.00 ?  516 GLN A C     1 
ATOM   4134  O  O     . GLN A 1 516 ? 151.090 155.195 104.803 1.00 33.02 ?  516 GLN A O     1 
ATOM   4135  C  CB    . GLN A 1 516 ? 150.527 156.054 107.360 1.00 25.48 ?  516 GLN A CB    1 
ATOM   4136  C  CG    . GLN A 1 516 ? 150.363 156.708 108.719 1.00 27.14 ?  516 GLN A CG    1 
ATOM   4137  C  CD    . GLN A 1 516 ? 150.640 155.749 109.856 1.00 29.50 ?  516 GLN A CD    1 
ATOM   4138  O  OE1   . GLN A 1 516 ? 151.789 155.388 110.112 1.00 29.48 ?  516 GLN A OE1   1 
ATOM   4139  N  NE2   . GLN A 1 516 ? 149.589 155.332 110.548 1.00 28.58 ?  516 GLN A NE2   1 
ATOM   4140  N  N     . TYR A 1 517 ? 149.932 156.817 103.767 1.00 23.76 ?  517 TYR A N     1 
ATOM   4141  C  CA    . TYR A 1 517 ? 150.188 156.242 102.451 1.00 23.56 ?  517 TYR A CA    1 
ATOM   4142  C  C     . TYR A 1 517 ? 151.638 156.429 102.029 1.00 27.07 ?  517 TYR A C     1 
ATOM   4143  O  O     . TYR A 1 517 ? 152.205 155.552 101.368 1.00 34.91 ?  517 TYR A O     1 
ATOM   4144  C  CB    . TYR A 1 517 ? 149.260 156.854 101.400 1.00 24.34 ?  517 TYR A CB    1 
ATOM   4145  C  CG    . TYR A 1 517 ? 149.846 156.815 100.006 1.00 26.69 ?  517 TYR A CG    1 
ATOM   4146  C  CD1   . TYR A 1 517 ? 149.811 155.649 99.251  1.00 21.22 ?  517 TYR A CD1   1 
ATOM   4147  C  CD2   . TYR A 1 517 ? 150.449 157.935 99.451  1.00 25.97 ?  517 TYR A CD2   1 
ATOM   4148  C  CE1   . TYR A 1 517 ? 150.352 155.603 97.986  1.00 27.38 ?  517 TYR A CE1   1 
ATOM   4149  C  CE2   . TYR A 1 517 ? 150.996 157.896 98.189  1.00 25.76 ?  517 TYR A CE2   1 
ATOM   4150  C  CZ    . TYR A 1 517 ? 150.946 156.727 97.461  1.00 26.31 ?  517 TYR A CZ    1 
ATOM   4151  O  OH    . TYR A 1 517 ? 151.485 156.688 96.198  1.00 34.34 ?  517 TYR A OH    1 
ATOM   4152  N  N     . GLU A 1 518 ? 152.250 157.557 102.394 1.00 30.87 ?  518 GLU A N     1 
ATOM   4153  C  CA    . GLU A 1 518 ? 153.584 157.882 101.900 1.00 33.64 ?  518 GLU A CA    1 
ATOM   4154  C  C     . GLU A 1 518 ? 154.637 156.876 102.345 1.00 35.51 ?  518 GLU A C     1 
ATOM   4155  O  O     . GLU A 1 518 ? 155.668 156.741 101.679 1.00 38.35 ?  518 GLU A O     1 
ATOM   4156  C  CB    . GLU A 1 518 ? 153.980 159.289 102.350 1.00 34.11 ?  518 GLU A CB    1 
ATOM   4157  C  CG    . GLU A 1 518 ? 153.204 160.404 101.667 1.00 36.55 ?  518 GLU A CG    1 
ATOM   4158  C  CD    . GLU A 1 518 ? 153.464 160.481 100.172 1.00 43.50 ?  518 GLU A CD    1 
ATOM   4159  O  OE1   . GLU A 1 518 ? 154.528 160.009 99.720  1.00 39.21 ?  518 GLU A OE1   1 
ATOM   4160  O  OE2   . GLU A 1 518 ? 152.600 161.018 99.447  1.00 40.04 -1 518 GLU A OE2   1 
ATOM   4161  N  N     . GLY A 1 519 ? 154.408 156.174 103.453 1.00 24.41 ?  519 GLY A N     1 
ATOM   4162  C  CA    . GLY A 1 519 ? 155.307 155.121 103.875 1.00 20.56 ?  519 GLY A CA    1 
ATOM   4163  C  C     . GLY A 1 519 ? 155.048 153.765 103.268 1.00 21.97 ?  519 GLY A C     1 
ATOM   4164  O  O     . GLY A 1 519 ? 155.839 152.842 103.479 1.00 31.43 ?  519 GLY A O     1 
ATOM   4165  N  N     . SER A 1 520 ? 153.961 153.617 102.517 1.00 22.12 ?  520 SER A N     1 
ATOM   4166  C  CA    . SER A 1 520 ? 153.587 152.340 101.932 1.00 24.05 ?  520 SER A CA    1 
ATOM   4167  C  C     . SER A 1 520 ? 154.476 152.009 100.737 1.00 22.41 ?  520 SER A C     1 
ATOM   4168  O  O     . SER A 1 520 ? 155.202 152.855 100.210 1.00 27.98 ?  520 SER A O     1 
ATOM   4169  C  CB    . SER A 1 520 ? 152.119 152.357 101.512 1.00 20.05 ?  520 SER A CB    1 
ATOM   4170  O  OG    . SER A 1 520 ? 151.882 153.368 100.550 1.00 20.38 ?  520 SER A OG    1 
ATOM   4171  N  N     . THR A 1 521 ? 154.411 150.748 100.305 1.00 20.89 ?  521 THR A N     1 
ATOM   4172  C  CA    . THR A 1 521 ? 155.186 150.321 99.148  1.00 19.04 ?  521 THR A CA    1 
ATOM   4173  C  C     . THR A 1 521 ? 154.615 150.859 97.844  1.00 25.45 ?  521 THR A C     1 
ATOM   4174  O  O     . THR A 1 521 ? 155.332 150.900 96.839  1.00 28.88 ?  521 THR A O     1 
ATOM   4175  C  CB    . THR A 1 521 ? 155.257 148.797 99.086  1.00 28.33 ?  521 THR A CB    1 
ATOM   4176  O  OG1   . THR A 1 521 ? 153.932 148.257 99.112  1.00 29.39 ?  521 THR A OG1   1 
ATOM   4177  C  CG2   . THR A 1 521 ? 156.036 148.257 100.271 1.00 20.51 ?  521 THR A CG2   1 
ATOM   4178  N  N     . TYR A 1 522 ? 153.341 151.258 97.832  1.00 28.74 ?  522 TYR A N     1 
ATOM   4179  C  CA    . TYR A 1 522 ? 152.801 151.949 96.667  1.00 21.52 ?  522 TYR A CA    1 
ATOM   4180  C  C     . TYR A 1 522 ? 153.502 153.284 96.454  1.00 25.88 ?  522 TYR A C     1 
ATOM   4181  O  O     . TYR A 1 522 ? 153.840 153.644 95.321  1.00 29.89 ?  522 TYR A O     1 
ATOM   4182  C  CB    . TYR A 1 522 ? 151.296 152.166 96.823  1.00 18.60 ?  522 TYR A CB    1 
ATOM   4183  C  CG    . TYR A 1 522 ? 150.496 150.920 97.121  1.00 21.92 ?  522 TYR A CG    1 
ATOM   4184  C  CD1   . TYR A 1 522 ? 150.267 149.965 96.141  1.00 21.23 ?  522 TYR A CD1   1 
ATOM   4185  C  CD2   . TYR A 1 522 ? 149.944 150.714 98.378  1.00 23.68 ?  522 TYR A CD2   1 
ATOM   4186  C  CE1   . TYR A 1 522 ? 149.527 148.833 96.408  1.00 20.05 ?  522 TYR A CE1   1 
ATOM   4187  C  CE2   . TYR A 1 522 ? 149.200 149.586 98.652  1.00 22.90 ?  522 TYR A CE2   1 
ATOM   4188  C  CZ    . TYR A 1 522 ? 148.996 148.648 97.664  1.00 23.08 ?  522 TYR A CZ    1 
ATOM   4189  O  OH    . TYR A 1 522 ? 148.257 147.522 97.936  1.00 27.20 ?  522 TYR A OH    1 
ATOM   4190  N  N     . ALA A 1 523 ? 153.724 154.034 97.536  1.00 28.81 ?  523 ALA A N     1 
ATOM   4191  C  CA    . ALA A 1 523 ? 154.379 155.331 97.422  1.00 26.99 ?  523 ALA A CA    1 
ATOM   4192  C  C     . ALA A 1 523 ? 155.843 155.183 97.032  1.00 28.38 ?  523 ALA A C     1 
ATOM   4193  O  O     . ALA A 1 523 ? 156.352 155.946 96.204  1.00 32.27 ?  523 ALA A O     1 
ATOM   4194  C  CB    . ALA A 1 523 ? 154.248 156.100 98.735  1.00 23.69 ?  523 ALA A CB    1 
ATOM   4195  N  N     . THR A 1 524 ? 156.537 154.205 97.619  1.00 29.12 ?  524 THR A N     1 
ATOM   4196  C  CA    . THR A 1 524 ? 157.938 153.984 97.285  1.00 28.63 ?  524 THR A CA    1 
ATOM   4197  C  C     . THR A 1 524 ? 158.112 153.317 95.929  1.00 31.29 ?  524 THR A C     1 
ATOM   4198  O  O     . THR A 1 524 ? 159.214 153.355 95.373  1.00 36.00 ?  524 THR A O     1 
ATOM   4199  C  CB    . THR A 1 524 ? 158.609 153.137 98.367  1.00 30.58 ?  524 THR A CB    1 
ATOM   4200  O  OG1   . THR A 1 524 ? 158.137 151.788 98.282  1.00 32.71 ?  524 THR A OG1   1 
ATOM   4201  C  CG2   . THR A 1 524 ? 158.300 153.692 99.746  1.00 27.59 ?  524 THR A CG2   1 
ATOM   4202  N  N     . GLY A 1 525 ? 157.057 152.713 95.386  1.00 25.73 ?  525 GLY A N     1 
ATOM   4203  C  CA    . GLY A 1 525 ? 157.133 152.031 94.113  1.00 27.99 ?  525 GLY A CA    1 
ATOM   4204  C  C     . GLY A 1 525 ? 157.648 150.611 94.173  1.00 32.06 ?  525 GLY A C     1 
ATOM   4205  O  O     . GLY A 1 525 ? 157.720 149.954 93.127  1.00 31.32 ?  525 GLY A O     1 
ATOM   4206  N  N     . GLU A 1 526 ? 158.012 150.117 95.357  1.00 32.87 ?  526 GLU A N     1 
ATOM   4207  C  CA    . GLU A 1 526 ? 158.492 148.748 95.488  1.00 33.19 ?  526 GLU A CA    1 
ATOM   4208  C  C     . GLU A 1 526 ? 157.389 147.728 95.238  1.00 36.82 ?  526 GLU A C     1 
ATOM   4209  O  O     . GLU A 1 526 ? 157.680 146.607 94.805  1.00 40.66 ?  526 GLU A O     1 
ATOM   4210  C  CB    . GLU A 1 526 ? 159.116 148.558 96.875  1.00 33.10 ?  526 GLU A CB    1 
ATOM   4211  C  CG    . GLU A 1 526 ? 159.152 147.130 97.392  1.00 33.56 ?  526 GLU A CG    1 
ATOM   4212  C  CD    . GLU A 1 526 ? 159.194 147.062 98.904  1.00 40.85 ?  526 GLU A CD    1 
ATOM   4213  O  OE1   . GLU A 1 526 ? 159.207 148.131 99.548  1.00 44.68 ?  526 GLU A OE1   1 
ATOM   4214  O  OE2   . GLU A 1 526 ? 159.215 145.939 99.449  1.00 39.17 -1 526 GLU A OE2   1 
ATOM   4215  N  N     . TYR A 1 527 ? 156.129 148.104 95.473  1.00 34.23 ?  527 TYR A N     1 
ATOM   4216  C  CA    . TYR A 1 527 ? 155.016 147.191 95.235  1.00 25.64 ?  527 TYR A CA    1 
ATOM   4217  C  C     . TYR A 1 527 ? 154.943 146.753 93.778  1.00 26.99 ?  527 TYR A C     1 
ATOM   4218  O  O     . TYR A 1 527 ? 154.551 145.616 93.492  1.00 29.87 ?  527 TYR A O     1 
ATOM   4219  C  CB    . TYR A 1 527 ? 153.702 147.855 95.655  1.00 22.95 ?  527 TYR A CB    1 
ATOM   4220  C  CG    . TYR A 1 527 ? 152.473 147.007 95.419  1.00 27.51 ?  527 TYR A CG    1 
ATOM   4221  C  CD1   . TYR A 1 527 ? 152.015 146.130 96.393  1.00 24.78 ?  527 TYR A CD1   1 
ATOM   4222  C  CD2   . TYR A 1 527 ? 151.766 147.088 94.227  1.00 28.27 ?  527 TYR A CD2   1 
ATOM   4223  C  CE1   . TYR A 1 527 ? 150.894 145.354 96.181  1.00 26.06 ?  527 TYR A CE1   1 
ATOM   4224  C  CE2   . TYR A 1 527 ? 150.647 146.315 94.008  1.00 24.90 ?  527 TYR A CE2   1 
ATOM   4225  C  CZ    . TYR A 1 527 ? 150.215 145.452 94.988  1.00 18.91 ?  527 TYR A CZ    1 
ATOM   4226  O  OH    . TYR A 1 527 ? 149.097 144.682 94.774  1.00 30.61 ?  527 TYR A OH    1 
ATOM   4227  N  N     . PHE A 1 528 ? 155.312 147.631 92.850  1.00 29.56 ?  528 PHE A N     1 
ATOM   4228  C  CA    . PHE A 1 528 ? 155.145 147.390 91.425  1.00 28.24 ?  528 PHE A CA    1 
ATOM   4229  C  C     . PHE A 1 528 ? 156.347 146.706 90.784  1.00 34.05 ?  528 PHE A C     1 
ATOM   4230  O  O     . PHE A 1 528 ? 156.413 146.641 89.554  1.00 41.91 ?  528 PHE A O     1 
ATOM   4231  C  CB    . PHE A 1 528 ? 154.868 148.708 90.698  1.00 29.14 ?  528 PHE A CB    1 
ATOM   4232  C  CG    . PHE A 1 528 ? 153.667 149.447 91.211  1.00 31.18 ?  528 PHE A CG    1 
ATOM   4233  C  CD1   . PHE A 1 528 ? 153.787 150.363 92.241  1.00 29.96 ?  528 PHE A CD1   1 
ATOM   4234  C  CD2   . PHE A 1 528 ? 152.418 149.233 90.656  1.00 29.03 ?  528 PHE A CD2   1 
ATOM   4235  C  CE1   . PHE A 1 528 ? 152.684 151.047 92.710  1.00 32.17 ?  528 PHE A CE1   1 
ATOM   4236  C  CE2   . PHE A 1 528 ? 151.312 149.914 91.121  1.00 29.46 ?  528 PHE A CE2   1 
ATOM   4237  C  CZ    . PHE A 1 528 ? 151.445 150.822 92.149  1.00 28.16 ?  528 PHE A CZ    1 
ATOM   4238  N  N     . ASP A 1 529 ? 157.293 146.201 91.580  1.00 34.97 ?  529 ASP A N     1 
ATOM   4239  C  CA    . ASP A 1 529 ? 158.525 145.654 91.019  1.00 32.88 ?  529 ASP A CA    1 
ATOM   4240  C  C     . ASP A 1 529 ? 158.246 144.460 90.114  1.00 34.45 ?  529 ASP A C     1 
ATOM   4241  O  O     . ASP A 1 529 ? 158.677 144.429 88.954  1.00 41.56 ?  529 ASP A O     1 
ATOM   4242  C  CB    . ASP A 1 529 ? 159.477 145.256 92.147  1.00 35.83 ?  529 ASP A CB    1 
ATOM   4243  C  CG    . ASP A 1 529 ? 160.198 146.443 92.749  1.00 42.01 ?  529 ASP A CG    1 
ATOM   4244  O  OD1   . ASP A 1 529 ? 160.117 147.547 92.171  1.00 41.20 ?  529 ASP A OD1   1 
ATOM   4245  O  OD2   . ASP A 1 529 ? 160.848 146.273 93.802  1.00 42.29 -1 529 ASP A OD2   1 
ATOM   4246  N  N     . LYS A 1 530 ? 157.513 143.468 90.625  1.00 37.67 ?  530 LYS A N     1 
ATOM   4247  C  CA    . LYS A 1 530 ? 157.212 142.284 89.831  1.00 38.51 ?  530 LYS A CA    1 
ATOM   4248  C  C     . LYS A 1 530 ? 156.262 142.589 88.684  1.00 36.82 ?  530 LYS A C     1 
ATOM   4249  O  O     . LYS A 1 530 ? 156.185 141.806 87.733  1.00 40.77 ?  530 LYS A O     1 
ATOM   4250  C  CB    . LYS A 1 530 ? 156.620 141.188 90.717  1.00 38.22 ?  530 LYS A CB    1 
ATOM   4251  C  CG    . LYS A 1 530 ? 155.105 141.196 90.795  1.00 32.22 ?  530 LYS A CG    1 
ATOM   4252  C  CD    . LYS A 1 530 ? 154.606 140.239 91.859  1.00 34.28 ?  530 LYS A CD    1 
ATOM   4253  C  CE    . LYS A 1 530 ? 153.095 140.164 91.862  1.00 34.98 ?  530 LYS A CE    1 
ATOM   4254  N  NZ    . LYS A 1 530 ? 152.555 140.310 93.237  1.00 38.69 1  530 LYS A NZ    1 
ATOM   4255  N  N     . TYR A 1 531 ? 155.543 143.703 88.750  1.00 32.53 ?  531 TYR A N     1 
ATOM   4256  C  CA    . TYR A 1 531 ? 154.623 144.075 87.688  1.00 28.43 ?  531 TYR A CA    1 
ATOM   4257  C  C     . TYR A 1 531 ? 155.305 144.847 86.571  1.00 29.37 ?  531 TYR A C     1 
ATOM   4258  O  O     . TYR A 1 531 ? 154.911 144.714 85.406  1.00 35.21 ?  531 TYR A O     1 
ATOM   4259  C  CB    . TYR A 1 531 ? 153.473 144.894 88.267  1.00 25.66 ?  531 TYR A CB    1 
ATOM   4260  C  CG    . TYR A 1 531 ? 152.491 144.065 89.052  1.00 29.92 ?  531 TYR A CG    1 
ATOM   4261  C  CD1   . TYR A 1 531 ? 151.902 142.941 88.490  1.00 29.59 ?  531 TYR A CD1   1 
ATOM   4262  C  CD2   . TYR A 1 531 ? 152.154 144.397 90.356  1.00 27.27 ?  531 TYR A CD2   1 
ATOM   4263  C  CE1   . TYR A 1 531 ? 151.003 142.177 89.199  1.00 32.41 ?  531 TYR A CE1   1 
ATOM   4264  C  CE2   . TYR A 1 531 ? 151.256 143.637 91.073  1.00 25.93 ?  531 TYR A CE2   1 
ATOM   4265  C  CZ    . TYR A 1 531 ? 150.683 142.529 90.489  1.00 28.95 ?  531 TYR A CZ    1 
ATOM   4266  O  OH    . TYR A 1 531 ? 149.787 141.767 91.199  1.00 30.57 ?  531 TYR A OH    1 
ATOM   4267  N  N     . VAL A 1 532 ? 156.321 145.649 86.897  1.00 36.10 ?  532 VAL A N     1 
ATOM   4268  C  CA    . VAL A 1 532 ? 157.109 146.325 85.872  1.00 35.37 ?  532 VAL A CA    1 
ATOM   4269  C  C     . VAL A 1 532 ? 158.236 145.452 85.342  1.00 37.91 ?  532 VAL A C     1 
ATOM   4270  O  O     . VAL A 1 532 ? 158.823 145.782 84.299  1.00 42.70 ?  532 VAL A O     1 
ATOM   4271  C  CB    . VAL A 1 532 ? 157.696 147.650 86.399  1.00 36.98 ?  532 VAL A CB    1 
ATOM   4272  C  CG1   . VAL A 1 532 ? 156.587 148.555 86.912  1.00 33.66 ?  532 VAL A CG1   1 
ATOM   4273  C  CG2   . VAL A 1 532 ? 158.728 147.387 87.483  1.00 36.45 ?  532 VAL A CG2   1 
ATOM   4274  N  N     . SER A 1 533 ? 158.559 144.349 86.017  1.00 37.93 ?  533 SER A N     1 
ATOM   4275  C  CA    . SER A 1 533 ? 159.612 143.448 85.563  1.00 36.60 ?  533 SER A CA    1 
ATOM   4276  C  C     . SER A 1 533 ? 159.080 142.201 84.871  1.00 41.39 ?  533 SER A C     1 
ATOM   4277  O  O     . SER A 1 533 ? 159.654 141.763 83.871  1.00 43.93 ?  533 SER A O     1 
ATOM   4278  C  CB    . SER A 1 533 ? 160.495 143.033 86.742  1.00 41.09 ?  533 SER A CB    1 
ATOM   4279  O  OG    . SER A 1 533 ? 159.933 141.936 87.441  1.00 42.74 ?  533 SER A OG    1 
ATOM   4280  N  N     . THR A 1 534 ? 157.997 141.617 85.376  1.00 42.79 ?  534 THR A N     1 
ATOM   4281  C  CA    . THR A 1 534 ? 157.469 140.357 84.873  1.00 38.26 ?  534 THR A CA    1 
ATOM   4282  C  C     . THR A 1 534 ? 156.170 140.594 84.114  1.00 37.89 ?  534 THR A C     1 
ATOM   4283  O  O     . THR A 1 534 ? 155.296 141.333 84.576  1.00 42.30 ?  534 THR A O     1 
ATOM   4284  C  CB    . THR A 1 534 ? 157.230 139.369 86.020  1.00 36.43 ?  534 THR A CB    1 
ATOM   4285  O  OG1   . THR A 1 534 ? 158.483 139.006 86.611  1.00 42.70 ?  534 THR A OG1   1 
ATOM   4286  C  CG2   . THR A 1 534 ? 156.531 138.112 85.520  1.00 39.87 ?  534 THR A CG2   1 
ATOM   4287  N  N     . ASP A 1 535 ? 156.055 139.968 82.946  1.00 40.76 ?  535 ASP A N     1 
ATOM   4288  C  CA    . ASP A 1 535 ? 154.830 140.007 82.160  1.00 41.03 ?  535 ASP A CA    1 
ATOM   4289  C  C     . ASP A 1 535 ? 153.908 138.880 82.607  1.00 44.13 ?  535 ASP A C     1 
ATOM   4290  O  O     . ASP A 1 535 ? 154.351 137.744 82.794  1.00 45.35 ?  535 ASP A O     1 
ATOM   4291  C  CB    . ASP A 1 535 ? 155.141 139.880 80.669  1.00 41.69 ?  535 ASP A CB    1 
ATOM   4292  C  CG    . ASP A 1 535 ? 153.932 139.464 79.855  1.00 47.77 ?  535 ASP A CG    1 
ATOM   4293  O  OD1   . ASP A 1 535 ? 153.091 140.336 79.549  1.00 48.39 ?  535 ASP A OD1   1 
ATOM   4294  O  OD2   . ASP A 1 535 ? 153.823 138.264 79.524  1.00 46.71 -1 535 ASP A OD2   1 
ATOM   4295  N  N     . PHE A 1 536 ? 152.625 139.200 82.779  1.00 33.07 ?  536 PHE A N     1 
ATOM   4296  C  CA    . PHE A 1 536 ? 151.640 138.236 83.252  1.00 31.59 ?  536 PHE A CA    1 
ATOM   4297  C  C     . PHE A 1 536 ? 150.619 137.879 82.179  1.00 38.43 ?  536 PHE A C     1 
ATOM   4298  O  O     . PHE A 1 536 ? 149.510 137.446 82.501  1.00 40.84 ?  536 PHE A O     1 
ATOM   4299  C  CB    . PHE A 1 536 ? 150.942 138.766 84.503  1.00 32.63 ?  536 PHE A CB    1 
ATOM   4300  C  CG    . PHE A 1 536 ? 151.849 138.891 85.694  1.00 33.32 ?  536 PHE A CG    1 
ATOM   4301  C  CD1   . PHE A 1 536 ? 152.595 140.037 85.895  1.00 32.41 ?  536 PHE A CD1   1 
ATOM   4302  C  CD2   . PHE A 1 536 ? 151.962 137.856 86.605  1.00 29.13 ?  536 PHE A CD2   1 
ATOM   4303  C  CE1   . PHE A 1 536 ? 153.431 140.151 86.987  1.00 33.49 ?  536 PHE A CE1   1 
ATOM   4304  C  CE2   . PHE A 1 536 ? 152.797 137.965 87.697  1.00 28.57 ?  536 PHE A CE2   1 
ATOM   4305  C  CZ    . PHE A 1 536 ? 153.530 139.113 87.889  1.00 31.83 ?  536 PHE A CZ    1 
ATOM   4306  N  N     . SER A 1 537 ? 150.972 138.061 80.909  1.00 39.75 ?  537 SER A N     1 
ATOM   4307  C  CA    . SER A 1 537 ? 150.125 137.613 79.820  1.00 37.63 ?  537 SER A CA    1 
ATOM   4308  C  C     . SER A 1 537 ? 150.031 136.086 79.833  1.00 38.56 ?  537 SER A C     1 
ATOM   4309  O  O     . SER A 1 537 ? 150.972 135.407 80.252  1.00 43.02 ?  537 SER A O     1 
ATOM   4310  C  CB    . SER A 1 537 ? 150.689 138.096 78.485  1.00 38.04 ?  537 SER A CB    1 
ATOM   4311  O  OG    . SER A 1 537 ? 149.812 137.818 77.408  1.00 45.62 ?  537 SER A OG    1 
ATOM   4312  N  N     . PRO A 1 538 ? 148.901 135.525 79.403  1.00 39.69 ?  538 PRO A N     1 
ATOM   4313  C  CA    . PRO A 1 538 ? 148.751 134.065 79.433  1.00 38.42 ?  538 PRO A CA    1 
ATOM   4314  C  C     . PRO A 1 538 ? 149.816 133.369 78.598  1.00 41.89 ?  538 PRO A C     1 
ATOM   4315  O  O     . PRO A 1 538 ? 150.164 133.813 77.502  1.00 40.90 ?  538 PRO A O     1 
ATOM   4316  C  CB    . PRO A 1 538 ? 147.350 133.839 78.855  1.00 37.81 ?  538 PRO A CB    1 
ATOM   4317  C  CG    . PRO A 1 538 ? 146.639 135.127 79.060  1.00 39.79 ?  538 PRO A CG    1 
ATOM   4318  C  CD    . PRO A 1 538 ? 147.678 136.192 78.927  1.00 37.05 ?  538 PRO A CD    1 
ATOM   4319  N  N     . LYS A 1 539 ? 150.333 132.263 79.132  1.00 42.14 ?  539 LYS A N     1 
ATOM   4320  C  CA    . LYS A 1 539 ? 151.356 131.478 78.459  1.00 41.99 ?  539 LYS A CA    1 
ATOM   4321  C  C     . LYS A 1 539 ? 150.782 130.398 77.552  1.00 44.20 ?  539 LYS A C     1 
ATOM   4322  O  O     . LYS A 1 539 ? 151.539 129.779 76.798  1.00 48.33 ?  539 LYS A O     1 
ATOM   4323  C  CB    . LYS A 1 539 ? 152.288 130.829 79.487  1.00 44.26 ?  539 LYS A CB    1 
ATOM   4324  C  CG    . LYS A 1 539 ? 152.575 131.695 80.700  1.00 46.33 ?  539 LYS A CG    1 
ATOM   4325  C  CD    . LYS A 1 539 ? 153.899 132.429 80.557  1.00 45.75 ?  539 LYS A CD    1 
ATOM   4326  C  CE    . LYS A 1 539 ? 153.995 133.585 81.541  1.00 46.33 ?  539 LYS A CE    1 
ATOM   4327  N  NZ    . LYS A 1 539 ? 153.195 134.761 81.099  1.00 44.50 1  539 LYS A NZ    1 
ATOM   4328  N  N     . TYR A 1 540 ? 149.476 130.158 77.606  1.00 43.85 ?  540 TYR A N     1 
ATOM   4329  C  CA    . TYR A 1 540 ? 148.825 129.139 76.799  1.00 43.78 ?  540 TYR A CA    1 
ATOM   4330  C  C     . TYR A 1 540 ? 147.880 129.789 75.799  1.00 46.70 ?  540 TYR A C     1 
ATOM   4331  O  O     . TYR A 1 540 ? 147.188 130.759 76.125  1.00 45.29 ?  540 TYR A O     1 
ATOM   4332  C  CB    . TYR A 1 540 ? 148.062 128.143 77.676  1.00 41.74 ?  540 TYR A CB    1 
ATOM   4333  C  CG    . TYR A 1 540 ? 148.939 127.435 78.682  1.00 45.65 ?  540 TYR A CG    1 
ATOM   4334  C  CD1   . TYR A 1 540 ? 149.188 127.988 79.929  1.00 45.44 ?  540 TYR A CD1   1 
ATOM   4335  C  CD2   . TYR A 1 540 ? 149.529 126.217 78.376  1.00 45.66 ?  540 TYR A CD2   1 
ATOM   4336  C  CE1   . TYR A 1 540 ? 149.994 127.346 80.845  1.00 46.54 ?  540 TYR A CE1   1 
ATOM   4337  C  CE2   . TYR A 1 540 ? 150.336 125.566 79.285  1.00 41.75 ?  540 TYR A CE2   1 
ATOM   4338  C  CZ    . TYR A 1 540 ? 150.565 126.135 80.519  1.00 45.77 ?  540 TYR A CZ    1 
ATOM   4339  O  OH    . TYR A 1 540 ? 151.371 125.490 81.426  1.00 45.71 ?  540 TYR A OH    1 
ATOM   4340  N  N     . GLU A 1 541 ? 147.864 129.253 74.577  1.00 49.36 ?  541 GLU A N     1 
ATOM   4341  C  CA    . GLU A 1 541 ? 146.998 129.802 73.541  1.00 47.22 ?  541 GLU A CA    1 
ATOM   4342  C  C     . GLU A 1 541 ? 145.526 129.620 73.887  1.00 49.17 ?  541 GLU A C     1 
ATOM   4343  O  O     . GLU A 1 541 ? 144.695 130.453 73.511  1.00 47.50 ?  541 GLU A O     1 
ATOM   4344  C  CB    . GLU A 1 541 ? 147.323 129.165 72.187  1.00 48.57 ?  541 GLU A CB    1 
ATOM   4345  C  CG    . GLU A 1 541 ? 146.768 127.759 71.976  1.00 52.66 ?  541 GLU A CG    1 
ATOM   4346  C  CD    . GLU A 1 541 ? 147.471 126.711 72.821  1.00 57.43 ?  541 GLU A CD    1 
ATOM   4347  O  OE1   . GLU A 1 541 ? 148.599 126.973 73.289  1.00 55.11 ?  541 GLU A OE1   1 
ATOM   4348  O  OE2   . GLU A 1 541 ? 146.893 125.621 73.016  1.00 52.48 -1 541 GLU A OE2   1 
ATOM   4349  N  N     . LYS A 1 542 ? 145.184 128.544 74.601  1.00 47.03 ?  542 LYS A N     1 
ATOM   4350  C  CA    . LYS A 1 542 ? 143.803 128.352 75.029  1.00 44.20 ?  542 LYS A CA    1 
ATOM   4351  C  C     . LYS A 1 542 ? 143.366 129.452 75.985  1.00 43.71 ?  542 LYS A C     1 
ATOM   4352  O  O     . LYS A 1 542 ? 142.252 129.977 75.876  1.00 46.35 ?  542 LYS A O     1 
ATOM   4353  C  CB    . LYS A 1 542 ? 143.645 126.981 75.683  1.00 42.74 ?  542 LYS A CB    1 
ATOM   4354  C  CG    . LYS A 1 542 ? 142.204 126.557 75.897  1.00 44.00 ?  542 LYS A CG    1 
ATOM   4355  C  CD    . LYS A 1 542 ? 142.095 125.523 77.005  1.00 44.81 ?  542 LYS A CD    1 
ATOM   4356  C  CE    . LYS A 1 542 ? 140.762 124.795 76.952  1.00 46.45 ?  542 LYS A CE    1 
ATOM   4357  N  NZ    . LYS A 1 542 ? 139.627 125.735 76.746  1.00 47.24 1  542 LYS A NZ    1 
ATOM   4358  N  N     . ILE A 1 543 ? 144.231 129.811 76.935  1.00 40.29 ?  543 ILE A N     1 
ATOM   4359  C  CA    . ILE A 1 543 ? 143.905 130.869 77.884  1.00 38.16 ?  543 ILE A CA    1 
ATOM   4360  C  C     . ILE A 1 543 ? 143.923 132.230 77.201  1.00 39.04 ?  543 ILE A C     1 
ATOM   4361  O  O     . ILE A 1 543 ? 143.107 133.106 77.512  1.00 41.31 ?  543 ILE A O     1 
ATOM   4362  C  CB    . ILE A 1 543 ? 144.869 130.819 79.082  1.00 38.43 ?  543 ILE A CB    1 
ATOM   4363  C  CG1   . ILE A 1 543 ? 144.839 129.436 79.734  1.00 38.67 ?  543 ILE A CG1   1 
ATOM   4364  C  CG2   . ILE A 1 543 ? 144.514 131.888 80.094  1.00 39.41 ?  543 ILE A CG2   1 
ATOM   4365  C  CD1   . ILE A 1 543 ? 143.446 128.923 80.023  1.00 37.81 ?  543 ILE A CD1   1 
ATOM   4366  N  N     . ALA A 1 544 ? 144.855 132.433 76.266  1.00 41.27 ?  544 ALA A N     1 
ATOM   4367  C  CA    . ALA A 1 544 ? 144.962 133.722 75.593  1.00 43.83 ?  544 ALA A CA    1 
ATOM   4368  C  C     . ALA A 1 544 ? 143.713 134.046 74.784  1.00 43.06 ?  544 ALA A C     1 
ATOM   4369  O  O     . ALA A 1 544 ? 143.371 135.222 74.618  1.00 43.78 ?  544 ALA A O     1 
ATOM   4370  C  CB    . ALA A 1 544 ? 146.196 133.743 74.692  1.00 44.54 ?  544 ALA A CB    1 
ATOM   4371  N  N     . ASN A 1 545 ? 143.022 133.025 74.268  1.00 44.96 ?  545 ASN A N     1 
ATOM   4372  C  CA    . ASN A 1 545 ? 141.775 133.276 73.554  1.00 46.63 ?  545 ASN A CA    1 
ATOM   4373  C  C     . ASN A 1 545 ? 140.642 133.628 74.508  1.00 46.37 ?  545 ASN A C     1 
ATOM   4374  O  O     . ASN A 1 545 ? 139.685 134.298 74.107  1.00 45.67 ?  545 ASN A O     1 
ATOM   4375  C  CB    . ASN A 1 545 ? 141.396 132.065 72.702  1.00 46.98 ?  545 ASN A CB    1 
ATOM   4376  C  CG    . ASN A 1 545 ? 142.531 131.600 71.813  1.00 50.71 ?  545 ASN A CG    1 
ATOM   4377  O  OD1   . ASN A 1 545 ? 143.445 132.364 71.504  1.00 50.89 ?  545 ASN A OD1   1 
ATOM   4378  N  ND2   . ASN A 1 545 ? 142.478 130.340 71.396  1.00 49.17 ?  545 ASN A ND2   1 
ATOM   4379  N  N     . LEU A 1 546 ? 140.726 133.182 75.764  1.00 44.44 ?  546 LEU A N     1 
ATOM   4380  C  CA    . LEU A 1 546 ? 139.709 133.544 76.744  1.00 42.41 ?  546 LEU A CA    1 
ATOM   4381  C  C     . LEU A 1 546 ? 139.707 135.042 77.016  1.00 42.24 ?  546 LEU A C     1 
ATOM   4382  O  O     . LEU A 1 546 ? 138.664 135.611 77.357  1.00 45.24 ?  546 LEU A O     1 
ATOM   4383  C  CB    . LEU A 1 546 ? 139.930 132.771 78.043  1.00 40.80 ?  546 LEU A CB    1 
ATOM   4384  C  CG    . LEU A 1 546 ? 139.731 131.256 77.997  1.00 39.12 ?  546 LEU A CG    1 
ATOM   4385  C  CD1   . LEU A 1 546 ? 140.069 130.640 79.342  1.00 39.65 ?  546 LEU A CD1   1 
ATOM   4386  C  CD2   . LEU A 1 546 ? 138.309 130.910 77.592  1.00 40.10 ?  546 LEU A CD2   1 
ATOM   4387  N  N     . PHE A 1 547 ? 140.857 135.694 76.867  1.00 40.24 ?  547 PHE A N     1 
ATOM   4388  C  CA    . PHE A 1 547 ? 140.985 137.127 77.086  1.00 40.24 ?  547 PHE A CA    1 
ATOM   4389  C  C     . PHE A 1 547 ? 140.929 137.924 75.790  1.00 40.78 ?  547 PHE A C     1 
ATOM   4390  O  O     . PHE A 1 547 ? 141.195 139.129 75.804  1.00 42.05 ?  547 PHE A O     1 
ATOM   4391  C  CB    . PHE A 1 547 ? 142.287 137.429 77.830  1.00 36.73 ?  547 PHE A CB    1 
ATOM   4392  C  CG    . PHE A 1 547 ? 142.281 136.996 79.267  1.00 38.42 ?  547 PHE A CG    1 
ATOM   4393  C  CD1   . PHE A 1 547 ? 141.765 137.820 80.251  1.00 37.60 ?  547 PHE A CD1   1 
ATOM   4394  C  CD2   . PHE A 1 547 ? 142.791 135.763 79.634  1.00 37.01 ?  547 PHE A CD2   1 
ATOM   4395  C  CE1   . PHE A 1 547 ? 141.761 137.424 81.573  1.00 33.39 ?  547 PHE A CE1   1 
ATOM   4396  C  CE2   . PHE A 1 547 ? 142.788 135.362 80.954  1.00 35.07 ?  547 PHE A CE2   1 
ATOM   4397  C  CZ    . PHE A 1 547 ? 142.272 136.193 81.924  1.00 34.33 ?  547 PHE A CZ    1 
ATOM   4398  N  N     . GLU A 1 548 ? 140.597 137.279 74.674  1.00 50.24 ?  548 GLU A N     1 
ATOM   4399  C  CA    . GLU A 1 548 ? 140.506 137.977 73.400  1.00 52.22 ?  548 GLU A CA    1 
ATOM   4400  C  C     . GLU A 1 548 ? 139.388 139.009 73.442  1.00 51.05 ?  548 GLU A C     1 
ATOM   4401  O  O     . GLU A 1 548 ? 138.292 138.744 73.941  1.00 51.91 ?  548 GLU A O     1 
ATOM   4402  C  CB    . GLU A 1 548 ? 140.276 136.974 72.266  1.00 48.82 ?  548 GLU A CB    1 
ATOM   4403  C  CG    . GLU A 1 548 ? 139.634 137.549 71.008  1.00 51.53 ?  548 GLU A CG    1 
ATOM   4404  C  CD    . GLU A 1 548 ? 138.119 137.448 71.019  1.00 52.72 ?  548 GLU A CD    1 
ATOM   4405  O  OE1   . GLU A 1 548 ? 137.457 138.364 70.488  1.00 51.34 ?  548 GLU A OE1   1 
ATOM   4406  O  OE2   . GLU A 1 548 ? 137.593 136.450 71.556  1.00 53.80 -1 548 GLU A OE2   1 
ATOM   4407  N  N     . GLY A 1 549 ? 139.669 140.195 72.905  1.00 45.32 ?  549 GLY A N     1 
ATOM   4408  C  CA    . GLY A 1 549 ? 138.748 141.306 72.991  1.00 46.85 ?  549 GLY A CA    1 
ATOM   4409  C  C     . GLY A 1 549 ? 138.846 142.110 74.266  1.00 47.31 ?  549 GLY A C     1 
ATOM   4410  O  O     . GLY A 1 549 ? 138.050 143.039 74.458  1.00 46.90 ?  549 GLY A O     1 
ATOM   4411  N  N     . MET A 1 550 ? 139.792 141.785 75.145  1.00 47.64 ?  550 MET A N     1 
ATOM   4412  C  CA    . MET A 1 550 ? 139.984 142.486 76.405  1.00 44.25 ?  550 MET A CA    1 
ATOM   4413  C  C     . MET A 1 550 ? 141.469 142.760 76.579  1.00 44.66 ?  550 MET A C     1 
ATOM   4414  O  O     . MET A 1 550 ? 142.282 141.832 76.533  1.00 48.18 ?  550 MET A O     1 
ATOM   4415  C  CB    . MET A 1 550 ? 139.441 141.660 77.574  1.00 43.54 ?  550 MET A CB    1 
ATOM   4416  C  CG    . MET A 1 550 ? 138.882 142.482 78.716  1.00 48.40 ?  550 MET A CG    1 
ATOM   4417  S  SD    . MET A 1 550 ? 138.582 141.501 80.197  1.00 55.01 ?  550 MET A SD    1 
ATOM   4418  C  CE    . MET A 1 550 ? 138.562 139.841 79.528  1.00 44.39 ?  550 MET A CE    1 
ATOM   4419  N  N     . HIS A 1 551 ? 141.821 144.028 76.776  1.00 40.57 ?  551 HIS A N     1 
ATOM   4420  C  CA    . HIS A 1 551 ? 143.225 144.408 76.839  1.00 40.38 ?  551 HIS A CA    1 
ATOM   4421  C  C     . HIS A 1 551 ? 143.868 143.901 78.124  1.00 41.17 ?  551 HIS A C     1 
ATOM   4422  O  O     . HIS A 1 551 ? 143.340 144.105 79.221  1.00 42.19 ?  551 HIS A O     1 
ATOM   4423  C  CB    . HIS A 1 551 ? 143.372 145.925 76.742  1.00 39.62 ?  551 HIS A CB    1 
ATOM   4424  C  CG    . HIS A 1 551 ? 144.750 146.417 77.059  1.00 43.71 ?  551 HIS A CG    1 
ATOM   4425  N  ND1   . HIS A 1 551 ? 145.785 146.366 76.150  1.00 46.46 ?  551 HIS A ND1   1 
ATOM   4426  C  CD2   . HIS A 1 551 ? 145.265 146.965 78.185  1.00 43.40 ?  551 HIS A CD2   1 
ATOM   4427  C  CE1   . HIS A 1 551 ? 146.877 146.863 76.702  1.00 44.87 ?  551 HIS A CE1   1 
ATOM   4428  N  NE2   . HIS A 1 551 ? 146.589 147.234 77.936  1.00 43.03 ?  551 HIS A NE2   1 
ATOM   4429  N  N     . ILE A 1 552 ? 145.011 143.243 77.983  1.00 37.11 ?  552 ILE A N     1 
ATOM   4430  C  CA    . ILE A 1 552 ? 145.787 142.737 79.111  1.00 36.65 ?  552 ILE A CA    1 
ATOM   4431  C  C     . ILE A 1 552 ? 146.926 143.716 79.372  1.00 39.13 ?  552 ILE A C     1 
ATOM   4432  O  O     . ILE A 1 552 ? 147.763 143.920 78.479  1.00 41.15 ?  552 ILE A O     1 
ATOM   4433  C  CB    . ILE A 1 552 ? 146.326 141.326 78.837  1.00 36.39 ?  552 ILE A CB    1 
ATOM   4434  C  CG1   . ILE A 1 552 ? 145.173 140.360 78.567  1.00 35.61 ?  552 ILE A CG1   1 
ATOM   4435  C  CG2   . ILE A 1 552 ? 147.167 140.842 80.001  1.00 35.93 ?  552 ILE A CG2   1 
ATOM   4436  C  CD1   . ILE A 1 552 ? 145.612 139.040 77.988  1.00 39.04 ?  552 ILE A CD1   1 
ATOM   4437  N  N     . PRO A 1 553 ? 146.989 144.345 80.545  1.00 41.21 ?  553 PRO A N     1 
ATOM   4438  C  CA    . PRO A 1 553 ? 148.083 145.285 80.818  1.00 37.58 ?  553 PRO A CA    1 
ATOM   4439  C  C     . PRO A 1 553 ? 149.441 144.608 80.735  1.00 37.53 ?  553 PRO A C     1 
ATOM   4440  O  O     . PRO A 1 553 ? 149.643 143.502 81.242  1.00 35.05 ?  553 PRO A O     1 
ATOM   4441  C  CB    . PRO A 1 553 ? 147.785 145.772 82.241  1.00 34.42 ?  553 PRO A CB    1 
ATOM   4442  C  CG    . PRO A 1 553 ? 146.334 145.515 82.435  1.00 32.51 ?  553 PRO A CG    1 
ATOM   4443  C  CD    . PRO A 1 553 ? 146.022 144.288 81.649  1.00 33.93 ?  553 PRO A CD    1 
ATOM   4444  N  N     . THR A 1 554 ? 150.375 145.290 80.090  1.00 42.64 ?  554 THR A N     1 
ATOM   4445  C  CA    . THR A 1 554 ? 151.727 144.804 79.895  1.00 40.12 ?  554 THR A CA    1 
ATOM   4446  C  C     . THR A 1 554 ? 152.645 145.409 80.953  1.00 36.10 ?  554 THR A C     1 
ATOM   4447  O  O     . THR A 1 554 ? 152.192 146.026 81.922  1.00 38.78 ?  554 THR A O     1 
ATOM   4448  C  CB    . THR A 1 554 ? 152.197 145.131 78.478  1.00 38.52 ?  554 THR A CB    1 
ATOM   4449  O  OG1   . THR A 1 554 ? 152.194 146.550 78.288  1.00 43.66 ?  554 THR A OG1   1 
ATOM   4450  C  CG2   . THR A 1 554 ? 151.276 144.489 77.453  1.00 40.83 ?  554 THR A CG2   1 
ATOM   4451  N  N     . THR A 1 555 ? 153.954 145.224 80.777  1.00 38.32 ?  555 THR A N     1 
ATOM   4452  C  CA    . THR A 1 555 ? 154.907 145.870 81.672  1.00 35.88 ?  555 THR A CA    1 
ATOM   4453  C  C     . THR A 1 555 ? 154.879 147.384 81.503  1.00 38.84 ?  555 THR A C     1 
ATOM   4454  O  O     . THR A 1 555 ? 155.039 148.123 82.479  1.00 42.01 ?  555 THR A O     1 
ATOM   4455  C  CB    . THR A 1 555 ? 156.313 145.330 81.427  1.00 39.23 ?  555 THR A CB    1 
ATOM   4456  O  OG1   . THR A 1 555 ? 156.494 145.079 80.027  1.00 47.13 ?  555 THR A OG1   1 
ATOM   4457  C  CG2   . THR A 1 555 ? 156.526 144.036 82.199  1.00 38.19 ?  555 THR A CG2   1 
ATOM   4458  N  N     . GLU A 1 556 ? 154.680 147.863 80.273  1.00 39.45 ?  556 GLU A N     1 
ATOM   4459  C  CA    . GLU A 1 556 ? 154.581 149.302 80.043  1.00 41.11 ?  556 GLU A CA    1 
ATOM   4460  C  C     . GLU A 1 556 ? 153.349 149.887 80.722  1.00 41.76 ?  556 GLU A C     1 
ATOM   4461  O  O     . GLU A 1 556 ? 153.408 150.974 81.311  1.00 44.03 ?  556 GLU A O     1 
ATOM   4462  C  CB    . GLU A 1 556 ? 154.555 149.590 78.542  1.00 41.87 ?  556 GLU A CB    1 
ATOM   4463  C  CG    . GLU A 1 556 ? 155.769 149.091 77.749  1.00 45.29 ?  556 GLU A CG    1 
ATOM   4464  C  CD    . GLU A 1 556 ? 157.091 149.162 78.509  1.00 49.26 ?  556 GLU A CD    1 
ATOM   4465  O  OE1   . GLU A 1 556 ? 157.916 148.239 78.346  1.00 49.26 ?  556 GLU A OE1   1 
ATOM   4466  O  OE2   . GLU A 1 556 ? 157.337 150.160 79.219  1.00 43.00 -1 556 GLU A OE2   1 
ATOM   4467  N  N     . ASP A 1 557 ? 152.219 149.181 80.643  1.00 42.48 ?  557 ASP A N     1 
ATOM   4468  C  CA    . ASP A 1 557 ? 151.013 149.640 81.322  1.00 39.88 ?  557 ASP A CA    1 
ATOM   4469  C  C     . ASP A 1 557 ? 151.221 149.684 82.829  1.00 37.08 ?  557 ASP A C     1 
ATOM   4470  O  O     . ASP A 1 557 ? 150.764 150.616 83.501  1.00 37.78 ?  557 ASP A O     1 
ATOM   4471  C  CB    . ASP A 1 557 ? 149.836 148.734 80.970  1.00 37.18 ?  557 ASP A CB    1 
ATOM   4472  C  CG    . ASP A 1 557 ? 149.078 149.215 79.754  1.00 43.58 ?  557 ASP A CG    1 
ATOM   4473  O  OD1   . ASP A 1 557 ? 148.777 150.424 79.680  1.00 45.62 ?  557 ASP A OD1   1 
ATOM   4474  O  OD2   . ASP A 1 557 ? 148.785 148.383 78.869  1.00 43.98 -1 557 ASP A OD2   1 
ATOM   4475  N  N     . TRP A 1 558 ? 151.917 148.688 83.377  1.00 30.18 ?  558 TRP A N     1 
ATOM   4476  C  CA    . TRP A 1 558 ? 152.192 148.686 84.808  1.00 27.84 ?  558 TRP A CA    1 
ATOM   4477  C  C     . TRP A 1 558 ? 153.162 149.793 85.200  1.00 34.90 ?  558 TRP A C     1 
ATOM   4478  O  O     . TRP A 1 558 ? 153.036 150.355 86.290  1.00 35.93 ?  558 TRP A O     1 
ATOM   4479  C  CB    . TRP A 1 558 ? 152.728 147.324 85.237  1.00 30.23 ?  558 TRP A CB    1 
ATOM   4480  C  CG    . TRP A 1 558 ? 151.655 146.360 85.636  1.00 29.42 ?  558 TRP A CG    1 
ATOM   4481  C  CD1   . TRP A 1 558 ? 151.208 145.287 84.923  1.00 28.16 ?  558 TRP A CD1   1 
ATOM   4482  C  CD2   . TRP A 1 558 ? 150.886 146.387 86.845  1.00 28.54 ?  558 TRP A CD2   1 
ATOM   4483  N  NE1   . TRP A 1 558 ? 150.215 144.640 85.614  1.00 30.68 ?  558 TRP A NE1   1 
ATOM   4484  C  CE2   . TRP A 1 558 ? 149.999 145.294 86.798  1.00 29.91 ?  558 TRP A CE2   1 
ATOM   4485  C  CE3   . TRP A 1 558 ? 150.868 147.222 87.965  1.00 32.95 ?  558 TRP A CE3   1 
ATOM   4486  C  CZ2   . TRP A 1 558 ? 149.104 145.018 87.827  1.00 24.29 ?  558 TRP A CZ2   1 
ATOM   4487  C  CZ3   . TRP A 1 558 ? 149.976 146.946 88.982  1.00 27.71 ?  558 TRP A CZ3   1 
ATOM   4488  C  CH2   . TRP A 1 558 ? 149.107 145.855 88.908  1.00 19.86 ?  558 TRP A CH2   1 
ATOM   4489  N  N     . LYS A 1 559 ? 154.128 150.122 84.339  1.00 40.62 ?  559 LYS A N     1 
ATOM   4490  C  CA    . LYS A 1 559 ? 155.001 151.262 84.611  1.00 35.82 ?  559 LYS A CA    1 
ATOM   4491  C  C     . LYS A 1 559 ? 154.214 152.567 84.621  1.00 36.87 ?  559 LYS A C     1 
ATOM   4492  O  O     . LYS A 1 559 ? 154.429 153.429 85.484  1.00 40.72 ?  559 LYS A O     1 
ATOM   4493  C  CB    . LYS A 1 559 ? 156.125 151.327 83.577  1.00 38.77 ?  559 LYS A CB    1 
ATOM   4494  C  CG    . LYS A 1 559 ? 157.136 150.201 83.672  1.00 38.52 ?  559 LYS A CG    1 
ATOM   4495  C  CD    . LYS A 1 559 ? 157.986 150.125 82.416  1.00 41.10 ?  559 LYS A CD    1 
ATOM   4496  C  CE    . LYS A 1 559 ? 159.056 149.053 82.532  1.00 40.35 ?  559 LYS A CE    1 
ATOM   4497  N  NZ    . LYS A 1 559 ? 159.804 149.145 83.816  1.00 43.81 1  559 LYS A NZ    1 
ATOM   4498  N  N     . LYS A 1 560 ? 153.299 152.728 83.662  1.00 36.29 ?  560 LYS A N     1 
ATOM   4499  C  CA    . LYS A 1 560 ? 152.456 153.918 83.643  1.00 33.56 ?  560 LYS A CA    1 
ATOM   4500  C  C     . LYS A 1 560 ? 151.583 153.993 84.890  1.00 36.41 ?  560 LYS A C     1 
ATOM   4501  O  O     . LYS A 1 560 ? 151.417 155.068 85.476  1.00 42.03 ?  560 LYS A O     1 
ATOM   4502  C  CB    . LYS A 1 560 ? 151.592 153.932 82.381  1.00 34.44 ?  560 LYS A CB    1 
ATOM   4503  C  CG    . LYS A 1 560 ? 152.373 154.153 81.098  1.00 38.39 ?  560 LYS A CG    1 
ATOM   4504  C  CD    . LYS A 1 560 ? 151.453 154.174 79.890  1.00 39.77 ?  560 LYS A CD    1 
ATOM   4505  C  CE    . LYS A 1 560 ? 152.141 153.602 78.661  1.00 40.30 ?  560 LYS A CE    1 
ATOM   4506  N  NZ    . LYS A 1 560 ? 151.800 152.169 78.448  1.00 40.83 1  560 LYS A NZ    1 
ATOM   4507  N  N     . LEU A 1 561 ? 151.023 152.858 85.313  1.00 33.41 ?  561 LEU A N     1 
ATOM   4508  C  CA    . LEU A 1 561 ? 150.218 152.837 86.531  1.00 29.59 ?  561 LEU A CA    1 
ATOM   4509  C  C     . LEU A 1 561 ? 151.063 153.144 87.761  1.00 32.43 ?  561 LEU A C     1 
ATOM   4510  O  O     . LEU A 1 561 ? 150.596 153.810 88.688  1.00 36.45 ?  561 LEU A O     1 
ATOM   4511  C  CB    . LEU A 1 561 ? 149.525 151.483 86.684  1.00 31.12 ?  561 LEU A CB    1 
ATOM   4512  C  CG    . LEU A 1 561 ? 148.705 151.329 87.966  1.00 31.43 ?  561 LEU A CG    1 
ATOM   4513  C  CD1   . LEU A 1 561 ? 147.600 152.368 88.012  1.00 27.55 ?  561 LEU A CD1   1 
ATOM   4514  C  CD2   . LEU A 1 561 ? 148.133 149.934 88.092  1.00 28.89 ?  561 LEU A CD2   1 
ATOM   4515  N  N     . LYS A 1 562 ? 152.301 152.650 87.796  1.00 34.56 ?  562 LYS A N     1 
ATOM   4516  C  CA    . LYS A 1 562 ? 153.194 152.952 88.908  1.00 33.38 ?  562 LYS A CA    1 
ATOM   4517  C  C     . LYS A 1 562 ? 153.492 154.442 88.982  1.00 34.22 ?  562 LYS A C     1 
ATOM   4518  O  O     . LYS A 1 562 ? 153.484 155.030 90.069  1.00 38.77 ?  562 LYS A O     1 
ATOM   4519  C  CB    . LYS A 1 562 ? 154.486 152.147 88.767  1.00 35.62 ?  562 LYS A CB    1 
ATOM   4520  C  CG    . LYS A 1 562 ? 155.594 152.562 89.714  1.00 31.08 ?  562 LYS A CG    1 
ATOM   4521  C  CD    . LYS A 1 562 ? 156.882 151.825 89.401  1.00 28.64 ?  562 LYS A CD    1 
ATOM   4522  C  CE    . LYS A 1 562 ? 158.012 152.271 90.310  1.00 34.47 ?  562 LYS A CE    1 
ATOM   4523  N  NZ    . LYS A 1 562 ? 159.083 151.241 90.399  1.00 41.45 1  562 LYS A NZ    1 
ATOM   4524  N  N     . ALA A 1 563 ? 153.750 155.071 87.833  1.00 32.24 ?  563 ALA A N     1 
ATOM   4525  C  CA    . ALA A 1 563 ? 153.953 156.517 87.815  1.00 33.14 ?  563 ALA A CA    1 
ATOM   4526  C  C     . ALA A 1 563 ? 152.694 157.256 88.259  1.00 36.18 ?  563 ALA A C     1 
ATOM   4527  O  O     . ALA A 1 563 ? 152.769 158.229 89.021  1.00 42.44 ?  563 ALA A O     1 
ATOM   4528  C  CB    . ALA A 1 563 ? 154.379 156.968 86.420  1.00 35.79 ?  563 ALA A CB    1 
ATOM   4529  N  N     . PHE A 1 564 ? 151.529 156.799 87.796  1.00 34.18 ?  564 PHE A N     1 
ATOM   4530  C  CA    . PHE A 1 564 ? 150.266 157.420 88.183  1.00 31.53 ?  564 PHE A CA    1 
ATOM   4531  C  C     . PHE A 1 564 ? 150.044 157.330 89.689  1.00 35.60 ?  564 PHE A C     1 
ATOM   4532  O  O     . PHE A 1 564 ? 149.596 158.295 90.317  1.00 38.50 ?  564 PHE A O     1 
ATOM   4533  C  CB    . PHE A 1 564 ? 149.118 156.752 87.425  1.00 32.91 ?  564 PHE A CB    1 
ATOM   4534  C  CG    . PHE A 1 564 ? 147.829 157.518 87.464  1.00 33.21 ?  564 PHE A CG    1 
ATOM   4535  C  CD1   . PHE A 1 564 ? 147.543 158.469 86.501  1.00 35.68 ?  564 PHE A CD1   1 
ATOM   4536  C  CD2   . PHE A 1 564 ? 146.895 157.273 88.455  1.00 34.31 ?  564 PHE A CD2   1 
ATOM   4537  C  CE1   . PHE A 1 564 ? 146.354 159.169 86.532  1.00 39.13 ?  564 PHE A CE1   1 
ATOM   4538  C  CE2   . PHE A 1 564 ? 145.705 157.970 88.492  1.00 35.63 ?  564 PHE A CE2   1 
ATOM   4539  C  CZ    . PHE A 1 564 ? 145.432 158.919 87.529  1.00 38.90 ?  564 PHE A CZ    1 
ATOM   4540  N  N     . VAL A 1 565 ? 150.350 156.177 90.282  1.00 35.82 ?  565 VAL A N     1 
ATOM   4541  C  CA    . VAL A 1 565 ? 150.188 156.000 91.720  1.00 29.96 ?  565 VAL A CA    1 
ATOM   4542  C  C     . VAL A 1 565 ? 151.192 156.854 92.482  1.00 33.54 ?  565 VAL A C     1 
ATOM   4543  O  O     . VAL A 1 565 ? 150.857 157.468 93.502  1.00 36.12 ?  565 VAL A O     1 
ATOM   4544  C  CB    . VAL A 1 565 ? 150.316 154.509 92.084  1.00 29.53 ?  565 VAL A CB    1 
ATOM   4545  C  CG1   . VAL A 1 565 ? 150.522 154.333 93.578  1.00 28.69 ?  565 VAL A CG1   1 
ATOM   4546  C  CG2   . VAL A 1 565 ? 149.086 153.757 91.626  1.00 33.70 ?  565 VAL A CG2   1 
ATOM   4547  N  N     . ALA A 1 566 ? 152.434 156.915 92.001  1.00 36.68 ?  566 ALA A N     1 
ATOM   4548  C  CA    . ALA A 1 566 ? 153.443 157.729 92.668  1.00 36.24 ?  566 ALA A CA    1 
ATOM   4549  C  C     . ALA A 1 566 ? 153.097 159.209 92.615  1.00 38.26 ?  566 ALA A C     1 
ATOM   4550  O  O     . ALA A 1 566 ? 153.454 159.960 93.528  1.00 42.85 ?  566 ALA A O     1 
ATOM   4551  C  CB    . ALA A 1 566 ? 154.814 157.482 92.040  1.00 36.68 ?  566 ALA A CB    1 
ATOM   4552  N  N     . GLU A 1 567 ? 152.406 159.645 91.564  1.00 40.84 ?  567 GLU A N     1 
ATOM   4553  C  CA    . GLU A 1 567 ? 152.076 161.055 91.416  1.00 40.06 ?  567 GLU A CA    1 
ATOM   4554  C  C     . GLU A 1 567 ? 150.722 161.433 92.008  1.00 39.80 ?  567 GLU A C     1 
ATOM   4555  O  O     . GLU A 1 567 ? 150.508 162.612 92.311  1.00 43.67 ?  567 GLU A O     1 
ATOM   4556  C  CB    . GLU A 1 567 ? 152.133 161.440 89.932  1.00 42.38 ?  567 GLU A CB    1 
ATOM   4557  C  CG    . GLU A 1 567 ? 152.163 162.931 89.656  1.00 43.90 ?  567 GLU A CG    1 
ATOM   4558  C  CD    . GLU A 1 567 ? 150.880 163.424 89.028  1.00 47.55 ?  567 GLU A CD    1 
ATOM   4559  O  OE1   . GLU A 1 567 ? 150.218 162.620 88.340  1.00 46.07 ?  567 GLU A OE1   1 
ATOM   4560  O  OE2   . GLU A 1 567 ? 150.534 164.609 89.219  1.00 47.17 -1 567 GLU A OE2   1 
ATOM   4561  N  N     . HIS A 1 568 ? 149.811 160.474 92.195  1.00 39.70 ?  568 HIS A N     1 
ATOM   4562  C  CA    . HIS A 1 568 ? 148.501 160.749 92.771  1.00 38.76 ?  568 HIS A CA    1 
ATOM   4563  C  C     . HIS A 1 568 ? 148.196 160.005 94.062  1.00 35.94 ?  568 HIS A C     1 
ATOM   4564  O  O     . HIS A 1 568 ? 147.294 160.429 94.791  1.00 40.11 ?  568 HIS A O     1 
ATOM   4565  C  CB    . HIS A 1 568 ? 147.387 160.427 91.762  1.00 37.02 ?  568 HIS A CB    1 
ATOM   4566  C  CG    . HIS A 1 568 ? 147.311 161.385 90.615  1.00 38.46 ?  568 HIS A CG    1 
ATOM   4567  N  ND1   . HIS A 1 568 ? 146.626 161.103 89.454  1.00 42.97 ?  568 HIS A ND1   1 
ATOM   4568  C  CD2   . HIS A 1 568 ? 147.839 162.619 90.451  1.00 38.74 ?  568 HIS A CD2   1 
ATOM   4569  C  CE1   . HIS A 1 568 ? 146.741 162.122 88.621  1.00 42.21 ?  568 HIS A CE1   1 
ATOM   4570  N  NE2   . HIS A 1 568 ? 147.467 163.058 89.205  1.00 41.84 ?  568 HIS A NE2   1 
ATOM   4571  N  N     . GLY A 1 569 ? 148.900 158.920 94.366  1.00 29.47 ?  569 GLY A N     1 
ATOM   4572  C  CA    . GLY A 1 569 ? 148.631 158.178 95.581  1.00 29.61 ?  569 GLY A CA    1 
ATOM   4573  C  C     . GLY A 1 569 ? 147.520 157.160 95.419  1.00 28.19 ?  569 GLY A C     1 
ATOM   4574  O  O     . GLY A 1 569 ? 146.920 156.995 94.358  1.00 33.66 ?  569 GLY A O     1 
ATOM   4575  N  N     . MET A 1 570 ? 147.244 156.459 96.516  1.00 24.21 ?  570 MET A N     1 
ATOM   4576  C  CA    . MET A 1 570 ? 146.220 155.426 96.565  1.00 22.67 ?  570 MET A CA    1 
ATOM   4577  C  C     . MET A 1 570 ? 145.203 155.764 97.643  1.00 24.38 ?  570 MET A C     1 
ATOM   4578  O  O     . MET A 1 570 ? 145.568 156.203 98.737  1.00 31.69 ?  570 MET A O     1 
ATOM   4579  C  CB    . MET A 1 570 ? 146.833 154.050 96.842  1.00 26.83 ?  570 MET A CB    1 
ATOM   4580  C  CG    . MET A 1 570 ? 147.729 153.535 95.735  1.00 24.76 ?  570 MET A CG    1 
ATOM   4581  S  SD    . MET A 1 570 ? 146.878 152.385 94.650  1.00 38.07 ?  570 MET A SD    1 
ATOM   4582  C  CE    . MET A 1 570 ? 146.730 150.974 95.735  1.00 24.88 ?  570 MET A CE    1 
ATOM   4583  N  N     . TYR A 1 571 ? 143.925 155.552 97.332  1.00 15.53 ?  571 TYR A N     1 
ATOM   4584  C  CA    . TYR A 1 571 ? 142.871 155.873 98.285  1.00 9.58  ?  571 TYR A CA    1 
ATOM   4585  C  C     . TYR A 1 571 ? 142.654 154.763 99.304  1.00 18.52 ?  571 TYR A C     1 
ATOM   4586  O  O     . TYR A 1 571 ? 142.311 155.048 100.457 1.00 20.21 ?  571 TYR A O     1 
ATOM   4587  C  CB    . TYR A 1 571 ? 141.566 156.159 97.544  1.00 20.46 ?  571 TYR A CB    1 
ATOM   4588  C  CG    . TYR A 1 571 ? 140.505 156.792 98.409  1.00 24.83 ?  571 TYR A CG    1 
ATOM   4589  C  CD1   . TYR A 1 571 ? 140.574 158.134 98.751  1.00 23.83 ?  571 TYR A CD1   1 
ATOM   4590  C  CD2   . TYR A 1 571 ? 139.436 156.049 98.887  1.00 19.14 ?  571 TYR A CD2   1 
ATOM   4591  C  CE1   . TYR A 1 571 ? 139.610 158.717 99.541  1.00 26.06 ?  571 TYR A CE1   1 
ATOM   4592  C  CE2   . TYR A 1 571 ? 138.469 156.624 99.679  1.00 20.62 ?  571 TYR A CE2   1 
ATOM   4593  C  CZ    . TYR A 1 571 ? 138.558 157.958 100.001 1.00 28.45 ?  571 TYR A CZ    1 
ATOM   4594  O  OH    . TYR A 1 571 ? 137.593 158.537 100.790 1.00 27.40 ?  571 TYR A OH    1 
ATOM   4595  N  N     . HIS A 1 572 ? 142.838 153.509 98.909  1.00 23.11 ?  572 HIS A N     1 
ATOM   4596  C  CA    . HIS A 1 572 ? 142.604 152.364 99.777  1.00 14.41 ?  572 HIS A CA    1 
ATOM   4597  C  C     . HIS A 1 572 ? 143.932 151.731 100.160 1.00 13.07 ?  572 HIS A C     1 
ATOM   4598  O  O     . HIS A 1 572 ? 144.763 151.450 99.292  1.00 26.25 ?  572 HIS A O     1 
ATOM   4599  C  CB    . HIS A 1 572 ? 141.710 151.328 99.094  1.00 14.72 ?  572 HIS A CB    1 
ATOM   4600  C  CG    . HIS A 1 572 ? 140.538 151.918 98.376  1.00 9.11  ?  572 HIS A CG    1 
ATOM   4601  N  ND1   . HIS A 1 572 ? 140.570 152.236 97.037  1.00 18.58 ?  572 HIS A ND1   1 
ATOM   4602  C  CD2   . HIS A 1 572 ? 139.299 152.242 98.810  1.00 15.19 ?  572 HIS A CD2   1 
ATOM   4603  C  CE1   . HIS A 1 572 ? 139.402 152.735 96.677  1.00 19.44 ?  572 HIS A CE1   1 
ATOM   4604  N  NE2   . HIS A 1 572 ? 138.612 152.748 97.735  1.00 24.26 ?  572 HIS A NE2   1 
ATOM   4605  N  N     . SER A 1 573 ? 144.128 151.515 101.462 1.00 8.03  ?  573 SER A N     1 
ATOM   4606  C  CA    . SER A 1 573 ? 145.309 150.788 101.915 1.00 8.56  ?  573 SER A CA    1 
ATOM   4607  C  C     . SER A 1 573 ? 145.281 149.349 101.423 1.00 15.34 ?  573 SER A C     1 
ATOM   4608  O  O     . SER A 1 573 ? 146.314 148.798 101.025 1.00 24.43 ?  573 SER A O     1 
ATOM   4609  C  CB    . SER A 1 573 ? 145.404 150.839 103.438 1.00 12.75 ?  573 SER A CB    1 
ATOM   4610  O  OG    . SER A 1 573 ? 144.157 150.531 104.031 1.00 21.38 ?  573 SER A OG    1 
ATOM   4611  N  N     . TYR A 1 574 ? 144.105 148.727 101.443 1.00 16.85 ?  574 TYR A N     1 
ATOM   4612  C  CA    . TYR A 1 574 ? 143.909 147.372 100.957 1.00 5.31  ?  574 TYR A CA    1 
ATOM   4613  C  C     . TYR A 1 574 ? 142.692 147.357 100.047 1.00 9.09  ?  574 TYR A C     1 
ATOM   4614  O  O     . TYR A 1 574 ? 141.717 148.072 100.294 1.00 13.59 ?  574 TYR A O     1 
ATOM   4615  C  CB    . TYR A 1 574 ? 143.727 146.392 102.118 1.00 12.98 ?  574 TYR A CB    1 
ATOM   4616  C  CG    . TYR A 1 574 ? 144.838 146.475 103.136 1.00 7.77  ?  574 TYR A CG    1 
ATOM   4617  C  CD1   . TYR A 1 574 ? 144.790 147.403 104.166 1.00 6.39  ?  574 TYR A CD1   1 
ATOM   4618  C  CD2   . TYR A 1 574 ? 145.939 145.637 103.062 1.00 10.01 ?  574 TYR A CD2   1 
ATOM   4619  C  CE1   . TYR A 1 574 ? 145.800 147.494 105.090 1.00 9.56  ?  574 TYR A CE1   1 
ATOM   4620  C  CE2   . TYR A 1 574 ? 146.955 145.720 103.988 1.00 17.92 ?  574 TYR A CE2   1 
ATOM   4621  C  CZ    . TYR A 1 574 ? 146.879 146.652 105.000 1.00 8.20  ?  574 TYR A CZ    1 
ATOM   4622  O  OH    . TYR A 1 574 ? 147.884 146.743 105.930 1.00 14.62 ?  574 TYR A OH    1 
ATOM   4623  N  N     . ARG A 1 575 ? 142.754 146.560 98.996  1.00 16.15 ?  575 ARG A N     1 
ATOM   4624  C  CA    . ARG A 1 575 ? 141.678 146.576 98.012  1.00 7.89  ?  575 ARG A CA    1 
ATOM   4625  C  C     . ARG A 1 575 ? 141.064 145.209 97.759  1.00 12.24 ?  575 ARG A C     1 
ATOM   4626  O  O     . ARG A 1 575 ? 139.848 145.113 97.593  1.00 20.45 ?  575 ARG A O     1 
ATOM   4627  C  CB    . ARG A 1 575 ? 142.188 147.153 96.687  1.00 15.51 ?  575 ARG A CB    1 
ATOM   4628  C  CG    . ARG A 1 575 ? 142.728 148.564 96.783  1.00 6.14  ?  575 ARG A CG    1 
ATOM   4629  C  CD    . ARG A 1 575 ? 143.761 148.810 95.703  1.00 12.48 ?  575 ARG A CD    1 
ATOM   4630  N  NE    . ARG A 1 575 ? 145.010 148.115 95.986  1.00 22.24 ?  575 ARG A NE    1 
ATOM   4631  C  CZ    . ARG A 1 575 ? 145.420 147.022 95.360  1.00 14.81 ?  575 ARG A CZ    1 
ATOM   4632  N  NH1   . ARG A 1 575 ? 144.704 146.467 94.398  1.00 16.91 1  575 ARG A NH1   1 
ATOM   4633  N  NH2   . ARG A 1 575 ? 146.577 146.469 95.710  1.00 10.77 ?  575 ARG A NH2   1 
ATOM   4634  N  N     . LEU A 1 576 ? 141.870 144.152 97.723  1.00 20.61 ?  576 LEU A N     1 
ATOM   4635  C  CA    . LEU A 1 576 ? 141.424 142.842 97.275  1.00 8.99  ?  576 LEU A CA    1 
ATOM   4636  C  C     . LEU A 1 576 ? 141.553 141.831 98.403  1.00 6.92  ?  576 LEU A C     1 
ATOM   4637  O  O     . LEU A 1 576 ? 142.627 141.689 98.994  1.00 16.05 ?  576 LEU A O     1 
ATOM   4638  C  CB    . LEU A 1 576 ? 142.235 142.378 96.064  1.00 4.75  ?  576 LEU A CB    1 
ATOM   4639  C  CG    . LEU A 1 576 ? 142.314 143.344 94.882  1.00 10.05 ?  576 LEU A CG    1 
ATOM   4640  C  CD1   . LEU A 1 576 ? 143.262 142.816 93.824  1.00 12.27 ?  576 LEU A CD1   1 
ATOM   4641  C  CD2   . LEU A 1 576 ? 140.938 143.583 94.295  1.00 10.86 ?  576 LEU A CD2   1 
ATOM   4642  N  N     . CYS A 1 577 ? 140.458 141.137 98.695  1.00 5.06  ?  577 CYS A N     1 
ATOM   4643  C  CA    . CYS A 1 577 ? 140.474 139.989 99.589  1.00 3.41  ?  577 CYS A CA    1 
ATOM   4644  C  C     . CYS A 1 577 ? 139.400 139.024 99.112  1.00 17.51 ?  577 CYS A C     1 
ATOM   4645  O  O     . CYS A 1 577 ? 138.285 139.445 98.799  1.00 21.24 ?  577 CYS A O     1 
ATOM   4646  C  CB    . CYS A 1 577 ? 140.245 140.401 101.051 1.00 3.50  ?  577 CYS A CB    1 
ATOM   4647  S  SG    . CYS A 1 577 ? 138.533 140.658 101.569 1.00 32.82 ?  577 CYS A SG    1 
ATOM   4648  N  N     . ILE A 1 578 ? 139.744 137.744 99.034  1.00 15.25 ?  578 ILE A N     1 
ATOM   4649  C  CA    . ILE A 1 578 ? 138.849 136.725 98.500  1.00 10.66 ?  578 ILE A CA    1 
ATOM   4650  C  C     . ILE A 1 578 ? 138.207 136.012 99.683  1.00 4.01  ?  578 ILE A C     1 
ATOM   4651  O  O     . ILE A 1 578 ? 138.818 135.151 100.320 1.00 14.86 ?  578 ILE A O     1 
ATOM   4652  C  CB    . ILE A 1 578 ? 139.582 135.759 97.568  1.00 10.51 ?  578 ILE A CB    1 
ATOM   4653  C  CG1   . ILE A 1 578 ? 140.216 136.533 96.413  1.00 0.00  ?  578 ILE A CG1   1 
ATOM   4654  C  CG2   . ILE A 1 578 ? 138.624 134.721 97.022  1.00 13.45 ?  578 ILE A CG2   1 
ATOM   4655  C  CD1   . ILE A 1 578 ? 140.846 135.662 95.370  1.00 6.95  ?  578 ILE A CD1   1 
ATOM   4656  N  N     . ALA A 1 579 ? 136.964 136.378 99.972  1.00 17.63 ?  579 ALA A N     1 
ATOM   4657  C  CA    . ALA A 1 579 ? 136.193 135.822 101.071 1.00 12.12 ?  579 ALA A CA    1 
ATOM   4658  C  C     . ALA A 1 579 ? 135.540 134.508 100.654 1.00 21.37 ?  579 ALA A C     1 
ATOM   4659  O  O     . ALA A 1 579 ? 135.514 134.160 99.474  1.00 27.27 ?  579 ALA A O     1 
ATOM   4660  C  CB    . ALA A 1 579 ? 135.147 136.840 101.518 1.00 9.65  ?  579 ALA A CB    1 
ATOM   4661  N  N     . PRO A 1 580 ? 135.028 133.731 101.616 1.00 26.58 ?  580 PRO A N     1 
ATOM   4662  C  CA    . PRO A 1 580 ? 134.341 132.479 101.250 1.00 22.98 ?  580 PRO A CA    1 
ATOM   4663  C  C     . PRO A 1 580 ? 133.123 132.667 100.355 1.00 25.85 ?  580 PRO A C     1 
ATOM   4664  O  O     . PRO A 1 580 ? 132.859 131.796 99.518  1.00 33.51 ?  580 PRO A O     1 
ATOM   4665  C  CB    . PRO A 1 580 ? 133.952 131.878 102.611 1.00 23.37 ?  580 PRO A CB    1 
ATOM   4666  C  CG    . PRO A 1 580 ? 134.207 132.945 103.624 1.00 24.80 ?  580 PRO A CG    1 
ATOM   4667  C  CD    . PRO A 1 580 ? 135.275 133.808 103.064 1.00 21.17 ?  580 PRO A CD    1 
ATOM   4668  N  N     . THR A 1 581 ? 132.384 133.767 100.497 1.00 22.49 ?  581 THR A N     1 
ATOM   4669  C  CA    . THR A 1 581 ? 131.176 134.040 99.707  1.00 33.36 ?  581 THR A CA    1 
ATOM   4670  C  C     . THR A 1 581 ? 130.195 132.866 99.776  1.00 31.70 ?  581 THR A C     1 
ATOM   4671  O  O     . THR A 1 581 ? 129.895 132.203 98.784  1.00 32.03 ?  581 THR A O     1 
ATOM   4672  C  CB    . THR A 1 581 ? 131.513 134.373 98.248  1.00 32.67 ?  581 THR A CB    1 
ATOM   4673  O  OG1   . THR A 1 581 ? 131.571 133.165 97.479  1.00 26.83 ?  581 THR A OG1   1 
ATOM   4674  C  CG2   . THR A 1 581 ? 132.832 135.116 98.142  1.00 30.85 ?  581 THR A CG2   1 
ATOM   4675  N  N     . GLY A 1 582 ? 129.702 132.631 100.989 1.00 35.50 ?  582 GLY A N     1 
ATOM   4676  C  CA    . GLY A 1 582 ? 128.913 131.448 101.269 1.00 32.59 ?  582 GLY A CA    1 
ATOM   4677  C  C     . GLY A 1 582 ? 127.569 131.352 100.574 1.00 35.28 ?  582 GLY A C     1 
ATOM   4678  O  O     . GLY A 1 582 ? 127.376 130.481 99.720  1.00 37.33 ?  582 GLY A O     1 
ATOM   4679  N  N     . SER A 1 583 ? 126.632 132.236 100.915 1.00 37.73 ?  583 SER A N     1 
ATOM   4680  C  CA    . SER A 1 583 ? 125.261 132.097 100.439 1.00 38.50 ?  583 SER A CA    1 
ATOM   4681  C  C     . SER A 1 583 ? 124.962 132.907 99.186  1.00 36.64 ?  583 SER A C     1 
ATOM   4682  O  O     . SER A 1 583 ? 124.011 132.578 98.469  1.00 38.67 ?  583 SER A O     1 
ATOM   4683  C  CB    . SER A 1 583 ? 124.276 132.501 101.541 1.00 42.09 ?  583 SER A CB    1 
ATOM   4684  O  OG    . SER A 1 583 ? 122.997 131.936 101.312 1.00 39.94 ?  583 SER A OG    1 
ATOM   4685  N  N     . ILE A 1 584 ? 125.740 133.954 98.902  1.00 33.14 ?  584 ILE A N     1 
ATOM   4686  C  CA    . ILE A 1 584 ? 125.516 134.723 97.685  1.00 31.28 ?  584 ILE A CA    1 
ATOM   4687  C  C     . ILE A 1 584 ? 125.941 133.949 96.446  1.00 33.16 ?  584 ILE A C     1 
ATOM   4688  O  O     . ILE A 1 584 ? 125.602 134.345 95.325  1.00 40.10 ?  584 ILE A O     1 
ATOM   4689  C  CB    . ILE A 1 584 ? 126.247 136.077 97.751  1.00 34.85 ?  584 ILE A CB    1 
ATOM   4690  C  CG1   . ILE A 1 584 ? 127.718 135.874 98.118  1.00 34.66 ?  584 ILE A CG1   1 
ATOM   4691  C  CG2   . ILE A 1 584 ? 125.559 137.008 98.735  1.00 33.01 ?  584 ILE A CG2   1 
ATOM   4692  C  CD1   . ILE A 1 584 ? 128.541 137.142 98.072  1.00 33.24 ?  584 ILE A CD1   1 
ATOM   4693  N  N     . SER A 1 585 ? 126.684 132.853 96.617  1.00 32.18 ?  585 SER A N     1 
ATOM   4694  C  CA    . SER A 1 585 ? 127.082 132.042 95.474  1.00 29.46 ?  585 SER A CA    1 
ATOM   4695  C  C     . SER A 1 585 ? 125.888 131.341 94.840  1.00 31.36 ?  585 SER A C     1 
ATOM   4696  O  O     . SER A 1 585 ? 125.862 131.147 93.620  1.00 33.66 ?  585 SER A O     1 
ATOM   4697  C  CB    . SER A 1 585 ? 128.138 131.023 95.898  1.00 29.82 ?  585 SER A CB    1 
ATOM   4698  O  OG    . SER A 1 585 ? 127.699 130.271 97.014  1.00 35.57 ?  585 SER A OG    1 
ATOM   4699  N  N     . TYR A 1 586 ? 124.901 130.945 95.647  1.00 31.83 ?  586 TYR A N     1 
ATOM   4700  C  CA    . TYR A 1 586 ? 123.681 130.370 95.093  1.00 33.16 ?  586 TYR A CA    1 
ATOM   4701  C  C     . TYR A 1 586 ? 122.922 131.397 94.265  1.00 32.37 ?  586 TYR A C     1 
ATOM   4702  O  O     . TYR A 1 586 ? 122.510 131.116 93.135  1.00 39.34 ?  586 TYR A O     1 
ATOM   4703  C  CB    . TYR A 1 586 ? 122.791 129.837 96.214  1.00 33.29 ?  586 TYR A CB    1 
ATOM   4704  C  CG    . TYR A 1 586 ? 123.400 128.718 97.020  1.00 34.35 ?  586 TYR A CG    1 
ATOM   4705  C  CD1   . TYR A 1 586 ? 123.334 127.405 96.580  1.00 35.32 ?  586 TYR A CD1   1 
ATOM   4706  C  CD2   . TYR A 1 586 ? 124.028 128.972 98.230  1.00 31.34 ?  586 TYR A CD2   1 
ATOM   4707  C  CE1   . TYR A 1 586 ? 123.885 126.379 97.317  1.00 36.39 ?  586 TYR A CE1   1 
ATOM   4708  C  CE2   . TYR A 1 586 ? 124.581 127.953 98.974  1.00 33.62 ?  586 TYR A CE2   1 
ATOM   4709  C  CZ    . TYR A 1 586 ? 124.508 126.658 98.513  1.00 37.41 ?  586 TYR A CZ    1 
ATOM   4710  O  OH    . TYR A 1 586 ? 125.058 125.639 99.253  1.00 40.64 ?  586 TYR A OH    1 
ATOM   4711  N  N     . VAL A 1 587 ? 122.742 132.601 94.814  1.00 29.24 ?  587 VAL A N     1 
ATOM   4712  C  CA    . VAL A 1 587 ? 121.985 133.645 94.130  1.00 27.25 ?  587 VAL A CA    1 
ATOM   4713  C  C     . VAL A 1 587 ? 122.636 133.992 92.799  1.00 30.87 ?  587 VAL A C     1 
ATOM   4714  O  O     . VAL A 1 587 ? 121.953 134.167 91.782  1.00 33.39 ?  587 VAL A O     1 
ATOM   4715  C  CB    . VAL A 1 587 ? 121.856 134.883 95.038  1.00 29.69 ?  587 VAL A CB    1 
ATOM   4716  C  CG1   . VAL A 1 587 ? 121.253 136.048 94.276  1.00 30.93 ?  587 VAL A CG1   1 
ATOM   4717  C  CG2   . VAL A 1 587 ? 121.026 134.552 96.264  1.00 31.47 ?  587 VAL A CG2   1 
ATOM   4718  N  N     . GLN A 1 588 ? 123.961 134.089 92.781  1.00 32.92 ?  588 GLN A N     1 
ATOM   4719  C  CA    . GLN A 1 588 ? 124.695 134.397 91.563  1.00 29.21 ?  588 GLN A CA    1 
ATOM   4720  C  C     . GLN A 1 588 ? 124.895 133.183 90.671  1.00 28.76 ?  588 GLN A C     1 
ATOM   4721  O  O     . GLN A 1 588 ? 125.459 133.327 89.581  1.00 31.83 ?  588 GLN A O     1 
ATOM   4722  C  CB    . GLN A 1 588 ? 126.054 135.004 91.910  1.00 26.58 ?  588 GLN A CB    1 
ATOM   4723  C  CG    . GLN A 1 588 ? 125.985 136.425 92.428  1.00 24.83 ?  588 GLN A CG    1 
ATOM   4724  C  CD    . GLN A 1 588 ? 126.209 137.447 91.336  1.00 27.77 ?  588 GLN A CD    1 
ATOM   4725  O  OE1   . GLN A 1 588 ? 127.055 137.262 90.464  1.00 29.67 ?  588 GLN A OE1   1 
ATOM   4726  N  NE2   . GLN A 1 588 ? 125.456 138.537 91.381  1.00 29.68 ?  588 GLN A NE2   1 
ATOM   4727  N  N     . SER A 1 589 ? 124.446 132.006 91.104  1.00 32.59 ?  589 SER A N     1 
ATOM   4728  C  CA    . SER A 1 589 ? 124.648 130.753 90.383  1.00 29.72 ?  589 SER A CA    1 
ATOM   4729  C  C     . SER A 1 589 ? 126.130 130.562 90.067  1.00 32.19 ?  589 SER A C     1 
ATOM   4730  O  O     . SER A 1 589 ? 126.550 130.458 88.914  1.00 30.48 ?  589 SER A O     1 
ATOM   4731  C  CB    . SER A 1 589 ? 123.792 130.702 89.116  1.00 30.42 ?  589 SER A CB    1 
ATOM   4732  O  OG    . SER A 1 589 ? 123.450 129.366 88.791  1.00 40.48 ?  589 SER A OG    1 
ATOM   4733  N  N     . SER A 1 590 ? 126.923 130.530 91.133  1.00 33.30 ?  590 SER A N     1 
ATOM   4734  C  CA    . SER A 1 590 ? 128.371 130.510 91.023  1.00 26.43 ?  590 SER A CA    1 
ATOM   4735  C  C     . SER A 1 590 ? 128.946 129.562 92.062  1.00 27.25 ?  590 SER A C     1 
ATOM   4736  O  O     . SER A 1 590 ? 128.338 129.320 93.108  1.00 31.48 ?  590 SER A O     1 
ATOM   4737  C  CB    . SER A 1 590 ? 128.958 131.914 91.211  1.00 23.21 ?  590 SER A CB    1 
ATOM   4738  O  OG    . SER A 1 590 ? 129.377 132.114 92.547  1.00 32.45 ?  590 SER A OG    1 
ATOM   4739  N  N     . THR A 1 591 ? 130.120 129.018 91.760  1.00 27.43 ?  591 THR A N     1 
ATOM   4740  C  CA    . THR A 1 591 ? 130.848 128.236 92.746  1.00 22.38 ?  591 THR A CA    1 
ATOM   4741  C  C     . THR A 1 591 ? 131.417 129.155 93.821  1.00 27.07 ?  591 THR A C     1 
ATOM   4742  O  O     . THR A 1 591 ? 131.739 130.319 93.569  1.00 25.19 ?  591 THR A O     1 
ATOM   4743  C  CB    . THR A 1 591 ? 131.966 127.432 92.083  1.00 25.20 ?  591 THR A CB    1 
ATOM   4744  O  OG1   . THR A 1 591 ? 132.984 128.321 91.610  1.00 33.06 ?  591 THR A OG1   1 
ATOM   4745  C  CG2   . THR A 1 591 ? 131.420 126.635 90.915  1.00 25.62 ?  591 THR A CG2   1 
ATOM   4746  N  N     . ALA A 1 592 ? 131.535 128.622 95.032  1.00 26.79 ?  592 ALA A N     1 
ATOM   4747  C  CA    . ALA A 1 592 ? 131.905 129.439 96.179  1.00 24.60 ?  592 ALA A CA    1 
ATOM   4748  C  C     . ALA A 1 592 ? 133.370 129.848 96.090  1.00 28.69 ?  592 ALA A C     1 
ATOM   4749  O  O     . ALA A 1 592 ? 134.262 128.992 96.085  1.00 31.31 ?  592 ALA A O     1 
ATOM   4750  C  CB    . ALA A 1 592 ? 131.641 128.679 97.475  1.00 28.80 ?  592 ALA A CB    1 
ATOM   4751  N  N     . SER A 1 593 ? 133.609 131.154 96.020  1.00 27.10 ?  593 SER A N     1 
ATOM   4752  C  CA    . SER A 1 593 ? 134.950 131.749 96.080  1.00 11.59 ?  593 SER A CA    1 
ATOM   4753  C  C     . SER A 1 593 ? 135.792 131.201 94.925  1.00 13.13 ?  593 SER A C     1 
ATOM   4754  O  O     . SER A 1 593 ? 135.256 130.794 93.886  1.00 27.44 ?  593 SER A O     1 
ATOM   4755  C  CB    . SER A 1 593 ? 135.537 131.515 97.461  1.00 28.10 ?  593 SER A CB    1 
ATOM   4756  O  OG    . SER A 1 593 ? 136.760 132.204 97.628  1.00 29.10 ?  593 SER A OG    1 
ATOM   4757  N  N     . VAL A 1 594 ? 137.116 131.198 95.090  1.00 23.32 ?  594 VAL A N     1 
ATOM   4758  C  CA    . VAL A 1 594 ? 138.022 130.614 94.110  1.00 19.82 ?  594 VAL A CA    1 
ATOM   4759  C  C     . VAL A 1 594 ? 138.388 129.179 94.451  1.00 14.86 ?  594 VAL A C     1 
ATOM   4760  O  O     . VAL A 1 594 ? 139.218 128.577 93.759  1.00 17.59 ?  594 VAL A O     1 
ATOM   4761  C  CB    . VAL A 1 594 ? 139.292 131.475 93.958  1.00 18.67 ?  594 VAL A CB    1 
ATOM   4762  C  CG1   . VAL A 1 594 ? 138.951 132.805 93.309  1.00 11.94 ?  594 VAL A CG1   1 
ATOM   4763  C  CG2   . VAL A 1 594 ? 139.949 131.696 95.307  1.00 18.42 ?  594 VAL A CG2   1 
ATOM   4764  N  N     . MET A 1 595 ? 137.793 128.617 95.499  1.00 22.05 ?  595 MET A N     1 
ATOM   4765  C  CA    . MET A 1 595 ? 138.045 127.236 95.866  1.00 20.53 ?  595 MET A CA    1 
ATOM   4766  C  C     . MET A 1 595 ? 137.299 126.285 94.932  1.00 23.58 ?  595 MET A C     1 
ATOM   4767  O  O     . MET A 1 595 ? 136.279 126.651 94.343  1.00 25.01 ?  595 MET A O     1 
ATOM   4768  C  CB    . MET A 1 595 ? 137.618 126.990 97.313  1.00 22.89 ?  595 MET A CB    1 
ATOM   4769  C  CG    . MET A 1 595 ? 138.767 126.783 98.302  1.00 21.47 ?  595 MET A CG    1 
ATOM   4770  S  SD    . MET A 1 595 ? 140.252 127.767 98.014  1.00 30.92 ?  595 MET A SD    1 
ATOM   4771  C  CE    . MET A 1 595 ? 139.621 129.437 98.128  1.00 31.89 ?  595 MET A CE    1 
ATOM   4772  N  N     . PRO A 1 596 ? 137.798 125.063 94.770  1.00 30.79 ?  596 PRO A N     1 
ATOM   4773  C  CA    . PRO A 1 596 ? 137.082 124.075 93.959  1.00 20.09 ?  596 PRO A CA    1 
ATOM   4774  C  C     . PRO A 1 596 ? 135.813 123.595 94.646  1.00 25.96 ?  596 PRO A C     1 
ATOM   4775  O  O     . PRO A 1 596 ? 135.645 123.703 95.862  1.00 30.13 ?  596 PRO A O     1 
ATOM   4776  C  CB    . PRO A 1 596 ? 138.096 122.938 93.807  1.00 23.39 ?  596 PRO A CB    1 
ATOM   4777  C  CG    . PRO A 1 596 ? 138.992 123.079 94.985  1.00 29.22 ?  596 PRO A CG    1 
ATOM   4778  C  CD    . PRO A 1 596 ? 139.083 124.544 95.268  1.00 28.42 ?  596 PRO A CD    1 
ATOM   4779  N  N     . ILE A 1 597 ? 134.906 123.055 93.830  1.00 27.79 ?  597 ILE A N     1 
ATOM   4780  C  CA    . ILE A 1 597 ? 133.619 122.597 94.334  1.00 30.69 ?  597 ILE A CA    1 
ATOM   4781  C  C     . ILE A 1 597 ? 133.804 121.365 95.210  1.00 31.57 ?  597 ILE A C     1 
ATOM   4782  O  O     . ILE A 1 597 ? 134.718 120.555 95.007  1.00 31.34 ?  597 ILE A O     1 
ATOM   4783  C  CB    . ILE A 1 597 ? 132.653 122.307 93.170  1.00 31.28 ?  597 ILE A CB    1 
ATOM   4784  C  CG1   . ILE A 1 597 ? 133.119 121.080 92.383  1.00 27.57 ?  597 ILE A CG1   1 
ATOM   4785  C  CG2   . ILE A 1 597 ? 132.546 123.509 92.262  1.00 29.49 ?  597 ILE A CG2   1 
ATOM   4786  C  CD1   . ILE A 1 597 ? 132.000 120.273 91.786  1.00 28.63 ?  597 ILE A CD1   1 
ATOM   4787  N  N     . MET A 1 598 ? 132.923 121.219 96.197  1.00 40.39 ?  598 MET A N     1 
ATOM   4788  C  CA    . MET A 1 598 ? 132.944 120.060 97.078  1.00 41.34 ?  598 MET A CA    1 
ATOM   4789  C  C     . MET A 1 598 ? 132.110 118.909 96.533  1.00 40.72 ?  598 MET A C     1 
ATOM   4790  O  O     . MET A 1 598 ? 132.549 117.755 96.569  1.00 44.88 ?  598 MET A O     1 
ATOM   4791  C  CB    . MET A 1 598 ? 132.447 120.451 98.471  1.00 42.03 ?  598 MET A CB    1 
ATOM   4792  C  CG    . MET A 1 598 ? 132.979 121.784 98.964  1.00 39.71 ?  598 MET A CG    1 
ATOM   4793  S  SD    . MET A 1 598 ? 132.851 121.981 100.751 1.00 57.19 ?  598 MET A SD    1 
ATOM   4794  C  CE    . MET A 1 598 ? 131.524 120.840 101.129 1.00 44.70 ?  598 MET A CE    1 
ATOM   4795  N  N     . GLU A 1 599 ? 130.910 119.199 96.032  1.00 41.01 ?  599 GLU A N     1 
ATOM   4796  C  CA    . GLU A 1 599 ? 130.030 118.201 95.443  1.00 39.32 ?  599 GLU A CA    1 
ATOM   4797  C  C     . GLU A 1 599 ? 129.575 118.680 94.075  1.00 38.14 ?  599 GLU A C     1 
ATOM   4798  O  O     . GLU A 1 599 ? 129.305 119.869 93.886  1.00 42.33 ?  599 GLU A O     1 
ATOM   4799  C  CB    . GLU A 1 599 ? 128.805 117.935 96.329  1.00 42.81 ?  599 GLU A CB    1 
ATOM   4800  C  CG    . GLU A 1 599 ? 129.079 118.012 97.820  1.00 44.35 ?  599 GLU A CG    1 
ATOM   4801  C  CD    . GLU A 1 599 ? 127.809 118.013 98.649  1.00 48.19 ?  599 GLU A CD    1 
ATOM   4802  O  OE1   . GLU A 1 599 ? 127.162 116.951 98.749  1.00 47.76 ?  599 GLU A OE1   1 
ATOM   4803  O  OE2   . GLU A 1 599 ? 127.460 119.076 99.202  1.00 45.85 -1 599 GLU A OE2   1 
ATOM   4804  N  N     . ARG A 1 600 ? 129.496 117.752 93.118  1.00 41.41 ?  600 ARG A N     1 
ATOM   4805  C  CA    . ARG A 1 600 ? 128.969 118.099 91.802  1.00 36.75 ?  600 ARG A CA    1 
ATOM   4806  C  C     . ARG A 1 600 ? 127.489 118.449 91.886  1.00 37.88 ?  600 ARG A C     1 
ATOM   4807  O  O     . ARG A 1 600 ? 127.050 119.474 91.353  1.00 41.00 ?  600 ARG A O     1 
ATOM   4808  C  CB    . ARG A 1 600 ? 129.193 116.948 90.824  1.00 36.61 ?  600 ARG A CB    1 
ATOM   4809  C  CG    . ARG A 1 600 ? 130.591 116.889 90.250  1.00 36.23 ?  600 ARG A CG    1 
ATOM   4810  C  CD    . ARG A 1 600 ? 130.660 115.908 89.102  1.00 36.48 ?  600 ARG A CD    1 
ATOM   4811  N  NE    . ARG A 1 600 ? 132.029 115.645 88.677  1.00 35.63 ?  600 ARG A NE    1 
ATOM   4812  C  CZ    . ARG A 1 600 ? 132.840 114.774 89.261  1.00 38.66 ?  600 ARG A CZ    1 
ATOM   4813  N  NH1   . ARG A 1 600 ? 132.457 114.077 90.316  1.00 37.64 1  600 ARG A NH1   1 
ATOM   4814  N  NH2   . ARG A 1 600 ? 134.064 114.600 88.774  1.00 39.46 ?  600 ARG A NH2   1 
ATOM   4815  N  N     . ILE A 1 601 ? 126.708 117.603 92.547  1.00 45.37 ?  601 ILE A N     1 
ATOM   4816  C  CA    . ILE A 1 601 ? 125.308 117.876 92.846  1.00 43.26 ?  601 ILE A CA    1 
ATOM   4817  C  C     . ILE A 1 601 ? 125.182 117.938 94.360  1.00 42.50 ?  601 ILE A C     1 
ATOM   4818  O  O     . ILE A 1 601 ? 125.486 116.961 95.054  1.00 46.73 ?  601 ILE A O     1 
ATOM   4819  C  CB    . ILE A 1 601 ? 124.371 116.813 92.255  1.00 42.87 ?  601 ILE A CB    1 
ATOM   4820  C  CG1   . ILE A 1 601 ? 124.707 116.570 90.783  1.00 43.32 ?  601 ILE A CG1   1 
ATOM   4821  C  CG2   . ILE A 1 601 ? 122.922 117.246 92.401  1.00 42.85 ?  601 ILE A CG2   1 
ATOM   4822  C  CD1   . ILE A 1 601 ? 123.857 115.513 90.127  1.00 43.38 ?  601 ILE A CD1   1 
ATOM   4823  N  N     . GLU A 1 602 ? 124.738 119.080 94.867  1.00 49.62 ?  602 GLU A N     1 
ATOM   4824  C  CA    . GLU A 1 602 ? 124.717 119.346 96.297  1.00 49.44 ?  602 GLU A CA    1 
ATOM   4825  C  C     . GLU A 1 602 ? 123.320 119.063 96.837  1.00 51.45 ?  602 GLU A C     1 
ATOM   4826  O  O     . GLU A 1 602 ? 122.344 119.680 96.401  1.00 53.93 ?  602 GLU A O     1 
ATOM   4827  C  CB    . GLU A 1 602 ? 125.134 120.788 96.578  1.00 49.41 ?  602 GLU A CB    1 
ATOM   4828  C  CG    . GLU A 1 602 ? 124.687 121.327 97.918  1.00 50.26 ?  602 GLU A CG    1 
ATOM   4829  C  CD    . GLU A 1 602 ? 124.954 122.811 98.056  1.00 54.59 ?  602 GLU A CD    1 
ATOM   4830  O  OE1   . GLU A 1 602 ? 125.947 123.293 97.472  1.00 52.32 ?  602 GLU A OE1   1 
ATOM   4831  O  OE2   . GLU A 1 602 ? 124.172 123.495 98.749  1.00 56.03 -1 602 GLU A OE2   1 
ATOM   4832  N  N     . GLU A 1 603 ? 123.232 118.129 97.779  1.00 56.98 ?  603 GLU A N     1 
ATOM   4833  C  CA    . GLU A 1 603 ? 121.967 117.722 98.374  1.00 57.36 ?  603 GLU A CA    1 
ATOM   4834  C  C     . GLU A 1 603 ? 121.797 118.412 99.721  1.00 58.62 ?  603 GLU A C     1 
ATOM   4835  O  O     . GLU A 1 603 ? 122.674 118.322 100.585 1.00 58.60 ?  603 GLU A O     1 
ATOM   4836  C  CB    . GLU A 1 603 ? 121.911 116.204 98.544  1.00 59.38 ?  603 GLU A CB    1 
ATOM   4837  C  CG    . GLU A 1 603 ? 120.616 115.689 99.145  1.00 60.68 ?  603 GLU A CG    1 
ATOM   4838  C  CD    . GLU A 1 603 ? 120.709 114.236 99.571  1.00 61.55 ?  603 GLU A CD    1 
ATOM   4839  O  OE1   . GLU A 1 603 ? 120.716 113.353 98.689  1.00 60.08 ?  603 GLU A OE1   1 
ATOM   4840  O  OE2   . GLU A 1 603 ? 120.777 113.976 100.791 1.00 59.52 -1 603 GLU A OE2   1 
ATOM   4841  N  N     . ARG A 1 604 ? 120.668 119.095 99.895  1.00 61.77 ?  604 ARG A N     1 
ATOM   4842  C  CA    . ARG A 1 604 ? 120.371 119.818 101.120 1.00 61.85 ?  604 ARG A CA    1 
ATOM   4843  C  C     . ARG A 1 604 ? 118.950 119.513 101.564 1.00 62.69 ?  604 ARG A C     1 
ATOM   4844  O  O     . ARG A 1 604 ? 118.090 119.161 100.753 1.00 64.24 ?  604 ARG A O     1 
ATOM   4845  C  CB    . ARG A 1 604 ? 120.536 121.333 100.940 1.00 59.98 ?  604 ARG A CB    1 
ATOM   4846  C  CG    . ARG A 1 604 ? 121.938 121.781 100.567 1.00 61.07 ?  604 ARG A CG    1 
ATOM   4847  C  CD    . ARG A 1 604 ? 122.898 121.622 101.732 1.00 62.30 ?  604 ARG A CD    1 
ATOM   4848  N  NE    . ARG A 1 604 ? 123.878 120.570 101.492 1.00 63.37 ?  604 ARG A NE    1 
ATOM   4849  C  CZ    . ARG A 1 604 ? 125.170 120.786 101.283 1.00 62.57 ?  604 ARG A CZ    1 
ATOM   4850  N  NH1   . ARG A 1 604 ? 125.675 122.008 101.281 1.00 61.28 1  604 ARG A NH1   1 
ATOM   4851  N  NH2   . ARG A 1 604 ? 125.975 119.750 101.069 1.00 60.05 ?  604 ARG A NH2   1 
ATOM   4852  N  N     . THR A 1 605 ? 118.712 119.650 102.865 1.00 68.82 ?  605 THR A N     1 
ATOM   4853  C  CA    . THR A 1 605 ? 117.385 119.493 103.448 1.00 70.06 ?  605 THR A CA    1 
ATOM   4854  C  C     . THR A 1 605 ? 116.993 120.804 104.113 1.00 69.42 ?  605 THR A C     1 
ATOM   4855  O  O     . THR A 1 605 ? 117.656 121.247 105.056 1.00 69.58 ?  605 THR A O     1 
ATOM   4856  C  CB    . THR A 1 605 ? 117.355 118.346 104.461 1.00 70.54 ?  605 THR A CB    1 
ATOM   4857  O  OG1   . THR A 1 605 ? 118.242 117.305 104.036 1.00 71.33 ?  605 THR A OG1   1 
ATOM   4858  C  CG2   . THR A 1 605 ? 115.948 117.784 104.581 1.00 69.20 ?  605 THR A CG2   1 
ATOM   4859  N  N     . TYR A 1 606 ? 115.921 121.419 103.623 1.00 68.76 ?  606 TYR A N     1 
ATOM   4860  C  CA    . TYR A 1 606 ? 115.401 122.666 104.172 1.00 71.10 ?  606 TYR A CA    1 
ATOM   4861  C  C     . TYR A 1 606 ? 114.060 122.363 104.826 1.00 72.93 ?  606 TYR A C     1 
ATOM   4862  O  O     . TYR A 1 606 ? 113.086 122.040 104.136 1.00 70.59 ?  606 TYR A O     1 
ATOM   4863  C  CB    . TYR A 1 606 ? 115.268 123.730 103.085 1.00 69.38 ?  606 TYR A CB    1 
ATOM   4864  C  CG    . TYR A 1 606 ? 116.595 124.180 102.519 1.00 70.30 ?  606 TYR A CG    1 
ATOM   4865  C  CD1   . TYR A 1 606 ? 117.381 125.109 103.188 1.00 68.23 ?  606 TYR A CD1   1 
ATOM   4866  C  CD2   . TYR A 1 606 ? 117.067 123.668 101.319 1.00 69.45 ?  606 TYR A CD2   1 
ATOM   4867  C  CE1   . TYR A 1 606 ? 118.597 125.517 102.674 1.00 68.83 ?  606 TYR A CE1   1 
ATOM   4868  C  CE2   . TYR A 1 606 ? 118.279 124.071 100.797 1.00 67.17 ?  606 TYR A CE2   1 
ATOM   4869  C  CZ    . TYR A 1 606 ? 119.040 124.993 101.479 1.00 70.11 ?  606 TYR A CZ    1 
ATOM   4870  O  OH    . TYR A 1 606 ? 120.249 125.395 100.960 1.00 70.97 ?  606 TYR A OH    1 
ATOM   4871  N  N     . GLY A 1 607 ? 114.009 122.473 106.147 1.00 80.04 ?  607 GLY A N     1 
ATOM   4872  C  CA    . GLY A 1 607 ? 112.820 122.052 106.869 1.00 78.48 ?  607 GLY A CA    1 
ATOM   4873  C  C     . GLY A 1 607 ? 112.615 120.560 106.698 1.00 78.34 ?  607 GLY A C     1 
ATOM   4874  O  O     . GLY A 1 607 ? 113.518 119.752 106.949 1.00 78.36 ?  607 GLY A O     1 
ATOM   4875  N  N     . ASN A 1 608 ? 111.416 120.175 106.260 1.00 79.97 ?  608 ASN A N     1 
ATOM   4876  C  CA    . ASN A 1 608 ? 111.095 118.785 105.970 1.00 81.03 ?  608 ASN A CA    1 
ATOM   4877  C  C     . ASN A 1 608 ? 111.116 118.491 104.474 1.00 80.88 ?  608 ASN A C     1 
ATOM   4878  O  O     . ASN A 1 608 ? 110.465 117.548 104.013 1.00 80.73 ?  608 ASN A O     1 
ATOM   4879  C  CB    . ASN A 1 608 ? 109.735 118.418 106.567 1.00 80.47 ?  608 ASN A CB    1 
ATOM   4880  C  CG    . ASN A 1 608 ? 109.699 118.575 108.076 1.00 81.27 ?  608 ASN A CG    1 
ATOM   4881  O  OD1   . ASN A 1 608 ? 110.739 118.679 108.727 1.00 80.58 ?  608 ASN A OD1   1 
ATOM   4882  N  ND2   . ASN A 1 608 ? 108.497 118.592 108.640 1.00 80.54 ?  608 ASN A ND2   1 
ATOM   4883  N  N     . SER A 1 609 ? 111.860 119.284 103.707 1.00 77.90 ?  609 SER A N     1 
ATOM   4884  C  CA    . SER A 1 609 ? 111.945 119.142 102.261 1.00 77.94 ?  609 SER A CA    1 
ATOM   4885  C  C     . SER A 1 609 ? 113.394 118.924 101.851 1.00 77.93 ?  609 SER A C     1 
ATOM   4886  O  O     . SER A 1 609 ? 114.298 119.602 102.347 1.00 78.15 ?  609 SER A O     1 
ATOM   4887  C  CB    . SER A 1 609 ? 111.385 120.379 101.554 1.00 76.58 ?  609 SER A CB    1 
ATOM   4888  O  OG    . SER A 1 609 ? 112.136 121.536 101.880 1.00 77.68 ?  609 SER A OG    1 
ATOM   4889  N  N     . LYS A 1 610 ? 113.606 117.979 100.940 1.00 66.97 ?  610 LYS A N     1 
ATOM   4890  C  CA    . LYS A 1 610 ? 114.931 117.654 100.430 1.00 66.32 ?  610 LYS A CA    1 
ATOM   4891  C  C     . LYS A 1 610 ? 115.044 118.130 98.989  1.00 66.53 ?  610 LYS A C     1 
ATOM   4892  O  O     . LYS A 1 610 ? 114.187 117.816 98.157  1.00 67.67 ?  610 LYS A O     1 
ATOM   4893  C  CB    . LYS A 1 610 ? 115.197 116.151 100.518 1.00 66.92 ?  610 LYS A CB    1 
ATOM   4894  C  CG    . LYS A 1 610 ? 116.204 115.632 99.505  1.00 66.39 ?  610 LYS A CG    1 
ATOM   4895  C  CD    . LYS A 1 610 ? 116.840 114.333 99.973  1.00 66.95 ?  610 LYS A CD    1 
ATOM   4896  C  CE    . LYS A 1 610 ? 117.338 114.439 101.406 1.00 66.22 ?  610 LYS A CE    1 
ATOM   4897  N  NZ    . LYS A 1 610 ? 118.330 115.537 101.568 1.00 66.39 1  610 LYS A NZ    1 
ATOM   4898  N  N     . THR A 1 611 ? 116.100 118.887 98.699  1.00 64.78 ?  611 THR A N     1 
ATOM   4899  C  CA    . THR A 1 611 ? 116.308 119.457 97.376  1.00 63.63 ?  611 THR A CA    1 
ATOM   4900  C  C     . THR A 1 611 ? 117.774 119.326 96.995  1.00 62.02 ?  611 THR A C     1 
ATOM   4901  O  O     . THR A 1 611 ? 118.653 119.280 97.858  1.00 61.18 ?  611 THR A O     1 
ATOM   4902  C  CB    . THR A 1 611 ? 115.879 120.927 97.324  1.00 64.51 ?  611 THR A CB    1 
ATOM   4903  O  OG1   . THR A 1 611 ? 116.307 121.506 96.085  1.00 68.33 ?  611 THR A OG1   1 
ATOM   4904  C  CG2   . THR A 1 611 ? 116.487 121.696 98.482  1.00 61.51 ?  611 THR A CG2   1 
ATOM   4905  N  N     . TYR A 1 612 ? 118.028 119.268 95.691  1.00 55.17 ?  612 TYR A N     1 
ATOM   4906  C  CA    . TYR A 1 612 ? 119.364 119.035 95.164  1.00 53.75 ?  612 TYR A CA    1 
ATOM   4907  C  C     . TYR A 1 612 ? 119.797 120.213 94.305  1.00 55.99 ?  612 TYR A C     1 
ATOM   4908  O  O     . TYR A 1 612 ? 119.003 120.761 93.534  1.00 55.12 ?  612 TYR A O     1 
ATOM   4909  C  CB    . TYR A 1 612 ? 119.437 117.740 94.339  1.00 56.44 ?  612 TYR A CB    1 
ATOM   4910  C  CG    . TYR A 1 612 ? 118.934 116.497 95.047  1.00 58.31 ?  612 TYR A CG    1 
ATOM   4911  C  CD1   . TYR A 1 612 ? 117.590 116.340 95.363  1.00 57.73 ?  612 TYR A CD1   1 
ATOM   4912  C  CD2   . TYR A 1 612 ? 119.813 115.493 95.423  1.00 57.67 ?  612 TYR A CD2   1 
ATOM   4913  C  CE1   . TYR A 1 612 ? 117.135 115.210 96.012  1.00 58.44 ?  612 TYR A CE1   1 
ATOM   4914  C  CE2   . TYR A 1 612 ? 119.368 114.360 96.073  1.00 58.52 ?  612 TYR A CE2   1 
ATOM   4915  C  CZ    . TYR A 1 612 ? 118.028 114.225 96.365  1.00 60.23 ?  612 TYR A CZ    1 
ATOM   4916  O  OH    . TYR A 1 612 ? 117.581 113.097 97.015  1.00 60.85 ?  612 TYR A OH    1 
ATOM   4917  N  N     . TYR A 1 613 ? 121.064 120.595 94.443  1.00 51.49 ?  613 TYR A N     1 
ATOM   4918  C  CA    . TYR A 1 613 ? 121.637 121.720 93.703  1.00 42.49 ?  613 TYR A CA    1 
ATOM   4919  C  C     . TYR A 1 613 ? 122.815 121.259 92.860  1.00 41.14 ?  613 TYR A C     1 
ATOM   4920  O  O     . TYR A 1 613 ? 123.929 121.088 93.386  1.00 44.64 ?  613 TYR A O     1 
ATOM   4921  C  CB    . TYR A 1 613 ? 122.074 122.828 94.658  1.00 41.40 ?  613 TYR A CB    1 
ATOM   4922  C  CG    . TYR A 1 613 ? 122.697 124.015 93.961  1.00 41.89 ?  613 TYR A CG    1 
ATOM   4923  C  CD1   . TYR A 1 613 ? 122.080 124.607 92.869  1.00 42.79 ?  613 TYR A CD1   1 
ATOM   4924  C  CD2   . TYR A 1 613 ? 123.903 124.545 94.397  1.00 42.04 ?  613 TYR A CD2   1 
ATOM   4925  C  CE1   . TYR A 1 613 ? 122.643 125.692 92.232  1.00 43.12 ?  613 TYR A CE1   1 
ATOM   4926  C  CE2   . TYR A 1 613 ? 124.476 125.630 93.766  1.00 43.78 ?  613 TYR A CE2   1 
ATOM   4927  C  CZ    . TYR A 1 613 ? 123.841 126.200 92.685  1.00 46.61 ?  613 TYR A CZ    1 
ATOM   4928  O  OH    . TYR A 1 613 ? 124.405 127.282 92.052  1.00 46.20 ?  613 TYR A OH    1 
ATOM   4929  N  N     . PRO A 1 614 ? 122.628 121.039 91.563  1.00 40.55 ?  614 PRO A N     1 
ATOM   4930  C  CA    . PRO A 1 614 ? 123.781 120.802 90.692  1.00 40.16 ?  614 PRO A CA    1 
ATOM   4931  C  C     . PRO A 1 614 ? 124.652 122.043 90.608  1.00 40.09 ?  614 PRO A C     1 
ATOM   4932  O  O     . PRO A 1 614 ? 124.177 123.174 90.746  1.00 43.40 ?  614 PRO A O     1 
ATOM   4933  C  CB    . PRO A 1 614 ? 123.149 120.473 89.333  1.00 37.04 ?  614 PRO A CB    1 
ATOM   4934  C  CG    . PRO A 1 614 ? 121.695 120.244 89.607  1.00 43.01 ?  614 PRO A CG    1 
ATOM   4935  C  CD    . PRO A 1 614 ? 121.362 121.047 90.816  1.00 42.07 ?  614 PRO A CD    1 
ATOM   4936  N  N     . MET A 1 615 ? 125.944 121.823 90.390  1.00 37.48 ?  615 MET A N     1 
ATOM   4937  C  CA    . MET A 1 615 ? 126.860 122.939 90.253  1.00 37.01 ?  615 MET A CA    1 
ATOM   4938  C  C     . MET A 1 615 ? 126.490 123.764 89.022  1.00 41.63 ?  615 MET A C     1 
ATOM   4939  O  O     . MET A 1 615 ? 125.985 123.223 88.034  1.00 38.54 ?  615 MET A O     1 
ATOM   4940  C  CB    . MET A 1 615 ? 128.299 122.443 90.152  1.00 33.82 ?  615 MET A CB    1 
ATOM   4941  C  CG    . MET A 1 615 ? 128.964 122.241 91.501  1.00 36.13 ?  615 MET A CG    1 
ATOM   4942  S  SD    . MET A 1 615 ? 128.537 123.535 92.682  1.00 52.76 ?  615 MET A SD    1 
ATOM   4943  C  CE    . MET A 1 615 ? 127.598 122.605 93.890  1.00 35.65 ?  615 MET A CE    1 
ATOM   4944  N  N     . PRO A 1 616 ? 126.698 125.078 89.068  1.00 40.49 ?  616 PRO A N     1 
ATOM   4945  C  CA    . PRO A 1 616 ? 126.275 125.934 87.952  1.00 35.85 ?  616 PRO A CA    1 
ATOM   4946  C  C     . PRO A 1 616 ? 126.926 125.515 86.643  1.00 36.86 ?  616 PRO A C     1 
ATOM   4947  O  O     . PRO A 1 616 ? 128.150 125.419 86.540  1.00 38.67 ?  616 PRO A O     1 
ATOM   4948  C  CB    . PRO A 1 616 ? 126.731 127.328 88.389  1.00 36.67 ?  616 PRO A CB    1 
ATOM   4949  C  CG    . PRO A 1 616 ? 126.788 127.249 89.876  1.00 38.59 ?  616 PRO A CG    1 
ATOM   4950  C  CD    . PRO A 1 616 ? 127.232 125.861 90.195  1.00 35.46 ?  616 PRO A CD    1 
ATOM   4951  N  N     . GLY A 1 617 ? 126.092 125.272 85.637  1.00 36.72 ?  617 GLY A N     1 
ATOM   4952  C  CA    . GLY A 1 617 ? 126.573 124.837 84.345  1.00 31.13 ?  617 GLY A CA    1 
ATOM   4953  C  C     . GLY A 1 617 ? 126.935 123.374 84.253  1.00 38.40 ?  617 GLY A C     1 
ATOM   4954  O  O     . GLY A 1 617 ? 127.491 122.956 83.231  1.00 40.80 ?  617 GLY A O     1 
ATOM   4955  N  N     . LEU A 1 618 ? 126.648 122.583 85.285  1.00 39.29 ?  618 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 618 ? 126.986 121.167 85.256  1.00 34.62 ?  618 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 618 ? 126.161 120.443 84.201  1.00 39.88 ?  618 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 618 ? 124.958 120.671 84.059  1.00 40.59 ?  618 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 618 ? 126.757 120.533 86.628  1.00 34.82 ?  618 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 618 ? 127.072 119.043 86.771  1.00 37.41 ?  618 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 618 ? 128.537 118.760 86.478  1.00 34.92 ?  618 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 618 ? 126.696 118.541 88.155  1.00 35.44 ?  618 LEU A CD2   1 
ATOM   4963  N  N     . ALA A 1 619 ? 126.823 119.564 83.458  1.00 43.40 ?  619 ALA A N     1 
ATOM   4964  C  CA    . ALA A 1 619 ? 126.192 118.781 82.406  1.00 43.12 ?  619 ALA A CA    1 
ATOM   4965  C  C     . ALA A 1 619 ? 127.022 117.519 82.209  1.00 44.84 ?  619 ALA A C     1 
ATOM   4966  O  O     . ALA A 1 619 ? 127.890 117.195 83.026  1.00 50.01 ?  619 ALA A O     1 
ATOM   4967  C  CB    . ALA A 1 619 ? 126.062 119.597 81.116  1.00 41.78 ?  619 ALA A CB    1 
ATOM   4968  N  N     . SER A 1 620 ? 126.754 116.799 81.120  1.00 50.05 ?  620 SER A N     1 
ATOM   4969  C  CA    . SER A 1 620 ? 127.558 115.627 80.800  1.00 50.39 ?  620 SER A CA    1 
ATOM   4970  C  C     . SER A 1 620 ? 128.803 115.996 80.005  1.00 50.52 ?  620 SER A C     1 
ATOM   4971  O  O     . SER A 1 620 ? 129.785 115.247 80.017  1.00 54.16 ?  620 SER A O     1 
ATOM   4972  C  CB    . SER A 1 620 ? 126.720 114.609 80.026  1.00 53.17 ?  620 SER A CB    1 
ATOM   4973  O  OG    . SER A 1 620 ? 125.557 114.254 80.753  1.00 55.31 ?  620 SER A OG    1 
ATOM   4974  N  N     . ASN A 1 621 ? 128.782 117.138 79.315  1.00 48.00 ?  621 ASN A N     1 
ATOM   4975  C  CA    . ASN A 1 621 ? 129.940 117.547 78.528  1.00 48.37 ?  621 ASN A CA    1 
ATOM   4976  C  C     . ASN A 1 621 ? 131.048 118.117 79.404  1.00 51.61 ?  621 ASN A C     1 
ATOM   4977  O  O     . ASN A 1 621 ? 132.203 118.189 78.969  1.00 51.96 ?  621 ASN A O     1 
ATOM   4978  C  CB    . ASN A 1 621 ? 129.520 118.566 77.469  1.00 49.02 ?  621 ASN A CB    1 
ATOM   4979  C  CG    . ASN A 1 621 ? 129.486 119.983 78.004  1.00 51.03 ?  621 ASN A CG    1 
ATOM   4980  O  OD1   . ASN A 1 621 ? 128.611 120.340 78.793  1.00 50.38 ?  621 ASN A OD1   1 
ATOM   4981  N  ND2   . ASN A 1 621 ? 130.439 120.801 77.575  1.00 47.50 ?  621 ASN A ND2   1 
ATOM   4982  N  N     . ASN A 1 622 ? 130.725 118.528 80.630  1.00 44.03 ?  622 ASN A N     1 
ATOM   4983  C  CA    . ASN A 1 622 ? 131.709 119.060 81.566  1.00 40.24 ?  622 ASN A CA    1 
ATOM   4984  C  C     . ASN A 1 622 ? 131.574 118.420 82.944  1.00 42.76 ?  622 ASN A C     1 
ATOM   4985  O  O     . ASN A 1 622 ? 131.880 119.047 83.960  1.00 48.61 ?  622 ASN A O     1 
ATOM   4986  C  CB    . ASN A 1 622 ? 131.603 120.584 81.659  1.00 42.91 ?  622 ASN A CB    1 
ATOM   4987  C  CG    . ASN A 1 622 ? 130.214 121.062 82.054  1.00 42.30 ?  622 ASN A CG    1 
ATOM   4988  O  OD1   . ASN A 1 622 ? 129.495 120.397 82.797  1.00 43.38 ?  622 ASN A OD1   1 
ATOM   4989  N  ND2   . ASN A 1 622 ? 129.834 122.232 81.557  1.00 41.97 ?  622 ASN A ND2   1 
ATOM   4990  N  N     . TRP A 1 623 ? 131.106 117.171 82.989  1.00 37.70 ?  623 TRP A N     1 
ATOM   4991  C  CA    . TRP A 1 623 ? 130.939 116.490 84.268  1.00 38.13 ?  623 TRP A CA    1 
ATOM   4992  C  C     . TRP A 1 623 ? 132.277 116.267 84.960  1.00 38.97 ?  623 TRP A C     1 
ATOM   4993  O  O     . TRP A 1 623 ? 132.400 116.484 86.172  1.00 36.89 ?  623 TRP A O     1 
ATOM   4994  C  CB    . TRP A 1 623 ? 130.219 115.158 84.057  1.00 41.13 ?  623 TRP A CB    1 
ATOM   4995  C  CG    . TRP A 1 623 ? 130.099 114.330 85.298  1.00 37.94 ?  623 TRP A CG    1 
ATOM   4996  C  CD1   . TRP A 1 623 ? 130.976 113.384 85.738  1.00 37.18 ?  623 TRP A CD1   1 
ATOM   4997  C  CD2   . TRP A 1 623 ? 129.036 114.367 86.255  1.00 36.34 ?  623 TRP A CD2   1 
ATOM   4998  N  NE1   . TRP A 1 623 ? 130.529 112.833 86.913  1.00 37.99 ?  623 TRP A NE1   1 
ATOM   4999  C  CE2   . TRP A 1 623 ? 129.337 113.417 87.250  1.00 38.89 ?  623 TRP A CE2   1 
ATOM   5000  C  CE3   . TRP A 1 623 ? 127.858 115.110 86.367  1.00 37.48 ?  623 TRP A CE3   1 
ATOM   5001  C  CZ2   . TRP A 1 623 ? 128.506 113.195 88.344  1.00 37.40 ?  623 TRP A CZ2   1 
ATOM   5002  C  CZ3   . TRP A 1 623 ? 127.034 114.887 87.453  1.00 38.40 ?  623 TRP A CZ3   1 
ATOM   5003  C  CH2   . TRP A 1 623 ? 127.362 113.938 88.427  1.00 37.73 ?  623 TRP A CH2   1 
ATOM   5004  N  N     . PHE A 1 624 ? 133.290 115.833 84.214  1.00 43.16 ?  624 PHE A N     1 
ATOM   5005  C  CA    . PHE A 1 624 ? 134.579 115.513 84.809  1.00 41.82 ?  624 PHE A CA    1 
ATOM   5006  C  C     . PHE A 1 624 ? 135.481 116.726 84.975  1.00 42.59 ?  624 PHE A C     1 
ATOM   5007  O  O     . PHE A 1 624 ? 136.480 116.642 85.699  1.00 50.03 ?  624 PHE A O     1 
ATOM   5008  C  CB    . PHE A 1 624 ? 135.287 114.442 83.976  1.00 41.56 ?  624 PHE A CB    1 
ATOM   5009  C  CG    . PHE A 1 624 ? 134.591 113.112 84.000  1.00 45.32 ?  624 PHE A CG    1 
ATOM   5010  C  CD1   . PHE A 1 624 ? 134.576 112.348 85.155  1.00 42.10 ?  624 PHE A CD1   1 
ATOM   5011  C  CD2   . PHE A 1 624 ? 133.934 112.635 82.878  1.00 44.92 ?  624 PHE A CD2   1 
ATOM   5012  C  CE1   . PHE A 1 624 ? 133.931 111.129 85.187  1.00 41.33 ?  624 PHE A CE1   1 
ATOM   5013  C  CE2   . PHE A 1 624 ? 133.287 111.417 82.905  1.00 42.77 ?  624 PHE A CE2   1 
ATOM   5014  C  CZ    . PHE A 1 624 ? 133.285 110.663 84.060  1.00 45.45 ?  624 PHE A CZ    1 
ATOM   5015  N  N     . PHE A 1 625 ? 135.157 117.848 84.332  1.00 34.98 ?  625 PHE A N     1 
ATOM   5016  C  CA    . PHE A 1 625 ? 135.843 119.095 84.641  1.00 32.84 ?  625 PHE A CA    1 
ATOM   5017  C  C     . PHE A 1 625 ? 135.373 119.685 85.961  1.00 32.46 ?  625 PHE A C     1 
ATOM   5018  O  O     . PHE A 1 625 ? 136.087 120.501 86.552  1.00 36.35 ?  625 PHE A O     1 
ATOM   5019  C  CB    . PHE A 1 625 ? 135.650 120.106 83.513  1.00 31.54 ?  625 PHE A CB    1 
ATOM   5020  C  CG    . PHE A 1 625 ? 136.407 119.769 82.265  1.00 30.72 ?  625 PHE A CG    1 
ATOM   5021  C  CD1   . PHE A 1 625 ? 137.789 119.764 82.262  1.00 33.14 ?  625 PHE A CD1   1 
ATOM   5022  C  CD2   . PHE A 1 625 ? 135.738 119.464 81.092  1.00 34.06 ?  625 PHE A CD2   1 
ATOM   5023  C  CE1   . PHE A 1 625 ? 138.492 119.459 81.116  1.00 36.70 ?  625 PHE A CE1   1 
ATOM   5024  C  CE2   . PHE A 1 625 ? 136.436 119.159 79.943  1.00 32.14 ?  625 PHE A CE2   1 
ATOM   5025  C  CZ    . PHE A 1 625 ? 137.814 119.155 79.955  1.00 36.32 ?  625 PHE A CZ    1 
ATOM   5026  N  N     . TYR A 1 626 ? 134.193 119.292 86.432  1.00 29.43 ?  626 TYR A N     1 
ATOM   5027  C  CA    . TYR A 1 626 ? 133.708 119.682 87.754  1.00 31.49 ?  626 TYR A CA    1 
ATOM   5028  C  C     . TYR A 1 626 ? 134.190 118.706 88.821  1.00 27.64 ?  626 TYR A C     1 
ATOM   5029  O  O     . TYR A 1 626 ? 133.412 118.176 89.609  1.00 30.79 ?  626 TYR A O     1 
ATOM   5030  C  CB    . TYR A 1 626 ? 132.188 119.775 87.744  1.00 32.51 ?  626 TYR A CB    1 
ATOM   5031  C  CG    . TYR A 1 626 ? 131.667 121.154 87.430  1.00 28.67 ?  626 TYR A CG    1 
ATOM   5032  C  CD1   . TYR A 1 626 ? 131.816 122.194 88.334  1.00 32.63 ?  626 TYR A CD1   1 
ATOM   5033  C  CD2   . TYR A 1 626 ? 131.028 121.417 86.227  1.00 30.61 ?  626 TYR A CD2   1 
ATOM   5034  C  CE1   . TYR A 1 626 ? 131.343 123.456 88.050  1.00 29.49 ?  626 TYR A CE1   1 
ATOM   5035  C  CE2   . TYR A 1 626 ? 130.552 122.675 85.934  1.00 28.96 ?  626 TYR A CE2   1 
ATOM   5036  C  CZ    . TYR A 1 626 ? 130.713 123.690 86.850  1.00 27.83 ?  626 TYR A CZ    1 
ATOM   5037  O  OH    . TYR A 1 626 ? 130.242 124.948 86.568  1.00 34.46 ?  626 TYR A OH    1 
ATOM   5038  N  N     . LYS A 1 627 ? 135.498 118.472 88.842  1.00 31.50 ?  627 LYS A N     1 
ATOM   5039  C  CA    . LYS A 1 627 ? 136.084 117.544 89.797  1.00 31.57 ?  627 LYS A CA    1 
ATOM   5040  C  C     . LYS A 1 627 ? 135.885 118.054 91.217  1.00 31.68 ?  627 LYS A C     1 
ATOM   5041  O  O     . LYS A 1 627 ? 136.108 119.234 91.504  1.00 35.85 ?  627 LYS A O     1 
ATOM   5042  C  CB    . LYS A 1 627 ? 137.570 117.362 89.494  1.00 34.95 ?  627 LYS A CB    1 
ATOM   5043  C  CG    . LYS A 1 627 ? 138.263 116.308 90.329  1.00 34.41 ?  627 LYS A CG    1 
ATOM   5044  C  CD    . LYS A 1 627 ? 139.660 116.041 89.802  1.00 32.48 ?  627 LYS A CD    1 
ATOM   5045  C  CE    . LYS A 1 627 ? 140.381 115.009 90.643  1.00 38.41 ?  627 LYS A CE    1 
ATOM   5046  N  NZ    . LYS A 1 627 ? 141.804 114.871 90.234  1.00 39.70 1  627 LYS A NZ    1 
ATOM   5047  N  N     . GLU A 1 628 ? 135.456 117.164 92.105  1.00 35.59 ?  628 GLU A N     1 
ATOM   5048  C  CA    . GLU A 1 628 ? 135.223 117.552 93.488  1.00 36.22 ?  628 GLU A CA    1 
ATOM   5049  C  C     . GLU A 1 628 ? 136.540 117.877 94.183  1.00 39.79 ?  628 GLU A C     1 
ATOM   5050  O  O     . GLU A 1 628 ? 137.596 117.331 93.854  1.00 42.87 ?  628 GLU A O     1 
ATOM   5051  C  CB    . GLU A 1 628 ? 134.485 116.444 94.236  1.00 37.35 ?  628 GLU A CB    1 
ATOM   5052  C  CG    . GLU A 1 628 ? 133.093 116.163 93.696  1.00 39.53 ?  628 GLU A CG    1 
ATOM   5053  C  CD    . GLU A 1 628 ? 132.319 115.186 94.558  1.00 47.64 ?  628 GLU A CD    1 
ATOM   5054  O  OE1   . GLU A 1 628 ? 132.770 114.900 95.687  1.00 43.85 ?  628 GLU A OE1   1 
ATOM   5055  O  OE2   . GLU A 1 628 ? 131.257 114.708 94.108  1.00 44.12 -1 628 GLU A OE2   1 
ATOM   5056  N  N     . ALA A 1 629 ? 136.464 118.789 95.155  1.00 38.57 ?  629 ALA A N     1 
ATOM   5057  C  CA    . ALA A 1 629 ? 137.667 119.257 95.835  1.00 34.48 ?  629 ALA A CA    1 
ATOM   5058  C  C     . ALA A 1 629 ? 138.353 118.144 96.612  1.00 37.29 ?  629 ALA A C     1 
ATOM   5059  O  O     . ALA A 1 629 ? 139.571 118.189 96.814  1.00 44.58 ?  629 ALA A O     1 
ATOM   5060  C  CB    . ALA A 1 629 ? 137.319 120.414 96.768  1.00 35.14 ?  629 ALA A CB    1 
ATOM   5061  N  N     . TYR A 1 630 ? 137.597 117.147 97.069  1.00 42.65 ?  630 TYR A N     1 
ATOM   5062  C  CA    . TYR A 1 630 ? 138.196 116.073 97.851  1.00 41.94 ?  630 TYR A CA    1 
ATOM   5063  C  C     . TYR A 1 630 ? 138.992 115.110 96.979  1.00 44.19 ?  630 TYR A C     1 
ATOM   5064  O  O     . TYR A 1 630 ? 139.935 114.477 97.465  1.00 44.91 ?  630 TYR A O     1 
ATOM   5065  C  CB    . TYR A 1 630 ? 137.114 115.323 98.622  1.00 39.33 ?  630 TYR A CB    1 
ATOM   5066  C  CG    . TYR A 1 630 ? 136.348 116.193 99.588  1.00 40.78 ?  630 TYR A CG    1 
ATOM   5067  C  CD1   . TYR A 1 630 ? 136.901 116.563 100.805 1.00 38.92 ?  630 TYR A CD1   1 
ATOM   5068  C  CD2   . TYR A 1 630 ? 135.072 116.644 99.283  1.00 40.39 ?  630 TYR A CD2   1 
ATOM   5069  C  CE1   . TYR A 1 630 ? 136.205 117.356 101.691 1.00 39.65 ?  630 TYR A CE1   1 
ATOM   5070  C  CE2   . TYR A 1 630 ? 134.369 117.438 100.164 1.00 40.55 ?  630 TYR A CE2   1 
ATOM   5071  C  CZ    . TYR A 1 630 ? 134.940 117.790 101.367 1.00 44.72 ?  630 TYR A CZ    1 
ATOM   5072  O  OH    . TYR A 1 630 ? 134.245 118.581 102.250 1.00 48.31 ?  630 TYR A OH    1 
ATOM   5073  N  N     . ASP A 1 631 ? 138.637 114.990 95.702  1.00 40.74 ?  631 ASP A N     1 
ATOM   5074  C  CA    . ASP A 1 631 ? 139.303 114.046 94.815  1.00 39.43 ?  631 ASP A CA    1 
ATOM   5075  C  C     . ASP A 1 631 ? 140.575 114.598 94.186  1.00 43.72 ?  631 ASP A C     1 
ATOM   5076  O  O     . ASP A 1 631 ? 141.300 113.838 93.536  1.00 46.48 ?  631 ASP A O     1 
ATOM   5077  C  CB    . ASP A 1 631 ? 138.346 113.602 93.705  1.00 42.42 ?  631 ASP A CB    1 
ATOM   5078  C  CG    . ASP A 1 631 ? 136.992 113.178 94.236  1.00 49.41 ?  631 ASP A CG    1 
ATOM   5079  O  OD1   . ASP A 1 631 ? 136.945 112.519 95.295  1.00 48.62 ?  631 ASP A OD1   1 
ATOM   5080  O  OD2   . ASP A 1 631 ? 135.973 113.503 93.591  1.00 51.07 -1 631 ASP A OD2   1 
ATOM   5081  N  N     . MET A 1 632 ? 140.869 115.883 94.357  1.00 39.69 ?  632 MET A N     1 
ATOM   5082  C  CA    . MET A 1 632 ? 142.022 116.492 93.714  1.00 37.62 ?  632 MET A CA    1 
ATOM   5083  C  C     . MET A 1 632 ? 143.187 116.634 94.684  1.00 36.03 ?  632 MET A C     1 
ATOM   5084  O  O     . MET A 1 632 ? 143.025 116.590 95.906  1.00 38.98 ?  632 MET A O     1 
ATOM   5085  C  CB    . MET A 1 632 ? 141.666 117.859 93.127  1.00 37.51 ?  632 MET A CB    1 
ATOM   5086  C  CG    . MET A 1 632 ? 140.722 118.694 93.951  1.00 39.98 ?  632 MET A CG    1 
ATOM   5087  S  SD    . MET A 1 632 ? 140.465 120.314 93.210  1.00 47.46 ?  632 MET A SD    1 
ATOM   5088  C  CE    . MET A 1 632 ? 139.336 119.910 91.884  1.00 33.77 ?  632 MET A CE    1 
ATOM   5089  N  N     . ASP A 1 633 ? 144.375 116.807 94.113  1.00 34.02 ?  633 ASP A N     1 
ATOM   5090  C  CA    . ASP A 1 633 ? 145.589 116.981 94.899  1.00 30.19 ?  633 ASP A CA    1 
ATOM   5091  C  C     . ASP A 1 633 ? 145.579 118.349 95.570  1.00 28.33 ?  633 ASP A C     1 
ATOM   5092  O  O     . ASP A 1 633 ? 145.434 119.377 94.900  1.00 30.74 ?  633 ASP A O     1 
ATOM   5093  C  CB    . ASP A 1 633 ? 146.814 116.833 94.000  1.00 26.25 ?  633 ASP A CB    1 
ATOM   5094  C  CG    . ASP A 1 633 ? 148.102 116.680 94.784  1.00 38.00 ?  633 ASP A CG    1 
ATOM   5095  O  OD1   . ASP A 1 633 ? 148.042 116.591 96.029  1.00 39.38 ?  633 ASP A OD1   1 
ATOM   5096  O  OD2   . ASP A 1 633 ? 149.178 116.654 94.153  1.00 36.15 -1 633 ASP A OD2   1 
ATOM   5097  N  N     . MET A 1 634 ? 145.733 118.364 96.895  1.00 26.57 ?  634 MET A N     1 
ATOM   5098  C  CA    . MET A 1 634 ? 145.794 119.629 97.615  1.00 23.16 ?  634 MET A CA    1 
ATOM   5099  C  C     . MET A 1 634 ? 147.052 120.421 97.288  1.00 25.24 ?  634 MET A C     1 
ATOM   5100  O  O     . MET A 1 634 ? 147.072 121.635 97.502  1.00 26.06 ?  634 MET A O     1 
ATOM   5101  C  CB    . MET A 1 634 ? 145.703 119.391 99.122  1.00 23.97 ?  634 MET A CB    1 
ATOM   5102  C  CG    . MET A 1 634 ? 144.281 119.277 99.638  1.00 29.04 ?  634 MET A CG    1 
ATOM   5103  S  SD    . MET A 1 634 ? 143.267 120.692 99.166  1.00 38.84 ?  634 MET A SD    1 
ATOM   5104  C  CE    . MET A 1 634 ? 142.041 119.894 98.133  1.00 28.17 ?  634 MET A CE    1 
ATOM   5105  N  N     . PHE A 1 635 ? 148.097 119.767 96.775  1.00 24.58 ?  635 PHE A N     1 
ATOM   5106  C  CA    . PHE A 1 635 ? 149.276 120.505 96.336  1.00 21.50 ?  635 PHE A CA    1 
ATOM   5107  C  C     . PHE A 1 635 ? 148.957 121.381 95.130  1.00 21.21 ?  635 PHE A C     1 
ATOM   5108  O  O     . PHE A 1 635 ? 149.411 122.528 95.051  1.00 26.87 ?  635 PHE A O     1 
ATOM   5109  C  CB    . PHE A 1 635 ? 150.414 119.536 96.018  1.00 20.93 ?  635 PHE A CB    1 
ATOM   5110  C  CG    . PHE A 1 635 ? 151.271 119.201 97.206  1.00 27.72 ?  635 PHE A CG    1 
ATOM   5111  C  CD1   . PHE A 1 635 ? 150.706 119.017 98.456  1.00 22.95 ?  635 PHE A CD1   1 
ATOM   5112  C  CD2   . PHE A 1 635 ? 152.642 119.074 97.073  1.00 23.97 ?  635 PHE A CD2   1 
ATOM   5113  C  CE1   . PHE A 1 635 ? 151.491 118.712 99.548  1.00 23.47 ?  635 PHE A CE1   1 
ATOM   5114  C  CE2   . PHE A 1 635 ? 153.431 118.769 98.163  1.00 26.52 ?  635 PHE A CE2   1 
ATOM   5115  C  CZ    . PHE A 1 635 ? 152.854 118.587 99.402  1.00 24.17 ?  635 PHE A CZ    1 
ATOM   5116  N  N     . LYS A 1 636 ? 148.158 120.870 94.193  1.00 26.05 ?  636 LYS A N     1 
ATOM   5117  C  CA    . LYS A 1 636 ? 147.781 121.672 93.033  1.00 24.89 ?  636 LYS A CA    1 
ATOM   5118  C  C     . LYS A 1 636 ? 146.803 122.779 93.410  1.00 23.61 ?  636 LYS A C     1 
ATOM   5119  O  O     . LYS A 1 636 ? 146.852 123.872 92.833  1.00 31.09 ?  636 LYS A O     1 
ATOM   5120  C  CB    . LYS A 1 636 ? 147.194 120.771 91.949  1.00 27.32 ?  636 LYS A CB    1 
ATOM   5121  C  CG    . LYS A 1 636 ? 148.168 119.713 91.454  1.00 27.16 ?  636 LYS A CG    1 
ATOM   5122  C  CD    . LYS A 1 636 ? 148.220 119.660 89.940  1.00 30.50 ?  636 LYS A CD    1 
ATOM   5123  C  CE    . LYS A 1 636 ? 148.050 118.239 89.431  1.00 32.33 ?  636 LYS A CE    1 
ATOM   5124  N  NZ    . LYS A 1 636 ? 148.197 118.163 87.952  1.00 32.76 1  636 LYS A NZ    1 
ATOM   5125  N  N     . VAL A 1 637 ? 145.925 122.529 94.382  1.00 20.12 ?  637 VAL A N     1 
ATOM   5126  C  CA    . VAL A 1 637 ? 145.053 123.589 94.880  1.00 17.76 ?  637 VAL A CA    1 
ATOM   5127  C  C     . VAL A 1 637 ? 145.876 124.664 95.581  1.00 23.34 ?  637 VAL A C     1 
ATOM   5128  O  O     . VAL A 1 637 ? 145.591 125.861 95.459  1.00 26.50 ?  637 VAL A O     1 
ATOM   5129  C  CB    . VAL A 1 637 ? 143.972 123.001 95.804  1.00 21.56 ?  637 VAL A CB    1 
ATOM   5130  C  CG1   . VAL A 1 637 ? 143.002 124.083 96.247  1.00 23.10 ?  637 VAL A CG1   1 
ATOM   5131  C  CG2   . VAL A 1 637 ? 143.232 121.877 95.101  1.00 24.87 ?  637 VAL A CG2   1 
ATOM   5132  N  N     . VAL A 1 638 ? 146.907 124.256 96.326  1.00 26.37 ?  638 VAL A N     1 
ATOM   5133  C  CA    . VAL A 1 638 ? 147.817 125.218 96.938  1.00 21.65 ?  638 VAL A CA    1 
ATOM   5134  C  C     . VAL A 1 638 ? 148.522 126.031 95.863  1.00 18.06 ?  638 VAL A C     1 
ATOM   5135  O  O     . VAL A 1 638 ? 148.692 127.247 95.996  1.00 31.86 ?  638 VAL A O     1 
ATOM   5136  C  CB    . VAL A 1 638 ? 148.828 124.498 97.852  1.00 21.89 ?  638 VAL A CB    1 
ATOM   5137  C  CG1   . VAL A 1 638 ? 150.053 125.366 98.076  1.00 15.98 ?  638 VAL A CG1   1 
ATOM   5138  C  CG2   . VAL A 1 638 ? 148.188 124.132 99.174  1.00 22.01 ?  638 VAL A CG2   1 
ATOM   5139  N  N     . ASP A 1 639 ? 148.947 125.371 94.786  1.00 13.54 ?  639 ASP A N     1 
ATOM   5140  C  CA    . ASP A 1 639 ? 149.576 126.080 93.677  1.00 16.83 ?  639 ASP A CA    1 
ATOM   5141  C  C     . ASP A 1 639 ? 148.632 127.115 93.080  1.00 24.01 ?  639 ASP A C     1 
ATOM   5142  O  O     . ASP A 1 639 ? 149.038 128.246 92.795  1.00 29.17 ?  639 ASP A O     1 
ATOM   5143  C  CB    . ASP A 1 639 ? 150.019 125.083 92.606  1.00 15.86 ?  639 ASP A CB    1 
ATOM   5144  C  CG    . ASP A 1 639 ? 151.267 124.323 92.997  1.00 29.95 ?  639 ASP A CG    1 
ATOM   5145  O  OD1   . ASP A 1 639 ? 152.164 124.928 93.621  1.00 34.26 ?  639 ASP A OD1   1 
ATOM   5146  O  OD2   . ASP A 1 639 ? 151.352 123.117 92.686  1.00 34.71 -1 639 ASP A OD2   1 
ATOM   5147  N  N     . MET A 1 640 ? 147.364 126.748 92.897  1.00 23.60 ?  640 MET A N     1 
ATOM   5148  C  CA    . MET A 1 640 ? 146.389 127.682 92.342  1.00 21.42 ?  640 MET A CA    1 
ATOM   5149  C  C     . MET A 1 640 ? 146.165 128.871 93.271  1.00 22.11 ?  640 MET A C     1 
ATOM   5150  O  O     . MET A 1 640 ? 146.151 130.028 92.831  1.00 25.58 ?  640 MET A O     1 
ATOM   5151  C  CB    . MET A 1 640 ? 145.074 126.953 92.070  1.00 24.83 ?  640 MET A CB    1 
ATOM   5152  C  CG    . MET A 1 640 ? 143.885 127.869 91.853  1.00 24.53 ?  640 MET A CG    1 
ATOM   5153  S  SD    . MET A 1 640 ? 143.945 128.718 90.268  1.00 27.79 ?  640 MET A SD    1 
ATOM   5154  C  CE    . MET A 1 640 ? 142.927 127.637 89.274  1.00 26.13 ?  640 MET A CE    1 
ATOM   5155  N  N     . ILE A 1 641 ? 145.997 128.604 94.568  1.00 21.70 ?  641 ILE A N     1 
ATOM   5156  C  CA    . ILE A 1 641 ? 145.731 129.681 95.516  1.00 16.23 ?  641 ILE A CA    1 
ATOM   5157  C  C     . ILE A 1 641 ? 146.944 130.593 95.645  1.00 18.08 ?  641 ILE A C     1 
ATOM   5158  O  O     . ILE A 1 641 ? 146.807 131.812 95.793  1.00 25.78 ?  641 ILE A O     1 
ATOM   5159  C  CB    . ILE A 1 641 ? 145.294 129.104 96.875  1.00 24.77 ?  641 ILE A CB    1 
ATOM   5160  C  CG1   . ILE A 1 641 ? 144.031 128.259 96.714  1.00 23.13 ?  641 ILE A CG1   1 
ATOM   5161  C  CG2   . ILE A 1 641 ? 145.036 130.215 97.877  1.00 16.45 ?  641 ILE A CG2   1 
ATOM   5162  C  CD1   . ILE A 1 641 ? 142.937 128.939 95.927  1.00 19.77 ?  641 ILE A CD1   1 
ATOM   5163  N  N     . ALA A 1 642 ? 148.149 130.024 95.582  1.00 13.80 ?  642 ALA A N     1 
ATOM   5164  C  CA    . ALA A 1 642 ? 149.358 130.834 95.629  1.00 14.95 ?  642 ALA A CA    1 
ATOM   5165  C  C     . ALA A 1 642 ? 149.531 131.654 94.359  1.00 15.06 ?  642 ALA A C     1 
ATOM   5166  O  O     . ALA A 1 642 ? 150.056 132.772 94.412  1.00 24.85 ?  642 ALA A O     1 
ATOM   5167  C  CB    . ALA A 1 642 ? 150.576 129.943 95.858  1.00 16.20 ?  642 ALA A CB    1 
ATOM   5168  N  N     . THR A 1 643 ? 149.112 131.115 93.213  1.00 17.82 ?  643 THR A N     1 
ATOM   5169  C  CA    . THR A 1 643 ? 149.107 131.905 91.988  1.00 20.13 ?  643 THR A CA    1 
ATOM   5170  C  C     . THR A 1 643 ? 148.151 133.084 92.105  1.00 18.40 ?  643 THR A C     1 
ATOM   5171  O  O     . THR A 1 643 ? 148.479 134.205 91.701  1.00 22.42 ?  643 THR A O     1 
ATOM   5172  C  CB    . THR A 1 643 ? 148.735 131.023 90.798  1.00 22.01 ?  643 THR A CB    1 
ATOM   5173  O  OG1   . THR A 1 643 ? 149.749 130.029 90.606  1.00 28.71 ?  643 THR A OG1   1 
ATOM   5174  C  CG2   . THR A 1 643 ? 148.609 131.854 89.536  1.00 17.65 ?  643 THR A CG2   1 
ATOM   5175  N  N     . ILE A 1 644 ? 146.963 132.852 92.666  1.00 16.05 ?  644 ILE A N     1 
ATOM   5176  C  CA    . ILE A 1 644 ? 146.022 133.947 92.868  1.00 14.62 ?  644 ILE A CA    1 
ATOM   5177  C  C     . ILE A 1 644 ? 146.526 134.897 93.950  1.00 17.27 ?  644 ILE A C     1 
ATOM   5178  O  O     . ILE A 1 644 ? 146.380 136.120 93.836  1.00 22.60 ?  644 ILE A O     1 
ATOM   5179  C  CB    . ILE A 1 644 ? 144.623 133.400 93.202  1.00 15.77 ?  644 ILE A CB    1 
ATOM   5180  C  CG1   . ILE A 1 644 ? 144.106 132.519 92.066  1.00 14.71 ?  644 ILE A CG1   1 
ATOM   5181  C  CG2   . ILE A 1 644 ? 143.656 134.536 93.459  1.00 7.74  ?  644 ILE A CG2   1 
ATOM   5182  C  CD1   . ILE A 1 644 ? 142.929 131.659 92.457  1.00 22.09 ?  644 ILE A CD1   1 
ATOM   5183  N  N     . GLN A 1 645 ? 147.133 134.352 95.009  1.00 11.57 ?  645 GLN A N     1 
ATOM   5184  C  CA    . GLN A 1 645 ? 147.514 135.167 96.159  1.00 11.89 ?  645 GLN A CA    1 
ATOM   5185  C  C     . GLN A 1 645 ? 148.551 136.224 95.801  1.00 18.71 ?  645 GLN A C     1 
ATOM   5186  O  O     . GLN A 1 645 ? 148.603 137.281 96.441  1.00 23.96 ?  645 GLN A O     1 
ATOM   5187  C  CB    . GLN A 1 645 ? 148.040 134.272 97.282  1.00 8.94  ?  645 GLN A CB    1 
ATOM   5188  C  CG    . GLN A 1 645 ? 148.392 135.005 98.567  1.00 10.21 ?  645 GLN A CG    1 
ATOM   5189  C  CD    . GLN A 1 645 ? 147.187 135.642 99.223  1.00 12.21 ?  645 GLN A CD    1 
ATOM   5190  O  OE1   . GLN A 1 645 ? 146.468 134.996 99.981  1.00 18.33 ?  645 GLN A OE1   1 
ATOM   5191  N  NE2   . GLN A 1 645 ? 146.963 136.917 98.937  1.00 4.73  ?  645 GLN A NE2   1 
ATOM   5192  N  N     . GLN A 1 646 ? 149.376 135.972 94.786  1.00 20.94 ?  646 GLN A N     1 
ATOM   5193  C  CA    . GLN A 1 646 ? 150.411 136.932 94.429  1.00 14.79 ?  646 GLN A CA    1 
ATOM   5194  C  C     . GLN A 1 646 ? 149.849 138.225 93.854  1.00 15.69 ?  646 GLN A C     1 
ATOM   5195  O  O     . GLN A 1 646 ? 150.582 139.216 93.779  1.00 20.87 ?  646 GLN A O     1 
ATOM   5196  C  CB    . GLN A 1 646 ? 151.394 136.299 93.444  1.00 20.94 ?  646 GLN A CB    1 
ATOM   5197  C  CG    . GLN A 1 646 ? 150.937 136.304 92.003  1.00 22.21 ?  646 GLN A CG    1 
ATOM   5198  C  CD    . GLN A 1 646 ? 151.874 135.529 91.100  1.00 30.10 ?  646 GLN A CD    1 
ATOM   5199  O  OE1   . GLN A 1 646 ? 151.483 134.537 90.486  1.00 25.03 ?  646 GLN A OE1   1 
ATOM   5200  N  NE2   . GLN A 1 646 ? 153.119 135.979 91.016  1.00 26.74 ?  646 GLN A NE2   1 
ATOM   5201  N  N     . HIS A 1 647 ? 148.577 138.247 93.464  1.00 21.92 ?  647 HIS A N     1 
ATOM   5202  C  CA    . HIS A 1 647 ? 147.925 139.456 92.984  1.00 14.76 ?  647 HIS A CA    1 
ATOM   5203  C  C     . HIS A 1 647 ? 146.914 140.014 93.975  1.00 15.27 ?  647 HIS A C     1 
ATOM   5204  O  O     . HIS A 1 647 ? 146.261 141.018 93.675  1.00 25.12 ?  647 HIS A O     1 
ATOM   5205  C  CB    . HIS A 1 647 ? 147.236 139.186 91.643  1.00 11.36 ?  647 HIS A CB    1 
ATOM   5206  C  CG    . HIS A 1 647 ? 148.133 138.565 90.621  1.00 16.48 ?  647 HIS A CG    1 
ATOM   5207  N  ND1   . HIS A 1 647 ? 149.270 139.188 90.154  1.00 19.03 ?  647 HIS A ND1   1 
ATOM   5208  C  CD2   . HIS A 1 647 ? 148.064 137.377 89.977  1.00 17.59 ?  647 HIS A CD2   1 
ATOM   5209  C  CE1   . HIS A 1 647 ? 149.863 138.410 89.267  1.00 20.83 ?  647 HIS A CE1   1 
ATOM   5210  N  NE2   . HIS A 1 647 ? 149.151 137.305 89.140  1.00 20.71 ?  647 HIS A NE2   1 
ATOM   5211  N  N     . ILE A 1 648 ? 146.766 139.392 95.140  1.00 13.52 ?  648 ILE A N     1 
ATOM   5212  C  CA    . ILE A 1 648 ? 145.806 139.807 96.155  1.00 12.03 ?  648 ILE A CA    1 
ATOM   5213  C  C     . ILE A 1 648 ? 146.592 140.393 97.318  1.00 12.20 ?  648 ILE A C     1 
ATOM   5214  O  O     . ILE A 1 648 ? 147.482 139.733 97.868  1.00 25.66 ?  648 ILE A O     1 
ATOM   5215  C  CB    . ILE A 1 648 ? 144.927 138.631 96.609  1.00 10.19 ?  648 ILE A CB    1 
ATOM   5216  C  CG1   . ILE A 1 648 ? 144.202 138.005 95.415  1.00 11.20 ?  648 ILE A CG1   1 
ATOM   5217  C  CG2   . ILE A 1 648 ? 143.920 139.078 97.651  1.00 5.66  ?  648 ILE A CG2   1 
ATOM   5218  C  CD1   . ILE A 1 648 ? 143.105 138.868 94.841  1.00 5.31  ?  648 ILE A CD1   1 
ATOM   5219  N  N     . ASP A 1 649 ? 146.273 141.636 97.691  1.00 7.57  ?  649 ASP A N     1 
ATOM   5220  C  CA    . ASP A 1 649 ? 147.026 142.290 98.756  1.00 8.07  ?  649 ASP A CA    1 
ATOM   5221  C  C     . ASP A 1 649 ? 146.680 141.716 100.122 1.00 9.20  ?  649 ASP A C     1 
ATOM   5222  O  O     . ASP A 1 649 ? 147.555 141.608 100.988 1.00 27.02 ?  649 ASP A O     1 
ATOM   5223  C  CB    . ASP A 1 649 ? 146.782 143.798 98.735  1.00 18.44 ?  649 ASP A CB    1 
ATOM   5224  C  CG    . ASP A 1 649 ? 145.326 144.151 98.532  1.00 19.25 ?  649 ASP A CG    1 
ATOM   5225  O  OD1   . ASP A 1 649 ? 144.862 144.109 97.378  1.00 24.05 ?  649 ASP A OD1   1 
ATOM   5226  O  OD2   . ASP A 1 649 ? 144.647 144.477 99.526  1.00 20.27 -1 649 ASP A OD2   1 
ATOM   5227  N  N     . GLN A 1 650 ? 145.422 141.364 100.339 1.00 13.71 ?  650 GLN A N     1 
ATOM   5228  C  CA    . GLN A 1 650 ? 144.997 140.670 101.543 1.00 4.37  ?  650 GLN A CA    1 
ATOM   5229  C  C     . GLN A 1 650 ? 145.049 139.164 101.276 1.00 10.77 ?  650 GLN A C     1 
ATOM   5230  O  O     . GLN A 1 650 ? 145.655 138.717 100.300 1.00 20.19 ?  650 GLN A O     1 
ATOM   5231  C  CB    . GLN A 1 650 ? 143.619 141.173 101.972 1.00 6.40  ?  650 GLN A CB    1 
ATOM   5232  C  CG    . GLN A 1 650 ? 143.571 142.670 102.215 1.00 9.80  ?  650 GLN A CG    1 
ATOM   5233  C  CD    . GLN A 1 650 ? 142.239 143.126 102.762 1.00 13.56 ?  650 GLN A CD    1 
ATOM   5234  O  OE1   . GLN A 1 650 ? 141.901 142.847 103.909 1.00 15.64 ?  650 GLN A OE1   1 
ATOM   5235  N  NE2   . GLN A 1 650 ? 141.473 143.835 101.943 1.00 3.67  ?  650 GLN A NE2   1 
ATOM   5236  N  N     . GLY A 1 651 ? 144.448 138.360 102.151 1.00 9.85  ?  651 GLY A N     1 
ATOM   5237  C  CA    . GLY A 1 651 ? 144.502 136.922 102.031 1.00 5.75  ?  651 GLY A CA    1 
ATOM   5238  C  C     . GLY A 1 651 ? 143.319 136.332 101.280 1.00 5.51  ?  651 GLY A C     1 
ATOM   5239  O  O     . GLY A 1 651 ? 142.420 137.021 100.806 1.00 10.85 ?  651 GLY A O     1 
ATOM   5240  N  N     . ILE A 1 652 ? 143.348 135.007 101.177 1.00 13.76 ?  652 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 652 ? 142.312 134.221 100.524 1.00 2.10  ?  652 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 652 ? 141.857 133.151 101.504 1.00 12.29 ?  652 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 652 ? 142.689 132.441 102.077 1.00 26.74 ?  652 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 652 ? 142.822 133.576 99.220  1.00 6.19  ?  652 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 652 ? 143.420 134.634 98.292  1.00 4.30  ?  652 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 652 ? 141.710 132.814 98.528  1.00 11.90 ?  652 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 652 ? 144.007 134.065 97.032  1.00 5.06  ?  652 ILE A CD1   1 
ATOM   5248  N  N     . SER A 1 653 ? 140.548 133.038 101.701 1.00 10.56 ?  653 SER A N     1 
ATOM   5249  C  CA    . SER A 1 653 ? 139.999 132.024 102.597 1.00 12.86 ?  653 SER A CA    1 
ATOM   5250  C  C     . SER A 1 653 ? 140.218 130.657 101.967 1.00 18.04 ?  653 SER A C     1 
ATOM   5251  O  O     . SER A 1 653 ? 139.455 130.228 101.102 1.00 20.45 ?  653 SER A O     1 
ATOM   5252  C  CB    . SER A 1 653 ? 138.520 132.282 102.854 1.00 13.46 ?  653 SER A CB    1 
ATOM   5253  O  OG    . SER A 1 653 ? 138.331 132.995 104.059 1.00 20.71 ?  653 SER A OG    1 
ATOM   5254  N  N     . PHE A 1 654 ? 141.256 129.960 102.416 1.00 22.22 ?  654 PHE A N     1 
ATOM   5255  C  CA    . PHE A 1 654 ? 141.731 128.737 101.779 1.00 10.48 ?  654 PHE A CA    1 
ATOM   5256  C  C     . PHE A 1 654 ? 141.315 127.542 102.627 1.00 13.54 ?  654 PHE A C     1 
ATOM   5257  O  O     . PHE A 1 654 ? 141.917 127.274 103.672 1.00 21.98 ?  654 PHE A O     1 
ATOM   5258  C  CB    . PHE A 1 654 ? 143.246 128.792 101.601 1.00 15.97 ?  654 PHE A CB    1 
ATOM   5259  C  CG    . PHE A 1 654 ? 143.815 127.644 100.822 1.00 16.96 ?  654 PHE A CG    1 
ATOM   5260  C  CD1   . PHE A 1 654 ? 143.005 126.844 100.037 1.00 18.84 ?  654 PHE A CD1   1 
ATOM   5261  C  CD2   . PHE A 1 654 ? 145.168 127.372 100.872 1.00 21.85 ?  654 PHE A CD2   1 
ATOM   5262  C  CE1   . PHE A 1 654 ? 143.533 125.794 99.325  1.00 18.09 ?  654 PHE A CE1   1 
ATOM   5263  C  CE2   . PHE A 1 654 ? 145.700 126.325 100.158 1.00 21.06 ?  654 PHE A CE2   1 
ATOM   5264  C  CZ    . PHE A 1 654 ? 144.882 125.534 99.383  1.00 19.78 ?  654 PHE A CZ    1 
ATOM   5265  N  N     . THR A 1 655 ? 140.302 126.817 102.165 1.00 22.24 ?  655 THR A N     1 
ATOM   5266  C  CA    . THR A 1 655 ? 139.844 125.606 102.829 1.00 23.33 ?  655 THR A CA    1 
ATOM   5267  C  C     . THR A 1 655 ? 140.610 124.403 102.293 1.00 26.54 ?  655 THR A C     1 
ATOM   5268  O  O     . THR A 1 655 ? 140.786 124.261 101.079 1.00 26.35 ?  655 THR A O     1 
ATOM   5269  C  CB    . THR A 1 655 ? 138.342 125.412 102.618 1.00 23.96 ?  655 THR A CB    1 
ATOM   5270  O  OG1   . THR A 1 655 ? 137.632 126.500 103.221 1.00 31.72 ?  655 THR A OG1   1 
ATOM   5271  C  CG2   . THR A 1 655 ? 137.878 124.109 103.243 1.00 26.42 ?  655 THR A CG2   1 
ATOM   5272  N  N     . LEU A 1 656 ? 141.071 123.545 103.200 1.00 29.51 ?  656 LEU A N     1 
ATOM   5273  C  CA    . LEU A 1 656 ? 141.728 122.302 102.825 1.00 29.05 ?  656 LEU A CA    1 
ATOM   5274  C  C     . LEU A 1 656 ? 140.711 121.172 102.818 1.00 28.32 ?  656 LEU A C     1 
ATOM   5275  O  O     . LEU A 1 656 ? 140.025 120.937 103.817 1.00 28.78 ?  656 LEU A O     1 
ATOM   5276  C  CB    . LEU A 1 656 ? 142.871 121.977 103.786 1.00 29.85 ?  656 LEU A CB    1 
ATOM   5277  C  CG    . LEU A 1 656 ? 144.072 122.919 103.748 1.00 32.35 ?  656 LEU A CG    1 
ATOM   5278  C  CD1   . LEU A 1 656 ? 145.212 122.352 104.573 1.00 29.79 ?  656 LEU A CD1   1 
ATOM   5279  C  CD2   . LEU A 1 656 ? 144.514 123.181 102.318 1.00 27.79 ?  656 LEU A CD2   1 
ATOM   5280  N  N     . PHE A 1 657 ? 140.622 120.474 101.694 1.00 27.28 ?  657 PHE A N     1 
ATOM   5281  C  CA    . PHE A 1 657 ? 139.654 119.401 101.505 1.00 27.17 ?  657 PHE A CA    1 
ATOM   5282  C  C     . PHE A 1 657 ? 140.390 118.073 101.608 1.00 34.16 ?  657 PHE A C     1 
ATOM   5283  O  O     . PHE A 1 657 ? 141.143 117.698 100.704 1.00 37.77 ?  657 PHE A O     1 
ATOM   5284  C  CB    . PHE A 1 657 ? 138.947 119.555 100.163 1.00 28.61 ?  657 PHE A CB    1 
ATOM   5285  C  CG    . PHE A 1 657 ? 138.320 120.903 99.970  1.00 33.56 ?  657 PHE A CG    1 
ATOM   5286  C  CD1   . PHE A 1 657 ? 137.038 121.156 100.423 1.00 30.41 ?  657 PHE A CD1   1 
ATOM   5287  C  CD2   . PHE A 1 657 ? 139.020 121.927 99.350  1.00 34.59 ?  657 PHE A CD2   1 
ATOM   5288  C  CE1   . PHE A 1 657 ? 136.460 122.396 100.250 1.00 33.52 ?  657 PHE A CE1   1 
ATOM   5289  C  CE2   . PHE A 1 657 ? 138.446 123.169 99.174  1.00 30.81 ?  657 PHE A CE2   1 
ATOM   5290  C  CZ    . PHE A 1 657 ? 137.165 123.403 99.628  1.00 32.22 ?  657 PHE A CZ    1 
ATOM   5291  N  N     . LEU A 1 658 ? 140.167 117.364 102.710 1.00 42.10 ?  658 LEU A N     1 
ATOM   5292  C  CA    . LEU A 1 658 ? 140.940 116.182 103.063 1.00 40.48 ?  658 LEU A CA    1 
ATOM   5293  C  C     . LEU A 1 658 ? 140.077 114.932 102.977 1.00 44.65 ?  658 LEU A C     1 
ATOM   5294  O  O     . LEU A 1 658 ? 138.896 114.953 103.335 1.00 48.50 ?  658 LEU A O     1 
ATOM   5295  C  CB    . LEU A 1 658 ? 141.508 116.315 104.477 1.00 38.92 ?  658 LEU A CB    1 
ATOM   5296  C  CG    . LEU A 1 658 ? 141.961 117.712 104.900 1.00 38.09 ?  658 LEU A CG    1 
ATOM   5297  C  CD1   . LEU A 1 658 ? 142.111 117.774 106.406 1.00 37.57 ?  658 LEU A CD1   1 
ATOM   5298  C  CD2   . LEU A 1 658 ? 143.263 118.084 104.214 1.00 39.85 ?  658 LEU A CD2   1 
ATOM   5299  N  N     . LYS A 1 659 ? 140.670 113.847 102.492 1.00 48.81 ?  659 LYS A N     1 
ATOM   5300  C  CA    . LYS A 1 659 ? 140.021 112.549 102.558 1.00 49.27 ?  659 LYS A CA    1 
ATOM   5301  C  C     . LYS A 1 659 ? 140.248 111.916 103.928 1.00 49.70 ?  659 LYS A C     1 
ATOM   5302  O  O     . LYS A 1 659 ? 141.125 112.324 104.693 1.00 53.26 ?  659 LYS A O     1 
ATOM   5303  C  CB    . LYS A 1 659 ? 140.541 111.624 101.458 1.00 50.47 ?  659 LYS A CB    1 
ATOM   5304  C  CG    . LYS A 1 659 ? 140.062 111.987 100.065 1.00 50.24 ?  659 LYS A CG    1 
ATOM   5305  C  CD    . LYS A 1 659 ? 140.432 110.910 99.060  1.00 50.40 ?  659 LYS A CD    1 
ATOM   5306  C  CE    . LYS A 1 659 ? 139.872 111.225 97.684  1.00 49.54 ?  659 LYS A CE    1 
ATOM   5307  N  NZ    . LYS A 1 659 ? 139.858 110.027 96.802  1.00 49.60 1  659 LYS A NZ    1 
ATOM   5308  N  N     . ASP A 1 660 ? 139.431 110.910 104.238 1.00 56.54 ?  660 ASP A N     1 
ATOM   5309  C  CA    . ASP A 1 660 ? 139.603 110.176 105.485 1.00 56.20 ?  660 ASP A CA    1 
ATOM   5310  C  C     . ASP A 1 660 ? 140.888 109.360 105.502 1.00 56.75 ?  660 ASP A C     1 
ATOM   5311  O  O     . ASP A 1 660 ? 141.430 109.102 106.582 1.00 56.19 ?  660 ASP A O     1 
ATOM   5312  C  CB    . ASP A 1 660 ? 138.403 109.258 105.725 1.00 57.79 ?  660 ASP A CB    1 
ATOM   5313  C  CG    . ASP A 1 660 ? 137.424 109.829 106.729 1.00 58.39 ?  660 ASP A CG    1 
ATOM   5314  O  OD1   . ASP A 1 660 ? 136.364 109.208 106.948 1.00 57.17 ?  660 ASP A OD1   1 
ATOM   5315  O  OD2   . ASP A 1 660 ? 137.716 110.898 107.304 1.00 56.44 -1 660 ASP A OD2   1 
ATOM   5316  N  N     . THR A 1 661 ? 141.386 108.954 104.332 1.00 54.72 ?  661 THR A N     1 
ATOM   5317  C  CA    . THR A 1 661 ? 142.551 108.078 104.278 1.00 54.28 ?  661 THR A CA    1 
ATOM   5318  C  C     . THR A 1 661 ? 143.829 108.785 104.714 1.00 54.79 ?  661 THR A C     1 
ATOM   5319  O  O     . THR A 1 661 ? 144.700 108.156 105.327 1.00 57.02 ?  661 THR A O     1 
ATOM   5320  C  CB    . THR A 1 661 ? 142.721 107.519 102.866 1.00 55.29 ?  661 THR A CB    1 
ATOM   5321  O  OG1   . THR A 1 661 ? 142.355 108.521 101.908 1.00 55.34 ?  661 THR A OG1   1 
ATOM   5322  C  CG2   . THR A 1 661 ? 141.842 106.295 102.671 1.00 54.88 ?  661 THR A CG2   1 
ATOM   5323  N  N     . MET A 1 662 ? 143.967 110.072 104.413 1.00 53.00 ?  662 MET A N     1 
ATOM   5324  C  CA    . MET A 1 662 ? 145.213 110.776 104.687 1.00 52.79 ?  662 MET A CA    1 
ATOM   5325  C  C     . MET A 1 662 ? 145.378 111.025 106.181 1.00 51.88 ?  662 MET A C     1 
ATOM   5326  O  O     . MET A 1 662 ? 144.408 111.288 106.897 1.00 52.12 ?  662 MET A O     1 
ATOM   5327  C  CB    . MET A 1 662 ? 145.270 112.096 103.917 1.00 51.51 ?  662 MET A CB    1 
ATOM   5328  C  CG    . MET A 1 662 ? 144.177 113.088 104.252 1.00 52.69 ?  662 MET A CG    1 
ATOM   5329  S  SD    . MET A 1 662 ? 144.301 114.592 103.262 1.00 60.26 ?  662 MET A SD    1 
ATOM   5330  C  CE    . MET A 1 662 ? 145.161 113.990 101.812 1.00 49.12 ?  662 MET A CE    1 
ATOM   5331  N  N     . THR A 1 663 ? 146.621 110.934 106.645 1.00 44.50 ?  663 THR A N     1 
ATOM   5332  C  CA    . THR A 1 663 ? 146.942 111.028 108.060 1.00 43.95 ?  663 THR A CA    1 
ATOM   5333  C  C     . THR A 1 663 ? 147.187 112.486 108.444 1.00 45.06 ?  663 THR A C     1 
ATOM   5334  O  O     . THR A 1 663 ? 146.970 113.406 107.653 1.00 48.51 ?  663 THR A O     1 
ATOM   5335  C  CB    . THR A 1 663 ? 148.155 110.157 108.380 1.00 43.10 ?  663 THR A CB    1 
ATOM   5336  O  OG1   . THR A 1 663 ? 149.335 110.772 107.849 1.00 41.26 ?  663 THR A OG1   1 
ATOM   5337  C  CG2   . THR A 1 663 ? 147.995 108.781 107.756 1.00 44.67 ?  663 THR A CG2   1 
ATOM   5338  N  N     . THR A 1 664 ? 147.639 112.712 109.680 1.00 39.46 ?  664 THR A N     1 
ATOM   5339  C  CA    . THR A 1 664 ? 148.025 114.060 110.079 1.00 41.82 ?  664 THR A CA    1 
ATOM   5340  C  C     . THR A 1 664 ? 149.310 114.495 109.389 1.00 40.57 ?  664 THR A C     1 
ATOM   5341  O  O     . THR A 1 664 ? 149.546 115.697 109.224 1.00 42.64 ?  664 THR A O     1 
ATOM   5342  C  CB    . THR A 1 664 ? 148.189 114.147 111.596 1.00 41.38 ?  664 THR A CB    1 
ATOM   5343  O  OG1   . THR A 1 664 ? 149.240 113.270 112.018 1.00 40.03 ?  664 THR A OG1   1 
ATOM   5344  C  CG2   . THR A 1 664 ? 146.897 113.765 112.298 1.00 39.88 ?  664 THR A CG2   1 
ATOM   5345  N  N     . ARG A 1 665 ? 150.148 113.538 108.985 1.00 39.85 ?  665 ARG A N     1 
ATOM   5346  C  CA    . ARG A 1 665 ? 151.358 113.881 108.246 1.00 38.49 ?  665 ARG A CA    1 
ATOM   5347  C  C     . ARG A 1 665 ? 151.021 114.504 106.900 1.00 41.53 ?  665 ARG A C     1 
ATOM   5348  O  O     . ARG A 1 665 ? 151.701 115.430 106.453 1.00 42.68 ?  665 ARG A O     1 
ATOM   5349  C  CB    . ARG A 1 665 ? 152.232 112.644 108.052 1.00 39.32 ?  665 ARG A CB    1 
ATOM   5350  C  CG    . ARG A 1 665 ? 153.521 112.925 107.303 1.00 37.71 ?  665 ARG A CG    1 
ATOM   5351  C  CD    . ARG A 1 665 ? 154.428 111.712 107.278 1.00 39.18 ?  665 ARG A CD    1 
ATOM   5352  N  NE    . ARG A 1 665 ? 155.500 111.853 106.301 1.00 41.76 ?  665 ARG A NE    1 
ATOM   5353  C  CZ    . ARG A 1 665 ? 155.344 111.730 104.990 1.00 45.20 ?  665 ARG A CZ    1 
ATOM   5354  N  NH1   . ARG A 1 665 ? 154.166 111.453 104.457 1.00 43.53 1  665 ARG A NH1   1 
ATOM   5355  N  NH2   . ARG A 1 665 ? 156.398 111.886 104.193 1.00 42.18 ?  665 ARG A NH2   1 
ATOM   5356  N  N     . ASP A 1 666 ? 149.980 114.003 106.232 1.00 38.83 ?  666 ASP A N     1 
ATOM   5357  C  CA    . ASP A 1 666 ? 149.580 114.587 104.956 1.00 35.10 ?  666 ASP A CA    1 
ATOM   5358  C  C     . ASP A 1 666 ? 149.059 116.008 105.135 1.00 37.66 ?  666 ASP A C     1 
ATOM   5359  O  O     . ASP A 1 666 ? 149.361 116.893 104.326 1.00 40.48 ?  666 ASP A O     1 
ATOM   5360  C  CB    . ASP A 1 666 ? 148.530 113.704 104.284 1.00 40.83 ?  666 ASP A CB    1 
ATOM   5361  C  CG    . ASP A 1 666 ? 149.071 112.337 103.919 1.00 45.35 ?  666 ASP A CG    1 
ATOM   5362  O  OD1   . ASP A 1 666 ? 150.172 112.268 103.334 1.00 45.48 ?  666 ASP A OD1   1 
ATOM   5363  O  OD2   . ASP A 1 666 ? 148.396 111.329 104.217 1.00 45.22 -1 666 ASP A OD2   1 
ATOM   5364  N  N     . LEU A 1 667 ? 148.276 116.246 106.189 1.00 36.21 ?  667 LEU A N     1 
ATOM   5365  C  CA    . LEU A 1 667 ? 147.806 117.597 106.471 1.00 31.15 ?  667 LEU A CA    1 
ATOM   5366  C  C     . LEU A 1 667 ? 148.977 118.523 106.780 1.00 29.82 ?  667 LEU A C     1 
ATOM   5367  O  O     . LEU A 1 667 ? 149.016 119.670 106.316 1.00 34.82 ?  667 LEU A O     1 
ATOM   5368  C  CB    . LEU A 1 667 ? 146.810 117.559 107.633 1.00 34.82 ?  667 LEU A CB    1 
ATOM   5369  C  CG    . LEU A 1 667 ? 146.172 118.830 108.206 1.00 36.50 ?  667 LEU A CG    1 
ATOM   5370  C  CD1   . LEU A 1 667 ? 145.966 119.900 107.144 1.00 35.38 ?  667 LEU A CD1   1 
ATOM   5371  C  CD2   . LEU A 1 667 ? 144.857 118.491 108.882 1.00 32.66 ?  667 LEU A CD2   1 
ATOM   5372  N  N     . ASN A 1 668 ? 149.951 118.036 107.550 1.00 32.07 ?  668 ASN A N     1 
ATOM   5373  C  CA    . ASN A 1 668 ? 151.135 118.836 107.847 1.00 26.94 ?  668 ASN A CA    1 
ATOM   5374  C  C     . ASN A 1 668 ? 151.938 119.125 106.585 1.00 26.92 ?  668 ASN A C     1 
ATOM   5375  O  O     . ASN A 1 668 ? 152.472 120.225 106.422 1.00 33.03 ?  668 ASN A O     1 
ATOM   5376  C  CB    . ASN A 1 668 ? 152.000 118.121 108.884 1.00 27.90 ?  668 ASN A CB    1 
ATOM   5377  C  CG    . ASN A 1 668 ? 151.709 118.579 110.296 1.00 30.77 ?  668 ASN A CG    1 
ATOM   5378  O  OD1   . ASN A 1 668 ? 151.195 119.675 110.512 1.00 31.97 ?  668 ASN A OD1   1 
ATOM   5379  N  ND2   . ASN A 1 668 ? 152.028 117.735 111.268 1.00 37.76 ?  668 ASN A ND2   1 
ATOM   5380  N  N     . ARG A 1 669 ? 152.042 118.145 105.687 1.00 30.35 ?  669 ARG A N     1 
ATOM   5381  C  CA    . ARG A 1 669 ? 152.739 118.360 104.424 1.00 31.14 ?  669 ARG A CA    1 
ATOM   5382  C  C     . ARG A 1 669 ? 152.030 119.406 103.578 1.00 27.39 ?  669 ARG A C     1 
ATOM   5383  O  O     . ARG A 1 669 ? 152.679 120.244 102.945 1.00 31.90 ?  669 ARG A O     1 
ATOM   5384  C  CB    . ARG A 1 669 ? 152.858 117.045 103.656 1.00 29.28 ?  669 ARG A CB    1 
ATOM   5385  C  CG    . ARG A 1 669 ? 153.962 116.132 104.145 1.00 31.02 ?  669 ARG A CG    1 
ATOM   5386  C  CD    . ARG A 1 669 ? 154.422 115.204 103.038 1.00 34.56 ?  669 ARG A CD    1 
ATOM   5387  N  NE    . ARG A 1 669 ? 155.330 115.866 102.110 1.00 33.91 ?  669 ARG A NE    1 
ATOM   5388  C  CZ    . ARG A 1 669 ? 155.238 115.789 100.790 1.00 33.75 ?  669 ARG A CZ    1 
ATOM   5389  N  NH1   . ARG A 1 669 ? 154.282 115.088 100.203 1.00 34.67 1  669 ARG A NH1   1 
ATOM   5390  N  NH2   . ARG A 1 669 ? 156.127 116.433 100.038 1.00 33.28 ?  669 ARG A NH2   1 
ATOM   5391  N  N     . ILE A 1 670 ? 150.697 119.367 103.546 1.00 23.06 ?  670 ILE A N     1 
ATOM   5392  C  CA    . ILE A 1 670 ? 149.947 120.384 102.814 1.00 27.95 ?  670 ILE A CA    1 
ATOM   5393  C  C     . ILE A 1 670 ? 150.186 121.760 103.421 1.00 30.84 ?  670 ILE A C     1 
ATOM   5394  O  O     . ILE A 1 670 ? 150.384 122.745 102.701 1.00 29.03 ?  670 ILE A O     1 
ATOM   5395  C  CB    . ILE A 1 670 ? 148.448 120.032 102.778 1.00 28.07 ?  670 ILE A CB    1 
ATOM   5396  C  CG1   . ILE A 1 670 ? 148.221 118.737 101.999 1.00 30.56 ?  670 ILE A CG1   1 
ATOM   5397  C  CG2   . ILE A 1 670 ? 147.651 121.159 102.146 1.00 27.64 ?  670 ILE A CG2   1 
ATOM   5398  C  CD1   . ILE A 1 670 ? 146.924 118.044 102.337 1.00 29.61 ?  670 ILE A CD1   1 
ATOM   5399  N  N     . ASP A 1 671 ? 150.182 121.849 104.754 1.00 28.70 ?  671 ASP A N     1 
ATOM   5400  C  CA    . ASP A 1 671 ? 150.430 123.128 105.415 1.00 22.91 ?  671 ASP A CA    1 
ATOM   5401  C  C     . ASP A 1 671 ? 151.832 123.650 105.114 1.00 23.48 ?  671 ASP A C     1 
ATOM   5402  O  O     . ASP A 1 671 ? 152.019 124.845 104.857 1.00 25.79 ?  671 ASP A O     1 
ATOM   5403  C  CB    . ASP A 1 671 ? 150.227 122.988 106.924 1.00 26.10 ?  671 ASP A CB    1 
ATOM   5404  C  CG    . ASP A 1 671 ? 148.812 122.583 107.288 1.00 37.56 ?  671 ASP A CG    1 
ATOM   5405  O  OD1   . ASP A 1 671 ? 147.882 122.909 106.523 1.00 36.26 ?  671 ASP A OD1   1 
ATOM   5406  O  OD2   . ASP A 1 671 ? 148.630 121.935 108.342 1.00 37.09 -1 671 ASP A OD2   1 
ATOM   5407  N  N     . LEU A 1 672 ? 152.830 122.766 105.134 1.00 25.36 ?  672 LEU A N     1 
ATOM   5408  C  CA    . LEU A 1 672 ? 154.203 123.184 104.873 1.00 19.20 ?  672 LEU A CA    1 
ATOM   5409  C  C     . LEU A 1 672 ? 154.412 123.558 103.412 1.00 19.80 ?  672 LEU A C     1 
ATOM   5410  O  O     . LEU A 1 672 ? 155.201 124.459 103.114 1.00 25.70 ?  672 LEU A O     1 
ATOM   5411  C  CB    . LEU A 1 672 ? 155.173 122.079 105.285 1.00 22.76 ?  672 LEU A CB    1 
ATOM   5412  C  CG    . LEU A 1 672 ? 155.271 121.821 106.788 1.00 23.94 ?  672 LEU A CG    1 
ATOM   5413  C  CD1   . LEU A 1 672 ? 155.922 120.476 107.063 1.00 19.57 ?  672 LEU A CD1   1 
ATOM   5414  C  CD2   . LEU A 1 672 ? 156.028 122.945 107.475 1.00 21.82 ?  672 LEU A CD2   1 
ATOM   5415  N  N     . TYR A 1 673 ? 153.723 122.883 102.491 1.00 21.30 ?  673 TYR A N     1 
ATOM   5416  C  CA    . TYR A 1 673 ? 153.805 123.259 101.086 1.00 18.93 ?  673 TYR A CA    1 
ATOM   5417  C  C     . TYR A 1 673 ? 153.103 124.587 100.834 1.00 21.16 ?  673 TYR A C     1 
ATOM   5418  O  O     . TYR A 1 673 ? 153.550 125.387 100.007 1.00 24.42 ?  673 TYR A O     1 
ATOM   5419  C  CB    . TYR A 1 673 ? 153.208 122.156 100.215 1.00 14.92 ?  673 TYR A CB    1 
ATOM   5420  C  CG    . TYR A 1 673 ? 153.308 122.424 98.734  1.00 19.19 ?  673 TYR A CG    1 
ATOM   5421  C  CD1   . TYR A 1 673 ? 154.543 122.518 98.110  1.00 18.76 ?  673 TYR A CD1   1 
ATOM   5422  C  CD2   . TYR A 1 673 ? 152.169 122.577 97.958  1.00 18.36 ?  673 TYR A CD2   1 
ATOM   5423  C  CE1   . TYR A 1 673 ? 154.639 122.761 96.758  1.00 23.48 ?  673 TYR A CE1   1 
ATOM   5424  C  CE2   . TYR A 1 673 ? 152.256 122.819 96.606  1.00 21.21 ?  673 TYR A CE2   1 
ATOM   5425  C  CZ    . TYR A 1 673 ? 153.493 122.909 96.011  1.00 25.20 ?  673 TYR A CZ    1 
ATOM   5426  O  OH    . TYR A 1 673 ? 153.587 123.151 94.661  1.00 24.69 ?  673 TYR A OH    1 
ATOM   5427  N  N     . ALA A 1 674 ? 151.993 124.831 101.533 1.00 23.17 ?  674 ALA A N     1 
ATOM   5428  C  CA    . ALA A 1 674 ? 151.334 126.128 101.450 1.00 16.78 ?  674 ALA A CA    1 
ATOM   5429  C  C     . ALA A 1 674 ? 152.239 127.235 101.973 1.00 17.23 ?  674 ALA A C     1 
ATOM   5430  O  O     . ALA A 1 674 ? 152.340 128.304 101.363 1.00 25.24 ?  674 ALA A O     1 
ATOM   5431  C  CB    . ALA A 1 674 ? 150.017 126.092 102.224 1.00 12.27 ?  674 ALA A CB    1 
ATOM   5432  N  N     . HIS A 1 675 ? 152.916 126.989 103.095 1.00 15.67 ?  675 HIS A N     1 
ATOM   5433  C  CA    . HIS A 1 675 ? 153.869 127.968 103.609 1.00 19.64 ?  675 HIS A CA    1 
ATOM   5434  C  C     . HIS A 1 675 ? 155.016 128.186 102.630 1.00 19.45 ?  675 HIS A C     1 
ATOM   5435  O  O     . HIS A 1 675 ? 155.473 129.319 102.438 1.00 24.55 ?  675 HIS A O     1 
ATOM   5436  C  CB    . HIS A 1 675 ? 154.401 127.518 104.967 1.00 18.08 ?  675 HIS A CB    1 
ATOM   5437  C  CG    . HIS A 1 675 ? 155.534 128.354 105.475 1.00 20.55 ?  675 HIS A CG    1 
ATOM   5438  N  ND1   . HIS A 1 675 ? 156.851 127.970 105.357 1.00 28.37 ?  675 HIS A ND1   1 
ATOM   5439  C  CD2   . HIS A 1 675 ? 155.545 129.554 106.097 1.00 18.60 ?  675 HIS A CD2   1 
ATOM   5440  C  CE1   . HIS A 1 675 ? 157.626 128.899 105.887 1.00 23.86 ?  675 HIS A CE1   1 
ATOM   5441  N  NE2   . HIS A 1 675 ? 156.858 129.871 106.344 1.00 24.59 ?  675 HIS A NE2   1 
ATOM   5442  N  N     . HIS A 1 676 ? 155.500 127.110 102.007 1.00 22.03 ?  676 HIS A N     1 
ATOM   5443  C  CA    . HIS A 1 676 ? 156.587 127.226 101.042 1.00 19.91 ?  676 HIS A CA    1 
ATOM   5444  C  C     . HIS A 1 676 ? 156.159 128.008 99.807  1.00 25.51 ?  676 HIS A C     1 
ATOM   5445  O  O     . HIS A 1 676 ? 156.947 128.776 99.244  1.00 25.79 ?  676 HIS A O     1 
ATOM   5446  C  CB    . HIS A 1 676 ? 157.080 125.833 100.648 1.00 23.94 ?  676 HIS A CB    1 
ATOM   5447  C  CG    . HIS A 1 676 ? 158.009 125.830 99.474  1.00 24.67 ?  676 HIS A CG    1 
ATOM   5448  N  ND1   . HIS A 1 676 ? 159.322 126.236 99.563  1.00 22.61 ?  676 HIS A ND1   1 
ATOM   5449  C  CD2   . HIS A 1 676 ? 157.813 125.469 98.185  1.00 25.58 ?  676 HIS A CD2   1 
ATOM   5450  C  CE1   . HIS A 1 676 ? 159.896 126.125 98.379  1.00 29.10 ?  676 HIS A CE1   1 
ATOM   5451  N  NE2   . HIS A 1 676 ? 159.002 125.662 97.525  1.00 27.74 ?  676 HIS A NE2   1 
ATOM   5452  N  N     . ARG A 1 677 ? 154.915 127.828 99.373  1.00 23.74 ?  677 ARG A N     1 
ATOM   5453  C  CA    . ARG A 1 677 ? 154.431 128.428 98.138  1.00 19.41 ?  677 ARG A CA    1 
ATOM   5454  C  C     . ARG A 1 677 ? 153.910 129.846 98.325  1.00 20.49 ?  677 ARG A C     1 
ATOM   5455  O  O     . ARG A 1 677 ? 153.415 130.439 97.361  1.00 27.52 ?  677 ARG A O     1 
ATOM   5456  C  CB    . ARG A 1 677 ? 153.335 127.554 97.523  1.00 22.31 ?  677 ARG A CB    1 
ATOM   5457  C  CG    . ARG A 1 677 ? 153.864 126.397 96.693  1.00 22.58 ?  677 ARG A CG    1 
ATOM   5458  C  CD    . ARG A 1 677 ? 154.458 126.882 95.382  1.00 18.82 ?  677 ARG A CD    1 
ATOM   5459  N  NE    . ARG A 1 677 ? 153.444 127.032 94.346  1.00 26.67 ?  677 ARG A NE    1 
ATOM   5460  C  CZ    . ARG A 1 677 ? 153.148 128.178 93.747  1.00 31.68 ?  677 ARG A CZ    1 
ATOM   5461  N  NH1   . ARG A 1 677 ? 153.773 129.302 94.056  1.00 29.78 1  677 ARG A NH1   1 
ATOM   5462  N  NH2   . ARG A 1 677 ? 152.200 128.197 92.814  1.00 25.25 ?  677 ARG A NH2   1 
ATOM   5463  N  N     . GLY A 1 678 ? 154.008 130.404 99.526  1.00 18.80 ?  678 GLY A N     1 
ATOM   5464  C  CA    . GLY A 1 678 ? 153.570 131.763 99.764  1.00 11.84 ?  678 GLY A CA    1 
ATOM   5465  C  C     . GLY A 1 678 ? 152.126 131.919 100.171 1.00 17.48 ?  678 GLY A C     1 
ATOM   5466  O  O     . GLY A 1 678 ? 151.589 133.027 100.070 1.00 21.36 ?  678 GLY A O     1 
ATOM   5467  N  N     . ILE A 1 679 ? 151.473 130.848 100.621 1.00 18.57 ?  679 ILE A N     1 
ATOM   5468  C  CA    . ILE A 1 679 ? 150.102 130.954 101.101 1.00 11.37 ?  679 ILE A CA    1 
ATOM   5469  C  C     . ILE A 1 679 ? 150.088 131.759 102.390 1.00 13.32 ?  679 ILE A C     1 
ATOM   5470  O  O     . ILE A 1 679 ? 150.875 131.504 103.311 1.00 29.23 ?  679 ILE A O     1 
ATOM   5471  C  CB    . ILE A 1 679 ? 149.489 129.561 101.301 1.00 16.02 ?  679 ILE A CB    1 
ATOM   5472  C  CG1   . ILE A 1 679 ? 149.299 128.865 99.953  1.00 13.20 ?  679 ILE A CG1   1 
ATOM   5473  C  CG2   . ILE A 1 679 ? 148.174 129.649 102.055 1.00 14.77 ?  679 ILE A CG2   1 
ATOM   5474  C  CD1   . ILE A 1 679 ? 148.417 129.617 99.006  1.00 13.30 ?  679 ILE A CD1   1 
ATOM   5475  N  N     . LYS A 1 680 ? 149.196 132.746 102.459 1.00 9.75  ?  680 LYS A N     1 
ATOM   5476  C  CA    . LYS A 1 680 ? 149.159 133.633 103.615 1.00 6.25  ?  680 LYS A CA    1 
ATOM   5477  C  C     . LYS A 1 680 ? 148.374 133.019 104.768 1.00 5.30  ?  680 LYS A C     1 
ATOM   5478  O  O     . LYS A 1 680 ? 148.824 133.047 105.917 1.00 17.26 ?  680 LYS A O     1 
ATOM   5479  C  CB    . LYS A 1 680 ? 148.564 134.981 103.213 1.00 8.74  ?  680 LYS A CB    1 
ATOM   5480  C  CG    . LYS A 1 680 ? 149.422 135.780 102.253 1.00 0.00  ?  680 LYS A CG    1 
ATOM   5481  C  CD    . LYS A 1 680 ? 148.839 137.159 102.034 1.00 5.72  ?  680 LYS A CD    1 
ATOM   5482  C  CE    . LYS A 1 680 ? 149.566 137.901 100.938 1.00 9.99  ?  680 LYS A CE    1 
ATOM   5483  N  NZ    . LYS A 1 680 ? 149.026 139.270 100.757 1.00 15.99 1  680 LYS A NZ    1 
ATOM   5484  N  N     . THR A 1 681 ? 147.201 132.461 104.482 1.00 10.68 ?  681 THR A N     1 
ATOM   5485  C  CA    . THR A 1 681 ? 146.346 131.882 105.506 1.00 8.05  ?  681 THR A CA    1 
ATOM   5486  C  C     . THR A 1 681 ? 145.742 130.583 104.996 1.00 14.02 ?  681 THR A C     1 
ATOM   5487  O  O     . THR A 1 681 ? 145.549 130.400 103.793 1.00 25.07 ?  681 THR A O     1 
ATOM   5488  C  CB    . THR A 1 681 ? 145.215 132.840 105.924 1.00 14.36 ?  681 THR A CB    1 
ATOM   5489  O  OG1   . THR A 1 681 ? 144.573 133.368 104.756 1.00 21.48 ?  681 THR A OG1   1 
ATOM   5490  C  CG2   . THR A 1 681 ? 145.753 133.987 106.762 1.00 11.98 ?  681 THR A CG2   1 
ATOM   5491  N  N     . ILE A 1 682 ? 145.442 129.683 105.929 1.00 10.50 ?  682 ILE A N     1 
ATOM   5492  C  CA    . ILE A 1 682 ? 144.699 128.460 105.651 1.00 11.42 ?  682 ILE A CA    1 
ATOM   5493  C  C     . ILE A 1 682 ? 143.438 128.481 106.500 1.00 14.42 ?  682 ILE A C     1 
ATOM   5494  O  O     . ILE A 1 682 ? 143.513 128.607 107.727 1.00 15.39 ?  682 ILE A O     1 
ATOM   5495  C  CB    . ILE A 1 682 ? 145.533 127.200 105.938 1.00 16.27 ?  682 ILE A CB    1 
ATOM   5496  C  CG1   . ILE A 1 682 ? 146.904 127.297 105.270 1.00 17.97 ?  682 ILE A CG1   1 
ATOM   5497  C  CG2   . ILE A 1 682 ? 144.803 125.973 105.455 1.00 19.16 ?  682 ILE A CG2   1 
ATOM   5498  C  CD1   . ILE A 1 682 ? 147.764 126.075 105.467 1.00 19.40 ?  682 ILE A CD1   1 
ATOM   5499  N  N     . TYR A 1 683 ? 142.280 128.362 105.848 1.00 16.60 ?  683 TYR A N     1 
ATOM   5500  C  CA    . TYR A 1 683 ? 141.012 128.575 106.546 1.00 11.86 ?  683 TYR A CA    1 
ATOM   5501  C  C     . TYR A 1 683 ? 140.545 127.326 107.287 1.00 23.72 ?  683 TYR A C     1 
ATOM   5502  O  O     . TYR A 1 683 ? 140.502 127.299 108.519 1.00 33.70 ?  683 TYR A O     1 
ATOM   5503  C  CB    . TYR A 1 683 ? 139.948 129.038 105.545 1.00 18.22 ?  683 TYR A CB    1 
ATOM   5504  C  CG    . TYR A 1 683 ? 138.639 129.451 106.173 1.00 15.29 ?  683 TYR A CG    1 
ATOM   5505  C  CD1   . TYR A 1 683 ? 138.586 129.904 107.483 1.00 15.83 ?  683 TYR A CD1   1 
ATOM   5506  C  CD2   . TYR A 1 683 ? 137.455 129.399 105.450 1.00 13.23 ?  683 TYR A CD2   1 
ATOM   5507  C  CE1   . TYR A 1 683 ? 137.397 130.282 108.058 1.00 19.36 ?  683 TYR A CE1   1 
ATOM   5508  C  CE2   . TYR A 1 683 ? 136.258 129.781 106.018 1.00 18.00 ?  683 TYR A CE2   1 
ATOM   5509  C  CZ    . TYR A 1 683 ? 136.236 130.221 107.322 1.00 20.89 ?  683 TYR A CZ    1 
ATOM   5510  O  OH    . TYR A 1 683 ? 135.047 130.603 107.898 1.00 28.35 ?  683 TYR A OH    1 
ATOM   5511  N  N     . TYR A 1 684 ? 140.217 126.272 106.556 1.00 31.22 ?  684 TYR A N     1 
ATOM   5512  C  CA    . TYR A 1 684 ? 139.551 125.125 107.147 1.00 24.27 ?  684 TYR A CA    1 
ATOM   5513  C  C     . TYR A 1 684 ? 140.177 123.839 106.645 1.00 33.98 ?  684 TYR A C     1 
ATOM   5514  O  O     . TYR A 1 684 ? 140.672 123.766 105.518 1.00 35.72 ?  684 TYR A O     1 
ATOM   5515  C  CB    . TYR A 1 684 ? 138.051 125.122 106.832 1.00 27.98 ?  684 TYR A CB    1 
ATOM   5516  C  CG    . TYR A 1 684 ? 137.198 125.747 107.907 1.00 25.86 ?  684 TYR A CG    1 
ATOM   5517  C  CD1   . TYR A 1 684 ? 137.442 125.494 109.248 1.00 28.64 ?  684 TYR A CD1   1 
ATOM   5518  C  CD2   . TYR A 1 684 ? 136.146 126.589 107.581 1.00 27.48 ?  684 TYR A CD2   1 
ATOM   5519  C  CE1   . TYR A 1 684 ? 136.666 126.062 110.235 1.00 32.74 ?  684 TYR A CE1   1 
ATOM   5520  C  CE2   . TYR A 1 684 ? 135.364 127.165 108.559 1.00 26.81 ?  684 TYR A CE2   1 
ATOM   5521  C  CZ    . TYR A 1 684 ? 135.628 126.899 109.884 1.00 33.03 ?  684 TYR A CZ    1 
ATOM   5522  O  OH    . TYR A 1 684 ? 134.850 127.468 110.864 1.00 36.74 ?  684 TYR A OH    1 
ATOM   5523  N  N     . ALA A 1 685 ? 140.152 122.827 107.502 1.00 33.01 ?  685 ALA A N     1 
ATOM   5524  C  CA    . ALA A 1 685 ? 140.546 121.471 107.147 1.00 30.94 ?  685 ALA A CA    1 
ATOM   5525  C  C     . ALA A 1 685 ? 139.263 120.649 107.096 1.00 33.77 ?  685 ALA A C     1 
ATOM   5526  O  O     . ALA A 1 685 ? 138.882 120.002 108.073 1.00 41.20 ?  685 ALA A O     1 
ATOM   5527  C  CB    . ALA A 1 685 ? 141.547 120.910 108.145 1.00 31.56 ?  685 ALA A CB    1 
ATOM   5528  N  N     . ARG A 1 686 ? 138.593 120.686 105.948 1.00 34.12 ?  686 ARG A N     1 
ATOM   5529  C  CA    . ARG A 1 686 ? 137.345 119.963 105.754 1.00 35.47 ?  686 ARG A CA    1 
ATOM   5530  C  C     . ARG A 1 686 ? 137.643 118.537 105.318 1.00 39.33 ?  686 ARG A C     1 
ATOM   5531  O  O     . ARG A 1 686 ? 138.380 118.316 104.353 1.00 41.11 ?  686 ARG A O     1 
ATOM   5532  C  CB    . ARG A 1 686 ? 136.470 120.661 104.714 1.00 38.70 ?  686 ARG A CB    1 
ATOM   5533  C  CG    . ARG A 1 686 ? 135.709 121.857 105.245 1.00 41.76 ?  686 ARG A CG    1 
ATOM   5534  C  CD    . ARG A 1 686 ? 134.445 122.091 104.441 1.00 42.10 ?  686 ARG A CD    1 
ATOM   5535  N  NE    . ARG A 1 686 ? 133.674 120.864 104.285 1.00 43.83 ?  686 ARG A NE    1 
ATOM   5536  C  CZ    . ARG A 1 686 ? 132.373 120.764 104.521 1.00 44.76 ?  686 ARG A CZ    1 
ATOM   5537  N  NH1   . ARG A 1 686 ? 131.661 121.806 104.917 1.00 42.57 1  686 ARG A NH1   1 
ATOM   5538  N  NH2   . ARG A 1 686 ? 131.772 119.590 104.356 1.00 43.63 ?  686 ARG A NH2   1 
ATOM   5539  N  N     . THR A 1 687 ? 137.066 117.574 106.027 1.00 44.90 ?  687 THR A N     1 
ATOM   5540  C  CA    . THR A 1 687 ? 137.300 116.162 105.768 1.00 47.74 ?  687 THR A CA    1 
ATOM   5541  C  C     . THR A 1 687 ? 136.007 115.500 105.311 1.00 46.02 ?  687 THR A C     1 
ATOM   5542  O  O     . THR A 1 687 ? 134.934 115.767 105.859 1.00 49.65 ?  687 THR A O     1 
ATOM   5543  C  CB    . THR A 1 687 ? 137.842 115.461 107.018 1.00 47.73 ?  687 THR A CB    1 
ATOM   5544  O  OG1   . THR A 1 687 ? 139.077 116.073 107.411 1.00 47.03 ?  687 THR A OG1   1 
ATOM   5545  C  CG2   . THR A 1 687 ? 138.094 113.997 106.737 1.00 47.44 ?  687 THR A CG2   1 
ATOM   5546  N  N     . LYS A 1 688 ? 136.114 114.644 104.299 1.00 44.89 ?  688 LYS A N     1 
ATOM   5547  C  CA    . LYS A 1 688 ? 134.960 113.917 103.787 1.00 50.69 ?  688 LYS A CA    1 
ATOM   5548  C  C     . LYS A 1 688 ? 134.967 112.474 104.280 1.00 54.40 ?  688 LYS A C     1 
ATOM   5549  O  O     . LYS A 1 688 ? 136.008 111.946 104.669 1.00 56.78 ?  688 LYS A O     1 
ATOM   5550  C  CB    . LYS A 1 688 ? 134.936 113.950 102.258 1.00 49.89 ?  688 LYS A CB    1 
ATOM   5551  C  CG    . LYS A 1 688 ? 135.815 112.900 101.601 1.00 49.17 ?  688 LYS A CG    1 
ATOM   5552  C  CD    . LYS A 1 688 ? 135.349 112.581 100.189 1.00 51.52 ?  688 LYS A CD    1 
ATOM   5553  C  CE    . LYS A 1 688 ? 133.832 112.531 100.094 1.00 51.01 ?  688 LYS A CE    1 
ATOM   5554  N  NZ    . LYS A 1 688 ? 133.382 112.153 98.726  1.00 50.48 ?  688 LYS A NZ    1 
ATOM   5555  N  N     . VAL B 1 6   ? 153.690 117.233 164.945 1.00 58.06 ?  6   VAL B N     1 
ATOM   5556  C  CA    . VAL B 1 6   ? 152.607 118.009 165.537 1.00 60.47 ?  6   VAL B CA    1 
ATOM   5557  C  C     . VAL B 1 6   ? 153.171 119.106 166.433 1.00 60.85 ?  6   VAL B C     1 
ATOM   5558  O  O     . VAL B 1 6   ? 153.926 118.827 167.364 1.00 56.42 ?  6   VAL B O     1 
ATOM   5559  C  CB    . VAL B 1 6   ? 151.639 117.108 166.320 1.00 59.34 ?  6   VAL B CB    1 
ATOM   5560  C  CG1   . VAL B 1 6   ? 150.455 117.915 166.823 1.00 55.45 ?  6   VAL B CG1   1 
ATOM   5561  C  CG2   . VAL B 1 6   ? 151.170 115.953 165.451 1.00 59.30 ?  6   VAL B CG2   1 
ATOM   5562  N  N     . PRO B 1 7   ? 152.811 120.355 166.140 1.00 59.15 ?  7   PRO B N     1 
ATOM   5563  C  CA    . PRO B 1 7   ? 153.315 121.476 166.944 1.00 53.13 ?  7   PRO B CA    1 
ATOM   5564  C  C     . PRO B 1 7   ? 152.856 121.385 168.391 1.00 55.56 ?  7   PRO B C     1 
ATOM   5565  O  O     . PRO B 1 7   ? 151.804 120.824 168.701 1.00 60.63 ?  7   PRO B O     1 
ATOM   5566  C  CB    . PRO B 1 7   ? 152.724 122.708 166.253 1.00 52.80 ?  7   PRO B CB    1 
ATOM   5567  C  CG    . PRO B 1 7   ? 152.342 122.273 164.893 1.00 56.23 ?  7   PRO B CG    1 
ATOM   5568  C  CD    . PRO B 1 7   ? 152.149 120.791 164.899 1.00 56.88 ?  7   PRO B CD    1 
ATOM   5569  N  N     . LYS B 1 8   ? 153.678 121.943 169.284 1.00 55.11 ?  8   LYS B N     1 
ATOM   5570  C  CA    . LYS B 1 8   ? 153.361 121.910 170.708 1.00 54.87 ?  8   LYS B CA    1 
ATOM   5571  C  C     . LYS B 1 8   ? 152.070 122.659 171.009 1.00 57.26 ?  8   LYS B C     1 
ATOM   5572  O  O     . LYS B 1 8   ? 151.239 122.189 171.796 1.00 59.71 ?  8   LYS B O     1 
ATOM   5573  C  CB    . LYS B 1 8   ? 154.518 122.496 171.516 1.00 55.07 ?  8   LYS B CB    1 
ATOM   5574  C  CG    . LYS B 1 8   ? 154.505 122.109 172.985 1.00 55.73 ?  8   LYS B CG    1 
ATOM   5575  C  CD    . LYS B 1 8   ? 155.042 123.231 173.857 1.00 56.79 ?  8   LYS B CD    1 
ATOM   5576  C  CE    . LYS B 1 8   ? 154.384 123.229 175.226 1.00 58.05 ?  8   LYS B CE    1 
ATOM   5577  N  NZ    . LYS B 1 8   ? 155.238 123.883 176.256 1.00 56.65 1  8   LYS B NZ    1 
ATOM   5578  N  N     . TRP B 1 9   ? 151.882 123.828 170.392 1.00 58.22 ?  9   TRP B N     1 
ATOM   5579  C  CA    . TRP B 1 9   ? 150.647 124.574 170.603 1.00 51.60 ?  9   TRP B CA    1 
ATOM   5580  C  C     . TRP B 1 9   ? 149.444 123.839 170.030 1.00 51.94 ?  9   TRP B C     1 
ATOM   5581  O  O     . TRP B 1 9   ? 148.346 123.929 170.584 1.00 58.14 ?  9   TRP B O     1 
ATOM   5582  C  CB    . TRP B 1 9   ? 150.754 125.970 169.993 1.00 50.43 ?  9   TRP B CB    1 
ATOM   5583  C  CG    . TRP B 1 9   ? 151.122 125.988 168.542 1.00 48.99 ?  9   TRP B CG    1 
ATOM   5584  C  CD1   . TRP B 1 9   ? 150.267 125.975 167.482 1.00 48.05 ?  9   TRP B CD1   1 
ATOM   5585  C  CD2   . TRP B 1 9   ? 152.443 126.051 167.992 1.00 48.63 ?  9   TRP B CD2   1 
ATOM   5586  N  NE1   . TRP B 1 9   ? 150.971 126.014 166.305 1.00 47.61 ?  9   TRP B NE1   1 
ATOM   5587  C  CE2   . TRP B 1 9   ? 152.309 126.063 166.591 1.00 50.20 ?  9   TRP B CE2   1 
ATOM   5588  C  CE3   . TRP B 1 9   ? 153.724 126.092 168.548 1.00 45.96 ?  9   TRP B CE3   1 
ATOM   5589  C  CZ2   . TRP B 1 9   ? 153.408 126.112 165.737 1.00 49.91 ?  9   TRP B CZ2   1 
ATOM   5590  C  CZ3   . TRP B 1 9   ? 154.812 126.142 167.699 1.00 51.15 ?  9   TRP B CZ3   1 
ATOM   5591  C  CH2   . TRP B 1 9   ? 154.647 126.151 166.311 1.00 51.69 ?  9   TRP B CH2   1 
ATOM   5592  N  N     . ILE B 1 10  ? 149.627 123.114 168.926 1.00 52.13 ?  10  ILE B N     1 
ATOM   5593  C  CA    . ILE B 1 10  ? 148.528 122.333 168.369 1.00 53.51 ?  10  ILE B CA    1 
ATOM   5594  C  C     . ILE B 1 10  ? 148.156 121.195 169.311 1.00 54.08 ?  10  ILE B C     1 
ATOM   5595  O  O     . ILE B 1 10  ? 146.972 120.897 169.510 1.00 56.39 ?  10  ILE B O     1 
ATOM   5596  C  CB    . ILE B 1 10  ? 148.894 121.822 166.964 1.00 54.76 ?  10  ILE B CB    1 
ATOM   5597  C  CG1   . ILE B 1 10  ? 148.770 122.949 165.937 1.00 53.72 ?  10  ILE B CG1   1 
ATOM   5598  C  CG2   . ILE B 1 10  ? 148.004 120.660 166.567 1.00 55.30 ?  10  ILE B CG2   1 
ATOM   5599  C  CD1   . ILE B 1 10  ? 147.588 123.866 166.165 1.00 54.18 ?  10  ILE B CD1   1 
ATOM   5600  N  N     . GLN B 1 11  ? 149.155 120.546 169.913 1.00 57.56 ?  11  GLN B N     1 
ATOM   5601  C  CA    . GLN B 1 11  ? 148.871 119.514 170.904 1.00 57.04 ?  11  GLN B CA    1 
ATOM   5602  C  C     . GLN B 1 11  ? 148.139 120.094 172.107 1.00 59.28 ?  11  GLN B C     1 
ATOM   5603  O  O     . GLN B 1 11  ? 147.152 119.518 172.576 1.00 60.20 ?  11  GLN B O     1 
ATOM   5604  C  CB    . GLN B 1 11  ? 150.165 118.835 171.351 1.00 56.99 ?  11  GLN B CB    1 
ATOM   5605  C  CG    . GLN B 1 11  ? 150.610 117.684 170.468 1.00 60.82 ?  11  GLN B CG    1 
ATOM   5606  C  CD    . GLN B 1 11  ? 152.116 117.518 170.454 1.00 62.31 ?  11  GLN B CD    1 
ATOM   5607  O  OE1   . GLN B 1 11  ? 152.713 117.254 169.412 1.00 61.39 ?  11  GLN B OE1   1 
ATOM   5608  N  NE2   . GLN B 1 11  ? 152.740 117.675 171.615 1.00 60.14 ?  11  GLN B NE2   1 
ATOM   5609  N  N     . LEU B 1 12  ? 148.604 121.240 172.612 1.00 58.79 ?  12  LEU B N     1 
ATOM   5610  C  CA    . LEU B 1 12  ? 147.963 121.853 173.772 1.00 54.13 ?  12  LEU B CA    1 
ATOM   5611  C  C     . LEU B 1 12  ? 146.528 122.260 173.462 1.00 57.99 ?  12  LEU B C     1 
ATOM   5612  O  O     . LEU B 1 12  ? 145.632 122.099 174.298 1.00 60.10 ?  12  LEU B O     1 
ATOM   5613  C  CB    . LEU B 1 12  ? 148.771 123.061 174.243 1.00 55.26 ?  12  LEU B CB    1 
ATOM   5614  C  CG    . LEU B 1 12  ? 149.874 122.780 175.263 1.00 58.07 ?  12  LEU B CG    1 
ATOM   5615  C  CD1   . LEU B 1 12  ? 150.769 123.995 175.421 1.00 58.53 ?  12  LEU B CD1   1 
ATOM   5616  C  CD2   . LEU B 1 12  ? 149.277 122.372 176.596 1.00 56.30 ?  12  LEU B CD2   1 
ATOM   5617  N  N     . ASN B 1 13  ? 146.294 122.801 172.265 1.00 53.89 ?  13  ASN B N     1 
ATOM   5618  C  CA    . ASN B 1 13  ? 144.941 123.169 171.867 1.00 52.68 ?  13  ASN B CA    1 
ATOM   5619  C  C     . ASN B 1 13  ? 144.059 121.936 171.717 1.00 56.13 ?  13  ASN B C     1 
ATOM   5620  O  O     . ASN B 1 13  ? 142.843 122.005 171.928 1.00 62.41 ?  13  ASN B O     1 
