data_9BYD
# 
_entry.id   9BYD 
# 
_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   9BYD         pdb_00009byd 10.2210/pdb9byd/pdb 
WWPDB D_1000284378 ?            ?                   
EMDB  EMD-45029    ?            ?                   
# 
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                        9BYD 
_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 16 model for product condition of Bacillus subtilis ribonucleotide reductase complex' EMD-45029 '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                   9BYD 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BYD 
_struct.title                        'Class 16 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        9BYD 
_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 9BYD A 1  ? 700 ? P50620 1 ? 700 ? 1 700 
2 1 9BYD B 1  ? 700 ? P50620 1 ? 700 ? 1 700 
3 2 9BYD C 22 ? 350 ? P50621 1 ? 329 ? 1 329 
4 2 9BYD 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 9BYD MET C 1  ? UNP P50621 ? ? 'initiating methionine' -20 1  
3 9BYD GLY C 2  ? UNP P50621 ? ? 'expression tag'        -19 2  
3 9BYD SER C 3  ? UNP P50621 ? ? 'expression tag'        -18 3  
3 9BYD SER C 4  ? UNP P50621 ? ? 'expression tag'        -17 4  
3 9BYD HIS C 5  ? UNP P50621 ? ? 'expression tag'        -16 5  
3 9BYD HIS C 6  ? UNP P50621 ? ? 'expression tag'        -15 6  
3 9BYD HIS C 7  ? UNP P50621 ? ? 'expression tag'        -14 7  
3 9BYD HIS C 8  ? UNP P50621 ? ? 'expression tag'        -13 8  
3 9BYD HIS C 9  ? UNP P50621 ? ? 'expression tag'        -12 9  
3 9BYD HIS C 10 ? UNP P50621 ? ? 'expression tag'        -11 10 
3 9BYD SER C 11 ? UNP P50621 ? ? 'expression tag'        -10 11 
3 9BYD SER C 12 ? UNP P50621 ? ? 'expression tag'        -9  12 
3 9BYD GLY C 13 ? UNP P50621 ? ? 'expression tag'        -8  13 
3 9BYD LEU C 14 ? UNP P50621 ? ? 'expression tag'        -7  14 
3 9BYD VAL C 15 ? UNP P50621 ? ? 'expression tag'        -6  15 
3 9BYD PRO C 16 ? UNP P50621 ? ? 'expression tag'        -5  16 
3 9BYD ARG C 17 ? UNP P50621 ? ? 'expression tag'        -4  17 
3 9BYD GLY C 18 ? UNP P50621 ? ? 'expression tag'        -3  18 
3 9BYD SER C 19 ? UNP P50621 ? ? 'expression tag'        -2  19 
3 9BYD HIS C 20 ? UNP P50621 ? ? 'expression tag'        -1  20 
3 9BYD MET C 21 ? UNP P50621 ? ? 'expression tag'        0   21 
4 9BYD MET D 1  ? UNP P50621 ? ? 'initiating methionine' -20 22 
4 9BYD GLY D 2  ? UNP P50621 ? ? 'expression tag'        -19 23 
4 9BYD SER D 3  ? UNP P50621 ? ? 'expression tag'        -18 24 
4 9BYD SER D 4  ? UNP P50621 ? ? 'expression tag'        -17 25 
4 9BYD HIS D 5  ? UNP P50621 ? ? 'expression tag'        -16 26 
4 9BYD HIS D 6  ? UNP P50621 ? ? 'expression tag'        -15 27 
4 9BYD HIS D 7  ? UNP P50621 ? ? 'expression tag'        -14 28 
4 9BYD HIS D 8  ? UNP P50621 ? ? 'expression tag'        -13 29 
4 9BYD HIS D 9  ? UNP P50621 ? ? 'expression tag'        -12 30 
4 9BYD HIS D 10 ? UNP P50621 ? ? 'expression tag'        -11 31 
4 9BYD SER D 11 ? UNP P50621 ? ? 'expression tag'        -10 32 
4 9BYD SER D 12 ? UNP P50621 ? ? 'expression tag'        -9  33 
4 9BYD GLY D 13 ? UNP P50621 ? ? 'expression tag'        -8  34 
4 9BYD LEU D 14 ? UNP P50621 ? ? 'expression tag'        -7  35 
4 9BYD VAL D 15 ? UNP P50621 ? ? 'expression tag'        -6  36 
4 9BYD PRO D 16 ? UNP P50621 ? ? 'expression tag'        -5  37 
4 9BYD ARG D 17 ? UNP P50621 ? ? 'expression tag'        -4  38 
4 9BYD GLY D 18 ? UNP P50621 ? ? 'expression tag'        -3  39 
4 9BYD SER D 19 ? UNP P50621 ? ? 'expression tag'        -2  40 
4 9BYD HIS D 20 ? UNP P50621 ? ? 'expression tag'        -1  41 
4 9BYD 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 ? ? ? ? ? ? ? 2.049 ? ? 
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 ? ? ? ? ? ? ? 2.342 ? ? 
metalc5  metalc ? ? I TTP .   O3G ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.103 ? ? 
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 ? ? ? ? ? ? ? 1.961 ? ? 
metalc8  metalc ? ? C GLU 118 OE1 ? ? ? 1_555 N MN . MN ? ? C GLU 97  C MN 402 1_555 ? ? ? ? ? ? ? 2.113 ? ? 
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 ? ? ? ? ? ? ? 2.130 ? ? 
metalc11 metalc ? ? C GLU 185 OE2 ? ? ? 1_555 M MN . MN ? ? C GLU 164 C MN 401 1_555 ? ? ? ? ? ? ? 1.965 ? ? 
metalc12 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 M MN . MN ? ? C GLU 198 C MN 401 1_555 ? ? ? ? ? ? ? 2.173 ? ? 
metalc13 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 N MN . MN ? ? C GLU 198 C MN 402 1_555 ? ? ? ? ? ? ? 2.710 ? ? 
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 ? ? ? ? ? ? ? 2.408 ? ? 
metalc16 metalc ? ? D ASP 87  OD1 ? ? ? 1_555 P MN . MN ? ? D ASP 66  D MN 402 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc17 metalc ? ? D ASP 87  OD2 ? ? ? 1_555 P MN . MN ? ? D ASP 66  D MN 402 1_555 ? ? ? ? ? ? ? 2.157 ? ? 
metalc18 metalc ? ? D GLU 118 OE2 ? ? ? 1_555 O MN . MN ? ? D GLU 97  D MN 401 1_555 ? ? ? ? ? ? ? 1.912 ? ? 
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 ? ? ? ? ? ? ? 2.146 ? ? 
metalc21 metalc ? ? D GLU 185 OE1 ? ? ? 1_555 O MN . MN ? ? D GLU 164 D MN 401 1_555 ? ? ? ? ? ? ? 2.304 ? ? 
metalc22 metalc ? ? D GLU 185 OE2 ? ? ? 1_555 O MN . MN ? ? D GLU 164 D MN 401 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc23 metalc ? ? D GLU 219 OE1 ? ? ? 1_555 O MN . MN ? ? D GLU 198 D MN 401 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
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 ? ? ? ? ? ? ? 2.330 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O2A ? E TTP .   ? A TTP 801 ? 1_555 MG ? F MG . ? A MG 802 ? 1_555 O2B ? E TTP .   ? A TTP 801 ? 1_555 71.9  ? 
2  O2A ? E TTP .   ? A TTP 801 ? 1_555 MG ? F MG . ? A MG 802 ? 1_555 O1G ? E TTP .   ? A TTP 801 ? 1_555 88.8  ? 
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 89.5  ? 
6  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 120.6 ? 
7  OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 90.1  ? 
8  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 138.4 ? 
9  OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 85.1  ? 
10 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 100.7 ? 
11 OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 117.3 ? 
12 OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 137.9 ? 
13 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 101.2 ? 
14 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 53.0  ? 
15 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 141.6 ? 
16 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 87.2  ? 
17 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 64.8  ? 
18 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 120.1 ? 
19 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 78.3  ? 
20 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 142.1 ? 
21 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 97.1  ? 
22 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 114.2 ? 
23 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 103.9 ? 
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_555 165.6 ? 
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 99.6  ? 
37 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 55.6  ? 
38 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 121.7 ? 
39 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 81.3  ? 
40 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 136.7 ? 
41 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 91.4  ? 
42 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 103.0 ? 
43 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 102.6 ? 
44 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 89.6  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 355 A . ? TYR 355 A PRO 356 A ? PRO 356 A 1 1.22  
2 TYR 355 B . ? TYR 355 B PRO 356 B ? PRO 356 B 1 -0.29 
# 
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                   9BYD 
_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 ALA 269 ? ? NZ  D LYS 27  ? ? 2.06 
2 1 O   A CYS 382 ? ? OG  A SER 653 ? ? 2.13 
3 1 O   B PRO 616 ? ? OH  B TYR 626 ? ? 2.13 
4 1 O   A PRO 616 ? ? OH  A TYR 626 ? ? 2.14 
5 1 NH2 D ARG 86  ? ? OE1 D GLU 211 ? ? 2.18 
6 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 ? ? 72.11   -7.45   
2  1 SER A 593 ? ? 59.75   -154.80 
3  1 SER A 653 ? ? -68.95  99.26   
4  1 ASP B 215 ? ? 79.70   -1.01   
5  1 ASP B 238 ? ? -95.44  31.32   
6  1 SER B 408 ? ? -160.49 113.53  
7  1 SER B 593 ? ? 58.47   -151.21 
8  1 THR C 72  ? ? -128.05 -59.06  
9  1 ASP C 148 ? ? 58.08   15.69   
10 1 PHE C 166 ? ? -125.63 -60.76  
11 1 THR D 72  ? ? -128.18 -58.42  
12 1 PHE D 166 ? ? -144.12 -61.21  
13 1 THR D 311 ? ? -168.74 116.07  
14 1 ASP D 317 ? ? 61.73   167.65  
15 1 ASP D 318 ? ? 67.17   -4.15   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BYD 
_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                    9BYD 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  4.2 
_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               19000 
_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                        9BYD 
_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              9BYD 
_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                9BYD 
_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              9BYD 
_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           9BYD 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              'Class 16 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 Chimera' ? 
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                    9BYD 
_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   ? 103.714 117.070 98.524  1.00 63.04 ?  6   VAL A N     1 
ATOM   2     C  CA    . VAL A 1 6   ? 105.028 117.560 98.131  1.00 62.74 ?  6   VAL A CA    1 
ATOM   3     C  C     . VAL A 1 6   ? 104.867 118.727 97.156  1.00 63.36 ?  6   VAL A C     1 
ATOM   4     O  O     . VAL A 1 6   ? 103.966 118.721 96.313  1.00 63.20 ?  6   VAL A O     1 
ATOM   5     C  CB    . VAL A 1 6   ? 105.891 116.414 97.533  1.00 64.24 ?  6   VAL A CB    1 
ATOM   6     C  CG1   . VAL A 1 6   ? 105.628 116.230 96.041  1.00 62.93 ?  6   VAL A CG1   1 
ATOM   7     C  CG2   . VAL A 1 6   ? 107.367 116.652 97.798  1.00 61.49 ?  6   VAL A CG2   1 
ATOM   8     N  N     . PRO A 1 7   ? 105.702 119.757 97.305  1.00 58.77 ?  7   PRO A N     1 
ATOM   9     C  CA    . PRO A 1 7   ? 105.674 120.864 96.345  1.00 54.02 ?  7   PRO A CA    1 
ATOM   10    C  C     . PRO A 1 7   ? 106.038 120.386 94.949  1.00 56.48 ?  7   PRO A C     1 
ATOM   11    O  O     . PRO A 1 7   ? 106.859 119.485 94.770  1.00 60.50 ?  7   PRO A O     1 
ATOM   12    C  CB    . PRO A 1 7   ? 106.720 121.837 96.895  1.00 55.37 ?  7   PRO A CB    1 
ATOM   13    C  CG    . PRO A 1 7   ? 106.770 121.539 98.351  1.00 57.08 ?  7   PRO A CG    1 
ATOM   14    C  CD    . PRO A 1 7   ? 106.562 120.056 98.462  1.00 57.20 ?  7   PRO A CD    1 
ATOM   15    N  N     . LYS A 1 8   ? 105.406 121.002 93.949  1.00 58.03 ?  8   LYS A N     1 
ATOM   16    C  CA    . LYS A 1 8   ? 105.656 120.605 92.567  1.00 56.12 ?  8   LYS A CA    1 
ATOM   17    C  C     . LYS A 1 8   ? 107.087 120.915 92.154  1.00 57.08 ?  8   LYS A C     1 
ATOM   18    O  O     . LYS A 1 8   ? 107.712 120.139 91.421  1.00 57.57 ?  8   LYS A O     1 
ATOM   19    C  CB    . LYS A 1 8   ? 104.667 121.298 91.632  1.00 55.64 ?  8   LYS A CB    1 
ATOM   20    C  CG    . LYS A 1 8   ? 104.510 120.607 90.288  1.00 56.25 ?  8   LYS A CG    1 
ATOM   21    C  CD    . LYS A 1 8   ? 104.277 121.607 89.172  1.00 57.80 ?  8   LYS A CD    1 
ATOM   22    C  CE    . LYS A 1 8   ? 104.475 120.967 87.810  1.00 57.13 ?  8   LYS A CE    1 
ATOM   23    N  NZ    . LYS A 1 8   ? 105.005 121.938 86.814  1.00 58.95 1  8   LYS A NZ    1 
ATOM   24    N  N     . TRP A 1 9   ? 107.623 122.048 92.611  1.00 57.42 ?  9   TRP A N     1 
ATOM   25    C  CA    . TRP A 1 9   ? 108.951 122.458 92.173  1.00 52.16 ?  9   TRP A CA    1 
ATOM   26    C  C     . TRP A 1 9   ? 110.037 121.565 92.759  1.00 54.06 ?  9   TRP A C     1 
ATOM   27    O  O     . TRP A 1 9   ? 111.010 121.239 92.070  1.00 57.94 ?  9   TRP A O     1 
ATOM   28    C  CB    . TRP A 1 9   ? 109.197 123.923 92.526  1.00 53.77 ?  9   TRP A CB    1 
ATOM   29    C  CG    . TRP A 1 9   ? 108.891 124.293 93.936  1.00 50.50 ?  9   TRP A CG    1 
ATOM   30    C  CD1   . TRP A 1 9   ? 109.732 124.211 95.000  1.00 51.38 ?  9   TRP A CD1   1 
ATOM   31    C  CD2   . TRP A 1 9   ? 107.659 124.818 94.437  1.00 51.33 ?  9   TRP A CD2   1 
ATOM   32    N  NE1   . TRP A 1 9   ? 109.102 124.646 96.139  1.00 52.90 ?  9   TRP A NE1   1 
ATOM   33    C  CE2   . TRP A 1 9   ? 107.826 125.026 95.820  1.00 52.26 ?  9   TRP A CE2   1 
ATOM   34    C  CE3   . TRP A 1 9   ? 106.430 125.130 93.853  1.00 51.69 ?  9   TRP A CE3   1 
ATOM   35    C  CZ2   . TRP A 1 9   ? 106.812 125.530 96.626  1.00 52.47 ?  9   TRP A CZ2   1 
ATOM   36    C  CZ3   . TRP A 1 9   ? 105.425 125.630 94.653  1.00 55.31 ?  9   TRP A CZ3   1 
ATOM   37    C  CH2   . TRP A 1 9   ? 105.621 125.826 96.025  1.00 54.90 ?  9   TRP A CH2   1 
ATOM   38    N  N     . ILE A 1 10  ? 109.896 121.148 94.021  1.00 54.45 ?  10  ILE A N     1 
ATOM   39    C  CA    . ILE A 1 10  ? 110.886 120.228 94.572  1.00 57.23 ?  10  ILE A CA    1 
ATOM   40    C  C     . ILE A 1 10  ? 110.686 118.813 94.049  1.00 55.75 ?  10  ILE A C     1 
ATOM   41    O  O     . ILE A 1 10  ? 111.637 118.022 94.050  1.00 59.01 ?  10  ILE A O     1 
ATOM   42    C  CB    . ILE A 1 10  ? 110.893 120.204 96.112  1.00 56.46 ?  10  ILE A CB    1 
ATOM   43    C  CG1   . ILE A 1 10  ? 109.910 119.170 96.659  1.00 58.14 ?  10  ILE A CG1   1 
ATOM   44    C  CG2   . ILE A 1 10  ? 110.603 121.574 96.685  1.00 55.14 ?  10  ILE A CG2   1 
ATOM   45    C  CD1   . ILE A 1 10  ? 110.115 118.877 98.124  1.00 58.28 ?  10  ILE A CD1   1 
ATOM   46    N  N     . GLN A 1 11  ? 109.477 118.468 93.604  1.00 57.10 ?  11  GLN A N     1 
ATOM   47    C  CA    . GLN A 1 11  ? 109.290 117.192 92.925  1.00 57.23 ?  11  GLN A CA    1 
ATOM   48    C  C     . GLN A 1 11  ? 109.993 117.190 91.574  1.00 56.41 ?  11  GLN A C     1 
ATOM   49    O  O     . GLN A 1 11  ? 110.640 116.203 91.206  1.00 58.51 ?  11  GLN A O     1 
ATOM   50    C  CB    . GLN A 1 11  ? 107.799 116.895 92.768  1.00 59.25 ?  11  GLN A CB    1 
ATOM   51    C  CG    . GLN A 1 11  ? 107.482 115.778 91.793  1.00 60.60 ?  11  GLN A CG    1 
ATOM   52    C  CD    . GLN A 1 11  ? 106.697 116.266 90.594  1.00 61.60 ?  11  GLN A CD    1 
ATOM   53    O  OE1   . GLN A 1 11  ? 105.715 116.993 90.735  1.00 60.15 ?  11  GLN A OE1   1 
ATOM   54    N  NE2   . GLN A 1 11  ? 107.130 115.869 89.403  1.00 60.38 ?  11  GLN A NE2   1 
ATOM   55    N  N     . LEU A 1 12  ? 109.885 118.293 90.830  1.00 56.36 ?  12  LEU A N     1 
ATOM   56    C  CA    . LEU A 1 12  ? 110.616 118.423 89.572  1.00 55.06 ?  12  LEU A CA    1 
ATOM   57    C  C     . LEU A 1 12  ? 112.121 118.459 89.809  1.00 57.48 ?  12  LEU A C     1 
ATOM   58    O  O     . LEU A 1 12  ? 112.895 117.914 89.015  1.00 59.89 ?  12  LEU A O     1 
ATOM   59    C  CB    . LEU A 1 12  ? 110.164 119.681 88.834  1.00 55.96 ?  12  LEU A CB    1 
ATOM   60    C  CG    . LEU A 1 12  ? 109.059 119.525 87.791  1.00 56.90 ?  12  LEU A CG    1 
ATOM   61    C  CD1   . LEU A 1 12  ? 108.313 120.835 87.615  1.00 55.45 ?  12  LEU A CD1   1 
ATOM   62    C  CD2   . LEU A 1 12  ? 109.638 119.052 86.470  1.00 57.52 ?  12  LEU A CD2   1 
ATOM   63    N  N     . ASN A 1 13  ? 112.552 119.109 90.892  1.00 56.01 ?  13  ASN A N     1 
ATOM   64    C  CA    . ASN A 1 13  ? 113.975 119.204 91.195  1.00 52.82 ?  13  ASN A CA    1 
ATOM   65    C  C     . ASN A 1 13  ? 114.562 117.849 91.568  1.00 54.86 ?  13  ASN A C     1 
ATOM   66    O  O     . ASN A 1 13  ? 115.758 117.617 91.365  1.00 60.62 ?  13  ASN A O     1 
ATOM   67    C  CB    . ASN A 1 13  ? 114.199 120.215 92.320  1.00 56.25 ?  13  ASN A CB    1 
ATOM   68    C  CG    . ASN A 1 13  ? 115.647 120.295 92.754  1.00 56.13 ?  13  ASN A CG    1 
ATOM   69    O  OD1   . ASN A 1 13  ? 116.028 119.744 93.785  1.00 54.72 ?  13  ASN A OD1   1 
ATOM   70    N  ND2   . ASN A 1 13  ? 116.462 120.987 91.968  1.00 55.92 ?  13  ASN A ND2   1 
ATOM   71    N  N     . ASN A 1 14  ? 113.744 116.948 92.110  1.00 57.72 ?  14  ASN A N     1 
ATOM   72    C  CA    . ASN A 1 14  ? 114.211 115.610 92.448  1.00 58.51 ?  14  ASN A CA    1 
ATOM   73    C  C     . ASN A 1 14  ? 114.290 114.689 91.238  1.00 57.77 ?  14  ASN A C     1 
ATOM   74    O  O     . ASN A 1 14  ? 114.864 113.602 91.348  1.00 60.03 ?  14  ASN A O     1 
ATOM   75    C  CB    . ASN A 1 14  ? 113.305 114.989 93.512  1.00 56.46 ?  14  ASN A CB    1 
ATOM   76    C  CG    . ASN A 1 14  ? 113.566 115.546 94.895  1.00 58.69 ?  14  ASN A CG    1 
ATOM   77    O  OD1   . ASN A 1 14  ? 113.910 116.717 95.049  1.00 60.90 ?  14  ASN A OD1   1 
ATOM   78    N  ND2   . ASN A 1 14  ? 113.402 114.709 95.912  1.00 59.30 ?  14  ASN A ND2   1 
ATOM   79    N  N     . GLU A 1 15  ? 113.737 115.093 90.096  1.00 57.87 ?  15  GLU A N     1 
ATOM   80    C  CA    . GLU A 1 15  ? 113.852 114.312 88.872  1.00 59.07 ?  15  GLU A CA    1 
ATOM   81    C  C     . GLU A 1 15  ? 115.218 114.450 88.214  1.00 61.72 ?  15  GLU A C     1 
ATOM   82    O  O     . GLU A 1 15  ? 115.469 113.786 87.203  1.00 63.52 ?  15  GLU A O     1 
ATOM   83    C  CB    . GLU A 1 15  ? 112.756 114.713 87.880  1.00 59.34 ?  15  GLU A CB    1 
ATOM   84    C  CG    . GLU A 1 15  ? 111.379 114.844 88.503  1.00 60.15 ?  15  GLU A CG    1 
ATOM   85    C  CD    . GLU A 1 15  ? 110.264 114.837 87.475  1.00 63.73 ?  15  GLU A CD    1 
ATOM   86    O  OE1   . GLU A 1 15  ? 110.565 114.929 86.268  1.00 63.57 ?  15  GLU A OE1   1 
ATOM   87    O  OE2   . GLU A 1 15  ? 109.086 114.740 87.877  1.00 63.84 -1 15  GLU A OE2   1 
ATOM   88    N  N     . ILE A 1 16  ? 116.093 115.303 88.750  1.00 59.98 ?  16  ILE A N     1 
ATOM   89    C  CA    . ILE A 1 16  ? 117.459 115.386 88.244  1.00 59.72 ?  16  ILE A CA    1 
ATOM   90    C  C     . ILE A 1 16  ? 118.191 114.072 88.480  1.00 59.78 ?  16  ILE A C     1 
ATOM   91    O  O     . ILE A 1 16  ? 118.907 113.574 87.603  1.00 61.09 ?  16  ILE A O     1 
ATOM   92    C  CB    . ILE A 1 16  ? 118.201 116.569 88.893  1.00 58.93 ?  16  ILE A CB    1 
ATOM   93    C  CG1   . ILE A 1 16  ? 117.485 117.885 88.589  1.00 57.54 ?  16  ILE A CG1   1 
ATOM   94    C  CG2   . ILE A 1 16  ? 119.645 116.627 88.416  1.00 59.58 ?  16  ILE A CG2   1 
ATOM   95    C  CD1   . ILE A 1 16  ? 117.985 119.051 89.408  1.00 56.90 ?  16  ILE A CD1   1 
ATOM   96    N  N     . MET A 1 17  ? 118.016 113.486 89.665  1.00 60.50 ?  17  MET A N     1 
ATOM   97    C  CA    . MET A 1 17  ? 118.719 112.261 90.017  1.00 61.98 ?  17  MET A CA    1 
ATOM   98    C  C     . MET A 1 17  ? 118.136 111.025 89.347  1.00 62.80 ?  17  MET A C     1 
ATOM   99    O  O     . MET A 1 17  ? 118.824 110.002 89.266  1.00 63.98 ?  17  MET A O     1 
ATOM   100   C  CB    . MET A 1 17  ? 118.710 112.074 91.533  1.00 61.29 ?  17  MET A CB    1 
ATOM   101   C  CG    . MET A 1 17  ? 119.177 113.297 92.286  1.00 61.55 ?  17  MET A CG    1 
ATOM   102   S  SD    . MET A 1 17  ? 120.721 113.971 91.645  1.00 68.12 ?  17  MET A SD    1 
ATOM   103   C  CE    . MET A 1 17  ? 121.919 112.970 92.523  1.00 61.05 ?  17  MET A CE    1 
ATOM   104   N  N     . ILE A 1 18  ? 116.894 111.088 88.873  1.00 62.62 ?  18  ILE A N     1 
ATOM   105   C  CA    . ILE A 1 18  ? 116.322 109.971 88.126  1.00 64.44 ?  18  ILE A CA    1 
ATOM   106   C  C     . ILE A 1 18  ? 117.060 109.891 86.794  1.00 65.28 ?  18  ILE A C     1 
ATOM   107   O  O     . ILE A 1 18  ? 116.876 110.740 85.916  1.00 66.44 ?  18  ILE A O     1 
ATOM   108   C  CB    . ILE A 1 18  ? 114.806 110.120 87.924  1.00 65.30 ?  18  ILE A CB    1 
ATOM   109   C  CG1   . ILE A 1 18  ? 113.994 109.856 89.210  1.00 64.60 ?  18  ILE A CG1   1 
ATOM   110   C  CG2   . ILE A 1 18  ? 114.318 109.179 86.829  1.00 64.87 ?  18  ILE A CG2   1 
ATOM   111   C  CD1   . ILE A 1 18  ? 114.450 110.531 90.489  1.00 64.07 ?  18  ILE A CD1   1 
ATOM   112   N  N     . GLN A 1 19  ? 117.911 108.881 86.648  1.00 68.96 ?  19  GLN A N     1 
ATOM   113   C  CA    . GLN A 1 19  ? 118.776 108.772 85.481  1.00 70.00 ?  19  GLN A CA    1 
ATOM   114   C  C     . GLN A 1 19  ? 117.989 108.209 84.306  1.00 69.78 ?  19  GLN A C     1 
ATOM   115   O  O     . GLN A 1 19  ? 117.554 107.053 84.338  1.00 71.76 ?  19  GLN A O     1 
ATOM   116   C  CB    . GLN A 1 19  ? 119.985 107.895 85.796  1.00 72.02 ?  19  GLN A CB    1 
ATOM   117   C  CG    . GLN A 1 19  ? 120.955 108.517 86.788  1.00 70.29 ?  19  GLN A CG    1 
ATOM   118   C  CD    . GLN A 1 19  ? 122.172 107.649 87.043  1.00 71.59 ?  19  GLN A CD    1 
ATOM   119   O  OE1   . GLN A 1 19  ? 122.299 106.559 86.486  1.00 71.28 ?  19  GLN A OE1   1 
ATOM   120   N  NE2   . GLN A 1 19  ? 123.073 108.130 87.892  1.00 71.39 ?  19  GLN A NE2   1 
ATOM   121   N  N     . LYS A 1 20  ? 117.805 109.026 83.275  1.00 71.28 ?  20  LYS A N     1 
ATOM   122   C  CA    . LYS A 1 20  ? 117.122 108.624 82.054  1.00 73.11 ?  20  LYS A CA    1 
ATOM   123   C  C     . LYS A 1 20  ? 118.161 108.468 80.953  1.00 73.64 ?  20  LYS A C     1 
ATOM   124   O  O     . LYS A 1 20  ? 118.915 109.406 80.673  1.00 73.55 ?  20  LYS A O     1 
ATOM   125   C  CB    . LYS A 1 20  ? 116.058 109.647 81.660  1.00 71.82 ?  20  LYS A CB    1 
ATOM   126   C  CG    . LYS A 1 20  ? 115.458 109.421 80.283  1.00 72.49 ?  20  LYS A CG    1 
ATOM   127   C  CD    . LYS A 1 20  ? 115.282 110.731 79.536  1.00 73.53 ?  20  LYS A CD    1 
ATOM   128   C  CE    . LYS A 1 20  ? 116.554 111.562 79.569  1.00 73.84 ?  20  LYS A CE    1 
ATOM   129   N  NZ    . LYS A 1 20  ? 117.694 110.859 78.923  1.00 73.93 1  20  LYS A NZ    1 
ATOM   130   N  N     . ASP A 1 21  ? 118.197 107.283 80.339  1.00 72.18 ?  21  ASP A N     1 
ATOM   131   C  CA    . ASP A 1 21  ? 119.178 106.953 79.304  1.00 73.50 ?  21  ASP A CA    1 
ATOM   132   C  C     . ASP A 1 21  ? 120.606 107.088 79.830  1.00 74.05 ?  21  ASP A C     1 
ATOM   133   O  O     . ASP A 1 21  ? 121.516 107.502 79.110  1.00 72.09 ?  21  ASP A O     1 
ATOM   134   C  CB    . ASP A 1 21  ? 118.975 107.810 78.052  1.00 73.43 ?  21  ASP A CB    1 
ATOM   135   C  CG    . ASP A 1 21  ? 117.520 107.895 77.635  1.00 74.57 ?  21  ASP A CG    1 
ATOM   136   O  OD1   . ASP A 1 21  ? 116.806 106.878 77.750  1.00 72.61 ?  21  ASP A OD1   1 
ATOM   137   O  OD2   . ASP A 1 21  ? 117.091 108.982 77.193  1.00 74.27 -1 21  ASP A OD2   1 
ATOM   138   N  N     . GLY A 1 22  ? 120.802 106.733 81.098  1.00 73.98 ?  22  GLY A N     1 
ATOM   139   C  CA    . GLY A 1 22  ? 122.122 106.741 81.694  1.00 74.01 ?  22  GLY A CA    1 
ATOM   140   C  C     . GLY A 1 22  ? 122.676 108.105 82.039  1.00 73.96 ?  22  GLY A C     1 
ATOM   141   O  O     . GLY A 1 22  ? 123.867 108.207 82.350  1.00 72.73 ?  22  GLY A O     1 
ATOM   142   N  N     . LYS A 1 23  ? 121.857 109.154 81.999  1.00 70.77 ?  23  LYS A N     1 
ATOM   143   C  CA    . LYS A 1 23  ? 122.312 110.506 82.277  1.00 68.48 ?  23  LYS A CA    1 
ATOM   144   C  C     . LYS A 1 23  ? 121.381 111.176 83.276  1.00 69.58 ?  23  LYS A C     1 
ATOM   145   O  O     . LYS A 1 23  ? 120.179 110.897 83.314  1.00 70.55 ?  23  LYS A O     1 
ATOM   146   C  CB    . LYS A 1 23  ? 122.375 111.354 81.000  1.00 68.39 ?  23  LYS A CB    1 
ATOM   147   C  CG    . LYS A 1 23  ? 123.455 110.943 80.016  1.00 68.46 ?  23  LYS A CG    1 
ATOM   148   C  CD    . LYS A 1 23  ? 123.486 111.895 78.832  1.00 68.57 ?  23  LYS A CD    1 
ATOM   149   C  CE    . LYS A 1 23  ? 124.478 111.447 77.777  1.00 68.95 ?  23  LYS A CE    1 
ATOM   150   N  NZ    . LYS A 1 23  ? 124.459 112.347 76.592  1.00 67.63 1  23  LYS A NZ    1 
ATOM   151   N  N     . PHE A 1 24  ? 121.951 112.063 84.087  1.00 63.30 ?  24  PHE A N     1 
ATOM   152   C  CA    . PHE A 1 24  ? 121.145 112.892 84.971  1.00 60.09 ?  24  PHE A CA    1 
ATOM   153   C  C     . PHE A 1 24  ? 120.285 113.844 84.152  1.00 60.84 ?  24  PHE A C     1 
ATOM   154   O  O     . PHE A 1 24  ? 120.725 114.385 83.134  1.00 59.40 ?  24  PHE A O     1 
ATOM   155   C  CB    . PHE A 1 24  ? 122.037 113.688 85.923  1.00 58.54 ?  24  PHE A CB    1 
ATOM   156   C  CG    . PHE A 1 24  ? 122.689 112.856 86.985  1.00 59.92 ?  24  PHE A CG    1 
ATOM   157   C  CD1   . PHE A 1 24  ? 122.010 112.540 88.148  1.00 60.45 ?  24  PHE A CD1   1 
ATOM   158   C  CD2   . PHE A 1 24  ? 123.983 112.394 86.823  1.00 59.89 ?  24  PHE A CD2   1 
ATOM   159   C  CE1   . PHE A 1 24  ? 122.611 111.777 89.129  1.00 60.18 ?  24  PHE A CE1   1 
ATOM   160   C  CE2   . PHE A 1 24  ? 124.588 111.631 87.801  1.00 59.21 ?  24  PHE A CE2   1 
ATOM   161   C  CZ    . PHE A 1 24  ? 123.900 111.322 88.955  1.00 60.10 ?  24  PHE A CZ    1 
ATOM   162   N  N     . GLN A 1 25  ? 119.047 114.048 84.602  1.00 61.85 ?  25  GLN A N     1 
ATOM   163   C  CA    . GLN A 1 25  ? 118.125 114.962 83.929  1.00 59.76 ?  25  GLN A CA    1 
ATOM   164   C  C     . GLN A 1 25  ? 118.371 116.366 84.471  1.00 60.95 ?  25  GLN A C     1 
ATOM   165   O  O     . GLN A 1 25  ? 117.667 116.869 85.348  1.00 61.19 ?  25  GLN A O     1 
ATOM   166   C  CB    . GLN A 1 25  ? 116.683 114.515 84.127  1.00 61.01 ?  25  GLN A CB    1 
ATOM   167   C  CG    . GLN A 1 25  ? 116.397 113.112 83.624  1.00 61.65 ?  25  GLN A CG    1 
ATOM   168   C  CD    . GLN A 1 25  ? 114.941 112.726 83.773  1.00 62.47 ?  25  GLN A CD    1 
ATOM   169   O  OE1   . GLN A 1 25  ? 114.126 112.982 82.887  1.00 62.18 ?  25  GLN A OE1   1 
ATOM   170   N  NE2   . GLN A 1 25  ? 114.605 112.105 84.897  1.00 60.78 ?  25  GLN A NE2   1 
ATOM   171   N  N     . PHE A 1 26  ? 119.407 117.007 83.925  1.00 57.38 ?  26  PHE A N     1 
ATOM   172   C  CA    . PHE A 1 26  ? 119.799 118.329 84.402  1.00 55.95 ?  26  PHE A CA    1 
ATOM   173   C  C     . PHE A 1 26  ? 118.786 119.396 84.009  1.00 57.41 ?  26  PHE A C     1 
ATOM   174   O  O     . PHE A 1 26  ? 118.642 120.400 84.715  1.00 56.88 ?  26  PHE A O     1 
ATOM   175   C  CB    . PHE A 1 26  ? 121.185 118.689 83.870  1.00 53.29 ?  26  PHE A CB    1 
ATOM   176   C  CG    . PHE A 1 26  ? 122.293 117.879 84.476  1.00 54.17 ?  26  PHE A CG    1 
ATOM   177   C  CD1   . PHE A 1 26  ? 122.467 117.836 85.848  1.00 54.44 ?  26  PHE A CD1   1 
ATOM   178   C  CD2   . PHE A 1 26  ? 123.159 117.157 83.674  1.00 55.39 ?  26  PHE A CD2   1 
ATOM   179   C  CE1   . PHE A 1 26  ? 123.485 117.090 86.408  1.00 53.11 ?  26  PHE A CE1   1 
ATOM   180   C  CE2   . PHE A 1 26  ? 124.177 116.410 84.229  1.00 54.08 ?  26  PHE A CE2   1 
ATOM   181   C  CZ    . PHE A 1 26  ? 124.340 116.378 85.598  1.00 51.66 ?  26  PHE A CZ    1 
ATOM   182   N  N     . ASP A 1 27  ? 118.079 119.203 82.893  1.00 62.63 ?  27  ASP A N     1 
ATOM   183   C  CA    . ASP A 1 27  ? 117.091 120.177 82.444  1.00 61.91 ?  27  ASP A CA    1 
ATOM   184   C  C     . ASP A 1 27  ? 115.882 120.265 83.364  1.00 62.06 ?  27  ASP A C     1 
ATOM   185   O  O     . ASP A 1 27  ? 115.083 121.196 83.217  1.00 62.82 ?  27  ASP A O     1 
ATOM   186   C  CB    . ASP A 1 27  ? 116.632 119.842 81.024  1.00 61.74 ?  27  ASP A CB    1 
ATOM   187   C  CG    . ASP A 1 27  ? 116.619 121.055 80.115  1.00 65.25 ?  27  ASP A CG    1 
ATOM   188   O  OD1   . ASP A 1 27  ? 116.613 120.876 78.879  1.00 66.74 ?  27  ASP A OD1   1 
ATOM   189   O  OD2   . ASP A 1 27  ? 116.613 122.189 80.637  1.00 65.33 -1 27  ASP A OD2   1 
ATOM   190   N  N     . LYS A 1 28  ? 115.722 119.323 84.295  1.00 58.49 ?  28  LYS A N     1 
ATOM   191   C  CA    . LYS A 1 28  ? 114.603 119.388 85.227  1.00 59.07 ?  28  LYS A CA    1 
ATOM   192   C  C     . LYS A 1 28  ? 114.711 120.590 86.155  1.00 59.76 ?  28  LYS A C     1 
ATOM   193   O  O     . LYS A 1 28  ? 113.689 121.095 86.632  1.00 62.05 ?  28  LYS A O     1 
ATOM   194   C  CB    . LYS A 1 28  ? 114.522 118.100 86.044  1.00 58.92 ?  28  LYS A CB    1 
ATOM   195   C  CG    . LYS A 1 28  ? 114.169 116.875 85.225  1.00 60.16 ?  28  LYS A CG    1 
ATOM   196   C  CD    . LYS A 1 28  ? 112.711 116.892 84.809  1.00 61.07 ?  28  LYS A CD    1 
ATOM   197   C  CE    . LYS A 1 28  ? 112.425 115.824 83.770  1.00 60.92 ?  28  LYS A CE    1 
ATOM   198   N  NZ    . LYS A 1 28  ? 110.974 115.737 83.453  1.00 61.66 1  28  LYS A NZ    1 
ATOM   199   N  N     . ASP A 1 29  ? 115.932 121.062 86.423  1.00 56.42 ?  29  ASP A N     1 
ATOM   200   C  CA    . ASP A 1 29  ? 116.103 122.198 87.321  1.00 54.47 ?  29  ASP A CA    1 
ATOM   201   C  C     . ASP A 1 29  ? 115.564 123.485 86.710  1.00 53.46 ?  29  ASP A C     1 
ATOM   202   O  O     . ASP A 1 29  ? 115.113 124.373 87.443  1.00 55.08 ?  29  ASP A O     1 
ATOM   203   C  CB    . ASP A 1 29  ? 117.575 122.358 87.692  1.00 52.84 ?  29  ASP A CB    1 
ATOM   204   C  CG    . ASP A 1 29  ? 117.778 122.573 89.176  1.00 56.37 ?  29  ASP A CG    1 
ATOM   205   O  OD1   . ASP A 1 29  ? 116.898 122.165 89.961  1.00 56.68 ?  29  ASP A OD1   1 
ATOM   206   O  OD2   . ASP A 1 29  ? 118.821 123.142 89.560  1.00 55.59 -1 29  ASP A OD2   1 
ATOM   207   N  N     . LYS A 1 30  ? 115.613 123.613 85.383  1.00 54.13 ?  30  LYS A N     1 
ATOM   208   C  CA    . LYS A 1 30  ? 114.957 124.739 84.728  1.00 56.39 ?  30  LYS A CA    1 
ATOM   209   C  C     . LYS A 1 30  ? 113.446 124.656 84.898  1.00 55.12 ?  30  LYS A C     1 
ATOM   210   O  O     . LYS A 1 30  ? 112.788 125.648 85.239  1.00 59.35 ?  30  LYS A O     1 
ATOM   211   C  CB    . LYS A 1 30  ? 115.337 124.777 83.248  1.00 55.60 ?  30  LYS A CB    1 
ATOM   212   C  CG    . LYS A 1 30  ? 114.750 125.949 82.483  1.00 57.24 ?  30  LYS A CG    1 
ATOM   213   C  CD    . LYS A 1 30  ? 115.752 126.514 81.490  1.00 57.04 ?  30  LYS A CD    1 
ATOM   214   C  CE    . LYS A 1 30  ? 115.190 127.726 80.767  1.00 57.35 ?  30  LYS A CE    1 
ATOM   215   N  NZ    . LYS A 1 30  ? 114.676 127.374 79.415  1.00 56.39 1  30  LYS A NZ    1 
ATOM   216   N  N     . GLU A 1 31  ? 112.879 123.468 84.681  1.00 52.94 ?  31  GLU A N     1 
ATOM   217   C  CA    . GLU A 1 31  ? 111.464 123.267 84.965  1.00 53.56 ?  31  GLU A CA    1 
ATOM   218   C  C     . GLU A 1 31  ? 111.181 123.429 86.451  1.00 54.66 ?  31  GLU A C     1 
ATOM   219   O  O     . GLU A 1 31  ? 110.128 123.947 86.838  1.00 56.52 ?  31  GLU A O     1 
ATOM   220   C  CB    . GLU A 1 31  ? 111.021 121.887 84.480  1.00 55.25 ?  31  GLU A CB    1 
ATOM   221   C  CG    . GLU A 1 31  ? 110.555 121.856 83.037  1.00 56.83 ?  31  GLU A CG    1 
ATOM   222   C  CD    . GLU A 1 31  ? 110.844 120.532 82.360  1.00 60.89 ?  31  GLU A CD    1 
ATOM   223   O  OE1   . GLU A 1 31  ? 111.556 119.700 82.961  1.00 60.98 ?  31  GLU A OE1   1 
ATOM   224   O  OE2   . GLU A 1 31  ? 110.361 120.322 81.227  1.00 58.42 -1 31  GLU A OE2   1 
ATOM   225   N  N     . ALA A 1 32  ? 112.117 122.999 87.300  1.00 50.02 ?  32  ALA A N     1 
ATOM   226   C  CA    . ALA A 1 32  ? 111.930 123.144 88.739  1.00 49.58 ?  32  ALA A CA    1 
ATOM   227   C  C     . ALA A 1 32  ? 111.827 124.608 89.140  1.00 52.01 ?  32  ALA A C     1 
ATOM   228   O  O     . ALA A 1 32  ? 110.938 124.982 89.910  1.00 51.91 ?  32  ALA A O     1 
ATOM   229   C  CB    . ALA A 1 32  ? 113.071 122.461 89.492  1.00 48.80 ?  32  ALA A CB    1 
ATOM   230   N  N     . VAL A 1 33  ? 112.713 125.458 88.616  1.00 53.52 ?  33  VAL A N     1 
ATOM   231   C  CA    . VAL A 1 33  ? 112.674 126.871 88.981  1.00 52.03 ?  33  VAL A CA    1 
ATOM   232   C  C     . VAL A 1 33  ? 111.473 127.562 88.341  1.00 52.95 ?  33  VAL A C     1 
ATOM   233   O  O     . VAL A 1 33  ? 110.866 128.458 88.941  1.00 54.60 ?  33  VAL A O     1 
ATOM   234   C  CB    . VAL A 1 33  ? 114.005 127.564 88.626  1.00 49.44 ?  33  VAL A CB    1 
ATOM   235   C  CG1   . VAL A 1 33  ? 114.164 127.742 87.127  1.00 51.09 ?  33  VAL A CG1   1 
ATOM   236   C  CG2   . VAL A 1 33  ? 114.110 128.903 89.335  1.00 49.46 ?  33  VAL A CG2   1 
ATOM   237   N  N     . HIS A 1 34  ? 111.100 127.154 87.125  1.00 50.73 ?  34  HIS A N     1 
ATOM   238   C  CA    . HIS A 1 34  ? 109.919 127.728 86.487  1.00 50.74 ?  34  HIS A CA    1 
ATOM   239   C  C     . HIS A 1 34  ? 108.668 127.430 87.307  1.00 52.66 ?  34  HIS A C     1 
ATOM   240   O  O     . HIS A 1 34  ? 107.842 128.321 87.556  1.00 53.04 ?  34  HIS A O     1 
ATOM   241   C  CB    . HIS A 1 34  ? 109.799 127.184 85.061  1.00 53.19 ?  34  HIS A CB    1 
ATOM   242   C  CG    . HIS A 1 34  ? 108.714 127.818 84.241  1.00 55.22 ?  34  HIS A CG    1 
ATOM   243   N  ND1   . HIS A 1 34  ? 107.477 128.147 84.752  1.00 54.82 ?  34  HIS A ND1   1 
ATOM   244   C  CD2   . HIS A 1 34  ? 108.690 128.185 82.939  1.00 54.74 ?  34  HIS A CD2   1 
ATOM   245   C  CE1   . HIS A 1 34  ? 106.737 128.684 83.798  1.00 55.21 ?  34  HIS A CE1   1 
ATOM   246   N  NE2   . HIS A 1 34  ? 107.452 128.722 82.689  1.00 55.54 ?  34  HIS A NE2   1 
ATOM   247   N  N     . SER A 1 35  ? 108.520 126.177 87.747  1.00 54.59 ?  35  SER A N     1 
ATOM   248   C  CA    . SER A 1 35  ? 107.396 125.813 88.599  1.00 51.97 ?  35  SER A CA    1 
ATOM   249   C  C     . SER A 1 35  ? 107.472 126.523 89.943  1.00 52.12 ?  35  SER A C     1 
ATOM   250   O  O     . SER A 1 35  ? 106.452 126.988 90.462  1.00 54.74 ?  35  SER A O     1 
ATOM   251   C  CB    . SER A 1 35  ? 107.357 124.298 88.798  1.00 51.86 ?  35  SER A CB    1 
ATOM   252   O  OG    . SER A 1 35  ? 106.564 123.956 89.919  1.00 54.09 ?  35  SER A OG    1 
ATOM   253   N  N     . TYR A 1 36  ? 108.673 126.619 90.519  1.00 51.70 ?  36  TYR A N     1 
ATOM   254   C  CA    . TYR A 1 36  ? 108.849 127.330 91.778  1.00 51.33 ?  36  TYR A CA    1 
ATOM   255   C  C     . TYR A 1 36  ? 108.308 128.742 91.675  1.00 48.41 ?  36  TYR A C     1 
ATOM   256   O  O     . TYR A 1 36  ? 107.500 129.173 92.503  1.00 48.38 ?  36  TYR A O     1 
ATOM   257   C  CB    . TYR A 1 36  ? 110.328 127.346 92.165  1.00 47.92 ?  36  TYR A CB    1 
ATOM   258   C  CG    . TYR A 1 36  ? 110.641 128.144 93.410  1.00 49.41 ?  36  TYR A CG    1 
ATOM   259   C  CD1   . TYR A 1 36  ? 110.077 127.811 94.633  1.00 47.81 ?  36  TYR A CD1   1 
ATOM   260   C  CD2   . TYR A 1 36  ? 111.507 129.227 93.361  1.00 48.66 ?  36  TYR A CD2   1 
ATOM   261   C  CE1   . TYR A 1 36  ? 110.367 128.535 95.771  1.00 46.14 ?  36  TYR A CE1   1 
ATOM   262   C  CE2   . TYR A 1 36  ? 111.800 129.958 94.493  1.00 46.68 ?  36  TYR A CE2   1 
ATOM   263   C  CZ    . TYR A 1 36  ? 111.228 129.607 95.694  1.00 48.10 ?  36  TYR A CZ    1 
ATOM   264   O  OH    . TYR A 1 36  ? 111.520 130.334 96.825  1.00 50.06 ?  36  TYR A OH    1 
ATOM   265   N  N     . PHE A 1 37  ? 108.698 129.459 90.622  1.00 52.38 ?  37  PHE A N     1 
ATOM   266   C  CA    . PHE A 1 37  ? 108.205 130.816 90.446  1.00 52.15 ?  37  PHE A CA    1 
ATOM   267   C  C     . PHE A 1 37  ? 106.695 130.826 90.261  1.00 53.54 ?  37  PHE A C     1 
ATOM   268   O  O     . PHE A 1 37  ? 105.968 131.327 91.124  1.00 56.56 ?  37  PHE A O     1 
ATOM   269   C  CB    . PHE A 1 37  ? 108.916 131.494 89.280  1.00 54.60 ?  37  PHE A CB    1 
ATOM   270   C  CG    . PHE A 1 37  ? 110.191 132.163 89.680  1.00 53.80 ?  37  PHE A CG    1 
ATOM   271   C  CD1   . PHE A 1 37  ? 110.171 133.424 90.247  1.00 51.23 ?  37  PHE A CD1   1 
ATOM   272   C  CD2   . PHE A 1 37  ? 111.403 131.520 89.527  1.00 53.12 ?  37  PHE A CD2   1 
ATOM   273   C  CE1   . PHE A 1 37  ? 111.339 134.040 90.632  1.00 52.41 ?  37  PHE A CE1   1 
ATOM   274   C  CE2   . PHE A 1 37  ? 112.572 132.132 89.910  1.00 52.36 ?  37  PHE A CE2   1 
ATOM   275   C  CZ    . PHE A 1 37  ? 112.540 133.391 90.466  1.00 52.98 ?  37  PHE A CZ    1 
ATOM   276   N  N     . VAL A 1 38  ? 106.203 130.191 89.192  1.00 56.41 ?  38  VAL A N     1 
ATOM   277   C  CA    . VAL A 1 38  ? 104.793 130.313 88.836  1.00 55.88 ?  38  VAL A CA    1 
ATOM   278   C  C     . VAL A 1 38  ? 103.847 129.635 89.815  1.00 55.62 ?  38  VAL A C     1 
ATOM   279   O  O     . VAL A 1 38  ? 102.628 129.735 89.642  1.00 57.68 ?  38  VAL A O     1 
ATOM   280   C  CB    . VAL A 1 38  ? 104.523 129.759 87.423  1.00 54.03 ?  38  VAL A CB    1 
ATOM   281   C  CG1   . VAL A 1 38  ? 105.464 130.399 86.420  1.00 55.29 ?  38  VAL A CG1   1 
ATOM   282   C  CG2   . VAL A 1 38  ? 104.647 128.244 87.410  1.00 52.16 ?  38  VAL A CG2   1 
ATOM   283   N  N     . ASP A 1 39  ? 104.358 128.949 90.841  1.00 54.34 ?  39  ASP A N     1 
ATOM   284   C  CA    . ASP A 1 39  ? 103.489 128.338 91.832  1.00 53.08 ?  39  ASP A CA    1 
ATOM   285   C  C     . ASP A 1 39  ? 103.682 128.859 93.248  1.00 57.49 ?  39  ASP A C     1 
ATOM   286   O  O     . ASP A 1 39  ? 102.772 128.697 94.067  1.00 61.79 ?  39  ASP A O     1 
ATOM   287   C  CB    . ASP A 1 39  ? 103.675 126.812 91.842  1.00 55.36 ?  39  ASP A CB    1 
ATOM   288   C  CG    . ASP A 1 39  ? 103.406 126.185 90.488  1.00 58.49 ?  39  ASP A CG    1 
ATOM   289   O  OD1   . ASP A 1 39  ? 102.571 126.727 89.735  1.00 59.03 ?  39  ASP A OD1   1 
ATOM   290   O  OD2   . ASP A 1 39  ? 104.024 125.145 90.178  1.00 58.25 -1 39  ASP A OD2   1 
ATOM   291   N  N     . TYR A 1 40  ? 104.824 129.465 93.569  1.00 56.20 ?  40  TYR A N     1 
ATOM   292   C  CA    . TYR A 1 40  ? 105.048 130.033 94.891  1.00 55.34 ?  40  TYR A CA    1 
ATOM   293   C  C     . TYR A 1 40  ? 105.353 131.520 94.846  1.00 59.10 ?  40  TYR A C     1 
ATOM   294   O  O     . TYR A 1 40  ? 104.756 132.293 95.602  1.00 61.95 ?  40  TYR A O     1 
ATOM   295   C  CB    . TYR A 1 40  ? 106.196 129.286 95.588  1.00 54.12 ?  40  TYR A CB    1 
ATOM   296   C  CG    . TYR A 1 40  ? 106.334 129.605 97.057  1.00 54.91 ?  40  TYR A CG    1 
ATOM   297   C  CD1   . TYR A 1 40  ? 105.304 129.333 97.946  1.00 55.80 ?  40  TYR A CD1   1 
ATOM   298   C  CD2   . TYR A 1 40  ? 107.494 130.182 97.553  1.00 55.91 ?  40  TYR A CD2   1 
ATOM   299   C  CE1   . TYR A 1 40  ? 105.428 129.625 99.290  1.00 57.94 ?  40  TYR A CE1   1 
ATOM   300   C  CE2   . TYR A 1 40  ? 107.626 130.478 98.894  1.00 58.46 ?  40  TYR A CE2   1 
ATOM   301   C  CZ    . TYR A 1 40  ? 106.591 130.198 99.757  1.00 60.69 ?  40  TYR A CZ    1 
ATOM   302   O  OH    . TYR A 1 40  ? 106.718 130.491 101.095 1.00 61.32 ?  40  TYR A OH    1 
ATOM   303   N  N     . ILE A 1 41  ? 106.257 131.948 93.965  1.00 55.06 ?  41  ILE A N     1 
ATOM   304   C  CA    . ILE A 1 41  ? 106.847 133.274 94.096  1.00 54.10 ?  41  ILE A CA    1 
ATOM   305   C  C     . ILE A 1 41  ? 105.893 134.342 93.582  1.00 53.77 ?  41  ILE A C     1 
ATOM   306   O  O     . ILE A 1 41  ? 105.609 135.324 94.276  1.00 56.11 ?  41  ILE A O     1 
ATOM   307   C  CB    . ILE A 1 41  ? 108.203 133.327 93.368  1.00 53.23 ?  41  ILE A CB    1 
ATOM   308   C  CG1   . ILE A 1 41  ? 109.208 132.392 94.043  1.00 51.97 ?  41  ILE A CG1   1 
ATOM   309   C  CG2   . ILE A 1 41  ? 108.740 134.747 93.346  1.00 52.91 ?  41  ILE A CG2   1 
ATOM   310   C  CD1   . ILE A 1 41  ? 109.492 132.736 95.480  1.00 49.09 ?  41  ILE A CD1   1 
ATOM   311   N  N     . ASN A 1 42  ? 105.383 134.167 92.361  1.00 55.14 ?  42  ASN A N     1 
ATOM   312   C  CA    . ASN A 1 42  ? 104.431 135.129 91.819  1.00 57.04 ?  42  ASN A CA    1 
ATOM   313   C  C     . ASN A 1 42  ? 103.153 135.173 92.644  1.00 60.67 ?  42  ASN A C     1 
ATOM   314   O  O     . ASN A 1 42  ? 102.485 136.212 92.701  1.00 60.98 ?  42  ASN A O     1 
ATOM   315   C  CB    . ASN A 1 42  ? 104.120 134.790 90.361  1.00 56.57 ?  42  ASN A CB    1 
ATOM   316   C  CG    . ASN A 1 42  ? 105.360 134.780 89.489  1.00 57.49 ?  42  ASN A CG    1 
ATOM   317   O  OD1   . ASN A 1 42  ? 106.410 135.287 89.879  1.00 61.31 ?  42  ASN A OD1   1 
ATOM   318   N  ND2   . ASN A 1 42  ? 105.244 134.199 88.302  1.00 57.43 ?  42  ASN A ND2   1 
ATOM   319   N  N     . GLN A 1 43  ? 102.796 134.059 93.286  1.00 62.95 ?  43  GLN A N     1 
ATOM   320   C  CA    . GLN A 1 43  ? 101.625 134.050 94.156  1.00 61.34 ?  43  GLN A CA    1 
ATOM   321   C  C     . GLN A 1 43  ? 101.890 134.808 95.450  1.00 59.55 ?  43  GLN A C     1 
ATOM   322   O  O     . GLN A 1 43  ? 101.043 135.588 95.904  1.00 62.85 ?  43  GLN A O     1 
ATOM   323   C  CB    . GLN A 1 43  ? 101.205 132.610 94.454  1.00 60.93 ?  43  GLN A CB    1 
ATOM   324   C  CG    . GLN A 1 43  ? 101.387 131.645 93.289  1.00 61.60 ?  43  GLN A CG    1 
ATOM   325   C  CD    . GLN A 1 43  ? 100.346 131.825 92.199  1.00 64.24 ?  43  GLN A CD    1 
ATOM   326   O  OE1   . GLN A 1 43  ? 100.306 132.851 91.521  1.00 62.89 ?  43  GLN A OE1   1 
ATOM   327   N  NE2   . GLN A 1 43  ? 99.497  130.819 92.024  1.00 62.68 ?  43  GLN A NE2   1 
ATOM   328   N  N     . ASN A 1 44  ? 103.058 134.601 96.056  1.00 54.88 ?  44  ASN A N     1 
ATOM   329   C  CA    . ASN A 1 44  ? 103.397 135.214 97.333  1.00 56.20 ?  44  ASN A CA    1 
ATOM   330   C  C     . ASN A 1 44  ? 104.035 136.589 97.190  1.00 56.44 ?  44  ASN A C     1 
ATOM   331   O  O     . ASN A 1 44  ? 104.400 137.192 98.203  1.00 57.09 ?  44  ASN A O     1 
ATOM   332   C  CB    . ASN A 1 44  ? 104.335 134.294 98.123  1.00 56.48 ?  44  ASN A CB    1 
ATOM   333   C  CG    . ASN A 1 44  ? 103.612 133.108 98.729  1.00 59.38 ?  44  ASN A CG    1 
ATOM   334   O  OD1   . ASN A 1 44  ? 103.242 133.126 99.903  1.00 60.88 ?  44  ASN A OD1   1 
ATOM   335   N  ND2   . ASN A 1 44  ? 103.405 132.069 97.930  1.00 58.08 ?  44  ASN A ND2   1 
ATOM   336   N  N     . THR A 1 45  ? 104.183 137.096 95.971  1.00 58.13 ?  45  THR A N     1 
ATOM   337   C  CA    . THR A 1 45  ? 104.776 138.406 95.747  1.00 59.07 ?  45  THR A CA    1 
ATOM   338   C  C     . THR A 1 45  ? 103.713 139.489 95.864  1.00 59.02 ?  45  THR A C     1 
ATOM   339   O  O     . THR A 1 45  ? 102.670 139.418 95.206  1.00 60.05 ?  45  THR A O     1 
ATOM   340   C  CB    . THR A 1 45  ? 105.439 138.477 94.372  1.00 58.07 ?  45  THR A CB    1 
ATOM   341   O  OG1   . THR A 1 45  ? 106.495 137.511 94.300  1.00 59.58 ?  45  THR A OG1   1 
ATOM   342   C  CG2   . THR A 1 45  ? 106.007 139.864 94.125  1.00 55.65 ?  45  THR A CG2   1 
ATOM   343   N  N     . VAL A 1 46  ? 103.980 140.488 96.704  1.00 60.32 ?  46  VAL A N     1 
ATOM   344   C  CA    . VAL A 1 46  ? 103.115 141.660 96.775  1.00 60.71 ?  46  VAL A CA    1 
ATOM   345   C  C     . VAL A 1 46  ? 103.366 142.519 95.544  1.00 60.62 ?  46  VAL A C     1 
ATOM   346   O  O     . VAL A 1 46  ? 104.503 142.926 95.275  1.00 62.72 ?  46  VAL A O     1 
ATOM   347   C  CB    . VAL A 1 46  ? 103.365 142.452 98.064  1.00 60.03 ?  46  VAL A CB    1 
ATOM   348   C  CG1   . VAL A 1 46  ? 102.323 143.543 98.224  1.00 60.24 ?  46  VAL A CG1   1 
ATOM   349   C  CG2   . VAL A 1 46  ? 103.360 141.527 99.264  1.00 59.25 ?  46  VAL A CG2   1 
ATOM   350   N  N     . PHE A 1 47  ? 102.308 142.801 94.792  1.00 64.09 ?  47  PHE A N     1 
ATOM   351   C  CA    . PHE A 1 47  ? 102.401 143.602 93.581  1.00 66.23 ?  47  PHE A CA    1 
ATOM   352   C  C     . PHE A 1 47  ? 101.605 144.884 93.765  1.00 67.45 ?  47  PHE A C     1 
ATOM   353   O  O     . PHE A 1 47  ? 100.455 144.849 94.213  1.00 67.74 ?  47  PHE A O     1 
ATOM   354   C  CB    . PHE A 1 47  ? 101.893 142.829 92.361  1.00 67.11 ?  47  PHE A CB    1 
ATOM   355   C  CG    . PHE A 1 47  ? 102.035 143.581 91.068  1.00 68.09 ?  47  PHE A CG    1 
ATOM   356   C  CD1   . PHE A 1 47  ? 103.243 143.601 90.392  1.00 67.12 ?  47  PHE A CD1   1 
ATOM   357   C  CD2   . PHE A 1 47  ? 100.959 144.264 90.526  1.00 66.60 ?  47  PHE A CD2   1 
ATOM   358   C  CE1   . PHE A 1 47  ? 103.378 144.291 89.203  1.00 67.08 ?  47  PHE A CE1   1 
ATOM   359   C  CE2   . PHE A 1 47  ? 101.086 144.955 89.336  1.00 67.40 ?  47  PHE A CE2   1 
ATOM   360   C  CZ    . PHE A 1 47  ? 102.298 144.970 88.674  1.00 68.47 ?  47  PHE A CZ    1 
ATOM   361   N  N     . PHE A 1 48  ? 102.224 146.008 93.424  1.00 66.92 ?  48  PHE A N     1 
ATOM   362   C  CA    . PHE A 1 48  ? 101.618 147.321 93.548  1.00 64.94 ?  48  PHE A CA    1 
ATOM   363   C  C     . PHE A 1 48  ? 101.263 147.851 92.167  1.00 65.55 ?  48  PHE A C     1 
ATOM   364   O  O     . PHE A 1 48  ? 101.798 147.402 91.149  1.00 67.21 ?  48  PHE A O     1 
ATOM   365   C  CB    . PHE A 1 48  ? 102.557 148.296 94.268  1.00 63.60 ?  48  PHE A CB    1 
ATOM   366   C  CG    . PHE A 1 48  ? 102.998 147.826 95.629  1.00 63.28 ?  48  PHE A CG    1 
ATOM   367   C  CD1   . PHE A 1 48  ? 102.488 148.408 96.774  1.00 64.12 ?  48  PHE A CD1   1 
ATOM   368   C  CD2   . PHE A 1 48  ? 103.941 146.819 95.760  1.00 63.11 ?  48  PHE A CD2   1 
ATOM   369   C  CE1   . PHE A 1 48  ? 102.893 147.981 98.021  1.00 65.24 ?  48  PHE A CE1   1 
ATOM   370   C  CE2   . PHE A 1 48  ? 104.349 146.391 97.005  1.00 63.83 ?  48  PHE A CE2   1 
ATOM   371   C  CZ    . PHE A 1 48  ? 103.825 146.972 98.135  1.00 64.21 ?  48  PHE A CZ    1 
ATOM   372   N  N     . HIS A 1 49  ? 100.339 148.815 92.140  1.00 68.07 ?  49  HIS A N     1 
ATOM   373   C  CA    . HIS A 1 49  ? 99.885  149.363 90.865  1.00 70.19 ?  49  HIS A CA    1 
ATOM   374   C  C     . HIS A 1 49  ? 101.030 150.021 90.106  1.00 69.96 ?  49  HIS A C     1 
ATOM   375   O  O     . HIS A 1 49  ? 101.162 149.840 88.890  1.00 70.21 ?  49  HIS A O     1 
ATOM   376   C  CB    . HIS A 1 49  ? 98.747  150.358 91.097  1.00 69.80 ?  49  HIS A CB    1 
ATOM   377   C  CG    . HIS A 1 49  ? 97.582  149.781 91.837  1.00 71.45 ?  49  HIS A CG    1 
ATOM   378   N  ND1   . HIS A 1 49  ? 97.611  149.525 93.191  1.00 71.84 ?  49  HIS A ND1   1 
ATOM   379   C  CD2   . HIS A 1 49  ? 96.352  149.408 91.411  1.00 70.55 ?  49  HIS A CD2   1 
ATOM   380   C  CE1   . HIS A 1 49  ? 96.450  149.020 93.567  1.00 69.89 ?  49  HIS A CE1   1 
ATOM   381   N  NE2   . HIS A 1 49  ? 95.668  148.938 92.506  1.00 71.70 ?  49  HIS A NE2   1 
ATOM   382   N  N     . ASN A 1 50  ? 101.867 150.783 90.804  1.00 67.49 ?  50  ASN A N     1 
ATOM   383   C  CA    . ASN A 1 50  ? 103.039 151.397 90.202  1.00 66.95 ?  50  ASN A CA    1 
ATOM   384   C  C     . ASN A 1 50  ? 104.187 151.358 91.200  1.00 65.92 ?  50  ASN A C     1 
ATOM   385   O  O     . ASN A 1 50  ? 103.994 151.101 92.390  1.00 67.91 ?  50  ASN A O     1 
ATOM   386   C  CB    . ASN A 1 50  ? 102.762 152.839 89.747  1.00 66.30 ?  50  ASN A CB    1 
ATOM   387   C  CG    . ASN A 1 50  ? 102.183 153.703 90.850  1.00 66.97 ?  50  ASN A CG    1 
ATOM   388   O  OD1   . ASN A 1 50  ? 102.059 153.272 91.995  1.00 66.48 ?  50  ASN A OD1   1 
ATOM   389   N  ND2   . ASN A 1 50  ? 101.826 154.934 90.508  1.00 66.32 ?  50  ASN A ND2   1 
ATOM   390   N  N     . LEU A 1 51  ? 105.397 151.607 90.692  1.00 60.19 ?  51  LEU A N     1 
ATOM   391   C  CA    . LEU A 1 51  ? 106.578 151.582 91.547  1.00 60.44 ?  51  LEU A CA    1 
ATOM   392   C  C     . LEU A 1 51  ? 106.515 152.657 92.626  1.00 62.18 ?  51  LEU A C     1 
ATOM   393   O  O     . LEU A 1 51  ? 107.091 152.483 93.706  1.00 64.40 ?  51  LEU A O     1 
ATOM   394   C  CB    . LEU A 1 51  ? 107.839 151.750 90.700  1.00 61.12 ?  51  LEU A CB    1 
ATOM   395   C  CG    . LEU A 1 51  ? 109.178 151.783 91.443  1.00 58.98 ?  51  LEU A CG    1 
ATOM   396   C  CD1   . LEU A 1 51  ? 109.441 150.457 92.132  1.00 58.21 ?  51  LEU A CD1   1 
ATOM   397   C  CD2   . LEU A 1 51  ? 110.309 152.141 90.497  1.00 58.63 ?  51  LEU A CD2   1 
ATOM   398   N  N     . LYS A 1 52  ? 105.829 153.771 92.355  1.00 62.24 ?  52  LYS A N     1 
ATOM   399   C  CA    . LYS A 1 52  ? 105.711 154.828 93.354  1.00 60.33 ?  52  LYS A CA    1 
ATOM   400   C  C     . LYS A 1 52  ? 104.975 154.337 94.592  1.00 61.87 ?  52  LYS A C     1 
ATOM   401   O  O     . LYS A 1 52  ? 105.404 154.598 95.723  1.00 61.87 ?  52  LYS A O     1 
ATOM   402   C  CB    . LYS A 1 52  ? 105.001 156.040 92.754  1.00 59.33 ?  52  LYS A CB    1 
ATOM   403   C  CG    . LYS A 1 52  ? 105.288 157.347 93.474  1.00 62.17 ?  52  LYS A CG    1 
ATOM   404   C  CD    . LYS A 1 52  ? 105.187 158.529 92.525  1.00 63.90 ?  52  LYS A CD    1 
ATOM   405   C  CE    . LYS A 1 52  ? 106.079 159.677 92.970  1.00 63.03 ?  52  LYS A CE    1 
ATOM   406   N  NZ    . LYS A 1 52  ? 106.313 159.665 94.440  1.00 61.51 1  52  LYS A NZ    1 
ATOM   407   N  N     . GLU A 1 53  ? 103.869 153.617 94.397  1.00 65.07 ?  53  GLU A N     1 
ATOM   408   C  CA    . GLU A 1 53  ? 103.137 153.064 95.530  1.00 65.62 ?  53  GLU A CA    1 
ATOM   409   C  C     . GLU A 1 53  ? 103.990 152.057 96.289  1.00 64.75 ?  53  GLU A C     1 
ATOM   410   O  O     . GLU A 1 53  ? 103.973 152.025 97.523  1.00 65.93 ?  53  GLU A O     1 
ATOM   411   C  CB    . GLU A 1 53  ? 101.836 152.420 95.050  1.00 65.41 ?  53  GLU A CB    1 
ATOM   412   C  CG    . GLU A 1 53  ? 101.129 151.571 96.094  1.00 67.11 ?  53  GLU A CG    1 
ATOM   413   C  CD    . GLU A 1 53  ? 99.878  150.907 95.551  1.00 69.03 ?  53  GLU A CD    1 
ATOM   414   O  OE1   . GLU A 1 53  ? 99.423  151.299 94.456  1.00 69.01 ?  53  GLU A OE1   1 
ATOM   415   O  OE2   . GLU A 1 53  ? 99.351  149.993 96.219  1.00 68.53 -1 53  GLU A OE2   1 
ATOM   416   N  N     . LYS A 1 54  ? 104.754 151.237 95.566  1.00 60.53 ?  54  LYS A N     1 
ATOM   417   C  CA    . LYS A 1 54  ? 105.624 150.259 96.212  1.00 62.09 ?  54  LYS A CA    1 
ATOM   418   C  C     . LYS A 1 54  ? 106.670 150.941 97.083  1.00 58.42 ?  54  LYS A C     1 
ATOM   419   O  O     . LYS A 1 54  ? 106.877 150.561 98.243  1.00 60.89 ?  54  LYS A O     1 
ATOM   420   C  CB    . LYS A 1 54  ? 106.297 149.387 95.153  1.00 61.73 ?  54  LYS A CB    1 
ATOM   421   C  CG    . LYS A 1 54  ? 107.374 148.471 95.697  1.00 59.32 ?  54  LYS A CG    1 
ATOM   422   C  CD    . LYS A 1 54  ? 107.691 147.358 94.721  1.00 59.69 ?  54  LYS A CD    1 
ATOM   423   C  CE    . LYS A 1 54  ? 108.598 146.319 95.348  1.00 60.84 ?  54  LYS A CE    1 
ATOM   424   N  NZ    . LYS A 1 54  ? 108.526 145.017 94.631  1.00 61.90 1  54  LYS A NZ    1 
ATOM   425   N  N     . LEU A 1 55  ? 107.341 151.957 96.539  1.00 56.48 ?  55  LEU A N     1 
ATOM   426   C  CA    . LEU A 1 55  ? 108.382 152.643 97.296  1.00 58.32 ?  55  LEU A CA    1 
ATOM   427   C  C     . LEU A 1 55  ? 107.798 153.396 98.483  1.00 61.53 ?  55  LEU A C     1 
ATOM   428   O  O     . LEU A 1 55  ? 108.390 153.405 99.568  1.00 63.78 ?  55  LEU A O     1 
ATOM   429   C  CB    . LEU A 1 55  ? 109.160 153.587 96.384  1.00 59.39 ?  55  LEU A CB    1 
ATOM   430   C  CG    . LEU A 1 55  ? 110.028 152.893 95.334  1.00 59.74 ?  55  LEU A CG    1 
ATOM   431   C  CD1   . LEU A 1 55  ? 110.684 153.913 94.428  1.00 59.60 ?  55  LEU A CD1   1 
ATOM   432   C  CD2   . LEU A 1 55  ? 111.071 152.009 95.998  1.00 59.41 ?  55  LEU A CD2   1 
ATOM   433   N  N     . ASP A 1 56  ? 106.638 154.034 98.302  1.00 65.92 ?  56  ASP A N     1 
ATOM   434   C  CA    . ASP A 1 56  ? 105.993 154.713 99.419  1.00 64.75 ?  56  ASP A CA    1 
ATOM   435   C  C     . ASP A 1 56  ? 105.607 153.725 100.512 1.00 64.19 ?  56  ASP A C     1 
ATOM   436   O  O     . ASP A 1 56  ? 105.804 153.995 101.702 1.00 65.16 ?  56  ASP A O     1 
ATOM   437   C  CB    . ASP A 1 56  ? 104.768 155.481 98.925  1.00 65.50 ?  56  ASP A CB    1 
ATOM   438   C  CG    . ASP A 1 56  ? 105.137 156.714 98.126  1.00 68.31 ?  56  ASP A CG    1 
ATOM   439   O  OD1   . ASP A 1 56  ? 106.268 157.216 98.292  1.00 67.57 ?  56  ASP A OD1   1 
ATOM   440   O  OD2   . ASP A 1 56  ? 104.297 157.183 97.329  1.00 67.50 -1 56  ASP A OD2   1 
ATOM   441   N  N     . TYR A 1 57  ? 105.069 152.567 100.124 1.00 59.50 ?  57  TYR A N     1 
ATOM   442   C  CA    . TYR A 1 57  ? 104.698 151.546 101.095 1.00 62.04 ?  57  TYR A CA    1 
ATOM   443   C  C     . TYR A 1 57  ? 105.916 151.042 101.855 1.00 61.86 ?  57  TYR A C     1 
ATOM   444   O  O     . TYR A 1 57  ? 105.853 150.821 103.070 1.00 63.68 ?  57  TYR A O     1 
ATOM   445   C  CB    . TYR A 1 57  ? 104.003 150.389 100.375 1.00 61.52 ?  57  TYR A CB    1 
ATOM   446   C  CG    . TYR A 1 57  ? 103.738 149.176 101.234 1.00 62.14 ?  57  TYR A CG    1 
ATOM   447   C  CD1   . TYR A 1 57  ? 102.672 149.148 102.120 1.00 62.07 ?  57  TYR A CD1   1 
ATOM   448   C  CD2   . TYR A 1 57  ? 104.567 148.065 101.175 1.00 63.16 ?  57  TYR A CD2   1 
ATOM   449   C  CE1   . TYR A 1 57  ? 102.424 148.038 102.901 1.00 62.91 ?  57  TYR A CE1   1 
ATOM   450   C  CE2   . TYR A 1 57  ? 104.333 146.957 101.959 1.00 63.73 ?  57  TYR A CE2   1 
ATOM   451   C  CZ    . TYR A 1 57  ? 103.262 146.950 102.823 1.00 63.36 ?  57  TYR A CZ    1 
ATOM   452   O  OH    . TYR A 1 57  ? 103.025 145.844 103.606 1.00 62.05 ?  57  TYR A OH    1 
ATOM   453   N  N     . LEU A 1 58  ? 107.035 150.846 101.153 1.00 56.04 ?  58  LEU A N     1 
ATOM   454   C  CA    . LEU A 1 58  ? 108.225 150.309 101.801 1.00 54.62 ?  58  LEU A CA    1 
ATOM   455   C  C     . LEU A 1 58  ? 108.878 151.337 102.717 1.00 55.12 ?  58  LEU A C     1 
ATOM   456   O  O     . LEU A 1 58  ? 109.382 150.988 103.790 1.00 58.06 ?  58  LEU A O     1 
ATOM   457   C  CB    . LEU A 1 58  ? 109.215 149.816 100.747 1.00 56.32 ?  58  LEU A CB    1 
ATOM   458   C  CG    . LEU A 1 58  ? 108.749 148.596 99.951  1.00 56.27 ?  58  LEU A CG    1 
ATOM   459   C  CD1   . LEU A 1 58  ? 109.524 148.472 98.655  1.00 55.04 ?  58  LEU A CD1   1 
ATOM   460   C  CD2   . LEU A 1 58  ? 108.881 147.333 100.777 1.00 56.23 ?  58  LEU A CD2   1 
ATOM   461   N  N     . VAL A 1 59  ? 108.887 152.609 102.314 1.00 60.11 ?  59  VAL A N     1 
ATOM   462   C  CA    . VAL A 1 59  ? 109.481 153.645 103.154 1.00 62.24 ?  59  VAL A CA    1 
ATOM   463   C  C     . VAL A 1 59  ? 108.618 153.897 104.384 1.00 64.10 ?  59  VAL A C     1 
ATOM   464   O  O     . VAL A 1 59  ? 109.125 154.003 105.506 1.00 63.20 ?  59  VAL A O     1 
ATOM   465   C  CB    . VAL A 1 59  ? 109.702 154.934 102.342 1.00 62.74 ?  59  VAL A CB    1 
ATOM   466   C  CG1   . VAL A 1 59  ? 110.137 156.067 103.254 1.00 60.59 ?  59  VAL A CG1   1 
ATOM   467   C  CG2   . VAL A 1 59  ? 110.740 154.702 101.256 1.00 62.18 ?  59  VAL A CG2   1 
ATOM   468   N  N     . GLU A 1 60  ? 107.299 153.994 104.193 1.00 64.88 ?  60  GLU A N     1 
ATOM   469   C  CA    . GLU A 1 60  ? 106.411 154.338 105.299 1.00 64.28 ?  60  GLU A CA    1 
ATOM   470   C  C     . GLU A 1 60  ? 106.388 153.252 106.367 1.00 65.21 ?  60  GLU A C     1 
ATOM   471   O  O     . GLU A 1 60  ? 106.355 153.555 107.566 1.00 67.47 ?  60  GLU A O     1 
ATOM   472   C  CB    . GLU A 1 60  ? 105.001 154.607 104.773 1.00 64.16 ?  60  GLU A CB    1 
ATOM   473   C  CG    . GLU A 1 60  ? 104.868 155.915 104.007 1.00 65.72 ?  60  GLU A CG    1 
ATOM   474   C  CD    . GLU A 1 60  ? 103.678 155.926 103.066 1.00 69.17 ?  60  GLU A CD    1 
ATOM   475   O  OE1   . GLU A 1 60  ? 102.836 155.008 103.157 1.00 68.12 ?  60  GLU A OE1   1 
ATOM   476   O  OE2   . GLU A 1 60  ? 103.585 156.853 102.233 1.00 67.57 -1 60  GLU A OE2   1 
ATOM   477   N  N     . ASN A 1 61  ? 106.404 151.983 105.961 1.00 59.25 ?  61  ASN A N     1 
ATOM   478   C  CA    . ASN A 1 61  ? 106.323 150.879 106.910 1.00 60.01 ?  61  ASN A CA    1 
ATOM   479   C  C     . ASN A 1 61  ? 107.683 150.401 107.393 1.00 61.33 ?  61  ASN A C     1 
ATOM   480   O  O     . ASN A 1 61  ? 107.814 149.223 107.750 1.00 64.86 ?  61  ASN A O     1 
ATOM   481   C  CB    . ASN A 1 61  ? 105.541 149.713 106.306 1.00 60.81 ?  61  ASN A CB    1 
ATOM   482   C  CG    . ASN A 1 61  ? 104.185 150.134 105.790 1.00 62.46 ?  61  ASN A CG    1 
ATOM   483   O  OD1   . ASN A 1 61  ? 103.895 151.322 105.673 1.00 63.19 ?  61  ASN A OD1   1 
ATOM   484   N  ND2   . ASN A 1 61  ? 103.330 149.161 105.522 1.00 61.88 ?  61  ASN A ND2   1 
ATOM   485   N  N     . GLN A 1 62  ? 108.686 151.279 107.397 1.00 57.49 ?  62  GLN A N     1 
ATOM   486   C  CA    . GLN A 1 62  ? 109.979 151.014 108.028 1.00 58.44 ?  62  GLN A CA    1 
ATOM   487   C  C     . GLN A 1 62  ? 110.713 149.847 107.374 1.00 57.89 ?  62  GLN A C     1 
ATOM   488   O  O     . GLN A 1 62  ? 111.477 149.136 108.031 1.00 58.51 ?  62  GLN A O     1 
ATOM   489   C  CB    . GLN A 1 62  ? 109.816 150.761 109.530 1.00 58.21 ?  62  GLN A CB    1 
ATOM   490   C  CG    . GLN A 1 62  ? 109.125 151.886 110.289 1.00 57.65 ?  62  GLN A CG    1 
ATOM   491   C  CD    . GLN A 1 62  ? 109.752 153.241 110.039 1.00 60.19 ?  62  GLN A CD    1 
ATOM   492   O  OE1   . GLN A 1 62  ? 110.720 153.623 110.696 1.00 59.91 ?  62  GLN A OE1   1 
ATOM   493   N  NE2   . GLN A 1 62  ? 109.205 153.977 109.079 1.00 58.82 ?  62  GLN A NE2   1 
ATOM   494   N  N     . TYR A 1 63  ? 110.489 149.633 106.078 1.00 55.04 ?  63  TYR A N     1 
ATOM   495   C  CA    . TYR A 1 63  ? 111.227 148.609 105.351 1.00 53.55 ?  63  TYR A CA    1 
ATOM   496   C  C     . TYR A 1 63  ? 112.491 149.164 104.710 1.00 53.47 ?  63  TYR A C     1 
ATOM   497   O  O     . TYR A 1 63  ? 113.536 148.503 104.728 1.00 52.88 ?  63  TYR A O     1 
ATOM   498   C  CB    . TYR A 1 63  ? 110.341 147.971 104.278 1.00 52.78 ?  63  TYR A CB    1 
ATOM   499   C  CG    . TYR A 1 63  ? 109.286 147.041 104.829 1.00 53.89 ?  63  TYR A CG    1 
ATOM   500   C  CD1   . TYR A 1 63  ? 109.626 146.010 105.692 1.00 52.87 ?  63  TYR A CD1   1 
ATOM   501   C  CD2   . TYR A 1 63  ? 107.951 147.192 104.482 1.00 55.05 ?  63  TYR A CD2   1 
ATOM   502   C  CE1   . TYR A 1 63  ? 108.666 145.157 106.198 1.00 53.91 ?  63  TYR A CE1   1 
ATOM   503   C  CE2   . TYR A 1 63  ? 106.984 146.345 104.982 1.00 55.36 ?  63  TYR A CE2   1 
ATOM   504   C  CZ    . TYR A 1 63  ? 107.347 145.330 105.840 1.00 56.36 ?  63  TYR A CZ    1 
ATOM   505   O  OH    . TYR A 1 63  ? 106.385 144.484 106.339 1.00 55.76 ?  63  TYR A OH    1 
ATOM   506   N  N     . TYR A 1 64  ? 112.418 150.365 104.151 1.00 49.94 ?  64  TYR A N     1 
ATOM   507   C  CA    . TYR A 1 64  ? 113.545 151.012 103.500 1.00 48.26 ?  64  TYR A CA    1 
ATOM   508   C  C     . TYR A 1 64  ? 114.000 152.217 104.311 1.00 50.88 ?  64  TYR A C     1 
ATOM   509   O  O     . TYR A 1 64  ? 113.389 152.593 105.314 1.00 53.87 ?  64  TYR A O     1 
ATOM   510   C  CB    . TYR A 1 64  ? 113.178 151.447 102.079 1.00 47.96 ?  64  TYR A CB    1 
ATOM   511   C  CG    . TYR A 1 64  ? 113.207 150.332 101.065 1.00 50.04 ?  64  TYR A CG    1 
ATOM   512   C  CD1   . TYR A 1 64  ? 113.642 149.060 101.412 1.00 48.97 ?  64  TYR A CD1   1 
ATOM   513   C  CD2   . TYR A 1 64  ? 112.799 150.550 99.758  1.00 49.89 ?  64  TYR A CD2   1 
ATOM   514   C  CE1   . TYR A 1 64  ? 113.668 148.040 100.487 1.00 45.60 ?  64  TYR A CE1   1 
ATOM   515   C  CE2   . TYR A 1 64  ? 112.824 149.538 98.828  1.00 48.10 ?  64  TYR A CE2   1 
ATOM   516   C  CZ    . TYR A 1 64  ? 113.257 148.285 99.196  1.00 47.41 ?  64  TYR A CZ    1 
ATOM   517   O  OH    . TYR A 1 64  ? 113.278 147.276 98.265  1.00 50.79 ?  64  TYR A OH    1 
ATOM   518   N  N     . GLU A 1 65  ? 115.089 152.824 103.858 1.00 53.79 ?  65  GLU A N     1 
ATOM   519   C  CA    . GLU A 1 65  ? 115.585 154.070 104.424 1.00 52.12 ?  65  GLU A CA    1 
ATOM   520   C  C     . GLU A 1 65  ? 115.227 155.215 103.488 1.00 55.07 ?  65  GLU A C     1 
ATOM   521   O  O     . GLU A 1 65  ? 115.449 155.126 102.276 1.00 56.78 ?  65  GLU A O     1 
ATOM   522   C  CB    . GLU A 1 65  ? 117.097 154.015 104.644 1.00 52.60 ?  65  GLU A CB    1 
ATOM   523   C  CG    . GLU A 1 65  ? 117.568 152.797 105.416 1.00 51.39 ?  65  GLU A CG    1 
ATOM   524   C  CD    . GLU A 1 65  ? 119.079 152.716 105.508 1.00 55.09 ?  65  GLU A CD    1 
ATOM   525   O  OE1   . GLU A 1 65  ? 119.756 153.100 104.531 1.00 57.01 ?  65  GLU A OE1   1 
ATOM   526   O  OE2   . GLU A 1 65  ? 119.588 152.272 106.558 1.00 54.12 -1 65  GLU A OE2   1 
ATOM   527   N  N     . GLU A 1 66  ? 114.665 156.283 104.052 1.00 58.01 ?  66  GLU A N     1 
ATOM   528   C  CA    . GLU A 1 66  ? 114.263 157.426 103.242 1.00 56.33 ?  66  GLU A CA    1 
ATOM   529   C  C     . GLU A 1 66  ? 115.454 158.250 102.771 1.00 56.91 ?  66  GLU A C     1 
ATOM   530   O  O     . GLU A 1 66  ? 115.386 158.855 101.696 1.00 57.92 ?  66  GLU A O     1 
ATOM   531   C  CB    . GLU A 1 66  ? 113.292 158.304 104.037 1.00 57.09 ?  66  GLU A CB    1 
ATOM   532   C  CG    . GLU A 1 66  ? 112.872 159.598 103.352 1.00 59.42 ?  66  GLU A CG    1 
ATOM   533   C  CD    . GLU A 1 66  ? 111.954 159.368 102.165 1.00 61.01 ?  66  GLU A CD    1 
ATOM   534   O  OE1   . GLU A 1 66  ? 110.756 159.707 102.267 1.00 58.42 ?  66  GLU A OE1   1 
ATOM   535   O  OE2   . GLU A 1 66  ? 112.429 158.863 101.125 1.00 62.31 -1 66  GLU A OE2   1 
ATOM   536   N  N     . GLU A 1 67  ? 116.543 158.274 103.543 1.00 58.05 ?  67  GLU A N     1 
ATOM   537   C  CA    . GLU A 1 67  ? 117.650 159.180 103.251 1.00 56.47 ?  67  GLU A CA    1 
ATOM   538   C  C     . GLU A 1 67  ? 118.298 158.870 101.907 1.00 57.31 ?  67  GLU A C     1 
ATOM   539   O  O     . GLU A 1 67  ? 118.562 159.780 101.113 1.00 57.76 ?  67  GLU A O     1 
ATOM   540   C  CB    . GLU A 1 67  ? 118.684 159.116 104.376 1.00 56.92 ?  67  GLU A CB    1 
ATOM   541   C  CG    . GLU A 1 67  ? 118.774 157.762 105.058 1.00 58.91 ?  67  GLU A CG    1 
ATOM   542   C  CD    . GLU A 1 67  ? 117.971 157.702 106.342 1.00 59.42 ?  67  GLU A CD    1 
ATOM   543   O  OE1   . GLU A 1 67  ? 116.725 157.699 106.267 1.00 57.57 ?  67  GLU A OE1   1 
ATOM   544   O  OE2   . GLU A 1 67  ? 118.587 157.662 107.427 1.00 62.17 -1 67  GLU A OE2   1 
ATOM   545   N  N     . PHE A 1 68  ? 118.562 157.593 101.628 1.00 54.61 ?  68  PHE A N     1 
ATOM   546   C  CA    . PHE A 1 68  ? 119.250 157.251 100.388 1.00 52.02 ?  68  PHE A CA    1 
ATOM   547   C  C     . PHE A 1 68  ? 118.323 157.324 99.182  1.00 51.81 ?  68  PHE A C     1 
ATOM   548   O  O     . PHE A 1 68  ? 118.778 157.633 98.076  1.00 55.05 ?  68  PHE A O     1 
ATOM   549   C  CB    . PHE A 1 68  ? 119.895 155.865 100.500 1.00 51.38 ?  68  PHE A CB    1 
ATOM   550   C  CG    . PHE A 1 68  ? 119.006 154.733 100.069 1.00 50.85 ?  68  PHE A CG    1 
ATOM   551   C  CD1   . PHE A 1 68  ? 118.087 154.185 100.945 1.00 51.28 ?  68  PHE A CD1   1 
ATOM   552   C  CD2   . PHE A 1 68  ? 119.114 154.195 98.797  1.00 48.03 ?  68  PHE A CD2   1 
ATOM   553   C  CE1   . PHE A 1 68  ? 117.276 153.139 100.553 1.00 48.97 ?  68  PHE A CE1   1 
ATOM   554   C  CE2   . PHE A 1 68  ? 118.308 153.149 98.402  1.00 46.98 ?  68  PHE A CE2   1 
ATOM   555   C  CZ    . PHE A 1 68  ? 117.390 152.619 99.282  1.00 48.15 ?  68  PHE A CZ    1 
ATOM   556   N  N     . LEU A 1 69  ? 117.031 157.051 99.369  1.00 50.98 ?  69  LEU A N     1 
ATOM   557   C  CA    . LEU A 1 69  ? 116.081 157.176 98.271  1.00 53.18 ?  69  LEU A CA    1 
ATOM   558   C  C     . LEU A 1 69  ? 115.736 158.627 97.970  1.00 53.68 ?  69  LEU A C     1 
ATOM   559   O  O     . LEU A 1 69  ? 115.208 158.914 96.890  1.00 54.19 ?  69  LEU A O     1 
ATOM   560   C  CB    . LEU A 1 69  ? 114.804 156.396 98.583  1.00 54.09 ?  69  LEU A CB    1 
ATOM   561   C  CG    . LEU A 1 69  ? 114.866 154.882 98.379  1.00 52.44 ?  69  LEU A CG    1 
ATOM   562   C  CD1   . LEU A 1 69  ? 113.642 154.208 98.975  1.00 51.87 ?  69  LEU A CD1   1 
ATOM   563   C  CD2   . LEU A 1 69  ? 115.003 154.546 96.906  1.00 50.13 ?  69  LEU A CD2   1 
ATOM   564   N  N     . SER A 1 70  ? 116.022 159.545 98.893  1.00 55.83 ?  70  SER A N     1 
ATOM   565   C  CA    . SER A 1 70  ? 115.705 160.954 98.697  1.00 54.06 ?  70  SER A CA    1 
ATOM   566   C  C     . SER A 1 70  ? 116.726 161.682 97.835  1.00 53.45 ?  70  SER A C     1 
ATOM   567   O  O     . SER A 1 70  ? 116.476 162.829 97.451  1.00 56.79 ?  70  SER A O     1 
ATOM   568   C  CB    . SER A 1 70  ? 115.587 161.658 100.052 1.00 54.37 ?  70  SER A CB    1 
ATOM   569   O  OG    . SER A 1 70  ? 116.853 161.780 100.673 1.00 54.27 ?  70  SER A OG    1 
ATOM   570   N  N     . LEU A 1 71  ? 117.859 161.054 97.522  1.00 50.47 ?  71  LEU A N     1 
ATOM   571   C  CA    . LEU A 1 71  ? 118.860 161.678 96.669  1.00 50.14 ?  71  LEU A CA    1 
ATOM   572   C  C     . LEU A 1 71  ? 118.533 161.559 95.188  1.00 50.99 ?  71  LEU A C     1 
ATOM   573   O  O     . LEU A 1 71  ? 119.233 162.159 94.365  1.00 50.24 ?  71  LEU A O     1 
ATOM   574   C  CB    . LEU A 1 71  ? 120.238 161.067 96.938  1.00 48.19 ?  71  LEU A CB    1 
ATOM   575   C  CG    . LEU A 1 71  ? 120.568 160.766 98.399  1.00 49.88 ?  71  LEU A CG    1 
ATOM   576   C  CD1   . LEU A 1 71  ? 121.571 159.633 98.496  1.00 51.77 ?  71  LEU A CD1   1 
ATOM   577   C  CD2   . LEU A 1 71  ? 121.095 162.012 99.089  1.00 51.24 ?  71  LEU A CD2   1 
ATOM   578   N  N     . TYR A 1 72  ? 117.495 160.807 94.831  1.00 48.11 ?  72  TYR A N     1 
ATOM   579   C  CA    . TYR A 1 72  ? 117.071 160.647 93.450  1.00 50.38 ?  72  TYR A CA    1 
ATOM   580   C  C     . TYR A 1 72  ? 115.636 161.126 93.295  1.00 52.50 ?  72  TYR A C     1 
ATOM   581   O  O     . TYR A 1 72  ? 114.788 160.858 94.150  1.00 52.67 ?  72  TYR A O     1 
ATOM   582   C  CB    . TYR A 1 72  ? 117.152 159.185 92.993  1.00 48.01 ?  72  TYR A CB    1 
ATOM   583   C  CG    . TYR A 1 72  ? 118.435 158.467 93.331  1.00 47.76 ?  72  TYR A CG    1 
ATOM   584   C  CD1   . TYR A 1 72  ? 118.608 157.858 94.567  1.00 46.66 ?  72  TYR A CD1   1 
ATOM   585   C  CD2   . TYR A 1 72  ? 119.460 158.367 92.402  1.00 46.11 ?  72  TYR A CD2   1 
ATOM   586   C  CE1   . TYR A 1 72  ? 119.771 157.193 94.875  1.00 44.18 ?  72  TYR A CE1   1 
ATOM   587   C  CE2   . TYR A 1 72  ? 120.626 157.699 92.700  1.00 42.59 ?  72  TYR A CE2   1 
ATOM   588   C  CZ    . TYR A 1 72  ? 120.776 157.116 93.938  1.00 44.18 ?  72  TYR A CZ    1 
ATOM   589   O  OH    . TYR A 1 72  ? 121.940 156.450 94.240  1.00 49.45 ?  72  TYR A OH    1 
ATOM   590   N  N     . SER A 1 73  ? 115.369 161.833 92.202  1.00 55.03 ?  73  SER A N     1 
ATOM   591   C  CA    . SER A 1 73  ? 113.991 162.059 91.798  1.00 56.45 ?  73  SER A CA    1 
ATOM   592   C  C     . SER A 1 73  ? 113.370 160.732 91.378  1.00 57.84 ?  73  SER A C     1 
ATOM   593   O  O     . SER A 1 73  ? 114.060 159.827 90.903  1.00 58.76 ?  73  SER A O     1 
ATOM   594   C  CB    . SER A 1 73  ? 113.921 163.066 90.651  1.00 57.18 ?  73  SER A CB    1 
ATOM   595   O  OG    . SER A 1 73  ? 114.124 162.432 89.402  1.00 57.54 ?  73  SER A OG    1 
ATOM   596   N  N     . PHE A 1 74  ? 112.054 160.612 91.570  1.00 58.15 ?  74  PHE A N     1 
ATOM   597   C  CA    . PHE A 1 74  ? 111.403 159.339 91.288  1.00 55.90 ?  74  PHE A CA    1 
ATOM   598   C  C     . PHE A 1 74  ? 111.537 158.918 89.832  1.00 58.32 ?  74  PHE A C     1 
ATOM   599   O  O     . PHE A 1 74  ? 111.462 157.721 89.539  1.00 60.17 ?  74  PHE A O     1 
ATOM   600   C  CB    . PHE A 1 74  ? 109.923 159.373 91.663  1.00 58.40 ?  74  PHE A CB    1 
ATOM   601   C  CG    . PHE A 1 74  ? 109.227 158.069 91.416  1.00 58.85 ?  74  PHE A CG    1 
ATOM   602   C  CD1   . PHE A 1 74  ? 109.455 156.982 92.241  1.00 57.77 ?  74  PHE A CD1   1 
ATOM   603   C  CD2   . PHE A 1 74  ? 108.378 157.918 90.333  1.00 58.58 ?  74  PHE A CD2   1 
ATOM   604   C  CE1   . PHE A 1 74  ? 108.834 155.775 92.001  1.00 59.26 ?  74  PHE A CE1   1 
ATOM   605   C  CE2   . PHE A 1 74  ? 107.753 156.714 90.090  1.00 59.84 ?  74  PHE A CE2   1 
ATOM   606   C  CZ    . PHE A 1 74  ? 107.983 155.642 90.923  1.00 61.18 ?  74  PHE A CZ    1 
ATOM   607   N  N     . GLU A 1 75  ? 111.734 159.862 88.910  1.00 61.63 ?  75  GLU A N     1 
ATOM   608   C  CA    . GLU A 1 75  ? 111.990 159.476 87.528  1.00 61.08 ?  75  GLU A CA    1 
ATOM   609   C  C     . GLU A 1 75  ? 113.301 158.708 87.412  1.00 62.99 ?  75  GLU A C     1 
ATOM   610   O  O     . GLU A 1 75  ? 113.394 157.730 86.663  1.00 62.51 ?  75  GLU A O     1 
ATOM   611   C  CB    . GLU A 1 75  ? 112.000 160.711 86.629  1.00 60.87 ?  75  GLU A CB    1 
ATOM   612   C  CG    . GLU A 1 75  ? 110.620 161.308 86.403  1.00 62.72 ?  75  GLU A CG    1 
ATOM   613   C  CD    . GLU A 1 75  ? 109.598 160.268 85.983  1.00 65.19 ?  75  GLU A CD    1 
ATOM   614   O  OE1   . GLU A 1 75  ? 109.795 159.628 84.929  1.00 65.33 ?  75  GLU A OE1   1 
ATOM   615   O  OE2   . GLU A 1 75  ? 108.598 160.088 86.708  1.00 64.89 -1 75  GLU A OE2   1 
ATOM   616   N  N     . ASP A 1 76  ? 114.320 159.126 88.164  1.00 58.05 ?  76  ASP A N     1 
ATOM   617   C  CA    . ASP A 1 76  ? 115.596 158.415 88.153  1.00 55.77 ?  76  ASP A CA    1 
ATOM   618   C  C     . ASP A 1 76  ? 115.468 157.024 88.763  1.00 55.43 ?  76  ASP A C     1 
ATOM   619   O  O     . ASP A 1 76  ? 116.043 156.058 88.245  1.00 60.04 ?  76  ASP A O     1 
ATOM   620   C  CB    . ASP A 1 76  ? 116.648 159.233 88.895  1.00 57.42 ?  76  ASP A CB    1 
ATOM   621   C  CG    . ASP A 1 76  ? 116.860 160.601 88.279  1.00 60.39 ?  76  ASP A CG    1 
ATOM   622   O  OD1   . ASP A 1 76  ? 116.843 160.702 87.034  1.00 59.97 ?  76  ASP A OD1   1 
ATOM   623   O  OD2   . ASP A 1 76  ? 117.045 161.575 89.038  1.00 59.16 -1 76  ASP A OD2   1 
ATOM   624   N  N     . ILE A 1 77  ? 114.728 156.901 89.867  1.00 51.09 ?  77  ILE A N     1 
ATOM   625   C  CA    . ILE A 1 77  ? 114.510 155.590 90.474  1.00 51.47 ?  77  ILE A CA    1 
ATOM   626   C  C     . ILE A 1 77  ? 113.742 154.688 89.519  1.00 51.41 ?  77  ILE A C     1 
ATOM   627   O  O     . ILE A 1 77  ? 114.028 153.490 89.399  1.00 53.07 ?  77  ILE A O     1 
ATOM   628   C  CB    . ILE A 1 77  ? 113.779 155.739 91.820  1.00 52.51 ?  77  ILE A CB    1 
ATOM   629   C  CG1   . ILE A 1 77  ? 114.474 156.785 92.690  1.00 52.79 ?  77  ILE A CG1   1 
ATOM   630   C  CG2   . ILE A 1 77  ? 113.714 154.401 92.536  1.00 51.51 ?  77  ILE A CG2   1 
ATOM   631   C  CD1   . ILE A 1 77  ? 114.048 156.759 94.138  1.00 52.94 ?  77  ILE A CD1   1 
ATOM   632   N  N     . LYS A 1 78  ? 112.747 155.250 88.831  1.00 54.77 ?  78  LYS A N     1 
ATOM   633   C  CA    . LYS A 1 78  ? 112.005 154.494 87.833  1.00 54.72 ?  78  LYS A CA    1 
ATOM   634   C  C     . LYS A 1 78  ? 112.918 154.027 86.710  1.00 54.66 ?  78  LYS A C     1 
ATOM   635   O  O     . LYS A 1 78  ? 112.815 152.885 86.256  1.00 57.65 ?  78  LYS A O     1 
ATOM   636   C  CB    . LYS A 1 78  ? 110.863 155.346 87.281  1.00 57.81 ?  78  LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 78  ? 109.621 154.564 86.893  1.00 56.70 ?  78  LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 78  ? 108.608 155.466 86.211  1.00 56.73 ?  78  LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 78  ? 107.816 154.712 85.160  1.00 57.73 ?  78  LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 78  ? 106.381 154.590 85.537  1.00 57.58 1  78  LYS A NZ    1 
ATOM   641   N  N     . GLU A 1 79  ? 113.820 154.897 86.249  1.00 55.66 ?  79  GLU A N     1 
ATOM   642   C  CA    . GLU A 1 79  ? 114.769 154.507 85.209  1.00 55.52 ?  79  GLU A CA    1 
ATOM   643   C  C     . GLU A 1 79  ? 115.674 153.379 85.686  1.00 52.99 ?  79  GLU A C     1 
ATOM   644   O  O     . GLU A 1 79  ? 115.968 152.446 84.929  1.00 55.14 ?  79  GLU A O     1 
ATOM   645   C  CB    . GLU A 1 79  ? 115.604 155.714 84.784  1.00 56.06 ?  79  GLU A CB    1 
ATOM   646   C  CG    . GLU A 1 79  ? 114.874 156.708 83.901  1.00 56.91 ?  79  GLU A CG    1 
ATOM   647   C  CD    . GLU A 1 79  ? 115.749 157.881 83.508  1.00 60.38 ?  79  GLU A CD    1 
ATOM   648   O  OE1   . GLU A 1 79  ? 116.784 157.656 82.847  1.00 60.58 ?  79  GLU A OE1   1 
ATOM   649   O  OE2   . GLU A 1 79  ? 115.407 159.028 83.863  1.00 61.84 -1 79  GLU A OE2   1 
ATOM   650   N  N     . VAL A 1 80  ? 116.129 153.452 86.936  1.00 45.61 ?  80  VAL A N     1 
ATOM   651   C  CA    . VAL A 1 80  ? 116.970 152.393 87.491  1.00 43.99 ?  80  VAL A CA    1 
ATOM   652   C  C     . VAL A 1 80  ? 116.212 151.071 87.527  1.00 48.77 ?  80  VAL A C     1 
ATOM   653   O  O     . VAL A 1 80  ? 116.742 150.018 87.144  1.00 49.84 ?  80  VAL A O     1 
ATOM   654   C  CB    . VAL A 1 80  ? 117.474 152.802 88.888  1.00 43.52 ?  80  VAL A CB    1 
ATOM   655   C  CG1   . VAL A 1 80  ? 118.035 151.607 89.629  1.00 45.04 ?  80  VAL A CG1   1 
ATOM   656   C  CG2   . VAL A 1 80  ? 118.519 153.896 88.768  1.00 44.18 ?  80  VAL A CG2   1 
ATOM   657   N  N     . PHE A 1 81  ? 114.956 151.106 87.978  1.00 48.14 ?  81  PHE A N     1 
ATOM   658   C  CA    . PHE A 1 81  ? 114.162 149.883 88.045  1.00 44.30 ?  81  PHE A CA    1 
ATOM   659   C  C     . PHE A 1 81  ? 113.865 149.332 86.654  1.00 47.34 ?  81  PHE A C     1 
ATOM   660   O  O     . PHE A 1 81  ? 113.823 148.112 86.461  1.00 49.22 ?  81  PHE A O     1 
ATOM   661   C  CB    . PHE A 1 81  ? 112.872 150.139 88.819  1.00 44.78 ?  81  PHE A CB    1 
ATOM   662   C  CG    . PHE A 1 81  ? 112.991 149.883 90.294  1.00 44.53 ?  81  PHE A CG    1 
ATOM   663   C  CD1   . PHE A 1 81  ? 113.602 150.809 91.121  1.00 45.67 ?  81  PHE A CD1   1 
ATOM   664   C  CD2   . PHE A 1 81  ? 112.493 148.720 90.852  1.00 46.79 ?  81  PHE A CD2   1 
ATOM   665   C  CE1   . PHE A 1 81  ? 113.713 150.579 92.478  1.00 45.99 ?  81  PHE A CE1   1 
ATOM   666   C  CE2   . PHE A 1 81  ? 112.602 148.486 92.209  1.00 45.17 ?  81  PHE A CE2   1 
ATOM   667   C  CZ    . PHE A 1 81  ? 113.213 149.416 93.022  1.00 43.40 ?  81  PHE A CZ    1 
ATOM   668   N  N     . LYS A 1 82  ? 113.649 150.212 85.672  1.00 47.06 ?  82  LYS A N     1 
ATOM   669   C  CA    . LYS A 1 82  ? 113.509 149.754 84.292  1.00 50.44 ?  82  LYS A CA    1 
ATOM   670   C  C     . LYS A 1 82  ? 114.782 149.076 83.812  1.00 50.45 ?  82  LYS A C     1 
ATOM   671   O  O     . LYS A 1 82  ? 114.728 148.042 83.139  1.00 52.83 ?  82  LYS A O     1 
ATOM   672   C  CB    . LYS A 1 82  ? 113.157 150.918 83.362  1.00 51.75 ?  82  LYS A CB    1 
ATOM   673   C  CG    . LYS A 1 82  ? 111.877 151.666 83.691  1.00 53.41 ?  82  LYS A CG    1 
ATOM   674   C  CD    . LYS A 1 82  ? 110.672 150.753 83.691  1.00 53.59 ?  82  LYS A CD    1 
ATOM   675   C  CE    . LYS A 1 82  ? 109.597 151.268 82.749  1.00 54.29 ?  82  LYS A CE    1 
ATOM   676   N  NZ    . LYS A 1 82  ? 110.135 151.521 81.384  1.00 52.75 1  82  LYS A NZ    1 
ATOM   677   N  N     . THR A 1 83  ? 115.939 149.649 84.148  1.00 43.33 ?  83  THR A N     1 
ATOM   678   C  CA    . THR A 1 83  ? 117.207 149.040 83.763  1.00 45.07 ?  83  THR A CA    1 
ATOM   679   C  C     . THR A 1 83  ? 117.354 147.653 84.374  1.00 46.81 ?  83  THR A C     1 
ATOM   680   O  O     . THR A 1 83  ? 117.838 146.724 83.716  1.00 47.75 ?  83  THR A O     1 
ATOM   681   C  CB    . THR A 1 83  ? 118.370 149.941 84.182  1.00 46.72 ?  83  THR A CB    1 
ATOM   682   O  OG1   . THR A 1 83  ? 118.169 151.255 83.650  1.00 50.88 ?  83  THR A OG1   1 
ATOM   683   C  CG2   . THR A 1 83  ? 119.684 149.393 83.659  1.00 46.24 ?  83  THR A CG2   1 
ATOM   684   N  N     . ALA A 1 84  ? 116.938 147.491 85.631  1.00 46.18 ?  84  ALA A N     1 
ATOM   685   C  CA    . ALA A 1 84  ? 116.994 146.173 86.257  1.00 41.53 ?  84  ALA A CA    1 
ATOM   686   C  C     . ALA A 1 84  ? 116.064 145.185 85.568  1.00 42.96 ?  84  ALA A C     1 
ATOM   687   O  O     . ALA A 1 84  ? 116.452 144.043 85.294  1.00 47.86 ?  84  ALA A O     1 
ATOM   688   C  CB    . ALA A 1 84  ? 116.652 146.281 87.741  1.00 43.85 ?  84  ALA A CB    1 
ATOM   689   N  N     . TYR A 1 85  ? 114.832 145.604 85.274  1.00 47.92 ?  85  TYR A N     1 
ATOM   690   C  CA    . TYR A 1 85  ? 113.853 144.702 84.683  1.00 47.31 ?  85  TYR A CA    1 
ATOM   691   C  C     . TYR A 1 85  ? 114.027 144.535 83.179  1.00 46.51 ?  85  TYR A C     1 
ATOM   692   O  O     . TYR A 1 85  ? 113.469 143.592 82.610  1.00 49.04 ?  85  TYR A O     1 
ATOM   693   C  CB    . TYR A 1 85  ? 112.436 145.192 84.986  1.00 47.59 ?  85  TYR A CB    1 
ATOM   694   C  CG    . TYR A 1 85  ? 111.955 144.847 86.378  1.00 48.42 ?  85  TYR A CG    1 
ATOM   695   C  CD1   . TYR A 1 85  ? 112.197 145.696 87.449  1.00 47.29 ?  85  TYR A CD1   1 
ATOM   696   C  CD2   . TYR A 1 85  ? 111.263 143.669 86.621  1.00 46.70 ?  85  TYR A CD2   1 
ATOM   697   C  CE1   . TYR A 1 85  ? 111.760 145.384 88.720  1.00 46.62 ?  85  TYR A CE1   1 
ATOM   698   C  CE2   . TYR A 1 85  ? 110.823 143.349 87.888  1.00 46.81 ?  85  TYR A CE2   1 
ATOM   699   C  CZ    . TYR A 1 85  ? 111.074 144.209 88.933  1.00 47.28 ?  85  TYR A CZ    1 
ATOM   700   O  OH    . TYR A 1 85  ? 110.637 143.892 90.197  1.00 49.55 ?  85  TYR A OH    1 
ATOM   701   N  N     . ALA A 1 86  ? 114.780 145.422 82.523  1.00 45.11 ?  86  ALA A N     1 
ATOM   702   C  CA    . ALA A 1 86  ? 115.004 145.278 81.089  1.00 44.63 ?  86  ALA A CA    1 
ATOM   703   C  C     . ALA A 1 86  ? 115.838 144.046 80.771  1.00 47.07 ?  86  ALA A C     1 
ATOM   704   O  O     . ALA A 1 86  ? 115.692 143.461 79.692  1.00 48.77 ?  86  ALA A O     1 
ATOM   705   C  CB    . ALA A 1 86  ? 115.680 146.528 80.527  1.00 44.19 ?  86  ALA A CB    1 
ATOM   706   N  N     . LYS A 1 87  ? 116.718 143.643 81.689  1.00 46.25 ?  87  LYS A N     1 
ATOM   707   C  CA    . LYS A 1 87  ? 117.533 142.455 81.466  1.00 45.97 ?  87  LYS A CA    1 
ATOM   708   C  C     . LYS A 1 87  ? 116.678 141.196 81.406  1.00 45.92 ?  87  LYS A C     1 
ATOM   709   O  O     . LYS A 1 87  ? 117.036 140.237 80.712  1.00 45.76 ?  87  LYS A O     1 
ATOM   710   C  CB    . LYS A 1 87  ? 118.593 142.344 82.565  1.00 42.62 ?  87  LYS A CB    1 
ATOM   711   C  CG    . LYS A 1 87  ? 119.171 140.953 82.771  1.00 44.03 ?  87  LYS A CG    1 
ATOM   712   C  CD    . LYS A 1 87  ? 120.540 140.814 82.127  1.00 45.15 ?  87  LYS A CD    1 
ATOM   713   C  CE    . LYS A 1 87  ? 121.149 139.455 82.425  1.00 45.16 ?  87  LYS A CE    1 
ATOM   714   N  NZ    . LYS A 1 87  ? 122.491 139.295 81.802  1.00 42.00 1  87  LYS A NZ    1 
ATOM   715   N  N     . LYS A 1 88  ? 115.534 141.196 82.092  1.00 48.62 ?  88  LYS A N     1 
ATOM   716   C  CA    . LYS A 1 88  ? 114.678 140.017 82.210  1.00 47.59 ?  88  LYS A CA    1 
ATOM   717   C  C     . LYS A 1 88  ? 115.475 138.828 82.735  1.00 43.20 ?  88  LYS A C     1 
ATOM   718   O  O     . LYS A 1 88  ? 115.517 137.754 82.131  1.00 46.03 ?  88  LYS A O     1 
ATOM   719   C  CB    . LYS A 1 88  ? 114.002 139.685 80.878  1.00 49.47 ?  88  LYS A CB    1 
ATOM   720   C  CG    . LYS A 1 88  ? 112.698 140.431 80.639  1.00 49.24 ?  88  LYS A CG    1 
ATOM   721   C  CD    . LYS A 1 88  ? 112.282 140.380 79.176  1.00 47.96 ?  88  LYS A CD    1 
ATOM   722   C  CE    . LYS A 1 88  ? 113.481 140.456 78.246  1.00 49.54 ?  88  LYS A CE    1 
ATOM   723   N  NZ    . LYS A 1 88  ? 113.074 140.427 76.815  1.00 47.96 1  88  LYS A NZ    1 
ATOM   724   N  N     . PHE A 1 89  ? 116.127 139.038 83.876  1.00 42.48 ?  89  PHE A N     1 
ATOM   725   C  CA    . PHE A 1 89  ? 116.959 138.002 84.468  1.00 38.98 ?  89  PHE A CA    1 
ATOM   726   C  C     . PHE A 1 89  ? 116.110 136.811 84.889  1.00 41.01 ?  89  PHE A C     1 
ATOM   727   O  O     . PHE A 1 89  ? 115.030 136.966 85.464  1.00 44.65 ?  89  PHE A O     1 
ATOM   728   C  CB    . PHE A 1 89  ? 117.722 138.558 85.671  1.00 35.95 ?  89  PHE A CB    1 
ATOM   729   C  CG    . PHE A 1 89  ? 118.413 137.508 86.492  1.00 37.82 ?  89  PHE A CG    1 
ATOM   730   C  CD1   . PHE A 1 89  ? 119.676 137.063 86.148  1.00 35.27 ?  89  PHE A CD1   1 
ATOM   731   C  CD2   . PHE A 1 89  ? 117.801 136.965 87.610  1.00 35.78 ?  89  PHE A CD2   1 
ATOM   732   C  CE1   . PHE A 1 89  ? 120.313 136.098 86.898  1.00 37.73 ?  89  PHE A CE1   1 
ATOM   733   C  CE2   . PHE A 1 89  ? 118.433 135.999 88.361  1.00 35.76 ?  89  PHE A CE2   1 
ATOM   734   C  CZ    . PHE A 1 89  ? 119.689 135.566 88.007  1.00 38.16 ?  89  PHE A CZ    1 
ATOM   735   N  N     . ARG A 1 90  ? 116.609 135.613 84.598  1.00 41.13 ?  90  ARG A N     1 
ATOM   736   C  CA    . ARG A 1 90  ? 115.960 134.375 84.998  1.00 40.95 ?  90  ARG A CA    1 
ATOM   737   C  C     . ARG A 1 90  ? 116.964 133.516 85.749  1.00 41.23 ?  90  ARG A C     1 
ATOM   738   O  O     . ARG A 1 90  ? 118.087 133.313 85.276  1.00 43.62 ?  90  ARG A O     1 
ATOM   739   C  CB    . ARG A 1 90  ? 115.409 133.615 83.788  1.00 42.51 ?  90  ARG A CB    1 
ATOM   740   C  CG    . ARG A 1 90  ? 114.453 134.423 82.932  1.00 42.59 ?  90  ARG A CG    1 
ATOM   741   C  CD    . ARG A 1 90  ? 113.039 134.370 83.483  1.00 45.13 ?  90  ARG A CD    1 
ATOM   742   N  NE    . ARG A 1 90  ? 112.163 135.328 82.821  1.00 45.28 ?  90  ARG A NE    1 
ATOM   743   C  CZ    . ARG A 1 90  ? 111.947 136.566 83.248  1.00 47.41 ?  90  ARG A CZ    1 
ATOM   744   N  NH1   . ARG A 1 90  ? 112.512 137.024 84.352  1.00 46.93 1  90  ARG A NH1   1 
ATOM   745   N  NH2   . ARG A 1 90  ? 111.142 137.360 82.550  1.00 44.82 ?  90  ARG A NH2   1 
ATOM   746   N  N     . PHE A 1 91  ? 116.564 133.027 86.912  1.00 36.44 ?  91  PHE A N     1 
ATOM   747   C  CA    . PHE A 1 91  ? 117.419 132.130 87.673  1.00 36.22 ?  91  PHE A CA    1 
ATOM   748   C  C     . PHE A 1 91  ? 117.588 130.821 86.910  1.00 42.87 ?  91  PHE A C     1 
ATOM   749   O  O     . PHE A 1 91  ? 116.591 130.221 86.490  1.00 45.07 ?  91  PHE A O     1 
ATOM   750   C  CB    . PHE A 1 91  ? 116.824 131.874 89.052  1.00 35.20 ?  91  PHE A CB    1 
ATOM   751   C  CG    . PHE A 1 91  ? 116.924 133.048 89.982  1.00 39.44 ?  91  PHE A CG    1 
ATOM   752   C  CD1   . PHE A 1 91  ? 118.073 133.268 90.723  1.00 42.42 ?  91  PHE A CD1   1 
ATOM   753   C  CD2   . PHE A 1 91  ? 115.872 133.936 90.114  1.00 39.20 ?  91  PHE A CD2   1 
ATOM   754   C  CE1   . PHE A 1 91  ? 118.168 134.345 91.579  1.00 38.91 ?  91  PHE A CE1   1 
ATOM   755   C  CE2   . PHE A 1 91  ? 115.961 135.016 90.968  1.00 39.18 ?  91  PHE A CE2   1 
ATOM   756   C  CZ    . PHE A 1 91  ? 117.110 135.221 91.701  1.00 38.29 ?  91  PHE A CZ    1 
ATOM   757   N  N     . PRO A 1 92  ? 118.820 130.347 86.704  1.00 41.57 ?  92  PRO A N     1 
ATOM   758   C  CA    . PRO A 1 92  ? 119.010 129.128 85.908  1.00 37.12 ?  92  PRO A CA    1 
ATOM   759   C  C     . PRO A 1 92  ? 118.688 127.851 86.657  1.00 38.04 ?  92  PRO A C     1 
ATOM   760   O  O     . PRO A 1 92  ? 118.523 126.805 86.015  1.00 40.67 ?  92  PRO A O     1 
ATOM   761   C  CB    . PRO A 1 92  ? 120.496 129.190 85.539  1.00 38.47 ?  92  PRO A CB    1 
ATOM   762   C  CG    . PRO A 1 92  ? 121.118 129.894 86.696  1.00 39.59 ?  92  PRO A CG    1 
ATOM   763   C  CD    . PRO A 1 92  ? 120.094 130.872 87.226  1.00 40.78 ?  92  PRO A CD    1 
ATOM   764   N  N     . SER A 1 93  ? 118.593 127.897 87.982  1.00 39.30 ?  93  SER A N     1 
ATOM   765   C  CA    . SER A 1 93  ? 118.373 126.707 88.785  1.00 42.91 ?  93  SER A CA    1 
ATOM   766   C  C     . SER A 1 93  ? 117.397 127.031 89.904  1.00 44.00 ?  93  SER A C     1 
ATOM   767   O  O     . SER A 1 93  ? 117.199 128.192 90.267  1.00 46.31 ?  93  SER A O     1 
ATOM   768   C  CB    . SER A 1 93  ? 119.690 126.172 89.364  1.00 41.29 ?  93  SER A CB    1 
ATOM   769   O  OG    . SER A 1 93  ? 120.118 126.954 90.464  1.00 40.49 ?  93  SER A OG    1 
ATOM   770   N  N     . PHE A 1 94  ? 116.779 125.981 90.446  1.00 41.93 ?  94  PHE A N     1 
ATOM   771   C  CA    . PHE A 1 94  ? 115.849 126.169 91.553  1.00 42.32 ?  94  PHE A CA    1 
ATOM   772   C  C     . PHE A 1 94  ? 116.566 126.665 92.801  1.00 43.88 ?  94  PHE A C     1 
ATOM   773   O  O     . PHE A 1 94  ? 116.015 127.471 93.558  1.00 46.67 ?  94  PHE A O     1 
ATOM   774   C  CB    . PHE A 1 94  ? 115.099 124.871 91.848  1.00 41.55 ?  94  PHE A CB    1 
ATOM   775   C  CG    . PHE A 1 94  ? 114.452 124.846 93.202  1.00 43.53 ?  94  PHE A CG    1 
ATOM   776   C  CD1   . PHE A 1 94  ? 113.353 125.641 93.471  1.00 44.19 ?  94  PHE A CD1   1 
ATOM   777   C  CD2   . PHE A 1 94  ? 114.944 124.032 94.207  1.00 44.94 ?  94  PHE A CD2   1 
ATOM   778   C  CE1   . PHE A 1 94  ? 112.760 125.628 94.715  1.00 43.92 ?  94  PHE A CE1   1 
ATOM   779   C  CE2   . PHE A 1 94  ? 114.352 124.014 95.454  1.00 46.60 ?  94  PHE A CE2   1 
ATOM   780   C  CZ    . PHE A 1 94  ? 113.259 124.813 95.708  1.00 44.64 ?  94  PHE A CZ    1 
ATOM   781   N  N     . MET A 1 95  ? 117.788 126.185 93.042  1.00 41.38 ?  95  MET A N     1 
ATOM   782   C  CA    . MET A 1 95  ? 118.507 126.572 94.251  1.00 36.23 ?  95  MET A CA    1 
ATOM   783   C  C     . MET A 1 95  ? 118.816 128.061 94.272  1.00 39.46 ?  95  MET A C     1 
ATOM   784   O  O     . MET A 1 95  ? 118.752 128.694 95.328  1.00 45.02 ?  95  MET A O     1 
ATOM   785   C  CB    . MET A 1 95  ? 119.795 125.761 94.388  1.00 42.26 ?  95  MET A CB    1 
ATOM   786   C  CG    . MET A 1 95  ? 120.203 125.371 95.817  1.00 44.32 ?  95  MET A CG    1 
ATOM   787   S  SD    . MET A 1 95  ? 118.948 125.085 97.093  1.00 53.46 ?  95  MET A SD    1 
ATOM   788   C  CE    . MET A 1 95  ? 117.783 123.997 96.276  1.00 45.67 ?  95  MET A CE    1 
ATOM   789   N  N     . SER A 1 96  ? 119.163 128.639 93.121  1.00 35.10 ?  96  SER A N     1 
ATOM   790   C  CA    . SER A 1 96  ? 119.474 130.065 93.077  1.00 33.05 ?  96  SER A CA    1 
ATOM   791   C  C     . SER A 1 96  ? 118.292 130.899 93.552  1.00 34.07 ?  96  SER A C     1 
ATOM   792   O  O     . SER A 1 96  ? 118.414 131.712 94.481  1.00 34.98 ?  96  SER A O     1 
ATOM   793   C  CB    . SER A 1 96  ? 119.869 130.459 91.655  1.00 35.24 ?  96  SER A CB    1 
ATOM   794   O  OG    . SER A 1 96  ? 120.635 129.438 91.043  1.00 38.59 ?  96  SER A OG    1 
ATOM   795   N  N     . ALA A 1 97  ? 117.126 130.684 92.940  1.00 40.03 ?  97  ALA A N     1 
ATOM   796   C  CA    . ALA A 1 97  ? 115.937 131.444 93.302  1.00 37.07 ?  97  ALA A CA    1 
ATOM   797   C  C     . ALA A 1 97  ? 115.487 131.127 94.720  1.00 37.56 ?  97  ALA A C     1 
ATOM   798   O  O     . ALA A 1 97  ? 115.054 132.021 95.452  1.00 45.57 ?  97  ALA A O     1 
ATOM   799   C  CB    . ALA A 1 97  ? 114.816 131.158 92.309  1.00 36.46 ?  97  ALA A CB    1 
ATOM   800   N  N     . PHE A 1 98  ? 115.569 129.857 95.120  1.00 33.25 ?  98  PHE A N     1 
ATOM   801   C  CA    . PHE A 1 98  ? 115.153 129.481 96.464  1.00 35.49 ?  98  PHE A CA    1 
ATOM   802   C  C     . PHE A 1 98  ? 116.013 130.171 97.512  1.00 37.06 ?  98  PHE A C     1 
ATOM   803   O  O     . PHE A 1 98  ? 115.497 130.736 98.483  1.00 45.07 ?  98  PHE A O     1 
ATOM   804   C  CB    . PHE A 1 98  ? 115.218 127.963 96.626  1.00 40.98 ?  98  PHE A CB    1 
ATOM   805   C  CG    . PHE A 1 98  ? 115.034 127.499 98.041  1.00 42.29 ?  98  PHE A CG    1 
ATOM   806   C  CD1   . PHE A 1 98  ? 113.768 127.425 98.596  1.00 41.66 ?  98  PHE A CD1   1 
ATOM   807   C  CD2   . PHE A 1 98  ? 116.123 127.145 98.817  1.00 42.38 ?  98  PHE A CD2   1 
ATOM   808   C  CE1   . PHE A 1 98  ? 113.594 127.006 99.896  1.00 41.14 ?  98  PHE A CE1   1 
ATOM   809   C  CE2   . PHE A 1 98  ? 115.953 126.725 100.119 1.00 42.94 ?  98  PHE A CE2   1 
ATOM   810   C  CZ    . PHE A 1 98  ? 114.686 126.654 100.659 1.00 42.27 ?  98  PHE A CZ    1 
ATOM   811   N  N     . LYS A 1 99  ? 117.332 130.145 97.324  1.00 39.01 ?  99  LYS A N     1 
ATOM   812   C  CA    . LYS A 1 99  ? 118.230 130.797 98.266  1.00 38.77 ?  99  LYS A CA    1 
ATOM   813   C  C     . LYS A 1 99  ? 117.993 132.297 98.299  1.00 39.03 ?  99  LYS A C     1 
ATOM   814   O  O     . LYS A 1 99  ? 117.965 132.899 99.379  1.00 41.24 ?  99  LYS A O     1 
ATOM   815   C  CB    . LYS A 1 99  ? 119.683 130.485 97.911  1.00 38.86 ?  99  LYS A CB    1 
ATOM   816   C  CG    . LYS A 1 99  ? 120.104 129.064 98.239  1.00 41.35 ?  99  LYS A CG    1 
ATOM   817   C  CD    . LYS A 1 99  ? 119.698 128.676 99.648  1.00 43.43 ?  99  LYS A CD    1 
ATOM   818   C  CE    . LYS A 1 99  ? 120.846 128.021 100.390 1.00 41.25 ?  99  LYS A CE    1 
ATOM   819   N  NZ    . LYS A 1 99  ? 120.735 128.224 101.859 1.00 42.13 1  99  LYS A NZ    1 
ATOM   820   N  N     . PHE A 1 100 ? 117.796 132.923 97.133  1.00 34.65 ?  100 PHE A N     1 
ATOM   821   C  CA    . PHE A 1 100 ? 117.540 134.359 97.140  1.00 34.54 ?  100 PHE A CA    1 
ATOM   822   C  C     . PHE A 1 100 ? 116.256 134.685 97.890  1.00 36.68 ?  100 PHE A C     1 
ATOM   823   O  O     . PHE A 1 100 ? 116.255 135.509 98.810  1.00 42.14 ?  100 PHE A O     1 
ATOM   824   C  CB    . PHE A 1 100 ? 117.468 134.918 95.723  1.00 36.23 ?  100 PHE A CB    1 
ATOM   825   C  CG    . PHE A 1 100 ? 117.072 136.363 95.690  1.00 36.68 ?  100 PHE A CG    1 
ATOM   826   C  CD1   . PHE A 1 100 ? 117.966 137.342 96.089  1.00 37.98 ?  100 PHE A CD1   1 
ATOM   827   C  CD2   . PHE A 1 100 ? 115.798 136.742 95.308  1.00 36.45 ?  100 PHE A CD2   1 
ATOM   828   C  CE1   . PHE A 1 100 ? 117.604 138.671 96.086  1.00 38.96 ?  100 PHE A CE1   1 
ATOM   829   C  CE2   . PHE A 1 100 ? 115.431 138.070 95.302  1.00 39.45 ?  100 PHE A CE2   1 
ATOM   830   C  CZ    . PHE A 1 100 ? 116.336 139.036 95.691  1.00 39.03 ?  100 PHE A CZ    1 
ATOM   831   N  N     . TYR A 1 101 ? 115.153 134.033 97.528  1.00 41.22 ?  101 TYR A N     1 
ATOM   832   C  CA    . TYR A 1 101 ? 113.864 134.371 98.113  1.00 38.44 ?  101 TYR A CA    1 
ATOM   833   C  C     . TYR A 1 101 ? 113.693 133.839 99.527  1.00 40.02 ?  101 TYR A C     1 
ATOM   834   O  O     . TYR A 1 101 ? 112.693 134.164 100.174 1.00 46.64 ?  101 TYR A O     1 
ATOM   835   C  CB    . TYR A 1 101 ? 112.735 133.871 97.210  1.00 38.76 ?  101 TYR A CB    1 
ATOM   836   C  CG    . TYR A 1 101 ? 112.594 134.692 95.949  1.00 36.64 ?  101 TYR A CG    1 
ATOM   837   C  CD1   . TYR A 1 101 ? 112.085 135.981 95.993  1.00 39.62 ?  101 TYR A CD1   1 
ATOM   838   C  CD2   . TYR A 1 101 ? 112.995 134.189 94.721  1.00 35.22 ?  101 TYR A CD2   1 
ATOM   839   C  CE1   . TYR A 1 101 ? 111.965 136.741 94.846  1.00 39.29 ?  101 TYR A CE1   1 
ATOM   840   C  CE2   . TYR A 1 101 ? 112.881 134.940 93.571  1.00 39.50 ?  101 TYR A CE2   1 
ATOM   841   C  CZ    . TYR A 1 101 ? 112.365 136.215 93.638  1.00 41.13 ?  101 TYR A CZ    1 
ATOM   842   O  OH    . TYR A 1 101 ? 112.250 136.967 92.492  1.00 39.45 ?  101 TYR A OH    1 
ATOM   843   N  N     . ASN A 1 102 ? 114.634 133.036 100.022 1.00 40.55 ?  102 ASN A N     1 
ATOM   844   C  CA    . ASN A 1 102 ? 114.605 132.607 101.412 1.00 41.46 ?  102 ASN A CA    1 
ATOM   845   C  C     . ASN A 1 102 ? 115.575 133.367 102.306 1.00 43.05 ?  102 ASN A C     1 
ATOM   846   O  O     . ASN A 1 102 ? 115.340 133.442 103.516 1.00 45.65 ?  102 ASN A O     1 
ATOM   847   C  CB    . ASN A 1 102 ? 114.910 131.107 101.509 1.00 42.60 ?  102 ASN A CB    1 
ATOM   848   C  CG    . ASN A 1 102 ? 113.658 130.255 101.502 1.00 44.82 ?  102 ASN A CG    1 
ATOM   849   O  OD1   . ASN A 1 102 ? 112.762 130.455 100.682 1.00 46.40 ?  102 ASN A OD1   1 
ATOM   850   N  ND2   . ASN A 1 102 ? 113.588 129.301 102.421 1.00 44.73 ?  102 ASN A ND2   1 
ATOM   851   N  N     . ASP A 1 103 ? 116.650 133.929 101.756 1.00 43.44 ?  103 ASP A N     1 
ATOM   852   C  CA    . ASP A 1 103 ? 117.670 134.584 102.567 1.00 41.09 ?  103 ASP A CA    1 
ATOM   853   C  C     . ASP A 1 103 ? 117.767 136.085 102.349 1.00 41.31 ?  103 ASP A C     1 
ATOM   854   O  O     . ASP A 1 103 ? 117.976 136.824 103.311 1.00 47.96 ?  103 ASP A O     1 
ATOM   855   C  CB    . ASP A 1 103 ? 119.041 133.956 102.291 1.00 44.45 ?  103 ASP A CB    1 
ATOM   856   C  CG    . ASP A 1 103 ? 119.128 132.515 102.752 1.00 46.42 ?  103 ASP A CG    1 
ATOM   857   O  OD1   . ASP A 1 103 ? 118.113 131.983 103.249 1.00 47.25 ?  103 ASP A OD1   1 
ATOM   858   O  OD2   . ASP A 1 103 ? 120.212 131.911 102.616 1.00 48.74 -1 103 ASP A OD2   1 
ATOM   859   N  N     . TYR A 1 104 ? 117.624 136.563 101.111 1.00 31.26 ?  104 TYR A N     1 
ATOM   860   C  CA    . TYR A 1 104 ? 117.905 137.954 100.792 1.00 37.51 ?  104 TYR A CA    1 
ATOM   861   C  C     . TYR A 1 104 ? 116.692 138.751 100.339 1.00 39.68 ?  104 TYR A C     1 
ATOM   862   O  O     . TYR A 1 104 ? 116.709 139.980 100.457 1.00 44.70 ?  104 TYR A O     1 
ATOM   863   C  CB    . TYR A 1 104 ? 118.984 138.038 99.702  1.00 36.23 ?  104 TYR A CB    1 
ATOM   864   C  CG    . TYR A 1 104 ? 120.252 137.301 100.059 1.00 39.20 ?  104 TYR A CG    1 
ATOM   865   C  CD1   . TYR A 1 104 ? 121.237 137.907 100.824 1.00 34.99 ?  104 TYR A CD1   1 
ATOM   866   C  CD2   . TYR A 1 104 ? 120.459 135.993 99.640  1.00 34.27 ?  104 TYR A CD2   1 
ATOM   867   C  CE1   . TYR A 1 104 ? 122.393 137.236 101.158 1.00 36.30 ?  104 TYR A CE1   1 
ATOM   868   C  CE2   . TYR A 1 104 ? 121.612 135.312 99.971  1.00 34.79 ?  104 TYR A CE2   1 
ATOM   869   C  CZ    . TYR A 1 104 ? 122.577 135.939 100.730 1.00 39.47 ?  104 TYR A CZ    1 
ATOM   870   O  OH    . TYR A 1 104 ? 123.729 135.268 101.063 1.00 37.58 ?  104 TYR A OH    1 
ATOM   871   N  N     . ALA A 1 105 ? 115.654 138.100 99.824  1.00 39.31 ?  105 ALA A N     1 
ATOM   872   C  CA    . ALA A 1 105 ? 114.474 138.830 99.383  1.00 40.02 ?  105 ALA A CA    1 
ATOM   873   C  C     . ALA A 1 105 ? 113.737 139.423 100.576 1.00 43.24 ?  105 ALA A C     1 
ATOM   874   O  O     . ALA A 1 105 ? 113.554 138.765 101.604 1.00 41.64 ?  105 ALA A O     1 
ATOM   875   C  CB    . ALA A 1 105 ? 113.541 137.915 98.594  1.00 37.86 ?  105 ALA A CB    1 
ATOM   876   N  N     . LEU A 1 106 ? 113.323 140.678 100.438 1.00 47.41 ?  106 LEU A N     1 
ATOM   877   C  CA    . LEU A 1 106 ? 112.581 141.339 101.500 1.00 45.87 ?  106 LEU A CA    1 
ATOM   878   C  C     . LEU A 1 106 ? 111.200 140.715 101.653 1.00 47.88 ?  106 LEU A C     1 
ATOM   879   O  O     . LEU A 1 106 ? 110.500 140.462 100.670 1.00 46.17 ?  106 LEU A O     1 
ATOM   880   C  CB    . LEU A 1 106 ? 112.453 142.834 101.213 1.00 46.17 ?  106 LEU A CB    1 
ATOM   881   C  CG    . LEU A 1 106 ? 111.822 143.692 102.309 1.00 44.92 ?  106 LEU A CG    1 
ATOM   882   C  CD1   . LEU A 1 106 ? 112.725 143.757 103.527 1.00 43.99 ?  106 LEU A CD1   1 
ATOM   883   C  CD2   . LEU A 1 106 ? 111.535 145.084 101.785 1.00 45.17 ?  106 LEU A CD2   1 
ATOM   884   N  N     . LYS A 1 107 ? 110.813 140.472 102.899 1.00 54.76 ?  107 LYS A N     1 
ATOM   885   C  CA    . LYS A 1 107 ? 109.519 139.900 103.226 1.00 53.91 ?  107 LYS A CA    1 
ATOM   886   C  C     . LYS A 1 107 ? 108.780 140.825 104.181 1.00 54.18 ?  107 LYS A C     1 
ATOM   887   O  O     . LYS A 1 107 ? 109.378 141.682 104.837 1.00 54.39 ?  107 LYS A O     1 
ATOM   888   C  CB    . LYS A 1 107 ? 109.667 138.506 103.849 1.00 51.79 ?  107 LYS A CB    1 
ATOM   889   C  CG    . LYS A 1 107 ? 110.079 137.430 102.863 1.00 50.81 ?  107 LYS A CG    1 
ATOM   890   C  CD    . LYS A 1 107 ? 110.359 136.115 103.566 1.00 55.44 ?  107 LYS A CD    1 
ATOM   891   C  CE    . LYS A 1 107 ? 110.729 135.029 102.572 1.00 54.96 ?  107 LYS A CE    1 
ATOM   892   N  NZ    . LYS A 1 107 ? 111.327 133.839 103.239 1.00 51.84 1  107 LYS A NZ    1 
ATOM   893   N  N     . THR A 1 108 ? 107.463 140.647 104.245 1.00 60.48 ?  108 THR A N     1 
ATOM   894   C  CA    . THR A 1 108 ? 106.643 141.444 105.139 1.00 61.10 ?  108 THR A CA    1 
ATOM   895   C  C     . THR A 1 108 ? 107.040 141.185 106.594 1.00 62.03 ?  108 THR A C     1 
ATOM   896   O  O     . THR A 1 108 ? 107.771 140.244 106.911 1.00 60.42 ?  108 THR A O     1 
ATOM   897   C  CB    . THR A 1 108 ? 105.163 141.138 104.924 1.00 60.24 ?  108 THR A CB    1 
ATOM   898   O  OG1   . THR A 1 108 ? 104.981 139.726 104.776 1.00 62.28 ?  108 THR A OG1   1 
ATOM   899   C  CG2   . THR A 1 108 ? 104.652 141.841 103.676 1.00 59.01 ?  108 THR A CG2   1 
ATOM   900   N  N     . ASN A 1 109 ? 106.540 142.043 107.486 1.00 63.53 ?  109 ASN A N     1 
ATOM   901   C  CA    . ASN A 1 109 ? 106.958 141.993 108.883 1.00 62.62 ?  109 ASN A CA    1 
ATOM   902   C  C     . ASN A 1 109 ? 106.611 140.664 109.539 1.00 64.06 ?  109 ASN A C     1 
ATOM   903   O  O     . ASN A 1 109 ? 107.280 140.252 110.494 1.00 65.05 ?  109 ASN A O     1 
ATOM   904   C  CB    . ASN A 1 109 ? 106.326 143.148 109.658 1.00 62.62 ?  109 ASN A CB    1 
ATOM   905   C  CG    . ASN A 1 109 ? 107.090 144.444 109.490 1.00 62.85 ?  109 ASN A CG    1 
ATOM   906   O  OD1   . ASN A 1 109 ? 108.313 144.444 109.361 1.00 64.74 ?  109 ASN A OD1   1 
ATOM   907   N  ND2   . ASN A 1 109 ? 106.371 145.560 109.489 1.00 63.04 ?  109 ASN A ND2   1 
ATOM   908   N  N     . ASP A 1 110 ? 105.582 139.978 109.047 1.00 68.70 ?  110 ASP A N     1 
ATOM   909   C  CA    . ASP A 1 110 ? 105.191 138.677 109.565 1.00 67.94 ?  110 ASP A CA    1 
ATOM   910   C  C     . ASP A 1 110 ? 105.826 137.525 108.797 1.00 68.31 ?  110 ASP A C     1 
ATOM   911   O  O     . ASP A 1 110 ? 105.451 136.369 109.015 1.00 69.86 ?  110 ASP A O     1 
ATOM   912   C  CB    . ASP A 1 110 ? 103.667 138.539 109.552 1.00 67.40 ?  110 ASP A CB    1 
ATOM   913   C  CG    . ASP A 1 110 ? 103.044 139.105 108.292 1.00 68.90 ?  110 ASP A CG    1 
ATOM   914   O  OD1   . ASP A 1 110 ? 103.679 139.962 107.646 1.00 69.20 ?  110 ASP A OD1   1 
ATOM   915   O  OD2   . ASP A 1 110 ? 101.916 138.693 107.949 1.00 70.98 -1 110 ASP A OD2   1 
ATOM   916   N  N     . LYS A 1 111 ? 106.779 137.818 107.907 1.00 66.46 ?  111 LYS A N     1 
ATOM   917   C  CA    . LYS A 1 111 ? 107.449 136.802 107.090 1.00 65.58 ?  111 LYS A CA    1 
ATOM   918   C  C     . LYS A 1 111 ? 106.441 135.988 106.284 1.00 65.91 ?  111 LYS A C     1 
ATOM   919   O  O     . LYS A 1 111 ? 106.576 134.774 106.127 1.00 67.92 ?  111 LYS A O     1 
ATOM   920   C  CB    . LYS A 1 111 ? 108.323 135.881 107.947 1.00 65.10 ?  111 LYS A CB    1 
ATOM   921   C  CG    . LYS A 1 111 ? 109.485 136.562 108.663 1.00 65.13 ?  111 LYS A CG    1 
ATOM   922   C  CD    . LYS A 1 111 ? 110.059 137.722 107.865 1.00 66.65 ?  111 LYS A CD    1 
ATOM   923   C  CE    . LYS A 1 111 ? 110.069 139.001 108.687 1.00 66.83 ?  111 LYS A CE    1 
ATOM   924   N  NZ    . LYS A 1 111 ? 110.571 140.162 107.902 1.00 64.70 1  111 LYS A NZ    1 
ATOM   925   N  N     . LYS A 1 112 ? 105.418 136.665 105.763 1.00 64.63 ?  112 LYS A N     1 
ATOM   926   C  CA    . LYS A 1 112 ? 104.315 136.002 105.078 1.00 66.88 ?  112 LYS A CA    1 
ATOM   927   C  C     . LYS A 1 112 ? 104.418 136.097 103.562 1.00 66.69 ?  112 LYS A C     1 
ATOM   928   O  O     . LYS A 1 112 ? 104.374 135.075 102.873 1.00 68.00 ?  112 LYS A O     1 
ATOM   929   C  CB    . LYS A 1 112 ? 102.980 136.593 105.549 1.00 66.48 ?  112 LYS A CB    1 
ATOM   930   C  CG    . LYS A 1 112 ? 101.767 135.752 105.188 1.00 67.80 ?  112 LYS A CG    1 
ATOM   931   C  CD    . LYS A 1 112 ? 101.744 134.446 105.968 1.00 68.20 ?  112 LYS A CD    1 
ATOM   932   C  CE    . LYS A 1 112 ? 101.894 134.683 107.464 1.00 68.46 ?  112 LYS A CE    1 
ATOM   933   N  NZ    . LYS A 1 112 ? 100.888 135.651 107.983 1.00 66.80 1  112 LYS A NZ    1 
ATOM   934   N  N     . LYS A 1 113 ? 104.552 137.305 103.029 1.00 59.74 ?  113 LYS A N     1 
ATOM   935   C  CA    . LYS A 1 113 ? 104.612 137.540 101.596 1.00 57.63 ?  113 LYS A CA    1 
ATOM   936   C  C     . LYS A 1 113 ? 105.993 138.066 101.214 1.00 57.10 ?  113 LYS A C     1 
ATOM   937   O  O     . LYS A 1 113 ? 106.862 138.282 102.062 1.00 58.08 ?  113 LYS A O     1 
ATOM   938   C  CB    . LYS A 1 113 ? 103.508 138.510 101.169 1.00 58.63 ?  113 LYS A CB    1 
ATOM   939   C  CG    . LYS A 1 113 ? 102.104 137.943 101.286 1.00 58.57 ?  113 LYS A CG    1 
ATOM   940   C  CD    . LYS A 1 113 ? 101.818 136.942 100.180 1.00 61.20 ?  113 LYS A CD    1 
ATOM   941   C  CE    . LYS A 1 113 ? 100.396 136.416 100.261 1.00 59.99 ?  113 LYS A CE    1 
ATOM   942   N  NZ    . LYS A 1 113 ? 100.130 135.383 99.222  1.00 58.80 1  113 LYS A NZ    1 
ATOM   943   N  N     . ILE A 1 114 ? 106.186 138.275 99.915  1.00 53.70 ?  114 ILE A N     1 
ATOM   944   C  CA    . ILE A 1 114 ? 107.467 138.692 99.356  1.00 52.40 ?  114 ILE A CA    1 
ATOM   945   C  C     . ILE A 1 114 ? 107.303 140.095 98.789  1.00 50.13 ?  114 ILE A C     1 
ATOM   946   O  O     . ILE A 1 114 ? 106.419 140.337 97.957  1.00 52.75 ?  114 ILE A O     1 
ATOM   947   C  CB    . ILE A 1 114 ? 107.959 137.713 98.279  1.00 52.98 ?  114 ILE A CB    1 
ATOM   948   C  CG1   . ILE A 1 114 ? 108.471 136.425 98.925  1.00 51.59 ?  114 ILE A CG1   1 
ATOM   949   C  CG2   . ILE A 1 114 ? 109.046 138.346 97.429  1.00 52.71 ?  114 ILE A CG2   1 
ATOM   950   C  CD1   . ILE A 1 114 ? 108.540 135.257 97.973  1.00 51.35 ?  114 ILE A CD1   1 
ATOM   951   N  N     . LEU A 1 115 ? 108.152 141.017 99.237  1.00 49.22 ?  115 LEU A N     1 
ATOM   952   C  CA    . LEU A 1 115 ? 108.116 142.401 98.781  1.00 51.09 ?  115 LEU A CA    1 
ATOM   953   C  C     . LEU A 1 115 ? 109.099 142.686 97.656  1.00 51.90 ?  115 LEU A C     1 
ATOM   954   O  O     . LEU A 1 115 ? 108.774 143.440 96.735  1.00 52.05 ?  115 LEU A O     1 
ATOM   955   C  CB    . LEU A 1 115 ? 108.398 143.350 99.949  1.00 50.85 ?  115 LEU A CB    1 
ATOM   956   C  CG    . LEU A 1 115 ? 107.344 143.379 101.053 1.00 49.79 ?  115 LEU A CG    1 
ATOM   957   C  CD1   . LEU A 1 115 ? 107.967 143.783 102.377 1.00 50.56 ?  115 LEU A CD1   1 
ATOM   958   C  CD2   . LEU A 1 115 ? 106.216 144.318 100.673 1.00 50.74 ?  115 LEU A CD2   1 
ATOM   959   N  N     . GLU A 1 116 ? 110.289 142.099 97.705  1.00 49.12 ?  116 GLU A N     1 
ATOM   960   C  CA    . GLU A 1 116 ? 111.347 142.374 96.744  1.00 45.80 ?  116 GLU A CA    1 
ATOM   961   C  C     . GLU A 1 116 ? 111.540 141.184 95.818  1.00 46.41 ?  116 GLU A C     1 
ATOM   962   O  O     . GLU A 1 116 ? 111.591 140.037 96.274  1.00 50.13 ?  116 GLU A O     1 
ATOM   963   C  CB    . GLU A 1 116 ? 112.665 142.685 97.454  1.00 44.75 ?  116 GLU A CB    1 
ATOM   964   C  CG    . GLU A 1 116 ? 112.964 144.159 97.607  1.00 44.63 ?  116 GLU A CG    1 
ATOM   965   C  CD    . GLU A 1 116 ? 114.205 144.407 98.436  1.00 47.03 ?  116 GLU A CD    1 
ATOM   966   O  OE1   . GLU A 1 116 ? 114.693 143.451 99.072  1.00 46.08 ?  116 GLU A OE1   1 
ATOM   967   O  OE2   . GLU A 1 116 ? 114.694 145.555 98.450  1.00 48.24 -1 116 GLU A OE2   1 
ATOM   968   N  N     . ARG A 1 117 ? 111.644 141.459 94.523  1.00 42.37 ?  117 ARG A N     1 
ATOM   969   C  CA    . ARG A 1 117 ? 112.143 140.483 93.570  1.00 42.21 ?  117 ARG A CA    1 
ATOM   970   C  C     . ARG A 1 117 ? 113.663 140.622 93.499  1.00 43.77 ?  117 ARG A C     1 
ATOM   971   O  O     . ARG A 1 117 ? 114.271 141.392 94.245  1.00 47.51 ?  117 ARG A O     1 
ATOM   972   C  CB    . ARG A 1 117 ? 111.478 140.675 92.207  1.00 42.43 ?  117 ARG A CB    1 
ATOM   973   C  CG    . ARG A 1 117 ? 109.959 140.688 92.246  1.00 44.77 ?  117 ARG A CG    1 
ATOM   974   C  CD    . ARG A 1 117 ? 109.411 139.483 92.995  1.00 49.50 ?  117 ARG A CD    1 
ATOM   975   N  NE    . ARG A 1 117 ? 109.507 138.255 92.217  1.00 47.61 ?  117 ARG A NE    1 
ATOM   976   C  CZ    . ARG A 1 117 ? 108.692 137.929 91.222  1.00 47.19 ?  117 ARG A CZ    1 
ATOM   977   N  NH1   . ARG A 1 117 ? 107.696 138.720 90.856  1.00 48.28 1  117 ARG A NH1   1 
ATOM   978   N  NH2   . ARG A 1 117 ? 108.880 136.780 90.580  1.00 47.65 ?  117 ARG A NH2   1 
ATOM   979   N  N     . TYR A 1 118 ? 114.301 139.866 92.605  1.00 42.19 ?  118 TYR A N     1 
ATOM   980   C  CA    . TYR A 1 118 ? 115.736 140.026 92.409  1.00 36.17 ?  118 TYR A CA    1 
ATOM   981   C  C     . TYR A 1 118 ? 116.056 141.402 91.838  1.00 37.76 ?  118 TYR A C     1 
ATOM   982   O  O     . TYR A 1 118 ? 117.009 142.062 92.272  1.00 40.66 ?  118 TYR A O     1 
ATOM   983   C  CB    . TYR A 1 118 ? 116.262 138.922 91.493  1.00 36.88 ?  118 TYR A CB    1 
ATOM   984   C  CG    . TYR A 1 118 ? 117.761 138.755 91.511  1.00 36.73 ?  118 TYR A CG    1 
ATOM   985   C  CD1   . TYR A 1 118 ? 118.441 138.552 92.703  1.00 36.21 ?  118 TYR A CD1   1 
ATOM   986   C  CD2   . TYR A 1 118 ? 118.496 138.794 90.338  1.00 36.96 ?  118 TYR A CD2   1 
ATOM   987   C  CE1   . TYR A 1 118 ? 119.809 138.397 92.723  1.00 35.71 ?  118 TYR A CE1   1 
ATOM   988   C  CE2   . TYR A 1 118 ? 119.863 138.634 90.347  1.00 31.19 ?  118 TYR A CE2   1 
ATOM   989   C  CZ    . TYR A 1 118 ? 120.515 138.437 91.542  1.00 35.72 ?  118 TYR A CZ    1 
ATOM   990   O  OH    . TYR A 1 118 ? 121.881 138.283 91.555  1.00 45.66 ?  118 TYR A OH    1 
ATOM   991   N  N     . GLU A 1 119 ? 115.251 141.858 90.876  1.00 41.38 ?  119 GLU A N     1 
ATOM   992   C  CA    . GLU A 1 119 ? 115.469 143.168 90.276  1.00 38.57 ?  119 GLU A CA    1 
ATOM   993   C  C     . GLU A 1 119 ? 115.261 144.286 91.288  1.00 40.41 ?  119 GLU A C     1 
ATOM   994   O  O     . GLU A 1 119 ? 115.995 145.278 91.277  1.00 43.54 ?  119 GLU A O     1 
ATOM   995   C  CB    . GLU A 1 119 ? 114.548 143.352 89.073  1.00 40.57 ?  119 GLU A CB    1 
ATOM   996   C  CG    . GLU A 1 119 ? 115.007 142.617 87.829  1.00 41.16 ?  119 GLU A CG    1 
ATOM   997   C  CD    . GLU A 1 119 ? 114.432 141.220 87.726  1.00 43.69 ?  119 GLU A CD    1 
ATOM   998   O  OE1   . GLU A 1 119 ? 114.003 140.670 88.762  1.00 43.92 ?  119 GLU A OE1   1 
ATOM   999   O  OE2   . GLU A 1 119 ? 114.415 140.668 86.606  1.00 44.72 -1 119 GLU A OE2   1 
ATOM   1000  N  N     . ASP A 1 120 ? 114.269 144.149 92.170  1.00 42.16 ?  120 ASP A N     1 
ATOM   1001  C  CA    . ASP A 1 120 ? 114.032 145.178 93.178  1.00 38.20 ?  120 ASP A CA    1 
ATOM   1002  C  C     . ASP A 1 120 ? 115.205 145.285 94.142  1.00 38.64 ?  120 ASP A C     1 
ATOM   1003  O  O     . ASP A 1 120 ? 115.677 146.388 94.443  1.00 45.44 ?  120 ASP A O     1 
ATOM   1004  C  CB    . ASP A 1 120 ? 112.740 144.881 93.940  1.00 42.51 ?  120 ASP A CB    1 
ATOM   1005  C  CG    . ASP A 1 120 ? 111.564 144.645 93.020  1.00 47.73 ?  120 ASP A CG    1 
ATOM   1006  O  OD1   . ASP A 1 120 ? 111.486 145.318 91.971  1.00 46.98 ?  120 ASP A OD1   1 
ATOM   1007  O  OD2   . ASP A 1 120 ? 110.716 143.789 93.343  1.00 51.12 -1 120 ASP A OD2   1 
ATOM   1008  N  N     . ARG A 1 121 ? 115.690 144.144 94.637  1.00 33.43 ?  121 ARG A N     1 
ATOM   1009  C  CA    . ARG A 1 121 ? 116.834 144.151 95.541  1.00 32.95 ?  121 ARG A CA    1 
ATOM   1010  C  C     . ARG A 1 121 ? 118.068 144.725 94.859  1.00 34.25 ?  121 ARG A C     1 
ATOM   1011  O  O     . ARG A 1 121 ? 118.797 145.529 95.452  1.00 41.31 ?  121 ARG A O     1 
ATOM   1012  C  CB    . ARG A 1 121 ? 117.112 142.736 96.046  1.00 34.34 ?  121 ARG A CB    1 
ATOM   1013  C  CG    . ARG A 1 121 ? 118.267 142.636 97.027  1.00 32.95 ?  121 ARG A CG    1 
ATOM   1014  C  CD    . ARG A 1 121 ? 117.783 142.771 98.458  1.00 33.48 ?  121 ARG A CD    1 
ATOM   1015  N  NE    . ARG A 1 121 ? 118.652 143.631 99.252  1.00 38.02 ?  121 ARG A NE    1 
ATOM   1016  C  CZ    . ARG A 1 121 ? 118.379 144.890 99.564  1.00 37.23 ?  121 ARG A CZ    1 
ATOM   1017  N  NH1   . ARG A 1 121 ? 117.267 145.478 99.156  1.00 36.19 1  121 ARG A NH1   1 
ATOM   1018  N  NH2   . ARG A 1 121 ? 119.244 145.576 100.304 1.00 34.72 ?  121 ARG A NH2   1 
ATOM   1019  N  N     . ILE A 1 122 ? 118.311 144.334 93.607  1.00 33.17 ?  122 ILE A N     1 
ATOM   1020  C  CA    . ILE A 1 122 ? 119.479 144.835 92.891  1.00 29.12 ?  122 ILE A CA    1 
ATOM   1021  C  C     . ILE A 1 122 ? 119.370 146.338 92.666  1.00 30.95 ?  122 ILE A C     1 
ATOM   1022  O  O     . ILE A 1 122 ? 120.350 147.072 92.828  1.00 36.66 ?  122 ILE A O     1 
ATOM   1023  C  CB    . ILE A 1 122 ? 119.667 144.065 91.573  1.00 32.31 ?  122 ILE A CB    1 
ATOM   1024  C  CG1   . ILE A 1 122 ? 120.399 142.752 91.843  1.00 27.19 ?  122 ILE A CG1   1 
ATOM   1025  C  CG2   . ILE A 1 122 ? 120.430 144.900 90.555  1.00 33.57 ?  122 ILE A CG2   1 
ATOM   1026  C  CD1   . ILE A 1 122 ? 120.712 141.976 90.605  1.00 33.73 ?  122 ILE A CD1   1 
ATOM   1027  N  N     . SER A 1 123 ? 118.181 146.824 92.299  1.00 34.94 ?  123 SER A N     1 
ATOM   1028  C  CA    . SER A 1 123 ? 117.997 148.255 92.086  1.00 32.04 ?  123 SER A CA    1 
ATOM   1029  C  C     . SER A 1 123 ? 118.198 149.037 93.375  1.00 31.85 ?  123 SER A C     1 
ATOM   1030  O  O     . SER A 1 123 ? 118.799 150.117 93.365  1.00 39.19 ?  123 SER A O     1 
ATOM   1031  C  CB    . SER A 1 123 ? 116.604 148.525 91.519  1.00 34.60 ?  123 SER A CB    1 
ATOM   1032  O  OG    . SER A 1 123 ? 116.252 147.552 90.557  1.00 39.38 ?  123 SER A OG    1 
ATOM   1033  N  N     . ILE A 1 124 ? 117.692 148.518 94.495  1.00 31.75 ?  124 ILE A N     1 
ATOM   1034  C  CA    . ILE A 1 124 ? 117.874 149.206 95.768  1.00 34.84 ?  124 ILE A CA    1 
ATOM   1035  C  C     . ILE A 1 124 ? 119.348 149.241 96.153  1.00 36.09 ?  124 ILE A C     1 
ATOM   1036  O  O     . ILE A 1 124 ? 119.862 150.275 96.597  1.00 39.49 ?  124 ILE A O     1 
ATOM   1037  C  CB    . ILE A 1 124 ? 117.009 148.550 96.857  1.00 38.69 ?  124 ILE A CB    1 
ATOM   1038  C  CG1   . ILE A 1 124 ? 115.530 148.814 96.575  1.00 39.24 ?  124 ILE A CG1   1 
ATOM   1039  C  CG2   . ILE A 1 124 ? 117.385 149.072 98.231  1.00 33.39 ?  124 ILE A CG2   1 
ATOM   1040  C  CD1   . ILE A 1 124 ? 115.221 150.259 96.243  1.00 37.19 ?  124 ILE A CD1   1 
ATOM   1041  N  N     . VAL A 1 125 ? 120.055 148.122 95.977  1.00 32.10 ?  125 VAL A N     1 
ATOM   1042  C  CA    . VAL A 1 125 ? 121.481 148.086 96.288  1.00 29.01 ?  125 VAL A CA    1 
ATOM   1043  C  C     . VAL A 1 125 ? 122.250 149.050 95.389  1.00 28.32 ?  125 VAL A C     1 
ATOM   1044  O  O     . VAL A 1 125 ? 123.185 149.725 95.834  1.00 39.80 ?  125 VAL A O     1 
ATOM   1045  C  CB    . VAL A 1 125 ? 122.014 146.645 96.174  1.00 33.53 ?  125 VAL A CB    1 
ATOM   1046  C  CG1   . VAL A 1 125 ? 123.518 146.616 96.315  1.00 30.75 ?  125 VAL A CG1   1 
ATOM   1047  C  CG2   . VAL A 1 125 ? 121.381 145.767 97.237  1.00 28.67 ?  125 VAL A CG2   1 
ATOM   1048  N  N     . ALA A 1 126 ? 121.854 149.147 94.120  1.00 26.22 ?  126 ALA A N     1 
ATOM   1049  C  CA    . ALA A 1 126 ? 122.540 150.038 93.191  1.00 26.65 ?  126 ALA A CA    1 
ATOM   1050  C  C     . ALA A 1 126 ? 122.298 151.501 93.533  1.00 34.15 ?  126 ALA A C     1 
ATOM   1051  O  O     . ALA A 1 126 ? 123.223 152.319 93.472  1.00 39.43 ?  126 ALA A O     1 
ATOM   1052  C  CB    . ALA A 1 126 ? 122.085 149.747 91.765  1.00 29.39 ?  126 ALA A CB    1 
ATOM   1053  N  N     . LEU A 1 127 ? 121.058 151.853 93.881  1.00 36.11 ?  127 LEU A N     1 
ATOM   1054  C  CA    . LEU A 1 127 ? 120.766 153.222 94.286  1.00 32.17 ?  127 LEU A CA    1 
ATOM   1055  C  C     . LEU A 1 127 ? 121.463 153.571 95.593  1.00 30.19 ?  127 LEU A C     1 
ATOM   1056  O  O     . LEU A 1 127 ? 121.852 154.727 95.797  1.00 35.16 ?  127 LEU A O     1 
ATOM   1057  C  CB    . LEU A 1 127 ? 119.256 153.422 94.413  1.00 33.59 ?  127 LEU A CB    1 
ATOM   1058  C  CG    . LEU A 1 127 ? 118.464 153.383 93.105  1.00 34.25 ?  127 LEU A CG    1 
ATOM   1059  C  CD1   . LEU A 1 127 ? 117.024 152.983 93.362  1.00 36.24 ?  127 LEU A CD1   1 
ATOM   1060  C  CD2   . LEU A 1 127 ? 118.528 154.719 92.390  1.00 34.84 ?  127 LEU A CD2   1 
ATOM   1061  N  N     . PHE A 1 128 ? 121.619 152.595 96.489  1.00 32.75 ?  128 PHE A N     1 
ATOM   1062  C  CA    . PHE A 1 128 ? 122.408 152.811 97.694  1.00 32.86 ?  128 PHE A CA    1 
ATOM   1063  C  C     . PHE A 1 128 ? 123.876 153.053 97.357  1.00 30.93 ?  128 PHE A C     1 
ATOM   1064  O  O     . PHE A 1 128 ? 124.511 153.943 97.931  1.00 38.78 ?  128 PHE A O     1 
ATOM   1065  C  CB    . PHE A 1 128 ? 122.253 151.611 98.628  1.00 30.53 ?  128 PHE A CB    1 
ATOM   1066  C  CG    . PHE A 1 128 ? 123.120 151.672 99.850  1.00 35.69 ?  128 PHE A CG    1 
ATOM   1067  C  CD1   . PHE A 1 128 ? 122.695 152.345 100.982 1.00 37.91 ?  128 PHE A CD1   1 
ATOM   1068  C  CD2   . PHE A 1 128 ? 124.353 151.044 99.874  1.00 33.56 ?  128 PHE A CD2   1 
ATOM   1069  C  CE1   . PHE A 1 128 ? 123.488 152.398 102.109 1.00 38.80 ?  128 PHE A CE1   1 
ATOM   1070  C  CE2   . PHE A 1 128 ? 125.150 151.100 100.995 1.00 33.60 ?  128 PHE A CE2   1 
ATOM   1071  C  CZ    . PHE A 1 128 ? 124.717 151.774 102.115 1.00 35.48 ?  128 PHE A CZ    1 
ATOM   1072  N  N     . PHE A 1 129 ? 124.428 152.267 96.430  1.00 28.02 ?  129 PHE A N     1 
ATOM   1073  C  CA    . PHE A 1 129 ? 125.832 152.418 96.059  1.00 25.55 ?  129 PHE A CA    1 
ATOM   1074  C  C     . PHE A 1 129 ? 126.098 153.759 95.389  1.00 29.30 ?  129 PHE A C     1 
ATOM   1075  O  O     . PHE A 1 129 ? 127.102 154.418 95.683  1.00 33.20 ?  129 PHE A O     1 
ATOM   1076  C  CB    . PHE A 1 129 ? 126.259 151.284 95.127  1.00 26.16 ?  129 PHE A CB    1 
ATOM   1077  C  CG    . PHE A 1 129 ? 126.479 149.974 95.817  1.00 25.05 ?  129 PHE A CG    1 
ATOM   1078  C  CD1   . PHE A 1 129 ? 126.631 149.913 97.188  1.00 27.59 ?  129 PHE A CD1   1 
ATOM   1079  C  CD2   . PHE A 1 129 ? 126.552 148.803 95.085  1.00 26.52 ?  129 PHE A CD2   1 
ATOM   1080  C  CE1   . PHE A 1 129 ? 126.835 148.705 97.819  1.00 24.89 ?  129 PHE A CE1   1 
ATOM   1081  C  CE2   . PHE A 1 129 ? 126.762 147.594 95.710  1.00 26.00 ?  129 PHE A CE2   1 
ATOM   1082  C  CZ    . PHE A 1 129 ? 126.903 147.546 97.078  1.00 27.59 ?  129 PHE A CZ    1 
ATOM   1083  N  N     . ALA A 1 130 ? 125.214 154.177 94.482  1.00 35.43 ?  130 ALA A N     1 
ATOM   1084  C  CA    . ALA A 1 130 ? 125.497 155.344 93.654  1.00 35.20 ?  130 ALA A CA    1 
ATOM   1085  C  C     . ALA A 1 130 ? 125.466 156.639 94.454  1.00 42.34 ?  130 ALA A C     1 
ATOM   1086  O  O     . ALA A 1 130 ? 126.178 157.590 94.111  1.00 47.09 ?  130 ALA A O     1 
ATOM   1087  C  CB    . ALA A 1 130 ? 124.507 155.413 92.498  1.00 34.43 ?  130 ALA A CB    1 
ATOM   1088  N  N     . ASN A 1 131 ? 124.646 156.701 95.505  1.00 42.79 ?  131 ASN A N     1 
ATOM   1089  C  CA    . ASN A 1 131 ? 124.585 157.857 96.400  1.00 43.74 ?  131 ASN A CA    1 
ATOM   1090  C  C     . ASN A 1 131 ? 124.213 159.134 95.643  1.00 43.29 ?  131 ASN A C     1 
ATOM   1091  O  O     . ASN A 1 131 ? 124.896 160.156 95.726  1.00 47.94 ?  131 ASN A O     1 
ATOM   1092  C  CB    . ASN A 1 131 ? 125.904 158.028 97.158  1.00 43.48 ?  131 ASN A CB    1 
ATOM   1093  C  CG    . ASN A 1 131 ? 125.760 158.895 98.392  1.00 48.16 ?  131 ASN A CG    1 
ATOM   1094  O  OD1   . ASN A 1 131 ? 124.808 158.752 99.158  1.00 44.83 ?  131 ASN A OD1   1 
ATOM   1095  N  ND2   . ASN A 1 131 ? 126.710 159.799 98.591  1.00 46.49 ?  131 ASN A ND2   1 
ATOM   1096  N  N     . GLY A 1 132 ? 123.112 159.066 94.897  1.00 41.46 ?  132 GLY A N     1 
ATOM   1097  C  CA    . GLY A 1 132 ? 122.569 160.209 94.202  1.00 41.96 ?  132 GLY A CA    1 
ATOM   1098  C  C     . GLY A 1 132 ? 122.829 160.243 92.709  1.00 44.87 ?  132 GLY A C     1 
ATOM   1099  O  O     . GLY A 1 132 ? 122.167 161.011 92.002  1.00 49.08 ?  132 GLY A O     1 
ATOM   1100  N  N     . ASP A 1 133 ? 123.761 159.437 92.210  1.00 47.04 ?  133 ASP A N     1 
ATOM   1101  C  CA    . ASP A 1 133 ? 124.107 159.434 90.794  1.00 46.05 ?  133 ASP A CA    1 
ATOM   1102  C  C     . ASP A 1 133 ? 123.211 158.447 90.053  1.00 49.14 ?  133 ASP A C     1 
ATOM   1103  O  O     . ASP A 1 133 ? 123.189 157.257 90.377  1.00 49.71 ?  133 ASP A O     1 
ATOM   1104  C  CB    . ASP A 1 133 ? 125.580 159.076 90.602  1.00 48.23 ?  133 ASP A CB    1 
ATOM   1105  C  CG    . ASP A 1 133 ? 126.145 159.604 89.298  1.00 53.27 ?  133 ASP A CG    1 
ATOM   1106  O  OD1   . ASP A 1 133 ? 125.364 159.810 88.345  1.00 52.24 ?  133 ASP A OD1   1 
ATOM   1107  O  OD2   . ASP A 1 133 ? 127.374 159.813 89.225  1.00 52.57 -1 133 ASP A OD2   1 
ATOM   1108  N  N     . THR A 1 134 ? 122.473 158.944 89.059  1.00 48.73 ?  134 THR A N     1 
ATOM   1109  C  CA    . THR A 1 134 ? 121.570 158.075 88.309  1.00 47.99 ?  134 THR A CA    1 
ATOM   1110  C  C     . THR A 1 134 ? 122.335 157.168 87.353  1.00 49.88 ?  134 THR A C     1 
ATOM   1111  O  O     . THR A 1 134 ? 122.047 155.969 87.259  1.00 51.80 ?  134 THR A O     1 
ATOM   1112  C  CB    . THR A 1 134 ? 120.553 158.922 87.548  1.00 52.41 ?  134 THR A CB    1 
ATOM   1113  O  OG1   . THR A 1 134 ? 119.714 159.605 88.485  1.00 53.72 ?  134 THR A OG1   1 
ATOM   1114  C  CG2   . THR A 1 134 ? 119.689 158.047 86.653  1.00 51.31 ?  134 THR A CG2   1 
ATOM   1115  N  N     . GLU A 1 135 ? 123.316 157.723 86.636  1.00 47.24 ?  135 GLU A N     1 
ATOM   1116  C  CA    . GLU A 1 135 ? 124.095 156.920 85.699  1.00 47.75 ?  135 GLU A CA    1 
ATOM   1117  C  C     . GLU A 1 135 ? 124.912 155.861 86.427  1.00 48.60 ?  135 GLU A C     1 
ATOM   1118  O  O     . GLU A 1 135 ? 125.023 154.723 85.957  1.00 51.03 ?  135 GLU A O     1 
ATOM   1119  C  CB    . GLU A 1 135 ? 125.002 157.822 84.866  1.00 49.48 ?  135 GLU A CB    1 
ATOM   1120  C  CG    . GLU A 1 135 ? 124.252 158.840 84.028  1.00 48.79 ?  135 GLU A CG    1 
ATOM   1121  C  CD    . GLU A 1 135 ? 123.144 158.211 83.208  1.00 54.08 ?  135 GLU A CD    1 
ATOM   1122  O  OE1   . GLU A 1 135 ? 123.443 157.319 82.388  1.00 54.31 ?  135 GLU A OE1   1 
ATOM   1123  O  OE2   . GLU A 1 135 ? 121.973 158.608 83.386  1.00 55.23 -1 135 GLU A OE2   1 
ATOM   1124  N  N     . LYS A 1 136 ? 125.496 156.217 87.572  1.00 40.59 ?  136 LYS A N     1 
ATOM   1125  C  CA    . LYS A 1 136 ? 126.226 155.236 88.365  1.00 40.58 ?  136 LYS A CA    1 
ATOM   1126  C  C     . LYS A 1 136 ? 125.292 154.155 88.893  1.00 41.54 ?  136 LYS A C     1 
ATOM   1127  O  O     . LYS A 1 136 ? 125.667 152.980 88.961  1.00 44.71 ?  136 LYS A O     1 
ATOM   1128  C  CB    . LYS A 1 136 ? 126.957 155.931 89.513  1.00 45.00 ?  136 LYS A CB    1 
ATOM   1129  C  CG    . LYS A 1 136 ? 128.110 155.135 90.092  1.00 42.10 ?  136 LYS A CG    1 
ATOM   1130  C  CD    . LYS A 1 136 ? 129.321 155.184 89.183  1.00 43.50 ?  136 LYS A CD    1 
ATOM   1131  C  CE    . LYS A 1 136 ? 130.599 154.888 89.948  1.00 46.23 ?  136 LYS A CE    1 
ATOM   1132  N  NZ    . LYS A 1 136 ? 131.804 155.092 89.099  1.00 47.84 1  136 LYS A NZ    1 
ATOM   1133  N  N     . ALA A 1 137 ? 124.071 154.534 89.275  1.00 39.31 ?  137 ALA A N     1 
ATOM   1134  C  CA    . ALA A 1 137 ? 123.095 153.543 89.716  1.00 34.47 ?  137 ALA A CA    1 
ATOM   1135  C  C     . ALA A 1 137 ? 122.741 152.583 88.589  1.00 36.75 ?  137 ALA A C     1 
ATOM   1136  O  O     . ALA A 1 137 ? 122.613 151.374 88.811  1.00 39.98 ?  137 ALA A O     1 
ATOM   1137  C  CB    . ALA A 1 137 ? 121.843 154.237 90.248  1.00 36.06 ?  137 ALA A CB    1 
ATOM   1138  N  N     . LYS A 1 138 ? 122.580 153.103 87.370  1.00 40.72 ?  138 LYS A N     1 
ATOM   1139  C  CA    . LYS A 1 138 ? 122.323 152.234 86.225  1.00 40.87 ?  138 LYS A CA    1 
ATOM   1140  C  C     . LYS A 1 138 ? 123.512 151.324 85.942  1.00 41.41 ?  138 LYS A C     1 
ATOM   1141  O  O     . LYS A 1 138 ? 123.334 150.155 85.580  1.00 43.37 ?  138 LYS A O     1 
ATOM   1142  C  CB    . LYS A 1 138 ? 121.980 153.073 84.995  1.00 45.21 ?  138 LYS A CB    1 
ATOM   1143  C  CG    . LYS A 1 138 ? 120.567 153.628 85.000  1.00 44.02 ?  138 LYS A CG    1 
ATOM   1144  C  CD    . LYS A 1 138 ? 120.469 154.892 84.166  1.00 43.87 ?  138 LYS A CD    1 
ATOM   1145  C  CE    . LYS A 1 138 ? 120.215 154.567 82.705  1.00 47.11 ?  138 LYS A CE    1 
ATOM   1146  N  NZ    . LYS A 1 138 ? 120.242 155.787 81.854  1.00 48.97 1  138 LYS A NZ    1 
ATOM   1147  N  N     . GLU A 1 139 ? 124.732 151.842 86.092  1.00 40.08 ?  139 GLU A N     1 
ATOM   1148  C  CA    . GLU A 1 139 ? 125.919 151.012 85.912  1.00 36.52 ?  139 GLU A CA    1 
ATOM   1149  C  C     . GLU A 1 139 ? 125.968 149.884 86.936  1.00 34.97 ?  139 GLU A C     1 
ATOM   1150  O  O     . GLU A 1 139 ? 126.288 148.740 86.598  1.00 40.47 ?  139 GLU A O     1 
ATOM   1151  C  CB    . GLU A 1 139 ? 127.179 151.874 86.003  1.00 38.10 ?  139 GLU A CB    1 
ATOM   1152  C  CG    . GLU A 1 139 ? 127.552 152.572 84.709  1.00 41.30 ?  139 GLU A CG    1 
ATOM   1153  C  CD    . GLU A 1 139 ? 128.678 153.568 84.889  1.00 48.31 ?  139 GLU A CD    1 
ATOM   1154  O  OE1   . GLU A 1 139 ? 128.740 154.211 85.958  1.00 45.67 ?  139 GLU A OE1   1 
ATOM   1155  O  OE2   . GLU A 1 139 ? 129.503 153.712 83.963  1.00 48.32 -1 139 GLU A OE2   1 
ATOM   1156  N  N     . TYR A 1 140 ? 125.654 150.189 88.197  1.00 32.51 ?  140 TYR A N     1 
ATOM   1157  C  CA    . TYR A 1 140 ? 125.614 149.156 89.228  1.00 30.56 ?  140 TYR A CA    1 
ATOM   1158  C  C     . TYR A 1 140 ? 124.518 148.136 88.942  1.00 33.75 ?  140 TYR A C     1 
ATOM   1159  O  O     . TYR A 1 140 ? 124.699 146.935 89.176  1.00 34.13 ?  140 TYR A O     1 
ATOM   1160  C  CB    . TYR A 1 140 ? 125.398 149.786 90.600  1.00 32.61 ?  140 TYR A CB    1 
ATOM   1161  C  CG    . TYR A 1 140 ? 126.616 150.437 91.205  1.00 32.42 ?  140 TYR A CG    1 
ATOM   1162  C  CD1   . TYR A 1 140 ? 127.785 149.718 91.410  1.00 34.45 ?  140 TYR A CD1   1 
ATOM   1163  C  CD2   . TYR A 1 140 ? 126.590 151.767 91.588  1.00 33.15 ?  140 TYR A CD2   1 
ATOM   1164  C  CE1   . TYR A 1 140 ? 128.894 150.314 91.970  1.00 34.20 ?  140 TYR A CE1   1 
ATOM   1165  C  CE2   . TYR A 1 140 ? 127.691 152.370 92.145  1.00 35.74 ?  140 TYR A CE2   1 
ATOM   1166  C  CZ    . TYR A 1 140 ? 128.839 151.642 92.335  1.00 30.78 ?  140 TYR A CZ    1 
ATOM   1167  O  OH    . TYR A 1 140 ? 129.932 152.254 92.895  1.00 33.69 ?  140 TYR A OH    1 
ATOM   1168  N  N     . VAL A 1 141 ? 123.366 148.604 88.456  1.00 33.86 ?  141 VAL A N     1 
ATOM   1169  C  CA    . VAL A 1 141 ? 122.285 147.696 88.086  1.00 33.00 ?  141 VAL A CA    1 
ATOM   1170  C  C     . VAL A 1 141 ? 122.739 146.749 86.987  1.00 35.02 ?  141 VAL A C     1 
ATOM   1171  O  O     . VAL A 1 141 ? 122.491 145.542 87.047  1.00 39.42 ?  141 VAL A O     1 
ATOM   1172  C  CB    . VAL A 1 141 ? 121.038 148.491 87.661  1.00 36.37 ?  141 VAL A CB    1 
ATOM   1173  C  CG1   . VAL A 1 141 ? 120.138 147.632 86.811  1.00 36.42 ?  141 VAL A CG1   1 
ATOM   1174  C  CG2   . VAL A 1 141 ? 120.284 148.961 88.874  1.00 35.34 ?  141 VAL A CG2   1 
ATOM   1175  N  N     . ASN A 1 142 ? 123.410 147.280 85.964  1.00 35.68 ?  142 ASN A N     1 
ATOM   1176  C  CA    . ASN A 1 142 ? 123.921 146.426 84.898  1.00 31.75 ?  142 ASN A CA    1 
ATOM   1177  C  C     . ASN A 1 142 ? 124.951 145.442 85.434  1.00 33.91 ?  142 ASN A C     1 
ATOM   1178  O  O     . ASN A 1 142 ? 124.980 144.277 85.027  1.00 40.10 ?  142 ASN A O     1 
ATOM   1179  C  CB    . ASN A 1 142 ? 124.519 147.279 83.783  1.00 32.37 ?  142 ASN A CB    1 
ATOM   1180  C  CG    . ASN A 1 142 ? 123.467 147.841 82.857  1.00 38.00 ?  142 ASN A CG    1 
ATOM   1181  O  OD1   . ASN A 1 142 ? 122.572 147.126 82.409  1.00 37.20 ?  142 ASN A OD1   1 
ATOM   1182  N  ND2   . ASN A 1 142 ? 123.566 149.132 82.565  1.00 36.90 ?  142 ASN A ND2   1 
ATOM   1183  N  N     . LEU A 1 143 ? 125.810 145.899 86.346  1.00 34.59 ?  143 LEU A N     1 
ATOM   1184  C  CA    . LEU A 1 143 ? 126.846 145.035 86.897  1.00 27.88 ?  143 LEU A CA    1 
ATOM   1185  C  C     . LEU A 1 143 ? 126.252 143.872 87.684  1.00 29.22 ?  143 LEU A C     1 
ATOM   1186  O  O     . LEU A 1 143 ? 126.720 142.734 87.570  1.00 29.56 ?  143 LEU A O     1 
ATOM   1187  C  CB    . LEU A 1 143 ? 127.783 145.857 87.781  1.00 27.94 ?  143 LEU A CB    1 
ATOM   1188  C  CG    . LEU A 1 143 ? 129.205 145.336 87.957  1.00 32.99 ?  143 LEU A CG    1 
ATOM   1189  C  CD1   . LEU A 1 143 ? 129.995 145.570 86.687  1.00 33.82 ?  143 LEU A CD1   1 
ATOM   1190  C  CD2   . LEU A 1 143 ? 129.859 146.032 89.128  1.00 28.96 ?  143 LEU A CD2   1 
ATOM   1191  N  N     . MET A 1 144 ? 125.226 144.136 88.494  1.00 33.23 ?  144 MET A N     1 
ATOM   1192  C  CA    . MET A 1 144 ? 124.691 143.081 89.350  1.00 27.56 ?  144 MET A CA    1 
ATOM   1193  C  C     . MET A 1 144 ? 123.653 142.219 88.636  1.00 28.03 ?  144 MET A C     1 
ATOM   1194  O  O     . MET A 1 144 ? 123.554 141.019 88.912  1.00 31.91 ?  144 MET A O     1 
ATOM   1195  C  CB    . MET A 1 144 ? 124.102 143.678 90.627  1.00 28.77 ?  144 MET A CB    1 
ATOM   1196  C  CG    . MET A 1 144 ? 125.098 144.475 91.450  1.00 30.13 ?  144 MET A CG    1 
ATOM   1197  S  SD    . MET A 1 144 ? 124.415 145.003 93.029  1.00 44.79 ?  144 MET A SD    1 
ATOM   1198  C  CE    . MET A 1 144 ? 123.672 146.558 92.565  1.00 33.81 ?  144 MET A CE    1 
ATOM   1199  N  N     . ILE A 1 145 ? 122.859 142.804 87.736  1.00 28.21 ?  145 ILE A N     1 
ATOM   1200  C  CA    . ILE A 1 145 ? 121.875 142.015 87.000  1.00 30.79 ?  145 ILE A CA    1 
ATOM   1201  C  C     . ILE A 1 145 ? 122.563 141.102 85.994  1.00 33.87 ?  145 ILE A C     1 
ATOM   1202  O  O     . ILE A 1 145 ? 122.077 139.999 85.715  1.00 37.32 ?  145 ILE A O     1 
ATOM   1203  C  CB    . ILE A 1 145 ? 120.824 142.931 86.338  1.00 31.53 ?  145 ILE A CB    1 