ATOM   5621  C  CB    . ASN B 1 13  ? 144.987 123.969 170.565 1.00 53.91 ?  13  ASN B CB    1 
ATOM   5622  C  CG    . ASN B 1 13  ? 143.616 124.178 169.959 1.00 53.99 ?  13  ASN B CG    1 
ATOM   5623  O  OD1   . ASN B 1 13  ? 143.186 123.417 169.094 1.00 55.79 ?  13  ASN B OD1   1 
ATOM   5624  N  ND2   . ASN B 1 13  ? 142.922 125.215 170.409 1.00 54.99 ?  13  ASN B ND2   1 
ATOM   5625  N  N     . ASN B 1 14  ? 144.654 120.797 171.356 1.00 59.08 ?  14  ASN B N     1 
ATOM   5626  C  CA    . ASN B 1 14  ? 143.885 119.569 171.207 1.00 55.76 ?  14  ASN B CA    1 
ATOM   5627  C  C     . ASN B 1 14  ? 143.523 118.940 172.546 1.00 58.53 ?  14  ASN B C     1 
ATOM   5628  O  O     . ASN B 1 14  ? 142.640 118.078 172.588 1.00 63.28 ?  14  ASN B O     1 
ATOM   5629  C  CB    . ASN B 1 14  ? 144.661 118.566 170.354 1.00 59.59 ?  14  ASN B CB    1 
ATOM   5630  C  CG    . ASN B 1 14  ? 144.561 118.863 168.872 1.00 59.07 ?  14  ASN B CG    1 
ATOM   5631  O  OD1   . ASN B 1 14  ? 144.301 119.996 168.471 1.00 59.30 ?  14  ASN B OD1   1 
ATOM   5632  N  ND2   . ASN B 1 14  ? 144.770 117.843 168.050 1.00 58.70 ?  14  ASN B ND2   1 
ATOM   5633  N  N     . GLU B 1 15  ? 144.174 119.349 173.636 1.00 59.48 ?  15  GLU B N     1 
ATOM   5634  C  CA    . GLU B 1 15  ? 143.847 118.813 174.952 1.00 59.95 ?  15  GLU B CA    1 
ATOM   5635  C  C     . GLU B 1 15  ? 142.576 119.410 175.537 1.00 61.82 ?  15  GLU B C     1 
ATOM   5636  O  O     . GLU B 1 15  ? 142.156 118.984 176.618 1.00 64.87 ?  15  GLU B O     1 
ATOM   5637  C  CB    . GLU B 1 15  ? 145.005 119.036 175.930 1.00 60.50 ?  15  GLU B CB    1 
ATOM   5638  C  CG    . GLU B 1 15  ? 146.362 118.617 175.404 1.00 62.55 ?  15  GLU B CG    1 
ATOM   5639  C  CD    . GLU B 1 15  ? 147.432 118.637 176.476 1.00 66.42 ?  15  GLU B CD    1 
ATOM   5640  O  OE1   . GLU B 1 15  ? 147.076 118.627 177.672 1.00 64.42 ?  15  GLU B OE1   1 
ATOM   5641  O  OE2   . GLU B 1 15  ? 148.630 118.664 176.122 1.00 66.45 -1 15  GLU B OE2   1 
ATOM   5642  N  N     . ILE B 1 16  ? 141.968 120.389 174.867 1.00 60.94 ?  16  ILE B N     1 
ATOM   5643  C  CA    . ILE B 1 16  ? 140.685 120.913 175.324 1.00 60.27 ?  16  ILE B CA    1 
ATOM   5644  C  C     . ILE B 1 16  ? 139.621 119.824 175.272 1.00 60.83 ?  16  ILE B C     1 
ATOM   5645  O  O     . ILE B 1 16  ? 138.824 119.668 176.205 1.00 61.27 ?  16  ILE B O     1 
ATOM   5646  C  CB    . ILE B 1 16  ? 140.281 122.143 174.491 1.00 61.94 ?  16  ILE B CB    1 
ATOM   5647  C  CG1   . ILE B 1 16  ? 141.402 123.183 174.501 1.00 60.80 ?  16  ILE B CG1   1 
ATOM   5648  C  CG2   . ILE B 1 16  ? 138.985 122.740 175.016 1.00 60.34 ?  16  ILE B CG2   1 
ATOM   5649  C  CD1   . ILE B 1 16  ? 140.961 124.563 174.081 1.00 58.23 ?  16  ILE B CD1   1 
ATOM   5650  N  N     . MET B 1 17  ? 139.596 119.052 174.184 1.00 62.13 ?  17  MET B N     1 
ATOM   5651  C  CA    . MET B 1 17  ? 138.605 117.992 174.044 1.00 63.00 ?  17  MET B CA    1 
ATOM   5652  C  C     . MET B 1 17  ? 138.866 116.820 174.979 1.00 63.88 ?  17  MET B C     1 
ATOM   5653  O  O     . MET B 1 17  ? 137.936 116.061 175.270 1.00 65.86 ?  17  MET B O     1 
ATOM   5654  C  CB    . MET B 1 17  ? 138.561 117.496 172.599 1.00 63.13 ?  17  MET B CB    1 
ATOM   5655  C  CG    . MET B 1 17  ? 138.389 118.563 171.509 1.00 63.32 ?  17  MET B CG    1 
ATOM   5656  S  SD    . MET B 1 17  ? 136.833 119.489 171.382 1.00 70.70 ?  17  MET B SD    1 
ATOM   5657  C  CE    . MET B 1 17  ? 136.851 120.557 172.818 1.00 62.37 ?  17  MET B CE    1 
ATOM   5658  N  N     . ILE B 1 18  ? 140.100 116.648 175.447 1.00 63.36 ?  18  ILE B N     1 
ATOM   5659  C  CA    . ILE B 1 18  ? 140.386 115.607 176.429 1.00 63.14 ?  18  ILE B CA    1 
ATOM   5660  C  C     . ILE B 1 18  ? 139.695 116.010 177.727 1.00 63.69 ?  18  ILE B C     1 
ATOM   5661  O  O     . ILE B 1 18  ? 140.087 116.983 178.377 1.00 64.62 ?  18  ILE B O     1 
ATOM   5662  C  CB    . ILE B 1 18  ? 141.893 115.403 176.627 1.00 63.13 ?  18  ILE B CB    1 
ATOM   5663  C  CG1   . ILE B 1 18  ? 142.479 114.539 175.506 1.00 62.85 ?  18  ILE B CG1   1 
ATOM   5664  C  CG2   . ILE B 1 18  ? 142.172 114.728 177.961 1.00 63.54 ?  18  ILE B CG2   1 
ATOM   5665  C  CD1   . ILE B 1 18  ? 142.652 115.248 174.180 1.00 62.27 ?  18  ILE B CD1   1 
ATOM   5666  N  N     . GLN B 1 19  ? 138.648 115.278 178.094 1.00 68.67 ?  19  GLN B N     1 
ATOM   5667  C  CA    . GLN B 1 19  ? 137.819 115.646 179.233 1.00 69.55 ?  19  GLN B CA    1 
ATOM   5668  C  C     . GLN B 1 19  ? 138.477 115.170 180.521 1.00 70.48 ?  19  GLN B C     1 
ATOM   5669  O  O     . GLN B 1 19  ? 138.662 113.966 180.725 1.00 71.79 ?  19  GLN B O     1 
ATOM   5670  C  CB    . GLN B 1 19  ? 136.421 115.052 179.084 1.00 70.06 ?  19  GLN B CB    1 
ATOM   5671  C  CG    . GLN B 1 19  ? 135.488 115.889 178.224 1.00 69.09 ?  19  GLN B CG    1 
ATOM   5672  C  CD    . GLN B 1 19  ? 134.079 115.946 178.776 1.00 72.31 ?  19  GLN B CD    1 
ATOM   5673  O  OE1   . GLN B 1 19  ? 133.830 115.556 179.916 1.00 72.66 ?  19  GLN B OE1   1 
ATOM   5674  N  NE2   . GLN B 1 19  ? 133.147 116.435 177.966 1.00 69.92 ?  19  GLN B NE2   1 
ATOM   5675  N  N     . LYS B 1 20  ? 138.832 116.115 181.386 1.00 74.71 ?  20  LYS B N     1 
ATOM   5676  C  CA    . LYS B 1 20  ? 139.419 115.823 182.685 1.00 74.45 ?  20  LYS B CA    1 
ATOM   5677  C  C     . LYS B 1 20  ? 138.400 116.165 183.763 1.00 77.20 ?  20  LYS B C     1 
ATOM   5678  O  O     . LYS B 1 20  ? 137.889 117.290 183.802 1.00 74.44 ?  20  LYS B O     1 
ATOM   5679  C  CB    . LYS B 1 20  ? 140.713 116.611 182.891 1.00 71.73 ?  20  LYS B CB    1 
ATOM   5680  C  CG    . LYS B 1 20  ? 141.395 116.349 184.223 1.00 74.91 ?  20  LYS B CG    1 
ATOM   5681  C  CD    . LYS B 1 20  ? 142.228 117.541 184.667 1.00 75.30 ?  20  LYS B CD    1 
ATOM   5682  C  CE    . LYS B 1 20  ? 141.376 118.789 184.820 1.00 76.62 ?  20  LYS B CE    1 
ATOM   5683  N  NZ    . LYS B 1 20  ? 140.105 118.513 185.545 1.00 78.76 1  20  LYS B NZ    1 
ATOM   5684  N  N     . ASP B 1 21  ? 138.104 115.191 184.627 1.00 82.99 ?  21  ASP B N     1 
ATOM   5685  C  CA    . ASP B 1 21  ? 137.125 115.352 185.704 1.00 82.58 ?  21  ASP B CA    1 
ATOM   5686  C  C     . ASP B 1 21  ? 135.751 115.731 185.155 1.00 82.92 ?  21  ASP B C     1 
ATOM   5687  O  O     . ASP B 1 21  ? 135.016 116.519 185.753 1.00 82.22 ?  21  ASP B O     1 
ATOM   5688  C  CB    . ASP B 1 21  ? 137.605 116.375 186.739 1.00 82.38 ?  21  ASP B CB    1 
ATOM   5689  C  CG    . ASP B 1 21  ? 136.870 116.256 188.061 1.00 84.51 ?  21  ASP B CG    1 
ATOM   5690  O  OD1   . ASP B 1 21  ? 136.603 115.115 188.495 1.00 82.89 ?  21  ASP B OD1   1 
ATOM   5691  O  OD2   . ASP B 1 21  ? 136.560 117.304 188.666 1.00 84.64 -1 21  ASP B OD2   1 
ATOM   5692  N  N     . GLY B 1 22  ? 135.402 115.167 184.000 1.00 75.34 ?  22  GLY B N     1 
ATOM   5693  C  CA    . GLY B 1 22  ? 134.098 115.394 183.411 1.00 74.48 ?  22  GLY B CA    1 
ATOM   5694  C  C     . GLY B 1 22  ? 133.900 116.749 182.772 1.00 76.15 ?  22  GLY B C     1 
ATOM   5695  O  O     . GLY B 1 22  ? 132.762 117.093 182.433 1.00 75.95 ?  22  GLY B O     1 
ATOM   5696  N  N     . LYS B 1 23  ? 134.964 117.530 182.597 1.00 72.59 ?  23  LYS B N     1 
ATOM   5697  C  CA    . LYS B 1 23  ? 134.870 118.859 182.015 1.00 69.37 ?  23  LYS B CA    1 
ATOM   5698  C  C     . LYS B 1 23  ? 135.970 119.051 180.983 1.00 70.04 ?  23  LYS B C     1 
ATOM   5699  O  O     . LYS B 1 23  ? 137.054 118.472 181.091 1.00 69.80 ?  23  LYS B O     1 
ATOM   5700  C  CB    . LYS B 1 23  ? 134.978 119.953 183.085 1.00 68.27 ?  23  LYS B CB    1 
ATOM   5701  C  CG    . LYS B 1 23  ? 133.841 119.967 184.089 1.00 68.38 ?  23  LYS B CG    1 
ATOM   5702  C  CD    . LYS B 1 23  ? 134.001 121.119 185.064 1.00 68.60 ?  23  LYS B CD    1 
ATOM   5703  C  CE    . LYS B 1 23  ? 132.952 121.075 186.159 1.00 69.97 ?  23  LYS B CE    1 
ATOM   5704  N  NZ    . LYS B 1 23  ? 133.197 122.120 187.190 1.00 68.39 1  23  LYS B NZ    1 
ATOM   5705  N  N     . PHE B 1 24  ? 135.678 119.873 179.977 1.00 65.61 ?  24  PHE B N     1 
ATOM   5706  C  CA    . PHE B 1 24  ? 136.695 120.244 179.006 1.00 62.62 ?  24  PHE B CA    1 
ATOM   5707  C  C     . PHE B 1 24  ? 137.787 121.065 179.680 1.00 61.66 ?  24  PHE B C     1 
ATOM   5708  O  O     . PHE B 1 24  ? 137.534 121.835 180.610 1.00 61.85 ?  24  PHE B O     1 
ATOM   5709  C  CB    . PHE B 1 24  ? 136.082 121.047 177.857 1.00 61.12 ?  24  PHE B CB    1 
ATOM   5710  C  CG    . PHE B 1 24  ? 135.095 120.276 177.033 1.00 61.30 ?  24  PHE B CG    1 
ATOM   5711  C  CD1   . PHE B 1 24  ? 135.508 119.566 175.921 1.00 64.24 ?  24  PHE B CD1   1 
ATOM   5712  C  CD2   . PHE B 1 24  ? 133.749 120.279 177.358 1.00 61.65 ?  24  PHE B CD2   1 
ATOM   5713  C  CE1   . PHE B 1 24  ? 134.599 118.862 175.156 1.00 64.73 ?  24  PHE B CE1   1 
ATOM   5714  C  CE2   . PHE B 1 24  ? 132.837 119.576 176.596 1.00 62.37 ?  24  PHE B CE2   1 
ATOM   5715  C  CZ    . PHE B 1 24  ? 133.263 118.866 175.493 1.00 61.31 ?  24  PHE B CZ    1 
ATOM   5716  N  N     . GLN B 1 25  ? 139.020 120.894 179.204 1.00 62.73 ?  25  GLN B N     1 
ATOM   5717  C  CA    . GLN B 1 25  ? 140.158 121.648 179.730 1.00 63.64 ?  25  GLN B CA    1 
ATOM   5718  C  C     . GLN B 1 25  ? 140.253 122.961 178.961 1.00 64.69 ?  25  GLN B C     1 
ATOM   5719  O  O     . GLN B 1 25  ? 141.072 123.140 178.056 1.00 64.40 ?  25  GLN B O     1 
ATOM   5720  C  CB    . GLN B 1 25  ? 141.439 120.830 179.631 1.00 64.71 ?  25  GLN B CB    1 
ATOM   5721  C  CG    . GLN B 1 25  ? 141.471 119.625 180.558 1.00 62.14 ?  25  GLN B CG    1 
ATOM   5722  C  CD    . GLN B 1 25  ? 142.641 118.708 180.277 1.00 63.89 ?  25  GLN B CD    1 
ATOM   5723  O  OE1   . GLN B 1 25  ? 143.729 118.887 180.821 1.00 63.37 ?  25  GLN B OE1   1 
ATOM   5724  N  NE2   . GLN B 1 25  ? 142.423 117.718 179.421 1.00 64.37 ?  25  GLN B NE2   1 
ATOM   5725  N  N     . PHE B 1 26  ? 139.382 123.900 179.340 1.00 59.58 ?  26  PHE B N     1 
ATOM   5726  C  CA    . PHE B 1 26  ? 139.341 125.192 178.666 1.00 56.88 ?  26  PHE B CA    1 
ATOM   5727  C  C     . PHE B 1 26  ? 140.602 126.006 178.927 1.00 59.74 ?  26  PHE B C     1 
ATOM   5728  O  O     . PHE B 1 26  ? 140.979 126.841 178.098 1.00 60.98 ?  26  PHE B O     1 
ATOM   5729  C  CB    . PHE B 1 26  ? 138.106 125.974 179.108 1.00 52.78 ?  26  PHE B CB    1 
ATOM   5730  C  CG    . PHE B 1 26  ? 136.819 125.433 178.557 1.00 55.55 ?  26  PHE B CG    1 
ATOM   5731  C  CD1   . PHE B 1 26  ? 136.671 125.212 177.199 1.00 55.27 ?  26  PHE B CD1   1 
ATOM   5732  C  CD2   . PHE B 1 26  ? 135.758 125.143 179.398 1.00 54.50 ?  26  PHE B CD2   1 
ATOM   5733  C  CE1   . PHE B 1 26  ? 135.490 124.713 176.690 1.00 56.32 ?  26  PHE B CE1   1 
ATOM   5734  C  CE2   . PHE B 1 26  ? 134.574 124.645 178.892 1.00 52.70 ?  26  PHE B CE2   1 
ATOM   5735  C  CZ    . PHE B 1 26  ? 134.440 124.429 177.537 1.00 52.96 ?  26  PHE B CZ    1 
ATOM   5736  N  N     . ASP B 1 27  ? 141.262 125.777 180.064 1.00 63.05 ?  27  ASP B N     1 
ATOM   5737  C  CA    . ASP B 1 27  ? 142.483 126.501 180.396 1.00 58.55 ?  27  ASP B CA    1 
ATOM   5738  C  C     . ASP B 1 27  ? 143.661 126.108 179.516 1.00 60.78 ?  27  ASP B C     1 
ATOM   5739  O  O     . ASP B 1 27  ? 144.686 126.798 179.544 1.00 62.31 ?  27  ASP B O     1 
ATOM   5740  C  CB    . ASP B 1 27  ? 142.839 126.273 181.865 1.00 60.43 ?  27  ASP B CB    1 
ATOM   5741  C  CG    . ASP B 1 27  ? 141.640 126.405 182.782 1.00 65.03 ?  27  ASP B CG    1 
ATOM   5742  O  OD1   . ASP B 1 27  ? 140.582 125.821 182.465 1.00 65.00 ?  27  ASP B OD1   1 
ATOM   5743  O  OD2   . ASP B 1 27  ? 141.753 127.092 183.818 1.00 65.17 -1 27  ASP B OD2   1 
ATOM   5744  N  N     . LYS B 1 28  ? 143.547 125.026 178.744 1.00 60.48 ?  28  LYS B N     1 
ATOM   5745  C  CA    . LYS B 1 28  ? 144.634 124.623 177.860 1.00 61.30 ?  28  LYS B CA    1 
ATOM   5746  C  C     . LYS B 1 28  ? 144.822 125.583 176.695 1.00 61.69 ?  28  LYS B C     1 
ATOM   5747  O  O     . LYS B 1 28  ? 145.906 125.612 176.103 1.00 62.22 ?  28  LYS B O     1 
ATOM   5748  C  CB    . LYS B 1 28  ? 144.384 123.210 177.329 1.00 61.12 ?  28  LYS B CB    1 
ATOM   5749  C  CG    . LYS B 1 28  ? 144.632 122.114 178.348 1.00 61.20 ?  28  LYS B CG    1 
ATOM   5750  C  CD    . LYS B 1 28  ? 146.117 121.886 178.555 1.00 61.63 ?  28  LYS B CD    1 
ATOM   5751  C  CE    . LYS B 1 28  ? 146.379 121.059 179.801 1.00 61.66 ?  28  LYS B CE    1 
ATOM   5752  N  NZ    . LYS B 1 28  ? 147.812 120.681 179.917 1.00 59.46 1  28  LYS B NZ    1 
ATOM   5753  N  N     . ASP B 1 29  ? 143.797 126.368 176.353 1.00 58.24 ?  29  ASP B N     1 
ATOM   5754  C  CA    . ASP B 1 29  ? 143.926 127.291 175.233 1.00 55.40 ?  29  ASP B CA    1 
ATOM   5755  C  C     . ASP B 1 29  ? 144.830 128.469 175.577 1.00 55.16 ?  29  ASP B C     1 
ATOM   5756  O  O     . ASP B 1 29  ? 145.503 129.008 174.692 1.00 57.74 ?  29  ASP B O     1 
ATOM   5757  C  CB    . ASP B 1 29  ? 142.547 127.777 174.794 1.00 55.23 ?  29  ASP B CB    1 
ATOM   5758  C  CG    . ASP B 1 29  ? 142.368 127.733 173.290 1.00 58.52 ?  29  ASP B CG    1 
ATOM   5759  O  OD1   . ASP B 1 29  ? 141.534 128.498 172.765 1.00 55.50 ?  29  ASP B OD1   1 
ATOM   5760  O  OD2   . ASP B 1 29  ? 143.063 126.932 172.631 1.00 58.35 -1 29  ASP B OD2   1 
ATOM   5761  N  N     . LYS B 1 30  ? 144.853 128.886 176.845 1.00 55.30 ?  30  LYS B N     1 
ATOM   5762  C  CA    . LYS B 1 30  ? 145.841 129.873 177.273 1.00 56.62 ?  30  LYS B CA    1 
ATOM   5763  C  C     . LYS B 1 30  ? 147.251 129.309 177.164 1.00 56.50 ?  30  LYS B C     1 
ATOM   5764  O  O     . LYS B 1 30  ? 148.167 129.992 176.689 1.00 57.10 ?  30  LYS B O     1 
ATOM   5765  C  CB    . LYS B 1 30  ? 145.552 130.323 178.704 1.00 54.70 ?  30  LYS B CB    1 
ATOM   5766  C  CG    . LYS B 1 30  ? 144.253 131.091 178.865 1.00 56.61 ?  30  LYS B CG    1 
ATOM   5767  C  CD    . LYS B 1 30  ? 144.510 132.542 179.244 1.00 58.11 ?  30  LYS B CD    1 
ATOM   5768  C  CE    . LYS B 1 30  ? 145.586 132.655 180.314 1.00 58.82 ?  30  LYS B CE    1 
ATOM   5769  N  NZ    . LYS B 1 30  ? 145.634 134.016 180.917 1.00 58.06 1  30  LYS B NZ    1 
ATOM   5770  N  N     . GLU B 1 31  ? 147.441 128.061 177.593 1.00 57.78 ?  31  GLU B N     1 
ATOM   5771  C  CA    . GLU B 1 31  ? 148.720 127.397 177.381 1.00 54.53 ?  31  GLU B CA    1 
ATOM   5772  C  C     . GLU B 1 31  ? 149.003 127.232 175.894 1.00 55.31 ?  31  GLU B C     1 
ATOM   5773  O  O     . GLU B 1 31  ? 150.145 127.386 175.452 1.00 57.92 ?  31  GLU B O     1 
ATOM   5774  C  CB    . GLU B 1 31  ? 148.736 126.043 178.086 1.00 55.06 ?  31  GLU B CB    1 
ATOM   5775  C  CG    . GLU B 1 31  ? 148.723 126.131 179.602 1.00 56.40 ?  31  GLU B CG    1 
ATOM   5776  C  CD    . GLU B 1 31  ? 148.794 124.769 180.265 1.00 63.70 ?  31  GLU B CD    1 
ATOM   5777  O  OE1   . GLU B 1 31  ? 148.761 123.753 179.540 1.00 65.30 ?  31  GLU B OE1   1 
ATOM   5778  O  OE2   . GLU B 1 31  ? 148.883 124.715 181.509 1.00 60.64 -1 31  GLU B OE2   1 
ATOM   5779  N  N     . ALA B 1 32  ? 147.970 126.924 175.108 1.00 52.44 ?  32  ALA B N     1 
ATOM   5780  C  CA    . ALA B 1 32  ? 148.158 126.759 173.672 1.00 49.90 ?  32  ALA B CA    1 
ATOM   5781  C  C     . ALA B 1 32  ? 148.624 128.053 173.018 1.00 51.55 ?  32  ALA B C     1 
ATOM   5782  O  O     . ALA B 1 32  ? 149.560 128.043 172.215 1.00 52.12 ?  32  ALA B O     1 
ATOM   5783  C  CB    . ALA B 1 32  ? 146.864 126.268 173.023 1.00 49.16 ?  32  ALA B CB    1 
ATOM   5784  N  N     . VAL B 1 33  ? 147.992 129.181 173.354 1.00 54.60 ?  33  VAL B N     1 
ATOM   5785  C  CA    . VAL B 1 33  ? 148.385 130.447 172.741 1.00 50.88 ?  33  VAL B CA    1 
ATOM   5786  C  C     . VAL B 1 33  ? 149.753 130.891 173.249 1.00 53.80 ?  33  VAL B C     1 
ATOM   5787  O  O     . VAL B 1 33  ? 150.559 131.446 172.491 1.00 55.05 ?  33  VAL B O     1 
ATOM   5788  C  CB    . VAL B 1 33  ? 147.305 131.525 172.964 1.00 45.90 ?  33  VAL B CB    1 
ATOM   5789  C  CG1   . VAL B 1 33  ? 147.160 131.880 174.431 1.00 47.37 ?  33  VAL B CG1   1 
ATOM   5790  C  CG2   . VAL B 1 33  ? 147.618 132.765 172.140 1.00 49.25 ?  33  VAL B CG2   1 
ATOM   5791  N  N     . HIS B 1 34  ? 150.043 130.656 174.533 1.00 51.44 ?  34  HIS B N     1 
ATOM   5792  C  CA    . HIS B 1 34  ? 151.361 130.998 175.059 1.00 47.49 ?  34  HIS B CA    1 
ATOM   5793  C  C     . HIS B 1 34  ? 152.454 130.210 174.350 1.00 48.88 ?  34  HIS B C     1 
ATOM   5794  O  O     . HIS B 1 34  ? 153.490 130.765 173.966 1.00 52.29 ?  34  HIS B O     1 
ATOM   5795  C  CB    . HIS B 1 34  ? 151.408 130.744 176.565 1.00 52.36 ?  34  HIS B CB    1 
ATOM   5796  C  CG    . HIS B 1 34  ? 152.724 131.086 177.191 1.00 53.70 ?  34  HIS B CG    1 
ATOM   5797  N  ND1   . HIS B 1 34  ? 153.742 130.168 177.333 1.00 52.99 ?  34  HIS B ND1   1 
ATOM   5798  C  CD2   . HIS B 1 34  ? 153.188 132.246 177.713 1.00 53.10 ?  34  HIS B CD2   1 
ATOM   5799  C  CE1   . HIS B 1 34  ? 154.777 130.747 177.915 1.00 51.59 ?  34  HIS B CE1   1 
ATOM   5800  N  NE2   . HIS B 1 34  ? 154.466 132.007 178.158 1.00 53.65 ?  34  HIS B NE2   1 
ATOM   5801  N  N     . SER B 1 35  ? 152.236 128.905 174.165 1.00 54.75 ?  35  SER B N     1 
ATOM   5802  C  CA    . SER B 1 35  ? 153.203 128.085 173.447 1.00 52.29 ?  35  SER B CA    1 
ATOM   5803  C  C     . SER B 1 35  ? 153.319 128.521 171.995 1.00 52.81 ?  35  SER B C     1 
ATOM   5804  O  O     . SER B 1 35  ? 154.427 128.610 171.457 1.00 55.62 ?  35  SER B O     1 
ATOM   5805  C  CB    . SER B 1 35  ? 152.810 126.611 173.536 1.00 52.45 ?  35  SER B CB    1 
ATOM   5806  O  OG    . SER B 1 35  ? 153.714 125.801 172.805 1.00 56.52 ?  35  SER B OG    1 
ATOM   5807  N  N     . TYR B 1 36  ? 152.185 128.805 171.349 1.00 49.85 ?  36  TYR B N     1 
ATOM   5808  C  CA    . TYR B 1 36  ? 152.205 129.280 169.970 1.00 50.26 ?  36  TYR B CA    1 
ATOM   5809  C  C     . TYR B 1 36  ? 153.084 130.510 169.836 1.00 47.90 ?  36  TYR B C     1 
ATOM   5810  O  O     . TYR B 1 36  ? 154.003 130.544 169.010 1.00 49.13 ?  36  TYR B O     1 
ATOM   5811  C  CB    . TYR B 1 36  ? 150.782 129.589 169.505 1.00 45.19 ?  36  TYR B CB    1 
ATOM   5812  C  CG    . TYR B 1 36  ? 150.697 130.142 168.102 1.00 43.48 ?  36  TYR B CG    1 
ATOM   5813  C  CD1   . TYR B 1 36  ? 151.351 129.521 167.048 1.00 44.00 ?  36  TYR B CD1   1 
ATOM   5814  C  CD2   . TYR B 1 36  ? 149.964 131.290 167.832 1.00 45.84 ?  36  TYR B CD2   1 
ATOM   5815  C  CE1   . TYR B 1 36  ? 151.273 130.021 165.766 1.00 46.30 ?  36  TYR B CE1   1 
ATOM   5816  C  CE2   . TYR B 1 36  ? 149.882 131.799 166.552 1.00 44.51 ?  36  TYR B CE2   1 
ATOM   5817  C  CZ    . TYR B 1 36  ? 150.539 131.161 165.523 1.00 46.87 ?  36  TYR B CZ    1 
ATOM   5818  O  OH    . TYR B 1 36  ? 150.462 131.664 164.246 1.00 47.50 ?  36  TYR B OH    1 
ATOM   5819  N  N     . PHE B 1 37  ? 152.842 131.520 170.673 1.00 51.88 ?  37  PHE B N     1 
ATOM   5820  C  CA    . PHE B 1 37  ? 153.671 132.716 170.639 1.00 50.44 ?  37  PHE B CA    1 
ATOM   5821  C  C     . PHE B 1 37  ? 155.133 132.370 170.881 1.00 51.90 ?  37  PHE B C     1 
ATOM   5822  O  O     . PHE B 1 37  ? 155.961 132.498 169.974 1.00 55.87 ?  37  PHE B O     1 
ATOM   5823  C  CB    . PHE B 1 37  ? 153.172 133.737 171.658 1.00 52.29 ?  37  PHE B CB    1 
ATOM   5824  C  CG    . PHE B 1 37  ? 152.304 134.798 171.058 1.00 53.14 ?  37  PHE B CG    1 
ATOM   5825  C  CD1   . PHE B 1 37  ? 152.866 135.930 170.499 1.00 51.94 ?  37  PHE B CD1   1 
ATOM   5826  C  CD2   . PHE B 1 37  ? 150.930 134.655 171.032 1.00 52.91 ?  37  PHE B CD2   1 
ATOM   5827  C  CE1   . PHE B 1 37  ? 152.073 136.905 169.937 1.00 53.84 ?  37  PHE B CE1   1 
ATOM   5828  C  CE2   . PHE B 1 37  ? 150.134 135.627 170.473 1.00 51.40 ?  37  PHE B CE2   1 
ATOM   5829  C  CZ    . PHE B 1 37  ? 150.706 136.751 169.923 1.00 51.87 ?  37  PHE B CZ    1 
ATOM   5830  N  N     . VAL B 1 38  ? 155.439 131.835 172.067 1.00 55.94 ?  38  VAL B N     1 
ATOM   5831  C  CA    . VAL B 1 38  ? 156.819 131.671 172.515 1.00 56.74 ?  38  VAL B CA    1 
ATOM   5832  C  C     . VAL B 1 38  ? 157.622 130.780 171.571 1.00 55.35 ?  38  VAL B C     1 
ATOM   5833  O  O     . VAL B 1 38  ? 158.841 130.946 171.443 1.00 57.62 ?  38  VAL B O     1 
ATOM   5834  C  CB    . VAL B 1 38  ? 156.815 131.139 173.966 1.00 54.50 ?  38  VAL B CB    1 
ATOM   5835  C  CG1   . VAL B 1 38  ? 158.059 130.319 174.271 1.00 56.35 ?  38  VAL B CG1   1 
ATOM   5836  C  CG2   . VAL B 1 38  ? 156.682 132.292 174.947 1.00 52.68 ?  38  VAL B CG2   1 
ATOM   5837  N  N     . ASP B 1 39  ? 156.968 129.856 170.867 1.00 53.36 ?  39  ASP B N     1 
ATOM   5838  C  CA    . ASP B 1 39  ? 157.686 128.913 170.021 1.00 52.42 ?  39  ASP B CA    1 
ATOM   5839  C  C     . ASP B 1 39  ? 157.692 129.281 168.545 1.00 57.74 ?  39  ASP B C     1 
ATOM   5840  O  O     . ASP B 1 39  ? 158.622 128.887 167.834 1.00 61.98 ?  39  ASP B O     1 
ATOM   5841  C  CB    . ASP B 1 39  ? 157.093 127.508 170.177 1.00 55.14 ?  39  ASP B CB    1 
ATOM   5842  C  CG    . ASP B 1 39  ? 157.224 126.975 171.588 1.00 60.48 ?  39  ASP B CG    1 
ATOM   5843  O  OD1   . ASP B 1 39  ? 157.828 127.667 172.433 1.00 59.89 ?  39  ASP B OD1   1 
ATOM   5844  O  OD2   . ASP B 1 39  ? 156.724 125.863 171.855 1.00 62.77 -1 39  ASP B OD2   1 
ATOM   5845  N  N     . TYR B 1 40  ? 156.696 130.015 168.050 1.00 58.16 ?  40  TYR B N     1 
ATOM   5846  C  CA    . TYR B 1 40  ? 156.621 130.324 166.629 1.00 55.81 ?  40  TYR B CA    1 
ATOM   5847  C  C     . TYR B 1 40  ? 156.649 131.816 166.347 1.00 59.41 ?  40  TYR B C     1 
ATOM   5848  O  O     . TYR B 1 40  ? 157.403 132.262 165.473 1.00 62.58 ?  40  TYR B O     1 
ATOM   5849  C  CB    . TYR B 1 40  ? 155.348 129.701 166.033 1.00 52.29 ?  40  TYR B CB    1 
ATOM   5850  C  CG    . TYR B 1 40  ? 155.265 129.776 164.528 1.00 56.35 ?  40  TYR B CG    1 
ATOM   5851  C  CD1   . TYR B 1 40  ? 155.989 128.902 163.730 1.00 56.20 ?  40  TYR B CD1   1 
ATOM   5852  C  CD2   . TYR B 1 40  ? 154.457 130.717 163.905 1.00 58.17 ?  40  TYR B CD2   1 
ATOM   5853  C  CE1   . TYR B 1 40  ? 155.914 128.967 162.352 1.00 57.45 ?  40  TYR B CE1   1 
ATOM   5854  C  CE2   . TYR B 1 40  ? 154.375 130.788 162.530 1.00 57.38 ?  40  TYR B CE2   1 
ATOM   5855  C  CZ    . TYR B 1 40  ? 155.106 129.911 161.757 1.00 59.93 ?  40  TYR B CZ    1 
ATOM   5856  O  OH    . TYR B 1 40  ? 155.027 129.980 160.386 1.00 61.60 ?  40  TYR B OH    1 
ATOM   5857  N  N     . ILE B 1 41  ? 155.848 132.607 167.062 1.00 54.61 ?  41  ILE B N     1 
ATOM   5858  C  CA    . ILE B 1 41  ? 155.674 134.007 166.691 1.00 54.22 ?  41  ILE B CA    1 
ATOM   5859  C  C     . ILE B 1 41  ? 156.916 134.810 167.050 1.00 53.52 ?  41  ILE B C     1 
ATOM   5860  O  O     . ILE B 1 41  ? 157.444 135.565 166.229 1.00 56.05 ?  41  ILE B O     1 
ATOM   5861  C  CB    . ILE B 1 41  ? 154.412 134.588 167.354 1.00 52.78 ?  41  ILE B CB    1 
ATOM   5862  C  CG1   . ILE B 1 41  ? 153.167 133.834 166.887 1.00 50.99 ?  41  ILE B CG1   1 
ATOM   5863  C  CG2   . ILE B 1 41  ? 154.282 136.069 167.044 1.00 51.98 ?  41  ILE B CG2   1 
ATOM   5864  C  CD1   . ILE B 1 41  ? 153.031 133.756 165.385 1.00 49.66 ?  41  ILE B CD1   1 
ATOM   5865  N  N     . ASN B 1 42  ? 157.407 134.648 168.280 1.00 52.27 ?  42  ASN B N     1 
ATOM   5866  C  CA    . ASN B 1 42  ? 158.608 135.368 168.691 1.00 54.55 ?  42  ASN B CA    1 
ATOM   5867  C  C     . ASN B 1 42  ? 159.827 134.923 167.893 1.00 56.60 ?  42  ASN B C     1 
ATOM   5868  O  O     . ASN B 1 42  ? 160.777 135.697 167.735 1.00 58.07 ?  42  ASN B O     1 
ATOM   5869  C  CB    . ASN B 1 42  ? 158.849 135.178 170.187 1.00 55.05 ?  42  ASN B CB    1 
ATOM   5870  C  CG    . ASN B 1 42  ? 157.720 135.735 171.033 1.00 56.64 ?  42  ASN B CG    1 
ATOM   5871  O  OD1   . ASN B 1 42  ? 156.725 136.232 170.507 1.00 59.11 ?  42  ASN B OD1   1 
ATOM   5872  N  ND2   . ASN B 1 42  ? 157.873 135.661 172.349 1.00 58.92 ?  42  ASN B ND2   1 
ATOM   5873  N  N     . GLN B 1 43  ? 159.819 133.690 167.386 1.00 59.89 ?  43  GLN B N     1 
ATOM   5874  C  CA    . GLN B 1 43  ? 160.909 133.226 166.536 1.00 57.85 ?  43  GLN B CA    1 
ATOM   5875  C  C     . GLN B 1 43  ? 160.816 133.813 165.132 1.00 58.98 ?  43  GLN B C     1 
ATOM   5876  O  O     . GLN B 1 43  ? 161.839 134.150 164.529 1.00 61.60 ?  43  GLN B O     1 
ATOM   5877  C  CB    . GLN B 1 43  ? 160.911 131.698 166.472 1.00 57.38 ?  43  GLN B CB    1 
ATOM   5878  C  CG    . GLN B 1 43  ? 161.781 131.027 167.524 1.00 60.30 ?  43  GLN B CG    1 
ATOM   5879  C  CD    . GLN B 1 43  ? 161.280 131.266 168.933 1.00 62.50 ?  43  GLN B CD    1 
ATOM   5880  O  OE1   . GLN B 1 43  ? 160.116 131.607 169.140 1.00 62.16 ?  43  GLN B OE1   1 
ATOM   5881  N  NE2   . GLN B 1 43  ? 162.157 131.090 169.913 1.00 60.18 ?  43  GLN B NE2   1 
ATOM   5882  N  N     . ASN B 1 44  ? 159.601 133.943 164.600 1.00 54.48 ?  44  ASN B N     1 
ATOM   5883  C  CA    . ASN B 1 44  ? 159.393 134.380 163.227 1.00 56.91 ?  44  ASN B CA    1 
ATOM   5884  C  C     . ASN B 1 44  ? 159.048 135.860 163.120 1.00 57.23 ?  44  ASN B C     1 
ATOM   5885  O  O     . ASN B 1 44  ? 158.702 136.325 162.030 1.00 55.75 ?  44  ASN B O     1 
ATOM   5886  C  CB    . ASN B 1 44  ? 158.297 133.540 162.566 1.00 54.58 ?  44  ASN B CB    1 
ATOM   5887  C  CG    . ASN B 1 44  ? 158.697 132.086 162.397 1.00 58.80 ?  44  ASN B CG    1 
ATOM   5888  O  OD1   . ASN B 1 44  ? 158.815 131.591 161.276 1.00 62.13 ?  44  ASN B OD1   1 
ATOM   5889  N  ND2   . ASN B 1 44  ? 158.896 131.389 163.510 1.00 57.89 ?  44  ASN B ND2   1 
ATOM   5890  N  N     . THR B 1 45  ? 159.135 136.608 164.215 1.00 57.35 ?  45  THR B N     1 
ATOM   5891  C  CA    . THR B 1 45  ? 158.885 138.043 164.193 1.00 58.16 ?  45  THR B CA    1 
ATOM   5892  C  C     . THR B 1 45  ? 160.199 138.775 163.955 1.00 57.10 ?  45  THR B C     1 
ATOM   5893  O  O     . THR B 1 45  ? 161.129 138.668 164.760 1.00 58.92 ?  45  THR B O     1 
ATOM   5894  C  CB    . THR B 1 45  ? 158.249 138.511 165.501 1.00 56.69 ?  45  THR B CB    1 
ATOM   5895  O  OG1   . THR B 1 45  ? 156.950 137.923 165.642 1.00 60.69 ?  45  THR B OG1   1 
ATOM   5896  C  CG2   . THR B 1 45  ? 158.121 140.026 165.518 1.00 54.98 ?  45  THR B CG2   1 
ATOM   5897  N  N     . VAL B 1 46  ? 160.277 139.513 162.847 1.00 56.57 ?  46  VAL B N     1 
ATOM   5898  C  CA    . VAL B 1 46  ? 161.451 140.333 162.582 1.00 56.20 ?  46  VAL B CA    1 
ATOM   5899  C  C     . VAL B 1 46  ? 161.531 141.432 163.630 1.00 57.03 ?  46  VAL B C     1 
ATOM   5900  O  O     . VAL B 1 46  ? 160.570 142.181 163.843 1.00 58.62 ?  46  VAL B O     1 
ATOM   5901  C  CB    . VAL B 1 46  ? 161.397 140.922 161.166 1.00 54.12 ?  46  VAL B CB    1 
ATOM   5902  C  CG1   . VAL B 1 46  ? 162.648 141.738 160.885 1.00 54.46 ?  46  VAL B CG1   1 
ATOM   5903  C  CG2   . VAL B 1 46  ? 161.238 139.823 160.142 1.00 54.07 ?  46  VAL B CG2   1 
ATOM   5904  N  N     . PHE B 1 47  ? 162.677 141.532 164.292 1.00 61.45 ?  47  PHE B N     1 
ATOM   5905  C  CA    . PHE B 1 47  ? 162.894 142.532 165.323 1.00 63.31 ?  47  PHE B CA    1 
ATOM   5906  C  C     . PHE B 1 47  ? 163.932 143.539 164.854 1.00 64.07 ?  47  PHE B C     1 
ATOM   5907  O  O     . PHE B 1 47  ? 164.902 143.181 164.178 1.00 63.48 ?  47  PHE B O     1 
ATOM   5908  C  CB    . PHE B 1 47  ? 163.342 141.892 166.636 1.00 62.59 ?  47  PHE B CB    1 
ATOM   5909  C  CG    . PHE B 1 47  ? 163.288 142.824 167.811 1.00 64.31 ?  47  PHE B CG    1 
ATOM   5910  C  CD1   . PHE B 1 47  ? 162.076 143.162 168.387 1.00 62.63 ?  47  PHE B CD1   1 
ATOM   5911  C  CD2   . PHE B 1 47  ? 164.449 143.365 168.337 1.00 63.97 ?  47  PHE B CD2   1 
ATOM   5912  C  CE1   . PHE B 1 47  ? 162.021 144.022 169.467 1.00 64.84 ?  47  PHE B CE1   1 
ATOM   5913  C  CE2   . PHE B 1 47  ? 164.402 144.225 169.417 1.00 63.35 ?  47  PHE B CE2   1 
ATOM   5914  C  CZ    . PHE B 1 47  ? 163.186 144.555 169.983 1.00 64.46 ?  47  PHE B CZ    1 
ATOM   5915  N  N     . PHE B 1 48  ? 163.717 144.799 165.214 1.00 61.83 ?  48  PHE B N     1 
ATOM   5916  C  CA    . PHE B 1 48  ? 164.607 145.890 164.863 1.00 57.75 ?  48  PHE B CA    1 
ATOM   5917  C  C     . PHE B 1 48  ? 165.098 146.557 166.139 1.00 60.79 ?  48  PHE B C     1 
ATOM   5918  O  O     . PHE B 1 48  ? 164.432 146.505 167.178 1.00 61.58 ?  48  PHE B O     1 
ATOM   5919  C  CB    . PHE B 1 48  ? 163.908 146.919 163.964 1.00 58.73 ?  48  PHE B CB    1 
ATOM   5920  C  CG    . PHE B 1 48  ? 163.361 146.345 162.685 1.00 57.73 ?  48  PHE B CG    1 
ATOM   5921  C  CD1   . PHE B 1 48  ? 162.194 145.599 162.683 1.00 57.85 ?  48  PHE B CD1   1 
ATOM   5922  C  CD2   . PHE B 1 48  ? 164.009 146.562 161.482 1.00 60.31 ?  48  PHE B CD2   1 
ATOM   5923  C  CE1   . PHE B 1 48  ? 161.690 145.079 161.508 1.00 59.31 ?  48  PHE B CE1   1 
ATOM   5924  C  CE2   . PHE B 1 48  ? 163.508 146.044 160.305 1.00 60.19 ?  48  PHE B CE2   1 
ATOM   5925  C  CZ    . PHE B 1 48  ? 162.347 145.301 160.319 1.00 57.88 ?  48  PHE B CZ    1 
ATOM   5926  N  N     . HIS B 1 49  ? 166.277 147.177 166.056 1.00 65.61 ?  49  HIS B N     1 
ATOM   5927  C  CA    . HIS B 1 49  ? 166.869 147.794 167.237 1.00 65.59 ?  49  HIS B CA    1 
ATOM   5928  C  C     . HIS B 1 49  ? 165.984 148.909 167.781 1.00 67.22 ?  49  HIS B C     1 
ATOM   5929  O  O     . HIS B 1 49  ? 165.841 149.061 168.999 1.00 67.83 ?  49  HIS B O     1 
ATOM   5930  C  CB    . HIS B 1 49  ? 168.264 148.325 166.908 1.00 66.47 ?  49  HIS B CB    1 
ATOM   5931  C  CG    . HIS B 1 49  ? 169.141 148.501 168.109 1.00 70.11 ?  49  HIS B CG    1 
ATOM   5932  N  ND1   . HIS B 1 49  ? 168.894 149.449 169.080 1.00 69.32 ?  49  HIS B ND1   1 
ATOM   5933  C  CD2   . HIS B 1 49  ? 170.261 147.849 168.498 1.00 69.08 ?  49  HIS B CD2   1 
ATOM   5934  C  CE1   . HIS B 1 49  ? 169.825 149.373 170.013 1.00 68.02 ?  49  HIS B CE1   1 
ATOM   5935  N  NE2   . HIS B 1 49  ? 170.667 148.410 169.684 1.00 68.93 ?  49  HIS B NE2   1 
ATOM   5936  N  N     . ASN B 1 50  ? 165.382 149.696 166.894 1.00 65.61 ?  50  ASN B N     1 
ATOM   5937  C  CA    . ASN B 1 50  ? 164.490 150.773 167.292 1.00 63.02 ?  50  ASN B CA    1 
ATOM   5938  C  C     . ASN B 1 50  ? 163.295 150.801 166.352 1.00 61.96 ?  50  ASN B C     1 
ATOM   5939  O  O     . ASN B 1 50  ? 163.309 150.197 165.278 1.00 61.45 ?  50  ASN B O     1 
ATOM   5940  C  CB    . ASN B 1 50  ? 165.206 152.129 167.289 1.00 61.90 ?  50  ASN B CB    1 
ATOM   5941  C  CG    . ASN B 1 50  ? 166.021 152.353 166.032 1.00 63.89 ?  50  ASN B CG    1 
ATOM   5942  O  OD1   . ASN B 1 50  ? 165.472 152.600 164.960 1.00 64.93 ?  50  ASN B OD1   1 
ATOM   5943  N  ND2   . ASN B 1 50  ? 167.338 152.266 166.159 1.00 64.38 ?  50  ASN B ND2   1 
ATOM   5944  N  N     . LEU B 1 51  ? 162.246 151.507 166.781 1.00 58.68 ?  51  LEU B N     1 
ATOM   5945  C  CA    . LEU B 1 51  ? 161.062 151.654 165.942 1.00 58.75 ?  51  LEU B CA    1 
ATOM   5946  C  C     . LEU B 1 51  ? 161.371 152.437 164.672 1.00 60.56 ?  51  LEU B C     1 
ATOM   5947  O  O     . LEU B 1 51  ? 160.745 152.201 163.633 1.00 62.00 ?  51  LEU B O     1 
ATOM   5948  C  CB    . LEU B 1 51  ? 159.943 152.334 166.730 1.00 58.13 ?  51  LEU B CB    1 
ATOM   5949  C  CG    . LEU B 1 51  ? 158.653 152.666 165.977 1.00 57.06 ?  51  LEU B CG    1 
ATOM   5950  C  CD1   . LEU B 1 51  ? 158.032 151.413 165.381 1.00 54.72 ?  51  LEU B CD1   1 
ATOM   5951  C  CD2   . LEU B 1 51  ? 157.672 153.372 166.892 1.00 57.42 ?  51  LEU B CD2   1 
ATOM   5952  N  N     . LYS B 1 52  ? 162.326 153.368 164.736 1.00 59.05 ?  52  LYS B N     1 
ATOM   5953  C  CA    . LYS B 1 52  ? 162.695 154.136 163.550 1.00 57.11 ?  52  LYS B CA    1 
ATOM   5954  C  C     . LYS B 1 52  ? 163.240 153.230 162.454 1.00 60.44 ?  52  LYS B C     1 
ATOM   5955  O  O     . LYS B 1 52  ? 162.886 153.384 161.279 1.00 61.28 ?  52  LYS B O     1 
ATOM   5956  C  CB    . LYS B 1 52  ? 163.721 155.204 163.920 1.00 56.54 ?  52  LYS B CB    1 
ATOM   5957  C  CG    . LYS B 1 52  ? 163.680 156.442 163.043 1.00 60.79 ?  52  LYS B CG    1 
ATOM   5958  C  CD    . LYS B 1 52  ? 164.837 157.376 163.363 1.00 63.71 ?  52  LYS B CD    1 
ATOM   5959  C  CE    . LYS B 1 52  ? 164.546 158.216 164.595 1.00 60.86 ?  52  LYS B CE    1 
ATOM   5960  N  NZ    . LYS B 1 52  ? 165.700 158.249 165.534 1.00 61.13 1  52  LYS B NZ    1 
ATOM   5961  N  N     . GLU B 1 53  ? 164.103 152.279 162.820 1.00 62.10 ?  53  GLU B N     1 
ATOM   5962  C  CA    . GLU B 1 53  ? 164.648 151.355 161.832 1.00 60.79 ?  53  GLU B CA    1 
ATOM   5963  C  C     . GLU B 1 53  ? 163.552 150.494 161.220 1.00 61.00 ?  53  GLU B C     1 
ATOM   5964  O  O     . GLU B 1 53  ? 163.541 150.260 160.005 1.00 61.80 ?  53  GLU B O     1 
ATOM   5965  C  CB    . GLU B 1 53  ? 165.724 150.479 162.472 1.00 60.31 ?  53  GLU B CB    1 
ATOM   5966  C  CG    . GLU B 1 53  ? 166.665 149.826 161.474 1.00 62.43 ?  53  GLU B CG    1 
ATOM   5967  C  CD    . GLU B 1 53  ? 166.939 148.372 161.798 1.00 65.53 ?  53  GLU B CD    1 
ATOM   5968  O  OE1   . GLU B 1 53  ? 167.099 148.046 162.993 1.00 66.13 ?  53  GLU B OE1   1 
ATOM   5969  O  OE2   . GLU B 1 53  ? 166.997 147.553 160.857 1.00 64.07 -1 53  GLU B OE2   1 
ATOM   5970  N  N     . LYS B 1 54  ? 162.617 150.016 162.045 1.00 58.53 ?  54  LYS B N     1 
ATOM   5971  C  CA    . LYS B 1 54  ? 161.514 149.207 161.535 1.00 58.25 ?  54  LYS B CA    1 
ATOM   5972  C  C     . LYS B 1 54  ? 160.654 150.006 160.566 1.00 54.87 ?  54  LYS B C     1 
ATOM   5973  O  O     . LYS B 1 54  ? 160.292 149.520 159.488 1.00 56.61 ?  54  LYS B O     1 
ATOM   5974  C  CB    . LYS B 1 54  ? 160.669 148.685 162.695 1.00 56.86 ?  54  LYS B CB    1 
ATOM   5975  C  CG    . LYS B 1 54  ? 159.351 148.068 162.265 1.00 56.41 ?  54  LYS B CG    1 
ATOM   5976  C  CD    . LYS B 1 54  ? 158.673 147.353 163.417 1.00 57.38 ?  54  LYS B CD    1 
ATOM   5977  C  CE    . LYS B 1 54  ? 157.359 146.733 162.978 1.00 59.39 ?  54  LYS B CE    1 
ATOM   5978  N  NZ    . LYS B 1 54  ? 156.932 145.638 163.892 1.00 59.58 1  54  LYS B NZ    1 
ATOM   5979  N  N     . LEU B 1 55  ? 160.321 151.244 160.935 1.00 55.55 ?  55  LEU B N     1 
ATOM   5980  C  CA    . LEU B 1 55  ? 159.494 152.075 160.068 1.00 56.17 ?  55  LEU B CA    1 
ATOM   5981  C  C     . LEU B 1 55  ? 160.203 152.381 158.758 1.00 59.21 ?  55  LEU B C     1 
ATOM   5982  O  O     . LEU B 1 55  ? 159.584 152.346 157.690 1.00 63.12 ?  55  LEU B O     1 
ATOM   5983  C  CB    . LEU B 1 55  ? 159.113 153.367 160.789 1.00 57.73 ?  55  LEU B CB    1 
ATOM   5984  C  CG    . LEU B 1 55  ? 158.064 153.224 161.892 1.00 57.81 ?  55  LEU B CG    1 
ATOM   5985  C  CD1   . LEU B 1 55  ? 157.896 154.536 162.631 1.00 58.16 ?  55  LEU B CD1   1 
ATOM   5986  C  CD2   . LEU B 1 55  ? 156.737 152.753 161.314 1.00 57.18 ?  55  LEU B CD2   1 
ATOM   5987  N  N     . ASP B 1 56  ? 161.504 152.686 158.822 1.00 60.82 ?  56  ASP B N     1 
ATOM   5988  C  CA    . ASP B 1 56  ? 162.266 152.960 157.608 1.00 60.69 ?  56  ASP B CA    1 
ATOM   5989  C  C     . ASP B 1 56  ? 162.326 151.734 156.708 1.00 59.63 ?  56  ASP B C     1 
ATOM   5990  O  O     . ASP B 1 56  ? 162.158 151.842 155.486 1.00 62.40 ?  56  ASP B O     1 
ATOM   5991  C  CB    . ASP B 1 56  ? 163.674 153.430 157.970 1.00 62.18 ?  56  ASP B CB    1 
ATOM   5992  C  CG    . ASP B 1 56  ? 163.764 154.935 158.121 1.00 64.79 ?  56  ASP B CG    1 
ATOM   5993  O  OD1   . ASP B 1 56  ? 164.709 155.411 158.784 1.00 65.13 ?  56  ASP B OD1   1 
ATOM   5994  O  OD2   . ASP B 1 56  ? 162.890 155.641 157.576 1.00 63.28 -1 56  ASP B OD2   1 
ATOM   5995  N  N     . TYR B 1 57  ? 162.555 150.556 157.294 1.00 55.20 ?  57  TYR B N     1 
ATOM   5996  C  CA    . TYR B 1 57  ? 162.561 149.325 156.513 1.00 56.47 ?  57  TYR B CA    1 
ATOM   5997  C  C     . TYR B 1 57  ? 161.210 149.088 155.855 1.00 57.12 ?  57  TYR B C     1 
ATOM   5998  O  O     . TYR B 1 57  ? 161.142 148.661 154.699 1.00 58.36 ?  57  TYR B O     1 
ATOM   5999  C  CB    . TYR B 1 57  ? 162.939 148.141 157.404 1.00 57.82 ?  57  TYR B CB    1 
ATOM   6000  C  CG    . TYR B 1 57  ? 162.799 146.790 156.735 1.00 57.26 ?  57  TYR B CG    1 
ATOM   6001  C  CD1   . TYR B 1 57  ? 163.822 146.270 155.955 1.00 57.59 ?  57  TYR B CD1   1 
ATOM   6002  C  CD2   . TYR B 1 57  ? 161.646 146.030 156.892 1.00 58.80 ?  57  TYR B CD2   1 
ATOM   6003  C  CE1   . TYR B 1 57  ? 163.699 145.038 155.344 1.00 57.28 ?  57  TYR B CE1   1 
ATOM   6004  C  CE2   . TYR B 1 57  ? 161.514 144.800 156.285 1.00 59.93 ?  57  TYR B CE2   1 
ATOM   6005  C  CZ    . TYR B 1 57  ? 162.543 144.307 155.513 1.00 60.41 ?  57  TYR B CZ    1 
ATOM   6006  O  OH    . TYR B 1 57  ? 162.412 143.078 154.908 1.00 60.67 ?  57  TYR B OH    1 
ATOM   6007  N  N     . LEU B 1 58  ? 160.123 149.358 156.578 1.00 55.53 ?  58  LEU B N     1 
ATOM   6008  C  CA    . LEU B 1 58  ? 158.801 149.081 156.032 1.00 55.09 ?  58  LEU B CA    1 
ATOM   6009  C  C     . LEU B 1 58  ? 158.434 150.058 154.920 1.00 52.51 ?  58  LEU B C     1 
ATOM   6010  O  O     . LEU B 1 58  ? 157.843 149.655 153.911 1.00 54.87 ?  58  LEU B O     1 
ATOM   6011  C  CB    . LEU B 1 58  ? 157.761 149.098 157.151 1.00 53.67 ?  58  LEU B CB    1 
ATOM   6012  C  CG    . LEU B 1 58  ? 157.885 147.900 158.098 1.00 53.10 ?  58  LEU B CG    1 
ATOM   6013  C  CD1   . LEU B 1 58  ? 157.071 148.095 159.363 1.00 53.31 ?  58  LEU B CD1   1 
ATOM   6014  C  CD2   . LEU B 1 58  ? 157.482 146.616 157.393 1.00 51.72 ?  58  LEU B CD2   1 
ATOM   6015  N  N     . VAL B 1 59  ? 158.768 151.342 155.072 1.00 55.94 ?  59  VAL B N     1 
ATOM   6016  C  CA    . VAL B 1 59  ? 158.419 152.292 154.017 1.00 59.41 ?  59  VAL B CA    1 
ATOM   6017  C  C     . VAL B 1 59  ? 159.307 152.088 152.796 1.00 61.68 ?  59  VAL B C     1 
ATOM   6018  O  O     . VAL B 1 59  ? 158.832 152.129 151.655 1.00 58.99 ?  59  VAL B O     1 
ATOM   6019  C  CB    . VAL B 1 59  ? 158.484 153.749 154.518 1.00 58.77 ?  59  VAL B CB    1 
ATOM   6020  C  CG1   . VAL B 1 59  ? 157.261 154.084 155.367 1.00 57.57 ?  59  VAL B CG1   1 
ATOM   6021  C  CG2   . VAL B 1 59  ? 159.789 154.049 155.232 1.00 59.07 ?  59  VAL B CG2   1 
ATOM   6022  N  N     . GLU B 1 60  ? 160.609 151.865 153.008 1.00 62.25 ?  60  GLU B N     1 
ATOM   6023  C  CA    . GLU B 1 60  ? 161.534 151.791 151.882 1.00 60.57 ?  60  GLU B CA    1 
ATOM   6024  C  C     . GLU B 1 60  ? 161.426 150.475 151.122 1.00 61.73 ?  60  GLU B C     1 
ATOM   6025  O  O     . GLU B 1 60  ? 161.747 150.430 149.930 1.00 64.04 ?  60  GLU B O     1 
ATOM   6026  C  CB    . GLU B 1 60  ? 162.970 152.019 152.366 1.00 60.61 ?  60  GLU B CB    1 
ATOM   6027  C  CG    . GLU B 1 60  ? 163.698 150.773 152.831 1.00 61.74 ?  60  GLU B CG    1 
ATOM   6028  C  CD    . GLU B 1 60  ? 164.930 151.093 153.656 1.00 64.83 ?  60  GLU B CD    1 
ATOM   6029  O  OE1   . GLU B 1 60  ? 165.223 152.293 153.848 1.00 64.26 ?  60  GLU B OE1   1 
ATOM   6030  O  OE2   . GLU B 1 60  ? 165.603 150.148 154.115 1.00 61.61 -1 60  GLU B OE2   1 
ATOM   6031  N  N     . ASN B 1 61  ? 160.981 149.402 151.776 1.00 57.46 ?  61  ASN B N     1 
ATOM   6032  C  CA    . ASN B 1 61  ? 160.808 148.112 151.121 1.00 57.98 ?  61  ASN B CA    1 
ATOM   6033  C  C     . ASN B 1 61  ? 159.402 147.918 150.568 1.00 57.86 ?  61  ASN B C     1 
ATOM   6034  O  O     . ASN B 1 61  ? 158.984 146.773 150.355 1.00 59.49 ?  61  ASN B O     1 
ATOM   6035  C  CB    . ASN B 1 61  ? 161.155 146.973 152.082 1.00 59.20 ?  61  ASN B CB    1 
ATOM   6036  C  CG    . ASN B 1 61  ? 162.647 146.747 152.200 1.00 61.20 ?  61  ASN B CG    1 
ATOM   6037  O  OD1   . ASN B 1 61  ? 163.210 145.882 151.531 1.00 60.39 ?  61  ASN B OD1   1 
ATOM   6038  N  ND2   . ASN B 1 61  ? 163.296 147.527 153.054 1.00 60.53 ?  61  ASN B ND2   1 
ATOM   6039  N  N     . GLN B 1 62  ? 158.668 149.008 150.341 1.00 56.47 ?  62  GLN B N     1 
ATOM   6040  C  CA    . GLN B 1 62  ? 157.347 148.969 149.710 1.00 58.76 ?  62  GLN B CA    1 
ATOM   6041  C  C     . GLN B 1 62  ? 156.351 148.146 150.525 1.00 57.86 ?  62  GLN B C     1 
ATOM   6042  O  O     . GLN B 1 62  ? 155.566 147.369 149.977 1.00 59.50 ?  62  GLN B O     1 
ATOM   6043  C  CB    . GLN B 1 62  ? 157.437 148.447 148.274 1.00 58.26 ?  62  GLN B CB    1 
ATOM   6044  C  CG    . GLN B 1 62  ? 158.396 149.227 147.388 1.00 58.23 ?  62  GLN B CG    1 
ATOM   6045  C  CD    . GLN B 1 62  ? 158.062 150.704 147.328 1.00 61.67 ?  62  GLN B CD    1 
ATOM   6046  O  OE1   . GLN B 1 62  ? 158.647 151.516 148.043 1.00 60.56 ?  62  GLN B OE1   1 
ATOM   6047  N  NE2   . GLN B 1 62  ? 157.113 151.060 146.470 1.00 59.67 ?  62  GLN B NE2   1 
ATOM   6048  N  N     . TYR B 1 63  ? 156.380 148.317 151.844 1.00 56.30 ?  63  TYR B N     1 
ATOM   6049  C  CA    . TYR B 1 63  ? 155.401 147.695 152.728 1.00 55.71 ?  63  TYR B CA    1 
ATOM   6050  C  C     . TYR B 1 63  ? 154.358 148.680 153.235 1.00 54.98 ?  63  TYR B C     1 
ATOM   6051  O  O     . TYR B 1 63  ? 153.175 148.336 153.310 1.00 55.89 ?  63  TYR B O     1 
ATOM   6052  C  CB    . TYR B 1 63  ? 156.098 147.040 153.926 1.00 52.99 ?  63  TYR B CB    1 
ATOM   6053  C  CG    . TYR B 1 63  ? 156.817 145.755 153.594 1.00 55.76 ?  63  TYR B CG    1 
ATOM   6054  C  CD1   . TYR B 1 63  ? 156.140 144.687 153.021 1.00 53.23 ?  63  TYR B CD1   1 
ATOM   6055  C  CD2   . TYR B 1 63  ? 158.171 145.607 153.859 1.00 55.99 ?  63  TYR B CD2   1 
ATOM   6056  C  CE1   . TYR B 1 63  ? 156.793 143.511 152.719 1.00 54.08 ?  63  TYR B CE1   1 
ATOM   6057  C  CE2   . TYR B 1 63  ? 158.831 144.435 153.561 1.00 55.25 ?  63  TYR B CE2   1 
ATOM   6058  C  CZ    . TYR B 1 63  ? 158.138 143.390 152.992 1.00 58.33 ?  63  TYR B CZ    1 
ATOM   6059  O  OH    . TYR B 1 63  ? 158.796 142.220 152.693 1.00 61.61 ?  63  TYR B OH    1 
ATOM   6060  N  N     . TYR B 1 64  ? 154.770 149.894 153.578 1.00 51.12 ?  64  TYR B N     1 
ATOM   6061  C  CA    . TYR B 1 64  ? 153.879 150.933 154.069 1.00 49.36 ?  64  TYR B CA    1 
ATOM   6062  C  C     . TYR B 1 64  ? 153.765 152.054 153.047 1.00 51.84 ?  64  TYR B C     1 
ATOM   6063  O  O     . TYR B 1 64  ? 154.442 152.067 152.015 1.00 56.22 ?  64  TYR B O     1 
ATOM   6064  C  CB    . TYR B 1 64  ? 154.379 151.496 155.403 1.00 51.22 ?  64  TYR B CB    1 
ATOM   6065  C  CG    . TYR B 1 64  ? 154.105 150.616 156.594 1.00 49.14 ?  64  TYR B CG    1 
ATOM   6066  C  CD1   . TYR B 1 64  ? 153.357 149.454 156.470 1.00 47.95 ?  64  TYR B CD1   1 
ATOM   6067  C  CD2   . TYR B 1 64  ? 154.594 150.949 157.847 1.00 50.77 ?  64  TYR B CD2   1 
ATOM   6068  C  CE1   . TYR B 1 64  ? 153.108 148.647 157.560 1.00 45.37 ?  64  TYR B CE1   1 
ATOM   6069  C  CE2   . TYR B 1 64  ? 154.350 150.152 158.940 1.00 50.87 ?  64  TYR B CE2   1 
ATOM   6070  C  CZ    . TYR B 1 64  ? 153.607 149.002 158.792 1.00 50.19 ?  64  TYR B CZ    1 
ATOM   6071  O  OH    . TYR B 1 64  ? 153.365 148.208 159.886 1.00 55.95 ?  64  TYR B OH    1 
ATOM   6072  N  N     . GLU B 1 65  ? 152.895 153.009 153.354 1.00 56.36 ?  65  GLU B N     1 
ATOM   6073  C  CA    . GLU B 1 65  ? 152.752 154.226 152.570 1.00 57.07 ?  65  GLU B CA    1 
ATOM   6074  C  C     . GLU B 1 65  ? 153.423 155.375 153.310 1.00 58.36 ?  65  GLU B C     1 
ATOM   6075  O  O     . GLU B 1 65  ? 153.129 155.617 154.485 1.00 59.05 ?  65  GLU B O     1 
ATOM   6076  C  CB    . GLU B 1 65  ? 151.279 154.549 152.316 1.00 54.02 ?  65  GLU B CB    1 
ATOM   6077  C  CG    . GLU B 1 65  ? 150.558 153.536 151.445 1.00 52.75 ?  65  GLU B CG    1 
ATOM   6078  C  CD    . GLU B 1 65  ? 149.060 153.769 151.403 1.00 59.36 ?  65  GLU B CD    1 
ATOM   6079  O  OE1   . GLU B 1 65  ? 148.454 153.955 152.479 1.00 59.54 ?  65  GLU B OE1   1 
ATOM   6080  O  OE2   . GLU B 1 65  ? 148.487 153.768 150.293 1.00 56.85 -1 65  GLU B OE2   1 
ATOM   6081  N  N     . GLU B 1 66  ? 154.329 156.072 152.624 1.00 58.13 ?  66  GLU B N     1 
ATOM   6082  C  CA    . GLU B 1 66  ? 155.016 157.196 153.246 1.00 59.42 ?  66  GLU B CA    1 
ATOM   6083  C  C     . GLU B 1 66  ? 154.102 158.399 153.433 1.00 60.55 ?  66  GLU B C     1 
ATOM   6084  O  O     . GLU B 1 66  ? 154.405 159.269 154.256 1.00 58.82 ?  66  GLU B O     1 
ATOM   6085  C  CB    . GLU B 1 66  ? 156.238 157.588 152.409 1.00 61.14 ?  66  GLU B CB    1 
ATOM   6086  C  CG    . GLU B 1 66  ? 157.249 158.501 153.106 1.00 61.57 ?  66  GLU B CG    1 
ATOM   6087  C  CD    . GLU B 1 66  ? 157.582 158.071 154.526 1.00 65.09 ?  66  GLU B CD    1 
ATOM   6088  O  OE1   . GLU B 1 66  ? 156.821 158.410 155.457 1.00 63.13 ?  66  GLU B OE1   1 
ATOM   6089  O  OE2   . GLU B 1 66  ? 158.613 157.390 154.711 1.00 62.81 -1 66  GLU B OE2   1 
ATOM   6090  N  N     . GLU B 1 67  ? 152.990 158.464 152.697 1.00 58.11 ?  67  GLU B N     1 
ATOM   6091  C  CA    . GLU B 1 67  ? 152.131 159.643 152.744 1.00 55.39 ?  67  GLU B CA    1 
ATOM   6092  C  C     . GLU B 1 67  ? 151.497 159.820 154.118 1.00 59.38 ?  67  GLU B C     1 
ATOM   6093  O  O     . GLU B 1 67  ? 151.555 160.910 154.702 1.00 60.34 ?  67  GLU B O     1 
ATOM   6094  C  CB    . GLU B 1 67  ? 151.053 159.546 151.665 1.00 57.45 ?  67  GLU B CB    1 
ATOM   6095  C  CG    . GLU B 1 67  ? 151.598 159.432 150.253 1.00 58.19 ?  67  GLU B CG    1 
ATOM   6096  C  CD    . GLU B 1 67  ? 151.655 157.998 149.766 1.00 61.21 ?  67  GLU B CD    1 
ATOM   6097  O  OE1   . GLU B 1 67  ? 150.582 157.413 149.509 1.00 62.20 ?  67  GLU B OE1   1 
ATOM   6098  O  OE2   . GLU B 1 67  ? 152.773 157.456 149.639 1.00 62.48 -1 67  GLU B OE2   1 
ATOM   6099  N  N     . PHE B 1 68  ? 150.885 158.763 154.654 1.00 53.85 ?  68  PHE B N     1 
ATOM   6100  C  CA    . PHE B 1 68  ? 150.192 158.891 155.932 1.00 49.12 ?  68  PHE B CA    1 
ATOM   6101  C  C     . PHE B 1 68  ? 151.159 158.945 157.107 1.00 50.48 ?  68  PHE B C     1 
ATOM   6102  O  O     . PHE B 1 68  ? 150.856 159.585 158.120 1.00 54.75 ?  68  PHE B O     1 
ATOM   6103  C  CB    . PHE B 1 68  ? 149.184 157.749 156.106 1.00 49.06 ?  68  PHE B CB    1 
ATOM   6104  C  CG    . PHE B 1 68  ? 149.755 156.507 156.731 1.00 45.75 ?  68  PHE B CG    1 
ATOM   6105  C  CD1   . PHE B 1 68  ? 150.393 155.556 155.955 1.00 48.64 ?  68  PHE B CD1   1 
ATOM   6106  C  CD2   . PHE B 1 68  ? 149.625 156.272 158.092 1.00 45.10 ?  68  PHE B CD2   1 
ATOM   6107  C  CE1   . PHE B 1 68  ? 150.913 154.411 156.524 1.00 48.69 ?  68  PHE B CE1   1 
ATOM   6108  C  CE2   . PHE B 1 68  ? 150.144 155.128 158.664 1.00 47.79 ?  68  PHE B CE2   1 
ATOM   6109  C  CZ    . PHE B 1 68  ? 150.784 154.196 157.879 1.00 48.99 ?  68  PHE B CZ    1 
ATOM   6110  N  N     . LEU B 1 69  ? 152.316 158.290 156.999 1.00 48.84 ?  69  LEU B N     1 
ATOM   6111  C  CA    . LEU B 1 69  ? 153.292 158.339 158.081 1.00 50.00 ?  69  LEU B CA    1 
ATOM   6112  C  C     . LEU B 1 69  ? 154.016 159.677 158.138 1.00 53.07 ?  69  LEU B C     1 
ATOM   6113  O  O     . LEU B 1 69  ? 154.462 160.088 159.215 1.00 50.57 ?  69  LEU B O     1 
ATOM   6114  C  CB    . LEU B 1 69  ? 154.302 157.201 157.936 1.00 50.19 ?  69  LEU B CB    1 
ATOM   6115  C  CG    . LEU B 1 69  ? 153.843 155.845 158.473 1.00 49.96 ?  69  LEU B CG    1 
ATOM   6116  C  CD1   . LEU B 1 69  ? 154.834 154.754 158.108 1.00 50.10 ?  69  LEU B CD1   1 
ATOM   6117  C  CD2   . LEU B 1 69  ? 153.636 155.909 159.977 1.00 50.65 ?  69  LEU B CD2   1 
ATOM   6118  N  N     . SER B 1 70  ? 154.141 160.367 157.003 1.00 57.68 ?  70  SER B N     1 
ATOM   6119  C  CA    . SER B 1 70  ? 154.787 161.675 156.990 1.00 54.92 ?  70  SER B CA    1 
ATOM   6120  C  C     . SER B 1 70  ? 153.958 162.736 157.698 1.00 51.98 ?  70  SER B C     1 
ATOM   6121  O  O     . SER B 1 70  ? 154.482 163.812 158.003 1.00 53.93 ?  70  SER B O     1 
ATOM   6122  C  CB    . SER B 1 70  ? 155.066 162.114 155.554 1.00 53.34 ?  70  SER B CB    1 
ATOM   6123  O  OG    . SER B 1 70  ? 153.891 162.048 154.767 1.00 54.26 ?  70  SER B OG    1 
ATOM   6124  N  N     . LEU B 1 71  ? 152.680 162.461 157.961 1.00 46.56 ?  71  LEU B N     1 
ATOM   6125  C  CA    . LEU B 1 71  ? 151.816 163.420 158.636 1.00 46.13 ?  71  LEU B CA    1 
ATOM   6126  C  C     . LEU B 1 71  ? 152.166 163.594 160.106 1.00 47.72 ?  71  LEU B C     1 
ATOM   6127  O  O     . LEU B 1 71  ? 151.663 164.530 160.737 1.00 50.28 ?  71  LEU B O     1 
ATOM   6128  C  CB    . LEU B 1 71  ? 150.356 162.988 158.500 1.00 46.23 ?  71  LEU B CB    1 
ATOM   6129  C  CG    . LEU B 1 71  ? 149.720 163.205 157.127 1.00 50.87 ?  71  LEU B CG    1 
ATOM   6130  C  CD1   . LEU B 1 71  ? 148.209 163.189 157.231 1.00 48.61 ?  71  LEU B CD1   1 
ATOM   6131  C  CD2   . LEU B 1 71  ? 150.202 164.507 156.510 1.00 49.17 ?  71  LEU B CD2   1 
ATOM   6132  N  N     . TYR B 1 72  ? 153.008 162.728 160.662 1.00 45.28 ?  72  TYR B N     1 
ATOM   6133  C  CA    . TYR B 1 72  ? 153.412 162.798 162.057 1.00 44.42 ?  72  TYR B CA    1 
ATOM   6134  C  C     . TYR B 1 72  ? 154.924 162.925 162.150 1.00 48.54 ?  72  TYR B C     1 
ATOM   6135  O  O     . TYR B 1 72  ? 155.655 162.357 161.333 1.00 50.77 ?  72  TYR B O     1 
ATOM   6136  C  CB    . TYR B 1 72  ? 152.975 161.551 162.838 1.00 46.60 ?  72  TYR B CB    1 
ATOM   6137  C  CG    . TYR B 1 72  ? 151.540 161.131 162.632 1.00 44.13 ?  72  TYR B CG    1 
ATOM   6138  C  CD1   . TYR B 1 72  ? 151.183 160.309 161.574 1.00 40.51 ?  72  TYR B CD1   1 
ATOM   6139  C  CD2   . TYR B 1 72  ? 150.545 161.537 163.510 1.00 45.33 ?  72  TYR B CD2   1 
ATOM   6140  C  CE1   . TYR B 1 72  ? 149.878 159.919 161.384 1.00 40.64 ?  72  TYR B CE1   1 
ATOM   6141  C  CE2   . TYR B 1 72  ? 149.236 161.149 163.331 1.00 41.64 ?  72  TYR B CE2   1 
ATOM   6142  C  CZ    . TYR B 1 72  ? 148.908 160.339 162.265 1.00 42.12 ?  72  TYR B CZ    1 
ATOM   6143  O  OH    . TYR B 1 72  ? 147.605 159.949 162.079 1.00 47.11 ?  72  TYR B OH    1 
ATOM   6144  N  N     . SER B 1 73  ? 155.387 163.671 163.147 1.00 54.10 ?  73  SER B N     1 
ATOM   6145  C  CA    . SER B 1 73  ? 156.777 163.559 163.553 1.00 54.69 ?  73  SER B CA    1 
ATOM   6146  C  C     . SER B 1 73  ? 157.014 162.176 164.144 1.00 54.99 ?  73  SER B C     1 
ATOM   6147  O  O     . SER B 1 73  ? 156.098 161.544 164.677 1.00 58.63 ?  73  SER B O     1 
ATOM   6148  C  CB    . SER B 1 73  ? 157.132 164.642 164.570 1.00 53.07 ?  73  SER B CB    1 
ATOM   6149  O  OG    . SER B 1 73  ? 156.505 164.394 165.815 1.00 51.89 ?  73  SER B OG    1 
ATOM   6150  N  N     . PHE B 1 74  ? 158.254 161.693 164.035 1.00 56.10 ?  74  PHE B N     1 
ATOM   6151  C  CA    . PHE B 1 74  ? 158.539 160.345 164.514 1.00 55.84 ?  74  PHE B CA    1 
ATOM   6152  C  C     . PHE B 1 74  ? 158.280 160.208 166.009 1.00 55.08 ?  74  PHE B C     1 
ATOM   6153  O  O     . PHE B 1 74  ? 157.993 159.107 166.487 1.00 60.39 ?  74  PHE B O     1 
ATOM   6154  C  CB    . PHE B 1 74  ? 159.977 159.942 164.202 1.00 56.32 ?  74  PHE B CB    1 
ATOM   6155  C  CG    . PHE B 1 74  ? 160.369 158.629 164.814 1.00 57.06 ?  74  PHE B CG    1 
ATOM   6156  C  CD1   . PHE B 1 74  ? 159.821 157.447 164.346 1.00 56.22 ?  74  PHE B CD1   1 
ATOM   6157  C  CD2   . PHE B 1 74  ? 161.251 158.577 165.879 1.00 57.99 ?  74  PHE B CD2   1 
ATOM   6158  C  CE1   . PHE B 1 74  ? 160.162 156.239 164.912 1.00 58.61 ?  74  PHE B CE1   1 
ATOM   6159  C  CE2   . PHE B 1 74  ? 161.597 157.371 166.450 1.00 57.74 ?  74  PHE B CE2   1 
ATOM   6160  C  CZ    . PHE B 1 74  ? 161.050 156.200 165.966 1.00 59.91 ?  74  PHE B CZ    1 
ATOM   6161  N  N     . GLU B 1 75  ? 158.376 161.306 166.762 1.00 54.53 ?  75  GLU B N     1 
ATOM   6162  C  CA    . GLU B 1 75  ? 158.059 161.244 168.184 1.00 58.15 ?  75  GLU B CA    1 
ATOM   6163  C  C     . GLU B 1 75  ? 156.597 160.875 168.404 1.00 60.11 ?  75  GLU B C     1 
ATOM   6164  O  O     . GLU B 1 75  ? 156.275 160.079 169.292 1.00 60.42 ?  75  GLU B O     1 
ATOM   6165  C  CB    . GLU B 1 75  ? 158.385 162.579 168.853 1.00 56.36 ?  75  GLU B CB    1 
ATOM   6166  C  CG    . GLU B 1 75  ? 159.870 162.894 168.903 1.00 56.59 ?  75  GLU B CG    1 
ATOM   6167  C  CD    . GLU B 1 75  ? 160.689 161.744 169.458 1.00 63.42 ?  75  GLU B CD    1 
ATOM   6168  O  OE1   . GLU B 1 75  ? 160.453 161.350 170.620 1.00 63.49 ?  75  GLU B OE1   1 
ATOM   6169  O  OE2   . GLU B 1 75  ? 161.568 161.234 168.732 1.00 62.13 -1 75  GLU B OE2   1 
ATOM   6170  N  N     . ASP B 1 76  ? 155.698 161.441 167.597 1.00 55.72 ?  76  ASP B N     1 
ATOM   6171  C  CA    . ASP B 1 76  ? 154.280 161.122 167.725 1.00 54.37 ?  76  ASP B CA    1 
ATOM   6172  C  C     . ASP B 1 76  ? 154.007 159.661 167.389 1.00 55.43 ?  76  ASP B C     1 
ATOM   6173  O  O     . ASP B 1 76  ? 153.224 158.994 168.075 1.00 58.92 ?  76  ASP B O     1 
ATOM   6174  C  CB    . ASP B 1 76  ? 153.457 162.043 166.828 1.00 55.73 ?  76  ASP B CB    1 
ATOM   6175  C  CG    . ASP B 1 76  ? 153.562 163.497 167.236 1.00 58.99 ?  76  ASP B CG    1 
ATOM   6176  O  OD1   . ASP B 1 76  ? 153.586 163.773 168.454 1.00 59.14 ?  76  ASP B OD1   1 
ATOM   6177  O  OD2   . ASP B 1 76  ? 153.615 164.366 166.341 1.00 58.03 -1 76  ASP B OD2   1 
ATOM   6178  N  N     . ILE B 1 77  ? 154.642 159.146 166.333 1.00 48.13 ?  77  ILE B N     1 
ATOM   6179  C  CA    . ILE B 1 77  ? 154.473 157.740 165.975 1.00 49.21 ?  77  ILE B CA    1 
ATOM   6180  C  C     . ILE B 1 77  ? 155.019 156.843 167.078 1.00 50.79 ?  77  ILE B C     1 
ATOM   6181  O  O     . ILE B 1 77  ? 154.433 155.803 167.405 1.00 54.21 ?  77  ILE B O     1 
ATOM   6182  C  CB    . ILE B 1 77  ? 155.147 157.451 164.622 1.00 49.26 ?  77  ILE B CB    1 
ATOM   6183  C  CG1   . ILE B 1 77  ? 154.516 158.304 163.523 1.00 49.08 ?  77  ILE B CG1   1 
ATOM   6184  C  CG2   . ILE B 1 77  ? 155.032 155.978 164.274 1.00 49.31 ?  77  ILE B CG2   1 
ATOM   6185  C  CD1   . ILE B 1 77  ? 155.319 158.338 162.248 1.00 50.74 ?  77  ILE B CD1   1 
ATOM   6186  N  N     . LYS B 1 78  ? 156.155 157.228 167.660 1.00 52.56 ?  78  LYS B N     1 
ATOM   6187  C  CA    . LYS B 1 78  ? 156.727 156.458 168.758 1.00 51.80 ?  78  LYS B CA    1 
ATOM   6188  C  C     . LYS B 1 78  ? 155.792 156.438 169.958 1.00 52.98 ?  78  LYS B C     1 
ATOM   6189  O  O     . LYS B 1 78  ? 155.627 155.401 170.605 1.00 56.49 ?  78  LYS B O     1 
ATOM   6190  C  CB    . LYS B 1 78  ? 158.090 157.032 169.143 1.00 55.18 ?  78  LYS B CB    1 
ATOM   6191  C  CG    . LYS B 1 78  ? 158.814 156.244 170.218 1.00 54.95 ?  78  LYS B CG    1 
ATOM   6192  C  CD    . LYS B 1 78  ? 160.240 155.934 169.800 1.00 55.76 ?  78  LYS B CD    1 
ATOM   6193  C  CE    . LYS B 1 78  ? 161.240 156.453 170.817 1.00 57.25 ?  78  LYS B CE    1 
ATOM   6194  N  NZ    . LYS B 1 78  ? 162.645 156.253 170.368 1.00 55.90 1  78  LYS B NZ    1 
ATOM   6195  N  N     . GLU B 1 79  ? 155.164 157.575 170.268 1.00 53.27 ?  79  GLU B N     1 
ATOM   6196  C  CA    . GLU B 1 79  ? 154.215 157.604 171.377 1.00 52.11 ?  79  GLU B CA    1 
ATOM   6197  C  C     . GLU B 1 79  ? 152.962 156.792 171.072 1.00 51.11 ?  79  GLU B C     1 
ATOM   6198  O  O     . GLU B 1 79  ? 152.391 156.176 171.978 1.00 52.30 ?  79  GLU B O     1 
ATOM   6199  C  CB    . GLU B 1 79  ? 153.848 159.047 171.725 1.00 52.64 ?  79  GLU B CB    1 
ATOM   6200  C  CG    . GLU B 1 79  ? 155.017 159.920 172.187 1.00 56.29 ?  79  GLU B CG    1 
ATOM   6201  C  CD    . GLU B 1 79  ? 156.069 159.172 172.999 1.00 58.47 ?  79  GLU B CD    1 
ATOM   6202  O  OE1   . GLU B 1 79  ? 157.272 159.436 172.788 1.00 56.16 ?  79  GLU B OE1   1 
ATOM   6203  O  OE2   . GLU B 1 79  ? 155.706 158.363 173.881 1.00 57.13 -1 79  GLU B OE2   1 
ATOM   6204  N  N     . VAL B 1 80  ? 152.524 156.773 169.813 1.00 48.64 ?  80  VAL B N     1 
ATOM   6205  C  CA    . VAL B 1 80  ? 151.387 155.937 169.437 1.00 45.07 ?  80  VAL B CA    1 
ATOM   6206  C  C     . VAL B 1 80  ? 151.722 154.460 169.628 1.00 48.97 ?  80  VAL B C     1 
ATOM   6207  O  O     . VAL B 1 80  ? 150.927 153.690 170.187 1.00 51.77 ?  80  VAL B O     1 
ATOM   6208  C  CB    . VAL B 1 80  ? 150.963 156.247 167.988 1.00 44.98 ?  80  VAL B CB    1 
ATOM   6209  C  CG1   . VAL B 1 80  ? 150.046 155.171 167.450 1.00 46.55 ?  80  VAL B CG1   1 
ATOM   6210  C  CG2   . VAL B 1 80  ? 150.284 157.605 167.920 1.00 45.90 ?  80  VAL B CG2   1 
ATOM   6211  N  N     . PHE B 1 81  ? 152.911 154.047 169.182 1.00 47.44 ?  81  PHE B N     1 
ATOM   6212  C  CA    . PHE B 1 81  ? 153.341 152.668 169.391 1.00 44.10 ?  81  PHE B CA    1 
ATOM   6213  C  C     . PHE B 1 81  ? 153.503 152.359 170.875 1.00 45.61 ?  81  PHE B C     1 
ATOM   6214  O  O     . PHE B 1 81  ? 153.219 151.240 171.318 1.00 51.04 ?  81  PHE B O     1 
ATOM   6215  C  CB    . PHE B 1 81  ? 154.645 152.405 168.639 1.00 43.36 ?  81  PHE B CB    1 
ATOM   6216  C  CG    . PHE B 1 81  ? 154.447 151.954 167.221 1.00 43.48 ?  81  PHE B CG    1 
ATOM   6217  C  CD1   . PHE B 1 81  ? 154.138 152.865 166.226 1.00 44.24 ?  81  PHE B CD1   1 
ATOM   6218  C  CD2   . PHE B 1 81  ? 154.575 150.619 166.883 1.00 43.71 ?  81  PHE B CD2   1 
ATOM   6219  C  CE1   . PHE B 1 81  ? 153.956 152.451 164.921 1.00 44.16 ?  81  PHE B CE1   1 
ATOM   6220  C  CE2   . PHE B 1 81  ? 154.394 150.199 165.580 1.00 45.21 ?  81  PHE B CE2   1 
ATOM   6221  C  CZ    . PHE B 1 81  ? 154.085 151.117 164.598 1.00 43.39 ?  81  PHE B CZ    1 
ATOM   6222  N  N     . LYS B 1 82  ? 153.961 153.337 171.657 1.00 47.11 ?  82  LYS B N     1 
ATOM   6223  C  CA    . LYS B 1 82  ? 154.034 153.173 173.105 1.00 51.39 ?  82  LYS B CA    1 
ATOM   6224  C  C     . LYS B 1 82  ? 152.654 152.918 173.691 1.00 51.71 ?  82  LYS B C     1 
ATOM   6225  O  O     . LYS B 1 82  ? 152.479 152.052 174.554 1.00 51.17 ?  82  LYS B O     1 
ATOM   6226  C  CB    . LYS B 1 82  ? 154.654 154.418 173.739 1.00 53.58 ?  82  LYS B CB    1 
ATOM   6227  C  CG    . LYS B 1 82  ? 155.983 154.201 174.435 1.00 53.04 ?  82  LYS B CG    1 
ATOM   6228  C  CD    . LYS B 1 82  ? 157.127 154.087 173.448 1.00 54.24 ?  82  LYS B CD    1 
ATOM   6229  C  CE    . LYS B 1 82  ? 158.461 154.234 174.160 1.00 55.14 ?  82  LYS B CE    1 
ATOM   6230  N  NZ    . LYS B 1 82  ? 159.492 153.302 173.635 1.00 56.03 1  82  LYS B NZ    1 
ATOM   6231  N  N     . THR B 1 83  ? 151.659 153.678 173.230 1.00 47.16 ?  83  THR B N     1 
ATOM   6232  C  CA    . THR B 1 83  ? 150.293 153.490 173.704 1.00 45.62 ?  83  THR B CA    1 
ATOM   6233  C  C     . THR B 1 83  ? 149.773 152.105 173.345 1.00 47.50 ?  83  THR B C     1 
ATOM   6234  O  O     . THR B 1 83  ? 149.077 151.468 174.145 1.00 51.83 ?  83  THR B O     1 
ATOM   6235  C  CB    . THR B 1 83  ? 149.383 154.573 173.125 1.00 45.08 ?  83  THR B CB    1 
ATOM   6236  O  OG1   . THR B 1 83  ? 149.958 155.861 173.378 1.00 51.98 ?  83  THR B OG1   1 
ATOM   6237  C  CG2   . THR B 1 83  ? 148.009 154.512 173.763 1.00 47.96 ?  83  THR B CG2   1 
ATOM   6238  N  N     . ALA B 1 84  ? 150.096 151.622 172.142 1.00 41.73 ?  84  ALA B N     1 
ATOM   6239  C  CA    . ALA B 1 84  ? 149.667 150.280 171.761 1.00 38.19 ?  84  ALA B CA    1 
ATOM   6240  C  C     . ALA B 1 84  ? 150.309 149.214 172.641 1.00 41.93 ?  84  ALA B C     1 
ATOM   6241  O  O     . ALA B 1 84  ? 149.636 148.269 173.069 1.00 50.02 ?  84  ALA B O     1 
ATOM   6242  C  CB    . ALA B 1 84  ? 149.989 150.021 170.293 1.00 41.37 ?  84  ALA B CB    1 
ATOM   6243  N  N     . TYR B 1 85  ? 151.606 149.343 172.920 1.00 48.73 ?  85  TYR B N     1 
ATOM   6244  C  CA    . TYR B 1 85  ? 152.300 148.351 173.731 1.00 44.08 ?  85  TYR B CA    1 
ATOM   6245  C  C     . TYR B 1 85  ? 152.115 148.572 175.224 1.00 45.71 ?  85  TYR B C     1 
ATOM   6246  O  O     . TYR B 1 85  ? 152.443 147.679 176.012 1.00 48.79 ?  85  TYR B O     1 
ATOM   6247  C  CB    . TYR B 1 85  ? 153.792 148.339 173.391 1.00 45.03 ?  85  TYR B CB    1 
ATOM   6248  C  CG    . TYR B 1 85  ? 154.118 147.655 172.083 1.00 45.73 ?  85  TYR B CG    1 
ATOM   6249  C  CD1   . TYR B 1 85  ? 154.091 148.353 170.885 1.00 45.47 ?  85  TYR B CD1   1 
ATOM   6250  C  CD2   . TYR B 1 85  ? 154.454 146.309 172.049 1.00 45.37 ?  85  TYR B CD2   1 
ATOM   6251  C  CE1   . TYR B 1 85  ? 154.389 147.732 169.691 1.00 45.26 ?  85  TYR B CE1   1 
ATOM   6252  C  CE2   . TYR B 1 85  ? 154.753 145.680 170.859 1.00 45.88 ?  85  TYR B CE2   1 
ATOM   6253  C  CZ    . TYR B 1 85  ? 154.718 146.395 169.683 1.00 47.44 ?  85  TYR B CZ    1 
ATOM   6254  O  OH    . TYR B 1 85  ? 155.016 145.772 168.496 1.00 49.52 ?  85  TYR B OH    1 
ATOM   6255  N  N     . ALA B 1 86  ? 151.604 149.734 175.635 1.00 48.77 ?  86  ALA B N     1 
ATOM   6256  C  CA    . ALA B 1 86  ? 151.358 149.972 177.053 1.00 49.11 ?  86  ALA B CA    1 
ATOM   6257  C  C     . ALA B 1 86  ? 150.242 149.094 177.600 1.00 51.18 ?  86  ALA B C     1 
ATOM   6258  O  O     . ALA B 1 86  ? 150.209 148.836 178.807 1.00 50.07 ?  86  ALA B O     1 
ATOM   6259  C  CB    . ALA B 1 86  ? 151.019 151.443 177.296 1.00 45.01 ?  86  ALA B CB    1 
ATOM   6260  N  N     . LYS B 1 87  ? 149.330 148.634 176.744 1.00 43.59 ?  87  LYS B N     1 
ATOM   6261  C  CA    . LYS B 1 87  ? 148.235 147.785 177.191 1.00 43.37 ?  87  LYS B CA    1 
ATOM   6262  C  C     . LYS B 1 87  ? 148.679 146.363 177.501 1.00 46.64 ?  87  LYS B C     1 
ATOM   6263  O  O     . LYS B 1 87  ? 147.986 145.666 178.249 1.00 46.53 ?  87  LYS B O     1 
ATOM   6264  C  CB    . LYS B 1 87  ? 147.127 147.755 176.136 1.00 46.41 ?  87  LYS B CB    1 
ATOM   6265  C  CG    . LYS B 1 87  ? 145.734 147.561 176.707 1.00 47.31 ?  87  LYS B CG    1 
ATOM   6266  C  CD    . LYS B 1 87  ? 145.037 146.374 176.065 1.00 43.91 ?  87  LYS B CD    1 
ATOM   6267  C  CE    . LYS B 1 87  ? 143.775 146.002 176.823 1.00 43.53 ?  87  LYS B CE    1 
ATOM   6268  N  NZ    . LYS B 1 87  ? 143.045 144.879 176.171 1.00 41.20 1  87  LYS B NZ    1 
ATOM   6269  N  N     . LYS B 1 88  ? 149.815 145.926 176.953 1.00 51.97 ?  88  LYS B N     1 
ATOM   6270  C  CA    . LYS B 1 88  ? 150.300 144.556 177.110 1.00 47.74 ?  88  LYS B CA    1 
ATOM   6271  C  C     . LYS B 1 88  ? 149.217 143.553 176.719 1.00 46.69 ?  88  LYS B C     1 
ATOM   6272  O  O     . LYS B 1 88  ? 148.898 142.621 177.459 1.00 49.88 ?  88  LYS B O     1 
ATOM   6273  C  CB    . LYS B 1 88  ? 150.796 144.304 178.535 1.00 48.98 ?  88  LYS B CB    1 
ATOM   6274  C  CG    . LYS B 1 88  ? 151.661 145.420 179.098 1.00 47.10 ?  88  LYS B CG    1 
ATOM   6275  C  CD    . LYS B 1 88  ? 152.987 144.886 179.610 1.00 50.61 ?  88  LYS B CD    1 
ATOM   6276  C  CE    . LYS B 1 88  ? 152.804 144.096 180.894 1.00 52.66 ?  88  LYS B CE    1 
ATOM   6277  N  NZ    . LYS B 1 88  ? 153.982 143.232 181.188 1.00 51.45 1  88  LYS B NZ    1 
ATOM   6278  N  N     . PHE B 1 89  ? 148.640 143.766 175.538 1.00 45.43 ?  89  PHE B N     1 
ATOM   6279  C  CA    . PHE B 1 89  ? 147.524 142.944 175.091 1.00 40.04 ?  89  PHE B CA    1 
ATOM   6280  C  C     . PHE B 1 89  ? 147.963 141.500 174.896 1.00 42.32 ?  89  PHE B C     1 
ATOM   6281  O  O     . PHE B 1 89  ? 149.006 141.227 174.297 1.00 43.62 ?  89  PHE B O     1 
ATOM   6282  C  CB    . PHE B 1 89  ? 146.946 143.495 173.787 1.00 39.99 ?  89  PHE B CB    1 
ATOM   6283  C  CG    . PHE B 1 89  ? 145.907 142.607 173.168 1.00 38.98 ?  89  PHE B CG    1 
ATOM   6284  C  CD1   . PHE B 1 89  ? 144.605 142.619 173.634 1.00 37.21 ?  89  PHE B CD1   1 
ATOM   6285  C  CD2   . PHE B 1 89  ? 146.232 141.755 172.128 1.00 39.03 ?  89  PHE B CD2   1 
ATOM   6286  C  CE1   . PHE B 1 89  ? 143.648 141.802 173.074 1.00 39.04 ?  89  PHE B CE1   1 
ATOM   6287  C  CE2   . PHE B 1 89  ? 145.278 140.935 171.564 1.00 35.00 ?  89  PHE B CE2   1 
ATOM   6288  C  CZ    . PHE B 1 89  ? 143.986 140.959 172.036 1.00 38.35 ?  89  PHE B CZ    1 
ATOM   6289  N  N     . ARG B 1 90  ? 147.153 140.574 175.399 1.00 43.49 ?  90  ARG B N     1 
ATOM   6290  C  CA    . ARG B 1 90  ? 147.398 139.148 175.256 1.00 43.41 ?  90  ARG B CA    1 
ATOM   6291  C  C     . ARG B 1 90  ? 146.208 138.508 174.561 1.00 43.90 ?  90  ARG B C     1 
ATOM   6292  O  O     . ARG B 1 90  ? 145.059 138.745 174.947 1.00 47.64 ?  90  ARG B O     1 
ATOM   6293  C  CB    . ARG B 1 90  ? 147.634 138.487 176.617 1.00 46.45 ?  90  ARG B CB    1 
ATOM   6294  C  CG    . ARG B 1 90  ? 148.817 139.048 177.378 1.00 46.45 ?  90  ARG B CG    1 
ATOM   6295  C  CD    . ARG B 1 90  ? 150.101 138.338 176.993 1.00 48.43 ?  90  ARG B CD    1 
ATOM   6296  N  NE    . ARG B 1 90  ? 150.916 139.145 176.095 1.00 51.01 ?  90  ARG B NE    1 
ATOM   6297  C  CZ    . ARG B 1 90  ? 151.677 140.160 176.479 1.00 49.77 ?  90  ARG B CZ    1 
ATOM   6298  N  NH1   . ARG B 1 90  ? 151.770 140.512 177.751 1.00 47.15 1  90  ARG B NH1   1 
ATOM   6299  N  NH2   . ARG B 1 90  ? 152.364 140.839 175.565 1.00 51.52 ?  90  ARG B NH2   1 
ATOM   6300  N  N     . PHE B 1 91  ? 146.483 137.714 173.539 1.00 36.62 ?  91  PHE B N     1 
ATOM   6301  C  CA    . PHE B 1 91  ? 145.428 136.944 172.899 1.00 39.12 ?  91  PHE B CA    1 
ATOM   6302  C  C     . PHE B 1 91  ? 144.930 135.878 173.868 1.00 44.74 ?  91  PHE B C     1 
ATOM   6303  O  O     . PHE B 1 91  ? 145.732 135.086 174.374 1.00 45.97 ?  91  PHE B O     1 
ATOM   6304  C  CB    . PHE B 1 91  ? 145.939 136.300 171.615 1.00 39.16 ?  91  PHE B CB    1 
ATOM   6305  C  CG    . PHE B 1 91  ? 146.080 137.260 170.469 1.00 40.47 ?  91  PHE B CG    1 
ATOM   6306  C  CD1   . PHE B 1 91  ? 144.964 137.726 169.795 1.00 43.58 ?  91  PHE B CD1   1 
ATOM   6307  C  CD2   . PHE B 1 91  ? 147.328 137.695 170.064 1.00 42.01 ?  91  PHE B CD2   1 
ATOM   6308  C  CE1   . PHE B 1 91  ? 145.092 138.605 168.740 1.00 40.28 ?  91  PHE B CE1   1 
ATOM   6309  C  CE2   . PHE B 1 91  ? 147.462 138.574 169.010 1.00 40.89 ?  91  PHE B CE2   1 
ATOM   6310  C  CZ    . PHE B 1 91  ? 146.342 139.029 168.346 1.00 36.90 ?  91  PHE B CZ    1 
ATOM   6311  N  N     . PRO B 1 92  ? 143.628 135.827 174.158 1.00 44.11 ?  92  PRO B N     1 
ATOM   6312  C  CA    . PRO B 1 92  ? 143.150 134.862 175.159 1.00 40.42 ?  92  PRO B CA    1 
ATOM   6313  C  C     . PRO B 1 92  ? 143.166 133.428 174.668 1.00 39.94 ?  92  PRO B C     1 
ATOM   6314  O  O     . PRO B 1 92  ? 143.326 132.508 175.480 1.00 43.37 ?  92  PRO B O     1 
ATOM   6315  C  CB    . PRO B 1 92  ? 141.725 135.346 175.450 1.00 40.58 ?  92  PRO B CB    1 
ATOM   6316  C  CG    . PRO B 1 92  ? 141.298 135.990 174.179 1.00 40.82 ?  92  PRO B CG    1 
ATOM   6317  C  CD    . PRO B 1 92  ? 142.528 136.617 173.580 1.00 42.53 ?  92  PRO B CD    1 
ATOM   6318  N  N     . SER B 1 93  ? 143.010 133.208 173.367 1.00 38.53 ?  93  SER B N     1 
ATOM   6319  C  CA    . SER B 1 93  ? 142.918 131.874 172.803 1.00 40.38 ?  93  SER B CA    1 
ATOM   6320  C  C     . SER B 1 93  ? 143.940 131.725 171.688 1.00 42.60 ?  93  SER B C     1 
ATOM   6321  O  O     . SER B 1 93  ? 144.421 132.710 171.122 1.00 47.55 ?  93  SER B O     1 
ATOM   6322  C  CB    . SER B 1 93  ? 141.508 131.593 172.271 1.00 44.04 ?  93  SER B CB    1 
ATOM   6323  O  OG    . SER B 1 93  ? 141.443 131.793 170.871 1.00 50.00 ?  93  SER B OG    1 
ATOM   6324  N  N     . PHE B 1 94  ? 144.281 130.472 171.384 1.00 41.90 ?  94  PHE B N     1 
ATOM   6325  C  CA    . PHE B 1 94  ? 145.223 130.215 170.302 1.00 40.14 ?  94  PHE B CA    1 
ATOM   6326  C  C     . PHE B 1 94  ? 144.652 130.640 168.956 1.00 42.76 ?  94  PHE B C     1 
ATOM   6327  O  O     . PHE B 1 94  ? 145.388 131.130 168.093 1.00 47.43 ?  94  PHE B O     1 
ATOM   6328  C  CB    . PHE B 1 94  ? 145.612 128.739 170.268 1.00 40.16 ?  94  PHE B CB    1 
ATOM   6329  C  CG    . PHE B 1 94  ? 146.194 128.306 168.956 1.00 41.76 ?  94  PHE B CG    1 
ATOM   6330  C  CD1   . PHE B 1 94  ? 147.447 128.741 168.567 1.00 42.32 ?  94  PHE B CD1   1 
ATOM   6331  C  CD2   . PHE B 1 94  ? 145.483 127.483 168.102 1.00 43.73 ?  94  PHE B CD2   1 
ATOM   6332  C  CE1   . PHE B 1 94  ? 147.981 128.358 167.356 1.00 42.88 ?  94  PHE B CE1   1 
ATOM   6333  C  CE2   . PHE B 1 94  ? 146.017 127.097 166.890 1.00 41.04 ?  94  PHE B CE2   1 
ATOM   6334  C  CZ    . PHE B 1 94  ? 147.266 127.534 166.518 1.00 40.39 ?  94  PHE B CZ    1 
ATOM   6335  N  N     . MET B 1 95  ? 143.347 130.451 168.755 1.00 38.81 ?  95  MET B N     1 
ATOM   6336  C  CA    . MET B 1 95  ? 142.752 130.753 167.458 1.00 34.84 ?  95  MET B CA    1 
ATOM   6337  C  C     . MET B 1 95  ? 142.776 132.244 167.149 1.00 41.06 ?  95  MET B C     1 
ATOM   6338  O  O     . MET B 1 95  ? 142.925 132.622 165.985 1.00 43.38 ?  95  MET B O     1 
ATOM   6339  C  CB    . MET B 1 95  ? 141.323 130.216 167.391 1.00 41.10 ?  95  MET B CB    1 
ATOM   6340  C  CG    . MET B 1 95  ? 140.630 130.364 166.032 1.00 45.93 ?  95  MET B CG    1 
ATOM   6341  S  SD    . MET B 1 95  ? 141.357 129.636 164.537 1.00 55.90 ?  95  MET B SD    1 
ATOM   6342  C  CE    . MET B 1 95  ? 142.382 128.307 165.159 1.00 43.07 ?  95  MET B CE    1 
ATOM   6343  N  N     . SER B 1 96  ? 142.645 133.100 168.163 1.00 36.73 ?  96  SER B N     1 
ATOM   6344  C  CA    . SER B 1 96  ? 142.730 134.539 167.926 1.00 33.30 ?  96  SER B CA    1 
ATOM   6345  C  C     . SER B 1 96  ? 144.083 134.920 167.336 1.00 36.80 ?  96  SER B C     1 
ATOM   6346  O  O     . SER B 1 96  ? 144.162 135.561 166.277 1.00 32.79 ?  96  SER B O     1 
ATOM   6347  C  CB    . SER B 1 96  ? 142.489 135.293 169.233 1.00 36.01 ?  96  SER B CB    1 
ATOM   6348  O  OG    . SER B 1 96  ? 141.482 134.666 170.003 1.00 42.95 ?  96  SER B OG    1 
ATOM   6349  N  N     . ALA B 1 97  ? 145.162 134.512 168.006 1.00 36.06 ?  97  ALA B N     1 
ATOM   6350  C  CA    . ALA B 1 97  ? 146.506 134.823 167.534 1.00 32.56 ?  97  ALA B CA    1 
ATOM   6351  C  C     . ALA B 1 97  ? 146.790 134.155 166.197 1.00 34.38 ?  97  ALA B C     1 
ATOM   6352  O  O     . ALA B 1 97  ? 147.414 134.758 165.319 1.00 40.22 ?  97  ALA B O     1 
ATOM   6353  C  CB    . ALA B 1 97  ? 147.536 134.396 168.575 1.00 38.51 ?  97  ALA B CB    1 
ATOM   6354  N  N     . PHE B 1 98  ? 146.355 132.906 166.033 1.00 37.04 ?  98  PHE B N     1 
ATOM   6355  C  CA    . PHE B 1 98  ? 146.578 132.201 164.777 1.00 34.05 ?  98  PHE B CA    1 
ATOM   6356  C  C     . PHE B 1 98  ? 145.893 132.916 163.622 1.00 36.17 ?  98  PHE B C     1 
ATOM   6357  O  O     . PHE B 1 98  ? 146.496 133.132 162.566 1.00 48.45 ?  98  PHE B O     1 
ATOM   6358  C  CB    . PHE B 1 98  ? 146.084 130.760 164.889 1.00 39.75 ?  98  PHE B CB    1 
ATOM   6359  C  CG    . PHE B 1 98  ? 146.174 129.988 163.604 1.00 39.93 ?  98  PHE B CG    1 
ATOM   6360  C  CD1   . PHE B 1 98  ? 147.370 129.416 163.208 1.00 39.71 ?  98  PHE B CD1   1 
ATOM   6361  C  CD2   . PHE B 1 98  ? 145.063 129.836 162.792 1.00 41.60 ?  98  PHE B CD2   1 
ATOM   6362  C  CE1   . PHE B 1 98  ? 147.456 128.708 162.028 1.00 39.50 ?  98  PHE B CE1   1 
ATOM   6363  C  CE2   . PHE B 1 98  ? 145.145 129.131 161.610 1.00 44.69 ?  98  PHE B CE2   1 
ATOM   6364  C  CZ    . PHE B 1 98  ? 146.342 128.566 161.228 1.00 43.40 ?  98  PHE B CZ    1 
ATOM   6365  N  N     . LYS B 1 99  ? 144.630 133.304 163.809 1.00 41.42 ?  99  LYS B N     1 
ATOM   6366  C  CA    . LYS B 1 99  ? 143.902 133.993 162.754 1.00 39.05 ?  99  LYS B CA    1 
ATOM   6367  C  C     . LYS B 1 99  ? 144.539 135.335 162.434 1.00 37.72 ?  99  LYS B C     1 
ATOM   6368  O  O     . LYS B 1 99  ? 144.687 135.691 161.260 1.00 42.56 ?  99  LYS B O     1 
ATOM   6369  C  CB    . LYS B 1 99  ? 142.439 134.172 163.157 1.00 37.97 ?  99  LYS B CB    1 
ATOM   6370  C  CG    . LYS B 1 99  ? 141.587 132.933 162.952 1.00 42.93 ?  99  LYS B CG    1 
ATOM   6371  C  CD    . LYS B 1 99  ? 141.690 132.417 161.531 1.00 42.94 ?  99  LYS B CD    1 
ATOM   6372  C  CE    . LYS B 1 99  ? 140.436 131.664 161.128 1.00 42.46 ?  99  LYS B CE    1 
ATOM   6373  N  NZ    . LYS B 1 99  ? 139.972 132.054 159.770 1.00 47.99 1  99  LYS B NZ    1 
ATOM   6374  N  N     . PHE B 1 100 ? 144.947 136.090 163.458 1.00 36.96 ?  100 PHE B N     1 
ATOM   6375  C  CA    . PHE B 1 100 ? 145.577 137.376 163.181 1.00 34.43 ?  100 PHE B CA    1 
ATOM   6376  C  C     . PHE B 1 100 ? 146.885 137.197 162.422 1.00 37.14 ?  100 PHE B C     1 
ATOM   6377  O  O     . PHE B 1 100 ? 147.099 137.821 161.378 1.00 41.84 ?  100 PHE B O     1 
ATOM   6378  C  CB    . PHE B 1 100 ? 145.827 138.162 164.465 1.00 34.19 ?  100 PHE B CB    1 
ATOM   6379  C  CG    . PHE B 1 100 ? 146.570 139.442 164.225 1.00 37.70 ?  100 PHE B CG    1 
ATOM   6380  C  CD1   . PHE B 1 100 ? 145.942 140.515 163.617 1.00 37.53 ?  100 PHE B CD1   1 
ATOM   6381  C  CD2   . PHE B 1 100 ? 147.906 139.556 164.557 1.00 34.09 ?  100 PHE B CD2   1 
ATOM   6382  C  CE1   . PHE B 1 100 ? 146.626 141.686 163.372 1.00 37.84 ?  100 PHE B CE1   1 
ATOM   6383  C  CE2   . PHE B 1 100 ? 148.594 140.723 164.312 1.00 35.09 ?  100 PHE B CE2   1 
ATOM   6384  C  CZ    . PHE B 1 100 ? 147.954 141.791 163.721 1.00 37.50 ?  100 PHE B CZ    1 
ATOM   6385  N  N     . TYR B 1 101 ? 147.767 136.335 162.919 1.00 40.14 ?  101 TYR B N     1 
ATOM   6386  C  CA    . TYR B 1 101 ? 149.082 136.182 162.316 1.00 36.34 ?  101 TYR B CA    1 
ATOM   6387  C  C     . TYR B 1 101 ? 149.059 135.355 161.040 1.00 35.53 ?  101 TYR B C     1 
ATOM   6388  O  O     . TYR B 1 101 ? 150.100 135.224 160.391 1.00 44.77 ?  101 TYR B O     1 
ATOM   6389  C  CB    . TYR B 1 101 ? 150.051 135.573 163.332 1.00 35.64 ?  101 TYR B CB    1 
ATOM   6390  C  CG    . TYR B 1 101 ? 150.479 136.567 164.385 1.00 33.35 ?  101 TYR B CG    1 
ATOM   6391  C  CD1   . TYR B 1 101 ? 151.350 137.601 164.077 1.00 34.17 ?  101 TYR B CD1   1 
ATOM   6392  C  CD2   . TYR B 1 101 ? 149.989 136.488 165.679 1.00 37.40 ?  101 TYR B CD2   1 
ATOM   6393  C  CE1   . TYR B 1 101 ? 151.733 138.519 165.032 1.00 36.52 ?  101 TYR B CE1   1 
ATOM   6394  C  CE2   . TYR B 1 101 ? 150.364 137.401 166.639 1.00 39.90 ?  101 TYR B CE2   1 
ATOM   6395  C  CZ    . TYR B 1 101 ? 151.237 138.414 166.311 1.00 40.02 ?  101 TYR B CZ    1 
ATOM   6396  O  OH    . TYR B 1 101 ? 151.611 139.323 167.270 1.00 39.82 ?  101 TYR B OH    1 
ATOM   6397  N  N     . ASN B 1 102 ? 147.909 134.793 160.665 1.00 38.82 ?  102 ASN B N     1 
ATOM   6398  C  CA    . ASN B 1 102 ? 147.785 134.124 159.381 1.00 41.96 ?  102 ASN B CA    1 
ATOM   6399  C  C     . ASN B 1 102 ? 146.994 134.922 158.353 1.00 43.72 ?  102 ASN B C     1 
ATOM   6400  O  O     . ASN B 1 102 ? 147.120 134.645 157.156 1.00 48.13 ?  102 ASN B O     1 
ATOM   6401  C  CB    . ASN B 1 102 ? 147.122 132.752 159.561 1.00 40.56 ?  102 ASN B CB    1 
ATOM   6402  C  CG    . ASN B 1 102 ? 148.126 131.654 159.848 1.00 44.81 ?  102 ASN B CG    1 
ATOM   6403  O  OD1   . ASN B 1 102 ? 148.989 131.795 160.715 1.00 48.40 ?  102 ASN B OD1   1 
ATOM   6404  N  ND2   . ASN B 1 102 ? 148.018 130.551 159.119 1.00 43.12 ?  102 ASN B ND2   1 
ATOM   6405  N  N     . ASP B 1 103 ? 146.188 135.895 158.776 1.00 42.99 ?  103 ASP B N     1 
ATOM   6406  C  CA    . ASP B 1 103 ? 145.354 136.636 157.838 1.00 42.91 ?  103 ASP B CA    1 
ATOM   6407  C  C     . ASP B 1 103 ? 145.675 138.120 157.761 1.00 42.58 ?  103 ASP B C     1 
ATOM   6408  O  O     . ASP B 1 103 ? 145.594 138.701 156.677 1.00 46.97 ?  103 ASP B O     1 
ATOM   6409  C  CB    . ASP B 1 103 ? 143.871 136.466 158.208 1.00 45.28 ?  103 ASP B CB    1 
ATOM   6410  C  CG    . ASP B 1 103 ? 143.392 135.035 158.064 1.00 50.09 ?  103 ASP B CG    1 
ATOM   6411  O  OD1   . ASP B 1 103 ? 144.177 134.183 157.602 1.00 50.18 ?  103 ASP B OD1   1 
ATOM   6412  O  OD2   . ASP B 1 103 ? 142.227 134.761 158.419 1.00 53.52 -1 103 ASP B OD2   1 
ATOM   6413  N  N     . TYR B 1 104 ? 146.037 138.753 158.874 1.00 36.66 ?  104 TYR B N     1 
ATOM   6414  C  CA    . TYR B 1 104 ? 146.154 140.202 158.935 1.00 41.43 ?  104 TYR B CA    1 
ATOM   6415  C  C     . TYR B 1 104 ? 147.555 140.707 159.238 1.00 39.97 ?  104 TYR B C     1 
ATOM   6416  O  O     . TYR B 1 104 ? 147.872 141.840 158.873 1.00 45.56 ?  104 TYR B O     1 
ATOM   6417  C  CB    . TYR B 1 104 ? 145.191 140.768 159.991 1.00 37.76 ?  104 TYR B CB    1 
ATOM   6418  C  CG    . TYR B 1 104 ? 143.758 140.342 159.781 1.00 41.00 ?  104 TYR B CG    1 
ATOM   6419  C  CD1   . TYR B 1 104 ? 142.925 141.047 158.926 1.00 40.31 ?  104 TYR B CD1   1 
ATOM   6420  C  CD2   . TYR B 1 104 ? 143.242 139.230 160.431 1.00 35.66 ?  104 TYR B CD2   1 
ATOM   6421  C  CE1   . TYR B 1 104 ? 141.618 140.660 158.727 1.00 39.93 ?  104 TYR B CE1   1 
ATOM   6422  C  CE2   . TYR B 1 104 ? 141.937 138.834 160.238 1.00 36.77 ?  104 TYR B CE2   1 
ATOM   6423  C  CZ    . TYR B 1 104 ? 141.128 139.554 159.384 1.00 41.95 ?  104 TYR B CZ    1 
ATOM   6424  O  OH    . TYR B 1 104 ? 139.825 139.167 159.187 1.00 41.50 ?  104 TYR B OH    1 
ATOM   6425  N  N     . ALA B 1 105 ? 148.393 139.914 159.899 1.00 42.71 ?  105 ALA B N     1 
ATOM   6426  C  CA    . ALA B 1 105 ? 149.740 140.363 160.219 1.00 42.57 ?  105 ALA B CA    1 
ATOM   6427  C  C     . ALA B 1 105 ? 150.568 140.519 158.951 1.00 45.88 ?  105 ALA B C     1 
ATOM   6428  O  O     . ALA B 1 105 ? 150.512 139.680 158.047 1.00 44.64 ?  105 ALA B O     1 
ATOM   6429  C  CB    . ALA B 1 105 ? 150.420 139.382 161.169 1.00 38.01 ?  105 ALA B CB    1 
ATOM   6430  N  N     . LEU B 1 106 ? 151.335 141.602 158.886 1.00 47.08 ?  106 LEU B N     1 
ATOM   6431  C  CA    . LEU B 1 106 ? 152.173 141.855 157.724 1.00 44.38 ?  106 LEU B CA    1 
ATOM   6432  C  C     . LEU B 1 106 ? 153.339 140.876 157.697 1.00 47.36 ?  106 LEU B C     1 
ATOM   6433  O  O     . LEU B 1 106 ? 154.050 140.710 158.691 1.00 47.74 ?  106 LEU B O     1 
ATOM   6434  C  CB    . LEU B 1 106 ? 152.688 143.293 157.741 1.00 48.24 ?  106 LEU B CB    1 
ATOM   6435  C  CG    . LEU B 1 106 ? 153.471 143.757 156.511 1.00 44.94 ?  106 LEU B CG    1 
ATOM   6436  C  CD1   . LEU B 1 106 ? 152.568 143.822 155.293 1.00 44.16 ?  106 LEU B CD1   1 
ATOM   6437  C  CD2   . LEU B 1 106 ? 154.121 145.105 156.770 1.00 44.60 ?  106 LEU B CD2   1 
ATOM   6438  N  N     . LYS B 1 107 ? 153.533 140.232 156.552 1.00 55.35 ?  107 LYS B N     1 
ATOM   6439  C  CA    . LYS B 1 107 ? 154.603 139.271 156.356 1.00 55.18 ?  107 LYS B CA    1 
ATOM   6440  C  C     . LYS B 1 107 ? 155.549 139.769 155.273 1.00 56.71 ?  107 LYS B C     1 
ATOM   6441  O  O     . LYS B 1 107 ? 155.231 140.689 154.513 1.00 55.21 ?  107 LYS B O     1 
ATOM   6442  C  CB    . LYS B 1 107 ? 154.054 137.893 155.974 1.00 54.68 ?  107 LYS B CB    1 
ATOM   6443  C  CG    . LYS B 1 107 ? 153.597 137.059 157.153 1.00 52.82 ?  107 LYS B CG    1 
ATOM   6444  C  CD    . LYS B 1 107 ? 152.752 135.886 156.698 1.00 55.63 ?  107 LYS B CD    1 
ATOM   6445  C  CE    . LYS B 1 107 ? 151.975 135.295 157.856 1.00 57.28 ?  107 LYS B CE    1 
ATOM   6446  N  NZ    . LYS B 1 107 ? 151.582 136.338 158.844 1.00 56.18 1  107 LYS B NZ    1 
ATOM   6447  N  N     . THR B 1 108 ? 156.726 139.150 155.215 1.00 60.92 ?  108 THR B N     1 
ATOM   6448  C  CA    . THR B 1 108 ? 157.695 139.481 154.186 1.00 60.71 ?  108 THR B CA    1 
ATOM   6449  C  C     . THR B 1 108 ? 157.135 139.138 152.806 1.00 62.10 ?  108 THR B C     1 
ATOM   6450  O  O     . THR B 1 108 ? 156.133 138.434 152.667 1.00 62.89 ?  108 THR B O     1 
ATOM   6451  C  CB    . THR B 1 108 ? 159.007 138.736 154.426 1.00 59.88 ?  108 THR B CB    1 
ATOM   6452  O  OG1   . THR B 1 108 ? 158.734 137.346 154.646 1.00 62.05 ?  108 THR B OG1   1 
ATOM   6453  C  CG2   . THR B 1 108 ? 159.732 139.297 155.636 1.00 57.02 ?  108 THR B CG2   1 
ATOM   6454  N  N     . ASN B 1 109 ? 157.804 139.654 151.770 1.00 63.27 ?  109 ASN B N     1 
ATOM   6455  C  CA    . ASN B 1 109 ? 157.340 139.425 150.405 1.00 63.09 ?  109 ASN B CA    1 
ATOM   6456  C  C     . ASN B 1 109 ? 157.329 137.945 150.049 1.00 66.07 ?  109 ASN B C     1 
ATOM   6457  O  O     . ASN B 1 109 ? 156.546 137.521 149.191 1.00 65.99 ?  109 ASN B O     1 
ATOM   6458  C  CB    . ASN B 1 109 ? 158.206 140.204 149.416 1.00 61.80 ?  109 ASN B CB    1 
ATOM   6459  C  CG    . ASN B 1 109 ? 158.235 141.689 149.713 1.00 64.04 ?  109 ASN B CG    1 
ATOM   6460  O  OD1   . ASN B 1 109 ? 157.217 142.373 149.614 1.00 66.19 ?  109 ASN B OD1   1 
ATOM   6461  N  ND2   . ASN B 1 109 ? 159.406 142.196 150.080 1.00 63.88 ?  109 ASN B ND2   1 
ATOM   6462  N  N     . ASP B 1 110 ? 158.182 137.145 150.686 1.00 66.04 ?  110 ASP B N     1 
ATOM   6463  C  CA    . ASP B 1 110 ? 158.169 135.701 150.505 1.00 67.63 ?  110 ASP B CA    1 
ATOM   6464  C  C     . ASP B 1 110 ? 157.290 134.992 151.528 1.00 66.77 ?  110 ASP B C     1 
ATOM   6465  O  O     . ASP B 1 110 ? 157.260 133.757 151.551 1.00 67.18 ?  110 ASP B O     1 
ATOM   6466  C  CB    . ASP B 1 110 ? 159.596 135.143 150.560 1.00 68.15 ?  110 ASP B CB    1 
ATOM   6467  C  CG    . ASP B 1 110 ? 160.261 135.365 151.901 1.00 69.90 ?  110 ASP B CG    1 
ATOM   6468  O  OD1   . ASP B 1 110 ? 159.882 136.322 152.602 1.00 69.54 ?  110 ASP B OD1   1 
ATOM   6469  O  OD2   . ASP B 1 110 ? 161.168 134.581 152.253 1.00 69.81 -1 110 ASP B OD2   1 
ATOM   6470  N  N     . LYS B 1 111 ? 156.574 135.748 152.366 1.00 64.62 ?  111 LYS B N     1 
ATOM   6471  C  CA    . LYS B 1 111 ? 155.655 135.195 153.364 1.00 64.06 ?  111 LYS B CA    1 
ATOM   6472  C  C     . LYS B 1 111 ? 156.363 134.208 154.290 1.00 66.24 ?  111 LYS B C     1 
ATOM   6473  O  O     . LYS B 1 111 ? 155.827 133.151 154.628 1.00 67.00 ?  111 LYS B O     1 
ATOM   6474  C  CB    . LYS B 1 111 ? 154.441 134.541 152.700 1.00 64.89 ?  111 LYS B CB    1 
ATOM   6475  C  CG    . LYS B 1 111 ? 153.811 135.364 151.585 1.00 64.51 ?  111 LYS B CG    1 
ATOM   6476  C  CD    . LYS B 1 111 ? 153.459 136.771 152.050 1.00 66.11 ?  111 LYS B CD    1 
ATOM   6477  C  CE    . LYS B 1 111 ? 152.260 136.765 152.984 1.00 67.79 ?  111 LYS B CE    1 
ATOM   6478  N  NZ    . LYS B 1 111 ? 151.041 136.218 152.327 1.00 68.04 1  111 LYS B NZ    1 
ATOM   6479  N  N     . LYS B 1 112 ? 157.578 134.558 154.705 1.00 65.24 ?  112 LYS B N     1 
ATOM   6480  C  CA    . LYS B 1 112 ? 158.389 133.712 155.572 1.00 64.41 ?  112 LYS B CA    1 
ATOM   6481  C  C     . LYS B 1 112 ? 158.470 134.219 157.003 1.00 64.17 ?  112 LYS B C     1 
ATOM   6482  O  O     . LYS B 1 112 ? 158.355 133.426 157.939 1.00 65.83 ?  112 LYS B O     1 
ATOM   6483  C  CB    . LYS B 1 112 ? 159.805 133.579 154.997 1.00 63.97 ?  112 LYS B CB    1 
ATOM   6484  C  CG    . LYS B 1 112 ? 160.886 133.255 156.019 1.00 67.04 ?  112 LYS B CG    1 
ATOM   6485  C  CD    . LYS B 1 112 ? 160.853 131.787 156.419 1.00 65.11 ?  112 LYS B CD    1 
ATOM   6486  C  CE    . LYS B 1 112 ? 161.417 131.585 157.816 1.00 65.22 ?  112 LYS B CE    1 
ATOM   6487  N  NZ    . LYS B 1 112 ? 160.562 132.220 158.857 1.00 64.88 1  112 LYS B NZ    1 
ATOM   6488  N  N     . LYS B 1 113 ? 158.653 135.518 157.196 1.00 60.20 ?  113 LYS B N     1 
ATOM   6489  C  CA    . LYS B 1 113 ? 158.785 136.120 158.515 1.00 59.08 ?  113 LYS B CA    1 
ATOM   6490  C  C     . LYS B 1 113 ? 157.611 137.060 158.774 1.00 59.43 ?  113 LYS B C     1 
ATOM   6491  O  O     . LYS B 1 113 ? 156.769 137.295 157.905 1.00 57.53 ?  113 LYS B O     1 
ATOM   6492  C  CB    . LYS B 1 113 ? 160.122 136.855 158.637 1.00 57.33 ?  113 LYS B CB    1 
ATOM   6493  C  CG    . LYS B 1 113 ? 161.316 135.946 158.875 1.00 57.95 ?  113 LYS B CG    1 
ATOM   6494  C  CD    . LYS B 1 113 ? 161.346 135.435 160.303 1.00 59.48 ?  113 LYS B CD    1 
ATOM   6495  C  CE    . LYS B 1 113 ? 162.742 134.996 160.704 1.00 57.00 ?  113 LYS B CE    1 
ATOM   6496  N  NZ    . LYS B 1 113 ? 162.824 133.522 160.892 1.00 58.77 1  113 LYS B NZ    1 
ATOM   6497  N  N     . ILE B 1 114 ? 157.564 137.602 159.988 1.00 52.83 ?  114 ILE B N     1 
ATOM   6498  C  CA    . ILE B 1 114 ? 156.472 138.459 160.437 1.00 49.84 ?  114 ILE B CA    1 
ATOM   6499  C  C     . ILE B 1 114 ? 157.039 139.837 160.747 1.00 51.40 ?  114 ILE B C     1 
ATOM   6500  O  O     . ILE B 1 114 ? 157.954 139.967 161.570 1.00 54.24 ?  114 ILE B O     1 
ATOM   6501  C  CB    . ILE B 1 114 ? 155.760 137.872 161.667 1.00 51.19 ?  114 ILE B CB    1 
ATOM   6502  C  CG1   . ILE B 1 114 ? 154.904 136.668 161.271 1.00 49.80 ?  114 ILE B CG1   1 
ATOM   6503  C  CG2   . ILE B 1 114 ? 154.909 138.926 162.351 1.00 51.04 ?  114 ILE B CG2   1 
ATOM   6504  C  CD1   . ILE B 1 114 ? 154.480 135.816 162.443 1.00 46.81 ?  114 ILE B CD1   1 
ATOM   6505  N  N     . LEU B 1 115 ? 156.497 140.864 160.092 1.00 48.43 ?  115 LEU B N     1 
ATOM   6506  C  CA    . LEU B 1 115 ? 156.905 142.238 160.365 1.00 47.70 ?  115 LEU B CA    1 
ATOM   6507  C  C     . LEU B 1 115 ? 156.041 142.904 161.426 1.00 50.04 ?  115 LEU B C     1 
ATOM   6508  O  O     . LEU B 1 115 ? 156.549 143.689 162.233 1.00 51.35 ?  115 LEU B O     1 
ATOM   6509  C  CB    . LEU B 1 115 ? 156.858 143.080 159.086 1.00 49.26 ?  115 LEU B CB    1 
ATOM   6510  C  CG    . LEU B 1 115 ? 157.959 142.919 158.038 1.00 47.40 ?  115 LEU B CG    1 
ATOM   6511  C  CD1   . LEU B 1 115 ? 159.322 142.756 158.693 1.00 49.77 ?  115 LEU B CD1   1 
ATOM   6512  C  CD2   . LEU B 1 115 ? 157.652 141.762 157.118 1.00 48.91 ?  115 LEU B CD2   1 
ATOM   6513  N  N     . GLU B 1 116 ? 154.745 142.609 161.443 1.00 46.96 ?  116 GLU B N     1 
ATOM   6514  C  CA    . GLU B 1 116 ? 153.786 143.319 162.276 1.00 46.21 ?  116 GLU B CA    1 
ATOM   6515  C  C     . GLU B 1 116 ? 153.265 142.415 163.381 1.00 44.69 ?  116 GLU B C     1 
ATOM   6516  O  O     . GLU B 1 116 ? 152.818 141.294 163.117 1.00 49.18 ?  116 GLU B O     1 
ATOM   6517  C  CB    . GLU B 1 116 ? 152.613 143.833 161.439 1.00 43.45 ?  116 GLU B CB    1 
ATOM   6518  C  CG    . GLU B 1 116 ? 152.717 145.290 161.047 1.00 44.40 ?  116 GLU B CG    1 
ATOM   6519  C  CD    . GLU B 1 116 ? 151.568 145.733 160.167 1.00 47.71 ?  116 GLU B CD    1 
ATOM   6520  O  OE1   . GLU B 1 116 ? 150.747 144.874 159.784 1.00 49.39 ?  116 GLU B OE1   1 
ATOM   6521  O  OE2   . GLU B 1 116 ? 151.483 146.939 159.860 1.00 50.22 -1 116 GLU B OE2   1 
ATOM   6522  N  N     . ARG B 1 117 ? 153.318 142.908 164.613 1.00 39.36 ?  117 ARG B N     1 
ATOM   6523  C  CA    . ARG B 1 117 ? 152.580 142.307 165.707 1.00 41.72 ?  117 ARG B CA    1 
ATOM   6524  C  C     . ARG B 1 117 ? 151.165 142.881 165.715 1.00 41.09 ?  117 ARG B C     1 
ATOM   6525  O  O     . ARG B 1 117 ? 150.793 143.691 164.863 1.00 39.45 ?  117 ARG B O     1 
ATOM   6526  C  CB    . ARG B 1 117 ? 153.289 142.557 167.037 1.00 42.00 ?  117 ARG B CB    1 
ATOM   6527  C  CG    . ARG B 1 117 ? 154.687 141.972 167.118 1.00 40.80 ?  117 ARG B CG    1 
ATOM   6528  C  CD    . ARG B 1 117 ? 154.699 140.500 166.737 1.00 46.77 ?  117 ARG B CD    1 
ATOM   6529  N  NE    . ARG B 1 117 ? 154.494 139.630 167.890 1.00 44.38 ?  117 ARG B NE    1 
ATOM   6530  C  CZ    . ARG B 1 117 ? 155.378 139.439 168.860 1.00 45.70 ?  117 ARG B CZ    1 
ATOM   6531  N  NH1   . ARG B 1 117 ? 156.563 140.028 168.843 1.00 43.54 1  117 ARG B NH1   1 
ATOM   6532  N  NH2   . ARG B 1 117 ? 155.068 138.632 169.871 1.00 47.75 ?  117 ARG B NH2   1 
ATOM   6533  N  N     . TYR B 1 118 ? 150.356 142.452 166.682 1.00 41.03 ?  118 TYR B N     1 
ATOM   6534  C  CA    . TYR B 1 118 ? 149.024 143.030 166.820 1.00 35.12 ?  118 TYR B CA    1 
ATOM   6535  C  C     . TYR B 1 118 ? 149.110 144.516 167.141 1.00 38.01 ?  118 TYR B C     1 
ATOM   6536  O  O     . TYR B 1 118 ? 148.367 145.330 166.578 1.00 40.88 ?  118 TYR B O     1 
ATOM   6537  C  CB    . TYR B 1 118 ? 148.237 142.285 167.895 1.00 36.39 ?  118 TYR B CB    1 
ATOM   6538  C  CG    . TYR B 1 118 ? 146.757 142.582 167.885 1.00 38.14 ?  118 TYR B CG    1 
ATOM   6539  C  CD1   . TYR B 1 118 ? 146.003 142.409 166.733 1.00 33.51 ?  118 TYR B CD1   1 
ATOM   6540  C  CD2   . TYR B 1 118 ? 146.114 143.037 169.024 1.00 36.95 ?  118 TYR B CD2   1 
ATOM   6541  C  CE1   . TYR B 1 118 ? 144.653 142.678 166.718 1.00 33.42 ?  118 TYR B CE1   1 
ATOM   6542  C  CE2   . TYR B 1 118 ? 144.762 143.306 169.021 1.00 33.77 ?  118 TYR B CE2   1 
ATOM   6543  C  CZ    . TYR B 1 118 ? 144.036 143.126 167.864 1.00 35.25 ?  118 TYR B CZ    1 
ATOM   6544  O  OH    . TYR B 1 118 ? 142.689 143.396 167.854 1.00 45.00 ?  118 TYR B OH    1 
ATOM   6545  N  N     . GLU B 1 119 ? 150.030 144.886 168.033 1.00 44.44 ?  119 GLU B N     1 
ATOM   6546  C  CA    . GLU B 1 119 ? 150.191 146.288 168.398 1.00 38.64 ?  119 GLU B CA    1 
ATOM   6547  C  C     . GLU B 1 119 ? 150.671 147.123 167.218 1.00 38.45 ?  119 GLU B C     1 
ATOM   6548  O  O     . GLU B 1 119 ? 150.227 148.260 167.044 1.00 49.14 ?  119 GLU B O     1 
ATOM   6549  C  CB    . GLU B 1 119 ? 151.154 146.411 169.577 1.00 38.99 ?  119 GLU B CB    1 
ATOM   6550  C  CG    . GLU B 1 119 ? 150.621 145.820 170.870 1.00 39.79 ?  119 GLU B CG    1 
ATOM   6551  C  CD    . GLU B 1 119 ? 151.064 144.387 171.084 1.00 45.71 ?  119 GLU B CD    1 
ATOM   6552  O  OE1   . GLU B 1 119 ? 151.301 143.679 170.082 1.00 45.33 ?  119 GLU B OE1   1 
ATOM   6553  O  OE2   . GLU B 1 119 ? 151.174 143.965 172.254 1.00 46.42 -1 119 GLU B OE2   1 
ATOM   6554  N  N     . ASP B 1 120 ? 151.580 146.586 166.400 1.00 40.96 ?  120 ASP B N     1 
ATOM   6555  C  CA    . ASP B 1 120 ? 152.056 147.339 165.241 1.00 39.84 ?  120 ASP B CA    1 
ATOM   6556  C  C     . ASP B 1 120 ? 150.937 147.566 164.233 1.00 39.51 ?  120 ASP B C     1 
ATOM   6557  O  O     . ASP B 1 120 ? 150.782 148.672 163.701 1.00 44.82 ?  120 ASP B O     1 
ATOM   6558  C  CB    . ASP B 1 120 ? 153.230 146.615 164.581 1.00 45.29 ?  120 ASP B CB    1 
ATOM   6559  C  CG    . ASP B 1 120 ? 154.236 146.100 165.583 1.00 47.85 ?  120 ASP B CG    1 
ATOM   6560  O  OD1   . ASP B 1 120 ? 154.651 144.931 165.458 1.00 51.60 ?  120 ASP B OD1   1 
ATOM   6561  O  OD2   . ASP B 1 120 ? 154.605 146.862 166.500 1.00 46.55 -1 120 ASP B OD2   1 
ATOM   6562  N  N     . ARG B 1 121 ? 150.151 146.525 163.953 1.00 34.52 ?  121 ARG B N     1 
ATOM   6563  C  CA    . ARG B 1 121 ? 149.024 146.667 163.038 1.00 31.09 ?  121 ARG B CA    1 
ATOM   6564  C  C     . ARG B 1 121 ? 148.018 147.681 163.561 1.00 35.79 ?  121 ARG B C     1 
ATOM   6565  O  O     . ARG B 1 121 ? 147.526 148.529 162.806 1.00 45.87 ?  121 ARG B O     1 
ATOM   6566  C  CB    . ARG B 1 121 ? 148.362 145.307 162.818 1.00 35.38 ?  121 ARG B CB    1 
ATOM   6567  C  CG    . ARG B 1 121 ? 147.107 145.338 161.965 1.00 32.93 ?  121 ARG B CG    1 
ATOM   6568  C  CD    . ARG B 1 121 ? 147.431 145.206 160.492 1.00 32.41 ?  121 ARG B CD    1 
ATOM   6569  N  NE    . ARG B 1 121 ? 147.241 146.468 159.790 1.00 43.28 ?  121 ARG B NE    1 
ATOM   6570  C  CZ    . ARG B 1 121 ? 148.028 146.912 158.821 1.00 39.89 ?  121 ARG B CZ    1 
ATOM   6571  N  NH1   . ARG B 1 121 ? 149.074 146.216 158.408 1.00 42.44 1  121 ARG B NH1   1 
ATOM   6572  N  NH2   . ARG B 1 121 ? 147.760 148.083 158.255 1.00 32.92 ?  121 ARG B NH2   1 
ATOM   6573  N  N     . ILE B 1 122 ? 147.713 147.622 164.859 1.00 35.39 ?  122 ILE B N     1 
ATOM   6574  C  CA    . ILE B 1 122 ? 146.753 148.556 165.436 1.00 29.58 ?  122 ILE B CA    1 
ATOM   6575  C  C     . ILE B 1 122 ? 147.295 149.980 165.401 1.00 30.42 ?  122 ILE B C     1 
ATOM   6576  O  O     . ILE B 1 122 ? 146.560 150.928 165.108 1.00 37.63 ?  122 ILE B O     1 
ATOM   6577  C  CB    . ILE B 1 122 ? 146.374 148.109 166.859 1.00 35.40 ?  122 ILE B CB    1 
ATOM   6578  C  CG1   . ILE B 1 122 ? 145.316 147.009 166.782 1.00 32.27 ?  122 ILE B CG1   1 
ATOM   6579  C  CG2   . ILE B 1 122 ? 145.871 149.281 167.689 1.00 31.89 ?  122 ILE B CG2   1 
ATOM   6580  C  CD1   . ILE B 1 122 ? 144.699 146.665 168.098 1.00 32.92 ?  122 ILE B CD1   1 
ATOM   6581  N  N     . SER B 1 123 ? 148.587 150.157 165.687 1.00 33.76 ?  123 SER B N     1 
ATOM   6582  C  CA    . SER B 1 123 ? 149.184 151.487 165.635 1.00 32.60 ?  123 SER B CA    1 
ATOM   6583  C  C     . SER B 1 123 ? 149.149 152.056 164.226 1.00 36.18 ?  123 SER B C     1 
ATOM   6584  O  O     . SER B 1 123 ? 148.850 153.239 164.035 1.00 36.84 ?  123 SER B O     1 
ATOM   6585  C  CB    . SER B 1 123 ? 150.624 151.439 166.142 1.00 32.05 ?  123 SER B CB    1 
ATOM   6586  O  OG    . SER B 1 123 ? 150.688 150.893 167.441 1.00 37.98 ?  123 SER B OG    1 
ATOM   6587  N  N     . ILE B 1 124 ? 149.457 151.232 163.224 1.00 36.71 ?  124 ILE B N     1 
ATOM   6588  C  CA    . ILE B 1 124 ? 149.434 151.711 161.846 1.00 34.76 ?  124 ILE B CA    1 
ATOM   6589  C  C     . ILE B 1 124 ? 148.015 152.073 161.429 1.00 39.62 ?  124 ILE B C     1 
ATOM   6590  O  O     . ILE B 1 124 ? 147.786 153.109 160.790 1.00 39.84 ?  124 ILE B O     1 
ATOM   6591  C  CB    . ILE B 1 124 ? 150.062 150.665 160.910 1.00 39.41 ?  124 ILE B CB    1 
ATOM   6592  C  CG1   . ILE B 1 124 ? 151.584 150.693 161.052 1.00 41.25 ?  124 ILE B CG1   1 
ATOM   6593  C  CG2   . ILE B 1 124 ? 149.658 150.918 159.468 1.00 36.46 ?  124 ILE B CG2   1 
ATOM   6594  C  CD1   . ILE B 1 124 ? 152.186 152.074 160.899 1.00 36.63 ?  124 ILE B CD1   1 
ATOM   6595  N  N     . VAL B 1 125 ? 147.036 151.243 161.800 1.00 32.40 ?  125 VAL B N     1 
ATOM   6596  C  CA    . VAL B 1 125 ? 145.647 151.538 161.462 1.00 30.50 ?  125 VAL B CA    1 
ATOM   6597  C  C     . VAL B 1 125 ? 145.194 152.828 162.137 1.00 25.65 ?  125 VAL B C     1 
ATOM   6598  O  O     . VAL B 1 125 ? 144.509 153.657 161.527 1.00 35.98 ?  125 VAL B O     1 
ATOM   6599  C  CB    . VAL B 1 125 ? 144.744 150.346 161.833 1.00 37.24 ?  125 VAL B CB    1 
ATOM   6600  C  CG1   . VAL B 1 125 ? 143.283 150.736 161.757 1.00 32.65 ?  125 VAL B CG1   1 
ATOM   6601  C  CG2   . VAL B 1 125 ? 145.019 149.171 160.910 1.00 27.59 ?  125 VAL B CG2   1 
ATOM   6602  N  N     . ALA B 1 126 ? 145.580 153.026 163.399 1.00 24.10 ?  126 ALA B N     1 
ATOM   6603  C  CA    . ALA B 1 126 ? 145.199 154.239 164.116 1.00 26.21 ?  126 ALA B CA    1 
ATOM   6604  C  C     . ALA B 1 126 ? 145.859 155.477 163.522 1.00 31.08 ?  126 ALA B C     1 
ATOM   6605  O  O     . ALA B 1 126 ? 145.227 156.534 163.418 1.00 34.62 ?  126 ALA B O     1 
ATOM   6606  C  CB    . ALA B 1 126 ? 145.560 154.104 165.592 1.00 29.96 ?  126 ALA B CB    1 
ATOM   6607  N  N     . LEU B 1 127 ? 147.135 155.370 163.146 1.00 36.91 ?  127 LEU B N     1 
ATOM   6608  C  CA    . LEU B 1 127 ? 147.827 156.503 162.543 1.00 26.42 ?  127 LEU B CA    1 
ATOM   6609  C  C     . LEU B 1 127 ? 147.231 156.846 161.186 1.00 26.74 ?  127 LEU B C     1 
ATOM   6610  O  O     . LEU B 1 127 ? 147.190 158.018 160.797 1.00 33.01 ?  127 LEU B O     1 
ATOM   6611  C  CB    . LEU B 1 127 ? 149.320 156.201 162.414 1.00 28.93 ?  127 LEU B CB    1 
ATOM   6612  C  CG    . LEU B 1 127 ? 150.144 156.214 163.703 1.00 32.83 ?  127 LEU B CG    1 
ATOM   6613  C  CD1   . LEU B 1 127 ? 151.449 155.467 163.508 1.00 38.52 ?  127 LEU B CD1   1 
ATOM   6614  C  CD2   . LEU B 1 127 ? 150.407 157.635 164.162 1.00 33.35 ?  127 LEU B CD2   1 
ATOM   6615  N  N     . PHE B 1 128 ? 146.773 155.835 160.446 1.00 32.50 ?  128 PHE B N     1 
ATOM   6616  C  CA    . PHE B 1 128 ? 146.080 156.100 159.191 1.00 33.27 ?  128 PHE B CA    1 
ATOM   6617  C  C     . PHE B 1 128 ? 144.720 156.743 159.442 1.00 30.13 ?  128 PHE B C     1 
ATOM   6618  O  O     . PHE B 1 128 ? 144.302 157.634 158.694 1.00 40.74 ?  128 PHE B O     1 
ATOM   6619  C  CB    . PHE B 1 128 ? 145.951 154.800 158.390 1.00 29.67 ?  128 PHE B CB    1 
ATOM   6620  C  CG    . PHE B 1 128 ? 144.962 154.865 157.260 1.00 35.44 ?  128 PHE B CG    1 
ATOM   6621  C  CD1   . PHE B 1 128 ? 143.617 154.595 157.466 1.00 33.75 ?  128 PHE B CD1   1 
ATOM   6622  C  CD2   . PHE B 1 128 ? 145.381 155.201 155.985 1.00 37.02 ?  128 PHE B CD2   1 
ATOM   6623  C  CE1   . PHE B 1 128 ? 142.717 154.662 156.425 1.00 34.62 ?  128 PHE B CE1   1 
ATOM   6624  C  CE2   . PHE B 1 128 ? 144.484 155.267 154.941 1.00 36.99 ?  128 PHE B CE2   1 
ATOM   6625  C  CZ    . PHE B 1 128 ? 143.152 154.999 155.161 1.00 34.68 ?  128 PHE B CZ    1 
ATOM   6626  N  N     . PHE B 1 129 ? 144.013 156.298 160.483 1.00 27.70 ?  129 PHE B N     1 
ATOM   6627  C  CA    . PHE B 1 129 ? 142.706 156.864 160.802 1.00 21.42 ?  129 PHE B CA    1 
ATOM   6628  C  C     . PHE B 1 129 ? 142.809 158.327 161.207 1.00 30.37 ?  129 PHE B C     1 
ATOM   6629  O  O     . PHE B 1 129 ? 141.995 159.153 160.781 1.00 33.81 ?  129 PHE B O     1 
ATOM   6630  C  CB    . PHE B 1 129 ? 142.044 156.066 161.924 1.00 24.55 ?  129 PHE B CB    1 
ATOM   6631  C  CG    . PHE B 1 129 ? 141.391 154.798 161.473 1.00 26.58 ?  129 PHE B CG    1 
ATOM   6632  C  CD1   . PHE B 1 129 ? 141.144 154.564 160.133 1.00 26.21 ?  129 PHE B CD1   1 
ATOM   6633  C  CD2   . PHE B 1 129 ? 141.012 153.841 162.397 1.00 28.07 ?  129 PHE B CD2   1 
ATOM   6634  C  CE1   . PHE B 1 129 ? 140.540 153.395 159.725 1.00 25.06 ?  129 PHE B CE1   1 
ATOM   6635  C  CE2   . PHE B 1 129 ? 140.404 152.671 161.994 1.00 30.63 ?  129 PHE B CE2   1 
ATOM   6636  C  CZ    . PHE B 1 129 ? 140.169 152.447 160.656 1.00 30.17 ?  129 PHE B CZ    1 
ATOM   6637  N  N     . ALA B 1 130 ? 143.796 158.664 162.040 1.00 35.74 ?  130 ALA B N     1 
ATOM   6638  C  CA    . ALA B 1 130 ? 143.856 160.007 162.608 1.00 35.44 ?  130 ALA B CA    1 
ATOM   6639  C  C     . ALA B 1 130 ? 144.213 161.058 161.565 1.00 42.14 ?  130 ALA B C     1 
ATOM   6640  O  O     . ALA B 1 130 ? 143.782 162.210 161.683 1.00 47.31 ?  130 ALA B O     1 
ATOM   6641  C  CB    . ALA B 1 130 ? 144.855 160.042 163.758 1.00 33.44 ?  130 ALA B CB    1 
ATOM   6642  N  N     . ASN B 1 131 ? 144.999 160.686 160.554 1.00 41.73 ?  131 ASN B N     1 
ATOM   6643  C  CA    . ASN B 1 131 ? 145.351 161.579 159.449 1.00 41.38 ?  131 ASN B CA    1 
ATOM   6644  C  C     . ASN B 1 131 ? 146.069 162.835 159.947 1.00 42.82 ?  131 ASN B C     1 
ATOM   6645  O  O     . ASN B 1 131 ? 145.762 163.957 159.540 1.00 46.71 ?  131 ASN B O     1 
ATOM   6646  C  CB    . ASN B 1 131 ? 144.110 161.943 158.629 1.00 40.39 ?  131 ASN B CB    1 
ATOM   6647  C  CG    . ASN B 1 131 ? 144.444 162.336 157.206 1.00 46.02 ?  131 ASN B CG    1 
ATOM   6648  O  OD1   . ASN B 1 131 ? 145.295 161.723 156.563 1.00 45.99 ?  131 ASN B OD1   1 
ATOM   6649  N  ND2   . ASN B 1 131 ? 143.773 163.365 156.704 1.00 44.13 ?  131 ASN B ND2   1 
ATOM   6650  N  N     . GLY B 1 132 ? 147.036 162.638 160.840 1.00 42.48 ?  132 GLY B N     1 
ATOM   6651  C  CA    . GLY B 1 132 ? 147.890 163.713 161.307 1.00 39.49 ?  132 GLY B CA    1 
ATOM   6652  C  C     . GLY B 1 132 ? 147.663 164.151 162.737 1.00 44.84 ?  132 GLY B C     1 
ATOM   6653  O  O     . GLY B 1 132 ? 148.436 164.979 163.236 1.00 50.55 ?  132 GLY B O     1 
ATOM   6654  N  N     . ASP B 1 133 ? 146.646 163.633 163.417 1.00 46.99 ?  133 ASP B N     1 
ATOM   6655  C  CA    . ASP B 1 133 ? 146.345 164.015 164.791 1.00 47.34 ?  133 ASP B CA    1 
ATOM   6656  C  C     . ASP B 1 133 ? 146.913 162.965 165.738 1.00 48.68 ?  133 ASP B C     1 
ATOM   6657  O  O     . ASP B 1 133 ? 146.538 161.791 165.669 1.00 48.93 ?  133 ASP B O     1 
ATOM   6658  C  CB    . ASP B 1 133 ? 144.838 164.168 164.992 1.00 47.18 ?  133 ASP B CB    1 
ATOM   6659  C  CG    . ASP B 1 133 ? 144.489 164.928 166.258 1.00 52.90 ?  133 ASP B CG    1 
ATOM   6660  O  OD1   . ASP B 1 133 ? 145.386 165.141 167.099 1.00 54.28 ?  133 ASP B OD1   1 
ATOM   6661  O  OD2   . ASP B 1 133 ? 143.309 165.308 166.414 1.00 50.36 -1 133 ASP B OD2   1 
ATOM   6662  N  N     . THR B 1 134 ? 147.816 163.388 166.625 1.00 49.26 ?  134 THR B N     1 
ATOM   6663  C  CA    . THR B 1 134 ? 148.459 162.439 167.529 1.00 45.20 ?  134 THR B CA    1 
ATOM   6664  C  C     . THR B 1 134 ? 147.510 161.986 168.632 1.00 47.30 ?  134 THR B C     1 
ATOM   6665  O  O     . THR B 1 134 ? 147.464 160.798 168.969 1.00 50.75 ?  134 THR B O     1 
ATOM   6666  C  CB    . THR B 1 134 ? 149.718 163.059 168.127 1.00 53.73 ?  134 THR B CB    1 
ATOM   6667  O  OG1   . THR B 1 134 ? 150.579 163.492 167.067 1.00 55.93 ?  134 THR B OG1   1 
ATOM   6668  C  CG2   . THR B 1 134 ? 150.454 162.044 168.986 1.00 50.56 ?  134 THR B CG2   1 
ATOM   6669  N  N     . GLU B 1 135 ? 146.748 162.918 169.210 1.00 46.01 ?  135 GLU B N     1 
ATOM   6670  C  CA    . GLU B 1 135 ? 145.787 162.546 170.241 1.00 45.42 ?  135 GLU B CA    1 
ATOM   6671  C  C     . GLU B 1 135 ? 144.689 161.656 169.674 1.00 50.14 ?  135 GLU B C     1 
ATOM   6672  O  O     . GLU B 1 135 ? 144.264 160.694 170.322 1.00 51.83 ?  135 GLU B O     1 
ATOM   6673  C  CB    . GLU B 1 135 ? 145.192 163.798 170.882 1.00 47.74 ?  135 GLU B CB    1 
ATOM   6674  C  CG    . GLU B 1 135 ? 146.229 164.761 171.430 1.00 48.68 ?  135 GLU B CG    1 
ATOM   6675  C  CD    . GLU B 1 135 ? 147.342 164.055 172.177 1.00 55.32 ?  135 GLU B CD    1 
ATOM   6676  O  OE1   . GLU B 1 135 ? 147.051 163.396 173.198 1.00 54.01 ?  135 GLU B OE1   1 
ATOM   6677  O  OE2   . GLU B 1 135 ? 148.508 164.157 171.744 1.00 55.95 -1 135 GLU B OE2   1 
ATOM   6678  N  N     . LYS B 1 136 ? 144.218 161.964 168.464 1.00 40.63 ?  136 LYS B N     1 
ATOM   6679  C  CA    . LYS B 1 136 ? 143.230 161.110 167.814 1.00 38.65 ?  136 LYS B CA    1 
ATOM   6680  C  C     . LYS B 1 136 ? 143.800 159.726 167.533 1.00 39.71 ?  136 LYS B C     1 
ATOM   6681  O  O     . LYS B 1 136 ? 143.106 158.715 167.691 1.00 46.00 ?  136 LYS B O     1 
ATOM   6682  C  CB    . LYS B 1 136 ? 142.743 161.768 166.524 1.00 46.29 ?  136 LYS B CB    1 
ATOM   6683  C  CG    . LYS B 1 136 ? 141.454 161.199 165.968 1.00 41.83 ?  136 LYS B CG    1 
ATOM   6684  C  CD    . LYS B 1 136 ? 140.244 161.799 166.654 1.00 43.62 ?  136 LYS B CD    1 
ATOM   6685  C  CE    . LYS B 1 136 ? 138.968 161.472 165.898 1.00 46.52 ?  136 LYS B CE    1 
ATOM   6686  N  NZ    . LYS B 1 136 ? 137.815 162.273 166.392 1.00 49.13 1  136 LYS B NZ    1 
ATOM   6687  N  N     . ALA B 1 137 ? 145.064 159.658 167.106 1.00 34.81 ?  137 ALA B N     1 
ATOM   6688  C  CA    . ALA B 1 137 ? 145.698 158.366 166.871 1.00 31.55 ?  137 ALA B CA    1 
ATOM   6689  C  C     . ALA B 1 137 ? 145.807 157.563 168.160 1.00 35.22 ?  137 ALA B C     1 
ATOM   6690  O  O     . ALA B 1 137 ? 145.583 156.348 168.164 1.00 38.48 ?  137 ALA B O     1 
ATOM   6691  C  CB    . ALA B 1 137 ? 147.078 158.559 166.242 1.00 31.27 ?  137 ALA B CB    1 
ATOM   6692  N  N     . LYS B 1 138 ? 146.153 158.225 169.266 1.00 39.95 ?  138 LYS B N     1 
ATOM   6693  C  CA    . LYS B 1 138 ? 146.211 157.536 170.551 1.00 38.43 ?  138 LYS B CA    1 
ATOM   6694  C  C     . LYS B 1 138 ? 144.830 157.063 170.984 1.00 38.29 ?  138 LYS B C     1 
ATOM   6695  O  O     . LYS B 1 138 ? 144.691 155.983 171.570 1.00 41.57 ?  138 LYS B O     1 
ATOM   6696  C  CB    . LYS B 1 138 ? 146.826 158.451 171.609 1.00 46.55 ?  138 LYS B CB    1 
ATOM   6697  C  CG    . LYS B 1 138 ? 148.297 158.183 171.873 1.00 45.57 ?  138 LYS B CG    1 
ATOM   6698  C  CD    . LYS B 1 138 ? 149.110 159.464 171.863 1.00 42.75 ?  138 LYS B CD    1 
ATOM   6699  C  CE    . LYS B 1 138 ? 148.595 160.456 172.888 1.00 41.41 ?  138 LYS B CE    1 
ATOM   6700  N  NZ    . LYS B 1 138 ? 149.463 161.663 172.969 1.00 45.27 1  138 LYS B NZ    1 
ATOM   6701  N  N     . GLU B 1 139 ? 143.795 157.861 170.714 1.00 42.21 ?  139 GLU B N     1 
ATOM   6702  C  CA    . GLU B 1 139 ? 142.433 157.439 171.022 1.00 37.82 ?  139 GLU B CA    1 
ATOM   6703  C  C     . GLU B 1 139 ? 142.040 156.209 170.215 1.00 34.72 ?  139 GLU B C     1 
ATOM   6704  O  O     . GLU B 1 139 ? 141.421 155.281 170.748 1.00 43.86 ?  139 GLU B O     1 
ATOM   6705  C  CB    . GLU B 1 139 ? 141.458 158.586 170.765 1.00 36.39 ?  139 GLU B CB    1 
ATOM   6706  C  CG    . GLU B 1 139 ? 140.999 159.297 172.022 1.00 41.29 ?  139 GLU B CG    1 
ATOM   6707  C  CD    . GLU B 1 139 ? 140.816 160.786 171.817 1.00 49.30 ?  139 GLU B CD    1 
ATOM   6708  O  OE1   . GLU B 1 139 ? 140.286 161.181 170.757 1.00 46.90 ?  139 GLU B OE1   1 
ATOM   6709  O  OE2   . GLU B 1 139 ? 141.199 161.562 172.717 1.00 47.07 -1 139 GLU B OE2   1 
ATOM   6710  N  N     . TYR B 1 140 ? 142.387 156.184 168.928 1.00 27.13 ?  140 TYR B N     1 
ATOM   6711  C  CA    . TYR B 1 140 ? 142.111 155.007 168.108 1.00 28.57 ?  140 TYR B CA    1 
ATOM   6712  C  C     . TYR B 1 140 ? 142.889 153.796 168.607 1.00 32.48 ?  140 TYR B C     1 
ATOM   6713  O  O     . TYR B 1 140 ? 142.374 152.670 168.603 1.00 35.20 ?  140 TYR B O     1 
ATOM   6714  C  CB    . TYR B 1 140 ? 142.450 155.285 166.646 1.00 31.21 ?  140 TYR B CB    1 
ATOM   6715  C  CG    . TYR B 1 140 ? 141.464 156.159 165.912 1.00 33.68 ?  140 TYR B CG    1 
ATOM   6716  C  CD1   . TYR B 1 140 ? 140.117 155.829 165.851 1.00 36.18 ?  140 TYR B CD1   1 
ATOM   6717  C  CD2   . TYR B 1 140 ? 141.886 157.306 165.260 1.00 34.26 ?  140 TYR B CD2   1 
ATOM   6718  C  CE1   . TYR B 1 140 ? 139.221 156.626 165.170 1.00 34.00 ?  140 TYR B CE1   1 
ATOM   6719  C  CE2   . TYR B 1 140 ? 141.000 158.106 164.581 1.00 32.61 ?  140 TYR B CE2   1 
ATOM   6720  C  CZ    . TYR B 1 140 ? 139.670 157.765 164.539 1.00 30.34 ?  140 TYR B CZ    1 
ATOM   6721  O  OH    . TYR B 1 140 ? 138.794 158.572 163.856 1.00 37.65 ?  140 TYR B OH    1 
ATOM   6722  N  N     . VAL B 1 141 ? 144.140 154.006 169.023 1.00 36.80 ?  141 VAL B N     1 
ATOM   6723  C  CA    . VAL B 1 141 ? 144.942 152.919 169.577 1.00 34.60 ?  141 VAL B CA    1 
ATOM   6724  C  C     . VAL B 1 141 ? 144.284 152.354 170.825 1.00 31.82 ?  141 VAL B C     1 
ATOM   6725  O  O     . VAL B 1 141 ? 144.198 151.137 171.001 1.00 38.24 ?  141 VAL B O     1 
ATOM   6726  C  CB    . VAL B 1 141 ? 146.375 153.402 169.870 1.00 36.80 ?  141 VAL B CB    1 
ATOM   6727  C  CG1   . VAL B 1 141 ? 147.034 152.497 170.884 1.00 35.04 ?  141 VAL B CG1   1 
ATOM   6728  C  CG2   . VAL B 1 141 ? 147.191 153.414 168.606 1.00 35.06 ?  141 VAL B CG2   1 
ATOM   6729  N  N     . ASN B 1 142 ? 143.817 153.229 171.715 1.00 33.90 ?  142 ASN B N     1 
ATOM   6730  C  CA    . ASN B 1 142 ? 143.144 152.757 172.921 1.00 33.04 ?  142 ASN B CA    1 
ATOM   6731  C  C     . ASN B 1 142 ? 141.849 152.035 172.577 1.00 34.96 ?  142 ASN B C     1 
ATOM   6732  O  O     . ASN B 1 142 ? 141.502 151.035 173.214 1.00 41.23 ?  142 ASN B O     1 
ATOM   6733  C  CB    . ASN B 1 142 ? 142.877 153.927 173.865 1.00 30.82 ?  142 ASN B CB    1 
ATOM   6734  C  CG    . ASN B 1 142 ? 144.120 154.368 174.606 1.00 36.66 ?  142 ASN B CG    1 
ATOM   6735  O  OD1   . ASN B 1 142 ? 144.849 153.546 175.161 1.00 37.28 ?  142 ASN B OD1   1 
ATOM   6736  N  ND2   . ASN B 1 142 ? 144.371 155.671 174.617 1.00 38.79 ?  142 ASN B ND2   1 
ATOM   6737  N  N     . LEU B 1 143 ? 141.121 152.527 171.574 1.00 34.18 ?  143 LEU B N     1 
ATOM   6738  C  CA    . LEU B 1 143 ? 139.865 151.898 171.185 1.00 28.75 ?  143 LEU B CA    1 
ATOM   6739  C  C     . LEU B 1 143 ? 140.088 150.500 170.620 1.00 32.78 ?  143 LEU B C     1 
ATOM   6740  O  O     . LEU B 1 143 ? 139.317 149.579 170.911 1.00 36.15 ?  143 LEU B O     1 
ATOM   6741  C  CB    . LEU B 1 143 ? 139.138 152.776 170.170 1.00 28.80 ?  143 LEU B CB    1 
ATOM   6742  C  CG    . LEU B 1 143 ? 137.627 152.588 170.095 1.00 34.07 ?  143 LEU B CG    1 
ATOM   6743  C  CD1   . LEU B 1 143 ? 136.974 153.170 171.334 1.00 32.88 ?  143 LEU B CD1   1 
ATOM   6744  C  CD2   . LEU B 1 143 ? 137.080 153.234 168.841 1.00 33.46 ?  143 LEU B CD2   1 
ATOM   6745  N  N     . MET B 1 144 ? 141.128 150.322 169.808 1.00 34.58 ?  144 MET B N     1 
ATOM   6746  C  CA    . MET B 1 144 ? 141.348 149.043 169.142 1.00 24.95 ?  144 MET B CA    1 
ATOM   6747  C  C     . MET B 1 144 ? 142.141 148.050 169.980 1.00 25.64 ?  144 MET B C     1 
ATOM   6748  O  O     . MET B 1 144 ? 141.879 146.845 169.903 1.00 34.30 ?  144 MET B O     1 
ATOM   6749  C  CB    . MET B 1 144 ? 142.049 149.264 167.800 1.00 27.95 ?  144 MET B CB    1 
ATOM   6750  C  CG    . MET B 1 144 ? 141.204 150.025 166.792 1.00 28.00 ?  144 MET B CG    1 
ATOM   6751  S  SD    . MET B 1 144 ? 141.913 150.022 165.139 1.00 45.60 ?  144 MET B SD    1 
ATOM   6752  C  CE    . MET B 1 144 ? 143.349 151.053 165.402 1.00 26.96 ?  144 MET B CE    1 
ATOM   6753  N  N     . ILE B 1 145 ? 143.113 148.514 170.770 1.00 28.38 ?  145 ILE B N     1 
ATOM   6754  C  CA    . ILE B 1 145 ? 143.859 147.605 171.634 1.00 29.34 ?  145 ILE B CA    1 
ATOM   6755  C  C     . ILE B 1 145 ? 142.984 147.124 172.783 1.00 35.80 ?  145 ILE B C     1 
ATOM   6756  O  O     . ILE B 1 145 ? 143.149 145.998 173.267 1.00 39.90 ?  145 ILE B O     1 
ATOM   6757  C  CB    . ILE B 1 145 ? 145.161 148.271 172.125 1.00 31.03 ?  145 ILE B CB    1 
ATOM   6758  C  CG1   . ILE B 1 145 ? 146.248 147.218 172.351 1.00 32.44 ?  145 ILE B CG1   1 
ATOM   6759  C  CG2   . ILE B 1 145 ? 144.935 149.082 173.394 1.00 33.30 ?  145 ILE B CG2   1 
ATOM   6760  C  CD1   . ILE B 1 145 ? 146.755 146.577 171.083 1.00 35.50 ?  145 ILE B CD1   1 
ATOM   6761  N  N     . ASN B 1 146 ? 142.040 147.953 173.237 1.00 33.84 ?  146 ASN B N     1 
ATOM   6762  C  CA    . ASN B 1 146 ? 141.005 147.480 174.144 1.00 27.26 ?  146 ASN B CA    1 
ATOM   6763  C  C     . ASN B 1 146 ? 139.985 146.610 173.430 1.00 29.59 ?  146 ASN B C     1 
ATOM   6764  O  O     . ASN B 1 146 ? 139.136 146.006 174.094 1.00 38.22 ?  146 ASN B O     1 
ATOM   6765  C  CB    . ASN B 1 146 ? 140.299 148.659 174.812 1.00 27.33 ?  146 ASN B CB    1 
ATOM   6766  C  CG    . ASN B 1 146 ? 141.181 149.376 175.809 1.00 33.18 ?  146 ASN B CG    1 
ATOM   6767  O  OD1   . ASN B 1 146 ? 142.180 148.832 176.276 1.00 41.26 ?  146 ASN B OD1   1 
ATOM   6768  N  ND2   . ASN B 1 146 ? 140.817 150.609 176.140 1.00 34.54 ?  146 ASN B ND2   1 
ATOM   6769  N  N     . GLN B 1 147 ? 140.052 146.549 172.100 1.00 33.55 ?  147 GLN B N     1 
ATOM   6770  C  CA    . GLN B 1 147 ? 139.181 145.706 171.286 1.00 24.10 ?  147 GLN B CA    1 
ATOM   6771  C  C     . GLN B 1 147 ? 137.716 146.079 171.475 1.00 23.97 ?  147 GLN B C     1 
ATOM   6772  O  O     . GLN B 1 147 ? 136.837 145.219 171.496 1.00 38.00 ?  147 GLN B O     1 
ATOM   6773  C  CB    . GLN B 1 147 ? 139.418 144.224 171.581 1.00 23.94 ?  147 GLN B CB    1 
ATOM   6774  C  CG    . GLN B 1 147 ? 140.774 143.728 171.118 1.00 24.48 ?  147 GLN B CG    1 
ATOM   6775  C  CD    . GLN B 1 147 ? 140.840 142.225 171.023 1.00 31.06 ?  147 GLN B CD    1 
ATOM   6776  O  OE1   . GLN B 1 147 ? 140.375 141.514 171.913 1.00 41.78 ?  147 GLN B OE1   1 
ATOM   6777  N  NE2   . GLN B 1 147 ? 141.425 141.726 169.943 1.00 31.16 ?  147 GLN B NE2   1 
ATOM   6778  N  N     . GLU B 1 148 ? 137.453 147.378 171.626 1.00 25.67 ?  148 GLU B N     1 
ATOM   6779  C  CA    . GLU B 1 148 ? 136.079 147.862 171.641 1.00 23.25 ?  148 GLU B CA    1 
ATOM   6780  C  C     . GLU B 1 148 ? 135.532 148.047 170.235 1.00 29.08 ?  148 GLU B C     1 
ATOM   6781  O  O     . GLU B 1 148 ? 134.334 147.851 170.008 1.00 35.96 ?  148 GLU B O     1 
ATOM   6782  C  CB    . GLU B 1 148 ? 135.990 149.183 172.403 1.00 18.14 ?  148 GLU B CB    1 
ATOM   6783  C  CG    . GLU B 1 148 ? 136.369 149.093 173.864 1.00 21.97 ?  148 GLU B CG    1 
ATOM   6784  C  CD    . GLU B 1 148 ? 136.751 150.440 174.438 1.00 35.44 ?  148 GLU B CD    1 
ATOM   6785  O  OE1   . GLU B 1 148 ? 137.885 150.894 174.187 1.00 35.25 ?  148 GLU B OE1   1 
ATOM   6786  O  OE2   . GLU B 1 148 ? 135.916 151.050 175.138 1.00 42.82 -1 148 GLU B OE2   1 
ATOM   6787  N  N     . TYR B 1 149 ? 136.387 148.425 169.289 1.00 26.98 ?  149 TYR B N     1 
ATOM   6788  C  CA    . TYR B 1 149 ? 135.997 148.624 167.902 1.00 19.69 ?  149 TYR B CA    1 
ATOM   6789  C  C     . TYR B 1 149 ? 136.966 147.877 167.003 1.00 24.35 ?  149 TYR B C     1 
ATOM   6790  O  O     . TYR B 1 149 ? 138.184 147.981 167.174 1.00 32.74 ?  149 TYR B O     1 
ATOM   6791  C  CB    . TYR B 1 149 ? 135.982 150.109 167.536 1.00 22.94 ?  149 TYR B CB    1 
ATOM   6792  C  CG    . TYR B 1 149 ? 135.851 150.367 166.055 1.00 24.46 ?  149 TYR B CG    1 
ATOM   6793  C  CD1   . TYR B 1 149 ? 134.716 149.973 165.361 1.00 19.89 ?  149 TYR B CD1   1 
ATOM   6794  C  CD2   . TYR B 1 149 ? 136.865 150.999 165.349 1.00 17.39 ?  149 TYR B CD2   1 
ATOM   6795  C  CE1   . TYR B 1 149 ? 134.593 150.205 164.008 1.00 19.99 ?  149 TYR B CE1   1 
ATOM   6796  C  CE2   . TYR B 1 149 ? 136.750 151.234 163.996 1.00 24.90 ?  149 TYR B CE2   1 
ATOM   6797  C  CZ    . TYR B 1 149 ? 135.611 150.837 163.330 1.00 20.08 ?  149 TYR B CZ    1 
ATOM   6798  O  OH    . TYR B 1 149 ? 135.491 151.067 161.981 1.00 16.11 ?  149 TYR B OH    1 
ATOM   6799  N  N     . GLN B 1 150 ? 136.423 147.127 166.055 1.00 19.57 ?  150 GLN B N     1 
ATOM   6800  C  CA    . GLN B 1 150 ? 137.227 146.400 165.076 1.00 12.37 ?  150 GLN B CA    1 
ATOM   6801  C  C     . GLN B 1 150 ? 136.914 146.914 163.682 1.00 20.86 ?  150 GLN B C     1 
ATOM   6802  O  O     . GLN B 1 150 ? 135.783 146.726 163.196 1.00 32.26 ?  150 GLN B O     1 
ATOM   6803  C  CB    . GLN B 1 150 ? 136.959 144.898 165.165 1.00 19.69 ?  150 GLN B CB    1 
ATOM   6804  C  CG    . GLN B 1 150 ? 137.611 144.062 164.077 1.00 20.88 ?  150 GLN B CG    1 
ATOM   6805  C  CD    . GLN B 1 150 ? 139.112 144.250 164.012 1.00 20.38 ?  150 GLN B CD    1 
ATOM   6806  O  OE1   . GLN B 1 150 ? 139.836 143.880 164.933 1.00 27.08 ?  150 GLN B OE1   1 
ATOM   6807  N  NE2   . GLN B 1 150 ? 139.587 144.821 162.914 1.00 15.99 ?  150 GLN B NE2   1 
ATOM   6808  N  N     . PRO B 1 151 ? 137.853 147.571 163.006 1.00 27.09 ?  151 PRO B N     1 
ATOM   6809  C  CA    . PRO B 1 151 ? 137.644 147.895 161.593 1.00 14.54 ?  151 PRO B CA    1 
ATOM   6810  C  C     . PRO B 1 151 ? 137.493 146.621 160.778 1.00 20.56 ?  151 PRO B C     1 
ATOM   6811  O  O     . PRO B 1 151 ? 138.012 145.562 161.138 1.00 29.40 ?  151 PRO B O     1 
ATOM   6812  C  CB    . PRO B 1 151 ? 138.913 148.664 161.208 1.00 18.53 ?  151 PRO B CB    1 
ATOM   6813  C  CG    . PRO B 1 151 ? 139.494 149.124 162.501 1.00 20.87 ?  151 PRO B CG    1 
ATOM   6814  C  CD    . PRO B 1 151 ? 139.134 148.089 163.512 1.00 17.91 ?  151 PRO B CD    1 
ATOM   6815  N  N     . SER B 1 152 ? 136.756 146.729 159.677 1.00 24.85 ?  152 SER B N     1 
ATOM   6816  C  CA    . SER B 1 152 ? 136.473 145.564 158.855 1.00 18.45 ?  152 SER B CA    1 
ATOM   6817  C  C     . SER B 1 152 ? 137.763 144.944 158.326 1.00 24.70 ?  152 SER B C     1 
ATOM   6818  O  O     . SER B 1 152 ? 138.836 145.551 158.356 1.00 25.54 ?  152 SER B O     1 
ATOM   6819  C  CB    . SER B 1 152 ? 135.560 145.940 157.690 1.00 21.43 ?  152 SER B CB    1 
ATOM   6820  O  OG    . SER B 1 152 ? 136.211 146.826 156.799 1.00 26.76 ?  152 SER B OG    1 
ATOM   6821  N  N     . THR B 1 153 ? 137.643 143.709 157.845 1.00 32.55 ?  153 THR B N     1 
ATOM   6822  C  CA    . THR B 1 153 ? 138.792 143.008 157.280 1.00 20.41 ?  153 THR B CA    1 
ATOM   6823  C  C     . THR B 1 153 ? 139.521 143.810 156.206 1.00 31.50 ?  153 THR B C     1 
ATOM   6824  O  O     . THR B 1 153 ? 140.760 143.871 156.266 1.00 34.82 ?  153 THR B O     1 
ATOM   6825  C  CB    . THR B 1 153 ? 138.343 141.643 156.733 1.00 27.31 ?  153 THR B CB    1 
ATOM   6826  O  OG1   . THR B 1 153 ? 138.043 140.764 157.824 1.00 33.85 ?  153 THR B OG1   1 
ATOM   6827  C  CG2   . THR B 1 153 ? 139.429 141.019 155.875 1.00 30.48 ?  153 THR B CG2   1 
ATOM   6828  N  N     . PRO B 1 154 ? 138.855 144.447 155.234 1.00 33.93 ?  154 PRO B N     1 
ATOM   6829  C  CA    . PRO B 1 154 ? 139.613 145.290 154.290 1.00 21.38 ?  154 PRO B CA    1 
ATOM   6830  C  C     . PRO B 1 154 ? 140.353 146.429 154.967 1.00 22.56 ?  154 PRO B C     1 
ATOM   6831  O  O     . PRO B 1 154 ? 141.548 146.627 154.712 1.00 31.19 ?  154 PRO B O     1 
ATOM   6832  C  CB    . PRO B 1 154 ? 138.525 145.801 153.335 1.00 24.01 ?  154 PRO B CB    1 
ATOM   6833  C  CG    . PRO B 1 154 ? 137.428 144.832 153.461 1.00 22.70 ?  154 PRO B CG    1 
ATOM   6834  C  CD    . PRO B 1 154 ? 137.428 144.394 154.875 1.00 25.54 ?  154 PRO B CD    1 
ATOM   6835  N  N     . THR B 1 155 ? 139.677 147.182 155.835 1.00 25.99 ?  155 THR B N     1 
ATOM   6836  C  CA    . THR B 1 155 ? 140.320 148.311 156.497 1.00 22.14 ?  155 THR B CA    1 
ATOM   6837  C  C     . THR B 1 155 ? 141.448 147.848 157.410 1.00 25.99 ?  155 THR B C     1 
ATOM   6838  O  O     . THR B 1 155 ? 142.566 148.368 157.347 1.00 25.30 ?  155 THR B O     1 
ATOM   6839  C  CB    . THR B 1 155 ? 139.287 149.112 157.290 1.00 23.99 ?  155 THR B CB    1 
ATOM   6840  O  OG1   . THR B 1 155 ? 138.169 149.418 156.450 1.00 26.39 ?  155 THR B OG1   1 
ATOM   6841  C  CG2   . THR B 1 155 ? 139.898 150.401 157.797 1.00 20.80 ?  155 THR B CG2   1 
ATOM   6842  N  N     . PHE B 1 156 ? 141.174 146.862 158.265 1.00 30.04 ?  156 PHE B N     1 
ATOM   6843  C  CA    . PHE B 1 156 ? 142.185 146.396 159.208 1.00 21.34 ?  156 PHE B CA    1 
ATOM   6844  C  C     . PHE B 1 156 ? 143.385 145.799 158.486 1.00 29.13 ?  156 PHE B C     1 
ATOM   6845  O  O     . PHE B 1 156 ? 144.533 146.018 158.886 1.00 32.96 ?  156 PHE B O     1 
ATOM   6846  C  CB    . PHE B 1 156 ? 141.573 145.378 160.170 1.00 26.41 ?  156 PHE B CB    1 
ATOM   6847  C  CG    . PHE B 1 156 ? 142.366 145.181 161.428 1.00 30.29 ?  156 PHE B CG    1 
ATOM   6848  C  CD1   . PHE B 1 156 ? 142.657 146.253 162.252 1.00 28.22 ?  156 PHE B CD1   1 
ATOM   6849  C  CD2   . PHE B 1 156 ? 142.820 143.923 161.786 1.00 23.06 ?  156 PHE B CD2   1 
ATOM   6850  C  CE1   . PHE B 1 156 ? 143.386 146.076 163.409 1.00 30.39 ?  156 PHE B CE1   1 
ATOM   6851  C  CE2   . PHE B 1 156 ? 143.549 143.741 162.943 1.00 25.10 ?  156 PHE B CE2   1 
ATOM   6852  C  CZ    . PHE B 1 156 ? 143.832 144.819 163.754 1.00 30.21 ?  156 PHE B CZ    1 
ATOM   6853  N  N     . LEU B 1 157 ? 143.138 145.039 157.419 1.00 32.80 ?  157 LEU B N     1 
ATOM   6854  C  CA    . LEU B 1 157 ? 144.222 144.368 156.713 1.00 27.12 ?  157 LEU B CA    1 
ATOM   6855  C  C     . LEU B 1 157 ? 145.043 145.342 155.874 1.00 33.90 ?  157 LEU B C     1 
ATOM   6856  O  O     . LEU B 1 157 ? 146.272 145.230 155.814 1.00 41.74 ?  157 LEU B O     1 
ATOM   6857  C  CB    . LEU B 1 157 ? 143.651 143.255 155.837 1.00 32.38 ?  157 LEU B CB    1 
ATOM   6858  C  CG    . LEU B 1 157 ? 144.597 142.590 154.840 1.00 33.14 ?  157 LEU B CG    1 
ATOM   6859  C  CD1   . LEU B 1 157 ? 145.629 141.753 155.567 1.00 33.58 ?  157 LEU B CD1   1 
ATOM   6860  C  CD2   . LEU B 1 157 ? 143.816 141.743 153.852 1.00 30.09 ?  157 LEU B CD2   1 
ATOM   6861  N  N     . ASN B 1 158 ? 144.390 146.306 155.227 1.00 35.49 ?  158 ASN B N     1 
ATOM   6862  C  CA    . ASN B 1 158 ? 145.037 147.070 154.170 1.00 28.83 ?  158 ASN B CA    1 
ATOM   6863  C  C     . ASN B 1 158 ? 145.444 148.481 154.570 1.00 32.73 ?  158 ASN B C     1 
ATOM   6864  O  O     . ASN B 1 158 ? 146.253 149.087 153.859 1.00 39.64 ?  158 ASN B O     1 
ATOM   6865  C  CB    . ASN B 1 158 ? 144.115 147.151 152.946 1.00 33.04 ?  158 ASN B CB    1 
ATOM   6866  C  CG    . ASN B 1 158 ? 143.917 145.808 152.279 1.00 38.50 ?  158 ASN B CG    1 
ATOM   6867  O  OD1   . ASN B 1 158 ? 144.866 145.047 152.096 1.00 39.97 ?  158 ASN B OD1   1 
ATOM   6868  N  ND2   . ASN B 1 158 ? 142.678 145.507 151.914 1.00 36.86 ?  158 ASN B ND2   1 
ATOM   6869  N  N     . ALA B 1 159 ? 144.922 149.021 155.669 1.00 32.24 ?  159 ALA B N     1 
ATOM   6870  C  CA    . ALA B 1 159 ? 145.212 150.407 156.018 1.00 32.52 ?  159 ALA B CA    1 
ATOM   6871  C  C     . ALA B 1 159 ? 146.705 150.610 156.236 1.00 38.45 ?  159 ALA B C     1 
ATOM   6872  O  O     . ALA B 1 159 ? 147.343 149.869 156.988 1.00 44.26 ?  159 ALA B O     1 
ATOM   6873  C  CB    . ALA B 1 159 ? 144.438 150.816 157.269 1.00 33.14 ?  159 ALA B CB    1 
ATOM   6874  N  N     . GLY B 1 160 ? 147.258 151.623 155.576 1.00 43.15 ?  160 GLY B N     1 
ATOM   6875  C  CA    . GLY B 1 160 ? 148.668 151.922 155.702 1.00 38.96 ?  160 GLY B CA    1 
ATOM   6876  C  C     . GLY B 1 160 ? 149.601 150.980 154.982 1.00 41.97 ?  160 GLY B C     1 
ATOM   6877  O  O     . GLY B 1 160 ? 150.775 150.891 155.352 1.00 50.62 ?  160 GLY B O     1 
ATOM   6878  N  N     . ARG B 1 161 ? 149.124 150.270 153.965 1.00 44.25 ?  161 ARG B N     1 
ATOM   6879  C  CA    . ARG B 1 161 ? 149.943 149.342 153.200 1.00 44.56 ?  161 ARG B CA    1 
ATOM   6880  C  C     . ARG B 1 161 ? 150.082 149.829 151.764 1.00 48.02 ?  161 ARG B C     1 
ATOM   6881  O  O     . ARG B 1 161 ? 149.102 150.252 151.145 1.00 49.36 ?  161 ARG B O     1 
ATOM   6882  C  CB    . ARG B 1 161 ? 149.345 147.933 153.216 1.00 41.42 ?  161 ARG B CB    1 
ATOM   6883  C  CG    . ARG B 1 161 ? 149.430 147.242 154.564 1.00 41.80 ?  161 ARG B CG    1 
ATOM   6884  C  CD    . ARG B 1 161 ? 149.378 145.734 154.408 1.00 42.34 ?  161 ARG B CD    1 
ATOM   6885  N  NE    . ARG B 1 161 ? 149.335 145.057 155.697 1.00 44.00 ?  161 ARG B NE    1 
ATOM   6886  C  CZ    . ARG B 1 161 ? 148.996 143.787 155.865 1.00 46.38 ?  161 ARG B CZ    1 
ATOM   6887  N  NH1   . ARG B 1 161 ? 148.674 143.017 154.839 1.00 49.01 1  161 ARG B NH1   1 
ATOM   6888  N  NH2   . ARG B 1 161 ? 148.978 143.277 157.093 1.00 45.53 ?  161 ARG B NH2   1 
ATOM   6889  N  N     . LYS B 1 162 ? 151.309 149.770 151.243 1.00 57.73 ?  162 LYS B N     1 
ATOM   6890  C  CA    . LYS B 1 162 ? 151.561 150.224 149.879 1.00 57.20 ?  162 LYS B CA    1 
ATOM   6891  C  C     . LYS B 1 162 ? 150.906 149.300 148.860 1.00 58.40 ?  162 LYS B C     1 
ATOM   6892  O  O     . LYS B 1 162 ? 150.213 149.760 147.944 1.00 60.39 ?  162 LYS B O     1 
ATOM   6893  C  CB    . LYS B 1 162 ? 153.066 150.320 149.632 1.00 57.41 ?  162 LYS B CB    1 
ATOM   6894  C  CG    . LYS B 1 162 ? 153.450 150.511 148.176 1.00 59.42 ?  162 LYS B CG    1 
ATOM   6895  C  CD    . LYS B 1 162 ? 153.393 151.975 147.780 1.00 58.54 ?  162 LYS B CD    1 
ATOM   6896  C  CE    . LYS B 1 162 ? 154.453 152.782 148.510 1.00 57.34 ?  162 LYS B CE    1 
ATOM   6897  N  NZ    . LYS B 1 162 ? 154.139 154.237 148.513 1.00 58.40 1  162 LYS B NZ    1 
ATOM   6898  N  N     . ARG B 1 163 ? 151.112 147.992 149.002 1.00 57.99 ?  163 ARG B N     1 
ATOM   6899  C  CA    . ARG B 1 163 ? 150.513 147.009 148.100 1.00 60.65 ?  163 ARG B CA    1 
ATOM   6900  C  C     . ARG B 1 163 ? 149.213 146.469 148.698 1.00 62.84 ?  163 ARG B C     1 
ATOM   6901  O  O     . ARG B 1 163 ? 149.093 145.303 149.073 1.00 61.14 ?  163 ARG B O     1 
ATOM   6902  C  CB    . ARG B 1 163 ? 151.500 145.886 147.806 1.00 61.32 ?  163 ARG B CB    1 
ATOM   6903  C  CG    . ARG B 1 163 ? 152.578 146.254 146.802 1.00 62.25 ?  163 ARG B CG    1 
ATOM   6904  C  CD    . ARG B 1 163 ? 153.736 145.276 146.861 1.00 61.92 ?  163 ARG B CD    1 
ATOM   6905  N  NE    . ARG B 1 163 ? 154.622 145.547 147.985 1.00 64.82 ?  163 ARG B NE    1 
ATOM   6906  C  CZ    . ARG B 1 163 ? 155.373 144.633 148.582 1.00 66.36 ?  163 ARG B CZ    1 
ATOM   6907  N  NH1   . ARG B 1 163 ? 155.369 143.370 148.189 1.00 63.10 1  163 ARG B NH1   1 
ATOM   6908  N  NH2   . ARG B 1 163 ? 156.149 144.995 149.601 1.00 62.68 ?  163 ARG B NH2   1 
ATOM   6909  N  N     . ARG B 1 164 ? 148.229 147.356 148.778 1.00 56.69 ?  164 ARG B N     1 
ATOM   6910  C  CA    . ARG B 1 164 ? 146.962 147.070 149.429 1.00 53.92 ?  164 ARG B CA    1 
ATOM   6911  C  C     . ARG B 1 164 ? 145.827 147.062 148.416 1.00 53.28 ?  164 ARG B C     1 
ATOM   6912  O  O     . ARG B 1 164 ? 145.899 147.705 147.366 1.00 52.80 ?  164 ARG B O     1 
ATOM   6913  C  CB    . ARG B 1 164 ? 146.661 148.103 150.520 1.00 52.22 ?  164 ARG B CB    1 
ATOM   6914  C  CG    . ARG B 1 164 ? 146.181 149.446 149.983 1.00 51.00 ?  164 ARG B CG    1 
ATOM   6915  C  CD    . ARG B 1 164 ? 145.681 150.348 151.099 1.00 53.16 ?  164 ARG B CD    1 
ATOM   6916  N  NE    . ARG B 1 164 ? 145.424 151.710 150.650 1.00 53.94 ?  164 ARG B NE    1 
ATOM   6917  C  CZ    . ARG B 1 164 ? 144.344 152.087 149.976 1.00 56.41 ?  164 ARG B CZ    1 
ATOM   6918  N  NH1   . ARG B 1 164 ? 143.396 151.224 149.651 1.00 51.21 1  164 ARG B NH1   1 
ATOM   6919  N  NH2   . ARG B 1 164 ? 144.215 153.361 149.621 1.00 56.21 ?  164 ARG B NH2   1 
ATOM   6920  N  N     . GLY B 1 165 ? 144.779 146.308 148.739 1.00 50.68 ?  165 GLY B N     1 
ATOM   6921  C  CA    . GLY B 1 165 ? 143.520 146.435 148.047 1.00 47.35 ?  165 GLY B CA    1 
ATOM   6922  C  C     . GLY B 1 165 ? 142.730 147.612 148.578 1.00 51.38 ?  165 GLY B C     1 
ATOM   6923  O  O     . GLY B 1 165 ? 143.184 148.379 149.426 1.00 52.32 ?  165 GLY B O     1 
ATOM   6924  N  N     . GLU B 1 166 ? 141.516 147.756 148.062 1.00 48.09 ?  166 GLU B N     1 
ATOM   6925  C  CA    . GLU B 1 166 ? 140.647 148.823 148.531 1.00 42.72 ?  166 GLU B CA    1 
ATOM   6926  C  C     . GLU B 1 166 ? 140.205 148.556 149.966 1.00 42.86 ?  166 GLU B C     1 
ATOM   6927  O  O     . GLU B 1 166 ? 140.130 147.410 150.415 1.00 39.32 ?  166 GLU B O     1 
ATOM   6928  C  CB    . GLU B 1 166 ? 139.429 148.963 147.618 1.00 41.35 ?  166 GLU B CB    1 
ATOM   6929  C  CG    . GLU B 1 166 ? 139.039 150.403 147.322 1.00 45.08 ?  166 GLU B CG    1 
ATOM   6930  C  CD    . GLU B 1 166 ? 140.107 151.157 146.550 1.00 49.94 ?  166 GLU B CD    1 
ATOM   6931  O  OE1   . GLU B 1 166 ? 140.900 150.510 145.835 1.00 49.58 ?  166 GLU B OE1   1 
ATOM   6932  O  OE2   . GLU B 1 166 ? 140.156 152.400 146.661 1.00 48.28 -1 166 GLU B OE2   1 
ATOM   6933  N  N     . LEU B 1 167 ? 139.918 149.636 150.691 1.00 38.04 ?  167 LEU B N     1 
ATOM   6934  C  CA    . LEU B 1 167 ? 139.415 149.519 152.053 1.00 32.21 ?  167 LEU B CA    1 
ATOM   6935  C  C     . LEU B 1 167 ? 137.930 149.191 152.101 1.00 35.31 ?  167 LEU B C     1 
ATOM   6936  O  O     . LEU B 1 167 ? 137.406 148.916 153.184 1.00 38.65 ?  167 LEU B O     1 
ATOM   6937  C  CB    . LEU B 1 167 ? 139.686 150.812 152.826 1.00 33.90 ?  167 LEU B CB    1 
ATOM   6938  C  CG    . LEU B 1 167 ? 140.928 150.854 153.719 1.00 34.71 ?  167 LEU B CG    1 
ATOM   6939  C  CD1   . LEU B 1 167 ? 142.127 150.226 153.032 1.00 31.87 ?  167 LEU B CD1   1 
ATOM   6940  C  CD2   . LEU B 1 167 ? 141.236 152.281 154.120 1.00 32.27 ?  167 LEU B CD2   1 
ATOM   6941  N  N     . VAL B 1 168 ? 137.249 149.214 150.959 1.00 36.93 ?  168 VAL B N     1 
ATOM   6942  C  CA    . VAL B 1 168 ? 135.846 148.840 150.849 1.00 28.61 ?  168 VAL B CA    1 
ATOM   6943  C  C     . VAL B 1 168 ? 135.768 147.535 150.071 1.00 33.31 ?  168 VAL B C     1 
ATOM   6944  O  O     . VAL B 1 168 ? 136.477 147.355 149.076 1.00 39.76 ?  168 VAL B O     1 
ATOM   6945  C  CB    . VAL B 1 168 ? 135.021 149.945 150.158 1.00 27.73 ?  168 VAL B CB    1 
ATOM   6946  C  CG1   . VAL B 1 168 ? 133.549 149.568 150.107 1.00 34.50 ?  168 VAL B CG1   1 
ATOM   6947  C  CG2   . VAL B 1 168 ? 135.211 151.270 150.869 1.00 31.65 ?  168 VAL B CG2   1 
ATOM   6948  N  N     . SER B 1 169 ? 134.916 146.618 150.532 1.00 29.47 ?  169 SER B N     1 
ATOM   6949  C  CA    . SER B 1 169 ? 134.754 145.337 149.865 1.00 29.73 ?  169 SER B CA    1 
ATOM   6950  C  C     . SER B 1 169 ? 133.317 145.006 149.492 1.00 31.28 ?  169 SER B C     1 
ATOM   6951  O  O     . SER B 1 169 ? 133.082 143.949 148.900 1.00 40.22 ?  169 SER B O     1 
ATOM   6952  C  CB    . SER B 1 169 ? 135.317 144.200 150.731 1.00 36.48 ?  169 SER B CB    1 
ATOM   6953  O  OG    . SER B 1 169 ? 136.704 144.029 150.499 1.00 43.76 ?  169 SER B OG    1 
ATOM   6954  N  N     . CYS B 1 170 ? 132.353 145.860 149.820 1.00 25.02 ?  170 CYS B N     1 
ATOM   6955  C  CA    . CYS B 1 170 ? 130.966 145.650 149.429 1.00 23.57 ?  170 CYS B CA    1 
ATOM   6956  C  C     . CYS B 1 170 ? 130.559 146.755 148.468 1.00 23.82 ?  170 CYS B C     1 
ATOM   6957  O  O     . CYS B 1 170 ? 130.662 147.940 148.798 1.00 31.72 ?  170 CYS B O     1 
ATOM   6958  C  CB    . CYS B 1 170 ? 130.038 145.608 150.647 1.00 34.88 ?  170 CYS B CB    1 
ATOM   6959  S  SG    . CYS B 1 170 ? 130.128 147.031 151.755 1.00 46.19 ?  170 CYS B SG    1 
ATOM   6960  N  N     . PHE B 1 171 ? 130.112 146.364 147.278 1.00 25.86 ?  171 PHE B N     1 
ATOM   6961  C  CA    . PHE B 1 171 ? 129.652 147.293 146.259 1.00 11.61 ?  171 PHE B CA    1 
ATOM   6962  C  C     . PHE B 1 171 ? 128.318 146.813 145.717 1.00 16.26 ?  171 PHE B C     1 
ATOM   6963  O  O     . PHE B 1 171 ? 128.082 145.607 145.605 1.00 24.49 ?  171 PHE B O     1 
ATOM   6964  C  CB    . PHE B 1 171 ? 130.670 147.428 145.121 1.00 17.72 ?  171 PHE B CB    1 
ATOM   6965  C  CG    . PHE B 1 171 ? 132.056 147.745 145.590 1.00 17.83 ?  171 PHE B CG    1 
ATOM   6966  C  CD1   . PHE B 1 171 ? 132.412 149.043 145.902 1.00 19.98 ?  171 PHE B CD1   1 
ATOM   6967  C  CD2   . PHE B 1 171 ? 133.003 146.746 145.719 1.00 19.73 ?  171 PHE B CD2   1 
ATOM   6968  C  CE1   . PHE B 1 171 ? 133.683 149.338 146.339 1.00 13.29 ?  171 PHE B CE1   1 
ATOM   6969  C  CE2   . PHE B 1 171 ? 134.275 147.038 146.155 1.00 17.80 ?  171 PHE B CE2   1 
ATOM   6970  C  CZ    . PHE B 1 171 ? 134.616 148.336 146.463 1.00 10.83 ?  171 PHE B CZ    1 
ATOM   6971  N  N     . LEU B 1 172 ? 127.447 147.762 145.390 1.00 14.93 ?  172 LEU B N     1 
ATOM   6972  C  CA    . LEU B 1 172 ? 126.117 147.468 144.871 1.00 7.54  ?  172 LEU B CA    1 
ATOM   6973  C  C     . LEU B 1 172 ? 125.923 148.261 143.591 1.00 13.54 ?  172 LEU B C     1 
ATOM   6974  O  O     . LEU B 1 172 ? 125.915 149.495 143.621 1.00 21.70 ?  172 LEU B O     1 
ATOM   6975  C  CB    . LEU B 1 172 ? 125.029 147.819 145.889 1.00 8.45  ?  172 LEU B CB    1 
ATOM   6976  C  CG    . LEU B 1 172 ? 124.926 147.005 147.176 1.00 2.85  ?  172 LEU B CG    1 
ATOM   6977  C  CD1   . LEU B 1 172 ? 125.964 147.445 148.193 1.00 11.18 ?  172 LEU B CD1   1 
ATOM   6978  C  CD2   . LEU B 1 172 ? 123.535 147.149 147.748 1.00 16.09 ?  172 LEU B CD2   1 
ATOM   6979  N  N     . LEU B 1 173 ? 125.753 147.558 142.477 1.00 20.16 ?  173 LEU B N     1 
ATOM   6980  C  CA    . LEU B 1 173 ? 125.634 148.177 141.167 1.00 8.80  ?  173 LEU B CA    1 
ATOM   6981  C  C     . LEU B 1 173 ? 124.226 148.004 140.620 1.00 18.02 ?  173 LEU B C     1 
ATOM   6982  O  O     . LEU B 1 173 ? 123.644 146.919 140.702 1.00 29.94 ?  173 LEU B O     1 
ATOM   6983  C  CB    . LEU B 1 173 ? 126.636 147.575 140.181 1.00 13.72 ?  173 LEU B CB    1 
ATOM   6984  C  CG    . LEU B 1 173 ? 128.095 147.459 140.615 1.00 19.57 ?  173 LEU B CG    1 
ATOM   6985  C  CD1   . LEU B 1 173 ? 128.921 146.938 139.456 1.00 22.40 ?  173 LEU B CD1   1 
ATOM   6986  C  CD2   . LEU B 1 173 ? 128.625 148.794 141.099 1.00 25.38 ?  173 LEU B CD2   1 
ATOM   6987  N  N     . GLU B 1 174 ? 123.683 149.083 140.069 1.00 26.42 ?  174 GLU B N     1 
ATOM   6988  C  CA    . GLU B 1 174 ? 122.465 149.017 139.278 1.00 22.09 ?  174 GLU B CA    1 
ATOM   6989  C  C     . GLU B 1 174 ? 122.830 148.772 137.822 1.00 20.40 ?  174 GLU B C     1 
ATOM   6990  O  O     . GLU B 1 174 ? 123.748 149.400 137.288 1.00 31.33 ?  174 GLU B O     1 
ATOM   6991  C  CB    . GLU B 1 174 ? 121.665 150.314 139.401 1.00 26.22 ?  174 GLU B CB    1 
ATOM   6992  C  CG    . GLU B 1 174 ? 121.092 150.583 140.774 1.00 22.93 ?  174 GLU B CG    1 
ATOM   6993  C  CD    . GLU B 1 174 ? 119.600 150.345 140.832 1.00 27.60 ?  174 GLU B CD    1 
ATOM   6994  O  OE1   . GLU B 1 174 ? 119.037 149.856 139.831 1.00 31.09 ?  174 GLU B OE1   1 
ATOM   6995  O  OE2   . GLU B 1 174 ? 118.988 150.651 141.874 1.00 26.84 -1 174 GLU B OE2   1 
ATOM   6996  N  N     . VAL B 1 175 ? 122.111 147.856 137.182 1.00 17.81 ?  175 VAL B N     1 
ATOM   6997  C  CA    . VAL B 1 175 ? 122.333 147.521 135.781 1.00 17.01 ?  175 VAL B CA    1 
ATOM   6998  C  C     . VAL B 1 175 ? 121.118 147.982 134.991 1.00 21.62 ?  175 VAL B C     1 
ATOM   6999  O  O     . VAL B 1 175 ? 119.990 147.556 135.269 1.00 24.85 ?  175 VAL B O     1 
ATOM   7000  C  CB    . VAL B 1 175 ? 122.584 146.017 135.587 1.00 18.44 ?  175 VAL B CB    1 
ATOM   7001  C  CG1   . VAL B 1 175 ? 123.090 145.742 134.181 1.00 7.81  ?  175 VAL B CG1   1 
ATOM   7002  C  CG2   . VAL B 1 175 ? 123.569 145.506 136.627 1.00 18.22 ?  175 VAL B CG2   1 
ATOM   7003  N  N     . ASN B 1 176 ? 121.345 148.849 134.013 1.00 17.07 ?  176 ASN B N     1 
ATOM   7004  C  CA    . ASN B 1 176 ? 120.276 149.350 133.164 1.00 18.01 ?  176 ASN B CA    1 
ATOM   7005  C  C     . ASN B 1 176 ? 120.014 148.390 132.009 1.00 22.69 ?  176 ASN B C     1 
ATOM   7006  O  O     . ASN B 1 176 ? 120.863 147.576 131.637 1.00 27.73 ?  176 ASN B O     1 
ATOM   7007  C  CB    . ASN B 1 176 ? 120.619 150.739 132.630 1.00 19.42 ?  176 ASN B CB    1 
ATOM   7008  C  CG    . ASN B 1 176 ? 119.421 151.656 132.576 1.00 17.10 ?  176 ASN B CG    1 
ATOM   7009  O  OD1   . ASN B 1 176 ? 118.279 151.204 132.559 1.00 26.13 ?  176 ASN B OD1   1 
ATOM   7010  N  ND2   . ASN B 1 176 ? 119.676 152.956 132.550 1.00 18.44 ?  176 ASN B ND2   1 
ATOM   7011  N  N     . ASP B 1 177 ? 118.817 148.500 131.436 1.00 27.31 ?  177 ASP B N     1 
ATOM   7012  C  CA    . ASP B 1 177 ? 118.359 147.585 130.392 1.00 23.71 ?  177 ASP B CA    1 
ATOM   7013  C  C     . ASP B 1 177 ? 118.911 148.045 129.045 1.00 24.80 ?  177 ASP B C     1 
ATOM   7014  O  O     . ASP B 1 177 ? 118.224 148.660 128.226 1.00 31.45 ?  177 ASP B O     1 
ATOM   7015  C  CB    . ASP B 1 177 ? 116.840 147.510 130.386 1.00 20.34 ?  177 ASP B CB    1 
ATOM   7016  C  CG    . ASP B 1 177 ? 116.319 146.354 129.569 1.00 26.79 ?  177 ASP B CG    1 
ATOM   7017  O  OD1   . ASP B 1 177 ? 116.974 145.291 129.557 1.00 34.35 ?  177 ASP B OD1   1 
ATOM   7018  O  OD2   . ASP B 1 177 ? 115.250 146.506 128.945 1.00 33.24 -1 177 ASP B OD2   1 
ATOM   7019  N  N     . SER B 1 178 ? 120.182 147.725 128.815 1.00 19.77 ?  178 SER B N     1 
ATOM   7020  C  CA    . SER B 1 178 ? 120.861 148.065 127.572 1.00 17.17 ?  178 SER B CA    1 
ATOM   7021  C  C     . SER B 1 178 ? 122.159 147.277 127.504 1.00 21.75 ?  178 SER B C     1 
ATOM   7022  O  O     . SER B 1 178 ? 122.729 146.902 128.533 1.00 34.49 ?  178 SER B O     1 
ATOM   7023  C  CB    . SER B 1 178 ? 121.136 149.568 127.470 1.00 14.65 ?  178 SER B CB    1 
ATOM   7024  O  OG    . SER B 1 178 ? 122.381 149.901 128.049 1.00 27.93 ?  178 SER B OG    1 
ATOM   7025  N  N     . LEU B 1 179 ? 122.617 147.022 126.276 1.00 32.35 ?  179 LEU B N     1 
ATOM   7026  C  CA    . LEU B 1 179 ? 123.874 146.305 126.093 1.00 19.98 ?  179 LEU B CA    1 
ATOM   7027  C  C     . LEU B 1 179 ? 125.057 147.138 126.565 1.00 17.04 ?  179 LEU B C     1 
ATOM   7028  O  O     . LEU B 1 179 ? 126.019 146.599 127.123 1.00 26.29 ?  179 LEU B O     1 
ATOM   7029  C  CB    . LEU B 1 179 ? 124.050 145.906 124.629 1.00 23.05 ?  179 LEU B CB    1 
ATOM   7030  C  CG    . LEU B 1 179 ? 125.250 145.005 124.331 1.00 23.10 ?  179 LEU B CG    1 
ATOM   7031  C  CD1   . LEU B 1 179 ? 125.042 143.624 124.932 1.00 20.90 ?  179 LEU B CD1   1 
ATOM   7032  C  CD2   . LEU B 1 179 ? 125.497 144.910 122.837 1.00 21.71 ?  179 LEU B CD2   1 
ATOM   7033  N  N     . ASN B 1 180 ? 125.010 148.453 126.341 1.00 19.32 ?  180 ASN B N     1 
ATOM   7034  C  CA    . ASN B 1 180 ? 126.059 149.333 126.843 1.00 14.81 ?  180 ASN B CA    1 
ATOM   7035  C  C     . ASN B 1 180 ? 126.161 149.243 128.358 1.00 22.05 ?  180 ASN B C     1 
ATOM   7036  O  O     . ASN B 1 180 ? 127.255 149.095 128.917 1.00 30.45 ?  180 ASN B O     1 
ATOM   7037  C  CB    . ASN B 1 180 ? 125.779 150.774 126.413 1.00 23.77 ?  180 ASN B CB    1 
ATOM   7038  C  CG    . ASN B 1 180 ? 126.238 151.065 125.002 1.00 29.53 ?  180 ASN B CG    1 
ATOM   7039  O  OD1   . ASN B 1 180 ? 127.071 150.353 124.448 1.00 34.41 ?  180 ASN B OD1   1 
ATOM   7040  N  ND2   . ASN B 1 180 ? 125.694 152.122 124.411 1.00 27.63 ?  180 ASN B ND2   1 
ATOM   7041  N  N     . ASP B 1 181 ? 125.017 149.305 129.040 1.00 24.53 ?  181 ASP B N     1 
ATOM   7042  C  CA    . ASP B 1 181 ? 125.008 149.251 130.494 1.00 15.71 ?  181 ASP B CA    1 
ATOM   7043  C  C     . ASP B 1 181 ? 125.391 147.870 131.011 1.00 20.15 ?  181 ASP B C     1 
ATOM   7044  O  O     . ASP B 1 181 ? 126.046 147.767 132.048 1.00 30.36 ?  181 ASP B O     1 
ATOM   7045  C  CB    . ASP B 1 181 ? 123.636 149.662 131.018 1.00 27.99 ?  181 ASP B CB    1 
ATOM   7046  C  CG    . ASP B 1 181 ? 123.345 151.133 130.784 1.00 31.71 ?  181 ASP B CG    1 
ATOM   7047  O  OD1   . ASP B 1 181 ? 123.958 151.977 131.468 1.00 32.18 ?  181 ASP B OD1   1 
ATOM   7048  O  OD2   . ASP B 1 181 ? 122.502 151.445 129.918 1.00 26.06 -1 181 ASP B OD2   1 
ATOM   7049  N  N     . ILE B 1 182 ? 125.008 146.805 130.306 1.00 21.62 ?  182 ILE B N     1 
ATOM   7050  C  CA    . ILE B 1 182 ? 125.390 145.461 130.728 1.00 21.44 ?  182 ILE B CA    1 
ATOM   7051  C  C     . ILE B 1 182 ? 126.896 145.259 130.586 1.00 19.32 ?  182 ILE B C     1 
ATOM   7052  O  O     . ILE B 1 182 ? 127.549 144.693 131.473 1.00 22.73 ?  182 ILE B O     1 
ATOM   7053  C  CB    . ILE B 1 182 ? 124.591 144.410 129.935 1.00 19.85 ?  182 ILE B CB    1 
ATOM   7054  C  CG1   . ILE B 1 182 ? 123.166 144.317 130.480 1.00 20.49 ?  182 ILE B CG1   1 
ATOM   7055  C  CG2   . ILE B 1 182 ? 125.270 143.054 129.990 1.00 22.79 ?  182 ILE B CG2   1 
ATOM   7056  C  CD1   . ILE B 1 182 ? 122.211 143.608 129.563 1.00 23.22 ?  182 ILE B CD1   1 
ATOM   7057  N  N     . SER B 1 183 ? 127.471 145.718 129.474 1.00 26.18 ?  183 SER B N     1 
ATOM   7058  C  CA    . SER B 1 183 ? 128.917 145.623 129.298 1.00 16.94 ?  183 SER B CA    1 
ATOM   7059  C  C     . SER B 1 183 ? 129.651 146.454 130.340 1.00 19.44 ?  183 SER B C     1 
ATOM   7060  O  O     . SER B 1 183 ? 130.673 146.018 130.887 1.00 27.79 ?  183 SER B O     1 
ATOM   7061  C  CB    . SER B 1 183 ? 129.302 146.066 127.889 1.00 17.25 ?  183 SER B CB    1 
ATOM   7062  O  OG    . SER B 1 183 ? 128.781 147.348 127.600 1.00 33.98 ?  183 SER B OG    1 
ATOM   7063  N  N     . ARG B 1 184 ? 129.147 147.655 130.632 1.00 25.39 ?  184 ARG B N     1 
ATOM   7064  C  CA    . ARG B 1 184 ? 129.761 148.473 131.670 1.00 17.87 ?  184 ARG B CA    1 
ATOM   7065  C  C     . ARG B 1 184 ? 129.641 147.813 133.037 1.00 26.39 ?  184 ARG B C     1 
ATOM   7066  O  O     . ARG B 1 184 ? 130.556 147.909 133.858 1.00 31.50 ?  184 ARG B O     1 
ATOM   7067  C  CB    . ARG B 1 184 ? 129.131 149.863 131.687 1.00 16.95 ?  184 ARG B CB    1 
ATOM   7068  C  CG    . ARG B 1 184 ? 129.830 150.835 132.617 1.00 27.61 ?  184 ARG B CG    1 
ATOM   7069  C  CD    . ARG B 1 184 ? 131.328 150.830 132.404 1.00 26.09 ?  184 ARG B CD    1 
ATOM   7070  N  NE    . ARG B 1 184 ? 131.727 151.778 131.373 1.00 34.37 ?  184 ARG B NE    1 
ATOM   7071  C  CZ    . ARG B 1 184 ? 132.896 151.758 130.749 1.00 34.93 ?  184 ARG B CZ    1 
ATOM   7072  N  NH1   . ARG B 1 184 ? 133.811 150.842 131.024 1.00 25.59 1  184 ARG B NH1   1 
ATOM   7073  N  NH2   . ARG B 1 184 ? 133.155 152.681 129.827 1.00 32.42 ?  184 ARG B NH2   1 
ATOM   7074  N  N     . ALA B 1 185 ? 128.515 147.150 133.305 1.00 31.15 ?  185 ALA B N     1 
ATOM   7075  C  CA    . ALA B 1 185 ? 128.352 146.435 134.564 1.00 8.29  ?  185 ALA B CA    1 
ATOM   7076  C  C     . ALA B 1 185 ? 129.353 145.299 134.682 1.00 12.71 ?  185 ALA B C     1 
ATOM   7077  O  O     . ALA B 1 185 ? 129.933 145.085 135.750 1.00 22.32 ?  185 ALA B O     1 
ATOM   7078  C  CB    . ALA B 1 185 ? 126.925 145.906 134.688 1.00 9.14  ?  185 ALA B CB    1 
ATOM   7079  N  N     . ILE B 1 186 ? 129.571 144.558 133.594 1.00 22.82 ?  186 ILE B N     1 
ATOM   7080  C  CA    . ILE B 1 186 ? 130.572 143.492 133.611 1.00 23.20 ?  186 ILE B CA    1 
ATOM   7081  C  C     . ILE B 1 186 ? 131.959 144.072 133.861 1.00 17.77 ?  186 ILE B C     1 
ATOM   7082  O  O     . ILE B 1 186 ? 132.737 143.544 134.669 1.00 26.42 ?  186 ILE B O     1 
ATOM   7083  C  CB    . ILE B 1 186 ? 130.519 142.689 132.297 1.00 27.87 ?  186 ILE B CB    1 
ATOM   7084  C  CG1   . ILE B 1 186 ? 129.337 141.720 132.313 1.00 21.95 ?  186 ILE B CG1   1 
ATOM   7085  C  CG2   . ILE B 1 186 ? 131.817 141.930 132.069 1.00 23.79 ?  186 ILE B CG2   1 
ATOM   7086  C  CD1   . ILE B 1 186 ? 128.681 141.550 130.967 1.00 27.46 ?  186 ILE B CD1   1 
ATOM   7087  N  N     . ASP B 1 187 ? 132.283 145.175 133.184 1.00 23.35 ?  187 ASP B N     1 
ATOM   7088  C  CA    . ASP B 1 187 ? 133.583 145.812 133.366 1.00 18.17 ?  187 ASP B CA    1 
ATOM   7089  C  C     . ASP B 1 187 ? 133.779 146.269 134.807 1.00 28.09 ?  187 ASP B C     1 
ATOM   7090  O  O     . ASP B 1 187 ? 134.823 146.011 135.415 1.00 34.35 ?  187 ASP B O     1 
ATOM   7091  C  CB    . ASP B 1 187 ? 133.722 146.992 132.406 1.00 17.20 ?  187 ASP B CB    1 
ATOM   7092  C  CG    . ASP B 1 187 ? 134.800 147.968 132.832 1.00 35.28 ?  187 ASP B CG    1 
ATOM   7093  O  OD1   . ASP B 1 187 ? 135.956 147.539 133.021 1.00 34.32 ?  187 ASP B OD1   1 
ATOM   7094  O  OD2   . ASP B 1 187 ? 134.488 149.168 132.984 1.00 41.83 -1 187 ASP B OD2   1 
ATOM   7095  N  N     . ILE B 1 188 ? 132.779 146.948 135.370 1.00 23.60 ?  188 ILE B N     1 
ATOM   7096  C  CA    . ILE B 1 188 ? 132.895 147.471 136.726 1.00 22.56 ?  188 ILE B CA    1 
ATOM   7097  C  C     . ILE B 1 188 ? 132.943 146.335 137.738 1.00 25.27 ?  188 ILE B C     1 
ATOM   7098  O  O     . ILE B 1 188 ? 133.659 146.411 138.741 1.00 27.77 ?  188 ILE B O     1 
ATOM   7099  C  CB    . ILE B 1 188 ? 131.745 148.451 137.021 1.00 26.73 ?  188 ILE B CB    1 
ATOM   7100  C  CG1   . ILE B 1 188 ? 131.851 149.685 136.129 1.00 25.52 ?  188 ILE B CG1   1 
ATOM   7101  C  CG2   . ILE B 1 188 ? 131.768 148.887 138.468 1.00 26.77 ?  188 ILE B CG2   1 
ATOM   7102  C  CD1   . ILE B 1 188 ? 130.675 150.619 136.261 1.00 21.59 ?  188 ILE B CD1   1 
ATOM   7103  N  N     . SER B 1 189 ? 132.185 145.264 137.496 1.00 19.85 ?  189 SER B N     1 
ATOM   7104  C  CA    . SER B 1 189 ? 132.242 144.104 138.375 1.00 13.40 ?  189 SER B CA    1 
ATOM   7105  C  C     . SER B 1 189 ? 133.632 143.490 138.377 1.00 20.94 ?  189 SER B C     1 
ATOM   7106  O  O     . SER B 1 189 ? 134.160 143.143 139.438 1.00 25.83 ?  189 SER B O     1 
ATOM   7107  C  CB    . SER B 1 189 ? 131.200 143.072 137.948 1.00 20.14 ?  189 SER B CB    1 
ATOM   7108  O  OG    . SER B 1 189 ? 129.904 143.640 137.931 1.00 29.91 ?  189 SER B OG    1 
ATOM   7109  N  N     . MET B 1 190 ? 134.248 143.354 137.199 1.00 30.19 ?  190 MET B N     1 
ATOM   7110  C  CA    . MET B 1 190 ? 135.605 142.819 137.148 1.00 22.37 ?  190 MET B CA    1 
ATOM   7111  C  C     . MET B 1 190 ? 136.600 143.761 137.815 1.00 16.93 ?  190 MET B C     1 
ATOM   7112  O  O     . MET B 1 190 ? 137.523 143.309 138.499 1.00 21.26 ?  190 MET B O     1 
ATOM   7113  C  CB    . MET B 1 190 ? 136.014 142.535 135.704 1.00 21.58 ?  190 MET B CB    1 
ATOM   7114  C  CG    . MET B 1 190 ? 135.216 141.423 135.057 1.00 27.32 ?  190 MET B CG    1 
ATOM   7115  S  SD    . MET B 1 190 ? 136.065 140.636 133.678 1.00 35.79 ?  190 MET B SD    1 
ATOM   7116  C  CE    . MET B 1 190 ? 136.053 141.965 132.481 1.00 25.79 ?  190 MET B CE    1 
ATOM   7117  N  N     . GLN B 1 191 ? 136.428 145.072 137.635 1.00 21.42 ?  191 GLN B N     1 
ATOM   7118  C  CA    . GLN B 1 191 ? 137.343 146.027 138.255 1.00 23.07 ?  191 GLN B CA    1 
ATOM   7119  C  C     . GLN B 1 191 ? 137.233 146.003 139.775 1.00 25.57 ?  191 GLN B C     1 
ATOM   7120  O  O     . GLN B 1 191 ? 138.247 146.106 140.476 1.00 32.40 ?  191 GLN B O     1 
ATOM   7121  C  CB    . GLN B 1 191 ? 137.082 147.437 137.723 1.00 24.32 ?  191 GLN B CB    1 
ATOM   7122  C  CG    . GLN B 1 191 ? 137.324 147.600 136.234 1.00 23.68 ?  191 GLN B CG    1 
ATOM   7123  C  CD    . GLN B 1 191 ? 138.794 147.607 135.870 1.00 27.63 ?  191 GLN B CD    1 
ATOM   7124  O  OE1   . GLN B 1 191 ? 139.665 147.622 136.738 1.00 30.80 ?  191 GLN B OE1   1 
ATOM   7125  N  NE2   . GLN B 1 191 ? 139.078 147.592 134.575 1.00 28.81 ?  191 GLN B NE2   1 
ATOM   7126  N  N     . LEU B 1 192 ? 136.016 145.879 140.303 1.00 24.98 ?  192 LEU B N     1 
ATOM   7127  C  CA    . LEU B 1 192 ? 135.832 145.870 141.749 1.00 16.38 ?  192 LEU B CA    1 
ATOM   7128  C  C     . LEU B 1 192 ? 136.236 144.534 142.359 1.00 23.84 ?  192 LEU B C     1 
ATOM   7129  O  O     . LEU B 1 192 ? 136.791 144.498 143.461 1.00 36.16 ?  192 LEU B O     1 
ATOM   7130  C  CB    . LEU B 1 192 ? 134.382 146.204 142.097 1.00 18.21 ?  192 LEU B CB    1 
ATOM   7131  C  CG    . LEU B 1 192 ? 133.921 147.619 141.744 1.00 19.83 ?  192 LEU B CG    1 
ATOM   7132  C  CD1   . LEU B 1 192 ? 132.415 147.737 141.873 1.00 19.10 ?  192 LEU B CD1   1 
ATOM   7133  C  CD2   . LEU B 1 192 ? 134.621 148.648 142.614 1.00 17.33 ?  192 LEU B CD2   1 
ATOM   7134  N  N     . SER B 1 193 ? 135.964 143.427 141.664 1.00 27.70 ?  193 SER B N     1 
ATOM   7135  C  CA    . SER B 1 193 ? 136.445 142.130 142.122 1.00 20.19 ?  193 SER B CA    1 
ATOM   7136  C  C     . SER B 1 193 ? 137.963 142.061 142.078 1.00 28.24 ?  193 SER B C     1 
ATOM   7137  O  O     . SER B 1 193 ? 138.577 141.381 142.903 1.00 36.87 ?  193 SER B O     1 
ATOM   7138  C  CB    . SER B 1 193 ? 135.830 141.018 141.274 1.00 25.64 ?  193 SER B CB    1 
ATOM   7139  O  OG    . SER B 1 193 ? 136.135 139.743 141.807 1.00 42.27 ?  193 SER B OG    1 
ATOM   7140  N  N     . LYS B 1 194 ? 138.580 142.759 141.123 1.00 34.56 ?  194 LYS B N     1 
ATOM   7141  C  CA    . LYS B 1 194 ? 140.034 142.862 141.090 1.00 32.01 ?  194 LYS B CA    1 
ATOM   7142  C  C     . LYS B 1 194 ? 140.563 143.525 142.355 1.00 35.73 ?  194 LYS B C     1 
ATOM   7143  O  O     . LYS B 1 194 ? 141.581 143.099 142.912 1.00 43.69 ?  194 LYS B O     1 
ATOM   7144  C  CB    . LYS B 1 194 ? 140.464 143.638 139.845 1.00 27.19 ?  194 LYS B CB    1 
ATOM   7145  C  CG    . LYS B 1 194 ? 141.869 144.193 139.898 1.00 36.44 ?  194 LYS B CG    1 
ATOM   7146  C  CD    . LYS B 1 194 ? 142.102 145.201 138.787 1.00 38.23 ?  194 LYS B CD    1 
ATOM   7147  C  CE    . LYS B 1 194 ? 143.587 145.432 138.556 1.00 36.81 ?  194 LYS B CE    1 
ATOM   7148  N  NZ    . LYS B 1 194 ? 143.828 146.423 137.472 1.00 37.91 1  194 LYS B NZ    1 
ATOM   7149  N  N     . LEU B 1 195 ? 139.875 144.564 142.830 1.00 34.15 ?  195 LEU B N     1 
ATOM   7150  C  CA    . LEU B 1 195 ? 140.239 145.216 144.082 1.00 35.73 ?  195 LEU B CA    1 
ATOM   7151  C  C     . LEU B 1 195 ? 139.971 144.345 145.301 1.00 35.64 ?  195 LEU B C     1 
ATOM   7152  O  O     . LEU B 1 195 ? 140.394 144.707 146.403 1.00 42.62 ?  195 LEU B O     1 
ATOM   7153  C  CB    . LEU B 1 195 ? 139.484 146.539 144.222 1.00 38.37 ?  195 LEU B CB    1 
ATOM   7154  C  CG    . LEU B 1 195 ? 139.720 147.564 143.114 1.00 37.71 ?  195 LEU B CG    1 
ATOM   7155  C  CD1   . LEU B 1 195 ? 138.927 148.834 143.381 1.00 32.38 ?  195 LEU B CD1   1 
ATOM   7156  C  CD2   . LEU B 1 195 ? 141.201 147.866 142.970 1.00 34.65 ?  195 LEU B CD2   1 
ATOM   7157  N  N     . GLY B 1 196 ? 139.280 143.223 145.135 1.00 31.06 ?  196 GLY B N     1 
ATOM   7158  C  CA    . GLY B 1 196 ? 138.986 142.329 146.231 1.00 30.00 ?  196 GLY B CA    1 
ATOM   7159  C  C     . GLY B 1 196 ? 137.627 142.502 146.864 1.00 36.77 ?  196 GLY B C     1 
ATOM   7160  O  O     . GLY B 1 196 ? 137.374 141.903 147.915 1.00 39.00 ?  196 GLY B O     1 
ATOM   7161  N  N     . GLY B 1 197 ? 136.745 143.293 146.264 1.00 30.42 ?  197 GLY B N     1 
ATOM   7162  C  CA    . GLY B 1 197 ? 135.447 143.589 146.844 1.00 25.49 ?  197 GLY B CA    1 
ATOM   7163  C  C     . GLY B 1 197 ? 134.340 142.730 146.256 1.00 27.37 ?  197 GLY B C     1 
ATOM   7164  O  O     . GLY B 1 197 ? 134.342 142.424 145.064 1.00 31.59 ?  197 GLY B O     1 
ATOM   7165  N  N     . GLY B 1 198 ? 133.398 142.347 147.113 1.00 25.08 ?  198 GLY B N     1 
ATOM   7166  C  CA    . GLY B 1 198 ? 132.206 141.672 146.637 1.00 14.95 ?  198 GLY B CA    1 
ATOM   7167  C  C     . GLY B 1 198 ? 131.264 142.655 145.964 1.00 14.13 ?  198 GLY B C     1 
ATOM   7168  O  O     . GLY B 1 198 ? 131.056 143.772 146.435 1.00 24.21 ?  198 GLY B O     1 
ATOM   7169  N  N     . VAL B 1 199 ? 130.693 142.230 144.842 1.00 22.61 ?  199 VAL B N     1 
ATOM   7170  C  CA    . VAL B 1 199 ? 129.882 143.093 143.993 1.00 17.88 ?  199 VAL B CA    1 
ATOM   7171  C  C     . VAL B 1 199 ? 128.475 142.522 143.918 1.00 8.99  ?  199 VAL B C     1 
ATOM   7172  O  O     . VAL B 1 199 ? 128.295 141.337 143.617 1.00 18.81 ?  199 VAL B O     1 
ATOM   7173  C  CB    . VAL B 1 199 ? 130.488 143.234 142.585 1.00 12.95 ?  199 VAL B CB    1 
ATOM   7174  C  CG1   . VAL B 1 199 ? 129.737 144.282 141.788 1.00 18.72 ?  199 VAL B CG1   1 
ATOM   7175  C  CG2   . VAL B 1 199 ? 131.962 143.579 142.677 1.00 17.15 ?  199 VAL B CG2   1 
ATOM   7176  N  N     . SER B 1 200 ? 127.485 143.361 144.195 1.00 18.60 ?  200 SER B N     1 
ATOM   7177  C  CA    . SER B 1 200 ? 126.081 142.998 144.078 1.00 7.07  ?  200 SER B CA    1 
ATOM   7178  C  C     . SER B 1 200 ? 125.471 143.767 142.917 1.00 13.22 ?  200 SER B C     1 
ATOM   7179  O  O     . SER B 1 200 ? 125.678 144.978 142.793 1.00 22.94 ?  200 SER B O     1 
ATOM   7180  C  CB    . SER B 1 200 ? 125.326 143.296 145.371 1.00 13.11 ?  200 SER B CB    1 
ATOM   7181  O  OG    . SER B 1 200 ? 124.138 142.529 145.449 1.00 22.00 ?  200 SER B OG    1 
ATOM   7182  N  N     . LEU B 1 201 ? 124.728 143.065 142.069 1.00 20.67 ?  201 LEU B N     1 
ATOM   7183  C  CA    . LEU B 1 201 ? 124.149 143.647 140.868 1.00 7.80  ?  201 LEU B CA    1 
ATOM   7184  C  C     . LEU B 1 201 ? 122.636 143.506 140.908 1.00 10.12 ?  201 LEU B C     1 
ATOM   7185  O  O     . LEU B 1 201 ? 122.116 142.429 141.218 1.00 14.11 ?  201 LEU B O     1 
ATOM   7186  C  CB    . LEU B 1 201 ? 124.716 142.981 139.614 1.00 20.30 ?  201 LEU B CB    1 
ATOM   7187  C  CG    . LEU B 1 201 ? 126.231 143.116 139.460 1.00 18.96 ?  201 LEU B CG    1 
ATOM   7188  C  CD1   . LEU B 1 201 ? 126.921 141.788 139.723 1.00 22.23 ?  201 LEU B CD1   1 
ATOM   7189  C  CD2   . LEU B 1 201 ? 126.583 143.645 138.083 1.00 16.03 ?  201 LEU B CD2   1 
ATOM   7190  N  N     . ASN B 1 202 ? 121.938 144.597 140.608 1.00 15.66 ?  202 ASN B N     1 
ATOM   7191  C  CA    . ASN B 1 202 ? 120.485 144.592 140.497 1.00 7.09  ?  202 ASN B CA    1 
ATOM   7192  C  C     . ASN B 1 202 ? 120.119 144.280 139.052 1.00 22.09 ?  202 ASN B C     1 
ATOM   7193  O  O     . ASN B 1 202 ? 120.412 145.066 138.146 1.00 34.99 ?  202 ASN B O     1 
ATOM   7194  C  CB    . ASN B 1 202 ? 119.907 145.934 140.935 1.00 9.23  ?  202 ASN B CB    1 
ATOM   7195  C  CG    . ASN B 1 202 ? 118.430 145.857 141.247 1.00 13.69 ?  202 ASN B CG    1 
ATOM   7196  O  OD1   . ASN B 1 202 ? 117.900 144.789 141.549 1.00 23.02 ?  202 ASN B OD1   1 
ATOM   7197  N  ND2   . ASN B 1 202 ? 117.753 146.995 141.177 1.00 13.77 ?  202 ASN B ND2   1 
ATOM   7198  N  N     . LEU B 1 203 ? 119.479 143.135 138.835 1.00 13.13 ?  203 LEU B N     1 
ATOM   7199  C  CA    . LEU B 1 203 ? 119.099 142.693 137.503 1.00 10.38 ?  203 LEU B CA    1 
ATOM   7200  C  C     . LEU B 1 203 ? 117.621 142.910 137.210 1.00 11.78 ?  203 LEU B C     1 
ATOM   7201  O  O     . LEU B 1 203 ? 117.120 142.407 136.201 1.00 20.55 ?  203 LEU B O     1 
ATOM   7202  C  CB    . LEU B 1 203 ? 119.458 141.216 137.320 1.00 19.25 ?  203 LEU B CB    1 
ATOM   7203  C  CG    . LEU B 1 203 ? 120.928 140.832 137.499 1.00 19.16 ?  203 LEU B CG    1 
ATOM   7204  C  CD1   . LEU B 1 203 ? 121.197 139.468 136.894 1.00 15.97 ?  203 LEU B CD1   1 
ATOM   7205  C  CD2   . LEU B 1 203 ? 121.848 141.878 136.890 1.00 18.43 ?  203 LEU B CD2   1 
ATOM   7206  N  N     . SER B 1 204 ? 116.914 143.651 138.066 1.00 16.09 ?  204 SER B N     1 
ATOM   7207  C  CA    . SER B 1 204 ? 115.470 143.789 137.910 1.00 17.71 ?  204 SER B CA    1 
ATOM   7208  C  C     . SER B 1 204 ? 115.103 144.687 136.735 1.00 20.50 ?  204 SER B C     1 
ATOM   7209  O  O     . SER B 1 204 ? 114.023 144.535 136.158 1.00 27.93 ?  204 SER B O     1 
ATOM   7210  C  CB    . SER B 1 204 ? 114.855 144.328 139.199 1.00 12.46 ?  204 SER B CB    1 
ATOM   7211  O  OG    . SER B 1 204 ? 115.061 143.424 140.267 1.00 24.39 ?  204 SER B OG    1 
ATOM   7212  N  N     . LYS B 1 205 ? 115.974 145.628 136.374 1.00 17.96 ?  205 LYS B N     1 
ATOM   7213  C  CA    . LYS B 1 205 ? 115.697 146.502 135.242 1.00 16.97 ?  205 LYS B CA    1 
ATOM   7214  C  C     . LYS B 1 205 ? 115.885 145.806 133.903 1.00 21.08 ?  205 LYS B C     1 
ATOM   7215  O  O     . LYS B 1 205 ? 115.275 146.224 132.915 1.00 30.01 ?  205 LYS B O     1 
ATOM   7216  C  CB    . LYS B 1 205 ? 116.578 147.747 135.303 1.00 17.17 ?  205 LYS B CB    1 
ATOM   7217  C  CG    . LYS B 1 205 ? 116.222 148.684 136.431 1.00 13.29 ?  205 LYS B CG    1 
ATOM   7218  C  CD    . LYS B 1 205 ? 117.071 149.933 136.390 1.00 19.85 ?  205 LYS B CD    1 
ATOM   7219  C  CE    . LYS B 1 205 ? 116.558 150.970 137.365 1.00 24.37 ?  205 LYS B CE    1 
ATOM   7220  N  NZ    . LYS B 1 205 ? 116.708 150.535 138.777 1.00 17.22 1  205 LYS B NZ    1 
ATOM   7221  N  N     . LEU B 1 206 ? 116.713 144.766 133.849 1.00 17.26 ?  206 LEU B N     1 
ATOM   7222  C  CA    . LEU B 1 206 ? 116.906 144.025 132.613 1.00 11.29 ?  206 LEU B CA    1 
ATOM   7223  C  C     . LEU B 1 206 ? 115.605 143.361 132.185 1.00 19.76 ?  206 LEU B C     1 
ATOM   7224  O  O     . LEU B 1 206 ? 114.919 142.732 132.995 1.00 25.80 ?  206 LEU B O     1 
ATOM   7225  C  CB    . LEU B 1 206 ? 117.997 142.973 132.794 1.00 19.80 ?  206 LEU B CB    1 
ATOM   7226  C  CG    . LEU B 1 206 ? 119.335 143.480 133.324 1.00 22.20 ?  206 LEU B CG    1 
ATOM   7227  C  CD1   . LEU B 1 206 ? 120.277 142.318 133.555 1.00 17.52 ?  206 LEU B CD1   1 
ATOM   7228  C  CD2   . LEU B 1 206 ? 119.938 144.482 132.362 1.00 26.19 ?  206 LEU B CD2   1 
ATOM   7229  N  N     . ARG B 1 207 ? 115.270 143.499 130.906 1.00 26.99 ?  207 ARG B N     1 
ATOM   7230  C  CA    . ARG B 1 207 ? 114.040 142.913 130.402 1.00 22.95 ?  207 ARG B CA    1 
ATOM   7231  C  C     . ARG B 1 207 ? 114.151 141.393 130.354 1.00 26.41 ?  207 ARG B C     1 
ATOM   7232  O  O     . ARG B 1 207 ? 115.237 140.826 130.202 1.00 30.49 ?  207 ARG B O     1 
ATOM   7233  C  CB    . ARG B 1 207 ? 113.698 143.473 129.021 1.00 23.26 ?  207 ARG B CB    1 
ATOM   7234  C  CG    . ARG B 1 207 ? 114.703 143.177 127.929 1.00 24.90 ?  207 ARG B CG    1 
ATOM   7235  C  CD    . ARG B 1 207 ? 114.377 143.982 126.683 1.00 22.50 ?  207 ARG B CD    1 
ATOM   7236  N  NE    . ARG B 1 207 ? 114.757 145.380 126.830 1.00 27.64 ?  207 ARG B NE    1 
ATOM   7237  C  CZ    . ARG B 1 207 ? 114.965 146.214 125.820 1.00 21.97 ?  207 ARG B CZ    1 
ATOM   7238  N  NH1   . ARG B 1 207 ? 114.803 145.832 124.565 1.00 28.60 1  207 ARG B NH1   1 
ATOM   7239  N  NH2   . ARG B 1 207 ? 115.349 147.460 126.076 1.00 18.36 ?  207 ARG B NH2   1 
ATOM   7240  N  N     . ALA B 1 208 ? 113.005 140.735 130.494 1.00 30.71 ?  208 ALA B N     1 
ATOM   7241  C  CA    . ALA B 1 208 ? 112.964 139.295 130.660 1.00 29.17 ?  208 ALA B CA    1 
ATOM   7242  C  C     . ALA B 1 208 ? 113.301 138.576 129.355 1.00 33.52 ?  208 ALA B C     1 
ATOM   7243  O  O     . ALA B 1 208 ? 113.501 139.186 128.301 1.00 35.30 ?  208 ALA B O     1 
ATOM   7244  C  CB    . ALA B 1 208 ? 111.589 138.858 131.156 1.00 26.41 ?  208 ALA B CB    1 
ATOM   7245  N  N     . LYS B 1 209 ? 113.369 137.252 129.448 1.00 26.37 ?  209 LYS B N     1 
ATOM   7246  C  CA    . LYS B 1 209 ? 113.607 136.420 128.280 1.00 22.11 ?  209 LYS B CA    1 
ATOM   7247  C  C     . LYS B 1 209 ? 112.406 136.464 127.344 1.00 33.53 ?  209 LYS B C     1 
ATOM   7248  O  O     . LYS B 1 209 ? 111.254 136.448 127.784 1.00 35.56 ?  209 LYS B O     1 
ATOM   7249  C  CB    . LYS B 1 209 ? 113.892 134.981 128.706 1.00 27.44 ?  209 LYS B CB    1 
ATOM   7250  C  CG    . LYS B 1 209 ? 114.695 134.174 127.702 1.00 33.01 ?  209 LYS B CG    1 
ATOM   7251  C  CD    . LYS B 1 209 ? 114.139 132.767 127.548 1.00 31.98 ?  209 LYS B CD    1 
ATOM   7252  C  CE    . LYS B 1 209 ? 113.594 132.236 128.863 1.00 36.48 ?  209 LYS B CE    1 
ATOM   7253  N  NZ    . LYS B 1 209 ? 112.891 130.935 128.692 1.00 35.63 1  209 LYS B NZ    1 
ATOM   7254  N  N     . GLY B 1 210 ? 112.683 136.510 126.044 1.00 36.34 ?  210 GLY B N     1 
ATOM   7255  C  CA    . GLY B 1 210 ? 111.620 136.608 125.067 1.00 32.08 ?  210 GLY B CA    1 
ATOM   7256  C  C     . GLY B 1 210 ? 111.018 137.986 124.924 1.00 36.40 ?  210 GLY B C     1 
ATOM   7257  O  O     . GLY B 1 210 ? 109.821 138.104 124.645 1.00 38.93 ?  210 GLY B O     1 
ATOM   7258  N  N     . GLU B 1 211 ? 111.807 139.034 125.121 1.00 39.33 ?  211 GLU B N     1 
ATOM   7259  C  CA    . GLU B 1 211 ? 111.366 140.404 124.916 1.00 33.16 ?  211 GLU B CA    1 
ATOM   7260  C  C     . GLU B 1 211 ? 111.971 140.958 123.633 1.00 36.67 ?  211 GLU B C     1 
ATOM   7261  O  O     . GLU B 1 211 ? 112.941 140.426 123.089 1.00 39.90 ?  211 GLU B O     1 
ATOM   7262  C  CB    . GLU B 1 211 ? 111.738 141.285 126.113 1.00 34.62 ?  211 GLU B CB    1 
ATOM   7263  C  CG    . GLU B 1 211 ? 110.894 141.026 127.345 1.00 35.76 ?  211 GLU B CG    1 
ATOM   7264  C  CD    . GLU B 1 211 ? 110.324 142.296 127.938 1.00 41.33 ?  211 GLU B CD    1 
ATOM   7265  O  OE1   . GLU B 1 211 ? 109.545 142.979 127.242 1.00 43.31 ?  211 GLU B OE1   1 
ATOM   7266  O  OE2   . GLU B 1 211 ? 110.642 142.608 129.103 1.00 41.92 -1 211 GLU B OE2   1 
ATOM   7267  N  N     . ALA B 1 212 ? 111.377 142.043 123.150 1.00 37.07 ?  212 ALA B N     1 
ATOM   7268  C  CA    . ALA B 1 212 ? 111.769 142.637 121.881 1.00 33.37 ?  212 ALA B CA    1 
ATOM   7269  C  C     . ALA B 1 212 ? 112.988 143.532 122.051 1.00 38.75 ?  212 ALA B C     1 
ATOM   7270  O  O     . ALA B 1 212 ? 113.116 144.248 123.049 1.00 40.21 ?  212 ALA B O     1 
ATOM   7271  C  CB    . ALA B 1 212 ? 110.613 143.440 121.285 1.00 37.58 ?  212 ALA B CB    1 
ATOM   7272  N  N     . ILE B 1 213 ? 113.882 143.486 121.068 1.00 35.60 ?  213 ILE B N     1 
ATOM   7273  C  CA    . ILE B 1 213 ? 115.029 144.383 120.990 1.00 35.47 ?  213 ILE B CA    1 
ATOM   7274  C  C     . ILE B 1 213 ? 114.848 145.208 119.723 1.00 35.53 ?  213 ILE B C     1 
ATOM   7275  O  O     . ILE B 1 213 ? 115.120 144.726 118.618 1.00 42.01 ?  213 ILE B O     1 
ATOM   7276  C  CB    . ILE B 1 213 ? 116.365 143.630 120.981 1.00 37.16 ?  213 ILE B CB    1 
ATOM   7277  C  CG1   . ILE B 1 213 ? 116.462 142.690 122.182 1.00 36.22 ?  213 ILE B CG1   1 
ATOM   7278  C  CG2   . ILE B 1 213 ? 117.527 144.609 120.982 1.00 33.09 ?  213 ILE B CG2   1 
ATOM   7279  C  CD1   . ILE B 1 213 ? 117.635 141.742 122.117 1.00 31.45 ?  213 ILE B CD1   1 
ATOM   7280  N  N     . LYS B 1 214 ? 114.383 146.451 119.885 1.00 40.21 ?  214 LYS B N     1 
ATOM   7281  C  CA    . LYS B 1 214 ? 114.143 147.410 118.805 1.00 39.89 ?  214 LYS B CA    1 
ATOM   7282  C  C     . LYS B 1 214 ? 113.459 146.770 117.600 1.00 45.59 ?  214 LYS B C     1 
ATOM   7283  O  O     . LYS B 1 214 ? 114.055 146.657 116.524 1.00 45.66 ?  214 LYS B O     1 
ATOM   7284  C  CB    . LYS B 1 214 ? 115.436 148.138 118.388 1.00 39.26 ?  214 LYS B CB    1 
ATOM   7285  C  CG    . LYS B 1 214 ? 116.667 147.298 118.082 1.00 41.69 ?  214 LYS B CG    1 
ATOM   7286  C  CD    . LYS B 1 214 ? 117.704 148.117 117.334 1.00 40.17 ?  214 LYS B CD    1 
ATOM   7287  C  CE    . LYS B 1 214 ? 119.042 147.406 117.286 1.00 42.26 ?  214 LYS B CE    1 
ATOM   7288  N  NZ    . LYS B 1 214 ? 120.174 148.374 117.307 1.00 44.06 1  214 LYS B NZ    1 
ATOM   7289  N  N     . ASP B 1 215 ? 112.213 146.333 117.792 1.00 52.33 ?  215 ASP B N     1 
ATOM   7290  C  CA    . ASP B 1 215 ? 111.282 145.780 116.813 1.00 53.60 ?  215 ASP B CA    1 
ATOM   7291  C  C     . ASP B 1 215 ? 111.561 144.315 116.491 1.00 54.25 ?  215 ASP B C     1 
ATOM   7292  O  O     . ASP B 1 215 ? 110.829 143.733 115.690 1.00 56.29 ?  215 ASP B O     1 
ATOM   7293  C  CB    . ASP B 1 215 ? 111.241 146.574 115.491 1.00 52.06 ?  215 ASP B CB    1 
ATOM   7294  C  CG    . ASP B 1 215 ? 110.570 147.923 115.644 1.00 59.18 ?  215 ASP B CG    1 
ATOM   7295  O  OD1   . ASP B 1 215 ? 109.338 147.956 115.851 1.00 56.38 ?  215 ASP B OD1   1 
ATOM   7296  O  OD2   . ASP B 1 215 ? 111.274 148.951 115.556 1.00 56.99 -1 215 ASP B OD2   1 
ATOM   7297  N  N     . VAL B 1 216 ? 112.580 143.695 117.075 1.00 48.01 ?  216 VAL B N     1 
ATOM   7298  C  CA    . VAL B 1 216 ? 112.801 142.264 116.896 1.00 43.71 ?  216 VAL B CA    1 
ATOM   7299  C  C     . VAL B 1 216 ? 112.304 141.547 118.145 1.00 48.49 ?  216 VAL B C     1 
ATOM   7300  O  O     . VAL B 1 216 ? 113.005 141.488 119.160 1.00 51.75 ?  216 VAL B O     1 
ATOM   7301  C  CB    . VAL B 1 216 ? 114.282 141.960 116.628 1.00 45.75 ?  216 VAL B CB    1 
ATOM   7302  C  CG1   . VAL B 1 216 ? 114.506 140.461 116.513 1.00 45.61 ?  216 VAL B CG1   1 
ATOM   7303  C  CG2   . VAL B 1 216 ? 114.745 142.672 115.370 1.00 43.69 ?  216 VAL B CG2   1 
ATOM   7304  N  N     . GLU B 1 217 ? 111.097 140.998 118.069 1.00 49.70 ?  217 GLU B N     1 
ATOM   7305  C  CA    . GLU B 1 217 ? 110.441 140.390 119.216 1.00 50.06 ?  217 GLU B CA    1 
ATOM   7306  C  C     . GLU B 1 217 ? 111.116 139.080 119.600 1.00 45.18 ?  217 GLU B C     1 
ATOM   7307  O  O     . GLU B 1 217 ? 111.756 138.421 118.780 1.00 45.39 ?  217 GLU B O     1 
ATOM   7308  C  CB    . GLU B 1 217 ? 108.962 140.141 118.919 1.00 46.34 ?  217 GLU B CB    1 
ATOM   7309  C  CG    . GLU B 1 217 ? 108.358 141.115 117.928 1.00 49.31 ?  217 GLU B CG    1 
ATOM   7310  C  CD    . GLU B 1 217 ? 108.013 142.446 118.564 1.00 52.31 ?  217 GLU B CD    1 
ATOM   7311  O  OE1   . GLU B 1 217 ? 107.413 142.444 119.659 1.00 50.98 ?  217 GLU B OE1   1 
ATOM   7312  O  OE2   . GLU B 1 217 ? 108.342 143.493 117.968 1.00 54.93 -1 217 GLU B OE2   1 
ATOM   7313  N  N     . ASN B 1 218 ? 110.962 138.712 120.874 1.00 42.09 ?  218 ASN B N     1 
ATOM   7314  C  CA    . ASN B 1 218 ? 111.440 137.432 121.399 1.00 43.42 ?  218 ASN B CA    1 
ATOM   7315  C  C     . ASN B 1 218 ? 112.934 137.240 121.151 1.00 46.69 ?  218 ASN B C     1 
ATOM   7316  O  O     . ASN B 1 218 ? 113.388 136.163 120.761 1.00 48.20 ?  218 ASN B O     1 
ATOM   7317  C  CB    . ASN B 1 218 ? 110.635 136.272 120.809 1.00 42.39 ?  218 ASN B CB    1 
ATOM   7318  C  CG    . ASN B 1 218 ? 110.581 135.074 121.729 1.00 46.35 ?  218 ASN B CG    1 
ATOM   7319  O  OD1   . ASN B 1 218 ? 109.704 134.976 122.588 1.00 49.47 ?  218 ASN B OD1   1 
ATOM   7320  N  ND2   . ASN B 1 218 ? 111.519 134.152 121.556 1.00 47.74 ?  218 ASN B ND2   1 
ATOM   7321  N  N     . ALA B 1 219 ? 113.714 138.298 121.385 1.00 35.88 ?  219 ALA B N     1 
ATOM   7322  C  CA    . ALA B 1 219 ? 115.140 138.281 121.092 1.00 33.97 ?  219 ALA B CA    1 
ATOM   7323  C  C     . ALA B 1 219 ? 116.034 138.355 122.321 1.00 37.71 ?  219 ALA B C     1 
ATOM   7324  O  O     . ALA B 1 219 ? 117.242 138.134 122.194 1.00 37.78 ?  219 ALA B O     1 
ATOM   7325  C  CB    . ALA B 1 219 ? 115.503 139.442 120.154 1.00 34.85 ?  219 ALA B CB    1 
ATOM   7326  N  N     . THR B 1 220 ? 115.484 138.655 123.492 1.00 34.96 ?  220 THR B N     1 
ATOM   7327  C  CA    . THR B 1 220 ? 116.282 138.849 124.694 1.00 33.11 ?  220 THR B CA    1 
ATOM   7328  C  C     . THR B 1 220 ? 116.456 137.526 125.429 1.00 35.08 ?  220 THR B C     1 
ATOM   7329  O  O     . THR B 1 220 ? 115.492 136.778 125.611 1.00 33.67 ?  220 THR B O     1 
ATOM   7330  C  CB    . THR B 1 220 ? 115.624 139.884 125.609 1.00 28.35 ?  220 THR B CB    1 
ATOM   7331  O  OG1   . THR B 1 220 ? 115.459 141.115 124.897 1.00 34.03 ?  220 THR B OG1   1 
ATOM   7332  C  CG2   . THR B 1 220 ? 116.479 140.135 126.837 1.00 33.35 ?  220 THR B CG2   1 
ATOM   7333  N  N     . LYS B 1 221 ? 117.693 137.240 125.842 1.00 35.88 ?  221 LYS B N     1 
ATOM   7334  C  CA    . LYS B 1 221 ? 117.977 136.053 126.638 1.00 32.46 ?  221 LYS B CA    1 
ATOM   7335  C  C     . LYS B 1 221 ? 117.551 136.198 128.090 1.00 36.33 ?  221 LYS B C     1 
ATOM   7336  O  O     . LYS B 1 221 ? 117.584 135.210 128.830 1.00 40.45 ?  221 LYS B O     1 
ATOM   7337  C  CB    . LYS B 1 221 ? 119.469 135.719 126.588 1.00 33.12 ?  221 LYS B CB    1 
ATOM   7338  C  CG    . LYS B 1 221 ? 120.186 136.234 125.361 1.00 31.06 ?  221 LYS B CG    1 
ATOM   7339  C  CD    . LYS B 1 221 ? 121.524 135.540 125.193 1.00 36.10 ?  221 LYS B CD    1 
ATOM   7340  C  CE    . LYS B 1 221 ? 121.350 134.101 124.750 1.00 37.98 ?  221 LYS B CE    1 
ATOM   7341  N  NZ    . LYS B 1 221 ? 120.612 134.011 123.465 1.00 37.38 1  221 LYS B NZ    1 
ATOM   7342  N  N     . GLY B 1 222 ? 117.165 137.393 128.513 1.00 34.14 ?  222 GLY B N     1 
ATOM   7343  C  CA    . GLY B 1 222 ? 116.712 137.604 129.868 1.00 32.70 ?  222 GLY B CA    1 
ATOM   7344  C  C     . GLY B 1 222 ? 117.853 137.879 130.827 1.00 31.75 ?  222 GLY B C     1 
ATOM   7345  O  O     . GLY B 1 222 ? 118.983 138.190 130.443 1.00 34.90 ?  222 GLY B O     1 
ATOM   7346  N  N     . VAL B 1 223 ? 117.534 137.762 132.118 1.00 26.93 ?  223 VAL B N     1 
ATOM   7347  C  CA    . VAL B 1 223 ? 118.531 138.004 133.156 1.00 30.96 ?  223 VAL B CA    1 
ATOM   7348  C  C     . VAL B 1 223 ? 119.515 136.859 133.304 1.00 22.59 ?  223 VAL B C     1 
ATOM   7349  O  O     . VAL B 1 223 ? 120.568 137.045 133.920 1.00 25.89 ?  223 VAL B O     1 
ATOM   7350  C  CB    . VAL B 1 223 ? 117.868 138.279 134.519 1.00 27.74 ?  223 VAL B CB    1 
ATOM   7351  C  CG1   . VAL B 1 223 ? 116.776 139.323 134.375 1.00 21.69 ?  223 VAL B CG1   1 
ATOM   7352  C  CG2   . VAL B 1 223 ? 117.316 136.997 135.121 1.00 26.44 ?  223 VAL B CG2   1 
ATOM   7353  N  N     . VAL B 1 224 ? 119.217 135.684 132.746 1.00 26.79 ?  224 VAL B N     1 
ATOM   7354  C  CA    . VAL B 1 224 ? 120.107 134.541 132.927 1.00 26.01 ?  224 VAL B CA    1 
ATOM   7355  C  C     . VAL B 1 224 ? 121.333 134.637 132.021 1.00 31.64 ?  224 VAL B C     1 
ATOM   7356  O  O     . VAL B 1 224 ? 122.421 134.192 132.400 1.00 37.19 ?  224 VAL B O     1 
ATOM   7357  C  CB    . VAL B 1 224 ? 119.336 133.231 132.704 1.00 32.12 ?  224 VAL B CB    1 
ATOM   7358  C  CG1   . VAL B 1 224 ? 120.219 132.036 133.015 1.00 28.23 ?  224 VAL B CG1   1 
ATOM   7359  C  CG2   . VAL B 1 224 ? 118.091 133.208 133.567 1.00 32.42 ?  224 VAL B CG2   1 
ATOM   7360  N  N     . GLY B 1 225 ? 121.197 135.211 130.825 1.00 20.31 ?  225 GLY B N     1 
ATOM   7361  C  CA    . GLY B 1 225 ? 122.375 135.461 130.010 1.00 17.94 ?  225 GLY B CA    1 
ATOM   7362  C  C     . GLY B 1 225 ? 123.328 136.441 130.665 1.00 20.10 ?  225 GLY B C     1 
ATOM   7363  O  O     . GLY B 1 225 ? 124.546 136.229 130.681 1.00 30.82 ?  225 GLY B O     1 
ATOM   7364  N  N     . VAL B 1 226 ? 122.784 137.520 131.230 1.00 18.63 ?  226 VAL B N     1 
ATOM   7365  C  CA    . VAL B 1 226 ? 123.598 138.456 131.996 1.00 21.71 ?  226 VAL B CA    1 
ATOM   7366  C  C     . VAL B 1 226 ? 124.176 137.774 133.226 1.00 18.90 ?  226 VAL B C     1 
ATOM   7367  O  O     . VAL B 1 226 ? 125.298 138.075 133.642 1.00 23.94 ?  226 VAL B O     1 
ATOM   7368  C  CB    . VAL B 1 226 ? 122.769 139.700 132.372 1.00 21.28 ?  226 VAL B CB    1 
ATOM   7369  C  CG1   . VAL B 1 226 ? 123.633 140.722 133.089 1.00 29.21 ?  226 VAL B CG1   1 
ATOM   7370  C  CG2   . VAL B 1 226 ? 122.143 140.304 131.130 1.00 23.54 ?  226 VAL B CG2   1 
ATOM   7371  N  N     . MET B 1 227 ? 123.424 136.851 133.827 1.00 22.86 ?  227 MET B N     1 
ATOM   7372  C  CA    . MET B 1 227 ? 123.930 136.097 134.969 1.00 23.74 ?  227 MET B CA    1 
ATOM   7373  C  C     . MET B 1 227 ? 125.144 135.262 134.588 1.00 25.47 ?  227 MET B C     1 
ATOM   7374  O  O     . MET B 1 227 ? 126.125 135.209 135.333 1.00 28.53 ?  227 MET B O     1 
ATOM   7375  C  CB    . MET B 1 227 ? 122.824 135.205 135.526 1.00 17.04 ?  227 MET B CB    1 
ATOM   7376  C  CG    . MET B 1 227 ? 121.903 135.887 136.512 1.00 18.35 ?  227 MET B CG    1 
ATOM   7377  S  SD    . MET B 1 227 ? 120.836 134.692 137.321 1.00 33.72 ?  227 MET B SD    1 
ATOM   7378  C  CE    . MET B 1 227 ? 121.899 134.179 138.656 1.00 30.40 ?  227 MET B CE    1 
ATOM   7379  N  N     . LYS B 1 228 ? 125.089 134.593 133.436 1.00 23.81 ?  228 LYS B N     1 
ATOM   7380  C  CA    . LYS B 1 228 ? 126.238 133.825 132.961 1.00 19.93 ?  228 LYS B CA    1 
ATOM   7381  C  C     . LYS B 1 228 ? 127.423 134.734 132.665 1.00 20.40 ?  228 LYS B C     1 
ATOM   7382  O  O     . LYS B 1 228 ? 128.571 134.405 133.000 1.00 26.34 ?  228 LYS B O     1 
ATOM   7383  C  CB    . LYS B 1 228 ? 125.861 133.029 131.714 1.00 22.60 ?  228 LYS B CB    1 
ATOM   7384  C  CG    . LYS B 1 228 ? 124.732 132.044 131.916 1.00 24.65 ?  228 LYS B CG    1 
ATOM   7385  C  CD    . LYS B 1 228 ? 124.713 131.018 130.801 1.00 33.66 ?  228 LYS B CD    1 
ATOM   7386  C  CE    . LYS B 1 228 ? 123.774 131.432 129.680 1.00 38.31 ?  228 LYS B CE    1 
ATOM   7387  N  NZ    . LYS B 1 228 ? 122.352 131.143 130.012 1.00 36.29 1  228 LYS B NZ    1 
ATOM   7388  N  N     . LEU B 1 229 ? 127.164 135.878 132.028 1.00 22.70 ?  229 LEU B N     1 
ATOM   7389  C  CA    . LEU B 1 229 ? 128.233 136.833 131.758 1.00 20.74 ?  229 LEU B CA    1 
ATOM   7390  C  C     . LEU B 1 229 ? 128.896 137.289 133.049 1.00 24.12 ?  229 LEU B C     1 
ATOM   7391  O  O     . LEU B 1 229 ? 130.127 137.342 133.145 1.00 29.02 ?  229 LEU B O     1 
ATOM   7392  C  CB    . LEU B 1 229 ? 127.684 138.038 130.996 1.00 23.24 ?  229 LEU B CB    1 
ATOM   7393  C  CG    . LEU B 1 229 ? 127.434 137.923 129.496 1.00 19.83 ?  229 LEU B CG    1 
ATOM   7394  C  CD1   . LEU B 1 229 ? 126.550 139.069 129.050 1.00 24.18 ?  229 LEU B CD1   1 
ATOM   7395  C  CD2   . LEU B 1 229 ? 128.744 137.927 128.736 1.00 19.50 ?  229 LEU B CD2   1 
ATOM   7396  N  N     . LEU B 1 230 ? 128.090 137.614 134.060 1.00 27.00 ?  230 LEU B N     1 
ATOM   7397  C  CA    . LEU B 1 230 ? 128.628 138.083 135.332 1.00 18.28 ?  230 LEU B CA    1 
ATOM   7398  C  C     . LEU B 1 230 ? 129.357 136.971 136.071 1.00 13.47 ?  230 LEU B C     1 
ATOM   7399  O  O     . LEU B 1 230 ? 130.373 137.220 136.724 1.00 32.34 ?  230 LEU B O     1 
ATOM   7400  C  CB    . LEU B 1 230 ? 127.505 138.654 136.196 1.00 19.19 ?  230 LEU B CB    1 
ATOM   7401  C  CG    . LEU B 1 230 ? 126.872 139.952 135.700 1.00 23.66 ?  230 LEU B CG    1 
ATOM   7402  C  CD1   . LEU B 1 230 ? 125.646 140.292 136.528 1.00 28.79 ?  230 LEU B CD1   1 
ATOM   7403  C  CD2   . LEU B 1 230 ? 127.881 141.089 135.730 1.00 24.41 ?  230 LEU B CD2   1 
ATOM   7404  N  N     . ASP B 1 231 ? 128.850 135.740 135.992 1.00 22.77 ?  231 ASP B N     1 
ATOM   7405  C  CA    . ASP B 1 231 ? 129.525 134.622 136.639 1.00 25.27 ?  231 ASP B CA    1 
ATOM   7406  C  C     . ASP B 1 231 ? 130.904 134.396 136.037 1.00 29.78 ?  231 ASP B C     1 
ATOM   7407  O  O     . ASP B 1 231 ? 131.885 134.207 136.766 1.00 33.95 ?  231 ASP B O     1 
ATOM   7408  C  CB    . ASP B 1 231 ? 128.673 133.359 136.524 1.00 24.32 ?  231 ASP B CB    1 
ATOM   7409  C  CG    . ASP B 1 231 ? 129.219 132.211 137.345 1.00 40.21 ?  231 ASP B CG    1 
ATOM   7410  O  OD1   . ASP B 1 231 ? 129.055 132.234 138.582 1.00 44.23 ?  231 ASP B OD1   1 
ATOM   7411  O  OD2   . ASP B 1 231 ? 129.814 131.284 136.756 1.00 39.45 -1 231 ASP B OD2   1 
ATOM   7412  N  N     . ASN B 1 232 ? 131.006 134.438 134.708 1.00 30.21 ?  232 ASN B N     1 
ATOM   7413  C  CA    . ASN B 1 232 ? 132.315 134.299 134.077 1.00 28.77 ?  232 ASN B CA    1 
ATOM   7414  C  C     . ASN B 1 232 ? 133.205 135.506 134.354 1.00 23.15 ?  232 ASN B C     1 
ATOM   7415  O  O     . ASN B 1 232 ? 134.425 135.362 134.491 1.00 31.63 ?  232 ASN B O     1 
ATOM   7416  C  CB    . ASN B 1 232 ? 132.150 134.064 132.580 1.00 26.34 ?  232 ASN B CB    1 
ATOM   7417  C  CG    . ASN B 1 232 ? 132.100 132.594 132.238 1.00 31.22 ?  232 ASN B CG    1 
ATOM   7418  O  OD1   . ASN B 1 232 ? 132.896 131.804 132.741 1.00 36.86 ?  232 ASN B OD1   1 
ATOM   7419  N  ND2   . ASN B 1 232 ? 131.135 132.210 131.426 1.00 35.04 ?  232 ASN B ND2   1 
ATOM   7420  N  N     . ALA B 1 233 ? 132.618 136.700 134.444 1.00 18.47 ?  233 ALA B N     1 
ATOM   7421  C  CA    . ALA B 1 233 ? 133.402 137.884 134.776 1.00 15.26 ?  233 ALA B CA    1 
ATOM   7422  C  C     . ALA B 1 233 ? 133.993 137.780 136.177 1.00 26.94 ?  233 ALA B C     1 
ATOM   7423  O  O     . ALA B 1 233 ? 135.146 138.163 136.403 1.00 30.67 ?  233 ALA B O     1 
ATOM   7424  C  CB    . ALA B 1 233 ? 132.533 139.133 134.647 1.00 20.26 ?  233 ALA B CB    1 
ATOM   7425  N  N     . PHE B 1 234 ? 133.211 137.272 137.132 1.00 30.52 ?  234 PHE B N     1 
ATOM   7426  C  CA    . PHE B 1 234 ? 133.709 137.102 138.492 1.00 24.01 ?  234 PHE B CA    1 
ATOM   7427  C  C     . PHE B 1 234 ? 134.704 135.955 138.585 1.00 24.34 ?  234 PHE B C     1 
ATOM   7428  O  O     . PHE B 1 234 ? 135.643 136.017 139.387 1.00 29.06 ?  234 PHE B O     1 
ATOM   7429  C  CB    . PHE B 1 234 ? 132.545 136.876 139.456 1.00 21.79 ?  234 PHE B CB    1 
ATOM   7430  C  CG    . PHE B 1 234 ? 131.809 138.131 139.815 1.00 21.25 ?  234 PHE B CG    1 
ATOM   7431  C  CD1   . PHE B 1 234 ? 132.474 139.197 140.393 1.00 24.86 ?  234 PHE B CD1   1 
ATOM   7432  C  CD2   . PHE B 1 234 ? 130.453 138.246 139.577 1.00 23.68 ?  234 PHE B CD2   1 
ATOM   7433  C  CE1   . PHE B 1 234 ? 131.797 140.352 140.720 1.00 24.28 ?  234 PHE B CE1   1 
ATOM   7434  C  CE2   . PHE B 1 234 ? 129.775 139.399 139.899 1.00 23.92 ?  234 PHE B CE2   1 
ATOM   7435  C  CZ    . PHE B 1 234 ? 130.446 140.451 140.474 1.00 24.77 ?  234 PHE B CZ    1 
ATOM   7436  N  N     . ARG B 1 235 ? 134.513 134.901 137.789 1.00 31.14 ?  235 ARG B N     1 
ATOM   7437  C  CA    . ARG B 1 235 ? 135.493 133.821 137.747 1.00 25.16 ?  235 ARG B CA    1 
ATOM   7438  C  C     . ARG B 1 235 ? 136.823 134.304 137.182 1.00 31.81 ?  235 ARG B C     1 
ATOM   7439  O  O     . ARG B 1 235 ? 137.888 133.889 137.652 1.00 40.91 ?  235 ARG B O     1 
ATOM   7440  C  CB    . ARG B 1 235 ? 134.953 132.648 136.931 1.00 28.01 ?  235 ARG B CB    1 
ATOM   7441  C  CG    . ARG B 1 235 ? 134.213 131.621 137.766 1.00 38.67 ?  235 ARG B CG    1 
ATOM   7442  C  CD    . ARG B 1 235 ? 133.945 130.338 137.000 1.00 33.71 ?  235 ARG B CD    1 
ATOM   7443  N  NE    . ARG B 1 235 ? 132.591 130.298 136.463 1.00 37.92 ?  235 ARG B NE    1 
ATOM   7444  C  CZ    . ARG B 1 235 ? 132.301 130.191 135.173 1.00 40.90 ?  235 ARG B CZ    1 
ATOM   7445  N  NH1   . ARG B 1 235 ? 133.252 130.093 134.259 1.00 42.51 1  235 ARG B NH1   1 
ATOM   7446  N  NH2   . ARG B 1 235 ? 131.028 130.184 134.794 1.00 36.14 ?  235 ARG B NH2   1 
ATOM   7447  N  N     . TYR B 1 236 ? 136.785 135.167 136.167 1.00 22.81 ?  236 TYR B N     1 
ATOM   7448  C  CA    . TYR B 1 236 ? 138.026 135.682 135.599 1.00 24.99 ?  236 TYR B CA    1 
ATOM   7449  C  C     . TYR B 1 236 ? 138.715 136.639 136.563 1.00 24.34 ?  236 TYR B C     1 
ATOM   7450  O  O     . TYR B 1 236 ? 139.922 136.529 136.806 1.00 26.55 ?  236 TYR B O     1 
ATOM   7451  C  CB    . TYR B 1 236 ? 137.751 136.376 134.267 1.00 24.45 ?  236 TYR B CB    1 
ATOM   7452  C  CG    . TYR B 1 236 ? 139.004 136.876 133.596 1.00 22.08 ?  236 TYR B CG    1 
ATOM   7453  C  CD1   . TYR B 1 236 ? 139.887 135.989 133.000 1.00 18.62 ?  236 TYR B CD1   1 
ATOM   7454  C  CD2   . TYR B 1 236 ? 139.315 138.228 133.570 1.00 18.79 ?  236 TYR B CD2   1 
ATOM   7455  C  CE1   . TYR B 1 236 ? 141.033 136.429 132.391 1.00 23.08 ?  236 TYR B CE1   1 
ATOM   7456  C  CE2   . TYR B 1 236 ? 140.463 138.678 132.960 1.00 13.61 ?  236 TYR B CE2   1 
ATOM   7457  C  CZ    . TYR B 1 236 ? 141.317 137.773 132.373 1.00 20.82 ?  236 TYR B CZ    1 
ATOM   7458  O  OH    . TYR B 1 236 ? 142.464 138.204 131.759 1.00 30.55 ?  236 TYR B OH    1 
ATOM   7459  N  N     . ALA B 1 237 ? 137.964 137.589 137.122 1.00 29.80 ?  237 ALA B N     1 
ATOM   7460  C  CA    . ALA B 1 237 ? 138.510 138.560 138.069 1.00 29.51 ?  237 ALA B CA    1 
ATOM   7461  C  C     . ALA B 1 237 ? 138.549 137.924 139.458 1.00 36.56 ?  237 ALA B C     1 
ATOM   7462  O  O     . ALA B 1 237 ? 137.785 138.258 140.365 1.00 36.35 ?  237 ALA B O     1 
ATOM   7463  C  CB    . ALA B 1 237 ? 137.693 139.843 138.054 1.00 30.47 ?  237 ALA B CB    1 
ATOM   7464  N  N     . ASP B 1 238 ? 139.478 136.979 139.610 1.00 51.59 ?  238 ASP B N     1 
ATOM   7465  C  CA    . ASP B 1 238 ? 139.578 136.159 140.809 1.00 51.32 ?  238 ASP B CA    1 
ATOM   7466  C  C     . ASP B 1 238 ? 140.585 136.703 141.812 1.00 55.56 ?  238 ASP B C     1 
ATOM   7467  O  O     . ASP B 1 238 ? 141.219 135.918 142.531 1.00 57.66 ?  238 ASP B O     1 
ATOM   7468  C  CB    . ASP B 1 238 ? 139.930 134.720 140.428 1.00 49.85 ?  238 ASP B CB    1 
ATOM   7469  C  CG    . ASP B 1 238 ? 138.781 133.763 140.652 1.00 54.08 ?  238 ASP B CG    1 
ATOM   7470  O  OD1   . ASP B 1 238 ? 138.771 132.686 140.021 1.00 53.16 ?  238 ASP B OD1   1 
ATOM   7471  O  OD2   . ASP B 1 238 ? 137.875 134.096 141.443 1.00 53.25 -1 238 ASP B OD2   1 
ATOM   7472  N  N     . GLN B 1 239 ? 140.759 138.025 141.865 1.00 64.45 ?  239 GLN B N     1 
ATOM   7473  C  CA    . GLN B 1 239 ? 141.653 138.676 142.825 1.00 65.28 ?  239 GLN B CA    1 
ATOM   7474  C  C     . GLN B 1 239 ? 143.082 138.150 142.699 1.00 67.16 ?  239 GLN B C     1 
ATOM   7475  O  O     . GLN B 1 239 ? 143.696 137.714 143.675 1.00 64.76 ?  239 GLN B O     1 
ATOM   7476  C  CB    . GLN B 1 239 ? 141.133 138.512 144.256 1.00 64.30 ?  239 GLN B CB    1 
ATOM   7477  C  CG    . GLN B 1 239 ? 139.685 138.926 144.437 1.00 63.46 ?  239 GLN B CG    1 
ATOM   7478  C  CD    . GLN B 1 239 ? 139.145 138.569 145.804 1.00 66.62 ?  239 GLN B CD    1 
ATOM   7479  O  OE1   . GLN B 1 239 ? 137.953 138.308 145.964 1.00 64.72 ?  239 GLN B OE1   1 
ATOM   7480  N  NE2   . GLN B 1 239 ? 140.020 138.557 146.801 1.00 66.44 ?  239 GLN B NE2   1 
ATOM   7481  N  N     . MET B 1 240 ? 143.606 138.188 141.472 1.00 68.36 ?  240 MET B N     1 
ATOM   7482  C  CA    . MET B 1 240 ? 144.967 137.741 141.170 1.00 67.11 ?  240 MET B CA    1 
ATOM   7483  C  C     . MET B 1 240 ? 145.199 136.293 141.590 1.00 67.96 ?  240 MET B C     1 
ATOM   7484  O  O     . MET B 1 240 ? 146.294 135.930 142.029 1.00 68.29 ?  240 MET B O     1 
ATOM   7485  C  CB    . MET B 1 240 ? 146.011 138.656 141.818 1.00 67.19 ?  240 MET B CB    1 
ATOM   7486  C  CG    . MET B 1 240 ? 146.081 140.051 141.224 1.00 68.64 ?  240 MET B CG    1 
ATOM   7487  S  SD    . MET B 1 240 ? 144.473 140.745 140.806 1.00 76.69 ?  240 MET B SD    1 
ATOM   7488  C  CE    . MET B 1 240 ? 144.912 142.467 140.606 1.00 66.55 ?  240 MET B CE    1 
ATOM   7489  N  N     . GLY B 1 241 ? 144.173 135.454 141.466 1.00 70.46 ?  241 GLY B N     1 
ATOM   7490  C  CA    . GLY B 1 241 ? 144.300 134.060 141.840 1.00 69.56 ?  241 GLY B CA    1 
ATOM   7491  C  C     . GLY B 1 241 ? 144.464 133.803 143.319 1.00 72.28 ?  241 GLY B C     1 
ATOM   7492  O  O     . GLY B 1 241 ? 144.901 132.713 143.698 1.00 72.91 ?  241 GLY B O     1 
ATOM   7493  N  N     . GLN B 1 242 ? 144.129 134.773 144.171 1.00 73.68 ?  242 GLN B N     1 
ATOM   7494  C  CA    . GLN B 1 242 ? 144.281 134.617 145.614 1.00 73.00 ?  242 GLN B CA    1 
ATOM   7495  C  C     . GLN B 1 242 ? 142.999 134.097 146.258 1.00 73.64 ?  242 GLN B C     1 
ATOM   7496  O  O     . GLN B 1 242 ? 142.996 133.038 146.893 1.00 71.98 ?  242 GLN B O     1 
ATOM   7497  C  CB    . GLN B 1 242 ? 144.694 135.952 146.245 1.00 71.35 ?  242 GLN B CB    1 
ATOM   7498  C  CG    . GLN B 1 242 ? 146.072 136.442 145.830 1.00 73.43 ?  242 GLN B CG    1 
ATOM   7499  C  CD    . GLN B 1 242 ? 146.628 137.491 146.775 1.00 75.32 ?  242 GLN B CD    1 
ATOM   7500  O  OE1   . GLN B 1 242 ? 146.068 137.742 147.841 1.00 75.18 ?  242 GLN B OE1   1 
ATOM   7501  N  NE2   . GLN B 1 242 ? 147.738 138.108 146.387 1.00 72.12 ?  242 GLN B NE2   1 
ATOM   7502  N  N     . ARG B 1 243 ? 141.902 134.833 146.097 1.00 68.25 ?  243 ARG B N     1 
ATOM   7503  C  CA    . ARG B 1 243 ? 140.611 134.473 146.660 1.00 66.93 ?  243 ARG B CA    1 
ATOM   7504  C  C     . ARG B 1 243 ? 139.565 134.505 145.558 1.00 66.24 ?  243 ARG B C     1 
ATOM   7505  O  O     . ARG B 1 243 ? 139.569 135.407 144.716 1.00 65.42 ?  243 ARG B O     1 
ATOM   7506  C  CB    . ARG B 1 243 ? 140.226 135.424 147.802 1.00 66.32 ?  243 ARG B CB    1 
ATOM   7507  C  CG    . ARG B 1 243 ? 138.868 135.158 148.429 1.00 66.93 ?  243 ARG B CG    1 
ATOM   7508  C  CD    . ARG B 1 243 ? 138.383 136.379 149.200 1.00 67.50 ?  243 ARG B CD    1 
ATOM   7509  N  NE    . ARG B 1 243 ? 137.661 137.318 148.350 1.00 69.40 ?  243 ARG B NE    1 
ATOM   7510  C  CZ    . ARG B 1 243 ? 136.497 137.872 148.664 1.00 69.52 ?  243 ARG B CZ    1 
ATOM   7511  N  NH1   . ARG B 1 243 ? 135.892 137.606 149.809 1.00 66.61 1  243 ARG B NH1   1 
ATOM   7512  N  NH2   . ARG B 1 243 ? 135.928 138.716 147.808 1.00 64.05 ?  243 ARG B NH2   1 
ATOM   7513  N  N     . GLN B 1 244 ? 138.676 133.514 145.567 1.00 64.22 ?  244 GLN B N     1 
ATOM   7514  C  CA    . GLN B 1 244 ? 137.697 133.371 144.497 1.00 63.23 ?  244 GLN B CA    1 
ATOM   7515  C  C     . GLN B 1 244 ? 136.790 134.593 144.420 1.00 63.95 ?  244 GLN B C     1 
ATOM   7516  O  O     . GLN B 1 244 ? 136.300 135.086 145.440 1.00 61.87 ?  244 GLN B O     1 
ATOM   7517  C  CB    . GLN B 1 244 ? 136.866 132.107 144.712 1.00 61.27 ?  244 GLN B CB    1 
ATOM   7518  C  CG    . GLN B 1 244 ? 137.684 130.824 144.720 1.00 62.33 ?  244 GLN B CG    1 
ATOM   7519  C  CD    . GLN B 1 244 ? 136.817 129.581 144.760 1.00 62.46 ?  244 GLN B CD    1 
ATOM   7520  O  OE1   . GLN B 1 244 ? 135.799 129.540 145.451 1.00 60.44 ?  244 GLN B OE1   1 
ATOM   7521  N  NE2   . GLN B 1 244 ? 137.219 128.556 144.016 1.00 60.00 ?  244 GLN B NE2   1 
ATOM   7522  N  N     . GLY B 1 245 ? 136.575 135.083 143.199 1.00 49.21 ?  245 GLY B N     1 
ATOM   7523  C  CA    . GLY B 1 245 ? 135.720 136.231 142.973 1.00 44.50 ?  245 GLY B CA    1 
ATOM   7524  C  C     . GLY B 1 245 ? 134.275 135.966 143.339 1.00 44.34 ?  245 GLY B C     1 
ATOM   7525  O  O     . GLY B 1 245 ? 133.652 135.040 142.812 1.00 41.39 ?  245 GLY B O     1 
ATOM   7526  N  N     . SER B 1 246 ? 133.729 136.776 144.240 1.00 39.46 ?  246 SER B N     1 
ATOM   7527  C  CA    . SER B 1 246 ? 132.385 136.585 144.761 1.00 33.42 ?  246 SER B CA    1 
ATOM   7528  C  C     . SER B 1 246 ? 131.494 137.735 144.315 1.00 30.07 ?  246 SER B C     1 
ATOM   7529  O  O     . SER B 1 246 ? 131.847 138.905 144.486 1.00 23.53 ?  246 SER B O     1 
ATOM   7530  C  CB    . SER B 1 246 ? 132.400 136.488 146.288 1.00 31.88 ?  246 SER B CB    1 
ATOM   7531  O  OG    . SER B 1 246 ? 133.069 137.597 146.864 1.00 38.37 ?  246 SER B OG    1 
ATOM   7532  N  N     . GLY B 1 247 ? 130.341 137.394 143.745 1.00 26.03 ?  247 GLY B N     1 
ATOM   7533  C  CA    . GLY B 1 247 ? 129.383 138.391 143.329 1.00 10.12 ?  247 GLY B CA    1 
ATOM   7534  C  C     . GLY B 1 247 ? 127.975 137.927 143.635 1.00 12.49 ?  247 GLY B C     1 
ATOM   7535  O  O     . GLY B 1 247 ? 127.719 136.741 143.849 1.00 22.70 ?  247 GLY B O     1 
ATOM   7536  N  N     . ALA B 1 248 ? 127.060 138.889 143.653 1.00 17.14 ?  248 ALA B N     1 
ATOM   7537  C  CA    . ALA B 1 248 ? 125.661 138.621 143.935 1.00 17.75 ?  248 ALA B CA    1 
ATOM   7538  C  C     . ALA B 1 248 ? 124.792 139.281 142.878 1.00 16.83 ?  248 ALA B C     1 
ATOM   7539  O  O     . ALA B 1 248 ? 125.120 140.348 142.355 1.00 23.25 ?  248 ALA B O     1 
ATOM   7540  C  CB    . ALA B 1 248 ? 125.256 139.119 145.328 1.00 4.65  ?  248 ALA B CB    1 
ATOM   7541  N  N     . ALA B 1 249 ? 123.680 138.626 142.563 1.00 16.18 ?  249 ALA B N     1 
ATOM   7542  C  CA    . ALA B 1 249 ? 122.688 139.151 141.638 1.00 14.30 ?  249 ALA B CA    1 
ATOM   7543  C  C     . ALA B 1 249 ? 121.344 139.200 142.347 1.00 16.37 ?  249 ALA B C     1 
ATOM   7544  O  O     . ALA B 1 249 ? 120.957 138.240 143.017 1.00 24.63 ?  249 ALA B O     1 
ATOM   7545  C  CB    . ALA B 1 249 ? 122.597 138.296 140.374 1.00 11.62 ?  249 ALA B CB    1 
ATOM   7546  N  N     . TYR B 1 250 ? 120.641 140.316 142.205 1.00 17.18 ?  250 TYR B N     1 
ATOM   7547  C  CA    . TYR B 1 250 ? 119.347 140.500 142.838 1.00 5.89  ?  250 TYR B CA    1 
ATOM   7548  C  C     . TYR B 1 250 ? 118.279 140.691 141.775 1.00 7.44  ?  250 TYR B C     1 
ATOM   7549  O  O     . TYR B 1 250 ? 118.482 141.415 140.798 1.00 21.34 ?  250 TYR B O     1 
ATOM   7550  C  CB    . TYR B 1 250 ? 119.359 141.697 143.790 1.00 12.37 ?  250 TYR B CB    1 
ATOM   7551  C  CG    . TYR B 1 250 ? 119.852 141.362 145.177 1.00 15.54 ?  250 TYR B CG    1 
ATOM   7552  C  CD1   . TYR B 1 250 ? 121.198 141.131 145.417 1.00 8.40  ?  250 TYR B CD1   1 
ATOM   7553  C  CD2   . TYR B 1 250 ? 118.969 141.265 146.243 1.00 12.52 ?  250 TYR B CD2   1 
ATOM   7554  C  CE1   . TYR B 1 250 ? 121.652 140.818 146.679 1.00 1.20  ?  250 TYR B CE1   1 
ATOM   7555  C  CE2   . TYR B 1 250 ? 119.416 140.953 147.510 1.00 7.97  ?  250 TYR B CE2   1 
ATOM   7556  C  CZ    . TYR B 1 250 ? 120.759 140.732 147.721 1.00 11.67 ?  250 TYR B CZ    1 
ATOM   7557  O  OH    . TYR B 1 250 ? 121.212 140.424 148.981 1.00 21.15 ?  250 TYR B OH    1 
ATOM   7558  N  N     . LEU B 1 251 ? 117.144 140.028 141.971 1.00 14.84 ?  251 LEU B N     1 
ATOM   7559  C  CA    . LEU B 1 251 ? 116.010 140.154 141.072 1.00 15.67 ?  251 LEU B CA    1 
ATOM   7560  C  C     . LEU B 1 251 ? 114.740 140.311 141.891 1.00 10.15 ?  251 LEU B C     1 
ATOM   7561  O  O     . LEU B 1 251 ? 114.567 139.643 142.912 1.00 19.07 ?  251 LEU B O     1 
ATOM   7562  C  CB    . LEU B 1 251 ? 115.884 138.939 140.148 1.00 14.63 ?  251 LEU B CB    1 
ATOM   7563  C  CG    . LEU B 1 251 ? 115.046 139.151 138.890 1.00 14.48 ?  251 LEU B CG    1 
ATOM   7564  C  CD1   . LEU B 1 251 ? 115.764 140.053 137.911 1.00 6.94  ?  251 LEU B CD1   1 
ATOM   7565  C  CD2   . LEU B 1 251 ? 114.702 137.823 138.248 1.00 10.11 ?  251 LEU B CD2   1 
ATOM   7566  N  N     . ASN B 1 252 ? 113.860 141.199 141.439 1.00 12.31 ?  252 ASN B N     1 
ATOM   7567  C  CA    . ASN B 1 252 ? 112.557 141.340 142.070 1.00 10.56 ?  252 ASN B CA    1 
ATOM   7568  C  C     . ASN B 1 252 ? 111.726 140.084 141.845 1.00 17.18 ?  252 ASN B C     1 
ATOM   7569  O  O     . ASN B 1 252 ? 111.798 139.452 140.789 1.00 27.97 ?  252 ASN B O     1 
ATOM   7570  C  CB    . ASN B 1 252 ? 111.829 142.562 141.517 1.00 13.51 ?  252 ASN B CB    1 
ATOM   7571  C  CG    . ASN B 1 252 ? 110.859 143.160 142.513 1.00 20.90 ?  252 ASN B CG    1 
ATOM   7572  O  OD1   . ASN B 1 252 ? 109.802 142.592 142.784 1.00 31.96 ?  252 ASN B OD1   1 
ATOM   7573  N  ND2   . ASN B 1 252 ? 111.216 144.310 143.067 1.00 16.81 ?  252 ASN B ND2   1 
ATOM   7574  N  N     . ILE B 1 253 ? 110.932 139.718 142.854 1.00 12.04 ?  253 ILE B N     1 
ATOM   7575  C  CA    . ILE B 1 253 ? 110.099 138.529 142.738 1.00 17.59 ?  253 ILE B CA    1 
ATOM   7576  C  C     . ILE B 1 253 ? 109.005 138.701 141.691 1.00 23.32 ?  253 ILE B C     1 
ATOM   7577  O  O     . ILE B 1 253 ? 108.476 137.706 141.184 1.00 24.82 ?  253 ILE B O     1 
ATOM   7578  C  CB    . ILE B 1 253 ? 109.502 138.161 144.111 1.00 20.99 ?  253 ILE B CB    1 
ATOM   7579  C  CG1   . ILE B 1 253 ? 109.100 136.686 144.138 1.00 16.36 ?  253 ILE B CG1   1 
ATOM   7580  C  CG2   . ILE B 1 253 ? 108.327 139.064 144.451 1.00 14.57 ?  253 ILE B CG2   1 
ATOM   7581  C  CD1   . ILE B 1 253 ? 109.243 136.041 145.488 1.00 18.96 ?  253 ILE B CD1   1 
ATOM   7582  N  N     . PHE B 1 254 ? 108.657 139.938 141.342 1.00 30.33 ?  254 PHE B N     1 
ATOM   7583  C  CA    . PHE B 1 254 ? 107.671 140.202 140.304 1.00 18.12 ?  254 PHE B CA    1 
ATOM   7584  C  C     . PHE B 1 254 ? 108.292 140.299 138.918 1.00 20.80 ?  254 PHE B C     1 
ATOM   7585  O  O     . PHE B 1 254 ? 107.570 140.521 137.942 1.00 27.34 ?  254 PHE B O     1 
ATOM   7586  C  CB    . PHE B 1 254 ? 106.898 141.484 140.626 1.00 21.69 ?  254 PHE B CB    1 
ATOM   7587  C  CG    . PHE B 1 254 ? 105.828 141.297 141.663 1.00 26.47 ?  254 PHE B CG    1 
ATOM   7588  C  CD1   . PHE B 1 254 ? 104.731 140.495 141.404 1.00 25.87 ?  254 PHE B CD1   1 
ATOM   7589  C  CD2   . PHE B 1 254 ? 105.923 141.912 142.898 1.00 25.47 ?  254 PHE B CD2   1 
ATOM   7590  C  CE1   . PHE B 1 254 ? 103.746 140.317 142.352 1.00 29.44 ?  254 PHE B CE1   1 
ATOM   7591  C  CE2   . PHE B 1 254 ? 104.940 141.736 143.851 1.00 26.38 ?  254 PHE B CE2   1 
ATOM   7592  C  CZ    . PHE B 1 254 ? 103.851 140.938 143.577 1.00 25.35 ?  254 PHE B CZ    1 
ATOM   7593  N  N     . HIS B 1 255 ? 109.608 140.145 138.814 1.00 27.15 ?  255 HIS B N     1 
ATOM   7594  C  CA    . HIS B 1 255 ? 110.254 140.039 137.516 1.00 20.76 ?  255 HIS B CA    1 
ATOM   7595  C  C     . HIS B 1 255 ? 109.834 138.747 136.832 1.00 23.58 ?  255 HIS B C     1 
ATOM   7596  O  O     . HIS B 1 255 ? 109.657 137.710 137.477 1.00 30.47 ?  255 HIS B O     1 
ATOM   7597  C  CB    . HIS B 1 255 ? 111.772 140.088 137.674 1.00 17.98 ?  255 HIS B CB    1 
ATOM   7598  C  CG    . HIS B 1 255 ? 112.507 140.417 136.412 1.00 22.26 ?  255 HIS B CG    1 
ATOM   7599  N  ND1   . HIS B 1 255 ? 112.690 139.504 135.396 1.00 14.82 ?  255 HIS B ND1   1 
ATOM   7600  C  CD2   . HIS B 1 255 ? 113.119 141.555 136.008 1.00 20.06 ?  255 HIS B CD2   1 
ATOM   7601  C  CE1   . HIS B 1 255 ? 113.376 140.068 134.419 1.00 12.90 ?  255 HIS B CE1   1 
ATOM   7602  N  NE2   . HIS B 1 255 ? 113.652 141.311 134.765 1.00 12.09 ?  255 HIS B NE2   1 
ATOM   7603  N  N     . ARG B 1 256 ? 109.676 138.818 135.511 1.00 26.39 ?  256 ARG B N     1 
ATOM   7604  C  CA    . ARG B 1 256 ? 109.210 137.664 134.754 1.00 22.29 ?  256 ARG B CA    1 
ATOM   7605  C  C     . ARG B 1 256 ? 110.195 136.506 134.835 1.00 24.96 ?  256 ARG B C     1 
ATOM   7606  O  O     . ARG B 1 256 ? 109.793 135.338 134.883 1.00 32.64 ?  256 ARG B O     1 
ATOM   7607  C  CB    . ARG B 1 256 ? 108.970 138.072 133.304 1.00 26.13 ?  256 ARG B CB    1 
ATOM   7608  C  CG    . ARG B 1 256 ? 107.788 137.402 132.664 1.00 35.87 ?  256 ARG B CG    1 
ATOM   7609  C  CD    . ARG B 1 256 ? 108.134 136.014 132.185 1.00 31.95 ?  256 ARG B CD    1 
ATOM   7610  N  NE    . ARG B 1 256 ? 109.509 135.895 131.719 1.00 30.96 ?  256 ARG B NE    1 
ATOM   7611  C  CZ    . ARG B 1 256 ? 110.049 134.764 131.288 1.00 33.29 ?  256 ARG B CZ    1 
ATOM   7612  N  NH1   . ARG B 1 256 ? 109.360 133.635 131.262 1.00 30.55 1  256 ARG B NH1   1 
ATOM   7613  N  NH2   . ARG B 1 256 ? 111.313 134.764 130.878 1.00 34.33 ?  256 ARG B NH2   1 
ATOM   7614  N  N     . ASP B 1 257 ? 111.490 136.807 134.860 1.00 26.22 ?  257 ASP B N     1 
ATOM   7615  C  CA    . ASP B 1 257 ? 112.534 135.794 134.887 1.00 21.49 ?  257 ASP B CA    1 
ATOM   7616  C  C     . ASP B 1 257 ? 112.816 135.256 136.281 1.00 22.72 ?  257 ASP B C     1 
ATOM   7617  O  O     . ASP B 1 257 ? 113.890 134.683 136.488 1.00 27.09 ?  257 ASP B O     1 
ATOM   7618  C  CB    . ASP B 1 257 ? 113.823 136.355 134.289 1.00 25.70 ?  257 ASP B CB    1 
ATOM   7619  C  CG    . ASP B 1 257 ? 113.823 136.330 132.781 1.00 32.76 ?  257 ASP B CG    1 
ATOM   7620  O  OD1   . ASP B 1 257 ? 112.931 135.687 132.193 1.00 31.80 ?  257 ASP B OD1   1 
ATOM   7621  O  OD2   . ASP B 1 257 ? 114.716 136.959 132.183 1.00 36.44 -1 257 ASP B OD2   1 
ATOM   7622  N  N     . ILE B 1 258 ? 111.897 135.419 137.234 1.00 26.47 ?  258 ILE B N     1 
ATOM   7623  C  CA    . ILE B 1 258 ? 112.183 135.023 138.610 1.00 23.00 ?  258 ILE B CA    1 
ATOM   7624  C  C     . ILE B 1 258 ? 112.376 133.514 138.711 1.00 22.75 ?  258 ILE B C     1 
ATOM   7625  O  O     . ILE B 1 258 ? 113.242 133.038 139.453 1.00 34.15 ?  258 ILE B O     1 
ATOM   7626  C  CB    . ILE B 1 258 ? 111.079 135.532 139.557 1.00 27.55 ?  258 ILE B CB    1 
ATOM   7627  C  CG1   . ILE B 1 258 ? 111.429 135.209 141.012 1.00 24.90 ?  258 ILE B CG1   1 
ATOM   7628  C  CG2   . ILE B 1 258 ? 109.717 134.969 139.174 1.00 19.92 ?  258 ILE B CG2   1 
ATOM   7629  C  CD1   . ILE B 1 258 ? 112.736 135.817 141.469 1.00 17.22 ?  258 ILE B CD1   1 
ATOM   7630  N  N     . ASN B 1 259 ? 111.593 132.736 137.959 1.00 31.64 ?  259 ASN B N     1 
ATOM   7631  C  CA    . ASN B 1 259 ? 111.738 131.285 138.016 1.00 28.34 ?  259 ASN B CA    1 
ATOM   7632  C  C     . ASN B 1 259 ? 113.035 130.834 137.355 1.00 28.53 ?  259 ASN B C     1 
ATOM   7633  O  O     . ASN B 1 259 ? 113.723 129.948 137.870 1.00 30.84 ?  259 ASN B O     1 
ATOM   7634  C  CB    . ASN B 1 259 ? 110.531 130.610 137.368 1.00 29.00 ?  259 ASN B CB    1 
ATOM   7635  C  CG    . ASN B 1 259 ? 109.329 130.568 138.287 1.00 33.29 ?  259 ASN B CG    1 
ATOM   7636  O  OD1   . ASN B 1 259 ? 109.391 130.012 139.383 1.00 34.36 ?  259 ASN B OD1   1 
ATOM   7637  N  ND2   . ASN B 1 259 ? 108.226 131.159 137.847 1.00 34.97 ?  259 ASN B ND2   1 
ATOM   7638  N  N     . ASP B 1 260 ? 113.386 131.437 136.218 1.00 31.47 ?  260 ASP B N     1 
ATOM   7639  C  CA    . ASP B 1 260 ? 114.690 131.178 135.615 1.00 24.64 ?  260 ASP B CA    1 
ATOM   7640  C  C     . ASP B 1 260 ? 115.814 131.630 136.538 1.00 28.75 ?  260 ASP B C     1 
ATOM   7641  O  O     . ASP B 1 260 ? 116.854 130.968 136.636 1.00 33.75 ?  260 ASP B O     1 
ATOM   7642  C  CB    . ASP B 1 260 ? 114.791 131.884 134.265 1.00 27.87 ?  260 ASP B CB    1 
ATOM   7643  C  CG    . ASP B 1 260 ? 113.707 131.454 133.300 1.00 40.56 ?  260 ASP B CG    1 
ATOM   7644  O  OD1   . ASP B 1 260 ? 113.606 132.059 132.212 1.00 37.76 ?  260 ASP B OD1   1 
ATOM   7645  O  OD2   . ASP B 1 260 ? 112.955 130.513 133.629 1.00 42.90 -1 260 ASP B OD2   1 
ATOM   7646  N  N     . PHE B 1 261 ? 115.621 132.766 137.211 1.00 33.42 ?  261 PHE B N     1 
ATOM   7647  C  CA    . PHE B 1 261 ? 116.602 133.261 138.171 1.00 20.73 ?  261 PHE B CA    1 
ATOM   7648  C  C     . PHE B 1 261 ? 116.846 132.249 139.283 1.00 23.47 ?  261 PHE B C     1 
ATOM   7649  O  O     . PHE B 1 261 ? 117.991 132.018 139.687 1.00 26.79 ?  261 PHE B O     1 
ATOM   7650  C  CB    . PHE B 1 261 ? 116.106 134.589 138.744 1.00 14.21 ?  261 PHE B CB    1 
ATOM   7651  C  CG    . PHE B 1 261 ? 117.087 135.285 139.639 1.00 27.64 ?  261 PHE B CG    1 
ATOM   7652  C  CD1   . PHE B 1 261 ? 118.164 135.967 139.107 1.00 22.13 ?  261 PHE B CD1   1 
ATOM   7653  C  CD2   . PHE B 1 261 ? 116.908 135.291 141.010 1.00 21.15 ?  261 PHE B CD2   1 
ATOM   7654  C  CE1   . PHE B 1 261 ? 119.057 136.619 139.925 1.00 14.29 ?  261 PHE B CE1   1 
ATOM   7655  C  CE2   . PHE B 1 261 ? 117.799 135.944 141.832 1.00 12.58 ?  261 PHE B CE2   1 
ATOM   7656  C  CZ    . PHE B 1 261 ? 118.874 136.608 141.287 1.00 17.93 ?  261 PHE B CZ    1 
ATOM   7657  N  N     . LEU B 1 262 ? 115.776 131.631 139.789 1.00 31.41 ?  262 LEU B N     1 
ATOM   7658  C  CA    . LEU B 1 262 ? 115.915 130.657 140.864 1.00 25.47 ?  262 LEU B CA    1 
ATOM   7659  C  C     . LEU B 1 262 ? 116.460 129.326 140.366 1.00 30.04 ?  262 LEU B C     1 
ATOM   7660  O  O     . LEU B 1 262 ? 117.158 128.630 141.111 1.00 32.42 ?  262 LEU B O     1 
ATOM   7661  C  CB    . LEU B 1 262 ? 114.570 130.450 141.554 1.00 32.20 ?  262 LEU B CB    1 
ATOM   7662  C  CG    . LEU B 1 262 ? 113.937 131.697 142.165 1.00 22.35 ?  262 LEU B CG    1 
ATOM   7663  C  CD1   . LEU B 1 262 ? 112.565 131.376 142.724 1.00 29.16 ?  262 LEU B CD1   1 
ATOM   7664  C  CD2   . LEU B 1 262 ? 114.844 132.271 143.231 1.00 22.81 ?  262 LEU B CD2   1 
ATOM   7665  N  N     . ASP B 1 263 ? 116.158 128.952 139.121 1.00 42.45 ?  263 ASP B N     1 
ATOM   7666  C  CA    . ASP B 1 263 ? 116.614 127.675 138.586 1.00 31.66 ?  263 ASP B CA    1 
ATOM   7667  C  C     . ASP B 1 263 ? 118.123 127.611 138.404 1.00 34.41 ?  263 ASP B C     1 
ATOM   7668  O  O     . ASP B 1 263 ? 118.658 126.516 138.209 1.00 47.73 ?  263 ASP B O     1 
ATOM   7669  C  CB    . ASP B 1 263 ? 115.928 127.385 137.251 1.00 37.05 ?  263 ASP B CB    1 
ATOM   7670  C  CG    . ASP B 1 263 ? 114.450 127.100 137.405 1.00 46.24 ?  263 ASP B CG    1 
ATOM   7671  O  OD1   . ASP B 1 263 ? 113.998 126.900 138.551 1.00 42.48 ?  263 ASP B OD1   1 
ATOM   7672  O  OD2   . ASP B 1 263 ? 113.738 127.079 136.379 1.00 47.80 -1 263 ASP B OD2   1 
ATOM   7673  N  N     . THR B 1 264 ? 118.819 128.747 138.455 1.00 38.94 ?  264 THR B N     1 
ATOM   7674  C  CA    . THR B 1 264 ? 120.272 128.745 138.349 1.00 37.20 ?  264 THR B CA    1 
ATOM   7675  C  C     . THR B 1 264 ? 120.952 128.143 139.571 1.00 40.49 ?  264 THR B C     1 
ATOM   7676  O  O     . THR B 1 264 ? 122.150 127.849 139.508 1.00 41.51 ?  264 THR B O     1 
ATOM   7677  C  CB    . THR B 1 264 ? 120.787 130.169 138.126 1.00 34.86 ?  264 THR B CB    1 
ATOM   7678  O  OG1   . THR B 1 264 ? 120.404 130.998 139.231 1.00 37.84 ?  264 THR B OG1   1 
ATOM   7679  C  CG2   . THR B 1 264 ? 120.212 130.748 136.848 1.00 35.27 ?  264 THR B CG2   1 
ATOM   7680  N  N     . LYS B 1 265 ? 120.225 127.948 140.670 1.00 34.45 ?  265 LYS B N     1 
ATOM   7681  C  CA    . LYS B 1 265 ? 120.792 127.409 141.897 1.00 36.43 ?  265 LYS B CA    1 
ATOM   7682  C  C     . LYS B 1 265 ? 120.350 125.983 142.194 1.00 41.95 ?  265 LYS B C     1 
ATOM   7683  O  O     . LYS B 1 265 ? 120.746 125.432 143.226 1.00 44.94 ?  265 LYS B O     1 
ATOM   7684  C  CB    . LYS B 1 265 ? 120.437 128.313 143.081 1.00 35.53 ?  265 LYS B CB    1 
ATOM   7685  C  CG    . LYS B 1 265 ? 121.249 129.585 143.140 1.00 38.41 ?  265 LYS B CG    1 
ATOM   7686  C  CD    . LYS B 1 265 ? 122.728 129.283 143.029 1.00 42.43 ?  265 LYS B CD    1 
ATOM   7687  C  CE    . LYS B 1 265 ? 123.538 130.554 142.961 1.00 39.18 ?  265 LYS B CE    1 
ATOM   7688  N  NZ    . LYS B 1 265 ? 124.961 130.277 142.636 1.00 43.31 1  265 LYS B NZ    1 
ATOM   7689  N  N     . LYS B 1 266 ? 119.546 125.374 141.330 1.00 46.48 ?  266 LYS B N     1 
ATOM   7690  C  CA    . LYS B 1 266 ? 119.150 123.989 141.539 1.00 48.96 ?  266 LYS B CA    1 
ATOM   7691  C  C     . LYS B 1 266 ? 120.336 123.057 141.322 1.00 55.08 ?  266 LYS B C     1 
ATOM   7692  O  O     . LYS B 1 266 ? 121.222 123.320 140.506 1.00 56.31 ?  266 LYS B O     1 
ATOM   7693  C  CB    . LYS B 1 266 ? 118.005 123.612 140.601 1.00 48.89 ?  266 LYS B CB    1 
ATOM   7694  C  CG    . LYS B 1 266 ? 116.651 124.146 141.032 1.00 50.80 ?  266 LYS B CG    1 
ATOM   7695  C  CD    . LYS B 1 266 ? 115.578 123.810 140.012 1.00 51.90 ?  266 LYS B CD    1 
ATOM   7696  C  CE    . LYS B 1 266 ? 114.195 124.178 140.522 1.00 50.94 ?  266 LYS B CE    1 
ATOM   7697  N  NZ    . LYS B 1 266 ? 113.164 124.076 139.452 1.00 50.51 1  266 LYS B NZ    1 
ATOM   7698  N  N     . ILE B 1 267 ? 120.351 121.957 142.079 1.00 58.24 ?  267 ILE B N     1 
ATOM   7699  C  CA    . ILE B 1 267 ? 121.434 120.988 141.949 1.00 60.88 ?  267 ILE B CA    1 
ATOM   7700  C  C     . ILE B 1 267 ? 121.385 120.304 140.590 1.00 62.41 ?  267 ILE B C     1 
ATOM   7701  O  O     . ILE B 1 267 ? 122.420 119.885 140.058 1.00 61.60 ?  267 ILE B O     1 
ATOM   7702  C  CB    . ILE B 1 267 ? 121.385 119.961 143.095 1.00 62.07 ?  267 ILE B CB    1 
ATOM   7703  C  CG1   . ILE B 1 267 ? 121.647 120.635 144.444 1.00 61.89 ?  267 ILE B CG1   1 
ATOM   7704  C  CG2   . ILE B 1 267 ? 122.392 118.848 142.857 1.00 58.67 ?  267 ILE B CG2   1 
ATOM   7705  C  CD1   . ILE B 1 267 ? 120.393 120.922 145.245 1.00 60.76 ?  267 ILE B CD1   1 
ATOM   7706  N  N     . SER B 1 268 ? 120.196 120.181 140.006 1.00 63.05 ?  268 SER B N     1 
ATOM   7707  C  CA    . SER B 1 268 ? 120.012 119.559 138.703 1.00 64.65 ?  268 SER B CA    1 
ATOM   7708  C  C     . SER B 1 268 ? 120.092 120.558 137.555 1.00 65.97 ?  268 SER B C     1 
ATOM   7709  O  O     . SER B 1 268 ? 119.721 120.217 136.428 1.00 65.58 ?  268 SER B O     1 
ATOM   7710  C  CB    . SER B 1 268 ? 118.668 118.828 138.655 1.00 66.48 ?  268 SER B CB    1 
ATOM   7711  O  OG    . SER B 1 268 ? 117.608 119.699 139.009 1.00 61.93 ?  268 SER B OG    1 
ATOM   7712  N  N     . ALA B 1 269 ? 120.555 121.779 137.817 1.00 70.03 ?  269 ALA B N     1 
ATOM   7713  C  CA    . ALA B 1 269 ? 120.564 122.812 136.791 1.00 70.26 ?  269 ALA B CA    1 
ATOM   7714  C  C     . ALA B 1 269 ? 121.517 122.453 135.658 1.00 71.13 ?  269 ALA B C     1 
ATOM   7715  O  O     . ALA B 1 269 ? 122.605 121.914 135.882 1.00 68.97 ?  269 ALA B O     1 
ATOM   7716  C  CB    . ALA B 1 269 ? 120.958 124.159 137.399 1.00 66.54 ?  269 ALA B CB    1 
ATOM   7717  N  N     . ASP B 1 270 ? 121.096 122.753 134.433 1.00 74.02 ?  270 ASP B N     1 
ATOM   7718  C  CA    . ASP B 1 270 ? 121.936 122.533 133.266 1.00 74.33 ?  270 ASP B CA    1 
ATOM   7719  C  C     . ASP B 1 270 ? 123.149 123.457 133.302 1.00 73.93 ?  270 ASP B C     1 
ATOM   7720  O  O     . ASP B 1 270 ? 123.103 124.560 133.855 1.00 75.43 ?  270 ASP B O     1 
ATOM   7721  C  CB    . ASP B 1 270 ? 121.136 122.762 131.985 1.00 73.65 ?  270 ASP B CB    1 
ATOM   7722  C  CG    . ASP B 1 270 ? 121.738 122.058 130.784 1.00 76.84 ?  270 ASP B CG    1 
ATOM   7723  O  OD1   . ASP B 1 270 ? 122.922 122.308 130.474 1.00 75.94 ?  270 ASP B OD1   1 
ATOM   7724  O  OD2   . ASP B 1 270 ? 121.025 121.255 130.146 1.00 75.61 -1 270 ASP B OD2   1 
ATOM   7725  N  N     . GLU B 1 271 ? 124.249 122.993 132.703 1.00 74.27 ?  271 GLU B N     1 
ATOM   7726  C  CA    . GLU B 1 271 ? 125.486 123.764 132.720 1.00 75.67 ?  271 GLU B CA    1 
ATOM   7727  C  C     . GLU B 1 271 ? 125.380 125.063 131.933 1.00 73.53 ?  271 GLU B C     1 
ATOM   7728  O  O     . GLU B 1 271 ? 126.182 125.975 132.159 1.00 73.03 ?  271 GLU B O     1 
ATOM   7729  C  CB    . GLU B 1 271 ? 126.640 122.919 132.177 1.00 73.87 ?  271 GLU B CB    1 
ATOM   7730  C  CG    . GLU B 1 271 ? 127.060 121.786 133.099 1.00 73.21 ?  271 GLU B CG    1 
ATOM   7731  C  CD    . GLU B 1 271 ? 127.600 122.283 134.426 1.00 75.05 ?  271 GLU B CD    1 
ATOM   7732  O  OE1   . GLU B 1 271 ? 128.299 123.318 134.438 1.00 75.43 ?  271 GLU B OE1   1 
ATOM   7733  O  OE2   . GLU B 1 271 ? 127.323 121.640 135.460 1.00 74.89 -1 271 GLU B OE2   1 
ATOM   7734  N  N     . ASP B 1 272 ? 124.419 125.173 131.018 1.00 69.75 ?  272 ASP B N     1 
ATOM   7735  C  CA    . ASP B 1 272 ? 124.170 126.425 130.317 1.00 71.73 ?  272 ASP B CA    1 
ATOM   7736  C  C     . ASP B 1 272 ? 123.218 127.340 131.075 1.00 70.44 ?  272 ASP B C     1 
ATOM   7737  O  O     . ASP B 1 272 ? 122.914 128.435 130.592 1.00 66.88 ?  272 ASP B O     1 
ATOM   7738  C  CB    . ASP B 1 272 ? 123.626 126.150 128.907 1.00 70.85 ?  272 ASP B CB    1 
ATOM   7739  C  CG    . ASP B 1 272 ? 122.173 125.710 128.911 1.00 73.30 ?  272 ASP B CG    1 
ATOM   7740  O  OD1   . ASP B 1 272 ? 121.735 125.083 129.896 1.00 72.91 ?  272 ASP B OD1   1 
ATOM   7741  O  OD2   . ASP B 1 272 ? 121.467 125.994 127.920 1.00 70.51 -1 272 ASP B OD2   1 
ATOM   7742  N  N     . VAL B 1 273 ? 122.727 126.907 132.238 1.00 66.23 ?  273 VAL B N     1 
ATOM   7743  C  CA    . VAL B 1 273 ? 121.883 127.722 133.098 1.00 66.52 ?  273 VAL B CA    1 
ATOM   7744  C  C     . VAL B 1 273 ? 122.530 127.968 134.455 1.00 64.95 ?  273 VAL B C     1 
ATOM   7745  O  O     . VAL B 1 273 ? 122.441 129.074 134.999 1.00 66.14 ?  273 VAL B O     1 
ATOM   7746  C  CB    . VAL B 1 273 ? 120.489 127.081 133.272 1.00 68.18 ?  273 VAL B CB    1 
ATOM   7747  C  CG1   . VAL B 1 273 ? 119.620 127.923 134.198 1.00 62.76 ?  273 VAL B CG1   1 
ATOM   7748  C  CG2   . VAL B 1 273 ? 119.817 126.897 131.922 1.00 65.62 ?  273 VAL B CG2   1 
ATOM   7749  N  N     . ARG B 1 274 ? 123.194 126.957 135.010 1.00 62.96 ?  274 ARG B N     1 
ATOM   7750  C  CA    . ARG B 1 274 ? 123.748 127.051 136.353 1.00 61.76 ?  274 ARG B CA    1 
ATOM   7751  C  C     . ARG B 1 274 ? 124.850 128.103 136.426 1.00 62.60 ?  274 ARG B C     1 
ATOM   7752  O  O     . ARG B 1 274 ? 125.680 128.225 135.523 1.00 62.96 ?  274 ARG B O     1 
ATOM   7753  C  CB    . ARG B 1 274 ? 124.294 125.687 136.785 1.00 65.11 ?  274 ARG B CB    1 
ATOM   7754  C  CG    . ARG B 1 274 ? 125.443 125.746 137.779 1.00 62.82 ?  274 ARG B CG    1 
ATOM   7755  C  CD    . ARG B 1 274 ? 125.474 124.518 138.672 1.00 63.74 ?  274 ARG B CD    1 
ATOM   7756  N  NE    . ARG B 1 274 ? 125.880 123.323 137.943 1.00 66.77 ?  274 ARG B NE    1 
ATOM   7757  C  CZ    . ARG B 1 274 ? 125.103 122.268 137.739 1.00 68.61 ?  274 ARG B CZ    1 
ATOM   7758  N  NH1   . ARG B 1 274 ? 123.865 122.221 138.203 1.00 67.06 1  274 ARG B NH1   1 
ATOM   7759  N  NH2   . ARG B 1 274 ? 125.581 121.234 137.052 1.00 66.55 ?  274 ARG B NH2   1 
ATOM   7760  N  N     . VAL B 1 275 ? 124.844 128.868 137.516 1.00 49.50 ?  275 VAL B N     1 
ATOM   7761  C  CA    . VAL B 1 275 ? 125.909 129.810 137.845 1.00 46.65 ?  275 VAL B CA    1 
ATOM   7762  C  C     . VAL B 1 275 ? 126.550 129.352 139.148 1.00 49.29 ?  275 VAL B C     1 
ATOM   7763  O  O     . VAL B 1 275 ? 125.855 128.914 140.073 1.00 54.55 ?  275 VAL B O     1 
ATOM   7764  C  CB    . VAL B 1 275 ? 125.385 131.255 137.957 1.00 45.30 ?  275 VAL B CB    1 
ATOM   7765  C  CG1   . VAL B 1 275 ? 124.992 131.784 136.587 1.00 41.64 ?  275 VAL B CG1   1 
ATOM   7766  C  CG2   . VAL B 1 275 ? 124.207 131.329 138.909 1.00 48.00 ?  275 VAL B CG2   1 
ATOM   7767  N  N     . LYS B 1 276 ? 127.877 129.435 139.214 1.00 43.13 ?  276 LYS B N     1 
ATOM   7768  C  CA    . LYS B 1 276 ? 128.637 128.864 140.322 1.00 44.19 ?  276 LYS B CA    1 
ATOM   7769  C  C     . LYS B 1 276 ? 129.087 129.906 141.338 1.00 42.13 ?  276 LYS B C     1 
ATOM   7770  O  O     . LYS B 1 276 ? 128.910 129.709 142.543 1.00 48.13 ?  276 LYS B O     1 
ATOM   7771  C  CB    . LYS B 1 276 ? 129.865 128.094 139.803 1.00 45.94 ?  276 LYS B CB    1 
ATOM   7772  C  CG    . LYS B 1 276 ? 129.583 126.756 139.099 1.00 47.42 ?  276 LYS B CG    1 
ATOM   7773  C  CD    . LYS B 1 276 ? 128.927 126.868 137.721 1.00 48.40 ?  276 LYS B CD    1 
ATOM   7774  C  CE    . LYS B 1 276 ? 129.444 128.052 136.916 1.00 45.33 ?  276 LYS B CE    1 
ATOM   7775  N  NZ    . LYS B 1 276 ? 129.118 127.916 135.469 1.00 49.22 1  276 LYS B NZ    1 
ATOM   7776  N  N     . THR B 1 277 ? 129.670 131.009 140.881 1.00 38.02 ?  277 THR B N     1 
ATOM   7777  C  CA    . THR B 1 277 ? 130.248 132.011 141.765 1.00 39.22 ?  277 THR B CA    1 
ATOM   7778  C  C     . THR B 1 277 ? 129.347 133.221 141.961 1.00 38.73 ?  277 THR B C     1 
ATOM   7779  O  O     . THR B 1 277 ? 129.803 134.241 142.488 1.00 39.15 ?  277 THR B O     1 
ATOM   7780  C  CB    . THR B 1 277 ? 131.609 132.462 141.235 1.00 41.69 ?  277 THR B CB    1 
ATOM   7781  O  OG1   . THR B 1 277 ? 131.422 133.316 140.098 1.00 33.70 ?  277 THR B OG1   1 
ATOM   7782  C  CG2   . THR B 1 277 ? 132.443 131.258 140.834 1.00 39.64 ?  277 THR B CG2   1 
ATOM   7783  N  N     . LEU B 1 278 ? 128.085 133.136 141.552 1.00 34.18 ?  278 LEU B N     1 
ATOM   7784  C  CA    . LEU B 1 278 ? 127.154 134.257 141.620 1.00 28.24 ?  278 LEU B CA    1 
ATOM   7785  C  C     . LEU B 1 278 ? 126.046 133.916 142.607 1.00 24.52 ?  278 LEU B C     1 
ATOM   7786  O  O     . LEU B 1 278 ? 125.155 133.122 142.294 1.00 36.61 ?  278 LEU B O     1 
ATOM   7787  C  CB    . LEU B 1 278 ? 126.579 134.569 140.240 1.00 30.67 ?  278 LEU B CB    1 
ATOM   7788  C  CG    . LEU B 1 278 ? 126.046 135.984 140.014 1.00 28.70 ?  278 LEU B CG    1 
ATOM   7789  C  CD1   . LEU B 1 278 ? 127.187 136.952 139.787 1.00 24.89 ?  278 LEU B CD1   1 
ATOM   7790  C  CD2   . LEU B 1 278 ? 125.089 136.006 138.839 1.00 27.96 ?  278 LEU B CD2   1 
ATOM   7791  N  N     . SER B 1 279 ? 126.106 134.512 143.794 1.00 24.89 ?  279 SER B N     1 
ATOM   7792  C  CA    . SER B 1 279 ? 125.011 134.398 144.745 1.00 17.98 ?  279 SER B CA    1 
ATOM   7793  C  C     . SER B 1 279 ? 123.785 135.125 144.211 1.00 21.42 ?  279 SER B C     1 
ATOM   7794  O  O     . SER B 1 279 ? 123.888 136.056 143.411 1.00 30.82 ?  279 SER B O     1 
ATOM   7795  C  CB    . SER B 1 279 ? 125.414 134.977 146.098 1.00 18.46 ?  279 SER B CB    1 
ATOM   7796  O  OG    . SER B 1 279 ? 126.603 134.377 146.576 1.00 31.78 ?  279 SER B OG    1 
ATOM   7797  N  N     . ILE B 1 280 ? 122.610 134.687 144.651 1.00 19.86 ?  280 ILE B N     1 
ATOM   7798  C  CA    . ILE B 1 280 ? 121.356 135.260 144.186 1.00 20.27 ?  280 ILE B CA    1 
ATOM   7799  C  C     . ILE B 1 280 ? 120.550 135.737 145.382 1.00 12.37 ?  280 ILE B C     1 
ATOM   7800  O  O     . ILE B 1 280 ? 120.535 135.094 146.436 1.00 25.03 ?  280 ILE B O     1 
ATOM   7801  C  CB    . ILE B 1 280 ? 120.542 134.264 143.333 1.00 15.42 ?  280 ILE B CB    1 
ATOM   7802  C  CG1   . ILE B 1 280 ? 120.180 133.009 144.125 1.00 21.88 ?  280 ILE B CG1   1 
ATOM   7803  C  CG2   . ILE B 1 280 ? 121.311 133.887 142.093 1.00 16.03 ?  280 ILE B CG2   1 
ATOM   7804  C  CD1   . ILE B 1 280 ? 118.955 132.305 143.591 1.00 15.40 ?  280 ILE B CD1   1 
ATOM   7805  N  N     . GLY B 1 281 ? 119.912 136.882 145.224 1.00 6.93  ?  281 GLY B N     1 
ATOM   7806  C  CA    . GLY B 1 281 ? 118.982 137.383 146.221 1.00 6.77  ?  281 GLY B CA    1 
ATOM   7807  C  C     . GLY B 1 281 ? 117.685 137.792 145.564 1.00 4.21  ?  281 GLY B C     1 
ATOM   7808  O  O     . GLY B 1 281 ? 117.681 138.350 144.471 1.00 20.89 ?  281 GLY B O     1 
ATOM   7809  N  N     . VAL B 1 282 ? 116.580 137.499 146.241 1.00 13.07 ?  282 VAL B N     1 
ATOM   7810  C  CA    . VAL B 1 282 ? 115.247 137.809 145.741 1.00 16.12 ?  282 VAL B CA    1 
ATOM   7811  C  C     . VAL B 1 282 ? 114.679 138.956 146.562 1.00 12.86 ?  282 VAL B C     1 
ATOM   7812  O  O     . VAL B 1 282 ? 114.715 138.924 147.797 1.00 21.68 ?  282 VAL B O     1 
ATOM   7813  C  CB    . VAL B 1 282 ? 114.325 136.578 145.786 1.00 16.31 ?  282 VAL B CB    1 
ATOM   7814  C  CG1   . VAL B 1 282 ? 112.885 136.982 145.545 1.00 20.40 ?  282 VAL B CG1   1 
ATOM   7815  C  CG2   . VAL B 1 282 ? 114.758 135.574 144.745 1.00 22.87 ?  282 VAL B CG2   1 
ATOM   7816  N  N     . VAL B 1 283 ? 114.168 139.970 145.874 1.00 2.61  ?  283 VAL B N     1 
ATOM   7817  C  CA    . VAL B 1 283 ? 113.519 141.110 146.505 1.00 9.73  ?  283 VAL B CA    1 
ATOM   7818  C  C     . VAL B 1 283 ? 112.018 140.874 146.483 1.00 12.01 ?  283 VAL B C     1 
ATOM   7819  O  O     . VAL B 1 283 ? 111.431 140.652 145.418 1.00 22.77 ?  283 VAL B O     1 
ATOM   7820  C  CB    . VAL B 1 283 ? 113.886 142.421 145.791 1.00 8.36  ?  283 VAL B CB    1 
ATOM   7821  C  CG1   . VAL B 1 283 ? 113.440 143.607 146.613 1.00 10.05 ?  283 VAL B CG1   1 
ATOM   7822  C  CG2   . VAL B 1 283 ? 115.381 142.473 145.536 1.00 9.21  ?  283 VAL B CG2   1 
ATOM   7823  N  N     . ILE B 1 284 ? 111.396 140.913 147.657 1.00 16.01 ?  284 ILE B N     1 
ATOM   7824  C  CA    . ILE B 1 284 ? 109.978 140.593 147.786 1.00 17.63 ?  284 ILE B CA    1 
ATOM   7825  C  C     . ILE B 1 284 ? 109.220 141.793 148.339 1.00 21.20 ?  284 ILE B C     1 
ATOM   7826  O  O     . ILE B 1 284 ? 109.383 142.139 149.519 1.00 24.03 ?  284 ILE B O     1 
ATOM   7827  C  CB    . ILE B 1 284 ? 109.767 139.359 148.678 1.00 14.12 ?  284 ILE B CB    1 
ATOM   7828  C  CG1   . ILE B 1 284 ? 110.614 138.190 148.180 1.00 17.29 ?  284 ILE B CG1   1 
ATOM   7829  C  CG2   . ILE B 1 284 ? 108.298 138.979 148.718 1.00 15.92 ?  284 ILE B CG2   1 
ATOM   7830  C  CD1   . ILE B 1 284 ? 110.393 136.911 148.944 1.00 20.09 ?  284 ILE B CD1   1 
ATOM   7831  N  N     . PRO B 1 285 ? 108.397 142.458 147.535 1.00 20.06 ?  285 PRO B N     1 
ATOM   7832  C  CA    . PRO B 1 285 ? 107.517 143.497 148.077 1.00 29.69 ?  285 PRO B CA    1 
ATOM   7833  C  C     . PRO B 1 285 ? 106.393 142.892 148.902 1.00 28.16 ?  285 PRO B C     1 
ATOM   7834  O  O     . PRO B 1 285 ? 106.124 141.690 148.857 1.00 23.12 ?  285 PRO B O     1 
ATOM   7835  C  CB    . PRO B 1 285 ? 106.971 144.194 146.826 1.00 22.68 ?  285 PRO B CB    1 
ATOM   7836  C  CG    . PRO B 1 285 ? 107.888 143.792 145.719 1.00 20.66 ?  285 PRO B CG    1 
ATOM   7837  C  CD    . PRO B 1 285 ? 108.369 142.424 146.066 1.00 14.72 ?  285 PRO B CD    1 
ATOM   7838  N  N     . ASP B 1 286 ? 105.731 143.755 149.674 1.00 31.68 ?  286 ASP B N     1 
ATOM   7839  C  CA    . ASP B 1 286 ? 104.590 143.313 150.470 1.00 25.85 ?  286 ASP B CA    1 
ATOM   7840  C  C     . ASP B 1 286 ? 103.448 142.806 149.602 1.00 32.58 ?  286 ASP B C     1 
ATOM   7841  O  O     . ASP B 1 286 ? 102.622 142.023 150.081 1.00 36.13 ?  286 ASP B O     1 
ATOM   7842  C  CB    . ASP B 1 286 ? 104.089 144.448 151.361 1.00 27.89 ?  286 ASP B CB    1 
ATOM   7843  C  CG    . ASP B 1 286 ? 104.673 144.397 152.756 1.00 42.45 ?  286 ASP B CG    1 
ATOM   7844  O  OD1   . ASP B 1 286 ? 105.584 143.577 152.994 1.00 38.68 ?  286 ASP B OD1   1 
ATOM   7845  O  OD2   . ASP B 1 286 ? 104.226 145.184 153.617 1.00 45.98 -1 286 ASP B OD2   1 
ATOM   7846  N  N     . LYS B 1 287 ? 103.382 143.241 148.342 1.00 35.56 ?  287 LYS B N     1 
ATOM   7847  C  CA    . LYS B 1 287 ? 102.320 142.788 147.451 1.00 29.84 ?  287 LYS B CA    1 
ATOM   7848  C  C     . LYS B 1 287 ? 102.396 141.285 147.215 1.00 31.94 ?  287 LYS B C     1 
ATOM   7849  O  O     . LYS B 1 287 ? 101.368 140.602 147.189 1.00 37.47 ?  287 LYS B O     1 
ATOM   7850  C  CB    . LYS B 1 287 ? 102.393 143.541 146.123 1.00 29.52 ?  287 LYS B CB    1 
ATOM   7851  C  CG    . LYS B 1 287 ? 101.152 143.391 145.262 1.00 27.75 ?  287 LYS B CG    1 
ATOM   7852  C  CD    . LYS B 1 287 ? 99.912  143.811 146.029 1.00 34.61 ?  287 LYS B CD    1 
ATOM   7853  C  CE    . LYS B 1 287 ? 98.684  143.808 145.142 1.00 35.33 ?  287 LYS B CE    1 
ATOM   7854  N  NZ    . LYS B 1 287 ? 97.522  144.450 145.812 1.00 36.98 1  287 LYS B NZ    1 
ATOM   7855  N  N     . PHE B 1 288 ? 103.607 140.753 147.036 1.00 31.64 ?  288 PHE B N     1 
ATOM   7856  C  CA    . PHE B 1 288 ? 103.755 139.316 146.824 1.00 25.08 ?  288 PHE B CA    1 
ATOM   7857  C  C     . PHE B 1 288 ? 103.321 138.526 148.051 1.00 26.26 ?  288 PHE B C     1 
ATOM   7858  O  O     . PHE B 1 288 ? 102.653 137.492 147.927 1.00 36.76 ?  288 PHE B O     1 
ATOM   7859  C  CB    . PHE B 1 288 ? 105.200 138.987 146.458 1.00 26.32 ?  288 PHE B CB    1 
ATOM   7860  C  CG    . PHE B 1 288 ? 105.402 137.567 146.017 1.00 26.81 ?  288 PHE B CG    1 
ATOM   7861  C  CD1   . PHE B 1 288 ? 105.697 136.579 146.939 1.00 23.51 ?  288 PHE B CD1   1 
ATOM   7862  C  CD2   . PHE B 1 288 ? 105.294 137.222 144.683 1.00 24.59 ?  288 PHE B CD2   1 
ATOM   7863  C  CE1   . PHE B 1 288 ? 105.881 135.275 146.539 1.00 23.18 ?  288 PHE B CE1   1 
ATOM   7864  C  CE2   . PHE B 1 288 ? 105.480 135.920 144.277 1.00 30.28 ?  288 PHE B CE2   1 
ATOM   7865  C  CZ    . PHE B 1 288 ? 105.773 134.945 145.206 1.00 29.49 ?  288 PHE B CZ    1 
ATOM   7866  N  N     . VAL B 1 289 ? 103.699 138.989 149.242 1.00 33.44 ?  289 VAL B N     1 
ATOM   7867  C  CA    . VAL B 1 289 ? 103.307 138.297 150.463 1.00 30.03 ?  289 VAL B CA    1 
ATOM   7868  C  C     . VAL B 1 289 ? 101.799 138.375 150.655 1.00 32.62 ?  289 VAL B C     1 
ATOM   7869  O  O     . VAL B 1 289 ? 101.171 137.426 151.136 1.00 35.56 ?  289 VAL B O     1 
ATOM   7870  C  CB    . VAL B 1 289 ? 104.070 138.872 151.670 1.00 32.52 ?  289 VAL B CB    1 
ATOM   7871  C  CG1   . VAL B 1 289 ? 103.671 138.153 152.947 1.00 31.58 ?  289 VAL B CG1   1 
ATOM   7872  C  CG2   . VAL B 1 289 ? 105.568 138.769 151.442 1.00 25.79 ?  289 VAL B CG2   1 
ATOM   7873  N  N     . GLU B 1 290 ? 101.192 139.503 150.282 1.00 36.62 ?  290 GLU B N     1 
ATOM   7874  C  CA    . GLU B 1 290 ? 99.742  139.627 150.369 1.00 33.24 ?  290 GLU B CA    1 
ATOM   7875  C  C     . GLU B 1 290 ? 99.044  138.685 149.395 1.00 37.81 ?  290 GLU B C     1 
ATOM   7876  O  O     . GLU B 1 290 ? 98.021  138.079 149.734 1.00 45.39 ?  290 GLU B O     1 
ATOM   7877  C  CB    . GLU B 1 290 ? 99.327  141.075 150.111 1.00 36.09 ?  290 GLU B CB    1 
ATOM   7878  C  CG    . GLU B 1 290 ? 97.829  141.312 150.138 1.00 39.32 ?  290 GLU B CG    1 
ATOM   7879  C  CD    . GLU B 1 290 ? 97.472  142.782 150.052 1.00 48.27 ?  290 GLU B CD    1 
ATOM   7880  O  OE1   . GLU B 1 290 ? 97.908  143.446 149.089 1.00 46.35 ?  290 GLU B OE1   1 
ATOM   7881  O  OE2   . GLU B 1 290 ? 96.752  143.274 150.946 1.00 49.09 -1 290 GLU B OE2   1 
ATOM   7882  N  N     . LEU B 1 291 ? 99.578  138.554 148.178 1.00 30.84 ?  291 LEU B N     1 
ATOM   7883  C  CA    . LEU B 1 291 ? 98.986  137.645 147.201 1.00 27.61 ?  291 LEU B CA    1 
ATOM   7884  C  C     . LEU B 1 291 ? 99.123  136.194 147.639 1.00 34.77 ?  291 LEU B C     1 
ATOM   7885  O  O     . LEU B 1 291 ? 98.189  135.400 147.479 1.00 38.54 ?  291 LEU B O     1 
ATOM   7886  C  CB    . LEU B 1 291 ? 99.630  137.851 145.830 1.00 32.42 ?  291 LEU B CB    1 
ATOM   7887  C  CG    . LEU B 1 291 ? 99.375  139.193 145.144 1.00 33.84 ?  291 LEU B CG    1 
ATOM   7888  C  CD1   . LEU B 1 291 ? 100.365 139.403 144.016 1.00 26.96 ?  291 LEU B CD1   1 
ATOM   7889  C  CD2   . LEU B 1 291 ? 97.948  139.275 144.636 1.00 31.97 ?  291 LEU B CD2   1 
ATOM   7890  N  N     . ALA B 1 292 ? 100.283 135.824 148.187 1.00 41.06 ?  292 ALA B N     1 
ATOM   7891  C  CA    . ALA B 1 292 ? 100.474 134.461 148.671 1.00 31.29 ?  292 ALA B CA    1 
ATOM   7892  C  C     . ALA B 1 292 ? 99.623  134.178 149.901 1.00 31.33 ?  292 ALA B C     1 
ATOM   7893  O  O     . ALA B 1 292 ? 99.153  133.050 150.083 1.00 38.52 ?  292 ALA B O     1 
ATOM   7894  C  CB    . ALA B 1 292 ? 101.949 134.213 148.978 1.00 27.35 ?  292 ALA B CB    1 
ATOM   7895  N  N     . ARG B 1 293 ? 99.420  135.183 150.755 1.00 36.05 ?  293 ARG B N     1 
ATOM   7896  C  CA    . ARG B 1 293 ? 98.617  134.998 151.958 1.00 36.19 ?  293 ARG B CA    1 
ATOM   7897  C  C     . ARG B 1 293 ? 97.176  134.646 151.613 1.00 41.29 ?  293 ARG B C     1 
ATOM   7898  O  O     . ARG B 1 293 ? 96.575  133.766 152.239 1.00 47.95 ?  293 ARG B O     1 
ATOM   7899  C  CB    . ARG B 1 293 ? 98.677  136.264 152.812 1.00 37.33 ?  293 ARG B CB    1 
ATOM   7900  C  CG    . ARG B 1 293 ? 97.716  136.300 153.981 1.00 37.72 ?  293 ARG B CG    1 
ATOM   7901  C  CD    . ARG B 1 293 ? 97.693  137.688 154.592 1.00 38.99 ?  293 ARG B CD    1 
ATOM   7902  N  NE    . ARG B 1 293 ? 99.040  138.217 154.758 1.00 45.33 ?  293 ARG B NE    1 
ATOM   7903  C  CZ    . ARG B 1 293 ? 99.426  139.425 154.368 1.00 43.13 ?  293 ARG B CZ    1 
ATOM   7904  N  NH1   . ARG B 1 293 ? 98.584  140.267 153.793 1.00 42.09 1  293 ARG B NH1   1 
ATOM   7905  N  NH2   . ARG B 1 293 ? 100.688 139.796 154.560 1.00 40.00 ?  293 ARG B NH2   1 
ATOM   7906  N  N     . GLU B 1 294 ? 96.608  135.319 150.618 1.00 48.58 ?  294 GLU B N     1 
ATOM   7907  C  CA    . GLU B 1 294 ? 95.236  135.081 150.195 1.00 47.69 ?  294 GLU B CA    1 
ATOM   7908  C  C     . GLU B 1 294 ? 95.131  134.030 149.098 1.00 45.66 ?  294 GLU B C     1 
ATOM   7909  O  O     . GLU B 1 294 ? 94.026  133.782 148.605 1.00 48.04 ?  294 GLU B O     1 
ATOM   7910  C  CB    . GLU B 1 294 ? 94.600  136.389 149.723 1.00 44.43 ?  294 GLU B CB    1 
ATOM   7911  C  CG    . GLU B 1 294 ? 94.506  137.452 150.803 1.00 48.49 ?  294 GLU B CG    1 
ATOM   7912  C  CD    . GLU B 1 294 ? 94.581  138.856 150.241 1.00 55.04 ?  294 GLU B CD    1 
ATOM   7913  O  OE1   . GLU B 1 294 ? 94.739  138.993 149.010 1.00 56.38 ?  294 GLU B OE1   1 
ATOM   7914  O  OE2   . GLU B 1 294 ? 94.485  139.820 151.029 1.00 54.30 -1 294 GLU B OE2   1 
ATOM   7915  N  N     . ASP B 1 295 ? 96.251  133.424 148.701 1.00 44.07 ?  295 ASP B N     1 
ATOM   7916  C  CA    . ASP B 1 295 ? 96.304  132.361 147.698 1.00 43.93 ?  295 ASP B CA    1 
ATOM   7917  C  C     . ASP B 1 295 ? 95.802  132.814 146.332 1.00 49.15 ?  295 ASP B C     1 
ATOM   7918  O  O     . ASP B 1 295 ? 95.489  131.979 145.476 1.00 47.46 ?  295 ASP B O     1 
ATOM   7919  C  CB    . ASP B 1 295 ? 95.530  131.118 148.156 1.00 45.64 ?  295 ASP B CB    1 
ATOM   7920  C  CG    . ASP B 1 295 ? 96.254  129.826 147.825 1.00 52.77 ?  295 ASP B CG    1 
ATOM   7921  O  OD1   . ASP B 1 295 ? 97.164  129.855 146.972 1.00 54.24 ?  295 ASP B OD1   1 
ATOM   7922  O  OD2   . ASP B 1 295 ? 95.908  128.781 148.412 1.00 50.23 -1 295 ASP B OD2   1 
ATOM   7923  N  N     . LYS B 1 296 ? 95.713  134.122 146.103 1.00 49.66 ?  296 LYS B N     1 
ATOM   7924  C  CA    . LYS B 1 296 ? 95.368  134.620 144.780 1.00 47.19 ?  296 LYS B CA    1 
ATOM   7925  C  C     . LYS B 1 296 ? 96.514  134.361 143.813 1.00 45.50 ?  296 LYS B C     1 
ATOM   7926  O  O     . LYS B 1 296 ? 97.687  134.511 144.163 1.00 51.87 ?  296 LYS B O     1 
ATOM   7927  C  CB    . LYS B 1 296 ? 95.060  136.116 144.831 1.00 46.04 ?  296 LYS B CB    1 
ATOM   7928  C  CG    . LYS B 1 296 ? 94.525  136.600 146.164 1.00 47.76 ?  296 LYS B CG    1 
ATOM   7929  C  CD    . LYS B 1 296 ? 93.533  137.734 145.985 1.00 49.04 ?  296 LYS B CD    1 
ATOM   7930  C  CE    . LYS B 1 296 ? 92.145  137.210 145.659 1.00 51.74 ?  296 LYS B CE    1 
ATOM   7931  N  NZ    . LYS B 1 296 ? 91.596  136.368 146.758 1.00 50.32 1  296 LYS B NZ    1 
ATOM   7932  N  N     . ALA B 1 297 ? 96.174  133.967 142.590 1.00 45.38 ?  297 ALA B N     1 
ATOM   7933  C  CA    . ALA B 1 297 ? 97.193  133.732 141.579 1.00 46.15 ?  297 ALA B CA    1 
ATOM   7934  C  C     . ALA B 1 297 ? 97.839  135.053 141.177 1.00 45.62 ?  297 ALA B C     1 
ATOM   7935  O  O     . ALA B 1 297 ? 97.146  136.022 140.852 1.00 53.38 ?  297 ALA B O     1 
ATOM   7936  C  CB    . ALA B 1 297 ? 96.586  133.039 140.363 1.00 44.20 ?  297 ALA B CB    1 
ATOM   7937  N  N     . ALA B 1 298 ? 99.166  135.090 141.202 1.00 38.81 ?  298 ALA B N     1 
ATOM   7938  C  CA    . ALA B 1 298 ? 99.921  136.313 140.985 1.00 39.74 ?  298 ALA B CA    1 
ATOM   7939  C  C     . ALA B 1 298 ? 100.444 136.384 139.557 1.00 37.91 ?  298 ALA B C     1 
ATOM   7940  O  O     . ALA B 1 298 ? 100.400 135.415 138.796 1.00 41.21 ?  298 ALA B O     1 
ATOM   7941  C  CB    . ALA B 1 298 ? 101.078 136.413 141.982 1.00 42.58 ?  298 ALA B CB    1 
ATOM   7942  N  N     . TYR B 1 299 ? 100.953 137.559 139.201 1.00 38.47 ?  299 TYR B N     1 
ATOM   7943  C  CA    . TYR B 1 299 ? 101.484 137.830 137.873 1.00 31.67 ?  299 TYR B CA    1 
ATOM   7944  C  C     . TYR B 1 299 ? 102.912 138.338 137.988 1.00 33.77 ?  299 TYR B C     1 
ATOM   7945  O  O     . TYR B 1 299 ? 103.196 139.225 138.799 1.00 41.45 ?  299 TYR B O     1 
ATOM   7946  C  CB    . TYR B 1 299 ? 100.626 138.864 137.140 1.00 32.93 ?  299 TYR B CB    1 
ATOM   7947  C  CG    . TYR B 1 299 ? 99.349  138.313 136.554 1.00 35.07 ?  299 TYR B CG    1 
ATOM   7948  C  CD1   . TYR B 1 299 ? 99.377  137.465 135.457 1.00 37.58 ?  299 TYR B CD1   1 
ATOM   7949  C  CD2   . TYR B 1 299 ? 98.116  138.645 137.095 1.00 36.23 ?  299 TYR B CD2   1 
ATOM   7950  C  CE1   . TYR B 1 299 ? 98.213  136.963 134.917 1.00 41.02 ?  299 TYR B CE1   1 
ATOM   7951  C  CE2   . TYR B 1 299 ? 96.947  138.148 136.563 1.00 39.48 ?  299 TYR B CE2   1 
ATOM   7952  C  CZ    . TYR B 1 299 ? 97.000  137.308 135.474 1.00 44.62 ?  299 TYR B CZ    1 
ATOM   7953  O  OH    . TYR B 1 299 ? 95.835  136.810 134.938 1.00 45.44 ?  299 TYR B OH    1 
ATOM   7954  N  N     . VAL B 1 300 ? 103.804 137.776 137.182 1.00 32.57 ?  300 VAL B N     1 
ATOM   7955  C  CA    . VAL B 1 300 ? 105.138 138.328 136.979 1.00 28.85 ?  300 VAL B CA    1 
ATOM   7956  C  C     . VAL B 1 300 ? 105.129 139.070 135.654 1.00 27.75 ?  300 VAL B C     1 
ATOM   7957  O  O     . VAL B 1 300 ? 104.490 138.633 134.691 1.00 32.37 ?  300 VAL B O     1 
ATOM   7958  C  CB    . VAL B 1 300 ? 106.221 137.232 137.006 1.00 24.24 ?  300 VAL B CB    1 
ATOM   7959  C  CG1   . VAL B 1 300 ? 106.478 136.785 138.433 1.00 26.78 ?  300 VAL B CG1   1 
ATOM   7960  C  CG2   . VAL B 1 300 ? 105.815 136.058 136.136 1.00 31.98 ?  300 VAL B CG2   1 
ATOM   7961  N  N     . PHE B 1 301 ? 105.827 140.197 135.600 1.00 30.11 ?  301 PHE B N     1 
ATOM   7962  C  CA    . PHE B 1 301 ? 105.691 141.132 134.496 1.00 23.39 ?  301 PHE B CA    1 
ATOM   7963  C  C     . PHE B 1 301 ? 106.982 141.227 133.699 1.00 31.95 ?  301 PHE B C     1 
ATOM   7964  O  O     . PHE B 1 301 ? 108.081 141.074 134.240 1.00 33.95 ?  301 PHE B O     1 
ATOM   7965  C  CB    . PHE B 1 301 ? 105.299 142.519 135.005 1.00 24.46 ?  301 PHE B CB    1 
ATOM   7966  C  CG    . PHE B 1 301 ? 104.123 142.507 135.934 1.00 31.13 ?  301 PHE B CG    1 
ATOM   7967  C  CD1   . PHE B 1 301 ? 102.833 142.519 135.439 1.00 28.85 ?  301 PHE B CD1   1 
ATOM   7968  C  CD2   . PHE B 1 301 ? 104.310 142.470 137.304 1.00 27.61 ?  301 PHE B CD2   1 
ATOM   7969  C  CE1   . PHE B 1 301 ? 101.751 142.501 136.291 1.00 30.97 ?  301 PHE B CE1   1 
ATOM   7970  C  CE2   . PHE B 1 301 ? 103.231 142.452 138.159 1.00 28.61 ?  301 PHE B CE2   1 
ATOM   7971  C  CZ    . PHE B 1 301 ? 101.950 142.469 137.652 1.00 33.66 ?  301 PHE B CZ    1 
ATOM   7972  N  N     . TYR B 1 302 ? 106.832 141.475 132.404 1.00 31.27 ?  302 TYR B N     1 
ATOM   7973  C  CA    . TYR B 1 302 ? 107.975 141.770 131.555 1.00 28.12 ?  302 TYR B CA    1 
ATOM   7974  C  C     . TYR B 1 302 ? 108.374 143.225 131.762 1.00 29.09 ?  302 TYR B C     1 
ATOM   7975  O  O     . TYR B 1 302 ? 107.576 144.121 131.469 1.00 32.21 ?  302 TYR B O     1 
ATOM   7976  C  CB    . TYR B 1 302 ? 107.640 141.513 130.091 1.00 29.30 ?  302 TYR B CB    1 
ATOM   7977  C  CG    . TYR B 1 302 ? 107.437 140.055 129.743 1.00 31.34 ?  302 TYR B CG    1 
ATOM   7978  C  CD1   . TYR B 1 302 ? 106.272 139.390 130.100 1.00 30.03 ?  302 TYR B CD1   1 
ATOM   7979  C  CD2   . TYR B 1 302 ? 108.408 139.344 129.052 1.00 29.42 ?  302 TYR B CD2   1 
ATOM   7980  C  CE1   . TYR B 1 302 ? 106.082 138.061 129.781 1.00 30.43 ?  302 TYR B CE1   1 
ATOM   7981  C  CE2   . TYR B 1 302 ? 108.227 138.015 128.732 1.00 31.36 ?  302 TYR B CE2   1 
ATOM   7982  C  CZ    . TYR B 1 302 ? 107.062 137.379 129.098 1.00 34.48 ?  302 TYR B CZ    1 
ATOM   7983  O  OH    . TYR B 1 302 ? 106.875 136.054 128.781 1.00 34.45 ?  302 TYR B OH    1 
ATOM   7984  N  N     . PRO B 1 303 ? 109.575 143.503 132.274 1.00 26.70 ?  303 PRO B N     1 
ATOM   7985  C  CA    . PRO B 1 303 ? 109.911 144.888 132.644 1.00 30.11 ?  303 PRO B CA    1 
ATOM   7986  C  C     . PRO B 1 303 ? 109.901 145.868 131.485 1.00 28.10 ?  303 PRO B C     1 
ATOM   7987  O  O     . PRO B 1 303 ? 109.561 147.041 131.688 1.00 33.19 ?  303 PRO B O     1 
ATOM   7988  C  CB    . PRO B 1 303 ? 111.315 144.750 133.248 1.00 29.93 ?  303 PRO B CB    1 
ATOM   7989  C  CG    . PRO B 1 303 ? 111.386 143.344 133.705 1.00 27.96 ?  303 PRO B CG    1 
ATOM   7990  C  CD    . PRO B 1 303 ? 110.615 142.553 132.698 1.00 23.22 ?  303 PRO B CD    1 
ATOM   7991  N  N     . HIS B 1 304 ? 110.270 145.437 130.278 1.00 29.44 ?  304 HIS B N     1 
ATOM   7992  C  CA    . HIS B 1 304 ? 110.348 146.383 129.171 1.00 27.98 ?  304 HIS B CA    1 
ATOM   7993  C  C     . HIS B 1 304 ? 108.970 146.863 128.739 1.00 34.11 ?  304 HIS B C     1 
ATOM   7994  O  O     . HIS B 1 304 ? 108.825 148.014 128.321 1.00 41.97 ?  304 HIS B O     1 
ATOM   7995  C  CB    . HIS B 1 304 ? 111.090 145.770 127.986 1.00 29.58 ?  304 HIS B CB    1 
ATOM   7996  C  CG    . HIS B 1 304 ? 111.466 146.769 126.937 1.00 33.21 ?  304 HIS B CG    1 
ATOM   7997  N  ND1   . HIS B 1 304 ? 112.087 147.962 127.238 1.00 33.55 ?  304 HIS B ND1   1 
ATOM   7998  C  CD2   . HIS B 1 304 ? 111.300 146.759 125.595 1.00 34.93 ?  304 HIS B CD2   1 
ATOM   7999  C  CE1   . HIS B 1 304 ? 112.293 148.642 126.125 1.00 32.26 ?  304 HIS B CE1   1 
ATOM   8000  N  NE2   . HIS B 1 304 ? 111.824 147.934 125.113 1.00 34.44 ?  304 HIS B NE2   1 
ATOM   8001  N  N     . THR B 1 305 ? 107.951 146.007 128.834 1.00 33.07 ?  305 THR B N     1 
ATOM   8002  C  CA    . THR B 1 305 ? 106.593 146.454 128.543 1.00 32.53 ?  305 THR B CA    1 
ATOM   8003  C  C     . THR B 1 305 ? 106.153 147.535 129.522 1.00 29.67 ?  305 THR B C     1 
ATOM   8004  O  O     . THR B 1 305 ? 105.538 148.531 129.124 1.00 35.87 ?  305 THR B O     1 
ATOM   8005  C  CB    . THR B 1 305 ? 105.630 145.269 128.580 1.00 31.15 ?  305 THR B CB    1 
ATOM   8006  O  OG1   . THR B 1 305 ? 105.497 144.802 129.927 1.00 29.56 ?  305 THR B OG1   1 
ATOM   8007  C  CG2   . THR B 1 305 ? 106.151 144.142 127.709 1.00 31.52 ?  305 THR B CG2   1 
ATOM   8008  N  N     . ILE B 1 306 ? 106.472 147.360 130.805 1.00 35.97 ?  306 ILE B N     1 
ATOM   8009  C  CA    . ILE B 1 306 ? 106.137 148.367 131.805 1.00 29.61 ?  306 ILE B CA    1 
ATOM   8010  C  C     . ILE B 1 306 ? 106.893 149.662 131.534 1.00 28.38 ?  306 ILE B C     1 
ATOM   8011  O  O     . ILE B 1 306 ? 106.331 150.759 131.638 1.00 35.85 ?  306 ILE B O     1 
ATOM   8012  C  CB    . ILE B 1 306 ? 106.421 147.825 133.216 1.00 27.13 ?  306 ILE B CB    1 
ATOM   8013  C  CG1   . ILE B 1 306 ? 105.348 146.812 133.614 1.00 27.32 ?  306 ILE B CG1   1 
ATOM   8014  C  CG2   . ILE B 1 306 ? 106.497 148.957 134.229 1.00 30.70 ?  306 ILE B CG2   1 
ATOM   8015  C  CD1   . ILE B 1 306 ? 105.624 146.116 134.912 1.00 29.91 ?  306 ILE B CD1   1 
ATOM   8016  N  N     . TYR B 1 307 ? 108.175 149.555 131.181 1.00 30.49 ?  307 TYR B N     1 
ATOM   8017  C  CA    . TYR B 1 307 ? 108.961 150.747 130.880 1.00 31.96 ?  307 TYR B CA    1 
ATOM   8018  C  C     . TYR B 1 307 ? 108.408 151.486 129.668 1.00 35.66 ?  307 TYR B C     1 
ATOM   8019  O  O     . TYR B 1 307 ? 108.368 152.720 129.647 1.00 39.51 ?  307 TYR B O     1 
ATOM   8020  C  CB    . TYR B 1 307 ? 110.424 150.368 130.655 1.00 26.23 ?  307 TYR B CB    1 
ATOM   8021  C  CG    . TYR B 1 307 ? 111.323 151.553 130.409 1.00 35.96 ?  307 TYR B CG    1 
ATOM   8022  C  CD1   . TYR B 1 307 ? 111.758 152.346 131.461 1.00 31.13 ?  307 TYR B CD1   1 
ATOM   8023  C  CD2   . TYR B 1 307 ? 111.731 151.885 129.126 1.00 37.14 ?  307 TYR B CD2   1 
ATOM   8024  C  CE1   . TYR B 1 307 ? 112.577 153.432 131.241 1.00 31.45 ?  307 TYR B CE1   1 
ATOM   8025  C  CE2   . TYR B 1 307 ? 112.549 152.969 128.897 1.00 36.70 ?  307 TYR B CE2   1 
ATOM   8026  C  CZ    . TYR B 1 307 ? 112.970 153.740 129.957 1.00 37.64 ?  307 TYR B CZ    1 
ATOM   8027  O  OH    . TYR B 1 307 ? 113.787 154.822 129.732 1.00 40.14 ?  307 TYR B OH    1 
ATOM   8028  N  N     . LYS B 1 308 ? 107.988 150.745 128.641 1.00 39.05 ?  308 LYS B N     1 
ATOM   8029  C  CA    . LYS B 1 308 ? 107.417 151.374 127.455 1.00 32.40 ?  308 LYS B CA    1 
ATOM   8030  C  C     . LYS B 1 308 ? 106.071 152.018 127.761 1.00 28.74 ?  308 LYS B C     1 
ATOM   8031  O  O     . LYS B 1 308 ? 105.756 153.090 127.231 1.00 37.26 ?  308 LYS B O     1 
ATOM   8032  C  CB    . LYS B 1 308 ? 107.273 150.341 126.339 1.00 32.55 ?  308 LYS B CB    1 
ATOM   8033  C  CG    . LYS B 1 308 ? 108.493 150.220 125.442 1.00 33.55 ?  308 LYS B CG    1 
ATOM   8034  C  CD    . LYS B 1 308 ? 108.572 148.850 124.779 1.00 37.52 ?  308 LYS B CD    1 
ATOM   8035  C  CE    . LYS B 1 308 ? 107.199 148.215 124.616 1.00 38.18 ?  308 LYS B CE    1 
ATOM   8036  N  NZ    . LYS B 1 308 ? 107.272 146.730 124.558 1.00 39.44 1  308 LYS B NZ    1 
ATOM   8037  N  N     . GLU B 1 309 ? 105.266 151.381 128.611 1.00 30.88 ?  309 GLU B N     1 
ATOM   8038  C  CA    . GLU B 1 309 ? 103.931 151.900 128.888 1.00 35.01 ?  309 GLU B CA    1 
ATOM   8039  C  C     . GLU B 1 309 ? 103.975 153.122 129.797 1.00 39.29 ?  309 GLU B C     1 
ATOM   8040  O  O     . GLU B 1 309 ? 103.223 154.081 129.590 1.00 42.53 ?  309 GLU B O     1 
ATOM   8041  C  CB    . GLU B 1 309 ? 103.066 150.802 129.506 1.00 31.66 ?  309 GLU B CB    1 
ATOM   8042  C  CG    . GLU B 1 309 ? 101.681 151.260 129.926 1.00 37.92 ?  309 GLU B CG    1 
ATOM   8043  C  CD    . GLU B 1 309 ? 100.808 151.655 128.753 1.00 44.26 ?  309 GLU B CD    1 
ATOM   8044  O  OE1   . GLU B 1 309 ? 101.158 151.318 127.603 1.00 44.90 ?  309 GLU B OE1   1 
ATOM   8045  O  OE2   . GLU B 1 309 ? 99.768  152.308 128.983 1.00 42.88 -1 309 GLU B OE2   1 
ATOM   8046  N  N     . TYR B 1 310 ? 104.845 153.113 130.807 1.00 38.41 ?  310 TYR B N     1 
ATOM   8047  C  CA    . TYR B 1 310 ? 104.832 154.144 131.834 1.00 32.71 ?  310 TYR B CA    1 
ATOM   8048  C  C     . TYR B 1 310 ? 106.056 155.048 131.822 1.00 31.48 ?  310 TYR B C     1 
ATOM   8049  O  O     . TYR B 1 310 ? 106.064 156.051 132.542 1.00 37.24 ?  310 TYR B O     1 
ATOM   8050  C  CB    . TYR B 1 310 ? 104.696 153.501 133.221 1.00 34.92 ?  310 TYR B CB    1 
ATOM   8051  C  CG    . TYR B 1 310 ? 103.451 152.661 133.375 1.00 35.19 ?  310 TYR B CG    1 
ATOM   8052  C  CD1   . TYR B 1 310 ? 102.230 153.246 133.682 1.00 31.87 ?  310 TYR B CD1   1 
ATOM   8053  C  CD2   . TYR B 1 310 ? 103.491 151.286 133.198 1.00 30.33 ?  310 TYR B CD2   1 
ATOM   8054  C  CE1   . TYR B 1 310 ? 101.089 152.485 133.816 1.00 34.98 ?  310 TYR B CE1   1 
ATOM   8055  C  CE2   . TYR B 1 310 ? 102.354 150.518 133.328 1.00 31.20 ?  310 TYR B CE2   1 
ATOM   8056  C  CZ    . TYR B 1 310 ? 101.158 151.121 133.640 1.00 35.71 ?  310 TYR B CZ    1 
ATOM   8057  O  OH    . TYR B 1 310 ? 100.022 150.359 133.772 1.00 36.16 ?  310 TYR B OH    1 
ATOM   8058  N  N     . GLY B 1 311 ? 107.080 154.729 131.037 1.00 27.99 ?  311 GLY B N     1 
ATOM   8059  C  CA    . GLY B 1 311 ? 108.295 155.513 131.051 1.00 30.48 ?  311 GLY B CA    1 
ATOM   8060  C  C     . GLY B 1 311 ? 109.156 155.327 132.278 1.00 31.62 ?  311 GLY B C     1 
ATOM   8061  O  O     . GLY B 1 311 ? 110.177 156.011 132.406 1.00 40.98 ?  311 GLY B O     1 
ATOM   8062  N  N     . GLN B 1 312 ? 108.777 154.429 133.182 1.00 31.69 ?  312 GLN B N     1 
ATOM   8063  C  CA    . GLN B 1 312 ? 109.533 154.152 134.391 1.00 30.03 ?  312 GLN B CA    1 
ATOM   8064  C  C     . GLN B 1 312 ? 109.781 152.656 134.488 1.00 31.15 ?  312 GLN B C     1 
ATOM   8065  O  O     . GLN B 1 312 ? 108.974 151.847 134.024 1.00 39.00 ?  312 GLN B O     1 
ATOM   8066  C  CB    . GLN B 1 312 ? 108.793 154.633 135.644 1.00 34.29 ?  312 GLN B CB    1 
ATOM   8067  C  CG    . GLN B 1 312 ? 108.404 156.096 135.616 1.00 37.13 ?  312 GLN B CG    1 
ATOM   8068  C  CD    . GLN B 1 312 ? 107.340 156.428 136.641 1.00 39.55 ?  312 GLN B CD    1 
ATOM   8069  O  OE1   . GLN B 1 312 ? 106.161 156.552 136.310 1.00 38.28 ?  312 GLN B OE1   1 
ATOM   8070  N  NE2   . GLN B 1 312 ? 107.751 156.571 137.894 1.00 37.71 ?  312 GLN B NE2   1 
ATOM   8071  N  N     . HIS B 1 313 ? 110.909 152.297 135.092 1.00 28.09 ?  313 HIS B N     1 
ATOM   8072  C  CA    . HIS B 1 313 ? 111.221 150.893 135.306 1.00 28.27 ?  313 HIS B CA    1 
ATOM   8073  C  C     . HIS B 1 313 ? 110.251 150.279 136.307 1.00 32.03 ?  313 HIS B C     1 
ATOM   8074  O  O     . HIS B 1 313 ? 109.724 150.956 137.192 1.00 34.17 ?  313 HIS B O     1 
ATOM   8075  C  CB    . HIS B 1 313 ? 112.658 150.735 135.800 1.00 26.18 ?  313 HIS B CB    1 
ATOM   8076  C  CG    . HIS B 1 313 ? 113.689 151.085 134.775 1.00 27.23 ?  313 HIS B CG    1 
ATOM   8077  N  ND1   . HIS B 1 313 ? 113.951 150.288 133.682 1.00 30.43 ?  313 HIS B ND1   1 
ATOM   8078  C  CD2   . HIS B 1 313 ? 114.527 152.144 134.678 1.00 28.25 ?  313 HIS B CD2   1 
ATOM   8079  C  CE1   . HIS B 1 313 ? 114.906 150.842 132.955 1.00 27.83 ?  313 HIS B CE1   1 
ATOM   8080  N  NE2   . HIS B 1 313 ? 115.272 151.968 133.538 1.00 32.42 ?  313 HIS B NE2   1 
ATOM   8081  N  N     . MET B 1 314 ? 110.014 148.976 136.152 1.00 34.99 ?  314 MET B N     1 
ATOM   8082  C  CA    . MET B 1 314 ? 109.074 148.287 137.030 1.00 29.03 ?  314 MET B CA    1 
ATOM   8083  C  C     . MET B 1 314 ? 109.557 148.307 138.475 1.00 34.23 ?  314 MET B C     1 
ATOM   8084  O  O     . MET B 1 314 ? 108.755 148.466 139.403 1.00 38.94 ?  314 MET B O     1 
ATOM   8085  C  CB    . MET B 1 314 ? 108.860 146.853 136.543 1.00 26.60 ?  314 MET B CB    1 
ATOM   8086  C  CG    . MET B 1 314 ? 108.280 145.909 137.577 1.00 27.15 ?  314 MET B CG    1 
ATOM   8087  S  SD    . MET B 1 314 ? 108.613 144.182 137.187 1.00 43.44 ?  314 MET B SD    1 
ATOM   8088  C  CE    . MET B 1 314 ? 110.259 143.992 137.866 1.00 34.29 ?  314 MET B CE    1 
ATOM   8089  N  N     . ASP B 1 315 ? 110.864 148.156 138.689 1.00 34.31 ?  315 ASP B N     1 
ATOM   8090  C  CA    . ASP B 1 315 ? 111.413 148.207 140.037 1.00 34.44 ?  315 ASP B CA    1 
ATOM   8091  C  C     . ASP B 1 315 ? 111.564 149.627 140.572 1.00 28.83 ?  315 ASP B C     1 
ATOM   8092  O  O     . ASP B 1 315 ? 111.869 149.795 141.757 1.00 38.87 ?  315 ASP B O     1 
ATOM   8093  C  CB    . ASP B 1 315 ? 112.744 147.430 140.088 1.00 29.64 ?  315 ASP B CB    1 
ATOM   8094  C  CG    . ASP B 1 315 ? 113.953 148.231 139.595 1.00 33.54 ?  315 ASP B CG    1 
ATOM   8095  O  OD1   . ASP B 1 315 ? 113.831 149.391 139.154 1.00 40.00 ?  315 ASP B OD1   1 
ATOM   8096  O  OD2   . ASP B 1 315 ? 115.068 147.671 139.661 1.00 35.00 -1 315 ASP B OD2   1 
ATOM   8097  N  N     . GLU B 1 316 ? 111.357 150.642 139.735 1.00 24.99 ?  316 GLU B N     1 
ATOM   8098  C  CA    . GLU B 1 316 ? 111.336 152.027 140.186 1.00 27.13 ?  316 GLU B CA    1 
ATOM   8099  C  C     . GLU B 1 316 ? 109.972 152.459 140.702 1.00 35.65 ?  316 GLU B C     1 
ATOM   8100  O  O     . GLU B 1 316 ? 109.850 153.575 141.219 1.00 35.99 ?  316 GLU B O     1 
ATOM   8101  C  CB    . GLU B 1 316 ? 111.762 152.956 139.048 1.00 31.43 ?  316 GLU B CB    1 
ATOM   8102  C  CG    . GLU B 1 316 ? 112.714 154.057 139.466 1.00 34.63 ?  316 GLU B CG    1 
ATOM   8103  C  CD    . GLU B 1 316 ? 114.088 153.536 139.808 1.00 39.24 ?  316 GLU B CD    1 
ATOM   8104  O  OE1   . GLU B 1 316 ? 114.518 152.546 139.182 1.00 40.91 ?  316 GLU B OE1   1 
ATOM   8105  O  OE2   . GLU B 1 316 ? 114.740 154.116 140.700 1.00 38.33 -1 316 GLU B OE2   1 
ATOM   8106  N  N     . MET B 1 317 ? 108.954 151.615 140.579 1.00 38.87 ?  317 MET B N     1 
ATOM   8107  C  CA    . MET B 1 317 ? 107.591 151.956 140.948 1.00 34.88 ?  317 MET B CA    1 
ATOM   8108  C  C     . MET B 1 317 ? 107.133 151.122 142.137 1.00 38.69 ?  317 MET B C     1 
ATOM   8109  O  O     . MET B 1 317 ? 107.658 150.040 142.410 1.00 39.26 ?  317 MET B O     1 
ATOM   8110  C  CB    . MET B 1 317 ? 106.641 151.749 139.764 1.00 35.43 ?  317 MET B CB    1 
ATOM   8111  C  CG    . MET B 1 317 ? 107.125 152.389 138.475 1.00 37.07 ?  317 MET B CG    1 
ATOM   8112  S  SD    . MET B 1 317 ? 106.480 151.579 137.004 1.00 48.33 ?  317 MET B SD    1 
ATOM   8113  C  CE    . MET B 1 317 ? 105.014 152.560 136.711 1.00 39.01 ?  317 MET B CE    1 
ATOM   8114  N  N     . ASP B 1 318 ? 106.135 151.646 142.844 1.00 40.07 ?  318 ASP B N     1 
ATOM   8115  C  CA    . ASP B 1 318 ? 105.587 150.983 144.021 1.00 37.58 ?  318 ASP B CA    1 
ATOM   8116  C  C     . ASP B 1 318 ? 104.630 149.888 143.568 1.00 42.08 ?  318 ASP B C     1 
ATOM   8117  O  O     . ASP B 1 318 ? 103.553 150.177 143.038 1.00 44.38 ?  318 ASP B O     1 
ATOM   8118  C  CB    . ASP B 1 318 ? 104.881 151.995 144.920 1.00 39.27 ?  318 ASP B CB    1 
ATOM   8119  C  CG    . ASP B 1 318 ? 104.444 151.397 146.240 1.00 49.10 ?  318 ASP B CG    1 
ATOM   8120  O  OD1   . ASP B 1 318 ? 105.147 150.500 146.752 1.00 46.36 ?  318 ASP B OD1   1 
ATOM   8121  O  OD2   . ASP B 1 318 ? 103.396 151.825 146.767 1.00 50.01 -1 318 ASP B OD2   1 
ATOM   8122  N  N     . MET B 1 319 ? 105.019 148.630 143.779 1.00 40.62 ?  319 MET B N     1 
ATOM   8123  C  CA    . MET B 1 319 ? 104.190 147.516 143.331 1.00 35.55 ?  319 MET B CA    1 
ATOM   8124  C  C     . MET B 1 319 ? 102.862 147.459 144.072 1.00 36.85 ?  319 MET B C     1 
ATOM   8125  O  O     . MET B 1 319 ? 101.879 146.945 143.529 1.00 42.15 ?  319 MET B O     1 
ATOM   8126  C  CB    . MET B 1 319 ? 104.942 146.197 143.498 1.00 35.05 ?  319 MET B CB    1 
ATOM   8127  C  CG    . MET B 1 319 ? 104.391 145.068 142.646 1.00 37.88 ?  319 MET B CG    1 
ATOM   8128  S  SD    . MET B 1 319 ? 104.515 145.388 140.878 1.00 47.61 ?  319 MET B SD    1 
ATOM   8129  C  CE    . MET B 1 319 ? 106.291 145.403 140.669 1.00 41.96 ?  319 MET B CE    1 
ATOM   8130  N  N     . ASN B 1 320 ? 102.804 147.992 145.293 1.00 39.09 ?  320 ASN B N     1 
ATOM   8131  C  CA    . ASN B 1 320 ? 101.560 147.952 146.054 1.00 39.65 ?  320 ASN B CA    1 
ATOM   8132  C  C     . ASN B 1 320 ? 100.458 148.742 145.360 1.00 46.07 ?  320 ASN B C     1 
ATOM   8133  O  O     . ASN B 1 320 ? 99.297  148.316 145.340 1.00 46.18 ?  320 ASN B O     1 
ATOM   8134  C  CB    . ASN B 1 320 ? 101.797 148.479 147.469 1.00 40.73 ?  320 ASN B CB    1 
ATOM   8135  C  CG    . ASN B 1 320 ? 102.837 147.671 148.221 1.00 43.14 ?  320 ASN B CG    1 
ATOM   8136  O  OD1   . ASN B 1 320 ? 102.620 146.504 148.539 1.00 42.76 ?  320 ASN B OD1   1 
ATOM   8137  N  ND2   . ASN B 1 320 ? 103.975 148.292 148.506 1.00 43.71 ?  320 ASN B ND2   1 
ATOM   8138  N  N     . GLU B 1 321 ? 100.799 149.892 144.782 1.00 46.25 ?  321 GLU B N     1 
ATOM   8139  C  CA    . GLU B 1 321 ? 99.822  150.683 144.046 1.00 44.91 ?  321 GLU B CA    1 
ATOM   8140  C  C     . GLU B 1 321 ? 99.806  150.369 142.557 1.00 43.62 ?  321 GLU B C     1 
ATOM   8141  O  O     . GLU B 1 321 ? 98.772  150.553 141.904 1.00 45.23 ?  321 GLU B O     1 
ATOM   8142  C  CB    . GLU B 1 321 ? 100.091 152.178 144.242 1.00 43.47 ?  321 GLU B CB    1 
ATOM   8143  C  CG    . GLU B 1 321 ? 101.449 152.636 143.740 1.00 47.11 ?  321 GLU B CG    1 
ATOM   8144  C  CD    . GLU B 1 321 ? 101.402 154.011 143.102 1.00 51.86 ?  321 GLU B CD    1 
ATOM   8145  O  OE1   . GLU B 1 321 ? 100.288 154.525 142.872 1.00 49.66 ?  321 GLU B OE1   1 
ATOM   8146  O  OE2   . GLU B 1 321 ? 102.481 154.579 142.830 1.00 51.96 -1 321 GLU B OE2   1 
ATOM   8147  N  N     . MET B 1 322 ? 100.922 149.898 142.005 1.00 40.70 ?  322 MET B N     1 
ATOM   8148  C  CA    . MET B 1 322 ? 101.040 149.702 140.569 1.00 35.62 ?  322 MET B CA    1 
ATOM   8149  C  C     . MET B 1 322 ? 100.702 148.290 140.110 1.00 37.11 ?  322 MET B C     1 
ATOM   8150  O  O     . MET B 1 322 ? 100.619 148.066 138.901 1.00 47.12 ?  322 MET B O     1 
ATOM   8151  C  CB    . MET B 1 322 ? 102.460 150.045 140.102 1.00 35.35 ?  322 MET B CB    1 
ATOM   8152  C  CG    . MET B 1 322 ? 102.739 151.530 139.968 1.00 39.64 ?  322 MET B CG    1 
ATOM   8153  S  SD    . MET B 1 322 ? 101.288 152.472 139.472 1.00 50.65 ?  322 MET B SD    1 
ATOM   8154  C  CE    . MET B 1 322 ? 101.371 152.302 137.692 1.00 39.32 ?  322 MET B CE    1 
ATOM   8155  N  N     . TYR B 1 323 ? 100.508 147.338 141.024 1.00 37.53 ?  323 TYR B N     1 
ATOM   8156  C  CA    . TYR B 1 323 ? 100.301 145.953 140.608 1.00 33.11 ?  323 TYR B CA    1 
ATOM   8157  C  C     . TYR B 1 323 ? 98.975  145.790 139.875 1.00 40.15 ?  323 TYR B C     1 
ATOM   8158  O  O     . TYR B 1 323 ? 98.909  145.140 138.825 1.00 43.00 ?  323 TYR B O     1 
ATOM   8159  C  CB    . TYR B 1 323 ? 100.366 145.026 141.821 1.00 34.53 ?  323 TYR B CB    1 
ATOM   8160  C  CG    . TYR B 1 323 ? 100.055 143.578 141.506 1.00 37.76 ?  323 TYR B CG    1 
ATOM   8161  C  CD1   . TYR B 1 323 ? 101.034 142.733 141.003 1.00 31.61 ?  323 TYR B CD1   1 
ATOM   8162  C  CD2   . TYR B 1 323 ? 98.785  143.058 141.714 1.00 37.36 ?  323 TYR B CD2   1 
ATOM   8163  C  CE1   . TYR B 1 323 ? 100.755 141.413 140.716 1.00 28.11 ?  323 TYR B CE1   1 
ATOM   8164  C  CE2   . TYR B 1 323 ? 98.498  141.740 141.428 1.00 33.00 ?  323 TYR B CE2   1 
ATOM   8165  C  CZ    . TYR B 1 323 ? 99.487  140.924 140.930 1.00 32.57 ?  323 TYR B CZ    1 
ATOM   8166  O  OH    . TYR B 1 323 ? 99.205  139.611 140.644 1.00 38.21 ?  323 TYR B OH    1 
ATOM   8167  N  N     . ASP B 1 324 ? 97.904  146.371 140.418 1.00 43.32 ?  324 ASP B N     1 
ATOM   8168  C  CA    . ASP B 1 324 ? 96.603  146.275 139.766 1.00 38.89 ?  324 ASP B CA    1 
ATOM   8169  C  C     . ASP B 1 324 ? 96.611  146.986 138.420 1.00 41.91 ?  324 ASP B C     1 
ATOM   8170  O  O     . ASP B 1 324 ? 96.012  146.505 137.452 1.00 47.99 ?  324 ASP B O     1 
ATOM   8171  C  CB    . ASP B 1 324 ? 95.517  146.848 140.674 1.00 42.11 ?  324 ASP B CB    1 
ATOM   8172  C  CG    . ASP B 1 324 ? 95.307  146.017 141.922 1.00 45.33 ?  324 ASP B CG    1 
ATOM   8173  O  OD1   . ASP B 1 324 ? 95.407  144.777 141.834 1.00 45.34 ?  324 ASP B OD1   1 
ATOM   8174  O  OD2   . ASP B 1 324 ? 95.040  146.604 142.991 1.00 46.45 -1 324 ASP B OD2   1 
ATOM   8175  N  N     . LYS B 1 325 ? 97.283  148.136 138.341 1.00 42.05 ?  325 LYS B N     1 
ATOM   8176  C  CA    . LYS B 1 325 ? 97.384  148.849 137.072 1.00 41.84 ?  325 LYS B CA    1 
ATOM   8177  C  C     . LYS B 1 325 ? 98.170  148.044 136.047 1.00 41.15 ?  325 LYS B C     1 
ATOM   8178  O  O     . LYS B 1 325 ? 97.814  148.019 134.864 1.00 46.54 ?  325 LYS B O     1 
ATOM   8179  C  CB    . LYS B 1 325 ? 98.023  150.219 137.293 1.00 39.41 ?  325 LYS B CB    1 
ATOM   8180  C  CG    . LYS B 1 325 ? 97.280  151.080 138.297 1.00 38.15 ?  325 LYS B CG    1 
ATOM   8181  C  CD    . LYS B 1 325 ? 97.225  152.532 137.853 1.00 43.84 ?  325 LYS B CD    1 
ATOM   8182  C  CE    . LYS B 1 325 ? 97.885  153.449 138.867 1.00 44.36 ?  325 LYS B CE    1 
ATOM   8183  N  NZ    . LYS B 1 325 ? 97.129  153.492 140.149 1.00 46.04 1  325 LYS B NZ    1 
ATOM   8184  N  N     . PHE B 1 326 ? 99.249  147.386 136.478 1.00 39.33 ?  326 PHE B N     1 
ATOM   8185  C  CA    . PHE B 1 326 ? 100.010 146.531 135.574 1.00 36.16 ?  326 PHE B CA    1 
ATOM   8186  C  C     . PHE B 1 326 ? 99.161  145.373 135.073 1.00 36.41 ?  326 PHE B C     1 
ATOM   8187  O  O     . PHE B 1 326 ? 99.179  145.051 133.880 1.00 44.28 ?  326 PHE B O     1 
ATOM   8188  C  CB    . PHE B 1 326 ? 101.258 145.994 136.279 1.00 34.73 ?  326 PHE B CB    1 
ATOM   8189  C  CG    . PHE B 1 326 ? 102.282 147.042 136.604 1.00 32.72 ?  326 PHE B CG    1 
ATOM   8190  C  CD1   . PHE B 1 326 ? 102.240 148.290 136.012 1.00 34.49 ?  326 PHE B CD1   1 
ATOM   8191  C  CD2   . PHE B 1 326 ? 103.296 146.770 137.507 1.00 36.10 ?  326 PHE B CD2   1 
ATOM   8192  C  CE1   . PHE B 1 326 ? 103.186 149.247 136.317 1.00 33.27 ?  326 PHE B CE1   1 
ATOM   8193  C  CE2   . PHE B 1 326 ? 104.244 147.721 137.813 1.00 39.21 ?  326 PHE B CE2   1 
ATOM   8194  C  CZ    . PHE B 1 326 ? 104.188 148.961 137.216 1.00 39.45 ?  326 PHE B CZ    1 
ATOM   8195  N  N     . VAL B 1 327 ? 98.412  144.733 135.974 1.00 40.83 ?  327 VAL B N     1 
ATOM   8196  C  CA    . VAL B 1 327 ? 97.607  143.577 135.591 1.00 43.25 ?  327 VAL B CA    1 
ATOM   8197  C  C     . VAL B 1 327 ? 96.488  143.992 134.642 1.00 43.55 ?  327 VAL B C     1 
ATOM   8198  O  O     . VAL B 1 327 ? 96.216  143.310 133.646 1.00 45.72 ?  327 VAL B O     1 
ATOM   8199  C  CB    . VAL B 1 327 ? 97.060  142.869 136.844 1.00 37.68 ?  327 VAL B CB    1 
ATOM   8200  C  CG1   . VAL B 1 327 ? 96.051  141.803 136.459 1.00 40.71 ?  327 VAL B CG1   1 
ATOM   8201  C  CG2   . VAL B 1 327 ? 98.196  142.256 137.642 1.00 31.33 ?  327 VAL B CG2   1 
ATOM   8202  N  N     . ASP B 1 328 ? 95.832  145.117 134.922 1.00 44.04 ?  328 ASP B N     1 
ATOM   8203  C  CA    . ASP B 1 328 ? 94.727  145.579 134.093 1.00 45.35 ?  328 ASP B CA    1 
ATOM   8204  C  C     . ASP B 1 328 ? 95.184  146.249 132.806 1.00 45.87 ?  328 ASP B C     1 
ATOM   8205  O  O     . ASP B 1 328 ? 94.346  146.513 131.937 1.00 49.89 ?  328 ASP B O     1 
ATOM   8206  C  CB    . ASP B 1 328 ? 93.844  146.545 134.883 1.00 45.98 ?  328 ASP B CB    1 
ATOM   8207  C  CG    . ASP B 1 328 ? 93.003  145.841 135.928 1.00 52.99 ?  328 ASP B CG    1 
ATOM   8208  O  OD1   . ASP B 1 328 ? 92.879  144.601 135.854 1.00 52.45 ?  328 ASP B OD1   1 
ATOM   8209  O  OD2   . ASP B 1 328 ? 92.467  146.527 136.823 1.00 51.64 -1 328 ASP B OD2   1 
ATOM   8210  N  N     . ASN B 1 329 ? 96.472  146.535 132.661 1.00 40.44 ?  329 ASN B N     1 
ATOM   8211  C  CA    . ASN B 1 329 ? 96.966  147.164 131.444 1.00 39.47 ?  329 ASN B CA    1 
ATOM   8212  C  C     . ASN B 1 329 ? 97.170  146.109 130.365 1.00 47.37 ?  329 ASN B C     1 
ATOM   8213  O  O     . ASN B 1 329 ? 97.997  145.207 130.545 1.00 44.71 ?  329 ASN B O     1 
ATOM   8214  C  CB    . ASN B 1 329 ? 98.272  147.898 131.712 1.00 36.96 ?  329 ASN B CB    1 
ATOM   8215  C  CG    . ASN B 1 329 ? 98.540  148.997 130.706 1.00 42.80 ?  329 ASN B CG    1 
ATOM   8216  O  OD1   . ASN B 1 329 ? 98.909  148.729 129.564 1.00 47.29 ?  329 ASN B OD1   1 
ATOM   8217  N  ND2   . ASN B 1 329 ? 98.357  150.242 131.126 1.00 40.27 ?  329 ASN B ND2   1 
ATOM   8218  N  N     . PRO B 1 330 ? 96.446  146.173 129.245 1.00 49.24 ?  330 PRO B N     1 
ATOM   8219  C  CA    . PRO B 1 330 ? 96.667  145.190 128.173 1.00 43.76 ?  330 PRO B CA    1 
ATOM   8220  C  C     . PRO B 1 330 ? 98.022  145.315 127.506 1.00 41.32 ?  330 PRO B C     1 
ATOM   8221  O  O     . PRO B 1 330 ? 98.511  144.324 126.949 1.00 44.94 ?  330 PRO B O     1 
ATOM   8222  C  CB    . PRO B 1 330 ? 95.530  145.485 127.187 1.00 46.22 ?  330 PRO B CB    1 
ATOM   8223  C  CG    . PRO B 1 330 ? 95.184  146.911 127.436 1.00 43.83 ?  330 PRO B CG    1 
ATOM   8224  C  CD    . PRO B 1 330 ? 95.385  147.135 128.904 1.00 42.32 ?  330 PRO B CD    1 
ATOM   8225  N  N     . ARG B 1 331 ? 98.643  146.491 127.540 1.00 39.59 ?  331 ARG B N     1 
ATOM   8226  C  CA    . ARG B 1 331 ? 99.941  146.698 126.913 1.00 42.99 ?  331 ARG B CA    1 
ATOM   8227  C  C     . ARG B 1 331 ? 101.100 146.243 127.789 1.00 42.42 ?  331 ARG B C     1 
ATOM   8228  O  O     . ARG B 1 331 ? 102.248 146.275 127.335 1.00 41.85 ?  331 ARG B O     1 
ATOM   8229  C  CB    . ARG B 1 331 ? 100.111 148.174 126.543 1.00 40.58 ?  331 ARG B CB    1 
ATOM   8230  C  CG    . ARG B 1 331 ? 98.989  148.712 125.672 1.00 41.00 ?  331 ARG B CG    1 
ATOM   8231  C  CD    . ARG B 1 331 ? 99.051  150.231 125.554 1.00 41.46 ?  331 ARG B CD    1 
ATOM   8232  N  NE    . ARG B 1 331 ? 98.330  150.950 126.602 1.00 41.04 ?  331 ARG B NE    1 
ATOM   8233  C  CZ    . ARG B 1 331 ? 97.078  150.725 126.987 1.00 45.31 ?  331 ARG B CZ    1 
ATOM   8234  N  NH1   . ARG B 1 331 ? 96.300  149.855 126.364 1.00 45.36 1  331 ARG B NH1   1 
ATOM   8235  N  NH2   . ARG B 1 331 ? 96.583  151.416 128.010 1.00 42.03 ?  331 ARG B NH2   1 
ATOM   8236  N  N     . VAL B 1 332 ? 100.830 145.830 129.023 1.00 37.76 ?  332 VAL B N     1 
ATOM   8237  C  CA    . VAL B 1 332 ? 101.839 145.260 129.907 1.00 34.85 ?  332 VAL B CA    1 
ATOM   8238  C  C     . VAL B 1 332 ? 101.733 143.745 129.813 1.00 38.85 ?  332 VAL B C     1 
ATOM   8239  O  O     . VAL B 1 332 ? 100.661 143.173 130.045 1.00 40.26 ?  332 VAL B O     1 
ATOM   8240  C  CB    . VAL B 1 332 ? 101.655 145.742 131.355 1.00 35.51 ?  332 VAL B CB    1 
ATOM   8241  C  CG1   . VAL B 1 332 ? 102.461 144.878 132.308 1.00 37.32 ?  332 VAL B CG1   1 
ATOM   8242  C  CG2   . VAL B 1 332 ? 102.062 147.201 131.484 1.00 34.26 ?  332 VAL B CG2   1 
ATOM   8243  N  N     . LYS B 1 333 ? 102.837 143.092 129.463 1.00 34.79 ?  333 LYS B N     1 
ATOM   8244  C  CA    . LYS B 1 333 ? 102.857 141.646 129.296 1.00 31.33 ?  333 LYS B CA    1 
ATOM   8245  C  C     . LYS B 1 333 ? 103.174 140.963 130.620 1.00 34.52 ?  333 LYS B C     1 
ATOM   8246  O  O     . LYS B 1 333 ? 104.030 141.423 131.383 1.00 35.76 ?  333 LYS B O     1 
ATOM   8247  C  CB    . LYS B 1 333 ? 103.877 141.242 128.231 1.00 30.40 ?  333 LYS B CB    1 
ATOM   8248  C  CG    . LYS B 1 333 ? 103.695 139.831 127.704 1.00 37.96 ?  333 LYS B CG    1 
ATOM   8249  C  CD    . LYS B 1 333 ? 104.832 139.436 126.777 1.00 38.66 ?  333 LYS B CD    1 
ATOM   8250  C  CE    . LYS B 1 333 ? 104.713 137.985 126.349 1.00 38.80 ?  333 LYS B CE    1 
ATOM   8251  N  NZ    . LYS B 1 333 ? 105.808 137.588 125.424 1.00 40.45 1  333 LYS B NZ    1 
ATOM   8252  N  N     . LYS B 1 334 ? 102.476 139.862 130.889 1.00 37.10 ?  334 LYS B N     1 
ATOM   8253  C  CA    . LYS B 1 334 ? 102.622 139.147 132.147 1.00 32.47 ?  334 LYS B CA    1 
ATOM   8254  C  C     . LYS B 1 334 ? 102.260 137.685 131.937 1.00 35.58 ?  334 LYS B C     1 
ATOM   8255  O  O     . LYS B 1 334 ? 101.609 137.323 130.955 1.00 43.50 ?  334 LYS B O     1 
ATOM   8256  C  CB    . LYS B 1 334 ? 101.733 139.756 133.235 1.00 33.98 ?  334 LYS B CB    1 
ATOM   8257  C  CG    . LYS B 1 334 ? 100.266 139.817 132.846 1.00 35.77 ?  334 LYS B CG    1 
ATOM   8258  C  CD    . LYS B 1 334 ? 99.522  140.902 133.595 1.00 33.80 ?  334 LYS B CD    1 
ATOM   8259  C  CE    . LYS B 1 334 ? 99.411  142.159 132.757 1.00 37.85 ?  334 LYS B CE    1 
ATOM   8260  N  NZ    . LYS B 1 334 ? 98.426  142.021 131.651 1.00 37.62 1  334 LYS B NZ    1 
ATOM   8261  N  N     . GLU B 1 335 ? 102.698 136.840 132.872 1.00 38.13 ?  335 GLU B N     1 
ATOM   8262  C  CA    . GLU B 1 335 ? 102.226 135.465 132.954 1.00 43.58 ?  335 GLU B CA    1 
ATOM   8263  C  C     . GLU B 1 335 ? 101.787 135.159 134.377 1.00 41.91 ?  335 GLU B C     1 
ATOM   8264  O  O     . GLU B 1 335 ? 102.379 135.655 135.339 1.00 44.95 ?  335 GLU B O     1 
ATOM   8265  C  CB    . GLU B 1 335 ? 103.281 134.435 132.538 1.00 39.57 ?  335 GLU B CB    1 
ATOM   8266  C  CG    . GLU B 1 335 ? 104.715 134.832 132.753 1.00 40.04 ?  335 GLU B CG    1 
ATOM   8267  C  CD    . GLU B 1 335 ? 105.662 133.903 132.024 1.00 47.14 ?  335 GLU B CD    1 
ATOM   8268  O  OE1   . GLU B 1 335 ? 106.588 133.372 132.672 1.00 44.33 ?  335 GLU B OE1   1 
ATOM   8269  O  OE2   . GLU B 1 335 ? 105.480 133.700 130.805 1.00 46.65 -1 335 GLU B OE2   1 
ATOM   8270  N  N     . LYS B 1 336 ? 100.753 134.333 134.497 1.00 38.84 ?  336 LYS B N     1 
ATOM   8271  C  CA    . LYS B 1 336 ? 100.261 133.923 135.803 1.00 30.35 ?  336 LYS B CA    1 
ATOM   8272  C  C     . LYS B 1 336 ? 101.288 133.052 136.514 1.00 37.36 ?  336 LYS B C     1 
ATOM   8273  O  O     . LYS B 1 336 ? 101.950 132.214 135.898 1.00 40.56 ?  336 LYS B O     1 
ATOM   8274  C  CB    . LYS B 1 336 ? 98.948  133.157 135.653 1.00 40.33 ?  336 LYS B CB    1 
ATOM   8275  C  CG    . LYS B 1 336 ? 98.137  133.050 136.929 1.00 43.04 ?  336 LYS B CG    1 
ATOM   8276  C  CD    . LYS B 1 336 ? 97.234  134.256 137.089 1.00 44.70 ?  336 LYS B CD    1 
ATOM   8277  C  CE    . LYS B 1 336 ? 95.869  134.002 136.474 1.00 41.52 ?  336 LYS B CE    1 
ATOM   8278  N  NZ    . LYS B 1 336 ? 94.974  133.259 137.400 1.00 41.81 1  336 LYS B NZ    1 
ATOM   8279  N  N     . ILE B 1 337 ? 101.423 133.261 137.823 1.00 38.68 ?  337 ILE B N     1 
ATOM   8280  C  CA    . ILE B 1 337 ? 102.218 132.400 138.686 1.00 36.88 ?  337 ILE B CA    1 
ATOM   8281  C  C     . ILE B 1 337 ? 101.406 132.108 139.939 1.00 39.62 ?  337 ILE B C     1 
ATOM   8282  O  O     . ILE B 1 337 ? 100.410 132.768 140.232 1.00 45.76 ?  337 ILE B O     1 
ATOM   8283  C  CB    . ILE B 1 337 ? 103.580 133.019 139.063 1.00 35.97 ?  337 ILE B CB    1 
ATOM   8284  C  CG1   . ILE B 1 337 ? 103.379 134.377 139.738 1.00 37.24 ?  337 ILE B CG1   1 
ATOM   8285  C  CG2   . ILE B 1 337 ? 104.480 133.135 137.844 1.00 37.46 ?  337 ILE B CG2   1 
ATOM   8286  C  CD1   . ILE B 1 337 ? 104.391 134.681 140.814 1.00 33.60 ?  337 ILE B CD1   1 
ATOM   8287  N  N     . ASN B 1 338 ? 101.846 131.096 140.680 1.00 38.80 ?  338 ASN B N     1 
ATOM   8288  C  CA    . ASN B 1 338 ? 101.283 130.824 141.992 1.00 34.32 ?  338 ASN B CA    1 
ATOM   8289  C  C     . ASN B 1 338 ? 102.239 131.366 143.040 1.00 35.85 ?  338 ASN B C     1 
ATOM   8290  O  O     . ASN B 1 338 ? 103.332 130.808 143.212 1.00 42.95 ?  338 ASN B O     1 
ATOM   8291  C  CB    . ASN B 1 338 ? 101.060 129.327 142.191 1.00 35.42 ?  338 ASN B CB    1 
ATOM   8292  C  CG    . ASN B 1 338 ? 100.058 129.030 143.287 1.00 39.78 ?  338 ASN B CG    1 
ATOM   8293  O  OD1   . ASN B 1 338 ? 99.608  129.930 143.994 1.00 41.66 ?  338 ASN B OD1   1 
ATOM   8294  N  ND2   . ASN B 1 338 ? 99.700  127.760 143.433 1.00 39.95 ?  338 ASN B ND2   1 
ATOM   8295  N  N     . PRO B 1 339 ? 101.894 132.448 143.743 1.00 36.61 ?  339 PRO B N     1 
ATOM   8296  C  CA    . PRO B 1 339 ? 102.831 133.004 144.731 1.00 34.86 ?  339 PRO B CA    1 
ATOM   8297  C  C     . PRO B 1 339 ? 103.171 132.043 145.854 1.00 32.01 ?  339 PRO B C     1 
ATOM   8298  O  O     . PRO B 1 339 ? 104.305 132.064 146.349 1.00 36.23 ?  339 PRO B O     1 
ATOM   8299  C  CB    . PRO B 1 339 ? 102.095 134.246 145.249 1.00 33.12 ?  339 PRO B CB    1 
ATOM   8300  C  CG    . PRO B 1 339 ? 100.665 133.976 144.978 1.00 36.79 ?  339 PRO B CG    1 
ATOM   8301  C  CD    . PRO B 1 339 ? 100.627 133.193 143.705 1.00 36.01 ?  339 PRO B CD    1 
ATOM   8302  N  N     . ARG B 1 340 ? 102.228 131.201 146.276 1.00 33.55 ?  340 ARG B N     1 
ATOM   8303  C  CA    . ARG B 1 340 ? 102.537 130.211 147.302 1.00 32.24 ?  340 ARG B CA    1 
ATOM   8304  C  C     . ARG B 1 340 ? 103.500 129.158 146.774 1.00 33.47 ?  340 ARG B C     1 
ATOM   8305  O  O     . ARG B 1 340 ? 104.405 128.721 147.493 1.00 39.77 ?  340 ARG B O     1 
ATOM   8306  C  CB    . ARG B 1 340 ? 101.255 129.562 147.815 1.00 31.38 ?  340 ARG B CB    1 
ATOM   8307  C  CG    . ARG B 1 340 ? 100.440 130.464 148.714 1.00 29.58 ?  340 ARG B CG    1 
ATOM   8308  C  CD    . ARG B 1 340 ? 99.522  129.671 149.622 1.00 31.39 ?  340 ARG B CD    1 
ATOM   8309  N  NE    . ARG B 1 340 ? 98.607  130.545 150.347 1.00 33.49 ?  340 ARG B NE    1 
ATOM   8310  C  CZ    . ARG B 1 340 ? 97.700  130.126 151.217 1.00 35.94 ?  340 ARG B CZ    1 
ATOM   8311  N  NH1   . ARG B 1 340 ? 97.558  128.842 151.502 1.00 35.30 1  340 ARG B NH1   1 
ATOM   8312  N  NH2   . ARG B 1 340 ? 96.915  131.017 151.814 1.00 36.79 ?  340 ARG B NH2   1 
ATOM   8313  N  N     . LYS B 1 341 ? 103.323 128.740 145.520 1.00 34.62 ?  341 LYS B N     1 
ATOM   8314  C  CA    . LYS B 1 341 ? 104.271 127.810 144.919 1.00 33.59 ?  341 LYS B CA    1 
ATOM   8315  C  C     . LYS B 1 341 ? 105.646 128.446 144.776 1.00 30.60 ?  341 LYS B C     1 
ATOM   8316  O  O     . LYS B 1 341 ? 106.666 127.777 144.964 1.00 32.98 ?  341 LYS B O     1 
ATOM   8317  C  CB    . LYS B 1 341 ? 103.753 127.329 143.564 1.00 37.60 ?  341 LYS B CB    1 
ATOM   8318  C  CG    . LYS B 1 341 ? 102.667 126.265 143.649 1.00 38.96 ?  341 LYS B CG    1 
ATOM   8319  C  CD    . LYS B 1 341 ? 102.784 125.439 144.922 1.00 40.97 ?  341 LYS B CD    1 
ATOM   8320  C  CE    . LYS B 1 341 ? 101.784 124.297 144.935 1.00 41.70 ?  341 LYS B CE    1 
ATOM   8321  N  NZ    . LYS B 1 341 ? 102.439 122.998 145.245 1.00 40.34 1  341 LYS B NZ    1 
ATOM   8322  N  N     . LEU B 1 342 ? 105.696 129.739 144.448 1.00 32.33 ?  342 LEU B N     1 
ATOM   8323  C  CA    . LEU B 1 342 ? 106.978 130.432 144.383 1.00 29.16 ?  342 LEU B CA    1 
ATOM   8324  C  C     . LEU B 1 342 ? 107.633 130.512 145.757 1.00 29.99 ?  342 LEU B C     1 
ATOM   8325  O  O     . LEU B 1 342 ? 108.853 130.354 145.877 1.00 38.62 ?  342 LEU B O     1 
ATOM   8326  C  CB    . LEU B 1 342 ? 106.792 131.828 143.788 1.00 28.81 ?  342 LEU B CB    1 
ATOM   8327  C  CG    . LEU B 1 342 ? 108.054 132.498 143.242 1.00 29.11 ?  342 LEU B CG    1 
ATOM   8328  C  CD1   . LEU B 1 342 ? 108.880 131.510 142.438 1.00 28.49 ?  342 LEU B CD1   1 
ATOM   8329  C  CD2   . LEU B 1 342 ? 107.699 133.707 142.397 1.00 28.15 ?  342 LEU B CD2   1 
ATOM   8330  N  N     . LEU B 1 343 ? 106.842 130.756 146.804 1.00 27.61 ?  343 LEU B N     1 
ATOM   8331  C  CA    . LEU B 1 343 ? 107.384 130.763 148.161 1.00 29.13 ?  343 LEU B CA    1 
ATOM   8332  C  C     . LEU B 1 343 ? 107.921 129.392 148.550 1.00 28.50 ?  343 LEU B C     1 
ATOM   8333  O  O     . LEU B 1 343 ? 108.986 129.283 149.171 1.00 32.52 ?  343 LEU B O     1 
ATOM   8334  C  CB    . LEU B 1 343 ? 106.310 131.212 149.149 1.00 31.73 ?  343 LEU B CB    1 
ATOM   8335  C  CG    . LEU B 1 343 ? 106.272 132.694 149.517 1.00 32.63 ?  343 LEU B CG    1 
ATOM   8336  C  CD1   . LEU B 1 343 ? 105.125 132.965 150.472 1.00 27.04 ?  343 LEU B CD1   1 
ATOM   8337  C  CD2   . LEU B 1 343 ? 107.593 133.129 150.126 1.00 33.94 ?  343 LEU B CD2   1 
ATOM   8338  N  N     . GLU B 1 344 ? 107.188 128.333 148.208 1.00 34.65 ?  344 GLU B N     1 
ATOM   8339  C  CA    . GLU B 1 344 ? 107.656 126.984 148.505 1.00 32.82 ?  344 GLU B CA    1 
ATOM   8340  C  C     . GLU B 1 344 ? 108.921 126.658 147.724 1.00 29.44 ?  344 GLU B C     1 
ATOM   8341  O  O     . GLU B 1 344 ? 109.815 125.978 148.236 1.00 34.99 ?  344 GLU B O     1 
ATOM   8342  C  CB    . GLU B 1 344 ? 106.555 125.968 148.206 1.00 35.28 ?  344 GLU B CB    1 
ATOM   8343  C  CG    . GLU B 1 344 ? 105.311 126.141 149.060 1.00 36.66 ?  344 GLU B CG    1 
ATOM   8344  C  CD    . GLU B 1 344 ? 104.176 125.238 148.623 1.00 45.78 ?  344 GLU B CD    1 
ATOM   8345  O  OE1   . GLU B 1 344 ? 104.457 124.150 148.080 1.00 44.97 ?  344 GLU B OE1   1 
ATOM   8346  O  OE2   . GLU B 1 344 ? 103.003 125.620 148.820 1.00 43.83 -1 344 GLU B OE2   1 
ATOM   8347  N  N     . LYS B 1 345 ? 109.013 127.135 146.481 1.00 29.73 ?  345 LYS B N     1 
ATOM   8348  C  CA    . LYS B 1 345 ? 110.233 126.958 145.702 1.00 28.05 ?  345 LYS B CA    1 
ATOM   8349  C  C     . LYS B 1 345 ? 111.401 127.700 146.336 1.00 33.02 ?  345 LYS B C     1 
ATOM   8350  O  O     . LYS B 1 345 ? 112.526 127.189 146.367 1.00 36.04 ?  345 LYS B O     1 
ATOM   8351  C  CB    . LYS B 1 345 ? 110.006 127.431 144.267 1.00 29.85 ?  345 LYS B CB    1 
ATOM   8352  C  CG    . LYS B 1 345 ? 111.198 127.241 143.353 1.00 30.65 ?  345 LYS B CG    1 
ATOM   8353  C  CD    . LYS B 1 345 ? 110.890 127.716 141.946 1.00 29.51 ?  345 LYS B CD    1 
ATOM   8354  C  CE    . LYS B 1 345 ? 112.113 127.617 141.057 1.00 34.19 ?  345 LYS B CE    1 
ATOM   8355  N  NZ    . LYS B 1 345 ? 111.854 128.157 139.698 1.00 34.65 1  345 LYS B NZ    1 
ATOM   8356  N  N     . LEU B 1 346 ? 111.151 128.907 146.848 1.00 33.81 ?  346 LEU B N     1 
ATOM   8357  C  CA    . LEU B 1 346 ? 112.189 129.648 147.558 1.00 27.40 ?  346 LEU B CA    1 
ATOM   8358  C  C     . LEU B 1 346 ? 112.672 128.873 148.775 1.00 25.79 ?  346 LEU B C     1 
ATOM   8359  O  O     . LEU B 1 346 ? 113.878 128.752 149.009 1.00 28.42 ?  346 LEU B O     1 
ATOM   8360  C  CB    . LEU B 1 346 ? 111.662 131.020 147.981 1.00 27.66 ?  346 LEU B CB    1 
ATOM   8361  C  CG    . LEU B 1 346 ? 111.398 132.076 146.911 1.00 26.18 ?  346 LEU B CG    1 
ATOM   8362  C  CD1   . LEU B 1 346 ? 110.784 133.312 147.540 1.00 30.49 ?  346 LEU B CD1   1 
ATOM   8363  C  CD2   . LEU B 1 346 ? 112.676 132.426 146.187 1.00 27.88 ?  346 LEU B CD2   1 
ATOM   8364  N  N     . ALA B 1 347 ? 111.736 128.338 149.561 1.00 26.69 ?  347 ALA B N     1 
ATOM   8365  C  CA    . ALA B 1 347 ? 112.115 127.590 150.756 1.00 20.04 ?  347 ALA B CA    1 
ATOM   8366  C  C     . ALA B 1 347 ? 112.878 126.320 150.397 1.00 27.48 ?  347 ALA B C     1 
ATOM   8367  O  O     . ALA B 1 347 ? 113.852 125.962 151.069 1.00 35.93 ?  347 ALA B O     1 
ATOM   8368  C  CB    . ALA B 1 347 ? 110.877 127.257 151.583 1.00 19.98 ?  347 ALA B CB    1 
ATOM   8369  N  N     . MET B 1 348 ? 112.446 125.623 149.344 1.00 33.95 ?  348 MET B N     1 
ATOM   8370  C  CA    . MET B 1 348 ? 113.153 124.427 148.900 1.00 31.21 ?  348 MET B CA    1 
ATOM   8371  C  C     . MET B 1 348 ? 114.568 124.760 148.449 1.00 31.70 ?  348 MET B C     1 
ATOM   8372  O  O     . MET B 1 348 ? 115.520 124.040 148.774 1.00 40.09 ?  348 MET B O     1 
ATOM   8373  C  CB    . MET B 1 348 ? 112.366 123.752 147.774 1.00 33.42 ?  348 MET B CB    1 
ATOM   8374  C  CG    . MET B 1 348 ? 113.101 122.624 147.070 1.00 40.99 ?  348 MET B CG    1 
ATOM   8375  S  SD    . MET B 1 348 ? 113.860 123.133 145.514 1.00 60.89 ?  348 MET B SD    1 
ATOM   8376  C  CE    . MET B 1 348 ? 112.529 124.069 144.767 1.00 38.33 ?  348 MET B CE    1 
ATOM   8377  N  N     . LEU B 1 349 ? 114.726 125.857 147.705 1.00 26.74 ?  349 LEU B N     1 
ATOM   8378  C  CA    . LEU B 1 349 ? 116.051 126.259 147.253 1.00 27.33 ?  349 LEU B CA    1 
ATOM   8379  C  C     . LEU B 1 349 ? 116.943 126.645 148.424 1.00 28.95 ?  349 LEU B C     1 
ATOM   8380  O  O     . LEU B 1 349 ? 118.140 126.340 148.426 1.00 32.49 ?  349 LEU B O     1 
ATOM   8381  C  CB    . LEU B 1 349 ? 115.929 127.417 146.266 1.00 27.93 ?  349 LEU B CB    1 
ATOM   8382  C  CG    . LEU B 1 349 ? 115.878 127.012 144.796 1.00 33.81 ?  349 LEU B CG    1 
ATOM   8383  C  CD1   . LEU B 1 349 ? 115.084 128.031 144.016 1.00 34.75 ?  349 LEU B CD1   1 
ATOM   8384  C  CD2   . LEU B 1 349 ? 117.280 126.875 144.233 1.00 33.96 ?  349 LEU B CD2   1 
ATOM   8385  N  N     . ARG B 1 350 ? 116.385 127.333 149.423 1.00 26.35 ?  350 ARG B N     1 
ATOM   8386  C  CA    . ARG B 1 350 ? 117.178 127.696 150.593 1.00 22.58 ?  350 ARG B CA    1 
ATOM   8387  C  C     . ARG B 1 350 ? 117.565 126.472 151.410 1.00 30.68 ?  350 ARG B C     1 
ATOM   8388  O  O     . ARG B 1 350 ? 118.669 126.421 151.962 1.00 41.06 ?  350 ARG B O     1 
ATOM   8389  C  CB    . ARG B 1 350 ? 116.421 128.701 151.460 1.00 25.27 ?  350 ARG B CB    1 
ATOM   8390  C  CG    . ARG B 1 350 ? 116.037 129.977 150.737 1.00 24.47 ?  350 ARG B CG    1 
ATOM   8391  C  CD    . ARG B 1 350 ? 115.667 131.074 151.709 1.00 26.29 ?  350 ARG B CD    1 
ATOM   8392  N  NE    . ARG B 1 350 ? 116.773 131.998 151.916 1.00 33.09 ?  350 ARG B NE    1 
ATOM   8393  C  CZ    . ARG B 1 350 ? 117.168 132.435 153.103 1.00 28.82 ?  350 ARG B CZ    1 
ATOM   8394  N  NH1   . ARG B 1 350 ? 116.585 132.030 154.216 1.00 26.87 1  350 ARG B NH1   1 
ATOM   8395  N  NH2   . ARG B 1 350 ? 118.179 133.296 153.172 1.00 32.13 ?  350 ARG B NH2   1 
ATOM   8396  N  N     . SER B 1 351 ? 116.674 125.485 151.512 1.00 33.84 ?  351 SER B N     1 
ATOM   8397  C  CA    . SER B 1 351 ? 117.033 124.238 152.177 1.00 33.14 ?  351 SER B CA    1 
ATOM   8398  C  C     . SER B 1 351 ? 118.148 123.519 151.430 1.00 34.19 ?  351 SER B C     1 
ATOM   8399  O  O     . SER B 1 351 ? 119.086 123.000 152.045 1.00 42.75 ?  351 SER B O     1 
ATOM   8400  C  CB    . SER B 1 351 ? 115.808 123.334 152.301 1.00 34.41 ?  351 SER B CB    1 
ATOM   8401  O  OG    . SER B 1 351 ? 114.841 123.897 153.168 1.00 44.10 ?  351 SER B OG    1 
ATOM   8402  N  N     . GLU B 1 352 ? 118.064 123.479 150.099 1.00 34.56 ?  352 GLU B N     1 
ATOM   8403  C  CA    . GLU B 1 352 ? 119.035 122.715 149.322 1.00 35.03 ?  352 GLU B CA    1 
ATOM   8404  C  C     . GLU B 1 352 ? 120.397 123.400 149.280 1.00 35.91 ?  352 GLU B C     1 
ATOM   8405  O  O     . GLU B 1 352 ? 121.430 122.743 149.454 1.00 44.61 ?  352 GLU B O     1 
ATOM   8406  C  CB    . GLU B 1 352 ? 118.505 122.486 147.909 1.00 36.46 ?  352 GLU B CB    1 
ATOM   8407  C  CG    . GLU B 1 352 ? 117.401 121.448 147.831 1.00 39.07 ?  352 GLU B CG    1 
ATOM   8408  C  CD    . GLU B 1 352 ? 116.673 121.471 146.504 1.00 47.81 ?  352 GLU B CD    1 
ATOM   8409  O  OE1   . GLU B 1 352 ? 116.962 122.368 145.685 1.00 44.81 ?  352 GLU B OE1   1 
ATOM   8410  O  OE2   . GLU B 1 352 ? 115.816 120.592 146.279 1.00 45.72 -1 352 GLU B OE2   1 
ATOM   8411  N  N     . SER B 1 353 ? 120.427 124.714 149.050 1.00 36.06 ?  353 SER B N     1 
ATOM   8412  C  CA    . SER B 1 353 ? 121.677 125.417 148.796 1.00 36.19 ?  353 SER B CA    1 
ATOM   8413  C  C     . SER B 1 353 ? 121.886 126.676 149.624 1.00 30.27 ?  353 SER B C     1 
ATOM   8414  O  O     . SER B 1 353 ? 122.953 127.288 149.508 1.00 32.66 ?  353 SER B O     1 
ATOM   8415  C  CB    . SER B 1 353 ? 121.783 125.795 147.311 1.00 37.72 ?  353 SER B CB    1 
ATOM   8416  O  OG    . SER B 1 353 ? 120.847 126.804 146.976 1.00 35.84 ?  353 SER B OG    1 
ATOM   8417  N  N     . GLY B 1 354 ? 120.920 127.088 150.442 1.00 25.89 ?  354 GLY B N     1 
ATOM   8418  C  CA    . GLY B 1 354 ? 121.039 128.314 151.201 1.00 27.51 ?  354 GLY B CA    1 
ATOM   8419  C  C     . GLY B 1 354 ? 120.662 129.569 150.451 1.00 23.43 ?  354 GLY B C     1 
ATOM   8420  O  O     . GLY B 1 354 ? 120.673 130.654 151.047 1.00 27.53 ?  354 GLY B O     1 
ATOM   8421  N  N     . TYR B 1 355 ? 120.327 129.463 149.174 1.00 26.70 ?  355 TYR B N     1 
ATOM   8422  C  CA    . TYR B 1 355 ? 119.963 130.578 148.320 1.00 16.72 ?  355 TYR B CA    1 
ATOM   8423  C  C     . TYR B 1 355 ? 118.482 130.517 147.972 1.00 24.56 ?  355 TYR B C     1 
ATOM   8424  O  O     . TYR B 1 355 ? 117.875 129.443 147.997 1.00 29.05 ?  355 TYR B O     1 
ATOM   8425  C  CB    . TYR B 1 355 ? 120.796 130.560 147.031 1.00 19.98 ?  355 TYR B CB    1 
ATOM   8426  C  CG    . TYR B 1 355 ? 122.249 130.901 147.241 1.00 28.27 ?  355 TYR B CG    1 
ATOM   8427  C  CD1   . TYR B 1 355 ? 122.620 132.080 147.872 1.00 25.74 ?  355 TYR B CD1   1 
ATOM   8428  C  CD2   . TYR B 1 355 ? 123.251 130.045 146.813 1.00 30.44 ?  355 TYR B CD2   1 
ATOM   8429  C  CE1   . TYR B 1 355 ? 123.946 132.394 148.066 1.00 27.80 ?  355 TYR B CE1   1 
ATOM   8430  C  CE2   . TYR B 1 355 ? 124.582 130.352 147.003 1.00 29.65 ?  355 TYR B CE2   1 
ATOM   8431  C  CZ    . TYR B 1 355 ? 124.923 131.529 147.631 1.00 30.27 ?  355 TYR B CZ    1 
ATOM   8432  O  OH    . TYR B 1 355 ? 126.246 131.844 147.825 1.00 34.28 ?  355 TYR B OH    1 
ATOM   8433  N  N     . PRO B 1 356 ? 117.863 131.651 147.634 1.00 27.49 ?  356 PRO B N     1 
ATOM   8434  C  CA    . PRO B 1 356 ? 118.406 133.012 147.547 1.00 15.66 ?  356 PRO B CA    1 
ATOM   8435  C  C     . PRO B 1 356 ? 118.377 133.776 148.861 1.00 16.09 ?  356 PRO B C     1 
ATOM   8436  O  O     . PRO B 1 356 ? 117.752 133.356 149.827 1.00 24.60 ?  356 PRO B O     1 
ATOM   8437  C  CB    . PRO B 1 356 ? 117.481 133.666 146.520 1.00 18.31 ?  356 PRO B CB    1 
ATOM   8438  C  CG    . PRO B 1 356 ? 116.158 133.040 146.817 1.00 22.80 ?  356 PRO B CG    1 
ATOM   8439  C  CD    . PRO B 1 356 ? 116.471 131.603 147.151 1.00 13.71 ?  356 PRO B CD    1 
ATOM   8440  N  N     . TYR B 1 357 ? 119.062 134.914 148.919 1.00 21.55 ?  357 TYR B N     1 
ATOM   8441  C  CA    . TYR B 1 357 ? 118.794 135.876 149.975 1.00 13.99 ?  357 TYR B CA    1 
ATOM   8442  C  C     . TYR B 1 357 ? 117.396 136.444 149.781 1.00 17.78 ?  357 TYR B C     1 
ATOM   8443  O  O     . TYR B 1 357 ? 116.943 136.643 148.651 1.00 26.50 ?  357 TYR B O     1 
ATOM   8444  C  CB    . TYR B 1 357 ? 119.821 137.011 149.964 1.00 12.95 ?  357 TYR B CB    1 
ATOM   8445  C  CG    . TYR B 1 357 ? 121.264 136.599 149.768 1.00 16.72 ?  357 TYR B CG    1 
ATOM   8446  C  CD1   . TYR B 1 357 ? 121.742 135.396 150.261 1.00 17.56 ?  357 TYR B CD1   1 
ATOM   8447  C  CD2   . TYR B 1 357 ? 122.153 137.426 149.097 1.00 19.44 ?  357 TYR B CD2   1 
ATOM   8448  C  CE1   . TYR B 1 357 ? 123.056 135.025 150.091 1.00 19.94 ?  357 TYR B CE1   1 
ATOM   8449  C  CE2   . TYR B 1 357 ? 123.470 137.063 148.919 1.00 15.34 ?  357 TYR B CE2   1 
ATOM   8450  C  CZ    . TYR B 1 357 ? 123.915 135.861 149.418 1.00 24.11 ?  357 TYR B CZ    1 
ATOM   8451  O  OH    . TYR B 1 357 ? 125.229 135.490 149.248 1.00 31.95 ?  357 TYR B OH    1 
ATOM   8452  N  N     . ILE B 1 358 ? 116.703 136.697 150.883 1.00 25.86 ?  358 ILE B N     1 
ATOM   8453  C  CA    . ILE B 1 358 ? 115.368 137.278 150.848 1.00 18.22 ?  358 ILE B CA    1 
ATOM   8454  C  C     . ILE B 1 358 ? 115.465 138.705 151.360 1.00 19.32 ?  358 ILE B C     1 
ATOM   8455  O  O     . ILE B 1 358 ? 115.888 138.933 152.499 1.00 24.72 ?  358 ILE B O     1 
ATOM   8456  C  CB    . ILE B 1 358 ? 114.364 136.463 151.678 1.00 18.88 ?  358 ILE B CB    1 
ATOM   8457  C  CG1   . ILE B 1 358 ? 114.343 135.003 151.222 1.00 15.46 ?  358 ILE B CG1   1 
ATOM   8458  C  CG2   . ILE B 1 358 ? 112.982 137.082 151.584 1.00 17.41 ?  358 ILE B CG2   1 
ATOM   8459  C  CD1   . ILE B 1 358 ? 113.892 134.811 149.795 1.00 21.51 ?  358 ILE B CD1   1 
ATOM   8460  N  N     . MET B 1 359 ? 115.079 139.662 150.525 1.00 13.23 ?  359 MET B N     1 
ATOM   8461  C  CA    . MET B 1 359 ? 114.998 141.062 150.912 1.00 2.07  ?  359 MET B CA    1 
ATOM   8462  C  C     . MET B 1 359 ? 113.539 141.488 150.854 1.00 7.01  ?  359 MET B C     1 
ATOM   8463  O  O     . MET B 1 359 ? 112.933 141.489 149.779 1.00 20.50 ?  359 MET B O     1 
ATOM   8464  C  CB    . MET B 1 359 ? 115.861 141.938 150.005 1.00 10.80 ?  359 MET B CB    1 
ATOM   8465  C  CG    . MET B 1 359 ? 115.848 143.412 150.373 1.00 9.94  ?  359 MET B CG    1 
ATOM   8466  S  SD    . MET B 1 359 ? 115.909 144.501 148.944 1.00 38.89 ?  359 MET B SD    1 
ATOM   8467  C  CE    . MET B 1 359 ? 115.026 145.925 149.559 1.00 16.35 ?  359 MET B CE    1 
ATOM   8468  N  N     . PHE B 1 360 ? 112.977 141.830 152.008 1.00 13.11 ?  360 PHE B N     1 
ATOM   8469  C  CA    . PHE B 1 360 ? 111.589 142.277 152.084 1.00 5.13  ?  360 PHE B CA    1 
ATOM   8470  C  C     . PHE B 1 360 ? 111.562 143.760 151.748 1.00 13.75 ?  360 PHE B C     1 
ATOM   8471  O  O     . PHE B 1 360 ? 111.906 144.604 152.577 1.00 21.20 ?  360 PHE B O     1 
ATOM   8472  C  CB    . PHE B 1 360 ? 111.010 141.986 153.463 1.00 11.94 ?  360 PHE B CB    1 
ATOM   8473  C  CG    . PHE B 1 360 ? 110.939 140.522 153.786 1.00 16.25 ?  360 PHE B CG    1 
ATOM   8474  C  CD1   . PHE B 1 360 ? 110.128 139.674 153.050 1.00 19.55 ?  360 PHE B CD1   1 
ATOM   8475  C  CD2   . PHE B 1 360 ? 111.701 139.987 154.810 1.00 13.35 ?  360 PHE B CD2   1 
ATOM   8476  C  CE1   . PHE B 1 360 ? 110.069 138.326 153.339 1.00 18.52 ?  360 PHE B CE1   1 
ATOM   8477  C  CE2   . PHE B 1 360 ? 111.646 138.641 155.103 1.00 18.20 ?  360 PHE B CE2   1 
ATOM   8478  C  CZ    . PHE B 1 360 ? 110.828 137.810 154.367 1.00 15.01 ?  360 PHE B CZ    1 
ATOM   8479  N  N     . GLN B 1 361 ? 111.138 144.073 150.521 1.00 18.99 ?  361 GLN B N     1 
ATOM   8480  C  CA    . GLN B 1 361 ? 111.292 145.421 149.981 1.00 9.60  ?  361 GLN B CA    1 
ATOM   8481  C  C     . GLN B 1 361 ? 110.566 146.460 150.826 1.00 9.13  ?  361 GLN B C     1 
ATOM   8482  O  O     . GLN B 1 361 ? 111.109 147.536 151.100 1.00 14.03 ?  361 GLN B O     1 
ATOM   8483  C  CB    . GLN B 1 361 ? 110.783 145.457 148.539 1.00 19.01 ?  361 GLN B CB    1 
ATOM   8484  C  CG    . GLN B 1 361 ? 110.676 146.845 147.941 1.00 20.19 ?  361 GLN B CG    1 
ATOM   8485  C  CD    . GLN B 1 361 ? 111.662 147.074 146.819 1.00 20.87 ?  361 GLN B CD    1 
ATOM   8486  O  OE1   . GLN B 1 361 ? 111.786 146.257 145.910 1.00 30.14 ?  361 GLN B OE1   1 
ATOM   8487  N  NE2   . GLN B 1 361 ? 112.377 148.190 146.878 1.00 20.20 ?  361 GLN B NE2   1 
ATOM   8488  N  N     . ASP B 1 362 ? 109.338 146.164 151.247 1.00 23.19 ?  362 ASP B N     1 
ATOM   8489  C  CA    . ASP B 1 362 ? 108.556 147.144 151.987 1.00 13.79 ?  362 ASP B CA    1 
ATOM   8490  C  C     . ASP B 1 362 ? 108.962 147.243 153.451 1.00 13.78 ?  362 ASP B C     1 
ATOM   8491  O  O     . ASP B 1 362 ? 108.716 148.279 154.075 1.00 23.01 ?  362 ASP B O     1 
ATOM   8492  C  CB    . ASP B 1 362 ? 107.066 146.825 151.871 1.00 16.01 ?  362 ASP B CB    1 
ATOM   8493  C  CG    . ASP B 1 362 ? 106.573 146.876 150.437 1.00 27.61 ?  362 ASP B CG    1 
ATOM   8494  O  OD1   . ASP B 1 362 ? 107.405 146.742 149.515 1.00 24.96 ?  362 ASP B OD1   1 
ATOM   8495  O  OD2   . ASP B 1 362 ? 105.359 147.067 150.227 1.00 37.15 -1 362 ASP B OD2   1 
ATOM   8496  N  N     . ASN B 1 363 ? 109.571 146.198 154.013 1.00 28.56 ?  363 ASN B N     1 
ATOM   8497  C  CA    . ASN B 1 363 ? 110.154 146.323 155.344 1.00 13.54 ?  363 ASN B CA    1 
ATOM   8498  C  C     . ASN B 1 363 ? 111.331 147.290 155.332 1.00 19.84 ?  363 ASN B C     1 
ATOM   8499  O  O     . ASN B 1 363 ? 111.512 148.069 156.274 1.00 25.82 ?  363 ASN B O     1 
ATOM   8500  C  CB    . ASN B 1 363 ? 110.593 144.953 155.862 1.00 10.51 ?  363 ASN B CB    1 
ATOM   8501  C  CG    . ASN B 1 363 ? 109.441 144.141 156.409 1.00 17.88 ?  363 ASN B CG    1 
ATOM   8502  O  OD1   . ASN B 1 363 ? 108.332 144.645 156.568 1.00 22.12 ?  363 ASN B OD1   1 
ATOM   8503  N  ND2   . ASN B 1 363 ? 109.700 142.875 156.706 1.00 20.62 ?  363 ASN B ND2   1 
ATOM   8504  N  N     . VAL B 1 364 ? 112.141 147.248 154.275 1.00 17.04 ?  364 VAL B N     1 
ATOM   8505  C  CA    . VAL B 1 364 ? 113.271 148.161 154.161 1.00 10.09 ?  364 VAL B CA    1 
ATOM   8506  C  C     . VAL B 1 364 ? 112.786 149.592 153.969 1.00 19.58 ?  364 VAL B C     1 
ATOM   8507  O  O     . VAL B 1 364 ? 113.256 150.520 154.636 1.00 25.50 ?  364 VAL B O     1 
ATOM   8508  C  CB    . VAL B 1 364 ? 114.194 147.728 153.007 1.00 0.06  ?  364 VAL B CB    1 
ATOM   8509  C  CG1   . VAL B 1 364 ? 115.426 148.600 152.967 1.00 7.05  ?  364 VAL B CG1   1 
ATOM   8510  C  CG2   . VAL B 1 364 ? 114.571 146.269 153.146 1.00 3.59  ?  364 VAL B CG2   1 
ATOM   8511  N  N     . ASN B 1 365 ? 111.835 149.790 153.058 1.00 14.89 ?  365 ASN B N     1 
ATOM   8512  C  CA    . ASN B 1 365 ? 111.478 151.129 152.612 1.00 4.58  ?  365 ASN B CA    1 
ATOM   8513  C  C     . ASN B 1 365 ? 110.455 151.819 153.502 1.00 12.69 ?  365 ASN B C     1 
ATOM   8514  O  O     . ASN B 1 365 ? 110.271 153.033 153.369 1.00 24.10 ?  365 ASN B O     1 
ATOM   8515  C  CB    . ASN B 1 365 ? 110.956 151.073 151.178 1.00 18.94 ?  365 ASN B CB    1 
ATOM   8516  C  CG    . ASN B 1 365 ? 112.028 150.671 150.190 1.00 16.80 ?  365 ASN B CG    1 
ATOM   8517  O  OD1   . ASN B 1 365 ? 113.085 151.293 150.121 1.00 14.28 ?  365 ASN B OD1   1 
ATOM   8518  N  ND2   . ASN B 1 365 ? 111.764 149.625 149.423 1.00 18.87 ?  365 ASN B ND2   1 
ATOM   8519  N  N     . LYS B 1 366 ? 109.788 151.092 154.400 1.00 16.21 ?  366 LYS B N     1 
ATOM   8520  C  CA    . LYS B 1 366 ? 108.866 151.744 155.321 1.00 19.85 ?  366 LYS B CA    1 
ATOM   8521  C  C     . LYS B 1 366 ? 109.597 152.507 156.413 1.00 20.14 ?  366 LYS B C     1 
ATOM   8522  O  O     . LYS B 1 366 ? 109.016 153.414 157.018 1.00 30.80 ?  366 LYS B O     1 
ATOM   8523  C  CB    . LYS B 1 366 ? 107.915 150.716 155.935 1.00 16.52 ?  366 LYS B CB    1 
ATOM   8524  C  CG    . LYS B 1 366 ? 108.508 149.901 157.067 1.00 25.80 ?  366 LYS B CG    1 
ATOM   8525  C  CD    . LYS B 1 366 ? 107.418 149.209 157.864 1.00 28.53 ?  366 LYS B CD    1 
ATOM   8526  C  CE    . LYS B 1 366 ? 106.511 148.391 156.960 1.00 23.89 ?  366 LYS B CE    1 
ATOM   8527  N  NZ    . LYS B 1 366 ? 105.571 147.546 157.745 1.00 28.97 1  366 LYS B NZ    1 
ATOM   8528  N  N     . VAL B 1 367 ? 110.859 152.166 156.671 1.00 26.19 ?  367 VAL B N     1 
ATOM   8529  C  CA    . VAL B 1 367 ? 111.697 152.860 157.634 1.00 18.01 ?  367 VAL B CA    1 
ATOM   8530  C  C     . VAL B 1 367 ? 112.910 153.498 156.973 1.00 17.99 ?  367 VAL B C     1 
ATOM   8531  O  O     . VAL B 1 367 ? 113.786 154.017 157.660 1.00 23.59 ?  367 VAL B O     1 
ATOM   8532  C  CB    . VAL B 1 367 ? 112.131 151.916 158.773 1.00 14.88 ?  367 VAL B CB    1 
ATOM   8533  C  CG1   . VAL B 1 367 ? 110.933 151.528 159.619 1.00 17.71 ?  367 VAL B CG1   1 
ATOM   8534  C  CG2   . VAL B 1 367 ? 112.800 150.687 158.202 1.00 8.15  ?  367 VAL B CG2   1 
ATOM   8535  N  N     . HIS B 1 368 ? 112.980 153.457 155.644 1.00 17.51 ?  368 HIS B N     1 
ATOM   8536  C  CA    . HIS B 1 368 ? 114.095 154.054 154.926 1.00 3.61  ?  368 HIS B CA    1 
ATOM   8537  C  C     . HIS B 1 368 ? 114.040 155.570 155.048 1.00 17.40 ?  368 HIS B C     1 
ATOM   8538  O  O     . HIS B 1 368 ? 112.985 156.184 154.860 1.00 30.35 ?  368 HIS B O     1 
ATOM   8539  C  CB    . HIS B 1 368 ? 114.057 153.634 153.459 1.00 10.78 ?  368 HIS B CB    1 
ATOM   8540  C  CG    . HIS B 1 368 ? 115.249 154.076 152.670 1.00 6.15  ?  368 HIS B CG    1 
ATOM   8541  N  ND1   . HIS B 1 368 ? 115.169 154.433 151.343 1.00 18.67 ?  368 HIS B ND1   1 
ATOM   8542  C  CD2   . HIS B 1 368 ? 116.548 154.217 153.020 1.00 7.27  ?  368 HIS B CD2   1 
ATOM   8543  C  CE1   . HIS B 1 368 ? 116.368 154.774 150.907 1.00 17.56 ?  368 HIS B CE1   1 
ATOM   8544  N  NE2   . HIS B 1 368 ? 117.222 154.653 151.906 1.00 16.59 ?  368 HIS B NE2   1 
ATOM   8545  N  N     . ALA B 1 369 ? 115.181 156.175 155.366 1.00 20.81 ?  369 ALA B N     1 
ATOM   8546  C  CA    . ALA B 1 369 ? 115.251 157.609 155.601 1.00 13.95 ?  369 ALA B CA    1 
ATOM   8547  C  C     . ALA B 1 369 ? 115.531 158.413 154.341 1.00 25.08 ?  369 ALA B C     1 
ATOM   8548  O  O     . ALA B 1 369 ? 115.489 159.646 154.394 1.00 32.91 ?  369 ALA B O     1 
ATOM   8549  C  CB    . ALA B 1 369 ? 116.326 157.916 156.647 1.00 11.15 ?  369 ALA B CB    1 
ATOM   8550  N  N     . ASN B 1 370 ? 115.801 157.760 153.216 1.00 18.57 ?  370 ASN B N     1 
ATOM   8551  C  CA    . ASN B 1 370 ? 116.189 158.438 151.988 1.00 12.01 ?  370 ASN B CA    1 
ATOM   8552  C  C     . ASN B 1 370 ? 115.348 157.961 150.816 1.00 13.34 ?  370 ASN B C     1 
ATOM   8553  O  O     . ASN B 1 370 ? 115.854 157.748 149.713 1.00 24.87 ?  370 ASN B O     1 
ATOM   8554  C  CB    . ASN B 1 370 ? 117.674 158.237 151.702 1.00 12.83 ?  370 ASN B CB    1 
ATOM   8555  C  CG    . ASN B 1 370 ? 118.561 158.839 152.773 1.00 12.83 ?  370 ASN B CG    1 
ATOM   8556  O  OD1   . ASN B 1 370 ? 118.547 160.047 152.997 1.00 29.53 ?  370 ASN B OD1   1 
ATOM   8557  N  ND2   . ASN B 1 370 ? 119.336 157.996 153.440 1.00 12.13 ?  370 ASN B ND2   1 
ATOM   8558  N  N     . ASN B 1 371 ? 114.043 157.788 151.037 1.00 19.78 ?  371 ASN B N     1 
ATOM   8559  C  CA    . ASN B 1 371 ? 113.152 157.387 149.954 1.00 11.60 ?  371 ASN B CA    1 
ATOM   8560  C  C     . ASN B 1 371 ? 113.016 158.466 148.890 1.00 16.37 ?  371 ASN B C     1 
ATOM   8561  O  O     . ASN B 1 371 ? 112.666 158.151 147.749 1.00 26.99 ?  371 ASN B O     1 
ATOM   8562  C  CB    . ASN B 1 371 ? 111.771 157.029 150.505 1.00 9.05  ?  371 ASN B CB    1 
ATOM   8563  C  CG    . ASN B 1 371 ? 111.705 155.615 151.035 1.00 17.59 ?  371 ASN B CG    1 
ATOM   8564  O  OD1   . ASN B 1 371 ? 112.528 154.771 150.687 1.00 23.47 ?  371 ASN B OD1   1 
ATOM   8565  N  ND2   . ASN B 1 371 ? 110.722 155.348 151.884 1.00 24.49 ?  371 ASN B ND2   1 
ATOM   8566  N  N     . HIS B 1 372 ? 113.274 159.727 149.241 1.00 19.85 ?  372 HIS B N     1 
ATOM   8567  C  CA    . HIS B 1 372 ? 113.253 160.796 148.249 1.00 19.82 ?  372 HIS B CA    1 
ATOM   8568  C  C     . HIS B 1 372 ? 114.350 160.602 147.211 1.00 22.75 ?  372 HIS B C     1 
ATOM   8569  O  O     . HIS B 1 372 ? 114.134 160.838 146.017 1.00 28.09 ?  372 HIS B O     1 
ATOM   8570  C  CB    . HIS B 1 372 ? 113.397 162.153 148.938 1.00 23.38 ?  372 HIS B CB    1 
ATOM   8571  C  CG    . HIS B 1 372 ? 114.728 162.358 149.589 1.00 22.20 ?  372 HIS B CG    1 
ATOM   8572  N  ND1   . HIS B 1 372 ? 115.163 161.593 150.649 1.00 21.74 ?  372 HIS B ND1   1 
ATOM   8573  C  CD2   . HIS B 1 372 ? 115.724 163.236 149.327 1.00 24.73 ?  372 HIS B CD2   1 
ATOM   8574  C  CE1   . HIS B 1 372 ? 116.369 161.989 151.011 1.00 20.00 ?  372 HIS B CE1   1 
ATOM   8575  N  NE2   . HIS B 1 372 ? 116.731 162.988 150.227 1.00 23.90 ?  372 HIS B NE2   1 
ATOM   8576  N  N     . ILE B 1 373 ? 115.539 160.188 147.650 1.00 16.66 ?  373 ILE B N     1 
ATOM   8577  C  CA    . ILE B 1 373 ? 116.621 159.900 146.713 1.00 19.92 ?  373 ILE B CA    1 
ATOM   8578  C  C     . ILE B 1 373 ? 116.245 158.722 145.829 1.00 21.25 ?  373 ILE B C     1 
ATOM   8579  O  O     . ILE B 1 373 ? 116.329 158.789 144.598 1.00 37.31 ?  373 ILE B O     1 
ATOM   8580  C  CB    . ILE B 1 373 ? 117.932 159.635 147.475 1.00 24.82 ?  373 ILE B CB    1 
ATOM   8581  C  CG1   . ILE B 1 373 ? 118.368 160.882 148.239 1.00 21.51 ?  373 ILE B CG1   1 
ATOM   8582  C  CG2   . ILE B 1 373 ? 119.022 159.177 146.521 1.00 21.97 ?  373 ILE B CG2   1 
ATOM   8583  C  CD1   . ILE B 1 373 ? 119.391 160.608 149.309 1.00 18.19 ?  373 ILE B CD1   1 
ATOM   8584  N  N     . SER B 1 374 ? 115.805 157.631 146.450 1.00 15.22 ?  374 SER B N     1 
ATOM   8585  C  CA    . SER B 1 374 ? 115.372 156.417 145.778 1.00 10.77 ?  374 SER B CA    1 
ATOM   8586  C  C     . SER B 1 374 ? 114.896 155.446 146.844 1.00 20.36 ?  374 SER B C     1 
ATOM   8587  O  O     . SER B 1 374 ? 115.252 155.568 148.019 1.00 23.07 ?  374 SER B O     1 
ATOM   8588  C  CB    . SER B 1 374 ? 116.494 155.782 144.952 1.00 21.86 ?  374 SER B CB    1 
ATOM   8589  O  OG    . SER B 1 374 ? 115.998 154.742 144.134 1.00 35.99 ?  374 SER B OG    1 
ATOM   8590  N  N     . LYS B 1 375 ? 114.082 154.485 146.426 1.00 26.47 ?  375 LYS B N     1 
ATOM   8591  C  CA    . LYS B 1 375 ? 113.783 153.357 147.287 1.00 12.12 ?  375 LYS B CA    1 
ATOM   8592  C  C     . LYS B 1 375 ? 114.955 152.383 147.282 1.00 15.13 ?  375 LYS B C     1 
ATOM   8593  O  O     . LYS B 1 375 ? 115.756 152.340 146.344 1.00 28.03 ?  375 LYS B O     1 
ATOM   8594  C  CB    . LYS B 1 375 ? 112.508 152.650 146.827 1.00 14.41 ?  375 LYS B CB    1 
ATOM   8595  C  CG    . LYS B 1 375 ? 111.270 153.525 146.824 1.00 18.59 ?  375 LYS B CG    1 
ATOM   8596  C  CD    . LYS B 1 375 ? 110.693 153.665 148.217 1.00 21.94 ?  375 LYS B CD    1 