ATOM   1204  C  CG1   . ILE A 1 145 ? 119.494 142.190 86.192  1.00 30.46 ?  145 ILE A CG1   1 
ATOM   1205  C  CG2   . ILE A 1 145 ? 121.292 143.441 84.982  1.00 30.98 ?  145 ILE A CG2   1 
ATOM   1206  C  CD1   . ILE A 1 145 ? 118.821 141.864 87.503  1.00 28.31 ?  145 ILE A CD1   1 
ATOM   1207  N  N     . ASN A 1 146 ? 123.695 141.532 85.432  1.00 29.04 ?  146 ASN A N     1 
ATOM   1208  C  CA    . ASN A 1 146 ? 124.538 140.624 84.670  1.00 27.56 ?  146 ASN A CA    1 
ATOM   1209  C  C     . ASN A 1 146 ? 125.278 139.653 85.574  1.00 29.54 ?  146 ASN A C     1 
ATOM   1210  O  O     . ASN A 1 146 ? 125.919 138.726 85.068  1.00 36.63 ?  146 ASN A O     1 
ATOM   1211  C  CB    . ASN A 1 146 ? 125.544 141.406 83.825  1.00 29.11 ?  146 ASN A CB    1 
ATOM   1212  C  CG    . ASN A 1 146 ? 124.877 142.266 82.773  1.00 33.00 ?  146 ASN A CG    1 
ATOM   1213  O  OD1   . ASN A 1 146 ? 123.708 142.069 82.444  1.00 34.73 ?  146 ASN A OD1   1 
ATOM   1214  N  ND2   . ASN A 1 146 ? 125.618 143.227 82.239  1.00 35.28 ?  146 ASN A ND2   1 
ATOM   1215  N  N     . GLN A 1 147 ? 125.202 139.857 86.889  1.00 28.22 ?  147 GLN A N     1 
ATOM   1216  C  CA    . GLN A 1 147 ? 125.858 139.013 87.882  1.00 24.26 ?  147 GLN A CA    1 
ATOM   1217  C  C     . GLN A 1 147 ? 127.365 138.975 87.677  1.00 27.66 ?  147 GLN A C     1 
ATOM   1218  O  O     . GLN A 1 147 ? 128.007 137.955 87.913  1.00 34.10 ?  147 GLN A O     1 
ATOM   1219  C  CB    . GLN A 1 147 ? 125.266 137.601 87.884  1.00 24.18 ?  147 GLN A CB    1 
ATOM   1220  C  CG    . GLN A 1 147 ? 123.824 137.556 88.359  1.00 23.63 ?  147 GLN A CG    1 
ATOM   1221  C  CD    . GLN A 1 147 ? 123.378 136.169 88.756  1.00 27.67 ?  147 GLN A CD    1 
ATOM   1222  O  OE1   . GLN A 1 147 ? 122.720 135.985 89.779  1.00 31.18 ?  147 GLN A OE1   1 
ATOM   1223  N  NE2   . GLN A 1 147 ? 123.724 135.182 87.941  1.00 35.38 ?  147 GLN A NE2   1 
ATOM   1224  N  N     . GLU A 1 148 ? 127.936 140.090 87.216  1.00 26.16 ?  148 GLU A N     1 
ATOM   1225  C  CA    . GLU A 1 148 ? 129.385 140.214 87.129  1.00 22.83 ?  148 GLU A CA    1 
ATOM   1226  C  C     . GLU A 1 148 ? 130.010 140.485 88.489  1.00 26.73 ?  148 GLU A C     1 
ATOM   1227  O  O     . GLU A 1 148 ? 131.127 140.032 88.759  1.00 28.77 ?  148 GLU A O     1 
ATOM   1228  C  CB    . GLU A 1 148 ? 129.757 141.326 86.150  1.00 21.54 ?  148 GLU A CB    1 
ATOM   1229  C  CG    . GLU A 1 148 ? 129.233 141.108 84.745  1.00 25.93 ?  148 GLU A CG    1 
ATOM   1230  C  CD    . GLU A 1 148 ? 129.392 142.332 83.871  1.00 32.88 ?  148 GLU A CD    1 
ATOM   1231  O  OE1   . GLU A 1 148 ? 128.471 143.173 83.849  1.00 33.79 ?  148 GLU A OE1   1 
ATOM   1232  O  OE2   . GLU A 1 148 ? 130.442 142.456 83.208  1.00 36.84 -1 148 GLU A OE2   1 
ATOM   1233  N  N     . TYR A 1 149 ? 129.312 141.221 89.349  1.00 24.71 ?  149 TYR A N     1 
ATOM   1234  C  CA    . TYR A 1 149 ? 129.770 141.513 90.698  1.00 19.22 ?  149 TYR A CA    1 
ATOM   1235  C  C     . TYR A 1 149 ? 128.646 141.229 91.679  1.00 22.08 ?  149 TYR A C     1 
ATOM   1236  O  O     . TYR A 1 149 ? 127.482 141.534 91.407  1.00 27.63 ?  149 TYR A O     1 
ATOM   1237  C  CB    . TYR A 1 149 ? 130.228 142.968 90.828  1.00 19.77 ?  149 TYR A CB    1 
ATOM   1238  C  CG    . TYR A 1 149 ? 130.425 143.434 92.252  1.00 24.10 ?  149 TYR A CG    1 
ATOM   1239  C  CD1   . TYR A 1 149 ? 131.428 142.897 93.047  1.00 16.11 ?  149 TYR A CD1   1 
ATOM   1240  C  CD2   . TYR A 1 149 ? 129.608 144.411 92.800  1.00 21.98 ?  149 TYR A CD2   1 
ATOM   1241  C  CE1   . TYR A 1 149 ? 131.610 143.323 94.346  1.00 16.16 ?  149 TYR A CE1   1 
ATOM   1242  C  CE2   . TYR A 1 149 ? 129.782 144.841 94.096  1.00 21.75 ?  149 TYR A CE2   1 
ATOM   1243  C  CZ    . TYR A 1 149 ? 130.785 144.295 94.865  1.00 18.88 ?  149 TYR A CZ    1 
ATOM   1244  O  OH    . TYR A 1 149 ? 130.961 144.721 96.159  1.00 21.26 ?  149 TYR A OH    1 
ATOM   1245  N  N     . GLN A 1 150 ? 128.998 140.638 92.811  1.00 18.57 ?  150 GLN A N     1 
ATOM   1246  C  CA    . GLN A 1 150 ? 128.031 140.325 93.860  1.00 14.00 ?  150 GLN A CA    1 
ATOM   1247  C  C     . GLN A 1 150 ? 128.482 140.934 95.176  1.00 16.18 ?  150 GLN A C     1 
ATOM   1248  O  O     . GLN A 1 150 ? 129.520 140.517 95.725  1.00 23.41 ?  150 GLN A O     1 
ATOM   1249  C  CB    . GLN A 1 150 ? 127.865 138.813 94.000  1.00 19.28 ?  150 GLN A CB    1 
ATOM   1250  C  CG    . GLN A 1 150 ? 127.111 138.366 95.238  1.00 21.38 ?  150 GLN A CG    1 
ATOM   1251  C  CD    . GLN A 1 150 ? 125.681 138.860 95.267  1.00 16.86 ?  150 GLN A CD    1 
ATOM   1252  O  OE1   . GLN A 1 150 ? 124.855 138.453 94.454  1.00 29.61 ?  150 GLN A OE1   1 
ATOM   1253  N  NE2   . GLN A 1 150 ? 125.381 139.740 96.210  1.00 14.13 ?  150 GLN A NE2   1 
ATOM   1254  N  N     . PRO A 1 151 ? 127.762 141.917 95.714  1.00 25.42 ?  151 PRO A N     1 
ATOM   1255  C  CA    . PRO A 1 151 ? 128.075 142.403 97.060  1.00 16.72 ?  151 PRO A CA    1 
ATOM   1256  C  C     . PRO A 1 151 ? 127.897 141.296 98.087  1.00 18.06 ?  151 PRO A C     1 
ATOM   1257  O  O     . PRO A 1 151 ? 127.099 140.374 97.908  1.00 24.62 ?  151 PRO A O     1 
ATOM   1258  C  CB    . PRO A 1 151 ? 127.067 143.537 97.275  1.00 15.05 ?  151 PRO A CB    1 
ATOM   1259  C  CG    . PRO A 1 151 ? 126.641 143.936 95.903  1.00 20.42 ?  151 PRO A CG    1 
ATOM   1260  C  CD    . PRO A 1 151 ? 126.685 142.692 95.079  1.00 22.10 ?  151 PRO A CD    1 
ATOM   1261  N  N     . SER A 1 152 ? 128.667 141.389 99.168  1.00 20.26 ?  152 SER A N     1 
ATOM   1262  C  CA    . SER A 1 152 ? 128.641 140.363 100.197 1.00 16.72 ?  152 SER A CA    1 
ATOM   1263  C  C     . SER A 1 152 ? 127.248 140.235 100.807 1.00 23.77 ?  152 SER A C     1 
ATOM   1264  O  O     . SER A 1 152 ? 126.378 141.091 100.630 1.00 26.90 ?  152 SER A O     1 
ATOM   1265  C  CB    . SER A 1 152 ? 129.661 140.678 101.289 1.00 25.81 ?  152 SER A CB    1 
ATOM   1266  O  OG    . SER A 1 152 ? 129.261 141.804 102.046 1.00 28.95 ?  152 SER A OG    1 
ATOM   1267  N  N     . THR A 1 153 ? 127.044 139.134 101.529 1.00 30.12 ?  153 THR A N     1 
ATOM   1268  C  CA    . THR A 1 153 ? 125.763 138.881 102.186 1.00 23.96 ?  153 THR A CA    1 
ATOM   1269  C  C     . THR A 1 153 ? 125.300 140.031 103.074 1.00 30.26 ?  153 THR A C     1 
ATOM   1270  O  O     . THR A 1 153 ? 124.123 140.410 102.979 1.00 27.34 ?  153 THR A O     1 
ATOM   1271  C  CB    . THR A 1 153 ? 125.851 137.566 102.974 1.00 23.09 ?  153 THR A CB    1 
ATOM   1272  O  OG1   . THR A 1 153 ? 125.891 136.463 102.062 1.00 35.60 ?  153 THR A OG1   1 
ATOM   1273  C  CG2   . THR A 1 153 ? 124.657 137.404 103.902 1.00 24.13 ?  153 THR A CG2   1 
ATOM   1274  N  N     . PRO A 1 154 ? 126.138 140.634 103.929 1.00 29.45 ?  154 PRO A N     1 
ATOM   1275  C  CA    . PRO A 1 154 ? 125.652 141.794 104.700 1.00 21.01 ?  154 PRO A CA    1 
ATOM   1276  C  C     . PRO A 1 154 ? 125.217 142.957 103.826 1.00 22.76 ?  154 PRO A C     1 
ATOM   1277  O  O     . PRO A 1 154 ? 124.126 143.506 104.024 1.00 30.56 ?  154 PRO A O     1 
ATOM   1278  C  CB    . PRO A 1 154 ? 126.857 142.156 105.577 1.00 23.98 ?  154 PRO A CB    1 
ATOM   1279  C  CG    . PRO A 1 154 ? 127.662 140.928 105.642 1.00 21.87 ?  154 PRO A CG    1 
ATOM   1280  C  CD    . PRO A 1 154 ? 127.509 140.266 104.324 1.00 22.33 ?  154 PRO A CD    1 
ATOM   1281  N  N     . THR A 1 155 ? 126.042 143.345 102.852 1.00 22.52 ?  155 THR A N     1 
ATOM   1282  C  CA    . THR A 1 155 ? 125.698 144.474 101.995 1.00 22.76 ?  155 THR A CA    1 
ATOM   1283  C  C     . THR A 1 155 ? 124.483 144.161 101.132 1.00 25.20 ?  155 THR A C     1 
ATOM   1284  O  O     . THR A 1 155 ? 123.529 144.943 101.084 1.00 25.43 ?  155 THR A O     1 
ATOM   1285  C  CB    . THR A 1 155 ? 126.893 144.853 101.122 1.00 21.27 ?  155 THR A CB    1 
ATOM   1286  O  OG1   . THR A 1 155 ? 128.019 145.153 101.954 1.00 27.97 ?  155 THR A OG1   1 
ATOM   1287  C  CG2   . THR A 1 155 ? 126.565 146.067 100.275 1.00 16.40 ?  155 THR A CG2   1 
ATOM   1288  N  N     . PHE A 1 156 ? 124.495 143.014 100.451 1.00 27.54 ?  156 PHE A N     1 
ATOM   1289  C  CA    . PHE A 1 156 ? 123.383 142.663 99.574  1.00 25.07 ?  156 PHE A CA    1 
ATOM   1290  C  C     . PHE A 1 156 ? 122.086 142.500 100.357 1.00 27.98 ?  156 PHE A C     1 
ATOM   1291  O  O     . PHE A 1 156 ? 121.002 142.805 99.849  1.00 29.53 ?  156 PHE A O     1 
ATOM   1292  C  CB    . PHE A 1 156 ? 123.708 141.381 98.806  1.00 25.40 ?  156 PHE A CB    1 
ATOM   1293  C  CG    . PHE A 1 156 ? 122.833 141.152 97.610  1.00 27.47 ?  156 PHE A CG    1 
ATOM   1294  C  CD1   . PHE A 1 156 ? 122.746 142.102 96.608  1.00 24.32 ?  156 PHE A CD1   1 
ATOM   1295  C  CD2   . PHE A 1 156 ? 122.101 139.985 97.486  1.00 26.19 ?  156 PHE A CD2   1 
ATOM   1296  C  CE1   . PHE A 1 156 ? 121.943 141.892 95.505  1.00 28.99 ?  156 PHE A CE1   1 
ATOM   1297  C  CE2   . PHE A 1 156 ? 121.297 139.770 96.387  1.00 24.92 ?  156 PHE A CE2   1 
ATOM   1298  C  CZ    . PHE A 1 156 ? 121.219 140.725 95.395  1.00 29.97 ?  156 PHE A CZ    1 
ATOM   1299  N  N     . LEU A 1 157 ? 122.180 142.022 101.597 1.00 31.66 ?  157 LEU A N     1 
ATOM   1300  C  CA    . LEU A 1 157 ? 120.995 141.794 102.413 1.00 28.13 ?  157 LEU A CA    1 
ATOM   1301  C  C     . LEU A 1 157 ? 120.460 143.073 103.045 1.00 29.68 ?  157 LEU A C     1 
ATOM   1302  O  O     . LEU A 1 157 ? 119.245 143.208 103.211 1.00 37.88 ?  157 LEU A O     1 
ATOM   1303  C  CB    . LEU A 1 157 ? 121.311 140.765 103.500 1.00 31.34 ?  157 LEU A CB    1 
ATOM   1304  C  CG    . LEU A 1 157 ? 120.209 140.426 104.505 1.00 31.00 ?  157 LEU A CG    1 
ATOM   1305  C  CD1   . LEU A 1 157 ? 119.006 139.839 103.799 1.00 29.27 ?  157 LEU A CD1   1 
ATOM   1306  C  CD2   . LEU A 1 157 ? 120.729 139.469 105.563 1.00 28.33 ?  157 LEU A CD2   1 
ATOM   1307  N  N     . ASN A 1 158 ? 121.329 144.018 103.395 1.00 32.61 ?  158 ASN A N     1 
ATOM   1308  C  CA    . ASN A 1 158 ? 120.930 145.152 104.215 1.00 26.65 ?  158 ASN A CA    1 
ATOM   1309  C  C     . ASN A 1 158 ? 121.014 146.496 103.503 1.00 31.48 ?  158 ASN A C     1 
ATOM   1310  O  O     . ASN A 1 158 ? 120.627 147.509 104.091 1.00 38.42 ?  158 ASN A O     1 
ATOM   1311  C  CB    . ASN A 1 158 ? 121.780 145.194 105.489 1.00 29.21 ?  158 ASN A CB    1 
ATOM   1312  C  CG    . ASN A 1 158 ? 121.747 143.887 106.253 1.00 36.03 ?  158 ASN A CG    1 
ATOM   1313  O  OD1   . ASN A 1 158 ? 120.706 143.241 106.356 1.00 38.85 ?  158 ASN A OD1   1 
ATOM   1314  N  ND2   . ASN A 1 158 ? 122.892 143.488 106.791 1.00 32.53 ?  158 ASN A ND2   1 
ATOM   1315  N  N     . ALA A 1 159 ? 121.502 146.544 102.264 1.00 33.82 ?  159 ALA A N     1 
ATOM   1316  C  CA    . ALA A 1 159 ? 121.643 147.824 101.578 1.00 29.94 ?  159 ALA A CA    1 
ATOM   1317  C  C     . ALA A 1 159 ? 120.288 148.480 101.350 1.00 36.52 ?  159 ALA A C     1 
ATOM   1318  O  O     . ALA A 1 159 ? 119.462 147.968 100.588 1.00 42.82 ?  159 ALA A O     1 
ATOM   1319  C  CB    . ALA A 1 159 ? 122.371 147.654 100.245 1.00 34.55 ?  159 ALA A CB    1 
ATOM   1320  N  N     . GLY A 1 160 ? 120.054 149.612 102.007 1.00 43.17 ?  160 GLY A N     1 
ATOM   1321  C  CA    . GLY A 1 160 ? 118.821 150.350 101.846 1.00 40.60 ?  160 GLY A CA    1 
ATOM   1322  C  C     . GLY A 1 160 ? 117.680 149.932 102.744 1.00 44.10 ?  160 GLY A C     1 
ATOM   1323  O  O     . GLY A 1 160 ? 116.565 150.434 102.566 1.00 45.10 ?  160 GLY A O     1 
ATOM   1324  N  N     . ARG A 1 161 ? 117.914 149.035 103.696 1.00 44.10 ?  161 ARG A N     1 
ATOM   1325  C  CA    . ARG A 1 161 ? 116.883 148.591 104.623 1.00 43.77 ?  161 ARG A CA    1 
ATOM   1326  C  C     . ARG A 1 161 ? 116.999 149.353 105.935 1.00 45.82 ?  161 ARG A C     1 
ATOM   1327  O  O     . ARG A 1 161 ? 118.105 149.642 106.401 1.00 48.53 ?  161 ARG A O     1 
ATOM   1328  C  CB    . ARG A 1 161 ? 116.985 147.086 104.875 1.00 41.51 ?  161 ARG A CB    1 
ATOM   1329  C  CG    . ARG A 1 161 ? 116.725 146.243 103.640 1.00 42.22 ?  161 ARG A CG    1 
ATOM   1330  C  CD    . ARG A 1 161 ? 116.483 144.788 103.993 1.00 41.57 ?  161 ARG A CD    1 
ATOM   1331  N  NE    . ARG A 1 161 ? 116.495 143.940 102.808 1.00 45.49 ?  161 ARG A NE    1 
ATOM   1332  C  CZ    . ARG A 1 161 ? 116.358 142.621 102.826 1.00 45.46 ?  161 ARG A CZ    1 
ATOM   1333  N  NH1   . ARG A 1 161 ? 116.192 141.958 103.958 1.00 43.98 1  161 ARG A NH1   1 
ATOM   1334  N  NH2   . ARG A 1 161 ? 116.395 141.950 101.679 1.00 42.72 ?  161 ARG A NH2   1 
ATOM   1335  N  N     . LYS A 1 162 ? 115.848 149.682 106.527 1.00 53.82 ?  162 LYS A N     1 
ATOM   1336  C  CA    . LYS A 1 162 ? 115.847 150.464 107.760 1.00 52.61 ?  162 LYS A CA    1 
ATOM   1337  C  C     . LYS A 1 162 ? 116.302 149.625 108.947 1.00 54.80 ?  162 LYS A C     1 
ATOM   1338  O  O     . LYS A 1 162 ? 117.323 149.923 109.577 1.00 55.62 ?  162 LYS A O     1 
ATOM   1339  C  CB    . LYS A 1 162 ? 114.453 151.038 108.014 1.00 52.45 ?  162 LYS A CB    1 
ATOM   1340  C  CG    . LYS A 1 162 ? 114.453 152.461 108.543 1.00 55.20 ?  162 LYS A CG    1 
ATOM   1341  C  CD    . LYS A 1 162 ? 113.076 153.093 108.428 1.00 55.29 ?  162 LYS A CD    1 
ATOM   1342  C  CE    . LYS A 1 162 ? 113.161 154.610 108.447 1.00 54.69 ?  162 LYS A CE    1 
ATOM   1343  N  NZ    . LYS A 1 162 ? 114.374 155.088 109.165 1.00 55.20 1  162 LYS A NZ    1 
ATOM   1344  N  N     . ARG A 1 163 ? 115.556 148.570 109.265 1.00 57.23 ?  163 ARG A N     1 
ATOM   1345  C  CA    . ARG A 1 163 ? 115.892 147.692 110.385 1.00 57.25 ?  163 ARG A CA    1 
ATOM   1346  C  C     . ARG A 1 163 ? 116.889 146.637 109.913 1.00 58.83 ?  163 ARG A C     1 
ATOM   1347  O  O     . ARG A 1 163 ? 116.555 145.488 109.620 1.00 57.95 ?  163 ARG A O     1 
ATOM   1348  C  CB    . ARG A 1 163 ? 114.626 147.067 110.963 1.00 60.18 ?  163 ARG A CB    1 
ATOM   1349  C  CG    . ARG A 1 163 ? 113.659 148.084 111.548 1.00 58.41 ?  163 ARG A CG    1 
ATOM   1350  C  CD    . ARG A 1 163 ? 112.301 147.466 111.822 1.00 58.40 ?  163 ARG A CD    1 
ATOM   1351  N  NE    . ARG A 1 163 ? 111.640 147.054 110.590 1.00 60.59 ?  163 ARG A NE    1 
ATOM   1352  C  CZ    . ARG A 1 163 ? 110.526 146.337 110.542 1.00 62.32 ?  163 ARG A CZ    1 
ATOM   1353  N  NH1   . ARG A 1 163 ? 109.909 145.945 111.644 1.00 61.42 1  163 ARG A NH1   1 
ATOM   1354  N  NH2   . ARG A 1 163 ? 110.016 146.008 109.358 1.00 59.59 ?  163 ARG A NH2   1 
ATOM   1355  N  N     . ARG A 1 164 ? 118.144 147.067 109.844 1.00 53.64 ?  164 ARG A N     1 
ATOM   1356  C  CA    . ARG A 1 164 ? 119.218 146.293 109.248 1.00 50.73 ?  164 ARG A CA    1 
ATOM   1357  C  C     . ARG A 1 164 ? 120.405 146.208 110.196 1.00 51.26 ?  164 ARG A C     1 
ATOM   1358  O  O     . ARG A 1 164 ? 120.568 147.028 111.104 1.00 52.65 ?  164 ARG A O     1 
ATOM   1359  C  CB    . ARG A 1 164 ? 119.674 146.917 107.925 1.00 49.66 ?  164 ARG A CB    1 
ATOM   1360  C  CG    . ARG A 1 164 ? 120.440 148.223 108.107 1.00 46.69 ?  164 ARG A CG    1 
ATOM   1361  C  CD    . ARG A 1 164 ? 121.342 148.506 106.923 1.00 49.28 ?  164 ARG A CD    1 
ATOM   1362  N  NE    . ARG A 1 164 ? 122.146 149.709 107.102 1.00 50.57 ?  164 ARG A NE    1 
ATOM   1363  C  CZ    . ARG A 1 164 ? 122.378 150.600 106.148 1.00 51.84 ?  164 ARG A CZ    1 
ATOM   1364  N  NH1   . ARG A 1 164 ? 121.867 150.462 104.934 1.00 47.62 1  164 ARG A NH1   1 
ATOM   1365  N  NH2   . ARG A 1 164 ? 123.140 151.655 106.416 1.00 50.81 ?  164 ARG A NH2   1 
ATOM   1366  N  N     . GLY A 1 165 ? 121.236 145.195 109.973 1.00 45.41 ?  165 GLY A N     1 
ATOM   1367  C  CA    . GLY A 1 165 ? 122.538 145.126 110.592 1.00 42.70 ?  165 GLY A CA    1 
ATOM   1368  C  C     . GLY A 1 165 ? 123.551 145.935 109.806 1.00 47.81 ?  165 GLY A C     1 
ATOM   1369  O  O     . GLY A 1 165 ? 123.225 146.676 108.877 1.00 44.98 ?  165 GLY A O     1 
ATOM   1370  N  N     . GLU A 1 166 ? 124.813 145.788 110.195 1.00 45.86 ?  166 GLU A N     1 
ATOM   1371  C  CA    . GLU A 1 166 ? 125.871 146.490 109.490 1.00 39.66 ?  166 GLU A CA    1 
ATOM   1372  C  C     . GLU A 1 166 ? 126.164 145.814 108.154 1.00 37.91 ?  166 GLU A C     1 
ATOM   1373  O  O     . GLU A 1 166 ? 125.869 144.635 107.943 1.00 38.58 ?  166 GLU A O     1 
ATOM   1374  C  CB    . GLU A 1 166 ? 127.139 146.551 110.339 1.00 37.81 ?  166 GLU A CB    1 
ATOM   1375  C  CG    . GLU A 1 166 ? 127.083 147.576 111.460 1.00 41.94 ?  166 GLU A CG    1 
ATOM   1376  C  CD    . GLU A 1 166 ? 126.868 148.992 110.957 1.00 47.92 ?  166 GLU A CD    1 
ATOM   1377  O  OE1   . GLU A 1 166 ? 127.307 149.305 109.830 1.00 46.33 ?  166 GLU A OE1   1 
ATOM   1378  O  OE2   . GLU A 1 166 ? 126.260 149.797 111.694 1.00 45.41 -1 166 GLU A OE2   1 
ATOM   1379  N  N     . LEU A 1 167 ? 126.751 146.587 107.242 1.00 33.25 ?  167 LEU A N     1 
ATOM   1380  C  CA    . LEU A 1 167 ? 127.160 146.059 105.948 1.00 25.75 ?  167 LEU A CA    1 
ATOM   1381  C  C     . LEU A 1 167 ? 128.496 145.334 106.009 1.00 30.06 ?  167 LEU A C     1 
ATOM   1382  O  O     . LEU A 1 167 ? 128.894 144.716 105.017 1.00 32.58 ?  167 LEU A O     1 
ATOM   1383  C  CB    . LEU A 1 167 ? 127.235 147.186 104.917 1.00 27.51 ?  167 LEU A CB    1 
ATOM   1384  C  CG    . LEU A 1 167 ? 125.952 147.960 104.610 1.00 28.18 ?  167 LEU A CG    1 
ATOM   1385  C  CD1   . LEU A 1 167 ? 126.052 148.611 103.249 1.00 31.34 ?  167 LEU A CD1   1 
ATOM   1386  C  CD2   . LEU A 1 167 ? 124.738 147.058 104.671 1.00 28.89 ?  167 LEU A CD2   1 
ATOM   1387  N  N     . VAL A 1 168 ? 129.191 145.398 107.140 1.00 33.17 ?  168 VAL A N     1 
ATOM   1388  C  CA    . VAL A 1 168 ? 130.439 144.682 107.359 1.00 26.44 ?  168 VAL A CA    1 
ATOM   1389  C  C     . VAL A 1 168 ? 130.190 143.607 108.405 1.00 30.61 ?  168 VAL A C     1 
ATOM   1390  O  O     . VAL A 1 168 ? 129.547 143.863 109.430 1.00 36.41 ?  168 VAL A O     1 
ATOM   1391  C  CB    . VAL A 1 168 ? 131.565 145.636 107.805 1.00 26.26 ?  168 VAL A CB    1 
ATOM   1392  C  CG1   . VAL A 1 168 ? 132.869 144.880 107.977 1.00 29.07 ?  168 VAL A CG1   1 
ATOM   1393  C  CG2   . VAL A 1 168 ? 131.728 146.764 106.802 1.00 31.34 ?  168 VAL A CG2   1 
ATOM   1394  N  N     . SER A 1 169 ? 130.692 142.402 108.148 1.00 29.13 ?  169 SER A N     1 
ATOM   1395  C  CA    . SER A 1 169 ? 130.505 141.288 109.065 1.00 30.02 ?  169 SER A CA    1 
ATOM   1396  C  C     . SER A 1 169 ? 131.806 140.667 109.550 1.00 25.74 ?  169 SER A C     1 
ATOM   1397  O  O     . SER A 1 169 ? 131.760 139.753 110.380 1.00 31.17 ?  169 SER A O     1 
ATOM   1398  C  CB    . SER A 1 169 ? 129.637 140.200 108.422 1.00 33.72 ?  169 SER A CB    1 
ATOM   1399  O  OG    . SER A 1 169 ? 128.270 140.392 108.743 1.00 37.71 ?  169 SER A OG    1 
ATOM   1400  N  N     . CYS A 1 170 ? 132.955 141.120 109.065 1.00 28.39 ?  170 CYS A N     1 
ATOM   1401  C  CA    . CYS A 1 170 ? 134.242 140.625 109.531 1.00 26.92 ?  170 CYS A CA    1 
ATOM   1402  C  C     . CYS A 1 170 ? 134.928 141.730 110.321 1.00 25.20 ?  170 CYS A C     1 
ATOM   1403  O  O     . CYS A 1 170 ? 135.119 142.839 109.812 1.00 27.42 ?  170 CYS A O     1 
ATOM   1404  C  CB    . CYS A 1 170 ? 135.112 140.147 108.365 1.00 33.70 ?  170 CYS A CB    1 
ATOM   1405  S  SG    . CYS A 1 170 ? 135.681 141.414 107.204 1.00 51.33 ?  170 CYS A SG    1 
ATOM   1406  N  N     . PHE A 1 171 ? 135.268 141.433 111.572 1.00 22.44 ?  171 PHE A N     1 
ATOM   1407  C  CA    . PHE A 1 171 ? 135.974 142.358 112.442 1.00 16.13 ?  171 PHE A CA    1 
ATOM   1408  C  C     . PHE A 1 171 ? 137.128 141.632 113.112 1.00 16.35 ?  171 PHE A C     1 
ATOM   1409  O  O     . PHE A 1 171 ? 137.007 140.459 113.476 1.00 27.33 ?  171 PHE A O     1 
ATOM   1410  C  CB    . PHE A 1 171 ? 135.043 142.957 113.503 1.00 17.63 ?  171 PHE A CB    1 
ATOM   1411  C  CG    . PHE A 1 171 ? 133.822 143.614 112.934 1.00 17.41 ?  171 PHE A CG    1 
ATOM   1412  C  CD1   . PHE A 1 171 ? 133.886 144.900 112.430 1.00 16.60 ?  171 PHE A CD1   1 
ATOM   1413  C  CD2   . PHE A 1 171 ? 132.610 142.947 112.906 1.00 16.10 ?  171 PHE A CD2   1 
ATOM   1414  C  CE1   . PHE A 1 171 ? 132.767 145.506 111.905 1.00 15.99 ?  171 PHE A CE1   1 
ATOM   1415  C  CE2   . PHE A 1 171 ? 131.489 143.550 112.383 1.00 16.69 ?  171 PHE A CE2   1 
ATOM   1416  C  CZ    . PHE A 1 171 ? 131.567 144.830 111.883 1.00 14.78 ?  171 PHE A CZ    1 
ATOM   1417  N  N     . LEU A 1 172 ? 138.246 142.334 113.264 1.00 17.80 ?  172 LEU A N     1 
ATOM   1418  C  CA    . LEU A 1 172 ? 139.443 141.792 113.891 1.00 7.46  ?  172 LEU A CA    1 
ATOM   1419  C  C     . LEU A 1 172 ? 139.840 142.712 115.031 1.00 13.17 ?  172 LEU A C     1 
ATOM   1420  O  O     . LEU A 1 172 ? 140.017 143.916 114.824 1.00 17.99 ?  172 LEU A O     1 
ATOM   1421  C  CB    . LEU A 1 172 ? 140.592 141.664 112.883 1.00 12.46 ?  172 LEU A CB    1 
ATOM   1422  C  CG    . LEU A 1 172 ? 140.496 140.608 111.781 1.00 7.26  ?  172 LEU A CG    1 
ATOM   1423  C  CD1   . LEU A 1 172 ? 139.609 141.084 110.644 1.00 11.37 ?  172 LEU A CD1   1 
ATOM   1424  C  CD2   . LEU A 1 172 ? 141.879 140.269 111.266 1.00 11.04 ?  172 LEU A CD2   1 
ATOM   1425  N  N     . LEU A 1 173 ? 139.981 142.151 116.228 1.00 22.03 ?  173 LEU A N     1 
ATOM   1426  C  CA    . LEU A 1 173 ? 140.267 142.925 117.427 1.00 9.24  ?  173 LEU A CA    1 
ATOM   1427  C  C     . LEU A 1 173 ? 141.599 142.501 118.027 1.00 16.79 ?  173 LEU A C     1 
ATOM   1428  O  O     . LEU A 1 173 ? 141.884 141.307 118.150 1.00 26.59 ?  173 LEU A O     1 
ATOM   1429  C  CB    . LEU A 1 173 ? 139.168 142.757 118.478 1.00 14.56 ?  173 LEU A CB    1 
ATOM   1430  C  CG    . LEU A 1 173 ? 137.715 142.997 118.071 1.00 16.55 ?  173 LEU A CG    1 
ATOM   1431  C  CD1   . LEU A 1 173 ? 136.823 142.861 119.289 1.00 20.59 ?  173 LEU A CD1   1 
ATOM   1432  C  CD2   . LEU A 1 173 ? 137.539 144.356 117.420 1.00 15.88 ?  173 LEU A CD2   1 
ATOM   1433  N  N     . GLU A 1 174 ? 142.406 143.485 118.402 1.00 23.22 ?  174 GLU A N     1 
ATOM   1434  C  CA    . GLU A 1 174 ? 143.632 143.255 119.153 1.00 19.58 ?  174 GLU A CA    1 
ATOM   1435  C  C     . GLU A 1 174 ? 143.340 143.477 120.631 1.00 17.36 ?  174 GLU A C     1 
ATOM   1436  O  O     . GLU A 1 174 ? 142.815 144.528 121.011 1.00 29.19 ?  174 GLU A O     1 
ATOM   1437  C  CB    . GLU A 1 174 ? 144.750 144.184 118.681 1.00 22.04 ?  174 GLU A CB    1 
ATOM   1438  C  CG    . GLU A 1 174 ? 145.295 143.862 117.308 1.00 20.41 ?  174 GLU A CG    1 
ATOM   1439  C  CD    . GLU A 1 174 ? 146.771 143.530 117.339 1.00 19.96 ?  174 GLU A CD    1 
ATOM   1440  O  OE1   . GLU A 1 174 ? 147.593 144.468 117.346 1.00 22.11 ?  174 GLU A OE1   1 
ATOM   1441  O  OE2   . GLU A 1 174 ? 147.110 142.330 117.353 1.00 32.00 -1 174 GLU A OE2   1 
ATOM   1442  N  N     . VAL A 1 175 ? 143.677 142.494 121.457 1.00 18.09 ?  175 VAL A N     1 
ATOM   1443  C  CA    . VAL A 1 175 ? 143.426 142.552 122.892 1.00 21.78 ?  175 VAL A CA    1 
ATOM   1444  C  C     . VAL A 1 175 ? 144.748 142.804 123.602 1.00 19.70 ?  175 VAL A C     1 
ATOM   1445  O  O     . VAL A 1 175 ? 145.700 142.028 123.451 1.00 21.46 ?  175 VAL A O     1 
ATOM   1446  C  CB    . VAL A 1 175 ? 142.765 141.261 123.400 1.00 21.89 ?  175 VAL A CB    1 
ATOM   1447  C  CG1   . VAL A 1 175 ? 142.108 141.495 124.751 1.00 15.48 ?  175 VAL A CG1   1 
ATOM   1448  C  CG2   . VAL A 1 175 ? 141.754 140.749 122.390 1.00 17.38 ?  175 VAL A CG2   1 
ATOM   1449  N  N     . ASN A 1 176 ? 144.809 143.883 124.375 1.00 15.24 ?  176 ASN A N     1 
ATOM   1450  C  CA    . ASN A 1 176 ? 145.996 144.188 125.154 1.00 18.20 ?  176 ASN A CA    1 
ATOM   1451  C  C     . ASN A 1 176 ? 146.002 143.387 126.453 1.00 21.81 ?  176 ASN A C     1 
ATOM   1452  O  O     . ASN A 1 176 ? 144.979 142.860 126.896 1.00 21.13 ?  176 ASN A O     1 
ATOM   1453  C  CB    . ASN A 1 176 ? 146.075 145.684 125.454 1.00 18.41 ?  176 ASN A CB    1 
ATOM   1454  C  CG    . ASN A 1 176 ? 147.481 146.223 125.356 1.00 23.52 ?  176 ASN A CG    1 
ATOM   1455  O  OD1   . ASN A 1 176 ? 148.452 145.480 125.479 1.00 27.38 ?  176 ASN A OD1   1 
ATOM   1456  N  ND2   . ASN A 1 176 ? 147.600 147.524 125.128 1.00 21.82 ?  176 ASN A ND2   1 
ATOM   1457  N  N     . ASP A 1 177 ? 147.181 143.310 127.070 1.00 29.34 ?  177 ASP A N     1 
ATOM   1458  C  CA    . ASP A 1 177 ? 147.390 142.476 128.253 1.00 22.42 ?  177 ASP A CA    1 
ATOM   1459  C  C     . ASP A 1 177 ? 146.979 143.241 129.514 1.00 22.88 ?  177 ASP A C     1 
ATOM   1460  O  O     . ASP A 1 177 ? 147.797 143.649 130.338 1.00 27.43 ?  177 ASP A O     1 
ATOM   1461  C  CB    . ASP A 1 177 ? 148.840 142.017 128.322 1.00 21.20 ?  177 ASP A CB    1 
ATOM   1462  C  CG    . ASP A 1 177 ? 149.070 140.969 129.387 1.00 27.82 ?  177 ASP A CG    1 
ATOM   1463  O  OD1   . ASP A 1 177 ? 148.164 140.142 129.612 1.00 30.56 ?  177 ASP A OD1   1 
ATOM   1464  O  OD2   . ASP A 1 177 ? 150.160 140.969 129.994 1.00 29.71 -1 177 ASP A OD2   1 
ATOM   1465  N  N     . SER A 1 178 ? 145.670 143.426 129.651 1.00 22.26 ?  178 SER A N     1 
ATOM   1466  C  CA    . SER A 1 178 ? 145.122 144.088 130.825 1.00 18.11 ?  178 SER A CA    1 
ATOM   1467  C  C     . SER A 1 178 ? 143.677 143.651 131.007 1.00 20.63 ?  178 SER A C     1 
ATOM   1468  O  O     . SER A 1 178 ? 143.015 143.224 130.060 1.00 29.47 ?  178 SER A O     1 
ATOM   1469  C  CB    . SER A 1 178 ? 145.220 145.611 130.710 1.00 19.31 ?  178 SER A CB    1 
ATOM   1470  O  OG    . SER A 1 178 ? 144.009 146.168 130.238 1.00 25.10 ?  178 SER A OG    1 
ATOM   1471  N  N     . LEU A 1 179 ? 143.196 143.764 132.248 1.00 27.75 ?  179 LEU A N     1 
ATOM   1472  C  CA    . LEU A 1 179 ? 141.805 143.429 132.534 1.00 20.46 ?  179 LEU A CA    1 
ATOM   1473  C  C     . LEU A 1 179 ? 140.856 144.451 131.925 1.00 22.67 ?  179 LEU A C     1 
ATOM   1474  O  O     . LEU A 1 179 ? 139.756 144.099 131.486 1.00 27.44 ?  179 LEU A O     1 
ATOM   1475  C  CB    . LEU A 1 179 ? 141.583 143.329 134.043 1.00 23.33 ?  179 LEU A CB    1 
ATOM   1476  C  CG    . LEU A 1 179 ? 140.226 142.782 134.487 1.00 22.04 ?  179 LEU A CG    1 
ATOM   1477  C  CD1   . LEU A 1 179 ? 140.118 141.299 134.177 1.00 24.32 ?  179 LEU A CD1   1 
ATOM   1478  C  CD2   . LEU A 1 179 ? 140.000 143.046 135.964 1.00 21.57 ?  179 LEU A CD2   1 
ATOM   1479  N  N     . ASN A 1 180 ? 141.255 145.725 131.904 1.00 23.10 ?  180 ASN A N     1 
ATOM   1480  C  CA    . ASN A 1 180 ? 140.448 146.738 131.233 1.00 21.89 ?  180 ASN A CA    1 
ATOM   1481  C  C     . ASN A 1 180 ? 140.309 146.423 129.751 1.00 26.71 ?  180 ASN A C     1 
ATOM   1482  O  O     . ASN A 1 180 ? 139.214 146.515 129.185 1.00 30.16 ?  180 ASN A O     1 
ATOM   1483  C  CB    . ASN A 1 180 ? 141.072 148.119 131.425 1.00 22.57 ?  180 ASN A CB    1 
ATOM   1484  C  CG    . ASN A 1 180 ? 140.714 148.744 132.754 1.00 27.08 ?  180 ASN A CG    1 
ATOM   1485  O  OD1   . ASN A 1 180 ? 139.686 148.423 133.350 1.00 33.00 ?  180 ASN A OD1   1 
ATOM   1486  N  ND2   . ASN A 1 180 ? 141.562 149.647 133.227 1.00 27.92 ?  180 ASN A ND2   1 
ATOM   1487  N  N     . ASP A 1 181 ? 141.411 146.028 129.114 1.00 25.42 ?  181 ASP A N     1 
ATOM   1488  C  CA    . ASP A 1 181 ? 141.372 145.695 127.696 1.00 16.89 ?  181 ASP A CA    1 
ATOM   1489  C  C     . ASP A 1 181 ? 140.609 144.404 127.439 1.00 20.98 ?  181 ASP A C     1 
ATOM   1490  O  O     . ASP A 1 181 ? 139.941 144.284 126.411 1.00 25.91 ?  181 ASP A O     1 
ATOM   1491  C  CB    . ASP A 1 181 ? 142.791 145.608 127.146 1.00 20.00 ?  181 ASP A CB    1 
ATOM   1492  C  CG    . ASP A 1 181 ? 143.427 146.971 126.971 1.00 32.71 ?  181 ASP A CG    1 
ATOM   1493  O  OD1   . ASP A 1 181 ? 143.095 147.659 125.984 1.00 36.80 ?  181 ASP A OD1   1 
ATOM   1494  O  OD2   . ASP A 1 181 ? 144.260 147.357 127.817 1.00 30.19 -1 181 ASP A OD2   1 
ATOM   1495  N  N     . ILE A 1 182 ? 140.678 143.437 128.353 1.00 21.36 ?  182 ILE A N     1 
ATOM   1496  C  CA    . ILE A 1 182 ? 139.909 142.206 128.183 1.00 21.47 ?  182 ILE A CA    1 
ATOM   1497  C  C     . ILE A 1 182 ? 138.416 142.485 128.322 1.00 18.86 ?  182 ILE A C     1 
ATOM   1498  O  O     . ILE A 1 182 ? 137.598 141.963 127.553 1.00 24.47 ?  182 ILE A O     1 
ATOM   1499  C  CB    . ILE A 1 182 ? 140.391 141.139 129.184 1.00 24.51 ?  182 ILE A CB    1 
ATOM   1500  C  CG1   . ILE A 1 182 ? 141.745 140.585 128.743 1.00 20.55 ?  182 ILE A CG1   1 
ATOM   1501  C  CG2   . ILE A 1 182 ? 139.373 140.016 129.312 1.00 26.74 ?  182 ILE A CG2   1 
ATOM   1502  C  CD1   . ILE A 1 182 ? 142.428 139.755 129.790 1.00 22.39 ?  182 ILE A CD1   1 
ATOM   1503  N  N     . SER A 1 183 ? 138.038 143.315 129.297 1.00 22.49 ?  183 SER A N     1 
ATOM   1504  C  CA    . SER A 1 183 ? 136.639 143.700 129.444 1.00 21.31 ?  183 SER A CA    1 
ATOM   1505  C  C     . SER A 1 183 ? 136.148 144.461 128.220 1.00 24.12 ?  183 SER A C     1 
ATOM   1506  O  O     . SER A 1 183 ? 135.036 144.219 127.733 1.00 30.09 ?  183 SER A O     1 
ATOM   1507  C  CB    . SER A 1 183 ? 136.458 144.543 130.703 1.00 21.24 ?  183 SER A CB    1 
ATOM   1508  O  OG    . SER A 1 183 ? 137.063 143.930 131.826 1.00 32.18 ?  183 SER A OG    1 
ATOM   1509  N  N     . ARG A 1 184 ? 136.963 145.384 127.709 1.00 23.49 ?  184 ARG A N     1 
ATOM   1510  C  CA    . ARG A 1 184 ? 136.583 146.104 126.500 1.00 23.99 ?  184 ARG A CA    1 
ATOM   1511  C  C     . ARG A 1 184 ? 136.495 145.176 125.298 1.00 28.93 ?  184 ARG A C     1 
ATOM   1512  O  O     . ARG A 1 184 ? 135.638 145.372 124.434 1.00 33.36 ?  184 ARG A O     1 
ATOM   1513  C  CB    . ARG A 1 184 ? 137.565 147.237 126.225 1.00 23.38 ?  184 ARG A CB    1 
ATOM   1514  C  CG    . ARG A 1 184 ? 136.973 148.358 125.396 1.00 27.12 ?  184 ARG A CG    1 
ATOM   1515  C  CD    . ARG A 1 184 ? 136.411 149.452 126.279 1.00 31.20 ?  184 ARG A CD    1 
ATOM   1516  N  NE    . ARG A 1 184 ? 134.976 149.618 126.091 1.00 31.34 ?  184 ARG A NE    1 
ATOM   1517  C  CZ    . ARG A 1 184 ? 134.242 150.533 126.710 1.00 35.55 ?  184 ARG A CZ    1 
ATOM   1518  N  NH1   . ARG A 1 184 ? 134.781 151.387 127.564 1.00 33.29 1  184 ARG A NH1   1 
ATOM   1519  N  NH2   . ARG A 1 184 ? 132.937 150.593 126.465 1.00 29.20 ?  184 ARG A NH2   1 
ATOM   1520  N  N     . ALA A 1 185 ? 137.368 144.170 125.220 1.00 28.47 ?  185 ALA A N     1 
ATOM   1521  C  CA    . ALA A 1 185 ? 137.288 143.202 124.134 1.00 15.38 ?  185 ALA A CA    1 
ATOM   1522  C  C     . ALA A 1 185 ? 135.994 142.407 124.204 1.00 21.04 ?  185 ALA A C     1 
ATOM   1523  O  O     . ALA A 1 185 ? 135.346 142.176 123.180 1.00 25.07 ?  185 ALA A O     1 
ATOM   1524  C  CB    . ALA A 1 185 ? 138.495 142.269 124.171 1.00 17.48 ?  185 ALA A CB    1 
ATOM   1525  N  N     . ILE A 1 186 ? 135.598 141.985 125.407 1.00 24.51 ?  186 ILE A N     1 
ATOM   1526  C  CA    . ILE A 1 186 ? 134.332 141.272 125.565 1.00 20.17 ?  186 ILE A CA    1 
ATOM   1527  C  C     . ILE A 1 186 ? 133.165 142.164 125.161 1.00 20.92 ?  186 ILE A C     1 
ATOM   1528  O  O     . ILE A 1 186 ? 132.252 141.737 124.440 1.00 27.02 ?  186 ILE A O     1 
ATOM   1529  C  CB    . ILE A 1 186 ? 134.180 140.769 127.013 1.00 27.30 ?  186 ILE A CB    1 
ATOM   1530  C  CG1   . ILE A 1 186 ? 135.166 139.640 127.299 1.00 24.05 ?  186 ILE A CG1   1 
ATOM   1531  C  CG2   . ILE A 1 186 ? 132.754 140.310 127.277 1.00 27.00 ?  186 ILE A CG2   1 
ATOM   1532  C  CD1   . ILE A 1 186 ? 135.370 139.385 128.774 1.00 25.30 ?  186 ILE A CD1   1 
ATOM   1533  N  N     . ASP A 1 187 ? 133.183 143.420 125.614 1.00 27.48 ?  187 ASP A N     1 
ATOM   1534  C  CA    . ASP A 1 187 ? 132.106 144.349 125.287 1.00 23.22 ?  187 ASP A CA    1 
ATOM   1535  C  C     . ASP A 1 187 ? 132.014 144.581 123.785 1.00 27.24 ?  187 ASP A C     1 
ATOM   1536  O  O     . ASP A 1 187 ? 130.927 144.527 123.205 1.00 32.57 ?  187 ASP A O     1 
ATOM   1537  C  CB    . ASP A 1 187 ? 132.320 145.670 126.026 1.00 22.13 ?  187 ASP A CB    1 
ATOM   1538  C  CG    . ASP A 1 187 ? 131.477 146.798 125.463 1.00 34.84 ?  187 ASP A CG    1 
ATOM   1539  O  OD1   . ASP A 1 187 ? 130.247 146.625 125.342 1.00 36.41 ?  187 ASP A OD1   1 
ATOM   1540  O  OD2   . ASP A 1 187 ? 132.047 147.861 125.140 1.00 37.56 -1 187 ASP A OD2   1 
ATOM   1541  N  N     . ILE A 1 188 ? 133.154 144.833 123.138 1.00 25.83 ?  188 ILE A N     1 
ATOM   1542  C  CA    . ILE A 1 188 ? 133.165 145.109 121.706 1.00 22.68 ?  188 ILE A CA    1 
ATOM   1543  C  C     . ILE A 1 188 ? 132.768 143.867 120.920 1.00 22.53 ?  188 ILE A C     1 
ATOM   1544  O  O     . ILE A 1 188 ? 132.080 143.958 119.899 1.00 28.19 ?  188 ILE A O     1 
ATOM   1545  C  CB    . ILE A 1 188 ? 134.544 145.641 121.278 1.00 25.08 ?  188 ILE A CB    1 
ATOM   1546  C  CG1   . ILE A 1 188 ? 134.787 147.029 121.868 1.00 23.81 ?  188 ILE A CG1   1 
ATOM   1547  C  CG2   . ILE A 1 188 ? 134.658 145.708 119.769 1.00 21.04 ?  188 ILE A CG2   1 
ATOM   1548  C  CD1   . ILE A 1 188 ? 136.143 147.596 121.542 1.00 23.99 ?  188 ILE A CD1   1 
ATOM   1549  N  N     . SER A 1 189 ? 133.188 142.688 121.383 1.00 24.80 ?  189 SER A N     1 
ATOM   1550  C  CA    . SER A 1 189 ? 132.790 141.452 120.725 1.00 14.85 ?  189 SER A CA    1 
ATOM   1551  C  C     . SER A 1 189 ? 131.282 141.264 120.784 1.00 21.48 ?  189 SER A C     1 
ATOM   1552  O  O     . SER A 1 189 ? 130.661 140.894 119.783 1.00 28.50 ?  189 SER A O     1 
ATOM   1553  C  CB    . SER A 1 189 ? 133.504 140.263 121.367 1.00 20.15 ?  189 SER A CB    1 
ATOM   1554  O  OG    . SER A 1 189 ? 134.899 140.488 121.444 1.00 24.99 ?  189 SER A OG    1 
ATOM   1555  N  N     . MET A 1 190 ? 130.674 141.523 121.943 1.00 24.96 ?  190 MET A N     1 
ATOM   1556  C  CA    . MET A 1 190 ? 129.221 141.418 122.033 1.00 25.46 ?  190 MET A CA    1 
ATOM   1557  C  C     . MET A 1 190 ? 128.529 142.478 121.184 1.00 24.52 ?  190 MET A C     1 
ATOM   1558  O  O     . MET A 1 190 ? 127.503 142.200 120.555 1.00 25.65 ?  190 MET A O     1 
ATOM   1559  C  CB    . MET A 1 190 ? 128.763 141.506 123.488 1.00 24.20 ?  190 MET A CB    1 
ATOM   1560  C  CG    . MET A 1 190 ? 128.921 140.203 124.253 1.00 25.61 ?  190 MET A CG    1 
ATOM   1561  S  SD    . MET A 1 190 ? 128.702 140.350 126.035 1.00 39.39 ?  190 MET A SD    1 
ATOM   1562  C  CE    . MET A 1 190 ? 128.916 142.108 126.264 1.00 30.50 ?  190 MET A CE    1 
ATOM   1563  N  N     . GLN A 1 191 ? 129.072 143.697 121.148 1.00 20.97 ?  191 GLN A N     1 
ATOM   1564  C  CA    . GLN A 1 191 ? 128.471 144.750 120.333 1.00 27.46 ?  191 GLN A CA    1 
ATOM   1565  C  C     . GLN A 1 191 ? 128.512 144.401 118.850 1.00 26.57 ?  191 GLN A C     1 
ATOM   1566  O  O     . GLN A 1 191 ? 127.534 144.622 118.127 1.00 30.30 ?  191 GLN A O     1 
ATOM   1567  C  CB    . GLN A 1 191 ? 129.175 146.085 120.582 1.00 28.45 ?  191 GLN A CB    1 
ATOM   1568  C  CG    . GLN A 1 191 ? 129.033 146.621 121.994 1.00 26.96 ?  191 GLN A CG    1 
ATOM   1569  C  CD    . GLN A 1 191 ? 127.616 147.036 122.331 1.00 29.87 ?  191 GLN A CD    1 
ATOM   1570  O  OE1   . GLN A 1 191 ? 127.206 146.988 123.489 1.00 30.00 ?  191 GLN A OE1   1 
ATOM   1571  N  NE2   . GLN A 1 191 ? 126.863 147.459 121.322 1.00 30.62 ?  191 GLN A NE2   1 
ATOM   1572  N  N     . LEU A 1 192 ? 129.637 143.861 118.377 1.00 26.64 ?  192 LEU A N     1 
ATOM   1573  C  CA    . LEU A 1 192 ? 129.771 143.532 116.964 1.00 21.91 ?  192 LEU A CA    1 
ATOM   1574  C  C     . LEU A 1 192 ? 129.010 142.267 116.594 1.00 24.46 ?  192 LEU A C     1 
ATOM   1575  O  O     . LEU A 1 192 ? 128.476 142.177 115.484 1.00 33.12 ?  192 LEU A O     1 
ATOM   1576  C  CB    . LEU A 1 192 ? 131.247 143.391 116.594 1.00 21.31 ?  192 LEU A CB    1 
ATOM   1577  C  CG    . LEU A 1 192 ? 132.087 144.669 116.656 1.00 20.35 ?  192 LEU A CG    1 
ATOM   1578  C  CD1   . LEU A 1 192 ? 133.565 144.347 116.544 1.00 20.92 ?  192 LEU A CD1   1 
ATOM   1579  C  CD2   . LEU A 1 192 ? 131.667 145.648 115.574 1.00 18.19 ?  192 LEU A CD2   1 
ATOM   1580  N  N     . SER A 1 193 ? 128.950 141.285 117.496 1.00 29.05 ?  193 SER A N     1 
ATOM   1581  C  CA    . SER A 1 193 ? 128.121 140.109 117.260 1.00 26.96 ?  193 SER A CA    1 
ATOM   1582  C  C     . SER A 1 193 ? 126.645 140.479 117.244 1.00 30.56 ?  193 SER A C     1 
ATOM   1583  O  O     . SER A 1 193 ? 125.855 139.878 116.508 1.00 34.58 ?  193 SER A O     1 
ATOM   1584  C  CB    . SER A 1 193 ? 128.403 139.052 118.326 1.00 28.66 ?  193 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 193 ? 127.635 137.884 118.105 1.00 37.95 ?  193 SER A OG    1 
ATOM   1586  N  N     . LYS A 1 194 ? 126.255 141.464 118.057 1.00 33.77 ?  194 LYS A N     1 
ATOM   1587  C  CA    . LYS A 1 194 ? 124.886 141.965 118.024 1.00 31.64 ?  194 LYS A CA    1 
ATOM   1588  C  C     . LYS A 1 194 ? 124.558 142.569 116.665 1.00 36.17 ?  194 LYS A C     1 
ATOM   1589  O  O     . LYS A 1 194 ? 123.439 142.415 116.161 1.00 39.77 ?  194 LYS A O     1 
ATOM   1590  C  CB    . LYS A 1 194 ? 124.693 142.989 119.142 1.00 29.29 ?  194 LYS A CB    1 
ATOM   1591  C  CG    . LYS A 1 194 ? 123.504 143.908 118.971 1.00 33.70 ?  194 LYS A CG    1 
ATOM   1592  C  CD    . LYS A 1 194 ? 123.604 145.099 119.908 1.00 36.36 ?  194 LYS A CD    1 
ATOM   1593  C  CE    . LYS A 1 194 ? 122.281 145.835 120.017 1.00 34.10 ?  194 LYS A CE    1 
ATOM   1594  N  NZ    . LYS A 1 194 ? 122.367 146.984 120.958 1.00 34.07 1  194 LYS A NZ    1 
ATOM   1595  N  N     . LEU A 1 195 ? 125.526 143.252 116.051 1.00 34.21 ?  195 LEU A N     1 
ATOM   1596  C  CA    . LEU A 1 195 ? 125.346 143.791 114.710 1.00 31.80 ?  195 LEU A CA    1 
ATOM   1597  C  C     . LEU A 1 195 ? 125.316 142.709 113.640 1.00 34.40 ?  195 LEU A C     1 
ATOM   1598  O  O     . LEU A 1 195 ? 124.999 143.014 112.486 1.00 38.44 ?  195 LEU A O     1 
ATOM   1599  C  CB    . LEU A 1 195 ? 126.459 144.790 114.394 1.00 33.76 ?  195 LEU A CB    1 
ATOM   1600  C  CG    . LEU A 1 195 ? 126.528 146.022 115.294 1.00 34.19 ?  195 LEU A CG    1 
ATOM   1601  C  CD1   . LEU A 1 195 ? 127.790 146.816 115.006 1.00 30.68 ?  195 LEU A CD1   1 
ATOM   1602  C  CD2   . LEU A 1 195 ? 125.290 146.883 115.116 1.00 36.49 ?  195 LEU A CD2   1 
ATOM   1603  N  N     . GLY A 1 196 ? 125.640 141.468 113.990 1.00 31.78 ?  196 GLY A N     1 
ATOM   1604  C  CA    . GLY A 1 196 ? 125.640 140.372 113.047 1.00 30.65 ?  196 GLY A CA    1 
ATOM   1605  C  C     . GLY A 1 196 ? 126.996 140.006 112.490 1.00 35.94 ?  196 GLY A C     1 
ATOM   1606  O  O     . GLY A 1 196 ? 127.085 139.061 111.698 1.00 40.43 ?  196 GLY A O     1 
ATOM   1607  N  N     . GLY A 1 197 ? 128.049 140.716 112.877 1.00 30.13 ?  197 GLY A N     1 
ATOM   1608  C  CA    . GLY A 1 197 ? 129.367 140.463 112.339 1.00 24.75 ?  197 GLY A CA    1 
ATOM   1609  C  C     . GLY A 1 197 ? 130.113 139.357 113.064 1.00 24.86 ?  197 GLY A C     1 
ATOM   1610  O  O     . GLY A 1 197 ? 129.881 139.087 114.239 1.00 30.82 ?  197 GLY A O     1 
ATOM   1611  N  N     . GLY A 1 198 ? 131.019 138.712 112.333 1.00 20.05 ?  198 GLY A N     1 
ATOM   1612  C  CA    . GLY A 1 198 ? 131.932 137.752 112.921 1.00 17.92 ?  198 GLY A CA    1 
ATOM   1613  C  C     . GLY A 1 198 ? 133.164 138.469 113.432 1.00 16.53 ?  198 GLY A C     1 
ATOM   1614  O  O     . GLY A 1 198 ? 133.740 139.307 112.733 1.00 22.13 ?  198 GLY A O     1 
ATOM   1615  N  N     . VAL A 1 199 ? 133.567 138.140 114.654 1.00 20.68 ?  199 VAL A N     1 
ATOM   1616  C  CA    . VAL A 1 199 ? 134.629 138.852 115.351 1.00 16.18 ?  199 VAL A CA    1 
ATOM   1617  C  C     . VAL A 1 199 ? 135.804 137.910 115.558 1.00 11.98 ?  199 VAL A C     1 
ATOM   1618  O  O     . VAL A 1 199 ? 135.632 136.795 116.062 1.00 15.18 ?  199 VAL A O     1 
ATOM   1619  C  CB    . VAL A 1 199 ? 134.143 139.417 116.698 1.00 14.84 ?  199 VAL A CB    1 
ATOM   1620  C  CG1   . VAL A 1 199 ? 135.206 140.304 117.313 1.00 14.75 ?  199 VAL A CG1   1 
ATOM   1621  C  CG2   . VAL A 1 199 ? 132.848 140.181 116.512 1.00 18.84 ?  199 VAL A CG2   1 
ATOM   1622  N  N     . SER A 1 200 ? 136.991 138.358 115.170 1.00 16.69 ?  200 SER A N     1 
ATOM   1623  C  CA    . SER A 1 200 ? 138.230 137.648 115.436 1.00 7.23  ?  200 SER A CA    1 
ATOM   1624  C  C     . SER A 1 200 ? 139.057 138.449 116.430 1.00 12.61 ?  200 SER A C     1 
ATOM   1625  O  O     . SER A 1 200 ? 139.119 139.679 116.351 1.00 19.88 ?  200 SER A O     1 
ATOM   1626  C  CB    . SER A 1 200 ? 139.027 137.423 114.152 1.00 14.12 ?  200 SER A CB    1 
ATOM   1627  O  OG    . SER A 1 200 ? 139.959 136.372 114.310 1.00 19.62 ?  200 SER A OG    1 
ATOM   1628  N  N     . LEU A 1 201 ? 139.686 137.751 117.368 1.00 18.50 ?  201 LEU A N     1 
ATOM   1629  C  CA    . LEU A 1 201 ? 140.468 138.389 118.413 1.00 10.78 ?  201 LEU A CA    1 
ATOM   1630  C  C     . LEU A 1 201 ? 141.865 137.793 118.454 1.00 10.09 ?  201 LEU A C     1 
ATOM   1631  O  O     . LEU A 1 201 ? 142.034 136.574 118.373 1.00 15.23 ?  201 LEU A O     1 
ATOM   1632  C  CB    . LEU A 1 201 ? 139.797 138.239 119.783 1.00 14.87 ?  201 LEU A CB    1 
ATOM   1633  C  CG    . LEU A 1 201 ? 138.400 138.850 119.914 1.00 15.59 ?  201 LEU A CG    1 
ATOM   1634  C  CD1   . LEU A 1 201 ? 137.340 137.762 119.955 1.00 20.18 ?  201 LEU A CD1   1 
ATOM   1635  C  CD2   . LEU A 1 201 ? 138.314 139.735 121.141 1.00 12.72 ?  201 LEU A CD2   1 
ATOM   1636  N  N     . ASN A 1 202 ? 142.864 138.663 118.576 1.00 10.92 ?  202 ASN A N     1 
ATOM   1637  C  CA    . ASN A 1 202 ? 144.240 138.243 118.787 1.00 8.56  ?  202 ASN A CA    1 
ATOM   1638  C  C     . ASN A 1 202 ? 144.488 138.122 120.284 1.00 18.53 ?  202 ASN A C     1 
ATOM   1639  O  O     . ASN A 1 202 ? 144.326 139.096 121.026 1.00 29.15 ?  202 ASN A O     1 
ATOM   1640  C  CB    . ASN A 1 202 ? 145.215 139.235 118.159 1.00 9.92  ?  202 ASN A CB    1 
ATOM   1641  C  CG    . ASN A 1 202 ? 146.603 138.657 117.986 1.00 12.50 ?  202 ASN A CG    1 
ATOM   1642  O  OD1   . ASN A 1 202 ? 146.770 137.447 117.849 1.00 17.38 ?  202 ASN A OD1   1 
ATOM   1643  N  ND2   . ASN A 1 202 ? 147.607 139.522 117.991 1.00 10.64 ?  202 ASN A ND2   1 
ATOM   1644  N  N     . LEU A 1 203 ? 144.881 136.929 120.729 1.00 13.46 ?  203 LEU A N     1 
ATOM   1645  C  CA    . LEU A 1 203 ? 145.128 136.666 122.139 1.00 11.52 ?  203 LEU A CA    1 
ATOM   1646  C  C     . LEU A 1 203 ? 146.612 136.494 122.441 1.00 13.48 ?  203 LEU A C     1 
ATOM   1647  O  O     . LEU A 1 203 ? 146.970 136.003 123.515 1.00 21.45 ?  203 LEU A O     1 
ATOM   1648  C  CB    . LEU A 1 203 ? 144.345 135.433 122.589 1.00 17.29 ?  203 LEU A CB    1 
ATOM   1649  C  CG    . LEU A 1 203 ? 142.824 135.491 122.438 1.00 16.61 ?  203 LEU A CG    1 
ATOM   1650  C  CD1   . LEU A 1 203 ? 142.171 134.402 123.265 1.00 17.98 ?  203 LEU A CD1   1 
ATOM   1651  C  CD2   . LEU A 1 203 ? 142.281 136.856 122.833 1.00 13.98 ?  203 LEU A CD2   1 
ATOM   1652  N  N     . SER A 1 204 ? 147.483 136.896 121.516 1.00 12.80 ?  204 SER A N     1 
ATOM   1653  C  CA    . SER A 1 204 ? 148.914 136.689 121.695 1.00 15.21 ?  204 SER A CA    1 
ATOM   1654  C  C     . SER A 1 204 ? 149.521 137.663 122.696 1.00 20.30 ?  204 SER A C     1 
ATOM   1655  O  O     . SER A 1 204 ? 150.462 137.301 123.410 1.00 27.24 ?  204 SER A O     1 
ATOM   1656  C  CB    . SER A 1 204 ? 149.631 136.804 120.353 1.00 15.24 ?  204 SER A CB    1 
ATOM   1657  O  OG    . SER A 1 204 ? 149.055 135.936 119.396 1.00 22.85 ?  204 SER A OG    1 
ATOM   1658  N  N     . LYS A 1 205 ? 149.012 138.896 122.760 1.00 19.51 ?  205 LYS A N     1 
ATOM   1659  C  CA    . LYS A 1 205 ? 149.542 139.862 123.715 1.00 16.00 ?  205 LYS A CA    1 
ATOM   1660  C  C     . LYS A 1 205 ? 149.175 139.519 125.149 1.00 18.09 ?  205 LYS A C     1 
ATOM   1661  O  O     . LYS A 1 205 ? 149.836 139.999 126.074 1.00 22.70 ?  205 LYS A O     1 
ATOM   1662  C  CB    . LYS A 1 205 ? 149.053 141.269 123.377 1.00 16.09 ?  205 LYS A CB    1 
ATOM   1663  C  CG    . LYS A 1 205 ? 149.658 141.839 122.116 1.00 18.07 ?  205 LYS A CG    1 
ATOM   1664  C  CD    . LYS A 1 205 ? 149.173 143.249 121.857 1.00 23.59 ?  205 LYS A CD    1 
ATOM   1665  C  CE    . LYS A 1 205 ? 149.930 143.883 120.706 1.00 26.62 ?  205 LYS A CE    1 
ATOM   1666  N  NZ    . LYS A 1 205 ? 149.744 143.132 119.437 1.00 19.06 1  205 LYS A NZ    1 
ATOM   1667  N  N     . LEU A 1 206 ? 148.143 138.705 125.352 1.00 17.87 ?  206 LEU A N     1 
ATOM   1668  C  CA    . LEU A 1 206 ? 147.761 138.294 126.694 1.00 12.12 ?  206 LEU A CA    1 
ATOM   1669  C  C     . LEU A 1 206 ? 148.832 137.392 127.290 1.00 17.25 ?  206 LEU A C     1 
ATOM   1670  O  O     . LEU A 1 206 ? 149.337 136.485 126.622 1.00 21.62 ?  206 LEU A O     1 
ATOM   1671  C  CB    . LEU A 1 206 ? 146.419 137.568 126.659 1.00 19.76 ?  206 LEU A CB    1 
ATOM   1672  C  CG    . LEU A 1 206 ? 145.222 138.406 126.218 1.00 20.73 ?  206 LEU A CG    1 
ATOM   1673  C  CD1   . LEU A 1 206 ? 143.965 137.561 126.221 1.00 16.80 ?  206 LEU A CD1   1 
ATOM   1674  C  CD2   . LEU A 1 206 ? 145.063 139.616 127.117 1.00 23.23 ?  206 LEU A CD2   1 
ATOM   1675  N  N     . ARG A 1 207 ? 149.176 137.637 128.550 1.00 24.80 ?  207 ARG A N     1 
ATOM   1676  C  CA    . ARG A 1 207 ? 150.206 136.842 129.199 1.00 22.16 ?  207 ARG A CA    1 
ATOM   1677  C  C     . ARG A 1 207 ? 149.690 135.440 129.501 1.00 27.34 ?  207 ARG A C     1 
ATOM   1678  O  O     . ARG A 1 207 ? 148.490 135.214 129.674 1.00 27.88 ?  207 ARG A O     1 
ATOM   1679  C  CB    . ARG A 1 207 ? 150.693 137.525 130.474 1.00 22.25 ?  207 ARG A CB    1 
ATOM   1680  C  CG    . ARG A 1 207 ? 149.680 137.620 131.590 1.00 23.35 ?  207 ARG A CG    1 
ATOM   1681  C  CD    . ARG A 1 207 ? 150.209 138.510 132.697 1.00 26.39 ?  207 ARG A CD    1 
ATOM   1682  N  NE    . ARG A 1 207 ? 150.263 139.907 132.287 1.00 28.94 ?  207 ARG A NE    1 
ATOM   1683  C  CZ    . ARG A 1 207 ? 150.280 140.934 133.124 1.00 24.31 ?  207 ARG A CZ    1 
ATOM   1684  N  NH1   . ARG A 1 207 ? 150.274 140.758 134.434 1.00 28.75 1  207 ARG A NH1   1 
ATOM   1685  N  NH2   . ARG A 1 207 ? 150.299 142.170 132.635 1.00 20.66 ?  207 ARG A NH2   1 
ATOM   1686  N  N     . ALA A 1 208 ? 150.620 134.493 129.559 1.00 33.04 ?  208 ALA A N     1 
ATOM   1687  C  CA    . ALA A 1 208 ? 150.286 133.084 129.632 1.00 24.77 ?  208 ALA A CA    1 
ATOM   1688  C  C     . ALA A 1 208 ? 149.827 132.696 131.036 1.00 31.73 ?  208 ALA A C     1 
ATOM   1689  O  O     . ALA A 1 208 ? 149.838 133.497 131.974 1.00 36.14 ?  208 ALA A O     1 
ATOM   1690  C  CB    . ALA A 1 208 ? 151.483 132.237 129.210 1.00 25.67 ?  208 ALA A CB    1 
ATOM   1691  N  N     . LYS A 1 209 ? 149.403 131.442 131.166 1.00 32.25 ?  209 LYS A N     1 
ATOM   1692  C  CA    . LYS A 1 209 ? 148.987 130.916 132.457 1.00 29.35 ?  209 LYS A CA    1 
ATOM   1693  C  C     . LYS A 1 209 ? 150.182 130.799 133.394 1.00 33.86 ?  209 LYS A C     1 
ATOM   1694  O  O     . LYS A 1 209 ? 151.259 130.344 133.000 1.00 34.76 ?  209 LYS A O     1 
ATOM   1695  C  CB    . LYS A 1 209 ? 148.319 129.553 132.281 1.00 29.71 ?  209 LYS A CB    1 
ATOM   1696  C  CG    . LYS A 1 209 ? 147.378 129.168 133.406 1.00 32.21 ?  209 LYS A CG    1 
ATOM   1697  C  CD    . LYS A 1 209 ? 147.052 127.684 133.366 1.00 31.43 ?  209 LYS A CD    1 
ATOM   1698  C  CE    . LYS A 1 209 ? 148.289 126.851 133.073 1.00 35.68 ?  209 LYS A CE    1 
ATOM   1699  N  NZ    . LYS A 1 209 ? 147.938 125.469 132.641 1.00 36.68 1  209 LYS A NZ    1 
ATOM   1700  N  N     . GLY A 1 210 ? 149.983 131.210 134.643 1.00 35.89 ?  210 GLY A N     1 
ATOM   1701  C  CA    . GLY A 1 210 ? 151.056 131.176 135.614 1.00 34.31 ?  210 GLY A CA    1 
ATOM   1702  C  C     . GLY A 1 210 ? 151.956 132.387 135.617 1.00 36.82 ?  210 GLY A C     1 
ATOM   1703  O  O     . GLY A 1 210 ? 153.074 132.312 136.134 1.00 38.71 ?  210 GLY A O     1 
ATOM   1704  N  N     . GLU A 1 211 ? 151.511 133.500 135.048 1.00 37.12 ?  211 GLU A N     1 
ATOM   1705  C  CA    . GLU A 1 211 ? 152.258 134.747 135.086 1.00 33.53 ?  211 GLU A CA    1 
ATOM   1706  C  C     . GLU A 1 211 ? 151.736 135.637 136.207 1.00 36.61 ?  211 GLU A C     1 
ATOM   1707  O  O     . GLU A 1 211 ? 150.619 135.467 136.701 1.00 37.11 ?  211 GLU A O     1 
ATOM   1708  C  CB    . GLU A 1 211 ? 152.173 135.476 133.744 1.00 32.02 ?  211 GLU A CB    1 
ATOM   1709  C  CG    . GLU A 1 211 ? 152.719 134.673 132.583 1.00 32.88 ?  211 GLU A CG    1 
ATOM   1710  C  CD    . GLU A 1 211 ? 153.680 135.468 131.728 1.00 37.46 ?  211 GLU A CD    1 
ATOM   1711  O  OE1   . GLU A 1 211 ? 154.793 135.765 132.209 1.00 41.10 ?  211 GLU A OE1   1 
ATOM   1712  O  OE2   . GLU A 1 211 ? 153.332 135.784 130.572 1.00 30.94 -1 211 GLU A OE2   1 
ATOM   1713  N  N     . ALA A 1 212 ? 152.565 136.595 136.605 1.00 34.70 ?  212 ALA A N     1 
ATOM   1714  C  CA    . ALA A 1 212 ? 152.245 137.454 137.735 1.00 31.46 ?  212 ALA A CA    1 
ATOM   1715  C  C     . ALA A 1 212 ? 151.297 138.573 137.327 1.00 36.01 ?  212 ALA A C     1 
ATOM   1716  O  O     . ALA A 1 212 ? 151.375 139.103 136.216 1.00 39.23 ?  212 ALA A O     1 
ATOM   1717  C  CB    . ALA A 1 212 ? 153.521 138.046 138.331 1.00 35.89 ?  212 ALA A CB    1 
ATOM   1718  N  N     . ILE A 1 213 ? 150.396 138.926 138.237 1.00 34.91 ?  213 ILE A N     1 
ATOM   1719  C  CA    . ILE A 1 213 ? 149.541 140.103 138.097 1.00 33.44 ?  213 ILE A CA    1 
ATOM   1720  C  C     . ILE A 1 213 ? 149.904 141.030 139.250 1.00 35.43 ?  213 ILE A C     1 
ATOM   1721  O  O     . ILE A 1 213 ? 149.358 140.915 140.350 1.00 40.52 ?  213 ILE A O     1 
ATOM   1722  C  CB    . ILE A 1 213 ? 148.051 139.759 138.110 1.00 35.77 ?  213 ILE A CB    1 
ATOM   1723  C  CG1   . ILE A 1 213 ? 147.756 138.572 137.196 1.00 37.06 ?  213 ILE A CG1   1 
ATOM   1724  C  CG2   . ILE A 1 213 ? 147.226 140.964 137.697 1.00 32.96 ?  213 ILE A CG2   1 
ATOM   1725  C  CD1   . ILE A 1 213 ? 146.410 137.941 137.455 1.00 30.23 ?  213 ILE A CD1   1 
ATOM   1726  N  N     . LYS A 1 214 ? 150.815 141.971 138.999 1.00 41.20 ?  214 LYS A N     1 
ATOM   1727  C  CA    . LYS A 1 214 ? 151.301 142.906 140.013 1.00 40.66 ?  214 LYS A CA    1 
ATOM   1728  C  C     . LYS A 1 214 ? 151.944 142.153 141.183 1.00 44.42 ?  214 LYS A C     1 
ATOM   1729  O  O     . LYS A 1 214 ? 151.431 142.108 142.302 1.00 46.37 ?  214 LYS A O     1 
ATOM   1730  C  CB    . LYS A 1 214 ? 150.177 143.834 140.491 1.00 39.51 ?  214 LYS A CB    1 
ATOM   1731  C  CG    . LYS A 1 214 ? 150.353 145.282 140.070 1.00 42.74 ?  214 LYS A CG    1 
ATOM   1732  C  CD    . LYS A 1 214 ? 149.199 146.144 140.551 1.00 42.94 ?  214 LYS A CD    1 
ATOM   1733  C  CE    . LYS A 1 214 ? 149.132 147.446 139.771 1.00 45.18 ?  214 LYS A CE    1 
ATOM   1734  N  NZ    . LYS A 1 214 ? 147.769 148.045 139.798 1.00 43.21 1  214 LYS A NZ    1 
ATOM   1735  N  N     . ASP A 1 215 ? 153.063 141.509 140.853 1.00 45.21 ?  215 ASP A N     1 
ATOM   1736  C  CA    . ASP A 1 215 ? 154.028 140.897 141.767 1.00 50.42 ?  215 ASP A CA    1 
ATOM   1737  C  C     . ASP A 1 215 ? 153.455 139.758 142.609 1.00 50.21 ?  215 ASP A C     1 
ATOM   1738  O  O     . ASP A 1 215 ? 154.098 139.331 143.575 1.00 52.51 ?  215 ASP A O     1 
ATOM   1739  C  CB    . ASP A 1 215 ? 154.708 141.946 142.672 1.00 49.52 ?  215 ASP A CB    1 
ATOM   1740  C  CG    . ASP A 1 215 ? 153.807 142.467 143.782 1.00 52.69 ?  215 ASP A CG    1 
ATOM   1741  O  OD1   . ASP A 1 215 ? 153.534 141.729 144.750 1.00 51.32 ?  215 ASP A OD1   1 
ATOM   1742  O  OD2   . ASP A 1 215 ? 153.373 143.635 143.686 1.00 51.14 -1 215 ASP A OD2   1 
ATOM   1743  N  N     . VAL A 1 216 ? 152.282 139.231 142.271 1.00 43.00 ?  216 VAL A N     1 
ATOM   1744  C  CA    . VAL A 1 216 ? 151.811 137.968 142.831 1.00 45.82 ?  216 VAL A CA    1 
ATOM   1745  C  C     . VAL A 1 216 ? 151.844 136.926 141.719 1.00 47.78 ?  216 VAL A C     1 
ATOM   1746  O  O     . VAL A 1 216 ? 151.173 137.076 140.691 1.00 50.41 ?  216 VAL A O     1 
ATOM   1747  C  CB    . VAL A 1 216 ? 150.413 138.098 143.461 1.00 45.53 ?  216 VAL A CB    1 
ATOM   1748  C  CG1   . VAL A 1 216 ? 149.445 138.778 142.527 1.00 44.93 ?  216 VAL A CG1   1 
ATOM   1749  C  CG2   . VAL A 1 216 ? 149.885 136.729 143.854 1.00 45.66 ?  216 VAL A CG2   1 
ATOM   1750  N  N     . GLU A 1 217 ? 152.630 135.877 141.922 1.00 48.05 ?  217 GLU A N     1 
ATOM   1751  C  CA    . GLU A 1 217 ? 152.986 134.950 140.861 1.00 46.87 ?  217 GLU A CA    1 
ATOM   1752  C  C     . GLU A 1 217 ? 151.942 133.850 140.703 1.00 48.29 ?  217 GLU A C     1 
ATOM   1753  O  O     . GLU A 1 217 ? 151.128 133.595 141.594 1.00 49.42 ?  217 GLU A O     1 
ATOM   1754  C  CB    . GLU A 1 217 ? 154.358 134.335 141.138 1.00 48.30 ?  217 GLU A CB    1 
ATOM   1755  C  CG    . GLU A 1 217 ? 155.359 135.323 141.714 1.00 49.23 ?  217 GLU A CG    1 
ATOM   1756  C  CD    . GLU A 1 217 ? 156.246 135.939 140.652 1.00 51.51 ?  217 GLU A CD    1 
ATOM   1757  O  OE1   . GLU A 1 217 ? 156.743 135.191 139.784 1.00 53.39 ?  217 GLU A OE1   1 
ATOM   1758  O  OE2   . GLU A 1 217 ? 156.441 137.172 140.681 1.00 49.38 -1 217 GLU A OE2   1 
ATOM   1759  N  N     . ASN A 1 218 ? 151.985 133.193 139.540 1.00 45.48 ?  218 ASN A N     1 
ATOM   1760  C  CA    . ASN A 1 218 ? 151.060 132.113 139.197 1.00 43.90 ?  218 ASN A CA    1 
ATOM   1761  C  C     . ASN A 1 218 ? 149.611 132.564 139.350 1.00 47.78 ?  218 ASN A C     1 
ATOM   1762  O  O     . ASN A 1 218 ? 148.741 131.811 139.793 1.00 49.11 ?  218 ASN A O     1 
ATOM   1763  C  CB    . ASN A 1 218 ? 151.338 130.863 140.033 1.00 45.70 ?  218 ASN A CB    1 
ATOM   1764  C  CG    . ASN A 1 218 ? 152.515 130.067 139.510 1.00 48.95 ?  218 ASN A CG    1 
ATOM   1765  O  OD1   . ASN A 1 218 ? 152.357 129.198 138.653 1.00 48.93 ?  218 ASN A OD1   1 
ATOM   1766  N  ND2   . ASN A 1 218 ? 153.704 130.365 140.019 1.00 46.74 ?  218 ASN A ND2   1 
ATOM   1767  N  N     . ALA A 1 219 ? 149.349 133.813 138.973 1.00 40.88 ?  219 ALA A N     1 
ATOM   1768  C  CA    . ALA A 1 219 ? 148.046 134.426 139.175 1.00 38.59 ?  219 ALA A CA    1 
ATOM   1769  C  C     . ALA A 1 219 ? 147.201 134.485 137.913 1.00 40.39 ?  219 ALA A C     1 
ATOM   1770  O  O     . ALA A 1 219 ? 145.971 134.437 138.003 1.00 41.10 ?  219 ALA A O     1 
ATOM   1771  C  CB    . ALA A 1 219 ? 148.219 135.842 139.731 1.00 37.28 ?  219 ALA A CB    1 
ATOM   1772  N  N     . THR A 1 220 ? 147.828 134.580 136.745 1.00 37.47 ?  220 THR A N     1 
ATOM   1773  C  CA    . THR A 1 220 ? 147.092 134.728 135.499 1.00 34.68 ?  220 THR A CA    1 
ATOM   1774  C  C     . THR A 1 220 ? 146.531 133.382 135.058 1.00 35.72 ?  220 THR A C     1 
ATOM   1775  O  O     . THR A 1 220 ? 147.212 132.355 135.127 1.00 37.02 ?  220 THR A O     1 
ATOM   1776  C  CB    . THR A 1 220 ? 148.003 135.313 134.418 1.00 33.58 ?  220 THR A CB    1 
ATOM   1777  O  OG1   . THR A 1 220 ? 148.264 136.690 134.710 1.00 36.06 ?  220 THR A OG1   1 
ATOM   1778  C  CG2   . THR A 1 220 ? 147.342 135.239 133.059 1.00 35.48 ?  220 THR A CG2   1 
ATOM   1779  N  N     . LYS A 1 221 ? 145.276 133.390 134.608 1.00 37.24 ?  221 LYS A N     1 
ATOM   1780  C  CA    . LYS A 1 221 ? 144.615 132.179 134.138 1.00 32.88 ?  221 LYS A CA    1 
ATOM   1781  C  C     . LYS A 1 221 ? 144.974 131.827 132.702 1.00 38.04 ?  221 LYS A C     1 
ATOM   1782  O  O     . LYS A 1 221 ? 144.518 130.792 132.203 1.00 43.49 ?  221 LYS A O     1 
ATOM   1783  C  CB    . LYS A 1 221 ? 143.097 132.322 134.259 1.00 33.02 ?  221 LYS A CB    1 
ATOM   1784  C  CG    . LYS A 1 221 ? 142.629 132.953 135.552 1.00 37.07 ?  221 LYS A CG    1 
ATOM   1785  C  CD    . LYS A 1 221 ? 141.132 132.789 135.722 1.00 36.66 ?  221 LYS A CD    1 
ATOM   1786  C  CE    . LYS A 1 221 ? 140.773 131.400 136.214 1.00 35.69 ?  221 LYS A CE    1 
ATOM   1787  N  NZ    . LYS A 1 221 ? 141.567 131.014 137.410 1.00 37.36 1  221 LYS A NZ    1 
ATOM   1788  N  N     . GLY A 1 222 ? 145.766 132.652 132.033 1.00 32.91 ?  222 GLY A N     1 
ATOM   1789  C  CA    . GLY A 1 222 ? 146.158 132.387 130.670 1.00 30.90 ?  222 GLY A CA    1 
ATOM   1790  C  C     . GLY A 1 222 ? 145.123 132.848 129.664 1.00 30.75 ?  222 GLY A C     1 
ATOM   1791  O  O     . GLY A 1 222 ? 144.134 133.511 129.987 1.00 31.07 ?  222 GLY A O     1 
ATOM   1792  N  N     . VAL A 1 223 ? 145.369 132.479 128.407 1.00 31.96 ?  223 VAL A N     1 
ATOM   1793  C  CA    . VAL A 1 223 ? 144.453 132.859 127.339 1.00 26.30 ?  223 VAL A CA    1 
ATOM   1794  C  C     . VAL A 1 223 ? 143.191 132.011 127.333 1.00 22.89 ?  223 VAL A C     1 
ATOM   1795  O  O     . VAL A 1 223 ? 142.208 132.394 126.695 1.00 31.06 ?  223 VAL A O     1 
ATOM   1796  C  CB    . VAL A 1 223 ? 145.135 132.780 125.961 1.00 25.90 ?  223 VAL A CB    1 
ATOM   1797  C  CG1   . VAL A 1 223 ? 146.470 133.500 125.986 1.00 25.11 ?  223 VAL A CG1   1 
ATOM   1798  C  CG2   . VAL A 1 223 ? 145.304 131.335 125.524 1.00 26.84 ?  223 VAL A CG2   1 
ATOM   1799  N  N     . VAL A 1 224 ? 143.186 130.870 128.024 1.00 25.50 ?  224 VAL A N     1 
ATOM   1800  C  CA    . VAL A 1 224 ? 142.008 130.008 128.016 1.00 25.72 ?  224 VAL A CA    1 
ATOM   1801  C  C     . VAL A 1 224 ? 140.874 130.601 128.849 1.00 27.40 ?  224 VAL A C     1 
ATOM   1802  O  O     . VAL A 1 224 ? 139.698 130.421 128.517 1.00 30.19 ?  224 VAL A O     1 
ATOM   1803  C  CB    . VAL A 1 224 ? 142.387 128.594 128.487 1.00 32.71 ?  224 VAL A CB    1 
ATOM   1804  C  CG1   . VAL A 1 224 ? 141.171 127.686 128.499 1.00 31.81 ?  224 VAL A CG1   1 
ATOM   1805  C  CG2   . VAL A 1 224 ? 143.462 128.019 127.583 1.00 29.46 ?  224 VAL A CG2   1 
ATOM   1806  N  N     . GLY A 1 225 ? 141.190 131.317 129.929 1.00 24.18 ?  225 GLY A N     1 
ATOM   1807  C  CA    . GLY A 1 225 ? 140.145 132.005 130.670 1.00 21.73 ?  225 GLY A CA    1 
ATOM   1808  C  C     . GLY A 1 225 ? 139.482 133.099 129.854 1.00 22.30 ?  225 GLY A C     1 
ATOM   1809  O  O     . GLY A 1 225 ? 138.252 133.232 129.852 1.00 31.46 ?  225 GLY A O     1 
ATOM   1810  N  N     . VAL A 1 226 ? 140.285 133.889 129.140 1.00 19.34 ?  226 VAL A N     1 
ATOM   1811  C  CA    . VAL A 1 226 ? 139.737 134.880 128.222 1.00 20.35 ?  226 VAL A CA    1 
ATOM   1812  C  C     . VAL A 1 226 ? 138.968 134.198 127.105 1.00 24.85 ?  226 VAL A C     1 
ATOM   1813  O  O     . VAL A 1 226 ? 137.970 134.730 126.611 1.00 26.82 ?  226 VAL A O     1 
ATOM   1814  C  CB    . VAL A 1 226 ? 140.866 135.772 127.673 1.00 18.19 ?  226 VAL A CB    1 
ATOM   1815  C  CG1   . VAL A 1 226 ? 140.291 136.923 126.859 1.00 25.76 ?  226 VAL A CG1   1 
ATOM   1816  C  CG2   . VAL A 1 226 ? 141.723 136.287 128.808 1.00 20.82 ?  226 VAL A CG2   1 
ATOM   1817  N  N     . MET A 1 227 ? 139.418 133.015 126.687 1.00 28.39 ?  227 MET A N     1 
ATOM   1818  C  CA    . MET A 1 227 ? 138.707 132.255 125.667 1.00 22.22 ?  227 MET A CA    1 
ATOM   1819  C  C     . MET A 1 227 ? 137.323 131.849 126.148 1.00 22.95 ?  227 MET A C     1 
ATOM   1820  O  O     . MET A 1 227 ? 136.350 131.929 125.396 1.00 29.97 ?  227 MET A O     1 
ATOM   1821  C  CB    . MET A 1 227 ? 139.528 131.025 125.286 1.00 19.68 ?  227 MET A CB    1 
ATOM   1822  C  CG    . MET A 1 227 ? 140.597 131.287 124.248 1.00 17.85 ?  227 MET A CG    1 
ATOM   1823  S  SD    . MET A 1 227 ? 141.270 129.766 123.567 1.00 33.28 ?  227 MET A SD    1 
ATOM   1824  C  CE    . MET A 1 227 ? 139.971 129.312 122.434 1.00 29.81 ?  227 MET A CE    1 
ATOM   1825  N  N     . LYS A 1 228 ? 137.218 131.401 127.401 1.00 26.79 ?  228 LYS A N     1 
ATOM   1826  C  CA    . LYS A 1 228 ? 135.914 131.062 127.965 1.00 23.10 ?  228 LYS A CA    1 
ATOM   1827  C  C     . LYS A 1 228 ? 135.028 132.295 128.087 1.00 24.38 ?  228 LYS A C     1 
ATOM   1828  O  O     . LYS A 1 228 ? 133.825 132.240 127.788 1.00 26.05 ?  228 LYS A O     1 
ATOM   1829  C  CB    . LYS A 1 228 ? 136.086 130.394 129.329 1.00 23.32 ?  228 LYS A CB    1 
ATOM   1830  C  CG    . LYS A 1 228 ? 136.863 129.093 129.290 1.00 29.04 ?  228 LYS A CG    1 
ATOM   1831  C  CD    . LYS A 1 228 ? 136.923 128.447 130.662 1.00 36.78 ?  228 LYS A CD    1 
ATOM   1832  C  CE    . LYS A 1 228 ? 138.053 129.023 131.500 1.00 36.15 ?  228 LYS A CE    1 
ATOM   1833  N  NZ    . LYS A 1 228 ? 139.209 128.090 131.592 1.00 30.76 1  228 LYS A NZ    1 
ATOM   1834  N  N     . LEU A 1 229 ? 135.607 133.415 128.527 1.00 24.46 ?  229 LEU A N     1 
ATOM   1835  C  CA    . LEU A 1 229 ? 134.856 134.666 128.590 1.00 21.84 ?  229 LEU A CA    1 
ATOM   1836  C  C     . LEU A 1 229 ? 134.302 135.041 127.222 1.00 21.51 ?  229 LEU A C     1 
ATOM   1837  O  O     . LEU A 1 229 ? 133.123 135.387 127.088 1.00 22.24 ?  229 LEU A O     1 
ATOM   1838  C  CB    . LEU A 1 229 ? 135.748 135.786 129.121 1.00 24.43 ?  229 LEU A CB    1 
ATOM   1839  C  CG    . LEU A 1 229 ? 136.124 135.817 130.599 1.00 23.02 ?  229 LEU A CG    1 
ATOM   1840  C  CD1   . LEU A 1 229 ? 137.267 136.789 130.793 1.00 24.40 ?  229 LEU A CD1   1 
ATOM   1841  C  CD2   . LEU A 1 229 ? 134.935 136.210 131.453 1.00 18.49 ?  229 LEU A CD2   1 
ATOM   1842  N  N     . LEU A 1 230 ? 135.144 134.972 126.191 1.00 26.92 ?  230 LEU A N     1 
ATOM   1843  C  CA    . LEU A 1 230 ? 134.720 135.329 124.842 1.00 18.66 ?  230 LEU A CA    1 
ATOM   1844  C  C     . LEU A 1 230 ? 133.695 134.342 124.303 1.00 17.88 ?  230 LEU A C     1 
ATOM   1845  O  O     . LEU A 1 230 ? 132.761 134.734 123.596 1.00 29.69 ?  230 LEU A O     1 
ATOM   1846  C  CB    . LEU A 1 230 ? 135.931 135.402 123.915 1.00 20.57 ?  230 LEU A CB    1 
ATOM   1847  C  CG    . LEU A 1 230 ? 136.842 136.613 124.105 1.00 27.78 ?  230 LEU A CG    1 
ATOM   1848  C  CD1   . LEU A 1 230 ? 138.183 136.380 123.430 1.00 28.12 ?  230 LEU A CD1   1 
ATOM   1849  C  CD2   . LEU A 1 230 ? 136.173 137.869 123.573 1.00 21.05 ?  230 LEU A CD2   1 
ATOM   1850  N  N     . ASP A 1 231 ? 133.856 133.057 124.616 1.00 20.37 ?  231 ASP A N     1 
ATOM   1851  C  CA    . ASP A 1 231 ? 132.899 132.058 124.163 1.00 24.19 ?  231 ASP A CA    1 
ATOM   1852  C  C     . ASP A 1 231 ? 131.519 132.319 124.749 1.00 28.73 ?  231 ASP A C     1 
ATOM   1853  O  O     . ASP A 1 231 ? 130.510 132.249 124.038 1.00 33.36 ?  231 ASP A O     1 
ATOM   1854  C  CB    . ASP A 1 231 ? 133.395 130.661 124.534 1.00 27.44 ?  231 ASP A CB    1 
ATOM   1855  C  CG    . ASP A 1 231 ? 132.446 129.569 124.095 1.00 35.91 ?  231 ASP A CG    1 
ATOM   1856  O  OD1   . ASP A 1 231 ? 132.303 129.360 122.873 1.00 39.62 ?  231 ASP A OD1   1 
ATOM   1857  O  OD2   . ASP A 1 231 ? 131.844 128.916 124.971 1.00 38.47 -1 231 ASP A OD2   1 
ATOM   1858  N  N     . ASN A 1 232 ? 131.452 132.648 126.041 1.00 29.49 ?  232 ASN A N     1 
ATOM   1859  C  CA    . ASN A 1 232 ? 130.155 132.974 126.626 1.00 27.94 ?  232 ASN A CA    1 
ATOM   1860  C  C     . ASN A 1 232 ? 129.624 134.313 126.132 1.00 28.52 ?  232 ASN A C     1 
ATOM   1861  O  O     . ASN A 1 232 ? 128.406 134.483 126.010 1.00 33.99 ?  232 ASN A O     1 
ATOM   1862  C  CB    . ASN A 1 232 ? 130.234 132.957 128.148 1.00 29.32 ?  232 ASN A CB    1 
ATOM   1863  C  CG    . ASN A 1 232 ? 130.081 131.568 128.710 1.00 36.30 ?  232 ASN A CG    1 
ATOM   1864  O  OD1   . ASN A 1 232 ? 130.969 130.727 128.572 1.00 38.87 ?  232 ASN A OD1   1 
ATOM   1865  N  ND2   . ASN A 1 232 ? 128.942 131.311 129.342 1.00 33.39 ?  232 ASN A ND2   1 
ATOM   1866  N  N     . ALA A 1 233 ? 130.509 135.267 125.840 1.00 25.87 ?  233 ALA A N     1 
ATOM   1867  C  CA    . ALA A 1 233 ? 130.061 136.534 125.274 1.00 17.88 ?  233 ALA A CA    1 
ATOM   1868  C  C     . ALA A 1 233 ? 129.441 136.332 123.898 1.00 30.07 ?  233 ALA A C     1 
ATOM   1869  O  O     . ALA A 1 233 ? 128.455 136.990 123.549 1.00 36.37 ?  233 ALA A O     1 
ATOM   1870  C  CB    . ALA A 1 233 ? 131.229 137.516 125.200 1.00 23.66 ?  233 ALA A CB    1 
ATOM   1871  N  N     . PHE A 1 234 ? 130.010 135.427 123.101 1.00 32.09 ?  234 PHE A N     1 
ATOM   1872  C  CA    . PHE A 1 234 ? 129.461 135.138 121.783 1.00 25.48 ?  234 PHE A CA    1 
ATOM   1873  C  C     . PHE A 1 234 ? 128.207 134.279 121.863 1.00 23.30 ?  234 PHE A C     1 
ATOM   1874  O  O     . PHE A 1 234 ? 127.317 134.412 121.018 1.00 29.86 ?  234 PHE A O     1 
ATOM   1875  C  CB    . PHE A 1 234 ? 130.521 134.465 120.912 1.00 24.96 ?  234 PHE A CB    1 
ATOM   1876  C  CG    . PHE A 1 234 ? 131.544 135.419 120.367 1.00 24.03 ?  234 PHE A CG    1 
ATOM   1877  C  CD1   . PHE A 1 234 ? 131.159 136.498 119.593 1.00 27.38 ?  234 PHE A CD1   1 
ATOM   1878  C  CD2   . PHE A 1 234 ? 132.888 135.247 120.641 1.00 23.01 ?  234 PHE A CD2   1 
ATOM   1879  C  CE1   . PHE A 1 234 ? 132.096 137.380 119.097 1.00 26.14 ?  234 PHE A CE1   1 
ATOM   1880  C  CE2   . PHE A 1 234 ? 133.827 136.129 120.153 1.00 24.47 ?  234 PHE A CE2   1 
ATOM   1881  C  CZ    . PHE A 1 234 ? 133.431 137.195 119.378 1.00 26.41 ?  234 PHE A CZ    1 
ATOM   1882  N  N     . ARG A 1 235 ? 128.117 133.394 122.857 1.00 31.26 ?  235 ARG A N     1 
ATOM   1883  C  CA    . ARG A 1 235 ? 126.866 132.680 123.082 1.00 26.90 ?  235 ARG A CA    1 
ATOM   1884  C  C     . ARG A 1 235 ? 125.748 133.623 123.501 1.00 32.93 ?  235 ARG A C     1 
ATOM   1885  O  O     . ARG A 1 235 ? 124.593 133.422 123.112 1.00 39.75 ?  235 ARG A O     1 
ATOM   1886  C  CB    . ARG A 1 235 ? 127.051 131.586 124.131 1.00 23.83 ?  235 ARG A CB    1 
ATOM   1887  C  CG    . ARG A 1 235 ? 126.952 130.186 123.568 1.00 35.16 ?  235 ARG A CG    1 
ATOM   1888  C  CD    . ARG A 1 235 ? 126.628 129.163 124.651 1.00 37.47 ?  235 ARG A CD    1 
ATOM   1889  N  NE    . ARG A 1 235 ? 127.525 129.216 125.801 1.00 36.06 ?  235 ARG A NE    1 
ATOM   1890  C  CZ    . ARG A 1 235 ? 128.838 129.033 125.750 1.00 36.85 ?  235 ARG A CZ    1 
ATOM   1891  N  NH1   . ARG A 1 235 ? 129.455 128.731 124.619 1.00 35.35 1  235 ARG A NH1   1 
ATOM   1892  N  NH2   . ARG A 1 235 ? 129.551 129.135 126.869 1.00 33.99 ?  235 ARG A NH2   1 
ATOM   1893  N  N     . TYR A 1 236 ? 126.063 134.644 124.298 1.00 29.33 ?  236 TYR A N     1 
ATOM   1894  C  CA    . TYR A 1 236 ? 125.034 135.583 124.728 1.00 27.39 ?  236 TYR A CA    1 
ATOM   1895  C  C     . TYR A 1 236 ? 124.533 136.426 123.562 1.00 26.88 ?  236 TYR A C     1 
ATOM   1896  O  O     . TYR A 1 236 ? 123.322 136.571 123.362 1.00 32.69 ?  236 TYR A O     1 
ATOM   1897  C  CB    . TYR A 1 236 ? 125.570 136.478 125.843 1.00 28.09 ?  236 TYR A CB    1 
ATOM   1898  C  CG    . TYR A 1 236 ? 124.528 137.414 126.398 1.00 29.84 ?  236 TYR A CG    1 
ATOM   1899  C  CD1   . TYR A 1 236 ? 123.506 136.936 127.204 1.00 26.03 ?  236 TYR A CD1   1 
ATOM   1900  C  CD2   . TYR A 1 236 ? 124.553 138.770 126.103 1.00 29.81 ?  236 TYR A CD2   1 
ATOM   1901  C  CE1   . TYR A 1 236 ? 122.549 137.779 127.708 1.00 30.09 ?  236 TYR A CE1   1 
ATOM   1902  C  CE2   . TYR A 1 236 ? 123.596 139.623 126.607 1.00 23.27 ?  236 TYR A CE2   1 
ATOM   1903  C  CZ    . TYR A 1 236 ? 122.597 139.119 127.411 1.00 24.22 ?  236 TYR A CZ    1 
ATOM   1904  O  OH    . TYR A 1 236 ? 121.635 139.952 127.921 1.00 29.49 ?  236 TYR A OH    1 
ATOM   1905  N  N     . ALA A 1 237 ? 125.451 136.993 122.780 1.00 30.76 ?  237 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 237 ? 125.087 137.831 121.638 1.00 33.92 ?  237 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 237 ? 124.962 136.935 120.410 1.00 38.01 ?  237 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 237 ? 125.899 136.746 119.632 1.00 37.56 ?  237 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 237 ? 126.109 138.941 121.436 1.00 31.93 ?  237 ALA A CB    1 
ATOM   1910  N  N     . ASP A 1 238 ? 123.769 136.368 120.243 1.00 54.09 ?  238 ASP A N     1 
ATOM   1911  C  CA    . ASP A 1 238 ? 123.510 135.396 119.192 1.00 57.14 ?  238 ASP A CA    1 
ATOM   1912  C  C     . ASP A 1 238 ? 122.410 135.821 118.228 1.00 59.65 ?  238 ASP A C     1 
ATOM   1913  O  O     . ASP A 1 238 ? 122.114 135.073 117.290 1.00 62.01 ?  238 ASP A O     1 
ATOM   1914  C  CB    . ASP A 1 238 ? 123.153 134.040 119.811 1.00 56.12 ?  238 ASP A CB    1 
ATOM   1915  C  CG    . ASP A 1 238 ? 121.921 134.108 120.688 1.00 59.17 ?  238 ASP A CG    1 
ATOM   1916  O  OD1   . ASP A 1 238 ? 121.562 135.219 121.130 1.00 58.79 ?  238 ASP A OD1   1 
ATOM   1917  O  OD2   . ASP A 1 238 ? 121.309 133.048 120.936 1.00 61.73 -1 238 ASP A OD2   1 
ATOM   1918  N  N     . GLN A 1 239 ? 121.796 136.988 118.432 1.00 61.84 ?  239 GLN A N     1 
ATOM   1919  C  CA    . GLN A 1 239 ? 120.785 137.535 117.525 1.00 63.57 ?  239 GLN A CA    1 
ATOM   1920  C  C     . GLN A 1 239 ? 119.631 136.545 117.333 1.00 64.40 ?  239 GLN A C     1 
ATOM   1921  O  O     . GLN A 1 239 ? 119.438 135.972 116.258 1.00 64.50 ?  239 GLN A O     1 
ATOM   1922  C  CB    . GLN A 1 239 ? 121.402 137.909 116.171 1.00 62.58 ?  239 GLN A CB    1 
ATOM   1923  C  CG    . GLN A 1 239 ? 122.792 138.510 116.244 1.00 60.47 ?  239 GLN A CG    1 
ATOM   1924  C  CD    . GLN A 1 239 ? 123.550 138.327 114.947 1.00 63.61 ?  239 GLN A CD    1 
ATOM   1925  O  OE1   . GLN A 1 239 ? 124.707 137.907 114.943 1.00 63.04 ?  239 GLN A OE1   1 
ATOM   1926  N  NE2   . GLN A 1 239 ? 122.899 138.640 113.834 1.00 62.96 ?  239 GLN A NE2   1 
ATOM   1927  N  N     . MET A 1 240 ? 118.904 136.321 118.434 1.00 72.88 ?  240 MET A N     1 
ATOM   1928  C  CA    . MET A 1 240 ? 117.771 135.397 118.489 1.00 74.86 ?  240 MET A CA    1 
ATOM   1929  C  C     . MET A 1 240 ? 118.217 133.940 118.437 1.00 74.66 ?  240 MET A C     1 
ATOM   1930  O  O     . MET A 1 240 ? 117.405 133.029 118.632 1.00 76.79 ?  240 MET A O     1 
ATOM   1931  C  CB    . MET A 1 240 ? 116.778 135.670 117.350 1.00 75.37 ?  240 MET A CB    1 
ATOM   1932  C  CG    . MET A 1 240 ? 115.393 135.077 117.552 1.00 74.25 ?  240 MET A CG    1 
ATOM   1933  S  SD    . MET A 1 240 ? 114.029 136.200 117.234 1.00 82.10 ?  240 MET A SD    1 
ATOM   1934  C  CE    . MET A 1 240 ? 112.654 135.058 117.362 1.00 74.95 ?  240 MET A CE    1 
ATOM   1935  N  N     . GLY A 1 241 ? 119.502 133.703 118.200 1.00 73.27 ?  241 GLY A N     1 
ATOM   1936  C  CA    . GLY A 1 241 ? 119.979 132.364 117.949 1.00 72.70 ?  241 GLY A CA    1 
ATOM   1937  C  C     . GLY A 1 241 ? 119.772 131.882 116.530 1.00 75.66 ?  241 GLY A C     1 
ATOM   1938  O  O     . GLY A 1 241 ? 120.172 130.753 116.214 1.00 74.83 ?  241 GLY A O     1 
ATOM   1939  N  N     . GLN A 1 242 ? 119.152 132.695 115.670 1.00 79.13 ?  242 GLN A N     1 
ATOM   1940  C  CA    . GLN A 1 242 ? 119.009 132.328 114.264 1.00 78.63 ?  242 GLN A CA    1 
ATOM   1941  C  C     . GLN A 1 242 ? 120.374 132.113 113.627 1.00 80.35 ?  242 GLN A C     1 
ATOM   1942  O  O     . GLN A 1 242 ? 120.604 131.115 112.934 1.00 79.65 ?  242 GLN A O     1 
ATOM   1943  C  CB    . GLN A 1 242 ? 118.235 133.417 113.518 1.00 77.99 ?  242 GLN A CB    1 
ATOM   1944  C  CG    . GLN A 1 242 ? 116.726 133.350 113.683 1.00 79.49 ?  242 GLN A CG    1 
ATOM   1945  C  CD    . GLN A 1 242 ? 115.995 134.221 112.679 1.00 79.66 ?  242 GLN A CD    1 
ATOM   1946  O  OE1   . GLN A 1 242 ? 116.615 134.862 111.830 1.00 78.67 ?  242 GLN A OE1   1 
ATOM   1947  N  NE2   . GLN A 1 242 ? 114.671 134.253 112.775 1.00 79.18 ?  242 GLN A NE2   1 
ATOM   1948  N  N     . ARG A 1 243 ? 121.295 133.045 113.858 1.00 67.57 ?  243 ARG A N     1 
ATOM   1949  C  CA    . ARG A 1 243 ? 122.708 132.873 113.544 1.00 64.53 ?  243 ARG A CA    1 
ATOM   1950  C  C     . ARG A 1 243 ? 123.479 133.183 114.818 1.00 65.13 ?  243 ARG A C     1 
ATOM   1951  O  O     . ARG A 1 243 ? 123.709 134.355 115.135 1.00 64.19 ?  243 ARG A O     1 
ATOM   1952  C  CB    . ARG A 1 243 ? 123.148 133.785 112.398 1.00 63.99 ?  243 ARG A CB    1 
ATOM   1953  C  CG    . ARG A 1 243 ? 124.562 133.517 111.911 1.00 65.11 ?  243 ARG A CG    1 
ATOM   1954  C  CD    . ARG A 1 243 ? 125.365 134.803 111.802 1.00 63.87 ?  243 ARG A CD    1 
ATOM   1955  N  NE    . ARG A 1 243 ? 125.679 135.354 113.114 1.00 65.64 ?  243 ARG A NE    1 
ATOM   1956  C  CZ    . ARG A 1 243 ? 126.757 136.079 113.385 1.00 62.31 ?  243 ARG A CZ    1 
ATOM   1957  N  NH1   . ARG A 1 243 ? 127.655 136.355 112.455 1.00 61.32 1  243 ARG A NH1   1 
ATOM   1958  N  NH2   . ARG A 1 243 ? 126.937 136.535 114.621 1.00 59.64 ?  243 ARG A NH2   1 
ATOM   1959  N  N     . GLN A 1 244 ? 123.869 132.138 115.546 1.00 62.49 ?  244 GLN A N     1 
ATOM   1960  C  CA    . GLN A 1 244 ? 124.518 132.325 116.835 1.00 60.92 ?  244 GLN A CA    1 
ATOM   1961  C  C     . GLN A 1 244 ? 125.830 133.082 116.671 1.00 61.50 ?  244 GLN A C     1 
ATOM   1962  O  O     . GLN A 1 244 ? 126.448 133.080 115.602 1.00 59.07 ?  244 GLN A O     1 
ATOM   1963  C  CB    . GLN A 1 244 ? 124.768 130.973 117.510 1.00 59.61 ?  244 GLN A CB    1 
ATOM   1964  C  CG    . GLN A 1 244 ? 126.020 130.251 117.038 1.00 61.35 ?  244 GLN A CG    1 
ATOM   1965  C  CD    . GLN A 1 244 ? 125.913 129.764 115.607 1.00 63.43 ?  244 GLN A CD    1 
ATOM   1966  O  OE1   . GLN A 1 244 ? 124.815 129.547 115.094 1.00 62.60 ?  244 GLN A OE1   1 
ATOM   1967  N  NE2   . GLN A 1 244 ? 127.055 129.590 114.953 1.00 60.79 ?  244 GLN A NE2   1 
ATOM   1968  N  N     . GLY A 1 245 ? 126.242 133.756 117.744 1.00 51.77 ?  245 GLY A N     1 
ATOM   1969  C  CA    . GLY A 1 245 ? 127.452 134.552 117.718 1.00 44.75 ?  245 GLY A CA    1 
ATOM   1970  C  C     . GLY A 1 245 ? 128.675 133.738 117.364 1.00 44.79 ?  245 GLY A C     1 
ATOM   1971  O  O     . GLY A 1 245 ? 128.971 132.727 118.008 1.00 45.23 ?  245 GLY A O     1 
ATOM   1972  N  N     . SER A 1 246 ? 129.395 134.171 116.334 1.00 39.42 ?  246 SER A N     1 
ATOM   1973  C  CA    . SER A 1 246 ? 130.565 133.466 115.837 1.00 34.17 ?  246 SER A CA    1 
ATOM   1974  C  C     . SER A 1 246 ? 131.809 134.285 116.138 1.00 31.18 ?  246 SER A C     1 
ATOM   1975  O  O     . SER A 1 246 ? 131.904 135.451 115.739 1.00 27.05 ?  246 SER A O     1 
ATOM   1976  C  CB    . SER A 1 246 ? 130.451 133.204 114.335 1.00 31.85 ?  246 SER A CB    1 
ATOM   1977  O  OG    . SER A 1 246 ? 129.445 132.246 114.061 1.00 41.80 ?  246 SER A OG    1 
ATOM   1978  N  N     . GLY A 1 247 ? 132.759 133.673 116.840 1.00 24.77 ?  247 GLY A N     1 
ATOM   1979  C  CA    . GLY A 1 247 ? 134.004 134.328 117.156 1.00 11.06 ?  247 GLY A CA    1 
ATOM   1980  C  C     . GLY A 1 247 ? 135.182 133.448 116.792 1.00 15.76 ?  247 GLY A C     1 
ATOM   1981  O  O     . GLY A 1 247 ? 135.066 132.230 116.668 1.00 22.75 ?  247 GLY A O     1 
ATOM   1982  N  N     . ALA A 1 248 ? 136.324 134.098 116.608 1.00 19.37 ?  248 ALA A N     1 
ATOM   1983  C  CA    . ALA A 1 248 ? 137.582 133.417 116.359 1.00 16.42 ?  248 ALA A CA    1 
ATOM   1984  C  C     . ALA A 1 248 ? 138.642 133.985 117.286 1.00 12.25 ?  248 ALA A C     1 
ATOM   1985  O  O     . ALA A 1 248 ? 138.681 135.192 117.532 1.00 20.81 ?  248 ALA A O     1 
ATOM   1986  C  CB    . ALA A 1 248 ? 138.027 133.558 114.900 1.00 9.18  ?  248 ALA A CB    1 
ATOM   1987  N  N     . ALA A 1 249 ? 139.490 133.108 117.806 1.00 17.17 ?  249 ALA A N     1 
ATOM   1988  C  CA    . ALA A 1 249 ? 140.629 133.503 118.618 1.00 11.41 ?  249 ALA A CA    1 
ATOM   1989  C  C     . ALA A 1 249 ? 141.904 133.073 117.913 1.00 10.22 ?  249 ALA A C     1 
ATOM   1990  O  O     . ALA A 1 249 ? 141.973 131.978 117.352 1.00 19.58 ?  249 ALA A O     1 
ATOM   1991  C  CB    . ALA A 1 249 ? 140.562 132.887 120.016 1.00 13.14 ?  249 ALA A CB    1 
ATOM   1992  N  N     . TYR A 1 250 ? 142.906 133.941 117.930 1.00 11.19 ?  250 TYR A N     1 
ATOM   1993  C  CA    . TYR A 1 250 ? 144.182 133.653 117.300 1.00 7.84  ?  250 TYR A CA    1 
ATOM   1994  C  C     . TYR A 1 250 ? 145.291 133.733 118.334 1.00 8.84  ?  250 TYR A C     1 
ATOM   1995  O  O     . TYR A 1 250 ? 145.312 134.640 119.171 1.00 13.20 ?  250 TYR A O     1 
ATOM   1996  C  CB    . TYR A 1 250 ? 144.464 134.617 116.146 1.00 10.59 ?  250 TYR A CB    1 
ATOM   1997  C  CG    . TYR A 1 250 ? 143.835 134.196 114.840 1.00 19.08 ?  250 TYR A CG    1 
ATOM   1998  C  CD1   . TYR A 1 250 ? 142.486 134.408 114.598 1.00 8.70  ?  250 TYR A CD1   1 
ATOM   1999  C  CD2   . TYR A 1 250 ? 144.586 133.572 113.853 1.00 12.91 ?  250 TYR A CD2   1 
ATOM   2000  C  CE1   . TYR A 1 250 ? 141.906 134.021 113.412 1.00 0.00  ?  250 TYR A CE1   1 
ATOM   2001  C  CE2   . TYR A 1 250 ? 144.013 133.183 112.661 1.00 7.59  ?  250 TYR A CE2   1 
ATOM   2002  C  CZ    . TYR A 1 250 ? 142.672 133.409 112.447 1.00 7.54  ?  250 TYR A CZ    1 
ATOM   2003  O  OH    . TYR A 1 250 ? 142.090 133.026 111.263 1.00 22.46 ?  250 TYR A OH    1 
ATOM   2004  N  N     . LEU A 1 251 ? 146.205 132.773 118.274 1.00 10.93 ?  251 LEU A N     1 
ATOM   2005  C  CA    . LEU A 1 251 ? 147.357 132.732 119.157 1.00 12.86 ?  251 LEU A CA    1 
ATOM   2006  C  C     . LEU A 1 251 ? 148.605 132.434 118.346 1.00 11.61 ?  251 LEU A C     1 
ATOM   2007  O  O     . LEU A 1 251 ? 148.595 131.561 117.473 1.00 17.27 ?  251 LEU A O     1 
ATOM   2008  C  CB    . LEU A 1 251 ? 147.186 131.676 120.250 1.00 18.54 ?  251 LEU A CB    1 
ATOM   2009  C  CG    . LEU A 1 251 ? 147.940 131.961 121.547 1.00 14.33 ?  251 LEU A CG    1 
ATOM   2010  C  CD1   . LEU A 1 251 ? 147.217 133.014 122.357 1.00 16.35 ?  251 LEU A CD1   1 
ATOM   2011  C  CD2   . LEU A 1 251 ? 148.114 130.692 122.351 1.00 13.33 ?  251 LEU A CD2   1 
ATOM   2012  N  N     . ASN A 1 252 ? 149.673 133.171 118.628 1.00 12.05 ?  252 ASN A N     1 
ATOM   2013  C  CA    . ASN A 1 252 ? 150.963 132.863 118.034 1.00 12.86 ?  252 ASN A CA    1 
ATOM   2014  C  C     . ASN A 1 252 ? 151.461 131.520 118.552 1.00 17.68 ?  252 ASN A C     1 
ATOM   2015  O  O     . ASN A 1 252 ? 151.281 131.183 119.724 1.00 23.42 ?  252 ASN A O     1 
ATOM   2016  C  CB    . ASN A 1 252 ? 151.970 133.967 118.347 1.00 15.86 ?  252 ASN A CB    1 
ATOM   2017  C  CG    . ASN A 1 252 ? 153.226 133.867 117.509 1.00 20.25 ?  252 ASN A CG    1 
ATOM   2018  O  OD1   . ASN A 1 252 ? 154.185 133.199 117.888 1.00 25.80 ?  252 ASN A OD1   1 
ATOM   2019  N  ND2   . ASN A 1 252 ? 153.223 134.528 116.360 1.00 15.68 ?  252 ASN A ND2   1 
ATOM   2020  N  N     . ILE A 1 253 ? 152.088 130.746 117.663 1.00 15.99 ?  253 ILE A N     1 
ATOM   2021  C  CA    . ILE A 1 253 ? 152.536 129.407 118.027 1.00 14.48 ?  253 ILE A CA    1 
ATOM   2022  C  C     . ILE A 1 253 ? 153.620 129.442 119.097 1.00 19.81 ?  253 ILE A C     1 
ATOM   2023  O  O     . ILE A 1 253 ? 153.847 128.436 119.776 1.00 23.62 ?  253 ILE A O     1 
ATOM   2024  C  CB    . ILE A 1 253 ? 153.012 128.654 116.769 1.00 17.64 ?  253 ILE A CB    1 
ATOM   2025  C  CG1   . ILE A 1 253 ? 153.059 127.148 117.030 1.00 19.79 ?  253 ILE A CG1   1 
ATOM   2026  C  CG2   . ILE A 1 253 ? 154.366 129.170 116.309 1.00 14.47 ?  253 ILE A CG2   1 
ATOM   2027  C  CD1   . ILE A 1 253 ? 152.541 126.317 115.886 1.00 16.32 ?  253 ILE A CD1   1 
ATOM   2028  N  N     . PHE A 1 254 ? 154.288 130.579 119.277 1.00 23.04 ?  254 PHE A N     1 
ATOM   2029  C  CA    . PHE A 1 254 ? 155.325 130.723 120.289 1.00 20.04 ?  254 PHE A CA    1 
ATOM   2030  C  C     . PHE A 1 254 ? 154.785 131.221 121.621 1.00 19.83 ?  254 PHE A C     1 
ATOM   2031  O  O     . PHE A 1 254 ? 155.566 131.419 122.557 1.00 29.11 ?  254 PHE A O     1 
ATOM   2032  C  CB    . PHE A 1 254 ? 156.422 131.663 119.783 1.00 23.31 ?  254 PHE A CB    1 
ATOM   2033  C  CG    . PHE A 1 254 ? 157.383 131.008 118.836 1.00 23.76 ?  254 PHE A CG    1 
ATOM   2034  C  CD1   . PHE A 1 254 ? 158.236 130.013 119.275 1.00 25.73 ?  254 PHE A CD1   1 
ATOM   2035  C  CD2   . PHE A 1 254 ? 157.421 131.376 117.503 1.00 24.41 ?  254 PHE A CD2   1 
ATOM   2036  C  CE1   . PHE A 1 254 ? 159.119 129.405 118.406 1.00 24.63 ?  254 PHE A CE1   1 
ATOM   2037  C  CE2   . PHE A 1 254 ? 158.302 130.771 116.630 1.00 28.73 ?  254 PHE A CE2   1 
ATOM   2038  C  CZ    . PHE A 1 254 ? 159.152 129.784 117.083 1.00 26.32 ?  254 PHE A CZ    1 
ATOM   2039  N  N     . HIS A 1 255 ? 153.478 131.440 121.724 1.00 22.21 ?  255 HIS A N     1 
ATOM   2040  C  CA    . HIS A 1 255 ? 152.857 131.711 123.011 1.00 22.02 ?  255 HIS A CA    1 
ATOM   2041  C  C     . HIS A 1 255 ? 152.935 130.468 123.888 1.00 23.79 ?  255 HIS A C     1 
ATOM   2042  O  O     . HIS A 1 255 ? 152.796 129.342 123.408 1.00 27.87 ?  255 HIS A O     1 
ATOM   2043  C  CB    . HIS A 1 255 ? 151.400 132.128 122.808 1.00 23.90 ?  255 HIS A CB    1 
ATOM   2044  C  CG    . HIS A 1 255 ? 150.809 132.873 123.965 1.00 19.97 ?  255 HIS A CG    1 
ATOM   2045  N  ND1   . HIS A 1 255 ? 150.422 132.252 125.132 1.00 16.34 ?  255 HIS A ND1   1 
ATOM   2046  C  CD2   . HIS A 1 255 ? 150.509 134.183 124.120 1.00 17.37 ?  255 HIS A CD2   1 
ATOM   2047  C  CE1   . HIS A 1 255 ? 149.928 133.150 125.964 1.00 17.98 ?  255 HIS A CE1   1 
ATOM   2048  N  NE2   . HIS A 1 255 ? 149.967 134.330 125.373 1.00 17.01 ?  255 HIS A NE2   1 
ATOM   2049  N  N     . ARG A 1 256 ? 153.174 130.677 125.184 1.00 23.57 ?  256 ARG A N     1 
ATOM   2050  C  CA    . ARG A 1 256 ? 153.286 129.546 126.099 1.00 26.08 ?  256 ARG A CA    1 
ATOM   2051  C  C     . ARG A 1 256 ? 151.979 128.770 126.201 1.00 25.39 ?  256 ARG A C     1 
ATOM   2052  O  O     . ARG A 1 256 ? 151.994 127.547 126.377 1.00 31.14 ?  256 ARG A O     1 
ATOM   2053  C  CB    . ARG A 1 256 ? 153.725 130.028 127.479 1.00 28.03 ?  256 ARG A CB    1 
ATOM   2054  C  CG    . ARG A 1 256 ? 153.971 128.909 128.466 1.00 29.43 ?  256 ARG A CG    1 
ATOM   2055  C  CD    . ARG A 1 256 ? 153.040 129.006 129.660 1.00 29.65 ?  256 ARG A CD    1 
ATOM   2056  N  NE    . ARG A 1 256 ? 151.772 128.326 129.435 1.00 31.35 ?  256 ARG A NE    1 
ATOM   2057  C  CZ    . ARG A 1 256 ? 151.515 127.081 129.808 1.00 34.72 ?  256 ARG A CZ    1 
ATOM   2058  N  NH1   . ARG A 1 256 ? 152.425 126.344 130.424 1.00 33.44 1  256 ARG A NH1   1 
ATOM   2059  N  NH2   . ARG A 1 256 ? 150.318 126.561 129.556 1.00 30.56 ?  256 ARG A NH2   1 
ATOM   2060  N  N     . ASP A 1 257 ? 150.846 129.455 126.085 1.00 23.03 ?  257 ASP A N     1 
ATOM   2061  C  CA    . ASP A 1 257 ? 149.534 128.835 126.199 1.00 19.77 ?  257 ASP A CA    1 
ATOM   2062  C  C     . ASP A 1 257 ? 149.092 128.126 124.929 1.00 23.50 ?  257 ASP A C     1 
ATOM   2063  O  O     . ASP A 1 257 ? 147.903 127.815 124.810 1.00 29.98 ?  257 ASP A O     1 
ATOM   2064  C  CB    . ASP A 1 257 ? 148.486 129.883 126.578 1.00 25.21 ?  257 ASP A CB    1 
ATOM   2065  C  CG    . ASP A 1 257 ? 148.587 130.316 128.020 1.00 31.90 ?  257 ASP A CG    1 
ATOM   2066  O  OD1   . ASP A 1 257 ? 149.298 129.651 128.801 1.00 32.69 ?  257 ASP A OD1   1 
ATOM   2067  O  OD2   . ASP A 1 257 ? 147.947 131.323 128.373 1.00 32.98 -1 257 ASP A OD2   1 
ATOM   2068  N  N     . ILE A 1 258 ? 149.999 127.863 123.986 1.00 24.69 ?  258 ILE A N     1 
ATOM   2069  C  CA    . ILE A 1 258 ? 149.586 127.325 122.693 1.00 21.61 ?  258 ILE A CA    1 
ATOM   2070  C  C     . ILE A 1 258 ? 148.988 125.932 122.849 1.00 20.20 ?  258 ILE A C     1 
ATOM   2071  O  O     . ILE A 1 258 ? 148.009 125.587 122.178 1.00 27.04 ?  258 ILE A O     1 
ATOM   2072  C  CB    . ILE A 1 258 ? 150.766 127.340 121.700 1.00 24.23 ?  258 ILE A CB    1 
ATOM   2073  C  CG1   . ILE A 1 258 ? 150.304 126.888 120.312 1.00 22.62 ?  258 ILE A CG1   1 
ATOM   2074  C  CG2   . ILE A 1 258 ? 151.928 126.489 122.199 1.00 17.77 ?  258 ILE A CG2   1 
ATOM   2075  C  CD1   . ILE A 1 258 ? 149.296 127.814 119.672 1.00 17.72 ?  258 ILE A CD1   1 
ATOM   2076  N  N     . ASN A 1 259 ? 149.552 125.113 123.738 1.00 31.20 ?  259 ASN A N     1 
ATOM   2077  C  CA    . ASN A 1 259 ? 149.028 123.764 123.924 1.00 25.53 ?  259 ASN A CA    1 
ATOM   2078  C  C     . ASN A 1 259 ? 147.661 123.787 124.596 1.00 29.96 ?  259 ASN A C     1 
ATOM   2079  O  O     . ASN A 1 259 ? 146.760 123.041 124.202 1.00 34.90 ?  259 ASN A O     1 
ATOM   2080  C  CB    . ASN A 1 259 ? 150.019 122.928 124.728 1.00 30.04 ?  259 ASN A CB    1 
ATOM   2081  C  CG    . ASN A 1 259 ? 151.314 122.687 123.981 1.00 34.90 ?  259 ASN A CG    1 
ATOM   2082  O  OD1   . ASN A 1 259 ? 151.335 122.005 122.960 1.00 34.38 ?  259 ASN A OD1   1 
ATOM   2083  N  ND2   . ASN A 1 259 ? 152.403 123.253 124.487 1.00 36.03 ?  259 ASN A ND2   1 
ATOM   2084  N  N     . ASP A 1 260 ? 147.487 124.637 125.611 1.00 29.27 ?  260 ASP A N     1 
ATOM   2085  C  CA    . ASP A 1 260 ? 146.167 124.805 126.208 1.00 25.18 ?  260 ASP A CA    1 
ATOM   2086  C  C     . ASP A 1 260 ? 145.200 125.470 125.238 1.00 26.78 ?  260 ASP A C     1 
ATOM   2087  O  O     . ASP A 1 260 ? 144.000 125.180 125.263 1.00 35.48 ?  260 ASP A O     1 
ATOM   2088  C  CB    . ASP A 1 260 ? 146.268 125.621 127.496 1.00 27.48 ?  260 ASP A CB    1 
ATOM   2089  C  CG    . ASP A 1 260 ? 147.394 125.153 128.395 1.00 39.93 ?  260 ASP A CG    1 
ATOM   2090  O  OD1   . ASP A 1 260 ? 147.534 123.927 128.588 1.00 37.41 ?  260 ASP A OD1   1 
ATOM   2091  O  OD2   . ASP A 1 260 ? 148.141 126.013 128.908 1.00 39.68 -1 260 ASP A OD2   1 
ATOM   2092  N  N     . PHE A 1 261 ? 145.705 126.371 124.392 1.00 31.54 ?  261 PHE A N     1 
ATOM   2093  C  CA    . PHE A 1 261 ? 144.877 126.991 123.364 1.00 22.38 ?  261 PHE A CA    1 
ATOM   2094  C  C     . PHE A 1 261 ? 144.341 125.946 122.397 1.00 21.58 ?  261 PHE A C     1 
ATOM   2095  O  O     . PHE A 1 261 ? 143.170 125.995 122.001 1.00 24.08 ?  261 PHE A O     1 
ATOM   2096  C  CB    . PHE A 1 261 ? 145.701 128.052 122.631 1.00 15.65 ?  261 PHE A CB    1 
ATOM   2097  C  CG    . PHE A 1 261 ? 144.989 128.719 121.491 1.00 22.10 ?  261 PHE A CG    1 
ATOM   2098  C  CD1   . PHE A 1 261 ? 144.146 129.791 121.719 1.00 20.48 ?  261 PHE A CD1   1 
ATOM   2099  C  CD2   . PHE A 1 261 ? 145.200 128.308 120.187 1.00 24.42 ?  261 PHE A CD2   1 
ATOM   2100  C  CE1   . PHE A 1 261 ? 143.504 130.418 120.674 1.00 14.82 ?  261 PHE A CE1   1 
ATOM   2101  C  CE2   . PHE A 1 261 ? 144.560 128.933 119.139 1.00 20.16 ?  261 PHE A CE2   1 
ATOM   2102  C  CZ    . PHE A 1 261 ? 143.713 129.990 119.385 1.00 14.38 ?  261 PHE A CZ    1 
ATOM   2103  N  N     . LEU A 1 262 ? 145.183 124.987 122.009 1.00 26.28 ?  262 LEU A N     1 
ATOM   2104  C  CA    . LEU A 1 262 ? 144.756 123.916 121.117 1.00 22.74 ?  262 LEU A CA    1 
ATOM   2105  C  C     . LEU A 1 262 ? 143.903 122.875 121.828 1.00 30.54 ?  262 LEU A C     1 
ATOM   2106  O  O     . LEU A 1 262 ? 143.044 122.252 121.195 1.00 34.37 ?  262 LEU A O     1 
ATOM   2107  C  CB    . LEU A 1 262 ? 145.973 123.242 120.486 1.00 26.69 ?  262 LEU A CB    1 
ATOM   2108  C  CG    . LEU A 1 262 ? 146.853 124.124 119.603 1.00 23.46 ?  262 LEU A CG    1 
ATOM   2109  C  CD1   . LEU A 1 262 ? 148.110 123.377 119.205 1.00 24.29 ?  262 LEU A CD1   1 
ATOM   2110  C  CD2   . LEU A 1 262 ? 146.088 124.592 118.381 1.00 22.16 ?  262 LEU A CD2   1 
ATOM   2111  N  N     . ASP A 1 263 ? 144.120 122.667 123.128 1.00 38.57 ?  263 ASP A N     1 
ATOM   2112  C  CA    . ASP A 1 263 ? 143.351 121.675 123.870 1.00 30.89 ?  263 ASP A CA    1 
ATOM   2113  C  C     . ASP A 1 263 ? 141.894 122.071 124.056 1.00 32.35 ?  263 ASP A C     1 
ATOM   2114  O  O     . ASP A 1 263 ? 141.089 121.224 124.459 1.00 41.94 ?  263 ASP A O     1 
ATOM   2115  C  CB    . ASP A 1 263 ? 143.989 121.422 125.236 1.00 33.94 ?  263 ASP A CB    1 
ATOM   2116  C  CG    . ASP A 1 263 ? 145.276 120.629 125.141 1.00 40.92 ?  263 ASP A CG    1 
ATOM   2117  O  OD1   . ASP A 1 263 ? 145.515 120.008 124.085 1.00 37.88 ?  263 ASP A OD1   1 
ATOM   2118  O  OD2   . ASP A 1 263 ? 146.046 120.628 126.124 1.00 42.51 -1 263 ASP A OD2   1 
ATOM   2119  N  N     . THR A 1 264 ? 141.534 123.326 123.786 1.00 37.53 ?  264 THR A N     1 
ATOM   2120  C  CA    . THR A 1 264 ? 140.138 123.737 123.850 1.00 36.65 ?  264 THR A CA    1 
ATOM   2121  C  C     . THR A 1 264 ? 139.299 123.141 122.728 1.00 38.27 ?  264 THR A C     1 
ATOM   2122  O  O     . THR A 1 264 ? 138.068 123.192 122.807 1.00 42.43 ?  264 THR A O     1 
ATOM   2123  C  CB    . THR A 1 264 ? 140.034 125.264 123.810 1.00 37.79 ?  264 THR A CB    1 
ATOM   2124  O  OG1   . THR A 1 264 ? 140.601 125.754 122.590 1.00 41.67 ?  264 THR A OG1   1 
ATOM   2125  C  CG2   . THR A 1 264 ? 140.771 125.879 124.987 1.00 33.19 ?  264 THR A CG2   1 
ATOM   2126  N  N     . LYS A 1 265 ? 139.929 122.581 121.697 1.00 34.74 ?  265 LYS A N     1 
ATOM   2127  C  CA    . LYS A 1 265 ? 139.220 121.997 120.569 1.00 38.69 ?  265 LYS A CA    1 
ATOM   2128  C  C     . LYS A 1 265 ? 139.272 120.477 120.548 1.00 38.10 ?  265 LYS A C     1 
ATOM   2129  O  O     . LYS A 1 265 ? 138.667 119.864 119.663 1.00 42.13 ?  265 LYS A O     1 
ATOM   2130  C  CB    . LYS A 1 265 ? 139.778 122.546 119.253 1.00 37.22 ?  265 LYS A CB    1 
ATOM   2131  C  CG    . LYS A 1 265 ? 139.269 123.926 118.899 1.00 37.99 ?  265 LYS A CG    1 
ATOM   2132  C  CD    . LYS A 1 265 ? 137.782 124.037 119.149 1.00 38.69 ?  265 LYS A CD    1 
ATOM   2133  C  CE    . LYS A 1 265 ? 137.259 125.384 118.711 1.00 36.61 ?  265 LYS A CE    1 
ATOM   2134  N  NZ    . LYS A 1 265 ? 135.877 125.622 119.204 1.00 42.06 1  265 LYS A NZ    1 
ATOM   2135  N  N     . LYS A 1 266 ? 139.977 119.854 121.487 1.00 40.85 ?  266 LYS A N     1 
ATOM   2136  C  CA    . LYS A 1 266 ? 140.005 118.401 121.551 1.00 45.78 ?  266 LYS A CA    1 
ATOM   2137  C  C     . LYS A 1 266 ? 138.630 117.859 121.922 1.00 51.25 ?  266 LYS A C     1 
ATOM   2138  O  O     . LYS A 1 266 ? 137.879 118.469 122.688 1.00 51.79 ?  266 LYS A O     1 
ATOM   2139  C  CB    . LYS A 1 266 ? 141.049 117.928 122.561 1.00 44.22 ?  266 LYS A CB    1 
ATOM   2140  C  CG    . LYS A 1 266 ? 142.467 117.919 122.020 1.00 46.23 ?  266 LYS A CG    1 
ATOM   2141  C  CD    . LYS A 1 266 ? 143.455 117.416 123.057 1.00 48.71 ?  266 LYS A CD    1 
ATOM   2142  C  CE    . LYS A 1 266 ? 144.810 117.129 122.430 1.00 49.28 ?  266 LYS A CE    1 
ATOM   2143  N  NZ    . LYS A 1 266 ? 145.887 117.005 123.451 1.00 47.87 1  266 LYS A NZ    1 
ATOM   2144  N  N     . ILE A 1 267 ? 138.299 116.698 121.356 1.00 54.28 ?  267 ILE A N     1 
ATOM   2145  C  CA    . ILE A 1 267 ? 137.006 116.078 121.631 1.00 55.14 ?  267 ILE A CA    1 
ATOM   2146  C  C     . ILE A 1 267 ? 136.905 115.672 123.096 1.00 57.07 ?  267 ILE A C     1 
ATOM   2147  O  O     . ILE A 1 267 ? 135.829 115.744 123.701 1.00 54.69 ?  267 ILE A O     1 
ATOM   2148  C  CB    . ILE A 1 267 ? 136.778 114.884 120.686 1.00 55.54 ?  267 ILE A CB    1 
ATOM   2149  C  CG1   . ILE A 1 267 ? 138.050 114.039 120.580 1.00 57.04 ?  267 ILE A CG1   1 
ATOM   2150  C  CG2   . ILE A 1 267 ? 136.333 115.367 119.317 1.00 55.23 ?  267 ILE A CG2   1 
ATOM   2151  C  CD1   . ILE A 1 267 ? 137.894 112.806 119.721 1.00 55.54 ?  267 ILE A CD1   1 
ATOM   2152  N  N     . SER A 1 268 ? 138.018 115.246 123.691 1.00 60.16 ?  268 SER A N     1 
ATOM   2153  C  CA    . SER A 1 268 ? 138.059 114.839 125.089 1.00 61.20 ?  268 SER A CA    1 
ATOM   2154  C  C     . SER A 1 268 ? 138.250 116.011 126.049 1.00 63.52 ?  268 SER A C     1 
ATOM   2155  O  O     . SER A 1 268 ? 138.633 115.791 127.204 1.00 63.03 ?  268 SER A O     1 
ATOM   2156  C  CB    . SER A 1 268 ? 139.170 113.809 125.301 1.00 63.43 ?  268 SER A CB    1 
ATOM   2157  O  OG    . SER A 1 268 ? 140.416 114.301 124.840 1.00 62.04 ?  268 SER A OG    1 
ATOM   2158  N  N     . ALA A 1 269 ? 137.997 117.240 125.607 1.00 67.34 ?  269 ALA A N     1 
ATOM   2159  C  CA    . ALA A 1 269 ? 138.183 118.396 126.473 1.00 66.38 ?  269 ALA A CA    1 
ATOM   2160  C  C     . ALA A 1 269 ? 137.051 118.501 127.487 1.00 67.63 ?  269 ALA A C     1 
ATOM   2161  O  O     . ALA A 1 269 ? 135.892 118.206 127.183 1.00 65.73 ?  269 ALA A O     1 
ATOM   2162  C  CB    . ALA A 1 269 ? 138.264 119.677 125.642 1.00 63.69 ?  269 ALA A CB    1 
ATOM   2163  N  N     . ASP A 1 270 ? 137.397 118.925 128.699 1.00 75.07 ?  270 ASP A N     1 
ATOM   2164  C  CA    . ASP A 1 270 ? 136.409 119.076 129.756 1.00 75.00 ?  270 ASP A CA    1 
ATOM   2165  C  C     . ASP A 1 270 ? 135.566 120.329 129.529 1.00 74.74 ?  270 ASP A C     1 
ATOM   2166  O  O     . ASP A 1 270 ? 135.936 121.237 128.780 1.00 75.33 ?  270 ASP A O     1 
ATOM   2167  C  CB    . ASP A 1 270 ? 137.094 119.139 131.121 1.00 75.61 ?  270 ASP A CB    1 
ATOM   2168  C  CG    . ASP A 1 270 ? 136.168 118.751 132.258 1.00 77.85 ?  270 ASP A CG    1 
ATOM   2169  O  OD1   . ASP A 1 270 ? 135.146 119.440 132.460 1.00 77.52 ?  270 ASP A OD1   1 
ATOM   2170  O  OD2   . ASP A 1 270 ? 136.461 117.753 132.951 1.00 76.02 -1 270 ASP A OD2   1 
ATOM   2171  N  N     . GLU A 1 271 ? 134.411 120.366 130.196 1.00 75.70 ?  271 GLU A N     1 
ATOM   2172  C  CA    . GLU A 1 271 ? 133.502 121.498 130.058 1.00 76.74 ?  271 GLU A CA    1 
ATOM   2173  C  C     . GLU A 1 271 ? 134.076 122.785 130.636 1.00 76.23 ?  271 GLU A C     1 
ATOM   2174  O  O     . GLU A 1 271 ? 133.626 123.872 130.260 1.00 75.27 ?  271 GLU A O     1 
ATOM   2175  C  CB    . GLU A 1 271 ? 132.163 121.180 130.724 1.00 75.14 ?  271 GLU A CB    1 
ATOM   2176  C  CG    . GLU A 1 271 ? 131.431 120.001 130.106 1.00 75.56 ?  271 GLU A CG    1 
ATOM   2177  C  CD    . GLU A 1 271 ? 131.046 120.249 128.661 1.00 76.58 ?  271 GLU A CD    1 
ATOM   2178  O  OE1   . GLU A 1 271 ? 130.632 121.383 128.341 1.00 76.79 ?  271 GLU A OE1   1 
ATOM   2179  O  OE2   . GLU A 1 271 ? 131.161 119.310 127.844 1.00 75.92 -1 271 GLU A OE2   1 
ATOM   2180  N  N     . ASP A 1 272 ? 135.053 122.691 131.537 1.00 74.59 ?  272 ASP A N     1 
ATOM   2181  C  CA    . ASP A 1 272 ? 135.686 123.872 132.108 1.00 75.23 ?  272 ASP A CA    1 
ATOM   2182  C  C     . ASP A 1 272 ? 136.814 124.416 131.242 1.00 73.89 ?  272 ASP A C     1 
ATOM   2183  O  O     . ASP A 1 272 ? 137.420 125.430 131.607 1.00 71.80 ?  272 ASP A O     1 
ATOM   2184  C  CB    . ASP A 1 272 ? 136.222 123.560 133.508 1.00 74.63 ?  272 ASP A CB    1 
ATOM   2185  C  CG    . ASP A 1 272 ? 135.151 123.656 134.578 1.00 76.48 ?  272 ASP A CG    1 
ATOM   2186  O  OD1   . ASP A 1 272 ? 134.080 124.236 134.300 1.00 76.29 ?  272 ASP A OD1   1 
ATOM   2187  O  OD2   . ASP A 1 272 ? 135.383 123.154 135.697 1.00 74.73 -1 272 ASP A OD2   1 
ATOM   2188  N  N     . VAL A 1 273 ? 137.118 123.766 130.118 1.00 64.46 ?  273 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 273 ? 138.179 124.185 129.212 1.00 63.69 ?  273 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 273 ? 137.655 124.391 127.796 1.00 61.79 ?  273 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 273 ? 137.979 125.385 127.139 1.00 62.73 ?  273 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 273 ? 139.353 123.179 129.219 1.00 64.13 ?  273 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 273 ? 140.280 123.424 128.039 1.00 60.73 ?  273 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 273 ? 140.117 123.264 130.531 1.00 62.17 ?  273 VAL A CG2   1 
ATOM   2195  N  N     . ARG A 1 274 ? 136.833 123.462 127.312 1.00 58.79 ?  274 ARG A N     1 
ATOM   2196  C  CA    . ARG A 1 274 ? 136.409 123.472 125.919 1.00 56.27 ?  274 ARG A CA    1 
ATOM   2197  C  C     . ARG A 1 274 ? 135.572 124.705 125.598 1.00 56.31 ?  274 ARG A C     1 
ATOM   2198  O  O     . ARG A 1 274 ? 134.704 125.110 126.377 1.00 59.27 ?  274 ARG A O     1 
ATOM   2199  C  CB    . ARG A 1 274 ? 135.617 122.201 125.606 1.00 58.56 ?  274 ARG A CB    1 
ATOM   2200  C  CG    . ARG A 1 274 ? 134.465 122.395 124.634 1.00 56.98 ?  274 ARG A CG    1 
ATOM   2201  C  CD    . ARG A 1 274 ? 133.900 121.061 124.165 1.00 57.29 ?  274 ARG A CD    1 
ATOM   2202  N  NE    . ARG A 1 274 ? 134.799 120.333 123.275 1.00 60.77 ?  274 ARG A NE    1 
ATOM   2203  C  CZ    . ARG A 1 274 ? 135.250 120.776 122.108 1.00 60.46 ?  274 ARG A CZ    1 
ATOM   2204  N  NH1   . ARG A 1 274 ? 134.870 121.943 121.611 1.00 59.29 1  274 ARG A NH1   1 
ATOM   2205  N  NH2   . ARG A 1 274 ? 136.092 120.020 121.410 1.00 56.10 ?  274 ARG A NH2   1 
ATOM   2206  N  N     . VAL A 1 275 ? 135.846 125.302 124.441 1.00 47.22 ?  275 VAL A N     1 
ATOM   2207  C  CA    . VAL A 1 275 ? 135.051 126.391 123.889 1.00 47.42 ?  275 VAL A CA    1 
ATOM   2208  C  C     . VAL A 1 275 ? 134.354 125.873 122.639 1.00 47.78 ?  275 VAL A C     1 
ATOM   2209  O  O     . VAL A 1 275 ? 134.950 125.135 121.846 1.00 49.68 ?  275 VAL A O     1 
ATOM   2210  C  CB    . VAL A 1 275 ? 135.909 127.632 123.573 1.00 45.57 ?  275 VAL A CB    1 
ATOM   2211  C  CG1   . VAL A 1 275 ? 136.404 128.273 124.858 1.00 42.16 ?  275 VAL A CG1   1 
ATOM   2212  C  CG2   . VAL A 1 275 ? 137.078 127.261 122.683 1.00 46.32 ?  275 VAL A CG2   1 
ATOM   2213  N  N     . LYS A 1 276 ? 133.087 126.240 122.476 1.00 47.35 ?  276 LYS A N     1 
ATOM   2214  C  CA    . LYS A 1 276 ? 132.255 125.696 121.409 1.00 48.92 ?  276 LYS A CA    1 
ATOM   2215  C  C     . LYS A 1 276 ? 131.947 126.691 120.303 1.00 45.86 ?  276 LYS A C     1 
ATOM   2216  O  O     . LYS A 1 276 ? 131.976 126.324 119.127 1.00 51.39 ?  276 LYS A O     1 
ATOM   2217  C  CB    . LYS A 1 276 ? 130.942 125.167 121.997 1.00 49.48 ?  276 LYS A CB    1 
ATOM   2218  C  CG    . LYS A 1 276 ? 131.137 124.007 122.961 1.00 50.86 ?  276 LYS A CG    1 
ATOM   2219  C  CD    . LYS A 1 276 ? 129.835 123.596 123.626 1.00 51.93 ?  276 LYS A CD    1 
ATOM   2220  C  CE    . LYS A 1 276 ? 130.059 122.435 124.584 1.00 52.38 ?  276 LYS A CE    1 
ATOM   2221  N  NZ    . LYS A 1 276 ? 128.897 122.226 125.492 1.00 54.84 1  276 LYS A NZ    1 
ATOM   2222  N  N     . THR A 1 277 ? 131.652 127.943 120.643 1.00 37.03 ?  277 THR A N     1 
ATOM   2223  C  CA    . THR A 1 277 ? 131.292 128.959 119.664 1.00 38.81 ?  277 THR A CA    1 
ATOM   2224  C  C     . THR A 1 277 ? 132.489 129.765 119.181 1.00 40.67 ?  277 THR A C     1 
ATOM   2225  O  O     . THR A 1 277 ? 132.313 130.720 118.418 1.00 39.52 ?  277 THR A O     1 
ATOM   2226  C  CB    . THR A 1 277 ? 130.237 129.902 120.246 1.00 39.99 ?  277 THR A CB    1 
ATOM   2227  O  OG1   . THR A 1 277 ? 130.886 130.980 120.933 1.00 38.24 ?  277 THR A OG1   1 
ATOM   2228  C  CG2   . THR A 1 277 ? 129.348 129.155 121.216 1.00 38.90 ?  277 THR A CG2   1 
ATOM   2229  N  N     . LEU A 1 278 ? 133.698 129.406 119.603 1.00 36.61 ?  278 LEU A N     1 
ATOM   2230  C  CA    . LEU A 1 278 ? 134.899 130.178 119.307 1.00 30.45 ?  278 LEU A CA    1 
ATOM   2231  C  C     . LEU A 1 278 ? 135.813 129.350 118.415 1.00 24.23 ?  278 LEU A C     1 
ATOM   2232  O  O     . LEU A 1 278 ? 136.389 128.357 118.865 1.00 32.43 ?  278 LEU A O     1 
ATOM   2233  C  CB    . LEU A 1 278 ? 135.614 130.583 120.595 1.00 30.01 ?  278 LEU A CB    1 
ATOM   2234  C  CG    . LEU A 1 278 ? 136.511 131.817 120.531 1.00 28.95 ?  278 LEU A CG    1 
ATOM   2235  C  CD1   . LEU A 1 278 ? 135.682 133.080 120.427 1.00 23.64 ?  278 LEU A CD1   1 
ATOM   2236  C  CD2   . LEU A 1 278 ? 137.410 131.874 121.749 1.00 26.19 ?  278 LEU A CD2   1 
ATOM   2237  N  N     . SER A 1 279 ? 135.943 129.762 117.157 1.00 24.49 ?  279 SER A N     1 
ATOM   2238  C  CA    . SER A 1 279 ? 136.958 129.193 116.287 1.00 15.83 ?  279 SER A CA    1 
ATOM   2239  C  C     . SER A 1 279 ? 138.340 129.620 116.765 1.00 17.60 ?  279 SER A C     1 
ATOM   2240  O  O     . SER A 1 279 ? 138.500 130.620 117.468 1.00 28.53 ?  279 SER A O     1 
ATOM   2241  C  CB    . SER A 1 279 ? 136.741 129.636 114.841 1.00 18.86 ?  279 SER A CB    1 
ATOM   2242  O  OG    . SER A 1 279 ? 135.444 129.294 114.388 1.00 26.41 ?  279 SER A OG    1 
ATOM   2243  N  N     . ILE A 1 280 ? 139.350 128.843 116.393 1.00 15.31 ?  280 ILE A N     1 
ATOM   2244  C  CA    . ILE A 1 280 ? 140.715 129.107 116.828 1.00 16.70 ?  280 ILE A CA    1 
ATOM   2245  C  C     . ILE A 1 280 ? 141.634 129.121 115.617 1.00 15.46 ?  280 ILE A C     1 
ATOM   2246  O  O     . ILE A 1 280 ? 141.462 128.335 114.681 1.00 20.73 ?  280 ILE A O     1 
ATOM   2247  C  CB    . ILE A 1 280 ? 141.198 128.086 117.879 1.00 17.82 ?  280 ILE A CB    1 
ATOM   2248  C  CG1   . ILE A 1 280 ? 141.198 126.663 117.323 1.00 23.63 ?  280 ILE A CG1   1 
ATOM   2249  C  CG2   . ILE A 1 280 ? 140.341 128.159 119.121 1.00 18.85 ?  280 ILE A CG2   1 
ATOM   2250  C  CD1   . ILE A 1 280 ? 142.178 125.753 118.023 1.00 18.27 ?  280 ILE A CD1   1 
ATOM   2251  N  N     . GLY A 1 281 ? 142.587 130.043 115.628 1.00 9.44  ?  281 GLY A N     1 
ATOM   2252  C  CA    . GLY A 1 281 ? 143.623 130.078 114.618 1.00 4.46  ?  281 GLY A CA    1 
ATOM   2253  C  C     . GLY A 1 281 ? 144.984 130.175 115.271 1.00 11.28 ?  281 GLY A C     1 
ATOM   2254  O  O     . GLY A 1 281 ? 145.136 130.723 116.362 1.00 21.39 ?  281 GLY A O     1 
ATOM   2255  N  N     . VAL A 1 282 ? 145.980 129.621 114.590 1.00 18.47 ?  282 VAL A N     1 
ATOM   2256  C  CA    . VAL A 1 282 ? 147.354 129.616 115.073 1.00 16.31 ?  282 VAL A CA    1 
ATOM   2257  C  C     . VAL A 1 282 ? 148.218 130.363 114.070 1.00 14.87 ?  282 VAL A C     1 
ATOM   2258  O  O     . VAL A 1 282 ? 148.199 130.054 112.874 1.00 19.62 ?  282 VAL A O     1 
ATOM   2259  C  CB    . VAL A 1 282 ? 147.880 128.187 115.296 1.00 12.54 ?  282 VAL A CB    1 
ATOM   2260  C  CG1   . VAL A 1 282 ? 149.379 128.203 115.514 1.00 19.43 ?  282 VAL A CG1   1 
ATOM   2261  C  CG2   . VAL A 1 282 ? 147.192 127.562 116.488 1.00 20.97 ?  282 VAL A CG2   1 
ATOM   2262  N  N     . VAL A 1 283 ? 148.968 131.343 114.559 1.00 12.30 ?  283 VAL A N     1 
ATOM   2263  C  CA    . VAL A 1 283 ? 149.874 132.130 113.736 1.00 8.37  ?  283 VAL A CA    1 
ATOM   2264  C  C     . VAL A 1 283 ? 151.257 131.508 113.846 1.00 13.12 ?  283 VAL A C     1 
ATOM   2265  O  O     . VAL A 1 283 ? 151.823 131.420 114.942 1.00 25.22 ?  283 VAL A O     1 
ATOM   2266  C  CB    . VAL A 1 283 ? 149.883 133.602 114.173 1.00 9.54  ?  283 VAL A CB    1 
ATOM   2267  C  CG1   . VAL A 1 283 ? 150.662 134.447 113.185 1.00 12.39 ?  283 VAL A CG1   1 
ATOM   2268  C  CG2   . VAL A 1 283 ? 148.461 134.105 114.312 1.00 9.73  ?  283 VAL A CG2   1 
ATOM   2269  N  N     . ILE A 1 284 ? 151.801 131.072 112.714 1.00 15.63 ?  284 ILE A N     1 
ATOM   2270  C  CA    . ILE A 1 284 ? 153.069 130.349 112.700 1.00 15.39 ?  284 ILE A CA    1 
ATOM   2271  C  C     . ILE A 1 284 ? 154.123 131.159 111.955 1.00 21.61 ?  284 ILE A C     1 
ATOM   2272  O  O     . ILE A 1 284 ? 154.058 131.278 110.724 1.00 21.50 ?  284 ILE A O     1 
ATOM   2273  C  CB    . ILE A 1 284 ? 152.907 128.955 112.076 1.00 15.46 ?  284 ILE A CB    1 
ATOM   2274  C  CG1   . ILE A 1 284 ? 151.739 128.215 112.727 1.00 12.76 ?  284 ILE A CG1   1 
ATOM   2275  C  CG2   . ILE A 1 284 ? 154.190 128.160 112.218 1.00 16.89 ?  284 ILE A CG2   1 
ATOM   2276  C  CD1   . ILE A 1 284 ? 151.554 126.806 112.225 1.00 16.53 ?  284 ILE A CD1   1 
ATOM   2277  N  N     . PRO A 1 285 ? 155.098 131.735 112.651 1.00 25.53 ?  285 PRO A N     1 
ATOM   2278  C  CA    . PRO A 1 285 ? 156.217 132.378 111.957 1.00 25.30 ?  285 PRO A CA    1 
ATOM   2279  C  C     . PRO A 1 285 ? 157.112 131.350 111.283 1.00 25.79 ?  285 PRO A C     1 
ATOM   2280  O  O     . PRO A 1 285 ? 157.100 130.161 111.606 1.00 25.01 ?  285 PRO A O     1 
ATOM   2281  C  CB    . PRO A 1 285 ? 156.961 133.110 113.080 1.00 26.35 ?  285 PRO A CB    1 
ATOM   2282  C  CG    . PRO A 1 285 ? 155.976 133.200 114.204 1.00 23.82 ?  285 PRO A CG    1 
ATOM   2283  C  CD    . PRO A 1 285 ? 155.149 131.964 114.102 1.00 19.89 ?  285 PRO A CD    1 
ATOM   2284  N  N     . ASP A 1 286 ? 157.898 131.835 110.318 1.00 31.22 ?  286 ASP A N     1 
ATOM   2285  C  CA    . ASP A 1 286 ? 158.854 130.976 109.630 1.00 25.97 ?  286 ASP A CA    1 
ATOM   2286  C  C     . ASP A 1 286 ? 159.852 130.345 110.592 1.00 34.55 ?  286 ASP A C     1 
ATOM   2287  O  O     . ASP A 1 286 ? 160.414 129.287 110.282 1.00 35.11 ?  286 ASP A O     1 
ATOM   2288  C  CB    . ASP A 1 286 ? 159.601 131.772 108.560 1.00 27.60 ?  286 ASP A CB    1 
ATOM   2289  C  CG    . ASP A 1 286 ? 159.057 131.531 107.168 1.00 38.61 ?  286 ASP A CG    1 
ATOM   2290  O  OD1   . ASP A 1 286 ? 157.823 131.414 107.022 1.00 42.79 ?  286 ASP A OD1   1 
ATOM   2291  O  OD2   . ASP A 1 286 ? 159.864 131.463 106.218 1.00 42.45 -1 286 ASP A OD2   1 
ATOM   2292  N  N     . LYS A 1 287 ? 160.083 130.972 111.748 1.00 32.80 ?  287 LYS A N     1 
ATOM   2293  C  CA    . LYS A 1 287 ? 160.999 130.409 112.734 1.00 27.94 ?  287 LYS A CA    1 
ATOM   2294  C  C     . LYS A 1 287 ? 160.518 129.053 113.230 1.00 27.59 ?  287 LYS A C     1 
ATOM   2295  O  O     . LYS A 1 287 ? 161.319 128.128 113.393 1.00 35.74 ?  287 LYS A O     1 
ATOM   2296  C  CB    . LYS A 1 287 ? 161.167 131.379 113.904 1.00 28.97 ?  287 LYS A CB    1 
ATOM   2297  C  CG    . LYS A 1 287 ? 162.282 130.998 114.862 1.00 27.77 ?  287 LYS A CG    1 
ATOM   2298  C  CD    . LYS A 1 287 ? 163.585 130.790 114.116 1.00 31.66 ?  287 LYS A CD    1 
ATOM   2299  C  CE    . LYS A 1 287 ? 164.720 130.458 115.062 1.00 32.61 ?  287 LYS A CE    1 
ATOM   2300  N  NZ    . LYS A 1 287 ? 166.031 130.431 114.361 1.00 33.85 1  287 LYS A NZ    1 
ATOM   2301  N  N     . PHE A 1 288 ? 159.215 128.918 113.490 1.00 27.34 ?  288 PHE A N     1 
ATOM   2302  C  CA    . PHE A 1 288 ? 158.690 127.642 113.966 1.00 22.62 ?  288 PHE A CA    1 
ATOM   2303  C  C     . PHE A 1 288 ? 158.844 126.549 112.916 1.00 25.80 ?  288 PHE A C     1 
ATOM   2304  O  O     . PHE A 1 288 ? 159.210 125.413 113.243 1.00 34.63 ?  288 PHE A O     1 
ATOM   2305  C  CB    . PHE A 1 288 ? 157.225 127.791 114.368 1.00 24.92 ?  288 PHE A CB    1 
ATOM   2306  C  CG    . PHE A 1 288 ? 156.648 126.565 115.012 1.00 27.45 ?  288 PHE A CG    1 
ATOM   2307  C  CD1   . PHE A 1 288 ? 156.811 126.338 116.367 1.00 23.19 ?  288 PHE A CD1   1 
ATOM   2308  C  CD2   . PHE A 1 288 ? 155.951 125.635 114.262 1.00 26.73 ?  288 PHE A CD2   1 
ATOM   2309  C  CE1   . PHE A 1 288 ? 156.287 125.212 116.961 1.00 27.14 ?  288 PHE A CE1   1 
ATOM   2310  C  CE2   . PHE A 1 288 ? 155.425 124.505 114.852 1.00 24.01 ?  288 PHE A CE2   1 
ATOM   2311  C  CZ    . PHE A 1 288 ? 155.592 124.296 116.201 1.00 27.79 ?  288 PHE A CZ    1 
ATOM   2312  N  N     . VAL A 1 289 ? 158.558 126.869 111.654 1.00 32.00 ?  289 VAL A N     1 
ATOM   2313  C  CA    . VAL A 1 289 ? 158.702 125.884 110.587 1.00 29.47 ?  289 VAL A CA    1 
ATOM   2314  C  C     . VAL A 1 289 ? 160.163 125.490 110.423 1.00 30.02 ?  289 VAL A C     1 
ATOM   2315  O  O     . VAL A 1 289 ? 160.483 124.321 110.184 1.00 35.14 ?  289 VAL A O     1 
ATOM   2316  C  CB    . VAL A 1 289 ? 158.108 126.428 109.275 1.00 30.34 ?  289 VAL A CB    1 
ATOM   2317  C  CG1   . VAL A 1 289 ? 158.281 125.421 108.151 1.00 30.45 ?  289 VAL A CG1   1 
ATOM   2318  C  CG2   . VAL A 1 289 ? 156.642 126.777 109.466 1.00 23.88 ?  289 VAL A CG2   1 
ATOM   2319  N  N     . GLU A 1 290 ? 161.073 126.459 110.552 1.00 37.54 ?  290 GLU A N     1 
ATOM   2320  C  CA    . GLU A 1 290 ? 162.496 126.149 110.482 1.00 34.55 ?  290 GLU A CA    1 
ATOM   2321  C  C     . GLU A 1 290 ? 162.926 125.251 111.637 1.00 35.20 ?  290 GLU A C     1 
ATOM   2322  O  O     . GLU A 1 290 ? 163.693 124.302 111.443 1.00 41.82 ?  290 GLU A O     1 
ATOM   2323  C  CB    . GLU A 1 290 ? 163.310 127.445 110.466 1.00 34.45 ?  290 GLU A CB    1 
ATOM   2324  C  CG    . GLU A 1 290 ? 164.657 127.353 111.160 1.00 39.30 ?  290 GLU A CG    1 
ATOM   2325  C  CD    . GLU A 1 290 ? 165.403 128.672 111.155 1.00 45.41 ?  290 GLU A CD    1 
ATOM   2326  O  OE1   . GLU A 1 290 ? 164.741 129.731 111.157 1.00 46.66 ?  290 GLU A OE1   1 
ATOM   2327  O  OE2   . GLU A 1 290 ? 166.651 128.651 111.150 1.00 43.61 -1 290 GLU A OE2   1 
ATOM   2328  N  N     . LEU A 1 291 ? 162.438 125.534 112.848 1.00 28.22 ?  291 LEU A N     1 
ATOM   2329  C  CA    . LEU A 1 291 ? 162.790 124.719 114.006 1.00 26.89 ?  291 LEU A CA    1 
ATOM   2330  C  C     . LEU A 1 291 ? 162.267 123.296 113.862 1.00 35.32 ?  291 LEU A C     1 
ATOM   2331  O  O     . LEU A 1 291 ? 162.964 122.334 114.202 1.00 38.89 ?  291 LEU A O     1 
ATOM   2332  C  CB    . LEU A 1 291 ? 162.246 125.358 115.284 1.00 31.08 ?  291 LEU A CB    1 
ATOM   2333  C  CG    . LEU A 1 291 ? 162.930 126.636 115.766 1.00 33.94 ?  291 LEU A CG    1 
ATOM   2334  C  CD1   . LEU A 1 291 ? 162.069 127.347 116.794 1.00 28.25 ?  291 LEU A CD1   1 
ATOM   2335  C  CD2   . LEU A 1 291 ? 164.302 126.330 116.331 1.00 31.72 ?  291 LEU A CD2   1 
ATOM   2336  N  N     . ALA A 1 292 ? 161.035 123.145 113.372 1.00 37.20 ?  292 ALA A N     1 
ATOM   2337  C  CA    . ALA A 1 292 ? 160.488 121.809 113.155 1.00 30.50 ?  292 ALA A CA    1 
ATOM   2338  C  C     . ALA A 1 292 ? 161.232 121.082 112.041 1.00 32.10 ?  292 ALA A C     1 
ATOM   2339  O  O     . ALA A 1 292 ? 161.426 119.864 112.108 1.00 35.83 ?  292 ALA A O     1 
ATOM   2340  C  CB    . ALA A 1 292 ? 158.997 121.899 112.839 1.00 26.04 ?  292 ALA A CB    1 
ATOM   2341  N  N     . ARG A 1 293 ? 161.652 121.815 111.007 1.00 32.95 ?  293 ARG A N     1 
ATOM   2342  C  CA    . ARG A 1 293 ? 162.377 121.204 109.899 1.00 33.13 ?  293 ARG A CA    1 
ATOM   2343  C  C     . ARG A 1 293 ? 163.708 120.626 110.357 1.00 39.16 ?  293 ARG A C     1 
ATOM   2344  O  O     . ARG A 1 293 ? 164.097 119.530 109.935 1.00 41.45 ?  293 ARG A O     1 
ATOM   2345  C  CB    . ARG A 1 293 ? 162.587 122.233 108.789 1.00 34.94 ?  293 ARG A CB    1 
ATOM   2346  C  CG    . ARG A 1 293 ? 163.455 121.759 107.640 1.00 35.23 ?  293 ARG A CG    1 
ATOM   2347  C  CD    . ARG A 1 293 ? 163.880 122.927 106.774 1.00 37.62 ?  293 ARG A CD    1 
ATOM   2348  N  NE    . ARG A 1 293 ? 162.759 123.809 106.476 1.00 42.26 ?  293 ARG A NE    1 
ATOM   2349  C  CZ    . ARG A 1 293 ? 162.787 125.127 106.615 1.00 40.70 ?  293 ARG A CZ    1 
ATOM   2350  N  NH1   . ARG A 1 293 ? 163.867 125.754 107.049 1.00 41.69 1  293 ARG A NH1   1 
ATOM   2351  N  NH2   . ARG A 1 293 ? 161.702 125.835 106.310 1.00 35.59 ?  293 ARG A NH2   1 
ATOM   2352  N  N     . GLU A 1 294 ? 164.420 121.343 111.222 1.00 44.74 ?  294 GLU A N     1 
ATOM   2353  C  CA    . GLU A 1 294 ? 165.706 120.887 111.732 1.00 43.18 ?  294 GLU A CA    1 
ATOM   2354  C  C     . GLU A 1 294 ? 165.570 119.932 112.908 1.00 44.44 ?  294 GLU A C     1 
ATOM   2355  O  O     . GLU A 1 294 ? 166.592 119.453 113.413 1.00 48.04 ?  294 GLU A O     1 
ATOM   2356  C  CB    . GLU A 1 294 ? 166.563 122.089 112.137 1.00 41.64 ?  294 GLU A CB    1 
ATOM   2357  C  CG    . GLU A 1 294 ? 166.685 123.151 111.057 1.00 43.84 ?  294 GLU A CG    1 
ATOM   2358  C  CD    . GLU A 1 294 ? 167.003 124.521 111.621 1.00 52.67 ?  294 GLU A CD    1 
ATOM   2359  O  OE1   . GLU A 1 294 ? 166.558 124.819 112.749 1.00 50.44 ?  294 GLU A OE1   1 
ATOM   2360  O  OE2   . GLU A 1 294 ? 167.697 125.302 110.937 1.00 51.67 -1 294 GLU A OE2   1 
ATOM   2361  N  N     . ASP A 1 295 ? 164.343 119.651 113.352 1.00 44.22 ?  295 ASP A N     1 
ATOM   2362  C  CA    . ASP A 1 295 ? 164.079 118.769 114.490 1.00 43.82 ?  295 ASP A CA    1 
ATOM   2363  C  C     . ASP A 1 295 ? 164.759 119.270 115.759 1.00 48.16 ?  295 ASP A C     1 
ATOM   2364  O  O     . ASP A 1 295 ? 165.101 118.486 116.647 1.00 51.21 ?  295 ASP A O     1 
ATOM   2365  C  CB    . ASP A 1 295 ? 164.497 117.327 114.192 1.00 46.89 ?  295 ASP A CB    1 
ATOM   2366  C  CG    . ASP A 1 295 ? 163.547 116.309 114.793 1.00 51.48 ?  295 ASP A CG    1 
ATOM   2367  O  OD1   . ASP A 1 295 ? 162.804 116.668 115.730 1.00 49.59 ?  295 ASP A OD1   1 
ATOM   2368  O  OD2   . ASP A 1 295 ? 163.541 115.150 114.327 1.00 50.75 -1 295 ASP A OD2   1 
ATOM   2369  N  N     . LYS A 1 296 ? 164.958 120.581 115.853 1.00 45.61 ?  296 LYS A N     1 
ATOM   2370  C  CA    . LYS A 1 296 ? 165.576 121.178 117.022 1.00 45.38 ?  296 LYS A CA    1 
ATOM   2371  C  C     . LYS A 1 296 ? 164.542 121.363 118.129 1.00 44.84 ?  296 LYS A C     1 
ATOM   2372  O  O     . LYS A 1 296 ? 163.342 121.159 117.938 1.00 45.52 ?  296 LYS A O     1 
ATOM   2373  C  CB    . LYS A 1 296 ? 166.227 122.511 116.658 1.00 45.77 ?  296 LYS A CB    1 
ATOM   2374  C  CG    . LYS A 1 296 ? 167.428 122.370 115.738 1.00 45.88 ?  296 LYS A CG    1 
ATOM   2375  C  CD    . LYS A 1 296 ? 168.069 123.713 115.448 1.00 46.45 ?  296 LYS A CD    1 
ATOM   2376  C  CE    . LYS A 1 296 ? 169.413 123.537 114.759 1.00 45.56 ?  296 LYS A CE    1 
ATOM   2377  N  NZ    . LYS A 1 296 ? 169.939 124.824 114.224 1.00 46.99 1  296 LYS A NZ    1 
ATOM   2378  N  N     . ALA A 1 297 ? 165.024 121.747 119.306 1.00 46.02 ?  297 ALA A N     1 
ATOM   2379  C  CA    . ALA A 1 297 ? 164.147 121.990 120.443 1.00 44.58 ?  297 ALA A CA    1 
ATOM   2380  C  C     . ALA A 1 297 ? 163.664 123.433 120.413 1.00 44.70 ?  297 ALA A C     1 
ATOM   2381  O  O     . ALA A 1 297 ? 164.458 124.364 120.582 1.00 46.57 ?  297 ALA A O     1 
ATOM   2382  C  CB    . ALA A 1 297 ? 164.873 121.691 121.752 1.00 44.33 ?  297 ALA A CB    1 
ATOM   2383  N  N     . ALA A 1 298 ? 162.367 123.618 120.195 1.00 38.12 ?  298 ALA A N     1 
ATOM   2384  C  CA    . ALA A 1 298 ? 161.777 124.945 120.181 1.00 36.96 ?  298 ALA A CA    1 
ATOM   2385  C  C     . ALA A 1 298 ? 161.352 125.348 121.589 1.00 35.89 ?  298 ALA A C     1 
ATOM   2386  O  O     . ALA A 1 298 ? 161.267 124.526 122.503 1.00 36.72 ?  298 ALA A O     1 
ATOM   2387  C  CB    . ALA A 1 298 ? 160.586 124.996 119.226 1.00 36.58 ?  298 ALA A CB    1 
ATOM   2388  N  N     . TYR A 1 299 ? 161.085 126.639 121.759 1.00 35.49 ?  299 TYR A N     1 
ATOM   2389  C  CA    . TYR A 1 299 ? 160.672 127.185 123.043 1.00 28.47 ?  299 TYR A CA    1 
ATOM   2390  C  C     . TYR A 1 299 ? 159.452 128.068 122.847 1.00 31.38 ?  299 TYR A C     1 
ATOM   2391  O  O     . TYR A 1 299 ? 159.441 128.928 121.962 1.00 40.14 ?  299 TYR A O     1 
ATOM   2392  C  CB    . TYR A 1 299 ? 161.801 127.993 123.690 1.00 34.24 ?  299 TYR A CB    1 
ATOM   2393  C  CG    . TYR A 1 299 ? 162.826 127.152 124.407 1.00 37.70 ?  299 TYR A CG    1 
ATOM   2394  C  CD1   . TYR A 1 299 ? 162.632 126.760 125.721 1.00 35.43 ?  299 TYR A CD1   1 
ATOM   2395  C  CD2   . TYR A 1 299 ? 163.997 126.762 123.773 1.00 37.20 ?  299 TYR A CD2   1 
ATOM   2396  C  CE1   . TYR A 1 299 ? 163.567 125.997 126.383 1.00 35.26 ?  299 TYR A CE1   1 
ATOM   2397  C  CE2   . TYR A 1 299 ? 164.939 125.997 124.425 1.00 37.25 ?  299 TYR A CE2   1 
ATOM   2398  C  CZ    . TYR A 1 299 ? 164.719 125.617 125.732 1.00 40.47 ?  299 TYR A CZ    1 
ATOM   2399  O  OH    . TYR A 1 299 ? 165.653 124.854 126.393 1.00 45.23 ?  299 TYR A OH    1 
ATOM   2400  N  N     . VAL A 1 300 ? 158.433 127.853 123.660 1.00 31.06 ?  300 VAL A N     1 
ATOM   2401  C  CA    . VAL A 1 300 ? 157.326 128.792 123.772 1.00 24.27 ?  300 VAL A CA    1 
ATOM   2402  C  C     . VAL A 1 300 ? 157.638 129.735 124.922 1.00 29.18 ?  300 VAL A C     1 
ATOM   2403  O  O     . VAL A 1 300 ? 158.315 129.368 125.887 1.00 29.35 ?  300 VAL A O     1 
ATOM   2404  C  CB    . VAL A 1 300 ? 155.979 128.068 123.974 1.00 26.12 ?  300 VAL A CB    1 
ATOM   2405  C  CG1   . VAL A 1 300 ? 155.583 127.328 122.709 1.00 29.40 ?  300 VAL A CG1   1 
ATOM   2406  C  CG2   . VAL A 1 300 ? 156.055 127.117 125.154 1.00 29.28 ?  300 VAL A CG2   1 
ATOM   2407  N  N     . PHE A 1 301 ? 157.153 130.966 124.826 1.00 27.32 ?  301 PHE A N     1 
ATOM   2408  C  CA    . PHE A 1 301 ? 157.577 132.025 125.724 1.00 25.15 ?  301 PHE A CA    1 
ATOM   2409  C  C     . PHE A 1 301 ? 156.400 132.594 126.499 1.00 25.22 ?  301 PHE A C     1 
ATOM   2410  O  O     . PHE A 1 301 ? 155.252 132.554 126.046 1.00 31.04 ?  301 PHE A O     1 
ATOM   2411  C  CB    . PHE A 1 301 ? 158.278 133.146 124.954 1.00 27.97 ?  301 PHE A CB    1 
ATOM   2412  C  CG    . PHE A 1 301 ? 159.435 132.672 124.130 1.00 31.39 ?  301 PHE A CG    1 
ATOM   2413  C  CD1   . PHE A 1 301 ? 160.665 132.436 124.715 1.00 29.04 ?  301 PHE A CD1   1 
ATOM   2414  C  CD2   . PHE A 1 301 ? 159.291 132.454 122.773 1.00 26.23 ?  301 PHE A CD2   1 
ATOM   2415  C  CE1   . PHE A 1 301 ? 161.730 131.994 123.963 1.00 31.76 ?  301 PHE A CE1   1 
ATOM   2416  C  CE2   . PHE A 1 301 ? 160.353 132.014 122.017 1.00 28.48 ?  301 PHE A CE2   1 
ATOM   2417  C  CZ    . PHE A 1 301 ? 161.574 131.785 122.613 1.00 32.52 ?  301 PHE A CZ    1 
ATOM   2418  N  N     . TYR A 1 302 ? 156.706 133.119 127.684 1.00 26.97 ?  302 TYR A N     1 
ATOM   2419  C  CA    . TYR A 1 302 ? 155.729 133.829 128.493 1.00 27.45 ?  302 TYR A CA    1 
ATOM   2420  C  C     . TYR A 1 302 ? 155.698 135.274 128.023 1.00 30.56 ?  302 TYR A C     1 
ATOM   2421  O  O     . TYR A 1 302 ? 156.708 135.980 128.166 1.00 29.62 ?  302 TYR A O     1 
ATOM   2422  C  CB    . TYR A 1 302 ? 156.093 133.751 129.967 1.00 28.30 ?  302 TYR A CB    1 
ATOM   2423  C  CG    . TYR A 1 302 ? 155.897 132.383 130.584 1.00 26.25 ?  302 TYR A CG    1 
ATOM   2424  C  CD1   . TYR A 1 302 ? 156.741 131.330 130.266 1.00 27.65 ?  302 TYR A CD1   1 
ATOM   2425  C  CD2   . TYR A 1 302 ? 154.874 132.151 131.490 1.00 27.48 ?  302 TYR A CD2   1 
ATOM   2426  C  CE1   . TYR A 1 302 ? 156.567 130.083 130.827 1.00 30.31 ?  302 TYR A CE1   1 
ATOM   2427  C  CE2   . TYR A 1 302 ? 154.694 130.908 132.059 1.00 30.14 ?  302 TYR A CE2   1 
ATOM   2428  C  CZ    . TYR A 1 302 ? 155.544 129.878 131.725 1.00 33.71 ?  302 TYR A CZ    1 
ATOM   2429  O  OH    . TYR A 1 302 ? 155.367 128.636 132.288 1.00 37.78 ?  302 TYR A OH    1 
ATOM   2430  N  N     . PRO A 1 303 ? 154.590 135.753 127.453 1.00 29.03 ?  303 PRO A N     1 
ATOM   2431  C  CA    . PRO A 1 303 ? 154.594 137.096 126.849 1.00 24.96 ?  303 PRO A CA    1 
ATOM   2432  C  C     . PRO A 1 303 ? 154.896 138.217 127.825 1.00 27.56 ?  303 PRO A C     1 
ATOM   2433  O  O     . PRO A 1 303 ? 155.523 139.210 127.434 1.00 30.61 ?  303 PRO A O     1 
ATOM   2434  C  CB    . PRO A 1 303 ? 153.174 137.224 126.278 1.00 24.83 ?  303 PRO A CB    1 
ATOM   2435  C  CG    . PRO A 1 303 ? 152.678 135.835 126.166 1.00 24.18 ?  303 PRO A CG    1 
ATOM   2436  C  CD    . PRO A 1 303 ? 153.299 135.073 127.283 1.00 25.44 ?  303 PRO A CD    1 
ATOM   2437  N  N     . HIS A 1 304 ? 154.463 138.099 129.082 1.00 32.27 ?  304 HIS A N     1 
ATOM   2438  C  CA    . HIS A 1 304 ? 154.682 139.186 130.028 1.00 27.96 ?  304 HIS A CA    1 
ATOM   2439  C  C     . HIS A 1 304 ? 156.156 139.357 130.360 1.00 32.41 ?  304 HIS A C     1 
ATOM   2440  O  O     . HIS A 1 304 ? 156.614 140.485 130.555 1.00 40.50 ?  304 HIS A O     1 
ATOM   2441  C  CB    . HIS A 1 304 ? 153.881 138.960 131.306 1.00 29.89 ?  304 HIS A CB    1 
ATOM   2442  C  CG    . HIS A 1 304 ? 153.766 140.183 132.160 1.00 32.74 ?  304 HIS A CG    1 
ATOM   2443  N  ND1   . HIS A 1 304 ? 153.509 141.431 131.637 1.00 31.93 ?  304 HIS A ND1   1 
ATOM   2444  C  CD2   . HIS A 1 304 ? 153.882 140.353 133.498 1.00 35.88 ?  304 HIS A CD2   1 
ATOM   2445  C  CE1   . HIS A 1 304 ? 153.467 142.317 132.615 1.00 33.55 ?  304 HIS A CE1   1 
ATOM   2446  N  NE2   . HIS A 1 304 ? 153.689 141.689 133.754 1.00 34.35 ?  304 HIS A NE2   1 
ATOM   2447  N  N     . THR A 1 305 ? 156.910 138.259 130.431 1.00 25.74 ?  305 THR A N     1 
ATOM   2448  C  CA    . THR A 1 305 ? 158.346 138.372 130.660 1.00 29.41 ?  305 THR A CA    1 
ATOM   2449  C  C     . THR A 1 305 ? 159.030 139.103 129.512 1.00 28.69 ?  305 THR A C     1 
ATOM   2450  O  O     . THR A 1 305 ? 159.897 139.956 129.736 1.00 37.07 ?  305 THR A O     1 
ATOM   2451  C  CB    . THR A 1 305 ? 158.955 136.986 130.855 1.00 33.48 ?  305 THR A CB    1 
ATOM   2452  O  OG1   . THR A 1 305 ? 158.817 136.228 129.648 1.00 32.73 ?  305 THR A OG1   1 
ATOM   2453  C  CG2   . THR A 1 305 ? 158.252 136.260 131.986 1.00 30.50 ?  305 THR A CG2   1 
ATOM   2454  N  N     . ILE A 1 306 ? 158.643 138.791 128.274 1.00 32.69 ?  306 ILE A N     1 
ATOM   2455  C  CA    . ILE A 1 306 ? 159.213 139.481 127.120 1.00 28.02 ?  306 ILE A CA    1 
ATOM   2456  C  C     . ILE A 1 306 ? 158.842 140.957 127.143 1.00 29.49 ?  306 ILE A C     1 
ATOM   2457  O  O     . ILE A 1 306 ? 159.675 141.824 126.858 1.00 35.55 ?  306 ILE A O     1 
ATOM   2458  C  CB    . ILE A 1 306 ? 158.759 138.801 125.816 1.00 30.36 ?  306 ILE A CB    1 
ATOM   2459  C  CG1   . ILE A 1 306 ? 159.412 137.427 125.679 1.00 28.05 ?  306 ILE A CG1   1 
ATOM   2460  C  CG2   . ILE A 1 306 ? 159.093 139.664 124.611 1.00 30.85 ?  306 ILE A CG2   1 
ATOM   2461  C  CD1   . ILE A 1 306 ? 158.912 136.638 124.505 1.00 31.24 ?  306 ILE A CD1   1 
ATOM   2462  N  N     . TYR A 1 307 ? 157.588 141.269 127.475 1.00 33.59 ?  307 TYR A N     1 
ATOM   2463  C  CA    . TYR A 1 307 ? 157.169 142.666 127.526 1.00 31.54 ?  307 TYR A CA    1 
ATOM   2464  C  C     . TYR A 1 307 ? 157.914 143.431 128.614 1.00 35.23 ?  307 TYR A C     1 
ATOM   2465  O  O     . TYR A 1 307 ? 158.307 144.585 128.409 1.00 36.72 ?  307 TYR A O     1 
ATOM   2466  C  CB    . TYR A 1 307 ? 155.659 142.754 127.744 1.00 29.33 ?  307 TYR A CB    1 
ATOM   2467  C  CG    . TYR A 1 307 ? 155.127 144.167 127.714 1.00 33.59 ?  307 TYR A CG    1 
ATOM   2468  C  CD1   . TYR A 1 307 ? 154.838 144.793 126.511 1.00 29.32 ?  307 TYR A CD1   1 
ATOM   2469  C  CD2   . TYR A 1 307 ? 154.914 144.874 128.889 1.00 34.47 ?  307 TYR A CD2   1 
ATOM   2470  C  CE1   . TYR A 1 307 ? 154.355 146.084 126.477 1.00 33.46 ?  307 TYR A CE1   1 
ATOM   2471  C  CE2   . TYR A 1 307 ? 154.431 146.166 128.865 1.00 34.77 ?  307 TYR A CE2   1 
ATOM   2472  C  CZ    . TYR A 1 307 ? 154.153 146.765 127.656 1.00 35.97 ?  307 TYR A CZ    1 
ATOM   2473  O  OH    . TYR A 1 307 ? 153.670 148.052 127.626 1.00 38.80 ?  307 TYR A OH    1 
ATOM   2474  N  N     . LYS A 1 308 ? 158.107 142.810 129.779 1.00 35.92 ?  308 LYS A N     1 
ATOM   2475  C  CA    . LYS A 1 308 ? 158.846 143.460 130.855 1.00 33.02 ?  308 LYS A CA    1 
ATOM   2476  C  C     . LYS A 1 308 ? 160.306 143.669 130.476 1.00 32.74 ?  308 LYS A C     1 
ATOM   2477  O  O     . LYS A 1 308 ? 160.886 144.721 130.770 1.00 39.07 ?  308 LYS A O     1 
ATOM   2478  C  CB    . LYS A 1 308 ? 158.739 142.632 132.136 1.00 34.34 ?  308 LYS A CB    1 
ATOM   2479  C  CG    . LYS A 1 308 ? 157.376 142.692 132.802 1.00 34.02 ?  308 LYS A CG    1 
ATOM   2480  C  CD    . LYS A 1 308 ? 157.384 141.981 134.143 1.00 34.74 ?  308 LYS A CD    1 
ATOM   2481  C  CE    . LYS A 1 308 ? 157.910 140.561 134.018 1.00 38.99 ?  308 LYS A CE    1 
ATOM   2482  N  NZ    . LYS A 1 308 ? 156.893 139.553 134.424 1.00 36.46 1  308 LYS A NZ    1 
ATOM   2483  N  N     . GLU A 1 309 ? 160.916 142.680 129.823 1.00 30.34 ?  309 GLU A N     1 
ATOM   2484  C  CA    . GLU A 1 309 ? 162.337 142.762 129.511 1.00 35.08 ?  309 GLU A CA    1 
ATOM   2485  C  C     . GLU A 1 309 ? 162.622 143.731 128.369 1.00 36.49 ?  309 GLU A C     1 
ATOM   2486  O  O     . GLU A 1 309 ? 163.607 144.476 128.419 1.00 39.85 ?  309 GLU A O     1 
ATOM   2487  C  CB    . GLU A 1 309 ? 162.872 141.369 129.177 1.00 32.16 ?  309 GLU A CB    1 
ATOM   2488  C  CG    . GLU A 1 309 ? 164.281 141.360 128.624 1.00 36.68 ?  309 GLU A CG    1 
ATOM   2489  C  CD    . GLU A 1 309 ? 165.325 141.675 129.671 1.00 43.34 ?  309 GLU A CD    1 
ATOM   2490  O  OE1   . GLU A 1 309 ? 164.987 141.665 130.873 1.00 44.25 ?  309 GLU A OE1   1 
ATOM   2491  O  OE2   . GLU A 1 309 ? 166.486 141.935 129.293 1.00 42.50 -1 309 GLU A OE2   1 
ATOM   2492  N  N     . TYR A 1 310 ? 161.776 143.744 127.340 1.00 34.65 ?  310 TYR A N     1 
ATOM   2493  C  CA    . TYR A 1 310 ? 162.057 144.487 126.121 1.00 35.73 ?  310 TYR A CA    1 
ATOM   2494  C  C     . TYR A 1 310 ? 161.159 145.696 125.912 1.00 33.98 ?  310 TYR A C     1 
ATOM   2495  O  O     . TYR A 1 310 ? 161.466 146.528 125.053 1.00 35.70 ?  310 TYR A O     1 
ATOM   2496  C  CB    . TYR A 1 310 ? 161.939 143.558 124.904 1.00 34.26 ?  310 TYR A CB    1 
ATOM   2497  C  CG    . TYR A 1 310 ? 162.967 142.453 124.889 1.00 34.23 ?  310 TYR A CG    1 
ATOM   2498  C  CD1   . TYR A 1 310 ? 164.228 142.660 124.349 1.00 33.53 ?  310 TYR A CD1   1 
ATOM   2499  C  CD2   . TYR A 1 310 ? 162.680 141.206 125.424 1.00 32.13 ?  310 TYR A CD2   1 
ATOM   2500  C  CE1   . TYR A 1 310 ? 165.170 141.654 124.337 1.00 36.62 ?  310 TYR A CE1   1 
ATOM   2501  C  CE2   . TYR A 1 310 ? 163.616 140.195 125.418 1.00 33.39 ?  310 TYR A CE2   1 
ATOM   2502  C  CZ    . TYR A 1 310 ? 164.860 140.425 124.873 1.00 36.69 ?  310 TYR A CZ    1 
ATOM   2503  O  OH    . TYR A 1 310 ? 165.796 139.421 124.863 1.00 35.81 ?  310 TYR A OH    1 
ATOM   2504  N  N     . GLY A 1 311 ? 160.068 145.820 126.661 1.00 31.00 ?  311 GLY A N     1 
ATOM   2505  C  CA    . GLY A 1 311 ? 159.156 146.927 126.482 1.00 32.53 ?  311 GLY A CA    1 
ATOM   2506  C  C     . GLY A 1 311 ? 158.191 146.780 125.328 1.00 35.66 ?  311 GLY A C     1 