ATOM   8597  C  CE    . LYS B 1 375 ? 109.179 153.732 148.181 1.00 23.73 ?  375 LYS B CE    1 
ATOM   8598  N  NZ    . LYS B 1 375 ? 108.699 155.136 148.080 1.00 26.61 1  375 LYS B NZ    1 
ATOM   8599  N  N     . VAL B 1 376 ? 115.063 151.601 148.349 1.00 12.10 ?  376 VAL B N     1 
ATOM   8600  C  CA    . VAL B 1 376 ? 116.048 150.527 148.396 1.00 13.01 ?  376 VAL B CA    1 
ATOM   8601  C  C     . VAL B 1 376 ? 115.505 149.363 147.578 1.00 15.90 ?  376 VAL B C     1 
ATOM   8602  O  O     . VAL B 1 376 ? 114.461 148.792 147.907 1.00 25.73 ?  376 VAL B O     1 
ATOM   8603  C  CB    . VAL B 1 376 ? 116.347 150.102 149.839 1.00 9.66  ?  376 VAL B CB    1 
ATOM   8604  C  CG1   . VAL B 1 376 ? 117.391 148.996 149.863 1.00 5.98  ?  376 VAL B CG1   1 
ATOM   8605  C  CG2   . VAL B 1 376 ? 116.805 151.293 150.659 1.00 6.35  ?  376 VAL B CG2   1 
ATOM   8606  N  N     . LYS B 1 377 ? 116.211 149.012 146.505 1.00 14.65 ?  377 LYS B N     1 
ATOM   8607  C  CA    . LYS B 1 377 ? 115.738 147.988 145.586 1.00 13.59 ?  377 LYS B CA    1 
ATOM   8608  C  C     . LYS B 1 377 ? 116.430 146.648 145.762 1.00 8.55  ?  377 LYS B C     1 
ATOM   8609  O  O     . LYS B 1 377 ? 115.874 145.628 145.346 1.00 25.31 ?  377 LYS B O     1 
ATOM   8610  C  CB    . LYS B 1 377 ? 115.921 148.450 144.137 1.00 16.40 ?  377 LYS B CB    1 
ATOM   8611  C  CG    . LYS B 1 377 ? 115.155 149.705 143.784 1.00 9.68  ?  377 LYS B CG    1 
ATOM   8612  C  CD    . LYS B 1 377 ? 115.814 150.411 142.621 1.00 20.92 ?  377 LYS B CD    1 
ATOM   8613  C  CE    . LYS B 1 377 ? 115.744 151.912 142.780 1.00 25.14 ?  377 LYS B CE    1 
ATOM   8614  N  NZ    . LYS B 1 377 ? 116.704 152.610 141.884 1.00 23.03 1  377 LYS B NZ    1 
ATOM   8615  N  N     . PHE B 1 378 ? 117.617 146.624 146.357 1.00 6.05  ?  378 PHE B N     1 
ATOM   8616  C  CA    . PHE B 1 378 ? 118.369 145.387 146.511 1.00 5.14  ?  378 PHE B CA    1 
ATOM   8617  C  C     . PHE B 1 378 ? 119.426 145.594 147.584 1.00 10.46 ?  378 PHE B C     1 
ATOM   8618  O  O     . PHE B 1 378 ? 119.624 146.702 148.087 1.00 14.98 ?  378 PHE B O     1 
ATOM   8619  C  CB    . PHE B 1 378 ? 118.992 144.935 145.185 1.00 2.96  ?  378 PHE B CB    1 
ATOM   8620  C  CG    . PHE B 1 378 ? 120.127 145.799 144.706 1.00 7.80  ?  378 PHE B CG    1 
ATOM   8621  C  CD1   . PHE B 1 378 ? 119.951 147.156 144.495 1.00 14.95 ?  378 PHE B CD1   1 
ATOM   8622  C  CD2   . PHE B 1 378 ? 121.366 145.244 144.438 1.00 4.48  ?  378 PHE B CD2   1 
ATOM   8623  C  CE1   . PHE B 1 378 ? 120.988 147.941 144.046 1.00 6.75  ?  378 PHE B CE1   1 
ATOM   8624  C  CE2   . PHE B 1 378 ? 122.406 146.027 143.986 1.00 7.80  ?  378 PHE B CE2   1 
ATOM   8625  C  CZ    . PHE B 1 378 ? 122.216 147.377 143.790 1.00 9.48  ?  378 PHE B CZ    1 
ATOM   8626  N  N     . SER B 1 379 ? 120.103 144.507 147.929 1.00 2.51  ?  379 SER B N     1 
ATOM   8627  C  CA    . SER B 1 379 ? 121.098 144.488 148.990 1.00 7.97  ?  379 SER B CA    1 
ATOM   8628  C  C     . SER B 1 379 ? 122.440 144.043 148.423 1.00 8.40  ?  379 SER B C     1 
ATOM   8629  O  O     . SER B 1 379 ? 122.596 143.834 147.219 1.00 19.01 ?  379 SER B O     1 
ATOM   8630  C  CB    . SER B 1 379 ? 120.653 143.573 150.133 1.00 6.80  ?  379 SER B CB    1 
ATOM   8631  O  OG    . SER B 1 379 ? 121.150 144.035 151.372 1.00 10.43 ?  379 SER B OG    1 
ATOM   8632  N  N     . ASN B 1 380 ? 123.418 143.899 149.311 1.00 10.17 ?  380 ASN B N     1 
ATOM   8633  C  CA    . ASN B 1 380 ? 124.773 143.549 148.919 1.00 7.85  ?  380 ASN B CA    1 
ATOM   8634  C  C     . ASN B 1 380 ? 124.944 142.031 148.935 1.00 13.89 ?  380 ASN B C     1 
ATOM   8635  O  O     . ASN B 1 380 ? 123.978 141.271 149.038 1.00 20.08 ?  380 ASN B O     1 
ATOM   8636  C  CB    . ASN B 1 380 ? 125.786 144.245 149.826 1.00 8.11  ?  380 ASN B CB    1 
ATOM   8637  C  CG    . ASN B 1 380 ? 125.699 143.784 151.261 1.00 8.77  ?  380 ASN B CG    1 
ATOM   8638  O  OD1   . ASN B 1 380 ? 124.610 143.608 151.802 1.00 22.19 ?  380 ASN B OD1   1 
ATOM   8639  N  ND2   . ASN B 1 380 ? 126.849 143.603 151.893 1.00 17.17 ?  380 ASN B ND2   1 
ATOM   8640  N  N     . LEU B 1 381 ? 126.192 141.579 148.820 1.00 19.78 ?  381 LEU B N     1 
ATOM   8641  C  CA    . LEU B 1 381 ? 126.487 140.153 148.840 1.00 8.77  ?  381 LEU B CA    1 
ATOM   8642  C  C     . LEU B 1 381 ? 126.254 139.535 150.212 1.00 6.62  ?  381 LEU B C     1 
ATOM   8643  O  O     . LEU B 1 381 ? 126.049 138.320 150.305 1.00 22.70 ?  381 LEU B O     1 
ATOM   8644  C  CB    . LEU B 1 381 ? 127.931 139.931 148.383 1.00 17.60 ?  381 LEU B CB    1 
ATOM   8645  C  CG    . LEU B 1 381 ? 128.558 138.537 148.408 1.00 20.47 ?  381 LEU B CG    1 
ATOM   8646  C  CD1   . LEU B 1 381 ? 127.815 137.579 147.496 1.00 22.72 ?  381 LEU B CD1   1 
ATOM   8647  C  CD2   . LEU B 1 381 ? 130.017 138.623 148.017 1.00 15.48 ?  381 LEU B CD2   1 
ATOM   8648  N  N     . CYS B 1 382 ? 126.267 140.339 151.273 1.00 21.44 ?  382 CYS B N     1 
ATOM   8649  C  CA    . CYS B 1 382 ? 126.058 139.849 152.627 1.00 3.70  ?  382 CYS B CA    1 
ATOM   8650  C  C     . CYS B 1 382 ? 124.695 140.222 153.192 1.00 12.64 ?  382 CYS B C     1 
ATOM   8651  O  O     . CYS B 1 382 ? 124.415 139.903 154.351 1.00 23.34 ?  382 CYS B O     1 
ATOM   8652  C  CB    . CYS B 1 382 ? 127.167 140.366 153.550 1.00 20.70 ?  382 CYS B CB    1 
ATOM   8653  S  SG    . CYS B 1 382 ? 128.846 140.008 152.979 1.00 37.09 ?  382 CYS B SG    1 
ATOM   8654  N  N     . SER B 1 383 ? 123.852 140.905 152.412 1.00 15.80 ?  383 SER B N     1 
ATOM   8655  C  CA    . SER B 1 383 ? 122.441 141.126 152.730 1.00 11.02 ?  383 SER B CA    1 
ATOM   8656  C  C     . SER B 1 383 ? 122.233 142.054 153.925 1.00 18.31 ?  383 SER B C     1 
ATOM   8657  O  O     . SER B 1 383 ? 121.243 141.926 154.646 1.00 27.77 ?  383 SER B O     1 
ATOM   8658  C  CB    . SER B 1 383 ? 121.710 139.800 152.966 1.00 8.16  ?  383 SER B CB    1 
ATOM   8659  O  OG    . SER B 1 383 ? 121.745 138.990 151.808 1.00 36.35 ?  383 SER B OG    1 
ATOM   8660  N  N     . GLU B 1 384 ? 123.143 142.996 154.158 1.00 11.76 ?  384 GLU B N     1 
ATOM   8661  C  CA    . GLU B 1 384 ? 122.951 143.971 155.221 1.00 9.89  ?  384 GLU B CA    1 
ATOM   8662  C  C     . GLU B 1 384 ? 122.998 145.416 154.746 1.00 16.66 ?  384 GLU B C     1 
ATOM   8663  O  O     . GLU B 1 384 ? 122.550 146.302 155.482 1.00 26.21 ?  384 GLU B O     1 
ATOM   8664  C  CB    . GLU B 1 384 ? 123.990 143.771 156.337 1.00 9.21  ?  384 GLU B CB    1 
ATOM   8665  C  CG    . GLU B 1 384 ? 125.201 144.679 156.256 1.00 11.23 ?  384 GLU B CG    1 
ATOM   8666  C  CD    . GLU B 1 384 ? 126.250 144.163 155.302 1.00 22.17 ?  384 GLU B CD    1 
ATOM   8667  O  OE1   . GLU B 1 384 ? 126.135 143.000 154.876 1.00 23.44 ?  384 GLU B OE1   1 
ATOM   8668  O  OE2   . GLU B 1 384 ? 127.192 144.916 154.987 1.00 29.48 -1 384 GLU B OE2   1 
ATOM   8669  N  N     . VAL B 1 385 ? 123.508 145.681 153.552 1.00 11.10 ?  385 VAL B N     1 
ATOM   8670  C  CA    . VAL B 1 385 ? 123.582 147.037 153.025 1.00 2.81  ?  385 VAL B CA    1 
ATOM   8671  C  C     . VAL B 1 385 ? 122.276 147.344 152.308 1.00 17.93 ?  385 VAL B C     1 
ATOM   8672  O  O     . VAL B 1 385 ? 121.929 146.688 151.322 1.00 25.12 ?  385 VAL B O     1 
ATOM   8673  C  CB    . VAL B 1 385 ? 124.780 147.203 152.081 1.00 5.27  ?  385 VAL B CB    1 
ATOM   8674  C  CG1   . VAL B 1 385 ? 124.750 148.568 151.446 1.00 8.53  ?  385 VAL B CG1   1 
ATOM   8675  C  CG2   . VAL B 1 385 ? 126.071 147.007 152.840 1.00 8.98  ?  385 VAL B CG2   1 
ATOM   8676  N  N     . LEU B 1 386 ? 121.548 148.343 152.808 1.00 19.30 ?  386 LEU B N     1 
ATOM   8677  C  CA    . LEU B 1 386 ? 120.237 148.721 152.282 1.00 2.15  ?  386 LEU B CA    1 
ATOM   8678  C  C     . LEU B 1 386 ? 120.222 150.234 152.109 1.00 5.61  ?  386 LEU B C     1 
ATOM   8679  O  O     . LEU B 1 386 ? 119.875 150.971 153.035 1.00 12.33 ?  386 LEU B O     1 
ATOM   8680  C  CB    . LEU B 1 386 ? 119.127 148.241 153.205 1.00 5.81  ?  386 LEU B CB    1 
ATOM   8681  C  CG    . LEU B 1 386 ? 119.025 146.721 153.318 1.00 0.77  ?  386 LEU B CG    1 
ATOM   8682  C  CD1   . LEU B 1 386 ? 117.995 146.340 154.345 1.00 7.88  ?  386 LEU B CD1   1 
ATOM   8683  C  CD2   . LEU B 1 386 ? 118.688 146.115 151.968 1.00 6.73  ?  386 LEU B CD2   1 
ATOM   8684  N  N     . GLN B 1 387 ? 120.599 150.696 150.920 1.00 13.17 ?  387 GLN B N     1 
ATOM   8685  C  CA    . GLN B 1 387 ? 120.729 152.114 150.636 1.00 3.15  ?  387 GLN B CA    1 
ATOM   8686  C  C     . GLN B 1 387 ? 120.054 152.446 149.314 1.00 8.38  ?  387 GLN B C     1 
ATOM   8687  O  O     . GLN B 1 387 ? 119.837 151.579 148.466 1.00 22.69 ?  387 GLN B O     1 
ATOM   8688  C  CB    . GLN B 1 387 ? 122.202 152.540 150.596 1.00 0.56  ?  387 GLN B CB    1 
ATOM   8689  C  CG    . GLN B 1 387 ? 122.978 152.154 151.835 1.00 4.37  ?  387 GLN B CG    1 
ATOM   8690  C  CD    . GLN B 1 387 ? 124.397 152.654 151.810 1.00 10.53 ?  387 GLN B CD    1 
ATOM   8691  O  OE1   . GLN B 1 387 ? 124.752 153.511 151.004 1.00 20.68 ?  387 GLN B OE1   1 
ATOM   8692  N  NE2   . GLN B 1 387 ? 125.224 152.121 152.694 1.00 9.52  ?  387 GLN B NE2   1 
ATOM   8693  N  N     . ALA B 1 388 ? 119.714 153.721 149.157 1.00 9.62  ?  388 ALA B N     1 
ATOM   8694  C  CA    . ALA B 1 388 ? 119.130 154.197 147.911 1.00 7.64  ?  388 ALA B CA    1 
ATOM   8695  C  C     . ALA B 1 388 ? 120.162 154.171 146.792 1.00 14.26 ?  388 ALA B C     1 
ATOM   8696  O  O     . ALA B 1 388 ? 121.328 154.527 146.990 1.00 25.40 ?  388 ALA B O     1 
ATOM   8697  C  CB    . ALA B 1 388 ? 118.585 155.612 148.087 1.00 11.59 ?  388 ALA B CB    1 
ATOM   8698  N  N     . SER B 1 389 ? 119.729 153.749 145.610 1.00 19.81 ?  389 SER B N     1 
ATOM   8699  C  CA    . SER B 1 389 ? 120.588 153.688 144.441 1.00 8.84  ?  389 SER B CA    1 
ATOM   8700  C  C     . SER B 1 389 ? 119.877 154.310 143.250 1.00 12.83 ?  389 SER B C     1 
ATOM   8701  O  O     . SER B 1 389 ? 118.648 154.296 143.161 1.00 23.31 ?  389 SER B O     1 
ATOM   8702  C  CB    . SER B 1 389 ? 120.987 152.245 144.107 1.00 17.11 ?  389 SER B CB    1 
ATOM   8703  O  OG    . SER B 1 389 ? 119.855 151.394 144.090 1.00 23.86 ?  389 SER B OG    1 
ATOM   8704  N  N     . GLN B 1 390 ? 120.667 154.859 142.333 1.00 22.95 ?  390 GLN B N     1 
ATOM   8705  C  CA    . GLN B 1 390 ? 120.161 155.398 141.081 1.00 12.92 ?  390 GLN B CA    1 
ATOM   8706  C  C     . GLN B 1 390 ? 120.920 154.741 139.942 1.00 14.09 ?  390 GLN B C     1 
ATOM   8707  O  O     . GLN B 1 390 ? 122.154 154.687 139.966 1.00 25.00 ?  390 GLN B O     1 
ATOM   8708  C  CB    . GLN B 1 390 ? 120.313 156.920 141.027 1.00 10.67 ?  390 GLN B CB    1 
ATOM   8709  C  CG    . GLN B 1 390 ? 119.365 157.654 141.953 1.00 11.92 ?  390 GLN B CG    1 
ATOM   8710  C  CD    . GLN B 1 390 ? 119.583 159.150 141.945 1.00 26.59 ?  390 GLN B CD    1 
ATOM   8711  O  OE1   . GLN B 1 390 ? 120.532 159.647 141.340 1.00 33.24 ?  390 GLN B OE1   1 
ATOM   8712  N  NE2   . GLN B 1 390 ? 118.704 159.877 142.622 1.00 18.02 ?  390 GLN B NE2   1 
ATOM   8713  N  N     . VAL B 1 391 ? 120.187 154.235 138.954 1.00 26.31 ?  391 VAL B N     1 
ATOM   8714  C  CA    . VAL B 1 391 ? 120.820 153.523 137.853 1.00 20.02 ?  391 VAL B CA    1 
ATOM   8715  C  C     . VAL B 1 391 ? 121.539 154.513 136.948 1.00 25.64 ?  391 VAL B C     1 
ATOM   8716  O  O     . VAL B 1 391 ? 121.080 155.643 136.731 1.00 22.59 ?  391 VAL B O     1 
ATOM   8717  C  CB    . VAL B 1 391 ? 119.780 152.690 137.081 1.00 15.69 ?  391 VAL B CB    1 
ATOM   8718  C  CG1   . VAL B 1 391 ? 118.838 153.584 136.287 1.00 16.52 ?  391 VAL B CG1   1 
ATOM   8719  C  CG2   . VAL B 1 391 ? 120.472 151.681 136.178 1.00 17.13 ?  391 VAL B CG2   1 
ATOM   8720  N  N     . SER B 1 392 ? 122.695 154.102 136.441 1.00 32.86 ?  392 SER B N     1 
ATOM   8721  C  CA    . SER B 1 392 ? 123.469 154.921 135.525 1.00 21.49 ?  392 SER B CA    1 
ATOM   8722  C  C     . SER B 1 392 ? 123.084 154.608 134.087 1.00 28.88 ?  392 SER B C     1 
ATOM   8723  O  O     . SER B 1 392 ? 122.750 153.472 133.743 1.00 31.81 ?  392 SER B O     1 
ATOM   8724  C  CB    . SER B 1 392 ? 124.967 154.693 135.723 1.00 25.83 ?  392 SER B CB    1 
ATOM   8725  O  OG    . SER B 1 392 ? 125.344 154.906 137.070 1.00 36.93 ?  392 SER B OG    1 
ATOM   8726  N  N     . SER B 1 393 ? 123.132 155.634 133.248 1.00 35.47 ?  393 SER B N     1 
ATOM   8727  C  CA    . SER B 1 393 ? 122.845 155.507 131.823 1.00 28.19 ?  393 SER B CA    1 
ATOM   8728  C  C     . SER B 1 393 ? 124.177 155.596 131.084 1.00 32.27 ?  393 SER B C     1 
ATOM   8729  O  O     . SER B 1 393 ? 124.618 156.678 130.694 1.00 35.82 ?  393 SER B O     1 
ATOM   8730  C  CB    . SER B 1 393 ? 121.870 156.581 131.360 1.00 31.94 ?  393 SER B CB    1 
ATOM   8731  O  OG    . SER B 1 393 ? 120.786 156.702 132.264 1.00 43.25 ?  393 SER B OG    1 
ATOM   8732  N  N     . TYR B 1 394 ? 124.817 154.446 130.897 1.00 32.45 ?  394 TYR B N     1 
ATOM   8733  C  CA    . TYR B 1 394 ? 126.069 154.379 130.153 1.00 29.04 ?  394 TYR B CA    1 
ATOM   8734  C  C     . TYR B 1 394 ? 125.742 154.354 128.667 1.00 30.77 ?  394 TYR B C     1 
ATOM   8735  O  O     . TYR B 1 394 ? 125.177 153.379 128.162 1.00 34.55 ?  394 TYR B O     1 
ATOM   8736  C  CB    . TYR B 1 394 ? 126.877 153.155 130.568 1.00 28.80 ?  394 TYR B CB    1 
ATOM   8737  C  CG    . TYR B 1 394 ? 127.296 153.172 132.019 1.00 28.49 ?  394 TYR B CG    1 
ATOM   8738  C  CD1   . TYR B 1 394 ? 128.291 154.031 132.465 1.00 29.28 ?  394 TYR B CD1   1 
ATOM   8739  C  CD2   . TYR B 1 394 ? 126.694 152.332 132.944 1.00 25.63 ?  394 TYR B CD2   1 
ATOM   8740  C  CE1   . TYR B 1 394 ? 128.676 154.050 133.790 1.00 29.53 ?  394 TYR B CE1   1 
ATOM   8741  C  CE2   . TYR B 1 394 ? 127.072 152.342 134.269 1.00 26.56 ?  394 TYR B CE2   1 
ATOM   8742  C  CZ    . TYR B 1 394 ? 128.061 153.203 134.688 1.00 36.49 ?  394 TYR B CZ    1 
ATOM   8743  O  OH    . TYR B 1 394 ? 128.438 153.214 136.012 1.00 40.21 ?  394 TYR B OH    1 
ATOM   8744  N  N     . THR B 1 395 ? 126.088 155.428 127.971 1.00 38.04 ?  395 THR B N     1 
ATOM   8745  C  CA    . THR B 1 395 ? 125.736 155.609 126.573 1.00 33.83 ?  395 THR B CA    1 
ATOM   8746  C  C     . THR B 1 395 ? 126.845 155.051 125.683 1.00 37.74 ?  395 THR B C     1 
ATOM   8747  O  O     . THR B 1 395 ? 127.740 154.335 126.139 1.00 34.98 ?  395 THR B O     1 
ATOM   8748  C  CB    . THR B 1 395 ? 125.467 157.083 126.295 1.00 36.13 ?  395 THR B CB    1 
ATOM   8749  O  OG1   . THR B 1 395 ? 126.657 157.839 126.549 1.00 37.24 ?  395 THR B OG1   1 
ATOM   8750  C  CG2   . THR B 1 395 ? 124.355 157.596 127.194 1.00 35.65 ?  395 THR B CG2   1 
ATOM   8751  N  N     . ASP B 1 396 ? 126.791 155.375 124.393 1.00 40.82 ?  396 ASP B N     1 
ATOM   8752  C  CA    . ASP B 1 396 ? 127.824 154.944 123.467 1.00 34.89 ?  396 ASP B CA    1 
ATOM   8753  C  C     . ASP B 1 396 ? 129.162 155.590 123.825 1.00 39.22 ?  396 ASP B C     1 
ATOM   8754  O  O     . ASP B 1 396 ? 129.248 156.490 124.664 1.00 46.61 ?  396 ASP B O     1 
ATOM   8755  C  CB    . ASP B 1 396 ? 127.432 155.284 122.030 1.00 39.86 ?  396 ASP B CB    1 
ATOM   8756  C  CG    . ASP B 1 396 ? 126.202 154.529 121.567 1.00 45.72 ?  396 ASP B CG    1 
ATOM   8757  O  OD1   . ASP B 1 396 ? 126.134 153.304 121.798 1.00 42.96 ?  396 ASP B OD1   1 
ATOM   8758  O  OD2   . ASP B 1 396 ? 125.307 155.158 120.968 1.00 46.25 -1 396 ASP B OD2   1 
ATOM   8759  N  N     . TYR B 1 397 ? 130.219 155.110 123.169 1.00 32.24 ?  397 TYR B N     1 
ATOM   8760  C  CA    . TYR B 1 397 ? 131.568 155.547 123.511 1.00 34.09 ?  397 TYR B CA    1 
ATOM   8761  C  C     . TYR B 1 397 ? 131.744 157.045 123.285 1.00 34.30 ?  397 TYR B C     1 
ATOM   8762  O  O     . TYR B 1 397 ? 132.378 157.731 124.094 1.00 41.35 ?  397 TYR B O     1 
ATOM   8763  C  CB    . TYR B 1 397 ? 132.594 154.752 122.705 1.00 32.22 ?  397 TYR B CB    1 
ATOM   8764  C  CG    . TYR B 1 397 ? 134.026 155.187 122.918 1.00 31.70 ?  397 TYR B CG    1 
ATOM   8765  C  CD1   . TYR B 1 397 ? 134.589 156.198 122.149 1.00 32.38 ?  397 TYR B CD1   1 
ATOM   8766  C  CD2   . TYR B 1 397 ? 134.817 154.585 123.886 1.00 28.43 ?  397 TYR B CD2   1 
ATOM   8767  C  CE1   . TYR B 1 397 ? 135.892 156.598 122.340 1.00 33.34 ?  397 TYR B CE1   1 
ATOM   8768  C  CE2   . TYR B 1 397 ? 136.123 154.978 124.083 1.00 30.86 ?  397 TYR B CE2   1 
ATOM   8769  C  CZ    . TYR B 1 397 ? 136.655 155.985 123.308 1.00 36.04 ?  397 TYR B CZ    1 
ATOM   8770  O  OH    . TYR B 1 397 ? 137.956 156.382 123.499 1.00 39.42 ?  397 TYR B OH    1 
ATOM   8771  N  N     . ASP B 1 398 ? 131.197 157.568 122.187 1.00 43.33 ?  398 ASP B N     1 
ATOM   8772  C  CA    . ASP B 1 398 ? 131.382 158.980 121.873 1.00 43.51 ?  398 ASP B CA    1 
ATOM   8773  C  C     . ASP B 1 398 ? 130.539 159.881 122.767 1.00 47.22 ?  398 ASP B C     1 
ATOM   8774  O  O     . ASP B 1 398 ? 130.906 161.038 122.998 1.00 49.56 ?  398 ASP B O     1 
ATOM   8775  C  CB    . ASP B 1 398 ? 131.052 159.237 120.403 1.00 45.31 ?  398 ASP B CB    1 
ATOM   8776  C  CG    . ASP B 1 398 ? 129.806 158.502 119.949 1.00 49.08 ?  398 ASP B CG    1 
ATOM   8777  O  OD1   . ASP B 1 398 ? 129.743 157.268 120.134 1.00 47.02 ?  398 ASP B OD1   1 
ATOM   8778  O  OD2   . ASP B 1 398 ? 128.891 159.155 119.405 1.00 51.13 -1 398 ASP B OD2   1 
ATOM   8779  N  N     . GLU B 1 399 ? 129.420 159.378 123.274 1.00 46.85 ?  399 GLU B N     1 
ATOM   8780  C  CA    . GLU B 1 399 ? 128.489 160.182 124.049 1.00 42.12 ?  399 GLU B CA    1 
ATOM   8781  C  C     . GLU B 1 399 ? 128.921 160.265 125.511 1.00 48.56 ?  399 GLU B C     1 
ATOM   8782  O  O     . GLU B 1 399 ? 129.829 159.566 125.966 1.00 48.89 ?  399 GLU B O     1 
ATOM   8783  C  CB    . GLU B 1 399 ? 127.077 159.608 123.943 1.00 44.22 ?  399 GLU B CB    1 
ATOM   8784  C  CG    . GLU B 1 399 ? 126.421 159.829 122.596 1.00 48.53 ?  399 GLU B CG    1 
ATOM   8785  C  CD    . GLU B 1 399 ? 125.378 158.779 122.281 1.00 52.02 ?  399 GLU B CD    1 
ATOM   8786  O  OE1   . GLU B 1 399 ? 124.778 158.234 123.231 1.00 50.37 ?  399 GLU B OE1   1 
ATOM   8787  O  OE2   . GLU B 1 399 ? 125.158 158.500 121.084 1.00 53.71 -1 399 GLU B OE2   1 
ATOM   8788  N  N     . GLU B 1 400 ? 128.250 161.145 126.250 1.00 47.89 ?  400 GLU B N     1 
ATOM   8789  C  CA    . GLU B 1 400 ? 128.514 161.341 127.669 1.00 41.02 ?  400 GLU B CA    1 
ATOM   8790  C  C     . GLU B 1 400 ? 127.572 160.475 128.495 1.00 44.36 ?  400 GLU B C     1 
ATOM   8791  O  O     . GLU B 1 400 ? 126.358 160.479 128.271 1.00 43.18 ?  400 GLU B O     1 
ATOM   8792  C  CB    . GLU B 1 400 ? 128.347 162.812 128.051 1.00 41.65 ?  400 GLU B CB    1 
ATOM   8793  C  CG    . GLU B 1 400 ? 129.569 163.674 127.785 1.00 47.55 ?  400 GLU B CG    1 
ATOM   8794  C  CD    . GLU B 1 400 ? 130.790 163.213 128.557 1.00 52.56 ?  400 GLU B CD    1 
ATOM   8795  O  OE1   . GLU B 1 400 ? 130.637 162.792 129.723 1.00 52.78 ?  400 GLU B OE1   1 
ATOM   8796  O  OE2   . GLU B 1 400 ? 131.906 163.276 127.999 1.00 49.93 -1 400 GLU B OE2   1 
ATOM   8797  N  N     . ASP B 1 401 ? 128.135 159.739 129.448 1.00 42.88 ?  401 ASP B N     1 
ATOM   8798  C  CA    . ASP B 1 401 ? 127.340 158.870 130.300 1.00 37.73 ?  401 ASP B CA    1 
ATOM   8799  C  C     . ASP B 1 401 ? 126.607 159.675 131.366 1.00 39.48 ?  401 ASP B C     1 
ATOM   8800  O  O     . ASP B 1 401 ? 127.066 160.731 131.805 1.00 43.20 ?  401 ASP B O     1 
ATOM   8801  C  CB    . ASP B 1 401 ? 128.223 157.819 130.971 1.00 37.41 ?  401 ASP B CB    1 
ATOM   8802  C  CG    . ASP B 1 401 ? 128.893 156.897 129.978 1.00 40.11 ?  401 ASP B CG    1 
ATOM   8803  O  OD1   . ASP B 1 401 ? 128.267 156.572 128.948 1.00 44.10 ?  401 ASP B OD1   1 
ATOM   8804  O  OD2   . ASP B 1 401 ? 130.048 156.499 130.227 1.00 40.53 -1 401 ASP B OD2   1 
ATOM   8805  N  N     . GLU B 1 402 ? 125.454 159.157 131.780 1.00 38.02 ?  402 GLU B N     1 
ATOM   8806  C  CA    . GLU B 1 402 ? 124.672 159.734 132.869 1.00 32.62 ?  402 GLU B CA    1 
ATOM   8807  C  C     . GLU B 1 402 ? 124.947 158.902 134.116 1.00 34.97 ?  402 GLU B C     1 
ATOM   8808  O  O     . GLU B 1 402 ? 124.368 157.830 134.303 1.00 39.72 ?  402 GLU B O     1 
ATOM   8809  C  CB    . GLU B 1 402 ? 123.186 159.759 132.526 1.00 37.87 ?  402 GLU B CB    1 
ATOM   8810  C  CG    . GLU B 1 402 ? 122.543 161.149 132.379 1.00 41.50 ?  402 GLU B CG    1 
ATOM   8811  C  CD    . GLU B 1 402 ? 122.646 162.062 133.606 1.00 48.02 ?  402 GLU B CD    1 
ATOM   8812  O  OE1   . GLU B 1 402 ? 121.883 163.049 133.651 1.00 46.69 ?  402 GLU B OE1   1 
ATOM   8813  O  OE2   . GLU B 1 402 ? 123.448 161.810 134.531 1.00 49.75 -1 402 GLU B OE2   1 
ATOM   8814  N  N     . ILE B 1 403 ? 125.829 159.404 134.971 1.00 32.50 ?  403 ILE B N     1 
ATOM   8815  C  CA    . ILE B 1 403 ? 126.286 158.651 136.133 1.00 28.63 ?  403 ILE B CA    1 
ATOM   8816  C  C     . ILE B 1 403 ? 125.256 158.766 137.249 1.00 31.15 ?  403 ILE B C     1 
ATOM   8817  O  O     . ILE B 1 403 ? 124.832 159.869 137.610 1.00 32.16 ?  403 ILE B O     1 
ATOM   8818  C  CB    . ILE B 1 403 ? 127.662 159.153 136.591 1.00 23.85 ?  403 ILE B CB    1 
ATOM   8819  C  CG1   . ILE B 1 403 ? 128.715 158.875 135.515 1.00 26.86 ?  403 ILE B CG1   1 
ATOM   8820  C  CG2   . ILE B 1 403 ? 128.047 158.511 137.905 1.00 23.30 ?  403 ILE B CG2   1 
ATOM   8821  C  CD1   . ILE B 1 403 ? 128.742 157.444 135.042 1.00 31.86 ?  403 ILE B CD1   1 
ATOM   8822  N  N     . GLY B 1 404 ? 124.855 157.626 137.794 1.00 26.12 ?  404 GLY B N     1 
ATOM   8823  C  CA    . GLY B 1 404 ? 123.938 157.547 138.911 1.00 14.51 ?  404 GLY B CA    1 
ATOM   8824  C  C     . GLY B 1 404 ? 124.655 157.338 140.228 1.00 21.90 ?  404 GLY B C     1 
ATOM   8825  O  O     . GLY B 1 404 ? 125.791 157.781 140.424 1.00 34.25 ?  404 GLY B O     1 
ATOM   8826  N  N     . LEU B 1 405 ? 123.982 156.652 141.148 1.00 25.58 ?  405 LEU B N     1 
ATOM   8827  C  CA    . LEU B 1 405 ? 124.527 156.358 142.469 1.00 9.14  ?  405 LEU B CA    1 
ATOM   8828  C  C     . LEU B 1 405 ? 124.561 154.851 142.668 1.00 12.56 ?  405 LEU B C     1 
ATOM   8829  O  O     . LEU B 1 405 ? 123.514 154.197 142.652 1.00 20.84 ?  405 LEU B O     1 
ATOM   8830  C  CB    . LEU B 1 405 ? 123.695 157.021 143.567 1.00 19.52 ?  405 LEU B CB    1 
ATOM   8831  C  CG    . LEU B 1 405 ? 123.561 158.543 143.514 1.00 17.62 ?  405 LEU B CG    1 
ATOM   8832  C  CD1   . LEU B 1 405 ? 122.599 159.026 144.581 1.00 25.45 ?  405 LEU B CD1   1 
ATOM   8833  C  CD2   . LEU B 1 405 ? 124.915 159.209 143.672 1.00 19.08 ?  405 LEU B CD2   1 
ATOM   8834  N  N     . ASP B 1 406 ? 125.758 154.307 142.865 1.00 24.10 ?  406 ASP B N     1 
ATOM   8835  C  CA    . ASP B 1 406 ? 125.945 152.900 143.184 1.00 12.26 ?  406 ASP B CA    1 
ATOM   8836  C  C     . ASP B 1 406 ? 126.475 152.773 144.605 1.00 23.28 ?  406 ASP B C     1 
ATOM   8837  O  O     . ASP B 1 406 ? 127.403 153.485 144.998 1.00 34.31 ?  406 ASP B O     1 
ATOM   8838  C  CB    . ASP B 1 406 ? 126.904 152.228 142.201 1.00 18.39 ?  406 ASP B CB    1 
ATOM   8839  C  CG    . ASP B 1 406 ? 126.249 151.906 140.873 1.00 35.02 ?  406 ASP B CG    1 
ATOM   8840  O  OD1   . ASP B 1 406 ? 125.021 152.095 140.746 1.00 37.66 ?  406 ASP B OD1   1 
ATOM   8841  O  OD2   . ASP B 1 406 ? 126.966 151.462 139.953 1.00 32.49 -1 406 ASP B OD2   1 
ATOM   8842  N  N     . ILE B 1 407 ? 125.898 151.853 145.361 1.00 30.17 ?  407 ILE B N     1 
ATOM   8843  C  CA    . ILE B 1 407 ? 126.107 151.801 146.802 1.00 17.45 ?  407 ILE B CA    1 
ATOM   8844  C  C     . ILE B 1 407 ? 127.457 151.176 147.123 1.00 16.83 ?  407 ILE B C     1 
ATOM   8845  O  O     . ILE B 1 407 ? 127.871 150.186 146.507 1.00 24.89 ?  407 ILE B O     1 
ATOM   8846  C  CB    . ILE B 1 407 ? 124.962 151.028 147.477 1.00 10.96 ?  407 ILE B CB    1 
ATOM   8847  C  CG1   . ILE B 1 407 ? 123.615 151.658 147.132 1.00 4.34  ?  407 ILE B CG1   1 
ATOM   8848  C  CG2   . ILE B 1 407 ? 125.154 150.997 148.965 1.00 16.64 ?  407 ILE B CG2   1 
ATOM   8849  C  CD1   . ILE B 1 407 ? 122.535 150.645 146.889 1.00 18.14 ?  407 ILE B CD1   1 
ATOM   8850  N  N     . SER B 1 408 ? 128.148 151.764 148.096 1.00 28.19 ?  408 SER B N     1 
ATOM   8851  C  CA    . SER B 1 408 ? 129.372 151.192 148.653 1.00 25.83 ?  408 SER B CA    1 
ATOM   8852  C  C     . SER B 1 408 ? 129.602 151.835 150.010 1.00 27.97 ?  408 SER B C     1 
ATOM   8853  O  O     . SER B 1 408 ? 129.865 153.040 150.080 1.00 38.52 ?  408 SER B O     1 
ATOM   8854  C  CB    . SER B 1 408 ? 130.564 151.431 147.730 1.00 30.99 ?  408 SER B CB    1 
ATOM   8855  O  OG    . SER B 1 408 ? 131.255 152.615 148.086 1.00 34.38 ?  408 SER B OG    1 
ATOM   8856  N  N     . CYS B 1 409 ? 129.504 151.051 151.078 1.00 21.98 ?  409 CYS B N     1 
ATOM   8857  C  CA    . CYS B 1 409 ? 129.645 151.580 152.426 1.00 31.49 ?  409 CYS B CA    1 
ATOM   8858  C  C     . CYS B 1 409 ? 130.813 150.911 153.138 1.00 26.72 ?  409 CYS B C     1 
ATOM   8859  O  O     . CYS B 1 409 ? 131.213 149.789 152.816 1.00 25.56 ?  409 CYS B O     1 
ATOM   8860  C  CB    . CYS B 1 409 ? 128.350 151.408 153.235 1.00 27.84 ?  409 CYS B CB    1 
ATOM   8861  S  SG    . CYS B 1 409 ? 128.222 149.897 154.208 1.00 38.82 ?  409 CYS B SG    1 
ATOM   8862  N  N     . ASN B 1 410 ? 131.360 151.628 154.114 1.00 22.62 ?  410 ASN B N     1 
ATOM   8863  C  CA    . ASN B 1 410 ? 132.542 151.203 154.849 1.00 22.90 ?  410 ASN B CA    1 
ATOM   8864  C  C     . ASN B 1 410 ? 132.110 150.536 156.147 1.00 24.05 ?  410 ASN B C     1 
ATOM   8865  O  O     . ASN B 1 410 ? 131.233 151.048 156.849 1.00 31.21 ?  410 ASN B O     1 
ATOM   8866  C  CB    . ASN B 1 410 ? 133.448 152.400 155.131 1.00 28.30 ?  410 ASN B CB    1 
ATOM   8867  C  CG    . ASN B 1 410 ? 133.395 153.434 154.026 1.00 37.57 ?  410 ASN B CG    1 
ATOM   8868  O  OD1   . ASN B 1 410 ? 134.353 153.601 153.275 1.00 42.49 ?  410 ASN B OD1   1 
ATOM   8869  N  ND2   . ASN B 1 410 ? 132.283 154.151 153.937 1.00 31.73 ?  410 ASN B ND2   1 
ATOM   8870  N  N     . LEU B 1 411 ? 132.731 149.406 156.464 1.00 16.74 ?  411 LEU B N     1 
ATOM   8871  C  CA    . LEU B 1 411 ? 132.275 148.542 157.543 1.00 9.81  ?  411 LEU B CA    1 
ATOM   8872  C  C     . LEU B 1 411 ? 133.154 148.685 158.778 1.00 13.17 ?  411 LEU B C     1 
ATOM   8873  O  O     . LEU B 1 411 ? 134.376 148.821 158.679 1.00 24.64 ?  411 LEU B O     1 
ATOM   8874  C  CB    . LEU B 1 411 ? 132.262 147.082 157.093 1.00 20.83 ?  411 LEU B CB    1 
ATOM   8875  C  CG    . LEU B 1 411 ? 131.418 146.721 155.874 1.00 19.90 ?  411 LEU B CG    1 
ATOM   8876  C  CD1   . LEU B 1 411 ? 131.137 145.239 155.867 1.00 25.47 ?  411 LEU B CD1   1 
ATOM   8877  C  CD2   . LEU B 1 411 ? 130.120 147.491 155.900 1.00 18.66 ?  411 LEU B CD2   1 
ATOM   8878  N  N     . GLY B 1 412 ? 132.510 148.662 159.941 1.00 18.40 ?  412 GLY B N     1 
ATOM   8879  C  CA    . GLY B 1 412 ? 133.204 148.580 161.210 1.00 4.64  ?  412 GLY B CA    1 
ATOM   8880  C  C     . GLY B 1 412 ? 132.283 147.936 162.221 1.00 11.43 ?  412 GLY B C     1 
ATOM   8881  O  O     . GLY B 1 412 ? 131.056 148.003 162.097 1.00 29.68 ?  412 GLY B O     1 
ATOM   8882  N  N     . SER B 1 413 ? 132.882 147.305 163.226 1.00 13.53 ?  413 SER B N     1 
ATOM   8883  C  CA    . SER B 1 413 ? 132.116 146.548 164.207 1.00 14.25 ?  413 SER B CA    1 
ATOM   8884  C  C     . SER B 1 413 ? 132.509 146.946 165.620 1.00 15.86 ?  413 SER B C     1 
ATOM   8885  O  O     . SER B 1 413 ? 133.691 146.920 165.971 1.00 23.31 ?  413 SER B O     1 
ATOM   8886  C  CB    . SER B 1 413 ? 132.315 145.043 164.022 1.00 10.59 ?  413 SER B CB    1 
ATOM   8887  O  OG    . SER B 1 413 ? 131.606 144.584 162.891 1.00 30.53 ?  413 SER B OG    1 
ATOM   8888  N  N     . LEU B 1 414 ? 131.514 147.311 166.420 1.00 17.46 ?  414 LEU B N     1 
ATOM   8889  C  CA    . LEU B 1 414 ? 131.717 147.432 167.854 1.00 9.58  ?  414 LEU B CA    1 
ATOM   8890  C  C     . LEU B 1 414 ? 131.741 146.051 168.488 1.00 20.99 ?  414 LEU B C     1 
ATOM   8891  O  O     . LEU B 1 414 ? 130.953 145.173 168.130 1.00 27.41 ?  414 LEU B O     1 
ATOM   8892  C  CB    . LEU B 1 414 ? 130.605 148.264 168.489 1.00 19.06 ?  414 LEU B CB    1 
ATOM   8893  C  CG    . LEU B 1 414 ? 130.204 149.579 167.827 1.00 20.59 ?  414 LEU B CG    1 
ATOM   8894  C  CD1   . LEU B 1 414 ? 128.954 150.119 168.488 1.00 23.38 ?  414 LEU B CD1   1 
ATOM   8895  C  CD2   . LEU B 1 414 ? 131.331 150.585 167.917 1.00 25.08 ?  414 LEU B CD2   1 
ATOM   8896  N  N     . ASN B 1 415 ? 132.656 145.856 169.428 1.00 30.18 ?  415 ASN B N     1 
ATOM   8897  C  CA    . ASN B 1 415 ? 132.651 144.664 170.266 1.00 26.52 ?  415 ASN B CA    1 
ATOM   8898  C  C     . ASN B 1 415 ? 131.729 144.944 171.446 1.00 24.97 ?  415 ASN B C     1 
ATOM   8899  O  O     . ASN B 1 415 ? 132.074 145.725 172.337 1.00 29.48 ?  415 ASN B O     1 
ATOM   8900  C  CB    . ASN B 1 415 ? 134.063 144.317 170.723 1.00 21.57 ?  415 ASN B CB    1 
ATOM   8901  C  CG    . ASN B 1 415 ? 134.180 142.902 171.243 1.00 21.47 ?  415 ASN B CG    1 
ATOM   8902  O  OD1   . ASN B 1 415 ? 133.409 142.477 172.102 1.00 37.85 ?  415 ASN B OD1   1 
ATOM   8903  N  ND2   . ASN B 1 415 ? 135.151 142.163 170.726 1.00 29.64 ?  415 ASN B ND2   1 
ATOM   8904  N  N     . ILE B 1 416 ? 130.554 144.313 171.443 1.00 17.78 ?  416 ILE B N     1 
ATOM   8905  C  CA    . ILE B 1 416 ? 129.537 144.619 172.446 1.00 21.17 ?  416 ILE B CA    1 
ATOM   8906  C  C     . ILE B 1 416 ? 130.045 144.291 173.844 1.00 28.90 ?  416 ILE B C     1 
ATOM   8907  O  O     . ILE B 1 416 ? 129.794 145.034 174.799 1.00 27.87 ?  416 ILE B O     1 
ATOM   8908  C  CB    . ILE B 1 416 ? 128.227 143.877 172.120 1.00 27.96 ?  416 ILE B CB    1 
ATOM   8909  C  CG1   . ILE B 1 416 ? 127.593 144.459 170.857 1.00 20.31 ?  416 ILE B CG1   1 
ATOM   8910  C  CG2   . ILE B 1 416 ? 127.251 143.959 173.277 1.00 9.74  ?  416 ILE B CG2   1 
ATOM   8911  C  CD1   . ILE B 1 416 ? 126.387 143.699 170.367 1.00 15.27 ?  416 ILE B CD1   1 
ATOM   8912  N  N     . LEU B 1 417 ? 130.779 143.187 173.986 1.00 21.36 ?  417 LEU B N     1 
ATOM   8913  C  CA    . LEU B 1 417 ? 131.309 142.814 175.294 1.00 26.32 ?  417 LEU B CA    1 
ATOM   8914  C  C     . LEU B 1 417 ? 132.308 143.848 175.804 1.00 30.42 ?  417 LEU B C     1 
ATOM   8915  O  O     . LEU B 1 417 ? 132.223 144.294 176.955 1.00 38.35 ?  417 LEU B O     1 
ATOM   8916  C  CB    . LEU B 1 417 ? 131.956 141.432 175.222 1.00 29.69 ?  417 LEU B CB    1 
ATOM   8917  C  CG    . LEU B 1 417 ? 132.756 140.977 176.443 1.00 30.91 ?  417 LEU B CG    1 
ATOM   8918  C  CD1   . LEU B 1 417 ? 131.843 140.376 177.493 1.00 28.98 ?  417 LEU B CD1   1 
ATOM   8919  C  CD2   . LEU B 1 417 ? 133.831 139.987 176.036 1.00 35.30 ?  417 LEU B CD2   1 
ATOM   8920  N  N     . ASN B 1 418 ? 133.257 144.249 174.958 1.00 30.35 ?  418 ASN B N     1 
ATOM   8921  C  CA    . ASN B 1 418 ? 134.286 145.191 175.382 1.00 27.79 ?  418 ASN B CA    1 
ATOM   8922  C  C     . ASN B 1 418 ? 133.749 146.609 175.519 1.00 29.87 ?  418 ASN B C     1 
ATOM   8923  O  O     . ASN B 1 418 ? 134.187 147.348 176.407 1.00 34.48 ?  418 ASN B O     1 
ATOM   8924  C  CB    . ASN B 1 418 ? 135.456 145.163 174.400 1.00 25.73 ?  418 ASN B CB    1 
ATOM   8925  C  CG    . ASN B 1 418 ? 136.255 143.882 174.491 1.00 26.42 ?  418 ASN B CG    1 
ATOM   8926  O  OD1   . ASN B 1 418 ? 136.413 143.313 175.568 1.00 34.90 ?  418 ASN B OD1   1 
ATOM   8927  N  ND2   . ASN B 1 418 ? 136.759 143.416 173.357 1.00 30.58 ?  418 ASN B ND2   1 
ATOM   8928  N  N     . VAL B 1 419 ? 132.818 147.006 174.652 1.00 32.67 ?  419 VAL B N     1 
ATOM   8929  C  CA    . VAL B 1 419 ? 132.186 148.313 174.787 1.00 31.64 ?  419 VAL B CA    1 
ATOM   8930  C  C     . VAL B 1 419 ? 131.347 148.368 176.057 1.00 30.72 ?  419 VAL B C     1 
ATOM   8931  O  O     . VAL B 1 419 ? 131.307 149.390 176.752 1.00 33.42 ?  419 VAL B O     1 
ATOM   8932  C  CB    . VAL B 1 419 ? 131.349 148.623 173.532 1.00 28.04 ?  419 VAL B CB    1 
ATOM   8933  C  CG1   . VAL B 1 419 ? 130.362 149.736 173.801 1.00 33.19 ?  419 VAL B CG1   1 
ATOM   8934  C  CG2   . VAL B 1 419 ? 132.255 148.984 172.372 1.00 24.47 ?  419 VAL B CG2   1 
ATOM   8935  N  N     . MET B 1 420 ? 130.683 147.262 176.391 1.00 36.25 ?  420 MET B N     1 
ATOM   8936  C  CA    . MET B 1 420 ? 129.821 147.230 177.564 1.00 33.76 ?  420 MET B CA    1 
ATOM   8937  C  C     . MET B 1 420 ? 130.639 147.194 178.849 1.00 31.81 ?  420 MET B C     1 
ATOM   8938  O  O     . MET B 1 420 ? 130.276 147.835 179.841 1.00 34.69 ?  420 MET B O     1 
ATOM   8939  C  CB    . MET B 1 420 ? 128.889 146.022 177.480 1.00 33.22 ?  420 MET B CB    1 
ATOM   8940  C  CG    . MET B 1 420 ? 127.511 146.328 176.915 1.00 24.56 ?  420 MET B CG    1 
ATOM   8941  S  SD    . MET B 1 420 ? 126.952 148.004 177.246 1.00 41.26 ?  420 MET B SD    1 
ATOM   8942  C  CE    . MET B 1 420 ? 126.187 147.774 178.843 1.00 33.19 ?  420 MET B CE    1 
ATOM   8943  N  N     . GLU B 1 421 ? 131.749 146.448 178.850 1.00 39.01 ?  421 GLU B N     1 
ATOM   8944  C  CA    . GLU B 1 421 ? 132.588 146.376 180.041 1.00 38.31 ?  421 GLU B CA    1 
ATOM   8945  C  C     . GLU B 1 421 ? 133.339 147.680 180.285 1.00 36.84 ?  421 GLU B C     1 
ATOM   8946  O  O     . GLU B 1 421 ? 133.640 148.011 181.437 1.00 39.33 ?  421 GLU B O     1 
ATOM   8947  C  CB    . GLU B 1 421 ? 133.562 145.200 179.928 1.00 33.75 ?  421 GLU B CB    1 
ATOM   8948  C  CG    . GLU B 1 421 ? 134.846 145.507 179.174 1.00 38.99 ?  421 GLU B CG    1 
ATOM   8949  C  CD    . GLU B 1 421 ? 135.884 144.410 179.303 1.00 46.20 ?  421 GLU B CD    1 
ATOM   8950  O  OE1   . GLU B 1 421 ? 136.658 144.431 180.282 1.00 43.21 ?  421 GLU B OE1   1 
ATOM   8951  O  OE2   . GLU B 1 421 ? 135.927 143.526 178.421 1.00 43.32 -1 421 GLU B OE2   1 
ATOM   8952  N  N     . HIS B 1 422 ? 133.648 148.428 179.228 1.00 36.68 ?  422 HIS B N     1 
ATOM   8953  C  CA    . HIS B 1 422 ? 134.312 149.717 179.363 1.00 37.50 ?  422 HIS B CA    1 
ATOM   8954  C  C     . HIS B 1 422 ? 133.339 150.866 179.584 1.00 41.79 ?  422 HIS B C     1 
ATOM   8955  O  O     . HIS B 1 422 ? 133.786 151.987 179.848 1.00 45.27 ?  422 HIS B O     1 
ATOM   8956  C  CB    . HIS B 1 422 ? 135.165 150.014 178.126 1.00 35.17 ?  422 HIS B CB    1 
ATOM   8957  C  CG    . HIS B 1 422 ? 136.511 149.360 178.143 1.00 38.00 ?  422 HIS B CG    1 
ATOM   8958  N  ND1   . HIS B 1 422 ? 136.676 147.994 178.071 1.00 39.87 ?  422 HIS B ND1   1 
ATOM   8959  C  CD2   . HIS B 1 422 ? 137.756 149.884 178.219 1.00 40.59 ?  422 HIS B CD2   1 
ATOM   8960  C  CE1   . HIS B 1 422 ? 137.964 147.704 178.105 1.00 41.07 ?  422 HIS B CE1   1 
ATOM   8961  N  NE2   . HIS B 1 422 ? 138.641 148.834 178.195 1.00 42.75 ?  422 HIS B NE2   1 
ATOM   8962  N  N     . LYS B 1 423 ? 132.032 150.611 179.486 1.00 43.51 ?  423 LYS B N     1 
ATOM   8963  C  CA    . LYS B 1 423 ? 131.007 151.643 179.642 1.00 44.04 ?  423 LYS B CA    1 
ATOM   8964  C  C     . LYS B 1 423 ? 131.250 152.805 178.683 1.00 47.14 ?  423 LYS B C     1 
ATOM   8965  O  O     . LYS B 1 423 ? 131.108 153.976 179.040 1.00 48.45 ?  423 LYS B O     1 
ATOM   8966  C  CB    . LYS B 1 423 ? 130.936 152.133 181.090 1.00 43.16 ?  423 LYS B CB    1 
ATOM   8967  C  CG    . LYS B 1 423 ? 130.304 151.145 182.051 1.00 44.78 ?  423 LYS B CG    1 
ATOM   8968  C  CD    . LYS B 1 423 ? 131.292 150.721 183.125 1.00 48.99 ?  423 LYS B CD    1 
ATOM   8969  C  CE    . LYS B 1 423 ? 130.770 149.536 183.922 1.00 47.55 ?  423 LYS B CE    1 
ATOM   8970  N  NZ    . LYS B 1 423 ? 131.218 148.236 183.350 1.00 42.92 1  423 LYS B NZ    1 
ATOM   8971  N  N     . SER B 1 424 ? 131.615 152.474 177.449 1.00 32.45 ?  424 SER B N     1 
ATOM   8972  C  CA    . SER B 1 424 ? 132.047 153.454 176.460 1.00 32.35 ?  424 SER B CA    1 
ATOM   8973  C  C     . SER B 1 424 ? 131.271 153.291 175.161 1.00 36.47 ?  424 SER B C     1 
ATOM   8974  O  O     . SER B 1 424 ? 131.846 153.216 174.075 1.00 38.35 ?  424 SER B O     1 
ATOM   8975  C  CB    . SER B 1 424 ? 133.545 153.335 176.203 1.00 36.99 ?  424 SER B CB    1 
ATOM   8976  O  OG    . SER B 1 424 ? 133.853 152.128 175.530 1.00 34.67 ?  424 SER B OG    1 
ATOM   8977  N  N     . ILE B 1 425 ? 129.942 153.222 175.253 1.00 35.88 ?  425 ILE B N     1 
ATOM   8978  C  CA    . ILE B 1 425 ? 129.131 153.169 174.038 1.00 28.36 ?  425 ILE B CA    1 
ATOM   8979  C  C     . ILE B 1 425 ? 129.292 154.456 173.241 1.00 34.18 ?  425 ILE B C     1 
ATOM   8980  O  O     . ILE B 1 425 ? 129.547 154.431 172.033 1.00 39.14 ?  425 ILE B O     1 
ATOM   8981  C  CB    . ILE B 1 425 ? 127.655 152.903 174.380 1.00 33.41 ?  425 ILE B CB    1 
ATOM   8982  C  CG1   . ILE B 1 425 ? 127.472 151.484 174.915 1.00 33.95 ?  425 ILE B CG1   1 
ATOM   8983  C  CG2   . ILE B 1 425 ? 126.781 153.119 173.155 1.00 29.70 ?  425 ILE B CG2   1 
ATOM   8984  C  CD1   . ILE B 1 425 ? 126.037 151.132 175.218 1.00 34.91 ?  425 ILE B CD1   1 
ATOM   8985  N  N     . GLU B 1 426 ? 129.174 155.601 173.916 1.00 32.69 ?  426 GLU B N     1 
ATOM   8986  C  CA    . GLU B 1 426 ? 129.235 156.885 173.223 1.00 31.07 ?  426 GLU B CA    1 
ATOM   8987  C  C     . GLU B 1 426 ? 130.596 157.107 172.577 1.00 31.81 ?  426 GLU B C     1 
ATOM   8988  O  O     . GLU B 1 426 ? 130.687 157.419 171.385 1.00 42.23 ?  426 GLU B O     1 
ATOM   8989  C  CB    . GLU B 1 426 ? 128.913 158.013 174.202 1.00 32.52 ?  426 GLU B CB    1 
ATOM   8990  C  CG    . GLU B 1 426 ? 129.322 159.391 173.722 1.00 33.06 ?  426 GLU B CG    1 
ATOM   8991  C  CD    . GLU B 1 426 ? 129.150 160.448 174.791 1.00 42.02 ?  426 GLU B CD    1 
ATOM   8992  O  OE1   . GLU B 1 426 ? 128.817 160.083 175.938 1.00 42.80 ?  426 GLU B OE1   1 
ATOM   8993  O  OE2   . GLU B 1 426 ? 129.351 161.642 174.489 1.00 46.74 -1 426 GLU B OE2   1 
ATOM   8994  N  N     . LYS B 1 427 ? 131.670 156.946 173.355 1.00 33.13 ?  427 LYS B N     1 
ATOM   8995  C  CA    . LYS B 1 427 ? 133.007 157.229 172.844 1.00 31.12 ?  427 LYS B CA    1 
ATOM   8996  C  C     . LYS B 1 427 ? 133.390 156.265 171.731 1.00 32.71 ?  427 LYS B C     1 
ATOM   8997  O  O     . LYS B 1 427 ? 133.926 156.685 170.698 1.00 37.83 ?  427 LYS B O     1 
ATOM   8998  C  CB    . LYS B 1 427 ? 134.052 157.183 173.970 1.00 34.87 ?  427 LYS B CB    1 
ATOM   8999  C  CG    . LYS B 1 427 ? 134.043 158.345 174.992 1.00 41.24 ?  427 LYS B CG    1 
ATOM   9000  C  CD    . LYS B 1 427 ? 132.785 158.507 175.861 1.00 40.26 ?  427 LYS B CD    1 
ATOM   9001  C  CE    . LYS B 1 427 ? 132.173 157.177 176.294 1.00 36.14 ?  427 LYS B CE    1 
ATOM   9002  N  NZ    . LYS B 1 427 ? 131.062 157.354 177.267 1.00 40.00 1  427 LYS B NZ    1 
ATOM   9003  N  N     . THR B 1 428 ? 133.127 154.970 171.920 1.00 28.98 ?  428 THR B N     1 
ATOM   9004  C  CA    . THR B 1 428 ? 133.449 154.000 170.880 1.00 24.30 ?  428 THR B CA    1 
ATOM   9005  C  C     . THR B 1 428 ? 132.639 154.253 169.618 1.00 26.69 ?  428 THR B C     1 
ATOM   9006  O  O     . THR B 1 428 ? 133.177 154.185 168.509 1.00 34.84 ?  428 THR B O     1 
ATOM   9007  C  CB    . THR B 1 428 ? 133.218 152.574 171.381 1.00 21.44 ?  428 THR B CB    1 
ATOM   9008  O  OG1   . THR B 1 428 ? 133.864 152.398 172.647 1.00 25.87 ?  428 THR B OG1   1 
ATOM   9009  C  CG2   . THR B 1 428 ? 133.778 151.574 170.389 1.00 27.34 ?  428 THR B CG2   1 
ATOM   9010  N  N     . VAL B 1 429 ? 131.346 154.551 169.764 1.00 26.34 ?  429 VAL B N     1 
ATOM   9011  C  CA    . VAL B 1 429 ? 130.511 154.799 168.593 1.00 23.04 ?  429 VAL B CA    1 
ATOM   9012  C  C     . VAL B 1 429 ? 131.006 156.022 167.835 1.00 24.84 ?  429 VAL B C     1 
ATOM   9013  O  O     . VAL B 1 429 ? 131.113 156.003 166.603 1.00 30.08 ?  429 VAL B O     1 
ATOM   9014  C  CB    . VAL B 1 429 ? 129.033 154.947 169.005 1.00 24.85 ?  429 VAL B CB    1 
ATOM   9015  C  CG1   . VAL B 1 429 ? 128.259 155.692 167.940 1.00 23.31 ?  429 VAL B CG1   1 
ATOM   9016  C  CG2   . VAL B 1 429 ? 128.409 153.588 169.234 1.00 26.10 ?  429 VAL B CG2   1 
ATOM   9017  N  N     . LYS B 1 430 ? 131.336 157.097 168.552 1.00 29.56 ?  430 LYS B N     1 
ATOM   9018  C  CA    . LYS B 1 430 ? 131.762 158.319 167.880 1.00 24.43 ?  430 LYS B CA    1 
ATOM   9019  C  C     . LYS B 1 430 ? 133.126 158.152 167.218 1.00 23.08 ?  430 LYS B C     1 
ATOM   9020  O  O     . LYS B 1 430 ? 133.336 158.621 166.093 1.00 31.25 ?  430 LYS B O     1 
ATOM   9021  C  CB    . LYS B 1 430 ? 131.764 159.482 168.868 1.00 26.41 ?  430 LYS B CB    1 
ATOM   9022  C  CG    . LYS B 1 430 ? 130.366 159.869 169.322 1.00 23.26 ?  430 LYS B CG    1 
ATOM   9023  C  CD    . LYS B 1 430 ? 130.348 161.199 170.042 1.00 31.44 ?  430 LYS B CD    1 
ATOM   9024  C  CE    . LYS B 1 430 ? 128.926 161.617 170.364 1.00 34.84 ?  430 LYS B CE    1 
ATOM   9025  N  NZ    . LYS B 1 430 ? 128.880 162.881 171.144 1.00 36.10 1  430 LYS B NZ    1 
ATOM   9026  N  N     . LEU B 1 431 ? 134.066 157.479 167.887 1.00 30.77 ?  431 LEU B N     1 
ATOM   9027  C  CA    . LEU B 1 431 ? 135.372 157.249 167.276 1.00 22.41 ?  431 LEU B CA    1 
ATOM   9028  C  C     . LEU B 1 431 ? 135.267 156.317 166.074 1.00 23.25 ?  431 LEU B C     1 
ATOM   9029  O  O     . LEU B 1 431 ? 135.955 156.516 165.066 1.00 32.08 ?  431 LEU B O     1 
ATOM   9030  C  CB    . LEU B 1 431 ? 136.343 156.688 168.312 1.00 30.91 ?  431 LEU B CB    1 
ATOM   9031  C  CG    . LEU B 1 431 ? 137.217 157.704 169.046 1.00 32.90 ?  431 LEU B CG    1 
ATOM   9032  C  CD1   . LEU B 1 431 ? 137.988 157.029 170.165 1.00 28.93 ?  431 LEU B CD1   1 
ATOM   9033  C  CD2   . LEU B 1 431 ? 138.164 158.393 168.081 1.00 34.52 ?  431 LEU B CD2   1 
ATOM   9034  N  N     . ALA B 1 432 ? 134.416 155.290 166.163 1.00 25.20 ?  432 ALA B N     1 
ATOM   9035  C  CA    . ALA B 1 432 ? 134.194 154.410 165.024 1.00 20.02 ?  432 ALA B CA    1 
ATOM   9036  C  C     . ALA B 1 432 ? 133.563 155.164 163.864 1.00 25.84 ?  432 ALA B C     1 
ATOM   9037  O  O     . ALA B 1 432 ? 133.909 154.929 162.702 1.00 29.63 ?  432 ALA B O     1 
ATOM   9038  C  CB    . ALA B 1 432 ? 133.318 153.231 165.441 1.00 24.13 ?  432 ALA B CB    1 
ATOM   9039  N  N     . THR B 1 433 ? 132.630 156.071 164.161 1.00 27.18 ?  433 THR B N     1 
ATOM   9040  C  CA    . THR B 1 433 ? 132.045 156.907 163.119 1.00 17.25 ?  433 THR B CA    1 
ATOM   9041  C  C     . THR B 1 433 ? 133.104 157.778 162.459 1.00 25.04 ?  433 THR B C     1 
ATOM   9042  O  O     . THR B 1 433 ? 133.119 157.925 161.233 1.00 33.17 ?  433 THR B O     1 
ATOM   9043  C  CB    . THR B 1 433 ? 130.928 157.769 163.710 1.00 24.03 ?  433 THR B CB    1 
ATOM   9044  O  OG1   . THR B 1 433 ? 129.945 156.925 164.319 1.00 32.99 ?  433 THR B OG1   1 
ATOM   9045  C  CG2   . THR B 1 433 ? 130.265 158.607 162.629 1.00 24.11 ?  433 THR B CG2   1 
ATOM   9046  N  N     . ASP B 1 434 ? 134.002 158.359 163.255 1.00 24.94 ?  434 ASP B N     1 
ATOM   9047  C  CA    . ASP B 1 434 ? 135.078 159.171 162.692 1.00 18.95 ?  434 ASP B CA    1 
ATOM   9048  C  C     . ASP B 1 434 ? 135.990 158.340 161.796 1.00 19.23 ?  434 ASP B C     1 
ATOM   9049  O  O     . ASP B 1 434 ? 136.374 158.782 160.706 1.00 26.71 ?  434 ASP B O     1 
ATOM   9050  C  CB    . ASP B 1 434 ? 135.883 159.826 163.812 1.00 25.35 ?  434 ASP B CB    1 
ATOM   9051  C  CG    . ASP B 1 434 ? 135.111 160.912 164.525 1.00 31.05 ?  434 ASP B CG    1 
ATOM   9052  O  OD1   . ASP B 1 434 ? 134.222 161.521 163.896 1.00 36.85 ?  434 ASP B OD1   1 
ATOM   9053  O  OD2   . ASP B 1 434 ? 135.393 161.157 165.716 1.00 33.18 -1 434 ASP B OD2   1 
ATOM   9054  N  N     . SER B 1 435 ? 136.349 157.134 162.239 1.00 22.83 ?  435 SER B N     1 
ATOM   9055  C  CA    . SER B 1 435 ? 137.225 156.280 161.441 1.00 15.90 ?  435 SER B CA    1 
ATOM   9056  C  C     . SER B 1 435 ? 136.548 155.843 160.146 1.00 23.26 ?  435 SER B C     1 
ATOM   9057  O  O     . SER B 1 435 ? 137.180 155.828 159.082 1.00 31.44 ?  435 SER B O     1 
ATOM   9058  C  CB    . SER B 1 435 ? 137.659 155.065 162.259 1.00 21.15 ?  435 SER B CB    1 
ATOM   9059  O  OG    . SER B 1 435 ? 136.574 154.185 162.487 1.00 22.23 ?  435 SER B OG    1 
ATOM   9060  N  N     . LEU B 1 436 ? 135.266 155.482 160.216 1.00 18.81 ?  436 LEU B N     1 
ATOM   9061  C  CA    . LEU B 1 436 ? 134.534 155.098 159.016 1.00 11.47 ?  436 LEU B CA    1 
ATOM   9062  C  C     . LEU B 1 436 ? 134.387 156.274 158.062 1.00 19.15 ?  436 LEU B C     1 
ATOM   9063  O  O     . LEU B 1 436 ? 134.472 156.106 156.841 1.00 31.33 ?  436 LEU B O     1 
ATOM   9064  C  CB    . LEU B 1 436 ? 133.167 154.536 159.398 1.00 22.51 ?  436 LEU B CB    1 
ATOM   9065  C  CG    . LEU B 1 436 ? 133.184 153.175 160.090 1.00 18.95 ?  436 LEU B CG    1 
ATOM   9066  C  CD1   . LEU B 1 436 ? 131.881 152.935 160.824 1.00 16.54 ?  436 LEU B CD1   1 
ATOM   9067  C  CD2   . LEU B 1 436 ? 133.448 152.078 159.084 1.00 20.71 ?  436 LEU B CD2   1 
ATOM   9068  N  N     . THR B 1 437 ? 134.171 157.476 158.600 1.00 22.48 ?  437 THR B N     1 
ATOM   9069  C  CA    . THR B 1 437 ? 134.136 158.669 157.766 1.00 19.89 ?  437 THR B CA    1 
ATOM   9070  C  C     . THR B 1 437 ? 135.470 158.886 157.066 1.00 24.99 ?  437 THR B C     1 
ATOM   9071  O  O     . THR B 1 437 ? 135.506 159.199 155.872 1.00 35.50 ?  437 THR B O     1 
ATOM   9072  C  CB    . THR B 1 437 ? 133.770 159.888 158.611 1.00 15.98 ?  437 THR B CB    1 
ATOM   9073  O  OG1   . THR B 1 437 ? 132.525 159.650 159.276 1.00 16.78 ?  437 THR B OG1   1 
ATOM   9074  C  CG2   . THR B 1 437 ? 133.646 161.123 157.742 1.00 21.42 ?  437 THR B CG2   1 
ATOM   9075  N  N     . HIS B 1 438 ? 136.578 158.724 157.793 1.00 18.58 ?  438 HIS B N     1 
ATOM   9076  C  CA    . HIS B 1 438 ? 137.892 158.872 157.175 1.00 18.73 ?  438 HIS B CA    1 
ATOM   9077  C  C     . HIS B 1 438 ? 138.097 157.849 156.065 1.00 20.69 ?  438 HIS B C     1 
ATOM   9078  O  O     . HIS B 1 438 ? 138.610 158.183 154.989 1.00 32.55 ?  438 HIS B O     1 
ATOM   9079  C  CB    . HIS B 1 438 ? 138.993 158.741 158.227 1.00 25.97 ?  438 HIS B CB    1 
ATOM   9080  C  CG    . HIS B 1 438 ? 140.374 158.750 157.652 1.00 28.78 ?  438 HIS B CG    1 
ATOM   9081  N  ND1   . HIS B 1 438 ? 141.062 159.914 157.384 1.00 26.69 ?  438 HIS B ND1   1 
ATOM   9082  C  CD2   . HIS B 1 438 ? 141.192 157.737 157.280 1.00 30.25 ?  438 HIS B CD2   1 
ATOM   9083  C  CE1   . HIS B 1 438 ? 142.245 159.618 156.878 1.00 27.89 ?  438 HIS B CE1   1 
ATOM   9084  N  NE2   . HIS B 1 438 ? 142.348 158.303 156.804 1.00 30.94 ?  438 HIS B NE2   1 
ATOM   9085  N  N     . VAL B 1 439 ? 137.702 156.598 156.306 1.00 23.92 ?  439 VAL B N     1 
ATOM   9086  C  CA    . VAL B 1 439 ? 137.830 155.569 155.279 1.00 17.52 ?  439 VAL B CA    1 
ATOM   9087  C  C     . VAL B 1 439 ? 136.988 155.927 154.061 1.00 27.55 ?  439 VAL B C     1 
ATOM   9088  O  O     . VAL B 1 439 ? 137.401 155.713 152.915 1.00 34.37 ?  439 VAL B O     1 
ATOM   9089  C  CB    . VAL B 1 439 ? 137.449 154.190 155.850 1.00 22.88 ?  439 VAL B CB    1 
ATOM   9090  C  CG1   . VAL B 1 439 ? 137.402 153.146 154.747 1.00 25.20 ?  439 VAL B CG1   1 
ATOM   9091  C  CG2   . VAL B 1 439 ? 138.427 153.776 156.927 1.00 21.17 ?  439 VAL B CG2   1 
ATOM   9092  N  N     . SER B 1 440 ? 135.794 156.476 154.290 1.00 27.83 ?  440 SER B N     1 
ATOM   9093  C  CA    . SER B 1 440 ? 134.938 156.885 153.181 1.00 17.71 ?  440 SER B CA    1 
ATOM   9094  C  C     . SER B 1 440 ? 135.576 158.003 152.365 1.00 23.44 ?  440 SER B C     1 
ATOM   9095  O  O     . SER B 1 440 ? 135.565 157.961 151.129 1.00 33.92 ?  440 SER B O     1 
ATOM   9096  C  CB    . SER B 1 440 ? 133.572 157.318 153.714 1.00 26.57 ?  440 SER B CB    1 
ATOM   9097  O  OG    . SER B 1 440 ? 132.630 157.456 152.664 1.00 33.83 ?  440 SER B OG    1 
ATOM   9098  N  N     . GLU B 1 441 ? 136.137 159.013 153.036 1.00 24.94 ?  441 GLU B N     1 
ATOM   9099  C  CA    . GLU B 1 441 ? 136.755 160.122 152.310 1.00 20.17 ?  441 GLU B CA    1 
ATOM   9100  C  C     . GLU B 1 441 ? 137.999 159.678 151.552 1.00 29.91 ?  441 GLU B C     1 
ATOM   9101  O  O     . GLU B 1 441 ? 138.241 160.136 150.430 1.00 41.35 ?  441 GLU B O     1 
ATOM   9102  C  CB    . GLU B 1 441 ? 137.100 161.277 153.252 1.00 22.01 ?  441 GLU B CB    1 
ATOM   9103  C  CG    . GLU B 1 441 ? 136.047 161.620 154.284 1.00 30.91 ?  441 GLU B CG    1 
ATOM   9104  C  CD    . GLU B 1 441 ? 134.760 162.130 153.667 1.00 42.82 ?  441 GLU B CD    1 
ATOM   9105  O  OE1   . GLU B 1 441 ? 134.692 163.333 153.341 1.00 39.73 ?  441 GLU B OE1   1 
ATOM   9106  O  OE2   . GLU B 1 441 ? 133.814 161.330 153.512 1.00 47.27 -1 441 GLU B OE2   1 
ATOM   9107  N  N     . THR B 1 442 ? 138.801 158.794 152.139 1.00 32.89 ?  442 THR B N     1 
ATOM   9108  C  CA    . THR B 1 442 ? 140.052 158.399 151.503 1.00 29.78 ?  442 THR B CA    1 
ATOM   9109  C  C     . THR B 1 442 ? 139.866 157.336 150.429 1.00 29.77 ?  442 THR B C     1 
ATOM   9110  O  O     . THR B 1 442 ? 140.851 156.944 149.794 1.00 38.02 ?  442 THR B O     1 
ATOM   9111  C  CB    . THR B 1 442 ? 141.050 157.898 152.552 1.00 31.77 ?  442 THR B CB    1 
ATOM   9112  O  OG1   . THR B 1 442 ? 140.512 156.752 153.221 1.00 38.47 ?  442 THR B OG1   1 
ATOM   9113  C  CG2   . THR B 1 442 ? 141.341 158.989 153.566 1.00 28.66 ?  442 THR B CG2   1 
ATOM   9114  N  N     . THR B 1 443 ? 138.645 156.865 150.206 1.00 33.92 ?  443 THR B N     1 
ATOM   9115  C  CA    . THR B 1 443 ? 138.374 155.870 149.177 1.00 37.93 ?  443 THR B CA    1 
ATOM   9116  C  C     . THR B 1 443 ? 138.057 156.575 147.864 1.00 38.05 ?  443 THR B C     1 
ATOM   9117  O  O     . THR B 1 443 ? 137.129 157.387 147.796 1.00 39.87 ?  443 THR B O     1 
ATOM   9118  C  CB    . THR B 1 443 ? 137.215 154.964 149.587 1.00 36.18 ?  443 THR B CB    1 
ATOM   9119  O  OG1   . THR B 1 443 ? 137.534 154.303 150.817 1.00 40.97 ?  443 THR B OG1   1 
ATOM   9120  C  CG2   . THR B 1 443 ? 136.956 153.921 148.514 1.00 29.03 ?  443 THR B CG2   1 
ATOM   9121  N  N     . ASP B 1 444 ? 138.830 156.264 146.825 1.00 46.08 ?  444 ASP B N     1 
ATOM   9122  C  CA    . ASP B 1 444 ? 138.591 156.790 145.483 1.00 44.30 ?  444 ASP B CA    1 
ATOM   9123  C  C     . ASP B 1 444 ? 138.764 155.644 144.499 1.00 47.74 ?  444 ASP B C     1 
ATOM   9124  O  O     . ASP B 1 444 ? 139.866 155.103 144.362 1.00 49.21 ?  444 ASP B O     1 
ATOM   9125  C  CB    . ASP B 1 444 ? 139.540 157.944 145.158 1.00 47.29 ?  444 ASP B CB    1 
ATOM   9126  C  CG    . ASP B 1 444 ? 138.943 158.924 144.168 1.00 51.21 ?  444 ASP B CG    1 
ATOM   9127  O  OD1   . ASP B 1 444 ? 137.834 159.434 144.430 1.00 48.14 ?  444 ASP B OD1   1 
ATOM   9128  O  OD2   . ASP B 1 444 ? 139.584 159.187 143.129 1.00 52.79 -1 444 ASP B OD2   1 
ATOM   9129  N  N     . ILE B 1 445 ? 137.684 155.274 143.818 1.00 38.65 ?  445 ILE B N     1 
ATOM   9130  C  CA    . ILE B 1 445 ? 137.685 154.158 142.881 1.00 40.61 ?  445 ILE B CA    1 
ATOM   9131  C  C     . ILE B 1 445 ? 137.580 154.732 141.474 1.00 45.93 ?  445 ILE B C     1 
ATOM   9132  O  O     . ILE B 1 445 ? 136.619 155.441 141.153 1.00 48.01 ?  445 ILE B O     1 
ATOM   9133  C  CB    . ILE B 1 445 ? 136.545 153.175 143.183 1.00 38.89 ?  445 ILE B CB    1 
ATOM   9134  C  CG1   . ILE B 1 445 ? 136.988 152.183 144.257 1.00 38.21 ?  445 ILE B CG1   1 
ATOM   9135  C  CG2   . ILE B 1 445 ? 136.148 152.414 141.934 1.00 41.28 ?  445 ILE B CG2   1 
ATOM   9136  C  CD1   . ILE B 1 445 ? 135.886 151.768 145.189 1.00 37.47 ?  445 ILE B CD1   1 
ATOM   9137  N  N     . ARG B 1 446 ? 138.572 154.431 140.639 1.00 46.10 ?  446 ARG B N     1 
ATOM   9138  C  CA    . ARG B 1 446 ? 138.741 155.114 139.365 1.00 46.88 ?  446 ARG B CA    1 
ATOM   9139  C  C     . ARG B 1 446 ? 138.014 154.445 138.207 1.00 48.00 ?  446 ARG B C     1 
ATOM   9140  O  O     . ARG B 1 446 ? 137.990 155.007 137.107 1.00 43.19 ?  446 ARG B O     1 
ATOM   9141  C  CB    . ARG B 1 446 ? 140.232 155.227 139.027 1.00 43.09 ?  446 ARG B CB    1 
ATOM   9142  C  CG    . ARG B 1 446 ? 141.140 155.409 140.237 1.00 41.76 ?  446 ARG B CG    1 
ATOM   9143  C  CD    . ARG B 1 446 ? 140.916 156.702 141.036 1.00 46.98 ?  446 ARG B CD    1 
ATOM   9144  N  NE    . ARG B 1 446 ? 141.155 157.926 140.278 1.00 48.53 ?  446 ARG B NE    1 
ATOM   9145  C  CZ    . ARG B 1 446 ? 140.242 158.595 139.584 1.00 49.20 ?  446 ARG B CZ    1 
ATOM   9146  N  NH1   . ARG B 1 446 ? 138.971 158.230 139.578 1.00 45.47 1  446 ARG B NH1   1 
ATOM   9147  N  NH2   . ARG B 1 446 ? 140.610 159.675 138.902 1.00 41.80 ?  446 ARG B NH2   1 
ATOM   9148  N  N     . ASN B 1 447 ? 137.421 153.271 138.414 1.00 37.86 ?  447 ASN B N     1 
ATOM   9149  C  CA    . ASN B 1 447 ? 136.767 152.550 137.333 1.00 30.21 ?  447 ASN B CA    1 
ATOM   9150  C  C     . ASN B 1 447 ? 135.295 152.271 137.592 1.00 33.78 ?  447 ASN B C     1 
ATOM   9151  O  O     . ASN B 1 447 ? 134.661 151.581 136.787 1.00 41.74 ?  447 ASN B O     1 
ATOM   9152  C  CB    . ASN B 1 447 ? 137.499 151.233 137.054 1.00 35.06 ?  447 ASN B CB    1 
ATOM   9153  C  CG    . ASN B 1 447 ? 138.590 151.388 136.019 1.00 33.26 ?  447 ASN B CG    1 
ATOM   9154  O  OD1   . ASN B 1 447 ? 138.314 151.549 134.832 1.00 39.91 ?  447 ASN B OD1   1 
ATOM   9155  N  ND2   . ASN B 1 447 ? 139.838 151.343 136.464 1.00 29.19 ?  447 ASN B ND2   1 
ATOM   9156  N  N     . ALA B 1 448 ? 134.734 152.780 138.687 1.00 35.20 ?  448 ALA B N     1 
ATOM   9157  C  CA    . ALA B 1 448 ? 133.306 152.689 138.982 1.00 30.98 ?  448 ALA B CA    1 
ATOM   9158  C  C     . ALA B 1 448 ? 132.808 154.106 139.222 1.00 34.36 ?  448 ALA B C     1 
ATOM   9159  O  O     . ALA B 1 448 ? 132.803 154.586 140.365 1.00 35.04 ?  448 ALA B O     1 
ATOM   9160  C  CB    . ALA B 1 448 ? 133.042 151.792 140.187 1.00 26.58 ?  448 ALA B CB    1 
ATOM   9161  N  N     . PRO B 1 449 ? 132.397 154.820 138.169 1.00 32.91 ?  449 PRO B N     1 
ATOM   9162  C  CA    . PRO B 1 449 ? 132.030 156.234 138.356 1.00 25.26 ?  449 PRO B CA    1 
ATOM   9163  C  C     . PRO B 1 449 ? 130.833 156.427 139.264 1.00 30.13 ?  449 PRO B C     1 
ATOM   9164  O  O     . PRO B 1 449 ? 130.800 157.392 140.038 1.00 29.44 ?  449 PRO B O     1 
ATOM   9165  C  CB    . PRO B 1 449 ? 131.749 156.725 136.928 1.00 27.13 ?  449 PRO B CB    1 
ATOM   9166  C  CG    . PRO B 1 449 ? 131.913 155.543 136.026 1.00 30.35 ?  449 PRO B CG    1 
ATOM   9167  C  CD    . PRO B 1 449 ? 132.016 154.310 136.843 1.00 24.54 ?  449 PRO B CD    1 
ATOM   9168  N  N     . ALA B 1 450 ? 129.844 155.533 139.196 1.00 32.95 ?  450 ALA B N     1 
ATOM   9169  C  CA    . ALA B 1 450 ? 128.674 155.664 140.057 1.00 19.72 ?  450 ALA B CA    1 
ATOM   9170  C  C     . ALA B 1 450 ? 129.021 155.361 141.507 1.00 27.50 ?  450 ALA B C     1 
ATOM   9171  O  O     . ALA B 1 450 ? 128.526 156.028 142.421 1.00 33.23 ?  450 ALA B O     1 
ATOM   9172  C  CB    . ALA B 1 450 ? 127.556 154.750 139.562 1.00 23.31 ?  450 ALA B CB    1 
ATOM   9173  N  N     . VAL B 1 451 ? 129.881 154.366 141.737 1.00 29.00 ?  451 VAL B N     1 
ATOM   9174  C  CA    . VAL B 1 451 ? 130.320 154.058 143.096 1.00 19.78 ?  451 VAL B CA    1 
ATOM   9175  C  C     . VAL B 1 451 ? 131.071 155.243 143.687 1.00 24.03 ?  451 VAL B C     1 
ATOM   9176  O  O     . VAL B 1 451 ? 130.842 155.635 144.836 1.00 36.06 ?  451 VAL B O     1 
ATOM   9177  C  CB    . VAL B 1 451 ? 131.184 152.783 143.105 1.00 28.00 ?  451 VAL B CB    1 
ATOM   9178  C  CG1   . VAL B 1 451 ? 132.000 152.698 144.382 1.00 28.64 ?  451 VAL B CG1   1 
ATOM   9179  C  CG2   . VAL B 1 451 ? 130.319 151.551 142.945 1.00 23.50 ?  451 VAL B CG2   1 
ATOM   9180  N  N     . ARG B 1 452 ? 131.978 155.833 142.907 1.00 25.98 ?  452 ARG B N     1 
ATOM   9181  C  CA    . ARG B 1 452 ? 132.738 156.984 143.383 1.00 23.15 ?  452 ARG B CA    1 
ATOM   9182  C  C     . ARG B 1 452 ? 131.830 158.181 143.644 1.00 22.13 ?  452 ARG B C     1 
ATOM   9183  O  O     . ARG B 1 452 ? 131.973 158.870 144.663 1.00 36.39 ?  452 ARG B O     1 
ATOM   9184  C  CB    . ARG B 1 452 ? 133.828 157.334 142.370 1.00 23.46 ?  452 ARG B CB    1 
ATOM   9185  C  CG    . ARG B 1 452 ? 134.681 158.531 142.743 1.00 31.33 ?  452 ARG B CG    1 
ATOM   9186  C  CD    . ARG B 1 452 ? 135.016 159.364 141.518 1.00 29.52 ?  452 ARG B CD    1 
ATOM   9187  N  NE    . ARG B 1 452 ? 133.991 159.249 140.487 1.00 41.86 ?  452 ARG B NE    1 
ATOM   9188  C  CZ    . ARG B 1 452 ? 132.969 160.082 140.344 1.00 41.89 ?  452 ARG B CZ    1 
ATOM   9189  N  NH1   . ARG B 1 452 ? 132.807 161.123 141.145 1.00 34.62 1  452 ARG B NH1   1 
ATOM   9190  N  NH2   . ARG B 1 452 ? 132.085 159.864 139.375 1.00 28.38 ?  452 ARG B NH2   1 
ATOM   9191  N  N     . ARG B 1 453 ? 130.882 158.439 142.740 1.00 23.37 ?  453 ARG B N     1 
ATOM   9192  C  CA    . ARG B 1 453 ? 129.965 159.557 142.926 1.00 22.37 ?  453 ARG B CA    1 
ATOM   9193  C  C     . ARG B 1 453 ? 129.107 159.366 144.170 1.00 29.71 ?  453 ARG B C     1 
ATOM   9194  O  O     . ARG B 1 453 ? 128.901 160.310 144.941 1.00 32.37 ?  453 ARG B O     1 
ATOM   9195  C  CB    . ARG B 1 453 ? 129.086 159.729 141.686 1.00 25.06 ?  453 ARG B CB    1 
ATOM   9196  C  CG    . ARG B 1 453 ? 127.920 160.681 141.879 1.00 25.17 ?  453 ARG B CG    1 
ATOM   9197  C  CD    . ARG B 1 453 ? 127.320 161.101 140.553 1.00 24.76 ?  453 ARG B CD    1 
ATOM   9198  N  NE    . ARG B 1 453 ? 125.911 160.738 140.455 1.00 27.52 ?  453 ARG B NE    1 
ATOM   9199  C  CZ    . ARG B 1 453 ? 124.914 161.467 140.936 1.00 29.14 ?  453 ARG B CZ    1 
ATOM   9200  N  NH1   . ARG B 1 453 ? 125.133 162.611 141.563 1.00 30.68 1  453 ARG B NH1   1 
ATOM   9201  N  NH2   . ARG B 1 453 ? 123.666 161.038 140.784 1.00 25.55 ?  453 ARG B NH2   1 
ATOM   9202  N  N     . ALA B 1 454 ? 128.603 158.149 144.388 1.00 31.94 ?  454 ALA B N     1 
ATOM   9203  C  CA    . ALA B 1 454 ? 127.781 157.896 145.563 1.00 20.44 ?  454 ALA B CA    1 
ATOM   9204  C  C     . ALA B 1 454 ? 128.601 157.929 146.843 1.00 20.06 ?  454 ALA B C     1 
ATOM   9205  O  O     . ALA B 1 454 ? 128.091 158.339 147.887 1.00 29.70 ?  454 ALA B O     1 
ATOM   9206  C  CB    . ALA B 1 454 ? 127.061 156.558 145.425 1.00 22.79 ?  454 ALA B CB    1 
ATOM   9207  N  N     . ASN B 1 455 ? 129.863 157.501 146.792 1.00 26.92 ?  455 ASN B N     1 
ATOM   9208  C  CA    . ASN B 1 455 ? 130.722 157.621 147.962 1.00 20.39 ?  455 ASN B CA    1 
ATOM   9209  C  C     . ASN B 1 455 ? 130.971 159.082 148.308 1.00 26.77 ?  455 ASN B C     1 
ATOM   9210  O  O     . ASN B 1 455 ? 130.978 159.456 149.485 1.00 39.86 ?  455 ASN B O     1 
ATOM   9211  C  CB    . ASN B 1 455 ? 132.041 156.888 147.722 1.00 20.18 ?  455 ASN B CB    1 
ATOM   9212  C  CG    . ASN B 1 455 ? 132.935 156.879 148.945 1.00 29.85 ?  455 ASN B CG    1 
ATOM   9213  O  OD1   . ASN B 1 455 ? 132.642 156.214 149.935 1.00 38.69 ?  455 ASN B OD1   1 
ATOM   9214  N  ND2   . ASN B 1 455 ? 134.033 157.620 148.880 1.00 29.79 ?  455 ASN B ND2   1 
ATOM   9215  N  N     . LYS B 1 456 ? 131.179 159.922 147.292 1.00 27.60 ?  456 LYS B N     1 
ATOM   9216  C  CA    . LYS B 1 456 ? 131.410 161.339 147.547 1.00 26.83 ?  456 LYS B CA    1 
ATOM   9217  C  C     . LYS B 1 456 ? 130.147 162.050 148.017 1.00 26.99 ?  456 LYS B C     1 
ATOM   9218  O  O     . LYS B 1 456 ? 130.225 162.962 148.845 1.00 31.45 ?  456 LYS B O     1 
ATOM   9219  C  CB    . LYS B 1 456 ? 131.962 162.011 146.291 1.00 24.22 ?  456 LYS B CB    1 
ATOM   9220  C  CG    . LYS B 1 456 ? 132.968 163.112 146.574 1.00 29.52 ?  456 LYS B CG    1 
ATOM   9221  C  CD    . LYS B 1 456 ? 132.308 164.481 146.549 1.00 35.87 ?  456 LYS B CD    1 
ATOM   9222  C  CE    . LYS B 1 456 ? 133.248 165.560 147.063 1.00 37.12 ?  456 LYS B CE    1 
ATOM   9223  N  NZ    . LYS B 1 456 ? 133.164 165.715 148.542 1.00 31.89 1  456 LYS B NZ    1 
ATOM   9224  N  N     . ALA B 1 457 ? 128.983 161.655 147.505 1.00 25.36 ?  457 ALA B N     1 
ATOM   9225  C  CA    . ALA B 1 457 ? 127.739 162.360 147.789 1.00 17.19 ?  457 ALA B CA    1 
ATOM   9226  C  C     . ALA B 1 457 ? 127.056 161.865 149.058 1.00 23.78 ?  457 ALA B C     1 
ATOM   9227  O  O     . ALA B 1 457 ? 126.742 162.659 149.949 1.00 27.47 ?  457 ALA B O     1 
ATOM   9228  C  CB    . ALA B 1 457 ? 126.787 162.224 146.598 1.00 20.86 ?  457 ALA B CB    1 
ATOM   9229  N  N     . MET B 1 458 ? 126.817 160.557 149.149 1.00 34.34 ?  458 MET B N     1 
ATOM   9230  C  CA    . MET B 1 458 ? 126.061 159.993 150.260 1.00 17.01 ?  458 MET B CA    1 
ATOM   9231  C  C     . MET B 1 458 ? 126.879 159.956 151.543 1.00 25.08 ?  458 MET B C     1 
ATOM   9232  O  O     . MET B 1 458 ? 126.330 160.165 152.631 1.00 33.26 ?  458 MET B O     1 
ATOM   9233  C  CB    . MET B 1 458 ? 125.581 158.589 149.897 1.00 18.15 ?  458 MET B CB    1 
ATOM   9234  C  CG    . MET B 1 458 ? 124.846 158.498 148.565 1.00 21.57 ?  458 MET B CG    1 
ATOM   9235  S  SD    . MET B 1 458 ? 123.063 158.729 148.700 1.00 35.77 ?  458 MET B SD    1 
ATOM   9236  C  CE    . MET B 1 458 ? 122.936 160.513 148.642 1.00 27.87 ?  458 MET B CE    1 
ATOM   9237  N  N     . LYS B 1 459 ? 128.181 159.690 151.437 1.00 15.58 ?  459 LYS B N     1 
ATOM   9238  C  CA    . LYS B 1 459 ? 129.060 159.564 152.600 1.00 18.95 ?  459 LYS B CA    1 
ATOM   9239  C  C     . LYS B 1 459 ? 128.524 158.526 153.582 1.00 20.49 ?  459 LYS B C     1 
ATOM   9240  O  O     . LYS B 1 459 ? 128.593 158.695 154.800 1.00 32.27 ?  459 LYS B O     1 
ATOM   9241  C  CB    . LYS B 1 459 ? 129.262 160.914 153.292 1.00 26.05 ?  459 LYS B CB    1 
ATOM   9242  C  CG    . LYS B 1 459 ? 129.758 162.017 152.378 1.00 31.44 ?  459 LYS B CG    1 
ATOM   9243  C  CD    . LYS B 1 459 ? 129.057 163.327 152.683 1.00 23.51 ?  459 LYS B CD    1 
ATOM   9244  C  CE    . LYS B 1 459 ? 129.444 164.405 151.691 1.00 27.85 ?  459 LYS B CE    1 
ATOM   9245  N  NZ    . LYS B 1 459 ? 128.749 165.688 151.973 1.00 33.22 1  459 LYS B NZ    1 
ATOM   9246  N  N     . SER B 1 460 ? 127.983 157.437 153.044 1.00 16.22 ?  460 SER B N     1 
ATOM   9247  C  CA    . SER B 1 460 ? 127.377 156.408 153.872 1.00 9.49  ?  460 SER B CA    1 
ATOM   9248  C  C     . SER B 1 460 ? 128.443 155.503 154.475 1.00 19.62 ?  460 SER B C     1 
ATOM   9249  O  O     . SER B 1 460 ? 129.425 155.149 153.817 1.00 32.72 ?  460 SER B O     1 
ATOM   9250  C  CB    . SER B 1 460 ? 126.391 155.575 153.056 1.00 17.17 ?  460 SER B CB    1 
ATOM   9251  O  OG    . SER B 1 460 ? 127.070 154.766 152.116 1.00 26.49 ?  460 SER B OG    1 
ATOM   9252  N  N     . ILE B 1 461 ? 128.239 155.129 155.736 1.00 19.65 ?  461 ILE B N     1 
ATOM   9253  C  CA    . ILE B 1 461 ? 129.129 154.224 156.446 1.00 15.15 ?  461 ILE B CA    1 
ATOM   9254  C  C     . ILE B 1 461 ? 128.288 153.110 157.048 1.00 20.77 ?  461 ILE B C     1 
ATOM   9255  O  O     . ILE B 1 461 ? 127.072 153.228 157.198 1.00 23.59 ?  461 ILE B O     1 
ATOM   9256  C  CB    . ILE B 1 461 ? 129.942 154.939 157.546 1.00 12.55 ?  461 ILE B CB    1 
ATOM   9257  C  CG1   . ILE B 1 461 ? 129.003 155.622 158.540 1.00 7.21  ?  461 ILE B CG1   1 
ATOM   9258  C  CG2   . ILE B 1 461 ? 130.898 155.946 156.933 1.00 18.35 ?  461 ILE B CG2   1 
ATOM   9259  C  CD1   . ILE B 1 461 ? 129.674 156.056 159.815 1.00 12.29 ?  461 ILE B CD1   1 
ATOM   9260  N  N     . GLY B 1 462 ? 128.950 152.005 157.370 1.00 20.59 ?  462 GLY B N     1 
ATOM   9261  C  CA    . GLY B 1 462 ? 128.280 150.952 158.100 1.00 9.98  ?  462 GLY B CA    1 
ATOM   9262  C  C     . GLY B 1 462 ? 128.991 150.617 159.391 1.00 11.74 ?  462 GLY B C     1 
ATOM   9263  O  O     . GLY B 1 462 ? 130.089 150.056 159.371 1.00 27.20 ?  462 GLY B O     1 
ATOM   9264  N  N     . LEU B 1 463 ? 128.371 150.939 160.519 1.00 12.75 ?  463 LEU B N     1 
ATOM   9265  C  CA    . LEU B 1 463 ? 128.911 150.613 161.832 1.00 8.74  ?  463 LEU B CA    1 
ATOM   9266  C  C     . LEU B 1 463 ? 128.103 149.456 162.400 1.00 20.47 ?  463 LEU B C     1 
ATOM   9267  O  O     . LEU B 1 463 ? 126.951 149.635 162.807 1.00 28.83 ?  463 LEU B O     1 
ATOM   9268  C  CB    . LEU B 1 463 ? 128.873 151.823 162.761 1.00 18.78 ?  463 LEU B CB    1 
ATOM   9269  C  CG    . LEU B 1 463 ? 129.307 151.550 164.202 1.00 16.77 ?  463 LEU B CG    1 
ATOM   9270  C  CD1   . LEU B 1 463 ? 130.717 150.992 164.229 1.00 3.19  ?  463 LEU B CD1   1 
ATOM   9271  C  CD2   . LEU B 1 463 ? 129.205 152.808 165.048 1.00 16.93 ?  463 LEU B CD2   1 
ATOM   9272  N  N     . GLY B 1 464 ? 128.706 148.270 162.426 1.00 22.67 ?  464 GLY B N     1 
ATOM   9273  C  CA    . GLY B 1 464 ? 128.060 147.084 162.937 1.00 13.17 ?  464 GLY B CA    1 
ATOM   9274  C  C     . GLY B 1 464 ? 128.410 146.806 164.385 1.00 9.46  ?  464 GLY B C     1 
ATOM   9275  O  O     . GLY B 1 464 ? 129.070 147.594 165.069 1.00 18.19 ?  464 GLY B O     1 
ATOM   9276  N  N     . ALA B 1 465 ? 127.949 145.653 164.855 1.00 15.21 ?  465 ALA B N     1 
ATOM   9277  C  CA    . ALA B 1 465 ? 128.241 145.184 166.198 1.00 8.92  ?  465 ALA B CA    1 
ATOM   9278  C  C     . ALA B 1 465 ? 128.475 143.684 166.145 1.00 16.15 ?  465 ALA B C     1 
ATOM   9279  O  O     . ALA B 1 465 ? 128.018 142.995 165.232 1.00 33.48 ?  465 ALA B O     1 
ATOM   9280  C  CB    . ALA B 1 465 ? 127.109 145.518 167.177 1.00 18.90 ?  465 ALA B CB    1 
ATOM   9281  N  N     . MET B 1 466 ? 129.202 143.186 167.139 1.00 22.79 ?  466 MET B N     1 
ATOM   9282  C  CA    . MET B 1 466 ? 129.495 141.766 167.239 1.00 19.06 ?  466 MET B CA    1 
ATOM   9283  C  C     . MET B 1 466 ? 129.601 141.405 168.712 1.00 18.39 ?  466 MET B C     1 
ATOM   9284  O  O     . MET B 1 466 ? 129.526 142.269 169.590 1.00 23.63 ?  466 MET B O     1 
ATOM   9285  C  CB    . MET B 1 466 ? 130.774 141.413 166.477 1.00 24.49 ?  466 MET B CB    1 
ATOM   9286  C  CG    . MET B 1 466 ? 132.039 141.838 167.187 1.00 27.81 ?  466 MET B CG    1 
ATOM   9287  S  SD    . MET B 1 466 ? 133.487 141.834 166.123 1.00 41.52 ?  466 MET B SD    1 
ATOM   9288  C  CE    . MET B 1 466 ? 134.445 143.112 166.920 1.00 25.51 ?  466 MET B CE    1 
ATOM   9289  N  N     . ASN B 1 467 ? 129.772 140.109 168.979 1.00 16.44 ?  467 ASN B N     1 
ATOM   9290  C  CA    . ASN B 1 467 ? 129.891 139.581 170.338 1.00 22.64 ?  467 ASN B CA    1 
ATOM   9291  C  C     . ASN B 1 467 ? 128.629 139.829 171.157 1.00 26.97 ?  467 ASN B C     1 
ATOM   9292  O  O     . ASN B 1 467 ? 128.697 140.033 172.370 1.00 26.62 ?  467 ASN B O     1 
ATOM   9293  C  CB    . ASN B 1 467 ? 131.114 140.154 171.060 1.00 21.75 ?  467 ASN B CB    1 
ATOM   9294  C  CG    . ASN B 1 467 ? 131.793 139.138 171.947 1.00 27.21 ?  467 ASN B CG    1 
ATOM   9295  O  OD1   . ASN B 1 467 ? 131.421 137.966 171.965 1.00 27.28 ?  467 ASN B OD1   1 
ATOM   9296  N  ND2   . ASN B 1 467 ? 132.801 139.579 172.686 1.00 30.72 ?  467 ASN B ND2   1 
ATOM   9297  N  N     . LEU B 1 468 ? 127.468 139.829 170.502 1.00 17.65 ?  468 LEU B N     1 
ATOM   9298  C  CA    . LEU B 1 468 ? 126.214 139.936 171.239 1.00 14.70 ?  468 LEU B CA    1 
ATOM   9299  C  C     . LEU B 1 468 ? 125.953 138.673 172.049 1.00 29.01 ?  468 LEU B C     1 
ATOM   9300  O  O     . LEU B 1 468 ? 125.673 138.738 173.251 1.00 33.40 ?  468 LEU B O     1 
ATOM   9301  C  CB    . LEU B 1 468 ? 125.059 140.205 170.276 1.00 24.99 ?  468 LEU B CB    1 
ATOM   9302  C  CG    . LEU B 1 468 ? 123.677 140.311 170.921 1.00 19.41 ?  468 LEU B CG    1 
ATOM   9303  C  CD1   . LEU B 1 468 ? 123.647 141.434 171.941 1.00 16.93 ?  468 LEU B CD1   1 
ATOM   9304  C  CD2   . LEU B 1 468 ? 122.601 140.508 169.871 1.00 16.14 ?  468 LEU B CD2   1 
ATOM   9305  N  N     . HIS B 1 469 ? 126.062 137.509 171.406 1.00 31.57 ?  469 HIS B N     1 
ATOM   9306  C  CA    . HIS B 1 469 ? 125.835 136.256 172.115 1.00 16.43 ?  469 HIS B CA    1 
ATOM   9307  C  C     . HIS B 1 469 ? 126.922 136.003 173.147 1.00 27.60 ?  469 HIS B C     1 
ATOM   9308  O  O     . HIS B 1 469 ? 126.643 135.484 174.230 1.00 38.08 ?  469 HIS B O     1 
ATOM   9309  C  CB    . HIS B 1 469 ? 125.749 135.092 171.131 1.00 15.93 ?  469 HIS B CB    1 
ATOM   9310  C  CG    . HIS B 1 469 ? 125.148 133.855 171.721 1.00 20.95 ?  469 HIS B CG    1 
ATOM   9311  N  ND1   . HIS B 1 469 ? 125.161 132.639 171.076 1.00 33.35 ?  469 HIS B ND1   1 
ATOM   9312  C  CD2   . HIS B 1 469 ? 124.518 133.648 172.901 1.00 27.48 ?  469 HIS B CD2   1 
ATOM   9313  C  CE1   . HIS B 1 469 ? 124.563 131.736 171.832 1.00 26.03 ?  469 HIS B CE1   1 
ATOM   9314  N  NE2   . HIS B 1 469 ? 124.165 132.322 172.946 1.00 25.19 ?  469 HIS B NE2   1 
ATOM   9315  N  N     . GLY B 1 470 ? 128.167 136.357 172.830 1.00 20.38 ?  470 GLY B N     1 
ATOM   9316  C  CA    . GLY B 1 470 ? 129.229 136.215 173.811 1.00 23.00 ?  470 GLY B CA    1 
ATOM   9317  C  C     . GLY B 1 470 ? 128.999 137.075 175.036 1.00 16.85 ?  470 GLY B C     1 
ATOM   9318  O  O     . GLY B 1 470 ? 129.155 136.614 176.170 1.00 35.43 ?  470 GLY B O     1 
ATOM   9319  N  N     . TYR B 1 471 ? 128.605 138.332 174.826 1.00 17.13 ?  471 TYR B N     1 
ATOM   9320  C  CA    . TYR B 1 471 ? 128.332 139.219 175.950 1.00 20.16 ?  471 TYR B CA    1 
ATOM   9321  C  C     . TYR B 1 471 ? 127.152 138.720 176.774 1.00 25.71 ?  471 TYR B C     1 
ATOM   9322  O  O     . TYR B 1 471 ? 127.179 138.781 178.008 1.00 30.05 ?  471 TYR B O     1 
ATOM   9323  C  CB    . TYR B 1 471 ? 128.066 140.639 175.455 1.00 25.45 ?  471 TYR B CB    1 
ATOM   9324  C  CG    . TYR B 1 471 ? 127.504 141.543 176.526 1.00 24.40 ?  471 TYR B CG    1 
ATOM   9325  C  CD1   . TYR B 1 471 ? 128.327 142.086 177.500 1.00 25.10 ?  471 TYR B CD1   1 
ATOM   9326  C  CD2   . TYR B 1 471 ? 126.148 141.829 176.579 1.00 15.35 ?  471 TYR B CD2   1 
ATOM   9327  C  CE1   . TYR B 1 471 ? 127.817 142.902 178.487 1.00 22.93 ?  471 TYR B CE1   1 
ATOM   9328  C  CE2   . TYR B 1 471 ? 125.631 142.635 177.566 1.00 19.90 ?  471 TYR B CE2   1 
ATOM   9329  C  CZ    . TYR B 1 471 ? 126.468 143.173 178.512 1.00 26.35 ?  471 TYR B CZ    1 
ATOM   9330  O  OH    . TYR B 1 471 ? 125.952 143.985 179.493 1.00 36.38 ?  471 TYR B OH    1 
ATOM   9331  N  N     . LEU B 1 472 ? 126.102 138.232 176.109 1.00 28.49 ?  472 LEU B N     1 
ATOM   9332  C  CA    . LEU B 1 472 ? 124.923 137.772 176.836 1.00 21.62 ?  472 LEU B CA    1 
ATOM   9333  C  C     . LEU B 1 472 ? 125.216 136.496 177.618 1.00 28.12 ?  472 LEU B C     1 
ATOM   9334  O  O     . LEU B 1 472 ? 124.839 136.375 178.789 1.00 35.09 ?  472 LEU B O     1 
ATOM   9335  C  CB    . LEU B 1 472 ? 123.760 137.556 175.867 1.00 23.44 ?  472 LEU B CB    1 
ATOM   9336  C  CG    . LEU B 1 472 ? 123.172 138.810 175.217 1.00 25.83 ?  472 LEU B CG    1 
ATOM   9337  C  CD1   . LEU B 1 472 ? 122.213 138.430 174.101 1.00 24.57 ?  472 LEU B CD1   1 
ATOM   9338  C  CD2   . LEU B 1 472 ? 122.482 139.685 176.250 1.00 22.97 ?  472 LEU B CD2   1 
ATOM   9339  N  N     . ALA B 1 473 ? 125.890 135.532 176.987 1.00 24.54 ?  473 ALA B N     1 
ATOM   9340  C  CA    . ALA B 1 473 ? 126.195 134.274 177.655 1.00 24.14 ?  473 ALA B CA    1 
ATOM   9341  C  C     . ALA B 1 473 ? 127.198 134.462 178.783 1.00 32.15 ?  473 ALA B C     1 
ATOM   9342  O  O     . ALA B 1 473 ? 127.119 133.765 179.800 1.00 39.89 ?  473 ALA B O     1 
ATOM   9343  C  CB    . ALA B 1 473 ? 126.715 133.259 176.640 1.00 25.75 ?  473 ALA B CB    1 
ATOM   9344  N  N     . GLN B 1 474 ? 128.144 135.390 178.630 1.00 31.34 ?  474 GLN B N     1 
ATOM   9345  C  CA    . GLN B 1 474 ? 129.073 135.684 179.710 1.00 29.33 ?  474 GLN B CA    1 
ATOM   9346  C  C     . GLN B 1 474 ? 128.442 136.513 180.819 1.00 29.76 ?  474 GLN B C     1 
ATOM   9347  O  O     . GLN B 1 474 ? 129.078 136.711 181.860 1.00 40.96 ?  474 GLN B O     1 
ATOM   9348  C  CB    . GLN B 1 474 ? 130.307 136.402 179.160 1.00 31.56 ?  474 GLN B CB    1 
ATOM   9349  C  CG    . GLN B 1 474 ? 131.240 135.491 178.386 1.00 29.28 ?  474 GLN B CG    1 
ATOM   9350  C  CD    . GLN B 1 474 ? 132.383 136.240 177.739 1.00 36.08 ?  474 GLN B CD    1 
ATOM   9351  O  OE1   . GLN B 1 474 ? 133.263 136.759 178.423 1.00 42.48 ?  474 GLN B OE1   1 
ATOM   9352  N  NE2   . GLN B 1 474 ? 132.376 136.298 176.413 1.00 36.55 ?  474 GLN B NE2   1 
ATOM   9353  N  N     . ASN B 1 475 ? 127.218 137.000 180.623 1.00 32.74 ?  475 ASN B N     1 
ATOM   9354  C  CA    . ASN B 1 475 ? 126.482 137.724 181.649 1.00 35.35 ?  475 ASN B CA    1 
ATOM   9355  C  C     . ASN B 1 475 ? 125.265 136.953 182.144 1.00 36.04 ?  475 ASN B C     1 
ATOM   9356  O  O     . ASN B 1 475 ? 124.409 137.532 182.820 1.00 38.28 ?  475 ASN B O     1 
ATOM   9357  C  CB    . ASN B 1 475 ? 126.058 139.098 181.129 1.00 34.60 ?  475 ASN B CB    1 
ATOM   9358  C  CG    . ASN B 1 475 ? 127.224 140.053 180.994 1.00 32.50 ?  475 ASN B CG    1 
ATOM   9359  O  OD1   . ASN B 1 475 ? 127.497 140.845 181.894 1.00 39.35 ?  475 ASN B OD1   1 
ATOM   9360  N  ND2   . ASN B 1 475 ? 127.923 139.975 179.870 1.00 28.42 ?  475 ASN B ND2   1 
ATOM   9361  N  N     . GLY B 1 476 ? 125.169 135.667 181.823 1.00 35.89 ?  476 GLY B N     1 
ATOM   9362  C  CA    . GLY B 1 476 ? 124.063 134.844 182.279 1.00 32.40 ?  476 GLY B CA    1 
ATOM   9363  C  C     . GLY B 1 476 ? 122.714 135.216 181.706 1.00 35.20 ?  476 GLY B C     1 
ATOM   9364  O  O     . GLY B 1 476 ? 121.713 135.207 182.434 1.00 42.73 ?  476 GLY B O     1 
ATOM   9365  N  N     . ILE B 1 477 ? 122.658 135.545 180.418 1.00 32.50 ?  477 ILE B N     1 
ATOM   9366  C  CA    . ILE B 1 477 ? 121.413 135.892 179.746 1.00 32.21 ?  477 ILE B CA    1 
ATOM   9367  C  C     . ILE B 1 477 ? 121.263 135.001 178.522 1.00 32.56 ?  477 ILE B C     1 
ATOM   9368  O  O     . ILE B 1 477 ? 122.163 134.942 177.677 1.00 36.67 ?  477 ILE B O     1 
ATOM   9369  C  CB    . ILE B 1 477 ? 121.373 137.379 179.343 1.00 27.66 ?  477 ILE B CB    1 
ATOM   9370  C  CG1   . ILE B 1 477 ? 121.371 138.270 180.585 1.00 30.97 ?  477 ILE B CG1   1 
ATOM   9371  C  CG2   . ILE B 1 477 ? 120.156 137.666 178.489 1.00 26.18 ?  477 ILE B CG2   1 
ATOM   9372  C  CD1   . ILE B 1 477 ? 122.024 139.614 180.372 1.00 33.59 ?  477 ILE B CD1   1 
ATOM   9373  N  N     . ALA B 1 478 ? 120.134 134.304 178.433 1.00 33.33 ?  478 ALA B N     1 
ATOM   9374  C  CA    . ALA B 1 478 ? 119.859 133.476 177.269 1.00 28.73 ?  478 ALA B CA    1 
ATOM   9375  C  C     . ALA B 1 478 ? 119.571 134.351 176.058 1.00 34.04 ?  478 ALA B C     1 
ATOM   9376  O  O     . ALA B 1 478 ? 118.945 135.406 176.171 1.00 38.65 ?  478 ALA B O     1 
ATOM   9377  C  CB    . ALA B 1 478 ? 118.679 132.546 177.542 1.00 29.59 ?  478 ALA B CB    1 
ATOM   9378  N  N     . TYR B 1 479 ? 120.036 133.904 174.889 1.00 29.89 ?  479 TYR B N     1 
ATOM   9379  C  CA    . TYR B 1 479 ? 119.877 134.695 173.672 1.00 21.31 ?  479 TYR B CA    1 
ATOM   9380  C  C     . TYR B 1 479 ? 118.407 134.892 173.323 1.00 33.73 ?  479 TYR B C     1 
ATOM   9381  O  O     . TYR B 1 479 ? 118.010 135.970 172.867 1.00 36.22 ?  479 TYR B O     1 
ATOM   9382  C  CB    . TYR B 1 479 ? 120.624 134.024 172.521 1.00 19.78 ?  479 TYR B CB    1 
ATOM   9383  C  CG    . TYR B 1 479 ? 120.741 134.863 171.270 1.00 26.75 ?  479 TYR B CG    1 
ATOM   9384  C  CD1   . TYR B 1 479 ? 119.774 134.803 170.275 1.00 30.18 ?  479 TYR B CD1   1 
ATOM   9385  C  CD2   . TYR B 1 479 ? 121.827 135.707 171.076 1.00 23.61 ?  479 TYR B CD2   1 
ATOM   9386  C  CE1   . TYR B 1 479 ? 119.880 135.565 169.130 1.00 23.94 ?  479 TYR B CE1   1 
ATOM   9387  C  CE2   . TYR B 1 479 ? 121.942 136.470 169.934 1.00 22.72 ?  479 TYR B CE2   1 
ATOM   9388  C  CZ    . TYR B 1 479 ? 120.967 136.396 168.965 1.00 30.34 ?  479 TYR B CZ    1 
ATOM   9389  O  OH    . TYR B 1 479 ? 121.077 137.156 167.825 1.00 35.04 ?  479 TYR B OH    1 
ATOM   9390  N  N     . GLU B 1 480 ? 117.584 133.862 173.524 1.00 36.31 ?  480 GLU B N     1 
ATOM   9391  C  CA    . GLU B 1 480 ? 116.161 133.959 173.223 1.00 31.16 ?  480 GLU B CA    1 
ATOM   9392  C  C     . GLU B 1 480 ? 115.358 134.607 174.339 1.00 33.32 ?  480 GLU B C     1 
ATOM   9393  O  O     . GLU B 1 480 ? 114.153 134.819 174.166 1.00 38.14 ?  480 GLU B O     1 
ATOM   9394  C  CB    . GLU B 1 480 ? 115.580 132.572 172.945 1.00 34.29 ?  480 GLU B CB    1 
ATOM   9395  C  CG    . GLU B 1 480 ? 116.296 131.780 171.878 1.00 35.17 ?  480 GLU B CG    1 
ATOM   9396  C  CD    . GLU B 1 480 ? 116.210 130.290 172.131 1.00 43.07 ?  480 GLU B CD    1 
ATOM   9397  O  OE1   . GLU B 1 480 ? 116.968 129.791 172.988 1.00 44.45 ?  480 GLU B OE1   1 
ATOM   9398  O  OE2   . GLU B 1 480 ? 115.386 129.618 171.477 1.00 39.62 -1 480 GLU B OE2   1 
ATOM   9399  N  N     . SER B 1 481 ? 115.981 134.915 175.470 1.00 31.50 ?  481 SER B N     1 
ATOM   9400  C  CA    . SER B 1 481 ? 115.247 135.460 176.596 1.00 32.57 ?  481 SER B CA    1 
ATOM   9401  C  C     . SER B 1 481 ? 114.759 136.875 176.286 1.00 36.64 ?  481 SER B C     1 
ATOM   9402  O  O     . SER B 1 481 ? 115.371 137.592 175.489 1.00 38.79 ?  481 SER B O     1 
ATOM   9403  C  CB    . SER B 1 481 ? 116.122 135.473 177.845 1.00 30.75 ?  481 SER B CB    1 
ATOM   9404  O  OG    . SER B 1 481 ? 116.967 136.608 177.862 1.00 35.20 ?  481 SER B OG    1 
ATOM   9405  N  N     . PRO B 1 482 ? 113.643 137.292 176.888 1.00 42.31 ?  482 PRO B N     1 
ATOM   9406  C  CA    . PRO B 1 482 ? 113.211 138.689 176.731 1.00 37.58 ?  482 PRO B CA    1 
ATOM   9407  C  C     . PRO B 1 482 ? 114.220 139.689 177.262 1.00 32.77 ?  482 PRO B C     1 
ATOM   9408  O  O     . PRO B 1 482 ? 114.260 140.828 176.784 1.00 36.90 ?  482 PRO B O     1 
ATOM   9409  C  CB    . PRO B 1 482 ? 111.894 138.737 177.518 1.00 35.59 ?  482 PRO B CB    1 
ATOM   9410  C  CG    . PRO B 1 482 ? 111.422 137.326 177.553 1.00 37.34 ?  482 PRO B CG    1 
ATOM   9411  C  CD    . PRO B 1 482 ? 112.660 136.490 177.633 1.00 37.93 ?  482 PRO B CD    1 
ATOM   9412  N  N     . GLU B 1 483 ? 115.036 139.297 178.244 1.00 35.62 ?  483 GLU B N     1 
ATOM   9413  C  CA    . GLU B 1 483 ? 116.067 140.195 178.755 1.00 32.90 ?  483 GLU B CA    1 
ATOM   9414  C  C     . GLU B 1 483 ? 117.145 140.449 177.710 1.00 30.00 ?  483 GLU B C     1 
ATOM   9415  O  O     . GLU B 1 483 ? 117.698 141.552 177.636 1.00 36.41 ?  483 GLU B O     1 
ATOM   9416  C  CB    . GLU B 1 483 ? 116.676 139.616 180.032 1.00 37.13 ?  483 GLU B CB    1 
ATOM   9417  C  CG    . GLU B 1 483 ? 115.701 139.519 181.192 1.00 39.21 ?  483 GLU B CG    1 
ATOM   9418  C  CD    . GLU B 1 483 ? 115.036 138.159 181.282 1.00 45.79 ?  483 GLU B CD    1 
ATOM   9419  O  OE1   . GLU B 1 483 ? 115.146 137.379 180.315 1.00 42.62 ?  483 GLU B OE1   1 
ATOM   9420  O  OE2   . GLU B 1 483 ? 114.401 137.872 182.318 1.00 44.24 -1 483 GLU B OE2   1 
ATOM   9421  N  N     . ALA B 1 484 ? 117.465 139.439 176.899 1.00 28.45 ?  484 ALA B N     1 
ATOM   9422  C  CA    . ALA B 1 484 ? 118.422 139.640 175.817 1.00 29.24 ?  484 ALA B CA    1 
ATOM   9423  C  C     . ALA B 1 484 ? 117.903 140.649 174.802 1.00 29.55 ?  484 ALA B C     1 
ATOM   9424  O  O     . ALA B 1 484 ? 118.648 141.525 174.348 1.00 31.34 ?  484 ALA B O     1 
ATOM   9425  C  CB    . ALA B 1 484 ? 118.730 138.309 175.136 1.00 21.96 ?  484 ALA B CB    1 
ATOM   9426  N  N     . ARG B 1 485 ? 116.625 140.543 174.438 1.00 26.43 ?  485 ARG B N     1 
ATOM   9427  C  CA    . ARG B 1 485 ? 116.036 141.523 173.534 1.00 26.24 ?  485 ARG B CA    1 
ATOM   9428  C  C     . ARG B 1 485 ? 115.961 142.899 174.176 1.00 24.75 ?  485 ARG B C     1 
ATOM   9429  O  O     . ARG B 1 485 ? 116.113 143.908 173.486 1.00 35.19 ?  485 ARG B O     1 
ATOM   9430  C  CB    . ARG B 1 485 ? 114.651 141.063 173.085 1.00 28.25 ?  485 ARG B CB    1 
ATOM   9431  C  CG    . ARG B 1 485 ? 114.681 139.956 172.054 1.00 26.08 ?  485 ARG B CG    1 
ATOM   9432  C  CD    . ARG B 1 485 ? 113.308 139.723 171.455 1.00 25.72 ?  485 ARG B CD    1 
ATOM   9433  N  NE    . ARG B 1 485 ? 112.345 139.265 172.448 1.00 29.58 ?  485 ARG B NE    1 
ATOM   9434  C  CZ    . ARG B 1 485 ? 112.260 138.017 172.891 1.00 33.69 ?  485 ARG B CZ    1 
ATOM   9435  N  NH1   . ARG B 1 485 ? 113.066 137.069 172.445 1.00 35.12 1  485 ARG B NH1   1 
ATOM   9436  N  NH2   . ARG B 1 485 ? 111.341 137.715 173.803 1.00 29.72 ?  485 ARG B NH2   1 
ATOM   9437  N  N     . ASP B 1 486 ? 115.732 142.959 175.488 1.00 30.77 ?  486 ASP B N     1 
ATOM   9438  C  CA    . ASP B 1 486 ? 115.741 144.240 176.189 1.00 30.72 ?  486 ASP B CA    1 
ATOM   9439  C  C     . ASP B 1 486 ? 117.117 144.893 176.116 1.00 30.06 ?  486 ASP B C     1 
ATOM   9440  O  O     . ASP B 1 486 ? 117.240 146.096 175.836 1.00 32.61 ?  486 ASP B O     1 
ATOM   9441  C  CB    . ASP B 1 486 ? 115.310 144.024 177.639 1.00 34.22 ?  486 ASP B CB    1 
ATOM   9442  C  CG    . ASP B 1 486 ? 115.044 145.319 178.367 1.00 43.15 ?  486 ASP B CG    1 
ATOM   9443  O  OD1   . ASP B 1 486 ? 114.340 146.186 177.809 1.00 45.20 ?  486 ASP B OD1   1 
ATOM   9444  O  OD2   . ASP B 1 486 ? 115.533 145.462 179.505 1.00 34.53 -1 486 ASP B OD2   1 
ATOM   9445  N  N     . PHE B 1 487 ? 118.171 144.107 176.354 1.00 26.92 ?  487 PHE B N     1 
ATOM   9446  C  CA    . PHE B 1 487 ? 119.520 144.643 176.236 1.00 23.40 ?  487 PHE B CA    1 
ATOM   9447  C  C     . PHE B 1 487 ? 119.816 145.083 174.812 1.00 28.27 ?  487 PHE B C     1 
ATOM   9448  O  O     . PHE B 1 487 ? 120.435 146.128 174.601 1.00 30.97 ?  487 PHE B O     1 
ATOM   9449  C  CB    . PHE B 1 487 ? 120.571 143.629 176.677 1.00 24.72 ?  487 PHE B CB    1 
ATOM   9450  C  CG    . PHE B 1 487 ? 121.950 143.979 176.200 1.00 28.11 ?  487 PHE B CG    1 
ATOM   9451  C  CD1   . PHE B 1 487 ? 122.665 144.991 176.815 1.00 21.12 ?  487 PHE B CD1   1 
ATOM   9452  C  CD2   . PHE B 1 487 ? 122.511 143.339 175.108 1.00 27.86 ?  487 PHE B CD2   1 
ATOM   9453  C  CE1   . PHE B 1 487 ? 123.919 145.342 176.368 1.00 23.42 ?  487 PHE B CE1   1 
ATOM   9454  C  CE2   . PHE B 1 487 ? 123.766 143.690 174.659 1.00 26.23 ?  487 PHE B CE2   1 
ATOM   9455  C  CZ    . PHE B 1 487 ? 124.468 144.693 175.290 1.00 25.18 ?  487 PHE B CZ    1 
ATOM   9456  N  N     . ALA B 1 488 ? 119.426 144.277 173.823 1.00 26.01 ?  488 ALA B N     1 
ATOM   9457  C  CA    . ALA B 1 488 ? 119.673 144.656 172.437 1.00 20.12 ?  488 ALA B CA    1 
ATOM   9458  C  C     . ALA B 1 488 ? 118.959 145.955 172.096 1.00 29.34 ?  488 ALA B C     1 
ATOM   9459  O  O     . ALA B 1 488 ? 119.541 146.849 171.472 1.00 38.20 ?  488 ALA B O     1 
ATOM   9460  C  CB    . ALA B 1 488 ? 119.232 143.536 171.498 1.00 21.50 ?  488 ALA B CB    1 
ATOM   9461  N  N     . ASN B 1 489 ? 117.704 146.083 172.528 1.00 28.70 ?  489 ASN B N     1 
ATOM   9462  C  CA    . ASN B 1 489 ? 116.945 147.308 172.318 1.00 26.11 ?  489 ASN B CA    1 
ATOM   9463  C  C     . ASN B 1 489 ? 117.683 148.513 172.884 1.00 20.40 ?  489 ASN B C     1 
ATOM   9464  O  O     . ASN B 1 489 ? 117.942 149.487 172.169 1.00 29.68 ?  489 ASN B O     1 
ATOM   9465  C  CB    . ASN B 1 489 ? 115.568 147.165 172.965 1.00 21.16 ?  489 ASN B CB    1 
ATOM   9466  C  CG    . ASN B 1 489 ? 114.545 148.113 172.391 1.00 32.36 ?  489 ASN B CG    1 
ATOM   9467  O  OD1   . ASN B 1 489 ? 114.289 148.118 171.188 1.00 39.21 ?  489 ASN B OD1   1 
ATOM   9468  N  ND2   . ASN B 1 489 ? 113.940 148.917 173.254 1.00 31.79 ?  489 ASN B ND2   1 
ATOM   9469  N  N     . THR B 1 490 ? 118.068 148.445 174.160 1.00 22.72 ?  490 THR B N     1 
ATOM   9470  C  CA    . THR B 1 490 ? 118.710 149.595 174.791 1.00 22.67 ?  490 THR B CA    1 
ATOM   9471  C  C     . THR B 1 490 ? 120.070 149.890 174.164 1.00 24.87 ?  490 THR B C     1 
ATOM   9472  O  O     . THR B 1 490 ? 120.381 151.045 173.845 1.00 21.06 ?  490 THR B O     1 
ATOM   9473  C  CB    . THR B 1 490 ? 118.853 149.361 176.294 1.00 33.48 ?  490 THR B CB    1 
ATOM   9474  O  OG1   . THR B 1 490 ? 117.587 148.970 176.836 1.00 39.12 ?  490 THR B OG1   1 
ATOM   9475  C  CG2   . THR B 1 490 ? 119.328 150.628 176.986 1.00 27.80 ?  490 THR B CG2   1 
ATOM   9476  N  N     . PHE B 1 491 ? 120.885 148.852 173.969 1.00 25.08 ?  491 PHE B N     1 
ATOM   9477  C  CA    . PHE B 1 491 ? 122.238 149.035 173.456 1.00 19.01 ?  491 PHE B CA    1 
ATOM   9478  C  C     . PHE B 1 491 ? 122.221 149.633 172.060 1.00 25.49 ?  491 PHE B C     1 
ATOM   9479  O  O     . PHE B 1 491 ? 122.965 150.575 171.767 1.00 33.73 ?  491 PHE B O     1 
ATOM   9480  C  CB    . PHE B 1 491 ? 122.976 147.695 173.459 1.00 23.13 ?  491 PHE B CB    1 
ATOM   9481  C  CG    . PHE B 1 491 ? 124.370 147.764 172.898 1.00 25.07 ?  491 PHE B CG    1 
ATOM   9482  C  CD1   . PHE B 1 491 ? 125.446 148.044 173.720 1.00 23.22 ?  491 PHE B CD1   1 
ATOM   9483  C  CD2   . PHE B 1 491 ? 124.607 147.536 171.552 1.00 20.50 ?  491 PHE B CD2   1 
ATOM   9484  C  CE1   . PHE B 1 491 ? 126.727 148.108 173.212 1.00 14.85 ?  491 PHE B CE1   1 
ATOM   9485  C  CE2   . PHE B 1 491 ? 125.883 147.601 171.039 1.00 15.76 ?  491 PHE B CE2   1 
ATOM   9486  C  CZ    . PHE B 1 491 ? 126.945 147.887 171.871 1.00 19.74 ?  491 PHE B CZ    1 
ATOM   9487  N  N     . PHE B 1 492 ? 121.381 149.099 171.175 1.00 20.89 ?  492 PHE B N     1 
ATOM   9488  C  CA    . PHE B 1 492 ? 121.366 149.610 169.817 1.00 12.88 ?  492 PHE B CA    1 
ATOM   9489  C  C     . PHE B 1 492 ? 120.624 150.932 169.699 1.00 10.87 ?  492 PHE B C     1 
ATOM   9490  O  O     . PHE B 1 492 ? 120.941 151.714 168.799 1.00 24.78 ?  492 PHE B O     1 
ATOM   9491  C  CB    . PHE B 1 492 ? 120.795 148.554 168.875 1.00 14.12 ?  492 PHE B CB    1 
ATOM   9492  C  CG    . PHE B 1 492 ? 121.753 147.432 168.604 1.00 16.24 ?  492 PHE B CG    1 
ATOM   9493  C  CD1   . PHE B 1 492 ? 122.788 147.594 167.702 1.00 10.13 ?  492 PHE B CD1   1 
ATOM   9494  C  CD2   . PHE B 1 492 ? 121.648 146.232 169.285 1.00 18.24 ?  492 PHE B CD2   1 
ATOM   9495  C  CE1   . PHE B 1 492 ? 123.681 146.574 167.463 1.00 8.63  ?  492 PHE B CE1   1 
ATOM   9496  C  CE2   . PHE B 1 492 ? 122.539 145.208 169.050 1.00 12.97 ?  492 PHE B CE2   1 
ATOM   9497  C  CZ    . PHE B 1 492 ? 123.556 145.378 168.138 1.00 15.74 ?  492 PHE B CZ    1 
ATOM   9498  N  N     . MET B 1 493 ? 119.692 151.234 170.610 1.00 14.89 ?  493 MET B N     1 
ATOM   9499  C  CA    . MET B 1 493 ? 119.175 152.596 170.674 1.00 17.34 ?  493 MET B CA    1 
ATOM   9500  C  C     . MET B 1 493 ? 120.284 153.576 171.023 1.00 22.68 ?  493 MET B C     1 
ATOM   9501  O  O     . MET B 1 493 ? 120.383 154.650 170.424 1.00 29.67 ?  493 MET B O     1 
ATOM   9502  C  CB    . MET B 1 493 ? 118.053 152.698 171.703 1.00 19.23 ?  493 MET B CB    1 
ATOM   9503  C  CG    . MET B 1 493 ? 117.480 154.103 171.825 1.00 18.99 ?  493 MET B CG    1 
ATOM   9504  S  SD    . MET B 1 493 ? 118.083 155.020 173.257 1.00 37.89 ?  493 MET B SD    1 
ATOM   9505  C  CE    . MET B 1 493 ? 118.038 153.762 174.525 1.00 27.76 ?  493 MET B CE    1 
ATOM   9506  N  N     . MET B 1 494 ? 121.131 153.222 171.995 1.00 22.12 ?  494 MET B N     1 
ATOM   9507  C  CA    . MET B 1 494 ? 122.249 154.091 172.353 1.00 17.02 ?  494 MET B CA    1 
ATOM   9508  C  C     . MET B 1 494 ? 123.233 154.230 171.198 1.00 18.65 ?  494 MET B C     1 
ATOM   9509  O  O     . MET B 1 494 ? 123.749 155.325 170.939 1.00 31.25 ?  494 MET B O     1 
ATOM   9510  C  CB    . MET B 1 494 ? 122.959 153.557 173.596 1.00 23.61 ?  494 MET B CB    1 
ATOM   9511  C  CG    . MET B 1 494 ? 122.078 153.443 174.824 1.00 22.05 ?  494 MET B CG    1 
ATOM   9512  S  SD    . MET B 1 494 ? 123.014 153.086 176.319 1.00 42.56 ?  494 MET B SD    1 
ATOM   9513  C  CE    . MET B 1 494 ? 124.287 154.338 176.222 1.00 31.53 ?  494 MET B CE    1 
ATOM   9514  N  N     . VAL B 1 495 ? 123.515 153.125 170.505 1.00 19.82 ?  495 VAL B N     1 
ATOM   9515  C  CA    . VAL B 1 495 ? 124.425 153.170 169.364 1.00 13.54 ?  495 VAL B CA    1 
ATOM   9516  C  C     . VAL B 1 495 ? 123.871 154.081 168.279 1.00 18.91 ?  495 VAL B C     1 
ATOM   9517  O  O     . VAL B 1 495 ? 124.595 154.906 167.714 1.00 31.74 ?  495 VAL B O     1 
ATOM   9518  C  CB    . VAL B 1 495 ? 124.686 151.748 168.835 1.00 15.39 ?  495 VAL B CB    1 
ATOM   9519  C  CG1   . VAL B 1 495 ? 125.341 151.799 167.465 1.00 13.43 ?  495 VAL B CG1   1 
ATOM   9520  C  CG2   . VAL B 1 495 ? 125.549 150.972 169.811 1.00 14.04 ?  495 VAL B CG2   1 
ATOM   9521  N  N     . ASN B 1 496 ? 122.576 153.952 167.977 1.00 25.04 ?  496 ASN B N     1 
ATOM   9522  C  CA    . ASN B 1 496 ? 121.952 154.822 166.987 1.00 14.39 ?  496 ASN B CA    1 
ATOM   9523  C  C     . ASN B 1 496 ? 121.985 156.276 167.432 1.00 17.48 ?  496 ASN B C     1 
ATOM   9524  O  O     . ASN B 1 496 ? 122.268 157.172 166.630 1.00 27.82 ?  496 ASN B O     1 
ATOM   9525  C  CB    . ASN B 1 496 ? 120.513 154.372 166.734 1.00 13.17 ?  496 ASN B CB    1 
ATOM   9526  C  CG    . ASN B 1 496 ? 119.956 154.903 165.433 1.00 14.73 ?  496 ASN B CG    1 
ATOM   9527  O  OD1   . ASN B 1 496 ? 120.654 154.955 164.424 1.00 25.58 ?  496 ASN B OD1   1 
ATOM   9528  N  ND2   . ASN B 1 496 ? 118.692 155.298 165.450 1.00 17.11 ?  496 ASN B ND2   1 
ATOM   9529  N  N     . PHE B 1 497 ? 121.702 156.529 168.711 1.00 18.74 ?  497 PHE B N     1 
ATOM   9530  C  CA    . PHE B 1 497 ? 121.714 157.890 169.231 1.00 12.68 ?  497 PHE B CA    1 
ATOM   9531  C  C     . PHE B 1 497 ? 123.079 158.531 169.047 1.00 24.73 ?  497 PHE B C     1 
ATOM   9532  O  O     . PHE B 1 497 ? 123.191 159.648 168.531 1.00 30.72 ?  497 PHE B O     1 
ATOM   9533  C  CB    . PHE B 1 497 ? 121.322 157.881 170.710 1.00 15.59 ?  497 PHE B CB    1 
ATOM   9534  C  CG    . PHE B 1 497 ? 121.260 159.244 171.334 1.00 19.96 ?  497 PHE B CG    1 
ATOM   9535  C  CD1   . PHE B 1 497 ? 120.097 159.991 171.281 1.00 29.44 ?  497 PHE B CD1   1 
ATOM   9536  C  CD2   . PHE B 1 497 ? 122.360 159.774 171.986 1.00 22.87 ?  497 PHE B CD2   1 
ATOM   9537  C  CE1   . PHE B 1 497 ? 120.037 161.242 171.856 1.00 27.07 ?  497 PHE B CE1   1 
ATOM   9538  C  CE2   . PHE B 1 497 ? 122.304 161.025 172.562 1.00 25.28 ?  497 PHE B CE2   1 
ATOM   9539  C  CZ    . PHE B 1 497 ? 121.142 161.759 172.497 1.00 28.44 ?  497 PHE B CZ    1 
ATOM   9540  N  N     . TYR B 1 498 ? 124.134 157.824 169.444 1.00 28.15 ?  498 TYR B N     1 
ATOM   9541  C  CA    . TYR B 1 498 ? 125.461 158.419 169.387 1.00 19.30 ?  498 TYR B CA    1 
ATOM   9542  C  C     . TYR B 1 498 ? 126.009 158.461 167.968 1.00 24.34 ?  498 TYR B C     1 
ATOM   9543  O  O     . TYR B 1 498 ? 126.781 159.366 167.644 1.00 35.03 ?  498 TYR B O     1 
ATOM   9544  C  CB    . TYR B 1 498 ? 126.401 157.681 170.337 1.00 20.21 ?  498 TYR B CB    1 
ATOM   9545  C  CG    . TYR B 1 498 ? 126.072 157.989 171.777 1.00 26.02 ?  498 TYR B CG    1 
ATOM   9546  C  CD1   . TYR B 1 498 ? 126.075 159.298 172.237 1.00 29.24 ?  498 TYR B CD1   1 
ATOM   9547  C  CD2   . TYR B 1 498 ? 125.723 156.982 172.665 1.00 25.53 ?  498 TYR B CD2   1 
ATOM   9548  C  CE1   . TYR B 1 498 ? 125.760 159.595 173.545 1.00 29.00 ?  498 TYR B CE1   1 
ATOM   9549  C  CE2   . TYR B 1 498 ? 125.406 157.270 173.977 1.00 26.42 ?  498 TYR B CE2   1 
ATOM   9550  C  CZ    . TYR B 1 498 ? 125.427 158.579 174.412 1.00 33.24 ?  498 TYR B CZ    1 
ATOM   9551  O  OH    . TYR B 1 498 ? 125.113 158.875 175.718 1.00 37.24 ?  498 TYR B OH    1 
ATOM   9552  N  N     . SER B 1 499 ? 125.588 157.546 167.092 1.00 18.28 ?  499 SER B N     1 
ATOM   9553  C  CA    . SER B 1 499 ? 125.991 157.647 165.693 1.00 10.43 ?  499 SER B CA    1 
ATOM   9554  C  C     . SER B 1 499 ? 125.315 158.831 165.013 1.00 18.82 ?  499 SER B C     1 
ATOM   9555  O  O     . SER B 1 499 ? 125.954 159.557 164.243 1.00 27.20 ?  499 SER B O     1 
ATOM   9556  C  CB    . SER B 1 499 ? 125.680 156.345 164.957 1.00 8.27  ?  499 SER B CB    1 
ATOM   9557  O  OG    . SER B 1 499 ? 124.299 156.229 164.676 1.00 24.13 ?  499 SER B OG    1 
ATOM   9558  N  N     . ILE B 1 500 ? 124.029 159.060 165.299 1.00 16.69 ?  500 ILE B N     1 
ATOM   9559  C  CA    . ILE B 1 500 ? 123.347 160.239 164.771 1.00 20.33 ?  500 ILE B CA    1 
ATOM   9560  C  C     . ILE B 1 500 ? 123.984 161.507 165.316 1.00 21.42 ?  500 ILE B C     1 
ATOM   9561  O  O     . ILE B 1 500 ? 124.179 162.487 164.586 1.00 26.70 ?  500 ILE B O     1 
ATOM   9562  C  CB    . ILE B 1 500 ? 121.843 160.185 165.097 1.00 24.31 ?  500 ILE B CB    1 
ATOM   9563  C  CG1   . ILE B 1 500 ? 121.165 159.041 164.353 1.00 21.83 ?  500 ILE B CG1   1 
ATOM   9564  C  CG2   . ILE B 1 500 ? 121.172 161.494 164.730 1.00 19.07 ?  500 ILE B CG2   1 
ATOM   9565  C  CD1   . ILE B 1 500 ? 119.805 158.708 164.898 1.00 18.71 ?  500 ILE B CD1   1 
ATOM   9566  N  N     . GLN B 1 501 ? 124.306 161.515 166.612 1.00 29.10 ?  501 GLN B N     1 
ATOM   9567  C  CA    . GLN B 1 501 ? 124.930 162.688 167.212 1.00 25.39 ?  501 GLN B CA    1 
ATOM   9568  C  C     . GLN B 1 501 ? 126.291 162.972 166.591 1.00 26.73 ?  501 GLN B C     1 
ATOM   9569  O  O     . GLN B 1 501 ? 126.609 164.124 166.282 1.00 39.62 ?  501 GLN B O     1 
ATOM   9570  C  CB    . GLN B 1 501 ? 125.059 162.499 168.721 1.00 30.32 ?  501 GLN B CB    1 
ATOM   9571  C  CG    . GLN B 1 501 ? 124.957 163.789 169.507 1.00 29.00 ?  501 GLN B CG    1 
ATOM   9572  C  CD    . GLN B 1 501 ? 125.092 163.571 170.995 1.00 33.80 ?  501 GLN B CD    1 
ATOM   9573  O  OE1   . GLN B 1 501 ? 126.086 163.019 171.464 1.00 39.72 ?  501 GLN B OE1   1 
ATOM   9574  N  NE2   . GLN B 1 501 ? 124.090 164.004 171.750 1.00 34.98 ?  501 GLN B NE2   1 
ATOM   9575  N  N     . ARG B 1 502 ? 127.105 161.934 166.387 1.00 31.15 ?  502 ARG B N     1 
ATOM   9576  C  CA    . ARG B 1 502 ? 128.410 162.134 165.770 1.00 23.02 ?  502 ARG B CA    1 
ATOM   9577  C  C     . ARG B 1 502 ? 128.277 162.583 164.322 1.00 22.55 ?  502 ARG B C     1 
ATOM   9578  O  O     . ARG B 1 502 ? 129.059 163.416 163.856 1.00 30.10 ?  502 ARG B O     1 
ATOM   9579  C  CB    . ARG B 1 502 ? 129.241 160.856 165.859 1.00 20.77 ?  502 ARG B CB    1 
ATOM   9580  C  CG    . ARG B 1 502 ? 130.705 161.063 165.519 1.00 25.50 ?  502 ARG B CG    1 
ATOM   9581  C  CD    . ARG B 1 502 ? 131.299 162.196 166.335 1.00 28.07 ?  502 ARG B CD    1 
ATOM   9582  N  NE    . ARG B 1 502 ? 132.604 162.604 165.833 1.00 28.04 ?  502 ARG B NE    1 
ATOM   9583  C  CZ    . ARG B 1 502 ? 133.042 163.855 165.815 1.00 27.28 ?  502 ARG B CZ    1 
ATOM   9584  N  NH1   . ARG B 1 502 ? 132.300 164.853 166.265 1.00 32.98 1  502 ARG B NH1   1 
ATOM   9585  N  NH2   . ARG B 1 502 ? 134.253 164.111 165.333 1.00 29.36 ?  502 ARG B NH2   1 
ATOM   9586  N  N     . SER B 1 503 ? 127.303 162.041 163.593 1.00 23.22 ?  503 SER B N     1 
ATOM   9587  C  CA    . SER B 1 503 ? 127.097 162.460 162.211 1.00 22.24 ?  503 SER B CA    1 
ATOM   9588  C  C     . SER B 1 503 ? 126.679 163.924 162.136 1.00 26.36 ?  503 SER B C     1 
ATOM   9589  O  O     . SER B 1 503 ? 127.174 164.677 161.290 1.00 33.93 ?  503 SER B O     1 
ATOM   9590  C  CB    . SER B 1 503 ? 126.053 161.562 161.553 1.00 16.91 ?  503 SER B CB    1 
ATOM   9591  O  OG    . SER B 1 503 ? 126.200 161.544 160.146 1.00 25.82 ?  503 SER B OG    1 
ATOM   9592  N  N     . ALA B 1 504 ? 125.779 164.349 163.024 1.00 25.08 ?  504 ALA B N     1 
ATOM   9593  C  CA    . ALA B 1 504 ? 125.382 165.752 163.055 1.00 22.29 ?  504 ALA B CA    1 
ATOM   9594  C  C     . ALA B 1 504 ? 126.537 166.645 163.489 1.00 31.28 ?  504 ALA B C     1 
ATOM   9595  O  O     . ALA B 1 504 ? 126.679 167.767 162.993 1.00 38.19 ?  504 ALA B O     1 
ATOM   9596  C  CB    . ALA B 1 504 ? 124.179 165.935 163.977 1.00 22.33 ?  504 ALA B CB    1 
ATOM   9597  N  N     . GLU B 1 505 ? 127.376 166.166 164.410 1.00 29.93 ?  505 GLU B N     1 
ATOM   9598  C  CA    . GLU B 1 505 ? 128.553 166.929 164.816 1.00 26.45 ?  505 GLU B CA    1 
ATOM   9599  C  C     . GLU B 1 505 ? 129.535 167.089 163.662 1.00 34.37 ?  505 GLU B C     1 
ATOM   9600  O  O     . GLU B 1 505 ? 130.116 168.164 163.481 1.00 39.07 ?  505 GLU B O     1 
ATOM   9601  C  CB    . GLU B 1 505 ? 129.230 166.248 166.005 1.00 26.96 ?  505 GLU B CB    1 
ATOM   9602  C  CG    . GLU B 1 505 ? 128.532 166.476 167.332 1.00 31.27 ?  505 GLU B CG    1 
ATOM   9603  C  CD    . GLU B 1 505 ? 128.907 165.439 168.372 1.00 37.60 ?  505 GLU B CD    1 
ATOM   9604  O  OE1   . GLU B 1 505 ? 129.786 164.600 168.088 1.00 39.01 ?  505 GLU B OE1   1 
ATOM   9605  O  OE2   . GLU B 1 505 ? 128.323 165.464 169.474 1.00 41.19 -1 505 GLU B OE2   1 
ATOM   9606  N  N     . ILE B 1 506 ? 129.740 166.028 162.879 1.00 32.03 ?  506 ILE B N     1 
ATOM   9607  C  CA    . ILE B 1 506 ? 130.610 166.117 161.711 1.00 26.15 ?  506 ILE B CA    1 
ATOM   9608  C  C     . ILE B 1 506 ? 130.021 167.071 160.681 1.00 26.57 ?  506 ILE B C     1 
ATOM   9609  O  O     . ILE B 1 506 ? 130.746 167.847 160.047 1.00 37.47 ?  506 ILE B O     1 
ATOM   9610  C  CB    . ILE B 1 506 ? 130.855 164.717 161.119 1.00 27.51 ?  506 ILE B CB    1 
ATOM   9611  C  CG1   . ILE B 1 506 ? 131.637 163.849 162.105 1.00 32.53 ?  506 ILE B CG1   1 
ATOM   9612  C  CG2   . ILE B 1 506 ? 131.601 164.810 159.799 1.00 24.74 ?  506 ILE B CG2   1 
ATOM   9613  C  CD1   . ILE B 1 506 ? 131.651 162.380 161.749 1.00 24.63 ?  506 ILE B CD1   1 
ATOM   9614  N  N     . ALA B 1 507 ? 128.700 167.029 160.494 1.00 29.52 ?  507 ALA B N     1 
ATOM   9615  C  CA    . ALA B 1 507 ? 128.055 167.960 159.574 1.00 29.58 ?  507 ALA B CA    1 
ATOM   9616  C  C     . ALA B 1 507 ? 128.235 169.402 160.032 1.00 31.40 ?  507 ALA B C     1 
ATOM   9617  O  O     . ALA B 1 507 ? 128.481 170.295 159.215 1.00 37.98 ?  507 ALA B O     1 
ATOM   9618  C  CB    . ALA B 1 507 ? 126.572 167.620 159.439 1.00 26.16 ?  507 ALA B CB    1 
ATOM   9619  N  N     . LYS B 1 508 ? 128.108 169.648 161.337 1.00 35.98 ?  508 LYS B N     1 
ATOM   9620  C  CA    . LYS B 1 508 ? 128.328 170.988 161.872 1.00 36.46 ?  508 LYS B CA    1 
ATOM   9621  C  C     . LYS B 1 508 ? 129.778 171.426 161.700 1.00 39.38 ?  508 LYS B C     1 
ATOM   9622  O  O     . LYS B 1 508 ? 130.047 172.583 161.358 1.00 43.84 ?  508 LYS B O     1 
ATOM   9623  C  CB    . LYS B 1 508 ? 127.925 171.029 163.346 1.00 41.04 ?  508 LYS B CB    1 
ATOM   9624  C  CG    . LYS B 1 508 ? 128.174 172.359 164.028 1.00 38.72 ?  508 LYS B CG    1 
ATOM   9625  C  CD    . LYS B 1 508 ? 127.980 172.247 165.528 1.00 39.11 ?  508 LYS B CD    1 
ATOM   9626  C  CE    . LYS B 1 508 ? 128.068 173.606 166.200 1.00 41.74 ?  508 LYS B CE    1 
ATOM   9627  N  NZ    . LYS B 1 508 ? 127.227 173.675 167.426 1.00 46.13 1  508 LYS B NZ    1 
ATOM   9628  N  N     . GLU B 1 509 ? 130.726 170.516 161.938 1.00 42.09 ?  509 GLU B N     1 
ATOM   9629  C  CA    . GLU B 1 509 ? 132.138 170.861 161.821 1.00 40.27 ?  509 GLU B CA    1 
ATOM   9630  C  C     . GLU B 1 509 ? 132.517 171.175 160.380 1.00 42.88 ?  509 GLU B C     1 
ATOM   9631  O  O     . GLU B 1 509 ? 133.218 172.159 160.117 1.00 49.18 ?  509 GLU B O     1 
ATOM   9632  C  CB    . GLU B 1 509 ? 133.000 169.720 162.362 1.00 37.70 ?  509 GLU B CB    1 
ATOM   9633  C  CG    . GLU B 1 509 ? 133.289 169.808 163.851 1.00 46.70 ?  509 GLU B CG    1 
ATOM   9634  C  CD    . GLU B 1 509 ? 133.506 168.445 164.484 1.00 50.17 ?  509 GLU B CD    1 
ATOM   9635  O  OE1   . GLU B 1 509 ? 134.070 167.557 163.810 1.00 48.52 ?  509 GLU B OE1   1 
ATOM   9636  O  OE2   . GLU B 1 509 ? 133.112 168.262 165.656 1.00 45.41 -1 509 GLU B OE2   1 
ATOM   9637  N  N     . LYS B 1 510 ? 132.068 170.352 159.436 1.00 38.56 ?  510 LYS B N     1 
ATOM   9638  C  CA    . LYS B 1 510 ? 132.378 170.550 158.029 1.00 32.84 ?  510 LYS B CA    1 
ATOM   9639  C  C     . LYS B 1 510 ? 131.398 171.478 157.325 1.00 38.42 ?  510 LYS B C     1 
ATOM   9640  O  O     . LYS B 1 510 ? 131.645 171.854 156.176 1.00 46.93 ?  510 LYS B O     1 
ATOM   9641  C  CB    . LYS B 1 510 ? 132.411 169.202 157.303 1.00 29.42 ?  510 LYS B CB    1 
ATOM   9642  C  CG    . LYS B 1 510 ? 133.323 168.176 157.946 1.00 32.23 ?  510 LYS B CG    1 
ATOM   9643  C  CD    . LYS B 1 510 ? 133.493 166.957 157.059 1.00 35.69 ?  510 LYS B CD    1 
ATOM   9644  C  CE    . LYS B 1 510 ? 134.436 165.944 157.684 1.00 39.38 ?  510 LYS B CE    1 
ATOM   9645  N  NZ    . LYS B 1 510 ? 135.134 165.126 156.658 1.00 41.14 1  510 LYS B NZ    1 
ATOM   9646  N  N     . GLY B 1 511 ? 130.304 171.854 157.982 1.00 36.32 ?  511 GLY B N     1 
ATOM   9647  C  CA    . GLY B 1 511 ? 129.314 172.710 157.361 1.00 37.95 ?  511 GLY B CA    1 
ATOM   9648  C  C     . GLY B 1 511 ? 128.571 172.091 156.203 1.00 40.49 ?  511 GLY B C     1 
ATOM   9649  O  O     . GLY B 1 511 ? 127.895 172.813 155.463 1.00 43.77 ?  511 GLY B O     1 
ATOM   9650  N  N     . GLU B 1 512 ? 128.668 170.777 156.021 1.00 34.43 ?  512 GLU B N     1 
ATOM   9651  C  CA    . GLU B 1 512 ? 128.043 170.100 154.895 1.00 30.22 ?  512 GLU B CA    1 
ATOM   9652  C  C     . GLU B 1 512 ? 127.352 168.833 155.371 1.00 31.48 ?  512 GLU B C     1 
ATOM   9653  O  O     . GLU B 1 512 ? 127.841 168.149 156.273 1.00 36.31 ?  512 GLU B O     1 
ATOM   9654  C  CB    . GLU B 1 512 ? 129.070 169.753 153.813 1.00 33.01 ?  512 GLU B CB    1 
ATOM   9655  C  CG    . GLU B 1 512 ? 130.301 169.043 154.343 1.00 32.71 ?  512 GLU B CG    1 
ATOM   9656  C  CD    . GLU B 1 512 ? 131.093 168.357 153.251 1.00 38.28 ?  512 GLU B CD    1 
ATOM   9657  O  OE1   . GLU B 1 512 ? 130.505 168.048 152.193 1.00 37.92 ?  512 GLU B OE1   1 
ATOM   9658  O  OE2   . GLU B 1 512 ? 132.304 168.123 153.451 1.00 39.66 -1 512 GLU B OE2   1 
ATOM   9659  N  N     . THR B 1 513 ? 126.215 168.532 154.759 1.00 34.26 ?  513 THR B N     1 
ATOM   9660  C  CA    . THR B 1 513 ? 125.484 167.293 154.967 1.00 32.81 ?  513 THR B CA    1 
ATOM   9661  C  C     . THR B 1 513 ? 125.681 166.395 153.752 1.00 28.84 ?  513 THR B C     1 
ATOM   9662  O  O     . THR B 1 513 ? 126.426 166.723 152.825 1.00 38.58 ?  513 THR B O     1 
ATOM   9663  C  CB    . THR B 1 513 ? 124.003 167.581 155.213 1.00 31.71 ?  513 THR B CB    1 
ATOM   9664  O  OG1   . THR B 1 513 ? 123.402 168.066 154.007 1.00 33.73 ?  513 THR B OG1   1 
ATOM   9665  C  CG2   . THR B 1 513 ? 123.848 168.630 156.291 1.00 29.90 ?  513 THR B CG2   1 
ATOM   9666  N  N     . PHE B 1 514 ? 125.011 165.247 153.753 1.00 22.87 ?  514 PHE B N     1 
ATOM   9667  C  CA    . PHE B 1 514 ? 125.082 164.419 152.562 1.00 25.65 ?  514 PHE B CA    1 
ATOM   9668  C  C     . PHE B 1 514 ? 124.137 164.962 151.496 1.00 25.87 ?  514 PHE B C     1 
ATOM   9669  O  O     . PHE B 1 514 ? 123.218 165.734 151.776 1.00 32.72 ?  514 PHE B O     1 
ATOM   9670  C  CB    . PHE B 1 514 ? 124.767 162.953 152.876 1.00 20.36 ?  514 PHE B CB    1 
ATOM   9671  C  CG    . PHE B 1 514 ? 123.369 162.705 153.372 1.00 20.87 ?  514 PHE B CG    1 
ATOM   9672  C  CD1   . PHE B 1 514 ? 123.059 162.842 154.712 1.00 18.94 ?  514 PHE B CD1   1 
ATOM   9673  C  CD2   . PHE B 1 514 ? 122.375 162.297 152.501 1.00 20.33 ?  514 PHE B CD2   1 
ATOM   9674  C  CE1   . PHE B 1 514 ? 121.784 162.595 155.171 1.00 13.71 ?  514 PHE B CE1   1 
ATOM   9675  C  CE2   . PHE B 1 514 ? 121.096 162.049 152.955 1.00 17.18 ?  514 PHE B CE2   1 
ATOM   9676  C  CZ    . PHE B 1 514 ? 120.801 162.199 154.291 1.00 16.99 ?  514 PHE B CZ    1 
ATOM   9677  N  N     . ASP B 1 515 ? 124.394 164.568 150.252 1.00 27.24 ?  515 ASP B N     1 
ATOM   9678  C  CA    . ASP B 1 515 ? 123.614 165.088 149.139 1.00 29.97 ?  515 ASP B CA    1 
ATOM   9679  C  C     . ASP B 1 515 ? 122.155 164.672 149.267 1.00 33.38 ?  515 ASP B C     1 
ATOM   9680  O  O     . ASP B 1 515 ? 121.844 163.524 149.594 1.00 43.02 ?  515 ASP B O     1 
ATOM   9681  C  CB    . ASP B 1 515 ? 124.194 164.602 147.812 1.00 31.84 ?  515 ASP B CB    1 
ATOM   9682  C  CG    . ASP B 1 515 ? 125.458 165.346 147.428 1.00 34.96 ?  515 ASP B CG    1 
ATOM   9683  O  OD1   . ASP B 1 515 ? 126.070 165.979 148.312 1.00 34.91 ?  515 ASP B OD1   1 
ATOM   9684  O  OD2   . ASP B 1 515 ? 125.839 165.298 146.240 1.00 37.22 -1 515 ASP B OD2   1 
ATOM   9685  N  N     . GLN B 1 516 ? 121.260 165.626 149.007 1.00 33.32 ?  516 GLN B N     1 
ATOM   9686  C  CA    . GLN B 1 516 ? 119.816 165.425 149.130 1.00 29.64 ?  516 GLN B CA    1 
ATOM   9687  C  C     . GLN B 1 516 ? 119.426 165.039 150.555 1.00 32.54 ?  516 GLN B C     1 
ATOM   9688  O  O     . GLN B 1 516 ? 118.515 164.237 150.772 1.00 39.69 ?  516 GLN B O     1 
ATOM   9689  C  CB    . GLN B 1 516 ? 119.313 164.385 148.125 1.00 27.02 ?  516 GLN B CB    1 
ATOM   9690  C  CG    . GLN B 1 516 ? 119.665 164.695 146.683 1.00 30.65 ?  516 GLN B CG    1 
ATOM   9691  C  CD    . GLN B 1 516 ? 119.518 163.490 145.779 1.00 38.64 ?  516 GLN B CD    1 
ATOM   9692  O  OE1   . GLN B 1 516 ? 118.416 163.158 145.345 1.00 37.40 ?  516 GLN B OE1   1 
ATOM   9693  N  NE2   . GLN B 1 516 ? 120.632 162.825 145.494 1.00 38.99 ?  516 GLN B NE2   1 
ATOM   9694  N  N     . TYR B 1 517 ? 120.126 165.610 151.537 1.00 27.08 ?  517 TYR B N     1 
ATOM   9695  C  CA    . TYR B 1 517 ? 119.742 165.401 152.929 1.00 23.87 ?  517 TYR B CA    1 
ATOM   9696  C  C     . TYR B 1 517 ? 118.417 166.084 153.242 1.00 33.52 ?  517 TYR B C     1 
ATOM   9697  O  O     . TYR B 1 517 ? 117.622 165.573 154.039 1.00 42.64 ?  517 TYR B O     1 
ATOM   9698  C  CB    . TYR B 1 517 ? 120.836 165.910 153.869 1.00 21.30 ?  517 TYR B CB    1 
ATOM   9699  C  CG    . TYR B 1 517 ? 120.317 166.341 155.225 1.00 30.35 ?  517 TYR B CG    1 
ATOM   9700  C  CD1   . TYR B 1 517 ? 120.124 165.416 156.241 1.00 21.55 ?  517 TYR B CD1   1 
ATOM   9701  C  CD2   . TYR B 1 517 ? 120.020 167.674 155.488 1.00 31.64 ?  517 TYR B CD2   1 
ATOM   9702  C  CE1   . TYR B 1 517 ? 119.646 165.802 157.476 1.00 28.97 ?  517 TYR B CE1   1 
ATOM   9703  C  CE2   . TYR B 1 517 ? 119.540 168.067 156.718 1.00 27.98 ?  517 TYR B CE2   1 
ATOM   9704  C  CZ    . TYR B 1 517 ? 119.355 167.128 157.708 1.00 32.53 ?  517 TYR B CZ    1 
ATOM   9705  O  OH    . TYR B 1 517 ? 118.880 167.520 158.937 1.00 37.96 ?  517 TYR B OH    1 
ATOM   9706  N  N     . GLU B 1 518 ? 118.169 167.243 152.629 1.00 31.78 ?  518 GLU B N     1 
ATOM   9707  C  CA    . GLU B 1 518 ? 117.011 168.061 152.973 1.00 35.03 ?  518 GLU B CA    1 
ATOM   9708  C  C     . GLU B 1 518 ? 115.691 167.340 152.741 1.00 37.14 ?  518 GLU B C     1 
ATOM   9709  O  O     . GLU B 1 518 ? 114.698 167.665 153.398 1.00 41.81 ?  518 GLU B O     1 
ATOM   9710  C  CB    . GLU B 1 518 ? 117.039 169.368 152.177 1.00 33.49 ?  518 GLU B CB    1 
ATOM   9711  C  CG    . GLU B 1 518 ? 118.407 170.038 152.113 1.00 37.43 ?  518 GLU B CG    1 
ATOM   9712  C  CD    . GLU B 1 518 ? 119.287 169.484 151.006 1.00 46.20 ?  518 GLU B CD    1 
ATOM   9713  O  OE1   . GLU B 1 518 ? 118.813 169.395 149.854 1.00 44.98 ?  518 GLU B OE1   1 
ATOM   9714  O  OE2   . GLU B 1 518 ? 120.452 169.133 151.290 1.00 40.78 -1 518 GLU B OE2   1 
ATOM   9715  N  N     . GLY B 1 519 ? 115.654 166.377 151.824 1.00 28.86 ?  519 GLY B N     1 
ATOM   9716  C  CA    . GLY B 1 519 ? 114.461 165.579 151.627 1.00 23.81 ?  519 GLY B CA    1 
ATOM   9717  C  C     . GLY B 1 519 ? 114.329 164.378 152.530 1.00 25.57 ?  519 GLY B C     1 
ATOM   9718  O  O     . GLY B 1 519 ? 113.290 163.715 152.513 1.00 33.54 ?  519 GLY B O     1 
ATOM   9719  N  N     . SER B 1 520 ? 115.352 164.084 153.328 1.00 25.82 ?  520 SER B N     1 
ATOM   9720  C  CA    . SER B 1 520 ? 115.352 162.887 154.152 1.00 23.88 ?  520 SER B CA    1 
ATOM   9721  C  C     . SER B 1 520 ? 114.429 163.048 155.356 1.00 26.94 ?  520 SER B C     1 
ATOM   9722  O  O     . SER B 1 520 ? 114.008 164.152 155.714 1.00 27.18 ?  520 SER B O     1 
ATOM   9723  C  CB    . SER B 1 520 ? 116.769 162.560 154.621 1.00 21.54 ?  520 SER B CB    1 
ATOM   9724  O  OG    . SER B 1 520 ? 117.333 163.644 155.336 1.00 26.70 ?  520 SER B OG    1 
ATOM   9725  N  N     . THR B 1 521 ? 114.108 161.914 155.982 1.00 24.19 ?  521 THR B N     1 
ATOM   9726  C  CA    . THR B 1 521 ? 113.305 161.932 157.197 1.00 24.61 ?  521 THR B CA    1 
ATOM   9727  C  C     . THR B 1 521 ? 114.062 162.530 158.373 1.00 28.11 ?  521 THR B C     1 
ATOM   9728  O  O     . THR B 1 521 ? 113.432 162.961 159.345 1.00 32.01 ?  521 THR B O     1 
ATOM   9729  C  CB    . THR B 1 521 ? 112.836 160.520 157.541 1.00 28.66 ?  521 THR B CB    1 
ATOM   9730  O  OG1   . THR B 1 521 ? 113.963 159.720 157.919 1.00 30.86 ?  521 THR B OG1   1 
ATOM   9731  C  CG2   . THR B 1 521 ? 112.156 159.886 156.345 1.00 19.23 ?  521 THR B CG2   1 
ATOM   9732  N  N     . TYR B 1 522 ? 115.394 162.553 158.312 1.00 27.68 ?  522 TYR B N     1 
ATOM   9733  C  CA    . TYR B 1 522 ? 116.167 163.275 159.316 1.00 19.35 ?  522 TYR B CA    1 
ATOM   9734  C  C     . TYR B 1 522 ? 115.867 164.766 159.268 1.00 26.13 ?  522 TYR B C     1 
ATOM   9735  O  O     . TYR B 1 522 ? 115.725 165.415 160.310 1.00 31.32 ?  522 TYR B O     1 
ATOM   9736  C  CB    . TYR B 1 522 ? 117.659 163.034 159.106 1.00 21.34 ?  522 TYR B CB    1 
ATOM   9737  C  CG    . TYR B 1 522 ? 118.080 161.589 159.185 1.00 21.56 ?  522 TYR B CG    1 
ATOM   9738  C  CD1   . TYR B 1 522 ? 117.988 160.885 160.374 1.00 20.11 ?  522 TYR B CD1   1 
ATOM   9739  C  CD2   . TYR B 1 522 ? 118.597 160.937 158.074 1.00 22.80 ?  522 TYR B CD2   1 
ATOM   9740  C  CE1   . TYR B 1 522 ? 118.388 159.570 160.455 1.00 24.06 ?  522 TYR B CE1   1 
ATOM   9741  C  CE2   . TYR B 1 522 ? 118.995 159.621 158.145 1.00 19.98 ?  522 TYR B CE2   1 
ATOM   9742  C  CZ    . TYR B 1 522 ? 118.886 158.942 159.338 1.00 25.74 ?  522 TYR B CZ    1 
ATOM   9743  O  OH    . TYR B 1 522 ? 119.282 157.630 159.413 1.00 29.11 ?  522 TYR B OH    1 
ATOM   9744  N  N     . ALA B 1 523 ? 115.781 165.328 158.060 1.00 33.00 ?  523 ALA B N     1 
ATOM   9745  C  CA    . ALA B 1 523 ? 115.524 166.756 157.916 1.00 26.34 ?  523 ALA B CA    1 
ATOM   9746  C  C     . ALA B 1 523 ? 114.119 167.117 158.379 1.00 30.52 ?  523 ALA B C     1 
ATOM   9747  O  O     . ALA B 1 523 ? 113.920 168.148 159.030 1.00 34.10 ?  523 ALA B O     1 
ATOM   9748  C  CB    . ALA B 1 523 ? 115.737 167.180 156.465 1.00 24.96 ?  523 ALA B CB    1 
ATOM   9749  N  N     . THR B 1 524 ? 113.132 166.283 158.052 1.00 30.85 ?  524 THR B N     1 
ATOM   9750  C  CA    . THR B 1 524 ? 111.752 166.557 158.427 1.00 26.94 ?  524 THR B CA    1 
ATOM   9751  C  C     . THR B 1 524 ? 111.426 166.136 159.852 1.00 34.75 ?  524 THR B C     1 
ATOM   9752  O  O     . THR B 1 524 ? 110.350 166.484 160.350 1.00 41.72 ?  524 THR B O     1 
ATOM   9753  C  CB    . THR B 1 524 ? 110.794 165.859 157.460 1.00 33.13 ?  524 THR B CB    1 
ATOM   9754  O  OG1   . THR B 1 524 ? 110.690 164.472 157.805 1.00 35.03 ?  524 THR B OG1   1 
ATOM   9755  C  CG2   . THR B 1 524 ? 111.299 165.980 156.034 1.00 32.61 ?  524 THR B CG2   1 
ATOM   9756  N  N     . GLY B 1 525 ? 112.316 165.405 160.518 1.00 29.82 ?  525 GLY B N     1 
ATOM   9757  C  CA    . GLY B 1 525 ? 112.073 164.948 161.868 1.00 27.05 ?  525 GLY B CA    1 
ATOM   9758  C  C     . GLY B 1 525 ? 111.218 163.707 161.980 1.00 33.85 ?  525 GLY B C     1 
ATOM   9759  O  O     . GLY B 1 525 ? 110.998 163.227 163.099 1.00 32.98 ?  525 GLY B O     1 
ATOM   9760  N  N     . GLU B 1 526 ? 110.729 163.171 160.860 1.00 37.62 ?  526 GLU B N     1 
ATOM   9761  C  CA    . GLU B 1 526 ? 109.921 161.958 160.898 1.00 35.57 ?  526 GLU B CA    1 
ATOM   9762  C  C     . GLU B 1 526 ? 110.726 160.757 161.375 1.00 35.56 ?  526 GLU B C     1 
ATOM   9763  O  O     . GLU B 1 526 ? 110.148 159.808 161.916 1.00 41.96 ?  526 GLU B O     1 
ATOM   9764  C  CB    . GLU B 1 526 ? 109.322 161.705 159.509 1.00 36.25 ?  526 GLU B CB    1 
ATOM   9765  C  CG    . GLU B 1 526 ? 108.664 160.351 159.317 1.00 36.93 ?  526 GLU B CG    1 
ATOM   9766  C  CD    . GLU B 1 526 ? 108.652 159.912 157.867 1.00 44.72 ?  526 GLU B CD    1 
ATOM   9767  O  OE1   . GLU B 1 526 ? 108.638 160.792 156.981 1.00 43.21 ?  526 GLU B OE1   1 
ATOM   9768  O  OE2   . GLU B 1 526 ? 108.659 158.690 157.613 1.00 42.49 -1 526 GLU B OE2   1 
ATOM   9769  N  N     . TYR B 1 527 ? 112.049 160.792 161.212 1.00 35.15 ?  527 TYR B N     1 
ATOM   9770  C  CA    . TYR B 1 527 ? 112.891 159.698 161.685 1.00 25.96 ?  527 TYR B CA    1 
ATOM   9771  C  C     . TYR B 1 527 ? 112.817 159.556 163.201 1.00 28.26 ?  527 TYR B C     1 
ATOM   9772  O  O     . TYR B 1 527 ? 112.795 158.439 163.728 1.00 35.04 ?  527 TYR B O     1 
ATOM   9773  C  CB    . TYR B 1 527 ? 114.335 159.925 161.239 1.00 23.59 ?  527 TYR B CB    1 
ATOM   9774  C  CG    . TYR B 1 527 ? 115.286 158.830 161.654 1.00 28.20 ?  527 TYR B CG    1 
ATOM   9775  C  CD1   . TYR B 1 527 ? 115.501 157.727 160.842 1.00 23.69 ?  527 TYR B CD1   1 
ATOM   9776  C  CD2   . TYR B 1 527 ? 115.970 158.897 162.861 1.00 28.68 ?  527 TYR B CD2   1 
ATOM   9777  C  CE1   . TYR B 1 527 ? 116.367 156.726 161.217 1.00 23.79 ?  527 TYR B CE1   1 
ATOM   9778  C  CE2   . TYR B 1 527 ? 116.836 157.899 163.244 1.00 24.28 ?  527 TYR B CE2   1 
ATOM   9779  C  CZ    . TYR B 1 527 ? 117.031 156.816 162.419 1.00 23.27 ?  527 TYR B CZ    1 
ATOM   9780  O  OH    . TYR B 1 527 ? 117.896 155.818 162.797 1.00 32.61 ?  527 TYR B OH    1 
ATOM   9781  N  N     . PHE B 1 528 ? 112.780 160.677 163.915 1.00 32.99 ?  528 PHE B N     1 
ATOM   9782  C  CA    . PHE B 1 528 ? 112.894 160.691 165.367 1.00 27.64 ?  528 PHE B CA    1 
ATOM   9783  C  C     . PHE B 1 528 ? 111.562 160.489 166.079 1.00 36.60 ?  528 PHE B C     1 
ATOM   9784  O  O     . PHE B 1 528 ? 111.513 160.612 167.305 1.00 46.33 ?  528 PHE B O     1 
ATOM   9785  C  CB    . PHE B 1 528 ? 113.521 162.009 165.828 1.00 30.83 ?  528 PHE B CB    1 
ATOM   9786  C  CG    . PHE B 1 528 ? 114.885 162.265 165.261 1.00 33.47 ?  528 PHE B CG    1 
ATOM   9787  C  CD1   . PHE B 1 528 ? 116.016 161.800 165.908 1.00 24.97 ?  528 PHE B CD1   1 
ATOM   9788  C  CD2   . PHE B 1 528 ? 115.039 162.979 164.085 1.00 34.19 ?  528 PHE B CD2   1 
ATOM   9789  C  CE1   . PHE B 1 528 ? 117.272 162.037 165.389 1.00 28.35 ?  528 PHE B CE1   1 
ATOM   9790  C  CE2   . PHE B 1 528 ? 116.293 163.217 163.563 1.00 33.73 ?  528 PHE B CE2   1 
ATOM   9791  C  CZ    . PHE B 1 528 ? 117.411 162.745 164.218 1.00 31.75 ?  528 PHE B CZ    1 
ATOM   9792  N  N     . ASP B 1 529 ? 110.488 160.184 165.346 1.00 37.70 ?  529 ASP B N     1 
ATOM   9793  C  CA    . ASP B 1 529 ? 109.165 160.110 165.960 1.00 35.02 ?  529 ASP B CA    1 
ATOM   9794  C  C     . ASP B 1 529 ? 109.107 159.034 167.038 1.00 38.65 ?  529 ASP B C     1 
ATOM   9795  O  O     . ASP B 1 529 ? 108.698 159.296 168.176 1.00 42.72 ?  529 ASP B O     1 
ATOM   9796  C  CB    . ASP B 1 529 ? 108.110 159.851 164.887 1.00 32.50 ?  529 ASP B CB    1 
ATOM   9797  C  CG    . ASP B 1 529 ? 107.959 161.011 163.927 1.00 43.06 ?  529 ASP B CG    1 
ATOM   9798  O  OD1   . ASP B 1 529 ? 108.456 162.114 164.239 1.00 42.20 ?  529 ASP B OD1   1 
ATOM   9799  O  OD2   . ASP B 1 529 ? 107.343 160.819 162.857 1.00 48.54 -1 529 ASP B OD2   1 
ATOM   9800  N  N     . LYS B 1 530 ? 109.524 157.813 166.698 1.00 39.76 ?  530 LYS B N     1 
ATOM   9801  C  CA    . LYS B 1 530 ? 109.492 156.724 167.666 1.00 35.45 ?  530 LYS B CA    1 
ATOM   9802  C  C     . LYS B 1 530 ? 110.488 156.926 168.797 1.00 38.94 ?  530 LYS B C     1 
ATOM   9803  O  O     . LYS B 1 530 ? 110.343 156.304 169.852 1.00 43.21 ?  530 LYS B O     1 
ATOM   9804  C  CB    . LYS B 1 530 ? 109.761 155.392 166.968 1.00 37.18 ?  530 LYS B CB    1 
ATOM   9805  C  CG    . LYS B 1 530 ? 111.213 154.960 166.994 1.00 32.74 ?  530 LYS B CG    1 
ATOM   9806  C  CD    . LYS B 1 530 ? 111.407 153.682 166.211 1.00 38.19 ?  530 LYS B CD    1 
ATOM   9807  C  CE    . LYS B 1 530 ? 112.818 153.163 166.350 1.00 34.66 ?  530 LYS B CE    1 
ATOM   9808  N  NZ    . LYS B 1 530 ? 113.344 152.743 165.028 1.00 43.09 1  530 LYS B NZ    1 
ATOM   9809  N  N     . TYR B 1 531 ? 111.493 157.775 168.603 1.00 39.67 ?  531 TYR B N     1 
ATOM   9810  C  CA    . TYR B 1 531 ? 112.472 158.033 169.646 1.00 32.48 ?  531 TYR B CA    1 
ATOM   9811  C  C     . TYR B 1 531 ? 112.048 159.159 170.575 1.00 31.41 ?  531 TYR B C     1 
ATOM   9812  O  O     . TYR B 1 531 ? 112.373 159.124 171.767 1.00 40.60 ?  531 TYR B O     1 
ATOM   9813  C  CB    . TYR B 1 531 ? 113.827 158.358 169.021 1.00 27.04 ?  531 TYR B CB    1 
ATOM   9814  C  CG    . TYR B 1 531 ? 114.541 157.151 168.462 1.00 32.01 ?  531 TYR B CG    1 
ATOM   9815  C  CD1   . TYR B 1 531 ? 114.885 156.086 169.281 1.00 26.09 ?  531 TYR B CD1   1 
ATOM   9816  C  CD2   . TYR B 1 531 ? 114.872 157.076 167.117 1.00 28.89 ?  531 TYR B CD2   1 
ATOM   9817  C  CE1   . TYR B 1 531 ? 115.539 154.983 168.778 1.00 31.55 ?  531 TYR B CE1   1 
ATOM   9818  C  CE2   . TYR B 1 531 ? 115.526 155.978 166.605 1.00 25.44 ?  531 TYR B CE2   1 
ATOM   9819  C  CZ    . TYR B 1 531 ? 115.857 154.934 167.440 1.00 31.42 ?  531 TYR B CZ    1 
ATOM   9820  O  OH    . TYR B 1 531 ? 116.510 153.834 166.938 1.00 30.43 ?  531 TYR B OH    1 
ATOM   9821  N  N     . VAL B 1 532 ? 111.332 160.159 170.054 1.00 38.40 ?  532 VAL B N     1 
ATOM   9822  C  CA    . VAL B 1 532 ? 110.774 161.208 170.902 1.00 34.75 ?  532 VAL B CA    1 
ATOM   9823  C  C     . VAL B 1 532 ? 109.428 160.824 171.490 1.00 39.86 ?  532 VAL B C     1 
ATOM   9824  O  O     . VAL B 1 532 ? 108.892 161.567 172.321 1.00 47.83 ?  532 VAL B O     1 
ATOM   9825  C  CB    . VAL B 1 532 ? 110.615 162.533 170.131 1.00 40.64 ?  532 VAL B CB    1 
ATOM   9826  C  CG1   . VAL B 1 532 ? 111.937 162.952 169.512 1.00 37.44 ?  532 VAL B CG1   1 
ATOM   9827  C  CG2   . VAL B 1 532 ? 109.534 162.404 169.070 1.00 37.46 ?  532 VAL B CG2   1 
ATOM   9828  N  N     . SER B 1 533 ? 108.861 159.690 171.079 1.00 40.67 ?  533 SER B N     1 
ATOM   9829  C  CA    . SER B 1 533 ? 107.593 159.223 171.625 1.00 40.28 ?  533 SER B CA    1 
ATOM   9830  C  C     . SER B 1 533 ? 107.721 158.012 172.535 1.00 41.24 ?  533 SER B C     1 
ATOM   9831  O  O     . SER B 1 533 ? 106.949 157.889 173.486 1.00 46.20 ?  533 SER B O     1 
ATOM   9832  C  CB    . SER B 1 533 ? 106.618 158.883 170.491 1.00 45.12 ?  533 SER B CB    1 
ATOM   9833  O  OG    . SER B 1 533 ? 106.866 157.585 169.981 1.00 46.69 ?  533 SER B OG    1 
ATOM   9834  N  N     . THR B 1 534 ? 108.672 157.120 172.272 1.00 46.10 ?  534 THR B N     1 
ATOM   9835  C  CA    . THR B 1 534 ? 108.831 155.887 173.029 1.00 41.87 ?  534 THR B CA    1 
ATOM   9836  C  C     . THR B 1 534 ? 110.140 155.919 173.804 1.00 41.15 ?  534 THR B C     1 
ATOM   9837  O  O     . THR B 1 534 ? 111.152 156.429 173.312 1.00 49.01 ?  534 THR B O     1 
ATOM   9838  C  CB    . THR B 1 534 ? 108.804 154.662 172.104 1.00 42.71 ?  534 THR B CB    1 
ATOM   9839  O  OG1   . THR B 1 534 ? 107.678 154.750 171.224 1.00 42.40 ?  534 THR B OG1   1 
ATOM   9840  C  CG2   . THR B 1 534 ? 108.709 153.376 172.911 1.00 43.68 ?  534 THR B CG2   1 
ATOM   9841  N  N     . ASP B 1 535 ? 110.114 155.376 175.016 1.00 43.04 ?  535 ASP B N     1 
ATOM   9842  C  CA    . ASP B 1 535 ? 111.299 155.255 175.853 1.00 42.66 ?  535 ASP B CA    1 
ATOM   9843  C  C     . ASP B 1 535 ? 111.928 153.886 175.632 1.00 45.35 ?  535 ASP B C     1 
ATOM   9844  O  O     . ASP B 1 535 ? 111.235 152.864 175.684 1.00 47.18 ?  535 ASP B O     1 
ATOM   9845  C  CB    . ASP B 1 535 ? 110.946 155.445 177.329 1.00 41.53 ?  535 ASP B CB    1 
ATOM   9846  C  CG    . ASP B 1 535 ? 112.172 155.556 178.211 1.00 47.31 ?  535 ASP B CG    1 
ATOM   9847  O  OD1   . ASP B 1 535 ? 112.935 156.532 178.050 1.00 48.84 ?  535 ASP B OD1   1 
ATOM   9848  O  OD2   . ASP B 1 535 ? 112.371 154.669 179.065 1.00 47.75 -1 535 ASP B OD2   1 
ATOM   9849  N  N     . PHE B 1 536 ? 113.238 153.869 175.386 1.00 40.14 ?  536 PHE B N     1 
ATOM   9850  C  CA    . PHE B 1 536 ? 113.958 152.639 175.087 1.00 34.91 ?  536 PHE B CA    1 
ATOM   9851  C  C     . PHE B 1 536 ? 114.918 152.242 176.204 1.00 35.66 ?  536 PHE B C     1 
ATOM   9852  O  O     . PHE B 1 536 ? 115.890 151.522 175.955 1.00 43.03 ?  536 PHE B O     1 
ATOM   9853  C  CB    . PHE B 1 536 ? 114.705 152.775 173.761 1.00 34.94 ?  536 PHE B CB    1 
ATOM   9854  C  CG    . PHE B 1 536 ? 113.804 152.846 172.562 1.00 31.98 ?  536 PHE B CG    1 
ATOM   9855  C  CD1   . PHE B 1 536 ? 113.398 151.693 171.915 1.00 32.97 ?  536 PHE B CD1   1 
ATOM   9856  C  CD2   . PHE B 1 536 ? 113.360 154.065 172.085 1.00 32.10 ?  536 PHE B CD2   1 
ATOM   9857  C  CE1   . PHE B 1 536 ? 112.569 151.754 170.814 1.00 31.04 ?  536 PHE B CE1   1 
ATOM   9858  C  CE2   . PHE B 1 536 ? 112.530 154.131 170.983 1.00 39.85 ?  536 PHE B CE2   1 
ATOM   9859  C  CZ    . PHE B 1 536 ? 112.135 152.973 170.348 1.00 30.69 ?  536 PHE B CZ    1 
ATOM   9860  N  N     . SER B 1 537 ? 114.669 152.704 177.426 1.00 36.35 ?  537 SER B N     1 
ATOM   9861  C  CA    . SER B 1 537 ? 115.427 152.245 178.574 1.00 34.06 ?  537 SER B CA    1 
ATOM   9862  C  C     . SER B 1 537 ? 115.076 150.791 178.879 1.00 38.38 ?  537 SER B C     1 
ATOM   9863  O  O     . SER B 1 537 ? 113.996 150.317 178.518 1.00 41.45 ?  537 SER B O     1 
ATOM   9864  C  CB    . SER B 1 537 ? 115.139 153.129 179.785 1.00 34.61 ?  537 SER B CB    1 
ATOM   9865  O  OG    . SER B 1 537 ? 113.775 153.056 180.155 1.00 39.68 ?  537 SER B OG    1 
ATOM   9866  N  N     . PRO B 1 538 ? 115.981 150.054 179.523 1.00 37.30 ?  538 PRO B N     1 
ATOM   9867  C  CA    . PRO B 1 538 ? 115.700 148.643 179.813 1.00 35.39 ?  538 PRO B CA    1 
ATOM   9868  C  C     . PRO B 1 538 ? 114.489 148.486 180.719 1.00 40.61 ?  538 PRO B C     1 
ATOM   9869  O  O     . PRO B 1 538 ? 114.261 149.282 181.631 1.00 39.18 ?  538 PRO B O     1 
ATOM   9870  C  CB    . PRO B 1 538 ? 116.984 148.158 180.499 1.00 35.57 ?  538 PRO B CB    1 
ATOM   9871  C  CG    . PRO B 1 538 ? 118.027 149.149 180.125 1.00 34.04 ?  538 PRO B CG    1 
ATOM   9872  C  CD    . PRO B 1 538 ? 117.313 150.454 180.005 1.00 36.00 ?  538 PRO B CD    1 
ATOM   9873  N  N     . LYS B 1 539 ? 113.706 147.442 180.453 1.00 45.36 ?  539 LYS B N     1 
ATOM   9874  C  CA    . LYS B 1 539 ? 112.531 147.120 181.249 1.00 45.52 ?  539 LYS B CA    1 
ATOM   9875  C  C     . LYS B 1 539 ? 112.817 146.091 182.333 1.00 47.99 ?  539 LYS B C     1 
ATOM   9876  O  O     . LYS B 1 539 ? 111.908 145.740 183.091 1.00 48.24 ?  539 LYS B O     1 
ATOM   9877  C  CB    . LYS B 1 539 ? 111.402 146.613 180.346 1.00 45.74 ?  539 LYS B CB    1 
ATOM   9878  C  CG    . LYS B 1 539 ? 111.414 147.196 178.944 1.00 43.95 ?  539 LYS B CG    1 
ATOM   9879  C  CD    . LYS B 1 539 ? 110.903 148.628 178.932 1.00 48.13 ?  539 LYS B CD    1 
ATOM   9880  C  CE    . LYS B 1 539 ? 110.127 148.924 177.658 1.00 49.03 ?  539 LYS B CE    1 
ATOM   9881  N  NZ    . LYS B 1 539 ? 111.005 148.927 176.456 1.00 49.69 1  539 LYS B NZ    1 
ATOM   9882  N  N     . TYR B 1 540 ? 114.050 145.604 182.424 1.00 45.89 ?  540 TYR B N     1 
ATOM   9883  C  CA    . TYR B 1 540 ? 114.436 144.600 183.401 1.00 43.91 ?  540 TYR B CA    1 
ATOM   9884  C  C     . TYR B 1 540 ? 115.537 145.153 184.291 1.00 46.08 ?  540 TYR B C     1 
ATOM   9885  O  O     . TYR B 1 540 ? 116.445 145.843 183.817 1.00 47.79 ?  540 TYR B O     1 
ATOM   9886  C  CB    . TYR B 1 540 ? 114.906 143.314 182.715 1.00 44.43 ?  540 TYR B CB    1 
ATOM   9887  C  CG    . TYR B 1 540 ? 113.812 142.595 181.960 1.00 47.68 ?  540 TYR B CG    1 
ATOM   9888  C  CD1   . TYR B 1 540 ? 113.522 142.918 180.642 1.00 44.57 ?  540 TYR B CD1   1 
ATOM   9889  C  CD2   . TYR B 1 540 ? 113.065 141.597 182.569 1.00 48.48 ?  540 TYR B CD2   1 
ATOM   9890  C  CE1   . TYR B 1 540 ? 112.522 142.266 179.951 1.00 43.43 ?  540 TYR B CE1   1 
ATOM   9891  C  CE2   . TYR B 1 540 ? 112.062 140.939 181.885 1.00 45.36 ?  540 TYR B CE2   1 
ATOM   9892  C  CZ    . TYR B 1 540 ? 111.795 141.277 180.577 1.00 44.75 ?  540 TYR B CZ    1 
ATOM   9893  O  OH    . TYR B 1 540 ? 110.797 140.625 179.894 1.00 49.48 ?  540 TYR B OH    1 
ATOM   9894  N  N     . GLU B 1 541 ? 115.446 144.851 185.589 1.00 49.92 ?  541 GLU B N     1 
ATOM   9895  C  CA    . GLU B 1 541 ? 116.433 145.354 186.540 1.00 45.77 ?  541 GLU B CA    1 
ATOM   9896  C  C     . GLU B 1 541 ? 117.822 144.807 186.237 1.00 46.72 ?  541 GLU B C     1 
ATOM   9897  O  O     . GLU B 1 541 ? 118.822 145.519 186.386 1.00 46.88 ?  541 GLU B O     1 
ATOM   9898  C  CB    . GLU B 1 541 ? 116.013 145.001 187.966 1.00 46.79 ?  541 GLU B CB    1 
ATOM   9899  C  CG    . GLU B 1 541 ? 116.861 145.655 189.044 1.00 48.67 ?  541 GLU B CG    1 
ATOM   9900  C  CD    . GLU B 1 541 ? 117.680 144.650 189.830 1.00 53.09 ?  541 GLU B CD    1 
ATOM   9901  O  OE1   . GLU B 1 541 ? 117.462 143.433 189.648 1.00 50.43 ?  541 GLU B OE1   1 
ATOM   9902  O  OE2   . GLU B 1 541 ? 118.540 145.076 190.628 1.00 53.20 -1 541 GLU B OE2   1 
ATOM   9903  N  N     . LYS B 1 542 ? 117.905 143.540 185.823 1.00 43.44 ?  542 LYS B N     1 
ATOM   9904  C  CA    . LYS B 1 542 ? 119.199 142.961 185.474 1.00 39.82 ?  542 LYS B CA    1 
ATOM   9905  C  C     . LYS B 1 542 ? 119.824 143.679 184.286 1.00 44.78 ?  542 LYS B C     1 
ATOM   9906  O  O     . LYS B 1 542 ? 121.027 143.966 184.286 1.00 42.69 ?  542 LYS B O     1 
ATOM   9907  C  CB    . LYS B 1 542 ? 119.042 141.470 185.175 1.00 41.29 ?  542 LYS B CB    1 
ATOM   9908  C  CG    . LYS B 1 542 ? 120.313 140.801 184.684 1.00 43.38 ?  542 LYS B CG    1 
ATOM   9909  C  CD    . LYS B 1 542 ? 120.144 139.297 184.571 1.00 41.03 ?  542 LYS B CD    1 
ATOM   9910  C  CE    . LYS B 1 542 ? 121.468 138.618 184.263 1.00 44.05 ?  542 LYS B CE    1 
ATOM   9911  N  NZ    . LYS B 1 542 ? 121.372 137.139 184.375 1.00 44.68 1  542 LYS B NZ    1 
ATOM   9912  N  N     . ILE B 1 543 ? 119.023 143.979 183.261 1.00 43.71 ?  543 ILE B N     1 
ATOM   9913  C  CA    . ILE B 1 543 ? 119.543 144.686 182.095 1.00 37.51 ?  543 ILE B CA    1 
ATOM   9914  C  C     . ILE B 1 543 ? 119.891 146.125 182.452 1.00 37.39 ?  543 ILE B C     1 
ATOM   9915  O  O     . ILE B 1 543 ? 120.912 146.659 182.004 1.00 37.90 ?  543 ILE B O     1 
ATOM   9916  C  CB    . ILE B 1 543 ? 118.534 144.616 180.936 1.00 36.35 ?  543 ILE B CB    1 
ATOM   9917  C  CG1   . ILE B 1 543 ? 118.164 143.164 180.632 1.00 39.05 ?  543 ILE B CG1   1 
ATOM   9918  C  CG2   . ILE B 1 543 ? 119.102 145.288 179.704 1.00 36.17 ?  543 ILE B CG2   1 
ATOM   9919  C  CD1   . ILE B 1 543 ? 119.355 142.250 180.463 1.00 33.21 ?  543 ILE B CD1   1 
ATOM   9920  N  N     . ALA B 1 544 ? 119.050 146.778 183.259 1.00 35.49 ?  544 ALA B N     1 
ATOM   9921  C  CA    . ALA B 1 544 ? 119.341 148.145 183.676 1.00 39.29 ?  544 ALA B CA    1 
ATOM   9922  C  C     . ALA B 1 544 ? 120.616 148.218 184.504 1.00 44.33 ?  544 ALA B C     1 
ATOM   9923  O  O     . ALA B 1 544 ? 121.287 149.256 184.518 1.00 48.55 ?  544 ALA B O     1 
ATOM   9924  C  CB    . ALA B 1 544 ? 118.163 148.717 184.462 1.00 40.47 ?  544 ALA B CB    1 
ATOM   9925  N  N     . ASN B 1 545 ? 120.965 147.133 185.198 1.00 45.04 ?  545 ASN B N     1 
ATOM   9926  C  CA    . ASN B 1 545 ? 122.221 147.103 185.938 1.00 45.81 ?  545 ASN B CA    1 
ATOM   9927  C  C     . ASN B 1 545 ? 123.416 146.957 185.007 1.00 44.60 ?  545 ASN B C     1 
ATOM   9928  O  O     . ASN B 1 545 ? 124.526 147.374 185.357 1.00 46.40 ?  545 ASN B O     1 
ATOM   9929  C  CB    . ASN B 1 545 ? 122.204 145.967 186.961 1.00 47.28 ?  545 ASN B CB    1 
ATOM   9930  C  CG    . ASN B 1 545 ? 121.363 146.293 188.178 1.00 49.62 ?  545 ASN B CG    1 
ATOM   9931  O  OD1   . ASN B 1 545 ? 121.197 147.458 188.537 1.00 48.80 ?  545 ASN B OD1   1 
ATOM   9932  N  ND2   . ASN B 1 545 ? 120.829 145.262 188.822 1.00 44.89 ?  545 ASN B ND2   1 
ATOM   9933  N  N     . LEU B 1 546 ? 123.215 146.364 183.828 1.00 44.21 ?  546 LEU B N     1 
ATOM   9934  C  CA    . LEU B 1 546 ? 124.306 146.233 182.869 1.00 37.40 ?  546 LEU B CA    1 
ATOM   9935  C  C     . LEU B 1 546 ? 124.773 147.590 182.364 1.00 37.79 ?  546 LEU B C     1 
ATOM   9936  O  O     . LEU B 1 546 ? 125.947 147.753 182.017 1.00 39.54 ?  546 LEU B O     1 
ATOM   9937  C  CB    . LEU B 1 546 ? 123.873 145.355 181.695 1.00 36.36 ?  546 LEU B CB    1 
ATOM   9938  C  CG    . LEU B 1 546 ? 123.476 143.913 182.011 1.00 38.55 ?  546 LEU B CG    1 
ATOM   9939  C  CD1   . LEU B 1 546 ? 122.982 143.215 180.756 1.00 37.37 ?  546 LEU B CD1   1 
ATOM   9940  C  CD2   . LEU B 1 546 ? 124.639 143.155 182.624 1.00 37.55 ?  546 LEU B CD2   1 
ATOM   9941  N  N     . PHE B 1 547 ? 123.877 148.575 182.329 1.00 39.72 ?  547 PHE B N     1 
ATOM   9942  C  CA    . PHE B 1 547 ? 124.189 149.911 181.840 1.00 38.97 ?  547 PHE B CA    1 
ATOM   9943  C  C     . PHE B 1 547 ? 124.532 150.876 182.966 1.00 40.70 ?  547 PHE B C     1 
ATOM   9944  O  O     . PHE B 1 547 ? 124.478 152.094 182.767 1.00 44.69 ?  547 PHE B O     1 
ATOM   9945  C  CB    . PHE B 1 547 ? 123.021 150.457 181.016 1.00 37.62 ?  547 PHE B CB    1 
ATOM   9946  C  CG    . PHE B 1 547 ? 122.799 149.732 179.720 1.00 39.12 ?  547 PHE B CG    1 
ATOM   9947  C  CD1   . PHE B 1 547 ? 121.975 148.622 179.664 1.00 37.61 ?  547 PHE B CD1   1 
ATOM   9948  C  CD2   . PHE B 1 547 ? 123.410 150.163 178.556 1.00 38.44 ?  547 PHE B CD2   1 
ATOM   9949  C  CE1   . PHE B 1 547 ? 121.768 147.955 178.472 1.00 38.08 ?  547 PHE B CE1   1 
ATOM   9950  C  CE2   . PHE B 1 547 ? 123.206 149.501 177.363 1.00 33.49 ?  547 PHE B CE2   1 
ATOM   9951  C  CZ    . PHE B 1 547 ? 122.384 148.397 177.321 1.00 35.40 ?  547 PHE B CZ    1 
ATOM   9952  N  N     . GLU B 1 548 ? 124.871 150.359 184.145 1.00 47.33 ?  548 GLU B N     1 
ATOM   9953  C  CA    . GLU B 1 548 ? 125.228 151.216 185.266 1.00 48.82 ?  548 GLU B CA    1 
ATOM   9954  C  C     . GLU B 1 548 ? 126.483 152.017 184.943 1.00 52.47 ?  548 GLU B C     1 
ATOM   9955  O  O     . GLU B 1 548 ? 127.422 151.511 184.324 1.00 52.34 ?  548 GLU B O     1 
ATOM   9956  C  CB    . GLU B 1 548 ? 125.447 150.378 186.525 1.00 47.67 ?  548 GLU B CB    1 
ATOM   9957  C  CG    . GLU B 1 548 ? 124.206 150.207 187.384 1.00 50.67 ?  548 GLU B CG    1 
ATOM   9958  C  CD    . GLU B 1 548 ? 124.375 149.131 188.440 1.00 56.24 ?  548 GLU B CD    1 
ATOM   9959  O  OE1   . GLU B 1 548 ? 125.249 148.257 188.264 1.00 55.02 ?  548 GLU B OE1   1 
ATOM   9960  O  OE2   . GLU B 1 548 ? 123.636 149.162 189.447 1.00 55.23 -1 548 GLU B OE2   1 
ATOM   9961  N  N     . GLY B 1 549 ? 126.493 153.278 185.365 1.00 50.26 ?  549 GLY B N     1 
ATOM   9962  C  CA    . GLY B 1 549 ? 127.587 154.167 185.034 1.00 49.92 ?  549 GLY B CA    1 
ATOM   9963  C  C     . GLY B 1 549 ? 127.571 154.679 183.615 1.00 51.73 ?  549 GLY B C     1 
ATOM   9964  O  O     . GLY B 1 549 ? 128.584 155.218 183.155 1.00 54.70 ?  549 GLY B O     1 
ATOM   9965  N  N     . MET B 1 550 ? 126.457 154.525 182.906 1.00 48.89 ?  550 MET B N     1 
ATOM   9966  C  CA    . MET B 1 550 ? 126.344 154.924 181.511 1.00 44.47 ?  550 MET B CA    1 
ATOM   9967  C  C     . MET B 1 550 ? 124.990 155.577 181.298 1.00 46.73 ?  550 MET B C     1 
ATOM   9968  O  O     . MET B 1 550 ? 123.958 154.985 181.621 1.00 52.25 ?  550 MET B O     1 
ATOM   9969  C  CB    . MET B 1 550 ? 126.508 153.716 180.586 1.00 44.64 ?  550 MET B CB    1 
ATOM   9970  C  CG    . MET B 1 550 ? 127.231 154.013 179.292 1.00 51.54 ?  550 MET B CG    1 
ATOM   9971  S  SD    . MET B 1 550 ? 127.324 152.564 178.229 1.00 60.33 ?  550 MET B SD    1 
ATOM   9972  C  CE    . MET B 1 550 ? 127.274 151.240 179.432 1.00 48.02 ?  550 MET B CE    1 
ATOM   9973  N  N     . HIS B 1 551 ? 124.994 156.792 180.756 1.00 42.96 ?  551 HIS B N     1 
ATOM   9974  C  CA    . HIS B 1 551 ? 123.755 157.529 180.553 1.00 43.58 ?  551 HIS B CA    1 
ATOM   9975  C  C     . HIS B 1 551 ? 123.012 156.969 179.346 1.00 46.12 ?  551 HIS B C     1 
ATOM   9976  O  O     . HIS B 1 551 ? 123.499 157.050 178.214 1.00 44.91 ?  551 HIS B O     1 
ATOM   9977  C  CB    . HIS B 1 551 ? 124.035 159.017 180.362 1.00 41.99 ?  551 HIS B CB    1 
ATOM   9978  C  CG    . HIS B 1 551 ? 122.834 159.802 179.937 1.00 46.24 ?  551 HIS B CG    1 
ATOM   9979  N  ND1   . HIS B 1 551 ? 121.873 160.229 180.827 1.00 49.73 ?  551 HIS B ND1   1 
ATOM   9980  C  CD2   . HIS B 1 551 ? 122.436 160.232 178.717 1.00 46.93 ?  551 HIS B CD2   1 
ATOM   9981  C  CE1   . HIS B 1 551 ? 120.934 160.890 180.172 1.00 47.40 ?  551 HIS B CE1   1 
ATOM   9982  N  NE2   . HIS B 1 551 ? 121.253 160.907 178.891 1.00 46.40 ?  551 HIS B NE2   1 
ATOM   9983  N  N     . ILE B 1 552 ? 121.837 156.402 179.591 1.00 40.04 ?  552 ILE B N     1 
ATOM   9984  C  CA    . ILE B 1 552 ? 120.975 155.891 178.532 1.00 37.77 ?  552 ILE B CA    1 
ATOM   9985  C  C     . ILE B 1 552 ? 120.155 157.062 177.992 1.00 38.12 ?  552 ILE B C     1 
ATOM   9986  O  O     . ILE B 1 552 ? 119.468 157.730 178.781 1.00 37.71 ?  552 ILE B O     1 
ATOM   9987  C  CB    . ILE B 1 552 ? 120.064 154.771 179.044 1.00 36.38 ?  552 ILE B CB    1 
ATOM   9988  C  CG1   . ILE B 1 552 ? 120.907 153.613 179.578 1.00 35.67 ?  552 ILE B CG1   1 
ATOM   9989  C  CG2   . ILE B 1 552 ? 119.130 154.294 177.946 1.00 36.34 ?  552 ILE B CG2   1 
ATOM   9990  C  CD1   . ILE B 1 552 ? 120.127 152.622 180.396 1.00 38.89 ?  552 ILE B CD1   1 
ATOM   9991  N  N     . PRO B 1 553 ? 120.214 157.352 176.693 1.00 40.67 ?  553 PRO B N     1 
ATOM   9992  C  CA    . PRO B 1 553 ? 119.458 158.491 176.158 1.00 37.77 ?  553 PRO B CA    1 
ATOM   9993  C  C     . PRO B 1 553 ? 117.967 158.348 176.419 1.00 40.06 ?  553 PRO B C     1 
ATOM   9994  O  O     . PRO B 1 553 ? 117.388 157.272 176.264 1.00 41.00 ?  553 PRO B O     1 
ATOM   9995  C  CB    . PRO B 1 553 ? 119.772 158.450 174.660 1.00 34.16 ?  553 PRO B CB    1 
ATOM   9996  C  CG    . PRO B 1 553 ? 121.073 157.736 174.570 1.00 32.33 ?  553 PRO B CG    1 
ATOM   9997  C  CD    . PRO B 1 553 ? 121.064 156.723 175.671 1.00 33.34 ?  553 PRO B CD    1 
ATOM   9998  N  N     . THR B 1 554 ? 117.351 159.455 176.813 1.00 43.12 ?  554 THR B N     1 
ATOM   9999  C  CA    . THR B 1 554 ? 115.937 159.492 177.134 1.00 41.44 ?  554 THR B CA    1 
ATOM   10000 C  C     . THR B 1 554 ? 115.160 160.133 175.989 1.00 38.99 ?  554 THR B C     1 
ATOM   10001 O  O     . THR B 1 554 ? 115.701 160.441 174.925 1.00 37.79 ?  554 THR B O     1 
ATOM   10002 C  CB    . THR B 1 554 ? 115.704 160.250 178.443 1.00 37.55 ?  554 THR B CB    1 
ATOM   10003 O  OG1   . THR B 1 554 ? 115.882 161.653 178.221 1.00 43.39 ?  554 THR B OG1   1 
ATOM   10004 C  CG2   . THR B 1 554 ? 116.684 159.784 179.505 1.00 36.57 ?  554 THR B CG2   1 
ATOM   10005 N  N     . THR B 1 555 ? 113.861 160.325 176.215 1.00 42.76 ?  555 THR B N     1 
ATOM   10006 C  CA    . THR B 1 555 ? 113.032 161.014 175.234 1.00 39.77 ?  555 THR B CA    1 
ATOM   10007 C  C     . THR B 1 555 ? 113.468 162.466 175.068 1.00 40.86 ?  555 THR B C     1 
ATOM   10008 O  O     . THR B 1 555 ? 113.499 162.987 173.947 1.00 44.26 ?  555 THR B O     1 
ATOM   10009 C  CB    . THR B 1 555 ? 111.562 160.921 175.644 1.00 43.88 ?  555 THR B CB    1 
ATOM   10010 O  OG1   . THR B 1 555 ? 111.059 159.619 175.320 1.00 42.11 ?  555 THR B OG1   1 
ATOM   10011 C  CG2   . THR B 1 555 ? 110.729 161.968 174.929 1.00 42.31 ?  555 THR B CG2   1 
ATOM   10012 N  N     . GLU B 1 556 ? 113.821 163.133 176.169 1.00 37.54 ?  556 GLU B N     1 
ATOM   10013 C  CA    . GLU B 1 556 ? 114.308 164.506 176.079 1.00 41.22 ?  556 GLU B CA    1 
ATOM   10014 C  C     . GLU B 1 556 ? 115.644 164.576 175.350 1.00 41.20 ?  556 GLU B C     1 
ATOM   10015 O  O     . GLU B 1 556 ? 115.883 165.504 174.568 1.00 45.19 ?  556 GLU B O     1 
ATOM   10016 C  CB    . GLU B 1 556 ? 114.422 165.114 177.476 1.00 42.16 ?  556 GLU B CB    1 
ATOM   10017 C  CG    . GLU B 1 556 ? 113.083 165.387 178.149 1.00 43.79 ?  556 GLU B CG    1 
ATOM   10018 C  CD    . GLU B 1 556 ? 112.046 165.945 177.191 1.00 46.68 ?  556 GLU B CD    1 
ATOM   10019 O  OE1   . GLU B 1 556 ? 112.061 167.168 176.943 1.00 44.65 ?  556 GLU B OE1   1 
ATOM   10020 O  OE2   . GLU B 1 556 ? 111.209 165.163 176.693 1.00 46.96 -1 556 GLU B OE2   1 
ATOM   10021 N  N     . ASP B 1 557 ? 116.530 163.608 175.596 1.00 39.92 ?  557 ASP B N     1 
ATOM   10022 C  CA    . ASP B 1 557 ? 117.789 163.555 174.862 1.00 35.53 ?  557 ASP B CA    1 
ATOM   10023 C  C     . ASP B 1 557 ? 117.543 163.361 173.373 1.00 36.19 ?  557 ASP B C     1 
ATOM   10024 O  O     . ASP B 1 557 ? 118.224 163.968 172.538 1.00 39.67 ?  557 ASP B O     1 
ATOM   10025 C  CB    . ASP B 1 557 ? 118.672 162.433 175.407 1.00 35.05 ?  557 ASP B CB    1 
ATOM   10026 C  CG    . ASP B 1 557 ? 119.150 162.701 176.817 1.00 42.94 ?  557 ASP B CG    1 
ATOM   10027 O  OD1   . ASP B 1 557 ? 119.746 163.773 177.050 1.00 44.87 ?  557 ASP B OD1   1 
ATOM   10028 O  OD2   . ASP B 1 557 ? 118.934 161.838 177.693 1.00 43.75 -1 557 ASP B OD2   1 
ATOM   10029 N  N     . TRP B 1 558 ? 116.569 162.523 173.020 1.00 30.30 ?  558 TRP B N     1 
ATOM   10030 C  CA    . TRP B 1 558 ? 116.244 162.324 171.613 1.00 26.01 ?  558 TRP B CA    1 
ATOM   10031 C  C     . TRP B 1 558 ? 115.621 163.569 170.994 1.00 31.95 ?  558 TRP B C     1 
ATOM   10032 O  O     . TRP B 1 558 ? 115.865 163.855 169.819 1.00 37.89 ?  558 TRP B O     1 
ATOM   10033 C  CB    . TRP B 1 558 ? 115.319 161.122 171.458 1.00 32.42 ?  558 TRP B CB    1 
ATOM   10034 C  CG    . TRP B 1 558 ? 116.058 159.832 171.318 1.00 28.63 ?  558 TRP B CG    1 
ATOM   10035 C  CD1   . TRP B 1 558 ? 116.171 158.846 172.251 1.00 25.06 ?  558 TRP B CD1   1 
ATOM   10036 C  CD2   . TRP B 1 558 ? 116.791 159.386 170.172 1.00 29.59 ?  558 TRP B CD2   1 
ATOM   10037 N  NE1   . TRP B 1 558 ? 116.927 157.813 171.758 1.00 31.93 ?  558 TRP B NE1   1 
ATOM   10038 C  CE2   . TRP B 1 558 ? 117.317 158.119 170.482 1.00 29.94 ?  558 TRP B CE2   1 
ATOM   10039 C  CE3   . TRP B 1 558 ? 117.045 159.933 168.911 1.00 30.69 ?  558 TRP B CE3   1 
ATOM   10040 C  CZ2   . TRP B 1 558 ? 118.085 157.391 169.578 1.00 25.80 ?  558 TRP B CZ2   1 
ATOM   10041 C  CZ3   . TRP B 1 558 ? 117.807 159.210 168.018 1.00 28.24 ?  558 TRP B CZ3   1 
ATOM   10042 C  CH2   . TRP B 1 558 ? 118.318 157.953 168.354 1.00 23.67 ?  558 TRP B CH2   1 
ATOM   10043 N  N     . LYS B 1 559 ? 114.821 164.318 171.755 1.00 36.67 ?  559 LYS B N     1 
ATOM   10044 C  CA    . LYS B 1 559 ? 114.304 165.587 171.249 1.00 34.56 ?  559 LYS B CA    1 
ATOM   10045 C  C     . LYS B 1 559 ? 115.430 166.587 171.015 1.00 37.87 ?  559 LYS B C     1 
ATOM   10046 O  O     . LYS B 1 559 ? 115.429 167.315 170.014 1.00 38.90 ?  559 LYS B O     1 
ATOM   10047 C  CB    . LYS B 1 559 ? 113.273 166.160 172.218 1.00 37.71 ?  559 LYS B CB    1 
ATOM   10048 C  CG    . LYS B 1 559 ? 111.922 165.477 172.162 1.00 42.19 ?  559 LYS B CG    1 
ATOM   10049 C  CD    . LYS B 1 559 ? 111.008 165.977 173.266 1.00 38.05 ?  559 LYS B CD    1 
ATOM   10050 C  CE    . LYS B 1 559 ? 109.773 165.107 173.394 1.00 41.69 ?  559 LYS B CE    1 
ATOM   10051 N  NZ    . LYS B 1 559 ? 109.235 165.117 174.781 1.00 39.05 1  559 LYS B NZ    1 
ATOM   10052 N  N     . LYS B 1 560 ? 116.397 166.638 171.933 1.00 34.00 ?  560 LYS B N     1 
ATOM   10053 C  CA    . LYS B 1 560 ? 117.552 167.508 171.743 1.00 33.62 ?  560 LYS B CA    1 
ATOM   10054 C  C     . LYS B 1 560 ? 118.352 167.094 170.513 1.00 38.20 ?  560 LYS B C     1 
ATOM   10055 O  O     . LYS B 1 560 ? 118.815 167.948 169.749 1.00 42.72 ?  560 LYS B O     1 
ATOM   10056 C  CB    . LYS B 1 560 ? 118.433 167.489 172.991 1.00 37.36 ?  560 LYS B CB    1 
ATOM   10057 C  CG    . LYS B 1 560 ? 118.015 168.485 174.057 1.00 37.70 ?  560 LYS B CG    1 
ATOM   10058 C  CD    . LYS B 1 560 ? 118.766 168.250 175.356 1.00 42.97 ?  560 LYS B CD    1 
ATOM   10059 C  CE    . LYS B 1 560 ? 117.847 168.394 176.558 1.00 39.49 ?  560 LYS B CE    1 
ATOM   10060 N  NZ    . LYS B 1 560 ? 117.929 167.213 177.463 1.00 44.10 1  560 LYS B NZ    1 
ATOM   10061 N  N     . LEU B 1 561 ? 118.523 165.788 170.306 1.00 36.05 ?  561 LEU B N     1 
ATOM   10062 C  CA    . LEU B 1 561 ? 119.213 165.308 169.113 1.00 30.62 ?  561 LEU B CA    1 
ATOM   10063 C  C     . LEU B 1 561 ? 118.439 165.653 167.847 1.00 34.86 ?  561 LEU B C     1 
ATOM   10064 O  O     . LEU B 1 561 ? 119.038 165.993 166.822 1.00 39.07 ?  561 LEU B O     1 
ATOM   10065 C  CB    . LEU B 1 561 ? 119.442 163.801 169.205 1.00 30.75 ?  561 LEU B CB    1 
ATOM   10066 C  CG    . LEU B 1 561 ? 120.239 163.199 168.046 1.00 32.12 ?  561 LEU B CG    1 
ATOM   10067 C  CD1   . LEU B 1 561 ? 121.569 163.912 167.900 1.00 28.52 ?  561 LEU B CD1   1 
ATOM   10068 C  CD2   . LEU B 1 561 ? 120.444 161.712 168.246 1.00 29.41 ?  561 LEU B CD2   1 
ATOM   10069 N  N     . LYS B 1 562 ? 117.110 165.554 167.895 1.00 30.80 ?  562 LYS B N     1 
ATOM   10070 C  CA    . LYS B 1 562 ? 116.290 165.927 166.747 1.00 32.43 ?  562 LYS B CA    1 
ATOM   10071 C  C     . LYS B 1 562 ? 116.452 167.403 166.413 1.00 37.34 ?  562 LYS B C     1 
ATOM   10072 O  O     . LYS B 1 562 ? 116.595 167.772 165.241 1.00 41.07 ?  562 LYS B O     1 
ATOM   10073 C  CB    . LYS B 1 562 ? 114.826 165.596 167.035 1.00 30.73 ?  562 LYS B CB    1 
ATOM   10074 C  CG    . LYS B 1 562 ? 113.847 166.071 165.982 1.00 31.43 ?  562 LYS B CG    1 
ATOM   10075 C  CD    . LYS B 1 562 ? 112.421 165.807 166.430 1.00 29.50 ?  562 LYS B CD    1 
ATOM   10076 C  CE    . LYS B 1 562 ? 111.423 166.090 165.325 1.00 35.36 ?  562 LYS B CE    1 
ATOM   10077 N  NZ    . LYS B 1 562 ? 110.118 165.430 165.595 1.00 39.56 1  562 LYS B NZ    1 
ATOM   10078 N  N     . ALA B 1 563 ? 116.446 168.261 167.434 1.00 33.87 ?  563 ALA B N     1 
ATOM   10079 C  CA    . ALA B 1 563 ? 116.669 169.685 167.205 1.00 30.54 ?  563 ALA B CA    1 
ATOM   10080 C  C     . ALA B 1 563 ? 118.065 169.941 166.647 1.00 33.60 ?  563 ALA B C     1 
ATOM   10081 O  O     . ALA B 1 563 ? 118.239 170.766 165.743 1.00 40.23 ?  563 ALA B O     1 
ATOM   10082 C  CB    . ALA B 1 563 ? 116.455 170.466 168.500 1.00 34.80 ?  563 ALA B CB    1 
ATOM   10083 N  N     . PHE B 1 564 ? 119.070 169.239 167.176 1.00 36.35 ?  564 PHE B N     1 
ATOM   10084 C  CA    . PHE B 1 564 ? 120.437 169.406 166.695 1.00 31.55 ?  564 PHE B CA    1 
ATOM   10085 C  C     . PHE B 1 564 ? 120.566 168.986 165.236 1.00 36.66 ?  564 PHE B C     1 
ATOM   10086 O  O     . PHE B 1 564 ? 121.253 169.648 164.450 1.00 41.78 ?  564 PHE B O     1 
ATOM   10087 C  CB    . PHE B 1 564 ? 121.392 168.600 167.576 1.00 32.48 ?  564 PHE B CB    1 
ATOM   10088 C  CG    . PHE B 1 564 ? 122.838 168.951 167.388 1.00 35.64 ?  564 PHE B CG    1 
ATOM   10089 C  CD1   . PHE B 1 564 ? 123.367 170.098 167.955 1.00 35.29 ?  564 PHE B CD1   1 
ATOM   10090 C  CD2   . PHE B 1 564 ? 123.672 168.129 166.652 1.00 39.70 ?  564 PHE B CD2   1 
ATOM   10091 C  CE1   . PHE B 1 564 ? 124.698 170.418 167.786 1.00 41.01 ?  564 PHE B CE1   1 
ATOM   10092 C  CE2   . PHE B 1 564 ? 125.003 168.445 166.478 1.00 38.51 ?  564 PHE B CE2   1 
ATOM   10093 C  CZ    . PHE B 1 564 ? 125.518 169.592 167.045 1.00 38.19 ?  564 PHE B CZ    1 
ATOM   10094 N  N     . VAL B 1 565 ? 119.914 167.886 164.857 1.00 32.89 ?  565 VAL B N     1 
ATOM   10095 C  CA    . VAL B 1 565 ? 119.977 167.414 163.478 1.00 29.38 ?  565 VAL B CA    1 
ATOM   10096 C  C     . VAL B 1 565 ? 119.230 168.365 162.554 1.00 35.25 ?  565 VAL B C     1 
ATOM   10097 O  O     . VAL B 1 565 ? 119.669 168.631 161.429 1.00 39.02 ?  565 VAL B O     1 
ATOM   10098 C  CB    . VAL B 1 565 ? 119.434 165.976 163.388 1.00 29.93 ?  565 VAL B CB    1 
ATOM   10099 C  CG1   . VAL B 1 565 ? 119.084 165.616 161.954 1.00 32.07 ?  565 VAL B CG1   1 
ATOM   10100 C  CG2   . VAL B 1 565 ? 120.448 165.000 163.948 1.00 32.11 ?  565 VAL B CG2   1 
ATOM   10101 N  N     . ALA B 1 566 ? 118.095 168.898 163.011 1.00 36.92 ?  566 ALA B N     1 
ATOM   10102 C  CA    . ALA B 1 566 ? 117.374 169.879 162.208 1.00 34.67 ?  566 ALA B CA    1 
ATOM   10103 C  C     . ALA B 1 566 ? 118.206 171.137 161.999 1.00 37.50 ?  566 ALA B C     1 
ATOM   10104 O  O     . ALA B 1 566 ? 118.194 171.727 160.913 1.00 43.33 ?  566 ALA B O     1 
ATOM   10105 C  CB    . ALA B 1 566 ? 116.041 170.222 162.871 1.00 34.64 ?  566 ALA B CB    1 
ATOM   10106 N  N     . GLU B 1 567 ? 118.935 171.565 163.030 1.00 38.02 ?  567 GLU B N     1 
ATOM   10107 C  CA    . GLU B 1 567 ? 119.729 172.782 162.923 1.00 37.40 ?  567 GLU B CA    1 
ATOM   10108 C  C     . GLU B 1 567 ? 120.959 172.576 162.044 1.00 42.54 ?  567 GLU B C     1 
ATOM   10109 O  O     . GLU B 1 567 ? 121.259 173.406 161.177 1.00 50.47 ?  567 GLU B O     1 
ATOM   10110 C  CB    . GLU B 1 567 ? 120.144 173.255 164.316 1.00 39.50 ?  567 GLU B CB    1 
ATOM   10111 C  CG    . GLU B 1 567 ? 120.896 174.571 164.325 1.00 42.29 ?  567 GLU B CG    1 
ATOM   10112 C  CD    . GLU B 1 567 ? 121.452 174.906 165.695 1.00 49.53 ?  567 GLU B CD    1 
ATOM   10113 O  OE1   . GLU B 1 567 ? 120.993 174.302 166.686 1.00 50.64 ?  567 GLU B OE1   1 
ATOM   10114 O  OE2   . GLU B 1 567 ? 122.342 175.777 165.780 1.00 46.30 -1 567 GLU B OE2   1 
ATOM   10115 N  N     . HIS B 1 568 ? 121.682 171.474 162.247 1.00 44.69 ?  568 HIS B N     1 
ATOM   10116 C  CA    . HIS B 1 568 ? 122.997 171.301 161.649 1.00 40.43 ?  568 HIS B CA    1 
ATOM   10117 C  C     . HIS B 1 568 ? 123.046 170.254 160.547 1.00 35.70 ?  568 HIS B C     1 
ATOM   10118 O  O     . HIS B 1 568 ? 124.055 170.175 159.840 1.00 44.65 ?  568 HIS B O     1 
ATOM   10119 C  CB    . HIS B 1 568 ? 124.023 170.935 162.730 1.00 39.32 ?  568 HIS B CB    1 
ATOM   10120 C  CG    . HIS B 1 568 ? 124.290 172.038 163.705 1.00 39.80 ?  568 HIS B CG    1 
ATOM   10121 N  ND1   . HIS B 1 568 ? 123.897 171.976 165.024 1.00 41.70 ?  568 HIS B ND1   1 
ATOM   10122 C  CD2   . HIS B 1 568 ? 124.897 173.237 163.549 1.00 40.68 ?  568 HIS B CD2   1 
ATOM   10123 C  CE1   . HIS B 1 568 ? 124.260 173.085 165.642 1.00 41.70 ?  568 HIS B CE1   1 
ATOM   10124 N  NE2   . HIS B 1 568 ? 124.869 173.867 164.770 1.00 46.63 ?  568 HIS B NE2   1 
ATOM   10125 N  N     . GLY B 1 569 ? 122.005 169.459 160.382 1.00 30.82 ?  569 GLY B N     1 
ATOM   10126 C  CA    . GLY B 1 569 ? 122.014 168.446 159.352 1.00 29.68 ?  569 GLY B CA    1 
ATOM   10127 C  C     . GLY B 1 569 ? 122.678 167.163 159.800 1.00 30.05 ?  569 GLY B C     1 
ATOM   10128 O  O     . GLY B 1 569 ? 123.031 166.963 160.965 1.00 38.28 ?  569 GLY B O     1 
ATOM   10129 N  N     . MET B 1 570 ? 122.842 166.268 158.833 1.00 26.75 ?  570 MET B N     1 
ATOM   10130 C  CA    . MET B 1 570 ? 123.362 164.932 159.078 1.00 22.89 ?  570 MET B CA    1 
ATOM   10131 C  C     . MET B 1 570 ? 124.396 164.621 158.008 1.00 24.69 ?  570 MET B C     1 
ATOM   10132 O  O     . MET B 1 570 ? 124.122 164.788 156.816 1.00 30.73 ?  570 MET B O     1 
ATOM   10133 C  CB    . MET B 1 570 ? 122.216 163.916 159.065 1.00 31.01 ?  570 MET B CB    1 
ATOM   10134 C  CG    . MET B 1 570 ? 121.695 163.555 160.446 1.00 24.56 ?  570 MET B CG    1 
ATOM   10135 S  SD    . MET B 1 570 ? 121.196 161.837 160.609 1.00 46.73 ?  570 MET B SD    1 
ATOM   10136 C  CE    . MET B 1 570 ? 122.768 161.022 160.708 1.00 26.89 ?  570 MET B CE    1 
ATOM   10137 N  N     . TYR B 1 571 ? 125.586 164.189 158.430 1.00 21.99 ?  571 TYR B N     1 
ATOM   10138 C  CA    . TYR B 1 571 ? 126.682 164.017 157.483 1.00 13.75 ?  571 TYR B CA    1 
ATOM   10139 C  C     . TYR B 1 571 ? 126.585 162.717 156.696 1.00 22.97 ?  571 TYR B C     1 
ATOM   10140 O  O     . TYR B 1 571 ? 126.977 162.681 155.526 1.00 21.03 ?  571 TYR B O     1 
ATOM   10141 C  CB    . TYR B 1 571 ? 128.026 164.077 158.207 1.00 18.76 ?  571 TYR B CB    1 
ATOM   10142 C  CG    . TYR B 1 571 ? 129.213 164.130 157.272 1.00 21.18 ?  571 TYR B CG    1 
ATOM   10143 C  CD1   . TYR B 1 571 ? 129.552 165.306 156.616 1.00 23.79 ?  571 TYR B CD1   1 
ATOM   10144 C  CD2   . TYR B 1 571 ? 129.991 163.005 157.041 1.00 21.32 ?  571 TYR B CD2   1 
ATOM   10145 C  CE1   . TYR B 1 571 ? 130.632 165.357 155.759 1.00 22.28 ?  571 TYR B CE1   1 
ATOM   10146 C  CE2   . TYR B 1 571 ? 131.070 163.047 156.188 1.00 23.34 ?  571 TYR B CE2   1 
ATOM   10147 C  CZ    . TYR B 1 571 ? 131.388 164.225 155.551 1.00 28.65 ?  571 TYR B CZ    1 
ATOM   10148 O  OH    . TYR B 1 571 ? 132.467 164.270 154.700 1.00 30.16 ?  571 TYR B OH    1 
ATOM   10149 N  N     . HIS B 1 572 ? 126.074 161.653 157.306 1.00 25.77 ?  572 HIS B N     1 
ATOM   10150 C  CA    . HIS B 1 572 ? 126.003 160.343 156.674 1.00 11.39 ?  572 HIS B CA    1 
ATOM   10151 C  C     . HIS B 1 572 ? 124.557 160.002 156.354 1.00 16.85 ?  572 HIS B C     1 
ATOM   10152 O  O     . HIS B 1 572 ? 123.690 160.067 157.233 1.00 31.90 ?  572 HIS B O     1 
ATOM   10153 C  CB    . HIS B 1 572 ? 126.607 159.260 157.573 1.00 12.19 ?  572 HIS B CB    1 
ATOM   10154 C  CG    . HIS B 1 572 ? 127.937 159.622 158.152 1.00 9.40  ?  572 HIS B CG    1 
ATOM   10155 N  ND1   . HIS B 1 572 ? 128.074 160.253 159.369 1.00 15.89 ?  572 HIS B ND1   1 
ATOM   10156 C  CD2   . HIS B 1 572 ? 129.193 159.436 157.684 1.00 13.40 ?  572 HIS B CD2   1 
ATOM   10157 C  CE1   . HIS B 1 572 ? 129.355 160.443 159.624 1.00 14.22 ?  572 HIS B CE1   1 
ATOM   10158 N  NE2   . HIS B 1 572 ? 130.055 159.957 158.616 1.00 24.57 ?  572 HIS B NE2   1 
ATOM   10159 N  N     . SER B 1 573 ? 124.301 159.642 155.096 1.00 10.81 ?  573 SER B N     1 
ATOM   10160 C  CA    . SER B 1 573 ? 122.979 159.147 154.728 1.00 8.56  ?  573 SER B CA    1 
ATOM   10161 C  C     . SER B 1 573 ? 122.669 157.849 155.456 1.00 17.12 ?  573 SER B C     1 
ATOM   10162 O  O     . SER B 1 573 ? 121.531 157.616 155.877 1.00 29.36 ?  573 SER B O     1 
ATOM   10163 C  CB    . SER B 1 573 ? 122.893 158.945 153.217 1.00 13.78 ?  573 SER B CB    1 
ATOM   10164 O  OG    . SER B 1 573 ? 124.077 158.351 152.723 1.00 25.31 ?  573 SER B OG    1 
ATOM   10165 N  N     . TYR B 1 574 ? 123.671 156.991 155.605 1.00 14.91 ?  574 TYR B N     1 
ATOM   10166 C  CA    . TYR B 1 574 ? 123.537 155.714 156.282 1.00 0.00  ?  574 TYR B CA    1 
ATOM   10167 C  C     . TYR B 1 574 ? 124.718 155.538 157.220 1.00 10.00 ?  574 TYR B C     1 
ATOM   10168 O  O     . TYR B 1 574 ? 125.846 155.906 156.883 1.00 19.34 ?  574 TYR B O     1 
ATOM   10169 C  CB    . TYR B 1 574 ? 123.468 154.569 155.273 1.00 10.33 ?  574 TYR B CB    1 
ATOM   10170 C  CG    . TYR B 1 574 ? 122.415 154.780 154.211 1.00 0.00  ?  574 TYR B CG    1 
ATOM   10171 C  CD1   . TYR B 1 574 ? 121.115 154.339 154.402 1.00 3.61  ?  574 TYR B CD1   1 
ATOM   10172 C  CD2   . TYR B 1 574 ? 122.717 155.434 153.025 1.00 3.57  ?  574 TYR B CD2   1 
ATOM   10173 C  CE1   . TYR B 1 574 ? 120.149 154.536 153.442 1.00 5.96  ?  574 TYR B CE1   1 
ATOM   10174 C  CE2   . TYR B 1 574 ? 121.755 155.637 152.059 1.00 10.55 ?  574 TYR B CE2   1 
ATOM   10175 C  CZ    . TYR B 1 574 ? 120.474 155.183 152.272 1.00 2.73  ?  574 TYR B CZ    1 
ATOM   10176 O  OH    . TYR B 1 574 ? 119.512 155.376 151.313 1.00 15.62 ?  574 TYR B OH    1 
ATOM   10177 N  N     . ARG B 1 575 ? 124.455 154.984 158.396 1.00 12.14 ?  575 ARG B N     1 
ATOM   10178 C  CA    . ARG B 1 575 ? 125.468 154.886 159.438 1.00 0.00  ?  575 ARG B CA    1 
ATOM   10179 C  C     . ARG B 1 575 ? 125.698 153.475 159.942 1.00 11.16 ?  575 ARG B C     1 
ATOM   10180 O  O     . ARG B 1 575 ? 126.845 153.090 160.174 1.00 23.55 ?  575 ARG B O     1 
ATOM   10181 C  CB    . ARG B 1 575 ? 125.082 155.770 160.624 1.00 13.58 ?  575 ARG B CB    1 
ATOM   10182 C  CG    . ARG B 1 575 ? 125.028 157.241 160.315 1.00 8.83  ?  575 ARG B CG    1 
ATOM   10183 C  CD    . ARG B 1 575 ? 124.202 157.954 161.353 1.00 11.19 ?  575 ARG B CD    1 
ATOM   10184 N  NE    . ARG B 1 575 ? 122.781 157.671 161.193 1.00 16.96 ?  575 ARG B NE    1 
ATOM   10185 C  CZ    . ARG B 1 575 ? 122.085 156.857 161.972 1.00 11.69 ?  575 ARG B CZ    1 
ATOM   10186 N  NH1   . ARG B 1 575 ? 122.650 156.217 162.981 1.00 11.22 1  575 ARG B NH1   1 
ATOM   10187 N  NH2   . ARG B 1 575 ? 120.790 156.684 161.737 1.00 11.31 ?  575 ARG B NH2   1 
ATOM   10188 N  N     . LEU B 1 576 ? 124.641 152.690 160.121 1.00 21.07 ?  576 LEU B N     1 
ATOM   10189 C  CA    . LEU B 1 576 ? 124.718 151.427 160.836 1.00 12.04 ?  576 LEU B CA    1 
ATOM   10190 C  C     . LEU B 1 576 ? 124.283 150.287 159.930 1.00 4.46  ?  576 LEU B C     1 
ATOM   10191 O  O     . LEU B 1 576 ? 123.203 150.340 159.335 1.00 20.33 ?  576 LEU B O     1 
ATOM   10192 C  CB    . LEU B 1 576 ? 123.842 151.463 162.090 1.00 7.86  ?  576 LEU B CB    1 
ATOM   10193 C  CG    . LEU B 1 576 ? 124.017 152.672 163.009 1.00 7.05  ?  576 LEU B CG    1 
ATOM   10194 C  CD1   . LEU B 1 576 ? 122.983 152.654 164.118 1.00 12.34 ?  576 LEU B CD1   1 
ATOM   10195 C  CD2   . LEU B 1 576 ? 125.417 152.705 163.586 1.00 11.05 ?  576 LEU B CD2   1 
ATOM   10196 N  N     . CYS B 1 577 ? 125.131 149.269 159.821 1.00 10.65 ?  577 CYS B N     1 
ATOM   10197 C  CA    . CYS B 1 577 ? 124.772 148.017 159.172 1.00 7.20  ?  577 CYS B CA    1 
ATOM   10198 C  C     . CYS B 1 577 ? 125.574 146.912 159.837 1.00 21.29 ?  577 CYS B C     1 
ATOM   10199 O  O     . CYS B 1 577 ? 126.781 147.059 160.043 1.00 26.91 ?  577 CYS B O     1 
ATOM   10200 C  CB    . CYS B 1 577 ? 125.034 148.062 157.659 1.00 4.23  ?  577 CYS B CB    1 
ATOM   10201 S  SG    . CYS B 1 577 ? 126.748 147.849 157.123 1.00 34.79 ?  577 CYS B SG    1 
ATOM   10202 N  N     . ILE B 1 578 ? 124.905 145.820 160.187 1.00 15.00 ?  578 ILE B N     1 
ATOM   10203 C  CA    . ILE B 1 578 ? 125.520 144.733 160.934 1.00 12.69 ?  578 ILE B CA    1 
ATOM   10204 C  C     . ILE B 1 578 ? 125.937 143.665 159.929 1.00 5.09  ?  578 ILE B C     1 
ATOM   10205 O  O     . ILE B 1 578 ? 125.131 142.831 159.514 1.00 20.00 ?  578 ILE B O     1 
ATOM   10206 C  CB    . ILE B 1 578 ? 124.583 144.182 162.010 1.00 10.95 ?  578 ILE B CB    1 
ATOM   10207 C  CG1   . ILE B 1 578 ? 124.091 145.321 162.906 1.00 2.62  ?  578 ILE B CG1   1 
ATOM   10208 C  CG2   . ILE B 1 578 ? 125.294 143.145 162.852 1.00 8.83  ?  578 ILE B CG2   1 
ATOM   10209 C  CD1   . ILE B 1 578 ? 123.333 144.856 164.119 1.00 9.60  ?  578 ILE B CD1   1 
ATOM   10210 N  N     . ALA B 1 579 ? 127.206 143.704 159.533 1.00 14.77 ?  579 ALA B N     1 
ATOM   10211 C  CA    . ALA B 1 579 ? 127.799 142.737 158.627 1.00 4.76  ?  579 ALA B CA    1 
ATOM   10212 C  C     . ALA B 1 579 ? 128.094 141.426 159.354 1.00 18.65 ?  579 ALA B C     1 
ATOM   10213 O  O     . ALA B 1 579 ? 128.115 141.383 160.585 1.00 31.68 ?  579 ALA B O     1 
ATOM   10214 C  CB    . ALA B 1 579 ? 129.076 143.312 158.025 1.00 9.76  ?  579 ALA B CB    1 
ATOM   10215 N  N     . PRO B 1 580 ? 128.303 140.332 158.613 1.00 25.93 ?  580 PRO B N     1 
ATOM   10216 C  CA    . PRO B 1 580 ? 128.589 139.047 159.278 1.00 23.57 ?  580 PRO B CA    1 
ATOM   10217 C  C     . PRO B 1 580 ? 129.844 139.047 160.142 1.00 31.60 ?  580 PRO B C     1 
ATOM   10218 O  O     . PRO B 1 580 ? 129.875 138.325 161.147 1.00 37.76 ?  580 PRO B O     1 
ATOM   10219 C  CB    . PRO B 1 580 ? 128.714 138.061 158.105 1.00 23.45 ?  580 PRO B CB    1 
ATOM   10220 C  CG    . PRO B 1 580 ? 128.818 138.896 156.877 1.00 23.60 ?  580 PRO B CG    1 
ATOM   10221 C  CD    . PRO B 1 580 ? 128.093 140.160 157.167 1.00 20.84 ?  580 PRO B CD    1 
ATOM   10222 N  N     . THR B 1 581 ? 130.869 139.825 159.792 1.00 24.16 ?  581 THR B N     1 
ATOM   10223 C  CA    . THR B 1 581 ? 132.130 139.887 160.544 1.00 33.88 ?  581 THR B CA    1 
ATOM   10224 C  C     . THR B 1 581 ? 132.738 138.492 160.711 1.00 32.21 ?  581 THR B C     1 
ATOM   10225 O  O     . THR B 1 581 ? 132.870 137.960 161.812 1.00 34.51 ?  581 THR B O     1 
ATOM   10226 C  CB    . THR B 1 581 ? 131.952 140.558 161.911 1.00 28.70 ?  581 THR B CB    1 
ATOM   10227 O  OG1   . THR B 1 581 ? 131.479 139.596 162.862 1.00 24.16 ?  581 THR B OG1   1 
ATOM   10228 C  CG2   . THR B 1 581 ? 130.981 141.718 161.829 1.00 31.20 ?  581 THR B CG2   1 
ATOM   10229 N  N     . GLY B 1 582 ? 133.104 137.914 159.571 1.00 31.94 ?  582 GLY B N     1 
ATOM   10230 C  CA    . GLY B 1 582 ? 133.536 136.532 159.529 1.00 34.72 ?  582 GLY B CA    1 
ATOM   10231 C  C     . GLY B 1 582 ? 134.831 136.219 160.251 1.00 37.48 ?  582 GLY B C     1 
ATOM   10232 O  O     . GLY B 1 582 ? 134.823 135.498 161.253 1.00 41.71 ?  582 GLY B O     1 
ATOM   10233 N  N     . SER B 1 583 ? 135.952 136.751 159.763 1.00 37.76 ?  583 SER B N     1 
ATOM   10234 C  CA    . SER B 1 583 ? 137.258 136.354 160.275 1.00 42.54 ?  583 SER B CA    1 
ATOM   10235 C  C     . SER B 1 583 ? 137.785 137.274 161.367 1.00 39.80 ?  583 SER B C     1 
ATOM   10236 O  O     . SER B 1 583 ? 138.604 136.837 162.185 1.00 39.77 ?  583 SER B O     1 
ATOM   10237 C  CB    . SER B 1 583 ? 138.275 136.289 159.134 1.00 47.40 ?  583 SER B CB    1 
ATOM   10238 O  OG    . SER B 1 583 ? 138.129 135.091 158.390 1.00 49.21 ?  583 SER B OG    1 
ATOM   10239 N  N     . ILE B 1 584 ? 137.348 138.534 161.403 1.00 33.05 ?  584 ILE B N     1 
ATOM   10240 C  CA    . ILE B 1 584 ? 137.779 139.446 162.455 1.00 28.91 ?  584 ILE B CA    1 
ATOM   10241 C  C     . ILE B 1 584 ? 137.205 139.089 163.815 1.00 31.88 ?  584 ILE B C     1 
ATOM   10242 O  O     . ILE B 1 584 ? 137.671 139.615 164.830 1.00 36.84 ?  584 ILE B O     1 
ATOM   10243 C  CB    . ILE B 1 584 ? 137.405 140.904 162.113 1.00 36.81 ?  584 ILE B CB    1 
ATOM   10244 C  CG1   . ILE B 1 584 ? 135.917 141.009 161.772 1.00 34.43 ?  584 ILE B CG1   1 
ATOM   10245 C  CG2   . ILE B 1 584 ? 138.275 141.431 160.986 1.00 32.57 ?  584 ILE B CG2   1 
ATOM   10246 C  CD1   . ILE B 1 584 ? 135.417 142.431 161.650 1.00 33.31 ?  584 ILE B CD1   1 
ATOM   10247 N  N     . SER B 1 585 ? 136.198 138.213 163.863 1.00 31.76 ?  585 SER B N     1 
ATOM   10248 C  CA    . SER B 1 585 ? 135.631 137.812 165.144 1.00 29.12 ?  585 SER B CA    1 
ATOM   10249 C  C     . SER B 1 585 ? 136.604 136.961 165.948 1.00 28.92 ?  585 SER B C     1 
ATOM   10250 O  O     . SER B 1 585 ? 136.637 137.060 167.178 1.00 29.13 ?  585 SER B O     1 
ATOM   10251 C  CB    . SER B 1 585 ? 134.319 137.060 164.925 1.00 32.20 ?  585 SER B CB    1 
ATOM   10252 O  OG    . SER B 1 585 ? 134.507 135.940 164.079 1.00 36.22 ?  585 SER B OG    1 
ATOM   10253 N  N     . TYR B 1 586 ? 137.393 136.118 165.278 1.00 35.47 ?  586 TYR B N     1 
ATOM   10254 C  CA    . TYR B 1 586 ? 138.397 135.329 165.984 1.00 36.44 ?  586 TYR B CA    1 
ATOM   10255 C  C     . TYR B 1 586 ? 139.453 136.224 166.615 1.00 34.72 ?  586 TYR B C     1 
ATOM   10256 O  O     . TYR B 1 586 ? 139.828 136.032 167.776 1.00 41.06 ?  586 TYR B O     1 
ATOM   10257 C  CB    . TYR B 1 586 ? 139.058 134.333 165.033 1.00 32.67 ?  586 TYR B CB    1 
ATOM   10258 C  CG    . TYR B 1 586 ? 138.114 133.338 164.406 1.00 33.53 ?  586 TYR B CG    1 
ATOM   10259 C  CD1   . TYR B 1 586 ? 137.543 133.581 163.165 1.00 36.90 ?  586 TYR B CD1   1 
ATOM   10260 C  CD2   . TYR B 1 586 ? 137.797 132.152 165.051 1.00 35.45 ?  586 TYR B CD2   1 
ATOM   10261 C  CE1   . TYR B 1 586 ? 136.682 132.672 162.585 1.00 39.70 ?  586 TYR B CE1   1 
ATOM   10262 C  CE2   . TYR B 1 586 ? 136.938 131.237 164.479 1.00 37.85 ?  586 TYR B CE2   1 
ATOM   10263 C  CZ    . TYR B 1 586 ? 136.382 131.502 163.247 1.00 39.59 ?  586 TYR B CZ    1 
ATOM   10264 O  OH    . TYR B 1 586 ? 135.524 130.593 162.674 1.00 44.24 ?  586 TYR B OH    1 
ATOM   10265 N  N     . VAL B 1 587 ? 139.938 137.215 165.861 1.00 29.79 ?  587 VAL B N     1 
ATOM   10266 C  CA    . VAL B 1 587 ? 140.977 138.109 166.364 1.00 24.81 ?  587 VAL B CA    1 
ATOM   10267 C  C     . VAL B 1 587 ? 140.476 138.879 167.579 1.00 30.49 ?  587 VAL B C     1 
ATOM   10268 O  O     . VAL B 1 587 ? 141.222 139.109 168.539 1.00 39.87 ?  587 VAL B O     1 
ATOM   10269 C  CB    . VAL B 1 587 ? 141.442 139.058 165.245 1.00 31.15 ?  587 VAL B CB    1 
ATOM   10270 C  CG1   . VAL B 1 587 ? 142.469 140.043 165.770 1.00 34.30 ?  587 VAL B CG1   1 
ATOM   10271 C  CG2   . VAL B 1 587 ? 142.005 138.264 164.080 1.00 31.54 ?  587 VAL B CG2   1 
ATOM   10272 N  N     . GLN B 1 588 ? 139.209 139.279 167.561 1.00 34.77 ?  588 GLN B N     1 
ATOM   10273 C  CA    . GLN B 1 588 ? 138.622 140.034 168.657 1.00 29.40 ?  588 GLN B CA    1 
ATOM   10274 C  C     . GLN B 1 588 ? 138.130 139.150 169.792 1.00 34.28 ?  588 GLN B C     1 
ATOM   10275 O  O     . GLN B 1 588 ? 137.640 139.683 170.793 1.00 36.74 ?  588 GLN B O     1 
ATOM   10276 C  CB    . GLN B 1 588 ? 137.467 140.891 168.139 1.00 22.63 ?  588 GLN B CB    1 
ATOM   10277 C  CG    . GLN B 1 588 ? 137.909 142.105 167.350 1.00 24.46 ?  588 GLN B CG    1 
ATOM   10278 C  CD    . GLN B 1 588 ? 138.014 143.343 168.211 1.00 29.18 ?  588 GLN B CD    1 
ATOM   10279 O  OE1   . GLN B 1 588 ? 137.175 143.582 169.077 1.00 29.62 ?  588 GLN B OE1   1 
ATOM   10280 N  NE2   . GLN B 1 588 ? 139.048 144.140 167.979 1.00 33.47 ?  588 GLN B NE2   1 
ATOM   10281 N  N     . SER B 1 589 ? 138.255 137.830 169.663 1.00 34.31 ?  589 SER B N     1 
ATOM   10282 C  CA    . SER B 1 589 ? 137.712 136.878 170.630 1.00 28.15 ?  589 SER B CA    1 
ATOM   10283 C  C     . SER B 1 589 ? 136.236 137.173 170.883 1.00 31.62 ?  589 SER B C     1 
ATOM   10284 O  O     . SER B 1 589 ? 135.799 137.438 172.003 1.00 35.30 ?  589 SER B O     1 
ATOM   10285 C  CB    . SER B 1 589 ? 138.518 136.896 171.931 1.00 36.32 ?  589 SER B CB    1 
ATOM   10286 O  OG    . SER B 1 589 ? 138.355 135.686 172.649 1.00 45.26 ?  589 SER B OG    1 
ATOM   10287 N  N     . SER B 1 590 ? 135.468 137.135 169.798 1.00 30.54 ?  590 SER B N     1 
ATOM   10288 C  CA    . SER B 1 590 ? 134.078 137.550 169.819 1.00 23.07 ?  590 SER B CA    1 
ATOM   10289 C  C     . SER B 1 590 ? 133.242 136.589 168.990 1.00 28.21 ?  590 SER B C     1 
ATOM   10290 O  O     . SER B 1 590 ? 133.744 135.943 168.067 1.00 36.37 ?  590 SER B O     1 
ATOM   10291 C  CB    . SER B 1 590 ? 133.918 138.976 169.280 1.00 26.65 ?  590 SER B CB    1 
ATOM   10292 O  OG    . SER B 1 590 ? 133.751 138.973 167.876 1.00 36.42 ?  590 SER B OG    1 
ATOM   10293 N  N     . THR B 1 591 ? 131.963 136.492 169.335 1.00 30.26 ?  591 THR B N     1 
ATOM   10294 C  CA    . THR B 1 591 ? 131.018 135.753 168.512 1.00 27.61 ?  591 THR B CA    1 
ATOM   10295 C  C     . THR B 1 591 ? 130.649 136.585 167.291 1.00 30.48 ?  591 THR B C     1 
ATOM   10296 O  O     . THR B 1 591 ? 130.577 137.815 167.358 1.00 25.23 ?  591 THR B O     1 
ATOM   10297 C  CB    . THR B 1 591 ? 129.767 135.390 169.312 1.00 28.23 ?  591 THR B CB    1 
ATOM   10298 O  OG1   . THR B 1 591 ? 129.009 136.572 169.589 1.00 36.89 ?  591 THR B OG1   1 
ATOM   10299 C  CG2   . THR B 1 591 ? 130.157 134.727 170.621 1.00 26.83 ?  591 THR B CG2   1 
ATOM   10300 N  N     . ALA B 1 592 ? 130.426 135.906 166.170 1.00 26.62 ?  592 ALA B N     1 
ATOM   10301 C  CA    . ALA B 1 592 ? 130.258 136.597 164.899 1.00 25.14 ?  592 ALA B CA    1 
ATOM   10302 C  C     . ALA B 1 592 ? 128.960 137.392 164.876 1.00 24.71 ?  592 ALA B C     1 
ATOM   10303 O  O     . ALA B 1 592 ? 127.871 136.831 165.033 1.00 32.62 ?  592 ALA B O     1 
ATOM   10304 C  CB    . ALA B 1 592 ? 130.279 135.594 163.748 1.00 31.49 ?  592 ALA B CB    1 
ATOM   10305 N  N     . SER B 1 593 ? 129.085 138.701 164.681 1.00 27.77 ?  593 SER B N     1 
ATOM   10306 C  CA    . SER B 1 593 ? 127.954 139.608 164.450 1.00 16.57 ?  593 SER B CA    1 
ATOM   10307 C  C     . SER B 1 593 ? 126.993 139.527 165.638 1.00 14.42 ?  593 SER B C     1 
ATOM   10308 O  O     . SER B 1 593 ? 127.403 139.245 166.770 1.00 29.93 ?  593 SER B O     1 
ATOM   10309 C  CB    . SER B 1 593 ? 127.328 139.286 163.107 1.00 28.74 ?  593 SER B CB    1 
ATOM   10310 O  OG    . SER B 1 593 ? 126.241 140.143 162.830 1.00 24.93 ?  593 SER B OG    1 
ATOM   10311 N  N     . VAL B 1 594 ? 125.707 139.774 165.390 1.00 20.91 ?  594 VAL B N     1 
ATOM   10312 C  CA    . VAL B 1 594 ? 124.676 139.619 166.404 1.00 17.98 ?  594 VAL B CA    1 
ATOM   10313 C  C     . VAL B 1 594 ? 124.034 138.239 166.345 1.00 15.70 ?  594 VAL B C     1 
ATOM   10314 O  O     . VAL B 1 594 ? 123.084 137.967 167.083 1.00 25.92 ?  594 VAL B O     1 
ATOM   10315 C  CB    . VAL B 1 594 ? 123.612 140.722 166.285 1.00 23.80 ?  594 VAL B CB    1 
ATOM   10316 C  CG1   . VAL B 1 594 ? 124.187 142.060 166.718 1.00 14.10 ?  594 VAL B CG1   1 
ATOM   10317 C  CG2   . VAL B 1 594 ? 123.083 140.799 164.865 1.00 22.03 ?  594 VAL B CG2   1 
ATOM   10318 N  N     . MET B 1 595 ? 124.535 137.361 165.482 1.00 25.63 ?  595 MET B N     1 
ATOM   10319 C  CA    . MET B 1 595 ? 123.994 136.019 165.370 1.00 19.42 ?  595 MET B CA    1 
ATOM   10320 C  C     . MET B 1 595 ? 124.378 135.183 166.588 1.00 24.87 ?  595 MET B C     1 
ATOM   10321 O  O     . MET B 1 595 ? 125.413 135.421 167.216 1.00 32.63 ?  595 MET B O     1 
ATOM   10322 C  CB    . MET B 1 595 ? 124.512 135.340 164.104 1.00 22.58 ?  595 MET B CB    1 
ATOM   10323 C  CG    . MET B 1 595 ? 124.100 135.978 162.779 1.00 24.99 ?  595 MET B CG    1 
ATOM   10324 S  SD    . MET B 1 595 ? 122.419 135.640 162.210 1.00 37.28 ?  595 MET B SD    1 
ATOM   10325 C  CE    . MET B 1 595 ? 121.437 136.742 163.220 1.00 16.63 ?  595 MET B CE    1 
ATOM   10326 N  N     . PRO B 1 596 ? 123.560 134.195 166.942 1.00 32.04 ?  596 PRO B N     1 
ATOM   10327 C  CA    . PRO B 1 596 ? 123.973 133.233 167.966 1.00 20.66 ?  596 PRO B CA    1 
ATOM   10328 C  C     . PRO B 1 596 ? 125.007 132.264 167.416 1.00 31.12 ?  596 PRO B C     1 
ATOM   10329 O  O     . PRO B 1 596 ? 125.161 132.091 166.204 1.00 37.74 ?  596 PRO B O     1 
ATOM   10330 C  CB    . PRO B 1 596 ? 122.670 132.521 168.329 1.00 22.35 ?  596 PRO B CB    1 
ATOM   10331 C  CG    . PRO B 1 596 ? 121.843 132.616 167.100 1.00 27.79 ?  596 PRO B CG    1 
ATOM   10332 C  CD    . PRO B 1 596 ? 122.202 133.920 166.439 1.00 32.26 ?  596 PRO B CD    1 
ATOM   10333 N  N     . ILE B 1 597 ? 125.729 131.626 168.337 1.00 28.45 ?  597 ILE B N     1 
ATOM   10334 C  CA    . ILE B 1 597 ? 126.836 130.762 167.948 1.00 28.60 ?  597 ILE B CA    1 
ATOM   10335 C  C     . ILE B 1 597 ? 126.305 129.493 167.295 1.00 37.55 ?  597 ILE B C     1 
ATOM   10336 O  O     . ILE B 1 597 ? 125.292 128.924 167.721 1.00 40.72 ?  597 ILE B O     1 
ATOM   10337 C  CB    . ILE B 1 597 ? 127.719 130.437 169.165 1.00 33.65 ?  597 ILE B CB    1 
ATOM   10338 C  CG1   . ILE B 1 597 ? 126.906 129.732 170.250 1.00 34.53 ?  597 ILE B CG1   1 
ATOM   10339 C  CG2   . ILE B 1 597 ? 128.342 131.703 169.714 1.00 31.62 ?  597 ILE B CG2   1 
ATOM   10340 C  CD1   . ILE B 1 597 ? 127.723 128.816 171.121 1.00 33.96 ?  597 ILE B CD1   1 
ATOM   10341 N  N     . MET B 1 598 ? 126.986 129.054 166.236 1.00 44.87 ?  598 MET B N     1 
ATOM   10342 C  CA    . MET B 1 598 ? 126.612 127.806 165.580 1.00 41.70 ?  598 MET B CA    1 
ATOM   10343 C  C     . MET B 1 598 ? 127.013 126.604 166.424 1.00 38.38 ?  598 MET B C     1 
ATOM   10344 O  O     . MET B 1 598 ? 126.228 125.666 166.601 1.00 46.97 ?  598 MET B O     1 
ATOM   10345 C  CB    . MET B 1 598 ? 127.257 127.731 164.197 1.00 40.80 ?  598 MET B CB    1 
ATOM   10346 C  CG    . MET B 1 598 ? 126.899 128.884 163.283 1.00 39.04 ?  598 MET B CG    1 
ATOM   10347 S  SD    . MET B 1 598 ? 127.225 128.515 161.551 1.00 59.89 ?  598 MET B SD    1 
ATOM   10348 C  CE    . MET B 1 598 ? 128.649 129.558 161.253 1.00 42.97 ?  598 MET B CE    1 
ATOM   10349 N  N     . GLU B 1 599 ? 128.235 126.617 166.953 1.00 42.37 ?  599 GLU B N     1 
ATOM   10350 C  CA    . GLU B 1 599 ? 128.757 125.534 167.773 1.00 42.26 ?  599 GLU B CA    1 
ATOM   10351 C  C     . GLU B 1 599 ? 129.362 126.110 169.042 1.00 40.25 ?  599 GLU B C     1 
ATOM   10352 O  O     . GLU B 1 599 ? 129.874 127.232 169.049 1.00 46.11 ?  599 GLU B O     1 
ATOM   10353 C  CB    . GLU B 1 599 ? 129.820 124.716 167.025 1.00 44.07 ?  599 GLU B CB    1 
ATOM   10354 C  CG    . GLU B 1 599 ? 129.711 124.775 165.512 1.00 43.73 ?  599 GLU B CG    1 
ATOM   10355 C  CD    . GLU B 1 599 ? 130.877 124.102 164.819 1.00 50.12 ?  599 GLU B CD    1 
ATOM   10356 O  OE1   . GLU B 1 599 ? 131.304 123.023 165.280 1.00 49.97 ?  599 GLU B OE1   1 
ATOM   10357 O  OE2   . GLU B 1 599 ? 131.367 124.652 163.810 1.00 48.55 -1 599 GLU B OE2   1 
ATOM   10358 N  N     . ARG B 1 600 ? 129.299 125.334 170.124 1.00 43.29 ?  600 ARG B N     1 
ATOM   10359 C  CA    . ARG B 1 600 ? 129.925 125.764 171.370 1.00 35.78 ?  600 ARG B CA    1 
ATOM   10360 C  C     . ARG B 1 600 ? 131.442 125.732 171.257 1.00 37.20 ?  600 ARG B C     1 
ATOM   10361 O  O     . ARG B 1 600 ? 132.127 126.673 171.677 1.00 41.36 ?  600 ARG B O     1 
ATOM   10362 C  CB    . ARG B 1 600 ? 129.451 124.891 172.528 1.00 38.87 ?  600 ARG B CB    1 
ATOM   10363 C  CG    . ARG B 1 600 ? 128.132 125.337 173.116 1.00 39.64 ?  600 ARG B CG    1 
ATOM   10364 C  CD    . ARG B 1 600 ? 127.860 124.647 174.430 1.00 36.65 ?  600 ARG B CD    1 
ATOM   10365 N  NE    . ARG B 1 600 ? 126.547 124.982 174.965 1.00 36.86 ?  600 ARG B NE    1 
ATOM   10366 C  CZ    . ARG B 1 600 ? 125.418 124.392 174.600 1.00 40.58 ?  600 ARG B CZ    1 
ATOM   10367 N  NH1   . ARG B 1 600 ? 125.403 123.435 173.687 1.00 39.73 1  600 ARG B NH1   1 
ATOM   10368 N  NH2   . ARG B 1 600 ? 124.276 124.770 175.166 1.00 41.50 ?  600 ARG B NH2   1 
ATOM   10369 N  N     . ILE B 1 601 ? 131.986 124.658 170.694 1.00 49.15 ?  601 ILE B N     1 
ATOM   10370 C  CA    . ILE B 1 601 ? 133.414 124.531 170.441 1.00 43.12 ?  601 ILE B CA    1 
ATOM   10371 C  C     . ILE B 1 601 ? 133.604 124.271 168.957 1.00 43.56 ?  601 ILE B C     1 
ATOM   10372 O  O     . ILE B 1 601 ? 132.999 123.347 168.400 1.00 46.37 ?  601 ILE B O     1 
ATOM   10373 C  CB    . ILE B 1 601 ? 134.048 123.414 171.288 1.00 40.56 ?  601 ILE B CB    1 
ATOM   10374 C  CG1   . ILE B 1 601 ? 133.765 123.658 172.770 1.00 42.38 ?  601 ILE B CG1   1 
ATOM   10375 C  CG2   . ILE B 1 601 ? 135.540 123.351 171.033 1.00 41.67 ?  601 ILE B CG2   1 
ATOM   10376 C  CD1   . ILE B 1 601 ? 133.935 122.443 173.639 1.00 44.89 ?  601 ILE B CD1   1 
ATOM   10377 N  N     . GLU B 1 602 ? 134.439 125.082 168.321 1.00 53.69 ?  602 GLU B N     1 
ATOM   10378 C  CA    . GLU B 1 602 ? 134.596 125.079 166.875 1.00 50.17 ?  602 GLU B CA    1 
ATOM   10379 C  C     . GLU B 1 602 ? 135.742 124.152 166.492 1.00 53.61 ?  602 GLU B C     1 
ATOM   10380 O  O     . GLU B 1 602 ? 136.889 124.380 166.890 1.00 57.39 ?  602 GLU B O     1 
ATOM   10381 C  CB    . GLU B 1 602 ? 134.852 126.499 166.373 1.00 50.44 ?  602 GLU B CB    1 
ATOM   10382 C  CG    . GLU B 1 602 ? 134.508 126.731 164.925 1.00 50.20 ?  602 GLU B CG    1 
ATOM   10383 C  CD    . GLU B 1 602 ? 134.528 128.200 164.559 1.00 56.99 ?  602 GLU B CD    1 
ATOM   10384 O  OE1   . GLU B 1 602 ? 133.724 128.966 165.129 1.00 55.91 ?  602 GLU B OE1   1 
ATOM   10385 O  OE2   . GLU B 1 602 ? 135.351 128.587 163.704 1.00 58.72 -1 602 GLU B OE2   1 
ATOM   10386 N  N     . GLU B 1 603 ? 135.431 123.111 165.724 1.00 56.22 ?  603 GLU B N     1 
ATOM   10387 C  CA    . GLU B 1 603 ? 136.423 122.153 165.251 1.00 55.13 ?  603 GLU B CA    1 
ATOM   10388 C  C     . GLU B 1 603 ? 136.774 122.477 163.804 1.00 57.66 ?  603 GLU B C     1 
ATOM   10389 O  O     . GLU B 1 603 ? 135.917 122.382 162.918 1.00 59.08 ?  603 GLU B O     1 
ATOM   10390 C  CB    . GLU B 1 603 ? 135.902 120.720 165.364 1.00 58.25 ?  603 GLU B CB    1 
ATOM   10391 C  CG    . GLU B 1 603 ? 135.367 120.347 166.736 1.00 60.56 ?  603 GLU B CG    1 
ATOM   10392 C  CD    . GLU B 1 603 ? 133.864 120.515 166.845 1.00 60.85 ?  603 GLU B CD    1 
ATOM   10393 O  OE1   . GLU B 1 603 ? 133.198 120.637 165.795 1.00 54.69 ?  603 GLU B OE1   1 
ATOM   10394 O  OE2   . GLU B 1 603 ? 133.347 120.521 167.983 1.00 59.56 -1 603 GLU B OE2   1 
ATOM   10395 N  N     . ARG B 1 604 ? 138.028 122.856 163.570 1.00 60.93 ?  604 ARG B N     1 
ATOM   10396 C  CA    . ARG B 1 604 ? 138.509 123.206 162.243 1.00 61.64 ?  604 ARG B CA    1 
ATOM   10397 C  C     . ARG B 1 604 ? 139.874 122.581 161.998 1.00 62.36 ?  604 ARG B C     1 
ATOM   10398 O  O     . ARG B 1 604 ? 140.630 122.311 162.933 1.00 61.58 ?  604 ARG B O     1 
ATOM   10399 C  CB    . ARG B 1 604 ? 138.590 124.728 162.057 1.00 61.50 ?  604 ARG B CB    1 
ATOM   10400 C  CG    . ARG B 1 604 ? 137.252 125.433 162.163 1.00 61.72 ?  604 ARG B CG    1 
ATOM   10401 C  CD    . ARG B 1 604 ? 136.563 125.453 160.804 1.00 61.06 ?  604 ARG B CD    1 
ATOM   10402 N  NE    . ARG B 1 604 ? 135.526 126.474 160.715 1.00 64.58 ?  604 ARG B NE    1 
ATOM   10403 C  CZ    . ARG B 1 604 ? 134.371 126.434 161.365 1.00 62.16 ?  604 ARG B CZ    1 
ATOM   10404 N  NH1   . ARG B 1 604 ? 134.023 125.385 162.092 1.00 59.27 1  604 ARG B NH1   1 
ATOM   10405 N  NH2   . ARG B 1 604 ? 133.534 127.463 161.264 1.00 60.26 ?  604 ARG B NH2   1 
ATOM   10406 N  N     . THR B 1 605 ? 140.175 122.353 160.723 1.00 68.88 ?  605 THR B N     1 
ATOM   10407 C  CA    . THR B 1 605 ? 141.439 121.768 160.297 1.00 69.05 ?  605 THR B CA    1 
ATOM   10408 C  C     . THR B 1 605 ? 142.211 122.799 159.486 1.00 68.94 ?  605 THR B C     1 
ATOM   10409 O  O     . THR B 1 605 ? 141.704 123.310 158.481 1.00 68.34 ?  605 THR B O     1 
ATOM   10410 C  CB    . THR B 1 605 ? 141.207 120.504 159.469 1.00 68.77 ?  605 THR B CB    1 
ATOM   10411 O  OG1   . THR B 1 605 ? 140.556 119.513 160.275 1.00 68.65 ?  605 THR B OG1   1 
ATOM   10412 C  CG2   . THR B 1 605 ? 142.528 119.951 158.962 1.00 69.06 ?  605 THR B CG2   1 
ATOM   10413 N  N     . TYR B 1 606 ? 143.429 123.101 159.922 1.00 70.93 ?  606 TYR B N     1 
ATOM   10414 C  CA    . TYR B 1 606 ? 144.322 124.006 159.211 1.00 72.42 ?  606 TYR B CA    1 
ATOM   10415 C  C     . TYR B 1 606 ? 145.576 123.232 158.832 1.00 73.83 ?  606 TYR B C     1 
ATOM   10416 O  O     . TYR B 1 606 ? 146.250 122.674 159.705 1.00 71.71 ?  606 TYR B O     1 
ATOM   10417 C  CB    . TYR B 1 606 ? 144.663 125.227 160.066 1.00 70.45 ?  606 TYR B CB    1 
ATOM   10418 C  CG    . TYR B 1 606 ? 143.462 126.093 160.365 1.00 71.00 ?  606 TYR B CG    1 
ATOM   10419 C  CD1   . TYR B 1 606 ? 142.986 127.001 159.429 1.00 68.19 ?  606 TYR B CD1   1 
ATOM   10420 C  CD2   . TYR B 1 606 ? 142.797 125.995 161.579 1.00 71.01 ?  606 TYR B CD2   1 
ATOM   10421 C  CE1   . TYR B 1 606 ? 141.886 127.790 159.696 1.00 69.99 ?  606 TYR B CE1   1 
ATOM   10422 C  CE2   . TYR B 1 606 ? 141.697 126.778 161.856 1.00 68.85 ?  606 TYR B CE2   1 
ATOM   10423 C  CZ    . TYR B 1 606 ? 141.246 127.675 160.911 1.00 72.54 ?  606 TYR B CZ    1 
ATOM   10424 O  OH    . TYR B 1 606 ? 140.147 128.457 161.184 1.00 74.18 ?  606 TYR B OH    1 
ATOM   10425 N  N     . GLY B 1 607 ? 145.888 123.210 157.542 1.00 79.93 ?  607 GLY B N     1 
ATOM   10426 C  CA    . GLY B 1 607 ? 146.946 122.333 157.073 1.00 79.31 ?  607 GLY B CA    1 
ATOM   10427 C  C     . GLY B 1 607 ? 146.557 120.886 157.304 1.00 79.82 ?  607 GLY B C     1 
ATOM   10428 O  O     . GLY B 1 607 ? 145.451 120.454 156.964 1.00 79.29 ?  607 GLY B O     1 
ATOM   10429 N  N     . ASN B 1 608 ? 147.475 120.120 157.892 1.00 81.39 ?  608 ASN B N     1 
ATOM   10430 C  CA    . ASN B 1 608 ? 147.221 118.726 158.229 1.00 82.54 ?  608 ASN B CA    1 
ATOM   10431 C  C     . ASN B 1 608 ? 146.865 118.540 159.698 1.00 83.77 ?  608 ASN B C     1 
ATOM   10432 O  O     . ASN B 1 608 ? 146.663 117.403 160.138 1.00 83.08 ?  608 ASN B O     1 
ATOM   10433 C  CB    . ASN B 1 608 ? 148.434 117.867 157.866 1.00 83.72 ?  608 ASN B CB    1 
ATOM   10434 C  CG    . ASN B 1 608 ? 148.732 117.879 156.378 1.00 84.36 ?  608 ASN B CG    1 
ATOM   10435 O  OD1   . ASN B 1 608 ? 147.926 118.352 155.576 1.00 82.31 ?  608 ASN B OD1   1 
ATOM   10436 N  ND2   . ASN B 1 608 ? 149.892 117.356 156.002 1.00 83.01 ?  608 ASN B ND2   1 
ATOM   10437 N  N     . SER B 1 609 ? 146.778 119.623 160.464 1.00 76.85 ?  609 SER B N     1 
ATOM   10438 C  CA    . SER B 1 609 ? 146.492 119.564 161.889 1.00 76.36 ?  609 SER B CA    1 
ATOM   10439 C  C     . SER B 1 609 ? 145.123 120.166 162.176 1.00 74.44 ?  609 SER B C     1 
ATOM   10440 O  O     . SER B 1 609 ? 144.774 121.224 161.643 1.00 74.33 ?  609 SER B O     1 
ATOM   10441 C  CB    . SER B 1 609 ? 147.567 120.300 162.694 1.00 73.85 ?  609 SER B CB    1 
ATOM   10442 O  OG    . SER B 1 609 ? 147.586 121.681 162.375 1.00 73.50 ?  609 SER B OG    1 
ATOM   10443 N  N     . LYS B 1 610 ? 144.353 119.483 163.017 1.00 64.40 ?  610 LYS B N     1 
ATOM   10444 C  CA    . LYS B 1 610 ? 143.024 119.936 163.399 1.00 63.80 ?  610 LYS B CA    1 
ATOM   10445 C  C     . LYS B 1 610 ? 143.093 120.809 164.646 1.00 63.31 ?  610 LYS B C     1 
ATOM   10446 O  O     . LYS B 1 610 ? 143.888 120.557 165.556 1.00 64.06 ?  610 LYS B O     1 
ATOM   10447 C  CB    . LYS B 1 610 ? 142.099 118.733 163.611 1.00 64.70 ?  610 LYS B CB    1 
ATOM   10448 C  CG    . LYS B 1 610 ? 142.026 118.193 165.029 1.00 63.25 ?  610 LYS B CG    1 
ATOM   10449 C  CD    . LYS B 1 610 ? 141.467 116.777 165.029 1.00 64.78 ?  610 LYS B CD    1 
ATOM   10450 C  CE    . LYS B 1 610 ? 142.112 115.916 166.105 1.00 64.56 ?  610 LYS B CE    1 
ATOM   10451 N  NZ    . LYS B 1 610 ? 141.659 116.266 167.475 1.00 64.14 1  610 LYS B NZ    1 
ATOM   10452 N  N     . THR B 1 611 ? 142.276 121.858 164.663 1.00 63.68 ?  611 THR B N     1 
ATOM   10453 C  CA    . THR B 1 611 ? 142.281 122.848 165.728 1.00 61.02 ?  611 THR B CA    1 
ATOM   10454 C  C     . THR B 1 611 ? 140.905 122.927 166.375 1.00 56.76 ?  611 THR B C     1 
ATOM   10455 O  O     . THR B 1 611 ? 139.886 122.632 165.743 1.00 60.25 ?  611 THR B O     1 
ATOM   10456 C  CB    . THR B 1 611 ? 142.684 124.232 165.203 1.00 61.00 ?  611 THR B CB    1 
ATOM   10457 O  OG1   . THR B 1 611 ? 143.653 124.086 164.158 1.00 61.18 ?  611 THR B OG1   1 
ATOM   10458 C  CG2   . THR B 1 611 ? 143.287 125.059 166.316 1.00 60.84 ?  611 THR B CG2   1 
ATOM   10459 N  N     . TYR B 1 612 ? 140.885 123.329 167.643 1.00 51.00 ?  612 TYR B N     1 
ATOM   10460 C  CA    . TYR B 1 612 ? 139.659 123.448 168.420 1.00 52.40 ?  612 TYR B CA    1 
ATOM   10461 C  C     . TYR B 1 612 ? 139.533 124.870 168.938 1.00 54.60 ?  612 TYR B C     1 
ATOM   10462 O  O     . TYR B 1 612 ? 140.479 125.410 169.521 1.00 53.52 ?  612 TYR B O     1 
ATOM   10463 C  CB    . TYR B 1 612 ? 139.658 122.453 169.579 1.00 54.04 ?  612 TYR B CB    1 
ATOM   10464 C  CG    . TYR B 1 612 ? 139.612 121.020 169.116 1.00 57.49 ?  612 TYR B CG    1 
ATOM   10465 C  CD1   . TYR B 1 612 ? 138.528 120.538 168.396 1.00 55.55 ?  612 TYR B CD1   1 
ATOM   10466 C  CD2   . TYR B 1 612 ? 140.667 120.156 169.369 1.00 56.40 ?  612 TYR B CD2   1 
ATOM   10467 C  CE1   . TYR B 1 612 ? 138.486 119.230 167.961 1.00 54.86 ?  612 TYR B CE1   1 
ATOM   10468 C  CE2   . TYR B 1 612 ? 140.636 118.849 168.935 1.00 59.31 ?  612 TYR B CE2   1 
ATOM   10469 C  CZ    . TYR B 1 612 ? 139.542 118.390 168.233 1.00 59.22 ?  612 TYR B CZ    1 
ATOM   10470 O  OH    . TYR B 1 612 ? 139.506 117.085 167.801 1.00 60.84 ?  612 TYR B OH    1 
ATOM   10471 N  N     . TYR B 1 613 ? 138.367 125.474 168.726 1.00 51.35 ?  613 TYR B N     1 
ATOM   10472 C  CA    . TYR B 1 613 ? 138.110 126.852 169.142 1.00 45.38 ?  613 TYR B CA    1 
ATOM   10473 C  C     . TYR B 1 613 ? 136.840 126.917 169.978 1.00 43.07 ?  613 TYR B C     1 
ATOM   10474 O  O     . TYR B 1 613 ? 135.731 126.985 169.422 1.00 43.80 ?  613 TYR B O     1 
ATOM   10475 C  CB    . TYR B 1 613 ? 138.002 127.778 167.938 1.00 42.88 ?  613 TYR B CB    1 
ATOM   10476 C  CG    . TYR B 1 613 ? 137.699 129.212 168.306 1.00 43.43 ?  613 TYR B CG    1 
ATOM   10477 C  CD1   . TYR B 1 613 ? 138.462 129.880 169.255 1.00 42.09 ?  613 TYR B CD1   1 
ATOM   10478 C  CD2   . TYR B 1 613 ? 136.653 129.896 167.706 1.00 45.50 ?  613 TYR B CD2   1 
ATOM   10479 C  CE1   . TYR B 1 613 ? 138.189 131.188 169.593 1.00 44.64 ?  613 TYR B CE1   1 
ATOM   10480 C  CE2   . TYR B 1 613 ? 136.373 131.205 168.039 1.00 45.24 ?  613 TYR B CE2   1 
ATOM   10481 C  CZ    . TYR B 1 613 ? 137.145 131.846 168.982 1.00 48.46 ?  613 TYR B CZ    1 
ATOM   10482 O  OH    . TYR B 1 613 ? 136.869 133.151 169.316 1.00 47.39 ?  613 TYR B OH    1 
ATOM   10483 N  N     . PRO B 1 614 ? 136.953 126.893 171.302 1.00 39.22 ?  614 PRO B N     1 
ATOM   10484 C  CA    . PRO B 1 614 ? 135.782 127.166 172.137 1.00 42.67 ?  614 PRO B CA    1 
ATOM   10485 C  C     . PRO B 1 614 ? 135.318 128.600 171.947 1.00 41.86 ?  614 PRO B C     1 
ATOM   10486 O  O     . PRO B 1 614 ? 136.112 129.501 171.665 1.00 42.89 ?  614 PRO B O     1 
ATOM   10487 C  CB    . PRO B 1 614 ? 136.291 126.931 173.566 1.00 39.16 ?  614 PRO B CB    1 
ATOM   10488 C  CG    . PRO B 1 614 ? 137.612 126.240 173.416 1.00 42.11 ?  614 PRO B CG    1 
ATOM   10489 C  CD    . PRO B 1 614 ? 138.165 126.675 172.104 1.00 40.31 ?  614 PRO B CD    1 
ATOM   10490 N  N     . MET B 1 615 ? 134.016 128.805 172.095 1.00 40.49 ?  615 MET B N     1 
ATOM   10491 C  CA    . MET B 1 615 ? 133.476 130.146 171.953 1.00 40.16 ?  615 MET B CA    1 
ATOM   10492 C  C     . MET B 1 615 ? 134.031 131.048 173.053 1.00 44.34 ?  615 MET B C     1 
ATOM   10493 O  O     . MET B 1 615 ? 134.274 130.584 174.173 1.00 42.90 ?  615 MET B O     1 
ATOM   10494 C  CB    . MET B 1 615 ? 131.948 130.120 171.992 1.00 38.52 ?  615 MET B CB    1 
ATOM   10495 C  CG    . MET B 1 615 ? 131.333 129.717 170.663 1.00 41.18 ?  615 MET B CG    1 
ATOM   10496 S  SD    . MET B 1 615 ? 132.398 130.196 169.287 1.00 52.06 ?  615 MET B SD    1 
ATOM   10497 C  CE    . MET B 1 615 ? 131.423 129.684 167.879 1.00 41.46 ?  615 MET B CE    1 
ATOM   10498 N  N     . PRO B 1 616 ? 134.269 132.325 172.762 1.00 45.96 ?  616 PRO B N     1 
ATOM   10499 C  CA    . PRO B 1 616 ? 134.954 133.193 173.730 1.00 39.83 ?  616 PRO B CA    1 
ATOM   10500 C  C     . PRO B 1 616 ? 134.175 133.312 175.030 1.00 41.31 ?  616 PRO B C     1 
ATOM   10501 O  O     . PRO B 1 616 ? 132.997 133.675 175.038 1.00 42.63 ?  616 PRO B O     1 
ATOM   10502 C  CB    . PRO B 1 616 ? 135.041 134.537 173.000 1.00 36.23 ?  616 PRO B CB    1 
ATOM   10503 C  CG    . PRO B 1 616 ? 134.857 134.205 171.558 1.00 41.50 ?  616 PRO B CG    1 
ATOM   10504 C  CD    . PRO B 1 616 ? 133.944 133.036 171.515 1.00 40.52 ?  616 PRO B CD    1 
ATOM   10505 N  N     . GLY B 1 617 ? 134.851 133.012 176.134 1.00 40.43 ?  617 GLY B N     1 
ATOM   10506 C  CA    . GLY B 1 617 ? 134.228 133.024 177.437 1.00 36.58 ?  617 GLY B CA    1 
ATOM   10507 C  C     . GLY B 1 617 ? 133.498 131.756 177.813 1.00 41.88 ?  617 GLY B C     1 
ATOM   10508 O  O     . GLY B 1 617 ? 132.863 131.721 178.874 1.00 45.55 ?  617 GLY B O     1 
ATOM   10509 N  N     . LEU B 1 618 ? 133.563 130.718 176.983 1.00 44.70 ?  618 LEU B N     1 
ATOM   10510 C  CA    . LEU B 1 618 ? 132.912 129.457 177.309 1.00 38.50 ?  618 LEU B CA    1 
ATOM   10511 C  C     . LEU B 1 618 ? 133.581 128.809 178.513 1.00 39.94 ?  618 LEU B C     1 
ATOM   10512 O  O     . LEU B 1 618 ? 134.809 128.759 178.613 1.00 44.64 ?  618 LEU B O     1 
ATOM   10513 C  CB    . LEU B 1 618 ? 132.955 128.508 176.113 1.00 38.04 ?  618 LEU B CB    1 
ATOM   10514 C  CG    . LEU B 1 618 ? 132.223 127.174 176.253 1.00 40.00 ?  618 LEU B CG    1 
ATOM   10515 C  CD1   . LEU B 1 618 ? 130.745 127.396 176.502 1.00 41.29 ?  618 LEU B CD1   1 
ATOM   10516 C  CD2   . LEU B 1 618 ? 132.436 126.323 175.017 1.00 40.82 ?  618 LEU B CD2   1 
ATOM   10517 N  N     . ALA B 1 619 ? 132.759 128.313 179.430 1.00 47.78 ?  619 ALA B N     1 
ATOM   10518 C  CA    . ALA B 1 619 ? 133.237 127.653 180.635 1.00 47.23 ?  619 ALA B CA    1 
ATOM   10519 C  C     . ALA B 1 619 ? 132.155 126.692 181.105 1.00 49.90 ?  619 ALA B C     1 
ATOM   10520 O  O     . ALA B 1 619 ? 131.197 126.405 180.381 1.00 54.00 ?  619 ALA B O     1 
ATOM   10521 C  CB    . ALA B 1 619 ? 133.611 128.683 181.707 1.00 46.77 ?  619 ALA B CB    1 
ATOM   10522 N  N     . SER B 1 620 ? 132.311 126.182 182.325 1.00 56.15 ?  620 SER B N     1 
ATOM   10523 C  CA    . SER B 1 620 ? 131.300 125.296 182.888 1.00 55.66 ?  620 SER B CA    1 
ATOM   10524 C  C     . SER B 1 620 ? 130.083 126.074 183.377 1.00 55.44 ?  620 SER B C     1 
ATOM   10525 O  O     . SER B 1 620 ? 128.950 125.596 183.257 1.00 57.57 ?  620 SER B O     1 
ATOM   10526 C  CB    . SER B 1 620 ? 131.902 124.474 184.028 1.00 57.26 ?  620 SER B CB    1 
ATOM   10527 O  OG    . SER B 1 620 ? 133.123 123.880 183.629 1.00 59.15 ?  620 SER B OG    1 
ATOM   10528 N  N     . ASN B 1 621 ? 130.300 127.271 183.926 1.00 50.85 ?  621 ASN B N     1 
ATOM   10529 C  CA    . ASN B 1 621 ? 129.194 128.033 184.499 1.00 52.15 ?  621 ASN B CA    1 
ATOM   10530 C  C     . ASN B 1 621 ? 128.273 128.589 183.418 1.00 54.39 ?  621 ASN B C     1 
ATOM   10531 O  O     . ASN B 1 621 ? 127.053 128.654 183.611 1.00 56.25 ?  621 ASN B O     1 
ATOM   10532 C  CB    . ASN B 1 621 ? 129.734 129.160 185.381 1.00 53.65 ?  621 ASN B CB    1 
ATOM   10533 C  CG    . ASN B 1 621 ? 130.506 130.201 184.593 1.00 57.66 ?  621 ASN B CG    1 
ATOM   10534 O  OD1   . ASN B 1 621 ? 131.536 129.903 183.989 1.00 59.16 ?  621 ASN B OD1   1 
ATOM   10535 N  ND2   . ASN B 1 621 ? 130.011 131.434 184.598 1.00 55.87 ?  621 ASN B ND2   1 
ATOM   10536 N  N     . ASN B 1 622 ? 128.831 128.994 182.277 1.00 46.91 ?  622 ASN B N     1 
ATOM   10537 C  CA    . ASN B 1 622 ? 128.052 129.584 181.195 1.00 45.83 ?  622 ASN B CA    1 
ATOM   10538 C  C     . ASN B 1 622 ? 127.915 128.649 179.999 1.00 47.47 ?  622 ASN B C     1 
ATOM   10539 O  O     . ASN B 1 622 ? 127.680 129.113 178.880 1.00 53.86 ?  622 ASN B O     1 
ATOM   10540 C  CB    . ASN B 1 622 ? 128.662 130.923 180.770 1.00 46.81 ?  622 ASN B CB    1 
ATOM   10541 C  CG    . ASN B 1 622 ? 130.078 130.790 180.225 1.00 46.56 ?  622 ASN B CG    1 
ATOM   10542 O  OD1   . ASN B 1 622 ? 130.545 129.696 179.913 1.00 52.25 ?  622 ASN B OD1   1 
ATOM   10543 N  ND2   . ASN B 1 622 ? 130.768 131.916 180.113 1.00 43.47 ?  622 ASN B ND2   1 
ATOM   10544 N  N     . TRP B 1 623 ? 128.066 127.341 180.213 1.00 41.95 ?  623 TRP B N     1 
ATOM   10545 C  CA    . TRP B 1 623 ? 128.015 126.397 179.102 1.00 40.84 ?  623 TRP B CA    1 
ATOM   10546 C  C     . TRP B 1 623 ? 126.647 126.397 178.431 1.00 42.27 ?  623 TRP B C     1 
ATOM   10547 O  O     . TRP B 1 623 ? 126.554 126.387 177.198 1.00 42.30 ?  623 TRP B O     1 
ATOM   10548 C  CB    . TRP B 1 623 ? 128.369 124.993 179.593 1.00 45.73 ?  623 TRP B CB    1 
ATOM   10549 C  CG    . TRP B 1 623 ? 128.160 123.920 178.569 1.00 43.63 ?  623 TRP B CG    1 
ATOM   10550 C  CD1   . TRP B 1 623 ? 127.019 123.207 178.351 1.00 40.76 ?  623 TRP B CD1   1 
ATOM   10551 C  CD2   . TRP B 1 623 ? 129.121 123.436 177.625 1.00 42.24 ?  623 TRP B CD2   1 
ATOM   10552 N  NE1   . TRP B 1 623 ? 127.209 122.310 177.331 1.00 42.99 ?  623 TRP B NE1   1 
ATOM   10553 C  CE2   . TRP B 1 623 ? 128.492 122.429 176.869 1.00 40.39 ?  623 TRP B CE2   1 
ATOM   10554 C  CE3   . TRP B 1 623 ? 130.454 123.755 177.349 1.00 39.81 ?  623 TRP B CE3   1 
ATOM   10555 C  CZ2   . TRP B 1 623 ? 129.149 121.741 175.852 1.00 38.39 ?  623 TRP B CZ2   1 
ATOM   10556 C  CZ3   . TRP B 1 623 ? 131.102 123.071 176.339 1.00 42.86 ?  623 TRP B CZ3   1 
ATOM   10557 C  CH2   . TRP B 1 623 ? 130.449 122.076 175.602 1.00 42.62 ?  623 TRP B CH2   1 
ATOM   10558 N  N     . PHE B 1 624 ? 125.576 126.411 179.220 1.00 48.20 ?  624 PHE B N     1 
ATOM   10559 C  CA    . PHE B 1 624 ? 124.234 126.317 178.666 1.00 45.50 ?  624 PHE B CA    1 
ATOM   10560 C  C     . PHE B 1 624 ? 123.654 127.664 178.259 1.00 45.25 ?  624 PHE B C     1 
ATOM   10561 O  O     . PHE B 1 624 ? 122.605 127.696 177.607 1.00 52.40 ?  624 PHE B O     1 
ATOM   10562 C  CB    . PHE B 1 624 ? 123.301 125.626 179.664 1.00 49.11 ?  624 PHE B CB    1 
ATOM   10563 C  CG    . PHE B 1 624 ? 123.505 124.140 179.740 1.00 50.34 ?  624 PHE B CG    1 
ATOM   10564 C  CD1   . PHE B 1 624 ? 123.104 123.320 178.698 1.00 44.39 ?  624 PHE B CD1   1 
ATOM   10565 C  CD2   . PHE B 1 624 ? 124.112 123.565 180.843 1.00 48.19 ?  624 PHE B CD2   1 
ATOM   10566 C  CE1   . PHE B 1 624 ? 123.295 121.955 178.759 1.00 44.64 ?  624 PHE B CE1   1 
ATOM   10567 C  CE2   . PHE B 1 624 ? 124.307 122.200 180.910 1.00 49.33 ?  624 PHE B CE2   1 
ATOM   10568 C  CZ    . PHE B 1 624 ? 123.897 121.393 179.867 1.00 48.15 ?  624 PHE B CZ    1 
ATOM   10569 N  N     . PHE B 1 625 ? 124.303 128.770 178.620 1.00 39.83 ?  625 PHE B N     1 
ATOM   10570 C  CA    . PHE B 1 625 ? 123.952 130.054 178.030 1.00 37.08 ?  625 PHE B CA    1 
ATOM   10571 C  C     . PHE B 1 625 ? 124.526 130.212 176.633 1.00 36.39 ?  625 PHE B C     1 
ATOM   10572 O  O     . PHE B 1 625 ? 124.047 131.055 175.869 1.00 41.33 ?  625 PHE B O     1 
ATOM   10573 C  CB    . PHE B 1 625 ? 124.427 131.202 178.920 1.00 32.77 ?  625 PHE B CB    1 
ATOM   10574 C  CG    . PHE B 1 625 ? 123.632 131.356 180.181 1.00 35.96 ?  625 PHE B CG    1 
ATOM   10575 C  CD1   . PHE B 1 625 ? 122.303 131.736 180.131 1.00 37.62 ?  625 PHE B CD1   1 
ATOM   10576 C  CD2   . PHE B 1 625 ? 124.212 131.124 181.416 1.00 37.97 ?  625 PHE B CD2   1 
ATOM   10577 C  CE1   . PHE B 1 625 ? 121.566 131.881 181.289 1.00 40.00 ?  625 PHE B CE1   1 
ATOM   10578 C  CE2   . PHE B 1 625 ? 123.480 131.269 182.577 1.00 37.58 ?  625 PHE B CE2   1 
ATOM   10579 C  CZ    . PHE B 1 625 ? 122.156 131.648 182.513 1.00 40.99 ?  625 PHE B CZ    1 
ATOM   10580 N  N     . TYR B 1 626 ? 125.535 129.420 176.283 1.00 29.50 ?  626 TYR B N     1 
ATOM   10581 C  CA    . TYR B 1 626 ? 126.067 129.384 174.924 1.00 33.44 ?  626 TYR B CA    1 
ATOM   10582 C  C     . TYR B 1 626 ? 125.297 128.385 174.069 1.00 30.15 ?  626 TYR B C     1 
ATOM   10583 O  O     . TYR B 1 626 ? 125.870 127.509 173.427 1.00 36.11 ?  626 TYR B O     1 
ATOM   10584 C  CB    . TYR B 1 626 ? 127.551 129.045 174.956 1.00 32.29 ?  626 TYR B CB    1 
ATOM   10585 C  CG    . TYR B 1 626 ? 128.447 130.251 175.080 1.00 34.18 ?  626 TYR B CG    1 
ATOM   10586 C  CD1   . TYR B 1 626 ? 128.697 131.069 173.988 1.00 35.39 ?  626 TYR B CD1   1 
ATOM   10587 C  CD2   . TYR B 1 626 ? 129.043 130.573 176.291 1.00 34.34 ?  626 TYR B CD2   1 
ATOM   10588 C  CE1   . TYR B 1 626 ? 129.515 132.172 174.098 1.00 35.36 ?  626 TYR B CE1   1 
ATOM   10589 C  CE2   . TYR B 1 626 ? 129.861 131.675 176.410 1.00 31.69 ?  626 TYR B CE2   1 
ATOM   10590 C  CZ    . TYR B 1 626 ? 130.094 132.470 175.311 1.00 30.87 ?  626 TYR B CZ    1 
ATOM   10591 O  OH    . TYR B 1 626 ? 130.906 133.569 175.423 1.00 38.82 ?  626 TYR B OH    1 
ATOM   10592 N  N     . LYS B 1 627 ? 123.975 128.519 174.067 1.00 33.87 ?  627 LYS B N     1 
ATOM   10593 C  CA    . LYS B 1 627 ? 123.126 127.612 173.310 1.00 34.18 ?  627 LYS B CA    1 
ATOM   10594 C  C     . LYS B 1 627 ? 123.425 127.729 171.822 1.00 37.69 ?  627 LYS B C     1 
ATOM   10595 O  O     . LYS B 1 627 ? 123.548 128.834 171.286 1.00 44.50 ?  627 LYS B O     1 
ATOM   10596 C  CB    . LYS B 1 627 ? 121.658 127.925 173.595 1.00 37.36 ?  627 LYS B CB    1 
ATOM   10597 C  CG    . LYS B 1 627 ? 120.664 126.971 172.968 1.00 37.26 ?  627 LYS B CG    1 
ATOM   10598 C  CD    . LYS B 1 627 ? 119.272 127.223 173.520 1.00 32.29 ?  627 LYS B CD    1 
ATOM   10599 C  CE    . LYS B 1 627 ? 118.245 126.316 172.877 1.00 39.91 ?  627 LYS B CE    1 
ATOM   10600 N  NZ    . LYS B 1 627 ? 116.883 126.559 173.422 1.00 41.71 1  627 LYS B NZ    1 
ATOM   10601 N  N     . GLU B 1 628 ? 123.561 126.587 171.158 1.00 39.03 ?  628 GLU B N     1 
ATOM   10602 C  CA    . GLU B 1 628 ? 123.863 126.593 169.736 1.00 35.29 ?  628 GLU B CA    1 
ATOM   10603 C  C     . GLU B 1 628 ? 122.677 127.126 168.942 1.00 40.27 ?  628 GLU B C     1 
ATOM   10604 O  O     . GLU B 1 628 ? 121.517 126.972 169.333 1.00 45.56 ?  628 GLU B O     1 
ATOM   10605 C  CB    . GLU B 1 628 ? 124.237 125.191 169.261 1.00 39.70 ?  628 GLU B CB    1 
ATOM   10606 C  CG    . GLU B 1 628 ? 125.394 124.575 170.028 1.00 41.43 ?  628 GLU B CG    1 
ATOM   10607 C  CD    . GLU B 1 628 ? 126.133 123.525 169.226 1.00 47.84 ?  628 GLU B CD    1 
ATOM   10608 O  OE1   . GLU B 1 628 ? 125.608 123.103 168.173 1.00 43.73 ?  628 GLU B OE1   1 
ATOM   10609 O  OE2   . GLU B 1 628 ? 127.238 123.123 169.644 1.00 45.74 -1 628 GLU B OE2   1 
ATOM   10610 N  N     . ALA B 1 629 ? 122.987 127.769 167.814 1.00 41.50 ?  629 ALA B N     1 
ATOM   10611 C  CA    . ALA B 1 629 ? 121.954 128.425 167.019 1.00 32.10 ?  629 ALA B CA    1 
ATOM   10612 C  C     . ALA B 1 629 ? 120.930 127.427 166.497 1.00 37.00 ?  629 ALA B C     1 
ATOM   10613 O  O     . ALA B 1 629 ? 119.732 127.728 166.441 1.00 44.16 ?  629 ALA B O     1 
ATOM   10614 C  CB    . ALA B 1 629 ? 122.597 129.191 165.865 1.00 30.45 ?  629 ALA B CB    1 
ATOM   10615 N  N     . TYR B 1 630 ? 121.381 126.236 166.100 1.00 40.68 ?  630 TYR B N     1 
ATOM   10616 C  CA    . TYR B 1 630 ? 120.458 125.236 165.572 1.00 39.14 ?  630 TYR B CA    1 
ATOM   10617 C  C     . TYR B 1 630 ? 119.486 124.745 166.637 1.00 42.65 ?  630 TYR B C     1 
ATOM   10618 O  O     . TYR B 1 630 ? 118.331 124.435 166.324 1.00 49.05 ?  630 TYR B O     1 
ATOM   10619 C  CB    . TYR B 1 630 ? 121.240 124.068 164.980 1.00 37.55 ?  630 TYR B CB    1 
ATOM   10620 C  CG    . TYR B 1 630 ? 122.208 124.484 163.900 1.00 37.64 ?  630 TYR B CG    1 
ATOM   10621 C  CD1   . TYR B 1 630 ? 121.778 124.684 162.597 1.00 38.02 ?  630 TYR B CD1   1 
ATOM   10622 C  CD2   . TYR B 1 630 ? 123.550 124.686 164.185 1.00 37.73 ?  630 TYR B CD2   1 
ATOM   10623 C  CE1   . TYR B 1 630 ? 122.657 125.067 161.607 1.00 38.57 ?  630 TYR B CE1   1 
ATOM   10624 C  CE2   . TYR B 1 630 ? 124.437 125.069 163.201 1.00 40.36 ?  630 TYR B CE2   1 
ATOM   10625 C  CZ    . TYR B 1 630 ? 123.985 125.258 161.914 1.00 45.55 ?  630 TYR B CZ    1 
ATOM   10626 O  OH    . TYR B 1 630 ? 124.865 125.639 160.929 1.00 51.53 ?  630 TYR B OH    1 
ATOM   10627 N  N     . ASP B 1 631 ? 119.926 124.668 167.893 1.00 42.26 ?  631 ASP B N     1 
ATOM   10628 C  CA    . ASP B 1 631 ? 119.040 124.278 168.982 1.00 37.01 ?  631 ASP B CA    1 
ATOM   10629 C  C     . ASP B 1 631 ? 118.040 125.367 169.346 1.00 43.14 ?  631 ASP B C     1 
ATOM   10630 O  O     . ASP B 1 631 ? 117.123 125.104 170.130 1.00 47.63 ?  631 ASP B O     1 
ATOM   10631 C  CB    . ASP B 1 631 ? 119.859 123.905 170.218 1.00 41.58 ?  631 ASP B CB    1 
ATOM   10632 C  CG    . ASP B 1 631 ? 120.843 122.786 169.950 1.00 48.57 ?  631 ASP B CG    1 
ATOM   10633 O  OD1   . ASP B 1 631 ? 120.515 121.880 169.156 1.00 49.25 ?  631 ASP B OD1   1 
ATOM   10634 O  OD2   . ASP B 1 631 ? 121.947 122.811 170.534 1.00 50.10 -1 631 ASP B OD2   1 
ATOM   10635 N  N     . MET B 1 632 ? 118.190 126.566 168.799 1.00 37.56 ?  632 MET B N     1 
ATOM   10636 C  CA    . MET B 1 632 ? 117.366 127.703 169.174 1.00 38.15 ?  632 MET B CA    1 
ATOM   10637 C  C     . MET B 1 632 ? 116.065 127.727 168.382 1.00 37.21 ?  632 MET B C     1 
ATOM   10638 O  O     . MET B 1 632 ? 115.931 127.099 167.329 1.00 36.18 ?  632 MET B O     1 
ATOM   10639 C  CB    . MET B 1 632 ? 118.123 129.010 168.948 1.00 36.52 ?  632 MET B CB    1 
ATOM   10640 C  CG    . MET B 1 632 ? 118.781 129.567 170.187 1.00 35.34 ?  632 MET B CG    1 
ATOM   10641 S  SD    . MET B 1 632 ? 120.169 130.634 169.800 1.00 45.68 ?  632 MET B SD    1 
ATOM   10642 C  CE    . MET B 1 632 ? 120.992 130.688 171.384 1.00 33.51 ?  632 MET B CE    1 
ATOM   10643 N  N     . ASP B 1 633 ? 115.098 128.473 168.910 1.00 37.50 ?  633 ASP B N     1 
ATOM   10644 C  CA    . ASP B 1 633 ? 113.860 128.745 168.194 1.00 33.40 ?  633 ASP B CA    1 
ATOM   10645 C  C     . ASP B 1 633 ? 114.091 129.912 167.244 1.00 36.19 ?  633 ASP B C     1 
ATOM   10646 O  O     . ASP B 1 633 ? 114.375 131.030 167.687 1.00 43.42 ?  633 ASP B O     1 
ATOM   10647 C  CB    . ASP B 1 633 ? 112.734 129.060 169.176 1.00 30.86 ?  633 ASP B CB    1 
ATOM   10648 C  CG    . ASP B 1 633 ? 111.388 129.209 168.495 1.00 40.37 ?  633 ASP B CG    1 
ATOM   10649 O  OD1   . ASP B 1 633 ? 111.279 128.867 167.299 1.00 43.37 ?  633 ASP B OD1   1 
ATOM   10650 O  OD2   . ASP B 1 633 ? 110.438 129.672 169.157 1.00 41.05 -1 633 ASP B OD2   1 
ATOM   10651 N  N     . MET B 1 634 ? 113.977 129.653 165.940 1.00 30.22 ?  634 MET B N     1 
ATOM   10652 C  CA    . MET B 1 634 ? 114.226 130.701 164.957 1.00 23.54 ?  634 MET B CA    1 
ATOM   10653 C  C     . MET B 1 634 ? 113.242 131.854 165.076 1.00 26.50 ?  634 MET B C     1 
ATOM   10654 O  O     . MET B 1 634 ? 113.561 132.966 164.645 1.00 31.39 ?  634 MET B O     1 
ATOM   10655 C  CB    . MET B 1 634 ? 114.185 130.122 163.543 1.00 26.08 ?  634 MET B CB    1 
ATOM   10656 C  CG    . MET B 1 634 ? 115.479 129.455 163.119 1.00 31.31 ?  634 MET B CG    1 
ATOM   10657 S  SD    . MET B 1 634 ? 116.909 130.539 163.310 1.00 43.09 ?  634 MET B SD    1 
ATOM   10658 C  CE    . MET B 1 634 ? 117.769 129.740 164.664 1.00 29.75 ?  634 MET B CE    1 
ATOM   10659 N  N     . PHE B 1 635 ? 112.059 131.622 165.646 1.00 26.09 ?  635 PHE B N     1 
ATOM   10660 C  CA    . PHE B 1 635 ? 111.137 132.726 165.890 1.00 23.44 ?  635 PHE B CA    1 
ATOM   10661 C  C     . PHE B 1 635 ? 111.712 133.706 166.904 1.00 21.59 ?  635 PHE B C     1 
ATOM   10662 O  O     . PHE B 1 635 ? 111.593 134.924 166.738 1.00 26.28 ?  635 PHE B O     1 
ATOM   10663 C  CB    . PHE B 1 635 ? 109.787 132.188 166.364 1.00 27.07 ?  635 PHE B CB    1 
ATOM   10664 C  CG    . PHE B 1 635 ? 108.817 131.926 165.249 1.00 30.07 ?  635 PHE B CG    1 
ATOM   10665 C  CD1   . PHE B 1 635 ? 109.230 131.293 164.090 1.00 26.06 ?  635 PHE B CD1   1 
ATOM   10666 C  CD2   . PHE B 1 635 ? 107.494 132.315 165.359 1.00 25.64 ?  635 PHE B CD2   1 
ATOM   10667 C  CE1   . PHE B 1 635 ? 108.342 131.051 163.062 1.00 24.41 ?  635 PHE B CE1   1 
ATOM   10668 C  CE2   . PHE B 1 635 ? 106.601 132.076 164.333 1.00 28.30 ?  635 PHE B CE2   1 
ATOM   10669 C  CZ    . PHE B 1 635 ? 107.026 131.442 163.184 1.00 25.18 ?  635 PHE B CZ    1 
ATOM   10670 N  N     . LYS B 1 636 ? 112.355 133.195 167.954 1.00 27.48 ?  636 LYS B N     1 
ATOM   10671 C  CA    . LYS B 1 636 ? 112.960 134.077 168.945 1.00 30.38 ?  636 LYS B CA    1 
ATOM   10672 C  C     . LYS B 1 636 ? 114.190 134.787 168.392 1.00 26.86 ?  636 LYS B C     1 
ATOM   10673 O  O     . LYS B 1 636 ? 114.459 135.936 168.757 1.00 36.77 ?  636 LYS B O     1 
ATOM   10674 C  CB    . LYS B 1 636 ? 113.312 133.284 170.200 1.00 30.54 ?  636 LYS B CB    1 
ATOM   10675 C  CG    . LYS B 1 636 ? 112.119 132.593 170.836 1.00 29.29 ?  636 LYS B CG    1 
ATOM   10676 C  CD    . LYS B 1 636 ? 111.637 133.345 172.061 1.00 34.76 ?  636 LYS B CD    1 
ATOM   10677 C  CE    . LYS B 1 636 ? 110.170 133.068 172.339 1.00 33.40 ?  636 LYS B CE    1 
ATOM   10678 N  NZ    . LYS B 1 636 ? 109.394 134.324 172.522 1.00 35.79 1  636 LYS B NZ    1 
ATOM   10679 N  N     . VAL B 1 637 ? 114.941 134.129 167.508 1.00 24.28 ?  637 VAL B N     1 
ATOM   10680 C  CA    . VAL B 1 637 ? 116.052 134.802 166.841 1.00 17.58 ?  637 VAL B CA    1 
ATOM   10681 C  C     . VAL B 1 637 ? 115.529 135.911 165.937 1.00 27.32 ?  637 VAL B C     1 
ATOM   10682 O  O     . VAL B 1 637 ? 116.121 136.995 165.851 1.00 31.76 ?  637 VAL B O     1 
ATOM   10683 C  CB    . VAL B 1 637 ? 116.903 133.782 166.065 1.00 21.70 ?  637 VAL B CB    1 
ATOM   10684 C  CG1   . VAL B 1 637 ? 118.082 134.469 165.401 1.00 22.34 ?  637 VAL B CG1   1 
ATOM   10685 C  CG2   . VAL B 1 637 ? 117.376 132.677 166.993 1.00 23.89 ?  637 VAL B CG2   1 
ATOM   10686 N  N     . VAL B 1 638 ? 114.412 135.658 165.250 1.00 25.42 ?  638 VAL B N     1 
ATOM   10687 C  CA    . VAL B 1 638 ? 113.766 136.700 164.457 1.00 22.70 ?  638 VAL B CA    1 
ATOM   10688 C  C     . VAL B 1 638 ? 113.349 137.858 165.351 1.00 19.58 ?  638 VAL B C     1 
ATOM   10689 O  O     . VAL B 1 638 ? 113.504 139.029 164.990 1.00 30.46 ?  638 VAL B O     1 
ATOM   10690 C  CB    . VAL B 1 638 ? 112.561 136.124 163.690 1.00 24.93 ?  638 VAL B CB    1 
ATOM   10691 C  CG1   . VAL B 1 638 ? 111.659 137.243 163.202 1.00 14.67 ?  638 VAL B CG1   1 
ATOM   10692 C  CG2   . VAL B 1 638 ? 113.016 135.266 162.527 1.00 23.91 ?  638 VAL B CG2   1 
ATOM   10693 N  N     . ASP B 1 639 ? 112.802 137.548 166.527 1.00 17.63 ?  639 ASP B N     1 
ATOM   10694 C  CA    . ASP B 1 639 ? 112.405 138.591 167.466 1.00 21.91 ?  639 ASP B CA    1 
ATOM   10695 C  C     . ASP B 1 639 ? 113.601 139.434 167.890 1.00 26.76 ?  639 ASP B C     1 
ATOM   10696 O  O     . ASP B 1 639 ? 113.515 140.665 167.947 1.00 34.74 ?  639 ASP B O     1 
ATOM   10697 C  CB    . ASP B 1 639 ? 111.735 137.965 168.688 1.00 25.22 ?  639 ASP B CB    1 
ATOM   10698 C  CG    . ASP B 1 639 ? 110.274 137.649 168.454 1.00 36.03 ?  639 ASP B CG    1 
ATOM   10699 O  OD1   . ASP B 1 639 ? 109.629 138.362 167.659 1.00 33.39 ?  639 ASP B OD1   1 
ATOM   10700 O  OD2   . ASP B 1 639 ? 109.770 136.686 169.068 1.00 39.17 -1 639 ASP B OD2   1 
ATOM   10701 N  N     . MET B 1 640 ? 114.727 138.784 168.182 1.00 24.69 ?  640 MET B N     1 
ATOM   10702 C  CA    . MET B 1 640 ? 115.937 139.510 168.559 1.00 17.97 ?  640 MET B CA    1 
ATOM   10703 C  C     . MET B 1 640 ? 116.420 140.411 167.427 1.00 23.27 ?  640 MET B C     1 
ATOM   10704 O  O     . MET B 1 640 ? 116.736 141.588 167.645 1.00 32.90 ?  640 MET B O     1 
ATOM   10705 C  CB    . MET B 1 640 ? 117.032 138.522 168.958 1.00 22.73 ?  640 MET B CB    1 
ATOM   10706 C  CG    . MET B 1 640 ? 118.429 139.109 168.933 1.00 28.17 ?  640 MET B CG    1 
ATOM   10707 S  SD    . MET B 1 640 ? 118.740 140.179 170.344 1.00 39.52 ?  640 MET B SD    1 
ATOM   10708 C  CE    . MET B 1 640 ? 119.104 138.965 171.601 1.00 26.08 ?  640 MET B CE    1 
ATOM   10709 N  N     . ILE B 1 641 ? 116.483 139.874 166.208 1.00 28.94 ?  641 ILE B N     1 
ATOM   10710 C  CA    . ILE B 1 641 ? 116.998 140.655 165.090 1.00 21.13 ?  641 ILE B CA    1 
ATOM   10711 C  C     . ILE B 1 641 ? 116.062 141.808 164.757 1.00 19.87 ?  641 ILE B C     1 
ATOM   10712 O  O     . ILE B 1 641 ? 116.518 142.895 164.382 1.00 29.61 ?  641 ILE B O     1 
ATOM   10713 C  CB    . ILE B 1 641 ? 117.249 139.747 163.873 1.00 25.85 ?  641 ILE B CB    1 
ATOM   10714 C  CG1   . ILE B 1 641 ? 118.253 138.654 164.234 1.00 18.83 ?  641 ILE B CG1   1 
ATOM   10715 C  CG2   . ILE B 1 641 ? 117.778 140.554 162.699 1.00 18.72 ?  641 ILE B CG2   1 
ATOM   10716 C  CD1   . ILE B 1 641 ? 119.475 139.170 164.962 1.00 20.70 ?  641 ILE B CD1   1 
ATOM   10717 N  N     . ALA B 1 642 ? 114.751 141.607 164.895 1.00 17.45 ?  642 ALA B N     1 
ATOM   10718 C  CA    . ALA B 1 642 ? 113.806 142.695 164.680 1.00 20.38 ?  642 ALA B CA    1 
ATOM   10719 C  C     . ALA B 1 642 ? 113.905 143.742 165.779 1.00 21.19 ?  642 ALA B C     1 
ATOM   10720 O  O     . ALA B 1 642 ? 113.681 144.930 165.522 1.00 25.52 ?  642 ALA B O     1 
ATOM   10721 C  CB    . ALA B 1 642 ? 112.383 142.147 164.595 1.00 15.88 ?  642 ALA B CB    1 
ATOM   10722 N  N     . THR B 1 643 ? 114.220 143.323 167.005 1.00 21.94 ?  643 THR B N     1 
ATOM   10723 C  CA    . THR B 1 643 ? 114.500 144.287 168.062 1.00 18.28 ?  643 THR B CA    1 
ATOM   10724 C  C     . THR B 1 643 ? 115.722 145.129 167.721 1.00 24.19 ?  643 THR B C     1 
ATOM   10725 O  O     . THR B 1 643 ? 115.726 146.347 167.928 1.00 26.56 ?  643 THR B O     1 
ATOM   10726 C  CB    . THR B 1 643 ? 114.702 143.562 169.390 1.00 17.26 ?  643 THR B CB    1 
ATOM   10727 O  OG1   . THR B 1 643 ? 113.543 142.774 169.685 1.00 22.86 ?  643 THR B OG1   1 
ATOM   10728 C  CG2   . THR B 1 643 ? 114.929 144.556 170.508 1.00 17.83 ?  643 THR B CG2   1 
ATOM   10729 N  N     . ILE B 1 644 ? 116.773 144.493 167.203 1.00 22.78 ?  644 ILE B N     1 
ATOM   10730 C  CA    . ILE B 1 644 ? 117.955 145.240 166.788 1.00 10.33 ?  644 ILE B CA    1 
ATOM   10731 C  C     . ILE B 1 644 ? 117.665 146.057 165.534 1.00 16.72 ?  644 ILE B C     1 
ATOM   10732 O  O     . ILE B 1 644 ? 118.114 147.201 165.406 1.00 22.18 ?  644 ILE B O     1 
ATOM   10733 C  CB    . ILE B 1 644 ? 119.144 144.287 166.577 1.00 12.86 ?  644 ILE B CB    1 
ATOM   10734 C  CG1   . ILE B 1 644 ? 119.411 143.474 167.843 1.00 16.38 ?  644 ILE B CG1   1 
ATOM   10735 C  CG2   . ILE B 1 644 ? 120.381 145.065 166.181 1.00 8.54  ?  644 ILE B CG2   1 
ATOM   10736 C  CD1   . ILE B 1 644 ? 120.234 142.236 167.596 1.00 22.52 ?  644 ILE B CD1   1 
ATOM   10737 N  N     . GLN B 1 645 ? 116.909 145.484 164.591 1.00 12.43 ?  645 GLN B N     1 
ATOM   10738 C  CA    . GLN B 1 645 ? 116.704 146.124 163.294 1.00 13.88 ?  645 GLN B CA    1 
ATOM   10739 C  C     . GLN B 1 645 ? 116.005 147.470 163.418 1.00 17.48 ?  645 GLN B C     1 
ATOM   10740 O  O     . GLN B 1 645 ? 116.192 148.345 162.566 1.00 29.59 ?  645 GLN B O     1 
ATOM   10741 C  CB    . GLN B 1 645 ? 115.904 145.198 162.378 1.00 12.98 ?  645 GLN B CB    1 
ATOM   10742 C  CG    . GLN B 1 645 ? 115.735 145.708 160.959 1.00 3.84  ?  645 GLN B CG    1 
ATOM   10743 C  CD    . GLN B 1 645 ? 117.003 145.589 160.147 1.00 19.17 ?  645 GLN B CD    1 
ATOM   10744 O  OE1   . GLN B 1 645 ? 117.800 146.521 160.081 1.00 13.42 ?  645 GLN B OE1   1 
ATOM   10745 N  NE2   . GLN B 1 645 ? 117.196 144.437 159.518 1.00 16.27 ?  645 GLN B NE2   1 
ATOM   10746 N  N     . GLN B 1 646 ? 115.209 147.666 164.467 1.00 19.98 ?  646 GLN B N     1 
ATOM   10747 C  CA    . GLN B 1 646 ? 114.499 148.927 164.624 1.00 11.37 ?  646 GLN B CA    1 
ATOM   10748 C  C     . GLN B 1 646 ? 115.421 150.087 164.973 1.00 11.49 ?  646 GLN B C     1 
ATOM   10749 O  O     . GLN B 1 646 ? 114.973 151.236 164.944 1.00 15.53 ?  646 GLN B O     1 
ATOM   10750 C  CB    . GLN B 1 646 ? 113.407 148.786 165.684 1.00 19.79 ?  646 GLN B CB    1 
ATOM   10751 C  CG    . GLN B 1 646 ? 113.908 148.831 167.108 1.00 22.80 ?  646 GLN B CG    1 
ATOM   10752 C  CD    . GLN B 1 646 ? 112.812 148.549 168.110 1.00 27.77 ?  646 GLN B CD    1 
ATOM   10753 O  OE1   . GLN B 1 646 ? 112.873 147.573 168.855 1.00 26.85 ?  646 GLN B OE1   1 
ATOM   10754 N  NE2   . GLN B 1 646 ? 111.799 149.406 168.134 1.00 23.34 ?  646 GLN B NE2   1 
ATOM   10755 N  N     . HIS B 1 647 ? 116.686 149.824 165.291 1.00 29.18 ?  647 HIS B N     1 
ATOM   10756 C  CA    . HIS B 1 647 ? 117.655 150.876 165.555 1.00 12.41 ?  647 HIS B CA    1 
ATOM   10757 C  C     . HIS B 1 647 ? 118.775 150.923 164.527 1.00 13.61 ?  647 HIS B C     1 
ATOM   10758 O  O     . HIS B 1 647 ? 119.679 151.756 164.656 1.00 27.00 ?  647 HIS B O     1 
ATOM   10759 C  CB    . HIS B 1 647 ? 118.254 150.711 166.958 1.00 5.67  ?  647 HIS B CB    1 
ATOM   10760 C  CG    . HIS B 1 647 ? 117.229 150.554 168.037 1.00 14.52 ?  647 HIS B CG    1 
ATOM   10761 N  ND1   . HIS B 1 647 ? 116.322 151.542 168.351 1.00 18.16 ?  647 HIS B ND1   1 
ATOM   10762 C  CD2   . HIS B 1 647 ? 116.968 149.524 168.876 1.00 12.29 ?  647 HIS B CD2   1 
ATOM   10763 C  CE1   . HIS B 1 647 ? 115.546 151.128 169.336 1.00 20.52 ?  647 HIS B CE1   1 
ATOM   10764 N  NE2   . HIS B 1 647 ? 115.919 149.906 169.673 1.00 15.87 ?  647 HIS B NE2   1 
ATOM   10765 N  N     . ILE B 1 648 ? 118.741 150.062 163.516 1.00 14.96 ?  648 ILE B N     1 
ATOM   10766 C  CA    . ILE B 1 648 ? 119.754 150.012 162.469 1.00 16.22 ?  648 ILE B CA    1 
ATOM   10767 C  C     . ILE B 1 648 ? 119.123 150.563 161.198 1.00 14.31 ?  648 ILE B C     1 
ATOM   10768 O  O     . ILE B 1 648 ? 118.081 150.066 160.753 1.00 28.02 ?  648 ILE B O     1 
ATOM   10769 C  CB    . ILE B 1 648 ? 120.274 148.580 162.263 1.00 10.01 ?  648 ILE B CB    1 
ATOM   10770 C  CG1   . ILE B 1 648 ? 120.862 148.029 163.565 1.00 10.50 ?  648 ILE B CG1   1 
ATOM   10771 C  CG2   . ILE B 1 648 ? 121.311 148.535 161.160 1.00 3.67  ?  648 ILE B CG2   1 
ATOM   10772 C  CD1   . ILE B 1 648 ? 122.015 148.835 164.110 1.00 4.55  ?  648 ILE B CD1   1 
ATOM   10773 N  N     . ASP B 1 649 ? 119.743 151.593 160.615 1.00 7.88  ?  649 ASP B N     1 
ATOM   10774 C  CA    . ASP B 1 649 ? 119.148 152.226 159.442 1.00 9.36  ?  649 ASP B CA    1 
ATOM   10775 C  C     . ASP B 1 649 ? 119.285 151.358 158.199 1.00 7.99  ?  649 ASP B C     1 
ATOM   10776 O  O     . ASP B 1 649 ? 118.391 151.354 157.346 1.00 32.55 ?  649 ASP B O     1 
ATOM   10777 C  CB    . ASP B 1 649 ? 119.764 153.608 159.207 1.00 21.54 ?  649 ASP B CB    1 
ATOM   10778 C  CG    . ASP B 1 649 ? 121.278 153.585 159.190 1.00 16.61 ?  649 ASP B CG    1 
ATOM   10779 O  OD1   . ASP B 1 649 ? 121.887 153.859 160.242 1.00 20.43 ?  649 ASP B OD1   1 
ATOM   10780 O  OD2   . ASP B 1 649 ? 121.860 153.304 158.124 1.00 28.60 -1 649 ASP B OD2   1 
ATOM   10781 N  N     . GLN B 1 650 ? 120.387 150.630 158.073 1.00 10.05 ?  650 GLN B N     1 
ATOM   10782 C  CA    . GLN B 1 650 ? 120.547 149.630 157.030 1.00 2.07  ?  650 GLN B CA    1 
ATOM   10783 C  C     . GLN B 1 650 ? 120.080 148.281 157.575 1.00 5.15  ?  650 GLN B C     1 
ATOM   10784 O  O     . GLN B 1 650 ? 119.405 148.217 158.605 1.00 22.73 ?  650 GLN B O     1 
ATOM   10785 C  CB    . GLN B 1 650 ? 121.993 149.612 156.536 1.00 9.86  ?  650 GLN B CB    1 
ATOM   10786 C  CG    . GLN B 1 650 ? 122.446 150.920 155.932 1.00 8.84  ?  650 GLN B CG    1 
ATOM   10787 C  CD    . GLN B 1 650 ? 123.816 150.821 155.314 1.00 14.00 ?  650 GLN B CD    1 
ATOM   10788 O  OE1   . GLN B 1 650 ? 123.999 150.164 154.292 1.00 17.40 ?  650 GLN B OE1   1 
ATOM   10789 N  NE2   . GLN B 1 650 ? 124.791 151.480 155.925 1.00 8.23  ?  650 GLN B NE2   1 
ATOM   10790 N  N     . GLY B 1 651 ? 120.400 147.191 156.883 1.00 12.16 ?  651 GLY B N     1 
ATOM   10791 C  CA    . GLY B 1 651 ? 119.961 145.877 157.299 1.00 13.22 ?  651 GLY B CA    1 
ATOM   10792 C  C     . GLY B 1 651 ? 120.959 145.164 158.192 1.00 7.23  ?  651 GLY B C     1 
ATOM   10793 O  O     . GLY B 1 651 ? 121.996 145.694 158.583 1.00 12.16 ?  651 GLY B O     1 
ATOM   10794 N  N     . ILE B 1 652 ? 120.608 143.925 158.524 1.00 20.05 ?  652 ILE B N     1 
ATOM   10795 C  CA    . ILE B 1 652 ? 121.420 143.044 159.353 1.00 4.72  ?  652 ILE B CA    1 
ATOM   10796 C  C     . ILE B 1 652 ? 121.560 141.717 158.624 1.00 13.37 ?  652 ILE B C     1 
ATOM   10797 O  O     . ILE B 1 652 ? 120.574 141.190 158.098 1.00 24.03 ?  652 ILE B O     1 
ATOM   10798 C  CB    . ILE B 1 652 ? 120.796 142.827 160.746 1.00 2.58  ?  652 ILE B CB    1 
ATOM   10799 C  CG1   . ILE B 1 652 ? 120.587 144.159 161.463 1.00 3.36  ?  652 ILE B CG1   1 
ATOM   10800 C  CG2   . ILE B 1 652 ? 121.649 141.891 161.581 1.00 7.53  ?  652 ILE B CG2   1 
ATOM   10801 C  CD1   . ILE B 1 652 ? 119.797 144.035 162.737 1.00 8.68  ?  652 ILE B CD1   1 
ATOM   10802 N  N     . SER B 1 653 ? 122.775 141.181 158.586 1.00 14.90 ?  653 SER B N     1 
ATOM   10803 C  CA    . SER B 1 653 ? 123.009 139.872 157.985 1.00 13.87 ?  653 SER B CA    1 
ATOM   10804 C  C     . SER B 1 653 ? 122.369 138.812 158.871 1.00 20.31 ?  653 SER B C     1 
ATOM   10805 O  O     . SER B 1 653 ? 122.921 138.427 159.903 1.00 26.45 ?  653 SER B O     1 
ATOM   10806 C  CB    . SER B 1 653 ? 124.501 139.623 157.809 1.00 16.66 ?  653 SER B CB    1 
ATOM   10807 O  OG    . SER B 1 653 ? 124.909 139.919 156.488 1.00 22.31 ?  653 SER B OG    1 
ATOM   10808 N  N     . PHE B 1 654 ? 121.197 138.335 158.466 1.00 23.30 ?  654 PHE B N     1 
ATOM   10809 C  CA    . PHE B 1 654 ? 120.384 137.427 159.267 1.00 6.98  ?  654 PHE B CA    1 
ATOM   10810 C  C     . PHE B 1 654 ? 120.456 136.033 158.653 1.00 18.15 ?  654 PHE B C     1 
ATOM   10811 O  O     . PHE B 1 654 ? 119.813 135.763 157.634 1.00 27.86 ?  654 PHE B O     1 
ATOM   10812 C  CB    . PHE B 1 654 ? 118.944 137.927 159.342 1.00 13.53 ?  654 PHE B CB    1 
ATOM   10813 C  CG    . PHE B 1 654 ? 118.072 137.149 160.284 1.00 17.85 ?  654 PHE B CG    1 
ATOM   10814 C  CD1   . PHE B 1 654 ? 118.622 136.286 161.215 1.00 21.93 ?  654 PHE B CD1   1 
ATOM   10815 C  CD2   . PHE B 1 654 ? 116.700 137.287 160.241 1.00 20.97 ?  654 PHE B CD2   1 
ATOM   10816 C  CE1   . PHE B 1 654 ? 117.822 135.574 162.077 1.00 18.47 ?  654 PHE B CE1   1 
ATOM   10817 C  CE2   . PHE B 1 654 ? 115.895 136.579 161.103 1.00 24.46 ?  654 PHE B CE2   1 
ATOM   10818 C  CZ    . PHE B 1 654 ? 116.457 135.721 162.022 1.00 16.24 ?  654 PHE B CZ    1 
ATOM   10819 N  N     . THR B 1 655 ? 121.218 135.150 159.289 1.00 22.48 ?  655 THR B N     1 
ATOM   10820 C  CA    . THR B 1 655 ? 121.342 133.769 158.850 1.00 19.91 ?  655 THR B CA    1 
ATOM   10821 C  C     . THR B 1 655 ? 120.314 132.908 159.572 1.00 20.63 ?  655 THR B C     1 
ATOM   10822 O  O     . THR B 1 655 ? 120.178 132.987 160.796 1.00 29.03 ?  655 THR B O     1 
ATOM   10823 C  CB    . THR B 1 655 ? 122.753 133.244 159.119 1.00 29.28 ?  655 THR B CB    1 
ATOM   10824 O  OG1   . THR B 1 655 ? 123.698 133.985 158.338 1.00 35.51 ?  655 THR B OG1   1 
ATOM   10825 C  CG2   . THR B 1 655 ? 122.857 131.771 158.759 1.00 29.23 ?  655 THR B CG2   1 
ATOM   10826 N  N     . LEU B 1 656 ? 119.586 132.097 158.811 1.00 31.41 ?  656 LEU B N     1 
ATOM   10827 C  CA    . LEU B 1 656 ? 118.662 131.128 159.379 1.00 31.82 ?  656 LEU B CA    1 
ATOM   10828 C  C     . LEU B 1 656 ? 119.408 129.839 159.682 1.00 28.18 ?  656 LEU B C     1 
ATOM   10829 O  O     . LEU B 1 656 ? 120.081 129.284 158.809 1.00 33.03 ?  656 LEU B O     1 
ATOM   10830 C  CB    . LEU B 1 656 ? 117.501 130.852 158.424 1.00 34.25 ?  656 LEU B CB    1 
ATOM   10831 C  CG    . LEU B 1 656 ? 116.595 132.033 158.083 1.00 34.34 ?  656 LEU B CG    1 
ATOM   10832 C  CD1   . LEU B 1 656 ? 115.344 131.547 157.369 1.00 29.57 ?  656 LEU B CD1   1 
ATOM   10833 C  CD2   . LEU B 1 656 ? 116.237 132.820 159.332 1.00 25.37 ?  656 LEU B CD2   1 
ATOM   10834 N  N     . PHE B 1 657 ? 119.293 129.370 160.917 1.00 30.01 ?  657 PHE B N     1 
ATOM   10835 C  CA    . PHE B 1 657 ? 119.936 128.140 161.361 1.00 27.17 ?  657 PHE B CA    1 
ATOM   10836 C  C     . PHE B 1 657 ? 118.850 127.089 161.535 1.00 36.86 ?  657 PHE B C     1 
ATOM   10837 O  O     . PHE B 1 657 ? 118.028 127.183 162.452 1.00 39.95 ?  657 PHE B O     1 
ATOM   10838 C  CB    . PHE B 1 657 ? 120.712 128.371 162.653 1.00 31.39 ?  657 PHE B CB    1 
ATOM   10839 C  CG    . PHE B 1 657 ? 121.702 129.492 162.565 1.00 38.03 ?  657 PHE B CG    1 
ATOM   10840 C  CD1   . PHE B 1 657 ? 122.970 129.274 162.055 1.00 32.64 ?  657 PHE B CD1   1 
ATOM   10841 C  CD2   . PHE B 1 657 ? 121.364 130.767 162.984 1.00 35.57 ?  657 PHE B CD2   1 
ATOM   10842 C  CE1   . PHE B 1 657 ? 123.882 130.302 161.970 1.00 34.17 ?  657 PHE B CE1   1 
ATOM   10843 C  CE2   . PHE B 1 657 ? 122.273 131.800 162.901 1.00 34.07 ?  657 PHE B CE2   1 
ATOM   10844 C  CZ    . PHE B 1 657 ? 123.534 131.567 162.393 1.00 38.39 ?  657 PHE B CZ    1 
ATOM   10845 N  N     . LEU B 1 658 ? 118.851 126.093 160.656 1.00 40.65 ?  658 LEU B N     1 
ATOM   10846 C  CA    . LEU B 1 658 ? 117.776 125.119 160.572 1.00 41.19 ?  658 LEU B CA    1 
ATOM   10847 C  C     . LEU B 1 658 ? 118.295 123.726 160.898 1.00 45.56 ?  658 LEU B C     1 
ATOM   10848 O  O     . LEU B 1 658 ? 119.462 123.407 160.659 1.00 48.21 ?  658 LEU B O     1 
ATOM   10849 C  CB    . LEU B 1 658 ? 117.149 125.115 159.175 1.00 41.13 ?  658 LEU B CB    1 
ATOM   10850 C  CG    . LEU B 1 658 ? 117.033 126.478 158.492 1.00 40.87 ?  658 LEU B CG    1 
ATOM   10851 C  CD1   . LEU B 1 658 ? 116.949 126.308 156.989 1.00 38.06 ?  658 LEU B CD1   1 
ATOM   10852 C  CD2   . LEU B 1 658 ? 115.828 127.239 159.018 1.00 41.11 ?  658 LEU B CD2   1 
ATOM   10853 N  N     . LYS B 1 659 ? 117.416 122.906 161.458 1.00 49.14 ?  659 LYS B N     1 
ATOM   10854 C  CA    . LYS B 1 659 ? 117.703 121.496 161.657 1.00 50.62 ?  659 LYS B CA    1 
ATOM   10855 C  C     . LYS B 1 659 ? 117.382 120.714 160.388 1.00 52.29 ?  659 LYS B C     1 
ATOM   10856 O  O     . LYS B 1 659 ? 116.682 121.194 159.494 1.00 52.44 ?  659 LYS B O     1 
ATOM   10857 C  CB    . LYS B 1 659 ? 116.907 120.943 162.838 1.00 49.58 ?  659 LYS B CB    1 
ATOM   10858 C  CG    . LYS B 1 659 ? 117.261 121.580 164.168 1.00 52.09 ?  659 LYS B CG    1 
ATOM   10859 C  CD    . LYS B 1 659 ? 116.703 120.785 165.334 1.00 52.73 ?  659 LYS B CD    1 
ATOM   10860 C  CE    . LYS B 1 659 ? 117.145 121.377 166.663 1.00 51.17 ?  659 LYS B CE    1 
ATOM   10861 N  NZ    . LYS B 1 659 ? 116.983 120.415 167.787 1.00 53.28 1  659 LYS B NZ    1 
ATOM   10862 N  N     . ASP B 1 660 ? 117.918 119.494 160.315 1.00 57.27 ?  660 ASP B N     1 
ATOM   10863 C  CA    . ASP B 1 660 ? 117.623 118.636 159.173 1.00 56.83 ?  660 ASP B CA    1 
ATOM   10864 C  C     . ASP B 1 660 ? 116.161 118.208 159.158 1.00 55.41 ?  660 ASP B C     1 
ATOM   10865 O  O     . ASP B 1 660 ? 115.608 117.936 158.087 1.00 55.37 ?  660 ASP B O     1 
ATOM   10866 C  CB    . ASP B 1 660 ? 118.536 117.411 159.182 1.00 57.50 ?  660 ASP B CB    1 
ATOM   10867 C  CG    . ASP B 1 660 ? 118.499 116.662 160.502 1.00 58.83 ?  660 ASP B CG    1 
ATOM   10868 O  OD1   . ASP B 1 660 ? 118.043 117.245 161.507 1.00 57.20 ?  660 ASP B OD1   1 
ATOM   10869 O  OD2   . ASP B 1 660 ? 118.929 115.490 160.533 1.00 59.06 -1 660 ASP B OD2   1 
ATOM   10870 N  N     . THR B 1 661 ? 115.524 118.146 160.328 1.00 52.39 ?  661 THR B N     1 
ATOM   10871 C  CA    . THR B 1 661 ? 114.129 117.739 160.411 1.00 53.63 ?  661 THR B CA    1 
ATOM   10872 C  C     . THR B 1 661 ? 113.166 118.824 159.950 1.00 56.03 ?  661 THR B C     1 
ATOM   10873 O  O     . THR B 1 661 ? 111.996 118.522 159.686 1.00 54.76 ?  661 THR B O     1 
ATOM   10874 C  CB    . THR B 1 661 ? 113.785 117.334 161.845 1.00 54.73 ?  661 THR B CB    1 
ATOM   10875 O  OG1   . THR B 1 661 ? 114.057 118.428 162.728 1.00 52.56 ?  661 THR B OG1   1 
ATOM   10876 C  CG2   . THR B 1 661 ? 114.613 116.132 162.267 1.00 54.63 ?  661 THR B CG2   1 
ATOM   10877 N  N     . MET B 1 662 ? 113.620 120.069 159.853 1.00 55.39 ?  662 MET B N     1 
ATOM   10878 C  CA    . MET B 1 662 ? 112.740 121.155 159.447 1.00 51.19 ?  662 MET B CA    1 
ATOM   10879 C  C     . MET B 1 662 ? 112.333 120.999 157.987 1.00 52.53 ?  662 MET B C     1 
ATOM   10880 O  O     . MET B 1 662 ? 113.155 120.672 157.127 1.00 53.26 ?  662 MET B O     1 
ATOM   10881 C  CB    . MET B 1 662 ? 113.425 122.503 159.666 1.00 51.81 ?  662 MET B CB    1 
ATOM   10882 C  CG    . MET B 1 662 ? 113.033 123.181 160.967 1.00 51.85 ?  662 MET B CG    1 
ATOM   10883 S  SD    . MET B 1 662 ? 114.045 124.621 161.348 1.00 60.76 ?  662 MET B SD    1 
ATOM   10884 C  CE    . MET B 1 662 ? 112.945 125.525 162.433 1.00 51.82 ?  662 MET B CE    1 
ATOM   10885 N  N     . THR B 1 663 ? 111.053 121.232 157.715 1.00 48.30 ?  663 THR B N     1 
ATOM   10886 C  CA    . THR B 1 663 ? 110.502 121.054 156.383 1.00 45.04 ?  663 THR B CA    1 
ATOM   10887 C  C     . THR B 1 663 ? 110.563 122.363 155.599 1.00 46.54 ?  663 THR B C     1 
ATOM   10888 O  O     . THR B 1 663 ? 111.050 123.390 156.077 1.00 49.48 ?  663 THR B O     1 
ATOM   10889 C  CB    . THR B 1 663 ? 109.062 120.549 156.467 1.00 41.89 ?  663 THR B CB    1 
ATOM   10890 O  OG1   . THR B 1 663 ? 108.386 121.207 157.545 1.00 42.37 ?  663 THR B OG1   1 
ATOM   10891 C  CG2   . THR B 1 663 ? 109.036 119.052 156.713 1.00 44.20 ?  663 THR B CG2   1 
ATOM   10892 N  N     . THR B 1 664 ? 110.064 122.318 154.362 1.00 41.28 ?  664 THR B N     1 
ATOM   10893 C  CA    . THR B 1 664 ? 109.900 123.537 153.580 1.00 38.99 ?  664 THR B CA    1 
ATOM   10894 C  C     . THR B 1 664 ? 108.900 124.477 154.243 1.00 38.44 ?  664 THR B C     1 
ATOM   10895 O  O     . THR B 1 664 ? 109.095 125.700 154.257 1.00 41.92 ?  664 THR B O     1 
ATOM   10896 C  CB    . THR B 1 664 ? 109.462 123.179 152.156 1.00 41.98 ?  664 THR B CB    1 
ATOM   10897 O  OG1   . THR B 1 664 ? 110.601 122.751 151.397 1.00 40.54 ?  664 THR B OG1   1 
ATOM   10898 C  CG2   . THR B 1 664 ? 108.801 124.356 151.460 1.00 41.48 ?  664 THR B CG2   1 
ATOM   10899 N  N     . ARG B 1 665 ? 107.834 123.919 154.819 1.00 39.22 ?  665 ARG B N     1 
ATOM   10900 C  CA    . ARG B 1 665 ? 106.832 124.741 155.488 1.00 38.75 ?  665 ARG B CA    1 
ATOM   10901 C  C     . ARG B 1 665 ? 107.428 125.485 156.674 1.00 41.96 ?  665 ARG B C     1 
ATOM   10902 O  O     . ARG B 1 665 ? 107.055 126.630 156.941 1.00 47.88 ?  665 ARG B O     1 
ATOM   10903 C  CB    . ARG B 1 665 ? 105.657 123.876 155.940 1.00 40.49 ?  665 ARG B CB    1 
ATOM   10904 C  CG    . ARG B 1 665 ? 104.375 124.655 156.174 1.00 37.78 ?  665 ARG B CG    1 
ATOM   10905 C  CD    . ARG B 1 665 ? 103.443 123.912 157.111 1.00 41.85 ?  665 ARG B CD    1 
ATOM   10906 N  NE    . ARG B 1 665 ? 103.724 124.214 158.509 1.00 46.72 ?  665 ARG B NE    1 
ATOM   10907 C  CZ    . ARG B 1 665 ? 102.907 123.932 159.514 1.00 48.71 ?  665 ARG B CZ    1 
ATOM   10908 N  NH1   . ARG B 1 665 ? 101.746 123.330 159.315 1.00 43.92 1  665 ARG B NH1   1 
ATOM   10909 N  NH2   . ARG B 1 665 ? 103.265 124.264 160.752 1.00 46.34 ?  665 ARG B NH2   1 
ATOM   10910 N  N     . ASP B 1 666 ? 108.350 124.854 157.402 1.00 39.87 ?  666 ASP B N     1 
ATOM   10911 C  CA    . ASP B 1 666 ? 108.966 125.523 158.545 1.00 35.12 ?  666 ASP B CA    1 
ATOM   10912 C  C     . ASP B 1 666 ? 109.838 126.693 158.104 1.00 40.01 ?  666 ASP B C     1 
ATOM   10913 O  O     . ASP B 1 666 ? 109.811 127.763 158.723 1.00 42.48 ?  666 ASP B O     1 
ATOM   10914 C  CB    . ASP B 1 666 ? 109.779 124.522 159.363 1.00 42.29 ?  666 ASP B CB    1 
ATOM   10915 C  CG    . ASP B 1 666 ? 108.914 123.453 159.995 1.00 49.42 ?  666 ASP B CG    1 
ATOM   10916 O  OD1   . ASP B 1 666 ? 107.796 123.783 160.442 1.00 46.16 ?  666 ASP B OD1   1 
ATOM   10917 O  OD2   . ASP B 1 666 ? 109.351 122.285 160.049 1.00 50.89 -1 666 ASP B OD2   1 
ATOM   10918 N  N     . LEU B 1 667 ? 110.617 126.511 157.035 1.00 35.25 ?  667 LEU B N     1 
ATOM   10919 C  CA    . LEU B 1 667 ? 111.418 127.613 156.512 1.00 28.35 ?  667 LEU B CA    1 
ATOM   10920 C  C     . LEU B 1 667 ? 110.527 128.745 156.017 1.00 30.94 ?  667 LEU B C     1 
ATOM   10921 O  O     . LEU B 1 667 ? 110.818 129.925 156.249 1.00 32.33 ?  667 LEU B O     1 
ATOM   10922 C  CB    . LEU B 1 667 ? 112.327 127.112 155.390 1.00 31.84 ?  667 LEU B CB    1 
ATOM   10923 C  CG    . LEU B 1 667 ? 113.731 127.711 155.273 1.00 33.11 ?  667 LEU B CG    1 
ATOM   10924 C  CD1   . LEU B 1 667 ? 114.541 126.939 154.249 1.00 33.42 ?  667 LEU B CD1   1 
ATOM   10925 C  CD2   . LEU B 1 667 ? 113.691 129.183 154.909 1.00 38.02 ?  667 LEU B CD2   1 
ATOM   10926 N  N     . ASN B 1 668 ? 109.433 128.404 155.333 1.00 36.62 ?  668 ASN B N     1 
ATOM   10927 C  CA    . ASN B 1 668 ? 108.497 129.426 154.879 1.00 23.50 ?  668 ASN B CA    1 
ATOM   10928 C  C     . ASN B 1 668 ? 107.867 130.158 156.055 1.00 22.91 ?  668 ASN B C     1 
ATOM   10929 O  O     . ASN B 1 668 ? 107.666 131.376 156.000 1.00 31.40 ?  668 ASN B O     1 
ATOM   10930 C  CB    . ASN B 1 668 ? 107.419 128.796 154.000 1.00 28.51 ?  668 ASN B CB    1 
ATOM   10931 C  CG    . ASN B 1 668 ? 107.852 128.661 152.559 1.00 33.12 ?  668 ASN B CG    1 
ATOM   10932 O  OD1   . ASN B 1 668 ? 107.551 127.667 151.900 1.00 40.18 ?  668 ASN B OD1   1 
ATOM   10933 N  ND2   . ASN B 1 668 ? 108.566 129.662 152.060 1.00 30.35 ?  668 ASN B ND2   1 
ATOM   10934 N  N     . ARG B 1 669 ? 107.539 129.433 157.124 1.00 31.32 ?  669 ARG B N     1 
ATOM   10935 C  CA    . ARG B 1 669 ? 106.985 130.067 158.314 1.00 32.98 ?  669 ARG B CA    1 
ATOM   10936 C  C     . ARG B 1 669 ? 107.986 131.024 158.942 1.00 29.08 ?  669 ARG B C     1 
ATOM   10937 O  O     . ARG B 1 669 ? 107.617 132.117 159.382 1.00 28.03 ?  669 ARG B O     1 
ATOM   10938 C  CB    . ARG B 1 669 ? 106.556 129.003 159.322 1.00 32.09 ?  669 ARG B CB    1 
ATOM   10939 C  CG    . ARG B 1 669 ? 105.059 128.796 159.398 1.00 28.78 ?  669 ARG B CG    1 
ATOM   10940 C  CD    . ARG B 1 669 ? 104.692 127.841 160.521 1.00 33.13 ?  669 ARG B CD    1 
ATOM   10941 N  NE    . ARG B 1 669 ? 104.665 128.495 161.824 1.00 35.06 ?  669 ARG B NE    1 
ATOM   10942 C  CZ    . ARG B 1 669 ? 103.772 129.402 162.196 1.00 36.71 ?  669 ARG B CZ    1 
ATOM   10943 N  NH1   . ARG B 1 669 ? 102.799 129.789 161.389 1.00 35.18 1  669 ARG B NH1   1 
ATOM   10944 N  NH2   . ARG B 1 669 ? 103.854 129.932 163.413 1.00 38.29 ?  669 ARG B NH2   1 
ATOM   10945 N  N     . ILE B 1 670 ? 109.259 130.627 158.997 1.00 25.86 ?  670 ILE B N     1 
ATOM   10946 C  CA    . ILE B 1 670 ? 110.288 131.519 159.527 1.00 25.29 ?  670 ILE B CA    1 
ATOM   10947 C  C     . ILE B 1 670 ? 110.400 132.772 158.668 1.00 24.13 ?  670 ILE B C     1 
ATOM   10948 O  O     . ILE B 1 670 ? 110.485 133.891 159.188 1.00 27.90 ?  670 ILE B O     1 
ATOM   10949 C  CB    . ILE B 1 670 ? 111.637 130.786 159.637 1.00 32.05 ?  670 ILE B CB    1 
ATOM   10950 C  CG1   . ILE B 1 670 ? 111.547 129.643 160.648 1.00 31.60 ?  670 ILE B CG1   1 
ATOM   10951 C  CG2   . ILE B 1 670 ? 112.736 131.753 160.040 1.00 28.90 ?  670 ILE B CG2   1 
ATOM   10952 C  CD1   . ILE B 1 670 ? 112.561 128.551 160.414 1.00 27.50 ?  670 ILE B CD1   1 
ATOM   10953 N  N     . ASP B 1 671 ? 110.393 132.608 157.343 1.00 25.07 ?  671 ASP B N     1 
ATOM   10954 C  CA    . ASP B 1 671 ? 110.482 133.763 156.451 1.00 20.62 ?  671 ASP B CA    1 
ATOM   10955 C  C     . ASP B 1 671 ? 109.282 134.690 156.613 1.00 21.54 ?  671 ASP B C     1 
ATOM   10956 O  O     . ASP B 1 671 ? 109.432 135.916 156.636 1.00 30.77 ?  671 ASP B O     1 
ATOM   10957 C  CB    . ASP B 1 671 ? 110.605 133.301 154.999 1.00 21.88 ?  671 ASP B CB    1 
ATOM   10958 C  CG    . ASP B 1 671 ? 111.800 132.397 154.773 1.00 40.20 ?  671 ASP B CG    1 
ATOM   10959 O  OD1   . ASP B 1 671 ? 112.732 132.422 155.602 1.00 39.79 ?  671 ASP B OD1   1 
ATOM   10960 O  OD2   . ASP B 1 671 ? 111.806 131.657 153.766 1.00 39.34 -1 671 ASP B OD2   1 
ATOM   10961 N  N     . LEU B 1 672 ? 108.082 134.122 156.734 1.00 21.76 ?  672 LEU B N     1 
ATOM   10962 C  CA    . LEU B 1 672 ? 106.882 134.940 156.864 1.00 16.89 ?  672 LEU B CA    1 
ATOM   10963 C  C     . LEU B 1 672 ? 106.809 135.626 158.220 1.00 18.59 ?  672 LEU B C     1 
ATOM   10964 O  O     . LEU B 1 672 ? 106.290 136.743 158.318 1.00 24.78 ?  672 LEU B O     1 
ATOM   10965 C  CB    . LEU B 1 672 ? 105.636 134.088 156.631 1.00 24.55 ?  672 LEU B CB    1 
ATOM   10966 C  CG    . LEU B 1 672 ? 105.469 133.546 155.212 1.00 24.78 ?  672 LEU B CG    1 
ATOM   10967 C  CD1   . LEU B 1 672 ? 104.477 132.396 155.192 1.00 20.61 ?  672 LEU B CD1   1 
ATOM   10968 C  CD2   . LEU B 1 672 ? 105.045 134.651 154.260 1.00 23.39 ?  672 LEU B CD2   1 
ATOM   10969 N  N     . TYR B 1 673 ? 107.311 134.983 159.275 1.00 22.69 ?  673 TYR B N     1 
ATOM   10970 C  CA    . TYR B 1 673 ? 107.362 135.642 160.575 1.00 14.92 ?  673 TYR B CA    1 
ATOM   10971 C  C     . TYR B 1 673 ? 108.413 136.743 160.589 1.00 18.79 ?  673 TYR B C     1 
ATOM   10972 O  O     . TYR B 1 673 ? 108.228 137.777 161.241 1.00 25.74 ?  673 TYR B O     1 
ATOM   10973 C  CB    . TYR B 1 673 ? 107.641 134.622 161.675 1.00 19.00 ?  673 TYR B CB    1 
ATOM   10974 C  CG    . TYR B 1 673 ? 107.674 135.225 163.059 1.00 20.29 ?  673 TYR B CG    1 
ATOM   10975 C  CD1   . TYR B 1 673 ? 106.543 135.811 163.607 1.00 22.11 ?  673 TYR B CD1   1 
ATOM   10976 C  CD2   . TYR B 1 673 ? 108.835 135.208 163.814 1.00 15.22 ?  673 TYR B CD2   1 
ATOM   10977 C  CE1   . TYR B 1 673 ? 106.568 136.362 164.869 1.00 20.83 ?  673 TYR B CE1   1 
ATOM   10978 C  CE2   . TYR B 1 673 ? 108.871 135.757 165.077 1.00 24.30 ?  673 TYR B CE2   1 
ATOM   10979 C  CZ    . TYR B 1 673 ? 107.735 136.332 165.600 1.00 25.45 ?  673 TYR B CZ    1 
ATOM   10980 O  OH    . TYR B 1 673 ? 107.767 136.881 166.859 1.00 29.84 ?  673 TYR B OH    1 
ATOM   10981 N  N     . ALA B 1 674 ? 109.528 136.534 159.887 1.00 21.72 ?  674 ALA B N     1 
ATOM   10982 C  CA    . ALA B 1 674 ? 110.510 137.599 159.728 1.00 12.28 ?  674 ALA B CA    1 
ATOM   10983 C  C     . ALA B 1 674 ? 109.908 138.785 158.989 1.00 17.86 ?  674 ALA B C     1 
ATOM   10984 O  O     . ALA B 1 674 ? 110.095 139.939 159.392 1.00 30.35 ?  674 ALA B O     1 
ATOM   10985 C  CB    . ALA B 1 674 ? 111.739 137.067 158.993 1.00 10.16 ?  674 ALA B CB    1 
ATOM   10986 N  N     . HIS B 1 675 ? 109.164 138.519 157.917 1.00 15.42 ?  675 HIS B N     1 
ATOM   10987 C  CA    . HIS B 1 675 ? 108.473 139.591 157.207 1.00 16.56 ?  675 HIS B CA    1 
ATOM   10988 C  C     . HIS B 1 675 ? 107.468 140.293 158.113 1.00 21.20 ?  675 HIS B C     1 
ATOM   10989 O  O     . HIS B 1 675 ? 107.343 141.522 158.081 1.00 26.90 ?  675 HIS B O     1 
ATOM   10990 C  CB    . HIS B 1 675 ? 107.781 139.031 155.966 1.00 18.38 ?  675 HIS B CB    1 
ATOM   10991 C  CG    . HIS B 1 675 ? 106.913 140.024 155.260 1.00 21.58 ?  675 HIS B CG    1 
ATOM   10992 N  ND1   . HIS B 1 675 ? 105.565 140.148 155.516 1.00 27.58 ?  675 HIS B ND1   1 
ATOM   10993 C  CD2   . HIS B 1 675 ? 107.201 140.945 154.311 1.00 15.77 ?  675 HIS B CD2   1 
ATOM   10994 C  CE1   . HIS B 1 675 ? 105.060 141.101 154.755 1.00 25.50 ?  675 HIS B CE1   1 
ATOM   10995 N  NE2   . HIS B 1 675 ? 106.032 141.600 154.014 1.00 29.27 ?  675 HIS B NE2   1 
ATOM   10996 N  N     . HIS B 1 676 ? 106.742 139.524 158.924 1.00 22.09 ?  676 HIS B N     1 
ATOM   10997 C  CA    . HIS B 1 676 ? 105.745 140.101 159.820 1.00 20.05 ?  676 HIS B CA    1 
ATOM   10998 C  C     . HIS B 1 676 ? 106.393 140.973 160.888 1.00 26.00 ?  676 HIS B C     1 
ATOM   10999 O  O     . HIS B 1 676 ? 105.837 142.006 161.275 1.00 25.33 ?  676 HIS B O     1 
ATOM   11000 C  CB    . HIS B 1 676 ? 104.923 138.985 160.463 1.00 24.17 ?  676 HIS B CB    1 
ATOM   11001 C  CG    . HIS B 1 676 ? 103.999 139.457 161.541 1.00 22.97 ?  676 HIS B CG    1 
ATOM   11002 N  ND1   . HIS B 1 676 ? 102.956 140.326 161.301 1.00 21.33 ?  676 HIS B ND1   1 
ATOM   11003 C  CD2   . HIS B 1 676 ? 103.959 139.180 162.865 1.00 25.21 ?  676 HIS B CD2   1 
ATOM   11004 C  CE1   . HIS B 1 676 ? 102.314 140.562 162.431 1.00 28.69 ?  676 HIS B CE1   1 
ATOM   11005 N  NE2   . HIS B 1 676 ? 102.904 139.880 163.395 1.00 27.27 ?  676 HIS B NE2   1 
ATOM   11006 N  N     . ARG B 1 677 ? 107.565 140.575 161.374 1.00 24.54 ?  677 ARG B N     1 
ATOM   11007 C  CA    . ARG B 1 677 ? 108.230 141.265 162.469 1.00 19.48 ?  677 ARG B CA    1 
ATOM   11008 C  C     . ARG B 1 677 ? 109.081 142.440 162.009 1.00 23.24 ?  677 ARG B C     1 
ATOM   11009 O  O     . ARG B 1 677 ? 109.724 143.084 162.844 1.00 30.96 ?  677 ARG B O     1 
ATOM   11010 C  CB    . ARG B 1 677 ? 109.096 140.282 163.258 1.00 19.00 ?  677 ARG B CB    1 
ATOM   11011 C  CG    . ARG B 1 677 ? 108.321 139.446 164.252 1.00 19.85 ?  677 ARG B CG    1 
ATOM   11012 C  CD    . ARG B 1 677 ? 107.787 140.296 165.387 1.00 23.48 ?  677 ARG B CD    1 
ATOM   11013 N  NE    . ARG B 1 677 ? 108.788 140.495 166.427 1.00 30.10 ?  677 ARG B NE    1 
ATOM   11014 C  CZ    . ARG B 1 677 ? 109.219 141.682 166.831 1.00 34.53 ?  677 ARG B CZ    1 
ATOM   11015 N  NH1   . ARG B 1 677 ? 108.755 142.802 166.303 1.00 29.29 1  677 ARG B NH1   1 
ATOM   11016 N  NH2   . ARG B 1 677 ? 110.141 141.746 167.786 1.00 29.06 ?  677 ARG B NH2   1 
ATOM   11017 N  N     . GLY B 1 678 ? 109.105 142.734 160.714 1.00 22.05 ?  678 GLY B N     1 
ATOM   11018 C  CA    . GLY B 1 678 ? 109.869 143.853 160.208 1.00 12.98 ?  678 GLY B CA    1 
ATOM   11019 C  C     . GLY B 1 678 ? 111.285 143.536 159.794 1.00 16.33 ?  678 GLY B C     1 
ATOM   11020 O  O     . GLY B 1 678 ? 112.082 144.466 159.621 1.00 24.40 ?  678 GLY B O     1 
ATOM   11021 N  N     . ILE B 1 679 ? 111.631 142.258 159.637 1.00 18.05 ?  679 ILE B N     1 
ATOM   11022 C  CA    . ILE B 1 679 ? 112.964 141.900 159.171 1.00 15.19 ?  679 ILE B CA    1 
ATOM   11023 C  C     . ILE B 1 679 ? 113.138 142.392 157.744 1.00 21.06 ?  679 ILE B C     1 
ATOM   11024 O  O     . ILE B 1 679 ? 112.258 142.210 156.894 1.00 28.13 ?  679 ILE B O     1 
ATOM   11025 C  CB    . ILE B 1 679 ? 113.179 140.383 159.281 1.00 13.44 ?  679 ILE B CB    1 
ATOM   11026 C  CG1   . ILE B 1 679 ? 113.234 139.954 160.750 1.00 13.99 ?  679 ILE B CG1   1 
ATOM   11027 C  CG2   . ILE B 1 679 ? 114.435 139.954 158.544 1.00 15.28 ?  679 ILE B CG2   1 
ATOM   11028 C  CD1   . ILE B 1 679 ? 114.359 140.572 161.520 1.00 18.66 ?  679 ILE B CD1   1 
ATOM   11029 N  N     . LYS B 1 680 ? 114.270 143.037 157.478 1.00 10.64 ?  680 LYS B N     1 
ATOM   11030 C  CA    . LYS B 1 680 ? 114.518 143.621 156.167 1.00 5.62  ?  680 LYS B CA    1 
ATOM   11031 C  C     . LYS B 1 680 ? 115.107 142.611 155.189 1.00 0.15  ?  680 LYS B C     1 
ATOM   11032 O  O     . LYS B 1 680 ? 114.668 142.529 154.040 1.00 19.15 ?  680 LYS B O     1 
ATOM   11033 C  CB    . LYS B 1 680 ? 115.448 144.827 156.302 1.00 11.81 ?  680 LYS B CB    1 
ATOM   11034 C  CG    . LYS B 1 680 ? 114.864 145.982 157.086 1.00 0.00  ?  680 LYS B CG    1 
ATOM   11035 C  CD    . LYS B 1 680 ? 115.792 147.178 157.045 1.00 2.10  ?  680 LYS B CD    1 
ATOM   11036 C  CE    . LYS B 1 680 ? 115.379 148.228 158.051 1.00 12.27 ?  680 LYS B CE    1 
ATOM   11037 N  NZ    . LYS B 1 680 ? 116.232 149.441 157.976 1.00 15.62 1  680 LYS B NZ    1 
ATOM   11038 N  N     . THR B 1 681 ? 116.104 141.847 155.623 1.00 6.84  ?  681 THR B N     1 
ATOM   11039 C  CA    . THR B 1 681 ? 116.766 140.882 154.760 1.00 7.07  ?  681 THR B CA    1 
ATOM   11040 C  C     . THR B 1 681 ? 116.990 139.586 155.521 1.00 12.62 ?  681 THR B C     1 
ATOM   11041 O  O     . THR B 1 681 ? 117.116 139.580 156.747 1.00 25.64 ?  681 THR B O     1 
ATOM   11042 C  CB    . THR B 1 681 ? 118.113 141.409 154.232 1.00 13.07 ?  681 THR B CB    1 
ATOM   11043 O  OG1   . THR B 1 681 ? 118.876 141.958 155.313 1.00 29.37 ?  681 THR B OG1   1 
ATOM   11044 C  CG2   . THR B 1 681 ? 117.905 142.478 153.176 1.00 7.92  ?  681 THR B CG2   1 
ATOM   11045 N  N     . ILE B 1 682 ? 117.037 138.484 154.778 1.00 13.30 ?  682 ILE B N     1 
ATOM   11046 C  CA    . ILE B 1 682 ? 117.413 137.181 155.309 1.00 8.69  ?  682 ILE B CA    1 
ATOM   11047 C  C     . ILE B 1 682 ? 118.623 136.692 154.527 1.00 17.51 ?  682 ILE B C     1 
ATOM   11048 O  O     . ILE B 1 682 ? 118.579 136.605 153.295 1.00 13.41 ?  682 ILE B O     1 
ATOM   11049 C  CB    . ILE B 1 682 ? 116.256 136.170 155.222 1.00 11.16 ?  682 ILE B CB    1 
ATOM   11050 C  CG1   . ILE B 1 682 ? 115.017 136.718 155.931 1.00 19.69 ?  682 ILE B CG1   1 
ATOM   11051 C  CG2   . ILE B 1 682 ? 116.670 134.858 155.842 1.00 18.50 ?  682 ILE B CG2   1 
ATOM   11052 C  CD1   . ILE B 1 682 ? 113.893 135.719 156.055 1.00 21.11 ?  682 ILE B CD1   1 
ATOM   11053 N  N     . TYR B 1 683 ? 119.703 136.379 155.242 1.00 23.45 ?  683 TYR B N     1 
ATOM   11054 C  CA    . TYR B 1 683 ? 120.975 136.088 154.581 1.00 18.72 ?  683 TYR B CA    1 
ATOM   11055 C  C     . TYR B 1 683 ? 121.056 134.644 154.097 1.00 21.31 ?  683 TYR B C     1 
ATOM   11056 O  O     . TYR B 1 683 ? 121.096 134.381 152.894 1.00 36.30 ?  683 TYR B O     1 
ATOM   11057 C  CB    . TYR B 1 683 ? 122.131 136.406 155.534 1.00 18.95 ?  683 TYR B CB    1 
ATOM   11058 C  CG    . TYR B 1 683 ? 123.499 136.365 154.899 1.00 13.76 ?  683 TYR B CG    1 
ATOM   11059 C  CD1   . TYR B 1 683 ? 123.657 136.541 153.533 1.00 10.60 ?  683 TYR B CD1   1 
ATOM   11060 C  CD2   . TYR B 1 683 ? 124.635 136.160 155.670 1.00 10.01 ?  683 TYR B CD2   1 
ATOM   11061 C  CE1   . TYR B 1 683 ? 124.903 136.506 152.952 1.00 19.38 ?  683 TYR B CE1   1 
ATOM   11062 C  CE2   . TYR B 1 683 ? 125.887 136.125 155.095 1.00 19.11 ?  683 TYR B CE2   1 
ATOM   11063 C  CZ    . TYR B 1 683 ? 126.015 136.301 153.735 1.00 21.30 ?  683 TYR B CZ    1 
ATOM   11064 O  OH    . TYR B 1 683 ? 127.260 136.267 153.154 1.00 23.65 ?  683 TYR B OH    1 
ATOM   11065 N  N     . TYR B 1 684 ? 121.054 133.691 155.021 1.00 29.13 ?  684 TYR B N     1 
ATOM   11066 C  CA    . TYR B 1 684 ? 121.398 132.323 154.676 1.00 22.22 ?  684 TYR B CA    1 
ATOM   11067 C  C     . TYR B 1 684 ? 120.485 131.360 155.409 1.00 37.02 ?  684 TYR B C     1 
ATOM   11068 O  O     . TYR B 1 684 ? 120.012 131.642 156.512 1.00 37.92 ?  684 TYR B O     1 
ATOM   11069 C  CB    . TYR B 1 684 ? 122.856 132.004 155.027 1.00 24.34 ?  684 TYR B CB    1 
ATOM   11070 C  CG    . TYR B 1 684 ? 123.814 132.110 153.868 1.00 25.68 ?  684 TYR B CG    1 
ATOM   11071 C  CD1   . TYR B 1 684 ? 123.456 131.668 152.603 1.00 26.99 ?  684 TYR B CD1   1 
ATOM   11072 C  CD2   . TYR B 1 684 ? 125.079 132.650 154.040 1.00 30.41 ?  684 TYR B CD2   1 
ATOM   11073 C  CE1   . TYR B 1 684 ? 124.331 131.764 151.540 1.00 33.90 ?  684 TYR B CE1   1 
ATOM   11074 C  CE2   . TYR B 1 684 ? 125.961 132.752 152.985 1.00 25.07 ?  684 TYR B CE2   1 
ATOM   11075 C  CZ    . TYR B 1 684 ? 125.583 132.307 151.739 1.00 30.64 ?  684 TYR B CZ    1 
ATOM   11076 O  OH    . TYR B 1 684 ? 126.461 132.405 150.684 1.00 35.44 ?  684 TYR B OH    1 
ATOM   11077 N  N     . ALA B 1 685 ? 120.247 130.216 154.781 1.00 37.12 ?  685 ALA B N     1 
ATOM   11078 C  CA    . ALA B 1 685 ? 119.553 129.096 155.401 1.00 33.67 ?  685 ALA B CA    1 
ATOM   11079 C  C     . ALA B 1 685 ? 120.606 128.017 155.643 1.00 34.24 ?  685 ALA B C     1 
ATOM   11080 O  O     . ALA B 1 685 ? 120.940 127.241 154.747 1.00 42.25 ?  685 ALA B O     1 
ATOM   11081 C  CB    . ALA B 1 685 ? 118.413 128.598 154.525 1.00 31.43 ?  685 ALA B CB    1 
ATOM   11082 N  N     . ARG B 1 686 ? 121.134 127.981 156.862 1.00 32.67 ?  686 ARG B N     1 
ATOM   11083 C  CA    . ARG B 1 686 ? 122.145 127.002 157.239 1.00 38.58 ?  686 ARG B CA    1 
ATOM   11084 C  C     . ARG B 1 686 ? 121.468 125.832 157.938 1.00 41.88 ?  686 ARG B C     1 
ATOM   11085 O  O     . ARG B 1 686 ? 120.807 126.014 158.966 1.00 42.46 ?  686 ARG B O     1 
ATOM   11086 C  CB    . ARG B 1 686 ? 123.201 127.635 158.143 1.00 40.04 ?  686 ARG B CB    1 
ATOM   11087 C  CG    . ARG B 1 686 ? 124.288 128.375 157.391 1.00 40.60 ?  686 ARG B CG    1 
ATOM   11088 C  CD    . ARG B 1 686 ? 125.536 128.531 158.241 1.00 44.30 ?  686 ARG B CD    1 
ATOM   11089 N  NE    . ARG B 1 686 ? 126.374 127.340 158.208 1.00 46.43 ?  686 ARG B NE    1 
ATOM   11090 C  CZ    . ARG B 1 686 ? 127.699 127.358 158.160 1.00 48.20 ?  686 ARG B CZ    1 
ATOM   11091 N  NH1   . ARG B 1 686 ? 128.373 128.495 158.117 1.00 43.79 1  686 ARG B NH1   1 
ATOM   11092 N  NH2   . ARG B 1 686 ? 128.364 126.206 158.149 1.00 47.81 ?  686 ARG B NH2   1 
ATOM   11093 N  N     . THR B 1 687 ? 121.634 124.636 157.383 1.00 46.89 ?  687 THR B N     1 
ATOM   11094 C  CA    . THR B 1 687 ? 121.007 123.431 157.904 1.00 50.40 ?  687 THR B CA    1 
ATOM   11095 C  C     . THR B 1 687 ? 122.051 122.550 158.577 1.00 49.85 ?  687 THR B C     1 
ATOM   11096 O  O     . THR B 1 687 ? 123.170 122.404 158.077 1.00 51.44 ?  687 THR B O     1 
ATOM   11097 C  CB    . THR B 1 687 ? 120.303 122.650 156.790 1.00 47.33 ?  687 THR B CB    1 
ATOM   11098 O  OG1   . THR B 1 687 ? 119.676 123.566 155.885 1.00 44.31 ?  687 THR B OG1   1 
ATOM   11099 C  CG2   . THR B 1 687 ? 119.251 121.725 157.373 1.00 45.39 ?  687 THR B CG2   1 
ATOM   11100 N  N     . LYS B 1 688 ? 121.678 121.971 159.713 1.00 47.38 ?  688 LYS B N     1 
ATOM   11101 C  CA    . LYS B 1 688 ? 122.570 121.083 160.448 1.00 49.75 ?  688 LYS B CA    1 
ATOM   11102 C  C     . LYS B 1 688 ? 122.378 119.635 160.011 1.00 54.70 ?  688 LYS B C     1 
ATOM   11103 O  O     . LYS B 1 688 ? 121.250 119.175 159.837 1.00 55.57 ?  688 LYS B O     1 
ATOM   11104 C  CB    . LYS B 1 688 ? 122.336 121.211 161.953 1.00 47.73 ?  688 LYS B CB    1 
ATOM   11105 C  CG    . LYS B 1 688 ? 123.403 120.542 162.801 1.00 49.97 ?  688 LYS B CG    1 
ATOM   11106 C  CD    . LYS B 1 688 ? 123.385 121.069 164.223 1.00 50.55 ?  688 LYS B CD    1 
ATOM   11107 C  CE    . LYS B 1 688 ? 124.586 120.573 165.010 1.00 52.82 ?  688 LYS B CE    1 
ATOM   11108 N  NZ    . LYS B 1 688 ? 124.634 121.166 166.374 1.00 54.26 ?  688 LYS B NZ    1 
ATOM   11109 N  N     . ASP C 2 37  ? 137.028 74.343  115.277 1.00 45.99 ?  16  ASP C N     1 
ATOM   11110 C  CA    . ASP C 2 37  ? 136.617 74.807  113.948 1.00 45.47 ?  16  ASP C CA    1 
ATOM   11111 C  C     . ASP C 2 37  ? 135.468 75.816  113.956 1.00 44.13 ?  16  ASP C C     1 
ATOM   11112 O  O     . ASP C 2 37  ? 135.105 76.346  112.904 1.00 44.46 ?  16  ASP C O     1 
ATOM   11113 C  CB    . ASP C 2 37  ? 136.227 73.608  113.080 1.00 45.90 ?  16  ASP C CB    1 
ATOM   11114 C  CG    . ASP C 2 37  ? 137.269 72.517  113.101 1.00 47.25 ?  16  ASP C CG    1 
ATOM   11115 O  OD1   . ASP C 2 37  ? 138.476 72.842  113.096 1.00 47.99 ?  16  ASP C OD1   1 
ATOM   11116 O  OD2   . ASP C 2 37  ? 136.878 71.332  113.126 1.00 49.50 -1 16  ASP C OD2   1 
ATOM   11117 N  N     . PHE C 2 38  ? 134.901 76.085  115.129 1.00 42.17 ?  17  PHE C N     1 
ATOM   11118 C  CA    . PHE C 2 38  ? 133.654 76.855  115.197 1.00 40.67 ?  17  PHE C CA    1 
ATOM   11119 C  C     . PHE C 2 38  ? 133.581 77.991  116.225 1.00 39.46 ?  17  PHE C C     1 
ATOM   11120 O  O     . PHE C 2 38  ? 132.790 78.921  116.052 1.00 39.17 ?  17  PHE C O     1 
ATOM   11121 C  CB    . PHE C 2 38  ? 132.455 75.906  115.373 1.00 40.24 ?  17  PHE C CB    1 
ATOM   11122 C  CG    . PHE C 2 38  ? 132.573 74.974  116.557 1.00 39.58 ?  17  PHE C CG    1 
ATOM   11123 C  CD1   . PHE C 2 38  ? 132.149 75.376  117.824 1.00 38.78 ?  17  PHE C CD1   1 
ATOM   11124 C  CD2   . PHE C 2 38  ? 133.095 73.689  116.403 1.00 39.43 ?  17  PHE C CD2   1 
ATOM   11125 C  CE1   . PHE C 2 38  ? 132.245 74.518  118.920 1.00 38.07 ?  17  PHE C CE1   1 
ATOM   11126 C  CE2   . PHE C 2 38  ? 133.196 72.821  117.494 1.00 39.10 ?  17  PHE C CE2   1 
ATOM   11127 C  CZ    . PHE C 2 38  ? 132.771 73.239  118.756 1.00 38.63 ?  17  PHE C CZ    1 
ATOM   11128 N  N     . THR C 2 39  ? 134.385 77.917  117.288 1.00 38.22 ?  18  THR C N     1 
ATOM   11129 C  CA    . THR C 2 39  ? 134.274 78.885  118.393 1.00 37.09 ?  18  THR C CA    1 
ATOM   11130 C  C     . THR C 2 39  ? 134.425 80.345  117.932 1.00 36.84 ?  18  THR C C     1 
ATOM   11131 O  O     . THR C 2 39  ? 133.625 81.209  118.326 1.00 36.13 ?  18  THR C O     1 
ATOM   11132 C  CB    . THR C 2 39  ? 135.202 78.543  119.595 1.00 36.59 ?  18  THR C CB    1 
ATOM   11133 O  OG1   . THR C 2 39  ? 134.657 77.425  120.301 1.00 36.50 ?  18  THR C OG1   1 
ATOM   11134 C  CG2   . THR C 2 39  ? 135.288 79.702  120.568 1.00 36.06 ?  18  THR C CG2   1 
ATOM   11135 N  N     . GLN C 2 40  ? 135.428 80.607  117.088 1.00 37.01 ?  19  GLN C N     1 
ATOM   11136 C  CA    . GLN C 2 40  ? 135.679 81.969  116.593 1.00 37.33 ?  19  GLN C CA    1 
ATOM   11137 C  C     . GLN C 2 40  ? 134.489 82.571  115.866 1.00 36.63 ?  19  GLN C C     1 
ATOM   11138 O  O     . GLN C 2 40  ? 134.158 83.737  116.076 1.00 36.10 ?  19  GLN C O     1 
ATOM   11139 C  CB    . GLN C 2 40  ? 136.923 82.038  115.707 1.00 38.24 ?  19  GLN C CB    1 
ATOM   11140 C  CG    . GLN C 2 40  ? 138.204 82.150  116.501 1.00 41.33 ?  19  GLN C CG    1 
ATOM   11141 C  CD    . GLN C 2 40  ? 139.248 83.021  115.831 1.00 45.15 ?  19  GLN C CD    1 
ATOM   11142 O  OE1   . GLN C 2 40  ? 139.351 83.064  114.599 1.00 47.33 ?  19  GLN C OE1   1 
ATOM   11143 N  NE2   . GLN C 2 40  ? 140.036 83.724  116.643 1.00 46.51 ?  19  GLN C NE2   1 
ATOM   11144 N  N     . MET C 2 41  ? 133.838 81.770  115.027 1.00 36.23 ?  20  MET C N     1 
ATOM   11145 C  CA    . MET C 2 41  ? 132.661 82.245  114.314 1.00 36.40 ?  20  MET C CA    1 
ATOM   11146 C  C     . MET C 2 41  ? 131.457 82.442  115.255 1.00 34.93 ?  20  MET C C     1 
ATOM   11147 O  O     . MET C 2 41  ? 130.674 83.369  115.063 1.00 34.20 ?  20  MET C O     1 
ATOM   11148 C  CB    . MET C 2 41  ? 132.357 81.390  113.063 1.00 37.35 ?  20  MET C CB    1 
ATOM   11149 C  CG    . MET C 2 41  ? 131.499 80.152  113.246 1.00 40.49 ?  20  MET C CG    1 
ATOM   11150 S  SD    . MET C 2 41  ? 131.079 79.422  111.632 1.00 48.68 ?  20  MET C SD    1 
ATOM   11151 C  CE    . MET C 2 41  ? 132.500 78.361  111.338 1.00 47.17 ?  20  MET C CE    1 
ATOM   11152 N  N     . PHE C 2 42  ? 131.344 81.608  116.291 1.00 33.75 ?  21  PHE C N     1 
ATOM   11153 C  CA    . PHE C 2 42  ? 130.325 81.830  117.328 1.00 32.62 ?  21  PHE C CA    1 
ATOM   11154 C  C     . PHE C 2 42  ? 130.626 83.060  118.176 1.00 32.59 ?  21  PHE C C     1 
ATOM   11155 O  O     . PHE C 2 42  ? 129.715 83.816  118.527 1.00 32.23 ?  21  PHE C O     1 
ATOM   11156 C  CB    . PHE C 2 42  ? 130.124 80.592  118.200 1.00 32.12 ?  21  PHE C CB    1 
ATOM   11157 C  CG    . PHE C 2 42  ? 129.219 79.566  117.583 1.00 31.04 ?  21  PHE C CG    1 
ATOM   11158 C  CD1   . PHE C 2 42  ? 127.857 79.550  117.880 1.00 30.75 ?  21  PHE C CD1   1 
ATOM   11159 C  CD2   . PHE C 2 42  ? 129.723 78.619  116.698 1.00 30.99 ?  21  PHE C CD2   1 
ATOM   11160 C  CE1   . PHE C 2 42  ? 127.008 78.599  117.304 1.00 30.30 ?  21  PHE C CE1   1 
ATOM   11161 C  CE2   . PHE C 2 42  ? 128.882 77.659  116.111 1.00 30.74 ?  21  PHE C CE2   1 
ATOM   11162 C  CZ    . PHE C 2 42  ? 127.525 77.651  116.415 1.00 30.48 ?  21  PHE C CZ    1 
ATOM   11163 N  N     . TYR C 2 43  ? 131.905 83.262  118.492 1.00 32.33 ?  22  TYR C N     1 
ATOM   11164 C  CA    . TYR C 2 43  ? 132.331 84.469  119.197 1.00 32.50 ?  22  TYR C CA    1 
ATOM   11165 C  C     . TYR C 2 43  ? 131.899 85.715  118.426 1.00 33.01 ?  22  TYR C C     1 
ATOM   11166 O  O     . TYR C 2 43  ? 131.272 86.614  118.993 1.00 32.50 ?  22  TYR C O     1 
ATOM   11167 C  CB    . TYR C 2 43  ? 133.850 84.481  119.454 1.00 32.53 ?  22  TYR C CB    1 
ATOM   11168 C  CG    . TYR C 2 43  ? 134.337 85.828  119.959 1.00 33.27 ?  22  TYR C CG    1 
ATOM   11169 C  CD1   . TYR C 2 43  ? 134.209 86.179  121.305 1.00 32.34 ?  22  TYR C CD1   1 
ATOM   11170 C  CD2   . TYR C 2 43  ? 134.887 86.764  119.080 1.00 33.71 ?  22  TYR C CD2   1 
ATOM   11171 C  CE1   . TYR C 2 43  ? 134.635 87.424  121.768 1.00 33.58 ?  22  TYR C CE1   1 
ATOM   11172 C  CE2   . TYR C 2 43  ? 135.311 88.016  119.528 1.00 35.12 ?  22  TYR C CE2   1 
ATOM   11173 C  CZ    . TYR C 2 43  ? 135.186 88.337  120.874 1.00 35.30 ?  22  TYR C CZ    1 
ATOM   11174 O  OH    . TYR C 2 43  ? 135.607 89.572  121.316 1.00 36.54 ?  22  TYR C OH    1 
ATOM   11175 N  N     . ASN C 2 44  ? 132.224 85.750  117.132 1.00 33.80 ?  23  ASN C N     1 
ATOM   11176 C  CA    . ASN C 2 44  ? 131.894 86.886  116.281 1.00 34.80 ?  23  ASN C CA    1 
ATOM   11177 C  C     . ASN C 2 44  ? 130.386 87.089  116.154 1.00 34.40 ?  23  ASN C C     1 
ATOM   11178 O  O     . ASN C 2 44  ? 129.906 88.216  116.223 1.00 33.99 ?  23  ASN C O     1 
ATOM   11179 C  CB    . ASN C 2 44  ? 132.547 86.750  114.896 1.00 35.46 ?  23  ASN C CB    1 
ATOM   11180 C  CG    . ASN C 2 44  ? 134.082 86.751  114.952 1.00 38.28 ?  23  ASN C CG    1 
ATOM   11181 O  OD1   . ASN C 2 44  ? 134.698 87.264  115.898 1.00 41.01 ?  23  ASN C OD1   1 
ATOM   11182 N  ND2   . ASN C 2 44  ? 134.703 86.177  113.923 1.00 39.13 ?  23  ASN C ND2   1 
ATOM   11183 N  N     . GLN C 2 45  ? 129.645 85.993  115.988 1.00 34.49 ?  24  GLN C N     1 
ATOM   11184 C  CA    . GLN C 2 45  ? 128.191 86.059  115.881 1.00 34.81 ?  24  GLN C CA    1 
ATOM   11185 C  C     . GLN C 2 45  ? 127.550 86.558  117.182 1.00 34.68 ?  24  GLN C C     1 
ATOM   11186 O  O     . GLN C 2 45  ? 126.669 87.420  117.152 1.00 34.59 ?  24  GLN C O     1 
ATOM   11187 C  CB    . GLN C 2 45  ? 127.614 84.703  115.461 1.00 34.83 ?  24  GLN C CB    1 
ATOM   11188 C  CG    . GLN C 2 45  ? 126.169 84.754  114.956 1.00 36.14 ?  24  GLN C CG    1 
ATOM   11189 C  CD    . GLN C 2 45  ? 125.986 85.626  113.711 1.00 38.04 ?  24  GLN C CD    1 
ATOM   11190 O  OE1   . GLN C 2 45  ? 126.899 85.780  112.895 1.00 38.57 ?  24  GLN C OE1   1 
ATOM   11191 N  NE2   . GLN C 2 45  ? 124.793 86.204  113.567 1.00 38.67 ?  24  GLN C NE2   1 
ATOM   11192 N  N     . ASN C 2 46  ? 128.002 86.035  118.319 1.00 34.71 ?  25  ASN C N     1 
ATOM   11193 C  CA    . ASN C 2 46  ? 127.461 86.464  119.609 1.00 34.99 ?  25  ASN C CA    1 
ATOM   11194 C  C     . ASN C 2 46  ? 127.686 87.950  119.880 1.00 35.69 ?  25  ASN C C     1 
ATOM   11195 O  O     . ASN C 2 46  ? 126.752 88.670  120.249 1.00 35.41 ?  25  ASN C O     1 
ATOM   11196 C  CB    . ASN C 2 46  ? 127.997 85.600  120.757 1.00 34.64 ?  25  ASN C CB    1 
ATOM   11197 C  CG    . ASN C 2 46  ? 127.244 84.295  120.897 1.00 34.71 ?  25  ASN C CG    1 
ATOM   11198 O  OD1   . ASN C 2 46  ? 126.285 84.211  121.660 1.00 35.68 ?  25  ASN C OD1   1 
ATOM   11199 N  ND2   . ASN C 2 46  ? 127.647 83.276  120.131 1.00 34.71 ?  25  ASN C ND2   1 
ATOM   11200 N  N     . VAL C 2 47  ? 128.913 88.420  119.673 1.00 36.69 ?  26  VAL C N     1 
ATOM   11201 C  CA    . VAL C 2 47  ? 129.218 89.825  119.950 1.00 38.00 ?  26  VAL C CA    1 
ATOM   11202 C  C     . VAL C 2 47  ? 128.549 90.788  118.960 1.00 38.90 ?  26  VAL C C     1 
ATOM   11203 O  O     . VAL C 2 47  ? 128.209 91.909  119.329 1.00 39.46 ?  26  VAL C O     1 
ATOM   11204 C  CB    . VAL C 2 47  ? 130.738 90.109  120.086 1.00 38.16 ?  26  VAL C CB    1 
ATOM   11205 C  CG1   . VAL C 2 47  ? 131.331 89.257  121.191 1.00 37.75 ?  26  VAL C CG1   1 
ATOM   11206 C  CG2   . VAL C 2 47  ? 131.472 89.893  118.764 1.00 38.81 ?  26  VAL C CG2   1 
ATOM   11207 N  N     . LYS C 2 48  ? 128.330 90.342  117.722 1.00 39.67 ?  27  LYS C N     1 
ATOM   11208 C  CA    . LYS C 2 48  ? 127.651 91.179  116.729 1.00 40.50 ?  27  LYS C CA    1 
ATOM   11209 C  C     . LYS C 2 48  ? 126.134 91.212  116.953 1.00 40.02 ?  27  LYS C C     1 
ATOM   11210 O  O     . LYS C 2 48  ? 125.433 92.063  116.402 1.00 40.55 ?  27  LYS C O     1 
ATOM   11211 C  CB    . LYS C 2 48  ? 127.995 90.740  115.293 1.00 41.23 ?  27  LYS C CB    1 
ATOM   11212 C  CG    . LYS C 2 48  ? 127.152 89.587  114.750 1.00 42.50 ?  27  LYS C CG    1 
ATOM   11213 C  CD    . LYS C 2 48  ? 127.494 89.240  113.294 1.00 44.92 ?  27  LYS C CD    1 
ATOM   11214 C  CE    . LYS C 2 48  ? 126.831 90.193  112.301 1.00 46.66 ?  27  LYS C CE    1 
ATOM   11215 N  NZ    . LYS C 2 48  ? 125.342 90.161  112.398 1.00 47.26 1  27  LYS C NZ    1 
ATOM   11216 N  N     . GLN C 2 49  ? 125.629 90.279  117.752 1.00 39.10 ?  28  GLN C N     1 
ATOM   11217 C  CA    . GLN C 2 49  ? 124.218 90.250  118.071 1.00 38.22 ?  28  GLN C CA    1 
ATOM   11218 C  C     . GLN C 2 49  ? 123.906 91.043  119.340 1.00 37.23 ?  28  GLN C C     1 
ATOM   11219 O  O     . GLN C 2 49  ? 122.744 91.125  119.731 1.00 37.40 ?  28  GLN C O     1 
ATOM   11220 C  CB    . GLN C 2 49  ? 123.701 88.805  118.178 1.00 38.69 ?  28  GLN C CB    1 
ATOM   11221 C  CG    . GLN C 2 49  ? 123.553 88.093  116.824 1.00 39.57 ?  28  GLN C CG    1 
ATOM   11222 C  CD    . GLN C 2 49  ? 122.860 86.736  116.913 1.00 41.20 ?  28  GLN C CD    1 
ATOM   11223 O  OE1   . GLN C 2 49  ? 122.749 86.028  115.911 1.00 42.94 ?  28  GLN C OE1   1 
ATOM   11224 N  NE2   . GLN C 2 49  ? 122.392 86.367  118.109 1.00 41.23 ?  28  GLN C NE2   1 
ATOM   11225 N  N     . PHE C 2 50  ? 124.928 91.640  119.963 1.00 35.83 ?  29  PHE C N     1 
ATOM   11226 C  CA    . PHE C 2 50  ? 124.734 92.354  121.233 1.00 34.51 ?  29  PHE C CA    1 
ATOM   11227 C  C     . PHE C 2 50  ? 123.645 93.428  121.161 1.00 33.81 ?  29  PHE C C     1 
ATOM   11228 O  O     . PHE C 2 50  ? 123.605 94.214  120.214 1.00 33.66 ?  29  PHE C O     1 
ATOM   11229 C  CB    . PHE C 2 50  ? 126.036 92.959  121.768 1.00 34.59 ?  29  PHE C CB    1 
ATOM   11230 C  CG    . PHE C 2 50  ? 125.870 93.673  123.098 1.00 34.59 ?  29  PHE C CG    1 
ATOM   11231 C  CD1   . PHE C 2 50  ? 125.664 92.950  124.278 1.00 34.34 ?  29  PHE C CD1   1 
ATOM   11232 C  CD2   . PHE C 2 50  ? 125.899 95.066  123.166 1.00 35.49 ?  29  PHE C CD2   1 
ATOM   11233 C  CE1   . PHE C 2 50  ? 125.503 93.604  125.509 1.00 33.88 ?  29  PHE C CE1   1 
ATOM   11234 C  CE2   . PHE C 2 50  ? 125.735 95.735  124.393 1.00 34.12 ?  29  PHE C CE2   1 
ATOM   11235 C  CZ    . PHE C 2 50  ? 125.538 95.004  125.564 1.00 33.87 ?  29  PHE C CZ    1 
ATOM   11236 N  N     . TRP C 2 51  ? 122.778 93.449  122.175 1.00 32.24 ?  30  TRP C N     1 
ATOM   11237 C  CA    . TRP C 2 51  ? 121.666 94.395  122.246 1.00 31.28 ?  30  TRP C CA    1 
ATOM   11238 C  C     . TRP C 2 51  ? 121.251 94.673  123.693 1.00 31.12 ?  30  TRP C C     1 
ATOM   11239 O  O     . TRP C 2 51  ? 121.633 93.931  124.605 1.00 30.71 ?  30  TRP C O     1 
ATOM   11240 C  CB    . TRP C 2 51  ? 120.470 93.883  121.431 1.00 30.85 ?  30  TRP C CB    1 
ATOM   11241 C  CG    . TRP C 2 51  ? 119.896 92.579  121.929 1.00 29.31 ?  30  TRP C CG    1 
ATOM   11242 C  CD1   . TRP C 2 51  ? 120.356 91.319  121.659 1.00 29.07 ?  30  TRP C CD1   1 
ATOM   11243 C  CD2   . TRP C 2 51  ? 118.772 92.415  122.799 1.00 28.33 ?  30  TRP C CD2   1 
ATOM   11244 N  NE1   . TRP C 2 51  ? 119.582 90.383  122.298 1.00 28.01 ?  30  TRP C NE1   1 
ATOM   11245 C  CE2   . TRP C 2 51  ? 118.601 91.027  123.005 1.00 27.67 ?  30  TRP C CE2   1 
ATOM   11246 C  CE3   . TRP C 2 51  ? 117.892 93.306  123.430 1.00 27.27 ?  30  TRP C CE3   1 
ATOM   11247 C  CZ2   . TRP C 2 51  ? 117.589 90.509  123.813 1.00 26.54 ?  30  TRP C CZ2   1 
ATOM   11248 C  CZ3   . TRP C 2 51  ? 116.878 92.791  124.226 1.00 27.07 ?  30  TRP C CZ3   1 
ATOM   11249 C  CH2   . TRP C 2 51  ? 116.740 91.403  124.416 1.00 26.52 ?  30  TRP C CH2   1 
ATOM   11250 N  N     . LEU C 2 52  ? 120.476 95.745  123.887 1.00 30.65 ?  31  LEU C N     1 
ATOM   11251 C  CA    . LEU C 2 52  ? 119.872 96.083  125.178 1.00 30.38 ?  31  LEU C CA    1 
ATOM   11252 C  C     . LEU C 2 52  ? 118.390 96.392  124.984 1.00 30.51 ?  31  LEU C C     1 
ATOM   11253 O  O     . LEU C 2 52  ? 118.026 97.007  123.981 1.00 30.77 ?  31  LEU C O     1 
ATOM   11254 C  CB    . LEU C 2 52  ? 120.577 97.294  125.812 1.00 30.45 ?  31  LEU C CB    1 
ATOM   11255 C  CG    . LEU C 2 52  ? 122.043 97.083  126.201 1.00 30.29 ?  31  LEU C CG    1 
ATOM   11256 C  CD1   . LEU C 2 52  ? 122.795 98.410  126.375 1.00 30.69 ?  31  LEU C CD1   1 
ATOM   11257 C  CD2   . LEU C 2 52  ? 122.161 96.199  127.452 1.00 29.91 ?  31  LEU C CD2   1 
ATOM   11258 N  N     . PRO C 2 53  ? 117.528 95.978  125.941 1.00 30.73 ?  32  PRO C N     1 
ATOM   11259 C  CA    . PRO C 2 53  ? 116.080 96.208  125.798 1.00 31.17 ?  32  PRO C CA    1 
ATOM   11260 C  C     . PRO C 2 53  ? 115.710 97.679  125.621 1.00 32.18 ?  32  PRO C C     1 
ATOM   11261 O  O     . PRO C 2 53  ? 114.718 97.983  124.938 1.00 32.66 ?  32  PRO C O     1 
ATOM   11262 C  CB    . PRO C 2 53  ? 115.498 95.671  127.110 1.00 30.99 ?  32  PRO C CB    1 
ATOM   11263 C  CG    . PRO C 2 53  ? 116.672 95.552  128.054 1.00 30.50 ?  32  PRO C CG    1 
ATOM   11264 C  CD    . PRO C 2 53  ? 117.840 95.241  127.182 1.00 30.46 ?  32  PRO C CD    1 
ATOM   11265 N  N     . GLU C 2 54  ? 116.506 98.574  126.211 1.00 32.62 ?  33  GLU C N     1 
ATOM   11266 C  CA    . GLU C 2 54  ? 116.275 100.024 126.113 1.00 33.44 ?  33  GLU C CA    1 
ATOM   11267 C  C     . GLU C 2 54  ? 116.352 100.566 124.680 1.00 33.59 ?  33  GLU C C     1 
ATOM   11268 O  O     . GLU C 2 54  ? 115.897 101.676 124.418 1.00 34.05 ?  33  GLU C O     1 
ATOM   11269 C  CB    . GLU C 2 54  ? 117.239 100.811 127.020 1.00 33.72 ?  33  GLU C CB    1 
ATOM   11270 C  CG    . GLU C 2 54  ? 116.950 100.698 128.530 1.00 34.53 ?  33  GLU C CG    1 
ATOM   11271 C  CD    . GLU C 2 54  ? 117.367 99.351  129.123 1.00 35.09 ?  33  GLU C CD    1 
ATOM   11272 O  OE1   . GLU C 2 54  ? 118.242 98.669  128.531 1.00 34.38 ?  33  GLU C OE1   1 
ATOM   11273 O  OE2   . GLU C 2 54  ? 116.815 98.976  130.182 1.00 35.53 -1 33  GLU C OE2   1 
ATOM   11274 N  N     . GLU C 2 55  ? 116.928 99.785  123.764 1.00 33.82 ?  34  GLU C N     1 
ATOM   11275 C  CA    . GLU C 2 55  ? 116.972 100.146 122.344 1.00 34.19 ?  34  GLU C CA    1 
ATOM   11276 C  C     . GLU C 2 55  ? 115.571 100.133 121.714 1.00 33.83 ?  34  GLU C C     1 
ATOM   11277 O  O     . GLU C 2 55  ? 115.347 100.758 120.679 1.00 33.93 ?  34  GLU C O     1 
ATOM   11278 C  CB    . GLU C 2 55  ? 117.887 99.195  121.551 1.00 34.52 ?  34  GLU C CB    1 
ATOM   11279 C  CG    . GLU C 2 55  ? 119.360 99.195  121.950 1.00 36.50 ?  34  GLU C CG    1 
ATOM   11280 C  CD    . GLU C 2 55  ? 120.232 98.446  120.947 1.00 40.03 ?  34  GLU C CD    1 
ATOM   11281 O  OE1   . GLU C 2 55  ? 120.648 99.051  119.934 1.00 42.43 ?  34  GLU C OE1   1 
ATOM   11282 O  OE2   . GLU C 2 55  ? 120.513 97.252  121.171 1.00 39.35 -1 34  GLU C OE2   1 
ATOM   11283 N  N     . ILE C 2 56  ? 114.654 99.391  122.336 1.00 33.31 ?  35  ILE C N     1 
ATOM   11284 C  CA    . ILE C 2 56  ? 113.281 99.217  121.857 1.00 33.14 ?  35  ILE C CA    1 
ATOM   11285 C  C     . ILE C 2 56  ? 112.330 99.995  122.772 1.00 32.58 ?  35  ILE C C     1 
ATOM   11286 O  O     . ILE C 2 56  ? 112.235 99.699  123.957 1.00 32.12 ?  35  ILE C O     1 
ATOM   11287 C  CB    . ILE C 2 56  ? 112.868 97.704  121.867 1.00 33.03 ?  35  ILE C CB    1 
ATOM   11288 C  CG1   . ILE C 2 56  ? 113.901 96.817  121.138 1.00 34.76 ?  35  ILE C CG1   1 
ATOM   11289 C  CG2   . ILE C 2 56  ? 111.451 97.501  121.317 1.00 33.61 ?  35  ILE C CG2   1 
ATOM   11290 C  CD1   . ILE C 2 56  ? 114.005 97.022  119.625 1.00 36.75 ?  35  ILE C CD1   1 
ATOM   11291 N  N     . ALA C 2 57  ? 111.639 100.995 122.226 1.00 32.36 ?  36  ALA C N     1 
ATOM   11292 C  CA    . ALA C 2 57  ? 110.637 101.740 122.993 1.00 32.17 ?  36  ALA C CA    1 
ATOM   11293 C  C     . ALA C 2 57  ? 109.345 100.922 123.097 1.00 31.76 ?  36  ALA C C     1 
ATOM   11294 O  O     . ALA C 2 57  ? 108.852 100.400 122.095 1.00 31.95 ?  36  ALA C O     1 
ATOM   11295 C  CB    . ALA C 2 57  ? 110.369 103.089 122.347 1.00 33.01 ?  36  ALA C CB    1 
ATOM   11296 N  N     . LEU C 2 58  ? 108.798 100.813 124.304 1.00 30.68 ?  37  LEU C N     1 
ATOM   11297 C  CA    . LEU C 2 58  ? 107.716 99.862  124.555 1.00 30.14 ?  37  LEU C CA    1 
ATOM   11298 C  C     . LEU C 2 58  ? 106.329 100.481 124.684 1.00 30.21 ?  37  LEU C C     1 
ATOM   11299 O  O     . LEU C 2 58  ? 105.323 99.759  124.672 1.00 29.91 ?  37  LEU C O     1 
ATOM   11300 C  CB    . LEU C 2 58  ? 108.037 99.003  125.784 1.00 29.46 ?  37  LEU C CB    1 
ATOM   11301 C  CG    . LEU C 2 58  ? 109.216 98.033  125.626 1.00 29.08 ?  37  LEU C CG    1 
ATOM   11302 C  CD1   . LEU C 2 58  ? 109.554 97.373  126.950 1.00 29.23 ?  37  LEU C CD1   1 
ATOM   11303 C  CD2   . LEU C 2 58  ? 108.931 96.975  124.561 1.00 28.84 ?  37  LEU C CD2   1 
ATOM   11304 N  N     . ASN C 2 59  ? 106.275 101.806 124.781 1.00 30.50 ?  38  ASN C N     1 
ATOM   11305 C  CA    . ASN C 2 59  ? 105.004 102.513 124.961 1.00 31.23 ?  38  ASN C CA    1 
ATOM   11306 C  C     . ASN C 2 59  ? 104.009 102.319 123.805 1.00 31.03 ?  38  ASN C C     1 
ATOM   11307 O  O     . ASN C 2 59  ? 102.809 102.507 123.981 1.00 30.82 ?  38  ASN C O     1 
ATOM   11308 C  CB    . ASN C 2 59  ? 105.232 104.003 125.283 1.00 31.98 ?  38  ASN C CB    1 
ATOM   11309 C  CG    . ASN C 2 59  ? 106.024 104.731 124.209 1.00 33.59 ?  38  ASN C CG    1 
ATOM   11310 O  OD1   . ASN C 2 59  ? 107.135 104.323 123.849 1.00 36.48 ?  38  ASN C OD1   1 
ATOM   11311 N  ND2   . ASN C 2 59  ? 105.462 105.824 123.700 1.00 34.77 ?  38  ASN C ND2   1 
ATOM   11312 N  N     . GLY C 2 60  ? 104.516 101.908 122.644 1.00 30.88 ?  39  GLY C N     1 
ATOM   11313 C  CA    . GLY C 2 60  ? 103.677 101.552 121.494 1.00 31.37 ?  39  GLY C CA    1 
ATOM   11314 C  C     . GLY C 2 60  ? 102.781 100.334 121.684 1.00 31.05 ?  39  GLY C C     1 
ATOM   11315 O  O     . GLY C 2 60  ? 101.743 100.241 121.044 1.00 31.21 ?  39  GLY C O     1 
ATOM   11316 N  N     . ASP C 2 61  ? 103.172 99.407  122.563 1.00 30.63 ?  40  ASP C N     1 
ATOM   11317 C  CA    . ASP C 2 61  ? 102.325 98.251  122.918 1.00 30.65 ?  40  ASP C CA    1 
ATOM   11318 C  C     . ASP C 2 61  ? 101.185 98.561  123.894 1.00 31.00 ?  40  ASP C C     1 
ATOM   11319 O  O     . ASP C 2 61  ? 100.339 97.697  124.132 1.00 30.91 ?  40  ASP C O     1 
ATOM   11320 C  CB    . ASP C 2 61  ? 103.162 97.122  123.531 1.00 30.00 ?  40  ASP C CB    1 
ATOM   11321 C  CG    . ASP C 2 61  ? 104.120 96.492  122.549 1.00 30.88 ?  40  ASP C CG    1 
ATOM   11322 O  OD1   . ASP C 2 61  ? 104.177 96.925  121.373 1.00 30.42 ?  40  ASP C OD1   1 
ATOM   11323 O  OD2   . ASP C 2 61  ? 104.830 95.553  122.970 1.00 31.17 -1 40  ASP C OD2   1 
ATOM   11324 N  N     . LEU C 2 62  ? 101.171 99.763  124.466 1.00 31.54 ?  41  LEU C N     1 
ATOM   11325 C  CA    . LEU C 2 62  ? 100.223 100.102 125.541 1.00 32.47 ?  41  LEU C CA    1 
ATOM   11326 C  C     . LEU C 2 62  ? 98.761  99.853  125.187 1.00 33.21 ?  41  LEU C C     1 
ATOM   11327 O  O     . LEU C 2 62  ? 97.996  99.342  126.012 1.00 32.84 ?  41  LEU C O     1 
ATOM   11328 C  CB    . LEU C 2 62  ? 100.403 101.547 126.010 1.00 33.14 ?  41  LEU C CB    1 
ATOM   11329 C  CG    . LEU C 2 62  ? 101.479 101.821 127.060 1.00 34.44 ?  41  LEU C CG    1 
ATOM   11330 C  CD1   . LEU C 2 62  ? 101.725 103.319 127.173 1.00 35.04 ?  41  LEU C CD1   1 
ATOM   11331 C  CD2   . LEU C 2 62  ? 101.081 101.224 128.416 1.00 35.52 ?  41  LEU C CD2   1 
ATOM   11332 N  N     . LEU C 2 63  ? 98.382  100.211 123.962 1.00 33.75 ?  42  LEU C N     1 
ATOM   11333 C  CA    . LEU C 2 63  ? 97.001  100.047 123.527 1.00 34.79 ?  42  LEU C CA    1 
ATOM   11334 C  C     . LEU C 2 63  ? 96.599  98.616  123.178 1.00 34.66 ?  42  LEU C C     1 
ATOM   11335 O  O     . LEU C 2 63  ? 95.541  98.170  123.617 1.00 34.67 ?  42  LEU C O     1 
ATOM   11336 C  CB    . LEU C 2 63  ? 96.649  101.015 122.395 1.00 35.27 ?  42  LEU C CB    1 
ATOM   11337 C  CG    . LEU C 2 63  ? 96.277  102.421 122.882 1.00 36.82 ?  42  LEU C CG    1 
ATOM   11338 C  CD1   . LEU C 2 63  ? 95.986  103.318 121.684 1.00 37.93 ?  42  LEU C CD1   1 
ATOM   11339 C  CD2   . LEU C 2 63  ? 95.078  102.403 123.828 1.00 37.85 ?  42  LEU C CD2   1 
ATOM   11340 N  N     . THR C 2 64  ? 97.416  97.896  122.404 1.00 34.70 ?  43  THR C N     1 
ATOM   11341 C  CA    . THR C 2 64  ? 97.089  96.491  122.107 1.00 35.10 ?  43  THR C CA    1 
ATOM   11342 C  C     . THR C 2 64  ? 97.078  95.624  123.376 1.00 34.78 ?  43  THR C C     1 
ATOM   11343 O  O     . THR C 2 64  ? 96.377  94.619  123.428 1.00 35.04 ?  43  THR C O     1 
ATOM   11344 C  CB    . THR C 2 64  ? 97.959  95.848  120.981 1.00 35.30 ?  43  THR C CB    1 
ATOM   11345 O  OG1   . THR C 2 64  ? 99.356  95.956  121.295 1.00 36.01 ?  43  THR C OG1   1 
ATOM   11346 C  CG2   . THR C 2 64  ? 97.677  96.504  119.630 1.00 35.96 ?  43  THR C CG2   1 
ATOM   11347 N  N     . TRP C 2 65  ? 97.827  96.034  124.402 1.00 34.63 ?  44  TRP C N     1 
ATOM   11348 C  CA    . TRP C 2 65  ? 97.815  95.350  125.702 1.00 34.37 ?  44  TRP C CA    1 
ATOM   11349 C  C     . TRP C 2 65  ? 96.512  95.614  126.455 1.00 35.13 ?  44  TRP C C     1 
ATOM   11350 O  O     . TRP C 2 65  ? 95.855  94.684  126.941 1.00 34.98 ?  44  TRP C O     1 
ATOM   11351 C  CB    . TRP C 2 65  ? 99.005  95.792  126.552 1.00 33.95 ?  44  TRP C CB    1 
ATOM   11352 C  CG    . TRP C 2 65  ? 98.955  95.308  127.966 1.00 33.26 ?  44  TRP C CG    1 
ATOM   11353 C  CD1   . TRP C 2 65  ? 98.617  96.035  129.073 1.00 32.51 ?  44  TRP C CD1   1 
ATOM   11354 C  CD2   . TRP C 2 65  ? 99.259  93.986  128.429 1.00 30.93 ?  44  TRP C CD2   1 
ATOM   11355 N  NE1   . TRP C 2 65  ? 98.697  95.247  130.201 1.00 31.66 ?  44  TRP C NE1   1 
ATOM   11356 C  CE2   . TRP C 2 65  ? 99.087  93.984  129.833 1.00 30.39 ?  44  TRP C CE2   1 
ATOM   11357 C  CE3   . TRP C 2 65  ? 99.664  92.803  127.794 1.00 30.36 ?  44  TRP C CE3   1 
ATOM   11358 C  CZ2   . TRP C 2 65  ? 99.297  92.845  130.613 1.00 29.16 ?  44  TRP C CZ2   1 
ATOM   11359 C  CZ3   . TRP C 2 65  ? 99.878  91.664  128.573 1.00 28.84 ?  44  TRP C CZ3   1 
ATOM   11360 C  CH2   . TRP C 2 65  ? 99.699  91.698  129.967 1.00 29.34 ?  44  TRP C CH2   1 
ATOM   11361 N  N     . LYS C 2 66  ? 96.161  96.894  126.560 1.00 35.69 ?  45  LYS C N     1 
ATOM   11362 C  CA    . LYS C 2 66  ? 94.914  97.330  127.169 1.00 36.38 ?  45  LYS C CA    1 
ATOM   11363 C  C     . LYS C 2 66  ? 93.701  96.578  126.609 1.00 36.24 ?  45  LYS C C     1 
ATOM   11364 O  O     . LYS C 2 66  ? 92.757  96.312  127.344 1.00 36.78 ?  45  LYS C O     1 
ATOM   11365 C  CB    . LYS C 2 66  ? 94.750  98.835  126.944 1.00 37.14 ?  45  LYS C CB    1 
ATOM   11366 C  CG    . LYS C 2 66  ? 93.512  99.458  127.565 1.00 38.91 ?  45  LYS C CG    1 
ATOM   11367 C  CD    . LYS C 2 66  ? 93.330  100.891 127.063 1.00 41.12 ?  45  LYS C CD    1 
ATOM   11368 C  CE    . LYS C 2 66  ? 92.323  101.648 127.913 1.00 43.00 ?  45  LYS C CE    1 
ATOM   11369 N  NZ    . LYS C 2 66  ? 92.623  101.507 129.371 1.00 44.38 1  45  LYS C NZ    1 
ATOM   11370 N  N     . TYR C 2 67  ? 93.767  96.214  125.325 1.00 36.03 ?  46  TYR C N     1 
ATOM   11371 C  CA    . TYR C 2 67  ? 92.652  95.613  124.575 1.00 36.03 ?  46  TYR C CA    1 
ATOM   11372 C  C     . TYR C 2 67  ? 92.497  94.095  124.733 1.00 35.25 ?  46  TYR C C     1 
ATOM   11373 O  O     . TYR C 2 67  ? 91.485  93.521  124.316 1.00 35.32 ?  46  TYR C O     1 
ATOM   11374 C  CB    . TYR C 2 67  ? 92.783  95.928  123.074 1.00 36.60 ?  46  TYR C CB    1 
ATOM   11375 C  CG    . TYR C 2 67  ? 92.726  97.405  122.703 1.00 37.85 ?  46  TYR C CG    1 
ATOM   11376 C  CD1   . TYR C 2 67  ? 92.270  98.360  123.610 1.00 38.97 ?  46  TYR C CD1   1 
ATOM   11377 C  CD2   . TYR C 2 67  ? 93.118  97.839  121.428 1.00 40.06 ?  46  TYR C CD2   1 
ATOM   11378 C  CE1   . TYR C 2 67  ? 92.224  99.713  123.279 1.00 40.36 ?  46  TYR C CE1   1 
ATOM   11379 C  CE2   . TYR C 2 67  ? 93.071  99.199  121.081 1.00 40.53 ?  46  TYR C CE2   1 
ATOM   11380 C  CZ    . TYR C 2 67  ? 92.618  100.128 122.017 1.00 41.43 ?  46  TYR C CZ    1 
ATOM   11381 O  OH    . TYR C 2 67  ? 92.549  101.474 121.706 1.00 41.48 ?  46  TYR C OH    1 
ATOM   11382 N  N     . LEU C 2 68  ? 93.504  93.443  125.308 1.00 33.80 ?  47  LEU C N     1 
ATOM   11383 C  CA    . LEU C 2 68  ? 93.444  92.002  125.529 1.00 32.77 ?  47  LEU C CA    1 
ATOM   11384 C  C     . LEU C 2 68  ? 92.510  91.685  126.689 1.00 31.84 ?  47  LEU C C     1 
ATOM   11385 O  O     . LEU C 2 68  ? 92.378  92.476  127.619 1.00 31.90 ?  47  LEU C O     1 
ATOM   11386 C  CB    . LEU C 2 68  ? 94.835  91.440  125.830 1.00 32.39 ?  47  LEU C CB    1 
ATOM   11387 C  CG    . LEU C 2 68  ? 95.956  91.482  124.789 1.00 32.68 ?  47  LEU C CG    1 
ATOM   11388 C  CD1   . LEU C 2 68  ? 97.218  90.863  125.383 1.00 33.03 ?  47  LEU C CD1   1 
ATOM   11389 C  CD2   . LEU C 2 68  ? 95.573  90.774  123.485 1.00 32.78 ?  47  LEU C CD2   1 
ATOM   11390 N  N     . GLY C 2 69  ? 91.879  90.517  126.639 1.00 30.99 ?  48  GLY C N     1 
ATOM   11391 C  CA    . GLY C 2 69  ? 91.076  90.037  127.762 1.00 30.58 ?  48  GLY C CA    1 
ATOM   11392 C  C     . GLY C 2 69  ? 91.915  89.770  129.005 1.00 29.87 ?  48  GLY C C     1 
ATOM   11393 O  O     . GLY C 2 69  ? 93.134  89.627  128.921 1.00 28.79 ?  48  GLY C O     1 
ATOM   11394 N  N     . LYS C 2 70  ? 91.264  89.713  130.162 1.00 29.89 ?  49  LYS C N     1 
ATOM   11395 C  CA    . LYS C 2 70  ? 91.963  89.437  131.416 1.00 29.49 ?  49  LYS C CA    1 
ATOM   11396 C  C     . LYS C 2 70  ? 92.694  88.082  131.386 1.00 28.74 ?  49  LYS C C     1 
ATOM   11397 O  O     . LYS C 2 70  ? 93.821  87.973  131.887 1.00 27.27 ?  49  LYS C O     1 
ATOM   11398 C  CB    . LYS C 2 70  ? 91.009  89.547  132.609 1.00 30.67 ?  49  LYS C CB    1 
ATOM   11399 C  CG    . LYS C 2 70  ? 90.742  91.012  133.037 1.00 33.73 ?  49  LYS C CG    1 
ATOM   11400 C  CD    . LYS C 2 70  ? 89.501  91.165  133.932 1.00 38.93 ?  49  LYS C CD    1 
ATOM   11401 C  CE    . LYS C 2 70  ? 89.752  90.765  135.392 1.00 41.04 ?  49  LYS C CE    1 
ATOM   11402 N  NZ    . LYS C 2 70  ? 90.596  91.744  136.141 1.00 42.21 1  49  LYS C NZ    1 
ATOM   11403 N  N     . ASN C 2 71  ? 92.054  87.075  130.782 1.00 27.54 ?  50  ASN C N     1 
ATOM   11404 C  CA    . ASN C 2 71  ? 92.666  85.758  130.589 1.00 27.00 ?  50  ASN C CA    1 
ATOM   11405 C  C     . ASN C 2 71  ? 93.952  85.822  129.765 1.00 26.19 ?  50  ASN C C     1 
ATOM   11406 O  O     . ASN C 2 71  ? 94.957  85.158  130.097 1.00 25.38 ?  50  ASN C O     1 
ATOM   11407 C  CB    . ASN C 2 71  ? 91.669  84.770  129.941 1.00 27.08 ?  50  ASN C CB    1 
ATOM   11408 C  CG    . ASN C 2 71  ? 91.163  85.226  128.552 1.00 28.69 ?  50  ASN C CG    1 
ATOM   11409 O  OD1   . ASN C 2 71  ? 90.816  86.403  128.333 1.00 30.45 ?  50  ASN C OD1   1 
ATOM   11410 N  ND2   . ASN C 2 71  ? 91.092  84.271  127.611 1.00 29.42 ?  50  ASN C ND2   1 
ATOM   11411 N  N     . GLU C 2 72  ? 93.914  86.619  128.699 1.00 24.91 ?  51  GLU C N     1 
ATOM   11412 C  CA    . GLU C 2 72  ? 95.053  86.761  127.800 1.00 24.97 ?  51  GLU C CA    1 
ATOM   11413 C  C     . GLU C 2 72  ? 96.229  87.459  128.491 1.00 24.45 ?  51  GLU C C     1 
ATOM   11414 O  O     . GLU C 2 72  ? 97.383  87.017  128.373 1.00 23.90 ?  51  GLU C O     1 
ATOM   11415 C  CB    . GLU C 2 72  ? 94.641  87.515  126.535 1.00 25.27 ?  51  GLU C CB    1 
ATOM   11416 C  CG    . GLU C 2 72  ? 93.638  86.764  125.662 1.00 26.16 ?  51  GLU C CG    1 
ATOM   11417 C  CD    . GLU C 2 72  ? 93.222  87.578  124.444 1.00 28.70 ?  51  GLU C CD    1 
ATOM   11418 O  OE1   . GLU C 2 72  ? 92.408  88.510  124.601 1.00 28.70 ?  51  GLU C OE1   1 
ATOM   11419 O  OE2   . GLU C 2 72  ? 93.709  87.286  123.328 1.00 28.92 -1 51  GLU C OE2   1 
ATOM   11420 N  N     . GLN C 2 73  ? 95.925  88.529  129.225 1.00 23.75 ?  52  GLN C N     1 
ATOM   11421 C  CA    . GLN C 2 73  ? 96.946  89.268  129.963 1.00 23.94 ?  52  GLN C CA    1 
ATOM   11422 C  C     . GLN C 2 73  ? 97.579  88.396  131.050 1.00 23.36 ?  52  GLN C C     1 
ATOM   11423 O  O     . GLN C 2 73  ? 98.782  88.463  131.272 1.00 22.95 ?  52  GLN C O     1 
ATOM   11424 C  CB    . GLN C 2 73  ? 96.357  90.535  130.602 1.00 24.28 ?  52  GLN C CB    1 
ATOM   11425 C  CG    . GLN C 2 73  ? 96.030  91.677  129.620 1.00 25.22 ?  52  GLN C CG    1 
ATOM   11426 C  CD    . GLN C 2 73  ? 95.537  92.949  130.321 1.00 29.02 ?  52  GLN C CD    1 
ATOM   11427 O  OE1   . GLN C 2 73  ? 95.420  92.993  131.544 1.00 32.08 ?  52  GLN C OE1   1 
ATOM   11428 N  NE2   . GLN C 2 73  ? 95.249  93.984  129.540 1.00 29.13 ?  52  GLN C NE2   1 
ATOM   11429 N  N     . ASP C 2 74  ? 96.750  87.608  131.737 1.00 23.02 ?  53  ASP C N     1 
ATOM   11430 C  CA    . ASP C 2 74  ? 97.214  86.716  132.791 1.00 23.44 ?  53  ASP C CA    1 
ATOM   11431 C  C     . ASP C 2 74  ? 98.201  85.685  132.230 1.00 23.00 ?  53  ASP C C     1 
ATOM   11432 O  O     . ASP C 2 74  ? 99.282  85.500  132.782 1.00 22.96 ?  53  ASP C O     1 
ATOM   11433 C  CB    . ASP C 2 74  ? 96.030  86.002  133.456 1.00 23.31 ?  53  ASP C CB    1 
ATOM   11434 C  CG    . ASP C 2 74  ? 96.442  85.195  134.671 1.00 25.80 ?  53  ASP C CG    1 
ATOM   11435 O  OD1   . ASP C 2 74  ? 96.970  85.788  135.647 1.00 27.95 ?  53  ASP C OD1   1 
ATOM   11436 O  OD2   . ASP C 2 74  ? 96.228  83.967  134.654 1.00 26.30 -1 53  ASP C OD2   1 
ATOM   11437 N  N     . THR C 2 75  ? 97.811  85.015  131.148 1.00 22.20 ?  54  THR C N     1 
ATOM   11438 C  CA    . THR C 2 75  ? 98.662  84.023  130.505 1.00 21.84 ?  54  THR C CA    1 
ATOM   11439 C  C     . THR C 2 75  ? 99.958  84.665  130.024 1.00 22.09 ?  54  THR C C     1 
ATOM   11440 O  O     . THR C 2 75  ? 101.035 84.118  130.235 1.00 21.88 ?  54  THR C O     1 
ATOM   11441 C  CB    . THR C 2 75  ? 97.931  83.293  129.344 1.00 21.74 ?  54  THR C CB    1 
ATOM   11442 O  OG1   . THR C 2 75  ? 96.855  82.527  129.890 1.00 22.09 ?  54  THR C OG1   1 
ATOM   11443 C  CG2   . THR C 2 75  ? 98.874  82.329  128.613 1.00 19.76 ?  54  THR C CG2   1 
ATOM   11444 N  N     . TYR C 2 76  ? 99.850  85.830  129.392 1.00 22.38 ?  55  TYR C N     1 
ATOM   11445 C  CA    . TYR C 2 76  ? 101.027 86.546  128.908 1.00 22.85 ?  55  TYR C CA    1 
ATOM   11446 C  C     . TYR C 2 76  ? 102.033 86.874  130.026 1.00 22.56 ?  55  TYR C C     1 
ATOM   11447 O  O     . TYR C 2 76  ? 103.225 86.629  129.861 1.00 21.97 ?  55  TYR C O     1 
ATOM   11448 C  CB    . TYR C 2 76  ? 100.611 87.815  128.178 1.00 23.57 ?  55  TYR C CB    1 
ATOM   11449 C  CG    . TYR C 2 76  ? 101.683 88.430  127.302 1.00 25.59 ?  55  TYR C CG    1 
ATOM   11450 C  CD1   . TYR C 2 76  ? 101.789 88.087  125.950 1.00 27.49 ?  55  TYR C CD1   1 
ATOM   11451 C  CD2   . TYR C 2 76  ? 102.566 89.379  127.814 1.00 27.70 ?  55  TYR C CD2   1 
ATOM   11452 C  CE1   . TYR C 2 76  ? 102.762 88.673  125.131 1.00 30.28 ?  55  TYR C CE1   1 
ATOM   11453 C  CE2   . TYR C 2 76  ? 103.549 89.968  127.006 1.00 30.38 ?  55  TYR C CE2   1 
ATOM   11454 C  CZ    . TYR C 2 76  ? 103.640 89.608  125.667 1.00 31.39 ?  55  TYR C CZ    1 
ATOM   11455 O  OH    . TYR C 2 76  ? 104.600 90.198  124.867 1.00 32.67 ?  55  TYR C OH    1 
ATOM   11456 N  N     . MET C 2 77  ? 101.552 87.427  131.141 1.00 23.14 ?  56  MET C N     1 
ATOM   11457 C  CA    . MET C 2 77  ? 102.416 87.773  132.286 1.00 23.90 ?  56  MET C CA    1 
ATOM   11458 C  C     . MET C 2 77  ? 103.125 86.537  132.823 1.00 23.24 ?  56  MET C C     1 
ATOM   11459 O  O     . MET C 2 77  ? 104.320 86.567  133.144 1.00 22.47 ?  56  MET C O     1 
ATOM   11460 C  CB    . MET C 2 77  ? 101.603 88.386  133.431 1.00 24.38 ?  56  MET C CB    1 
ATOM   11461 C  CG    . MET C 2 77  ? 100.944 89.727  133.144 1.00 28.52 ?  56  MET C CG    1 
ATOM   11462 S  SD    . MET C 2 77  ? 102.104 91.087  133.151 1.00 34.32 ?  56  MET C SD    1 
ATOM   11463 C  CE    . MET C 2 77  ? 102.622 91.119  134.871 1.00 33.84 ?  56  MET C CE    1 
ATOM   11464 N  N     . LYS C 2 78  ? 102.367 85.449  132.928 1.00 23.25 ?  57  LYS C N     1 
ATOM   11465 C  CA    . LYS C 2 78  ? 102.862 84.236  133.566 1.00 22.98 ?  57  LYS C CA    1 
ATOM   11466 C  C     . LYS C 2 78  ? 103.901 83.567  132.679 1.00 22.77 ?  57  LYS C C     1 
ATOM   11467 O  O     . LYS C 2 78  ? 104.944 83.131  133.159 1.00 22.56 ?  57  LYS C O     1 
ATOM   11468 C  CB    . LYS C 2 78  ? 101.696 83.304  133.919 1.00 22.99 ?  57  LYS C CB    1 
ATOM   11469 C  CG    . LYS C 2 78  ? 100.919 83.775  135.151 1.00 24.86 ?  57  LYS C CG    1 
ATOM   11470 C  CD    . LYS C 2 78  ? 99.647  82.961  135.389 1.00 27.37 ?  57  LYS C CD    1 
ATOM   11471 C  CE    . LYS C 2 78  ? 99.031  83.293  136.754 1.00 28.99 ?  57  LYS C CE    1 
ATOM   11472 N  NZ    . LYS C 2 78  ? 97.693  82.641  136.878 1.00 29.82 1  57  LYS C NZ    1 
ATOM   11473 N  N     . VAL C 2 79  ? 103.605 83.523  131.382 1.00 22.70 ?  58  VAL C N     1 
ATOM   11474 C  CA    . VAL C 2 79  ? 104.509 83.021  130.349 1.00 23.48 ?  58  VAL C CA    1 
ATOM   11475 C  C     . VAL C 2 79  ? 105.887 83.724  130.414 1.00 23.04 ?  58  VAL C C     1 
ATOM   11476 O  O     . VAL C 2 79  ? 106.939 83.056  130.484 1.00 22.83 ?  58  VAL C O     1 
ATOM   11477 C  CB    . VAL C 2 79  ? 103.797 83.147  128.966 1.00 24.24 ?  58  VAL C CB    1 
ATOM   11478 C  CG1   . VAL C 2 79  ? 104.742 83.512  127.836 1.00 25.71 ?  58  VAL C CG1   1 
ATOM   11479 C  CG2   . VAL C 2 79  ? 102.972 81.874  128.674 1.00 25.04 ?  58  VAL C CG2   1 
ATOM   11480 N  N     . LEU C 2 80  ? 105.878 85.053  130.446 1.00 22.84 ?  59  LEU C N     1 
ATOM   11481 C  CA    . LEU C 2 80  ? 107.125 85.819  130.508 1.00 23.35 ?  59  LEU C CA    1 
ATOM   11482 C  C     . LEU C 2 80  ? 107.835 85.632  131.854 1.00 22.75 ?  59  LEU C C     1 
ATOM   11483 O  O     . LEU C 2 80  ? 109.063 85.626  131.904 1.00 22.75 ?  59  LEU C O     1 
ATOM   11484 C  CB    . LEU C 2 80  ? 106.896 87.311  130.229 1.00 23.91 ?  59  LEU C CB    1 
ATOM   11485 C  CG    . LEU C 2 80  ? 106.455 87.839  128.850 1.00 26.63 ?  59  LEU C CG    1 
ATOM   11486 C  CD1   . LEU C 2 80  ? 106.740 89.330  128.748 1.00 26.99 ?  59  LEU C CD1   1 
ATOM   11487 C  CD2   . LEU C 2 80  ? 107.115 87.113  127.690 1.00 27.23 ?  59  LEU C CD2   1 
ATOM   11488 N  N     . ALA C 2 81  ? 107.063 85.453  132.928 1.00 22.28 ?  60  ALA C N     1 
ATOM   11489 C  CA    . ALA C 2 81  ? 107.627 85.192  134.256 1.00 22.21 ?  60  ALA C CA    1 
ATOM   11490 C  C     . ALA C 2 81  ? 108.361 83.848  134.298 1.00 22.07 ?  60  ALA C C     1 
ATOM   11491 O  O     . ALA C 2 81  ? 109.441 83.762  134.873 1.00 21.97 ?  60  ALA C O     1 
ATOM   11492 C  CB    . ALA C 2 81  ? 106.536 85.278  135.345 1.00 22.38 ?  60  ALA C CB    1 
ATOM   11493 N  N     . GLY C 2 82  ? 107.786 82.827  133.650 1.00 21.67 ?  61  GLY C N     1 
ATOM   11494 C  CA    . GLY C 2 82  ? 108.412 81.516  133.501 1.00 21.74 ?  61  GLY C CA    1 
ATOM   11495 C  C     . GLY C 2 82  ? 109.711 81.595  132.716 1.00 21.79 ?  61  GLY C C     1 
ATOM   11496 O  O     . GLY C 2 82  ? 110.699 80.922  133.046 1.00 21.93 ?  61  GLY C O     1 
ATOM   11497 N  N     . LEU C 2 83  ? 109.711 82.438  131.685 1.00 21.54 ?  62  LEU C N     1 
ATOM   11498 C  CA    . LEU C 2 83  ? 110.913 82.710  130.899 1.00 21.12 ?  62  LEU C CA    1 
ATOM   11499 C  C     . LEU C 2 83  ? 111.967 83.416  131.740 1.00 20.89 ?  62  LEU C C     1 
ATOM   11500 O  O     . LEU C 2 83  ? 113.147 83.071  131.661 1.00 20.84 ?  62  LEU C O     1 
ATOM   11501 C  CB    . LEU C 2 83  ? 110.594 83.554  129.659 1.00 21.23 ?  62  LEU C CB    1 
ATOM   11502 C  CG    . LEU C 2 83  ? 109.714 82.958  128.553 1.00 21.98 ?  62  LEU C CG    1 
ATOM   11503 C  CD1   . LEU C 2 83  ? 109.379 84.006  127.488 1.00 24.12 ?  62  LEU C CD1   1 
ATOM   11504 C  CD2   . LEU C 2 83  ? 110.357 81.748  127.902 1.00 22.03 ?  62  LEU C CD2   1 
ATOM   11505 N  N     . THR C 2 84  ? 111.535 84.400  132.531 1.00 19.93 ?  63  THR C N     1 
ATOM   11506 C  CA    . THR C 2 84  ? 112.442 85.149  133.398 1.00 19.71 ?  63  THR C CA    1 
ATOM   11507 C  C     . THR C 2 84  ? 113.166 84.218  134.356 1.00 19.63 ?  63  THR C C     1 
ATOM   11508 O  O     . THR C 2 84  ? 114.371 84.370  134.579 1.00 19.62 ?  63  THR C O     1 
ATOM   11509 C  CB    . THR C 2 84  ? 111.695 86.239  134.206 1.00 20.22 ?  63  THR C CB    1 
ATOM   11510 O  OG1   . THR C 2 84  ? 110.899 87.043  133.317 1.00 19.37 ?  63  THR C OG1   1 
ATOM   11511 C  CG2   . THR C 2 84  ? 112.674 87.107  134.957 1.00 19.45 ?  63  THR C CG2   1 
ATOM   11512 N  N     . LEU C 2 85  ? 112.433 83.263  134.923 1.00 19.66 ?  64  LEU C N     1 
ATOM   11513 C  CA    . LEU C 2 85  ? 113.010 82.302  135.860 1.00 20.51 ?  64  LEU C CA    1 
ATOM   11514 C  C     . LEU C 2 85  ? 114.098 81.463  135.183 1.00 20.84 ?  64  LEU C C     1 
ATOM   11515 O  O     . LEU C 2 85  ? 115.210 81.348  135.702 1.00 21.30 ?  64  LEU C O     1 
ATOM   11516 C  CB    . LEU C 2 85  ? 111.929 81.410  136.494 1.00 20.03 ?  64  LEU C CB    1 
ATOM   11517 C  CG    . LEU C 2 85  ? 112.480 80.346  137.471 1.00 21.43 ?  64  LEU C CG    1 
ATOM   11518 C  CD1   . LEU C 2 85  ? 113.117 80.980  138.729 1.00 21.61 ?  64  LEU C CD1   1 
ATOM   11519 C  CD2   . LEU C 2 85  ? 111.423 79.321  137.877 1.00 20.99 ?  64  LEU C CD2   1 
ATOM   11520 N  N     . LEU C 2 86  ? 113.773 80.900  134.025 1.00 21.37 ?  65  LEU C N     1 
ATOM   11521 C  CA    . LEU C 2 86  ? 114.729 80.118  133.238 1.00 21.92 ?  65  LEU C CA    1 
ATOM   11522 C  C     . LEU C 2 86  ? 116.018 80.893  132.921 1.00 21.76 ?  65  LEU C C     1 
ATOM   11523 O  O     . LEU C 2 86  ? 117.115 80.371  133.119 1.00 21.72 ?  65  LEU C O     1 
ATOM   11524 C  CB    . LEU C 2 86  ? 114.082 79.612  131.939 1.00 22.42 ?  65  LEU C CB    1 
ATOM   11525 C  CG    . LEU C 2 86  ? 112.970 78.543  131.971 1.00 24.26 ?  65  LEU C CG    1 
ATOM   11526 C  CD1   . LEU C 2 86  ? 112.419 78.331  130.562 1.00 24.67 ?  65  LEU C CD1   1 
ATOM   11527 C  CD2   . LEU C 2 86  ? 113.471 77.227  132.541 1.00 25.60 ?  65  LEU C CD2   1 
ATOM   11528 N  N     . ASP C 2 87  ? 115.884 82.127  132.430 1.00 21.75 ?  66  ASP C N     1 
ATOM   11529 C  CA    . ASP C 2 87  ? 117.050 82.984  132.139 1.00 21.99 ?  66  ASP C CA    1 
ATOM   11530 C  C     . ASP C 2 87  ? 117.845 83.400  133.382 1.00 21.76 ?  66  ASP C C     1 
ATOM   11531 O  O     . ASP C 2 87  ? 119.073 83.553  133.322 1.00 21.65 ?  66  ASP C O     1 
ATOM   11532 C  CB    . ASP C 2 87  ? 116.628 84.249  131.387 1.00 22.23 ?  66  ASP C CB    1 
ATOM   11533 C  CG    . ASP C 2 87  ? 116.740 84.101  129.895 1.00 24.59 ?  66  ASP C CG    1 
ATOM   11534 O  OD1   . ASP C 2 87  ? 117.750 83.537  129.416 1.00 27.46 ?  66  ASP C OD1   1 
ATOM   11535 O  OD2   . ASP C 2 87  ? 115.815 84.566  129.199 1.00 27.98 -1 66  ASP C OD2   1 
ATOM   11536 N  N     . THR C 2 88  ? 117.138 83.617  134.489 1.00 21.50 ?  67  THR C N     1 
ATOM   11537 C  CA    . THR C 2 88  ? 117.783 83.894  135.767 1.00 21.80 ?  67  THR C CA    1 
ATOM   11538 C  C     . THR C 2 88  ? 118.766 82.766  136.133 1.00 22.04 ?  67  THR C C     1 
ATOM   11539 O  O     . THR C 2 88  ? 119.926 83.031  136.480 1.00 22.21 ?  67  THR C O     1 
ATOM   11540 C  CB    . THR C 2 88  ? 116.740 84.110  136.878 1.00 22.15 ?  67  THR C CB    1 
ATOM   11541 O  OG1   . THR C 2 88  ? 115.908 85.218  136.528 1.00 22.23 ?  67  THR C OG1   1 
ATOM   11542 C  CG2   . THR C 2 88  ? 117.404 84.400  138.228 1.00 21.19 ?  67  THR C CG2   1 
ATOM   11543 N  N     . GLU C 2 89  ? 118.310 81.522  136.021 1.00 21.55 ?  68  GLU C N     1 
ATOM   11544 C  CA    . GLU C 2 89  ? 119.137 80.384  136.397 1.00 21.81 ?  68  GLU C CA    1 
ATOM   11545 C  C     . GLU C 2 89  ? 120.189 80.050  135.327 1.00 21.35 ?  68  GLU C C     1 
ATOM   11546 O  O     . GLU C 2 89  ? 121.303 79.647  135.654 1.00 21.34 ?  68  GLU C O     1 
ATOM   11547 C  CB    . GLU C 2 89  ? 118.268 79.179  136.774 1.00 22.25 ?  68  GLU C CB    1 
ATOM   11548 C  CG    . GLU C 2 89  ? 117.685 79.284  138.213 1.00 24.02 ?  68  GLU C CG    1 
ATOM   11549 C  CD    . GLU C 2 89  ? 118.760 79.548  139.269 1.00 25.78 ?  68  GLU C CD    1 
ATOM   11550 O  OE1   . GLU C 2 89  ? 119.817 78.883  139.241 1.00 26.69 ?  68  GLU C OE1   1 
ATOM   11551 O  OE2   . GLU C 2 89  ? 118.550 80.427  140.139 1.00 28.98 -1 68  GLU C OE2   1 
ATOM   11552 N  N     . GLN C 2 90  ? 119.851 80.272  134.058 1.00 20.82 ?  69  GLN C N     1 
ATOM   11553 C  CA    . GLN C 2 90  ? 120.804 80.076  132.972 1.00 21.28 ?  69  GLN C CA    1 
ATOM   11554 C  C     . GLN C 2 90  ? 121.966 81.069  133.078 1.00 21.24 ?  69  GLN C C     1 
ATOM   11555 O  O     . GLN C 2 90  ? 123.116 80.713  132.805 1.00 20.99 ?  69  GLN C O     1 
ATOM   11556 C  CB    . GLN C 2 90  ? 120.109 80.172  131.601 1.00 21.86 ?  69  GLN C CB    1 
ATOM   11557 C  CG    . GLN C 2 90  ? 120.958 79.633  130.428 1.00 24.29 ?  69  GLN C CG    1 
ATOM   11558 C  CD    . GLN C 2 90  ? 121.134 78.111  130.464 1.00 27.14 ?  69  GLN C CD    1 
ATOM   11559 O  OE1   . GLN C 2 90  ? 120.982 77.481  131.514 1.00 27.13 ?  69  GLN C OE1   1 
ATOM   11560 N  NE2   . GLN C 2 90  ? 121.472 77.522  129.314 1.00 27.69 ?  69  GLN C NE2   1 
ATOM   11561 N  N     . GLY C 2 91  ? 121.660 82.295  133.510 1.00 20.62 ?  70  GLY C N     1 
ATOM   11562 C  CA    . GLY C 2 91  ? 122.671 83.344  133.676 1.00 22.00 ?  70  GLY C CA    1 
ATOM   11563 C  C     . GLY C 2 91  ? 123.454 83.234  134.969 1.00 22.45 ?  70  GLY C C     1 
ATOM   11564 O  O     . GLY C 2 91  ? 124.674 83.379  134.954 1.00 23.53 ?  70  GLY C O     1 
ATOM   11565 N  N     . ASN C 2 92  ? 122.758 82.977  136.078 1.00 22.79 ?  71  ASN C N     1 
ATOM   11566 C  CA    . ASN C 2 92  ? 123.390 82.874  137.403 1.00 23.85 ?  71  ASN C CA    1 
ATOM   11567 C  C     . ASN C 2 92  ? 124.225 81.609  137.560 1.00 24.33 ?  71  ASN C C     1 
ATOM   11568 O  O     . ASN C 2 92  ? 125.262 81.624  138.233 1.00 24.17 ?  71  ASN C O     1 
ATOM   11569 C  CB    . ASN C 2 92  ? 122.339 82.868  138.521 1.00 23.74 ?  71  ASN C CB    1 
ATOM   11570 C  CG    . ASN C 2 92  ? 121.631 84.201  138.696 1.00 24.38 ?  71  ASN C CG    1 
ATOM   11571 O  OD1   . ASN C 2 92  ? 121.875 85.172  137.968 1.00 25.16 ?  71  ASN C OD1   1 
ATOM   11572 N  ND2   . ASN C 2 92  ? 120.737 84.248  139.669 1.00 24.07 ?  71  ASN C ND2   1 