ATOM   2507  O  O     . GLY A 1 311 ? 157.389 147.692 125.094 1.00 39.25 ?  311 GLY A O     1 
ATOM   2508  N  N     . GLN A 1 312 ? 158.242 145.668 124.600 1.00 36.16 ?  312 GLN A N     1 
ATOM   2509  C  CA    . GLN A 1 312 ? 157.347 145.410 123.486 1.00 32.63 ?  312 GLN A CA    1 
ATOM   2510  C  C     . GLN A 1 312 ? 156.705 144.043 123.665 1.00 33.64 ?  312 GLN A C     1 
ATOM   2511  O  O     . GLN A 1 312 ? 157.274 143.153 124.299 1.00 38.49 ?  312 GLN A O     1 
ATOM   2512  C  CB    . GLN A 1 312 ? 158.084 145.457 122.141 1.00 32.24 ?  312 GLN A CB    1 
ATOM   2513  C  CG    . GLN A 1 312 ? 158.772 146.774 121.846 1.00 35.80 ?  312 GLN A CG    1 
ATOM   2514  C  CD    . GLN A 1 312 ? 160.067 146.591 121.080 1.00 40.31 ?  312 GLN A CD    1 
ATOM   2515  O  OE1   . GLN A 1 312 ? 160.088 146.659 119.851 1.00 39.60 ?  312 GLN A OE1   1 
ATOM   2516  N  NE2   . GLN A 1 312 ? 161.155 146.356 121.802 1.00 37.60 ?  312 GLN A NE2   1 
ATOM   2517  N  N     . HIS A 1 313 ? 155.511 143.889 123.101 1.00 30.44 ?  313 HIS A N     1 
ATOM   2518  C  CA    . HIS A 1 313 ? 154.851 142.596 123.106 1.00 28.09 ?  313 HIS A CA    1 
ATOM   2519  C  C     . HIS A 1 313 ? 155.606 141.617 122.211 1.00 32.02 ?  313 HIS A C     1 
ATOM   2520  O  O     . HIS A 1 313 ? 156.314 142.004 121.278 1.00 32.61 ?  313 HIS A O     1 
ATOM   2521  C  CB    . HIS A 1 313 ? 153.403 142.729 122.641 1.00 25.78 ?  313 HIS A CB    1 
ATOM   2522  C  CG    . HIS A 1 313 ? 152.553 143.569 123.544 1.00 31.16 ?  313 HIS A CG    1 
ATOM   2523  N  ND1   . HIS A 1 313 ? 152.074 143.112 124.752 1.00 29.95 ?  313 HIS A ND1   1 
ATOM   2524  C  CD2   . HIS A 1 313 ? 152.095 144.836 123.413 1.00 30.97 ?  313 HIS A CD2   1 
ATOM   2525  C  CE1   . HIS A 1 313 ? 151.358 144.061 125.326 1.00 29.39 ?  313 HIS A CE1   1 
ATOM   2526  N  NE2   . HIS A 1 313 ? 151.355 145.117 124.535 1.00 31.94 ?  313 HIS A NE2   1 
ATOM   2527  N  N     . MET A 1 314 ? 155.456 140.327 122.519 1.00 35.83 ?  314 MET A N     1 
ATOM   2528  C  CA    . MET A 1 314 ? 156.161 139.304 121.754 1.00 29.72 ?  314 MET A CA    1 
ATOM   2529  C  C     . MET A 1 314 ? 155.706 139.284 120.300 1.00 35.52 ?  314 MET A C     1 
ATOM   2530  O  O     . MET A 1 314 ? 156.531 139.172 119.386 1.00 38.07 ?  314 MET A O     1 
ATOM   2531  C  CB    . MET A 1 314 ? 155.958 137.931 122.393 1.00 27.22 ?  314 MET A CB    1 
ATOM   2532  C  CG    . MET A 1 314 ? 156.587 136.796 121.605 1.00 32.36 ?  314 MET A CG    1 
ATOM   2533  S  SD    . MET A 1 314 ? 156.353 135.164 122.332 1.00 41.78 ?  314 MET A SD    1 
ATOM   2534  C  CE    . MET A 1 314 ? 154.997 135.476 123.451 1.00 30.24 ?  314 MET A CE    1 
ATOM   2535  N  N     . ASP A 1 315 ? 154.398 139.395 120.064 1.00 33.93 ?  315 ASP A N     1 
ATOM   2536  C  CA    . ASP A 1 315 ? 153.884 139.354 118.702 1.00 38.13 ?  315 ASP A CA    1 
ATOM   2537  C  C     . ASP A 1 315 ? 154.139 140.644 117.934 1.00 31.39 ?  315 ASP A C     1 
ATOM   2538  O  O     . ASP A 1 315 ? 153.956 140.663 116.713 1.00 39.47 ?  315 ASP A O     1 
ATOM   2539  C  CB    . ASP A 1 315 ? 152.384 139.045 118.707 1.00 31.26 ?  315 ASP A CB    1 
ATOM   2540  C  CG    . ASP A 1 315 ? 151.604 139.968 119.611 1.00 35.74 ?  315 ASP A CG    1 
ATOM   2541  O  OD1   . ASP A 1 315 ? 152.193 140.478 120.585 1.00 39.29 ?  315 ASP A OD1   1 
ATOM   2542  O  OD2   . ASP A 1 315 ? 150.403 140.184 119.346 1.00 32.58 -1 315 ASP A OD2   1 
ATOM   2543  N  N     . GLU A 1 316 ? 154.551 141.711 118.611 1.00 24.36 ?  316 GLU A N     1 
ATOM   2544  C  CA    . GLU A 1 316 ? 154.968 142.934 117.941 1.00 28.82 ?  316 GLU A CA    1 
ATOM   2545  C  C     . GLU A 1 316 ? 156.434 142.905 117.535 1.00 33.83 ?  316 GLU A C     1 
ATOM   2546  O  O     . GLU A 1 316 ? 156.912 143.870 116.929 1.00 32.98 ?  316 GLU A O     1 
ATOM   2547  C  CB    . GLU A 1 316 ? 154.708 144.144 118.842 1.00 31.77 ?  316 GLU A CB    1 
ATOM   2548  C  CG    . GLU A 1 316 ? 153.241 144.389 119.138 1.00 31.04 ?  316 GLU A CG    1 
ATOM   2549  C  CD    . GLU A 1 316 ? 152.577 145.269 118.100 1.00 38.93 ?  316 GLU A CD    1 
ATOM   2550  O  OE1   . GLU A 1 316 ? 151.433 145.710 118.335 1.00 41.23 ?  316 GLU A OE1   1 
ATOM   2551  O  OE2   . GLU A 1 316 ? 153.201 145.522 117.048 1.00 41.62 -1 316 GLU A OE2   1 
ATOM   2552  N  N     . MET A 1 317 ? 157.152 141.835 117.854 1.00 39.09 ?  317 MET A N     1 
ATOM   2553  C  CA    . MET A 1 317 ? 158.564 141.696 117.546 1.00 35.78 ?  317 MET A CA    1 
ATOM   2554  C  C     . MET A 1 317 ? 158.767 140.619 116.489 1.00 34.44 ?  317 MET A C     1 
ATOM   2555  O  O     . MET A 1 317 ? 157.918 139.748 116.285 1.00 36.95 ?  317 MET A O     1 
ATOM   2556  C  CB    . MET A 1 317 ? 159.367 141.351 118.806 1.00 34.12 ?  317 MET A CB    1 
ATOM   2557  C  CG    . MET A 1 317 ? 159.270 142.391 119.907 1.00 34.36 ?  317 MET A CG    1 
ATOM   2558  S  SD    . MET A 1 317 ? 160.104 141.884 121.420 1.00 44.92 ?  317 MET A SD    1 
ATOM   2559  C  CE    . MET A 1 317 ? 161.600 142.858 121.322 1.00 38.89 ?  317 MET A CE    1 
ATOM   2560  N  N     . ASP A 1 318 ? 159.912 140.692 115.817 1.00 41.30 ?  318 ASP A N     1 
ATOM   2561  C  CA    . ASP A 1 318 ? 160.260 139.722 114.786 1.00 38.66 ?  318 ASP A CA    1 
ATOM   2562  C  C     . ASP A 1 318 ? 160.829 138.479 115.455 1.00 37.96 ?  318 ASP A C     1 
ATOM   2563  O  O     . ASP A 1 318 ? 161.913 138.524 116.044 1.00 41.69 ?  318 ASP A O     1 
ATOM   2564  C  CB    . ASP A 1 318 ? 161.261 140.324 113.804 1.00 36.96 ?  318 ASP A CB    1 
ATOM   2565  C  CG    . ASP A 1 318 ? 161.394 139.508 112.536 1.00 46.58 ?  318 ASP A CG    1 
ATOM   2566  O  OD1   . ASP A 1 318 ? 160.428 138.802 112.175 1.00 43.51 ?  318 ASP A OD1   1 
ATOM   2567  O  OD2   . ASP A 1 318 ? 162.465 139.571 111.899 1.00 49.50 -1 318 ASP A OD2   1 
ATOM   2568  N  N     . MET A 1 319 ? 160.099 137.366 115.370 1.00 34.59 ?  319 MET A N     1 
ATOM   2569  C  CA    . MET A 1 319 ? 160.566 136.143 116.009 1.00 35.93 ?  319 MET A CA    1 
ATOM   2570  C  C     . MET A 1 319 ? 161.781 135.561 115.300 1.00 33.84 ?  319 MET A C     1 
ATOM   2571  O  O     . MET A 1 319 ? 162.658 134.990 115.953 1.00 37.29 ?  319 MET A O     1 
ATOM   2572  C  CB    . MET A 1 319 ? 159.441 135.112 116.069 1.00 33.86 ?  319 MET A CB    1 
ATOM   2573  C  CG    . MET A 1 319 ? 159.756 133.928 116.963 1.00 35.19 ?  319 MET A CG    1 
ATOM   2574  S  SD    . MET A 1 319 ? 160.094 134.404 118.668 1.00 43.77 ?  319 MET A SD    1 
ATOM   2575  C  CE    . MET A 1 319 ? 158.436 134.668 119.282 1.00 36.00 ?  319 MET A CE    1 
ATOM   2576  N  N     . ASN A 1 320 ? 161.863 135.711 113.977 1.00 39.08 ?  320 ASN A N     1 
ATOM   2577  C  CA    . ASN A 1 320 ? 163.008 135.187 113.244 1.00 40.11 ?  320 ASN A CA    1 
ATOM   2578  C  C     . ASN A 1 320 ? 164.306 135.897 113.604 1.00 41.59 ?  320 ASN A C     1 
ATOM   2579  O  O     . ASN A 1 320 ? 165.386 135.377 113.301 1.00 41.30 ?  320 ASN A O     1 
ATOM   2580  C  CB    . ASN A 1 320 ? 162.754 135.284 111.740 1.00 42.00 ?  320 ASN A CB    1 
ATOM   2581  C  CG    . ASN A 1 320 ? 161.765 134.246 111.253 1.00 43.63 ?  320 ASN A CG    1 
ATOM   2582  O  OD1   . ASN A 1 320 ? 160.562 134.501 111.184 1.00 38.11 ?  320 ASN A OD1   1 
ATOM   2583  N  ND2   . ASN A 1 320 ? 162.268 133.066 110.910 1.00 40.53 ?  320 ASN A ND2   1 
ATOM   2584  N  N     . GLU A 1 321 ? 164.231 137.068 114.239 1.00 42.57 ?  321 GLU A N     1 
ATOM   2585  C  CA    . GLU A 1 321 ? 165.418 137.786 114.675 1.00 41.38 ?  321 GLU A CA    1 
ATOM   2586  C  C     . GLU A 1 321 ? 165.548 137.894 116.187 1.00 43.34 ?  321 GLU A C     1 
ATOM   2587  O  O     . GLU A 1 321 ? 166.639 138.210 116.673 1.00 46.03 ?  321 GLU A O     1 
ATOM   2588  C  CB    . GLU A 1 321 ? 165.439 139.198 114.067 1.00 41.68 ?  321 GLU A CB    1 
ATOM   2589  C  CG    . GLU A 1 321 ? 164.911 140.287 114.985 1.00 44.45 ?  321 GLU A CG    1 
ATOM   2590  C  CD    . GLU A 1 321 ? 164.571 141.567 114.247 1.00 47.32 ?  321 GLU A CD    1 
ATOM   2591  O  OE1   . GLU A 1 321 ? 164.441 141.523 113.006 1.00 47.11 ?  321 GLU A OE1   1 
ATOM   2592  O  OE2   . GLU A 1 321 ? 164.433 142.617 114.911 1.00 43.73 -1 321 GLU A OE2   1 
ATOM   2593  N  N     . MET A 1 322 ? 164.481 137.629 116.942 1.00 40.61 ?  322 MET A N     1 
ATOM   2594  C  CA    . MET A 1 322 ? 164.505 137.759 118.392 1.00 38.13 ?  322 MET A CA    1 
ATOM   2595  C  C     . MET A 1 322 ? 164.307 136.443 119.129 1.00 35.74 ?  322 MET A C     1 
ATOM   2596  O  O     . MET A 1 322 ? 164.327 136.443 120.362 1.00 41.25 ?  322 MET A O     1 
ATOM   2597  C  CB    . MET A 1 322 ? 163.440 138.761 118.857 1.00 37.48 ?  322 MET A CB    1 
ATOM   2598  C  CG    . MET A 1 322 ? 163.586 140.154 118.273 1.00 38.97 ?  322 MET A CG    1 
ATOM   2599  S  SD    . MET A 1 322 ? 164.757 141.200 119.160 1.00 48.56 ?  322 MET A SD    1 
ATOM   2600  C  CE    . MET A 1 322 ? 164.546 140.619 120.837 1.00 39.49 ?  322 MET A CE    1 
ATOM   2601  N  N     . TYR A 1 323 ? 164.102 135.329 118.423 1.00 33.93 ?  323 TYR A N     1 
ATOM   2602  C  CA    . TYR A 1 323 ? 163.893 134.054 119.104 1.00 32.83 ?  323 TYR A CA    1 
ATOM   2603  C  C     . TYR A 1 323 ? 165.129 133.644 119.892 1.00 36.92 ?  323 TYR A C     1 
ATOM   2604  O  O     . TYR A 1 323 ? 165.034 133.217 121.048 1.00 39.12 ?  323 TYR A O     1 
ATOM   2605  C  CB    . TYR A 1 323 ? 163.515 132.973 118.091 1.00 33.05 ?  323 TYR A CB    1 
ATOM   2606  C  CG    . TYR A 1 323 ? 163.482 131.577 118.673 1.00 34.69 ?  323 TYR A CG    1 
ATOM   2607  C  CD1   . TYR A 1 323 ? 162.357 131.105 119.331 1.00 33.75 ?  323 TYR A CD1   1 
ATOM   2608  C  CD2   . TYR A 1 323 ? 164.577 130.729 118.563 1.00 32.20 ?  323 TYR A CD2   1 
ATOM   2609  C  CE1   . TYR A 1 323 ? 162.323 129.834 119.866 1.00 32.07 ?  323 TYR A CE1   1 
ATOM   2610  C  CE2   . TYR A 1 323 ? 164.552 129.459 119.095 1.00 32.37 ?  323 TYR A CE2   1 
ATOM   2611  C  CZ    . TYR A 1 323 ? 163.424 129.016 119.744 1.00 31.69 ?  323 TYR A CZ    1 
ATOM   2612  O  OH    . TYR A 1 323 ? 163.398 127.749 120.274 1.00 31.64 ?  323 TYR A OH    1 
ATOM   2613  N  N     . ASP A 1 324 ? 166.306 133.771 119.277 1.00 38.72 ?  324 ASP A N     1 
ATOM   2614  C  CA    . ASP A 1 324 ? 167.542 133.416 119.961 1.00 35.27 ?  324 ASP A CA    1 
ATOM   2615  C  C     . ASP A 1 324 ? 167.809 134.349 121.133 1.00 40.31 ?  324 ASP A C     1 
ATOM   2616  O  O     . ASP A 1 324 ? 168.319 133.917 122.172 1.00 47.00 ?  324 ASP A O     1 
ATOM   2617  C  CB    . ASP A 1 324 ? 168.708 133.436 118.976 1.00 41.26 ?  324 ASP A CB    1 
ATOM   2618  C  CG    . ASP A 1 324 ? 168.584 132.371 117.907 1.00 44.72 ?  324 ASP A CG    1 
ATOM   2619  O  OD1   . ASP A 1 324 ? 168.368 131.193 118.261 1.00 41.76 ?  324 ASP A OD1   1 
ATOM   2620  O  OD2   . ASP A 1 324 ? 168.699 132.711 116.711 1.00 44.08 -1 324 ASP A OD2   1 
ATOM   2621  N  N     . LYS A 1 325 ? 167.480 135.634 120.983 1.00 38.81 ?  325 LYS A N     1 
ATOM   2622  C  CA    . LYS A 1 325 ? 167.632 136.569 122.091 1.00 35.53 ?  325 LYS A CA    1 
ATOM   2623  C  C     . LYS A 1 325 ? 166.698 136.217 123.243 1.00 38.86 ?  325 LYS A C     1 
ATOM   2624  O  O     . LYS A 1 325 ? 167.089 136.301 124.412 1.00 43.73 ?  325 LYS A O     1 
ATOM   2625  C  CB    . LYS A 1 325 ? 167.384 137.997 121.606 1.00 37.33 ?  325 LYS A CB    1 
ATOM   2626  C  CG    . LYS A 1 325 ? 168.394 138.475 120.580 1.00 37.87 ?  325 LYS A CG    1 
ATOM   2627  C  CD    . LYS A 1 325 ? 168.069 139.873 120.092 1.00 41.16 ?  325 LYS A CD    1 
ATOM   2628  C  CE    . LYS A 1 325 ? 169.032 140.312 119.002 1.00 42.11 ?  325 LYS A CE    1 
ATOM   2629  N  NZ    . LYS A 1 325 ? 168.540 141.513 118.275 1.00 43.60 1  325 LYS A NZ    1 
ATOM   2630  N  N     . PHE A 1 326 ? 165.459 135.826 122.934 1.00 39.16 ?  326 PHE A N     1 
ATOM   2631  C  CA    . PHE A 1 326 ? 164.533 135.394 123.975 1.00 33.41 ?  326 PHE A CA    1 
ATOM   2632  C  C     . PHE A 1 326 ? 165.046 134.147 124.681 1.00 36.37 ?  326 PHE A C     1 
ATOM   2633  O  O     . PHE A 1 326 ? 164.950 134.033 125.909 1.00 40.55 ?  326 PHE A O     1 
ATOM   2634  C  CB    . PHE A 1 326 ? 163.151 135.120 123.377 1.00 32.69 ?  326 PHE A CB    1 
ATOM   2635  C  CG    . PHE A 1 326 ? 162.470 136.333 122.815 1.00 35.56 ?  326 PHE A CG    1 
ATOM   2636  C  CD1   . PHE A 1 326 ? 162.872 137.606 123.173 1.00 35.09 ?  326 PHE A CD1   1 
ATOM   2637  C  CD2   . PHE A 1 326 ? 161.420 136.192 121.926 1.00 34.20 ?  326 PHE A CD2   1 
ATOM   2638  C  CE1   . PHE A 1 326 ? 162.239 138.715 122.652 1.00 33.20 ?  326 PHE A CE1   1 
ATOM   2639  C  CE2   . PHE A 1 326 ? 160.785 137.297 121.402 1.00 37.15 ?  326 PHE A CE2   1 
ATOM   2640  C  CZ    . PHE A 1 326 ? 161.196 138.560 121.766 1.00 38.91 ?  326 PHE A CZ    1 
ATOM   2641  N  N     . VAL A 1 327 ? 165.581 133.193 123.917 1.00 39.05 ?  327 VAL A N     1 
ATOM   2642  C  CA    . VAL A 1 327 ? 166.082 131.957 124.510 1.00 38.24 ?  327 VAL A CA    1 
ATOM   2643  C  C     . VAL A 1 327 ? 167.289 132.237 125.396 1.00 40.04 ?  327 VAL A C     1 
ATOM   2644  O  O     . VAL A 1 327 ? 167.399 131.704 126.506 1.00 45.64 ?  327 VAL A O     1 
ATOM   2645  C  CB    . VAL A 1 327 ? 166.407 130.934 123.406 1.00 36.91 ?  327 VAL A CB    1 
ATOM   2646  C  CG1   . VAL A 1 327 ? 167.194 129.766 123.973 1.00 40.92 ?  327 VAL A CG1   1 
ATOM   2647  C  CG2   . VAL A 1 327 ? 165.130 130.447 122.751 1.00 33.27 ?  327 VAL A CG2   1 
ATOM   2648  N  N     . ASP A 1 328 ? 168.206 133.085 124.929 1.00 38.45 ?  328 ASP A N     1 
ATOM   2649  C  CA    . ASP A 1 328 ? 169.408 133.401 125.688 1.00 36.87 ?  328 ASP A CA    1 
ATOM   2650  C  C     . ASP A 1 328 ? 169.142 134.335 126.859 1.00 40.52 ?  328 ASP A C     1 
ATOM   2651  O  O     . ASP A 1 328 ? 169.970 134.410 127.773 1.00 45.52 ?  328 ASP A O     1 
ATOM   2652  C  CB    . ASP A 1 328 ? 170.460 134.026 124.769 1.00 38.98 ?  328 ASP A CB    1 
ATOM   2653  C  CG    . ASP A 1 328 ? 170.925 133.074 123.689 1.00 44.83 ?  328 ASP A CG    1 
ATOM   2654  O  OD1   . ASP A 1 328 ? 170.747 131.850 123.857 1.00 48.01 ?  328 ASP A OD1   1 
ATOM   2655  O  OD2   . ASP A 1 328 ? 171.469 133.551 122.670 1.00 44.15 -1 328 ASP A OD2   1 
ATOM   2656  N  N     . ASN A 1 329 ? 168.020 135.044 126.855 1.00 41.66 ?  329 ASN A N     1 
ATOM   2657  C  CA    . ASN A 1 329 ? 167.725 135.995 127.920 1.00 38.80 ?  329 ASN A CA    1 
ATOM   2658  C  C     . ASN A 1 329 ? 167.294 135.249 129.176 1.00 42.53 ?  329 ASN A C     1 
ATOM   2659  O  O     . ASN A 1 329 ? 166.301 134.515 129.137 1.00 42.49 ?  329 ASN A O     1 
ATOM   2660  C  CB    . ASN A 1 329 ? 166.634 136.961 127.482 1.00 33.89 ?  329 ASN A CB    1 
ATOM   2661  C  CG    . ASN A 1 329 ? 166.613 138.232 128.305 1.00 40.78 ?  329 ASN A CG    1 
ATOM   2662  O  OD1   . ASN A 1 329 ? 166.542 138.191 129.531 1.00 45.18 ?  329 ASN A OD1   1 
ATOM   2663  N  ND2   . ASN A 1 329 ? 166.684 139.372 127.630 1.00 41.09 ?  329 ASN A ND2   1 
ATOM   2664  N  N     . PRO A 1 330 ? 168.003 135.398 130.299 1.00 44.27 ?  330 PRO A N     1 
ATOM   2665  C  CA    . PRO A 1 330 ? 167.560 134.727 131.528 1.00 40.96 ?  330 PRO A CA    1 
ATOM   2666  C  C     . PRO A 1 330 ? 166.289 135.317 132.112 1.00 39.46 ?  330 PRO A C     1 
ATOM   2667  O  O     . PRO A 1 330 ? 165.525 134.589 132.757 1.00 40.15 ?  330 PRO A O     1 
ATOM   2668  C  CB    . PRO A 1 330 ? 168.753 134.908 132.475 1.00 39.08 ?  330 PRO A CB    1 
ATOM   2669  C  CG    . PRO A 1 330 ? 169.437 136.131 131.977 1.00 36.96 ?  330 PRO A CG    1 
ATOM   2670  C  CD    . PRO A 1 330 ? 169.271 136.121 130.487 1.00 38.41 ?  330 PRO A CD    1 
ATOM   2671  N  N     . ARG A 1 331 ? 166.037 136.609 131.904 1.00 38.41 ?  331 ARG A N     1 
ATOM   2672  C  CA    . ARG A 1 331 ? 164.856 137.253 132.462 1.00 40.80 ?  331 ARG A CA    1 
ATOM   2673  C  C     . ARG A 1 331 ? 163.588 136.940 131.682 1.00 41.59 ?  331 ARG A C     1 
ATOM   2674  O  O     . ARG A 1 331 ? 162.490 137.216 132.179 1.00 40.35 ?  331 ARG A O     1 
ATOM   2675  C  CB    . ARG A 1 331 ? 165.068 138.767 132.526 1.00 39.81 ?  331 ARG A CB    1 
ATOM   2676  C  CG    . ARG A 1 331 ? 166.027 139.201 133.623 1.00 40.33 ?  331 ARG A CG    1 
ATOM   2677  C  CD    . ARG A 1 331 ? 166.654 140.548 133.315 1.00 42.11 ?  331 ARG A CD    1 
ATOM   2678  N  NE    . ARG A 1 331 ? 167.276 140.575 131.996 1.00 41.88 ?  331 ARG A NE    1 
ATOM   2679  C  CZ    . ARG A 1 331 ? 168.446 140.025 131.706 1.00 43.13 ?  331 ARG A CZ    1 
ATOM   2680  N  NH1   . ARG A 1 331 ? 169.167 139.405 132.626 1.00 42.61 1  331 ARG A NH1   1 
ATOM   2681  N  NH2   . ARG A 1 331 ? 168.909 140.103 130.462 1.00 43.39 ?  331 ARG A NH2   1 
ATOM   2682  N  N     . VAL A 1 332 ? 163.708 136.381 130.486 1.00 37.30 ?  332 VAL A N     1 
ATOM   2683  C  CA    . VAL A 1 332 ? 162.562 135.892 129.731 1.00 32.98 ?  332 VAL A CA    1 
ATOM   2684  C  C     . VAL A 1 332 ? 162.275 134.467 130.181 1.00 37.43 ?  332 VAL A C     1 
ATOM   2685  O  O     . VAL A 1 332 ? 163.191 133.642 130.277 1.00 38.83 ?  332 VAL A O     1 
ATOM   2686  C  CB    . VAL A 1 332 ? 162.828 135.956 128.218 1.00 33.47 ?  332 VAL A CB    1 
ATOM   2687  C  CG1   . VAL A 1 332 ? 161.748 135.215 127.451 1.00 33.96 ?  332 VAL A CG1   1 
ATOM   2688  C  CG2   . VAL A 1 332 ? 162.916 137.400 127.756 1.00 34.85 ?  332 VAL A CG2   1 
ATOM   2689  N  N     . LYS A 1 333 ? 161.013 134.179 130.483 1.00 35.97 ?  333 LYS A N     1 
ATOM   2690  C  CA    . LYS A 1 333 ? 160.607 132.838 130.877 1.00 29.96 ?  333 LYS A CA    1 
ATOM   2691  C  C     . LYS A 1 333 ? 160.145 132.069 129.646 1.00 32.69 ?  333 LYS A C     1 
ATOM   2692  O  O     . LYS A 1 333 ? 159.318 132.560 128.873 1.00 35.64 ?  333 LYS A O     1 
ATOM   2693  C  CB    . LYS A 1 333 ? 159.495 132.889 131.924 1.00 28.38 ?  333 LYS A CB    1 
ATOM   2694  C  CG    . LYS A 1 333 ? 159.371 131.626 132.756 1.00 34.79 ?  333 LYS A CG    1 
ATOM   2695  C  CD    . LYS A 1 333 ? 158.176 131.695 133.689 1.00 35.04 ?  333 LYS A CD    1 
ATOM   2696  C  CE    . LYS A 1 333 ? 157.911 130.350 134.346 1.00 37.13 ?  333 LYS A CE    1 
ATOM   2697  N  NZ    . LYS A 1 333 ? 156.735 130.393 135.259 1.00 37.74 1  333 LYS A NZ    1 
ATOM   2698  N  N     . LYS A 1 334 ? 160.688 130.869 129.467 1.00 38.85 ?  334 LYS A N     1 
ATOM   2699  C  CA    . LYS A 1 334 ? 160.395 130.058 128.297 1.00 34.29 ?  334 LYS A CA    1 
ATOM   2700  C  C     . LYS A 1 334 ? 160.147 128.619 128.722 1.00 36.06 ?  334 LYS A C     1 
ATOM   2701  O  O     . LYS A 1 334 ? 160.644 128.165 129.755 1.00 39.70 ?  334 LYS A O     1 
ATOM   2702  C  CB    . LYS A 1 334 ? 161.537 130.116 127.274 1.00 32.87 ?  334 LYS A CB    1 
ATOM   2703  C  CG    . LYS A 1 334 ? 162.820 129.461 127.743 1.00 35.31 ?  334 LYS A CG    1 
ATOM   2704  C  CD    . LYS A 1 334 ? 164.035 130.293 127.389 1.00 35.92 ?  334 LYS A CD    1 
ATOM   2705  C  CE    . LYS A 1 334 ? 163.998 131.637 128.081 1.00 38.84 ?  334 LYS A CE    1 
ATOM   2706  N  NZ    . LYS A 1 334 ? 165.286 132.368 127.963 1.00 39.45 1  334 LYS A NZ    1 
ATOM   2707  N  N     . GLU A 1 335 ? 159.361 127.910 127.917 1.00 38.00 ?  335 GLU A N     1 
ATOM   2708  C  CA    . GLU A 1 335 ? 159.063 126.504 128.136 1.00 36.54 ?  335 GLU A CA    1 
ATOM   2709  C  C     . GLU A 1 335 ? 159.490 125.698 126.918 1.00 36.29 ?  335 GLU A C     1 
ATOM   2710  O  O     . GLU A 1 335 ? 159.236 126.096 125.778 1.00 40.84 ?  335 GLU A O     1 
ATOM   2711  C  CB    . GLU A 1 335 ? 157.573 126.283 128.411 1.00 36.06 ?  335 GLU A CB    1 
ATOM   2712  C  CG    . GLU A 1 335 ? 157.295 125.309 129.541 1.00 38.94 ?  335 GLU A CG    1 
ATOM   2713  C  CD    . GLU A 1 335 ? 156.023 125.633 130.296 1.00 44.57 ?  335 GLU A CD    1 
ATOM   2714  O  OE1   . GLU A 1 335 ? 155.943 125.300 131.497 1.00 44.53 ?  335 GLU A OE1   1 
ATOM   2715  O  OE2   . GLU A 1 335 ? 155.100 126.213 129.689 1.00 42.08 -1 335 GLU A OE2   1 
ATOM   2716  N  N     . LYS A 1 336 ? 160.141 124.566 127.167 1.00 37.35 ?  336 LYS A N     1 
ATOM   2717  C  CA    . LYS A 1 336 ? 160.641 123.721 126.093 1.00 32.44 ?  336 LYS A CA    1 
ATOM   2718  C  C     . LYS A 1 336 ? 159.502 122.923 125.473 1.00 37.58 ?  336 LYS A C     1 
ATOM   2719  O  O     . LYS A 1 336 ? 158.703 122.305 126.184 1.00 40.53 ?  336 LYS A O     1 
ATOM   2720  C  CB    . LYS A 1 336 ? 161.720 122.779 126.626 1.00 38.26 ?  336 LYS A CB    1 
ATOM   2721  C  CG    . LYS A 1 336 ? 162.619 122.178 125.563 1.00 43.11 ?  336 LYS A CG    1 
ATOM   2722  C  CD    . LYS A 1 336 ? 163.566 121.163 126.182 1.00 41.37 ?  336 LYS A CD    1 
ATOM   2723  C  CE    . LYS A 1 336 ? 164.762 120.893 125.286 1.00 41.46 ?  336 LYS A CE    1 
ATOM   2724  N  NZ    . LYS A 1 336 ? 164.576 119.667 124.463 1.00 42.28 1  336 LYS A NZ    1 
ATOM   2725  N  N     . ILE A 1 337 ? 159.427 122.941 124.142 1.00 34.86 ?  337 ILE A N     1 
ATOM   2726  C  CA    . ILE A 1 337 ? 158.440 122.176 123.396 1.00 30.93 ?  337 ILE A CA    1 
ATOM   2727  C  C     . ILE A 1 337 ? 159.138 121.492 122.229 1.00 34.73 ?  337 ILE A C     1 
ATOM   2728  O  O     . ILE A 1 337 ? 160.249 121.853 121.840 1.00 42.14 ?  337 ILE A O     1 
ATOM   2729  C  CB    . ILE A 1 337 ? 157.275 123.049 122.880 1.00 32.72 ?  337 ILE A CB    1 
ATOM   2730  C  CG1   . ILE A 1 337 ? 157.809 124.201 122.028 1.00 35.14 ?  337 ILE A CG1   1 
ATOM   2731  C  CG2   . ILE A 1 337 ? 156.440 123.571 124.035 1.00 36.24 ?  337 ILE A CG2   1 
ATOM   2732  C  CD1   . ILE A 1 337 ? 157.010 124.451 120.775 1.00 32.24 ?  337 ILE A CD1   1 
ATOM   2733  N  N     . ASN A 1 338 ? 158.464 120.487 121.673 1.00 36.42 ?  338 ASN A N     1 
ATOM   2734  C  CA    . ASN A 1 338 ? 158.938 119.837 120.462 1.00 31.75 ?  338 ASN A CA    1 
ATOM   2735  C  C     . ASN A 1 338 ? 158.158 120.391 119.283 1.00 33.43 ?  338 ASN A C     1 
ATOM   2736  O  O     . ASN A 1 338 ? 156.950 120.130 119.177 1.00 36.67 ?  338 ASN A O     1 
ATOM   2737  C  CB    . ASN A 1 338 ? 158.768 118.323 120.554 1.00 33.95 ?  338 ASN A CB    1 
ATOM   2738  C  CG    . ASN A 1 338 ? 159.480 117.589 119.437 1.00 36.09 ?  338 ASN A CG    1 
ATOM   2739  O  OD1   . ASN A 1 338 ? 158.848 117.087 118.508 1.00 38.24 ?  338 ASN A OD1   1 
ATOM   2740  N  ND2   . ASN A 1 338 ? 160.803 117.524 119.519 1.00 35.46 ?  338 ASN A ND2   1 
ATOM   2741  N  N     . PRO A 1 339 ? 158.782 121.164 118.390 1.00 35.15 ?  339 PRO A N     1 
ATOM   2742  C  CA    . PRO A 1 339 ? 158.023 121.765 117.283 1.00 29.42 ?  339 PRO A CA    1 
ATOM   2743  C  C     . PRO A 1 339 ? 157.376 120.749 116.360 1.00 32.59 ?  339 PRO A C     1 
ATOM   2744  O  O     . PRO A 1 339 ? 156.274 121.000 115.859 1.00 37.75 ?  339 PRO A O     1 
ATOM   2745  C  CB    . PRO A 1 339 ? 159.079 122.604 116.551 1.00 33.56 ?  339 PRO A CB    1 
ATOM   2746  C  CG    . PRO A 1 339 ? 160.382 121.996 116.932 1.00 36.27 ?  339 PRO A CG    1 
ATOM   2747  C  CD    . PRO A 1 339 ? 160.214 121.495 118.330 1.00 36.81 ?  339 PRO A CD    1 
ATOM   2748  N  N     . ARG A 1 340 ? 158.021 119.607 116.118 1.00 35.29 ?  340 ARG A N     1 
ATOM   2749  C  CA    . ARG A 1 340 ? 157.405 118.581 115.282 1.00 28.41 ?  340 ARG A CA    1 
ATOM   2750  C  C     . ARG A 1 340 ? 156.215 117.942 115.985 1.00 30.40 ?  340 ARG A C     1 
ATOM   2751  O  O     . ARG A 1 340 ? 155.211 117.616 115.343 1.00 37.55 ?  340 ARG A O     1 
ATOM   2752  C  CB    . ARG A 1 340 ? 158.436 117.524 114.894 1.00 28.21 ?  340 ARG A CB    1 
ATOM   2753  C  CG    . ARG A 1 340 ? 159.393 117.985 113.817 1.00 29.17 ?  340 ARG A CG    1 
ATOM   2754  C  CD    . ARG A 1 340 ? 160.032 116.814 113.101 1.00 33.78 ?  340 ARG A CD    1 
ATOM   2755  N  NE    . ARG A 1 340 ? 161.082 117.254 112.193 1.00 35.44 ?  340 ARG A NE    1 
ATOM   2756  C  CZ    . ARG A 1 340 ? 161.814 116.443 111.444 1.00 32.17 ?  340 ARG A CZ    1 
ATOM   2757  N  NH1   . ARG A 1 340 ? 161.636 115.133 111.468 1.00 30.86 1  340 ARG A NH1   1 
ATOM   2758  N  NH2   . ARG A 1 340 ? 162.746 116.958 110.648 1.00 33.45 ?  340 ARG A NH2   1 
ATOM   2759  N  N     . LYS A 1 341 ? 156.307 117.756 117.302 1.00 32.09 ?  341 LYS A N     1 
ATOM   2760  C  CA    . LYS A 1 341 ? 155.157 117.264 118.053 1.00 30.76 ?  341 LYS A CA    1 
ATOM   2761  C  C     . LYS A 1 341 ? 154.009 118.263 118.003 1.00 33.23 ?  341 LYS A C     1 
ATOM   2762  O  O     . LYS A 1 341 ? 152.842 117.872 117.891 1.00 36.39 ?  341 LYS A O     1 
ATOM   2763  C  CB    . LYS A 1 341 ? 155.556 116.974 119.498 1.00 35.55 ?  341 LYS A CB    1 
ATOM   2764  C  CG    . LYS A 1 341 ? 155.464 115.510 119.881 1.00 35.82 ?  341 LYS A CG    1 
ATOM   2765  C  CD    . LYS A 1 341 ? 156.224 114.637 118.898 1.00 38.75 ?  341 LYS A CD    1 
ATOM   2766  C  CE    . LYS A 1 341 ? 156.248 113.187 119.352 1.00 41.67 ?  341 LYS A CE    1 
ATOM   2767  N  NZ    . LYS A 1 341 ? 157.321 112.942 120.355 1.00 36.89 1  341 LYS A NZ    1 
ATOM   2768  N  N     . LEU A 1 342 ? 154.320 119.558 118.079 1.00 30.62 ?  342 LEU A N     1 
ATOM   2769  C  CA    . LEU A 1 342 ? 153.284 120.577 117.958 1.00 27.32 ?  342 LEU A CA    1 
ATOM   2770  C  C     . LEU A 1 342 ? 152.654 120.563 116.570 1.00 29.90 ?  342 LEU A C     1 
ATOM   2771  O  O     . LEU A 1 342 ? 151.439 120.732 116.434 1.00 33.99 ?  342 LEU A O     1 
ATOM   2772  C  CB    . LEU A 1 342 ? 153.865 121.955 118.275 1.00 31.11 ?  342 LEU A CB    1 
ATOM   2773  C  CG    . LEU A 1 342 ? 152.871 123.080 118.560 1.00 30.19 ?  342 LEU A CG    1 
ATOM   2774  C  CD1   . LEU A 1 342 ? 151.708 122.568 119.390 1.00 28.04 ?  342 LEU A CD1   1 
ATOM   2775  C  CD2   . LEU A 1 342 ? 153.562 124.232 119.266 1.00 26.81 ?  342 LEU A CD2   1 
ATOM   2776  N  N     . LEU A 1 343 ? 153.465 120.364 115.528 1.00 31.54 ?  343 LEU A N     1 
ATOM   2777  C  CA    . LEU A 1 343 ? 152.927 120.268 114.175 1.00 25.59 ?  343 LEU A CA    1 
ATOM   2778  C  C     . LEU A 1 343 ? 152.018 119.054 114.025 1.00 26.60 ?  343 LEU A C     1 
ATOM   2779  O  O     . LEU A 1 343 ? 150.952 119.137 113.401 1.00 37.59 ?  343 LEU A O     1 
ATOM   2780  C  CB    . LEU A 1 343 ? 154.070 120.207 113.163 1.00 30.44 ?  343 LEU A CB    1 
ATOM   2781  C  CG    . LEU A 1 343 ? 154.406 121.490 112.407 1.00 29.59 ?  343 LEU A CG    1 
ATOM   2782  C  CD1   . LEU A 1 343 ? 155.429 121.208 111.323 1.00 25.32 ?  343 LEU A CD1   1 
ATOM   2783  C  CD2   . LEU A 1 343 ? 153.152 122.111 111.817 1.00 33.56 ?  343 LEU A CD2   1 
ATOM   2784  N  N     . GLU A 1 344 ? 152.431 117.914 114.579 1.00 33.26 ?  344 GLU A N     1 
ATOM   2785  C  CA    . GLU A 1 344 ? 151.595 116.720 114.531 1.00 33.22 ?  344 GLU A CA    1 
ATOM   2786  C  C     . GLU A 1 344 ? 150.297 116.929 115.299 1.00 31.00 ?  344 GLU A C     1 
ATOM   2787  O  O     . GLU A 1 344 ? 149.235 116.458 114.877 1.00 34.27 ?  344 GLU A O     1 
ATOM   2788  C  CB    . GLU A 1 344 ? 152.363 115.519 115.082 1.00 30.91 ?  344 GLU A CB    1 
ATOM   2789  C  CG    . GLU A 1 344 ? 153.548 115.099 114.226 1.00 34.30 ?  344 GLU A CG    1 
ATOM   2790  C  CD    . GLU A 1 344 ? 154.621 114.381 115.020 1.00 41.97 ?  344 GLU A CD    1 
ATOM   2791  O  OE1   . GLU A 1 344 ? 154.345 113.983 116.172 1.00 44.43 ?  344 GLU A OE1   1 
ATOM   2792  O  OE2   . GLU A 1 344 ? 155.741 114.215 114.494 1.00 38.74 -1 344 GLU A OE2   1 
ATOM   2793  N  N     . LYS A 1 345 ? 150.363 117.625 116.436 1.00 29.36 ?  345 LYS A N     1 
ATOM   2794  C  CA    . LYS A 1 345 ? 149.150 117.940 117.183 1.00 28.66 ?  345 LYS A CA    1 
ATOM   2795  C  C     . LYS A 1 345 ? 148.231 118.849 116.381 1.00 31.02 ?  345 LYS A C     1 
ATOM   2796  O  O     . LYS A 1 345 ? 147.008 118.674 116.396 1.00 36.42 ?  345 LYS A O     1 
ATOM   2797  C  CB    . LYS A 1 345 ? 149.511 118.583 118.522 1.00 29.68 ?  345 LYS A CB    1 
ATOM   2798  C  CG    . LYS A 1 345 ? 148.310 119.055 119.321 1.00 30.37 ?  345 LYS A CG    1 
ATOM   2799  C  CD    . LYS A 1 345 ? 148.706 119.465 120.725 1.00 32.15 ?  345 LYS A CD    1 
ATOM   2800  C  CE    . LYS A 1 345 ? 147.496 119.903 121.529 1.00 36.64 ?  345 LYS A CE    1 
ATOM   2801  N  NZ    . LYS A 1 345 ? 147.847 120.198 122.944 1.00 33.99 1  345 LYS A NZ    1 
ATOM   2802  N  N     . LEU A 1 346 ? 148.802 119.831 115.680 1.00 30.76 ?  346 LEU A N     1 
ATOM   2803  C  CA    . LEU A 1 346 ? 148.002 120.685 114.807 1.00 25.94 ?  346 LEU A CA    1 
ATOM   2804  C  C     . LEU A 1 346 ? 147.304 119.862 113.733 1.00 28.41 ?  346 LEU A C     1 
ATOM   2805  O  O     . LEU A 1 346 ? 146.110 120.041 113.474 1.00 29.87 ?  346 LEU A O     1 
ATOM   2806  C  CB    . LEU A 1 346 ? 148.886 121.754 114.162 1.00 27.27 ?  346 LEU A CB    1 
ATOM   2807  C  CG    . LEU A 1 346 ? 149.479 122.856 115.038 1.00 29.07 ?  346 LEU A CG    1 
ATOM   2808  C  CD1   . LEU A 1 346 ? 150.460 123.688 114.235 1.00 29.73 ?  346 LEU A CD1   1 
ATOM   2809  C  CD2   . LEU A 1 346 ? 148.389 123.729 115.609 1.00 29.79 ?  346 LEU A CD2   1 
ATOM   2810  N  N     . ALA A 1 347 ? 148.042 118.948 113.099 1.00 30.42 ?  347 ALA A N     1 
ATOM   2811  C  CA    . ALA A 1 347 ? 147.452 118.114 112.056 1.00 26.76 ?  347 ALA A CA    1 
ATOM   2812  C  C     . ALA A 1 347 ? 146.344 117.230 112.611 1.00 32.78 ?  347 ALA A C     1 
ATOM   2813  O  O     . ALA A 1 347 ? 145.285 117.086 111.990 1.00 34.48 ?  347 ALA A O     1 
ATOM   2814  C  CB    . ALA A 1 347 ? 148.531 117.263 111.389 1.00 28.67 ?  347 ALA A CB    1 
ATOM   2815  N  N     . MET A 1 348 ? 146.569 116.631 113.782 1.00 35.83 ?  348 MET A N     1 
ATOM   2816  C  CA    . MET A 1 348 ? 145.552 115.783 114.396 1.00 34.31 ?  348 MET A CA    1 
ATOM   2817  C  C     . MET A 1 348 ? 144.306 116.584 114.755 1.00 34.62 ?  348 MET A C     1 
ATOM   2818  O  O     . MET A 1 348 ? 143.178 116.120 114.550 1.00 39.98 ?  348 MET A O     1 
ATOM   2819  C  CB    . MET A 1 348 ? 146.130 115.095 115.633 1.00 35.33 ?  348 MET A CB    1 
ATOM   2820  C  CG    . MET A 1 348 ? 145.107 114.371 116.486 1.00 42.25 ?  348 MET A CG    1 
ATOM   2821  S  SD    . MET A 1 348 ? 144.905 115.129 118.110 1.00 54.03 ?  348 MET A SD    1 
ATOM   2822  C  CE    . MET A 1 348 ? 146.584 115.055 118.728 1.00 37.83 ?  348 MET A CE    1 
ATOM   2823  N  N     . LEU A 1 349 ? 144.493 117.791 115.291 1.00 30.71 ?  349 LEU A N     1 
ATOM   2824  C  CA    . LEU A 1 349 ? 143.357 118.630 115.654 1.00 28.89 ?  349 LEU A CA    1 
ATOM   2825  C  C     . LEU A 1 349 ? 142.577 119.068 114.422 1.00 24.96 ?  349 LEU A C     1 
ATOM   2826  O  O     . LEU A 1 349 ? 141.345 119.145 114.460 1.00 29.91 ?  349 LEU A O     1 
ATOM   2827  C  CB    . LEU A 1 349 ? 143.838 119.841 116.449 1.00 31.98 ?  349 LEU A CB    1 
ATOM   2828  C  CG    . LEU A 1 349 ? 142.840 120.436 117.442 1.00 32.78 ?  349 LEU A CG    1 
ATOM   2829  C  CD1   . LEU A 1 349 ? 142.590 119.475 118.590 1.00 35.13 ?  349 LEU A CD1   1 
ATOM   2830  C  CD2   . LEU A 1 349 ? 143.332 121.778 117.955 1.00 28.86 ?  349 LEU A CD2   1 
ATOM   2831  N  N     . ARG A 1 350 ? 143.272 119.375 113.325 1.00 27.26 ?  350 ARG A N     1 
ATOM   2832  C  CA    . ARG A 1 350 ? 142.567 119.730 112.097 1.00 26.52 ?  350 ARG A CA    1 
ATOM   2833  C  C     . ARG A 1 350 ? 141.843 118.531 111.501 1.00 31.57 ?  350 ARG A C     1 
ATOM   2834  O  O     . ARG A 1 350 ? 140.763 118.687 110.922 1.00 35.26 ?  350 ARG A O     1 
ATOM   2835  C  CB    . ARG A 1 350 ? 143.536 120.327 111.076 1.00 24.25 ?  350 ARG A CB    1 
ATOM   2836  C  CG    . ARG A 1 350 ? 144.267 121.564 111.559 1.00 27.97 ?  350 ARG A CG    1 
ATOM   2837  C  CD    . ARG A 1 350 ? 144.973 122.270 110.420 1.00 29.70 ?  350 ARG A CD    1 
ATOM   2838  N  NE    . ARG A 1 350 ? 144.135 123.319 109.852 1.00 36.09 ?  350 ARG A NE    1 
ATOM   2839  C  CZ    . ARG A 1 350 ? 144.004 123.556 108.556 1.00 34.03 ?  350 ARG A CZ    1 
ATOM   2840  N  NH1   . ARG A 1 350 ? 144.647 122.837 107.653 1.00 30.09 1  350 ARG A NH1   1 
ATOM   2841  N  NH2   . ARG A 1 350 ? 143.202 124.539 108.156 1.00 30.10 ?  350 ARG A NH2   1 
ATOM   2842  N  N     . SER A 1 351 ? 142.423 117.336 111.620 1.00 35.31 ?  351 SER A N     1 
ATOM   2843  C  CA    . SER A 1 351 ? 141.744 116.135 111.147 1.00 32.15 ?  351 SER A CA    1 
ATOM   2844  C  C     . SER A 1 351 ? 140.481 115.859 111.952 1.00 37.40 ?  351 SER A C     1 
ATOM   2845  O  O     . SER A 1 351 ? 139.444 115.495 111.388 1.00 43.54 ?  351 SER A O     1 
ATOM   2846  C  CB    . SER A 1 351 ? 142.691 114.939 111.213 1.00 34.90 ?  351 SER A CB    1 
ATOM   2847  O  OG    . SER A 1 351 ? 143.745 115.070 110.277 1.00 45.11 ?  351 SER A OG    1 
ATOM   2848  N  N     . GLU A 1 352 ? 140.548 116.023 113.272 1.00 34.86 ?  352 GLU A N     1 
ATOM   2849  C  CA    . GLU A 1 352 ? 139.427 115.660 114.130 1.00 32.54 ?  352 GLU A CA    1 
ATOM   2850  C  C     . GLU A 1 352 ? 138.375 116.755 114.258 1.00 37.94 ?  352 GLU A C     1 
ATOM   2851  O  O     . GLU A 1 352 ? 137.219 116.444 114.568 1.00 46.70 ?  352 GLU A O     1 
ATOM   2852  C  CB    . GLU A 1 352 ? 139.936 115.270 115.523 1.00 38.24 ?  352 GLU A CB    1 
ATOM   2853  C  CG    . GLU A 1 352 ? 140.022 116.415 116.516 1.00 41.92 ?  352 GLU A CG    1 
ATOM   2854  C  CD    . GLU A 1 352 ? 140.573 115.980 117.858 1.00 45.83 ?  352 GLU A CD    1 
ATOM   2855  O  OE1   . GLU A 1 352 ? 141.607 115.280 117.880 1.00 43.39 ?  352 GLU A OE1   1 
ATOM   2856  O  OE2   . GLU A 1 352 ? 139.972 116.337 118.893 1.00 46.21 -1 352 GLU A OE2   1 
ATOM   2857  N  N     . SER A 1 353 ? 138.731 118.020 114.033 1.00 35.27 ?  353 SER A N     1 
ATOM   2858  C  CA    . SER A 1 353 ? 137.778 119.110 114.200 1.00 36.63 ?  353 SER A CA    1 
ATOM   2859  C  C     . SER A 1 353 ? 137.832 120.176 113.116 1.00 32.80 ?  353 SER A C     1 
ATOM   2860  O  O     . SER A 1 353 ? 136.905 120.989 113.048 1.00 32.09 ?  353 SER A O     1 
ATOM   2861  C  CB    . SER A 1 353 ? 137.983 119.788 115.562 1.00 35.94 ?  353 SER A CB    1 
ATOM   2862  O  OG    . SER A 1 353 ? 139.268 120.378 115.649 1.00 33.36 ?  353 SER A OG    1 
ATOM   2863  N  N     . GLY A 1 354 ? 138.863 120.214 112.275 1.00 25.10 ?  354 GLY A N     1 
ATOM   2864  C  CA    . GLY A 1 354 ? 139.027 121.275 111.308 1.00 27.40 ?  354 GLY A CA    1 
ATOM   2865  C  C     . GLY A 1 354 ? 139.765 122.491 111.821 1.00 23.52 ?  354 GLY A C     1 
ATOM   2866  O  O     . GLY A 1 354 ? 140.071 123.389 111.028 1.00 29.14 ?  354 GLY A O     1 
ATOM   2867  N  N     . TYR A 1 355 ? 140.068 122.544 113.114 1.00 22.42 ?  355 TYR A N     1 
ATOM   2868  C  CA    . TYR A 1 355 ? 140.754 123.631 113.784 1.00 16.59 ?  355 TYR A CA    1 
ATOM   2869  C  C     . TYR A 1 355 ? 142.164 123.206 114.175 1.00 22.01 ?  355 TYR A C     1 
ATOM   2870  O  O     . TYR A 1 355 ? 142.424 122.017 114.367 1.00 27.95 ?  355 TYR A O     1 
ATOM   2871  C  CB    . TYR A 1 355 ? 139.988 124.071 115.037 1.00 23.87 ?  355 TYR A CB    1 
ATOM   2872  C  CG    . TYR A 1 355 ? 138.653 124.707 114.740 1.00 28.43 ?  355 TYR A CG    1 
ATOM   2873  C  CD1   . TYR A 1 355 ? 138.558 125.798 113.890 1.00 21.92 ?  355 TYR A CD1   1 
ATOM   2874  C  CD2   . TYR A 1 355 ? 137.487 124.214 115.309 1.00 30.32 ?  355 TYR A CD2   1 
ATOM   2875  C  CE1   . TYR A 1 355 ? 137.341 126.380 113.614 1.00 28.77 ?  355 TYR A CE1   1 
ATOM   2876  C  CE2   . TYR A 1 355 ? 136.266 124.792 115.039 1.00 26.19 ?  355 TYR A CE2   1 
ATOM   2877  C  CZ    . TYR A 1 355 ? 136.197 125.874 114.192 1.00 29.94 ?  355 TYR A CZ    1 
ATOM   2878  O  OH    . TYR A 1 355 ? 134.980 126.452 113.921 1.00 31.97 ?  355 TYR A OH    1 
ATOM   2879  N  N     . PRO A 1 356 ? 143.104 124.147 114.312 1.00 30.72 ?  356 PRO A N     1 
ATOM   2880  C  CA    . PRO A 1 356 ? 142.981 125.600 114.160 1.00 15.39 ?  356 PRO A CA    1 
ATOM   2881  C  C     . PRO A 1 356 ? 143.132 126.085 112.727 1.00 15.29 ?  356 PRO A C     1 
ATOM   2882  O  O     . PRO A 1 356 ? 143.585 125.354 111.854 1.00 24.86 ?  356 PRO A O     1 
ATOM   2883  C  CB    . PRO A 1 356 ? 144.122 126.116 115.037 1.00 17.74 ?  356 PRO A CB    1 
ATOM   2884  C  CG    . PRO A 1 356 ? 145.192 125.092 114.832 1.00 22.45 ?  356 PRO A CG    1 
ATOM   2885  C  CD    . PRO A 1 356 ? 144.472 123.767 114.710 1.00 19.53 ?  356 PRO A CD    1 
ATOM   2886  N  N     . TYR A 1 357 ? 142.737 127.327 112.462 1.00 24.77 ?  357 TYR A N     1 
ATOM   2887  C  CA    . TYR A 1 357 ? 143.181 127.999 111.253 1.00 12.22 ?  357 TYR A CA    1 
ATOM   2888  C  C     . TYR A 1 357 ? 144.686 128.204 111.330 1.00 13.71 ?  357 TYR A C     1 
ATOM   2889  O  O     . TYR A 1 357 ? 145.233 128.475 112.400 1.00 26.45 ?  357 TYR A O     1 
ATOM   2890  C  CB    . TYR A 1 357 ? 142.479 129.349 111.093 1.00 13.47 ?  357 TYR A CB    1 
ATOM   2891  C  CG    . TYR A 1 357 ? 140.975 129.313 111.227 1.00 15.80 ?  357 TYR A CG    1 
ATOM   2892  C  CD1   . TYR A 1 357 ? 140.250 128.193 110.860 1.00 17.54 ?  357 TYR A CD1   1 
ATOM   2893  C  CD2   . TYR A 1 357 ? 140.279 130.408 111.716 1.00 18.09 ?  357 TYR A CD2   1 
ATOM   2894  C  CE1   . TYR A 1 357 ? 138.878 128.158 110.975 1.00 20.23 ?  357 TYR A CE1   1 
ATOM   2895  C  CE2   . TYR A 1 357 ? 138.908 130.384 111.837 1.00 15.86 ?  357 TYR A CE2   1 
ATOM   2896  C  CZ    . TYR A 1 357 ? 138.211 129.256 111.463 1.00 19.73 ?  357 TYR A CZ    1 
ATOM   2897  O  OH    . TYR A 1 357 ? 136.841 129.226 111.580 1.00 28.22 ?  357 TYR A OH    1 
ATOM   2898  N  N     . ILE A 1 358 ? 145.363 128.064 110.198 1.00 16.22 ?  358 ILE A N     1 
ATOM   2899  C  CA    . ILE A 1 358 ? 146.812 128.199 110.138 1.00 22.30 ?  358 ILE A CA    1 
ATOM   2900  C  C     . ILE A 1 358 ? 147.138 129.468 109.368 1.00 18.25 ?  358 ILE A C     1 
ATOM   2901  O  O     . ILE A 1 358 ? 146.756 129.609 108.201 1.00 20.96 ?  358 ILE A O     1 
ATOM   2902  C  CB    . ILE A 1 358 ? 147.476 126.976 109.488 1.00 22.40 ?  358 ILE A CB    1 
ATOM   2903  C  CG1   . ILE A 1 358 ? 147.088 125.692 110.225 1.00 19.24 ?  358 ILE A CG1   1 
ATOM   2904  C  CG2   . ILE A 1 358 ? 148.986 127.145 109.462 1.00 16.40 ?  358 ILE A CG2   1 
ATOM   2905  C  CD1   . ILE A 1 358 ? 147.303 125.751 111.714 1.00 19.28 ?  358 ILE A CD1   1 
ATOM   2906  N  N     . MET A 1 359 ? 147.840 130.389 110.019 1.00 15.72 ?  359 MET A N     1 
ATOM   2907  C  CA    . MET A 1 359 ? 148.356 131.588 109.375 1.00 9.17  ?  359 MET A CA    1 
ATOM   2908  C  C     . MET A 1 359 ? 149.874 131.507 109.346 1.00 11.86 ?  359 MET A C     1 
ATOM   2909  O  O     . MET A 1 359 ? 150.513 131.412 110.397 1.00 21.73 ?  359 MET A O     1 
ATOM   2910  C  CB    . MET A 1 359 ? 147.905 132.853 110.103 1.00 11.58 ?  359 MET A CB    1 
ATOM   2911  C  CG    . MET A 1 359 ? 148.264 134.127 109.361 1.00 12.28 ?  359 MET A CG    1 
ATOM   2912  S  SD    . MET A 1 359 ? 147.937 135.624 110.298 1.00 30.94 ?  359 MET A SD    1 
ATOM   2913  C  CE    . MET A 1 359 ? 149.527 136.432 110.210 1.00 9.99  ?  359 MET A CE    1 
ATOM   2914  N  N     . PHE A 1 360 ? 150.444 131.546 108.148 1.00 12.36 ?  360 PHE A N     1 
ATOM   2915  C  CA    . PHE A 1 360 ? 151.894 131.564 107.980 1.00 10.56 ?  360 PHE A CA    1 
ATOM   2916  C  C     . PHE A 1 360 ? 152.328 133.022 108.001 1.00 14.38 ?  360 PHE A C     1 
ATOM   2917  O  O     . PHE A 1 360 ? 152.243 133.723 106.991 1.00 20.45 ?  360 PHE A O     1 
ATOM   2918  C  CB    . PHE A 1 360 ? 152.292 130.853 106.694 1.00 14.32 ?  360 PHE A CB    1 
ATOM   2919  C  CG    . PHE A 1 360 ? 151.941 129.394 106.689 1.00 19.70 ?  360 PHE A CG    1 
ATOM   2920  C  CD1   . PHE A 1 360 ? 152.448 128.543 107.655 1.00 19.15 ?  360 PHE A CD1   1 
ATOM   2921  C  CD2   . PHE A 1 360 ? 151.085 128.878 105.733 1.00 14.52 ?  360 PHE A CD2   1 
ATOM   2922  C  CE1   . PHE A 1 360 ? 152.121 127.205 107.659 1.00 19.62 ?  360 PHE A CE1   1 
ATOM   2923  C  CE2   . PHE A 1 360 ? 150.755 127.541 105.733 1.00 15.20 ?  360 PHE A CE2   1 
ATOM   2924  C  CZ    . PHE A 1 360 ? 151.272 126.704 106.696 1.00 17.18 ?  360 PHE A CZ    1 
ATOM   2925  N  N     . GLN A 1 361 ? 152.802 133.473 109.165 1.00 17.83 ?  361 GLN A N     1 
ATOM   2926  C  CA    . GLN A 1 361 ? 152.978 134.901 109.411 1.00 10.93 ?  361 GLN A CA    1 
ATOM   2927  C  C     . GLN A 1 361 ? 153.999 135.519 108.464 1.00 17.63 ?  361 GLN A C     1 
ATOM   2928  O  O     . GLN A 1 361 ? 153.793 136.628 107.958 1.00 22.44 ?  361 GLN A O     1 
ATOM   2929  C  CB    . GLN A 1 361 ? 153.385 135.121 110.867 1.00 19.39 ?  361 GLN A CB    1 
ATOM   2930  C  CG    . GLN A 1 361 ? 154.005 136.471 111.158 1.00 22.88 ?  361 GLN A CG    1 
ATOM   2931  C  CD    . GLN A 1 361 ? 153.389 137.131 112.372 1.00 22.79 ?  361 GLN A CD    1 
ATOM   2932  O  OE1   . GLN A 1 361 ? 153.284 136.524 113.435 1.00 24.42 ?  361 GLN A OE1   1 
ATOM   2933  N  NE2   . GLN A 1 361 ? 152.971 138.381 112.218 1.00 23.32 ?  361 GLN A NE2   1 
ATOM   2934  N  N     . ASP A 1 362 ? 155.108 134.824 108.212 1.00 25.25 ?  362 ASP A N     1 
ATOM   2935  C  CA    . ASP A 1 362 ? 156.117 135.364 107.309 1.00 18.40 ?  362 ASP A CA    1 
ATOM   2936  C  C     . ASP A 1 362 ? 155.688 135.293 105.852 1.00 17.69 ?  362 ASP A C     1 
ATOM   2937  O  O     . ASP A 1 362 ? 156.212 136.051 105.030 1.00 28.33 ?  362 ASP A O     1 
ATOM   2938  C  CB    . ASP A 1 362 ? 157.445 134.638 107.503 1.00 24.85 ?  362 ASP A CB    1 
ATOM   2939  C  CG    . ASP A 1 362 ? 158.041 134.880 108.873 1.00 31.03 ?  362 ASP A CG    1 
ATOM   2940  O  OD1   . ASP A 1 362 ? 157.396 134.520 109.878 1.00 29.17 ?  362 ASP A OD1   1 
ATOM   2941  O  OD2   . ASP A 1 362 ? 159.154 135.440 108.943 1.00 33.69 -1 362 ASP A OD2   1 
ATOM   2942  N  N     . ASN A 1 363 ? 154.759 134.399 105.510 1.00 24.62 ?  363 ASN A N     1 
ATOM   2943  C  CA    . ASN A 1 363 ? 154.185 134.414 104.169 1.00 14.12 ?  363 ASN A CA    1 
ATOM   2944  C  C     . ASN A 1 363 ? 153.295 135.632 103.974 1.00 18.06 ?  363 ASN A C     1 
ATOM   2945  O  O     . ASN A 1 363 ? 153.238 136.202 102.879 1.00 28.52 ?  363 ASN A O     1 
ATOM   2946  C  CB    . ASN A 1 363 ? 153.397 133.129 103.920 1.00 12.26 ?  363 ASN A CB    1 
ATOM   2947  C  CG    . ASN A 1 363 ? 154.275 131.986 103.466 1.00 18.23 ?  363 ASN A CG    1 
ATOM   2948  O  OD1   . ASN A 1 363 ? 155.418 132.188 103.065 1.00 21.41 ?  363 ASN A OD1   1 
ATOM   2949  N  ND2   . ASN A 1 363 ? 153.743 130.773 103.527 1.00 20.23 ?  363 ASN A ND2   1 
ATOM   2950  N  N     . VAL A 1 364 ? 152.587 136.038 105.027 1.00 14.61 ?  364 VAL A N     1 
ATOM   2951  C  CA    . VAL A 1 364 ? 151.745 137.225 104.952 1.00 9.24  ?  364 VAL A CA    1 
ATOM   2952  C  C     . VAL A 1 364 ? 152.595 138.487 104.888 1.00 16.15 ?  364 VAL A C     1 
ATOM   2953  O  O     . VAL A 1 364 ? 152.309 139.405 104.111 1.00 19.34 ?  364 VAL A O     1 
ATOM   2954  C  CB    . VAL A 1 364 ? 150.775 137.261 106.145 1.00 1.23  ?  364 VAL A CB    1 
ATOM   2955  C  CG1   . VAL A 1 364 ? 149.819 138.425 106.010 1.00 9.60  ?  364 VAL A CG1   1 
ATOM   2956  C  CG2   . VAL A 1 364 ? 150.024 135.952 106.254 1.00 6.84  ?  364 VAL A CG2   1 
ATOM   2957  N  N     . ASN A 1 365 ? 153.652 138.553 105.696 1.00 22.21 ?  365 ASN A N     1 
ATOM   2958  C  CA    . ASN A 1 365 ? 154.358 139.805 105.922 1.00 11.29 ?  365 ASN A CA    1 
ATOM   2959  C  C     . ASN A 1 365 ? 155.512 140.047 104.962 1.00 14.01 ?  365 ASN A C     1 
ATOM   2960  O  O     . ASN A 1 365 ? 155.987 141.183 104.871 1.00 23.15 ?  365 ASN A O     1 
ATOM   2961  C  CB    . ASN A 1 365 ? 154.877 139.860 107.360 1.00 17.60 ?  365 ASN A CB    1 
ATOM   2962  C  CG    . ASN A 1 365 ? 153.792 140.214 108.350 1.00 16.59 ?  365 ASN A CG    1 
ATOM   2963  O  OD1   . ASN A 1 365 ? 153.105 141.221 108.196 1.00 22.15 ?  365 ASN A OD1   1 
ATOM   2964  N  ND2   . ASN A 1 365 ? 153.629 139.387 109.371 1.00 15.77 ?  365 ASN A ND2   1 
ATOM   2965  N  N     . LYS A 1 366 ? 155.980 139.022 104.248 1.00 19.65 ?  366 LYS A N     1 
ATOM   2966  C  CA    . LYS A 1 366 ? 157.017 139.253 103.252 1.00 22.10 ?  366 LYS A CA    1 
ATOM   2967  C  C     . LYS A 1 366 ? 156.475 139.976 102.027 1.00 24.85 ?  366 LYS A C     1 
ATOM   2968  O  O     . LYS A 1 366 ? 157.249 140.602 101.295 1.00 30.20 ?  366 LYS A O     1 
ATOM   2969  C  CB    . LYS A 1 366 ? 157.668 137.931 102.842 1.00 18.14 ?  366 LYS A CB    1 
ATOM   2970  C  CG    . LYS A 1 366 ? 156.783 137.019 102.013 1.00 27.92 ?  366 LYS A CG    1 
ATOM   2971  C  CD    . LYS A 1 366 ? 157.616 136.042 101.202 1.00 29.61 ?  366 LYS A CD    1 
ATOM   2972  C  CE    . LYS A 1 366 ? 158.101 134.884 102.059 1.00 24.39 ?  366 LYS A CE    1 
ATOM   2973  N  NZ    . LYS A 1 366 ? 159.290 134.216 101.460 1.00 31.12 1  366 LYS A NZ    1 
ATOM   2974  N  N     . VAL A 1 367 ? 155.165 139.908 101.798 1.00 24.91 ?  367 VAL A N     1 
ATOM   2975  C  CA    . VAL A 1 367 ? 154.503 140.630 100.721 1.00 13.81 ?  367 VAL A CA    1 
ATOM   2976  C  C     . VAL A 1 367 ? 153.551 141.694 101.239 1.00 21.55 ?  367 VAL A C     1 
ATOM   2977  O  O     . VAL A 1 367 ? 152.900 142.368 100.436 1.00 26.26 ?  367 VAL A O     1 
ATOM   2978  C  CB    . VAL A 1 367 ? 153.761 139.663 99.777  1.00 16.64 ?  367 VAL A CB    1 
ATOM   2979  C  CG1   . VAL A 1 367 ? 154.741 138.980 98.844  1.00 22.54 ?  367 VAL A CG1   1 
ATOM   2980  C  CG2   . VAL A 1 367 ? 152.995 138.636 100.580 1.00 13.91 ?  367 VAL A CG2   1 
ATOM   2981  N  N     . HIS A 1 368 ? 153.446 141.858 102.555 1.00 21.75 ?  368 HIS A N     1 
ATOM   2982  C  CA    . HIS A 1 368 ? 152.548 142.847 103.134 1.00 9.89  ?  368 HIS A CA    1 
ATOM   2983  C  C     . HIS A 1 368 ? 152.997 144.254 102.759 1.00 14.33 ?  368 HIS A C     1 
ATOM   2984  O  O     . HIS A 1 368 ? 154.175 144.598 102.886 1.00 24.79 ?  368 HIS A O     1 
ATOM   2985  C  CB    . HIS A 1 368 ? 152.505 142.685 104.650 1.00 8.77  ?  368 HIS A CB    1 
ATOM   2986  C  CG    . HIS A 1 368 ? 151.563 143.623 105.335 1.00 10.72 ?  368 HIS A CG    1 
ATOM   2987  N  ND1   . HIS A 1 368 ? 151.772 144.076 106.619 1.00 18.69 ?  368 HIS A ND1   1 
ATOM   2988  C  CD2   . HIS A 1 368 ? 150.404 144.187 104.921 1.00 6.90  ?  368 HIS A CD2   1 
ATOM   2989  C  CE1   . HIS A 1 368 ? 150.784 144.880 106.965 1.00 16.05 ?  368 HIS A CE1   1 
ATOM   2990  N  NE2   . HIS A 1 368 ? 149.941 144.965 105.952 1.00 10.79 ?  368 HIS A NE2   1 
ATOM   2991  N  N     . ALA A 1 369 ? 152.049 145.069 102.298 1.00 18.19 ?  369 ALA A N     1 
ATOM   2992  C  CA    . ALA A 1 369 ? 152.370 146.392 101.782 1.00 9.05  ?  369 ALA A CA    1 
ATOM   2993  C  C     . ALA A 1 369 ? 152.438 147.461 102.863 1.00 20.16 ?  369 ALA A C     1 
ATOM   2994  O  O     . ALA A 1 369 ? 152.952 148.553 102.599 1.00 24.96 ?  369 ALA A O     1 
ATOM   2995  C  CB    . ALA A 1 369 ? 151.342 146.802 100.728 1.00 14.58 ?  369 ALA A CB    1 
ATOM   2996  N  N     . ASN A 1 370 ? 151.947 147.181 104.066 1.00 19.06 ?  370 ASN A N     1 
ATOM   2997  C  CA    . ASN A 1 370 ? 151.838 148.181 105.122 1.00 9.80  ?  370 ASN A CA    1 
ATOM   2998  C  C     . ASN A 1 370 ? 152.509 147.692 106.394 1.00 8.58  ?  370 ASN A C     1 
ATOM   2999  O  O     . ASN A 1 370 ? 151.965 147.796 107.494 1.00 18.09 ?  370 ASN A O     1 
ATOM   3000  C  CB    . ASN A 1 370 ? 150.379 148.534 105.386 1.00 10.11 ?  370 ASN A CB    1 
ATOM   3001  C  CG    . ASN A 1 370 ? 149.682 149.074 104.159 1.00 12.97 ?  370 ASN A CG    1 
ATOM   3002  O  OD1   . ASN A 1 370 ? 150.113 150.065 103.575 1.00 28.26 ?  370 ASN A OD1   1 
ATOM   3003  N  ND2   . ASN A 1 370 ? 148.597 148.424 103.760 1.00 13.93 ?  370 ASN A ND2   1 
ATOM   3004  N  N     . ASN A 1 371 ? 153.718 147.144 106.259 1.00 17.89 ?  371 ASN A N     1 
ATOM   3005  C  CA    . ASN A 1 371 ? 154.468 146.723 107.436 1.00 11.60 ?  371 ASN A CA    1 
ATOM   3006  C  C     . ASN A 1 371 ? 154.943 147.905 108.268 1.00 19.41 ?  371 ASN A C     1 
ATOM   3007  O  O     . ASN A 1 371 ? 155.235 147.732 109.456 1.00 22.71 ?  371 ASN A O     1 
ATOM   3008  C  CB    . ASN A 1 371 ? 155.665 145.867 107.025 1.00 6.17  ?  371 ASN A CB    1 
ATOM   3009  C  CG    . ASN A 1 371 ? 155.298 144.417 106.813 1.00 15.84 ?  371 ASN A CG    1 
ATOM   3010  O  OD1   . ASN A 1 371 ? 154.308 143.929 107.354 1.00 23.36 ?  371 ASN A OD1   1 
ATOM   3011  N  ND2   . ASN A 1 371 ? 156.097 143.716 106.020 1.00 18.12 ?  371 ASN A ND2   1 
ATOM   3012  N  N     . HIS A 1 372 ? 155.034 149.094 107.669 1.00 20.00 ?  372 HIS A N     1 
ATOM   3013  C  CA    . HIS A 1 372 ? 155.388 150.286 108.432 1.00 17.08 ?  372 HIS A CA    1 
ATOM   3014  C  C     . HIS A 1 372 ? 154.329 150.602 109.480 1.00 20.55 ?  372 HIS A C     1 
ATOM   3015  O  O     . HIS A 1 372 ? 154.658 150.985 110.609 1.00 30.06 ?  372 HIS A O     1 
ATOM   3016  C  CB    . HIS A 1 372 ? 155.585 151.471 107.488 1.00 18.82 ?  372 HIS A CB    1 
ATOM   3017  C  CG    . HIS A 1 372 ? 154.324 151.928 106.825 1.00 19.92 ?  372 HIS A CG    1 
ATOM   3018  N  ND1   . HIS A 1 372 ? 153.594 151.120 105.981 1.00 19.60 ?  372 HIS A ND1   1 
ATOM   3019  C  CD2   . HIS A 1 372 ? 153.655 153.103 106.892 1.00 23.20 ?  372 HIS A CD2   1 
ATOM   3020  C  CE1   . HIS A 1 372 ? 152.534 151.780 105.551 1.00 18.35 ?  372 HIS A CE1   1 
ATOM   3021  N  NE2   . HIS A 1 372 ? 152.548 152.985 106.088 1.00 23.99 ?  372 HIS A NE2   1 
ATOM   3022  N  N     . ILE A 1 373 ? 153.051 150.462 109.124 1.00 14.86 ?  373 ILE A N     1 
ATOM   3023  C  CA    . ILE A 1 373 ? 151.986 150.635 110.103 1.00 16.32 ?  373 ILE A CA    1 
ATOM   3024  C  C     . ILE A 1 373 ? 152.071 149.553 111.168 1.00 19.30 ?  373 ILE A C     1 
ATOM   3025  O  O     . ILE A 1 373 ? 152.095 149.839 112.370 1.00 29.97 ?  373 ILE A O     1 
ATOM   3026  C  CB    . ILE A 1 373 ? 150.612 150.632 109.406 1.00 17.88 ?  373 ILE A CB    1 
ATOM   3027  C  CG1   . ILE A 1 373 ? 150.521 151.774 108.394 1.00 16.77 ?  373 ILE A CG1   1 
ATOM   3028  C  CG2   . ILE A 1 373 ? 149.491 150.730 110.428 1.00 17.56 ?  373 ILE A CG2   1 
ATOM   3029  C  CD1   . ILE A 1 373 ? 149.341 151.666 107.459 1.00 13.85 ?  373 ILE A CD1   1 
ATOM   3030  N  N     . SER A 1 374 ? 152.146 148.296 110.738 1.00 20.52 ?  374 SER A N     1 
ATOM   3031  C  CA    . SER A 1 374 ? 152.223 147.139 111.617 1.00 12.72 ?  374 SER A CA    1 
ATOM   3032  C  C     . SER A 1 374 ? 152.362 145.898 110.749 1.00 15.89 ?  374 SER A C     1 
ATOM   3033  O  O     . SER A 1 374 ? 152.029 145.913 109.561 1.00 16.80 ?  374 SER A O     1 
ATOM   3034  C  CB    . SER A 1 374 ? 150.991 147.015 112.514 1.00 17.29 ?  374 SER A CB    1 
ATOM   3035  O  OG    . SER A 1 374 ? 151.151 145.972 113.454 1.00 25.82 ?  374 SER A OG    1 
ATOM   3036  N  N     . LYS A 1 375 ? 152.856 144.828 111.354 1.00 22.63 ?  375 LYS A N     1 
ATOM   3037  C  CA    . LYS A 1 375 ? 152.824 143.527 110.709 1.00 15.46 ?  375 LYS A CA    1 
ATOM   3038  C  C     . LYS A 1 375 ? 151.473 142.866 110.944 1.00 14.23 ?  375 LYS A C     1 
ATOM   3039  O  O     . LYS A 1 375 ? 150.793 143.130 111.939 1.00 25.63 ?  375 LYS A O     1 
ATOM   3040  C  CB    . LYS A 1 375 ? 153.940 142.630 111.240 1.00 11.70 ?  375 LYS A CB    1 
ATOM   3041  C  CG    . LYS A 1 375 ? 155.318 143.247 111.170 1.00 19.34 ?  375 LYS A CG    1 
ATOM   3042  C  CD    . LYS A 1 375 ? 156.195 142.499 110.189 1.00 19.61 ?  375 LYS A CD    1 
ATOM   3043  C  CE    . LYS A 1 375 ? 157.501 143.227 109.942 1.00 20.30 ?  375 LYS A CE    1 
ATOM   3044  N  NZ    . LYS A 1 375 ? 158.225 142.662 108.771 1.00 25.16 1  375 LYS A NZ    1 
ATOM   3045  N  N     . VAL A 1 376 ? 151.081 142.005 110.010 1.00 11.48 ?  376 VAL A N     1 
ATOM   3046  C  CA    . VAL A 1 376 ? 149.859 141.235 110.192 1.00 17.46 ?  376 VAL A CA    1 
ATOM   3047  C  C     . VAL A 1 376 ? 150.123 140.161 111.237 1.00 14.05 ?  376 VAL A C     1 
ATOM   3048  O  O     . VAL A 1 376 ? 151.024 139.329 111.082 1.00 20.12 ?  376 VAL A O     1 
ATOM   3049  C  CB    . VAL A 1 376 ? 149.387 140.625 108.867 1.00 12.52 ?  376 VAL A CB    1 
ATOM   3050  C  CG1   . VAL A 1 376 ? 148.075 139.889 109.065 1.00 13.55 ?  376 VAL A CG1   1 
ATOM   3051  C  CG2   . VAL A 1 376 ? 149.244 141.702 107.812 1.00 3.43  ?  376 VAL A CG2   1 
ATOM   3052  N  N     . LYS A 1 377 ? 149.340 140.179 112.316 1.00 17.05 ?  377 LYS A N     1 
ATOM   3053  C  CA    . LYS A 1 377 ? 149.541 139.252 113.419 1.00 10.87 ?  377 LYS A CA    1 
ATOM   3054  C  C     . LYS A 1 377 ? 148.463 138.191 113.533 1.00 11.62 ?  377 LYS A C     1 
ATOM   3055  O  O     . LYS A 1 377 ? 148.675 137.204 114.241 1.00 27.28 ?  377 LYS A O     1 
ATOM   3056  C  CB    . LYS A 1 377 ? 149.618 140.009 114.752 1.00 13.24 ?  377 LYS A CB    1 
ATOM   3057  C  CG    . LYS A 1 377 ? 150.521 141.222 114.737 1.00 11.59 ?  377 LYS A CG    1 
ATOM   3058  C  CD    . LYS A 1 377 ? 150.073 142.216 115.785 1.00 22.02 ?  377 LYS A CD    1 
ATOM   3059  C  CE    . LYS A 1 377 ? 150.314 143.637 115.338 1.00 18.69 ?  377 LYS A CE    1 
ATOM   3060  N  NZ    . LYS A 1 377 ? 149.620 144.609 116.224 1.00 20.26 1  377 LYS A NZ    1 
ATOM   3061  N  N     . PHE A 1 378 ? 147.322 138.369 112.877 1.00 13.99 ?  378 PHE A N     1 
ATOM   3062  C  CA    . PHE A 1 378 ? 146.255 137.382 112.930 1.00 7.50  ?  378 PHE A CA    1 
ATOM   3063  C  C     . PHE A 1 378 ? 145.293 137.634 111.782 1.00 10.29 ?  378 PHE A C     1 
ATOM   3064  O  O     . PHE A 1 378 ? 145.315 138.693 111.150 1.00 18.96 ?  378 PHE A O     1 
ATOM   3065  C  CB    . PHE A 1 378 ? 145.526 137.397 114.283 1.00 6.96  ?  378 PHE A CB    1 
ATOM   3066  C  CG    . PHE A 1 378 ? 144.697 138.629 114.536 1.00 6.75  ?  378 PHE A CG    1 
ATOM   3067  C  CD1   . PHE A 1 378 ? 145.235 139.898 114.403 1.00 10.61 ?  378 PHE A CD1   1 
ATOM   3068  C  CD2   . PHE A 1 378 ? 143.381 138.510 114.944 1.00 4.93  ?  378 PHE A CD2   1 
ATOM   3069  C  CE1   . PHE A 1 378 ? 144.473 141.017 114.651 1.00 8.34  ?  378 PHE A CE1   1 
ATOM   3070  C  CE2   . PHE A 1 378 ? 142.616 139.627 115.194 1.00 10.30 ?  378 PHE A CE2   1 
ATOM   3071  C  CZ    . PHE A 1 378 ? 143.164 140.881 115.048 1.00 8.75  ?  378 PHE A CZ    1 
ATOM   3072  N  N     . SER A 1 379 ? 144.458 136.640 111.515 1.00 5.32  ?  379 SER A N     1 
ATOM   3073  C  CA    . SER A 1 379 ? 143.462 136.700 110.460 1.00 7.81  ?  379 SER A CA    1 
ATOM   3074  C  C     . SER A 1 379 ? 142.074 136.822 111.081 1.00 8.33  ?  379 SER A C     1 
ATOM   3075  O  O     . SER A 1 379 ? 141.925 136.972 112.298 1.00 16.72 ?  379 SER A O     1 
ATOM   3076  C  CB    . SER A 1 379 ? 143.579 135.475 109.552 1.00 13.39 ?  379 SER A CB    1 
ATOM   3077  O  OG    . SER A 1 379 ? 143.170 135.787 108.234 1.00 14.39 ?  379 SER A OG    1 
ATOM   3078  N  N     . ASN A 1 380 ? 141.053 136.775 110.236 1.00 8.33  ?  380 ASN A N     1 
ATOM   3079  C  CA    . ASN A 1 380 ? 139.677 136.933 110.670 1.00 7.79  ?  380 ASN A CA    1 
ATOM   3080  C  C     . ASN A 1 380 ? 139.044 135.566 110.925 1.00 16.69 ?  380 ASN A C     1 
ATOM   3081  O  O     . ASN A 1 380 ? 139.713 134.530 110.916 1.00 19.66 ?  380 ASN A O     1 
ATOM   3082  C  CB    . ASN A 1 380 ? 138.892 137.742 109.639 1.00 10.47 ?  380 ASN A CB    1 
ATOM   3083  C  CG    . ASN A 1 380 ? 138.781 137.040 108.306 1.00 7.14  ?  380 ASN A CG    1 
ATOM   3084  O  OD1   . ASN A 1 380 ? 139.741 136.444 107.824 1.00 18.25 ?  380 ASN A OD1   1 
ATOM   3085  N  ND2   . ASN A 1 380 ? 137.606 137.111 107.700 1.00 14.30 ?  380 ASN A ND2   1 
ATOM   3086  N  N     . LEU A 1 381 ? 137.733 135.567 111.167 1.00 17.42 ?  381 LEU A N     1 
ATOM   3087  C  CA    . LEU A 1 381 ? 137.015 134.318 111.394 1.00 10.98 ?  381 LEU A CA    1 
ATOM   3088  C  C     . LEU A 1 381 ? 136.994 133.447 110.144 1.00 10.10 ?  381 LEU A C     1 
ATOM   3089  O  O     . LEU A 1 381 ? 136.979 132.216 110.249 1.00 20.39 ?  381 LEU A O     1 
ATOM   3090  C  CB    . LEU A 1 381 ? 135.594 134.622 111.870 1.00 12.55 ?  381 LEU A CB    1 
ATOM   3091  C  CG    . LEU A 1 381 ? 134.590 133.476 111.988 1.00 14.65 ?  381 LEU A CG    1 
ATOM   3092  C  CD1   . LEU A 1 381 ? 134.924 132.573 113.160 1.00 16.28 ?  381 LEU A CD1   1 
ATOM   3093  C  CD2   . LEU A 1 381 ? 133.188 134.033 112.120 1.00 17.94 ?  381 LEU A CD2   1 
ATOM   3094  N  N     . CYS A 1 382 ? 136.993 134.058 108.964 1.00 18.94 ?  382 CYS A N     1 
ATOM   3095  C  CA    . CYS A 1 382 ? 137.049 133.320 107.711 1.00 13.00 ?  382 CYS A CA    1 
ATOM   3096  C  C     . CYS A 1 382 ? 138.473 133.107 107.217 1.00 7.71  ?  382 CYS A C     1 
ATOM   3097  O  O     . CYS A 1 382 ? 138.662 132.476 106.173 1.00 17.19 ?  382 CYS A O     1 
ATOM   3098  C  CB    . CYS A 1 382 ? 136.224 134.039 106.640 1.00 20.13 ?  382 CYS A CB    1 
ATOM   3099  S  SG    . CYS A 1 382 ? 134.516 134.373 107.121 1.00 26.50 ?  382 CYS A SG    1 
ATOM   3100  N  N     . SER A 1 383 ? 139.468 133.625 107.939 1.00 15.62 ?  383 SER A N     1 
ATOM   3101  C  CA    . SER A 1 383 ? 140.881 133.330 107.693 1.00 10.49 ?  383 SER A CA    1 
ATOM   3102  C  C     . SER A 1 383 ? 141.346 133.836 106.329 1.00 12.80 ?  383 SER A C     1 
ATOM   3103  O  O     . SER A 1 383 ? 142.147 133.193 105.651 1.00 26.33 ?  383 SER A O     1 
ATOM   3104  C  CB    . SER A 1 383 ? 141.161 131.832 107.843 1.00 16.56 ?  383 SER A CB    1 
ATOM   3105  O  OG    . SER A 1 383 ? 142.538 131.546 107.695 1.00 24.81 ?  383 SER A OG    1 
ATOM   3106  N  N     . GLU A 1 384 ? 140.846 135.001 105.919 1.00 14.02 ?  384 GLU A N     1 
ATOM   3107  C  CA    . GLU A 1 384 ? 141.320 135.608 104.680 1.00 5.78  ?  384 GLU A CA    1 
ATOM   3108  C  C     . GLU A 1 384 ? 141.631 137.093 104.789 1.00 14.42 ?  384 GLU A C     1 
ATOM   3109  O  O     . GLU A 1 384 ? 142.301 137.622 103.899 1.00 20.38 ?  384 GLU A O     1 
ATOM   3110  C  CB    . GLU A 1 384 ? 140.305 135.380 103.545 1.00 9.03  ?  384 GLU A CB    1 
ATOM   3111  C  CG    . GLU A 1 384 ? 139.477 136.586 103.128 1.00 10.86 ?  384 GLU A CG    1 
ATOM   3112  C  CD    . GLU A 1 384 ? 138.339 136.879 104.078 1.00 21.19 ?  384 GLU A CD    1 
ATOM   3113  O  OE1   . GLU A 1 384 ? 137.959 135.974 104.846 1.00 14.47 ?  384 GLU A OE1   1 
ATOM   3114  O  OE2   . GLU A 1 384 ? 137.811 138.006 104.039 1.00 27.61 -1 384 GLU A OE2   1 
ATOM   3115  N  N     . VAL A 1 385 ? 141.198 137.780 105.841 1.00 17.24 ?  385 VAL A N     1 
ATOM   3116  C  CA    . VAL A 1 385 ? 141.525 139.187 106.034 1.00 5.14  ?  385 VAL A CA    1 
ATOM   3117  C  C     . VAL A 1 385 ? 142.897 139.270 106.688 1.00 15.31 ?  385 VAL A C     1 
ATOM   3118  O  O     . VAL A 1 385 ? 143.105 138.738 107.783 1.00 23.18 ?  385 VAL A O     1 
ATOM   3119  C  CB    . VAL A 1 385 ? 140.464 139.895 106.888 1.00 7.09  ?  385 VAL A CB    1 
ATOM   3120  C  CG1   . VAL A 1 385 ? 140.907 141.303 107.191 1.00 8.27  ?  385 VAL A CG1   1 
ATOM   3121  C  CG2   . VAL A 1 385 ? 139.136 139.905 106.173 1.00 7.56  ?  385 VAL A CG2   1 
ATOM   3122  N  N     . LEU A 1 386 ? 143.834 139.939 106.017 1.00 16.57 ?  386 LEU A N     1 
ATOM   3123  C  CA    . LEU A 1 386 ? 145.224 140.036 106.463 1.00 2.61  ?  386 LEU A CA    1 
ATOM   3124  C  C     . LEU A 1 386 ? 145.659 141.492 106.346 1.00 5.27  ?  386 LEU A C     1 
ATOM   3125  O  O     . LEU A 1 386 ? 146.167 141.917 105.307 1.00 11.88 ?  386 LEU A O     1 
ATOM   3126  C  CB    . LEU A 1 386 ? 146.116 139.111 105.650 1.00 2.13  ?  386 LEU A CB    1 
ATOM   3127  C  CG    . LEU A 1 386 ? 145.855 137.623 105.881 1.00 6.65  ?  386 LEU A CG    1 
ATOM   3128  C  CD1   . LEU A 1 386 ? 146.711 136.795 104.964 1.00 10.46 ?  386 LEU A CD1   1 
ATOM   3129  C  CD2   . LEU A 1 386 ? 146.117 137.259 107.330 1.00 13.82 ?  386 LEU A CD2   1 
ATOM   3130  N  N     . GLN A 1 387 ? 145.464 142.249 107.422 1.00 14.61 ?  387 GLN A N     1 
ATOM   3131  C  CA    . GLN A 1 387 ? 145.740 143.676 107.442 1.00 10.55 ?  387 GLN A CA    1 
ATOM   3132  C  C     . GLN A 1 387 ? 146.522 144.035 108.696 1.00 12.82 ?  387 GLN A C     1 
ATOM   3133  O  O     . GLN A 1 387 ? 146.516 143.307 109.690 1.00 25.68 ?  387 GLN A O     1 
ATOM   3134  C  CB    . GLN A 1 387 ? 144.444 144.495 107.381 1.00 3.94  ?  387 GLN A CB    1 
ATOM   3135  C  CG    . GLN A 1 387 ? 143.549 144.144 106.213 1.00 7.66  ?  387 GLN A CG    1 
ATOM   3136  C  CD    . GLN A 1 387 ? 142.318 145.008 106.150 1.00 9.54  ?  387 GLN A CD    1 
ATOM   3137  O  OE1   . GLN A 1 387 ? 142.238 146.040 106.812 1.00 26.99 ?  387 GLN A OE1   1 
ATOM   3138  N  NE2   . GLN A 1 387 ? 141.343 144.593 105.354 1.00 13.40 ?  387 GLN A NE2   1 
ATOM   3139  N  N     . ALA A 1 388 ? 147.210 145.171 108.631 1.00 12.69 ?  388 ALA A N     1 
ATOM   3140  C  CA    . ALA A 1 388 ? 147.952 145.667 109.780 1.00 10.57 ?  388 ALA A CA    1 
ATOM   3141  C  C     . ALA A 1 388 ? 146.998 146.162 110.859 1.00 13.36 ?  388 ALA A C     1 
ATOM   3142  O  O     . ALA A 1 388 ? 145.989 146.809 110.571 1.00 25.27 ?  388 ALA A O     1 
ATOM   3143  C  CB    . ALA A 1 388 ? 148.894 146.792 109.357 1.00 11.56 ?  388 ALA A CB    1 
ATOM   3144  N  N     . SER A 1 389 ? 147.320 145.850 112.111 1.00 19.36 ?  389 SER A N     1 
ATOM   3145  C  CA    . SER A 1 389 ? 146.526 146.281 113.249 1.00 13.85 ?  389 SER A CA    1 
ATOM   3146  C  C     . SER A 1 389 ? 147.435 146.839 114.330 1.00 15.70 ?  389 SER A C     1 
ATOM   3147  O  O     . SER A 1 389 ? 148.574 146.396 114.499 1.00 23.18 ?  389 SER A O     1 
ATOM   3148  C  CB    . SER A 1 389 ? 145.688 145.133 113.827 1.00 14.60 ?  389 SER A CB    1 
ATOM   3149  O  OG    . SER A 1 389 ? 146.489 143.995 114.094 1.00 25.24 ?  389 SER A OG    1 
ATOM   3150  N  N     . GLN A 1 390 ? 146.918 147.817 115.064 1.00 17.82 ?  390 GLN A N     1 
ATOM   3151  C  CA    . GLN A 1 390 ? 147.595 148.385 116.221 1.00 14.43 ?  390 GLN A CA    1 
ATOM   3152  C  C     . GLN A 1 390 ? 146.694 148.220 117.433 1.00 14.63 ?  390 GLN A C     1 
ATOM   3153  O  O     . GLN A 1 390 ? 145.517 148.589 117.389 1.00 27.28 ?  390 GLN A O     1 
ATOM   3154  C  CB    . GLN A 1 390 ? 147.934 149.859 115.996 1.00 17.79 ?  390 GLN A CB    1 
ATOM   3155  C  CG    . GLN A 1 390 ? 148.968 150.090 114.913 1.00 17.56 ?  390 GLN A CG    1 
ATOM   3156  C  CD    . GLN A 1 390 ? 149.139 151.553 114.569 1.00 22.86 ?  390 GLN A CD    1 
ATOM   3157  O  OE1   . GLN A 1 390 ? 148.372 152.403 115.021 1.00 31.19 ?  390 GLN A OE1   1 
ATOM   3158  N  NE2   . GLN A 1 390 ? 150.152 151.857 113.768 1.00 21.59 ?  390 GLN A NE2   1 
ATOM   3159  N  N     . VAL A 1 391 ? 147.245 147.657 118.508 1.00 23.96 ?  391 VAL A N     1 
ATOM   3160  C  CA    . VAL A 1 391 ? 146.441 147.368 119.686 1.00 24.92 ?  391 VAL A CA    1 
ATOM   3161  C  C     . VAL A 1 391 ? 146.045 148.666 120.381 1.00 25.86 ?  391 VAL A C     1 
ATOM   3162  O  O     . VAL A 1 391 ? 146.781 149.661 120.373 1.00 26.45 ?  391 VAL A O     1 
ATOM   3163  C  CB    . VAL A 1 391 ? 147.195 146.421 120.641 1.00 15.46 ?  391 VAL A CB    1 
ATOM   3164  C  CG1   . VAL A 1 391 ? 148.262 147.168 121.423 1.00 21.40 ?  391 VAL A CG1   1 
ATOM   3165  C  CG2   . VAL A 1 391 ? 146.224 145.727 121.580 1.00 16.26 ?  391 VAL A CG2   1 
ATOM   3166  N  N     . SER A 1 392 ? 144.852 148.664 120.963 1.00 28.22 ?  392 SER A N     1 
ATOM   3167  C  CA    . SER A 1 392 ? 144.367 149.795 121.733 1.00 18.16 ?  392 SER A CA    1 
ATOM   3168  C  C     . SER A 1 392 ? 144.774 149.651 123.194 1.00 27.95 ?  392 SER A C     1 
ATOM   3169  O  O     . SER A 1 392 ? 145.088 148.560 123.675 1.00 36.07 ?  392 SER A O     1 
ATOM   3170  C  CB    . SER A 1 392 ? 142.847 149.917 121.621 1.00 24.73 ?  392 SER A CB    1 
ATOM   3171  O  OG    . SER A 1 392 ? 142.453 150.215 120.295 1.00 33.95 ?  392 SER A OG    1 
ATOM   3172  N  N     . SER A 1 393 ? 144.767 150.775 123.900 1.00 33.60 ?  393 SER A N     1 
ATOM   3173  C  CA    . SER A 1 393 ? 145.088 150.817 125.323 1.00 31.95 ?  393 SER A CA    1 
ATOM   3174  C  C     . SER A 1 393 ? 143.870 151.383 126.045 1.00 32.73 ?  393 SER A C     1 
ATOM   3175  O  O     . SER A 1 393 ? 143.784 152.589 126.292 1.00 34.99 ?  393 SER A O     1 
ATOM   3176  C  CB    . SER A 1 393 ? 146.339 151.648 125.584 1.00 31.84 ?  393 SER A CB    1 
ATOM   3177  O  OG    . SER A 1 393 ? 147.092 151.112 126.658 1.00 39.31 ?  393 SER A OG    1 
ATOM   3178  N  N     . TYR A 1 394 ? 142.928 150.507 126.380 1.00 34.05 ?  394 TYR A N     1 
ATOM   3179  C  CA    . TYR A 1 394 ? 141.737 150.913 127.112 1.00 31.62 ?  394 TYR A CA    1 
ATOM   3180  C  C     . TYR A 1 394 ? 142.086 151.037 128.589 1.00 35.26 ?  394 TYR A C     1 
ATOM   3181  O  O     . TYR A 1 394 ? 142.462 150.051 129.232 1.00 37.43 ?  394 TYR A O     1 
ATOM   3182  C  CB    . TYR A 1 394 ? 140.607 149.911 126.894 1.00 28.57 ?  394 TYR A CB    1 
ATOM   3183  C  CG    . TYR A 1 394 ? 140.150 149.825 125.456 1.00 30.05 ?  394 TYR A CG    1 
ATOM   3184  C  CD1   . TYR A 1 394 ? 139.428 150.859 124.874 1.00 31.16 ?  394 TYR A CD1   1 
ATOM   3185  C  CD2   . TYR A 1 394 ? 140.444 148.715 124.678 1.00 31.12 ?  394 TYR A CD2   1 
ATOM   3186  C  CE1   . TYR A 1 394 ? 139.011 150.786 123.563 1.00 33.30 ?  394 TYR A CE1   1 
ATOM   3187  C  CE2   . TYR A 1 394 ? 140.030 148.633 123.367 1.00 30.57 ?  394 TYR A CE2   1 
ATOM   3188  C  CZ    . TYR A 1 394 ? 139.315 149.671 122.813 1.00 37.78 ?  394 TYR A CZ    1 
ATOM   3189  O  OH    . TYR A 1 394 ? 138.903 149.592 121.503 1.00 39.81 ?  394 TYR A OH    1 
ATOM   3190  N  N     . THR A 1 395 ? 141.968 152.245 129.120 1.00 34.33 ?  395 THR A N     1 
ATOM   3191  C  CA    . THR A 1 395 ? 142.396 152.569 130.468 1.00 36.56 ?  395 THR A CA    1 
ATOM   3192  C  C     . THR A 1 395 ? 141.195 152.571 131.411 1.00 37.82 ?  395 THR A C     1 
ATOM   3193  O  O     . THR A 1 395 ? 140.094 152.139 131.055 1.00 34.94 ?  395 THR A O     1 
ATOM   3194  C  CB    . THR A 1 395 ? 143.124 153.913 130.464 1.00 35.93 ?  395 THR A CB    1 
ATOM   3195  O  OG1   . THR A 1 395 ? 142.253 154.926 129.945 1.00 37.71 ?  395 THR A OG1   1 
ATOM   3196  C  CG2   . THR A 1 395 ? 144.363 153.835 129.591 1.00 34.69 ?  395 THR A CG2   1 
ATOM   3197  N  N     . ASP A 1 396 ? 141.411 153.044 132.637 1.00 39.46 ?  396 ASP A N     1 
ATOM   3198  C  CA    . ASP A 1 396 ? 140.340 153.135 133.615 1.00 35.04 ?  396 ASP A CA    1 
ATOM   3199  C  C     . ASP A 1 396 ? 139.233 154.062 133.115 1.00 37.72 ?  396 ASP A C     1 
ATOM   3200  O  O     . ASP A 1 396 ? 139.376 154.774 132.119 1.00 43.75 ?  396 ASP A O     1 
ATOM   3201  C  CB    . ASP A 1 396 ? 140.879 153.627 134.956 1.00 37.84 ?  396 ASP A CB    1 
ATOM   3202  C  CG    . ASP A 1 396 ? 141.877 152.666 135.572 1.00 43.06 ?  396 ASP A CG    1 
ATOM   3203  O  OD1   . ASP A 1 396 ? 141.556 151.465 135.681 1.00 40.24 ?  396 ASP A OD1   1 
ATOM   3204  O  OD2   . ASP A 1 396 ? 142.979 153.112 135.950 1.00 44.39 -1 396 ASP A OD2   1 
ATOM   3205  N  N     . TYR A 1 397 ? 138.107 154.040 133.833 1.00 35.15 ?  397 TYR A N     1 
ATOM   3206  C  CA    . TYR A 1 397 ? 136.938 154.802 133.406 1.00 35.34 ?  397 TYR A CA    1 
ATOM   3207  C  C     . TYR A 1 397 ? 137.238 156.294 133.337 1.00 36.99 ?  397 TYR A C     1 
ATOM   3208  O  O     . TYR A 1 397 ? 136.825 156.975 132.392 1.00 41.13 ?  397 TYR A O     1 
ATOM   3209  C  CB    . TYR A 1 397 ? 135.766 154.536 134.351 1.00 30.96 ?  397 TYR A CB    1 
ATOM   3210  C  CG    . TYR A 1 397 ? 134.491 155.240 133.953 1.00 33.12 ?  397 TYR A CG    1 
ATOM   3211  C  CD1   . TYR A 1 397 ? 133.611 154.662 133.048 1.00 33.56 ?  397 TYR A CD1   1 
ATOM   3212  C  CD2   . TYR A 1 397 ? 134.169 156.485 134.477 1.00 34.28 ?  397 TYR A CD2   1 
ATOM   3213  C  CE1   . TYR A 1 397 ? 132.448 155.304 132.679 1.00 29.73 ?  397 TYR A CE1   1 
ATOM   3214  C  CE2   . TYR A 1 397 ? 133.010 157.132 134.113 1.00 33.91 ?  397 TYR A CE2   1 
ATOM   3215  C  CZ    . TYR A 1 397 ? 132.153 156.538 133.216 1.00 34.95 ?  397 TYR A CZ    1 
ATOM   3216  O  OH    . TYR A 1 397 ? 130.994 157.182 132.852 1.00 39.62 ?  397 TYR A OH    1 
ATOM   3217  N  N     . ASP A 1 398 ? 137.957 156.819 134.325 1.00 40.12 ?  398 ASP A N     1 
ATOM   3218  C  CA    . ASP A 1 398 ? 138.241 158.246 134.388 1.00 39.48 ?  398 ASP A CA    1 
ATOM   3219  C  C     . ASP A 1 398 ? 139.304 158.694 133.394 1.00 45.32 ?  398 ASP A C     1 
ATOM   3220  O  O     . ASP A 1 398 ? 139.401 159.895 133.121 1.00 46.74 ?  398 ASP A O     1 
ATOM   3221  C  CB    . ASP A 1 398 ? 138.676 158.627 135.805 1.00 43.35 ?  398 ASP A CB    1 
ATOM   3222  C  CG    . ASP A 1 398 ? 139.551 157.568 136.450 1.00 46.91 ?  398 ASP A CG    1 
ATOM   3223  O  OD1   . ASP A 1 398 ? 139.041 156.462 136.722 1.00 43.86 ?  398 ASP A OD1   1 
ATOM   3224  O  OD2   . ASP A 1 398 ? 140.747 157.839 136.683 1.00 45.84 -1 398 ASP A OD2   1 
ATOM   3225  N  N     . GLU A 1 399 ? 140.092 157.775 132.849 1.00 46.09 ?  399 GLU A N     1 
ATOM   3226  C  CA    . GLU A 1 399 ? 141.207 158.116 131.979 1.00 42.81 ?  399 GLU A CA    1 
ATOM   3227  C  C     . GLU A 1 399 ? 140.821 157.970 130.512 1.00 45.49 ?  399 GLU A C     1 
ATOM   3228  O  O     . GLU A 1 399 ? 139.895 157.238 130.152 1.00 45.00 ?  399 GLU A O     1 
ATOM   3229  C  CB    . GLU A 1 399 ? 142.420 157.237 132.285 1.00 42.35 ?  399 GLU A CB    1 
ATOM   3230  C  CG    . GLU A 1 399 ? 142.494 156.757 133.719 1.00 44.59 ?  399 GLU A CG    1 
ATOM   3231  C  CD    . GLU A 1 399 ? 143.850 156.178 134.068 1.00 50.14 ?  399 GLU A CD    1 
ATOM   3232  O  OE1   . GLU A 1 399 ? 144.131 155.032 133.657 1.00 46.87 ?  399 GLU A OE1   1 
ATOM   3233  O  OE2   . GLU A 1 399 ? 144.634 156.866 134.754 1.00 49.31 -1 399 GLU A OE2   1 
ATOM   3234  N  N     . GLU A 1 400 ? 141.552 158.689 129.663 1.00 43.20 ?  400 GLU A N     1 
ATOM   3235  C  CA    . GLU A 1 400 ? 141.346 158.598 128.226 1.00 40.44 ?  400 GLU A CA    1 
ATOM   3236  C  C     . GLU A 1 400 ? 141.971 157.322 127.676 1.00 41.95 ?  400 GLU A C     1 
ATOM   3237  O  O     . GLU A 1 400 ? 143.023 156.876 128.139 1.00 41.73 ?  400 GLU A O     1 
ATOM   3238  C  CB    . GLU A 1 400 ? 141.945 159.818 127.526 1.00 40.61 ?  400 GLU A CB    1 
ATOM   3239  C  CG    . GLU A 1 400 ? 141.109 161.079 127.648 1.00 44.10 ?  400 GLU A CG    1 
ATOM   3240  C  CD    . GLU A 1 400 ? 140.130 161.243 126.503 1.00 49.46 ?  400 GLU A CD    1 
ATOM   3241  O  OE1   . GLU A 1 400 ? 139.045 161.819 126.724 1.00 45.54 ?  400 GLU A OE1   1 
ATOM   3242  O  OE2   . GLU A 1 400 ? 140.444 160.794 125.381 1.00 49.57 -1 400 GLU A OE2   1 
ATOM   3243  N  N     . ASP A 1 401 ? 141.314 156.735 126.681 1.00 39.60 ?  401 ASP A N     1 
ATOM   3244  C  CA    . ASP A 1 401 ? 141.792 155.511 126.057 1.00 36.96 ?  401 ASP A CA    1 
ATOM   3245  C  C     . ASP A 1 401 ? 142.639 155.832 124.835 1.00 37.21 ?  401 ASP A C     1 
ATOM   3246  O  O     . ASP A 1 401 ? 142.347 156.771 124.090 1.00 39.03 ?  401 ASP A O     1 
ATOM   3247  C  CB    . ASP A 1 401 ? 140.621 154.617 125.651 1.00 35.70 ?  401 ASP A CB    1 
ATOM   3248  C  CG    . ASP A 1 401 ? 139.720 154.268 126.817 1.00 39.29 ?  401 ASP A CG    1 
ATOM   3249  O  OD1   . ASP A 1 401 ? 140.218 154.216 127.960 1.00 41.78 ?  401 ASP A OD1   1 
ATOM   3250  O  OD2   . ASP A 1 401 ? 138.515 154.041 126.589 1.00 40.69 -1 401 ASP A OD2   1 
ATOM   3251  N  N     . GLU A 1 402 ? 143.694 155.046 124.637 1.00 33.55 ?  402 GLU A N     1 
ATOM   3252  C  CA    . GLU A 1 402 ? 144.513 155.128 123.433 1.00 32.92 ?  402 GLU A CA    1 
ATOM   3253  C  C     . GLU A 1 402 ? 143.931 154.167 122.404 1.00 31.86 ?  402 GLU A C     1 
ATOM   3254  O  O     . GLU A 1 402 ? 144.089 152.949 122.523 1.00 39.81 ?  402 GLU A O     1 
ATOM   3255  C  CB    . GLU A 1 402 ? 145.970 154.792 123.741 1.00 36.93 ?  402 GLU A CB    1 
ATOM   3256  C  CG    . GLU A 1 402 ? 146.652 155.772 124.677 1.00 36.37 ?  402 GLU A CG    1 
ATOM   3257  C  CD    . GLU A 1 402 ? 147.484 155.081 125.739 1.00 43.09 ?  402 GLU A CD    1 
ATOM   3258  O  OE1   . GLU A 1 402 ? 148.664 154.776 125.467 1.00 43.53 ?  402 GLU A OE1   1 
ATOM   3259  O  OE2   . GLU A 1 402 ? 146.958 154.844 126.846 1.00 43.84 -1 402 GLU A OE2   1 
ATOM   3260  N  N     . ILE A 1 403 ? 143.258 154.712 121.400 1.00 29.35 ?  403 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 403 ? 142.557 153.910 120.406 1.00 30.38 ?  403 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 403 ? 143.537 153.492 119.319 1.00 29.83 ?  403 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 403 ? 144.225 154.334 118.730 1.00 31.37 ?  403 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 403 ? 141.372 154.690 119.813 1.00 27.23 ?  403 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 403 ? 140.338 154.994 120.901 1.00 30.31 ?  403 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 403 ? 140.743 153.916 118.670 1.00 22.57 ?  403 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 403 ? 139.971 153.798 121.751 1.00 30.63 ?  403 ILE A CD1   1 
ATOM   3268  N  N     . GLY A 1 404 ? 143.599 152.189 119.052 1.00 24.83 ?  404 GLY A N     1 
ATOM   3269  C  CA    . GLY A 1 404 ? 144.456 151.665 118.008 1.00 15.92 ?  404 GLY A CA    1 
ATOM   3270  C  C     . GLY A 1 404 ? 143.736 151.475 116.691 1.00 22.98 ?  404 GLY A C     1 
ATOM   3271  O  O     . GLY A 1 404 ? 142.847 152.257 116.345 1.00 33.56 ?  404 GLY A O     1 
ATOM   3272  N  N     . LEU A 1 405 ? 144.110 150.439 115.942 1.00 21.63 ?  405 LEU A N     1 
ATOM   3273  C  CA    . LEU A 1 405 ? 143.511 150.142 114.645 1.00 8.88  ?  405 LEU A CA    1 
ATOM   3274  C  C     . LEU A 1 405 ? 143.026 148.699 114.651 1.00 15.28 ?  405 LEU A C     1 
ATOM   3275  O  O     . LEU A 1 405 ? 143.838 147.770 114.680 1.00 16.33 ?  405 LEU A O     1 
ATOM   3276  C  CB    . LEU A 1 405 ? 144.508 150.370 113.509 1.00 18.00 ?  405 LEU A CB    1 
ATOM   3277  C  CG    . LEU A 1 405 ? 145.046 151.786 113.304 1.00 17.66 ?  405 LEU A CG    1 
ATOM   3278  C  CD1   . LEU A 1 405 ? 146.170 151.777 112.285 1.00 18.80 ?  405 LEU A CD1   1 
ATOM   3279  C  CD2   . LEU A 1 405 ? 143.942 152.733 112.879 1.00 16.03 ?  405 LEU A CD2   1 
ATOM   3280  N  N     . ASP A 1 406 ? 141.711 148.513 114.619 1.00 23.95 ?  406 ASP A N     1 
ATOM   3281  C  CA    . ASP A 1 406 ? 141.107 147.191 114.537 1.00 12.97 ?  406 ASP A CA    1 
ATOM   3282  C  C     . ASP A 1 406 ? 140.568 146.964 113.132 1.00 17.53 ?  406 ASP A C     1 
ATOM   3283  O  O     . ASP A 1 406 ? 139.883 147.822 112.569 1.00 31.72 ?  406 ASP A O     1 
ATOM   3284  C  CB    . ASP A 1 406 ? 139.988 147.032 115.565 1.00 16.10 ?  406 ASP A CB    1 
ATOM   3285  C  CG    . ASP A 1 406 ? 140.506 146.644 116.937 1.00 30.19 ?  406 ASP A CG    1 
ATOM   3286  O  OD1   . ASP A 1 406 ? 141.712 146.345 117.062 1.00 30.73 ?  406 ASP A OD1   1 
ATOM   3287  O  OD2   . ASP A 1 406 ? 139.709 146.642 117.897 1.00 30.34 -1 406 ASP A OD2   1 
ATOM   3288  N  N     . ILE A 1 407 ? 140.861 145.798 112.580 1.00 23.30 ?  407 ILE A N     1 
ATOM   3289  C  CA    . ILE A 1 407 ? 140.649 145.549 111.161 1.00 17.70 ?  407 ILE A CA    1 
ATOM   3290  C  C     . ILE A 1 407 ? 139.176 145.287 110.880 1.00 18.01 ?  407 ILE A C     1 
ATOM   3291  O  O     . ILE A 1 407 ? 138.476 144.637 111.664 1.00 21.33 ?  407 ILE A O     1 
ATOM   3292  C  CB    . ILE A 1 407 ? 141.521 144.370 110.696 1.00 13.02 ?  407 ILE A CB    1 
ATOM   3293  C  CG1   . ILE A 1 407 ? 142.996 144.649 110.972 1.00 2.81  ?  407 ILE A CG1   1 
ATOM   3294  C  CG2   . ILE A 1 407 ? 141.307 144.097 109.235 1.00 16.48 ?  407 ILE A CG2   1 
ATOM   3295  C  CD1   . ILE A 1 407 ? 143.753 143.432 111.415 1.00 18.29 ?  407 ILE A CD1   1 
ATOM   3296  N  N     . SER A 1 408 ? 138.707 145.804 109.746 1.00 27.38 ?  408 SER A N     1 
ATOM   3297  C  CA    . SER A 1 408 ? 137.412 145.459 109.180 1.00 20.37 ?  408 SER A CA    1 
ATOM   3298  C  C     . SER A 1 408 ? 137.418 145.889 107.720 1.00 24.30 ?  408 SER A C     1 
ATOM   3299  O  O     . SER A 1 408 ? 137.868 146.992 107.399 1.00 36.21 ?  408 SER A O     1 
ATOM   3300  C  CB    . SER A 1 408 ? 136.260 146.133 109.935 1.00 21.57 ?  408 SER A CB    1 
ATOM   3301  O  OG    . SER A 1 408 ? 135.937 147.389 109.367 1.00 28.81 ?  408 SER A OG    1 
ATOM   3302  N  N     . CYS A 1 409 ? 136.933 145.017 106.842 1.00 20.11 ?  409 CYS A N     1 
ATOM   3303  C  CA    . CYS A 1 409 ? 136.850 145.332 105.425 1.00 26.27 ?  409 CYS A CA    1 
ATOM   3304  C  C     . CYS A 1 409 ? 135.510 144.875 104.870 1.00 26.33 ?  409 CYS A C     1 
ATOM   3305  O  O     . CYS A 1 409 ? 134.897 143.924 105.359 1.00 24.50 ?  409 CYS A O     1 
ATOM   3306  C  CB    . CYS A 1 409 ? 138.004 144.699 104.629 1.00 22.59 ?  409 CYS A CB    1 
ATOM   3307  S  SG    . CYS A 1 409 ? 137.896 142.916 104.387 1.00 39.49 ?  409 CYS A SG    1 
ATOM   3308  N  N     . ASN A 1 410 ? 135.057 145.581 103.838 1.00 22.83 ?  410 ASN A N     1 
ATOM   3309  C  CA    . ASN A 1 410 ? 133.818 145.252 103.156 1.00 18.43 ?  410 ASN A CA    1 
ATOM   3310  C  C     . ASN A 1 410 ? 134.109 144.243 102.059 1.00 20.75 ?  410 ASN A C     1 
ATOM   3311  O  O     . ASN A 1 410 ? 135.064 144.405 101.294 1.00 22.15 ?  410 ASN A O     1 
ATOM   3312  C  CB    . ASN A 1 410 ? 133.172 146.499 102.559 1.00 22.82 ?  410 ASN A CB    1 
ATOM   3313  C  CG    . ASN A 1 410 ? 133.860 147.766 102.992 1.00 30.14 ?  410 ASN A CG    1 
ATOM   3314  O  OD1   . ASN A 1 410 ? 134.340 147.876 104.120 1.00 31.24 ?  410 ASN A OD1   1 
ATOM   3315  N  ND2   . ASN A 1 410 ? 133.926 148.733 102.090 1.00 28.88 ?  410 ASN A ND2   1 
ATOM   3316  N  N     . LEU A 1 411 ? 133.282 143.212 101.980 1.00 17.79 ?  411 LEU A N     1 
ATOM   3317  C  CA    . LEU A 1 411 ? 133.502 142.108 101.063 1.00 12.06 ?  411 LEU A CA    1 
ATOM   3318  C  C     . LEU A 1 411 ? 132.671 142.288 99.800  1.00 13.10 ?  411 LEU A C     1 
ATOM   3319  O  O     . LEU A 1 411 ? 131.585 142.870 99.821  1.00 19.18 ?  411 LEU A O     1 
ATOM   3320  C  CB    . LEU A 1 411 ? 133.153 140.779 101.733 1.00 21.93 ?  411 LEU A CB    1 
ATOM   3321  C  CG    . LEU A 1 411 ? 133.872 140.451 103.039 1.00 14.94 ?  411 LEU A CG    1 
ATOM   3322  C  CD1   . LEU A 1 411 ? 133.799 138.970 103.305 1.00 20.54 ?  411 LEU A CD1   1 
ATOM   3323  C  CD2   . LEU A 1 411 ? 135.319 140.897 102.983 1.00 19.17 ?  411 LEU A CD2   1 
ATOM   3324  N  N     . GLY A 1 412 ? 133.205 141.784 98.693  1.00 21.24 ?  412 GLY A N     1 
ATOM   3325  C  CA    . GLY A 1 412 ? 132.508 141.777 97.426  1.00 10.26 ?  412 GLY A CA    1 
ATOM   3326  C  C     . GLY A 1 412 ? 133.209 140.851 96.460  1.00 11.55 ?  412 GLY A C     1 
ATOM   3327  O  O     . GLY A 1 412 ? 134.441 140.828 96.413  1.00 25.53 ?  412 GLY A O     1 
ATOM   3328  N  N     . SER A 1 413 ? 132.453 140.080 95.687  1.00 15.23 ?  413 SER A N     1 
ATOM   3329  C  CA    . SER A 1 413 ? 133.022 139.052 94.829  1.00 9.33  ?  413 SER A CA    1 
ATOM   3330  C  C     . SER A 1 413 ? 132.716 139.346 93.370  1.00 15.97 ?  413 SER A C     1 
ATOM   3331  O  O     . SER A 1 413 ? 131.573 139.652 93.020  1.00 24.07 ?  413 SER A O     1 
ATOM   3332  C  CB    . SER A 1 413 ? 132.488 137.671 95.203  1.00 10.90 ?  413 SER A CB    1 
ATOM   3333  O  OG    . SER A 1 413 ? 133.013 137.252 96.447  1.00 29.53 ?  413 SER A OG    1 
ATOM   3334  N  N     . LEU A 1 414 ? 133.740 139.253 92.529  1.00 20.43 ?  414 LEU A N     1 
ATOM   3335  C  CA    . LEU A 1 414 ? 133.534 139.187 91.093  1.00 13.30 ?  414 LEU A CA    1 
ATOM   3336  C  C     . LEU A 1 414 ? 133.126 137.774 90.705  1.00 21.18 ?  414 LEU A C     1 
ATOM   3337  O  O     . LEU A 1 414 ? 133.647 136.794 91.242  1.00 21.96 ?  414 LEU A O     1 
ATOM   3338  C  CB    . LEU A 1 414 ? 134.806 139.577 90.342  1.00 14.83 ?  414 LEU A CB    1 
ATOM   3339  C  CG    . LEU A 1 414 ? 135.567 140.820 90.791  1.00 19.22 ?  414 LEU A CG    1 
ATOM   3340  C  CD1   . LEU A 1 414 ? 136.884 140.903 90.045  1.00 24.86 ?  414 LEU A CD1   1 
ATOM   3341  C  CD2   . LEU A 1 414 ? 134.737 142.065 90.552  1.00 24.81 ?  414 LEU A CD2   1 
ATOM   3342  N  N     . ASN A 1 415 ? 132.189 137.669 89.772  1.00 28.22 ?  415 ASN A N     1 
ATOM   3343  C  CA    . ASN A 1 415 ? 131.842 136.385 89.179  1.00 25.19 ?  415 ASN A CA    1 
ATOM   3344  C  C     . ASN A 1 415 ? 132.748 136.179 87.973  1.00 27.36 ?  415 ASN A C     1 
ATOM   3345  O  O     . ASN A 1 415 ? 132.569 136.827 86.939  1.00 29.83 ?  415 ASN A O     1 
ATOM   3346  C  CB    . ASN A 1 415 ? 130.369 136.344 88.790  1.00 20.33 ?  415 ASN A CB    1 
ATOM   3347  C  CG    . ASN A 1 415 ? 129.850 134.934 88.607  1.00 23.73 ?  415 ASN A CG    1 
ATOM   3348  O  OD1   . ASN A 1 415 ? 130.450 134.127 87.901  1.00 32.26 ?  415 ASN A OD1   1 
ATOM   3349  N  ND2   . ASN A 1 415 ? 128.728 134.632 89.244  1.00 30.02 ?  415 ASN A ND2   1 
ATOM   3350  N  N     . ILE A 1 416 ? 133.723 135.278 88.113  1.00 19.85 ?  416 ILE A N     1 
ATOM   3351  C  CA    . ILE A 1 416 ? 134.742 135.110 87.081  1.00 22.02 ?  416 ILE A CA    1 
ATOM   3352  C  C     . ILE A 1 416 ? 134.109 134.688 85.763  1.00 28.81 ?  416 ILE A C     1 
ATOM   3353  O  O     . ILE A 1 416 ? 134.501 135.162 84.690  1.00 26.69 ?  416 ILE A O     1 
ATOM   3354  C  CB    . ILE A 1 416 ? 135.813 134.107 87.549  1.00 24.02 ?  416 ILE A CB    1 
ATOM   3355  C  CG1   . ILE A 1 416 ? 136.588 134.681 88.736  1.00 21.73 ?  416 ILE A CG1   1 
ATOM   3356  C  CG2   . ILE A 1 416 ? 136.764 133.769 86.419  1.00 15.94 ?  416 ILE A CG2   1 
ATOM   3357  C  CD1   . ILE A 1 416 ? 137.498 133.688 89.415  1.00 19.62 ?  416 ILE A CD1   1 
ATOM   3358  N  N     . LEU A 1 417 ? 133.109 133.806 85.819  1.00 23.98 ?  417 LEU A N     1 
ATOM   3359  C  CA    . LEU A 1 417 ? 132.461 133.342 84.596  1.00 27.03 ?  417 LEU A CA    1 
ATOM   3360  C  C     . LEU A 1 417 ? 131.768 134.487 83.867  1.00 28.59 ?  417 LEU A C     1 
ATOM   3361  O  O     . LEU A 1 417 ? 131.956 134.673 82.659  1.00 36.05 ?  417 LEU A O     1 
ATOM   3362  C  CB    . LEU A 1 417 ? 131.464 132.233 84.924  1.00 27.64 ?  417 LEU A CB    1 
ATOM   3363  C  CG    . LEU A 1 417 ? 130.924 131.426 83.744  1.00 25.66 ?  417 LEU A CG    1 
ATOM   3364  C  CD1   . LEU A 1 417 ? 130.896 129.959 84.096  1.00 26.86 ?  417 LEU A CD1   1 
ATOM   3365  C  CD2   . LEU A 1 417 ? 129.538 131.906 83.358  1.00 32.99 ?  417 LEU A CD2   1 
ATOM   3366  N  N     . ASN A 1 418 ? 130.963 135.269 84.587  1.00 30.17 ?  418 ASN A N     1 
ATOM   3367  C  CA    . ASN A 1 418 ? 130.207 136.341 83.949  1.00 30.26 ?  418 ASN A CA    1 
ATOM   3368  C  C     . ASN A 1 418 ? 131.090 137.527 83.592  1.00 29.72 ?  418 ASN A C     1 
ATOM   3369  O  O     . ASN A 1 418 ? 130.831 138.206 82.591  1.00 32.38 ?  418 ASN A O     1 
ATOM   3370  C  CB    . ASN A 1 418 ? 129.064 136.787 84.860  1.00 26.41 ?  418 ASN A CB    1 
ATOM   3371  C  CG    . ASN A 1 418 ? 127.998 135.726 85.013  1.00 31.04 ?  418 ASN A CG    1 
ATOM   3372  O  OD1   . ASN A 1 418 ? 127.684 135.006 84.067  1.00 36.97 ?  418 ASN A OD1   1 
ATOM   3373  N  ND2   . ASN A 1 418 ? 127.436 135.617 86.210  1.00 32.23 ?  418 ASN A ND2   1 
ATOM   3374  N  N     . VAL A 1 419 ? 132.122 137.795 84.391  1.00 29.60 ?  419 VAL A N     1 
ATOM   3375  C  CA    . VAL A 1 419 ? 133.069 138.852 84.053  1.00 28.99 ?  419 VAL A CA    1 
ATOM   3376  C  C     . VAL A 1 419 ? 133.841 138.490 82.791  1.00 31.93 ?  419 VAL A C     1 
ATOM   3377  O  O     . VAL A 1 419 ? 134.043 139.330 81.907  1.00 35.55 ?  419 VAL A O     1 
ATOM   3378  C  CB    . VAL A 1 419 ? 134.008 139.119 85.244  1.00 27.28 ?  419 VAL A CB    1 
ATOM   3379  C  CG1   . VAL A 1 419 ? 135.255 139.835 84.792  1.00 31.92 ?  419 VAL A CG1   1 
ATOM   3380  C  CG2   . VAL A 1 419 ? 133.294 139.927 86.306  1.00 27.21 ?  419 VAL A CG2   1 
ATOM   3381  N  N     . MET A 1 420 ? 134.273 137.231 82.680  1.00 37.60 ?  420 MET A N     1 
ATOM   3382  C  CA    . MET A 1 420 ? 135.015 136.795 81.503  1.00 31.13 ?  420 MET A CA    1 
ATOM   3383  C  C     . MET A 1 420 ? 134.123 136.708 80.273  1.00 29.91 ?  420 MET A C     1 
ATOM   3384  O  O     . MET A 1 420 ? 134.582 136.980 79.158  1.00 35.71 ?  420 MET A O     1 
ATOM   3385  C  CB    . MET A 1 420 ? 135.678 135.447 81.776  1.00 32.87 ?  420 MET A CB    1 
ATOM   3386  C  CG    . MET A 1 420 ? 136.952 135.544 82.594  1.00 30.68 ?  420 MET A CG    1 
ATOM   3387  S  SD    . MET A 1 420 ? 138.175 136.613 81.824  1.00 39.19 ?  420 MET A SD    1 
ATOM   3388  C  CE    . MET A 1 420 ? 138.896 135.490 80.632  1.00 30.33 ?  420 MET A CE    1 
ATOM   3389  N  N     . GLU A 1 421 ? 132.857 136.325 80.450  1.00 38.79 ?  421 GLU A N     1 
ATOM   3390  C  CA    . GLU A 1 421 ? 131.927 136.291 79.326  1.00 37.01 ?  421 GLU A CA    1 
ATOM   3391  C  C     . GLU A 1 421 ? 131.692 137.686 78.764  1.00 41.48 ?  421 GLU A C     1 
ATOM   3392  O  O     . GLU A 1 421 ? 131.633 137.870 77.542  1.00 43.64 ?  421 GLU A O     1 
ATOM   3393  C  CB    . GLU A 1 421 ? 130.605 135.662 79.761  1.00 35.64 ?  421 GLU A CB    1 
ATOM   3394  C  CG    . GLU A 1 421 ? 130.557 134.150 79.632  1.00 40.90 ?  421 GLU A CG    1 
ATOM   3395  C  CD    . GLU A 1 421 ? 129.223 133.575 80.067  1.00 46.28 ?  421 GLU A CD    1 
ATOM   3396  O  OE1   . GLU A 1 421 ? 128.443 134.308 80.709  1.00 45.01 ?  421 GLU A OE1   1 
ATOM   3397  O  OE2   . GLU A 1 421 ? 128.955 132.393 79.766  1.00 45.47 -1 421 GLU A OE2   1 
ATOM   3398  N  N     . HIS A 1 422 ? 131.557 138.681 79.638  1.00 37.78 ?  422 HIS A N     1 
ATOM   3399  C  CA    . HIS A 1 422 ? 131.310 140.053 79.221  1.00 34.71 ?  422 HIS A CA    1 
ATOM   3400  C  C     . HIS A 1 422 ? 132.581 140.797 78.839  1.00 39.06 ?  422 HIS A C     1 
ATOM   3401  O  O     . HIS A 1 422 ? 132.487 141.938 78.372  1.00 39.00 ?  422 HIS A O     1 
ATOM   3402  C  CB    . HIS A 1 422 ? 130.586 140.815 80.333  1.00 34.38 ?  422 HIS A CB    1 
ATOM   3403  C  CG    . HIS A 1 422 ? 129.211 140.303 80.621  1.00 36.59 ?  422 HIS A CG    1 
ATOM   3404  N  ND1   . HIS A 1 422 ? 128.967 139.307 81.540  1.00 36.17 ?  422 HIS A ND1   1 
ATOM   3405  C  CD2   . HIS A 1 422 ? 128.004 140.650 80.113  1.00 38.64 ?  422 HIS A CD2   1 
ATOM   3406  C  CE1   . HIS A 1 422 ? 127.670 139.059 81.586  1.00 39.68 ?  422 HIS A CE1   1 
ATOM   3407  N  NE2   . HIS A 1 422 ? 127.063 139.860 80.729  1.00 41.23 ?  422 HIS A NE2   1 
ATOM   3408  N  N     . LYS A 1 423 ? 133.751 140.183 79.019  1.00 42.93 ?  423 LYS A N     1 
ATOM   3409  C  CA    . LYS A 1 423 ? 135.038 140.822 78.746  1.00 43.56 ?  423 LYS A CA    1 
ATOM   3410  C  C     . LYS A 1 423 ? 135.137 142.167 79.461  1.00 43.41 ?  423 LYS A C     1 
ATOM   3411  O  O     . LYS A 1 423 ? 135.516 143.186 78.881  1.00 46.66 ?  423 LYS A O     1 
ATOM   3412  C  CB    . LYS A 1 423 ? 135.264 140.983 77.242  1.00 40.83 ?  423 LYS A CB    1 
ATOM   3413  C  CG    . LYS A 1 423 ? 135.024 139.719 76.439  1.00 42.34 ?  423 LYS A CG    1 
ATOM   3414  C  CD    . LYS A 1 423 ? 136.304 138.917 76.288  1.00 46.49 ?  423 LYS A CD    1 
ATOM   3415  C  CE    . LYS A 1 423 ? 136.014 137.468 75.934  1.00 46.50 ?  423 LYS A CE    1 
ATOM   3416  N  NZ    . LYS A 1 423 ? 135.835 136.622 77.146  1.00 44.64 1  423 LYS A NZ    1 
ATOM   3417  N  N     . SER A 1 424 ? 134.787 142.159 80.742  1.00 33.13 ?  424 SER A N     1 
ATOM   3418  C  CA    . SER A 1 424 ? 134.624 143.380 81.523  1.00 32.99 ?  424 SER A CA    1 
ATOM   3419  C  C     . SER A 1 424 ? 135.349 143.275 82.853  1.00 36.41 ?  424 SER A C     1 
ATOM   3420  O  O     . SER A 1 424 ? 134.793 143.569 83.912  1.00 39.49 ?  424 SER A O     1 
ATOM   3421  C  CB    . SER A 1 424 ? 133.146 143.677 81.751  1.00 35.65 ?  424 SER A CB    1 
ATOM   3422  O  OG    . SER A 1 424 ? 132.590 142.771 82.687  1.00 32.10 ?  424 SER A OG    1 
ATOM   3423  N  N     . ILE A 1 425 ? 136.612 142.846 82.825  1.00 34.09 ?  425 ILE A N     1 
ATOM   3424  C  CA    . ILE A 1 425 ? 137.396 142.807 84.058  1.00 28.18 ?  425 ILE A CA    1 
ATOM   3425  C  C     . ILE A 1 425 ? 137.604 144.218 84.594  1.00 31.11 ?  425 ILE A C     1 
ATOM   3426  O  O     . ILE A 1 425 ? 137.384 144.489 85.779  1.00 36.98 ?  425 ILE A O     1 
ATOM   3427  C  CB    . ILE A 1 425 ? 138.735 142.085 83.828  1.00 32.28 ?  425 ILE A CB    1 
ATOM   3428  C  CG1   . ILE A 1 425 ? 138.525 140.572 83.791  1.00 33.29 ?  425 ILE A CG1   1 
ATOM   3429  C  CG2   . ILE A 1 425 ? 139.734 142.449 84.915  1.00 28.28 ?  425 ILE A CG2   1 
ATOM   3430  C  CD1   . ILE A 1 425 ? 139.770 139.784 83.497  1.00 32.74 ?  425 ILE A CD1   1 
ATOM   3431  N  N     . GLU A 1 426 ? 138.001 145.144 83.719  1.00 28.74 ?  426 GLU A N     1 
ATOM   3432  C  CA    . GLU A 1 426 ? 138.318 146.500 84.157  1.00 27.28 ?  426 GLU A CA    1 
ATOM   3433  C  C     . GLU A 1 426 ? 137.097 147.199 84.741  1.00 30.36 ?  426 GLU A C     1 
ATOM   3434  O  O     . GLU A 1 426 ? 137.143 147.723 85.861  1.00 37.14 ?  426 GLU A O     1 
ATOM   3435  C  CB    . GLU A 1 426 ? 138.882 147.300 82.986  1.00 29.43 ?  426 GLU A CB    1 
ATOM   3436  C  CG    . GLU A 1 426 ? 138.878 148.800 83.201  1.00 33.41 ?  426 GLU A CG    1 
ATOM   3437  C  CD    . GLU A 1 426 ? 139.590 149.547 82.094  1.00 39.47 ?  426 GLU A CD    1 
ATOM   3438  O  OE1   . GLU A 1 426 ? 139.870 148.931 81.044  1.00 38.35 ?  426 GLU A OE1   1 
ATOM   3439  O  OE2   . GLU A 1 426 ? 139.868 150.751 82.273  1.00 38.54 -1 426 GLU A OE2   1 
ATOM   3440  N  N     . LYS A 1 427 ? 135.994 147.218 83.992  1.00 32.91 ?  427 LYS A N     1 
ATOM   3441  C  CA    . LYS A 1 427 ? 134.806 147.936 84.439  1.00 28.97 ?  427 LYS A CA    1 
ATOM   3442  C  C     . LYS A 1 427 ? 134.223 147.310 85.697  1.00 30.16 ?  427 LYS A C     1 
ATOM   3443  O  O     . LYS A 1 427 ? 133.832 148.025 86.626  1.00 36.77 ?  427 LYS A O     1 
ATOM   3444  C  CB    . LYS A 1 427 ? 133.735 148.008 83.337  1.00 34.40 ?  427 LYS A CB    1 
ATOM   3445  C  CG    . LYS A 1 427 ? 134.080 148.669 81.967  1.00 38.16 ?  427 LYS A CG    1 
ATOM   3446  C  CD    . LYS A 1 427 ? 135.389 148.290 81.261  1.00 38.84 ?  427 LYS A CD    1 
ATOM   3447  C  CE    . LYS A 1 427 ? 135.515 146.789 81.033  1.00 34.59 ?  427 LYS A CE    1 
ATOM   3448  N  NZ    . LYS A 1 427 ? 136.816 146.420 80.410  1.00 35.02 1  427 LYS A NZ    1 
ATOM   3449  N  N     . THR A 1 428 ? 134.158 145.977 85.748  1.00 29.14 ?  428 THR A N     1 
ATOM   3450  C  CA    . THR A 1 428 ? 133.632 145.317 86.937  1.00 22.10 ?  428 THR A CA    1 
ATOM   3451  C  C     . THR A 1 428 ? 134.503 145.595 88.152  1.00 28.69 ?  428 THR A C     1 
ATOM   3452  O  O     . THR A 1 428 ? 133.987 145.890 89.234  1.00 31.20 ?  428 THR A O     1 
ATOM   3453  C  CB    . THR A 1 428 ? 133.511 143.813 86.710  1.00 24.52 ?  428 THR A CB    1 
ATOM   3454  O  OG1   . THR A 1 428 ? 132.903 143.566 85.437  1.00 28.64 ?  428 THR A OG1   1 
ATOM   3455  C  CG2   . THR A 1 428 ? 132.661 143.189 87.798  1.00 25.65 ?  428 THR A CG2   1 
ATOM   3456  N  N     . VAL A 1 429 ? 135.826 145.515 87.994  1.00 28.73 ?  429 VAL A N     1 
ATOM   3457  C  CA    . VAL A 1 429 ? 136.718 145.745 89.127  1.00 22.63 ?  429 VAL A CA    1 
ATOM   3458  C  C     . VAL A 1 429 ? 136.592 147.179 89.622  1.00 23.97 ?  429 VAL A C     1 
ATOM   3459  O  O     . VAL A 1 429 ? 136.518 147.426 90.829  1.00 30.65 ?  429 VAL A O     1 
ATOM   3460  C  CB    . VAL A 1 429 ? 138.171 145.398 88.751  1.00 24.00 ?  429 VAL A CB    1 
ATOM   3461  C  CG1   . VAL A 1 429 ? 139.130 145.992 89.759  1.00 19.09 ?  429 VAL A CG1   1 
ATOM   3462  C  CG2   . VAL A 1 429 ? 138.358 143.896 88.691  1.00 23.11 ?  429 VAL A CG2   1 
ATOM   3463  N  N     . LYS A 1 430 ? 136.539 148.145 88.701  1.00 24.20 ?  430 LYS A N     1 
ATOM   3464  C  CA    . LYS A 1 430 ? 136.454 149.541 89.118  1.00 23.38 ?  430 LYS A CA    1 
ATOM   3465  C  C     . LYS A 1 430 ? 135.114 149.853 89.777  1.00 23.32 ?  430 LYS A C     1 
ATOM   3466  O  O     . LYS A 1 430 ? 135.068 150.544 90.802  1.00 31.57 ?  430 LYS A O     1 
ATOM   3467  C  CB    . LYS A 1 430 ? 136.708 150.456 87.922  1.00 24.45 ?  430 LYS A CB    1 
ATOM   3468  C  CG    . LYS A 1 430 ? 138.120 150.340 87.374  1.00 26.85 ?  430 LYS A CG    1 
ATOM   3469  C  CD    . LYS A 1 430 ? 138.502 151.537 86.530  1.00 29.76 ?  430 LYS A CD    1 
ATOM   3470  C  CE    . LYS A 1 430 ? 139.948 151.438 86.081  1.00 29.64 ?  430 LYS A CE    1 
ATOM   3471  N  NZ    . LYS A 1 430 ? 140.349 152.593 85.234  1.00 33.48 1  430 LYS A NZ    1 
ATOM   3472  N  N     . LEU A 1 431 ? 134.012 149.349 89.214  1.00 24.92 ?  431 LEU A N     1 
ATOM   3473  C  CA    . LEU A 1 431 ? 132.704 149.595 89.813  1.00 20.54 ?  431 LEU A CA    1 
ATOM   3474  C  C     . LEU A 1 431 ? 132.575 148.911 91.169  1.00 22.83 ?  431 LEU A C     1 
ATOM   3475  O  O     . LEU A 1 431 ? 131.994 149.476 92.103  1.00 28.68 ?  431 LEU A O     1 
ATOM   3476  C  CB    . LEU A 1 431 ? 131.602 149.126 88.867  1.00 27.17 ?  431 LEU A CB    1 
ATOM   3477  C  CG    . LEU A 1 431 ? 130.917 150.189 88.007  1.00 30.22 ?  431 LEU A CG    1 
ATOM   3478  C  CD1   . LEU A 1 431 ? 129.809 149.559 87.183  1.00 29.53 ?  431 LEU A CD1   1 
ATOM   3479  C  CD2   . LEU A 1 431 ? 130.374 151.313 88.869  1.00 31.29 ?  431 LEU A CD2   1 
ATOM   3480  N  N     . ALA A 1 432 ? 133.105 147.692 91.297  1.00 24.46 ?  432 ALA A N     1 
ATOM   3481  C  CA    . ALA A 1 432 ? 133.094 147.005 92.582  1.00 15.27 ?  432 ALA A CA    1 
ATOM   3482  C  C     . ALA A 1 432 ? 133.946 147.741 93.604  1.00 26.11 ?  432 ALA A C     1 
ATOM   3483  O  O     . ALA A 1 432 ? 133.588 147.813 94.783  1.00 28.99 ?  432 ALA A O     1 
ATOM   3484  C  CB    . ALA A 1 432 ? 133.585 145.570 92.409  1.00 21.06 ?  432 ALA A CB    1 
ATOM   3485  N  N     . THR A 1 433 ? 135.084 148.287 93.170  1.00 28.03 ?  433 THR A N     1 
ATOM   3486  C  CA    . THR A 1 433 ? 135.911 149.086 94.064  1.00 21.24 ?  433 THR A CA    1 
ATOM   3487  C  C     . THR A 1 433 ? 135.162 150.322 94.538  1.00 23.51 ?  433 THR A C     1 
ATOM   3488  O  O     . THR A 1 433 ? 135.224 150.678 95.720  1.00 34.90 ?  433 THR A O     1 
ATOM   3489  C  CB    . THR A 1 433 ? 137.209 149.480 93.362  1.00 27.47 ?  433 THR A CB    1 
ATOM   3490  O  OG1   . THR A 1 433 ? 137.924 148.299 92.977  1.00 29.32 ?  433 THR A OG1   1 
ATOM   3491  C  CG2   . THR A 1 433 ? 138.084 150.317 94.281  1.00 24.32 ?  433 THR A CG2   1 
ATOM   3492  N  N     . ASP A 1 434 ? 134.444 150.986 93.632  1.00 22.85 ?  434 ASP A N     1 
ATOM   3493  C  CA    . ASP A 1 434 ? 133.650 152.147 94.023  1.00 22.59 ?  434 ASP A CA    1 
ATOM   3494  C  C     . ASP A 1 434 ? 132.561 151.765 95.021  1.00 20.26 ?  434 ASP A C     1 
ATOM   3495  O  O     . ASP A 1 434 ? 132.338 152.472 96.011  1.00 24.84 ?  434 ASP A O     1 
ATOM   3496  C  CB    . ASP A 1 434 ? 133.034 152.801 92.788  1.00 24.86 ?  434 ASP A CB    1 
ATOM   3497  C  CG    . ASP A 1 434 ? 134.076 153.371 91.851  1.00 31.71 ?  434 ASP A CG    1 
ATOM   3498  O  OD1   . ASP A 1 434 ? 135.194 153.671 92.316  1.00 35.06 ?  434 ASP A OD1   1 
ATOM   3499  O  OD2   . ASP A 1 434 ? 133.776 153.522 90.648  1.00 33.12 -1 434 ASP A OD2   1 
ATOM   3500  N  N     . SER A 1 435 ? 131.869 150.651 94.773  1.00 22.09 ?  435 SER A N     1 
ATOM   3501  C  CA    . SER A 1 435 ? 130.810 150.217 95.682  1.00 20.46 ?  435 SER A CA    1 
ATOM   3502  C  C     . SER A 1 435 ? 131.365 149.861 97.055  1.00 23.29 ?  435 SER A C     1 
ATOM   3503  O  O     . SER A 1 435 ? 130.774 150.213 98.084  1.00 29.51 ?  435 SER A O     1 
ATOM   3504  C  CB    . SER A 1 435 ? 130.060 149.031 95.079  1.00 23.10 ?  435 SER A CB    1 
ATOM   3505  O  OG    . SER A 1 435 ? 130.823 147.844 95.173  1.00 20.02 ?  435 SER A OG    1 
ATOM   3506  N  N     . LEU A 1 436 ? 132.506 149.170 97.094  1.00 19.07 ?  436 LEU A N     1 
ATOM   3507  C  CA    . LEU A 1 436 ? 133.117 148.818 98.371  1.00 10.90 ?  436 LEU A CA    1 
ATOM   3508  C  C     . LEU A 1 436 ? 133.624 150.056 99.099  1.00 17.35 ?  436 LEU A C     1 
ATOM   3509  O  O     . LEU A 1 436 ? 133.544 150.135 100.329 1.00 21.46 ?  436 LEU A O     1 
ATOM   3510  C  CB    . LEU A 1 436 ? 134.246 147.815 98.146  1.00 22.54 ?  436 LEU A CB    1 
ATOM   3511  C  CG    . LEU A 1 436 ? 133.817 146.415 97.704  1.00 19.18 ?  436 LEU A CG    1 
ATOM   3512  C  CD1   . LEU A 1 436 ? 135.007 145.612 97.208  1.00 10.93 ?  436 LEU A CD1   1 
ATOM   3513  C  CD2   . LEU A 1 436 ? 133.111 145.689 98.830  1.00 20.99 ?  436 LEU A CD2   1 
ATOM   3514  N  N     . THR A 1 437 ? 134.144 151.035 98.356  1.00 23.18 ?  437 THR A N     1 
ATOM   3515  C  CA    . THR A 1 437 ? 134.538 152.302 98.962  1.00 21.46 ?  437 THR A CA    1 
ATOM   3516  C  C     . THR A 1 437 ? 133.341 153.009 99.579  1.00 24.16 ?  437 THR A C     1 
ATOM   3517  O  O     . THR A 1 437 ? 133.436 153.564 100.679 1.00 35.32 ?  437 THR A O     1 
ATOM   3518  C  CB    . THR A 1 437 ? 135.202 153.194 97.916  1.00 19.83 ?  437 THR A CB    1 
ATOM   3519  O  OG1   . THR A 1 437 ? 136.190 152.441 97.204  1.00 21.94 ?  437 THR A OG1   1 
ATOM   3520  C  CG2   . THR A 1 437 ? 135.858 154.392 98.573  1.00 22.56 ?  437 THR A CG2   1 
ATOM   3521  N  N     . HIS A 1 438 ? 132.204 153.005 98.881  1.00 21.99 ?  438 HIS A N     1 
ATOM   3522  C  CA    . HIS A 1 438 ? 131.001 153.619 99.432  1.00 23.39 ?  438 HIS A CA    1 
ATOM   3523  C  C     . HIS A 1 438 ? 130.538 152.893 100.689 1.00 23.90 ?  438 HIS A C     1 
ATOM   3524  O  O     . HIS A 1 438 ? 130.124 153.529 101.666 1.00 31.71 ?  438 HIS A O     1 
ATOM   3525  C  CB    . HIS A 1 438 ? 129.891 153.638 98.383  1.00 26.69 ?  438 HIS A CB    1 
ATOM   3526  C  CG    . HIS A 1 438 ? 128.591 154.168 98.897  1.00 27.28 ?  438 HIS A CG    1 
ATOM   3527  N  ND1   . HIS A 1 438 ? 128.323 155.517 98.994  1.00 27.32 ?  438 HIS A ND1   1 
ATOM   3528  C  CD2   . HIS A 1 438 ? 127.484 153.533 99.349  1.00 28.60 ?  438 HIS A CD2   1 
ATOM   3529  C  CE1   . HIS A 1 438 ? 127.108 155.689 99.481  1.00 31.76 ?  438 HIS A CE1   1 
ATOM   3530  N  NE2   . HIS A 1 438 ? 126.578 154.500 99.706  1.00 31.05 ?  438 HIS A NE2   1 
ATOM   3531  N  N     . VAL A 1 439 ? 130.596 151.559 100.682 1.00 25.03 ?  439 VAL A N     1 
ATOM   3532  C  CA    . VAL A 1 439 ? 130.203 150.798 101.865 1.00 20.09 ?  439 VAL A CA    1 
ATOM   3533  C  C     . VAL A 1 439 ? 131.129 151.113 103.034 1.00 27.11 ?  439 VAL A C     1 
ATOM   3534  O  O     . VAL A 1 439 ? 130.688 151.229 104.182 1.00 36.62 ?  439 VAL A O     1 
ATOM   3535  C  CB    . VAL A 1 439 ? 130.174 149.290 101.552 1.00 23.14 ?  439 VAL A CB    1 
ATOM   3536  C  CG1   . VAL A 1 439 ? 129.894 148.492 102.809 1.00 24.30 ?  439 VAL A CG1   1 
ATOM   3537  C  CG2   . VAL A 1 439 ? 129.125 148.992 100.503 1.00 25.36 ?  439 VAL A CG2   1 
ATOM   3538  N  N     . SER A 1 440 ? 132.427 151.257 102.759 1.00 25.44 ?  440 SER A N     1 
ATOM   3539  C  CA    . SER A 1 440 ? 133.369 151.642 103.804 1.00 20.24 ?  440 SER A CA    1 
ATOM   3540  C  C     . SER A 1 440 ? 133.055 153.031 104.344 1.00 26.38 ?  440 SER A C     1 
ATOM   3541  O  O     . SER A 1 440 ? 133.121 153.266 105.556 1.00 34.05 ?  440 SER A O     1 
ATOM   3542  C  CB    . SER A 1 440 ? 134.799 151.590 103.266 1.00 25.82 ?  440 SER A CB    1 
ATOM   3543  O  OG    . SER A 1 440 ? 135.745 151.605 104.320 1.00 30.51 ?  440 SER A OG    1 
ATOM   3544  N  N     . GLU A 1 441 ? 132.716 153.966 103.456 1.00 29.54 ?  441 GLU A N     1 
ATOM   3545  C  CA    . GLU A 1 441 ? 132.463 155.338 103.879 1.00 21.89 ?  441 GLU A CA    1 
ATOM   3546  C  C     . GLU A 1 441 ? 131.171 155.466 104.675 1.00 31.00 ?  441 GLU A C     1 
ATOM   3547  O  O     . GLU A 1 441 ? 131.082 156.309 105.573 1.00 40.06 ?  441 GLU A O     1 
ATOM   3548  C  CB    . GLU A 1 441 ? 132.429 156.260 102.662 1.00 22.46 ?  441 GLU A CB    1 
ATOM   3549  C  CG    . GLU A 1 441 ? 133.796 156.550 102.075 1.00 28.54 ?  441 GLU A CG    1 
ATOM   3550  C  CD    . GLU A 1 441 ? 133.720 157.355 100.796 1.00 38.58 ?  441 GLU A CD    1 
ATOM   3551  O  OE1   . GLU A 1 441 ? 133.311 156.793 99.758  1.00 38.78 ?  441 GLU A OE1   1 
ATOM   3552  O  OE2   . GLU A 1 441 ? 134.067 158.554 100.825 1.00 37.83 -1 441 GLU A OE2   1 
ATOM   3553  N  N     . THR A 1 442 ? 130.162 154.655 104.365 1.00 32.28 ?  442 THR A N     1 
ATOM   3554  C  CA    . THR A 1 442 ? 128.882 154.735 105.057 1.00 31.30 ?  442 THR A CA    1 
ATOM   3555  C  C     . THR A 1 442 ? 128.825 153.881 106.315 1.00 32.40 ?  442 THR A C     1 
ATOM   3556  O  O     . THR A 1 442 ? 127.800 153.887 107.004 1.00 38.71 ?  442 THR A O     1 
ATOM   3557  C  CB    . THR A 1 442 ? 127.738 154.334 104.119 1.00 30.83 ?  442 THR A CB    1 
ATOM   3558  O  OG1   . THR A 1 442 ? 127.899 152.968 103.717 1.00 30.72 ?  442 THR A OG1   1 
ATOM   3559  C  CG2   . THR A 1 442 ? 127.718 155.227 102.892 1.00 30.57 ?  442 THR A CG2   1 
ATOM   3560  N  N     . THR A 1 443 ? 129.888 153.148 106.632 1.00 31.71 ?  443 THR A N     1 
ATOM   3561  C  CA    . THR A 1 443 ? 129.934 152.344 107.844 1.00 34.28 ?  443 THR A CA    1 
ATOM   3562  C  C     . THR A 1 443 ? 130.474 153.184 108.994 1.00 37.40 ?  443 THR A C     1 
ATOM   3563  O  O     . THR A 1 443 ? 131.518 153.829 108.862 1.00 39.22 ?  443 THR A O     1 
ATOM   3564  C  CB    . THR A 1 443 ? 130.803 151.104 107.640 1.00 33.99 ?  443 THR A CB    1 
ATOM   3565  O  OG1   . THR A 1 443 ? 130.205 150.257 106.651 1.00 38.06 ?  443 THR A OG1   1 
ATOM   3566  C  CG2   . THR A 1 443 ? 130.942 150.332 108.939 1.00 30.56 ?  443 THR A CG2   1 
ATOM   3567  N  N     . ASP A 1 444 ? 129.757 153.178 110.117 1.00 42.90 ?  444 ASP A N     1 
ATOM   3568  C  CA    . ASP A 1 444 ? 130.165 153.922 111.308 1.00 42.22 ?  444 ASP A CA    1 
ATOM   3569  C  C     . ASP A 1 444 ? 129.794 153.093 112.533 1.00 41.14 ?  444 ASP A C     1 
ATOM   3570  O  O     . ASP A 1 444 ? 128.639 153.101 112.968 1.00 42.24 ?  444 ASP A O     1 
ATOM   3571  C  CB    . ASP A 1 444 ? 129.516 155.300 111.350 1.00 43.39 ?  444 ASP A CB    1 
ATOM   3572  C  CG    . ASP A 1 444 ? 130.421 156.351 111.958 1.00 46.17 ?  444 ASP A CG    1 
ATOM   3573  O  OD1   . ASP A 1 444 ? 130.792 156.202 113.141 1.00 45.39 ?  444 ASP A OD1   1 
ATOM   3574  O  OD2   . ASP A 1 444 ? 130.763 157.323 111.255 1.00 47.95 -1 444 ASP A OD2   1 
ATOM   3575  N  N     . ILE A 1 445 ? 130.773 152.384 113.083 1.00 38.07 ?  445 ILE A N     1 
ATOM   3576  C  CA    . ILE A 1 445 ? 130.574 151.561 114.270 1.00 40.95 ?  445 ILE A CA    1 
ATOM   3577  C  C     . ILE A 1 445 ? 130.832 152.442 115.487 1.00 44.55 ?  445 ILE A C     1 
ATOM   3578  O  O     . ILE A 1 445 ? 131.973 152.826 115.756 1.00 44.52 ?  445 ILE A O     1 
ATOM   3579  C  CB    . ILE A 1 445 ? 131.492 150.333 114.265 1.00 39.74 ?  445 ILE A CB    1 
ATOM   3580  C  CG1   . ILE A 1 445 ? 131.409 149.615 112.916 1.00 37.73 ?  445 ILE A CG1   1 
ATOM   3581  C  CG2   . ILE A 1 445 ? 131.132 149.397 115.407 1.00 39.98 ?  445 ILE A CG2   1 
ATOM   3582  C  CD1   . ILE A 1 445 ? 130.337 148.551 112.839 1.00 37.05 ?  445 ILE A CD1   1 
ATOM   3583  N  N     . ARG A 1 446 ? 129.772 152.758 116.230 1.00 47.24 ?  446 ARG A N     1 
ATOM   3584  C  CA    . ARG A 1 446 ? 129.851 153.702 117.337 1.00 50.94 ?  446 ARG A CA    1 
ATOM   3585  C  C     . ARG A 1 446 ? 130.023 153.013 118.687 1.00 49.67 ?  446 ARG A C     1 
ATOM   3586  O  O     . ARG A 1 446 ? 129.849 153.654 119.729 1.00 45.92 ?  446 ARG A O     1 
ATOM   3587  C  CB    . ARG A 1 446 ? 128.614 154.602 117.347 1.00 47.16 ?  446 ARG A CB    1 
ATOM   3588  C  CG    . ARG A 1 446 ? 127.296 153.857 117.237 1.00 46.72 ?  446 ARG A CG    1 
ATOM   3589  C  CD    . ARG A 1 446 ? 126.160 154.786 116.823 1.00 50.06 ?  446 ARG A CD    1 
ATOM   3590  N  NE    . ARG A 1 446 ? 126.406 155.415 115.529 1.00 52.22 ?  446 ARG A NE    1 
ATOM   3591  C  CZ    . ARG A 1 446 ? 126.847 156.654 115.364 1.00 52.70 ?  446 ARG A CZ    1 
ATOM   3592  N  NH1   . ARG A 1 446 ? 127.089 157.446 116.395 1.00 49.54 1  446 ARG A NH1   1 
ATOM   3593  N  NH2   . ARG A 1 446 ? 127.051 157.112 114.132 1.00 51.25 ?  446 ARG A NH2   1 
ATOM   3594  N  N     . ASN A 1 447 ? 130.360 151.723 118.689 1.00 39.92 ?  447 ASN A N     1 
ATOM   3595  C  CA    . ASN A 1 447 ? 130.674 151.014 119.919 1.00 34.85 ?  447 ASN A CA    1 
ATOM   3596  C  C     . ASN A 1 447 ? 131.983 150.243 119.840 1.00 35.19 ?  447 ASN A C     1 
ATOM   3597  O  O     . ASN A 1 447 ? 132.353 149.581 120.815 1.00 36.74 ?  447 ASN A O     1 
ATOM   3598  C  CB    . ASN A 1 447 ? 129.535 150.055 120.295 1.00 34.46 ?  447 ASN A CB    1 
ATOM   3599  C  CG    . ASN A 1 447 ? 128.783 150.507 121.527 1.00 33.05 ?  447 ASN A CG    1 
ATOM   3600  O  OD1   . ASN A 1 447 ? 129.381 150.782 122.567 1.00 37.76 ?  447 ASN A OD1   1 
ATOM   3601  N  ND2   . ASN A 1 447 ? 127.465 150.597 121.416 1.00 34.04 ?  447 ASN A ND2   1 
ATOM   3602  N  N     . ALA A 1 448 ? 132.688 150.306 118.711 1.00 38.72 ?  448 ALA A N     1 
ATOM   3603  C  CA    . ALA A 1 448 ? 134.019 149.725 118.548 1.00 33.62 ?  448 ALA A CA    1 
ATOM   3604  C  C     . ALA A 1 448 ? 134.935 150.848 118.086 1.00 33.26 ?  448 ALA A C     1 
ATOM   3605  O  O     . ALA A 1 448 ? 135.062 151.100 116.878 1.00 33.62 ?  448 ALA A O     1 
ATOM   3606  C  CB    . ALA A 1 448 ? 134.004 148.566 117.555 1.00 29.25 ?  448 ALA A CB    1 
ATOM   3607  N  N     . PRO A 1 449 ? 135.573 151.566 119.015 1.00 30.75 ?  449 PRO A N     1 
ATOM   3608  C  CA    . PRO A 1 449 ? 136.343 152.758 118.617 1.00 27.60 ?  449 PRO A CA    1 
ATOM   3609  C  C     . PRO A 1 449 ? 137.481 152.462 117.659 1.00 29.34 ?  449 PRO A C     1 
ATOM   3610  O  O     . PRO A 1 449 ? 137.720 153.240 116.727 1.00 29.06 ?  449 PRO A O     1 
ATOM   3611  C  CB    . PRO A 1 449 ? 136.863 153.302 119.956 1.00 27.90 ?  449 PRO A CB    1 
ATOM   3612  C  CG    . PRO A 1 449 ? 136.091 152.586 121.011 1.00 31.86 ?  449 PRO A CG    1 
ATOM   3613  C  CD    . PRO A 1 449 ? 135.700 151.275 120.450 1.00 30.43 ?  449 PRO A CD    1 
ATOM   3614  N  N     . ALA A 1 450 ? 138.188 151.348 117.856 1.00 31.60 ?  450 ALA A N     1 
ATOM   3615  C  CA    . ALA A 1 450 ? 139.317 151.034 116.991 1.00 23.57 ?  450 ALA A CA    1 
ATOM   3616  C  C     . ALA A 1 450 ? 138.854 150.582 115.614 1.00 25.16 ?  450 ALA A C     1 
ATOM   3617  O  O     . ALA A 1 450 ? 139.500 150.903 114.611 1.00 27.25 ?  450 ALA A O     1 
ATOM   3618  C  CB    . ALA A 1 450 ? 140.196 149.969 117.642 1.00 24.69 ?  450 ALA A CB    1 
ATOM   3619  N  N     . VAL A 1 451 ? 137.739 149.854 115.544 1.00 30.39 ?  451 VAL A N     1 
ATOM   3620  C  CA    . VAL A 1 451 ? 137.166 149.484 114.253 1.00 23.44 ?  451 VAL A CA    1 
ATOM   3621  C  C     . VAL A 1 451 ? 136.777 150.734 113.474 1.00 24.66 ?  451 VAL A C     1 
ATOM   3622  O  O     . VAL A 1 451 ? 137.069 150.861 112.280 1.00 30.89 ?  451 VAL A O     1 
ATOM   3623  C  CB    . VAL A 1 451 ? 135.964 148.542 114.450 1.00 25.62 ?  451 VAL A CB    1 
ATOM   3624  C  CG1   . VAL A 1 451 ? 135.119 148.477 113.191 1.00 26.43 ?  451 VAL A CG1   1 
ATOM   3625  C  CG2   . VAL A 1 451 ? 136.438 147.158 114.846 1.00 25.40 ?  451 VAL A CG2   1 
ATOM   3626  N  N     . ARG A 1 452 ? 136.125 151.683 114.148 1.00 24.67 ?  452 ARG A N     1 
ATOM   3627  C  CA    . ARG A 1 452 ? 135.733 152.931 113.501 1.00 25.38 ?  452 ARG A CA    1 
ATOM   3628  C  C     . ARG A 1 452 ? 136.953 153.715 113.029 1.00 26.48 ?  452 ARG A C     1 
ATOM   3629  O  O     . ARG A 1 452 ? 136.989 154.213 111.896 1.00 31.93 ?  452 ARG A O     1 
ATOM   3630  C  CB    . ARG A 1 452 ? 134.896 153.767 114.471 1.00 26.48 ?  452 ARG A CB    1 
ATOM   3631  C  CG    . ARG A 1 452 ? 133.863 154.665 113.820 1.00 29.65 ?  452 ARG A CG    1 
ATOM   3632  C  CD    . ARG A 1 452 ? 134.046 156.103 114.264 1.00 28.18 ?  452 ARG A CD    1 
ATOM   3633  N  NE    . ARG A 1 452 ? 133.645 156.308 115.650 1.00 37.09 ?  452 ARG A NE    1 
ATOM   3634  C  CZ    . ARG A 1 452 ? 132.451 156.743 116.031 1.00 39.49 ?  452 ARG A CZ    1 
ATOM   3635  N  NH1   . ARG A 1 452 ? 131.509 157.033 115.149 1.00 35.94 1  452 ARG A NH1   1 
ATOM   3636  N  NH2   . ARG A 1 452 ? 132.199 156.893 117.328 1.00 36.35 ?  452 ARG A NH2   1 
ATOM   3637  N  N     . ARG A 1 453 ? 137.969 153.828 113.888 1.00 27.41 ?  453 ARG A N     1 
ATOM   3638  C  CA    . ARG A 1 453 ? 139.157 154.596 113.528 1.00 24.98 ?  453 ARG A CA    1 
ATOM   3639  C  C     . ARG A 1 453 ? 139.889 153.963 112.353 1.00 30.87 ?  453 ARG A C     1 
ATOM   3640  O  O     . ARG A 1 453 ? 140.322 154.665 111.433 1.00 35.58 ?  453 ARG A O     1 
ATOM   3641  C  CB    . ARG A 1 453 ? 140.088 154.724 114.733 1.00 26.76 ?  453 ARG A CB    1 
ATOM   3642  C  CG    . ARG A 1 453 ? 141.216 155.718 114.532 1.00 30.43 ?  453 ARG A CG    1 
ATOM   3643  C  CD    . ARG A 1 453 ? 142.351 155.483 115.510 1.00 27.05 ?  453 ARG A CD    1 
ATOM   3644  N  NE    . ARG A 1 453 ? 143.616 155.991 114.996 1.00 29.09 ?  453 ARG A NE    1 
ATOM   3645  C  CZ    . ARG A 1 453 ? 144.802 155.467 115.271 1.00 30.96 ?  453 ARG A CZ    1 
ATOM   3646  N  NH1   . ARG A 1 453 ? 144.926 154.417 116.066 1.00 31.00 1  453 ARG A NH1   1 
ATOM   3647  N  NH2   . ARG A 1 453 ? 145.890 156.007 114.732 1.00 30.21 ?  453 ARG A NH2   1 
ATOM   3648  N  N     . ALA A 1 454 ? 140.030 152.636 112.361 1.00 26.81 ?  454 ALA A N     1 
ATOM   3649  C  CA    . ALA A 1 454 ? 140.720 151.964 111.269 1.00 20.64 ?  454 ALA A CA    1 
ATOM   3650  C  C     . ALA A 1 454 ? 139.904 151.991 109.986 1.00 19.20 ?  454 ALA A C     1 
ATOM   3651  O  O     . ALA A 1 454 ? 140.479 152.027 108.896 1.00 25.25 ?  454 ALA A O     1 
ATOM   3652  C  CB    . ALA A 1 454 ? 141.055 150.529 111.660 1.00 23.13 ?  454 ALA A CB    1 
ATOM   3653  N  N     . ASN A 1 455 ? 138.575 151.973 110.085 1.00 23.57 ?  455 ASN A N     1 
ATOM   3654  C  CA    . ASN A 1 455 ? 137.757 152.117 108.888 1.00 23.02 ?  455 ASN A CA    1 
ATOM   3655  C  C     . ASN A 1 455 ? 137.914 153.503 108.282 1.00 26.24 ?  455 ASN A C     1 
ATOM   3656  O  O     . ASN A 1 455 ? 137.961 153.648 107.055 1.00 32.44 ?  455 ASN A O     1 
ATOM   3657  C  CB    . ASN A 1 455 ? 136.293 151.833 109.215 1.00 21.33 ?  455 ASN A CB    1 
ATOM   3658  C  CG    . ASN A 1 455 ? 135.407 151.870 107.988 1.00 27.83 ?  455 ASN A CG    1 
ATOM   3659  O  OD1   . ASN A 1 455 ? 135.564 151.064 107.073 1.00 34.90 ?  455 ASN A OD1   1 
ATOM   3660  N  ND2   . ASN A 1 455 ? 134.470 152.809 107.962 1.00 26.61 ?  455 ASN A ND2   1 
ATOM   3661  N  N     . LYS A 1 456 ? 137.991 154.536 109.123 1.00 29.69 ?  456 LYS A N     1 
ATOM   3662  C  CA    . LYS A 1 456 ? 138.177 155.885 108.598 1.00 26.25 ?  456 LYS A CA    1 
ATOM   3663  C  C     . LYS A 1 456 ? 139.582 156.085 108.041 1.00 27.17 ?  456 LYS A C     1 
ATOM   3664  O  O     . LYS A 1 456 ? 139.763 156.791 107.043 1.00 31.74 ?  456 LYS A O     1 
ATOM   3665  C  CB    . LYS A 1 456 ? 137.879 156.920 109.682 1.00 26.62 ?  456 LYS A CB    1 
ATOM   3666  C  CG    . LYS A 1 456 ? 136.475 156.837 110.248 1.00 29.67 ?  456 LYS A CG    1 
ATOM   3667  C  CD    . LYS A 1 456 ? 136.134 158.072 111.059 1.00 34.00 ?  456 LYS A CD    1 
ATOM   3668  C  CE    . LYS A 1 456 ? 134.647 158.141 111.356 1.00 32.56 ?  456 LYS A CE    1 
ATOM   3669  N  NZ    . LYS A 1 456 ? 133.826 157.773 110.170 1.00 33.57 1  456 LYS A NZ    1 
ATOM   3670  N  N     . ALA A 1 457 ? 140.590 155.473 108.663 1.00 26.25 ?  457 ALA A N     1 
ATOM   3671  C  CA    . ALA A 1 457 ? 141.976 155.734 108.296 1.00 22.46 ?  457 ALA A CA    1 
ATOM   3672  C  C     . ALA A 1 457 ? 142.470 154.840 107.162 1.00 27.03 ?  457 ALA A C     1 
ATOM   3673  O  O     . ALA A 1 457 ? 142.989 155.336 106.159 1.00 31.58 ?  457 ALA A O     1 
ATOM   3674  C  CB    . ALA A 1 457 ? 142.877 155.569 109.523 1.00 22.61 ?  457 ALA A CB    1 
ATOM   3675  N  N     . MET A 1 458 ? 142.322 153.524 107.310 1.00 29.41 ?  458 MET A N     1 
ATOM   3676  C  CA    . MET A 1 458 ? 142.848 152.584 106.328 1.00 19.45 ?  458 MET A CA    1 
ATOM   3677  C  C     . MET A 1 458 ? 142.004 152.547 105.061 1.00 21.76 ?  458 MET A C     1 
ATOM   3678  O  O     . MET A 1 458 ? 142.547 152.395 103.962 1.00 29.94 ?  458 MET A O     1 
ATOM   3679  C  CB    . MET A 1 458 ? 142.935 151.186 106.941 1.00 22.04 ?  458 MET A CB    1 
ATOM   3680  C  CG    . MET A 1 458 ? 143.607 151.147 108.299 1.00 22.23 ?  458 MET A CG    1 
ATOM   3681  S  SD    . MET A 1 458 ? 145.347 151.596 108.208 1.00 33.05 ?  458 MET A SD    1 
ATOM   3682  C  CE    . MET A 1 458 ? 146.101 149.974 108.127 1.00 25.27 ?  458 MET A CE    1 
ATOM   3683  N  N     . LYS A 1 459 ? 140.683 152.675 105.196 1.00 17.12 ?  459 LYS A N     1 
ATOM   3684  C  CA    . LYS A 1 459 ? 139.759 152.585 104.064 1.00 21.91 ?  459 LYS A CA    1 
ATOM   3685  C  C     . LYS A 1 459 ? 139.941 151.272 103.306 1.00 17.93 ?  459 LYS A C     1 
ATOM   3686  O  O     . LYS A 1 459 ? 139.936 151.238 102.075 1.00 25.40 ?  459 LYS A O     1 
ATOM   3687  C  CB    . LYS A 1 459 ? 139.914 153.782 103.124 1.00 21.80 ?  459 LYS A CB    1 
ATOM   3688  C  CG    . LYS A 1 459 ? 139.894 155.126 103.824 1.00 24.86 ?  459 LYS A CG    1 
ATOM   3689  C  CD    . LYS A 1 459 ? 140.825 156.109 103.144 1.00 25.02 ?  459 LYS A CD    1 
ATOM   3690  C  CE    . LYS A 1 459 ? 140.823 157.449 103.852 1.00 28.55 ?  459 LYS A CE    1 
ATOM   3691  N  NZ    . LYS A 1 459 ? 141.855 158.363 103.292 1.00 31.75 1  459 LYS A NZ    1 
ATOM   3692  N  N     . SER A 1 460 ? 140.101 150.182 104.050 1.00 20.38 ?  460 SER A N     1 
ATOM   3693  C  CA    . SER A 1 460 ? 140.360 148.880 103.454 1.00 14.03 ?  460 SER A CA    1 
ATOM   3694  C  C     . SER A 1 460 ? 139.078 148.264 102.912 1.00 20.49 ?  460 SER A C     1 
ATOM   3695  O  O     . SER A 1 460 ? 138.014 148.362 103.527 1.00 29.78 ?  460 SER A O     1 
ATOM   3696  C  CB    . SER A 1 460 ? 140.990 147.939 104.478 1.00 8.71  ?  460 SER A CB    1 
ATOM   3697  O  OG    . SER A 1 460 ? 142.075 148.558 105.142 1.00 30.12 ?  460 SER A OG    1 
ATOM   3698  N  N     . ILE A 1 461 ? 139.191 147.622 101.751 1.00 13.07 ?  461 ILE A N     1 
ATOM   3699  C  CA    . ILE A 1 461 ? 138.091 146.893 101.141 1.00 14.90 ?  461 ILE A CA    1 
ATOM   3700  C  C     . ILE A 1 461 ? 138.592 145.506 100.772 1.00 15.17 ?  461 ILE A C     1 
ATOM   3701  O  O     . ILE A 1 461 ? 139.794 145.267 100.645 1.00 22.96 ?  461 ILE A O     1 
ATOM   3702  C  CB    . ILE A 1 461 ? 137.525 147.610 99.896  1.00 14.02 ?  461 ILE A CB    1 
ATOM   3703  C  CG1   . ILE A 1 461 ? 138.608 147.755 98.827  1.00 7.16  ?  461 ILE A CG1   1 
ATOM   3704  C  CG2   . ILE A 1 461 ? 136.956 148.968 100.274 1.00 14.31 ?  461 ILE A CG2   1 
ATOM   3705  C  CD1   . ILE A 1 461 ? 138.141 148.445 97.576  1.00 7.09  ?  461 ILE A CD1   1 
ATOM   3706  N  N     . GLY A 1 462 ? 137.652 144.581 100.622 1.00 16.88 ?  462 GLY A N     1 
ATOM   3707  C  CA    . GLY A 1 462 ? 138.002 143.268 100.122 1.00 8.05  ?  462 GLY A CA    1 
ATOM   3708  C  C     . GLY A 1 462 ? 137.219 142.898 98.884  1.00 5.76  ?  462 GLY A C     1 
ATOM   3709  O  O     . GLY A 1 462 ? 136.012 142.661 98.957  1.00 24.60 ?  462 GLY A O     1 
ATOM   3710  N  N     . LEU A 1 463 ? 137.896 142.829 97.743  1.00 13.49 ?  463 LEU A N     1 
ATOM   3711  C  CA    . LEU A 1 463 ? 137.269 142.453 96.483  1.00 11.99 ?  463 LEU A CA    1 
ATOM   3712  C  C     . LEU A 1 463 ? 137.728 141.045 96.128  1.00 15.77 ?  463 LEU A C     1 
ATOM   3713  O  O     . LEU A 1 463 ? 138.872 140.844 95.711  1.00 27.78 ?  463 LEU A O     1 
ATOM   3714  C  CB    . LEU A 1 463 ? 137.615 143.447 95.377  1.00 18.12 ?  463 LEU A CB    1 
ATOM   3715  C  CG    . LEU A 1 463 ? 137.036 143.144 93.992  1.00 17.19 ?  463 LEU A CG    1 
ATOM   3716  C  CD1   . LEU A 1 463 ? 135.538 142.905 94.076  1.00 7.19  ?  463 LEU A CD1   1 
ATOM   3717  C  CD2   . LEU A 1 463 ? 137.349 144.266 93.018  1.00 15.33 ?  463 LEU A CD2   1 
ATOM   3718  N  N     . GLY A 1 464 ? 136.834 140.074 96.299  1.00 17.43 ?  464 GLY A N     1 
ATOM   3719  C  CA    . GLY A 1 464 ? 137.124 138.693 95.995  1.00 11.70 ?  464 GLY A CA    1 
ATOM   3720  C  C     . GLY A 1 464 ? 136.574 138.269 94.646  1.00 11.76 ?  464 GLY A C     1 
ATOM   3721  O  O     . GLY A 1 464 ? 136.093 139.073 93.847  1.00 18.98 ?  464 GLY A O     1 
ATOM   3722  N  N     . ALA A 1 465 ? 136.662 136.967 94.397  1.00 14.71 ?  465 ALA A N     1 
ATOM   3723  C  CA    . ALA A 1 465 ? 136.124 136.376 93.187  1.00 11.19 ?  465 ALA A CA    1 
ATOM   3724  C  C     . ALA A 1 465 ? 135.544 135.012 93.522  1.00 16.81 ?  465 ALA A C     1 
ATOM   3725  O  O     . ALA A 1 465 ? 135.914 134.386 94.518  1.00 29.03 ?  465 ALA A O     1 
ATOM   3726  C  CB    . ALA A 1 465 ? 137.192 136.256 92.094  1.00 15.71 ?  465 ALA A CB    1 
ATOM   3727  N  N     . MET A 1 466 ? 134.615 134.561 92.684  1.00 22.27 ?  466 MET A N     1 
ATOM   3728  C  CA    . MET A 1 466 ? 134.058 133.222 92.786  1.00 21.62 ?  466 MET A CA    1 
ATOM   3729  C  C     . MET A 1 466 ? 133.879 132.667 91.381  1.00 19.91 ?  466 MET A C     1 
ATOM   3730  O  O     . MET A 1 466 ? 134.194 133.328 90.386  1.00 23.91 ?  466 MET A O     1 
ATOM   3731  C  CB    . MET A 1 466 ? 132.725 133.207 93.541  1.00 26.40 ?  466 MET A CB    1 
ATOM   3732  C  CG    . MET A 1 466 ? 131.725 134.243 93.080  1.00 27.60 ?  466 MET A CG    1 
ATOM   3733  S  SD    . MET A 1 466 ? 130.192 134.118 94.014  1.00 40.18 ?  466 MET A SD    1 
ATOM   3734  C  CE    . MET A 1 466 ? 129.665 135.819 94.013  1.00 26.82 ?  466 MET A CE    1 
ATOM   3735  N  N     . ASN A 1 467 ? 133.367 131.438 91.311  1.00 20.36 ?  467 ASN A N     1 
ATOM   3736  C  CA    . ASN A 1 467 ? 133.100 130.750 90.049  1.00 20.74 ?  467 ASN A CA    1 
ATOM   3737  C  C     . ASN A 1 467 ? 134.377 130.496 89.254  1.00 21.97 ?  467 ASN A C     1 
ATOM   3738  O  O     . ASN A 1 467 ? 134.345 130.409 88.026  1.00 27.77 ?  467 ASN A O     1 
ATOM   3739  C  CB    . ASN A 1 467 ? 132.087 131.516 89.193  1.00 21.02 ?  467 ASN A CB    1 
ATOM   3740  C  CG    . ASN A 1 467 ? 131.041 130.613 88.583  1.00 26.60 ?  467 ASN A CG    1 
ATOM   3741  O  OD1   . ASN A 1 467 ? 130.981 129.424 88.885  1.00 30.58 ?  467 ASN A OD1   1 
ATOM   3742  N  ND2   . ASN A 1 467 ? 130.201 131.177 87.729  1.00 28.87 ?  467 ASN A ND2   1 
ATOM   3743  N  N     . LEU A 1 468 ? 135.515 130.382 89.941  1.00 17.20 ?  468 LEU A N     1 
ATOM   3744  C  CA    . LEU A 1 468 ? 136.746 130.014 89.252  1.00 18.24 ?  468 LEU A CA    1 
ATOM   3745  C  C     . LEU A 1 468 ? 136.665 128.588 88.726  1.00 22.11 ?  468 LEU A C     1 
ATOM   3746  O  O     . LEU A 1 468 ? 136.923 128.334 87.542  1.00 24.19 ?  468 LEU A O     1 
ATOM   3747  C  CB    . LEU A 1 468 ? 137.944 130.173 90.188  1.00 22.48 ?  468 LEU A CB    1 
ATOM   3748  C  CG    . LEU A 1 468 ? 139.255 129.577 89.670  1.00 20.24 ?  468 LEU A CG    1 
ATOM   3749  C  CD1   . LEU A 1 468 ? 139.831 130.424 88.551  1.00 17.75 ?  468 LEU A CD1   1 
ATOM   3750  C  CD2   . LEU A 1 468 ? 140.263 129.406 90.788  1.00 14.67 ?  468 LEU A CD2   1 
ATOM   3751  N  N     . HIS A 1 469 ? 136.290 127.643 89.591  1.00 25.00 ?  469 HIS A N     1 
ATOM   3752  C  CA    . HIS A 1 469 ? 136.146 126.263 89.149  1.00 15.91 ?  469 HIS A CA    1 
ATOM   3753  C  C     . HIS A 1 469 ? 134.990 126.118 88.173  1.00 25.43 ?  469 HIS A C     1 
ATOM   3754  O  O     . HIS A 1 469 ? 135.075 125.339 87.220  1.00 35.75 ?  469 HIS A O     1 
ATOM   3755  C  CB    . HIS A 1 469 ? 135.955 125.332 90.344  1.00 20.66 ?  469 HIS A CB    1 
ATOM   3756  C  CG    . HIS A 1 469 ? 136.081 123.880 90.000  1.00 24.47 ?  469 HIS A CG    1 
ATOM   3757  N  ND1   . HIS A 1 469 ? 135.797 122.875 90.897  1.00 30.41 ?  469 HIS A ND1   1 
ATOM   3758  C  CD2   . HIS A 1 469 ? 136.469 123.266 88.858  1.00 25.57 ?  469 HIS A CD2   1 
ATOM   3759  C  CE1   . HIS A 1 469 ? 135.997 121.704 90.321  1.00 26.91 ?  469 HIS A CE1   1 
ATOM   3760  N  NE2   . HIS A 1 469 ? 136.406 121.913 89.083  1.00 23.55 ?  469 HIS A NE2   1 
ATOM   3761  N  N     . GLY A 1 470 ? 133.899 126.852 88.392  1.00 23.18 ?  470 GLY A N     1 
ATOM   3762  C  CA    . GLY A 1 470 ? 132.798 126.808 87.444  1.00 18.91 ?  470 GLY A CA    1 
ATOM   3763  C  C     . GLY A 1 470 ? 133.204 127.296 86.068  1.00 13.76 ?  470 GLY A C     1 
ATOM   3764  O  O     . GLY A 1 470 ? 132.881 126.675 85.053  1.00 30.84 ?  470 GLY A O     1 
ATOM   3765  N  N     . TYR A 1 471 ? 133.937 128.411 86.021  1.00 17.80 ?  471 TYR A N     1 
ATOM   3766  C  CA    . TYR A 1 471 ? 134.405 128.938 84.745  1.00 20.66 ?  471 TYR A CA    1 
ATOM   3767  C  C     . TYR A 1 471 ? 135.368 127.974 84.066  1.00 26.74 ?  471 TYR A C     1 
ATOM   3768  O  O     . TYR A 1 471 ? 135.292 127.765 82.851  1.00 30.29 ?  471 TYR A O     1 
ATOM   3769  C  CB    . TYR A 1 471 ? 135.071 130.299 84.950  1.00 21.83 ?  471 TYR A CB    1 
ATOM   3770  C  CG    . TYR A 1 471 ? 135.689 130.866 83.696  1.00 25.96 ?  471 TYR A CG    1 
ATOM   3771  C  CD1   . TYR A 1 471 ? 134.899 131.438 82.710  1.00 25.94 ?  471 TYR A CD1   1 
ATOM   3772  C  CD2   . TYR A 1 471 ? 137.060 130.817 83.490  1.00 20.53 ?  471 TYR A CD2   1 
ATOM   3773  C  CE1   . TYR A 1 471 ? 135.457 131.954 81.560  1.00 26.67 ?  471 TYR A CE1   1 
ATOM   3774  C  CE2   . TYR A 1 471 ? 137.626 131.327 82.341  1.00 20.47 ?  471 TYR A CE2   1 
ATOM   3775  C  CZ    . TYR A 1 471 ? 136.820 131.895 81.381  1.00 28.50 ?  471 TYR A CZ    1 
ATOM   3776  O  OH    . TYR A 1 471 ? 137.382 132.407 80.236  1.00 31.36 ?  471 TYR A OH    1 
ATOM   3777  N  N     . LEU A 1 472 ? 136.288 127.382 84.833  1.00 22.56 ?  472 LEU A N     1 
ATOM   3778  C  CA    . LEU A 1 472 ? 137.257 126.466 84.237  1.00 21.54 ?  472 LEU A CA    1 
ATOM   3779  C  C     . LEU A 1 472 ? 136.590 125.189 83.739  1.00 26.87 ?  472 LEU A C     1 
ATOM   3780  O  O     . LEU A 1 472 ? 136.905 124.705 82.646  1.00 31.87 ?  472 LEU A O     1 
ATOM   3781  C  CB    . LEU A 1 472 ? 138.357 126.139 85.246  1.00 27.45 ?  472 LEU A CB    1 
ATOM   3782  C  CG    . LEU A 1 472 ? 139.253 127.302 85.676  1.00 29.85 ?  472 LEU A CG    1 
ATOM   3783  C  CD1   . LEU A 1 472 ? 140.019 126.938 86.933  1.00 22.43 ?  472 LEU A CD1   1 
ATOM   3784  C  CD2   . LEU A 1 472 ? 140.201 127.705 84.560  1.00 22.59 ?  472 LEU A CD2   1 
ATOM   3785  N  N     . ALA A 1 473 ? 135.669 124.628 84.525  1.00 28.89 ?  473 ALA A N     1 
ATOM   3786  C  CA    . ALA A 1 473 ? 134.995 123.398 84.130  1.00 25.05 ?  473 ALA A CA    1 
ATOM   3787  C  C     . ALA A 1 473 ? 134.070 123.629 82.943  1.00 32.50 ?  473 ALA A C     1 
ATOM   3788  O  O     . ALA A 1 473 ? 133.925 122.751 82.085  1.00 40.07 ?  473 ALA A O     1 
ATOM   3789  C  CB    . ALA A 1 473 ? 134.219 122.828 85.315  1.00 26.38 ?  473 ALA A CB    1 
ATOM   3790  N  N     . GLN A 1 474 ? 133.436 124.799 82.875  1.00 28.34 ?  474 GLN A N     1 
ATOM   3791  C  CA    . GLN A 1 474 ? 132.594 125.120 81.733  1.00 25.63 ?  474 GLN A CA    1 
ATOM   3792  C  C     . GLN A 1 474 ? 133.397 125.545 80.513  1.00 24.52 ?  474 GLN A C     1 
ATOM   3793  O  O     . GLN A 1 474 ? 132.809 125.759 79.448  1.00 35.27 ?  474 GLN A O     1 
ATOM   3794  C  CB    . GLN A 1 474 ? 131.594 126.215 82.108  1.00 27.87 ?  474 GLN A CB    1 
ATOM   3795  C  CG    . GLN A 1 474 ? 130.434 125.706 82.944  1.00 31.27 ?  474 GLN A CG    1 
ATOM   3796  C  CD    . GLN A 1 474 ? 129.625 126.823 83.561  1.00 30.88 ?  474 GLN A CD    1 
ATOM   3797  O  OE1   . GLN A 1 474 ? 128.944 127.571 82.862  1.00 33.25 ?  474 GLN A OE1   1 
ATOM   3798  N  NE2   . GLN A 1 474 ? 129.692 126.942 84.881  1.00 31.70 ?  474 GLN A NE2   1 
ATOM   3799  N  N     . ASN A 1 475 ? 134.716 125.679 80.641  1.00 30.94 ?  475 ASN A N     1 
ATOM   3800  C  CA    . ASN A 1 475 ? 135.593 125.981 79.519  1.00 32.64 ?  475 ASN A CA    1 
ATOM   3801  C  C     . ASN A 1 475 ? 136.538 124.832 79.197  1.00 33.12 ?  475 ASN A C     1 
ATOM   3802  O  O     . ASN A 1 475 ? 137.509 125.028 78.459  1.00 36.54 ?  475 ASN A O     1 
ATOM   3803  C  CB    . ASN A 1 475 ? 136.392 127.255 79.800  1.00 34.58 ?  475 ASN A CB    1 
ATOM   3804  C  CG    . ASN A 1 475 ? 135.555 128.508 79.660  1.00 30.33 ?  475 ASN A CG    1 
ATOM   3805  O  OD1   . ASN A 1 475 ? 135.514 129.125 78.597  1.00 35.59 ?  475 ASN A OD1   1 
ATOM   3806  N  ND2   . ASN A 1 475 ? 134.874 128.886 80.733  1.00 25.96 ?  475 ASN A ND2   1 
ATOM   3807  N  N     . GLY A 1 476 ? 136.279 123.643 79.731  1.00 29.91 ?  476 GLY A N     1 
ATOM   3808  C  CA    . GLY A 1 476 ? 137.116 122.486 79.463  1.00 30.17 ?  476 GLY A CA    1 
ATOM   3809  C  C     . GLY A 1 476 ? 138.521 122.579 80.014  1.00 34.66 ?  476 GLY A C     1 
ATOM   3810  O  O     . GLY A 1 476 ? 139.475 122.172 79.338  1.00 36.43 ?  476 GLY A O     1 
ATOM   3811  N  N     . ILE A 1 477 ? 138.678 123.107 81.225  1.00 31.37 ?  477 ILE A N     1 