ATOM   11573 N  N     . THR C 2 93  ? 123.770 80.520  136.936 1.00 23.97 ?  72  THR C N     1 
ATOM   11574 C  CA    . THR C 2 93  ? 124.265 79.181  137.289 1.00 24.97 ?  72  THR C CA    1 
ATOM   11575 C  C     . THR C 2 93  ? 124.746 78.394  136.080 1.00 24.52 ?  72  THR C C     1 
ATOM   11576 O  O     . THR C 2 93  ? 125.904 78.000  136.025 1.00 25.39 ?  72  THR C O     1 
ATOM   11577 C  CB    . THR C 2 93  ? 123.184 78.358  138.041 1.00 24.54 ?  72  THR C CB    1 
ATOM   11578 O  OG1   . THR C 2 93  ? 122.711 79.100  139.172 1.00 26.43 ?  72  THR C OG1   1 
ATOM   11579 C  CG2   . THR C 2 93  ? 123.743 77.029  138.524 1.00 26.83 ?  72  THR C CG2   1 
ATOM   11580 N  N     . GLY C 2 94  ? 123.853 78.180  135.124 1.00 24.37 ?  73  GLY C N     1 
ATOM   11581 C  CA    . GLY C 2 94  ? 124.090 77.273  133.991 1.00 24.24 ?  73  GLY C CA    1 
ATOM   11582 C  C     . GLY C 2 94  ? 125.278 77.643  133.129 1.00 24.94 ?  73  GLY C C     1 
ATOM   11583 O  O     . GLY C 2 94  ? 126.230 76.866  133.002 1.00 25.86 ?  73  GLY C O     1 
ATOM   11584 N  N     . MET C 2 95  ? 125.228 78.828  132.532 1.00 24.07 ?  74  MET C N     1 
ATOM   11585 C  CA    . MET C 2 95  ? 126.321 79.262  131.671 1.00 24.35 ?  74  MET C CA    1 
ATOM   11586 C  C     . MET C 2 95  ? 127.671 79.460  132.387 1.00 23.52 ?  74  MET C C     1 
ATOM   11587 O  O     . MET C 2 95  ? 128.679 79.007  131.856 1.00 23.40 ?  74  MET C O     1 
ATOM   11588 C  CB    . MET C 2 95  ? 125.926 80.477  130.831 1.00 24.38 ?  74  MET C CB    1 
ATOM   11589 C  CG    . MET C 2 95  ? 124.906 80.167  129.734 1.00 27.47 ?  74  MET C CG    1 
ATOM   11590 S  SD    . MET C 2 95  ? 125.585 78.990  128.532 1.00 32.54 ?  74  MET C SD    1 
ATOM   11591 C  CE    . MET C 2 95  ? 126.757 80.007  127.705 1.00 34.32 ?  74  MET C CE    1 
ATOM   11592 N  N     . PRO C 2 96  ? 127.696 80.120  133.579 1.00 23.36 ?  75  PRO C N     1 
ATOM   11593 C  CA    . PRO C 2 96  ? 128.966 80.244  134.328 1.00 23.27 ?  75  PRO C CA    1 
ATOM   11594 C  C     . PRO C 2 96  ? 129.593 78.912  134.726 1.00 23.77 ?  75  PRO C C     1 
ATOM   11595 O  O     . PRO C 2 96  ? 130.811 78.763  134.629 1.00 23.46 ?  75  PRO C O     1 
ATOM   11596 C  CB    . PRO C 2 96  ? 128.563 81.006  135.601 1.00 23.55 ?  75  PRO C CB    1 
ATOM   11597 C  CG    . PRO C 2 96  ? 127.361 81.792  135.203 1.00 23.85 ?  75  PRO C CG    1 
ATOM   11598 C  CD    . PRO C 2 96  ? 126.617 80.890  134.231 1.00 22.76 ?  75  PRO C CD    1 
ATOM   11599 N  N     . ILE C 2 97  ? 128.780 77.960  135.189 1.00 23.81 ?  76  ILE C N     1 
ATOM   11600 C  CA    . ILE C 2 97  ? 129.300 76.650  135.588 1.00 24.52 ?  76  ILE C CA    1 
ATOM   11601 C  C     . ILE C 2 97  ? 129.859 75.834  134.402 1.00 23.92 ?  76  ILE C C     1 
ATOM   11602 O  O     . ILE C 2 97  ? 130.927 75.215  134.510 1.00 23.99 ?  76  ILE C O     1 
ATOM   11603 C  CB    . ILE C 2 97  ? 128.271 75.845  136.432 1.00 24.49 ?  76  ILE C CB    1 
ATOM   11604 C  CG1   . ILE C 2 97  ? 128.982 74.795  137.284 1.00 27.08 ?  76  ILE C CG1   1 
ATOM   11605 C  CG2   . ILE C 2 97  ? 127.186 75.185  135.556 1.00 26.06 ?  76  ILE C CG2   1 
ATOM   11606 C  CD1   . ILE C 2 97  ? 128.190 74.404  138.523 1.00 31.37 ?  76  ILE C CD1   1 
ATOM   11607 N  N     . VAL C 2 98  ? 129.161 75.858  133.271 1.00 23.97 ?  77  VAL C N     1 
ATOM   11608 C  CA    . VAL C 2 98  ? 129.679 75.229  132.048 1.00 24.01 ?  77  VAL C CA    1 
ATOM   11609 C  C     . VAL C 2 98  ? 130.979 75.933  131.604 1.00 25.23 ?  77  VAL C C     1 
ATOM   11610 O  O     . VAL C 2 98  ? 131.965 75.271  131.264 1.00 25.77 ?  77  VAL C O     1 
ATOM   11611 C  CB    . VAL C 2 98  ? 128.615 75.206  130.921 1.00 23.98 ?  77  VAL C CB    1 
ATOM   11612 C  CG1   . VAL C 2 98  ? 129.235 74.813  129.583 1.00 23.17 ?  77  VAL C CG1   1 
ATOM   11613 C  CG2   . VAL C 2 98  ? 127.484 74.239  131.293 1.00 22.55 ?  77  VAL C CG2   1 
ATOM   11614 N  N     . ALA C 2 99  ? 130.998 77.266  131.665 1.00 25.42 ?  78  ALA C N     1 
ATOM   11615 C  CA    . ALA C 2 99  ? 132.220 78.024  131.345 1.00 26.72 ?  78  ALA C CA    1 
ATOM   11616 C  C     . ALA C 2 99  ? 133.403 77.566  132.204 1.00 27.46 ?  78  ALA C C     1 
ATOM   11617 O  O     . ALA C 2 99  ? 134.512 77.399  131.698 1.00 28.07 ?  78  ALA C O     1 
ATOM   11618 C  CB    . ALA C 2 99  ? 131.995 79.516  131.506 1.00 26.52 ?  78  ALA C CB    1 
ATOM   11619 N  N     . GLU C 2 100 ? 133.147 77.326  133.488 1.00 28.33 ?  79  GLU C N     1 
ATOM   11620 C  CA    . GLU C 2 100 ? 134.193 76.910  134.426 1.00 29.60 ?  79  GLU C CA    1 
ATOM   11621 C  C     . GLU C 2 100 ? 134.849 75.587  134.022 1.00 29.64 ?  79  GLU C C     1 
ATOM   11622 O  O     . GLU C 2 100 ? 136.063 75.410  134.178 1.00 29.72 ?  79  GLU C O     1 
ATOM   11623 C  CB    . GLU C 2 100 ? 133.636 76.821  135.848 1.00 29.70 ?  79  GLU C CB    1 
ATOM   11624 C  CG    . GLU C 2 100 ? 134.680 76.469  136.906 1.00 33.58 ?  79  GLU C CG    1 
ATOM   11625 C  CD    . GLU C 2 100 ? 134.098 76.257  138.290 1.00 37.83 ?  79  GLU C CD    1 
ATOM   11626 O  OE1   . GLU C 2 100 ? 132.894 76.534  138.511 1.00 40.64 ?  79  GLU C OE1   1 
ATOM   11627 O  OE2   . GLU C 2 100 ? 134.858 75.799  139.171 1.00 41.40 -1 79  GLU C OE2   1 
ATOM   11628 N  N     . HIS C 2 101 ? 134.049 74.669  133.484 1.00 29.43 ?  80  HIS C N     1 
ATOM   11629 C  CA    . HIS C 2 101 ? 134.524 73.316  133.223 1.00 29.74 ?  80  HIS C CA    1 
ATOM   11630 C  C     . HIS C 2 101 ? 135.016 73.066  131.796 1.00 30.18 ?  80  HIS C C     1 
ATOM   11631 O  O     . HIS C 2 101 ? 135.705 72.084  131.546 1.00 30.30 ?  80  HIS C O     1 
ATOM   11632 C  CB    . HIS C 2 101 ? 133.472 72.288  133.672 1.00 29.21 ?  80  HIS C CB    1 
ATOM   11633 C  CG    . HIS C 2 101 ? 133.321 72.215  135.160 1.00 29.60 ?  80  HIS C CG    1 
ATOM   11634 N  ND1   . HIS C 2 101 ? 132.409 72.979  135.857 1.00 30.06 ?  80  HIS C ND1   1 
ATOM   11635 C  CD2   . HIS C 2 101 ? 133.999 71.500  136.088 1.00 29.49 ?  80  HIS C CD2   1 
ATOM   11636 C  CE1   . HIS C 2 101 ? 132.522 72.727  137.151 1.00 29.56 ?  80  HIS C CE1   1 
ATOM   11637 N  NE2   . HIS C 2 101 ? 133.478 71.833  137.317 1.00 30.20 ?  80  HIS C NE2   1 
ATOM   11638 N  N     . VAL C 2 102 ? 134.677 73.962  130.874 1.00 30.70 ?  81  VAL C N     1 
ATOM   11639 C  CA    . VAL C 2 102 ? 135.109 73.854  129.483 1.00 31.47 ?  81  VAL C CA    1 
ATOM   11640 C  C     . VAL C 2 102 ? 136.494 74.479  129.328 1.00 32.45 ?  81  VAL C C     1 
ATOM   11641 O  O     . VAL C 2 102 ? 136.722 75.603  129.792 1.00 32.50 ?  81  VAL C O     1 
ATOM   11642 C  CB    . VAL C 2 102 ? 134.106 74.530  128.511 1.00 31.18 ?  81  VAL C CB    1 
ATOM   11643 C  CG1   . VAL C 2 102 ? 134.670 74.593  127.089 1.00 31.20 ?  81  VAL C CG1   1 
ATOM   11644 C  CG2   . VAL C 2 102 ? 132.784 73.777  128.505 1.00 31.28 ?  81  VAL C CG2   1 
ATOM   11645 N  N     . ASP C 2 103 ? 137.398 73.751  128.670 1.00 33.38 ?  82  ASP C N     1 
ATOM   11646 C  CA    . ASP C 2 103 ? 138.780 74.201  128.470 1.00 34.82 ?  82  ASP C CA    1 
ATOM   11647 C  C     . ASP C 2 103 ? 138.953 75.082  127.238 1.00 34.74 ?  82  ASP C C     1 
ATOM   11648 O  O     . ASP C 2 103 ? 138.337 74.837  126.193 1.00 35.00 ?  82  ASP C O     1 
ATOM   11649 C  CB    . ASP C 2 103 ? 139.735 73.001  128.385 1.00 35.82 ?  82  ASP C CB    1 
ATOM   11650 C  CG    . ASP C 2 103 ? 139.967 72.333  129.737 1.00 38.29 ?  82  ASP C CG    1 
ATOM   11651 O  OD1   . ASP C 2 103 ? 139.947 73.031  130.779 1.00 41.49 ?  82  ASP C OD1   1 
ATOM   11652 O  OD2   . ASP C 2 103 ? 140.172 71.104  129.759 1.00 41.10 -1 82  ASP C OD2   1 
ATOM   11653 N  N     . GLY C 2 104 ? 139.801 76.102  127.373 1.00 34.89 ?  83  GLY C N     1 
ATOM   11654 C  CA    . GLY C 2 104 ? 140.146 76.996  126.262 1.00 35.11 ?  83  GLY C CA    1 
ATOM   11655 C  C     . GLY C 2 104 ? 139.592 78.396  126.439 1.00 34.96 ?  83  GLY C C     1 
ATOM   11656 O  O     . GLY C 2 104 ? 138.379 78.571  126.580 1.00 34.57 ?  83  GLY C O     1 
ATOM   11657 N  N     . HIS C 2 105 ? 140.480 79.392  126.415 1.00 35.02 ?  84  HIS C N     1 
ATOM   11658 C  CA    . HIS C 2 105 ? 140.109 80.789  126.683 1.00 34.83 ?  84  HIS C CA    1 
ATOM   11659 C  C     . HIS C 2 105 ? 139.048 81.346  125.744 1.00 33.77 ?  84  HIS C C     1 
ATOM   11660 O  O     . HIS C 2 105 ? 138.201 82.137  126.164 1.00 33.25 ?  84  HIS C O     1 
ATOM   11661 C  CB    . HIS C 2 105 ? 141.340 81.703  126.704 1.00 36.09 ?  84  HIS C CB    1 
ATOM   11662 C  CG    . HIS C 2 105 ? 142.164 81.568  127.949 1.00 39.17 ?  84  HIS C CG    1 
ATOM   11663 N  ND1   . HIS C 2 105 ? 143.537 81.712  127.954 1.00 43.00 ?  84  HIS C ND1   1 
ATOM   11664 C  CD2   . HIS C 2 105 ? 141.811 81.281  129.226 1.00 41.84 ?  84  HIS C CD2   1 
ATOM   11665 C  CE1   . HIS C 2 105 ? 143.990 81.529  129.183 1.00 43.47 ?  84  HIS C CE1   1 
ATOM   11666 N  NE2   . HIS C 2 105 ? 142.964 81.266  129.974 1.00 43.10 ?  84  HIS C NE2   1 
ATOM   11667 N  N     . GLN C 2 106 ? 139.080 80.926  124.484 1.00 32.84 ?  85  GLN C N     1 
ATOM   11668 C  CA    . GLN C 2 106 ? 138.079 81.387  123.526 1.00 32.29 ?  85  GLN C CA    1 
ATOM   11669 C  C     . GLN C 2 106 ? 136.707 80.748  123.767 1.00 30.88 ?  85  GLN C C     1 
ATOM   11670 O  O     . GLN C 2 106 ? 135.680 81.429  123.671 1.00 30.44 ?  85  GLN C O     1 
ATOM   11671 C  CB    . GLN C 2 106 ? 138.542 81.146  122.097 1.00 32.85 ?  85  GLN C CB    1 
ATOM   11672 C  CG    . GLN C 2 106 ? 139.763 81.968  121.706 1.00 35.55 ?  85  GLN C CG    1 
ATOM   11673 C  CD    . GLN C 2 106 ? 140.258 81.626  120.325 1.00 38.12 ?  85  GLN C CD    1 
ATOM   11674 O  OE1   . GLN C 2 106 ? 139.466 81.368  119.418 1.00 39.96 ?  85  GLN C OE1   1 
ATOM   11675 N  NE2   . GLN C 2 106 ? 141.578 81.621  120.152 1.00 40.39 ?  85  GLN C NE2   1 
ATOM   11676 N  N     . ARG C 2 107 ? 136.693 79.451  124.070 1.00 29.75 ?  86  ARG C N     1 
ATOM   11677 C  CA    . ARG C 2 107 ? 135.443 78.765  124.420 1.00 28.87 ?  86  ARG C CA    1 
ATOM   11678 C  C     . ARG C 2 107 ? 134.848 79.397  125.671 1.00 28.16 ?  86  ARG C C     1 
ATOM   11679 O  O     . ARG C 2 107 ? 133.642 79.628  125.736 1.00 27.55 ?  86  ARG C O     1 
ATOM   11680 C  CB    . ARG C 2 107 ? 135.665 77.270  124.639 1.00 28.48 ?  86  ARG C CB    1 
ATOM   11681 C  CG    . ARG C 2 107 ? 135.936 76.508  123.354 1.00 29.86 ?  86  ARG C CG    1 
ATOM   11682 C  CD    . ARG C 2 107 ? 136.191 75.031  123.604 1.00 30.23 ?  86  ARG C CD    1 
ATOM   11683 N  NE    . ARG C 2 107 ? 135.990 74.299  122.359 1.00 33.04 ?  86  ARG C NE    1 
ATOM   11684 C  CZ    . ARG C 2 107 ? 135.776 72.997  122.271 1.00 31.54 ?  86  ARG C CZ    1 
ATOM   11685 N  NH1   . ARG C 2 107 ? 135.751 72.244  123.361 1.00 31.85 1  86  ARG C NH1   1 
ATOM   11686 N  NH2   . ARG C 2 107 ? 135.594 72.454  121.079 1.00 34.74 ?  86  ARG C NH2   1 
ATOM   11687 N  N     . LYS C 2 108 ? 135.702 79.689  126.651 1.00 27.65 ?  87  LYS C N     1 
ATOM   11688 C  CA    . LYS C 2 108 ? 135.253 80.353  127.880 1.00 27.96 ?  87  LYS C CA    1 
ATOM   11689 C  C     . LYS C 2 108 ? 134.715 81.754  127.631 1.00 27.75 ?  87  LYS C C     1 
ATOM   11690 O  O     . LYS C 2 108 ? 133.749 82.163  128.275 1.00 28.29 ?  87  LYS C O     1 
ATOM   11691 C  CB    . LYS C 2 108 ? 136.361 80.405  128.932 1.00 27.80 ?  87  LYS C CB    1 
ATOM   11692 C  CG    . LYS C 2 108 ? 136.714 79.052  129.515 1.00 29.04 ?  87  LYS C CG    1 
ATOM   11693 C  CD    . LYS C 2 108 ? 137.800 79.209  130.570 1.00 31.15 ?  87  LYS C CD    1 
ATOM   11694 C  CE    . LYS C 2 108 ? 138.333 77.862  131.021 1.00 32.05 ?  87  LYS C CE    1 
ATOM   11695 N  NZ    . LYS C 2 108 ? 137.390 77.208  131.962 1.00 30.88 1  87  LYS C NZ    1 
ATOM   11696 N  N     . ALA C 2 109 ? 135.330 82.485  126.701 1.00 27.69 ?  88  ALA C N     1 
ATOM   11697 C  CA    . ALA C 2 109 ? 134.860 83.832  126.351 1.00 27.46 ?  88  ALA C CA    1 
ATOM   11698 C  C     . ALA C 2 109 ? 133.458 83.826  125.735 1.00 26.87 ?  88  ALA C C     1 
ATOM   11699 O  O     . ALA C 2 109 ? 132.648 84.705  126.023 1.00 26.47 ?  88  ALA C O     1 
ATOM   11700 C  CB    . ALA C 2 109 ? 135.840 84.514  125.418 1.00 27.98 ?  88  ALA C CB    1 
ATOM   11701 N  N     . VAL C 2 110 ? 133.187 82.844  124.877 1.00 25.98 ?  89  VAL C N     1 
ATOM   11702 C  CA    . VAL C 2 110 ? 131.863 82.682  124.273 1.00 25.46 ?  89  VAL C CA    1 
ATOM   11703 C  C     . VAL C 2 110 ? 130.833 82.349  125.358 1.00 24.57 ?  89  VAL C C     1 
ATOM   11704 O  O     . VAL C 2 110 ? 129.786 82.995  125.451 1.00 23.62 ?  89  VAL C O     1 
ATOM   11705 C  CB    . VAL C 2 110 ? 131.871 81.596  123.168 1.00 25.80 ?  89  VAL C CB    1 
ATOM   11706 C  CG1   . VAL C 2 110 ? 130.448 81.251  122.707 1.00 25.44 ?  89  VAL C CG1   1 
ATOM   11707 C  CG2   . VAL C 2 110 ? 132.726 82.050  121.985 1.00 26.23 ?  89  VAL C CG2   1 
ATOM   11708 N  N     . LEU C 2 111 ? 131.155 81.367  126.197 1.00 24.33 ?  90  LEU C N     1 
ATOM   11709 C  CA    . LEU C 2 111 ? 130.241 80.959  127.264 1.00 23.93 ?  90  LEU C CA    1 
ATOM   11710 C  C     . LEU C 2 111 ? 129.988 82.064  128.290 1.00 23.77 ?  90  LEU C C     1 
ATOM   11711 O  O     . LEU C 2 111 ? 128.861 82.215  128.764 1.00 23.04 ?  90  LEU C O     1 
ATOM   11712 C  CB    . LEU C 2 111 ? 130.711 79.669  127.943 1.00 23.73 ?  90  LEU C CB    1 
ATOM   11713 C  CG    . LEU C 2 111 ? 130.738 78.439  127.031 1.00 24.50 ?  90  LEU C CG    1 
ATOM   11714 C  CD1   . LEU C 2 111 ? 131.633 77.353  127.609 1.00 24.02 ?  90  LEU C CD1   1 
ATOM   11715 C  CD2   . LEU C 2 111 ? 129.330 77.903  126.763 1.00 25.38 ?  90  LEU C CD2   1 
ATOM   11716 N  N     . ASN C 2 112 ? 131.033 82.824  128.636 1.00 24.24 ?  91  ASN C N     1 
ATOM   11717 C  CA    . ASN C 2 112 ? 130.876 84.003  129.501 1.00 24.95 ?  91  ASN C CA    1 
ATOM   11718 C  C     . ASN C 2 112 ? 129.979 85.080  128.896 1.00 24.25 ?  91  ASN C C     1 
ATOM   11719 O  O     . ASN C 2 112 ? 129.180 85.692  129.604 1.00 23.99 ?  91  ASN C O     1 
ATOM   11720 C  CB    . ASN C 2 112 ? 132.231 84.626  129.849 1.00 25.81 ?  91  ASN C CB    1 
ATOM   11721 C  CG    . ASN C 2 112 ? 132.870 83.979  131.047 1.00 29.96 ?  91  ASN C CG    1 
ATOM   11722 O  OD1   . ASN C 2 112 ? 132.668 84.423  132.179 1.00 35.44 ?  91  ASN C OD1   1 
ATOM   11723 N  ND2   . ASN C 2 112 ? 133.646 82.920  130.816 1.00 32.37 ?  91  ASN C ND2   1 
ATOM   11724 N  N     . PHE C 2 113 ? 130.143 85.330  127.598 1.00 23.60 ?  92  PHE C N     1 
ATOM   11725 C  CA    . PHE C 2 113 ? 129.290 86.280  126.892 1.00 23.32 ?  92  PHE C CA    1 
ATOM   11726 C  C     . PHE C 2 113 ? 127.823 85.828  126.903 1.00 22.63 ?  92  PHE C C     1 
ATOM   11727 O  O     . PHE C 2 113 ? 126.928 86.634  127.165 1.00 21.94 ?  92  PHE C O     1 
ATOM   11728 C  CB    . PHE C 2 113 ? 129.743 86.468  125.437 1.00 23.27 ?  92  PHE C CB    1 
ATOM   11729 C  CG    . PHE C 2 113 ? 129.059 87.614  124.744 1.00 24.66 ?  92  PHE C CG    1 
ATOM   11730 C  CD1   . PHE C 2 113 ? 129.600 88.907  124.805 1.00 25.72 ?  92  PHE C CD1   1 
ATOM   11731 C  CD2   . PHE C 2 113 ? 127.865 87.417  124.055 1.00 25.36 ?  92  PHE C CD2   1 
ATOM   11732 C  CE1   . PHE C 2 113 ? 128.960 89.978  124.181 1.00 25.92 ?  92  PHE C CE1   1 
ATOM   11733 C  CE2   . PHE C 2 113 ? 127.213 88.485  123.426 1.00 25.82 ?  92  PHE C CE2   1 
ATOM   11734 C  CZ    . PHE C 2 113 ? 127.760 89.768  123.493 1.00 25.80 ?  92  PHE C CZ    1 
ATOM   11735 N  N     . MET C 2 114 ? 127.593 84.550  126.592 1.00 22.03 ?  93  MET C N     1 
ATOM   11736 C  CA    . MET C 2 114 ? 126.244 83.968  126.636 1.00 22.14 ?  93  MET C CA    1 
ATOM   11737 C  C     . MET C 2 114 ? 125.610 84.083  128.033 1.00 21.64 ?  93  MET C C     1 
ATOM   11738 O  O     . MET C 2 114 ? 124.432 84.437  128.150 1.00 21.59 ?  93  MET C O     1 
ATOM   11739 C  CB    . MET C 2 114 ? 126.272 82.514  126.177 1.00 22.46 ?  93  MET C CB    1 
ATOM   11740 C  CG    . MET C 2 114 ? 126.585 82.345  124.698 1.00 23.80 ?  93  MET C CG    1 
ATOM   11741 S  SD    . MET C 2 114 ? 126.796 80.612  124.237 1.00 28.07 ?  93  MET C SD    1 
ATOM   11742 C  CE    . MET C 2 114 ? 126.792 80.781  122.433 1.00 26.42 ?  93  MET C CE    1 
ATOM   11743 N  N     . ALA C 2 115 ? 126.399 83.818  129.080 1.00 20.98 ?  94  ALA C N     1 
ATOM   11744 C  CA    . ALA C 2 115 ? 125.954 83.997  130.475 1.00 20.58 ?  94  ALA C CA    1 
ATOM   11745 C  C     . ALA C 2 115 ? 125.502 85.424  130.778 1.00 21.01 ?  94  ALA C C     1 
ATOM   11746 O  O     . ALA C 2 115 ? 124.475 85.644  131.446 1.00 21.06 ?  94  ALA C O     1 
ATOM   11747 C  CB    . ALA C 2 115 ? 127.075 83.571  131.453 1.00 20.83 ?  94  ALA C CB    1 
ATOM   11748 N  N     . MET C 2 116 ? 126.288 86.396  130.320 1.00 20.36 ?  95  MET C N     1 
ATOM   11749 C  CA    . MET C 2 116 ? 125.949 87.796  130.499 1.00 20.83 ?  95  MET C CA    1 
ATOM   11750 C  C     . MET C 2 116 ? 124.609 88.115  129.817 1.00 20.55 ?  95  MET C C     1 
ATOM   11751 O  O     . MET C 2 116 ? 123.746 88.766  130.405 1.00 20.70 ?  95  MET C O     1 
ATOM   11752 C  CB    . MET C 2 116 ? 127.083 88.680  129.963 1.00 20.64 ?  95  MET C CB    1 
ATOM   11753 C  CG    . MET C 2 116 ? 126.802 90.183  129.975 1.00 21.42 ?  95  MET C CG    1 
ATOM   11754 S  SD    . MET C 2 116 ? 125.784 90.701  128.579 1.00 22.51 ?  95  MET C SD    1 
ATOM   11755 C  CE    . MET C 2 116 ? 126.815 90.234  127.187 1.00 20.66 ?  95  MET C CE    1 
ATOM   11756 N  N     . MET C 2 117 ? 124.435 87.634  128.591 1.00 20.50 ?  96  MET C N     1 
ATOM   11757 C  CA    . MET C 2 117 ? 123.195 87.855  127.859 1.00 21.22 ?  96  MET C CA    1 
ATOM   11758 C  C     . MET C 2 117 ? 121.990 87.328  128.637 1.00 21.11 ?  96  MET C C     1 
ATOM   11759 O  O     . MET C 2 117 ? 120.970 88.016  128.727 1.00 20.71 ?  96  MET C O     1 
ATOM   11760 C  CB    . MET C 2 117 ? 123.259 87.241  126.454 1.00 21.35 ?  96  MET C CB    1 
ATOM   11761 C  CG    . MET C 2 117 ? 124.179 87.996  125.444 1.00 22.54 ?  96  MET C CG    1 
ATOM   11762 S  SD    . MET C 2 117 ? 123.836 89.757  125.227 1.00 24.89 ?  96  MET C SD    1 
ATOM   11763 C  CE    . MET C 2 117 ? 122.348 89.705  124.229 1.00 24.95 ?  96  MET C CE    1 
ATOM   11764 N  N     . GLU C 2 118 ? 122.123 86.132  129.209 1.00 21.18 ?  97  GLU C N     1 
ATOM   11765 C  CA    . GLU C 2 118 ? 121.040 85.500  129.971 1.00 21.99 ?  97  GLU C CA    1 
ATOM   11766 C  C     . GLU C 2 118 ? 120.503 86.396  131.089 1.00 22.10 ?  97  GLU C C     1 
ATOM   11767 O  O     . GLU C 2 118 ? 119.303 86.675  131.141 1.00 22.22 ?  97  GLU C O     1 
ATOM   11768 C  CB    . GLU C 2 118 ? 121.462 84.143  130.558 1.00 22.01 ?  97  GLU C CB    1 
ATOM   11769 C  CG    . GLU C 2 118 ? 122.047 83.110  129.588 1.00 24.38 ?  97  GLU C CG    1 
ATOM   11770 C  CD    . GLU C 2 118 ? 121.113 82.682  128.448 1.00 26.32 ?  97  GLU C CD    1 
ATOM   11771 O  OE1   . GLU C 2 118 ? 120.290 83.481  127.979 1.00 29.86 ?  97  GLU C OE1   1 
ATOM   11772 O  OE2   . GLU C 2 118 ? 121.243 81.539  127.977 1.00 29.19 -1 97  GLU C OE2   1 
ATOM   11773 N  N     . ASN C 2 119 ? 121.381 86.848  131.983 1.00 22.26 ?  98  ASN C N     1 
ATOM   11774 C  CA    . ASN C 2 119 ? 120.903 87.591  133.149 1.00 21.91 ?  98  ASN C CA    1 
ATOM   11775 C  C     . ASN C 2 119 ? 120.981 89.123  133.077 1.00 22.41 ?  98  ASN C C     1 
ATOM   11776 O  O     . ASN C 2 119 ? 120.173 89.810  133.701 1.00 23.07 ?  98  ASN C O     1 
ATOM   11777 C  CB    . ASN C 2 119 ? 121.426 87.007  134.480 1.00 21.93 ?  98  ASN C CB    1 
ATOM   11778 C  CG    . ASN C 2 119 ? 122.931 87.080  134.622 1.00 21.31 ?  98  ASN C CG    1 
ATOM   11779 O  OD1   . ASN C 2 119 ? 123.641 87.536  133.724 1.00 21.88 ?  98  ASN C OD1   1 
ATOM   11780 N  ND2   . ASN C 2 119 ? 123.429 86.636  135.774 1.00 21.73 ?  98  ASN C ND2   1 
ATOM   11781 N  N     . ALA C 2 120 ? 121.951 89.652  132.335 1.00 22.75 ?  99  ALA C N     1 
ATOM   11782 C  CA    . ALA C 2 120 ? 122.097 91.099  132.181 1.00 23.12 ?  99  ALA C CA    1 
ATOM   11783 C  C     . ALA C 2 120 ? 121.248 91.662  131.058 1.00 23.60 ?  99  ALA C C     1 
ATOM   11784 O  O     . ALA C 2 120 ? 120.920 92.853  131.082 1.00 24.14 ?  99  ALA C O     1 
ATOM   11785 C  CB    . ALA C 2 120 ? 123.575 91.502  132.000 1.00 23.28 ?  99  ALA C CB    1 
ATOM   11786 N  N     . VAL C 2 121 ? 120.885 90.824  130.082 1.00 23.23 ?  100 VAL C N     1 
ATOM   11787 C  CA    . VAL C 2 121 ? 120.065 91.301  128.953 1.00 23.74 ?  100 VAL C CA    1 
ATOM   11788 C  C     . VAL C 2 121 ? 118.677 90.662  128.887 1.00 23.62 ?  100 VAL C C     1 
ATOM   11789 O  O     . VAL C 2 121 ? 117.678 91.374  128.932 1.00 24.51 ?  100 VAL C O     1 
ATOM   11790 C  CB    . VAL C 2 121 ? 120.788 91.162  127.596 1.00 23.19 ?  100 VAL C CB    1 
ATOM   11791 C  CG1   . VAL C 2 121 ? 119.881 91.622  126.441 1.00 24.10 ?  100 VAL C CG1   1 
ATOM   11792 C  CG2   . VAL C 2 121 ? 122.097 91.969  127.608 1.00 23.48 ?  100 VAL C CG2   1 
ATOM   11793 N  N     . HIS C 2 122 ? 118.623 89.335  128.791 1.00 23.45 ?  101 HIS C N     1 
ATOM   11794 C  CA    . HIS C 2 122 ? 117.353 88.627  128.612 1.00 23.81 ?  101 HIS C CA    1 
ATOM   11795 C  C     . HIS C 2 122 ? 116.432 88.732  129.810 1.00 24.33 ?  101 HIS C C     1 
ATOM   11796 O  O     . HIS C 2 122 ? 115.292 89.185  129.667 1.00 24.80 ?  101 HIS C O     1 
ATOM   11797 C  CB    . HIS C 2 122 ? 117.564 87.153  128.281 1.00 23.30 ?  101 HIS C CB    1 
ATOM   11798 C  CG    . HIS C 2 122 ? 118.295 86.916  126.998 1.00 22.96 ?  101 HIS C CG    1 
ATOM   11799 N  ND1   . HIS C 2 122 ? 118.693 85.659  126.593 1.00 22.78 ?  101 HIS C ND1   1 
ATOM   11800 C  CD2   . HIS C 2 122 ? 118.729 87.777  126.047 1.00 23.25 ?  101 HIS C CD2   1 
ATOM   11801 C  CE1   . HIS C 2 122 ? 119.327 85.755  125.440 1.00 22.57 ?  101 HIS C CE1   1 
ATOM   11802 N  NE2   . HIS C 2 122 ? 119.362 87.027  125.086 1.00 21.75 ?  101 HIS C NE2   1 
ATOM   11803 N  N     . ALA C 2 123 ? 116.908 88.283  130.974 1.00 24.40 ?  102 ALA C N     1 
ATOM   11804 C  CA    . ALA C 2 123 ? 116.085 88.295  132.185 1.00 24.00 ?  102 ALA C CA    1 
ATOM   11805 C  C     . ALA C 2 123 ? 115.599 89.713  132.489 1.00 24.05 ?  102 ALA C C     1 
ATOM   11806 O  O     . ALA C 2 123 ? 114.447 89.903  132.875 1.00 23.89 ?  102 ALA C O     1 
ATOM   11807 C  CB    . ALA C 2 123 ? 116.843 87.704  133.372 1.00 23.73 ?  102 ALA C CB    1 
ATOM   11808 N  N     . LYS C 2 124 ? 116.471 90.702  132.294 1.00 24.36 ?  103 LYS C N     1 
ATOM   11809 C  CA    . LYS C 2 124 ? 116.126 92.106  132.546 1.00 24.31 ?  103 LYS C CA    1 
ATOM   11810 C  C     . LYS C 2 124 ? 115.077 92.678  131.585 1.00 23.84 ?  103 LYS C C     1 
ATOM   11811 O  O     . LYS C 2 124 ? 114.203 93.444  132.008 1.00 24.21 ?  103 LYS C O     1 
ATOM   11812 C  CB    . LYS C 2 124 ? 117.372 92.996  132.592 1.00 24.93 ?  103 LYS C CB    1 
ATOM   11813 C  CG    . LYS C 2 124 ? 117.072 94.424  133.073 1.00 26.37 ?  103 LYS C CG    1 
ATOM   11814 C  CD    . LYS C 2 124 ? 118.337 95.237  133.287 1.00 29.42 ?  103 LYS C CD    1 
ATOM   11815 C  CE    . LYS C 2 124 ? 117.998 96.699  133.596 1.00 31.51 ?  103 LYS C CE    1 
ATOM   11816 N  NZ    . LYS C 2 124 ? 117.339 97.383  132.444 1.00 32.37 1  103 LYS C NZ    1 
ATOM   11817 N  N     . SER C 2 125 ? 115.155 92.300  130.306 1.00 23.52 ?  104 SER C N     1 
ATOM   11818 C  CA    . SER C 2 125 ? 114.187 92.737  129.295 0.50 23.23 ?  104 SER C CA    1 
ATOM   11819 C  C     . SER C 2 125 ? 112.746 92.432  129.706 1.00 22.91 ?  104 SER C C     1 
ATOM   11820 O  O     . SER C 2 125 ? 111.835 93.197  129.415 1.00 22.33 ?  104 SER C O     1 
ATOM   11821 C  CB    . SER C 2 125 ? 114.475 92.075  127.942 0.50 23.25 ?  104 SER C CB    1 
ATOM   11822 O  OG    . SER C 2 125 ? 115.769 92.399  127.470 0.50 24.57 ?  104 SER C OG    1 
ATOM   11823 N  N     . TYR C 2 126 ? 112.535 91.299  130.371 1.00 22.72 ?  105 TYR C N     1 
ATOM   11824 C  CA    . TYR C 2 126 ? 111.181 90.944  130.799 1.00 23.34 ?  105 TYR C CA    1 
ATOM   11825 C  C     . TYR C 2 126 ? 110.640 91.933  131.805 1.00 23.32 ?  105 TYR C C     1 
ATOM   11826 O  O     . TYR C 2 126 ? 109.454 92.227  131.780 1.00 23.17 ?  105 TYR C O     1 
ATOM   11827 C  CB    . TYR C 2 126 ? 111.090 89.528  131.371 1.00 23.45 ?  105 TYR C CB    1 
ATOM   11828 C  CG    . TYR C 2 126 ? 111.570 88.449  130.429 1.00 25.16 ?  105 TYR C CG    1 
ATOM   11829 C  CD1   . TYR C 2 126 ? 110.949 88.232  129.202 1.00 26.75 ?  105 TYR C CD1   1 
ATOM   11830 C  CD2   . TYR C 2 126 ? 112.654 87.642  130.775 1.00 26.36 ?  105 TYR C CD2   1 
ATOM   11831 C  CE1   . TYR C 2 126 ? 111.410 87.238  128.331 1.00 28.22 ?  105 TYR C CE1   1 
ATOM   11832 C  CE2   . TYR C 2 126 ? 113.120 86.657  129.919 1.00 27.17 ?  105 TYR C CE2   1 
ATOM   11833 C  CZ    . TYR C 2 126 ? 112.487 86.450  128.707 1.00 29.26 ?  105 TYR C CZ    1 
ATOM   11834 O  OH    . TYR C 2 126 ? 112.944 85.458  127.862 1.00 30.76 ?  105 TYR C OH    1 
ATOM   11835 N  N     . SER C 2 127 ? 111.513 92.437  132.681 1.00 23.61 ?  106 SER C N     1 
ATOM   11836 C  CA    . SER C 2 127 ? 111.127 93.467  133.638 1.00 24.40 ?  106 SER C CA    1 
ATOM   11837 C  C     . SER C 2 127 ? 110.798 94.779  132.939 1.00 24.55 ?  106 SER C C     1 
ATOM   11838 O  O     . SER C 2 127 ? 109.930 95.505  133.398 1.00 24.74 ?  106 SER C O     1 
ATOM   11839 C  CB    . SER C 2 127 ? 112.197 93.685  134.707 1.00 24.54 ?  106 SER C CB    1 
ATOM   11840 O  OG    . SER C 2 127 ? 112.160 92.648  135.681 1.00 24.69 ?  106 SER C OG    1 
ATOM   11841 N  N     . ASN C 2 128 ? 111.495 95.081  131.844 1.00 25.28 ?  107 ASN C N     1 
ATOM   11842 C  CA    . ASN C 2 128 ? 111.174 96.265  131.041 1.00 25.88 ?  107 ASN C CA    1 
ATOM   11843 C  C     . ASN C 2 128 ? 109.764 96.139  130.479 1.00 25.48 ?  107 ASN C C     1 
ATOM   11844 O  O     . ASN C 2 128 ? 108.981 97.085  130.521 1.00 25.23 ?  107 ASN C O     1 
ATOM   11845 C  CB    . ASN C 2 128 ? 112.178 96.470  129.900 1.00 26.40 ?  107 ASN C CB    1 
ATOM   11846 C  CG    . ASN C 2 128 ? 113.505 97.055  130.368 1.00 27.90 ?  107 ASN C CG    1 
ATOM   11847 O  OD1   . ASN C 2 128 ? 113.949 96.814  131.492 1.00 30.62 ?  107 ASN C OD1   1 
ATOM   11848 N  ND2   . ASN C 2 128 ? 114.151 97.816  129.491 1.00 27.91 ?  107 ASN C ND2   1 
ATOM   11849 N  N     . ILE C 2 129 ? 109.447 94.956  129.962 1.00 25.44 ?  108 ILE C N     1 
ATOM   11850 C  CA    . ILE C 2 129 ? 108.097 94.691  129.464 1.00 25.48 ?  108 ILE C CA    1 
ATOM   11851 C  C     . ILE C 2 129 ? 107.069 94.806  130.601 1.00 25.93 ?  108 ILE C C     1 
ATOM   11852 O  O     . ILE C 2 129 ? 106.083 95.540  130.463 1.00 25.54 ?  108 ILE C O     1 
ATOM   11853 C  CB    . ILE C 2 129 ? 108.001 93.346  128.698 1.00 25.21 ?  108 ILE C CB    1 
ATOM   11854 C  CG1   . ILE C 2 129 ? 108.920 93.384  127.465 1.00 25.96 ?  108 ILE C CG1   1 
ATOM   11855 C  CG2   . ILE C 2 129 ? 106.540 93.051  128.294 1.00 24.43 ?  108 ILE C CG2   1 
ATOM   11856 C  CD1   . ILE C 2 129 ? 109.141 92.039  126.773 1.00 26.11 ?  108 ILE C CD1   1 
ATOM   11857 N  N     . PHE C 2 130 ? 107.305 94.111  131.718 1.00 26.04 ?  109 PHE C N     1 
ATOM   11858 C  CA    . PHE C 2 130 ? 106.396 94.169  132.877 1.00 26.66 ?  109 PHE C CA    1 
ATOM   11859 C  C     . PHE C 2 130 ? 106.160 95.601  133.366 1.00 27.38 ?  109 PHE C C     1 
ATOM   11860 O  O     . PHE C 2 130 ? 105.015 95.995  133.642 1.00 27.22 ?  109 PHE C O     1 
ATOM   11861 C  CB    . PHE C 2 130 ? 106.932 93.334  134.061 1.00 26.98 ?  109 PHE C CB    1 
ATOM   11862 C  CG    . PHE C 2 130 ? 106.877 91.840  133.856 1.00 27.46 ?  109 PHE C CG    1 
ATOM   11863 C  CD1   . PHE C 2 130 ? 105.911 91.255  133.045 1.00 28.57 ?  109 PHE C CD1   1 
ATOM   11864 C  CD2   . PHE C 2 130 ? 107.795 91.013  134.504 1.00 28.51 ?  109 PHE C CD2   1 
ATOM   11865 C  CE1   . PHE C 2 130 ? 105.871 89.873  132.866 1.00 29.17 ?  109 PHE C CE1   1 
ATOM   11866 C  CE2   . PHE C 2 130 ? 107.760 89.622  134.337 1.00 29.27 ?  109 PHE C CE2   1 
ATOM   11867 C  CZ    . PHE C 2 130 ? 106.796 89.048  133.522 1.00 28.83 ?  109 PHE C CZ    1 
ATOM   11868 N  N     . MET C 2 131 ? 107.236 96.380  133.474 1.00 27.52 ?  110 MET C N     1 
ATOM   11869 C  CA    . MET C 2 131 ? 107.144 97.736  134.029 1.00 29.07 ?  110 MET C CA    1 
ATOM   11870 C  C     . MET C 2 131 ? 106.371 98.696  133.142 1.00 29.58 ?  110 MET C C     1 
ATOM   11871 O  O     . MET C 2 131 ? 105.794 99.667  133.631 1.00 30.07 ?  110 MET C O     1 
ATOM   11872 C  CB    . MET C 2 131 ? 108.523 98.308  134.347 1.00 28.96 ?  110 MET C CB    1 
ATOM   11873 C  CG    . MET C 2 131 ? 109.092 97.799  135.654 1.00 31.09 ?  110 MET C CG    1 
ATOM   11874 S  SD    . MET C 2 131 ? 110.747 98.425  136.026 1.00 35.43 ?  110 MET C SD    1 
ATOM   11875 C  CE    . MET C 2 131 ? 111.736 97.675  134.736 1.00 33.13 ?  110 MET C CE    1 
ATOM   11876 N  N     . THR C 2 132 ? 106.362 98.412  131.846 1.00 30.25 ?  111 THR C N     1 
ATOM   11877 C  CA    . THR C 2 132 ? 105.589 99.185  130.877 1.00 30.97 ?  111 THR C CA    1 
ATOM   11878 C  C     . THR C 2 132 ? 104.097 98.843  130.943 1.00 31.36 ?  111 THR C C     1 
ATOM   11879 O  O     . THR C 2 132 ? 103.246 99.733  131.078 1.00 31.60 ?  111 THR C O     1 
ATOM   11880 C  CB    . THR C 2 132 ? 106.138 98.951  129.441 1.00 30.88 ?  111 THR C CB    1 
ATOM   11881 O  OG1   . THR C 2 132 ? 107.491 99.412  129.377 1.00 29.86 ?  111 THR C OG1   1 
ATOM   11882 C  CG2   . THR C 2 132 ? 105.308 99.696  128.383 1.00 31.44 ?  111 THR C CG2   1 
ATOM   11883 N  N     . LEU C 2 133 ? 103.789 97.552  130.860 1.00 31.34 ?  112 LEU C N     1 
ATOM   11884 C  CA    . LEU C 2 133 ? 102.409 97.092  130.695 1.00 31.68 ?  112 LEU C CA    1 
ATOM   11885 C  C     . LEU C 2 133 ? 101.587 96.941  131.979 1.00 31.96 ?  112 LEU C C     1 
ATOM   11886 O  O     . LEU C 2 133 ? 100.370 97.122  131.962 1.00 31.69 ?  112 LEU C O     1 
ATOM   11887 C  CB    . LEU C 2 133 ? 102.389 95.773  129.930 1.00 31.35 ?  112 LEU C CB    1 
ATOM   11888 C  CG    . LEU C 2 133 ? 103.130 95.725  128.589 1.00 32.14 ?  112 LEU C CG    1 
ATOM   11889 C  CD1   . LEU C 2 133 ? 103.053 94.325  128.029 1.00 32.15 ?  112 LEU C CD1   1 
ATOM   11890 C  CD2   . LEU C 2 133 ? 102.564 96.745  127.603 1.00 32.39 ?  112 LEU C CD2   1 
ATOM   11891 N  N     . ALA C 2 134 ? 102.247 96.608  133.083 1.00 32.12 ?  113 ALA C N     1 
ATOM   11892 C  CA    . ALA C 2 134 ? 101.539 96.187  134.284 1.00 32.53 ?  113 ALA C CA    1 
ATOM   11893 C  C     . ALA C 2 134 ? 101.798 97.079  135.492 1.00 33.15 ?  113 ALA C C     1 
ATOM   11894 O  O     . ALA C 2 134 ? 102.894 97.614  135.642 1.00 32.47 ?  113 ALA C O     1 
ATOM   11895 C  CB    . ALA C 2 134 ? 101.882 94.729  134.614 1.00 32.20 ?  113 ALA C CB    1 
ATOM   11896 N  N     . PRO C 2 135 ? 100.784 97.223  136.369 1.00 34.27 ?  114 PRO C N     1 
ATOM   11897 C  CA    . PRO C 2 135 ? 100.983 97.921  137.633 1.00 35.35 ?  114 PRO C CA    1 
ATOM   11898 C  C     . PRO C 2 135 ? 101.803 97.064  138.592 1.00 36.17 ?  114 PRO C C     1 
ATOM   11899 O  O     . PRO C 2 135 ? 101.825 95.837  138.462 1.00 35.92 ?  114 PRO C O     1 
ATOM   11900 C  CB    . PRO C 2 135 ? 99.557  98.135  138.155 1.00 35.48 ?  114 PRO C CB    1 
ATOM   11901 C  CG    . PRO C 2 135 ? 98.734  97.094  137.502 1.00 34.94 ?  114 PRO C CG    1 
ATOM   11902 C  CD    . PRO C 2 135 ? 99.404  96.724  136.211 1.00 34.50 ?  114 PRO C CD    1 
ATOM   11903 N  N     . THR C 2 136 ? 102.476 97.715  139.534 1.00 37.30 ?  115 THR C N     1 
ATOM   11904 C  CA    . THR C 2 136 ? 103.396 97.052  140.465 1.00 38.49 ?  115 THR C CA    1 
ATOM   11905 C  C     . THR C 2 136 ? 102.822 95.819  141.176 1.00 38.48 ?  115 THR C C     1 
ATOM   11906 O  O     . THR C 2 136 ? 103.540 94.831  141.370 1.00 38.74 ?  115 THR C O     1 
ATOM   11907 C  CB    . THR C 2 136 ? 103.927 98.052  141.512 1.00 38.95 ?  115 THR C CB    1 
ATOM   11908 O  OG1   . THR C 2 136 ? 104.456 99.196  140.835 1.00 40.08 ?  115 THR C OG1   1 
ATOM   11909 C  CG2   . THR C 2 136 ? 105.026 97.428  142.374 1.00 39.82 ?  115 THR C CG2   1 
ATOM   11910 N  N     . GLU C 2 137 ? 101.544 95.878  141.555 1.00 38.89 ?  116 GLU C N     1 
ATOM   11911 C  CA    . GLU C 2 137 ? 100.897 94.788  142.299 1.00 38.65 ?  116 GLU C CA    1 
ATOM   11912 C  C     . GLU C 2 137 ? 100.768 93.524  141.457 1.00 37.38 ?  116 GLU C C     1 
ATOM   11913 O  O     . GLU C 2 137 ? 100.940 92.416  141.962 1.00 37.22 ?  116 GLU C O     1 
ATOM   11914 C  CB    . GLU C 2 137 ? 99.528  95.206  142.880 1.00 39.52 ?  116 GLU C CB    1 
ATOM   11915 C  CG    . GLU C 2 137 ? 98.383  95.420  141.862 1.00 41.90 ?  116 GLU C CG    1 
ATOM   11916 C  CD    . GLU C 2 137 ? 97.796  96.842  141.868 1.00 46.43 ?  116 GLU C CD    1 
ATOM   11917 O  OE1   . GLU C 2 137 ? 98.394  97.756  142.485 1.00 47.84 ?  116 GLU C OE1   1 
ATOM   11918 O  OE2   . GLU C 2 137 ? 96.724  97.043  141.247 1.00 47.52 -1 116 GLU C OE2   1 
ATOM   11919 N  N     . THR C 2 138 ? 100.478 93.705  140.172 1.00 36.05 ?  117 THR C N     1 
ATOM   11920 C  CA    . THR C 2 138 ? 100.381 92.597  139.234 1.00 34.88 ?  117 THR C CA    1 
ATOM   11921 C  C     . THR C 2 138 ? 101.764 92.004  138.991 1.00 33.58 ?  117 THR C C     1 
ATOM   11922 O  O     . THR C 2 138 ? 101.904 90.783  138.871 1.00 33.61 ?  117 THR C O     1 
ATOM   11923 C  CB    . THR C 2 138 ? 99.744  93.041  137.910 1.00 34.85 ?  117 THR C CB    1 
ATOM   11924 O  OG1   . THR C 2 138 ? 98.512  93.717  138.189 1.00 35.98 ?  117 THR C OG1   1 
ATOM   11925 C  CG2   . THR C 2 138 ? 99.466  91.845  137.011 1.00 34.92 ?  117 THR C CG2   1 
ATOM   11926 N  N     . ILE C 2 139 ? 102.775 92.869  138.925 1.00 32.29 ?  118 ILE C N     1 
ATOM   11927 C  CA    . ILE C 2 139 ? 104.164 92.427  138.807 1.00 31.19 ?  118 ILE C CA    1 
ATOM   11928 C  C     . ILE C 2 139 ? 104.584 91.622  140.051 1.00 30.85 ?  118 ILE C C     1 
ATOM   11929 O  O     . ILE C 2 139 ? 105.121 90.522  139.921 1.00 29.77 ?  118 ILE C O     1 
ATOM   11930 C  CB    . ILE C 2 139 ? 105.150 93.602  138.532 1.00 31.25 ?  118 ILE C CB    1 
ATOM   11931 C  CG1   . ILE C 2 139 ? 104.773 94.355  137.244 1.00 30.12 ?  118 ILE C CG1   1 
ATOM   11932 C  CG2   . ILE C 2 139 ? 106.598 93.096  138.441 1.00 30.21 ?  118 ILE C CG2   1 
ATOM   11933 C  CD1   . ILE C 2 139 ? 105.615 95.619  136.991 1.00 29.41 ?  118 ILE C CD1   1 
ATOM   11934 N  N     . ASN C 2 140 ? 104.320 92.166  141.244 1.00 31.17 ?  119 ASN C N     1 
ATOM   11935 C  CA    . ASN C 2 140 ? 104.615 91.468  142.506 1.00 31.76 ?  119 ASN C CA    1 
ATOM   11936 C  C     . ASN C 2 140 ? 103.942 90.093  142.576 1.00 31.25 ?  119 ASN C C     1 
ATOM   11937 O  O     . ASN C 2 140 ? 104.578 89.106  142.946 1.00 31.47 ?  119 ASN C O     1 
ATOM   11938 C  CB    . ASN C 2 140 ? 104.189 92.297  143.728 1.00 32.65 ?  119 ASN C CB    1 
ATOM   11939 C  CG    . ASN C 2 140 ? 105.074 93.515  143.970 1.00 35.14 ?  119 ASN C CG    1 
ATOM   11940 O  OD1   . ASN C 2 140 ? 106.253 93.546  143.601 1.00 36.75 ?  119 ASN C OD1   1 
ATOM   11941 N  ND2   . ASN C 2 140 ? 104.501 94.527  144.629 1.00 38.05 ?  119 ASN C ND2   1 
ATOM   11942 N  N     . GLU C 2 141 ? 102.663 90.047  142.206 1.00 30.96 ?  120 GLU C N     1 
ATOM   11943 C  CA    . GLU C 2 141 ? 101.874 88.817  142.207 1.00 30.36 ?  120 GLU C CA    1 
ATOM   11944 C  C     . GLU C 2 141 ? 102.439 87.752  141.264 1.00 28.60 ?  120 GLU C C     1 
ATOM   11945 O  O     . GLU C 2 141 ? 102.494 86.579  141.626 1.00 27.94 ?  120 GLU C O     1 
ATOM   11946 C  CB    . GLU C 2 141 ? 100.415 89.108  141.844 1.00 30.86 ?  120 GLU C CB    1 
ATOM   11947 C  CG    . GLU C 2 141 ? 99.589  89.722  142.969 1.00 34.89 ?  120 GLU C CG    1 
ATOM   11948 C  CD    . GLU C 2 141 ? 98.212  90.175  142.503 1.00 39.82 ?  120 GLU C CD    1 
ATOM   11949 O  OE1   . GLU C 2 141 ? 97.782  89.778  141.391 1.00 41.95 ?  120 GLU C OE1   1 
ATOM   11950 O  OE2   . GLU C 2 141 ? 97.551  90.926  143.251 1.00 41.94 -1 120 GLU C OE2   1 
ATOM   11951 N  N     . VAL C 2 142 ? 102.854 88.148  140.063 1.00 27.29 ?  121 VAL C N     1 
ATOM   11952 C  CA    . VAL C 2 142 ? 103.382 87.146  139.113 1.00 25.89 ?  121 VAL C CA    1 
ATOM   11953 C  C     . VAL C 2 142 ? 104.725 86.558  139.564 1.00 25.11 ?  121 VAL C C     1 
ATOM   11954 O  O     . VAL C 2 142 ? 104.999 85.381  139.333 1.00 24.23 ?  121 VAL C O     1 
ATOM   11955 C  CB    . VAL C 2 142 ? 103.401 87.638  137.624 1.00 25.99 ?  121 VAL C CB    1 
ATOM   11956 C  CG1   . VAL C 2 142 ? 104.666 88.430  137.283 1.00 25.21 ?  121 VAL C CG1   1 
ATOM   11957 C  CG2   . VAL C 2 142 ? 103.266 86.456  136.677 1.00 25.78 ?  121 VAL C CG2   1 
ATOM   11958 N  N     . PHE C 2 143 ? 105.557 87.362  140.219 1.00 24.69 ?  122 PHE C N     1 
ATOM   11959 C  CA    . PHE C 2 143 ? 106.817 86.833  140.762 1.00 24.77 ?  122 PHE C CA    1 
ATOM   11960 C  C     . PHE C 2 143 ? 106.574 85.917  141.974 1.00 24.99 ?  122 PHE C C     1 
ATOM   11961 O  O     . PHE C 2 143 ? 107.287 84.933  142.174 1.00 24.73 ?  122 PHE C O     1 
ATOM   11962 C  CB    . PHE C 2 143 ? 107.825 87.953  141.052 1.00 24.83 ?  122 PHE C CB    1 
ATOM   11963 C  CG    . PHE C 2 143 ? 108.519 88.465  139.808 1.00 25.12 ?  122 PHE C CG    1 
ATOM   11964 C  CD1   . PHE C 2 143 ? 109.492 87.698  139.171 1.00 26.58 ?  122 PHE C CD1   1 
ATOM   11965 C  CD2   . PHE C 2 143 ? 108.186 89.697  139.266 1.00 24.49 ?  122 PHE C CD2   1 
ATOM   11966 C  CE1   . PHE C 2 143 ? 110.124 88.162  138.011 1.00 26.96 ?  122 PHE C CE1   1 
ATOM   11967 C  CE2   . PHE C 2 143 ? 108.808 90.168  138.119 1.00 25.79 ?  122 PHE C CE2   1 
ATOM   11968 C  CZ    . PHE C 2 143 ? 109.780 89.400  137.483 1.00 26.45 ?  122 PHE C CZ    1 
ATOM   11969 N  N     . GLU C 2 144 ? 105.549 86.230  142.763 1.00 25.22 ?  123 GLU C N     1 
ATOM   11970 C  CA    . GLU C 2 144 ? 105.107 85.317  143.822 1.00 25.72 ?  123 GLU C CA    1 
ATOM   11971 C  C     . GLU C 2 144 ? 104.574 84.015  143.225 1.00 25.08 ?  123 GLU C C     1 
ATOM   11972 O  O     . GLU C 2 144 ? 104.845 82.930  143.741 1.00 24.67 ?  123 GLU C O     1 
ATOM   11973 C  CB    . GLU C 2 144 ? 104.066 85.980  144.720 1.00 26.23 ?  123 GLU C CB    1 
ATOM   11974 C  CG    . GLU C 2 144 ? 104.664 87.051  145.617 1.00 29.96 ?  123 GLU C CG    1 
ATOM   11975 C  CD    . GLU C 2 144 ? 105.843 86.531  146.423 1.00 33.82 ?  123 GLU C CD    1 
ATOM   11976 O  OE1   . GLU C 2 144 ? 105.628 85.650  147.282 1.00 36.54 ?  123 GLU C OE1   1 
ATOM   11977 O  OE2   . GLU C 2 144 ? 106.982 86.987  146.188 1.00 35.84 -1 123 GLU C OE2   1 
ATOM   11978 N  N     . TRP C 2 145 ? 103.843 84.135  142.119 1.00 24.21 ?  124 TRP C N     1 
ATOM   11979 C  CA    . TRP C 2 145 ? 103.314 82.974  141.404 1.00 23.99 ?  124 TRP C CA    1 
ATOM   11980 C  C     . TRP C 2 145 ? 104.403 82.031  140.872 1.00 23.95 ?  124 TRP C C     1 
ATOM   11981 O  O     . TRP C 2 145 ? 104.225 80.799  140.914 1.00 23.31 ?  124 TRP C O     1 
ATOM   11982 C  CB    . TRP C 2 145 ? 102.375 83.416  140.270 1.00 24.13 ?  124 TRP C CB    1 
ATOM   11983 C  CG    . TRP C 2 145 ? 102.024 82.304  139.308 1.00 24.37 ?  124 TRP C CG    1 
ATOM   11984 C  CD1   . TRP C 2 145 ? 100.980 81.416  139.409 1.00 24.76 ?  124 TRP C CD1   1 
ATOM   11985 C  CD2   . TRP C 2 145 ? 102.722 81.970  138.101 1.00 23.31 ?  124 TRP C CD2   1 
ATOM   11986 N  NE1   . TRP C 2 145 ? 100.997 80.546  138.334 1.00 24.97 ?  124 TRP C NE1   1 
ATOM   11987 C  CE2   . TRP C 2 145 ? 102.051 80.866  137.518 1.00 24.20 ?  124 TRP C CE2   1 
ATOM   11988 C  CE3   . TRP C 2 145 ? 103.854 82.489  137.459 1.00 23.76 ?  124 TRP C CE3   1 
ATOM   11989 C  CZ2   . TRP C 2 145 ? 102.478 80.277  136.320 1.00 23.41 ?  124 TRP C CZ2   1 
ATOM   11990 C  CZ3   . TRP C 2 145 ? 104.281 81.901  136.269 1.00 23.29 ?  124 TRP C CZ3   1 
ATOM   11991 C  CH2   . TRP C 2 145 ? 103.585 80.808  135.711 1.00 22.93 ?  124 TRP C CH2   1 
ATOM   11992 N  N     . VAL C 2 146 ? 105.517 82.571  140.367 1.00 23.35 ?  125 VAL C N     1 
ATOM   11993 C  CA    . VAL C 2 146 ? 106.610 81.657  139.944 1.00 23.53 ?  125 VAL C CA    1 
ATOM   11994 C  C     . VAL C 2 146 ? 107.149 80.815  141.108 1.00 23.73 ?  125 VAL C C     1 
ATOM   11995 O  O     . VAL C 2 146 ? 107.388 79.629  140.935 1.00 23.03 ?  125 VAL C O     1 
ATOM   11996 C  CB    . VAL C 2 146 ? 107.750 82.285  139.012 1.00 23.63 ?  125 VAL C CB    1 
ATOM   11997 C  CG1   . VAL C 2 146 ? 107.487 83.707  138.597 1.00 24.40 ?  125 VAL C CG1   1 
ATOM   11998 C  CG2   . VAL C 2 146 ? 109.180 82.082  139.548 1.00 22.97 ?  125 VAL C CG2   1 
ATOM   11999 N  N     . LYS C 2 147 ? 107.276 81.420  142.291 1.00 24.06 ?  126 LYS C N     1 
ATOM   12000 C  CA    . LYS C 2 147 ? 107.811 80.715  143.469 1.00 25.41 ?  126 LYS C CA    1 
ATOM   12001 C  C     . LYS C 2 147 ? 106.967 79.511  143.896 1.00 25.82 ?  126 LYS C C     1 
ATOM   12002 O  O     . LYS C 2 147 ? 107.510 78.526  144.400 1.00 26.08 ?  126 LYS C O     1 
ATOM   12003 C  CB    . LYS C 2 147 ? 107.949 81.666  144.661 1.00 25.49 ?  126 LYS C CB    1 
ATOM   12004 C  CG    . LYS C 2 147 ? 109.009 82.738  144.512 1.00 27.52 ?  126 LYS C CG    1 
ATOM   12005 C  CD    . LYS C 2 147 ? 108.968 83.655  145.729 1.00 30.43 ?  126 LYS C CD    1 
ATOM   12006 C  CE    . LYS C 2 147 ? 109.747 84.932  145.495 1.00 33.10 ?  126 LYS C CE    1 
ATOM   12007 N  NZ    . LYS C 2 147 ? 109.584 85.851  146.656 1.00 34.86 1  126 LYS C NZ    1 
ATOM   12008 N  N     . GLN C 2 148 ? 105.653 79.597  143.695 1.00 26.45 ?  127 GLN C N     1 
ATOM   12009 C  CA    . GLN C 2 148 ? 104.725 78.570  144.175 1.00 26.85 ?  127 GLN C CA    1 
ATOM   12010 C  C     . GLN C 2 148 ? 104.189 77.637  143.087 1.00 26.01 ?  127 GLN C C     1 
ATOM   12011 O  O     . GLN C 2 148 ? 103.488 76.672  143.398 1.00 26.12 ?  127 GLN C O     1 
ATOM   12012 C  CB    . GLN C 2 148 ? 103.561 79.201  144.964 1.00 28.08 ?  127 GLN C CB    1 
ATOM   12013 C  CG    . GLN C 2 148 ? 102.661 80.146  144.163 1.00 30.69 ?  127 GLN C CG    1 
ATOM   12014 C  CD    . GLN C 2 148 ? 101.709 79.419  143.218 1.00 34.64 ?  127 GLN C CD    1 
ATOM   12015 O  OE1   . GLN C 2 148 ? 101.813 79.545  141.985 1.00 33.80 ?  127 GLN C OE1   1 
ATOM   12016 N  NE2   . GLN C 2 148 ? 100.779 78.642  143.789 1.00 36.24 ?  127 GLN C NE2   1 
ATOM   12017 N  N     . ASN C 2 149 ? 104.505 77.924  141.821 1.00 24.97 ?  128 ASN C N     1 
ATOM   12018 C  CA    . ASN C 2 149 ? 104.049 77.092  140.712 1.00 24.03 ?  128 ASN C CA    1 
ATOM   12019 C  C     . ASN C 2 149 ? 104.851 75.802  140.643 1.00 24.13 ?  128 ASN C C     1 
ATOM   12020 O  O     . ASN C 2 149 ? 106.071 75.853  140.466 1.00 22.93 ?  128 ASN C O     1 
ATOM   12021 C  CB    . ASN C 2 149 ? 104.196 77.834  139.393 1.00 23.97 ?  128 ASN C CB    1 
ATOM   12022 C  CG    . ASN C 2 149 ? 103.609 77.064  138.234 1.00 23.94 ?  128 ASN C CG    1 
ATOM   12023 O  OD1   . ASN C 2 149 ? 104.289 76.262  137.598 1.00 24.85 ?  128 ASN C OD1   1 
ATOM   12024 N  ND2   . ASN C 2 149 ? 102.322 77.266  137.984 1.00 24.76 ?  128 ASN C ND2   1 
ATOM   12025 N  N     . LYS C 2 150 ? 104.171 74.657  140.750 1.00 24.32 ?  129 LYS C N     1 
ATOM   12026 C  CA    . LYS C 2 150 ? 104.869 73.365  140.900 1.00 24.77 ?  129 LYS C CA    1 
ATOM   12027 C  C     . LYS C 2 150 ? 105.633 72.883  139.664 1.00 24.54 ?  129 LYS C C     1 
ATOM   12028 O  O     . LYS C 2 150 ? 106.665 72.223  139.796 1.00 24.17 ?  129 LYS C O     1 
ATOM   12029 C  CB    . LYS C 2 150 ? 103.934 72.273  141.435 1.00 25.27 ?  129 LYS C CB    1 
ATOM   12030 C  CG    . LYS C 2 150 ? 102.754 71.923  140.551 1.00 28.72 ?  129 LYS C CG    1 
ATOM   12031 C  CD    . LYS C 2 150 ? 102.124 70.612  141.024 1.00 33.40 ?  129 LYS C CD    1 
ATOM   12032 C  CE    . LYS C 2 150 ? 100.689 70.486  140.550 1.00 36.77 ?  129 LYS C CE    1 
ATOM   12033 N  NZ    . LYS C 2 150 ? 100.030 69.311  141.201 1.00 39.66 1  129 LYS C NZ    1 
ATOM   12034 N  N     . TYR C 2 151 ? 105.125 73.209  138.471 1.00 23.92 ?  130 TYR C N     1 
ATOM   12035 C  CA    . TYR C 2 151 ? 105.786 72.821  137.218 1.00 24.12 ?  130 TYR C CA    1 
ATOM   12036 C  C     . TYR C 2 151 ? 107.049 73.625  136.958 1.00 23.54 ?  130 TYR C C     1 
ATOM   12037 O  O     . TYR C 2 151 ? 108.060 73.085  136.483 1.00 23.32 ?  130 TYR C O     1 
ATOM   12038 C  CB    . TYR C 2 151 ? 104.804 72.932  136.036 1.00 24.53 ?  130 TYR C CB    1 
ATOM   12039 C  CG    . TYR C 2 151 ? 103.443 72.358  136.364 1.00 25.83 ?  130 TYR C CG    1 
ATOM   12040 C  CD1   . TYR C 2 151 ? 103.291 70.998  136.639 1.00 26.57 ?  130 TYR C CD1   1 
ATOM   12041 C  CD2   . TYR C 2 151 ? 102.315 73.182  136.446 1.00 27.87 ?  130 TYR C CD2   1 
ATOM   12042 C  CE1   . TYR C 2 151 ? 102.050 70.461  136.963 1.00 29.65 ?  130 TYR C CE1   1 
ATOM   12043 C  CE2   . TYR C 2 151 ? 101.061 72.653  136.775 1.00 29.91 ?  130 TYR C CE2   1 
ATOM   12044 C  CZ    . TYR C 2 151 ? 100.941 71.295  137.033 1.00 31.19 ?  130 TYR C CZ    1 
ATOM   12045 O  OH    . TYR C 2 151 ? 99.713  70.755  137.358 1.00 34.44 ?  130 TYR C OH    1 
ATOM   12046 N  N     . LEU C 2 152 ? 106.988 74.915  137.271 1.00 23.38 ?  131 LEU C N     1 
ATOM   12047 C  CA    . LEU C 2 152 ? 108.128 75.800  137.117 1.00 23.43 ?  131 LEU C CA    1 
ATOM   12048 C  C     . LEU C 2 152 ? 109.206 75.448  138.147 1.00 23.37 ?  131 LEU C C     1 
ATOM   12049 O  O     . LEU C 2 152 ? 110.394 75.409  137.814 1.00 23.05 ?  131 LEU C O     1 
ATOM   12050 C  CB    . LEU C 2 152 ? 107.660 77.247  137.269 1.00 23.73 ?  131 LEU C CB    1 
ATOM   12051 C  CG    . LEU C 2 152 ? 108.068 78.395  136.354 1.00 24.71 ?  131 LEU C CG    1 
ATOM   12052 C  CD1   . LEU C 2 152 ? 108.623 77.978  134.982 1.00 21.63 ?  131 LEU C CD1   1 
ATOM   12053 C  CD2   . LEU C 2 152 ? 106.886 79.322  136.190 1.00 26.87 ?  131 LEU C CD2   1 
ATOM   12054 N  N     . GLN C 2 153 ? 108.801 75.191  139.395 1.00 22.80 ?  132 GLN C N     1 
ATOM   12055 C  CA    . GLN C 2 153 ? 109.759 74.703  140.399 1.00 22.70 ?  132 GLN C CA    1 
ATOM   12056 C  C     . GLN C 2 153 ? 110.383 73.354  140.032 1.00 22.54 ?  132 GLN C C     1 
ATOM   12057 O  O     . GLN C 2 153 ? 111.603 73.178  140.172 1.00 21.73 ?  132 GLN C O     1 
ATOM   12058 C  CB    . GLN C 2 153 ? 109.159 74.680  141.807 1.00 23.07 ?  132 GLN C CB    1 
ATOM   12059 C  CG    . GLN C 2 153 ? 108.797 76.074  142.320 1.00 21.83 ?  132 GLN C CG    1 
ATOM   12060 C  CD    . GLN C 2 153 ? 109.986 77.037  142.355 1.00 22.34 ?  132 GLN C CD    1 
ATOM   12061 O  OE1   . GLN C 2 153 ? 111.064 76.700  142.850 1.00 24.07 ?  132 GLN C OE1   1 
ATOM   12062 N  NE2   . GLN C 2 153 ? 109.784 78.243  141.842 1.00 22.26 ?  132 GLN C NE2   1 
ATOM   12063 N  N     . LYS C 2 154 ? 109.564 72.412  139.555 1.00 22.53 ?  133 LYS C N     1 
ATOM   12064 C  CA    . LYS C 2 154 ? 110.096 71.119  139.125 1.00 22.84 ?  133 LYS C CA    1 
ATOM   12065 C  C     . LYS C 2 154 ? 111.129 71.263  138.006 1.00 22.42 ?  133 LYS C C     1 
ATOM   12066 O  O     . LYS C 2 154 ? 112.184 70.643  138.075 1.00 21.90 ?  133 LYS C O     1 
ATOM   12067 C  CB    . LYS C 2 154 ? 108.988 70.112  138.738 1.00 22.96 ?  133 LYS C CB    1 
ATOM   12068 C  CG    . LYS C 2 154 ? 109.519 68.707  138.317 1.00 23.45 ?  133 LYS C CG    1 
ATOM   12069 C  CD    . LYS C 2 154 ? 110.227 67.950  139.462 1.00 26.74 ?  133 LYS C CD    1 
ATOM   12070 C  CE    . LYS C 2 154 ? 110.693 66.557  139.013 1.00 27.93 ?  133 LYS C CE    1 
ATOM   12071 N  NZ    . LYS C 2 154 ? 111.556 65.871  140.011 1.00 27.86 1  133 LYS C NZ    1 
ATOM   12072 N  N     . LYS C 2 155 ? 110.849 72.087  136.992 1.00 22.77 ?  134 LYS C N     1 
ATOM   12073 C  CA    . LYS C 2 155 ? 111.777 72.181  135.861 1.00 22.87 ?  134 LYS C CA    1 
ATOM   12074 C  C     . LYS C 2 155 ? 113.088 72.851  136.260 1.00 22.30 ?  134 LYS C C     1 
ATOM   12075 O  O     . LYS C 2 155 ? 114.167 72.386  135.855 1.00 21.89 ?  134 LYS C O     1 
ATOM   12076 C  CB    . LYS C 2 155 ? 111.136 72.789  134.591 1.00 23.33 ?  134 LYS C CB    1 
ATOM   12077 C  CG    . LYS C 2 155 ? 110.930 74.283  134.567 1.00 24.25 ?  134 LYS C CG    1 
ATOM   12078 C  CD    . LYS C 2 155 ? 110.300 74.735  133.238 1.00 26.87 ?  134 LYS C CD    1 
ATOM   12079 C  CE    . LYS C 2 155 ? 108.780 74.612  133.276 1.00 28.26 ?  134 LYS C CE    1 
ATOM   12080 N  NZ    . LYS C 2 155 ? 108.171 75.342  132.122 1.00 28.97 1  134 LYS C NZ    1 
ATOM   12081 N  N     . ALA C 2 156 ? 112.995 73.896  137.082 1.00 21.96 ?  135 ALA C N     1 
ATOM   12082 C  CA    . ALA C 2 156 ? 114.183 74.518  137.697 1.00 22.43 ?  135 ALA C CA    1 
ATOM   12083 C  C     . ALA C 2 156 ? 114.977 73.544  138.569 1.00 22.02 ?  135 ALA C C     1 
ATOM   12084 O  O     . ALA C 2 156 ? 116.203 73.516  138.500 1.00 22.60 ?  135 ALA C O     1 
ATOM   12085 C  CB    . ALA C 2 156 ? 113.799 75.764  138.524 1.00 22.05 ?  135 ALA C CB    1 
ATOM   12086 N  N     . GLN C 2 157 ? 114.284 72.766  139.401 1.00 21.97 ?  136 GLN C N     1 
ATOM   12087 C  CA    . GLN C 2 157 ? 114.947 71.771  140.254 1.00 22.10 ?  136 GLN C CA    1 
ATOM   12088 C  C     . GLN C 2 157 ? 115.764 70.799  139.426 1.00 21.87 ?  136 GLN C C     1 
ATOM   12089 O  O     . GLN C 2 157 ? 116.899 70.484  139.781 1.00 21.75 ?  136 GLN C O     1 
ATOM   12090 C  CB    . GLN C 2 157 ? 113.935 70.957  141.061 1.00 22.50 ?  136 GLN C CB    1 
ATOM   12091 C  CG    . GLN C 2 157 ? 113.400 71.646  142.307 1.00 23.55 ?  136 GLN C CG    1 
ATOM   12092 C  CD    . GLN C 2 157 ? 112.118 70.985  142.780 1.00 26.93 ?  136 GLN C CD    1 
ATOM   12093 O  OE1   . GLN C 2 157 ? 111.875 69.817  142.483 1.00 26.36 ?  136 GLN C OE1   1 
ATOM   12094 N  NE2   . GLN C 2 157 ? 111.281 71.733  143.491 1.00 28.09 ?  136 GLN C NE2   1 
ATOM   12095 N  N     . MET C 2 158 ? 115.166 70.321  138.336 1.00 21.38 ?  137 MET C N     1 
ATOM   12096 C  CA    . MET C 2 158 ? 115.786 69.312  137.491 1.00 22.08 ?  137 MET C CA    1 
ATOM   12097 C  C     . MET C 2 158 ? 116.985 69.858  136.724 1.00 21.70 ?  137 MET C C     1 
ATOM   12098 O  O     . MET C 2 158 ? 118.027 69.205  136.625 1.00 21.83 ?  137 MET C O     1 
ATOM   12099 C  CB    . MET C 2 158 ? 114.774 68.764  136.490 1.00 22.05 ?  137 MET C CB    1 
ATOM   12100 C  CG    . MET C 2 158 ? 113.744 67.800  137.093 1.00 23.93 ?  137 MET C CG    1 
ATOM   12101 S  SD    . MET C 2 158 ? 112.481 67.403  135.867 1.00 27.75 ?  137 MET C SD    1 
ATOM   12102 C  CE    . MET C 2 158 ? 113.461 66.411  134.730 1.00 26.00 ?  137 MET C CE    1 
ATOM   12103 N  N     . ILE C 2 159 ? 116.820 71.040  136.148 1.00 20.90 ?  138 ILE C N     1 
ATOM   12104 C  CA    . ILE C 2 159 ? 117.870 71.612  135.322 1.00 20.60 ?  138 ILE C CA    1 
ATOM   12105 C  C     . ILE C 2 159 ? 119.046 72.062  136.193 1.00 20.36 ?  138 ILE C C     1 
ATOM   12106 O  O     . ILE C 2 159 ? 120.192 71.702  135.916 1.00 19.65 ?  138 ILE C O     1 
ATOM   12107 C  CB    . ILE C 2 159 ? 117.331 72.761  134.420 1.00 20.17 ?  138 ILE C CB    1 
ATOM   12108 C  CG1   . ILE C 2 159 ? 116.341 72.214  133.375 1.00 20.66 ?  138 ILE C CG1   1 
ATOM   12109 C  CG2   . ILE C 2 159 ? 118.486 73.571  133.807 1.00 20.62 ?  138 ILE C CG2   1 
ATOM   12110 C  CD1   . ILE C 2 159 ? 116.899 71.244  132.329 1.00 22.17 ?  138 ILE C CD1   1 
ATOM   12111 N  N     . VAL C 2 160 ? 118.755 72.819  137.252 1.00 19.58 ?  139 VAL C N     1 
ATOM   12112 C  CA    . VAL C 2 160 ? 119.795 73.349  138.140 1.00 19.88 ?  139 VAL C CA    1 
ATOM   12113 C  C     . VAL C 2 160 ? 120.487 72.213  138.899 1.00 19.44 ?  139 VAL C C     1 
ATOM   12114 O  O     . VAL C 2 160 ? 121.670 72.297  139.209 1.00 19.88 ?  139 VAL C O     1 
ATOM   12115 C  CB    . VAL C 2 160 ? 119.242 74.418  139.150 1.00 19.52 ?  139 VAL C CB    1 
ATOM   12116 C  CG1   . VAL C 2 160 ? 120.342 74.880  140.122 1.00 20.75 ?  139 VAL C CG1   1 
ATOM   12117 C  CG2   . VAL C 2 160 ? 118.694 75.631  138.407 1.00 20.03 ?  139 VAL C CG2   1 
ATOM   12118 N  N     . GLY C 2 161 ? 119.748 71.147  139.190 1.00 19.13 ?  140 GLY C N     1 
ATOM   12119 C  CA    . GLY C 2 161 ? 120.335 70.004  139.870 1.00 18.05 ?  140 GLY C CA    1 
ATOM   12120 C  C     . GLY C 2 161 ? 121.449 69.413  139.044 1.00 17.86 ?  140 GLY C C     1 
ATOM   12121 O  O     . GLY C 2 161 ? 122.528 69.099  139.559 1.00 17.47 ?  140 GLY C O     1 
ATOM   12122 N  N     . LEU C 2 162 ? 121.184 69.248  137.753 1.00 17.92 ?  141 LEU C N     1 
ATOM   12123 C  CA    . LEU C 2 162 ? 122.195 68.741  136.832 1.00 18.32 ?  141 LEU C CA    1 
ATOM   12124 C  C     . LEU C 2 162 ? 123.410 69.686  136.697 1.00 18.55 ?  141 LEU C C     1 
ATOM   12125 O  O     . LEU C 2 162 ? 124.550 69.222  136.680 1.00 18.49 ?  141 LEU C O     1 
ATOM   12126 C  CB    . LEU C 2 162 ? 121.561 68.444  135.468 1.00 18.50 ?  141 LEU C CB    1 
ATOM   12127 C  CG    . LEU C 2 162 ? 120.623 67.234  135.470 1.00 19.32 ?  141 LEU C CG    1 
ATOM   12128 C  CD1   . LEU C 2 162 ? 119.747 67.234  134.221 1.00 20.38 ?  141 LEU C CD1   1 
ATOM   12129 C  CD2   . LEU C 2 162 ? 121.410 65.927  135.595 1.00 19.94 ?  141 LEU C CD2   1 
ATOM   12130 N  N     . TYR C 2 163 ? 123.176 70.994  136.638 1.00 19.16 ?  142 TYR C N     1 
ATOM   12131 C  CA    . TYR C 2 163 ? 124.286 71.969  136.644 1.00 20.16 ?  142 TYR C CA    1 
ATOM   12132 C  C     . TYR C 2 163 ? 125.168 71.823  137.870 1.00 20.78 ?  142 TYR C C     1 
ATOM   12133 O  O     . TYR C 2 163 ? 126.398 71.870  137.780 1.00 20.36 ?  142 TYR C O     1 
ATOM   12134 C  CB    . TYR C 2 163 ? 123.773 73.419  136.595 1.00 20.34 ?  142 TYR C CB    1 
ATOM   12135 C  CG    . TYR C 2 163 ? 123.047 73.806  135.315 1.00 22.46 ?  142 TYR C CG    1 
ATOM   12136 C  CD1   . TYR C 2 163 ? 123.272 73.129  134.121 1.00 23.88 ?  142 TYR C CD1   1 
ATOM   12137 C  CD2   . TYR C 2 163 ? 122.142 74.861  135.306 1.00 22.41 ?  142 TYR C CD2   1 
ATOM   12138 C  CE1   . TYR C 2 163 ? 122.594 73.493  132.943 1.00 25.93 ?  142 TYR C CE1   1 
ATOM   12139 C  CE2   . TYR C 2 163 ? 121.470 75.230  134.143 1.00 22.07 ?  142 TYR C CE2   1 
ATOM   12140 C  CZ    . TYR C 2 163 ? 121.706 74.553  132.970 1.00 25.19 ?  142 TYR C CZ    1 
ATOM   12141 O  OH    . TYR C 2 163 ? 121.025 74.939  131.834 1.00 27.43 ?  142 TYR C OH    1 
ATOM   12142 N  N     . LYS C 2 164 ? 124.536 71.644  139.024 1.00 21.39 ?  143 LYS C N     1 
ATOM   12143 C  CA    . LYS C 2 164 ? 125.289 71.610  140.267 1.00 22.49 ?  143 LYS C CA    1 
ATOM   12144 C  C     . LYS C 2 164 ? 125.913 70.244  140.543 1.00 22.49 ?  143 LYS C C     1 
ATOM   12145 O  O     . LYS C 2 164 ? 126.760 70.120  141.421 1.00 22.45 ?  143 LYS C O     1 
ATOM   12146 C  CB    . LYS C 2 164 ? 124.451 72.136  141.430 1.00 23.16 ?  143 LYS C CB    1 
ATOM   12147 C  CG    . LYS C 2 164 ? 124.173 73.631  141.285 1.00 26.08 ?  143 LYS C CG    1 
ATOM   12148 C  CD    . LYS C 2 164 ? 123.843 74.281  142.597 1.00 30.38 ?  143 LYS C CD    1 
ATOM   12149 C  CE    . LYS C 2 164 ? 123.764 75.781  142.447 1.00 32.69 ?  143 LYS C CE    1 
ATOM   12150 N  NZ    . LYS C 2 164 ? 123.388 76.410  143.743 1.00 35.60 1  143 LYS C NZ    1 
ATOM   12151 N  N     . ALA C 2 165 ? 125.549 69.246  139.737 1.00 22.02 ?  144 ALA C N     1 
ATOM   12152 C  CA    . ALA C 2 165 ? 126.144 67.929  139.853 1.00 22.69 ?  144 ALA C CA    1 
ATOM   12153 C  C     . ALA C 2 165 ? 127.448 67.781  139.050 1.00 23.20 ?  144 ALA C C     1 
ATOM   12154 O  O     . ALA C 2 165 ? 128.131 66.771  139.169 1.00 23.80 ?  144 ALA C O     1 
ATOM   12155 C  CB    . ALA C 2 165 ? 125.121 66.833  139.462 1.00 21.79 ?  144 ALA C CB    1 
ATOM   12156 N  N     . ILE C 2 166 ? 127.800 68.778  138.234 1.00 23.97 ?  145 ILE C N     1 
ATOM   12157 C  CA    . ILE C 2 166 ? 129.045 68.706  137.460 1.00 24.29 ?  145 ILE C CA    1 
ATOM   12158 C  C     . ILE C 2 166 ? 130.245 68.531  138.393 1.00 25.49 ?  145 ILE C C     1 
ATOM   12159 O  O     . ILE C 2 166 ? 130.369 69.233  139.392 1.00 25.82 ?  145 ILE C O     1 
ATOM   12160 C  CB    . ILE C 2 166 ? 129.268 69.950  136.551 1.00 24.22 ?  145 ILE C CB    1 
ATOM   12161 C  CG1   . ILE C 2 166 ? 128.136 70.103  135.541 1.00 23.45 ?  145 ILE C CG1   1 
ATOM   12162 C  CG2   . ILE C 2 166 ? 130.604 69.844  135.813 1.00 23.42 ?  145 ILE C CG2   1 
ATOM   12163 C  CD1   . ILE C 2 166 ? 128.124 71.479  134.826 1.00 21.99 ?  145 ILE C CD1   1 
ATOM   12164 N  N     . GLN C 2 167 ? 131.090 67.558  138.084 1.00 26.83 ?  146 GLN C N     1 
ATOM   12165 C  CA    . GLN C 2 167 ? 132.297 67.312  138.860 1.00 28.85 ?  146 GLN C CA    1 
ATOM   12166 C  C     . GLN C 2 167 ? 133.491 67.696  138.009 1.00 29.77 ?  146 GLN C C     1 
ATOM   12167 O  O     . GLN C 2 167 ? 133.532 67.391  136.812 1.00 29.74 ?  146 GLN C O     1 
ATOM   12168 C  CB    . GLN C 2 167 ? 132.399 65.839  139.285 1.00 28.99 ?  146 GLN C CB    1 
ATOM   12169 C  CG    . GLN C 2 167 ? 131.408 65.415  140.369 1.00 30.30 ?  146 GLN C CG    1 
ATOM   12170 C  CD    . GLN C 2 167 ? 131.725 66.014  141.733 1.00 33.32 ?  146 GLN C CD    1 
ATOM   12171 O  OE1   . GLN C 2 167 ? 132.791 66.598  141.934 1.00 34.63 ?  146 GLN C OE1   1 
ATOM   12172 N  NE2   . GLN C 2 167 ? 130.807 65.849  142.683 1.00 32.32 ?  146 GLN C NE2   1 
ATOM   12173 N  N     . LYS C 2 168 ? 134.455 68.370  138.625 1.00 31.29 ?  147 LYS C N     1 
ATOM   12174 C  CA    . LYS C 2 168 ? 135.670 68.790  137.928 1.00 33.14 ?  147 LYS C CA    1 
ATOM   12175 C  C     . LYS C 2 168 ? 136.317 67.581  137.264 1.00 33.79 ?  147 LYS C C     1 
ATOM   12176 O  O     . LYS C 2 168 ? 136.320 66.479  137.824 1.00 34.06 ?  147 LYS C O     1 
ATOM   12177 C  CB    . LYS C 2 168 ? 136.635 69.467  138.898 1.00 33.44 ?  147 LYS C CB    1 
ATOM   12178 C  CG    . LYS C 2 168 ? 137.678 70.379  138.256 1.00 35.61 ?  147 LYS C CG    1 
ATOM   12179 C  CD    . LYS C 2 168 ? 138.536 71.022  139.341 1.00 38.40 ?  147 LYS C CD    1 
ATOM   12180 C  CE    . LYS C 2 168 ? 139.404 72.151  138.811 1.00 40.48 ?  147 LYS C CE    1 
ATOM   12181 N  NZ    . LYS C 2 168 ? 140.780 71.669  138.521 1.00 41.56 1  147 LYS C NZ    1 
ATOM   12182 N  N     . ASP C 2 169 ? 136.814 67.787  136.049 1.00 35.10 ?  148 ASP C N     1 
ATOM   12183 C  CA    . ASP C 2 169 ? 137.478 66.733  135.264 1.00 36.27 ?  148 ASP C CA    1 
ATOM   12184 C  C     . ASP C 2 169 ? 136.626 65.493  134.988 1.00 36.29 ?  148 ASP C C     1 
ATOM   12185 O  O     . ASP C 2 169 ? 137.151 64.446  134.606 1.00 36.95 ?  148 ASP C O     1 
ATOM   12186 C  CB    . ASP C 2 169 ? 138.792 66.315  135.931 1.00 37.15 ?  148 ASP C CB    1 
ATOM   12187 C  CG    . ASP C 2 169 ? 139.850 67.383  135.852 1.00 38.94 ?  148 ASP C CG    1 
ATOM   12188 O  OD1   . ASP C 2 169 ? 139.756 68.261  134.962 1.00 41.71 ?  148 ASP C OD1   1 
ATOM   12189 O  OD2   . ASP C 2 169 ? 140.778 67.343  136.685 1.00 41.64 -1 148 ASP C OD2   1 
ATOM   12190 N  N     . ASP C 2 170 ? 135.317 65.602  135.183 1.00 35.87 ?  149 ASP C N     1 
ATOM   12191 C  CA    . ASP C 2 170 ? 134.422 64.488  134.900 1.00 35.24 ?  149 ASP C CA    1 
ATOM   12192 C  C     . ASP C 2 170 ? 133.523 64.899  133.742 1.00 34.12 ?  149 ASP C C     1 
ATOM   12193 O  O     . ASP C 2 170 ? 132.542 65.651  133.914 1.00 33.52 ?  149 ASP C O     1 
ATOM   12194 C  CB    . ASP C 2 170 ? 133.637 64.083  136.152 1.00 36.09 ?  149 ASP C CB    1 
ATOM   12195 C  CG    . ASP C 2 170 ? 132.546 63.049  135.871 1.00 38.39 ?  149 ASP C CG    1 
ATOM   12196 O  OD1   . ASP C 2 170 ? 132.539 62.411  134.792 1.00 42.06 ?  149 ASP C OD1   1 
ATOM   12197 O  OD2   . ASP C 2 170 ? 131.686 62.865  136.754 1.00 42.21 -1 149 ASP C OD2   1 
ATOM   12198 N  N     . GLU C 2 171 ? 133.889 64.408  132.562 1.00 32.48 ?  150 GLU C N     1 
ATOM   12199 C  CA    . GLU C 2 171 ? 133.260 64.810  131.317 1.00 30.93 ?  150 GLU C CA    1 
ATOM   12200 C  C     . GLU C 2 171 ? 131.813 64.323  131.199 1.00 29.37 ?  150 GLU C C     1 
ATOM   12201 O  O     . GLU C 2 171 ? 131.001 64.958  130.526 1.00 28.99 ?  150 GLU C O     1 
ATOM   12202 C  CB    . GLU C 2 171 ? 134.110 64.373  130.108 1.00 31.30 ?  150 GLU C CB    1 
ATOM   12203 C  CG    . GLU C 2 171 ? 134.141 62.857  129.797 1.00 33.64 ?  150 GLU C CG    1 
ATOM   12204 C  CD    . GLU C 2 171 ? 135.235 62.447  128.782 1.00 36.40 ?  150 GLU C CD    1 
ATOM   12205 O  OE1   . GLU C 2 171 ? 135.965 63.324  128.271 1.00 38.62 ?  150 GLU C OE1   1 
ATOM   12206 O  OE2   . GLU C 2 171 ? 135.368 61.235  128.494 1.00 37.42 -1 150 GLU C OE2   1 
ATOM   12207 N  N     . ILE C 2 172 ? 131.496 63.202  131.848 1.00 27.68 ?  151 ILE C N     1 
ATOM   12208 C  CA    . ILE C 2 172 ? 130.138 62.654  131.793 1.00 26.26 ?  151 ILE C CA    1 
ATOM   12209 C  C     . ILE C 2 172 ? 129.148 63.550  132.544 1.00 24.85 ?  151 ILE C C     1 
ATOM   12210 O  O     . ILE C 2 172 ? 128.064 63.820  132.030 1.00 23.53 ?  151 ILE C O     1 
ATOM   12211 C  CB    . ILE C 2 172 ? 130.067 61.184  132.288 1.00 26.53 ?  151 ILE C CB    1 
ATOM   12212 C  CG1   . ILE C 2 172 ? 130.936 60.272  131.407 1.00 27.59 ?  151 ILE C CG1   1 
ATOM   12213 C  CG2   . ILE C 2 172 ? 128.613 60.684  132.370 1.00 26.51 ?  151 ILE C CG2   1 
ATOM   12214 C  CD1   . ILE C 2 172 ? 130.458 60.101  129.959 1.00 26.91 ?  151 ILE C CD1   1 
ATOM   12215 N  N     . SER C 2 173 ? 129.517 64.019  133.738 1.00 23.58 ?  152 SER C N     1 
ATOM   12216 C  CA    . SER C 2 173 ? 128.631 64.925  134.466 1.00 22.36 ?  152 SER C CA    1 
ATOM   12217 C  C     . SER C 2 173 ? 128.457 66.236  133.695 1.00 21.79 ?  152 SER C C     1 
ATOM   12218 O  O     . SER C 2 173 ? 127.380 66.843  133.720 1.00 20.91 ?  152 SER C O     1 
ATOM   12219 C  CB    . SER C 2 173 ? 129.103 65.168  135.905 1.00 22.43 ?  152 SER C CB    1 
ATOM   12220 O  OG    . SER C 2 173 ? 130.390 65.764  135.941 1.00 24.02 ?  152 SER C OG    1 
ATOM   12221 N  N     . LEU C 2 174 ? 129.522 66.662  133.015 1.00 21.65 ?  153 LEU C N     1 
ATOM   12222 C  CA    . LEU C 2 174 ? 129.482 67.870  132.194 1.00 21.86 ?  153 LEU C CA    1 
ATOM   12223 C  C     . LEU C 2 174 ? 128.539 67.692  131.001 1.00 21.98 ?  153 LEU C C     1 
ATOM   12224 O  O     . LEU C 2 174 ? 127.718 68.573  130.738 1.00 21.64 ?  153 LEU C O     1 
ATOM   12225 C  CB    . LEU C 2 174 ? 130.892 68.304  131.742 1.00 21.71 ?  153 LEU C CB    1 
ATOM   12226 C  CG    . LEU C 2 174 ? 131.033 69.556  130.855 1.00 22.04 ?  153 LEU C CG    1 
ATOM   12227 C  CD1   . LEU C 2 174 ? 130.327 70.778  131.440 1.00 21.99 ?  153 LEU C CD1   1 
ATOM   12228 C  CD2   . LEU C 2 174 ? 132.516 69.859  130.612 1.00 23.37 ?  153 LEU C CD2   1 
ATOM   12229 N  N     . PHE C 2 175 ? 128.654 66.559  130.301 1.00 22.17 ?  154 PHE C N     1 
ATOM   12230 C  CA    . PHE C 2 175 ? 127.742 66.215  129.187 1.00 22.02 ?  154 PHE C CA    1 
ATOM   12231 C  C     . PHE C 2 175 ? 126.278 66.280  129.607 1.00 21.86 ?  154 PHE C C     1 
ATOM   12232 O  O     . PHE C 2 175 ? 125.430 66.806  128.875 1.00 21.62 ?  154 PHE C O     1 
ATOM   12233 C  CB    . PHE C 2 175 ? 128.034 64.804  128.654 1.00 22.08 ?  154 PHE C CB    1 
ATOM   12234 C  CG    . PHE C 2 175 ? 127.032 64.315  127.625 1.00 21.99 ?  154 PHE C CG    1 
ATOM   12235 C  CD1   . PHE C 2 175 ? 127.155 64.680  126.282 1.00 20.87 ?  154 PHE C CD1   1 
ATOM   12236 C  CD2   . PHE C 2 175 ? 125.956 63.500  128.008 1.00 20.82 ?  154 PHE C CD2   1 
ATOM   12237 C  CE1   . PHE C 2 175 ? 126.221 64.258  125.334 1.00 20.27 ?  154 PHE C CE1   1 
ATOM   12238 C  CE2   . PHE C 2 175 ? 125.018 63.060  127.070 1.00 20.19 ?  154 PHE C CE2   1 
ATOM   12239 C  CZ    . PHE C 2 175 ? 125.153 63.435  125.721 1.00 20.93 ?  154 PHE C CZ    1 
ATOM   12240 N  N     . LYS C 2 176 ? 125.984 65.702  130.772 1.00 21.98 ?  155 LYS C N     1 
ATOM   12241 C  CA    . LYS C 2 176 ? 124.612 65.666  131.286 1.00 21.79 ?  155 LYS C CA    1 
ATOM   12242 C  C     . LYS C 2 176 ? 124.064 67.080  131.512 1.00 21.70 ?  155 LYS C C     1 
ATOM   12243 O  O     . LYS C 2 176 ? 122.915 67.374  131.151 1.00 21.10 ?  155 LYS C O     1 
ATOM   12244 C  CB    . LYS C 2 176 ? 124.538 64.820  132.564 1.00 22.00 ?  155 LYS C CB    1 
ATOM   12245 C  CG    . LYS C 2 176 ? 124.815 63.339  132.341 1.00 21.93 ?  155 LYS C CG    1 
ATOM   12246 C  CD    . LYS C 2 176 ? 124.797 62.561  133.646 1.00 23.06 ?  155 LYS C CD    1 
ATOM   12247 C  CE    . LYS C 2 176 ? 125.008 61.079  133.411 1.00 24.91 ?  155 LYS C CE    1 
ATOM   12248 N  NZ    . LYS C 2 176 ? 125.319 60.361  134.691 1.00 25.16 1  155 LYS C NZ    1 
ATOM   12249 N  N     . ALA C 2 177 ? 124.889 67.950  132.103 1.00 21.49 ?  156 ALA C N     1 
ATOM   12250 C  CA    . ALA C 2 177 ? 124.516 69.351  132.272 1.00 20.60 ?  156 ALA C CA    1 
ATOM   12251 C  C     . ALA C 2 177 ? 124.355 70.105  130.933 1.00 20.37 ?  156 ALA C C     1 
ATOM   12252 O  O     . ALA C 2 177 ? 123.477 70.948  130.807 1.00 19.61 ?  156 ALA C O     1 
ATOM   12253 C  CB    . ALA C 2 177 ? 125.502 70.076  133.183 1.00 20.88 ?  156 ALA C CB    1 
ATOM   12254 N  N     . MET C 2 178 ? 125.190 69.788  129.944 1.00 20.70 ?  157 MET C N     1 
ATOM   12255 C  CA    . MET C 2 178 ? 125.070 70.402  128.610 1.00 21.06 ?  157 MET C CA    1 
ATOM   12256 C  C     . MET C 2 178 ? 123.805 69.962  127.898 1.00 20.83 ?  157 MET C C     1 
ATOM   12257 O  O     . MET C 2 178 ? 123.228 70.735  127.127 1.00 21.28 ?  157 MET C O     1 
ATOM   12258 C  CB    . MET C 2 178 ? 126.283 70.078  127.718 1.00 20.68 ?  157 MET C CB    1 
ATOM   12259 C  CG    . MET C 2 178 ? 127.605 70.721  128.131 1.00 21.61 ?  157 MET C CG    1 
ATOM   12260 S  SD    . MET C 2 178 ? 128.970 70.056  127.151 1.00 24.32 ?  157 MET C SD    1 
ATOM   12261 C  CE    . MET C 2 178 ? 130.283 71.222  127.569 1.00 23.64 ?  157 MET C CE    1 
ATOM   12262 N  N     . VAL C 2 179 ? 123.390 68.714  128.116 1.00 20.76 ?  158 VAL C N     1 
ATOM   12263 C  CA    . VAL C 2 179 ? 122.118 68.231  127.565 1.00 20.14 ?  158 VAL C CA    1 
ATOM   12264 C  C     . VAL C 2 179 ? 120.972 69.026  128.200 1.00 20.35 ?  158 VAL C C     1 
ATOM   12265 O  O     . VAL C 2 179 ? 120.058 69.485  127.510 1.00 19.82 ?  158 VAL C O     1 
ATOM   12266 C  CB    . VAL C 2 179 ? 121.903 66.716  127.826 1.00 20.07 ?  158 VAL C CB    1 
ATOM   12267 C  CG1   . VAL C 2 179 ? 120.472 66.305  127.472 1.00 20.07 ?  158 VAL C CG1   1 
ATOM   12268 C  CG2   . VAL C 2 179 ? 122.904 65.887  127.027 1.00 20.57 ?  158 VAL C CG2   1 
ATOM   12269 N  N     . ALA C 2 180 ? 121.042 69.180  129.518 1.00 19.89 ?  159 ALA C N     1 
ATOM   12270 C  CA    . ALA C 2 180 ? 120.058 69.960  130.268 1.00 20.50 ?  159 ALA C CA    1 
ATOM   12271 C  C     . ALA C 2 180 ? 119.988 71.401  129.736 1.00 20.67 ?  159 ALA C C     1 
ATOM   12272 O  O     . ALA C 2 180 ? 118.898 71.932  129.516 1.00 21.27 ?  159 ALA C O     1 
ATOM   12273 C  CB    . ALA C 2 180 ? 120.416 69.959  131.739 1.00 20.03 ?  159 ALA C CB    1 
ATOM   12274 N  N     . SER C 2 181 ? 121.152 72.013  129.521 1.00 20.78 ?  160 SER C N     1 
ATOM   12275 C  CA    . SER C 2 181 ? 121.241 73.368  128.963 1.00 21.26 ?  160 SER C CA    1 
ATOM   12276 C  C     . SER C 2 181 ? 120.653 73.459  127.547 1.00 21.19 ?  160 SER C C     1 
ATOM   12277 O  O     . SER C 2 181 ? 119.885 74.369  127.257 1.00 20.89 ?  160 SER C O     1 
ATOM   12278 C  CB    . SER C 2 181 ? 122.690 73.877  128.986 1.00 21.42 ?  160 SER C CB    1 
ATOM   12279 O  OG    . SER C 2 181 ? 122.770 75.220  128.531 1.00 23.69 ?  160 SER C OG    1 
ATOM   12280 N  N     . VAL C 2 182 ? 121.009 72.521  126.662 1.00 20.99 ?  161 VAL C N     1 
ATOM   12281 C  CA    . VAL C 2 182 ? 120.374 72.497  125.340 1.00 21.18 ?  161 VAL C CA    1 
ATOM   12282 C  C     . VAL C 2 182 ? 118.846 72.368  125.464 1.00 21.15 ?  161 VAL C C     1 
ATOM   12283 O  O     . VAL C 2 182 ? 118.100 73.075  124.767 1.00 21.18 ?  161 VAL C O     1 
ATOM   12284 C  CB    . VAL C 2 182 ? 120.959 71.389  124.408 1.00 21.11 ?  161 VAL C CB    1 
ATOM   12285 C  CG1   . VAL C 2 182 ? 120.134 71.268  123.129 1.00 21.75 ?  161 VAL C CG1   1 
ATOM   12286 C  CG2   . VAL C 2 182 ? 122.418 71.691  124.070 1.00 20.98 ?  161 VAL C CG2   1 
ATOM   12287 N  N     . TYR C 2 183 ? 118.369 71.488  126.354 1.00 21.10 ?  162 TYR C N     1 
ATOM   12288 C  CA    . TYR C 2 183 ? 116.919 71.344  126.558 1.00 21.21 ?  162 TYR C CA    1 
ATOM   12289 C  C     . TYR C 2 183 ? 116.261 72.622  127.077 1.00 21.38 ?  162 TYR C C     1 
ATOM   12290 O  O     . TYR C 2 183 ? 115.120 72.912  126.736 1.00 20.97 ?  162 TYR C O     1 
ATOM   12291 C  CB    . TYR C 2 183 ? 116.560 70.159  127.478 1.00 21.50 ?  162 TYR C CB    1 
ATOM   12292 C  CG    . TYR C 2 183 ? 116.777 68.808  126.853 1.00 22.20 ?  162 TYR C CG    1 
ATOM   12293 C  CD1   . TYR C 2 183 ? 116.841 68.660  125.469 1.00 23.80 ?  162 TYR C CD1   1 
ATOM   12294 C  CD2   . TYR C 2 183 ? 116.900 67.662  127.648 1.00 23.71 ?  162 TYR C CD2   1 
ATOM   12295 C  CE1   . TYR C 2 183 ? 117.043 67.404  124.885 1.00 25.52 ?  162 TYR C CE1   1 
ATOM   12296 C  CE2   . TYR C 2 183 ? 117.095 66.413  127.079 1.00 24.01 ?  162 TYR C CE2   1 
ATOM   12297 C  CZ    . TYR C 2 183 ? 117.176 66.289  125.703 1.00 25.47 ?  162 TYR C CZ    1 
ATOM   12298 O  OH    . TYR C 2 183 ? 117.387 65.051  125.132 1.00 25.37 ?  162 TYR C OH    1 
ATOM   12299 N  N     . LEU C 2 184 ? 116.976 73.366  127.908 1.00 22.12 ?  163 LEU C N     1 
ATOM   12300 C  CA    . LEU C 2 184 ? 116.493 74.684  128.362 1.00 23.80 ?  163 LEU C CA    1 
ATOM   12301 C  C     . LEU C 2 184 ? 116.473 75.679  127.193 1.00 24.21 ?  163 LEU C C     1 
ATOM   12302 O  O     . LEU C 2 184 ? 115.486 76.357  126.998 1.00 24.72 ?  163 LEU C O     1 
ATOM   12303 C  CB    . LEU C 2 184 ? 117.347 75.215  129.518 1.00 23.52 ?  163 LEU C CB    1 
ATOM   12304 C  CG    . LEU C 2 184 ? 116.970 76.535  130.222 1.00 24.91 ?  163 LEU C CG    1 
ATOM   12305 C  CD1   . LEU C 2 184 ? 117.342 76.457  131.680 1.00 24.81 ?  163 LEU C CD1   1 
ATOM   12306 C  CD2   . LEU C 2 184 ? 117.609 77.772  129.575 1.00 26.39 ?  163 LEU C CD2   1 
ATOM   12307 N  N     . GLU C 2 185 ? 117.560 75.739  126.412 1.00 25.17 ?  164 GLU C N     1 
ATOM   12308 C  CA    . GLU C 2 185 ? 117.695 76.725  125.328 1.00 25.30 ?  164 GLU C CA    1 
ATOM   12309 C  C     . GLU C 2 185 ? 116.709 76.501  124.169 1.00 25.07 ?  164 GLU C C     1 
ATOM   12310 O  O     . GLU C 2 185 ? 116.108 77.452  123.641 1.00 24.49 ?  164 GLU C O     1 
ATOM   12311 C  CB    . GLU C 2 185 ? 119.129 76.717  124.748 1.00 26.17 ?  164 GLU C CB    1 
ATOM   12312 C  CG    . GLU C 2 185 ? 120.232 77.188  125.721 1.00 27.05 ?  164 GLU C CG    1 
ATOM   12313 C  CD    . GLU C 2 185 ? 120.286 78.712  125.884 1.00 29.23 ?  164 GLU C CD    1 
ATOM   12314 O  OE1   . GLU C 2 185 ? 119.466 79.445  125.261 1.00 28.79 ?  164 GLU C OE1   1 
ATOM   12315 O  OE2   . GLU C 2 185 ? 121.179 79.200  126.615 1.00 28.65 -1 164 GLU C OE2   1 
ATOM   12316 N  N     . SER C 2 186 ? 116.577 75.241  123.776 1.00 24.23 ?  165 SER C N     1 
ATOM   12317 C  CA    . SER C 2 186 ? 115.991 74.870  122.494 1.00 24.71 ?  165 SER C CA    1 
ATOM   12318 C  C     . SER C 2 186 ? 114.635 74.182  122.614 1.00 24.51 ?  165 SER C C     1 
ATOM   12319 O  O     . SER C 2 186 ? 113.970 73.959  121.605 1.00 24.87 ?  165 SER C O     1 
ATOM   12320 C  CB    . SER C 2 186 ? 116.956 73.950  121.733 1.00 25.06 ?  165 SER C CB    1 
ATOM   12321 O  OG    . SER C 2 186 ? 118.211 74.572  121.526 1.00 26.29 ?  165 SER C OG    1 
ATOM   12322 N  N     . PHE C 2 187 ? 114.242 73.837  123.837 1.00 24.71 ?  166 PHE C N     1 
ATOM   12323 C  CA    . PHE C 2 187 ? 112.967 73.167  124.092 1.00 25.69 ?  166 PHE C CA    1 
ATOM   12324 C  C     . PHE C 2 187 ? 112.112 73.913  125.129 1.00 25.87 ?  166 PHE C C     1 
ATOM   12325 O  O     . PHE C 2 187 ? 111.009 74.352  124.799 1.00 26.03 ?  166 PHE C O     1 
ATOM   12326 C  CB    . PHE C 2 187 ? 113.183 71.699  124.508 1.00 25.54 ?  166 PHE C CB    1 
ATOM   12327 C  CG    . PHE C 2 187 ? 111.941 71.017  125.045 1.00 26.64 ?  166 PHE C CG    1 
ATOM   12328 C  CD1   . PHE C 2 187 ? 110.802 70.861  124.245 1.00 25.90 ?  166 PHE C CD1   1 
ATOM   12329 C  CD2   . PHE C 2 187 ? 111.916 70.517  126.350 1.00 27.45 ?  166 PHE C CD2   1 
ATOM   12330 C  CE1   . PHE C 2 187 ? 109.646 70.230  124.743 1.00 25.64 ?  166 PHE C CE1   1 
ATOM   12331 C  CE2   . PHE C 2 187 ? 110.763 69.877  126.863 1.00 26.52 ?  166 PHE C CE2   1 
ATOM   12332 C  CZ    . PHE C 2 187 ? 109.632 69.735  126.055 1.00 27.18 ?  166 PHE C CZ    1 
ATOM   12333 N  N     . LEU C 2 188 ? 112.629 74.059  126.351 1.00 26.13 ?  167 LEU C N     1 
ATOM   12334 C  CA    . LEU C 2 188 ? 111.854 74.599  127.499 1.00 27.13 ?  167 LEU C CA    1 
ATOM   12335 C  C     . LEU C 2 188 ? 111.369 76.054  127.366 1.00 27.22 ?  167 LEU C C     1 
ATOM   12336 O  O     . LEU C 2 188 ? 110.321 76.414  127.918 1.00 28.03 ?  167 LEU C O     1 
ATOM   12337 C  CB    . LEU C 2 188 ? 112.644 74.467  128.811 1.00 26.89 ?  167 LEU C CB    1 
ATOM   12338 C  CG    . LEU C 2 188 ? 112.993 73.105  129.429 1.00 28.64 ?  167 LEU C CG    1 
ATOM   12339 C  CD1   . LEU C 2 188 ? 113.817 73.298  130.700 1.00 28.34 ?  167 LEU C CD1   1 
ATOM   12340 C  CD2   . LEU C 2 188 ? 111.761 72.269  129.730 1.00 27.90 ?  167 LEU C CD2   1 
ATOM   12341 N  N     . PHE C 2 189 ? 112.142 76.891  126.683 1.00 26.79 ?  168 PHE C N     1 
ATOM   12342 C  CA    . PHE C 2 189 ? 111.747 78.284  126.480 1.00 26.90 ?  168 PHE C CA    1 
ATOM   12343 C  C     . PHE C 2 189 ? 110.489 78.386  125.609 1.00 26.52 ?  168 PHE C C     1 
ATOM   12344 O  O     . PHE C 2 189 ? 109.787 79.405  125.636 1.00 26.02 ?  168 PHE C O     1 
ATOM   12345 C  CB    . PHE C 2 189 ? 112.871 79.093  125.802 1.00 27.03 ?  168 PHE C CB    1 
ATOM   12346 C  CG    . PHE C 2 189 ? 113.904 79.684  126.759 1.00 28.09 ?  168 PHE C CG    1 
ATOM   12347 C  CD1   . PHE C 2 189 ? 113.526 80.516  127.815 1.00 28.69 ?  168 PHE C CD1   1 
ATOM   12348 C  CD2   . PHE C 2 189 ? 115.260 79.464  126.550 1.00 29.15 ?  168 PHE C CD2   1 
ATOM   12349 C  CE1   . PHE C 2 189 ? 114.478 81.076  128.680 1.00 28.50 ?  168 PHE C CE1   1 
ATOM   12350 C  CE2   . PHE C 2 189 ? 116.228 80.018  127.407 1.00 30.19 ?  168 PHE C CE2   1 
ATOM   12351 C  CZ    . PHE C 2 189 ? 115.828 80.830  128.484 1.00 29.81 ?  168 PHE C CZ    1 
ATOM   12352 N  N     . TYR C 2 190 ? 110.215 77.345  124.822 1.00 26.18 ?  169 TYR C N     1 
ATOM   12353 C  CA    . TYR C 2 190 ? 109.267 77.503  123.725 1.00 26.24 ?  169 TYR C CA    1 
ATOM   12354 C  C     . TYR C 2 190 ? 107.777 77.502  124.100 1.00 25.94 ?  169 TYR C C     1 
ATOM   12355 O  O     . TYR C 2 190 ? 106.954 78.076  123.385 1.00 25.71 ?  169 TYR C O     1 
ATOM   12356 C  CB    . TYR C 2 190 ? 109.637 76.586  122.558 1.00 27.13 ?  169 TYR C CB    1 
ATOM   12357 C  CG    . TYR C 2 190 ? 110.821 77.168  121.815 1.00 28.07 ?  169 TYR C CG    1 
ATOM   12358 C  CD1   . TYR C 2 190 ? 112.131 76.931  122.248 1.00 29.54 ?  169 TYR C CD1   1 
ATOM   12359 C  CD2   . TYR C 2 190 ? 110.632 78.014  120.722 1.00 29.31 ?  169 TYR C CD2   1 
ATOM   12360 C  CE1   . TYR C 2 190 ? 113.224 77.494  121.583 1.00 30.44 ?  169 TYR C CE1   1 
ATOM   12361 C  CE2   . TYR C 2 190 ? 111.723 78.583  120.046 1.00 30.64 ?  169 TYR C CE2   1 
ATOM   12362 C  CZ    . TYR C 2 190 ? 113.013 78.321  120.488 1.00 30.40 ?  169 TYR C CZ    1 
ATOM   12363 O  OH    . TYR C 2 190 ? 114.086 78.884  119.835 1.00 28.85 ?  169 TYR C OH    1 
ATOM   12364 N  N     . SER C 2 191 ? 107.448 76.913  125.246 1.00 25.17 ?  170 SER C N     1 
ATOM   12365 C  CA    . SER C 2 191 ? 106.091 76.994  125.779 1.00 25.10 ?  170 SER C CA    1 
ATOM   12366 C  C     . SER C 2 191 ? 105.787 78.455  126.133 1.00 25.16 ?  170 SER C C     1 
ATOM   12367 O  O     . SER C 2 191 ? 104.633 78.889  126.065 1.00 25.30 ?  170 SER C O     1 
ATOM   12368 C  CB    . SER C 2 191 ? 105.924 76.083  126.996 1.00 24.56 ?  170 SER C CB    1 
ATOM   12369 O  OG    . SER C 2 191 ? 106.742 76.505  128.070 1.00 24.98 ?  170 SER C OG    1 
ATOM   12370 N  N     . GLY C 2 192 ? 106.845 79.189  126.497 1.00 24.32 ?  171 GLY C N     1 
ATOM   12371 C  CA    . GLY C 2 192 ? 106.793 80.618  126.772 1.00 23.97 ?  171 GLY C CA    1 
ATOM   12372 C  C     . GLY C 2 192 ? 106.825 81.483  125.523 1.00 23.85 ?  171 GLY C C     1 
ATOM   12373 O  O     . GLY C 2 192 ? 105.970 82.355  125.370 1.00 23.99 ?  171 GLY C O     1 
ATOM   12374 N  N     . PHE C 2 193 ? 107.784 81.233  124.630 1.00 23.28 ?  172 PHE C N     1 
ATOM   12375 C  CA    . PHE C 2 193 ? 107.920 82.003  123.379 1.00 23.85 ?  172 PHE C CA    1 
ATOM   12376 C  C     . PHE C 2 193 ? 106.675 81.985  122.491 1.00 23.72 ?  172 PHE C C     1 
ATOM   12377 O  O     . PHE C 2 193 ? 106.452 82.926  121.731 1.00 23.92 ?  172 PHE C O     1 
ATOM   12378 C  CB    . PHE C 2 193 ? 109.098 81.513  122.527 1.00 23.47 ?  172 PHE C CB    1 
ATOM   12379 C  CG    . PHE C 2 193 ? 110.460 81.897  123.061 1.00 24.32 ?  172 PHE C CG    1 
ATOM   12380 C  CD1   . PHE C 2 193 ? 110.624 83.000  123.900 1.00 22.28 ?  172 PHE C CD1   1 
ATOM   12381 C  CD2   . PHE C 2 193 ? 111.587 81.160  122.692 1.00 23.82 ?  172 PHE C CD2   1 
ATOM   12382 C  CE1   . PHE C 2 193 ? 111.887 83.355  124.391 1.00 23.41 ?  172 PHE C CE1   1 
ATOM   12383 C  CE2   . PHE C 2 193 ? 112.863 81.502  123.173 1.00 24.70 ?  172 PHE C CE2   1 
ATOM   12384 C  CZ    . PHE C 2 193 ? 113.013 82.608  124.024 1.00 24.87 ?  172 PHE C CZ    1 
ATOM   12385 N  N     . TYR C 2 194 ? 105.891 80.906  122.563 1.00 23.31 ?  173 TYR C N     1 
ATOM   12386 C  CA    . TYR C 2 194 ? 104.725 80.740  121.692 1.00 23.26 ?  173 TYR C CA    1 
ATOM   12387 C  C     . TYR C 2 194 ? 103.833 81.985  121.690 1.00 23.04 ?  173 TYR C C     1 
ATOM   12388 O  O     . TYR C 2 194 ? 103.422 82.463  120.629 1.00 23.47 ?  173 TYR C O     1 
ATOM   12389 C  CB    . TYR C 2 194 ? 103.886 79.512  122.086 1.00 23.13 ?  173 TYR C CB    1 
ATOM   12390 C  CG    . TYR C 2 194 ? 102.724 79.247  121.137 1.00 24.10 ?  173 TYR C CG    1 
ATOM   12391 C  CD1   . TYR C 2 194 ? 102.864 78.357  120.071 1.00 25.72 ?  173 TYR C CD1   1 
ATOM   12392 C  CD2   . TYR C 2 194 ? 101.502 79.903  121.289 1.00 27.04 ?  173 TYR C CD2   1 
ATOM   12393 C  CE1   . TYR C 2 194 ? 101.803 78.109  119.189 1.00 28.94 ?  173 TYR C CE1   1 
ATOM   12394 C  CE2   . TYR C 2 194 ? 100.433 79.670  120.403 1.00 27.84 ?  173 TYR C CE2   1 
ATOM   12395 C  CZ    . TYR C 2 194 ? 100.599 78.773  119.360 1.00 29.97 ?  173 TYR C CZ    1 
ATOM   12396 O  OH    . TYR C 2 194 ? 99.565  78.535  118.472 1.00 34.34 ?  173 TYR C OH    1 
ATOM   12397 N  N     . TYR C 2 195 ? 103.535 82.493  122.876 1.00 22.51 ?  174 TYR C N     1 
ATOM   12398 C  CA    . TYR C 2 195 ? 102.484 83.493  123.025 1.00 22.60 ?  174 TYR C CA    1 
ATOM   12399 C  C     . TYR C 2 195 ? 102.881 84.885  122.499 1.00 22.64 ?  174 TYR C C     1 
ATOM   12400 O  O     . TYR C 2 195 ? 102.103 85.483  121.749 1.00 22.39 ?  174 TYR C O     1 
ATOM   12401 C  CB    . TYR C 2 195 ? 101.977 83.524  124.467 1.00 22.32 ?  174 TYR C CB    1 
ATOM   12402 C  CG    . TYR C 2 195 ? 100.519 83.911  124.622 1.00 23.39 ?  174 TYR C CG    1 
ATOM   12403 C  CD1   . TYR C 2 195 ? 99.566  83.581  123.645 1.00 22.84 ?  174 TYR C CD1   1 
ATOM   12404 C  CD2   . TYR C 2 195 ? 100.087 84.575  125.767 1.00 22.23 ?  174 TYR C CD2   1 
ATOM   12405 C  CE1   . TYR C 2 195 ? 98.221  83.934  123.803 1.00 24.05 ?  174 TYR C CE1   1 
ATOM   12406 C  CE2   . TYR C 2 195 ? 98.745  84.920  125.942 1.00 24.11 ?  174 TYR C CE2   1 
ATOM   12407 C  CZ    . TYR C 2 195 ? 97.823  84.595  124.962 1.00 23.92 ?  174 TYR C CZ    1 
ATOM   12408 O  OH    . TYR C 2 195 ? 96.516  84.961  125.138 1.00 25.00 ?  174 TYR C OH    1 
ATOM   12409 N  N     . PRO C 2 196 ? 104.094 85.394  122.868 1.00 22.25 ?  175 PRO C N     1 
ATOM   12410 C  CA    . PRO C 2 196 ? 104.555 86.636  122.226 1.00 22.45 ?  175 PRO C CA    1 
ATOM   12411 C  C     . PRO C 2 196 ? 104.636 86.524  120.703 1.00 22.59 ?  175 PRO C C     1 
ATOM   12412 O  O     . PRO C 2 196 ? 104.304 87.490  120.007 1.00 22.19 ?  175 PRO C O     1 
ATOM   12413 C  CB    . PRO C 2 196 ? 105.956 86.863  122.814 1.00 22.25 ?  175 PRO C CB    1 
ATOM   12414 C  CG    . PRO C 2 196 ? 105.991 86.083  124.087 1.00 22.22 ?  175 PRO C CG    1 
ATOM   12415 C  CD    . PRO C 2 196 ? 105.044 84.923  123.902 1.00 22.32 ?  175 PRO C CD    1 
ATOM   12416 N  N     . LEU C 2 197 ? 105.060 85.362  120.195 1.00 21.92 ?  176 LEU C N     1 
ATOM   12417 C  CA    . LEU C 2 197 ? 105.129 85.139  118.749 1.00 22.35 ?  176 LEU C CA    1 
ATOM   12418 C  C     . LEU C 2 197 ? 103.732 85.105  118.122 1.00 22.60 ?  176 LEU C C     1 
ATOM   12419 O  O     . LEU C 2 197 ? 103.517 85.621  117.021 1.00 22.41 ?  176 LEU C O     1 
ATOM   12420 C  CB    . LEU C 2 197 ? 105.864 83.841  118.418 1.00 22.69 ?  176 LEU C CB    1 
ATOM   12421 C  CG    . LEU C 2 197 ? 107.351 83.680  118.765 1.00 23.68 ?  176 LEU C CG    1 
ATOM   12422 C  CD1   . LEU C 2 197 ? 107.823 82.276  118.353 1.00 23.70 ?  176 LEU C CD1   1 
ATOM   12423 C  CD2   . LEU C 2 197 ? 108.194 84.753  118.085 1.00 23.09 ?  176 LEU C CD2   1 
ATOM   12424 N  N     . TYR C 2 198 ? 102.791 84.493  118.836 1.00 22.64 ?  177 TYR C N     1 
ATOM   12425 C  CA    . TYR C 2 198 ? 101.410 84.374  118.388 1.00 22.92 ?  177 TYR C CA    1 
ATOM   12426 C  C     . TYR C 2 198 ? 100.795 85.777  118.226 1.00 23.68 ?  177 TYR C C     1 
ATOM   12427 O  O     . TYR C 2 198 ? 100.122 86.060  117.232 1.00 23.81 ?  177 TYR C O     1 
ATOM   12428 C  CB    . TYR C 2 198 ? 100.647 83.521  119.396 1.00 22.73 ?  177 TYR C CB    1 
ATOM   12429 C  CG    . TYR C 2 198 ? 99.179  83.308  119.148 1.00 22.91 ?  177 TYR C CG    1 
ATOM   12430 C  CD1   . TYR C 2 198 ? 98.742  82.432  118.154 1.00 23.49 ?  177 TYR C CD1   1 
ATOM   12431 C  CD2   . TYR C 2 198 ? 98.225  83.932  119.953 1.00 21.97 ?  177 TYR C CD2   1 
ATOM   12432 C  CE1   . TYR C 2 198 ? 97.382  82.206  117.940 1.00 23.57 ?  177 TYR C CE1   1 
ATOM   12433 C  CE2   . TYR C 2 198 ? 96.852  83.710  119.750 1.00 22.54 ?  177 TYR C CE2   1 
ATOM   12434 C  CZ    . TYR C 2 198 ? 96.444  82.850  118.741 1.00 22.88 ?  177 TYR C CZ    1 
ATOM   12435 O  OH    . TYR C 2 198 ? 95.099  82.608  118.529 1.00 23.17 ?  177 TYR C OH    1 
ATOM   12436 N  N     . PHE C 2 199 ? 101.065 86.663  119.177 1.00 23.50 ?  178 PHE C N     1 
ATOM   12437 C  CA    . PHE C 2 199 ? 100.606 88.048  119.063 1.00 24.60 ?  178 PHE C CA    1 
ATOM   12438 C  C     . PHE C 2 199 ? 101.333 88.866  117.986 1.00 24.72 ?  178 PHE C C     1 
ATOM   12439 O  O     . PHE C 2 199 ? 100.698 89.564  117.197 1.00 24.19 ?  178 PHE C O     1 
ATOM   12440 C  CB    . PHE C 2 199 ? 100.667 88.753  120.420 1.00 24.35 ?  178 PHE C CB    1 
ATOM   12441 C  CG    . PHE C 2 199 ? 99.564  88.350  121.352 1.00 26.36 ?  178 PHE C CG    1 
ATOM   12442 C  CD1   . PHE C 2 199 ? 98.246  88.270  120.902 1.00 28.53 ?  178 PHE C CD1   1 
ATOM   12443 C  CD2   . PHE C 2 199 ? 99.830  88.067  122.684 1.00 28.23 ?  178 PHE C CD2   1 
ATOM   12444 C  CE1   . PHE C 2 199 ? 97.215  87.889  121.767 1.00 29.37 ?  178 PHE C CE1   1 
ATOM   12445 C  CE2   . PHE C 2 199 ? 98.795  87.696  123.560 1.00 28.69 ?  178 PHE C CE2   1 
ATOM   12446 C  CZ    . PHE C 2 199 ? 97.498  87.607  123.100 1.00 28.43 ?  178 PHE C CZ    1 
ATOM   12447 N  N     . TYR C 2 200 ? 102.660 88.766  117.961 1.00 25.36 ?  179 TYR C N     1 
ATOM   12448 C  CA    . TYR C 2 200 ? 103.489 89.442  116.956 1.00 26.02 ?  179 TYR C CA    1 
ATOM   12449 C  C     . TYR C 2 200 ? 102.968 89.137  115.551 1.00 26.57 ?  179 TYR C C     1 
ATOM   12450 O  O     . TYR C 2 200 ? 102.829 90.035  114.714 1.00 26.30 ?  179 TYR C O     1 
ATOM   12451 C  CB    . TYR C 2 200 ? 104.947 88.978  117.079 1.00 26.19 ?  179 TYR C CB    1 
ATOM   12452 C  CG    . TYR C 2 200 ? 105.933 89.763  116.241 1.00 27.82 ?  179 TYR C CG    1 
ATOM   12453 C  CD1   . TYR C 2 200 ? 106.409 89.252  115.030 1.00 30.77 ?  179 TYR C CD1   1 
ATOM   12454 C  CD2   . TYR C 2 200 ? 106.400 91.010  116.662 1.00 29.20 ?  179 TYR C CD2   1 
ATOM   12455 C  CE1   . TYR C 2 200 ? 107.317 89.966  114.257 1.00 31.82 ?  179 TYR C CE1   1 
ATOM   12456 C  CE2   . TYR C 2 200 ? 107.305 91.734  115.900 1.00 30.44 ?  179 TYR C CE2   1 
ATOM   12457 C  CZ    . TYR C 2 200 ? 107.760 91.204  114.697 1.00 32.74 ?  179 TYR C CZ    1 
ATOM   12458 O  OH    . TYR C 2 200 ? 108.650 91.909  113.924 1.00 34.58 ?  179 TYR C OH    1 
ATOM   12459 N  N     . GLY C 2 201 ? 102.657 87.864  115.318 1.00 26.71 ?  180 GLY C N     1 
ATOM   12460 C  CA    . GLY C 2 201 ? 102.156 87.404  114.031 1.00 27.38 ?  180 GLY C CA    1 
ATOM   12461 C  C     . GLY C 2 201 ? 100.798 87.962  113.636 1.00 27.62 ?  180 GLY C C     1 
ATOM   12462 O  O     . GLY C 2 201 ? 100.444 87.916  112.470 1.00 28.25 ?  180 GLY C O     1 
ATOM   12463 N  N     . GLN C 2 202 ? 100.048 88.485  114.605 1.00 27.60 ?  181 GLN C N     1 
ATOM   12464 C  CA    . GLN C 2 202 ? 98.742  89.120  114.352 1.00 28.24 ?  181 GLN C CA    1 
ATOM   12465 C  C     . GLN C 2 202 ? 98.845  90.637  114.361 1.00 28.30 ?  181 GLN C C     1 
ATOM   12466 O  O     . GLN C 2 202 ? 97.821  91.322  114.294 1.00 27.98 ?  181 GLN C O     1 
ATOM   12467 C  CB    . GLN C 2 202 ? 97.728  88.744  115.436 1.00 27.90 ?  181 GLN C CB    1 
ATOM   12468 C  CG    . GLN C 2 202 ? 97.402  87.290  115.555 1.00 29.54 ?  181 GLN C CG    1 
ATOM   12469 C  CD    . GLN C 2 202 ? 96.491  87.021  116.731 1.00 31.54 ?  181 GLN C CD    1 
ATOM   12470 O  OE1   . GLN C 2 202 ? 95.315  87.395  116.722 1.00 32.11 ?  181 GLN C OE1   1 
ATOM   12471 N  NE2   . GLN C 2 202 ? 97.030  86.378  117.759 1.00 31.29 ?  181 GLN C NE2   1 
ATOM   12472 N  N     . GLY C 2 203 ? 100.067 91.151  114.493 1.00 28.14 ?  182 GLY C N     1 
ATOM   12473 C  CA    . GLY C 2 203 ? 100.310 92.584  114.563 1.00 28.38 ?  182 GLY C CA    1 
ATOM   12474 C  C     . GLY C 2 203 ? 99.961  93.179  115.911 1.00 28.71 ?  182 GLY C C     1 
ATOM   12475 O  O     . GLY C 2 203 ? 99.572  94.340  115.991 1.00 28.80 ?  182 GLY C O     1 
ATOM   12476 N  N     . LYS C 2 204 ? 100.088 92.375  116.966 1.00 28.24 ?  183 LYS C N     1 
ATOM   12477 C  CA    . LYS C 2 204 ? 99.771  92.813  118.316 1.00 28.48 ?  183 LYS C CA    1 
ATOM   12478 C  C     . LYS C 2 204 ? 100.994 92.678  119.218 1.00 27.82 ?  183 LYS C C     1 
ATOM   12479 O  O     . LYS C 2 204 ? 101.778 91.729  119.081 1.00 26.73 ?  183 LYS C O     1 
ATOM   12480 C  CB    . LYS C 2 204 ? 98.603  92.009  118.890 1.00 29.13 ?  183 LYS C CB    1 
ATOM   12481 C  CG    . LYS C 2 204 ? 97.276  92.228  118.164 1.00 30.41 ?  183 LYS C CG    1 
ATOM   12482 C  CD    . LYS C 2 204 ? 96.337  91.052  118.382 1.00 33.74 ?  183 LYS C CD    1 
ATOM   12483 C  CE    . LYS C 2 204 ? 94.973  91.304  117.720 1.00 36.26 ?  183 LYS C CE    1 
ATOM   12484 N  NZ    . LYS C 2 204 ? 94.051  90.158  117.968 1.00 39.17 1  183 LYS C NZ    1 
ATOM   12485 N  N     . LEU C 2 205 ? 101.143 93.632  120.135 1.00 27.77 ?  184 LEU C N     1 
ATOM   12486 C  CA    . LEU C 2 205 ? 102.278 93.673  121.067 1.00 27.79 ?  184 LEU C CA    1 
ATOM   12487 C  C     . LEU C 2 205 ? 103.613 93.536  120.330 1.00 27.85 ?  184 LEU C C     1 
ATOM   12488 O  O     . LEU C 2 205 ? 104.472 92.712  120.677 1.00 27.07 ?  184 LEU C O     1 
ATOM   12489 C  CB    . LEU C 2 205 ? 102.124 92.601  122.165 1.00 27.76 ?  184 LEU C CB    1 
ATOM   12490 C  CG    . LEU C 2 205 ? 100.825 92.665  122.980 1.00 28.62 ?  184 LEU C CG    1 
ATOM   12491 C  CD1   . LEU C 2 205 ? 100.726 91.492  123.935 1.00 29.18 ?  184 LEU C CD1   1 
ATOM   12492 C  CD2   . LEU C 2 205 ? 100.717 93.976  123.744 1.00 28.43 ?  184 LEU C CD2   1 
ATOM   12493 N  N     . MET C 2 206 ? 103.794 94.364  119.313 1.00 28.15 ?  185 MET C N     1 
ATOM   12494 C  CA    . MET C 2 206 ? 104.910 94.169  118.415 1.00 28.80 ?  185 MET C CA    1 
ATOM   12495 C  C     . MET C 2 206 ? 106.254 94.651  118.946 1.00 28.77 ?  185 MET C C     1 
ATOM   12496 O  O     . MET C 2 206 ? 107.292 94.152  118.515 1.00 28.79 ?  185 MET C O     1 
ATOM   12497 C  CB    . MET C 2 206 ? 104.585 94.747  117.051 1.00 29.96 ?  185 MET C CB    1 
ATOM   12498 C  CG    . MET C 2 206 ? 103.470 93.951  116.364 1.00 31.23 ?  185 MET C CG    1 
ATOM   12499 S  SD    . MET C 2 206 ? 103.458 94.283  114.623 1.00 40.10 ?  185 MET C SD    1 
ATOM   12500 C  CE    . MET C 2 206 ? 104.915 93.419  114.072 1.00 35.10 ?  185 MET C CE    1 
ATOM   12501 N  N     . GLN C 2 207 ? 106.242 95.585  119.891 1.00 28.62 ?  186 GLN C N     1 
ATOM   12502 C  CA    . GLN C 2 207 ? 107.490 96.060  120.497 1.00 29.10 ?  186 GLN C CA    1 
ATOM   12503 C  C     . GLN C 2 207 ? 108.045 95.024  121.478 1.00 28.52 ?  186 GLN C C     1 
ATOM   12504 O  O     . GLN C 2 207 ? 109.225 94.683  121.406 1.00 28.28 ?  186 GLN C O     1 
ATOM   12505 C  CB    . GLN C 2 207 ? 107.315 97.425  121.171 1.00 29.21 ?  186 GLN C CB    1 
ATOM   12506 C  CG    . GLN C 2 207 ? 106.947 98.555  120.207 1.00 31.41 ?  186 GLN C CG    1 
ATOM   12507 C  CD    . GLN C 2 207 ? 108.044 98.843  119.203 1.00 34.70 ?  186 GLN C CD    1 
ATOM   12508 O  OE1   . GLN C 2 207 ? 108.060 98.282  118.111 1.00 37.69 ?  186 GLN C OE1   1 
ATOM   12509 N  NE2   . GLN C 2 207 ? 108.988 99.698  119.580 1.00 34.75 ?  186 GLN C NE2   1 
ATOM   12510 N  N     . SER C 2 208 ? 107.186 94.531  122.378 1.00 28.38 ?  187 SER C N     1 
ATOM   12511 C  CA    . SER C 2 208 ? 107.506 93.389  123.246 1.00 28.25 ?  187 SER C CA    1 
ATOM   12512 C  C     . SER C 2 208 ? 107.939 92.202  122.394 1.00 28.00 ?  187 SER C C     1 
ATOM   12513 O  O     . SER C 2 208 ? 108.894 91.504  122.735 1.00 27.90 ?  187 SER C O     1 
ATOM   12514 C  CB    . SER C 2 208 ? 106.284 92.967  124.064 1.00 27.88 ?  187 SER C CB    1 
ATOM   12515 O  OG    . SER C 2 208 ? 105.846 93.999  124.922 1.00 30.27 ?  187 SER C OG    1 
ATOM   12516 N  N     . GLY C 2 209 ? 107.214 91.981  121.292 1.00 27.31 ?  188 GLY C N     1 
ATOM   12517 C  CA    . GLY C 2 209 ? 107.508 90.902  120.353 1.00 27.86 ?  188 GLY C CA    1 
ATOM   12518 C  C     . GLY C 2 209 ? 108.874 91.021  119.704 1.00 27.96 ?  188 GLY C C     1 
ATOM   12519 O  O     . GLY C 2 209 ? 109.539 90.009  119.452 1.00 27.84 ?  188 GLY C O     1 
ATOM   12520 N  N     . GLU C 2 210 ? 109.293 92.257  119.430 1.00 28.21 ?  189 GLU C N     1 
ATOM   12521 C  CA    . GLU C 2 210 ? 110.620 92.521  118.883 1.00 29.15 ?  189 GLU C CA    1 
ATOM   12522 C  C     . GLU C 2 210 ? 111.717 92.102  119.881 1.00 28.02 ?  189 GLU C C     1 
ATOM   12523 O  O     . GLU C 2 210 ? 112.718 91.488  119.506 1.00 27.15 ?  189 GLU C O     1 
ATOM   12524 C  CB    . GLU C 2 210 ? 110.752 94.002  118.515 1.00 30.17 ?  189 GLU C CB    1 
ATOM   12525 C  CG    . GLU C 2 210 ? 111.276 94.254  117.111 1.00 35.68 ?  189 GLU C CG    1 
ATOM   12526 C  CD    . GLU C 2 210 ? 110.205 94.070  116.032 1.00 40.25 ?  189 GLU C CD    1 
ATOM   12527 O  OE1   . GLU C 2 210 ? 109.190 94.807  116.028 1.00 42.98 ?  189 GLU C OE1   1 
ATOM   12528 O  OE2   . GLU C 2 210 ? 110.383 93.188  115.170 1.00 43.59 -1 189 GLU C OE2   1 
ATOM   12529 N  N     . ILE C 2 211 ? 111.519 92.437  121.154 1.00 27.57 ?  190 ILE C N     1 
ATOM   12530 C  CA    . ILE C 2 211 ? 112.424 91.995  122.221 1.00 27.47 ?  190 ILE C CA    1 
ATOM   12531 C  C     . ILE C 2 211 ? 112.523 90.467  122.269 1.00 26.69 ?  190 ILE C C     1 
ATOM   12532 O  O     . ILE C 2 211 ? 113.620 89.893  122.265 1.00 26.56 ?  190 ILE C O     1 
ATOM   12533 C  CB    . ILE C 2 211 ? 111.997 92.579  123.600 1.00 27.84 ?  190 ILE C CB    1 
ATOM   12534 C  CG1   . ILE C 2 211 ? 112.282 94.089  123.635 1.00 28.56 ?  190 ILE C CG1   1 
ATOM   12535 C  CG2   . ILE C 2 211 ? 112.706 91.832  124.754 1.00 27.27 ?  190 ILE C CG2   1 
ATOM   12536 C  CD1   . ILE C 2 211 ? 111.953 94.766  124.961 1.00 30.09 ?  190 ILE C CD1   1 
ATOM   12537 N  N     . ILE C 2 212 ? 111.368 89.812  122.273 1.00 26.33 ?  191 ILE C N     1 
ATOM   12538 C  CA    . ILE C 2 212 ? 111.294 88.356  122.330 1.00 25.96 ?  191 ILE C CA    1 
ATOM   12539 C  C     . ILE C 2 212 ? 112.004 87.691  121.142 1.00 25.46 ?  191 ILE C C     1 
ATOM   12540 O  O     . ILE C 2 212 ? 112.694 86.691  121.325 1.00 24.84 ?  191 ILE C O     1 
ATOM   12541 C  CB    . ILE C 2 212 ? 109.820 87.867  122.468 1.00 26.00 ?  191 ILE C CB    1 
ATOM   12542 C  CG1   . ILE C 2 212 ? 109.226 88.319  123.813 1.00 27.16 ?  191 ILE C CG1   1 
ATOM   12543 C  CG2   . ILE C 2 212 ? 109.705 86.356  122.316 1.00 26.87 ?  191 ILE C CG2   1 
ATOM   12544 C  CD1   . ILE C 2 212 ? 109.900 87.736  125.041 1.00 29.84 ?  191 ILE C CD1   1 
ATOM   12545 N  N     . ASN C 2 213 ? 111.839 88.246  119.939 1.00 25.35 ?  192 ASN C N     1 
ATOM   12546 C  CA    . ASN C 2 213 ? 112.532 87.735  118.751 1.00 25.60 ?  192 ASN C CA    1 
ATOM   12547 C  C     . ASN C 2 213 ? 114.049 87.846  118.863 1.00 25.14 ?  192 ASN C C     1 
ATOM   12548 O  O     . ASN C 2 213 ? 114.788 86.962  118.403 1.00 25.61 ?  192 ASN C O     1 
ATOM   12549 C  CB    . ASN C 2 213 ? 112.054 88.439  117.474 1.00 26.55 ?  192 ASN C CB    1 
ATOM   12550 C  CG    . ASN C 2 213 ? 110.832 87.781  116.872 1.00 28.10 ?  192 ASN C CG    1 
ATOM   12551 O  OD1   . ASN C 2 213 ? 110.871 86.618  116.456 1.00 31.67 ?  192 ASN C OD1   1 
ATOM   12552 N  ND2   . ASN C 2 213 ? 109.740 88.522  116.809 1.00 30.36 ?  192 ASN C ND2   1 
ATOM   12553 N  N     . LEU C 2 214 ? 114.514 88.927  119.475 1.00 24.54 ?  193 LEU C N     1 
ATOM   12554 C  CA    . LEU C 2 214 ? 115.949 89.088  119.728 1.00 24.40 ?  193 LEU C CA    1 
ATOM   12555 C  C     . LEU C 2 214 ? 116.451 88.048  120.731 1.00 23.55 ?  193 LEU C C     1 
ATOM   12556 O  O     . LEU C 2 214 ? 117.499 87.434  120.517 1.00 23.09 ?  193 LEU C O     1 
ATOM   12557 C  CB    . LEU C 2 214 ? 116.273 90.514  120.165 1.00 24.00 ?  193 LEU C CB    1 
ATOM   12558 C  CG    . LEU C 2 214 ? 116.175 91.589  119.060 1.00 25.69 ?  193 LEU C CG    1 
ATOM   12559 C  CD1   . LEU C 2 214 ? 116.226 93.002  119.642 1.00 26.28 ?  193 LEU C CD1   1 
ATOM   12560 C  CD2   . LEU C 2 214 ? 117.275 91.427  118.008 1.00 26.05 ?  193 LEU C CD2   1 
ATOM   12561 N  N     . ILE C 2 215 ? 115.694 87.846  121.813 1.00 23.19 ?  194 ILE C N     1 
ATOM   12562 C  CA    . ILE C 2 215 ? 115.990 86.791  122.789 1.00 22.88 ?  194 ILE C CA    1 
ATOM   12563 C  C     . ILE C 2 215 ? 116.023 85.427  122.080 1.00 23.81 ?  194 ILE C C     1 
ATOM   12564 O  O     . ILE C 2 215 ? 116.968 84.656  122.257 1.00 23.83 ?  194 ILE C O     1 
ATOM   12565 C  CB    . ILE C 2 215 ? 114.970 86.777  123.963 1.00 22.92 ?  194 ILE C CB    1 
ATOM   12566 C  CG1   . ILE C 2 215 ? 115.008 88.103  124.725 1.00 21.11 ?  194 ILE C CG1   1 
ATOM   12567 C  CG2   . ILE C 2 215 ? 115.218 85.596  124.915 1.00 21.89 ?  194 ILE C CG2   1 
ATOM   12568 C  CD1   . ILE C 2 215 ? 114.025 88.188  125.875 1.00 22.26 ?  194 ILE C CD1   1 
ATOM   12569 N  N     . LEU C 2 216 ? 115.020 85.148  121.247 1.00 24.23 ?  195 LEU C N     1 
ATOM   12570 C  CA    . LEU C 2 216 ? 114.933 83.853  120.563 1.00 25.41 ?  195 LEU C CA    1 
ATOM   12571 C  C     . LEU C 2 216 ? 116.105 83.632  119.605 1.00 25.63 ?  195 LEU C C     1 
ATOM   12572 O  O     . LEU C 2 216 ? 116.675 82.531  119.550 1.00 25.46 ?  195 LEU C O     1 
ATOM   12573 C  CB    . LEU C 2 216 ? 113.587 83.711  119.828 1.00 26.03 ?  195 LEU C CB    1 
ATOM   12574 C  CG    . LEU C 2 216 ? 113.237 82.417  119.079 1.00 28.00 ?  195 LEU C CG    1 
ATOM   12575 C  CD1   . LEU C 2 216 ? 111.728 82.335  118.918 1.00 31.45 ?  195 LEU C CD1   1 
ATOM   12576 C  CD2   . LEU C 2 216 ? 113.930 82.324  117.714 1.00 29.83 ?  195 LEU C CD2   1 
ATOM   12577 N  N     . ARG C 2 217 ? 116.462 84.676  118.864 1.00 25.98 ?  196 ARG C N     1 
ATOM   12578 C  CA    . ARG C 2 217 ? 117.623 84.647  117.980 1.00 26.73 ?  196 ARG C CA    1 
ATOM   12579 C  C     . ARG C 2 217 ? 118.903 84.260  118.762 1.00 25.95 ?  196 ARG C C     1 
ATOM   12580 O  O     . ARG C 2 217 ? 119.683 83.429  118.284 1.00 25.75 ?  196 ARG C O     1 
ATOM   12581 C  CB    . ARG C 2 217 ? 117.789 86.003  117.289 1.00 27.29 ?  196 ARG C CB    1 
ATOM   12582 C  CG    . ARG C 2 217 ? 118.796 86.038  116.131 1.00 30.12 ?  196 ARG C CG    1 
ATOM   12583 C  CD    . ARG C 2 217 ? 119.420 87.418  116.043 1.00 35.40 ?  196 ARG C CD    1 
ATOM   12584 N  NE    . ARG C 2 217 ? 119.783 87.852  117.393 1.00 39.87 ?  196 ARG C NE    1 
ATOM   12585 C  CZ    . ARG C 2 217 ? 120.140 89.079  117.749 1.00 40.55 ?  196 ARG C CZ    1 
ATOM   12586 N  NH1   . ARG C 2 217 ? 120.210 90.063  116.854 1.00 40.77 1  196 ARG C NH1   1 
ATOM   12587 N  NH2   . ARG C 2 217 ? 120.426 89.312  119.024 1.00 41.10 ?  196 ARG C NH2   1 
ATOM   12588 N  N     . ASP C 2 218 ? 119.096 84.847  119.949 1.00 24.70 ?  197 ASP C N     1 
ATOM   12589 C  CA    . ASP C 2 218 ? 120.213 84.483  120.844 1.00 24.55 ?  197 ASP C CA    1 
ATOM   12590 C  C     . ASP C 2 218 ? 120.134 83.010  121.295 1.00 24.23 ?  197 ASP C C     1 
ATOM   12591 O  O     . ASP C 2 218 ? 121.118 82.275  121.172 1.00 23.69 ?  197 ASP C O     1 
ATOM   12592 C  CB    . ASP C 2 218 ? 120.290 85.384  122.094 1.00 24.50 ?  197 ASP C CB    1 
ATOM   12593 C  CG    . ASP C 2 218 ? 120.652 86.848  121.782 1.00 25.84 ?  197 ASP C CG    1 
ATOM   12594 O  OD1   . ASP C 2 218 ? 121.281 87.143  120.742 1.00 26.91 ?  197 ASP C OD1   1 
ATOM   12595 O  OD2   . ASP C 2 218 ? 120.317 87.715  122.613 1.00 25.72 -1 197 ASP C OD2   1 
ATOM   12596 N  N     . GLU C 2 219 ? 118.971 82.574  121.787 1.00 23.92 ?  198 GLU C N     1 
ATOM   12597 C  CA    . GLU C 2 219 ? 118.871 81.210  122.334 1.00 24.20 ?  198 GLU C CA    1 
ATOM   12598 C  C     . GLU C 2 219 ? 119.135 80.160  121.271 1.00 24.02 ?  198 GLU C C     1 
ATOM   12599 O  O     . GLU C 2 219 ? 119.716 79.124  121.577 1.00 24.24 ?  198 GLU C O     1 
ATOM   12600 C  CB    . GLU C 2 219 ? 117.530 80.919  123.013 1.00 24.05 ?  198 GLU C CB    1 
ATOM   12601 C  CG    . GLU C 2 219 ? 116.922 82.035  123.844 1.00 25.03 ?  198 GLU C CG    1 
ATOM   12602 C  CD    . GLU C 2 219 ? 117.627 82.355  125.176 1.00 26.31 ?  198 GLU C CD    1 
ATOM   12603 O  OE1   . GLU C 2 219 ? 118.850 82.088  125.368 1.00 27.65 ?  198 GLU C OE1   1 
ATOM   12604 O  OE2   . GLU C 2 219 ? 116.917 82.930  126.047 1.00 26.87 -1 198 GLU C OE2   1 
ATOM   12605 N  N     . ALA C 2 220 ? 118.709 80.422  120.034 1.00 24.00 ?  199 ALA C N     1 
ATOM   12606 C  CA    . ALA C 2 220 ? 118.956 79.495  118.934 1.00 24.72 ?  199 ALA C CA    1 
ATOM   12607 C  C     . ALA C 2 220 ? 120.457 79.219  118.740 1.00 24.80 ?  199 ALA C C     1 
ATOM   12608 O  O     . ALA C 2 220 ? 120.860 78.062  118.595 1.00 25.04 ?  199 ALA C O     1 
ATOM   12609 C  CB    . ALA C 2 220 ? 118.309 79.996  117.619 1.00 24.66 ?  199 ALA C CB    1 
ATOM   12610 N  N     . ILE C 2 221 ? 121.273 80.271  118.749 1.00 24.85 ?  200 ILE C N     1 
ATOM   12611 C  CA    . ILE C 2 221 ? 122.731 80.099  118.621 1.00 25.07 ?  200 ILE C CA    1 
ATOM   12612 C  C     . ILE C 2 221 ? 123.368 79.531  119.898 1.00 23.86 ?  200 ILE C C     1 
ATOM   12613 O  O     . ILE C 2 221 ? 124.338 78.772  119.813 1.00 23.72 ?  200 ILE C O     1 
ATOM   12614 C  CB    . ILE C 2 221 ? 123.485 81.384  118.121 1.00 25.71 ?  200 ILE C CB    1 
ATOM   12615 C  CG1   . ILE C 2 221 ? 123.566 82.457  119.212 1.00 27.10 ?  200 ILE C CG1   1 
ATOM   12616 C  CG2   . ILE C 2 221 ? 122.860 81.912  116.814 1.00 27.18 ?  200 ILE C CG2   1 
ATOM   12617 C  CD1   . ILE C 2 221 ? 124.450 83.663  118.872 1.00 29.63 ?  200 ILE C CD1   1 
ATOM   12618 N  N     . HIS C 2 222 ? 122.818 79.879  121.061 1.00 22.79 ?  201 HIS C N     1 
ATOM   12619 C  CA    . HIS C 2 222 ? 123.277 79.293  122.341 1.00 22.48 ?  201 HIS C CA    1 
ATOM   12620 C  C     . HIS C 2 222 ? 123.058 77.782  122.371 1.00 22.04 ?  201 HIS C C     1 
ATOM   12621 O  O     . HIS C 2 222 ? 123.929 77.045  122.817 1.00 22.06 ?  201 HIS C O     1 
ATOM   12622 C  CB    . HIS C 2 222 ? 122.534 79.878  123.543 1.00 21.77 ?  201 HIS C CB    1 
ATOM   12623 C  CG    . HIS C 2 222 ? 122.793 81.326  123.793 1.00 21.76 ?  201 HIS C CG    1 
ATOM   12624 N  ND1   . HIS C 2 222 ? 122.288 81.983  124.892 1.00 20.70 ?  201 HIS C ND1   1 
ATOM   12625 C  CD2   . HIS C 2 222 ? 123.502 82.246  123.098 1.00 22.07 ?  201 HIS C CD2   1 
ATOM   12626 C  CE1   . HIS C 2 222 ? 122.664 83.247  124.861 1.00 22.26 ?  201 HIS C CE1   1 
ATOM   12627 N  NE2   . HIS C 2 222 ? 123.395 83.435  123.779 1.00 22.52 ?  201 HIS C NE2   1 
ATOM   12628 N  N     . GLY C 2 223 ? 121.879 77.339  121.933 1.00 22.35 ?  202 GLY C N     1 
ATOM   12629 C  CA    . GLY C 2 223 ? 121.542 75.908  121.860 1.00 22.01 ?  202 GLY C CA    1 
ATOM   12630 C  C     . GLY C 2 223 ? 122.419 75.127  120.885 1.00 22.73 ?  202 GLY C C     1 
ATOM   12631 O  O     . GLY C 2 223 ? 122.829 73.990  121.173 1.00 21.99 ?  202 GLY C O     1 
ATOM   12632 N  N     . VAL C 2 224 ? 122.720 75.732  119.733 1.00 22.45 ?  203 VAL C N     1 
ATOM   12633 C  CA    . VAL C 2 224 ? 123.622 75.104  118.765 1.00 22.54 ?  203 VAL C CA    1 
ATOM   12634 C  C     . VAL C 2 224 ? 125.028 74.960  119.350 1.00 22.28 ?  203 VAL C C     1 
ATOM   12635 O  O     . VAL C 2 224 ? 125.606 73.876  119.319 1.00 22.44 ?  203 VAL C O     1 
ATOM   12636 C  CB    . VAL C 2 224 ? 123.676 75.872  117.401 1.00 23.00 ?  203 VAL C CB    1 
ATOM   12637 C  CG1   . VAL C 2 224 ? 124.792 75.305  116.504 1.00 23.10 ?  203 VAL C CG1   1 
ATOM   12638 C  CG2   . VAL C 2 224 ? 122.312 75.796  116.663 1.00 23.14 ?  203 VAL C CG2   1 
ATOM   12639 N  N     . TYR C 2 225 ? 125.555 76.047  119.911 1.00 22.41 ?  204 TYR C N     1 
ATOM   12640 C  CA    . TYR C 2 225 ? 126.907 76.048  120.467 1.00 22.03 ?  204 TYR C CA    1 
ATOM   12641 C  C     . TYR C 2 225 ? 127.091 75.016  121.579 1.00 21.66 ?  204 TYR C C     1 
ATOM   12642 O  O     . TYR C 2 225 ? 128.007 74.183  121.512 1.00 21.72 ?  204 TYR C O     1 
ATOM   12643 C  CB    . TYR C 2 225 ? 127.318 77.446  120.956 1.00 22.22 ?  204 TYR C CB    1 
ATOM   12644 C  CG    . TYR C 2 225 ? 128.785 77.525  121.329 1.00 21.92 ?  204 TYR C CG    1 
ATOM   12645 C  CD1   . TYR C 2 225 ? 129.776 77.432  120.351 1.00 22.36 ?  204 TYR C CD1   1 
ATOM   12646 C  CD2   . TYR C 2 225 ? 129.177 77.682  122.659 1.00 21.43 ?  204 TYR C CD2   1 
ATOM   12647 C  CE1   . TYR C 2 225 ? 131.127 77.487  120.690 1.00 23.82 ?  204 TYR C CE1   1 
ATOM   12648 C  CE2   . TYR C 2 225 ? 130.529 77.748  123.014 1.00 21.49 ?  204 TYR C CE2   1 
ATOM   12649 C  CZ    . TYR C 2 225 ? 131.490 77.650  122.027 1.00 23.58 ?  204 TYR C CZ    1 
ATOM   12650 O  OH    . TYR C 2 225 ? 132.814 77.714  122.372 1.00 25.42 ?  204 TYR C OH    1 
ATOM   12651 N  N     . VAL C 2 226 ? 126.224 75.060  122.593 1.00 20.95 ?  205 VAL C N     1 
ATOM   12652 C  CA    . VAL C 2 226 ? 126.285 74.079  123.684 1.00 20.49 ?  205 VAL C CA    1 
ATOM   12653 C  C     . VAL C 2 226 ? 126.083 72.649  123.149 1.00 20.84 ?  205 VAL C C     1 
ATOM   12654 O  O     . VAL C 2 226 ? 126.769 71.712  123.578 1.00 21.10 ?  205 VAL C O     1 
ATOM   12655 C  CB    . VAL C 2 226 ? 125.317 74.425  124.849 1.00 20.57 ?  205 VAL C CB    1 
ATOM   12656 C  CG1   . VAL C 2 226 ? 125.382 73.354  125.939 1.00 20.35 ?  205 VAL C CG1   1 
ATOM   12657 C  CG2   . VAL C 2 226 ? 125.681 75.796  125.437 1.00 19.60 ?  205 VAL C CG2   1 
ATOM   12658 N  N     . GLY C 2 227 ? 125.186 72.497  122.180 1.00 21.08 ?  206 GLY C N     1 
ATOM   12659 C  CA    . GLY C 2 227 ? 125.017 71.211  121.485 1.00 21.43 ?  206 GLY C CA    1 
ATOM   12660 C  C     . GLY C 2 227 ? 126.302 70.662  120.880 1.00 21.95 ?  206 GLY C C     1 
ATOM   12661 O  O     . GLY C 2 227 ? 126.600 69.461  121.003 1.00 21.84 ?  206 GLY C O     1 
ATOM   12662 N  N     . LEU C 2 228 ? 127.075 71.532  120.229 1.00 22.09 ?  207 LEU C N     1 
ATOM   12663 C  CA    . LEU C 2 228 ? 128.353 71.113  119.646 1.00 22.96 ?  207 LEU C CA    1 
ATOM   12664 C  C     . LEU C 2 228 ? 129.365 70.673  120.714 1.00 22.60 ?  207 LEU C C     1 
ATOM   12665 O  O     . LEU C 2 228 ? 130.090 69.691  120.522 1.00 22.04 ?  207 LEU C O     1 
ATOM   12666 C  CB    . LEU C 2 228 ? 128.936 72.197  118.729 1.00 23.39 ?  207 LEU C CB    1 
ATOM   12667 C  CG    . LEU C 2 228 ? 128.169 72.527  117.436 1.00 24.35 ?  207 LEU C CG    1 
ATOM   12668 C  CD1   . LEU C 2 228 ? 128.633 73.882  116.883 1.00 25.01 ?  207 LEU C CD1   1 
ATOM   12669 C  CD2   . LEU C 2 228 ? 128.322 71.442  116.376 1.00 25.11 ?  207 LEU C CD2   1 
ATOM   12670 N  N     . LEU C 2 229 ? 129.396 71.374  121.845 1.00 22.37 ?  208 LEU C N     1 
ATOM   12671 C  CA    . LEU C 2 229 ? 130.263 70.969  122.968 1.00 22.62 ?  208 LEU C CA    1 
ATOM   12672 C  C     . LEU C 2 229 ? 129.857 69.616  123.563 1.00 22.77 ?  208 LEU C C     1 
ATOM   12673 O  O     . LEU C 2 229 ? 130.719 68.778  123.880 1.00 22.57 ?  208 LEU C O     1 
ATOM   12674 C  CB    . LEU C 2 229 ? 130.317 72.053  124.049 1.00 22.44 ?  208 LEU C CB    1 
ATOM   12675 C  CG    . LEU C 2 229 ? 130.796 73.438  123.589 1.00 23.54 ?  208 LEU C CG    1 
ATOM   12676 C  CD1   . LEU C 2 229 ? 130.707 74.444  124.734 1.00 23.37 ?  208 LEU C CD1   1 
ATOM   12677 C  CD2   . LEU C 2 229 ? 132.224 73.385  123.017 1.00 23.91 ?  208 LEU C CD2   1 
ATOM   12678 N  N     . ALA C 2 230 ? 128.548 69.402  123.701 1.00 22.42 ?  209 ALA C N     1 
ATOM   12679 C  CA    . ALA C 2 230 ? 128.020 68.122  124.171 1.00 22.02 ?  209 ALA C CA    1 
ATOM   12680 C  C     . ALA C 2 230 ? 128.411 66.977  123.232 1.00 22.58 ?  209 ALA C C     1 
ATOM   12681 O  O     . ALA C 2 230 ? 128.851 65.928  123.685 1.00 22.14 ?  209 ALA C O     1 
ATOM   12682 C  CB    . ALA C 2 230 ? 126.518 68.191  124.320 1.00 22.04 ?  209 ALA C CB    1 
ATOM   12683 N  N     . GLN C 2 231 ? 128.264 67.199  121.927 1.00 22.96 ?  210 GLN C N     1 
ATOM   12684 C  CA    . GLN C 2 231 ? 128.662 66.194  120.924 1.00 24.30 ?  210 GLN C CA    1 
ATOM   12685 C  C     . GLN C 2 231 ? 130.136 65.837  120.987 1.00 25.11 ?  210 GLN C C     1 
ATOM   12686 O  O     . GLN C 2 231 ? 130.505 64.681  120.756 1.00 24.97 ?  210 GLN C O     1 
ATOM   12687 C  CB    . GLN C 2 231 ? 128.303 66.662  119.517 1.00 24.38 ?  210 GLN C CB    1 
ATOM   12688 C  CG    . GLN C 2 231 ? 126.787 66.714  119.270 1.00 25.12 ?  210 GLN C CG    1 
ATOM   12689 C  CD    . GLN C 2 231 ? 126.448 67.177  117.870 1.00 28.08 ?  210 GLN C CD    1 
ATOM   12690 O  OE1   . GLN C 2 231 ? 126.916 66.601  116.887 1.00 27.83 ?  210 GLN C OE1   1 
ATOM   12691 N  NE2   . GLN C 2 231 ? 125.642 68.236  117.768 1.00 26.38 ?  210 GLN C NE2   1 
ATOM   12692 N  N     . GLU C 2 232 ? 130.980 66.825  121.296 1.00 25.80 ?  211 GLU C N     1 
ATOM   12693 C  CA    . GLU C 2 232 ? 132.411 66.572  121.485 1.00 27.16 ?  211 GLU C CA    1 
ATOM   12694 C  C     . GLU C 2 232 ? 132.647 65.511  122.555 1.00 26.47 ?  211 GLU C C     1 
ATOM   12695 O  O     . GLU C 2 232 ? 133.457 64.595  122.370 1.00 26.10 ?  211 GLU C O     1 
ATOM   12696 C  CB    . GLU C 2 232 ? 133.139 67.840  121.912 1.00 27.59 ?  211 GLU C CB    1 
ATOM   12697 C  CG    . GLU C 2 232 ? 133.680 68.666  120.786 1.00 32.55 ?  211 GLU C CG    1 
ATOM   12698 C  CD    . GLU C 2 232 ? 134.964 69.390  121.170 1.00 36.72 ?  211 GLU C CD    1 
ATOM   12699 O  OE1   . GLU C 2 232 ? 135.379 69.319  122.352 1.00 38.32 ?  211 GLU C OE1   1 
ATOM   12700 O  OE2   . GLU C 2 232 ? 135.562 70.028  120.280 1.00 40.62 -1 211 GLU C OE2   1 
ATOM   12701 N  N     . ILE C 2 233 ? 131.949 65.652  123.681 1.00 25.55 ?  212 ILE C N     1 
ATOM   12702 C  CA    . ILE C 2 233 ? 132.108 64.725  124.801 1.00 25.32 ?  212 ILE C CA    1 
ATOM   12703 C  C     . ILE C 2 233 ? 131.528 63.355  124.473 1.00 25.48 ?  212 ILE C C     1 
ATOM   12704 O  O     . ILE C 2 233 ? 132.184 62.331  124.681 1.00 25.82 ?  212 ILE C O     1 
ATOM   12705 C  CB    . ILE C 2 233 ? 131.494 65.281  126.105 1.00 25.39 ?  212 ILE C CB    1 
ATOM   12706 C  CG1   . ILE C 2 233 ? 132.294 66.500  126.570 1.00 24.37 ?  212 ILE C CG1   1 
ATOM   12707 C  CG2   . ILE C 2 233 ? 131.453 64.195  127.186 1.00 24.86 ?  212 ILE C CG2   1 
ATOM   12708 C  CD1   . ILE C 2 233 ? 131.560 67.361  127.585 1.00 25.10 ?  212 ILE C CD1   1 
ATOM   12709 N  N     . TYR C 2 234 ? 130.311 63.344  123.935 1.00 25.27 ?  213 TYR C N     1 
ATOM   12710 C  CA    . TYR C 2 234 ? 129.658 62.117  123.473 1.00 25.77 ?  213 TYR C CA    1 
ATOM   12711 C  C     . TYR C 2 234 ? 130.541 61.320  122.497 1.00 26.44 ?  213 TYR C C     1 
ATOM   12712 O  O     . TYR C 2 234 ? 130.634 60.093  122.587 1.00 26.29 ?  213 TYR C O     1 
ATOM   12713 C  CB    . TYR C 2 234 ? 128.316 62.478  122.817 1.00 25.67 ?  213 TYR C CB    1 
ATOM   12714 C  CG    . TYR C 2 234 ? 127.517 61.339  122.218 1.00 25.65 ?  213 TYR C CG    1 
ATOM   12715 C  CD1   . TYR C 2 234 ? 126.547 60.672  122.972 1.00 25.02 ?  213 TYR C CD1   1 
ATOM   12716 C  CD2   . TYR C 2 234 ? 127.691 60.964  120.876 1.00 26.59 ?  213 TYR C CD2   1 
ATOM   12717 C  CE1   . TYR C 2 234 ? 125.792 59.643  122.419 1.00 26.52 ?  213 TYR C CE1   1 
ATOM   12718 C  CE2   . TYR C 2 234 ? 126.943 59.929  120.313 1.00 27.00 ?  213 TYR C CE2   1 
ATOM   12719 C  CZ    . TYR C 2 234 ? 125.999 59.275  121.095 1.00 27.79 ?  213 TYR C CZ    1 
ATOM   12720 O  OH    . TYR C 2 234 ? 125.250 58.271  120.548 1.00 29.00 ?  213 TYR C OH    1 
ATOM   12721 N  N     . ASN C 2 235 ? 131.187 62.015  121.563 1.00 26.96 ?  214 ASN C N     1 
ATOM   12722 C  CA    . ASN C 2 235 ? 131.993 61.339  120.548 1.00 28.05 ?  214 ASN C CA    1 
ATOM   12723 C  C     . ASN C 2 235 ? 133.262 60.677  121.074 1.00 28.24 ?  214 ASN C C     1 
ATOM   12724 O  O     . ASN C 2 235 ? 133.854 59.853  120.384 1.00 28.63 ?  214 ASN C O     1 
ATOM   12725 C  CB    . ASN C 2 235 ? 132.291 62.265  119.359 1.00 28.38 ?  214 ASN C CB    1 
ATOM   12726 C  CG    . ASN C 2 235 ? 131.039 62.605  118.558 1.00 31.14 ?  214 ASN C CG    1 
ATOM   12727 O  OD1   . ASN C 2 235 ? 130.111 61.798  118.453 1.00 34.16 ?  214 ASN C OD1   1 
ATOM   12728 N  ND2   . ASN C 2 235 ? 131.007 63.807  117.994 1.00 32.42 ?  214 ASN C ND2   1 
ATOM   12729 N  N     . LYS C 2 236 ? 133.662 61.019  122.298 1.00 27.91 ?  215 LYS C N     1 
ATOM   12730 C  CA    . LYS C 2 236 ? 134.813 60.395  122.955 1.00 28.49 ?  215 LYS C CA    1 
ATOM   12731 C  C     . LYS C 2 236 ? 134.493 59.032  123.580 1.00 28.50 ?  215 LYS C C     1 
ATOM   12732 O  O     . LYS C 2 236 ? 135.401 58.284  123.952 1.00 28.98 ?  215 LYS C O     1 
ATOM   12733 C  CB    . LYS C 2 236 ? 135.387 61.320  124.033 1.00 28.10 ?  215 LYS C CB    1 
ATOM   12734 C  CG    . LYS C 2 236 ? 135.965 62.623  123.499 1.00 29.25 ?  215 LYS C CG    1 
ATOM   12735 C  CD    . LYS C 2 236 ? 136.535 63.479  124.618 1.00 30.19 ?  215 LYS C CD    1 
ATOM   12736 C  CE    . LYS C 2 236 ? 136.811 64.875  124.111 1.00 32.63 ?  215 LYS C CE    1 
ATOM   12737 N  NZ    . LYS C 2 236 ? 137.361 65.741  125.179 1.00 35.39 1  215 LYS C NZ    1 
ATOM   12738 N  N     . GLN C 2 237 ? 133.211 58.698  123.680 1.00 28.25 ?  216 GLN C N     1 
ATOM   12739 C  CA    . GLN C 2 237 ? 132.803 57.520  124.447 1.00 28.34 ?  216 GLN C CA    1 
ATOM   12740 C  C     . GLN C 2 237 ? 132.824 56.209  123.642 1.00 28.92 ?  216 GLN C C     1 
ATOM   12741 O  O     . GLN C 2 237 ? 132.795 56.225  122.411 1.00 28.53 ?  216 GLN C O     1 
ATOM   12742 C  CB    . GLN C 2 237 ? 131.425 57.762  125.080 1.00 27.68 ?  216 GLN C CB    1 
ATOM   12743 C  CG    . GLN C 2 237 ? 131.307 59.092  125.862 1.00 26.67 ?  216 GLN C CG    1 
ATOM   12744 C  CD    . GLN C 2 237 ? 132.422 59.311  126.880 1.00 25.32 ?  216 GLN C CD    1 
ATOM   12745 O  OE1   . GLN C 2 237 ? 132.792 58.401  127.626 1.00 25.49 ?  216 GLN C OE1   1 
ATOM   12746 N  NE2   . GLN C 2 237 ? 132.962 60.527  126.916 1.00 23.63 ?  216 GLN C NE2   1 
ATOM   12747 N  N     . THR C 2 238 ? 132.870 55.081  124.351 1.00 29.53 ?  217 THR C N     1 
ATOM   12748 C  CA    . THR C 2 238 ? 132.640 53.770  123.736 1.00 30.73 ?  217 THR C CA    1 
ATOM   12749 C  C     . THR C 2 238 ? 131.194 53.701  123.229 1.00 31.13 ?  217 THR C C     1 
ATOM   12750 O  O     . THR C 2 238 ? 130.343 54.515  123.631 1.00 30.17 ?  217 THR C O     1 
ATOM   12751 C  CB    . THR C 2 238 ? 132.825 52.618  124.739 1.00 30.79 ?  217 THR C CB    1 
ATOM   12752 O  OG1   . THR C 2 238 ? 131.775 52.667  125.714 1.00 31.16 ?  217 THR C OG1   1 
ATOM   12753 C  CG2   . THR C 2 238 ? 134.187 52.695  125.439 1.00 31.22 ?  217 THR C CG2   1 
ATOM   12754 N  N     . GLU C 2 239 ? 130.910 52.717  122.372 1.00 31.67 ?  218 GLU C N     1 
ATOM   12755 C  CA    . GLU C 2 239 ? 129.547 52.523  121.876 1.00 32.25 ?  218 GLU C CA    1 
ATOM   12756 C  C     . GLU C 2 239 ? 128.562 52.216  123.010 1.00 31.86 ?  218 GLU C C     1 
ATOM   12757 O  O     . GLU C 2 239 ? 127.427 52.702  123.007 1.00 31.09 ?  218 GLU C O     1 
ATOM   12758 C  CB    . GLU C 2 239 ? 129.505 51.447  120.777 1.00 33.29 ?  218 GLU C CB    1 
ATOM   12759 C  CG    . GLU C 2 239 ? 130.202 51.878  119.473 1.00 35.65 ?  218 GLU C CG    1 
ATOM   12760 C  CD    . GLU C 2 239 ? 129.594 53.146  118.860 1.00 39.17 ?  218 GLU C CD    1 
ATOM   12761 O  OE1   . GLU C 2 239 ? 128.343 53.236  118.768 1.00 41.08 ?  218 GLU C OE1   1 
ATOM   12762 O  OE2   . GLU C 2 239 ? 130.365 54.058  118.474 1.00 39.64 -1 218 GLU C OE2   1 
ATOM   12763 N  N     . GLU C 2 240 ? 129.023 51.442  123.993 1.00 31.72 ?  219 GLU C N     1 
ATOM   12764 C  CA    . GLU C 2 240 ? 128.227 51.097  125.163 1.00 31.76 ?  219 GLU C CA    1 
ATOM   12765 C  C     . GLU C 2 240 ? 127.872 52.344  125.986 1.00 30.21 ?  219 GLU C C     1 
ATOM   12766 O  O     . GLU C 2 240 ? 126.716 52.524  126.396 1.00 29.63 ?  219 GLU C O     1 
ATOM   12767 C  CB    . GLU C 2 240 ? 128.979 50.067  126.010 1.00 32.58 ?  219 GLU C CB    1 
ATOM   12768 C  CG    . GLU C 2 240 ? 128.165 49.446  127.134 1.00 36.93 ?  219 GLU C CG    1 
ATOM   12769 C  CD    . GLU C 2 240 ? 128.810 48.180  127.687 1.00 42.06 ?  219 GLU C CD    1 
ATOM   12770 O  OE1   . GLU C 2 240 ? 129.241 48.189  128.862 1.00 44.09 ?  219 GLU C OE1   1 
ATOM   12771 O  OE2   . GLU C 2 240 ? 128.894 47.175  126.943 1.00 44.45 -1 219 GLU C OE2   1 
ATOM   12772 N  N     . LYS C 2 241 ? 128.868 53.201  126.207 1.00 28.91 ?  220 LYS C N     1 
ATOM   12773 C  CA    . LYS C 2 241 ? 128.675 54.446  126.937 1.00 28.14 ?  220 LYS C CA    1 
ATOM   12774 C  C     . LYS C 2 241 ? 127.740 55.408  126.200 1.00 27.03 ?  220 LYS C C     1 
ATOM   12775 O  O     . LYS C 2 241 ? 126.884 56.043  126.824 1.00 26.72 ?  220 LYS C O     1 
ATOM   12776 C  CB    . LYS C 2 241 ? 130.016 55.125  127.232 1.00 27.83 ?  220 LYS C CB    1 
ATOM   12777 C  CG    . LYS C 2 241 ? 129.891 56.384  128.102 1.00 29.68 ?  220 LYS C CG    1 
ATOM   12778 C  CD    . LYS C 2 241 ? 130.176 56.102  129.570 1.00 33.58 ?  220 LYS C CD    1 
ATOM   12779 C  CE    . LYS C 2 241 ? 128.972 55.559  130.288 1.00 33.71 ?  220 LYS C CE    1 
ATOM   12780 N  NZ    . LYS C 2 241 ? 129.289 55.127  131.688 1.00 34.69 1  220 LYS C NZ    1 
ATOM   12781 N  N     . LYS C 2 242 ? 127.921 55.510  124.882 1.00 26.38 ?  221 LYS C N     1 
ATOM   12782 C  CA    . LYS C 2 242 ? 127.047 56.303  124.012 1.00 25.87 ?  221 LYS C CA    1 
ATOM   12783 C  C     . LYS C 2 242 ? 125.594 55.883  124.128 1.00 25.72 ?  221 LYS C C     1 
ATOM   12784 O  O     . LYS C 2 242 ? 124.703 56.738  124.220 1.00 24.52 ?  221 LYS C O     1 
ATOM   12785 C  CB    . LYS C 2 242 ? 127.480 56.202  122.548 1.00 25.83 ?  221 LYS C CB    1 
ATOM   12786 C  CG    . LYS C 2 242 ? 128.707 57.009  122.187 1.00 26.76 ?  221 LYS C CG    1 
ATOM   12787 C  CD    . LYS C 2 242 ? 128.951 56.933  120.684 1.00 28.40 ?  221 LYS C CD    1 
ATOM   12788 C  CE    . LYS C 2 242 ? 130.279 57.525  120.305 1.00 29.84 ?  221 LYS C CE    1 
ATOM   12789 N  NZ    . LYS C 2 242 ? 130.591 57.242  118.884 1.00 30.96 1  221 LYS C NZ    1 
ATOM   12790 N  N     . ALA C 2 243 ? 125.365 54.566  124.112 1.00 25.97 ?  222 ALA C N     1 
ATOM   12791 C  CA    . ALA C 2 243 ? 124.019 54.010  124.283 1.00 25.79 ?  222 ALA C CA    1 
ATOM   12792 C  C     . ALA C 2 243 ? 123.388 54.457  125.603 1.00 25.24 ?  222 ALA C C     1 
ATOM   12793 O  O     . ALA C 2 243 ? 122.198 54.802  125.638 1.00 25.37 ?  222 ALA C O     1 
ATOM   12794 C  CB    . ALA C 2 243 ? 124.043 52.486  124.166 1.00 26.17 ?  222 ALA C CB    1 
ATOM   12795 N  N     . GLU C 2 244 ? 124.177 54.482  126.675 1.00 25.02 ?  223 GLU C N     1 
ATOM   12796 C  CA    . GLU C 2 244 ? 123.695 54.981  127.972 1.00 25.08 ?  223 GLU C CA    1 
ATOM   12797 C  C     . GLU C 2 244 ? 123.402 56.492  127.950 1.00 24.70 ?  223 GLU C C     1 
ATOM   12798 O  O     . GLU C 2 244 ? 122.419 56.956  128.546 1.00 24.20 ?  223 GLU C O     1 
ATOM   12799 C  CB    . GLU C 2 244 ? 124.680 54.646  129.097 1.00 25.35 ?  223 GLU C CB    1 
ATOM   12800 C  CG    . GLU C 2 244 ? 124.190 55.096  130.484 1.00 26.67 ?  223 GLU C CG    1 
ATOM   12801 C  CD    . GLU C 2 244 ? 125.269 55.030  131.550 1.00 28.29 ?  223 GLU C CD    1 
ATOM   12802 O  OE1   . GLU C 2 244 ? 126.234 54.257  131.394 1.00 29.51 ?  223 GLU C OE1   1 
ATOM   12803 O  OE2   . GLU C 2 244 ? 125.150 55.760  132.551 1.00 29.09 -1 223 GLU C OE2   1 
ATOM   12804 N  N     . LEU C 2 245 ? 124.258 57.253  127.274 1.00 24.27 ?  224 LEU C N     1 
ATOM   12805 C  CA    . LEU C 2 245 ? 124.067 58.701  127.173 1.00 24.54 ?  224 LEU C CA    1 
ATOM   12806 C  C     . LEU C 2 245 ? 122.806 59.081  126.385 1.00 24.42 ?  224 LEU C C     1 
ATOM   12807 O  O     . LEU C 2 245 ? 122.111 60.035  126.745 1.00 24.10 ?  224 LEU C O     1 
ATOM   12808 C  CB    . LEU C 2 245 ? 125.327 59.385  126.610 1.00 23.86 ?  224 LEU C CB    1 
ATOM   12809 C  CG    . LEU C 2 245 ? 126.567 59.340  127.514 1.00 24.78 ?  224 LEU C CG    1 
ATOM   12810 C  CD1   . LEU C 2 245 ? 127.736 60.099  126.878 1.00 25.54 ?  224 LEU C CD1   1 
ATOM   12811 C  CD2   . LEU C 2 245 ? 126.282 59.884  128.921 1.00 25.29 ?  224 LEU C CD2   1 
ATOM   12812 N  N     . ARG C 2 246 ? 122.510 58.325  125.328 1.00 25.26 ?  225 ARG C N     1 
ATOM   12813 C  CA    . ARG C 2 246 ? 121.261 58.496  124.571 1.00 25.97 ?  225 ARG C CA    1 
ATOM   12814 C  C     . ARG C 2 246 ? 120.062 58.192  125.459 1.00 25.85 ?  225 ARG C C     1 
ATOM   12815 O  O     . ARG C 2 246 ? 119.069 58.920  125.429 1.00 25.01 ?  225 ARG C O     1 
ATOM   12816 C  CB    . ARG C 2 246 ? 121.233 57.619  123.301 1.00 26.65 ?  225 ARG C CB    1 
ATOM   12817 C  CG    . ARG C 2 246 ? 122.262 58.023  122.248 1.00 28.90 ?  225 ARG C CG    1 
ATOM   12818 C  CD    . ARG C 2 246 ? 121.981 57.418  120.851 1.00 31.26 ?  225 ARG C CD    1 
ATOM   12819 N  NE    . ARG C 2 246 ? 121.964 55.953  120.854 1.00 34.01 ?  225 ARG C NE    1 
ATOM   12820 C  CZ    . ARG C 2 246 ? 123.045 55.175  120.897 1.00 35.64 ?  225 ARG C CZ    1 
ATOM   12821 N  NH1   . ARG C 2 246 ? 124.261 55.704  120.946 1.00 36.11 1  225 ARG C NH1   1 
ATOM   12822 N  NH2   . ARG C 2 246 ? 122.907 53.854  120.893 1.00 37.05 ?  225 ARG C NH2   1 
ATOM   12823 N  N     . GLU C 2 247 ? 120.162 57.124  126.256 1.00 26.01 ?  226 GLU C N     1 
ATOM   12824 C  CA    . GLU C 2 247 ? 119.120 56.790  127.234 1.00 26.48 ?  226 GLU C CA    1 
ATOM   12825 C  C     . GLU C 2 247 ? 118.903 57.940  128.216 1.00 25.72 ?  226 GLU C C     1 
ATOM   12826 O  O     . GLU C 2 247 ? 117.757 58.336  128.474 1.00 25.16 ?  226 GLU C O     1 
ATOM   12827 C  CB    . GLU C 2 247 ? 119.462 55.518  128.014 1.00 27.18 ?  226 GLU C CB    1 
ATOM   12828 C  CG    . GLU C 2 247 ? 118.253 54.908  128.714 1.00 30.38 ?  226 GLU C CG    1 
ATOM   12829 C  CD    . GLU C 2 247 ? 118.558 54.293  130.068 1.00 35.77 ?  226 GLU C CD    1 
ATOM   12830 O  OE1   . GLU C 2 247 ? 119.692 53.823  130.302 1.00 38.02 ?  226 GLU C OE1   1 
ATOM   12831 O  OE2   . GLU C 2 247 ? 117.638 54.277  130.915 1.00 40.39 -1 226 GLU C OE2   1 
ATOM   12832 N  N     . PHE C 2 248 ? 120.002 58.473  128.755 1.00 24.71 ?  227 PHE C N     1 
ATOM   12833 C  CA    . PHE C 2 248 ? 119.923 59.619  129.659 1.00 23.71 ?  227 PHE C CA    1 
ATOM   12834 C  C     . PHE C 2 248 ? 119.194 60.783  128.985 1.00 23.14 ?  227 PHE C C     1 
ATOM   12835 O  O     . PHE C 2 248 ? 118.278 61.363  129.571 1.00 22.40 ?  227 PHE C O     1 
ATOM   12836 C  CB    . PHE C 2 248 ? 121.311 60.080  130.141 1.00 23.85 ?  227 PHE C CB    1 
ATOM   12837 C  CG    . PHE C 2 248 ? 121.292 61.446  130.779 1.00 23.64 ?  227 PHE C CG    1 
ATOM   12838 C  CD1   . PHE C 2 248 ? 120.924 61.593  132.119 1.00 23.07 ?  227 PHE C CD1   1 
ATOM   12839 C  CD2   . PHE C 2 248 ? 121.573 62.594  130.019 1.00 23.04 ?  227 PHE C CD2   1 
ATOM   12840 C  CE1   . PHE C 2 248 ? 120.876 62.853  132.714 1.00 22.73 ?  227 PHE C CE1   1 
ATOM   12841 C  CE2   . PHE C 2 248 ? 121.522 63.864  130.597 1.00 23.31 ?  227 PHE C CE2   1 
ATOM   12842 C  CZ    . PHE C 2 248 ? 121.175 63.997  131.952 1.00 21.51 ?  227 PHE C CZ    1 
ATOM   12843 N  N     . ALA C 2 249 ? 119.603 61.107  127.757 1.00 22.95 ?  228 ALA C N     1 
ATOM   12844 C  CA    . ALA C 2 249 ? 119.075 62.275  127.039 1.00 22.96 ?  228 ALA C CA    1 
ATOM   12845 C  C     . ALA C 2 249 ? 117.585 62.127  126.741 1.00 23.31 ?  228 ALA C C     1 
ATOM   12846 O  O     . ALA C 2 249 ? 116.812 63.072  126.912 1.00 22.63 ?  228 ALA C O     1 
ATOM   12847 C  CB    . ALA C 2 249 ? 119.857 62.514  125.750 1.00 22.40 ?  228 ALA C CB    1 
ATOM   12848 N  N     . ILE C 2 250 ? 117.197 60.937  126.298 1.00 23.66 ?  229 ILE C N     1 
ATOM   12849 C  CA    . ILE C 2 250 ? 115.801 60.650  125.963 1.00 25.00 ?  229 ILE C CA    1 
ATOM   12850 C  C     . ILE C 2 250 ? 114.917 60.553  127.214 1.00 24.64 ?  229 ILE C C     1 
ATOM   12851 O  O     . ILE C 2 250 ? 113.815 61.117  127.238 1.00 24.26 ?  229 ILE C O     1 
ATOM   12852 C  CB    . ILE C 2 250 ? 115.681 59.409  125.024 1.00 25.43 ?  229 ILE C CB    1 
ATOM   12853 C  CG1   . ILE C 2 250 ? 116.205 59.780  123.629 1.00 27.27 ?  229 ILE C CG1   1 
ATOM   12854 C  CG2   . ILE C 2 250 ? 114.202 58.955  124.889 1.00 27.62 ?  229 ILE C CG2   1 
ATOM   12855 C  CD1   . ILE C 2 250 ? 116.947 58.655  122.893 1.00 31.32 ?  229 ILE C CD1   1 
ATOM   12856 N  N     . ASP C 2 251 ? 115.403 59.879  128.256 1.00 24.78 ?  230 ASP C N     1 
ATOM   12857 C  CA    . ASP C 2 251 ? 114.681 59.847  129.543 1.00 25.20 ?  230 ASP C CA    1 
ATOM   12858 C  C     . ASP C 2 251 ? 114.476 61.247  130.120 1.00 24.08 ?  230 ASP C C     1 
ATOM   12859 O  O     . ASP C 2 251 ? 113.395 61.570  130.637 1.00 23.34 ?  230 ASP C O     1 
ATOM   12860 C  CB    . ASP C 2 251 ? 115.429 59.010  130.591 1.00 25.73 ?  230 ASP C CB    1 
ATOM   12861 C  CG    . ASP C 2 251 ? 115.300 57.522  130.362 1.00 28.78 ?  230 ASP C CG    1 
ATOM   12862 O  OD1   . ASP C 2 251 ? 114.547 57.097  129.454 1.00 29.99 ?  230 ASP C OD1   1 
ATOM   12863 O  OD2   . ASP C 2 251 ? 115.969 56.772  131.104 1.00 33.31 -1 230 ASP C OD2   1 
ATOM   12864 N  N     . LEU C 2 252 ? 115.518 62.070  130.045 1.00 22.98 ?  231 LEU C N     1 
ATOM   12865 C  CA    . LEU C 2 252 ? 115.430 63.436  130.563 1.00 21.63 ?  231 LEU C CA    1 
ATOM   12866 C  C     . LEU C 2 252 ? 114.439 64.252  129.740 1.00 21.66 ?  231 LEU C C     1 
ATOM   12867 O  O     . LEU C 2 252 ? 113.634 65.010  130.283 1.00 19.41 ?  231 LEU C O     1 
ATOM   12868 C  CB    . LEU C 2 252 ? 116.796 64.121  130.556 1.00 21.89 ?  231 LEU C CB    1 
ATOM   12869 C  CG    . LEU C 2 252 ? 116.846 65.598  130.990 1.00 21.33 ?  231 LEU C CG    1 
ATOM   12870 C  CD1   . LEU C 2 252 ? 116.298 65.796  132.419 1.00 20.89 ?  231 LEU C CD1   1 
ATOM   12871 C  CD2   . LEU C 2 252 ? 118.284 66.110  130.864 1.00 20.31 ?  231 LEU C CD2   1 
ATOM   12872 N  N     . LEU C 2 253 ? 114.512 64.097  128.421 1.00 22.28 ?  232 LEU C N     1 
ATOM   12873 C  CA    . LEU C 2 253 ? 113.611 64.834  127.541 1.00 23.05 ?  232 LEU C CA    1 
ATOM   12874 C  C     . LEU C 2 253 ? 112.157 64.481  127.838 1.00 23.36 ?  232 LEU C C     1 
ATOM   12875 O  O     . LEU C 2 253 ? 111.323 65.385  128.013 1.00 22.96 ?  232 LEU C O     1 
ATOM   12876 C  CB    . LEU C 2 253 ? 113.948 64.589  126.069 1.00 23.53 ?  232 LEU C CB    1 
ATOM   12877 C  CG    . LEU C 2 253 ? 113.041 65.344  125.090 1.00 25.63 ?  232 LEU C CG    1 
ATOM   12878 C  CD1   . LEU C 2 253 ? 113.203 66.859  125.222 1.00 25.88 ?  232 LEU C CD1   1 
ATOM   12879 C  CD2   . LEU C 2 253 ? 113.335 64.889  123.668 1.00 27.67 ?  232 LEU C CD2   1 
ATOM   12880 N  N     . ASN C 2 254 ? 111.863 63.179  127.911 1.00 23.55 ?  233 ASN C N     1 
ATOM   12881 C  CA    . ASN C 2 254 ? 110.508 62.709  128.251 1.00 24.61 ?  233 ASN C CA    1 
ATOM   12882 C  C     . ASN C 2 254 ? 110.006 63.213  129.607 1.00 23.57 ?  233 ASN C C     1 
ATOM   12883 O  O     . ASN C 2 254 ? 108.852 63.614  129.741 1.00 23.52 ?  233 ASN C O     1 
ATOM   12884 C  CB    . ASN C 2 254 ? 110.416 61.183  128.182 1.00 24.99 ?  233 ASN C CB    1 
ATOM   12885 C  CG    . ASN C 2 254 ? 110.143 60.676  126.771 1.00 28.92 ?  233 ASN C CG    1 
ATOM   12886 O  OD1   . ASN C 2 254 ? 109.149 61.043  126.141 1.00 33.75 ?  233 ASN C OD1   1 
ATOM   12887 N  ND2   . ASN C 2 254 ? 111.023 59.827  126.275 1.00 30.99 ?  233 ASN C ND2   1 
ATOM   12888 N  N     . GLN C 2 255 ? 110.877 63.196  130.611 1.00 23.22 ?  234 GLN C N     1 
ATOM   12889 C  CA    . GLN C 2 255 ? 110.508 63.696  131.928 1.00 22.54 ?  234 GLN C CA    1 
ATOM   12890 C  C     . GLN C 2 255 ? 110.187 65.204  131.894 1.00 22.00 ?  234 GLN C C     1 
ATOM   12891 O  O     . GLN C 2 255 ? 109.185 65.658  132.474 1.00 21.73 ?  234 GLN C O     1 
ATOM   12892 C  CB    . GLN C 2 255 ? 111.608 63.393  132.943 1.00 22.85 ?  234 GLN C CB    1 
ATOM   12893 C  CG    . GLN C 2 255 ? 111.175 63.603  134.379 1.00 23.87 ?  234 GLN C CG    1 
ATOM   12894 C  CD    . GLN C 2 255 ? 112.286 63.331  135.386 1.00 24.95 ?  234 GLN C CD    1 
ATOM   12895 O  OE1   . GLN C 2 255 ? 113.354 62.816  135.035 1.00 24.21 ?  234 GLN C OE1   1 
ATOM   12896 N  NE2   . GLN C 2 255 ? 112.045 63.703  136.645 1.00 25.97 ?  234 GLN C NE2   1 
ATOM   12897 N  N     . LEU C 2 256 ? 111.034 65.972  131.219 1.00 21.27 ?  235 LEU C N     1 
ATOM   12898 C  CA    . LEU C 2 256 ? 110.803 67.404  131.055 1.00 21.37 ?  235 LEU C CA    1 
ATOM   12899 C  C     . LEU C 2 256 ? 109.545 67.663  130.220 1.00 21.21 ?  235 LEU C C     1 
ATOM   12900 O  O     . LEU C 2 256 ? 108.767 68.568  130.515 1.00 20.75 ?  235 LEU C O     1 
ATOM   12901 C  CB    . LEU C 2 256 ? 112.019 68.060  130.385 1.00 20.93 ?  235 LEU C CB    1 
ATOM   12902 C  CG    . LEU C 2 256 ? 113.311 68.219  131.191 1.00 21.74 ?  235 LEU C CG    1 
ATOM   12903 C  CD1   . LEU C 2 256 ? 114.423 68.775  130.290 1.00 20.15 ?  235 LEU C CD1   1 
ATOM   12904 C  CD2   . LEU C 2 256 ? 113.118 69.105  132.420 1.00 20.90 ?  235 LEU C CD2   1 
ATOM   12905 N  N     . TYR C 2 257 ? 109.376 66.866  129.171 1.00 21.68 ?  236 TYR C N     1 
ATOM   12906 C  CA    . TYR C 2 257 ? 108.230 66.977  128.269 1.00 22.40 ?  236 TYR C CA    1 
ATOM   12907 C  C     . TYR C 2 257 ? 106.901 66.792  129.020 1.00 23.31 ?  236 TYR C C     1 
ATOM   12908 O  O     . TYR C 2 257 ? 105.992 67.638  128.905 1.00 22.99 ?  236 TYR C O     1 
ATOM   12909 C  CB    . TYR C 2 257 ? 108.367 65.978  127.116 1.00 22.81 ?  236 TYR C CB    1 
ATOM   12910 C  CG    . TYR C 2 257 ? 107.170 65.899  126.189 1.00 23.76 ?  236 TYR C CG    1 
ATOM   12911 C  CD1   . TYR C 2 257 ? 106.824 66.976  125.368 1.00 24.05 ?  236 TYR C CD1   1 
ATOM   12912 C  CD2   . TYR C 2 257 ? 106.379 64.754  126.143 1.00 24.04 ?  236 TYR C CD2   1 
ATOM   12913 C  CE1   . TYR C 2 257 ? 105.720 66.914  124.525 1.00 24.40 ?  236 TYR C CE1   1 
ATOM   12914 C  CE2   . TYR C 2 257 ? 105.273 64.682  125.298 1.00 26.30 ?  236 TYR C CE2   1 
ATOM   12915 C  CZ    . TYR C 2 257 ? 104.961 65.762  124.493 1.00 25.80 ?  236 TYR C CZ    1 
ATOM   12916 O  OH    . TYR C 2 257 ? 103.882 65.684  123.659 1.00 28.42 ?  236 TYR C OH    1 
ATOM   12917 N  N     . GLU C 2 258 ? 106.807 65.721  129.815 1.00 22.99 ?  237 GLU C N     1 
ATOM   12918 C  CA    . GLU C 2 258 ? 105.586 65.426  130.573 1.00 24.46 ?  237 GLU C CA    1 
ATOM   12919 C  C     . GLU C 2 258 ? 105.231 66.547  131.535 1.00 23.86 ?  237 GLU C C     1 
ATOM   12920 O  O     . GLU C 2 258 ? 104.064 66.918  131.658 1.00 24.01 ?  237 GLU C O     1 
ATOM   12921 C  CB    . GLU C 2 258 ? 105.681 64.075  131.304 1.00 25.21 ?  237 GLU C CB    1 
ATOM   12922 C  CG    . GLU C 2 258 ? 105.681 62.855  130.354 1.00 30.12 ?  237 GLU C CG    1 
ATOM   12923 C  CD    . GLU C 2 258 ? 104.358 62.680  129.602 1.00 35.29 ?  237 GLU C CD    1 
ATOM   12924 O  OE1   . GLU C 2 258 ? 103.294 63.077  130.131 1.00 37.71 ?  237 GLU C OE1   1 
ATOM   12925 O  OE2   . GLU C 2 258 ? 104.381 62.136  128.472 1.00 39.07 -1 237 GLU C OE2   1 
ATOM   12926 N  N     . ASN C 2 259 ? 106.245 67.108  132.193 1.00 23.25 ?  238 ASN C N     1 
ATOM   12927 C  CA    . ASN C 2 259 ? 106.047 68.271  133.056 1.00 23.10 ?  238 ASN C CA    1 
ATOM   12928 C  C     . ASN C 2 259 ? 105.610 69.509  132.250 1.00 22.68 ?  238 ASN C C     1 
ATOM   12929 O  O     . ASN C 2 259 ? 104.725 70.259  132.673 1.00 22.73 ?  238 ASN C O     1 
ATOM   12930 C  CB    . ASN C 2 259 ? 107.322 68.548  133.856 1.00 23.22 ?  238 ASN C CB    1 
ATOM   12931 C  CG    . ASN C 2 259 ? 107.172 69.721  134.803 1.00 24.46 ?  238 ASN C CG    1 
ATOM   12932 O  OD1   . ASN C 2 259 ? 106.456 69.642  135.806 1.00 26.28 ?  238 ASN C OD1   1 
ATOM   12933 N  ND2   . ASN C 2 259 ? 107.848 70.820  134.490 1.00 24.93 ?  238 ASN C ND2   1 
ATOM   12934 N  N     . GLU C 2 260 ? 106.211 69.705  131.079 1.00 22.64 ?  239 GLU C N     1 
ATOM   12935 C  CA    . GLU C 2 260 ? 105.893 70.864  130.243 1.00 23.18 ?  239 GLU C CA    1 
ATOM   12936 C  C     . GLU C 2 260 ? 104.448 70.813  129.717 1.00 23.40 ?  239 GLU C C     1 
ATOM   12937 O  O     . GLU C 2 260 ? 103.790 71.857  129.579 1.00 23.57 ?  239 GLU C O     1 
ATOM   12938 C  CB    . GLU C 2 260 ? 106.896 71.004  129.089 1.00 23.19 ?  239 GLU C CB    1 
ATOM   12939 C  CG    . GLU C 2 260 ? 107.079 72.455  128.585 1.00 24.33 ?  239 GLU C CG    1 
ATOM   12940 C  CD    . GLU C 2 260 ? 107.696 73.397  129.635 1.00 27.99 ?  239 GLU C CD    1 
ATOM   12941 O  OE1   . GLU C 2 260 ? 108.128 72.937  130.715 1.00 27.36 ?  239 GLU C OE1   1 
ATOM   12942 O  OE2   . GLU C 2 260 ? 107.740 74.621  129.382 1.00 28.98 -1 239 GLU C OE2   1 
ATOM   12943 N  N     . LEU C 2 261 ? 103.959 69.605  129.438 1.00 23.35 ?  240 LEU C N     1 
ATOM   12944 C  CA    . LEU C 2 261 ? 102.552 69.412  129.052 1.00 23.74 ?  240 LEU C CA    1 
ATOM   12945 C  C     . LEU C 2 261 ? 101.584 69.954  130.107 1.00 23.80 ?  240 LEU C C     1 
ATOM   12946 O  O     . LEU C 2 261 ? 100.638 70.691  129.786 1.00 23.33 ?  240 LEU C O     1 
ATOM   12947 C  CB    . LEU C 2 261 ? 102.250 67.935  128.784 1.00 24.09 ?  240 LEU C CB    1 
ATOM   12948 C  CG    . LEU C 2 261 ? 102.876 67.309  127.537 1.00 24.07 ?  240 LEU C CG    1 
ATOM   12949 C  CD1   . LEU C 2 261 ? 102.483 65.841  127.446 1.00 24.77 ?  240 LEU C CD1   1 
ATOM   12950 C  CD2   . LEU C 2 261 ? 102.462 68.073  126.263 1.00 24.38 ?  240 LEU C CD2   1 
ATOM   12951 N  N     . GLU C 2 262 ? 101.820 69.578  131.359 1.00 23.41 ?  241 GLU C N     1 
ATOM   12952 C  CA    . GLU C 2 262 ? 100.998 70.048  132.473 1.00 24.02 ?  241 GLU C CA    1 
ATOM   12953 C  C     . GLU C 2 262 ? 101.099 71.569  132.662 1.00 22.91 ?  241 GLU C C     1 
ATOM   12954 O  O     . GLU C 2 262 ? 100.096 72.228  132.903 1.00 22.94 ?  241 GLU C O     1 
ATOM   12955 C  CB    . GLU C 2 262 ? 101.399 69.321  133.758 1.00 24.92 ?  241 GLU C CB    1 
ATOM   12956 C  CG    . GLU C 2 262 ? 101.108 67.829  133.750 1.00 27.82 ?  241 GLU C CG    1 
ATOM   12957 C  CD    . GLU C 2 262 ? 101.495 67.160  135.057 1.00 33.08 ?  241 GLU C CD    1 
ATOM   12958 O  OE1   . GLU C 2 262 ? 102.690 66.843  135.252 1.00 36.94 ?  241 GLU C OE1   1 
ATOM   12959 O  OE2   . GLU C 2 262 ? 100.598 66.941  135.891 1.00 37.48 -1 241 GLU C OE2   1 
ATOM   12960 N  N     . TYR C 2 263 ? 102.317 72.107  132.561 1.00 21.84 ?  242 TYR C N     1 
ATOM   12961 C  CA    . TYR C 2 263 ? 102.567 73.547  132.601 1.00 21.66 ?  242 TYR C CA    1 
ATOM   12962 C  C     . TYR C 2 263 ? 101.817 74.262  131.484 1.00 21.28 ?  242 TYR C C     1 
ATOM   12963 O  O     . TYR C 2 263 ? 101.188 75.305  131.712 1.00 21.14 ?  242 TYR C O     1 
ATOM   12964 C  CB    . TYR C 2 263 ? 104.071 73.817  132.442 1.00 21.44 ?  242 TYR C CB    1 
ATOM   12965 C  CG    . TYR C 2 263 ? 104.500 75.277  132.488 1.00 21.89 ?  242 TYR C CG    1 
ATOM   12966 C  CD1   . TYR C 2 263 ? 104.449 76.005  133.678 1.00 22.52 ?  242 TYR C CD1   1 
ATOM   12967 C  CD2   . TYR C 2 263 ? 104.994 75.916  131.347 1.00 22.58 ?  242 TYR C CD2   1 
ATOM   12968 C  CE1   . TYR C 2 263 ? 104.864 77.336  133.727 1.00 22.67 ?  242 TYR C CE1   1 
ATOM   12969 C  CE2   . TYR C 2 263 ? 105.418 77.250  131.387 1.00 24.03 ?  242 TYR C CE2   1 
ATOM   12970 C  CZ    . TYR C 2 263 ? 105.356 77.947  132.588 1.00 23.75 ?  242 TYR C CZ    1 
ATOM   12971 O  OH    . TYR C 2 263 ? 105.763 79.265  132.649 1.00 26.82 ?  242 TYR C OH    1 
ATOM   12972 N  N     . THR C 2 264 ? 101.891 73.699  130.280 1.00 20.66 ?  243 THR C N     1 
ATOM   12973 C  CA    . THR C 2 264 ? 101.239 74.290  129.103 1.00 20.99 ?  243 THR C CA    1 
ATOM   12974 C  C     . THR C 2 264 ? 99.718  74.338  129.286 1.00 21.22 ?  243 THR C C     1 
ATOM   12975 O  O     . THR C 2 264 ? 99.089  75.379  129.039 1.00 20.95 ?  243 THR C O     1 
ATOM   12976 C  CB    . THR C 2 264 ? 101.616 73.523  127.806 1.00 20.58 ?  243 THR C CB    1 
ATOM   12977 O  OG1   . THR C 2 264 ? 103.015 73.687  127.558 1.00 20.84 ?  243 THR C OG1   1 
ATOM   12978 C  CG2   . THR C 2 264 ? 100.837 74.047  126.597 1.00 20.90 ?  243 THR C CG2   1 
ATOM   12979 N  N     . GLU C 2 265 ? 99.135  73.230  129.745 1.00 21.62 ?  244 GLU C N     1 
ATOM   12980 C  CA    . GLU C 2 265 ? 97.692  73.184  129.987 1.00 23.46 ?  244 GLU C CA    1 
ATOM   12981 C  C     . GLU C 2 265 ? 97.278  74.183  131.048 1.00 23.33 ?  244 GLU C C     1 
ATOM   12982 O  O     . GLU C 2 265 ? 96.277  74.887  130.904 1.00 22.86 ?  244 GLU C O     1 
ATOM   12983 C  CB    . GLU C 2 265 ? 97.230  71.780  130.381 1.00 24.31 ?  244 GLU C CB    1 
ATOM   12984 C  CG    . GLU C 2 265 ? 97.253  70.785  129.226 1.00 27.63 ?  244 GLU C CG    1 
ATOM   12985 C  CD    . GLU C 2 265 ? 96.779  69.395  129.641 1.00 33.27 ?  244 GLU C CD    1 
ATOM   12986 O  OE1   . GLU C 2 265 ? 95.941  69.292  130.566 1.00 35.56 ?  244 GLU C OE1   1 
ATOM   12987 O  OE2   . GLU C 2 265 ? 97.240  68.403  129.032 1.00 35.96 -1 244 GLU C OE2   1 
ATOM   12988 N  N     . ASP C 2 266 ? 98.062  74.247  132.114 1.00 23.36 ?  245 ASP C N     1 
ATOM   12989 C  CA    . ASP C 2 266 ? 97.797  75.174  133.201 1.00 24.18 ?  245 ASP C CA    1 
ATOM   12990 C  C     . ASP C 2 266 ? 97.749  76.638  132.723 1.00 23.96 ?  245 ASP C C     1 
ATOM   12991 O  O     . ASP C 2 266 ? 96.894  77.409  133.153 1.00 24.19 ?  245 ASP C O     1 
ATOM   12992 C  CB    . ASP C 2 266 ? 98.864  75.001  134.279 1.00 25.14 ?  245 ASP C CB    1 
ATOM   12993 C  CG    . ASP C 2 266 ? 98.528  75.739  135.539 1.00 27.35 ?  245 ASP C CG    1 
ATOM   12994 O  OD1   . ASP C 2 266 ? 97.436  75.498  136.095 1.00 28.45 ?  245 ASP C OD1   1 
ATOM   12995 O  OD2   . ASP C 2 266 ? 99.363  76.564  135.969 1.00 31.99 -1 245 ASP C OD2   1 
ATOM   12996 N  N     . LEU C 2 267 ? 98.651  77.008  131.822 1.00 23.34 ?  246 LEU C N     1 
ATOM   12997 C  CA    . LEU C 2 267 ? 98.712  78.386  131.325 1.00 23.53 ?  246 LEU C CA    1 
ATOM   12998 C  C     . LEU C 2 267 ? 97.757  78.692  130.181 1.00 22.94 ?  246 LEU C C     1 
ATOM   12999 O  O     . LEU C 2 267 ? 97.149  79.763  130.149 1.00 23.14 ?  246 LEU C O     1 
ATOM   13000 C  CB    . LEU C 2 267 ? 100.133 78.724  130.882 1.00 23.37 ?  246 LEU C CB    1 
ATOM   13001 C  CG    . LEU C 2 267 ? 101.186 78.904  131.977 1.00 26.17 ?  246 LEU C CG    1 
ATOM   13002 C  CD1   . LEU C 2 267 ? 102.503 79.253  131.321 1.00 27.31 ?  246 LEU C CD1   1 
ATOM   13003 C  CD2   . LEU C 2 267 ? 100.776 80.005  132.950 1.00 28.08 ?  246 LEU C CD2   1 
ATOM   13004 N  N     . TYR C 2 268 ? 97.649  77.764  129.236 1.00 22.46 ?  247 TYR C N     1 
ATOM   13005 C  CA    . TYR C 2 268 ? 96.959  78.042  127.979 1.00 22.00 ?  247 TYR C CA    1 
ATOM   13006 C  C     . TYR C 2 268 ? 95.502  77.627  127.863 1.00 22.26 ?  247 TYR C C     1 
ATOM   13007 O  O     . TYR C 2 268 ? 94.824  78.095  126.947 1.00 22.17 ?  247 TYR C O     1 
ATOM   13008 C  CB    . TYR C 2 268 ? 97.749  77.470  126.795 1.00 21.73 ?  247 TYR C CB    1 
ATOM   13009 C  CG    . TYR C 2 268 ? 99.026  78.221  126.505 1.00 21.49 ?  247 TYR C CG    1 
ATOM   13010 C  CD1   . TYR C 2 268 ? 100.260 77.729  126.939 1.00 19.45 ?  247 TYR C CD1   1 
ATOM   13011 C  CD2   . TYR C 2 268 ? 98.998  79.435  125.809 1.00 22.71 ?  247 TYR C CD2   1 
ATOM   13012 C  CE1   . TYR C 2 268 ? 101.443 78.428  126.681 1.00 20.30 ?  247 TYR C CE1   1 
ATOM   13013 C  CE2   . TYR C 2 268 ? 100.179 80.147  125.537 1.00 21.69 ?  247 TYR C CE2   1 
ATOM   13014 C  CZ    . TYR C 2 268 ? 101.391 79.627  125.965 1.00 21.40 ?  247 TYR C CZ    1 
ATOM   13015 O  OH    . TYR C 2 268 ? 102.544 80.317  125.693 1.00 22.11 ?  247 TYR C OH    1 
ATOM   13016 N  N     . ASP C 2 269 ? 95.014  76.746  128.743 1.00 22.40 ?  248 ASP C N     1 
ATOM   13017 C  CA    . ASP C 2 269 ? 93.596  76.347  128.679 1.00 22.75 ?  248 ASP C CA    1 
ATOM   13018 C  C     . ASP C 2 269 ? 92.659  77.553  128.744 1.00 22.55 ?  248 ASP C C     1 
ATOM   13019 O  O     . ASP C 2 269 ? 91.642  77.587  128.040 1.00 22.22 ?  248 ASP C O     1 
ATOM   13020 C  CB    . ASP C 2 269 ? 93.223  75.313  129.759 1.00 23.03 ?  248 ASP C CB    1 
ATOM   13021 C  CG    . ASP C 2 269 ? 93.619  73.895  129.384 1.00 25.02 ?  248 ASP C CG    1 
ATOM   13022 O  OD1   . ASP C 2 269 ? 94.002  73.643  128.221 1.00 26.85 ?  248 ASP C OD1   1 
ATOM   13023 O  OD2   . ASP C 2 269 ? 93.540  73.014  130.264 1.00 28.74 -1 248 ASP C OD2   1 
ATOM   13024 N  N     . GLN C 2 270 ? 93.006  78.543  129.571 1.00 22.21 ?  249 GLN C N     1 
ATOM   13025 C  CA    . GLN C 2 270 ? 92.154  79.746  129.718 1.00 22.39 ?  249 GLN C CA    1 
ATOM   13026 C  C     . GLN C 2 270 ? 92.124  80.659  128.485 1.00 21.65 ?  249 GLN C C     1 
ATOM   13027 O  O     . GLN C 2 270 ? 91.279  81.551  128.402 1.00 21.70 ?  249 GLN C O     1 
ATOM   13028 C  CB    . GLN C 2 270 ? 92.509  80.550  130.979 1.00 22.53 ?  249 GLN C CB    1 
ATOM   13029 C  CG    . GLN C 2 270 ? 93.948  81.124  131.033 1.00 22.73 ?  249 GLN C CG    1 
ATOM   13030 C  CD    . GLN C 2 270 ? 94.195  81.898  132.311 1.00 25.39 ?  249 GLN C CD    1 
ATOM   13031 O  OE1   . GLN C 2 270 ? 93.442  81.771  133.279 1.00 27.88 ?  249 GLN C OE1   1 
ATOM   13032 N  NE2   . GLN C 2 270 ? 95.246  82.715  132.327 1.00 24.88 ?  249 GLN C NE2   1 
ATOM   13033 N  N     . VAL C 2 271 ? 93.041  80.438  127.541 1.00 20.91 ?  250 VAL C N     1 
ATOM   13034 C  CA    . VAL C 2 271 ? 93.067  81.205  126.274 1.00 20.62 ?  250 VAL C CA    1 
ATOM   13035 C  C     . VAL C 2 271 ? 92.822  80.304  125.049 1.00 20.53 ?  250 VAL C C     1 
ATOM   13036 O  O     . VAL C 2 271 ? 92.837  80.772  123.899 1.00 20.05 ?  250 VAL C O     1 
ATOM   13037 C  CB    . VAL C 2 271 ? 94.365  82.081  126.108 1.00 20.32 ?  250 VAL C CB    1 
ATOM   13038 C  CG1   . VAL C 2 271 ? 94.430  83.165  127.180 1.00 20.35 ?  250 VAL C CG1   1 
ATOM   13039 C  CG2   . VAL C 2 271 ? 95.646  81.235  126.141 1.00 19.32 ?  250 VAL C CG2   1 
ATOM   13040 N  N     . GLY C 2 272 ? 92.586  79.017  125.313 1.00 20.29 ?  251 GLY C N     1 
ATOM   13041 C  CA    . GLY C 2 272 ? 92.152  78.066  124.286 1.00 20.51 ?  251 GLY C CA    1 
ATOM   13042 C  C     . GLY C 2 272 ? 93.234  77.538  123.358 1.00 20.99 ?  251 GLY C C     1 
ATOM   13043 O  O     . GLY C 2 272 ? 92.931  77.064  122.251 1.00 20.22 ?  251 GLY C O     1 
ATOM   13044 N  N     . LEU C 2 273 ? 94.495  77.615  123.794 1.00 20.76 ?  252 LEU C N     1 
ATOM   13045 C  CA    . LEU C 2 273 ? 95.615  77.357  122.883 1.00 21.38 ?  252 LEU C CA    1 
ATOM   13046 C  C     . LEU C 2 273 ? 96.507  76.168  123.230 1.00 21.86 ?  252 LEU C C     1 
ATOM   13047 O  O     . LEU C 2 273 ? 97.522  75.949  122.570 1.00 22.45 ?  252 LEU C O     1 
ATOM   13048 C  CB    . LEU C 2 273 ? 96.467  78.625  122.696 1.00 21.44 ?  252 LEU C CB    1 
ATOM   13049 C  CG    . LEU C 2 273 ? 95.794  79.891  122.161 1.00 22.02 ?  252 LEU C CG    1 
ATOM   13050 C  CD1   . LEU C 2 273 ? 96.805  81.032  122.133 1.00 22.86 ?  252 LEU C CD1   1 
ATOM   13051 C  CD2   . LEU C 2 273 ? 95.184  79.653  120.763 1.00 23.88 ?  252 LEU C CD2   1 
ATOM   13052 N  N     . SER C 2 274 ? 96.129  75.387  124.240 1.00 22.19 ?  253 SER C N     1 
ATOM   13053 C  CA    . SER C 2 274 ? 97.029  74.374  124.787 1.00 22.47 ?  253 SER C CA    1 
ATOM   13054 C  C     . SER C 2 274 ? 97.502  73.356  123.747 1.00 22.94 ?  253 SER C C     1 
ATOM   13055 O  O     . SER C 2 274 ? 98.686  73.044  123.679 1.00 22.07 ?  253 SER C O     1 
ATOM   13056 C  CB    . SER C 2 274 ? 96.375  73.659  125.973 1.00 22.91 ?  253 SER C CB    1 
ATOM   13057 O  OG    . SER C 2 274 ? 96.246  74.556  127.057 1.00 24.25 ?  253 SER C OG    1 
ATOM   13058 N  N     . HIS C 2 275 ? 96.578  72.875  122.919 1.00 24.59 ?  254 HIS C N     1 
ATOM   13059 C  CA    . HIS C 2 275 ? 96.906  71.875  121.897 1.00 25.66 ?  254 HIS C CA    1 
ATOM   13060 C  C     . HIS C 2 275 ? 97.900  72.420  120.857 1.00 26.01 ?  254 HIS C C     1 