ATOM   3812  C  CA    . ILE A 1 477 ? 139.978 123.228 81.873  1.00 28.71 ?  477 ILE A CA    1 
ATOM   3813  C  C     . ILE A 1 477 ? 139.902 122.552 83.233  1.00 31.58 ?  477 ILE A C     1 
ATOM   3814  O  O     . ILE A 1 477 ? 139.013 122.859 84.035  1.00 35.25 ?  477 ILE A O     1 
ATOM   3815  C  CB    . ILE A 1 477 ? 140.408 124.699 82.025  1.00 28.00 ?  477 ILE A CB    1 
ATOM   3816  C  CG1   . ILE A 1 477 ? 140.418 125.400 80.666  1.00 30.91 ?  477 ILE A CG1   1 
ATOM   3817  C  CG2   . ILE A 1 477 ? 141.775 124.785 82.673  1.00 31.37 ?  477 ILE A CG2   1 
ATOM   3818  C  CD1   . ILE A 1 477 ? 140.360 126.905 80.757  1.00 32.68 ?  477 ILE A CD1   1 
ATOM   3819  N  N     . ALA A 1 478 ? 140.827 121.632 83.489  1.00 31.56 ?  478 ALA A N     1 
ATOM   3820  C  CA    . ALA A 1 478 ? 140.894 120.983 84.790  1.00 26.59 ?  478 ALA A CA    1 
ATOM   3821  C  C     . ALA A 1 478 ? 141.438 121.950 85.832  1.00 33.48 ?  478 ALA A C     1 
ATOM   3822  O  O     . ALA A 1 478 ? 142.320 122.761 85.546  1.00 35.57 ?  478 ALA A O     1 
ATOM   3823  C  CB    . ALA A 1 478 ? 141.771 119.735 84.719  1.00 28.38 ?  478 ALA A CB    1 
ATOM   3824  N  N     . TYR A 1 479 ? 140.906 121.856 87.053  1.00 31.35 ?  479 TYR A N     1 
ATOM   3825  C  CA    . TYR A 1 479 ? 141.331 122.757 88.119  1.00 22.61 ?  479 TYR A CA    1 
ATOM   3826  C  C     . TYR A 1 479 ? 142.811 122.580 88.435  1.00 30.04 ?  479 TYR A C     1 
ATOM   3827  O  O     . TYR A 1 479 ? 143.520 123.561 88.688  1.00 39.24 ?  479 TYR A O     1 
ATOM   3828  C  CB    . TYR A 1 479 ? 140.482 122.522 89.368  1.00 21.64 ?  479 TYR A CB    1 
ATOM   3829  C  CG    . TYR A 1 479 ? 140.663 123.559 90.452  1.00 27.42 ?  479 TYR A CG    1 
ATOM   3830  C  CD1   . TYR A 1 479 ? 139.881 124.705 90.477  1.00 23.50 ?  479 TYR A CD1   1 
ATOM   3831  C  CD2   . TYR A 1 479 ? 141.609 123.390 91.455  1.00 28.82 ?  479 TYR A CD2   1 
ATOM   3832  C  CE1   . TYR A 1 479 ? 140.037 125.653 91.463  1.00 24.74 ?  479 TYR A CE1   1 
ATOM   3833  C  CE2   . TYR A 1 479 ? 141.772 124.336 92.446  1.00 26.82 ?  479 TYR A CE2   1 
ATOM   3834  C  CZ    . TYR A 1 479 ? 140.984 125.465 92.445  1.00 30.44 ?  479 TYR A CZ    1 
ATOM   3835  O  OH    . TYR A 1 479 ? 141.141 126.410 93.430  1.00 31.19 ?  479 TYR A OH    1 
ATOM   3836  N  N     . GLU A 1 480 ? 143.294 121.339 88.428  1.00 34.75 ?  480 GLU A N     1 
ATOM   3837  C  CA    . GLU A 1 480 ? 144.694 121.060 88.716  1.00 30.47 ?  480 GLU A CA    1 
ATOM   3838  C  C     . GLU A 1 480 ? 145.611 121.312 87.530  1.00 32.31 ?  480 GLU A C     1 
ATOM   3839  O  O     . GLU A 1 480 ? 146.834 121.275 87.700  1.00 38.83 ?  480 GLU A O     1 
ATOM   3840  C  CB    . GLU A 1 480 ? 144.861 119.609 89.160  1.00 35.32 ?  480 GLU A CB    1 
ATOM   3841  C  CG    . GLU A 1 480 ? 144.050 119.214 90.369  1.00 33.17 ?  480 GLU A CG    1 
ATOM   3842  C  CD    . GLU A 1 480 ? 143.734 117.736 90.372  1.00 41.41 ?  480 GLU A CD    1 
ATOM   3843  O  OE1   . GLU A 1 480 ? 142.714 117.344 89.767  1.00 41.14 ?  480 GLU A OE1   1 
ATOM   3844  O  OE2   . GLU A 1 480 ? 144.506 116.962 90.973  1.00 42.62 -1 480 GLU A OE2   1 
ATOM   3845  N  N     . SER A 1 481 ? 145.063 121.558 86.346  1.00 33.54 ?  481 SER A N     1 
ATOM   3846  C  CA    . SER A 1 481 ? 145.885 121.689 85.157  1.00 32.41 ?  481 SER A CA    1 
ATOM   3847  C  C     . SER A 1 481 ? 146.720 122.969 85.211  1.00 34.48 ?  481 SER A C     1 
ATOM   3848  O  O     . SER A 1 481 ? 146.322 123.955 85.834  1.00 37.49 ?  481 SER A O     1 
ATOM   3849  C  CB    . SER A 1 481 ? 145.013 121.690 83.906  1.00 32.23 ?  481 SER A CB    1 
ATOM   3850  O  OG    . SER A 1 481 ? 144.472 122.975 83.664  1.00 36.70 ?  481 SER A OG    1 
ATOM   3851  N  N     . PRO A 1 482 ? 147.895 122.967 84.577  1.00 39.26 ?  482 PRO A N     1 
ATOM   3852  C  CA    . PRO A 1 482 ? 148.678 124.209 84.492  1.00 35.92 ?  482 PRO A CA    1 
ATOM   3853  C  C     . PRO A 1 482 ? 147.960 125.325 83.757  1.00 35.70 ?  482 PRO A C     1 
ATOM   3854  O  O     . PRO A 1 482 ? 148.221 126.502 84.032  1.00 39.30 ?  482 PRO A O     1 
ATOM   3855  C  CB    . PRO A 1 482 ? 149.950 123.770 83.751  1.00 35.33 ?  482 PRO A CB    1 
ATOM   3856  C  CG    . PRO A 1 482 ? 150.028 122.299 83.961  1.00 36.84 ?  482 PRO A CG    1 
ATOM   3857  C  CD    . PRO A 1 482 ? 148.613 121.819 84.001  1.00 40.09 ?  482 PRO A CD    1 
ATOM   3858  N  N     . GLU A 1 483 ? 147.069 124.991 82.821  1.00 37.21 ?  483 GLU A N     1 
ATOM   3859  C  CA    . GLU A 1 483 ? 146.309 126.019 82.117  1.00 36.11 ?  483 GLU A CA    1 
ATOM   3860  C  C     . GLU A 1 483 ? 145.380 126.766 83.065  1.00 33.32 ?  483 GLU A C     1 
ATOM   3861  O  O     . GLU A 1 483 ? 145.174 127.976 82.919  1.00 36.83 ?  483 GLU A O     1 
ATOM   3862  C  CB    . GLU A 1 483 ? 145.517 125.392 80.970  1.00 38.31 ?  483 GLU A CB    1 
ATOM   3863  C  CG    . GLU A 1 483 ? 146.380 124.891 79.827  1.00 40.47 ?  483 GLU A CG    1 
ATOM   3864  C  CD    . GLU A 1 483 ? 146.798 123.446 80.007  1.00 43.75 ?  483 GLU A CD    1 
ATOM   3865  O  OE1   . GLU A 1 483 ? 146.514 122.874 81.079  1.00 41.03 ?  483 GLU A OE1   1 
ATOM   3866  O  OE2   . GLU A 1 483 ? 147.417 122.882 79.081  1.00 43.14 -1 483 GLU A OE2   1 
ATOM   3867  N  N     . ALA A 1 484 ? 144.805 126.059 84.039  1.00 27.96 ?  484 ALA A N     1 
ATOM   3868  C  CA    . ALA A 1 484 ? 143.962 126.716 85.031  1.00 28.48 ?  484 ALA A CA    1 
ATOM   3869  C  C     . ALA A 1 484 ? 144.759 127.717 85.854  1.00 29.73 ?  484 ALA A C     1 
ATOM   3870  O  O     . ALA A 1 484 ? 144.295 128.835 86.109  1.00 31.79 ?  484 ALA A O     1 
ATOM   3871  C  CB    . ALA A 1 484 ? 143.312 125.677 85.940  1.00 27.81 ?  484 ALA A CB    1 
ATOM   3872  N  N     . ARG A 1 485 ? 145.963 127.333 86.281  1.00 30.89 ?  485 ARG A N     1 
ATOM   3873  C  CA    . ARG A 1 485 ? 146.808 128.255 87.030  1.00 24.15 ?  485 ARG A CA    1 
ATOM   3874  C  C     . ARG A 1 485 ? 147.269 129.417 86.163  1.00 25.15 ?  485 ARG A C     1 
ATOM   3875  O  O     . ARG A 1 485 ? 147.408 130.536 86.660  1.00 35.58 ?  485 ARG A O     1 
ATOM   3876  C  CB    . ARG A 1 485 ? 148.007 127.512 87.615  1.00 27.04 ?  485 ARG A CB    1 
ATOM   3877  C  CG    . ARG A 1 485 ? 147.648 126.607 88.777  1.00 26.39 ?  485 ARG A CG    1 
ATOM   3878  C  CD    . ARG A 1 485 ? 148.889 126.066 89.458  1.00 28.57 ?  485 ARG A CD    1 
ATOM   3879  N  NE    . ARG A 1 485 ? 149.702 125.264 88.554  1.00 31.77 ?  485 ARG A NE    1 
ATOM   3880  C  CZ    . ARG A 1 485 ? 149.485 123.985 88.286  1.00 32.64 ?  485 ARG A CZ    1 
ATOM   3881  N  NH1   . ARG A 1 485 ? 148.479 123.324 88.837  1.00 30.58 1  485 ARG A NH1   1 
ATOM   3882  N  NH2   . ARG A 1 485 ? 150.298 123.351 87.448  1.00 29.50 ?  485 ARG A NH2   1 
ATOM   3883  N  N     . ASP A 1 486 ? 147.504 129.175 84.874  1.00 30.78 ?  486 ASP A N     1 
ATOM   3884  C  CA    . ASP A 1 486 ? 147.842 130.260 83.956  1.00 29.20 ?  486 ASP A CA    1 
ATOM   3885  C  C     . ASP A 1 486 ? 146.697 131.261 83.846  1.00 29.58 ?  486 ASP A C     1 
ATOM   3886  O  O     . ASP A 1 486 ? 146.909 132.483 83.897  1.00 36.63 ?  486 ASP A O     1 
ATOM   3887  C  CB    . ASP A 1 486 ? 148.189 129.674 82.588  1.00 33.34 ?  486 ASP A CB    1 
ATOM   3888  C  CG    . ASP A 1 486 ? 148.709 130.711 81.625  1.00 40.71 ?  486 ASP A CG    1 
ATOM   3889  O  OD1   . ASP A 1 486 ? 149.671 131.425 81.974  1.00 42.51 ?  486 ASP A OD1   1 
ATOM   3890  O  OD2   . ASP A 1 486 ? 148.158 130.804 80.510  1.00 39.27 -1 486 ASP A OD2   1 
ATOM   3891  N  N     . PHE A 1 487 ? 145.469 130.756 83.706  1.00 30.32 ?  487 PHE A N     1 
ATOM   3892  C  CA    . PHE A 1 487 ? 144.317 131.646 83.659  1.00 25.86 ?  487 PHE A CA    1 
ATOM   3893  C  C     . PHE A 1 487 ? 144.166 132.416 84.959  1.00 25.25 ?  487 PHE A C     1 
ATOM   3894  O  O     . PHE A 1 487 ? 143.876 133.614 84.942  1.00 31.24 ?  487 PHE A O     1 
ATOM   3895  C  CB    . PHE A 1 487 ? 143.029 130.879 83.374  1.00 26.95 ?  487 PHE A CB    1 
ATOM   3896  C  CG    . PHE A 1 487 ? 141.796 131.651 83.744  1.00 29.75 ?  487 PHE A CG    1 
ATOM   3897  C  CD1   . PHE A 1 487 ? 141.355 132.691 82.945  1.00 26.34 ?  487 PHE A CD1   1 
ATOM   3898  C  CD2   . PHE A 1 487 ? 141.101 131.369 84.909  1.00 26.22 ?  487 PHE A CD2   1 
ATOM   3899  C  CE1   . PHE A 1 487 ? 140.239 133.421 83.287  1.00 26.84 ?  487 PHE A CE1   1 
ATOM   3900  C  CE2   . PHE A 1 487 ? 139.984 132.098 85.255  1.00 25.28 ?  487 PHE A CE2   1 
ATOM   3901  C  CZ    . PHE A 1 487 ? 139.554 133.125 84.442  1.00 28.34 ?  487 PHE A CZ    1 
ATOM   3902  N  N     . ALA A 1 488 ? 144.320 131.737 86.096  1.00 25.81 ?  488 ALA A N     1 
ATOM   3903  C  CA    . ALA A 1 488 ? 144.195 132.418 87.379  1.00 20.51 ?  488 ALA A CA    1 
ATOM   3904  C  C     . ALA A 1 488 ? 145.253 133.502 87.522  1.00 27.80 ?  488 ALA A C     1 
ATOM   3905  O  O     . ALA A 1 488 ? 144.960 134.610 87.983  1.00 34.78 ?  488 ALA A O     1 
ATOM   3906  C  CB    . ALA A 1 488 ? 144.294 131.409 88.520  1.00 18.44 ?  488 ALA A CB    1 
ATOM   3907  N  N     . ASN A 1 489 ? 146.486 133.205 87.106  1.00 28.19 ?  489 ASN A N     1 
ATOM   3908  C  CA    . ASN A 1 489 ? 147.553 134.195 87.143  1.00 20.94 ?  489 ASN A CA    1 
ATOM   3909  C  C     . ASN A 1 489 ? 147.176 135.434 86.345  1.00 20.93 ?  489 ASN A C     1 
ATOM   3910  O  O     . ASN A 1 489 ? 147.208 136.553 86.866  1.00 30.25 ?  489 ASN A O     1 
ATOM   3911  C  CB    . ASN A 1 489 ? 148.842 133.575 86.603  1.00 22.28 ?  489 ASN A CB    1 
ATOM   3912  C  CG    . ASN A 1 489 ? 150.081 134.314 87.051  1.00 30.45 ?  489 ASN A CG    1 
ATOM   3913  O  OD1   . ASN A 1 489 ? 150.219 134.667 88.220  1.00 36.75 ?  489 ASN A OD1   1 
ATOM   3914  N  ND2   . ASN A 1 489 ? 151.000 134.542 86.122  1.00 28.71 ?  489 ASN A ND2   1 
ATOM   3915  N  N     . THR A 1 490 ? 146.786 135.247 85.081  1.00 26.43 ?  490 THR A N     1 
ATOM   3916  C  CA    . THR A 1 490 ? 146.459 136.401 84.245  1.00 24.41 ?  490 THR A CA    1 
ATOM   3917  C  C     . THR A 1 490 ? 145.244 137.152 84.778  1.00 26.18 ?  490 THR A C     1 
ATOM   3918  O  O     . THR A 1 490 ? 145.256 138.387 84.869  1.00 27.97 ?  490 THR A O     1 
ATOM   3919  C  CB    . THR A 1 490 ? 146.221 135.957 82.804  1.00 26.36 ?  490 THR A CB    1 
ATOM   3920  O  OG1   . THR A 1 490 ? 147.344 135.195 82.350  1.00 31.50 ?  490 THR A OG1   1 
ATOM   3921  C  CG2   . THR A 1 490 ? 146.038 137.166 81.900  1.00 25.93 ?  490 THR A CG2   1 
ATOM   3922  N  N     . PHE A 1 491 ? 144.193 136.421 85.153  1.00 21.58 ?  491 PHE A N     1 
ATOM   3923  C  CA    . PHE A 1 491 ? 142.953 137.044 85.595  1.00 18.72 ?  491 PHE A CA    1 
ATOM   3924  C  C     . PHE A 1 491 ? 143.168 137.865 86.857  1.00 25.92 ?  491 PHE A C     1 
ATOM   3925  O  O     . PHE A 1 491 ? 142.729 139.016 86.945  1.00 28.50 ?  491 PHE A O     1 
ATOM   3926  C  CB    . PHE A 1 491 ? 141.890 135.969 85.832  1.00 24.90 ?  491 PHE A CB    1 
ATOM   3927  C  CG    . PHE A 1 491 ? 140.595 136.503 86.369  1.00 22.44 ?  491 PHE A CG    1 
ATOM   3928  C  CD1   . PHE A 1 491 ? 139.625 136.986 85.511  1.00 18.33 ?  491 PHE A CD1   1 
ATOM   3929  C  CD2   . PHE A 1 491 ? 140.348 136.524 87.731  1.00 18.60 ?  491 PHE A CD2   1 
ATOM   3930  C  CE1   . PHE A 1 491 ? 138.436 137.482 85.998  1.00 15.30 ?  491 PHE A CE1   1 
ATOM   3931  C  CE2   . PHE A 1 491 ? 139.163 137.022 88.223  1.00 18.33 ?  491 PHE A CE2   1 
ATOM   3932  C  CZ    . PHE A 1 491 ? 138.205 137.500 87.355  1.00 19.82 ?  491 PHE A CZ    1 
ATOM   3933  N  N     . PHE A 1 492 ? 143.849 137.292 87.848  1.00 20.75 ?  492 PHE A N     1 
ATOM   3934  C  CA    . PHE A 1 492 ? 144.025 138.006 89.100  1.00 13.53 ?  492 PHE A CA    1 
ATOM   3935  C  C     . PHE A 1 492 ? 145.109 139.068 89.019  1.00 12.28 ?  492 PHE A C     1 
ATOM   3936  O  O     . PHE A 1 492 ? 145.030 140.054 89.756  1.00 22.08 ?  492 PHE A O     1 
ATOM   3937  C  CB    . PHE A 1 492 ? 144.297 137.011 90.226  1.00 20.06 ?  492 PHE A CB    1 
ATOM   3938  C  CG    . PHE A 1 492 ? 143.074 136.256 90.651  1.00 16.34 ?  492 PHE A CG    1 
ATOM   3939  C  CD1   . PHE A 1 492 ? 142.126 136.854 91.462  1.00 15.80 ?  492 PHE A CD1   1 
ATOM   3940  C  CD2   . PHE A 1 492 ? 142.849 134.967 90.205  1.00 21.73 ?  492 PHE A CD2   1 
ATOM   3941  C  CE1   . PHE A 1 492 ? 140.992 136.169 91.841  1.00 14.75 ?  492 PHE A CE1   1 
ATOM   3942  C  CE2   . PHE A 1 492 ? 141.716 134.278 90.581  1.00 16.11 ?  492 PHE A CE2   1 
ATOM   3943  C  CZ    . PHE A 1 492 ? 140.788 134.878 91.400  1.00 15.69 ?  492 PHE A CZ    1 
ATOM   3944  N  N     . MET A 1 493 ? 146.082 138.934 88.114  1.00 13.10 ?  493 MET A N     1 
ATOM   3945  C  CA    . MET A 1 493 ? 146.969 140.059 87.848  1.00 22.63 ?  493 MET A CA    1 
ATOM   3946  C  C     . MET A 1 493 ? 146.185 141.224 87.263  1.00 18.41 ?  493 MET A C     1 
ATOM   3947  O  O     . MET A 1 493 ? 146.409 142.379 87.634  1.00 28.96 ?  493 MET A O     1 
ATOM   3948  C  CB    . MET A 1 493 ? 148.105 139.634 86.914  1.00 25.38 ?  493 MET A CB    1 
ATOM   3949  C  CG    . MET A 1 493 ? 148.895 140.774 86.257  1.00 20.10 ?  493 MET A CG    1 
ATOM   3950  S  SD    . MET A 1 493 ? 148.154 141.543 84.801  1.00 34.53 ?  493 MET A SD    1 
ATOM   3951  C  CE    . MET A 1 493 ? 148.130 140.160 83.671  1.00 28.29 ?  493 MET A CE    1 
ATOM   3952  N  N     . MET A 1 494 ? 145.256 140.937 86.347  1.00 22.19 ?  494 MET A N     1 
ATOM   3953  C  CA    . MET A 1 494 ? 144.449 142.004 85.764  1.00 17.81 ?  494 MET A CA    1 
ATOM   3954  C  C     . MET A 1 494 ? 143.539 142.636 86.811  1.00 19.45 ?  494 MET A C     1 
ATOM   3955  O  O     . MET A 1 494 ? 143.360 143.861 86.835  1.00 32.12 ?  494 MET A O     1 
ATOM   3956  C  CB    . MET A 1 494 ? 143.629 141.457 84.595  1.00 24.00 ?  494 MET A CB    1 
ATOM   3957  C  CG    . MET A 1 494 ? 144.374 141.494 83.277  1.00 23.09 ?  494 MET A CG    1 
ATOM   3958  S  SD    . MET A 1 494 ? 143.599 140.576 81.936  1.00 41.86 ?  494 MET A SD    1 
ATOM   3959  C  CE    . MET A 1 494 ? 142.153 141.586 81.644  1.00 27.84 ?  494 MET A CE    1 
ATOM   3960  N  N     . VAL A 1 495 ? 142.956 141.810 87.681  1.00 22.31 ?  495 VAL A N     1 
ATOM   3961  C  CA    . VAL A 1 495 ? 142.119 142.323 88.760  1.00 13.04 ?  495 VAL A CA    1 
ATOM   3962  C  C     . VAL A 1 495 ? 142.932 143.219 89.684  1.00 19.56 ?  495 VAL A C     1 
ATOM   3963  O  O     . VAL A 1 495 ? 142.478 144.295 90.083  1.00 26.90 ?  495 VAL A O     1 
ATOM   3964  C  CB    . VAL A 1 495 ? 141.465 141.159 89.527  1.00 15.82 ?  495 VAL A CB    1 
ATOM   3965  C  CG1   . VAL A 1 495 ? 140.861 141.648 90.833  1.00 11.99 ?  495 VAL A CG1   1 
ATOM   3966  C  CG2   . VAL A 1 495 ? 140.411 140.488 88.670  1.00 18.51 ?  495 VAL A CG2   1 
ATOM   3967  N  N     . ASN A 1 496 ? 144.147 142.790 90.038  1.00 23.48 ?  496 ASN A N     1 
ATOM   3968  C  CA    . ASN A 1 496 ? 145.015 143.619 90.867  1.00 15.17 ?  496 ASN A CA    1 
ATOM   3969  C  C     . ASN A 1 496 ? 145.363 144.925 90.168  1.00 17.85 ?  496 ASN A C     1 
ATOM   3970  O  O     . ASN A 1 496 ? 145.349 145.993 90.789  1.00 23.80 ?  496 ASN A O     1 
ATOM   3971  C  CB    . ASN A 1 496 ? 146.285 142.848 91.225  1.00 19.22 ?  496 ASN A CB    1 
ATOM   3972  C  CG    . ASN A 1 496 ? 147.010 143.437 92.414  1.00 18.58 ?  496 ASN A CG    1 
ATOM   3973  O  OD1   . ASN A 1 496 ? 146.387 143.940 93.345  1.00 25.12 ?  496 ASN A OD1   1 
ATOM   3974  N  ND2   . ASN A 1 496 ? 148.333 143.377 92.388  1.00 18.92 ?  496 ASN A ND2   1 
ATOM   3975  N  N     . PHE A 1 497 ? 145.674 144.859 88.872  1.00 21.05 ?  497 PHE A N     1 
ATOM   3976  C  CA    . PHE A 1 497 ? 146.010 146.059 88.115  1.00 15.64 ?  497 PHE A CA    1 
ATOM   3977  C  C     . PHE A 1 497 ? 144.870 147.063 88.150  1.00 24.19 ?  497 PHE A C     1 
ATOM   3978  O  O     . PHE A 1 497 ? 145.073 148.245 88.448  1.00 28.93 ?  497 PHE A O     1 
ATOM   3979  C  CB    . PHE A 1 497 ? 146.344 145.685 86.671  1.00 17.27 ?  497 PHE A CB    1 
ATOM   3980  C  CG    . PHE A 1 497 ? 146.708 146.858 85.806  1.00 19.90 ?  497 PHE A CG    1 
ATOM   3981  C  CD1   . PHE A 1 497 ? 148.018 147.296 85.727  1.00 23.61 ?  497 PHE A CD1   1 
ATOM   3982  C  CD2   . PHE A 1 497 ? 145.741 147.520 85.069  1.00 21.10 ?  497 PHE A CD2   1 
ATOM   3983  C  CE1   . PHE A 1 497 ? 148.353 148.372 84.932  1.00 24.21 ?  497 PHE A CE1   1 
ATOM   3984  C  CE2   . PHE A 1 497 ? 146.073 148.597 84.275  1.00 22.95 ?  497 PHE A CE2   1 
ATOM   3985  C  CZ    . PHE A 1 497 ? 147.380 149.022 84.206  1.00 24.69 ?  497 PHE A CZ    1 
ATOM   3986  N  N     . TYR A 1 498 ? 143.653 146.604 87.868  1.00 26.98 ?  498 TYR A N     1 
ATOM   3987  C  CA    . TYR A 1 498 ? 142.535 147.531 87.796  1.00 18.45 ?  498 TYR A CA    1 
ATOM   3988  C  C     . TYR A 1 498 ? 142.069 147.983 89.173  1.00 22.85 ?  498 TYR A C     1 
ATOM   3989  O  O     . TYR A 1 498 ? 141.589 149.110 89.311  1.00 25.76 ?  498 TYR A O     1 
ATOM   3990  C  CB    . TYR A 1 498 ? 141.396 146.909 86.992  1.00 19.95 ?  498 TYR A CB    1 
ATOM   3991  C  CG    . TYR A 1 498 ? 141.728 146.836 85.522  1.00 24.72 ?  498 TYR A CG    1 
ATOM   3992  C  CD1   . TYR A 1 498 ? 142.009 147.988 84.804  1.00 24.50 ?  498 TYR A CD1   1 
ATOM   3993  C  CD2   . TYR A 1 498 ? 141.787 145.620 84.860  1.00 26.25 ?  498 TYR A CD2   1 
ATOM   3994  C  CE1   . TYR A 1 498 ? 142.326 147.933 83.464  1.00 25.80 ?  498 TYR A CE1   1 
ATOM   3995  C  CE2   . TYR A 1 498 ? 142.101 145.555 83.519  1.00 24.86 ?  498 TYR A CE2   1 
ATOM   3996  C  CZ    . TYR A 1 498 ? 142.370 146.715 82.827  1.00 30.37 ?  498 TYR A CZ    1 
ATOM   3997  O  OH    . TYR A 1 498 ? 142.685 146.661 81.490  1.00 32.57 ?  498 TYR A OH    1 
ATOM   3998  N  N     . SER A 1 499 ? 142.241 147.158 90.209  1.00 23.88 ?  499 SER A N     1 
ATOM   3999  C  CA    . SER A 1 499 ? 141.930 147.612 91.559  1.00 15.88 ?  499 SER A CA    1 
ATOM   4000  C  C     . SER A 1 499 ? 142.918 148.675 92.021  1.00 19.19 ?  499 SER A C     1 
ATOM   4001  O  O     . SER A 1 499 ? 142.522 149.665 92.646  1.00 30.15 ?  499 SER A O     1 
ATOM   4002  C  CB    . SER A 1 499 ? 141.917 146.430 92.527  1.00 15.23 ?  499 SER A CB    1 
ATOM   4003  O  OG    . SER A 1 499 ? 143.223 145.942 92.768  1.00 23.12 ?  499 SER A OG    1 
ATOM   4004  N  N     . ILE A 1 500 ? 144.206 148.497 91.714  1.00 17.80 ?  500 ILE A N     1 
ATOM   4005  C  CA    . ILE A 1 500 ? 145.196 149.518 92.043  1.00 19.65 ?  500 ILE A CA    1 
ATOM   4006  C  C     . ILE A 1 500 ? 144.918 150.794 91.261  1.00 18.17 ?  500 ILE A C     1 
ATOM   4007  O  O     . ILE A 1 500 ? 145.022 151.904 91.797  1.00 28.08 ?  500 ILE A O     1 
ATOM   4008  C  CB    . ILE A 1 500 ? 146.618 148.990 91.782  1.00 22.99 ?  500 ILE A CB    1 
ATOM   4009  C  CG1   . ILE A 1 500 ? 146.972 147.887 92.775  1.00 19.08 ?  500 ILE A CG1   1 
ATOM   4010  C  CG2   . ILE A 1 500 ? 147.633 150.107 91.884  1.00 20.01 ?  500 ILE A CG2   1 
ATOM   4011  C  CD1   . ILE A 1 500 ? 148.142 147.053 92.346  1.00 19.14 ?  500 ILE A CD1   1 
ATOM   4012  N  N     . GLN A 1 501 ? 144.554 150.657 89.984  1.00 24.23 ?  501 GLN A N     1 
ATOM   4013  C  CA    . GLN A 1 501 ? 144.227 151.825 89.174  1.00 22.16 ?  501 GLN A CA    1 
ATOM   4014  C  C     . GLN A 1 501 ? 143.023 152.569 89.733  1.00 28.31 ?  501 GLN A C     1 
ATOM   4015  O  O     . GLN A 1 501 ? 143.031 153.801 89.817  1.00 35.38 ?  501 GLN A O     1 
ATOM   4016  C  CB    . GLN A 1 501 ? 143.971 151.402 87.730  1.00 24.46 ?  501 GLN A CB    1 
ATOM   4017  C  CG    . GLN A 1 501 ? 144.460 152.398 86.701  1.00 25.08 ?  501 GLN A CG    1 
ATOM   4018  C  CD    . GLN A 1 501 ? 144.181 151.950 85.285  1.00 29.25 ?  501 GLN A CD    1 
ATOM   4019  O  OE1   . GLN A 1 501 ? 143.030 151.757 84.897  1.00 28.56 ?  501 GLN A OE1   1 
ATOM   4020  N  NE2   . GLN A 1 501 ? 145.237 151.779 84.501  1.00 33.56 ?  501 GLN A NE2   1 
ATOM   4021  N  N     . ARG A 1 502 ? 141.975 151.840 90.125  1.00 29.65 ?  502 ARG A N     1 
ATOM   4022  C  CA    . ARG A 1 502 ? 140.798 152.486 90.691  1.00 20.32 ?  502 ARG A CA    1 
ATOM   4023  C  C     . ARG A 1 502 ? 141.114 153.139 92.030  1.00 18.03 ?  502 ARG A C     1 
ATOM   4024  O  O     . ARG A 1 502 ? 140.616 154.229 92.322  1.00 30.49 ?  502 ARG A O     1 
ATOM   4025  C  CB    . ARG A 1 502 ? 139.662 151.476 90.839  1.00 24.31 ?  502 ARG A CB    1 
ATOM   4026  C  CG    . ARG A 1 502 ? 138.309 152.114 91.088  1.00 26.79 ?  502 ARG A CG    1 
ATOM   4027  C  CD    . ARG A 1 502 ? 138.020 153.215 90.087  1.00 27.43 ?  502 ARG A CD    1 
ATOM   4028  N  NE    . ARG A 1 502 ? 136.918 154.062 90.522  1.00 25.88 ?  502 ARG A NE    1 
ATOM   4029  C  CZ    . ARG A 1 502 ? 136.863 155.373 90.339  1.00 28.77 ?  502 ARG A CZ    1 
ATOM   4030  N  NH1   . ARG A 1 502 ? 137.833 156.026 89.722  1.00 32.34 1  502 ARG A NH1   1 
ATOM   4031  N  NH2   . ARG A 1 502 ? 135.809 156.048 90.788  1.00 30.22 ?  502 ARG A NH2   1 
ATOM   4032  N  N     . SER A 1 503 ? 141.932 152.489 92.860  1.00 18.39 ?  503 SER A N     1 
ATOM   4033  C  CA    . SER A 1 503 ? 142.315 153.088 94.134  1.00 23.96 ?  503 SER A CA    1 
ATOM   4034  C  C     . SER A 1 503 ? 143.102 154.374 93.921  1.00 24.98 ?  503 SER A C     1 
ATOM   4035  O  O     . SER A 1 503 ? 142.871 155.376 94.608  1.00 27.44 ?  503 SER A O     1 
ATOM   4036  C  CB    . SER A 1 503 ? 143.127 152.085 94.954  1.00 18.45 ?  503 SER A CB    1 
ATOM   4037  O  OG    . SER A 1 503 ? 143.067 152.385 96.335  1.00 22.93 ?  503 SER A OG    1 
ATOM   4038  N  N     . ALA A 1 504 ? 144.026 154.370 92.958  1.00 27.15 ?  504 ALA A N     1 
ATOM   4039  C  CA    . ALA A 1 504 ? 144.793 155.573 92.656  1.00 25.35 ?  504 ALA A CA    1 
ATOM   4040  C  C     . ALA A 1 504 ? 143.903 156.673 92.092  1.00 30.07 ?  504 ALA A C     1 
ATOM   4041  O  O     . ALA A 1 504 ? 144.079 157.850 92.422  1.00 37.59 ?  504 ALA A O     1 
ATOM   4042  C  CB    . ALA A 1 504 ? 145.922 155.239 91.683  1.00 27.51 ?  504 ALA A CB    1 
ATOM   4043  N  N     . GLU A 1 505 ? 142.939 156.312 91.242  1.00 28.85 ?  505 GLU A N     1 
ATOM   4044  C  CA    . GLU A 1 505 ? 142.018 157.304 90.699  1.00 28.97 ?  505 GLU A CA    1 
ATOM   4045  C  C     . GLU A 1 505 ? 141.132 157.896 91.790  1.00 30.69 ?  505 GLU A C     1 
ATOM   4046  O  O     . GLU A 1 505 ? 140.854 159.099 91.785  1.00 35.21 ?  505 GLU A O     1 
ATOM   4047  C  CB    . GLU A 1 505 ? 141.166 156.679 89.597  1.00 29.45 ?  505 GLU A CB    1 
ATOM   4048  C  CG    . GLU A 1 505 ? 141.926 156.403 88.313  1.00 32.55 ?  505 GLU A CG    1 
ATOM   4049  C  CD    . GLU A 1 505 ? 141.297 155.297 87.490  1.00 35.89 ?  505 GLU A CD    1 
ATOM   4050  O  OE1   . GLU A 1 505 ? 140.231 154.786 87.890  1.00 36.53 ?  505 GLU A OE1   1 
ATOM   4051  O  OE2   . GLU A 1 505 ? 141.870 154.939 86.440  1.00 39.44 -1 505 GLU A OE2   1 
ATOM   4052  N  N     . ILE A 1 506 ? 140.676 157.065 92.729  1.00 28.29 ?  506 ILE A N     1 
ATOM   4053  C  CA    . ILE A 1 506 ? 139.879 157.566 93.844  1.00 25.45 ?  506 ILE A CA    1 
ATOM   4054  C  C     . ILE A 1 506 ? 140.712 158.493 94.719  1.00 28.32 ?  506 ILE A C     1 
ATOM   4055  O  O     . ILE A 1 506 ? 140.232 159.538 95.170  1.00 37.79 ?  506 ILE A O     1 
ATOM   4056  C  CB    . ILE A 1 506 ? 139.295 156.392 94.651  1.00 25.65 ?  506 ILE A CB    1 
ATOM   4057  C  CG1   . ILE A 1 506 ? 138.237 155.656 93.831  1.00 28.37 ?  506 ILE A CG1   1 
ATOM   4058  C  CG2   . ILE A 1 506 ? 138.691 156.882 95.953  1.00 27.04 ?  506 ILE A CG2   1 
ATOM   4059  C  CD1   . ILE A 1 506 ? 137.861 154.308 94.398  1.00 22.37 ?  506 ILE A CD1   1 
ATOM   4060  N  N     . ALA A 1 507 ? 141.971 158.129 94.972  1.00 30.87 ?  507 ALA A N     1 
ATOM   4061  C  CA    . ALA A 1 507 ? 142.850 159.002 95.744  1.00 28.95 ?  507 ALA A CA    1 
ATOM   4062  C  C     . ALA A 1 507 ? 143.074 160.330 95.030  1.00 30.76 ?  507 ALA A C     1 
ATOM   4063  O  O     . ALA A 1 507 ? 143.103 161.389 95.668  1.00 33.56 ?  507 ALA A O     1 
ATOM   4064  C  CB    . ALA A 1 507 ? 144.182 158.302 96.010  1.00 25.37 ?  507 ALA A CB    1 
ATOM   4065  N  N     . LYS A 1 508 ? 143.243 160.294 93.708  1.00 36.54 ?  508 LYS A N     1 
ATOM   4066  C  CA    . LYS A 1 508 ? 143.417 161.525 92.941  1.00 33.53 ?  508 LYS A CA    1 
ATOM   4067  C  C     . LYS A 1 508 ? 142.163 162.391 92.984  1.00 38.04 ?  508 LYS A C     1 
ATOM   4068  O  O     . LYS A 1 508 ? 142.254 163.615 93.136  1.00 44.21 ?  508 LYS A O     1 
ATOM   4069  C  CB    . LYS A 1 508 ? 143.782 161.189 91.497  1.00 36.70 ?  508 LYS A CB    1 
ATOM   4070  C  CG    . LYS A 1 508 ? 143.774 162.384 90.561  1.00 40.47 ?  508 LYS A CG    1 
ATOM   4071  C  CD    . LYS A 1 508 ? 143.781 161.947 89.108  1.00 38.88 ?  508 LYS A CD    1 
ATOM   4072  C  CE    . LYS A 1 508 ? 144.033 163.123 88.181  1.00 39.18 ?  508 LYS A CE    1 
ATOM   4073  N  NZ    . LYS A 1 508 ? 144.860 162.737 87.008  1.00 42.23 1  508 LYS A NZ    1 
ATOM   4074  N  N     . GLU A 1 509 ? 140.988 161.777 92.849  1.00 36.02 ?  509 GLU A N     1 
ATOM   4075  C  CA    . GLU A 1 509 ? 139.744 162.540 92.830  1.00 36.32 ?  509 GLU A CA    1 
ATOM   4076  C  C     . GLU A 1 509 ? 139.450 163.148 94.194  1.00 39.00 ?  509 GLU A C     1 
ATOM   4077  O  O     . GLU A 1 509 ? 139.139 164.340 94.302  1.00 43.38 ?  509 GLU A O     1 
ATOM   4078  C  CB    . GLU A 1 509 ? 138.590 161.644 92.379  1.00 36.42 ?  509 GLU A CB    1 
ATOM   4079  C  CG    . GLU A 1 509 ? 138.589 161.331 90.892  1.00 42.34 ?  509 GLU A CG    1 
ATOM   4080  C  CD    . GLU A 1 509 ? 137.811 160.072 90.562  1.00 44.67 ?  509 GLU A CD    1 
ATOM   4081  O  OE1   . GLU A 1 509 ? 137.157 159.520 91.472  1.00 42.56 ?  509 GLU A OE1   1 
ATOM   4082  O  OE2   . GLU A 1 509 ? 137.851 159.635 89.393  1.00 42.61 -1 509 GLU A OE2   1 
ATOM   4083  N  N     . LYS A 1 510 ? 139.543 162.343 95.252  1.00 35.73 ?  510 LYS A N     1 
ATOM   4084  C  CA    . LYS A 1 510 ? 139.276 162.820 96.602  1.00 31.94 ?  510 LYS A CA    1 
ATOM   4085  C  C     . LYS A 1 510 ? 140.456 163.561 97.211  1.00 34.00 ?  510 LYS A C     1 
ATOM   4086  O  O     . LYS A 1 510 ? 140.305 164.152 98.286  1.00 39.30 ?  510 LYS A O     1 
ATOM   4087  C  CB    . LYS A 1 510 ? 138.883 161.646 97.499  1.00 30.48 ?  510 LYS A CB    1 
ATOM   4088  C  CG    . LYS A 1 510 ? 137.776 160.787 96.917  1.00 33.39 ?  510 LYS A CG    1 
ATOM   4089  C  CD    . LYS A 1 510 ? 137.153 159.883 97.963  1.00 33.07 ?  510 LYS A CD    1 
ATOM   4090  C  CE    . LYS A 1 510 ? 136.030 159.060 97.357  1.00 35.82 ?  510 LYS A CE    1 
ATOM   4091  N  NZ    . LYS A 1 510 ? 134.973 158.734 98.347  1.00 34.70 1  510 LYS A NZ    1 
ATOM   4092  N  N     . GLY A 1 511 ? 141.617 163.542 96.561  1.00 37.13 ?  511 GLY A N     1 
ATOM   4093  C  CA    . GLY A 1 511 ? 142.775 164.253 97.063  1.00 37.04 ?  511 GLY A CA    1 
ATOM   4094  C  C     . GLY A 1 511 ? 143.362 163.705 98.340  1.00 40.69 ?  511 GLY A C     1 
ATOM   4095  O  O     . GLY A 1 511 ? 144.216 164.361 98.942  1.00 42.75 ?  511 GLY A O     1 
ATOM   4096  N  N     . GLU A 1 512 ? 142.934 162.523 98.778  1.00 34.12 ?  512 GLU A N     1 
ATOM   4097  C  CA    . GLU A 1 512 ? 143.423 161.929 100.011 1.00 29.43 ?  512 GLU A CA    1 
ATOM   4098  C  C     . GLU A 1 512 ? 143.756 160.462 99.787  1.00 29.65 ?  512 GLU A C     1 
ATOM   4099  O  O     . GLU A 1 512 ? 143.110 159.772 98.996  1.00 33.10 ?  512 GLU A O     1 
ATOM   4100  C  CB    . GLU A 1 512 ? 142.399 162.066 101.146 1.00 31.02 ?  512 GLU A CB    1 
ATOM   4101  C  CG    . GLU A 1 512 ? 141.057 161.418 100.862 1.00 31.59 ?  512 GLU A CG    1 
ATOM   4102  C  CD    . GLU A 1 512 ? 140.357 160.964 102.125 1.00 35.46 ?  512 GLU A CD    1 
ATOM   4103  O  OE1   . GLU A 1 512 ? 141.057 160.630 103.102 1.00 35.24 ?  512 GLU A OE1   1 
ATOM   4104  O  OE2   . GLU A 1 512 ? 139.108 160.940 102.141 1.00 34.76 -1 512 GLU A OE2   1 
ATOM   4105  N  N     . THR A 1 513 ? 144.780 159.999 100.491 1.00 29.89 ?  513 THR A N     1 
ATOM   4106  C  CA    . THR A 1 513 ? 145.193 158.605 100.508 1.00 25.22 ?  513 THR A CA    1 
ATOM   4107  C  C     . THR A 1 513 ? 144.849 158.000 101.865 1.00 27.22 ?  513 THR A C     1 
ATOM   4108  O  O     . THR A 1 513 ? 144.365 158.684 102.771 1.00 36.88 ?  513 THR A O     1 
ATOM   4109  C  CB    . THR A 1 513 ? 146.688 158.484 100.211 1.00 24.19 ?  513 THR A CB    1 
ATOM   4110  O  OG1   . THR A 1 513 ? 147.431 159.215 101.194 1.00 28.55 ?  513 THR A OG1   1 
ATOM   4111  C  CG2   . THR A 1 513 ? 147.005 159.039 98.836  1.00 23.90 ?  513 THR A CG2   1 
ATOM   4112  N  N     . PHE A 1 514 ? 145.099 156.702 102.007 1.00 23.27 ?  514 PHE A N     1 
ATOM   4113  C  CA    . PHE A 1 514 ? 144.890 156.082 103.303 1.00 25.13 ?  514 PHE A CA    1 
ATOM   4114  C  C     . PHE A 1 514 ? 145.997 156.498 104.267 1.00 25.64 ?  514 PHE A C     1 
ATOM   4115  O  O     . PHE A 1 514 ? 147.098 156.881 103.862 1.00 28.15 ?  514 PHE A O     1 
ATOM   4116  C  CB    . PHE A 1 514 ? 144.806 154.557 103.179 1.00 18.28 ?  514 PHE A CB    1 
ATOM   4117  C  CG    . PHE A 1 514 ? 146.093 153.892 102.781 1.00 19.11 ?  514 PHE A CG    1 
ATOM   4118  C  CD1   . PHE A 1 514 ? 146.409 153.708 101.448 1.00 17.86 ?  514 PHE A CD1   1 
ATOM   4119  C  CD2   . PHE A 1 514 ? 146.971 153.418 103.742 1.00 22.51 ?  514 PHE A CD2   1 
ATOM   4120  C  CE1   . PHE A 1 514 ? 147.582 153.082 101.082 1.00 18.86 ?  514 PHE A CE1   1 
ATOM   4121  C  CE2   . PHE A 1 514 ? 148.143 152.793 103.380 1.00 17.63 ?  514 PHE A CE2   1 
ATOM   4122  C  CZ    . PHE A 1 514 ? 148.450 152.628 102.048 1.00 18.53 ?  514 PHE A CZ    1 
ATOM   4123  N  N     . ASP A 1 515 ? 145.682 156.441 105.558 1.00 29.13 ?  515 ASP A N     1 
ATOM   4124  C  CA    . ASP A 1 515 ? 146.606 156.924 106.575 1.00 27.15 ?  515 ASP A CA    1 
ATOM   4125  C  C     . ASP A 1 515 ? 147.916 156.150 106.531 1.00 29.36 ?  515 ASP A C     1 
ATOM   4126  O  O     . ASP A 1 515 ? 147.930 154.921 106.413 1.00 35.37 ?  515 ASP A O     1 
ATOM   4127  C  CB    . ASP A 1 515 ? 145.974 156.812 107.960 1.00 30.15 ?  515 ASP A CB    1 
ATOM   4128  C  CG    . ASP A 1 515 ? 145.066 157.982 108.281 1.00 38.05 ?  515 ASP A CG    1 
ATOM   4129  O  OD1   . ASP A 1 515 ? 144.581 158.638 107.335 1.00 36.62 ?  515 ASP A OD1   1 
ATOM   4130  O  OD2   . ASP A 1 515 ? 144.836 158.244 109.480 1.00 38.93 -1 515 ASP A OD2   1 
ATOM   4131  N  N     . GLN A 1 516 ? 149.023 156.887 106.633 1.00 27.50 ?  516 GLN A N     1 
ATOM   4132  C  CA    . GLN A 1 516 ? 150.370 156.323 106.553 1.00 28.05 ?  516 GLN A CA    1 
ATOM   4133  C  C     . GLN A 1 516 ? 150.598 155.611 105.221 1.00 25.00 ?  516 GLN A C     1 
ATOM   4134  O  O     . GLN A 1 516 ? 151.226 154.555 105.161 1.00 33.02 ?  516 GLN A O     1 
ATOM   4135  C  CB    . GLN A 1 516 ? 150.653 155.381 107.727 1.00 25.48 ?  516 GLN A CB    1 
ATOM   4136  C  CG    . GLN A 1 516 ? 150.484 156.016 109.093 1.00 27.14 ?  516 GLN A CG    1 
ATOM   4137  C  CD    . GLN A 1 516 ? 150.753 155.042 110.219 1.00 29.50 ?  516 GLN A CD    1 
ATOM   4138  O  OE1   . GLN A 1 516 ? 151.900 154.676 110.475 1.00 29.48 ?  516 GLN A OE1   1 
ATOM   4139  N  NE2   . GLN A 1 516 ? 149.698 154.618 110.900 1.00 28.58 ?  516 GLN A NE2   1 
ATOM   4140  N  N     . TYR A 1 517 ? 150.075 156.193 104.141 1.00 23.76 ?  517 TYR A N     1 
ATOM   4141  C  CA    . TYR A 1 517 ? 150.337 155.635 102.819 1.00 23.56 ?  517 TYR A CA    1 
ATOM   4142  C  C     . TYR A 1 517 ? 151.789 155.825 102.406 1.00 27.07 ?  517 TYR A C     1 
ATOM   4143  O  O     . TYR A 1 517 ? 152.357 154.955 101.736 1.00 34.91 ?  517 TYR A O     1 
ATOM   4144  C  CB    . TYR A 1 517 ? 149.415 156.263 101.772 1.00 24.34 ?  517 TYR A CB    1 
ATOM   4145  C  CG    . TYR A 1 517 ? 150.007 156.241 100.380 1.00 26.69 ?  517 TYR A CG    1 
ATOM   4146  C  CD1   . TYR A 1 517 ? 149.973 155.086 99.610  1.00 21.22 ?  517 TYR A CD1   1 
ATOM   4147  C  CD2   . TYR A 1 517 ? 150.615 157.368 99.843  1.00 25.97 ?  517 TYR A CD2   1 
ATOM   4148  C  CE1   . TYR A 1 517 ? 150.520 155.055 98.347  1.00 27.38 ?  517 TYR A CE1   1 
ATOM   4149  C  CE2   . TYR A 1 517 ? 151.168 157.344 98.583  1.00 25.76 ?  517 TYR A CE2   1 
ATOM   4150  C  CZ    . TYR A 1 517 ? 151.118 156.186 97.839  1.00 26.31 ?  517 TYR A CZ    1 
ATOM   4151  O  OH    . TYR A 1 517 ? 151.664 156.162 96.578  1.00 34.34 ?  517 TYR A OH    1 
ATOM   4152  N  N     . GLU A 1 518 ? 152.402 156.946 102.790 1.00 30.87 ?  518 GLU A N     1 
ATOM   4153  C  CA    . GLU A 1 518 ? 153.739 157.275 102.305 1.00 33.64 ?  518 GLU A CA    1 
ATOM   4154  C  C     . GLU A 1 518 ? 154.787 156.261 102.742 1.00 35.51 ?  518 GLU A C     1 
ATOM   4155  O  O     . GLU A 1 518 ? 155.822 156.133 102.079 1.00 38.35 ?  518 GLU A O     1 
ATOM   4156  C  CB    . GLU A 1 518 ? 154.135 158.675 102.776 1.00 34.11 ?  518 GLU A CB    1 
ATOM   4157  C  CG    . GLU A 1 518 ? 153.364 159.801 102.105 1.00 36.55 ?  518 GLU A CG    1 
ATOM   4158  C  CD    . GLU A 1 518 ? 153.632 159.897 100.612 1.00 43.50 ?  518 GLU A CD    1 
ATOM   4159  O  OE1   . GLU A 1 518 ? 154.698 159.429 100.158 1.00 39.21 ?  518 GLU A OE1   1 
ATOM   4160  O  OE2   . GLU A 1 518 ? 152.773 160.446 99.890  1.00 40.04 -1 518 GLU A OE2   1 
ATOM   4161  N  N     . GLY A 1 519 ? 154.552 155.545 103.839 1.00 24.41 ?  519 GLY A N     1 
ATOM   4162  C  CA    . GLY A 1 519 ? 155.446 154.484 104.251 1.00 20.56 ?  519 GLY A CA    1 
ATOM   4163  C  C     . GLY A 1 519 ? 155.188 153.137 103.625 1.00 21.97 ?  519 GLY A C     1 
ATOM   4164  O  O     . GLY A 1 519 ? 155.976 152.210 103.827 1.00 31.43 ?  519 GLY A O     1 
ATOM   4165  N  N     . SER A 1 520 ? 154.104 153.001 102.867 1.00 22.12 ?  520 SER A N     1 
ATOM   4166  C  CA    . SER A 1 520 ? 153.730 151.733 102.264 1.00 24.05 ?  520 SER A CA    1 
ATOM   4167  C  C     . SER A 1 520 ? 154.624 151.416 101.068 1.00 22.41 ?  520 SER A C     1 
ATOM   4168  O  O     . SER A 1 520 ? 155.354 152.267 100.556 1.00 27.98 ?  520 SER A O     1 
ATOM   4169  C  CB    . SER A 1 520 ? 152.264 151.759 101.837 1.00 20.05 ?  520 SER A CB    1 
ATOM   4170  O  OG    . SER A 1 520 ? 152.034 152.784 100.887 1.00 20.38 ?  520 SER A OG    1 
ATOM   4171  N  N     . THR A 1 521 ? 154.558 150.161 100.619 1.00 20.89 ?  521 THR A N     1 
ATOM   4172  C  CA    . THR A 1 521 ? 155.338 149.749 99.460  1.00 19.04 ?  521 THR A CA    1 
ATOM   4173  C  C     . THR A 1 521 ? 154.774 150.305 98.160  1.00 25.45 ?  521 THR A C     1 
ATOM   4174  O  O     . THR A 1 521 ? 155.496 150.358 97.160  1.00 28.88 ?  521 THR A O     1 
ATOM   4175  C  CB    . THR A 1 521 ? 155.406 148.225 99.378  1.00 28.33 ?  521 THR A CB    1 
ATOM   4176  O  OG1   . THR A 1 521 ? 154.080 147.687 99.391  1.00 29.39 ?  521 THR A OG1   1 
ATOM   4177  C  CG2   . THR A 1 521 ? 156.178 147.667 100.559 1.00 20.51 ?  521 THR A CG2   1 
ATOM   4178  N  N     . TYR A 1 522 ? 153.500 150.707 98.148  1.00 28.74 ?  522 TYR A N     1 
ATOM   4179  C  CA    . TYR A 1 522 ? 152.968 151.415 96.990  1.00 21.52 ?  522 TYR A CA    1 
ATOM   4180  C  C     . TYR A 1 522 ? 153.673 152.751 96.798  1.00 25.88 ?  522 TYR A C     1 
ATOM   4181  O  O     . TYR A 1 522 ? 154.016 153.126 95.671  1.00 29.89 ?  522 TYR A O     1 
ATOM   4182  C  CB    . TYR A 1 522 ? 151.462 151.632 97.142  1.00 18.60 ?  522 TYR A CB    1 
ATOM   4183  C  CG    . TYR A 1 522 ? 150.658 150.384 97.420  1.00 21.92 ?  522 TYR A CG    1 
ATOM   4184  C  CD1   . TYR A 1 522 ? 150.432 149.443 96.426  1.00 21.23 ?  522 TYR A CD1   1 
ATOM   4185  C  CD2   . TYR A 1 522 ? 150.100 150.163 98.671  1.00 23.68 ?  522 TYR A CD2   1 
ATOM   4186  C  CE1   . TYR A 1 522 ? 149.688 148.309 96.674  1.00 20.05 ?  522 TYR A CE1   1 
ATOM   4187  C  CE2   . TYR A 1 522 ? 149.352 149.033 98.927  1.00 22.90 ?  522 TYR A CE2   1 
ATOM   4188  C  CZ    . TYR A 1 522 ? 149.151 148.109 97.926  1.00 23.08 ?  522 TYR A CZ    1 
ATOM   4189  O  OH    . TYR A 1 522 ? 148.409 146.981 98.179  1.00 27.20 ?  522 TYR A OH    1 
ATOM   4190  N  N     . ALA A 1 523 ? 153.891 153.485 97.891  1.00 28.81 ?  523 ALA A N     1 
ATOM   4191  C  CA    . ALA A 1 523 ? 154.549 154.783 97.797  1.00 26.99 ?  523 ALA A CA    1 
ATOM   4192  C  C     . ALA A 1 523 ? 156.015 154.636 97.412  1.00 28.38 ?  523 ALA A C     1 
ATOM   4193  O  O     . ALA A 1 523 ? 156.529 155.410 96.597  1.00 32.27 ?  523 ALA A O     1 
ATOM   4194  C  CB    . ALA A 1 523 ? 154.413 155.534 99.120  1.00 23.69 ?  523 ALA A CB    1 
ATOM   4195  N  N     . THR A 1 524 ? 156.703 153.650 97.990  1.00 29.12 ?  524 THR A N     1 
ATOM   4196  C  CA    . THR A 1 524 ? 158.105 153.430 97.659  1.00 28.63 ?  524 THR A CA    1 
ATOM   4197  C  C     . THR A 1 524 ? 158.285 152.781 96.295  1.00 31.29 ?  524 THR A C     1 
ATOM   4198  O  O     . THR A 1 524 ? 159.390 152.824 95.744  1.00 36.00 ?  524 THR A O     1 
ATOM   4199  C  CB    . THR A 1 524 ? 158.770 152.567 98.732  1.00 30.58 ?  524 THR A CB    1 
ATOM   4200  O  OG1   . THR A 1 524 ? 158.296 151.220 98.627  1.00 32.71 ?  524 THR A OG1   1 
ATOM   4201  C  CG2   . THR A 1 524 ? 158.456 153.104 100.118 1.00 27.59 ?  524 THR A CG2   1 
ATOM   4202  N  N     . GLY A 1 525 ? 157.231 152.186 95.739  1.00 25.73 ?  525 GLY A N     1 
ATOM   4203  C  CA    . GLY A 1 525 ? 157.312 151.521 94.457  1.00 27.99 ?  525 GLY A CA    1 
ATOM   4204  C  C     . GLY A 1 525 ? 157.824 150.100 94.500  1.00 32.06 ?  525 GLY A C     1 
ATOM   4205  O  O     . GLY A 1 525 ? 157.899 149.456 93.446  1.00 31.32 ?  525 GLY A O     1 
ATOM   4206  N  N     . GLU A 1 526 ? 158.180 149.589 95.680  1.00 32.87 ?  526 GLU A N     1 
ATOM   4207  C  CA    . GLU A 1 526 ? 158.658 148.217 95.794  1.00 33.19 ?  526 GLU A CA    1 
ATOM   4208  C  C     . GLU A 1 526 ? 157.554 147.203 95.526  1.00 36.82 ?  526 GLU A C     1 
ATOM   4209  O  O     . GLU A 1 526 ? 157.845 146.088 95.079  1.00 40.66 ?  526 GLU A O     1 
ATOM   4210  C  CB    . GLU A 1 526 ? 159.275 148.008 97.182  1.00 33.10 ?  526 GLU A CB    1 
ATOM   4211  C  CG    . GLU A 1 526 ? 159.305 146.573 97.679  1.00 33.56 ?  526 GLU A CG    1 
ATOM   4212  C  CD    . GLU A 1 526 ? 159.340 146.485 99.191  1.00 40.85 ?  526 GLU A CD    1 
ATOM   4213  O  OE1   . GLU A 1 526 ? 159.352 147.545 99.849  1.00 44.68 ?  526 GLU A OE1   1 
ATOM   4214  O  OE2   . GLU A 1 526 ? 159.357 145.354 99.720  1.00 39.17 -1 526 GLU A OE2   1 
ATOM   4215  N  N     . TYR A 1 527 ? 156.294 147.579 95.760  1.00 34.23 ?  527 TYR A N     1 
ATOM   4216  C  CA    . TYR A 1 527 ? 155.179 146.671 95.505  1.00 25.64 ?  527 TYR A CA    1 
ATOM   4217  C  C     . TYR A 1 527 ? 155.112 146.253 94.041  1.00 26.99 ?  527 TYR A C     1 
ATOM   4218  O  O     . TYR A 1 527 ? 154.720 145.121 93.738  1.00 29.87 ?  527 TYR A O     1 
ATOM   4219  C  CB    . TYR A 1 527 ? 153.865 147.332 95.927  1.00 22.95 ?  527 TYR A CB    1 
ATOM   4220  C  CG    . TYR A 1 527 ? 152.636 146.491 95.674  1.00 27.51 ?  527 TYR A CG    1 
ATOM   4221  C  CD1   . TYR A 1 527 ? 152.171 145.601 96.634  1.00 24.78 ?  527 TYR A CD1   1 
ATOM   4222  C  CD2   . TYR A 1 527 ? 151.934 146.589 94.480  1.00 28.27 ?  527 TYR A CD2   1 
ATOM   4223  C  CE1   . TYR A 1 527 ? 151.049 144.831 96.407  1.00 26.06 ?  527 TYR A CE1   1 
ATOM   4224  C  CE2   . TYR A 1 527 ? 150.815 145.821 94.246  1.00 24.90 ?  527 TYR A CE2   1 
ATOM   4225  C  CZ    . TYR A 1 527 ? 150.376 144.946 95.213  1.00 18.91 ?  527 TYR A CZ    1 
ATOM   4226  O  OH    . TYR A 1 527 ? 149.258 144.182 94.983  1.00 30.61 ?  527 TYR A OH    1 
ATOM   4227  N  N     . PHE A 1 528 ? 155.487 147.143 93.127  1.00 29.56 ?  528 PHE A N     1 
ATOM   4228  C  CA    . PHE A 1 528 ? 155.327 146.921 91.698  1.00 28.24 ?  528 PHE A CA    1 
ATOM   4229  C  C     . PHE A 1 528 ? 156.530 146.243 91.053  1.00 34.05 ?  528 PHE A C     1 
ATOM   4230  O  O     . PHE A 1 528 ? 156.602 146.194 89.823  1.00 41.91 ?  528 PHE A O     1 
ATOM   4231  C  CB    . PHE A 1 528 ? 155.056 148.249 90.988  1.00 29.14 ?  528 PHE A CB    1 
ATOM   4232  C  CG    . PHE A 1 528 ? 153.854 148.984 91.505  1.00 31.18 ?  528 PHE A CG    1 
ATOM   4233  C  CD1   . PHE A 1 528 ? 153.971 149.886 92.548  1.00 29.96 ?  528 PHE A CD1   1 
ATOM   4234  C  CD2   . PHE A 1 528 ? 152.607 148.780 90.941  1.00 29.03 ?  528 PHE A CD2   1 
ATOM   4235  C  CE1   . PHE A 1 528 ? 152.867 150.566 93.020  1.00 32.17 ?  528 PHE A CE1   1 
ATOM   4236  C  CE2   . PHE A 1 528 ? 151.500 149.457 91.411  1.00 29.46 ?  528 PHE A CE2   1 
ATOM   4237  C  CZ    . PHE A 1 528 ? 151.630 150.351 92.451  1.00 28.16 ?  528 PHE A CZ    1 
ATOM   4238  N  N     . ASP A 1 529 ? 157.471 145.726 91.848  1.00 34.97 ?  529 ASP A N     1 
ATOM   4239  C  CA    . ASP A 1 529 ? 158.705 145.184 91.285  1.00 32.88 ?  529 ASP A CA    1 
ATOM   4240  C  C     . ASP A 1 529 ? 158.427 144.003 90.362  1.00 34.45 ?  529 ASP A C     1 
ATOM   4241  O  O     . ASP A 1 529 ? 158.863 143.986 89.204  1.00 41.56 ?  529 ASP A O     1 
ATOM   4242  C  CB    . ASP A 1 529 ? 159.651 144.768 92.412  1.00 35.83 ?  529 ASP A CB    1 
ATOM   4243  C  CG    . ASP A 1 529 ? 160.371 145.946 93.033  1.00 42.01 ?  529 ASP A CG    1 
ATOM   4244  O  OD1   . ASP A 1 529 ? 160.296 147.057 92.469  1.00 41.20 ?  529 ASP A OD1   1 
ATOM   4245  O  OD2   . ASP A 1 529 ? 161.016 145.760 94.086  1.00 42.29 -1 529 ASP A OD2   1 
ATOM   4246  N  N     . LYS A 1 530 ? 157.690 143.005 90.857  1.00 37.67 ?  530 LYS A N     1 
ATOM   4247  C  CA    . LYS A 1 530 ? 157.390 141.833 90.045  1.00 38.51 ?  530 LYS A CA    1 
ATOM   4248  C  C     . LYS A 1 530 ? 156.446 142.155 88.898  1.00 36.82 ?  530 LYS A C     1 
ATOM   4249  O  O     . LYS A 1 530 ? 156.372 141.385 87.936  1.00 40.77 ?  530 LYS A O     1 
ATOM   4250  C  CB    . LYS A 1 530 ? 156.792 140.726 90.914  1.00 38.22 ?  530 LYS A CB    1 
ATOM   4251  C  CG    . LYS A 1 530 ? 155.277 140.736 90.985  1.00 32.22 ?  530 LYS A CG    1 
ATOM   4252  C  CD    . LYS A 1 530 ? 154.771 139.766 92.034  1.00 34.28 ?  530 LYS A CD    1 
ATOM   4253  C  CE    . LYS A 1 530 ? 153.259 139.694 92.028  1.00 34.98 ?  530 LYS A CE    1 
ATOM   4254  N  NZ    . LYS A 1 530 ? 152.714 139.823 93.403  1.00 38.69 1  530 LYS A NZ    1 
ATOM   4255  N  N     . TYR A 1 531 ? 155.729 143.270 88.976  1.00 32.53 ?  531 TYR A N     1 
ATOM   4256  C  CA    . TYR A 1 531 ? 154.815 143.658 87.914  1.00 28.43 ?  531 TYR A CA    1 
ATOM   4257  C  C     . TYR A 1 531 ? 155.504 144.443 86.811  1.00 29.37 ?  531 TYR A C     1 
ATOM   4258  O  O     . TYR A 1 531 ? 155.115 144.327 85.643  1.00 35.21 ?  531 TYR A O     1 
ATOM   4259  C  CB    . TYR A 1 531 ? 153.664 144.471 88.499  1.00 25.66 ?  531 TYR A CB    1 
ATOM   4260  C  CG    . TYR A 1 531 ? 152.676 143.633 89.269  1.00 29.92 ?  531 TYR A CG    1 
ATOM   4261  C  CD1   . TYR A 1 531 ? 152.088 142.519 88.689  1.00 29.59 ?  531 TYR A CD1   1 
ATOM   4262  C  CD2   . TYR A 1 531 ? 152.334 143.949 90.575  1.00 27.27 ?  531 TYR A CD2   1 
ATOM   4263  C  CE1   . TYR A 1 531 ? 151.184 141.747 89.383  1.00 32.41 ?  531 TYR A CE1   1 
ATOM   4264  C  CE2   . TYR A 1 531 ? 151.431 143.182 91.278  1.00 25.93 ?  531 TYR A CE2   1 
ATOM   4265  C  CZ    . TYR A 1 531 ? 150.859 142.083 90.677  1.00 28.95 ?  531 TYR A CZ    1 
ATOM   4266  O  OH    . TYR A 1 531 ? 149.958 141.313 91.372  1.00 30.57 ?  531 TYR A OH    1 
ATOM   4267  N  N     . VAL A 1 532 ? 156.520 145.239 87.152  1.00 36.10 ?  532 VAL A N     1 
ATOM   4268  C  CA    . VAL A 1 532 ? 157.314 145.926 86.140  1.00 35.37 ?  532 VAL A CA    1 
ATOM   4269  C  C     . VAL A 1 532 ? 158.441 145.058 85.604  1.00 37.91 ?  532 VAL A C     1 
ATOM   4270  O  O     . VAL A 1 532 ? 159.034 145.401 84.569  1.00 42.70 ?  532 VAL A O     1 
ATOM   4271  C  CB    . VAL A 1 532 ? 157.901 147.243 86.688  1.00 36.98 ?  532 VAL A CB    1 
ATOM   4272  C  CG1   . VAL A 1 532 ? 156.792 148.143 87.208  1.00 33.66 ?  532 VAL A CG1   1 
ATOM   4273  C  CG2   . VAL A 1 532 ? 158.928 146.963 87.773  1.00 36.45 ?  532 VAL A CG2   1 
ATOM   4274  N  N     . SER A 1 533 ? 158.759 143.946 86.266  1.00 37.93 ?  533 SER A N     1 
ATOM   4275  C  CA    . SER A 1 533 ? 159.812 143.049 85.804  1.00 36.60 ?  533 SER A CA    1 
ATOM   4276  C  C     . SER A 1 533 ? 159.281 141.812 85.094  1.00 41.39 ?  533 SER A C     1 
ATOM   4277  O  O     . SER A 1 533 ? 159.859 141.386 84.090  1.00 43.93 ?  533 SER A O     1 
ATOM   4278  C  CB    . SER A 1 533 ? 160.689 142.616 86.982  1.00 41.09 ?  533 SER A CB    1 
ATOM   4279  O  OG    . SER A 1 533 ? 160.121 141.511 87.663  1.00 42.74 ?  533 SER A OG    1 
ATOM   4280  N  N     . THR A 1 534 ? 158.194 141.224 85.586  1.00 42.79 ?  534 THR A N     1 
ATOM   4281  C  CA    . THR A 1 534 ? 157.667 139.972 85.063  1.00 38.26 ?  534 THR A CA    1 
ATOM   4282  C  C     . THR A 1 534 ? 156.372 140.222 84.302  1.00 37.89 ?  534 THR A C     1 
ATOM   4283  O  O     . THR A 1 534 ? 155.497 140.957 84.769  1.00 42.30 ?  534 THR A O     1 
ATOM   4284  C  CB    . THR A 1 534 ? 157.420 138.968 86.196  1.00 36.43 ?  534 THR A CB    1 
ATOM   4285  O  OG1   . THR A 1 534 ? 158.669 138.595 86.788  1.00 42.70 ?  534 THR A OG1   1 
ATOM   4286  C  CG2   . THR A 1 534 ? 156.721 137.721 85.676  1.00 39.87 ?  534 THR A CG2   1 
ATOM   4287  N  N     . ASP A 1 535 ? 156.261 139.611 83.125  1.00 40.76 ?  535 ASP A N     1 
ATOM   4288  C  CA    . ASP A 1 535 ? 155.040 139.663 82.334  1.00 41.03 ?  535 ASP A CA    1 
ATOM   4289  C  C     . ASP A 1 535 ? 154.113 138.533 82.761  1.00 44.13 ?  535 ASP A C     1 
ATOM   4290  O  O     . ASP A 1 535 ? 154.553 137.393 82.935  1.00 45.35 ?  535 ASP A O     1 
ATOM   4291  C  CB    . ASP A 1 535 ? 155.357 139.556 80.843  1.00 41.69 ?  535 ASP A CB    1 
ATOM   4292  C  CG    . ASP A 1 535 ? 154.151 139.154 80.017  1.00 47.77 ?  535 ASP A CG    1 
ATOM   4293  O  OD1   . ASP A 1 535 ? 153.312 140.031 79.719  1.00 48.39 ?  535 ASP A OD1   1 
ATOM   4294  O  OD2   . ASP A 1 535 ? 154.041 137.959 79.669  1.00 46.71 -1 535 ASP A OD2   1 
ATOM   4295  N  N     . PHE A 1 536 ? 152.830 138.853 82.932  1.00 33.07 ?  536 PHE A N     1 
ATOM   4296  C  CA    . PHE A 1 536 ? 151.841 137.885 83.387  1.00 31.59 ?  536 PHE A CA    1 
ATOM   4297  C  C     . PHE A 1 536 ? 150.824 137.544 82.304  1.00 38.43 ?  536 PHE A C     1 
ATOM   4298  O  O     . PHE A 1 536 ? 149.712 137.110 82.616  1.00 40.84 ?  536 PHE A O     1 
ATOM   4299  C  CB    . PHE A 1 536 ? 151.138 138.399 84.642  1.00 32.63 ?  536 PHE A CB    1 
ATOM   4300  C  CG    . PHE A 1 536 ? 152.039 138.506 85.838  1.00 33.32 ?  536 PHE A CG    1 
ATOM   4301  C  CD1   . PHE A 1 536 ? 152.787 139.649 86.059  1.00 32.41 ?  536 PHE A CD1   1 
ATOM   4302  C  CD2   . PHE A 1 536 ? 152.146 137.460 86.737  1.00 29.13 ?  536 PHE A CD2   1 
ATOM   4303  C  CE1   . PHE A 1 536 ? 153.618 139.746 87.156  1.00 33.49 ?  536 PHE A CE1   1 
ATOM   4304  C  CE2   . PHE A 1 536 ? 152.976 137.552 87.834  1.00 28.57 ?  536 PHE A CE2   1 
ATOM   4305  C  CZ    . PHE A 1 536 ? 153.711 138.696 88.044  1.00 31.83 ?  536 PHE A CZ    1 
ATOM   4306  N  N     . SER A 1 537 ? 151.183 137.743 81.039  1.00 39.75 ?  537 SER A N     1 
ATOM   4307  C  CA    . SER A 1 537 ? 150.341 137.311 79.940  1.00 37.63 ?  537 SER A CA    1 
ATOM   4308  C  C     . SER A 1 537 ? 150.243 135.784 79.932  1.00 38.56 ?  537 SER A C     1 
ATOM   4309  O  O     . SER A 1 537 ? 151.181 135.098 80.346  1.00 43.02 ?  537 SER A O     1 
ATOM   4310  C  CB    . SER A 1 537 ? 150.912 137.811 78.614  1.00 38.04 ?  537 SER A CB    1 
ATOM   4311  O  OG    . SER A 1 537 ? 150.039 137.549 77.530  1.00 45.62 ?  537 SER A OG    1 
ATOM   4312  N  N     . PRO A 1 538 ? 149.113 135.231 79.490  1.00 39.69 ?  538 PRO A N     1 
ATOM   4313  C  CA    . PRO A 1 538 ? 148.961 133.772 79.499  1.00 38.42 ?  538 PRO A CA    1 
ATOM   4314  C  C     . PRO A 1 538 ? 150.028 133.085 78.660  1.00 41.89 ?  538 PRO A C     1 
ATOM   4315  O  O     . PRO A 1 538 ? 150.382 133.543 77.571  1.00 40.90 ?  538 PRO A O     1 
ATOM   4316  C  CB    . PRO A 1 538 ? 147.562 133.556 78.912  1.00 37.81 ?  538 PRO A CB    1 
ATOM   4317  C  CG    . PRO A 1 538 ? 146.853 134.843 79.131  1.00 39.79 ?  538 PRO A CG    1 
ATOM   4318  C  CD    . PRO A 1 538 ? 147.894 135.908 79.017  1.00 37.05 ?  538 PRO A CD    1 
ATOM   4319  N  N     . LYS A 1 539 ? 150.540 131.971 79.182  1.00 42.14 ?  539 LYS A N     1 
ATOM   4320  C  CA    . LYS A 1 539 ? 151.565 131.193 78.502  1.00 41.99 ?  539 LYS A CA    1 
ATOM   4321  C  C     . LYS A 1 539 ? 150.993 130.126 77.579  1.00 44.20 ?  539 LYS A C     1 
ATOM   4322  O  O     . LYS A 1 539 ? 151.752 129.515 76.820  1.00 48.33 ?  539 LYS A O     1 
ATOM   4323  C  CB    . LYS A 1 539 ? 152.491 130.528 79.526  1.00 44.26 ?  539 LYS A CB    1 
ATOM   4324  C  CG    . LYS A 1 539 ? 152.774 131.377 80.752  1.00 46.33 ?  539 LYS A CG    1 
ATOM   4325  C  CD    . LYS A 1 539 ? 154.100 132.110 80.625  1.00 45.75 ?  539 LYS A CD    1 
ATOM   4326  C  CE    . LYS A 1 539 ? 154.194 133.252 81.624  1.00 46.33 ?  539 LYS A CE    1 
ATOM   4327  N  NZ    . LYS A 1 539 ? 153.398 134.435 81.195  1.00 44.50 1  539 LYS A NZ    1 
ATOM   4328  N  N     . TYR A 1 540 ? 149.686 129.888 77.623  1.00 43.85 ?  540 TYR A N     1 
ATOM   4329  C  CA    . TYR A 1 540 ? 149.037 128.881 76.799  1.00 43.78 ?  540 TYR A CA    1 
ATOM   4330  C  C     . TYR A 1 540 ? 148.097 129.547 75.804  1.00 46.70 ?  540 TYR A C     1 
ATOM   4331  O  O     . TYR A 1 540 ? 147.406 130.514 76.140  1.00 45.29 ?  540 TYR A O     1 
ATOM   4332  C  CB    . TYR A 1 540 ? 148.267 127.875 77.660  1.00 41.74 ?  540 TYR A CB    1 
ATOM   4333  C  CG    . TYR A 1 540 ? 149.138 127.152 78.660  1.00 45.65 ?  540 TYR A CG    1 
ATOM   4334  C  CD1   . TYR A 1 540 ? 149.383 127.688 79.916  1.00 45.44 ?  540 TYR A CD1   1 
ATOM   4335  C  CD2   . TYR A 1 540 ? 149.727 125.937 78.341  1.00 45.66 ?  540 TYR A CD2   1 
ATOM   4336  C  CE1   . TYR A 1 540 ? 150.184 127.032 80.827  1.00 46.54 ?  540 TYR A CE1   1 
ATOM   4337  C  CE2   . TYR A 1 540 ? 150.529 125.273 79.245  1.00 41.75 ?  540 TYR A CE2   1 
ATOM   4338  C  CZ    . TYR A 1 540 ? 150.753 125.824 80.487  1.00 45.77 ?  540 TYR A CZ    1 
ATOM   4339  O  OH    . TYR A 1 540 ? 151.554 125.165 81.389  1.00 45.71 ?  540 TYR A OH    1 
ATOM   4340  N  N     . GLU A 1 541 ? 148.087 129.027 74.575  1.00 49.36 ?  541 GLU A N     1 
ATOM   4341  C  CA    . GLU A 1 541 ? 147.226 129.592 73.543  1.00 47.22 ?  541 GLU A CA    1 
ATOM   4342  C  C     . GLU A 1 541 ? 145.752 129.408 73.880  1.00 49.17 ?  541 GLU A C     1 
ATOM   4343  O  O     . GLU A 1 541 ? 144.925 130.248 73.510  1.00 47.50 ?  541 GLU A O     1 
ATOM   4344  C  CB    . GLU A 1 541 ? 147.557 128.972 72.182  1.00 48.57 ?  541 GLU A CB    1 
ATOM   4345  C  CG    . GLU A 1 541 ? 147.000 127.571 71.949  1.00 52.66 ?  541 GLU A CG    1 
ATOM   4346  C  CD    . GLU A 1 541 ? 147.696 126.509 72.783  1.00 57.43 ?  541 GLU A CD    1 
ATOM   4347  O  OE1   . GLU A 1 541 ? 148.822 126.763 73.260  1.00 55.11 ?  541 GLU A OE1   1 
ATOM   4348  O  OE2   . GLU A 1 541 ? 147.115 125.418 72.961  1.00 52.48 -1 541 GLU A OE2   1 
ATOM   4349  N  N     . LYS A 1 542 ? 145.405 128.324 74.577  1.00 47.03 ?  542 LYS A N     1 
ATOM   4350  C  CA    . LYS A 1 542 ? 144.021 128.128 74.996  1.00 44.20 ?  542 LYS A CA    1 
ATOM   4351  C  C     . LYS A 1 542 ? 143.583 129.217 75.965  1.00 43.71 ?  542 LYS A C     1 
ATOM   4352  O  O     . LYS A 1 542 ? 142.470 129.746 75.857  1.00 46.35 ?  542 LYS A O     1 
ATOM   4353  C  CB    . LYS A 1 542 ? 143.858 126.749 75.631  1.00 42.74 ?  542 LYS A CB    1 
ATOM   4354  C  CG    . LYS A 1 542 ? 142.414 126.326 75.833  1.00 44.00 ?  542 LYS A CG    1 
ATOM   4355  C  CD    . LYS A 1 542 ? 142.298 125.277 76.926  1.00 44.81 ?  542 LYS A CD    1 
ATOM   4356  C  CE    . LYS A 1 542 ? 140.965 124.553 76.858  1.00 46.45 ?  542 LYS A CE    1 
ATOM   4357  N  NZ    . LYS A 1 542 ? 139.832 125.498 76.659  1.00 47.24 1  542 LYS A NZ    1 
ATOM   4358  N  N     . ILE A 1 543 ? 144.443 129.561 76.923  1.00 40.29 ?  543 ILE A N     1 
ATOM   4359  C  CA    . ILE A 1 543 ? 144.115 130.607 77.886  1.00 38.16 ?  543 ILE A CA    1 
ATOM   4360  C  C     . ILE A 1 543 ? 144.139 131.976 77.220  1.00 39.04 ?  543 ILE A C     1 
ATOM   4361  O  O     . ILE A 1 543 ? 143.324 132.850 77.539  1.00 41.31 ?  543 ILE A O     1 
ATOM   4362  C  CB    . ILE A 1 543 ? 145.074 130.539 79.087  1.00 38.43 ?  543 ILE A CB    1 
ATOM   4363  C  CG1   . ILE A 1 543 ? 145.038 129.147 79.720  1.00 38.67 ?  543 ILE A CG1   1 
ATOM   4364  C  CG2   . ILE A 1 543 ? 144.716 131.595 80.112  1.00 39.41 ?  543 ILE A CG2   1 
ATOM   4365  C  CD1   . ILE A 1 543 ? 143.643 128.634 79.996  1.00 37.81 ?  543 ILE A CD1   1 
ATOM   4366  N  N     . ALA A 1 544 ? 145.076 132.190 76.293  1.00 41.27 ?  544 ALA A N     1 
ATOM   4367  C  CA    . ALA A 1 544 ? 145.188 133.489 75.637  1.00 43.83 ?  544 ALA A CA    1 
ATOM   4368  C  C     . ALA A 1 544 ? 143.944 133.825 74.827  1.00 43.06 ?  544 ALA A C     1 
ATOM   4369  O  O     . ALA A 1 544 ? 143.605 135.005 74.676  1.00 43.78 ?  544 ALA A O     1 
ATOM   4370  C  CB    . ALA A 1 544 ? 146.427 133.519 74.743  1.00 44.54 ?  544 ALA A CB    1 
ATOM   4371  N  N     . ASN A 1 545 ? 143.254 132.814 74.294  1.00 44.96 ?  545 ASN A N     1 
ATOM   4372  C  CA    . ASN A 1 545 ? 142.010 133.076 73.578  1.00 46.63 ?  545 ASN A CA    1 
ATOM   4373  C  C     . ASN A 1 545 ? 140.874 133.418 74.531  1.00 46.37 ?  545 ASN A C     1 
ATOM   4374  O  O     . ASN A 1 545 ? 139.920 134.095 74.136  1.00 45.67 ?  545 ASN A O     1 
ATOM   4375  C  CB    . ASN A 1 545 ? 141.633 131.877 72.708  1.00 46.98 ?  545 ASN A CB    1 
ATOM   4376  C  CG    . ASN A 1 545 ? 142.771 131.422 71.818  1.00 50.71 ?  545 ASN A CG    1 
ATOM   4377  O  OD1   . ASN A 1 545 ? 143.688 132.188 71.524  1.00 50.89 ?  545 ASN A OD1   1 
ATOM   4378  N  ND2   . ASN A 1 545 ? 142.718 130.168 71.384  1.00 49.17 ?  545 ASN A ND2   1 
ATOM   4379  N  N     . LEU A 1 546 ? 140.951 132.954 75.782  1.00 44.44 ?  546 LEU A N     1 
ATOM   4380  C  CA    . LEU A 1 546 ? 139.930 133.306 76.762  1.00 42.41 ?  546 LEU A CA    1 
ATOM   4381  C  C     . LEU A 1 546 ? 139.930 134.800 77.054  1.00 42.24 ?  546 LEU A C     1 
ATOM   4382  O  O     . LEU A 1 546 ? 138.886 135.366 77.398  1.00 45.24 ?  546 LEU A O     1 
ATOM   4383  C  CB    . LEU A 1 546 ? 140.143 132.515 78.052  1.00 40.80 ?  546 LEU A CB    1 
ATOM   4384  C  CG    . LEU A 1 546 ? 139.942 131.001 77.984  1.00 39.12 ?  546 LEU A CG    1 
ATOM   4385  C  CD1   . LEU A 1 546 ? 140.273 130.367 79.322  1.00 39.65 ?  546 LEU A CD1   1 
ATOM   4386  C  CD2   . LEU A 1 546 ? 138.521 130.663 77.568  1.00 40.10 ?  546 LEU A CD2   1 
ATOM   4387  N  N     . PHE A 1 547 ? 141.082 135.452 76.919  1.00 40.24 ?  547 PHE A N     1 
ATOM   4388  C  CA    . PHE A 1 547 ? 141.212 136.881 77.158  1.00 40.24 ?  547 PHE A CA    1 
ATOM   4389  C  C     . PHE A 1 547 ? 141.163 137.695 75.872  1.00 40.78 ?  547 PHE A C     1 
ATOM   4390  O  O     . PHE A 1 547 ? 141.432 138.900 75.904  1.00 42.05 ?  547 PHE A O     1 
ATOM   4391  C  CB    . PHE A 1 547 ? 142.511 137.171 77.912  1.00 36.73 ?  547 PHE A CB    1 
ATOM   4392  C  CG    . PHE A 1 547 ? 142.497 136.718 79.343  1.00 38.42 ?  547 PHE A CG    1 
ATOM   4393  C  CD1   . PHE A 1 547 ? 141.979 137.530 80.335  1.00 37.60 ?  547 PHE A CD1   1 
ATOM   4394  C  CD2   . PHE A 1 547 ? 143.004 135.479 79.695  1.00 37.01 ?  547 PHE A CD2   1 
ATOM   4395  C  CE1   . PHE A 1 547 ? 141.967 137.117 81.652  1.00 33.39 ?  547 PHE A CE1   1 
ATOM   4396  C  CE2   . PHE A 1 547 ? 142.993 135.060 81.010  1.00 35.07 ?  547 PHE A CE2   1 
ATOM   4397  C  CZ    . PHE A 1 547 ? 142.475 135.880 81.989  1.00 34.33 ?  547 PHE A CZ    1 
ATOM   4398  N  N     . GLU A 1 548 ? 140.835 137.066 74.747  1.00 50.24 ?  548 GLU A N     1 
ATOM   4399  C  CA    . GLU A 1 548 ? 140.751 137.781 73.481  1.00 52.22 ?  548 GLU A CA    1 
ATOM   4400  C  C     . GLU A 1 548 ? 139.635 138.816 73.532  1.00 51.05 ?  548 GLU A C     1 
ATOM   4401  O  O     . GLU A 1 548 ? 138.537 138.546 74.023  1.00 51.91 ?  548 GLU A O     1 
ATOM   4402  C  CB    . GLU A 1 548 ? 140.525 136.795 72.333  1.00 48.82 ?  548 GLU A CB    1 
ATOM   4403  C  CG    . GLU A 1 548 ? 139.890 137.388 71.079  1.00 51.53 ?  548 GLU A CG    1 
ATOM   4404  C  CD    . GLU A 1 548 ? 138.374 137.289 71.083  1.00 52.72 ?  548 GLU A CD    1 
ATOM   4405  O  OE1   . GLU A 1 548 ? 137.717 138.214 70.561  1.00 51.34 ?  548 GLU A OE1   1 
ATOM   4406  O  OE2   . GLU A 1 548 ? 137.844 136.285 71.603  1.00 53.80 -1 548 GLU A OE2   1 
ATOM   4407  N  N     . GLY A 1 549 ? 139.922 140.008 73.012  1.00 45.32 ?  549 GLY A N     1 
ATOM   4408  C  CA    . GLY A 1 549 ? 139.003 141.119 73.109  1.00 46.85 ?  549 GLY A CA    1 
ATOM   4409  C  C     . GLY A 1 549 ? 139.096 141.906 74.396  1.00 47.31 ?  549 GLY A C     1 
ATOM   4410  O  O     . GLY A 1 549 ? 138.301 142.834 74.595  1.00 46.90 ?  549 GLY A O     1 
ATOM   4411  N  N     . MET A 1 550 ? 140.037 141.568 75.274  1.00 47.64 ?  550 MET A N     1 
ATOM   4412  C  CA    . MET A 1 550 ? 140.225 142.251 76.544  1.00 44.25 ?  550 MET A CA    1 
ATOM   4413  C  C     . MET A 1 550 ? 141.709 142.519 76.729  1.00 44.66 ?  550 MET A C     1 
ATOM   4414  O  O     . MET A 1 550 ? 142.521 141.590 76.674  1.00 48.18 ?  550 MET A O     1 
ATOM   4415  C  CB    . MET A 1 550 ? 139.675 141.411 77.699  1.00 43.54 ?  550 MET A CB    1 
ATOM   4416  C  CG    . MET A 1 550 ? 139.112 142.219 78.850  1.00 48.40 ?  550 MET A CG    1 
ATOM   4417  S  SD    . MET A 1 550 ? 138.803 141.219 80.316  1.00 55.01 ?  550 MET A SD    1 
ATOM   4418  C  CE    . MET A 1 550 ? 138.783 139.567 79.625  1.00 44.39 ?  550 MET A CE    1 
ATOM   4419  N  N     . HIS A 1 551 ? 142.064 143.784 76.944  1.00 40.57 ?  551 HIS A N     1 
ATOM   4420  C  CA    . HIS A 1 551 ? 143.468 144.161 77.019  1.00 40.38 ?  551 HIS A CA    1 
ATOM   4421  C  C     . HIS A 1 551 ? 144.104 143.634 78.300  1.00 41.17 ?  551 HIS A C     1 
ATOM   4422  O  O     . HIS A 1 551 ? 143.571 143.825 79.397  1.00 42.19 ?  551 HIS A O     1 
ATOM   4423  C  CB    . HIS A 1 551 ? 143.619 145.678 76.943  1.00 39.62 ?  551 HIS A CB    1 
ATOM   4424  C  CG    . HIS A 1 551 ? 144.996 146.163 77.273  1.00 43.71 ?  551 HIS A CG    1 
ATOM   4425  N  ND1   . HIS A 1 551 ? 146.035 146.122 76.368  1.00 46.46 ?  551 HIS A ND1   1 
ATOM   4426  C  CD2   . HIS A 1 551 ? 145.507 146.695 78.409  1.00 43.40 ?  551 HIS A CD2   1 
ATOM   4427  C  CE1   . HIS A 1 551 ? 147.126 146.609 76.932  1.00 44.87 ?  551 HIS A CE1   1 
ATOM   4428  N  NE2   . HIS A 1 551 ? 146.833 146.964 78.169  1.00 43.03 ?  551 HIS A NE2   1 
ATOM   4429  N  N     . ILE A 1 552 ? 145.246 142.976 78.155  1.00 37.11 ?  552 ILE A N     1 
ATOM   4430  C  CA    . ILE A 1 552 ? 146.016 142.453 79.280  1.00 36.65 ?  552 ILE A CA    1 
ATOM   4431  C  C     . ILE A 1 552 ? 147.156 143.427 79.559  1.00 39.13 ?  552 ILE A C     1 
ATOM   4432  O  O     . ILE A 1 552 ? 147.997 143.641 78.673  1.00 41.15 ?  552 ILE A O     1 
ATOM   4433  C  CB    . ILE A 1 552 ? 146.554 141.045 78.989  1.00 36.39 ?  552 ILE A CB    1 
ATOM   4434  C  CG1   . ILE A 1 552 ? 145.399 140.085 78.701  1.00 35.61 ?  552 ILE A CG1   1 
ATOM   4435  C  CG2   . ILE A 1 552 ? 147.388 140.544 80.151  1.00 35.93 ?  552 ILE A CG2   1 
ATOM   4436  C  CD1   . ILE A 1 552 ? 145.839 138.772 78.106  1.00 39.04 ?  552 ILE A CD1   1 
ATOM   4437  N  N     . PRO A 1 553 ? 147.215 144.040 80.741  1.00 41.21 ?  553 PRO A N     1 
ATOM   4438  C  CA    . PRO A 1 553 ? 148.310 144.974 81.032  1.00 37.58 ?  553 PRO A CA    1 
ATOM   4439  C  C     . PRO A 1 553 ? 149.667 144.294 80.945  1.00 37.53 ?  553 PRO A C     1 
ATOM   4440  O  O     . PRO A 1 553 ? 149.864 143.182 81.439  1.00 35.05 ?  553 PRO A O     1 
ATOM   4441  C  CB    . PRO A 1 553 ? 148.005 145.442 82.459  1.00 34.42 ?  553 PRO A CB    1 
ATOM   4442  C  CG    . PRO A 1 553 ? 146.553 145.185 82.643  1.00 32.51 ?  553 PRO A CG    1 
ATOM   4443  C  CD    . PRO A 1 553 ? 146.242 143.970 81.840  1.00 33.93 ?  553 PRO A CD    1 
ATOM   4444  N  N     . THR A 1 554 ? 150.605 144.984 80.314  1.00 42.64 ?  554 THR A N     1 
ATOM   4445  C  CA    . THR A 1 554 ? 151.957 144.497 80.119  1.00 40.12 ?  554 THR A CA    1 
ATOM   4446  C  C     . THR A 1 554 ? 152.871 145.086 81.189  1.00 36.10 ?  554 THR A C     1 
ATOM   4447  O  O     . THR A 1 554 ? 152.415 145.691 82.164  1.00 38.78 ?  554 THR A O     1 
ATOM   4448  C  CB    . THR A 1 554 ? 152.434 144.842 78.708  1.00 38.52 ?  554 THR A CB    1 
ATOM   4449  O  OG1   . THR A 1 554 ? 152.435 146.264 78.538  1.00 43.66 ?  554 THR A OG1   1 
ATOM   4450  C  CG2   . THR A 1 554 ? 151.517 144.216 77.671  1.00 40.83 ?  554 THR A CG2   1 
ATOM   4451  N  N     . THR A 1 555 ? 154.180 144.901 81.017  1.00 38.32 ?  555 THR A N     1 
ATOM   4452  C  CA    . THR A 1 555 ? 155.130 145.532 81.924  1.00 35.88 ?  555 THR A CA    1 
ATOM   4453  C  C     . THR A 1 555 ? 155.106 147.048 81.776  1.00 38.84 ?  555 THR A C     1 
ATOM   4454  O  O     . THR A 1 555 ? 155.263 147.774 82.763  1.00 42.01 ?  555 THR A O     1 
ATOM   4455  C  CB    . THR A 1 555 ? 156.537 144.993 81.679  1.00 39.23 ?  555 THR A CB    1 
ATOM   4456  O  OG1   . THR A 1 555 ? 156.723 144.760 80.277  1.00 47.13 ?  555 THR A OG1   1 
ATOM   4457  C  CG2   . THR A 1 555 ? 156.743 143.689 82.435  1.00 38.19 ?  555 THR A CG2   1 
ATOM   4458  N  N     . GLU A 1 556 ? 154.914 147.545 80.552  1.00 39.45 ?  556 GLU A N     1 
ATOM   4459  C  CA    . GLU A 1 556 ? 154.819 148.987 80.341  1.00 41.11 ?  556 GLU A CA    1 
ATOM   4460  C  C     . GLU A 1 556 ? 153.585 149.565 81.022  1.00 41.76 ?  556 GLU A C     1 
ATOM   4461  O  O     . GLU A 1 556 ? 153.644 150.644 81.626  1.00 44.03 ?  556 GLU A O     1 
ATOM   4462  C  CB    . GLU A 1 556 ? 154.801 149.294 78.843  1.00 41.87 ?  556 GLU A CB    1 
ATOM   4463  C  CG    . GLU A 1 556 ? 156.017 148.804 78.049  1.00 45.29 ?  556 GLU A CG    1 
ATOM   4464  C  CD    . GLU A 1 556 ? 157.336 148.862 78.817  1.00 49.26 ?  556 GLU A CD    1 
ATOM   4465  O  OE1   . GLU A 1 556 ? 158.160 147.939 78.645  1.00 49.26 ?  556 GLU A OE1   1 
ATOM   4466  O  OE2   . GLU A 1 556 ? 157.580 149.850 79.541  1.00 43.00 -1 556 GLU A OE2   1 
ATOM   4467  N  N     . ASP A 1 557 ? 152.454 148.862 80.928  1.00 42.48 ?  557 ASP A N     1 
ATOM   4468  C  CA    . ASP A 1 557 ? 151.246 149.316 81.608  1.00 39.88 ?  557 ASP A CA    1 
ATOM   4469  C  C     . ASP A 1 557 ? 151.447 149.339 83.116  1.00 37.08 ?  557 ASP A C     1 
ATOM   4470  O  O     . ASP A 1 557 ? 150.989 150.263 83.798  1.00 37.78 ?  557 ASP A O     1 
ATOM   4471  C  CB    . ASP A 1 557 ? 150.068 148.416 81.238  1.00 37.18 ?  557 ASP A CB    1 
ATOM   4472  C  CG    . ASP A 1 557 ? 149.318 148.915 80.025  1.00 43.58 ?  557 ASP A CG    1 
ATOM   4473  O  OD1   . ASP A 1 557 ? 149.019 150.126 79.965  1.00 45.62 ?  557 ASP A OD1   1 
ATOM   4474  O  OD2   . ASP A 1 557 ? 149.026 148.096 79.128  1.00 43.98 -1 557 ASP A OD2   1 
ATOM   4475  N  N     . TRP A 1 558 ? 152.138 148.334 83.653  1.00 30.18 ?  558 TRP A N     1 
ATOM   4476  C  CA    . TRP A 1 558 ? 152.406 148.312 85.085  1.00 27.84 ?  558 TRP A CA    1 
ATOM   4477  C  C     . TRP A 1 558 ? 153.377 149.411 85.497  1.00 34.90 ?  558 TRP A C     1 
ATOM   4478  O  O     . TRP A 1 558 ? 153.248 149.960 86.593  1.00 35.93 ?  558 TRP A O     1 
ATOM   4479  C  CB    . TRP A 1 558 ? 152.938 146.943 85.499  1.00 30.23 ?  558 TRP A CB    1 
ATOM   4480  C  CG    . TRP A 1 558 ? 151.861 145.976 85.880  1.00 29.42 ?  558 TRP A CG    1 
ATOM   4481  C  CD1   . TRP A 1 558 ? 151.415 144.914 85.151  1.00 28.16 ?  558 TRP A CD1   1 
ATOM   4482  C  CD2   . TRP A 1 558 ? 151.087 145.988 87.085  1.00 28.54 ?  558 TRP A CD2   1 
ATOM   4483  N  NE1   . TRP A 1 558 ? 150.418 144.259 85.829  1.00 30.68 ?  558 TRP A NE1   1 
ATOM   4484  C  CE2   . TRP A 1 558 ? 150.198 144.898 87.020  1.00 29.91 ?  558 TRP A CE2   1 
ATOM   4485  C  CE3   . TRP A 1 558 ? 151.065 146.809 88.216  1.00 32.95 ?  558 TRP A CE3   1 
ATOM   4486  C  CZ2   . TRP A 1 558 ? 149.297 144.610 88.041  1.00 24.29 ?  558 TRP A CZ2   1 
ATOM   4487  C  CZ3   . TRP A 1 558 ? 150.168 146.521 89.226  1.00 27.71 ?  558 TRP A CZ3   1 
ATOM   4488  C  CH2   . TRP A 1 558 ? 149.297 145.433 89.133  1.00 19.86 ?  558 TRP A CH2   1 
ATOM   4489  N  N     . LYS A 1 559 ? 154.348 149.750 84.645  1.00 40.62 ?  559 LYS A N     1 
ATOM   4490  C  CA    . LYS A 1 559 ? 155.222 150.884 84.936  1.00 35.82 ?  559 LYS A CA    1 
ATOM   4491  C  C     . LYS A 1 559 ? 154.438 152.190 84.960  1.00 36.87 ?  559 LYS A C     1 
ATOM   4492  O  O     . LYS A 1 559 ? 154.651 153.040 85.835  1.00 40.72 ?  559 LYS A O     1 
ATOM   4493  C  CB    . LYS A 1 559 ? 156.351 150.961 83.909  1.00 38.77 ?  559 LYS A CB    1 
ATOM   4494  C  CG    . LYS A 1 559 ? 157.359 149.832 83.993  1.00 38.52 ?  559 LYS A CG    1 
ATOM   4495  C  CD    . LYS A 1 559 ? 158.215 149.771 82.740  1.00 41.10 ?  559 LYS A CD    1 
ATOM   4496  C  CE    . LYS A 1 559 ? 159.282 148.695 82.847  1.00 40.35 ?  559 LYS A CE    1 
ATOM   4497  N  NZ    . LYS A 1 559 ? 160.024 148.768 84.135  1.00 43.81 1  559 LYS A NZ    1 
ATOM   4498  N  N     . LYS A 1 560 ? 153.528 152.367 83.999  1.00 36.29 ?  560 LYS A N     1 
ATOM   4499  C  CA    . LYS A 1 560 ? 152.687 153.559 83.992  1.00 33.56 ?  560 LYS A CA    1 
ATOM   4500  C  C     . LYS A 1 560 ? 151.809 153.619 85.236  1.00 36.41 ?  560 LYS A C     1 
ATOM   4501  O  O     . LYS A 1 560 ? 151.642 154.687 85.835  1.00 42.03 ?  560 LYS A O     1 
ATOM   4502  C  CB    . LYS A 1 560 ? 151.829 153.591 82.727  1.00 34.44 ?  560 LYS A CB    1 
ATOM   4503  C  CG    . LYS A 1 560 ? 152.616 153.828 81.450  1.00 38.39 ?  560 LYS A CG    1 
ATOM   4504  C  CD    . LYS A 1 560 ? 151.702 153.866 80.238  1.00 39.77 ?  560 LYS A CD    1 
ATOM   4505  C  CE    . LYS A 1 560 ? 152.394 153.310 79.005  1.00 40.30 ?  560 LYS A CE    1 
ATOM   4506  N  NZ    . LYS A 1 560 ? 152.052 151.881 78.771  1.00 40.83 1  560 LYS A NZ    1 
ATOM   4507  N  N     . LEU A 1 561 ? 151.244 152.480 85.641  1.00 33.41 ?  561 LEU A N     1 
ATOM   4508  C  CA    . LEU A 1 561 ? 150.433 152.443 86.855  1.00 29.59 ?  561 LEU A CA    1 
ATOM   4509  C  C     . LEU A 1 561 ? 151.273 152.732 88.092  1.00 32.43 ?  561 LEU A C     1 
ATOM   4510  O  O     . LEU A 1 561 ? 150.803 153.387 89.027  1.00 36.45 ?  561 LEU A O     1 
ATOM   4511  C  CB    . LEU A 1 561 ? 149.737 151.089 86.987  1.00 31.12 ?  561 LEU A CB    1 
ATOM   4512  C  CG    . LEU A 1 561 ? 148.911 150.920 88.263  1.00 31.43 ?  561 LEU A CG    1 
ATOM   4513  C  CD1   . LEU A 1 561 ? 147.808 151.961 88.318  1.00 27.55 ?  561 LEU A CD1   1 
ATOM   4514  C  CD2   . LEU A 1 561 ? 148.335 149.524 88.367  1.00 28.89 ?  561 LEU A CD2   1 
ATOM   4515  N  N     . LYS A 1 562 ? 152.510 152.235 88.127  1.00 34.56 ?  562 LYS A N     1 
ATOM   4516  C  CA    . LYS A 1 562 ? 153.398 152.520 89.247  1.00 33.38 ?  562 LYS A CA    1 
ATOM   4517  C  C     . LYS A 1 562 ? 153.699 154.009 89.342  1.00 34.22 ?  562 LYS A C     1 
ATOM   4518  O  O     . LYS A 1 562 ? 153.687 154.582 90.437  1.00 38.77 ?  562 LYS A O     1 
ATOM   4519  C  CB    . LYS A 1 562 ? 154.690 151.715 89.101  1.00 35.62 ?  562 LYS A CB    1 
ATOM   4520  C  CG    . LYS A 1 562 ? 155.794 152.115 90.059  1.00 31.08 ?  562 LYS A CG    1 
ATOM   4521  C  CD    . LYS A 1 562 ? 157.082 151.379 89.741  1.00 28.64 ?  562 LYS A CD    1 
ATOM   4522  C  CE    . LYS A 1 562 ? 158.209 151.810 90.662  1.00 34.47 ?  562 LYS A CE    1 
ATOM   4523  N  NZ    . LYS A 1 562 ? 159.277 150.777 90.742  1.00 41.45 1  562 LYS A NZ    1 
ATOM   4524  N  N     . ALA A 1 563 ? 153.964 154.652 88.203  1.00 32.24 ?  563 ALA A N     1 
ATOM   4525  C  CA    . ALA A 1 563 ? 154.170 156.098 88.205  1.00 33.14 ?  563 ALA A CA    1 
ATOM   4526  C  C     . ALA A 1 563 ? 152.911 156.834 88.654  1.00 36.18 ?  563 ALA A C     1 
ATOM   4527  O  O     . ALA A 1 563 ? 152.984 157.796 89.428  1.00 42.44 ?  563 ALA A O     1 
ATOM   4528  C  CB    . ALA A 1 563 ? 154.604 156.567 86.818  1.00 35.79 ?  563 ALA A CB    1 
ATOM   4529  N  N     . PHE A 1 564 ? 151.746 156.385 88.179  1.00 34.18 ?  564 PHE A N     1 
ATOM   4530  C  CA    . PHE A 1 564 ? 150.483 157.004 88.568  1.00 31.53 ?  564 PHE A CA    1 
ATOM   4531  C  C     . PHE A 1 564 ? 150.254 156.895 90.072  1.00 35.60 ?  564 PHE A C     1 
ATOM   4532  O  O     . PHE A 1 564 ? 149.805 157.852 90.711  1.00 38.50 ?  564 PHE A O     1 
ATOM   4533  C  CB    . PHE A 1 564 ? 149.337 156.349 87.797  1.00 32.91 ?  564 PHE A CB    1 
ATOM   4534  C  CG    . PHE A 1 564 ? 148.050 157.116 87.840  1.00 33.21 ?  564 PHE A CG    1 
ATOM   4535  C  CD1   . PHE A 1 564 ? 147.770 158.081 86.888  1.00 35.68 ?  564 PHE A CD1   1 
ATOM   4536  C  CD2   . PHE A 1 564 ? 147.110 156.861 88.823  1.00 34.31 ?  564 PHE A CD2   1 
ATOM   4537  C  CE1   . PHE A 1 564 ? 146.582 158.783 86.923  1.00 39.13 ?  564 PHE A CE1   1 
ATOM   4538  C  CE2   . PHE A 1 564 ? 145.922 157.560 88.864  1.00 35.63 ?  564 PHE A CE2   1 
ATOM   4539  C  CZ    . PHE A 1 564 ? 145.656 158.522 87.912  1.00 38.90 ?  564 PHE A CZ    1 
ATOM   4540  N  N     . VAL A 1 565 ? 150.555 155.732 90.651  1.00 35.82 ?  565 VAL A N     1 
ATOM   4541  C  CA    . VAL A 1 565 ? 150.386 155.537 92.086  1.00 29.96 ?  565 VAL A CA    1 
ATOM   4542  C  C     . VAL A 1 565 ? 151.388 156.379 92.863  1.00 33.54 ?  565 VAL A C     1 
ATOM   4543  O  O     . VAL A 1 565 ? 151.050 156.979 93.890  1.00 36.12 ?  565 VAL A O     1 
ATOM   4544  C  CB    . VAL A 1 565 ? 150.509 154.041 92.431  1.00 29.53 ?  565 VAL A CB    1 
ATOM   4545  C  CG1   . VAL A 1 565 ? 150.708 153.844 93.923  1.00 28.69 ?  565 VAL A CG1   1 
ATOM   4546  C  CG2   . VAL A 1 565 ? 149.280 153.298 91.956  1.00 33.70 ?  565 VAL A CG2   1 
ATOM   4547  N  N     . ALA A 1 566 ? 152.633 156.444 92.389  1.00 36.68 ?  566 ALA A N     1 
ATOM   4548  C  CA    . ALA A 1 566 ? 153.640 157.246 93.071  1.00 36.24 ?  566 ALA A CA    1 
ATOM   4549  C  C     . ALA A 1 566 ? 153.297 158.727 93.037  1.00 38.26 ?  566 ALA A C     1 
ATOM   4550  O  O     . ALA A 1 566 ? 153.652 159.466 93.962  1.00 42.85 ?  566 ALA A O     1 
ATOM   4551  C  CB    . ALA A 1 566 ? 155.013 157.004 92.447  1.00 36.68 ?  566 ALA A CB    1 
ATOM   4552  N  N     . GLU A 1 567 ? 152.612 159.179 91.989  1.00 40.84 ?  567 GLU A N     1 
ATOM   4553  C  CA    . GLU A 1 567 ? 152.286 160.592 91.858  1.00 40.06 ?  567 GLU A CA    1 
ATOM   4554  C  C     . GLU A 1 567 ? 150.930 160.964 92.449  1.00 39.80 ?  567 GLU A C     1 
ATOM   4555  O  O     . GLU A 1 567 ? 150.717 162.140 92.767  1.00 43.67 ?  567 GLU A O     1 
ATOM   4556  C  CB    . GLU A 1 567 ? 152.350 160.997 90.379  1.00 42.38 ?  567 GLU A CB    1 
ATOM   4557  C  CG    . GLU A 1 567 ? 152.385 162.491 90.124  1.00 43.90 ?  567 GLU A CG    1 
ATOM   4558  C  CD    . GLU A 1 567 ? 151.105 162.995 89.497  1.00 47.55 ?  567 GLU A CD    1 
ATOM   4559  O  OE1   . GLU A 1 567 ? 150.445 162.201 88.796  1.00 46.07 ?  567 GLU A OE1   1 
ATOM   4560  O  OE2   . GLU A 1 567 ? 150.761 164.178 89.702  1.00 47.17 -1 567 GLU A OE2   1 
ATOM   4561  N  N     . HIS A 1 568 ? 150.016 160.005 92.619  1.00 39.70 ?  568 HIS A N     1 
ATOM   4562  C  CA    . HIS A 1 568 ? 148.704 160.275 93.192  1.00 38.76 ?  568 HIS A CA    1 
ATOM   4563  C  C     . HIS A 1 568 ? 148.391 159.514 94.472  1.00 35.94 ?  568 HIS A C     1 
ATOM   4564  O  O     . HIS A 1 568 ? 147.486 159.931 95.202  1.00 40.11 ?  568 HIS A O     1 
ATOM   4565  C  CB    . HIS A 1 568 ? 147.594 159.969 92.174  1.00 37.02 ?  568 HIS A CB    1 
ATOM   4566  C  CG    . HIS A 1 568 ? 147.525 160.942 91.040  1.00 38.46 ?  568 HIS A CG    1 
ATOM   4567  N  ND1   . HIS A 1 568 ? 146.845 160.677 89.872  1.00 42.97 ?  568 HIS A ND1   1 
ATOM   4568  C  CD2   . HIS A 1 568 ? 148.056 162.177 90.895  1.00 38.74 ?  568 HIS A CD2   1 
ATOM   4569  C  CE1   . HIS A 1 568 ? 146.966 161.707 89.053  1.00 42.21 ?  568 HIS A CE1   1 
ATOM   4570  N  NE2   . HIS A 1 568 ? 147.691 162.634 89.653  1.00 41.84 ?  568 HIS A NE2   1 
ATOM   4571  N  N     . GLY A 1 569 ? 149.091 158.424 94.765  1.00 29.47 ?  569 GLY A N     1 
ATOM   4572  C  CA    . GLY A 1 569 ? 148.815 157.667 95.968  1.00 29.61 ?  569 GLY A CA    1 
ATOM   4573  C  C     . GLY A 1 569 ? 147.703 156.653 95.788  1.00 28.19 ?  569 GLY A C     1 
ATOM   4574  O  O     . GLY A 1 569 ? 147.108 156.504 94.722  1.00 33.66 ?  569 GLY A O     1 
ATOM   4575  N  N     . MET A 1 570 ? 147.421 155.938 96.874  1.00 24.21 ?  570 MET A N     1 
ATOM   4576  C  CA    . MET A 1 570 ? 146.394 154.907 96.904  1.00 22.67 ?  570 MET A CA    1 
ATOM   4577  C  C     . MET A 1 570 ? 145.373 155.232 97.982  1.00 24.38 ?  570 MET A C     1 
ATOM   4578  O  O     . MET A 1 570 ? 145.734 155.656 99.083  1.00 31.69 ?  570 MET A O     1 
ATOM   4579  C  CB    . MET A 1 570 ? 147.003 153.525 97.166  1.00 26.83 ?  570 MET A CB    1 
ATOM   4580  C  CG    . MET A 1 570 ? 147.904 153.024 96.056  1.00 24.76 ?  570 MET A CG    1 
ATOM   4581  S  SD    . MET A 1 570 ? 147.055 151.890 94.951  1.00 38.07 ?  570 MET A SD    1 
ATOM   4582  C  CE    . MET A 1 570 ? 146.899 150.465 96.017  1.00 24.88 ?  570 MET A CE    1 
ATOM   4583  N  N     . TYR A 1 571 ? 144.096 155.027 97.663  1.00 15.53 ?  571 TYR A N     1 
ATOM   4584  C  CA    . TYR A 1 571 ? 143.038 155.338 98.615  1.00 9.58  ?  571 TYR A CA    1 
ATOM   4585  C  C     . TYR A 1 571 ? 142.814 154.215 99.618  1.00 18.52 ?  571 TYR A C     1 
ATOM   4586  O  O     . TYR A 1 571 ? 142.467 154.485 100.773 1.00 20.21 ?  571 TYR A O     1 
ATOM   4587  C  CB    . TYR A 1 571 ? 141.737 155.636 97.872  1.00 20.46 ?  571 TYR A CB    1 
ATOM   4588  C  CG    . TYR A 1 571 ? 140.674 156.260 98.740  1.00 24.83 ?  571 TYR A CG    1 
ATOM   4589  C  CD1   . TYR A 1 571 ? 140.744 157.597 99.100  1.00 23.83 ?  571 TYR A CD1   1 
ATOM   4590  C  CD2   . TYR A 1 571 ? 139.601 155.512 99.203  1.00 19.14 ?  571 TYR A CD2   1 
ATOM   4591  C  CE1   . TYR A 1 571 ? 139.778 158.171 99.893  1.00 26.06 ?  571 TYR A CE1   1 
ATOM   4592  C  CE2   . TYR A 1 571 ? 138.631 156.079 99.998  1.00 20.62 ?  571 TYR A CE2   1 
ATOM   4593  C  CZ    . TYR A 1 571 ? 138.722 157.409 100.339 1.00 28.45 ?  571 TYR A CZ    1 
ATOM   4594  O  OH    . TYR A 1 571 ? 137.755 157.979 101.131 1.00 27.40 ?  571 TYR A OH    1 
ATOM   4595  N  N     . HIS A 1 572 ? 142.998 152.965 99.207  1.00 23.11 ?  572 HIS A N     1 
ATOM   4596  C  CA    . HIS A 1 572 ? 142.758 151.810 100.058 1.00 14.41 ?  572 HIS A CA    1 
ATOM   4597  C  C     . HIS A 1 572 ? 144.082 151.169 100.439 1.00 13.07 ?  572 HIS A C     1 
ATOM   4598  O  O     . HIS A 1 572 ? 144.916 150.897 99.571  1.00 26.25 ?  572 HIS A O     1 
ATOM   4599  C  CB    . HIS A 1 572 ? 141.864 150.784 99.357  1.00 14.72 ?  572 HIS A CB    1 
ATOM   4600  C  CG    . HIS A 1 572 ? 140.697 151.386 98.642  1.00 9.11  ?  572 HIS A CG    1 
ATOM   4601  N  ND1   . HIS A 1 572 ? 140.735 151.722 97.307  1.00 18.58 ?  572 HIS A ND1   1 
ATOM   4602  C  CD2   . HIS A 1 572 ? 139.457 151.708 99.075  1.00 15.19 ?  572 HIS A CD2   1 
ATOM   4603  C  CE1   . HIS A 1 572 ? 139.571 152.229 96.949  1.00 19.44 ?  572 HIS A CE1   1 
ATOM   4604  N  NE2   . HIS A 1 572 ? 138.775 152.230 98.003  1.00 24.26 ?  572 HIS A NE2   1 
ATOM   4605  N  N     . SER A 1 573 ? 144.272 150.934 101.739 1.00 8.03  ?  573 SER A N     1 
ATOM   4606  C  CA    . SER A 1 573 ? 145.449 150.200 102.187 1.00 8.56  ?  573 SER A CA    1 
ATOM   4607  C  C     . SER A 1 573 ? 145.420 148.767 101.677 1.00 15.34 ?  573 SER A C     1 
ATOM   4608  O  O     . SER A 1 573 ? 146.454 148.220 101.275 1.00 24.43 ?  573 SER A O     1 
ATOM   4609  C  CB    . SER A 1 573 ? 145.537 150.229 103.712 1.00 12.75 ?  573 SER A CB    1 
ATOM   4610  O  OG    . SER A 1 573 ? 144.287 149.916 104.295 1.00 21.38 ?  573 SER A OG    1 
ATOM   4611  N  N     . TYR A 1 574 ? 144.243 148.147 101.682 1.00 16.85 ?  574 TYR A N     1 
ATOM   4612  C  CA    . TYR A 1 574 ? 144.046 146.799 101.177 1.00 5.31  ?  574 TYR A CA    1 
ATOM   4613  C  C     . TYR A 1 574 ? 142.834 146.799 100.261 1.00 9.09  ?  574 TYR A C     1 
ATOM   4614  O  O     . TYR A 1 574 ? 141.859 147.513 100.514 1.00 13.59 ?  574 TYR A O     1 
ATOM   4615  C  CB    . TYR A 1 574 ? 143.857 145.804 102.325 1.00 12.98 ?  574 TYR A CB    1 
ATOM   4616  C  CG    . TYR A 1 574 ? 144.963 145.871 103.349 1.00 7.77  ?  574 TYR A CG    1 
ATOM   4617  C  CD1   . TYR A 1 574 ? 144.913 146.785 104.390 1.00 6.39  ?  574 TYR A CD1   1 
ATOM   4618  C  CD2   . TYR A 1 574 ? 146.063 145.032 103.268 1.00 10.01 ?  574 TYR A CD2   1 
ATOM   4619  C  CE1   . TYR A 1 574 ? 145.919 146.862 105.321 1.00 9.56  ?  574 TYR A CE1   1 
ATOM   4620  C  CE2   . TYR A 1 574 ? 147.075 145.100 104.199 1.00 17.92 ?  574 TYR A CE2   1 
ATOM   4621  C  CZ    . TYR A 1 574 ? 146.996 146.018 105.224 1.00 8.20  ?  574 TYR A CZ    1 
ATOM   4622  O  OH    . TYR A 1 574 ? 147.997 146.095 106.159 1.00 14.62 ?  574 TYR A OH    1 
ATOM   4623  N  N     . ARG A 1 575 ? 142.899 146.016 99.200  1.00 16.15 ?  575 ARG A N     1 
ATOM   4624  C  CA    . ARG A 1 575 ? 141.828 146.047 98.212  1.00 7.89  ?  575 ARG A CA    1 
ATOM   4625  C  C     . ARG A 1 575 ? 141.212 144.686 97.938  1.00 12.24 ?  575 ARG A C     1 
ATOM   4626  O  O     . ARG A 1 575 ? 139.996 144.594 97.765  1.00 20.45 ?  575 ARG A O     1 
ATOM   4627  C  CB    . ARG A 1 575 ? 142.345 146.641 96.897  1.00 15.51 ?  575 ARG A CB    1 
ATOM   4628  C  CG    . ARG A 1 575 ? 142.887 148.050 97.015  1.00 6.14  ?  575 ARG A CG    1 
ATOM   4629  C  CD    . ARG A 1 575 ? 143.925 148.307 95.942  1.00 12.48 ?  575 ARG A CD    1 
ATOM   4630  N  NE    . ARG A 1 575 ? 145.172 147.606 96.222  1.00 22.24 ?  575 ARG A NE    1 
ATOM   4631  C  CZ    . ARG A 1 575 ? 145.583 146.521 95.583  1.00 14.81 ?  575 ARG A CZ    1 
ATOM   4632  N  NH1   . ARG A 1 575 ? 144.870 145.981 94.610  1.00 16.91 1  575 ARG A NH1   1 
ATOM   4633  N  NH2   . ARG A 1 575 ? 146.737 145.961 95.931  1.00 10.77 ?  575 ARG A NH2   1 
ATOM   4634  N  N     . LEU A 1 576 ? 142.015 143.628 97.891  1.00 20.61 ?  576 LEU A N     1 
ATOM   4635  C  CA    . LEU A 1 576 ? 141.569 142.324 97.424  1.00 8.99  ?  576 LEU A CA    1 
ATOM   4636  C  C     . LEU A 1 576 ? 141.691 141.298 98.538  1.00 6.92  ?  576 LEU A C     1 
ATOM   4637  O  O     . LEU A 1 576 ? 142.762 141.146 99.132  1.00 16.05 ?  576 LEU A O     1 
ATOM   4638  C  CB    . LEU A 1 576 ? 142.385 141.874 96.210  1.00 4.75  ?  576 LEU A CB    1 
ATOM   4639  C  CG    . LEU A 1 576 ? 142.471 142.856 95.042  1.00 10.05 ?  576 LEU A CG    1 
ATOM   4640  C  CD1   . LEU A 1 576 ? 143.423 142.340 93.981  1.00 12.27 ?  576 LEU A CD1   1 
ATOM   4641  C  CD2   . LEU A 1 576 ? 141.099 143.106 94.451  1.00 10.86 ?  576 LEU A CD2   1 
ATOM   4642  N  N     . CYS A 1 577 ? 140.594 140.602 98.816  1.00 5.06  ?  577 CYS A N     1 
ATOM   4643  C  CA    . CYS A 1 577 ? 140.602 139.442 99.695  1.00 3.41  ?  577 CYS A CA    1 
ATOM   4644  C  C     . CYS A 1 577 ? 139.529 138.487 99.200  1.00 17.51 ?  577 CYS A C     1 
ATOM   4645  O  O     . CYS A 1 577 ? 138.416 138.914 98.888  1.00 21.24 ?  577 CYS A O     1 
ATOM   4646  C  CB    . CYS A 1 577 ? 140.368 139.836 101.161 1.00 3.50  ?  577 CYS A CB    1 
ATOM   4647  S  SG    . CYS A 1 577 ? 138.654 140.089 101.674 1.00 32.82 ?  577 CYS A SG    1 
ATOM   4648  N  N     . ILE A 1 578 ? 139.870 137.206 99.107  1.00 15.25 ?  578 ILE A N     1 
ATOM   4649  C  CA    . ILE A 1 578 ? 138.976 136.197 98.554  1.00 10.66 ?  578 ILE A CA    1 
ATOM   4650  C  C     . ILE A 1 578 ? 138.327 135.469 99.725  1.00 4.01  ?  578 ILE A C     1 
ATOM   4651  O  O     . ILE A 1 578 ? 138.934 134.598 100.353 1.00 14.86 ?  578 ILE A O     1 
ATOM   4652  C  CB    . ILE A 1 578 ? 139.712 135.241 97.613  1.00 10.51 ?  578 ILE A CB    1 
ATOM   4653  C  CG1   . ILE A 1 578 ? 140.352 136.030 96.471  1.00 0.00  ?  578 ILE A CG1   1 
ATOM   4654  C  CG2   . ILE A 1 578 ? 138.754 134.213 97.049  1.00 13.45 ?  578 ILE A CG2   1 
ATOM   4655  C  CD1   . ILE A 1 578 ? 140.985 135.171 95.420  1.00 6.95  ?  578 ILE A CD1   1 
ATOM   4656  N  N     . ALA A 1 579 ? 137.083 135.835 100.013 1.00 17.63 ?  579 ALA A N     1 
ATOM   4657  C  CA    . ALA A 1 579 ? 136.306 135.265 101.101 1.00 12.12 ?  579 ALA A CA    1 
ATOM   4658  C  C     . ALA A 1 579 ? 135.653 133.958 100.664 1.00 21.37 ?  579 ALA A C     1 
ATOM   4659  O  O     . ALA A 1 579 ? 135.631 133.626 99.478  1.00 27.27 ?  579 ALA A O     1 
ATOM   4660  C  CB    . ALA A 1 579 ? 135.260 136.279 101.557 1.00 9.65  ?  579 ALA A CB    1 
ATOM   4661  N  N     . PRO A 1 580 ? 135.135 133.169 101.612 1.00 26.58 ?  580 PRO A N     1 
ATOM   4662  C  CA    . PRO A 1 580 ? 134.447 131.924 101.226 1.00 22.98 ?  580 PRO A CA    1 
ATOM   4663  C  C     . PRO A 1 580 ? 133.234 132.126 100.329 1.00 25.85 ?  580 PRO A C     1 
ATOM   4664  O  O     . PRO A 1 580 ? 132.971 131.267 99.479  1.00 33.51 ?  580 PRO A O     1 
ATOM   4665  C  CB    . PRO A 1 580 ? 134.051 131.306 102.577 1.00 23.37 ?  580 PRO A CB    1 
ATOM   4666  C  CG    . PRO A 1 580 ? 134.303 132.359 103.605 1.00 24.80 ?  580 PRO A CG    1 
ATOM   4667  C  CD    . PRO A 1 580 ? 135.375 133.227 103.063 1.00 21.17 ?  580 PRO A CD    1 
ATOM   4668  N  N     . THR A 1 581 ? 132.496 133.226 100.482 1.00 22.49 ?  581 THR A N     1 
ATOM   4669  C  CA    . THR A 1 581 ? 131.292 133.512 99.690  1.00 33.36 ?  581 THR A CA    1 
ATOM   4670  C  C     . THR A 1 581 ? 130.308 132.339 99.738  1.00 31.70 ?  581 THR A C     1 
ATOM   4671  O  O     . THR A 1 581 ? 130.011 131.690 98.737  1.00 32.03 ?  581 THR A O     1 
ATOM   4672  C  CB    . THR A 1 581 ? 131.637 133.864 98.238  1.00 32.67 ?  581 THR A CB    1 
ATOM   4673  O  OG1   . THR A 1 581 ? 131.696 132.666 97.452  1.00 26.83 ?  581 THR A OG1   1 
ATOM   4674  C  CG2   . THR A 1 581 ? 132.958 134.605 98.147  1.00 30.85 ?  581 THR A CG2   1 
ATOM   4675  N  N     . GLY A 1 582 ? 129.809 132.090 100.946 1.00 35.50 ?  582 GLY A N     1 
ATOM   4676  C  CA    . GLY A 1 582 ? 129.017 130.904 101.206 1.00 32.59 ?  582 GLY A CA    1 
ATOM   4677  C  C     . GLY A 1 582 ? 127.676 130.821 100.504 1.00 35.28 ?  582 GLY A C     1 
ATOM   4678  O  O     . GLY A 1 582 ? 127.485 129.962 99.638  1.00 37.33 ?  582 GLY A O     1 
ATOM   4679  N  N     . SER A 1 583 ? 126.738 131.702 100.853 1.00 37.73 ?  583 SER A N     1 
ATOM   4680  C  CA    . SER A 1 583 ? 125.369 131.572 100.369 1.00 38.50 ?  583 SER A CA    1 
ATOM   4681  C  C     . SER A 1 583 ? 125.078 132.399 99.125  1.00 36.64 ?  583 SER A C     1 
ATOM   4682  O  O     . SER A 1 583 ? 124.130 132.083 98.400  1.00 38.67 ?  583 SER A O     1 
ATOM   4683  C  CB    . SER A 1 583 ? 124.380 131.963 101.472 1.00 42.09 ?  583 SER A CB    1 
ATOM   4684  O  OG    . SER A 1 583 ? 123.101 131.404 101.229 1.00 39.94 ?  583 SER A OG    1 
ATOM   4685  N  N     . ILE A 1 584 ? 125.860 133.449 98.859  1.00 33.14 ?  584 ILE A N     1 
ATOM   4686  C  CA    . ILE A 1 584 ? 125.643 134.234 97.651  1.00 31.28 ?  584 ILE A CA    1 
ATOM   4687  C  C     . ILE A 1 584 ? 126.072 133.476 96.404  1.00 33.16 ?  584 ILE A C     1 
ATOM   4688  O  O     . ILE A 1 584 ? 125.739 133.887 95.287  1.00 40.10 ?  584 ILE A O     1 
ATOM   4689  C  CB    . ILE A 1 584 ? 126.376 135.585 97.739  1.00 34.85 ?  584 ILE A CB    1 
ATOM   4690  C  CG1   . ILE A 1 584 ? 127.846 135.374 98.110  1.00 34.66 ?  584 ILE A CG1   1 
ATOM   4691  C  CG2   . ILE A 1 584 ? 125.686 136.505 98.732  1.00 33.01 ?  584 ILE A CG2   1 
ATOM   4692  C  CD1   . ILE A 1 584 ? 128.671 136.641 98.084  1.00 33.24 ?  584 ILE A CD1   1 
ATOM   4693  N  N     . SER A 1 585 ? 126.812 132.376 96.564  1.00 32.18 ?  585 SER A N     1 
ATOM   4694  C  CA    . SER A 1 585 ? 127.214 131.579 95.411  1.00 29.46 ?  585 SER A CA    1 
ATOM   4695  C  C     . SER A 1 585 ? 126.021 130.890 94.763  1.00 31.36 ?  585 SER A C     1 
ATOM   4696  O  O     . SER A 1 585 ? 126.001 130.713 93.541  1.00 33.66 ?  585 SER A O     1 
ATOM   4697  C  CB    . SER A 1 585 ? 128.265 130.553 95.827  1.00 29.82 ?  585 SER A CB    1 
ATOM   4698  O  OG    . SER A 1 585 ? 127.820 129.786 96.931  1.00 35.57 ?  585 SER A OG    1 
ATOM   4699  N  N     . TYR A 1 586 ? 125.030 130.485 95.560  1.00 31.83 ?  586 TYR A N     1 
ATOM   4700  C  CA    . TYR A 1 586 ? 123.811 129.920 94.992  1.00 33.16 ?  586 TYR A CA    1 
ATOM   4701  C  C     . TYR A 1 586 ? 123.058 130.960 94.175  1.00 32.37 ?  586 TYR A C     1 
ATOM   4702  O  O     . TYR A 1 586 ? 122.651 130.695 93.039  1.00 39.34 ?  586 TYR A O     1 
ATOM   4703  C  CB    . TYR A 1 586 ? 122.915 129.374 96.102  1.00 33.29 ?  586 TYR A CB    1 
ATOM   4704  C  CG    . TYR A 1 586 ? 123.518 128.243 96.897  1.00 34.35 ?  586 TYR A CG    1 
ATOM   4705  C  CD1   . TYR A 1 586 ? 123.451 126.936 96.438  1.00 35.32 ?  586 TYR A CD1   1 
ATOM   4706  C  CD2   . TYR A 1 586 ? 124.141 128.480 98.113  1.00 31.34 ?  586 TYR A CD2   1 
ATOM   4707  C  CE1   . TYR A 1 586 ? 123.996 125.899 97.164  1.00 36.39 ?  586 TYR A CE1   1 
ATOM   4708  C  CE2   . TYR A 1 586 ? 124.688 127.450 98.846  1.00 33.62 ?  586 TYR A CE2   1 
ATOM   4709  C  CZ    . TYR A 1 586 ? 124.614 126.161 98.366  1.00 37.41 ?  586 TYR A CZ    1 
ATOM   4710  O  OH    . TYR A 1 586 ? 125.159 125.131 99.095  1.00 40.64 ?  586 TYR A OH    1 
ATOM   4711  N  N     . VAL A 1 587 ? 122.878 132.157 94.739  1.00 29.24 ?  587 VAL A N     1 
ATOM   4712  C  CA    . VAL A 1 587 ? 122.126 133.212 94.066  1.00 27.25 ?  587 VAL A CA    1 
ATOM   4713  C  C     . VAL A 1 587 ? 122.784 133.575 92.742  1.00 30.87 ?  587 VAL A C     1 
ATOM   4714  O  O     . VAL A 1 587 ? 122.106 133.765 91.725  1.00 33.39 ?  587 VAL A O     1 
ATOM   4715  C  CB    . VAL A 1 587 ? 121.995 134.437 94.990  1.00 29.69 ?  587 VAL A CB    1 
ATOM   4716  C  CG1   . VAL A 1 587 ? 121.399 135.614 94.241  1.00 30.93 ?  587 VAL A CG1   1 
ATOM   4717  C  CG2   . VAL A 1 587 ? 121.159 134.092 96.208  1.00 31.47 ?  587 VAL A CG2   1 
ATOM   4718  N  N     . GLN A 1 588 ? 124.109 133.669 92.732  1.00 32.92 ?  588 GLN A N     1 
ATOM   4719  C  CA    . GLN A 1 588 ? 124.849 133.992 91.522  1.00 29.21 ?  588 GLN A CA    1 
ATOM   4720  C  C     . GLN A 1 588 ? 125.051 132.789 90.614  1.00 28.76 ?  588 GLN A C     1 
ATOM   4721  O  O     . GLN A 1 588 ? 125.620 132.947 89.530  1.00 31.83 ?  588 GLN A O     1 
ATOM   4722  C  CB    . GLN A 1 588 ? 126.209 134.592 91.884  1.00 26.58 ?  588 GLN A CB    1 
ATOM   4723  C  CG    . GLN A 1 588 ? 126.139 136.006 92.419  1.00 24.83 ?  588 GLN A CG    1 
ATOM   4724  C  CD    . GLN A 1 588 ? 126.371 137.041 91.343  1.00 27.77 ?  588 GLN A CD    1 
ATOM   4725  O  OE1   . GLN A 1 588 ? 127.220 136.866 90.473  1.00 29.67 ?  588 GLN A OE1   1 
ATOM   4726  N  NE2   . GLN A 1 588 ? 125.619 138.132 91.399  1.00 29.68 ?  588 GLN A NE2   1 
ATOM   4727  N  N     . SER A 1 589 ? 124.597 131.608 91.030  1.00 32.59 ?  589 SER A N     1 
ATOM   4728  C  CA    . SER A 1 589 ? 124.801 130.364 90.292  1.00 29.72 ?  589 SER A CA    1 
ATOM   4729  C  C     . SER A 1 589 ? 126.284 130.174 89.981  1.00 32.19 ?  589 SER A C     1 
ATOM   4730  O  O     . SER A 1 589 ? 126.709 130.085 88.828  1.00 30.48 ?  589 SER A O     1 
ATOM   4731  C  CB    . SER A 1 589 ? 123.951 130.332 89.021  1.00 30.42 ?  589 SER A CB    1 
ATOM   4732  O  OG    . SER A 1 589 ? 123.607 129.001 88.677  1.00 40.48 ?  589 SER A OG    1 
ATOM   4733  N  N     . SER A 1 590 ? 127.072 130.127 91.050  1.00 33.30 ?  590 SER A N     1 
ATOM   4734  C  CA    . SER A 1 590 ? 128.519 130.105 90.947  1.00 26.43 ?  590 SER A CA    1 
ATOM   4735  C  C     . SER A 1 590 ? 129.088 129.142 91.976  1.00 27.25 ?  590 SER A C     1 
ATOM   4736  O  O     . SER A 1 590 ? 128.475 128.887 93.015  1.00 31.48 ?  590 SER A O     1 
ATOM   4737  C  CB    . SER A 1 590 ? 129.109 131.505 91.157  1.00 23.21 ?  590 SER A CB    1 
ATOM   4738  O  OG    . SER A 1 590 ? 129.522 131.686 92.496  1.00 32.45 ?  590 SER A OG    1 
ATOM   4739  N  N     . THR A 1 591 ? 130.263 128.600 91.671  1.00 27.43 ?  591 THR A N     1 
ATOM   4740  C  CA    . THR A 1 591 ? 130.984 127.803 92.651  1.00 22.38 ?  591 THR A CA    1 
ATOM   4741  C  C     . THR A 1 591 ? 131.550 128.706 93.740  1.00 27.07 ?  591 THR A C     1 
ATOM   4742  O  O     . THR A 1 591 ? 131.876 129.873 93.505  1.00 25.19 ?  591 THR A O     1 
ATOM   4743  C  CB    . THR A 1 591 ? 132.104 127.005 91.982  1.00 25.20 ?  591 THR A CB    1 
ATOM   4744  O  OG1   . THR A 1 591 ? 133.126 127.898 91.525  1.00 33.06 ?  591 THR A OG1   1 
ATOM   4745  C  CG2   . THR A 1 591 ? 131.561 126.225 90.801  1.00 25.62 ?  591 THR A CG2   1 
ATOM   4746  N  N     . ALA A 1 592 ? 131.661 128.157 94.945  1.00 26.79 ?  592 ALA A N     1 
ATOM   4747  C  CA    . ALA A 1 592 ? 132.028 128.957 96.104  1.00 24.60 ?  592 ALA A CA    1 
ATOM   4748  C  C     . ALA A 1 592 ? 133.494 129.365 96.028  1.00 28.69 ?  592 ALA A C     1 
ATOM   4749  O  O     . ALA A 1 592 ? 134.384 128.507 96.015  1.00 31.31 ?  592 ALA A O     1 
ATOM   4750  C  CB    . ALA A 1 592 ? 131.757 128.180 97.389  1.00 28.80 ?  592 ALA A CB    1 
ATOM   4751  N  N     . SER A 1 593 ? 133.736 130.671 95.975  1.00 27.10 ?  593 SER A N     1 
ATOM   4752  C  CA    . SER A 1 593 ? 135.078 131.262 96.050  1.00 11.59 ?  593 SER A CA    1 
ATOM   4753  C  C     . SER A 1 593 ? 135.924 130.728 94.892  1.00 13.13 ?  593 SER A C     1 
ATOM   4754  O  O     . SER A 1 593 ? 135.393 130.336 93.845  1.00 27.44 ?  593 SER A O     1 
ATOM   4755  C  CB    . SER A 1 593 ? 135.658 131.009 97.430  1.00 28.10 ?  593 SER A CB    1 
ATOM   4756  O  OG    . SER A 1 593 ? 136.882 131.692 97.613  1.00 29.10 ?  593 SER A OG    1 
ATOM   4757  N  N     . VAL A 1 594 ? 137.247 130.719 95.063  1.00 23.32 ?  594 VAL A N     1 
ATOM   4758  C  CA    . VAL A 1 594 ? 138.156 130.147 94.079  1.00 19.82 ?  594 VAL A CA    1 
ATOM   4759  C  C     . VAL A 1 594 ? 138.519 128.707 94.402  1.00 14.86 ?  594 VAL A C     1 
ATOM   4760  O  O     . VAL A 1 594 ? 139.350 128.112 93.707  1.00 17.59 ?  594 VAL A O     1 
ATOM   4761  C  CB    . VAL A 1 594 ? 139.429 131.007 93.945  1.00 18.67 ?  594 VAL A CB    1 
ATOM   4762  C  CG1   . VAL A 1 594 ? 139.094 132.346 93.312  1.00 11.94 ?  594 VAL A CG1   1 
ATOM   4763  C  CG2   . VAL A 1 594 ? 140.081 131.209 95.300  1.00 18.42 ?  594 VAL A CG2   1 
ATOM   4764  N  N     . MET A 1 595 ? 137.917 128.132 95.440  1.00 22.05 ?  595 MET A N     1 
ATOM   4765  C  CA    . MET A 1 595 ? 138.164 126.746 95.790  1.00 20.53 ?  595 MET A CA    1 
ATOM   4766  C  C     . MET A 1 595 ? 137.422 125.809 94.840  1.00 23.58 ?  595 MET A C     1 
ATOM   4767  O  O     . MET A 1 595 ? 136.405 126.185 94.251  1.00 25.01 ?  595 MET A O     1 
ATOM   4768  C  CB    . MET A 1 595 ? 137.731 126.481 97.231  1.00 22.89 ?  595 MET A CB    1 
ATOM   4769  C  CG    . MET A 1 595 ? 138.874 126.258 98.223  1.00 21.47 ?  595 MET A CG    1 
ATOM   4770  S  SD    . MET A 1 595 ? 140.362 127.243 97.955  1.00 30.92 ?  595 MET A SD    1 
ATOM   4771  C  CE    . MET A 1 595 ? 139.735 128.913 98.088  1.00 31.89 ?  595 MET A CE    1 
ATOM   4772  N  N     . PRO A 1 596 ? 137.918 124.588 94.664  1.00 30.79 ?  596 PRO A N     1 
ATOM   4773  C  CA    . PRO A 1 596 ? 137.204 123.612 93.836  1.00 20.09 ?  596 PRO A CA    1 
ATOM   4774  C  C     . PRO A 1 596 ? 135.931 123.126 94.511  1.00 25.96 ?  596 PRO A C     1 
ATOM   4775  O  O     . PRO A 1 596 ? 135.757 123.218 95.728  1.00 30.13 ?  596 PRO A O     1 
ATOM   4776  C  CB    . PRO A 1 596 ? 138.216 122.476 93.673  1.00 23.39 ?  596 PRO A CB    1 
ATOM   4777  C  CG    . PRO A 1 596 ? 139.108 122.599 94.857  1.00 29.22 ?  596 PRO A CG    1 
ATOM   4778  C  CD    . PRO A 1 596 ? 139.200 124.060 95.160  1.00 28.42 ?  596 PRO A CD    1 
ATOM   4779  N  N     . ILE A 1 597 ? 135.026 122.599 93.683  1.00 27.79 ?  597 ILE A N     1 
ATOM   4780  C  CA    . ILE A 1 597 ? 133.736 122.137 94.175  1.00 30.69 ?  597 ILE A CA    1 
ATOM   4781  C  C     . ILE A 1 597 ? 133.914 120.893 95.035  1.00 31.57 ?  597 ILE A C     1 
ATOM   4782  O  O     . ILE A 1 597 ? 134.828 120.083 94.826  1.00 31.34 ?  597 ILE A O     1 
ATOM   4783  C  CB    . ILE A 1 597 ? 132.775 121.865 93.003  1.00 31.28 ?  597 ILE A CB    1 
ATOM   4784  C  CG1   . ILE A 1 597 ? 133.243 120.648 92.201  1.00 27.57 ?  597 ILE A CG1   1 
ATOM   4785  C  CG2   . ILE A 1 597 ? 132.674 123.079 92.111  1.00 29.49 ?  597 ILE A CG2   1 
ATOM   4786  C  CD1   . ILE A 1 597 ? 132.124 119.851 91.589  1.00 28.63 ?  597 ILE A CD1   1 
ATOM   4787  N  N     . MET A 1 598 ? 133.029 120.736 96.016  1.00 40.39 ?  598 MET A N     1 
ATOM   4788  C  CA    . MET A 1 598 ? 133.043 119.565 96.882  1.00 41.34 ?  598 MET A CA    1 
ATOM   4789  C  C     . MET A 1 598 ? 132.209 118.423 96.317  1.00 40.72 ?  598 MET A C     1 
ATOM   4790  O  O     . MET A 1 598 ? 132.646 117.268 96.341  1.00 44.88 ?  598 MET A O     1 
ATOM   4791  C  CB    . MET A 1 598 ? 132.541 119.938 98.278  1.00 42.03 ?  598 MET A CB    1 
ATOM   4792  C  CG    . MET A 1 598 ? 133.073 121.263 98.791  1.00 39.71 ?  598 MET A CG    1 
ATOM   4793  S  SD    . MET A 1 598 ? 132.937 121.436 100.579 1.00 57.19 ?  598 MET A SD    1 
ATOM   4794  C  CE    . MET A 1 598 ? 131.606 120.293 100.937 1.00 44.70 ?  598 MET A CE    1 
ATOM   4795  N  N     . GLU A 1 599 ? 131.013 118.722 95.815  1.00 41.01 ?  599 GLU A N     1 
ATOM   4796  C  CA    . GLU A 1 599 ? 130.134 117.734 95.209  1.00 39.32 ?  599 GLU A CA    1 
ATOM   4797  C  C     . GLU A 1 599 ? 129.685 118.232 93.845  1.00 38.14 ?  599 GLU A C     1 
ATOM   4798  O  O     . GLU A 1 599 ? 129.419 119.424 93.671  1.00 42.33 ?  599 GLU A O     1 
ATOM   4799  C  CB    . GLU A 1 599 ? 128.904 117.459 96.086  1.00 42.81 ?  599 GLU A CB    1 
ATOM   4800  C  CG    . GLU A 1 599 ? 129.171 117.515 97.579  1.00 44.35 ?  599 GLU A CG    1 
ATOM   4801  C  CD    . GLU A 1 599 ? 127.897 117.508 98.402  1.00 48.19 ?  599 GLU A CD    1 
ATOM   4802  O  OE1   . GLU A 1 599 ? 127.247 116.446 98.485  1.00 47.76 ?  599 GLU A OE1   1 
ATOM   4803  O  OE2   . GLU A 1 599 ? 127.548 118.565 98.967  1.00 45.85 -1 599 GLU A OE2   1 
ATOM   4804  N  N     . ARG A 1 600 ? 129.609 117.318 92.875  1.00 41.41 ?  600 ARG A N     1 
ATOM   4805  C  CA    . ARG A 1 600 ? 129.089 117.683 91.562  1.00 36.75 ?  600 ARG A CA    1 
ATOM   4806  C  C     . ARG A 1 600 ? 127.610 118.036 91.644  1.00 37.88 ?  600 ARG A C     1 
ATOM   4807  O  O     . ARG A 1 600 ? 127.175 119.068 91.123  1.00 41.00 ?  600 ARG A O     1 
ATOM   4808  C  CB    . ARG A 1 600 ? 129.315 116.545 90.569  1.00 36.61 ?  600 ARG A CB    1 
ATOM   4809  C  CG    . ARG A 1 600 ? 130.715 116.491 90.001  1.00 36.23 ?  600 ARG A CG    1 
ATOM   4810  C  CD    . ARG A 1 600 ? 130.788 115.525 88.841  1.00 36.48 ?  600 ARG A CD    1 
ATOM   4811  N  NE    . ARG A 1 600 ? 132.158 115.265 88.418  1.00 35.63 ?  600 ARG A NE    1 
ATOM   4812  C  CZ    . ARG A 1 600 ? 132.964 114.384 88.994  1.00 38.66 ?  600 ARG A CZ    1 
ATOM   4813  N  NH1   . ARG A 1 600 ? 132.576 113.674 90.039  1.00 37.64 1  600 ARG A NH1   1 
ATOM   4814  N  NH2   . ARG A 1 600 ? 134.191 114.215 88.511  1.00 39.46 ?  600 ARG A NH2   1 
ATOM   4815  N  N     . ILE A 1 601 ? 126.823 117.182 92.290  1.00 45.37 ?  601 ILE A N     1 
ATOM   4816  C  CA    . ILE A 1 601 ? 125.423 117.454 92.586  1.00 43.26 ?  601 ILE A CA    1 
ATOM   4817  C  C     . ILE A 1 601 ? 125.290 117.496 94.100  1.00 42.50 ?  601 ILE A C     1 
ATOM   4818  O  O     . ILE A 1 601 ? 125.588 116.509 94.783  1.00 46.73 ?  601 ILE A O     1 
ATOM   4819  C  CB    . ILE A 1 601 ? 124.486 116.401 91.976  1.00 42.87 ?  601 ILE A CB    1 
ATOM   4820  C  CG1   . ILE A 1 601 ? 124.829 116.177 90.503  1.00 43.32 ?  601 ILE A CG1   1 
ATOM   4821  C  CG2   . ILE A 1 601 ? 123.037 116.835 92.122  1.00 42.85 ?  601 ILE A CG2   1 
ATOM   4822  C  CD1   . ILE A 1 601 ? 123.979 115.131 89.829  1.00 43.38 ?  601 ILE A CD1   1 
ATOM   4823  N  N     . GLU A 1 602 ? 124.846 118.632 94.621  1.00 49.62 ?  602 GLU A N     1 
ATOM   4824  C  CA    . GLU A 1 602 ? 124.819 118.879 96.054  1.00 49.44 ?  602 GLU A CA    1 
ATOM   4825  C  C     . GLU A 1 602 ? 123.419 118.592 96.584  1.00 51.45 ?  602 GLU A C     1 
ATOM   4826  O  O     . GLU A 1 602 ? 122.445 119.217 96.151  1.00 53.93 ?  602 GLU A O     1 
ATOM   4827  C  CB    . GLU A 1 602 ? 125.238 120.316 96.356  1.00 49.41 ?  602 GLU A CB    1 
ATOM   4828  C  CG    . GLU A 1 602 ? 124.785 120.838 97.700  1.00 50.26 ?  602 GLU A CG    1 
ATOM   4829  C  CD    . GLU A 1 602 ? 125.054 122.320 97.860  1.00 54.59 ?  602 GLU A CD    1 
ATOM   4830  O  OE1   . GLU A 1 602 ? 126.052 122.807 97.287  1.00 52.32 ?  602 GLU A OE1   1 
ATOM   4831  O  OE2   . GLU A 1 602 ? 124.271 122.996 98.559  1.00 56.03 -1 602 GLU A OE2   1 
ATOM   4832  N  N     . GLU A 1 603 ? 123.324 117.645 97.512  1.00 56.98 ?  603 GLU A N     1 
ATOM   4833  C  CA    . GLU A 1 603 ? 122.056 117.234 98.096  1.00 57.36 ?  603 GLU A CA    1 
ATOM   4834  C  C     . GLU A 1 603 ? 121.881 117.905 99.451  1.00 58.62 ?  603 GLU A C     1 
ATOM   4835  O  O     . GLU A 1 603 ? 122.754 117.802 100.318 1.00 58.60 ?  603 GLU A O     1 
ATOM   4836  C  CB    . GLU A 1 603 ? 121.996 115.713 98.245  1.00 59.38 ?  603 GLU A CB    1 
ATOM   4837  C  CG    . GLU A 1 603 ? 120.697 115.193 98.833  1.00 60.68 ?  603 GLU A CG    1 
ATOM   4838  C  CD    . GLU A 1 603 ? 120.785 113.734 99.240  1.00 61.55 ?  603 GLU A CD    1 
ATOM   4839  O  OE1   . GLU A 1 603 ? 120.795 112.863 98.346  1.00 60.08 ?  603 GLU A OE1   1 
ATOM   4840  O  OE2   . GLU A 1 603 ? 120.847 113.458 100.457 1.00 59.52 -1 603 GLU A OE2   1 
ATOM   4841  N  N     . ARG A 1 604 ? 120.753 118.588 99.629  1.00 61.77 ?  604 ARG A N     1 
ATOM   4842  C  CA    . ARG A 1 604 ? 120.452 119.295 100.863 1.00 61.85 ?  604 ARG A CA    1 
ATOM   4843  C  C     . ARG A 1 604 ? 119.028 118.988 101.296 1.00 62.69 ?  604 ARG A C     1 
ATOM   4844  O  O     . ARG A 1 604 ? 118.170 118.649 100.476 1.00 64.24 ?  604 ARG A O     1 
ATOM   4845  C  CB    . ARG A 1 604 ? 120.621 120.812 100.703 1.00 59.98 ?  604 ARG A CB    1 
ATOM   4846  C  CG    . ARG A 1 604 ? 122.025 121.263 100.343 1.00 61.07 ?  604 ARG A CG    1 
ATOM   4847  C  CD    . ARG A 1 604 ? 122.979 121.086 101.510 1.00 62.30 ?  604 ARG A CD    1 
ATOM   4848  N  NE    . ARG A 1 604 ? 123.958 120.035 101.260 1.00 63.37 ?  604 ARG A NE    1 
ATOM   4849  C  CZ    . ARG A 1 604 ? 125.252 120.251 101.060 1.00 62.57 ?  604 ARG A CZ    1 
ATOM   4850  N  NH1   . ARG A 1 604 ? 125.759 121.472 101.077 1.00 61.28 1  604 ARG A NH1   1 
ATOM   4851  N  NH2   . ARG A 1 604 ? 126.055 119.216 100.836 1.00 60.05 ?  604 ARG A NH2   1 
ATOM   4852  N  N     . THR A 1 605 ? 118.784 119.108 102.598 1.00 68.82 ?  605 THR A N     1 
ATOM   4853  C  CA    . THR A 1 605 ? 117.454 118.946 103.172 1.00 70.06 ?  605 THR A CA    1 
ATOM   4854  C  C     . THR A 1 605 ? 117.061 120.248 103.853 1.00 69.42 ?  605 THR A C     1 
ATOM   4855  O  O     . THR A 1 605 ? 117.722 120.677 104.805 1.00 69.58 ?  605 THR A O     1 
ATOM   4856  C  CB    . THR A 1 605 ? 117.417 117.785 104.170 1.00 70.54 ?  605 THR A CB    1 
ATOM   4857  O  OG1   . THR A 1 605 ? 118.304 116.748 103.735 1.00 71.33 ?  605 THR A OG1   1 
ATOM   4858  C  CG2   . THR A 1 605 ? 116.009 117.224 104.275 1.00 69.20 ?  605 THR A CG2   1 
ATOM   4859  N  N     . TYR A 1 606 ? 115.994 120.872 103.366 1.00 68.76 ?  606 TYR A N     1 
ATOM   4860  C  CA    . TYR A 1 606 ? 115.473 122.113 103.930 1.00 71.10 ?  606 TYR A CA    1 
ATOM   4861  C  C     . TYR A 1 606 ? 114.128 121.804 104.573 1.00 72.93 ?  606 TYR A C     1 
ATOM   4862  O  O     . TYR A 1 606 ? 113.157 121.492 103.874 1.00 70.59 ?  606 TYR A O     1 
ATOM   4863  C  CB    . TYR A 1 606 ? 115.347 123.192 102.856 1.00 69.38 ?  606 TYR A CB    1 
ATOM   4864  C  CG    . TYR A 1 606 ? 116.678 123.646 102.302 1.00 70.30 ?  606 TYR A CG    1 
ATOM   4865  C  CD1   . TYR A 1 606 ? 117.463 124.564 102.988 1.00 68.23 ?  606 TYR A CD1   1 
ATOM   4866  C  CD2   . TYR A 1 606 ? 117.154 123.150 101.098 1.00 69.45 ?  606 TYR A CD2   1 
ATOM   4867  C  CE1   . TYR A 1 606 ? 118.682 124.977 102.485 1.00 68.83 ?  606 TYR A CE1   1 
ATOM   4868  C  CE2   . TYR A 1 606 ? 118.370 123.556 100.587 1.00 67.17 ?  606 TYR A CE2   1 
ATOM   4869  C  CZ    . TYR A 1 606 ? 119.129 124.468 101.285 1.00 70.11 ?  606 TYR A CZ    1 
ATOM   4870  O  OH    . TYR A 1 606 ? 120.342 124.874 100.777 1.00 70.97 ?  606 TYR A OH    1 
ATOM   4871  N  N     . GLY A 1 607 ? 114.071 121.896 105.895 1.00 80.04 ?  607 GLY A N     1 
ATOM   4872  C  CA    . GLY A 1 607 ? 112.879 121.468 106.606 1.00 78.48 ?  607 GLY A CA    1 
ATOM   4873  C  C     . GLY A 1 607 ? 112.672 119.979 106.414 1.00 78.34 ?  607 GLY A C     1 
ATOM   4874  O  O     . GLY A 1 607 ? 113.571 119.165 106.658 1.00 78.36 ?  607 GLY A O     1 
ATOM   4875  N  N     . ASN A 1 608 ? 111.474 119.603 105.966 1.00 79.97 ?  608 ASN A N     1 
ATOM   4876  C  CA    . ASN A 1 608 ? 111.151 118.217 105.655 1.00 81.03 ?  608 ASN A CA    1 
ATOM   4877  C  C     . ASN A 1 608 ? 111.179 117.944 104.156 1.00 80.88 ?  608 ASN A C     1 
ATOM   4878  O  O     . ASN A 1 608 ? 110.528 117.008 103.679 1.00 80.73 ?  608 ASN A O     1 
ATOM   4879  C  CB    . ASN A 1 608 ? 109.787 117.845 106.241 1.00 80.47 ?  608 ASN A CB    1 
ATOM   4880  C  CG    . ASN A 1 608 ? 109.745 117.982 107.752 1.00 81.27 ?  608 ASN A CG    1 
ATOM   4881  O  OD1   . ASN A 1 608 ? 110.782 118.075 108.410 1.00 80.58 ?  608 ASN A OD1   1 
ATOM   4882  N  ND2   . ASN A 1 608 ? 108.540 117.994 108.310 1.00 80.54 ?  608 ASN A ND2   1 
ATOM   4883  N  N     . SER A 1 609 ? 111.927 118.745 103.403 1.00 77.90 ?  609 SER A N     1 
ATOM   4884  C  CA    . SER A 1 609 ? 112.019 118.622 101.956 1.00 77.94 ?  609 SER A CA    1 
ATOM   4885  C  C     . SER A 1 609 ? 113.469 118.406 101.549 1.00 77.93 ?  609 SER A C     1 
ATOM   4886  O  O     . SER A 1 609 ? 114.373 119.076 102.058 1.00 78.15 ?  609 SER A O     1 
ATOM   4887  C  CB    . SER A 1 609 ? 111.465 119.870 101.262 1.00 76.58 ?  609 SER A CB    1 
ATOM   4888  O  OG    . SER A 1 609 ? 112.217 121.021 101.608 1.00 77.68 ?  609 SER A OG    1 
ATOM   4889  N  N     . LYS A 1 610 ? 113.684 117.473 100.627 1.00 66.97 ?  610 LYS A N     1 
ATOM   4890  C  CA    . LYS A 1 610 ? 115.010 117.152 100.119 1.00 66.32 ?  610 LYS A CA    1 
ATOM   4891  C  C     . LYS A 1 610 ? 115.131 117.648 98.685  1.00 66.53 ?  610 LYS A C     1 
ATOM   4892  O  O     . LYS A 1 610 ? 114.277 117.346 97.844  1.00 67.67 ?  610 LYS A O     1 
ATOM   4893  C  CB    . LYS A 1 610 ? 115.273 115.648 100.188 1.00 66.92 ?  610 LYS A CB    1 
ATOM   4894  C  CG    . LYS A 1 610 ? 116.283 115.141 99.173  1.00 66.39 ?  610 LYS A CG    1 
ATOM   4895  C  CD    . LYS A 1 610 ? 116.914 113.834 99.626  1.00 66.95 ?  610 LYS A CD    1 
ATOM   4896  C  CE    . LYS A 1 610 ? 117.406 113.920 101.062 1.00 66.22 ?  610 LYS A CE    1 
ATOM   4897  N  NZ    . LYS A 1 610 ? 118.399 115.013 101.243 1.00 66.39 1  610 LYS A NZ    1 
ATOM   4898  N  N     . THR A 1 611 ? 116.189 118.406 98.410  1.00 64.78 ?  611 THR A N     1 
ATOM   4899  C  CA    . THR A 1 611 ? 116.405 118.993 97.096  1.00 63.63 ?  611 THR A CA    1 
ATOM   4900  C  C     . THR A 1 611 ? 117.872 118.865 96.719  1.00 62.02 ?  611 THR A C     1 
ATOM   4901  O  O     . THR A 1 611 ? 118.747 118.805 97.585  1.00 61.18 ?  611 THR A O     1 
ATOM   4902  C  CB    . THR A 1 611 ? 115.979 120.465 97.061  1.00 64.51 ?  611 THR A CB    1 
ATOM   4903  O  OG1   . THR A 1 611 ? 116.414 121.059 95.832  1.00 68.33 ?  611 THR A OG1   1 
ATOM   4904  C  CG2   . THR A 1 611 ? 116.584 121.216 98.232  1.00 61.51 ?  611 THR A CG2   1 
ATOM   4905  N  N     . TYR A 1 612 ? 118.133 118.823 95.415  1.00 55.17 ?  612 TYR A N     1 
ATOM   4906  C  CA    . TYR A 1 612 ? 119.470 118.595 94.892  1.00 53.75 ?  612 TYR A CA    1 
ATOM   4907  C  C     . TYR A 1 612 ? 119.910 119.783 94.050  1.00 55.99 ?  612 TYR A C     1 
ATOM   4908  O  O     . TYR A 1 612 ? 119.121 120.343 93.284  1.00 55.12 ?  612 TYR A O     1 
ATOM   4909  C  CB    . TYR A 1 612 ? 119.544 117.311 94.050  1.00 56.44 ?  612 TYR A CB    1 
ATOM   4910  C  CG    . TYR A 1 612 ? 119.036 116.060 94.739  1.00 58.31 ?  612 TYR A CG    1 
ATOM   4911  C  CD1   . TYR A 1 612 ? 117.690 115.901 95.047  1.00 57.73 ?  612 TYR A CD1   1 
ATOM   4912  C  CD2   . TYR A 1 612 ? 119.911 115.048 95.106  1.00 57.67 ?  612 TYR A CD2   1 
ATOM   4913  C  CE1   . TYR A 1 612 ? 117.230 114.764 95.678  1.00 58.44 ?  612 TYR A CE1   1 
ATOM   4914  C  CE2   . TYR A 1 612 ? 119.460 113.907 95.738  1.00 58.52 ?  612 TYR A CE2   1 
ATOM   4915  C  CZ    . TYR A 1 612 ? 118.119 113.771 96.023  1.00 60.23 ?  612 TYR A CZ    1 
ATOM   4916  O  OH    . TYR A 1 612 ? 117.667 112.635 96.655  1.00 60.85 ?  612 TYR A OH    1 
ATOM   4917  N  N     . TYR A 1 613 ? 121.177 120.161 94.199  1.00 51.49 ?  613 TYR A N     1 
ATOM   4918  C  CA    . TYR A 1 613 ? 121.756 121.294 93.478  1.00 42.49 ?  613 TYR A CA    1 
ATOM   4919  C  C     . TYR A 1 613 ? 122.936 120.841 92.634  1.00 41.14 ?  613 TYR A C     1 
ATOM   4920  O  O     . TYR A 1 613 ? 124.048 120.661 93.163  1.00 44.64 ?  613 TYR A O     1 
ATOM   4921  C  CB    . TYR A 1 613 ? 122.191 122.389 94.449  1.00 41.40 ?  613 TYR A CB    1 
ATOM   4922  C  CG    . TYR A 1 613 ? 122.820 123.583 93.772  1.00 41.89 ?  613 TYR A CG    1 
ATOM   4923  C  CD1   . TYR A 1 613 ? 122.209 124.191 92.684  1.00 42.79 ?  613 TYR A CD1   1 
ATOM   4924  C  CD2   . TYR A 1 613 ? 124.025 124.105 94.220  1.00 42.04 ?  613 TYR A CD2   1 
ATOM   4925  C  CE1   . TYR A 1 613 ? 122.776 125.283 92.065  1.00 43.12 ?  613 TYR A CE1   1 
ATOM   4926  C  CE2   . TYR A 1 613 ? 124.602 125.197 93.606  1.00 43.78 ?  613 TYR A CE2   1 
ATOM   4927  C  CZ    . TYR A 1 613 ? 123.973 125.783 92.530  1.00 46.61 ?  613 TYR A CZ    1 
ATOM   4928  O  OH    . TYR A 1 613 ? 124.543 126.871 91.914  1.00 46.20 ?  613 TYR A OH    1 
ATOM   4929  N  N     . PRO A 1 614 ? 122.755 120.640 91.333  1.00 40.55 ?  614 PRO A N     1 
ATOM   4930  C  CA    . PRO A 1 614 ? 123.912 120.412 90.464  1.00 40.16 ?  614 PRO A CA    1 
ATOM   4931  C  C     . PRO A 1 614 ? 124.785 121.652 90.401  1.00 40.09 ?  614 PRO A C     1 
ATOM   4932  O  O     . PRO A 1 614 ? 124.312 122.782 90.552  1.00 43.40 ?  614 PRO A O     1 
ATOM   4933  C  CB    . PRO A 1 614 ? 123.285 120.102 89.098  1.00 37.04 ?  614 PRO A CB    1 
ATOM   4934  C  CG    . PRO A 1 614 ? 121.829 119.873 89.363  1.00 43.01 ?  614 PRO A CG    1 
ATOM   4935  C  CD    . PRO A 1 614 ? 121.493 120.661 90.581  1.00 42.07 ?  614 PRO A CD    1 
ATOM   4936  N  N     . MET A 1 615 ? 126.078 121.432 90.187  1.00 37.48 ?  615 MET A N     1 
ATOM   4937  C  CA    . MET A 1 615 ? 126.997 122.548 90.069  1.00 37.01 ?  615 MET A CA    1 
ATOM   4938  C  C     . MET A 1 615 ? 126.634 123.390 88.847  1.00 41.63 ?  615 MET A C     1 
ATOM   4939  O  O     . MET A 1 615 ? 126.133 122.864 87.849  1.00 38.54 ?  615 MET A O     1 
ATOM   4940  C  CB    . MET A 1 615 ? 128.436 122.051 89.967  1.00 33.82 ?  615 MET A CB    1 
ATOM   4941  C  CG    . MET A 1 615 ? 129.094 121.829 91.316  1.00 36.13 ?  615 MET A CG    1 
ATOM   4942  S  SD    . MET A 1 615 ? 128.664 123.108 92.512  1.00 52.76 ?  615 MET A SD    1 
ATOM   4943  C  CE    . MET A 1 615 ? 127.717 122.164 93.704  1.00 35.65 ?  615 MET A CE    1 
ATOM   4944  N  N     . PRO A 1 616 ? 126.845 124.703 88.912  1.00 40.49 ?  616 PRO A N     1 
ATOM   4945  C  CA    . PRO A 1 616 ? 126.429 125.574 87.805  1.00 35.85 ?  616 PRO A CA    1 
ATOM   4946  C  C     . PRO A 1 616 ? 127.085 125.172 86.493  1.00 36.86 ?  616 PRO A C     1 
ATOM   4947  O  O     . PRO A 1 616 ? 128.309 125.074 86.395  1.00 38.67 ?  616 PRO A O     1 
ATOM   4948  C  CB    . PRO A 1 616 ? 126.886 126.962 88.263  1.00 36.67 ?  616 PRO A CB    1 
ATOM   4949  C  CG    . PRO A 1 616 ? 126.935 126.863 89.749  1.00 38.59 ?  616 PRO A CG    1 
ATOM   4950  C  CD    . PRO A 1 616 ? 127.375 125.469 90.051  1.00 35.46 ?  616 PRO A CD    1 
ATOM   4951  N  N     . GLY A 1 617 ? 126.255 124.944 85.480  1.00 36.72 ?  617 GLY A N     1 
ATOM   4952  C  CA    . GLY A 1 617 ? 126.741 124.525 84.185  1.00 31.13 ?  617 GLY A CA    1 
ATOM   4953  C  C     . GLY A 1 617 ? 127.101 123.063 84.075  1.00 38.40 ?  617 GLY A C     1 
ATOM   4954  O  O     . GLY A 1 617 ? 127.661 122.658 83.050  1.00 40.80 ?  617 GLY A O     1 
ATOM   4955  N  N     . LEU A 1 618 ? 126.808 122.259 85.095  1.00 39.29 ?  618 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 618 ? 127.142 120.843 85.049  1.00 34.62 ?  618 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 618 ? 126.321 120.134 83.980  1.00 39.88 ?  618 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 618 ? 125.119 120.368 83.836  1.00 40.59 ?  618 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 618 ? 126.905 120.191 86.411  1.00 34.82 ?  618 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 618 ? 127.217 118.699 86.535  1.00 37.41 ?  618 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 618 ? 128.683 118.416 86.245  1.00 34.92 ?  618 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 618 ? 126.834 118.179 87.911  1.00 35.44 ?  618 LEU A CD2   1 
ATOM   4963  N  N     . ALA A 1 619 ? 126.985 119.265 83.229  1.00 43.40 ?  619 ALA A N     1 
ATOM   4964  C  CA    . ALA A 1 619 ? 126.357 118.497 82.163  1.00 43.12 ?  619 ALA A CA    1 
ATOM   4965  C  C     . ALA A 1 619 ? 127.185 117.236 81.953  1.00 44.84 ?  619 ALA A C     1 
ATOM   4966  O  O     . ALA A 1 619 ? 128.049 116.899 82.769  1.00 50.01 ?  619 ALA A O     1 
ATOM   4967  C  CB    . ALA A 1 619 ? 126.234 119.331 80.883  1.00 41.78 ?  619 ALA A CB    1 
ATOM   4968  N  N     . SER A 1 620 ? 126.921 116.531 80.854  1.00 50.05 ?  620 SER A N     1 
ATOM   4969  C  CA    . SER A 1 620 ? 127.724 115.362 80.522  1.00 50.39 ?  620 SER A CA    1 
ATOM   4970  C  C     . SER A 1 620 ? 128.973 115.738 79.737  1.00 50.52 ?  620 SER A C     1 
ATOM   4971  O  O     . SER A 1 620 ? 129.954 114.987 79.743  1.00 54.16 ?  620 SER A O     1 
ATOM   4972  C  CB    . SER A 1 620 ? 126.887 114.356 79.730  1.00 53.17 ?  620 SER A CB    1 
ATOM   4973  O  OG    . SER A 1 620 ? 125.720 113.994 80.447  1.00 55.31 ?  620 SER A OG    1 
ATOM   4974  N  N     . ASN A 1 621 ? 128.958 116.890 79.062  1.00 48.00 ?  621 ASN A N     1 
ATOM   4975  C  CA    . ASN A 1 621 ? 130.120 117.307 78.286  1.00 48.37 ?  621 ASN A CA    1 
ATOM   4976  C  C     . ASN A 1 621 ? 131.226 117.863 79.175  1.00 51.61 ?  621 ASN A C     1 
ATOM   4977  O  O     . ASN A 1 621 ? 132.383 117.938 78.746  1.00 51.96 ?  621 ASN A O     1 
ATOM   4978  C  CB    . ASN A 1 621 ? 129.707 118.341 77.239  1.00 49.02 ?  621 ASN A CB    1 
ATOM   4979  C  CG    . ASN A 1 621 ? 129.673 119.751 77.793  1.00 51.03 ?  621 ASN A CG    1 
ATOM   4980  O  OD1   . ASN A 1 621 ? 128.795 120.099 78.582  1.00 50.38 ?  621 ASN A OD1   1 
ATOM   4981  N  ND2   . ASN A 1 621 ? 130.630 120.572 77.379  1.00 47.50 ?  621 ASN A ND2   1 
ATOM   4982  N  N     . ASN A 1 622 ? 130.897 118.258 80.405  1.00 44.03 ?  622 ASN A N     1 
ATOM   4983  C  CA    . ASN A 1 622 ? 131.878 118.776 81.352  1.00 40.24 ?  622 ASN A CA    1 
ATOM   4984  C  C     . ASN A 1 622 ? 131.736 118.118 82.721  1.00 42.76 ?  622 ASN A C     1 
ATOM   4985  O  O     . ASN A 1 622 ? 132.038 118.730 83.746  1.00 48.61 ?  622 ASN A O     1 
ATOM   4986  C  CB    . ASN A 1 622 ? 131.775 120.298 81.465  1.00 42.91 ?  622 ASN A CB    1 
ATOM   4987  C  CG    . ASN A 1 622 ? 130.385 120.774 81.861  1.00 42.30 ?  622 ASN A CG    1 
ATOM   4988  O  OD1   . ASN A 1 622 ? 129.662 120.100 82.591  1.00 43.38 ?  622 ASN A OD1   1 
ATOM   4989  N  ND2   . ASN A 1 622 ? 130.010 121.952 81.377  1.00 41.97 ?  622 ASN A ND2   1 
ATOM   4990  N  N     . TRP A 1 623 ? 131.265 116.869 82.747  1.00 37.70 ?  623 TRP A N     1 
ATOM   4991  C  CA    . TRP A 1 623 ? 131.090 116.171 84.016  1.00 38.13 ?  623 TRP A CA    1 
ATOM   4992  C  C     . TRP A 1 623 ? 132.425 115.937 84.712  1.00 38.97 ?  623 TRP A C     1 
ATOM   4993  O  O     . TRP A 1 623 ? 132.543 116.137 85.927  1.00 36.89 ?  623 TRP A O     1 
ATOM   4994  C  CB    . TRP A 1 623 ? 130.369 114.844 83.784  1.00 41.13 ?  623 TRP A CB    1 
ATOM   4995  C  CG    . TRP A 1 623 ? 130.241 113.999 85.013  1.00 37.94 ?  623 TRP A CG    1 
ATOM   4996  C  CD1   . TRP A 1 623 ? 131.114 113.046 85.445  1.00 37.18 ?  623 TRP A CD1   1 
ATOM   4997  C  CD2   . TRP A 1 623 ? 129.173 114.026 85.966  1.00 36.34 ?  623 TRP A CD2   1 
ATOM   4998  N  NE1   . TRP A 1 623 ? 130.660 112.480 86.610  1.00 37.99 ?  623 TRP A NE1   1 
ATOM   4999  C  CE2   . TRP A 1 623 ? 129.469 113.062 86.949  1.00 38.89 ?  623 TRP A CE2   1 
ATOM   5000  C  CE3   . TRP A 1 623 ? 127.997 114.770 86.082  1.00 37.48 ?  623 TRP A CE3   1 
ATOM   5001  C  CZ2   . TRP A 1 623 ? 128.632 112.827 88.036  1.00 37.40 ?  623 TRP A CZ2   1 
ATOM   5002  C  CZ3   . TRP A 1 623 ? 127.167 114.534 87.162  1.00 38.40 ?  623 TRP A CZ3   1 
ATOM   5003  C  CH2   . TRP A 1 623 ? 127.489 113.571 88.124  1.00 37.73 ?  623 TRP A CH2   1 
ATOM   5004  N  N     . PHE A 1 624 ? 133.440 115.510 83.964  1.00 43.16 ?  624 PHE A N     1 
ATOM   5005  C  CA    . PHE A 1 624 ? 134.726 115.179 84.561  1.00 41.82 ?  624 PHE A CA    1 
ATOM   5006  C  C     . PHE A 1 624 ? 135.630 116.388 84.747  1.00 42.59 ?  624 PHE A C     1 
ATOM   5007  O  O     . PHE A 1 624 ? 136.625 116.292 85.474  1.00 50.03 ?  624 PHE A O     1 
ATOM   5008  C  CB    . PHE A 1 624 ? 135.435 114.119 83.717  1.00 41.56 ?  624 PHE A CB    1 
ATOM   5009  C  CG    . PHE A 1 624 ? 134.737 112.789 83.720  1.00 45.32 ?  624 PHE A CG    1 
ATOM   5010  C  CD1   . PHE A 1 624 ? 134.715 112.010 84.864  1.00 42.10 ?  624 PHE A CD1   1 
ATOM   5011  C  CD2   . PHE A 1 624 ? 134.084 112.329 82.589  1.00 44.92 ?  624 PHE A CD2   1 
ATOM   5012  C  CE1   . PHE A 1 624 ? 134.067 110.792 84.877  1.00 41.33 ?  624 PHE A CE1   1 
ATOM   5013  C  CE2   . PHE A 1 624 ? 133.434 111.112 82.597  1.00 42.77 ?  624 PHE A CE2   1 
ATOM   5014  C  CZ    . PHE A 1 624 ? 133.425 110.343 83.741  1.00 45.45 ?  624 PHE A CZ    1 
ATOM   5015  N  N     . PHE A 1 625 ? 135.311 117.520 84.117  1.00 34.98 ?  625 PHE A N     1 
ATOM   5016  C  CA    . PHE A 1 625 ? 135.998 118.761 84.446  1.00 32.84 ?  625 PHE A CA    1 
ATOM   5017  C  C     . PHE A 1 625 ? 135.523 119.334 85.772  1.00 32.46 ?  625 PHE A C     1 
ATOM   5018  O  O     . PHE A 1 625 ? 136.236 120.140 86.377  1.00 36.35 ?  625 PHE A O     1 
ATOM   5019  C  CB    . PHE A 1 625 ? 135.812 119.787 83.331  1.00 31.54 ?  625 PHE A CB    1 
ATOM   5020  C  CG    . PHE A 1 625 ? 136.574 119.465 82.082  1.00 30.72 ?  625 PHE A CG    1 
ATOM   5021  C  CD1   . PHE A 1 625 ? 137.956 119.457 82.085  1.00 33.14 ?  625 PHE A CD1   1 
ATOM   5022  C  CD2   . PHE A 1 625 ? 135.910 119.177 80.902  1.00 34.06 ?  625 PHE A CD2   1 
ATOM   5023  C  CE1   . PHE A 1 625 ? 138.664 119.166 80.939  1.00 36.70 ?  625 PHE A CE1   1 
ATOM   5024  C  CE2   . PHE A 1 625 ? 136.613 118.886 79.752  1.00 32.14 ?  625 PHE A CE2   1 
ATOM   5025  C  CZ    . PHE A 1 625 ? 137.991 118.879 79.771  1.00 36.32 ?  625 PHE A CZ    1 
ATOM   5026  N  N     . TYR A 1 626 ? 134.340 118.937 86.233  1.00 29.43 ?  626 TYR A N     1 
ATOM   5027  C  CA    . TYR A 1 626 ? 133.850 119.310 87.558  1.00 31.49 ?  626 TYR A CA    1 
ATOM   5028  C  C     . TYR A 1 626 ? 134.325 118.319 88.613  1.00 27.64 ?  626 TYR A C     1 
ATOM   5029  O  O     . TYR A 1 626 ? 133.542 117.781 89.391  1.00 30.79 ?  626 TYR A O     1 
ATOM   5030  C  CB    . TYR A 1 626 ? 132.330 119.407 87.541  1.00 32.51 ?  626 TYR A CB    1 
ATOM   5031  C  CG    . TYR A 1 626 ? 131.814 120.791 87.244  1.00 28.67 ?  626 TYR A CG    1 
ATOM   5032  C  CD1   . TYR A 1 626 ? 131.961 121.818 88.162  1.00 32.63 ?  626 TYR A CD1   1 
ATOM   5033  C  CD2   . TYR A 1 626 ? 131.181 121.071 86.041  1.00 30.61 ?  626 TYR A CD2   1 
ATOM   5034  C  CE1   . TYR A 1 626 ? 131.491 123.085 87.893  1.00 29.49 ?  626 TYR A CE1   1 
ATOM   5035  C  CE2   . TYR A 1 626 ? 130.709 122.334 85.763  1.00 28.96 ?  626 TYR A CE2   1 
ATOM   5036  C  CZ    . TYR A 1 626 ? 130.867 123.337 86.694  1.00 27.83 ?  626 TYR A CZ    1 
ATOM   5037  O  OH    . TYR A 1 626 ? 130.400 124.599 86.426  1.00 34.46 ?  626 TYR A OH    1 
ATOM   5038  N  N     . LYS A 1 627 ? 135.632 118.082 88.637  1.00 31.50 ?  627 LYS A N     1 
ATOM   5039  C  CA    . LYS A 1 627 ? 136.212 117.140 89.583  1.00 31.57 ?  627 LYS A CA    1 
ATOM   5040  C  C     . LYS A 1 627 ? 136.007 117.632 91.008  1.00 31.68 ?  627 LYS A C     1 
ATOM   5041  O  O     . LYS A 1 627 ? 136.232 118.807 91.312  1.00 35.85 ?  627 LYS A O     1 
ATOM   5042  C  CB    . LYS A 1 627 ? 137.699 116.959 89.283  1.00 34.95 ?  627 LYS A CB    1 
ATOM   5043  C  CG    . LYS A 1 627 ? 138.386 115.893 90.108  1.00 34.41 ?  627 LYS A CG    1 
ATOM   5044  C  CD    . LYS A 1 627 ? 139.784 115.630 89.584  1.00 32.48 ?  627 LYS A CD    1 
ATOM   5045  C  CE    . LYS A 1 627 ? 140.499 114.585 90.414  1.00 38.41 ?  627 LYS A CE    1 
ATOM   5046  N  NZ    . LYS A 1 627 ? 141.925 114.449 90.010  1.00 39.70 1  627 LYS A NZ    1 
ATOM   5047  N  N     . GLU A 1 628 ? 135.572 116.731 91.883  1.00 35.59 ?  628 GLU A N     1 
ATOM   5048  C  CA    . GLU A 1 628 ? 135.334 117.101 93.269  1.00 36.22 ?  628 GLU A CA    1 
ATOM   5049  C  C     . GLU A 1 628 ? 136.648 117.413 93.975  1.00 39.79 ?  628 GLU A C     1 
ATOM   5050  O  O     . GLU A 1 628 ? 137.705 116.870 93.643  1.00 42.87 ?  628 GLU A O     1 
ATOM   5051  C  CB    . GLU A 1 628 ? 134.590 115.984 93.999  1.00 37.35 ?  628 GLU A CB    1 
ATOM   5052  C  CG    . GLU A 1 628 ? 133.200 115.713 93.449  1.00 39.53 ?  628 GLU A CG    1 
ATOM   5053  C  CD    . GLU A 1 628 ? 132.420 114.726 94.294  1.00 47.64 ?  628 GLU A CD    1 
ATOM   5054  O  OE1   . GLU A 1 628 ? 132.865 114.424 95.421  1.00 43.85 ?  628 GLU A OE1   1 
ATOM   5055  O  OE2   . GLU A 1 628 ? 131.359 114.256 93.833  1.00 44.12 -1 628 GLU A OE2   1 
ATOM   5056  N  N     . ALA A 1 629 ? 136.570 118.313 94.958  1.00 38.57 ?  629 ALA A N     1 
ATOM   5057  C  CA    . ALA A 1 629 ? 137.770 118.769 95.650  1.00 34.48 ?  629 ALA A CA    1 
ATOM   5058  C  C     . ALA A 1 629 ? 138.450 117.643 96.416  1.00 37.29 ?  629 ALA A C     1 
ATOM   5059  O  O     . ALA A 1 629 ? 139.668 117.683 96.623  1.00 44.58 ?  629 ALA A O     1 
ATOM   5060  C  CB    . ALA A 1 629 ? 137.421 119.914 96.597  1.00 35.14 ?  629 ALA A CB    1 
ATOM   5061  N  N     . TYR A 1 630 ? 137.690 116.642 96.855  1.00 42.65 ?  630 TYR A N     1 
ATOM   5062  C  CA    . TYR A 1 630 ? 138.284 115.557 97.626  1.00 41.94 ?  630 TYR A CA    1 
ATOM   5063  C  C     . TYR A 1 630 ? 139.082 114.604 96.745  1.00 44.19 ?  630 TYR A C     1 
ATOM   5064  O  O     . TYR A 1 630 ? 140.021 113.962 97.226  1.00 44.91 ?  630 TYR A O     1 
ATOM   5065  C  CB    . TYR A 1 630 ? 137.196 114.799 98.382  1.00 39.33 ?  630 TYR A CB    1 
ATOM   5066  C  CG    . TYR A 1 630 ? 136.428 115.658 99.355  1.00 40.78 ?  630 TYR A CG    1 
ATOM   5067  C  CD1   . TYR A 1 630 ? 136.976 116.010 100.580 1.00 38.92 ?  630 TYR A CD1   1 
ATOM   5068  C  CD2   . TYR A 1 630 ? 135.154 116.115 99.050  1.00 40.39 ?  630 TYR A CD2   1 
ATOM   5069  C  CE1   . TYR A 1 630 ? 136.277 116.793 101.473 1.00 39.65 ?  630 TYR A CE1   1 
ATOM   5070  C  CE2   . TYR A 1 630 ? 134.448 116.898 99.939  1.00 40.55 ?  630 TYR A CE2   1 
ATOM   5071  C  CZ    . TYR A 1 630 ? 135.015 117.234 101.149 1.00 44.72 ?  630 TYR A CZ    1 
ATOM   5072  O  OH    . TYR A 1 630 ? 134.317 118.014 102.040 1.00 48.31 ?  630 TYR A OH    1 
ATOM   5073  N  N     . ASP A 1 631 ? 138.733 114.502 95.464  1.00 40.74 ?  631 ASP A N     1 
ATOM   5074  C  CA    . ASP A 1 631 ? 139.400 113.568 94.567  1.00 39.43 ?  631 ASP A CA    1 
ATOM   5075  C  C     . ASP A 1 631 ? 140.676 114.126 93.952  1.00 43.72 ?  631 ASP A C     1 
ATOM   5076  O  O     . ASP A 1 631 ? 141.403 113.374 93.295  1.00 46.48 ?  631 ASP A O     1 
ATOM   5077  C  CB    . ASP A 1 631 ? 138.447 113.141 93.447  1.00 42.42 ?  631 ASP A CB    1 
ATOM   5078  C  CG    . ASP A 1 631 ? 137.090 112.714 93.967  1.00 49.41 ?  631 ASP A CG    1 
ATOM   5079  O  OD1   . ASP A 1 631 ? 137.037 112.040 95.016  1.00 48.62 ?  631 ASP A OD1   1 
ATOM   5080  O  OD2   . ASP A 1 631 ? 136.075 113.049 93.322  1.00 51.07 -1 631 ASP A OD2   1 
ATOM   5081  N  N     . MET A 1 632 ? 140.973 115.408 94.142  1.00 39.69 ?  632 MET A N     1 
ATOM   5082  C  CA    . MET A 1 632 ? 142.129 116.023 93.512  1.00 37.62 ?  632 MET A CA    1 
ATOM   5083  C  C     . MET A 1 632 ? 143.290 116.150 94.490  1.00 36.03 ?  632 MET A C     1 
ATOM   5084  O  O     . MET A 1 632 ? 143.123 116.089 95.710  1.00 38.98 ?  632 MET A O     1 
ATOM   5085  C  CB    . MET A 1 632 ? 141.780 117.399 92.942  1.00 37.51 ?  632 MET A CB    1 
ATOM   5086  C  CG    . MET A 1 632 ? 140.833 118.224 93.773  1.00 39.98 ?  632 MET A CG    1 
ATOM   5087  S  SD    . MET A 1 632 ? 140.583 119.855 93.053  1.00 47.46 ?  632 MET A SD    1 
ATOM   5088  C  CE    . MET A 1 632 ? 139.459 119.471 91.716  1.00 33.77 ?  632 MET A CE    1 
ATOM   5089  N  N     . ASP A 1 633 ? 144.481 116.328 93.926  1.00 34.02 ?  633 ASP A N     1 
ATOM   5090  C  CA    . ASP A 1 633 ? 145.692 116.489 94.720  1.00 30.19 ?  633 ASP A CA    1 
ATOM   5091  C  C     . ASP A 1 633 ? 145.682 117.847 95.409  1.00 28.33 ?  633 ASP A C     1 
ATOM   5092  O  O     . ASP A 1 633 ? 145.542 118.884 94.752  1.00 30.74 ?  633 ASP A O     1 
ATOM   5093  C  CB    . ASP A 1 633 ? 146.921 116.350 93.825  1.00 26.25 ?  633 ASP A CB    1 
ATOM   5094  C  CG    . ASP A 1 633 ? 148.204 116.184 94.613  1.00 38.00 ?  633 ASP A CG    1 
ATOM   5095  O  OD1   . ASP A 1 633 ? 148.139 116.078 95.856  1.00 39.38 ?  633 ASP A OD1   1 
ATOM   5096  O  OD2   . ASP A 1 633 ? 149.283 116.164 93.986  1.00 36.15 -1 633 ASP A OD2   1 
ATOM   5097  N  N     . MET A 1 634 ? 145.830 117.844 96.735  1.00 26.57 ?  634 MET A N     1 
ATOM   5098  C  CA    . MET A 1 634 ? 145.890 119.100 97.472  1.00 23.16 ?  634 MET A CA    1 
ATOM   5099  C  C     . MET A 1 634 ? 147.151 119.893 97.162  1.00 25.24 ?  634 MET A C     1 
ATOM   5100  O  O     . MET A 1 634 ? 147.173 121.104 97.392  1.00 26.06 ?  634 MET A O     1 
ATOM   5101  C  CB    . MET A 1 634 ? 145.792 118.842 98.975  1.00 23.97 ?  634 MET A CB    1 
ATOM   5102  C  CG    . MET A 1 634 ? 144.367 118.724 99.483  1.00 29.04 ?  634 MET A CG    1 
ATOM   5103  S  SD    . MET A 1 634 ? 143.358 120.147 99.025  1.00 38.84 ?  634 MET A SD    1 
ATOM   5104  C  CE    . MET A 1 634 ? 142.135 119.366 97.977  1.00 28.17 ?  634 MET A CE    1 
ATOM   5105  N  N     . PHE A 1 635 ? 148.197 119.244 96.645  1.00 24.58 ?  635 PHE A N     1 
ATOM   5106  C  CA    . PHE A 1 635 ? 149.379 119.986 96.221  1.00 21.50 ?  635 PHE A CA    1 
ATOM   5107  C  C     . PHE A 1 635 ? 149.068 120.879 95.026  1.00 21.21 ?  635 PHE A C     1 
ATOM   5108  O  O     . PHE A 1 635 ? 149.525 122.025 94.964  1.00 26.87 ?  635 PHE A O     1 
ATOM   5109  C  CB    . PHE A 1 635 ? 150.517 119.019 95.896  1.00 20.93 ?  635 PHE A CB    1 
ATOM   5110  C  CG    . PHE A 1 635 ? 151.368 118.665 97.082  1.00 27.72 ?  635 PHE A CG    1 
ATOM   5111  C  CD1   . PHE A 1 635 ? 150.796 118.466 98.327  1.00 22.95 ?  635 PHE A CD1   1 
ATOM   5112  C  CD2   . PHE A 1 635 ? 152.739 118.537 96.954  1.00 23.97 ?  635 PHE A CD2   1 
ATOM   5113  C  CE1   . PHE A 1 635 ? 151.576 118.145 99.419  1.00 23.47 ?  635 PHE A CE1   1 
ATOM   5114  C  CE2   . PHE A 1 635 ? 153.523 118.216 98.044  1.00 26.52 ?  635 PHE A CE2   1 
ATOM   5115  C  CZ    . PHE A 1 635 ? 152.939 118.019 99.277  1.00 24.17 ?  635 PHE A CZ    1 
ATOM   5116  N  N     . LYS A 1 636 ? 148.272 120.382 94.078  1.00 26.05 ?  636 LYS A N     1 
ATOM   5117  C  CA    . LYS A 1 636 ? 147.902 121.199 92.927  1.00 24.89 ?  636 LYS A CA    1 
ATOM   5118  C  C     . LYS A 1 636 ? 146.925 122.304 93.314  1.00 23.61 ?  636 LYS A C     1 
ATOM   5119  O  O     . LYS A 1 636 ? 146.978 123.404 92.752  1.00 31.09 ?  636 LYS A O     1 
ATOM   5120  C  CB    . LYS A 1 636 ? 147.318 120.315 91.828  1.00 27.32 ?  636 LYS A CB    1 
ATOM   5121  C  CG    . LYS A 1 636 ? 148.293 119.261 91.324  1.00 27.16 ?  636 LYS A CG    1 
ATOM   5122  C  CD    . LYS A 1 636 ? 148.352 119.228 89.810  1.00 30.50 ?  636 LYS A CD    1 
ATOM   5123  C  CE    . LYS A 1 636 ? 148.181 117.815 89.281  1.00 32.33 ?  636 LYS A CE    1 
ATOM   5124  N  NZ    . LYS A 1 636 ? 148.335 117.758 87.802  1.00 32.76 1  636 LYS A NZ    1 
ATOM   5125  N  N     . VAL A 1 637 ? 146.041 122.042 94.279  1.00 20.12 ?  637 VAL A N     1 
ATOM   5126  C  CA    . VAL A 1 637 ? 145.170 123.098 94.787  1.00 17.76 ?  637 VAL A CA    1 
ATOM   5127  C  C     . VAL A 1 637 ? 145.991 124.161 95.507  1.00 23.34 ?  637 VAL A C     1 
ATOM   5128  O  O     . VAL A 1 637 ? 145.710 125.361 95.399  1.00 26.50 ?  637 VAL A O     1 
ATOM   5129  C  CB    . VAL A 1 637 ? 144.083 122.499 95.698  1.00 21.56 ?  637 VAL A CB    1 
ATOM   5130  C  CG1   . VAL A 1 637 ? 143.113 123.578 96.151  1.00 23.10 ?  637 VAL A CG1   1 
ATOM   5131  C  CG2   . VAL A 1 637 ? 143.344 121.386 94.977  1.00 24.87 ?  637 VAL A CG2   1 
ATOM   5132  N  N     . VAL A 1 638 ? 147.018 123.741 96.251  1.00 26.37 ?  638 VAL A N     1 
ATOM   5133  C  CA    . VAL A 1 638 ? 147.927 124.693 96.880  1.00 21.65 ?  638 VAL A CA    1 
ATOM   5134  C  C     . VAL A 1 638 ? 148.639 125.519 95.819  1.00 18.06 ?  638 VAL A C     1 
ATOM   5135  O  O     . VAL A 1 638 ? 148.811 126.732 95.969  1.00 31.86 ?  638 VAL A O     1 
ATOM   5136  C  CB    . VAL A 1 638 ? 148.932 123.959 97.788  1.00 21.89 ?  638 VAL A CB    1 
ATOM   5137  C  CG1   . VAL A 1 638 ? 150.159 124.820 98.030  1.00 15.98 ?  638 VAL A CG1   1 
ATOM   5138  C  CG2   . VAL A 1 638 ? 148.286 123.576 99.103  1.00 22.01 ?  638 VAL A CG2   1 
ATOM   5139  N  N     . ASP A 1 639 ? 149.068 124.872 94.735  1.00 13.54 ?  639 ASP A N     1 
ATOM   5140  C  CA    . ASP A 1 639 ? 149.704 125.594 93.638  1.00 16.83 ?  639 ASP A CA    1 
ATOM   5141  C  C     . ASP A 1 639 ? 148.764 126.639 93.051  1.00 24.01 ?  639 ASP A C     1 
ATOM   5142  O  O     . ASP A 1 639 ? 149.174 127.774 92.783  1.00 29.17 ?  639 ASP A O     1 
ATOM   5143  C  CB    . ASP A 1 639 ? 150.150 124.611 92.557  1.00 15.86 ?  639 ASP A CB    1 
ATOM   5144  C  CG    . ASP A 1 639 ? 151.394 123.843 92.943  1.00 29.95 ?  639 ASP A CG    1 
ATOM   5145  O  OD1   . ASP A 1 639 ? 152.289 124.438 93.579  1.00 34.26 ?  639 ASP A OD1   1 
ATOM   5146  O  OD2   . ASP A 1 639 ? 151.478 122.641 92.616  1.00 34.71 -1 639 ASP A OD2   1 
ATOM   5147  N  N     . MET A 1 640 ? 147.496 126.277 92.858  1.00 23.60 ?  640 MET A N     1 
ATOM   5148  C  CA    . MET A 1 640 ? 146.526 127.221 92.310  1.00 21.42 ?  640 MET A CA    1 
ATOM   5149  C  C     . MET A 1 640 ? 146.300 128.398 93.255  1.00 22.11 ?  640 MET A C     1 
ATOM   5150  O  O     . MET A 1 640 ? 146.290 129.561 92.830  1.00 25.58 ?  640 MET A O     1 
ATOM   5151  C  CB    . MET A 1 640 ? 145.210 126.499 92.023  1.00 24.83 ?  640 MET A CB    1 
ATOM   5152  C  CG    . MET A 1 640 ? 144.024 127.421 91.812  1.00 24.53 ?  640 MET A CG    1 
ATOM   5153  S  SD    . MET A 1 640 ? 144.093 128.290 90.239  1.00 27.79 ?  640 MET A SD    1 
ATOM   5154  C  CE    . MET A 1 640 ? 143.078 127.225 89.226  1.00 26.13 ?  640 MET A CE    1 
ATOM   5155  N  N     . ILE A 1 641 ? 146.125 128.115 94.547  1.00 21.70 ?  641 ILE A N     1 
ATOM   5156  C  CA    . ILE A 1 641 ? 145.857 129.179 95.508  1.00 16.23 ?  641 ILE A CA    1 
ATOM   5157  C  C     . ILE A 1 641 ? 147.071 130.087 95.655  1.00 18.08 ?  641 ILE A C     1 
ATOM   5158  O  O     . ILE A 1 641 ? 146.936 131.304 95.819  1.00 25.78 ?  641 ILE A O     1 
ATOM   5159  C  CB    . ILE A 1 641 ? 145.413 128.584 96.857  1.00 24.77 ?  641 ILE A CB    1 
ATOM   5160  C  CG1   . ILE A 1 641 ? 144.149 127.744 96.679  1.00 23.13 ?  641 ILE A CG1   1 
ATOM   5161  C  CG2   . ILE A 1 641 ? 145.152 129.683 97.873  1.00 16.45 ?  641 ILE A CG2   1 
ATOM   5162  C  CD1   . ILE A 1 641 ? 143.059 128.437 95.896  1.00 19.77 ?  641 ILE A CD1   1 
ATOM   5163  N  N     . ALA A 1 642 ? 148.276 129.516 95.590  1.00 13.80 ?  642 ALA A N     1 
ATOM   5164  C  CA    . ALA A 1 642 ? 149.486 130.323 95.653  1.00 14.95 ?  642 ALA A CA    1 
ATOM   5165  C  C     . ALA A 1 642 ? 149.667 131.159 94.395  1.00 15.06 ?  642 ALA A C     1 
ATOM   5166  O  O     . ALA A 1 642 ? 150.194 132.275 94.465  1.00 24.85 ?  642 ALA A O     1 
ATOM   5167  C  CB    . ALA A 1 642 ? 150.702 129.426 95.875  1.00 16.20 ?  642 ALA A CB    1 
ATOM   5168  N  N     . THR A 1 643 ? 149.252 130.637 93.240  1.00 17.82 ?  643 THR A N     1 
ATOM   5169  C  CA    . THR A 1 643 ? 149.254 131.443 92.026  1.00 20.13 ?  643 THR A CA    1 
ATOM   5170  C  C     . THR A 1 643 ? 148.300 132.622 92.154  1.00 18.40 ?  643 THR A C     1 
ATOM   5171  O  O     . THR A 1 643 ? 148.632 133.747 91.767  1.00 22.42 ?  643 THR A O     1 
ATOM   5172  C  CB    . THR A 1 643 ? 148.886 130.578 90.822  1.00 22.01 ?  643 THR A CB    1 
ATOM   5173  O  OG1   . THR A 1 643 ? 149.898 129.584 90.621  1.00 28.71 ?  643 THR A OG1   1 
ATOM   5174  C  CG2   . THR A 1 643 ? 148.768 131.426 89.571  1.00 17.65 ?  643 THR A CG2   1 
ATOM   5175  N  N     . ILE A 1 644 ? 147.109 132.385 92.706  1.00 16.05 ?  644 ILE A N     1 
ATOM   5176  C  CA    . ILE A 1 644 ? 146.169 133.480 92.919  1.00 14.62 ?  644 ILE A CA    1 
ATOM   5177  C  C     . ILE A 1 644 ? 146.670 134.414 94.015  1.00 17.27 ?  644 ILE A C     1 
ATOM   5178  O  O     . ILE A 1 644 ? 146.527 135.638 93.917  1.00 22.60 ?  644 ILE A O     1 
ATOM   5179  C  CB    . ILE A 1 644 ? 144.768 132.931 93.239  1.00 15.77 ?  644 ILE A CB    1 
ATOM   5180  C  CG1   . ILE A 1 644 ? 144.254 132.066 92.089  1.00 14.71 ?  644 ILE A CG1   1 
ATOM   5181  C  CG2   . ILE A 1 644 ? 143.802 134.065 93.507  1.00 7.74  ?  644 ILE A CG2   1 
ATOM   5182  C  CD1   . ILE A 1 644 ? 143.074 131.204 92.463  1.00 22.09 ?  644 ILE A CD1   1 
ATOM   5183  N  N     . GLN A 1 645 ? 147.271 133.854 95.071  1.00 11.57 ?  645 GLN A N     1 
ATOM   5184  C  CA    . GLN A 1 645 ? 147.649 134.652 96.233  1.00 11.89 ?  645 GLN A CA    1 
ATOM   5185  C  C     . GLN A 1 645 ? 148.690 135.712 95.894  1.00 18.71 ?  645 GLN A C     1 
ATOM   5186  O  O     . GLN A 1 645 ? 148.741 136.759 96.548  1.00 23.96 ?  645 GLN A O     1 
ATOM   5187  C  CB    . GLN A 1 645 ? 148.167 133.740 97.346  1.00 8.94  ?  645 GLN A CB    1 
ATOM   5188  C  CG    . GLN A 1 645 ? 148.515 134.456 98.642  1.00 10.21 ?  645 GLN A CG    1 
ATOM   5189  C  CD    . GLN A 1 645 ? 147.309 135.087 99.301  1.00 12.21 ?  645 GLN A CD    1 
ATOM   5190  O  OE1   . GLN A 1 645 ? 146.584 134.432 100.048 1.00 18.33 ?  645 GLN A OE1   1 
ATOM   5191  N  NE2   . GLN A 1 645 ? 147.088 136.366 99.031  1.00 4.73  ?  645 GLN A NE2   1 
ATOM   5192  N  N     . GLN A 1 646 ? 149.518 135.471 94.880  1.00 20.94 ?  646 GLN A N     1 
ATOM   5193  C  CA    . GLN A 1 646 ? 150.557 136.434 94.540  1.00 14.79 ?  646 GLN A CA    1 
ATOM   5194  C  C     . GLN A 1 646 ? 150.001 137.736 93.979  1.00 15.69 ?  646 GLN A C     1 
ATOM   5195  O  O     . GLN A 1 646 ? 150.736 138.726 93.921  1.00 20.87 ?  646 GLN A O     1 
ATOM   5196  C  CB    . GLN A 1 646 ? 151.543 135.812 93.551  1.00 20.94 ?  646 GLN A CB    1 
ATOM   5197  C  CG    . GLN A 1 646 ? 151.093 135.837 92.108  1.00 22.21 ?  646 GLN A CG    1 
ATOM   5198  C  CD    . GLN A 1 646 ? 152.032 135.073 91.199  1.00 30.10 ?  646 GLN A CD    1 
ATOM   5199  O  OE1   . GLN A 1 646 ? 151.643 134.090 90.570  1.00 25.03 ?  646 GLN A OE1   1 
ATOM   5200  N  NE2   . GLN A 1 646 ? 153.279 135.521 91.127  1.00 26.74 ?  646 GLN A NE2   1 
ATOM   5201  N  N     . HIS A 1 647 ? 148.730 137.766 93.584  1.00 21.92 ?  647 HIS A N     1 
ATOM   5202  C  CA    . HIS A 1 647 ? 148.083 138.982 93.118  1.00 14.76 ?  647 HIS A CA    1 
ATOM   5203  C  C     . HIS A 1 647 ? 147.068 139.529 94.111  1.00 15.27 ?  647 HIS A C     1 
ATOM   5204  O  O     . HIS A 1 647 ? 146.419 140.538 93.821  1.00 25.12 ?  647 HIS A O     1 
ATOM   5205  C  CB    . HIS A 1 647 ? 147.400 138.731 91.770  1.00 11.36 ?  647 HIS A CB    1 
ATOM   5206  C  CG    . HIS A 1 647 ? 148.301 138.123 90.744  1.00 16.48 ?  647 HIS A CG    1 
ATOM   5207  N  ND1   . HIS A 1 647 ? 149.441 138.749 90.291  1.00 19.03 ?  647 HIS A ND1   1 
ATOM   5208  C  CD2   . HIS A 1 647 ? 148.232 136.943 90.084  1.00 17.59 ?  647 HIS A CD2   1 
ATOM   5209  C  CE1   . HIS A 1 647 ? 150.037 137.982 89.396  1.00 20.83 ?  647 HIS A CE1   1 
ATOM   5210  N  NE2   . HIS A 1 647 ? 149.322 136.881 89.251  1.00 20.71 ?  647 HIS A NE2   1 
ATOM   5211  N  N     . ILE A 1 648 ? 146.914 138.892 95.267  1.00 13.52 ?  648 ILE A N     1 
ATOM   5212  C  CA    . ILE A 1 648 ? 145.950 139.295 96.283  1.00 12.03 ?  648 ILE A CA    1 
ATOM   5213  C  C     . ILE A 1 648 ? 146.731 139.864 97.457  1.00 12.20 ?  648 ILE A C     1 
ATOM   5214  O  O     . ILE A 1 648 ? 147.618 139.195 98.003  1.00 25.66 ?  648 ILE A O     1 
ATOM   5215  C  CB    . ILE A 1 648 ? 145.067 138.115 96.717  1.00 10.19 ?  648 ILE A CB    1 
ATOM   5216  C  CG1   . ILE A 1 648 ? 144.346 137.507 95.511  1.00 11.20 ?  648 ILE A CG1   1 
ATOM   5217  C  CG2   . ILE A 1 648 ? 144.056 138.551 97.760  1.00 5.66  ?  648 ILE A CG2   1 
ATOM   5218  C  CD1   . ILE A 1 648 ? 143.253 138.380 94.944  1.00 5.31  ?  648 ILE A CD1   1 
ATOM   5219  N  N     . ASP A 1 649 ? 146.414 141.102 97.845  1.00 7.57  ?  649 ASP A N     1 
ATOM   5220  C  CA    . ASP A 1 649 ? 147.163 141.741 98.923  1.00 8.07  ?  649 ASP A CA    1 
ATOM   5221  C  C     . ASP A 1 649 ? 146.810 141.149 100.280 1.00 9.20  ?  649 ASP A C     1 
ATOM   5222  O  O     . ASP A 1 649 ? 147.681 141.028 101.148 1.00 27.02 ?  649 ASP A O     1 
ATOM   5223  C  CB    . ASP A 1 649 ? 146.922 143.250 98.921  1.00 18.44 ?  649 ASP A CB    1 
ATOM   5224  C  CG    . ASP A 1 649 ? 145.468 143.608 98.716  1.00 19.25 ?  649 ASP A CG    1 
ATOM   5225  O  OD1   . ASP A 1 649 ? 145.009 143.583 97.559  1.00 24.05 ?  649 ASP A OD1   1 
ATOM   5226  O  OD2   . ASP A 1 649 ? 144.785 143.922 99.711  1.00 20.27 -1 649 ASP A OD2   1 
ATOM   5227  N  N     . GLN A 1 650 ? 145.550 140.797 100.486 1.00 13.71 ?  650 GLN A N     1 
ATOM   5228  C  CA    . GLN A 1 650 ? 145.118 140.087 101.678 1.00 4.37  ?  650 GLN A CA    1 
ATOM   5229  C  C     . GLN A 1 650 ? 145.168 138.585 101.392 1.00 10.77 ?  650 GLN A C     1 
ATOM   5230  O  O     . GLN A 1 650 ? 145.777 138.150 100.412 1.00 20.19 ?  650 GLN A O     1 
ATOM   5231  C  CB    . GLN A 1 650 ? 143.739 140.588 102.108 1.00 6.40  ?  650 GLN A CB    1 
ATOM   5232  C  CG    . GLN A 1 650 ? 143.693 142.082 102.371 1.00 9.80  ?  650 GLN A CG    1 
ATOM   5233  C  CD    . GLN A 1 650 ? 142.359 142.533 102.917 1.00 13.56 ?  650 GLN A CD    1 
ATOM   5234  O  OE1   . GLN A 1 650 ? 142.016 142.239 104.059 1.00 15.64 ?  650 GLN A OE1   1 
ATOM   5235  N  NE2   . GLN A 1 650 ? 141.599 143.255 102.105 1.00 3.67  ?  650 GLN A NE2   1 
ATOM   5236  N  N     . GLY A 1 651 ? 144.562 137.771 102.253 1.00 9.85  ?  651 GLY A N     1 
ATOM   5237  C  CA    . GLY A 1 651 ? 144.613 136.334 102.114 1.00 5.75  ?  651 GLY A CA    1 
ATOM   5238  C  C     . GLY A 1 651 ? 143.432 135.757 101.349 1.00 5.51  ?  651 GLY A C     1 
ATOM   5239  O  O     . GLY A 1 651 ? 142.537 136.455 100.880 1.00 10.85 ?  651 GLY A O     1 
ATOM   5240  N  N     . ILE A 1 652 ? 143.460 134.434 101.229 1.00 13.76 ?  652 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 652 ? 142.424 133.658 100.560 1.00 2.10  ?  652 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 652 ? 141.963 132.577 101.524 1.00 12.29 ?  652 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 652 ? 142.790 131.857 102.091 1.00 26.74 ?  652 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 652 ? 142.939 133.030 99.251  1.00 6.19  ?  652 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 652 ? 143.544 134.099 98.340  1.00 4.30  ?  652 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 652 ? 141.829 132.280 98.543  1.00 11.90 ?  652 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 652 ? 144.135 133.546 97.074  1.00 5.06  ?  652 ILE A CD1   1 
ATOM   5248  N  N     . SER A 1 653 ? 140.653 132.464 101.713 1.00 10.56 ?  653 SER A N     1 
ATOM   5249  C  CA    . SER A 1 653 ? 140.097 131.439 102.593 1.00 12.86 ?  653 SER A CA    1 
ATOM   5250  C  C     . SER A 1 653 ? 140.316 130.080 101.946 1.00 18.04 ?  653 SER A C     1 
ATOM   5251  O  O     . SER A 1 653 ? 139.556 129.664 101.072 1.00 20.45 ?  653 SER A O     1 
ATOM   5252  C  CB    . SER A 1 653 ? 138.618 131.697 102.847 1.00 13.46 ?  653 SER A CB    1 
ATOM   5253  O  OG    . SER A 1 653 ? 138.424 132.393 104.060 1.00 20.71 ?  653 SER A OG    1 
ATOM   5254  N  N     . PHE A 1 654 ? 141.351 129.375 102.390 1.00 22.22 ?  654 PHE A N     1 
ATOM   5255  C  CA    . PHE A 1 654 ? 141.826 128.160 101.739 1.00 10.48 ?  654 PHE A CA    1 
ATOM   5256  C  C     . PHE A 1 654 ? 141.404 126.954 102.569 1.00 13.54 ?  654 PHE A C     1 
ATOM   5257  O  O     . PHE A 1 654 ? 142.000 126.670 103.614 1.00 21.98 ?  654 PHE A O     1 
ATOM   5258  C  CB    . PHE A 1 654 ? 143.342 128.214 101.569 1.00 15.97 ?  654 PHE A CB    1 
ATOM   5259  C  CG    . PHE A 1 654 ? 143.912 127.075 100.777 1.00 16.96 ?  654 PHE A CG    1 
ATOM   5260  C  CD1   . PHE A 1 654 ? 143.104 126.287 99.978  1.00 18.84 ?  654 PHE A CD1   1 
ATOM   5261  C  CD2   . PHE A 1 654 ? 145.265 126.800 100.829 1.00 21.85 ?  654 PHE A CD2   1 
ATOM   5262  C  CE1   . PHE A 1 654 ? 143.634 125.246 99.254  1.00 18.09 ?  654 PHE A CE1   1 
ATOM   5263  C  CE2   . PHE A 1 654 ? 145.797 125.761 100.104 1.00 21.06 ?  654 PHE A CE2   1 
ATOM   5264  C  CZ    . PHE A 1 654 ? 144.981 124.982 99.315  1.00 19.78 ?  654 PHE A CZ    1 
ATOM   5265  N  N     . THR A 1 655 ? 140.392 126.237 102.093 1.00 22.24 ?  655 THR A N     1 
ATOM   5266  C  CA    . THR A 1 655 ? 139.928 125.018 102.738 1.00 23.33 ?  655 THR A CA    1 
ATOM   5267  C  C     . THR A 1 655 ? 140.694 123.822 102.190 1.00 26.54 ?  655 THR A C     1 
ATOM   5268  O  O     . THR A 1 655 ? 140.876 123.695 100.975 1.00 26.35 ?  655 THR A O     1 
ATOM   5269  C  CB    . THR A 1 655 ? 138.426 124.831 102.518 1.00 23.96 ?  655 THR A CB    1 
ATOM   5270  O  OG1   . THR A 1 655 ? 137.716 125.912 103.132 1.00 31.72 ?  655 THR A OG1   1 
ATOM   5271  C  CG2   . THR A 1 655 ? 137.957 123.520 103.123 1.00 26.42 ?  655 THR A CG2   1 
ATOM   5272  N  N     . LEU A 1 656 ? 141.149 122.951 103.087 1.00 29.51 ?  656 LEU A N     1 
ATOM   5273  C  CA    . LEU A 1 656 ? 141.805 121.712 102.699 1.00 29.05 ?  656 LEU A CA    1 
ATOM   5274  C  C     . LEU A 1 656 ? 140.786 120.584 102.672 1.00 28.32 ?  656 LEU A C     1 
ATOM   5275  O  O     . LEU A 1 656 ? 140.095 120.337 103.665 1.00 28.78 ?  656 LEU A O     1 
ATOM   5276  C  CB    . LEU A 1 656 ? 142.944 121.371 103.660 1.00 29.85 ?  656 LEU A CB    1 
ATOM   5277  C  CG    . LEU A 1 656 ? 144.146 122.311 103.641 1.00 32.35 ?  656 LEU A CG    1 
ATOM   5278  C  CD1   . LEU A 1 656 ? 145.282 121.731 104.463 1.00 29.79 ?  656 LEU A CD1   1 
ATOM   5279  C  CD2   . LEU A 1 656 ? 144.595 122.591 102.217 1.00 27.79 ?  656 LEU A CD2   1 
ATOM   5280  N  N     . PHE A 1 657 ? 140.700 119.900 101.538 1.00 27.28 ?  657 PHE A N     1 
ATOM   5281  C  CA    . PHE A 1 657 ? 139.732 118.833 101.331 1.00 27.17 ?  657 PHE A CA    1 
ATOM   5282  C  C     . PHE A 1 657 ? 140.465 117.501 101.419 1.00 34.16 ?  657 PHE A C     1 
ATOM   5283  O  O     . PHE A 1 657 ? 141.220 117.137 100.513 1.00 37.77 ?  657 PHE A O     1 
ATOM   5284  C  CB    . PHE A 1 657 ? 139.031 119.006 99.987  1.00 28.61 ?  657 PHE A CB    1 
ATOM   5285  C  CG    . PHE A 1 657 ? 138.408 120.358 99.810  1.00 33.56 ?  657 PHE A CG    1 
ATOM   5286  C  CD1   . PHE A 1 657 ? 137.124 120.607 100.260 1.00 30.41 ?  657 PHE A CD1   1 
ATOM   5287  C  CD2   . PHE A 1 657 ? 139.113 121.388 99.207  1.00 34.59 ?  657 PHE A CD2   1 
ATOM   5288  C  CE1   . PHE A 1 657 ? 136.550 121.851 100.101 1.00 33.52 ?  657 PHE A CE1   1 
ATOM   5289  C  CE2   . PHE A 1 657 ? 138.542 122.634 99.045  1.00 30.81 ?  657 PHE A CE2   1 
ATOM   5290  C  CZ    . PHE A 1 657 ? 137.259 122.865 99.496  1.00 32.22 ?  657 PHE A CZ    1 
ATOM   5291  N  N     . LEU A 1 658 ? 140.235 116.778 102.510 1.00 42.10 ?  658 LEU A N     1 
ATOM   5292  C  CA    . LEU A 1 658 ? 141.003 115.590 102.851 1.00 40.48 ?  658 LEU A CA    1 
ATOM   5293  C  C     . LEU A 1 658 ? 140.138 114.343 102.745 1.00 44.65 ?  658 LEU A C     1 
ATOM   5294  O  O     . LEU A 1 658 ? 138.956 114.362 103.097 1.00 48.50 ?  658 LEU A O     1 
ATOM   5295  C  CB    . LEU A 1 658 ? 141.566 115.703 104.269 1.00 38.92 ?  658 LEU A CB    1 
ATOM   5296  C  CG    . LEU A 1 658 ? 142.019 117.093 104.713 1.00 38.09 ?  658 LEU A CG    1 
ATOM   5297  C  CD1   . LEU A 1 658 ? 142.162 117.135 106.221 1.00 37.57 ?  658 LEU A CD1   1 
ATOM   5298  C  CD2   . LEU A 1 658 ? 143.325 117.471 104.038 1.00 39.85 ?  658 LEU A CD2   1 
ATOM   5299  N  N     . LYS A 1 659 ? 140.732 113.264 102.247 1.00 48.81 ?  659 LYS A N     1 
ATOM   5300  C  CA    . LYS A 1 659 ? 140.079 111.966 102.293 1.00 49.27 ?  659 LYS A CA    1 
ATOM   5301  C  C     . LYS A 1 659 ? 140.299 111.315 103.656 1.00 49.70 ?  659 LYS A C     1 
ATOM   5302  O  O     . LYS A 1 659 ? 141.173 111.710 104.430 1.00 53.26 ?  659 LYS A O     1 
ATOM   5303  C  CB    . LYS A 1 659 ? 140.603 111.055 101.183 1.00 50.47 ?  659 LYS A CB    1 
ATOM   5304  C  CG    . LYS A 1 659 ? 140.131 111.438 99.793  1.00 50.24 ?  659 LYS A CG    1 
ATOM   5305  C  CD    . LYS A 1 659 ? 140.504 110.374 98.776  1.00 50.40 ?  659 LYS A CD    1 
ATOM   5306  C  CE    . LYS A 1 659 ? 139.950 110.708 97.401  1.00 49.54 ?  659 LYS A CE    1 
ATOM   5307  N  NZ    . LYS A 1 659 ? 139.938 109.522 96.503  1.00 49.60 1  659 LYS A NZ    1 
ATOM   5308  N  N     . ASP A 1 660 ? 139.478 110.306 103.948 1.00 56.54 ?  660 ASP A N     1 
ATOM   5309  C  CA    . ASP A 1 660 ? 139.643 109.555 105.186 1.00 56.20 ?  660 ASP A CA    1 
ATOM   5310  C  C     . ASP A 1 660 ? 140.926 108.736 105.199 1.00 56.75 ?  660 ASP A C     1 
ATOM   5311  O  O     . ASP A 1 660 ? 141.462 108.462 106.277 1.00 56.19 ?  660 ASP A O     1 
ATOM   5312  C  CB    . ASP A 1 660 ? 138.441 108.637 105.408 1.00 57.79 ?  660 ASP A CB    1 
ATOM   5313  C  CG    . ASP A 1 660 ? 137.457 109.197 106.415 1.00 58.39 ?  660 ASP A CG    1 
ATOM   5314  O  OD1   . ASP A 1 660 ? 136.395 108.574 106.621 1.00 57.17 ?  660 ASP A OD1   1 
ATOM   5315  O  OD2   . ASP A 1 660 ? 137.749 110.256 107.005 1.00 56.44 -1 660 ASP A OD2   1 
ATOM   5316  N  N     . THR A 1 661 ? 141.429 108.345 104.025 1.00 54.72 ?  661 THR A N     1 
ATOM   5317  C  CA    . THR A 1 661 ? 142.592 107.467 103.965 1.00 54.28 ?  661 THR A CA    1 
ATOM   5318  C  C     . THR A 1 661 ? 143.869 108.166 104.416 1.00 54.79 ?  661 THR A C     1 
ATOM   5319  O  O     . THR A 1 661 ? 144.737 107.527 105.025 1.00 57.02 ?  661 THR A O     1 
ATOM   5320  C  CB    . THR A 1 661 ? 142.768 106.927 102.546 1.00 55.29 ?  661 THR A CB    1 
ATOM   5321  O  OG1   . THR A 1 661 ? 142.409 107.943 101.600 1.00 55.34 ?  661 THR A OG1   1 
ATOM   5322  C  CG2   . THR A 1 661 ? 141.887 105.707 102.331 1.00 54.88 ?  661 THR A CG2   1 
ATOM   5323  N  N     . MET A 1 662 ? 144.012 109.457 104.132 1.00 53.00 ?  662 MET A N     1 
ATOM   5324  C  CA    . MET A 1 662 ? 145.258 110.153 104.422 1.00 52.79 ?  662 MET A CA    1 
ATOM   5325  C  C     . MET A 1 662 ? 145.417 110.382 105.920 1.00 51.88 ?  662 MET A C     1 
ATOM   5326  O  O     . MET A 1 662 ? 144.444 110.638 106.635 1.00 52.12 ?  662 MET A O     1 
ATOM   5327  C  CB    . MET A 1 662 ? 145.321 111.484 103.670 1.00 51.51 ?  662 MET A CB    1 
ATOM   5328  C  CG    . MET A 1 662 ? 144.229 112.474 104.013 1.00 52.69 ?  662 MET A CG    1 
ATOM   5329  S  SD    . MET A 1 662 ? 144.361 113.991 103.045 1.00 60.26 ?  662 MET A SD    1 
ATOM   5330  C  CE    . MET A 1 662 ? 145.226 113.407 101.590 1.00 49.12 ?  662 MET A CE    1 
ATOM   5331  N  N     . THR A 1 663 ? 146.657 110.283 106.388 1.00 44.50 ?  663 THR A N     1 
ATOM   5332  C  CA    . THR A 1 663 ? 146.972 110.357 107.806 1.00 43.95 ?  663 THR A CA    1 
ATOM   5333  C  C     . THR A 1 663 ? 147.218 111.810 108.211 1.00 45.06 ?  663 THR A C     1 
ATOM   5334  O  O     . THR A 1 663 ? 147.007 112.740 107.431 1.00 48.51 ?  663 THR A O     1 
ATOM   5335  C  CB    . THR A 1 663 ? 148.181 109.479 108.120 1.00 43.10 ?  663 THR A CB    1 
ATOM   5336  O  OG1   . THR A 1 663 ? 149.365 110.099 107.602 1.00 41.26 ?  663 THR A OG1   1 
ATOM   5337  C  CG2   . THR A 1 663 ? 148.022 108.112 107.477 1.00 44.67 ?  663 THR A CG2   1 
ATOM   5338  N  N     . THR A 1 664 ? 147.665 112.017 109.452 1.00 39.46 ?  664 THR A N     1 
ATOM   5339  C  CA    . THR A 1 664 ? 148.052 113.360 109.871 1.00 41.82 ?  664 THR A CA    1 
ATOM   5340  C  C     . THR A 1 664 ? 149.341 113.801 109.192 1.00 40.57 ?  664 THR A C     1 
ATOM   5341  O  O     . THR A 1 664 ? 149.580 115.004 109.044 1.00 42.64 ?  664 THR A O     1 
ATOM   5342  C  CB    . THR A 1 664 ? 148.209 113.426 111.389 1.00 41.38 ?  664 THR A CB    1 
ATOM   5343  O  OG1   . THR A 1 664 ? 149.256 112.540 111.805 1.00 40.03 ?  664 THR A OG1   1 
ATOM   5344  C  CG2   . THR A 1 664 ? 146.912 113.037 112.081 1.00 39.88 ?  664 THR A CG2   1 
ATOM   5345  N  N     . ARG A 1 665 ? 150.179 112.848 108.780 1.00 39.85 ?  665 ARG A N     1 
ATOM   5346  C  CA    . ARG A 1 665 ? 151.393 113.197 108.051 1.00 38.49 ?  665 ARG A CA    1 
ATOM   5347  C  C     . ARG A 1 665 ? 151.064 113.839 106.712 1.00 41.53 ?  665 ARG A C     1 
ATOM   5348  O  O     . ARG A 1 665 ? 151.748 114.770 106.281 1.00 42.68 ?  665 ARG A O     1 
ATOM   5349  C  CB    . ARG A 1 665 ? 152.265 111.962 107.844 1.00 39.32 ?  665 ARG A CB    1 
ATOM   5350  C  CG    . ARG A 1 665 ? 153.558 112.250 107.105 1.00 37.71 ?  665 ARG A CG    1 
ATOM   5351  C  CD    . ARG A 1 665 ? 154.463 111.036 107.068 1.00 39.18 ?  665 ARG A CD    1 
ATOM   5352  N  NE    . ARG A 1 665 ? 155.540 111.187 106.098 1.00 41.76 ?  665 ARG A NE    1 
ATOM   5353  C  CZ    . ARG A 1 665 ? 155.390 111.082 104.784 1.00 45.20 ?  665 ARG A CZ    1 
ATOM   5354  N  NH1   . ARG A 1 665 ? 154.213 110.815 104.242 1.00 43.53 1  665 ARG A NH1   1 
ATOM   5355  N  NH2   . ARG A 1 665 ? 156.447 111.247 103.995 1.00 42.18 ?  665 ARG A NH2   1 
ATOM   5356  N  N     . ASP A 1 666 ? 150.025 113.350 106.032 1.00 38.83 ?  666 ASP A N     1 
ATOM   5357  C  CA    . ASP A 1 666 ? 149.631 113.952 104.762 1.00 35.10 ?  666 ASP A CA    1 
ATOM   5358  C  C     . ASP A 1 666 ? 149.113 115.371 104.957 1.00 37.66 ?  666 ASP A C     1 
ATOM   5359  O  O     . ASP A 1 666 ? 149.420 116.266 104.162 1.00 40.48 ?  666 ASP A O     1 
ATOM   5360  C  CB    . ASP A 1 666 ? 148.583 113.080 104.074 1.00 40.83 ?  666 ASP A CB    1 
ATOM   5361  C  CG    . ASP A 1 666 ? 149.122 111.716 103.693 1.00 45.35 ?  666 ASP A CG    1 
ATOM   5362  O  OD1   . ASP A 1 666 ? 150.226 111.653 103.112 1.00 45.48 ?  666 ASP A OD1   1 
ATOM   5363  O  OD2   . ASP A 1 666 ? 148.444 110.707 103.974 1.00 45.22 -1 666 ASP A OD2   1 
ATOM   5364  N  N     . LEU A 1 667 ? 148.325 115.597 106.012 1.00 36.21 ?  667 LEU A N     1 
ATOM   5365  C  CA    . LEU A 1 667 ? 147.857 116.945 106.310 1.00 31.15 ?  667 LEU A CA    1 
ATOM   5366  C  C     . LEU A 1 667 ? 149.028 117.864 106.636 1.00 29.82 ?  667 LEU A C     1 
ATOM   5367  O  O     . LEU A 1 667 ? 149.071 119.017 106.188 1.00 34.82 ?  667 LEU A O     1 
ATOM   5368  C  CB    . LEU A 1 667 ? 146.855 116.894 107.466 1.00 34.82 ?  667 LEU A CB    1 
ATOM   5369  C  CG    . LEU A 1 667 ? 146.217 118.158 108.053 1.00 36.50 ?  667 LEU A CG    1 
ATOM   5370  C  CD1   . LEU A 1 667 ? 146.018 119.242 107.005 1.00 35.38 ?  667 LEU A CD1   1 
ATOM   5371  C  CD2   . LEU A 1 667 ? 144.898 117.813 108.718 1.00 32.66 ?  667 LEU A CD2   1 
ATOM   5372  N  N     . ASN A 1 668 ? 149.998 117.364 107.404 1.00 32.07 ?  668 ASN A N     1 
ATOM   5373  C  CA    . ASN A 1 668 ? 151.182 118.158 107.717 1.00 26.94 ?  668 ASN A CA    1 
ATOM   5374  C  C     . ASN A 1 668 ? 151.991 118.462 106.463 1.00 26.92 ?  668 ASN A C     1 
ATOM   5375  O  O     . ASN A 1 668 ? 152.528 119.563 106.317 1.00 33.03 ?  668 ASN A O     1 
ATOM   5376  C  CB    . ASN A 1 668 ? 152.040 117.428 108.749 1.00 27.90 ?  668 ASN A CB    1 
ATOM   5377  C  CG    . ASN A 1 668 ? 151.744 117.868 110.165 1.00 30.77 ?  668 ASN A CG    1 
ATOM   5378  O  OD1   . ASN A 1 668 ? 151.231 118.961 110.393 1.00 31.97 ?  668 ASN A OD1   1 
ATOM   5379  N  ND2   . ASN A 1 668 ? 152.057 117.010 111.127 1.00 37.76 ?  668 ASN A ND2   1 
ATOM   5380  N  N     . ARG A 1 669 ? 152.098 117.494 105.552 1.00 30.35 ?  669 ARG A N     1 
ATOM   5381  C  CA    . ARG A 1 669 ? 152.801 117.725 104.295 1.00 31.14 ?  669 ARG A CA    1 
ATOM   5382  C  C     . ARG A 1 669 ? 152.098 118.783 103.460 1.00 27.39 ?  669 ARG A C     1 
ATOM   5383  O  O     . ARG A 1 669 ? 152.751 119.628 102.842 1.00 31.90 ?  669 ARG A O     1 
ATOM   5384  C  CB    . ARG A 1 669 ? 152.921 116.420 103.510 1.00 29.28 ?  669 ARG A CB    1 
ATOM   5385  C  CG    . ARG A 1 669 ? 154.020 115.498 103.992 1.00 31.02 ?  669 ARG A CG    1 
ATOM   5386  C  CD    . ARG A 1 669 ? 154.484 114.584 102.875 1.00 34.56 ?  669 ARG A CD    1 
ATOM   5387  N  NE    . ARG A 1 669 ? 155.397 115.256 101.960 1.00 33.91 ?  669 ARG A NE    1 
ATOM   5388  C  CZ    . ARG A 1 669 ? 155.312 115.198 100.638 1.00 33.75 ?  669 ARG A CZ    1 
ATOM   5389  N  NH1   . ARG A 1 669 ? 154.357 114.507 100.038 1.00 34.67 1  669 ARG A NH1   1 
ATOM   5390  N  NH2   . ARG A 1 669 ? 156.205 115.850 99.900  1.00 33.28 ?  669 ARG A NH2   1 
ATOM   5391  N  N     . ILE A 1 670 ? 150.765 118.748 103.422 1.00 23.06 ?  670 ILE A N     1 
ATOM   5392  C  CA    . ILE A 1 670 ? 150.020 119.776 102.699 1.00 27.95 ?  670 ILE A CA    1 
ATOM   5393  C  C     . ILE A 1 670 ? 150.260 121.144 103.326 1.00 30.84 ?  670 ILE A C     1 
ATOM   5394  O  O     . ILE A 1 670 ? 150.462 122.137 102.621 1.00 29.03 ?  670 ILE A O     1 
ATOM   5395  C  CB    . ILE A 1 670 ? 148.521 119.428 102.652 1.00 28.07 ?  670 ILE A CB    1 
ATOM   5396  C  CG1   . ILE A 1 670 ? 148.294 118.144 101.855 1.00 30.56 ?  670 ILE A CG1   1 
ATOM   5397  C  CG2   . ILE A 1 670 ? 147.729 120.565 102.031 1.00 27.64 ?  670 ILE A CG2   1 
ATOM   5398  C  CD1   . ILE A 1 670 ? 146.995 117.449 102.177 1.00 29.61 ?  670 ILE A CD1   1 
ATOM   5399  N  N     . ASP A 1 671 ? 150.249 121.215 104.660 1.00 28.70 ?  671 ASP A N     1 
ATOM   5400  C  CA    . ASP A 1 671 ? 150.497 122.484 105.340 1.00 22.91 ?  671 ASP A CA    1 
ATOM   5401  C  C     . ASP A 1 671 ? 151.902 123.007 105.053 1.00 23.48 ?  671 ASP A C     1 
ATOM   5402  O  O     . ASP A 1 671 ? 152.092 124.205 104.812 1.00 25.79 ?  671 ASP A O     1 
ATOM   5403  C  CB    . ASP A 1 671 ? 150.286 122.324 106.846 1.00 26.10 ?  671 ASP A CB    1 
ATOM   5404  C  CG    . ASP A 1 671 ? 148.869 121.917 107.198 1.00 37.56 ?  671 ASP A CG    1 
ATOM   5405  O  OD1   . ASP A 1 671 ? 147.943 122.255 106.433 1.00 36.26 ?  671 ASP A OD1   1 
ATOM   5406  O  OD2   . ASP A 1 671 ? 148.681 121.256 108.242 1.00 37.09 -1 671 ASP A OD2   1 
ATOM   5407  N  N     . LEU A 1 672 ? 152.897 122.120 105.065 1.00 25.36 ?  672 LEU A N     1 
ATOM   5408  C  CA    . LEU A 1 672 ? 154.272 122.540 104.816 1.00 19.20 ?  672 LEU A CA    1 
ATOM   5409  C  C     . LEU A 1 672 ? 154.489 122.932 103.361 1.00 19.80 ?  672 LEU A C     1 
ATOM   5410  O  O     . LEU A 1 672 ? 155.282 123.836 103.079 1.00 25.70 ?  672 LEU A O     1 
ATOM   5411  C  CB    . LEU A 1 672 ? 155.238 121.427 105.217 1.00 22.76 ?  672 LEU A CB    1 
ATOM   5412  C  CG    . LEU A 1 672 ? 155.329 121.149 106.717 1.00 23.94 ?  672 LEU A CG    1 
ATOM   5413  C  CD1   . LEU A 1 672 ? 155.976 119.798 106.978 1.00 19.57 ?  672 LEU A CD1   1 
ATOM   5414  C  CD2   . LEU A 1 672 ? 156.085 122.261 107.423 1.00 21.82 ?  672 LEU A CD2   1 
ATOM   5415  N  N     . TYR A 1 673 ? 153.803 122.271 102.428 1.00 21.30 ?  673 TYR A N     1 
ATOM   5416  C  CA    . TYR A 1 673 ? 153.892 122.666 101.028 1.00 18.93 ?  673 TYR A CA    1 
ATOM   5417  C  C     . TYR A 1 673 ? 153.194 123.998 100.791 1.00 21.16 ?  673 TYR A C     1 
ATOM   5418  O  O     . TYR A 1 673 ? 153.647 124.808 99.977  1.00 24.42 ?  673 TYR A O     1 
ATOM   5419  C  CB    . TYR A 1 673 ? 153.297 121.575 100.140 1.00 14.92 ?  673 TYR A CB    1 
ATOM   5420  C  CG    . TYR A 1 673 ? 153.405 121.864 98.663  1.00 19.19 ?  673 TYR A CG    1 
ATOM   5421  C  CD1   . TYR A 1 673 ? 154.642 121.963 98.046  1.00 18.76 ?  673 TYR A CD1   1 
ATOM   5422  C  CD2   . TYR A 1 673 ? 152.269 122.029 97.884  1.00 18.36 ?  673 TYR A CD2   1 
ATOM   5423  C  CE1   . TYR A 1 673 ? 154.745 122.225 96.698  1.00 23.48 ?  673 TYR A CE1   1 
ATOM   5424  C  CE2   . TYR A 1 673 ? 152.363 122.289 96.536  1.00 21.21 ?  673 TYR A CE2   1 
ATOM   5425  C  CZ    . TYR A 1 673 ? 153.603 122.385 95.948  1.00 25.20 ?  673 TYR A CZ    1 
ATOM   5426  O  OH    . TYR A 1 673 ? 153.704 122.644 94.602  1.00 24.69 ?  673 TYR A OH    1 
ATOM   5427  N  N     . ALA A 1 674 ? 152.081 124.236 101.488 1.00 23.17 ?  674 ALA A N     1 
ATOM   5428  C  CA    . ALA A 1 674 ? 151.425 125.535 101.419 1.00 16.78 ?  674 ALA A CA    1 
ATOM   5429  C  C     . ALA A 1 674 ? 152.330 126.632 101.961 1.00 17.23 ?  674 ALA A C     1 
ATOM   5430  O  O     . ALA A 1 674 ? 152.436 127.710 101.366 1.00 25.24 ?  674 ALA A O     1 
ATOM   5431  C  CB    . ALA A 1 674 ? 150.105 125.491 102.187 1.00 12.27 ?  674 ALA A CB    1 
ATOM   5432  N  N     . HIS A 1 675 ? 153.002 126.370 103.083 1.00 15.67 ?  675 HIS A N     1 
ATOM   5433  C  CA    . HIS A 1 675 ? 153.954 127.340 103.614 1.00 19.64 ?  675 HIS A CA    1 
ATOM   5434  C  C     . HIS A 1 675 ? 155.107 127.569 102.644 1.00 19.45 ?  675 HIS A C     1 
ATOM   5435  O  O     . HIS A 1 675 ? 155.566 128.704 102.469 1.00 24.55 ?  675 HIS A O     1 
ATOM   5436  C  CB    . HIS A 1 675 ? 154.479 126.871 104.969 1.00 18.08 ?  675 HIS A CB    1 
ATOM   5437  C  CG    . HIS A 1 675 ? 155.611 127.697 105.493 1.00 20.55 ?  675 HIS A CG    1 
ATOM   5438  N  ND1   . HIS A 1 675 ? 156.929 127.313 105.376 1.00 28.37 ?  675 HIS A ND1   1 
ATOM   5439  C  CD2   . HIS A 1 675 ? 155.622 128.890 106.131 1.00 18.60 ?  675 HIS A CD2   1 
ATOM   5440  C  CE1   . HIS A 1 675 ? 157.703 128.233 105.922 1.00 23.86 ?  675 HIS A CE1   1 
ATOM   5441  N  NE2   . HIS A 1 675 ? 156.935 129.200 106.388 1.00 24.59 ?  675 HIS A NE2   1 
ATOM   5442  N  N     . HIS A 1 676 ? 155.591 126.500 102.009 1.00 22.03 ?  676 HIS A N     1 
ATOM   5443  C  CA    . HIS A 1 676 ? 156.683 126.627 101.050 1.00 19.91 ?  676 HIS A CA    1 
ATOM   5444  C  C     . HIS A 1 676 ? 156.261 127.426 99.824  1.00 25.51 ?  676 HIS A C     1 
ATOM   5445  O  O     . HIS A 1 676 ? 157.054 128.200 99.276  1.00 25.79 ?  676 HIS A O     1 
ATOM   5446  C  CB    . HIS A 1 676 ? 157.174 125.239 100.640 1.00 23.94 ?  676 HIS A CB    1 
ATOM   5447  C  CG    . HIS A 1 676 ? 158.109 125.249 99.470  1.00 24.67 ?  676 HIS A CG    1 
ATOM   5448  N  ND1   . HIS A 1 676 ? 159.422 125.651 99.571  1.00 22.61 ?  676 HIS A ND1   1 
ATOM   5449  C  CD2   . HIS A 1 676 ? 157.918 124.905 98.176  1.00 25.58 ?  676 HIS A CD2   1 
ATOM   5450  C  CE1   . HIS A 1 676 ? 160.002 125.555 98.388  1.00 29.10 ?  676 HIS A CE1   1 
ATOM   5451  N  NE2   . HIS A 1 676 ? 159.111 125.105 97.524  1.00 27.74 ?  676 HIS A NE2   1 
ATOM   5452  N  N     . ARG A 1 677 ? 155.020 127.255 99.382  1.00 23.74 ?  677 ARG A N     1 
ATOM   5453  C  CA    . ARG A 1 677 ? 154.542 127.873 98.153  1.00 19.41 ?  677 ARG A CA    1 
ATOM   5454  C  C     . ARG A 1 677 ? 154.023 129.289 98.356  1.00 20.49 ?  677 ARG A C     1 
ATOM   5455  O  O     . ARG A 1 677 ? 153.535 129.896 97.398  1.00 27.52 ?  677 ARG A O     1 
ATOM   5456  C  CB    . ARG A 1 677 ? 153.447 127.009 97.521  1.00 22.31 ?  677 ARG A CB    1 
ATOM   5457  C  CG    . ARG A 1 677 ? 153.978 125.862 96.679  1.00 22.58 ?  677 ARG A CG    1 
ATOM   5458  C  CD    . ARG A 1 677 ? 154.579 126.363 95.377  1.00 18.82 ?  677 ARG A CD    1 
ATOM   5459  N  NE    . ARG A 1 677 ? 153.571 126.530 94.338  1.00 26.67 ?  677 ARG A NE    1 
ATOM   5460  C  CZ    . ARG A 1 677 ? 153.279 127.684 93.753  1.00 31.68 ?  677 ARG A CZ    1 
ATOM   5461  N  NH1   . ARG A 1 677 ? 153.905 128.803 94.080  1.00 29.78 1  677 ARG A NH1   1 
ATOM   5462  N  NH2   . ARG A 1 677 ? 152.335 127.717 92.817  1.00 25.25 ?  677 ARG A NH2   1 
ATOM   5463  N  N     . GLY A 1 678 ? 154.117 129.830 99.566  1.00 18.80 ?  678 GLY A N     1 
ATOM   5464  C  CA    . GLY A 1 678 ? 153.681 131.187 99.820  1.00 11.84 ?  678 GLY A CA    1 
ATOM   5465  C  C     . GLY A 1 678 ? 152.235 131.341 100.222 1.00 17.48 ?  678 GLY A C     1 
ATOM   5466  O  O     . GLY A 1 678 ? 151.701 132.452 100.133 1.00 21.36 ?  678 GLY A O     1 
ATOM   5467  N  N     . ILE A 1 679 ? 151.578 130.265 100.654 1.00 18.57 ?  679 ILE A N     1 
ATOM   5468  C  CA    . ILE A 1 679 ? 150.205 130.368 101.129 1.00 11.37 ?  679 ILE A CA    1 
ATOM   5469  C  C     . ILE A 1 679 ? 150.187 131.155 102.429 1.00 13.32 ?  679 ILE A C     1 
ATOM   5470  O  O     . ILE A 1 679 ? 150.969 130.886 103.350 1.00 29.23 ?  679 ILE A O     1 
ATOM   5471  C  CB    . ILE A 1 679 ? 149.588 128.974 101.308 1.00 16.02 ?  679 ILE A CB    1 
ATOM   5472  C  CG1   . ILE A 1 679 ? 149.403 128.296 99.950  1.00 13.20 ?  679 ILE A CG1   1 
ATOM   5473  C  CG2   . ILE A 1 679 ? 148.270 129.054 102.057 1.00 14.77 ?  679 ILE A CG2   1 
ATOM   5474  C  CD1   . ILE A 1 679 ? 148.527 129.062 99.010  1.00 13.30 ?  679 ILE A CD1   1 
ATOM   5475  N  N     . LYS A 1 680 ? 149.296 132.143 102.507 1.00 9.75  ?  680 LYS A N     1 
ATOM   5476  C  CA    . LYS A 1 680 ? 149.256 133.014 103.675 1.00 6.25  ?  680 LYS A CA    1 
ATOM   5477  C  C     . LYS A 1 680 ? 148.464 132.387 104.816 1.00 5.30  ?  680 LYS A C     1 
ATOM   5478  O  O     . LYS A 1 680 ? 148.909 132.399 105.967 1.00 17.26 ?  680 LYS A O     1 
ATOM   5479  C  CB    . LYS A 1 680 ? 148.665 134.369 103.288 1.00 8.74  ?  680 LYS A CB    1 
ATOM   5480  C  CG    . LYS A 1 680 ? 149.530 135.179 102.343 1.00 0.00  ?  680 LYS A CG    1 
ATOM   5481  C  CD    . LYS A 1 680 ? 148.950 136.563 102.140 1.00 5.72  ?  680 LYS A CD    1 
ATOM   5482  C  CE    . LYS A 1 680 ? 149.684 137.318 101.057 1.00 9.99  ?  680 LYS A CE    1 
ATOM   5483  N  NZ    . LYS A 1 680 ? 149.147 138.690 100.893 1.00 15.99 1  680 LYS A NZ    1 
ATOM   5484  N  N     . THR A 1 681 ? 147.291 131.836 104.517 1.00 10.68 ?  681 THR A N     1 
ATOM   5485  C  CA    . THR A 1 681 ? 146.430 131.244 105.530 1.00 8.05  ?  681 THR A CA    1 
ATOM   5486  C  C     . THR A 1 681 ? 145.826 129.954 104.999 1.00 14.02 ?  681 THR A C     1 
ATOM   5487  O  O     . THR A 1 681 ? 145.639 129.787 103.793 1.00 25.07 ?  681 THR A O     1 
ATOM   5488  C  CB    . THR A 1 681 ? 145.299 132.199 105.955 1.00 14.36 ?  681 THR A CB    1 
ATOM   5489  O  OG1   . THR A 1 681 ? 144.664 132.744 104.791 1.00 21.48 ?  681 THR A OG1   1 
ATOM   5490  C  CG2   . THR A 1 681 ? 145.836 133.334 106.811 1.00 11.98 ?  681 THR A CG2   1 
ATOM   5491  N  N     . ILE A 1 682 ? 145.520 129.042 105.918 1.00 10.50 ?  682 ILE A N     1 
ATOM   5492  C  CA    . ILE A 1 682 ? 144.776 127.825 105.620 1.00 11.42 ?  682 ILE A CA    1 
ATOM   5493  C  C     . ILE A 1 682 ? 143.510 127.837 106.464 1.00 14.42 ?  682 ILE A C     1 
ATOM   5494  O  O     . ILE A 1 682 ? 143.580 127.946 107.693 1.00 15.39 ?  682 ILE A O     1 
ATOM   5495  C  CB    . ILE A 1 682 ? 145.606 126.559 105.895 1.00 16.27 ?  682 ILE A CB    1 
ATOM   5496  C  CG1   . ILE A 1 682 ? 146.980 126.662 105.234 1.00 17.97 ?  682 ILE A CG1   1 
ATOM   5497  C  CG2   . ILE A 1 682 ? 144.876 125.340 105.392 1.00 19.16 ?  682 ILE A CG2   1 
ATOM   5498  C  CD1   . ILE A 1 682 ? 147.837 125.435 105.419 1.00 19.40 ?  682 ILE A CD1   1 
ATOM   5499  N  N     . TYR A 1 683 ? 142.356 127.729 105.806 1.00 16.60 ?  683 TYR A N     1 
ATOM   5500  C  CA    . TYR A 1 683 ? 141.085 127.936 106.500 1.00 11.86 ?  683 TYR A CA    1 
ATOM   5501  C  C     . TYR A 1 683 ? 140.612 126.677 107.223 1.00 23.72 ?  683 TYR A C     1 
ATOM   5502  O  O     . TYR A 1 683 ? 140.563 126.634 108.454 1.00 33.70 ?  683 TYR A O     1 
ATOM   5503  C  CB    . TYR A 1 683 ? 140.026 128.414 105.501 1.00 18.22 ?  683 TYR A CB    1 
ATOM   5504  C  CG    . TYR A 1 683 ? 138.715 128.821 106.128 1.00 15.29 ?  683 TYR A CG    1 
ATOM   5505  C  CD1   . TYR A 1 683 ? 138.658 129.256 107.444 1.00 15.83 ?  683 TYR A CD1   1 
ATOM   5506  C  CD2   . TYR A 1 683 ? 137.535 128.781 105.399 1.00 13.23 ?  683 TYR A CD2   1 
ATOM   5507  C  CE1   . TYR A 1 683 ? 137.467 129.630 108.018 1.00 19.36 ?  683 TYR A CE1   1 
ATOM   5508  C  CE2   . TYR A 1 683 ? 136.336 129.158 105.967 1.00 18.00 ?  683 TYR A CE2   1 
ATOM   5509  C  CZ    . TYR A 1 683 ? 136.309 129.581 107.276 1.00 20.89 ?  683 TYR A CZ    1 
ATOM   5510  O  OH    . TYR A 1 683 ? 135.118 129.958 107.852 1.00 28.35 ?  683 TYR A OH    1 
ATOM   5511  N  N     . TYR A 1 684 ? 140.285 125.634 106.476 1.00 31.22 ?  684 TYR A N     1 
ATOM   5512  C  CA    . TYR A 1 684 ? 139.614 124.481 107.049 1.00 24.27 ?  684 TYR A CA    1 
ATOM   5513  C  C     . TYR A 1 684 ? 140.240 123.200 106.532 1.00 33.98 ?  684 TYR A C     1 
ATOM   5514  O  O     . TYR A 1 684 ? 140.740 123.141 105.406 1.00 35.72 ?  684 TYR A O     1 
ATOM   5515  C  CB    . TYR A 1 684 ? 138.116 124.485 106.726 1.00 27.98 ?  684 TYR A CB    1 
ATOM   5516  C  CG    . TYR A 1 684 ? 137.259 125.097 107.806 1.00 25.86 ?  684 TYR A CG    1 
ATOM   5517  C  CD1   . TYR A 1 684 ? 137.497 124.826 109.144 1.00 28.64 ?  684 TYR A CD1   1 
ATOM   5518  C  CD2   . TYR A 1 684 ? 136.210 125.946 107.486 1.00 27.48 ?  684 TYR A CD2   1 
ATOM   5519  C  CE1   . TYR A 1 684 ? 136.716 125.383 110.135 1.00 32.74 ?  684 TYR A CE1   1 
ATOM   5520  C  CE2   . TYR A 1 684 ? 135.425 126.510 108.468 1.00 26.81 ?  684 TYR A CE2   1 
ATOM   5521  C  CZ    . TYR A 1 684 ? 135.682 126.226 109.790 1.00 33.03 ?  684 TYR A CZ    1 
ATOM   5522  O  OH    . TYR A 1 684 ? 134.901 126.784 110.775 1.00 36.74 ?  684 TYR A OH    1 
ATOM   5523  N  N     . ALA A 1 685 ? 140.209 122.177 107.375 1.00 33.01 ?  685 ALA A N     1 
ATOM   5524  C  CA    . ALA A 1 685 ? 140.602 120.824 107.004 1.00 30.94 ?  685 ALA A CA    1 
ATOM   5525  C  C     . ALA A 1 685 ? 139.317 120.006 106.936 1.00 33.77 ?  685 ALA A C     1 
ATOM   5526  O  O     . ALA A 1 685 ? 138.930 119.347 107.902 1.00 41.20 ?  685 ALA A O     1 
ATOM   5527  C  CB    . ALA A 1 685 ? 141.597 120.248 107.999 1.00 31.56 ?  685 ALA A CB    1 
ATOM   5528  N  N     . ARG A 1 686 ? 138.652 120.060 105.786 1.00 34.12 ?  686 ARG A N     1 
ATOM   5529  C  CA    . ARG A 1 686 ? 137.404 119.342 105.576 1.00 35.47 ?  686 ARG A CA    1 
ATOM   5530  C  C     . ARG A 1 686 ? 137.701 117.921 105.123 1.00 39.33 ?  686 ARG A C     1 
ATOM   5531  O  O     . ARG A 1 686 ? 138.442 117.712 104.158 1.00 41.11 ?  686 ARG A O     1 
ATOM   5532  C  CB    . ARG A 1 686 ? 136.535 120.056 104.541 1.00 38.70 ?  686 ARG A CB    1 
ATOM   5533  C  CG    . ARG A 1 686 ? 135.774 121.247 105.085 1.00 41.76 ?  686 ARG A CG    1 
ATOM   5534  C  CD    . ARG A 1 686 ? 134.515 121.494 104.278 1.00 42.10 ?  686 ARG A CD    1 
ATOM   5535  N  NE    . ARG A 1 686 ? 133.741 120.271 104.102 1.00 43.83 ?  686 ARG A NE    1 
ATOM   5536  C  CZ    . ARG A 1 686 ? 132.440 120.170 104.331 1.00 44.76 ?  686 ARG A CZ    1 
ATOM   5537  N  NH1   . ARG A 1 686 ? 131.728 121.208 104.737 1.00 42.57 1  686 ARG A NH1   1 
ATOM   5538  N  NH2   . ARG A 1 686 ? 131.837 119.000 104.148 1.00 43.63 ?  686 ARG A NH2   1 
ATOM   5539  N  N     . THR A 1 687 ? 137.119 116.951 105.816 1.00 44.90 ?  687 THR A N     1 
ATOM   5540  C  CA    . THR A 1 687 ? 137.351 115.542 105.539 1.00 47.74 ?  687 THR A CA    1 
ATOM   5541  C  C     . THR A 1 687 ? 136.059 114.888 105.067 1.00 46.02 ?  687 THR A C     1 
ATOM   5542  O  O     . THR A 1 687 ? 134.984 115.150 105.614 1.00 49.65 ?  687 THR A O     1 
ATOM   5543  C  CB    . THR A 1 687 ? 137.886 114.823 106.781 1.00 47.73 ?  687 THR A CB    1 
ATOM   5544  O  OG1   . THR A 1 687 ? 139.120 115.427 107.189 1.00 47.03 ?  687 THR A OG1   1 
ATOM   5545  C  CG2   . THR A 1 687 ? 138.136 113.362 106.483 1.00 47.44 ?  687 THR A CG2   1 
ATOM   5546  N  N     . LYS A 1 688 ? 136.169 114.046 104.044 1.00 44.89 ?  688 LYS A N     1 
ATOM   5547  C  CA    . LYS A 1 688 ? 135.016 113.328 103.517 1.00 50.69 ?  688 LYS A CA    1 
ATOM   5548  C  C     . LYS A 1 688 ? 135.017 111.878 103.991 1.00 54.40 ?  688 LYS A C     1 
ATOM   5549  O  O     . LYS A 1 688 ? 136.055 111.343 104.378 1.00 56.78 ?  688 LYS A O     1 
ATOM   5550  C  CB    . LYS A 1 688 ? 134.999 113.382 101.989 1.00 49.89 ?  688 LYS A CB    1 
ATOM   5551  C  CG    . LYS A 1 688 ? 135.879 112.339 101.321 1.00 49.17 ?  688 LYS A CG    1 
ATOM   5552  C  CD    . LYS A 1 688 ? 135.418 112.040 99.904  1.00 51.52 ?  688 LYS A CD    1 
ATOM   5553  C  CE    . LYS A 1 688 ? 133.902 111.994 99.801  1.00 51.01 ?  688 LYS A CE    1 
ATOM   5554  N  NZ    . LYS A 1 688 ? 133.457 111.635 98.426  1.00 50.48 ?  688 LYS A NZ    1 
ATOM   5555  N  N     . VAL B 1 6   ? 153.469 115.784 164.800 1.00 58.06 ?  6   VAL B N     1 
ATOM   5556  C  CA    . VAL B 1 6   ? 152.385 116.555 165.397 1.00 60.47 ?  6   VAL B CA    1 
ATOM   5557  C  C     . VAL B 1 6   ? 152.947 117.639 166.310 1.00 60.85 ?  6   VAL B C     1 
ATOM   5558  O  O     . VAL B 1 6   ? 153.697 117.345 167.241 1.00 56.42 ?  6   VAL B O     1 
ATOM   5559  C  CB    . VAL B 1 6   ? 151.412 115.645 166.163 1.00 59.34 ?  6   VAL B CB    1 
ATOM   5560  C  CG1   . VAL B 1 6   ? 150.227 116.448 166.671 1.00 55.45 ?  6   VAL B CG1   1 
ATOM   5561  C  CG2   . VAL B 1 6   ? 150.944 114.503 165.276 1.00 59.30 ?  6   VAL B CG2   1 
ATOM   5562  N  N     . PRO B 1 7   ? 152.591 118.892 166.033 1.00 59.15 ?  7   PRO B N     1 
ATOM   5563  C  CA    . PRO B 1 7   ? 153.094 120.001 166.853 1.00 53.13 ?  7   PRO B CA    1 
ATOM   5564  C  C     . PRO B 1 7   ? 152.628 119.892 168.297 1.00 55.56 ?  7   PRO B C     1 
ATOM   5565  O  O     . PRO B 1 7   ? 151.573 119.329 168.595 1.00 60.63 ?  7   PRO B O     1 
ATOM   5566  C  CB    . PRO B 1 7   ? 152.508 121.244 166.177 1.00 52.80 ?  7   PRO B CB    1 
ATOM   5567  C  CG    . PRO B 1 7   ? 152.132 120.828 164.809 1.00 56.23 ?  7   PRO B CG    1 
ATOM   5568  C  CD    . PRO B 1 7   ? 151.936 119.347 164.795 1.00 56.88 ?  7   PRO B CD    1 
ATOM   5569  N  N     . LYS B 1 8   ? 153.447 120.436 169.202 1.00 55.11 ?  8   LYS B N     1 
ATOM   5570  C  CA    . LYS B 1 8   ? 153.123 120.385 170.624 1.00 54.87 ?  8   LYS B CA    1 
ATOM   5571  C  C     . LYS B 1 8   ? 151.832 121.132 170.928 1.00 57.26 ?  8   LYS B C     1 
ATOM   5572  O  O     . LYS B 1 8   ? 150.996 120.654 171.705 1.00 59.71 ?  8   LYS B O     1 
ATOM   5573  C  CB    . LYS B 1 8   ? 154.278 120.957 171.444 1.00 55.07 ?  8   LYS B CB    1 
ATOM   5574  C  CG    . LYS B 1 8   ? 154.257 120.551 172.908 1.00 55.73 ?  8   LYS B CG    1 
ATOM   5575  C  CD    . LYS B 1 8   ? 154.793 121.660 173.797 1.00 56.79 ?  8   LYS B CD    1 
ATOM   5576  C  CE    . LYS B 1 8   ? 154.128 121.641 175.164 1.00 58.05 ?  8   LYS B CE    1 
ATOM   5577  N  NZ    . LYS B 1 8   ? 154.978 122.279 176.205 1.00 56.65 1  8   LYS B NZ    1 
ATOM   5578  N  N     . TRP B 1 9   ? 151.649 122.310 170.326 1.00 58.22 ?  9   TRP B N     1 
ATOM   5579  C  CA    . TRP B 1 9   ? 150.415 123.055 170.541 1.00 51.60 ?  9   TRP B CA    1 
ATOM   5580  C  C     . TRP B 1 9   ? 149.214 122.331 169.953 1.00 51.94 ?  9   TRP B C     1 
ATOM   5581  O  O     . TRP B 1 9   ? 148.113 122.416 170.504 1.00 58.14 ?  9   TRP B O     1 
ATOM   5582  C  CB    . TRP B 1 9   ? 150.528 124.460 169.951 1.00 50.43 ?  9   TRP B CB    1 
ATOM   5583  C  CG    . TRP B 1 9   ? 150.903 124.496 168.502 1.00 48.99 ?  9   TRP B CG    1 
ATOM   5584  C  CD1   . TRP B 1 9   ? 150.052 124.499 167.438 1.00 48.05 ?  9   TRP B CD1   1 
ATOM   5585  C  CD2   . TRP B 1 9   ? 152.226 124.563 167.959 1.00 48.63 ?  9   TRP B CD2   1 
ATOM   5586  N  NE1   . TRP B 1 9   ? 150.762 124.552 166.265 1.00 47.61 ?  9   TRP B NE1   1 
ATOM   5587  C  CE2   . TRP B 1 9   ? 152.099 124.595 166.557 1.00 50.20 ?  9   TRP B CE2   1 
ATOM   5588  C  CE3   . TRP B 1 9   ? 153.505 124.594 168.521 1.00 45.96 ?  9   TRP B CE3   1 
ATOM   5589  C  CZ2   . TRP B 1 9   ? 153.202 124.653 165.709 1.00 49.91 ?  9   TRP B CZ2   1 
ATOM   5590  C  CZ3   . TRP B 1 9   ? 154.597 124.654 167.678 1.00 51.15 ?  9   TRP B CZ3   1 
ATOM   5591  C  CH2   . TRP B 1 9   ? 154.438 124.681 166.289 1.00 51.69 ?  9   TRP B CH2   1 
ATOM   5592  N  N     . ILE B 1 10  ? 149.400 121.620 168.840 1.00 52.13 ?  10  ILE B N     1 
ATOM   5593  C  CA    . ILE B 1 10  ? 148.302 120.850 168.268 1.00 53.51 ?  10  ILE B CA    1 
ATOM   5594  C  C     . ILE B 1 10  ? 147.923 119.700 169.193 1.00 54.08 ?  10  ILE B C     1 
ATOM   5595  O  O     . ILE B 1 10  ? 146.737 119.402 169.382 1.00 56.39 ?  10  ILE B O     1 
ATOM   5596  C  CB    . ILE B 1 10  ? 148.674 120.356 166.858 1.00 54.76 ?  10  ILE B CB    1 
ATOM   5597  C  CG1   . ILE B 1 10  ? 148.557 121.498 165.846 1.00 53.72 ?  10  ILE B CG1   1 
ATOM   5598  C  CG2   . ILE B 1 10  ? 147.783 119.201 166.441 1.00 55.30 ?  10  ILE B CG2   1 
ATOM   5599  C  CD1   . ILE B 1 10  ? 147.376 122.414 166.080 1.00 54.18 ?  10  ILE B CD1   1 
ATOM   5600  N  N     . GLN B 1 11  ? 148.919 119.041 169.791 1.00 57.56 ?  11  GLN B N     1 
ATOM   5601  C  CA    . GLN B 1 11  ? 148.627 117.996 170.767 1.00 57.04 ?  11  GLN B CA    1 
ATOM   5602  C  C     . GLN B 1 11  ? 147.892 118.561 171.974 1.00 59.28 ?  11  GLN B C     1 
ATOM   5603  O  O     . GLN B 1 11  ? 146.901 117.981 172.431 1.00 60.20 ?  11  GLN B O     1 
ATOM   5604  C  CB    . GLN B 1 11  ? 149.918 117.308 171.210 1.00 56.99 ?  11  GLN B CB    1 
ATOM   5605  C  CG    . GLN B 1 11  ? 150.365 116.168 170.314 1.00 60.82 ?  11  GLN B CG    1 
ATOM   5606  C  CD    . GLN B 1 11  ? 151.870 115.999 170.305 1.00 62.31 ?  11  GLN B CD    1 
ATOM   5607  O  OE1   . GLN B 1 11  ? 152.472 115.748 169.262 1.00 61.39 ?  11  GLN B OE1   1 
ATOM   5608  N  NE2   . GLN B 1 11  ? 152.489 116.139 171.471 1.00 60.14 ?  11  GLN B NE2   1 
ATOM   5609  N  N     . LEU B 1 12  ? 148.356 119.699 172.497 1.00 58.79 ?  12  LEU B N     1 
ATOM   5610  C  CA    . LEU B 1 12  ? 147.711 120.298 173.662 1.00 54.13 ?  12  LEU B CA    1 
ATOM   5611  C  C     . LEU B 1 12  ? 146.279 120.713 173.350 1.00 57.99 ?  12  LEU B C     1 
ATOM   5612  O  O     . LEU B 1 12  ? 145.378 120.542 174.180 1.00 60.10 ?  12  LEU B O     1 
ATOM   5613  C  CB    . LEU B 1 12  ? 148.520 121.498 174.152 1.00 55.26 ?  12  LEU B CB    1 
ATOM   5614  C  CG    . LEU B 1 12  ? 149.617 121.201 175.173 1.00 58.07 ?  12  LEU B CG    1 
ATOM   5615  C  CD1   . LEU B 1 12  ? 150.513 122.412 175.352 1.00 58.53 ?  12  LEU B CD1   1 
ATOM   5616  C  CD2   . LEU B 1 12  ? 149.013 120.776 176.498 1.00 56.30 ?  12  LEU B CD2   1 
ATOM   5617  N  N     . ASN B 1 13  ? 146.051 121.270 172.160 1.00 53.89 ?  13  ASN B N     1 
ATOM   5618  C  CA    . ASN B 1 13  ? 144.701 121.646 171.760 1.00 52.68 ?  13  ASN B CA    1 
ATOM   5619  C  C     . ASN B 1 13  ? 143.817 120.417 171.589 1.00 56.13 ?  13  ASN B C     1 
ATOM   5620  O  O     . ASN B 1 13  ? 142.600 120.485 171.796 1.00 62.41 ?  13  ASN B O     1 
ATOM   5621  C  CB    . ASN B 1 13  ? 144.754 122.464 170.470 1.00 53.91 ?  13  ASN B CB    1 
ATOM   5622  C  CG    . ASN B 1 13  ? 143.387 122.684 169.860 1.00 53.99 ?  13  ASN B CG    1 
ATOM   5623  O  OD1   . ASN B 1 13  ? 142.959 121.934 168.983 1.00 55.79 ?  13  ASN B OD1   1 
ATOM   5624  N  ND2   . ASN B 1 13  ? 142.692 123.716 170.320 1.00 54.99 ?  13  ASN B ND2   1 
ATOM   5625  N  N     . ASN B 1 14  ? 144.411 119.282 171.216 1.00 59.08 ?  14  ASN B N     1 
ATOM   5626  C  CA    . ASN B 1 14  ? 143.641 118.057 171.047 1.00 55.76 ?  14  ASN B CA    1 
ATOM   5627  C  C     . ASN B 1 14  ? 143.271 117.411 172.376 1.00 58.53 ?  14  ASN B C     1 
ATOM   5628  O  O     . ASN B 1 14  ? 142.386 116.551 172.402 1.00 63.28 ?  14  ASN B O     1 
ATOM   5629  C  CB    . ASN B 1 14  ? 144.418 117.064 170.184 1.00 59.59 ?  14  ASN B CB    1 
ATOM   5630  C  CG    . ASN B 1 14  ? 144.326 117.382 168.706 1.00 59.07 ?  14  ASN B CG    1 
ATOM   5631  O  OD1   . ASN B 1 14  ? 144.070 118.520 168.319 1.00 59.30 ?  14  ASN B OD1   1 
ATOM   5632  N  ND2   . ASN B 1 14  ? 144.536 116.372 167.871 1.00 58.70 ?  14  ASN B ND2   1 
ATOM   5633  N  N     . GLU B 1 15  ? 143.918 117.804 173.474 1.00 59.48 ?  15  GLU B N     1 
ATOM   5634  C  CA    . GLU B 1 15  ? 143.584 117.252 174.782 1.00 59.95 ?  15  GLU B CA    1 
ATOM   5635  C  C     . GLU B 1 15  ? 142.311 117.843 175.369 1.00 61.82 ?  15  GLU B C     1 
ATOM   5636  O  O     . GLU B 1 15  ? 141.885 117.403 176.442 1.00 64.87 ?  15  GLU B O     1 
ATOM   5637  C  CB    . GLU B 1 15  ? 144.737 117.459 175.768 1.00 60.50 ?  15  GLU B CB    1 
ATOM   5638  C  CG    . GLU B 1 15  ? 146.096 117.044 175.243 1.00 62.55 ?  15  GLU B CG    1 
ATOM   5639  C  CD    . GLU B 1 15  ? 147.161 117.047 176.320 1.00 66.42 ?  15  GLU B CD    1 
ATOM   5640  O  OE1   . GLU B 1 15  ? 146.800 117.022 177.514 1.00 64.42 ?  15  GLU B OE1   1 
ATOM   5641  O  OE2   . GLU B 1 15  ? 148.361 117.077 175.972 1.00 66.45 -1 15  GLU B OE2   1 
ATOM   5642  N  N     . ILE B 1 16  ? 141.708 118.832 174.709 1.00 60.94 ?  16  ILE B N     1 
ATOM   5643  C  CA    . ILE B 1 16  ? 140.424 119.353 175.167 1.00 60.27 ?  16  ILE B CA    1 
ATOM   5644  C  C     . ILE B 1 16  ? 139.358 118.267 175.096 1.00 60.83 ?  16  ILE B C     1 
ATOM   5645  O  O     . ILE B 1 16  ? 138.556 118.100 176.022 1.00 61.27 ?  16  ILE B O     1 
ATOM   5646  C  CB    . ILE B 1 16  ? 140.027 120.595 174.349 1.00 61.94 ?  16  ILE B CB    1 
ATOM   5647  C  CG1   . ILE B 1 16  ? 141.150 121.632 174.378 1.00 60.80 ?  16  ILE B CG1   1 
ATOM   5648  C  CG2   . ILE B 1 16  ? 138.730 121.188 174.876 1.00 60.34 ?  16  ILE B CG2   1 
ATOM   5649  C  CD1   . ILE B 1 16  ? 140.713 123.018 173.974 1.00 58.23 ?  16  ILE B CD1   1 
ATOM   5650  N  N     . MET B 1 17  ? 139.337 117.510 173.997 1.00 62.13 ?  17  MET B N     1 
ATOM   5651  C  CA    . MET B 1 17  ? 138.344 116.454 173.838 1.00 63.00 ?  17  MET B CA    1 
ATOM   5652  C  C     . MET B 1 17  ? 138.598 115.269 174.759 1.00 63.88 ?  17  MET B C     1 
ATOM   5653  O  O     . MET B 1 17  ? 137.665 114.508 175.035 1.00 65.86 ?  17  MET B O     1 
ATOM   5654  C  CB    . MET B 1 17  ? 138.306 115.977 172.387 1.00 63.13 ?  17  MET B CB    1 
ATOM   5655  C  CG    . MET B 1 17  ? 138.140 117.059 171.311 1.00 63.32 ?  17  MET B CG    1 
ATOM   5656  S  SD    . MET B 1 17  ? 136.587 117.990 171.189 1.00 70.70 ?  17  MET B SD    1 
ATOM   5657  C  CE    . MET B 1 17  ? 136.601 119.039 172.639 1.00 62.37 ?  17  MET B CE    1 
ATOM   5658  N  N     . ILE B 1 18  ? 139.830 115.088 175.230 1.00 63.36 ?  18  ILE B N     1 
ATOM   5659  C  CA    . ILE B 1 18  ? 140.109 114.033 176.199 1.00 63.14 ?  18  ILE B CA    1 
ATOM   5660  C  C     . ILE B 1 18  ? 139.413 114.420 177.500 1.00 63.69 ?  18  ILE B C     1 
ATOM   5661  O  O     . ILE B 1 18  ? 139.804 115.384 178.165 1.00 64.62 ?  18  ILE B O     1 
ATOM   5662  C  CB    . ILE B 1 18  ? 141.614 113.823 176.402 1.00 63.13 ?  18  ILE B CB    1 
ATOM   5663  C  CG1   . ILE B 1 18  ? 142.204 112.973 175.271 1.00 62.85 ?  18  ILE B CG1   1 
ATOM   5664  C  CG2   . ILE B 1 18  ? 141.886 113.130 177.728 1.00 63.54 ?  18  ILE B CG2   1 
ATOM   5665  C  CD1   . ILE B 1 18  ? 142.384 113.700 173.957 1.00 62.27 ?  18  ILE B CD1   1 
ATOM   5666  N  N     . GLN B 1 19  ? 138.362 113.685 177.852 1.00 68.67 ?  19  GLN B N     1 
ATOM   5667  C  CA    . GLN B 1 19  ? 137.529 114.040 178.992 1.00 69.55 ?  19  GLN B CA    1 
ATOM   5668  C  C     . GLN B 1 19  ? 138.180 113.545 180.276 1.00 70.48 ?  19  GLN B C     1 
ATOM   5669  O  O     . GLN B 1 19  ? 138.362 112.338 180.465 1.00 71.79 ?  19  GLN B O     1 
ATOM   5670  C  CB    . GLN B 1 19  ? 136.131 113.451 178.828 1.00 70.06 ?  19  GLN B CB    1 
ATOM   5671  C  CG    . GLN B 1 19  ? 135.203 114.301 177.976 1.00 69.09 ?  19  GLN B CG    1 
ATOM   5672  C  CD    . GLN B 1 19  ? 133.792 114.354 178.522 1.00 72.31 ?  19  GLN B CD    1 
ATOM   5673  O  OE1   . GLN B 1 19  ? 133.537 113.949 179.655 1.00 72.66 ?  19  GLN B OE1   1 
ATOM   5674  N  NE2   . GLN B 1 19  ? 132.865 114.856 177.715 1.00 69.92 ?  19  GLN B NE2   1 
ATOM   5675  N  N     . LYS B 1 20  ? 138.533 114.478 181.155 1.00 74.71 ?  20  LYS B N     1 
ATOM   5676  C  CA    . LYS B 1 20  ? 139.114 114.167 182.454 1.00 74.45 ?  20  LYS B CA    1 
ATOM   5677  C  C     . LYS B 1 20  ? 138.090 114.497 183.531 1.00 77.20 ?  20  LYS B C     1 
ATOM   5678  O  O     . LYS B 1 20  ? 137.582 115.623 183.583 1.00 74.44 ?  20  LYS B O     1 
ATOM   5679  C  CB    . LYS B 1 20  ? 140.408 114.950 182.676 1.00 71.73 ?  20  LYS B CB    1 
ATOM   5680  C  CG    . LYS B 1 20  ? 141.083 114.668 184.007 1.00 74.91 ?  20  LYS B CG    1 
ATOM   5681  C  CD    . LYS B 1 20  ? 141.917 115.853 184.471 1.00 75.30 ?  20  LYS B CD    1 
ATOM   5682  C  CE    . LYS B 1 20  ? 141.067 117.100 184.637 1.00 76.62 ?  20  LYS B CE    1 
ATOM   5683  N  NZ    . LYS B 1 20  ? 139.792 116.817 185.353 1.00 78.76 1  20  LYS B NZ    1 
ATOM   5684  N  N     . ASP B 1 21  ? 137.788 113.513 184.381 1.00 82.99 ?  21  ASP B N     1 
ATOM   5685  C  CA    . ASP B 1 21  ? 136.805 113.660 185.455 1.00 82.58 ?  21  ASP B CA    1 
ATOM   5686  C  C     . ASP B 1 21  ? 135.434 114.050 184.905 1.00 82.92 ?  21  ASP B C     1 
ATOM   5687  O  O     . ASP B 1 21  ? 134.697 114.832 185.510 1.00 82.22 ?  21  ASP B O     1 
ATOM   5688  C  CB    . ASP B 1 21  ? 137.282 114.669 186.506 1.00 82.38 ?  21  ASP B CB    1 
ATOM   5689  C  CG    . ASP B 1 21  ? 136.541 114.533 187.823 1.00 84.51 ?  21  ASP B CG    1 
ATOM   5690  O  OD1   . ASP B 1 21  ? 136.269 113.387 188.240 1.00 82.89 ?  21  ASP B OD1   1 
ATOM   5691  O  OD2   . ASP B 1 21  ? 136.230 115.574 188.441 1.00 84.64 -1 21  ASP B OD2   1 
ATOM   5692  N  N     . GLY B 1 22  ? 135.089 113.502 183.741 1.00 75.34 ?  22  GLY B N     1 
ATOM   5693  C  CA    . GLY B 1 22  ? 133.788 113.740 183.149 1.00 74.48 ?  22  GLY B CA    1 
ATOM   5694  C  C     . GLY B 1 22  ? 133.596 115.104 182.527 1.00 76.15 ?  22  GLY B C     1 
ATOM   5695  O  O     . GLY B 1 22  ? 132.461 115.455 182.188 1.00 75.95 ?  22  GLY B O     1 
ATOM   5696  N  N     . LYS B 1 23  ? 134.662 115.885 182.367 1.00 72.59 ?  23  LYS B N     1 
ATOM   5697  C  CA    . LYS B 1 23  ? 134.573 117.222 181.803 1.00 69.37 ?  23  LYS B CA    1 
ATOM   5698  C  C     . LYS B 1 23  ? 135.679 117.425 180.779 1.00 70.04 ?  23  LYS B C     1 
ATOM   5699  O  O     . LYS B 1 23  ? 136.761 116.843 180.884 1.00 69.80 ?  23  LYS B O     1 
ATOM   5700  C  CB    . LYS B 1 23  ? 134.679 118.301 182.888 1.00 68.27 ?  23  LYS B CB    1 
ATOM   5701  C  CG    . LYS B 1 23  ? 133.537 118.304 183.887 1.00 68.38 ?  23  LYS B CG    1 
ATOM   5702  C  CD    . LYS B 1 23  ? 133.695 119.443 184.878 1.00 68.60 ?  23  LYS B CD    1 
ATOM   5703  C  CE    . LYS B 1 23  ? 132.641 119.386 185.968 1.00 69.97 ?  23  LYS B CE    1 
ATOM   5704  N  NZ    . LYS B 1 23  ? 132.884 120.416 187.014 1.00 68.39 1  23  LYS B NZ    1 
ATOM   5705  N  N     . PHE B 1 24  ? 135.393 118.261 179.783 1.00 65.61 ?  24  PHE B N     1 
ATOM   5706  C  CA    . PHE B 1 24  ? 136.416 118.643 178.822 1.00 62.62 ?  24  PHE B CA    1 
ATOM   5707  C  C     . PHE B 1 24  ? 137.506 119.453 179.512 1.00 61.66 ?  24  PHE B C     1 
ATOM   5708  O  O     . PHE B 1 24  ? 137.250 120.211 180.450 1.00 61.85 ?  24  PHE B O     1 
ATOM   5709  C  CB    . PHE B 1 24  ? 135.810 119.463 177.681 1.00 61.12 ?  24  PHE B CB    1 
ATOM   5710  C  CG    . PHE B 1 24  ? 134.825 118.705 176.842 1.00 61.30 ?  24  PHE B CG    1 
ATOM   5711  C  CD1   . PHE B 1 24  ? 135.241 118.009 175.722 1.00 64.24 ?  24  PHE B CD1   1 
ATOM   5712  C  CD2   . PHE B 1 24  ? 133.478 118.706 177.161 1.00 61.65 ?  24  PHE B CD2   1 
ATOM   5713  C  CE1   . PHE B 1 24  ? 134.335 117.317 174.943 1.00 64.73 ?  24  PHE B CE1   1 
ATOM   5714  C  CE2   . PHE B 1 24  ? 132.567 118.015 176.385 1.00 62.37 ?  24  PHE B CE2   1 
ATOM   5715  C  CZ    . PHE B 1 24  ? 132.997 117.320 175.275 1.00 61.31 ?  24  PHE B CZ    1 
ATOM   5716  N  N     . GLN B 1 25  ? 138.741 119.286 179.039 1.00 62.73 ?  25  GLN B N     1 
ATOM   5717  C  CA    . GLN B 1 25  ? 139.878 120.030 179.580 1.00 63.64 ?  25  GLN B CA    1 
ATOM   5718  C  C     . GLN B 1 25  ? 139.980 121.353 178.829 1.00 64.69 ?  25  GLN B C     1 
ATOM   5719  O  O     . GLN B 1 25  ? 140.803 121.542 177.930 1.00 64.40 ?  25  GLN B O     1 
ATOM   5720  C  CB    . GLN B 1 25  ? 141.158 119.210 179.476 1.00 64.71 ?  25  GLN B CB    1 
ATOM   5721  C  CG    . GLN B 1 25  ? 141.183 117.993 180.387 1.00 62.14 ?  25  GLN B CG    1 
ATOM   5722  C  CD    . GLN B 1 25  ? 142.352 117.077 180.099 1.00 63.89 ?  25  GLN B CD    1 
ATOM   5723  O  OE1   . GLN B 1 25  ? 143.438 117.247 180.650 1.00 63.37 ?  25  GLN B OE1   1 
ATOM   5724  N  NE2   . GLN B 1 25  ? 142.136 116.099 179.228 1.00 64.37 ?  25  GLN B NE2   1 
ATOM   5725  N  N     . PHE B 1 26  ? 139.108 122.288 179.216 1.00 59.58 ?  26  PHE B N     1 
ATOM   5726  C  CA    . PHE B 1 26  ? 139.074 123.590 178.560 1.00 56.88 ?  26  PHE B CA    1 
ATOM   5727  C  C     . PHE B 1 26  ? 140.335 124.397 178.837 1.00 59.74 ?  26  PHE B C     1 
ATOM   5728  O  O     . PHE B 1 26  ? 140.718 125.243 178.022 1.00 60.98 ?  26  PHE B O     1 
ATOM   5729  C  CB    . PHE B 1 26  ? 137.837 124.368 179.007 1.00 52.78 ?  26  PHE B CB    1 
ATOM   5730  C  CG    . PHE B 1 26  ? 136.552 123.838 178.443 1.00 55.55 ?  26  PHE B CG    1 
ATOM   5731  C  CD1   . PHE B 1 26  ? 136.410 123.635 177.081 1.00 55.27 ?  26  PHE B CD1   1 
ATOM   5732  C  CD2   . PHE B 1 26  ? 135.486 123.538 179.275 1.00 54.50 ?  26  PHE B CD2   1 
ATOM   5733  C  CE1   . PHE B 1 26  ? 135.231 123.145 176.560 1.00 56.32 ?  26  PHE B CE1   1 
ATOM   5734  C  CE2   . PHE B 1 26  ? 134.304 123.049 178.757 1.00 52.70 ?  26  PHE B CE2   1 
ATOM   5735  C  CZ    . PHE B 1 26  ? 134.176 122.852 177.398 1.00 52.96 ?  26  PHE B CZ    1 
ATOM   5736  N  N     . ASP B 1 27  ? 140.989 124.152 179.975 1.00 63.05 ?  27  ASP B N     1 
ATOM   5737  C  CA    . ASP B 1 27  ? 142.210 124.868 180.321 1.00 58.55 ?  27  ASP B CA    1 
ATOM   5738  C  C     . ASP B 1 27  ? 143.391 124.485 179.442 1.00 60.78 ?  27  ASP B C     1 
ATOM   5739  O  O     . ASP B 1 27  ? 144.417 125.172 179.484 1.00 62.31 ?  27  ASP B O     1 
ATOM   5740  C  CB    . ASP B 1 27  ? 142.559 124.620 181.789 1.00 60.43 ?  27  ASP B CB    1 
ATOM   5741  C  CG    . ASP B 1 27  ? 141.356 124.742 182.702 1.00 65.03 ?  27  ASP B CG    1 
ATOM   5742  O  OD1   . ASP B 1 27  ? 140.298 124.164 182.372 1.00 65.00 ?  27  ASP B OD1   1 
ATOM   5743  O  OD2   . ASP B 1 27  ? 141.465 125.416 183.748 1.00 65.17 -1 27  ASP B OD2   1 
ATOM   5744  N  N     . LYS B 1 28  ? 143.279 123.414 178.655 1.00 60.48 ?  28  LYS B N     1 
ATOM   5745  C  CA    . LYS B 1 28  ? 144.369 123.020 177.771 1.00 61.30 ?  28  LYS B CA    1 
ATOM   5746  C  C     . LYS B 1 28  ? 144.564 123.995 176.620 1.00 61.69 ?  28  LYS B C     1 
ATOM   5747  O  O     . LYS B 1 28  ? 145.651 124.030 176.033 1.00 62.22 ?  28  LYS B O     1 
ATOM   5748  C  CB    . LYS B 1 28  ? 144.119 121.615 177.220 1.00 61.12 ?  28  LYS B CB    1 
ATOM   5749  C  CG    . LYS B 1 28  ? 144.360 120.504 178.225 1.00 61.20 ?  28  LYS B CG    1 
ATOM   5750  C  CD    . LYS B 1 28  ? 145.843 120.270 178.436 1.00 61.63 ?  28  LYS B CD    1 
ATOM   5751  C  CE    . LYS B 1 28  ? 146.097 119.427 179.671 1.00 61.66 ?  28  LYS B CE    1 
ATOM   5752  N  NZ    . LYS B 1 28  ? 147.530 119.044 179.789 1.00 59.46 1  28  LYS B NZ    1 
ATOM   5753  N  N     . ASP B 1 29  ? 143.543 124.787 176.284 1.00 58.24 ?  29  ASP B N     1 
ATOM   5754  C  CA    . ASP B 1 29  ? 143.678 125.725 175.176 1.00 55.40 ?  29  ASP B CA    1 
ATOM   5755  C  C     . ASP B 1 29  ? 144.583 126.896 175.540 1.00 55.16 ?  29  ASP B C     1 
ATOM   5756  O  O     . ASP B 1 29  ? 145.261 127.445 174.666 1.00 57.74 ?  29  ASP B O     1 
ATOM   5757  C  CB    . ASP B 1 29  ? 142.302 126.219 174.738 1.00 55.23 ?  29  ASP B CB    1 
ATOM   5758  C  CG    . ASP B 1 29  ? 142.130 126.196 173.232 1.00 58.52 ?  29  ASP B CG    1 
ATOM   5759  O  OD1   . ASP B 1 29  ? 141.301 126.970 172.714 1.00 55.50 ?  29  ASP B OD1   1 
ATOM   5760  O  OD2   . ASP B 1 29  ? 142.827 125.403 172.566 1.00 58.35 -1 29  ASP B OD2   1 
ATOM   5761  N  N     . LYS B 1 30  ? 144.601 127.296 176.814 1.00 55.30 ?  30  LYS B N     1 
ATOM   5762  C  CA    . LYS B 1 30  ? 145.589 128.275 177.259 1.00 56.62 ?  30  LYS B CA    1 
ATOM   5763  C  C     . LYS B 1 30  ? 146.999 127.710 177.150 1.00 56.50 ?  30  LYS B C     1 
ATOM   5764  O  O     . LYS B 1 30  ? 147.919 128.397 176.688 1.00 57.10 ?  30  LYS B O     1 
ATOM   5765  C  CB    . LYS B 1 30  ? 145.295 128.707 178.695 1.00 54.70 ?  30  LYS B CB    1 
ATOM   5766  C  CG    . LYS B 1 30  ? 143.997 129.475 178.861 1.00 56.61 ?  30  LYS B CG    1 
ATOM   5767  C  CD    . LYS B 1 30  ? 144.255 130.920 179.260 1.00 58.11 ?  30  LYS B CD    1 
ATOM   5768  C  CE    . LYS B 1 30  ? 145.326 131.017 180.337 1.00 58.82 ?  30  LYS B CE    1 
ATOM   5769  N  NZ    . LYS B 1 30  ? 145.374 132.369 180.958 1.00 58.06 1  30  LYS B NZ    1 
ATOM   5770  N  N     . GLU B 1 31  ? 147.184 126.455 177.563 1.00 57.78 ?  31  GLU B N     1 
ATOM   5771  C  CA    . GLU B 1 31  ? 148.463 125.792 177.347 1.00 54.53 ?  31  GLU B CA    1 
ATOM   5772  C  C     . GLU B 1 31  ? 148.752 125.646 175.860 1.00 55.31 ?  31  GLU B C     1 
ATOM   5773  O  O     . GLU B 1 31  ? 149.897 125.803 175.425 1.00 57.92 ?  31  GLU B O     1 
ATOM   5774  C  CB    . GLU B 1 31  ? 148.473 124.428 178.035 1.00 55.06 ?  31  GLU B CB    1 
ATOM   5775  C  CG    . GLU B 1 31  ? 148.453 124.496 179.552 1.00 56.40 ?  31  GLU B CG    1 
ATOM   5776  C  CD    . GLU B 1 31  ? 148.518 123.126 180.196 1.00 63.70 ?  31  GLU B CD    1 
ATOM   5777  O  OE1   . GLU B 1 31  ? 148.486 122.119 179.458 1.00 65.30 ?  31  GLU B OE1   1 
ATOM   5778  O  OE2   . GLU B 1 31  ? 148.601 123.055 181.440 1.00 60.64 -1 31  GLU B OE2   1 
ATOM   5779  N  N     . ALA B 1 32  ? 147.722 125.351 175.066 1.00 52.44 ?  32  ALA B N     1 
ATOM   5780  C  CA    . ALA B 1 32  ? 147.917 125.204 173.628 1.00 49.90 ?  32  ALA B CA    1 
ATOM   5781  C  C     . ALA B 1 32  ? 148.388 126.507 172.994 1.00 51.55 ?  32  ALA B C     1 
ATOM   5782  O  O     . ALA B 1 32  ? 149.328 126.505 172.195 1.00 52.12 ?  32  ALA B O     1 
ATOM   5783  C  CB    . ALA B 1 32  ? 146.625 124.725 172.967 1.00 49.16 ?  32  ALA B CB    1 
ATOM   5784  N  N     . VAL B 1 33  ? 147.757 127.631 173.342 1.00 54.60 ?  33  VAL B N     1 
ATOM   5785  C  CA    . VAL B 1 33  ? 148.155 128.905 172.748 1.00 50.88 ?  33  VAL B CA    1 
ATOM   5786  C  C     . VAL B 1 33  ? 149.522 129.339 173.268 1.00 53.80 ?  33  VAL B C     1 
ATOM   5787  O  O     . VAL B 1 33  ? 150.333 129.902 172.521 1.00 55.05 ?  33  VAL B O     1 
ATOM   5788  C  CB    . VAL B 1 33  ? 147.077 129.981 172.980 1.00 45.90 ?  33  VAL B CB    1 
ATOM   5789  C  CG1   . VAL B 1 33  ? 146.925 130.317 174.451 1.00 47.37 ?  33  VAL B CG1   1 
ATOM   5790  C  CG2   . VAL B 1 33  ? 147.396 131.232 172.175 1.00 49.25 ?  33  VAL B CG2   1 
ATOM   5791  N  N     . HIS B 1 34  ? 149.806 129.086 174.550 1.00 51.44 ?  34  HIS B N     1 
ATOM   5792  C  CA    . HIS B 1 34  ? 151.122 129.418 175.086 1.00 47.49 ?  34  HIS B CA    1 
ATOM   5793  C  C     . HIS B 1 34  ? 152.216 128.637 174.372 1.00 48.88 ?  34  HIS B C     1 
ATOM   5794  O  O     . HIS B 1 34  ? 153.255 129.195 174.001 1.00 52.29 ?  34  HIS B O     1 
ATOM   5795  C  CB    . HIS B 1 34  ? 151.162 129.144 176.589 1.00 52.36 ?  34  HIS B CB    1 
ATOM   5796  C  CG    . HIS B 1 34  ? 152.475 129.475 177.226 1.00 53.70 ?  34  HIS B CG    1 
ATOM   5797  N  ND1   . HIS B 1 34  ? 153.490 128.553 177.360 1.00 52.99 ?  34  HIS B ND1   1 
ATOM   5798  C  CD2   . HIS B 1 34  ? 152.939 130.626 177.765 1.00 53.10 ?  34  HIS B CD2   1 
ATOM   5799  C  CE1   . HIS B 1 34  ? 154.524 129.121 177.955 1.00 51.59 ?  34  HIS B CE1   1 
ATOM   5800  N  NE2   . HIS B 1 34  ? 154.214 130.379 178.213 1.00 53.65 ?  34  HIS B NE2   1 
ATOM   5801  N  N     . SER B 1 35  ? 151.997 127.335 174.169 1.00 54.75 ?  35  SER B N     1 
ATOM   5802  C  CA    . SER B 1 35  ? 152.966 126.523 173.444 1.00 52.29 ?  35  SER B CA    1 
ATOM   5803  C  C     . SER B 1 35  ? 153.089 126.978 171.999 1.00 52.81 ?  35  SER B C     1 
ATOM   5804  O  O     . SER B 1 35  ? 154.200 127.072 171.467 1.00 55.62 ?  35  SER B O     1 
ATOM   5805  C  CB    . SER B 1 35  ? 152.569 125.049 173.511 1.00 52.45 ?  35  SER B CB    1 
ATOM   5806  O  OG    . SER B 1 35  ? 153.474 124.247 172.774 1.00 56.52 ?  35  SER B OG    1 
ATOM   5807  N  N     . TYR B 1 36  ? 151.958 127.273 171.351 1.00 49.85 ?  36  TYR B N     1 
ATOM   5808  C  CA    . TYR B 1 36  ? 151.986 127.767 169.979 1.00 50.26 ?  36  TYR B CA    1 
ATOM   5809  C  C     . TYR B 1 36  ? 152.868 128.996 169.866 1.00 47.90 ?  36  TYR B C     1 
ATOM   5810  O  O     . TYR B 1 36  ? 153.791 129.039 169.044 1.00 49.13 ?  36  TYR B O     1 
ATOM   5811  C  CB    . TYR B 1 36  ? 150.566 128.084 169.512 1.00 45.19 ?  36  TYR B CB    1 
ATOM   5812  C  CG    . TYR B 1 36  ? 150.488 128.657 168.116 1.00 43.48 ?  36  TYR B CG    1 
ATOM   5813  C  CD1   . TYR B 1 36  ? 151.145 128.048 167.057 1.00 44.00 ?  36  TYR B CD1   1 
ATOM   5814  C  CD2   . TYR B 1 36  ? 149.759 129.809 167.858 1.00 45.84 ?  36  TYR B CD2   1 
ATOM   5815  C  CE1   . TYR B 1 36  ? 151.074 128.565 165.780 1.00 46.30 ?  36  TYR B CE1   1 
ATOM   5816  C  CE2   . TYR B 1 36  ? 149.684 130.336 166.584 1.00 44.51 ?  36  TYR B CE2   1 
ATOM   5817  C  CZ    . TYR B 1 36  ? 150.344 129.710 165.550 1.00 46.87 ?  36  TYR B CZ    1 
ATOM   5818  O  OH    . TYR B 1 36  ? 150.274 130.230 164.279 1.00 47.50 ?  36  TYR B OH    1 
ATOM   5819  N  N     . PHE B 1 37  ? 152.624 129.995 170.715 1.00 51.88 ?  37  PHE B N     1 
ATOM   5820  C  CA    . PHE B 1 37  ? 153.456 131.190 170.700 1.00 50.44 ?  37  PHE B CA    1 
ATOM   5821  C  C     . PHE B 1 37  ? 154.915 130.837 170.945 1.00 51.90 ?  37  PHE B C     1 
ATOM   5822  O  O     . PHE B 1 37  ? 155.749 130.976 170.043 1.00 55.87 ?  37  PHE B O     1 
ATOM   5823  C  CB    . PHE B 1 37  ? 152.954 132.199 171.731 1.00 52.29 ?  37  PHE B CB    1 
ATOM   5824  C  CG    . PHE B 1 37  ? 152.091 133.269 171.141 1.00 53.14 ?  37  PHE B CG    1 
ATOM   5825  C  CD1   . PHE B 1 37  ? 152.658 134.408 170.600 1.00 51.94 ?  37  PHE B CD1   1 
ATOM   5826  C  CD2   . PHE B 1 37  ? 150.717 133.129 171.107 1.00 52.91 ?  37  PHE B CD2   1 
ATOM   5827  C  CE1   . PHE B 1 37  ? 151.870 135.391 170.048 1.00 53.84 ?  37  PHE B CE1   1 
ATOM   5828  C  CE2   . PHE B 1 37  ? 149.926 134.110 170.557 1.00 51.40 ?  37  PHE B CE2   1 
ATOM   5829  C  CZ    . PHE B 1 37  ? 150.502 135.241 170.025 1.00 51.87 ?  37  PHE B CZ    1 
ATOM   5830  N  N     . VAL B 1 38  ? 155.215 130.286 172.125 1.00 55.94 ?  38  VAL B N     1 
ATOM   5831  C  CA    . VAL B 1 38  ? 156.593 130.114 172.577 1.00 56.74 ?  38  VAL B CA    1 
ATOM   5832  C  C     . VAL B 1 38  ? 157.399 129.234 171.625 1.00 55.35 ?  38  VAL B C     1 
ATOM   5833  O  O     . VAL B 1 38  ? 158.619 129.399 171.505 1.00 57.62 ?  38  VAL B O     1 
ATOM   5834  C  CB    . VAL B 1 38  ? 156.582 129.562 174.020 1.00 54.50 ?  38  VAL B CB    1 
ATOM   5835  C  CG1   . VAL B 1 38  ? 157.822 128.736 174.320 1.00 56.35 ?  38  VAL B CG1   1 
ATOM   5836  C  CG2   . VAL B 1 38  ? 156.445 130.702 175.016 1.00 52.68 ?  38  VAL B CG2   1 
ATOM   5837  N  N     . ASP B 1 39  ? 156.746 128.320 170.905 1.00 53.36 ?  39  ASP B N     1 
ATOM   5838  C  CA    . ASP B 1 39  ? 157.465 127.387 170.051 1.00 52.42 ?  39  ASP B CA    1 
ATOM   5839  C  C     . ASP B 1 39  ? 157.479 127.775 168.579 1.00 57.74 ?  39  ASP B C     1 
ATOM   5840  O  O     . ASP B 1 39  ? 158.412 127.388 167.867 1.00 61.98 ?  39  ASP B O     1 
ATOM   5841  C  CB    . ASP B 1 39  ? 156.869 125.982 170.185 1.00 55.14 ?  39  ASP B CB    1 
ATOM   5842  C  CG    . ASP B 1 39  ? 156.992 125.430 171.589 1.00 60.48 ?  39  ASP B CG    1 
ATOM   5843  O  OD1   . ASP B 1 39  ? 157.594 126.109 172.446 1.00 59.89 ?  39  ASP B OD1   1 
ATOM   5844  O  OD2   . ASP B 1 39  ? 156.489 124.315 171.838 1.00 62.77 -1 39  ASP B OD2   1 
ATOM   5845  N  N     . TYR B 1 40  ? 156.487 128.517 168.089 1.00 58.16 ?  40  TYR B N     1 
ATOM   5846  C  CA    . TYR B 1 40  ? 156.419 128.846 166.673 1.00 55.81 ?  40  TYR B CA    1 
ATOM   5847  C  C     . TYR B 1 40  ? 156.452 130.341 166.411 1.00 59.41 ?  40  TYR B C     1 
ATOM   5848  O  O     . TYR B 1 40  ? 157.211 130.797 165.546 1.00 62.58 ?  40  TYR B O     1 
ATOM   5849  C  CB    . TYR B 1 40  ? 155.148 128.233 166.063 1.00 52.29 ?  40  TYR B CB    1 
ATOM   5850  C  CG    . TYR B 1 40  ? 155.072 128.329 164.558 1.00 56.35 ?  40  TYR B CG    1 
ATOM   5851  C  CD1   . TYR B 1 40  ? 155.798 127.464 163.752 1.00 56.20 ?  40  TYR B CD1   1 
ATOM   5852  C  CD2   . TYR B 1 40  ? 154.269 129.279 163.944 1.00 58.17 ?  40  TYR B CD2   1 
ATOM   5853  C  CE1   . TYR B 1 40  ? 155.730 127.547 162.375 1.00 57.45 ?  40  TYR B CE1   1 
ATOM   5854  C  CE2   . TYR B 1 40  ? 154.193 129.370 162.569 1.00 57.38 ?  40  TYR B CE2   1 
ATOM   5855  C  CZ    . TYR B 1 40  ? 154.926 128.501 161.789 1.00 59.93 ?  40  TYR B CZ    1 
ATOM   5856  O  OH    . TYR B 1 40  ? 154.854 128.588 160.418 1.00 61.60 ?  40  TYR B OH    1 
ATOM   5857  N  N     . ILE B 1 41  ? 155.649 131.124 167.132 1.00 54.61 ?  41  ILE B N     1 
ATOM   5858  C  CA    . ILE B 1 41  ? 155.479 132.530 166.780 1.00 54.22 ?  41  ILE B CA    1 
ATOM   5859  C  C     . ILE B 1 41  ? 156.722 133.325 167.155 1.00 53.52 ?  41  ILE B C     1 
ATOM   5860  O  O     . ILE B 1 41  ? 157.255 134.090 166.346 1.00 56.05 ?  41  ILE B O     1 
ATOM   5861  C  CB    . ILE B 1 41  ? 154.216 133.104 167.445 1.00 52.78 ?  41  ILE B CB    1 
ATOM   5862  C  CG1   . ILE B 1 41  ? 152.972 132.359 166.961 1.00 50.99 ?  41  ILE B CG1   1 
ATOM   5863  C  CG2   . ILE B 1 41  ? 154.091 134.590 167.154 1.00 51.98 ?  41  ILE B CG2   1 
ATOM   5864  C  CD1   . ILE B 1 41  ? 152.842 132.302 165.459 1.00 49.66 ?  41  ILE B CD1   1 
ATOM   5865  N  N     . ASN B 1 42  ? 157.207 133.146 168.385 1.00 52.27 ?  42  ASN B N     1 
ATOM   5866  C  CA    . ASN B 1 42  ? 158.407 133.857 168.811 1.00 54.55 ?  42  ASN B CA    1 
ATOM   5867  C  C     . ASN B 1 42  ? 159.628 133.421 168.013 1.00 56.60 ?  42  ASN B C     1 
ATOM   5868  O  O     . ASN B 1 42  ? 160.581 134.195 167.870 1.00 58.07 ?  42  ASN B O     1 
ATOM   5869  C  CB    . ASN B 1 42  ? 158.640 133.646 170.306 1.00 55.05 ?  42  ASN B CB    1 
ATOM   5870  C  CG    . ASN B 1 42  ? 157.509 134.195 171.153 1.00 56.64 ?  42  ASN B CG    1 
ATOM   5871  O  OD1   . ASN B 1 42  ? 156.517 134.701 170.629 1.00 59.11 ?  42  ASN B OD1   1 
ATOM   5872  N  ND2   . ASN B 1 42  ? 157.656 134.103 172.469 1.00 58.92 ?  42  ASN B ND2   1 
ATOM   5873  N  N     . GLN B 1 43  ? 159.621 132.195 167.490 1.00 59.89 ?  43  GLN B N     1 
ATOM   5874  C  CA    . GLN B 1 43  ? 160.714 131.740 166.638 1.00 57.85 ?  43  GLN B CA    1 
ATOM   5875  C  C     . GLN B 1 43  ? 160.628 132.345 165.242 1.00 58.98 ?  43  GLN B C     1 
ATOM   5876  O  O     . GLN B 1 43  ? 161.655 132.688 164.648 1.00 61.60 ?  43  GLN B O     1 
ATOM   5877  C  CB    . GLN B 1 43  ? 160.713 130.213 166.553 1.00 57.38 ?  43  GLN B CB    1 
ATOM   5878  C  CG    . GLN B 1 43  ? 161.576 129.526 167.601 1.00 60.30 ?  43  GLN B CG    1 
ATOM   5879  C  CD    . GLN B 1 43  ? 161.069 129.747 169.011 1.00 62.50 ?  43  GLN B CD    1 
ATOM   5880  O  OE1   . GLN B 1 43  ? 159.905 130.088 169.216 1.00 62.16 ?  43  GLN B OE1   1 
ATOM   5881  N  NE2   . GLN B 1 43  ? 161.942 129.556 169.992 1.00 60.18 ?  43  GLN B NE2   1 
ATOM   5882  N  N     . ASN B 1 44  ? 159.416 132.485 164.706 1.00 54.48 ?  44  ASN B N     1 
ATOM   5883  C  CA    . ASN B 1 44  ? 159.215 132.942 163.338 1.00 56.91 ?  44  ASN B CA    1 
ATOM   5884  C  C     . ASN B 1 44  ? 158.874 134.423 163.249 1.00 57.23 ?  44  ASN B C     1 
ATOM   5885  O  O     . ASN B 1 44  ? 158.534 134.904 162.164 1.00 55.75 ?  44  ASN B O     1 
ATOM   5886  C  CB    . ASN B 1 44  ? 158.121 132.112 162.661 1.00 54.58 ?  44  ASN B CB    1 
ATOM   5887  C  CG    . ASN B 1 44  ? 158.519 130.660 162.474 1.00 58.80 ?  44  ASN B CG    1 
ATOM   5888  O  OD1   . ASN B 1 44  ? 158.641 130.180 161.347 1.00 62.13 ?  44  ASN B OD1   1 
ATOM   5889  N  ND2   . ASN B 1 44  ? 158.711 129.948 163.578 1.00 57.89 ?  44  ASN B ND2   1 
ATOM   5890  N  N     . THR B 1 45  ? 158.957 135.156 164.354 1.00 57.35 ?  45  THR B N     1 
ATOM   5891  C  CA    . THR B 1 45  ? 158.711 136.592 164.351 1.00 58.16 ?  45  THR B CA    1 
ATOM   5892  C  C     . THR B 1 45  ? 160.028 137.325 164.128 1.00 57.10 ?  45  THR B C     1 
ATOM   5893  O  O     . THR B 1 45  ? 160.953 137.204 164.937 1.00 58.92 ?  45  THR B O     1 
ATOM   5894  C  CB    . THR B 1 45  ? 158.069 137.043 165.662 1.00 56.69 ?  45  THR B CB    1 
ATOM   5895  O  OG1   . THR B 1 45  ? 156.769 136.457 165.789 1.00 60.69 ?  45  THR B OG1   1 
ATOM   5896  C  CG2   . THR B 1 45  ? 157.944 138.559 165.699 1.00 54.98 ?  45  THR B CG2   1 
ATOM   5897  N  N     . VAL B 1 46  ? 160.112 138.076 163.031 1.00 56.57 ?  46  VAL B N     1 
ATOM   5898  C  CA    . VAL B 1 46  ? 161.289 138.898 162.783 1.00 56.20 ?  46  VAL B CA    1 
ATOM   5899  C  C     . VAL B 1 46  ? 161.366 139.983 163.846 1.00 57.03 ?  46  VAL B C     1 
ATOM   5900  O  O     . VAL B 1 46  ? 160.406 140.731 164.064 1.00 58.62 ?  46  VAL B O     1 
ATOM   5901  C  CB    . VAL B 1 46  ? 161.242 139.506 161.374 1.00 54.12 ?  46  VAL B CB    1 
ATOM   5902  C  CG1   . VAL B 1 46  ? 162.496 140.323 161.110 1.00 54.46 ?  46  VAL B CG1   1 
ATOM   5903  C  CG2   . VAL B 1 46  ? 161.086 138.421 160.335 1.00 54.07 ?  46  VAL B CG2   1 
ATOM   5904  N  N     . PHE B 1 47  ? 162.509 140.072 164.514 1.00 61.45 ?  47  PHE B N     1 
ATOM   5905  C  CA    . PHE B 1 47  ? 162.723 141.057 165.559 1.00 63.31 ?  47  PHE B CA    1 
ATOM   5906  C  C     . PHE B 1 47  ? 163.766 142.068 165.109 1.00 64.07 ?  47  PHE B C     1 
ATOM   5907  O  O     . PHE B 1 47  ? 164.738 141.717 164.433 1.00 63.48 ?  47  PHE B O     1 
ATOM   5908  C  CB    . PHE B 1 47  ? 163.164 140.398 166.866 1.00 62.59 ?  47  PHE B CB    1 
ATOM   5909  C  CG    . PHE B 1 47  ? 163.107 141.314 168.053 1.00 64.31 ?  47  PHE B CG    1 
ATOM   5910  C  CD1   . PHE B 1 47  ? 161.893 141.648 168.628 1.00 62.63 ?  47  PHE B CD1   1 
ATOM   5911  C  CD2   . PHE B 1 47  ? 164.266 141.846 168.592 1.00 63.97 ?  47  PHE B CD2   1 
ATOM   5912  C  CE1   . PHE B 1 47  ? 161.835 142.493 169.719 1.00 64.84 ?  47  PHE B CE1   1 
ATOM   5913  C  CE2   . PHE B 1 47  ? 164.216 142.692 169.683 1.00 63.35 ?  47  PHE B CE2   1 
ATOM   5914  C  CZ    . PHE B 1 47  ? 162.998 143.016 170.247 1.00 64.46 ?  47  PHE B CZ    1 
ATOM   5915  N  N     . PHE B 1 48  ? 163.552 143.324 165.485 1.00 61.83 ?  48  PHE B N     1 
ATOM   5916  C  CA    . PHE B 1 48  ? 164.445 144.417 165.152 1.00 57.75 ?  48  PHE B CA    1 
ATOM   5917  C  C     . PHE B 1 48  ? 164.932 145.066 166.439 1.00 60.79 ?  48  PHE B C     1 
ATOM   5918  O  O     . PHE B 1 48  ? 164.261 145.002 167.474 1.00 61.58 ?  48  PHE B O     1 
ATOM   5919  C  CB    . PHE B 1 48  ? 163.753 145.460 164.264 1.00 58.73 ?  48  PHE B CB    1 
ATOM   5920  C  CG    . PHE B 1 48  ? 163.210 144.904 162.975 1.00 57.73 ?  48  PHE B CG    1 
ATOM   5921  C  CD1   . PHE B 1 48  ? 162.042 144.160 162.957 1.00 57.85 ?  48  PHE B CD1   1 
ATOM   5922  C  CD2   . PHE B 1 48  ? 163.865 145.136 161.778 1.00 60.31 ?  48  PHE B CD2   1 
ATOM   5923  C  CE1   . PHE B 1 48  ? 161.542 143.657 161.773 1.00 59.31 ?  48  PHE B CE1   1 
ATOM   5924  C  CE2   . PHE B 1 48  ? 163.368 144.634 160.592 1.00 60.19 ?  48  PHE B CE2   1 
ATOM   5925  C  CZ    . PHE B 1 48  ? 162.206 143.894 160.590 1.00 57.88 ?  48  PHE B CZ    1 
ATOM   5926  N  N     . HIS B 1 49  ? 166.112 145.684 166.370 1.00 65.61 ?  49  HIS B N     1 
ATOM   5927  C  CA    . HIS B 1 49  ? 166.700 146.285 167.562 1.00 65.59 ?  49  HIS B CA    1 
ATOM   5928  C  C     . HIS B 1 49  ? 165.815 147.394 168.117 1.00 67.22 ?  49  HIS B C     1 
ATOM   5929  O  O     . HIS B 1 49  ? 165.667 147.529 169.336 1.00 67.83 ?  49  HIS B O     1 
ATOM   5930  C  CB    . HIS B 1 49  ? 168.098 146.817 167.247 1.00 66.47 ?  49  HIS B CB    1 
ATOM   5931  C  CG    . HIS B 1 49  ? 168.969 146.975 168.454 1.00 70.11 ?  49  HIS B CG    1 
ATOM   5932  N  ND1   . HIS B 1 49  ? 168.720 147.910 169.436 1.00 69.32 ?  49  HIS B ND1   1 
ATOM   5933  C  CD2   . HIS B 1 49  ? 170.087 146.315 168.839 1.00 69.08 ?  49  HIS B CD2   1 
ATOM   5934  C  CE1   . HIS B 1 49  ? 169.647 147.820 170.373 1.00 68.02 ?  49  HIS B CE1   1 
ATOM   5935  N  NE2   . HIS B 1 49  ? 170.488 146.859 170.035 1.00 68.93 ?  49  HIS B NE2   1 
ATOM   5936  N  N     . ASN B 1 50  ? 165.219 148.194 167.238 1.00 65.61 ?  50  ASN B N     1 
ATOM   5937  C  CA    . ASN B 1 50  ? 164.327 149.267 167.646 1.00 63.02 ?  50  ASN B CA    1 
ATOM   5938  C  C     . ASN B 1 50  ? 163.136 149.310 166.701 1.00 61.96 ?  50  ASN B C     1 
ATOM   5939  O  O     . ASN B 1 50  ? 163.155 148.721 165.619 1.00 61.45 ?  50  ASN B O     1 
ATOM   5940  C  CB    . ASN B 1 50  ? 165.046 150.621 167.664 1.00 61.90 ?  50  ASN B CB    1 
ATOM   5941  C  CG    . ASN B 1 50  ? 165.867 150.861 166.414 1.00 63.89 ?  50  ASN B CG    1 
ATOM   5942  O  OD1   . ASN B 1 50  ? 165.324 151.124 165.343 1.00 64.93 ?  50  ASN B OD1   1 
ATOM   5943  N  ND2   . ASN B 1 50  ? 167.184 150.769 166.546 1.00 64.38 ?  50  ASN B ND2   1 
ATOM   5944  N  N     . LEU B 1 51  ? 162.087 150.012 167.135 1.00 58.68 ?  51  LEU B N     1 
ATOM   5945  C  CA    . LEU B 1 51  ? 160.908 150.174 166.292 1.00 58.75 ?  51  LEU B CA    1 
ATOM   5946  C  C     . LEU B 1 51  ? 161.223 150.973 165.034 1.00 60.56 ?  51  LEU B C     1 
ATOM   5947  O  O     . LEU B 1 51  ? 160.602 150.752 163.989 1.00 62.00 ?  51  LEU B O     1 
ATOM   5948  C  CB    . LEU B 1 51  ? 159.786 150.845 167.084 1.00 58.13 ?  51  LEU B CB    1 
ATOM   5949  C  CG    . LEU B 1 51  ? 158.501 151.190 166.330 1.00 57.06 ?  51  LEU B CG    1 
ATOM   5950  C  CD1   . LEU B 1 51  ? 157.880 149.946 165.714 1.00 54.72 ?  51  LEU B CD1   1 
ATOM   5951  C  CD2   . LEU B 1 51  ? 157.517 151.886 167.249 1.00 57.42 ?  51  LEU B CD2   1 
ATOM   5952  N  N     . LYS B 1 52  ? 162.180 151.901 165.115 1.00 59.05 ?  52  LYS B N     1 
ATOM   5953  C  CA    . LYS B 1 52  ? 162.556 152.684 163.941 1.00 57.11 ?  52  LYS B CA    1 
ATOM   5954  C  C     . LYS B 1 52  ? 163.105 151.792 162.835 1.00 60.44 ?  52  LYS B C     1 
ATOM   5955  O  O     . LYS B 1 52  ? 162.757 151.962 161.661 1.00 61.28 ?  52  LYS B O     1 
ATOM   5956  C  CB    . LYS B 1 52  ? 163.583 153.745 164.330 1.00 56.54 ?  52  LYS B CB    1 
ATOM   5957  C  CG    . LYS B 1 52  ? 163.549 154.994 163.469 1.00 60.79 ?  52  LYS B CG    1 
ATOM   5958  C  CD    . LYS B 1 52  ? 164.706 155.921 163.807 1.00 63.71 ?  52  LYS B CD    1 
ATOM   5959  C  CE    . LYS B 1 52  ? 164.411 156.745 165.049 1.00 60.86 ?  52  LYS B CE    1 
ATOM   5960  N  NZ    . LYS B 1 52  ? 165.561 156.764 165.993 1.00 61.13 1  52  LYS B NZ    1 
ATOM   5961  N  N     . GLU B 1 53  ? 163.964 150.834 163.193 1.00 62.10 ?  53  GLU B N     1 
ATOM   5962  C  CA    . GLU B 1 53  ? 164.512 149.922 162.195 1.00 60.79 ?  53  GLU B CA    1 
ATOM   5963  C  C     . GLU B 1 53  ? 163.417 149.072 161.566 1.00 61.00 ?  53  GLU B C     1 
ATOM   5964  O  O     . GLU B 1 53  ? 163.411 148.854 160.349 1.00 61.80 ?  53  GLU B O     1 
ATOM   5965  C  CB    . GLU B 1 53  ? 165.583 149.036 162.828 1.00 60.31 ?  53  GLU B CB    1 
ATOM   5966  C  CG    . GLU B 1 53  ? 166.527 148.394 161.826 1.00 62.43 ?  53  GLU B CG    1 
ATOM   5967  C  CD    . GLU B 1 53  ? 166.797 146.935 162.132 1.00 65.53 ?  53  GLU B CD    1 
ATOM   5968  O  OE1   . GLU B 1 53  ? 166.950 146.593 163.323 1.00 66.13 ?  53  GLU B OE1   1 
ATOM   5969  O  OE2   . GLU B 1 53  ? 166.858 146.129 161.179 1.00 64.07 -1 53  GLU B OE2   1 
ATOM   5970  N  N     . LYS B 1 54  ? 162.477 148.585 162.381 1.00 58.53 ?  54  LYS B N     1 
ATOM   5971  C  CA    . LYS B 1 54  ? 161.375 147.785 161.855 1.00 58.25 ?  54  LYS B CA    1 
ATOM   5972  C  C     . LYS B 1 54  ? 160.520 148.599 160.893 1.00 54.87 ?  54  LYS B C     1 
ATOM   5973  O  O     . LYS B 1 54  ? 160.163 148.128 159.806 1.00 56.61 ?  54  LYS B O     1 
ATOM   5974  C  CB    . LYS B 1 54  ? 160.524 147.250 163.004 1.00 56.86 ?  54  LYS B CB    1 
ATOM   5975  C  CG    . LYS B 1 54  ? 159.206 146.641 162.560 1.00 56.41 ?  54  LYS B CG    1 
ATOM   5976  C  CD    . LYS B 1 54  ? 158.522 145.912 163.699 1.00 57.38 ?  54  LYS B CD    1 
ATOM   5977  C  CE    . LYS B 1 54  ? 157.208 145.301 163.245 1.00 59.39 ?  54  LYS B CE    1 
ATOM   5978  N  NZ    . LYS B 1 54  ? 156.775 144.195 164.143 1.00 59.58 1  54  LYS B NZ    1 
ATOM   5979  N  N     . LEU B 1 55  ? 160.189 149.832 161.276 1.00 55.55 ?  55  LEU B N     1 
ATOM   5980  C  CA    . LEU B 1 55  ? 159.368 150.677 160.417 1.00 56.17 ?  55  LEU B CA    1 
ATOM   5981  C  C     . LEU B 1 55  ? 160.083 150.999 159.115 1.00 59.21 ?  55  LEU B C     1 
ATOM   5982  O  O     . LEU B 1 55  ? 159.469 150.979 158.043 1.00 63.12 ?  55  LEU B O     1 
ATOM   5983  C  CB    . LEU B 1 55  ? 158.986 151.959 161.154 1.00 57.73 ?  55  LEU B CB    1 
ATOM   5984  C  CG    . LEU B 1 55  ? 157.931 151.804 162.249 1.00 57.81 ?  55  LEU B CG    1 
ATOM   5985  C  CD1   . LEU B 1 55  ? 157.763 153.106 163.006 1.00 58.16 ?  55  LEU B CD1   1 
ATOM   5986  C  CD2   . LEU B 1 55  ? 156.607 151.344 161.660 1.00 57.18 ?  55  LEU B CD2   1 
ATOM   5987  N  N     . ASP B 1 56  ? 161.384 151.300 159.189 1.00 60.82 ?  56  ASP B N     1 
ATOM   5988  C  CA    . ASP B 1 56  ? 162.153 151.589 157.982 1.00 60.69 ?  56  ASP B CA    1 
ATOM   5989  C  C     . ASP B 1 56  ? 162.214 150.375 157.066 1.00 59.63 ?  56  ASP B C     1 
ATOM   5990  O  O     . ASP B 1 56  ? 162.052 150.500 155.844 1.00 62.40 ?  56  ASP B O     1 
ATOM   5991  C  CB    . ASP B 1 56  ? 163.560 152.051 158.357 1.00 62.18 ?  56  ASP B CB    1 
ATOM   5992  C  CG    . ASP B 1 56  ? 163.652 153.553 158.528 1.00 64.79 ?  56  ASP B CG    1 
ATOM   5993  O  OD1   . ASP B 1 56  ? 164.595 154.018 159.202 1.00 65.13 ?  56  ASP B OD1   1 
ATOM   5994  O  OD2   . ASP B 1 56  ? 162.782 154.269 157.989 1.00 63.28 -1 56  ASP B OD2   1 
ATOM   5995  N  N     . TYR B 1 57  ? 162.438 149.188 157.638 1.00 55.20 ?  57  TYR B N     1 
ATOM   5996  C  CA    . TYR B 1 57  ? 162.445 147.968 156.840 1.00 56.47 ?  57  TYR B CA    1 
ATOM   5997  C  C     . TYR B 1 57  ? 161.097 147.743 156.173 1.00 57.12 ?  57  TYR B C     1 
ATOM   5998  O  O     . TYR B 1 57  ? 161.033 147.332 155.010 1.00 58.36 ?  57  TYR B O     1 
ATOM   5999  C  CB    . TYR B 1 57  ? 162.816 146.771 157.716 1.00 57.82 ?  57  TYR B CB    1 
ATOM   6000  C  CG    . TYR B 1 57  ? 162.677 145.429 157.028 1.00 57.26 ?  57  TYR B CG    1 
ATOM   6001  C  CD1   . TYR B 1 57  ? 163.702 144.918 156.246 1.00 57.59 ?  57  TYR B CD1   1 
ATOM   6002  C  CD2   . TYR B 1 57  ? 161.522 144.670 157.170 1.00 58.80 ?  57  TYR B CD2   1 
ATOM   6003  C  CE1   . TYR B 1 57  ? 163.579 143.694 155.618 1.00 57.28 ?  57  TYR B CE1   1 
ATOM   6004  C  CE2   . TYR B 1 57  ? 161.390 143.449 156.546 1.00 59.93 ?  57  TYR B CE2   1 
ATOM   6005  C  CZ    . TYR B 1 57  ? 162.421 142.964 155.772 1.00 60.41 ?  57  TYR B CZ    1 
ATOM   6006  O  OH    . TYR B 1 57  ? 162.291 141.744 155.150 1.00 60.67 ?  57  TYR B OH    1 
ATOM   6007  N  N     . LEU B 1 58  ? 160.007 148.005 156.894 1.00 55.53 ?  58  LEU B N     1 
ATOM   6008  C  CA    . LEU B 1 58  ? 158.687 147.738 156.338 1.00 55.09 ?  58  LEU B CA    1 
ATOM   6009  C  C     . LEU B 1 58  ? 158.327 148.731 155.237 1.00 52.51 ?  58  LEU B C     1 
ATOM   6010  O  O     . LEU B 1 58  ? 157.740 148.343 154.221 1.00 54.87 ?  58  LEU B O     1 
ATOM   6011  C  CB    . LEU B 1 58  ? 157.642 147.743 157.453 1.00 53.67 ?  58  LEU B CB    1 
ATOM   6012  C  CG    . LEU B 1 58  ? 157.759 146.531 158.384 1.00 53.10 ?  58  LEU B CG    1 
ATOM   6013  C  CD1   . LEU B 1 58  ? 156.939 146.712 159.648 1.00 53.31 ?  58  LEU B CD1   1 
ATOM   6014  C  CD2   . LEU B 1 58  ? 157.357 145.258 157.660 1.00 51.72 ?  58  LEU B CD2   1 
ATOM   6015  N  N     . VAL B 1 59  ? 158.663 150.012 155.409 1.00 55.94 ?  59  VAL B N     1 
ATOM   6016  C  CA    . VAL B 1 59  ? 158.321 150.977 154.365 1.00 59.41 ?  59  VAL B CA    1 
ATOM   6017  C  C     . VAL B 1 59  ? 159.214 150.788 153.145 1.00 61.68 ?  59  VAL B C     1 
ATOM   6018  O  O     . VAL B 1 59  ? 158.744 150.845 152.002 1.00 58.99 ?  59  VAL B O     1 
ATOM   6019  C  CB    . VAL B 1 59  ? 158.386 152.427 154.886 1.00 58.77 ?  59  VAL B CB    1 
ATOM   6020  C  CG1   . VAL B 1 59  ? 157.161 152.753 155.733 1.00 57.57 ?  59  VAL B CG1   1 
ATOM   6021  C  CG2   . VAL B 1 59  ? 159.689 152.714 155.609 1.00 59.07 ?  59  VAL B CG2   1 
ATOM   6022  N  N     . GLU B 1 60  ? 160.514 150.559 153.360 1.00 62.25 ?  60  GLU B N     1 
ATOM   6023  C  CA    . GLU B 1 60  ? 161.445 150.498 152.238 1.00 60.57 ?  60  GLU B CA    1 
ATOM   6024  C  C     . GLU B 1 60  ? 161.337 149.192 151.459 1.00 61.73 ?  60  GLU B C     1 
ATOM   6025  O  O     . GLU B 1 60  ? 161.664 149.162 150.268 1.00 64.04 ?  60  GLU B O     1 
ATOM   6026  C  CB    . GLU B 1 60  ? 162.878 150.716 152.731 1.00 60.61 ?  60  GLU B CB    1 
ATOM   6027  C  CG    . GLU B 1 60  ? 163.602 149.462 153.183 1.00 61.74 ?  60  GLU B CG    1 
ATOM   6028  C  CD    . GLU B 1 60  ? 164.831 149.770 154.018 1.00 64.83 ?  60  GLU B CD    1 
ATOM   6029  O  OE1   . GLU B 1 60  ? 165.125 150.966 154.227 1.00 64.26 ?  60  GLU B OE1   1 
ATOM   6030  O  OE2   . GLU B 1 60  ? 165.500 148.816 154.467 1.00 61.61 -1 60  GLU B OE2   1 
ATOM   6031  N  N     . ASN B 1 61  ? 160.887 148.111 152.097 1.00 57.46 ?  61  ASN B N     1 
ATOM   6032  C  CA    . ASN B 1 61  ? 160.715 146.831 151.424 1.00 57.98 ?  61  ASN B CA    1 
ATOM   6033  C  C     . ASN B 1 61  ? 159.311 146.647 150.862 1.00 57.86 ?  61  ASN B C     1 
ATOM   6034  O  O     . ASN B 1 61  ? 158.892 145.506 150.632 1.00 59.49 ?  61  ASN B O     1 
ATOM   6035  C  CB    . ASN B 1 61  ? 161.055 145.679 152.371 1.00 59.20 ?  61  ASN B CB    1 
ATOM   6036  C  CG    . ASN B 1 61  ? 162.546 145.448 152.493 1.00 61.20 ?  61  ASN B CG    1 
ATOM   6037  O  OD1   . ASN B 1 61  ? 163.110 144.591 151.815 1.00 60.39 ?  61  ASN B OD1   1 
ATOM   6038  N  ND2   . ASN B 1 61  ? 163.193 146.215 153.360 1.00 60.53 ?  61  ASN B ND2   1 
ATOM   6039  N  N     . GLN B 1 62  ? 158.580 147.742 150.646 1.00 56.47 ?  62  GLN B N     1 
ATOM   6040  C  CA    . GLN B 1 62  ? 157.262 147.714 150.009 1.00 58.76 ?  62  GLN B CA    1 
ATOM   6041  C  C     . GLN B 1 62  ? 156.260 146.882 150.808 1.00 57.86 ?  62  GLN B C     1 
ATOM   6042  O  O     . GLN B 1 62  ? 155.476 146.115 150.246 1.00 59.50 ?  62  GLN B O     1 
ATOM   6043  C  CB    . GLN B 1 62  ? 157.358 147.211 148.566 1.00 58.26 ?  62  GLN B CB    1 
ATOM   6044  C  CG    . GLN B 1 62  ? 158.322 148.001 147.696 1.00 58.23 ?  62  GLN B CG    1 
ATOM   6045  C  CD    . GLN B 1 62  ? 157.992 149.479 147.653 1.00 61.67 ?  62  GLN B CD    1 
ATOM   6046  O  OE1   . GLN B 1 62  ? 158.575 150.280 148.382 1.00 60.56 ?  62  GLN B OE1   1 
ATOM   6047  N  NE2   . GLN B 1 62  ? 157.048 149.849 146.796 1.00 59.67 ?  62  GLN B NE2   1 
ATOM   6048  N  N     . TYR B 1 63  ? 156.283 147.036 152.130 1.00 56.30 ?  63  TYR B N     1 
ATOM   6049  C  CA    . TYR B 1 63  ? 155.300 146.404 153.000 1.00 55.71 ?  63  TYR B CA    1 
ATOM   6050  C  C     . TYR B 1 63  ? 154.256 147.384 153.515 1.00 54.98 ?  63  TYR B C     1 
ATOM   6051  O  O     . TYR B 1 63  ? 153.072 147.042 153.581 1.00 55.89 ?  63  TYR B O     1 
ATOM   6052  C  CB    . TYR B 1 63  ? 155.989 145.732 154.192 1.00 52.99 ?  63  TYR B CB    1 
ATOM   6053  C  CG    . TYR B 1 63  ? 156.707 144.450 153.847 1.00 55.76 ?  63  TYR B CG    1 
ATOM   6054  C  CD1   . TYR B 1 63  ? 156.031 143.391 153.256 1.00 53.23 ?  63  TYR B CD1   1 
ATOM   6055  C  CD2   . TYR B 1 63  ? 158.060 144.295 154.116 1.00 55.99 ?  63  TYR B CD2   1 
ATOM   6056  C  CE1   . TYR B 1 63  ? 156.683 142.218 152.942 1.00 54.08 ?  63  TYR B CE1   1 
ATOM   6057  C  CE2   . TYR B 1 63  ? 158.719 143.126 153.805 1.00 55.25 ?  63  TYR B CE2   1 
ATOM   6058  C  CZ    . TYR B 1 63  ? 158.027 142.090 153.219 1.00 58.33 ?  63  TYR B CZ    1 
ATOM   6059  O  OH    . TYR B 1 63  ? 158.683 140.922 152.907 1.00 61.61 ?  63  TYR B OH    1 
ATOM   6060  N  N     . TYR B 1 64  ? 154.669 148.593 153.877 1.00 51.12 ?  64  TYR B N     1 
ATOM   6061  C  CA    . TYR B 1 64  ? 153.777 149.627 154.378 1.00 49.36 ?  64  TYR B CA    1 
ATOM   6062  C  C     . TYR B 1 64  ? 153.671 150.762 153.370 1.00 51.84 ?  64  TYR B C     1 
ATOM   6063  O  O     . TYR B 1 64  ? 154.353 150.787 152.342 1.00 56.22 ?  64  TYR B O     1 
ATOM   6064  C  CB    . TYR B 1 64  ? 154.272 150.171 155.721 1.00 51.22 ?  64  TYR B CB    1 
ATOM   6065  C  CG    . TYR B 1 64  ? 153.992 149.276 156.899 1.00 49.14 ?  64  TYR B CG    1 
ATOM   6066  C  CD1   . TYR B 1 64  ? 153.242 148.117 156.756 1.00 47.95 ?  64  TYR B CD1   1 
ATOM   6067  C  CD2   . TYR B 1 64  ? 154.476 149.591 158.159 1.00 50.77 ?  64  TYR B CD2   1 
ATOM   6068  C  CE1   . TYR B 1 64  ? 152.986 147.297 157.834 1.00 45.37 ?  64  TYR B CE1   1 
ATOM   6069  C  CE2   . TYR B 1 64  ? 154.225 148.780 159.240 1.00 50.87 ?  64  TYR B CE2   1 
ATOM   6070  C  CZ    . TYR B 1 64  ? 153.480 147.634 159.073 1.00 50.19 ?  64  TYR B CZ    1 
ATOM   6071  O  OH    . TYR B 1 64  ? 153.232 146.825 160.155 1.00 55.95 ?  64  TYR B OH    1 
ATOM   6072  N  N     . GLU B 1 65  ? 152.802 151.715 153.686 1.00 56.36 ?  65  GLU B N     1 
ATOM   6073  C  CA    . GLU B 1 65  ? 152.665 152.942 152.917 1.00 57.07 ?  65  GLU B CA    1 
ATOM   6074  C  C     . GLU B 1 65  ? 153.335 154.079 153.676 1.00 58.36 ?  65  GLU B C     1 
ATOM   6075  O  O     . GLU B 1 65  ? 153.036 154.306 154.853 1.00 59.05 ?  65  GLU B O     1 
ATOM   6076  C  CB    . GLU B 1 65  ? 151.193 153.272 152.661 1.00 54.02 ?  65  GLU B CB    1 
ATOM   6077  C  CG    . GLU B 1 65  ? 150.474 152.272 151.773 1.00 52.75 ?  65  GLU B CG    1 
ATOM   6078  C  CD    . GLU B 1 65  ? 148.977 152.509 151.728 1.00 59.36 ?  65  GLU B CD    1 
ATOM   6079  O  OE1   . GLU B 1 65  ? 148.367 152.682 152.803 1.00 59.54 ?  65  GLU B OE1   1 
ATOM   6080  O  OE2   . GLU B 1 65  ? 148.409 152.524 150.615 1.00 56.85 -1 65  GLU B OE2   1 
ATOM   6081  N  N     . GLU B 1 66  ? 154.245 154.784 153.004 1.00 58.13 ?  66  GLU B N     1 
ATOM   6082  C  CA    . GLU B 1 66  ? 154.932 155.898 153.644 1.00 59.42 ?  66  GLU B CA    1 
ATOM   6083  C  C     . GLU B 1 66  ? 154.020 157.101 153.842 1.00 60.55 ?  66  GLU B C     1 
ATOM   6084  O  O     . GLU B 1 66  ? 154.320 157.959 154.678 1.00 58.82 ?  66  GLU B O     1 
ATOM   6085  C  CB    . GLU B 1 66  ? 156.158 156.298 152.818 1.00 61.14 ?  66  GLU B CB    1 
ATOM   6086  C  CG    . GLU B 1 66  ? 157.168 157.200 153.531 1.00 61.57 ?  66  GLU B CG    1 
ATOM   6087  C  CD    . GLU B 1 66  ? 157.493 156.750 154.947 1.00 65.09 ?  66  GLU B CD    1 
ATOM   6088  O  OE1   . GLU B 1 66  ? 156.729 157.078 155.879 1.00 63.13 ?  66  GLU B OE1   1 
ATOM   6089  O  OE2   . GLU B 1 66  ? 158.522 156.065 155.128 1.00 62.81 -1 66  GLU B OE2   1 
ATOM   6090  N  N     . GLU B 1 67  ? 152.911 157.178 153.102 1.00 58.11 ?  67  GLU B N     1 
ATOM   6091  C  CA    . GLU B 1 67  ? 152.054 158.358 153.162 1.00 55.39 ?  67  GLU B CA    1 
ATOM   6092  C  C     . GLU B 1 67  ? 151.414 158.518 154.535 1.00 59.38 ?  67  GLU B C     1 
ATOM   6093  O  O     . GLU B 1 67  ? 151.472 159.599 155.133 1.00 60.34 ?  67  GLU B O     1 
ATOM   6094  C  CB    . GLU B 1 67  ? 150.981 158.278 152.076 1.00 57.45 ?  67  GLU B CB    1 
ATOM   6095  C  CG    . GLU B 1 67  ? 151.532 158.181 150.665 1.00 58.19 ?  67  GLU B CG    1 
ATOM   6096  C  CD    . GLU B 1 67  ? 151.588 156.754 150.160 1.00 61.21 ?  67  GLU B CD    1 
ATOM   6097  O  OE1   . GLU B 1 67  ? 150.515 156.175 149.890 1.00 62.20 ?  67  GLU B OE1   1 
ATOM   6098  O  OE2   . GLU B 1 67  ? 152.706 156.212 150.030 1.00 62.48 -1 67  GLU B OE2   1 
ATOM   6099  N  N     . PHE B 1 68  ? 150.797 157.455 155.054 1.00 53.85 ?  68  PHE B N     1 
ATOM   6100  C  CA    . PHE B 1 68  ? 150.099 157.567 156.330 1.00 49.12 ?  68  PHE B CA    1 
ATOM   6101  C  C     . PHE B 1 68  ? 151.060 157.604 157.510 1.00 50.48 ?  68  PHE B C     1 
ATOM   6102  O  O     . PHE B 1 68  ? 150.754 158.230 158.530 1.00 54.75 ?  68  PHE B O     1 
ATOM   6103  C  CB    . PHE B 1 68  ? 149.087 156.425 156.484 1.00 49.06 ?  68  PHE B CB    1 
ATOM   6104  C  CG    . PHE B 1 68  ? 149.653 155.173 157.096 1.00 45.75 ?  68  PHE B CG    1 
ATOM   6105  C  CD1   . PHE B 1 68  ? 150.292 154.232 156.309 1.00 48.64 ?  68  PHE B CD1   1 
ATOM   6106  C  CD2   . PHE B 1 68  ? 149.516 154.921 158.452 1.00 45.10 ?  68  PHE B CD2   1 
ATOM   6107  C  CE1   . PHE B 1 68  ? 150.808 153.078 156.865 1.00 48.69 ?  68  PHE B CE1   1 
ATOM   6108  C  CE2   . PHE B 1 68  ? 150.030 153.768 159.012 1.00 47.79 ?  68  PHE B CE2   1 
ATOM   6109  C  CZ    . PHE B 1 68  ? 150.672 152.845 158.216 1.00 48.99 ?  68  PHE B CZ    1 
ATOM   6110  N  N     . LEU B 1 69  ? 152.217 156.947 157.399 1.00 48.84 ?  69  LEU B N     1 
ATOM   6111  C  CA    . LEU B 1 69  ? 153.188 156.980 158.486 1.00 50.00 ?  69  LEU B CA    1 
ATOM   6112  C  C     . LEU B 1 69  ? 153.914 158.315 158.564 1.00 53.07 ?  69  LEU B C     1 
ATOM   6113  O  O     . LEU B 1 69  ? 154.356 158.711 159.648 1.00 50.57 ?  69  LEU B O     1 
ATOM   6114  C  CB    . LEU B 1 69  ? 154.196 155.842 158.330 1.00 50.19 ?  69  LEU B CB    1 
ATOM   6115  C  CG    . LEU B 1 69  ? 153.731 154.480 158.846 1.00 49.96 ?  69  LEU B CG    1 
ATOM   6116  C  CD1   . LEU B 1 69  ? 154.722 153.391 158.472 1.00 50.10 ?  69  LEU B CD1   1 
ATOM   6117  C  CD2   . LEU B 1 69  ? 153.518 154.524 160.350 1.00 50.65 ?  69  LEU B CD2   1 
ATOM   6118  N  N     . SER B 1 70  ? 154.046 159.020 157.439 1.00 57.68 ?  70  SER B N     1 
ATOM   6119  C  CA    . SER B 1 70  ? 154.694 160.327 157.447 1.00 54.92 ?  70  SER B CA    1 
ATOM   6120  C  C     . SER B 1 70  ? 153.865 161.380 158.165 1.00 51.98 ?  70  SER B C     1 
ATOM   6121  O  O     . SER B 1 70  ? 154.390 162.451 158.486 1.00 53.93 ?  70  SER B O     1 
ATOM   6122  C  CB    . SER B 1 70  ? 154.981 160.785 156.017 1.00 53.34 ?  70  SER B CB    1 
ATOM   6123  O  OG    . SER B 1 70  ? 153.810 160.732 155.224 1.00 54.26 ?  70  SER B OG    1 
ATOM   6124  N  N     . LEU B 1 71  ? 152.585 161.104 158.418 1.00 46.56 ?  71  LEU B N     1 
ATOM   6125  C  CA    . LEU B 1 71  ? 151.720 162.056 159.102 1.00 46.13 ?  71  LEU B CA    1 
ATOM   6126  C  C     . LEU B 1 71  ? 152.063 162.210 160.576 1.00 47.72 ?  71  LEU B C     1 
ATOM   6127  O  O     . LEU B 1 71  ? 151.559 163.138 161.217 1.00 50.28 ?  71  LEU B O     1 
ATOM   6128  C  CB    . LEU B 1 71  ? 150.259 161.629 158.954 1.00 46.23 ?  71  LEU B CB    1 
ATOM   6129  C  CG    . LEU B 1 71  ? 149.630 161.865 157.580 1.00 50.87 ?  71  LEU B CG    1 
ATOM   6130  C  CD1   . LEU B 1 71  ? 148.119 161.852 157.678 1.00 48.61 ?  71  LEU B CD1   1 
ATOM   6131  C  CD2   . LEU B 1 71  ? 150.118 163.175 156.983 1.00 49.17 ?  71  LEU B CD2   1 
ATOM   6132  N  N     . TYR B 1 72  ? 152.900 161.334 161.124 1.00 45.28 ?  72  TYR B N     1 
ATOM   6133  C  CA    . TYR B 1 72  ? 153.298 161.385 162.522 1.00 44.42 ?  72  TYR B CA    1 
ATOM   6134  C  C     . TYR B 1 72  ? 154.810 161.507 162.624 1.00 48.54 ?  72  TYR B C     1 
ATOM   6135  O  O     . TYR B 1 72  ? 155.544 160.949 161.803 1.00 50.77 ?  72  TYR B O     1 
ATOM   6136  C  CB    . TYR B 1 72  ? 152.855 160.129 163.284 1.00 46.60 ?  72  TYR B CB    1 
ATOM   6137  C  CG    . TYR B 1 72  ? 151.420 159.715 163.066 1.00 44.13 ?  72  TYR B CG    1 
ATOM   6138  C  CD1   . TYR B 1 72  ? 151.066 158.907 161.995 1.00 40.51 ?  72  TYR B CD1   1 
ATOM   6139  C  CD2   . TYR B 1 72  ? 150.422 160.111 163.945 1.00 45.33 ?  72  TYR B CD2   1 
ATOM   6140  C  CE1   . TYR B 1 72  ? 149.761 158.523 161.794 1.00 40.64 ?  72  TYR B CE1   1 
ATOM   6141  C  CE2   . TYR B 1 72  ? 149.113 159.728 163.754 1.00 41.64 ?  72  TYR B CE2   1 
ATOM   6142  C  CZ    . TYR B 1 72  ? 148.789 158.933 162.676 1.00 42.12 ?  72  TYR B CZ    1 
ATOM   6143  O  OH    . TYR B 1 72  ? 147.486 158.548 162.479 1.00 47.11 ?  72  TYR B OH    1 
ATOM   6144  N  N     . SER B 1 73  ? 155.270 162.239 163.632 1.00 54.10 ?  73  SER B N     1 
ATOM   6145  C  CA    . SER B 1 73  ? 156.658 162.118 164.043 1.00 54.69 ?  73  SER B CA    1 
ATOM   6146  C  C     . SER B 1 73  ? 156.890 160.727 164.617 1.00 54.99 ?  73  SER B C     1 
ATOM   6147  O  O     . SER B 1 73  ? 155.970 160.090 165.137 1.00 58.63 ?  73  SER B O     1 
ATOM   6148  C  CB    . SER B 1 73  ? 157.010 163.187 165.076 1.00 53.07 ?  73  SER B CB    1 
ATOM   6149  O  OG    . SER B 1 73  ? 156.377 162.923 166.315 1.00 51.89 ?  73  SER B OG    1 
ATOM   6150  N  N     . PHE B 1 74  ? 158.129 160.243 164.507 1.00 56.10 ?  74  PHE B N     1 
ATOM   6151  C  CA    . PHE B 1 74  ? 158.409 158.888 164.969 1.00 55.84 ?  74  PHE B CA    1 
ATOM   6152  C  C     . PHE B 1 74  ? 158.143 158.732 166.461 1.00 55.08 ?  74  PHE B C     1 
ATOM   6153  O  O     . PHE B 1 74  ? 157.851 157.625 166.923 1.00 60.39 ?  74  PHE B O     1 
ATOM   6154  C  CB    . PHE B 1 74  ? 159.848 158.486 164.659 1.00 56.32 ?  74  PHE B CB    1 
ATOM   6155  C  CG    . PHE B 1 74  ? 160.234 157.165 165.255 1.00 57.06 ?  74  PHE B CG    1 
ATOM   6156  C  CD1   . PHE B 1 74  ? 159.686 155.990 164.768 1.00 56.22 ?  74  PHE B CD1   1 
ATOM   6157  C  CD2   . PHE B 1 74  ? 161.111 157.097 166.323 1.00 57.99 ?  74  PHE B CD2   1 
ATOM   6158  C  CE1   . PHE B 1 74  ? 160.022 154.773 165.320 1.00 58.61 ?  74  PHE B CE1   1 
ATOM   6159  C  CE2   . PHE B 1 74  ? 161.452 155.882 166.879 1.00 57.74 ?  74  PHE B CE2   1 
ATOM   6160  C  CZ    . PHE B 1 74  ? 160.905 154.719 166.377 1.00 59.91 ?  74  PHE B CZ    1 
ATOM   6161  N  N     . GLU B 1 75  ? 158.237 159.819 167.229 1.00 54.53 ?  75  GLU B N     1 
ATOM   6162  C  CA    . GLU B 1 75  ? 157.914 159.739 168.649 1.00 58.15 ?  75  GLU B CA    1 
ATOM   6163  C  C     . GLU B 1 75  ? 156.450 159.371 168.857 1.00 60.11 ?  75  GLU B C     1 
ATOM   6164  O  O     . GLU B 1 75  ? 156.122 158.563 169.733 1.00 60.42 ?  75  GLU B O     1 
ATOM   6165  C  CB    . GLU B 1 75  ? 158.240 161.064 169.337 1.00 56.36 ?  75  GLU B CB    1 
ATOM   6166  C  CG    . GLU B 1 75  ? 159.724 161.375 169.398 1.00 56.59 ?  75  GLU B CG    1 
ATOM   6167  C  CD    . GLU B 1 75  ? 160.539 160.217 169.941 1.00 63.42 ?  75  GLU B CD    1 
ATOM   6168  O  OE1   . GLU B 1 75  ? 160.297 159.807 171.097 1.00 63.49 ?  75  GLU B OE1   1 
ATOM   6169  O  OE2   . GLU B 1 75  ? 161.420 159.714 169.213 1.00 62.13 -1 75  GLU B OE2   1 
ATOM   6170  N  N     . ASP B 1 76  ? 155.556 159.949 168.053 1.00 55.72 ?  76  ASP B N     1 
ATOM   6171  C  CA    . ASP B 1 76  ? 154.136 159.631 168.171 1.00 54.37 ?  76  ASP B CA    1 
ATOM   6172  C  C     . ASP B 1 76  ? 153.862 158.175 167.814 1.00 55.43 ?  76  ASP B C     1 
ATOM   6173  O  O     . ASP B 1 76  ? 153.075 157.500 168.487 1.00 58.92 ?  76  ASP B O     1 
ATOM   6174  C  CB    . ASP B 1 76  ? 153.320 160.566 167.282 1.00 55.73 ?  76  ASP B CB    1 
ATOM   6175  C  CG    . ASP B 1 76  ? 153.426 162.014 167.710 1.00 58.99 ?  76  ASP B CG    1 
ATOM   6176  O  OD1   . ASP B 1 76  ? 153.445 162.274 168.932 1.00 59.14 ?  76  ASP B OD1   1 
ATOM   6177  O  OD2   . ASP B 1 76  ? 153.485 162.895 166.827 1.00 58.03 -1 76  ASP B OD2   1 
ATOM   6178  N  N     . ILE B 1 77  ? 154.501 157.674 166.754 1.00 48.13 ?  77  ILE B N     1 
ATOM   6179  C  CA    . ILE B 1 77  ? 154.331 156.272 166.376 1.00 49.21 ?  77  ILE B CA    1 
ATOM   6180  C  C     . ILE B 1 77  ? 154.870 155.360 167.469 1.00 50.79 ?  77  ILE B C     1 
ATOM   6181  O  O     . ILE B 1 77  ? 154.280 154.316 167.780 1.00 54.21 ?  77  ILE B O     1 
ATOM   6182  C  CB    . ILE B 1 77  ? 155.010 156.000 165.023 1.00 49.26 ?  77  ILE B CB    1 
ATOM   6183  C  CG1   . ILE B 1 77  ? 154.386 156.869 163.932 1.00 49.08 ?  77  ILE B CG1   1 
ATOM   6184  C  CG2   . ILE B 1 77  ? 154.894 154.532 164.654 1.00 49.31 ?  77  ILE B CG2   1 
ATOM   6185  C  CD1   . ILE B 1 77  ? 155.196 156.919 162.662 1.00 50.74 ?  77  ILE B CD1   1 
ATOM   6186  N  N     . LYS B 1 78  ? 156.004 155.734 168.062 1.00 52.56 ?  78  LYS B N     1 
ATOM   6187  C  CA    . LYS B 1 78  ? 156.569 154.949 169.152 1.00 51.80 ?  78  LYS B CA    1 
ATOM   6188  C  C     . LYS B 1 78  ? 155.628 154.915 170.347 1.00 52.98 ?  78  LYS B C     1 
ATOM   6189  O  O     . LYS B 1 78  ? 155.459 153.869 170.980 1.00 56.49 ?  78  LYS B O     1 
ATOM   6190  C  CB    . LYS B 1 78  ? 157.932 155.514 169.551 1.00 55.18 ?  78  LYS B CB    1 
ATOM   6191  C  CG    . LYS B 1 78  ? 158.649 154.710 170.618 1.00 54.95 ?  78  LYS B CG    1 
ATOM   6192  C  CD    . LYS B 1 78  ? 160.077 154.403 170.203 1.00 55.76 ?  78  LYS B CD    1 
ATOM   6193  C  CE    . LYS B 1 78  ? 161.073 154.907 171.232 1.00 57.25 ?  78  LYS B CE    1 
ATOM   6194  N  NZ    . LYS B 1 78  ? 162.479 154.709 170.787 1.00 55.90 1  78  LYS B NZ    1 
ATOM   6195  N  N     . GLU B 1 79  ? 155.002 156.048 170.670 1.00 53.27 ?  79  GLU B N     1 
ATOM   6196  C  CA    . GLU B 1 79  ? 154.048 156.064 171.775 1.00 52.11 ?  79  GLU B CA    1 
ATOM   6197  C  C     . GLU B 1 79  ? 152.795 155.260 171.454 1.00 51.11 ?  79  GLU B C     1 
ATOM   6198  O  O     . GLU B 1 79  ? 152.218 154.633 172.348 1.00 52.30 ?  79  GLU B O     1 
ATOM   6199  C  CB    . GLU B 1 79  ? 153.682 157.504 172.140 1.00 52.64 ?  79  GLU B CB    1 
ATOM   6200  C  CG    . GLU B 1 79  ? 154.850 158.368 172.619 1.00 56.29 ?  79  GLU B CG    1 
ATOM   6201  C  CD    . GLU B 1 79  ? 155.897 157.607 173.427 1.00 58.47 ?  79  GLU B CD    1 
ATOM   6202  O  OE1   . GLU B 1 79  ? 157.102 157.871 173.225 1.00 56.16 ?  79  GLU B OE1   1 
ATOM   6203  O  OE2   . GLU B 1 79  ? 155.528 156.787 174.296 1.00 57.13 -1 79  GLU B OE2   1 
ATOM   6204  N  N     . VAL B 1 80  ? 152.362 155.258 170.192 1.00 48.64 ?  80  VAL B N     1 
ATOM   6205  C  CA    . VAL B 1 80  ? 151.225 154.430 169.799 1.00 45.07 ?  80  VAL B CA    1 
ATOM   6206  C  C     . VAL B 1 80  ? 151.556 152.950 169.972 1.00 48.97 ?  80  VAL B C     1 
ATOM   6207  O  O     . VAL B 1 80  ? 150.757 152.174 170.517 1.00 51.77 ?  80  VAL B O     1 
ATOM   6208  C  CB    . VAL B 1 80  ? 150.808 154.760 168.353 1.00 44.98 ?  80  VAL B CB    1 
ATOM   6209  C  CG1   . VAL B 1 80  ? 149.891 153.694 167.796 1.00 46.55 ?  80  VAL B CG1   1 
ATOM   6210  C  CG2   . VAL B 1 80  ? 150.132 156.120 168.300 1.00 45.90 ?  80  VAL B CG2   1 
ATOM   6211  N  N     . PHE B 1 81  ? 152.746 152.541 169.527 1.00 47.44 ?  81  PHE B N     1 
ATOM   6212  C  CA    . PHE B 1 81  ? 153.173 151.157 169.719 1.00 44.10 ?  81  PHE B CA    1 
ATOM   6213  C  C     . PHE B 1 81  ? 153.327 150.828 171.200 1.00 45.61 ?  81  PHE B C     1 
ATOM   6214  O  O     . PHE B 1 81  ? 153.039 149.704 171.626 1.00 51.04 ?  81  PHE B O     1 
ATOM   6215  C  CB    . PHE B 1 81  ? 154.479 150.902 168.970 1.00 43.36 ?  81  PHE B CB    1 
ATOM   6216  C  CG    . PHE B 1 81  ? 154.288 150.470 167.545 1.00 43.48 ?  81  PHE B CG    1 
ATOM   6217  C  CD1   . PHE B 1 81  ? 153.984 151.395 166.560 1.00 44.24 ?  81  PHE B CD1   1 
ATOM   6218  C  CD2   . PHE B 1 81  ? 154.414 149.140 167.189 1.00 43.71 ?  81  PHE B CD2   1 
ATOM   6219  C  CE1   . PHE B 1 81  ? 153.808 150.999 165.249 1.00 44.16 ?  81  PHE B CE1   1 
ATOM   6220  C  CE2   . PHE B 1 81  ? 154.238 148.738 165.880 1.00 45.21 ?  81  PHE B CE2   1 
ATOM   6221  C  CZ    . PHE B 1 81  ? 153.935 149.670 164.909 1.00 43.39 ?  81  PHE B CZ    1 
ATOM   6222  N  N     . LYS B 1 82  ? 153.784 151.795 171.996 1.00 47.11 ?  82  LYS B N     1 
ATOM   6223  C  CA    . LYS B 1 82  ? 153.850 151.611 173.443 1.00 51.39 ?  82  LYS B CA    1 
ATOM   6224  C  C     . LYS B 1 82  ? 152.466 151.352 174.018 1.00 51.71 ?  82  LYS B C     1 
ATOM   6225  O  O     . LYS B 1 82  ? 152.285 150.474 174.869 1.00 51.17 ?  82  LYS B O     1 
ATOM   6226  C  CB    . LYS B 1 82  ? 154.469 152.847 174.096 1.00 53.58 ?  82  LYS B CB    1 
ATOM   6227  C  CG    . LYS B 1 82  ? 155.794 152.617 174.795 1.00 53.04 ?  82  LYS B CG    1 
ATOM   6228  C  CD    . LYS B 1 82  ? 156.942 152.514 173.812 1.00 54.24 ?  82  LYS B CD    1 
ATOM   6229  C  CE    . LYS B 1 82  ? 158.273 152.649 174.532 1.00 55.14 ?  82  LYS B CE    1 
ATOM   6230  N  NZ    . LYS B 1 82  ? 159.305 151.722 174.000 1.00 56.03 1  82  LYS B NZ    1 
ATOM   6231  N  N     . THR B 1 83  ? 151.474 152.119 173.564 1.00 47.16 ?  83  THR B N     1 
ATOM   6232  C  CA    . THR B 1 83  ? 150.106 151.928 174.028 1.00 45.62 ?  83  THR B CA    1 
ATOM   6233  C  C     . THR B 1 83  ? 149.585 150.549 173.648 1.00 47.50 ?  83  THR B C     1 
ATOM   6234  O  O     . THR B 1 83  ? 148.884 149.903 174.436 1.00 51.83 ?  83  THR B O     1 
ATOM   6235  C  CB    . THR B 1 83  ? 149.202 153.020 173.460 1.00 45.08 ?  83  THR B CB    1 
ATOM   6236  O  OG1   . THR B 1 83  ? 149.777 154.304 173.732 1.00 51.98 ?  83  THR B OG1   1 
ATOM   6237  C  CG2   . THR B 1 83  ? 147.824 152.954 174.090 1.00 47.96 ?  83  THR B CG2   1 
ATOM   6238  N  N     . ALA B 1 84  ? 149.913 150.082 172.441 1.00 41.73 ?  84  ALA B N     1 
ATOM   6239  C  CA    . ALA B 1 84  ? 149.483 148.745 172.040 1.00 38.19 ?  84  ALA B CA    1 
ATOM   6240  C  C     . ALA B 1 84  ? 150.118 147.666 172.908 1.00 41.93 ?  84  ALA B C     1 
ATOM   6241  O  O     . ALA B 1 84  ? 149.441 146.718 173.320 1.00 50.02 ?  84  ALA B O     1 
ATOM   6242  C  CB    . ALA B 1 84  ? 149.811 148.506 170.570 1.00 41.37 ?  84  ALA B CB    1 
ATOM   6243  N  N     . TYR B 1 85  ? 151.415 147.790 173.195 1.00 48.73 ?  85  TYR B N     1 
ATOM   6244  C  CA    . TYR B 1 85  ? 152.102 146.785 173.995 1.00 44.08 ?  85  TYR B CA    1 
ATOM   6245  C  C     . TYR B 1 85  ? 151.912 146.986 175.491 1.00 45.71 ?  85  TYR B C     1 
ATOM   6246  O  O     . TYR B 1 85  ? 152.234 146.082 176.268 1.00 48.79 ?  85  TYR B O     1 
ATOM   6247  C  CB    . TYR B 1 85  ? 153.596 146.775 173.662 1.00 45.03 ?  85  TYR B CB    1 
ATOM   6248  C  CG    . TYR B 1 85  ? 153.927 146.107 172.347 1.00 45.73 ?  85  TYR B CG    1 
ATOM   6249  C  CD1   . TYR B 1 85  ? 153.907 146.821 171.158 1.00 45.47 ?  85  TYR B CD1   1 
ATOM   6250  C  CD2   . TYR B 1 85  ? 154.260 144.762 172.296 1.00 45.37 ?  85  TYR B CD2   1 
ATOM   6251  C  CE1   . TYR B 1 85  ? 154.209 146.216 169.957 1.00 45.26 ?  85  TYR B CE1   1 
ATOM   6252  C  CE2   . TYR B 1 85  ? 154.563 144.148 171.099 1.00 45.88 ?  85  TYR B CE2   1 
ATOM   6253  C  CZ    . TYR B 1 85  ? 154.536 144.879 169.933 1.00 47.44 ?  85  TYR B CZ    1 
ATOM   6254  O  OH    . TYR B 1 85  ? 154.837 144.271 168.740 1.00 49.52 ?  85  TYR B OH    1 
ATOM   6255  N  N     . ALA B 1 86  ? 151.400 148.144 175.915 1.00 48.77 ?  86  ALA B N     1 
ATOM   6256  C  CA    . ALA B 1 86  ? 151.148 148.363 177.334 1.00 49.11 ?  86  ALA B CA    1 
ATOM   6257  C  C     . ALA B 1 86  ? 150.028 147.480 177.864 1.00 51.18 ?  86  ALA B C     1 
ATOM   6258  O  O     . ALA B 1 86  ? 149.989 147.207 179.068 1.00 50.07 ?  86  ALA B O     1 
ATOM   6259  C  CB    . ALA B 1 86  ? 150.812 149.831 177.596 1.00 45.01 ?  86  ALA B CB    1 
ATOM   6260  N  N     . LYS B 1 87  ? 149.120 147.034 176.998 1.00 43.59 ?  87  LYS B N     1 
ATOM   6261  C  CA    . LYS B 1 87  ? 148.020 146.182 177.429 1.00 43.37 ?  87  LYS B CA    1 
ATOM   6262  C  C     . LYS B 1 87  ? 148.460 144.755 177.722 1.00 46.64 ?  87  LYS B C     1 
ATOM   6263  O  O     . LYS B 1 87  ? 147.762 144.049 178.457 1.00 46.53 ?  87  LYS B O     1 
ATOM   6264  C  CB    . LYS B 1 87  ? 146.918 146.168 176.369 1.00 46.41 ?  87  LYS B CB    1 
ATOM   6265  C  CG    . LYS B 1 87  ? 145.522 145.969 176.930 1.00 47.31 ?  87  LYS B CG    1 
ATOM   6266  C  CD    . LYS B 1 87  ? 144.825 144.792 176.270 1.00 43.91 ?  87  LYS B CD    1 
ATOM   6267  C  CE    . LYS B 1 87  ? 143.559 144.413 177.017 1.00 43.53 ?  87  LYS B CE    1 
ATOM   6268  N  NZ    . LYS B 1 87  ? 142.830 143.300 176.347 1.00 41.20 1  87  LYS B NZ    1 
ATOM   6269  N  N     . LYS B 1 88  ? 149.598 144.323 177.173 1.00 51.97 ?  88  LYS B N     1 
ATOM   6270  C  CA    . LYS B 1 88  ? 150.079 142.949 177.314 1.00 47.74 ?  88  LYS B CA    1 
ATOM   6271  C  C     . LYS B 1 88  ? 148.996 141.954 176.905 1.00 46.69 ?  88  LYS B C     1 
ATOM   6272  O  O     . LYS B 1 88  ? 148.672 141.013 177.631 1.00 49.88 ?  88  LYS B O     1 
ATOM   6273  C  CB    . LYS B 1 88  ? 150.568 142.678 178.738 1.00 48.98 ?  88  LYS B CB    1 
ATOM   6274  C  CG    . LYS B 1 88  ? 151.433 143.783 179.320 1.00 47.10 ?  88  LYS B CG    1 
ATOM   6275  C  CD    . LYS B 1 88  ? 152.755 143.240 179.831 1.00 50.61 ?  88  LYS B CD    1 
ATOM   6276  C  CE    . LYS B 1 88  ? 152.565 142.434 181.104 1.00 52.66 ?  88  LYS B CE    1 
ATOM   6277  N  NZ    . LYS B 1 88  ? 153.739 141.563 181.391 1.00 51.45 1  88  LYS B NZ    1 
ATOM   6278  N  N     . PHE B 1 89  ? 148.425 142.184 175.724 1.00 45.43 ?  89  PHE B N     1 
ATOM   6279  C  CA    . PHE B 1 89  ? 147.309 141.371 175.261 1.00 40.04 ?  89  PHE B CA    1 
ATOM   6280  C  C     . PHE B 1 89  ? 147.746 139.928 175.049 1.00 42.32 ?  89  PHE B C     1 
ATOM   6281  O  O     . PHE B 1 89  ? 148.791 139.661 174.451 1.00 43.62 ?  89  PHE B O     1 
ATOM   6282  C  CB    . PHE B 1 89  ? 146.738 141.940 173.962 1.00 39.99 ?  89  PHE B CB    1 
ATOM   6283  C  CG    . PHE B 1 89  ? 145.700 141.063 173.326 1.00 38.98 ?  89  PHE B CG    1 
ATOM   6284  C  CD1   . PHE B 1 89  ? 144.397 141.071 173.787 1.00 37.21 ?  89  PHE B CD1   1 
ATOM   6285  C  CD2   . PHE B 1 89  ? 146.029 140.224 172.277 1.00 39.03 ?  89  PHE B CD2   1 
ATOM   6286  C  CE1   . PHE B 1 89  ? 143.441 140.264 173.211 1.00 39.04 ?  89  PHE B CE1   1 
ATOM   6287  C  CE2   . PHE B 1 89  ? 145.076 139.414 171.697 1.00 35.00 ?  89  PHE B CE2   1 
ATOM   6288  C  CZ    . PHE B 1 89  ? 143.781 139.434 172.164 1.00 38.35 ?  89  PHE B CZ    1 
ATOM   6289  N  N     . ARG B 1 90  ? 146.932 138.998 175.535 1.00 43.49 ?  90  ARG B N     1 
ATOM   6290  C  CA    . ARG B 1 90  ? 147.175 137.573 175.375 1.00 43.41 ?  90  ARG B CA    1 
ATOM   6291  C  C     . ARG B 1 90  ? 145.986 136.945 174.665 1.00 43.90 ?  90  ARG B C     1 
ATOM   6292  O  O     . ARG B 1 90  ? 144.836 137.179 175.050 1.00 47.64 ?  90  ARG B O     1 
ATOM   6293  C  CB    . ARG B 1 90  ? 147.403 136.893 176.727 1.00 46.45 ?  90  ARG B CB    1 
ATOM   6294  C  CG    . ARG B 1 90  ? 148.584 137.441 177.502 1.00 46.45 ?  90  ARG B CG    1 
ATOM   6295  C  CD    . ARG B 1 90  ? 149.868 136.734 177.113 1.00 48.43 ?  90  ARG B CD    1 
ATOM   6296  N  NE    . ARG B 1 90  ? 150.689 137.551 176.229 1.00 51.01 ?  90  ARG B NE    1 
ATOM   6297  C  CZ    . ARG B 1 90  ? 151.450 138.560 176.631 1.00 49.77 ?  90  ARG B CZ    1 
ATOM   6298  N  NH1   . ARG B 1 90  ? 151.538 138.894 177.908 1.00 47.15 1  90  ARG B NH1   1 
ATOM   6299  N  NH2   . ARG B 1 90  ? 152.143 139.249 175.729 1.00 51.52 ?  90  ARG B NH2   1 
ATOM   6300  N  N     . PHE B 1 91  ? 146.264 136.163 173.634 1.00 36.62 ?  91  PHE B N     1 
ATOM   6301  C  CA    . PHE B 1 91  ? 145.211 135.405 172.979 1.00 39.12 ?  91  PHE B CA    1 
ATOM   6302  C  C     . PHE B 1 91  ? 144.707 134.327 173.932 1.00 44.74 ?  91  PHE B C     1 
ATOM   6303  O  O     . PHE B 1 91  ? 145.504 133.527 174.431 1.00 45.97 ?  91  PHE B O     1 
ATOM   6304  C  CB    . PHE B 1 91  ? 145.726 134.777 171.689 1.00 39.16 ?  91  PHE B CB    1 
ATOM   6305  C  CG    . PHE B 1 91  ? 145.875 135.752 170.556 1.00 40.47 ?  91  PHE B CG    1 
ATOM   6306  C  CD1   . PHE B 1 91  ? 144.763 136.230 169.884 1.00 43.58 ?  91  PHE B CD1   1 
ATOM   6307  C  CD2   . PHE B 1 91  ? 147.126 136.190 170.163 1.00 42.01 ?  91  PHE B CD2   1 
ATOM   6308  C  CE1   . PHE B 1 91  ? 144.898 137.122 168.841 1.00 40.28 ?  91  PHE B CE1   1 
ATOM   6309  C  CE2   . PHE B 1 91  ? 147.266 137.083 169.122 1.00 40.89 ?  91  PHE B CE2   1 
ATOM   6310  C  CZ    . PHE B 1 91  ? 146.150 137.549 168.459 1.00 36.90 ?  91  PHE B CZ    1 
ATOM   6311  N  N     . PRO B 1 92  ? 143.403 134.275 174.215 1.00 44.11 ?  92  PRO B N     1 
ATOM   6312  C  CA    . PRO B 1 92  ? 142.918 133.298 175.201 1.00 40.42 ?  92  PRO B CA    1 
ATOM   6313  C  C     . PRO B 1 92  ? 142.933 131.871 174.690 1.00 39.94 ?  92  PRO B C     1 
ATOM   6314  O  O     . PRO B 1 92  ? 143.088 130.940 175.490 1.00 43.37 ?  92  PRO B O     1 
ATOM   6315  C  CB    . PRO B 1 92  ? 141.493 133.781 175.491 1.00 40.58 ?  92  PRO B CB    1 
ATOM   6316  C  CG    . PRO B 1 92  ? 141.073 134.442 174.228 1.00 40.82 ?  92  PRO B CG    1 
ATOM   6317  C  CD    . PRO B 1 92  ? 142.308 135.075 173.642 1.00 42.53 ?  92  PRO B CD    1 
ATOM   6318  N  N     . SER B 1 93  ? 142.784 131.669 173.386 1.00 38.53 ?  93  SER B N     1 
ATOM   6319  C  CA    . SER B 1 93  ? 142.691 130.342 172.804 1.00 40.38 ?  93  SER B CA    1 
ATOM   6320  C  C     . SER B 1 93  ? 143.718 130.206 171.691 1.00 42.60 ?  93  SER B C     1 
ATOM   6321  O  O     . SER B 1 93  ? 144.203 131.197 171.141 1.00 47.55 ?  93  SER B O     1 
ATOM   6322  C  CB    . SER B 1 93  ? 141.283 130.071 172.262 1.00 44.04 ?  93  SER B CB    1 
ATOM   6323  O  OG    . SER B 1 93  ? 141.225 130.290 170.864 1.00 50.00 ?  93  SER B OG    1 
ATOM   6324  N  N     . PHE B 1 94  ? 144.058 128.956 171.373 1.00 41.90 ?  94  PHE B N     1 
ATOM   6325  C  CA    . PHE B 1 94  ? 145.004 128.712 170.291 1.00 40.14 ?  94  PHE B CA    1 
ATOM   6326  C  C     . PHE B 1 94  ? 144.441 129.156 168.948 1.00 42.76 ?  94  PHE B C     1 
ATOM   6327  O  O     . PHE B 1 94  ? 145.181 129.656 168.095 1.00 47.43 ?  94  PHE B O     1 
ATOM   6328  C  CB    . PHE B 1 94  ? 145.391 127.235 170.239 1.00 40.16 ?  94  PHE B CB    1 
ATOM   6329  C  CG    . PHE B 1 94  ? 145.978 126.819 168.924 1.00 41.76 ?  94  PHE B CG    1 
ATOM   6330  C  CD1   . PHE B 1 94  ? 147.234 127.256 168.546 1.00 42.32 ?  94  PHE B CD1   1 
ATOM   6331  C  CD2   . PHE B 1 94  ? 145.269 126.009 168.056 1.00 43.73 ?  94  PHE B CD2   1 
ATOM   6332  C  CE1   . PHE B 1 94  ? 147.772 126.888 167.333 1.00 42.88 ?  94  PHE B CE1   1 
ATOM   6333  C  CE2   . PHE B 1 94  ? 145.808 125.638 166.842 1.00 41.04 ?  94  PHE B CE2   1 
ATOM   6334  C  CZ    . PHE B 1 94  ? 147.059 126.078 166.481 1.00 40.39 ?  94  PHE B CZ    1 
ATOM   6335  N  N     . MET B 1 95  ? 143.136 128.973 168.739 1.00 38.81 ?  95  MET B N     1 
ATOM   6336  C  CA    . MET B 1 95  ? 142.548 129.293 167.443 1.00 34.84 ?  95  MET B CA    1 
ATOM   6337  C  C     . MET B 1 95  ? 142.576 130.788 167.155 1.00 41.06 ?  95  MET B C     1 
ATOM   6338  O  O     . MET B 1 95  ? 142.731 131.181 165.997 1.00 43.38 ?  95  MET B O     1 
ATOM   6339  C  CB    . MET B 1 95  ? 141.118 128.760 167.363 1.00 41.10 ?  95  MET B CB    1 
ATOM   6340  C  CG    . MET B 1 95  ? 140.431 128.928 166.002 1.00 45.93 ?  95  MET B CG    1 
ATOM   6341  S  SD    . MET B 1 95  ? 141.163 128.218 164.501 1.00 55.90 ?  95  MET B SD    1 
ATOM   6342  C  CE    . MET B 1 95  ? 142.183 126.878 165.110 1.00 43.07 ?  95  MET B CE    1 
ATOM   6343  N  N     . SER B 1 96  ? 142.443 131.631 168.179 1.00 36.73 ?  96  SER B N     1 
ATOM   6344  C  CA    . SER B 1 96  ? 142.532 133.073 167.962 1.00 33.30 ?  96  SER B CA    1 
ATOM   6345  C  C     . SER B 1 96  ? 143.888 133.458 167.383 1.00 36.80 ?  96  SER B C     1 
ATOM   6346  O  O     . SER B 1 96  ? 143.973 134.114 166.334 1.00 32.79 ?  96  SER B O     1 
ATOM   6347  C  CB    . SER B 1 96  ? 142.286 133.809 169.278 1.00 36.01 ?  96  SER B CB    1 
ATOM   6348  O  OG    . SER B 1 96  ? 141.273 133.174 170.034 1.00 42.95 ?  96  SER B OG    1 
ATOM   6349  N  N     . ALA B 1 97  ? 144.963 133.040 168.053 1.00 36.06 ?  97  ALA B N     1 
ATOM   6350  C  CA    . ALA B 1 97  ? 146.309 133.354 167.591 1.00 32.56 ?  97  ALA B CA    1 
ATOM   6351  C  C     . ALA B 1 97  ? 146.599 132.703 166.247 1.00 34.38 ?  97  ALA B C     1 
ATOM   6352  O  O     . ALA B 1 97  ? 147.228 133.316 165.380 1.00 40.22 ?  97  ALA B O     1 
ATOM   6353  C  CB    . ALA B 1 97  ? 147.334 132.911 168.631 1.00 38.51 ?  97  ALA B CB    1 
ATOM   6354  N  N     . PHE B 1 98  ? 146.161 131.457 166.064 1.00 37.04 ?  98  PHE B N     1 
ATOM   6355  C  CA    . PHE B 1 98  ? 146.389 130.769 164.800 1.00 34.05 ?  98  PHE B CA    1 
ATOM   6356  C  C     . PHE B 1 98  ? 145.710 131.501 163.651 1.00 36.17 ?  98  PHE B C     1 
ATOM   6357  O  O     . PHE B 1 98  ? 146.320 131.730 162.601 1.00 48.45 ?  98  PHE B O     1 
ATOM   6358  C  CB    . PHE B 1 98  ? 145.891 129.327 164.890 1.00 39.75 ?  98  PHE B CB    1 
ATOM   6359  C  CG    . PHE B 1 98  ? 145.986 128.573 163.595 1.00 39.93 ?  98  PHE B CG    1 
ATOM   6360  C  CD1   . PHE B 1 98  ? 147.182 128.003 163.197 1.00 39.71 ?  98  PHE B CD1   1 
ATOM   6361  C  CD2   . PHE B 1 98  ? 144.878 128.433 162.776 1.00 41.60 ?  98  PHE B CD2   1 
ATOM   6362  C  CE1   . PHE B 1 98  ? 147.272 127.311 162.008 1.00 39.50 ?  98  PHE B CE1   1 
ATOM   6363  C  CE2   . PHE B 1 98  ? 144.965 127.744 161.585 1.00 44.69 ?  98  PHE B CE2   1 
ATOM   6364  C  CZ    . PHE B 1 98  ? 146.162 127.182 161.201 1.00 43.40 ?  98  PHE B CZ    1 
ATOM   6365  N  N     . LYS B 1 99  ? 144.448 131.889 163.838 1.00 41.42 ?  99  LYS B N     1 
ATOM   6366  C  CA    . LYS B 1 99  ? 143.726 132.594 162.789 1.00 39.05 ?  99  LYS B CA    1 
ATOM   6367  C  C     . LYS B 1 99  ? 144.367 133.938 162.489 1.00 37.72 ?  99  LYS B C     1 
ATOM   6368  O  O     . LYS B 1 99  ? 144.521 134.309 161.321 1.00 42.56 ?  99  LYS B O     1 
ATOM   6369  C  CB    . LYS B 1 99  ? 142.261 132.770 163.187 1.00 37.97 ?  99  LYS B CB    1 
ATOM   6370  C  CG    . LYS B 1 99  ? 141.408 131.536 162.962 1.00 42.93 ?  99  LYS B CG    1 
ATOM   6371  C  CD    . LYS B 1 99  ? 141.516 131.038 161.534 1.00 42.94 ?  99  LYS B CD    1 
ATOM   6372  C  CE    . LYS B 1 99  ? 140.262 130.294 161.115 1.00 42.46 ?  99  LYS B CE    1 
ATOM   6373  N  NZ    . LYS B 1 99  ? 139.806 130.703 159.761 1.00 47.99 1  99  LYS B NZ    1 
ATOM   6374  N  N     . PHE B 1 100 ? 144.772 134.678 163.526 1.00 36.96 ?  100 PHE B N     1 
ATOM   6375  C  CA    . PHE B 1 100 ? 145.406 135.967 163.269 1.00 34.43 ?  100 PHE B CA    1 
ATOM   6376  C  C     . PHE B 1 100 ? 146.717 135.795 162.513 1.00 37.14 ?  100 PHE B C     1 
ATOM   6377  O  O     . PHE B 1 100 ? 146.937 136.432 161.479 1.00 41.84 ?  100 PHE B O     1 
ATOM   6378  C  CB    . PHE B 1 100 ? 145.652 136.735 164.564 1.00 34.19 ?  100 PHE B CB    1 
ATOM   6379  C  CG    . PHE B 1 100 ? 146.399 138.016 164.345 1.00 37.70 ?  100 PHE B CG    1 
ATOM   6380  C  CD1   . PHE B 1 100 ? 145.775 139.099 163.748 1.00 37.53 ?  100 PHE B CD1   1 
ATOM   6381  C  CD2   . PHE B 1 100 ? 147.733 138.123 164.684 1.00 34.09 ?  100 PHE B CD2   1 
ATOM   6382  C  CE1   . PHE B 1 100 ? 146.463 140.272 163.522 1.00 37.84 ?  100 PHE B CE1   1 
ATOM   6383  C  CE2   . PHE B 1 100 ? 148.425 139.292 164.458 1.00 35.09 ?  100 PHE B CE2   1 
ATOM   6384  C  CZ    . PHE B 1 100 ? 147.789 140.369 163.879 1.00 37.50 ?  100 PHE B CZ    1 
ATOM   6385  N  N     . TYR B 1 101 ? 147.595 134.925 163.003 1.00 40.14 ?  101 TYR B N     1 
ATOM   6386  C  CA    . TYR B 1 101 ? 148.913 134.777 162.404 1.00 36.34 ?  101 TYR B CA    1 
ATOM   6387  C  C     . TYR B 1 101 ? 148.893 133.967 161.116 1.00 35.53 ?  101 TYR B C     1 
ATOM   6388  O  O     . TYR B 1 101 ? 149.938 133.843 160.471 1.00 44.77 ?  101 TYR B O     1 
ATOM   6389  C  CB    . TYR B 1 101 ? 149.876 134.152 163.416 1.00 35.64 ?  101 TYR B CB    1 
ATOM   6390  C  CG    . TYR B 1 101 ? 150.300 135.131 164.484 1.00 33.35 ?  101 TYR B CG    1 
ATOM   6391  C  CD1   . TYR B 1 101 ? 151.175 136.168 164.194 1.00 34.17 ?  101 TYR B CD1   1 
ATOM   6392  C  CD2   . TYR B 1 101 ? 149.804 135.036 165.774 1.00 37.40 ?  101 TYR B CD2   1 
ATOM   6393  C  CE1   . TYR B 1 101 ? 151.555 137.072 165.163 1.00 36.52 ?  101 TYR B CE1   1 
ATOM   6394  C  CE2   . TYR B 1 101 ? 150.177 135.935 166.748 1.00 39.90 ?  101 TYR B CE2   1 
ATOM   6395  C  CZ    . TYR B 1 101 ? 151.053 136.951 166.438 1.00 40.02 ?  101 TYR B CZ    1 
ATOM   6396  O  OH    . TYR B 1 101 ? 151.425 137.846 167.411 1.00 39.82 ?  101 TYR B OH    1 
ATOM   6397  N  N     . ASN B 1 102 ? 147.745 133.413 160.729 1.00 38.82 ?  102 ASN B N     1 
ATOM   6398  C  CA    . ASN B 1 102 ? 147.624 132.761 159.435 1.00 41.96 ?  102 ASN B CA    1 
ATOM   6399  C  C     . ASN B 1 102 ? 146.840 133.574 158.415 1.00 43.72 ?  102 ASN B C     1 
ATOM   6400  O  O     . ASN B 1 102 ? 146.971 133.313 157.214 1.00 48.13 ?  102 ASN B O     1 
ATOM   6401  C  CB    . ASN B 1 102 ? 146.958 131.389 159.594 1.00 40.56 ?  102 ASN B CB    1 
ATOM   6402  C  CG    . ASN B 1 102 ? 147.958 130.284 159.871 1.00 44.81 ?  102 ASN B CG    1 
ATOM   6403  O  OD1   . ASN B 1 102 ? 148.818 130.412 160.744 1.00 48.40 ?  102 ASN B OD1   1 
ATOM   6404  N  ND2   . ASN B 1 102 ? 147.852 129.191 159.126 1.00 43.12 ?  102 ASN B ND2   1 
ATOM   6405  N  N     . ASP B 1 103 ? 146.034 134.544 158.847 1.00 42.99 ?  103 ASP B N     1 
ATOM   6406  C  CA    . ASP B 1 103 ? 145.206 135.299 157.915 1.00 42.91 ?  103 ASP B CA    1 
ATOM   6407  C  C     . ASP B 1 103 ? 145.531 136.783 157.860 1.00 42.58 ?  103 ASP B C     1 
ATOM   6408  O  O     . ASP B 1 103 ? 145.456 137.379 156.783 1.00 46.97 ?  103 ASP B O     1 
ATOM   6409  C  CB    . ASP B 1 103 ? 143.722 135.127 158.276 1.00 45.28 ?  103 ASP B CB    1 
ATOM   6410  C  CG    . ASP B 1 103 ? 143.240 133.699 158.111 1.00 50.09 ?  103 ASP B CG    1 
ATOM   6411  O  OD1   . ASP B 1 103 ? 144.026 132.851 157.641 1.00 50.18 ?  103 ASP B OD1   1 
ATOM   6412  O  OD2   . ASP B 1 103 ? 142.073 133.423 158.457 1.00 53.52 -1 103 ASP B OD2   1 
ATOM   6413  N  N     . TYR B 1 104 ? 145.889 137.400 158.983 1.00 36.66 ?  104 TYR B N     1 
ATOM   6414  C  CA    . TYR B 1 104 ? 146.008 138.849 159.063 1.00 41.43 ?  104 TYR B CA    1 
ATOM   6415  C  C     . TYR B 1 104 ? 147.409 139.346 159.380 1.00 39.97 ?  104 TYR B C     1 
ATOM   6416  O  O     . TYR B 1 104 ? 147.730 140.483 159.031 1.00 45.56 ?  104 TYR B O     1 
ATOM   6417  C  CB    . TYR B 1 104 ? 145.042 139.402 160.122 1.00 37.76 ?  104 TYR B CB    1 
ATOM   6418  C  CG    . TYR B 1 104 ? 143.609 138.982 159.901 1.00 41.00 ?  104 TYR B CG    1 
ATOM   6419  C  CD1   . TYR B 1 104 ? 142.782 139.700 159.051 1.00 40.31 ?  104 TYR B CD1   1 