ATOM   13061 O  O     . HIS C 2 275 ? 98.826  71.712  120.425 1.00 26.23 ?  254 HIS C O     1 
ATOM   13062 C  CB    . HIS C 2 275 ? 95.626  71.376  121.213 1.00 26.89 ?  254 HIS C CB    1 
ATOM   13063 C  CG    . HIS C 2 275 ? 95.860  70.278  120.222 1.00 29.10 ?  254 HIS C CG    1 
ATOM   13064 N  ND1   . HIS C 2 275 ? 96.527  69.114  120.544 1.00 32.70 ?  254 HIS C ND1   1 
ATOM   13065 C  CD2   . HIS C 2 275 ? 95.514  70.164  118.919 1.00 31.68 ?  254 HIS C CD2   1 
ATOM   13066 C  CE1   . HIS C 2 275 ? 96.585  68.334  119.480 1.00 33.55 ?  254 HIS C CE1   1 
ATOM   13067 N  NE2   . HIS C 2 275 ? 95.964  68.940  118.485 1.00 33.71 ?  254 HIS C NE2   1 
ATOM   13068 N  N     . ASP C 2 276 ? 97.697  73.672  120.465 1.00 25.93 ?  255 ASP C N     1 
ATOM   13069 C  CA    . ASP C 2 276 ? 98.582  74.354  119.525 1.00 26.65 ?  255 ASP C CA    1 
ATOM   13070 C  C     . ASP C 2 276 ? 99.999  74.513  120.078 1.00 25.61 ?  255 ASP C C     1 
ATOM   13071 O  O     . ASP C 2 276 ? 100.977 74.234  119.371 1.00 25.34 ?  255 ASP C O     1 
ATOM   13072 C  CB    . ASP C 2 276 ? 98.008  75.719  119.141 1.00 27.44 ?  255 ASP C CB    1 
ATOM   13073 C  CG    . ASP C 2 276 ? 97.589  75.780  117.689 1.00 32.09 ?  255 ASP C CG    1 
ATOM   13074 O  OD1   . ASP C 2 276 ? 98.364  75.300  116.826 1.00 36.67 ?  255 ASP C OD1   1 
ATOM   13075 O  OD2   . ASP C 2 276 ? 96.482  76.294  117.405 1.00 36.30 -1 255 ASP C OD2   1 
ATOM   13076 N  N     . VAL C 2 277 ? 100.097 74.960  121.334 1.00 24.17 ?  256 VAL C N     1 
ATOM   13077 C  CA    . VAL C 2 277 ? 101.392 75.121  122.009 1.00 23.71 ?  256 VAL C CA    1 
ATOM   13078 C  C     . VAL C 2 277 ? 102.115 73.777  122.129 1.00 23.48 ?  256 VAL C C     1 
ATOM   13079 O  O     . VAL C 2 277 ? 103.326 73.700  121.917 1.00 23.08 ?  256 VAL C O     1 
ATOM   13080 C  CB    . VAL C 2 277 ? 101.253 75.762  123.418 1.00 23.27 ?  256 VAL C CB    1 
ATOM   13081 C  CG1   . VAL C 2 277 ? 102.624 75.916  124.086 1.00 24.02 ?  256 VAL C CG1   1 
ATOM   13082 C  CG2   . VAL C 2 277 ? 100.555 77.113  123.339 1.00 23.35 ?  256 VAL C CG2   1 
ATOM   13083 N  N     . LYS C 2 278 ? 101.373 72.726  122.466 1.00 23.36 ?  257 LYS C N     1 
ATOM   13084 C  CA    . LYS C 2 278 ? 101.938 71.380  122.562 1.00 24.12 ?  257 LYS C CA    1 
ATOM   13085 C  C     . LYS C 2 278 ? 102.612 70.930  121.268 1.00 24.30 ?  257 LYS C C     1 
ATOM   13086 O  O     . LYS C 2 278 ? 103.693 70.324  121.298 1.00 24.37 ?  257 LYS C O     1 
ATOM   13087 C  CB    . LYS C 2 278 ? 100.877 70.366  122.986 1.00 24.22 ?  257 LYS C CB    1 
ATOM   13088 C  CG    . LYS C 2 278 ? 100.489 70.454  124.452 1.00 24.96 ?  257 LYS C CG    1 
ATOM   13089 C  CD    . LYS C 2 278 ? 99.330  69.507  124.730 1.00 26.34 ?  257 LYS C CD    1 
ATOM   13090 C  CE    . LYS C 2 278 ? 98.880  69.589  126.163 1.00 27.16 ?  257 LYS C CE    1 
ATOM   13091 N  NZ    . LYS C 2 278 ? 97.751  68.633  126.371 1.00 29.60 1  257 LYS C NZ    1 
ATOM   13092 N  N     . LYS C 2 279 ? 101.982 71.227  120.133 1.00 24.55 ?  258 LYS C N     1 
ATOM   13093 C  CA    . LYS C 2 279 ? 102.584 70.924  118.838 1.00 24.85 ?  258 LYS C CA    1 
ATOM   13094 C  C     . LYS C 2 279 ? 103.893 71.691  118.665 1.00 24.57 ?  258 LYS C C     1 
ATOM   13095 O  O     . LYS C 2 279 ? 104.873 71.141  118.163 1.00 24.07 ?  258 LYS C O     1 
ATOM   13096 C  CB    . LYS C 2 279 ? 101.622 71.264  117.700 1.00 25.30 ?  258 LYS C CB    1 
ATOM   13097 C  CG    . LYS C 2 279 ? 100.329 70.482  117.730 1.00 26.63 ?  258 LYS C CG    1 
ATOM   13098 C  CD    . LYS C 2 279 ? 99.450  70.906  116.560 1.00 29.30 ?  258 LYS C CD    1 
ATOM   13099 C  CE    . LYS C 2 279 ? 98.230  70.041  116.470 1.00 31.79 ?  258 LYS C CE    1 
ATOM   13100 N  NZ    . LYS C 2 279 ? 97.240  70.678  115.565 1.00 33.80 1  258 LYS C NZ    1 
ATOM   13101 N  N     . PHE C 2 280 ? 103.904 72.948  119.113 1.00 24.29 ?  259 PHE C N     1 
ATOM   13102 C  CA    . PHE C 2 280 ? 105.082 73.819  119.007 1.00 24.90 ?  259 PHE C CA    1 
ATOM   13103 C  C     . PHE C 2 280 ? 106.264 73.309  119.852 1.00 24.86 ?  259 PHE C C     1 
ATOM   13104 O  O     . PHE C 2 280 ? 107.410 73.303  119.391 1.00 24.68 ?  259 PHE C O     1 
ATOM   13105 C  CB    . PHE C 2 280 ? 104.688 75.253  119.389 1.00 24.70 ?  259 PHE C CB    1 
ATOM   13106 C  CG    . PHE C 2 280 ? 105.740 76.298  119.098 1.00 25.70 ?  259 PHE C CG    1 
ATOM   13107 C  CD1   . PHE C 2 280 ? 106.221 76.495  117.803 1.00 26.86 ?  259 PHE C CD1   1 
ATOM   13108 C  CD2   . PHE C 2 280 ? 106.219 77.123  120.124 1.00 26.19 ?  259 PHE C CD2   1 
ATOM   13109 C  CE1   . PHE C 2 280 ? 107.179 77.482  117.530 1.00 26.66 ?  259 PHE C CE1   1 
ATOM   13110 C  CE2   . PHE C 2 280 ? 107.169 78.115  119.861 1.00 26.52 ?  259 PHE C CE2   1 
ATOM   13111 C  CZ    . PHE C 2 280 ? 107.655 78.290  118.559 1.00 26.23 ?  259 PHE C CZ    1 
ATOM   13112 N  N     . ILE C 2 281 ? 105.982 72.874  121.081 1.00 25.53 ?  260 ILE C N     1 
ATOM   13113 C  CA    . ILE C 2 281 ? 107.044 72.375  121.956 1.00 26.21 ?  260 ILE C CA    1 
ATOM   13114 C  C     . ILE C 2 281 ? 107.631 71.047  121.455 1.00 26.47 ?  260 ILE C C     1 
ATOM   13115 O  O     . ILE C 2 281 ? 108.826 70.811  121.601 1.00 26.52 ?  260 ILE C O     1 
ATOM   13116 C  CB    . ILE C 2 281 ? 106.643 72.330  123.472 1.00 26.27 ?  260 ILE C CB    1 
ATOM   13117 C  CG1   . ILE C 2 281 ? 105.762 71.122  123.797 1.00 27.37 ?  260 ILE C CG1   1 
ATOM   13118 C  CG2   . ILE C 2 281 ? 105.998 73.667  123.901 1.00 26.92 ?  260 ILE C CG2   1 
ATOM   13119 C  CD1   . ILE C 2 281 ? 105.399 70.989  125.277 1.00 29.51 ?  260 ILE C CD1   1 
ATOM   13120 N  N     . ARG C 2 282 ? 106.800 70.212  120.828 1.00 26.57 ?  261 ARG C N     1 
ATOM   13121 C  CA    . ARG C 2 282 ? 107.286 68.969  120.220 1.00 26.84 ?  261 ARG C CA    1 
ATOM   13122 C  C     . ARG C 2 282 ? 108.212 69.265  119.041 1.00 27.34 ?  261 ARG C C     1 
ATOM   13123 O  O     . ARG C 2 282 ? 109.268 68.652  118.909 1.00 27.54 ?  261 ARG C O     1 
ATOM   13124 C  CB    . ARG C 2 282 ? 106.131 68.059  119.795 1.00 26.98 ?  261 ARG C CB    1 
ATOM   13125 C  CG    . ARG C 2 282 ? 105.500 67.277  120.931 1.00 26.53 ?  261 ARG C CG    1 
ATOM   13126 C  CD    . ARG C 2 282 ? 104.553 66.177  120.408 1.00 27.77 ?  261 ARG C CD    1 
ATOM   13127 N  NE    . ARG C 2 282 ? 103.334 66.716  119.812 1.00 28.67 ?  261 ARG C NE    1 
ATOM   13128 C  CZ    . ARG C 2 282 ? 102.234 67.041  120.496 1.00 29.68 ?  261 ARG C CZ    1 
ATOM   13129 N  NH1   . ARG C 2 282 ? 102.183 66.886  121.818 1.00 28.31 1  261 ARG C NH1   1 
ATOM   13130 N  NH2   . ARG C 2 282 ? 101.178 67.515  119.856 1.00 29.15 ?  261 ARG C NH2   1 
ATOM   13131 N  N     . TYR C 2 283 ? 107.806 70.216  118.203 1.00 27.78 ?  262 TYR C N     1 
ATOM   13132 C  CA    . TYR C 2 283 ? 108.628 70.724  117.106 1.00 28.18 ?  262 TYR C CA    1 
ATOM   13133 C  C     . TYR C 2 283 ? 110.018 71.156  117.606 1.00 27.08 ?  262 TYR C C     1 
ATOM   13134 O  O     . TYR C 2 283 ? 111.057 70.755  117.058 1.00 26.51 ?  262 TYR C O     1 
ATOM   13135 C  CB    . TYR C 2 283 ? 107.909 71.903  116.439 1.00 29.11 ?  262 TYR C CB    1 
ATOM   13136 C  CG    . TYR C 2 283 ? 108.643 72.516  115.271 1.00 32.56 ?  262 TYR C CG    1 
ATOM   13137 C  CD1   . TYR C 2 283 ? 108.672 71.874  114.032 1.00 36.59 ?  262 TYR C CD1   1 
ATOM   13138 C  CD2   . TYR C 2 283 ? 109.295 73.747  115.396 1.00 36.34 ?  262 TYR C CD2   1 
ATOM   13139 C  CE1   . TYR C 2 283 ? 109.344 72.435  112.941 1.00 39.47 ?  262 TYR C CE1   1 
ATOM   13140 C  CE2   . TYR C 2 283 ? 109.969 74.323  114.303 1.00 39.23 ?  262 TYR C CE2   1 
ATOM   13141 C  CZ    . TYR C 2 283 ? 109.987 73.655  113.083 1.00 40.48 ?  262 TYR C CZ    1 
ATOM   13142 O  OH    . TYR C 2 283 ? 110.645 74.198  112.002 1.00 44.00 ?  262 TYR C OH    1 
ATOM   13143 N  N     . ASN C 2 284 ? 110.030 71.953  118.666 1.00 26.08 ?  263 ASN C N     1 
ATOM   13144 C  CA    . ASN C 2 284 ? 111.282 72.436  119.228 1.00 25.73 ?  263 ASN C CA    1 
ATOM   13145 C  C     . ASN C 2 284 ? 112.091 71.388  119.994 1.00 25.24 ?  263 ASN C C     1 
ATOM   13146 O  O     . ASN C 2 284 ? 113.329 71.438  119.982 1.00 25.56 ?  263 ASN C O     1 
ATOM   13147 C  CB    . ASN C 2 284 ? 111.043 73.712  120.036 1.00 25.69 ?  263 ASN C CB    1 
ATOM   13148 C  CG    . ASN C 2 284 ? 110.801 74.908  119.144 1.00 26.39 ?  263 ASN C CG    1 
ATOM   13149 O  OD1   . ASN C 2 284 ? 111.734 75.451  118.548 1.00 26.91 ?  263 ASN C OD1   1 
ATOM   13150 N  ND2   . ASN C 2 284 ? 109.547 75.323  119.037 1.00 27.56 ?  263 ASN C ND2   1 
ATOM   13151 N  N     . ALA C 2 285 ? 111.414 70.427  120.629 1.00 24.51 ?  264 ALA C N     1 
ATOM   13152 C  CA    . ALA C 2 285 ? 112.107 69.254  121.193 1.00 24.19 ?  264 ALA C CA    1 
ATOM   13153 C  C     . ALA C 2 285 ? 112.973 68.531  120.142 1.00 24.63 ?  264 ALA C C     1 
ATOM   13154 O  O     . ALA C 2 285 ? 114.108 68.150  120.421 1.00 24.01 ?  264 ALA C O     1 
ATOM   13155 C  CB    . ALA C 2 285 ? 111.122 68.281  121.815 1.00 23.63 ?  264 ALA C CB    1 
ATOM   13156 N  N     . ASN C 2 286 ? 112.429 68.351  118.939 1.00 24.66 ?  265 ASN C N     1 
ATOM   13157 C  CA    . ASN C 2 286 ? 113.186 67.769  117.830 1.00 25.24 ?  265 ASN C CA    1 
ATOM   13158 C  C     . ASN C 2 286 ? 114.423 68.569  117.435 1.00 25.09 ?  265 ASN C C     1 
ATOM   13159 O  O     . ASN C 2 286 ? 115.452 67.976  117.073 1.00 24.14 ?  265 ASN C O     1 
ATOM   13160 C  CB    . ASN C 2 286 ? 112.290 67.549  116.597 1.00 25.62 ?  265 ASN C CB    1 
ATOM   13161 C  CG    . ASN C 2 286 ? 111.349 66.366  116.766 1.00 26.46 ?  265 ASN C CG    1 
ATOM   13162 O  OD1   . ASN C 2 286 ? 111.494 65.566  117.693 1.00 27.14 ?  265 ASN C OD1   1 
ATOM   13163 N  ND2   . ASN C 2 286 ? 110.361 66.262  115.874 1.00 27.89 ?  265 ASN C ND2   1 
ATOM   13164 N  N     . LYS C 2 287 ? 114.307 69.899  117.490 1.00 24.99 ?  266 LYS C N     1 
ATOM   13165 C  CA    . LYS C 2 287 ? 115.425 70.807  117.226 1.00 25.91 ?  266 LYS C CA    1 
ATOM   13166 C  C     . LYS C 2 287 ? 116.497 70.685  118.305 1.00 25.23 ?  266 LYS C C     1 
ATOM   13167 O  O     . LYS C 2 287 ? 117.691 70.721  118.001 1.00 25.34 ?  266 LYS C O     1 
ATOM   13168 C  CB    . LYS C 2 287 ? 114.963 72.263  117.164 1.00 25.96 ?  266 LYS C CB    1 
ATOM   13169 C  CG    . LYS C 2 287 ? 114.218 72.668  115.901 1.00 29.60 ?  266 LYS C CG    1 
ATOM   13170 C  CD    . LYS C 2 287 ? 114.068 74.195  115.886 1.00 34.20 ?  266 LYS C CD    1 
ATOM   13171 C  CE    . LYS C 2 287 ? 113.425 74.700  114.618 1.00 37.67 ?  266 LYS C CE    1 
ATOM   13172 N  NZ    . LYS C 2 287 ? 113.435 76.200  114.600 1.00 39.48 1  266 LYS C NZ    1 
ATOM   13173 N  N     . ALA C 2 288 ? 116.071 70.557  119.559 1.00 24.87 ?  267 ALA C N     1 
ATOM   13174 C  CA    . ALA C 2 288 ? 117.008 70.312  120.671 1.00 24.23 ?  267 ALA C CA    1 
ATOM   13175 C  C     . ALA C 2 288 ? 117.768 68.992  120.482 1.00 24.24 ?  267 ALA C C     1 
ATOM   13176 O  O     . ALA C 2 288 ? 118.991 68.947  120.629 1.00 23.96 ?  267 ALA C O     1 
ATOM   13177 C  CB    . ALA C 2 288 ? 116.278 70.321  122.000 1.00 24.23 ?  267 ALA C CB    1 
ATOM   13178 N  N     . LEU C 2 289 ? 117.046 67.922  120.152 1.00 24.63 ?  268 LEU C N     1 
ATOM   13179 C  CA    . LEU C 2 289 ? 117.688 66.636  119.868 1.00 25.14 ?  268 LEU C CA    1 
ATOM   13180 C  C     . LEU C 2 289 ? 118.687 66.774  118.730 1.00 25.58 ?  268 LEU C C     1 
ATOM   13181 O  O     . LEU C 2 289 ? 119.801 66.271  118.818 1.00 25.42 ?  268 LEU C O     1 
ATOM   13182 C  CB    . LEU C 2 289 ? 116.659 65.539  119.550 1.00 25.28 ?  268 LEU C CB    1 
ATOM   13183 C  CG    . LEU C 2 289 ? 115.870 65.013  120.753 1.00 25.93 ?  268 LEU C CG    1 
ATOM   13184 C  CD1   . LEU C 2 289 ? 114.610 64.301  120.303 1.00 26.50 ?  268 LEU C CD1   1 
ATOM   13185 C  CD2   . LEU C 2 289 ? 116.723 64.119  121.671 1.00 25.20 ?  268 LEU C CD2   1 
ATOM   13186 N  N     . MET C 2 290 ? 118.294 67.477  117.668 1.00 26.32 ?  269 MET C N     1 
ATOM   13187 C  CA    . MET C 2 290 ? 119.197 67.673  116.538 1.00 27.41 ?  269 MET C CA    1 
ATOM   13188 C  C     . MET C 2 290 ? 120.452 68.460  116.910 1.00 26.66 ?  269 MET C C     1 
ATOM   13189 O  O     . MET C 2 290 ? 121.544 68.136  116.438 1.00 26.69 ?  269 MET C O     1 
ATOM   13190 C  CB    . MET C 2 290 ? 118.469 68.283  115.345 1.00 28.28 ?  269 MET C CB    1 
ATOM   13191 C  CG    . MET C 2 290 ? 117.903 67.203  114.424 1.00 32.91 ?  269 MET C CG    1 
ATOM   13192 S  SD    . MET C 2 290 ? 116.757 67.849  113.202 1.00 42.49 ?  269 MET C SD    1 
ATOM   13193 C  CE    . MET C 2 290 ? 115.192 67.273  113.859 1.00 38.74 ?  269 MET C CE    1 
ATOM   13194 N  N     . ASN C 2 291 ? 120.299 69.462  117.778 1.00 25.48 ?  270 ASN C N     1 
ATOM   13195 C  CA    . ASN C 2 291 ? 121.441 70.227  118.305 1.00 25.39 ?  270 ASN C CA    1 
ATOM   13196 C  C     . ASN C 2 291 ? 122.439 69.334  119.061 1.00 25.18 ?  270 ASN C C     1 
ATOM   13197 O  O     . ASN C 2 291 ? 123.638 69.639  119.131 1.00 24.73 ?  270 ASN C O     1 
ATOM   13198 C  CB    . ASN C 2 291 ? 120.959 71.373  119.204 1.00 24.83 ?  270 ASN C CB    1 
ATOM   13199 C  CG    . ASN C 2 291 ? 120.369 72.543  118.410 1.00 25.58 ?  270 ASN C CG    1 
ATOM   13200 O  OD1   . ASN C 2 291 ? 120.522 72.630  117.195 1.00 25.58 ?  270 ASN C OD1   1 
ATOM   13201 N  ND2   . ASN C 2 291 ? 119.692 73.444  119.105 1.00 24.32 ?  270 ASN C ND2   1 
ATOM   13202 N  N     . LEU C 2 292 ? 121.922 68.223  119.593 1.00 25.09 ?  271 LEU C N     1 
ATOM   13203 C  CA    . LEU C 2 292 ? 122.713 67.201  120.292 1.00 25.46 ?  271 LEU C CA    1 
ATOM   13204 C  C     . LEU C 2 292 ? 123.214 66.061  119.391 1.00 26.18 ?  271 LEU C C     1 
ATOM   13205 O  O     . LEU C 2 292 ? 123.873 65.116  119.862 1.00 26.06 ?  271 LEU C O     1 
ATOM   13206 C  CB    . LEU C 2 292 ? 121.905 66.643  121.471 1.00 25.19 ?  271 LEU C CB    1 
ATOM   13207 C  CG    . LEU C 2 292 ? 121.607 67.641  122.602 1.00 25.03 ?  271 LEU C CG    1 
ATOM   13208 C  CD1   . LEU C 2 292 ? 120.568 67.079  123.546 1.00 24.50 ?  271 LEU C CD1   1 
ATOM   13209 C  CD2   . LEU C 2 292 ? 122.897 68.001  123.356 1.00 25.64 ?  271 LEU C CD2   1 
ATOM   13210 N  N     . GLY C 2 293 ? 122.908 66.150  118.097 1.00 26.71 ?  272 GLY C N     1 
ATOM   13211 C  CA    . GLY C 2 293 ? 123.308 65.123  117.127 1.00 28.06 ?  272 GLY C CA    1 
ATOM   13212 C  C     . GLY C 2 293 ? 122.454 63.865  117.133 1.00 29.34 ?  272 GLY C C     1 
ATOM   13213 O  O     . GLY C 2 293 ? 122.900 62.799  116.681 1.00 29.73 ?  272 GLY C O     1 
ATOM   13214 N  N     . PHE C 2 294 ? 121.229 63.980  117.642 1.00 29.88 ?  273 PHE C N     1 
ATOM   13215 C  CA    . PHE C 2 294 ? 120.302 62.855  117.720 1.00 31.24 ?  273 PHE C CA    1 
ATOM   13216 C  C     . PHE C 2 294 ? 119.154 63.010  116.713 1.00 32.42 ?  273 PHE C C     1 
ATOM   13217 O  O     . PHE C 2 294 ? 118.846 64.125  116.267 1.00 32.30 ?  273 PHE C O     1 
ATOM   13218 C  CB    . PHE C 2 294 ? 119.748 62.698  119.142 1.00 30.82 ?  273 PHE C CB    1 
ATOM   13219 C  CG    . PHE C 2 294 ? 120.805 62.433  120.194 1.00 30.93 ?  273 PHE C CG    1 
ATOM   13220 C  CD1   . PHE C 2 294 ? 121.780 61.454  120.006 1.00 30.85 ?  273 PHE C CD1   1 
ATOM   13221 C  CD2   . PHE C 2 294 ? 120.813 63.156  121.378 1.00 30.30 ?  273 PHE C CD2   1 
ATOM   13222 C  CE1   . PHE C 2 294 ? 122.753 61.218  120.975 1.00 30.75 ?  273 PHE C CE1   1 
ATOM   13223 C  CE2   . PHE C 2 294 ? 121.773 62.918  122.363 1.00 30.41 ?  273 PHE C CE2   1 
ATOM   13224 C  CZ    . PHE C 2 294 ? 122.742 61.944  122.164 1.00 30.88 ?  273 PHE C CZ    1 
ATOM   13225 N  N     . ASP C 2 295 ? 118.542 61.885  116.350 1.00 33.81 ?  274 ASP C N     1 
ATOM   13226 C  CA    . ASP C 2 295 ? 117.385 61.868  115.450 1.00 35.32 ?  274 ASP C CA    1 
ATOM   13227 C  C     . ASP C 2 295 ? 116.140 62.484  116.114 1.00 35.36 ?  274 ASP C C     1 
ATOM   13228 O  O     . ASP C 2 295 ? 115.978 62.378  117.327 1.00 34.78 ?  274 ASP C O     1 
ATOM   13229 C  CB    . ASP C 2 295 ? 117.063 60.426  115.031 1.00 35.95 ?  274 ASP C CB    1 
ATOM   13230 C  CG    . ASP C 2 295 ? 118.180 59.776  114.219 1.00 37.98 ?  274 ASP C CG    1 
ATOM   13231 O  OD1   . ASP C 2 295 ? 118.947 60.490  113.536 1.00 39.83 ?  274 ASP C OD1   1 
ATOM   13232 O  OD2   . ASP C 2 295 ? 118.285 58.532  114.266 1.00 40.03 -1 274 ASP C OD2   1 
ATOM   13233 N  N     . PRO C 2 296 ? 115.257 63.119  115.320 1.00 36.33 ?  275 PRO C N     1 
ATOM   13234 C  CA    . PRO C 2 296 ? 113.977 63.623  115.863 1.00 36.92 ?  275 PRO C CA    1 
ATOM   13235 C  C     . PRO C 2 296 ? 113.145 62.522  116.542 1.00 37.68 ?  275 PRO C C     1 
ATOM   13236 O  O     . PRO C 2 296 ? 113.152 61.374  116.089 1.00 38.07 ?  275 PRO C O     1 
ATOM   13237 C  CB    . PRO C 2 296 ? 113.247 64.163  114.623 1.00 36.82 ?  275 PRO C CB    1 
ATOM   13238 C  CG    . PRO C 2 296 ? 114.019 63.623  113.427 1.00 37.42 ?  275 PRO C CG    1 
ATOM   13239 C  CD    . PRO C 2 296 ? 115.428 63.473  113.899 1.00 36.41 ?  275 PRO C CD    1 
ATOM   13240 N  N     . TYR C 2 297 ? 112.442 62.877  117.618 1.00 38.10 ?  276 TYR C N     1 
ATOM   13241 C  CA    . TYR C 2 297 ? 111.708 61.909  118.446 1.00 38.96 ?  276 TYR C CA    1 
ATOM   13242 C  C     . TYR C 2 297 ? 110.188 61.995  118.258 1.00 39.71 ?  276 TYR C C     1 
ATOM   13243 O  O     . TYR C 2 297 ? 109.476 61.001  118.432 1.00 40.18 ?  276 TYR C O     1 
ATOM   13244 C  CB    . TYR C 2 297 ? 112.065 62.135  119.919 1.00 38.94 ?  276 TYR C CB    1 
ATOM   13245 C  CG    . TYR C 2 297 ? 111.492 61.167  120.932 1.00 39.64 ?  276 TYR C CG    1 
ATOM   13246 C  CD1   . TYR C 2 297 ? 112.095 59.929  121.170 1.00 40.43 ?  276 TYR C CD1   1 
ATOM   13247 C  CD2   . TYR C 2 297 ? 110.384 61.513  121.699 1.00 41.04 ?  276 TYR C CD2   1 
ATOM   13248 C  CE1   . TYR C 2 297 ? 111.578 59.045  122.119 1.00 41.69 ?  276 TYR C CE1   1 
ATOM   13249 C  CE2   . TYR C 2 297 ? 109.857 60.638  122.650 1.00 41.60 ?  276 TYR C CE2   1 
ATOM   13250 C  CZ    . TYR C 2 297 ? 110.461 59.410  122.858 1.00 41.92 ?  276 TYR C CZ    1 
ATOM   13251 O  OH    . TYR C 2 297 ? 109.942 58.553  123.805 1.00 42.52 ?  276 TYR C OH    1 
ATOM   13252 N  N     . PHE C 2 298 ? 109.694 63.180  117.918 1.00 39.85 ?  277 PHE C N     1 
ATOM   13253 C  CA    . PHE C 2 298 ? 108.261 63.378  117.729 1.00 40.77 ?  277 PHE C CA    1 
ATOM   13254 C  C     . PHE C 2 298 ? 107.927 63.495  116.250 1.00 41.95 ?  277 PHE C C     1 
ATOM   13255 O  O     . PHE C 2 298 ? 108.743 63.978  115.466 1.00 41.91 ?  277 PHE C O     1 
ATOM   13256 C  CB    . PHE C 2 298 ? 107.789 64.629  118.478 1.00 39.94 ?  277 PHE C CB    1 
ATOM   13257 C  CG    . PHE C 2 298 ? 107.953 64.545  119.971 1.00 39.09 ?  277 PHE C CG    1 
ATOM   13258 C  CD1   . PHE C 2 298 ? 108.949 65.269  120.615 1.00 37.84 ?  277 PHE C CD1   1 
ATOM   13259 C  CD2   . PHE C 2 298 ? 107.100 63.753  120.737 1.00 38.97 ?  277 PHE C CD2   1 
ATOM   13260 C  CE1   . PHE C 2 298 ? 109.105 65.203  121.998 1.00 37.46 ?  277 PHE C CE1   1 
ATOM   13261 C  CE2   . PHE C 2 298 ? 107.245 63.678  122.117 1.00 38.20 ?  277 PHE C CE2   1 
ATOM   13262 C  CZ    . PHE C 2 298 ? 108.250 64.405  122.751 1.00 37.91 ?  277 PHE C CZ    1 
ATOM   13263 N  N     . GLU C 2 299 ? 106.732 63.051  115.860 1.00 43.74 ?  278 GLU C N     1 
ATOM   13264 C  CA    . GLU C 2 299 ? 106.310 63.171  114.460 1.00 45.61 ?  278 GLU C CA    1 
ATOM   13265 C  C     . GLU C 2 299 ? 105.986 64.626  114.118 1.00 46.04 ?  278 GLU C C     1 
ATOM   13266 O  O     . GLU C 2 299 ? 105.556 65.395  114.978 1.00 45.88 ?  278 GLU C O     1 
ATOM   13267 C  CB    . GLU C 2 299 ? 105.112 62.269  114.146 1.00 46.43 ?  278 GLU C CB    1 
ATOM   13268 C  CG    . GLU C 2 299 ? 105.089 61.773  112.690 1.00 48.82 ?  278 GLU C CG    1 
ATOM   13269 C  CD    . GLU C 2 299 ? 103.714 61.317  112.225 1.00 51.86 ?  278 GLU C CD    1 
ATOM   13270 O  OE1   . GLU C 2 299 ? 103.595 60.912  111.046 1.00 53.35 ?  278 GLU C OE1   1 
ATOM   13271 O  OE2   . GLU C 2 299 ? 102.750 61.364  113.024 1.00 53.10 -1 278 GLU C OE2   1 
ATOM   13272 N  N     . GLU C 2 300 ? 106.210 64.995  112.858 1.00 47.16 ?  279 GLU C N     1 
ATOM   13273 C  CA    . GLU C 2 300 ? 105.933 66.348  112.366 1.00 47.75 ?  279 GLU C CA    1 
ATOM   13274 C  C     . GLU C 2 300 ? 104.434 66.687  112.382 1.00 47.71 ?  279 GLU C C     1 
ATOM   13275 O  O     . GLU C 2 300 ? 103.593 65.833  112.079 1.00 47.77 ?  279 GLU C O     1 
ATOM   13276 C  CB    . GLU C 2 300 ? 106.526 66.538  110.958 1.00 48.42 ?  279 GLU C CB    1 
ATOM   13277 C  CG    . GLU C 2 300 ? 106.155 65.443  109.952 1.00 50.63 ?  279 GLU C CG    1 
ATOM   13278 C  CD    . GLU C 2 300 ? 107.146 65.329  108.793 1.00 53.06 ?  279 GLU C CD    1 
ATOM   13279 O  OE1   . GLU C 2 300 ? 107.412 66.354  108.120 1.00 54.35 ?  279 GLU C OE1   1 
ATOM   13280 O  OE2   . GLU C 2 300 ? 107.650 64.209  108.550 1.00 53.32 -1 279 GLU C OE2   1 
ATOM   13281 N  N     . GLU C 2 301 ? 104.121 67.927  112.758 1.00 47.40 ?  280 GLU C N     1 
ATOM   13282 C  CA    . GLU C 2 301 ? 102.744 68.437  112.798 1.00 47.46 ?  280 GLU C CA    1 
ATOM   13283 C  C     . GLU C 2 301 ? 102.685 69.868  112.249 1.00 47.31 ?  280 GLU C C     1 
ATOM   13284 O  O     . GLU C 2 301 ? 103.693 70.581  112.257 1.00 47.21 ?  280 GLU C O     1 
ATOM   13285 C  CB    . GLU C 2 301 ? 102.199 68.425  114.233 1.00 47.19 ?  280 GLU C CB    1 
ATOM   13286 C  CG    . GLU C 2 301 ? 102.121 67.054  114.907 1.00 47.14 ?  280 GLU C CG    1 
ATOM   13287 C  CD    . GLU C 2 301 ? 102.074 67.156  116.429 1.00 47.21 ?  280 GLU C CD    1 
ATOM   13288 O  OE1   . GLU C 2 301 ? 100.992 66.923  117.005 1.00 46.97 ?  280 GLU C OE1   1 
ATOM   13289 O  OE2   . GLU C 2 301 ? 103.117 67.480  117.047 1.00 46.13 -1 280 GLU C OE2   1 
ATOM   13290 N  N     . ASP C 2 302 ? 101.508 70.285  111.781 1.00 47.15 ?  281 ASP C N     1 
ATOM   13291 C  CA    . ASP C 2 302 ? 101.316 71.654  111.291 1.00 47.04 ?  281 ASP C CA    1 
ATOM   13292 C  C     . ASP C 2 302 ? 101.240 72.643  112.458 1.00 46.05 ?  281 ASP C C     1 
ATOM   13293 O  O     . ASP C 2 302 ? 100.350 72.544  113.310 1.00 46.10 ?  281 ASP C O     1 
ATOM   13294 C  CB    . ASP C 2 302 ? 100.048 71.767  110.424 1.00 47.66 ?  281 ASP C CB    1 
ATOM   13295 C  CG    . ASP C 2 302 ? 100.202 71.122  109.044 1.00 49.53 ?  281 ASP C CG    1 
ATOM   13296 O  OD1   . ASP C 2 302 ? 101.312 71.161  108.467 1.00 50.58 ?  281 ASP C OD1   1 
ATOM   13297 O  OD2   . ASP C 2 302 ? 99.190  70.592  108.523 1.00 51.14 -1 281 ASP C OD2   1 
ATOM   13298 N  N     . ILE C 2 303 ? 102.185 73.581  112.496 1.00 44.96 ?  282 ILE C N     1 
ATOM   13299 C  CA    . ILE C 2 303 ? 102.211 74.644  113.506 1.00 43.99 ?  282 ILE C CA    1 
ATOM   13300 C  C     . ILE C 2 303 ? 101.323 75.807  113.052 1.00 43.53 ?  282 ILE C C     1 
ATOM   13301 O  O     . ILE C 2 303 ? 101.219 76.074  111.854 1.00 43.52 ?  282 ILE C O     1 
ATOM   13302 C  CB    . ILE C 2 303 ? 103.662 75.151  113.759 1.00 43.84 ?  282 ILE C CB    1 
ATOM   13303 C  CG1   . ILE C 2 303 ? 104.603 73.990  114.129 1.00 43.91 ?  282 ILE C CG1   1 
ATOM   13304 C  CG2   . ILE C 2 303 ? 103.694 76.275  114.809 1.00 43.55 ?  282 ILE C CG2   1 
ATOM   13305 C  CD1   . ILE C 2 303 ? 104.204 73.194  115.376 1.00 42.76 ?  282 ILE C CD1   1 
ATOM   13306 N  N     . ASN C 2 304 ? 100.679 76.482  114.005 1.00 42.51 ?  283 ASN C N     1 
ATOM   13307 C  CA    . ASN C 2 304 ? 99.847  77.648  113.705 1.00 41.93 ?  283 ASN C CA    1 
ATOM   13308 C  C     . ASN C 2 304 ? 100.613 78.638  112.815 1.00 41.78 ?  283 ASN C C     1 
ATOM   13309 O  O     . ASN C 2 304 ? 101.690 79.111  113.203 1.00 41.13 ?  283 ASN C O     1 
ATOM   13310 C  CB    . ASN C 2 304 ? 99.394  78.329  115.006 1.00 41.83 ?  283 ASN C CB    1 
ATOM   13311 C  CG    . ASN C 2 304 ? 98.165  79.218  114.822 1.00 41.27 ?  283 ASN C CG    1 
ATOM   13312 O  OD1   . ASN C 2 304 ? 98.073  79.996  113.875 1.00 41.28 ?  283 ASN C OD1   1 
ATOM   13313 N  ND2   . ASN C 2 304 ? 97.219  79.105  115.742 1.00 40.67 ?  283 ASN C ND2   1 
ATOM   13314 N  N     . PRO C 2 305 ? 100.072 78.941  111.609 1.00 41.74 ?  284 PRO C N     1 
ATOM   13315 C  CA    . PRO C 2 305 ? 100.788 79.822  110.671 1.00 41.82 ?  284 PRO C CA    1 
ATOM   13316 C  C     . PRO C 2 305 ? 100.991 81.241  111.213 1.00 41.56 ?  284 PRO C C     1 
ATOM   13317 O  O     . PRO C 2 305 ? 101.901 81.943  110.770 1.00 41.46 ?  284 PRO C O     1 
ATOM   13318 C  CB    . PRO C 2 305 ? 99.892  79.826  109.417 1.00 42.14 ?  284 PRO C CB    1 
ATOM   13319 C  CG    . PRO C 2 305 ? 98.551  79.397  109.888 1.00 42.59 ?  284 PRO C CG    1 
ATOM   13320 C  CD    . PRO C 2 305 ? 98.799  78.456  111.042 1.00 42.05 ?  284 PRO C CD    1 
ATOM   13321 N  N     . ILE C 2 306 ? 100.158 81.641  112.172 1.00 41.19 ?  285 ILE C N     1 
ATOM   13322 C  CA    . ILE C 2 306 ? 100.310 82.922  112.863 1.00 41.47 ?  285 ILE C CA    1 
ATOM   13323 C  C     . ILE C 2 306 ? 101.667 82.983  113.577 1.00 41.71 ?  285 ILE C C     1 
ATOM   13324 O  O     . ILE C 2 306 ? 102.388 83.974  113.470 1.00 41.38 ?  285 ILE C O     1 
ATOM   13325 C  CB    . ILE C 2 306 ? 99.170  83.152  113.890 1.00 41.22 ?  285 ILE C CB    1 
ATOM   13326 C  CG1   . ILE C 2 306 ? 97.807  83.208  113.186 1.00 41.27 ?  285 ILE C CG1   1 
ATOM   13327 C  CG2   . ILE C 2 306 ? 99.421  84.415  114.711 1.00 40.37 ?  285 ILE C CG2   1 
ATOM   13328 C  CD1   . ILE C 2 306 ? 96.622  83.054  114.130 1.00 41.85 ?  285 ILE C CD1   1 
ATOM   13329 N  N     . VAL C 2 307 ? 101.996 81.912  114.297 1.00 42.33 ?  286 VAL C N     1 
ATOM   13330 C  CA    . VAL C 2 307 ? 103.271 81.796  115.013 1.00 43.36 ?  286 VAL C CA    1 
ATOM   13331 C  C     . VAL C 2 307 ? 104.470 81.787  114.056 1.00 44.51 ?  286 VAL C C     1 
ATOM   13332 O  O     . VAL C 2 307 ? 105.524 82.332  114.381 1.00 44.57 ?  286 VAL C O     1 
ATOM   13333 C  CB    . VAL C 2 307 ? 103.271 80.566  115.953 1.00 42.97 ?  286 VAL C CB    1 
ATOM   13334 C  CG1   . VAL C 2 307 ? 104.689 80.220  116.437 1.00 42.86 ?  286 VAL C CG1   1 
ATOM   13335 C  CG2   . VAL C 2 307 ? 102.352 80.833  117.130 1.00 41.93 ?  286 VAL C CG2   1 
ATOM   13336 N  N     . LEU C 2 308 ? 104.285 81.190  112.880 1.00 46.21 ?  287 LEU C N     1 
ATOM   13337 C  CA    . LEU C 2 308 ? 105.302 81.166  111.818 1.00 47.66 ?  287 LEU C CA    1 
ATOM   13338 C  C     . LEU C 2 308 ? 105.537 82.547  111.209 1.00 48.82 ?  287 LEU C C     1 
ATOM   13339 O  O     . LEU C 2 308 ? 106.670 82.885  110.839 1.00 49.02 ?  287 LEU C O     1 
ATOM   13340 C  CB    . LEU C 2 308 ? 104.923 80.151  110.730 1.00 47.95 ?  287 LEU C CB    1 
ATOM   13341 C  CG    . LEU C 2 308 ? 105.425 78.702  110.869 1.00 48.23 ?  287 LEU C CG    1 
ATOM   13342 C  CD1   . LEU C 2 308 ? 105.695 78.273  112.318 1.00 48.10 ?  287 LEU C CD1   1 
ATOM   13343 C  CD2   . LEU C 2 308 ? 104.481 77.723  110.176 1.00 48.81 ?  287 LEU C CD2   1 
ATOM   13344 N  N     . ASN C 2 309 ? 104.466 83.335  111.105 1.00 49.80 ?  288 ASN C N     1 
ATOM   13345 C  CA    . ASN C 2 309 ? 104.572 84.750  110.760 1.00 51.09 ?  288 ASN C CA    1 
ATOM   13346 C  C     . ASN C 2 309 ? 105.186 85.586  111.888 1.00 51.08 ?  288 ASN C C     1 
ATOM   13347 O  O     . ASN C 2 309 ? 105.761 86.645  111.635 1.00 51.41 ?  288 ASN C O     1 
ATOM   13348 C  CB    . ASN C 2 309 ? 103.216 85.319  110.337 1.00 51.37 ?  288 ASN C CB    1 
ATOM   13349 C  CG    . ASN C 2 309 ? 102.874 84.994  108.897 1.00 53.22 ?  288 ASN C CG    1 
ATOM   13350 O  OD1   . ASN C 2 309 ? 103.020 83.852  108.448 1.00 54.39 ?  288 ASN C OD1   1 
ATOM   13351 N  ND2   . ASN C 2 309 ? 102.417 86.001  108.159 1.00 54.70 ?  288 ASN C ND2   1 
ATOM   13352 N  N     . GLY C 2 310 ? 105.060 85.103  113.124 1.00 51.25 ?  289 GLY C N     1 
ATOM   13353 C  CA    . GLY C 2 310 ? 105.716 85.715  114.282 1.00 51.35 ?  289 GLY C CA    1 
ATOM   13354 C  C     . GLY C 2 310 ? 107.236 85.622  114.232 1.00 51.86 ?  289 GLY C C     1 
ATOM   13355 O  O     . GLY C 2 310 ? 107.933 86.400  114.894 1.00 51.49 ?  289 GLY C O     1 
ATOM   13356 N  N     . LEU C 2 311 ? 107.749 84.670  113.452 1.00 52.45 ?  290 LEU C N     1 
ATOM   13357 C  CA    . LEU C 2 311 ? 109.191 84.501  113.259 1.00 52.99 ?  290 LEU C CA    1 
ATOM   13358 C  C     . LEU C 2 311 ? 109.709 85.377  112.115 1.00 53.65 ?  290 LEU C C     1 
ATOM   13359 O  O     . LEU C 2 311 ? 109.426 85.128  110.937 1.00 54.22 ?  290 LEU C O     1 
ATOM   13360 C  CB    . LEU C 2 311 ? 109.535 83.031  113.000 1.00 53.08 ?  290 LEU C CB    1 
ATOM   13361 C  CG    . LEU C 2 311 ? 109.457 82.029  114.156 1.00 53.33 ?  290 LEU C CG    1 
ATOM   13362 C  CD1   . LEU C 2 311 ? 109.461 80.604  113.622 1.00 53.79 ?  290 LEU C CD1   1 
ATOM   13363 C  CD2   . LEU C 2 311 ? 110.598 82.235  115.155 1.00 53.22 ?  290 LEU C CD2   1 
ATOM   13364 N  N     . LYS C 2 330 ? 139.011 109.997 115.159 1.00 57.38 ?  309 LYS C N     1 
ATOM   13365 C  CA    . LYS C 2 330 ? 140.241 110.750 114.943 1.00 58.57 ?  309 LYS C CA    1 
ATOM   13366 C  C     . LYS C 2 330 ? 140.955 110.288 113.678 1.00 57.73 ?  309 LYS C C     1 
ATOM   13367 O  O     . LYS C 2 330 ? 140.771 109.158 113.226 1.00 59.72 ?  309 LYS C O     1 
ATOM   13368 C  CB    . LYS C 2 330 ? 141.175 110.610 116.146 1.00 55.66 ?  309 LYS C CB    1 
ATOM   13369 C  CG    . LYS C 2 330 ? 140.898 111.586 117.276 1.00 56.05 ?  309 LYS C CG    1 
ATOM   13370 C  CD    . LYS C 2 330 ? 142.041 111.594 118.279 1.00 57.52 ?  309 LYS C CD    1 
ATOM   13371 C  CE    . LYS C 2 330 ? 141.758 112.532 119.440 1.00 58.27 ?  309 LYS C CE    1 
ATOM   13372 N  NZ    . LYS C 2 330 ? 140.948 111.874 120.502 1.00 57.81 1  309 LYS C NZ    1 
ATOM   13373 N  N     . ALA C 2 331 ? 141.773 111.169 113.111 1.00 46.74 ?  310 ALA C N     1 
ATOM   13374 C  CA    . ALA C 2 331 ? 142.611 110.816 111.977 1.00 47.69 ?  310 ALA C CA    1 
ATOM   13375 C  C     . ALA C 2 331 ? 143.931 110.241 112.472 1.00 44.34 ?  310 ALA C C     1 
ATOM   13376 O  O     . ALA C 2 331 ? 144.451 110.638 113.518 1.00 44.88 ?  310 ALA C O     1 
ATOM   13377 C  CB    . ALA C 2 331 ? 142.867 112.031 111.085 1.00 44.94 ?  310 ALA C CB    1 
ATOM   13378 N  N     . THR C 2 332 ? 144.464 109.287 111.711 1.00 40.86 ?  311 THR C N     1 
ATOM   13379 C  CA    . THR C 2 332 ? 145.690 108.603 112.100 1.00 38.81 ?  311 THR C CA    1 
ATOM   13380 C  C     . THR C 2 332 ? 146.840 109.589 112.236 1.00 36.15 ?  311 THR C C     1 
ATOM   13381 O  O     . THR C 2 332 ? 147.057 110.432 111.362 1.00 43.30 ?  311 THR C O     1 
ATOM   13382 C  CB    . THR C 2 332 ? 146.037 107.519 111.076 1.00 39.78 ?  311 THR C CB    1 
ATOM   13383 O  OG1   . THR C 2 332 ? 144.980 106.553 111.025 1.00 41.99 ?  311 THR C OG1   1 
ATOM   13384 C  CG2   . THR C 2 332 ? 147.337 106.824 111.451 1.00 37.37 ?  311 THR C CG2   1 
ATOM   13385 N  N     . VAL C 2 333 ? 147.573 109.479 113.338 1.00 29.00 ?  312 VAL C N     1 
ATOM   13386 C  CA    . VAL C 2 333 ? 148.692 110.376 113.608 1.00 27.73 ?  312 VAL C CA    1 
ATOM   13387 C  C     . VAL C 2 333 ? 149.968 109.740 113.073 1.00 34.73 ?  312 VAL C C     1 
ATOM   13388 O  O     . VAL C 2 333 ? 150.354 108.646 113.495 1.00 34.24 ?  312 VAL C O     1 
ATOM   13389 C  CB    . VAL C 2 333 ? 148.809 110.675 115.109 1.00 29.67 ?  312 VAL C CB    1 
ATOM   13390 C  CG1   . VAL C 2 333 ? 150.101 111.421 115.402 1.00 33.09 ?  312 VAL C CG1   1 
ATOM   13391 C  CG2   . VAL C 2 333 ? 147.606 111.473 115.583 1.00 33.00 ?  312 VAL C CG2   1 
ATOM   13392 N  N     . GLU C 2 334 ? 150.621 110.426 112.139 1.00 31.99 ?  313 GLU C N     1 
ATOM   13393 C  CA    . GLU C 2 334 ? 151.868 109.966 111.561 1.00 30.19 ?  313 GLU C CA    1 
ATOM   13394 C  C     . GLU C 2 334 ? 152.938 111.030 111.764 1.00 35.47 ?  313 GLU C C     1 
ATOM   13395 O  O     . GLU C 2 334 ? 152.719 112.196 111.403 1.00 39.91 ?  313 GLU C O     1 
ATOM   13396 C  CB    . GLU C 2 334 ? 151.700 109.661 110.064 1.00 31.98 ?  313 GLU C CB    1 
ATOM   13397 C  CG    . GLU C 2 334 ? 152.737 108.701 109.507 1.00 30.40 ?  313 GLU C CG    1 
ATOM   13398 C  CD    . GLU C 2 334 ? 152.753 108.671 107.993 1.00 36.69 ?  313 GLU C CD    1 
ATOM   13399 O  OE1   . GLU C 2 334 ? 151.663 108.648 107.386 1.00 35.22 ?  313 GLU C OE1   1 
ATOM   13400 O  OE2   . GLU C 2 334 ? 153.856 108.652 107.408 1.00 37.50 -1 313 GLU C OE2   1 
ATOM   13401 N  N     . PRO C 2 335 ? 154.087 110.685 112.338 1.00 33.23 ?  314 PRO C N     1 
ATOM   13402 C  CA    . PRO C 2 335 ? 155.100 111.704 112.630 1.00 32.48 ?  314 PRO C CA    1 
ATOM   13403 C  C     . PRO C 2 335 ? 155.664 112.329 111.365 1.00 32.75 ?  314 PRO C C     1 
ATOM   13404 O  O     . PRO C 2 335 ? 155.761 111.692 110.313 1.00 33.62 ?  314 PRO C O     1 
ATOM   13405 C  CB    . PRO C 2 335 ? 156.178 110.924 113.391 1.00 27.14 ?  314 PRO C CB    1 
ATOM   13406 C  CG    . PRO C 2 335 ? 156.023 109.522 112.910 1.00 33.25 ?  314 PRO C CG    1 
ATOM   13407 C  CD    . PRO C 2 335 ? 154.547 109.332 112.698 1.00 31.97 ?  314 PRO C CD    1 
ATOM   13408 N  N     . LEU C 2 336 ? 156.035 113.601 111.482 1.00 31.37 ?  315 LEU C N     1 
ATOM   13409 C  CA    . LEU C 2 336 ? 156.638 114.325 110.374 1.00 25.32 ?  315 LEU C CA    1 
ATOM   13410 C  C     . LEU C 2 336 ? 158.078 113.881 110.170 1.00 30.05 ?  315 LEU C C     1 
ATOM   13411 O  O     . LEU C 2 336 ? 158.841 113.733 111.129 1.00 28.04 ?  315 LEU C O     1 
ATOM   13412 C  CB    . LEU C 2 336 ? 156.598 115.830 110.634 1.00 24.68 ?  315 LEU C CB    1 
ATOM   13413 C  CG    . LEU C 2 336 ? 155.386 116.624 110.150 1.00 29.53 ?  315 LEU C CG    1 
ATOM   13414 C  CD1   . LEU C 2 336 ? 155.330 117.960 110.870 1.00 23.58 ?  315 LEU C CD1   1 
ATOM   13415 C  CD2   . LEU C 2 336 ? 155.435 116.824 108.647 1.00 23.76 ?  315 LEU C CD2   1 
ATOM   13416 N  N     . LYS C 2 337 ? 158.451 113.675 108.912 1.00 29.08 ?  316 LYS C N     1 
ATOM   13417 C  CA    . LYS C 2 337 ? 159.825 113.358 108.568 1.00 24.90 ?  316 LYS C CA    1 
ATOM   13418 C  C     . LYS C 2 337 ? 160.598 114.636 108.251 1.00 25.51 ?  316 LYS C C     1 
ATOM   13419 O  O     . LYS C 2 337 ? 160.026 115.711 108.065 1.00 33.13 ?  316 LYS C O     1 
ATOM   13420 C  CB    . LYS C 2 337 ? 159.878 112.396 107.381 1.00 29.23 ?  316 LYS C CB    1 
ATOM   13421 C  CG    . LYS C 2 337 ? 158.965 111.191 107.504 1.00 29.66 ?  316 LYS C CG    1 
ATOM   13422 C  CD    . LYS C 2 337 ? 159.395 110.083 106.555 1.00 30.93 ?  316 LYS C CD    1 
ATOM   13423 C  CE    . LYS C 2 337 ? 158.812 108.741 106.965 1.00 33.14 ?  316 LYS C CE    1 
ATOM   13424 N  NZ    . LYS C 2 337 ? 157.454 108.882 107.561 1.00 33.67 1  316 LYS C NZ    1 
ATOM   13425 N  N     . ASP C 2 338 ? 161.924 114.506 108.200 1.00 26.51 ?  317 ASP C N     1 
ATOM   13426 C  CA    . ASP C 2 338 ? 162.755 115.640 107.812 1.00 29.94 ?  317 ASP C CA    1 
ATOM   13427 C  C     . ASP C 2 338 ? 162.490 116.042 106.368 1.00 29.65 ?  317 ASP C C     1 
ATOM   13428 O  O     . ASP C 2 338 ? 162.440 117.234 106.046 1.00 24.94 ?  317 ASP C O     1 
ATOM   13429 C  CB    . ASP C 2 338 ? 164.232 115.305 108.016 1.00 32.12 ?  317 ASP C CB    1 
ATOM   13430 C  CG    . ASP C 2 338 ? 164.715 115.631 109.415 1.00 35.61 ?  317 ASP C CG    1 
ATOM   13431 O  OD1   . ASP C 2 338 ? 164.526 114.793 110.321 1.00 36.45 ?  317 ASP C OD1   1 
ATOM   13432 O  OD2   . ASP C 2 338 ? 165.284 116.726 109.610 1.00 32.88 -1 317 ASP C OD2   1 
ATOM   13433 N  N     . ASP C 2 339 ? 162.307 115.059 105.485 1.00 31.98 ?  318 ASP C N     1 
ATOM   13434 C  CA    . ASP C 2 339 ? 162.065 115.336 104.074 1.00 23.82 ?  318 ASP C CA    1 
ATOM   13435 C  C     . ASP C 2 339 ? 160.710 115.981 103.817 1.00 21.90 ?  318 ASP C C     1 
ATOM   13436 O  O     . ASP C 2 339 ? 160.482 116.477 102.708 1.00 29.62 ?  318 ASP C O     1 
ATOM   13437 C  CB    . ASP C 2 339 ? 162.184 114.045 103.261 1.00 24.61 ?  318 ASP C CB    1 
ATOM   13438 C  CG    . ASP C 2 339 ? 163.617 113.568 103.133 1.00 36.61 ?  318 ASP C CG    1 
ATOM   13439 O  OD1   . ASP C 2 339 ? 164.530 114.419 103.113 1.00 34.94 ?  318 ASP C OD1   1 
ATOM   13440 O  OD2   . ASP C 2 339 ? 163.830 112.339 103.052 1.00 37.02 -1 318 ASP C OD2   1 
ATOM   13441 N  N     . ASP C 2 340 ? 159.807 115.981 104.799 1.00 21.75 ?  319 ASP C N     1 
ATOM   13442 C  CA    . ASP C 2 340 ? 158.511 116.628 104.635 1.00 12.52 ?  319 ASP C CA    1 
ATOM   13443 C  C     . ASP C 2 340 ? 158.609 118.147 104.613 1.00 11.68 ?  319 ASP C C     1 
ATOM   13444 O  O     . ASP C 2 340 ? 157.660 118.804 104.173 1.00 29.94 ?  319 ASP C O     1 
ATOM   13445 C  CB    . ASP C 2 340 ? 157.565 116.197 105.755 1.00 15.38 ?  319 ASP C CB    1 
ATOM   13446 C  CG    . ASP C 2 340 ? 157.082 114.774 105.593 1.00 27.80 ?  319 ASP C CG    1 
ATOM   13447 O  OD1   . ASP C 2 340 ? 156.382 114.279 106.499 1.00 35.11 ?  319 ASP C OD1   1 
ATOM   13448 O  OD2   . ASP C 2 340 ? 157.397 114.151 104.558 1.00 32.85 -1 319 ASP C OD2   1 
ATOM   13449 N  N     . PHE C 2 341 ? 159.720 118.713 105.073 1.00 19.10 ?  320 PHE C N     1 
ATOM   13450 C  CA    . PHE C 2 341 ? 159.892 120.156 105.159 1.00 9.08  ?  320 PHE C CA    1 
ATOM   13451 C  C     . PHE C 2 341 ? 160.566 120.750 103.931 1.00 17.46 ?  320 PHE C C     1 
ATOM   13452 O  O     . PHE C 2 341 ? 160.761 121.967 103.879 1.00 21.47 ?  320 PHE C O     1 
ATOM   13453 C  CB    . PHE C 2 341 ? 160.696 120.509 106.411 1.00 14.57 ?  320 PHE C CB    1 
ATOM   13454 C  CG    . PHE C 2 341 ? 159.938 120.313 107.690 1.00 10.84 ?  320 PHE C CG    1 
ATOM   13455 C  CD1   . PHE C 2 341 ? 159.220 121.353 108.250 1.00 9.48  ?  320 PHE C CD1   1 
ATOM   13456 C  CD2   . PHE C 2 341 ? 159.936 119.084 108.328 1.00 12.36 ?  320 PHE C CD2   1 
ATOM   13457 C  CE1   . PHE C 2 341 ? 158.519 121.174 109.425 1.00 7.91  ?  320 PHE C CE1   1 
ATOM   13458 C  CE2   . PHE C 2 341 ? 159.236 118.901 109.501 1.00 13.16 ?  320 PHE C CE2   1 
ATOM   13459 C  CZ    . PHE C 2 341 ? 158.527 119.946 110.050 1.00 4.56  ?  320 PHE C CZ    1 
ATOM   13460 N  N     . TYR C 2 342 ? 160.926 119.930 102.948 1.00 9.53  ?  321 TYR C N     1 
ATOM   13461 C  CA    . TYR C 2 342 ? 161.533 120.408 101.716 1.00 17.23 ?  321 TYR C CA    1 
ATOM   13462 C  C     . TYR C 2 342 ? 160.715 119.935 100.526 1.00 16.10 ?  321 TYR C C     1 
ATOM   13463 O  O     . TYR C 2 342 ? 160.146 118.841 100.533 1.00 16.88 ?  321 TYR C O     1 
ATOM   13464 C  CB    . TYR C 2 342 ? 163.001 119.957 101.563 1.00 17.88 ?  321 TYR C CB    1 
ATOM   13465 C  CG    . TYR C 2 342 ? 163.833 120.037 102.825 1.00 13.83 ?  321 TYR C CG    1 
ATOM   13466 C  CD1   . TYR C 2 342 ? 163.682 119.118 103.854 1.00 18.12 ?  321 TYR C CD1   1 
ATOM   13467 C  CD2   . TYR C 2 342 ? 164.770 121.048 102.988 1.00 16.03 ?  321 TYR C CD2   1 
ATOM   13468 C  CE1   . TYR C 2 342 ? 164.445 119.201 105.003 1.00 15.48 ?  321 TYR C CE1   1 
ATOM   13469 C  CE2   . TYR C 2 342 ? 165.534 121.138 104.133 1.00 17.80 ?  321 TYR C CE2   1 
ATOM   13470 C  CZ    . TYR C 2 342 ? 165.368 120.213 105.137 1.00 19.62 ?  321 TYR C CZ    1 
ATOM   13471 O  OH    . TYR C 2 342 ? 166.129 120.299 106.280 1.00 28.71 ?  321 TYR C OH    1 
ATOM   13472 N  N     . PHE C 2 343 ? 160.663 120.781 99.503  1.00 7.71  ?  322 PHE C N     1 
ATOM   13473 C  CA    . PHE C 2 343 ? 159.813 120.545 98.344  1.00 20.35 ?  322 PHE C CA    1 
ATOM   13474 C  C     . PHE C 2 343 ? 160.564 120.830 97.049  1.00 25.47 ?  322 PHE C C     1 
ATOM   13475 O  O     . PHE C 2 343 ? 161.541 121.578 97.035  1.00 26.11 ?  322 PHE C O     1 
ATOM   13476 C  CB    . PHE C 2 343 ? 158.555 121.412 98.434  1.00 15.28 ?  322 PHE C CB    1 
ATOM   13477 C  CG    . PHE C 2 343 ? 157.784 121.223 99.708  1.00 13.74 ?  322 PHE C CG    1 
ATOM   13478 C  CD1   . PHE C 2 343 ? 156.882 120.184 99.840  1.00 17.31 ?  322 PHE C CD1   1 
ATOM   13479 C  CD2   . PHE C 2 343 ? 157.977 122.075 100.780 1.00 4.75  ?  322 PHE C CD2   1 
ATOM   13480 C  CE1   . PHE C 2 343 ? 156.179 120.006 101.013 1.00 16.31 ?  322 PHE C CE1   1 
ATOM   13481 C  CE2   . PHE C 2 343 ? 157.280 121.900 101.954 1.00 5.64  ?  322 PHE C CE2   1 
ATOM   13482 C  CZ    . PHE C 2 343 ? 156.378 120.865 102.071 1.00 10.19 ?  322 PHE C CZ    1 
ATOM   13483 N  N     . ASP D 2 37  ? 121.304 99.861  147.151 1.00 32.44 ?  16  ASP D N     1 
ATOM   13484 C  CA    . ASP D 2 37  ? 121.251 101.288 146.818 1.00 32.83 ?  16  ASP D CA    1 
ATOM   13485 C  C     . ASP D 2 37  ? 122.004 101.658 145.542 1.00 31.65 ?  16  ASP D C     1 
ATOM   13486 O  O     . ASP D 2 37  ? 121.935 102.809 145.104 1.00 32.65 ?  16  ASP D O     1 
ATOM   13487 C  CB    . ASP D 2 37  ? 121.833 102.134 147.961 1.00 33.73 ?  16  ASP D CB    1 
ATOM   13488 C  CG    . ASP D 2 37  ? 121.017 102.056 149.242 1.00 36.81 ?  16  ASP D CG    1 
ATOM   13489 O  OD1   . ASP D 2 37  ? 121.581 102.399 150.309 1.00 39.69 ?  16  ASP D OD1   1 
ATOM   13490 O  OD2   . ASP D 2 37  ? 119.832 101.654 149.195 1.00 39.67 -1 16  ASP D OD2   1 
ATOM   13491 N  N     . PHE D 2 38  ? 122.723 100.708 144.946 1.00 29.55 ?  17  PHE D N     1 
ATOM   13492 C  CA    . PHE D 2 38  ? 123.721 101.075 143.941 1.00 27.75 ?  17  PHE D CA    1 
ATOM   13493 C  C     . PHE D 2 38  ? 123.829 100.188 142.690 1.00 26.21 ?  17  PHE D C     1 
ATOM   13494 O  O     . PHE D 2 38  ? 124.375 100.622 141.682 1.00 25.93 ?  17  PHE D O     1 
ATOM   13495 C  CB    . PHE D 2 38  ? 125.102 101.220 144.618 1.00 27.37 ?  17  PHE D CB    1 
ATOM   13496 C  CG    . PHE D 2 38  ? 125.578 99.961  145.295 1.00 27.32 ?  17  PHE D CG    1 
ATOM   13497 C  CD1   . PHE D 2 38  ? 126.235 98.973  144.569 1.00 27.01 ?  17  PHE D CD1   1 
ATOM   13498 C  CD2   . PHE D 2 38  ? 125.368 99.762  146.654 1.00 28.02 ?  17  PHE D CD2   1 
ATOM   13499 C  CE1   . PHE D 2 38  ? 126.671 97.803  145.188 1.00 27.66 ?  17  PHE D CE1   1 
ATOM   13500 C  CE2   . PHE D 2 38  ? 125.796 98.595  147.275 1.00 27.68 ?  17  PHE D CE2   1 
ATOM   13501 C  CZ    . PHE D 2 38  ? 126.450 97.613  146.539 1.00 27.47 ?  17  PHE D CZ    1 
ATOM   13502 N  N     . THR D 2 39  ? 123.321 98.961  142.751 1.00 24.88 ?  18  THR D N     1 
ATOM   13503 C  CA    . THR D 2 39  ? 123.540 97.987  141.669 1.00 23.81 ?  18  THR D CA    1 
ATOM   13504 C  C     . THR D 2 39  ? 122.922 98.388  140.318 1.00 23.56 ?  18  THR D C     1 
ATOM   13505 O  O     . THR D 2 39  ? 123.547 98.232  139.269 1.00 23.02 ?  18  THR D O     1 
ATOM   13506 C  CB    . THR D 2 39  ? 123.146 96.553  142.102 1.00 23.40 ?  18  THR D CB    1 
ATOM   13507 O  OG1   . THR D 2 39  ? 124.186 96.013  142.926 1.00 23.77 ?  18  THR D OG1   1 
ATOM   13508 C  CG2   . THR D 2 39  ? 122.969 95.634  140.904 1.00 22.31 ?  18  THR D CG2   1 
ATOM   13509 N  N     . GLN D 2 40  ? 121.707 98.919  140.333 1.00 23.78 ?  19  GLN D N     1 
ATOM   13510 C  CA    . GLN D 2 40  ? 121.094 99.351  139.074 1.00 23.88 ?  19  GLN D CA    1 
ATOM   13511 C  C     . GLN D 2 40  ? 121.847 100.521 138.436 1.00 24.09 ?  19  GLN D C     1 
ATOM   13512 O  O     . GLN D 2 40  ? 122.058 100.541 137.231 1.00 23.15 ?  19  GLN D O     1 
ATOM   13513 C  CB    . GLN D 2 40  ? 119.606 99.659  139.250 1.00 24.53 ?  19  GLN D CB    1 
ATOM   13514 C  CG    . GLN D 2 40  ? 118.795 98.407  139.546 1.00 24.06 ?  19  GLN D CG    1 
ATOM   13515 C  CD    . GLN D 2 40  ? 117.317 98.573  139.284 1.00 25.83 ?  19  GLN D CD    1 
ATOM   13516 O  OE1   . GLN D 2 40  ? 116.894 99.543  138.659 1.00 25.90 ?  19  GLN D OE1   1 
ATOM   13517 N  NE2   . GLN D 2 40  ? 116.520 97.607  139.743 1.00 23.56 ?  19  GLN D NE2   1 
ATOM   13518 N  N     . MET D 2 41  ? 122.292 101.468 139.252 1.00 24.07 ?  20  MET D N     1 
ATOM   13519 C  CA    . MET D 2 41  ? 123.141 102.553 138.757 1.00 25.53 ?  20  MET D CA    1 
ATOM   13520 C  C     . MET D 2 41  ? 124.442 102.038 138.109 1.00 24.24 ?  20  MET D C     1 
ATOM   13521 O  O     . MET D 2 41  ? 124.837 102.510 137.039 1.00 23.16 ?  20  MET D O     1 
ATOM   13522 C  CB    . MET D 2 41  ? 123.444 103.540 139.889 1.00 26.79 ?  20  MET D CB    1 
ATOM   13523 C  CG    . MET D 2 41  ? 124.343 104.698 139.503 1.00 32.62 ?  20  MET D CG    1 
ATOM   13524 S  SD    . MET D 2 41  ? 124.887 105.580 140.985 1.00 44.01 ?  20  MET D SD    1 
ATOM   13525 C  CE    . MET D 2 41  ? 126.417 106.320 140.406 1.00 41.93 ?  20  MET D CE    1 
ATOM   13526 N  N     . PHE D 2 42  ? 125.097 101.064 138.745 1.00 23.31 ?  21  PHE D N     1 
ATOM   13527 C  CA    . PHE D 2 42  ? 126.323 100.501 138.178 1.00 23.44 ?  21  PHE D CA    1 
ATOM   13528 C  C     . PHE D 2 42  ? 126.049 99.663  136.945 1.00 23.55 ?  21  PHE D C     1 
ATOM   13529 O  O     . PHE D 2 42  ? 126.856 99.641  136.023 1.00 23.74 ?  21  PHE D O     1 
ATOM   13530 C  CB    . PHE D 2 42  ? 127.116 99.707  139.218 1.00 22.97 ?  21  PHE D CB    1 
ATOM   13531 C  CG    . PHE D 2 42  ? 128.026 100.563 140.027 1.00 23.86 ?  21  PHE D CG    1 
ATOM   13532 C  CD1   . PHE D 2 42  ? 129.363 100.710 139.670 1.00 24.55 ?  21  PHE D CD1   1 
ATOM   13533 C  CD2   . PHE D 2 42  ? 127.544 101.261 141.119 1.00 24.06 ?  21  PHE D CD2   1 
ATOM   13534 C  CE1   . PHE D 2 42  ? 130.214 101.529 140.416 1.00 25.78 ?  21  PHE D CE1   1 
ATOM   13535 C  CE2   . PHE D 2 42  ? 128.388 102.084 141.870 1.00 25.25 ?  21  PHE D CE2   1 
ATOM   13536 C  CZ    . PHE D 2 42  ? 129.714 102.221 141.518 1.00 25.79 ?  21  PHE D CZ    1 
ATOM   13537 N  N     . TYR D 2 43  ? 124.899 98.992  136.932 1.00 24.08 ?  22  TYR D N     1 
ATOM   13538 C  CA    . TYR D 2 43  ? 124.454 98.275  135.749 1.00 24.74 ?  22  TYR D CA    1 
ATOM   13539 C  C     . TYR D 2 43  ? 124.438 99.228  134.552 1.00 25.72 ?  22  TYR D C     1 
ATOM   13540 O  O     . TYR D 2 43  ? 125.003 98.925  133.496 1.00 25.56 ?  22  TYR D O     1 
ATOM   13541 C  CB    . TYR D 2 43  ? 123.066 97.644  135.948 1.00 24.90 ?  22  TYR D CB    1 
ATOM   13542 C  CG    . TYR D 2 43  ? 122.527 97.042  134.658 1.00 24.38 ?  22  TYR D CG    1 
ATOM   13543 C  CD1   . TYR D 2 43  ? 122.799 95.723  134.320 1.00 23.96 ?  22  TYR D CD1   1 
ATOM   13544 C  CD2   . TYR D 2 43  ? 121.796 97.818  133.754 1.00 24.73 ?  22  TYR D CD2   1 
ATOM   13545 C  CE1   . TYR D 2 43  ? 122.337 95.177  133.120 1.00 23.42 ?  22  TYR D CE1   1 
ATOM   13546 C  CE2   . TYR D 2 43  ? 121.316 97.282  132.557 1.00 26.65 ?  22  TYR D CE2   1 
ATOM   13547 C  CZ    . TYR D 2 43  ? 121.596 95.962  132.250 1.00 25.68 ?  22  TYR D CZ    1 
ATOM   13548 O  OH    . TYR D 2 43  ? 121.128 95.430  131.070 1.00 26.57 ?  22  TYR D OH    1 
ATOM   13549 N  N     . ASN D 2 44  ? 123.782 100.372 134.732 1.00 26.77 ?  23  ASN D N     1 
ATOM   13550 C  CA    . ASN D 2 44  ? 123.656 101.376 133.682 1.00 28.57 ?  23  ASN D CA    1 
ATOM   13551 C  C     . ASN D 2 44  ? 125.003 101.864 133.182 1.00 28.70 ?  23  ASN D C     1 
ATOM   13552 O  O     . ASN D 2 44  ? 125.261 101.840 131.976 1.00 28.99 ?  23  ASN D O     1 
ATOM   13553 C  CB    . ASN D 2 44  ? 122.778 102.538 134.154 1.00 29.62 ?  23  ASN D CB    1 
ATOM   13554 C  CG    . ASN D 2 44  ? 121.316 102.135 134.300 1.00 32.44 ?  23  ASN D CG    1 
ATOM   13555 O  OD1   . ASN D 2 44  ? 120.864 101.155 133.693 1.00 34.30 ?  23  ASN D OD1   1 
ATOM   13556 N  ND2   . ASN D 2 44  ? 120.568 102.883 135.107 1.00 35.17 ?  23  ASN D ND2   1 
ATOM   13557 N  N     . GLN D 2 45  ? 125.869 102.259 134.112 1.00 28.97 ?  24  GLN D N     1 
ATOM   13558 C  CA    . GLN D 2 45  ? 127.191 102.761 133.759 1.00 29.99 ?  24  GLN D CA    1 
ATOM   13559 C  C     . GLN D 2 45  ? 128.050 101.702 133.052 1.00 29.69 ?  24  GLN D C     1 
ATOM   13560 O  O     . GLN D 2 45  ? 128.758 102.015 132.096 1.00 30.01 ?  24  GLN D O     1 
ATOM   13561 C  CB    . GLN D 2 45  ? 127.913 103.325 134.990 1.00 30.27 ?  24  GLN D CB    1 
ATOM   13562 C  CG    . GLN D 2 45  ? 129.217 104.084 134.655 1.00 32.29 ?  24  GLN D CG    1 
ATOM   13563 C  CD    . GLN D 2 45  ? 128.989 105.322 133.797 1.00 35.95 ?  24  GLN D CD    1 
ATOM   13564 O  OE1   . GLN D 2 45  ? 127.922 105.941 133.841 1.00 36.72 ?  24  GLN D OE1   1 
ATOM   13565 N  NE2   . GLN D 2 45  ? 129.996 105.690 133.011 1.00 37.05 ?  24  GLN D NE2   1 
ATOM   13566 N  N     . ASN D 2 46  ? 127.962 100.452 133.505 1.00 28.93 ?  25  ASN D N     1 
ATOM   13567 C  CA    . ASN D 2 46  ? 128.686 99.361  132.874 1.00 28.70 ?  25  ASN D CA    1 
ATOM   13568 C  C     . ASN D 2 46  ? 128.267 99.101  131.433 1.00 29.05 ?  25  ASN D C     1 
ATOM   13569 O  O     . ASN D 2 46  ? 129.118 99.053  130.540 1.00 28.51 ?  25  ASN D O     1 
ATOM   13570 C  CB    . ASN D 2 46  ? 128.582 98.072  133.700 1.00 28.36 ?  25  ASN D CB    1 
ATOM   13571 C  CG    . ASN D 2 46  ? 129.661 97.976  134.757 1.00 28.45 ?  25  ASN D CG    1 
ATOM   13572 O  OD1   . ASN D 2 46  ? 130.687 97.337  134.537 1.00 28.03 ?  25  ASN D OD1   1 
ATOM   13573 N  ND2   . ASN D 2 46  ? 129.450 98.633  135.896 1.00 26.53 ?  25  ASN D ND2   1 
ATOM   13574 N  N     . VAL D 2 47  ? 126.962 98.959  131.203 1.00 29.66 ?  26  VAL D N     1 
ATOM   13575 C  CA    . VAL D 2 47  ? 126.473 98.593  129.873 1.00 31.15 ?  26  VAL D CA    1 
ATOM   13576 C  C     . VAL D 2 47  ? 126.627 99.742  128.879 1.00 32.39 ?  26  VAL D C     1 
ATOM   13577 O  O     . VAL D 2 47  ? 126.828 99.511  127.688 1.00 32.80 ?  26  VAL D O     1 
ATOM   13578 C  CB    . VAL D 2 47  ? 125.017 98.019  129.870 1.00 31.08 ?  26  VAL D CB    1 
ATOM   13579 C  CG1   . VAL D 2 47  ? 124.907 96.821  130.806 1.00 31.09 ?  26  VAL D CG1   1 
ATOM   13580 C  CG2   . VAL D 2 47  ? 123.975 99.092  130.213 1.00 30.81 ?  26  VAL D CG2   1 
ATOM   13581 N  N     . LYS D 2 48  ? 126.566 100.977 129.362 1.00 33.28 ?  27  LYS D N     1 
ATOM   13582 C  CA    . LYS D 2 48  ? 126.755 102.098 128.455 1.00 34.87 ?  27  LYS D CA    1 
ATOM   13583 C  C     . LYS D 2 48  ? 128.231 102.336 128.073 1.00 34.91 ?  27  LYS D C     1 
ATOM   13584 O  O     . LYS D 2 48  ? 128.517 103.082 127.140 1.00 34.92 ?  27  LYS D O     1 
ATOM   13585 C  CB    . LYS D 2 48  ? 126.051 103.363 128.968 1.00 35.45 ?  27  LYS D CB    1 
ATOM   13586 C  CG    . LYS D 2 48  ? 126.828 104.218 129.943 1.00 37.41 ?  27  LYS D CG    1 
ATOM   13587 C  CD    . LYS D 2 48  ? 126.176 105.606 130.050 1.00 40.91 ?  27  LYS D CD    1 
ATOM   13588 C  CE    . LYS D 2 48  ? 127.130 106.615 130.695 1.00 42.46 ?  27  LYS D CE    1 
ATOM   13589 N  NZ    . LYS D 2 48  ? 126.598 108.010 130.679 1.00 45.13 1  27  LYS D NZ    1 
ATOM   13590 N  N     . GLN D 2 49  ? 129.147 101.677 128.787 1.00 34.66 ?  28  GLN D N     1 
ATOM   13591 C  CA    . GLN D 2 49  ? 130.577 101.728 128.493 1.00 34.64 ?  28  GLN D CA    1 
ATOM   13592 C  C     . GLN D 2 49  ? 131.009 100.577 127.586 1.00 34.20 ?  28  GLN D C     1 
ATOM   13593 O  O     . GLN D 2 49  ? 132.207 100.385 127.369 1.00 34.53 ?  28  GLN D O     1 
ATOM   13594 C  CB    . GLN D 2 49  ? 131.405 101.683 129.793 1.00 34.89 ?  28  GLN D CB    1 
ATOM   13595 C  CG    . GLN D 2 49  ? 131.659 103.041 130.444 1.00 36.47 ?  28  GLN D CG    1 
ATOM   13596 C  CD    . GLN D 2 49  ? 132.311 102.943 131.826 1.00 38.37 ?  28  GLN D CD    1 
ATOM   13597 O  OE1   . GLN D 2 49  ? 132.070 103.788 132.688 1.00 40.68 ?  28  GLN D OE1   1 
ATOM   13598 N  NE2   . GLN D 2 49  ? 133.133 101.916 132.041 1.00 38.57 ?  28  GLN D NE2   1 
ATOM   13599 N  N     . PHE D 2 50  ? 130.053 99.808  127.065 1.00 33.42 ?  29  PHE D N     1 
ATOM   13600 C  CA    . PHE D 2 50  ? 130.388 98.637  126.256 1.00 32.57 ?  29  PHE D CA    1 
ATOM   13601 C  C     . PHE D 2 50  ? 131.153 99.057  125.001 1.00 32.60 ?  29  PHE D C     1 
ATOM   13602 O  O     . PHE D 2 50  ? 130.825 100.064 124.366 1.00 32.39 ?  29  PHE D O     1 
ATOM   13603 C  CB    . PHE D 2 50  ? 129.142 97.811  125.896 1.00 32.77 ?  29  PHE D CB    1 
ATOM   13604 C  CG    . PHE D 2 50  ? 129.444 96.566  125.086 1.00 32.24 ?  29  PHE D CG    1 
ATOM   13605 C  CD1   . PHE D 2 50  ? 129.998 95.440  125.687 1.00 31.50 ?  29  PHE D CD1   1 
ATOM   13606 C  CD2   . PHE D 2 50  ? 129.175 96.526  123.723 1.00 33.60 ?  29  PHE D CD2   1 
ATOM   13607 C  CE1   . PHE D 2 50  ? 130.279 94.300  124.951 1.00 33.02 ?  29  PHE D CE1   1 
ATOM   13608 C  CE2   . PHE D 2 50  ? 129.456 95.385  122.968 1.00 33.78 ?  29  PHE D CE2   1 
ATOM   13609 C  CZ    . PHE D 2 50  ? 130.001 94.269  123.583 1.00 33.13 ?  29  PHE D CZ    1 
ATOM   13610 N  N     . TRP D 2 51  ? 132.176 98.283  124.663 1.00 31.95 ?  30  TRP D N     1 
ATOM   13611 C  CA    . TRP D 2 51  ? 133.016 98.552  123.495 1.00 32.03 ?  30  TRP D CA    1 
ATOM   13612 C  C     . TRP D 2 51  ? 133.625 97.247  123.001 1.00 33.03 ?  30  TRP D C     1 
ATOM   13613 O  O     . TRP D 2 51  ? 133.564 96.224  123.687 1.00 32.54 ?  30  TRP D O     1 
ATOM   13614 C  CB    . TRP D 2 51  ? 134.106 99.586  123.819 1.00 31.19 ?  30  TRP D CB    1 
ATOM   13615 C  CG    . TRP D 2 51  ? 135.066 99.151  124.908 1.00 28.11 ?  30  TRP D CG    1 
ATOM   13616 C  CD1   . TRP D 2 51  ? 134.844 99.179  126.250 1.00 26.51 ?  30  TRP D CD1   1 
ATOM   13617 C  CD2   . TRP D 2 51  ? 136.389 98.619  124.731 1.00 25.93 ?  30  TRP D CD2   1 
ATOM   13618 N  NE1   . TRP D 2 51  ? 135.949 98.704  126.927 1.00 24.52 ?  30  TRP D NE1   1 
ATOM   13619 C  CE2   . TRP D 2 51  ? 136.908 98.351  126.019 1.00 24.42 ?  30  TRP D CE2   1 
ATOM   13620 C  CE3   . TRP D 2 51  ? 137.189 98.349  123.611 1.00 25.37 ?  30  TRP D CE3   1 
ATOM   13621 C  CZ2   . TRP D 2 51  ? 138.194 97.830  126.220 1.00 24.00 ?  30  TRP D CZ2   1 
ATOM   13622 C  CZ3   . TRP D 2 51  ? 138.466 97.822  123.811 1.00 24.99 ?  30  TRP D CZ3   1 
ATOM   13623 C  CH2   . TRP D 2 51  ? 138.953 97.568  125.105 1.00 23.72 ?  30  TRP D CH2   1 
ATOM   13624 N  N     . LEU D 2 52  ? 134.194 97.291  121.800 1.00 34.81 ?  31  LEU D N     1 
ATOM   13625 C  CA    . LEU D 2 52  ? 134.802 96.129  121.171 1.00 36.58 ?  31  LEU D CA    1 
ATOM   13626 C  C     . LEU D 2 52  ? 136.174 96.497  120.611 1.00 37.80 ?  31  LEU D C     1 
ATOM   13627 O  O     . LEU D 2 52  ? 136.374 97.627  120.174 1.00 37.92 ?  31  LEU D O     1 
ATOM   13628 C  CB    . LEU D 2 52  ? 133.893 95.582  120.059 1.00 36.95 ?  31  LEU D CB    1 
ATOM   13629 C  CG    . LEU D 2 52  ? 132.712 94.683  120.440 1.00 38.15 ?  31  LEU D CG    1 
ATOM   13630 C  CD1   . LEU D 2 52  ? 132.167 93.978  119.203 1.00 39.50 ?  31  LEU D CD1   1 
ATOM   13631 C  CD2   . LEU D 2 52  ? 133.097 93.646  121.489 1.00 37.94 ?  31  LEU D CD2   1 
ATOM   13632 N  N     . PRO D 2 53  ? 137.125 95.541  120.615 1.00 39.26 ?  32  PRO D N     1 
ATOM   13633 C  CA    . PRO D 2 53  ? 138.492 95.783  120.119 1.00 40.41 ?  32  PRO D CA    1 
ATOM   13634 C  C     . PRO D 2 53  ? 138.540 96.331  118.686 1.00 41.91 ?  32  PRO D C     1 
ATOM   13635 O  O     . PRO D 2 53  ? 139.285 97.277  118.409 1.00 42.52 ?  32  PRO D O     1 
ATOM   13636 C  CB    . PRO D 2 53  ? 139.130 94.389  120.158 1.00 40.42 ?  32  PRO D CB    1 
ATOM   13637 C  CG    . PRO D 2 53  ? 138.318 93.617  121.118 1.00 40.01 ?  32  PRO D CG    1 
ATOM   13638 C  CD    . PRO D 2 53  ? 136.929 94.141  121.029 1.00 39.30 ?  32  PRO D CD    1 
ATOM   13639 N  N     . GLU D 2 54  ? 137.735 95.749  117.801 1.00 43.27 ?  33  GLU D N     1 
ATOM   13640 C  CA    . GLU D 2 54  ? 137.680 96.117  116.377 1.00 45.17 ?  33  GLU D CA    1 
ATOM   13641 C  C     . GLU D 2 54  ? 137.448 97.610  116.091 1.00 45.57 ?  33  GLU D C     1 
ATOM   13642 O  O     . GLU D 2 54  ? 137.769 98.092  115.000 1.00 46.08 ?  33  GLU D O     1 
ATOM   13643 C  CB    . GLU D 2 54  ? 136.601 95.286  115.665 1.00 45.55 ?  33  GLU D CB    1 
ATOM   13644 C  CG    . GLU D 2 54  ? 137.036 93.876  115.261 1.00 48.19 ?  33  GLU D CG    1 
ATOM   13645 C  CD    . GLU D 2 54  ? 137.380 92.979  116.443 1.00 50.61 ?  33  GLU D CD    1 
ATOM   13646 O  OE1   . GLU D 2 54  ? 136.587 92.926  117.412 1.00 51.10 ?  33  GLU D OE1   1 
ATOM   13647 O  OE2   . GLU D 2 54  ? 138.452 92.329  116.397 1.00 52.64 -1 33  GLU D OE2   1 
ATOM   13648 N  N     . GLU D 2 55  ? 136.895 98.329  117.067 1.00 45.74 ?  34  GLU D N     1 
ATOM   13649 C  CA    . GLU D 2 55  ? 136.563 99.750  116.908 1.00 46.28 ?  34  GLU D CA    1 
ATOM   13650 C  C     . GLU D 2 55  ? 137.796 100.646 116.740 1.00 46.49 ?  34  GLU D C     1 
ATOM   13651 O  O     . GLU D 2 55  ? 137.729 101.686 116.077 1.00 46.73 ?  34  GLU D O     1 
ATOM   13652 C  CB    . GLU D 2 55  ? 135.707 100.245 118.079 1.00 46.17 ?  34  GLU D CB    1 
ATOM   13653 C  CG    . GLU D 2 55  ? 134.335 99.575  118.204 1.00 47.10 ?  34  GLU D CG    1 
ATOM   13654 C  CD    . GLU D 2 55  ? 133.510 100.152 119.352 1.00 48.43 ?  34  GLU D CD    1 
ATOM   13655 O  OE1   . GLU D 2 55  ? 133.170 101.355 119.302 1.00 49.62 ?  34  GLU D OE1   1 
ATOM   13656 O  OE2   . GLU D 2 55  ? 133.198 99.404  120.302 1.00 47.11 -1 34  GLU D OE2   1 
ATOM   13657 N  N     . ILE D 2 56  ? 138.913 100.244 117.345 1.00 46.23 ?  35  ILE D N     1 
ATOM   13658 C  CA    . ILE D 2 56  ? 140.165 100.988 117.236 1.00 46.25 ?  35  ILE D CA    1 
ATOM   13659 C  C     . ILE D 2 56  ? 141.091 100.283 116.247 1.00 46.30 ?  35  ILE D C     1 
ATOM   13660 O  O     . ILE D 2 56  ? 141.451 99.118  116.446 1.00 46.36 ?  35  ILE D O     1 
ATOM   13661 C  CB    . ILE D 2 56  ? 140.887 101.133 118.621 1.00 45.84 ?  35  ILE D CB    1 
ATOM   13662 C  CG1   . ILE D 2 56  ? 139.902 101.460 119.763 1.00 46.15 ?  35  ILE D CG1   1 
ATOM   13663 C  CG2   . ILE D 2 56  ? 142.054 102.138 118.541 1.00 45.72 ?  35  ILE D CG2   1 
ATOM   13664 C  CD1   . ILE D 2 56  ? 139.162 102.787 119.646 1.00 47.27 ?  35  ILE D CD1   1 
ATOM   13665 N  N     . ALA D 2 57  ? 141.465 100.981 115.179 1.00 46.51 ?  36  ALA D N     1 
ATOM   13666 C  CA    . ALA D 2 57  ? 142.451 100.464 114.225 1.00 46.56 ?  36  ALA D CA    1 
ATOM   13667 C  C     . ALA D 2 57  ? 143.852 100.597 114.827 1.00 46.08 ?  36  ALA D C     1 
ATOM   13668 O  O     . ALA D 2 57  ? 144.246 101.688 115.238 1.00 45.70 ?  36  ALA D O     1 
ATOM   13669 C  CB    . ALA D 2 57  ? 142.359 101.211 112.897 1.00 47.10 ?  36  ALA D CB    1 
ATOM   13670 N  N     . LEU D 2 58  ? 144.599 99.495  114.865 1.00 45.66 ?  37  LEU D N     1 
ATOM   13671 C  CA    . LEU D 2 58  ? 145.895 99.469  115.560 1.00 45.27 ?  37  LEU D CA    1 
ATOM   13672 C  C     . LEU D 2 58  ? 147.135 99.714  114.702 1.00 45.25 ?  37  LEU D C     1 
ATOM   13673 O  O     . LEU D 2 58  ? 148.187 100.094 115.226 1.00 44.82 ?  37  LEU D O     1 
ATOM   13674 C  CB    . LEU D 2 58  ? 146.061 98.160  116.331 1.00 45.05 ?  37  LEU D CB    1 
ATOM   13675 C  CG    . LEU D 2 58  ? 145.307 98.100  117.657 1.00 45.41 ?  37  LEU D CG    1 
ATOM   13676 C  CD1   . LEU D 2 58  ? 145.492 96.736  118.294 1.00 45.40 ?  37  LEU D CD1   1 
ATOM   13677 C  CD2   . LEU D 2 58  ? 145.773 99.208  118.600 1.00 44.70 ?  37  LEU D CD2   1 
ATOM   13678 N  N     . ASN D 2 59  ? 147.013 99.513  113.392 1.00 45.33 ?  38  ASN D N     1 
ATOM   13679 C  CA    . ASN D 2 59  ? 148.186 99.491  112.513 1.00 45.22 ?  38  ASN D CA    1 
ATOM   13680 C  C     . ASN D 2 59  ? 149.037 100.768 112.506 1.00 44.39 ?  38  ASN D C     1 
ATOM   13681 O  O     . ASN D 2 59  ? 150.262 100.695 112.351 1.00 44.33 ?  38  ASN D O     1 
ATOM   13682 C  CB    . ASN D 2 59  ? 147.779 99.101  111.094 1.00 46.22 ?  38  ASN D CB    1 
ATOM   13683 C  CG    . ASN D 2 59  ? 148.833 98.258  110.399 1.00 47.90 ?  38  ASN D CG    1 
ATOM   13684 O  OD1   . ASN D 2 59  ? 149.393 98.660  109.379 1.00 49.28 ?  38  ASN D OD1   1 
ATOM   13685 N  ND2   . ASN D 2 59  ? 149.109 97.075  110.951 1.00 49.18 ?  38  ASN D ND2   1 
ATOM   13686 N  N     . GLY D 2 60  ? 148.393 101.921 112.697 1.00 43.45 ?  39  GLY D N     1 
ATOM   13687 C  CA    . GLY D 2 60  ? 149.079 103.217 112.731 1.00 42.42 ?  39  GLY D CA    1 
ATOM   13688 C  C     . GLY D 2 60  ? 150.039 103.437 113.897 1.00 41.55 ?  39  GLY D C     1 
ATOM   13689 O  O     . GLY D 2 60  ? 150.765 104.435 113.933 1.00 41.29 ?  39  GLY D O     1 
ATOM   13690 N  N     . ASP D 2 61  ? 150.042 102.515 114.858 1.00 40.35 ?  40  ASP D N     1 
ATOM   13691 C  CA    . ASP D 2 61  ? 151.005 102.561 115.965 1.00 39.53 ?  40  ASP D CA    1 
ATOM   13692 C  C     . ASP D 2 61  ? 152.426 102.221 115.536 1.00 39.38 ?  40  ASP D C     1 
ATOM   13693 O  O     . ASP D 2 61  ? 153.389 102.619 116.188 1.00 38.90 ?  40  ASP D O     1 
ATOM   13694 C  CB    . ASP D 2 61  ? 150.582 101.617 117.080 1.00 38.93 ?  40  ASP D CB    1 
ATOM   13695 C  CG    . ASP D 2 61  ? 149.608 102.249 118.033 1.00 38.21 ?  40  ASP D CG    1 
ATOM   13696 O  OD1   . ASP D 2 61  ? 149.262 103.438 117.855 1.00 38.79 ?  40  ASP D OD1   1 
ATOM   13697 O  OD2   . ASP D 2 61  ? 149.193 101.552 118.973 1.00 38.02 -1 40  ASP D OD2   1 
ATOM   13698 N  N     . LEU D 2 62  ? 152.547 101.482 114.437 1.00 39.82 ?  41  LEU D N     1 
ATOM   13699 C  CA    . LEU D 2 62  ? 153.844 101.067 113.918 1.00 40.22 ?  41  LEU D CA    1 
ATOM   13700 C  C     . LEU D 2 62  ? 154.692 102.265 113.489 1.00 40.40 ?  41  LEU D C     1 
ATOM   13701 O  O     . LEU D 2 62  ? 155.916 102.161 113.401 1.00 40.91 ?  41  LEU D O     1 
ATOM   13702 C  CB    . LEU D 2 62  ? 153.658 100.077 112.764 1.00 40.52 ?  41  LEU D CB    1 
ATOM   13703 C  CG    . LEU D 2 62  ? 153.029 98.727  113.130 1.00 41.03 ?  41  LEU D CG    1 
ATOM   13704 C  CD1   . LEU D 2 62  ? 152.812 97.882  111.882 1.00 42.53 ?  41  LEU D CD1   1 
ATOM   13705 C  CD2   . LEU D 2 62  ? 153.875 97.973  114.164 1.00 41.89 ?  41  LEU D CD2   1 
ATOM   13706 N  N     . LEU D 2 63  ? 154.027 103.399 113.251 1.00 40.20 ?  42  LEU D N     1 
ATOM   13707 C  CA    . LEU D 2 63  ? 154.670 104.651 112.854 1.00 39.85 ?  42  LEU D CA    1 
ATOM   13708 C  C     . LEU D 2 63  ? 155.368 105.376 114.020 1.00 38.90 ?  42  LEU D C     1 
ATOM   13709 O  O     . LEU D 2 63  ? 156.182 106.281 113.801 1.00 39.48 ?  42  LEU D O     1 
ATOM   13710 C  CB    . LEU D 2 63  ? 153.633 105.567 112.185 1.00 40.50 ?  42  LEU D CB    1 
ATOM   13711 C  CG    . LEU D 2 63  ? 152.957 105.203 110.853 1.00 41.98 ?  42  LEU D CG    1 
ATOM   13712 C  CD1   . LEU D 2 63  ? 151.864 106.191 110.463 1.00 43.07 ?  42  LEU D CD1   1 
ATOM   13713 C  CD2   . LEU D 2 63  ? 154.004 105.153 109.753 1.00 43.17 ?  42  LEU D CD2   1 
ATOM   13714 N  N     . THR D 2 64  ? 155.049 105.000 115.257 1.00 37.28 ?  43  THR D N     1 
ATOM   13715 C  CA    . THR D 2 64  ? 155.789 105.528 116.413 1.00 35.53 ?  43  THR D CA    1 
ATOM   13716 C  C     . THR D 2 64  ? 156.589 104.443 117.125 1.00 34.57 ?  43  THR D C     1 
ATOM   13717 O  O     . THR D 2 64  ? 157.630 104.723 117.723 1.00 34.23 ?  43  THR D O     1 
ATOM   13718 C  CB    . THR D 2 64  ? 154.899 106.285 117.423 1.00 35.18 ?  43  THR D CB    1 
ATOM   13719 O  OG1   . THR D 2 64  ? 153.734 105.515 117.737 1.00 34.59 ?  43  THR D OG1   1 
ATOM   13720 C  CG2   . THR D 2 64  ? 154.480 107.615 116.861 1.00 35.48 ?  43  THR D CG2   1 
ATOM   13721 N  N     . TRP D 2 65  ? 156.095 103.207 117.043 1.00 33.62 ?  44  TRP D N     1 
ATOM   13722 C  CA    . TRP D 2 65  ? 156.757 102.037 117.641 1.00 32.87 ?  44  TRP D CA    1 
ATOM   13723 C  C     . TRP D 2 65  ? 158.188 101.858 117.116 1.00 33.46 ?  44  TRP D C     1 
ATOM   13724 O  O     . TRP D 2 65  ? 159.112 101.600 117.889 1.00 32.58 ?  44  TRP D O     1 
ATOM   13725 C  CB    . TRP D 2 65  ? 155.925 100.773 117.373 1.00 32.09 ?  44  TRP D CB    1 
ATOM   13726 C  CG    . TRP D 2 65  ? 156.531 99.495  117.880 1.00 30.42 ?  44  TRP D CG    1 
ATOM   13727 C  CD1   . TRP D 2 65  ? 157.114 98.513  117.128 1.00 29.35 ?  44  TRP D CD1   1 
ATOM   13728 C  CD2   . TRP D 2 65  ? 156.609 99.054  119.245 1.00 28.04 ?  44  TRP D CD2   1 
ATOM   13729 N  NE1   . TRP D 2 65  ? 157.549 97.490  117.938 1.00 28.44 ?  44  TRP D NE1   1 
ATOM   13730 C  CE2   . TRP D 2 65  ? 157.255 97.798  119.241 1.00 28.14 ?  44  TRP D CE2   1 
ATOM   13731 C  CE3   . TRP D 2 65  ? 156.203 99.602  120.470 1.00 27.11 ?  44  TRP D CE3   1 
ATOM   13732 C  CZ2   . TRP D 2 65  ? 157.500 97.071  120.415 1.00 27.21 ?  44  TRP D CZ2   1 
ATOM   13733 C  CZ3   . TRP D 2 65  ? 156.439 98.874  121.640 1.00 27.45 ?  44  TRP D CZ3   1 
ATOM   13734 C  CH2   . TRP D 2 65  ? 157.078 97.619  121.598 1.00 27.25 ?  44  TRP D CH2   1 
ATOM   13735 N  N     . LYS D 2 66  ? 158.347 102.007 115.802 1.00 34.52 ?  45  LYS D N     1 
ATOM   13736 C  CA    . LYS D 2 66  ? 159.642 101.893 115.137 1.00 36.41 ?  45  LYS D CA    1 
ATOM   13737 C  C     . LYS D 2 66  ? 160.679 102.906 115.618 1.00 36.26 ?  45  LYS D C     1 
ATOM   13738 O  O     . LYS D 2 66  ? 161.878 102.685 115.449 1.00 36.52 ?  45  LYS D O     1 
ATOM   13739 C  CB    . LYS D 2 66  ? 159.476 101.995 113.615 1.00 36.98 ?  45  LYS D CB    1 
ATOM   13740 C  CG    . LYS D 2 66  ? 159.535 100.652 112.892 1.00 40.03 ?  45  LYS D CG    1 
ATOM   13741 C  CD    . LYS D 2 66  ? 158.302 99.782  113.164 1.00 43.70 ?  45  LYS D CD    1 
ATOM   13742 C  CE    . LYS D 2 66  ? 158.363 98.467  112.381 1.00 45.57 ?  45  LYS D CE    1 
ATOM   13743 N  NZ    . LYS D 2 66  ? 158.380 98.673  110.903 1.00 46.59 1  45  LYS D NZ    1 
ATOM   13744 N  N     . TYR D 2 67  ? 160.219 103.996 116.226 1.00 36.26 ?  46  TYR D N     1 
ATOM   13745 C  CA    . TYR D 2 67  ? 161.132 105.040 116.702 1.00 36.90 ?  46  TYR D CA    1 
ATOM   13746 C  C     . TYR D 2 67  ? 161.526 104.932 118.177 1.00 36.28 ?  46  TYR D C     1 
ATOM   13747 O  O     . TYR D 2 67  ? 162.306 105.746 118.662 1.00 36.44 ?  46  TYR D O     1 
ATOM   13748 C  CB    . TYR D 2 67  ? 160.590 106.439 116.389 1.00 37.15 ?  46  TYR D CB    1 
ATOM   13749 C  CG    . TYR D 2 67  ? 160.322 106.669 114.920 1.00 39.40 ?  46  TYR D CG    1 
ATOM   13750 C  CD1   . TYR D 2 67  ? 161.232 106.244 113.948 1.00 41.26 ?  46  TYR D CD1   1 
ATOM   13751 C  CD2   . TYR D 2 67  ? 159.174 107.333 114.500 1.00 41.06 ?  46  TYR D CD2   1 
ATOM   13752 C  CE1   . TYR D 2 67  ? 160.989 106.451 112.591 1.00 43.03 ?  46  TYR D CE1   1 
ATOM   13753 C  CE2   . TYR D 2 67  ? 158.924 107.554 113.144 1.00 43.05 ?  46  TYR D CE2   1 
ATOM   13754 C  CZ    . TYR D 2 67  ? 159.833 107.112 112.196 1.00 43.80 ?  46  TYR D CZ    1 
ATOM   13755 O  OH    . TYR D 2 67  ? 159.581 107.327 110.853 1.00 45.18 ?  46  TYR D OH    1 
ATOM   13756 N  N     . LEU D 2 68  ? 160.987 103.944 118.890 1.00 35.71 ?  47  LEU D N     1 
ATOM   13757 C  CA    . LEU D 2 68  ? 161.375 103.730 120.286 1.00 34.92 ?  47  LEU D CA    1 
ATOM   13758 C  C     . LEU D 2 68  ? 162.679 102.931 120.371 1.00 34.32 ?  47  LEU D C     1 
ATOM   13759 O  O     . LEU D 2 68  ? 162.954 102.082 119.519 1.00 34.50 ?  47  LEU D O     1 
ATOM   13760 C  CB    . LEU D 2 68  ? 160.264 103.024 121.076 1.00 35.00 ?  47  LEU D CB    1 
ATOM   13761 C  CG    . LEU D 2 68  ? 158.833 103.590 121.047 1.00 35.82 ?  47  LEU D CG    1 
ATOM   13762 C  CD1   . LEU D 2 68  ? 157.915 102.729 121.901 1.00 35.95 ?  47  LEU D CD1   1 
ATOM   13763 C  CD2   . LEU D 2 68  ? 158.762 105.050 121.492 1.00 35.97 ?  47  LEU D CD2   1 
ATOM   13764 N  N     . GLY D 2 69  ? 163.474 103.211 121.402 1.00 33.50 ?  48  GLY D N     1 
ATOM   13765 C  CA    . GLY D 2 69  ? 164.664 102.423 121.710 1.00 32.41 ?  48  GLY D CA    1 
ATOM   13766 C  C     . GLY D 2 69  ? 164.329 101.008 122.163 1.00 32.15 ?  48  GLY D C     1 
ATOM   13767 O  O     . GLY D 2 69  ? 163.172 100.698 122.475 1.00 30.98 ?  48  GLY D O     1 
ATOM   13768 N  N     . LYS D 2 70  ? 165.348 100.154 122.207 1.00 32.14 ?  49  LYS D N     1 
ATOM   13769 C  CA    . LYS D 2 70  ? 165.183 98.768  122.632 1.00 32.25 ?  49  LYS D CA    1 
ATOM   13770 C  C     . LYS D 2 70  ? 164.649 98.651  124.058 1.00 31.24 ?  49  LYS D C     1 
ATOM   13771 O  O     . LYS D 2 70  ? 163.773 97.827  124.310 1.00 31.34 ?  49  LYS D O     1 
ATOM   13772 C  CB    . LYS D 2 70  ? 166.494 97.991  122.493 1.00 33.07 ?  49  LYS D CB    1 
ATOM   13773 C  CG    . LYS D 2 70  ? 167.006 97.895  121.064 1.00 35.74 ?  49  LYS D CG    1 
ATOM   13774 C  CD    . LYS D 2 70  ? 168.438 97.370  121.049 1.00 39.67 ?  49  LYS D CD    1 
ATOM   13775 C  CE    . LYS D 2 70  ? 169.087 97.567  119.688 1.00 40.96 ?  49  LYS D CE    1 
ATOM   13776 N  NZ    . LYS D 2 70  ? 170.549 97.332  119.784 1.00 42.55 1  49  LYS D NZ    1 
ATOM   13777 N  N     . ASN D 2 71  ? 165.164 99.476  124.977 1.00 29.92 ?  50  ASN D N     1 
ATOM   13778 C  CA    . ASN D 2 71  ? 164.707 99.459  126.371 1.00 29.37 ?  50  ASN D CA    1 
ATOM   13779 C  C     . ASN D 2 71  ? 163.240 99.861  126.494 1.00 28.35 ?  50  ASN D C     1 
ATOM   13780 O  O     . ASN D 2 71  ? 162.499 99.264  127.283 1.00 27.64 ?  50  ASN D O     1 
ATOM   13781 C  CB    . ASN D 2 71  ? 165.572 100.346 127.287 1.00 29.38 ?  50  ASN D CB    1 
ATOM   13782 C  CG    . ASN D 2 71  ? 166.921 99.716  127.628 1.00 31.22 ?  50  ASN D CG    1 
ATOM   13783 O  OD1   . ASN D 2 71  ? 167.060 98.493  127.704 1.00 33.03 ?  50  ASN D OD1   1 
ATOM   13784 N  ND2   . ASN D 2 71  ? 167.924 100.560 127.848 1.00 31.97 ?  50  ASN D ND2   1 
ATOM   13785 N  N     . GLU D 2 72  ? 162.830 100.859 125.707 1.00 27.72 ?  51  GLU D N     1 
ATOM   13786 C  CA    . GLU D 2 72  ? 161.427 101.302 125.691 1.00 27.70 ?  51  GLU D CA    1 
ATOM   13787 C  C     . GLU D 2 72  ? 160.498 100.206 125.162 1.00 27.62 ?  51  GLU D C     1 
ATOM   13788 O  O     . GLU D 2 72  ? 159.418 99.972  125.714 1.00 27.56 ?  51  GLU D O     1 
ATOM   13789 C  CB    . GLU D 2 72  ? 161.250 102.573 124.854 1.00 27.55 ?  51  GLU D CB    1 
ATOM   13790 C  CG    . GLU D 2 72  ? 162.065 103.782 125.330 1.00 28.77 ?  51  GLU D CG    1 
ATOM   13791 C  CD    . GLU D 2 72  ? 161.738 105.028 124.526 1.00 31.18 ?  51  GLU D CD    1 
ATOM   13792 O  OE1   . GLU D 2 72  ? 162.142 105.101 123.346 1.00 33.17 ?  51  GLU D OE1   1 
ATOM   13793 O  OE2   . GLU D 2 72  ? 161.069 105.928 125.072 1.00 31.66 -1 51  GLU D OE2   1 
ATOM   13794 N  N     . GLN D 2 73  ? 160.926 99.541  124.093 1.00 27.32 ?  52  GLN D N     1 
ATOM   13795 C  CA    . GLN D 2 73  ? 160.144 98.466  123.489 1.00 27.33 ?  52  GLN D CA    1 
ATOM   13796 C  C     . GLN D 2 73  ? 160.066 97.269  124.440 1.00 26.85 ?  52  GLN D C     1 
ATOM   13797 O  O     . GLN D 2 73  ? 159.001 96.665  124.601 1.00 26.24 ?  52  GLN D O     1 
ATOM   13798 C  CB    . GLN D 2 73  ? 160.732 98.059  122.144 1.00 27.65 ?  52  GLN D CB    1 
ATOM   13799 C  CG    . GLN D 2 73  ? 160.499 99.070  121.004 1.00 29.66 ?  52  GLN D CG    1 
ATOM   13800 C  CD    . GLN D 2 73  ? 160.931 98.540  119.637 1.00 32.60 ?  52  GLN D CD    1 
ATOM   13801 O  OE1   . GLN D 2 73  ? 161.729 97.611  119.541 1.00 34.76 ?  52  GLN D OE1   1 
ATOM   13802 N  NE2   . GLN D 2 73  ? 160.417 99.146  118.577 1.00 33.42 ?  52  GLN D NE2   1 
ATOM   13803 N  N     . ASP D 2 74  ? 161.189 96.968  125.089 1.00 26.26 ?  53  ASP D N     1 
ATOM   13804 C  CA    . ASP D 2 74  ? 161.288 95.883  126.072 1.00 26.50 ?  53  ASP D CA    1 
ATOM   13805 C  C     . ASP D 2 74  ? 160.382 96.134  127.268 1.00 25.81 ?  53  ASP D C     1 
ATOM   13806 O  O     . ASP D 2 74  ? 159.637 95.248  127.678 1.00 26.12 ?  53  ASP D O     1 
ATOM   13807 C  CB    . ASP D 2 74  ? 162.743 95.739  126.543 1.00 26.84 ?  53  ASP D CB    1 
ATOM   13808 C  CG    . ASP D 2 74  ? 162.967 94.535  127.456 1.00 29.50 ?  53  ASP D CG    1 
ATOM   13809 O  OD1   . ASP D 2 74  ? 162.791 93.382  127.008 1.00 32.08 ?  53  ASP D OD1   1 
ATOM   13810 O  OD2   . ASP D 2 74  ? 163.370 94.743  128.619 1.00 33.52 -1 53  ASP D OD2   1 
ATOM   13811 N  N     . THR D 2 75  ? 160.441 97.342  127.829 1.00 25.10 ?  54  THR D N     1 
ATOM   13812 C  CA    . THR D 2 75  ? 159.599 97.680  128.980 1.00 24.11 ?  54  THR D CA    1 
ATOM   13813 C  C     . THR D 2 75  ? 158.117 97.585  128.606 1.00 23.82 ?  54  THR D C     1 
ATOM   13814 O  O     . THR D 2 75  ? 157.329 96.973  129.327 1.00 23.81 ?  54  THR D O     1 
ATOM   13815 C  CB    . THR D 2 75  ? 159.943 99.069  129.554 1.00 23.80 ?  54  THR D CB    1 
ATOM   13816 O  OG1   . THR D 2 75  ? 161.292 99.051  130.039 1.00 24.62 ?  54  THR D OG1   1 
ATOM   13817 C  CG2   . THR D 2 75  ? 158.997 99.436  130.711 1.00 23.25 ?  54  THR D CG2   1 
ATOM   13818 N  N     . TYR D 2 76  ? 157.749 98.200  127.490 1.00 24.06 ?  55  TYR D N     1 
ATOM   13819 C  CA    . TYR D 2 76  ? 156.376 98.145  126.998 1.00 24.76 ?  55  TYR D CA    1 
ATOM   13820 C  C     . TYR D 2 76  ? 155.854 96.708  126.851 1.00 24.85 ?  55  TYR D C     1 
ATOM   13821 O  O     . TYR D 2 76  ? 154.762 96.394  127.332 1.00 24.83 ?  55  TYR D O     1 
ATOM   13822 C  CB    . TYR D 2 76  ? 156.242 98.887  125.668 1.00 24.78 ?  55  TYR D CB    1 
ATOM   13823 C  CG    . TYR D 2 76  ? 154.817 99.295  125.357 1.00 26.19 ?  55  TYR D CG    1 
ATOM   13824 C  CD1   . TYR D 2 76  ? 154.333 100.539 125.766 1.00 27.81 ?  55  TYR D CD1   1 
ATOM   13825 C  CD2   . TYR D 2 76  ? 153.947 98.440  124.673 1.00 28.03 ?  55  TYR D CD2   1 
ATOM   13826 C  CE1   . TYR D 2 76  ? 153.030 100.932 125.492 1.00 29.32 ?  55  TYR D CE1   1 
ATOM   13827 C  CE2   . TYR D 2 76  ? 152.627 98.825  124.394 1.00 29.01 ?  55  TYR D CE2   1 
ATOM   13828 C  CZ    . TYR D 2 76  ? 152.184 100.075 124.810 1.00 30.76 ?  55  TYR D CZ    1 
ATOM   13829 O  OH    . TYR D 2 76  ? 150.899 100.492 124.549 1.00 34.50 ?  55  TYR D OH    1 
ATOM   13830 N  N     . MET D 2 77  ? 156.631 95.853  126.189 1.00 25.76 ?  56  MET D N     1 
ATOM   13831 C  CA    . MET D 2 77  ? 156.265 94.442  126.021 1.00 26.81 ?  56  MET D CA    1 
ATOM   13832 C  C     . MET D 2 77  ? 156.039 93.749  127.369 1.00 26.23 ?  56  MET D C     1 
ATOM   13833 O  O     . MET D 2 77  ? 155.046 93.042  127.554 1.00 25.00 ?  56  MET D O     1 
ATOM   13834 C  CB    . MET D 2 77  ? 157.334 93.693  125.228 1.00 28.11 ?  56  MET D CB    1 
ATOM   13835 C  CG    . MET D 2 77  ? 157.436 94.076  123.747 1.00 32.52 ?  56  MET D CG    1 
ATOM   13836 S  SD    . MET D 2 77  ? 156.074 93.470  122.736 1.00 42.68 ?  56  MET D SD    1 
ATOM   13837 C  CE    . MET D 2 77  ? 154.841 94.756  122.930 1.00 38.97 ?  56  MET D CE    1 
ATOM   13838 N  N     . LYS D 2 78  ? 156.975 93.956  128.296 1.00 26.01 ?  57  LYS D N     1 
ATOM   13839 C  CA    . LYS D 2 78  ? 156.916 93.319  129.614 1.00 26.07 ?  57  LYS D CA    1 
ATOM   13840 C  C     . LYS D 2 78  ? 155.727 93.803  130.441 1.00 25.69 ?  57  LYS D C     1 
ATOM   13841 O  O     . LYS D 2 78  ? 155.073 93.010  131.130 1.00 25.58 ?  57  LYS D O     1 
ATOM   13842 C  CB    . LYS D 2 78  ? 158.227 93.527  130.386 1.00 26.08 ?  57  LYS D CB    1 
ATOM   13843 C  CG    . LYS D 2 78  ? 159.418 92.754  129.802 1.00 27.64 ?  57  LYS D CG    1 
ATOM   13844 C  CD    . LYS D 2 78  ? 160.722 93.130  130.494 1.00 29.47 ?  57  LYS D CD    1 
ATOM   13845 C  CE    . LYS D 2 78  ? 161.848 92.207  130.053 1.00 31.69 ?  57  LYS D CE    1 
ATOM   13846 N  NZ    . LYS D 2 78  ? 163.135 92.528  130.725 1.00 33.36 1  57  LYS D NZ    1 
ATOM   13847 N  N     . VAL D 2 79  ? 155.455 95.104  130.370 1.00 25.32 ?  58  VAL D N     1 
ATOM   13848 C  CA    . VAL D 2 79  ? 154.322 95.710  131.078 1.00 25.47 ?  58  VAL D CA    1 
ATOM   13849 C  C     . VAL D 2 79  ? 153.021 95.148  130.513 1.00 25.09 ?  58  VAL D C     1 
ATOM   13850 O  O     . VAL D 2 79  ? 152.131 94.727  131.258 1.00 24.46 ?  58  VAL D O     1 
ATOM   13851 C  CB    . VAL D 2 79  ? 154.364 97.258  130.938 1.00 25.83 ?  58  VAL D CB    1 
ATOM   13852 C  CG1   . VAL D 2 79  ? 152.983 97.865  131.044 1.00 27.35 ?  58  VAL D CG1   1 
ATOM   13853 C  CG2   . VAL D 2 79  ? 155.329 97.851  131.964 1.00 26.42 ?  58  VAL D CG2   1 
ATOM   13854 N  N     . LEU D 2 80  ? 152.949 95.101  129.185 1.00 25.27 ?  59  LEU D N     1 
ATOM   13855 C  CA    . LEU D 2 80  ? 151.768 94.633  128.495 1.00 25.55 ?  59  LEU D CA    1 
ATOM   13856 C  C     . LEU D 2 80  ? 151.465 93.186  128.878 1.00 24.94 ?  59  LEU D C     1 
ATOM   13857 O  O     . LEU D 2 80  ? 150.315 92.846  129.148 1.00 24.82 ?  59  LEU D O     1 
ATOM   13858 C  CB    . LEU D 2 80  ? 151.959 94.755  126.982 1.00 25.80 ?  59  LEU D CB    1 
ATOM   13859 C  CG    . LEU D 2 80  ? 151.001 95.567  126.104 1.00 28.76 ?  59  LEU D CG    1 
ATOM   13860 C  CD1   . LEU D 2 80  ? 150.947 94.913  124.723 1.00 30.25 ?  59  LEU D CD1   1 
ATOM   13861 C  CD2   . LEU D 2 80  ? 149.599 95.718  126.672 1.00 27.79 ?  59  LEU D CD2   1 
ATOM   13862 N  N     . ALA D 2 81  ? 152.502 92.347  128.905 1.00 24.86 ?  60  ALA D N     1 
ATOM   13863 C  CA    . ALA D 2 81  ? 152.352 90.930  129.267 1.00 24.60 ?  60  ALA D CA    1 
ATOM   13864 C  C     . ALA D 2 81  ? 151.914 90.789  130.721 1.00 23.80 ?  60  ALA D C     1 
ATOM   13865 O  O     . ALA D 2 81  ? 151.102 89.931  131.052 1.00 24.07 ?  60  ALA D O     1 
ATOM   13866 C  CB    . ALA D 2 81  ? 153.655 90.171  129.024 1.00 24.48 ?  60  ALA D CB    1 
ATOM   13867 N  N     . GLY D 2 82  ? 152.453 91.642  131.584 1.00 23.54 ?  61  GLY D N     1 
ATOM   13868 C  CA    . GLY D 2 82  ? 152.049 91.686  132.985 1.00 22.53 ?  61  GLY D CA    1 
ATOM   13869 C  C     . GLY D 2 82  ? 150.566 91.955  133.129 1.00 22.23 ?  61  GLY D C     1 
ATOM   13870 O  O     . GLY D 2 82  ? 149.864 91.240  133.842 1.00 21.27 ?  61  GLY D O     1 
ATOM   13871 N  N     . LEU D 2 83  ? 150.083 92.991  132.443 1.00 22.36 ?  62  LEU D N     1 
ATOM   13872 C  CA    . LEU D 2 83  ? 148.656 93.331  132.473 1.00 22.42 ?  62  LEU D CA    1 
ATOM   13873 C  C     . LEU D 2 83  ? 147.805 92.194  131.923 1.00 22.91 ?  62  LEU D C     1 
ATOM   13874 O  O     . LEU D 2 83  ? 146.766 91.850  132.502 1.00 22.99 ?  62  LEU D O     1 
ATOM   13875 C  CB    . LEU D 2 83  ? 148.373 94.614  131.683 1.00 22.19 ?  62  LEU D CB    1 
ATOM   13876 C  CG    . LEU D 2 83  ? 148.981 95.915  132.234 1.00 22.17 ?  62  LEU D CG    1 
ATOM   13877 C  CD1   . LEU D 2 83  ? 148.908 97.016  131.168 1.00 21.55 ?  62  LEU D CD1   1 
ATOM   13878 C  CD2   . LEU D 2 83  ? 148.250 96.330  133.498 1.00 22.42 ?  62  LEU D CD2   1 
ATOM   13879 N  N     . THR D 2 84  ? 148.260 91.602  130.823 1.00 23.39 ?  63  THR D N     1 
ATOM   13880 C  CA    . THR D 2 84  ? 147.521 90.521  130.174 1.00 24.42 ?  63  THR D CA    1 
ATOM   13881 C  C     . THR D 2 84  ? 147.344 89.332  131.122 1.00 24.55 ?  63  THR D C     1 
ATOM   13882 O  O     . THR D 2 84  ? 146.232 88.826  131.299 1.00 23.68 ?  63  THR D O     1 
ATOM   13883 C  CB    . THR D 2 84  ? 148.215 90.050  128.871 1.00 24.70 ?  63  THR D CB    1 
ATOM   13884 O  OG1   . THR D 2 84  ? 148.322 91.153  127.962 1.00 25.57 ?  63  THR D OG1   1 
ATOM   13885 C  CG2   . THR D 2 84  ? 147.402 88.952  128.205 1.00 25.36 ?  63  THR D CG2   1 
ATOM   13886 N  N     . LEU D 2 85  ? 148.452 88.909  131.721 1.00 25.38 ?  64  LEU D N     1 
ATOM   13887 C  CA    . LEU D 2 85  ? 148.454 87.773  132.634 1.00 26.44 ?  64  LEU D CA    1 
ATOM   13888 C  C     . LEU D 2 85  ? 147.563 88.009  133.857 1.00 25.96 ?  64  LEU D C     1 
ATOM   13889 O  O     . LEU D 2 85  ? 146.750 87.138  134.198 1.00 25.83 ?  64  LEU D O     1 
ATOM   13890 C  CB    . LEU D 2 85  ? 149.889 87.367  133.006 1.00 26.65 ?  64  LEU D CB    1 
ATOM   13891 C  CG    . LEU D 2 85  ? 150.598 86.599  131.873 1.00 29.62 ?  64  LEU D CG    1 
ATOM   13892 C  CD1   . LEU D 2 85  ? 152.109 86.690  131.981 1.00 31.57 ?  64  LEU D CD1   1 
ATOM   13893 C  CD2   . LEU D 2 85  ? 150.162 85.123  131.815 1.00 30.96 ?  64  LEU D CD2   1 
ATOM   13894 N  N     . LEU D 2 86  ? 147.668 89.185  134.480 1.00 25.63 ?  65  LEU D N     1 
ATOM   13895 C  CA    . LEU D 2 86  ? 146.799 89.500  135.616 1.00 25.59 ?  65  LEU D CA    1 
ATOM   13896 C  C     . LEU D 2 86  ? 145.319 89.578  135.246 1.00 25.60 ?  65  LEU D C     1 
ATOM   13897 O  O     . LEU D 2 86  ? 144.454 89.152  136.017 1.00 25.47 ?  65  LEU D O     1 
ATOM   13898 C  CB    . LEU D 2 86  ? 147.240 90.784  136.346 1.00 25.76 ?  65  LEU D CB    1 
ATOM   13899 C  CG    . LEU D 2 86  ? 148.563 90.702  137.119 1.00 26.71 ?  65  LEU D CG    1 
ATOM   13900 C  CD1   . LEU D 2 86  ? 149.065 92.086  137.521 1.00 28.01 ?  65  LEU D CD1   1 
ATOM   13901 C  CD2   . LEU D 2 86  ? 148.435 89.823  138.341 1.00 28.01 ?  65  LEU D CD2   1 
ATOM   13902 N  N     . ASP D 2 87  ? 145.021 90.128  134.074 1.00 25.49 ?  66  ASP D N     1 
ATOM   13903 C  CA    . ASP D 2 87  ? 143.637 90.301  133.668 1.00 25.83 ?  66  ASP D CA    1 
ATOM   13904 C  C     . ASP D 2 87  ? 142.956 88.965  133.341 1.00 26.20 ?  66  ASP D C     1 
ATOM   13905 O  O     . ASP D 2 87  ? 141.756 88.811  133.541 1.00 25.99 ?  66  ASP D O     1 
ATOM   13906 C  CB    . ASP D 2 87  ? 143.538 91.268  132.495 1.00 25.50 ?  66  ASP D CB    1 
ATOM   13907 C  CG    . ASP D 2 87  ? 142.260 92.056  132.517 1.00 25.76 ?  66  ASP D CG    1 
ATOM   13908 O  OD1   . ASP D 2 87  ? 141.716 92.271  133.627 1.00 26.91 ?  66  ASP D OD1   1 
ATOM   13909 O  OD2   . ASP D 2 87  ? 141.791 92.467  131.437 1.00 23.11 -1 66  ASP D OD2   1 
ATOM   13910 N  N     . THR D 2 88  ? 143.741 88.004  132.861 1.00 27.12 ?  67  THR D N     1 
ATOM   13911 C  CA    . THR D 2 88  ? 143.262 86.652  132.605 1.00 28.40 ?  67  THR D CA    1 
ATOM   13912 C  C     . THR D 2 88  ? 142.823 85.967  133.888 1.00 28.28 ?  67  THR D C     1 
ATOM   13913 O  O     . THR D 2 88  ? 141.791 85.298  133.911 1.00 28.10 ?  67  THR D O     1 
ATOM   13914 C  CB    . THR D 2 88  ? 144.331 85.800  131.893 1.00 29.04 ?  67  THR D CB    1 
ATOM   13915 O  OG1   . THR D 2 88  ? 144.671 86.425  130.653 1.00 31.00 ?  67  THR D OG1   1 
ATOM   13916 C  CG2   . THR D 2 88  ? 143.797 84.399  131.600 1.00 30.16 ?  67  THR D CG2   1 
ATOM   13917 N  N     . GLU D 2 89  ? 143.597 86.134  134.959 1.00 28.28 ?  68  GLU D N     1 
ATOM   13918 C  CA    . GLU D 2 89  ? 143.196 85.598  136.255 1.00 29.16 ?  68  GLU D CA    1 
ATOM   13919 C  C     . GLU D 2 89  ? 141.860 86.206  136.678 1.00 28.65 ?  68  GLU D C     1 
ATOM   13920 O  O     . GLU D 2 89  ? 140.994 85.505  137.184 1.00 28.44 ?  68  GLU D O     1 
ATOM   13921 C  CB    . GLU D 2 89  ? 144.258 85.857  137.333 1.00 29.32 ?  68  GLU D CB    1 
ATOM   13922 C  CG    . GLU D 2 89  ? 145.629 85.227  137.045 1.00 31.95 ?  68  GLU D CG    1 
ATOM   13923 C  CD    . GLU D 2 89  ? 145.613 83.702  137.006 1.00 35.19 ?  68  GLU D CD    1 
ATOM   13924 O  OE1   . GLU D 2 89  ? 144.647 83.071  137.491 1.00 35.47 ?  68  GLU D OE1   1 
ATOM   13925 O  OE2   . GLU D 2 89  ? 146.587 83.128  136.475 1.00 38.06 -1 68  GLU D OE2   1 
ATOM   13926 N  N     . GLN D 2 90  ? 141.694 87.506  136.452 1.00 28.45 ?  69  GLN D N     1 
ATOM   13927 C  CA    . GLN D 2 90  ? 140.460 88.189  136.842 1.00 28.47 ?  69  GLN D CA    1 
ATOM   13928 C  C     . GLN D 2 90  ? 139.250 87.689  136.040 1.00 28.97 ?  69  GLN D C     1 
ATOM   13929 O  O     . GLN D 2 90  ? 138.162 87.532  136.592 1.00 28.84 ?  69  GLN D O     1 
ATOM   13930 C  CB    . GLN D 2 90  ? 140.621 89.708  136.735 1.00 28.21 ?  69  GLN D CB    1 
ATOM   13931 C  CG    . GLN D 2 90  ? 139.573 90.515  137.499 1.00 27.75 ?  69  GLN D CG    1 
ATOM   13932 C  CD    . GLN D 2 90  ? 139.731 90.461  139.014 1.00 28.91 ?  69  GLN D CD    1 
ATOM   13933 O  OE1   . GLN D 2 90  ? 140.350 89.542  139.569 1.00 27.62 ?  69  GLN D OE1   1 
ATOM   13934 N  NE2   . GLN D 2 90  ? 139.146 91.447  139.697 1.00 28.23 ?  69  GLN D NE2   1 
ATOM   13935 N  N     . GLY D 2 91  ? 139.453 87.418  134.751 1.00 29.62 ?  70  GLY D N     1 
ATOM   13936 C  CA    . GLY D 2 91  ? 138.394 86.883  133.893 1.00 30.43 ?  70  GLY D CA    1 
ATOM   13937 C  C     . GLY D 2 91  ? 138.031 85.425  134.153 1.00 31.11 ?  70  GLY D C     1 
ATOM   13938 O  O     . GLY D 2 91  ? 136.855 85.049  134.132 1.00 30.77 ?  70  GLY D O     1 
ATOM   13939 N  N     . ASN D 2 92  ? 139.038 84.596  134.388 1.00 31.69 ?  71  ASN D N     1 
ATOM   13940 C  CA    . ASN D 2 92  ? 138.787 83.178  134.613 1.00 32.72 ?  71  ASN D CA    1 
ATOM   13941 C  C     . ASN D 2 92  ? 138.377 82.810  136.032 1.00 32.60 ?  71  ASN D C     1 
ATOM   13942 O  O     . ASN D 2 92  ? 137.644 81.836  136.222 1.00 33.12 ?  71  ASN D O     1 
ATOM   13943 C  CB    . ASN D 2 92  ? 139.986 82.346  134.175 1.00 33.68 ?  71  ASN D CB    1 
ATOM   13944 C  CG    . ASN D 2 92  ? 140.131 82.296  132.669 1.00 35.15 ?  71  ASN D CG    1 
ATOM   13945 O  OD1   . ASN D 2 92  ? 141.231 82.119  132.159 1.00 40.21 ?  71  ASN D OD1   1 
ATOM   13946 N  ND2   . ASN D 2 92  ? 139.021 82.463  131.948 1.00 36.91 ?  71  ASN D ND2   1 
ATOM   13947 N  N     . THR D 2 93  ? 138.828 83.595  137.010 1.00 31.76 ?  72  THR D N     1 
ATOM   13948 C  CA    . THR D 2 93  ? 138.611 83.270  138.415 1.00 31.47 ?  72  THR D CA    1 
ATOM   13949 C  C     . THR D 2 93  ? 137.998 84.409  139.227 1.00 30.62 ?  72  THR D C     1 
ATOM   13950 O  O     . THR D 2 93  ? 136.928 84.243  139.805 1.00 30.71 ?  72  THR D O     1 
ATOM   13951 C  CB    . THR D 2 93  ? 139.911 82.814  139.072 1.00 31.60 ?  72  THR D CB    1 
ATOM   13952 O  OG1   . THR D 2 93  ? 140.447 81.713  138.327 1.00 33.14 ?  72  THR D OG1   1 
ATOM   13953 C  CG2   . THR D 2 93  ? 139.666 82.383  140.509 1.00 31.89 ?  72  THR D CG2   1 
ATOM   13954 N  N     . GLY D 2 94  ? 138.676 85.554  139.260 1.00 29.61 ?  73  GLY D N     1 
ATOM   13955 C  CA    . GLY D 2 94  ? 138.287 86.673  140.120 1.00 28.47 ?  73  GLY D CA    1 
ATOM   13956 C  C     . GLY D 2 94  ? 136.840 87.114  140.019 1.00 27.90 ?  73  GLY D C     1 
ATOM   13957 O  O     . GLY D 2 94  ? 136.120 87.167  141.025 1.00 28.27 ?  73  GLY D O     1 
ATOM   13958 N  N     . MET D 2 95  ? 136.402 87.460  138.817 1.00 26.67 ?  74  MET D N     1 
ATOM   13959 C  CA    . MET D 2 95  ? 135.019 87.909  138.675 1.00 26.00 ?  74  MET D CA    1 
ATOM   13960 C  C     . MET D 2 95  ? 134.032 86.753  138.779 1.00 25.25 ?  74  MET D C     1 
ATOM   13961 O  O     . MET D 2 95  ? 133.015 86.897  139.444 1.00 24.97 ?  74  MET D O     1 
ATOM   13962 C  CB    . MET D 2 95  ? 134.787 88.723  137.395 1.00 26.00 ?  74  MET D CB    1 
ATOM   13963 C  CG    . MET D 2 95  ? 135.244 90.158  137.493 1.00 26.40 ?  74  MET D CG    1 
ATOM   13964 S  SD    . MET D 2 95  ? 134.392 91.118  138.771 1.00 28.10 ?  74  MET D SD    1 
ATOM   13965 C  CE    . MET D 2 95  ? 135.344 92.629  138.674 1.00 28.95 ?  74  MET D CE    1 
ATOM   13966 N  N     . PRO D 2 96  ? 134.316 85.613  138.120 1.00 24.98 ?  75  PRO D N     1 
ATOM   13967 C  CA    . PRO D 2 96  ? 133.311 84.542  138.240 1.00 24.59 ?  75  PRO D CA    1 
ATOM   13968 C  C     . PRO D 2 96  ? 133.157 83.980  139.651 1.00 23.90 ?  75  PRO D C     1 
ATOM   13969 O  O     . PRO D 2 96  ? 132.058 83.571  140.009 1.00 23.45 ?  75  PRO D O     1 
ATOM   13970 C  CB    . PRO D 2 96  ? 133.831 83.450  137.295 1.00 24.80 ?  75  PRO D CB    1 
ATOM   13971 C  CG    . PRO D 2 96  ? 134.680 84.193  136.289 1.00 25.75 ?  75  PRO D CG    1 
ATOM   13972 C  CD    . PRO D 2 96  ? 135.313 85.317  137.068 1.00 25.07 ?  75  PRO D CD    1 
ATOM   13973 N  N     . ILE D 2 97  ? 134.237 83.947  140.436 1.00 23.36 ?  76  ILE D N     1 
ATOM   13974 C  CA    . ILE D 2 97  ? 134.149 83.393  141.784 1.00 23.48 ?  76  ILE D CA    1 
ATOM   13975 C  C     . ILE D 2 97  ? 133.349 84.311  142.692 1.00 23.30 ?  76  ILE D C     1 
ATOM   13976 O  O     . ILE D 2 97  ? 132.587 83.837  143.533 1.00 23.45 ?  76  ILE D O     1 
ATOM   13977 C  CB    . ILE D 2 97  ? 135.539 83.048  142.389 1.00 23.96 ?  76  ILE D CB    1 
ATOM   13978 C  CG1   . ILE D 2 97  ? 135.412 81.950  143.440 1.00 24.71 ?  76  ILE D CG1   1 
ATOM   13979 C  CG2   . ILE D 2 97  ? 136.254 84.294  142.966 1.00 24.02 ?  76  ILE D CG2   1 
ATOM   13980 C  CD1   . ILE D 2 97  ? 136.649 81.020  143.477 1.00 29.17 ?  76  ILE D CD1   1 
ATOM   13981 N  N     . VAL D 2 98  ? 133.511 85.621  142.514 1.00 22.71 ?  77  VAL D N     1 
ATOM   13982 C  CA    . VAL D 2 98  ? 132.743 86.600  143.301 1.00 22.78 ?  77  VAL D CA    1 
ATOM   13983 C  C     . VAL D 2 98  ? 131.265 86.556  142.908 1.00 22.89 ?  77  VAL D C     1 
ATOM   13984 O  O     . VAL D 2 98  ? 130.386 86.572  143.769 1.00 23.72 ?  77  VAL D O     1 
ATOM   13985 C  CB    . VAL D 2 98  ? 133.347 88.028  143.188 1.00 22.49 ?  77  VAL D CB    1 
ATOM   13986 C  CG1   . VAL D 2 98  ? 132.423 89.088  143.816 1.00 21.91 ?  77  VAL D CG1   1 
ATOM   13987 C  CG2   . VAL D 2 98  ? 134.706 88.063  143.867 1.00 23.02 ?  77  VAL D CG2   1 
ATOM   13988 N  N     . ALA D 2 99  ? 130.993 86.463  141.607 1.00 23.19 ?  78  ALA D N     1 
ATOM   13989 C  CA    . ALA D 2 99  ? 129.611 86.335  141.123 1.00 23.05 ?  78  ALA D CA    1 
ATOM   13990 C  C     . ALA D 2 99  ? 128.935 85.094  141.712 1.00 23.52 ?  78  ALA D C     1 
ATOM   13991 O  O     . ALA D 2 99  ? 127.747 85.113  142.052 1.00 23.68 ?  78  ALA D O     1 
ATOM   13992 C  CB    . ALA D 2 99  ? 129.583 86.300  139.604 1.00 22.81 ?  78  ALA D CB    1 
ATOM   13993 N  N     . GLU D 2 100 ? 129.697 84.013  141.843 1.00 23.68 ?  79  GLU D N     1 
ATOM   13994 C  CA    . GLU D 2 100 ? 129.175 82.775  142.418 1.00 24.14 ?  79  GLU D CA    1 
ATOM   13995 C  C     . GLU D 2 100 ? 128.734 82.902  143.885 1.00 23.66 ?  79  GLU D C     1 
ATOM   13996 O  O     . GLU D 2 100 ? 127.687 82.375  144.274 1.00 22.94 ?  79  GLU D O     1 
ATOM   13997 C  CB    . GLU D 2 100 ? 130.215 81.665  142.272 1.00 24.47 ?  79  GLU D CB    1 
ATOM   13998 C  CG    . GLU D 2 100 ? 129.695 80.283  142.619 1.00 27.90 ?  79  GLU D CG    1 
ATOM   13999 C  CD    . GLU D 2 100 ? 130.792 79.234  142.637 1.00 32.30 ?  79  GLU D CD    1 
ATOM   14000 O  OE1   . GLU D 2 100 ? 131.814 79.413  141.936 1.00 32.88 ?  79  GLU D OE1   1 
ATOM   14001 O  OE2   . GLU D 2 100 ? 130.627 78.231  143.361 1.00 34.74 -1 79  GLU D OE2   1 
ATOM   14002 N  N     . HIS D 2 101 ? 129.533 83.589  144.700 1.00 23.62 ?  80  HIS D N     1 
ATOM   14003 C  CA    . HIS D 2 101 ? 129.260 83.679  146.147 1.00 23.99 ?  80  HIS D CA    1 
ATOM   14004 C  C     . HIS D 2 101 ? 128.391 84.859  146.603 1.00 24.35 ?  80  HIS D C     1 
ATOM   14005 O  O     . HIS D 2 101 ? 127.851 84.832  147.710 1.00 24.21 ?  80  HIS D O     1 
ATOM   14006 C  CB    . HIS D 2 101 ? 130.573 83.626  146.942 1.00 24.13 ?  80  HIS D CB    1 
ATOM   14007 C  CG    . HIS D 2 101 ? 131.286 82.311  146.823 1.00 24.76 ?  80  HIS D CG    1 
ATOM   14008 N  ND1   . HIS D 2 101 ? 131.118 81.288  147.733 1.00 25.68 ?  80  HIS D ND1   1 
ATOM   14009 C  CD2   . HIS D 2 101 ? 132.147 81.845  145.889 1.00 25.75 ?  80  HIS D CD2   1 
ATOM   14010 C  CE1   . HIS D 2 101 ? 131.851 80.250  147.365 1.00 26.21 ?  80  HIS D CE1   1 
ATOM   14011 N  NE2   . HIS D 2 101 ? 132.486 80.563  146.250 1.00 25.35 ?  80  HIS D NE2   1 
ATOM   14012 N  N     . VAL D 2 102 ? 128.265 85.892  145.772 1.00 24.50 ?  81  VAL D N     1 
ATOM   14013 C  CA    . VAL D 2 102 ? 127.414 87.036  146.094 1.00 25.50 ?  81  VAL D CA    1 
ATOM   14014 C  C     . VAL D 2 102 ? 125.934 86.670  145.893 1.00 26.14 ?  81  VAL D C     1 
ATOM   14015 O  O     . VAL D 2 102 ? 125.582 86.072  144.879 1.00 26.96 ?  81  VAL D O     1 
ATOM   14016 C  CB    . VAL D 2 102 ? 127.787 88.278  145.232 1.00 25.30 ?  81  VAL D CB    1 
ATOM   14017 C  CG1   . VAL D 2 102 ? 126.746 89.364  145.359 1.00 27.08 ?  81  VAL D CG1   1 
ATOM   14018 C  CG2   . VAL D 2 102 ? 129.142 88.824  145.654 1.00 25.41 ?  81  VAL D CG2   1 
ATOM   14019 N  N     . ASP D 2 103 ? 125.090 87.013  146.862 1.00 26.45 ?  82  ASP D N     1 
ATOM   14020 C  CA    . ASP D 2 103 ? 123.644 86.817  146.738 1.00 27.15 ?  82  ASP D CA    1 
ATOM   14021 C  C     . ASP D 2 103 ? 122.988 88.043  146.119 1.00 26.39 ?  82  ASP D C     1 
ATOM   14022 O  O     . ASP D 2 103 ? 123.367 89.184  146.416 1.00 26.40 ?  82  ASP D O     1 
ATOM   14023 C  CB    . ASP D 2 103 ? 123.003 86.532  148.101 1.00 27.72 ?  82  ASP D CB    1 
ATOM   14024 C  CG    . ASP D 2 103 ? 123.509 85.247  148.745 1.00 31.46 ?  82  ASP D CG    1 
ATOM   14025 O  OD1   . ASP D 2 103 ? 123.848 84.271  148.022 1.00 34.26 ?  82  ASP D OD1   1 
ATOM   14026 O  OD2   . ASP D 2 103 ? 123.561 85.208  149.996 1.00 35.52 -1 82  ASP D OD2   1 
ATOM   14027 N  N     . GLY D 2 104 ? 121.991 87.801  145.274 1.00 25.52 ?  83  GLY D N     1 
ATOM   14028 C  CA    . GLY D 2 104 ? 121.239 88.880  144.636 1.00 24.31 ?  83  GLY D CA    1 
ATOM   14029 C  C     . GLY D 2 104 ? 121.306 88.716  143.122 1.00 23.27 ?  83  GLY D C     1 
ATOM   14030 O  O     . GLY D 2 104 ? 122.390 88.650  142.544 1.00 22.38 ?  83  GLY D O     1 
ATOM   14031 N  N     . HIS D 2 105 ? 120.144 88.632  142.481 1.00 22.46 ?  84  HIS D N     1 
ATOM   14032 C  CA    . HIS D 2 105 ? 120.091 88.461  141.027 1.00 22.17 ?  84  HIS D CA    1 
ATOM   14033 C  C     . HIS D 2 105 ? 120.715 89.615  140.260 1.00 21.13 ?  84  HIS D C     1 
ATOM   14034 O  O     . HIS D 2 105 ? 121.391 89.396  139.257 1.00 20.91 ?  84  HIS D O     1 
ATOM   14035 C  CB    . HIS D 2 105 ? 118.647 88.235  140.559 1.00 22.07 ?  84  HIS D CB    1 
ATOM   14036 C  CG    . HIS D 2 105 ? 118.014 87.029  141.178 1.00 23.85 ?  84  HIS D CG    1 
ATOM   14037 N  ND1   . HIS D 2 105 ? 118.616 85.789  141.158 1.00 24.86 ?  84  HIS D ND1   1 
ATOM   14038 C  CD2   . HIS D 2 105 ? 116.858 86.878  141.865 1.00 25.19 ?  84  HIS D CD2   1 
ATOM   14039 C  CE1   . HIS D 2 105 ? 117.846 84.920  141.788 1.00 24.94 ?  84  HIS D CE1   1 
ATOM   14040 N  NE2   . HIS D 2 105 ? 116.777 85.558  142.231 1.00 26.41 ?  84  HIS D NE2   1 
ATOM   14041 N  N     . GLN D 2 106 ? 120.490 90.835  140.726 1.00 20.66 ?  85  GLN D N     1 
ATOM   14042 C  CA    . GLN D 2 106 ? 120.949 92.004  139.981 1.00 20.70 ?  85  GLN D CA    1 
ATOM   14043 C  C     . GLN D 2 106 ? 122.465 92.147  140.109 1.00 20.46 ?  85  GLN D C     1 
ATOM   14044 O  O     . GLN D 2 106 ? 123.138 92.488  139.136 1.00 20.72 ?  85  GLN D O     1 
ATOM   14045 C  CB    . GLN D 2 106 ? 120.174 93.268  140.387 1.00 20.60 ?  85  GLN D CB    1 
ATOM   14046 C  CG    . GLN D 2 106 ? 118.652 93.160  140.094 1.00 20.74 ?  85  GLN D CG    1 
ATOM   14047 C  CD    . GLN D 2 106 ? 117.815 94.312  140.663 1.00 22.11 ?  85  GLN D CD    1 
ATOM   14048 O  OE1   . GLN D 2 106 ? 118.294 95.431  140.815 1.00 22.88 ?  85  GLN D OE1   1 
ATOM   14049 N  NE2   . GLN D 2 106 ? 116.549 94.034  140.965 1.00 21.64 ?  85  GLN D NE2   1 
ATOM   14050 N  N     . ARG D 2 107 ? 122.997 91.832  141.292 1.00 20.17 ?  86  ARG D N     1 
ATOM   14051 C  CA    . ARG D 2 107 ? 124.444 91.846  141.515 1.00 20.29 ?  86  ARG D CA    1 
ATOM   14052 C  C     . ARG D 2 107 ? 125.130 90.786  140.669 1.00 20.07 ?  86  ARG D C     1 
ATOM   14053 O  O     . ARG D 2 107 ? 126.177 91.043  140.088 1.00 19.53 ?  86  ARG D O     1 
ATOM   14054 C  CB    . ARG D 2 107 ? 124.775 91.599  142.985 1.00 20.88 ?  86  ARG D CB    1 
ATOM   14055 C  CG    . ARG D 2 107 ? 124.162 92.609  143.899 1.00 22.56 ?  86  ARG D CG    1 
ATOM   14056 C  CD    . ARG D 2 107 ? 124.233 92.146  145.332 1.00 27.21 ?  86  ARG D CD    1 
ATOM   14057 N  NE    . ARG D 2 107 ? 124.116 93.332  146.159 1.00 31.70 ?  86  ARG D NE    1 
ATOM   14058 C  CZ    . ARG D 2 107 ? 124.508 93.427  147.412 1.00 32.23 ?  86  ARG D CZ    1 
ATOM   14059 N  NH1   . ARG D 2 107 ? 125.051 92.383  148.036 1.00 34.27 1  86  ARG D NH1   1 
ATOM   14060 N  NH2   . ARG D 2 107 ? 124.352 94.584  148.029 1.00 33.79 ?  86  ARG D NH2   1 
ATOM   14061 N  N     . LYS D 2 108 ? 124.545 89.589  140.616 1.00 19.61 ?  87  LYS D N     1 
ATOM   14062 C  CA    . LYS D 2 108 ? 125.100 88.526  139.779 1.00 19.92 ?  87  LYS D CA    1 
ATOM   14063 C  C     . LYS D 2 108 ? 125.143 88.932  138.303 1.00 20.08 ?  87  LYS D C     1 
ATOM   14064 O  O     . LYS D 2 108 ? 126.069 88.553  137.577 1.00 20.38 ?  87  LYS D O     1 
ATOM   14065 C  CB    . LYS D 2 108 ? 124.345 87.206  139.957 1.00 19.54 ?  87  LYS D CB    1 
ATOM   14066 C  CG    . LYS D 2 108 ? 124.499 86.580  141.331 1.00 20.55 ?  87  LYS D CG    1 
ATOM   14067 C  CD    . LYS D 2 108 ? 123.743 85.253  141.427 1.00 21.09 ?  87  LYS D CD    1 
ATOM   14068 C  CE    . LYS D 2 108 ? 123.921 84.589  142.788 1.00 22.98 ?  87  LYS D CE    1 
ATOM   14069 N  NZ    . LYS D 2 108 ? 125.319 84.033  142.942 1.00 22.30 1  87  LYS D NZ    1 
ATOM   14070 N  N     . ALA D 2 109 ? 124.141 89.691  137.859 1.00 19.72 ?  88  ALA D N     1 
ATOM   14071 C  CA    . ALA D 2 109 ? 124.091 90.135  136.471 1.00 19.83 ?  88  ALA D CA    1 
ATOM   14072 C  C     . ALA D 2 109 ? 125.197 91.148  136.170 1.00 19.84 ?  88  ALA D C     1 
ATOM   14073 O  O     . ALA D 2 109 ? 125.890 91.036  135.153 1.00 19.96 ?  88  ALA D O     1 
ATOM   14074 C  CB    . ALA D 2 109 ? 122.703 90.702  136.126 1.00 19.65 ?  88  ALA D CB    1 
ATOM   14075 N  N     . VAL D 2 110 ? 125.378 92.117  137.064 1.00 19.33 ?  89  VAL D N     1 
ATOM   14076 C  CA    . VAL D 2 110 ? 126.439 93.122  136.902 1.00 19.22 ?  89  VAL D CA    1 
ATOM   14077 C  C     . VAL D 2 110 ? 127.806 92.415  136.910 1.00 19.45 ?  89  VAL D C     1 
ATOM   14078 O  O     . VAL D 2 110 ? 128.619 92.590  135.992 1.00 18.97 ?  89  VAL D O     1 
ATOM   14079 C  CB    . VAL D 2 110 ? 126.317 94.247  137.969 1.00 19.01 ?  89  VAL D CB    1 
ATOM   14080 C  CG1   . VAL D 2 110 ? 127.537 95.213  137.939 1.00 19.90 ?  89  VAL D CG1   1 
ATOM   14081 C  CG2   . VAL D 2 110 ? 125.045 95.030  137.732 1.00 19.69 ?  89  VAL D CG2   1 
ATOM   14082 N  N     . LEU D 2 111 ? 128.022 91.557  137.910 1.00 19.27 ?  90  LEU D N     1 
ATOM   14083 C  CA    . LEU D 2 111 ? 129.264 90.784  137.980 1.00 19.96 ?  90  LEU D CA    1 
ATOM   14084 C  C     . LEU D 2 111 ? 129.521 89.926  136.734 1.00 20.30 ?  90  LEU D C     1 
ATOM   14085 O  O     . LEU D 2 111 ? 130.654 89.868  136.249 1.00 19.88 ?  90  LEU D O     1 
ATOM   14086 C  CB    . LEU D 2 111 ? 129.338 89.961  139.273 1.00 19.87 ?  90  LEU D CB    1 
ATOM   14087 C  CG    . LEU D 2 111 ? 129.458 90.825  140.530 1.00 20.24 ?  90  LEU D CG    1 
ATOM   14088 C  CD1   . LEU D 2 111 ? 129.180 90.041  141.824 1.00 21.85 ?  90  LEU D CD1   1 
ATOM   14089 C  CD2   . LEU D 2 111 ? 130.824 91.534  140.588 1.00 20.29 ?  90  LEU D CD2   1 
ATOM   14090 N  N     . ASN D 2 112 ? 128.474 89.287  136.207 1.00 20.92 ?  91  ASN D N     1 
ATOM   14091 C  CA    . ASN D 2 112 ? 128.575 88.563  134.918 1.00 20.70 ?  91  ASN D CA    1 
ATOM   14092 C  C     . ASN D 2 112 ? 128.999 89.456  133.765 1.00 20.57 ?  91  ASN D C     1 
ATOM   14093 O  O     . ASN D 2 112 ? 129.751 89.030  132.874 1.00 20.45 ?  91  ASN D O     1 
ATOM   14094 C  CB    . ASN D 2 112 ? 127.234 87.945  134.519 1.00 21.16 ?  91  ASN D CB    1 
ATOM   14095 C  CG    . ASN D 2 112 ? 127.104 86.491  134.927 1.00 21.98 ?  91  ASN D CG    1 
ATOM   14096 O  OD1   . ASN D 2 112 ? 127.971 85.929  135.603 1.00 25.37 ?  91  ASN D OD1   1 
ATOM   14097 N  ND2   . ASN D 2 112 ? 125.999 85.881  134.538 1.00 21.12 ?  91  ASN D ND2   1 
ATOM   14098 N  N     . PHE D 2 113 ? 128.445 90.666  133.736 1.00 19.70 ?  92  PHE D N     1 
ATOM   14099 C  CA    . PHE D 2 113 ? 128.805 91.620  132.710 1.00 20.02 ?  92  PHE D CA    1 
ATOM   14100 C  C     . PHE D 2 113 ? 130.293 91.990  132.805 1.00 19.97 ?  92  PHE D C     1 
ATOM   14101 O  O     . PHE D 2 113 ? 130.998 92.028  131.791 1.00 19.22 ?  92  PHE D O     1 
ATOM   14102 C  CB    . PHE D 2 113 ? 127.918 92.876  132.748 1.00 20.09 ?  92  PHE D CB    1 
ATOM   14103 C  CG    . PHE D 2 113 ? 128.156 93.787  131.595 1.00 20.54 ?  92  PHE D CG    1 
ATOM   14104 C  CD1   . PHE D 2 113 ? 127.438 93.630  130.408 1.00 20.14 ?  92  PHE D CD1   1 
ATOM   14105 C  CD2   . PHE D 2 113 ? 129.149 94.766  131.667 1.00 20.77 ?  92  PHE D CD2   1 
ATOM   14106 C  CE1   . PHE D 2 113 ? 127.688 94.458  129.317 1.00 20.54 ?  92  PHE D CE1   1 
ATOM   14107 C  CE2   . PHE D 2 113 ? 129.409 95.594  130.576 1.00 21.23 ?  92  PHE D CE2   1 
ATOM   14108 C  CZ    . PHE D 2 113 ? 128.672 95.431  129.395 1.00 20.92 ?  92  PHE D CZ    1 
ATOM   14109 N  N     . MET D 2 114 ? 130.760 92.247  134.023 1.00 19.67 ?  93  MET D N     1 
ATOM   14110 C  CA    . MET D 2 114 ? 132.170 92.543  134.245 1.00 20.55 ?  93  MET D CA    1 
ATOM   14111 C  C     . MET D 2 114 ? 133.077 91.379  133.841 1.00 20.82 ?  93  MET D C     1 
ATOM   14112 O  O     . MET D 2 114 ? 134.101 91.616  133.215 1.00 20.43 ?  93  MET D O     1 
ATOM   14113 C  CB    . MET D 2 114 ? 132.422 92.948  135.693 1.00 20.24 ?  93  MET D CB    1 
ATOM   14114 C  CG    . MET D 2 114 ? 131.582 94.146  136.084 1.00 22.05 ?  93  MET D CG    1 
ATOM   14115 S  SD    . MET D 2 114 ? 131.663 94.571  137.809 1.00 25.85 ?  93  MET D SD    1 
ATOM   14116 C  CE    . MET D 2 114 ? 131.197 96.307  137.707 1.00 27.57 ?  93  MET D CE    1 
ATOM   14117 N  N     . ALA D 2 115 ? 132.696 90.143  134.195 1.00 21.19 ?  94  ALA D N     1 
ATOM   14118 C  CA    . ALA D 2 115 ? 133.460 88.948  133.785 1.00 21.53 ?  94  ALA D CA    1 
ATOM   14119 C  C     . ALA D 2 115 ? 133.520 88.839  132.263 1.00 21.75 ?  94  ALA D C     1 
ATOM   14120 O  O     . ALA D 2 115 ? 134.581 88.558  131.705 1.00 22.18 ?  94  ALA D O     1 
ATOM   14121 C  CB    . ALA D 2 115 ? 132.876 87.672  134.401 1.00 21.32 ?  94  ALA D CB    1 
ATOM   14122 N  N     . MET D 2 116 ? 132.390 89.091  131.598 1.00 21.47 ?  95  MET D N     1 
ATOM   14123 C  CA    . MET D 2 116 ? 132.339 89.120  130.139 1.00 21.83 ?  95  MET D CA    1 
ATOM   14124 C  C     . MET D 2 116 ? 133.362 90.111  129.550 1.00 22.15 ?  95  MET D C     1 
ATOM   14125 O  O     . MET D 2 116 ? 134.086 89.771  128.616 1.00 22.09 ?  95  MET D O     1 
ATOM   14126 C  CB    . MET D 2 116 ? 130.917 89.444  129.653 1.00 21.72 ?  95  MET D CB    1 
ATOM   14127 C  CG    . MET D 2 116 ? 130.768 89.600  128.131 1.00 22.57 ?  95  MET D CG    1 
ATOM   14128 S  SD    . MET D 2 116 ? 131.315 91.200  127.480 1.00 22.75 ?  95  MET D SD    1 
ATOM   14129 C  CE    . MET D 2 116 ? 130.107 92.315  128.193 1.00 22.96 ?  95  MET D CE    1 
ATOM   14130 N  N     . MET D 2 117 ? 133.412 91.326  130.099 1.00 22.04 ?  96  MET D N     1 
ATOM   14131 C  CA    . MET D 2 117 ? 134.351 92.355  129.618 1.00 22.45 ?  96  MET D CA    1 
ATOM   14132 C  C     . MET D 2 117 ? 135.813 91.892  129.736 1.00 22.39 ?  96  MET D C     1 
ATOM   14133 O  O     . MET D 2 117 ? 136.619 92.132  128.836 1.00 21.88 ?  96  MET D O     1 
ATOM   14134 C  CB    . MET D 2 117 ? 134.133 93.696  130.349 1.00 22.00 ?  96  MET D CB    1 
ATOM   14135 C  CG    . MET D 2 117 ? 132.827 94.426  129.941 1.00 23.25 ?  96  MET D CG    1 
ATOM   14136 S  SD    . MET D 2 117 ? 132.720 94.799  128.174 1.00 24.28 ?  96  MET D SD    1 
ATOM   14137 C  CE    . MET D 2 117 ? 133.905 96.130  128.013 1.00 24.59 ?  96  MET D CE    1 
ATOM   14138 N  N     . GLU D 2 118 ? 136.141 91.211  130.834 1.00 22.66 ?  97  GLU D N     1 
ATOM   14139 C  CA    . GLU D 2 118 ? 137.493 90.671  131.021 1.00 23.52 ?  97  GLU D CA    1 
ATOM   14140 C  C     . GLU D 2 118 ? 137.853 89.676  129.931 1.00 24.25 ?  97  GLU D C     1 
ATOM   14141 O  O     . GLU D 2 118 ? 138.906 89.803  129.303 1.00 25.05 ?  97  GLU D O     1 
ATOM   14142 C  CB    . GLU D 2 118 ? 137.679 90.004  132.404 1.00 23.11 ?  97  GLU D CB    1 
ATOM   14143 C  CG    . GLU D 2 118 ? 137.114 90.766  133.610 1.00 23.08 ?  97  GLU D CG    1 
ATOM   14144 C  CD    . GLU D 2 118 ? 137.858 92.048  133.949 1.00 24.08 ?  97  GLU D CD    1 
ATOM   14145 O  OE1   . GLU D 2 118 ? 138.622 92.544  133.107 1.00 26.39 ?  97  GLU D OE1   1 
ATOM   14146 O  OE2   . GLU D 2 118 ? 137.655 92.582  135.059 1.00 27.52 -1 97  GLU D OE2   1 
ATOM   14147 N  N     . ASN D 2 119 ? 136.967 88.709  129.702 1.00 25.47 ?  98  ASN D N     1 
ATOM   14148 C  CA    . ASN D 2 119 ? 137.240 87.551  128.826 1.00 26.32 ?  98  ASN D CA    1 
ATOM   14149 C  C     . ASN D 2 119 ? 137.009 87.793  127.338 1.00 26.22 ?  98  ASN D C     1 
ATOM   14150 O  O     . ASN D 2 119 ? 137.763 87.282  126.485 1.00 26.54 ?  98  ASN D O     1 
ATOM   14151 C  CB    . ASN D 2 119 ? 136.408 86.336  129.274 1.00 26.72 ?  98  ASN D CB    1 
ATOM   14152 C  CG    . ASN D 2 119 ? 136.815 85.828  130.657 1.00 29.12 ?  98  ASN D CG    1 
ATOM   14153 O  OD1   . ASN D 2 119 ? 137.991 85.543  130.909 1.00 32.07 ?  98  ASN D OD1   1 
ATOM   14154 N  ND2   . ASN D 2 119 ? 135.848 85.744  131.565 1.00 29.12 ?  98  ASN D ND2   1 
ATOM   14155 N  N     . ALA D 2 120 ? 135.957 88.546  127.034 1.00 25.46 ?  99  ALA D N     1 
ATOM   14156 C  CA    . ALA D 2 120 ? 135.533 88.763  125.651 1.00 25.77 ?  99  ALA D CA    1 
ATOM   14157 C  C     . ALA D 2 120 ? 136.098 90.041  125.038 1.00 25.51 ?  99  ALA D C     1 
ATOM   14158 O  O     . ALA D 2 120 ? 136.261 90.119  123.818 1.00 26.64 ?  99  ALA D O     1 
ATOM   14159 C  CB    . ALA D 2 120 ? 133.999 88.759  125.548 1.00 25.75 ?  99  ALA D CB    1 
ATOM   14160 N  N     . VAL D 2 121 ? 136.384 91.039  125.868 1.00 24.40 ?  100 VAL D N     1 
ATOM   14161 C  CA    . VAL D 2 121 ? 136.780 92.343  125.347 1.00 24.15 ?  100 VAL D CA    1 
ATOM   14162 C  C     . VAL D 2 121 ? 138.237 92.671  125.683 1.00 23.94 ?  100 VAL D C     1 
ATOM   14163 O  O     . VAL D 2 121 ? 139.058 92.867  124.782 1.00 23.75 ?  100 VAL D O     1 
ATOM   14164 C  CB    . VAL D 2 121 ? 135.812 93.471  125.819 1.00 23.68 ?  100 VAL D CB    1 
ATOM   14165 C  CG1   . VAL D 2 121 ? 136.224 94.820  125.229 1.00 23.76 ?  100 VAL D CG1   1 
ATOM   14166 C  CG2   . VAL D 2 121 ? 134.375 93.138  125.407 1.00 23.99 ?  100 VAL D CG2   1 
ATOM   14167 N  N     . HIS D 2 122 ? 138.551 92.721  126.976 1.00 23.68 ?  101 HIS D N     1 
ATOM   14168 C  CA    . HIS D 2 122 ? 139.906 93.046  127.426 1.00 24.02 ?  101 HIS D CA    1 
ATOM   14169 C  C     . HIS D 2 122 ? 140.950 92.063  126.922 1.00 24.39 ?  101 HIS D C     1 
ATOM   14170 O  O     . HIS D 2 122 ? 141.988 92.483  126.417 1.00 24.71 ?  101 HIS D O     1 
ATOM   14171 C  CB    . HIS D 2 122 ? 139.989 93.170  128.953 1.00 23.20 ?  101 HIS D CB    1 
ATOM   14172 C  CG    . HIS D 2 122 ? 139.173 94.291  129.515 1.00 22.82 ?  101 HIS D CG    1 
ATOM   14173 N  ND1   . HIS D 2 122 ? 139.068 94.525  130.869 1.00 20.48 ?  101 HIS D ND1   1 
ATOM   14174 C  CD2   . HIS D 2 122 ? 138.400 95.227  128.911 1.00 21.03 ?  101 HIS D CD2   1 
ATOM   14175 C  CE1   . HIS D 2 122 ? 138.281 95.564  131.074 1.00 19.88 ?  101 HIS D CE1   1 
ATOM   14176 N  NE2   . HIS D 2 122 ? 137.863 96.011  129.902 1.00 21.62 ?  101 HIS D NE2   1 
ATOM   14177 N  N     . ALA D 2 123 ? 140.678 90.764  127.045 1.00 25.30 ?  102 ALA D N     1 
ATOM   14178 C  CA    . ALA D 2 123 ? 141.668 89.748  126.656 1.00 25.77 ?  102 ALA D CA    1 
ATOM   14179 C  C     . ALA D 2 123 ? 141.980 89.785  125.156 1.00 26.37 ?  102 ALA D C     1 
ATOM   14180 O  O     . ALA D 2 123 ? 143.138 89.632  124.747 1.00 25.87 ?  102 ALA D O     1 
ATOM   14181 C  CB    . ALA D 2 123 ? 141.213 88.347  127.084 1.00 26.43 ?  102 ALA D CB    1 
ATOM   14182 N  N     . LYS D 2 124 ? 140.941 89.993  124.345 1.00 26.51 ?  103 LYS D N     1 
ATOM   14183 C  CA    . LYS D 2 124 ? 141.102 90.109  122.903 1.00 27.22 ?  103 LYS D CA    1 
ATOM   14184 C  C     . LYS D 2 124 ? 141.866 91.392  122.546 1.00 26.63 ?  103 LYS D C     1 
ATOM   14185 O  O     . LYS D 2 124 ? 142.669 91.396  121.612 1.00 26.07 ?  103 LYS D O     1 
ATOM   14186 C  CB    . LYS D 2 124 ? 139.732 90.062  122.197 1.00 27.51 ?  103 LYS D CB    1 
ATOM   14187 C  CG    . LYS D 2 124 ? 139.764 90.264  120.667 1.00 30.58 ?  103 LYS D CG    1 
ATOM   14188 C  CD    . LYS D 2 124 ? 140.445 89.110  119.945 1.00 35.72 ?  103 LYS D CD    1 
ATOM   14189 C  CE    . LYS D 2 124 ? 140.505 89.327  118.431 1.00 37.33 ?  103 LYS D CE    1 
ATOM   14190 N  NZ    . LYS D 2 124 ? 139.137 89.318  117.846 1.00 40.73 1  103 LYS D NZ    1 
ATOM   14191 N  N     . SER D 2 125 ? 141.622 92.461  123.309 1.00 26.02 ?  104 SER D N     1 
ATOM   14192 C  CA    . SER D 2 125 ? 142.269 93.757  123.091 1.00 26.16 ?  104 SER D CA    1 
ATOM   14193 C  C     . SER D 2 125 ? 143.776 93.702  123.342 1.00 26.18 ?  104 SER D C     1 
ATOM   14194 O  O     . SER D 2 125 ? 144.557 94.254  122.558 1.00 26.06 ?  104 SER D O     1 
ATOM   14195 C  CB    . SER D 2 125 ? 141.635 94.844  123.963 1.00 26.10 ?  104 SER D CB    1 
ATOM   14196 O  OG    . SER D 2 125 ? 140.292 95.065  123.570 1.00 26.58 ?  104 SER D OG    1 
ATOM   14197 N  N     . TYR D 2 126 ? 144.171 93.041  124.427 1.00 25.68 ?  105 TYR D N     1 
ATOM   14198 C  CA    . TYR D 2 126 ? 145.591 92.857  124.752 1.00 26.12 ?  105 TYR D CA    1 
ATOM   14199 C  C     . TYR D 2 126 ? 146.286 92.010  123.680 1.00 26.38 ?  105 TYR D C     1 
ATOM   14200 O  O     . TYR D 2 126 ? 147.389 92.334  123.236 1.00 26.83 ?  105 TYR D O     1 
ATOM   14201 C  CB    . TYR D 2 126 ? 145.772 92.201  126.134 1.00 25.35 ?  105 TYR D CB    1 
ATOM   14202 C  CG    . TYR D 2 126 ? 145.599 93.132  127.318 1.00 25.46 ?  105 TYR D CG    1 
ATOM   14203 C  CD1   . TYR D 2 126 ? 146.357 94.299  127.426 1.00 25.41 ?  105 TYR D CD1   1 
ATOM   14204 C  CD2   . TYR D 2 126 ? 144.700 92.832  128.353 1.00 24.77 ?  105 TYR D CD2   1 
ATOM   14205 C  CE1   . TYR D 2 126 ? 146.211 95.161  128.511 1.00 25.89 ?  105 TYR D CE1   1 
ATOM   14206 C  CE2   . TYR D 2 126 ? 144.545 93.695  129.449 1.00 23.11 ?  105 TYR D CE2   1 
ATOM   14207 C  CZ    . TYR D 2 126 ? 145.315 94.847  129.526 1.00 25.38 ?  105 TYR D CZ    1 
ATOM   14208 O  OH    . TYR D 2 126 ? 145.192 95.715  130.589 1.00 23.31 ?  105 TYR D OH    1 
ATOM   14209 N  N     . SER D 2 127 ? 145.622 90.940  123.256 1.00 27.16 ?  106 SER D N     1 
ATOM   14210 C  CA    . SER D 2 127 ? 146.144 90.070  122.197 1.00 27.83 ?  106 SER D CA    1 
ATOM   14211 C  C     . SER D 2 127 ? 146.362 90.852  120.894 1.00 28.21 ?  106 SER D C     1 
ATOM   14212 O  O     . SER D 2 127 ? 147.431 90.747  120.277 1.00 28.30 ?  106 SER D O     1 
ATOM   14213 C  CB    . SER D 2 127 ? 145.209 88.869  121.977 1.00 28.37 ?  106 SER D CB    1 
ATOM   14214 O  OG    . SER D 2 127 ? 145.637 88.067  120.878 1.00 29.33 ?  106 SER D OG    1 
ATOM   14215 N  N     . ASN D 2 128 ? 145.355 91.636  120.496 1.00 28.27 ?  107 ASN D N     1 
ATOM   14216 C  CA    . ASN D 2 128 ? 145.429 92.522  119.323 1.00 28.79 ?  107 ASN D CA    1 
ATOM   14217 C  C     . ASN D 2 128 ? 146.603 93.496  119.358 1.00 28.53 ?  107 ASN D C     1 
ATOM   14218 O  O     . ASN D 2 128 ? 147.294 93.668  118.348 1.00 28.03 ?  107 ASN D O     1 
ATOM   14219 C  CB    . ASN D 2 128 ? 144.123 93.313  119.127 1.00 29.05 ?  107 ASN D CB    1 
ATOM   14220 C  CG    . ASN D 2 128 ? 142.955 92.433  118.674 1.00 30.48 ?  107 ASN D CG    1 
ATOM   14221 O  OD1   . ASN D 2 128 ? 143.137 91.272  118.314 1.00 32.19 ?  107 ASN D OD1   1 
ATOM   14222 N  ND2   . ASN D 2 128 ? 141.747 92.986  118.712 1.00 31.59 ?  107 ASN D ND2   1 
ATOM   14223 N  N     . ILE D 2 129 ? 146.811 94.149  120.503 1.00 28.21 ?  108 ILE D N     1 
ATOM   14224 C  CA    . ILE D 2 129 ? 147.962 95.049  120.661 1.00 28.76 ?  108 ILE D CA    1 
ATOM   14225 C  C     . ILE D 2 129 ? 149.283 94.293  120.439 1.00 29.83 ?  108 ILE D C     1 
ATOM   14226 O  O     . ILE D 2 129 ? 150.150 94.748  119.680 1.00 29.99 ?  108 ILE D O     1 
ATOM   14227 C  CB    . ILE D 2 129 ? 147.964 95.793  122.035 1.00 28.28 ?  108 ILE D CB    1 
ATOM   14228 C  CG1   . ILE D 2 129 ? 146.739 96.710  122.164 1.00 27.94 ?  108 ILE D CG1   1 
ATOM   14229 C  CG2   . ILE D 2 129 ? 149.249 96.618  122.199 1.00 27.52 ?  108 ILE D CG2   1 
ATOM   14230 C  CD1   . ILE D 2 129 ? 146.463 97.187  123.585 1.00 27.98 ?  108 ILE D CD1   1 
ATOM   14231 N  N     . PHE D 2 130 ? 149.431 93.145  121.094 1.00 30.86 ?  109 PHE D N     1 
ATOM   14232 C  CA    . PHE D 2 130 ? 150.626 92.321  120.936 1.00 32.76 ?  109 PHE D CA    1 
ATOM   14233 C  C     . PHE D 2 130 ? 150.897 91.918  119.484 1.00 34.37 ?  109 PHE D C     1 
ATOM   14234 O  O     . PHE D 2 130 ? 151.995 92.136  118.976 1.00 34.61 ?  109 PHE D O     1 
ATOM   14235 C  CB    . PHE D 2 130 ? 150.547 91.072  121.811 1.00 32.81 ?  109 PHE D CB    1 
ATOM   14236 C  CG    . PHE D 2 130 ? 151.239 91.213  123.136 1.00 33.84 ?  109 PHE D CG    1 
ATOM   14237 C  CD1   . PHE D 2 130 ? 152.627 91.320  123.203 1.00 34.61 ?  109 PHE D CD1   1 
ATOM   14238 C  CD2   . PHE D 2 130 ? 150.508 91.203  124.318 1.00 35.74 ?  109 PHE D CD2   1 
ATOM   14239 C  CE1   . PHE D 2 130 ? 153.278 91.439  124.430 1.00 36.99 ?  109 PHE D CE1   1 
ATOM   14240 C  CE2   . PHE D 2 130 ? 151.148 91.321  125.558 1.00 36.96 ?  109 PHE D CE2   1 
ATOM   14241 C  CZ    . PHE D 2 130 ? 152.536 91.439  125.615 1.00 36.91 ?  109 PHE D CZ    1 
ATOM   14242 N  N     . MET D 2 131 ? 149.887 91.346  118.828 1.00 35.90 ?  110 MET D N     1 
ATOM   14243 C  CA    . MET D 2 131 ? 150.002 90.868  117.449 1.00 37.94 ?  110 MET D CA    1 
ATOM   14244 C  C     . MET D 2 131 ? 150.359 91.983  116.476 1.00 38.05 ?  110 MET D C     1 
ATOM   14245 O  O     . MET D 2 131 ? 150.985 91.729  115.452 1.00 38.20 ?  110 MET D O     1 
ATOM   14246 C  CB    . MET D 2 131 ? 148.712 90.168  116.992 1.00 38.63 ?  110 MET D CB    1 
ATOM   14247 C  CG    . MET D 2 131 ? 148.419 88.834  117.699 1.00 42.34 ?  110 MET D CG    1 
ATOM   14248 S  SD    . MET D 2 131 ? 146.895 88.001  117.146 1.00 50.15 ?  110 MET D SD    1 
ATOM   14249 C  CE    . MET D 2 131 ? 145.599 89.072  117.785 1.00 48.14 ?  110 MET D CE    1 
ATOM   14250 N  N     . THR D 2 132 ? 149.959 93.212  116.800 1.00 38.12 ?  111 THR D N     1 
ATOM   14251 C  CA    . THR D 2 132 ? 150.280 94.370  115.965 1.00 38.79 ?  111 THR D CA    1 
ATOM   14252 C  C     . THR D 2 132 ? 151.757 94.786  116.089 1.00 38.81 ?  111 THR D C     1 
ATOM   14253 O  O     . THR D 2 132 ? 152.401 95.095  115.081 1.00 39.26 ?  111 THR D O     1 
ATOM   14254 C  CB    . THR D 2 132 ? 149.354 95.562  116.281 1.00 38.78 ?  111 THR D CB    1 
ATOM   14255 O  OG1   . THR D 2 132 ? 147.990 95.162  116.105 1.00 39.32 ?  111 THR D OG1   1 
ATOM   14256 C  CG2   . THR D 2 132 ? 149.635 96.738  115.351 1.00 39.75 ?  111 THR D CG2   1 
ATOM   14257 N  N     . LEU D 2 133 ? 152.280 94.776  117.316 1.00 38.34 ?  112 LEU D N     1 
ATOM   14258 C  CA    . LEU D 2 133 ? 153.608 95.319  117.619 1.00 38.36 ?  112 LEU D CA    1 
ATOM   14259 C  C     . LEU D 2 133 ? 154.760 94.316  117.528 1.00 38.94 ?  112 LEU D C     1 
ATOM   14260 O  O     . LEU D 2 133 ? 155.884 94.694  117.202 1.00 39.14 ?  112 LEU D O     1 
ATOM   14261 C  CB    . LEU D 2 133 ? 153.619 95.969  119.013 1.00 37.62 ?  112 LEU D CB    1 
ATOM   14262 C  CG    . LEU D 2 133 ? 152.587 97.058  119.319 1.00 36.50 ?  112 LEU D CG    1 
ATOM   14263 C  CD1   . LEU D 2 133 ? 152.597 97.397  120.813 1.00 35.80 ?  112 LEU D CD1   1 
ATOM   14264 C  CD2   . LEU D 2 133 ? 152.798 98.304  118.476 1.00 35.32 ?  112 LEU D CD2   1 
ATOM   14265 N  N     . ALA D 2 134 ? 154.499 93.049  117.826 1.00 39.41 ?  113 ALA D N     1 
ATOM   14266 C  CA    . ALA D 2 134 ? 155.580 92.057  117.822 1.00 40.33 ?  113 ALA D CA    1 
ATOM   14267 C  C     . ALA D 2 134 ? 155.275 90.857  116.930 1.00 41.05 ?  113 ALA D C     1 
ATOM   14268 O  O     . ALA D 2 134 ? 154.113 90.504  116.762 1.00 40.81 ?  113 ALA D O     1 
ATOM   14269 C  CB    . ALA D 2 134 ? 155.880 91.604  119.239 1.00 40.15 ?  113 ALA D CB    1 
ATOM   14270 N  N     . PRO D 2 135 ? 156.319 90.231  116.345 1.00 42.21 ?  114 PRO D N     1 
ATOM   14271 C  CA    . PRO D 2 135 ? 156.085 88.966  115.639 1.00 43.27 ?  114 PRO D CA    1 
ATOM   14272 C  C     . PRO D 2 135 ? 155.809 87.822  116.626 1.00 43.89 ?  114 PRO D C     1 
ATOM   14273 O  O     . PRO D 2 135 ? 156.162 87.927  117.804 1.00 43.31 ?  114 PRO D O     1 
ATOM   14274 C  CB    . PRO D 2 135 ? 157.399 88.728  114.890 1.00 43.69 ?  114 PRO D CB    1 
ATOM   14275 C  CG    . PRO D 2 135 ? 158.420 89.442  115.690 1.00 43.01 ?  114 PRO D CG    1 
ATOM   14276 C  CD    . PRO D 2 135 ? 157.735 90.642  116.283 1.00 42.16 ?  114 PRO D CD    1 
ATOM   14277 N  N     . THR D 2 136 ? 155.196 86.746  116.135 1.00 45.26 ?  115 THR D N     1 
ATOM   14278 C  CA    . THR D 2 136 ? 154.749 85.622  116.974 1.00 46.11 ?  115 THR D CA    1 
ATOM   14279 C  C     . THR D 2 136 ? 155.829 85.108  117.931 1.00 46.35 ?  115 THR D C     1 
ATOM   14280 O  O     . THR D 2 136 ? 155.558 84.906  119.119 1.00 46.25 ?  115 THR D O     1 
ATOM   14281 C  CB    . THR D 2 136 ? 154.173 84.458  116.122 1.00 46.59 ?  115 THR D CB    1 
ATOM   14282 O  OG1   . THR D 2 136 ? 153.153 84.965  115.255 1.00 47.80 ?  115 THR D OG1   1 
ATOM   14283 C  CG2   . THR D 2 136 ? 153.550 83.375  117.002 1.00 46.94 ?  115 THR D CG2   1 
ATOM   14284 N  N     . GLU D 2 137 ? 157.047 84.921  117.421 1.00 46.92 ?  116 GLU D N     1 
ATOM   14285 C  CA    . GLU D 2 137 ? 158.148 84.401  118.231 1.00 47.37 ?  116 GLU D CA    1 
ATOM   14286 C  C     . GLU D 2 137 ? 158.520 85.318  119.399 1.00 46.64 ?  116 GLU D C     1 
ATOM   14287 O  O     . GLU D 2 137 ? 158.826 84.833  120.489 1.00 46.89 ?  116 GLU D O     1 
ATOM   14288 C  CB    . GLU D 2 137 ? 159.379 84.090  117.366 1.00 48.04 ?  116 GLU D CB    1 
ATOM   14289 C  CG    . GLU D 2 137 ? 160.544 83.419  118.118 1.00 49.86 ?  116 GLU D CG    1 
ATOM   14290 C  CD    . GLU D 2 137 ? 160.272 81.964  118.528 1.00 52.40 ?  116 GLU D CD    1 
ATOM   14291 O  OE1   . GLU D 2 137 ? 159.243 81.690  119.186 1.00 52.97 ?  116 GLU D OE1   1 
ATOM   14292 O  OE2   . GLU D 2 137 ? 161.111 81.089  118.211 1.00 54.12 -1 116 GLU D OE2   1 
ATOM   14293 N  N     . THR D 2 138 ? 158.487 86.629  119.165 1.00 46.09 ?  117 THR D N     1 
ATOM   14294 C  CA    . THR D 2 138 ? 158.763 87.627  120.210 1.00 45.30 ?  117 THR D CA    1 
ATOM   14295 C  C     . THR D 2 138 ? 157.690 87.624  121.306 1.00 44.63 ?  117 THR D C     1 
ATOM   14296 O  O     . THR D 2 138 ? 158.007 87.743  122.493 1.00 44.51 ?  117 THR D O     1 
ATOM   14297 C  CB    . THR D 2 138 ? 158.906 89.047  119.614 1.00 45.20 ?  117 THR D CB    1 
ATOM   14298 O  OG1   . THR D 2 138 ? 159.933 89.044  118.617 1.00 45.69 ?  117 THR D OG1   1 
ATOM   14299 C  CG2   . THR D 2 138 ? 159.267 90.072  120.689 1.00 44.67 ?  117 THR D CG2   1 
ATOM   14300 N  N     . ILE D 2 139 ? 156.426 87.479  120.905 1.00 44.24 ?  118 ILE D N     1 
ATOM   14301 C  CA    . ILE D 2 139 ? 155.316 87.400  121.858 1.00 43.65 ?  118 ILE D CA    1 
ATOM   14302 C  C     . ILE D 2 139 ? 155.483 86.187  122.785 1.00 43.87 ?  118 ILE D C     1 
ATOM   14303 O  O     . ILE D 2 139 ? 155.398 86.316  124.009 1.00 43.36 ?  118 ILE D O     1 
ATOM   14304 C  CB    . ILE D 2 139 ? 153.944 87.392  121.137 1.00 43.68 ?  118 ILE D CB    1 
ATOM   14305 C  CG1   . ILE D 2 139 ? 153.698 88.748  120.457 1.00 43.30 ?  118 ILE D CG1   1 
ATOM   14306 C  CG2   . ILE D 2 139 ? 152.802 87.061  122.115 1.00 43.11 ?  118 ILE D CG2   1 
ATOM   14307 C  CD1   . ILE D 2 139 ? 152.600 88.751  119.401 1.00 43.41 ?  118 ILE D CD1   1 
ATOM   14308 N  N     . ASN D 2 140 ? 155.750 85.022  122.195 1.00 44.52 ?  119 ASN D N     1 
ATOM   14309 C  CA    . ASN D 2 140 ? 155.966 83.789  122.960 1.00 45.00 ?  119 ASN D CA    1 
ATOM   14310 C  C     . ASN D 2 140 ? 157.116 83.903  123.983 1.00 44.99 ?  119 ASN D C     1 
ATOM   14311 O  O     . ASN D 2 140 ? 156.997 83.418  125.115 1.00 44.61 ?  119 ASN D O     1 
ATOM   14312 C  CB    . ASN D 2 140 ? 156.177 82.591  122.018 1.00 45.74 ?  119 ASN D CB    1 
ATOM   14313 C  CG    . ASN D 2 140 ? 154.970 82.320  121.113 1.00 46.40 ?  119 ASN D CG    1 
ATOM   14314 O  OD1   . ASN D 2 140 ? 153.864 82.820  121.345 1.00 46.85 ?  119 ASN D OD1   1 
ATOM   14315 N  ND2   . ASN D 2 140 ? 155.183 81.512  120.076 1.00 48.16 ?  119 ASN D ND2   1 
ATOM   14316 N  N     . GLU D 2 141 ? 158.206 84.567  123.591 1.00 45.09 ?  120 GLU D N     1 
ATOM   14317 C  CA    . GLU D 2 141 ? 159.363 84.755  124.471 1.00 45.27 ?  120 GLU D CA    1 
ATOM   14318 C  C     . GLU D 2 141 ? 159.098 85.718  125.638 1.00 44.75 ?  120 GLU D C     1 
ATOM   14319 O  O     . GLU D 2 141 ? 159.511 85.455  126.773 1.00 44.37 ?  120 GLU D O     1 
ATOM   14320 C  CB    . GLU D 2 141 ? 160.587 85.212  123.677 1.00 45.75 ?  120 GLU D CB    1 
ATOM   14321 C  CG    . GLU D 2 141 ? 161.153 84.146  122.737 1.00 48.17 ?  120 GLU D CG    1 
ATOM   14322 C  CD    . GLU D 2 141 ? 162.400 84.598  122.006 1.00 50.15 ?  120 GLU D CD    1 
ATOM   14323 O  OE1   . GLU D 2 141 ? 163.337 85.102  122.661 1.00 50.90 ?  120 GLU D OE1   1 
ATOM   14324 O  OE2   . GLU D 2 141 ? 162.447 84.442  120.768 1.00 52.25 -1 120 GLU D OE2   1 
ATOM   14325 N  N     . VAL D 2 142 ? 158.428 86.833  125.348 1.00 44.31 ?  121 VAL D N     1 
ATOM   14326 C  CA    . VAL D 2 142 ? 158.050 87.804  126.376 1.00 43.91 ?  121 VAL D CA    1 
ATOM   14327 C  C     . VAL D 2 142 ? 157.141 87.154  127.424 1.00 43.71 ?  121 VAL D C     1 
ATOM   14328 O  O     . VAL D 2 142 ? 157.325 87.358  128.623 1.00 43.44 ?  121 VAL D O     1 
ATOM   14329 C  CB    . VAL D 2 142 ? 157.368 89.061  125.768 1.00 43.65 ?  121 VAL D CB    1 
ATOM   14330 C  CG1   . VAL D 2 142 ? 156.866 89.997  126.868 1.00 43.40 ?  121 VAL D CG1   1 
ATOM   14331 C  CG2   . VAL D 2 142 ? 158.340 89.807  124.859 1.00 43.96 ?  121 VAL D CG2   1 
ATOM   14332 N  N     . PHE D 2 143 ? 156.175 86.362  126.967 1.00 44.03 ?  122 PHE D N     1 
ATOM   14333 C  CA    . PHE D 2 143 ? 155.276 85.670  127.884 1.00 44.42 ?  122 PHE D CA    1 
ATOM   14334 C  C     . PHE D 2 143 ? 155.975 84.584  128.695 1.00 45.38 ?  122 PHE D C     1 
ATOM   14335 O  O     . PHE D 2 143 ? 155.656 84.393  129.865 1.00 45.50 ?  122 PHE D O     1 
ATOM   14336 C  CB    . PHE D 2 143 ? 154.032 85.140  127.167 1.00 44.27 ?  122 PHE D CB    1 
ATOM   14337 C  CG    . PHE D 2 143 ? 152.931 86.154  127.081 1.00 43.28 ?  122 PHE D CG    1 
ATOM   14338 C  CD1   . PHE D 2 143 ? 152.075 86.360  128.162 1.00 42.17 ?  122 PHE D CD1   1 
ATOM   14339 C  CD2   . PHE D 2 143 ? 152.770 86.929  125.941 1.00 42.76 ?  122 PHE D CD2   1 
ATOM   14340 C  CE1   . PHE D 2 143 ? 151.063 87.310  128.101 1.00 42.16 ?  122 PHE D CE1   1 
ATOM   14341 C  CE2   . PHE D 2 143 ? 151.761 87.883  125.868 1.00 42.77 ?  122 PHE D CE2   1 
ATOM   14342 C  CZ    . PHE D 2 143 ? 150.904 88.075  126.951 1.00 42.28 ?  122 PHE D CZ    1 
ATOM   14343 N  N     . GLU D 2 144 ? 156.938 83.901  128.081 1.00 46.18 ?  123 GLU D N     1 
ATOM   14344 C  CA    . GLU D 2 144 ? 157.801 82.968  128.805 1.00 47.19 ?  123 GLU D CA    1 
ATOM   14345 C  C     . GLU D 2 144 ? 158.576 83.679  129.925 1.00 46.99 ?  123 GLU D C     1 
ATOM   14346 O  O     . GLU D 2 144 ? 158.641 83.168  131.047 1.00 46.94 ?  123 GLU D O     1 
ATOM   14347 C  CB    . GLU D 2 144 ? 158.764 82.267  127.837 1.00 47.80 ?  123 GLU D CB    1 
ATOM   14348 C  CG    . GLU D 2 144 ? 159.623 81.156  128.450 1.00 49.54 ?  123 GLU D CG    1 
ATOM   14349 C  CD    . GLU D 2 144 ? 160.644 80.578  127.465 1.00 52.37 ?  123 GLU D CD    1 
ATOM   14350 O  OE1   . GLU D 2 144 ? 161.329 81.360  126.765 1.00 52.92 ?  123 GLU D OE1   1 
ATOM   14351 O  OE2   . GLU D 2 144 ? 160.768 79.337  127.395 1.00 53.55 -1 123 GLU D OE2   1 
ATOM   14352 N  N     . TRP D 2 145 ? 159.149 84.848  129.612 1.00 47.02 ?  124 TRP D N     1 
ATOM   14353 C  CA    . TRP D 2 145 ? 159.921 85.652  130.576 1.00 46.93 ?  124 TRP D CA    1 
ATOM   14354 C  C     . TRP D 2 145 ? 159.045 86.150  131.716 1.00 46.55 ?  124 TRP D C     1 
ATOM   14355 O  O     . TRP D 2 145 ? 159.375 85.963  132.884 1.00 46.42 ?  124 TRP D O     1 
ATOM   14356 C  CB    . TRP D 2 145 ? 160.590 86.853  129.888 1.00 47.07 ?  124 TRP D CB    1 
ATOM   14357 C  CG    . TRP D 2 145 ? 161.579 87.634  130.758 1.00 47.82 ?  124 TRP D CG    1 
ATOM   14358 C  CD1   . TRP D 2 145 ? 162.933 87.441  130.834 1.00 48.78 ?  124 TRP D CD1   1 
ATOM   14359 C  CD2   . TRP D 2 145 ? 161.286 88.735  131.643 1.00 47.80 ?  124 TRP D CD2   1 
ATOM   14360 N  NE1   . TRP D 2 145 ? 163.498 88.341  131.711 1.00 49.06 ?  124 TRP D NE1   1 
ATOM   14361 C  CE2   . TRP D 2 145 ? 162.512 89.144  132.224 1.00 48.24 ?  124 TRP D CE2   1 
ATOM   14362 C  CE3   . TRP D 2 145 ? 160.111 89.408  132.007 1.00 47.65 ?  124 TRP D CE3   1 
ATOM   14363 C  CZ2   . TRP D 2 145 ? 162.594 90.197  133.150 1.00 47.74 ?  124 TRP D CZ2   1 
ATOM   14364 C  CZ3   . TRP D 2 145 ? 160.192 90.456  132.927 1.00 46.92 ?  124 TRP D CZ3   1 
ATOM   14365 C  CH2   . TRP D 2 145 ? 161.430 90.838  133.486 1.00 47.88 ?  124 TRP D CH2   1 
ATOM   14366 N  N     . VAL D 2 146 ? 157.930 86.787  131.371 1.00 46.09 ?  125 VAL D N     1 
ATOM   14367 C  CA    . VAL D 2 146 ? 157.044 87.373  132.370 1.00 45.36 ?  125 VAL D CA    1 
ATOM   14368 C  C     . VAL D 2 146 ? 156.384 86.273  133.217 1.00 45.28 ?  125 VAL D C     1 
ATOM   14369 O  O     . VAL D 2 146 ? 156.147 86.463  134.415 1.00 45.29 ?  125 VAL D O     1 
ATOM   14370 C  CB    . VAL D 2 146 ? 156.048 88.386  131.717 1.00 45.33 ?  125 VAL D CB    1 
ATOM   14371 C  CG1   . VAL D 2 146 ? 155.030 88.886  132.709 1.00 44.97 ?  125 VAL D CG1   1 
ATOM   14372 C  CG2   . VAL D 2 146 ? 156.817 89.580  131.148 1.00 44.52 ?  125 VAL D CG2   1 
ATOM   14373 N  N     . LYS D 2 147 ? 156.142 85.112  132.607 1.00 44.98 ?  126 LYS D N     1 
ATOM   14374 C  CA    . LYS D 2 147 ? 155.613 83.947  133.328 1.00 44.65 ?  126 LYS D CA    1 
ATOM   14375 C  C     . LYS D 2 147 ? 156.575 83.421  134.405 1.00 44.06 ?  126 LYS D C     1 
ATOM   14376 O  O     . LYS D 2 147 ? 156.141 82.863  135.415 1.00 44.65 ?  126 LYS D O     1 
ATOM   14377 C  CB    . LYS D 2 147 ? 155.259 82.812  132.363 1.00 45.31 ?  126 LYS D CB    1 
ATOM   14378 C  CG    . LYS D 2 147 ? 153.908 82.170  132.646 1.00 46.54 ?  126 LYS D CG    1 
ATOM   14379 C  CD    . LYS D 2 147 ? 153.942 80.645  132.533 1.00 49.06 ?  126 LYS D CD    1 
ATOM   14380 C  CE    . LYS D 2 147 ? 154.351 79.997  133.863 1.00 50.46 ?  126 LYS D CE    1 
ATOM   14381 N  NZ    . LYS D 2 147 ? 153.820 78.609  134.016 1.00 51.33 1  126 LYS D NZ    1 
ATOM   14382 N  N     . GLN D 2 148 ? 157.875 83.598  134.184 1.00 42.58 ?  127 GLN D N     1 
ATOM   14383 C  CA    . GLN D 2 148 ? 158.897 83.162  135.134 1.00 41.39 ?  127 GLN D CA    1 
ATOM   14384 C  C     . GLN D 2 148 ? 159.316 84.274  136.105 1.00 39.56 ?  127 GLN D C     1 
ATOM   14385 O  O     . GLN D 2 148 ? 159.940 83.999  137.129 1.00 39.77 ?  127 GLN D O     1 
ATOM   14386 C  CB    . GLN D 2 148 ? 160.106 82.587  134.369 1.00 42.11 ?  127 GLN D CB    1 
ATOM   14387 C  CG    . GLN D 2 148 ? 161.480 82.831  134.987 1.00 44.08 ?  127 GLN D CG    1 
ATOM   14388 C  CD    . GLN D 2 148 ? 162.220 84.022  134.375 1.00 46.12 ?  127 GLN D CD    1 
ATOM   14389 O  OE1   . GLN D 2 148 ? 161.633 85.080  134.109 1.00 46.47 ?  127 GLN D OE1   1 
ATOM   14390 N  NE2   . GLN D 2 148 ? 163.526 83.855  134.163 1.00 45.69 ?  127 GLN D NE2   1 
ATOM   14391 N  N     . ASN D 2 149 ? 158.958 85.519  135.782 1.00 36.99 ?  128 ASN D N     1 
ATOM   14392 C  CA    . ASN D 2 149 ? 159.345 86.682  136.581 1.00 34.54 ?  128 ASN D CA    1 
ATOM   14393 C  C     . ASN D 2 149 ? 158.853 86.639  138.030 1.00 33.13 ?  128 ASN D C     1 
ATOM   14394 O  O     . ASN D 2 149 ? 157.661 86.488  138.288 1.00 32.62 ?  128 ASN D O     1 
ATOM   14395 C  CB    . ASN D 2 149 ? 158.878 87.977  135.913 1.00 34.24 ?  128 ASN D CB    1 
ATOM   14396 C  CG    . ASN D 2 149 ? 159.362 89.209  136.651 1.00 33.83 ?  128 ASN D CG    1 
ATOM   14397 O  OD1   . ASN D 2 149 ? 158.616 89.820  137.418 1.00 32.21 ?  128 ASN D OD1   1 
ATOM   14398 N  ND2   . ASN D 2 149 ? 160.630 89.560  136.446 1.00 33.26 ?  128 ASN D ND2   1 
ATOM   14399 N  N     . LYS D 2 150 ? 159.785 86.808  138.963 1.00 31.49 ?  129 LYS D N     1 
ATOM   14400 C  CA    . LYS D 2 150 ? 159.517 86.672  140.393 1.00 30.68 ?  129 LYS D CA    1 
ATOM   14401 C  C     . LYS D 2 150 ? 158.465 87.664  140.946 1.00 28.95 ?  129 LYS D C     1 
ATOM   14402 O  O     . LYS D 2 150 ? 157.612 87.284  141.756 1.00 27.90 ?  129 LYS D O     1 
ATOM   14403 C  CB    . LYS D 2 150 ? 160.850 86.773  141.149 1.00 31.17 ?  129 LYS D CB    1 
ATOM   14404 C  CG    . LYS D 2 150 ? 160.789 87.010  142.644 1.00 33.66 ?  129 LYS D CG    1 
ATOM   14405 C  CD    . LYS D 2 150 ? 162.217 87.109  143.202 1.00 38.08 ?  129 LYS D CD    1 
ATOM   14406 C  CE    . LYS D 2 150 ? 162.280 87.936  144.492 1.00 40.20 ?  129 LYS D CE    1 
ATOM   14407 N  NZ    . LYS D 2 150 ? 162.140 87.097  145.713 1.00 42.60 1  129 LYS D NZ    1 
ATOM   14408 N  N     . TYR D 2 151 ? 158.529 88.922  140.512 1.00 27.36 ?  130 TYR D N     1 
ATOM   14409 C  CA    . TYR D 2 151 ? 157.648 89.968  141.063 1.00 26.56 ?  130 TYR D CA    1 
ATOM   14410 C  C     . TYR D 2 151 ? 156.241 89.898  140.492 1.00 25.66 ?  130 TYR D C     1 
ATOM   14411 O  O     . TYR D 2 151 ? 155.272 90.123  141.224 1.00 25.61 ?  130 TYR D O     1 
ATOM   14412 C  CB    . TYR D 2 151 ? 158.264 91.372  140.902 1.00 26.32 ?  130 TYR D CB    1 
ATOM   14413 C  CG    . TYR D 2 151 ? 159.728 91.395  141.297 1.00 27.20 ?  130 TYR D CG    1 
ATOM   14414 C  CD1   . TYR D 2 151 ? 160.105 91.258  142.633 1.00 27.31 ?  130 TYR D CD1   1 
ATOM   14415 C  CD2   . TYR D 2 151 ? 160.732 91.496  140.335 1.00 27.22 ?  130 TYR D CD2   1 
ATOM   14416 C  CE1   . TYR D 2 151 ? 161.448 91.243  143.006 1.00 29.65 ?  130 TYR D CE1   1 
ATOM   14417 C  CE2   . TYR D 2 151 ? 162.088 91.483  140.699 1.00 28.75 ?  130 TYR D CE2   1 
ATOM   14418 C  CZ    . TYR D 2 151 ? 162.426 91.364  142.050 1.00 29.17 ?  130 TYR D CZ    1 
ATOM   14419 O  OH    . TYR D 2 151 ? 163.742 91.348  142.454 1.00 30.61 ?  130 TYR D OH    1 
ATOM   14420 N  N     . LEU D 2 152 ? 156.133 89.585  139.199 1.00 24.87 ?  131 LEU D N     1 
ATOM   14421 C  CA    . LEU D 2 152 ? 154.829 89.351  138.587 1.00 24.37 ?  131 LEU D CA    1 
ATOM   14422 C  C     . LEU D 2 152 ? 154.157 88.127  139.220 1.00 24.18 ?  131 LEU D C     1 
ATOM   14423 O  O     . LEU D 2 152 ? 153.008 88.210  139.653 1.00 23.16 ?  131 LEU D O     1 
ATOM   14424 C  CB    . LEU D 2 152 ? 154.906 89.194  137.065 1.00 24.45 ?  131 LEU D CB    1 
ATOM   14425 C  CG    . LEU D 2 152 ? 153.454 89.007  136.588 1.00 26.33 ?  131 LEU D CG    1 
ATOM   14426 C  CD1   . LEU D 2 152 ? 152.686 90.335  136.635 1.00 25.00 ?  131 LEU D CD1   1 
ATOM   14427 C  CD2   . LEU D 2 152 ? 153.329 88.335  135.251 1.00 29.15 ?  131 LEU D CD2   1 
ATOM   14428 N  N     . GLN D 2 153 ? 154.885 87.011  139.301 1.00 24.07 ?  132 GLN D N     1 
ATOM   14429 C  CA    . GLN D 2 153 ? 154.352 85.797  139.953 1.00 24.99 ?  132 GLN D CA    1 
ATOM   14430 C  C     . GLN D 2 153 ? 153.937 86.014  141.406 1.00 24.24 ?  132 GLN D C     1 
ATOM   14431 O  O     . GLN D 2 153 ? 152.860 85.559  141.831 1.00 23.75 ?  132 GLN D O     1 
ATOM   14432 C  CB    . GLN D 2 153 ? 155.322 84.610  139.830 1.00 25.84 ?  132 GLN D CB    1 
ATOM   14433 C  CG    . GLN D 2 153 ? 155.425 84.040  138.390 1.00 28.48 ?  132 GLN D CG    1 
ATOM   14434 C  CD    . GLN D 2 153 ? 154.094 83.503  137.840 1.00 30.95 ?  132 GLN D CD    1 
ATOM   14435 O  OE1   . GLN D 2 153 ? 153.293 82.936  138.573 1.00 31.78 ?  132 GLN D OE1   1 
ATOM   14436 N  NE2   . GLN D 2 153 ? 153.870 83.676  136.536 1.00 32.81 ?  132 GLN D NE2   1 
ATOM   14437 N  N     . LYS D 2 154 ? 154.766 86.711  142.178 1.00 24.00 ?  133 LYS D N     1 
ATOM   14438 C  CA    . LYS D 2 154 ? 154.418 86.928  143.581 1.00 24.43 ?  133 LYS D CA    1 
ATOM   14439 C  C     . LYS D 2 154 ? 153.023 87.554  143.720 1.00 23.40 ?  133 LYS D C     1 
ATOM   14440 O  O     . LYS D 2 154 ? 152.166 87.022  144.430 1.00 22.68 ?  133 LYS D O     1 
ATOM   14441 C  CB    . LYS D 2 154 ? 155.448 87.783  144.327 1.00 24.64 ?  133 LYS D CB    1 
ATOM   14442 C  CG    . LYS D 2 154 ? 155.058 87.951  145.806 1.00 28.01 ?  133 LYS D CG    1 
ATOM   14443 C  CD    . LYS D 2 154 ? 156.108 88.634  146.652 1.00 32.56 ?  133 LYS D CD    1 
ATOM   14444 C  CE    . LYS D 2 154 ? 157.316 87.752  146.849 1.00 34.45 ?  133 LYS D CE    1 
ATOM   14445 N  NZ    . LYS D 2 154 ? 158.347 88.450  147.680 1.00 36.11 1  133 LYS D NZ    1 
ATOM   14446 N  N     . LYS D 2 155 ? 152.794 88.677  143.039 1.00 23.07 ?  134 LYS D N     1 
ATOM   14447 C  CA    . LYS D 2 155 ? 151.489 89.327  143.125 1.00 22.70 ?  134 LYS D CA    1 
ATOM   14448 C  C     . LYS D 2 155 ? 150.376 88.494  142.490 1.00 21.96 ?  134 LYS D C     1 
ATOM   14449 O  O     . LYS D 2 155 ? 149.301 88.383  143.070 1.00 22.25 ?  134 LYS D O     1 
ATOM   14450 C  CB    . LYS D 2 155 ? 151.512 90.772  142.596 1.00 22.70 ?  134 LYS D CB    1 
ATOM   14451 C  CG    . LYS D 2 155 ? 151.800 90.951  141.119 1.00 23.62 ?  134 LYS D CG    1 
ATOM   14452 C  CD    . LYS D 2 155 ? 151.705 92.434  140.766 1.00 25.32 ?  134 LYS D CD    1 
ATOM   14453 C  CE    . LYS D 2 155 ? 152.716 92.793  139.681 1.00 27.09 ?  134 LYS D CE    1 
ATOM   14454 N  NZ    . LYS D 2 155 ? 152.574 94.224  139.284 1.00 26.65 1  134 LYS D NZ    1 
ATOM   14455 N  N     . ALA D 2 156 ? 150.623 87.883  141.331 1.00 21.76 ?  135 ALA D N     1 
ATOM   14456 C  CA    . ALA D 2 156 ? 149.570 87.076  140.686 1.00 21.83 ?  135 ALA D CA    1 
ATOM   14457 C  C     . ALA D 2 156 ? 149.097 85.943  141.613 1.00 22.30 ?  135 ALA D C     1 
ATOM   14458 O  O     . ALA D 2 156 ? 147.892 85.742  141.795 1.00 21.92 ?  135 ALA D O     1 
ATOM   14459 C  CB    . ALA D 2 156 ? 150.045 86.510  139.336 1.00 22.30 ?  135 ALA D CB    1 
ATOM   14460 N  N     . GLN D 2 157 ? 150.045 85.226  142.219 1.00 22.15 ?  136 GLN D N     1 
ATOM   14461 C  CA    . GLN D 2 157 ? 149.693 84.099  143.090 1.00 22.38 ?  136 GLN D CA    1 
ATOM   14462 C  C     . GLN D 2 157 ? 149.089 84.522  144.436 1.00 21.59 ?  136 GLN D C     1 
ATOM   14463 O  O     . GLN D 2 157 ? 148.257 83.806  144.992 1.00 21.44 ?  136 GLN D O     1 
ATOM   14464 C  CB    . GLN D 2 157 ? 150.883 83.146  143.298 1.00 22.94 ?  136 GLN D CB    1 
ATOM   14465 C  CG    . GLN D 2 157 ? 151.467 82.545  142.009 1.00 25.31 ?  136 GLN D CG    1 
ATOM   14466 C  CD    . GLN D 2 157 ? 150.408 82.019  141.035 1.00 28.02 ?  136 GLN D CD    1 
ATOM   14467 O  OE1   . GLN D 2 157 ? 149.402 81.424  141.434 1.00 27.14 ?  136 GLN D OE1   1 
ATOM   14468 N  NE2   . GLN D 2 157 ? 150.647 82.234  139.743 1.00 29.47 ?  136 GLN D NE2   1 
ATOM   14469 N  N     . MET D 2 158 ? 149.506 85.667  144.964 1.00 21.52 ?  137 MET D N     1 
ATOM   14470 C  CA    . MET D 2 158 ? 148.889 86.205  146.190 1.00 22.20 ?  137 MET D CA    1 
ATOM   14471 C  C     . MET D 2 158 ? 147.390 86.467  146.006 1.00 21.84 ?  137 MET D C     1 
ATOM   14472 O  O     . MET D 2 158 ? 146.580 86.116  146.867 1.00 21.91 ?  137 MET D O     1 
ATOM   14473 C  CB    . MET D 2 158 ? 149.584 87.487  146.648 1.00 22.52 ?  137 MET D CB    1 
ATOM   14474 C  CG    . MET D 2 158 ? 150.926 87.246  147.354 1.00 25.81 ?  137 MET D CG    1 
ATOM   14475 S  SD    . MET D 2 158 ? 151.747 88.774  147.886 1.00 31.19 ?  137 MET D SD    1 
ATOM   14476 C  CE    . MET D 2 158 ? 150.532 89.334  149.051 1.00 23.91 ?  137 MET D CE    1 
ATOM   14477 N  N     . ILE D 2 159 ? 147.039 87.080  144.878 1.00 21.41 ?  138 ILE D N     1 
ATOM   14478 C  CA    . ILE D 2 159 ? 145.652 87.407  144.562 1.00 21.51 ?  138 ILE D CA    1 
ATOM   14479 C  C     . ILE D 2 159 ? 144.834 86.124  144.345 1.00 21.77 ?  138 ILE D C     1 
ATOM   14480 O  O     . ILE D 2 159 ? 143.755 85.959  144.936 1.00 21.44 ?  138 ILE D O     1 
ATOM   14481 C  CB    . ILE D 2 159 ? 145.579 88.388  143.328 1.00 21.49 ?  138 ILE D CB    1 
ATOM   14482 C  CG1   . ILE D 2 159 ? 146.273 89.723  143.636 1.00 21.16 ?  138 ILE D CG1   1 
ATOM   14483 C  CG2   . ILE D 2 159 ? 144.138 88.616  142.857 1.00 22.34 ?  138 ILE D CG2   1 
ATOM   14484 C  CD1   . ILE D 2 159 ? 145.644 90.536  144.787 1.00 23.85 ?  138 ILE D CD1   1 
ATOM   14485 N  N     . VAL D 2 160 ? 145.366 85.223  143.510 1.00 21.96 ?  139 VAL D N     1 
ATOM   14486 C  CA    . VAL D 2 160 ? 144.720 83.947  143.168 1.00 22.59 ?  139 VAL D CA    1 
ATOM   14487 C  C     . VAL D 2 160 ? 144.522 83.082  144.420 1.00 22.36 ?  139 VAL D C     1 
ATOM   14488 O  O     . VAL D 2 160 ? 143.496 82.408  144.558 1.00 21.64 ?  139 VAL D O     1 
ATOM   14489 C  CB    . VAL D 2 160 ? 145.528 83.178  142.068 1.00 23.08 ?  139 VAL D CB    1 
ATOM   14490 C  CG1   . VAL D 2 160 ? 145.110 81.699  141.960 1.00 24.33 ?  139 VAL D CG1   1 
ATOM   14491 C  CG2   . VAL D 2 160 ? 145.378 83.870  140.704 1.00 22.87 ?  139 VAL D CG2   1 
ATOM   14492 N  N     . GLY D 2 161 ? 145.503 83.114  145.326 1.00 22.21 ?  140 GLY D N     1 
ATOM   14493 C  CA    . GLY D 2 161 ? 145.408 82.396  146.596 1.00 22.50 ?  140 GLY D CA    1 
ATOM   14494 C  C     . GLY D 2 161 ? 144.176 82.797  147.400 1.00 22.88 ?  140 GLY D C     1 
ATOM   14495 O  O     . GLY D 2 161 ? 143.476 81.935  147.949 1.00 23.54 ?  140 GLY D O     1 
ATOM   14496 N  N     . LEU D 2 162 ? 143.898 84.099  147.463 1.00 22.25 ?  141 LEU D N     1 
ATOM   14497 C  CA    . LEU D 2 162 ? 142.716 84.586  148.179 1.00 22.48 ?  141 LEU D CA    1 
ATOM   14498 C  C     . LEU D 2 162 ? 141.399 84.210  147.496 1.00 22.27 ?  141 LEU D C     1 
ATOM   14499 O  O     . LEU D 2 162 ? 140.413 83.934  148.181 1.00 22.31 ?  141 LEU D O     1 
ATOM   14500 C  CB    . LEU D 2 162 ? 142.804 86.098  148.473 1.00 22.07 ?  141 LEU D CB    1 
ATOM   14501 C  CG    . LEU D 2 162 ? 143.788 86.460  149.607 1.00 22.81 ?  141 LEU D CG    1 
ATOM   14502 C  CD1   . LEU D 2 162 ? 144.238 87.918  149.535 1.00 21.65 ?  141 LEU D CD1   1 
ATOM   14503 C  CD2   . LEU D 2 162 ? 143.254 86.101  150.998 1.00 23.35 ?  141 LEU D CD2   1 
ATOM   14504 N  N     . TYR D 2 163 ? 141.375 84.198  146.161 1.00 22.63 ?  142 TYR D N     1 
ATOM   14505 C  CA    . TYR D 2 163 ? 140.190 83.713  145.424 1.00 23.30 ?  142 TYR D CA    1 
ATOM   14506 C  C     . TYR D 2 163 ? 139.930 82.234  145.676 1.00 23.40 ?  142 TYR D C     1 
ATOM   14507 O  O     . TYR D 2 163 ? 138.788 81.822  145.815 1.00 23.75 ?  142 TYR D O     1 
ATOM   14508 C  CB    . TYR D 2 163 ? 140.342 83.890  143.920 1.00 23.22 ?  142 TYR D CB    1 
ATOM   14509 C  CG    . TYR D 2 163 ? 140.497 85.303  143.430 1.00 24.01 ?  142 TYR D CG    1 
ATOM   14510 C  CD1   . TYR D 2 163 ? 140.050 86.380  144.184 1.00 24.47 ?  142 TYR D CD1   1 
ATOM   14511 C  CD2   . TYR D 2 163 ? 141.089 85.556  142.196 1.00 24.62 ?  142 TYR D CD2   1 
ATOM   14512 C  CE1   . TYR D 2 163 ? 140.192 87.675  143.729 1.00 26.33 ?  142 TYR D CE1   1 
ATOM   14513 C  CE2   . TYR D 2 163 ? 141.227 86.851  141.723 1.00 26.07 ?  142 TYR D CE2   1 
ATOM   14514 C  CZ    . TYR D 2 163 ? 140.769 87.906  142.501 1.00 26.65 ?  142 TYR D CZ    1 
ATOM   14515 O  OH    . TYR D 2 163 ? 140.905 89.201  142.057 1.00 31.13 ?  142 TYR D OH    1 
ATOM   14516 N  N     . LYS D 2 164 ? 140.991 81.438  145.723 1.00 23.70 ?  143 LYS D N     1 
ATOM   14517 C  CA    . LYS D 2 164 ? 140.861 79.995  145.981 1.00 24.47 ?  143 LYS D CA    1 
ATOM   14518 C  C     . LYS D 2 164 ? 140.435 79.663  147.421 1.00 24.55 ?  143 LYS D C     1 
ATOM   14519 O  O     . LYS D 2 164 ? 139.976 78.553  147.697 1.00 24.49 ?  143 LYS D O     1 
ATOM   14520 C  CB    . LYS D 2 164 ? 142.174 79.285  145.646 1.00 24.98 ?  143 LYS D CB    1 
ATOM   14521 C  CG    . LYS D 2 164 ? 142.447 79.114  144.144 1.00 27.10 ?  143 LYS D CG    1 
ATOM   14522 C  CD    . LYS D 2 164 ? 143.711 78.293  143.940 1.00 30.75 ?  143 LYS D CD    1 
ATOM   14523 C  CE    . LYS D 2 164 ? 143.990 77.992  142.468 1.00 32.81 ?  143 LYS D CE    1 
ATOM   14524 N  NZ    . LYS D 2 164 ? 145.309 77.266  142.278 1.00 33.68 1  143 LYS D NZ    1 
ATOM   14525 N  N     . ALA D 2 165 ? 140.600 80.617  148.332 1.00 24.18 ?  144 ALA D N     1 
ATOM   14526 C  CA    . ALA D 2 165 ? 140.298 80.396  149.749 1.00 25.04 ?  144 ALA D CA    1 
ATOM   14527 C  C     . ALA D 2 165 ? 138.865 80.764  150.161 1.00 25.00 ?  144 ALA D C     1 
ATOM   14528 O  O     . ALA D 2 165 ? 138.494 80.584  151.330 1.00 25.50 ?  144 ALA D O     1 
ATOM   14529 C  CB    . ALA D 2 165 ? 141.316 81.130  150.639 1.00 25.02 ?  144 ALA D CB    1 
ATOM   14530 N  N     . ILE D 2 166 ? 138.065 81.278  149.224 1.00 24.60 ?  145 ILE D N     1 
ATOM   14531 C  CA    . ILE D 2 166 ? 136.664 81.585  149.512 1.00 24.40 ?  145 ILE D CA    1 
ATOM   14532 C  C     . ILE D 2 166 ? 135.921 80.285  149.854 1.00 25.75 ?  145 ILE D C     1 
ATOM   14533 O  O     . ILE D 2 166 ? 136.057 79.277  149.152 1.00 25.84 ?  145 ILE D O     1 
ATOM   14534 C  CB    . ILE D 2 166 ? 135.934 82.287  148.332 1.00 24.15 ?  145 ILE D CB    1 
ATOM   14535 C  CG1   . ILE D 2 166 ? 136.729 83.490  147.829 1.00 23.15 ?  145 ILE D CG1   1 
ATOM   14536 C  CG2   . ILE D 2 166 ? 134.530 82.719  148.756 1.00 22.72 ?  145 ILE D CG2   1 
ATOM   14537 C  CD1   . ILE D 2 166 ? 136.198 84.080  146.539 1.00 21.70 ?  145 ILE D CD1   1 
ATOM   14538 N  N     . GLN D 2 167 ? 135.172 80.311  150.949 1.00 26.52 ?  146 GLN D N     1 
ATOM   14539 C  CA    . GLN D 2 167 ? 134.369 79.164  151.352 1.00 28.77 ?  146 GLN D CA    1 
ATOM   14540 C  C     . GLN D 2 167 ? 132.884 79.482  151.231 1.00 29.20 ?  146 GLN D C     1 
ATOM   14541 O  O     . GLN D 2 167 ? 132.450 80.601  151.542 1.00 28.89 ?  146 GLN D O     1 
ATOM   14542 C  CB    . GLN D 2 167 ? 134.705 78.759  152.784 1.00 29.04 ?  146 GLN D CB    1 
ATOM   14543 C  CG    . GLN D 2 167 ? 136.126 78.255  152.947 1.00 31.87 ?  146 GLN D CG    1 
ATOM   14544 C  CD    . GLN D 2 167 ? 136.787 78.815  154.177 1.00 35.35 ?  146 GLN D CD    1 
ATOM   14545 O  OE1   . GLN D 2 167 ? 136.412 78.483  155.305 1.00 36.91 ?  146 GLN D OE1   1 
ATOM   14546 N  NE2   . GLN D 2 167 ? 137.784 79.674  153.973 1.00 36.19 ?  146 GLN D NE2   1 
ATOM   14547 N  N     . LYS D 2 168 ? 132.112 78.495  150.783 1.00 30.29 ?  147 LYS D N     1 
ATOM   14548 C  CA    . LYS D 2 168 ? 130.661 78.644  150.680 1.00 31.24 ?  147 LYS D CA    1 