ATOM   6420  C  CD2   . TYR B 1 104 ? 143.088 137.862 160.533 1.00 35.66 ?  104 TYR B CD2   1 
ATOM   6421  C  CE1   . TYR B 1 104 ? 141.475 139.318 158.841 1.00 39.93 ?  104 TYR B CE1   1 
ATOM   6422  C  CE2   . TYR B 1 104 ? 141.782 137.472 160.329 1.00 36.77 ?  104 TYR B CE2   1 
ATOM   6423  C  CZ    . TYR B 1 104 ? 140.980 138.205 159.481 1.00 41.95 ?  104 TYR B CZ    1 
ATOM   6424  O  OH    . TYR B 1 104 ? 139.677 137.823 159.272 1.00 41.50 ?  104 TYR B OH    1 
ATOM   6425  N  N     . ALA B 1 105 ? 148.242 138.542 160.034 1.00 42.71 ?  105 ALA B N     1 
ATOM   6426  C  CA    . ALA B 1 105 ? 149.589 138.985 160.366 1.00 42.57 ?  105 ALA B CA    1 
ATOM   6427  C  C     . ALA B 1 105 ? 150.423 139.155 159.104 1.00 45.88 ?  105 ALA B C     1 
ATOM   6428  O  O     . ALA B 1 105 ? 150.370 138.329 158.188 1.00 44.64 ?  105 ALA B O     1 
ATOM   6429  C  CB    . ALA B 1 105 ? 150.262 137.989 161.306 1.00 38.01 ?  105 ALA B CB    1 
ATOM   6430  N  N     . LEU B 1 106 ? 151.192 140.238 159.058 1.00 47.08 ?  106 LEU B N     1 
ATOM   6431  C  CA    . LEU B 1 106 ? 152.037 140.505 157.903 1.00 44.38 ?  106 LEU B CA    1 
ATOM   6432  C  C     . LEU B 1 106 ? 153.201 139.523 157.868 1.00 47.36 ?  106 LEU B C     1 
ATOM   6433  O  O     . LEU B 1 106 ? 153.907 139.343 158.863 1.00 47.74 ?  106 LEU B O     1 
ATOM   6434  C  CB    . LEU B 1 106 ? 152.554 141.941 157.941 1.00 48.24 ?  106 LEU B CB    1 
ATOM   6435  C  CG    . LEU B 1 106 ? 153.344 142.420 156.722 1.00 44.94 ?  106 LEU B CG    1 
ATOM   6436  C  CD1   . LEU B 1 106 ? 152.447 142.503 155.500 1.00 44.16 ?  106 LEU B CD1   1 
ATOM   6437  C  CD2   . LEU B 1 106 ? 153.996 143.762 157.001 1.00 44.60 ?  106 LEU B CD2   1 
ATOM   6438  N  N     . LYS B 1 107 ? 153.399 138.895 156.715 1.00 55.35 ?  107 LYS B N     1 
ATOM   6439  C  CA    . LYS B 1 107 ? 154.468 137.934 156.511 1.00 55.18 ?  107 LYS B CA    1 
ATOM   6440  C  C     . LYS B 1 107 ? 155.419 138.444 155.440 1.00 56.71 ?  107 LYS B C     1 
ATOM   6441  O  O     . LYS B 1 107 ? 155.107 139.375 154.691 1.00 55.21 ?  107 LYS B O     1 
ATOM   6442  C  CB    . LYS B 1 107 ? 153.917 136.562 156.109 1.00 54.68 ?  107 LYS B CB    1 
ATOM   6443  C  CG    . LYS B 1 107 ? 153.453 135.713 157.274 1.00 52.82 ?  107 LYS B CG    1 
ATOM   6444  C  CD    . LYS B 1 107 ? 152.607 134.549 156.799 1.00 55.63 ?  107 LYS B CD    1 
ATOM   6445  C  CE    . LYS B 1 107 ? 151.824 133.944 157.946 1.00 57.28 ?  107 LYS B CE    1 
ATOM   6446  N  NZ    . LYS B 1 107 ? 151.429 134.974 158.946 1.00 56.18 1  107 LYS B NZ    1 
ATOM   6447  N  N     . THR B 1 108 ? 156.595 137.824 155.379 1.00 60.92 ?  108 THR B N     1 
ATOM   6448  C  CA    . THR B 1 108 ? 157.570 138.166 154.359 1.00 60.71 ?  108 THR B CA    1 
ATOM   6449  C  C     . THR B 1 108 ? 157.016 137.843 152.971 1.00 62.10 ?  108 THR B C     1 
ATOM   6450  O  O     . THR B 1 108 ? 156.013 137.143 152.818 1.00 62.89 ?  108 THR B O     1 
ATOM   6451  C  CB    . THR B 1 108 ? 158.880 137.415 154.594 1.00 59.88 ?  108 THR B CB    1 
ATOM   6452  O  OG1   . THR B 1 108 ? 158.602 136.024 154.795 1.00 62.05 ?  108 THR B OG1   1 
ATOM   6453  C  CG2   . THR B 1 108 ? 159.599 137.958 155.815 1.00 57.02 ?  108 THR B CG2   1 
ATOM   6454  N  N     . ASN B 1 109 ? 157.691 138.372 151.946 1.00 63.27 ?  109 ASN B N     1 
ATOM   6455  C  CA    . ASN B 1 109 ? 157.232 138.162 150.576 1.00 63.09 ?  109 ASN B CA    1 
ATOM   6456  C  C     . ASN B 1 109 ? 157.220 136.686 150.199 1.00 66.07 ?  109 ASN B C     1 
ATOM   6457  O  O     . ASN B 1 109 ? 156.440 136.276 149.332 1.00 65.99 ?  109 ASN B O     1 
ATOM   6458  C  CB    . ASN B 1 109 ? 158.104 138.952 149.601 1.00 61.80 ?  109 ASN B CB    1 
ATOM   6459  C  CG    . ASN B 1 109 ? 158.135 140.433 149.918 1.00 64.04 ?  109 ASN B CG    1 
ATOM   6460  O  OD1   . ASN B 1 109 ? 157.118 141.120 149.824 1.00 66.19 ?  109 ASN B OD1   1 
ATOM   6461  N  ND2   . ASN B 1 109 ? 159.305 140.933 150.297 1.00 63.88 ?  109 ASN B ND2   1 
ATOM   6462  N  N     . ASP B 1 110 ? 158.068 135.877 150.829 1.00 66.04 ?  110 ASP B N     1 
ATOM   6463  C  CA    . ASP B 1 110 ? 158.053 134.435 150.630 1.00 67.63 ?  110 ASP B CA    1 
ATOM   6464  C  C     . ASP B 1 110 ? 157.167 133.714 151.639 1.00 66.77 ?  110 ASP B C     1 
ATOM   6465  O  O     . ASP B 1 110 ? 157.136 132.479 151.645 1.00 67.18 ?  110 ASP B O     1 
ATOM   6466  C  CB    . ASP B 1 110 ? 159.478 133.873 150.683 1.00 68.15 ?  110 ASP B CB    1 
ATOM   6467  C  CG    . ASP B 1 110 ? 160.138 134.076 152.030 1.00 69.90 ?  110 ASP B CG    1 
ATOM   6468  O  OD1   . ASP B 1 110 ? 159.758 135.024 152.742 1.00 69.54 ?  110 ASP B OD1   1 
ATOM   6469  O  OD2   . ASP B 1 110 ? 161.041 133.286 152.376 1.00 69.81 -1 110 ASP B OD2   1 
ATOM   6470  N  N     . LYS B 1 111 ? 156.450 134.461 152.483 1.00 64.62 ?  111 LYS B N     1 
ATOM   6471  C  CA    . LYS B 1 111 ? 155.525 133.896 153.470 1.00 64.06 ?  111 LYS B CA    1 
ATOM   6472  C  C     . LYS B 1 111 ? 156.226 132.895 154.385 1.00 66.24 ?  111 LYS B C     1 
ATOM   6473  O  O     . LYS B 1 111 ? 155.686 131.835 154.707 1.00 67.00 ?  111 LYS B O     1 
ATOM   6474  C  CB    . LYS B 1 111 ? 154.313 133.254 152.791 1.00 64.89 ?  111 LYS B CB    1 
ATOM   6475  C  CG    . LYS B 1 111 ? 153.690 134.093 151.685 1.00 64.51 ?  111 LYS B CG    1 
ATOM   6476  C  CD    . LYS B 1 111 ? 153.338 135.494 152.166 1.00 66.11 ?  111 LYS B CD    1 
ATOM   6477  C  CE    . LYS B 1 111 ? 152.135 135.478 153.095 1.00 67.79 ?  111 LYS B CE    1 
ATOM   6478  N  NZ    . LYS B 1 111 ? 150.918 134.943 152.425 1.00 68.04 1  111 LYS B NZ    1 
ATOM   6479  N  N     . LYS B 1 112 ? 157.440 133.237 154.810 1.00 65.24 ?  112 LYS B N     1 
ATOM   6480  C  CA    . LYS B 1 112 ? 158.245 132.378 155.671 1.00 64.41 ?  112 LYS B CA    1 
ATOM   6481  C  C     . LYS B 1 112 ? 158.321 132.866 157.108 1.00 64.17 ?  112 LYS B C     1 
ATOM   6482  O  O     . LYS B 1 112 ? 158.200 132.060 158.033 1.00 65.83 ?  112 LYS B O     1 
ATOM   6483  C  CB    . LYS B 1 112 ? 159.664 132.250 155.100 1.00 63.97 ?  112 LYS B CB    1 
ATOM   6484  C  CG    . LYS B 1 112 ? 160.739 131.910 156.122 1.00 67.04 ?  112 LYS B CG    1 
ATOM   6485  C  CD    . LYS B 1 112 ? 160.702 130.437 156.503 1.00 65.11 ?  112 LYS B CD    1 
ATOM   6486  C  CE    . LYS B 1 112 ? 161.259 130.215 157.899 1.00 65.22 ?  112 LYS B CE    1 
ATOM   6487  N  NZ    . LYS B 1 112 ? 160.400 130.838 158.945 1.00 64.88 1  112 LYS B NZ    1 
ATOM   6488  N  N     . LYS B 1 113 ? 158.505 134.161 157.320 1.00 60.20 ?  113 LYS B N     1 
ATOM   6489  C  CA    . LYS B 1 113 ? 158.633 134.745 158.647 1.00 59.08 ?  113 LYS B CA    1 
ATOM   6490  C  C     . LYS B 1 113 ? 157.459 135.684 158.913 1.00 59.43 ?  113 LYS B C     1 
ATOM   6491  O  O     . LYS B 1 113 ? 156.622 135.933 158.043 1.00 57.53 ?  113 LYS B O     1 
ATOM   6492  C  CB    . LYS B 1 113 ? 159.971 135.476 158.785 1.00 57.33 ?  113 LYS B CB    1 
ATOM   6493  C  CG    . LYS B 1 113 ? 161.161 134.561 159.016 1.00 57.95 ?  113 LYS B CG    1 
ATOM   6494  C  CD    . LYS B 1 113 ? 161.184 134.031 160.437 1.00 59.48 ?  113 LYS B CD    1 
ATOM   6495  C  CE    . LYS B 1 113 ? 162.578 133.584 160.839 1.00 57.00 ?  113 LYS B CE    1 
ATOM   6496  N  NZ    . LYS B 1 113 ? 162.655 132.107 161.008 1.00 58.77 1  113 LYS B NZ    1 
ATOM   6497  N  N     . ILE B 1 114 ? 157.408 136.210 160.134 1.00 52.83 ?  114 ILE B N     1 
ATOM   6498  C  CA    . ILE B 1 114 ? 156.315 137.064 160.590 1.00 49.84 ?  114 ILE B CA    1 
ATOM   6499  C  C     . ILE B 1 114 ? 156.884 138.436 160.921 1.00 51.40 ?  114 ILE B C     1 
ATOM   6500  O  O     . ILE B 1 114 ? 157.795 138.553 161.749 1.00 54.24 ?  114 ILE B O     1 
ATOM   6501  C  CB    . ILE B 1 114 ? 155.597 136.462 161.809 1.00 51.19 ?  114 ILE B CB    1 
ATOM   6502  C  CG1   . ILE B 1 114 ? 154.740 135.265 161.392 1.00 49.80 ?  114 ILE B CG1   1 
ATOM   6503  C  CG2   . ILE B 1 114 ? 154.745 137.508 162.502 1.00 51.04 ?  114 ILE B CG2   1 
ATOM   6504  C  CD1   . ILE B 1 114 ? 154.309 134.398 162.551 1.00 46.81 ?  114 ILE B CD1   1 
ATOM   6505  N  N     . LEU B 1 115 ? 156.347 139.473 160.277 1.00 48.43 ?  115 LEU B N     1 
ATOM   6506  C  CA    . LEU B 1 115 ? 156.757 140.842 160.570 1.00 47.70 ?  115 LEU B CA    1 
ATOM   6507  C  C     . LEU B 1 115 ? 155.889 141.495 161.636 1.00 50.04 ?  115 LEU B C     1 
ATOM   6508  O  O     . LEU B 1 115 ? 156.395 142.269 162.456 1.00 51.35 ?  115 LEU B O     1 
ATOM   6509  C  CB    . LEU B 1 115 ? 156.718 141.701 159.303 1.00 49.26 ?  115 LEU B CB    1 
ATOM   6510  C  CG    . LEU B 1 115 ? 157.823 141.552 158.258 1.00 47.40 ?  115 LEU B CG    1 
ATOM   6511  C  CD1   . LEU B 1 115 ? 159.182 141.377 158.917 1.00 49.77 ?  115 LEU B CD1   1 
ATOM   6512  C  CD2   . LEU B 1 115 ? 157.518 140.408 157.321 1.00 48.91 ?  115 LEU B CD2   1 
ATOM   6513  N  N     . GLU B 1 116 ? 154.593 141.203 161.643 1.00 46.96 ?  116 GLU B N     1 
ATOM   6514  C  CA    . GLU B 1 116 ? 153.631 141.904 162.481 1.00 46.21 ?  116 GLU B CA    1 
ATOM   6515  C  C     . GLU B 1 116 ? 153.103 140.986 163.572 1.00 44.69 ?  116 GLU B C     1 
ATOM   6516  O  O     . GLU B 1 116 ? 152.655 139.870 163.290 1.00 49.18 ?  116 GLU B O     1 
ATOM   6517  C  CB    . GLU B 1 116 ? 152.463 142.431 161.646 1.00 43.45 ?  116 GLU B CB    1 
ATOM   6518  C  CG    . GLU B 1 116 ? 152.572 143.893 161.274 1.00 44.40 ?  116 GLU B CG    1 
ATOM   6519  C  CD    . GLU B 1 116 ? 151.428 144.351 160.395 1.00 47.71 ?  116 GLU B CD    1 
ATOM   6520  O  OE1   . GLU B 1 116 ? 150.607 143.498 159.997 1.00 49.39 ?  116 GLU B OE1   1 
ATOM   6521  O  OE2   . GLU B 1 116 ? 151.347 145.561 160.103 1.00 50.22 -1 116 GLU B OE2   1 
ATOM   6522  N  N     . ARG B 1 117 ? 153.151 141.463 164.810 1.00 39.36 ?  117 ARG B N     1 
ATOM   6523  C  CA    . ARG B 1 117 ? 152.407 140.849 165.893 1.00 41.72 ?  117 ARG B CA    1 
ATOM   6524  C  C     . ARG B 1 117 ? 150.993 141.425 165.902 1.00 41.09 ?  117 ARG B C     1 
ATOM   6525  O  O     . ARG B 1 117 ? 150.627 142.247 165.059 1.00 39.45 ?  117 ARG B O     1 
ATOM   6526  C  CB    . ARG B 1 117 ? 153.111 141.079 167.229 1.00 42.00 ?  117 ARG B CB    1 
ATOM   6527  C  CG    . ARG B 1 117 ? 154.507 140.491 167.308 1.00 40.80 ?  117 ARG B CG    1 
ATOM   6528  C  CD    . ARG B 1 117 ? 154.518 139.023 166.909 1.00 46.77 ?  117 ARG B CD    1 
ATOM   6529  N  NE    . ARG B 1 117 ? 154.305 138.139 168.048 1.00 44.38 ?  117 ARG B NE    1 
ATOM   6530  C  CZ    . ARG B 1 117 ? 155.185 137.933 169.020 1.00 45.70 ?  117 ARG B CZ    1 
ATOM   6531  N  NH1   . ARG B 1 117 ? 156.371 138.519 169.016 1.00 43.54 1  117 ARG B NH1   1 
ATOM   6532  N  NH2   . ARG B 1 117 ? 154.868 137.113 170.018 1.00 47.75 ?  117 ARG B NH2   1 
ATOM   6533  N  N     . TYR B 1 118 ? 150.179 140.985 166.859 1.00 41.03 ?  118 TYR B N     1 
ATOM   6534  C  CA    . TYR B 1 118 ? 148.847 141.564 166.999 1.00 35.12 ?  118 TYR B CA    1 
ATOM   6535  C  C     . TYR B 1 118 ? 148.935 143.045 167.340 1.00 38.01 ?  118 TYR B C     1 
ATOM   6536  O  O     . TYR B 1 118 ? 148.196 143.868 166.784 1.00 40.88 ?  118 TYR B O     1 
ATOM   6537  C  CB    . TYR B 1 118 ? 148.054 140.806 168.060 1.00 36.39 ?  118 TYR B CB    1 
ATOM   6538  C  CG    . TYR B 1 118 ? 146.574 141.107 168.047 1.00 38.14 ?  118 TYR B CG    1 
ATOM   6539  C  CD1   . TYR B 1 118 ? 145.826 140.950 166.889 1.00 33.51 ?  118 TYR B CD1   1 
ATOM   6540  C  CD2   . TYR B 1 118 ? 145.927 141.548 169.190 1.00 36.95 ?  118 TYR B CD2   1 
ATOM   6541  C  CE1   . TYR B 1 118 ? 144.477 141.223 166.872 1.00 33.42 ?  118 TYR B CE1   1 
ATOM   6542  C  CE2   . TYR B 1 118 ? 144.576 141.819 169.184 1.00 33.77 ?  118 TYR B CE2   1 
ATOM   6543  C  CZ    . TYR B 1 118 ? 143.856 141.656 168.021 1.00 35.25 ?  118 TYR B CZ    1 
ATOM   6544  O  OH    . TYR B 1 118 ? 142.509 141.930 168.008 1.00 45.00 ?  118 TYR B OH    1 
ATOM   6545  N  N     . GLU B 1 119 ? 149.852 143.402 168.241 1.00 44.44 ?  119 GLU B N     1 
ATOM   6546  C  CA    . GLU B 1 119 ? 150.014 144.798 168.626 1.00 38.64 ?  119 GLU B CA    1 
ATOM   6547  C  C     . GLU B 1 119 ? 150.501 145.648 167.459 1.00 38.45 ?  119 GLU B C     1 
ATOM   6548  O  O     . GLU B 1 119 ? 150.061 146.788 167.298 1.00 49.14 ?  119 GLU B O     1 
ATOM   6549  C  CB    . GLU B 1 119 ? 150.972 144.903 169.811 1.00 38.99 ?  119 GLU B CB    1 
ATOM   6550  C  CG    . GLU B 1 119 ? 150.431 144.296 171.093 1.00 39.79 ?  119 GLU B CG    1 
ATOM   6551  C  CD    . GLU B 1 119 ? 150.871 142.859 171.290 1.00 45.71 ?  119 GLU B CD    1 
ATOM   6552  O  OE1   . GLU B 1 119 ? 151.111 142.164 170.280 1.00 45.33 ?  119 GLU B OE1   1 
ATOM   6553  O  OE2   . GLU B 1 119 ? 150.974 142.421 172.455 1.00 46.42 -1 119 GLU B OE2   1 
ATOM   6554  N  N     . ASP B 1 120 ? 151.413 145.120 166.639 1.00 40.96 ?  120 ASP B N     1 
ATOM   6555  C  CA    . ASP B 1 120 ? 151.896 145.887 165.492 1.00 39.84 ?  120 ASP B CA    1 
ATOM   6556  C  C     . ASP B 1 120 ? 150.782 146.131 164.482 1.00 39.51 ?  120 ASP B C     1 
ATOM   6557  O  O     . ASP B 1 120 ? 150.632 147.244 163.964 1.00 44.82 ?  120 ASP B O     1 
ATOM   6558  C  CB    . ASP B 1 120 ? 153.071 145.170 164.828 1.00 45.29 ?  120 ASP B CB    1 
ATOM   6559  C  CG    . ASP B 1 120 ? 154.071 144.639 165.828 1.00 47.85 ?  120 ASP B CG    1 
ATOM   6560  O  OD1   . ASP B 1 120 ? 154.485 143.472 165.689 1.00 51.60 ?  120 ASP B OD1   1 
ATOM   6561  O  OD2   . ASP B 1 120 ? 154.438 145.388 166.756 1.00 46.55 -1 120 ASP B OD2   1 
ATOM   6562  N  N     . ARG B 1 121 ? 149.995 145.095 164.185 1.00 34.52 ?  121 ARG B N     1 
ATOM   6563  C  CA    . ARG B 1 121 ? 148.873 145.252 163.266 1.00 31.09 ?  121 ARG B CA    1 
ATOM   6564  C  C     . ARG B 1 121 ? 147.866 146.260 163.798 1.00 35.79 ?  121 ARG B C     1 
ATOM   6565  O  O     . ARG B 1 121 ? 147.379 147.120 163.052 1.00 45.87 ?  121 ARG B O     1 
ATOM   6566  C  CB    . ARG B 1 121 ? 148.209 143.896 163.024 1.00 35.38 ?  121 ARG B CB    1 
ATOM   6567  C  CG    . ARG B 1 121 ? 146.958 143.941 162.167 1.00 32.93 ?  121 ARG B CG    1 
ATOM   6568  C  CD    . ARG B 1 121 ? 147.288 143.828 160.694 1.00 32.41 ?  121 ARG B CD    1 
ATOM   6569  N  NE    . ARG B 1 121 ? 147.104 145.100 160.008 1.00 43.28 ?  121 ARG B NE    1 
ATOM   6570  C  CZ    . ARG B 1 121 ? 147.897 145.555 159.048 1.00 39.89 ?  121 ARG B CZ    1 
ATOM   6571  N  NH1   . ARG B 1 121 ? 148.943 144.863 158.631 1.00 42.44 1  121 ARG B NH1   1 
ATOM   6572  N  NH2   . ARG B 1 121 ? 147.634 146.734 158.497 1.00 32.92 ?  121 ARG B NH2   1 
ATOM   6573  N  N     . ILE B 1 122 ? 147.555 146.185 165.093 1.00 35.39 ?  122 ILE B N     1 
ATOM   6574  C  CA    . ILE B 1 122 ? 146.594 147.113 165.679 1.00 29.58 ?  122 ILE B CA    1 
ATOM   6575  C  C     . ILE B 1 122 ? 147.139 148.536 165.666 1.00 30.42 ?  122 ILE B C     1 
ATOM   6576  O  O     . ILE B 1 122 ? 146.408 149.489 165.381 1.00 37.63 ?  122 ILE B O     1 
ATOM   6577  C  CB    . ILE B 1 122 ? 146.208 146.648 167.094 1.00 35.40 ?  122 ILE B CB    1 
ATOM   6578  C  CG1   . ILE B 1 122 ? 145.148 145.551 166.997 1.00 32.27 ?  122 ILE B CG1   1 
ATOM   6579  C  CG2   . ILE B 1 122 ? 145.704 147.810 167.937 1.00 31.89 ?  122 ILE B CG2   1 
ATOM   6580  C  CD1   . ILE B 1 122 ? 144.524 145.191 168.306 1.00 32.92 ?  122 ILE B CD1   1 
ATOM   6581  N  N     . SER B 1 123 ? 148.431 148.706 165.959 1.00 33.76 ?  123 SER B N     1 
ATOM   6582  C  CA    . SER B 1 123 ? 149.031 150.035 165.928 1.00 32.60 ?  123 SER B CA    1 
ATOM   6583  C  C     . SER B 1 123 ? 149.003 150.624 164.527 1.00 36.18 ?  123 SER B C     1 
ATOM   6584  O  O     . SER B 1 123 ? 148.708 151.810 164.350 1.00 36.84 ?  123 SER B O     1 
ATOM   6585  C  CB    . SER B 1 123 ? 150.468 149.978 166.442 1.00 32.05 ?  123 SER B CB    1 
ATOM   6586  O  OG    . SER B 1 123 ? 150.525 149.415 167.733 1.00 37.98 ?  123 SER B OG    1 
ATOM   6587  N  N     . ILE B 1 124 ? 149.315 149.813 163.515 1.00 36.71 ?  124 ILE B N     1 
ATOM   6588  C  CA    . ILE B 1 124 ? 149.298 150.310 162.144 1.00 34.76 ?  124 ILE B CA    1 
ATOM   6589  C  C     . ILE B 1 124 ? 147.882 150.681 161.726 1.00 39.62 ?  124 ILE B C     1 
ATOM   6590  O  O     . ILE B 1 124 ? 147.659 151.725 161.099 1.00 39.84 ?  124 ILE B O     1 
ATOM   6591  C  CB    . ILE B 1 124 ? 149.929 149.275 161.197 1.00 39.41 ?  124 ILE B CB    1 
ATOM   6592  C  CG1   . ILE B 1 124 ? 151.450 149.298 161.346 1.00 41.25 ?  124 ILE B CG1   1 
ATOM   6593  C  CG2   . ILE B 1 124 ? 149.532 149.548 159.756 1.00 36.46 ?  124 ILE B CG2   1 
ATOM   6594  C  CD1   . ILE B 1 124 ? 152.055 150.680 161.215 1.00 36.63 ?  124 ILE B CD1   1 
ATOM   6595  N  N     . VAL B 1 125 ? 146.900 149.848 162.080 1.00 32.40 ?  125 VAL B N     1 
ATOM   6596  C  CA    . VAL B 1 125 ? 145.513 150.150 161.740 1.00 30.50 ?  125 VAL B CA    1 
ATOM   6597  C  C     . VAL B 1 125 ? 145.060 151.432 162.430 1.00 25.65 ?  125 VAL B C     1 
ATOM   6598  O  O     . VAL B 1 125 ? 144.379 152.270 161.829 1.00 35.98 ?  125 VAL B O     1 
ATOM   6599  C  CB    . VAL B 1 125 ? 144.606 148.955 162.091 1.00 37.24 ?  125 VAL B CB    1 
ATOM   6600  C  CG1   . VAL B 1 125 ? 143.146 149.349 162.014 1.00 32.65 ?  125 VAL B CG1   1 
ATOM   6601  C  CG2   . VAL B 1 125 ? 144.883 147.793 161.154 1.00 27.59 ?  125 VAL B CG2   1 
ATOM   6602  N  N     . ALA B 1 126 ? 145.440 151.612 163.696 1.00 24.10 ?  126 ALA B N     1 
ATOM   6603  C  CA    . ALA B 1 126 ? 145.058 152.817 164.428 1.00 26.21 ?  126 ALA B CA    1 
ATOM   6604  C  C     . ALA B 1 126 ? 145.724 154.061 163.854 1.00 31.08 ?  126 ALA B C     1 
ATOM   6605  O  O     . ALA B 1 126 ? 145.094 155.121 163.761 1.00 34.62 ?  126 ALA B O     1 
ATOM   6606  C  CB    . ALA B 1 126 ? 145.412 152.661 165.904 1.00 29.96 ?  126 ALA B CB    1 
ATOM   6607  N  N     . LEU B 1 127 ? 147.001 153.956 163.482 1.00 36.91 ?  127 LEU B N     1 
ATOM   6608  C  CA    . LEU B 1 127 ? 147.698 155.096 162.897 1.00 26.42 ?  127 LEU B CA    1 
ATOM   6609  C  C     . LEU B 1 127 ? 147.110 155.458 161.543 1.00 26.74 ?  127 LEU B C     1 
ATOM   6610  O  O     . LEU B 1 127 ? 147.073 156.636 161.169 1.00 33.01 ?  127 LEU B O     1 
ATOM   6611  C  CB    . LEU B 1 127 ? 149.191 154.792 162.772 1.00 28.93 ?  127 LEU B CB    1 
ATOM   6612  C  CG    . LEU B 1 127 ? 150.009 154.787 164.064 1.00 32.83 ?  127 LEU B CG    1 
ATOM   6613  C  CD1   . LEU B 1 127 ? 151.314 154.039 163.865 1.00 38.52 ?  127 LEU B CD1   1 
ATOM   6614  C  CD2   . LEU B 1 127 ? 150.273 156.200 164.544 1.00 33.35 ?  127 LEU B CD2   1 
ATOM   6615  N  N     . PHE B 1 128 ? 146.653 154.458 160.787 1.00 32.50 ?  128 PHE B N     1 
ATOM   6616  C  CA    . PHE B 1 128 ? 145.966 154.741 159.532 1.00 33.27 ?  128 PHE B CA    1 
ATOM   6617  C  C     . PHE B 1 128 ? 144.606 155.384 159.786 1.00 30.13 ?  128 PHE B C     1 
ATOM   6618  O  O     . PHE B 1 128 ? 144.194 156.286 159.048 1.00 40.74 ?  128 PHE B O     1 
ATOM   6619  C  CB    . PHE B 1 128 ? 145.838 153.452 158.714 1.00 29.67 ?  128 PHE B CB    1 
ATOM   6620  C  CG    . PHE B 1 128 ? 144.854 153.535 157.580 1.00 35.44 ?  128 PHE B CG    1 
ATOM   6621  C  CD1   . PHE B 1 128 ? 143.508 153.265 157.776 1.00 33.75 ?  128 PHE B CD1   1 
ATOM   6622  C  CD2   . PHE B 1 128 ? 145.280 153.887 156.311 1.00 37.02 ?  128 PHE B CD2   1 
ATOM   6623  C  CE1   . PHE B 1 128 ? 142.613 153.348 156.732 1.00 34.62 ?  128 PHE B CE1   1 
ATOM   6624  C  CE2   . PHE B 1 128 ? 144.388 153.969 155.265 1.00 36.99 ?  128 PHE B CE2   1 
ATOM   6625  C  CZ    . PHE B 1 128 ? 143.054 153.700 155.475 1.00 34.68 ?  128 PHE B CZ    1 
ATOM   6626  N  N     . PHE B 1 129 ? 143.894 154.926 160.818 1.00 27.70 ?  129 PHE B N     1 
ATOM   6627  C  CA    . PHE B 1 129 ? 142.586 155.490 161.138 1.00 21.42 ?  129 PHE B CA    1 
ATOM   6628  C  C     . PHE B 1 129 ? 142.690 156.948 161.563 1.00 30.37 ?  129 PHE B C     1 
ATOM   6629  O  O     . PHE B 1 129 ? 141.880 157.782 161.144 1.00 33.81 ?  129 PHE B O     1 
ATOM   6630  C  CB    . PHE B 1 129 ? 141.917 154.680 162.246 1.00 24.55 ?  129 PHE B CB    1 
ATOM   6631  C  CG    . PHE B 1 129 ? 141.263 153.419 161.775 1.00 26.58 ?  129 PHE B CG    1 
ATOM   6632  C  CD1   . PHE B 1 129 ? 141.023 153.204 160.431 1.00 26.21 ?  129 PHE B CD1   1 
ATOM   6633  C  CD2   . PHE B 1 129 ? 140.878 152.450 162.684 1.00 28.07 ?  129 PHE B CD2   1 
ATOM   6634  C  CE1   . PHE B 1 129 ? 140.418 152.041 160.004 1.00 25.06 ?  129 PHE B CE1   1 
ATOM   6635  C  CE2   . PHE B 1 129 ? 140.270 151.288 162.263 1.00 30.63 ?  129 PHE B CE2   1 
ATOM   6636  C  CZ    . PHE B 1 129 ? 140.041 151.082 160.922 1.00 30.17 ?  129 PHE B CZ    1 
ATOM   6637  N  N     . ALA B 1 130 ? 143.674 157.272 162.405 1.00 35.74 ?  130 ALA B N     1 
ATOM   6638  C  CA    . ALA B 1 130 ? 143.734 158.607 162.991 1.00 35.44 ?  130 ALA B CA    1 
ATOM   6639  C  C     . ALA B 1 130 ? 144.098 159.671 161.964 1.00 42.14 ?  130 ALA B C     1 
ATOM   6640  O  O     . ALA B 1 130 ? 143.669 160.823 162.095 1.00 47.31 ?  130 ALA B O     1 
ATOM   6641  C  CB    . ALA B 1 130 ? 144.728 158.624 164.146 1.00 33.44 ?  130 ALA B CB    1 
ATOM   6642  N  N     . ASN B 1 131 ? 144.889 159.311 160.952 1.00 41.73 ?  131 ASN B N     1 
ATOM   6643  C  CA    . ASN B 1 131 ? 145.247 160.218 159.861 1.00 41.38 ?  131 ASN B CA    1 
ATOM   6644  C  C     . ASN B 1 131 ? 145.965 161.466 160.379 1.00 42.82 ?  131 ASN B C     1 
ATOM   6645  O  O     . ASN B 1 131 ? 145.663 162.594 159.985 1.00 46.71 ?  131 ASN B O     1 
ATOM   6646  C  CB    . ASN B 1 131 ? 144.010 160.596 159.040 1.00 40.39 ?  131 ASN B CB    1 
ATOM   6647  C  CG    . ASN B 1 131 ? 144.352 161.007 157.624 1.00 46.02 ?  131 ASN B CG    1 
ATOM   6648  O  OD1   . ASN B 1 131 ? 145.204 160.400 156.976 1.00 45.99 ?  131 ASN B OD1   1 
ATOM   6649  N  ND2   . ASN B 1 131 ? 143.686 162.044 157.133 1.00 44.13 ?  131 ASN B ND2   1 
ATOM   6650  N  N     . GLY B 1 132 ? 146.928 161.255 161.273 1.00 42.48 ?  132 GLY B N     1 
ATOM   6651  C  CA    . GLY B 1 132 ? 147.782 162.321 161.759 1.00 39.49 ?  132 GLY B CA    1 
ATOM   6652  C  C     . GLY B 1 132 ? 147.549 162.741 163.194 1.00 44.84 ?  132 GLY B C     1 
ATOM   6653  O  O     . GLY B 1 132 ? 148.321 163.561 163.707 1.00 50.55 ?  132 GLY B O     1 
ATOM   6654  N  N     . ASP B 1 133 ? 146.527 162.216 163.862 1.00 46.99 ?  133 ASP B N     1 
ATOM   6655  C  CA    . ASP B 1 133 ? 146.221 162.581 165.239 1.00 47.34 ?  133 ASP B CA    1 
ATOM   6656  C  C     . ASP B 1 133 ? 146.783 161.516 166.175 1.00 48.68 ?  133 ASP B C     1 
ATOM   6657  O  O     . ASP B 1 133 ? 146.405 160.344 166.088 1.00 48.93 ?  133 ASP B O     1 
ATOM   6658  C  CB    . ASP B 1 133 ? 144.713 162.734 165.436 1.00 47.18 ?  133 ASP B CB    1 
ATOM   6659  C  CG    . ASP B 1 133 ? 144.360 163.478 166.710 1.00 52.90 ?  133 ASP B CG    1 
ATOM   6660  O  OD1   . ASP B 1 133 ? 145.254 163.677 167.558 1.00 54.28 ?  133 ASP B OD1   1 
ATOM   6661  O  OD2   . ASP B 1 133 ? 143.181 163.858 166.866 1.00 50.36 -1 133 ASP B OD2   1 
ATOM   6662  N  N     . THR B 1 134 ? 147.682 161.926 167.071 1.00 49.26 ?  134 THR B N     1 
ATOM   6663  C  CA    . THR B 1 134 ? 148.319 160.963 167.965 1.00 45.20 ?  134 THR B CA    1 
ATOM   6664  C  C     . THR B 1 134 ? 147.364 160.498 169.058 1.00 47.30 ?  134 THR B C     1 
ATOM   6665  O  O     . THR B 1 134 ? 147.314 159.305 169.379 1.00 50.75 ?  134 THR B O     1 
ATOM   6666  C  CB    . THR B 1 134 ? 149.577 161.572 168.577 1.00 53.73 ?  134 THR B CB    1 
ATOM   6667  O  OG1   . THR B 1 134 ? 150.443 162.018 167.528 1.00 55.93 ?  134 THR B OG1   1 
ATOM   6668  C  CG2   . THR B 1 134 ? 150.306 160.545 169.427 1.00 50.56 ?  134 THR B CG2   1 
ATOM   6669  N  N     . GLU B 1 135 ? 146.602 161.423 169.645 1.00 46.01 ?  135 GLU B N     1 
ATOM   6670  C  CA    . GLU B 1 135 ? 145.635 161.039 170.667 1.00 45.42 ?  135 GLU B CA    1 
ATOM   6671  C  C     . GLU B 1 135 ? 144.537 160.159 170.082 1.00 50.14 ?  135 GLU B C     1 
ATOM   6672  O  O     . GLU B 1 135 ? 144.107 159.190 170.716 1.00 51.83 ?  135 GLU B O     1 
ATOM   6673  C  CB    . GLU B 1 135 ? 145.039 162.284 171.321 1.00 47.74 ?  135 GLU B CB    1 
ATOM   6674  C  CG    . GLU B 1 135 ? 146.077 163.237 171.887 1.00 48.68 ?  135 GLU B CG    1 
ATOM   6675  C  CD    . GLU B 1 135 ? 147.184 162.519 172.630 1.00 55.32 ?  135 GLU B CD    1 
ATOM   6676  O  OE1   . GLU B 1 135 ? 146.887 161.847 173.640 1.00 54.01 ?  135 GLU B OE1   1 
ATOM   6677  O  OE2   . GLU B 1 135 ? 148.353 162.624 172.203 1.00 55.95 -1 135 GLU B OE2   1 
ATOM   6678  N  N     . LYS B 1 136 ? 144.074 160.485 168.874 1.00 40.63 ?  136 LYS B N     1 
ATOM   6679  C  CA    . LYS B 1 136 ? 143.086 159.642 168.209 1.00 38.65 ?  136 LYS B CA    1 
ATOM   6680  C  C     . LYS B 1 136 ? 143.655 158.260 167.911 1.00 39.71 ?  136 LYS B C     1 
ATOM   6681  O  O     . LYS B 1 136 ? 142.958 157.249 168.053 1.00 46.00 ?  136 LYS B O     1 
ATOM   6682  C  CB    . LYS B 1 136 ? 142.606 160.318 166.925 1.00 46.29 ?  136 LYS B CB    1 
ATOM   6683  C  CG    . LYS B 1 136 ? 141.319 159.759 166.356 1.00 41.83 ?  136 LYS B CG    1 
ATOM   6684  C  CD    . LYS B 1 136 ? 140.107 160.352 167.044 1.00 43.62 ?  136 LYS B CD    1 
ATOM   6685  C  CE    . LYS B 1 136 ? 138.834 160.038 166.278 1.00 46.52 ?  136 LYS B CE    1 
ATOM   6686  N  NZ    . LYS B 1 136 ? 137.680 160.835 166.777 1.00 49.13 1  136 LYS B NZ    1 
ATOM   6687  N  N     . ALA B 1 137 ? 144.921 158.195 167.490 1.00 34.81 ?  137 ALA B N     1 
ATOM   6688  C  CA    . ALA B 1 137 ? 145.554 156.905 167.240 1.00 31.55 ?  137 ALA B CA    1 
ATOM   6689  C  C     . ALA B 1 137 ? 145.654 156.085 168.519 1.00 35.22 ?  137 ALA B C     1 
ATOM   6690  O  O     . ALA B 1 137 ? 145.428 154.871 168.505 1.00 38.48 ?  137 ALA B O     1 
ATOM   6691  C  CB    . ALA B 1 137 ? 146.936 157.103 166.620 1.00 31.27 ?  137 ALA B CB    1 
ATOM   6692  N  N     . LYS B 1 138 ? 145.997 156.731 169.635 1.00 39.95 ?  138 LYS B N     1 
ATOM   6693  C  CA    . LYS B 1 138 ? 146.048 156.025 170.911 1.00 38.43 ?  138 LYS B CA    1 
ATOM   6694  C  C     . LYS B 1 138 ? 144.664 155.549 171.332 1.00 38.29 ?  138 LYS B C     1 
ATOM   6695  O  O     . LYS B 1 138 ? 144.519 154.461 171.902 1.00 41.57 ?  138 LYS B O     1 
ATOM   6696  C  CB    . LYS B 1 138 ? 146.659 156.925 171.984 1.00 46.55 ?  138 LYS B CB    1 
ATOM   6697  C  CG    . LYS B 1 138 ? 148.128 156.650 172.252 1.00 45.57 ?  138 LYS B CG    1 
ATOM   6698  C  CD    . LYS B 1 138 ? 148.944 157.929 172.262 1.00 42.75 ?  138 LYS B CD    1 
ATOM   6699  C  CE    . LYS B 1 138 ? 148.426 158.908 173.298 1.00 41.41 ?  138 LYS B CE    1 
ATOM   6700  N  NZ    . LYS B 1 138 ? 149.296 160.112 173.400 1.00 45.27 1  138 LYS B NZ    1 
ATOM   6701  N  N     . GLU B 1 139 ? 143.632 156.353 171.067 1.00 42.21 ?  139 GLU B N     1 
ATOM   6702  C  CA    . GLU B 1 139 ? 142.267 155.930 171.364 1.00 37.82 ?  139 GLU B CA    1 
ATOM   6703  C  C     . GLU B 1 139 ? 141.875 154.711 170.538 1.00 34.72 ?  139 GLU B C     1 
ATOM   6704  O  O     . GLU B 1 139 ? 141.252 153.777 171.056 1.00 43.86 ?  139 GLU B O     1 
ATOM   6705  C  CB    . GLU B 1 139 ? 141.295 157.082 171.117 1.00 36.39 ?  139 GLU B CB    1 
ATOM   6706  C  CG    . GLU B 1 139 ? 140.832 157.776 172.382 1.00 41.29 ?  139 GLU B CG    1 
ATOM   6707  C  CD    . GLU B 1 139 ? 140.653 159.269 172.196 1.00 49.30 ?  139 GLU B CD    1 
ATOM   6708  O  OE1   . GLU B 1 139 ? 140.129 159.679 171.138 1.00 46.90 ?  139 GLU B OE1   1 
ATOM   6709  O  OE2   . GLU B 1 139 ? 141.034 160.032 173.108 1.00 47.07 -1 139 GLU B OE2   1 
ATOM   6710  N  N     . TYR B 1 140 ? 142.228 154.703 169.252 1.00 27.13 ?  140 TYR B N     1 
ATOM   6711  C  CA    . TYR B 1 140 ? 141.953 153.538 168.416 1.00 28.57 ?  140 TYR B CA    1 
ATOM   6712  C  C     . TYR B 1 140 ? 142.727 152.318 168.902 1.00 32.48 ?  140 TYR B C     1 
ATOM   6713  O  O     . TYR B 1 140 ? 142.209 151.193 168.880 1.00 35.20 ?  140 TYR B O     1 
ATOM   6714  C  CB    . TYR B 1 140 ? 142.300 153.834 166.959 1.00 31.21 ?  140 TYR B CB    1 
ATOM   6715  C  CG    . TYR B 1 140 ? 141.319 154.720 166.232 1.00 33.68 ?  140 TYR B CG    1 
ATOM   6716  C  CD1   . TYR B 1 140 ? 139.972 154.394 166.161 1.00 36.18 ?  140 TYR B CD1   1 
ATOM   6717  C  CD2   . TYR B 1 140 ? 141.747 155.875 165.597 1.00 34.26 ?  140 TYR B CD2   1 
ATOM   6718  C  CE1   . TYR B 1 140 ? 139.081 155.202 165.487 1.00 34.00 ?  140 TYR B CE1   1 
ATOM   6719  C  CE2   . TYR B 1 140 ? 140.865 156.685 164.925 1.00 32.61 ?  140 TYR B CE2   1 
ATOM   6720  C  CZ    . TYR B 1 140 ? 139.535 156.348 164.873 1.00 30.34 ?  140 TYR B CZ    1 
ATOM   6721  O  OH    . TYR B 1 140 ? 138.663 157.166 164.197 1.00 37.65 ?  140 TYR B OH    1 
ATOM   6722  N  N     . VAL B 1 141 ? 143.976 152.520 169.326 1.00 36.80 ?  141 VAL B N     1 
ATOM   6723  C  CA    . VAL B 1 141 ? 144.774 151.424 169.869 1.00 34.60 ?  141 VAL B CA    1 
ATOM   6724  C  C     . VAL B 1 141 ? 144.108 150.844 171.107 1.00 31.82 ?  141 VAL B C     1 
ATOM   6725  O  O     . VAL B 1 141 ? 144.019 149.624 171.266 1.00 38.24 ?  141 VAL B O     1 
ATOM   6726  C  CB    . VAL B 1 141 ? 146.206 151.899 170.176 1.00 36.80 ?  141 VAL B CB    1 
ATOM   6727  C  CG1   . VAL B 1 141 ? 146.859 150.981 171.181 1.00 35.04 ?  141 VAL B CG1   1 
ATOM   6728  C  CG2   . VAL B 1 141 ? 147.028 151.927 168.916 1.00 35.06 ?  141 VAL B CG2   1 
ATOM   6729  N  N     . ASN B 1 142 ? 143.639 151.708 172.007 1.00 33.90 ?  142 ASN B N     1 
ATOM   6730  C  CA    . ASN B 1 142 ? 142.959 151.221 173.203 1.00 33.04 ?  142 ASN B CA    1 
ATOM   6731  C  C     . ASN B 1 142 ? 141.665 150.506 172.843 1.00 34.96 ?  142 ASN B C     1 
ATOM   6732  O  O     . ASN B 1 142 ? 141.313 149.498 173.465 1.00 41.23 ?  142 ASN B O     1 
ATOM   6733  C  CB    . ASN B 1 142 ? 142.690 152.378 174.161 1.00 30.82 ?  142 ASN B CB    1 
ATOM   6734  C  CG    . ASN B 1 142 ? 143.931 152.807 174.914 1.00 36.66 ?  142 ASN B CG    1 
ATOM   6735  O  OD1   . ASN B 1 142 ? 144.656 151.977 175.461 1.00 37.28 ?  142 ASN B OD1   1 
ATOM   6736  N  ND2   . ASN B 1 142 ? 144.184 154.109 174.944 1.00 38.79 ?  142 ASN B ND2   1 
ATOM   6737  N  N     . LEU B 1 143 ? 140.943 151.014 171.843 1.00 34.18 ?  143 LEU B N     1 
ATOM   6738  C  CA    . LEU B 1 143 ? 139.687 150.392 171.440 1.00 28.75 ?  143 LEU B CA    1 
ATOM   6739  C  C     . LEU B 1 143 ? 139.909 149.002 170.858 1.00 32.78 ?  143 LEU B C     1 
ATOM   6740  O  O     . LEU B 1 143 ? 139.136 148.078 171.132 1.00 36.15 ?  143 LEU B O     1 
ATOM   6741  C  CB    . LEU B 1 143 ? 138.966 151.285 170.434 1.00 28.80 ?  143 LEU B CB    1 
ATOM   6742  C  CG    . LEU B 1 143 ? 137.455 151.101 170.350 1.00 34.07 ?  143 LEU B CG    1 
ATOM   6743  C  CD1   . LEU B 1 143 ? 136.797 151.668 171.593 1.00 32.88 ?  143 LEU B CD1   1 
ATOM   6744  C  CD2   . LEU B 1 143 ? 136.915 151.765 169.101 1.00 33.46 ?  143 LEU B CD2   1 
ATOM   6745  N  N     . MET B 1 144 ? 140.953 148.832 170.048 1.00 34.58 ?  144 MET B N     1 
ATOM   6746  C  CA    . MET B 1 144 ? 141.173 147.562 169.366 1.00 24.95 ?  144 MET B CA    1 
ATOM   6747  C  C     . MET B 1 144 ? 141.961 146.555 170.195 1.00 25.64 ?  144 MET B C     1 
ATOM   6748  O  O     . MET B 1 144 ? 141.697 145.352 170.100 1.00 34.30 ?  144 MET B O     1 
ATOM   6749  C  CB    . MET B 1 144 ? 141.881 147.800 168.030 1.00 27.95 ?  144 MET B CB    1 
ATOM   6750  C  CG    . MET B 1 144 ? 141.042 148.576 167.029 1.00 28.00 ?  144 MET B CG    1 
ATOM   6751  S  SD    . MET B 1 144 ? 141.759 148.593 165.380 1.00 45.60 ?  144 MET B SD    1 
ATOM   6752  C  CE    . MET B 1 144 ? 143.196 149.617 165.663 1.00 26.96 ?  144 MET B CE    1 
ATOM   6753  N  N     . ILE B 1 145 ? 142.930 147.007 170.995 1.00 28.38 ?  145 ILE B N     1 
ATOM   6754  C  CA    . ILE B 1 145 ? 143.670 146.085 171.850 1.00 29.34 ?  145 ILE B CA    1 
ATOM   6755  C  C     . ILE B 1 145 ? 142.789 145.590 172.989 1.00 35.80 ?  145 ILE B C     1 
ATOM   6756  O  O     . ILE B 1 145 ? 142.949 144.457 173.458 1.00 39.90 ?  145 ILE B O     1 
ATOM   6757  C  CB    . ILE B 1 145 ? 144.971 146.742 172.356 1.00 31.03 ?  145 ILE B CB    1 
ATOM   6758  C  CG1   . ILE B 1 145 ? 146.055 145.684 172.573 1.00 32.44 ?  145 ILE B CG1   1 
ATOM   6759  C  CG2   . ILE B 1 145 ? 144.741 147.536 173.635 1.00 33.30 ?  145 ILE B CG2   1 
ATOM   6760  C  CD1   . ILE B 1 145 ? 146.566 145.059 171.299 1.00 35.50 ?  145 ILE B CD1   1 
ATOM   6761  N  N     . ASN B 1 146 ? 141.844 146.415 173.449 1.00 33.84 ?  146 ASN B N     1 
ATOM   6762  C  CA    . ASN B 1 146 ? 140.804 145.933 174.345 1.00 27.26 ?  146 ASN B CA    1 
ATOM   6763  C  C     . ASN B 1 146 ? 139.785 145.075 173.615 1.00 29.59 ?  146 ASN B C     1 
ATOM   6764  O  O     . ASN B 1 146 ? 138.933 144.464 174.267 1.00 38.22 ?  146 ASN B O     1 
ATOM   6765  C  CB    . ASN B 1 146 ? 140.097 147.104 175.026 1.00 27.33 ?  146 ASN B CB    1 
ATOM   6766  C  CG    . ASN B 1 146 ? 140.976 147.806 176.037 1.00 33.18 ?  146 ASN B CG    1 
ATOM   6767  O  OD1   . ASN B 1 146 ? 141.972 147.253 176.500 1.00 41.26 ?  146 ASN B OD1   1 
ATOM   6768  N  ND2   . ASN B 1 146 ? 140.613 149.034 176.382 1.00 34.54 ?  146 ASN B ND2   1 
ATOM   6769  N  N     . GLN B 1 147 ? 139.859 145.031 172.284 1.00 33.55 ?  147 GLN B N     1 
ATOM   6770  C  CA    . GLN B 1 147 ? 138.990 144.201 171.455 1.00 24.10 ?  147 GLN B CA    1 
ATOM   6771  C  C     . GLN B 1 147 ? 137.525 144.575 171.642 1.00 23.97 ?  147 GLN B C     1 
ATOM   6772  O  O     . GLN B 1 147 ? 136.644 143.716 171.648 1.00 38.00 ?  147 GLN B O     1 
ATOM   6773  C  CB    . GLN B 1 147 ? 139.222 142.715 171.732 1.00 23.94 ?  147 GLN B CB    1 
ATOM   6774  C  CG    . GLN B 1 147 ? 140.579 142.222 171.268 1.00 24.48 ?  147 GLN B CG    1 
ATOM   6775  C  CD    . GLN B 1 147 ? 140.643 140.720 171.153 1.00 31.06 ?  147 GLN B CD    1 
ATOM   6776  O  OE1   . GLN B 1 147 ? 140.172 139.998 172.031 1.00 41.78 ?  147 GLN B OE1   1 
ATOM   6777  N  NE2   . GLN B 1 147 ? 141.232 140.235 170.069 1.00 31.16 ?  147 GLN B NE2   1 
ATOM   6778  N  N     . GLU B 1 148 ? 137.264 145.871 171.809 1.00 25.67 ?  148 GLU B N     1 
ATOM   6779  C  CA    . GLU B 1 148 ? 135.891 146.359 171.825 1.00 23.25 ?  148 GLU B CA    1 
ATOM   6780  C  C     . GLU B 1 148 ? 135.351 146.564 170.419 1.00 29.08 ?  148 GLU B C     1 
ATOM   6781  O  O     . GLU B 1 148 ? 134.153 146.373 170.184 1.00 35.96 ?  148 GLU B O     1 
ATOM   6782  C  CB    . GLU B 1 148 ? 135.801 147.669 172.604 1.00 18.14 ?  148 GLU B CB    1 
ATOM   6783  C  CG    . GLU B 1 148 ? 136.172 147.559 174.065 1.00 21.97 ?  148 GLU B CG    1 
ATOM   6784  C  CD    . GLU B 1 148 ? 136.555 148.897 174.659 1.00 35.44 ?  148 GLU B CD    1 
ATOM   6785  O  OE1   . GLU B 1 148 ? 137.691 149.352 174.420 1.00 35.25 ?  148 GLU B OE1   1 
ATOM   6786  O  OE2   . GLU B 1 148 ? 135.717 149.500 175.363 1.00 42.82 -1 148 GLU B OE2   1 
ATOM   6787  N  N     . TYR B 1 149 ? 136.210 146.952 169.482 1.00 26.98 ?  149 TYR B N     1 
ATOM   6788  C  CA    . TYR B 1 149 ? 135.827 147.171 168.096 1.00 19.69 ?  149 TYR B CA    1 
ATOM   6789  C  C     . TYR B 1 149 ? 136.799 146.434 167.192 1.00 24.35 ?  149 TYR B C     1 
ATOM   6790  O  O     . TYR B 1 149 ? 138.016 146.533 167.369 1.00 32.74 ?  149 TYR B O     1 
ATOM   6791  C  CB    . TYR B 1 149 ? 135.817 148.660 167.750 1.00 22.94 ?  149 TYR B CB    1 
ATOM   6792  C  CG    . TYR B 1 149 ? 135.693 148.938 166.271 1.00 24.46 ?  149 TYR B CG    1 
ATOM   6793  C  CD1   . TYR B 1 149 ? 134.561 148.556 165.567 1.00 19.89 ?  149 TYR B CD1   1 
ATOM   6794  C  CD2   . TYR B 1 149 ? 136.712 149.578 165.579 1.00 17.39 ?  149 TYR B CD2   1 
ATOM   6795  C  CE1   . TYR B 1 149 ? 134.445 148.806 164.217 1.00 19.99 ?  149 TYR B CE1   1 
ATOM   6796  C  CE2   . TYR B 1 149 ? 136.604 149.831 164.229 1.00 24.90 ?  149 TYR B CE2   1 
ATOM   6797  C  CZ    . TYR B 1 149 ? 135.467 149.445 163.553 1.00 20.08 ?  149 TYR B CZ    1 
ATOM   6798  O  OH    . TYR B 1 149 ? 135.354 149.694 162.206 1.00 16.11 ?  149 TYR B OH    1 
ATOM   6799  N  N     . GLN B 1 150 ? 136.259 145.698 166.231 1.00 19.57 ?  150 GLN B N     1 
ATOM   6800  C  CA    . GLN B 1 150 ? 137.066 144.982 165.246 1.00 12.37 ?  150 GLN B CA    1 
ATOM   6801  C  C     . GLN B 1 150 ? 136.761 145.515 163.858 1.00 20.86 ?  150 GLN B C     1 
ATOM   6802  O  O     . GLN B 1 150 ? 135.631 145.336 163.364 1.00 32.26 ?  150 GLN B O     1 
ATOM   6803  C  CB    . GLN B 1 150 ? 136.794 143.480 165.314 1.00 19.69 ?  150 GLN B CB    1 
ATOM   6804  C  CG    . GLN B 1 150 ? 137.450 142.657 164.218 1.00 20.88 ?  150 GLN B CG    1 
ATOM   6805  C  CD    . GLN B 1 150 ? 138.951 142.843 164.162 1.00 20.38 ?  150 GLN B CD    1 
ATOM   6806  O  OE1   . GLN B 1 150 ? 139.670 142.459 165.081 1.00 27.08 ?  150 GLN B OE1   1 
ATOM   6807  N  NE2   . GLN B 1 150 ? 139.432 143.427 163.074 1.00 15.99 ?  150 GLN B NE2   1 
ATOM   6808  N  N     . PRO B 1 151 ? 137.704 146.180 163.195 1.00 27.09 ?  151 PRO B N     1 
ATOM   6809  C  CA    . PRO B 1 151 ? 137.502 146.522 161.785 1.00 14.54 ?  151 PRO B CA    1 
ATOM   6810  C  C     . PRO B 1 151 ? 137.352 145.261 160.952 1.00 20.56 ?  151 PRO B C     1 
ATOM   6811  O  O     . PRO B 1 151 ? 137.867 144.196 161.301 1.00 29.40 ?  151 PRO B O     1 
ATOM   6812  C  CB    . PRO B 1 151 ? 138.774 147.294 161.417 1.00 18.53 ?  151 PRO B CB    1 
ATOM   6813  C  CG    . PRO B 1 151 ? 139.351 147.735 162.718 1.00 20.87 ?  151 PRO B CG    1 
ATOM   6814  C  CD    . PRO B 1 151 ? 138.983 146.687 163.713 1.00 17.91 ?  151 PRO B CD    1 
ATOM   6815  N  N     . SER B 1 152 ? 136.620 145.384 159.850 1.00 24.85 ?  152 SER B N     1 
ATOM   6816  C  CA    . SER B 1 152 ? 136.339 144.231 159.011 1.00 18.45 ?  152 SER B CA    1 
ATOM   6817  C  C     . SER B 1 152 ? 137.630 143.616 158.479 1.00 24.70 ?  152 SER B C     1 
ATOM   6818  O  O     . SER B 1 152 ? 138.704 144.220 158.523 1.00 25.54 ?  152 SER B O     1 
ATOM   6819  C  CB    . SER B 1 152 ? 135.432 144.625 157.847 1.00 21.43 ?  152 SER B CB    1 
ATOM   6820  O  OG    . SER B 1 152 ? 136.089 145.521 156.971 1.00 26.76 ?  152 SER B OG    1 
ATOM   6821  N  N     . THR B 1 153 ? 137.510 142.388 157.981 1.00 32.55 ?  153 THR B N     1 
ATOM   6822  C  CA    . THR B 1 153 ? 138.660 141.691 157.412 1.00 20.41 ?  153 THR B CA    1 
ATOM   6823  C  C     . THR B 1 153 ? 139.395 142.506 156.353 1.00 31.50 ?  153 THR B C     1 
ATOM   6824  O  O     . THR B 1 153 ? 140.634 142.564 156.420 1.00 34.82 ?  153 THR B O     1 
ATOM   6825  C  CB    . THR B 1 153 ? 138.211 140.335 156.845 1.00 27.31 ?  153 THR B CB    1 
ATOM   6826  O  OG1   . THR B 1 153 ? 137.904 139.442 157.922 1.00 33.85 ?  153 THR B OG1   1 
ATOM   6827  C  CG2   . THR B 1 153 ? 139.300 139.720 155.984 1.00 30.48 ?  153 THR B CG2   1 
ATOM   6828  N  N     . PRO B 1 154 ? 138.736 143.158 155.386 1.00 33.93 ?  154 PRO B N     1 
ATOM   6829  C  CA    . PRO B 1 154 ? 139.499 144.012 154.457 1.00 21.38 ?  154 PRO B CA    1 
ATOM   6830  C  C     . PRO B 1 154 ? 140.239 145.140 155.153 1.00 22.56 ?  154 PRO B C     1 
ATOM   6831  O  O     . PRO B 1 154 ? 141.435 145.339 154.906 1.00 31.19 ?  154 PRO B O     1 
ATOM   6832  C  CB    . PRO B 1 154 ? 138.417 144.538 153.505 1.00 24.01 ?  154 PRO B CB    1 
ATOM   6833  C  CG    . PRO B 1 154 ? 137.317 143.569 153.612 1.00 22.70 ?  154 PRO B CG    1 
ATOM   6834  C  CD    . PRO B 1 154 ? 137.310 143.112 155.020 1.00 25.54 ?  154 PRO B CD    1 
ATOM   6835  N  N     . THR B 1 155 ? 139.560 145.882 156.028 1.00 25.99 ?  155 THR B N     1 
ATOM   6836  C  CA    . THR B 1 155 ? 140.202 147.002 156.708 1.00 22.14 ?  155 THR B CA    1 
ATOM   6837  C  C     . THR B 1 155 ? 141.325 146.524 157.620 1.00 25.99 ?  155 THR B C     1 
ATOM   6838  O  O     . THR B 1 155 ? 142.444 147.042 157.568 1.00 25.30 ?  155 THR B O     1 
ATOM   6839  C  CB    . THR B 1 155 ? 139.167 147.794 157.507 1.00 23.99 ?  155 THR B CB    1 
ATOM   6840  O  OG1   . THR B 1 155 ? 138.054 148.113 156.666 1.00 26.39 ?  155 THR B OG1   1 
ATOM   6841  C  CG2   . THR B 1 155 ? 139.779 149.075 158.034 1.00 20.80 ?  155 THR B CG2   1 
ATOM   6842  N  N     . PHE B 1 156 ? 141.045 145.527 158.461 1.00 30.04 ?  156 PHE B N     1 
ATOM   6843  C  CA    . PHE B 1 156 ? 142.050 145.047 159.401 1.00 21.34 ?  156 PHE B CA    1 
ATOM   6844  C  C     . PHE B 1 156 ? 143.253 144.456 158.677 1.00 29.13 ?  156 PHE B C     1 
ATOM   6845  O  O     . PHE B 1 156 ? 144.399 144.668 159.085 1.00 32.96 ?  156 PHE B O     1 
ATOM   6846  C  CB    . PHE B 1 156 ? 141.433 144.017 160.346 1.00 26.41 ?  156 PHE B CB    1 
ATOM   6847  C  CG    . PHE B 1 156 ? 142.219 143.801 161.605 1.00 30.29 ?  156 PHE B CG    1 
ATOM   6848  C  CD1   . PHE B 1 156 ? 142.508 144.861 162.446 1.00 28.22 ?  156 PHE B CD1   1 
ATOM   6849  C  CD2   . PHE B 1 156 ? 142.669 142.538 161.949 1.00 23.06 ?  156 PHE B CD2   1 
ATOM   6850  C  CE1   . PHE B 1 156 ? 143.232 144.668 163.603 1.00 30.39 ?  156 PHE B CE1   1 
ATOM   6851  C  CE2   . PHE B 1 156 ? 143.392 142.339 163.107 1.00 25.10 ?  156 PHE B CE2   1 
ATOM   6852  C  CZ    . PHE B 1 156 ? 143.674 143.405 163.934 1.00 30.21 ?  156 PHE B CZ    1 
ATOM   6853  N  N     . LEU B 1 157 ? 143.010 143.712 157.598 1.00 32.80 ?  157 LEU B N     1 
ATOM   6854  C  CA    . LEU B 1 157 ? 144.096 143.048 156.889 1.00 27.12 ?  157 LEU B CA    1 
ATOM   6855  C  C     . LEU B 1 157 ? 144.922 144.031 156.067 1.00 33.90 ?  157 LEU B C     1 
ATOM   6856  O  O     . LEU B 1 157 ? 146.151 143.917 156.011 1.00 41.74 ?  157 LEU B O     1 
ATOM   6857  C  CB    . LEU B 1 157 ? 143.526 141.948 155.996 1.00 32.38 ?  157 LEU B CB    1 
ATOM   6858  C  CG    . LEU B 1 157 ? 144.476 141.294 154.993 1.00 33.14 ?  157 LEU B CG    1 
ATOM   6859  C  CD1   . LEU B 1 157 ? 145.502 140.445 155.714 1.00 33.58 ?  157 LEU B CD1   1 
ATOM   6860  C  CD2   . LEU B 1 157 ? 143.697 140.462 153.991 1.00 30.09 ?  157 LEU B CD2   1 
ATOM   6861  N  N     . ASN B 1 158 ? 144.274 145.005 155.430 1.00 35.49 ?  158 ASN B N     1 
ATOM   6862  C  CA    . ASN B 1 158 ? 144.927 145.782 154.386 1.00 28.83 ?  158 ASN B CA    1 
ATOM   6863  C  C     . ASN B 1 158 ? 145.336 147.186 154.806 1.00 32.73 ?  158 ASN B C     1 
ATOM   6864  O  O     . ASN B 1 158 ? 146.149 147.800 154.108 1.00 39.64 ?  158 ASN B O     1 
ATOM   6865  C  CB    . ASN B 1 158 ? 144.011 145.881 153.159 1.00 33.04 ?  158 ASN B CB    1 
ATOM   6866  C  CG    . ASN B 1 158 ? 143.814 144.548 152.474 1.00 38.50 ?  158 ASN B CG    1 
ATOM   6867  O  OD1   . ASN B 1 158 ? 144.762 143.788 152.284 1.00 39.97 ?  158 ASN B OD1   1 
ATOM   6868  N  ND2   . ASN B 1 158 ? 142.576 144.254 152.099 1.00 36.86 ?  158 ASN B ND2   1 
ATOM   6869  N  N     . ALA B 1 159 ? 144.810 147.712 155.911 1.00 32.24 ?  159 ALA B N     1 
ATOM   6870  C  CA    . ALA B 1 159 ? 145.101 149.094 156.279 1.00 32.52 ?  159 ALA B CA    1 
ATOM   6871  C  C     . ALA B 1 159 ? 146.593 149.291 156.507 1.00 38.45 ?  159 ALA B C     1 
ATOM   6872  O  O     . ALA B 1 159 ? 147.227 148.538 157.252 1.00 44.26 ?  159 ALA B O     1 
ATOM   6873  C  CB    . ALA B 1 159 ? 144.322 149.487 157.533 1.00 33.14 ?  159 ALA B CB    1 
ATOM   6874  N  N     . GLY B 1 160 ? 147.151 150.311 155.864 1.00 43.15 ?  160 GLY B N     1 
ATOM   6875  C  CA    . GLY B 1 160 ? 148.561 150.605 156.000 1.00 38.96 ?  160 GLY B CA    1 
ATOM   6876  C  C     . GLY B 1 160 ? 149.496 149.670 155.272 1.00 41.97 ?  160 GLY B C     1 
ATOM   6877  O  O     . GLY B 1 160 ? 150.668 149.575 155.645 1.00 50.62 ?  160 GLY B O     1 
ATOM   6878  N  N     . ARG B 1 161 ? 149.022 148.975 154.242 1.00 44.25 ?  161 ARG B N     1 
ATOM   6879  C  CA    . ARG B 1 161 ? 149.843 148.056 153.470 1.00 44.56 ?  161 ARG B CA    1 
ATOM   6880  C  C     . ARG B 1 161 ? 149.989 148.562 152.041 1.00 48.02 ?  161 ARG B C     1 
ATOM   6881  O  O     . ARG B 1 161 ? 149.013 148.996 151.423 1.00 49.36 ?  161 ARG B O     1 
ATOM   6882  C  CB    . ARG B 1 161 ? 149.242 146.648 153.464 1.00 41.42 ?  161 ARG B CB    1 
ATOM   6883  C  CG    . ARG B 1 161 ? 149.319 145.939 154.803 1.00 41.80 ?  161 ARG B CG    1 
ATOM   6884  C  CD    . ARG B 1 161 ? 149.265 144.434 154.626 1.00 42.34 ?  161 ARG B CD    1 
ATOM   6885  N  NE    . ARG B 1 161 ? 149.215 143.739 155.906 1.00 44.00 ?  161 ARG B NE    1 
ATOM   6886  C  CZ    . ARG B 1 161 ? 148.872 142.468 156.055 1.00 46.38 ?  161 ARG B CZ    1 
ATOM   6887  N  NH1   . ARG B 1 161 ? 148.553 141.712 155.018 1.00 49.01 1  161 ARG B NH1   1 
ATOM   6888  N  NH2   . ARG B 1 161 ? 148.847 141.942 157.276 1.00 45.53 ?  161 ARG B NH2   1 
ATOM   6889  N  N     . LYS B 1 162 ? 151.219 148.507 151.524 1.00 57.73 ?  162 LYS B N     1 
ATOM   6890  C  CA    . LYS B 1 162 ? 151.478 148.979 150.168 1.00 57.20 ?  162 LYS B CA    1 
ATOM   6891  C  C     . LYS B 1 162 ? 150.826 148.070 149.133 1.00 58.40 ?  162 LYS B C     1 
ATOM   6892  O  O     . LYS B 1 162 ? 150.138 148.544 148.221 1.00 60.39 ?  162 LYS B O     1 
ATOM   6893  C  CB    . LYS B 1 162 ? 152.984 149.075 149.929 1.00 57.41 ?  162 LYS B CB    1 
ATOM   6894  C  CG    . LYS B 1 162 ? 153.375 149.285 148.477 1.00 59.42 ?  162 LYS B CG    1 
ATOM   6895  C  CD    . LYS B 1 162 ? 153.323 150.754 148.101 1.00 58.54 ?  162 LYS B CD    1 
ATOM   6896  C  CE    . LYS B 1 162 ? 154.381 151.549 148.847 1.00 57.34 ?  162 LYS B CE    1 
ATOM   6897  N  NZ    . LYS B 1 162 ? 154.070 153.005 148.867 1.00 58.40 1  162 LYS B NZ    1 
ATOM   6898  N  N     . ARG B 1 163 ? 151.029 146.760 149.259 1.00 57.99 ?  163 ARG B N     1 
ATOM   6899  C  CA    . ARG B 1 163 ? 150.431 145.790 148.341 1.00 60.65 ?  163 ARG B CA    1 
ATOM   6900  C  C     . ARG B 1 163 ? 149.128 145.245 148.926 1.00 62.84 ?  163 ARG B C     1 
ATOM   6901  O  O     . ARG B 1 163 ? 149.004 144.075 149.285 1.00 61.14 ?  163 ARG B O     1 
ATOM   6902  C  CB    . ARG B 1 163 ? 151.418 144.669 148.037 1.00 61.32 ?  163 ARG B CB    1 
ATOM   6903  C  CG    . ARG B 1 163 ? 152.501 145.049 147.043 1.00 62.25 ?  163 ARG B CG    1 
ATOM   6904  C  CD    . ARG B 1 163 ? 153.656 144.068 147.093 1.00 61.92 ?  163 ARG B CD    1 
ATOM   6905  N  NE    . ARG B 1 163 ? 154.538 144.322 148.226 1.00 64.82 ?  163 ARG B NE    1 
ATOM   6906  C  CZ    . ARG B 1 163 ? 155.285 143.398 148.814 1.00 66.36 ?  163 ARG B CZ    1 
ATOM   6907  N  NH1   . ARG B 1 163 ? 155.279 142.140 148.403 1.00 63.10 1  163 ARG B NH1   1 
ATOM   6908  N  NH2   . ARG B 1 163 ? 156.057 143.744 149.841 1.00 62.68 ?  163 ARG B NH2   1 
ATOM   6909  N  N     . ARG B 1 164 ? 148.145 146.133 149.013 1.00 56.69 ?  164 ARG B N     1 
ATOM   6910  C  CA    . ARG B 1 164 ? 146.874 145.841 149.654 1.00 53.92 ?  164 ARG B CA    1 
ATOM   6911  C  C     . ARG B 1 164 ? 145.744 145.849 148.636 1.00 53.28 ?  164 ARG B C     1 
ATOM   6912  O  O     . ARG B 1 164 ? 145.823 146.506 147.595 1.00 52.80 ?  164 ARG B O     1 
ATOM   6913  C  CB    . ARG B 1 164 ? 146.570 146.860 150.758 1.00 52.22 ?  164 ARG B CB    1 
ATOM   6914  C  CG    . ARG B 1 164 ? 146.096 148.212 150.237 1.00 51.00 ?  164 ARG B CG    1 
ATOM   6915  C  CD    . ARG B 1 164 ? 145.592 149.099 151.363 1.00 53.16 ?  164 ARG B CD    1 
ATOM   6916  N  NE    . ARG B 1 164 ? 145.340 150.468 150.930 1.00 53.94 ?  164 ARG B NE    1 
ATOM   6917  C  CZ    . ARG B 1 164 ? 144.265 150.856 150.256 1.00 56.41 ?  164 ARG B CZ    1 
ATOM   6918  N  NH1   . ARG B 1 164 ? 143.316 149.999 149.916 1.00 51.21 1  164 ARG B NH1   1 
ATOM   6919  N  NH2   . ARG B 1 164 ? 144.139 152.135 149.918 1.00 56.21 ?  164 ARG B NH2   1 
ATOM   6920  N  N     . GLY B 1 165 ? 144.694 145.093 148.944 1.00 50.68 ?  165 GLY B N     1 
ATOM   6921  C  CA    . GLY B 1 165 ? 143.437 145.232 148.248 1.00 47.35 ?  165 GLY B CA    1 
ATOM   6922  C  C     . GLY B 1 165 ? 142.647 146.403 148.791 1.00 51.38 ?  165 GLY B C     1 
ATOM   6923  O  O     . GLY B 1 165 ? 143.099 147.158 149.651 1.00 52.32 ?  165 GLY B O     1 
ATOM   6924  N  N     . GLU B 1 166 ? 141.436 146.557 148.271 1.00 48.09 ?  166 GLU B N     1 
ATOM   6925  C  CA    . GLU B 1 166 ? 140.567 147.619 148.751 1.00 42.72 ?  166 GLU B CA    1 
ATOM   6926  C  C     . GLU B 1 166 ? 140.118 147.334 150.180 1.00 42.86 ?  166 GLU B C     1 
ATOM   6927  O  O     . GLU B 1 166 ? 140.039 146.182 150.614 1.00 39.32 ?  166 GLU B O     1 
ATOM   6928  C  CB    . GLU B 1 166 ? 139.354 147.774 147.834 1.00 41.35 ?  166 GLU B CB    1 
ATOM   6929  C  CG    . GLU B 1 166 ? 138.968 149.219 147.556 1.00 45.08 ?  166 GLU B CG    1 
ATOM   6930  C  CD    . GLU B 1 166 ? 140.042 149.981 146.799 1.00 49.94 ?  166 GLU B CD    1 
ATOM   6931  O  OE1   . GLU B 1 166 ? 140.836 149.342 146.079 1.00 49.58 ?  166 GLU B OE1   1 
ATOM   6932  O  OE2   . GLU B 1 166 ? 140.092 151.222 146.926 1.00 48.28 -1 166 GLU B OE2   1 
ATOM   6933  N  N     . LEU B 1 167 ? 139.830 148.405 150.918 1.00 38.04 ?  167 LEU B N     1 
ATOM   6934  C  CA    . LEU B 1 167 ? 139.320 148.271 152.276 1.00 32.21 ?  167 LEU B CA    1 
ATOM   6935  C  C     . LEU B 1 167 ? 137.834 147.945 152.313 1.00 35.31 ?  167 LEU B C     1 
ATOM   6936  O  O     . LEU B 1 167 ? 137.305 147.656 153.390 1.00 38.65 ?  167 LEU B O     1 
ATOM   6937  C  CB    . LEU B 1 167 ? 139.591 149.553 153.067 1.00 33.90 ?  167 LEU B CB    1 
ATOM   6938  C  CG    . LEU B 1 167 ? 140.829 149.580 153.967 1.00 34.71 ?  167 LEU B CG    1 
ATOM   6939  C  CD1   . LEU B 1 167 ? 142.030 148.959 153.277 1.00 31.87 ?  167 LEU B CD1   1 
ATOM   6940  C  CD2   . LEU B 1 167 ? 141.137 151.001 154.389 1.00 32.27 ?  167 LEU B CD2   1 
ATOM   6941  N  N     . VAL B 1 168 ? 137.159 147.985 151.168 1.00 36.93 ?  168 VAL B N     1 
ATOM   6942  C  CA    . VAL B 1 168 ? 135.755 147.616 151.047 1.00 28.61 ?  168 VAL B CA    1 
ATOM   6943  C  C     . VAL B 1 168 ? 135.679 146.321 150.251 1.00 33.31 ?  168 VAL B C     1 
ATOM   6944  O  O     . VAL B 1 168 ? 136.392 146.153 149.257 1.00 39.76 ?  168 VAL B O     1 
ATOM   6945  C  CB    . VAL B 1 168 ? 134.936 148.731 150.367 1.00 27.73 ?  168 VAL B CB    1 
ATOM   6946  C  CG1   . VAL B 1 168 ? 133.464 148.358 150.304 1.00 34.50 ?  168 VAL B CG1   1 
ATOM   6947  C  CG2   . VAL B 1 168 ? 135.125 150.046 151.097 1.00 31.65 ?  168 VAL B CG2   1 
ATOM   6948  N  N     . SER B 1 169 ? 134.823 145.400 150.696 1.00 29.47 ?  169 SER B N     1 
ATOM   6949  C  CA    . SER B 1 169 ? 134.661 144.128 150.011 1.00 29.73 ?  169 SER B CA    1 
ATOM   6950  C  C     . SER B 1 169 ? 133.225 143.806 149.627 1.00 31.28 ?  169 SER B C     1 
ATOM   6951  O  O     . SER B 1 169 ? 132.991 142.757 149.020 1.00 40.22 ?  169 SER B O     1 
ATOM   6952  C  CB    . SER B 1 169 ? 135.218 142.979 150.864 1.00 36.48 ?  169 SER B CB    1 
ATOM   6953  O  OG    . SER B 1 169 ? 136.606 142.808 150.636 1.00 43.76 ?  169 SER B OG    1 
ATOM   6954  N  N     . CYS B 1 170 ? 132.261 144.657 149.962 1.00 25.02 ?  170 CYS B N     1 
ATOM   6955  C  CA    . CYS B 1 170 ? 130.876 144.455 149.562 1.00 23.57 ?  170 CYS B CA    1 
ATOM   6956  C  C     . CYS B 1 170 ? 130.476 145.573 148.614 1.00 23.82 ?  170 CYS B C     1 
ATOM   6957  O  O     . CYS B 1 170 ? 130.579 146.755 148.960 1.00 31.72 ?  170 CYS B O     1 
ATOM   6958  C  CB    . CYS B 1 170 ? 129.942 144.399 150.775 1.00 34.88 ?  170 CYS B CB    1 
ATOM   6959  S  SG    . CYS B 1 170 ? 130.030 145.806 151.903 1.00 46.19 ?  170 CYS B SG    1 
ATOM   6960  N  N     . PHE B 1 171 ? 130.033 145.200 147.417 1.00 25.86 ?  171 PHE B N     1 
ATOM   6961  C  CA    . PHE B 1 171 ? 129.580 146.144 146.409 1.00 11.61 ?  171 PHE B CA    1 
ATOM   6962  C  C     . PHE B 1 171 ? 128.248 145.674 145.854 1.00 16.26 ?  171 PHE B C     1 
ATOM   6963  O  O     . PHE B 1 171 ? 128.009 144.470 145.724 1.00 24.49 ?  171 PHE B O     1 
ATOM   6964  C  CB    . PHE B 1 171 ? 130.603 146.291 145.277 1.00 17.72 ?  171 PHE B CB    1 
ATOM   6965  C  CG    . PHE B 1 171 ? 131.988 146.599 145.757 1.00 17.83 ?  171 PHE B CG    1 
ATOM   6966  C  CD1   . PHE B 1 171 ? 132.345 147.892 146.087 1.00 19.98 ?  171 PHE B CD1   1 
ATOM   6967  C  CD2   . PHE B 1 171 ? 132.932 145.597 145.876 1.00 19.73 ?  171 PHE B CD2   1 
ATOM   6968  C  CE1   . PHE B 1 171 ? 133.615 148.178 146.534 1.00 13.29 ?  171 PHE B CE1   1 
ATOM   6969  C  CE2   . PHE B 1 171 ? 134.203 145.880 146.322 1.00 17.80 ?  171 PHE B CE2   1 
ATOM   6970  C  CZ    . PHE B 1 171 ? 134.545 147.173 146.649 1.00 10.83 ?  171 PHE B CZ    1 
ATOM   6971  N  N     . LEU B 1 172 ? 127.380 146.629 145.535 1.00 14.93 ?  172 LEU B N     1 
ATOM   6972  C  CA    . LEU B 1 172 ? 126.052 146.345 145.006 1.00 7.54  ?  172 LEU B CA    1 
ATOM   6973  C  C     . LEU B 1 172 ? 125.866 147.154 143.736 1.00 13.54 ?  172 LEU B C     1 
ATOM   6974  O  O     . LEU B 1 172 ? 125.860 148.388 143.782 1.00 21.70 ?  172 LEU B O     1 
ATOM   6975  C  CB    . LEU B 1 172 ? 124.960 146.684 146.023 1.00 8.45  ?  172 LEU B CB    1 
ATOM   6976  C  CG    . LEU B 1 172 ? 124.849 145.853 147.300 1.00 2.85  ?  172 LEU B CG    1 
ATOM   6977  C  CD1   . LEU B 1 172 ? 125.883 146.277 148.327 1.00 11.18 ?  172 LEU B CD1   1 
ATOM   6978  C  CD2   . LEU B 1 172 ? 123.456 145.993 147.867 1.00 16.09 ?  172 LEU B CD2   1 
ATOM   6979  N  N     . LEU B 1 173 ? 125.699 146.467 142.613 1.00 20.16 ?  173 LEU B N     1 
ATOM   6980  C  CA    . LEU B 1 173 ? 125.587 147.104 141.310 1.00 8.80  ?  173 LEU B CA    1 
ATOM   6981  C  C     . LEU B 1 173 ? 124.181 146.942 140.754 1.00 18.02 ?  173 LEU B C     1 
ATOM   6982  O  O     . LEU B 1 173 ? 123.597 145.857 140.819 1.00 29.94 ?  173 LEU B O     1 
ATOM   6983  C  CB    . LEU B 1 173 ? 126.593 146.513 140.320 1.00 13.72 ?  173 LEU B CB    1 
ATOM   6984  C  CG    . LEU B 1 173 ? 128.049 146.388 140.760 1.00 19.57 ?  173 LEU B CG    1 
ATOM   6985  C  CD1   . LEU B 1 173 ? 128.880 145.881 139.598 1.00 22.40 ?  173 LEU B CD1   1 
ATOM   6986  C  CD2   . LEU B 1 173 ? 128.580 147.716 141.264 1.00 25.38 ?  173 LEU B CD2   1 
ATOM   6987  N  N     . GLU B 1 174 ? 123.643 148.029 140.216 1.00 26.42 ?  174 GLU B N     1 
ATOM   6988  C  CA    . GLU B 1 174 ? 122.428 147.976 139.418 1.00 22.09 ?  174 GLU B CA    1 
ATOM   6989  C  C     . GLU B 1 174 ? 122.800 147.749 137.960 1.00 20.40 ?  174 GLU B C     1 
ATOM   6990  O  O     . GLU B 1 174 ? 123.721 148.382 137.439 1.00 31.33 ?  174 GLU B O     1 
ATOM   6991  C  CB    . GLU B 1 174 ? 121.630 149.273 139.554 1.00 26.22 ?  174 GLU B CB    1 
ATOM   6992  C  CG    . GLU B 1 174 ? 121.052 149.525 140.928 1.00 22.93 ?  174 GLU B CG    1 
ATOM   6993  C  CD    . GLU B 1 174 ? 119.559 149.289 140.976 1.00 27.60 ?  174 GLU B CD    1 
ATOM   6994  O  OE1   . GLU B 1 174 ? 119.000 148.815 139.966 1.00 31.09 ?  174 GLU B OE1   1 
ATOM   6995  O  OE2   . GLU B 1 174 ? 118.944 149.582 142.020 1.00 26.84 -1 174 GLU B OE2   1 
ATOM   6996  N  N     . VAL B 1 175 ? 122.083 146.843 137.305 1.00 17.81 ?  175 VAL B N     1 
ATOM   6997  C  CA    . VAL B 1 175 ? 122.310 146.527 135.900 1.00 17.01 ?  175 VAL B CA    1 
ATOM   6998  C  C     . VAL B 1 175 ? 121.099 147.001 135.111 1.00 21.62 ?  175 VAL B C     1 
ATOM   6999  O  O     . VAL B 1 175 ? 119.969 146.574 135.378 1.00 24.85 ?  175 VAL B O     1 
ATOM   7000  C  CB    . VAL B 1 175 ? 122.559 145.026 135.688 1.00 18.44 ?  175 VAL B CB    1 
ATOM   7001  C  CG1   . VAL B 1 175 ? 123.070 144.768 134.281 1.00 7.81  ?  175 VAL B CG1   1 
ATOM   7002  C  CG2   . VAL B 1 175 ? 123.538 144.498 136.725 1.00 18.22 ?  175 VAL B CG2   1 
ATOM   7003  N  N     . ASN B 1 176 ? 121.332 147.880 134.146 1.00 17.07 ?  176 ASN B N     1 
ATOM   7004  C  CA    . ASN B 1 176 ? 120.269 148.395 133.299 1.00 18.01 ?  176 ASN B CA    1 
ATOM   7005  C  C     . ASN B 1 176 ? 120.010 147.451 132.130 1.00 22.69 ?  176 ASN B C     1 
ATOM   7006  O  O     . ASN B 1 176 ? 120.859 146.641 131.751 1.00 27.73 ?  176 ASN B O     1 
ATOM   7007  C  CB    . ASN B 1 176 ? 120.617 149.791 132.785 1.00 19.42 ?  176 ASN B CB    1 
ATOM   7008  C  CG    . ASN B 1 176 ? 119.421 150.711 132.738 1.00 17.10 ?  176 ASN B CG    1 
ATOM   7009  O  OD1   . ASN B 1 176 ? 118.278 150.261 132.710 1.00 26.13 ?  176 ASN B OD1   1 
ATOM   7010  N  ND2   . ASN B 1 176 ? 119.679 152.011 132.730 1.00 18.44 ?  176 ASN B ND2   1 
ATOM   7011  N  N     . ASP B 1 177 ? 118.816 147.572 131.553 1.00 27.31 ?  177 ASP B N     1 
ATOM   7012  C  CA    . ASP B 1 177 ? 118.361 146.672 130.495 1.00 23.71 ?  177 ASP B CA    1 
ATOM   7013  C  C     . ASP B 1 177 ? 118.920 147.149 129.156 1.00 24.80 ?  177 ASP B C     1 
ATOM   7014  O  O     . ASP B 1 177 ? 118.238 147.776 128.342 1.00 31.45 ?  177 ASP B O     1 
ATOM   7015  C  CB    . ASP B 1 177 ? 116.842 146.600 130.481 1.00 20.34 ?  177 ASP B CB    1 
ATOM   7016  C  CG    . ASP B 1 177 ? 116.322 145.456 129.646 1.00 26.79 ?  177 ASP B CG    1 
ATOM   7017  O  OD1   . ASP B 1 177 ? 116.976 144.392 129.623 1.00 34.35 ?  177 ASP B OD1   1 
ATOM   7018  O  OD2   . ASP B 1 177 ? 115.256 145.619 129.019 1.00 33.24 -1 177 ASP B OD2   1 
ATOM   7019  N  N     . SER B 1 178 ? 120.191 146.829 128.928 1.00 19.77 ?  178 SER B N     1 
ATOM   7020  C  CA    . SER B 1 178 ? 120.877 147.184 127.693 1.00 17.17 ?  178 SER B CA    1 
ATOM   7021  C  C     . SER B 1 178 ? 122.174 146.394 127.621 1.00 21.75 ?  178 SER B C     1 
ATOM   7022  O  O     . SER B 1 178 ? 122.738 146.005 128.646 1.00 34.49 ?  178 SER B O     1 
ATOM   7023  C  CB    . SER B 1 178 ? 121.155 148.688 127.612 1.00 14.65 ?  178 SER B CB    1 
ATOM   7024  O  OG    . SER B 1 178 ? 122.399 149.011 128.201 1.00 27.93 ?  178 SER B OG    1 
ATOM   7025  N  N     . LEU B 1 179 ? 122.637 146.155 126.391 1.00 32.35 ?  179 LEU B N     1 
ATOM   7026  C  CA    . LEU B 1 179 ? 123.894 145.438 126.205 1.00 19.98 ?  179 LEU B CA    1 
ATOM   7027  C  C     . LEU B 1 179 ? 125.076 146.262 126.692 1.00 17.04 ?  179 LEU B C     1 
ATOM   7028  O  O     . LEU B 1 179 ? 126.034 145.714 127.248 1.00 26.29 ?  179 LEU B O     1 
ATOM   7029  C  CB    . LEU B 1 179 ? 124.075 145.058 124.735 1.00 23.05 ?  179 LEU B CB    1 
ATOM   7030  C  CG    . LEU B 1 179 ? 125.275 144.158 124.431 1.00 23.10 ?  179 LEU B CG    1 
ATOM   7031  C  CD1   . LEU B 1 179 ? 125.062 142.771 125.012 1.00 20.90 ?  179 LEU B CD1   1 
ATOM   7032  C  CD2   . LEU B 1 179 ? 125.529 144.083 122.937 1.00 21.71 ?  179 LEU B CD2   1 
ATOM   7033  N  N     . ASN B 1 180 ? 125.032 147.580 126.486 1.00 19.32 ?  180 ASN B N     1 
ATOM   7034  C  CA    . ASN B 1 180 ? 126.081 148.451 127.004 1.00 14.81 ?  180 ASN B CA    1 
ATOM   7035  C  C     . ASN B 1 180 ? 126.175 148.340 128.519 1.00 22.05 ?  180 ASN B C     1 
ATOM   7036  O  O     . ASN B 1 180 ? 127.267 148.183 129.081 1.00 30.45 ?  180 ASN B O     1 
ATOM   7037  C  CB    . ASN B 1 180 ? 125.806 149.899 126.593 1.00 23.77 ?  180 ASN B CB    1 
ATOM   7038  C  CG    . ASN B 1 180 ? 126.272 150.208 125.188 1.00 29.53 ?  180 ASN B CG    1 
ATOM   7039  O  OD1   . ASN B 1 180 ? 127.106 149.500 124.628 1.00 34.41 ?  180 ASN B OD1   1 
ATOM   7040  N  ND2   . ASN B 1 180 ? 125.733 151.273 124.609 1.00 27.63 ?  180 ASN B ND2   1 
ATOM   7041  N  N     . ASP B 1 181 ? 125.028 148.396 129.196 1.00 24.53 ?  181 ASP B N     1 
ATOM   7042  C  CA    . ASP B 1 181 ? 125.013 148.322 130.650 1.00 15.71 ?  181 ASP B CA    1 
ATOM   7043  C  C     . ASP B 1 181 ? 125.391 146.934 131.150 1.00 20.15 ?  181 ASP B C     1 
ATOM   7044  O  O     . ASP B 1 181 ? 126.041 146.815 132.189 1.00 30.36 ?  181 ASP B O     1 
ATOM   7045  C  CB    . ASP B 1 181 ? 123.640 148.729 131.172 1.00 27.99 ?  181 ASP B CB    1 
ATOM   7046  C  CG    . ASP B 1 181 ? 123.353 150.203 130.957 1.00 31.71 ?  181 ASP B CG    1 
ATOM   7047  O  OD1   . ASP B 1 181 ? 123.964 151.037 131.655 1.00 32.18 ?  181 ASP B OD1   1 
ATOM   7048  O  OD2   . ASP B 1 181 ? 122.514 150.529 130.091 1.00 26.06 -1 181 ASP B OD2   1 
ATOM   7049  N  N     . ILE B 1 182 ? 125.008 145.879 130.429 1.00 21.62 ?  182 ILE B N     1 
ATOM   7050  C  CA    . ILE B 1 182 ? 125.386 144.528 130.834 1.00 21.44 ?  182 ILE B CA    1 
ATOM   7051  C  C     . ILE B 1 182 ? 126.892 144.325 130.697 1.00 19.32 ?  182 ILE B C     1 
ATOM   7052  O  O     . ILE B 1 182 ? 127.540 143.746 131.579 1.00 22.73 ?  182 ILE B O     1 
ATOM   7053  C  CB    . ILE B 1 182 ? 124.589 143.490 130.024 1.00 19.85 ?  182 ILE B CB    1 
ATOM   7054  C  CG1   . ILE B 1 182 ? 123.161 143.393 130.561 1.00 20.49 ?  182 ILE B CG1   1 
ATOM   7055  C  CG2   . ILE B 1 182 ? 125.264 142.132 130.064 1.00 22.79 ?  182 ILE B CG2   1 
ATOM   7056  C  CD1   . ILE B 1 182 ? 122.209 142.698 129.630 1.00 23.22 ?  182 ILE B CD1   1 
ATOM   7057  N  N     . SER B 1 183 ? 127.474 144.798 129.593 1.00 26.18 ?  183 SER B N     1 
ATOM   7058  C  CA    . SER B 1 183 ? 128.920 144.703 129.423 1.00 16.94 ?  183 SER B CA    1 
ATOM   7059  C  C     . SER B 1 183 ? 129.651 145.518 130.479 1.00 19.44 ?  183 SER B C     1 
ATOM   7060  O  O     . SER B 1 183 ? 130.669 145.072 131.025 1.00 27.79 ?  183 SER B O     1 
ATOM   7061  C  CB    . SER B 1 183 ? 129.312 145.163 128.022 1.00 17.25 ?  183 SER B CB    1 
ATOM   7062  O  OG    . SER B 1 183 ? 128.795 146.450 127.748 1.00 33.98 ?  183 SER B OG    1 
ATOM   7063  N  N     . ARG B 1 184 ? 129.147 146.716 130.786 1.00 25.39 ?  184 ARG B N     1 
ATOM   7064  C  CA    . ARG B 1 184 ? 129.759 147.519 131.836 1.00 17.87 ?  184 ARG B CA    1 
ATOM   7065  C  C     . ARG B 1 184 ? 129.631 146.841 133.194 1.00 26.39 ?  184 ARG B C     1 
ATOM   7066  O  O     . ARG B 1 184 ? 130.543 146.923 134.021 1.00 31.50 ?  184 ARG B O     1 
ATOM   7067  C  CB    . ARG B 1 184 ? 129.131 148.910 131.869 1.00 16.95 ?  184 ARG B CB    1 
ATOM   7068  C  CG    . ARG B 1 184 ? 129.828 149.867 132.816 1.00 27.61 ?  184 ARG B CG    1 
ATOM   7069  C  CD    . ARG B 1 184 ? 131.327 149.862 132.610 1.00 26.09 ?  184 ARG B CD    1 
ATOM   7070  N  NE    . ARG B 1 184 ? 131.733 150.823 131.593 1.00 34.37 ?  184 ARG B NE    1 
ATOM   7071  C  CZ    . ARG B 1 184 ? 132.905 150.808 130.974 1.00 34.93 ?  184 ARG B CZ    1 
ATOM   7072  N  NH1   . ARG B 1 184 ? 133.816 149.888 131.241 1.00 25.59 1  184 ARG B NH1   1 
ATOM   7073  N  NH2   . ARG B 1 184 ? 133.170 151.744 130.066 1.00 32.42 ?  184 ARG B NH2   1 
ATOM   7074  N  N     . ALA B 1 185 ? 128.502 146.177 133.448 1.00 31.15 ?  185 ALA B N     1 
ATOM   7075  C  CA    . ALA B 1 185 ? 128.332 145.445 134.697 1.00 8.29  ?  185 ALA B CA    1 
ATOM   7076  C  C     . ALA B 1 185 ? 129.330 144.305 134.804 1.00 12.71 ?  185 ALA B C     1 
ATOM   7077  O  O     . ALA B 1 185 ? 129.905 144.076 135.872 1.00 22.32 ?  185 ALA B O     1 
ATOM   7078  C  CB    . ALA B 1 185 ? 126.903 144.917 134.807 1.00 9.14  ?  185 ALA B CB    1 
ATOM   7079  N  N     . ILE B 1 186 ? 129.552 143.579 133.708 1.00 22.82 ?  186 ILE B N     1 
ATOM   7080  C  CA    . ILE B 1 186 ? 130.551 142.510 133.715 1.00 23.20 ?  186 ILE B CA    1 
ATOM   7081  C  C     . ILE B 1 186 ? 131.938 143.084 133.979 1.00 17.77 ?  186 ILE B C     1 
ATOM   7082  O  O     . ILE B 1 186 ? 132.711 142.544 134.783 1.00 26.42 ?  186 ILE B O     1 
ATOM   7083  C  CB    . ILE B 1 186 ? 130.502 141.725 132.390 1.00 27.87 ?  186 ILE B CB    1 
ATOM   7084  C  CG1   . ILE B 1 186 ? 129.317 140.759 132.387 1.00 21.95 ?  186 ILE B CG1   1 
ATOM   7085  C  CG2   . ILE B 1 186 ? 131.800 140.966 132.158 1.00 23.79 ?  186 ILE B CG2   1 
ATOM   7086  C  CD1   . ILE B 1 186 ? 128.667 140.608 131.036 1.00 27.46 ?  186 ILE B CD1   1 
ATOM   7087  N  N     . ASP B 1 187 ? 132.267 144.195 133.318 1.00 23.35 ?  187 ASP B N     1 
ATOM   7088  C  CA    . ASP B 1 187 ? 133.567 144.827 133.515 1.00 18.17 ?  187 ASP B CA    1 
ATOM   7089  C  C     . ASP B 1 187 ? 133.757 145.264 134.963 1.00 28.09 ?  187 ASP B C     1 
ATOM   7090  O  O     . ASP B 1 187 ? 134.798 144.996 135.572 1.00 34.35 ?  187 ASP B O     1 
ATOM   7091  C  CB    . ASP B 1 187 ? 133.713 146.019 132.571 1.00 17.20 ?  187 ASP B CB    1 
ATOM   7092  C  CG    . ASP B 1 187 ? 134.791 146.987 133.015 1.00 35.28 ?  187 ASP B CG    1 
ATOM   7093  O  OD1   . ASP B 1 187 ? 135.946 146.554 133.204 1.00 34.32 ?  187 ASP B OD1   1 
ATOM   7094  O  OD2   . ASP B 1 187 ? 134.481 148.186 133.182 1.00 41.83 -1 187 ASP B OD2   1 
ATOM   7095  N  N     . ILE B 1 188 ? 132.756 145.937 135.530 1.00 23.60 ?  188 ILE B N     1 
ATOM   7096  C  CA    . ILE B 1 188 ? 132.867 146.442 136.893 1.00 22.56 ?  188 ILE B CA    1 
ATOM   7097  C  C     . ILE B 1 188 ? 132.909 145.292 137.890 1.00 25.27 ?  188 ILE B C     1 
ATOM   7098  O  O     . ILE B 1 188 ? 133.620 145.353 138.897 1.00 27.77 ?  188 ILE B O     1 
ATOM   7099  C  CB    . ILE B 1 188 ? 131.718 147.420 137.196 1.00 26.73 ?  188 ILE B CB    1 
ATOM   7100  C  CG1   . ILE B 1 188 ? 131.830 148.666 136.321 1.00 25.52 ?  188 ILE B CG1   1 
ATOM   7101  C  CG2   . ILE B 1 188 ? 131.736 147.837 138.649 1.00 26.77 ?  188 ILE B CG2   1 
ATOM   7102  C  CD1   . ILE B 1 188 ? 130.656 149.601 136.461 1.00 21.59 ?  188 ILE B CD1   1 
ATOM   7103  N  N     . SER B 1 189 ? 132.149 144.227 137.630 1.00 19.85 ?  189 SER B N     1 
ATOM   7104  C  CA    . SER B 1 189 ? 132.200 143.055 138.494 1.00 13.40 ?  189 SER B CA    1 
ATOM   7105  C  C     . SER B 1 189 ? 133.589 142.438 138.494 1.00 20.94 ?  189 SER B C     1 
ATOM   7106  O  O     . SER B 1 189 ? 134.111 142.076 139.553 1.00 25.83 ?  189 SER B O     1 
ATOM   7107  C  CB    . SER B 1 189 ? 131.157 142.031 138.048 1.00 20.14 ?  189 SER B CB    1 
ATOM   7108  O  OG    . SER B 1 189 ? 129.863 142.602 138.033 1.00 29.91 ?  189 SER B OG    1 
ATOM   7109  N  N     . MET B 1 190 ? 134.209 142.316 137.318 1.00 30.19 ?  190 MET B N     1 
ATOM   7110  C  CA    . MET B 1 190 ? 135.566 141.779 137.265 1.00 22.37 ?  190 MET B CA    1 
ATOM   7111  C  C     . MET B 1 190 ? 136.560 142.710 137.950 1.00 16.93 ?  190 MET B C     1 
ATOM   7112  O  O     . MET B 1 190 ? 137.478 142.247 138.632 1.00 21.26 ?  190 MET B O     1 
ATOM   7113  C  CB    . MET B 1 190 ? 135.981 141.514 135.820 1.00 21.58 ?  190 MET B CB    1 
ATOM   7114  C  CG    . MET B 1 190 ? 135.184 140.413 135.154 1.00 27.32 ?  190 MET B CG    1 
ATOM   7115  S  SD    . MET B 1 190 ? 136.037 139.642 133.768 1.00 35.79 ?  190 MET B SD    1 
ATOM   7116  C  CE    . MET B 1 190 ? 136.033 140.987 132.590 1.00 25.79 ?  190 MET B CE    1 
ATOM   7117  N  N     . GLN B 1 191 ? 136.391 144.023 137.786 1.00 21.42 ?  191 GLN B N     1 
ATOM   7118  C  CA    . GLN B 1 191 ? 137.305 144.968 138.423 1.00 23.07 ?  191 GLN B CA    1 
ATOM   7119  C  C     . GLN B 1 191 ? 137.189 144.924 139.942 1.00 25.57 ?  191 GLN B C     1 
ATOM   7120  O  O     . GLN B 1 191 ? 138.199 145.016 140.649 1.00 32.40 ?  191 GLN B O     1 
ATOM   7121  C  CB    . GLN B 1 191 ? 137.049 146.386 137.909 1.00 24.32 ?  191 GLN B CB    1 
ATOM   7122  C  CG    . GLN B 1 191 ? 137.299 146.569 136.424 1.00 23.68 ?  191 GLN B CG    1 
ATOM   7123  C  CD    . GLN B 1 191 ? 138.771 146.577 136.067 1.00 27.63 ?  191 GLN B CD    1 
ATOM   7124  O  OE1   . GLN B 1 191 ? 139.638 146.578 136.939 1.00 30.80 ?  191 GLN B OE1   1 
ATOM   7125  N  NE2   . GLN B 1 191 ? 139.060 146.579 134.773 1.00 28.81 ?  191 GLN B NE2   1 
ATOM   7126  N  N     . LEU B 1 192 ? 135.968 144.796 140.463 1.00 24.98 ?  192 LEU B N     1 
ATOM   7127  C  CA    . LEU B 1 192 ? 135.777 144.768 141.908 1.00 16.38 ?  192 LEU B CA    1 
ATOM   7128  C  C     . LEU B 1 192 ? 136.176 143.423 142.502 1.00 23.84 ?  192 LEU B C     1 
ATOM   7129  O  O     . LEU B 1 192 ? 136.726 143.371 143.606 1.00 36.16 ?  192 LEU B O     1 
ATOM   7130  C  CB    . LEU B 1 192 ? 134.327 145.100 142.254 1.00 18.21 ?  192 LEU B CB    1 
ATOM   7131  C  CG    . LEU B 1 192 ? 133.871 146.521 141.918 1.00 19.83 ?  192 LEU B CG    1 
ATOM   7132  C  CD1   . LEU B 1 192 ? 132.364 146.641 142.041 1.00 19.10 ?  192 LEU B CD1   1 
ATOM   7133  C  CD2   . LEU B 1 192 ? 134.569 147.537 142.805 1.00 17.33 ?  192 LEU B CD2   1 
ATOM   7134  N  N     . SER B 1 193 ? 135.905 142.326 141.791 1.00 27.70 ?  193 SER B N     1 
ATOM   7135  C  CA    . SER B 1 193 ? 136.381 141.022 142.234 1.00 20.19 ?  193 SER B CA    1 
ATOM   7136  C  C     . SER B 1 193 ? 137.899 140.951 142.195 1.00 28.24 ?  193 SER B C     1 
ATOM   7137  O  O     . SER B 1 193 ? 138.508 140.258 143.014 1.00 36.87 ?  193 SER B O     1 
ATOM   7138  C  CB    . SER B 1 193 ? 135.768 139.923 141.367 1.00 25.64 ?  193 SER B CB    1 
ATOM   7139  O  OG    . SER B 1 193 ? 136.067 138.640 141.885 1.00 42.27 ?  193 SER B OG    1 
ATOM   7140  N  N     . LYS B 1 194 ? 138.522 141.660 141.253 1.00 34.56 ?  194 LYS B N     1 
ATOM   7141  C  CA    . LYS B 1 194 ? 139.977 141.760 141.228 1.00 32.01 ?  194 LYS B CA    1 
ATOM   7142  C  C     . LYS B 1 194 ? 140.501 142.405 142.504 1.00 35.73 ?  194 LYS B C     1 
ATOM   7143  O  O     . LYS B 1 194 ? 141.515 141.969 143.060 1.00 43.69 ?  194 LYS B O     1 
ATOM   7144  C  CB    . LYS B 1 194 ? 140.414 142.552 139.995 1.00 27.19 ?  194 LYS B CB    1 
ATOM   7145  C  CG    . LYS B 1 194 ? 141.820 143.103 140.062 1.00 36.44 ?  194 LYS B CG    1 
ATOM   7146  C  CD    . LYS B 1 194 ? 142.060 144.125 138.966 1.00 38.23 ?  194 LYS B CD    1 
ATOM   7147  C  CE    . LYS B 1 194 ? 143.546 144.357 138.745 1.00 36.81 ?  194 LYS B CE    1 
ATOM   7148  N  NZ    . LYS B 1 194 ? 143.795 145.361 137.676 1.00 37.91 1  194 LYS B NZ    1 
ATOM   7149  N  N     . LEU B 1 195 ? 139.813 143.439 142.990 1.00 34.15 ?  195 LEU B N     1 
ATOM   7150  C  CA    . LEU B 1 195 ? 140.173 144.073 144.252 1.00 35.73 ?  195 LEU B CA    1 
ATOM   7151  C  C     . LEU B 1 195 ? 139.897 143.187 145.458 1.00 35.64 ?  195 LEU B C     1 
ATOM   7152  O  O     . LEU B 1 195 ? 140.316 143.533 146.567 1.00 42.62 ?  195 LEU B O     1 
ATOM   7153  C  CB    . LEU B 1 195 ? 139.420 145.396 144.406 1.00 38.37 ?  195 LEU B CB    1 
ATOM   7154  C  CG    . LEU B 1 195 ? 139.663 146.435 143.313 1.00 37.71 ?  195 LEU B CG    1 
ATOM   7155  C  CD1   . LEU B 1 195 ? 138.871 147.703 143.594 1.00 32.38 ?  195 LEU B CD1   1 
ATOM   7156  C  CD2   . LEU B 1 195 ? 141.145 146.736 143.181 1.00 34.65 ?  195 LEU B CD2   1 
ATOM   7157  N  N     . GLY B 1 196 ? 139.204 142.068 145.274 1.00 31.06 ?  196 GLY B N     1 
ATOM   7158  C  CA    . GLY B 1 196 ? 138.904 141.161 146.357 1.00 30.00 ?  196 GLY B CA    1 
ATOM   7159  C  C     . GLY B 1 196 ? 137.542 141.328 146.986 1.00 36.77 ?  196 GLY B C     1 
ATOM   7160  O  O     . GLY B 1 196 ? 137.283 140.716 148.027 1.00 39.00 ?  196 GLY B O     1 
ATOM   7161  N  N     . GLY B 1 197 ? 136.664 142.129 146.392 1.00 30.42 ?  197 GLY B N     1 
ATOM   7162  C  CA    . GLY B 1 197 ? 135.365 142.419 146.970 1.00 25.49 ?  197 GLY B CA    1 
ATOM   7163  C  C     . GLY B 1 197 ? 134.259 141.571 146.366 1.00 27.37 ?  197 GLY B C     1 
ATOM   7164  O  O     . GLY B 1 197 ? 134.265 141.281 145.169 1.00 31.59 ?  197 GLY B O     1 
ATOM   7165  N  N     . GLY B 1 198 ? 133.312 141.178 147.213 1.00 25.08 ?  198 GLY B N     1 
ATOM   7166  C  CA    . GLY B 1 198 ? 132.120 140.513 146.722 1.00 14.95 ?  198 GLY B CA    1 
ATOM   7167  C  C     . GLY B 1 198 ? 131.184 141.506 146.058 1.00 14.13 ?  198 GLY B C     1 
ATOM   7168  O  O     . GLY B 1 198 ? 130.976 142.617 146.543 1.00 24.21 ?  198 GLY B O     1 
ATOM   7169  N  N     . VAL B 1 199 ? 130.617 141.097 144.928 1.00 22.61 ?  199 VAL B N     1 
ATOM   7170  C  CA    . VAL B 1 199 ? 129.812 141.973 144.087 1.00 17.88 ?  199 VAL B CA    1 
ATOM   7171  C  C     . VAL B 1 199 ? 128.404 141.407 143.998 1.00 8.99  ?  199 VAL B C     1 
ATOM   7172  O  O     . VAL B 1 199 ? 128.223 140.226 143.680 1.00 18.81 ?  199 VAL B O     1 
ATOM   7173  C  CB    . VAL B 1 199 ? 130.425 142.132 142.684 1.00 12.95 ?  199 VAL B CB    1 
ATOM   7174  C  CG1   . VAL B 1 199 ? 129.679 143.192 141.898 1.00 18.72 ?  199 VAL B CG1   1 
ATOM   7175  C  CG2   . VAL B 1 199 ? 131.899 142.472 142.787 1.00 17.15 ?  199 VAL B CG2   1 
ATOM   7176  N  N     . SER B 1 200 ? 127.414 142.244 144.282 1.00 18.60 ?  200 SER B N     1 
ATOM   7177  C  CA    . SER B 1 200 ? 126.010 141.886 144.153 1.00 7.07  ?  200 SER B CA    1 
ATOM   7178  C  C     . SER B 1 200 ? 125.407 142.671 143.000 1.00 13.22 ?  200 SER B C     1 
ATOM   7179  O  O     . SER B 1 200 ? 125.617 143.883 142.893 1.00 22.94 ?  200 SER B O     1 
ATOM   7180  C  CB    . SER B 1 200 ? 125.249 142.167 145.447 1.00 13.11 ?  200 SER B CB    1 
ATOM   7181  O  OG    . SER B 1 200 ? 124.060 141.402 145.509 1.00 22.00 ?  200 SER B OG    1 
ATOM   7182  N  N     . LEU B 1 201 ? 124.667 141.982 142.139 1.00 20.67 ?  201 LEU B N     1 
ATOM   7183  C  CA    . LEU B 1 201 ? 124.094 142.582 140.944 1.00 7.80  ?  201 LEU B CA    1 
ATOM   7184  C  C     . LEU B 1 201 ? 122.581 142.443 140.975 1.00 10.12 ?  201 LEU B C     1 
ATOM   7185  O  O     . LEU B 1 201 ? 122.058 141.364 141.267 1.00 14.11 ?  201 LEU B O     1 
ATOM   7186  C  CB    . LEU B 1 201 ? 124.666 141.931 139.683 1.00 20.30 ?  201 LEU B CB    1 
ATOM   7187  C  CG    . LEU B 1 201 ? 126.182 142.065 139.538 1.00 18.96 ?  201 LEU B CG    1 
ATOM   7188  C  CD1   . LEU B 1 201 ? 126.868 140.732 139.787 1.00 22.23 ?  201 LEU B CD1   1 
ATOM   7189  C  CD2   . LEU B 1 201 ? 126.542 142.611 138.170 1.00 16.03 ?  201 LEU B CD2   1 
ATOM   7190  N  N     . ASN B 1 202 ? 121.887 143.539 140.686 1.00 15.66 ?  202 ASN B N     1 
ATOM   7191  C  CA    . ASN B 1 202 ? 120.434 143.539 140.569 1.00 7.09  ?  202 ASN B CA    1 
ATOM   7192  C  C     . ASN B 1 202 ? 120.074 143.247 139.118 1.00 22.09 ?  202 ASN B C     1 
ATOM   7193  O  O     . ASN B 1 202 ? 120.373 144.045 138.223 1.00 34.99 ?  202 ASN B O     1 
ATOM   7194  C  CB    . ASN B 1 202 ? 119.857 144.876 141.021 1.00 9.23  ?  202 ASN B CB    1 
ATOM   7195  C  CG    . ASN B 1 202 ? 118.378 144.798 141.325 1.00 13.69 ?  202 ASN B CG    1 
ATOM   7196  O  OD1   . ASN B 1 202 ? 117.845 143.727 141.611 1.00 23.02 ?  202 ASN B OD1   1 
ATOM   7197  N  ND2   . ASN B 1 202 ? 117.704 145.939 141.268 1.00 13.77 ?  202 ASN B ND2   1 
ATOM   7198  N  N     . LEU B 1 203 ? 119.432 142.106 138.882 1.00 13.13 ?  203 LEU B N     1 
ATOM   7199  C  CA    . LEU B 1 203 ? 119.058 141.683 137.542 1.00 10.38 ?  203 LEU B CA    1 
ATOM   7200  C  C     . LEU B 1 203 ? 117.582 141.907 137.246 1.00 11.78 ?  203 LEU B C     1 
ATOM   7201  O  O     . LEU B 1 203 ? 117.085 141.419 136.228 1.00 20.55 ?  203 LEU B O     1 
ATOM   7202  C  CB    . LEU B 1 203 ? 119.414 140.208 137.341 1.00 19.25 ?  203 LEU B CB    1 
ATOM   7203  C  CG    . LEU B 1 203 ? 120.883 139.819 137.523 1.00 19.16 ?  203 LEU B CG    1 
ATOM   7204  C  CD1   . LEU B 1 203 ? 121.153 138.462 136.900 1.00 15.97 ?  203 LEU B CD1   1 
ATOM   7205  C  CD2   . LEU B 1 203 ? 121.808 140.870 136.932 1.00 18.43 ?  203 LEU B CD2   1 
ATOM   7206  N  N     . SER B 1 204 ? 116.872 142.639 138.108 1.00 16.09 ?  204 SER B N     1 
ATOM   7207  C  CA    . SER B 1 204 ? 115.430 142.782 137.947 1.00 17.71 ?  204 SER B CA    1 
ATOM   7208  C  C     . SER B 1 204 ? 115.070 143.696 136.784 1.00 20.50 ?  204 SER B C     1 
ATOM   7209  O  O     . SER B 1 204 ? 113.992 143.554 136.199 1.00 27.93 ?  204 SER B O     1 
ATOM   7210  C  CB    . SER B 1 204 ? 114.810 143.304 139.241 1.00 12.46 ?  204 SER B CB    1 
ATOM   7211  O  OG    . SER B 1 204 ? 115.009 142.386 140.297 1.00 24.39 ?  204 SER B OG    1 
ATOM   7212  N  N     . LYS B 1 205 ? 115.944 144.640 136.439 1.00 17.96 ?  205 LYS B N     1 
ATOM   7213  C  CA    . LYS B 1 205 ? 115.674 145.529 135.318 1.00 16.97 ?  205 LYS B CA    1 
ATOM   7214  C  C     . LYS B 1 205 ? 115.868 144.851 133.970 1.00 21.08 ?  205 LYS B C     1 
ATOM   7215  O  O     . LYS B 1 205 ? 115.263 145.284 132.985 1.00 30.01 ?  205 LYS B O     1 
ATOM   7216  C  CB    . LYS B 1 205 ? 116.558 146.771 135.399 1.00 17.17 ?  205 LYS B CB    1 
ATOM   7217  C  CG    . LYS B 1 205 ? 116.199 147.694 136.538 1.00 13.29 ?  205 LYS B CG    1 
ATOM   7218  C  CD    . LYS B 1 205 ? 117.050 148.942 136.518 1.00 19.85 ?  205 LYS B CD    1 
ATOM   7219  C  CE    . LYS B 1 205 ? 116.535 149.967 137.504 1.00 24.37 ?  205 LYS B CE    1 
ATOM   7220  N  NZ    . LYS B 1 205 ? 116.677 149.513 138.911 1.00 17.22 1  205 LYS B NZ    1 
ATOM   7221  N  N     . LEU B 1 206 ? 116.694 143.810 133.906 1.00 17.26 ?  206 LEU B N     1 
ATOM   7222  C  CA    . LEU B 1 206 ? 116.891 143.085 132.661 1.00 11.29 ?  206 LEU B CA    1 
ATOM   7223  C  C     . LEU B 1 206 ? 115.590 142.430 132.218 1.00 19.76 ?  206 LEU B C     1 
ATOM   7224  O  O     . LEU B 1 206 ? 114.899 141.792 133.016 1.00 25.80 ?  206 LEU B O     1 
ATOM   7225  C  CB    . LEU B 1 206 ? 117.979 142.028 132.832 1.00 19.80 ?  206 LEU B CB    1 
ATOM   7226  C  CG    . LEU B 1 206 ? 119.315 142.525 133.375 1.00 22.20 ?  206 LEU B CG    1 
ATOM   7227  C  CD1   . LEU B 1 206 ? 120.254 141.359 133.596 1.00 17.52 ?  206 LEU B CD1   1 
ATOM   7228  C  CD2   . LEU B 1 206 ? 119.925 143.540 132.430 1.00 26.19 ?  206 LEU B CD2   1 
ATOM   7229  N  N     . ARG B 1 207 ? 115.261 142.586 130.940 1.00 26.99 ?  207 ARG B N     1 
ATOM   7230  C  CA    . ARG B 1 207 ? 114.032 142.009 130.422 1.00 22.95 ?  207 ARG B CA    1 
ATOM   7231  C  C     . ARG B 1 207 ? 114.140 140.489 130.354 1.00 26.41 ?  207 ARG B C     1 
ATOM   7232  O  O     . ARG B 1 207 ? 115.226 139.923 130.200 1.00 30.49 ?  207 ARG B O     1 
ATOM   7233  C  CB    . ARG B 1 207 ? 113.698 142.589 129.047 1.00 23.26 ?  207 ARG B CB    1 
ATOM   7234  C  CG    . ARG B 1 207 ? 114.707 142.305 127.956 1.00 24.90 ?  207 ARG B CG    1 
ATOM   7235  C  CD    . ARG B 1 207 ? 114.389 143.127 126.719 1.00 22.50 ?  207 ARG B CD    1 
ATOM   7236  N  NE    . ARG B 1 207 ? 114.771 144.523 126.887 1.00 27.64 ?  207 ARG B NE    1 
ATOM   7237  C  CZ    . ARG B 1 207 ? 114.986 145.369 125.889 1.00 21.97 ?  207 ARG B CZ    1 
ATOM   7238  N  NH1   . ARG B 1 207 ? 114.828 145.005 124.628 1.00 28.60 1  207 ARG B NH1   1 
ATOM   7239  N  NH2   . ARG B 1 207 ? 115.370 146.612 126.164 1.00 18.36 ?  207 ARG B NH2   1 
ATOM   7240  N  N     . ALA B 1 208 ? 112.992 139.833 130.480 1.00 30.71 ?  208 ALA B N     1 
ATOM   7241  C  CA    . ALA B 1 208 ? 112.948 138.390 130.627 1.00 29.17 ?  208 ALA B CA    1 
ATOM   7242  C  C     . ALA B 1 208 ? 113.290 137.688 129.314 1.00 33.52 ?  208 ALA B C     1 
ATOM   7243  O  O     . ALA B 1 208 ? 113.496 138.312 128.269 1.00 35.30 ?  208 ALA B O     1 
ATOM   7244  C  CB    . ALA B 1 208 ? 111.570 137.950 131.110 1.00 26.41 ?  208 ALA B CB    1 
ATOM   7245  N  N     . LYS B 1 209 ? 113.354 136.363 129.389 1.00 26.37 ?  209 LYS B N     1 
ATOM   7246  C  CA    . LYS B 1 209 ? 113.596 135.546 128.211 1.00 22.11 ?  209 LYS B CA    1 
ATOM   7247  C  C     . LYS B 1 209 ? 112.400 135.605 127.271 1.00 33.53 ?  209 LYS B C     1 
ATOM   7248  O  O     . LYS B 1 209 ? 111.245 135.586 127.705 1.00 35.56 ?  209 LYS B O     1 
ATOM   7249  C  CB    . LYS B 1 209 ? 113.876 134.101 128.620 1.00 27.44 ?  209 LYS B CB    1 
ATOM   7250  C  CG    . LYS B 1 209 ? 114.682 133.306 127.608 1.00 33.01 ?  209 LYS B CG    1 
ATOM   7251  C  CD    . LYS B 1 209 ? 114.124 131.903 127.433 1.00 31.98 ?  209 LYS B CD    1 
ATOM   7252  C  CE    . LYS B 1 209 ? 113.572 131.354 128.738 1.00 36.48 ?  209 LYS B CE    1 
ATOM   7253  N  NZ    . LYS B 1 209 ? 112.867 130.058 128.546 1.00 35.63 1  209 LYS B NZ    1 
ATOM   7254  N  N     . GLY B 1 210 ? 112.683 135.668 125.973 1.00 36.34 ?  210 GLY B N     1 
ATOM   7255  C  CA    . GLY B 1 210 ? 111.624 135.781 124.992 1.00 32.08 ?  210 GLY B CA    1 
ATOM   7256  C  C     . GLY B 1 210 ? 111.025 137.163 124.865 1.00 36.40 ?  210 GLY B C     1 
ATOM   7257  O  O     . GLY B 1 210 ? 109.830 137.287 124.582 1.00 38.93 ?  210 GLY B O     1 
ATOM   7258  N  N     . GLU B 1 211 ? 111.816 138.206 125.080 1.00 39.33 ?  211 GLU B N     1 
ATOM   7259  C  CA    . GLU B 1 211 ? 111.379 139.579 124.891 1.00 33.16 ?  211 GLU B CA    1 
ATOM   7260  C  C     . GLU B 1 211 ? 111.990 140.150 123.618 1.00 36.67 ?  211 GLU B C     1 
ATOM   7261  O  O     . GLU B 1 211 ? 112.962 139.623 123.071 1.00 39.90 ?  211 GLU B O     1 
ATOM   7262  C  CB    . GLU B 1 211 ? 111.747 140.444 126.101 1.00 34.62 ?  211 GLU B CB    1 
ATOM   7263  C  CG    . GLU B 1 211 ? 110.896 140.170 127.325 1.00 35.76 ?  211 GLU B CG    1 
ATOM   7264  C  CD    . GLU B 1 211 ? 110.326 141.433 127.933 1.00 41.33 ?  211 GLU B CD    1 
ATOM   7265  O  OE1   . GLU B 1 211 ? 109.552 142.127 127.242 1.00 43.31 ?  211 GLU B OE1   1 
ATOM   7266  O  OE2   . GLU B 1 211 ? 110.640 141.729 129.104 1.00 41.92 -1 211 GLU B OE2   1 
ATOM   7267  N  N     . ALA B 1 212 ? 111.401 141.242 123.147 1.00 37.07 ?  212 ALA B N     1 
ATOM   7268  C  CA    . ALA B 1 212 ? 111.800 141.852 121.888 1.00 33.37 ?  212 ALA B CA    1 
ATOM   7269  C  C     . ALA B 1 212 ? 113.020 142.743 122.076 1.00 38.75 ?  212 ALA B C     1 
ATOM   7270  O  O     . ALA B 1 212 ? 113.145 143.444 123.083 1.00 40.21 ?  212 ALA B O     1 
ATOM   7271  C  CB    . ALA B 1 212 ? 110.649 142.666 121.297 1.00 37.58 ?  212 ALA B CB    1 
ATOM   7272  N  N     . ILE B 1 213 ? 113.919 142.707 121.096 1.00 35.60 ?  213 ILE B N     1 
ATOM   7273  C  CA    . ILE B 1 213 ? 115.068 143.603 121.035 1.00 35.47 ?  213 ILE B CA    1 
ATOM   7274  C  C     . ILE B 1 213 ? 114.895 144.446 119.779 1.00 35.53 ?  213 ILE B C     1 
ATOM   7275  O  O     . ILE B 1 213 ? 115.171 143.977 118.669 1.00 42.01 ?  213 ILE B O     1 
ATOM   7276  C  CB    . ILE B 1 213 ? 116.402 142.848 121.023 1.00 37.16 ?  213 ILE B CB    1 
ATOM   7277  C  CG1   . ILE B 1 213 ? 116.492 141.892 122.211 1.00 36.22 ?  213 ILE B CG1   1 
ATOM   7278  C  CG2   . ILE B 1 213 ? 117.566 143.824 121.042 1.00 33.09 ?  213 ILE B CG2   1 
ATOM   7279  C  CD1   . ILE B 1 213 ? 117.663 140.942 122.139 1.00 31.45 ?  213 ILE B CD1   1 
ATOM   7280  N  N     . LYS B 1 214 ? 114.431 145.687 119.955 1.00 40.21 ?  214 LYS B N     1 
ATOM   7281  C  CA    . LYS B 1 214 ? 114.199 146.661 118.887 1.00 39.89 ?  214 LYS B CA    1 
ATOM   7282  C  C     . LYS B 1 214 ? 113.518 146.038 117.671 1.00 45.59 ?  214 LYS B C     1 
ATOM   7283  O  O     . LYS B 1 214 ? 114.119 145.939 116.596 1.00 45.66 ?  214 LYS B O     1 
ATOM   7284  C  CB    . LYS B 1 214 ? 115.495 147.392 118.485 1.00 39.26 ?  214 LYS B CB    1 
ATOM   7285  C  CG    . LYS B 1 214 ? 116.726 146.554 118.174 1.00 41.69 ?  214 LYS B CG    1 
ATOM   7286  C  CD    . LYS B 1 214 ? 117.767 147.380 117.442 1.00 40.17 ?  214 LYS B CD    1 
ATOM   7287  C  CE    . LYS B 1 214 ? 119.104 146.667 117.391 1.00 42.26 ?  214 LYS B CE    1 
ATOM   7288  N  NZ    . LYS B 1 214 ? 120.238 147.632 117.430 1.00 44.06 1  214 LYS B NZ    1 
ATOM   7289  N  N     . ASP B 1 215 ? 112.271 145.602 117.851 1.00 52.33 ?  215 ASP B N     1 
ATOM   7290  C  CA    . ASP B 1 215 ? 111.343 145.064 116.860 1.00 53.60 ?  215 ASP B CA    1 
ATOM   7291  C  C     . ASP B 1 215 ? 111.620 143.602 116.520 1.00 54.25 ?  215 ASP B C     1 
ATOM   7292  O  O     . ASP B 1 215 ? 110.891 143.033 115.707 1.00 56.29 ?  215 ASP B O     1 
ATOM   7293  C  CB    . ASP B 1 215 ? 111.310 145.876 115.549 1.00 52.06 ?  215 ASP B CB    1 
ATOM   7294  C  CG    . ASP B 1 215 ? 110.641 147.224 115.717 1.00 59.18 ?  215 ASP B CG    1 
ATOM   7295  O  OD1   . ASP B 1 215 ? 109.408 147.256 115.919 1.00 56.38 ?  215 ASP B OD1   1 
ATOM   7296  O  OD2   . ASP B 1 215 ? 111.347 148.251 115.646 1.00 56.99 -1 215 ASP B OD2   1 
ATOM   7297  N  N     . VAL B 1 216 ? 112.636 142.973 117.100 1.00 48.01 ?  216 VAL B N     1 
ATOM   7298  C  CA    . VAL B 1 216 ? 112.855 141.544 116.903 1.00 43.71 ?  216 VAL B CA    1 
ATOM   7299  C  C     . VAL B 1 216 ? 112.351 140.811 118.140 1.00 48.49 ?  216 VAL B C     1 
ATOM   7300  O  O     . VAL B 1 216 ? 113.047 140.737 119.157 1.00 51.75 ?  216 VAL B O     1 
ATOM   7301  C  CB    . VAL B 1 216 ? 114.337 141.241 116.638 1.00 45.75 ?  216 VAL B CB    1 
ATOM   7302  C  CG1   . VAL B 1 216 ? 114.557 139.743 116.504 1.00 45.61 ?  216 VAL B CG1   1 
ATOM   7303  C  CG2   . VAL B 1 216 ? 114.807 141.968 115.391 1.00 43.69 ?  216 VAL B CG2   1 
ATOM   7304  N  N     . GLU B 1 217 ? 111.142 140.266 118.051 1.00 49.70 ?  217 GLU B N     1 
ATOM   7305  C  CA    . GLU B 1 217 ? 110.480 139.644 119.187 1.00 50.06 ?  217 GLU B CA    1 
ATOM   7306  C  C     . GLU B 1 217 ? 111.150 138.327 119.556 1.00 45.18 ?  217 GLU B C     1 
ATOM   7307  O  O     . GLU B 1 217 ? 111.793 137.679 118.731 1.00 45.39 ?  217 GLU B O     1 
ATOM   7308  C  CB    . GLU B 1 217 ? 109.002 139.403 118.880 1.00 46.34 ?  217 GLU B CB    1 
ATOM   7309  C  CG    . GLU B 1 217 ? 108.405 140.391 117.899 1.00 49.31 ?  217 GLU B CG    1 
ATOM   7310  C  CD    . GLU B 1 217 ? 108.060 141.713 118.551 1.00 52.31 ?  217 GLU B CD    1 
ATOM   7311  O  OE1   . GLU B 1 217 ? 107.455 141.698 119.643 1.00 50.98 ?  217 GLU B OE1   1 
ATOM   7312  O  OE2   . GLU B 1 217 ? 108.394 142.768 117.971 1.00 54.93 -1 217 GLU B OE2   1 
ATOM   7313  N  N     . ASN B 1 218 ? 110.989 137.943 120.824 1.00 42.09 ?  218 ASN B N     1 
ATOM   7314  C  CA    . ASN B 1 218 ? 111.463 136.655 121.335 1.00 43.42 ?  218 ASN B CA    1 
ATOM   7315  C  C     . ASN B 1 218 ? 112.958 136.464 121.091 1.00 46.69 ?  218 ASN B C     1 
ATOM   7316  O  O     . ASN B 1 218 ? 113.412 135.390 120.689 1.00 48.20 ?  218 ASN B O     1 
ATOM   7317  C  CB    . ASN B 1 218 ? 110.658 135.505 120.725 1.00 42.39 ?  218 ASN B CB    1 
ATOM   7318  C  CG    . ASN B 1 218 ? 110.597 134.294 121.629 1.00 46.35 ?  218 ASN B CG    1 
ATOM   7319  O  OD1   . ASN B 1 218 ? 109.717 134.187 122.482 1.00 49.47 ?  218 ASN B OD1   1 
ATOM   7320  N  ND2   . ASN B 1 218 ? 111.534 133.373 121.448 1.00 47.74 ?  218 ASN B ND2   1 
ATOM   7321  N  N     . ALA B 1 219 ? 113.738 137.516 121.343 1.00 35.88 ?  219 ALA B N     1 
ATOM   7322  C  CA    . ALA B 1 219 ? 115.166 137.500 121.056 1.00 33.97 ?  219 ALA B CA    1 
ATOM   7323  C  C     . ALA B 1 219 ? 116.055 137.555 122.290 1.00 37.71 ?  219 ALA B C     1 
ATOM   7324  O  O     . ALA B 1 219 ? 117.262 137.334 122.165 1.00 37.78 ?  219 ALA B O     1 
ATOM   7325  C  CB    . ALA B 1 219 ? 115.535 138.672 120.135 1.00 34.85 ?  219 ALA B CB    1 
ATOM   7326  N  N     . THR B 1 220 ? 115.499 137.841 123.462 1.00 34.96 ?  220 THR B N     1 
ATOM   7327  C  CA    . THR B 1 220 ? 116.293 138.018 124.671 1.00 33.11 ?  220 THR B CA    1 
ATOM   7328  C  C     . THR B 1 220 ? 116.461 136.685 125.388 1.00 35.08 ?  220 THR B C     1 
ATOM   7329  O  O     . THR B 1 220 ? 115.494 135.936 125.556 1.00 33.67 ?  220 THR B O     1 
ATOM   7330  C  CB    . THR B 1 220 ? 115.633 139.041 125.596 1.00 28.35 ?  220 THR B CB    1 
ATOM   7331  O  OG1   . THR B 1 220 ? 115.473 140.282 124.900 1.00 34.03 ?  220 THR B OG1   1 
ATOM   7332  C  CG2   . THR B 1 220 ? 116.482 139.274 126.831 1.00 33.35 ?  220 THR B CG2   1 
ATOM   7333  N  N     . LYS B 1 221 ? 117.695 136.390 125.804 1.00 35.88 ?  221 LYS B N     1 
ATOM   7334  C  CA    . LYS B 1 221 ? 117.972 135.192 126.584 1.00 32.46 ?  221 LYS B CA    1 
ATOM   7335  C  C     . LYS B 1 221 ? 117.540 135.319 128.036 1.00 36.33 ?  221 LYS B C     1 
ATOM   7336  O  O     . LYS B 1 221 ? 117.567 134.320 128.763 1.00 40.45 ?  221 LYS B O     1 
ATOM   7337  C  CB    . LYS B 1 221 ? 119.464 134.855 126.537 1.00 33.12 ?  221 LYS B CB    1 
ATOM   7338  C  CG    . LYS B 1 221 ? 120.188 135.385 125.320 1.00 31.06 ?  221 LYS B CG    1 
ATOM   7339  C  CD    . LYS B 1 221 ? 121.525 134.691 125.149 1.00 36.10 ?  221 LYS B CD    1 
ATOM   7340  C  CE    . LYS B 1 221 ? 121.350 133.259 124.686 1.00 37.98 ?  221 LYS B CE    1 
ATOM   7341  N  NZ    . LYS B 1 221 ? 120.618 133.188 123.397 1.00 37.38 1  221 LYS B NZ    1 
ATOM   7342  N  N     . GLY B 1 222 ? 117.155 136.508 128.474 1.00 34.14 ?  222 GLY B N     1 
ATOM   7343  C  CA    . GLY B 1 222 ? 116.696 136.703 129.830 1.00 32.70 ?  222 GLY B CA    1 
ATOM   7344  C  C     . GLY B 1 222 ? 117.833 136.962 130.797 1.00 31.75 ?  222 GLY B C     1 
ATOM   7345  O  O     . GLY B 1 222 ? 118.966 137.276 130.422 1.00 34.90 ?  222 GLY B O     1 
ATOM   7346  N  N     . VAL B 1 223 ? 117.508 136.828 132.085 1.00 26.93 ?  223 VAL B N     1 
ATOM   7347  C  CA    . VAL B 1 223 ? 118.500 137.055 133.131 1.00 30.96 ?  223 VAL B CA    1 
ATOM   7348  C  C     . VAL B 1 223 ? 119.481 135.905 133.268 1.00 22.59 ?  223 VAL B C     1 
ATOM   7349  O  O     . VAL B 1 223 ? 120.532 136.081 133.892 1.00 25.89 ?  223 VAL B O     1 
ATOM   7350  C  CB    . VAL B 1 223 ? 117.832 137.313 134.494 1.00 27.74 ?  223 VAL B CB    1 
ATOM   7351  C  CG1   . VAL B 1 223 ? 116.743 138.360 134.360 1.00 21.69 ?  223 VAL B CG1   1 
ATOM   7352  C  CG2   . VAL B 1 223 ? 117.274 136.023 135.076 1.00 26.44 ?  223 VAL B CG2   1 
ATOM   7353  N  N     . VAL B 1 224 ? 119.184 134.738 132.693 1.00 26.79 ?  224 VAL B N     1 
ATOM   7354  C  CA    . VAL B 1 224 ? 120.070 133.592 132.862 1.00 26.01 ?  224 VAL B CA    1 
ATOM   7355  C  C     . VAL B 1 224 ? 121.301 133.697 131.964 1.00 31.64 ?  224 VAL B C     1 
ATOM   7356  O  O     . VAL B 1 224 ? 122.386 133.245 132.342 1.00 37.19 ?  224 VAL B O     1 
ATOM   7357  C  CB    . VAL B 1 224 ? 119.298 132.286 132.618 1.00 32.12 ?  224 VAL B CB    1 
ATOM   7358  C  CG1   . VAL B 1 224 ? 120.177 131.085 132.918 1.00 28.23 ?  224 VAL B CG1   1 
ATOM   7359  C  CG2   . VAL B 1 224 ? 118.049 132.254 133.476 1.00 32.42 ?  224 VAL B CG2   1 
ATOM   7360  N  N     . GLY B 1 225 ? 121.172 134.288 130.775 1.00 20.31 ?  225 GLY B N     1 
ATOM   7361  C  CA    . GLY B 1 225 ? 122.354 134.545 129.968 1.00 17.94 ?  225 GLY B CA    1 
ATOM   7362  C  C     . GLY B 1 225 ? 123.306 135.514 130.641 1.00 20.10 ?  225 GLY B C     1 
ATOM   7363  O  O     . GLY B 1 225 ? 124.523 135.300 130.660 1.00 30.82 ?  225 GLY B O     1 
ATOM   7364  N  N     . VAL B 1 226 ? 122.762 136.587 131.218 1.00 18.63 ?  226 VAL B N     1 
ATOM   7365  C  CA    . VAL B 1 226 ? 123.574 137.511 132.000 1.00 21.71 ?  226 VAL B CA    1 
ATOM   7366  C  C     . VAL B 1 226 ? 124.145 136.811 133.224 1.00 18.90 ?  226 VAL B C     1 
ATOM   7367  O  O     . VAL B 1 226 ? 125.265 137.104 133.649 1.00 23.94 ?  226 VAL B O     1 
ATOM   7368  C  CB    . VAL B 1 226 ? 122.745 138.751 132.389 1.00 21.28 ?  226 VAL B CB    1 
ATOM   7369  C  CG1   . VAL B 1 226 ? 123.608 139.762 133.124 1.00 29.21 ?  226 VAL B CG1   1 
ATOM   7370  C  CG2   . VAL B 1 226 ? 122.127 139.374 131.153 1.00 23.54 ?  226 VAL B CG2   1 
ATOM   7371  N  N     . MET B 1 227 ? 123.388 135.882 133.808 1.00 22.86 ?  227 MET B N     1 
ATOM   7372  C  CA    . MET B 1 227 ? 123.887 135.112 134.943 1.00 23.74 ?  227 MET B CA    1 
ATOM   7373  C  C     . MET B 1 227 ? 125.101 134.279 134.556 1.00 25.47 ?  227 MET B C     1 
ATOM   7374  O  O     . MET B 1 227 ? 126.079 134.214 135.305 1.00 28.53 ?  227 MET B O     1 
ATOM   7375  C  CB    . MET B 1 227 ? 122.777 134.215 135.482 1.00 17.04 ?  227 MET B CB    1 
ATOM   7376  C  CG    . MET B 1 227 ? 121.853 134.885 136.473 1.00 18.35 ?  227 MET B CG    1 
ATOM   7377  S  SD    . MET B 1 227 ? 120.779 133.682 137.262 1.00 33.72 ?  227 MET B SD    1 
ATOM   7378  C  CE    . MET B 1 227 ? 121.835 133.148 138.595 1.00 30.40 ?  227 MET B CE    1 
ATOM   7379  N  N     . LYS B 1 228 ? 125.050 133.626 133.395 1.00 23.81 ?  228 LYS B N     1 
ATOM   7380  C  CA    . LYS B 1 228 ? 126.199 132.862 132.915 1.00 19.93 ?  228 LYS B CA    1 
ATOM   7381  C  C     . LYS B 1 228 ? 127.388 133.772 132.637 1.00 20.40 ?  228 LYS B C     1 
ATOM   7382  O  O     . LYS B 1 228 ? 128.534 133.436 132.972 1.00 26.34 ?  228 LYS B O     1 
ATOM   7383  C  CB    . LYS B 1 228 ? 125.827 132.083 131.656 1.00 22.60 ?  228 LYS B CB    1 
ATOM   7384  C  CG    . LYS B 1 228 ? 124.695 131.099 131.839 1.00 24.65 ?  228 LYS B CG    1 
ATOM   7385  C  CD    . LYS B 1 228 ? 124.679 130.088 130.711 1.00 33.66 ?  228 LYS B CD    1 
ATOM   7386  C  CE    . LYS B 1 228 ? 123.746 130.519 129.591 1.00 38.31 ?  228 LYS B CE    1 
ATOM   7387  N  NZ    . LYS B 1 228 ? 122.322 130.228 129.912 1.00 36.29 1  228 LYS B NZ    1 
ATOM   7388  N  N     . LEU B 1 229 ? 127.134 134.925 132.014 1.00 22.70 ?  229 LEU B N     1 
ATOM   7389  C  CA    . LEU B 1 229 ? 128.206 135.882 131.761 1.00 20.74 ?  229 LEU B CA    1 
ATOM   7390  C  C     . LEU B 1 229 ? 128.865 136.319 133.061 1.00 24.12 ?  229 LEU B C     1 
ATOM   7391  O  O     . LEU B 1 229 ? 130.095 136.368 133.164 1.00 29.02 ?  229 LEU B O     1 
ATOM   7392  C  CB    . LEU B 1 229 ? 127.664 137.098 131.014 1.00 23.24 ?  229 LEU B CB    1 
ATOM   7393  C  CG    . LEU B 1 229 ? 127.420 137.004 129.511 1.00 19.83 ?  229 LEU B CG    1 
ATOM   7394  C  CD1   . LEU B 1 229 ? 126.541 138.157 129.076 1.00 24.18 ?  229 LEU B CD1   1 
ATOM   7395  C  CD2   . LEU B 1 229 ? 128.733 137.015 128.757 1.00 19.50 ?  229 LEU B CD2   1 
ATOM   7396  N  N     . LEU B 1 230 ? 128.055 136.632 134.074 1.00 27.00 ?  230 LEU B N     1 
ATOM   7397  C  CA    . LEU B 1 230 ? 128.587 137.083 135.354 1.00 18.28 ?  230 LEU B CA    1 
ATOM   7398  C  C     . LEU B 1 230 ? 129.311 135.959 136.081 1.00 13.47 ?  230 LEU B C     1 
ATOM   7399  O  O     . LEU B 1 230 ? 130.324 136.198 136.742 1.00 32.34 ?  230 LEU B O     1 
ATOM   7400  C  CB    . LEU B 1 230 ? 127.461 137.644 136.220 1.00 19.19 ?  230 LEU B CB    1 
ATOM   7401  C  CG    . LEU B 1 230 ? 126.834 138.951 135.739 1.00 23.66 ?  230 LEU B CG    1 
ATOM   7402  C  CD1   . LEU B 1 230 ? 125.604 139.282 136.565 1.00 28.79 ?  230 LEU B CD1   1 
ATOM   7403  C  CD2   . LEU B 1 230 ? 127.845 140.085 135.788 1.00 24.41 ?  230 LEU B CD2   1 
ATOM   7404  N  N     . ASP B 1 231 ? 128.802 134.731 135.984 1.00 22.77 ?  231 ASP B N     1 
ATOM   7405  C  CA    . ASP B 1 231 ? 129.472 133.603 136.618 1.00 25.27 ?  231 ASP B CA    1 
ATOM   7406  C  C     . ASP B 1 231 ? 130.853 133.382 136.020 1.00 29.78 ?  231 ASP B C     1 
ATOM   7407  O  O     . ASP B 1 231 ? 131.830 133.181 136.750 1.00 33.95 ?  231 ASP B O     1 
ATOM   7408  C  CB    . ASP B 1 231 ? 128.617 132.343 136.483 1.00 24.32 ?  231 ASP B CB    1 
ATOM   7409  C  CG    . ASP B 1 231 ? 129.157 131.183 137.290 1.00 40.21 ?  231 ASP B CG    1 
ATOM   7410  O  OD1   . ASP B 1 231 ? 128.987 131.190 138.527 1.00 44.23 ?  231 ASP B OD1   1 
ATOM   7411  O  OD2   . ASP B 1 231 ? 129.752 130.263 136.692 1.00 39.45 -1 231 ASP B OD2   1 
ATOM   7412  N  N     . ASN B 1 232 ? 130.961 133.441 134.692 1.00 30.21 ?  232 ASN B N     1 
ATOM   7413  C  CA    . ASN B 1 232 ? 132.272 133.308 134.065 1.00 28.77 ?  232 ASN B CA    1 
ATOM   7414  C  C     . ASN B 1 232 ? 133.163 134.509 134.362 1.00 23.15 ?  232 ASN B C     1 
ATOM   7415  O  O     . ASN B 1 232 ? 134.383 134.361 134.503 1.00 31.63 ?  232 ASN B O     1 
ATOM   7416  C  CB    . ASN B 1 232 ? 132.114 133.093 132.564 1.00 26.34 ?  232 ASN B CB    1 
ATOM   7417  C  CG    . ASN B 1 232 ? 132.062 131.629 132.203 1.00 31.22 ?  232 ASN B CG    1 
ATOM   7418  O  OD1   . ASN B 1 232 ? 132.855 130.830 132.699 1.00 36.86 ?  232 ASN B OD1   1 
ATOM   7419  N  ND2   . ASN B 1 232 ? 131.101 131.258 131.381 1.00 35.04 ?  232 ASN B ND2   1 
ATOM   7420  N  N     . ALA B 1 233 ? 132.579 135.703 134.466 1.00 18.47 ?  233 ALA B N     1 
ATOM   7421  C  CA    . ALA B 1 233 ? 133.363 136.881 134.817 1.00 15.26 ?  233 ALA B CA    1 
ATOM   7422  C  C     . ALA B 1 233 ? 133.948 136.757 136.219 1.00 26.94 ?  233 ALA B C     1 
ATOM   7423  O  O     . ALA B 1 233 ? 135.101 137.135 136.455 1.00 30.67 ?  233 ALA B O     1 
ATOM   7424  C  CB    . ALA B 1 233 ? 132.498 138.134 134.701 1.00 20.26 ?  233 ALA B CB    1 
ATOM   7425  N  N     . PHE B 1 234 ? 133.161 136.238 137.164 1.00 30.52 ?  234 PHE B N     1 
ATOM   7426  C  CA    . PHE B 1 234 ? 133.651 136.049 138.524 1.00 24.01 ?  234 PHE B CA    1 
ATOM   7427  C  C     . PHE B 1 234 ? 134.644 134.899 138.606 1.00 24.34 ?  234 PHE B C     1 
ATOM   7428  O  O     . PHE B 1 234 ? 135.579 134.947 139.413 1.00 29.06 ?  234 PHE B O     1 
ATOM   7429  C  CB    . PHE B 1 234 ? 132.483 135.812 139.479 1.00 21.79 ?  234 PHE B CB    1 
ATOM   7430  C  CG    . PHE B 1 234 ? 131.748 137.064 139.852 1.00 21.25 ?  234 PHE B CG    1 
ATOM   7431  C  CD1   . PHE B 1 234 ? 132.412 138.121 140.447 1.00 24.86 ?  234 PHE B CD1   1 
ATOM   7432  C  CD2   . PHE B 1 234 ? 130.394 137.185 139.609 1.00 23.68 ?  234 PHE B CD2   1 
ATOM   7433  C  CE1   . PHE B 1 234 ? 131.736 139.273 140.787 1.00 24.28 ?  234 PHE B CE1   1 
ATOM   7434  C  CE2   . PHE B 1 234 ? 129.716 138.335 139.944 1.00 23.92 ?  234 PHE B CE2   1 
ATOM   7435  C  CZ    . PHE B 1 234 ? 130.387 139.377 140.536 1.00 24.77 ?  234 PHE B CZ    1 
ATOM   7436  N  N     . ARG B 1 235 ? 134.455 133.856 137.795 1.00 31.14 ?  235 ARG B N     1 
ATOM   7437  C  CA    . ARG B 1 235 ? 135.433 132.775 137.743 1.00 25.16 ?  235 ARG B CA    1 
ATOM   7438  C  C     . ARG B 1 235 ? 136.767 133.262 137.191 1.00 31.81 ?  235 ARG B C     1 
ATOM   7439  O  O     . ARG B 1 235 ? 137.828 132.839 137.660 1.00 40.91 ?  235 ARG B O     1 
ATOM   7440  C  CB    . ARG B 1 235 ? 134.894 131.614 136.909 1.00 28.01 ?  235 ARG B CB    1 
ATOM   7441  C  CG    . ARG B 1 235 ? 134.148 130.577 137.727 1.00 38.67 ?  235 ARG B CG    1 
ATOM   7442  C  CD    . ARG B 1 235 ? 133.881 129.305 136.943 1.00 33.71 ?  235 ARG B CD    1 
ATOM   7443  N  NE    . ARG B 1 235 ? 132.529 129.275 136.398 1.00 37.92 ?  235 ARG B NE    1 
ATOM   7444  C  CZ    . ARG B 1 235 ? 132.245 129.186 135.106 1.00 40.90 ?  235 ARG B CZ    1 
ATOM   7445  N  NH1   . ARG B 1 235 ? 133.200 129.098 134.195 1.00 42.51 1  235 ARG B NH1   1 
ATOM   7446  N  NH2   . ARG B 1 235 ? 130.974 129.186 134.721 1.00 36.14 ?  235 ARG B NH2   1 
ATOM   7447  N  N     . TYR B 1 236 ? 136.735 134.139 136.187 1.00 22.81 ?  236 TYR B N     1 
ATOM   7448  C  CA    . TYR B 1 236 ? 137.979 134.659 135.632 1.00 24.99 ?  236 TYR B CA    1 
ATOM   7449  C  C     . TYR B 1 236 ? 138.666 135.601 136.612 1.00 24.34 ?  236 TYR B C     1 
ATOM   7450  O  O     . TYR B 1 236 ? 139.871 135.486 136.859 1.00 26.55 ?  236 TYR B O     1 
ATOM   7451  C  CB    . TYR B 1 236 ? 137.712 135.371 134.308 1.00 24.45 ?  236 TYR B CB    1 
ATOM   7452  C  CG    . TYR B 1 236 ? 138.969 135.877 133.649 1.00 22.08 ?  236 TYR B CG    1 
ATOM   7453  C  CD1   . TYR B 1 236 ? 139.852 134.996 133.046 1.00 18.62 ?  236 TYR B CD1   1 
ATOM   7454  C  CD2   . TYR B 1 236 ? 139.283 137.229 133.643 1.00 18.79 ?  236 TYR B CD2   1 
ATOM   7455  C  CE1   . TYR B 1 236 ? 141.002 135.442 132.448 1.00 23.08 ?  236 TYR B CE1   1 
ATOM   7456  C  CE2   . TYR B 1 236 ? 140.434 137.685 133.044 1.00 13.61 ?  236 TYR B CE2   1 
ATOM   7457  C  CZ    . TYR B 1 236 ? 141.290 136.786 132.449 1.00 20.82 ?  236 TYR B CZ    1 
ATOM   7458  O  OH    . TYR B 1 236 ? 142.440 137.222 131.847 1.00 30.55 ?  236 TYR B OH    1 
ATOM   7459  N  N     . ALA B 1 237 ? 137.914 136.545 137.180 1.00 29.80 ?  237 ALA B N     1 
ATOM   7460  C  CA    . ALA B 1 237 ? 138.458 137.502 138.142 1.00 29.51 ?  237 ALA B CA    1 
ATOM   7461  C  C     . ALA B 1 237 ? 138.489 136.848 139.523 1.00 36.56 ?  237 ALA B C     1 
ATOM   7462  O  O     . ALA B 1 237 ? 137.722 137.171 140.431 1.00 36.35 ?  237 ALA B O     1 
ATOM   7463  C  CB    . ALA B 1 237 ? 137.644 138.787 138.141 1.00 30.47 ?  237 ALA B CB    1 
ATOM   7464  N  N     . ASP B 1 238 ? 139.415 135.899 139.667 1.00 51.59 ?  238 ASP B N     1 
ATOM   7465  C  CA    . ASP B 1 238 ? 139.508 135.062 140.855 1.00 51.32 ?  238 ASP B CA    1 
ATOM   7466  C  C     . ASP B 1 238 ? 140.512 135.591 141.870 1.00 55.56 ?  238 ASP B C     1 
ATOM   7467  O  O     . ASP B 1 238 ? 141.141 134.795 142.582 1.00 57.66 ?  238 ASP B O     1 
ATOM   7468  C  CB    . ASP B 1 238 ? 139.859 133.628 140.457 1.00 49.85 ?  238 ASP B CB    1 
ATOM   7469  C  CG    . ASP B 1 238 ? 138.707 132.670 140.663 1.00 54.08 ?  238 ASP B CG    1 
ATOM   7470  O  OD1   . ASP B 1 238 ? 138.698 131.602 140.016 1.00 53.16 ?  238 ASP B OD1   1 
ATOM   7471  O  OD2   . ASP B 1 238 ? 137.798 132.995 141.453 1.00 53.25 -1 238 ASP B OD2   1 
ATOM   7472  N  N     . GLN B 1 239 ? 140.688 136.912 141.942 1.00 64.45 ?  239 GLN B N     1 
ATOM   7473  C  CA    . GLN B 1 239 ? 141.579 137.548 142.914 1.00 65.28 ?  239 GLN B CA    1 
ATOM   7474  C  C     . GLN B 1 239 ? 143.008 137.020 142.788 1.00 67.16 ?  239 GLN B C     1 
ATOM   7475  O  O     . GLN B 1 239 ? 143.616 136.570 143.761 1.00 64.76 ?  239 GLN B O     1 
ATOM   7476  C  CB    . GLN B 1 239 ? 141.051 137.366 144.340 1.00 64.30 ?  239 GLN B CB    1 
ATOM   7477  C  CG    . GLN B 1 239 ? 139.604 137.780 144.520 1.00 63.46 ?  239 GLN B CG    1 
ATOM   7478  C  CD    . GLN B 1 239 ? 139.057 137.406 145.880 1.00 66.62 ?  239 GLN B CD    1 
ATOM   7479  O  OE1   . GLN B 1 239 ? 137.863 137.146 146.031 1.00 64.72 ?  239 GLN B OE1   1 
ATOM   7480  N  NE2   . GLN B 1 239 ? 139.927 137.379 146.881 1.00 66.44 ?  239 GLN B NE2   1 
ATOM   7481  N  N     . MET B 1 240 ? 143.537 137.074 141.564 1.00 68.36 ?  240 MET B N     1 
ATOM   7482  C  CA    . MET B 1 240 ? 144.898 136.628 141.261 1.00 67.11 ?  240 MET B CA    1 
ATOM   7483  C  C     . MET B 1 240 ? 145.126 135.174 141.664 1.00 67.96 ?  240 MET B C     1 
ATOM   7484  O  O     . MET B 1 240 ? 146.217 134.803 142.103 1.00 68.29 ?  240 MET B O     1 
ATOM   7485  C  CB    . MET B 1 240 ? 145.941 137.532 141.927 1.00 67.19 ?  240 MET B CB    1 
ATOM   7486  C  CG    . MET B 1 240 ? 146.017 138.935 141.352 1.00 68.64 ?  240 MET B CG    1 
ATOM   7487  S  SD    . MET B 1 240 ? 144.412 139.637 140.936 1.00 76.69 ?  240 MET B SD    1 
ATOM   7488  C  CE    . MET B 1 240 ? 144.856 141.362 140.761 1.00 66.55 ?  240 MET B CE    1 
ATOM   7489  N  N     . GLY B 1 241 ? 144.099 134.339 141.524 1.00 70.46 ?  241 GLY B N     1 
ATOM   7490  C  CA    . GLY B 1 241 ? 144.221 132.940 141.880 1.00 69.56 ?  241 GLY B CA    1 
ATOM   7491  C  C     . GLY B 1 241 ? 144.377 132.663 143.356 1.00 72.28 ?  241 GLY B C     1 
ATOM   7492  O  O     . GLY B 1 241 ? 144.811 131.567 143.722 1.00 72.91 ?  241 GLY B O     1 
ATOM   7493  N  N     . GLN B 1 242 ? 144.041 133.621 144.219 1.00 73.68 ?  242 GLN B N     1 
ATOM   7494  C  CA    . GLN B 1 242 ? 144.186 133.446 145.660 1.00 73.00 ?  242 GLN B CA    1 
ATOM   7495  C  C     . GLN B 1 242 ? 142.899 132.920 146.291 1.00 73.64 ?  242 GLN B C     1 
ATOM   7496  O  O     . GLN B 1 242 ? 142.892 131.853 146.912 1.00 71.98 ?  242 GLN B O     1 
ATOM   7497  C  CB    . GLN B 1 242 ? 144.598 134.772 146.311 1.00 71.35 ?  242 GLN B CB    1 
ATOM   7498  C  CG    . GLN B 1 242 ? 145.979 135.264 145.909 1.00 73.43 ?  242 GLN B CG    1 
ATOM   7499  C  CD    . GLN B 1 242 ? 146.533 136.300 146.870 1.00 75.32 ?  242 GLN B CD    1 
ATOM   7500  O  OE1   . GLN B 1 242 ? 145.968 136.538 147.938 1.00 75.18 ?  242 GLN B OE1   1 
ATOM   7501  N  NE2   . GLN B 1 242 ? 147.646 136.920 146.496 1.00 72.12 ?  242 GLN B NE2   1 
ATOM   7502  N  N     . ARG B 1 243 ? 141.805 133.661 146.135 1.00 68.25 ?  243 ARG B N     1 
ATOM   7503  C  CA    . ARG B 1 243 ? 140.511 133.296 146.688 1.00 66.93 ?  243 ARG B CA    1 
ATOM   7504  C  C     . ARG B 1 243 ? 139.470 133.345 145.582 1.00 66.24 ?  243 ARG B C     1 
ATOM   7505  O  O     . ARG B 1 243 ? 139.479 134.258 144.752 1.00 65.42 ?  243 ARG B O     1 
ATOM   7506  C  CB    . ARG B 1 243 ? 140.122 134.233 147.840 1.00 66.32 ?  243 ARG B CB    1 
ATOM   7507  C  CG    . ARG B 1 243 ? 138.761 133.961 148.458 1.00 66.93 ?  243 ARG B CG    1 
ATOM   7508  C  CD    . ARG B 1 243 ? 138.274 135.172 149.242 1.00 67.50 ?  243 ARG B CD    1 
ATOM   7509  N  NE    . ARG B 1 243 ? 137.559 136.124 148.402 1.00 69.40 ?  243 ARG B NE    1 
ATOM   7510  C  CZ    . ARG B 1 243 ? 136.394 136.676 148.717 1.00 69.52 ?  243 ARG B CZ    1 
ATOM   7511  N  NH1   . ARG B 1 243 ? 135.784 136.396 149.856 1.00 66.61 1  243 ARG B NH1   1 
ATOM   7512  N  NH2   . ARG B 1 243 ? 135.831 137.533 147.870 1.00 64.05 ?  243 ARG B NH2   1 
ATOM   7513  N  N     . GLN B 1 244 ? 138.578 132.356 145.573 1.00 64.22 ?  244 GLN B N     1 
ATOM   7514  C  CA    . GLN B 1 244 ? 137.604 132.229 144.497 1.00 63.23 ?  244 GLN B CA    1 
ATOM   7515  C  C     . GLN B 1 244 ? 136.700 133.454 144.432 1.00 63.95 ?  244 GLN B C     1 
ATOM   7516  O  O     . GLN B 1 244 ? 136.206 133.934 145.456 1.00 61.87 ?  244 GLN B O     1 
ATOM   7517  C  CB    . GLN B 1 244 ? 136.769 130.964 144.690 1.00 61.27 ?  244 GLN B CB    1 
ATOM   7518  C  CG    . GLN B 1 244 ? 137.585 129.680 144.685 1.00 62.33 ?  244 GLN B CG    1 
ATOM   7519  C  CD    . GLN B 1 244 ? 136.716 128.438 144.705 1.00 62.46 ?  244 GLN B CD    1 
ATOM   7520  O  OE1   . GLN B 1 244 ? 135.694 128.390 145.390 1.00 60.44 ?  244 GLN B OE1   1 
ATOM   7521  N  NE2   . GLN B 1 244 ? 137.118 127.422 143.949 1.00 60.00 ?  244 GLN B NE2   1 
ATOM   7522  N  N     . GLY B 1 245 ? 136.492 133.960 143.217 1.00 49.21 ?  245 GLY B N     1 
ATOM   7523  C  CA    . GLY B 1 245 ? 135.640 135.113 143.002 1.00 44.50 ?  245 GLY B CA    1 
ATOM   7524  C  C     . GLY B 1 245 ? 134.193 134.847 143.358 1.00 44.34 ?  245 GLY B C     1 
ATOM   7525  O  O     . GLY B 1 245 ? 133.571 133.929 142.815 1.00 41.39 ?  245 GLY B O     1 
ATOM   7526  N  N     . SER B 1 246 ? 133.645 135.646 144.267 1.00 39.46 ?  246 SER B N     1 
ATOM   7527  C  CA    . SER B 1 246 ? 132.297 135.451 144.779 1.00 33.42 ?  246 SER B CA    1 
ATOM   7528  C  C     . SER B 1 246 ? 131.411 136.608 144.345 1.00 30.07 ?  246 SER B C     1 
ATOM   7529  O  O     . SER B 1 246 ? 131.766 137.776 144.533 1.00 23.53 ?  246 SER B O     1 
ATOM   7530  C  CB    . SER B 1 246 ? 132.305 135.333 146.305 1.00 31.88 ?  246 SER B CB    1 
ATOM   7531  O  OG    . SER B 1 246 ? 132.974 136.433 146.898 1.00 38.37 ?  246 SER B OG    1 
ATOM   7532  N  N     . GLY B 1 247 ? 130.261 136.277 143.765 1.00 26.03 ?  247 GLY B N     1 
ATOM   7533  C  CA    . GLY B 1 247 ? 129.306 137.282 143.358 1.00 10.12 ?  247 GLY B CA    1 
ATOM   7534  C  C     . GLY B 1 247 ? 127.896 136.816 143.651 1.00 12.49 ?  247 GLY B C     1 
ATOM   7535  O  O     . GLY B 1 247 ? 127.636 135.629 143.848 1.00 22.70 ?  247 GLY B O     1 
ATOM   7536  N  N     . ALA B 1 248 ? 126.983 137.781 143.678 1.00 17.14 ?  248 ALA B N     1 
ATOM   7537  C  CA    . ALA B 1 248 ? 125.582 137.512 143.949 1.00 17.75 ?  248 ALA B CA    1 
ATOM   7538  C  C     . ALA B 1 248 ? 124.719 138.188 142.897 1.00 16.83 ?  248 ALA B C     1 
ATOM   7539  O  O     . ALA B 1 248 ? 125.052 139.261 142.390 1.00 23.25 ?  248 ALA B O     1 
ATOM   7540  C  CB    . ALA B 1 248 ? 125.172 137.992 145.347 1.00 4.65  ?  248 ALA B CB    1 
ATOM   7541  N  N     . ALA B 1 249 ? 123.607 137.540 142.568 1.00 16.18 ?  249 ALA B N     1 
ATOM   7542  C  CA    . ALA B 1 249 ? 122.620 138.079 141.647 1.00 14.30 ?  249 ALA B CA    1 
ATOM   7543  C  C     . ALA B 1 249 ? 121.273 138.121 142.349 1.00 16.37 ?  249 ALA B C     1 
ATOM   7544  O  O     . ALA B 1 249 ? 120.881 137.153 143.005 1.00 24.63 ?  249 ALA B O     1 
ATOM   7545  C  CB    . ALA B 1 249 ? 122.534 137.241 140.371 1.00 11.62 ?  249 ALA B CB    1 
ATOM   7546  N  N     . TYR B 1 250 ? 120.573 139.240 142.219 1.00 17.18 ?  250 TYR B N     1 
ATOM   7547  C  CA    . TYR B 1 250 ? 119.277 139.419 142.849 1.00 5.89  ?  250 TYR B CA    1 
ATOM   7548  C  C     . TYR B 1 250 ? 118.214 139.626 141.784 1.00 7.44  ?  250 TYR B C     1 
ATOM   7549  O  O     . TYR B 1 250 ? 118.423 140.363 140.817 1.00 21.34 ?  250 TYR B O     1 
ATOM   7550  C  CB    . TYR B 1 250 ? 119.287 140.603 143.817 1.00 12.37 ?  250 TYR B CB    1 
ATOM   7551  C  CG    . TYR B 1 250 ? 119.773 140.249 145.201 1.00 15.54 ?  250 TYR B CG    1 
ATOM   7552  C  CD1   . TYR B 1 250 ? 121.117 140.011 145.445 1.00 8.40  ?  250 TYR B CD1   1 
ATOM   7553  C  CD2   . TYR B 1 250 ? 118.885 140.139 146.262 1.00 12.52 ?  250 TYR B CD2   1 
ATOM   7554  C  CE1   . TYR B 1 250 ? 121.565 139.681 146.704 1.00 1.20  ?  250 TYR B CE1   1 
ATOM   7555  C  CE2   . TYR B 1 250 ? 119.325 139.809 147.527 1.00 7.97  ?  250 TYR B CE2   1 
ATOM   7556  C  CZ    . TYR B 1 250 ? 120.667 139.582 147.741 1.00 11.67 ?  250 TYR B CZ    1 
ATOM   7557  O  OH    . TYR B 1 250 ? 121.113 139.257 148.999 1.00 21.15 ?  250 TYR B OH    1 
ATOM   7558  N  N     . LEU B 1 251 ? 117.077 138.963 141.965 1.00 14.84 ?  251 LEU B N     1 
ATOM   7559  C  CA    . LEU B 1 251 ? 115.947 139.104 141.063 1.00 15.67 ?  251 LEU B CA    1 
ATOM   7560  C  C     . LEU B 1 251 ? 114.674 139.252 141.878 1.00 10.15 ?  251 LEU B C     1 
ATOM   7561  O  O     . LEU B 1 251 ? 114.495 138.571 142.890 1.00 19.07 ?  251 LEU B O     1 
ATOM   7562  C  CB    . LEU B 1 251 ? 115.824 137.901 140.122 1.00 14.63 ?  251 LEU B CB    1 
ATOM   7563  C  CG    . LEU B 1 251 ? 114.991 138.131 138.863 1.00 14.48 ?  251 LEU B CG    1 
ATOM   7564  C  CD1   . LEU B 1 251 ? 115.716 139.045 137.900 1.00 6.94  ?  251 LEU B CD1   1 
ATOM   7565  C  CD2   . LEU B 1 251 ? 114.648 136.814 138.202 1.00 10.11 ?  251 LEU B CD2   1 
ATOM   7566  N  N     . ASN B 1 252 ? 113.798 140.148 141.434 1.00 12.31 ?  252 ASN B N     1 
ATOM   7567  C  CA    . ASN B 1 252 ? 112.493 140.283 142.061 1.00 10.56 ?  252 ASN B CA    1 
ATOM   7568  C  C     . ASN B 1 252 ? 111.660 139.033 141.815 1.00 17.18 ?  252 ASN B C     1 
ATOM   7569  O  O     . ASN B 1 252 ? 111.735 138.414 140.751 1.00 27.97 ?  252 ASN B O     1 
ATOM   7570  C  CB    . ASN B 1 252 ? 111.770 141.514 141.521 1.00 13.51 ?  252 ASN B CB    1 
ATOM   7571  C  CG    . ASN B 1 252 ? 110.796 142.100 142.521 1.00 20.90 ?  252 ASN B CG    1 
ATOM   7572  O  OD1   . ASN B 1 252 ? 109.737 141.531 142.779 1.00 31.96 ?  252 ASN B OD1   1 
ATOM   7573  N  ND2   . ASN B 1 252 ? 111.153 143.243 143.092 1.00 16.81 ?  252 ASN B ND2   1 
ATOM   7574  N  N     . ILE B 1 253 ? 110.860 138.654 142.816 1.00 12.04 ?  253 ILE B N     1 
ATOM   7575  C  CA    . ILE B 1 253 ? 110.026 137.468 142.680 1.00 17.59 ?  253 ILE B CA    1 
ATOM   7576  C  C     . ILE B 1 253 ? 108.937 137.657 141.630 1.00 23.32 ?  253 ILE B C     1 
ATOM   7577  O  O     . ILE B 1 253 ? 108.408 136.670 141.108 1.00 24.82 ?  253 ILE B O     1 
ATOM   7578  C  CB    . ILE B 1 253 ? 109.421 137.084 144.045 1.00 20.99 ?  253 ILE B CB    1 
ATOM   7579  C  CG1   . ILE B 1 253 ? 109.017 135.609 144.051 1.00 16.36 ?  253 ILE B CG1   1 
ATOM   7580  C  CG2   . ILE B 1 253 ? 108.247 137.985 144.392 1.00 14.57 ?  253 ILE B CG2   1 
ATOM   7581  C  CD1   . ILE B 1 253 ? 109.152 134.946 145.392 1.00 18.96 ?  253 ILE B CD1   1 
ATOM   7582  N  N     . PHE B 1 254 ? 108.593 138.899 141.296 1.00 30.33 ?  254 PHE B N     1 
ATOM   7583  C  CA    . PHE B 1 254 ? 107.613 139.179 140.258 1.00 18.12 ?  254 PHE B CA    1 
ATOM   7584  C  C     . PHE B 1 254 ? 108.240 139.293 138.876 1.00 20.80 ?  254 PHE B C     1 
ATOM   7585  O  O     . PHE B 1 254 ? 107.523 139.530 137.899 1.00 27.34 ?  254 PHE B O     1 
ATOM   7586  C  CB    . PHE B 1 254 ? 106.840 140.458 140.593 1.00 21.69 ?  254 PHE B CB    1 
ATOM   7587  C  CG    . PHE B 1 254 ? 105.765 140.260 141.622 1.00 26.47 ?  254 PHE B CG    1 
ATOM   7588  C  CD1   . PHE B 1 254 ? 104.668 139.464 141.347 1.00 25.87 ?  254 PHE B CD1   1 
ATOM   7589  C  CD2   . PHE B 1 254 ? 105.855 140.858 142.866 1.00 25.47 ?  254 PHE B CD2   1 
ATOM   7590  C  CE1   . PHE B 1 254 ? 103.678 139.276 142.289 1.00 29.44 ?  254 PHE B CE1   1 
ATOM   7591  C  CE2   . PHE B 1 254 ? 104.868 140.672 143.812 1.00 26.38 ?  254 PHE B CE2   1 
ATOM   7592  C  CZ    . PHE B 1 254 ? 103.778 139.880 143.522 1.00 25.35 ?  254 PHE B CZ    1 
ATOM   7593  N  N     . HIS B 1 255 ? 109.556 139.138 138.776 1.00 27.15 ?  255 HIS B N     1 
ATOM   7594  C  CA    . HIS B 1 255 ? 110.207 139.049 137.479 1.00 20.76 ?  255 HIS B CA    1 
ATOM   7595  C  C     . HIS B 1 255 ? 109.788 137.766 136.776 1.00 23.58 ?  255 HIS B C     1 
ATOM   7596  O  O     . HIS B 1 255 ? 109.606 136.722 137.407 1.00 30.47 ?  255 HIS B O     1 
ATOM   7597  C  CB    . HIS B 1 255 ? 111.725 139.092 137.645 1.00 17.98 ?  255 HIS B CB    1 
ATOM   7598  C  CG    . HIS B 1 255 ? 112.467 139.436 136.391 1.00 22.26 ?  255 HIS B CG    1 
ATOM   7599  N  ND1   . HIS B 1 255 ? 112.653 138.536 135.364 1.00 14.82 ?  255 HIS B ND1   1 
ATOM   7600  C  CD2   . HIS B 1 255 ? 113.083 140.578 136.005 1.00 20.06 ?  255 HIS B CD2   1 
ATOM   7601  C  CE1   . HIS B 1 255 ? 113.344 139.112 134.397 1.00 12.90 ?  255 HIS B CE1   1 
ATOM   7602  N  NE2   . HIS B 1 255 ? 113.621 140.350 134.762 1.00 12.09 ?  255 HIS B NE2   1 
ATOM   7603  N  N     . ARG B 1 256 ? 109.636 137.855 135.456 1.00 26.39 ?  256 ARG B N     1 
ATOM   7604  C  CA    . ARG B 1 256 ? 109.171 136.713 134.681 1.00 22.29 ?  256 ARG B CA    1 
ATOM   7605  C  C     . ARG B 1 256 ? 110.154 135.551 134.751 1.00 24.96 ?  256 ARG B C     1 
ATOM   7606  O  O     . ARG B 1 256 ? 109.749 134.384 134.781 1.00 32.64 ?  256 ARG B O     1 
ATOM   7607  C  CB    . ARG B 1 256 ? 108.939 137.140 133.236 1.00 26.13 ?  256 ARG B CB    1 
ATOM   7608  C  CG    . ARG B 1 256 ? 107.759 136.482 132.581 1.00 35.87 ?  256 ARG B CG    1 
ATOM   7609  C  CD    . ARG B 1 256 ? 108.104 135.099 132.085 1.00 31.95 ?  256 ARG B CD    1 
ATOM   7610  N  NE    . ARG B 1 256 ? 109.481 134.984 131.624 1.00 30.96 ?  256 ARG B NE    1 
ATOM   7611  C  CZ    . ARG B 1 256 ? 110.021 133.858 131.181 1.00 33.29 ?  256 ARG B CZ    1 
ATOM   7612  N  NH1   . ARG B 1 256 ? 109.329 132.731 131.136 1.00 30.55 1  256 ARG B NH1   1 
ATOM   7613  N  NH2   . ARG B 1 256 ? 111.287 133.861 130.776 1.00 34.33 ?  256 ARG B NH2   1 
ATOM   7614  N  N     . ASP B 1 257 ? 111.449 135.850 134.786 1.00 26.22 ?  257 ASP B N     1 
ATOM   7615  C  CA    . ASP B 1 257 ? 112.491 134.834 134.804 1.00 21.49 ?  257 ASP B CA    1 
ATOM   7616  C  C     . ASP B 1 257 ? 112.766 134.277 136.192 1.00 22.72 ?  257 ASP B C     1 
ATOM   7617  O  O     . ASP B 1 257 ? 113.837 133.699 136.396 1.00 27.09 ?  257 ASP B O     1 
ATOM   7618  C  CB    . ASP B 1 257 ? 113.784 135.400 134.219 1.00 25.70 ?  257 ASP B CB    1 
ATOM   7619  C  CG    . ASP B 1 257 ? 113.791 135.396 132.711 1.00 32.76 ?  257 ASP B CG    1 
ATOM   7620  O  OD1   . ASP B 1 257 ? 112.900 134.762 132.111 1.00 31.80 ?  257 ASP B OD1   1 
ATOM   7621  O  OD2   . ASP B 1 257 ? 114.688 136.031 132.126 1.00 36.44 -1 257 ASP B OD2   1 
ATOM   7622  N  N     . ILE B 1 258 ? 111.842 134.429 137.143 1.00 26.47 ?  258 ILE B N     1 
ATOM   7623  C  CA    . ILE B 1 258 ? 112.121 134.014 138.515 1.00 23.00 ?  258 ILE B CA    1 
ATOM   7624  C  C     . ILE B 1 258 ? 112.311 132.503 138.596 1.00 22.75 ?  258 ILE B C     1 
ATOM   7625  O  O     . ILE B 1 258 ? 113.172 132.016 139.336 1.00 34.15 ?  258 ILE B O     1 
ATOM   7626  C  CB    . ILE B 1 258 ? 111.014 134.512 139.463 1.00 27.55 ?  258 ILE B CB    1 
ATOM   7627  C  CG1   . ILE B 1 258 ? 111.357 134.169 140.916 1.00 24.90 ?  258 ILE B CG1   1 
ATOM   7628  C  CG2   . ILE B 1 258 ? 109.652 133.958 139.066 1.00 19.92 ?  258 ILE B CG2   1 
ATOM   7629  C  CD1   . ILE B 1 258 ? 112.662 134.768 141.387 1.00 17.22 ?  258 ILE B CD1   1 
ATOM   7630  N  N     . ASN B 1 259 ? 111.530 131.738 137.831 1.00 31.64 ?  259 ASN B N     1 
ATOM   7631  C  CA    . ASN B 1 259 ? 111.671 130.285 137.869 1.00 28.34 ?  259 ASN B CA    1 
ATOM   7632  C  C     . ASN B 1 259 ? 112.970 129.840 137.208 1.00 28.53 ?  259 ASN B C     1 
ATOM   7633  O  O     . ASN B 1 259 ? 113.654 128.946 137.714 1.00 30.84 ?  259 ASN B O     1 
ATOM   7634  C  CB    . ASN B 1 259 ? 110.466 129.621 137.206 1.00 29.00 ?  259 ASN B CB    1 
ATOM   7635  C  CG    . ASN B 1 259 ? 109.260 129.570 138.120 1.00 33.29 ?  259 ASN B CG    1 
ATOM   7636  O  OD1   . ASN B 1 259 ? 109.315 128.999 139.208 1.00 34.36 ?  259 ASN B OD1   1 
ATOM   7637  N  ND2   . ASN B 1 259 ? 108.160 130.169 137.682 1.00 34.97 ?  259 ASN B ND2   1 
ATOM   7638  N  N     . ASP B 1 260 ? 113.328 130.457 136.080 1.00 31.47 ?  260 ASP B N     1 
ATOM   7639  C  CA    . ASP B 1 260 ? 114.634 130.205 135.480 1.00 24.64 ?  260 ASP B CA    1 
ATOM   7640  C  C     . ASP B 1 260 ? 115.754 130.641 136.414 1.00 28.75 ?  260 ASP B C     1 
ATOM   7641  O  O     . ASP B 1 260 ? 116.793 129.976 136.509 1.00 33.75 ?  260 ASP B O     1 
ATOM   7642  C  CB    . ASP B 1 260 ? 114.743 130.928 134.140 1.00 27.87 ?  260 ASP B CB    1 
ATOM   7643  C  CG    . ASP B 1 260 ? 113.663 130.514 133.164 1.00 40.56 ?  260 ASP B CG    1 
ATOM   7644  O  OD1   . ASP B 1 260 ? 113.568 131.133 132.084 1.00 37.76 ?  260 ASP B OD1   1 
ATOM   7645  O  OD2   . ASP B 1 260 ? 112.907 129.569 133.478 1.00 42.90 -1 260 ASP B OD2   1 
ATOM   7646  N  N     . PHE B 1 261 ? 115.561 131.768 137.102 1.00 33.42 ?  261 PHE B N     1 
ATOM   7647  C  CA    . PHE B 1 261 ? 116.538 132.249 138.073 1.00 20.73 ?  261 PHE B CA    1 
ATOM   7648  C  C     . PHE B 1 261 ? 116.775 131.221 139.172 1.00 23.47 ?  261 PHE B C     1 
ATOM   7649  O  O     . PHE B 1 261 ? 117.918 130.983 139.578 1.00 26.79 ?  261 PHE B O     1 
ATOM   7650  C  CB    . PHE B 1 261 ? 116.043 133.570 138.661 1.00 14.21 ?  261 PHE B CB    1 
ATOM   7651  C  CG    . PHE B 1 261 ? 117.021 134.252 139.570 1.00 27.64 ?  261 PHE B CG    1 
ATOM   7652  C  CD1   . PHE B 1 261 ? 118.101 134.939 139.052 1.00 22.13 ?  261 PHE B CD1   1 
ATOM   7653  C  CD2   . PHE B 1 261 ? 116.836 134.240 140.940 1.00 21.15 ?  261 PHE B CD2   1 
ATOM   7654  C  CE1   . PHE B 1 261 ? 118.992 135.578 139.882 1.00 14.29 ?  261 PHE B CE1   1 
ATOM   7655  C  CE2   . PHE B 1 261 ? 117.724 134.879 141.775 1.00 12.58 ?  261 PHE B CE2   1 
ATOM   7656  C  CZ    . PHE B 1 261 ? 118.803 135.548 141.244 1.00 17.93 ?  261 PHE B CZ    1 
ATOM   7657  N  N     . LEU B 1 262 ? 115.702 130.599 139.665 1.00 31.41 ?  262 LEU B N     1 
ATOM   7658  C  CA    . LEU B 1 262 ? 115.834 129.610 140.728 1.00 25.47 ?  262 LEU B CA    1 
ATOM   7659  C  C     . LEU B 1 262 ? 116.378 128.285 140.214 1.00 30.04 ?  262 LEU B C     1 
ATOM   7660  O  O     . LEU B 1 262 ? 117.071 127.577 140.953 1.00 32.42 ?  262 LEU B O     1 
ATOM   7661  C  CB    . LEU B 1 262 ? 114.485 129.397 141.408 1.00 32.20 ?  262 LEU B CB    1 
ATOM   7662  C  CG    . LEU B 1 262 ? 113.852 130.637 142.033 1.00 22.35 ?  262 LEU B CG    1 
ATOM   7663  C  CD1   . LEU B 1 262 ? 112.477 130.312 142.581 1.00 29.16 ?  262 LEU B CD1   1 
ATOM   7664  C  CD2   . LEU B 1 262 ? 114.755 131.194 143.111 1.00 22.81 ?  262 LEU B CD2   1 
ATOM   7665  N  N     . ASP B 1 263 ? 116.082 127.929 138.963 1.00 42.45 ?  263 ASP B N     1 
ATOM   7666  C  CA    . ASP B 1 263 ? 116.537 126.657 138.413 1.00 31.66 ?  263 ASP B CA    1 
ATOM   7667  C  C     . ASP B 1 263 ? 118.047 126.593 138.237 1.00 34.41 ?  263 ASP B C     1 
ATOM   7668  O  O     . ASP B 1 263 ? 118.580 125.499 138.030 1.00 47.73 ?  263 ASP B O     1 
ATOM   7669  C  CB    . ASP B 1 263 ? 115.857 126.387 137.071 1.00 37.05 ?  263 ASP B CB    1 
ATOM   7670  C  CG    . ASP B 1 263 ? 114.378 126.103 137.215 1.00 46.24 ?  263 ASP B CG    1 
ATOM   7671  O  OD1   . ASP B 1 263 ? 113.920 125.889 138.355 1.00 42.48 ?  263 ASP B OD1   1 
ATOM   7672  O  OD2   . ASP B 1 263 ? 113.670 126.097 136.185 1.00 47.80 -1 263 ASP B OD2   1 
ATOM   7673  N  N     . THR B 1 264 ? 118.745 127.727 138.306 1.00 38.94 ?  264 THR B N     1 
ATOM   7674  C  CA    . THR B 1 264 ? 120.198 127.723 138.207 1.00 37.20 ?  264 THR B CA    1 
ATOM   7675  C  C     . THR B 1 264 ? 120.872 127.103 139.424 1.00 40.49 ?  264 THR B C     1 
ATOM   7676  O  O     . THR B 1 264 ? 122.069 126.808 139.362 1.00 41.51 ?  264 THR B O     1 
ATOM   7677  C  CB    . THR B 1 264 ? 120.717 129.149 138.006 1.00 34.86 ?  264 THR B CB    1 
ATOM   7678  O  OG1   . THR B 1 264 ? 120.331 129.963 139.120 1.00 37.84 ?  264 THR B OG1   1 
ATOM   7679  C  CG2   . THR B 1 264 ? 120.150 129.746 136.732 1.00 35.27 ?  264 THR B CG2   1 
ATOM   7680  N  N     . LYS B 1 265 ? 120.139 126.895 140.517 1.00 34.45 ?  265 LYS B N     1 
ATOM   7681  C  CA    . LYS B 1 265 ? 120.699 126.338 141.740 1.00 36.43 ?  265 LYS B CA    1 
ATOM   7682  C  C     . LYS B 1 265 ? 120.253 124.910 142.014 1.00 41.95 ?  265 LYS B C     1 
ATOM   7683  O  O     . LYS B 1 265 ? 120.643 124.344 143.041 1.00 44.94 ?  265 LYS B O     1 
ATOM   7684  C  CB    . LYS B 1 265 ? 120.340 127.227 142.934 1.00 35.53 ?  265 LYS B CB    1 
ATOM   7685  C  CG    . LYS B 1 265 ? 121.155 128.497 143.014 1.00 38.41 ?  265 LYS B CG    1 
ATOM   7686  C  CD    . LYS B 1 265 ? 122.633 128.193 142.905 1.00 42.43 ?  265 LYS B CD    1 
ATOM   7687  C  CE    . LYS B 1 265 ? 123.447 129.463 142.858 1.00 39.18 ?  265 LYS B CE    1 
ATOM   7688  N  NZ    . LYS B 1 265 ? 124.870 129.188 142.535 1.00 43.31 1  265 LYS B NZ    1 
ATOM   7689  N  N     . LYS B 1 266 ? 119.451 124.314 141.140 1.00 46.48 ?  266 LYS B N     1 
ATOM   7690  C  CA    . LYS B 1 266 ? 119.052 122.927 141.327 1.00 48.96 ?  266 LYS B CA    1 
ATOM   7691  C  C     . LYS B 1 266 ? 120.237 121.995 141.104 1.00 55.08 ?  266 LYS B C     1 
ATOM   7692  O  O     . LYS B 1 266 ? 121.127 122.268 140.295 1.00 56.31 ?  266 LYS B O     1 
ATOM   7693  C  CB    . LYS B 1 266 ? 117.910 122.565 140.380 1.00 48.89 ?  266 LYS B CB    1 
ATOM   7694  C  CG    . LYS B 1 266 ? 116.556 123.096 140.811 1.00 50.80 ?  266 LYS B CG    1 
ATOM   7695  C  CD    . LYS B 1 266 ? 115.487 122.776 139.782 1.00 51.90 ?  266 LYS B CD    1 
ATOM   7696  C  CE    . LYS B 1 266 ? 114.102 123.140 140.291 1.00 50.94 ?  266 LYS B CE    1 
ATOM   7697  N  NZ    . LYS B 1 266 ? 113.076 123.054 139.215 1.00 50.51 1  266 LYS B NZ    1 
ATOM   7698  N  N     . ILE B 1 267 ? 120.247 120.886 141.846 1.00 58.24 ?  267 ILE B N     1 
ATOM   7699  C  CA    . ILE B 1 267 ? 121.328 119.916 141.708 1.00 60.88 ?  267 ILE B CA    1 
ATOM   7700  C  C     . ILE B 1 267 ? 121.284 119.251 140.339 1.00 62.41 ?  267 ILE B C     1 
ATOM   7701  O  O     . ILE B 1 267 ? 122.321 118.836 139.807 1.00 61.60 ?  267 ILE B O     1 
ATOM   7702  C  CB    . ILE B 1 267 ? 121.271 118.873 142.840 1.00 62.07 ?  267 ILE B CB    1 
ATOM   7703  C  CG1   . ILE B 1 267 ? 121.529 119.529 144.199 1.00 61.89 ?  267 ILE B CG1   1 
ATOM   7704  C  CG2   . ILE B 1 267 ? 122.277 117.762 142.592 1.00 58.67 ?  267 ILE B CG2   1 
ATOM   7705  C  CD1   . ILE B 1 267 ? 120.271 119.808 144.997 1.00 60.76 ?  267 ILE B CD1   1 
ATOM   7706  N  N     . SER B 1 268 ? 120.097 119.137 139.748 1.00 63.05 ?  268 SER B N     1 
ATOM   7707  C  CA    . SER B 1 268 ? 119.918 118.534 138.436 1.00 64.65 ?  268 SER B CA    1 
ATOM   7708  C  C     . SER B 1 268 ? 120.005 119.548 137.302 1.00 65.97 ?  268 SER B C     1 
ATOM   7709  O  O     . SER B 1 268 ? 119.639 119.222 136.169 1.00 65.58 ?  268 SER B O     1 
ATOM   7710  C  CB    . SER B 1 268 ? 118.573 117.806 138.373 1.00 66.48 ?  268 SER B CB    1 
ATOM   7711  O  OG    . SER B 1 268 ? 117.513 118.675 138.734 1.00 61.93 ?  268 SER B OG    1 
ATOM   7712  N  N     . ALA B 1 269 ? 120.469 120.764 137.583 1.00 70.03 ?  269 ALA B N     1 
ATOM   7713  C  CA    . ALA B 1 269 ? 120.486 121.811 136.571 1.00 70.26 ?  269 ALA B CA    1 
ATOM   7714  C  C     . ALA B 1 269 ? 121.443 121.465 135.437 1.00 71.13 ?  269 ALA B C     1 
ATOM   7715  O  O     . ALA B 1 269 ? 122.529 120.920 135.660 1.00 68.97 ?  269 ALA B O     1 
ATOM   7716  C  CB    . ALA B 1 269 ? 120.879 123.148 137.199 1.00 66.54 ?  269 ALA B CB    1 
ATOM   7717  N  N     . ASP B 1 270 ? 121.028 121.783 134.215 1.00 74.02 ?  270 ASP B N     1 
ATOM   7718  C  CA    . ASP B 1 270 ? 121.873 121.576 133.049 1.00 74.33 ?  270 ASP B CA    1 
ATOM   7719  C  C     . ASP B 1 270 ? 123.088 122.497 133.103 1.00 73.93 ?  270 ASP B C     1 
ATOM   7720  O  O     . ASP B 1 270 ? 123.042 123.592 133.670 1.00 75.43 ?  270 ASP B O     1 
ATOM   7721  C  CB    . ASP B 1 270 ? 121.080 121.824 131.767 1.00 73.65 ?  270 ASP B CB    1 
ATOM   7722  C  CG    . ASP B 1 270 ? 121.686 121.135 130.560 1.00 76.84 ?  270 ASP B CG    1 
ATOM   7723  O  OD1   . ASP B 1 270 ? 122.872 121.386 130.259 1.00 75.94 ?  270 ASP B OD1   1 
ATOM   7724  O  OD2   . ASP B 1 270 ? 120.974 120.342 129.907 1.00 75.61 -1 270 ASP B OD2   1 
ATOM   7725  N  N     . GLU B 1 271 ? 124.189 122.038 132.503 1.00 74.27 ?  271 GLU B N     1 
ATOM   7726  C  CA    . GLU B 1 271 ? 125.429 122.806 132.536 1.00 75.67 ?  271 GLU B CA    1 
ATOM   7727  C  C     . GLU B 1 271 ? 125.328 124.117 131.766 1.00 73.53 ?  271 GLU B C     1 
ATOM   7728  O  O     . GLU B 1 271 ? 126.132 125.023 132.008 1.00 73.03 ?  271 GLU B O     1 
ATOM   7729  C  CB    . GLU B 1 271 ? 126.583 121.967 131.987 1.00 73.87 ?  271 GLU B CB    1 
ATOM   7730  C  CG    . GLU B 1 271 ? 126.997 120.821 132.896 1.00 73.21 ?  271 GLU B CG    1 
ATOM   7731  C  CD    . GLU B 1 271 ? 127.531 121.299 134.232 1.00 75.05 ?  271 GLU B CD    1 
ATOM   7732  O  OE1   . GLU B 1 271 ? 128.232 122.332 134.260 1.00 75.43 ?  271 GLU B OE1   1 
ATOM   7733  O  OE2   . GLU B 1 271 ? 127.248 120.642 135.256 1.00 74.89 -1 271 GLU B OE2   1 
ATOM   7734  N  N     . ASP B 1 272 ? 124.372 124.241 130.848 1.00 69.75 ?  272 ASP B N     1 
ATOM   7735  C  CA    . ASP B 1 272 ? 124.129 125.503 130.162 1.00 71.73 ?  272 ASP B CA    1 
ATOM   7736  C  C     . ASP B 1 272 ? 123.175 126.409 130.929 1.00 70.44 ?  272 ASP B C     1 
ATOM   7737  O  O     . ASP B 1 272 ? 122.876 127.511 130.459 1.00 66.88 ?  272 ASP B O     1 
ATOM   7738  C  CB    . ASP B 1 272 ? 123.591 125.248 128.747 1.00 70.85 ?  272 ASP B CB    1 
ATOM   7739  C  CG    . ASP B 1 272 ? 122.137 124.811 128.738 1.00 73.30 ?  272 ASP B CG    1 
ATOM   7740  O  OD1   . ASP B 1 272 ? 121.693 124.171 129.712 1.00 72.91 ?  272 ASP B OD1   1 
ATOM   7741  O  OD2   . ASP B 1 272 ? 121.436 125.109 127.747 1.00 70.51 -1 272 ASP B OD2   1 
ATOM   7742  N  N     . VAL B 1 273 ? 122.678 125.961 132.083 1.00 66.23 ?  273 VAL B N     1 
ATOM   7743  C  CA    . VAL B 1 273 ? 121.831 126.767 132.950 1.00 66.52 ?  273 VAL B CA    1 
ATOM   7744  C  C     . VAL B 1 273 ? 122.473 126.994 134.313 1.00 64.95 ?  273 VAL B C     1 
ATOM   7745  O  O     . VAL B 1 273 ? 122.384 128.093 134.872 1.00 66.14 ?  273 VAL B O     1 
ATOM   7746  C  CB    . VAL B 1 273 ? 120.435 126.127 133.109 1.00 68.18 ?  273 VAL B CB    1 
ATOM   7747  C  CG1   . VAL B 1 273 ? 119.564 126.958 134.042 1.00 62.76 ?  273 VAL B CG1   1 
ATOM   7748  C  CG2   . VAL B 1 273 ? 119.769 125.962 131.753 1.00 65.62 ?  273 VAL B CG2   1 
ATOM   7749  N  N     . ARG B 1 274 ? 123.132 125.973 134.858 1.00 62.96 ?  274 ARG B N     1 
ATOM   7750  C  CA    . ARG B 1 274 ? 123.680 126.048 136.205 1.00 61.76 ?  274 ARG B CA    1 
ATOM   7751  C  C     . ARG B 1 274 ? 124.784 127.097 136.297 1.00 62.60 ?  274 ARG B C     1 
ATOM   7752  O  O     . ARG B 1 274 ? 125.619 127.229 135.399 1.00 62.96 ?  274 ARG B O     1 
ATOM   7753  C  CB    . ARG B 1 274 ? 124.222 124.678 136.620 1.00 65.11 ?  274 ARG B CB    1 
ATOM   7754  C  CG    . ARG B 1 274 ? 125.366 124.721 137.620 1.00 62.82 ?  274 ARG B CG    1 
ATOM   7755  C  CD    . ARG B 1 274 ? 125.390 123.481 138.498 1.00 63.74 ?  274 ARG B CD    1 
ATOM   7756  N  NE    . ARG B 1 274 ? 125.797 122.295 137.754 1.00 66.77 ?  274 ARG B NE    1 
ATOM   7757  C  CZ    . ARG B 1 274 ? 125.019 121.244 137.532 1.00 68.61 ?  274 ARG B CZ    1 
ATOM   7758  N  NH1   . ARG B 1 274 ? 123.779 121.194 137.990 1.00 67.06 1  274 ARG B NH1   1 
ATOM   7759  N  NH2   . ARG B 1 274 ? 125.497 120.218 136.833 1.00 66.55 ?  274 ARG B NH2   1 
ATOM   7760  N  N     . VAL B 1 275 ? 124.775 127.847 137.397 1.00 49.50 ?  275 VAL B N     1 
ATOM   7761  C  CA    . VAL B 1 275 ? 125.839 128.782 137.743 1.00 46.65 ?  275 VAL B CA    1 
ATOM   7762  C  C     . VAL B 1 275 ? 126.474 128.306 139.043 1.00 49.29 ?  275 VAL B C     1 
ATOM   7763  O  O     . VAL B 1 275 ? 125.774 127.857 139.958 1.00 54.55 ?  275 VAL B O     1 
ATOM   7764  C  CB    . VAL B 1 275 ? 125.319 130.228 137.872 1.00 45.30 ?  275 VAL B CB    1 
ATOM   7765  C  CG1   . VAL B 1 275 ? 124.933 130.775 136.508 1.00 41.64 ?  275 VAL B CG1   1 
ATOM   7766  C  CG2   . VAL B 1 275 ? 124.136 130.291 138.820 1.00 48.00 ?  275 VAL B CG2   1 
ATOM   7767  N  N     . LYS B 1 276 ? 127.801 128.385 139.116 1.00 43.13 ?  276 LYS B N     1 
ATOM   7768  C  CA    . LYS B 1 276 ? 128.554 127.798 140.220 1.00 44.19 ?  276 LYS B CA    1 
ATOM   7769  C  C     . LYS B 1 276 ? 129.002 128.825 141.252 1.00 42.13 ?  276 LYS B C     1 
ATOM   7770  O  O     . LYS B 1 276 ? 128.819 128.612 142.454 1.00 48.13 ?  276 LYS B O     1 
ATOM   7771  C  CB    . LYS B 1 276 ? 129.783 127.032 139.696 1.00 45.94 ?  276 LYS B CB    1 
ATOM   7772  C  CG    . LYS B 1 276 ? 129.502 125.705 138.973 1.00 47.42 ?  276 LYS B CG    1 
ATOM   7773  C  CD    . LYS B 1 276 ? 128.852 125.836 137.593 1.00 48.40 ?  276 LYS B CD    1 
ATOM   7774  C  CE    . LYS B 1 276 ? 129.376 127.030 136.807 1.00 45.33 ?  276 LYS B CE    1 
ATOM   7775  N  NZ    . LYS B 1 276 ? 129.056 126.914 135.357 1.00 49.22 1  276 LYS B NZ    1 
ATOM   7776  N  N     . THR B 1 277 ? 129.590 129.933 140.812 1.00 38.02 ?  277 THR B N     1 
ATOM   7777  C  CA    . THR B 1 277 ? 130.165 130.922 141.713 1.00 39.22 ?  277 THR B CA    1 
ATOM   7778  C  C     . THR B 1 277 ? 129.266 132.131 141.920 1.00 38.73 ?  277 THR B C     1 
ATOM   7779  O  O     . THR B 1 277 ? 129.722 133.143 142.463 1.00 39.15 ?  277 THR B O     1 
ATOM   7780  C  CB    . THR B 1 277 ? 131.530 131.377 141.194 1.00 41.69 ?  277 THR B CB    1 
ATOM   7781  O  OG1   . THR B 1 277 ? 131.350 132.247 140.068 1.00 33.70 ?  277 THR B OG1   1 
ATOM   7782  C  CG2   . THR B 1 277 ? 132.363 130.177 140.781 1.00 39.64 ?  277 THR B CG2   1 
ATOM   7783  N  N     . LEU B 1 278 ? 128.005 132.054 141.505 1.00 34.18 ?  278 LEU B N     1 
ATOM   7784  C  CA    . LEU B 1 278 ? 127.076 133.176 141.583 1.00 28.24 ?  278 LEU B CA    1 
ATOM   7785  C  C     . LEU B 1 278 ? 125.963 132.824 142.561 1.00 24.52 ?  278 LEU B C     1 
ATOM   7786  O  O     . LEU B 1 278 ? 125.072 132.036 142.233 1.00 36.61 ?  278 LEU B O     1 
ATOM   7787  C  CB    . LEU B 1 278 ? 126.509 133.508 140.205 1.00 30.67 ?  278 LEU B CB    1 
ATOM   7788  C  CG    . LEU B 1 278 ? 125.980 134.926 139.995 1.00 28.70 ?  278 LEU B CG    1 
ATOM   7789  C  CD1   . LEU B 1 278 ? 127.123 135.895 139.787 1.00 24.89 ?  278 LEU B CD1   1 
ATOM   7790  C  CD2   . LEU B 1 278 ? 125.028 134.966 138.816 1.00 27.96 ?  278 LEU B CD2   1 
ATOM   7791  N  N     . SER B 1 279 ? 126.019 133.404 143.755 1.00 24.89 ?  279 SER B N     1 
ATOM   7792  C  CA    . SER B 1 279 ? 124.920 133.279 144.700 1.00 17.98 ?  279 SER B CA    1 
ATOM   7793  C  C     . SER B 1 279 ? 123.697 134.016 144.170 1.00 21.42 ?  279 SER B C     1 
ATOM   7794  O  O     . SER B 1 279 ? 123.806 134.958 143.383 1.00 30.82 ?  279 SER B O     1 
ATOM   7795  C  CB    . SER B 1 279 ? 125.318 133.840 146.062 1.00 18.46 ?  279 SER B CB    1 
ATOM   7796  O  OG    . SER B 1 279 ? 126.503 133.231 146.538 1.00 31.78 ?  279 SER B OG    1 
ATOM   7797  N  N     . ILE B 1 280 ? 122.520 133.575 144.599 1.00 19.86 ?  280 ILE B N     1 
ATOM   7798  C  CA    . ILE B 1 280 ? 121.269 134.157 144.136 1.00 20.27 ?  280 ILE B CA    1 
ATOM   7799  C  C     . ILE B 1 280 ? 120.458 134.620 145.334 1.00 12.37 ?  280 ILE B C     1 
ATOM   7800  O  O     . ILE B 1 280 ? 120.437 133.962 146.379 1.00 25.03 ?  280 ILE B O     1 
ATOM   7801  C  CB    . ILE B 1 280 ? 120.457 133.174 143.265 1.00 15.42 ?  280 ILE B CB    1 
ATOM   7802  C  CG1   . ILE B 1 280 ? 120.089 131.909 144.039 1.00 21.88 ?  280 ILE B CG1   1 
ATOM   7803  C  CG2   . ILE B 1 280 ? 121.230 132.812 142.024 1.00 16.03 ?  280 ILE B CG2   1 
ATOM   7804  C  CD1   . ILE B 1 280 ? 118.864 131.215 143.490 1.00 15.40 ?  280 ILE B CD1   1 
ATOM   7805  N  N     . GLY B 1 281 ? 119.823 135.768 145.189 1.00 6.93  ?  281 GLY B N     1 
ATOM   7806  C  CA    . GLY B 1 281 ? 118.890 136.257 146.189 1.00 6.77  ?  281 GLY B CA    1 
ATOM   7807  C  C     . GLY B 1 281 ? 117.597 136.677 145.531 1.00 4.21  ?  281 GLY B C     1 
ATOM   7808  O  O     . GLY B 1 281 ? 117.599 137.251 144.445 1.00 20.89 ?  281 GLY B O     1 
ATOM   7809  N  N     . VAL B 1 282 ? 116.488 136.378 146.198 1.00 13.07 ?  282 VAL B N     1 
ATOM   7810  C  CA    . VAL B 1 282 ? 115.158 136.697 145.696 1.00 16.12 ?  282 VAL B CA    1 
ATOM   7811  C  C     . VAL B 1 282 ? 114.588 137.834 146.531 1.00 12.86 ?  282 VAL B C     1 
ATOM   7812  O  O     . VAL B 1 282 ? 114.619 137.786 147.765 1.00 21.68 ?  282 VAL B O     1 
ATOM   7813  C  CB    . VAL B 1 282 ? 114.233 135.469 145.721 1.00 16.31 ?  282 VAL B CB    1 
ATOM   7814  C  CG1   . VAL B 1 282 ? 112.795 135.879 145.479 1.00 20.40 ?  282 VAL B CG1   1 
ATOM   7815  C  CG2   . VAL B 1 282 ? 114.669 134.477 144.668 1.00 22.87 ?  282 VAL B CG2   1 
ATOM   7816  N  N     . VAL B 1 283 ? 114.083 138.859 145.854 1.00 2.61  ?  283 VAL B N     1 
ATOM   7817  C  CA    . VAL B 1 283 ? 113.434 139.992 146.497 1.00 9.73  ?  283 VAL B CA    1 
ATOM   7818  C  C     . VAL B 1 283 ? 111.932 139.759 146.465 1.00 12.01 ?  283 VAL B C     1 
ATOM   7819  O  O     . VAL B 1 283 ? 111.350 139.553 145.394 1.00 22.77 ?  283 VAL B O     1 
ATOM   7820  C  CB    . VAL B 1 283 ? 113.807 141.311 145.802 1.00 8.36  ?  283 VAL B CB    1 
ATOM   7821  C  CG1   . VAL B 1 283 ? 113.359 142.487 146.638 1.00 10.05 ?  283 VAL B CG1   1 
ATOM   7822  C  CG2   . VAL B 1 283 ? 115.303 141.364 145.555 1.00 9.21  ?  283 VAL B CG2   1 
ATOM   7823  N  N     . ILE B 1 284 ? 111.305 139.784 147.636 1.00 16.01 ?  284 ILE B N     1 
ATOM   7824  C  CA    . ILE B 1 284 ? 109.886 139.465 147.755 1.00 17.63 ?  284 ILE B CA    1 
ATOM   7825  C  C     . ILE B 1 284 ? 109.128 140.659 148.320 1.00 21.20 ?  284 ILE B C     1 
ATOM   7826  O  O     . ILE B 1 284 ? 109.285 140.989 149.505 1.00 24.03 ?  284 ILE B O     1 
ATOM   7827  C  CB    . ILE B 1 284 ? 109.668 138.220 148.629 1.00 14.12 ?  284 ILE B CB    1 
ATOM   7828  C  CG1   . ILE B 1 284 ? 110.515 137.055 148.119 1.00 17.29 ?  284 ILE B CG1   1 
ATOM   7829  C  CG2   . ILE B 1 284 ? 108.198 137.842 148.657 1.00 15.92 ?  284 ILE B CG2   1 
ATOM   7830  C  CD1   . ILE B 1 284 ? 110.288 135.767 148.865 1.00 20.09 ?  284 ILE B CD1   1 
ATOM   7831  N  N     . PRO B 1 285 ? 108.309 141.336 147.522 1.00 20.06 ?  285 PRO B N     1 
ATOM   7832  C  CA    . PRO B 1 285 ? 107.429 142.370 148.073 1.00 29.69 ?  285 PRO B CA    1 
ATOM   7833  C  C     . PRO B 1 285 ? 106.300 141.757 148.884 1.00 28.16 ?  285 PRO B C     1 
ATOM   7834  O  O     . PRO B 1 285 ? 106.029 140.555 148.823 1.00 23.12 ?  285 PRO B O     1 
ATOM   7835  C  CB    . PRO B 1 285 ? 106.890 143.085 146.829 1.00 22.68 ?  285 PRO B CB    1 
ATOM   7836  C  CG    . PRO B 1 285 ? 107.811 142.696 145.721 1.00 20.66 ?  285 PRO B CG    1 
ATOM   7837  C  CD    . PRO B 1 285 ? 108.288 141.323 146.052 1.00 14.72 ?  285 PRO B CD    1 
ATOM   7838  N  N     . ASP B 1 286 ? 105.636 142.611 149.666 1.00 31.68 ?  286 ASP B N     1 
ATOM   7839  C  CA    . ASP B 1 286 ? 104.491 142.160 150.450 1.00 25.85 ?  286 ASP B CA    1 
ATOM   7840  C  C     . ASP B 1 286 ? 103.352 141.667 149.570 1.00 32.58 ?  286 ASP B C     1 
ATOM   7841  O  O     . ASP B 1 286 ? 102.521 140.880 150.035 1.00 36.13 ?  286 ASP B O     1 
ATOM   7842  C  CB    . ASP B 1 286 ? 103.988 143.284 151.354 1.00 27.89 ?  286 ASP B CB    1 
ATOM   7843  C  CG    . ASP B 1 286 ? 104.565 143.214 152.751 1.00 42.45 ?  286 ASP B CG    1 
ATOM   7844  O  OD1   . ASP B 1 286 ? 105.473 142.389 152.982 1.00 38.68 ?  286 ASP B OD1   1 
ATOM   7845  O  OD2   . ASP B 1 286 ? 104.116 143.989 153.620 1.00 45.98 -1 286 ASP B OD2   1 
ATOM   7846  N  N     . LYS B 1 287 ? 103.292 142.120 148.315 1.00 35.56 ?  287 LYS B N     1 
ATOM   7847  C  CA    . LYS B 1 287 ? 102.233 141.680 147.414 1.00 29.84 ?  287 LYS B CA    1 
ATOM   7848  C  C     . LYS B 1 287 ? 102.308 140.181 147.159 1.00 31.94 ?  287 LYS B C     1 
ATOM   7849  O  O     . LYS B 1 287 ? 101.278 139.500 147.118 1.00 37.47 ?  287 LYS B O     1 
ATOM   7850  C  CB    . LYS B 1 287 ? 102.314 142.451 146.096 1.00 29.52 ?  287 LYS B CB    1 
ATOM   7851  C  CG    . LYS B 1 287 ? 101.076 142.315 145.227 1.00 27.75 ?  287 LYS B CG    1 
ATOM   7852  C  CD    . LYS B 1 287 ? 99.834  142.727 145.994 1.00 34.61 ?  287 LYS B CD    1 
ATOM   7853  C  CE    . LYS B 1 287 ? 98.610  142.739 145.102 1.00 35.33 ?  287 LYS B CE    1 
ATOM   7854  N  NZ    . LYS B 1 287 ? 97.446  143.375 145.775 1.00 36.98 1  287 LYS B NZ    1 
ATOM   7855  N  N     . PHE B 1 288 ? 103.518 139.648 146.978 1.00 31.64 ?  288 PHE B N     1 
ATOM   7856  C  CA    . PHE B 1 288 ? 103.664 138.214 146.746 1.00 25.08 ?  288 PHE B CA    1 
ATOM   7857  C  C     . PHE B 1 288 ? 103.223 137.409 147.961 1.00 26.26 ?  288 PHE B C     1 
ATOM   7858  O  O     . PHE B 1 288 ? 102.553 136.378 147.820 1.00 36.76 ?  288 PHE B O     1 
ATOM   7859  C  CB    . PHE B 1 288 ? 105.110 137.887 146.383 1.00 26.32 ?  288 PHE B CB    1 
ATOM   7860  C  CG    . PHE B 1 288 ? 105.312 136.473 145.925 1.00 26.81 ?  288 PHE B CG    1 
ATOM   7861  C  CD1   . PHE B 1 288 ? 105.600 135.472 146.834 1.00 23.51 ?  288 PHE B CD1   1 
ATOM   7862  C  CD2   . PHE B 1 288 ? 105.209 136.146 144.586 1.00 24.59 ?  288 PHE B CD2   1 
ATOM   7863  C  CE1   . PHE B 1 288 ? 105.783 134.173 146.417 1.00 23.18 ?  288 PHE B CE1   1 
ATOM   7864  C  CE2   . PHE B 1 288 ? 105.394 134.849 144.162 1.00 30.28 ?  288 PHE B CE2   1 
ATOM   7865  C  CZ    . PHE B 1 288 ? 105.681 133.861 145.080 1.00 29.49 ?  288 PHE B CZ    1 
ATOM   7866  N  N     . VAL B 1 289 ? 103.596 137.855 149.160 1.00 33.44 ?  289 VAL B N     1 
ATOM   7867  C  CA    . VAL B 1 289 ? 103.197 137.148 150.370 1.00 30.03 ?  289 VAL B CA    1 
ATOM   7868  C  C     . VAL B 1 289 ? 101.688 137.226 150.556 1.00 32.62 ?  289 VAL B C     1 
ATOM   7869  O  O     . VAL B 1 289 ? 101.057 136.272 151.021 1.00 35.56 ?  289 VAL B O     1 
ATOM   7870  C  CB    . VAL B 1 289 ? 103.956 137.705 151.588 1.00 32.52 ?  289 VAL B CB    1 
ATOM   7871  C  CG1   . VAL B 1 289 ? 103.550 136.969 152.853 1.00 31.58 ?  289 VAL B CG1   1 
ATOM   7872  C  CG2   . VAL B 1 289 ? 105.454 137.602 151.365 1.00 25.79 ?  289 VAL B CG2   1 
ATOM   7873  N  N     . GLU B 1 290 ? 101.085 138.360 150.196 1.00 36.62 ?  290 GLU B N     1 
ATOM   7874  C  CA    . GLU B 1 290 ? 99.635  138.486 150.277 1.00 33.24 ?  290 GLU B CA    1 
ATOM   7875  C  C     . GLU B 1 290 ? 98.940  137.559 149.287 1.00 37.81 ?  290 GLU B C     1 
ATOM   7876  O  O     . GLU B 1 290 ? 97.914  136.950 149.613 1.00 45.39 ?  290 GLU B O     1 
ATOM   7877  C  CB    . GLU B 1 290 ? 99.225  139.938 150.037 1.00 36.09 ?  290 GLU B CB    1 
ATOM   7878  C  CG    . GLU B 1 290 ? 97.727  140.178 150.060 1.00 39.32 ?  290 GLU B CG    1 
ATOM   7879  C  CD    . GLU B 1 290 ? 97.373  141.650 149.993 1.00 48.27 ?  290 GLU B CD    1 
ATOM   7880  O  OE1   . GLU B 1 290 ? 97.816  142.326 149.040 1.00 46.35 ?  290 GLU B OE1   1 
ATOM   7881  O  OE2   . GLU B 1 290 ? 96.650  142.132 150.890 1.00 49.09 -1 290 GLU B OE2   1 
ATOM   7882  N  N     . LEU B 1 291 ? 99.479  137.443 148.071 1.00 30.84 ?  291 LEU B N     1 
ATOM   7883  C  CA    . LEU B 1 291 ? 98.890  136.548 147.079 1.00 27.61 ?  291 LEU B CA    1 
ATOM   7884  C  C     . LEU B 1 291 ? 99.022  135.091 147.499 1.00 34.77 ?  291 LEU B C     1 
ATOM   7885  O  O     . LEU B 1 291 ? 98.087  134.302 147.324 1.00 38.54 ?  291 LEU B O     1 
ATOM   7886  C  CB    . LEU B 1 291 ? 99.540  136.771 145.714 1.00 32.42 ?  291 LEU B CB    1 
ATOM   7887  C  CG    . LEU B 1 291 ? 99.291  138.123 145.046 1.00 33.84 ?  291 LEU B CG    1 
ATOM   7888  C  CD1   . LEU B 1 291 ? 100.287 138.346 143.924 1.00 26.96 ?  291 LEU B CD1   1 
ATOM   7889  C  CD2   . LEU B 1 291 ? 97.867  138.215 144.532 1.00 31.97 ?  291 LEU B CD2   1 
ATOM   7890  N  N     . ALA B 1 292 ? 100.179 134.711 148.047 1.00 41.06 ?  292 ALA B N     1 
ATOM   7891  C  CA    . ALA B 1 292 ? 100.364 133.342 148.513 1.00 31.29 ?  292 ALA B CA    1 
ATOM   7892  C  C     . ALA B 1 292 ? 99.507  133.044 149.736 1.00 31.33 ?  292 ALA B C     1 
ATOM   7893  O  O     . ALA B 1 292 ? 99.034  131.915 149.900 1.00 38.52 ?  292 ALA B O     1 
ATOM   7894  C  CB    . ALA B 1 292 ? 101.838 133.087 148.824 1.00 27.35 ?  292 ALA B CB    1 
ATOM   7895  N  N     . ARG B 1 293 ? 99.302  134.038 150.602 1.00 36.05 ?  293 ARG B N     1 
ATOM   7896  C  CA    . ARG B 1 293 ? 98.493  133.839 151.799 1.00 36.19 ?  293 ARG B CA    1 
ATOM   7897  C  C     . ARG B 1 293 ? 97.054  133.495 151.442 1.00 41.29 ?  293 ARG B C     1 
ATOM   7898  O  O     . ARG B 1 293 ? 96.448  132.607 152.054 1.00 47.95 ?  293 ARG B O     1 
ATOM   7899  C  CB    . ARG B 1 293 ? 98.552  135.093 152.670 1.00 37.33 ?  293 ARG B CB    1 
ATOM   7900  C  CG    . ARG B 1 293 ? 97.586  135.116 153.835 1.00 37.72 ?  293 ARG B CG    1 
ATOM   7901  C  CD    . ARG B 1 293 ? 97.563  136.495 154.464 1.00 38.99 ?  293 ARG B CD    1 
ATOM   7902  N  NE    . ARG B 1 293 ? 98.911  137.019 154.644 1.00 45.33 ?  293 ARG B NE    1 
ATOM   7903  C  CZ    . ARG B 1 293 ? 99.300  138.232 154.272 1.00 43.13 ?  293 ARG B CZ    1 
ATOM   7904  N  NH1   . ARG B 1 293 ? 98.463  139.083 153.704 1.00 42.09 1  293 ARG B NH1   1 
ATOM   7905  N  NH2   . ARG B 1 293 ? 100.562 138.597 154.475 1.00 40.00 ?  293 ARG B NH2   1 
ATOM   7906  N  N     . GLU B 1 294 ? 96.492  134.182 150.454 1.00 48.58 ?  294 GLU B N     1 
ATOM   7907  C  CA    . GLU B 1 294 ? 95.121  133.952 150.022 1.00 47.69 ?  294 GLU B CA    1 
ATOM   7908  C  C     . GLU B 1 294 ? 95.019  132.917 148.910 1.00 45.66 ?  294 GLU B C     1 
ATOM   7909  O  O     . GLU B 1 294 ? 93.916  132.678 148.408 1.00 48.04 ?  294 GLU B O     1 
ATOM   7910  C  CB    . GLU B 1 294 ? 94.490  135.269 149.564 1.00 44.43 ?  294 GLU B CB    1 
ATOM   7911  C  CG    . GLU B 1 294 ? 94.393  136.317 150.658 1.00 48.49 ?  294 GLU B CG    1 
ATOM   7912  C  CD    . GLU B 1 294 ? 94.473  137.728 150.115 1.00 55.04 ?  294 GLU B CD    1 
ATOM   7913  O  OE1   . GLU B 1 294 ? 94.637  137.881 148.887 1.00 56.38 ?  294 GLU B OE1   1 
ATOM   7914  O  OE2   . GLU B 1 294 ? 94.376  138.681 150.916 1.00 54.30 -1 294 GLU B OE2   1 
ATOM   7915  N  N     . ASP B 1 295 ? 96.139  132.314 148.510 1.00 44.07 ?  295 ASP B N     1 
ATOM   7916  C  CA    . ASP B 1 295 ? 96.195  131.264 147.494 1.00 43.93 ?  295 ASP B CA    1 
ATOM   7917  C  C     . ASP B 1 295 ? 95.700  131.737 146.131 1.00 49.15 ?  295 ASP B C     1 
ATOM   7918  O  O     . ASP B 1 295 ? 95.390  130.914 145.263 1.00 47.46 ?  295 ASP B O     1 
ATOM   7919  C  CB    . ASP B 1 295 ? 95.417  130.017 147.931 1.00 45.64 ?  295 ASP B CB    1 
ATOM   7920  C  CG    . ASP B 1 295 ? 96.139  128.728 147.586 1.00 52.77 ?  295 ASP B CG    1 
ATOM   7921  O  OD1   . ASP B 1 295 ? 97.054  128.766 146.738 1.00 54.24 ?  295 ASP B OD1   1 
ATOM   7922  O  OD2   . ASP B 1 295 ? 95.788  127.676 148.158 1.00 50.23 -1 295 ASP B OD2   1 
ATOM   7923  N  N     . LYS B 1 296 ? 95.615  133.047 145.920 1.00 49.66 ?  296 LYS B N     1 
ATOM   7924  C  CA    . LYS B 1 296 ? 95.277  133.564 144.602 1.00 47.19 ?  296 LYS B CA    1 
ATOM   7925  C  C     . LYS B 1 296 ? 96.427  133.315 143.636 1.00 45.50 ?  296 LYS B C     1 
ATOM   7926  O  O     . LYS B 1 296 ? 97.599  133.458 143.994 1.00 51.87 ?  296 LYS B O     1 
ATOM   7927  C  CB    . LYS B 1 296 ? 94.972  135.060 144.671 1.00 46.04 ?  296 LYS B CB    1 
ATOM   7928  C  CG    . LYS B 1 296 ? 94.432  135.526 146.008 1.00 47.76 ?  296 LYS B CG    1 
ATOM   7929  C  CD    . LYS B 1 296 ? 93.443  136.666 145.840 1.00 49.04 ?  296 LYS B CD    1 
ATOM   7930  C  CE    . LYS B 1 296 ? 92.056  136.148 145.501 1.00 51.74 ?  296 LYS B CE    1 
ATOM   7931  N  NZ    . LYS B 1 296 ? 91.500  135.293 146.586 1.00 50.32 1  296 LYS B NZ    1 
ATOM   7932  N  N     . ALA B 1 297 ? 96.092  132.939 142.407 1.00 45.38 ?  297 ALA B N     1 
ATOM   7933  C  CA    . ALA B 1 297 ? 97.115  132.715 141.397 1.00 46.15 ?  297 ALA B CA    1 
ATOM   7934  C  C     . ALA B 1 297 ? 97.765  134.040 141.016 1.00 45.62 ?  297 ALA B C     1 
ATOM   7935  O  O     . ALA B 1 297 ? 97.076  135.015 140.701 1.00 53.38 ?  297 ALA B O     1 
ATOM   7936  C  CB    . ALA B 1 297 ? 96.512  132.040 140.169 1.00 44.20 ?  297 ALA B CB    1 
ATOM   7937  N  N     . ALA B 1 298 ? 99.092  134.073 141.048 1.00 38.81 ?  298 ALA B N     1 
ATOM   7938  C  CA    . ALA B 1 298 ? 99.851  135.298 140.850 1.00 39.74 ?  298 ALA B CA    1 
ATOM   7939  C  C     . ALA B 1 298 ? 100.381 135.387 139.426 1.00 37.91 ?  298 ALA B C     1 
ATOM   7940  O  O     . ALA B 1 298 ? 100.338 134.428 138.652 1.00 41.21 ?  298 ALA B O     1 
ATOM   7941  C  CB    . ALA B 1 298 ? 101.004 135.382 141.854 1.00 42.58 ?  298 ALA B CB    1 
ATOM   7942  N  N     . TYR B 1 299 ? 100.894 136.566 139.088 1.00 38.47 ?  299 TYR B N     1 
ATOM   7943  C  CA    . TYR B 1 299 ? 101.431 136.853 137.767 1.00 31.67 ?  299 TYR B CA    1 
ATOM   7944  C  C     . TYR B 1 299 ? 102.860 137.357 137.895 1.00 33.77 ?  299 TYR B C     1 
ATOM   7945  O  O     . TYR B 1 299 ? 103.142 138.232 138.719 1.00 41.45 ?  299 TYR B O     1 
ATOM   7946  C  CB    . TYR B 1 299 ? 100.579 137.899 137.044 1.00 32.93 ?  299 TYR B CB    1 
ATOM   7947  C  CG    . TYR B 1 299 ? 99.304  137.358 136.445 1.00 35.07 ?  299 TYR B CG    1 
ATOM   7948  C  CD1   . TYR B 1 299 ? 99.335  136.525 135.336 1.00 37.58 ?  299 TYR B CD1   1 
ATOM   7949  C  CD2   . TYR B 1 299 ? 98.069  137.686 136.984 1.00 36.23 ?  299 TYR B CD2   1 
ATOM   7950  C  CE1   . TYR B 1 299 ? 98.173  136.033 134.784 1.00 41.02 ?  299 TYR B CE1   1 
ATOM   7951  C  CE2   . TYR B 1 299 ? 96.902  137.198 136.440 1.00 39.48 ?  299 TYR B CE2   1 
ATOM   7952  C  CZ    . TYR B 1 299 ? 96.958  136.373 135.340 1.00 44.62 ?  299 TYR B CZ    1 
ATOM   7953  O  OH    . TYR B 1 299 ? 95.794  135.885 134.792 1.00 45.44 ?  299 TYR B OH    1 
ATOM   7954  N  N     . VAL B 1 300 ? 103.755 136.803 137.085 1.00 32.57 ?  300 VAL B N     1 
ATOM   7955  C  CA    . VAL B 1 300 ? 105.091 137.355 136.896 1.00 28.85 ?  300 VAL B CA    1 
ATOM   7956  C  C     . VAL B 1 300 ? 105.089 138.116 135.581 1.00 27.75 ?  300 VAL B C     1 
ATOM   7957  O  O     . VAL B 1 300 ? 104.454 137.693 134.609 1.00 32.37 ?  300 VAL B O     1 
ATOM   7958  C  CB    . VAL B 1 300 ? 106.171 136.257 136.913 1.00 24.24 ?  300 VAL B CB    1 
ATOM   7959  C  CG1   . VAL B 1 300 ? 106.421 135.790 138.335 1.00 26.78 ?  300 VAL B CG1   1 
ATOM   7960  C  CG2   . VAL B 1 300 ? 105.767 135.095 136.025 1.00 31.98 ?  300 VAL B CG2   1 
ATOM   7961  N  N     . PHE B 1 301 ? 105.790 139.241 135.545 1.00 30.11 ?  301 PHE B N     1 
ATOM   7962  C  CA    . PHE B 1 301 ? 105.661 140.192 134.454 1.00 23.39 ?  301 PHE B CA    1 
ATOM   7963  C  C     . PHE B 1 301 ? 106.956 140.294 133.664 1.00 31.95 ?  301 PHE B C     1 
ATOM   7964  O  O     . PHE B 1 301 ? 108.052 140.132 134.207 1.00 33.95 ?  301 PHE B O     1 
ATOM   7965  C  CB    . PHE B 1 301 ? 105.269 141.572 134.980 1.00 24.46 ?  301 PHE B CB    1 
ATOM   7966  C  CG    . PHE B 1 301 ? 104.089 141.550 135.903 1.00 31.13 ?  301 PHE B CG    1 
ATOM   7967  C  CD1   . PHE B 1 301 ? 102.802 141.571 135.401 1.00 28.85 ?  301 PHE B CD1   1 
ATOM   7968  C  CD2   . PHE B 1 301 ? 104.270 141.494 137.273 1.00 27.61 ?  301 PHE B CD2   1 
ATOM   7969  C  CE1   . PHE B 1 301 ? 101.716 141.544 136.248 1.00 30.97 ?  301 PHE B CE1   1 
ATOM   7970  C  CE2   . PHE B 1 301 ? 103.187 141.467 138.123 1.00 28.61 ?  301 PHE B CE2   1 
ATOM   7971  C  CZ    . PHE B 1 301 ? 101.908 141.493 137.609 1.00 33.66 ?  301 PHE B CZ    1 
ATOM   7972  N  N     . TYR B 1 302 ? 106.812 140.560 132.371 1.00 31.27 ?  302 TYR B N     1 
ATOM   7973  C  CA    . TYR B 1 302 ? 107.960 140.864 131.531 1.00 28.12 ?  302 TYR B CA    1 
ATOM   7974  C  C     . TYR B 1 302 ? 108.361 142.315 131.760 1.00 29.09 ?  302 TYR B C     1 
ATOM   7975  O  O     . TYR B 1 302 ? 107.566 143.217 131.475 1.00 32.21 ?  302 TYR B O     1 
ATOM   7976  C  CB    . TYR B 1 302 ? 107.631 140.628 130.063 1.00 29.30 ?  302 TYR B CB    1 
ATOM   7977  C  CG    . TYR B 1 302 ? 107.426 139.174 129.694 1.00 31.34 ?  302 TYR B CG    1 
ATOM   7978  C  CD1   . TYR B 1 302 ? 106.259 138.507 130.038 1.00 30.03 ?  302 TYR B CD1   1 
ATOM   7979  C  CD2   . TYR B 1 302 ? 108.400 138.471 128.999 1.00 29.42 ?  302 TYR B CD2   1 
ATOM   7980  C  CE1   . TYR B 1 302 ? 106.067 137.183 129.700 1.00 30.43 ?  302 TYR B CE1   1 
ATOM   7981  C  CE2   . TYR B 1 302 ? 108.217 137.146 128.660 1.00 31.36 ?  302 TYR B CE2   1 
ATOM   7982  C  CZ    . TYR B 1 302 ? 107.049 136.508 129.012 1.00 34.48 ?  302 TYR B CZ    1 
ATOM   7983  O  OH    . TYR B 1 302 ? 106.861 135.187 128.677 1.00 34.45 ?  302 TYR B OH    1 
ATOM   7984  N  N     . PRO B 1 303 ? 109.560 142.584 132.282 1.00 26.70 ?  303 PRO B N     1 
ATOM   7985  C  CA    . PRO B 1 303 ? 109.897 143.963 132.671 1.00 30.11 ?  303 PRO B CA    1 
ATOM   7986  C  C     . PRO B 1 303 ? 109.894 144.958 131.525 1.00 28.10 ?  303 PRO B C     1 
ATOM   7987  O  O     . PRO B 1 303 ? 109.556 146.129 131.743 1.00 33.19 ?  303 PRO B O     1 
ATOM   7988  C  CB    . PRO B 1 303 ? 111.298 143.814 133.280 1.00 29.93 ?  303 PRO B CB    1 
ATOM   7989  C  CG    . PRO B 1 303 ? 111.364 142.402 133.718 1.00 27.96 ?  303 PRO B CG    1 
ATOM   7990  C  CD    . PRO B 1 303 ? 110.596 141.626 132.697 1.00 23.22 ?  303 PRO B CD    1 
ATOM   7991  N  N     . HIS B 1 304 ? 110.268 144.542 130.315 1.00 29.44 ?  304 HIS B N     1 
ATOM   7992  C  CA    . HIS B 1 304 ? 110.354 145.503 129.220 1.00 27.98 ?  304 HIS B CA    1 
ATOM   7993  C  C     . HIS B 1 304 ? 108.979 145.992 128.789 1.00 34.11 ?  304 HIS B C     1 
ATOM   7994  O  O     . HIS B 1 304 ? 108.837 147.149 128.386 1.00 41.97 ?  304 HIS B O     1 
ATOM   7995  C  CB    . HIS B 1 304 ? 111.099 144.904 128.031 1.00 29.58 ?  304 HIS B CB    1 
ATOM   7996  C  CG    . HIS B 1 304 ? 111.483 145.916 126.998 1.00 33.21 ?  304 HIS B CG    1 
ATOM   7997  N  ND1   . HIS B 1 304 ? 112.104 147.104 127.317 1.00 33.55 ?  304 HIS B ND1   1 
ATOM   7998  C  CD2   . HIS B 1 304 ? 111.323 145.925 125.654 1.00 34.93 ?  304 HIS B CD2   1 
ATOM   7999  C  CE1   . HIS B 1 304 ? 112.317 147.798 126.214 1.00 32.26 ?  304 HIS B CE1   1 
ATOM   8000  N  NE2   . HIS B 1 304 ? 111.852 147.105 125.191 1.00 34.44 ?  304 HIS B NE2   1 
ATOM   8001  N  N     . THR B 1 305 ? 107.957 145.137 128.867 1.00 33.07 ?  305 THR B N     1 
ATOM   8002  C  CA    . THR B 1 305 ? 106.602 145.590 128.577 1.00 32.53 ?  305 THR B CA    1 
ATOM   8003  C  C     . THR B 1 305 ? 106.159 146.659 129.567 1.00 29.67 ?  305 THR B C     1 
ATOM   8004  O  O     . THR B 1 305 ? 105.548 147.661 129.181 1.00 35.87 ?  305 THR B O     1 
ATOM   8005  C  CB    . THR B 1 305 ? 105.636 144.408 128.594 1.00 31.15 ?  305 THR B CB    1 
ATOM   8006  O  OG1   . THR B 1 305 ? 105.496 143.922 129.934 1.00 29.56 ?  305 THR B OG1   1 
ATOM   8007  C  CG2   . THR B 1 305 ? 106.158 143.291 127.709 1.00 31.52 ?  305 THR B CG2   1 
ATOM   8008  N  N     . ILE B 1 306 ? 106.471 146.466 130.850 1.00 35.97 ?  306 ILE B N     1 
ATOM   8009  C  CA    . ILE B 1 306 ? 106.134 147.461 131.861 1.00 29.61 ?  306 ILE B CA    1 
ATOM   8010  C  C     . ILE B 1 306 ? 106.894 148.757 131.611 1.00 28.38 ?  306 ILE B C     1 
ATOM   8011  O  O     . ILE B 1 306 ? 106.334 149.854 131.728 1.00 35.85 ?  306 ILE B O     1 
ATOM   8012  C  CB    . ILE B 1 306 ? 106.411 146.899 133.267 1.00 27.13 ?  306 ILE B CB    1 
ATOM   8013  C  CG1   . ILE B 1 306 ? 105.334 145.883 133.646 1.00 27.32 ?  306 ILE B CG1   1 
ATOM   8014  C  CG2   . ILE B 1 306 ? 106.484 148.017 134.295 1.00 30.70 ?  306 ILE B CG2   1 
ATOM   8015  C  CD1   . ILE B 1 306 ? 105.602 145.169 134.936 1.00 29.91 ?  306 ILE B CD1   1 
ATOM   8016  N  N     . TYR B 1 307 ? 108.177 148.653 131.263 1.00 30.49 ?  307 TYR B N     1 
ATOM   8017  C  CA    . TYR B 1 307 ? 108.967 149.847 130.981 1.00 31.96 ?  307 TYR B CA    1 
ATOM   8018  C  C     . TYR B 1 307 ? 108.421 150.603 129.777 1.00 35.66 ?  307 TYR B C     1 
ATOM   8019  O  O     . TYR B 1 307 ? 108.384 151.838 129.773 1.00 39.51 ?  307 TYR B O     1 
ATOM   8020  C  CB    . TYR B 1 307 ? 110.430 149.468 130.759 1.00 26.23 ?  307 TYR B CB    1 
ATOM   8021  C  CG    . TYR B 1 307 ? 111.333 150.654 130.533 1.00 35.96 ?  307 TYR B CG    1 
ATOM   8022  C  CD1   . TYR B 1 307 ? 111.765 151.432 131.597 1.00 31.13 ?  307 TYR B CD1   1 
ATOM   8023  C  CD2   . TYR B 1 307 ? 111.748 151.002 129.256 1.00 37.14 ?  307 TYR B CD2   1 
ATOM   8024  C  CE1   . TYR B 1 307 ? 112.588 152.520 131.396 1.00 31.45 ?  307 TYR B CE1   1 
ATOM   8025  C  CE2   . TYR B 1 307 ? 112.569 152.087 129.045 1.00 36.70 ?  307 TYR B CE2   1 
ATOM   8026  C  CZ    . TYR B 1 307 ? 112.987 152.843 130.118 1.00 37.64 ?  307 TYR B CZ    1 
ATOM   8027  O  OH    . TYR B 1 307 ? 113.807 153.926 129.911 1.00 40.14 ?  307 TYR B OH    1 
ATOM   8028  N  N     . LYS B 1 308 ? 108.005 149.877 128.739 1.00 39.05 ?  308 LYS B N     1 
ATOM   8029  C  CA    . LYS B 1 308 ? 107.441 150.523 127.558 1.00 32.40 ?  308 LYS B CA    1 
ATOM   8030  C  C     . LYS B 1 308 ? 106.095 151.166 127.867 1.00 28.74 ?  308 LYS B C     1 
ATOM   8031  O  O     . LYS B 1 308 ? 105.784 152.245 127.350 1.00 37.26 ?  308 LYS B O     1 
ATOM   8032  C  CB    . LYS B 1 308 ? 107.300 149.505 126.428 1.00 32.55 ?  308 LYS B CB    1 
ATOM   8033  C  CG    . LYS B 1 308 ? 108.523 149.394 125.535 1.00 33.55 ?  308 LYS B CG    1 
ATOM   8034  C  CD    . LYS B 1 308 ? 108.603 148.033 124.854 1.00 37.52 ?  308 LYS B CD    1 
ATOM   8035  C  CE    . LYS B 1 308 ? 107.229 147.403 124.677 1.00 38.18 ?  308 LYS B CE    1 
ATOM   8036  N  NZ    . LYS B 1 308 ? 107.299 145.919 124.599 1.00 39.44 1  308 LYS B NZ    1 
ATOM   8037  N  N     . GLU B 1 309 ? 105.284 150.519 128.704 1.00 30.88 ?  309 GLU B N     1 
ATOM   8038  C  CA    . GLU B 1 309 ? 103.949 151.037 128.982 1.00 35.01 ?  309 GLU B CA    1 
ATOM   8039  C  C     . GLU B 1 309 ? 103.992 152.247 129.908 1.00 39.29 ?  309 GLU B C     1 
ATOM   8040  O  O     . GLU B 1 309 ? 103.242 153.210 129.710 1.00 42.53 ?  309 GLU B O     1 
ATOM   8041  C  CB    . GLU B 1 309 ? 103.079 149.933 129.581 1.00 31.66 ?  309 GLU B CB    1 
ATOM   8042  C  CG    . GLU B 1 309 ? 101.693 150.389 130.002 1.00 37.92 ?  309 GLU B CG    1 
ATOM   8043  C  CD    . GLU B 1 309 ? 100.826 150.801 128.830 1.00 44.26 ?  309 GLU B CD    1 
ATOM   8044  O  OE1   . GLU B 1 309 ? 101.180 150.479 127.676 1.00 44.90 ?  309 GLU B OE1   1 
ATOM   8045  O  OE2   . GLU B 1 309 ? 99.786  151.452 129.063 1.00 42.88 -1 309 GLU B OE2   1 
ATOM   8046  N  N     . TYR B 1 310 ? 104.856 152.222 130.922 1.00 38.41 ?  310 TYR B N     1 
ATOM   8047  C  CA    . TYR B 1 310 ? 104.841 153.240 131.962 1.00 32.71 ?  310 TYR B CA    1 
ATOM   8048  C  C     . TYR B 1 310 ? 106.066 154.141 131.968 1.00 31.48 ?  310 TYR B C     1 
ATOM   8049  O  O     . TYR B 1 310 ? 106.073 155.134 132.702 1.00 37.24 ?  310 TYR B O     1 
ATOM   8050  C  CB    . TYR B 1 310 ? 104.697 152.578 133.340 1.00 34.92 ?  310 TYR B CB    1 
ATOM   8051  C  CG    . TYR B 1 310 ? 103.450 151.739 133.477 1.00 35.19 ?  310 TYR B CG    1 
ATOM   8052  C  CD1   . TYR B 1 310 ? 102.229 152.323 133.786 1.00 31.87 ?  310 TYR B CD1   1 
ATOM   8053  C  CD2   . TYR B 1 310 ? 103.488 150.366 133.281 1.00 30.33 ?  310 TYR B CD2   1 
ATOM   8054  C  CE1   . TYR B 1 310 ? 101.086 151.562 133.905 1.00 34.98 ?  310 TYR B CE1   1 
ATOM   8055  C  CE2   . TYR B 1 310 ? 102.349 149.599 133.396 1.00 31.20 ?  310 TYR B CE2   1 
ATOM   8056  C  CZ    . TYR B 1 310 ? 101.152 150.200 133.710 1.00 35.71 ?  310 TYR B CZ    1 
ATOM   8057  O  OH    . TYR B 1 310 ? 100.014 149.439 133.827 1.00 36.16 ?  310 TYR B OH    1 
ATOM   8058  N  N     . GLY B 1 311 ? 107.094 153.831 131.184 1.00 27.99 ?  311 GLY B N     1 
ATOM   8059  C  CA    . GLY B 1 311 ? 108.311 154.612 131.213 1.00 30.48 ?  311 GLY B CA    1 
ATOM   8060  C  C     . GLY B 1 311 ? 109.165 154.408 132.442 1.00 31.62 ?  311 GLY B C     1 
ATOM   8061  O  O     . GLY B 1 311 ? 110.187 155.087 132.584 1.00 40.98 ?  311 GLY B O     1 
ATOM   8062  N  N     . GLN B 1 312 ? 108.781 153.499 133.332 1.00 31.69 ?  312 GLN B N     1 
ATOM   8063  C  CA    . GLN B 1 312 ? 109.530 153.203 134.540 1.00 30.03 ?  312 GLN B CA    1 
ATOM   8064  C  C     . GLN B 1 312 ? 109.775 151.706 134.619 1.00 31.15 ?  312 GLN B C     1 
ATOM   8065  O  O     . GLN B 1 312 ? 108.968 150.905 134.141 1.00 39.00 ?  312 GLN B O     1 
ATOM   8066  C  CB    . GLN B 1 312 ? 108.785 153.669 135.796 1.00 34.29 ?  312 GLN B CB    1 
ATOM   8067  C  CG    . GLN B 1 312 ? 108.399 155.133 135.787 1.00 37.13 ?  312 GLN B CG    1 
ATOM   8068  C  CD    . GLN B 1 312 ? 107.331 155.453 136.811 1.00 39.55 ?  312 GLN B CD    1 
ATOM   8069  O  OE1   . GLN B 1 312 ? 106.154 155.585 136.476 1.00 38.28 ?  312 GLN B OE1   1 
ATOM   8070  N  NE2   . GLN B 1 312 ? 107.737 155.579 138.067 1.00 37.71 ?  312 GLN B NE2   1 
ATOM   8071  N  N     . HIS B 1 313 ? 110.899 151.336 135.223 1.00 28.09 ?  313 HIS B N     1 
ATOM   8072  C  CA    . HIS B 1 313 ? 111.208 149.929 135.420 1.00 28.27 ?  313 HIS B CA    1 
ATOM   8073  C  C     . HIS B 1 313 ? 110.231 149.303 136.408 1.00 32.03 ?  313 HIS B C     1 
ATOM   8074  O  O     . HIS B 1 313 ? 109.702 149.969 137.300 1.00 34.17 ?  313 HIS B O     1 
ATOM   8075  C  CB    . HIS B 1 313 ? 112.641 149.762 135.918 1.00 26.18 ?  313 HIS B CB    1 
ATOM   8076  C  CG    . HIS B 1 313 ? 113.678 150.123 134.903 1.00 27.23 ?  313 HIS B CG    1 
ATOM   8077  N  ND1   . HIS B 1 313 ? 113.944 149.339 133.800 1.00 30.43 ?  313 HIS B ND1   1 
ATOM   8078  C  CD2   . HIS B 1 313 ? 114.518 151.181 134.823 1.00 28.25 ?  313 HIS B CD2   1 
ATOM   8079  C  CE1   . HIS B 1 313 ? 114.903 149.901 133.085 1.00 27.83 ?  313 HIS B CE1   1 
ATOM   8080  N  NE2   . HIS B 1 313 ? 115.268 151.019 133.685 1.00 32.42 ?  313 HIS B NE2   1 
ATOM   8081  N  N     . MET B 1 314 ? 109.992 148.003 136.235 1.00 34.99 ?  314 MET B N     1 
ATOM   8082  C  CA    . MET B 1 314 ? 109.047 147.304 137.099 1.00 29.03 ?  314 MET B CA    1 
ATOM   8083  C  C     . MET B 1 314 ? 109.523 147.304 138.546 1.00 34.23 ?  314 MET B C     1 
ATOM   8084  O  O     . MET B 1 314 ? 108.717 147.452 139.472 1.00 38.94 ?  314 MET B O     1 
ATOM   8085  C  CB    . MET B 1 314 ? 108.833 145.878 136.591 1.00 26.60 ?  314 MET B CB    1 
ATOM   8086  C  CG    . MET B 1 314 ? 108.246 144.921 137.610 1.00 27.15 ?  314 MET B CG    1 
ATOM   8087  S  SD    . MET B 1 314 ? 108.577 143.199 137.199 1.00 43.44 ?  314 MET B SD    1 
ATOM   8088  C  CE    . MET B 1 314 ? 110.219 142.996 137.883 1.00 34.29 ?  314 MET B CE    1 
ATOM   8089  N  N     . ASP B 1 315 ? 110.829 147.147 138.764 1.00 34.31 ?  315 ASP B N     1 
ATOM   8090  C  CA    . ASP B 1 315 ? 111.372 147.179 140.115 1.00 34.44 ?  315 ASP B CA    1 
ATOM   8091  C  C     . ASP B 1 315 ? 111.524 148.591 140.670 1.00 28.83 ?  315 ASP B C     1 
ATOM   8092  O  O     . ASP B 1 315 ? 111.823 148.743 141.858 1.00 38.87 ?  315 ASP B O     1 
ATOM   8093  C  CB    . ASP B 1 315 ? 112.701 146.399 140.162 1.00 29.64 ?  315 ASP B CB    1 
ATOM   8094  C  CG    . ASP B 1 315 ? 113.914 147.203 139.685 1.00 33.54 ?  315 ASP B CG    1 
ATOM   8095  O  OD1   . ASP B 1 315 ? 113.796 148.370 139.260 1.00 40.00 ?  315 ASP B OD1   1 
ATOM   8096  O  OD2   . ASP B 1 315 ? 115.027 146.641 139.748 1.00 35.00 -1 315 ASP B OD2   1 
ATOM   8097  N  N     . GLU B 1 316 ? 111.323 149.618 139.846 1.00 24.99 ?  316 GLU B N     1 
ATOM   8098  C  CA    . GLU B 1 316 ? 111.301 150.997 140.315 1.00 27.13 ?  316 GLU B CA    1 
ATOM   8099  C  C     . GLU B 1 316 ? 109.936 151.425 140.831 1.00 35.65 ?  316 GLU B C     1 
ATOM   8100  O  O     . GLU B 1 316 ? 109.815 152.534 141.362 1.00 35.99 ?  316 GLU B O     1 
ATOM   8101  C  CB    . GLU B 1 316 ? 111.735 151.940 139.191 1.00 31.43 ?  316 GLU B CB    1 
ATOM   8102  C  CG    . GLU B 1 316 ? 112.687 153.033 139.629 1.00 34.63 ?  316 GLU B CG    1 
ATOM   8103  C  CD    . GLU B 1 316 ? 114.059 152.505 139.970 1.00 39.24 ?  316 GLU B CD    1 
ATOM   8104  O  OE1   . GLU B 1 316 ? 114.489 151.523 139.333 1.00 40.91 ?  316 GLU B OE1   1 
ATOM   8105  O  OE2   . GLU B 1 316 ? 114.708 153.072 140.873 1.00 38.33 -1 316 GLU B OE2   1 
ATOM   8106  N  N     . MET B 1 317 ? 108.918 150.584 140.691 1.00 38.87 ?  317 MET B N     1 
ATOM   8107  C  CA    . MET B 1 317 ? 107.553 150.923 141.059 1.00 34.88 ?  317 MET B CA    1 
ATOM   8108  C  C     . MET B 1 317 ? 107.088 150.075 142.234 1.00 38.69 ?  317 MET B C     1 
ATOM   8109  O  O     . MET B 1 317 ? 107.610 148.988 142.495 1.00 39.26 ?  317 MET B O     1 
ATOM   8110  C  CB    . MET B 1 317 ? 106.608 150.735 139.868 1.00 35.43 ?  317 MET B CB    1 
ATOM   8111  C  CG    . MET B 1 317 ? 107.099 151.391 138.590 1.00 37.07 ?  317 MET B CG    1 
ATOM   8112  S  SD    . MET B 1 317 ? 106.460 150.602 137.105 1.00 48.33 ?  317 MET B SD    1 
ATOM   8113  C  CE    . MET B 1 317 ? 104.997 151.590 136.818 1.00 39.01 ?  317 MET B CE    1 
ATOM   8114  N  N     . ASP B 1 318 ? 106.088 150.592 142.943 1.00 40.07 ?  318 ASP B N     1 
ATOM   8115  C  CA    . ASP B 1 318 ? 105.533 149.914 144.110 1.00 37.58 ?  318 ASP B CA    1 
ATOM   8116  C  C     . ASP B 1 318 ? 104.576 148.828 143.637 1.00 42.08 ?  318 ASP B C     1 
ATOM   8117  O  O     . ASP B 1 318 ? 103.502 149.126 143.106 1.00 44.38 ?  318 ASP B O     1 
ATOM   8118  C  CB    . ASP B 1 318 ? 104.825 150.915 145.018 1.00 39.27 ?  318 ASP B CB    1 
ATOM   8119  C  CG    . ASP B 1 318 ? 104.381 150.300 146.328 1.00 49.10 ?  318 ASP B CG    1 
ATOM   8120  O  OD1   . ASP B 1 318 ? 105.079 149.395 146.832 1.00 46.36 ?  318 ASP B OD1   1 
ATOM   8121  O  OD2   . ASP B 1 318 ? 103.332 150.724 146.856 1.00 50.01 -1 318 ASP B OD2   1 
ATOM   8122  N  N     . MET B 1 319 ? 104.962 147.565 143.833 1.00 40.62 ?  319 MET B N     1 
ATOM   8123  C  CA    . MET B 1 319 ? 104.132 146.460 143.366 1.00 35.55 ?  319 MET B CA    1 
ATOM   8124  C  C     . MET B 1 319 ? 102.800 146.395 144.100 1.00 36.85 ?  319 MET B C     1 
ATOM   8125  O  O     . MET B 1 319 ? 101.819 145.891 143.546 1.00 42.15 ?  319 MET B O     1 
ATOM   8126  C  CB    . MET B 1 319 ? 104.881 145.137 143.519 1.00 35.05 ?  319 MET B CB    1 
ATOM   8127  C  CG    . MET B 1 319 ? 104.331 144.020 142.650 1.00 37.88 ?  319 MET B CG    1 
ATOM   8128  S  SD    . MET B 1 319 ? 104.464 144.364 140.887 1.00 47.61 ?  319 MET B SD    1 
ATOM   8129  C  CE    . MET B 1 319 ? 106.241 144.378 140.686 1.00 41.96 ?  319 MET B CE    1 
ATOM   8130  N  N     . ASN B 1 320 ? 102.738 146.912 145.328 1.00 39.09 ?  320 ASN B N     1 
ATOM   8131  C  CA    . ASN B 1 320 ? 101.491 146.864 146.083 1.00 39.65 ?  320 ASN B CA    1 
ATOM   8132  C  C     . ASN B 1 320 ? 100.394 147.666 145.394 1.00 46.07 ?  320 ASN B C     1 
ATOM   8133  O  O     . ASN B 1 320 ? 99.232  147.243 145.364 1.00 46.18 ?  320 ASN B O     1 
ATOM   8134  C  CB    . ASN B 1 320 ? 101.722 147.372 147.506 1.00 40.73 ?  320 ASN B CB    1 
ATOM   8135  C  CG    . ASN B 1 320 ? 102.757 146.552 148.251 1.00 43.14 ?  320 ASN B CG    1 
ATOM   8136  O  OD1   . ASN B 1 320 ? 102.536 145.381 148.553 1.00 42.76 ?  320 ASN B OD1   1 
ATOM   8137  N  ND2   . ASN B 1 320 ? 103.895 147.166 148.550 1.00 43.71 ?  320 ASN B ND2   1 
ATOM   8138  N  N     . GLU B 1 321 ? 100.740 148.823 144.833 1.00 46.25 ?  321 GLU B N     1 
ATOM   8139  C  CA    . GLU B 1 321 ? 99.767  149.626 144.104 1.00 44.91 ?  321 GLU B CA    1 
ATOM   8140  C  C     . GLU B 1 321 ? 99.758  149.332 142.610 1.00 43.62 ?  321 GLU B C     1 
ATOM   8141  O  O     . GLU B 1 321 ? 98.727  149.527 141.955 1.00 45.23 ?  321 GLU B O     1 
ATOM   8142  C  CB    . GLU B 1 321 ? 100.039 151.117 144.321 1.00 43.47 ?  321 GLU B CB    1 
ATOM   8143  C  CG    . GLU B 1 321 ? 101.400 151.580 143.831 1.00 47.11 ?  321 GLU B CG    1 
ATOM   8144  C  CD    . GLU B 1 321 ? 101.359 152.963 143.212 1.00 51.86 ?  321 GLU B CD    1 
ATOM   8145  O  OE1   . GLU B 1 321 ? 100.246 153.482 142.983 1.00 49.66 ?  321 GLU B OE1   1 
ATOM   8146  O  OE2   . GLU B 1 321 ? 102.440 153.532 142.952 1.00 51.96 -1 321 GLU B OE2   1 
ATOM   8147  N  N     . MET B 1 322 ? 100.875 148.866 142.058 1.00 40.70 ?  322 MET B N     1 
ATOM   8148  C  CA    . MET B 1 322 ? 101.000 148.688 140.619 1.00 35.62 ?  322 MET B CA    1 
ATOM   8149  C  C     . MET B 1 322 ? 100.661 147.284 140.140 1.00 37.11 ?  322 MET B C     1 
ATOM   8150  O  O     . MET B 1 322 ? 100.583 147.076 138.928 1.00 47.12 ?  322 MET B O     1 
ATOM   8151  C  CB    . MET B 1 322 ? 102.422 149.035 140.163 1.00 35.35 ?  322 MET B CB    1 
ATOM   8152  C  CG    . MET B 1 322 ? 102.705 150.522 140.051 1.00 39.64 ?  322 MET B CG    1 
ATOM   8153  S  SD    . MET B 1 322 ? 101.258 151.473 139.560 1.00 50.65 ?  322 MET B SD    1 
ATOM   8154  C  CE    . MET B 1 322 ? 101.349 151.327 137.779 1.00 39.32 ?  322 MET B CE    1 
ATOM   8155  N  N     . TYR B 1 323 ? 100.461 146.320 141.040 1.00 37.53 ?  323 TYR B N     1 
ATOM   8156  C  CA    . TYR B 1 323 ? 100.252 144.942 140.604 1.00 33.11 ?  323 TYR B CA    1 
ATOM   8157  C  C     . TYR B 1 323 ? 98.929  144.791 139.864 1.00 40.15 ?  323 TYR B C     1 
ATOM   8158  O  O     . TYR B 1 323 ? 98.868  144.155 138.804 1.00 43.00 ?  323 TYR B O     1 
ATOM   8159  C  CB    . TYR B 1 323 ? 100.310 143.998 141.805 1.00 34.53 ?  323 TYR B CB    1 
ATOM   8160  C  CG    . TYR B 1 323 ? 99.998  142.555 141.469 1.00 37.76 ?  323 TYR B CG    1 
ATOM   8161  C  CD1   . TYR B 1 323 ? 100.977 141.715 140.960 1.00 31.61 ?  323 TYR B CD1   1 
ATOM   8162  C  CD2   . TYR B 1 323 ? 98.725  142.035 141.664 1.00 37.36 ?  323 TYR B CD2   1 
ATOM   8163  C  CE1   . TYR B 1 323 ? 100.697 140.400 140.653 1.00 28.11 ?  323 TYR B CE1   1 
ATOM   8164  C  CE2   . TYR B 1 323 ? 98.438  140.722 141.360 1.00 33.00 ?  323 TYR B CE2   1 
ATOM   8165  C  CZ    . TYR B 1 323 ? 99.427  139.910 140.855 1.00 32.57 ?  323 TYR B CZ    1 
ATOM   8166  O  OH    . TYR B 1 323 ? 99.143  138.601 140.551 1.00 38.21 ?  323 TYR B OH    1 
ATOM   8167  N  N     . ASP B 1 324 ? 97.857  145.367 140.409 1.00 43.32 ?  324 ASP B N     1 
ATOM   8168  C  CA    . ASP B 1 324 ? 96.559  145.283 139.750 1.00 38.89 ?  324 ASP B CA    1 
ATOM   8169  C  C     . ASP B 1 324 ? 96.575  146.011 138.413 1.00 41.91 ?  324 ASP B C     1 
ATOM   8170  O  O     . ASP B 1 324 ? 95.979  145.544 137.437 1.00 47.99 ?  324 ASP B O     1 
ATOM   8171  C  CB    . ASP B 1 324 ? 95.470  145.845 140.660 1.00 42.11 ?  324 ASP B CB    1 
ATOM   8172  C  CG    . ASP B 1 324 ? 95.252  144.999 141.896 1.00 45.33 ?  324 ASP B CG    1 
ATOM   8173  O  OD1   . ASP B 1 324 ? 95.351  143.759 141.792 1.00 45.34 ?  324 ASP B OD1   1 
ATOM   8174  O  OD2   . ASP B 1 324 ? 94.982  145.572 142.972 1.00 46.45 -1 324 ASP B OD2   1 
ATOM   8175  N  N     . LYS B 1 325 ? 97.249  147.161 138.353 1.00 42.05 ?  325 LYS B N     1 
ATOM   8176  C  CA    . LYS B 1 325 ? 97.358  147.891 137.095 1.00 41.84 ?  325 LYS B CA    1 
ATOM   8177  C  C     . LYS B 1 325 ? 98.148  147.098 136.062 1.00 41.15 ?  325 LYS B C     1 
ATOM   8178  O  O     . LYS B 1 325 ? 97.796  147.089 134.877 1.00 46.54 ?  325 LYS B O     1 
ATOM   8179  C  CB    . LYS B 1 325 ? 97.998  149.257 137.336 1.00 39.41 ?  325 LYS B CB    1 
ATOM   8180  C  CG    . LYS B 1 325 ? 97.253  150.106 138.349 1.00 38.15 ?  325 LYS B CG    1 
ATOM   8181  C  CD    . LYS B 1 325 ? 97.203  151.563 137.924 1.00 43.84 ?  325 LYS B CD    1 
ATOM   8182  C  CE    . LYS B 1 325 ? 97.860  152.465 138.954 1.00 44.36 ?  325 LYS B CE    1 
ATOM   8183  N  NZ    . LYS B 1 325 ? 97.099  152.493 140.232 1.00 46.04 1  325 LYS B NZ    1 
ATOM   8184  N  N     . PHE B 1 326 ? 99.222  146.432 136.490 1.00 39.33 ?  326 PHE B N     1 
ATOM   8185  C  CA    . PHE B 1 326 ? 99.986  145.587 135.578 1.00 36.16 ?  326 PHE B CA    1 
ATOM   8186  C  C     . PHE B 1 326 ? 99.137  144.438 135.058 1.00 36.41 ?  326 PHE B C     1 
ATOM   8187  O  O     . PHE B 1 326 ? 99.159  144.132 133.860 1.00 44.28 ?  326 PHE B O     1 
ATOM   8188  C  CB    . PHE B 1 326 ? 101.230 145.039 136.281 1.00 34.73 ?  326 PHE B CB    1 
ATOM   8189  C  CG    . PHE B 1 326 ? 102.255 146.079 136.625 1.00 32.72 ?  326 PHE B CG    1 
ATOM   8190  C  CD1   . PHE B 1 326 ? 102.217 147.336 136.049 1.00 34.49 ?  326 PHE B CD1   1 
ATOM   8191  C  CD2   . PHE B 1 326 ? 103.263 145.793 137.529 1.00 36.10 ?  326 PHE B CD2   1 
ATOM   8192  C  CE1   . PHE B 1 326 ? 103.164 148.286 136.372 1.00 33.27 ?  326 PHE B CE1   1 
ATOM   8193  C  CE2   . PHE B 1 326 ? 104.212 146.739 137.851 1.00 39.21 ?  326 PHE B CE2   1 
ATOM   8194  C  CZ    . PHE B 1 326 ? 104.161 147.986 137.271 1.00 39.45 ?  326 PHE B CZ    1 
ATOM   8195  N  N     . VAL B 1 327 ? 98.382  143.787 135.947 1.00 40.83 ?  327 VAL B N     1 
ATOM   8196  C  CA    . VAL B 1 327 ? 97.577  142.639 135.544 1.00 43.25 ?  327 VAL B CA    1 
ATOM   8197  C  C     . VAL B 1 327 ? 96.463  143.068 134.595 1.00 43.55 ?  327 VAL B C     1 
ATOM   8198  O  O     . VAL B 1 327 ? 96.194  142.400 133.590 1.00 45.72 ?  327 VAL B O     1 
ATOM   8199  C  CB    . VAL B 1 327 ? 97.023  141.915 136.785 1.00 37.68 ?  327 VAL B CB    1 
ATOM   8200  C  CG1   . VAL B 1 327 ? 96.013  140.857 136.380 1.00 40.71 ?  327 VAL B CG1   1 
ATOM   8201  C  CG2   . VAL B 1 327 ? 98.154  141.289 137.579 1.00 31.33 ?  327 VAL B CG2   1 
ATOM   8202  N  N     . ASP B 1 328 ? 95.809  144.191 134.887 1.00 44.04 ?  328 ASP B N     1 
ATOM   8203  C  CA    . ASP B 1 328 ? 94.708  144.666 134.059 1.00 45.35 ?  328 ASP B CA    1 
ATOM   8204  C  C     . ASP B 1 328 ? 95.173  145.353 132.784 1.00 45.87 ?  328 ASP B C     1 
ATOM   8205  O  O     . ASP B 1 328 ? 94.339  145.630 131.915 1.00 49.89 ?  328 ASP B O     1 
ATOM   8206  C  CB    . ASP B 1 328 ? 93.823  145.624 134.859 1.00 45.98 ?  328 ASP B CB    1 
ATOM   8207  C  CG    . ASP B 1 328 ? 92.977  144.907 135.890 1.00 52.99 ?  328 ASP B CG    1 
ATOM   8208  O  OD1   . ASP B 1 328 ? 92.850  143.669 135.799 1.00 52.45 ?  328 ASP B OD1   1 
ATOM   8209  O  OD2   . ASP B 1 328 ? 92.437  145.583 136.792 1.00 51.64 -1 328 ASP B OD2   1 
ATOM   8210  N  N     . ASN B 1 329 ? 96.462  145.638 132.648 1.00 40.44 ?  329 ASN B N     1 
ATOM   8211  C  CA    . ASN B 1 329 ? 96.962  146.282 131.442 1.00 39.47 ?  329 ASN B CA    1 
ATOM   8212  C  C     . ASN B 1 329 ? 97.170  145.241 130.350 1.00 47.37 ?  329 ASN B C     1 
ATOM   8213  O  O     . ASN B 1 329 ? 97.994  144.336 130.522 1.00 44.71 ?  329 ASN B O     1 
ATOM   8214  C  CB    . ASN B 1 329 ? 98.269  147.010 131.727 1.00 36.96 ?  329 ASN B CB    1 
ATOM   8215  C  CG    . ASN B 1 329 ? 98.544  148.121 130.736 1.00 42.80 ?  329 ASN B CG    1 
ATOM   8216  O  OD1   . ASN B 1 329 ? 98.917  147.868 129.592 1.00 47.29 ?  329 ASN B OD1   1 
ATOM   8217  N  ND2   . ASN B 1 329 ? 98.361  149.361 131.172 1.00 40.27 ?  329 ASN B ND2   1 
ATOM   8218  N  N     . PRO B 1 330 ? 96.450  145.322 129.228 1.00 49.24 ?  330 PRO B N     1 
ATOM   8219  C  CA    . PRO B 1 330 ? 96.674  144.353 128.144 1.00 43.76 ?  330 PRO B CA    1 
ATOM   8220  C  C     . PRO B 1 330 ? 98.033  144.483 127.484 1.00 41.32 ?  330 PRO B C     1 
ATOM   8221  O  O     . PRO B 1 330 ? 98.522  143.499 126.917 1.00 44.94 ?  330 PRO B O     1 
ATOM   8222  C  CB    . PRO B 1 330 ? 95.543  144.663 127.156 1.00 46.22 ?  330 PRO B CB    1 
ATOM   8223  C  CG    . PRO B 1 330 ? 95.199  146.086 127.423 1.00 43.83 ?  330 PRO B CG    1 
ATOM   8224  C  CD    . PRO B 1 330 ? 95.393  146.291 128.895 1.00 42.32 ?  330 PRO B CD    1 
ATOM   8225  N  N     . ARG B 1 331 ? 98.657  145.658 127.538 1.00 39.59 ?  331 ARG B N     1 
ATOM   8226  C  CA    . ARG B 1 331 ? 99.957  145.871 126.919 1.00 42.99 ?  331 ARG B CA    1 
ATOM   8227  C  C     . ARG B 1 331 ? 101.112 145.401 127.795 1.00 42.42 ?  331 ARG B C     1 
ATOM   8228  O  O     . ARG B 1 331 ? 102.262 145.437 127.347 1.00 41.85 ?  331 ARG B O     1 
ATOM   8229  C  CB    . ARG B 1 331 ? 100.132 147.351 126.570 1.00 40.58 ?  331 ARG B CB    1 
ATOM   8230  C  CG    . ARG B 1 331 ? 99.015  147.903 125.701 1.00 41.00 ?  331 ARG B CG    1 
ATOM   8231  C  CD    . ARG B 1 331 ? 99.081  149.423 125.604 1.00 41.46 ?  331 ARG B CD    1 
ATOM   8232  N  NE    . ARG B 1 331 ? 98.357  150.130 126.658 1.00 41.04 ?  331 ARG B NE    1 
ATOM   8233  C  CZ    . ARG B 1 331 ? 97.103  149.902 127.034 1.00 45.31 ?  331 ARG B CZ    1 
ATOM   8234  N  NH1   . ARG B 1 331 ? 96.326  149.042 126.396 1.00 45.36 1  331 ARG B NH1   1 
ATOM   8235  N  NH2   . ARG B 1 331 ? 96.604  150.581 128.064 1.00 42.03 ?  331 ARG B NH2   1 
ATOM   8236  N  N     . VAL B 1 332 ? 100.835 144.972 129.021 1.00 37.76 ?  332 VAL B N     1 
ATOM   8237  C  CA    . VAL B 1 332 ? 101.838 144.388 129.903 1.00 34.85 ?  332 VAL B CA    1 
ATOM   8238  C  C     . VAL B 1 332 ? 101.730 142.875 129.788 1.00 38.85 ?  332 VAL B C     1 
ATOM   8239  O  O     . VAL B 1 332 ? 100.656 142.302 130.007 1.00 40.26 ?  332 VAL B O     1 
ATOM   8240  C  CB    . VAL B 1 332 ? 101.649 144.852 131.356 1.00 35.51 ?  332 VAL B CB    1 
ATOM   8241  C  CG1   . VAL B 1 332 ? 102.449 143.973 132.301 1.00 37.32 ?  332 VAL B CG1   1 
ATOM   8242  C  CG2   . VAL B 1 332 ? 102.058 146.307 131.506 1.00 34.26 ?  332 VAL B CG2   1 
ATOM   8243  N  N     . LYS B 1 333 ? 102.834 142.225 129.434 1.00 34.79 ?  333 LYS B N     1 
ATOM   8244  C  CA    . LYS B 1 333 ? 102.852 140.781 129.248 1.00 31.33 ?  333 LYS B CA    1 
ATOM   8245  C  C     . LYS B 1 333 ? 103.162 140.080 130.564 1.00 34.52 ?  333 LYS B C     1 
ATOM   8246  O  O     . LYS B 1 333 ? 104.014 140.527 131.337 1.00 35.76 ?  333 LYS B O     1 
ATOM   8247  C  CB    . LYS B 1 333 ? 103.876 140.389 128.182 1.00 30.40 ?  333 LYS B CB    1 
ATOM   8248  C  CG    . LYS B 1 333 ? 103.694 138.986 127.635 1.00 37.96 ?  333 LYS B CG    1 
ATOM   8249  C  CD    . LYS B 1 333 ? 104.834 138.601 126.709 1.00 38.66 ?  333 LYS B CD    1 
ATOM   8250  C  CE    . LYS B 1 333 ? 104.714 137.156 126.260 1.00 38.80 ?  333 LYS B CE    1 
ATOM   8251  N  NZ    . LYS B 1 333 ? 105.813 136.769 125.335 1.00 40.45 1  333 LYS B NZ    1 
ATOM   8252  N  N     . LYS B 1 334 ? 102.460 138.976 130.814 1.00 37.10 ?  334 LYS B N     1 
ATOM   8253  C  CA    . LYS B 1 334 ? 102.598 138.244 132.064 1.00 32.47 ?  334 LYS B CA    1 
ATOM   8254  C  C     . LYS B 1 334 ? 102.235 136.786 131.833 1.00 35.58 ?  334 LYS B C     1 
ATOM   8255  O  O     . LYS B 1 334 ? 101.588 136.439 130.843 1.00 43.50 ?  334 LYS B O     1 
ATOM   8256  C  CB    . LYS B 1 334 ? 101.706 138.841 133.156 1.00 33.98 ?  334 LYS B CB    1 
ATOM   8257  C  CG    . LYS B 1 334 ? 100.241 138.910 132.761 1.00 35.77 ?  334 LYS B CG    1 
ATOM   8258  C  CD    . LYS B 1 334 ? 99.496  139.986 133.521 1.00 33.80 ?  334 LYS B CD    1 
ATOM   8259  C  CE    . LYS B 1 334 ? 99.392  141.255 132.700 1.00 37.85 ?  334 LYS B CE    1 
ATOM   8260  N  NZ    . LYS B 1 334 ? 98.411  141.133 131.587 1.00 37.62 1  334 LYS B NZ    1 
ATOM   8261  N  N     . GLU B 1 335 ? 102.666 135.928 132.758 1.00 38.13 ?  335 GLU B N     1 
ATOM   8262  C  CA    . GLU B 1 335 ? 102.191 134.552 132.819 1.00 43.58 ?  335 GLU B CA    1 
ATOM   8263  C  C     . GLU B 1 335 ? 101.746 134.229 134.236 1.00 41.91 ?  335 GLU B C     1 
ATOM   8264  O  O     . GLU B 1 335 ? 102.334 134.710 135.208 1.00 44.95 ?  335 GLU B O     1 
ATOM   8265  C  CB    . GLU B 1 335 ? 103.246 133.526 132.394 1.00 39.57 ?  335 GLU B CB    1 
ATOM   8266  C  CG    . GLU B 1 335 ? 104.680 133.917 132.622 1.00 40.04 ?  335 GLU B CG    1 
ATOM   8267  C  CD    . GLU B 1 335 ? 105.629 132.996 131.884 1.00 47.14 ?  335 GLU B CD    1 
ATOM   8268  O  OE1   . GLU B 1 335 ? 106.551 132.454 132.529 1.00 44.33 ?  335 GLU B OE1   1 
ATOM   8269  O  OE2   . GLU B 1 335 ? 105.451 132.810 130.662 1.00 46.65 -1 335 GLU B OE2   1 
ATOM   8270  N  N     . LYS B 1 336 ? 100.709 133.403 134.340 1.00 38.84 ?  336 LYS B N     1 
ATOM   8271  C  CA    . LYS B 1 336 ? 100.210 132.977 135.638 1.00 30.35 ?  336 LYS B CA    1 
ATOM   8272  C  C     . LYS B 1 336 ? 101.232 132.094 136.343 1.00 37.36 ?  336 LYS B C     1 
ATOM   8273  O  O     . LYS B 1 336 ? 101.896 131.263 135.718 1.00 40.56 ?  336 LYS B O     1 
ATOM   8274  C  CB    . LYS B 1 336 ? 98.896  132.216 135.472 1.00 40.33 ?  336 LYS B CB    1 
ATOM   8275  C  CG    . LYS B 1 336 ? 98.079  132.093 136.743 1.00 43.04 ?  336 LYS B CG    1 
ATOM   8276  C  CD    . LYS B 1 336 ? 97.178  133.299 136.915 1.00 44.70 ?  336 LYS B CD    1 
ATOM   8277  C  CE    . LYS B 1 336 ? 95.816  133.056 136.290 1.00 41.52 ?  336 LYS B CE    1 
ATOM   8278  N  NZ    . LYS B 1 336 ? 94.915  132.302 137.202 1.00 41.81 1  336 LYS B NZ    1 
ATOM   8279  N  N     . ILE B 1 337 ? 101.361 132.286 137.655 1.00 38.68 ?  337 ILE B N     1 
ATOM   8280  C  CA    . ILE B 1 337 ? 102.151 131.411 138.510 1.00 36.88 ?  337 ILE B CA    1 
ATOM   8281  C  C     . ILE B 1 337 ? 101.333 131.104 139.755 1.00 39.62 ?  337 ILE B C     1 
ATOM   8282  O  O     . ILE B 1 337 ? 100.336 131.763 140.053 1.00 45.76 ?  337 ILE B O     1 
ATOM   8283  C  CB    . ILE B 1 337 ? 103.512 132.023 138.902 1.00 35.97 ?  337 ILE B CB    1 
ATOM   8284  C  CG1   . ILE B 1 337 ? 103.311 133.372 139.594 1.00 37.24 ?  337 ILE B CG1   1 
ATOM   8285  C  CG2   . ILE B 1 337 ? 104.418 132.153 137.689 1.00 37.46 ?  337 ILE B CG2   1 
ATOM   8286  C  CD1   . ILE B 1 337 ? 104.318 133.659 140.679 1.00 33.60 ?  337 ILE B CD1   1 
ATOM   8287  N  N     . ASN B 1 338 ? 101.767 130.081 140.485 1.00 38.80 ?  338 ASN B N     1 
ATOM   8288  C  CA    . ASN B 1 338 ? 101.197 129.793 141.790 1.00 34.32 ?  338 ASN B CA    1 
ATOM   8289  C  C     . ASN B 1 338 ? 102.149 130.319 142.850 1.00 35.85 ?  338 ASN B C     1 
ATOM   8290  O  O     . ASN B 1 338 ? 103.241 129.756 143.019 1.00 42.95 ?  338 ASN B O     1 
ATOM   8291  C  CB    . ASN B 1 338 ? 100.970 128.294 141.968 1.00 35.42 ?  338 ASN B CB    1 
ATOM   8292  C  CG    . ASN B 1 338 ? 99.963  127.984 143.055 1.00 39.78 ?  338 ASN B CG    1 
ATOM   8293  O  OD1   . ASN B 1 338 ? 99.511  128.876 143.772 1.00 41.66 ?  338 ASN B OD1   1 
ATOM   8294  N  ND2   . ASN B 1 338 ? 99.601  126.713 143.182 1.00 39.95 ?  338 ASN B ND2   1 
ATOM   8295  N  N     . PRO B 1 339 ? 101.804 131.392 143.566 1.00 36.61 ?  339 PRO B N     1 
ATOM   8296  C  CA    . PRO B 1 339 ? 102.737 131.933 144.565 1.00 34.86 ?  339 PRO B CA    1 
ATOM   8297  C  C     . PRO B 1 339 ? 103.070 130.956 145.677 1.00 32.01 ?  339 PRO B C     1 
ATOM   8298  O  O     . PRO B 1 339 ? 104.202 130.968 146.177 1.00 36.23 ?  339 PRO B O     1 
ATOM   8299  C  CB    . PRO B 1 339 ? 102.001 133.170 145.096 1.00 33.12 ?  339 PRO B CB    1 
ATOM   8300  C  CG    . PRO B 1 339 ? 100.571 132.906 144.815 1.00 36.79 ?  339 PRO B CG    1 
ATOM   8301  C  CD    . PRO B 1 339 ? 100.538 132.141 143.531 1.00 36.01 ?  339 PRO B CD    1 
ATOM   8302  N  N     . ARG B 1 340 ? 102.123 130.110 146.083 1.00 33.55 ?  340 ARG B N     1 
ATOM   8303  C  CA    . ARG B 1 340 ? 102.425 129.107 147.097 1.00 32.24 ?  340 ARG B CA    1 
ATOM   8304  C  C     . ARG B 1 340 ? 103.389 128.059 146.560 1.00 33.47 ?  340 ARG B C     1 
ATOM   8305  O  O     . ARG B 1 340 ? 104.289 127.610 147.277 1.00 39.77 ?  340 ARG B O     1 
ATOM   8306  C  CB    . ARG B 1 340 ? 101.139 128.454 147.596 1.00 31.38 ?  340 ARG B CB    1 
ATOM   8307  C  CG    . ARG B 1 340 ? 100.322 129.345 148.503 1.00 29.58 ?  340 ARG B CG    1 
ATOM   8308  C  CD    . ARG B 1 340 ? 99.398  128.542 149.396 1.00 31.39 ?  340 ARG B CD    1 
ATOM   8309  N  NE    . ARG B 1 340 ? 98.482  129.407 150.128 1.00 33.49 ?  340 ARG B NE    1 
ATOM   8310  C  CZ    . ARG B 1 340 ? 97.570  128.979 150.988 1.00 35.94 ?  340 ARG B CZ    1 
ATOM   8311  N  NH1   . ARG B 1 340 ? 97.424  127.692 151.255 1.00 35.30 1  340 ARG B NH1   1 
ATOM   8312  N  NH2   . ARG B 1 340 ? 96.784  129.863 151.594 1.00 36.79 ?  340 ARG B NH2   1 
ATOM   8313  N  N     . LYS B 1 341 ? 103.216 127.658 145.300 1.00 34.62 ?  341 LYS B N     1 
ATOM   8314  C  CA    . LYS B 1 341 ? 104.166 126.734 144.690 1.00 33.59 ?  341 LYS B CA    1 
ATOM   8315  C  C     . LYS B 1 341 ? 105.542 127.369 144.562 1.00 30.60 ?  341 LYS B C     1 
ATOM   8316  O  O     . LYS B 1 341 ? 106.560 126.695 144.746 1.00 32.98 ?  341 LYS B O     1 
ATOM   8317  C  CB    . LYS B 1 341 ? 103.653 126.272 143.326 1.00 37.60 ?  341 LYS B CB    1 
ATOM   8318  C  CG    . LYS B 1 341 ? 102.564 125.210 143.392 1.00 38.96 ?  341 LYS B CG    1 
ATOM   8319  C  CD    . LYS B 1 341 ? 102.673 124.367 144.655 1.00 40.97 ?  341 LYS B CD    1 
ATOM   8320  C  CE    . LYS B 1 341 ? 101.671 123.227 144.648 1.00 41.70 ?  341 LYS B CE    1 
ATOM   8321  N  NZ    . LYS B 1 341 ? 102.322 121.922 144.943 1.00 40.34 1  341 LYS B NZ    1 
ATOM   8322  N  N     . LEU B 1 342 ? 105.596 128.666 144.251 1.00 32.33 ?  342 LEU B N     1 
ATOM   8323  C  CA    . LEU B 1 342 ? 106.880 129.357 144.202 1.00 29.16 ?  342 LEU B CA    1 
ATOM   8324  C  C     . LEU B 1 342 ? 107.529 129.418 145.580 1.00 29.99 ?  342 LEU B C     1 
ATOM   8325  O  O     . LEU B 1 342 ? 108.748 129.255 145.703 1.00 38.62 ?  342 LEU B O     1 
ATOM   8326  C  CB    . LEU B 1 342 ? 106.700 130.761 143.625 1.00 28.81 ?  342 LEU B CB    1 
ATOM   8327  C  CG    . LEU B 1 342 ? 107.966 131.436 143.093 1.00 29.11 ?  342 LEU B CG    1 
ATOM   8328  C  CD1   . LEU B 1 342 ? 108.794 130.457 142.280 1.00 28.49 ?  342 LEU B CD1   1 
ATOM   8329  C  CD2   . LEU B 1 342 ? 107.617 132.657 142.263 1.00 28.15 ?  342 LEU B CD2   1 
ATOM   8330  N  N     . LEU B 1 343 ? 106.734 129.648 146.627 1.00 27.61 ?  343 LEU B N     1 
ATOM   8331  C  CA    . LEU B 1 343 ? 107.270 129.636 147.986 1.00 29.13 ?  343 LEU B CA    1 
ATOM   8332  C  C     . LEU B 1 343 ? 107.802 128.260 148.359 1.00 28.50 ?  343 LEU B C     1 
ATOM   8333  O  O     . LEU B 1 343 ? 108.864 128.140 148.983 1.00 32.52 ?  343 LEU B O     1 
ATOM   8334  C  CB    . LEU B 1 343 ? 106.192 130.075 148.975 1.00 31.73 ?  343 LEU B CB    1 
ATOM   8335  C  CG    . LEU B 1 343 ? 106.155 131.551 149.363 1.00 32.63 ?  343 LEU B CG    1 
ATOM   8336  C  CD1   . LEU B 1 343 ? 105.004 131.812 150.315 1.00 27.04 ?  343 LEU B CD1   1 
ATOM   8337  C  CD2   . LEU B 1 343 ? 107.474 131.975 149.984 1.00 33.94 ?  343 LEU B CD2   1 
ATOM   8338  N  N     . GLU B 1 344 ? 107.068 127.206 148.000 1.00 34.65 ?  344 GLU B N     1 
ATOM   8339  C  CA    . GLU B 1 344 ? 107.532 125.852 148.280 1.00 32.82 ?  344 GLU B CA    1 
ATOM   8340  C  C     . GLU B 1 344 ? 108.800 125.534 147.501 1.00 29.44 ?  344 GLU B C     1 
ATOM   8341  O  O     . GLU B 1 344 ? 109.691 124.846 148.008 1.00 34.99 ?  344 GLU B O     1 
ATOM   8342  C  CB    . GLU B 1 344 ? 106.430 124.843 147.963 1.00 35.28 ?  344 GLU B CB    1 
ATOM   8343  C  CG    . GLU B 1 344 ? 105.183 125.007 148.814 1.00 36.66 ?  344 GLU B CG    1 
ATOM   8344  C  CD    . GLU B 1 344 ? 104.048 124.113 148.359 1.00 45.78 ?  344 GLU B CD    1 
ATOM   8345  O  OE1   . GLU B 1 344 ? 104.329 123.031 147.802 1.00 44.97 ?  344 GLU B OE1   1 
ATOM   8346  O  OE2   . GLU B 1 344 ? 102.875 124.494 148.555 1.00 43.83 -1 344 GLU B OE2   1 
ATOM   8347  N  N     . LYS B 1 345 ? 108.899 126.027 146.265 1.00 29.73 ?  345 LYS B N     1 
ATOM   8348  C  CA    . LYS B 1 345 ? 110.122 125.858 145.489 1.00 28.05 ?  345 LYS B CA    1 
ATOM   8349  C  C     . LYS B 1 345 ? 111.288 126.589 146.138 1.00 33.02 ?  345 LYS B C     1 
ATOM   8350  O  O     . LYS B 1 345 ? 112.412 126.076 146.167 1.00 36.04 ?  345 LYS B O     1 
ATOM   8351  C  CB    . LYS B 1 345 ? 109.902 126.351 144.060 1.00 29.85 ?  345 LYS B CB    1 
ATOM   8352  C  CG    . LYS B 1 345 ? 111.098 126.171 143.148 1.00 30.65 ?  345 LYS B CG    1 
ATOM   8353  C  CD    . LYS B 1 345 ? 110.798 126.665 141.747 1.00 29.51 ?  345 LYS B CD    1 
ATOM   8354  C  CE    . LYS B 1 345 ? 112.025 126.576 140.862 1.00 34.19 ?  345 LYS B CE    1 
ATOM   8355  N  NZ    . LYS B 1 345 ? 111.773 127.135 139.509 1.00 34.65 1  345 LYS B NZ    1 
ATOM   8356  N  N     . LEU B 1 346 ? 111.038 127.791 146.665 1.00 33.81 ?  346 LEU B N     1 
ATOM   8357  C  CA    . LEU B 1 346 ? 112.074 128.520 147.390 1.00 27.40 ?  346 LEU B CA    1 
ATOM   8358  C  C     . LEU B 1 346 ? 112.551 127.728 148.599 1.00 25.79 ?  346 LEU B C     1 
ATOM   8359  O  O     . LEU B 1 346 ? 113.755 127.600 148.837 1.00 28.42 ?  346 LEU B O     1 
ATOM   8360  C  CB    . LEU B 1 346 ? 111.549 129.887 147.829 1.00 27.66 ?  346 LEU B CB    1 
ATOM   8361  C  CG    . LEU B 1 346 ? 111.292 130.958 146.772 1.00 26.18 ?  346 LEU B CG    1 
ATOM   8362  C  CD1   . LEU B 1 346 ? 110.677 132.186 147.415 1.00 30.49 ?  346 LEU B CD1   1 
ATOM   8363  C  CD2   . LEU B 1 346 ? 112.574 131.315 146.059 1.00 27.88 ?  346 LEU B CD2   1 
ATOM   8364  N  N     . ALA B 1 347 ? 111.610 127.184 149.374 1.00 26.69 ?  347 ALA B N     1 
ATOM   8365  C  CA    . ALA B 1 347 ? 111.982 126.419 150.559 1.00 20.04 ?  347 ALA B CA    1 
ATOM   8366  C  C     . ALA B 1 347 ? 112.744 125.153 150.187 1.00 27.48 ?  347 ALA B C     1 
ATOM   8367  O  O     . ALA B 1 347 ? 113.714 124.784 150.858 1.00 35.93 ?  347 ALA B O     1 
ATOM   8368  C  CB    . ALA B 1 347 ? 110.739 126.077 151.376 1.00 19.98 ?  347 ALA B CB    1 
ATOM   8369  N  N     . MET B 1 348 ? 112.315 124.471 149.123 1.00 33.95 ?  348 MET B N     1 
ATOM   8370  C  CA    . MET B 1 348 ? 113.022 123.279 148.666 1.00 31.21 ?  348 MET B CA    1 
ATOM   8371  C  C     . MET B 1 348 ? 114.440 123.615 148.226 1.00 31.70 ?  348 MET B C     1 
ATOM   8372  O  O     . MET B 1 348 ? 115.388 122.889 148.546 1.00 40.09 ?  348 MET B O     1 
ATOM   8373  C  CB    . MET B 1 348 ? 112.239 122.620 147.528 1.00 33.42 ?  348 MET B CB    1 
ATOM   8374  C  CG    . MET B 1 348 ? 112.975 121.501 146.812 1.00 40.99 ?  348 MET B CG    1 
ATOM   8375  S  SD    . MET B 1 348 ? 113.742 122.028 145.266 1.00 60.89 ?  348 MET B SD    1 
ATOM   8376  C  CE    . MET B 1 348 ? 112.417 122.978 144.526 1.00 38.33 ?  348 MET B CE    1 
ATOM   8377  N  N     . LEU B 1 349 ? 114.604 124.721 147.498 1.00 26.74 ?  349 LEU B N     1 
ATOM   8378  C  CA    . LEU B 1 349 ? 115.931 125.127 147.057 1.00 27.33 ?  349 LEU B CA    1 
ATOM   8379  C  C     . LEU B 1 349 ? 116.818 125.495 148.237 1.00 28.95 ?  349 LEU B C     1 
ATOM   8380  O  O     . LEU B 1 349 ? 118.015 125.188 148.241 1.00 32.49 ?  349 LEU B O     1 
ATOM   8381  C  CB    . LEU B 1 349 ? 115.816 126.298 146.086 1.00 27.93 ?  349 LEU B CB    1 
ATOM   8382  C  CG    . LEU B 1 349 ? 115.772 125.913 144.609 1.00 33.81 ?  349 LEU B CG    1 
ATOM   8383  C  CD1   . LEU B 1 349 ? 114.983 126.944 143.840 1.00 34.75 ?  349 LEU B CD1   1 
ATOM   8384  C  CD2   . LEU B 1 349 ? 117.175 125.781 144.051 1.00 33.96 ?  349 LEU B CD2   1 
ATOM   8385  N  N     . ARG B 1 350 ? 116.258 126.171 149.243 1.00 26.35 ?  350 ARG B N     1 
ATOM   8386  C  CA    . ARG B 1 350 ? 117.046 126.517 150.422 1.00 22.58 ?  350 ARG B CA    1 
ATOM   8387  C  C     . ARG B 1 350 ? 117.426 125.281 151.224 1.00 30.68 ?  350 ARG B C     1 
ATOM   8388  O  O     . ARG B 1 350 ? 118.528 125.220 151.780 1.00 41.06 ?  350 ARG B O     1 
ATOM   8389  C  CB    . ARG B 1 350 ? 116.287 127.511 151.299 1.00 25.27 ?  350 ARG B CB    1 
ATOM   8390  C  CG    . ARG B 1 350 ? 115.908 128.798 150.590 1.00 24.47 ?  350 ARG B CG    1 
ATOM   8391  C  CD    . ARG B 1 350 ? 115.536 129.882 151.576 1.00 26.29 ?  350 ARG B CD    1 
ATOM   8392  N  NE    . ARG B 1 350 ? 116.644 130.801 151.800 1.00 33.09 ?  350 ARG B NE    1 
ATOM   8393  C  CZ    . ARG B 1 350 ? 117.034 131.222 152.994 1.00 28.82 ?  350 ARG B CZ    1 
ATOM   8394  N  NH1   . ARG B 1 350 ? 116.445 130.802 154.100 1.00 26.87 1  350 ARG B NH1   1 
ATOM   8395  N  NH2   . ARG B 1 350 ? 118.046 132.080 153.080 1.00 32.13 ?  350 ARG B NH2   1 
ATOM   8396  N  N     . SER B 1 351 ? 116.533 124.294 151.308 1.00 33.84 ?  351 SER B N     1 
ATOM   8397  C  CA    . SER B 1 351 ? 116.887 123.038 151.958 1.00 33.14 ?  351 SER B CA    1 
ATOM   8398  C  C     . SER B 1 351 ? 118.003 122.326 151.206 1.00 34.19 ?  351 SER B C     1 
ATOM   8399  O  O     . SER B 1 351 ? 118.937 121.797 151.820 1.00 42.75 ?  351 SER B O     1 
ATOM   8400  C  CB    . SER B 1 351 ? 115.658 122.135 152.064 1.00 34.41 ?  351 SER B CB    1 
ATOM   8401  O  OG    . SER B 1 351 ? 114.689 122.688 152.935 1.00 44.10 ?  351 SER B OG    1 
ATOM   8402  N  N     . GLU B 1 352 ? 117.925 122.305 149.875 1.00 34.56 ?  352 GLU B N     1 
ATOM   8403  C  CA    . GLU B 1 352 ? 118.898 121.549 149.092 1.00 35.03 ?  352 GLU B CA    1 
ATOM   8404  C  C     . GLU B 1 352 ? 120.261 122.231 149.065 1.00 35.91 ?  352 GLU B C     1 
ATOM   8405  O  O     . GLU B 1 352 ? 121.292 121.570 149.236 1.00 44.61 ?  352 GLU B O     1 
ATOM   8406  C  CB    . GLU B 1 352 ? 118.374 121.340 147.674 1.00 36.46 ?  352 GLU B CB    1 
ATOM   8407  C  CG    . GLU B 1 352 ? 117.269 120.305 147.577 1.00 39.07 ?  352 GLU B CG    1 
ATOM   8408  C  CD    . GLU B 1 352 ? 116.547 120.348 146.247 1.00 47.81 ?  352 GLU B CD    1 
ATOM   8409  O  OE1   . GLU B 1 352 ? 116.841 121.256 145.441 1.00 44.81 ?  352 GLU B OE1   1 
ATOM   8410  O  OE2   . GLU B 1 352 ? 115.689 119.474 146.006 1.00 45.72 -1 352 GLU B OE2   1 
ATOM   8411  N  N     . SER B 1 353 ? 120.295 123.549 148.854 1.00 36.06 ?  353 SER B N     1 
ATOM   8412  C  CA    . SER B 1 353 ? 121.548 124.252 148.615 1.00 36.19 ?  353 SER B CA    1 
ATOM   8413  C  C     . SER B 1 353 ? 121.756 125.499 149.461 1.00 30.27 ?  353 SER B C     1 
ATOM   8414  O  O     . SER B 1 353 ? 122.824 126.110 149.358 1.00 32.66 ?  353 SER B O     1 
ATOM   8415  C  CB    . SER B 1 353 ? 121.662 124.649 147.135 1.00 37.72 ?  353 SER B CB    1 
ATOM   8416  O  OG    . SER B 1 353 ? 120.730 125.665 146.810 1.00 35.84 ?  353 SER B OG    1 
ATOM   8417  N  N     . GLY B 1 354 ? 120.787 125.902 150.280 1.00 25.89 ?  354 GLY B N     1 
ATOM   8418  C  CA    . GLY B 1 354 ? 120.905 127.118 151.056 1.00 27.51 ?  354 GLY B CA    1 
ATOM   8419  C  C     . GLY B 1 354 ? 120.534 128.384 150.321 1.00 23.43 ?  354 GLY B C     1 
ATOM   8420  O  O     . GLY B 1 354 ? 120.544 129.460 150.931 1.00 27.53 ?  354 GLY B O     1 
ATOM   8421  N  N     . TYR B 1 355 ? 120.204 128.296 149.041 1.00 26.70 ?  355 TYR B N     1 
ATOM   8422  C  CA    . TYR B 1 355 ? 119.847 129.423 148.200 1.00 16.72 ?  355 TYR B CA    1 
ATOM   8423  C  C     . TYR B 1 355 ? 118.368 129.369 147.844 1.00 24.56 ?  355 TYR B C     1 
ATOM   8424  O  O     . TYR B 1 355 ? 117.758 128.296 147.852 1.00 29.05 ?  355 TYR B O     1 
ATOM   8425  C  CB    . TYR B 1 355 ? 120.686 129.420 146.915 1.00 19.98 ?  355 TYR B CB    1 
ATOM   8426  C  CG    . TYR B 1 355 ? 122.139 129.756 147.137 1.00 28.27 ?  355 TYR B CG    1 
ATOM   8427  C  CD1   . TYR B 1 355 ? 122.509 130.925 147.785 1.00 25.74 ?  355 TYR B CD1   1 
ATOM   8428  C  CD2   . TYR B 1 355 ? 123.141 128.903 146.701 1.00 30.44 ?  355 TYR B CD2   1 
ATOM   8429  C  CE1   . TYR B 1 355 ? 123.835 131.233 147.989 1.00 27.80 ?  355 TYR B CE1   1 
ATOM   8430  C  CE2   . TYR B 1 355 ? 124.471 129.205 146.902 1.00 29.65 ?  355 TYR B CE2   1 
ATOM   8431  C  CZ    . TYR B 1 355 ? 124.812 130.373 147.547 1.00 30.27 ?  355 TYR B CZ    1 
ATOM   8432  O  OH    . TYR B 1 355 ? 126.135 130.682 147.752 1.00 34.28 ?  355 TYR B OH    1 
ATOM   8433  N  N     . PRO B 1 356 ? 117.752 130.510 147.519 1.00 27.49 ?  356 PRO B N     1 
ATOM   8434  C  CA    . PRO B 1 356 ? 118.299 131.871 147.453 1.00 15.66 ?  356 PRO B CA    1 
ATOM   8435  C  C     . PRO B 1 356 ? 118.265 132.617 148.777 1.00 16.09 ?  356 PRO B C     1 
ATOM   8436  O  O     . PRO B 1 356 ? 117.635 132.185 149.734 1.00 24.60 ?  356 PRO B O     1 
ATOM   8437  C  CB    . PRO B 1 356 ? 117.380 132.540 146.431 1.00 18.31 ?  356 PRO B CB    1 
ATOM   8438  C  CG    . PRO B 1 356 ? 116.054 131.912 146.712 1.00 22.80 ?  356 PRO B CG    1 
ATOM   8439  C  CD    . PRO B 1 356 ? 116.363 130.470 147.029 1.00 13.71 ?  356 PRO B CD    1 
ATOM   8440  N  N     . TYR B 1 357 ? 118.952 133.752 148.853 1.00 21.55 ?  357 TYR B N     1 
ATOM   8441  C  CA    . TYR B 1 357 ? 118.682 134.700 149.921 1.00 13.99 ?  357 TYR B CA    1 
ATOM   8442  C  C     . TYR B 1 357 ? 117.285 135.274 149.728 1.00 17.78 ?  357 TYR B C     1 
ATOM   8443  O  O     . TYR B 1 357 ? 116.838 135.489 148.599 1.00 26.50 ?  357 TYR B O     1 
ATOM   8444  C  CB    . TYR B 1 357 ? 119.710 135.834 149.929 1.00 12.95 ?  357 TYR B CB    1 
ATOM   8445  C  CG    . TYR B 1 357 ? 121.154 135.421 149.735 1.00 16.72 ?  357 TYR B CG    1 
ATOM   8446  C  CD1   . TYR B 1 357 ? 121.627 134.211 150.214 1.00 17.56 ?  357 TYR B CD1   1 
ATOM   8447  C  CD2   . TYR B 1 357 ? 122.047 136.255 149.078 1.00 19.44 ?  357 TYR B CD2   1 
ATOM   8448  C  CE1   . TYR B 1 357 ? 122.941 133.839 150.045 1.00 19.94 ?  357 TYR B CE1   1 
ATOM   8449  C  CE2   . TYR B 1 357 ? 123.364 135.892 148.902 1.00 15.34 ?  357 TYR B CE2   1 
ATOM   8450  C  CZ    . TYR B 1 357 ? 123.805 134.682 149.387 1.00 24.11 ?  357 TYR B CZ    1 
ATOM   8451  O  OH    . TYR B 1 357 ? 125.118 134.311 149.218 1.00 31.95 ?  357 TYR B OH    1 
ATOM   8452  N  N     . ILE B 1 358 ? 116.588 135.514 150.830 1.00 25.86 ?  358 ILE B N     1 
ATOM   8453  C  CA    . ILE B 1 358 ? 115.254 136.098 150.796 1.00 18.22 ?  358 ILE B CA    1 
ATOM   8454  C  C     . ILE B 1 358 ? 115.352 137.517 151.329 1.00 19.32 ?  358 ILE B C     1 
ATOM   8455  O  O     . ILE B 1 358 ? 115.770 137.729 152.472 1.00 24.72 ?  358 ILE B O     1 
ATOM   8456  C  CB    . ILE B 1 358 ? 114.245 135.274 151.611 1.00 18.88 ?  358 ILE B CB    1 
ATOM   8457  C  CG1   . ILE B 1 358 ? 114.222 133.820 151.135 1.00 15.46 ?  358 ILE B CG1   1 
ATOM   8458  C  CG2   . ILE B 1 358 ? 112.864 135.897 151.519 1.00 17.41 ?  358 ILE B CG2   1 
ATOM   8459  C  CD1   . ILE B 1 358 ? 113.778 133.649 149.704 1.00 21.51 ?  358 ILE B CD1   1 
ATOM   8460  N  N     . MET B 1 359 ? 114.972 138.487 150.504 1.00 13.23 ?  359 MET B N     1 
ATOM   8461  C  CA    . MET B 1 359 ? 114.892 139.882 150.910 1.00 2.07  ?  359 MET B CA    1 
ATOM   8462  C  C     . MET B 1 359 ? 113.434 140.312 150.851 1.00 7.01  ?  359 MET B C     1 
ATOM   8463  O  O     . MET B 1 359 ? 112.832 140.328 149.773 1.00 20.50 ?  359 MET B O     1 
ATOM   8464  C  CB    . MET B 1 359 ? 115.761 140.768 150.019 1.00 10.80 ?  359 MET B CB    1 
ATOM   8465  C  CG    . MET B 1 359 ? 115.749 142.237 150.406 1.00 9.94  ?  359 MET B CG    1 
ATOM   8466  S  SD    . MET B 1 359 ? 115.819 143.345 148.992 1.00 38.89 ?  359 MET B SD    1 
ATOM   8467  C  CE    . MET B 1 359 ? 114.936 144.762 149.622 1.00 16.35 ?  359 MET B CE    1 
ATOM   8468  N  N     . PHE B 1 360 ? 112.868 140.639 152.007 1.00 13.11 ?  360 PHE B N     1 
ATOM   8469  C  CA    . PHE B 1 360 ? 111.480 141.087 152.082 1.00 5.13  ?  360 PHE B CA    1 
ATOM   8470  C  C     . PHE B 1 360 ? 111.457 142.576 151.766 1.00 13.75 ?  360 PHE B C     1 
ATOM   8471  O  O     . PHE B 1 360 ? 111.799 143.407 152.608 1.00 21.20 ?  360 PHE B O     1 
ATOM   8472  C  CB    . PHE B 1 360 ? 110.894 140.780 153.454 1.00 11.94 ?  360 PHE B CB    1 
ATOM   8473  C  CG    . PHE B 1 360 ? 110.818 139.311 153.758 1.00 16.25 ?  360 PHE B CG    1 
ATOM   8474  C  CD1   . PHE B 1 360 ? 110.009 138.475 153.006 1.00 19.55 ?  360 PHE B CD1   1 
ATOM   8475  C  CD2   . PHE B 1 360 ? 111.575 138.762 154.777 1.00 13.35 ?  360 PHE B CD2   1 
ATOM   8476  C  CE1   . PHE B 1 360 ? 109.945 137.123 153.277 1.00 18.52 ?  360 PHE B CE1   1 
ATOM   8477  C  CE2   . PHE B 1 360 ? 111.515 137.412 155.052 1.00 18.20 ?  360 PHE B CE2   1 
ATOM   8478  C  CZ    . PHE B 1 360 ? 110.699 136.592 154.302 1.00 15.01 ?  360 PHE B CZ    1 
ATOM   8479  N  N     . GLN B 1 361 ? 111.039 142.906 150.541 1.00 18.99 ?  361 GLN B N     1 
ATOM   8480  C  CA    . GLN B 1 361 ? 111.199 144.261 150.020 1.00 9.60  ?  361 GLN B CA    1 
ATOM   8481  C  C     . GLN B 1 361 ? 110.472 145.290 150.876 1.00 9.13  ?  361 GLN B C     1 
ATOM   8482  O  O     . GLN B 1 361 ? 111.015 146.360 151.166 1.00 14.03 ?  361 GLN B O     1 
ATOM   8483  C  CB    . GLN B 1 361 ? 110.696 144.317 148.577 1.00 19.01 ?  361 GLN B CB    1 
ATOM   8484  C  CG    . GLN B 1 361 ? 110.596 145.713 147.997 1.00 20.19 ?  361 GLN B CG    1 
ATOM   8485  C  CD    . GLN B 1 361 ? 111.587 145.955 146.883 1.00 20.87 ?  361 GLN B CD    1 
ATOM   8486  O  OE1   . GLN B 1 361 ? 111.713 145.150 145.963 1.00 30.14 ?  361 GLN B OE1   1 
ATOM   8487  N  NE2   . GLN B 1 361 ? 112.304 147.069 146.959 1.00 20.20 ?  361 GLN B NE2   1 
ATOM   8488  N  N     . ASP B 1 362 ? 109.241 144.990 151.287 1.00 23.19 ?  362 ASP B N     1 
ATOM   8489  C  CA    . ASP B 1 362 ? 108.457 145.963 152.037 1.00 13.79 ?  362 ASP B CA    1 
ATOM   8490  C  C     . ASP B 1 362 ? 108.857 146.041 153.503 1.00 13.78 ?  362 ASP B C     1 
ATOM   8491  O  O     . ASP B 1 362 ? 108.610 147.069 154.140 1.00 23.01 ?  362 ASP B O     1 
ATOM   8492  C  CB    . ASP B 1 362 ? 106.968 145.648 151.910 1.00 16.01 ?  362 ASP B CB    1 
ATOM   8493  C  CG    . ASP B 1 362 ? 106.481 145.719 150.474 1.00 27.61 ?  362 ASP B CG    1 
ATOM   8494  O  OD1   . ASP B 1 362 ? 107.317 145.596 149.554 1.00 24.96 ?  362 ASP B OD1   1 
ATOM   8495  O  OD2   . ASP B 1 362 ? 105.268 145.916 150.261 1.00 37.15 -1 362 ASP B OD2   1 
ATOM   8496  N  N     . ASN B 1 363 ? 109.461 144.987 154.054 1.00 28.56 ?  363 ASN B N     1 
ATOM   8497  C  CA    . ASN B 1 363 ? 110.039 145.092 155.389 1.00 13.54 ?  363 ASN B CA    1 
ATOM   8498  C  C     . ASN B 1 363 ? 111.217 146.057 155.396 1.00 19.84 ?  363 ASN B C     1 
ATOM   8499  O  O     . ASN B 1 363 ? 111.395 146.823 156.349 1.00 25.82 ?  363 ASN B O     1 
ATOM   8500  C  CB    . ASN B 1 363 ? 110.472 143.715 155.891 1.00 10.51 ?  363 ASN B CB    1 
ATOM   8501  C  CG    . ASN B 1 363 ? 109.316 142.899 156.422 1.00 17.88 ?  363 ASN B CG    1 
ATOM   8502  O  OD1   . ASN B 1 363 ? 108.207 143.403 156.583 1.00 22.12 ?  363 ASN B OD1   1 
ATOM   8503  N  ND2   . ASN B 1 363 ? 109.570 141.628 156.703 1.00 20.62 ?  363 ASN B ND2   1 
ATOM   8504  N  N     . VAL B 1 364 ? 112.032 146.028 154.342 1.00 17.04 ?  364 VAL B N     1 
ATOM   8505  C  CA    . VAL B 1 364 ? 113.164 146.940 154.245 1.00 10.09 ?  364 VAL B CA    1 
ATOM   8506  C  C     . VAL B 1 364 ? 112.683 148.374 154.071 1.00 19.58 ?  364 VAL B C     1 
ATOM   8507  O  O     . VAL B 1 364 ? 113.152 149.293 154.752 1.00 25.50 ?  364 VAL B O     1 
ATOM   8508  C  CB    . VAL B 1 364 ? 114.091 146.520 153.091 1.00 0.06  ?  364 VAL B CB    1 
ATOM   8509  C  CG1   . VAL B 1 364 ? 115.326 147.390 153.067 1.00 7.05  ?  364 VAL B CG1   1 
ATOM   8510  C  CG2   . VAL B 1 364 ? 114.465 145.059 153.212 1.00 3.59  ?  364 VAL B CG2   1 
ATOM   8511  N  N     . ASN B 1 365 ? 111.736 148.587 153.158 1.00 14.89 ?  365 ASN B N     1 
ATOM   8512  C  CA    . ASN B 1 365 ? 111.384 149.932 152.728 1.00 4.58  ?  365 ASN B CA    1 
ATOM   8513  C  C     . ASN B 1 365 ? 110.359 150.612 153.622 1.00 12.69 ?  365 ASN B C     1 
ATOM   8514  O  O     . ASN B 1 365 ? 110.178 151.828 153.506 1.00 24.10 ?  365 ASN B O     1 
ATOM   8515  C  CB    . ASN B 1 365 ? 110.869 149.897 151.291 1.00 18.94 ?  365 ASN B CB    1 
ATOM   8516  C  CG    . ASN B 1 365 ? 111.945 149.506 150.303 1.00 16.80 ?  365 ASN B CG    1 
ATOM   8517  O  OD1   . ASN B 1 365 ? 113.004 150.126 150.248 1.00 14.28 ?  365 ASN B OD1   1 
ATOM   8518  N  ND2   . ASN B 1 365 ? 111.682 148.471 149.520 1.00 18.87 ?  365 ASN B ND2   1 
ATOM   8519  N  N     . LYS B 1 366 ? 109.686 149.875 154.508 1.00 16.21 ?  366 LYS B N     1 
ATOM   8520  C  CA    . LYS B 1 366 ? 108.761 150.516 155.433 1.00 19.85 ?  366 LYS B CA    1 
ATOM   8521  C  C     . LYS B 1 366 ? 109.489 151.263 156.538 1.00 20.14 ?  366 LYS B C     1 
ATOM   8522  O  O     . LYS B 1 366 ? 108.907 152.163 157.153 1.00 30.80 ?  366 LYS B O     1 
ATOM   8523  C  CB    . LYS B 1 366 ? 107.805 149.483 156.029 1.00 16.52 ?  366 LYS B CB    1 
ATOM   8524  C  CG    . LYS B 1 366 ? 108.391 148.651 157.153 1.00 25.80 ?  366 LYS B CG    1 
ATOM   8525  C  CD    . LYS B 1 366 ? 107.296 147.951 157.935 1.00 28.53 ?  366 LYS B CD    1 
ATOM   8526  C  CE    . LYS B 1 366 ? 106.392 147.147 157.016 1.00 23.89 ?  366 LYS B CE    1 
ATOM   8527  N  NZ    . LYS B 1 366 ? 105.447 146.293 157.786 1.00 28.97 1  366 LYS B NZ    1 
ATOM   8528  N  N     . VAL B 1 367 ? 110.749 150.916 156.797 1.00 26.19 ?  367 VAL B N     1 
ATOM   8529  C  CA    . VAL B 1 367 ? 111.584 151.595 157.774 1.00 18.01 ?  367 VAL B CA    1 
ATOM   8530  C  C     . VAL B 1 367 ? 112.801 152.239 157.127 1.00 17.99 ?  367 VAL B C     1 
ATOM   8531  O  O     . VAL B 1 367 ? 113.675 152.748 157.825 1.00 23.59 ?  367 VAL B O     1 
ATOM   8532  C  CB    . VAL B 1 367 ? 112.011 150.635 158.903 1.00 14.88 ?  367 VAL B CB    1 
ATOM   8533  C  CG1   . VAL B 1 367 ? 110.808 150.238 159.737 1.00 17.71 ?  367 VAL B CG1   1 
ATOM   8534  C  CG2   . VAL B 1 367 ? 112.680 149.413 158.318 1.00 8.15  ?  367 VAL B CG2   1 
ATOM   8535  N  N     . HIS B 1 368 ? 112.877 152.216 155.798 1.00 17.51 ?  368 HIS B N     1 
ATOM   8536  C  CA    . HIS B 1 368 ? 113.996 152.820 155.093 1.00 3.61  ?  368 HIS B CA    1 
ATOM   8537  C  C     . HIS B 1 368 ? 113.944 154.335 155.235 1.00 17.40 ?  368 HIS B C     1 
ATOM   8538  O  O     . HIS B 1 368 ? 112.892 154.953 155.051 1.00 30.35 ?  368 HIS B O     1 
ATOM   8539  C  CB    . HIS B 1 368 ? 113.965 152.420 153.621 1.00 10.78 ?  368 HIS B CB    1 
ATOM   8540  C  CG    . HIS B 1 368 ? 115.161 152.870 152.843 1.00 6.15  ?  368 HIS B CG    1 
ATOM   8541  N  ND1   . HIS B 1 368 ? 115.088 153.245 151.521 1.00 18.67 ?  368 HIS B ND1   1 
ATOM   8542  C  CD2   . HIS B 1 368 ? 116.459 153.004 153.201 1.00 7.27  ?  368 HIS B CD2   1 
ATOM   8543  C  CE1   . HIS B 1 368 ? 116.290 153.590 151.095 1.00 17.56 ?  368 HIS B CE1   1 
ATOM   8544  N  NE2   . HIS B 1 368 ? 117.139 153.454 152.096 1.00 16.59 ?  368 HIS B NE2   1 
ATOM   8545  N  N     . ALA B 1 369 ? 115.085 154.933 155.567 1.00 20.81 ?  369 ALA B N     1 
ATOM   8546  C  CA    . ALA B 1 369 ? 115.157 156.363 155.821 1.00 13.95 ?  369 ALA B CA    1 
ATOM   8547  C  C     . ALA B 1 369 ? 115.444 157.184 154.573 1.00 25.08 ?  369 ALA B C     1 
ATOM   8548  O  O     . ALA B 1 369 ? 115.405 158.416 154.643 1.00 32.91 ?  369 ALA B O     1 
ATOM   8549  C  CB    . ALA B 1 369 ? 116.228 156.654 156.876 1.00 11.15 ?  369 ALA B CB    1 
ATOM   8550  N  N     . ASN B 1 370 ? 115.718 156.545 153.442 1.00 18.57 ?  370 ASN B N     1 
ATOM   8551  C  CA    . ASN B 1 370 ? 116.114 157.239 152.224 1.00 12.01 ?  370 ASN B CA    1 
ATOM   8552  C  C     . ASN B 1 370 ? 115.277 156.780 151.042 1.00 13.34 ?  370 ASN B C     1 
ATOM   8553  O  O     . ASN B 1 370 ? 115.788 156.580 149.938 1.00 24.87 ?  370 ASN B O     1 
ATOM   8554  C  CB    . ASN B 1 370 ? 117.600 157.039 151.942 1.00 12.83 ?  370 ASN B CB    1 
ATOM   8555  C  CG    . ASN B 1 370 ? 118.483 157.624 153.025 1.00 12.83 ?  370 ASN B CG    1 
ATOM   8556  O  OD1   . ASN B 1 370 ? 118.470 158.830 153.266 1.00 29.53 ?  370 ASN B OD1   1 
ATOM   8557  N  ND2   . ASN B 1 370 ? 119.253 156.771 153.684 1.00 12.13 ?  370 ASN B ND2   1 
ATOM   8558  N  N     . ASN B 1 371 ? 113.970 156.606 151.255 1.00 19.78 ?  371 ASN B N     1 
ATOM   8559  C  CA    . ASN B 1 371 ? 113.083 156.222 150.162 1.00 11.60 ?  371 ASN B CA    1 
ATOM   8560  C  C     . ASN B 1 371 ? 112.955 157.315 149.112 1.00 16.37 ?  371 ASN B C     1 
ATOM   8561  O  O     . ASN B 1 371 ? 112.610 157.016 147.965 1.00 26.99 ?  371 ASN B O     1 
ATOM   8562  C  CB    . ASN B 1 371 ? 111.700 155.859 150.702 1.00 9.05  ?  371 ASN B CB    1 
ATOM   8563  C  CG    . ASN B 1 371 ? 111.628 154.438 151.212 1.00 17.59 ?  371 ASN B CG    1 
ATOM   8564  O  OD1   . ASN B 1 371 ? 112.451 153.598 150.858 1.00 23.47 ?  371 ASN B OD1   1 
ATOM   8565  N  ND2   . ASN B 1 371 ? 110.641 154.163 152.054 1.00 24.49 ?  371 ASN B ND2   1 
ATOM   8566  N  N     . HIS B 1 372 ? 113.214 158.571 149.482 1.00 19.85 ?  372 HIS B N     1 
ATOM   8567  C  CA    . HIS B 1 372 ? 113.200 159.653 148.504 1.00 19.82 ?  372 HIS B CA    1 
ATOM   8568  C  C     . HIS B 1 372 ? 114.301 159.471 147.468 1.00 22.75 ?  372 HIS B C     1 
ATOM   8569  O  O     . HIS B 1 372 ? 114.091 159.723 146.276 1.00 28.09 ?  372 HIS B O     1 
ATOM   8570  C  CB    . HIS B 1 372 ? 113.343 161.000 149.211 1.00 23.38 ?  372 HIS B CB    1 
ATOM   8571  C  CG    . HIS B 1 372 ? 114.672 161.194 149.872 1.00 22.20 ?  372 HIS B CG    1 
ATOM   8572  N  ND1   . HIS B 1 372 ? 115.100 160.414 150.923 1.00 21.74 ?  372 HIS B ND1   1 
ATOM   8573  C  CD2   . HIS B 1 372 ? 115.671 162.073 149.625 1.00 24.73 ?  372 HIS B CD2   1 
ATOM   8574  C  CE1   . HIS B 1 372 ? 116.306 160.802 151.295 1.00 20.00 ?  372 HIS B CE1   1 
ATOM   8575  N  NE2   . HIS B 1 372 ? 116.673 161.811 150.526 1.00 23.90 ?  372 HIS B NE2   1 
ATOM   8576  N  N     . ILE B 1 373 ? 115.487 159.048 147.907 1.00 16.66 ?  373 ILE B N     1 
ATOM   8577  C  CA    . ILE B 1 373 ? 116.573 158.771 146.971 1.00 19.92 ?  373 ILE B CA    1 
ATOM   8578  C  C     . ILE B 1 373 ? 116.198 157.605 146.070 1.00 21.25 ?  373 ILE B C     1 
ATOM   8579  O  O     . ILE B 1 373 ? 116.288 157.689 144.840 1.00 37.31 ?  373 ILE B O     1 
ATOM   8580  C  CB    . ILE B 1 373 ? 117.880 158.492 147.735 1.00 24.82 ?  373 ILE B CB    1 
ATOM   8581  C  CG1   . ILE B 1 373 ? 118.315 159.729 148.518 1.00 21.51 ?  373 ILE B CG1   1 
ATOM   8582  C  CG2   . ILE B 1 373 ? 118.973 158.045 146.781 1.00 21.97 ?  373 ILE B CG2   1 
ATOM   8583  C  CD1   . ILE B 1 373 ? 119.332 159.438 149.589 1.00 18.19 ?  373 ILE B CD1   1 
ATOM   8584  N  N     . SER B 1 374 ? 115.754 156.507 146.674 1.00 15.22 ?  374 SER B N     1 
ATOM   8585  C  CA    . SER B 1 374 ? 115.321 155.303 145.983 1.00 10.77 ?  374 SER B CA    1 
ATOM   8586  C  C     . SER B 1 374 ? 114.838 154.319 147.035 1.00 20.36 ?  374 SER B C     1 
ATOM   8587  O  O     . SER B 1 374 ? 115.189 154.425 148.213 1.00 23.07 ?  374 SER B O     1 
ATOM   8588  C  CB    . SER B 1 374 ? 116.445 154.677 145.155 1.00 21.86 ?  374 SER B CB    1 
ATOM   8589  O  OG    . SER B 1 374 ? 115.952 153.649 144.320 1.00 35.99 ?  374 SER B OG    1 
ATOM   8590  N  N     . LYS B 1 375 ? 114.024 153.366 146.600 1.00 26.47 ?  375 LYS B N     1 
ATOM   8591  C  CA    . LYS B 1 375 ? 113.718 152.226 147.444 1.00 12.12 ?  375 LYS B CA    1 
ATOM   8592  C  C     . LYS B 1 375 ? 114.889 151.250 147.431 1.00 15.13 ?  375 LYS B C     1 
ATOM   8593  O  O     . LYS B 1 375 ? 115.694 151.218 146.497 1.00 28.03 ?  375 LYS B O     1 
ATOM   8594  C  CB    . LYS B 1 375 ? 112.444 151.528 146.969 1.00 14.41 ?  375 LYS B CB    1 
ATOM   8595  C  CG    . LYS B 1 375 ? 111.208 152.406 146.973 1.00 18.59 ?  375 LYS B CG    1 
ATOM   8596  C  CD    . LYS B 1 375 ? 110.625 152.529 148.364 1.00 21.94 ?  375 LYS B CD    1 
ATOM   8597  C  CE    . LYS B 1 375 ? 109.112 152.599 148.322 1.00 23.73 ?  375 LYS B CE    1 
ATOM   8598  N  NZ    . LYS B 1 375 ? 108.634 154.005 148.237 1.00 26.61 1  375 LYS B NZ    1 
ATOM   8599  N  N     . VAL B 1 376 ? 114.990 150.454 148.489 1.00 12.10 ?  376 VAL B N     1 
ATOM   8600  C  CA    . VAL B 1 376 ? 115.972 149.377 148.525 1.00 13.01 ?  376 VAL B CA    1 
ATOM   8601  C  C     . VAL B 1 376 ? 115.431 148.225 147.690 1.00 15.90 ?  376 VAL B C     1 
ATOM   8602  O  O     . VAL B 1 376 ? 114.384 147.653 148.006 1.00 25.73 ?  376 VAL B O     1 
ATOM   8603  C  CB    . VAL B 1 376 ? 116.265 148.933 149.965 1.00 9.66  ?  376 VAL B CB    1 
ATOM   8604  C  CG1   . VAL B 1 376 ? 117.306 147.824 149.978 1.00 5.98  ?  376 VAL B CG1   1 
ATOM   8605  C  CG2   . VAL B 1 376 ? 116.721 150.111 150.802 1.00 6.35  ?  376 VAL B CG2   1 
ATOM   8606  N  N     . LYS B 1 377 ? 116.141 147.887 146.615 1.00 14.65 ?  377 LYS B N     1 
ATOM   8607  C  CA    . LYS B 1 377 ? 115.671 146.877 145.680 1.00 13.59 ?  377 LYS B CA    1 
ATOM   8608  C  C     . LYS B 1 377 ? 116.359 145.533 145.841 1.00 8.55  ?  377 LYS B C     1 
ATOM   8609  O  O     . LYS B 1 377 ? 115.802 144.520 145.409 1.00 25.31 ?  377 LYS B O     1 
ATOM   8610  C  CB    . LYS B 1 377 ? 115.861 147.357 144.238 1.00 16.40 ?  377 LYS B CB    1 
ATOM   8611  C  CG    . LYS B 1 377 ? 115.100 148.619 143.899 1.00 9.68  ?  377 LYS B CG    1 
ATOM   8612  C  CD    . LYS B 1 377 ? 115.765 149.339 142.749 1.00 20.92 ?  377 LYS B CD    1 
ATOM   8613  C  CE    . LYS B 1 377 ? 115.697 150.838 142.928 1.00 25.14 ?  377 LYS B CE    1 
ATOM   8614  N  NZ    . LYS B 1 377 ? 116.663 151.546 142.045 1.00 23.03 1  377 LYS B NZ    1 
ATOM   8615  N  N     . PHE B 1 378 ? 117.543 145.498 146.442 1.00 6.05  ?  378 PHE B N     1 
ATOM   8616  C  CA    . PHE B 1 378 ? 118.292 144.258 146.583 1.00 5.14  ?  378 PHE B CA    1 
ATOM   8617  C  C     . PHE B 1 378 ? 119.345 144.449 147.664 1.00 10.46 ?  378 PHE B C     1 
ATOM   8618  O  O     . PHE B 1 378 ? 119.542 145.549 148.182 1.00 14.98 ?  378 PHE B O     1 
ATOM   8619  C  CB    . PHE B 1 378 ? 118.920 143.822 145.253 1.00 2.96  ?  378 PHE B CB    1 
ATOM   8620  C  CG    . PHE B 1 378 ? 120.059 144.691 144.791 1.00 7.80  ?  378 PHE B CG    1 
ATOM   8621  C  CD1   . PHE B 1 378 ? 119.887 146.051 144.598 1.00 14.95 ?  378 PHE B CD1   1 
ATOM   8622  C  CD2   . PHE B 1 378 ? 121.298 144.137 144.521 1.00 4.48  ?  378 PHE B CD2   1 
ATOM   8623  C  CE1   . PHE B 1 378 ? 120.928 146.840 144.164 1.00 6.75  ?  378 PHE B CE1   1 
ATOM   8624  C  CE2   . PHE B 1 378 ? 122.342 144.924 144.085 1.00 7.80  ?  378 PHE B CE2   1 
ATOM   8625  C  CZ    . PHE B 1 378 ? 122.156 146.276 143.906 1.00 9.48  ?  378 PHE B CZ    1 
ATOM   8626  N  N     . SER B 1 379 ? 120.017 143.355 147.997 1.00 2.51  ?  379 SER B N     1 
ATOM   8627  C  CA    . SER B 1 379 ? 121.007 143.320 149.061 1.00 7.97  ?  379 SER B CA    1 
ATOM   8628  C  C     . SER B 1 379 ? 122.351 142.879 148.495 1.00 8.40  ?  379 SER B C     1 
ATOM   8629  O  O     . SER B 1 379 ? 122.512 142.687 147.289 1.00 19.01 ?  379 SER B O     1 
ATOM   8630  C  CB    . SER B 1 379 ? 120.556 142.391 150.190 1.00 6.80  ?  379 SER B CB    1 
ATOM   8631  O  OG    . SER B 1 379 ? 121.048 142.835 151.438 1.00 10.43 ?  379 SER B OG    1 
ATOM   8632  N  N     . ASN B 1 380 ? 123.324 142.722 149.386 1.00 10.17 ?  380 ASN B N     1 
ATOM   8633  C  CA    . ASN B 1 380 ? 124.681 142.374 148.995 1.00 7.85  ?  380 ASN B CA    1 
ATOM   8634  C  C     . ASN B 1 380 ? 124.848 140.856 148.992 1.00 13.89 ?  380 ASN B C     1 
ATOM   8635  O  O     . ASN B 1 380 ? 123.880 140.096 149.080 1.00 20.08 ?  380 ASN B O     1 
ATOM   8636  C  CB    . ASN B 1 380 ? 125.691 143.056 149.916 1.00 8.11  ?  380 ASN B CB    1 
ATOM   8637  C  CG    . ASN B 1 380 ? 125.596 142.576 151.344 1.00 8.77  ?  380 ASN B CG    1 
ATOM   8638  O  OD1   . ASN B 1 380 ? 124.505 142.395 151.878 1.00 22.19 ?  380 ASN B OD1   1 
ATOM   8639  N  ND2   . ASN B 1 380 ? 126.743 142.384 151.979 1.00 17.17 ?  380 ASN B ND2   1 
ATOM   8640  N  N     . LEU B 1 381 ? 126.096 140.402 148.876 1.00 19.78 ?  381 LEU B N     1 
ATOM   8641  C  CA    . LEU B 1 381 ? 126.388 138.976 148.878 1.00 8.77  ?  381 LEU B CA    1 
ATOM   8642  C  C     . LEU B 1 381 ? 126.148 138.340 150.242 1.00 6.62  ?  381 LEU B C     1 
ATOM   8643  O  O     . LEU B 1 381 ? 125.939 137.125 150.317 1.00 22.70 ?  381 LEU B O     1 
ATOM   8644  C  CB    . LEU B 1 381 ? 127.834 138.757 148.425 1.00 17.60 ?  381 LEU B CB    1 
ATOM   8645  C  CG    . LEU B 1 381 ? 128.458 137.362 148.434 1.00 20.47 ?  381 LEU B CG    1 
ATOM   8646  C  CD1   . LEU B 1 381 ? 127.717 136.418 147.507 1.00 22.72 ?  381 LEU B CD1   1 
ATOM   8647  C  CD2   . LEU B 1 381 ? 129.919 137.450 148.051 1.00 15.48 ?  381 LEU B CD2   1 
ATOM   8648  N  N     . CYS B 1 382 ? 126.157 139.130 151.312 1.00 21.44 ?  382 CYS B N     1 
ATOM   8649  C  CA    . CYS B 1 382 ? 125.941 138.622 152.660 1.00 3.70  ?  382 CYS B CA    1 
ATOM   8650  C  C     . CYS B 1 382 ? 124.576 138.991 153.223 1.00 12.64 ?  382 CYS B C     1 
ATOM   8651  O  O     . CYS B 1 382 ? 124.290 138.657 154.376 1.00 23.34 ?  382 CYS B O     1 
ATOM   8652  C  CB    . CYS B 1 382 ? 127.047 139.124 153.594 1.00 20.70 ?  382 CYS B CB    1 
ATOM   8653  S  SG    . CYS B 1 382 ? 128.728 138.770 153.026 1.00 37.09 ?  382 CYS B SG    1 
ATOM   8654  N  N     . SER B 1 383 ? 123.738 139.686 152.449 1.00 15.80 ?  383 SER B N     1 
ATOM   8655  C  CA    . SER B 1 383 ? 122.326 139.905 152.763 1.00 11.02 ?  383 SER B CA    1 
ATOM   8656  C  C     . SER B 1 383 ? 122.115 140.818 153.969 1.00 18.31 ?  383 SER B C     1 
ATOM   8657  O  O     . SER B 1 383 ? 121.121 140.682 154.684 1.00 27.77 ?  383 SER B O     1 
ATOM   8658  C  CB    . SER B 1 383 ? 121.591 138.578 152.978 1.00 8.16  ?  383 SER B CB    1 
ATOM   8659  O  OG    . SER B 1 383 ? 121.630 137.784 151.809 1.00 36.35 ?  383 SER B OG    1 
ATOM   8660  N  N     . GLU B 1 384 ? 123.025 141.755 154.219 1.00 11.76 ?  384 GLU B N     1 
ATOM   8661  C  CA    . GLU B 1 384 ? 122.830 142.716 155.293 1.00 9.89  ?  384 GLU B CA    1 
ATOM   8662  C  C     . GLU B 1 384 ? 122.882 144.167 154.839 1.00 16.66 ?  384 GLU B C     1 
ATOM   8663  O  O     . GLU B 1 384 ? 122.434 145.043 155.584 1.00 26.21 ?  384 GLU B O     1 
ATOM   8664  C  CB    . GLU B 1 384 ? 123.864 142.498 156.411 1.00 9.21  ?  384 GLU B CB    1 
ATOM   8665  C  CG    . GLU B 1 384 ? 125.078 143.405 156.348 1.00 11.23 ?  384 GLU B CG    1 
ATOM   8666  C  CD    . GLU B 1 384 ? 126.130 142.900 155.393 1.00 22.17 ?  384 GLU B CD    1 
ATOM   8667  O  OE1   . GLU B 1 384 ? 126.014 141.743 154.950 1.00 23.44 ?  384 GLU B OE1   1 
ATOM   8668  O  OE2   . GLU B 1 384 ? 127.075 143.655 155.092 1.00 29.48 -1 384 GLU B OE2   1 
ATOM   8669  N  N     . VAL B 1 385 ? 123.399 144.446 153.650 1.00 11.10 ?  385 VAL B N     1 
ATOM   8670  C  CA    . VAL B 1 385 ? 123.478 145.809 153.142 1.00 2.81  ?  385 VAL B CA    1 
ATOM   8671  C  C     . VAL B 1 385 ? 122.176 146.129 152.424 1.00 17.93 ?  385 VAL B C     1 
ATOM   8672  O  O     . VAL B 1 385 ? 121.832 145.486 151.427 1.00 25.12 ?  385 VAL B O     1 
ATOM   8673  C  CB    . VAL B 1 385 ? 124.681 145.986 152.206 1.00 5.27  ?  385 VAL B CB    1 
ATOM   8674  C  CG1   . VAL B 1 385 ? 124.656 147.359 151.589 1.00 8.53  ?  385 VAL B CG1   1 
ATOM   8675  C  CG2   . VAL B 1 385 ? 125.968 145.777 152.968 1.00 8.98  ?  385 VAL B CG2   1 
ATOM   8676  N  N     . LEU B 1 386 ? 121.448 147.123 152.933 1.00 19.30 ?  386 LEU B N     1 
ATOM   8677  C  CA    . LEU B 1 386 ? 120.140 147.510 152.406 1.00 2.15  ?  386 LEU B CA    1 
ATOM   8678  C  C     . LEU B 1 386 ? 120.129 149.026 152.253 1.00 5.61  ?  386 LEU B C     1 
ATOM   8679  O  O     . LEU B 1 386 ? 119.779 149.751 153.187 1.00 12.33 ?  386 LEU B O     1 
ATOM   8680  C  CB    . LEU B 1 386 ? 119.025 147.020 153.318 1.00 5.81  ?  386 LEU B CB    1 
ATOM   8681  C  CG    . LEU B 1 386 ? 118.919 145.500 153.409 1.00 0.77  ?  386 LEU B CG    1 
ATOM   8682  C  CD1   . LEU B 1 386 ? 117.883 145.106 154.427 1.00 7.88  ?  386 LEU B CD1   1 
ATOM   8683  C  CD2   . LEU B 1 386 ? 118.587 144.913 152.050 1.00 6.73  ?  386 LEU B CD2   1 
ATOM   8684  N  N     . GLN B 1 387 ? 120.513 149.502 151.072 1.00 13.17 ?  387 GLN B N     1 
ATOM   8685  C  CA    . GLN B 1 387 ? 120.647 150.924 150.809 1.00 3.15  ?  387 GLN B CA    1 
ATOM   8686  C  C     . GLN B 1 387 ? 119.978 151.276 149.487 1.00 8.38  ?  387 GLN B C     1 
ATOM   8687  O  O     . GLN B 1 387 ? 119.764 150.421 148.627 1.00 22.69 ?  387 GLN B O     1 
ATOM   8688  C  CB    . GLN B 1 387 ? 122.121 151.348 150.781 1.00 0.56  ?  387 GLN B CB    1 
ATOM   8689  C  CG    . GLN B 1 387 ? 122.890 150.943 152.018 1.00 4.37  ?  387 GLN B CG    1 
ATOM   8690  C  CD    . GLN B 1 387 ? 124.311 151.441 152.006 1.00 10.53 ?  387 GLN B CD    1 
ATOM   8691  O  OE1   . GLN B 1 387 ? 124.671 152.308 151.213 1.00 20.68 ?  387 GLN B OE1   1 
ATOM   8692  N  NE2   . GLN B 1 387 ? 125.132 150.894 152.887 1.00 9.52  ?  387 GLN B NE2   1 
ATOM   8693  N  N     . ALA B 1 388 ? 119.642 152.553 149.346 1.00 9.62  ?  388 ALA B N     1 
ATOM   8694  C  CA    . ALA B 1 388 ? 119.065 153.047 148.104 1.00 7.64  ?  388 ALA B CA    1 
ATOM   8695  C  C     . ALA B 1 388 ? 120.102 153.033 146.990 1.00 14.26 ?  388 ALA B C     1 
ATOM   8696  O  O     . ALA B 1 388 ? 121.267 153.385 147.197 1.00 25.40 ?  388 ALA B O     1 
ATOM   8697  C  CB    . ALA B 1 388 ? 118.522 154.461 148.296 1.00 11.59 ?  388 ALA B CB    1 
ATOM   8698  N  N     . SER B 1 389 ? 119.673 152.629 145.800 1.00 19.81 ?  389 SER B N     1 
ATOM   8699  C  CA    . SER B 1 389 ? 120.538 152.581 144.634 1.00 8.84  ?  389 SER B CA    1 
ATOM   8700  C  C     . SER B 1 389 ? 119.834 153.221 143.448 1.00 12.83 ?  389 SER B C     1 
ATOM   8701  O  O     . SER B 1 389 ? 118.604 153.210 143.353 1.00 23.31 ?  389 SER B O     1 
ATOM   8702  C  CB    . SER B 1 389 ? 120.935 151.143 144.283 1.00 17.11 ?  389 SER B CB    1 
ATOM   8703  O  OG    . SER B 1 389 ? 119.802 150.294 144.249 1.00 23.86 ?  389 SER B OG    1 
ATOM   8704  N  N     . GLN B 1 390 ? 120.629 153.780 142.543 1.00 22.95 ?  390 GLN B N     1 
ATOM   8705  C  CA    . GLN B 1 390 ? 120.130 154.337 141.295 1.00 12.92 ?  390 GLN B CA    1 
ATOM   8706  C  C     . GLN B 1 390 ? 120.893 153.694 140.152 1.00 14.09 ?  390 GLN B C     1 
ATOM   8707  O  O     . GLN B 1 390 ? 122.126 153.637 140.180 1.00 25.00 ?  390 GLN B O     1 
ATOM   8708  C  CB    . GLN B 1 390 ? 120.285 155.859 141.263 1.00 10.67 ?  390 GLN B CB    1 
ATOM   8709  C  CG    . GLN B 1 390 ? 119.335 156.583 142.194 1.00 11.92 ?  390 GLN B CG    1 
ATOM   8710  C  CD    . GLN B 1 390 ? 119.555 158.078 142.207 1.00 26.59 ?  390 GLN B CD    1 
ATOM   8711  O  OE1   . GLN B 1 390 ? 120.508 158.582 141.613 1.00 33.24 ?  390 GLN B OE1   1 
ATOM   8712  N  NE2   . GLN B 1 390 ? 118.675 158.798 142.890 1.00 18.02 ?  390 GLN B NE2   1 
ATOM   8713  N  N     . VAL B 1 391 ? 120.163 153.203 139.153 1.00 26.31 ?  391 VAL B N     1 
ATOM   8714  C  CA    . VAL B 1 391 ? 120.799 152.504 138.046 1.00 20.02 ?  391 VAL B CA    1 
ATOM   8715  C  C     . VAL B 1 391 ? 121.525 153.505 137.157 1.00 25.64 ?  391 VAL B C     1 
ATOM   8716  O  O     . VAL B 1 391 ? 121.069 154.638 136.953 1.00 22.59 ?  391 VAL B O     1 
ATOM   8717  C  CB    . VAL B 1 391 ? 119.761 151.684 137.258 1.00 15.69 ?  391 VAL B CB    1 
ATOM   8718  C  CG1   . VAL B 1 391 ? 118.825 152.590 136.472 1.00 16.52 ?  391 VAL B CG1   1 
ATOM   8719  C  CG2   . VAL B 1 391 ? 120.455 150.686 136.345 1.00 17.13 ?  391 VAL B CG2   1 
ATOM   8720  N  N     . SER B 1 392 ? 122.682 153.098 136.651 1.00 32.86 ?  392 SER B N     1 
ATOM   8721  C  CA    . SER B 1 392 ? 123.462 153.927 135.749 1.00 21.49 ?  392 SER B CA    1 
ATOM   8722  C  C     . SER B 1 392 ? 123.084 153.635 134.305 1.00 28.88 ?  392 SER B C     1 
ATOM   8723  O  O     . SER B 1 392 ? 122.749 152.504 133.945 1.00 31.81 ?  392 SER B O     1 
ATOM   8724  C  CB    . SER B 1 392 ? 124.959 153.693 135.951 1.00 25.83 ?  392 SER B CB    1 
ATOM   8725  O  OG    . SER B 1 392 ? 125.330 153.888 137.302 1.00 36.93 ?  392 SER B OG    1 
ATOM   8726  N  N     . SER B 1 393 ? 123.138 154.671 133.480 1.00 35.47 ?  393 SER B N     1 
ATOM   8727  C  CA    . SER B 1 393 ? 122.857 154.565 132.052 1.00 28.19 ?  393 SER B CA    1 
ATOM   8728  C  C     . SER B 1 393 ? 124.192 154.660 131.320 1.00 32.27 ?  393 SER B C     1 
ATOM   8729  O  O     . SER B 1 393 ? 124.637 155.747 130.947 1.00 35.82 ?  393 SER B O     1 
ATOM   8730  C  CB    . SER B 1 393 ? 121.886 155.646 131.600 1.00 31.94 ?  393 SER B CB    1 
ATOM   8731  O  OG    . SER B 1 393 ? 120.798 155.758 132.500 1.00 43.25 ?  393 SER B OG    1 
ATOM   8732  N  N     . TYR B 1 394 ? 124.831 153.511 131.122 1.00 32.45 ?  394 TYR B N     1 
ATOM   8733  C  CA    . TYR B 1 394 ? 126.086 153.452 130.382 1.00 29.04 ?  394 TYR B CA    1 
ATOM   8734  C  C     . TYR B 1 394 ? 125.765 153.448 128.894 1.00 30.77 ?  394 TYR B C     1 
ATOM   8735  O  O     . TYR B 1 394 ? 125.201 152.481 128.374 1.00 34.55 ?  394 TYR B O     1 
ATOM   8736  C  CB    . TYR B 1 394 ? 126.889 152.221 130.785 1.00 28.80 ?  394 TYR B CB    1 
ATOM   8737  C  CG    . TYR B 1 394 ? 127.302 152.217 132.238 1.00 28.49 ?  394 TYR B CG    1 
ATOM   8738  C  CD1   . TYR B 1 394 ? 128.297 153.069 132.700 1.00 29.28 ?  394 TYR B CD1   1 
ATOM   8739  C  CD2   . TYR B 1 394 ? 126.694 151.366 133.149 1.00 25.63 ?  394 TYR B CD2   1 
ATOM   8740  C  CE1   . TYR B 1 394 ? 128.675 153.069 134.027 1.00 29.53 ?  394 TYR B CE1   1 
ATOM   8741  C  CE2   . TYR B 1 394 ? 127.065 151.358 134.475 1.00 26.56 ?  394 TYR B CE2   1 
ATOM   8742  C  CZ    . TYR B 1 394 ? 128.055 152.211 134.910 1.00 36.49 ?  394 TYR B CZ    1 
ATOM   8743  O  OH    . TYR B 1 394 ? 128.425 152.204 136.236 1.00 40.21 ?  394 TYR B OH    1 
ATOM   8744  N  N     . THR B 1 395 ? 126.118 154.530 128.214 1.00 38.04 ?  395 THR B N     1 
ATOM   8745  C  CA    . THR B 1 395 ? 125.772 154.730 126.818 1.00 33.83 ?  395 THR B CA    1 
ATOM   8746  C  C     . THR B 1 395 ? 126.884 154.183 125.925 1.00 37.74 ?  395 THR B C     1 
ATOM   8747  O  O     . THR B 1 395 ? 127.776 153.459 126.375 1.00 34.98 ?  395 THR B O     1 
ATOM   8748  C  CB    . THR B 1 395 ? 125.508 156.209 126.559 1.00 36.13 ?  395 THR B CB    1 
ATOM   8749  O  OG1   . THR B 1 395 ? 126.698 156.959 126.828 1.00 37.24 ?  395 THR B OG1   1 
ATOM   8750  C  CG2   . THR B 1 395 ? 124.392 156.712 127.459 1.00 35.65 ?  395 THR B CG2   1 
ATOM   8751  N  N     . ASP B 1 396 ? 126.836 154.524 124.640 1.00 40.82 ?  396 ASP B N     1 
ATOM   8752  C  CA    . ASP B 1 396 ? 127.873 154.103 123.713 1.00 34.89 ?  396 ASP B CA    1 
ATOM   8753  C  C     . ASP B 1 396 ? 129.210 154.741 124.086 1.00 39.22 ?  396 ASP B C     1 
ATOM   8754  O  O     . ASP B 1 396 ? 129.295 155.630 124.936 1.00 46.61 ?  396 ASP B O     1 
ATOM   8755  C  CB    . ASP B 1 396 ? 127.488 154.463 122.278 1.00 39.86 ?  396 ASP B CB    1 
ATOM   8756  C  CG    . ASP B 1 396 ? 126.259 153.717 121.800 1.00 45.72 ?  396 ASP B CG    1 
ATOM   8757  O  OD1   . ASP B 1 396 ? 126.187 152.489 122.014 1.00 42.96 ?  396 ASP B OD1   1 
ATOM   8758  O  OD2   . ASP B 1 396 ? 125.368 154.356 121.205 1.00 46.25 -1 396 ASP B OD2   1 
ATOM   8759  N  N     . TYR B 1 397 ? 130.269 154.267 123.427 1.00 32.24 ?  397 TYR B N     1 
ATOM   8760  C  CA    . TYR B 1 397 ? 131.618 154.698 123.782 1.00 34.09 ?  397 TYR B CA    1 
ATOM   8761  C  C     . TYR B 1 397 ? 131.798 156.198 123.576 1.00 34.30 ?  397 TYR B C     1 
ATOM   8762  O  O     . TYR B 1 397 ? 132.430 156.872 124.398 1.00 41.35 ?  397 TYR B O     1 
ATOM   8763  C  CB    . TYR B 1 397 ? 132.647 153.911 122.970 1.00 32.22 ?  397 TYR B CB    1 
ATOM   8764  C  CG    . TYR B 1 397 ? 134.078 154.340 123.195 1.00 31.70 ?  397 TYR B CG    1 
ATOM   8765  C  CD1   . TYR B 1 397 ? 134.647 155.360 122.442 1.00 32.38 ?  397 TYR B CD1   1 
ATOM   8766  C  CD2   . TYR B 1 397 ? 134.864 153.723 124.159 1.00 28.43 ?  397 TYR B CD2   1 
ATOM   8767  C  CE1   . TYR B 1 397 ? 135.949 155.754 122.645 1.00 33.34 ?  397 TYR B CE1   1 
ATOM   8768  C  CE2   . TYR B 1 397 ? 136.169 154.111 124.368 1.00 30.86 ?  397 TYR B CE2   1 
ATOM   8769  C  CZ    . TYR B 1 397 ? 136.707 155.127 123.608 1.00 36.04 ?  397 TYR B CZ    1 
ATOM   8770  O  OH    . TYR B 1 397 ? 138.008 155.519 123.811 1.00 39.42 ?  397 TYR B OH    1 
ATOM   8771  N  N     . ASP B 1 398 ? 131.258 156.736 122.484 1.00 43.33 ?  398 ASP B N     1 
ATOM   8772  C  CA    . ASP B 1 398 ? 131.447 158.153 122.189 1.00 43.51 ?  398 ASP B CA    1 
ATOM   8773  C  C     . ASP B 1 398 ? 130.602 159.044 123.091 1.00 47.22 ?  398 ASP B C     1 
ATOM   8774  O  O     . ASP B 1 398 ? 130.970 160.196 123.340 1.00 49.56 ?  398 ASP B O     1 
ATOM   8775  C  CB    . ASP B 1 398 ? 131.124 158.430 120.721 1.00 45.31 ?  398 ASP B CB    1 
ATOM   8776  C  CG    . ASP B 1 398 ? 129.878 157.703 120.252 1.00 49.08 ?  398 ASP B CG    1 
ATOM   8777  O  OD1   . ASP B 1 398 ? 129.812 156.468 120.420 1.00 47.02 ?  398 ASP B OD1   1 
ATOM   8778  O  OD2   . ASP B 1 398 ? 128.968 158.365 119.713 1.00 51.13 -1 398 ASP B OD2   1 
ATOM   8779  N  N     . GLU B 1 399 ? 129.479 158.535 123.586 1.00 46.85 ?  399 GLU B N     1 
ATOM   8780  C  CA    . GLU B 1 399 ? 128.547 159.331 124.367 1.00 42.12 ?  399 GLU B CA    1 
ATOM   8781  C  C     . GLU B 1 399 ? 128.971 159.394 125.833 1.00 48.56 ?  399 GLU B C     1 
ATOM   8782  O  O     . GLU B 1 399 ? 129.875 158.687 126.282 1.00 48.89 ?  399 GLU B O     1 
ATOM   8783  C  CB    . GLU B 1 399 ? 127.134 158.762 124.248 1.00 44.22 ?  399 GLU B CB    1 
ATOM   8784  C  CG    . GLU B 1 399 ? 126.484 159.002 122.900 1.00 48.53 ?  399 GLU B CG    1 
ATOM   8785  C  CD    . GLU B 1 399 ? 125.441 157.959 122.567 1.00 52.02 ?  399 GLU B CD    1 
ATOM   8786  O  OE1   . GLU B 1 399 ? 124.835 157.403 123.506 1.00 50.37 ?  399 GLU B OE1   1 
ATOM   8787  O  OE2   . GLU B 1 399 ? 125.225 157.696 121.365 1.00 53.71 -1 399 GLU B OE2   1 
ATOM   8788  N  N     . GLU B 1 400 ? 128.299 160.265 126.580 1.00 47.89 ?  400 GLU B N     1 
ATOM   8789  C  CA    . GLU B 1 400 ? 128.557 160.442 128.003 1.00 41.02 ?  400 GLU B CA    1 
ATOM   8790  C  C     . GLU B 1 400 ? 127.609 159.567 128.813 1.00 44.36 ?  400 GLU B C     1 
ATOM   8791  O  O     . GLU B 1 400 ? 126.396 159.576 128.583 1.00 43.18 ?  400 GLU B O     1 
ATOM   8792  C  CB    . GLU B 1 400 ? 128.391 161.907 128.404 1.00 41.65 ?  400 GLU B CB    1 
ATOM   8793  C  CG    . GLU B 1 400 ? 129.616 162.771 128.156 1.00 47.55 ?  400 GLU B CG    1 
ATOM   8794  C  CD    . GLU B 1 400 ? 130.833 162.297 128.927 1.00 52.56 ?  400 GLU B CD    1 
ATOM   8795  O  OE1   . GLU B 1 400 ? 130.673 161.861 130.086 1.00 52.78 ?  400 GLU B OE1   1 
ATOM   8796  O  OE2   . GLU B 1 400 ? 131.951 162.365 128.375 1.00 49.93 -1 400 GLU B OE2   1 
ATOM   8797  N  N     . ASP B 1 401 ? 128.166 158.817 129.758 1.00 42.88 ?  401 ASP B N     1 
ATOM   8798  C  CA    . ASP B 1 401 ? 127.365 157.938 130.595 1.00 37.73 ?  401 ASP B CA    1 
ATOM   8799  C  C     . ASP B 1 401 ? 126.629 158.730 131.669 1.00 39.48 ?  401 ASP B C     1 
ATOM   8800  O  O     . ASP B 1 401 ? 127.089 159.779 132.124 1.00 43.20 ?  401 ASP B O     1 
ATOM   8801  C  CB    . ASP B 1 401 ? 128.243 156.876 131.257 1.00 37.41 ?  401 ASP B CB    1 
ATOM   8802  C  CG    . ASP B 1 401 ? 128.916 155.967 130.254 1.00 40.11 ?  401 ASP B CG    1 
ATOM   8803  O  OD1   . ASP B 1 401 ? 128.294 155.657 129.217 1.00 44.10 ?  401 ASP B OD1   1 
ATOM   8804  O  OD2   . ASP B 1 401 ? 130.069 155.562 130.503 1.00 40.53 -1 401 ASP B OD2   1 
ATOM   8805  N  N     . GLU B 1 402 ? 125.473 158.210 132.070 1.00 38.02 ?  402 GLU B N     1 
ATOM   8806  C  CA    . GLU B 1 402 ? 124.687 158.773 133.163 1.00 32.62 ?  402 GLU B CA    1 
ATOM   8807  C  C     . GLU B 1 402 ? 124.955 157.924 134.401 1.00 34.97 ?  402 GLU B C     1 
ATOM   8808  O  O     . GLU B 1 402 ? 124.373 156.851 134.570 1.00 39.72 ?  402 GLU B O     1 
ATOM   8809  C  CB    . GLU B 1 402 ? 123.203 158.805 132.814 1.00 37.87 ?  402 GLU B CB    1 
ATOM   8810  C  CG    . GLU B 1 402 ? 122.563 160.199 132.683 1.00 41.50 ?  402 GLU B CG    1 
ATOM   8811  C  CD    . GLU B 1 402 ? 122.663 161.095 133.922 1.00 48.02 ?  402 GLU B CD    1 
ATOM   8812  O  OE1   . GLU B 1 402 ? 121.902 162.084 133.977 1.00 46.69 ?  402 GLU B OE1   1 
ATOM   8813  O  OE2   . GLU B 1 402 ? 123.460 160.829 134.847 1.00 49.75 -1 402 GLU B OE2   1 
ATOM   8814  N  N     . ILE B 1 403 ? 125.834 158.413 135.266 1.00 32.50 ?  403 ILE B N     1 
ATOM   8815  C  CA    . ILE B 1 403 ? 126.284 157.643 136.420 1.00 28.63 ?  403 ILE B CA    1 
ATOM   8816  C  C     . ILE B 1 403 ? 125.250 157.745 137.532 1.00 31.15 ?  403 ILE B C     1 
ATOM   8817  O  O     . ILE B 1 403 ? 124.825 158.844 137.906 1.00 32.16 ?  403 ILE B O     1 
ATOM   8818  C  CB    . ILE B 1 403 ? 127.659 158.136 136.891 1.00 23.85 ?  403 ILE B CB    1 
ATOM   8819  C  CG1   . ILE B 1 403 ? 128.716 157.870 135.816 1.00 26.86 ?  403 ILE B CG1   1 
ATOM   8820  C  CG2   . ILE B 1 403 ? 128.036 157.476 138.198 1.00 23.30 ?  403 ILE B CG2   1 
ATOM   8821  C  CD1   . ILE B 1 403 ? 128.742 156.446 135.324 1.00 31.86 ?  403 ILE B CD1   1 
ATOM   8822  N  N     . GLY B 1 404 ? 124.843 156.599 138.060 1.00 26.12 ?  404 GLY B N     1 
ATOM   8823  C  CA    . GLY B 1 404 ? 123.921 156.507 139.173 1.00 14.51 ?  404 GLY B CA    1 
ATOM   8824  C  C     . GLY B 1 404 ? 124.631 156.278 140.490 1.00 21.90 ?  404 GLY B C     1 
ATOM   8825  O  O     . GLY B 1 404 ? 125.768 156.717 140.696 1.00 34.25 ?  404 GLY B O     1 
ATOM   8826  N  N     . LEU B 1 405 ? 123.953 155.582 141.397 1.00 25.58 ?  405 LEU B N     1 
ATOM   8827  C  CA    . LEU B 1 405 ? 124.491 155.269 142.716 1.00 9.14  ?  405 LEU B CA    1 
ATOM   8828  C  C     . LEU B 1 405 ? 124.521 153.760 142.895 1.00 12.56 ?  405 LEU B C     1 
ATOM   8829  O  O     . LEU B 1 405 ? 123.473 153.108 142.866 1.00 20.84 ?  405 LEU B O     1 
ATOM   8830  C  CB    . LEU B 1 405 ? 123.656 155.920 143.820 1.00 19.52 ?  405 LEU B CB    1 
ATOM   8831  C  CG    . LEU B 1 405 ? 123.525 157.442 143.786 1.00 17.62 ?  405 LEU B CG    1 
ATOM   8832  C  CD1   . LEU B 1 405 ? 122.558 157.913 144.855 1.00 25.45 ?  405 LEU B CD1   1 
ATOM   8833  C  CD2   . LEU B 1 405 ? 124.879 158.102 143.959 1.00 19.08 ?  405 LEU B CD2   1 
ATOM   8834  N  N     . ASP B 1 406 ? 125.717 153.211 143.090 1.00 24.10 ?  406 ASP B N     1 
ATOM   8835  C  CA    . ASP B 1 406 ? 125.899 151.799 143.391 1.00 12.26 ?  406 ASP B CA    1 
ATOM   8836  C  C     . ASP B 1 406 ? 126.422 151.652 144.813 1.00 23.28 ?  406 ASP B C     1 
ATOM   8837  O  O     . ASP B 1 406 ? 127.349 152.356 145.220 1.00 34.31 ?  406 ASP B O     1 
ATOM   8838  C  CB    . ASP B 1 406 ? 126.860 151.138 142.404 1.00 18.39 ?  406 ASP B CB    1 
ATOM   8839  C  CG    . ASP B 1 406 ? 126.211 150.835 141.069 1.00 35.02 ?  406 ASP B CG    1 
ATOM   8840  O  OD1   . ASP B 1 406 ? 124.985 151.028 140.938 1.00 37.66 ?  406 ASP B OD1   1 
ATOM   8841  O  OD2   . ASP B 1 406 ? 126.932 150.402 140.146 1.00 32.49 -1 406 ASP B OD2   1 
ATOM   8842  N  N     . ILE B 1 407 ? 125.839 150.723 145.554 1.00 30.17 ?  407 ILE B N     1 
ATOM   8843  C  CA    . ILE B 1 407 ? 126.042 150.652 146.995 1.00 17.45 ?  407 ILE B CA    1 
ATOM   8844  C  C     . ILE B 1 407 ? 127.389 150.019 147.314 1.00 16.83 ?  407 ILE B C     1 
ATOM   8845  O  O     . ILE B 1 407 ? 127.804 149.037 146.686 1.00 24.89 ?  407 ILE B O     1 
ATOM   8846  C  CB    . ILE B 1 407 ? 124.892 149.872 147.654 1.00 10.96 ?  407 ILE B CB    1 
ATOM   8847  C  CG1   . ILE B 1 407 ? 123.548 150.509 147.312 1.00 4.34  ?  407 ILE B CG1   1 
ATOM   8848  C  CG2   . ILE B 1 407 ? 125.077 149.820 149.143 1.00 16.64 ?  407 ILE B CG2   1 
ATOM   8849  C  CD1   . ILE B 1 407 ? 122.467 149.502 147.051 1.00 18.14 ?  407 ILE B CD1   1 
ATOM   8850  N  N     . SER B 1 408 ? 128.077 150.592 148.298 1.00 28.19 ?  408 SER B N     1 
ATOM   8851  C  CA    . SER B 1 408 ? 129.297 150.010 148.853 1.00 25.83 ?  408 SER B CA    1 
ATOM   8852  C  C     . SER B 1 408 ? 129.521 150.635 150.219 1.00 27.97 ?  408 SER B C     1 
ATOM   8853  O  O     . SER B 1 408 ? 129.787 151.838 150.307 1.00 38.52 ?  408 SER B O     1 
ATOM   8854  C  CB    . SER B 1 408 ? 130.493 150.259 147.938 1.00 30.99 ?  408 SER B CB    1 
ATOM   8855  O  OG    . SER B 1 408 ? 131.186 151.437 148.314 1.00 34.38 ?  408 SER B OG    1 
ATOM   8856  N  N     . CYS B 1 409 ? 129.417 149.837 151.276 1.00 21.98 ?  409 CYS B N     1 
ATOM   8857  C  CA    . CYS B 1 409 ? 129.553 150.347 152.632 1.00 31.49 ?  409 CYS B CA    1 
ATOM   8858  C  C     . CYS B 1 409 ? 130.716 149.666 153.341 1.00 26.72 ?  409 CYS B C     1 
ATOM   8859  O  O     . CYS B 1 409 ? 131.115 148.548 153.005 1.00 25.56 ?  409 CYS B O     1 
ATOM   8860  C  CB    . CYS B 1 409 ? 128.254 150.167 153.433 1.00 27.84 ?  409 CYS B CB    1 
ATOM   8861  S  SG    . CYS B 1 409 ? 128.119 148.644 154.385 1.00 38.82 ?  409 CYS B SG    1 
ATOM   8862  N  N     . ASN B 1 410 ? 131.260 150.369 154.329 1.00 22.62 ?  410 ASN B N     1 
ATOM   8863  C  CA    . ASN B 1 410 ? 132.438 149.931 155.063 1.00 22.90 ?  410 ASN B CA    1 
ATOM   8864  C  C     . ASN B 1 410 ? 131.999 149.249 156.350 1.00 24.05 ?  410 ASN B C     1 
ATOM   8865  O  O     . ASN B 1 410 ? 131.120 149.753 157.054 1.00 31.21 ?  410 ASN B O     1 
ATOM   8866  C  CB    . ASN B 1 410 ? 133.345 151.123 155.365 1.00 28.30 ?  410 ASN B CB    1 
ATOM   8867  C  CG    . ASN B 1 410 ? 133.299 152.172 154.274 1.00 37.57 ?  410 ASN B CG    1 
ATOM   8868  O  OD1   . ASN B 1 410 ? 134.262 152.346 153.529 1.00 42.49 ?  410 ASN B OD1   1 
ATOM   8869  N  ND2   . ASN B 1 410 ? 132.189 152.892 154.189 1.00 31.73 ?  410 ASN B ND2   1 
ATOM   8870  N  N     . LEU B 1 411 ? 132.615 148.112 156.654 1.00 16.74 ?  411 LEU B N     1 
ATOM   8871  C  CA    . LEU B 1 411 ? 132.154 147.236 157.720 1.00 9.81  ?  411 LEU B CA    1 
ATOM   8872  C  C     . LEU B 1 411 ? 133.026 147.360 158.961 1.00 13.17 ?  411 LEU B C     1 
ATOM   8873  O  O     . LEU B 1 411 ? 134.249 147.495 158.869 1.00 24.64 ?  411 LEU B O     1 
ATOM   8874  C  CB    . LEU B 1 411 ? 132.139 145.781 157.250 1.00 20.83 ?  411 LEU B CB    1 
ATOM   8875  C  CG    . LEU B 1 411 ? 131.300 145.439 156.023 1.00 19.90 ?  411 LEU B CG    1 
ATOM   8876  C  CD1   . LEU B 1 411 ? 131.016 143.957 155.994 1.00 25.47 ?  411 LEU B CD1   1 
ATOM   8877  C  CD2   . LEU B 1 411 ? 130.004 146.211 156.053 1.00 18.66 ?  411 LEU B CD2   1 
ATOM   8878  N  N     . GLY B 1 412 ? 132.378 147.323 160.120 1.00 18.40 ?  412 GLY B N     1 
ATOM   8879  C  CA    . GLY B 1 412 ? 133.066 147.222 161.392 1.00 4.64  ?  412 GLY B CA    1 
ATOM   8880  C  C     . GLY B 1 412 ? 132.138 146.567 162.389 1.00 11.43 ?  412 GLY B C     1 
ATOM   8881  O  O     . GLY B 1 412 ? 130.912 146.638 162.261 1.00 29.68 ?  412 GLY B O     1 
ATOM   8882  N  N     . SER B 1 413 ? 132.731 145.921 163.388 1.00 13.53 ?  413 SER B N     1 
ATOM   8883  C  CA    . SER B 1 413 ? 131.959 145.153 164.356 1.00 14.25 ?  413 SER B CA    1 
ATOM   8884  C  C     . SER B 1 413 ? 132.346 145.531 165.775 1.00 15.86 ?  413 SER B C     1 
ATOM   8885  O  O     . SER B 1 413 ? 133.527 145.498 166.132 1.00 23.31 ?  413 SER B O     1 
ATOM   8886  C  CB    . SER B 1 413 ? 132.156 143.650 164.152 1.00 10.59 ?  413 SER B CB    1 
ATOM   8887  O  OG    . SER B 1 413 ? 131.451 143.207 163.011 1.00 30.53 ?  413 SER B OG    1 
ATOM   8888  N  N     . LEU B 1 414 ? 131.348 145.887 166.576 1.00 17.46 ?  414 LEU B N     1 
ATOM   8889  C  CA    . LEU B 1 414 ? 131.545 145.989 168.013 1.00 9.58  ?  414 LEU B CA    1 
ATOM   8890  C  C     . LEU B 1 414 ? 131.564 144.599 168.628 1.00 20.99 ?  414 LEU B C     1 
ATOM   8891  O  O     . LEU B 1 414 ? 130.775 143.728 168.255 1.00 27.41 ?  414 LEU B O     1 
ATOM   8892  C  CB    . LEU B 1 414 ? 130.432 146.814 168.653 1.00 19.06 ?  414 LEU B CB    1 
ATOM   8893  C  CG    . LEU B 1 414 ? 130.037 148.139 168.007 1.00 20.59 ?  414 LEU B CG    1 
ATOM   8894  C  CD1   . LEU B 1 414 ? 128.785 148.672 168.669 1.00 23.38 ?  414 LEU B CD1   1 
ATOM   8895  C  CD2   . LEU B 1 414 ? 131.166 149.142 168.116 1.00 25.08 ?  414 LEU B CD2   1 
ATOM   8896  N  N     . ASN B 1 415 ? 132.473 144.389 169.569 1.00 30.18 ?  415 ASN B N     1 
ATOM   8897  C  CA    . ASN B 1 415 ? 132.462 143.186 170.391 1.00 26.52 ?  415 ASN B CA    1 
ATOM   8898  C  C     . ASN B 1 415 ? 131.536 143.452 171.571 1.00 24.97 ?  415 ASN B C     1 
ATOM   8899  O  O     . ASN B 1 415 ? 131.878 144.221 172.473 1.00 29.48 ?  415 ASN B O     1 
ATOM   8900  C  CB    . ASN B 1 415 ? 133.871 142.831 170.850 1.00 21.57 ?  415 ASN B CB    1 
ATOM   8901  C  CG    . ASN B 1 415 ? 133.983 141.409 171.352 1.00 21.47 ?  415 ASN B CG    1 
ATOM   8902  O  OD1   . ASN B 1 415 ? 133.207 140.974 172.201 1.00 37.85 ?  415 ASN B OD1   1 
ATOM   8903  N  ND2   . ASN B 1 415 ? 134.955 140.674 170.829 1.00 29.64 ?  415 ASN B ND2   1 
ATOM   8904  N  N     . ILE B 1 416 ? 130.359 142.825 171.554 1.00 17.78 ?  416 ILE B N     1 
ATOM   8905  C  CA    . ILE B 1 416 ? 129.338 143.119 172.556 1.00 21.17 ?  416 ILE B CA    1 
ATOM   8906  C  C     . ILE B 1 416 ? 129.839 142.771 173.952 1.00 28.90 ?  416 ILE B C     1 
ATOM   8907  O  O     . ILE B 1 416 ? 129.585 143.502 174.916 1.00 27.87 ?  416 ILE B O     1 
ATOM   8908  C  CB    . ILE B 1 416 ? 128.028 142.384 172.214 1.00 27.96 ?  416 ILE B CB    1 
ATOM   8909  C  CG1   . ILE B 1 416 ? 127.401 142.985 170.956 1.00 20.31 ?  416 ILE B CG1   1 
ATOM   8910  C  CG2   . ILE B 1 416 ? 127.047 142.453 173.367 1.00 9.74  ?  416 ILE B CG2   1 
ATOM   8911  C  CD1   . ILE B 1 416 ? 126.196 142.233 170.450 1.00 15.27 ?  416 ILE B CD1   1 
ATOM   8912  N  N     . LEU B 1 417 ? 130.571 141.664 174.082 1.00 21.36 ?  417 LEU B N     1 
ATOM   8913  C  CA    . LEU B 1 417 ? 131.093 141.273 175.388 1.00 26.32 ?  417 LEU B CA    1 
ATOM   8914  C  C     . LEU B 1 417 ? 132.092 142.297 175.916 1.00 30.42 ?  417 LEU B C     1 
ATOM   8915  O  O     . LEU B 1 417 ? 132.003 142.728 177.072 1.00 38.35 ?  417 LEU B O     1 
ATOM   8916  C  CB    . LEU B 1 417 ? 131.738 139.890 175.300 1.00 29.69 ?  417 LEU B CB    1 
ATOM   8917  C  CG    . LEU B 1 417 ? 132.531 139.417 176.518 1.00 30.91 ?  417 LEU B CG    1 
ATOM   8918  C  CD1   . LEU B 1 417 ? 131.612 138.804 177.556 1.00 28.98 ?  417 LEU B CD1   1 
ATOM   8919  C  CD2   . LEU B 1 417 ? 133.606 138.430 176.104 1.00 35.30 ?  417 LEU B CD2   1 
ATOM   8920  N  N     . ASN B 1 418 ? 133.046 142.708 175.080 1.00 30.35 ?  418 ASN B N     1 
ATOM   8921  C  CA    . ASN B 1 418 ? 134.075 143.641 175.521 1.00 27.79 ?  418 ASN B CA    1 
ATOM   8922  C  C     . ASN B 1 418 ? 133.540 145.058 175.675 1.00 29.87 ?  418 ASN B C     1 
ATOM   8923  O  O     . ASN B 1 418 ? 133.975 145.784 176.575 1.00 34.48 ?  418 ASN B O     1 
ATOM   8924  C  CB    . ASN B 1 418 ? 135.250 143.624 174.545 1.00 25.73 ?  418 ASN B CB    1 
ATOM   8925  C  CG    . ASN B 1 418 ? 136.045 142.340 174.622 1.00 26.42 ?  418 ASN B CG    1 
ATOM   8926  O  OD1   . ASN B 1 418 ? 136.197 141.756 175.692 1.00 34.90 ?  418 ASN B OD1   1 
ATOM   8927  N  ND2   . ASN B 1 418 ? 136.553 141.889 173.484 1.00 30.58 ?  418 ASN B ND2   1 
ATOM   8928  N  N     . VAL B 1 419 ? 132.613 145.469 174.809 1.00 32.67 ?  419 VAL B N     1 
ATOM   8929  C  CA    . VAL B 1 419 ? 131.984 146.776 174.959 1.00 31.64 ?  419 VAL B CA    1 
ATOM   8930  C  C     . VAL B 1 419 ? 131.140 146.815 176.225 1.00 30.72 ?  419 VAL B C     1 
ATOM   8931  O  O     . VAL B 1 419 ? 131.098 147.828 176.933 1.00 33.42 ?  419 VAL B O     1 
ATOM   8932  C  CB    . VAL B 1 419 ? 131.153 147.104 173.704 1.00 28.04 ?  419 VAL B CB    1 
ATOM   8933  C  CG1   . VAL B 1 419 ? 130.168 148.216 173.983 1.00 33.19 ?  419 VAL B CG1   1 
ATOM   8934  C  CG2   . VAL B 1 419 ? 132.065 147.479 172.554 1.00 24.47 ?  419 VAL B CG2   1 
ATOM   8935  N  N     . MET B 1 420 ? 130.471 145.706 176.541 1.00 36.25 ?  420 MET B N     1 
ATOM   8936  C  CA    . MET B 1 420 ? 129.604 145.661 177.710 1.00 33.76 ?  420 MET B CA    1 
ATOM   8937  C  C     . MET B 1 420 ? 130.415 145.605 178.998 1.00 31.81 ?  420 MET B C     1 
ATOM   8938  O  O     . MET B 1 420 ? 130.050 146.234 179.997 1.00 34.69 ?  420 MET B O     1 
ATOM   8939  C  CB    . MET B 1 420 ? 128.670 144.456 177.605 1.00 33.22 ?  420 MET B CB    1 
ATOM   8940  C  CG    . MET B 1 420 ? 127.296 144.772 177.038 1.00 24.56 ?  420 MET B CG    1 
ATOM   8941  S  SD    . MET B 1 420 ? 126.737 146.445 177.389 1.00 41.26 ?  420 MET B SD    1 
ATOM   8942  C  CE    . MET B 1 420 ? 125.965 146.195 178.980 1.00 33.19 ?  420 MET B CE    1 
ATOM   8943  N  N     . GLU B 1 421 ? 131.524 144.857 178.994 1.00 39.01 ?  421 GLU B N     1 
ATOM   8944  C  CA    . GLU B 1 421 ? 132.358 144.767 180.188 1.00 38.31 ?  421 GLU B CA    1 
ATOM   8945  C  C     . GLU B 1 421 ? 133.110 146.067 180.453 1.00 36.84 ?  421 GLU B C     1 
ATOM   8946  O  O     . GLU B 1 421 ? 133.407 146.382 181.611 1.00 39.33 ?  421 GLU B O     1 
ATOM   8947  C  CB    . GLU B 1 421 ? 133.330 143.591 180.064 1.00 33.75 ?  421 GLU B CB    1 
ATOM   8948  C  CG    . GLU B 1 421 ? 134.618 143.905 179.319 1.00 38.99 ?  421 GLU B CG    1 
ATOM   8949  C  CD    . GLU B 1 421 ? 135.653 142.804 179.438 1.00 46.20 ?  421 GLU B CD    1 
ATOM   8950  O  OE1   . GLU B 1 421 ? 136.422 142.811 180.422 1.00 43.21 ?  421 GLU B OE1   1 
ATOM   8951  O  OE2   . GLU B 1 421 ? 135.698 141.933 178.545 1.00 43.32 -1 421 GLU B OE2   1 
ATOM   8952  N  N     . HIS B 1 422 ? 133.426 146.828 179.407 1.00 36.68 ?  422 HIS B N     1 
ATOM   8953  C  CA    . HIS B 1 422 ? 134.092 148.114 179.563 1.00 37.50 ?  422 HIS B CA    1 
ATOM   8954  C  C     . HIS B 1 422 ? 133.120 149.261 179.795 1.00 41.79 ?  422 HIS B C     1 
ATOM   8955  O  O     . HIS B 1 422 ? 133.568 150.378 180.076 1.00 45.27 ?  422 HIS B O     1 
ATOM   8956  C  CB    . HIS B 1 422 ? 134.951 148.425 178.334 1.00 35.17 ?  422 HIS B CB    1 
ATOM   8957  C  CG    . HIS B 1 422 ? 136.295 147.768 178.348 1.00 38.00 ?  422 HIS B CG    1 
ATOM   8958  N  ND1   . HIS B 1 422 ? 136.458 146.403 178.259 1.00 39.87 ?  422 HIS B ND1   1 
ATOM   8959  C  CD2   . HIS B 1 422 ? 137.541 148.289 178.437 1.00 40.59 ?  422 HIS B CD2   1 
ATOM   8960  C  CE1   . HIS B 1 422 ? 137.746 146.110 178.295 1.00 41.07 ?  422 HIS B CE1   1 
ATOM   8961  N  NE2   . HIS B 1 422 ? 138.424 147.237 178.403 1.00 42.75 ?  422 HIS B NE2   1 
ATOM   8962  N  N     . LYS B 1 423 ? 131.813 149.011 179.687 1.00 43.51 ?  423 LYS B N     1 
ATOM   8963  C  CA    . LYS B 1 423 ? 130.789 150.043 179.852 1.00 44.04 ?  423 LYS B CA    1 
ATOM   8964  C  C     . LYS B 1 423 ? 131.039 151.217 178.911 1.00 47.14 ?  423 LYS B C     1 
ATOM   8965  O  O     . LYS B 1 423 ? 130.898 152.383 179.282 1.00 48.45 ?  423 LYS B O     1 
ATOM   8966  C  CB    . LYS B 1 423 ? 130.712 150.514 181.306 1.00 43.16 ?  423 LYS B CB    1 
ATOM   8967  C  CG    . LYS B 1 423 ? 130.074 149.513 182.251 1.00 44.78 ?  423 LYS B CG    1 
ATOM   8968  C  CD    . LYS B 1 423 ? 131.056 149.073 183.324 1.00 48.99 ?  423 LYS B CD    1 
ATOM   8969  C  CE    . LYS B 1 423 ? 130.528 147.879 184.102 1.00 47.55 ?  423 LYS B CE    1 
ATOM   8970  N  NZ    . LYS B 1 423 ? 130.976 146.585 183.515 1.00 42.92 1  423 LYS B NZ    1 
ATOM   8971  N  N     . SER B 1 424 ? 131.410 150.902 177.674 1.00 32.45 ?  424 SER B N     1 
ATOM   8972  C  CA    . SER B 1 424 ? 131.847 151.894 176.699 1.00 32.35 ?  424 SER B CA    1 
ATOM   8973  C  C     . SER B 1 424 ? 131.077 151.750 175.395 1.00 36.47 ?  424 SER B C     1 
ATOM   8974  O  O     . SER B 1 424 ? 131.657 151.689 174.311 1.00 38.35 ?  424 SER B O     1 
ATOM   8975  C  CB    . SER B 1 424 ? 133.347 151.776 176.448 1.00 36.99 ?  424 SER B CB    1 
ATOM   8976  O  OG    . SER B 1 424 ? 133.655 150.577 175.761 1.00 34.67 ?  424 SER B OG    1 
ATOM   8977  N  N     . ILE B 1 425 ? 129.748 151.683 175.480 1.00 35.88 ?  425 ILE B N     1 
ATOM   8978  C  CA    . ILE B 1 425 ? 128.943 151.647 174.260 1.00 28.36 ?  425 ILE B CA    1 
ATOM   8979  C  C     . ILE B 1 425 ? 129.110 152.945 173.481 1.00 34.18 ?  425 ILE B C     1 
ATOM   8980  O  O     . ILE B 1 425 ? 129.370 152.936 172.274 1.00 39.14 ?  425 ILE B O     1 
ATOM   8981  C  CB    . ILE B 1 425 ? 127.464 151.380 174.592 1.00 33.41 ?  425 ILE B CB    1 
ATOM   8982  C  CG1   . ILE B 1 425 ? 127.276 149.954 175.107 1.00 33.95 ?  425 ILE B CG1   1 
ATOM   8983  C  CG2   . ILE B 1 425 ? 126.597 151.614 173.367 1.00 29.70 ?  425 ILE B CG2   1 
ATOM   8984  C  CD1   . ILE B 1 425 ? 125.839 149.602 175.399 1.00 34.91 ?  425 ILE B CD1   1 
ATOM   8985  N  N     . GLU B 1 426 ? 128.990 154.081 174.171 1.00 32.69 ?  426 GLU B N     1 
ATOM   8986  C  CA    . GLU B 1 426 ? 129.058 155.374 173.496 1.00 31.07 ?  426 GLU B CA    1 
ATOM   8987  C  C     . GLU B 1 426 ? 130.422 155.601 172.860 1.00 31.81 ?  426 GLU B C     1 
ATOM   8988  O  O     . GLU B 1 426 ? 130.520 155.929 171.672 1.00 42.23 ?  426 GLU B O     1 
ATOM   8989  C  CB    . GLU B 1 426 ? 128.734 156.489 174.489 1.00 32.52 ?  426 GLU B CB    1 
ATOM   8990  C  CG    . GLU B 1 426 ? 129.147 157.873 174.029 1.00 33.06 ?  426 GLU B CG    1 
ATOM   8991  C  CD    . GLU B 1 426 ? 128.973 158.916 175.112 1.00 42.02 ?  426 GLU B CD    1 
ATOM   8992  O  OE1   . GLU B 1 426 ? 128.634 158.537 176.252 1.00 42.80 ?  426 GLU B OE1   1 
ATOM   8993  O  OE2   . GLU B 1 426 ? 129.178 160.113 174.827 1.00 46.74 -1 426 GLU B OE2   1 
ATOM   8994  N  N     . LYS B 1 427 ? 131.492 155.428 173.640 1.00 33.13 ?  427 LYS B N     1 
ATOM   8995  C  CA    . LYS B 1 427 ? 132.832 155.715 173.139 1.00 31.12 ?  427 LYS B CA    1 
ATOM   8996  C  C     . LYS B 1 427 ? 133.219 154.765 172.015 1.00 32.71 ?  427 LYS B C     1 
ATOM   8997  O  O     . LYS B 1 427 ? 133.760 155.198 170.991 1.00 37.83 ?  427 LYS B O     1 
ATOM   8998  C  CB    . LYS B 1 427 ? 133.872 155.652 174.269 1.00 34.87 ?  427 LYS B CB    1 
ATOM   8999  C  CG    . LYS B 1 427 ? 133.860 156.800 175.306 1.00 41.24 ?  427 LYS B CG    1 
ATOM   9000  C  CD    . LYS B 1 427 ? 132.598 156.953 176.172 1.00 40.26 ?  427 LYS B CD    1 
ATOM   9001  C  CE    . LYS B 1 427 ? 131.982 155.619 176.584 1.00 36.14 ?  427 LYS B CE    1 
ATOM   9002  N  NZ    . LYS B 1 427 ? 130.867 155.785 177.555 1.00 40.00 1  427 LYS B NZ    1 
ATOM   9003  N  N     . THR B 1 428 ? 132.952 153.469 172.185 1.00 28.98 ?  428 THR B N     1 
ATOM   9004  C  CA    . THR B 1 428 ? 133.277 152.512 171.134 1.00 24.30 ?  428 THR B CA    1 
ATOM   9005  C  C     . THR B 1 428 ? 132.473 152.783 169.872 1.00 26.69 ?  428 THR B C     1 
ATOM   9006  O  O     . THR B 1 428 ? 133.016 152.729 168.764 1.00 34.84 ?  428 THR B O     1 
ATOM   9007  C  CB    . THR B 1 428 ? 133.040 151.080 171.614 1.00 21.44 ?  428 THR B CB    1 
ATOM   9008  O  OG1   . THR B 1 428 ? 133.680 150.885 172.881 1.00 25.87 ?  428 THR B OG1   1 
ATOM   9009  C  CG2   . THR B 1 428 ? 133.603 150.092 170.612 1.00 27.34 ?  428 THR B CG2   1 
ATOM   9010  N  N     . VAL B 1 429 ? 131.180 153.083 170.016 1.00 26.34 ?  429 VAL B N     1 
ATOM   9011  C  CA    . VAL B 1 429 ? 130.350 153.348 168.844 1.00 23.04 ?  429 VAL B CA    1 
ATOM   9012  C  C     . VAL B 1 429 ? 130.852 154.579 168.105 1.00 24.84 ?  429 VAL B C     1 
ATOM   9013  O  O     . VAL B 1 429 ? 130.964 154.577 166.874 1.00 30.08 ?  429 VAL B O     1 
ATOM   9014  C  CB    . VAL B 1 429 ? 128.871 153.493 169.252 1.00 24.85 ?  429 VAL B CB    1 
ATOM   9015  C  CG1   . VAL B 1 429 ? 128.104 154.254 168.193 1.00 23.31 ?  429 VAL B CG1   1 
ATOM   9016  C  CG2   . VAL B 1 429 ? 128.244 152.133 169.459 1.00 26.10 ?  429 VAL B CG2   1 
ATOM   9017  N  N     . LYS B 1 430 ? 131.181 155.644 168.838 1.00 29.56 ?  430 LYS B N     1 
ATOM   9018  C  CA    . LYS B 1 430 ? 131.613 156.874 168.184 1.00 24.43 ?  430 LYS B CA    1 
ATOM   9019  C  C     . LYS B 1 430 ? 132.979 156.713 167.527 1.00 23.08 ?  430 LYS B C     1 
ATOM   9020  O  O     . LYS B 1 430 ? 133.195 157.197 166.409 1.00 31.25 ?  430 LYS B O     1 
ATOM   9021  C  CB    . LYS B 1 430 ? 131.613 158.024 169.188 1.00 26.41 ?  430 LYS B CB    1 
ATOM   9022  C  CG    . LYS B 1 430 ? 130.213 158.407 169.641 1.00 23.26 ?  430 LYS B CG    1 
ATOM   9023  C  CD    . LYS B 1 430 ? 130.194 159.728 170.378 1.00 31.44 ?  430 LYS B CD    1 
ATOM   9024  C  CE    . LYS B 1 430 ? 128.771 160.145 170.699 1.00 34.84 ?  430 LYS B CE    1 
ATOM   9025  N  NZ    . LYS B 1 430 ? 128.725 161.398 171.497 1.00 36.10 1  430 LYS B NZ    1 
ATOM   9026  N  N     . LEU B 1 431 ? 133.915 156.029 168.191 1.00 30.77 ?  431 LEU B N     1 
ATOM   9027  C  CA    . LEU B 1 431 ? 135.223 155.804 167.583 1.00 22.41 ?  431 LEU B CA    1 
ATOM   9028  C  C     . LEU B 1 431 ? 135.121 154.889 166.368 1.00 23.25 ?  431 LEU B C     1 