ATOM   14549 C  C     . LYS D 2 168 ? 130.061 79.155  151.990 1.00 31.73 ?  147 LYS D C     1 
ATOM   14550 O  O     . LYS D 2 168 ? 130.436 78.689  153.066 1.00 31.46 ?  147 LYS D O     1 
ATOM   14551 C  CB    . LYS D 2 168 ? 130.014 77.323  150.272 1.00 31.92 ?  147 LYS D CB    1 
ATOM   14552 C  CG    . LYS D 2 168 ? 128.510 77.424  150.061 1.00 33.23 ?  147 LYS D CG    1 
ATOM   14553 C  CD    . LYS D 2 168 ? 127.946 76.162  149.428 1.00 36.06 ?  147 LYS D CD    1 
ATOM   14554 C  CE    . LYS D 2 168 ? 126.440 76.244  149.291 1.00 35.46 ?  147 LYS D CE    1 
ATOM   14555 N  NZ    . LYS D 2 168 ? 126.023 77.216  148.244 1.00 38.24 1  147 LYS D NZ    1 
ATOM   14556 N  N     . ASP D 2 169 ? 129.151 80.126  151.884 1.00 32.28 ?  148 ASP D N     1 
ATOM   14557 C  CA    . ASP D 2 169 ? 128.470 80.730  153.042 1.00 33.45 ?  148 ASP D CA    1 
ATOM   14558 C  C     . ASP D 2 169 ? 129.384 81.333  154.108 1.00 33.30 ?  148 ASP D C     1 
ATOM   14559 O  O     . ASP D 2 169 ? 128.994 81.445  155.272 1.00 34.32 ?  148 ASP D O     1 
ATOM   14560 C  CB    . ASP D 2 169 ? 127.534 79.715  153.721 1.00 34.63 ?  148 ASP D CB    1 
ATOM   14561 C  CG    . ASP D 2 169 ? 126.284 79.429  152.916 1.00 36.09 ?  148 ASP D CG    1 
ATOM   14562 O  OD1   . ASP D 2 169 ? 125.981 80.163  151.952 1.00 37.80 ?  148 ASP D OD1   1 
ATOM   14563 O  OD2   . ASP D 2 169 ? 125.595 78.450  153.269 1.00 40.47 -1 148 ASP D OD2   1 
ATOM   14564 N  N     . ASP D 2 170 ? 130.600 81.700  153.736 1.00 32.58 ?  149 ASP D N     1 
ATOM   14565 C  CA    . ASP D 2 170 ? 131.481 82.393  154.674 1.00 32.01 ?  149 ASP D CA    1 
ATOM   14566 C  C     . ASP D 2 170 ? 131.811 83.770  154.111 1.00 30.59 ?  149 ASP D C     1 
ATOM   14567 O  O     . ASP D 2 170 ? 132.626 83.903  153.197 1.00 29.11 ?  149 ASP D O     1 
ATOM   14568 C  CB    . ASP D 2 170 ? 132.741 81.574  154.966 1.00 32.93 ?  149 ASP D CB    1 
ATOM   14569 C  CG    . ASP D 2 170 ? 133.794 82.358  155.738 1.00 35.05 ?  149 ASP D CG    1 
ATOM   14570 O  OD1   . ASP D 2 170 ? 133.455 83.274  156.519 1.00 39.25 ?  149 ASP D OD1   1 
ATOM   14571 O  OD2   . ASP D 2 170 ? 134.980 82.043  155.575 1.00 39.22 -1 149 ASP D OD2   1 
ATOM   14572 N  N     . GLU D 2 171 ? 131.154 84.784  154.669 1.00 29.34 ?  150 GLU D N     1 
ATOM   14573 C  CA    . GLU D 2 171 ? 131.278 86.154  154.182 1.00 28.51 ?  150 GLU D CA    1 
ATOM   14574 C  C     . GLU D 2 171 ? 132.635 86.796  154.502 1.00 27.27 ?  150 GLU D C     1 
ATOM   14575 O  O     . GLU D 2 171 ? 133.042 87.730  153.829 1.00 26.62 ?  150 GLU D O     1 
ATOM   14576 C  CB    . GLU D 2 171 ? 130.116 87.017  154.693 1.00 29.09 ?  150 GLU D CB    1 
ATOM   14577 C  CG    . GLU D 2 171 ? 130.127 87.310  156.192 1.00 30.68 ?  150 GLU D CG    1 
ATOM   14578 C  CD    . GLU D 2 171 ? 128.860 88.011  156.656 1.00 33.92 ?  150 GLU D CD    1 
ATOM   14579 O  OE1   . GLU D 2 171 ? 127.990 88.306  155.800 1.00 36.31 ?  150 GLU D OE1   1 
ATOM   14580 O  OE2   . GLU D 2 171 ? 128.724 88.276  157.870 1.00 34.02 -1 150 GLU D OE2   1 
ATOM   14581 N  N     . ILE D 2 172 ? 133.337 86.280  155.510 1.00 26.19 ?  151 ILE D N     1 
ATOM   14582 C  CA    . ILE D 2 172 ? 134.670 86.782  155.847 1.00 25.49 ?  151 ILE D CA    1 
ATOM   14583 C  C     . ILE D 2 172 ? 135.668 86.449  154.734 1.00 24.61 ?  151 ILE D C     1 
ATOM   14584 O  O     . ILE D 2 172 ? 136.414 87.323  154.276 1.00 24.09 ?  151 ILE D O     1 
ATOM   14585 C  CB    . ILE D 2 172 ? 135.160 86.261  157.227 1.00 25.98 ?  151 ILE D CB    1 
ATOM   14586 C  CG1   . ILE D 2 172 ? 134.257 86.769  158.352 1.00 26.86 ?  151 ILE D CG1   1 
ATOM   14587 C  CG2   . ILE D 2 172 ? 136.640 86.636  157.505 1.00 26.50 ?  151 ILE D CG2   1 
ATOM   14588 C  CD1   . ILE D 2 172 ? 134.204 88.285  158.480 1.00 27.81 ?  151 ILE D CD1   1 
ATOM   14589 N  N     . SER D 2 173 ? 135.655 85.196  154.289 1.00 23.71 ?  152 SER D N     1 
ATOM   14590 C  CA    . SER D 2 173 ? 136.532 84.757  153.205 1.00 23.38 ?  152 SER D CA    1 
ATOM   14591 C  C     . SER D 2 173 ? 136.160 85.446  151.879 1.00 22.41 ?  152 SER D C     1 
ATOM   14592 O  O     . SER D 2 173 ? 137.028 85.749  151.057 1.00 21.43 ?  152 SER D O     1 
ATOM   14593 C  CB    . SER D 2 173 ? 136.519 83.228  153.069 1.00 23.90 ?  152 SER D CB    1 
ATOM   14594 O  OG    . SER D 2 173 ? 135.289 82.717  152.560 1.00 23.74 ?  152 SER D OG    1 
ATOM   14595 N  N     . LEU D 2 174 ? 134.870 85.709  151.690 1.00 21.63 ?  153 LEU D N     1 
ATOM   14596 C  CA    . LEU D 2 174 ? 134.424 86.443  150.503 1.00 20.75 ?  153 LEU D CA    1 
ATOM   14597 C  C     . LEU D 2 174 ? 134.964 87.872  150.542 1.00 20.96 ?  153 LEU D C     1 
ATOM   14598 O  O     . LEU D 2 174 ? 135.463 88.377  149.537 1.00 20.41 ?  153 LEU D O     1 
ATOM   14599 C  CB    . LEU D 2 174 ? 132.886 86.444  150.388 1.00 20.62 ?  153 LEU D CB    1 
ATOM   14600 C  CG    . LEU D 2 174 ? 132.282 87.220  149.199 1.00 19.55 ?  153 LEU D CG    1 
ATOM   14601 C  CD1   . LEU D 2 174 ? 132.900 86.760  147.873 1.00 20.44 ?  153 LEU D CD1   1 
ATOM   14602 C  CD2   . LEU D 2 174 ? 130.755 87.059  149.186 1.00 20.99 ?  153 LEU D CD2   1 
ATOM   14603 N  N     . PHE D 2 175 ? 134.868 88.515  151.705 1.00 21.07 ?  154 PHE D N     1 
ATOM   14604 C  CA    . PHE D 2 175 ? 135.368 89.878  151.868 1.00 21.32 ?  154 PHE D CA    1 
ATOM   14605 C  C     . PHE D 2 175 ? 136.863 89.971  151.544 1.00 21.08 ?  154 PHE D C     1 
ATOM   14606 O  O     . PHE D 2 175 ? 137.300 90.883  150.840 1.00 20.85 ?  154 PHE D O     1 
ATOM   14607 C  CB    . PHE D 2 175 ? 135.105 90.379  153.293 1.00 21.20 ?  154 PHE D CB    1 
ATOM   14608 C  CG    . PHE D 2 175 ? 135.819 91.655  153.628 1.00 22.46 ?  154 PHE D CG    1 
ATOM   14609 C  CD1   . PHE D 2 175 ? 135.204 92.887  153.406 1.00 21.21 ?  154 PHE D CD1   1 
ATOM   14610 C  CD2   . PHE D 2 175 ? 137.105 91.634  154.175 1.00 22.53 ?  154 PHE D CD2   1 
ATOM   14611 C  CE1   . PHE D 2 175 ? 135.848 94.067  153.721 1.00 22.11 ?  154 PHE D CE1   1 
ATOM   14612 C  CE2   . PHE D 2 175 ? 137.769 92.820  154.479 1.00 23.26 ?  154 PHE D CE2   1 
ATOM   14613 C  CZ    . PHE D 2 175 ? 137.139 94.040  154.259 1.00 22.08 ?  154 PHE D CZ    1 
ATOM   14614 N  N     . LYS D 2 176 ? 137.640 89.030  152.071 1.00 21.14 ?  155 LYS D N     1 
ATOM   14615 C  CA    . LYS D 2 176 ? 139.084 88.991  151.819 1.00 20.93 ?  155 LYS D CA    1 
ATOM   14616 C  C     . LYS D 2 176 ? 139.409 88.888  150.331 1.00 20.61 ?  155 LYS D C     1 
ATOM   14617 O  O     . LYS D 2 176 ? 140.312 89.568  149.832 1.00 20.62 ?  155 LYS D O     1 
ATOM   14618 C  CB    . LYS D 2 176 ? 139.711 87.837  152.587 1.00 21.27 ?  155 LYS D CB    1 
ATOM   14619 C  CG    . LYS D 2 176 ? 139.780 88.116  154.063 1.00 22.04 ?  155 LYS D CG    1 
ATOM   14620 C  CD    . LYS D 2 176 ? 140.307 86.934  154.860 1.00 25.24 ?  155 LYS D CD    1 
ATOM   14621 C  CE    . LYS D 2 176 ? 140.403 87.321  156.313 1.00 25.83 ?  155 LYS D CE    1 
ATOM   14622 N  NZ    . LYS D 2 176 ? 140.931 86.223  157.174 1.00 26.64 1  155 LYS D NZ    1 
ATOM   14623 N  N     . ALA D 2 177 ? 138.649 88.058  149.624 1.00 20.02 ?  156 ALA D N     1 
ATOM   14624 C  CA    . ALA D 2 177 ? 138.782 87.944  148.174 1.00 19.86 ?  156 ALA D CA    1 
ATOM   14625 C  C     . ALA D 2 177 ? 138.382 89.240  147.453 1.00 19.61 ?  156 ALA D C     1 
ATOM   14626 O  O     . ALA D 2 177 ? 138.969 89.601  146.431 1.00 19.69 ?  156 ALA D O     1 
ATOM   14627 C  CB    . ALA D 2 177 ? 137.952 86.801  147.689 1.00 19.99 ?  156 ALA D CB    1 
ATOM   14628 N  N     . MET D 2 178 ? 137.374 89.931  147.980 1.00 19.75 ?  157 MET D N     1 
ATOM   14629 C  CA    . MET D 2 178 ? 136.914 91.197  147.372 1.00 18.89 ?  157 MET D CA    1 
ATOM   14630 C  C     . MET D 2 178 ? 137.977 92.273  147.528 1.00 18.62 ?  157 MET D C     1 
ATOM   14631 O  O     . MET D 2 178 ? 138.212 93.063  146.606 1.00 18.10 ?  157 MET D O     1 
ATOM   14632 C  CB    . MET D 2 178 ? 135.600 91.656  147.995 1.00 18.82 ?  157 MET D CB    1 
ATOM   14633 C  CG    . MET D 2 178 ? 134.400 90.844  147.535 1.00 20.20 ?  157 MET D CG    1 
ATOM   14634 S  SD    . MET D 2 178 ? 132.926 91.353  148.431 1.00 23.78 ?  157 MET D SD    1 
ATOM   14635 C  CE    . MET D 2 178 ? 131.681 90.441  147.522 1.00 22.62 ?  157 MET D CE    1 
ATOM   14636 N  N     . VAL D 2 179 ? 138.632 92.276  148.691 1.00 18.34 ?  158 VAL D N     1 
ATOM   14637 C  CA    . VAL D 2 179 ? 139.754 93.167  148.945 1.00 18.75 ?  158 VAL D CA    1 
ATOM   14638 C  C     . VAL D 2 179 ? 140.868 92.914  147.937 1.00 18.86 ?  158 VAL D C     1 
ATOM   14639 O  O     . VAL D 2 179 ? 141.408 93.871  147.356 1.00 18.79 ?  158 VAL D O     1 
ATOM   14640 C  CB    . VAL D 2 179 ? 140.308 93.036  150.388 1.00 19.02 ?  158 VAL D CB    1 
ATOM   14641 C  CG1   . VAL D 2 179 ? 141.619 93.824  150.526 1.00 19.10 ?  158 VAL D CG1   1 
ATOM   14642 C  CG2   . VAL D 2 179 ? 139.270 93.511  151.416 1.00 18.94 ?  158 VAL D CG2   1 
ATOM   14643 N  N     . ALA D 2 180 ? 141.212 91.633  147.748 1.00 18.96 ?  159 ALA D N     1 
ATOM   14644 C  CA    . ALA D 2 180 ? 142.192 91.233  146.736 1.00 19.05 ?  159 ALA D CA    1 
ATOM   14645 C  C     . ALA D 2 180 ? 141.778 91.719  145.345 1.00 18.67 ?  159 ALA D C     1 
ATOM   14646 O  O     . ALA D 2 180 ? 142.600 92.275  144.606 1.00 17.72 ?  159 ALA D O     1 
ATOM   14647 C  CB    . ALA D 2 180 ? 142.392 89.706  146.741 1.00 19.43 ?  159 ALA D CB    1 
ATOM   14648 N  N     . SER D 2 181 ? 140.497 91.536  145.011 1.00 18.49 ?  160 SER D N     1 
ATOM   14649 C  CA    . SER D 2 181 ? 139.980 91.974  143.713 1.00 18.51 ?  160 SER D CA    1 
ATOM   14650 C  C     . SER D 2 181 ? 140.079 93.488  143.524 1.00 18.23 ?  160 SER D C     1 
ATOM   14651 O  O     . SER D 2 181 ? 140.531 93.957  142.487 1.00 18.18 ?  160 SER D O     1 
ATOM   14652 C  CB    . SER D 2 181 ? 138.531 91.522  143.511 1.00 18.51 ?  160 SER D CB    1 
ATOM   14653 O  OG    . SER D 2 181 ? 138.131 91.815  142.186 1.00 19.42 ?  160 SER D OG    1 
ATOM   14654 N  N     . VAL D 2 182 ? 139.663 94.248  144.535 1.00 18.43 ?  161 VAL D N     1 
ATOM   14655 C  CA    . VAL D 2 182 ? 139.791 95.708  144.484 1.00 18.09 ?  161 VAL D CA    1 
ATOM   14656 C  C     . VAL D 2 182 ? 141.257 96.131  144.346 1.00 18.41 ?  161 VAL D C     1 
ATOM   14657 O  O     . VAL D 2 182 ? 141.576 97.025  143.559 1.00 18.52 ?  161 VAL D O     1 
ATOM   14658 C  CB    . VAL D 2 182 ? 139.126 96.385  145.689 1.00 17.71 ?  161 VAL D CB    1 
ATOM   14659 C  CG1   . VAL D 2 182 ? 139.457 97.896  145.725 1.00 16.02 ?  161 VAL D CG1   1 
ATOM   14660 C  CG2   . VAL D 2 182 ? 137.607 96.173  145.618 1.00 17.78 ?  161 VAL D CG2   1 
ATOM   14661 N  N     . TYR D 2 183 ? 142.150 95.458  145.074 1.00 19.06 ?  162 TYR D N     1 
ATOM   14662 C  CA    . TYR D 2 183 ? 143.571 95.769  144.958 1.00 19.73 ?  162 TYR D CA    1 
ATOM   14663 C  C     . TYR D 2 183 ? 144.087 95.508  143.550 1.00 19.90 ?  162 TYR D C     1 
ATOM   14664 O  O     . TYR D 2 183 ? 144.924 96.251  143.064 1.00 20.73 ?  162 TYR D O     1 
ATOM   14665 C  CB    . TYR D 2 183 ? 144.430 95.036  146.005 1.00 19.84 ?  162 TYR D CB    1 
ATOM   14666 C  CG    . TYR D 2 183 ? 144.293 95.575  147.414 1.00 20.24 ?  162 TYR D CG    1 
ATOM   14667 C  CD1   . TYR D 2 183 ? 143.665 96.792  147.663 1.00 21.51 ?  162 TYR D CD1   1 
ATOM   14668 C  CD2   . TYR D 2 183 ? 144.816 94.870  148.506 1.00 20.45 ?  162 TYR D CD2   1 
ATOM   14669 C  CE1   . TYR D 2 183 ? 143.546 97.292  148.966 1.00 21.68 ?  162 TYR D CE1   1 
ATOM   14670 C  CE2   . TYR D 2 183 ? 144.720 95.373  149.811 1.00 19.97 ?  162 TYR D CE2   1 
ATOM   14671 C  CZ    . TYR D 2 183 ? 144.080 96.580  150.030 1.00 21.83 ?  162 TYR D CZ    1 
ATOM   14672 O  OH    . TYR D 2 183 ? 143.969 97.082  151.312 1.00 21.96 ?  162 TYR D OH    1 
ATOM   14673 N  N     . LEU D 2 184 ? 143.583 94.477  142.885 1.00 20.22 ?  163 LEU D N     1 
ATOM   14674 C  CA    . LEU D 2 184 ? 144.007 94.218  141.512 1.00 20.89 ?  163 LEU D CA    1 
ATOM   14675 C  C     . LEU D 2 184 ? 143.449 95.297  140.572 1.00 20.72 ?  163 LEU D C     1 
ATOM   14676 O  O     . LEU D 2 184 ? 144.208 95.948  139.860 1.00 21.07 ?  163 LEU D O     1 
ATOM   14677 C  CB    . LEU D 2 184 ? 143.640 92.788  141.066 1.00 21.16 ?  163 LEU D CB    1 
ATOM   14678 C  CG    . LEU D 2 184 ? 143.969 92.343  139.626 1.00 22.77 ?  163 LEU D CG    1 
ATOM   14679 C  CD1   . LEU D 2 184 ? 145.443 92.599  139.240 1.00 22.44 ?  163 LEU D CD1   1 
ATOM   14680 C  CD2   . LEU D 2 184 ? 143.617 90.879  139.407 1.00 24.75 ?  163 LEU D CD2   1 
ATOM   14681 N  N     . GLU D 2 185 ? 142.134 95.504  140.612 1.00 20.65 ?  164 GLU D N     1 
ATOM   14682 C  CA    . GLU D 2 185 ? 141.448 96.461  139.732 1.00 20.69 ?  164 GLU D CA    1 
ATOM   14683 C  C     . GLU D 2 185 ? 141.907 97.910  139.891 1.00 20.64 ?  164 GLU D C     1 
ATOM   14684 O  O     . GLU D 2 185 ? 142.027 98.646  138.900 1.00 20.25 ?  164 GLU D O     1 
ATOM   14685 C  CB    . GLU D 2 185 ? 139.931 96.410  139.969 1.00 21.03 ?  164 GLU D CB    1 
ATOM   14686 C  CG    . GLU D 2 185 ? 139.286 95.040  139.742 1.00 22.19 ?  164 GLU D CG    1 
ATOM   14687 C  CD    . GLU D 2 185 ? 138.953 94.747  138.281 1.00 24.19 ?  164 GLU D CD    1 
ATOM   14688 O  OE1   . GLU D 2 185 ? 139.290 95.540  137.384 1.00 27.97 ?  164 GLU D OE1   1 
ATOM   14689 O  OE2   . GLU D 2 185 ? 138.323 93.722  138.020 1.00 25.47 -1 164 GLU D OE2   1 
ATOM   14690 N  N     . SER D 2 186 ? 142.128 98.324  141.134 1.00 20.42 ?  165 SER D N     1 
ATOM   14691 C  CA    . SER D 2 186 ? 142.325 99.738  141.451 1.00 20.70 ?  165 SER D CA    1 
ATOM   14692 C  C     . SER D 2 186 ? 143.758 100.099 141.841 1.00 20.88 ?  165 SER D C     1 
ATOM   14693 O  O     . SER D 2 186 ? 144.044 101.260 142.134 1.00 21.21 ?  165 SER D O     1 
ATOM   14694 C  CB    . SER D 2 186 ? 141.364 100.180 142.569 1.00 21.25 ?  165 SER D CB    1 
ATOM   14695 O  OG    . SER D 2 186 ? 140.016 99.844  142.271 1.00 20.97 ?  165 SER D OG    1 
ATOM   14696 N  N     . PHE D 2 187 ? 144.667 99.123  141.840 1.00 20.94 ?  166 PHE D N     1 
ATOM   14697 C  CA    . PHE D 2 187 ? 145.999 99.372  142.372 1.00 21.19 ?  166 PHE D CA    1 
ATOM   14698 C  C     . PHE D 2 187 ? 147.086 98.630  141.595 1.00 21.22 ?  166 PHE D C     1 
ATOM   14699 O  O     . PHE D 2 187 ? 147.939 99.283  140.983 1.00 21.10 ?  166 PHE D O     1 
ATOM   14700 C  CB    . PHE D 2 187 ? 146.013 99.117  143.906 1.00 21.63 ?  166 PHE D CB    1 
ATOM   14701 C  CG    . PHE D 2 187 ? 147.374 98.868  144.502 1.00 24.05 ?  166 PHE D CG    1 
ATOM   14702 C  CD1   . PHE D 2 187 ? 148.393 99.814  144.398 1.00 25.52 ?  166 PHE D CD1   1 
ATOM   14703 C  CD2   . PHE D 2 187 ? 147.620 97.699  145.216 1.00 27.03 ?  166 PHE D CD2   1 
ATOM   14704 C  CE1   . PHE D 2 187 ? 149.636 99.583  144.973 1.00 26.73 ?  166 PHE D CE1   1 
ATOM   14705 C  CE2   . PHE D 2 187 ? 148.878 97.458  145.788 1.00 27.36 ?  166 PHE D CE2   1 
ATOM   14706 C  CZ    . PHE D 2 187 ? 149.879 98.401  145.661 1.00 27.87 ?  166 PHE D CZ    1 
ATOM   14707 N  N     . LEU D 2 188 ? 147.027 97.302  141.569 1.00 20.78 ?  167 LEU D N     1 
ATOM   14708 C  CA    . LEU D 2 188 ? 148.096 96.490  140.950 1.00 21.78 ?  167 LEU D CA    1 
ATOM   14709 C  C     . LEU D 2 188 ? 148.279 96.696  139.442 1.00 21.91 ?  167 LEU D C     1 
ATOM   14710 O  O     . LEU D 2 188 ? 149.398 96.591  138.940 1.00 22.87 ?  167 LEU D O     1 
ATOM   14711 C  CB    . LEU D 2 188 ? 147.892 95.003  141.241 1.00 22.32 ?  167 LEU D CB    1 
ATOM   14712 C  CG    . LEU D 2 188 ? 148.026 94.470  142.666 1.00 23.33 ?  167 LEU D CG    1 
ATOM   14713 C  CD1   . LEU D 2 188 ? 147.749 92.977  142.654 1.00 22.43 ?  167 LEU D CD1   1 
ATOM   14714 C  CD2   . LEU D 2 188 ? 149.401 94.760  143.283 1.00 25.71 ?  167 LEU D CD2   1 
ATOM   14715 N  N     . PHE D 2 189 ? 147.188 96.967  138.722 1.00 21.56 ?  168 PHE D N     1 
ATOM   14716 C  CA    . PHE D 2 189 ? 147.257 97.255  137.287 1.00 21.86 ?  168 PHE D CA    1 
ATOM   14717 C  C     . PHE D 2 189 ? 148.051 98.541  136.974 1.00 21.87 ?  168 PHE D C     1 
ATOM   14718 O  O     . PHE D 2 189 ? 148.567 98.707  135.865 1.00 21.79 ?  168 PHE D O     1 
ATOM   14719 C  CB    . PHE D 2 189 ? 145.848 97.418  136.686 1.00 21.79 ?  168 PHE D CB    1 
ATOM   14720 C  CG    . PHE D 2 189 ? 145.131 96.119  136.398 1.00 21.88 ?  168 PHE D CG    1 
ATOM   14721 C  CD1   . PHE D 2 189 ? 145.811 95.009  135.892 1.00 21.44 ?  168 PHE D CD1   1 
ATOM   14722 C  CD2   . PHE D 2 189 ? 143.755 96.026  136.605 1.00 22.82 ?  168 PHE D CD2   1 
ATOM   14723 C  CE1   . PHE D 2 189 ? 145.132 93.813  135.623 1.00 22.35 ?  168 PHE D CE1   1 
ATOM   14724 C  CE2   . PHE D 2 189 ? 143.062 94.843  136.339 1.00 22.08 ?  168 PHE D CE2   1 
ATOM   14725 C  CZ    . PHE D 2 189 ? 143.753 93.728  135.857 1.00 22.60 ?  168 PHE D CZ    1 
ATOM   14726 N  N     . TYR D 2 190 ? 148.128 99.456  137.934 1.00 21.91 ?  169 TYR D N     1 
ATOM   14727 C  CA    . TYR D 2 190 ? 148.589 100.816 137.620 1.00 22.52 ?  169 TYR D CA    1 
ATOM   14728 C  C     . TYR D 2 190 ? 150.098 100.988 137.436 1.00 22.75 ?  169 TYR D C     1 
ATOM   14729 O  O     . TYR D 2 190 ? 150.512 101.889 136.718 1.00 21.93 ?  169 TYR D O     1 
ATOM   14730 C  CB    . TYR D 2 190 ? 147.985 101.851 138.574 1.00 22.67 ?  169 TYR D CB    1 
ATOM   14731 C  CG    . TYR D 2 190 ? 146.536 102.119 138.222 1.00 24.77 ?  169 TYR D CG    1 
ATOM   14732 C  CD1   . TYR D 2 190 ? 145.534 101.199 138.545 1.00 25.65 ?  169 TYR D CD1   1 
ATOM   14733 C  CD2   . TYR D 2 190 ? 146.175 103.268 137.523 1.00 25.94 ?  169 TYR D CD2   1 
ATOM   14734 C  CE1   . TYR D 2 190 ? 144.201 101.433 138.190 1.00 26.62 ?  169 TYR D CE1   1 
ATOM   14735 C  CE2   . TYR D 2 190 ? 144.848 103.519 137.180 1.00 26.91 ?  169 TYR D CE2   1 
ATOM   14736 C  CZ    . TYR D 2 190 ? 143.870 102.600 137.511 1.00 27.39 ?  169 TYR D CZ    1 
ATOM   14737 O  OH    . TYR D 2 190 ? 142.561 102.864 137.155 1.00 27.50 ?  169 TYR D OH    1 
ATOM   14738 N  N     . SER D 2 191 ? 150.907 100.115 138.044 1.00 22.74 ?  170 SER D N     1 
ATOM   14739 C  CA    . SER D 2 191 ? 152.341 100.087 137.728 1.00 23.43 ?  170 SER D CA    1 
ATOM   14740 C  C     . SER D 2 191 ? 152.522 99.749  136.248 1.00 23.08 ?  170 SER D C     1 
ATOM   14741 O  O     . SER D 2 191 ? 153.479 100.171 135.623 1.00 23.67 ?  170 SER D O     1 
ATOM   14742 C  CB    . SER D 2 191 ? 153.107 99.086  138.607 1.00 23.39 ?  170 SER D CB    1 
ATOM   14743 O  OG    . SER D 2 191 ? 152.639 97.758  138.416 1.00 24.10 ?  170 SER D OG    1 
ATOM   14744 N  N     . GLY D 2 192 ? 151.566 99.016  135.693 1.00 22.82 ?  171 GLY D N     1 
ATOM   14745 C  CA    . GLY D 2 192 ? 151.562 98.663  134.279 1.00 22.08 ?  171 GLY D CA    1 
ATOM   14746 C  C     . GLY D 2 192 ? 150.952 99.731  133.386 1.00 22.12 ?  171 GLY D C     1 
ATOM   14747 O  O     . GLY D 2 192 ? 151.559 100.124 132.388 1.00 22.86 ?  171 GLY D O     1 
ATOM   14748 N  N     . PHE D 2 193 ? 149.758 100.206 133.741 1.00 21.48 ?  172 PHE D N     1 
ATOM   14749 C  CA    . PHE D 2 193 ? 149.068 101.256 132.969 1.00 21.06 ?  172 PHE D CA    1 
ATOM   14750 C  C     . PHE D 2 193 ? 149.930 102.504 132.779 1.00 21.13 ?  172 PHE D C     1 
ATOM   14751 O  O     . PHE D 2 193 ? 149.778 103.213 131.783 1.00 21.18 ?  172 PHE D O     1 
ATOM   14752 C  CB    . PHE D 2 193 ? 147.764 101.673 133.649 1.00 21.33 ?  172 PHE D CB    1 
ATOM   14753 C  CG    . PHE D 2 193 ? 146.657 100.648 133.570 1.00 20.93 ?  172 PHE D CG    1 
ATOM   14754 C  CD1   . PHE D 2 193 ? 146.554 99.766  132.494 1.00 20.88 ?  172 PHE D CD1   1 
ATOM   14755 C  CD2   . PHE D 2 193 ? 145.683 100.609 134.559 1.00 19.83 ?  172 PHE D CD2   1 
ATOM   14756 C  CE1   . PHE D 2 193 ? 145.508 98.838  132.434 1.00 22.31 ?  172 PHE D CE1   1 
ATOM   14757 C  CE2   . PHE D 2 193 ? 144.627 99.693  134.498 1.00 20.67 ?  172 PHE D CE2   1 
ATOM   14758 C  CZ    . PHE D 2 193 ? 144.540 98.807  133.434 1.00 21.00 ?  172 PHE D CZ    1 
ATOM   14759 N  N     . TYR D 2 194 ? 150.838 102.758 133.723 1.00 20.48 ?  173 TYR D N     1 
ATOM   14760 C  CA    . TYR D 2 194 ? 151.683 103.949 133.685 1.00 20.76 ?  173 TYR D CA    1 
ATOM   14761 C  C     . TYR D 2 194 ? 152.319 104.160 132.306 1.00 20.53 ?  173 TYR D C     1 
ATOM   14762 O  O     . TYR D 2 194 ? 152.247 105.247 131.724 1.00 19.89 ?  173 TYR D O     1 
ATOM   14763 C  CB    . TYR D 2 194 ? 152.779 103.896 134.778 1.00 20.94 ?  173 TYR D CB    1 
ATOM   14764 C  CG    . TYR D 2 194 ? 153.526 105.211 134.918 1.00 21.56 ?  173 TYR D CG    1 
ATOM   14765 C  CD1   . TYR D 2 194 ? 153.199 106.117 135.930 1.00 22.23 ?  173 TYR D CD1   1 
ATOM   14766 C  CD2   . TYR D 2 194 ? 154.544 105.561 134.023 1.00 22.00 ?  173 TYR D CD2   1 
ATOM   14767 C  CE1   . TYR D 2 194 ? 153.866 107.336 136.046 1.00 21.58 ?  173 TYR D CE1   1 
ATOM   14768 C  CE2   . TYR D 2 194 ? 155.214 106.765 134.137 1.00 20.52 ?  173 TYR D CE2   1 
ATOM   14769 C  CZ    . TYR D 2 194 ? 154.872 107.647 135.147 1.00 21.66 ?  173 TYR D CZ    1 
ATOM   14770 O  OH    . TYR D 2 194 ? 155.522 108.855 135.242 1.00 21.37 ?  173 TYR D OH    1 
ATOM   14771 N  N     . TYR D 2 195 ? 152.916 103.108 131.772 1.00 20.77 ?  174 TYR D N     1 
ATOM   14772 C  CA    . TYR D 2 195 ? 153.728 103.259 130.577 1.00 21.12 ?  174 TYR D CA    1 
ATOM   14773 C  C     . TYR D 2 195 ? 152.907 103.603 129.321 1.00 21.49 ?  174 TYR D C     1 
ATOM   14774 O  O     . TYR D 2 195 ? 153.233 104.581 128.642 1.00 21.60 ?  174 TYR D O     1 
ATOM   14775 C  CB    . TYR D 2 195 ? 154.646 102.046 130.399 1.00 21.23 ?  174 TYR D CB    1 
ATOM   14776 C  CG    . TYR D 2 195 ? 155.957 102.334 129.704 1.00 21.77 ?  174 TYR D CG    1 
ATOM   14777 C  CD1   . TYR D 2 195 ? 156.663 103.519 129.942 1.00 23.28 ?  174 TYR D CD1   1 
ATOM   14778 C  CD2   . TYR D 2 195 ? 156.508 101.406 128.823 1.00 22.87 ?  174 TYR D CD2   1 
ATOM   14779 C  CE1   . TYR D 2 195 ? 157.882 103.771 129.296 1.00 23.81 ?  174 TYR D CE1   1 
ATOM   14780 C  CE2   . TYR D 2 195 ? 157.723 101.647 128.186 1.00 24.09 ?  174 TYR D CE2   1 
ATOM   14781 C  CZ    . TYR D 2 195 ? 158.398 102.827 128.421 1.00 23.51 ?  174 TYR D CZ    1 
ATOM   14782 O  OH    . TYR D 2 195 ? 159.598 103.063 127.777 1.00 25.36 ?  174 TYR D OH    1 
ATOM   14783 N  N     . PRO D 2 196 ? 151.840 102.822 129.012 1.00 21.86 ?  175 PRO D N     1 
ATOM   14784 C  CA    . PRO D 2 196 ? 150.967 103.203 127.891 1.00 22.03 ?  175 PRO D CA    1 
ATOM   14785 C  C     . PRO D 2 196 ? 150.386 104.608 128.039 1.00 22.18 ?  175 PRO D C     1 
ATOM   14786 O  O     . PRO D 2 196 ? 150.283 105.325 127.041 1.00 23.00 ?  175 PRO D O     1 
ATOM   14787 C  CB    . PRO D 2 196 ? 149.835 102.169 127.937 1.00 21.50 ?  175 PRO D CB    1 
ATOM   14788 C  CG    . PRO D 2 196 ? 150.369 101.035 128.660 1.00 22.47 ?  175 PRO D CG    1 
ATOM   14789 C  CD    . PRO D 2 196 ? 151.523 101.472 129.513 1.00 20.91 ?  175 PRO D CD    1 
ATOM   14790 N  N     . LEU D 2 197 ? 150.022 105.002 129.262 1.00 21.70 ?  176 LEU D N     1 
ATOM   14791 C  CA    . LEU D 2 197 ? 149.528 106.363 129.514 1.00 22.40 ?  176 LEU D CA    1 
ATOM   14792 C  C     . LEU D 2 197 ? 150.606 107.427 129.293 1.00 22.58 ?  176 LEU D C     1 
ATOM   14793 O  O     . LEU D 2 197 ? 150.315 108.521 128.791 1.00 22.15 ?  176 LEU D O     1 
ATOM   14794 C  CB    . LEU D 2 197 ? 148.984 106.496 130.931 1.00 22.15 ?  176 LEU D CB    1 
ATOM   14795 C  CG    . LEU D 2 197 ? 147.666 105.802 131.297 1.00 23.08 ?  176 LEU D CG    1 
ATOM   14796 C  CD1   . LEU D 2 197 ? 147.541 105.784 132.812 1.00 21.62 ?  176 LEU D CD1   1 
ATOM   14797 C  CD2   . LEU D 2 197 ? 146.461 106.511 130.645 1.00 21.94 ?  176 LEU D CD2   1 
ATOM   14798 N  N     . TYR D 2 198 ? 151.839 107.091 129.681 1.00 22.76 ?  177 TYR D N     1 
ATOM   14799 C  CA    . TYR D 2 198 ? 153.012 107.940 129.465 1.00 23.23 ?  177 TYR D CA    1 
ATOM   14800 C  C     . TYR D 2 198 ? 153.249 108.184 127.974 1.00 23.91 ?  177 TYR D C     1 
ATOM   14801 O  O     . TYR D 2 198 ? 153.454 109.333 127.555 1.00 24.20 ?  177 TYR D O     1 
ATOM   14802 C  CB    . TYR D 2 198 ? 154.246 107.319 130.140 1.00 23.19 ?  177 TYR D CB    1 
ATOM   14803 C  CG    . TYR D 2 198 ? 155.532 108.117 130.032 1.00 23.52 ?  177 TYR D CG    1 
ATOM   14804 C  CD1   . TYR D 2 198 ? 155.668 109.342 130.669 1.00 24.85 ?  177 TYR D CD1   1 
ATOM   14805 C  CD2   . TYR D 2 198 ? 156.631 107.616 129.323 1.00 25.30 ?  177 TYR D CD2   1 
ATOM   14806 C  CE1   . TYR D 2 198 ? 156.857 110.072 130.589 1.00 26.05 ?  177 TYR D CE1   1 
ATOM   14807 C  CE2   . TYR D 2 198 ? 157.833 108.339 129.239 1.00 26.38 ?  177 TYR D CE2   1 
ATOM   14808 C  CZ    . TYR D 2 198 ? 157.930 109.562 129.877 1.00 26.68 ?  177 TYR D CZ    1 
ATOM   14809 O  OH    . TYR D 2 198 ? 159.097 110.290 129.814 1.00 30.01 ?  177 TYR D OH    1 
ATOM   14810 N  N     . PHE D 2 199 ? 153.210 107.124 127.167 1.00 24.84 ?  178 PHE D N     1 
ATOM   14811 C  CA    . PHE D 2 199 ? 153.298 107.298 125.714 1.00 25.81 ?  178 PHE D CA    1 
ATOM   14812 C  C     . PHE D 2 199 ? 152.112 108.056 125.130 1.00 26.23 ?  178 PHE D C     1 
ATOM   14813 O  O     . PHE D 2 199 ? 152.291 108.959 124.312 1.00 26.58 ?  178 PHE D O     1 
ATOM   14814 C  CB    . PHE D 2 199 ? 153.474 105.962 125.003 1.00 26.08 ?  178 PHE D CB    1 
ATOM   14815 C  CG    . PHE D 2 199 ? 154.859 105.400 125.122 1.00 28.71 ?  178 PHE D CG    1 
ATOM   14816 C  CD1   . PHE D 2 199 ? 155.971 106.205 124.910 1.00 32.03 ?  178 PHE D CD1   1 
ATOM   14817 C  CD2   . PHE D 2 199 ? 155.059 104.069 125.450 1.00 31.77 ?  178 PHE D CD2   1 
ATOM   14818 C  CE1   . PHE D 2 199 ? 157.272 105.692 125.031 1.00 32.29 ?  178 PHE D CE1   1 
ATOM   14819 C  CE2   . PHE D 2 199 ? 156.353 103.549 125.563 1.00 32.72 ?  178 PHE D CE2   1 
ATOM   14820 C  CZ    . PHE D 2 199 ? 157.456 104.368 125.351 1.00 31.91 ?  178 PHE D CZ    1 
ATOM   14821 N  N     . TYR D 2 200 ? 150.914 107.674 125.563 1.00 26.46 ?  179 TYR D N     1 
ATOM   14822 C  CA    . TYR D 2 200 ? 149.647 108.270 125.112 1.00 27.43 ?  179 TYR D CA    1 
ATOM   14823 C  C     . TYR D 2 200 ? 149.635 109.775 125.358 1.00 27.68 ?  179 TYR D C     1 
ATOM   14824 O  O     . TYR D 2 200 ? 149.165 110.542 124.518 1.00 28.71 ?  179 TYR D O     1 
ATOM   14825 C  CB    . TYR D 2 200 ? 148.508 107.607 125.878 1.00 27.27 ?  179 TYR D CB    1 
ATOM   14826 C  CG    . TYR D 2 200 ? 147.111 107.757 125.326 1.00 28.90 ?  179 TYR D CG    1 
ATOM   14827 C  CD1   . TYR D 2 200 ? 146.833 107.531 123.985 1.00 29.00 ?  179 TYR D CD1   1 
ATOM   14828 C  CD2   . TYR D 2 200 ? 146.048 108.062 126.181 1.00 30.14 ?  179 TYR D CD2   1 
ATOM   14829 C  CE1   . TYR D 2 200 ? 145.535 107.643 123.492 1.00 31.26 ?  179 TYR D CE1   1 
ATOM   14830 C  CE2   . TYR D 2 200 ? 144.751 108.165 125.707 1.00 31.86 ?  179 TYR D CE2   1 
ATOM   14831 C  CZ    . TYR D 2 200 ? 144.500 107.960 124.361 1.00 32.51 ?  179 TYR D CZ    1 
ATOM   14832 O  OH    . TYR D 2 200 ? 143.214 108.066 123.889 1.00 33.77 ?  179 TYR D OH    1 
ATOM   14833 N  N     . GLY D 2 201 ? 150.158 110.192 126.510 1.00 27.68 ?  180 GLY D N     1 
ATOM   14834 C  CA    . GLY D 2 201 ? 150.268 111.607 126.848 1.00 28.02 ?  180 GLY D CA    1 
ATOM   14835 C  C     . GLY D 2 201 ? 151.302 112.386 126.041 1.00 28.60 ?  180 GLY D C     1 
ATOM   14836 O  O     . GLY D 2 201 ? 151.293 113.610 126.063 1.00 28.44 ?  180 GLY D O     1 
ATOM   14837 N  N     . GLN D 2 202 ? 152.194 111.670 125.350 1.00 29.34 ?  181 GLN D N     1 
ATOM   14838 C  CA    . GLN D 2 202 ? 153.250 112.256 124.506 1.00 30.39 ?  181 GLN D CA    1 
ATOM   14839 C  C     . GLN D 2 202 ? 152.935 112.203 123.011 1.00 30.55 ?  181 GLN D C     1 
ATOM   14840 O  O     . GLN D 2 202 ? 153.734 112.674 122.195 1.00 31.23 ?  181 GLN D O     1 
ATOM   14841 C  CB    . GLN D 2 202 ? 154.551 111.464 124.654 1.00 30.31 ?  181 GLN D CB    1 
ATOM   14842 C  CG    . GLN D 2 202 ? 155.261 111.523 125.954 1.00 32.40 ?  181 GLN D CG    1 
ATOM   14843 C  CD    . GLN D 2 202 ? 156.513 110.673 125.906 1.00 33.85 ?  181 GLN D CD    1 
ATOM   14844 O  OE1   . GLN D 2 202 ? 156.564 109.585 126.475 1.00 33.94 ?  181 GLN D OE1   1 
ATOM   14845 N  NE2   . GLN D 2 202 ? 157.515 111.145 125.185 1.00 34.92 ?  181 GLN D NE2   1 
ATOM   14846 N  N     . GLY D 2 203 ? 151.826 111.574 122.641 1.00 30.57 ?  182 GLY D N     1 
ATOM   14847 C  CA    . GLY D 2 203 ? 151.477 111.413 121.227 1.00 30.83 ?  182 GLY D CA    1 
ATOM   14848 C  C     . GLY D 2 203 ? 152.045 110.157 120.584 1.00 30.80 ?  182 GLY D C     1 
ATOM   14849 O  O     . GLY D 2 203 ? 151.996 110.007 119.360 1.00 30.86 ?  182 GLY D O     1 
ATOM   14850 N  N     . LYS D 2 204 ? 152.577 109.253 121.406 1.00 30.14 ?  183 LYS D N     1 
ATOM   14851 C  CA    . LYS D 2 204 ? 153.127 107.984 120.917 1.00 30.35 ?  183 LYS D CA    1 
ATOM   14852 C  C     . LYS D 2 204 ? 152.188 106.813 121.197 1.00 29.52 ?  183 LYS D C     1 
ATOM   14853 O  O     . LYS D 2 204 ? 151.496 106.803 122.212 1.00 28.60 ?  183 LYS D O     1 
ATOM   14854 C  CB    . LYS D 2 204 ? 154.497 107.722 121.538 1.00 30.76 ?  183 LYS D CB    1 
ATOM   14855 C  CG    . LYS D 2 204 ? 155.567 108.730 121.109 1.00 32.95 ?  183 LYS D CG    1 
ATOM   14856 C  CD    . LYS D 2 204 ? 156.795 108.580 121.974 1.00 36.37 ?  183 LYS D CD    1 
ATOM   14857 C  CE    . LYS D 2 204 ? 157.891 109.558 121.588 1.00 38.47 ?  183 LYS D CE    1 
ATOM   14858 N  NZ    . LYS D 2 204 ? 158.950 109.512 122.641 1.00 40.21 1  183 LYS D NZ    1 
ATOM   14859 N  N     . LEU D 2 205 ? 152.181 105.828 120.295 1.00 29.47 ?  184 LEU D N     1 
ATOM   14860 C  CA    . LEU D 2 205 ? 151.327 104.636 120.413 1.00 29.06 ?  184 LEU D CA    1 
ATOM   14861 C  C     . LEU D 2 205 ? 149.895 105.000 120.859 1.00 28.96 ?  184 LEU D C     1 
ATOM   14862 O  O     . LEU D 2 205 ? 149.372 104.482 121.854 1.00 27.68 ?  184 LEU D O     1 
ATOM   14863 C  CB    . LEU D 2 205 ? 151.959 103.593 121.348 1.00 28.63 ?  184 LEU D CB    1 
ATOM   14864 C  CG    . LEU D 2 205 ? 153.374 103.093 121.017 1.00 29.00 ?  184 LEU D CG    1 
ATOM   14865 C  CD1   . LEU D 2 205 ? 153.862 102.126 122.099 1.00 28.90 ?  184 LEU D CD1   1 
ATOM   14866 C  CD2   . LEU D 2 205 ? 153.424 102.422 119.651 1.00 28.67 ?  184 LEU D CD2   1 
ATOM   14867 N  N     . MET D 2 206 ? 149.288 105.899 120.091 1.00 29.02 ?  185 MET D N     1 
ATOM   14868 C  CA    . MET D 2 206 ? 147.975 106.457 120.374 1.00 29.72 ?  185 MET D CA    1 
ATOM   14869 C  C     . MET D 2 206 ? 146.806 105.486 120.247 1.00 29.54 ?  185 MET D C     1 
ATOM   14870 O  O     . MET D 2 206 ? 145.826 105.615 120.976 1.00 29.47 ?  185 MET D O     1 
ATOM   14871 C  CB    . MET D 2 206 ? 147.729 107.679 119.480 1.00 30.69 ?  185 MET D CB    1 
ATOM   14872 C  CG    . MET D 2 206 ? 148.772 108.771 119.668 1.00 32.03 ?  185 MET D CG    1 
ATOM   14873 S  SD    . MET D 2 206 ? 148.827 109.339 121.377 1.00 36.63 ?  185 MET D SD    1 
ATOM   14874 C  CE    . MET D 2 206 ? 147.518 110.550 121.361 1.00 33.80 ?  185 MET D CE    1 
ATOM   14875 N  N     . GLN D 2 207 ? 146.896 104.541 119.312 1.00 29.56 ?  186 GLN D N     1 
ATOM   14876 C  CA    . GLN D 2 207 ? 145.817 103.573 119.087 1.00 29.17 ?  186 GLN D CA    1 
ATOM   14877 C  C     . GLN D 2 207 ? 145.755 102.562 120.228 1.00 28.26 ?  186 GLN D C     1 
ATOM   14878 O  O     . GLN D 2 207 ? 144.682 102.301 120.766 1.00 27.98 ?  186 GLN D O     1 
ATOM   14879 C  CB    . GLN D 2 207 ? 145.979 102.853 117.738 1.00 29.80 ?  186 GLN D CB    1 
ATOM   14880 C  CG    . GLN D 2 207 ? 146.110 103.781 116.532 1.00 31.75 ?  186 GLN D CG    1 
ATOM   14881 C  CD    . GLN D 2 207 ? 144.998 104.810 116.478 1.00 34.93 ?  186 GLN D CD    1 
ATOM   14882 O  OE1   . GLN D 2 207 ? 143.837 104.485 116.196 1.00 36.91 ?  186 GLN D OE1   1 
ATOM   14883 N  NE2   . GLN D 2 207 ? 145.345 106.061 116.761 1.00 36.09 ?  186 GLN D NE2   1 
ATOM   14884 N  N     . SER D 2 208 ? 146.903 101.998 120.597 0.50 27.75 ?  187 SER D N     1 
ATOM   14885 C  CA    . SER D 2 208 ? 146.957 101.061 121.713 0.50 27.12 ?  187 SER D CA    1 
ATOM   14886 C  C     . SER D 2 208 ? 146.720 101.783 123.037 0.50 26.72 ?  187 SER D C     1 
ATOM   14887 O  O     . SER D 2 208 ? 146.152 101.202 123.960 0.50 26.30 ?  187 SER D O     1 
ATOM   14888 C  CB    . SER D 2 208 ? 148.285 100.303 121.739 0.50 26.88 ?  187 SER D CB    1 
ATOM   14889 O  OG    . SER D 2 208 ? 149.372 101.200 121.687 0.50 26.59 ?  187 SER D OG    1 
ATOM   14890 N  N     . GLY D 2 209 ? 147.153 103.042 123.117 1.00 26.64 ?  188 GLY D N     1 
ATOM   14891 C  CA    . GLY D 2 209 ? 146.901 103.887 124.302 1.00 26.43 ?  188 GLY D CA    1 
ATOM   14892 C  C     . GLY D 2 209 ? 145.421 104.187 124.501 1.00 26.66 ?  188 GLY D C     1 
ATOM   14893 O  O     . GLY D 2 209 ? 144.936 104.258 125.631 1.00 26.57 ?  188 GLY D O     1 
ATOM   14894 N  N     . GLU D 2 210 ? 144.697 104.370 123.401 1.00 27.42 ?  189 GLU D N     1 
ATOM   14895 C  CA    . GLU D 2 210 ? 143.248 104.551 123.461 1.00 27.73 ?  189 GLU D CA    1 
ATOM   14896 C  C     . GLU D 2 210 ? 142.584 103.273 123.995 1.00 27.04 ?  189 GLU D C     1 
ATOM   14897 O  O     . GLU D 2 210 ? 141.729 103.331 124.879 1.00 26.57 ?  189 GLU D O     1 
ATOM   14898 C  CB    . GLU D 2 210 ? 142.678 104.948 122.088 1.00 28.28 ?  189 GLU D CB    1 
ATOM   14899 C  CG    . GLU D 2 210 ? 141.171 105.249 122.115 1.00 30.71 ?  189 GLU D CG    1 
ATOM   14900 C  CD    . GLU D 2 210 ? 140.635 105.894 120.838 1.00 35.43 ?  189 GLU D CD    1 
ATOM   14901 O  OE1   . GLU D 2 210 ? 141.374 105.989 119.827 1.00 36.89 ?  189 GLU D OE1   1 
ATOM   14902 O  OE2   . GLU D 2 210 ? 139.458 106.321 120.857 1.00 37.04 -1 189 GLU D OE2   1 
ATOM   14903 N  N     . ILE D 2 211 ? 142.993 102.126 123.462 1.00 26.80 ?  190 ILE D N     1 
ATOM   14904 C  CA    . ILE D 2 211 ? 142.517 100.839 123.960 1.00 26.92 ?  190 ILE D CA    1 
ATOM   14905 C  C     . ILE D 2 211 ? 142.793 100.690 125.450 1.00 26.45 ?  190 ILE D C     1 
ATOM   14906 O  O     . ILE D 2 211 ? 141.897 100.317 126.204 1.00 26.65 ?  190 ILE D O     1 
ATOM   14907 C  CB    . ILE D 2 211 ? 143.103 99.648  123.159 1.00 27.00 ?  190 ILE D CB    1 
ATOM   14908 C  CG1   . ILE D 2 211 ? 142.493 99.627  121.752 1.00 28.77 ?  190 ILE D CG1   1 
ATOM   14909 C  CG2   . ILE D 2 211 ? 142.827 98.317  123.878 1.00 26.82 ?  190 ILE D CG2   1 
ATOM   14910 C  CD1   . ILE D 2 211 ? 143.097 98.597  120.805 1.00 30.88 ?  190 ILE D CD1   1 
ATOM   14911 N  N     . ILE D 2 212 ? 144.017 101.007 125.883 1.00 26.49 ?  191 ILE D N     1 
ATOM   14912 C  CA    . ILE D 2 212 ? 144.384 100.849 127.291 1.00 25.73 ?  191 ILE D CA    1 
ATOM   14913 C  C     . ILE D 2 212 ? 143.532 101.758 128.179 1.00 25.48 ?  191 ILE D C     1 
ATOM   14914 O  O     . ILE D 2 212 ? 143.104 101.356 129.265 1.00 24.95 ?  191 ILE D O     1 
ATOM   14915 C  CB    . ILE D 2 212 ? 145.904 101.082 127.539 1.00 26.44 ?  191 ILE D CB    1 
ATOM   14916 C  CG1   . ILE D 2 212 ? 146.742 100.002 126.842 1.00 26.71 ?  191 ILE D CG1   1 
ATOM   14917 C  CG2   . ILE D 2 212 ? 146.221 101.138 129.050 1.00 26.01 ?  191 ILE D CG2   1 
ATOM   14918 C  CD1   . ILE D 2 212 ? 146.517 98.579  127.318 1.00 30.50 ?  191 ILE D CD1   1 
ATOM   14919 N  N     . ASN D 2 213 ? 143.270 102.970 127.699 1.00 24.79 ?  192 ASN D N     1 
ATOM   14920 C  CA    . ASN D 2 213 ? 142.437 103.914 128.432 1.00 24.80 ?  192 ASN D CA    1 
ATOM   14921 C  C     . ASN D 2 213 ? 140.994 103.403 128.626 1.00 24.44 ?  192 ASN D C     1 
ATOM   14922 O  O     . ASN D 2 213 ? 140.369 103.659 129.661 1.00 23.25 ?  192 ASN D O     1 
ATOM   14923 C  CB    . ASN D 2 213 ? 142.456 105.279 127.743 1.00 25.68 ?  192 ASN D CB    1 
ATOM   14924 C  CG    . ASN D 2 213 ? 142.453 106.432 128.729 1.00 27.89 ?  192 ASN D CG    1 
ATOM   14925 O  OD1   . ASN D 2 213 ? 142.969 106.324 129.838 1.00 31.05 ?  192 ASN D OD1   1 
ATOM   14926 N  ND2   . ASN D 2 213 ? 141.872 107.551 128.320 1.00 31.70 ?  192 ASN D ND2   1 
ATOM   14927 N  N     . LEU D 2 214 ? 140.480 102.673 127.636 1.00 23.60 ?  193 LEU D N     1 
ATOM   14928 C  CA    . LEU D 2 214 ? 139.135 102.101 127.732 1.00 23.84 ?  193 LEU D CA    1 
ATOM   14929 C  C     . LEU D 2 214 ? 139.124 100.954 128.726 1.00 23.48 ?  193 LEU D C     1 
ATOM   14930 O  O     . LEU D 2 214 ? 138.191 100.829 129.524 1.00 24.12 ?  193 LEU D O     1 
ATOM   14931 C  CB    . LEU D 2 214 ? 138.651 101.623 126.364 1.00 23.71 ?  193 LEU D CB    1 
ATOM   14932 C  CG    . LEU D 2 214 ? 138.257 102.730 125.378 1.00 25.29 ?  193 LEU D CG    1 
ATOM   14933 C  CD1   . LEU D 2 214 ? 137.935 102.136 124.006 1.00 25.41 ?  193 LEU D CD1   1 
ATOM   14934 C  CD2   . LEU D 2 214 ? 137.081 103.546 125.889 1.00 25.80 ?  193 LEU D CD2   1 
ATOM   14935 N  N     . ILE D 2 215 ? 140.170 100.129 128.676 1.00 22.89 ?  194 ILE D N     1 
ATOM   14936 C  CA    . ILE D 2 215 ? 140.336 99.027  129.612 1.00 22.25 ?  194 ILE D CA    1 
ATOM   14937 C  C     . ILE D 2 215 ? 140.415 99.583  131.029 1.00 22.55 ?  194 ILE D C     1 
ATOM   14938 O  O     . ILE D 2 215 ? 139.691 99.135  131.930 1.00 22.53 ?  194 ILE D O     1 
ATOM   14939 C  CB    . ILE D 2 215 ? 141.602 98.200  129.306 1.00 22.37 ?  194 ILE D CB    1 
ATOM   14940 C  CG1   . ILE D 2 215 ? 141.451 97.471  127.964 1.00 21.89 ?  194 ILE D CG1   1 
ATOM   14941 C  CG2   . ILE D 2 215 ? 141.900 97.222  130.460 1.00 20.25 ?  194 ILE D CG2   1 
ATOM   14942 C  CD1   . ILE D 2 215 ? 142.667 96.629  127.560 1.00 20.48 ?  194 ILE D CD1   1 
ATOM   14943 N  N     . LEU D 2 216 ? 141.284 100.573 131.218 1.00 22.35 ?  195 LEU D N     1 
ATOM   14944 C  CA    . LEU D 2 216 ? 141.502 101.166 132.534 1.00 22.51 ?  195 LEU D CA    1 
ATOM   14945 C  C     . LEU D 2 216 ? 140.192 101.735 133.088 1.00 22.30 ?  195 LEU D C     1 
ATOM   14946 O  O     . LEU D 2 216 ? 139.900 101.573 134.280 1.00 21.62 ?  195 LEU D O     1 
ATOM   14947 C  CB    . LEU D 2 216 ? 142.578 102.258 132.435 1.00 23.06 ?  195 LEU D CB    1 
ATOM   14948 C  CG    . LEU D 2 216 ? 142.974 103.173 133.604 1.00 23.98 ?  195 LEU D CG    1 
ATOM   14949 C  CD1   . LEU D 2 216 ? 144.289 103.824 133.266 1.00 24.44 ?  195 LEU D CD1   1 
ATOM   14950 C  CD2   . LEU D 2 216 ? 141.917 104.256 133.883 1.00 25.00 ?  195 LEU D CD2   1 
ATOM   14951 N  N     . ARG D 2 217 ? 139.419 102.402 132.223 1.00 21.64 ?  196 ARG D N     1 
ATOM   14952 C  CA    . ARG D 2 217 ? 138.117 102.956 132.613 1.00 22.49 ?  196 ARG D CA    1 
ATOM   14953 C  C     . ARG D 2 217 ? 137.148 101.850 133.099 1.00 21.56 ?  196 ARG D C     1 
ATOM   14954 O  O     . ARG D 2 217 ? 136.417 102.058 134.059 1.00 21.32 ?  196 ARG D O     1 
ATOM   14955 C  CB    . ARG D 2 217 ? 137.492 103.806 131.490 1.00 23.07 ?  196 ARG D CB    1 
ATOM   14956 C  CG    . ARG D 2 217 ? 136.208 104.556 131.907 1.00 25.64 ?  196 ARG D CG    1 
ATOM   14957 C  CD    . ARG D 2 217 ? 135.480 105.216 130.722 1.00 32.11 ?  196 ARG D CD    1 
ATOM   14958 N  NE    . ARG D 2 217 ? 135.092 104.243 129.692 1.00 35.06 ?  196 ARG D NE    1 
ATOM   14959 C  CZ    . ARG D 2 217 ? 134.273 104.499 128.677 1.00 37.65 ?  196 ARG D CZ    1 
ATOM   14960 N  NH1   . ARG D 2 217 ? 133.716 105.699 128.548 1.00 40.20 1  196 ARG D NH1   1 
ATOM   14961 N  NH2   . ARG D 2 217 ? 133.994 103.547 127.791 1.00 38.20 ?  196 ARG D NH2   1 
ATOM   14962 N  N     . ASP D 2 218 ? 137.151 100.688 132.444 1.00 21.34 ?  197 ASP D N     1 
ATOM   14963 C  CA    . ASP D 2 218 ? 136.402 99.523  132.937 1.00 21.09 ?  197 ASP D CA    1 
ATOM   14964 C  C     . ASP D 2 218 ? 136.929 99.034  134.302 1.00 20.65 ?  197 ASP D C     1 
ATOM   14965 O  O     . ASP D 2 218 ? 136.139 98.789  135.217 1.00 20.16 ?  197 ASP D O     1 
ATOM   14966 C  CB    . ASP D 2 218 ? 136.432 98.364  131.929 1.00 21.58 ?  197 ASP D CB    1 
ATOM   14967 C  CG    . ASP D 2 218 ? 135.677 98.672  130.637 1.00 22.60 ?  197 ASP D CG    1 
ATOM   14968 O  OD1   . ASP D 2 218 ? 134.775 99.542  130.634 1.00 24.72 ?  197 ASP D OD1   1 
ATOM   14969 O  OD2   . ASP D 2 218 ? 136.004 98.037  129.608 1.00 22.64 -1 197 ASP D OD2   1 
ATOM   14970 N  N     . GLU D 2 219 ? 138.248 98.888  134.449 1.00 20.59 ?  198 GLU D N     1 
ATOM   14971 C  CA    . GLU D 2 219 ? 138.801 98.382  135.725 1.00 20.66 ?  198 GLU D CA    1 
ATOM   14972 C  C     . GLU D 2 219 ? 138.483 99.320  136.893 1.00 20.45 ?  198 GLU D C     1 
ATOM   14973 O  O     . GLU D 2 219 ? 138.229 98.861  138.011 1.00 20.59 ?  198 GLU D O     1 
ATOM   14974 C  CB    . GLU D 2 219 ? 140.313 98.117  135.649 1.00 20.55 ?  198 GLU D CB    1 
ATOM   14975 C  CG    . GLU D 2 219 ? 140.829 97.429  134.348 1.00 21.99 ?  198 GLU D CG    1 
ATOM   14976 C  CD    . GLU D 2 219 ? 140.250 96.037  134.063 1.00 24.00 ?  198 GLU D CD    1 
ATOM   14977 O  OE1   . GLU D 2 219 ? 139.143 95.692  134.530 1.00 25.06 ?  198 GLU D OE1   1 
ATOM   14978 O  OE2   . GLU D 2 219 ? 140.901 95.277  133.328 1.00 24.49 -1 198 GLU D OE2   1 
ATOM   14979 N  N     . ALA D 2 220 ? 138.483 100.624 136.626 1.00 20.47 ?  199 ALA D N     1 
ATOM   14980 C  CA    . ALA D 2 220 ? 138.112 101.627 137.646 1.00 21.10 ?  199 ALA D CA    1 
ATOM   14981 C  C     . ALA D 2 220 ? 136.714 101.384 138.208 1.00 21.34 ?  199 ALA D C     1 
ATOM   14982 O  O     . ALA D 2 220 ? 136.553 101.263 139.421 1.00 21.19 ?  199 ALA D O     1 
ATOM   14983 C  CB    . ALA D 2 220 ? 138.244 103.052 137.100 1.00 21.09 ?  199 ALA D CB    1 
ATOM   14984 N  N     . ILE D 2 221 ? 135.715 101.284 137.329 1.00 21.31 ?  200 ILE D N     1 
ATOM   14985 C  CA    . ILE D 2 221 ? 134.360 100.966 137.774 1.00 21.80 ?  200 ILE D CA    1 
ATOM   14986 C  C     . ILE D 2 221 ? 134.230 99.562  138.403 1.00 20.90 ?  200 ILE D C     1 
ATOM   14987 O  O     . ILE D 2 221 ? 133.485 99.390  139.367 1.00 20.54 ?  200 ILE D O     1 
ATOM   14988 C  CB    . ILE D 2 221 ? 133.280 101.240 136.688 1.00 22.75 ?  200 ILE D CB    1 
ATOM   14989 C  CG1   . ILE D 2 221 ? 131.901 101.293 137.336 1.00 24.63 ?  200 ILE D CG1   1 
ATOM   14990 C  CG2   . ILE D 2 221 ? 133.291 100.173 135.595 1.00 23.38 ?  200 ILE D CG2   1 
ATOM   14991 C  CD1   . ILE D 2 221 ? 130.876 102.037 136.531 1.00 26.91 ?  200 ILE D CD1   1 
ATOM   14992 N  N     . HIS D 2 222 ? 134.978 98.576  137.895 1.00 20.31 ?  201 HIS D N     1 
ATOM   14993 C  CA    . HIS D 2 222 ? 134.988 97.251  138.521 1.00 20.25 ?  201 HIS D CA    1 
ATOM   14994 C  C     . HIS D 2 222 ? 135.453 97.355  139.972 1.00 20.51 ?  201 HIS D C     1 
ATOM   14995 O  O     . HIS D 2 222 ? 134.798 96.835  140.884 1.00 20.99 ?  201 HIS D O     1 
ATOM   14996 C  CB    . HIS D 2 222 ? 135.877 96.257  137.764 1.00 19.79 ?  201 HIS D CB    1 
ATOM   14997 C  CG    . HIS D 2 222 ? 135.445 95.980  136.357 1.00 19.25 ?  201 HIS D CG    1 
ATOM   14998 N  ND1   . HIS D 2 222 ? 136.215 95.237  135.487 1.00 18.35 ?  201 HIS D ND1   1 
ATOM   14999 C  CD2   . HIS D 2 222 ? 134.340 96.350  135.661 1.00 17.64 ?  201 HIS D CD2   1 
ATOM   15000 C  CE1   . HIS D 2 222 ? 135.600 95.147  134.320 1.00 18.28 ?  201 HIS D CE1   1 
ATOM   15001 N  NE2   . HIS D 2 222 ? 134.465 95.821  134.397 1.00 20.01 ?  201 HIS D NE2   1 
ATOM   15002 N  N     . GLY D 2 223 ? 136.573 98.049  140.183 1.00 20.33 ?  202 GLY D N     1 
ATOM   15003 C  CA    . GLY D 2 223 ? 137.118 98.274  141.528 1.00 19.94 ?  202 GLY D CA    1 
ATOM   15004 C  C     . GLY D 2 223 ? 136.151 98.984  142.470 1.00 19.80 ?  202 GLY D C     1 
ATOM   15005 O  O     . GLY D 2 223 ? 135.990 98.570  143.617 1.00 19.96 ?  202 GLY D O     1 
ATOM   15006 N  N     . VAL D 2 224 ? 135.483 100.032 141.983 1.00 19.49 ?  203 VAL D N     1 
ATOM   15007 C  CA    . VAL D 2 224 ? 134.498 100.760 142.799 1.00 18.88 ?  203 VAL D CA    1 
ATOM   15008 C  C     . VAL D 2 224 ? 133.315 99.868  143.197 1.00 18.55 ?  203 VAL D C     1 
ATOM   15009 O  O     . VAL D 2 224 ? 132.884 99.861  144.361 1.00 17.65 ?  203 VAL D O     1 
ATOM   15010 C  CB    . VAL D 2 224 ? 133.989 102.069 142.091 1.00 19.22 ?  203 VAL D CB    1 
ATOM   15011 C  CG1   . VAL D 2 224 ? 132.938 102.791 142.959 1.00 18.51 ?  203 VAL D CG1   1 
ATOM   15012 C  CG2   . VAL D 2 224 ? 135.165 103.020 141.786 1.00 19.69 ?  203 VAL D CG2   1 
ATOM   15013 N  N     . TYR D 2 225 ? 132.811 99.098  142.234 1.00 18.17 ?  204 TYR D N     1 
ATOM   15014 C  CA    . TYR D 2 225 ? 131.660 98.221  142.458 1.00 18.76 ?  204 TYR D CA    1 
ATOM   15015 C  C     . TYR D 2 225 ? 131.976 97.101  143.465 1.00 18.93 ?  204 TYR D C     1 
ATOM   15016 O  O     . TYR D 2 225 ? 131.256 96.916  144.456 1.00 18.77 ?  204 TYR D O     1 
ATOM   15017 C  CB    . TYR D 2 225 ? 131.145 97.627  141.131 1.00 18.96 ?  204 TYR D CB    1 
ATOM   15018 C  CG    . TYR D 2 225 ? 129.865 96.822  141.329 1.00 20.06 ?  204 TYR D CG    1 
ATOM   15019 C  CD1   . TYR D 2 225 ? 128.678 97.457  141.717 1.00 21.79 ?  204 TYR D CD1   1 
ATOM   15020 C  CD2   . TYR D 2 225 ? 129.849 95.434  141.162 1.00 19.51 ?  204 TYR D CD2   1 
ATOM   15021 C  CE1   . TYR D 2 225 ? 127.506 96.729  141.929 1.00 20.38 ?  204 TYR D CE1   1 
ATOM   15022 C  CE2   . TYR D 2 225 ? 128.666 94.691  141.369 1.00 19.38 ?  204 TYR D CE2   1 
ATOM   15023 C  CZ    . TYR D 2 225 ? 127.505 95.355  141.756 1.00 20.84 ?  204 TYR D CZ    1 
ATOM   15024 O  OH    . TYR D 2 225 ? 126.337 94.662  141.982 1.00 20.77 ?  204 TYR D OH    1 
ATOM   15025 N  N     . VAL D 2 226 ? 133.056 96.363  143.218 1.00 18.76 ?  205 VAL D N     1 
ATOM   15026 C  CA    . VAL D 2 226 ? 133.458 95.302  144.139 1.00 18.85 ?  205 VAL D CA    1 
ATOM   15027 C  C     . VAL D 2 226 ? 133.745 95.892  145.519 1.00 19.19 ?  205 VAL D C     1 
ATOM   15028 O  O     . VAL D 2 226 ? 133.428 95.267  146.533 1.00 19.87 ?  205 VAL D O     1 
ATOM   15029 C  CB    . VAL D 2 226 ? 134.649 94.498  143.604 1.00 19.28 ?  205 VAL D CB    1 
ATOM   15030 C  CG1   . VAL D 2 226 ? 135.097 93.421  144.629 1.00 18.22 ?  205 VAL D CG1   1 
ATOM   15031 C  CG2   . VAL D 2 226 ? 134.257 93.855  142.263 1.00 18.40 ?  205 VAL D CG2   1 
ATOM   15032 N  N     . GLY D 2 227 ? 134.313 97.099  145.546 1.00 18.53 ?  206 GLY D N     1 
ATOM   15033 C  CA    . GLY D 2 227 ? 134.531 97.834  146.806 1.00 18.74 ?  206 GLY D CA    1 
ATOM   15034 C  C     . GLY D 2 227 ? 133.268 98.061  147.620 1.00 19.17 ?  206 GLY D C     1 
ATOM   15035 O  O     . GLY D 2 227 ? 133.277 97.937  148.853 1.00 18.66 ?  206 GLY D O     1 
ATOM   15036 N  N     . LEU D 2 228 ? 132.180 98.412  146.937 1.00 19.00 ?  207 LEU D N     1 
ATOM   15037 C  CA    . LEU D 2 228 ? 130.898 98.616  147.614 1.00 19.73 ?  207 LEU D CA    1 
ATOM   15038 C  C     . LEU D 2 228 ? 130.351 97.294  148.170 1.00 19.76 ?  207 LEU D C     1 
ATOM   15039 O  O     . LEU D 2 228 ? 129.826 97.261  149.283 1.00 20.07 ?  207 LEU D O     1 
ATOM   15040 C  CB    . LEU D 2 228 ? 129.893 99.299  146.683 1.00 19.36 ?  207 LEU D CB    1 
ATOM   15041 C  CG    . LEU D 2 228 ? 130.202 100.765 146.342 1.00 20.50 ?  207 LEU D CG    1 
ATOM   15042 C  CD1   . LEU D 2 228 ? 129.307 101.253 145.218 1.00 19.87 ?  207 LEU D CD1   1 
ATOM   15043 C  CD2   . LEU D 2 228 ? 130.061 101.685 147.590 1.00 22.38 ?  207 LEU D CD2   1 
ATOM   15044 N  N     . LEU D 2 229 ? 130.515 96.205  147.420 1.00 19.27 ?  208 LEU D N     1 
ATOM   15045 C  CA    . LEU D 2 229 ? 130.131 94.868  147.912 1.00 19.47 ?  208 LEU D CA    1 
ATOM   15046 C  C     . LEU D 2 229 ? 130.940 94.432  149.140 1.00 19.67 ?  208 LEU D C     1 
ATOM   15047 O  O     . LEU D 2 229 ? 130.404 93.780  150.044 1.00 19.82 ?  208 LEU D O     1 
ATOM   15048 C  CB    . LEU D 2 229 ? 130.252 93.807  146.798 1.00 19.51 ?  208 LEU D CB    1 
ATOM   15049 C  CG    . LEU D 2 229 ? 129.405 93.949  145.522 1.00 19.48 ?  208 LEU D CG    1 
ATOM   15050 C  CD1   . LEU D 2 229 ? 129.806 92.873  144.496 1.00 20.14 ?  208 LEU D CD1   1 
ATOM   15051 C  CD2   . LEU D 2 229 ? 127.886 93.914  145.796 1.00 19.95 ?  208 LEU D CD2   1 
ATOM   15052 N  N     . ALA D 2 230 ? 132.227 94.781  149.172 1.00 19.43 ?  209 ALA D N     1 
ATOM   15053 C  CA    . ALA D 2 230 ? 133.077 94.508  150.338 1.00 20.29 ?  209 ALA D CA    1 
ATOM   15054 C  C     . ALA D 2 230 ? 132.658 95.326  151.561 1.00 21.17 ?  209 ALA D C     1 
ATOM   15055 O  O     . ALA D 2 230 ? 132.598 94.799  152.667 1.00 21.73 ?  209 ALA D O     1 
ATOM   15056 C  CB    . ALA D 2 230 ? 134.545 94.756  150.003 1.00 19.99 ?  209 ALA D CB    1 
ATOM   15057 N  N     . GLN D 2 231 ? 132.364 96.611  151.361 1.00 22.26 ?  210 GLN D N     1 
ATOM   15058 C  CA    . GLN D 2 231 ? 131.891 97.481  152.454 1.00 23.33 ?  210 GLN D CA    1 
ATOM   15059 C  C     . GLN D 2 231 ? 130.578 96.978  153.063 1.00 23.85 ?  210 GLN D C     1 
ATOM   15060 O  O     . GLN D 2 231 ? 130.379 97.070  154.271 1.00 24.91 ?  210 GLN D O     1 
ATOM   15061 C  CB    . GLN D 2 231 ? 131.707 98.925  151.975 1.00 23.49 ?  210 GLN D CB    1 
ATOM   15062 C  CG    . GLN D 2 231 ? 132.993 99.651  151.570 1.00 23.05 ?  210 GLN D CG    1 
ATOM   15063 C  CD    . GLN D 2 231 ? 132.715 101.072 151.081 1.00 24.65 ?  210 GLN D CD    1 
ATOM   15064 O  OE1   . GLN D 2 231 ? 132.037 101.841 151.761 1.00 25.85 ?  210 GLN D OE1   1 
ATOM   15065 N  NE2   . GLN D 2 231 ? 133.223 101.417 149.897 1.00 22.30 ?  210 GLN D NE2   1 
ATOM   15066 N  N     . GLU D 2 232 ? 129.683 96.466  152.223 1.00 24.36 ?  211 GLU D N     1 
ATOM   15067 C  CA    . GLU D 2 232 ? 128.452 95.839  152.697 1.00 24.83 ?  211 GLU D CA    1 
ATOM   15068 C  C     . GLU D 2 232 ? 128.731 94.707  153.693 1.00 24.34 ?  211 GLU D C     1 
ATOM   15069 O  O     . GLU D 2 232 ? 128.087 94.635  154.741 1.00 24.20 ?  211 GLU D O     1 
ATOM   15070 C  CB    . GLU D 2 232 ? 127.632 95.310  151.526 1.00 25.15 ?  211 GLU D CB    1 
ATOM   15071 C  CG    . GLU D 2 232 ? 126.235 94.887  151.898 1.00 28.55 ?  211 GLU D CG    1 
ATOM   15072 C  CD    . GLU D 2 232 ? 125.472 94.400  150.696 1.00 33.83 ?  211 GLU D CD    1 
ATOM   15073 O  OE1   . GLU D 2 232 ? 124.785 95.230  150.067 1.00 35.09 ?  211 GLU D OE1   1 
ATOM   15074 O  OE2   . GLU D 2 232 ? 125.594 93.202  150.356 1.00 35.51 -1 211 GLU D OE2   1 
ATOM   15075 N  N     . ILE D 2 233 ? 129.687 93.837  153.372 1.00 23.39 ?  212 ILE D N     1 
ATOM   15076 C  CA    . ILE D 2 233 ? 130.086 92.761  154.296 1.00 23.42 ?  212 ILE D CA    1 
ATOM   15077 C  C     . ILE D 2 233 ? 130.741 93.334  155.553 1.00 23.74 ?  212 ILE D C     1 
ATOM   15078 O  O     . ILE D 2 233 ? 130.376 92.977  156.672 1.00 24.61 ?  212 ILE D O     1 
ATOM   15079 C  CB    . ILE D 2 233 ? 131.007 91.710  153.619 1.00 22.81 ?  212 ILE D CB    1 
ATOM   15080 C  CG1   . ILE D 2 233 ? 130.242 90.952  152.524 1.00 22.94 ?  212 ILE D CG1   1 
ATOM   15081 C  CG2   . ILE D 2 233 ? 131.554 90.714  154.651 1.00 22.45 ?  212 ILE D CG2   1 
ATOM   15082 C  CD1   . ILE D 2 233 ? 131.148 90.147  151.567 1.00 22.21 ?  212 ILE D CD1   1 
ATOM   15083 N  N     . TYR D 2 234 ? 131.697 94.239  155.362 1.00 24.19 ?  213 TYR D N     1 
ATOM   15084 C  CA    . TYR D 2 234 ? 132.410 94.885  156.455 1.00 24.59 ?  213 TYR D CA    1 
ATOM   15085 C  C     . TYR D 2 234 ? 131.446 95.506  157.472 1.00 25.15 ?  213 TYR D C     1 
ATOM   15086 O  O     . TYR D 2 234 ? 131.651 95.373  158.681 1.00 24.94 ?  213 TYR D O     1 
ATOM   15087 C  CB    . TYR D 2 234 ? 133.346 95.960  155.896 1.00 24.41 ?  213 TYR D CB    1 
ATOM   15088 C  CG    . TYR D 2 234 ? 134.142 96.725  156.933 1.00 25.93 ?  213 TYR D CG    1 
ATOM   15089 C  CD1   . TYR D 2 234 ? 135.351 96.231  157.411 1.00 24.70 ?  213 TYR D CD1   1 
ATOM   15090 C  CD2   . TYR D 2 234 ? 133.684 97.954  157.429 1.00 26.11 ?  213 TYR D CD2   1 
ATOM   15091 C  CE1   . TYR D 2 234 ? 136.090 96.933  158.359 1.00 27.90 ?  213 TYR D CE1   1 
ATOM   15092 C  CE2   . TYR D 2 234 ? 134.419 98.662  158.370 1.00 27.70 ?  213 TYR D CE2   1 
ATOM   15093 C  CZ    . TYR D 2 234 ? 135.619 98.149  158.828 1.00 27.89 ?  213 TYR D CZ    1 
ATOM   15094 O  OH    . TYR D 2 234 ? 136.349 98.845  159.763 1.00 32.34 ?  213 TYR D OH    1 
ATOM   15095 N  N     . ASN D 2 235 ? 130.411 96.182  156.971 1.00 25.43 ?  214 ASN D N     1 
ATOM   15096 C  CA    . ASN D 2 235 ? 129.439 96.885  157.825 1.00 26.77 ?  214 ASN D CA    1 
ATOM   15097 C  C     . ASN D 2 235 ? 128.507 95.958  158.605 1.00 27.06 ?  214 ASN D C     1 
ATOM   15098 O  O     . ASN D 2 235 ? 127.809 96.396  159.515 1.00 27.42 ?  214 ASN D O     1 
ATOM   15099 C  CB    . ASN D 2 235 ? 128.591 97.863  157.009 1.00 26.80 ?  214 ASN D CB    1 
ATOM   15100 C  CG    . ASN D 2 235 ? 129.404 98.971  156.396 1.00 28.19 ?  214 ASN D CG    1 
ATOM   15101 O  OD1   . ASN D 2 235 ? 130.385 99.437  156.971 1.00 29.35 ?  214 ASN D OD1   1 
ATOM   15102 N  ND2   . ASN D 2 235 ? 128.992 99.410  155.218 1.00 30.84 ?  214 ASN D ND2   1 
ATOM   15103 N  N     . LYS D 2 236 ? 128.498 94.684  158.244 1.00 26.87 ?  215 LYS D N     1 
ATOM   15104 C  CA    . LYS D 2 236 ? 127.694 93.699  158.956 1.00 27.86 ?  215 LYS D CA    1 
ATOM   15105 C  C     . LYS D 2 236 ? 128.462 93.092  160.138 1.00 28.07 ?  215 LYS D C     1 
ATOM   15106 O  O     . LYS D 2 236 ? 127.919 92.277  160.883 1.00 28.22 ?  215 LYS D O     1 
ATOM   15107 C  CB    . LYS D 2 236 ? 127.223 92.601  158.001 1.00 27.52 ?  215 LYS D CB    1 
ATOM   15108 C  CG    . LYS D 2 236 ? 126.285 93.080  156.921 1.00 29.60 ?  215 LYS D CG    1 
ATOM   15109 C  CD    . LYS D 2 236 ? 125.386 91.962  156.416 1.00 34.24 ?  215 LYS D CD    1 
ATOM   15110 C  CE    . LYS D 2 236 ? 125.867 91.342  155.119 1.00 36.75 ?  215 LYS D CE    1 
ATOM   15111 N  NZ    . LYS D 2 236 ? 127.156 90.639  155.291 1.00 40.41 1  215 LYS D NZ    1 
ATOM   15112 N  N     . GLN D 2 237 ? 129.717 93.499  160.309 1.00 28.33 ?  216 GLN D N     1 
ATOM   15113 C  CA    . GLN D 2 237 ? 130.593 92.890  161.312 1.00 29.60 ?  216 GLN D CA    1 
ATOM   15114 C  C     . GLN D 2 237 ? 130.617 93.667  162.623 1.00 30.69 ?  216 GLN D C     1 
ATOM   15115 O  O     . GLN D 2 237 ? 130.292 94.859  162.655 1.00 30.85 ?  216 GLN D O     1 
ATOM   15116 C  CB    . GLN D 2 237 ? 132.034 92.746  160.777 1.00 29.08 ?  216 GLN D CB    1 
ATOM   15117 C  CG    . GLN D 2 237 ? 132.173 92.030  159.430 1.00 27.78 ?  216 GLN D CG    1 
ATOM   15118 C  CD    . GLN D 2 237 ? 131.428 90.706  159.369 1.00 28.38 ?  216 GLN D CD    1 
ATOM   15119 O  OE1   . GLN D 2 237 ? 131.577 89.855  160.244 1.00 29.30 ?  216 GLN D OE1   1 
ATOM   15120 N  NE2   . GLN D 2 237 ? 130.627 90.524  158.323 1.00 26.88 ?  216 GLN D NE2   1 
ATOM   15121 N  N     . THR D 2 238 ? 131.017 92.985  163.695 1.00 32.02 ?  217 THR D N     1 
ATOM   15122 C  CA    . THR D 2 238 ? 131.255 93.629  164.991 1.00 33.47 ?  217 THR D CA    1 
ATOM   15123 C  C     . THR D 2 238 ? 132.442 94.596  164.917 1.00 34.29 ?  217 THR D C     1 
ATOM   15124 O  O     . THR D 2 238 ? 133.192 94.614  163.927 1.00 33.78 ?  217 THR D O     1 
ATOM   15125 C  CB    . THR D 2 238 ? 131.528 92.580  166.105 1.00 34.00 ?  217 THR D CB    1 
ATOM   15126 O  OG1   . THR D 2 238 ? 132.760 91.894  165.833 1.00 34.33 ?  217 THR D OG1   1 
ATOM   15127 C  CG2   . THR D 2 238 ? 130.382 91.559  166.193 1.00 33.53 ?  217 THR D CG2   1 
ATOM   15128 N  N     . GLU D 2 239 ? 132.626 95.390  165.966 1.00 35.45 ?  218 GLU D N     1 
ATOM   15129 C  CA    . GLU D 2 239 ? 133.739 96.333  166.006 1.00 36.37 ?  218 GLU D CA    1 
ATOM   15130 C  C     . GLU D 2 239 ? 135.097 95.637  166.056 1.00 36.29 ?  218 GLU D C     1 
ATOM   15131 O  O     . GLU D 2 239 ? 136.044 96.077  165.397 1.00 36.18 ?  218 GLU D O     1 
ATOM   15132 C  CB    . GLU D 2 239 ? 133.580 97.335  167.153 1.00 37.27 ?  218 GLU D CB    1 
ATOM   15133 C  CG    . GLU D 2 239 ? 132.429 98.335  166.938 1.00 39.45 ?  218 GLU D CG    1 
ATOM   15134 C  CD    . GLU D 2 239 ? 132.546 99.121  165.634 1.00 41.22 ?  218 GLU D CD    1 
ATOM   15135 O  OE1   . GLU D 2 239 ? 133.647 99.629  165.326 1.00 42.62 ?  218 GLU D OE1   1 
ATOM   15136 O  OE2   . GLU D 2 239 ? 131.532 99.232  164.912 1.00 41.24 -1 218 GLU D OE2   1 
ATOM   15137 N  N     . GLU D 2 240 ? 135.186 94.546  166.815 1.00 36.66 ?  219 GLU D N     1 
ATOM   15138 C  CA    . GLU D 2 240 ? 136.428 93.775  166.898 1.00 37.01 ?  219 GLU D CA    1 
ATOM   15139 C  C     . GLU D 2 240 ? 136.750 93.110  165.560 1.00 35.85 ?  219 GLU D C     1 
ATOM   15140 O  O     . GLU D 2 240 ? 137.908 93.103  165.133 1.00 35.62 ?  219 GLU D O     1 
ATOM   15141 C  CB    . GLU D 2 240 ? 136.371 92.724  168.017 1.00 37.98 ?  219 GLU D CB    1 
ATOM   15142 C  CG    . GLU D 2 240 ? 137.696 91.968  168.202 1.00 40.87 ?  219 GLU D CG    1 
ATOM   15143 C  CD    . GLU D 2 240 ? 137.668 90.906  169.300 1.00 44.58 ?  219 GLU D CD    1 
ATOM   15144 O  OE1   . GLU D 2 240 ? 138.756 90.608  169.850 1.00 45.86 ?  219 GLU D OE1   1 
ATOM   15145 O  OE2   . GLU D 2 240 ? 136.577 90.368  169.610 1.00 45.75 -1 219 GLU D OE2   1 
ATOM   15146 N  N     . LYS D 2 241 ? 135.724 92.554  164.916 1.00 34.54 ?  220 LYS D N     1 
ATOM   15147 C  CA    . LYS D 2 241 ? 135.877 91.910  163.610 1.00 33.65 ?  220 LYS D CA    1 
ATOM   15148 C  C     . LYS D 2 241 ? 136.261 92.934  162.533 1.00 32.67 ?  220 LYS D C     1 
ATOM   15149 O  O     . LYS D 2 241 ? 137.076 92.632  161.667 1.00 32.05 ?  220 LYS D O     1 
ATOM   15150 C  CB    . LYS D 2 241 ? 134.608 91.145  163.220 1.00 33.30 ?  220 LYS D CB    1 
ATOM   15151 C  CG    . LYS D 2 241 ? 134.710 90.298  161.937 1.00 34.50 ?  220 LYS D CG    1 
ATOM   15152 C  CD    . LYS D 2 241 ? 135.784 89.206  162.022 1.00 36.30 ?  220 LYS D CD    1 
ATOM   15153 C  CE    . LYS D 2 241 ? 135.383 88.089  162.978 1.00 38.44 ?  220 LYS D CE    1 
ATOM   15154 N  NZ    . LYS D 2 241 ? 136.576 87.355  163.480 1.00 39.28 1  220 LYS D NZ    1 
ATOM   15155 N  N     . LYS D 2 242 ? 135.674 94.132  162.602 1.00 31.90 ?  221 LYS D N     1 
ATOM   15156 C  CA    . LYS D 2 242 ? 136.032 95.229  161.702 1.00 31.28 ?  221 LYS D CA    1 
ATOM   15157 C  C     . LYS D 2 242 ? 137.512 95.589  161.820 1.00 31.32 ?  221 LYS D C     1 
ATOM   15158 O  O     . LYS D 2 242 ? 138.202 95.674  160.812 1.00 30.72 ?  221 LYS D O     1 
ATOM   15159 C  CB    . LYS D 2 242 ? 135.173 96.475  161.962 1.00 31.38 ?  221 LYS D CB    1 
ATOM   15160 C  CG    . LYS D 2 242 ? 133.798 96.452  161.302 1.00 30.64 ?  221 LYS D CG    1 
ATOM   15161 C  CD    . LYS D 2 242 ? 133.037 97.739  161.617 1.00 32.51 ?  221 LYS D CD    1 
ATOM   15162 C  CE    . LYS D 2 242 ? 131.681 97.749  160.946 1.00 32.66 ?  221 LYS D CE    1 
ATOM   15163 N  NZ    . LYS D 2 242 ? 130.855 98.872  161.441 1.00 35.31 1  221 LYS D NZ    1 
ATOM   15164 N  N     . ALA D 2 243 ? 137.986 95.803  163.051 1.00 31.62 ?  222 ALA D N     1 
ATOM   15165 C  CA    . ALA D 2 243 ? 139.397 96.113  163.305 1.00 31.66 ?  222 ALA D CA    1 
ATOM   15166 C  C     . ALA D 2 243 ? 140.332 95.033  162.746 1.00 31.52 ?  222 ALA D C     1 
ATOM   15167 O  O     . ALA D 2 243 ? 141.420 95.332  162.247 1.00 31.41 ?  222 ALA D O     1 
ATOM   15168 C  CB    . ALA D 2 243 ? 139.638 96.322  164.805 1.00 31.89 ?  222 ALA D CB    1 
ATOM   15169 N  N     . GLU D 2 244 ? 139.876 93.786  162.819 1.00 31.35 ?  223 GLU D N     1 
ATOM   15170 C  CA    . GLU D 2 244 ? 140.602 92.628  162.325 1.00 31.54 ?  223 GLU D CA    1 
ATOM   15171 C  C     . GLU D 2 244 ? 140.646 92.597  160.780 1.00 30.63 ?  223 GLU D C     1 
ATOM   15172 O  O     . GLU D 2 244 ? 141.675 92.262  160.176 1.00 29.47 ?  223 GLU D O     1 
ATOM   15173 C  CB    . GLU D 2 244 ? 139.918 91.388  162.878 1.00 32.45 ?  223 GLU D CB    1 
ATOM   15174 C  CG    . GLU D 2 244 ? 140.661 90.093  162.757 1.00 35.31 ?  223 GLU D CG    1 
ATOM   15175 C  CD    . GLU D 2 244 ? 140.027 89.021  163.620 1.00 38.36 ?  223 GLU D CD    1 
ATOM   15176 O  OE1   . GLU D 2 244 ? 140.098 89.134  164.861 1.00 41.93 ?  223 GLU D OE1   1 
ATOM   15177 O  OE2   . GLU D 2 244 ? 139.445 88.068  163.063 1.00 39.37 -1 223 GLU D OE2   1 
ATOM   15178 N  N     . LEU D 2 245 ? 139.527 92.954  160.158 1.00 29.62 ?  224 LEU D N     1 
ATOM   15179 C  CA    . LEU D 2 245 ? 139.451 93.077  158.705 1.00 29.44 ?  224 LEU D CA    1 
ATOM   15180 C  C     . LEU D 2 245 ? 140.266 94.259  158.175 1.00 28.99 ?  224 LEU D C     1 
ATOM   15181 O  O     . LEU D 2 245 ? 140.846 94.166  157.097 1.00 28.63 ?  224 LEU D O     1 
ATOM   15182 C  CB    . LEU D 2 245 ? 137.992 93.174  158.246 1.00 29.06 ?  224 LEU D CB    1 
ATOM   15183 C  CG    . LEU D 2 245 ? 137.133 91.918  158.431 1.00 29.27 ?  224 LEU D CG    1 
ATOM   15184 C  CD1   . LEU D 2 245 ? 135.735 92.174  157.876 1.00 30.76 ?  224 LEU D CD1   1 
ATOM   15185 C  CD2   . LEU D 2 245 ? 137.750 90.698  157.755 1.00 28.11 ?  224 LEU D CD2   1 
ATOM   15186 N  N     . ARG D 2 246 ? 140.306 95.358  158.931 1.00 29.31 ?  225 ARG D N     1 
ATOM   15187 C  CA    . ARG D 2 246 ? 141.158 96.501  158.586 1.00 29.86 ?  225 ARG D CA    1 
ATOM   15188 C  C     . ARG D 2 246 ? 142.630 96.116  158.619 1.00 29.23 ?  225 ARG D C     1 
ATOM   15189 O  O     . ARG D 2 246 ? 143.385 96.472  157.725 1.00 28.95 ?  225 ARG D O     1 
ATOM   15190 C  CB    . ARG D 2 246 ? 140.943 97.689  159.531 1.00 30.56 ?  225 ARG D CB    1 
ATOM   15191 C  CG    . ARG D 2 246 ? 139.680 98.478  159.277 1.00 33.71 ?  225 ARG D CG    1 
ATOM   15192 C  CD    . ARG D 2 246 ? 139.762 99.911  159.837 1.00 37.42 ?  225 ARG D CD    1 
ATOM   15193 N  NE    . ARG D 2 246 ? 140.081 99.964  161.268 1.00 39.17 ?  225 ARG D NE    1 
ATOM   15194 C  CZ    . ARG D 2 246 ? 139.218 99.742  162.261 1.00 40.68 ?  225 ARG D CZ    1 
ATOM   15195 N  NH1   . ARG D 2 246 ? 137.950 99.430  162.010 1.00 40.28 1  225 ARG D NH1   1 
ATOM   15196 N  NH2   . ARG D 2 246 ? 139.634 99.824  163.521 1.00 41.65 ?  225 ARG D NH2   1 
ATOM   15197 N  N     . GLU D 2 247 ? 143.030 95.404  159.666 1.00 28.89 ?  226 GLU D N     1 
ATOM   15198 C  CA    . GLU D 2 247 ? 144.404 94.924  159.783 1.00 29.27 ?  226 GLU D CA    1 
ATOM   15199 C  C     . GLU D 2 247 ? 144.756 94.001  158.616 1.00 27.84 ?  226 GLU D C     1 
ATOM   15200 O  O     . GLU D 2 247 ? 145.845 94.122  158.050 1.00 27.37 ?  226 GLU D O     1 
ATOM   15201 C  CB    . GLU D 2 247 ? 144.642 94.229  161.135 1.00 30.21 ?  226 GLU D CB    1 
ATOM   15202 C  CG    . GLU D 2 247 ? 146.034 93.585  161.296 1.00 34.46 ?  226 GLU D CG    1 
ATOM   15203 C  CD    . GLU D 2 247 ? 147.177 94.587  161.154 1.00 40.77 ?  226 GLU D CD    1 
ATOM   15204 O  OE1   . GLU D 2 247 ? 147.260 95.518  161.989 1.00 44.03 ?  226 GLU D OE1   1 
ATOM   15205 O  OE2   . GLU D 2 247 ? 147.994 94.449  160.208 1.00 42.98 -1 226 GLU D OE2   1 
ATOM   15206 N  N     . PHE D 2 248 ? 143.836 93.102  158.255 1.00 26.73 ?  227 PHE D N     1 
ATOM   15207 C  CA    . PHE D 2 248 ? 144.012 92.239  157.080 1.00 26.15 ?  227 PHE D CA    1 
ATOM   15208 C  C     . PHE D 2 248 ? 144.277 93.058  155.814 1.00 25.33 ?  227 PHE D C     1 
ATOM   15209 O  O     . PHE D 2 248 ? 145.219 92.770  155.080 1.00 24.70 ?  227 PHE D O     1 
ATOM   15210 C  CB    . PHE D 2 248 ? 142.812 91.306  156.829 1.00 26.02 ?  227 PHE D CB    1 
ATOM   15211 C  CG    . PHE D 2 248 ? 142.805 90.691  155.430 1.00 25.61 ?  227 PHE D CG    1 
ATOM   15212 C  CD1   . PHE D 2 248 ? 143.512 89.522  155.164 1.00 26.51 ?  227 PHE D CD1   1 
ATOM   15213 C  CD2   . PHE D 2 248 ? 142.123 91.310  154.379 1.00 26.21 ?  227 PHE D CD2   1 
ATOM   15214 C  CE1   . PHE D 2 248 ? 143.535 88.966  153.884 1.00 26.16 ?  227 PHE D CE1   1 
ATOM   15215 C  CE2   . PHE D 2 248 ? 142.138 90.765  153.088 1.00 26.07 ?  227 PHE D CE2   1 
ATOM   15216 C  CZ    . PHE D 2 248 ? 142.852 89.588  152.844 1.00 25.82 ?  227 PHE D CZ    1 
ATOM   15217 N  N     . ALA D 2 249 ? 143.428 94.057  155.566 1.00 24.83 ?  228 ALA D N     1 
ATOM   15218 C  CA    . ALA D 2 249 ? 143.504 94.881  154.352 1.00 24.08 ?  228 ALA D CA    1 
ATOM   15219 C  C     . ALA D 2 249 ? 144.820 95.670  154.273 1.00 23.93 ?  228 ALA D C     1 
ATOM   15220 O  O     . ALA D 2 249 ? 145.447 95.737  153.214 1.00 22.51 ?  228 ALA D O     1 
ATOM   15221 C  CB    . ALA D 2 249 ? 142.309 95.839  154.294 1.00 24.18 ?  228 ALA D CB    1 
ATOM   15222 N  N     . ILE D 2 250 ? 145.223 96.265  155.395 1.00 24.20 ?  229 ILE D N     1 
ATOM   15223 C  CA    . ILE D 2 250 ? 146.458 97.049  155.451 1.00 24.86 ?  229 ILE D CA    1 
ATOM   15224 C  C     . ILE D 2 250 ? 147.687 96.145  155.308 1.00 24.68 ?  229 ILE D C     1 
ATOM   15225 O  O     . ILE D 2 250 ? 148.626 96.484  154.597 1.00 24.30 ?  229 ILE D O     1 
ATOM   15226 C  CB    . ILE D 2 250 ? 146.539 97.933  156.745 1.00 25.44 ?  229 ILE D CB    1 
ATOM   15227 C  CG1   . ILE D 2 250 ? 145.352 98.911  156.844 1.00 26.49 ?  229 ILE D CG1   1 
ATOM   15228 C  CG2   . ILE D 2 250 ? 147.871 98.691  156.830 1.00 27.13 ?  229 ILE D CG2   1 
ATOM   15229 C  CD1   . ILE D 2 250 ? 145.125 99.805  155.623 1.00 28.58 ?  229 ILE D CD1   1 
ATOM   15230 N  N     . ASP D 2 251 ? 147.671 94.993  155.981 1.00 24.90 ?  230 ASP D N     1 
ATOM   15231 C  CA    . ASP D 2 251 ? 148.753 94.020  155.885 1.00 25.04 ?  230 ASP D CA    1 
ATOM   15232 C  C     . ASP D 2 251 ? 148.917 93.523  154.437 1.00 24.25 ?  230 ASP D C     1 
ATOM   15233 O  O     . ASP D 2 251 ? 150.033 93.472  153.914 1.00 23.60 ?  230 ASP D O     1 
ATOM   15234 C  CB    . ASP D 2 251 ? 148.487 92.851  156.839 1.00 26.23 ?  230 ASP D CB    1 
ATOM   15235 C  CG    . ASP D 2 251 ? 149.500 91.735  156.704 1.00 28.91 ?  230 ASP D CG    1 
ATOM   15236 O  OD1   . ASP D 2 251 ? 150.680 91.933  157.061 1.00 32.03 ?  230 ASP D OD1   1 
ATOM   15237 O  OD2   . ASP D 2 251 ? 149.103 90.640  156.259 1.00 33.16 -1 230 ASP D OD2   1 
ATOM   15238 N  N     . LEU D 2 252 ? 147.805 93.153  153.806 1.00 23.43 ?  231 LEU D N     1 
ATOM   15239 C  CA    . LEU D 2 252 ? 147.820 92.745  152.404 1.00 22.79 ?  231 LEU D CA    1 
ATOM   15240 C  C     . LEU D 2 252 ? 148.354 93.867  151.507 1.00 22.71 ?  231 LEU D C     1 
ATOM   15241 O  O     . LEU D 2 252 ? 149.191 93.623  150.630 1.00 21.58 ?  231 LEU D O     1 
ATOM   15242 C  CB    . LEU D 2 252 ? 146.423 92.322  151.937 1.00 22.48 ?  231 LEU D CB    1 
ATOM   15243 C  CG    . LEU D 2 252 ? 146.322 91.866  150.469 1.00 21.05 ?  231 LEU D CG    1 
ATOM   15244 C  CD1   . LEU D 2 252 ? 147.264 90.680  150.168 1.00 22.94 ?  231 LEU D CD1   1 
ATOM   15245 C  CD2   . LEU D 2 252 ? 144.890 91.494  150.111 1.00 19.31 ?  231 LEU D CD2   1 
ATOM   15246 N  N     . LEU D 2 253 ? 147.863 95.087  151.729 1.00 22.90 ?  232 LEU D N     1 
ATOM   15247 C  CA    . LEU D 2 253 ? 148.322 96.238  150.936 1.00 23.78 ?  232 LEU D CA    1 
ATOM   15248 C  C     . LEU D 2 253 ? 149.841 96.412  151.048 1.00 23.75 ?  232 LEU D C     1 
ATOM   15249 O  O     . LEU D 2 253 ? 150.521 96.616  150.042 1.00 23.26 ?  232 LEU D O     1 
ATOM   15250 C  CB    . LEU D 2 253 ? 147.626 97.529  151.372 1.00 24.03 ?  232 LEU D CB    1 
ATOM   15251 C  CG    . LEU D 2 253 ? 148.215 98.812  150.757 1.00 26.46 ?  232 LEU D CG    1 
ATOM   15252 C  CD1   . LEU D 2 253 ? 147.855 98.900  149.293 1.00 26.52 ?  232 LEU D CD1   1 
ATOM   15253 C  CD2   . LEU D 2 253 ? 147.741 100.067 151.494 1.00 27.50 ?  232 LEU D CD2   1 
ATOM   15254 N  N     . ASN D 2 254 ? 150.350 96.355  152.280 1.00 24.63 ?  233 ASN D N     1 
ATOM   15255 C  CA    . ASN D 2 254 ? 151.790 96.439  152.537 1.00 25.49 ?  233 ASN D CA    1 
ATOM   15256 C  C     . ASN D 2 254 ? 152.615 95.386  151.782 1.00 24.94 ?  233 ASN D C     1 
ATOM   15257 O  O     . ASN D 2 254 ? 153.654 95.719  151.206 1.00 24.64 ?  233 ASN D O     1 
ATOM   15258 C  CB    . ASN D 2 254 ? 152.083 96.339  154.031 1.00 26.98 ?  233 ASN D CB    1 
ATOM   15259 C  CG    . ASN D 2 254 ? 151.994 97.677  154.731 1.00 29.94 ?  233 ASN D CG    1 
ATOM   15260 O  OD1   . ASN D 2 254 ? 152.432 98.707  154.202 1.00 34.55 ?  233 ASN D OD1   1 
ATOM   15261 N  ND2   . ASN D 2 254 ? 151.439 97.673  155.935 1.00 33.81 ?  233 ASN D ND2   1 
ATOM   15262 N  N     . GLN D 2 255 ? 152.160 94.132  151.800 1.00 24.08 ?  234 GLN D N     1 
ATOM   15263 C  CA    . GLN D 2 255 ? 152.870 93.057  151.103 1.00 24.35 ?  234 GLN D CA    1 
ATOM   15264 C  C     . GLN D 2 255 ? 152.911 93.339  149.613 1.00 23.26 ?  234 GLN D C     1 
ATOM   15265 O  O     . GLN D 2 255 ? 153.977 93.242  148.995 1.00 23.12 ?  234 GLN D O     1 
ATOM   15266 C  CB    . GLN D 2 255 ? 152.214 91.688  151.323 1.00 24.84 ?  234 GLN D CB    1 
ATOM   15267 C  CG    . GLN D 2 255 ? 152.383 91.086  152.700 1.00 27.45 ?  234 GLN D CG    1 
ATOM   15268 C  CD    . GLN D 2 255 ? 153.837 90.952  153.118 1.00 32.02 ?  234 GLN D CD    1 
ATOM   15269 O  OE1   . GLN D 2 255 ? 154.254 91.550  154.108 1.00 35.80 ?  234 GLN D OE1   1 
ATOM   15270 N  NE2   . GLN D 2 255 ? 154.614 90.165  152.372 1.00 32.12 ?  234 GLN D NE2   1 
ATOM   15271 N  N     . LEU D 2 256 ? 151.753 93.690  149.050 1.00 21.77 ?  235 LEU D N     1 
ATOM   15272 C  CA    . LEU D 2 256 ? 151.647 93.975  147.617 1.00 21.68 ?  235 LEU D CA    1 
ATOM   15273 C  C     . LEU D 2 256 ? 152.455 95.213  147.244 1.00 21.49 ?  235 LEU D C     1 
ATOM   15274 O  O     . LEU D 2 256 ? 153.123 95.231  146.215 1.00 20.89 ?  235 LEU D O     1 
ATOM   15275 C  CB    . LEU D 2 256 ? 150.180 94.158  147.180 1.00 20.49 ?  235 LEU D CB    1 
ATOM   15276 C  CG    . LEU D 2 256 ? 149.286 92.911  147.224 1.00 21.52 ?  235 LEU D CG    1 
ATOM   15277 C  CD1   . LEU D 2 256 ? 147.807 93.259  146.986 1.00 20.71 ?  235 LEU D CD1   1 
ATOM   15278 C  CD2   . LEU D 2 256 ? 149.739 91.858  146.222 1.00 20.74 ?  235 LEU D CD2   1 
ATOM   15279 N  N     . TYR D 2 257 ? 152.394 96.239  148.091 1.00 21.42 ?  236 TYR D N     1 
ATOM   15280 C  CA    . TYR D 2 257 ? 153.122 97.479  147.826 1.00 22.02 ?  236 TYR D CA    1 
ATOM   15281 C  C     . TYR D 2 257 ? 154.636 97.273  147.788 1.00 22.61 ?  236 TYR D C     1 
ATOM   15282 O  O     . TYR D 2 257 ? 155.315 97.797  146.904 1.00 22.19 ?  236 TYR D O     1 
ATOM   15283 C  CB    . TYR D 2 257 ? 152.746 98.564  148.829 1.00 22.06 ?  236 TYR D CB    1 
ATOM   15284 C  CG    . TYR D 2 257 ? 153.578 99.822  148.714 1.00 23.44 ?  236 TYR D CG    1 
ATOM   15285 C  CD1   . TYR D 2 257 ? 153.487 100.645 147.585 1.00 24.01 ?  236 TYR D CD1   1 
ATOM   15286 C  CD2   . TYR D 2 257 ? 154.448 100.192 149.736 1.00 25.22 ?  236 TYR D CD2   1 
ATOM   15287 C  CE1   . TYR D 2 257 ? 154.251 101.806 147.482 1.00 25.14 ?  236 TYR D CE1   1 
ATOM   15288 C  CE2   . TYR D 2 257 ? 155.223 101.345 149.639 1.00 26.71 ?  236 TYR D CE2   1 
ATOM   15289 C  CZ    . TYR D 2 257 ? 155.116 102.145 148.516 1.00 25.35 ?  236 TYR D CZ    1 
ATOM   15290 O  OH    . TYR D 2 257 ? 155.876 103.283 148.439 1.00 26.77 ?  236 TYR D OH    1 
ATOM   15291 N  N     . GLU D 2 258 ? 155.166 96.502  148.734 1.00 23.09 ?  237 GLU D N     1 
ATOM   15292 C  CA    . GLU D 2 258 ? 156.612 96.275  148.768 1.00 23.98 ?  237 GLU D CA    1 
ATOM   15293 C  C     . GLU D 2 258 ? 157.088 95.491  147.545 1.00 23.13 ?  237 GLU D C     1 
ATOM   15294 O  O     . GLU D 2 258 ? 158.146 95.783  146.995 1.00 23.02 ?  237 GLU D O     1 
ATOM   15295 C  CB    . GLU D 2 258 ? 157.050 95.614  150.084 1.00 25.20 ?  237 GLU D CB    1 
ATOM   15296 C  CG    . GLU D 2 258 ? 156.847 96.509  151.318 1.00 28.82 ?  237 GLU D CG    1 
ATOM   15297 C  CD    . GLU D 2 258 ? 157.803 97.708  151.393 1.00 34.48 ?  237 GLU D CD    1 
ATOM   15298 O  OE1   . GLU D 2 258 ? 158.947 97.629  150.872 1.00 37.75 ?  237 GLU D OE1   1 
ATOM   15299 O  OE2   . GLU D 2 258 ? 157.413 98.740  151.993 1.00 37.16 -1 237 GLU D OE2   1 
ATOM   15300 N  N     . ASN D 2 259 ? 156.289 94.526  147.108 1.00 22.12 ?  238 ASN D N     1 
ATOM   15301 C  CA    . ASN D 2 259 ? 156.554 93.816  145.856 1.00 22.35 ?  238 ASN D CA    1 
ATOM   15302 C  C     . ASN D 2 259 ? 156.408 94.710  144.595 1.00 22.11 ?  238 ASN D C     1 
ATOM   15303 O  O     . ASN D 2 259 ? 157.175 94.560  143.641 1.00 22.24 ?  238 ASN D O     1 
ATOM   15304 C  CB    . ASN D 2 259 ? 155.671 92.566  145.753 1.00 21.69 ?  238 ASN D CB    1 
ATOM   15305 C  CG    . ASN D 2 259 ? 155.942 91.764  144.493 1.00 23.38 ?  238 ASN D CG    1 
ATOM   15306 O  OD1   . ASN D 2 259 ? 156.982 91.099  144.369 1.00 23.95 ?  238 ASN D OD1   1 
ATOM   15307 N  ND2   . ASN D 2 259 ? 155.017 91.830  143.545 1.00 21.14 ?  238 ASN D ND2   1 
ATOM   15308 N  N     . GLU D 2 260 ? 155.437 95.629  144.602 1.00 21.95 ?  239 GLU D N     1 
ATOM   15309 C  CA    . GLU D 2 260 ? 155.269 96.609  143.509 1.00 22.50 ?  239 GLU D CA    1 
ATOM   15310 C  C     . GLU D 2 260 ? 156.496 97.502  143.337 1.00 22.03 ?  239 GLU D C     1 
ATOM   15311 O  O     . GLU D 2 260 ? 156.853 97.862  142.219 1.00 22.03 ?  239 GLU D O     1 
ATOM   15312 C  CB    . GLU D 2 260 ? 154.054 97.528  143.736 1.00 22.90 ?  239 GLU D CB    1 
ATOM   15313 C  CG    . GLU D 2 260 ? 152.690 96.973  143.298 1.00 25.84 ?  239 GLU D CG    1 
ATOM   15314 C  CD    . GLU D 2 260 ? 152.685 96.374  141.895 1.00 28.59 ?  239 GLU D CD    1 
ATOM   15315 O  OE1   . GLU D 2 260 ? 153.129 95.217  141.744 1.00 28.18 ?  239 GLU D OE1   1 
ATOM   15316 O  OE2   . GLU D 2 260 ? 152.201 97.043  140.952 1.00 30.32 -1 239 GLU D OE2   1 
ATOM   15317 N  N     . LEU D 2 261 ? 157.115 97.886  144.448 1.00 21.50 ?  240 LEU D N     1 
ATOM   15318 C  CA    . LEU D 2 261 ? 158.315 98.716  144.388 1.00 22.03 ?  240 LEU D CA    1 
ATOM   15319 C  C     . LEU D 2 261 ? 159.427 97.964  143.679 1.00 21.52 ?  240 LEU D C     1 
ATOM   15320 O  O     . LEU D 2 261 ? 160.110 98.533  142.826 1.00 21.44 ?  240 LEU D O     1 
ATOM   15321 C  CB    . LEU D 2 261 ? 158.771 99.153  145.778 1.00 21.57 ?  240 LEU D CB    1 
ATOM   15322 C  CG    . LEU D 2 261 ? 157.813 100.005 146.612 1.00 23.22 ?  240 LEU D CG    1 
ATOM   15323 C  CD1   . LEU D 2 261 ? 158.453 100.294 147.957 1.00 23.06 ?  240 LEU D CD1   1 
ATOM   15324 C  CD2   . LEU D 2 261 ? 157.454 101.304 145.892 1.00 23.52 ?  240 LEU D CD2   1 
ATOM   15325 N  N     . GLU D 2 262 ? 159.587 96.685  144.017 1.00 21.69 ?  241 GLU D N     1 
ATOM   15326 C  CA    . GLU D 2 262 ? 160.589 95.833  143.356 1.00 22.31 ?  241 GLU D CA    1 
ATOM   15327 C  C     . GLU D 2 262 ? 160.243 95.586  141.886 1.00 21.69 ?  241 GLU D C     1 
ATOM   15328 O  O     . GLU D 2 262 ? 161.115 95.644  141.014 1.00 21.75 ?  241 GLU D O     1 
ATOM   15329 C  CB    . GLU D 2 262 ? 160.737 94.491  144.080 1.00 22.46 ?  241 GLU D CB    1 
ATOM   15330 C  CG    . GLU D 2 262 ? 161.213 94.567  145.532 1.00 25.63 ?  241 GLU D CG    1 
ATOM   15331 C  CD    . GLU D 2 262 ? 161.419 93.177  146.118 1.00 29.83 ?  241 GLU D CD    1 
ATOM   15332 O  OE1   . GLU D 2 262 ? 160.421 92.533  146.507 1.00 33.22 ?  241 GLU D OE1   1 
ATOM   15333 O  OE2   . GLU D 2 262 ? 162.571 92.711  146.164 1.00 33.36 -1 241 GLU D OE2   1 
ATOM   15334 N  N     . TYR D 2 263 ? 158.973 95.288  141.619 1.00 21.42 ?  242 TYR D N     1 
ATOM   15335 C  CA    . TYR D 2 263 ? 158.468 95.109  140.252 1.00 21.04 ?  242 TYR D CA    1 
ATOM   15336 C  C     . TYR D 2 263 ? 158.770 96.356  139.412 1.00 21.15 ?  242 TYR D C     1 
ATOM   15337 O  O     . TYR D 2 263 ? 159.185 96.259  138.256 1.00 20.32 ?  242 TYR D O     1 
ATOM   15338 C  CB    . TYR D 2 263 ? 156.952 94.855  140.297 1.00 20.95 ?  242 TYR D CB    1 
ATOM   15339 C  CG    . TYR D 2 263 ? 156.262 94.748  138.950 1.00 21.86 ?  242 TYR D CG    1 
ATOM   15340 C  CD1   . TYR D 2 263 ? 156.306 93.562  138.216 1.00 23.53 ?  242 TYR D CD1   1 
ATOM   15341 C  CD2   . TYR D 2 263 ? 155.564 95.833  138.408 1.00 21.20 ?  242 TYR D CD2   1 
ATOM   15342 C  CE1   . TYR D 2 263 ? 155.674 93.458  136.985 1.00 23.34 ?  242 TYR D CE1   1 
ATOM   15343 C  CE2   . TYR D 2 263 ? 154.929 95.735  137.175 1.00 23.11 ?  242 TYR D CE2   1 
ATOM   15344 C  CZ    . TYR D 2 263 ? 154.995 94.546  136.468 1.00 23.27 ?  242 TYR D CZ    1 
ATOM   15345 O  OH    . TYR D 2 263 ? 154.366 94.444  135.245 1.00 27.07 ?  242 TYR D OH    1 
ATOM   15346 N  N     . THR D 2 264 ? 158.536 97.520  140.016 1.00 21.12 ?  243 THR D N     1 
ATOM   15347 C  CA    . THR D 2 264 ? 158.706 98.812  139.360 1.00 21.98 ?  243 THR D CA    1 
ATOM   15348 C  C     . THR D 2 264 ? 160.164 99.059  138.978 1.00 22.32 ?  243 THR D C     1 
ATOM   15349 O  O     . THR D 2 264 ? 160.453 99.373  137.825 1.00 21.78 ?  243 THR D O     1 
ATOM   15350 C  CB    . THR D 2 264 ? 158.150 99.955  140.238 1.00 21.68 ?  243 THR D CB    1 
ATOM   15351 O  OG1   . THR D 2 264 ? 156.733 99.801  140.355 1.00 23.29 ?  243 THR D OG1   1 
ATOM   15352 C  CG2   . THR D 2 264 ? 158.468 101.346 139.654 1.00 23.16 ?  243 THR D CG2   1 
ATOM   15353 N  N     . GLU D 2 265 ? 161.077 98.892  139.934 1.00 22.48 ?  244 GLU D N     1 
ATOM   15354 C  CA    . GLU D 2 265 ? 162.500 99.080  139.641 1.00 23.73 ?  244 GLU D CA    1 
ATOM   15355 C  C     . GLU D 2 265 ? 162.982 98.112  138.571 1.00 23.85 ?  244 GLU D C     1 
ATOM   15356 O  O     . GLU D 2 265 ? 163.736 98.502  137.689 1.00 24.40 ?  244 GLU D O     1 
ATOM   15357 C  CB    . GLU D 2 265 ? 163.342 98.938  140.900 1.00 23.19 ?  244 GLU D CB    1 
ATOM   15358 C  CG    . GLU D 2 265 ? 163.199 100.129 141.810 1.00 25.08 ?  244 GLU D CG    1 
ATOM   15359 C  CD    . GLU D 2 265 ? 163.886 99.941  143.147 1.00 27.30 ?  244 GLU D CD    1 
ATOM   15360 O  OE1   . GLU D 2 265 ? 164.653 98.972  143.307 1.00 27.77 ?  244 GLU D OE1   1 
ATOM   15361 O  OE2   . GLU D 2 265 ? 163.653 100.778 144.038 1.00 28.63 -1 244 GLU D OE2   1 
ATOM   15362 N  N     . ASP D 2 266 ? 162.507 96.868  138.640 1.00 24.13 ?  245 ASP D N     1 
ATOM   15363 C  CA    . ASP D 2 266 ? 162.875 95.816  137.689 1.00 25.22 ?  245 ASP D CA    1 
ATOM   15364 C  C     . ASP D 2 266 ? 162.534 96.187  136.228 1.00 24.84 ?  245 ASP D C     1 
ATOM   15365 O  O     . ASP D 2 266 ? 163.292 95.861  135.309 1.00 25.64 ?  245 ASP D O     1 
ATOM   15366 C  CB    . ASP D 2 266 ? 162.192 94.501  138.098 1.00 25.79 ?  245 ASP D CB    1 
ATOM   15367 C  CG    . ASP D 2 266 ? 162.622 93.312  137.249 1.00 27.71 ?  245 ASP D CG    1 
ATOM   15368 O  OD1   . ASP D 2 266 ? 163.831 93.044  137.172 1.00 31.57 ?  245 ASP D OD1   1 
ATOM   15369 O  OD2   . ASP D 2 266 ? 161.748 92.626  136.677 1.00 30.29 -1 245 ASP D OD2   1 
ATOM   15370 N  N     . LEU D 2 267 ? 161.417 96.880  136.027 1.00 24.07 ?  246 LEU D N     1 
ATOM   15371 C  CA    . LEU D 2 267 ? 160.945 97.235  134.686 1.00 23.98 ?  246 LEU D CA    1 
ATOM   15372 C  C     . LEU D 2 267 ? 161.332 98.641  134.225 1.00 22.83 ?  246 LEU D C     1 
ATOM   15373 O  O     . LEU D 2 267 ? 161.654 98.840  133.047 1.00 23.00 ?  246 LEU D O     1 
ATOM   15374 C  CB    . LEU D 2 267 ? 159.416 97.091  134.592 1.00 23.82 ?  246 LEU D CB    1 
ATOM   15375 C  CG    . LEU D 2 267 ? 158.855 95.663  134.642 1.00 26.05 ?  246 LEU D CG    1 
ATOM   15376 C  CD1   . LEU D 2 267 ? 157.396 95.655  134.277 1.00 26.74 ?  246 LEU D CD1   1 
ATOM   15377 C  CD2   . LEU D 2 267 ? 159.617 94.728  133.722 1.00 28.00 ?  246 LEU D CD2   1 
ATOM   15378 N  N     . TYR D 2 268 ? 161.293 99.601  135.150 1.00 21.68 ?  247 TYR D N     1 
ATOM   15379 C  CA    . TYR D 2 268 ? 161.381 101.021 134.795 1.00 20.95 ?  247 TYR D CA    1 
ATOM   15380 C  C     . TYR D 2 268 ? 162.734 101.711 135.012 1.00 21.43 ?  247 TYR D C     1 
ATOM   15381 O  O     . TYR D 2 268 ? 162.949 102.793 134.468 1.00 20.73 ?  247 TYR D O     1 
ATOM   15382 C  CB    . TYR D 2 268 ? 160.289 101.826 135.505 1.00 20.27 ?  247 TYR D CB    1 
ATOM   15383 C  CG    . TYR D 2 268 ? 158.883 101.576 134.992 1.00 19.54 ?  247 TYR D CG    1 
ATOM   15384 C  CD1   . TYR D 2 268 ? 158.005 100.752 135.688 1.00 18.52 ?  247 TYR D CD1   1 
ATOM   15385 C  CD2   . TYR D 2 268 ? 158.436 102.166 133.800 1.00 20.62 ?  247 TYR D CD2   1 
ATOM   15386 C  CE1   . TYR D 2 268 ? 156.684 100.523 135.220 1.00 18.33 ?  247 TYR D CE1   1 
ATOM   15387 C  CE2   . TYR D 2 268 ? 157.124 101.945 133.322 1.00 20.79 ?  247 TYR D CE2   1 
ATOM   15388 C  CZ    . TYR D 2 268 ? 156.261 101.132 134.044 1.00 20.23 ?  247 TYR D CZ    1 
ATOM   15389 O  OH    . TYR D 2 268 ? 154.983 100.923 133.566 1.00 20.50 ?  247 TYR D OH    1 
ATOM   15390 N  N     . ASP D 2 269 ? 163.634 101.120 135.807 1.00 21.65 ?  248 ASP D N     1 
ATOM   15391 C  CA    . ASP D 2 269 ? 164.976 101.701 135.930 1.00 22.30 ?  248 ASP D CA    1 
ATOM   15392 C  C     . ASP D 2 269 ? 165.682 101.866 134.563 1.00 22.54 ?  248 ASP D C     1 
ATOM   15393 O  O     . ASP D 2 269 ? 166.366 102.868 134.339 1.00 22.49 ?  248 ASP D O     1 
ATOM   15394 C  CB    . ASP D 2 269 ? 165.856 100.908 136.897 1.00 22.83 ?  248 ASP D CB    1 
ATOM   15395 C  CG    . ASP D 2 269 ? 165.591 101.259 138.358 1.00 23.55 ?  248 ASP D CG    1 
ATOM   15396 O  OD1   . ASP D 2 269 ? 164.842 102.220 138.625 1.00 24.95 ?  248 ASP D OD1   1 
ATOM   15397 O  OD2   . ASP D 2 269 ? 166.137 100.566 139.246 1.00 24.47 -1 248 ASP D OD2   1 
ATOM   15398 N  N     . GLN D 2 270 ? 165.507 100.897 133.662 1.00 22.79 ?  249 GLN D N     1 
ATOM   15399 C  CA    . GLN D 2 270 ? 166.164 100.938 132.349 1.00 23.41 ?  249 GLN D CA    1 
ATOM   15400 C  C     . GLN D 2 270 ? 165.667 102.071 131.445 1.00 22.83 ?  249 GLN D C     1 
ATOM   15401 O  O     . GLN D 2 270 ? 166.317 102.399 130.455 1.00 23.75 ?  249 GLN D O     1 
ATOM   15402 C  CB    . GLN D 2 270 ? 166.064 99.594  131.622 1.00 24.02 ?  249 GLN D CB    1 
ATOM   15403 C  CG    . GLN D 2 270 ? 164.651 99.224  131.135 1.00 25.40 ?  249 GLN D CG    1 
ATOM   15404 C  CD    . GLN D 2 270 ? 164.542 97.770  130.707 1.00 29.23 ?  249 GLN D CD    1 
ATOM   15405 O  OE1   . GLN D 2 270 ? 165.230 96.902  131.246 1.00 31.31 ?  249 GLN D OE1   1 
ATOM   15406 N  NE2   . GLN D 2 270 ? 163.665 97.495  129.745 1.00 30.04 ?  249 GLN D NE2   1 
ATOM   15407 N  N     . VAL D 2 271 ? 164.512 102.649 131.776 1.00 21.93 ?  250 VAL D N     1 
ATOM   15408 C  CA    . VAL D 2 271 ? 163.997 103.812 131.045 1.00 21.29 ?  250 VAL D CA    1 
ATOM   15409 C  C     . VAL D 2 271 ? 163.873 105.057 131.943 1.00 21.16 ?  250 VAL D C     1 
ATOM   15410 O  O     . VAL D 2 271 ? 163.260 106.055 131.552 1.00 21.54 ?  250 VAL D O     1 
ATOM   15411 C  CB    . VAL D 2 271 ? 162.653 103.483 130.318 1.00 21.62 ?  250 VAL D CB    1 
ATOM   15412 C  CG1   . VAL D 2 271 ? 162.876 102.425 129.239 1.00 21.36 ?  250 VAL D CG1   1 
ATOM   15413 C  CG2   . VAL D 2 271 ? 161.572 103.027 131.316 1.00 21.17 ?  250 VAL D CG2   1 
ATOM   15414 N  N     . GLY D 2 272 ? 164.439 104.980 133.153 1.00 20.92 ?  251 GLY D N     1 
ATOM   15415 C  CA    . GLY D 2 272 ? 164.574 106.134 134.064 1.00 20.61 ?  251 GLY D CA    1 
ATOM   15416 C  C     . GLY D 2 272 ? 163.306 106.712 134.689 1.00 20.77 ?  251 GLY D C     1 
ATOM   15417 O  O     . GLY D 2 272 ? 163.272 107.895 135.062 1.00 20.28 ?  251 GLY D O     1 
ATOM   15418 N  N     . LEU D 2 273 ? 162.273 105.886 134.830 1.00 19.85 ?  252 LEU D N     1 
ATOM   15419 C  CA    . LEU D 2 273 ? 160.964 106.400 135.238 1.00 20.09 ?  252 LEU D CA    1 
ATOM   15420 C  C     . LEU D 2 273 ? 160.480 105.994 136.633 1.00 19.88 ?  252 LEU D C     1 
ATOM   15421 O  O     . LEU D 2 273 ? 159.435 106.466 137.070 1.00 20.04 ?  252 LEU D O     1 
ATOM   15422 C  CB    . LEU D 2 273 ? 159.905 105.975 134.207 1.00 19.97 ?  252 LEU D CB    1 
ATOM   15423 C  CG    . LEU D 2 273 ? 160.118 106.433 132.771 1.00 20.26 ?  252 LEU D CG    1 
ATOM   15424 C  CD1   . LEU D 2 273 ? 158.917 106.002 131.960 1.00 18.98 ?  252 LEU D CD1   1 
ATOM   15425 C  CD2   . LEU D 2 273 ? 160.331 107.970 132.673 1.00 21.03 ?  252 LEU D CD2   1 
ATOM   15426 N  N     . SER D 2 274 ? 161.243 105.142 137.319 0.50 19.54 ?  253 SER D N     1 
ATOM   15427 C  CA    . SER D 2 274 ? 160.769 104.470 138.540 0.50 19.34 ?  253 SER D CA    1 
ATOM   15428 C  C     . SER D 2 274 ? 160.254 105.403 139.642 0.50 20.05 ?  253 SER D C     1 
ATOM   15429 O  O     . SER D 2 274 ? 159.236 105.111 140.268 0.50 20.31 ?  253 SER D O     1 
ATOM   15430 C  CB    . SER D 2 274 ? 161.836 103.518 139.096 0.50 18.97 ?  253 SER D CB    1 
ATOM   15431 O  OG    . SER D 2 274 ? 162.241 102.573 138.124 0.50 15.35 ?  253 SER D OG    1 
ATOM   15432 N  N     . HIS D 2 275 ? 160.958 106.508 139.881 1.00 20.77 ?  254 HIS D N     1 
ATOM   15433 C  CA    . HIS D 2 275 ? 160.529 107.506 140.882 1.00 21.18 ?  254 HIS D CA    1 
ATOM   15434 C  C     . HIS D 2 275 ? 159.077 107.966 140.658 1.00 21.50 ?  254 HIS D C     1 
ATOM   15435 O  O     . HIS D 2 275 ? 158.258 107.954 141.593 1.00 19.88 ?  254 HIS D O     1 
ATOM   15436 C  CB    . HIS D 2 275 ? 161.474 108.718 140.918 1.00 21.60 ?  254 HIS D CB    1 
ATOM   15437 C  CG    . HIS D 2 275 ? 161.007 109.813 141.828 1.00 22.43 ?  254 HIS D CG    1 
ATOM   15438 N  ND1   . HIS D 2 275 ? 161.332 109.863 143.169 1.00 22.77 ?  254 HIS D ND1   1 
ATOM   15439 C  CD2   . HIS D 2 275 ? 160.221 110.893 141.590 1.00 22.50 ?  254 HIS D CD2   1 
ATOM   15440 C  CE1   . HIS D 2 275 ? 160.771 110.930 143.714 1.00 24.05 ?  254 HIS D CE1   1 
ATOM   15441 N  NE2   . HIS D 2 275 ? 160.087 111.568 142.779 1.00 23.22 ?  254 HIS D NE2   1 
ATOM   15442 N  N     . ASP D 2 276 ? 158.768 108.352 139.420 1.00 22.34 ?  255 ASP D N     1 
ATOM   15443 C  CA    . ASP D 2 276 ? 157.429 108.823 139.078 1.00 23.19 ?  255 ASP D CA    1 
ATOM   15444 C  C     . ASP D 2 276 ? 156.394 107.707 139.093 1.00 22.17 ?  255 ASP D C     1 
ATOM   15445 O  O     . ASP D 2 276 ? 155.250 107.944 139.452 1.00 21.87 ?  255 ASP D O     1 
ATOM   15446 C  CB    . ASP D 2 276 ? 157.409 109.525 137.710 1.00 24.33 ?  255 ASP D CB    1 
ATOM   15447 C  CG    . ASP D 2 276 ? 157.737 111.017 137.796 1.00 27.58 ?  255 ASP D CG    1 
ATOM   15448 O  OD1   . ASP D 2 276 ? 157.541 111.636 138.865 1.00 31.10 ?  255 ASP D OD1   1 
ATOM   15449 O  OD2   . ASP D 2 276 ? 158.201 111.571 136.773 1.00 29.88 -1 255 ASP D OD2   1 
ATOM   15450 N  N     . VAL D 2 277 ? 156.785 106.506 138.668 1.00 21.21 ?  256 VAL D N     1 
ATOM   15451 C  CA    . VAL D 2 277 ? 155.878 105.355 138.721 1.00 20.51 ?  256 VAL D CA    1 
ATOM   15452 C  C     . VAL D 2 277 ? 155.474 105.034 140.165 1.00 20.32 ?  256 VAL D C     1 
ATOM   15453 O  O     . VAL D 2 277 ? 154.313 104.735 140.430 1.00 19.81 ?  256 VAL D O     1 
ATOM   15454 C  CB    . VAL D 2 277 ? 156.471 104.093 138.032 1.00 20.30 ?  256 VAL D CB    1 
ATOM   15455 C  CG1   . VAL D 2 277 ? 155.528 102.911 138.177 1.00 21.16 ?  256 VAL D CG1   1 
ATOM   15456 C  CG2   . VAL D 2 277 ? 156.733 104.367 136.561 1.00 19.06 ?  256 VAL D CG2   1 
ATOM   15457 N  N     . LYS D 2 278 ? 156.436 105.119 141.084 1.00 19.84 ?  257 LYS D N     1 
ATOM   15458 C  CA    . LYS D 2 278 ? 156.173 104.893 142.505 1.00 20.27 ?  257 LYS D CA    1 
ATOM   15459 C  C     . LYS D 2 278 ? 155.127 105.861 143.072 1.00 20.16 ?  257 LYS D C     1 
ATOM   15460 O  O     . LYS D 2 278 ? 154.258 105.437 143.831 1.00 19.88 ?  257 LYS D O     1 
ATOM   15461 C  CB    . LYS D 2 278 ? 157.467 104.926 143.323 1.00 20.20 ?  257 LYS D CB    1 
ATOM   15462 C  CG    . LYS D 2 278 ? 158.334 103.688 143.122 1.00 21.60 ?  257 LYS D CG    1 
ATOM   15463 C  CD    . LYS D 2 278 ? 159.724 103.865 143.722 1.00 21.53 ?  257 LYS D CD    1 
ATOM   15464 C  CE    . LYS D 2 278 ? 160.596 102.689 143.353 1.00 24.52 ?  257 LYS D CE    1 
ATOM   15465 N  NZ    . LYS D 2 278 ? 161.958 102.825 143.965 1.00 26.32 1  257 LYS D NZ    1 
ATOM   15466 N  N     . LYS D 2 279 ? 155.197 107.139 142.684 1.00 19.67 ?  258 LYS D N     1 
ATOM   15467 C  CA    . LYS D 2 279 ? 154.172 108.114 143.084 1.00 20.10 ?  258 LYS D CA    1 
ATOM   15468 C  C     . LYS D 2 279 ? 152.783 107.694 142.586 1.00 19.12 ?  258 LYS D C     1 
ATOM   15469 O  O     . LYS D 2 279 ? 151.799 107.820 143.316 1.00 18.59 ?  258 LYS D O     1 
ATOM   15470 C  CB    . LYS D 2 279 ? 154.504 109.536 142.591 1.00 20.54 ?  258 LYS D CB    1 
ATOM   15471 C  CG    . LYS D 2 279 ? 155.809 110.116 143.131 1.00 22.84 ?  258 LYS D CG    1 
ATOM   15472 C  CD    . LYS D 2 279 ? 155.824 111.662 143.099 1.00 24.16 ?  258 LYS D CD    1 
ATOM   15473 C  CE    . LYS D 2 279 ? 155.818 112.223 141.680 1.00 25.61 ?  258 LYS D CE    1 
ATOM   15474 N  NZ    . LYS D 2 279 ? 155.839 113.738 141.659 1.00 24.70 1  258 LYS D NZ    1 
ATOM   15475 N  N     . PHE D 2 280 ? 152.730 107.178 141.354 1.00 19.04 ?  259 PHE D N     1 
ATOM   15476 C  CA    . PHE D 2 280 ? 151.480 106.726 140.714 1.00 19.31 ?  259 PHE D CA    1 
ATOM   15477 C  C     . PHE D 2 280 ? 150.880 105.485 141.384 1.00 19.25 ?  259 PHE D C     1 
ATOM   15478 O  O     . PHE D 2 280 ? 149.656 105.373 141.528 1.00 19.71 ?  259 PHE D O     1 
ATOM   15479 C  CB    . PHE D 2 280 ? 151.733 106.440 139.233 1.00 19.04 ?  259 PHE D CB    1 
ATOM   15480 C  CG    . PHE D 2 280 ? 150.479 106.348 138.384 1.00 20.15 ?  259 PHE D CG    1 
ATOM   15481 C  CD1   . PHE D 2 280 ? 149.564 107.390 138.344 1.00 21.63 ?  259 PHE D CD1   1 
ATOM   15482 C  CD2   . PHE D 2 280 ? 150.255 105.226 137.584 1.00 19.95 ?  259 PHE D CD2   1 
ATOM   15483 C  CE1   . PHE D 2 280 ? 148.420 107.313 137.519 1.00 22.56 ?  259 PHE D CE1   1 
ATOM   15484 C  CE2   . PHE D 2 280 ? 149.131 105.134 136.764 1.00 20.29 ?  259 PHE D CE2   1 
ATOM   15485 C  CZ    . PHE D 2 280 ? 148.208 106.180 136.733 1.00 21.30 ?  259 PHE D CZ    1 
ATOM   15486 N  N     . ILE D 2 281 ? 151.736 104.549 141.780 1.00 19.36 ?  260 ILE D N     1 
ATOM   15487 C  CA    . ILE D 2 281 ? 151.310 103.395 142.578 1.00 19.45 ?  260 ILE D CA    1 
ATOM   15488 C  C     . ILE D 2 281 ? 150.643 103.813 143.906 1.00 19.61 ?  260 ILE D C     1 
ATOM   15489 O  O     . ILE D 2 281 ? 149.569 103.307 144.238 1.00 19.72 ?  260 ILE D O     1 
ATOM   15490 C  CB    . ILE D 2 281 ? 152.510 102.444 142.822 1.00 19.49 ?  260 ILE D CB    1 
ATOM   15491 C  CG1   . ILE D 2 281 ? 152.964 101.836 141.491 1.00 20.10 ?  260 ILE D CG1   1 
ATOM   15492 C  CG2   . ILE D 2 281 ? 152.202 101.362 143.881 1.00 20.53 ?  260 ILE D CG2   1 
ATOM   15493 C  CD1   . ILE D 2 281 ? 154.338 101.164 141.595 1.00 21.17 ?  260 ILE D CD1   1 
ATOM   15494 N  N     . ARG D 2 282 ? 151.268 104.731 144.646 1.00 19.75 ?  261 ARG D N     1 
ATOM   15495 C  CA    . ARG D 2 282 ? 150.744 105.160 145.957 1.00 20.34 ?  261 ARG D CA    1 
ATOM   15496 C  C     . ARG D 2 282 ? 149.416 105.897 145.825 1.00 21.18 ?  261 ARG D C     1 
ATOM   15497 O  O     . ARG D 2 282 ? 148.491 105.700 146.626 1.00 21.68 ?  261 ARG D O     1 
ATOM   15498 C  CB    . ARG D 2 282 ? 151.765 106.020 146.714 1.00 20.20 ?  261 ARG D CB    1 
ATOM   15499 C  CG    . ARG D 2 282 ? 152.964 105.242 147.226 1.00 20.57 ?  261 ARG D CG    1 
ATOM   15500 C  CD    . ARG D 2 282 ? 153.856 106.115 148.112 1.00 23.15 ?  261 ARG D CD    1 
ATOM   15501 N  NE    . ARG D 2 282 ? 154.643 107.098 147.364 1.00 23.46 ?  261 ARG D NE    1 
ATOM   15502 C  CZ    . ARG D 2 282 ? 155.851 106.870 146.851 1.00 22.84 ?  261 ARG D CZ    1 
ATOM   15503 N  NH1   . ARG D 2 282 ? 156.420 105.677 146.963 1.00 23.37 1  261 ARG D NH1   1 
ATOM   15504 N  NH2   . ARG D 2 282 ? 156.489 107.841 146.211 1.00 22.27 ?  261 ARG D NH2   1 
ATOM   15505 N  N     . TYR D 2 283 ? 149.341 106.760 144.818 1.00 21.46 ?  262 TYR D N     1 
ATOM   15506 C  CA    . TYR D 2 283 ? 148.118 107.495 144.500 1.00 22.97 ?  262 TYR D CA    1 
ATOM   15507 C  C     . TYR D 2 283 ? 146.964 106.513 144.198 1.00 22.12 ?  262 TYR D C     1 
ATOM   15508 O  O     . TYR D 2 283 ? 145.841 106.694 144.675 1.00 22.00 ?  262 TYR D O     1 
ATOM   15509 C  CB    . TYR D 2 283 ? 148.411 108.445 143.334 1.00 23.37 ?  262 TYR D CB    1 
ATOM   15510 C  CG    . TYR D 2 283 ? 147.216 109.042 142.627 1.00 27.31 ?  262 TYR D CG    1 
ATOM   15511 C  CD1   . TYR D 2 283 ? 146.627 110.220 143.086 1.00 30.79 ?  262 TYR D CD1   1 
ATOM   15512 C  CD2   . TYR D 2 283 ? 146.704 108.451 141.472 1.00 30.31 ?  262 TYR D CD2   1 
ATOM   15513 C  CE1   . TYR D 2 283 ? 145.521 110.780 142.426 1.00 33.18 ?  262 TYR D CE1   1 
ATOM   15514 C  CE2   . TYR D 2 283 ? 145.611 109.005 140.799 1.00 33.20 ?  262 TYR D CE2   1 
ATOM   15515 C  CZ    . TYR D 2 283 ? 145.031 110.173 141.280 1.00 34.74 ?  262 TYR D CZ    1 
ATOM   15516 O  OH    . TYR D 2 283 ? 143.956 110.721 140.609 1.00 37.63 ?  262 TYR D OH    1 
ATOM   15517 N  N     . ASN D 2 284 ? 147.254 105.451 143.452 1.00 21.63 ?  263 ASN D N     1 
ATOM   15518 C  CA    . ASN D 2 284 ? 146.228 104.463 143.128 1.00 21.41 ?  263 ASN D CA    1 
ATOM   15519 C  C     . ASN D 2 284 ? 145.917 103.503 144.281 1.00 20.86 ?  263 ASN D C     1 
ATOM   15520 O  O     . ASN D 2 284 ? 144.785 103.051 144.411 1.00 20.92 ?  263 ASN D O     1 
ATOM   15521 C  CB    . ASN D 2 284 ? 146.552 103.729 141.825 1.00 21.15 ?  263 ASN D CB    1 
ATOM   15522 C  CG    . ASN D 2 284 ? 146.299 104.600 140.602 1.00 22.59 ?  263 ASN D CG    1 
ATOM   15523 O  OD1   . ASN D 2 284 ? 145.148 104.869 140.247 1.00 22.35 ?  263 ASN D OD1   1 
ATOM   15524 N  ND2   . ASN D 2 284 ? 147.371 105.057 139.962 1.00 22.93 ?  263 ASN D ND2   1 
ATOM   15525 N  N     . ALA D 2 285 ? 146.913 103.208 145.115 1.00 20.92 ?  264 ALA D N     1 
ATOM   15526 C  CA    . ALA D 2 285 ? 146.683 102.487 146.379 1.00 20.77 ?  264 ALA D CA    1 
ATOM   15527 C  C     . ALA D 2 285 ? 145.663 103.210 147.265 1.00 21.13 ?  264 ALA D C     1 
ATOM   15528 O  O     . ALA D 2 285 ? 144.766 102.575 147.836 1.00 19.92 ?  264 ALA D O     1 
ATOM   15529 C  CB    . ALA D 2 285 ? 148.002 102.270 147.134 1.00 20.68 ?  264 ALA D CB    1 
ATOM   15530 N  N     . ASN D 2 286 ? 145.803 104.536 147.370 1.00 21.38 ?  265 ASN D N     1 
ATOM   15531 C  CA    . ASN D 2 286 ? 144.855 105.371 148.112 1.00 21.94 ?  265 ASN D CA    1 
ATOM   15532 C  C     . ASN D 2 286 ? 143.432 105.303 147.528 1.00 22.13 ?  265 ASN D C     1 
ATOM   15533 O  O     . ASN D 2 286 ? 142.460 105.270 148.273 1.00 21.95 ?  265 ASN D O     1 
ATOM   15534 C  CB    . ASN D 2 286 ? 145.324 106.827 148.154 1.00 22.22 ?  265 ASN D CB    1 
ATOM   15535 C  CG    . ASN D 2 286 ? 146.412 107.082 149.194 1.00 22.80 ?  265 ASN D CG    1 
ATOM   15536 O  OD1   . ASN D 2 286 ? 146.685 106.256 150.071 1.00 22.57 ?  265 ASN D OD1   1 
ATOM   15537 N  ND2   . ASN D 2 286 ? 147.042 108.246 149.087 1.00 23.91 ?  265 ASN D ND2   1 
ATOM   15538 N  N     . LYS D 2 287 ? 143.316 105.275 146.203 1.00 22.51 ?  266 LYS D N     1 
ATOM   15539 C  CA    . LYS D 2 287 ? 142.001 105.127 145.562 1.00 22.91 ?  266 LYS D CA    1 
ATOM   15540 C  C     . LYS D 2 287 ? 141.369 103.770 145.898 1.00 22.33 ?  266 LYS D C     1 
ATOM   15541 O  O     . LYS D 2 287 ? 140.180 103.700 146.185 1.00 22.24 ?  266 LYS D O     1 
ATOM   15542 C  CB    . LYS D 2 287 ? 142.093 105.317 144.042 1.00 23.65 ?  266 LYS D CB    1 
ATOM   15543 C  CG    . LYS D 2 287 ? 142.273 106.773 143.612 1.00 26.50 ?  266 LYS D CG    1 
ATOM   15544 C  CD    . LYS D 2 287 ? 142.342 106.884 142.078 1.00 31.30 ?  266 LYS D CD    1 
ATOM   15545 C  CE    . LYS D 2 287 ? 142.016 108.299 141.635 1.00 35.08 ?  266 LYS D CE    1 
ATOM   15546 N  NZ    . LYS D 2 287 ? 142.026 108.484 140.153 1.00 37.66 1  266 LYS D NZ    1 
ATOM   15547 N  N     . ALA D 2 288 ? 142.179 102.710 145.872 1.00 21.41 ?  267 ALA D N     1 
ATOM   15548 C  CA    . ALA D 2 288 ? 141.742 101.356 146.215 1.00 21.53 ?  267 ALA D CA    1 
ATOM   15549 C  C     . ALA D 2 288 ? 141.231 101.276 147.664 1.00 21.77 ?  267 ALA D C     1 
ATOM   15550 O  O     . ALA D 2 288 ? 140.174 100.683 147.942 1.00 21.59 ?  267 ALA D O     1 
ATOM   15551 C  CB    . ALA D 2 288 ? 142.878 100.352 145.978 1.00 21.33 ?  267 ALA D CB    1 
ATOM   15552 N  N     . LEU D 2 289 ? 141.967 101.892 148.579 1.00 21.71 ?  268 LEU D N     1 
ATOM   15553 C  CA    . LEU D 2 289 ? 141.528 101.977 149.966 1.00 22.36 ?  268 LEU D CA    1 
ATOM   15554 C  C     . LEU D 2 289 ? 140.214 102.738 150.080 1.00 23.01 ?  268 LEU D C     1 
ATOM   15555 O  O     . LEU D 2 289 ? 139.290 102.290 150.763 1.00 23.14 ?  268 LEU D O     1 
ATOM   15556 C  CB    . LEU D 2 289 ? 142.614 102.597 150.852 1.00 22.61 ?  268 LEU D CB    1 
ATOM   15557 C  CG    . LEU D 2 289 ? 143.861 101.718 151.087 1.00 21.22 ?  268 LEU D CG    1 
ATOM   15558 C  CD1   . LEU D 2 289 ? 144.992 102.530 151.699 1.00 20.77 ?  268 LEU D CD1   1 
ATOM   15559 C  CD2   . LEU D 2 289 ? 143.544 100.484 151.962 1.00 21.40 ?  268 LEU D CD2   1 
ATOM   15560 N  N     . MET D 2 290 ? 140.106 103.872 149.395 1.00 23.87 ?  269 MET D N     1 
ATOM   15561 C  CA    . MET D 2 290 ? 138.853 104.620 149.442 1.00 25.26 ?  269 MET D CA    1 
ATOM   15562 C  C     . MET D 2 290 ? 137.677 103.808 148.874 1.00 24.37 ?  269 MET D C     1 
ATOM   15563 O  O     . MET D 2 290 ? 136.583 103.862 149.428 1.00 23.97 ?  269 MET D O     1 
ATOM   15564 C  CB    . MET D 2 290 ? 139.008 106.006 148.824 1.00 25.94 ?  269 MET D CB    1 
ATOM   15565 C  CG    . MET D 2 290 ? 139.689 106.978 149.808 1.00 31.08 ?  269 MET D CG    1 
ATOM   15566 S  SD    . MET D 2 290 ? 139.948 108.644 149.158 1.00 41.28 ?  269 MET D SD    1 
ATOM   15567 C  CE    . MET D 2 290 ? 138.282 109.073 148.590 1.00 38.56 ?  269 MET D CE    1 
ATOM   15568 N  N     . ASN D 2 291 ? 137.915 103.022 147.819 1.00 23.66 ?  270 ASN D N     1 
ATOM   15569 C  CA    . ASN D 2 291 ? 136.896 102.075 147.309 1.00 23.17 ?  270 ASN D CA    1 
ATOM   15570 C  C     . ASN D 2 291 ? 136.384 101.078 148.354 1.00 23.22 ?  270 ASN D C     1 
ATOM   15571 O  O     . ASN D 2 291 ? 135.236 100.640 148.289 1.00 22.68 ?  270 ASN D O     1 
ATOM   15572 C  CB    . ASN D 2 291 ? 137.403 101.301 146.082 1.00 22.41 ?  270 ASN D CB    1 
ATOM   15573 C  CG    . ASN D 2 291 ? 137.549 102.177 144.860 1.00 21.93 ?  270 ASN D CG    1 
ATOM   15574 O  OD1   . ASN D 2 291 ? 137.050 103.306 144.824 1.00 20.94 ?  270 ASN D OD1   1 
ATOM   15575 N  ND2   . ASN D 2 291 ? 138.237 101.663 143.843 1.00 19.20 ?  270 ASN D ND2   1 
ATOM   15576 N  N     . LEU D 2 292 ? 137.251 100.731 149.303 1.00 23.53 ?  271 LEU D N     1 
ATOM   15577 C  CA    . LEU D 2 292 ? 136.915 99.808  150.390 1.00 24.21 ?  271 LEU D CA    1 
ATOM   15578 C  C     . LEU D 2 292 ? 136.432 100.545 151.643 1.00 25.14 ?  271 LEU D C     1 
ATOM   15579 O  O     . LEU D 2 292 ? 136.279 99.940  152.717 1.00 25.14 ?  271 LEU D O     1 
ATOM   15580 C  CB    . LEU D 2 292 ? 138.121 98.902  150.716 1.00 23.71 ?  271 LEU D CB    1 
ATOM   15581 C  CG    . LEU D 2 292 ? 138.602 97.937  149.622 1.00 23.37 ?  271 LEU D CG    1 
ATOM   15582 C  CD1   . LEU D 2 292 ? 140.009 97.417  149.929 1.00 23.28 ?  271 LEU D CD1   1 
ATOM   15583 C  CD2   . LEU D 2 292 ? 137.618 96.767  149.420 1.00 23.06 ?  271 LEU D CD2   1 
ATOM   15584 N  N     . GLY D 2 293 ? 136.185 101.848 151.498 1.00 25.82 ?  272 GLY D N     1 
ATOM   15585 C  CA    . GLY D 2 293 ? 135.709 102.681 152.596 1.00 27.13 ?  272 GLY D CA    1 
ATOM   15586 C  C     . GLY D 2 293 ? 136.744 102.962 153.666 1.00 27.99 ?  272 GLY D C     1 
ATOM   15587 O  O     . GLY D 2 293 ? 136.390 103.339 154.779 1.00 27.97 ?  272 GLY D O     1 
ATOM   15588 N  N     . PHE D 2 294 ? 138.025 102.778 153.331 1.00 28.02 ?  273 PHE D N     1 
ATOM   15589 C  CA    . PHE D 2 294 ? 139.128 103.026 154.268 1.00 28.75 ?  273 PHE D CA    1 
ATOM   15590 C  C     . PHE D 2 294 ? 139.836 104.360 153.999 1.00 29.00 ?  273 PHE D C     1 
ATOM   15591 O  O     . PHE D 2 294 ? 139.741 104.908 152.903 1.00 28.74 ?  273 PHE D O     1 
ATOM   15592 C  CB    . PHE D 2 294 ? 140.154 101.883 154.204 1.00 28.32 ?  273 PHE D CB    1 
ATOM   15593 C  CG    . PHE D 2 294 ? 139.618 100.553 154.660 1.00 28.66 ?  273 PHE D CG    1 
ATOM   15594 C  CD1   . PHE D 2 294 ? 138.797 100.461 155.784 1.00 30.23 ?  273 PHE D CD1   1 
ATOM   15595 C  CD2   . PHE D 2 294 ? 139.948 99.392  153.974 1.00 26.94 ?  273 PHE D CD2   1 
ATOM   15596 C  CE1   . PHE D 2 294 ? 138.300 99.224  156.208 1.00 31.04 ?  273 PHE D CE1   1 
ATOM   15597 C  CE2   . PHE D 2 294 ? 139.467 98.157  154.386 1.00 27.39 ?  273 PHE D CE2   1 
ATOM   15598 C  CZ    . PHE D 2 294 ? 138.645 98.064  155.502 1.00 29.80 ?  273 PHE D CZ    1 
ATOM   15599 N  N     . ASP D 2 295 ? 140.540 104.871 155.007 1.00 29.60 ?  274 ASP D N     1 
ATOM   15600 C  CA    . ASP D 2 295 ? 141.316 106.102 154.871 1.00 30.40 ?  274 ASP D CA    1 
ATOM   15601 C  C     . ASP D 2 295 ? 142.548 105.899 153.967 1.00 29.58 ?  274 ASP D C     1 
ATOM   15602 O  O     . ASP D 2 295 ? 143.079 104.792 153.881 1.00 28.68 ?  274 ASP D O     1 
ATOM   15603 C  CB    . ASP D 2 295 ? 141.766 106.615 156.245 1.00 31.44 ?  274 ASP D CB    1 
ATOM   15604 C  CG    . ASP D 2 295 ? 140.602 107.047 157.130 1.00 34.27 ?  274 ASP D CG    1 
ATOM   15605 O  OD1   . ASP D 2 295 ? 139.547 107.474 156.601 1.00 36.43 ?  274 ASP D OD1   1 
ATOM   15606 O  OD2   . ASP D 2 295 ? 140.755 106.960 158.368 1.00 38.03 -1 274 ASP D OD2   1 
ATOM   15607 N  N     . PRO D 2 296 ? 143.009 106.976 153.301 1.00 29.59 ?  275 PRO D N     1 
ATOM   15608 C  CA    . PRO D 2 296 ? 144.235 106.842 152.508 1.00 29.09 ?  275 PRO D CA    1 
ATOM   15609 C  C     . PRO D 2 296 ? 145.421 106.477 153.399 1.00 29.26 ?  275 PRO D C     1 
ATOM   15610 O  O     . PRO D 2 296 ? 145.495 106.911 154.549 1.00 29.36 ?  275 PRO D O     1 
ATOM   15611 C  CB    . PRO D 2 296 ? 144.428 108.239 151.901 1.00 29.49 ?  275 PRO D CB    1 
ATOM   15612 C  CG    . PRO D 2 296 ? 143.587 109.163 152.739 1.00 30.28 ?  275 PRO D CG    1 
ATOM   15613 C  CD    . PRO D 2 296 ? 142.441 108.337 153.233 1.00 29.63 ?  275 PRO D CD    1 
ATOM   15614 N  N     . TYR D 2 297 ? 146.328 105.667 152.874 1.00 28.97 ?  276 TYR D N     1 
ATOM   15615 C  CA    . TYR D 2 297 ? 147.483 105.206 153.635 1.00 29.63 ?  276 TYR D CA    1 
ATOM   15616 C  C     . TYR D 2 297 ? 148.703 106.115 153.411 1.00 29.55 ?  276 TYR D C     1 
ATOM   15617 O  O     . TYR D 2 297 ? 149.515 106.333 154.319 1.00 30.12 ?  276 TYR D O     1 
ATOM   15618 C  CB    . TYR D 2 297 ? 147.812 103.776 153.209 1.00 29.49 ?  276 TYR D CB    1 
ATOM   15619 C  CG    . TYR D 2 297 ? 148.768 103.038 154.108 1.00 31.19 ?  276 TYR D CG    1 
ATOM   15620 C  CD1   . TYR D 2 297 ? 148.435 102.771 155.440 1.00 31.93 ?  276 TYR D CD1   1 
ATOM   15621 C  CD2   . TYR D 2 297 ? 149.996 102.581 153.626 1.00 31.98 ?  276 TYR D CD2   1 
ATOM   15622 C  CE1   . TYR D 2 297 ? 149.307 102.084 156.275 1.00 33.86 ?  276 TYR D CE1   1 
ATOM   15623 C  CE2   . TYR D 2 297 ? 150.877 101.885 154.455 1.00 33.88 ?  276 TYR D CE2   1 
ATOM   15624 C  CZ    . TYR D 2 297 ? 150.516 101.639 155.775 1.00 34.42 ?  276 TYR D CZ    1 
ATOM   15625 O  OH    . TYR D 2 297 ? 151.370 100.962 156.608 1.00 37.63 ?  276 TYR D OH    1 
ATOM   15626 N  N     . PHE D 2 298 ? 148.812 106.632 152.192 1.00 29.10 ?  277 PHE D N     1 
ATOM   15627 C  CA    . PHE D 2 298 ? 149.969 107.400 151.746 1.00 28.97 ?  277 PHE D CA    1 
ATOM   15628 C  C     . PHE D 2 298 ? 149.636 108.894 151.667 1.00 29.77 ?  277 PHE D C     1 
ATOM   15629 O  O     . PHE D 2 298 ? 148.496 109.269 151.380 1.00 29.07 ?  277 PHE D O     1 
ATOM   15630 C  CB    . PHE D 2 298 ? 150.428 106.906 150.369 1.00 27.99 ?  277 PHE D CB    1 
ATOM   15631 C  CG    . PHE D 2 298 ? 150.855 105.458 150.344 1.00 27.61 ?  277 PHE D CG    1 
ATOM   15632 C  CD1   . PHE D 2 298 ? 150.062 104.495 149.733 1.00 25.91 ?  277 PHE D CD1   1 
ATOM   15633 C  CD2   . PHE D 2 298 ? 152.065 105.064 150.918 1.00 27.32 ?  277 PHE D CD2   1 
ATOM   15634 C  CE1   . PHE D 2 298 ? 150.458 103.169 149.702 1.00 26.65 ?  277 PHE D CE1   1 
ATOM   15635 C  CE2   . PHE D 2 298 ? 152.474 103.742 150.893 1.00 25.38 ?  277 PHE D CE2   1 
ATOM   15636 C  CZ    . PHE D 2 298 ? 151.672 102.789 150.295 1.00 26.20 ?  277 PHE D CZ    1 
ATOM   15637 N  N     . GLU D 2 299 ? 150.637 109.735 151.931 1.00 31.10 ?  278 GLU D N     1 
ATOM   15638 C  CA    . GLU D 2 299 ? 150.503 111.184 151.766 1.00 32.86 ?  278 GLU D CA    1 
ATOM   15639 C  C     . GLU D 2 299 ? 150.200 111.516 150.298 1.00 33.04 ?  278 GLU D C     1 
ATOM   15640 O  O     . GLU D 2 299 ? 150.611 110.787 149.391 1.00 32.23 ?  278 GLU D O     1 
ATOM   15641 C  CB    . GLU D 2 299 ? 151.778 111.907 152.235 1.00 33.45 ?  278 GLU D CB    1 
ATOM   15642 C  CG    . GLU D 2 299 ? 153.032 111.526 151.434 1.00 36.27 ?  278 GLU D CG    1 
ATOM   15643 C  CD    . GLU D 2 299 ? 154.277 112.327 151.788 1.00 40.47 ?  278 GLU D CD    1 
ATOM   15644 O  OE1   . GLU D 2 299 ? 154.519 112.596 152.987 1.00 41.72 ?  278 GLU D OE1   1 
ATOM   15645 O  OE2   . GLU D 2 299 ? 155.030 112.660 150.847 1.00 42.65 -1 278 GLU D OE2   1 
ATOM   15646 N  N     . GLU D 2 300 ? 149.475 112.612 150.086 1.00 34.09 ?  279 GLU D N     1 
ATOM   15647 C  CA    . GLU D 2 300 ? 149.123 113.081 148.753 1.00 35.06 ?  279 GLU D CA    1 
ATOM   15648 C  C     . GLU D 2 300 ? 150.376 113.536 148.002 1.00 34.97 ?  279 GLU D C     1 
ATOM   15649 O  O     . GLU D 2 300 ? 151.227 114.232 148.559 1.00 34.96 ?  279 GLU D O     1 
ATOM   15650 C  CB    . GLU D 2 300 ? 148.095 114.221 148.845 1.00 35.81 ?  279 GLU D CB    1 
ATOM   15651 C  CG    . GLU D 2 300 ? 147.514 114.658 147.499 1.00 38.58 ?  279 GLU D CG    1 
ATOM   15652 C  CD    . GLU D 2 300 ? 146.140 115.313 147.621 1.00 43.09 ?  279 GLU D CD    1 
ATOM   15653 O  OE1   . GLU D 2 300 ? 145.189 114.820 146.971 1.00 44.69 ?  279 GLU D OE1   1 
ATOM   15654 O  OE2   . GLU D 2 300 ? 146.006 116.309 148.369 1.00 44.94 -1 279 GLU D OE2   1 
ATOM   15655 N  N     . GLU D 2 301 ? 150.485 113.110 146.748 1.00 34.73 ?  280 GLU D N     1 
ATOM   15656 C  CA    . GLU D 2 301 ? 151.598 113.483 145.883 1.00 35.16 ?  280 GLU D CA    1 
ATOM   15657 C  C     . GLU D 2 301 ? 151.050 113.921 144.536 1.00 35.23 ?  280 GLU D C     1 
ATOM   15658 O  O     . GLU D 2 301 ? 149.975 113.478 144.120 1.00 34.92 ?  280 GLU D O     1 
ATOM   15659 C  CB    . GLU D 2 301 ? 152.546 112.292 145.683 1.00 35.10 ?  280 GLU D CB    1 
ATOM   15660 C  CG    . GLU D 2 301 ? 153.532 112.057 146.825 1.00 36.62 ?  280 GLU D CG    1 
ATOM   15661 C  CD    . GLU D 2 301 ? 154.261 110.717 146.713 1.00 37.59 ?  280 GLU D CD    1 
ATOM   15662 O  OE1   . GLU D 2 301 ? 153.591 109.665 146.659 1.00 38.10 ?  280 GLU D OE1   1 
ATOM   15663 O  OE2   . GLU D 2 301 ? 155.507 110.714 146.706 1.00 38.93 -1 280 GLU D OE2   1 
ATOM   15664 N  N     . ASP D 2 302 ? 151.783 114.790 143.851 1.00 35.60 ?  281 ASP D N     1 
ATOM   15665 C  CA    . ASP D 2 302 ? 151.404 115.179 142.498 1.00 35.96 ?  281 ASP D CA    1 
ATOM   15666 C  C     . ASP D 2 302 ? 151.853 114.085 141.538 1.00 35.01 ?  281 ASP D C     1 
ATOM   15667 O  O     . ASP D 2 302 ? 152.806 113.361 141.824 1.00 35.52 ?  281 ASP D O     1 
ATOM   15668 C  CB    . ASP D 2 302 ? 151.982 116.556 142.127 1.00 36.82 ?  281 ASP D CB    1 
ATOM   15669 C  CG    . ASP D 2 302 ? 153.521 116.586 142.095 1.00 39.01 ?  281 ASP D CG    1 
ATOM   15670 O  OD1   . ASP D 2 302 ? 154.191 115.724 142.717 1.00 40.83 ?  281 ASP D OD1   1 
ATOM   15671 O  OD2   . ASP D 2 302 ? 154.063 117.510 141.454 1.00 41.13 -1 281 ASP D OD2   1 
ATOM   15672 N  N     . ILE D 2 303 ? 151.150 113.933 140.423 1.00 33.94 ?  282 ILE D N     1 
ATOM   15673 C  CA    . ILE D 2 303 ? 151.493 112.900 139.449 1.00 33.00 ?  282 ILE D CA    1 
ATOM   15674 C  C     . ILE D 2 303 ? 152.156 113.487 138.195 1.00 31.59 ?  282 ILE D C     1 
ATOM   15675 O  O     . ILE D 2 303 ? 151.909 114.640 137.836 1.00 31.14 ?  282 ILE D O     1 
ATOM   15676 C  CB    . ILE D 2 303 ? 150.262 111.997 139.117 1.00 33.44 ?  282 ILE D CB    1 
ATOM   15677 C  CG1   . ILE D 2 303 ? 150.321 111.448 137.687 1.00 34.29 ?  282 ILE D CG1   1 
ATOM   15678 C  CG2   . ILE D 2 303 ? 148.963 112.743 139.373 1.00 35.47 ?  282 ILE D CG2   1 
ATOM   15679 C  CD1   . ILE D 2 303 ? 149.060 110.733 137.243 1.00 36.30 ?  282 ILE D CD1   1 
ATOM   15680 N  N     . ASN D 2 304 ? 153.016 112.693 137.556 1.00 29.53 ?  283 ASN D N     1 
ATOM   15681 C  CA    . ASN D 2 304 ? 153.651 113.086 136.301 1.00 28.49 ?  283 ASN D CA    1 
ATOM   15682 C  C     . ASN D 2 304 ? 152.629 113.691 135.314 1.00 27.87 ?  283 ASN D C     1 
ATOM   15683 O  O     . ASN D 2 304 ? 151.622 113.057 135.003 1.00 27.02 ?  283 ASN D O     1 
ATOM   15684 C  CB    . ASN D 2 304 ? 154.355 111.882 135.672 1.00 28.20 ?  283 ASN D CB    1 
ATOM   15685 C  CG    . ASN D 2 304 ? 155.109 112.246 134.420 1.00 28.17 ?  283 ASN D CG    1 
ATOM   15686 O  OD1   . ASN D 2 304 ? 154.538 112.278 133.335 1.00 29.01 ?  283 ASN D OD1   1 
ATOM   15687 N  ND2   . ASN D 2 304 ? 156.395 112.522 134.560 1.00 27.24 ?  283 ASN D ND2   1 
ATOM   15688 N  N     . PRO D 2 305 ? 152.881 114.926 134.834 1.00 28.00 ?  284 PRO D N     1 
ATOM   15689 C  CA    . PRO D 2 305 ? 151.900 115.619 133.983 1.00 27.58 ?  284 PRO D CA    1 
ATOM   15690 C  C     . PRO D 2 305 ? 151.665 114.968 132.619 1.00 27.01 ?  284 PRO D C     1 
ATOM   15691 O  O     . PRO D 2 305 ? 150.601 115.147 132.035 1.00 26.66 ?  284 PRO D O     1 
ATOM   15692 C  CB    . PRO D 2 305 ? 152.498 117.021 133.810 1.00 28.21 ?  284 PRO D CB    1 
ATOM   15693 C  CG    . PRO D 2 305 ? 153.923 116.887 134.123 1.00 28.80 ?  284 PRO D CG    1 
ATOM   15694 C  CD    . PRO D 2 305 ? 154.013 115.807 135.178 1.00 28.11 ?  284 PRO D CD    1 
ATOM   15695 N  N     . ILE D 2 306 ? 152.644 114.219 132.121 1.00 26.52 ?  285 ILE D N     1 
ATOM   15696 C  CA    . ILE D 2 306 ? 152.484 113.515 130.854 1.00 26.50 ?  285 ILE D CA    1 
ATOM   15697 C  C     . ILE D 2 306 ? 151.479 112.366 131.017 1.00 26.43 ?  285 ILE D C     1 
ATOM   15698 O  O     . ILE D 2 306 ? 150.543 112.215 130.218 1.00 26.00 ?  285 ILE D O     1 
ATOM   15699 C  CB    . ILE D 2 306 ? 153.842 113.030 130.287 1.00 26.88 ?  285 ILE D CB    1 
ATOM   15700 C  CG1   . ILE D 2 306 ? 154.763 114.239 130.039 1.00 26.98 ?  285 ILE D CG1   1 
ATOM   15701 C  CG2   . ILE D 2 306 ? 153.616 112.215 129.014 1.00 24.94 ?  285 ILE D CG2   1 
ATOM   15702 C  CD1   . ILE D 2 306 ? 156.179 113.896 129.665 1.00 26.65 ?  285 ILE D CD1   1 
ATOM   15703 N  N     . VAL D 2 307 ? 151.660 111.585 132.076 1.00 26.36 ?  286 VAL D N     1 
ATOM   15704 C  CA    . VAL D 2 307 ? 150.693 110.561 132.450 1.00 26.71 ?  286 VAL D CA    1 
ATOM   15705 C  C     . VAL D 2 307 ? 149.314 111.163 132.739 1.00 27.68 ?  286 VAL D C     1 
ATOM   15706 O  O     . VAL D 2 307 ? 148.307 110.608 132.299 1.00 27.92 ?  286 VAL D O     1 
ATOM   15707 C  CB    . VAL D 2 307 ? 151.213 109.681 133.619 1.00 26.37 ?  286 VAL D CB    1 
ATOM   15708 C  CG1   . VAL D 2 307 ? 150.107 108.772 134.179 1.00 25.48 ?  286 VAL D CG1   1 
ATOM   15709 C  CG2   . VAL D 2 307 ? 152.353 108.847 133.131 1.00 25.55 ?  286 VAL D CG2   1 
ATOM   15710 N  N     . LEU D 2 308 ? 149.262 112.304 133.431 1.00 28.80 ?  287 LEU D N     1 
ATOM   15711 C  CA    . LEU D 2 308 ? 147.980 113.000 133.633 1.00 30.07 ?  287 LEU D CA    1 
ATOM   15712 C  C     . LEU D 2 308 ? 147.298 113.371 132.312 1.00 30.38 ?  287 LEU D C     1 
ATOM   15713 O  O     . LEU D 2 308 ? 146.080 113.221 132.164 1.00 30.71 ?  287 LEU D O     1 
ATOM   15714 C  CB    . LEU D 2 308 ? 148.145 114.247 134.507 1.00 30.86 ?  287 LEU D CB    1 
ATOM   15715 C  CG    . LEU D 2 308 ? 148.121 114.008 136.020 1.00 32.62 ?  287 LEU D CG    1 
ATOM   15716 C  CD1   . LEU D 2 308 ? 148.497 115.268 136.768 1.00 33.97 ?  287 LEU D CD1   1 
ATOM   15717 C  CD2   . LEU D 2 308 ? 146.749 113.486 136.488 1.00 34.73 ?  287 LEU D CD2   1 
ATOM   15718 N  N     . ASN D 2 309 ? 148.081 113.844 131.349 1.00 30.81 ?  288 ASN D N     1 
ATOM   15719 C  CA    . ASN D 2 309 ? 147.540 114.180 130.037 1.00 31.25 ?  288 ASN D CA    1 
ATOM   15720 C  C     . ASN D 2 309 ? 146.999 112.945 129.315 1.00 31.83 ?  288 ASN D C     1 
ATOM   15721 O  O     . ASN D 2 309 ? 146.008 113.029 128.584 1.00 31.73 ?  288 ASN D O     1 
ATOM   15722 C  CB    . ASN D 2 309 ? 148.570 114.918 129.174 1.00 31.21 ?  288 ASN D CB    1 
ATOM   15723 C  CG    . ASN D 2 309 ? 147.967 115.451 127.885 1.00 31.41 ?  288 ASN D CG    1 
ATOM   15724 O  OD1   . ASN D 2 309 ? 146.871 116.023 127.891 1.00 31.88 ?  288 ASN D OD1   1 
ATOM   15725 N  ND2   . ASN D 2 309 ? 148.672 115.263 126.774 1.00 29.12 ?  288 ASN D ND2   1 
ATOM   15726 N  N     . GLY D 2 310 ? 147.651 111.802 129.534 1.00 32.04 ?  289 GLY D N     1 
ATOM   15727 C  CA    . GLY D 2 310 ? 147.161 110.520 129.041 1.00 33.04 ?  289 GLY D CA    1 
ATOM   15728 C  C     . GLY D 2 310 ? 145.847 110.132 129.706 1.00 33.85 ?  289 GLY D C     1 
ATOM   15729 O  O     . GLY D 2 310 ? 144.896 109.748 129.026 1.00 34.05 ?  289 GLY D O     1 
ATOM   15730 N  N     . LEU D 2 311 ? 145.798 110.238 131.033 1.00 34.33 ?  290 LEU D N     1 
ATOM   15731 C  CA    . LEU D 2 311 ? 144.612 109.882 131.817 1.00 35.77 ?  290 LEU D CA    1 
ATOM   15732 C  C     . LEU D 2 311 ? 143.386 110.723 131.475 1.00 37.01 ?  290 LEU D C     1 
ATOM   15733 O  O     . LEU D 2 311 ? 142.272 110.204 131.403 1.00 37.18 ?  290 LEU D O     1 
ATOM   15734 C  CB    . LEU D 2 311 ? 144.895 110.022 133.318 1.00 35.50 ?  290 LEU D CB    1 
ATOM   15735 C  CG    . LEU D 2 311 ? 145.433 108.857 134.143 1.00 35.45 ?  290 LEU D CG    1 
ATOM   15736 C  CD1   . LEU D 2 311 ? 145.791 109.359 135.552 1.00 35.28 ?  290 LEU D CD1   1 
ATOM   15737 C  CD2   . LEU D 2 311 ? 144.440 107.695 134.226 1.00 34.16 ?  290 LEU D CD2   1 
ATOM   15738 N  N     . LYS D 2 330 ? 117.517 118.911 149.920 1.00 61.72 ?  309 LYS D N     1 
ATOM   15739 C  CA    . LYS D 2 330 ? 116.219 118.250 149.924 1.00 61.83 ?  309 LYS D CA    1 
ATOM   15740 C  C     . LYS D 2 330 ? 115.871 117.743 151.316 1.00 62.21 ?  309 LYS D C     1 
ATOM   15741 O  O     . LYS D 2 330 ? 116.118 116.578 151.628 1.00 61.32 ?  309 LYS D O     1 
ATOM   15742 C  CB    . LYS D 2 330 ? 116.204 117.076 148.941 1.00 59.60 ?  309 LYS D CB    1 
ATOM   15743 C  CG    . LYS D 2 330 ? 116.785 117.371 147.572 1.00 60.95 ?  309 LYS D CG    1 
ATOM   15744 C  CD    . LYS D 2 330 ? 115.766 117.111 146.473 1.00 60.77 ?  309 LYS D CD    1 
ATOM   15745 C  CE    . LYS D 2 330 ? 116.190 117.752 145.163 1.00 61.40 ?  309 LYS D CE    1 
ATOM   15746 N  NZ    . LYS D 2 330 ? 115.380 118.957 144.840 1.00 62.04 1  309 LYS D NZ    1 
ATOM   15747 N  N     . ALA D 2 331 ? 115.309 118.602 152.166 1.00 57.72 ?  310 ALA D N     1 
ATOM   15748 C  CA    . ALA D 2 331 ? 114.919 118.145 153.492 1.00 58.04 ?  310 ALA D CA    1 
ATOM   15749 C  C     . ALA D 2 331 ? 113.563 117.449 153.490 1.00 58.14 ?  310 ALA D C     1 
ATOM   15750 O  O     . ALA D 2 331 ? 113.499 116.230 153.676 1.00 58.87 ?  310 ALA D O     1 
ATOM   15751 C  CB    . ALA D 2 331 ? 114.898 119.326 154.470 1.00 56.57 ?  310 ALA D CB    1 
ATOM   15752 N  N     . THR D 2 332 ? 112.479 118.199 153.276 1.00 46.15 ?  311 THR D N     1 
ATOM   15753 C  CA    . THR D 2 332 ? 111.167 117.644 152.959 1.00 42.78 ?  311 THR D CA    1 
ATOM   15754 C  C     . THR D 2 332 ? 110.215 118.746 152.502 1.00 42.27 ?  311 THR D C     1 
ATOM   15755 O  O     . THR D 2 332 ? 109.888 119.649 153.281 1.00 45.09 ?  311 THR D O     1 
ATOM   15756 C  CB    . THR D 2 332 ? 110.591 116.872 154.153 1.00 46.86 ?  311 THR D CB    1 
ATOM   15757 O  OG1   . THR D 2 332 ? 109.408 116.164 153.757 1.00 46.97 ?  311 THR D OG1   1 
ATOM   15758 C  CG2   . THR D 2 332 ? 110.306 117.792 155.323 1.00 43.65 ?  311 THR D CG2   1 
ATOM   15759 N  N     . VAL D 2 333 ? 109.763 118.688 151.251 1.00 39.49 ?  312 VAL D N     1 
ATOM   15760 C  CA    . VAL D 2 333 ? 108.819 119.673 150.735 1.00 35.97 ?  312 VAL D CA    1 
ATOM   15761 C  C     . VAL D 2 333 ? 107.476 119.502 151.434 1.00 40.19 ?  312 VAL D C     1 
ATOM   15762 O  O     . VAL D 2 333 ? 106.901 118.407 151.437 1.00 43.38 ?  312 VAL D O     1 
ATOM   15763 C  CB    . VAL D 2 333 ? 108.665 119.555 149.207 1.00 38.60 ?  312 VAL D CB    1 
ATOM   15764 C  CG1   . VAL D 2 333 ? 107.336 120.143 148.752 1.00 39.63 ?  312 VAL D CG1   1 
ATOM   15765 C  CG2   . VAL D 2 333 ? 109.824 120.239 148.502 1.00 39.03 ?  312 VAL D CG2   1 
ATOM   15766 N  N     . GLU D 2 334 ? 106.971 120.577 152.037 1.00 39.20 ?  313 GLU D N     1 
ATOM   15767 C  CA    . GLU D 2 334 ? 105.643 120.585 152.643 1.00 36.81 ?  313 GLU D CA    1 
ATOM   15768 C  C     . GLU D 2 334 ? 104.932 121.859 152.205 1.00 37.73 ?  313 GLU D C     1 
ATOM   15769 O  O     . GLU D 2 334 ? 105.522 122.955 152.294 1.00 40.12 ?  313 GLU D O     1 
ATOM   15770 C  CB    . GLU D 2 334 ? 105.711 120.494 154.168 1.00 34.61 ?  313 GLU D CB    1 
ATOM   15771 C  CG    . GLU D 2 334 ? 104.347 120.326 154.819 1.00 37.90 ?  313 GLU D CG    1 
ATOM   15772 C  CD    . GLU D 2 334 ? 104.413 120.210 156.328 1.00 39.43 ?  313 GLU D CD    1 
ATOM   15773 O  OE1   . GLU D 2 334 ? 105.530 120.139 156.873 1.00 37.54 ?  313 GLU D OE1   1 
ATOM   15774 O  OE2   . GLU D 2 334 ? 103.343 120.185 156.971 1.00 39.69 -1 313 GLU D OE2   1 
ATOM   15775 N  N     . PRO D 2 335 ? 103.694 121.776 151.726 1.00 38.18 ?  314 PRO D N     1 
ATOM   15776 C  CA    . PRO D 2 335 ? 103.000 122.982 151.265 1.00 40.62 ?  314 PRO D CA    1 
ATOM   15777 C  C     . PRO D 2 335 ? 102.603 123.891 152.417 1.00 40.02 ?  314 PRO D C     1 
ATOM   15778 O  O     . PRO D 2 335 ? 102.444 123.458 153.560 1.00 41.11 ?  314 PRO D O     1 
ATOM   15779 C  CB    . PRO D 2 335 ? 101.765 122.424 150.551 1.00 37.91 ?  314 PRO D CB    1 
ATOM   15780 C  CG    . PRO D 2 335 ? 101.516 121.117 151.226 1.00 34.58 ?  314 PRO D CG    1 
ATOM   15781 C  CD    . PRO D 2 335 ? 102.878 120.564 151.539 1.00 36.60 ?  314 PRO D CD    1 
ATOM   15782 N  N     . LEU D 2 336 ? 102.452 125.174 152.098 1.00 34.57 ?  315 LEU D N     1 
ATOM   15783 C  CA    . LEU D 2 336 ? 101.898 126.134 153.042 1.00 30.08 ?  315 LEU D CA    1 
ATOM   15784 C  C     . LEU D 2 336 ? 100.384 125.978 153.082 1.00 33.20 ?  315 LEU D C     1 
ATOM   15785 O  O     . LEU D 2 336 ? 99.705  126.173 152.069 1.00 37.22 ?  315 LEU D O     1 
ATOM   15786 C  CB    . LEU D 2 336 ? 102.279 127.559 152.640 1.00 28.04 ?  315 LEU D CB    1 
ATOM   15787 C  CG    . LEU D 2 336 ? 103.696 128.022 152.980 1.00 27.76 ?  315 LEU D CG    1 
ATOM   15788 C  CD1   . LEU D 2 336 ? 104.129 129.139 152.044 1.00 24.11 ?  315 LEU D CD1   1 
ATOM   15789 C  CD2   . LEU D 2 336 ? 103.772 128.474 154.426 1.00 29.08 ?  315 LEU D CD2   1 
ATOM   15790 N  N     . LYS D 2 337 ? 99.854  125.629 154.253 1.00 36.25 ?  316 LYS D N     1 
ATOM   15791 C  CA    . LYS D 2 337 ? 98.447  125.273 154.400 1.00 47.76 ?  316 LYS D CA    1 
ATOM   15792 C  C     . LYS D 2 337 ? 97.647  126.385 155.068 1.00 47.26 ?  316 LYS D C     1 
ATOM   15793 O  O     . LYS D 2 337 ? 96.723  126.112 155.838 1.00 51.37 ?  316 LYS D O     1 
ATOM   15794 C  CB    . LYS D 2 337 ? 98.303  123.970 155.184 1.00 44.37 ?  316 LYS D CB    1 
ATOM   15795 C  CG    . LYS D 2 337 ? 99.260  123.851 156.358 1.00 46.03 ?  316 LYS D CG    1 
ATOM   15796 C  CD    . LYS D 2 337 ? 99.697  122.413 156.576 1.00 46.40 ?  316 LYS D CD    1 
ATOM   15797 C  CE    . LYS D 2 337 ? 100.238 121.802 155.294 1.00 45.29 ?  316 LYS D CE    1 
ATOM   15798 N  NZ    . LYS D 2 337 ? 101.085 120.609 155.561 1.00 42.09 1  316 LYS D NZ    1 
ATOM   15799 N  N     . ASP D 2 338 ? 98.000  127.640 154.782 1.00 29.55 ?  317 ASP D N     1 
ATOM   15800 C  CA    . ASP D 2 338 ? 97.358  128.816 155.365 1.00 32.48 ?  317 ASP D CA    1 
ATOM   15801 C  C     . ASP D 2 338 ? 97.521  128.854 156.880 1.00 37.94 ?  317 ASP D C     1 
ATOM   15802 O  O     . ASP D 2 338 ? 97.977  127.881 157.490 1.00 40.84 ?  317 ASP D O     1 
ATOM   15803 C  CB    . ASP D 2 338 ? 95.877  128.876 154.985 1.00 36.01 ?  317 ASP D CB    1 
ATOM   15804 C  CG    . ASP D 2 338 ? 95.349  130.294 154.935 1.00 38.86 ?  317 ASP D CG    1 
ATOM   15805 O  OD1   . ASP D 2 338 ? 96.147  131.229 155.155 1.00 36.19 ?  317 ASP D OD1   1 
ATOM   15806 O  OD2   . ASP D 2 338 ? 94.141  130.474 154.676 1.00 34.94 -1 317 ASP D OD2   1 
ATOM   15807 N  N     . ASP D 2 339 ? 97.200  130.003 157.483 1.00 32.37 ?  318 ASP D N     1 
ATOM   15808 C  CA    . ASP D 2 339 ? 97.391  130.260 158.909 1.00 28.49 ?  318 ASP D CA    1 
ATOM   15809 C  C     . ASP D 2 339 ? 98.877  130.312 159.247 1.00 28.80 ?  318 ASP D C     1 
ATOM   15810 O  O     . ASP D 2 339 ? 99.252  130.595 160.389 1.00 36.28 ?  318 ASP D O     1 
ATOM   15811 C  CB    . ASP D 2 339 ? 96.672  129.218 159.770 1.00 30.55 ?  318 ASP D CB    1 
ATOM   15812 C  CG    . ASP D 2 339 ? 95.813  129.847 160.849 1.00 37.05 ?  318 ASP D CG    1 
ATOM   15813 O  OD1   . ASP D 2 339 ? 96.182  130.931 161.347 1.00 32.14 ?  318 ASP D OD1   1 
ATOM   15814 O  OD2   . ASP D 2 339 ? 94.768  129.258 161.199 1.00 39.30 -1 318 ASP D OD2   1 
ATOM   15815 N  N     . ASP D 2 340 ? 99.726  130.040 158.258 1.00 24.72 ?  319 ASP D N     1 
ATOM   15816 C  CA    . ASP D 2 340 ? 101.155 130.287 158.352 1.00 24.52 ?  319 ASP D CA    1 
ATOM   15817 C  C     . ASP D 2 340 ? 101.513 131.714 157.973 1.00 21.51 ?  319 ASP D C     1 
ATOM   15818 O  O     . ASP D 2 340 ? 102.650 132.137 158.198 1.00 32.71 ?  319 ASP D O     1 
ATOM   15819 C  CB    . ASP D 2 340 ? 101.920 129.310 157.455 1.00 23.05 ?  319 ASP D CB    1 
ATOM   15820 C  CG    . ASP D 2 340 ? 101.821 127.876 157.936 1.00 28.00 ?  319 ASP D CG    1 
ATOM   15821 O  OD1   . ASP D 2 340 ? 101.713 127.663 159.162 1.00 34.28 ?  319 ASP D OD1   1 
ATOM   15822 O  OD2   . ASP D 2 340 ? 101.851 126.960 157.089 1.00 31.08 -1 319 ASP D OD2   1 
ATOM   15823 N  N     . PHE D 2 341 ? 100.567 132.455 157.399 1.00 10.52 ?  320 PHE D N     1 
ATOM   15824 C  CA    . PHE D 2 341 ? 100.732 133.862 157.078 1.00 15.27 ?  320 PHE D CA    1 
ATOM   15825 C  C     . PHE D 2 341 ? 100.176 134.769 158.162 1.00 12.85 ?  320 PHE D C     1 
ATOM   15826 O  O     . PHE D 2 341 ? 100.220 135.994 158.013 1.00 22.40 ?  320 PHE D O     1 
ATOM   15827 C  CB    . PHE D 2 341 ? 100.050 134.179 155.743 1.00 21.01 ?  320 PHE D CB    1 
ATOM   15828 C  CG    . PHE D 2 341 ? 100.621 133.428 154.573 1.00 15.79 ?  320 PHE D CG    1 
ATOM   15829 C  CD1   . PHE D 2 341 ? 100.187 132.147 154.280 1.00 11.88 ?  320 PHE D CD1   1 
ATOM   15830 C  CD2   . PHE D 2 341 ? 101.581 134.005 153.763 1.00 9.87  ?  320 PHE D CD2   1 
ATOM   15831 C  CE1   . PHE D 2 341 ? 100.707 131.455 153.207 1.00 13.02 ?  320 PHE D CE1   1 
ATOM   15832 C  CE2   . PHE D 2 341 ? 102.103 133.317 152.687 1.00 10.78 ?  320 PHE D CE2   1 
ATOM   15833 C  CZ    . PHE D 2 341 ? 101.667 132.040 152.410 1.00 4.79  ?  320 PHE D CZ    1 
ATOM   15834 N  N     . TYR D 2 342 ? 99.654  134.198 159.244 1.00 12.46 ?  321 TYR D N     1 
ATOM   15835 C  CA    . TYR D 2 342 ? 99.057  134.953 160.333 1.00 17.95 ?  321 TYR D CA    1 
ATOM   15836 C  C     . TYR D 2 342 ? 99.743  134.571 161.634 1.00 22.41 ?  321 TYR D C     1 
ATOM   15837 O  O     . TYR D 2 342 ? 100.061 133.398 161.855 1.00 24.04 ?  321 TYR D O     1 
ATOM   15838 C  CB    . TYR D 2 342 ? 97.553  134.685 160.431 1.00 13.28 ?  321 TYR D CB    1 
ATOM   15839 C  CG    . TYR D 2 342 ? 96.780  135.122 159.209 1.00 11.63 ?  321 TYR D CG    1 
ATOM   15840 C  CD1   . TYR D 2 342 ? 96.365  136.438 159.058 1.00 16.81 ?  321 TYR D CD1   1 
ATOM   15841 C  CD2   . TYR D 2 342 ? 96.473  134.219 158.201 1.00 15.94 ?  321 TYR D CD2   1 
ATOM   15842 C  CE1   . TYR D 2 342 ? 95.661  136.840 157.940 1.00 20.80 ?  321 TYR D CE1   1 
ATOM   15843 C  CE2   . TYR D 2 342 ? 95.770  134.611 157.080 1.00 15.55 ?  321 TYR D CE2   1 
ATOM   15844 C  CZ    . TYR D 2 342 ? 95.366  135.923 156.954 1.00 24.69 ?  321 TYR D CZ    1 
ATOM   15845 O  OH    . TYR D 2 342 ? 94.664  136.320 155.839 1.00 21.45 ?  321 TYR D OH    1 
ATOM   15846 N  N     . PHE D 2 343 ? 99.976  135.562 162.486 1.00 12.93 ?  322 PHE D N     1 
ATOM   15847 C  CA    . PHE D 2 343 ? 100.693 135.340 163.736 1.00 18.66 ?  322 PHE D CA    1 
ATOM   15848 C  C     . PHE D 2 343 ? 100.027 136.080 164.889 1.00 24.79 ?  322 PHE D C     1 
ATOM   15849 O  O     . PHE D 2 343 ? 99.713  137.265 164.784 1.00 23.91 ?  322 PHE D O     1 
ATOM   15850 C  CB    . PHE D 2 343 ? 102.155 135.780 163.598 1.00 13.99 ?  322 PHE D CB    1 
ATOM   15851 C  CG    . PHE D 2 343 ? 102.805 135.328 162.321 1.00 14.21 ?  322 PHE D CG    1 
ATOM   15852 C  CD1   . PHE D 2 343 ? 102.764 136.120 161.186 1.00 13.48 ?  322 PHE D CD1   1 
ATOM   15853 C  CD2   . PHE D 2 343 ? 103.454 134.108 162.254 1.00 16.65 ?  322 PHE D CD2   1 
ATOM   15854 C  CE1   . PHE D 2 343 ? 103.355 135.702 160.012 1.00 9.34  ?  322 PHE D CE1   1 
ATOM   15855 C  CE2   . PHE D 2 343 ? 104.046 133.687 161.082 1.00 9.50  ?  322 PHE D CE2   1 
ATOM   15856 C  CZ    . PHE D 2 343 ? 103.997 134.485 159.962 1.00 5.03  ?  322 PHE D CZ    1 
HETATM 15857 P  PA    . TTP E 3 .   ? 146.039 144.851 134.418 1.00 19.37 ?  801 TTP A PA    1 
HETATM 15858 O  O1A   . TTP E 3 .   ? 144.618 145.336 134.310 1.00 21.91 -1 801 TTP A O1A   1 
HETATM 15859 O  O2A   . TTP E 3 .   ? 146.941 145.626 133.491 1.00 26.56 ?  801 TTP A O2A   1 
HETATM 15860 O  O3A   . TTP E 3 .   ? 146.535 144.886 135.946 1.00 35.02 ?  801 TTP A O3A   1 
HETATM 15861 P  PB    . TTP E 3 .   ? 147.644 145.931 136.456 1.00 29.77 ?  801 TTP A PB    1 
HETATM 15862 O  O1B   . TTP E 3 .   ? 147.299 146.395 137.847 1.00 33.96 -1 801 TTP A O1B   1 
HETATM 15863 O  O2B   . TTP E 3 .   ? 147.807 147.116 135.539 1.00 25.37 ?  801 TTP A O2B   1 
HETATM 15864 O  O3B   . TTP E 3 .   ? 148.948 144.990 136.467 1.00 28.38 ?  801 TTP A O3B   1 
HETATM 15865 P  PG    . TTP E 3 .   ? 150.308 145.405 135.716 1.00 32.16 ?  801 TTP A PG    1 
HETATM 15866 O  O1G   . TTP E 3 .   ? 150.001 145.921 134.332 1.00 33.52 ?  801 TTP A O1G   1 
HETATM 15867 O  O2G   . TTP E 3 .   ? 151.190 144.188 135.607 1.00 23.47 -1 801 TTP A O2G   1 
HETATM 15868 O  O3G   . TTP E 3 .   ? 151.027 146.473 136.501 1.00 34.78 ?  801 TTP A O3G   1 
HETATM 15869 O  "O5'" . TTP E 3 .   ? 146.135 143.286 134.088 1.00 18.77 ?  801 TTP A "O5'" 1 
HETATM 15870 C  "C5'" . TTP E 3 .   ? 147.052 142.860 133.088 1.00 25.04 ?  801 TTP A "C5'" 1 
HETATM 15871 C  "C4'" . TTP E 3 .   ? 146.816 141.397 132.755 1.00 26.93 ?  801 TTP A "C4'" 1 
HETATM 15872 O  "O4'" . TTP E 3 .   ? 146.478 140.677 133.938 1.00 30.38 ?  801 TTP A "O4'" 1 
HETATM 15873 C  "C3'" . TTP E 3 .   ? 145.656 141.243 131.793 1.00 25.75 ?  801 TTP A "C3'" 1 
HETATM 15874 O  "O3'" . TTP E 3 .   ? 146.133 140.893 130.492 1.00 30.86 ?  801 TTP A "O3'" 1 
HETATM 15875 C  "C2'" . TTP E 3 .   ? 144.811 140.119 132.352 1.00 28.56 ?  801 TTP A "C2'" 1 
HETATM 15876 C  "C1'" . TTP E 3 .   ? 145.472 139.704 133.657 1.00 25.58 ?  801 TTP A "C1'" 1 
HETATM 15877 N  N1    . TTP E 3 .   ? 144.482 139.681 134.733 1.00 26.58 ?  801 TTP A N1    1 
HETATM 15878 C  C2    . TTP E 3 .   ? 143.891 138.455 135.108 1.00 30.61 ?  801 TTP A C2    1 
HETATM 15879 O  O2    . TTP E 3 .   ? 144.227 137.409 134.516 1.00 27.38 ?  801 TTP A O2    1 
HETATM 15880 N  N3    . TTP E 3 .   ? 142.983 138.387 136.089 1.00 28.52 ?  801 TTP A N3    1 
HETATM 15881 C  C4    . TTP E 3 .   ? 142.609 139.491 136.739 1.00 31.97 ?  801 TTP A C4    1 
HETATM 15882 O  O4    . TTP E 3 .   ? 141.762 139.430 137.653 1.00 33.14 ?  801 TTP A O4    1 
HETATM 15883 C  C5    . TTP E 3 .   ? 143.213 140.790 136.362 1.00 26.42 ?  801 TTP A C5    1 
HETATM 15884 C  C5M   . TTP E 3 .   ? 142.818 142.054 137.073 1.00 26.94 ?  801 TTP A C5M   1 
HETATM 15885 C  C6    . TTP E 3 .   ? 144.151 140.821 135.343 1.00 25.12 ?  801 TTP A C6    1 
HETATM 15886 MG MG    . MG  F 4 .   ? 148.235 147.166 133.106 1.00 24.14 ?  802 MG  A MG    1 
HETATM 15887 P  PG    . ATP G 5 .   ? 108.733 133.427 78.164  1.00 73.57 ?  803 ATP A PG    1 
HETATM 15888 O  O1G   . ATP G 5 .   ? 109.204 134.315 77.063  1.00 63.77 ?  803 ATP A O1G   1 
HETATM 15889 O  O2G   . ATP G 5 .   ? 108.204 132.074 77.679  1.00 64.13 -1 803 ATP A O2G   1 
HETATM 15890 O  O3G   . ATP G 5 .   ? 109.780 133.194 79.257  1.00 61.47 ?  803 ATP A O3G   1 
HETATM 15891 P  PB    . ATP G 5 .   ? 107.187 134.933 80.244  1.00 71.75 ?  803 ATP A PB    1 
HETATM 15892 O  O1B   . ATP G 5 .   ? 107.999 136.165 80.309  1.00 63.94 -1 803 ATP A O1B   1 
HETATM 15893 O  O2B   . ATP G 5 .   ? 105.674 135.143 80.307  1.00 62.90 ?  803 ATP A O2B   1 
HETATM 15894 O  O3B   . ATP G 5 .   ? 107.494 134.091 78.930  1.00 66.82 ?  803 ATP A O3B   1 
HETATM 15895 P  PA    . ATP G 5 .   ? 106.816 132.829 82.298  1.00 70.68 ?  803 ATP A PA    1 
HETATM 15896 O  O1A   . ATP G 5 .   ? 107.459 131.502 82.225  1.00 64.00 -1 803 ATP A O1A   1 
HETATM 15897 O  O2A   . ATP G 5 .   ? 105.344 132.847 81.888  1.00 62.49 ?  803 ATP A O2A   1 
HETATM 15898 O  O3A   . ATP G 5 .   ? 107.574 133.900 81.393  1.00 63.22 ?  803 ATP A O3A   1 
HETATM 15899 O  "O5'" . ATP G 5 .   ? 106.934 133.453 83.744  1.00 62.47 ?  803 ATP A "O5'" 1 
HETATM 15900 C  "C5'" . ATP G 5 .   ? 106.055 134.514 84.174  1.00 61.67 ?  803 ATP A "C5'" 1 
HETATM 15901 C  "C4'" . ATP G 5 .   ? 106.765 135.349 85.209  1.00 61.88 ?  803 ATP A "C4'" 1 
HETATM 15902 O  "O4'" . ATP G 5 .   ? 107.250 134.497 86.269  1.00 63.84 ?  803 ATP A "O4'" 1 
HETATM 15903 C  "C3'" . ATP G 5 .   ? 107.993 136.099 84.709  1.00 60.84 ?  803 ATP A "C3'" 1 
HETATM 15904 O  "O3'" . ATP G 5 .   ? 107.631 137.362 84.161  1.00 63.01 ?  803 ATP A "O3'" 1 
HETATM 15905 C  "C2'" . ATP G 5 .   ? 108.818 136.258 85.985  1.00 62.28 ?  803 ATP A "C2'" 1 
HETATM 15906 O  "O2'" . ATP G 5 .   ? 108.378 137.365 86.762  1.00 61.13 ?  803 ATP A "O2'" 1 
HETATM 15907 C  "C1'" . ATP G 5 .   ? 108.522 134.941 86.711  1.00 61.93 ?  803 ATP A "C1'" 1 
HETATM 15908 N  N9    . ATP G 5 .   ? 109.494 133.885 86.454  1.00 60.22 ?  803 ATP A N9    1 
HETATM 15909 C  C8    . ATP G 5 .   ? 109.252 132.654 85.902  1.00 60.42 ?  803 ATP A C8    1 
HETATM 15910 N  N7    . ATP G 5 .   ? 110.318 131.899 85.787  1.00 60.85 ?  803 ATP A N7    1 
HETATM 15911 C  C5    . ATP G 5 .   ? 111.335 132.688 86.303  1.00 61.63 ?  803 ATP A C5    1 
HETATM 15912 C  C6    . ATP G 5 .   ? 112.716 132.469 86.471  1.00 58.03 ?  803 ATP A C6    1 
HETATM 15913 N  N6    . ATP G 5 .   ? 113.339 131.340 86.120  1.00 57.72 ?  803 ATP A N6    1 
HETATM 15914 N  N1    . ATP G 5 .   ? 113.446 133.463 87.020  1.00 58.44 ?  803 ATP A N1    1 
HETATM 15915 C  C2    . ATP G 5 .   ? 112.833 134.597 87.368  1.00 58.37 ?  803 ATP A C2    1 
HETATM 15916 N  N3    . ATP G 5 .   ? 111.542 134.914 87.263  1.00 61.94 ?  803 ATP A N3    1 
HETATM 15917 C  C4    . ATP G 5 .   ? 110.842 133.915 86.719  1.00 62.47 ?  803 ATP A C4    1 
HETATM 15918 O  O1B   . DGI H 6 .   ? 104.819 150.612 83.731  1.00 65.79 ?  804 DGI A O1B   1 
HETATM 15919 P  PB    . DGI H 6 .   ? 104.945 152.088 84.034  1.00 74.95 ?  804 DGI A PB    1 
HETATM 15920 O  O2B   . DGI H 6 .   ? 103.616 152.814 84.006  1.00 66.56 -1 804 DGI A O2B   1 
HETATM 15921 O  O3B   . DGI H 6 .   ? 106.006 152.776 83.202  1.00 66.82 ?  804 DGI A O3B   1 
HETATM 15922 O  O3A   . DGI H 6 .   ? 105.461 152.120 85.576  1.00 67.64 ?  804 DGI A O3A   1 
HETATM 15923 P  PA    . DGI H 6 .   ? 105.354 151.306 86.950  1.00 72.66 ?  804 DGI A PA    1 
HETATM 15924 O  O1A   . DGI H 6 .   ? 105.488 152.248 88.081  1.00 65.42 -1 804 DGI A O1A   1 
HETATM 15925 O  O2A   . DGI H 6 .   ? 104.173 150.413 86.889  1.00 66.08 ?  804 DGI A O2A   1 
HETATM 15926 O  "O5'" . DGI H 6 .   ? 106.683 150.425 86.893  1.00 64.30 ?  804 DGI A "O5'" 1 
HETATM 15927 C  "C5'" . DGI H 6 .   ? 107.948 151.052 86.602  1.00 63.95 ?  804 DGI A "C5'" 1 
HETATM 15928 C  "C4'" . DGI H 6 .   ? 109.062 150.081 86.900  1.00 63.55 ?  804 DGI A "C4'" 1 
HETATM 15929 O  "O4'" . DGI H 6 .   ? 108.989 149.669 88.284  1.00 62.06 ?  804 DGI A "O4'" 1 
HETATM 15930 C  "C3'" . DGI H 6 .   ? 109.045 148.799 86.059  1.00 64.87 ?  804 DGI A "C3'" 1 
HETATM 15931 O  "O3'" . DGI H 6 .   ? 110.348 148.525 85.546  1.00 62.86 ?  804 DGI A "O3'" 1 
HETATM 15932 C  "C2'" . DGI H 6 .   ? 108.621 147.724 87.053  1.00 62.93 ?  804 DGI A "C2'" 1 
HETATM 15933 C  "C1'" . DGI H 6 .   ? 109.153 148.269 88.363  1.00 59.66 ?  804 DGI A "C1'" 1 
HETATM 15934 N  N9    . DGI H 6 .   ? 108.432 147.788 89.557  1.00 62.34 ?  804 DGI A N9    1 
HETATM 15935 C  C8    . DGI H 6 .   ? 108.972 147.180 90.658  1.00 63.25 ?  804 DGI A C8    1 
HETATM 15936 N  N7    . DGI H 6 .   ? 108.076 146.846 91.556  1.00 62.94 ?  804 DGI A N7    1 
HETATM 15937 C  C5    . DGI H 6 .   ? 106.873 147.261 91.013  1.00 64.85 ?  804 DGI A C5    1 
HETATM 15938 C  C4    . DGI H 6 .   ? 107.076 147.844 89.780  1.00 64.28 ?  804 DGI A C4    1 
HETATM 15939 N  N3    . DGI H 6 .   ? 106.159 148.370 88.948  1.00 64.32 ?  804 DGI A N3    1 
HETATM 15940 C  C2    . DGI H 6 .   ? 104.922 148.287 89.429  1.00 62.71 ?  804 DGI A C2    1 
HETATM 15941 N  N2    . DGI H 6 .   ? 103.901 148.769 88.716  1.00 63.01 ?  804 DGI A N2    1 
HETATM 15942 N  N1    . DGI H 6 .   ? 104.620 147.726 90.640  1.00 63.42 ?  804 DGI A N1    1 
HETATM 15943 C  C6    . DGI H 6 .   ? 105.539 147.179 91.515  1.00 64.23 ?  804 DGI A C6    1 
HETATM 15944 O  O6    . DGI H 6 .   ? 105.175 146.692 92.585  1.00 64.17 ?  804 DGI A O6    1 
HETATM 15945 P  PA    . TTP I 3 .   ? 119.600 147.514 124.103 1.00 22.87 ?  801 TTP B PA    1 
HETATM 15946 O  O1A   . TTP I 3 .   ? 120.961 147.020 123.689 1.00 21.90 -1 801 TTP B O1A   1 
HETATM 15947 O  O2A   . TTP I 3 .   ? 119.683 148.920 124.641 1.00 27.07 ?  801 TTP B O2A   1 
HETATM 15948 O  O3A   . TTP I 3 .   ? 118.550 147.439 122.888 1.00 36.80 ?  801 TTP B O3A   1 
HETATM 15949 P  PB    . TTP I 3 .   ? 118.519 148.529 121.707 1.00 32.44 ?  801 TTP B PB    1 
HETATM 15950 O  O1B   . TTP I 3 .   ? 119.347 148.072 120.535 1.00 35.04 -1 801 TTP B O1B   1 
HETATM 15951 O  O2B   . TTP I 3 .   ? 118.967 149.889 122.174 1.00 28.12 ?  801 TTP B O2B   1 
HETATM 15952 O  O3B   . TTP I 3 .   ? 116.959 148.547 121.324 1.00 37.21 ?  801 TTP B O3B   1 
HETATM 15953 P  PG    . TTP I 3 .   ? 115.857 148.833 122.461 1.00 30.08 ?  801 TTP B PG    1 
HETATM 15954 O  O1G   . TTP I 3 .   ? 115.376 147.516 123.012 1.00 20.36 ?  801 TTP B O1G   1 
HETATM 15955 O  O2G   . TTP I 3 .   ? 114.680 149.569 121.871 1.00 33.83 -1 801 TTP B O2G   1 
HETATM 15956 O  O3G   . TTP I 3 .   ? 116.467 149.651 123.573 1.00 27.09 ?  801 TTP B O3G   1 
HETATM 15957 O  "O5'" . TTP I 3 .   ? 118.931 146.531 125.182 1.00 24.10 ?  801 TTP B "O5'" 1 
HETATM 15958 C  "C5'" . TTP I 3 .   ? 118.180 145.406 124.738 1.00 22.09 ?  801 TTP B "C5'" 1 
HETATM 15959 C  "C4'" . TTP I 3 .   ? 118.067 144.397 125.869 1.00 23.21 ?  801 TTP B "C4'" 1 
HETATM 15960 O  "O4'" . TTP I 3 .   ? 118.131 143.092 125.296 1.00 35.77 ?  801 TTP B "O4'" 1 
HETATM 15961 C  "C3'" . TTP I 3 .   ? 119.226 144.539 126.836 1.00 25.49 ?  801 TTP B "C3'" 1 
HETATM 15962 O  "O3'" . TTP I 3 .   ? 118.735 144.694 128.168 1.00 27.76 ?  801 TTP B "O3'" 1 
HETATM 15963 C  "C2'" . TTP I 3 .   ? 120.022 143.256 126.735 1.00 25.02 ?  801 TTP B "C2'" 1 
HETATM 15964 C  "C1'" . TTP I 3 .   ? 119.218 142.336 125.830 1.00 28.60 ?  801 TTP B "C1'" 1 
HETATM 15965 N  N1    . TTP I 3 .   ? 120.052 141.853 124.731 1.00 27.06 ?  801 TTP B N1    1 
HETATM 15966 C  C2    . TTP I 3 .   ? 120.178 140.464 124.506 1.00 29.68 ?  801 TTP B C2    1 
HETATM 15967 O  O2    . TTP I 3 .   ? 119.574 139.665 125.252 1.00 27.86 ?  801 TTP B O2    1 
HETATM 15968 N  N3    . TTP I 3 .   ? 120.931 139.986 123.508 1.00 27.67 ?  801 TTP B N3    1 
HETATM 15969 C  C4    . TTP I 3 .   ? 121.586 140.818 122.696 1.00 32.29 ?  801 TTP B C4    1 
HETATM 15970 O  O4    . TTP I 3 .   ? 122.288 140.370 121.765 1.00 35.26 ?  801 TTP B O4    1 
HETATM 15971 C  C5    . TTP I 3 .   ? 121.469 142.279 122.912 1.00 27.29 ?  801 TTP B C5    1 
HETATM 15972 C  C5M   . TTP I 3 .   ? 122.191 143.249 122.018 1.00 27.10 ?  801 TTP B C5M   1 
HETATM 15973 C  C6    . TTP I 3 .   ? 120.681 142.737 123.953 1.00 25.61 ?  801 TTP B C6    1 
HETATM 15974 MG MG    . MG  J 4 .   ? 117.876 150.377 124.957 1.00 27.32 ?  802 MG  B MG    1 
HETATM 15975 P  PG    . ATP K 5 .   ? 154.997 139.672 179.549 1.00 78.28 ?  803 ATP B PG    1 
HETATM 15976 O  O1G   . ATP K 5 .   ? 154.782 140.197 180.927 1.00 64.48 ?  803 ATP B O1G   1 
HETATM 15977 O  O2G   . ATP K 5 .   ? 153.706 139.528 178.737 1.00 66.98 -1 803 ATP B O2G   1 
HETATM 15978 O  O3G   . ATP K 5 .   ? 156.013 140.478 178.733 1.00 64.37 ?  803 ATP B O3G   1 
HETATM 15979 P  PB    . ATP K 5 .   ? 156.957 137.452 179.980 1.00 74.62 ?  803 ATP B PB    1 
HETATM 15980 O  O1B   . ATP K 5 .   ? 158.098 137.940 179.181 1.00 63.94 -1 803 ATP B O1B   1 
HETATM 15981 O  O2B   . ATP K 5 .   ? 157.115 137.551 181.497 1.00 65.48 ?  803 ATP B O2B   1 
HETATM 15982 O  O3B   . ATP K 5 .   ? 155.606 138.196 179.599 1.00 67.90 ?  803 ATP B O3B   1 
HETATM 15983 P  PA    . ATP K 5 .   ? 155.840 135.159 178.482 1.00 74.99 ?  803 ATP B PA    1 
HETATM 15984 O  O1A   . ATP K 5 .   ? 154.488 134.747 178.911 1.00 65.28 -1 803 ATP B O1A   1 
HETATM 15985 O  O2A   . ATP K 5 .   ? 156.754 134.020 178.035 1.00 66.62 ?  803 ATP B O2A   1 
HETATM 15986 O  O3A   . ATP K 5 .   ? 156.599 135.939 179.640 1.00 66.93 ?  803 ATP B O3A   1 
HETATM 15987 O  "O5'" . ATP K 5 .   ? 155.773 136.226 177.320 1.00 63.34 ?  803 ATP B "O5'" 1 
HETATM 15988 C  "C5'" . ATP K 5 .   ? 156.816 136.319 176.328 1.00 62.23 ?  803 ATP B "C5'" 1 
HETATM 15989 C  "C4'" . ATP K 5 .   ? 156.343 137.204 175.204 1.00 64.37 ?  803 ATP B "C4'" 1 
HETATM 15990 O  "O4'" . ATP K 5 .   ? 155.580 136.421 174.261 1.00 66.78 ?  803 ATP B "O4'" 1 
HETATM 15991 C  "C3'" . ATP K 5 .   ? 155.417 138.342 175.617 1.00 61.93 ?  803 ATP B "C3'" 1 
HETATM 15992 O  "O3'" . ATP K 5 .   ? 156.160 139.491 176.004 1.00 65.20 ?  803 ATP B "O3'" 1 
HETATM 15993 C  "C2'" . ATP K 5 .   ? 154.621 138.594 174.336 1.00 61.89 ?  803 ATP B "C2'" 1 
HETATM 15994 O  "O2'" . ATP K 5 .   ? 155.331 139.426 173.428 1.00 64.23 ?  803 ATP B "O2'" 1 
HETATM 15995 C  "C1'" . ATP K 5 .   ? 154.485 137.177 173.770 1.00 63.64 ?  803 ATP B "C1'" 1 
HETATM 15996 N  N9    . ATP K 5 .   ? 153.250 136.496 174.144 1.00 61.39 ?  803 ATP B N9    1 
HETATM 15997 C  C8    . ATP K 5 .   ? 153.124 135.347 174.881 1.00 60.31 ?  803 ATP B C8    1 
HETATM 15998 N  N7    . ATP K 5 .   ? 151.885 134.959 175.061 1.00 61.85 ?  803 ATP B N7    1 
HETATM 15999 C  C5    . ATP K 5 .   ? 151.140 135.919 174.392 1.00 64.90 ?  803 ATP B C5    1 
HETATM 16000 C  C6    . ATP K 5 .   ? 149.756 136.085 174.201 1.00 60.15 ?  803 ATP B C6    1 
HETATM 16001 N  N6    . ATP K 5 .   ? 148.830 135.253 174.689 1.00 59.38 ?  803 ATP B N6    1 
HETATM 16002 N  N1    . ATP K 5 .   ? 149.344 137.152 173.483 1.00 59.56 ?  803 ATP B N1    1 
HETATM 16003 C  C2    . ATP K 5 .   ? 150.261 137.992 172.996 1.00 58.45 ?  803 ATP B C2    1 
HETATM 16004 N  N3    . ATP K 5 .   ? 151.589 137.936 173.108 1.00 61.55 ?  803 ATP B N3    1 
HETATM 16005 C  C4    . ATP K 5 .   ? 151.968 136.873 173.822 1.00 64.32 ?  803 ATP B C4    1 
HETATM 16006 O  O1B   . DGI L 6 .   ? 162.500 154.620 173.392 1.00 62.73 -1 804 DGI B O1B   1 
HETATM 16007 P  PB    . DGI L 6 .   ? 162.729 153.142 173.151 1.00 78.16 ?  804 DGI B PB    1 
HETATM 16008 O  O2B   . DGI L 6 .   ? 164.171 152.808 172.841 1.00 66.34 ?  804 DGI B O2B   1 
HETATM 16009 O  O3B   . DGI L 6 .   ? 162.140 152.273 174.242 1.00 63.38 ?  804 DGI B O3B   1 
HETATM 16010 O  O3A   . DGI L 6 .   ? 161.943 152.762 171.777 1.00 65.58 ?  804 DGI B O3A   1 
HETATM 16011 P  PA    . DGI L 6 .   ? 161.963 151.711 170.572 1.00 72.25 ?  804 DGI B PA    1 
HETATM 16012 O  O1A   . DGI L 6 .   ? 162.820 150.564 170.954 1.00 65.11 ?  804 DGI B O1A   1 
HETATM 16013 O  O2A   . DGI L 6 .   ? 162.240 152.430 169.311 1.00 63.88 -1 804 DGI B O2A   1 
HETATM 16014 O  "O5'" . DGI L 6 .   ? 160.438 151.242 170.539 1.00 64.69 ?  804 DGI B "O5'" 1 
HETATM 16015 C  "C5'" . DGI L 6 .   ? 159.385 152.228 170.563 1.00 61.37 ?  804 DGI B "C5'" 1 
HETATM 16016 C  "C4'" . DGI L 6 .   ? 158.052 151.532 170.447 1.00 62.25 ?  804 DGI B "C4'" 1 
HETATM 16017 O  "O4'" . DGI L 6 .   ? 157.989 150.809 169.198 1.00 62.79 ?  804 DGI B "O4'" 1 
HETATM 16018 C  "C3'" . DGI L 6 .   ? 157.748 150.521 171.558 1.00 63.26 ?  804 DGI B "C3'" 1 
HETATM 16019 O  "O3'" . DGI L 6 .   ? 156.435 150.732 172.077 1.00 62.44 ?  804 DGI B "O3'" 1 
HETATM 16020 C  "C2'" . DGI L 6 .   ? 157.840 149.173 170.851 1.00 58.79 ?  804 DGI B "C2'" 1 
HETATM 16021 C  "C1'" . DGI L 6 .   ? 157.450 149.526 169.430 1.00 58.08 ?  804 DGI B "C1'" 1 
HETATM 16022 N  N9    . DGI L 6 .   ? 157.987 148.609 168.405 1.00 59.64 ?  804 DGI B N9    1 
HETATM 16023 C  C8    . DGI L 6 .   ? 157.280 147.963 167.426 1.00 62.54 ?  804 DGI B C8    1 
HETATM 16024 N  N7    . DGI L 6 .   ? 158.029 147.208 166.658 1.00 61.46 ?  804 DGI B N7    1 
HETATM 16025 C  C5    . DGI L 6 .   ? 159.308 147.366 167.163 1.00 64.08 ?  804 DGI B C5    1 
HETATM 16026 C  C4    . DGI L 6 .   ? 159.298 148.227 168.240 1.00 62.76 ?  804 DGI B C4    1 
HETATM 16027 N  N3    . DGI L 6 .   ? 160.339 148.628 168.993 1.00 63.02 ?  804 DGI B N3    1 
HETATM 16028 C  C2    . DGI L 6 .   ? 161.493 148.090 168.603 1.00 61.32 ?  804 DGI B C2    1 
HETATM 16029 N  N2    . DGI L 6 .   ? 162.616 148.389 169.259 1.00 62.38 ?  804 DGI B N2    1 
HETATM 16030 N  N1    . DGI L 6 .   ? 161.601 147.226 167.546 1.00 60.59 ?  804 DGI B N1    1 
HETATM 16031 C  C6    . DGI L 6 .   ? 160.553 146.799 166.756 1.00 62.82 ?  804 DGI B C6    1 
HETATM 16032 O  O6    . DGI L 6 .   ? 160.747 146.019 165.824 1.00 61.55 ?  804 DGI B O6    1 
HETATM 16033 MN MN    . MN  M 7 .   ? 120.532 81.015  126.227 0.85 25.05 ?  401 MN  C MN    1 
HETATM 16034 MN MN    . MN  N 7 .   ? 118.256 83.710  127.457 0.85 26.37 ?  402 MN  C MN    1 
HETATM 16035 MN MN    . MN  O 7 .   ? 138.303 94.238  135.761 1.00 22.51 ?  401 MN  D MN    1 
HETATM 16036 MN MN    . MN  P 7 .   ? 140.196 93.543  132.410 1.00 24.72 ?  402 MN  D MN    1 
# 