ATOM   9029  O  O     . LEU B 1 431 ? 135.815 155.100 165.366 1.00 32.08 ?  431 LEU B O     1 
ATOM   9030  C  CB    . LEU B 1 431 ? 136.188 155.228 168.616 1.00 30.91 ?  431 LEU B CB    1 
ATOM   9031  C  CG    . LEU B 1 431 ? 137.061 156.232 169.367 1.00 32.90 ?  431 LEU B CG    1 
ATOM   9032  C  CD1   . LEU B 1 431 ? 137.825 155.541 170.481 1.00 28.93 ?  431 LEU B CD1   1 
ATOM   9033  C  CD2   . LEU B 1 431 ? 138.013 156.932 168.416 1.00 34.52 ?  431 LEU B CD2   1 
ATOM   9034  N  N     . ALA B 1 432 ? 134.269 153.863 166.439 1.00 25.20 ?  432 ALA B N     1 
ATOM   9035  C  CA    . ALA B 1 432 ? 134.050 152.998 165.288 1.00 20.02 ?  432 ALA B CA    1 
ATOM   9036  C  C     . ALA B 1 432 ? 133.426 153.770 164.135 1.00 25.84 ?  432 ALA B C     1 
ATOM   9037  O  O     . ALA B 1 432 ? 133.777 153.550 162.972 1.00 29.63 ?  432 ALA B O     1 
ATOM   9038  C  CB    . ALA B 1 432 ? 133.169 151.815 165.685 1.00 24.13 ?  432 ALA B CB    1 
ATOM   9039  N  N     . THR B 1 433 ? 132.493 154.675 164.439 1.00 27.18 ?  433 THR B N     1 
ATOM   9040  C  CA    . THR B 1 433 ? 131.915 155.525 163.406 1.00 17.25 ?  433 THR B CA    1 
ATOM   9041  C  C     . THR B 1 433 ? 132.978 156.403 162.763 1.00 25.04 ?  433 THR B C     1 
ATOM   9042  O  O     . THR B 1 433 ? 132.999 156.567 161.539 1.00 33.17 ?  433 THR B O     1 
ATOM   9043  C  CB    . THR B 1 433 ? 130.796 156.382 164.003 1.00 24.03 ?  433 THR B CB    1 
ATOM   9044  O  OG1   . THR B 1 433 ? 129.809 155.532 164.597 1.00 32.99 ?  433 THR B OG1   1 
ATOM   9045  C  CG2   . THR B 1 433 ? 130.140 157.236 162.931 1.00 24.11 ?  433 THR B CG2   1 
ATOM   9046  N  N     . ASP B 1 434 ? 133.874 156.972 163.571 1.00 24.94 ?  434 ASP B N     1 
ATOM   9047  C  CA    . ASP B 1 434 ? 134.954 157.789 163.023 1.00 18.95 ?  434 ASP B CA    1 
ATOM   9048  C  C     . ASP B 1 434 ? 135.869 156.968 162.121 1.00 19.23 ?  434 ASP B C     1 
ATOM   9049  O  O     . ASP B 1 434 ? 136.259 157.423 161.038 1.00 26.71 ?  434 ASP B O     1 
ATOM   9050  C  CB    . ASP B 1 434 ? 135.755 158.427 164.156 1.00 25.35 ?  434 ASP B CB    1 
ATOM   9051  C  CG    . ASP B 1 434 ? 134.982 159.504 164.880 1.00 31.05 ?  434 ASP B CG    1 
ATOM   9052  O  OD1   . ASP B 1 434 ? 134.098 160.124 164.255 1.00 36.85 ?  434 ASP B OD1   1 
ATOM   9053  O  OD2   . ASP B 1 434 ? 135.259 159.733 166.076 1.00 33.18 -1 434 ASP B OD2   1 
ATOM   9054  N  N     . SER B 1 435 ? 136.224 155.755 162.550 1.00 22.83 ?  435 SER B N     1 
ATOM   9055  C  CA    . SER B 1 435 ? 137.101 154.910 161.743 1.00 15.90 ?  435 SER B CA    1 
ATOM   9056  C  C     . SER B 1 435 ? 136.429 154.492 160.440 1.00 23.26 ?  435 SER B C     1 
ATOM   9057  O  O     . SER B 1 435 ? 137.066 154.489 159.379 1.00 31.44 ?  435 SER B O     1 
ATOM   9058  C  CB    . SER B 1 435 ? 137.529 153.683 162.547 1.00 21.15 ?  435 SER B CB    1 
ATOM   9059  O  OG    . SER B 1 435 ? 136.441 152.802 162.758 1.00 22.23 ?  435 SER B OG    1 
ATOM   9060  N  N     . LEU B 1 436 ? 135.146 154.132 160.499 1.00 18.81 ?  436 LEU B N     1 
ATOM   9061  C  CA    . LEU B 1 436 ? 134.419 153.766 159.291 1.00 11.47 ?  436 LEU B CA    1 
ATOM   9062  C  C     . LEU B 1 436 ? 134.279 154.956 158.352 1.00 19.15 ?  436 LEU B C     1 
ATOM   9063  O  O     . LEU B 1 436 ? 134.369 154.804 157.129 1.00 31.33 ?  436 LEU B O     1 
ATOM   9064  C  CB    . LEU B 1 436 ? 133.049 153.202 159.659 1.00 22.51 ?  436 LEU B CB    1 
ATOM   9065  C  CG    . LEU B 1 436 ? 133.060 151.832 160.333 1.00 18.95 ?  436 LEU B CG    1 
ATOM   9066  C  CD1   . LEU B 1 436 ? 131.753 151.585 161.057 1.00 16.54 ?  436 LEU B CD1   1 
ATOM   9067  C  CD2   . LEU B 1 436 ? 133.326 150.748 159.314 1.00 20.71 ?  436 LEU B CD2   1 
ATOM   9068  N  N     . THR B 1 437 ? 134.063 156.150 158.906 1.00 22.48 ?  437 THR B N     1 
ATOM   9069  C  CA    . THR B 1 437 ? 134.034 157.355 158.087 1.00 19.89 ?  437 THR B CA    1 
ATOM   9070  C  C     . THR B 1 437 ? 135.371 157.578 157.397 1.00 24.99 ?  437 THR B C     1 
ATOM   9071  O  O     . THR B 1 437 ? 135.414 157.907 156.207 1.00 35.50 ?  437 THR B O     1 
ATOM   9072  C  CB    . THR B 1 437 ? 133.667 158.563 158.947 1.00 15.98 ?  437 THR B CB    1 
ATOM   9073  O  OG1   . THR B 1 437 ? 132.418 158.319 159.603 1.00 16.78 ?  437 THR B OG1   1 
ATOM   9074  C  CG2   . THR B 1 437 ? 133.549 159.809 158.094 1.00 21.42 ?  437 THR B CG2   1 
ATOM   9075  N  N     . HIS B 1 438 ? 136.476 157.404 158.127 1.00 18.58 ?  438 HIS B N     1 
ATOM   9076  C  CA    . HIS B 1 438 ? 137.793 157.557 157.516 1.00 18.73 ?  438 HIS B CA    1 
ATOM   9077  C  C     . HIS B 1 438 ? 138.001 156.549 156.393 1.00 20.69 ?  438 HIS B C     1 
ATOM   9078  O  O     . HIS B 1 438 ? 138.520 156.896 155.325 1.00 32.55 ?  438 HIS B O     1 
ATOM   9079  C  CB    . HIS B 1 438 ? 138.888 157.410 158.571 1.00 25.97 ?  438 HIS B CB    1 
ATOM   9080  C  CG    . HIS B 1 438 ? 140.272 157.424 158.003 1.00 28.78 ?  438 HIS B CG    1 
ATOM   9081  N  ND1   . HIS B 1 438 ? 140.964 158.589 157.754 1.00 26.69 ?  438 HIS B ND1   1 
ATOM   9082  C  CD2   . HIS B 1 438 ? 141.090 156.414 157.621 1.00 30.25 ?  438 HIS B CD2   1 
ATOM   9083  C  CE1   . HIS B 1 438 ? 142.148 158.298 157.250 1.00 27.89 ?  438 HIS B CE1   1 
ATOM   9084  N  NE2   . HIS B 1 438 ? 142.250 156.984 157.158 1.00 30.94 ?  438 HIS B NE2   1 
ATOM   9085  N  N     . VAL B 1 439 ? 137.602 155.296 156.616 1.00 23.92 ?  439 VAL B N     1 
ATOM   9086  C  CA    . VAL B 1 439 ? 137.733 154.280 155.575 1.00 17.52 ?  439 VAL B CA    1 
ATOM   9087  C  C     . VAL B 1 439 ? 136.897 154.656 154.359 1.00 27.55 ?  439 VAL B C     1 
ATOM   9088  O  O     . VAL B 1 439 ? 137.315 154.457 153.212 1.00 34.37 ?  439 VAL B O     1 
ATOM   9089  C  CB    . VAL B 1 439 ? 137.346 152.894 156.126 1.00 22.88 ?  439 VAL B CB    1 
ATOM   9090  C  CG1   . VAL B 1 439 ? 137.302 151.866 155.009 1.00 25.20 ?  439 VAL B CG1   1 
ATOM   9091  C  CG2   . VAL B 1 439 ? 138.319 152.464 157.202 1.00 21.17 ?  439 VAL B CG2   1 
ATOM   9092  N  N     . SER B 1 440 ? 135.703 155.205 154.590 1.00 27.83 ?  440 SER B N     1 
ATOM   9093  C  CA    . SER B 1 440 ? 134.853 155.630 153.482 1.00 17.71 ?  440 SER B CA    1 
ATOM   9094  C  C     . SER B 1 440 ? 135.498 156.757 152.684 1.00 23.44 ?  440 SER B C     1 
ATOM   9095  O  O     . SER B 1 440 ? 135.492 156.733 151.448 1.00 33.92 ?  440 SER B O     1 
ATOM   9096  C  CB    . SER B 1 440 ? 133.486 156.059 154.014 1.00 26.57 ?  440 SER B CB    1 
ATOM   9097  O  OG    . SER B 1 440 ? 132.550 156.214 152.963 1.00 33.83 ?  440 SER B OG    1 
ATOM   9098  N  N     . GLU B 1 441 ? 136.057 157.757 153.371 1.00 24.94 ?  441 GLU B N     1 
ATOM   9099  C  CA    . GLU B 1 441 ? 136.681 158.875 152.663 1.00 20.17 ?  441 GLU B CA    1 
ATOM   9100  C  C     . GLU B 1 441 ? 137.928 158.438 151.905 1.00 29.91 ?  441 GLU B C     1 
ATOM   9101  O  O     . GLU B 1 441 ? 138.176 158.911 150.790 1.00 41.35 ?  441 GLU B O     1 
ATOM   9102  C  CB    . GLU B 1 441 ? 137.024 160.017 153.623 1.00 22.01 ?  441 GLU B CB    1 
ATOM   9103  C  CG    . GLU B 1 441 ? 135.967 160.348 154.654 1.00 30.91 ?  441 GLU B CG    1 
ATOM   9104  C  CD    . GLU B 1 441 ? 134.684 160.869 154.038 1.00 42.82 ?  441 GLU B CD    1 
ATOM   9105  O  OE1   . GLU B 1 441 ? 134.620 162.076 153.728 1.00 39.73 ?  441 GLU B OE1   1 
ATOM   9106  O  OE2   . GLU B 1 441 ? 133.737 160.073 153.867 1.00 47.27 -1 441 GLU B OE2   1 
ATOM   9107  N  N     . THR B 1 442 ? 138.725 157.545 152.484 1.00 32.89 ?  442 THR B N     1 
ATOM   9108  C  CA    . THR B 1 442 ? 139.978 157.156 151.848 1.00 29.78 ?  442 THR B CA    1 
ATOM   9109  C  C     . THR B 1 442 ? 139.795 156.108 150.759 1.00 29.77 ?  442 THR B C     1 
ATOM   9110  O  O     . THR B 1 442 ? 140.782 155.723 150.123 1.00 38.02 ?  442 THR B O     1 
ATOM   9111  C  CB    . THR B 1 442 ? 140.970 156.639 152.895 1.00 31.77 ?  442 THR B CB    1 
ATOM   9112  O  OG1   . THR B 1 442 ? 140.427 155.485 153.546 1.00 38.47 ?  442 THR B OG1   1 
ATOM   9113  C  CG2   . THR B 1 442 ? 141.259 157.715 153.925 1.00 28.66 ?  442 THR B CG2   1 
ATOM   9114  N  N     . THR B 1 443 ? 138.574 155.642 150.524 1.00 33.92 ?  443 THR B N     1 
ATOM   9115  C  CA    . THR B 1 443 ? 138.306 154.662 149.481 1.00 37.93 ?  443 THR B CA    1 
ATOM   9116  C  C     . THR B 1 443 ? 137.997 155.385 148.176 1.00 38.05 ?  443 THR B C     1 
ATOM   9117  O  O     . THR B 1 443 ? 137.071 156.200 148.115 1.00 39.87 ?  443 THR B O     1 
ATOM   9118  C  CB    . THR B 1 443 ? 137.143 153.753 149.874 1.00 36.18 ?  443 THR B CB    1 
ATOM   9119  O  OG1   . THR B 1 443 ? 137.456 153.075 151.096 1.00 40.97 ?  443 THR B OG1   1 
ATOM   9120  C  CG2   . THR B 1 443 ? 136.887 152.725 148.786 1.00 29.03 ?  443 THR B CG2   1 
ATOM   9121  N  N     . ASP B 1 444 ? 138.774 155.086 147.137 1.00 46.08 ?  444 ASP B N     1 
ATOM   9122  C  CA    . ASP B 1 444 ? 138.542 155.631 145.801 1.00 44.30 ?  444 ASP B CA    1 
ATOM   9123  C  C     . ASP B 1 444 ? 138.717 154.498 144.802 1.00 47.74 ?  444 ASP B C     1 
ATOM   9124  O  O     . ASP B 1 444 ? 139.819 153.956 144.663 1.00 49.21 ?  444 ASP B O     1 
ATOM   9125  C  CB    . ASP B 1 444 ? 139.495 156.787 145.495 1.00 47.29 ?  444 ASP B CB    1 
ATOM   9126  C  CG    . ASP B 1 444 ? 138.904 157.782 144.516 1.00 51.21 ?  444 ASP B CG    1 
ATOM   9127  O  OD1   . ASP B 1 444 ? 137.796 158.290 144.780 1.00 48.14 ?  444 ASP B OD1   1 
ATOM   9128  O  OD2   . ASP B 1 444 ? 139.550 158.057 143.483 1.00 52.79 -1 444 ASP B OD2   1 
ATOM   9129  N  N     . ILE B 1 445 ? 137.640 154.139 144.112 1.00 38.65 ?  445 ILE B N     1 
ATOM   9130  C  CA    . ILE B 1 445 ? 137.643 153.036 143.159 1.00 40.61 ?  445 ILE B CA    1 
ATOM   9131  C  C     . ILE B 1 445 ? 137.545 153.629 141.760 1.00 45.93 ?  445 ILE B C     1 
ATOM   9132  O  O     . ILE B 1 445 ? 136.587 154.344 141.443 1.00 48.01 ?  445 ILE B O     1 
ATOM   9133  C  CB    . ILE B 1 445 ? 136.499 152.051 143.443 1.00 38.89 ?  445 ILE B CB    1 
ATOM   9134  C  CG1   . ILE B 1 445 ? 136.935 151.044 144.505 1.00 38.21 ?  445 ILE B CG1   1 
ATOM   9135  C  CG2   . ILE B 1 445 ? 136.106 151.308 142.182 1.00 41.28 ?  445 ILE B CG2   1 
ATOM   9136  C  CD1   . ILE B 1 445 ? 135.828 150.619 145.427 1.00 37.47 ?  445 ILE B CD1   1 
ATOM   9137  N  N     . ARG B 1 446 ? 138.541 153.337 140.925 1.00 46.10 ?  446 ARG B N     1 
ATOM   9138  C  CA    . ARG B 1 446 ? 138.717 154.037 139.662 1.00 46.88 ?  446 ARG B CA    1 
ATOM   9139  C  C     . ARG B 1 446 ? 137.994 153.385 138.491 1.00 48.00 ?  446 ARG B C     1 
ATOM   9140  O  O     . ARG B 1 446 ? 137.976 153.962 137.399 1.00 43.19 ?  446 ARG B O     1 
ATOM   9141  C  CB    . ARG B 1 446 ? 140.210 154.152 139.331 1.00 43.09 ?  446 ARG B CB    1 
ATOM   9142  C  CG    . ARG B 1 446 ? 141.112 154.315 140.548 1.00 41.76 ?  446 ARG B CG    1 
ATOM   9143  C  CD    . ARG B 1 446 ? 140.887 155.598 141.364 1.00 46.98 ?  446 ARG B CD    1 
ATOM   9144  N  NE    . ARG B 1 446 ? 141.132 156.832 140.623 1.00 48.53 ?  446 ARG B NE    1 
ATOM   9145  C  CZ    . ARG B 1 446 ? 140.223 157.511 139.934 1.00 49.20 ?  446 ARG B CZ    1 
ATOM   9146  N  NH1   . ARG B 1 446 ? 138.952 157.149 139.917 1.00 45.47 1  446 ARG B NH1   1 
ATOM   9147  N  NH2   . ARG B 1 446 ? 140.597 158.600 139.268 1.00 41.80 ?  446 ARG B NH2   1 
ATOM   9148  N  N     . ASN B 1 447 ? 137.397 152.209 138.680 1.00 37.86 ?  447 ASN B N     1 
ATOM   9149  C  CA    . ASN B 1 447 ? 136.747 151.505 137.587 1.00 30.21 ?  447 ASN B CA    1 
ATOM   9150  C  C     . ASN B 1 447 ? 135.273 151.225 137.834 1.00 33.78 ?  447 ASN B C     1 
ATOM   9151  O  O     . ASN B 1 447 ? 134.642 150.547 137.018 1.00 41.74 ?  447 ASN B O     1 
ATOM   9152  C  CB    . ASN B 1 447 ? 137.477 150.189 137.293 1.00 35.06 ?  447 ASN B CB    1 
ATOM   9153  C  CG    . ASN B 1 447 ? 138.574 150.356 136.265 1.00 33.26 ?  447 ASN B CG    1 
ATOM   9154  O  OD1   . ASN B 1 447 ? 138.304 150.534 135.079 1.00 39.91 ?  447 ASN B OD1   1 
ATOM   9155  N  ND2   . ASN B 1 447 ? 139.820 150.303 136.715 1.00 29.19 ?  447 ASN B ND2   1 
ATOM   9156  N  N     . ALA B 1 448 ? 134.708 151.721 138.934 1.00 35.20 ?  448 ALA B N     1 
ATOM   9157  C  CA    . ALA B 1 448 ? 133.279 151.628 139.221 1.00 30.98 ?  448 ALA B CA    1 
ATOM   9158  C  C     . ALA B 1 448 ? 132.783 153.044 139.477 1.00 34.36 ?  448 ALA B C     1 
ATOM   9159  O  O     . ALA B 1 448 ? 132.774 153.508 140.627 1.00 35.04 ?  448 ALA B O     1 
ATOM   9160  C  CB    . ALA B 1 448 ? 133.008 150.716 140.413 1.00 26.58 ?  448 ALA B CB    1 
ATOM   9161  N  N     . PRO B 1 449 ? 132.378 153.772 138.433 1.00 32.91 ?  449 PRO B N     1 
ATOM   9162  C  CA    . PRO B 1 449 ? 132.013 155.184 138.637 1.00 25.26 ?  449 PRO B CA    1 
ATOM   9163  C  C     . PRO B 1 449 ? 130.812 155.368 139.542 1.00 30.13 ?  449 PRO B C     1 
ATOM   9164  O  O     . PRO B 1 449 ? 130.778 156.322 140.328 1.00 29.44 ?  449 PRO B O     1 
ATOM   9165  C  CB    . PRO B 1 449 ? 131.740 155.695 137.214 1.00 27.13 ?  449 PRO B CB    1 
ATOM   9166  C  CG    . PRO B 1 449 ? 131.905 154.525 136.297 1.00 30.35 ?  449 PRO B CG    1 
ATOM   9167  C  CD    . PRO B 1 449 ? 132.002 153.281 137.098 1.00 24.54 ?  449 PRO B CD    1 
ATOM   9168  N  N     . ALA B 1 450 ? 129.822 154.477 139.457 1.00 32.95 ?  450 ALA B N     1 
ATOM   9169  C  CA    . ALA B 1 450 ? 128.648 154.598 140.315 1.00 19.72 ?  450 ALA B CA    1 
ATOM   9170  C  C     . ALA B 1 450 ? 128.988 154.275 141.762 1.00 27.50 ?  450 ALA B C     1 
ATOM   9171  O  O     . ALA B 1 450 ? 128.490 154.932 142.683 1.00 33.23 ?  450 ALA B O     1 
ATOM   9172  C  CB    . ALA B 1 450 ? 127.531 153.693 139.803 1.00 23.31 ?  450 ALA B CB    1 
ATOM   9173  N  N     . VAL B 1 451 ? 129.844 153.276 141.983 1.00 29.00 ?  451 VAL B N     1 
ATOM   9174  C  CA    . VAL B 1 451 ? 130.277 152.949 143.339 1.00 19.78 ?  451 VAL B CA    1 
ATOM   9175  C  C     . VAL B 1 451 ? 131.027 154.124 143.950 1.00 24.03 ?  451 VAL B C     1 
ATOM   9176  O  O     . VAL B 1 451 ? 130.793 154.501 145.103 1.00 36.06 ?  451 VAL B O     1 
ATOM   9177  C  CB    . VAL B 1 451 ? 131.138 151.672 143.336 1.00 28.00 ?  451 VAL B CB    1 
ATOM   9178  C  CG1   . VAL B 1 451 ? 131.948 151.568 144.615 1.00 28.64 ?  451 VAL B CG1   1 
ATOM   9179  C  CG2   . VAL B 1 451 ? 130.271 150.444 143.154 1.00 23.50 ?  451 VAL B CG2   1 
ATOM   9180  N  N     . ARG B 1 452 ? 131.938 154.722 143.181 1.00 25.98 ?  452 ARG B N     1 
ATOM   9181  C  CA    . ARG B 1 452 ? 132.699 155.865 143.677 1.00 23.15 ?  452 ARG B CA    1 
ATOM   9182  C  C     . ARG B 1 452 ? 131.793 157.061 143.950 1.00 22.13 ?  452 ARG B C     1 
ATOM   9183  O  O     . ARG B 1 452 ? 131.932 157.736 144.978 1.00 36.39 ?  452 ARG B O     1 
ATOM   9184  C  CB    . ARG B 1 452 ? 133.794 156.227 142.673 1.00 23.46 ?  452 ARG B CB    1 
ATOM   9185  C  CG    . ARG B 1 452 ? 134.648 157.417 143.066 1.00 31.33 ?  452 ARG B CG    1 
ATOM   9186  C  CD    . ARG B 1 452 ? 134.990 158.266 141.854 1.00 29.52 ?  452 ARG B CD    1 
ATOM   9187  N  NE    . ARG B 1 452 ? 133.970 158.166 140.817 1.00 41.86 ?  452 ARG B NE    1 
ATOM   9188  C  CZ    . ARG B 1 452 ? 132.951 159.003 140.681 1.00 41.89 ?  452 ARG B CZ    1 
ATOM   9189  N  NH1   . ARG B 1 452 ? 132.787 160.033 141.494 1.00 34.62 1  452 ARG B NH1   1 
ATOM   9190  N  NH2   . ARG B 1 452 ? 132.070 158.800 139.705 1.00 28.38 ?  452 ARG B NH2   1 
ATOM   9191  N  N     . ARG B 1 453 ? 130.849 157.333 143.044 1.00 23.37 ?  453 ARG B N     1 
ATOM   9192  C  CA    . ARG B 1 453 ? 129.933 158.450 143.242 1.00 22.37 ?  453 ARG B CA    1 
ATOM   9193  C  C     . ARG B 1 453 ? 129.070 158.245 144.478 1.00 29.71 ?  453 ARG B C     1 
ATOM   9194  O  O     . ARG B 1 453 ? 128.862 159.179 145.261 1.00 32.37 ?  453 ARG B O     1 
ATOM   9195  C  CB    . ARG B 1 453 ? 129.061 158.640 142.000 1.00 25.06 ?  453 ARG B CB    1 
ATOM   9196  C  CG    . ARG B 1 453 ? 127.896 159.592 142.200 1.00 25.17 ?  453 ARG B CG    1 
ATOM   9197  C  CD    . ARG B 1 453 ? 127.303 160.031 140.877 1.00 24.76 ?  453 ARG B CD    1 
ATOM   9198  N  NE    . ARG B 1 453 ? 125.893 159.673 140.767 1.00 27.52 ?  453 ARG B NE    1 
ATOM   9199  C  CZ    . ARG B 1 453 ? 124.896 160.398 141.254 1.00 29.14 ?  453 ARG B CZ    1 
ATOM   9200  N  NH1   . ARG B 1 453 ? 125.114 161.532 141.897 1.00 30.68 1  453 ARG B NH1   1 
ATOM   9201  N  NH2   . ARG B 1 453 ? 123.647 159.973 141.091 1.00 25.55 ?  453 ARG B NH2   1 
ATOM   9202  N  N     . ALA B 1 454 ? 128.562 157.026 144.678 1.00 31.94 ?  454 ALA B N     1 
ATOM   9203  C  CA    . ALA B 1 454 ? 127.734 156.758 145.845 1.00 20.44 ?  454 ALA B CA    1 
ATOM   9204  C  C     . ALA B 1 454 ? 128.548 156.773 147.130 1.00 20.06 ?  454 ALA B C     1 
ATOM   9205  O  O     . ALA B 1 454 ? 128.034 157.170 148.177 1.00 29.70 ?  454 ALA B O     1 
ATOM   9206  C  CB    . ALA B 1 454 ? 127.012 155.424 145.686 1.00 22.79 ?  454 ALA B CB    1 
ATOM   9207  N  N     . ASN B 1 455 ? 129.809 156.343 147.079 1.00 26.92 ?  455 ASN B N     1 
ATOM   9208  C  CA    . ASN B 1 455 ? 130.663 156.445 148.255 1.00 20.39 ?  455 ASN B CA    1 
ATOM   9209  C  C     . ASN B 1 455 ? 130.914 157.901 148.621 1.00 26.77 ?  455 ASN B C     1 
ATOM   9210  O  O     . ASN B 1 455 ? 130.916 158.259 149.803 1.00 39.86 ?  455 ASN B O     1 
ATOM   9211  C  CB    . ASN B 1 455 ? 131.982 155.713 148.010 1.00 20.18 ?  455 ASN B CB    1 
ATOM   9212  C  CG    . ASN B 1 455 ? 132.870 155.686 149.237 1.00 29.85 ?  455 ASN B CG    1 
ATOM   9213  O  OD1   . ASN B 1 455 ? 132.571 155.008 150.217 1.00 38.69 ?  455 ASN B OD1   1 
ATOM   9214  N  ND2   . ASN B 1 455 ? 133.970 156.425 149.187 1.00 29.79 ?  455 ASN B ND2   1 
ATOM   9215  N  N     . LYS B 1 456 ? 131.128 158.754 147.618 1.00 27.60 ?  456 LYS B N     1 
ATOM   9216  C  CA    . LYS B 1 456 ? 131.361 160.167 147.893 1.00 26.83 ?  456 LYS B CA    1 
ATOM   9217  C  C     . LYS B 1 456 ? 130.097 160.874 148.366 1.00 26.99 ?  456 LYS B C     1 
ATOM   9218  O  O     . LYS B 1 456 ? 130.173 161.775 149.207 1.00 31.45 ?  456 LYS B O     1 
ATOM   9219  C  CB    . LYS B 1 456 ? 131.920 160.855 146.649 1.00 24.22 ?  456 LYS B CB    1 
ATOM   9220  C  CG    . LYS B 1 456 ? 132.927 161.950 146.950 1.00 29.52 ?  456 LYS B CG    1 
ATOM   9221  C  CD    . LYS B 1 456 ? 132.270 163.320 146.941 1.00 35.87 ?  456 LYS B CD    1 
ATOM   9222  C  CE    . LYS B 1 456 ? 133.210 164.390 147.473 1.00 37.12 ?  456 LYS B CE    1 
ATOM   9223  N  NZ    . LYS B 1 456 ? 133.119 164.525 148.954 1.00 31.89 1  456 LYS B NZ    1 
ATOM   9224  N  N     . ALA B 1 457 ? 128.934 160.489 147.844 1.00 25.36 ?  457 ALA B N     1 
ATOM   9225  C  CA    . ALA B 1 457 ? 127.691 161.192 148.131 1.00 17.19 ?  457 ALA B CA    1 
ATOM   9226  C  C     . ALA B 1 457 ? 127.001 160.682 149.391 1.00 23.78 ?  457 ALA B C     1 
ATOM   9227  O  O     . ALA B 1 457 ? 126.684 161.465 150.291 1.00 27.47 ?  457 ALA B O     1 
ATOM   9228  C  CB    . ALA B 1 457 ? 126.744 161.074 146.934 1.00 20.86 ?  457 ALA B CB    1 
ATOM   9229  N  N     . MET B 1 458 ? 126.759 159.373 149.463 1.00 34.34 ?  458 MET B N     1 
ATOM   9230  C  CA    . MET B 1 458 ? 125.996 158.796 150.562 1.00 17.01 ?  458 MET B CA    1 
ATOM   9231  C  C     . MET B 1 458 ? 126.808 158.741 151.849 1.00 25.08 ?  458 MET B C     1 
ATOM   9232  O  O     . MET B 1 458 ? 126.255 158.936 152.937 1.00 33.26 ?  458 MET B O     1 
ATOM   9233  C  CB    . MET B 1 458 ? 125.516 157.398 150.178 1.00 18.15 ?  458 MET B CB    1 
ATOM   9234  C  CG    . MET B 1 458 ? 124.786 157.326 148.843 1.00 21.57 ?  458 MET B CG    1 
ATOM   9235  S  SD    . MET B 1 458 ? 123.003 157.559 148.972 1.00 35.77 ?  458 MET B SD    1 
ATOM   9236  C  CE    . MET B 1 458 ? 122.880 159.345 148.938 1.00 27.87 ?  458 MET B CE    1 
ATOM   9237  N  N     . LYS B 1 459 ? 128.110 158.473 151.745 1.00 15.58 ?  459 LYS B N     1 
ATOM   9238  C  CA    . LYS B 1 459 ? 128.984 158.329 152.910 1.00 18.95 ?  459 LYS B CA    1 
ATOM   9239  C  C     . LYS B 1 459 ? 128.441 157.279 153.876 1.00 20.49 ?  459 LYS B C     1 
ATOM   9240  O  O     . LYS B 1 459 ? 128.505 157.432 155.097 1.00 32.27 ?  459 LYS B O     1 
ATOM   9241  C  CB    . LYS B 1 459 ? 129.186 159.669 153.621 1.00 26.05 ?  459 LYS B CB    1 
ATOM   9242  C  CG    . LYS B 1 459 ? 129.688 160.784 152.724 1.00 31.44 ?  459 LYS B CG    1 
ATOM   9243  C  CD    . LYS B 1 459 ? 128.988 162.091 153.043 1.00 23.51 ?  459 LYS B CD    1 
ATOM   9244  C  CE    . LYS B 1 459 ? 129.382 163.181 152.068 1.00 27.85 ?  459 LYS B CE    1 
ATOM   9245  N  NZ    . LYS B 1 459 ? 128.689 164.462 152.364 1.00 33.22 1  459 LYS B NZ    1 
ATOM   9246  N  N     . SER B 1 460 ? 127.901 156.199 153.321 1.00 16.22 ?  460 SER B N     1 
ATOM   9247  C  CA    . SER B 1 460 ? 127.289 155.160 154.132 1.00 9.49  ?  460 SER B CA    1 
ATOM   9248  C  C     . SER B 1 460 ? 128.349 154.245 154.727 1.00 19.62 ?  460 SER B C     1 
ATOM   9249  O  O     . SER B 1 460 ? 129.334 153.897 154.070 1.00 32.72 ?  460 SER B O     1 
ATOM   9250  C  CB    . SER B 1 460 ? 126.305 154.340 153.301 1.00 17.17 ?  460 SER B CB    1 
ATOM   9251  O  OG    . SER B 1 460 ? 126.986 153.543 152.352 1.00 26.49 ?  460 SER B OG    1 
ATOM   9252  N  N     . ILE B 1 461 ? 128.139 153.854 155.983 1.00 19.65 ?  461 ILE B N     1 
ATOM   9253  C  CA    . ILE B 1 461 ? 129.024 152.939 156.685 1.00 15.15 ?  461 ILE B CA    1 
ATOM   9254  C  C     . ILE B 1 461 ? 128.178 151.818 157.268 1.00 20.77 ?  461 ILE B C     1 
ATOM   9255  O  O     . ILE B 1 461 ? 126.961 151.937 157.414 1.00 23.59 ?  461 ILE B O     1 
ATOM   9256  C  CB    . ILE B 1 461 ? 129.833 153.636 157.797 1.00 12.55 ?  461 ILE B CB    1 
ATOM   9257  C  CG1   . ILE B 1 461 ? 128.891 154.309 158.797 1.00 7.21  ?  461 ILE B CG1   1 
ATOM   9258  C  CG2   . ILE B 1 461 ? 130.794 154.650 157.202 1.00 18.35 ?  461 ILE B CG2   1 
ATOM   9259  C  CD1   . ILE B 1 461 ? 129.557 154.723 160.081 1.00 12.29 ?  461 ILE B CD1   1 
ATOM   9260  N  N     . GLY B 1 462 ? 128.836 150.708 157.578 1.00 20.59 ?  462 GLY B N     1 
ATOM   9261  C  CA    . GLY B 1 462 ? 128.161 149.647 158.291 1.00 9.98  ?  462 GLY B CA    1 
ATOM   9262  C  C     . GLY B 1 462 ? 128.865 149.292 159.580 1.00 11.74 ?  462 GLY B C     1 
ATOM   9263  O  O     . GLY B 1 462 ? 129.962 148.730 159.558 1.00 27.20 ?  462 GLY B O     1 
ATOM   9264  N  N     . LEU B 1 463 ? 128.240 149.601 160.709 1.00 12.75 ?  463 LEU B N     1 
ATOM   9265  C  CA    . LEU B 1 463 ? 128.774 149.256 162.021 1.00 8.74  ?  463 LEU B CA    1 
ATOM   9266  C  C     . LEU B 1 463 ? 127.960 148.093 162.570 1.00 20.47 ?  463 LEU B C     1 
ATOM   9267  O  O     . LEU B 1 463 ? 126.807 148.269 162.974 1.00 28.83 ?  463 LEU B O     1 
ATOM   9268  C  CB    . LEU B 1 463 ? 128.734 150.454 162.966 1.00 18.78 ?  463 LEU B CB    1 
ATOM   9269  C  CG    . LEU B 1 463 ? 129.161 150.160 164.405 1.00 16.77 ?  463 LEU B CG    1 
ATOM   9270  C  CD1   . LEU B 1 463 ? 130.569 149.599 164.431 1.00 3.19  ?  463 LEU B CD1   1 
ATOM   9271  C  CD2   . LEU B 1 463 ? 129.057 151.407 165.267 1.00 16.93 ?  463 LEU B CD2   1 
ATOM   9272  N  N     . GLY B 1 464 ? 128.561 146.905 162.582 1.00 22.67 ?  464 GLY B N     1 
ATOM   9273  C  CA    . GLY B 1 464 ? 127.910 145.715 163.074 1.00 13.17 ?  464 GLY B CA    1 
ATOM   9274  C  C     . GLY B 1 464 ? 128.253 145.417 164.520 1.00 9.46  ?  464 GLY B C     1 
ATOM   9275  O  O     . GLY B 1 464 ? 128.911 146.193 165.217 1.00 18.19 ?  464 GLY B O     1 
ATOM   9276  N  N     . ALA B 1 465 ? 127.788 144.258 164.973 1.00 15.21 ?  465 ALA B N     1 
ATOM   9277  C  CA    . ALA B 1 465 ? 128.072 143.770 166.310 1.00 8.92  ?  465 ALA B CA    1 
ATOM   9278  C  C     . ALA B 1 465 ? 128.303 142.271 166.239 1.00 16.15 ?  465 ALA B C     1 
ATOM   9279  O  O     . ALA B 1 465 ? 127.849 141.595 165.314 1.00 33.48 ?  465 ALA B O     1 
ATOM   9280  C  CB    . ALA B 1 465 ? 126.937 144.094 167.289 1.00 18.90 ?  465 ALA B CB    1 
ATOM   9281  N  N     . MET B 1 466 ? 129.025 141.758 167.228 1.00 22.79 ?  466 MET B N     1 
ATOM   9282  C  CA    . MET B 1 466 ? 129.314 140.336 167.311 1.00 19.06 ?  466 MET B CA    1 
ATOM   9283  C  C     . MET B 1 466 ? 129.413 139.955 168.780 1.00 18.39 ?  466 MET B C     1 
ATOM   9284  O  O     . MET B 1 466 ? 129.335 140.808 169.668 1.00 23.63 ?  466 MET B O     1 
ATOM   9285  C  CB    . MET B 1 466 ? 130.596 139.991 166.550 1.00 24.49 ?  466 MET B CB    1 
ATOM   9286  C  CG    . MET B 1 466 ? 131.859 140.403 167.272 1.00 27.81 ?  466 MET B CG    1 
ATOM   9287  S  SD    . MET B 1 466 ? 133.312 140.410 166.215 1.00 41.52 ?  466 MET B SD    1 
ATOM   9288  C  CE    . MET B 1 466 ? 134.269 141.675 167.033 1.00 25.51 ?  466 MET B CE    1 
ATOM   9289  N  N     . ASN B 1 467 ? 129.580 138.656 169.030 1.00 16.44 ?  467 ASN B N     1 
ATOM   9290  C  CA    . ASN B 1 467 ? 129.691 138.109 170.382 1.00 22.64 ?  467 ASN B CA    1 
ATOM   9291  C  C     . ASN B 1 467 ? 128.427 138.348 171.199 1.00 26.97 ?  467 ASN B C     1 
ATOM   9292  O  O     . ASN B 1 467 ? 128.489 138.536 172.415 1.00 26.62 ?  467 ASN B O     1 
ATOM   9293  C  CB    . ASN B 1 467 ? 130.912 138.670 171.117 1.00 21.75 ?  467 ASN B CB    1 
ATOM   9294  C  CG    . ASN B 1 467 ? 131.585 137.640 171.994 1.00 27.21 ?  467 ASN B CG    1 
ATOM   9295  O  OD1   . ASN B 1 467 ? 131.211 136.469 171.995 1.00 27.28 ?  467 ASN B OD1   1 
ATOM   9296  N  ND2   . ASN B 1 467 ? 132.591 138.069 172.744 1.00 30.72 ?  467 ASN B ND2   1 
ATOM   9297  N  N     . LEU B 1 468 ? 127.268 138.359 170.539 1.00 17.65 ?  468 LEU B N     1 
ATOM   9298  C  CA    . LEU B 1 468 ? 126.011 138.459 171.271 1.00 14.70 ?  468 LEU B CA    1 
ATOM   9299  C  C     . LEU B 1 468 ? 125.743 137.186 172.063 1.00 29.01 ?  468 LEU B C     1 
ATOM   9300  O  O     . LEU B 1 468 ? 125.458 137.236 173.265 1.00 33.40 ?  468 LEU B O     1 
ATOM   9301  C  CB    . LEU B 1 468 ? 124.862 138.744 170.307 1.00 24.99 ?  468 LEU B CB    1 
ATOM   9302  C  CG    . LEU B 1 468 ? 123.476 138.844 170.947 1.00 19.41 ?  468 LEU B CG    1 
ATOM   9303  C  CD1   . LEU B 1 468 ? 123.444 139.954 171.981 1.00 16.93 ?  468 LEU B CD1   1 
ATOM   9304  C  CD2   . LEU B 1 468 ? 122.406 139.057 169.895 1.00 16.14 ?  468 LEU B CD2   1 
ATOM   9305  N  N     . HIS B 1 469 ? 125.854 136.030 171.405 1.00 31.57 ?  469 HIS B N     1 
ATOM   9306  C  CA    . HIS B 1 469 ? 125.621 134.769 172.096 1.00 16.43 ?  469 HIS B CA    1 
ATOM   9307  C  C     . HIS B 1 469 ? 126.703 134.500 173.129 1.00 27.60 ?  469 HIS B C     1 
ATOM   9308  O  O     . HIS B 1 469 ? 126.417 133.967 174.204 1.00 38.08 ?  469 HIS B O     1 
ATOM   9309  C  CB    . HIS B 1 469 ? 125.537 133.618 171.096 1.00 15.93 ?  469 HIS B CB    1 
ATOM   9310  C  CG    . HIS B 1 469 ? 124.931 132.374 171.667 1.00 20.95 ?  469 HIS B CG    1 
ATOM   9311  N  ND1   . HIS B 1 469 ? 124.943 131.167 171.005 1.00 33.35 ?  469 HIS B ND1   1 
ATOM   9312  C  CD2   . HIS B 1 469 ? 124.295 132.153 172.841 1.00 27.48 ?  469 HIS B CD2   1 
ATOM   9313  C  CE1   . HIS B 1 469 ? 124.341 130.255 171.747 1.00 26.03 ?  469 HIS B CE1   1 
ATOM   9314  N  NE2   . HIS B 1 469 ? 123.939 130.828 172.867 1.00 25.19 ?  469 HIS B NE2   1 
ATOM   9315  N  N     . GLY B 1 470 ? 127.950 134.855 172.823 1.00 20.38 ?  470 GLY B N     1 
ATOM   9316  C  CA    . GLY B 1 470 ? 129.007 134.698 173.806 1.00 23.00 ?  470 GLY B CA    1 
ATOM   9317  C  C     . GLY B 1 470 ? 128.773 135.542 175.042 1.00 16.85 ?  470 GLY B C     1 
ATOM   9318  O  O     . GLY B 1 470 ? 128.922 135.066 176.170 1.00 35.43 ?  470 GLY B O     1 
ATOM   9319  N  N     . TYR B 1 471 ? 128.382 136.803 174.847 1.00 17.13 ?  471 TYR B N     1 
ATOM   9320  C  CA    . TYR B 1 471 ? 128.106 137.675 175.982 1.00 20.16 ?  471 TYR B CA    1 
ATOM   9321  C  C     . TYR B 1 471 ? 126.921 137.167 176.794 1.00 25.71 ?  471 TYR B C     1 
ATOM   9322  O  O     . TYR B 1 471 ? 126.942 137.212 178.029 1.00 30.05 ?  471 TYR B O     1 
ATOM   9323  C  CB    . TYR B 1 471 ? 127.845 139.102 175.505 1.00 25.45 ?  471 TYR B CB    1 
ATOM   9324  C  CG    . TYR B 1 471 ? 127.280 139.992 176.585 1.00 24.40 ?  471 TYR B CG    1 
ATOM   9325  C  CD1   . TYR B 1 471 ? 128.099 140.521 177.570 1.00 25.10 ?  471 TYR B CD1   1 
ATOM   9326  C  CD2   . TYR B 1 471 ? 125.924 140.281 176.636 1.00 15.35 ?  471 TYR B CD2   1 
ATOM   9327  C  CE1   . TYR B 1 471 ? 127.587 141.324 178.565 1.00 22.93 ?  471 TYR B CE1   1 
ATOM   9328  C  CE2   . TYR B 1 471 ? 125.405 141.075 177.631 1.00 19.90 ?  471 TYR B CE2   1 
ATOM   9329  C  CZ    . TYR B 1 471 ? 126.239 141.598 178.588 1.00 26.35 ?  471 TYR B CZ    1 
ATOM   9330  O  OH    . TYR B 1 471 ? 125.719 142.398 179.577 1.00 36.38 ?  471 TYR B OH    1 
ATOM   9331  N  N     . LEU B 1 472 ? 125.873 136.691 176.118 1.00 28.49 ?  472 LEU B N     1 
ATOM   9332  C  CA    . LEU B 1 472 ? 124.690 136.223 176.832 1.00 21.62 ?  472 LEU B CA    1 
ATOM   9333  C  C     . LEU B 1 472 ? 124.977 134.937 177.599 1.00 28.12 ?  472 LEU B C     1 
ATOM   9334  O  O     . LEU B 1 472 ? 124.594 134.800 178.766 1.00 35.09 ?  472 LEU B O     1 
ATOM   9335  C  CB    . LEU B 1 472 ? 123.531 136.023 175.855 1.00 23.44 ?  472 LEU B CB    1 
ATOM   9336  C  CG    . LEU B 1 472 ? 122.948 137.287 175.220 1.00 25.83 ?  472 LEU B CG    1 
ATOM   9337  C  CD1   . LEU B 1 472 ? 121.994 136.924 174.095 1.00 24.57 ?  472 LEU B CD1   1 
ATOM   9338  C  CD2   . LEU B 1 472 ? 122.255 138.149 176.261 1.00 22.97 ?  472 LEU B CD2   1 
ATOM   9339  N  N     . ALA B 1 473 ? 125.652 133.980 176.958 1.00 24.54 ?  473 ALA B N     1 
ATOM   9340  C  CA    . ALA B 1 473 ? 125.951 132.712 177.611 1.00 24.14 ?  473 ALA B CA    1 
ATOM   9341  C  C     . ALA B 1 473 ? 126.949 132.883 178.745 1.00 32.15 ?  473 ALA B C     1 
ATOM   9342  O  O     . ALA B 1 473 ? 126.864 132.172 179.753 1.00 39.89 ?  473 ALA B O     1 
ATOM   9343  C  CB    . ALA B 1 473 ? 126.473 131.709 176.585 1.00 25.75 ?  473 ALA B CB    1 
ATOM   9344  N  N     . GLN B 1 474 ? 127.897 133.811 178.609 1.00 31.34 ?  474 GLN B N     1 
ATOM   9345  C  CA    . GLN B 1 474 ? 128.823 134.088 179.697 1.00 29.33 ?  474 GLN B CA    1 
ATOM   9346  C  C     . GLN B 1 474 ? 128.188 134.904 180.815 1.00 29.76 ?  474 GLN B C     1 
ATOM   9347  O  O     . GLN B 1 474 ? 128.819 135.087 181.861 1.00 40.96 ?  474 GLN B O     1 
ATOM   9348  C  CB    . GLN B 1 474 ? 130.060 134.811 179.163 1.00 31.56 ?  474 GLN B CB    1 
ATOM   9349  C  CG    . GLN B 1 474 ? 130.995 133.908 178.380 1.00 29.28 ?  474 GLN B CG    1 
ATOM   9350  C  CD    . GLN B 1 474 ? 132.142 134.664 177.749 1.00 36.08 ?  474 GLN B CD    1 
ATOM   9351  O  OE1   . GLN B 1 474 ? 133.020 135.171 178.444 1.00 42.48 ?  474 GLN B OE1   1 
ATOM   9352  N  NE2   . GLN B 1 474 ? 132.142 134.739 176.424 1.00 36.55 ?  474 GLN B NE2   1 
ATOM   9353  N  N     . ASN B 1 475 ? 126.965 135.396 180.619 1.00 32.74 ?  475 ASN B N     1 
ATOM   9354  C  CA    . ASN B 1 475 ? 126.227 136.108 181.652 1.00 35.35 ?  475 ASN B CA    1 
ATOM   9355  C  C     . ASN B 1 475 ? 125.006 135.332 182.130 1.00 36.04 ?  475 ASN B C     1 
ATOM   9356  O  O     . ASN B 1 475 ? 124.148 135.904 182.810 1.00 38.28 ?  475 ASN B O     1 
ATOM   9357  C  CB    . ASN B 1 475 ? 125.808 137.490 181.148 1.00 34.60 ?  475 ASN B CB    1 
ATOM   9358  C  CG    . ASN B 1 475 ? 126.976 138.444 181.031 1.00 32.50 ?  475 ASN B CG    1 
ATOM   9359  O  OD1   . ASN B 1 475 ? 127.247 139.223 181.943 1.00 39.35 ?  475 ASN B OD1   1 
ATOM   9360  N  ND2   . ASN B 1 475 ? 127.680 138.379 179.909 1.00 28.42 ?  475 ASN B ND2   1 
ATOM   9361  N  N     . GLY B 1 476 ? 124.908 134.051 181.792 1.00 35.89 ?  476 GLY B N     1 
ATOM   9362  C  CA    . GLY B 1 476 ? 123.799 133.224 182.232 1.00 32.40 ?  476 GLY B CA    1 
ATOM   9363  C  C     . GLY B 1 476 ? 122.453 133.607 181.657 1.00 35.20 ?  476 GLY B C     1 
ATOM   9364  O  O     . GLY B 1 476 ? 121.448 133.591 182.381 1.00 42.73 ?  476 GLY B O     1 
ATOM   9365  N  N     . ILE B 1 477 ? 122.404 133.954 180.374 1.00 32.50 ?  477 ILE B N     1 
ATOM   9366  C  CA    . ILE B 1 477 ? 121.162 134.312 179.701 1.00 32.21 ?  477 ILE B CA    1 
ATOM   9367  C  C     . ILE B 1 477 ? 121.016 133.438 178.464 1.00 32.56 ?  477 ILE B C     1 
ATOM   9368  O  O     . ILE B 1 477 ? 121.920 133.389 177.623 1.00 36.67 ?  477 ILE B O     1 
ATOM   9369  C  CB    . ILE B 1 477 ? 121.128 135.805 179.317 1.00 27.66 ?  477 ILE B CB    1 
ATOM   9370  C  CG1   . ILE B 1 477 ? 121.122 136.679 180.571 1.00 30.97 ?  477 ILE B CG1   1 
ATOM   9371  C  CG2   . ILE B 1 477 ? 119.915 136.106 178.462 1.00 26.18 ?  477 ILE B CG2   1 
ATOM   9372  C  CD1   . ILE B 1 477 ? 121.778 138.024 180.380 1.00 33.59 ?  477 ILE B CD1   1 
ATOM   9373  N  N     . ALA B 1 478 ? 119.886 132.745 178.361 1.00 33.33 ?  478 ALA B N     1 
ATOM   9374  C  CA    . ALA B 1 478 ? 119.615 131.933 177.184 1.00 28.73 ?  478 ALA B CA    1 
ATOM   9375  C  C     . ALA B 1 478 ? 119.335 132.825 175.984 1.00 34.04 ?  478 ALA B C     1 
ATOM   9376  O  O     . ALA B 1 478 ? 118.710 133.880 176.109 1.00 38.65 ?  478 ALA B O     1 
ATOM   9377  C  CB    . ALA B 1 478 ? 118.432 131.002 177.439 1.00 29.59 ?  478 ALA B CB    1 
ATOM   9378  N  N     . TYR B 1 479 ? 119.804 132.392 174.811 1.00 29.89 ?  479 TYR B N     1 
ATOM   9379  C  CA    . TYR B 1 479 ? 119.652 133.200 173.605 1.00 21.31 ?  479 TYR B CA    1 
ATOM   9380  C  C     . TYR B 1 479 ? 118.184 133.404 173.251 1.00 33.73 ?  479 TYR B C     1 
ATOM   9381  O  O     . TYR B 1 479 ? 117.791 134.490 172.808 1.00 36.22 ?  479 TYR B O     1 
ATOM   9382  C  CB    . TYR B 1 479 ? 120.404 132.543 172.448 1.00 19.78 ?  479 TYR B CB    1 
ATOM   9383  C  CG    . TYR B 1 479 ? 120.528 133.398 171.209 1.00 26.75 ?  479 TYR B CG    1 
ATOM   9384  C  CD1   . TYR B 1 479 ? 119.565 133.354 170.209 1.00 30.18 ?  479 TYR B CD1   1 
ATOM   9385  C  CD2   . TYR B 1 479 ? 121.616 134.242 171.031 1.00 23.61 ?  479 TYR B CD2   1 
ATOM   9386  C  CE1   . TYR B 1 479 ? 119.678 134.131 169.074 1.00 23.94 ?  479 TYR B CE1   1 
ATOM   9387  C  CE2   . TYR B 1 479 ? 121.739 135.021 169.900 1.00 22.72 ?  479 TYR B CE2   1 
ATOM   9388  C  CZ    . TYR B 1 479 ? 120.767 134.961 168.926 1.00 30.34 ?  479 TYR B CZ    1 
ATOM   9389  O  OH    . TYR B 1 479 ? 120.885 135.736 167.796 1.00 35.04 ?  479 TYR B OH    1 
ATOM   9390  N  N     . GLU B 1 480 ? 117.358 132.374 173.435 1.00 36.31 ?  480 GLU B N     1 
ATOM   9391  C  CA    . GLU B 1 480 ? 115.937 132.477 173.129 1.00 31.16 ?  480 GLU B CA    1 
ATOM   9392  C  C     . GLU B 1 480 ? 115.130 133.112 174.249 1.00 33.32 ?  480 GLU B C     1 
ATOM   9393  O  O     . GLU B 1 480 ? 113.926 133.329 174.074 1.00 38.14 ?  480 GLU B O     1 
ATOM   9394  C  CB    . GLU B 1 480 ? 115.354 131.096 172.829 1.00 34.29 ?  480 GLU B CB    1 
ATOM   9395  C  CG    . GLU B 1 480 ? 116.073 130.317 171.755 1.00 35.17 ?  480 GLU B CG    1 
ATOM   9396  C  CD    . GLU B 1 480 ? 115.983 128.824 171.987 1.00 43.07 ?  480 GLU B CD    1 
ATOM   9397  O  OE1   . GLU B 1 480 ? 116.736 128.312 172.841 1.00 44.45 ?  480 GLU B OE1   1 
ATOM   9398  O  OE2   . GLU B 1 480 ? 115.161 128.163 171.321 1.00 39.62 -1 480 GLU B OE2   1 
ATOM   9399  N  N     . SER B 1 481 ? 115.749 133.404 175.387 1.00 31.50 ?  481 SER B N     1 
ATOM   9400  C  CA    . SER B 1 481 ? 115.010 133.936 176.517 1.00 32.57 ?  481 SER B CA    1 
ATOM   9401  C  C     . SER B 1 481 ? 114.527 135.356 176.224 1.00 36.64 ?  481 SER B C     1 
ATOM   9402  O  O     . SER B 1 481 ? 115.144 136.082 175.440 1.00 38.79 ?  481 SER B O     1 
ATOM   9403  C  CB    . SER B 1 481 ? 115.879 133.930 177.770 1.00 30.75 ?  481 SER B CB    1 
ATOM   9404  O  OG    . SER B 1 481 ? 116.727 135.063 177.806 1.00 35.20 ?  481 SER B OG    1 
ATOM   9405  N  N     . PRO B 1 482 ? 113.409 135.767 176.827 1.00 42.31 ?  482 PRO B N     1 
ATOM   9406  C  CA    . PRO B 1 482 ? 112.981 137.167 176.686 1.00 37.58 ?  482 PRO B CA    1 
ATOM   9407  C  C     . PRO B 1 482 ? 113.989 138.157 177.235 1.00 32.77 ?  482 PRO B C     1 
ATOM   9408  O  O     . PRO B 1 482 ? 114.033 139.303 176.772 1.00 36.90 ?  482 PRO B O     1 
ATOM   9409  C  CB    . PRO B 1 482 ? 111.660 137.207 177.467 1.00 35.59 ?  482 PRO B CB    1 
ATOM   9410  C  CG    . PRO B 1 482 ? 111.185 135.797 177.481 1.00 37.34 ?  482 PRO B CG    1 
ATOM   9411  C  CD    . PRO B 1 482 ? 112.421 134.957 177.556 1.00 37.93 ?  482 PRO B CD    1 
ATOM   9412  N  N     . GLU B 1 483 ? 114.799 137.751 178.215 1.00 35.62 ?  483 GLU B N     1 
ATOM   9413  C  CA    . GLU B 1 483 ? 115.830 138.639 178.743 1.00 32.90 ?  483 GLU B CA    1 
ATOM   9414  C  C     . GLU B 1 483 ? 116.914 138.905 177.707 1.00 30.00 ?  483 GLU B C     1 
ATOM   9415  O  O     . GLU B 1 483 ? 117.469 140.008 177.650 1.00 36.41 ?  483 GLU B O     1 
ATOM   9416  C  CB    . GLU B 1 483 ? 116.432 138.042 180.015 1.00 37.13 ?  483 GLU B CB    1 
ATOM   9417  C  CG    . GLU B 1 483 ? 115.452 137.931 181.169 1.00 39.21 ?  483 GLU B CG    1 
ATOM   9418  C  CD    . GLU B 1 483 ? 114.784 136.572 181.238 1.00 45.79 ?  483 GLU B CD    1 
ATOM   9419  O  OE1   . GLU B 1 483 ? 114.896 135.805 180.261 1.00 42.62 ?  483 GLU B OE1   1 
ATOM   9420  O  OE2   . GLU B 1 483 ? 114.143 136.273 182.267 1.00 44.24 -1 483 GLU B OE2   1 
ATOM   9421  N  N     . ALA B 1 484 ? 117.235 137.905 176.884 1.00 28.45 ?  484 ALA B N     1 
ATOM   9422  C  CA    . ALA B 1 484 ? 118.198 138.118 175.808 1.00 29.24 ?  484 ALA B CA    1 
ATOM   9423  C  C     . ALA B 1 484 ? 117.685 139.142 174.805 1.00 29.55 ?  484 ALA B C     1 
ATOM   9424  O  O     . ALA B 1 484 ? 118.434 140.022 174.367 1.00 31.34 ?  484 ALA B O     1 
ATOM   9425  C  CB    . ALA B 1 484 ? 118.506 136.797 175.112 1.00 21.96 ?  484 ALA B CB    1 
ATOM   9426  N  N     . ARG B 1 485 ? 116.408 139.044 174.434 1.00 26.43 ?  485 ARG B N     1 
ATOM   9427  C  CA    . ARG B 1 485 ? 115.826 140.037 173.540 1.00 26.24 ?  485 ARG B CA    1 
ATOM   9428  C  C     . ARG B 1 485 ? 115.751 141.404 174.201 1.00 24.75 ?  485 ARG B C     1 
ATOM   9429  O  O     . ARG B 1 485 ? 115.909 142.423 173.524 1.00 35.19 ?  485 ARG B O     1 
ATOM   9430  C  CB    . ARG B 1 485 ? 114.442 139.586 173.079 1.00 28.25 ?  485 ARG B CB    1 
ATOM   9431  C  CG    . ARG B 1 485 ? 114.475 138.493 172.033 1.00 26.08 ?  485 ARG B CG    1 
ATOM   9432  C  CD    . ARG B 1 485 ? 113.104 138.270 171.424 1.00 25.72 ?  485 ARG B CD    1 
ATOM   9433  N  NE    . ARG B 1 485 ? 112.135 137.802 172.407 1.00 29.58 ?  485 ARG B NE    1 
ATOM   9434  C  CZ    . ARG B 1 485 ? 112.046 136.549 172.833 1.00 33.69 ?  485 ARG B CZ    1 
ATOM   9435  N  NH1   . ARG B 1 485 ? 112.852 135.604 172.378 1.00 35.12 1  485 ARG B NH1   1 
ATOM   9436  N  NH2   . ARG B 1 485 ? 111.122 136.236 173.737 1.00 29.72 ?  485 ARG B NH2   1 
ATOM   9437  N  N     . ASP B 1 486 ? 115.516 141.448 175.512 1.00 30.77 ?  486 ASP B N     1 
ATOM   9438  C  CA    . ASP B 1 486 ? 115.525 142.719 176.230 1.00 30.72 ?  486 ASP B CA    1 
ATOM   9439  C  C     . ASP B 1 486 ? 116.902 143.370 176.172 1.00 30.06 ?  486 ASP B C     1 
ATOM   9440  O  O     . ASP B 1 486 ? 117.028 144.577 175.909 1.00 32.61 ?  486 ASP B O     1 
ATOM   9441  C  CB    . ASP B 1 486 ? 115.086 142.485 177.675 1.00 34.22 ?  486 ASP B CB    1 
ATOM   9442  C  CG    . ASP B 1 486 ? 114.819 143.770 178.419 1.00 43.15 ?  486 ASP B CG    1 
ATOM   9443  O  OD1   . ASP B 1 486 ? 114.120 144.646 177.869 1.00 45.20 ?  486 ASP B OD1   1 
ATOM   9444  O  OD2   . ASP B 1 486 ? 115.303 143.897 179.561 1.00 34.53 -1 486 ASP B OD2   1 
ATOM   9445  N  N     . PHE B 1 487 ? 117.953 142.579 176.404 1.00 26.92 ?  487 PHE B N     1 
ATOM   9446  C  CA    . PHE B 1 487 ? 119.304 143.113 176.300 1.00 23.40 ?  487 PHE B CA    1 
ATOM   9447  C  C     . PHE B 1 487 ? 119.608 143.572 174.884 1.00 28.27 ?  487 PHE B C     1 
ATOM   9448  O  O     . PHE B 1 487 ? 120.230 144.618 174.689 1.00 30.97 ?  487 PHE B O     1 
ATOM   9449  C  CB    . PHE B 1 487 ? 120.351 142.091 176.732 1.00 24.72 ?  487 PHE B CB    1 
ATOM   9450  C  CG    . PHE B 1 487 ? 121.732 142.444 176.266 1.00 28.11 ?  487 PHE B CG    1 
ATOM   9451  C  CD1   . PHE B 1 487 ? 122.446 143.447 176.898 1.00 21.12 ?  487 PHE B CD1   1 
ATOM   9452  C  CD2   . PHE B 1 487 ? 122.297 141.818 175.168 1.00 27.86 ?  487 PHE B CD2   1 
ATOM   9453  C  CE1   . PHE B 1 487 ? 123.703 143.801 176.462 1.00 23.42 ?  487 PHE B CE1   1 
ATOM   9454  C  CE2   . PHE B 1 487 ? 123.555 142.172 174.730 1.00 26.23 ?  487 PHE B CE2   1 
ATOM   9455  C  CZ    . PHE B 1 487 ? 124.257 143.166 175.377 1.00 25.18 ?  487 PHE B CZ    1 
ATOM   9456  N  N     . ALA B 1 488 ? 119.220 142.780 173.882 1.00 26.01 ?  488 ALA B N     1 
ATOM   9457  C  CA    . ALA B 1 488 ? 119.474 143.177 172.502 1.00 20.12 ?  488 ALA B CA    1 
ATOM   9458  C  C     . ALA B 1 488 ? 118.765 144.482 172.176 1.00 29.34 ?  488 ALA B C     1 
ATOM   9459  O  O     . ALA B 1 488 ? 119.351 145.383 171.566 1.00 38.20 ?  488 ALA B O     1 
ATOM   9460  C  CB    . ALA B 1 488 ? 119.035 142.071 171.546 1.00 21.50 ?  488 ALA B CB    1 
ATOM   9461  N  N     . ASN B 1 489 ? 117.508 144.607 172.603 1.00 28.70 ?  489 ASN B N     1 
ATOM   9462  C  CA    . ASN B 1 489 ? 116.753 145.836 172.406 1.00 26.11 ?  489 ASN B CA    1 
ATOM   9463  C  C     . ASN B 1 489 ? 117.490 147.031 172.991 1.00 20.40 ?  489 ASN B C     1 
ATOM   9464  O  O     . ASN B 1 489 ? 117.755 148.015 172.292 1.00 29.68 ?  489 ASN B O     1 
ATOM   9465  C  CB    . ASN B 1 489 ? 115.372 145.687 173.045 1.00 21.16 ?  489 ASN B CB    1 
ATOM   9466  C  CG    . ASN B 1 489 ? 114.354 146.645 172.479 1.00 32.36 ?  489 ASN B CG    1 
ATOM   9467  O  OD1   . ASN B 1 489 ? 114.104 146.667 171.275 1.00 39.21 ?  489 ASN B OD1   1 
ATOM   9468  N  ND2   . ASN B 1 489 ? 113.746 147.438 173.350 1.00 31.79 ?  489 ASN B ND2   1 
ATOM   9469  N  N     . THR B 1 490 ? 117.869 146.946 174.269 1.00 22.72 ?  490 THR B N     1 
ATOM   9470  C  CA    . THR B 1 490 ? 118.511 148.086 174.918 1.00 22.67 ?  490 THR B CA    1 
ATOM   9471  C  C     . THR B 1 490 ? 119.874 148.387 174.302 1.00 24.87 ?  490 THR B C     1 
ATOM   9472  O  O     . THR B 1 490 ? 120.189 149.545 173.999 1.00 21.06 ?  490 THR B O     1 
ATOM   9473  C  CB    . THR B 1 490 ? 118.646 147.831 176.418 1.00 33.48 ?  490 THR B CB    1 
ATOM   9474  O  OG1   . THR B 1 490 ? 117.377 147.436 176.949 1.00 39.12 ?  490 THR B OG1   1 
ATOM   9475  C  CG2   . THR B 1 490 ? 119.120 149.089 177.129 1.00 27.80 ?  490 THR B CG2   1 
ATOM   9476  N  N     . PHE B 1 491 ? 120.688 147.350 174.095 1.00 25.08 ?  491 PHE B N     1 
ATOM   9477  C  CA    . PHE B 1 491 ? 122.044 147.536 173.592 1.00 19.01 ?  491 PHE B CA    1 
ATOM   9478  C  C     . PHE B 1 491 ? 122.035 148.153 172.204 1.00 25.49 ?  491 PHE B C     1 
ATOM   9479  O  O     . PHE B 1 491 ? 122.782 149.098 171.927 1.00 33.73 ?  491 PHE B O     1 
ATOM   9480  C  CB    . PHE B 1 491 ? 122.779 146.195 173.580 1.00 23.13 ?  491 PHE B CB    1 
ATOM   9481  C  CG    . PHE B 1 491 ? 124.176 146.268 173.027 1.00 25.07 ?  491 PHE B CG    1 
ATOM   9482  C  CD1   . PHE B 1 491 ? 125.249 146.536 173.857 1.00 23.22 ?  491 PHE B CD1   1 
ATOM   9483  C  CD2   . PHE B 1 491 ? 124.418 146.058 171.679 1.00 20.50 ?  491 PHE B CD2   1 
ATOM   9484  C  CE1   . PHE B 1 491 ? 126.532 146.604 173.356 1.00 14.85 ?  491 PHE B CE1   1 
ATOM   9485  C  CE2   . PHE B 1 491 ? 125.697 146.127 171.172 1.00 15.76 ?  491 PHE B CE2   1 
ATOM   9486  C  CZ    . PHE B 1 491 ? 126.756 146.400 172.013 1.00 19.74 ?  491 PHE B CZ    1 
ATOM   9487  N  N     . PHE B 1 492 ? 121.197 147.633 171.308 1.00 20.89 ?  492 PHE B N     1 
ATOM   9488  C  CA    . PHE B 1 492 ? 121.190 148.162 169.957 1.00 12.88 ?  492 PHE B CA    1 
ATOM   9489  C  C     . PHE B 1 492 ? 120.451 149.487 169.853 1.00 10.87 ?  492 PHE B C     1 
ATOM   9490  O  O     . PHE B 1 492 ? 120.774 150.280 168.966 1.00 24.78 ?  492 PHE B O     1 
ATOM   9491  C  CB    . PHE B 1 492 ? 120.621 147.120 168.998 1.00 14.12 ?  492 PHE B CB    1 
ATOM   9492  C  CG    . PHE B 1 492 ? 121.578 146.000 168.717 1.00 16.24 ?  492 PHE B CG    1 
ATOM   9493  C  CD1   . PHE B 1 492 ? 122.617 146.172 167.821 1.00 10.13 ?  492 PHE B CD1   1 
ATOM   9494  C  CD2   . PHE B 1 492 ? 121.467 144.791 169.381 1.00 18.24 ?  492 PHE B CD2   1 
ATOM   9495  C  CE1   . PHE B 1 492 ? 123.509 145.152 167.573 1.00 8.63  ?  492 PHE B CE1   1 
ATOM   9496  C  CE2   . PHE B 1 492 ? 122.358 143.768 169.136 1.00 12.97 ?  492 PHE B CE2   1 
ATOM   9497  C  CZ    . PHE B 1 492 ? 123.379 143.948 168.231 1.00 15.74 ?  492 PHE B CZ    1 
ATOM   9498  N  N     . MET B 1 493 ? 119.516 149.779 170.763 1.00 14.89 ?  493 MET B N     1 
ATOM   9499  C  CA    . MET B 1 493 ? 119.001 151.140 170.844 1.00 17.34 ?  493 MET B CA    1 
ATOM   9500  C  C     . MET B 1 493 ? 120.111 152.113 171.211 1.00 22.68 ?  493 MET B C     1 
ATOM   9501  O  O     . MET B 1 493 ? 120.214 153.196 170.627 1.00 29.67 ?  493 MET B O     1 
ATOM   9502  C  CB    . MET B 1 493 ? 117.874 151.232 171.869 1.00 19.23 ?  493 MET B CB    1 
ATOM   9503  C  CG    . MET B 1 493 ? 117.304 152.636 172.007 1.00 18.99 ?  493 MET B CG    1 
ATOM   9504  S  SD    . MET B 1 493 ? 117.901 153.532 173.453 1.00 37.89 ?  493 MET B SD    1 
ATOM   9505  C  CE    . MET B 1 493 ? 117.848 152.257 174.704 1.00 27.76 ?  493 MET B CE    1 
ATOM   9506  N  N     . MET B 1 494 ? 120.952 151.744 172.182 1.00 22.12 ?  494 MET B N     1 
ATOM   9507  C  CA    . MET B 1 494 ? 122.070 152.607 172.557 1.00 17.02 ?  494 MET B CA    1 
ATOM   9508  C  C     . MET B 1 494 ? 123.060 152.759 171.408 1.00 18.65 ?  494 MET B C     1 
ATOM   9509  O  O     . MET B 1 494 ? 123.579 153.857 171.166 1.00 31.25 ?  494 MET B O     1 
ATOM   9510  C  CB    . MET B 1 494 ? 122.773 152.055 173.796 1.00 23.61 ?  494 MET B CB    1 
ATOM   9511  C  CG    . MET B 1 494 ? 121.886 151.926 175.018 1.00 22.05 ?  494 MET B CG    1 
ATOM   9512  S  SD    . MET B 1 494 ? 122.815 151.547 176.512 1.00 42.56 ?  494 MET B SD    1 
ATOM   9513  C  CE    . MET B 1 494 ? 124.091 152.798 176.438 1.00 31.53 ?  494 MET B CE    1 
ATOM   9514  N  N     . VAL B 1 495 ? 123.343 151.663 170.702 1.00 19.82 ?  495 VAL B N     1 
ATOM   9515  C  CA    . VAL B 1 495 ? 124.258 151.721 169.566 1.00 13.54 ?  495 VAL B CA    1 
ATOM   9516  C  C     . VAL B 1 495 ? 123.711 152.647 168.490 1.00 18.91 ?  495 VAL B C     1 
ATOM   9517  O  O     . VAL B 1 495 ? 124.439 153.479 167.939 1.00 31.74 ?  495 VAL B O     1 
ATOM   9518  C  CB    . VAL B 1 495 ? 124.519 150.306 169.018 1.00 15.39 ?  495 VAL B CB    1 
ATOM   9519  C  CG1   . VAL B 1 495 ? 125.180 150.374 167.652 1.00 13.43 ?  495 VAL B CG1   1 
ATOM   9520  C  CG2   . VAL B 1 495 ? 125.375 149.515 169.988 1.00 14.04 ?  495 VAL B CG2   1 
ATOM   9521  N  N     . ASN B 1 496 ? 122.417 152.525 168.180 1.00 25.04 ?  496 ASN B N     1 
ATOM   9522  C  CA    . ASN B 1 496 ? 121.799 153.411 167.200 1.00 14.39 ?  496 ASN B CA    1 
ATOM   9523  C  C     . ASN B 1 496 ? 121.834 154.858 167.664 1.00 17.48 ?  496 ASN B C     1 
ATOM   9524  O  O     . ASN B 1 496 ? 122.122 155.764 166.875 1.00 27.82 ?  496 ASN B O     1 
ATOM   9525  C  CB    . ASN B 1 496 ? 120.360 152.967 166.934 1.00 13.17 ?  496 ASN B CB    1 
ATOM   9526  C  CG    . ASN B 1 496 ? 119.811 153.517 165.638 1.00 14.73 ?  496 ASN B CG    1 
ATOM   9527  O  OD1   . ASN B 1 496 ? 120.513 153.580 164.632 1.00 25.58 ?  496 ASN B OD1   1 
ATOM   9528  N  ND2   . ASN B 1 496 ? 118.547 153.913 165.655 1.00 17.11 ?  496 ASN B ND2   1 
ATOM   9529  N  N     . PHE B 1 497 ? 121.545 155.094 168.945 1.00 18.74 ?  497 PHE B N     1 
ATOM   9530  C  CA    . PHE B 1 497 ? 121.557 156.449 169.483 1.00 12.68 ?  497 PHE B CA    1 
ATOM   9531  C  C     . PHE B 1 497 ? 122.924 157.089 169.314 1.00 24.73 ?  497 PHE B C     1 
ATOM   9532  O  O     . PHE B 1 497 ? 123.041 158.213 168.814 1.00 30.72 ?  497 PHE B O     1 
ATOM   9533  C  CB    . PHE B 1 497 ? 121.159 156.420 170.960 1.00 15.59 ?  497 PHE B CB    1 
ATOM   9534  C  CG    . PHE B 1 497 ? 121.096 157.775 171.602 1.00 19.96 ?  497 PHE B CG    1 
ATOM   9535  C  CD1   . PHE B 1 497 ? 119.935 158.525 171.554 1.00 29.44 ?  497 PHE B CD1   1 
ATOM   9536  C  CD2   . PHE B 1 497 ? 122.195 158.294 172.266 1.00 22.87 ?  497 PHE B CD2   1 
ATOM   9537  C  CE1   . PHE B 1 497 ? 119.875 159.768 172.146 1.00 27.07 ?  497 PHE B CE1   1 
ATOM   9538  C  CE2   . PHE B 1 497 ? 122.139 159.537 172.859 1.00 25.28 ?  497 PHE B CE2   1 
ATOM   9539  C  CZ    . PHE B 1 497 ? 120.978 160.274 172.799 1.00 28.44 ?  497 PHE B CZ    1 
ATOM   9540  N  N     . TYR B 1 498 ? 123.976 156.374 169.706 1.00 28.15 ?  498 TYR B N     1 
ATOM   9541  C  CA    . TYR B 1 498 ? 125.304 156.967 169.663 1.00 19.30 ?  498 TYR B CA    1 
ATOM   9542  C  C     . TYR B 1 498 ? 125.859 157.027 168.248 1.00 24.34 ?  498 TYR B C     1 
ATOM   9543  O  O     . TYR B 1 498 ? 126.635 157.935 167.940 1.00 35.03 ?  498 TYR B O     1 
ATOM   9544  C  CB    . TYR B 1 498 ? 126.238 156.214 170.608 1.00 20.21 ?  498 TYR B CB    1 
ATOM   9545  C  CG    . TYR B 1 498 ? 125.904 156.504 172.051 1.00 26.02 ?  498 TYR B CG    1 
ATOM   9546  C  CD1   . TYR B 1 498 ? 125.907 157.807 172.528 1.00 29.24 ?  498 TYR B CD1   1 
ATOM   9547  C  CD2   . TYR B 1 498 ? 125.549 155.486 172.923 1.00 25.53 ?  498 TYR B CD2   1 
ATOM   9548  C  CE1   . TYR B 1 498 ? 125.586 158.086 173.839 1.00 29.00 ?  498 TYR B CE1   1 
ATOM   9549  C  CE2   . TYR B 1 498 ? 125.226 155.757 174.237 1.00 26.42 ?  498 TYR B CE2   1 
ATOM   9550  C  CZ    . TYR B 1 498 ? 125.248 157.060 174.690 1.00 33.24 ?  498 TYR B CZ    1 
ATOM   9551  O  OH    . TYR B 1 498 ? 124.929 157.339 175.998 1.00 37.24 ?  498 TYR B OH    1 
ATOM   9552  N  N     . SER B 1 499 ? 125.440 156.124 167.358 1.00 18.28 ?  499 SER B N     1 
ATOM   9553  C  CA    . SER B 1 499 ? 125.850 156.244 165.963 1.00 10.43 ?  499 SER B CA    1 
ATOM   9554  C  C     . SER B 1 499 ? 125.180 157.439 165.295 1.00 18.82 ?  499 SER B C     1 
ATOM   9555  O  O     . SER B 1 499 ? 125.824 158.173 164.538 1.00 27.20 ?  499 SER B O     1 
ATOM   9556  C  CB    . SER B 1 499 ? 125.540 154.952 165.207 1.00 8.27  ?  499 SER B CB    1 
ATOM   9557  O  OG    . SER B 1 499 ? 124.160 154.843 164.919 1.00 24.13 ?  499 SER B OG    1 
ATOM   9558  N  N     . ILE B 1 500 ? 123.894 157.666 165.578 1.00 16.69 ?  500 ILE B N     1 
ATOM   9559  C  CA    . ILE B 1 500 ? 123.216 158.853 165.063 1.00 20.33 ?  500 ILE B CA    1 
ATOM   9560  C  C     . ILE B 1 500 ? 123.853 160.113 165.628 1.00 21.42 ?  500 ILE B C     1 
ATOM   9561  O  O     . ILE B 1 500 ? 124.053 161.102 164.912 1.00 26.70 ?  500 ILE B O     1 
ATOM   9562  C  CB    . ILE B 1 500 ? 121.710 158.798 165.381 1.00 24.31 ?  500 ILE B CB    1 
ATOM   9563  C  CG1   . ILE B 1 500 ? 121.033 157.666 164.619 1.00 21.83 ?  500 ILE B CG1   1 
ATOM   9564  C  CG2   . ILE B 1 500 ? 121.043 160.114 165.029 1.00 19.07 ?  500 ILE B CG2   1 
ATOM   9565  C  CD1   . ILE B 1 500 ? 119.671 157.329 165.153 1.00 18.71 ?  500 ILE B CD1   1 
ATOM   9566  N  N     . GLN B 1 501 ? 124.169 160.103 166.925 1.00 29.10 ?  501 GLN B N     1 
ATOM   9567  C  CA    . GLN B 1 501 ? 124.793 161.266 167.543 1.00 25.39 ?  501 GLN B CA    1 
ATOM   9568  C  C     . GLN B 1 501 ? 126.157 161.556 166.933 1.00 26.73 ?  501 GLN B C     1 
ATOM   9569  O  O     . GLN B 1 501 ? 126.478 162.710 166.641 1.00 39.62 ?  501 GLN B O     1 
ATOM   9570  C  CB    . GLN B 1 501 ? 124.914 161.057 169.051 1.00 30.32 ?  501 GLN B CB    1 
ATOM   9571  C  CG    . GLN B 1 501 ? 124.811 162.336 169.853 1.00 29.00 ?  501 GLN B CG    1 
ATOM   9572  C  CD    . GLN B 1 501 ? 124.939 162.098 171.339 1.00 33.80 ?  501 GLN B CD    1 
ATOM   9573  O  OE1   . GLN B 1 501 ? 125.929 161.538 171.805 1.00 39.72 ?  501 GLN B OE1   1 
ATOM   9574  N  NE2   . GLN B 1 501 ? 123.934 162.523 172.095 1.00 34.98 ?  501 GLN B NE2   1 
ATOM   9575  N  N     . ARG B 1 502 ? 126.969 160.519 166.719 1.00 31.15 ?  502 ARG B N     1 
ATOM   9576  C  CA    . ARG B 1 502 ? 128.278 160.724 166.110 1.00 23.02 ?  502 ARG B CA    1 
ATOM   9577  C  C     . ARG B 1 502 ? 128.153 161.193 164.668 1.00 22.55 ?  502 ARG B C     1 
ATOM   9578  O  O     . ARG B 1 502 ? 128.938 162.030 164.217 1.00 30.10 ?  502 ARG B O     1 
ATOM   9579  C  CB    . ARG B 1 502 ? 129.106 159.443 166.186 1.00 20.77 ?  502 ARG B CB    1 
ATOM   9580  C  CG    . ARG B 1 502 ? 130.572 159.652 165.856 1.00 25.50 ?  502 ARG B CG    1 
ATOM   9581  C  CD    . ARG B 1 502 ? 131.164 160.773 166.689 1.00 28.07 ?  502 ARG B CD    1 
ATOM   9582  N  NE    . ARG B 1 502 ? 132.472 161.185 166.199 1.00 28.04 ?  502 ARG B NE    1 
ATOM   9583  C  CZ    . ARG B 1 502 ? 132.913 162.435 166.200 1.00 27.28 ?  502 ARG B CZ    1 
ATOM   9584  N  NH1   . ARG B 1 502 ? 132.171 163.428 166.660 1.00 32.98 1  502 ARG B NH1   1 
ATOM   9585  N  NH2   . ARG B 1 502 ? 134.127 162.694 165.727 1.00 29.36 ?  502 ARG B NH2   1 
ATOM   9586  N  N     . SER B 1 503 ? 127.181 160.662 163.927 1.00 23.22 ?  503 SER B N     1 
ATOM   9587  C  CA    . SER B 1 503 ? 126.982 161.101 162.550 1.00 22.24 ?  503 SER B CA    1 
ATOM   9588  C  C     . SER B 1 503 ? 126.568 162.566 162.492 1.00 26.36 ?  503 SER B C     1 
ATOM   9589  O  O     . SER B 1 503 ? 127.068 163.329 161.660 1.00 33.93 ?  503 SER B O     1 
ATOM   9590  C  CB    . SER B 1 503 ? 125.940 160.213 161.875 1.00 16.91 ?  503 SER B CB    1 
ATOM   9591  O  OG    . SER B 1 503 ? 126.093 160.214 160.469 1.00 25.82 ?  503 SER B OG    1 
ATOM   9592  N  N     . ALA B 1 504 ? 125.665 162.981 163.382 1.00 25.08 ?  504 ALA B N     1 
ATOM   9593  C  CA    . ALA B 1 504 ? 125.270 164.384 163.430 1.00 22.29 ?  504 ALA B CA    1 
ATOM   9594  C  C     . ALA B 1 504 ? 126.425 165.270 163.881 1.00 31.28 ?  504 ALA B C     1 
ATOM   9595  O  O     . ALA B 1 504 ? 126.572 166.398 163.401 1.00 38.19 ?  504 ALA B O     1 
ATOM   9596  C  CB    . ALA B 1 504 ? 124.063 164.557 164.350 1.00 22.33 ?  504 ALA B CB    1 
ATOM   9597  N  N     . GLU B 1 505 ? 127.259 164.777 164.800 1.00 29.93 ?  505 GLU B N     1 
ATOM   9598  C  CA    . GLU B 1 505 ? 128.435 165.531 165.221 1.00 26.45 ?  505 GLU B CA    1 
ATOM   9599  C  C     . GLU B 1 505 ? 129.423 165.704 164.074 1.00 34.37 ?  505 GLU B C     1 
ATOM   9600  O  O     . GLU B 1 505 ? 130.007 166.780 163.910 1.00 39.07 ?  505 GLU B O     1 
ATOM   9601  C  CB    . GLU B 1 505 ? 129.105 164.833 166.404 1.00 26.96 ?  505 GLU B CB    1 
ATOM   9602  C  CG    . GLU B 1 505 ? 128.402 165.045 167.731 1.00 31.27 ?  505 GLU B CG    1 
ATOM   9603  C  CD    . GLU B 1 505 ? 128.770 163.993 168.758 1.00 37.60 ?  505 GLU B CD    1 
ATOM   9604  O  OE1   . GLU B 1 505 ? 129.649 163.156 168.467 1.00 39.01 ?  505 GLU B OE1   1 
ATOM   9605  O  OE2   . GLU B 1 505 ? 128.180 164.004 169.859 1.00 41.19 -1 505 GLU B OE2   1 
ATOM   9606  N  N     . ILE B 1 506 ? 129.629 164.654 163.278 1.00 32.03 ?  506 ILE B N     1 
ATOM   9607  C  CA    . ILE B 1 506 ? 130.505 164.757 162.115 1.00 26.15 ?  506 ILE B CA    1 
ATOM   9608  C  C     . ILE B 1 506 ? 129.923 165.725 161.095 1.00 26.57 ?  506 ILE B C     1 
ATOM   9609  O  O     . ILE B 1 506 ? 130.652 166.508 160.476 1.00 37.47 ?  506 ILE B O     1 
ATOM   9610  C  CB    . ILE B 1 506 ? 130.750 163.364 161.506 1.00 27.51 ?  506 ILE B CB    1 
ATOM   9611  C  CG1   . ILE B 1 506 ? 131.526 162.481 162.484 1.00 32.53 ?  506 ILE B CG1   1 
ATOM   9612  C  CG2   . ILE B 1 506 ? 131.502 163.473 160.190 1.00 24.74 ?  506 ILE B CG2   1 
ATOM   9613  C  CD1   . ILE B 1 506 ? 131.538 161.017 162.108 1.00 24.63 ?  506 ILE B CD1   1 
ATOM   9614  N  N     . ALA B 1 507 ? 128.603 165.689 160.902 1.00 29.52 ?  507 ALA B N     1 
ATOM   9615  C  CA    . ALA B 1 507 ? 127.964 166.634 159.991 1.00 29.58 ?  507 ALA B CA    1 
ATOM   9616  C  C     . ALA B 1 507 ? 128.144 168.069 160.469 1.00 31.40 ?  507 ALA B C     1 
ATOM   9617  O  O     . ALA B 1 507 ? 128.396 168.972 159.666 1.00 37.98 ?  507 ALA B O     1 
ATOM   9618  C  CB    . ALA B 1 507 ? 126.481 166.299 159.845 1.00 26.16 ?  507 ALA B CB    1 
ATOM   9619  N  N     . LYS B 1 508 ? 128.012 168.298 161.777 1.00 35.98 ?  508 LYS B N     1 
ATOM   9620  C  CA    . LYS B 1 508 ? 128.232 169.629 162.331 1.00 36.46 ?  508 LYS B CA    1 
ATOM   9621  C  C     . LYS B 1 508 ? 129.684 170.067 162.171 1.00 39.38 ?  508 LYS B C     1 
ATOM   9622  O  O     . LYS B 1 508 ? 129.957 171.227 161.847 1.00 43.84 ?  508 LYS B O     1 
ATOM   9623  C  CB    . LYS B 1 508 ? 127.822 169.652 163.803 1.00 41.04 ?  508 LYS B CB    1 
ATOM   9624  C  CG    . LYS B 1 508 ? 128.071 170.972 164.505 1.00 38.72 ?  508 LYS B CG    1 
ATOM   9625  C  CD    . LYS B 1 508 ? 127.870 170.840 166.003 1.00 39.11 ?  508 LYS B CD    1 
ATOM   9626  C  CE    . LYS B 1 508 ? 127.958 172.190 166.693 1.00 41.74 ?  508 LYS B CE    1 
ATOM   9627  N  NZ    . LYS B 1 508 ? 127.111 172.244 167.916 1.00 46.13 1  508 LYS B NZ    1 
ATOM   9628  N  N     . GLU B 1 509 ? 130.629 169.152 162.402 1.00 42.09 ?  509 GLU B N     1 
ATOM   9629  C  CA    . GLU B 1 509 ? 132.043 169.495 162.296 1.00 40.27 ?  509 GLU B CA    1 
ATOM   9630  C  C     . GLU B 1 509 ? 132.429 169.828 160.861 1.00 42.88 ?  509 GLU B C     1 
ATOM   9631  O  O     . GLU B 1 509 ? 133.133 170.814 160.615 1.00 49.18 ?  509 GLU B O     1 
ATOM   9632  C  CB    . GLU B 1 509 ? 132.899 168.346 162.826 1.00 37.70 ?  509 GLU B CB    1 
ATOM   9633  C  CG    . GLU B 1 509 ? 133.182 168.412 164.317 1.00 46.70 ?  509 GLU B CG    1 
ATOM   9634  C  CD    . GLU B 1 509 ? 133.393 167.041 164.933 1.00 50.17 ?  509 GLU B CD    1 
ATOM   9635  O  OE1   . GLU B 1 509 ? 133.958 166.161 164.250 1.00 48.52 ?  509 GLU B OE1   1 
ATOM   9636  O  OE2   . GLU B 1 509 ? 132.993 166.843 166.100 1.00 45.41 -1 509 GLU B OE2   1 
ATOM   9637  N  N     . LYS B 1 510 ? 131.983 169.019 159.904 1.00 38.56 ?  510 LYS B N     1 
ATOM   9638  C  CA    . LYS B 1 510 ? 132.300 169.235 158.501 1.00 32.84 ?  510 LYS B CA    1 
ATOM   9639  C  C     . LYS B 1 510 ? 131.325 170.174 157.806 1.00 38.42 ?  510 LYS B C     1 
ATOM   9640  O  O     . LYS B 1 510 ? 131.578 170.565 156.662 1.00 46.93 ?  510 LYS B O     1 
ATOM   9641  C  CB    . LYS B 1 510 ? 132.333 167.896 157.757 1.00 29.42 ?  510 LYS B CB    1 
ATOM   9642  C  CG    . LYS B 1 510 ? 133.240 166.860 158.391 1.00 32.23 ?  510 LYS B CG    1 
ATOM   9643  C  CD    . LYS B 1 510 ? 133.411 165.653 157.488 1.00 35.69 ?  510 LYS B CD    1 
ATOM   9644  C  CE    . LYS B 1 510 ? 134.349 164.629 158.104 1.00 39.38 ?  510 LYS B CE    1 
ATOM   9645  N  NZ    . LYS B 1 510 ? 135.050 163.824 157.070 1.00 41.14 1  510 LYS B NZ    1 
ATOM   9646  N  N     . GLY B 1 511 ? 130.228 170.544 158.462 1.00 36.32 ?  511 GLY B N     1 
ATOM   9647  C  CA    . GLY B 1 511 ? 129.243 171.410 157.848 1.00 37.95 ?  511 GLY B CA    1 
ATOM   9648  C  C     . GLY B 1 511 ? 128.503 170.808 156.678 1.00 40.49 ?  511 GLY B C     1 
ATOM   9649  O  O     . GLY B 1 511 ? 127.833 171.541 155.945 1.00 43.77 ?  511 GLY B O     1 
ATOM   9650  N  N     . GLU B 1 512 ? 128.599 169.496 156.479 1.00 34.43 ?  512 GLU B N     1 
ATOM   9651  C  CA    . GLU B 1 512 ? 127.977 168.836 155.342 1.00 30.22 ?  512 GLU B CA    1 
ATOM   9652  C  C     . GLU B 1 512 ? 127.282 167.564 155.798 1.00 31.48 ?  512 GLU B C     1 
ATOM   9653  O  O     . GLU B 1 512 ? 127.766 166.867 156.692 1.00 36.31 ?  512 GLU B O     1 
ATOM   9654  C  CB    . GLU B 1 512 ? 129.009 168.502 154.260 1.00 33.01 ?  512 GLU B CB    1 
ATOM   9655  C  CG    . GLU B 1 512 ? 130.236 167.781 154.786 1.00 32.71 ?  512 GLU B CG    1 
ATOM   9656  C  CD    . GLU B 1 512 ? 131.032 167.108 153.688 1.00 38.28 ?  512 GLU B CD    1 
ATOM   9657  O  OE1   . GLU B 1 512 ? 130.448 166.815 152.624 1.00 37.92 ?  512 GLU B OE1   1 
ATOM   9658  O  OE2   . GLU B 1 512 ? 132.241 166.869 153.890 1.00 39.66 -1 512 GLU B OE2   1 
ATOM   9659  N  N     . THR B 1 513 ? 126.148 167.274 155.176 1.00 34.26 ?  513 THR B N     1 
ATOM   9660  C  CA    . THR B 1 513 ? 125.412 166.034 155.365 1.00 32.81 ?  513 THR B CA    1 
ATOM   9661  C  C     . THR B 1 513 ? 125.613 165.151 154.138 1.00 28.84 ?  513 THR B C     1 
ATOM   9662  O  O     . THR B 1 513 ? 126.363 165.490 153.220 1.00 38.58 ?  513 THR B O     1 
ATOM   9663  C  CB    . THR B 1 513 ? 123.931 166.321 155.607 1.00 31.71 ?  513 THR B CB    1 
ATOM   9664  O  OG1   . THR B 1 513 ? 123.337 166.824 154.405 1.00 33.73 ?  513 THR B OG1   1 
ATOM   9665  C  CG2   . THR B 1 513 ? 123.773 167.356 156.699 1.00 29.90 ?  513 THR B CG2   1 
ATOM   9666  N  N     . PHE B 1 514 ? 124.941 164.005 154.121 1.00 22.87 ?  514 PHE B N     1 
ATOM   9667  C  CA    . PHE B 1 514 ? 125.016 163.193 152.920 1.00 25.65 ?  514 PHE B CA    1 
ATOM   9668  C  C     . PHE B 1 514 ? 124.077 163.752 151.857 1.00 25.87 ?  514 PHE B C     1 
ATOM   9669  O  O     . PHE B 1 514 ? 123.158 164.522 152.143 1.00 32.72 ?  514 PHE B O     1 
ATOM   9670  C  CB    . PHE B 1 514 ? 124.696 161.724 153.212 1.00 20.36 ?  514 PHE B CB    1 
ATOM   9671  C  CG    . PHE B 1 514 ? 123.296 161.472 153.699 1.00 20.87 ?  514 PHE B CG    1 
ATOM   9672  C  CD1   . PHE B 1 514 ? 122.980 161.592 155.039 1.00 18.94 ?  514 PHE B CD1   1 
ATOM   9673  C  CD2   . PHE B 1 514 ? 122.305 161.077 152.818 1.00 20.33 ?  514 PHE B CD2   1 
ATOM   9674  C  CE1   . PHE B 1 514 ? 121.702 161.341 155.488 1.00 13.71 ?  514 PHE B CE1   1 
ATOM   9675  C  CE2   . PHE B 1 514 ? 121.024 160.826 153.262 1.00 17.18 ?  514 PHE B CE2   1 
ATOM   9676  C  CZ    . PHE B 1 514 ? 120.723 160.959 154.598 1.00 16.99 ?  514 PHE B CZ    1 
ATOM   9677  N  N     . ASP B 1 515 ? 124.339 163.374 150.608 1.00 27.24 ?  515 ASP B N     1 
ATOM   9678  C  CA    . ASP B 1 515 ? 123.565 163.910 149.499 1.00 29.97 ?  515 ASP B CA    1 
ATOM   9679  C  C     . ASP B 1 515 ? 122.105 163.496 149.614 1.00 33.38 ?  515 ASP B C     1 
ATOM   9680  O  O     . ASP B 1 515 ? 121.790 162.344 149.925 1.00 43.02 ?  515 ASP B O     1 
ATOM   9681  C  CB    . ASP B 1 515 ? 124.151 163.442 148.168 1.00 31.84 ?  515 ASP B CB    1 
ATOM   9682  C  CG    . ASP B 1 515 ? 125.418 164.188 147.799 1.00 34.96 ?  515 ASP B CG    1 
ATOM   9683  O  OD1   . ASP B 1 515 ? 126.027 164.808 148.695 1.00 34.91 ?  515 ASP B OD1   1 
ATOM   9684  O  OD2   . ASP B 1 515 ? 125.804 164.155 146.613 1.00 37.22 -1 515 ASP B OD2   1 
ATOM   9685  N  N     . GLN B 1 516 ? 121.213 164.456 149.363 1.00 33.32 ?  516 GLN B N     1 
ATOM   9686  C  CA    . GLN B 1 516 ? 119.768 164.256 149.476 1.00 29.64 ?  516 GLN B CA    1 
ATOM   9687  C  C     . GLN B 1 516 ? 119.370 163.852 150.894 1.00 32.54 ?  516 GLN B C     1 
ATOM   9688  O  O     . GLN B 1 516 ? 118.457 163.049 151.097 1.00 39.69 ?  516 GLN B O     1 
ATOM   9689  C  CB    . GLN B 1 516 ? 119.268 163.230 148.456 1.00 27.02 ?  516 GLN B CB    1 
ATOM   9690  C  CG    . GLN B 1 516 ? 119.627 163.559 147.020 1.00 30.65 ?  516 GLN B CG    1 
ATOM   9691  C  CD    . GLN B 1 516 ? 119.482 162.366 146.099 1.00 38.64 ?  516 GLN B CD    1 
ATOM   9692  O  OE1   . GLN B 1 516 ? 118.381 162.042 145.656 1.00 37.40 ?  516 GLN B OE1   1 
ATOM   9693  N  NE2   . GLN B 1 516 ? 120.595 161.703 145.810 1.00 38.99 ?  516 GLN B NE2   1 
ATOM   9694  N  N     . TYR B 1 517 ? 120.067 164.408 151.887 1.00 27.08 ?  517 TYR B N     1 
ATOM   9695  C  CA    . TYR B 1 517 ? 119.676 164.181 153.275 1.00 23.87 ?  517 TYR B CA    1 
ATOM   9696  C  C     . TYR B 1 517 ? 118.352 164.863 153.591 1.00 33.52 ?  517 TYR B C     1 
ATOM   9697  O  O     . TYR B 1 517 ? 117.552 164.343 154.377 1.00 42.64 ?  517 TYR B O     1 
ATOM   9698  C  CB    . TYR B 1 517 ? 120.767 164.675 154.226 1.00 21.30 ?  517 TYR B CB    1 
ATOM   9699  C  CG    . TYR B 1 517 ? 120.243 165.089 155.586 1.00 30.35 ?  517 TYR B CG    1 
ATOM   9700  C  CD1   . TYR B 1 517 ? 120.043 164.151 156.588 1.00 21.55 ?  517 TYR B CD1   1 
ATOM   9701  C  CD2   . TYR B 1 517 ? 119.947 166.419 155.865 1.00 31.64 ?  517 TYR B CD2   1 
ATOM   9702  C  CE1   . TYR B 1 517 ? 119.560 164.522 157.826 1.00 28.97 ?  517 TYR B CE1   1 
ATOM   9703  C  CE2   . TYR B 1 517 ? 119.463 166.796 157.098 1.00 27.98 ?  517 TYR B CE2   1 
ATOM   9704  C  CZ    . TYR B 1 517 ? 119.271 165.845 158.075 1.00 32.53 ?  517 TYR B CZ    1 
ATOM   9705  O  OH    . TYR B 1 517 ? 118.791 166.221 159.306 1.00 37.96 ?  517 TYR B OH    1 
ATOM   9706  N  N     . GLU B 1 518 ? 118.109 166.030 152.992 1.00 31.78 ?  518 GLU B N     1 
ATOM   9707  C  CA    . GLU B 1 518 ? 116.951 166.846 153.342 1.00 35.03 ?  518 GLU B CA    1 
ATOM   9708  C  C     . GLU B 1 518 ? 115.631 166.131 153.094 1.00 37.14 ?  518 GLU B C     1 
ATOM   9709  O  O     . GLU B 1 518 ? 114.634 166.449 153.751 1.00 41.81 ?  518 GLU B O     1 
ATOM   9710  C  CB    . GLU B 1 518 ? 116.985 168.163 152.564 1.00 33.49 ?  518 GLU B CB    1 
ATOM   9711  C  CG    . GLU B 1 518 ? 118.354 168.831 152.515 1.00 37.43 ?  518 GLU B CG    1 
ATOM   9712  C  CD    . GLU B 1 518 ? 119.239 168.291 151.405 1.00 46.20 ?  518 GLU B CD    1 
ATOM   9713  O  OE1   . GLU B 1 518 ? 118.769 168.218 150.249 1.00 44.98 ?  518 GLU B OE1   1 
ATOM   9714  O  OE2   . GLU B 1 518 ? 120.402 167.933 151.689 1.00 40.78 -1 518 GLU B OE2   1 
ATOM   9715  N  N     . GLY B 1 519 ? 115.595 165.181 152.164 1.00 28.86 ?  519 GLY B N     1 
ATOM   9716  C  CA    . GLY B 1 519 ? 114.402 164.388 151.951 1.00 23.81 ?  519 GLY B CA    1 
ATOM   9717  C  C     . GLY B 1 519 ? 114.263 163.176 152.837 1.00 25.57 ?  519 GLY B C     1 
ATOM   9718  O  O     . GLY B 1 519 ? 113.222 162.514 152.806 1.00 33.54 ?  519 GLY B O     1 
ATOM   9719  N  N     . SER B 1 520 ? 115.282 162.869 153.635 1.00 25.82 ?  520 SER B N     1 
ATOM   9720  C  CA    . SER B 1 520 ? 115.275 161.661 154.444 1.00 23.88 ?  520 SER B CA    1 
ATOM   9721  C  C     . SER B 1 520 ? 114.347 161.808 155.646 1.00 26.94 ?  520 SER B C     1 
ATOM   9722  O  O     . SER B 1 520 ? 113.927 162.907 156.016 1.00 27.18 ?  520 SER B O     1 
ATOM   9723  C  CB    . SER B 1 520 ? 116.690 161.324 154.915 1.00 21.54 ?  520 SER B CB    1 
ATOM   9724  O  OG    . SER B 1 520 ? 117.253 162.397 155.647 1.00 26.70 ?  520 SER B OG    1 
ATOM   9725  N  N     . THR B 1 521 ? 114.021 160.665 156.254 1.00 24.19 ?  521 THR B N     1 
ATOM   9726  C  CA    . THR B 1 521 ? 113.213 160.669 157.466 1.00 24.61 ?  521 THR B CA    1 
ATOM   9727  C  C     . THR B 1 521 ? 113.965 161.249 158.653 1.00 28.11 ?  521 THR B C     1 
ATOM   9728  O  O     . THR B 1 521 ? 113.332 161.669 159.628 1.00 32.01 ?  521 THR B O     1 
ATOM   9729  C  CB    . THR B 1 521 ? 112.739 159.253 157.789 1.00 28.66 ?  521 THR B CB    1 
ATOM   9730  O  OG1   . THR B 1 521 ? 113.862 158.446 158.161 1.00 30.86 ?  521 THR B OG1   1 
ATOM   9731  C  CG2   . THR B 1 521 ? 112.063 158.637 156.582 1.00 19.23 ?  521 THR B CG2   1 
ATOM   9732  N  N     . TYR B 1 522 ? 115.298 161.271 158.599 1.00 27.68 ?  522 TYR B N     1 
ATOM   9733  C  CA    . TYR B 1 522 ? 116.067 161.977 159.616 1.00 19.35 ?  522 TYR B CA    1 
ATOM   9734  C  C     . TYR B 1 522 ? 115.771 163.470 159.587 1.00 26.13 ?  522 TYR B C     1 
ATOM   9735  O  O     . TYR B 1 522 ? 115.625 164.105 160.637 1.00 31.32 ?  522 TYR B O     1 
ATOM   9736  C  CB    . TYR B 1 522 ? 117.560 161.736 159.410 1.00 21.34 ?  522 TYR B CB    1 
ATOM   9737  C  CG    . TYR B 1 522 ? 117.978 160.289 159.471 1.00 21.56 ?  522 TYR B CG    1 
ATOM   9738  C  CD1   . TYR B 1 522 ? 117.879 159.569 160.651 1.00 20.11 ?  522 TYR B CD1   1 
ATOM   9739  C  CD2   . TYR B 1 522 ? 118.498 159.651 158.354 1.00 22.80 ?  522 TYR B CD2   1 
ATOM   9740  C  CE1   . TYR B 1 522 ? 118.275 158.253 160.716 1.00 24.06 ?  522 TYR B CE1   1 
ATOM   9741  C  CE2   . TYR B 1 522 ? 118.893 158.334 158.410 1.00 19.98 ?  522 TYR B CE2   1 
ATOM   9742  C  CZ    . TYR B 1 522 ? 118.778 157.639 159.592 1.00 25.74 ?  522 TYR B CZ    1 
ATOM   9743  O  OH    . TYR B 1 522 ? 119.170 156.325 159.652 1.00 29.11 ?  522 TYR B OH    1 
ATOM   9744  N  N     . ALA B 1 523 ? 115.692 164.048 158.386 1.00 33.00 ?  523 ALA B N     1 
ATOM   9745  C  CA    . ALA B 1 523 ? 115.438 165.478 158.260 1.00 26.34 ?  523 ALA B CA    1 
ATOM   9746  C  C     . ALA B 1 523 ? 114.032 165.835 158.721 1.00 30.52 ?  523 ALA B C     1 
ATOM   9747  O  O     . ALA B 1 523 ? 113.832 166.859 159.385 1.00 34.10 ?  523 ALA B O     1 
ATOM   9748  C  CB    . ALA B 1 523 ? 115.659 165.921 156.816 1.00 24.96 ?  523 ALA B CB    1 
ATOM   9749  N  N     . THR B 1 524 ? 113.045 165.008 158.379 1.00 30.85 ?  524 THR B N     1 
ATOM   9750  C  CA    . THR B 1 524 ? 111.664 165.281 158.751 1.00 26.94 ?  524 THR B CA    1 
ATOM   9751  C  C     . THR B 1 524 ? 111.330 164.841 160.169 1.00 34.75 ?  524 THR B C     1 
ATOM   9752  O  O     . THR B 1 524 ? 110.252 165.185 160.666 1.00 41.72 ?  524 THR B O     1 
ATOM   9753  C  CB    . THR B 1 524 ? 110.709 164.597 157.771 1.00 33.13 ?  524 THR B CB    1 
ATOM   9754  O  OG1   . THR B 1 524 ? 110.600 163.206 158.096 1.00 35.03 ?  524 THR B OG1   1 
ATOM   9755  C  CG2   . THR B 1 524 ? 111.220 164.736 156.348 1.00 32.61 ?  524 THR B CG2   1 
ATOM   9756  N  N     . GLY B 1 525 ? 112.216 164.099 160.829 1.00 29.82 ?  525 GLY B N     1 
ATOM   9757  C  CA    . GLY B 1 525 ? 111.965 163.625 162.171 1.00 27.05 ?  525 GLY B CA    1 
ATOM   9758  C  C     . GLY B 1 525 ? 111.107 162.384 162.263 1.00 33.85 ?  525 GLY B C     1 
ATOM   9759  O  O     . GLY B 1 525 ? 110.881 161.889 163.374 1.00 32.98 ?  525 GLY B O     1 
ATOM   9760  N  N     . GLU B 1 526 ? 110.622 161.864 161.134 1.00 37.62 ?  526 GLU B N     1 
ATOM   9761  C  CA    . GLU B 1 526 ? 109.812 160.653 161.151 1.00 35.57 ?  526 GLU B CA    1 
ATOM   9762  C  C     . GLU B 1 526 ? 110.612 159.443 161.616 1.00 35.56 ?  526 GLU B C     1 
ATOM   9763  O  O     . GLU B 1 526 ? 110.029 158.489 162.142 1.00 41.96 ?  526 GLU B O     1 
ATOM   9764  C  CB    . GLU B 1 526 ? 109.218 160.419 159.757 1.00 36.25 ?  526 GLU B CB    1 
ATOM   9765  C  CG    . GLU B 1 526 ? 108.558 159.069 159.544 1.00 36.93 ?  526 GLU B CG    1 
ATOM   9766  C  CD    . GLU B 1 526 ? 108.552 158.650 158.087 1.00 44.72 ?  526 GLU B CD    1 
ATOM   9767  O  OE1   . GLU B 1 526 ? 108.545 159.542 157.213 1.00 43.21 ?  526 GLU B OE1   1 
ATOM   9768  O  OE2   . GLU B 1 526 ? 108.558 157.431 157.817 1.00 42.49 -1 526 GLU B OE2   1 
ATOM   9769  N  N     . TYR B 1 527 ? 111.936 159.478 161.459 1.00 35.15 ?  527 TYR B N     1 
ATOM   9770  C  CA    . TYR B 1 527 ? 112.773 158.376 161.922 1.00 25.96 ?  527 TYR B CA    1 
ATOM   9771  C  C     . TYR B 1 527 ? 112.692 158.214 163.435 1.00 28.26 ?  527 TYR B C     1 
ATOM   9772  O  O     . TYR B 1 527 ? 112.665 157.089 163.947 1.00 35.04 ?  527 TYR B O     1 
ATOM   9773  C  CB    . TYR B 1 527 ? 114.219 158.606 161.485 1.00 23.59 ?  527 TYR B CB    1 
ATOM   9774  C  CG    . TYR B 1 527 ? 115.166 157.503 161.891 1.00 28.20 ?  527 TYR B CG    1 
ATOM   9775  C  CD1   . TYR B 1 527 ? 115.383 156.411 161.065 1.00 23.69 ?  527 TYR B CD1   1 
ATOM   9776  C  CD2   . TYR B 1 527 ? 115.845 157.553 163.101 1.00 28.68 ?  527 TYR B CD2   1 
ATOM   9777  C  CE1   . TYR B 1 527 ? 116.245 155.403 161.430 1.00 23.79 ?  527 TYR B CE1   1 
ATOM   9778  C  CE2   . TYR B 1 527 ? 116.708 156.548 163.475 1.00 24.28 ?  527 TYR B CE2   1 
ATOM   9779  C  CZ    . TYR B 1 527 ? 116.904 155.476 162.636 1.00 23.27 ?  527 TYR B CZ    1 
ATOM   9780  O  OH    . TYR B 1 527 ? 117.765 154.471 163.005 1.00 32.61 ?  527 TYR B OH    1 
ATOM   9781  N  N     . PHE B 1 528 ? 112.654 159.325 164.165 1.00 32.99 ?  528 PHE B N     1 
ATOM   9782  C  CA    . PHE B 1 528 ? 112.761 159.320 165.616 1.00 27.64 ?  528 PHE B CA    1 
ATOM   9783  C  C     . PHE B 1 528 ? 111.426 159.111 166.320 1.00 36.60 ?  528 PHE B C     1 
ATOM   9784  O  O     . PHE B 1 528 ? 111.372 159.218 167.547 1.00 46.33 ?  528 PHE B O     1 
ATOM   9785  C  CB    . PHE B 1 528 ? 113.389 160.629 166.099 1.00 30.83 ?  528 PHE B CB    1 
ATOM   9786  C  CG    . PHE B 1 528 ? 114.756 160.891 165.541 1.00 33.47 ?  528 PHE B CG    1 
ATOM   9787  C  CD1   . PHE B 1 528 ? 115.883 160.415 166.187 1.00 24.97 ?  528 PHE B CD1   1 
ATOM   9788  C  CD2   . PHE B 1 528 ? 114.917 161.620 164.375 1.00 34.19 ?  528 PHE B CD2   1 
ATOM   9789  C  CE1   . PHE B 1 528 ? 117.142 160.656 165.677 1.00 28.35 ?  528 PHE B CE1   1 
ATOM   9790  C  CE2   . PHE B 1 528 ? 116.174 161.862 163.862 1.00 33.73 ?  528 PHE B CE2   1 
ATOM   9791  C  CZ    . PHE B 1 528 ? 117.287 161.380 164.516 1.00 31.75 ?  528 PHE B CZ    1 
ATOM   9792  N  N     . ASP B 1 529 ? 110.355 158.818 165.578 1.00 37.70 ?  529 ASP B N     1 
ATOM   9793  C  CA    . ASP B 1 529 ? 109.028 158.739 166.185 1.00 35.02 ?  529 ASP B CA    1 
ATOM   9794  C  C     . ASP B 1 529 ? 108.963 157.648 167.248 1.00 38.65 ?  529 ASP B C     1 
ATOM   9795  O  O     . ASP B 1 529 ? 108.549 157.896 168.387 1.00 42.72 ?  529 ASP B O     1 
ATOM   9796  C  CB    . ASP B 1 529 ? 107.977 158.496 165.103 1.00 32.50 ?  529 ASP B CB    1 
ATOM   9797  C  CG    . ASP B 1 529 ? 107.833 159.669 164.158 1.00 43.06 ?  529 ASP B CG    1 
ATOM   9798  O  OD1   . ASP B 1 529 ? 108.331 160.766 164.488 1.00 42.20 ?  529 ASP B OD1   1 
ATOM   9799  O  OD2   . ASP B 1 529 ? 107.222 159.493 163.083 1.00 48.54 -1 529 ASP B OD2   1 
ATOM   9800  N  N     . LYS B 1 530 ? 109.379 156.431 166.894 1.00 39.76 ?  530 LYS B N     1 
ATOM   9801  C  CA    . LYS B 1 530 ? 109.341 155.329 167.847 1.00 35.45 ?  530 LYS B CA    1 
ATOM   9802  C  C     . LYS B 1 530 ? 110.332 155.514 168.984 1.00 38.94 ?  530 LYS B C     1 
ATOM   9803  O  O     . LYS B 1 530 ? 110.181 154.878 170.031 1.00 43.21 ?  530 LYS B O     1 
ATOM   9804  C  CB    . LYS B 1 530 ? 109.610 154.007 167.132 1.00 37.18 ?  530 LYS B CB    1 
ATOM   9805  C  CG    . LYS B 1 530 ? 111.061 153.571 167.159 1.00 32.74 ?  530 LYS B CG    1 
ATOM   9806  C  CD    . LYS B 1 530 ? 111.256 152.303 166.359 1.00 38.19 ?  530 LYS B CD    1 
ATOM   9807  C  CE    . LYS B 1 530 ? 112.666 151.779 166.499 1.00 34.66 ?  530 LYS B CE    1 
ATOM   9808  N  NZ    . LYS B 1 530 ? 113.196 151.376 165.173 1.00 43.09 1  530 LYS B NZ    1 
ATOM   9809  N  N     . TYR B 1 531 ? 111.339 156.363 168.807 1.00 39.67 ?  531 TYR B N     1 
ATOM   9810  C  CA    . TYR B 1 531 ? 112.314 156.606 169.858 1.00 32.48 ?  531 TYR B CA    1 
ATOM   9811  C  C     . TYR B 1 531 ? 111.888 157.719 170.800 1.00 31.41 ?  531 TYR B C     1 
ATOM   9812  O  O     . TYR B 1 531 ? 112.208 157.668 171.992 1.00 40.60 ?  531 TYR B O     1 
ATOM   9813  C  CB    . TYR B 1 531 ? 113.673 156.936 169.243 1.00 27.04 ?  531 TYR B CB    1 
ATOM   9814  C  CG    . TYR B 1 531 ? 114.387 155.735 168.671 1.00 32.01 ?  531 TYR B CG    1 
ATOM   9815  C  CD1   . TYR B 1 531 ? 114.725 154.658 169.478 1.00 26.09 ?  531 TYR B CD1   1 
ATOM   9816  C  CD2   . TYR B 1 531 ? 114.723 155.678 167.327 1.00 28.89 ?  531 TYR B CD2   1 
ATOM   9817  C  CE1   . TYR B 1 531 ? 115.379 153.561 168.963 1.00 31.55 ?  531 TYR B CE1   1 
ATOM   9818  C  CE2   . TYR B 1 531 ? 115.378 154.584 166.804 1.00 25.44 ?  531 TYR B CE2   1 
ATOM   9819  C  CZ    . TYR B 1 531 ? 115.703 153.529 167.626 1.00 31.42 ?  531 TYR B CZ    1 
ATOM   9820  O  OH    . TYR B 1 531 ? 116.356 152.435 167.113 1.00 30.43 ?  531 TYR B OH    1 
ATOM   9821  N  N     . VAL B 1 532 ? 111.177 158.728 170.289 1.00 38.40 ?  532 VAL B N     1 
ATOM   9822  C  CA    . VAL B 1 532 ? 110.616 159.767 171.148 1.00 34.75 ?  532 VAL B CA    1 
ATOM   9823  C  C     . VAL B 1 532 ? 109.267 159.377 171.725 1.00 39.86 ?  532 VAL B C     1 
ATOM   9824  O  O     . VAL B 1 532 ? 108.729 160.111 172.563 1.00 47.83 ?  532 VAL B O     1 
ATOM   9825  C  CB    . VAL B 1 532 ? 110.464 161.102 170.394 1.00 40.64 ?  532 VAL B CB    1 
ATOM   9826  C  CG1   . VAL B 1 532 ? 111.790 161.527 169.787 1.00 37.44 ?  532 VAL B CG1   1 
ATOM   9827  C  CG2   . VAL B 1 532 ? 109.388 160.990 169.327 1.00 37.46 ?  532 VAL B CG2   1 
ATOM   9828  N  N     . SER B 1 533 ? 108.699 158.250 171.296 1.00 40.67 ?  533 SER B N     1 
ATOM   9829  C  CA    . SER B 1 533 ? 107.429 157.779 171.830 1.00 40.28 ?  533 SER B CA    1 
ATOM   9830  C  C     . SER B 1 533 ? 107.550 156.556 172.724 1.00 41.24 ?  533 SER B C     1 
ATOM   9831  O  O     . SER B 1 533 ? 106.773 156.422 173.670 1.00 46.20 ?  533 SER B O     1 
ATOM   9832  C  CB    . SER B 1 533 ? 106.458 157.456 170.687 1.00 45.12 ?  533 SER B CB    1 
ATOM   9833  O  OG    . SER B 1 533 ? 106.706 156.165 170.161 1.00 46.69 ?  533 SER B OG    1 
ATOM   9834  N  N     . THR B 1 534 ? 108.500 155.665 172.454 1.00 46.10 ?  534 THR B N     1 
ATOM   9835  C  CA    . THR B 1 534 ? 108.653 154.422 173.195 1.00 41.87 ?  534 THR B CA    1 
ATOM   9836  C  C     . THR B 1 534 ? 109.959 154.441 173.976 1.00 41.15 ?  534 THR B C     1 
ATOM   9837  O  O     . THR B 1 534 ? 110.973 154.955 173.496 1.00 49.01 ?  534 THR B O     1 
ATOM   9838  C  CB    . THR B 1 534 ? 108.628 153.210 172.254 1.00 42.71 ?  534 THR B CB    1 
ATOM   9839  O  OG1   . THR B 1 534 ? 107.506 153.311 171.370 1.00 42.40 ?  534 THR B OG1   1 
ATOM   9840  C  CG2   . THR B 1 534 ? 108.526 151.913 173.043 1.00 43.68 ?  534 THR B CG2   1 
ATOM   9841  N  N     . ASP B 1 535 ? 109.926 153.882 175.181 1.00 43.04 ?  535 ASP B N     1 
ATOM   9842  C  CA    . ASP B 1 535 ? 111.106 153.746 176.022 1.00 42.66 ?  535 ASP B CA    1 
ATOM   9843  C  C     . ASP B 1 535 ? 111.733 152.380 175.785 1.00 45.35 ?  535 ASP B C     1 
ATOM   9844  O  O     . ASP B 1 535 ? 111.038 151.358 175.820 1.00 47.18 ?  535 ASP B O     1 
ATOM   9845  C  CB    . ASP B 1 535 ? 110.747 153.918 177.498 1.00 41.53 ?  535 ASP B CB    1 
ATOM   9846  C  CG    . ASP B 1 535 ? 111.969 154.015 178.387 1.00 47.31 ?  535 ASP B CG    1 
ATOM   9847  O  OD1   . ASP B 1 535 ? 112.735 154.991 178.243 1.00 48.84 ?  535 ASP B OD1   1 
ATOM   9848  O  OD2   . ASP B 1 535 ? 112.163 153.116 179.230 1.00 47.75 -1 535 ASP B OD2   1 
ATOM   9849  N  N     . PHE B 1 536 ? 113.045 152.363 175.545 1.00 40.14 ?  536 PHE B N     1 
ATOM   9850  C  CA    . PHE B 1 536 ? 113.763 151.135 175.232 1.00 34.91 ?  536 PHE B CA    1 
ATOM   9851  C  C     . PHE B 1 536 ? 114.717 150.722 176.348 1.00 35.66 ?  536 PHE B C     1 
ATOM   9852  O  O     . PHE B 1 536 ? 115.689 150.003 176.094 1.00 43.03 ?  536 PHE B O     1 
ATOM   9853  C  CB    . PHE B 1 536 ? 114.517 151.288 173.912 1.00 34.94 ?  536 PHE B CB    1 
ATOM   9854  C  CG    . PHE B 1 536 ? 113.621 151.377 172.710 1.00 31.98 ?  536 PHE B CG    1 
ATOM   9855  C  CD1   . PHE B 1 536 ? 113.217 150.233 172.046 1.00 32.97 ?  536 PHE B CD1   1 
ATOM   9856  C  CD2   . PHE B 1 536 ? 113.183 152.603 172.247 1.00 32.10 ?  536 PHE B CD2   1 
ATOM   9857  C  CE1   . PHE B 1 536 ? 112.392 150.311 170.942 1.00 31.04 ?  536 PHE B CE1   1 
ATOM   9858  C  CE2   . PHE B 1 536 ? 112.357 152.685 171.143 1.00 39.85 ?  536 PHE B CE2   1 
ATOM   9859  C  CZ    . PHE B 1 536 ? 111.963 151.537 170.490 1.00 30.69 ?  536 PHE B CZ    1 
ATOM   9860  N  N     . SER B 1 537 ? 114.464 151.168 177.576 1.00 36.35 ?  537 SER B N     1 
ATOM   9861  C  CA    . SER B 1 537 ? 115.216 150.692 178.721 1.00 34.06 ?  537 SER B CA    1 
ATOM   9862  C  C     . SER B 1 537 ? 114.860 149.234 179.004 1.00 38.38 ?  537 SER B C     1 
ATOM   9863  O  O     . SER B 1 537 ? 113.781 148.767 178.632 1.00 41.45 ?  537 SER B O     1 
ATOM   9864  C  CB    . SER B 1 537 ? 114.924 151.560 179.943 1.00 34.61 ?  537 SER B CB    1 
ATOM   9865  O  OG    . SER B 1 537 ? 113.558 151.485 180.305 1.00 39.68 ?  537 SER B OG    1 
ATOM   9866  N  N     . PRO B 1 538 ? 115.761 148.487 179.643 1.00 37.30 ?  538 PRO B N     1 
ATOM   9867  C  CA    . PRO B 1 538 ? 115.476 147.073 179.912 1.00 35.39 ?  538 PRO B CA    1 
ATOM   9868  C  C     . PRO B 1 538 ? 114.260 146.906 180.811 1.00 40.61 ?  538 PRO B C     1 
ATOM   9869  O  O     . PRO B 1 538 ? 114.029 147.691 181.732 1.00 39.18 ?  538 PRO B O     1 
ATOM   9870  C  CB    . PRO B 1 538 ? 116.755 146.576 180.598 1.00 35.57 ?  538 PRO B CB    1 
ATOM   9871  C  CG    . PRO B 1 538 ? 117.802 147.570 180.242 1.00 34.04 ?  538 PRO B CG    1 
ATOM   9872  C  CD    . PRO B 1 538 ? 117.091 148.878 180.136 1.00 36.00 ?  538 PRO B CD    1 
ATOM   9873  N  N     . LYS B 1 539 ? 113.476 145.868 180.527 1.00 45.36 ?  539 LYS B N     1 
ATOM   9874  C  CA    . LYS B 1 539 ? 112.296 145.538 181.314 1.00 45.52 ?  539 LYS B CA    1 
ATOM   9875  C  C     . LYS B 1 539 ? 112.575 144.494 182.385 1.00 47.99 ?  539 LYS B C     1 
ATOM   9876  O  O     . LYS B 1 539 ? 111.663 144.135 183.133 1.00 48.24 ?  539 LYS B O     1 
ATOM   9877  C  CB    . LYS B 1 539 ? 111.171 145.045 180.398 1.00 45.74 ?  539 LYS B CB    1 
ATOM   9878  C  CG    . LYS B 1 539 ? 111.191 145.647 179.005 1.00 43.95 ?  539 LYS B CG    1 
ATOM   9879  C  CD    . LYS B 1 539 ? 110.683 147.080 179.009 1.00 48.13 ?  539 LYS B CD    1 
ATOM   9880  C  CE    . LYS B 1 539 ? 109.913 147.394 177.736 1.00 49.03 ?  539 LYS B CE    1 
ATOM   9881  N  NZ    . LYS B 1 539 ? 110.796 147.412 176.538 1.00 49.69 1  539 LYS B NZ    1 
ATOM   9882  N  N     . TYR B 1 540 ? 113.807 144.003 182.475 1.00 45.89 ?  540 TYR B N     1 
ATOM   9883  C  CA    . TYR B 1 540 ? 114.187 142.985 183.440 1.00 43.91 ?  540 TYR B CA    1 
ATOM   9884  C  C     . TYR B 1 540 ? 115.285 143.524 184.343 1.00 46.08 ?  540 TYR B C     1 
ATOM   9885  O  O     . TYR B 1 540 ? 116.196 144.218 183.882 1.00 47.79 ?  540 TYR B O     1 
ATOM   9886  C  CB    . TYR B 1 540 ? 114.657 141.708 182.739 1.00 44.43 ?  540 TYR B CB    1 
ATOM   9887  C  CG    . TYR B 1 540 ? 113.565 141.001 181.970 1.00 47.68 ?  540 TYR B CG    1 
ATOM   9888  C  CD1   . TYR B 1 540 ? 113.282 141.342 180.655 1.00 44.57 ?  540 TYR B CD1   1 
ATOM   9889  C  CD2   . TYR B 1 540 ? 112.813 139.997 182.562 1.00 48.48 ?  540 TYR B CD2   1 
ATOM   9890  C  CE1   . TYR B 1 540 ? 112.284 140.701 179.950 1.00 43.43 ?  540 TYR B CE1   1 
ATOM   9891  C  CE2   . TYR B 1 540 ? 111.812 139.350 181.864 1.00 45.36 ?  540 TYR B CE2   1 
ATOM   9892  C  CZ    . TYR B 1 540 ? 111.552 139.706 180.560 1.00 44.75 ?  540 TYR B CZ    1 
ATOM   9893  O  OH    . TYR B 1 540 ? 110.555 139.065 179.863 1.00 49.48 ?  540 TYR B OH    1 
ATOM   9894  N  N     . GLU B 1 541 ? 115.187 143.205 185.636 1.00 49.92 ?  541 GLU B N     1 
ATOM   9895  C  CA    . GLU B 1 541 ? 116.170 143.693 186.598 1.00 45.77 ?  541 GLU B CA    1 
ATOM   9896  C  C     . GLU B 1 541 ? 117.560 143.147 186.295 1.00 46.72 ?  541 GLU B C     1 
ATOM   9897  O  O     . GLU B 1 541 ? 118.561 143.855 186.458 1.00 46.88 ?  541 GLU B O     1 
ATOM   9898  C  CB    . GLU B 1 541 ? 115.743 143.322 188.017 1.00 46.79 ?  541 GLU B CB    1 
ATOM   9899  C  CG    . GLU B 1 541 ? 116.588 143.959 189.108 1.00 48.67 ?  541 GLU B CG    1 
ATOM   9900  C  CD    . GLU B 1 541 ? 117.401 142.942 189.884 1.00 53.09 ?  541 GLU B CD    1 
ATOM   9901  O  OE1   . GLU B 1 541 ? 117.181 141.728 189.685 1.00 50.43 ?  541 GLU B OE1   1 
ATOM   9902  O  OE2   . GLU B 1 541 ? 118.258 143.355 190.691 1.00 53.20 -1 541 GLU B OE2   1 
ATOM   9903  N  N     . LYS B 1 542 ? 117.643 141.886 185.864 1.00 43.44 ?  542 LYS B N     1 
ATOM   9904  C  CA    . LYS B 1 542 ? 118.936 141.309 185.513 1.00 39.82 ?  542 LYS B CA    1 
ATOM   9905  C  C     . LYS B 1 542 ? 119.569 142.041 184.337 1.00 44.78 ?  542 LYS B C     1 
ATOM   9906  O  O     . LYS B 1 542 ? 120.772 142.325 184.347 1.00 42.69 ?  542 LYS B O     1 
ATOM   9907  C  CB    . LYS B 1 542 ? 118.777 139.822 185.193 1.00 41.29 ?  542 LYS B CB    1 
ATOM   9908  C  CG    . LYS B 1 542 ? 120.050 139.157 184.699 1.00 43.38 ?  542 LYS B CG    1 
ATOM   9909  C  CD    . LYS B 1 542 ? 119.878 137.654 184.565 1.00 41.03 ?  542 LYS B CD    1 
ATOM   9910  C  CE    . LYS B 1 542 ? 121.202 136.977 184.255 1.00 44.05 ?  542 LYS B CE    1 
ATOM   9911  N  NZ    . LYS B 1 542 ? 121.103 135.497 184.346 1.00 44.68 1  542 LYS B NZ    1 
ATOM   9912  N  N     . ILE B 1 543 ? 118.773 142.356 183.313 1.00 43.71 ?  543 ILE B N     1 
ATOM   9913  C  CA    . ILE B 1 543 ? 119.300 143.077 182.159 1.00 37.51 ?  543 ILE B CA    1 
ATOM   9914  C  C     . ILE B 1 543 ? 119.649 144.511 182.537 1.00 37.39 ?  543 ILE B C     1 
ATOM   9915  O  O     . ILE B 1 543 ? 120.673 145.049 182.101 1.00 37.90 ?  543 ILE B O     1 
ATOM   9916  C  CB    . ILE B 1 543 ? 118.296 143.026 180.995 1.00 36.35 ?  543 ILE B CB    1 
ATOM   9917  C  CG1   . ILE B 1 543 ? 117.925 141.578 180.669 1.00 39.05 ?  543 ILE B CG1   1 
ATOM   9918  C  CG2   . ILE B 1 543 ? 118.871 143.713 179.775 1.00 36.17 ?  543 ILE B CG2   1 
ATOM   9919  C  CD1   . ILE B 1 543 ? 119.115 140.664 180.493 1.00 33.21 ?  543 ILE B CD1   1 
ATOM   9920  N  N     . ALA B 1 544 ? 118.806 145.155 183.349 1.00 35.49 ?  544 ALA B N     1 
ATOM   9921  C  CA    . ALA B 1 544 ? 119.097 146.515 183.785 1.00 39.29 ?  544 ALA B CA    1 
ATOM   9922  C  C     . ALA B 1 544 ? 120.369 146.575 184.620 1.00 44.33 ?  544 ALA B C     1 
ATOM   9923  O  O     . ALA B 1 544 ? 121.042 147.611 184.652 1.00 48.55 ?  544 ALA B O     1 
ATOM   9924  C  CB    . ALA B 1 544 ? 117.917 147.080 184.574 1.00 40.47 ?  544 ALA B CB    1 
ATOM   9925  N  N     . ASN B 1 545 ? 120.713 145.480 185.301 1.00 45.04 ?  545 ASN B N     1 
ATOM   9926  C  CA    . ASN B 1 545 ? 121.965 145.437 186.047 1.00 45.81 ?  545 ASN B CA    1 
ATOM   9927  C  C     . ASN B 1 545 ? 123.164 145.301 185.119 1.00 44.60 ?  545 ASN B C     1 
ATOM   9928  O  O     . ASN B 1 545 ? 124.273 145.711 185.480 1.00 46.40 ?  545 ASN B O     1 
ATOM   9929  C  CB    . ASN B 1 545 ? 121.941 144.288 187.054 1.00 47.28 ?  545 ASN B CB    1 
ATOM   9930  C  CG    . ASN B 1 545 ? 121.095 144.599 188.271 1.00 49.62 ?  545 ASN B CG    1 
ATOM   9931  O  OD1   . ASN B 1 545 ? 120.929 145.760 188.645 1.00 48.80 ?  545 ASN B OD1   1 
ATOM   9932  N  ND2   . ASN B 1 545 ? 120.556 143.561 188.899 1.00 44.89 ?  545 ASN B ND2   1 
ATOM   9933  N  N     . LEU B 1 546 ? 122.967 144.724 183.931 1.00 44.21 ?  546 LEU B N     1 
ATOM   9934  C  CA    . LEU B 1 546 ? 124.062 144.604 182.975 1.00 37.40 ?  546 LEU B CA    1 
ATOM   9935  C  C     . LEU B 1 546 ? 124.535 145.967 182.491 1.00 37.79 ?  546 LEU B C     1 
ATOM   9936  O  O     . LEU B 1 546 ? 125.711 146.132 182.151 1.00 39.54 ?  546 LEU B O     1 
ATOM   9937  C  CB    . LEU B 1 546 ? 123.633 143.743 181.788 1.00 36.36 ?  546 LEU B CB    1 
ATOM   9938  C  CG    . LEU B 1 546 ? 123.231 142.298 182.083 1.00 38.55 ?  546 LEU B CG    1 
ATOM   9939  C  CD1   . LEU B 1 546 ? 122.742 141.618 180.817 1.00 37.37 ?  546 LEU B CD1   1 
ATOM   9940  C  CD2   . LEU B 1 546 ? 124.390 141.529 182.691 1.00 37.55 ?  546 LEU B CD2   1 
ATOM   9941  N  N     . PHE B 1 547 ? 123.641 146.954 182.465 1.00 39.72 ?  547 PHE B N     1 
ATOM   9942  C  CA    . PHE B 1 547 ? 123.957 148.296 181.995 1.00 38.97 ?  547 PHE B CA    1 
ATOM   9943  C  C     . PHE B 1 547 ? 124.298 149.245 183.136 1.00 40.70 ?  547 PHE B C     1 
ATOM   9944  O  O     . PHE B 1 547 ? 124.247 150.466 182.953 1.00 44.69 ?  547 PHE B O     1 
ATOM   9945  C  CB    . PHE B 1 547 ? 122.795 148.855 181.174 1.00 37.62 ?  547 PHE B CB    1 
ATOM   9946  C  CG    . PHE B 1 547 ? 122.577 148.148 179.867 1.00 39.12 ?  547 PHE B CG    1 
ATOM   9947  C  CD1   . PHE B 1 547 ? 121.751 147.040 179.792 1.00 37.61 ?  547 PHE B CD1   1 
ATOM   9948  C  CD2   . PHE B 1 547 ? 123.194 148.594 178.712 1.00 38.44 ?  547 PHE B CD2   1 
ATOM   9949  C  CE1   . PHE B 1 547 ? 121.548 146.391 178.590 1.00 38.08 ?  547 PHE B CE1   1 
ATOM   9950  C  CE2   . PHE B 1 547 ? 122.994 147.948 177.509 1.00 33.49 ?  547 PHE B CE2   1 
ATOM   9951  C  CZ    . PHE B 1 547 ? 122.171 146.846 177.449 1.00 35.40 ?  547 PHE B CZ    1 
ATOM   9952  N  N     . GLU B 1 548 ? 124.630 148.711 184.309 1.00 47.33 ?  548 GLU B N     1 
ATOM   9953  C  CA    . GLU B 1 548 ? 124.983 149.553 185.443 1.00 48.82 ?  548 GLU B CA    1 
ATOM   9954  C  C     . GLU B 1 548 ? 126.241 150.355 185.136 1.00 52.47 ?  548 GLU B C     1 
ATOM   9955  O  O     . GLU B 1 548 ? 127.183 149.856 184.516 1.00 52.34 ?  548 GLU B O     1 
ATOM   9956  C  CB    . GLU B 1 548 ? 125.195 148.697 186.692 1.00 47.67 ?  548 GLU B CB    1 
ATOM   9957  C  CG    . GLU B 1 548 ? 123.950 148.517 187.543 1.00 50.67 ?  548 GLU B CG    1 
ATOM   9958  C  CD    . GLU B 1 548 ? 124.112 147.428 188.586 1.00 56.24 ?  548 GLU B CD    1 
ATOM   9959  O  OE1   . GLU B 1 548 ? 124.985 146.554 188.401 1.00 55.02 ?  548 GLU B OE1   1 
ATOM   9960  O  OE2   . GLU B 1 548 ? 123.368 147.446 189.589 1.00 55.23 -1 548 GLU B OE2   1 
ATOM   9961  N  N     . GLY B 1 549 ? 126.253 151.611 185.576 1.00 50.26 ?  549 GLY B N     1 
ATOM   9962  C  CA    . GLY B 1 549 ? 127.349 152.502 185.262 1.00 49.92 ?  549 GLY B CA    1 
ATOM   9963  C  C     . GLY B 1 549 ? 127.342 153.032 183.850 1.00 51.73 ?  549 GLY B C     1 
ATOM   9964  O  O     . GLY B 1 549 ? 128.357 153.576 183.402 1.00 54.70 ?  549 GLY B O     1 
ATOM   9965  N  N     . MET B 1 550 ? 126.230 152.891 183.133 1.00 48.89 ?  550 MET B N     1 
ATOM   9966  C  CA    . MET B 1 550 ? 126.125 153.309 181.743 1.00 44.47 ?  550 MET B CA    1 
ATOM   9967  C  C     . MET B 1 550 ? 124.773 153.967 181.533 1.00 46.73 ?  550 MET B C     1 
ATOM   9968  O  O     . MET B 1 550 ? 123.738 153.373 181.844 1.00 52.25 ?  550 MET B O     1 
ATOM   9969  C  CB    . MET B 1 550 ? 126.290 152.113 180.803 1.00 44.64 ?  550 MET B CB    1 
ATOM   9970  C  CG    . MET B 1 550 ? 127.019 152.425 179.517 1.00 51.54 ?  550 MET B CG    1 
ATOM   9971  S  SD    . MET B 1 550 ? 127.115 150.990 178.435 1.00 60.33 ?  550 MET B SD    1 
ATOM   9972  C  CE    . MET B 1 550 ? 127.056 149.651 179.620 1.00 48.02 ?  550 MET B CE    1 
ATOM   9973  N  N     . HIS B 1 551 ? 124.782 155.189 181.007 1.00 42.96 ?  551 HIS B N     1 
ATOM   9974  C  CA    . HIS B 1 551 ? 123.546 155.931 180.808 1.00 43.58 ?  551 HIS B CA    1 
ATOM   9975  C  C     . HIS B 1 551 ? 122.807 155.389 179.591 1.00 46.12 ?  551 HIS B C     1 
ATOM   9976  O  O     . HIS B 1 551 ? 123.300 155.485 178.463 1.00 44.91 ?  551 HIS B O     1 
ATOM   9977  C  CB    . HIS B 1 551 ? 123.830 157.421 180.639 1.00 41.99 ?  551 HIS B CB    1 
ATOM   9978  C  CG    . HIS B 1 551 ? 122.632 158.214 180.219 1.00 46.24 ?  551 HIS B CG    1 
ATOM   9979  N  ND1   . HIS B 1 551 ? 121.667 158.631 181.110 1.00 49.73 ?  551 HIS B ND1   1 
ATOM   9980  C  CD2   . HIS B 1 551 ? 122.241 158.662 179.003 1.00 46.93 ?  551 HIS B CD2   1 
ATOM   9981  C  CE1   . HIS B 1 551 ? 120.733 159.303 180.460 1.00 47.40 ?  551 HIS B CE1   1 
ATOM   9982  N  NE2   . HIS B 1 551 ? 121.058 159.337 179.181 1.00 46.40 ?  551 HIS B NE2   1 
ATOM   9983  N  N     . ILE B 1 552 ? 121.630 154.822 179.823 1.00 40.04 ?  552 ILE B N     1 
ATOM   9984  C  CA    . ILE B 1 552 ? 120.771 154.327 178.753 1.00 37.77 ?  552 ILE B CA    1 
ATOM   9985  C  C     . ILE B 1 552 ? 119.957 155.506 178.226 1.00 38.12 ?  552 ILE B C     1 
ATOM   9986  O  O     . ILE B 1 552 ? 119.267 156.165 179.020 1.00 37.71 ?  552 ILE B O     1 
ATOM   9987  C  CB    . ILE B 1 552 ? 119.856 153.202 179.246 1.00 36.38 ?  552 ILE B CB    1 
ATOM   9988  C  CG1   . ILE B 1 552 ? 120.694 152.035 179.768 1.00 35.67 ?  552 ILE B CG1   1 
ATOM   9989  C  CG2   . ILE B 1 552 ? 118.926 152.741 178.137 1.00 36.34 ?  552 ILE B CG2   1 
ATOM   9990  C  CD1   . ILE B 1 552 ? 119.908 151.034 180.570 1.00 38.89 ?  552 ILE B CD1   1 
ATOM   9991  N  N     . PRO B 1 553 ? 120.021 155.813 176.931 1.00 40.67 ?  553 PRO B N     1 
ATOM   9992  C  CA    . PRO B 1 553 ? 119.271 156.961 176.408 1.00 37.77 ?  553 PRO B CA    1 
ATOM   9993  C  C     . PRO B 1 553 ? 117.779 156.818 176.660 1.00 40.06 ?  553 PRO B C     1 
ATOM   9994  O  O     . PRO B 1 553 ? 117.197 155.745 176.488 1.00 41.00 ?  553 PRO B O     1 
ATOM   9995  C  CB    . PRO B 1 553 ? 119.592 156.940 174.911 1.00 34.16 ?  553 PRO B CB    1 
ATOM   9996  C  CG    . PRO B 1 553 ? 120.891 156.224 174.817 1.00 32.33 ?  553 PRO B CG    1 
ATOM   9997  C  CD    . PRO B 1 553 ? 120.875 155.197 175.904 1.00 33.34 ?  553 PRO B CD    1 
ATOM   9998  N  N     . THR B 1 554 ? 117.162 157.921 177.065 1.00 43.12 ?  554 THR B N     1 
ATOM   9999  C  CA    . THR B 1 554 ? 115.747 157.957 177.380 1.00 41.44 ?  554 THR B CA    1 
ATOM   10000 C  C     . THR B 1 554 ? 114.977 158.614 176.241 1.00 38.99 ?  554 THR B C     1 
ATOM   10001 O  O     . THR B 1 554 ? 115.524 158.935 175.183 1.00 37.79 ?  554 THR B O     1 
ATOM   10002 C  CB    . THR B 1 554 ? 115.509 158.697 178.698 1.00 37.55 ?  554 THR B CB    1 
ATOM   10003 O  OG1   . THR B 1 554 ? 115.692 160.103 178.496 1.00 43.39 ?  554 THR B OG1   1 
ATOM   10004 C  CG2   . THR B 1 554 ? 116.483 158.215 179.759 1.00 36.57 ?  554 THR B CG2   1 
ATOM   10005 N  N     . THR B 1 555 ? 113.677 158.807 176.464 1.00 42.76 ?  555 THR B N     1 
ATOM   10006 C  CA    . THR B 1 555 ? 112.854 159.510 175.487 1.00 39.77 ?  555 THR B CA    1 
ATOM   10007 C  C     . THR B 1 555 ? 113.294 160.963 175.343 1.00 40.86 ?  555 THR B C     1 
ATOM   10008 O  O     . THR B 1 555 ? 113.331 161.499 174.230 1.00 44.26 ?  555 THR B O     1 
ATOM   10009 C  CB    . THR B 1 555 ? 111.382 159.415 175.889 1.00 43.88 ?  555 THR B CB    1 
ATOM   10010 O  OG1   . THR B 1 555 ? 110.878 158.118 175.546 1.00 42.11 ?  555 THR B OG1   1 
ATOM   10011 C  CG2   . THR B 1 555 ? 110.554 160.473 175.185 1.00 42.31 ?  555 THR B CG2   1 
ATOM   10012 N  N     . GLU B 1 556 ? 113.643 161.614 176.455 1.00 37.54 ?  556 GLU B N     1 
ATOM   10013 C  CA    . GLU B 1 556 ? 114.133 162.988 176.386 1.00 41.22 ?  556 GLU B CA    1 
ATOM   10014 C  C     . GLU B 1 556 ? 115.473 163.064 175.663 1.00 41.20 ?  556 GLU B C     1 
ATOM   10015 O  O     . GLU B 1 556 ? 115.718 164.003 174.895 1.00 45.19 ?  556 GLU B O     1 
ATOM   10016 C  CB    . GLU B 1 556 ? 114.242 163.577 177.791 1.00 42.16 ?  556 GLU B CB    1 
ATOM   10017 C  CG    . GLU B 1 556 ? 112.901 163.843 178.461 1.00 43.79 ?  556 GLU B CG    1 
ATOM   10018 C  CD    . GLU B 1 556 ? 111.869 164.416 177.506 1.00 46.68 ?  556 GLU B CD    1 
ATOM   10019 O  OE1   . GLU B 1 556 ? 111.888 165.643 177.275 1.00 44.65 ?  556 GLU B OE1   1 
ATOM   10020 O  OE2   . GLU B 1 556 ? 111.033 163.643 176.994 1.00 46.96 -1 556 GLU B OE2   1 
ATOM   10021 N  N     . ASP B 1 557 ? 116.356 162.092 175.901 1.00 39.92 ?  557 ASP B N     1 
ATOM   10022 C  CA    . ASP B 1 557 ? 117.618 162.046 175.171 1.00 35.53 ?  557 ASP B CA    1 
ATOM   10023 C  C     . ASP B 1 557 ? 117.379 161.872 173.679 1.00 36.19 ?  557 ASP B C     1 
ATOM   10024 O  O     . ASP B 1 557 ? 118.065 162.489 172.855 1.00 39.67 ?  557 ASP B O     1 
ATOM   10025 C  CB    . ASP B 1 557 ? 118.496 160.914 175.706 1.00 35.05 ?  557 ASP B CB    1 
ATOM   10026 C  CG    . ASP B 1 557 ? 118.969 161.163 177.122 1.00 42.94 ?  557 ASP B CG    1 
ATOM   10027 O  OD1   . ASP B 1 557 ? 119.565 162.231 177.372 1.00 44.87 ?  557 ASP B OD1   1 
ATOM   10028 O  OD2   . ASP B 1 557 ? 118.746 160.289 177.984 1.00 43.75 -1 557 ASP B OD2   1 
ATOM   10029 N  N     . TRP B 1 558 ? 116.405 161.041 173.311 1.00 30.30 ?  558 TRP B N     1 
ATOM   10030 C  CA    . TRP B 1 558 ? 116.086 160.862 171.899 1.00 26.01 ?  558 TRP B CA    1 
ATOM   10031 C  C     . TRP B 1 558 ? 115.468 162.116 171.294 1.00 31.95 ?  558 TRP B C     1 
ATOM   10032 O  O     . TRP B 1 558 ? 115.718 162.417 170.125 1.00 37.89 ?  558 TRP B O     1 
ATOM   10033 C  CB    . TRP B 1 558 ? 115.159 159.664 171.724 1.00 32.42 ?  558 TRP B CB    1 
ATOM   10034 C  CG    . TRP B 1 558 ? 115.896 158.374 171.570 1.00 28.63 ?  558 TRP B CG    1 
ATOM   10035 C  CD1   . TRP B 1 558 ? 116.002 157.376 172.491 1.00 25.06 ?  558 TRP B CD1   1 
ATOM   10036 C  CD2   . TRP B 1 558 ? 116.633 157.942 170.422 1.00 29.59 ?  558 TRP B CD2   1 
ATOM   10037 N  NE1   . TRP B 1 558 ? 116.758 156.348 171.987 1.00 31.93 ?  558 TRP B NE1   1 
ATOM   10038 C  CE2   . TRP B 1 558 ? 117.155 156.670 170.717 1.00 29.94 ?  558 TRP B CE2   1 
ATOM   10039 C  CE3   . TRP B 1 558 ? 116.894 158.505 169.170 1.00 30.69 ?  558 TRP B CE3   1 
ATOM   10040 C  CZ2   . TRP B 1 558 ? 117.926 155.952 169.807 1.00 25.80 ?  558 TRP B CZ2   1 
ATOM   10041 C  CZ3   . TRP B 1 558 ? 117.659 157.793 168.270 1.00 28.24 ?  558 TRP B CZ3   1 
ATOM   10042 C  CH2   . TRP B 1 558 ? 118.166 156.530 168.592 1.00 23.67 ?  558 TRP B CH2   1 
ATOM   10043 N  N     . LYS B 1 559 ? 114.666 162.857 172.062 1.00 36.67 ?  559 LYS B N     1 
ATOM   10044 C  CA    . LYS B 1 559 ? 114.154 164.133 171.570 1.00 34.56 ?  559 LYS B CA    1 
ATOM   10045 C  C     . LYS B 1 559 ? 115.283 165.134 171.355 1.00 37.87 ?  559 LYS B C     1 
ATOM   10046 O  O     . LYS B 1 559 ? 115.289 165.875 170.364 1.00 38.90 ?  559 LYS B O     1 
ATOM   10047 C  CB    . LYS B 1 559 ? 113.120 164.696 172.542 1.00 37.71 ?  559 LYS B CB    1 
ATOM   10048 C  CG    . LYS B 1 559 ? 111.767 164.016 172.470 1.00 42.19 ?  559 LYS B CG    1 
ATOM   10049 C  CD    . LYS B 1 559 ? 110.850 164.503 173.577 1.00 38.05 ?  559 LYS B CD    1 
ATOM   10050 C  CE    . LYS B 1 559 ? 109.612 163.634 173.687 1.00 41.69 ?  559 LYS B CE    1 
ATOM   10051 N  NZ    . LYS B 1 559 ? 109.068 163.627 175.072 1.00 39.05 1  559 LYS B NZ    1 
ATOM   10052 N  N     . LYS B 1 560 ? 116.246 165.170 172.278 1.00 34.00 ?  560 LYS B N     1 
ATOM   10053 C  CA    . LYS B 1 560 ? 117.404 166.040 172.105 1.00 33.62 ?  560 LYS B CA    1 
ATOM   10054 C  C     . LYS B 1 560 ? 118.209 165.642 170.874 1.00 38.20 ?  560 LYS B C     1 
ATOM   10055 O  O     . LYS B 1 560 ? 118.677 166.505 170.123 1.00 42.72 ?  560 LYS B O     1 
ATOM   10056 C  CB    . LYS B 1 560 ? 118.279 166.003 173.357 1.00 37.36 ?  560 LYS B CB    1 
ATOM   10057 C  CG    . LYS B 1 560 ? 117.857 166.986 174.434 1.00 37.70 ?  560 LYS B CG    1 
ATOM   10058 C  CD    . LYS B 1 560 ? 118.602 166.732 175.733 1.00 42.97 ?  560 LYS B CD    1 
ATOM   10059 C  CE    . LYS B 1 560 ? 117.678 166.861 176.933 1.00 39.49 ?  560 LYS B CE    1 
ATOM   10060 N  NZ    . LYS B 1 560 ? 117.754 165.668 177.822 1.00 44.10 1  560 LYS B NZ    1 
ATOM   10061 N  N     . LEU B 1 561 ? 118.377 164.338 170.649 1.00 36.05 ?  561 LEU B N     1 
ATOM   10062 C  CA    . LEU B 1 561 ? 119.072 163.873 169.453 1.00 30.62 ?  561 LEU B CA    1 
ATOM   10063 C  C     . LEU B 1 561 ? 118.305 164.236 168.189 1.00 34.86 ?  561 LEU B C     1 
ATOM   10064 O  O     . LEU B 1 561 ? 118.909 164.589 167.171 1.00 39.07 ?  561 LEU B O     1 
ATOM   10065 C  CB    . LEU B 1 561 ? 119.298 162.364 169.526 1.00 30.75 ?  561 LEU B CB    1 
ATOM   10066 C  CG    . LEU B 1 561 ? 120.099 161.776 168.363 1.00 32.12 ?  561 LEU B CG    1 
ATOM   10067 C  CD1   . LEU B 1 561 ? 121.431 162.488 168.233 1.00 28.52 ?  561 LEU B CD1   1 
ATOM   10068 C  CD2   . LEU B 1 561 ? 120.300 160.286 168.544 1.00 29.41 ?  561 LEU B CD2   1 
ATOM   10069 N  N     . LYS B 1 562 ? 116.976 164.140 168.229 1.00 30.80 ?  562 LYS B N     1 
ATOM   10070 C  CA    . LYS B 1 562 ? 116.162 164.529 167.082 1.00 32.43 ?  562 LYS B CA    1 
ATOM   10071 C  C     . LYS B 1 562 ? 116.328 166.009 166.769 1.00 37.34 ?  562 LYS B C     1 
ATOM   10072 O  O     . LYS B 1 562 ? 116.477 166.393 165.602 1.00 41.07 ?  562 LYS B O     1 
ATOM   10073 C  CB    . LYS B 1 562 ? 114.695 164.197 167.359 1.00 30.73 ?  562 LYS B CB    1 
ATOM   10074 C  CG    . LYS B 1 562 ? 113.722 164.689 166.308 1.00 31.43 ?  562 LYS B CG    1 
ATOM   10075 C  CD    . LYS B 1 562 ? 112.294 164.421 166.746 1.00 29.50 ?  562 LYS B CD    1 
ATOM   10076 C  CE    . LYS B 1 562 ? 111.302 164.722 165.641 1.00 35.36 ?  562 LYS B CE    1 
ATOM   10077 N  NZ    . LYS B 1 562 ? 109.994 164.061 165.896 1.00 39.56 1  562 LYS B NZ    1 
ATOM   10078 N  N     . ALA B 1 563 ? 116.319 166.854 167.802 1.00 33.87 ?  563 ALA B N     1 
ATOM   10079 C  CA    . ALA B 1 563 ? 116.546 168.280 167.592 1.00 30.54 ?  563 ALA B CA    1 
ATOM   10080 C  C     . ALA B 1 563 ? 117.945 168.541 167.045 1.00 33.60 ?  563 ALA B C     1 
ATOM   10081 O  O     . ALA B 1 563 ? 118.126 169.377 166.152 1.00 40.23 ?  563 ALA B O     1 
ATOM   10082 C  CB    . ALA B 1 563 ? 116.328 169.044 168.897 1.00 34.80 ?  563 ALA B CB    1 
ATOM   10083 N  N     . PHE B 1 564 ? 118.946 167.829 167.568 1.00 36.35 ?  564 PHE B N     1 
ATOM   10084 C  CA    . PHE B 1 564 ? 120.316 168.000 167.096 1.00 31.55 ?  564 PHE B CA    1 
ATOM   10085 C  C     . PHE B 1 564 ? 120.451 167.599 165.632 1.00 36.66 ?  564 PHE B C     1 
ATOM   10086 O  O     . PHE B 1 564 ? 121.143 168.270 164.858 1.00 41.78 ?  564 PHE B O     1 
ATOM   10087 C  CB    . PHE B 1 564 ? 121.265 167.180 167.971 1.00 32.48 ?  564 PHE B CB    1 
ATOM   10088 C  CG    . PHE B 1 564 ? 122.713 167.531 167.794 1.00 35.64 ?  564 PHE B CG    1 
ATOM   10089 C  CD1   . PHE B 1 564 ? 123.241 168.669 168.378 1.00 35.29 ?  564 PHE B CD1   1 
ATOM   10090 C  CD2   . PHE B 1 564 ? 123.548 166.717 167.051 1.00 39.70 ?  564 PHE B CD2   1 
ATOM   10091 C  CE1   . PHE B 1 564 ? 124.574 168.988 168.220 1.00 41.01 ?  564 PHE B CE1   1 
ATOM   10092 C  CE2   . PHE B 1 564 ? 124.881 167.032 166.888 1.00 38.51 ?  564 PHE B CE2   1 
ATOM   10093 C  CZ    . PHE B 1 564 ? 125.395 168.170 167.472 1.00 38.19 ?  564 PHE B CZ    1 
ATOM   10094 N  N     . VAL B 1 565 ? 119.799 166.506 165.236 1.00 32.89 ?  565 VAL B N     1 
ATOM   10095 C  CA    . VAL B 1 565 ? 119.867 166.052 163.851 1.00 29.38 ?  565 VAL B CA    1 
ATOM   10096 C  C     . VAL B 1 565 ? 119.126 167.017 162.936 1.00 35.25 ?  565 VAL B C     1 
ATOM   10097 O  O     . VAL B 1 565 ? 119.571 167.297 161.817 1.00 39.02 ?  565 VAL B O     1 
ATOM   10098 C  CB    . VAL B 1 565 ? 119.321 164.617 163.739 1.00 29.93 ?  565 VAL B CB    1 
ATOM   10099 C  CG1   . VAL B 1 565 ? 118.977 164.277 162.298 1.00 32.07 ?  565 VAL B CG1   1 
ATOM   10100 C  CG2   . VAL B 1 565 ? 120.330 163.631 164.291 1.00 32.11 ?  565 VAL B CG2   1 
ATOM   10101 N  N     . ALA B 1 566 ? 117.990 167.546 163.395 1.00 36.92 ?  566 ALA B N     1 
ATOM   10102 C  CA    . ALA B 1 566 ? 117.274 168.540 162.602 1.00 34.67 ?  566 ALA B CA    1 
ATOM   10103 C  C     . ALA B 1 566 ? 118.110 169.798 162.414 1.00 37.50 ?  566 ALA B C     1 
ATOM   10104 O  O     . ALA B 1 566 ? 118.105 170.403 161.335 1.00 43.33 ?  566 ALA B O     1 
ATOM   10105 C  CB    . ALA B 1 566 ? 115.939 168.877 163.263 1.00 34.64 ?  566 ALA B CB    1 
ATOM   10106 N  N     . GLU B 1 567 ? 118.835 170.211 163.454 1.00 38.02 ?  567 GLU B N     1 
ATOM   10107 C  CA    . GLU B 1 567 ? 119.633 171.428 163.366 1.00 37.40 ?  567 GLU B CA    1 
ATOM   10108 C  C     . GLU B 1 567 ? 120.866 171.231 162.491 1.00 42.54 ?  567 GLU B C     1 
ATOM   10109 O  O     . GLU B 1 567 ? 121.171 172.071 161.637 1.00 50.47 ?  567 GLU B O     1 
ATOM   10110 C  CB    . GLU B 1 567 ? 120.041 171.881 164.767 1.00 39.50 ?  567 GLU B CB    1 
ATOM   10111 C  CG    . GLU B 1 567 ? 120.796 173.195 164.798 1.00 42.29 ?  567 GLU B CG    1 
ATOM   10112 C  CD    . GLU B 1 567 ? 121.346 173.511 166.175 1.00 49.53 ?  567 GLU B CD    1 
ATOM   10113 O  OE1   . GLU B 1 567 ? 120.882 172.894 167.156 1.00 50.64 ?  567 GLU B OE1   1 
ATOM   10114 O  OE2   . GLU B 1 567 ? 122.238 174.378 166.276 1.00 46.30 -1 567 GLU B OE2   1 
ATOM   10115 N  N     . HIS B 1 568 ? 121.586 170.125 162.682 1.00 44.69 ?  568 HIS B N     1 
ATOM   10116 C  CA    . HIS B 1 568 ? 122.904 169.957 162.088 1.00 40.43 ?  568 HIS B CA    1 
ATOM   10117 C  C     . HIS B 1 568 ? 122.955 168.925 160.973 1.00 35.70 ?  568 HIS B C     1 
ATOM   10118 O  O     . HIS B 1 568 ? 123.968 168.853 160.269 1.00 44.65 ?  568 HIS B O     1 
ATOM   10119 C  CB    . HIS B 1 568 ? 123.923 169.574 163.169 1.00 39.32 ?  568 HIS B CB    1 
ATOM   10120 C  CG    . HIS B 1 568 ? 124.188 170.663 164.159 1.00 39.80 ?  568 HIS B CG    1 
ATOM   10121 N  ND1   . HIS B 1 568 ? 123.789 170.585 165.476 1.00 41.70 ?  568 HIS B ND1   1 
ATOM   10122 C  CD2   . HIS B 1 568 ? 124.798 171.863 164.023 1.00 40.68 ?  568 HIS B CD2   1 
ATOM   10123 C  CE1   . HIS B 1 568 ? 124.151 171.685 166.111 1.00 41.70 ?  568 HIS B CE1   1 
ATOM   10124 N  NE2   . HIS B 1 568 ? 124.766 172.477 165.251 1.00 46.63 ?  568 HIS B NE2   1 
ATOM   10125 N  N     . GLY B 1 569 ? 121.913 168.134 160.791 1.00 30.82 ?  569 GLY B N     1 
ATOM   10126 C  CA    . GLY B 1 569 ? 121.925 167.135 159.748 1.00 29.68 ?  569 GLY B CA    1 
ATOM   10127 C  C     . GLY B 1 569 ? 122.584 165.845 160.182 1.00 30.05 ?  569 GLY B C     1 
ATOM   10128 O  O     . GLY B 1 569 ? 122.931 165.628 161.346 1.00 38.28 ?  569 GLY B O     1 
ATOM   10129 N  N     . MET B 1 570 ? 122.751 164.963 159.204 1.00 26.75 ?  570 MET B N     1 
ATOM   10130 C  CA    . MET B 1 570 ? 123.266 163.622 159.433 1.00 22.89 ?  570 MET B CA    1 
ATOM   10131 C  C     . MET B 1 570 ? 124.305 163.324 158.364 1.00 24.69 ?  570 MET B C     1 
ATOM   10132 O  O     . MET B 1 570 ? 124.037 163.507 157.173 1.00 30.73 ?  570 MET B O     1 
ATOM   10133 C  CB    . MET B 1 570 ? 122.119 162.609 159.401 1.00 31.01 ?  570 MET B CB    1 
ATOM   10134 C  CG    . MET B 1 570 ? 121.591 162.230 160.776 1.00 24.56 ?  570 MET B CG    1 
ATOM   10135 S  SD    . MET B 1 570 ? 121.087 160.512 160.912 1.00 46.73 ?  570 MET B SD    1 
ATOM   10136 C  CE    . MET B 1 570 ? 122.657 159.692 161.008 1.00 26.89 ?  570 MET B CE    1 
ATOM   10137 N  N     . TYR B 1 571 ? 125.492 162.883 158.786 1.00 21.99 ?  571 TYR B N     1 
ATOM   10138 C  CA    . TYR B 1 571 ? 126.592 162.721 157.842 1.00 13.75 ?  571 TYR B CA    1 
ATOM   10139 C  C     . TYR B 1 571 ? 126.496 161.433 157.036 1.00 22.97 ?  571 TYR B C     1 
ATOM   10140 O  O     . TYR B 1 571 ? 126.894 161.411 155.868 1.00 21.03 ?  571 TYR B O     1 
ATOM   10141 C  CB    . TYR B 1 571 ? 127.933 162.769 158.573 1.00 18.76 ?  571 TYR B CB    1 
ATOM   10142 C  CG    . TYR B 1 571 ? 129.124 162.832 157.644 1.00 21.18 ?  571 TYR B CG    1 
ATOM   10143 C  CD1   . TYR B 1 571 ? 129.469 164.016 157.005 1.00 23.79 ?  571 TYR B CD1   1 
ATOM   10144 C  CD2   . TYR B 1 571 ? 129.901 161.708 157.402 1.00 21.32 ?  571 TYR B CD2   1 
ATOM   10145 C  CE1   . TYR B 1 571 ? 130.553 164.076 156.154 1.00 22.28 ?  571 TYR B CE1   1 
ATOM   10146 C  CE2   . TYR B 1 571 ? 130.985 161.760 156.554 1.00 23.34 ?  571 TYR B CE2   1 
ATOM   10147 C  CZ    . TYR B 1 571 ? 131.308 162.946 155.934 1.00 28.65 ?  571 TYR B CZ    1 
ATOM   10148 O  OH    . TYR B 1 571 ? 132.390 162.999 155.088 1.00 30.16 ?  571 TYR B OH    1 
ATOM   10149 N  N     . HIS B 1 572 ? 125.980 160.362 157.630 1.00 25.77 ?  572 HIS B N     1 
ATOM   10150 C  CA    . HIS B 1 572 ? 125.909 159.060 156.981 1.00 11.39 ?  572 HIS B CA    1 
ATOM   10151 C  C     . HIS B 1 572 ? 124.464 158.726 156.649 1.00 16.85 ?  572 HIS B C     1 
ATOM   10152 O  O     . HIS B 1 572 ? 123.594 158.782 157.524 1.00 31.90 ?  572 HIS B O     1 
ATOM   10153 C  CB    . HIS B 1 572 ? 126.507 157.964 157.867 1.00 12.19 ?  572 HIS B CB    1 
ATOM   10154 C  CG    . HIS B 1 572 ? 127.835 158.316 158.457 1.00 9.40  ?  572 HIS B CG    1 
ATOM   10155 N  ND1   . HIS B 1 572 ? 127.968 158.930 159.683 1.00 15.89 ?  572 HIS B ND1   1 
ATOM   10156 C  CD2   . HIS B 1 572 ? 129.093 158.133 157.992 1.00 13.40 ?  572 HIS B CD2   1 
ATOM   10157 C  CE1   . HIS B 1 572 ? 129.248 159.114 159.947 1.00 14.22 ?  572 HIS B CE1   1 
ATOM   10158 N  NE2   . HIS B 1 572 ? 129.951 158.640 158.936 1.00 24.57 ?  572 HIS B NE2   1 
ATOM   10159 N  N     . SER B 1 573 ? 124.213 158.384 155.385 1.00 10.81 ?  573 SER B N     1 
ATOM   10160 C  CA    . SER B 1 573 ? 122.892 157.897 155.005 1.00 8.56  ?  573 SER B CA    1 
ATOM   10161 C  C     . SER B 1 573 ? 122.576 156.590 155.713 1.00 17.12 ?  573 SER B C     1 
ATOM   10162 O  O     . SER B 1 573 ? 121.436 156.354 156.126 1.00 29.36 ?  573 SER B O     1 
ATOM   10163 C  CB    . SER B 1 573 ? 122.813 157.715 153.491 1.00 13.78 ?  573 SER B CB    1 
ATOM   10164 O  OG    . SER B 1 573 ? 123.998 157.125 152.994 1.00 25.31 ?  573 SER B OG    1 
ATOM   10165 N  N     . TYR B 1 574 ? 123.576 155.728 155.856 1.00 14.91 ?  574 TYR B N     1 
ATOM   10166 C  CA    . TYR B 1 574 ? 123.436 154.442 156.515 1.00 0.00  ?  574 TYR B CA    1 
ATOM   10167 C  C     . TYR B 1 574 ? 124.612 154.251 157.456 1.00 10.00 ?  574 TYR B C     1 
ATOM   10168 O  O     . TYR B 1 574 ? 125.743 154.621 157.129 1.00 19.34 ?  574 TYR B O     1 
ATOM   10169 C  CB    . TYR B 1 574 ? 123.370 153.311 155.490 1.00 10.33 ?  574 TYR B CB    1 
ATOM   10170 C  CG    . TYR B 1 574 ? 122.322 153.538 154.427 1.00 0.00  ?  574 TYR B CG    1 
ATOM   10171 C  CD1   . TYR B 1 574 ? 121.019 153.098 154.606 1.00 3.61  ?  574 TYR B CD1   1 
ATOM   10172 C  CD2   . TYR B 1 574 ? 122.630 154.207 153.250 1.00 3.57  ?  574 TYR B CD2   1 
ATOM   10173 C  CE1   . TYR B 1 574 ? 120.059 153.309 153.643 1.00 5.96  ?  574 TYR B CE1   1 
ATOM   10174 C  CE2   . TYR B 1 574 ? 121.674 154.426 152.283 1.00 10.55 ?  574 TYR B CE2   1 
ATOM   10175 C  CZ    . TYR B 1 574 ? 120.391 153.971 152.484 1.00 2.73  ?  574 TYR B CZ    1 
ATOM   10176 O  OH    . TYR B 1 574 ? 119.433 154.180 151.524 1.00 15.62 ?  574 TYR B OH    1 
ATOM   10177 N  N     . ARG B 1 575 ? 124.343 153.682 158.623 1.00 12.14 ?  575 ARG B N     1 
ATOM   10178 C  CA    . ARG B 1 575 ? 125.351 153.568 159.668 1.00 0.00  ?  575 ARG B CA    1 
ATOM   10179 C  C     . ARG B 1 575 ? 125.576 152.150 160.155 1.00 11.16 ?  575 ARG B C     1 
ATOM   10180 O  O     . ARG B 1 575 ? 126.720 151.759 160.386 1.00 23.55 ?  575 ARG B O     1 
ATOM   10181 C  CB    . ARG B 1 575 ? 124.961 154.437 160.865 1.00 13.58 ?  575 ARG B CB    1 
ATOM   10182 C  CG    . ARG B 1 575 ? 124.912 155.912 160.574 1.00 8.83  ?  575 ARG B CG    1 
ATOM   10183 C  CD    . ARG B 1 575 ? 124.082 156.613 161.618 1.00 11.19 ?  575 ARG B CD    1 
ATOM   10184 N  NE    . ARG B 1 575 ? 122.662 156.335 161.448 1.00 16.96 ?  575 ARG B NE    1 
ATOM   10185 C  CZ    . ARG B 1 575 ? 121.960 155.512 162.213 1.00 11.69 ?  575 ARG B CZ    1 
ATOM   10186 N  NH1   . ARG B 1 575 ? 122.519 154.857 163.216 1.00 11.22 1  575 ARG B NH1   1 
ATOM   10187 N  NH2   . ARG B 1 575 ? 120.665 155.345 161.970 1.00 11.31 ?  575 ARG B NH2   1 
ATOM   10188 N  N     . LEU B 1 576 ? 124.516 151.365 160.318 1.00 21.07 ?  576 LEU B N     1 
ATOM   10189 C  CA    . LEU B 1 576 ? 124.587 150.092 161.017 1.00 12.04 ?  576 LEU B CA    1 
ATOM   10190 C  C     . LEU B 1 576 ? 124.154 148.966 160.093 1.00 4.46  ?  576 LEU B C     1 
ATOM   10191 O  O     . LEU B 1 576 ? 123.077 149.028 159.494 1.00 20.33 ?  576 LEU B O     1 
ATOM   10192 C  CB    . LEU B 1 576 ? 123.705 150.113 162.267 1.00 7.86  ?  576 LEU B CB    1 
ATOM   10193 C  CG    . LEU B 1 576 ? 123.879 151.310 163.203 1.00 7.05  ?  576 LEU B CG    1 
ATOM   10194 C  CD1   . LEU B 1 576 ? 122.840 151.278 164.306 1.00 12.34 ?  576 LEU B CD1   1 
ATOM   10195 C  CD2   . LEU B 1 576 ? 125.276 151.332 163.787 1.00 11.05 ?  576 LEU B CD2   1 
ATOM   10196 N  N     . CYS B 1 577 ? 125.000 147.947 159.975 1.00 10.65 ?  577 CYS B N     1 
ATOM   10197 C  CA    . CYS B 1 577 ? 124.642 146.705 159.307 1.00 7.20  ?  577 CYS B CA    1 
ATOM   10198 C  C     . CYS B 1 577 ? 125.438 145.589 159.961 1.00 21.29 ?  577 CYS B C     1 
ATOM   10199 O  O     . CYS B 1 577 ? 126.645 145.731 160.174 1.00 26.91 ?  577 CYS B O     1 
ATOM   10200 C  CB    . CYS B 1 577 ? 124.911 146.769 157.796 1.00 4.23  ?  577 CYS B CB    1 
ATOM   10201 S  SG    . CYS B 1 577 ? 126.627 146.560 157.265 1.00 34.79 ?  577 CYS B SG    1 
ATOM   10202 N  N     . ILE B 1 578 ? 124.765 144.494 160.293 1.00 15.00 ?  578 ILE B N     1 
ATOM   10203 C  CA    . ILE B 1 578 ? 125.375 143.395 161.028 1.00 12.69 ?  578 ILE B CA    1 
ATOM   10204 C  C     . ILE B 1 578 ? 125.795 142.341 160.010 1.00 5.09  ?  578 ILE B C     1 
ATOM   10205 O  O     . ILE B 1 578 ? 124.988 141.513 159.581 1.00 20.00 ?  578 ILE B O     1 
ATOM   10206 C  CB    . ILE B 1 578 ? 124.432 142.833 162.093 1.00 10.95 ?  578 ILE B CB    1 
ATOM   10207 C  CG1   . ILE B 1 578 ? 123.938 143.960 163.001 1.00 2.62  ?  578 ILE B CG1   1 
ATOM   10208 C  CG2   . ILE B 1 578 ? 125.137 141.783 162.924 1.00 8.83  ?  578 ILE B CG2   1 
ATOM   10209 C  CD1   . ILE B 1 578 ? 123.174 143.481 164.204 1.00 9.60  ?  578 ILE B CD1   1 
ATOM   10210 N  N     . ALA B 1 579 ? 127.065 142.381 159.621 1.00 14.77 ?  579 ALA B N     1 
ATOM   10211 C  CA    . ALA B 1 579 ? 127.661 141.425 158.705 1.00 4.76  ?  579 ALA B CA    1 
ATOM   10212 C  C     . ALA B 1 579 ? 127.950 140.105 159.416 1.00 18.65 ?  579 ALA B C     1 
ATOM   10213 O  O     . ALA B 1 579 ? 127.964 140.045 160.646 1.00 31.68 ?  579 ALA B O     1 
ATOM   10214 C  CB    . ALA B 1 579 ? 128.942 142.006 158.117 1.00 9.76  ?  579 ALA B CB    1 
ATOM   10215 N  N     . PRO B 1 580 ? 128.159 139.020 158.661 1.00 25.93 ?  580 PRO B N     1 
ATOM   10216 C  CA    . PRO B 1 580 ? 128.440 137.726 159.311 1.00 23.57 ?  580 PRO B CA    1 
ATOM   10217 C  C     . PRO B 1 580 ? 129.690 137.712 160.180 1.00 31.60 ?  580 PRO B C     1 
ATOM   10218 O  O     . PRO B 1 580 ? 129.715 136.977 161.175 1.00 37.76 ?  580 PRO B O     1 
ATOM   10219 C  CB    . PRO B 1 580 ? 128.568 136.756 158.125 1.00 23.45 ?  580 PRO B CB    1 
ATOM   10220 C  CG    . PRO B 1 580 ? 128.679 137.607 156.909 1.00 23.60 ?  580 PRO B CG    1 
ATOM   10221 C  CD    . PRO B 1 580 ? 127.956 138.868 157.212 1.00 20.84 ?  580 PRO B CD    1 
ATOM   10222 N  N     . THR B 1 581 ? 130.719 138.492 159.846 1.00 24.16 ?  581 THR B N     1 
ATOM   10223 C  CA    . THR B 1 581 ? 131.977 138.541 160.603 1.00 33.88 ?  581 THR B CA    1 
ATOM   10224 C  C     . THR B 1 581 ? 132.581 137.143 160.755 1.00 32.21 ?  581 THR B C     1 
ATOM   10225 O  O     . THR B 1 581 ? 132.707 136.596 161.849 1.00 34.51 ?  581 THR B O     1 
ATOM   10226 C  CB    . THR B 1 581 ? 131.793 139.194 161.979 1.00 28.70 ?  581 THR B CB    1 
ATOM   10227 O  OG1   . THR B 1 581 ? 131.314 138.220 162.914 1.00 24.16 ?  581 THR B OG1   1 
ATOM   10228 C  CG2   . THR B 1 581 ? 130.825 140.357 161.907 1.00 31.20 ?  581 THR B CG2   1 
ATOM   10229 N  N     . GLY B 1 582 ? 132.951 136.579 159.609 1.00 31.94 ?  582 GLY B N     1 
ATOM   10230 C  CA    . GLY B 1 582 ? 133.380 135.198 159.550 1.00 34.72 ?  582 GLY B CA    1 
ATOM   10231 C  C     . GLY B 1 582 ? 134.672 134.872 160.274 1.00 37.48 ?  582 GLY B C     1 
ATOM   10232 O  O     . GLY B 1 582 ? 134.657 134.138 161.266 1.00 41.71 ?  582 GLY B O     1 
ATOM   10233 N  N     . SER B 1 583 ? 135.795 135.408 159.798 1.00 37.76 ?  583 SER B N     1 
ATOM   10234 C  CA    . SER B 1 583 ? 137.098 135.001 160.311 1.00 42.54 ?  583 SER B CA    1 
ATOM   10235 C  C     . SER B 1 583 ? 137.623 135.905 161.417 1.00 39.80 ?  583 SER B C     1 
ATOM   10236 O  O     . SER B 1 583 ? 138.437 135.456 162.233 1.00 39.77 ?  583 SER B O     1 
ATOM   10237 C  CB    . SER B 1 583 ? 138.120 134.949 159.173 1.00 47.40 ?  583 SER B CB    1 
ATOM   10238 O  OG    . SER B 1 583 ? 137.976 133.762 158.414 1.00 49.21 ?  583 SER B OG    1 
ATOM   10239 N  N     . ILE B 1 584 ? 137.188 137.166 161.468 1.00 33.05 ?  584 ILE B N     1 
ATOM   10240 C  CA    . ILE B 1 584 ? 137.616 138.063 162.535 1.00 28.91 ?  584 ILE B CA    1 
ATOM   10241 C  C     . ILE B 1 584 ? 137.034 137.689 163.888 1.00 31.88 ?  584 ILE B C     1 
ATOM   10242 O  O     . ILE B 1 584 ? 137.497 138.201 164.912 1.00 36.84 ?  584 ILE B O     1 
ATOM   10243 C  CB    . ILE B 1 584 ? 137.247 139.526 162.211 1.00 36.81 ?  584 ILE B CB    1 
ATOM   10244 C  CG1   . ILE B 1 584 ? 135.760 139.639 161.864 1.00 34.43 ?  584 ILE B CG1   1 
ATOM   10245 C  CG2   . ILE B 1 584 ? 138.123 140.066 161.094 1.00 32.57 ?  584 ILE B CG2   1 
ATOM   10246 C  CD1   . ILE B 1 584 ? 135.263 141.063 161.759 1.00 33.31 ?  584 ILE B CD1   1 
ATOM   10247 N  N     . SER B 1 585 ? 136.026 136.814 163.919 1.00 31.76 ?  585 SER B N     1 
ATOM   10248 C  CA    . SER B 1 585 ? 135.451 136.397 165.192 1.00 29.12 ?  585 SER B CA    1 
ATOM   10249 C  C     . SER B 1 585 ? 136.419 135.534 165.988 1.00 28.92 ?  585 SER B C     1 
ATOM   10250 O  O     . SER B 1 585 ? 136.447 135.616 167.220 1.00 29.13 ?  585 SER B O     1 
ATOM   10251 C  CB    . SER B 1 585 ? 134.139 135.651 164.956 1.00 32.20 ?  585 SER B CB    1 
ATOM   10252 O  OG    . SER B 1 585 ? 134.329 134.542 164.096 1.00 36.22 ?  585 SER B OG    1 
ATOM   10253 N  N     . TYR B 1 586 ? 137.210 134.698 165.310 1.00 35.47 ?  586 TYR B N     1 
ATOM   10254 C  CA    . TYR B 1 586 ? 138.209 133.898 166.011 1.00 36.44 ?  586 TYR B CA    1 
ATOM   10255 C  C     . TYR B 1 586 ? 139.264 134.782 166.658 1.00 34.72 ?  586 TYR B C     1 
ATOM   10256 O  O     . TYR B 1 586 ? 139.633 134.574 167.819 1.00 41.06 ?  586 TYR B O     1 
ATOM   10257 C  CB    . TYR B 1 586 ? 138.872 132.913 165.049 1.00 32.67 ?  586 TYR B CB    1 
ATOM   10258 C  CG    . TYR B 1 586 ? 137.929 131.928 164.405 1.00 33.53 ?  586 TYR B CG    1 
ATOM   10259 C  CD1   . TYR B 1 586 ? 137.364 132.189 163.165 1.00 36.90 ?  586 TYR B CD1   1 
ATOM   10260 C  CD2   . TYR B 1 586 ? 137.607 130.735 165.032 1.00 35.45 ?  586 TYR B CD2   1 
ATOM   10261 C  CE1   . TYR B 1 586 ? 136.504 131.290 162.569 1.00 39.70 ?  586 TYR B CE1   1 
ATOM   10262 C  CE2   . TYR B 1 586 ? 136.748 129.829 164.444 1.00 37.85 ?  586 TYR B CE2   1 
ATOM   10263 C  CZ    . TYR B 1 586 ? 136.199 130.112 163.214 1.00 39.59 ?  586 TYR B CZ    1 
ATOM   10264 O  OH    . TYR B 1 586 ? 135.342 129.213 162.625 1.00 44.24 ?  586 TYR B OH    1 
ATOM   10265 N  N     . VAL B 1 587 ? 139.754 135.781 165.921 1.00 29.79 ?  587 VAL B N     1 
ATOM   10266 C  CA    . VAL B 1 587 ? 140.793 136.667 166.440 1.00 24.81 ?  587 VAL B CA    1 
ATOM   10267 C  C     . VAL B 1 587 ? 140.288 137.421 167.663 1.00 30.49 ?  587 VAL B C     1 
ATOM   10268 O  O     . VAL B 1 587 ? 141.029 137.637 168.629 1.00 39.87 ?  587 VAL B O     1 
ATOM   10269 C  CB    . VAL B 1 587 ? 141.265 137.630 165.336 1.00 31.15 ?  587 VAL B CB    1 
ATOM   10270 C  CG1   . VAL B 1 587 ? 142.291 138.605 165.879 1.00 34.30 ?  587 VAL B CG1   1 
ATOM   10271 C  CG2   . VAL B 1 587 ? 141.832 136.850 164.163 1.00 31.54 ?  587 VAL B CG2   1 
ATOM   10272 N  N     . GLN B 1 588 ? 139.022 137.824 167.645 1.00 34.77 ?  588 GLN B N     1 
ATOM   10273 C  CA    . GLN B 1 588 ? 138.431 138.566 168.748 1.00 29.40 ?  588 GLN B CA    1 
ATOM   10274 C  C     . GLN B 1 588 ? 137.932 137.668 169.868 1.00 34.28 ?  588 GLN B C     1 
ATOM   10275 O  O     . GLN B 1 588 ? 137.439 138.188 170.875 1.00 36.74 ?  588 GLN B O     1 
ATOM   10276 C  CB    . GLN B 1 588 ? 137.280 139.433 168.236 1.00 22.63 ?  588 GLN B CB    1 
ATOM   10277 C  CG    . GLN B 1 588 ? 137.728 140.656 167.466 1.00 24.46 ?  588 GLN B CG    1 
ATOM   10278 C  CD    . GLN B 1 588 ? 137.832 141.882 168.344 1.00 29.18 ?  588 GLN B CD    1 
ATOM   10279 O  OE1   . GLN B 1 588 ? 136.989 142.111 169.209 1.00 29.62 ?  588 GLN B OE1   1 
ATOM   10280 N  NE2   . GLN B 1 588 ? 138.869 142.680 168.127 1.00 33.47 ?  588 GLN B NE2   1 
ATOM   10281 N  N     . SER B 1 589 ? 138.055 136.350 169.722 1.00 34.31 ?  589 SER B N     1 
ATOM   10282 C  CA    . SER B 1 589 ? 137.506 135.386 170.674 1.00 28.15 ?  589 SER B CA    1 
ATOM   10283 C  C     . SER B 1 589 ? 136.029 135.680 170.924 1.00 31.62 ?  589 SER B C     1 
ATOM   10284 O  O     . SER B 1 589 ? 135.588 135.932 172.046 1.00 35.30 ?  589 SER B O     1 
ATOM   10285 C  CB    . SER B 1 589 ? 138.305 135.384 171.978 1.00 36.32 ?  589 SER B CB    1 
ATOM   10286 O  OG    . SER B 1 589 ? 138.137 134.165 172.680 1.00 45.26 ?  589 SER B OG    1 
ATOM   10287 N  N     . SER B 1 590 ? 135.266 135.659 169.835 1.00 30.54 ?  590 SER B N     1 
ATOM   10288 C  CA    . SER B 1 590 ? 133.876 136.076 169.856 1.00 23.07 ?  590 SER B CA    1 
ATOM   10289 C  C     . SER B 1 590 ? 133.043 135.128 169.010 1.00 28.21 ?  590 SER B C     1 
ATOM   10290 O  O     . SER B 1 590 ? 133.548 134.493 168.080 1.00 36.37 ?  590 SER B O     1 
ATOM   10291 C  CB    . SER B 1 590 ? 133.722 137.510 169.335 1.00 26.65 ?  590 SER B CB    1 
ATOM   10292 O  OG    . SER B 1 590 ? 133.561 137.526 167.931 1.00 36.42 ?  590 SER B OG    1 
ATOM   10293 N  N     . THR B 1 591 ? 131.762 135.029 169.348 1.00 30.26 ?  591 THR B N     1 
ATOM   10294 C  CA    . THR B 1 591 ? 130.819 134.303 168.510 1.00 27.61 ?  591 THR B CA    1 
ATOM   10295 C  C     . THR B 1 591 ? 130.458 135.152 167.299 1.00 30.48 ?  591 THR B C     1 
ATOM   10296 O  O     . THR B 1 591 ? 130.388 136.382 167.382 1.00 25.23 ?  591 THR B O     1 
ATOM   10297 C  CB    . THR B 1 591 ? 129.564 133.932 169.299 1.00 28.23 ?  591 THR B CB    1 
ATOM   10298 O  OG1   . THR B 1 591 ? 128.807 135.112 169.589 1.00 36.89 ?  591 THR B OG1   1 
ATOM   10299 C  CG2   . THR B 1 591 ? 129.946 133.250 170.601 1.00 26.83 ?  591 THR B CG2   1 
ATOM   10300 N  N     . ALA B 1 592 ? 130.238 134.489 166.168 1.00 26.62 ?  592 ALA B N     1 
ATOM   10301 C  CA    . ALA B 1 592 ? 130.077 135.197 164.905 1.00 25.14 ?  592 ALA B CA    1 
ATOM   10302 C  C     . ALA B 1 592 ? 128.781 135.996 164.888 1.00 24.71 ?  592 ALA B C     1 
ATOM   10303 O  O     . ALA B 1 592 ? 127.690 135.434 165.032 1.00 32.62 ?  592 ALA B O     1 
ATOM   10304 C  CB    . ALA B 1 592 ? 130.102 134.209 163.741 1.00 31.49 ?  592 ALA B CB    1 
ATOM   10305 N  N     . SER B 1 593 ? 128.910 137.306 164.711 1.00 27.77 ?  593 SER B N     1 
ATOM   10306 C  CA    . SER B 1 593 ? 127.782 138.219 164.487 1.00 16.57 ?  593 SER B CA    1 
ATOM   10307 C  C     . SER B 1 593 ? 126.815 138.124 165.669 1.00 14.42 ?  593 SER B C     1 
ATOM   10308 O  O     . SER B 1 593 ? 127.220 137.826 166.799 1.00 29.93 ?  593 SER B O     1 
ATOM   10309 C  CB    . SER B 1 593 ? 127.162 137.916 163.137 1.00 28.74 ?  593 SER B CB    1 
ATOM   10310 O  OG    . SER B 1 593 ? 126.077 138.779 162.865 1.00 24.93 ?  593 SER B OG    1 
ATOM   10311 N  N     . VAL B 1 594 ? 125.531 138.377 165.418 1.00 20.91 ?  594 VAL B N     1 
ATOM   10312 C  CA    . VAL B 1 594 ? 124.495 138.211 166.425 1.00 17.98 ?  594 VAL B CA    1 
ATOM   10313 C  C     . VAL B 1 594 ? 123.850 136.833 166.345 1.00 15.70 ?  594 VAL B C     1 
ATOM   10314 O  O     . VAL B 1 594 ? 122.896 136.553 167.075 1.00 25.92 ?  594 VAL B O     1 
ATOM   10315 C  CB    . VAL B 1 594 ? 123.434 139.318 166.316 1.00 23.80 ?  594 VAL B CB    1 
ATOM   10316 C  CG1   . VAL B 1 594 ? 124.010 140.648 166.770 1.00 14.10 ?  594 VAL B CG1   1 
ATOM   10317 C  CG2   . VAL B 1 594 ? 122.911 139.415 164.895 1.00 22.03 ?  594 VAL B CG2   1 
ATOM   10318 N  N     . MET B 1 595 ? 124.353 135.965 165.472 1.00 25.63 ?  595 MET B N     1 
ATOM   10319 C  CA    . MET B 1 595 ? 123.810 134.626 165.339 1.00 19.42 ?  595 MET B CA    1 
ATOM   10320 C  C     . MET B 1 595 ? 124.187 133.773 166.548 1.00 24.87 ?  595 MET B C     1 
ATOM   10321 O  O     . MET B 1 595 ? 125.219 134.000 167.184 1.00 32.63 ?  595 MET B O     1 
ATOM   10322 C  CB    . MET B 1 595 ? 124.333 133.964 164.067 1.00 22.58 ?  595 MET B CB    1 
ATOM   10323 C  CG    . MET B 1 595 ? 123.928 134.620 162.749 1.00 24.99 ?  595 MET B CG    1 
ATOM   10324 S  SD    . MET B 1 595 ? 122.249 134.293 162.168 1.00 37.28 ?  595 MET B SD    1 
ATOM   10325 C  CE    . MET B 1 595 ? 121.265 135.383 163.188 1.00 16.63 ?  595 MET B CE    1 
ATOM   10326 N  N     . PRO B 1 596 ? 123.365 132.782 166.885 1.00 32.04 ?  596 PRO B N     1 
ATOM   10327 C  CA    . PRO B 1 596 ? 123.771 131.806 167.898 1.00 20.66 ?  596 PRO B CA    1 
ATOM   10328 C  C     . PRO B 1 596 ? 124.806 130.842 167.340 1.00 31.12 ?  596 PRO B C     1 
ATOM   10329 O  O     . PRO B 1 596 ? 124.966 130.685 166.127 1.00 37.74 ?  596 PRO B O     1 
ATOM   10330 C  CB    . PRO B 1 596 ? 122.465 131.091 168.246 1.00 22.35 ?  596 PRO B CB    1 
ATOM   10331 C  CG    . PRO B 1 596 ? 121.644 131.205 167.014 1.00 27.79 ?  596 PRO B CG    1 
ATOM   10332 C  CD    . PRO B 1 596 ? 122.009 132.517 166.372 1.00 32.26 ?  596 PRO B CD    1 
ATOM   10333 N  N     . ILE B 1 597 ? 125.523 130.190 168.255 1.00 28.45 ?  597 ILE B N     1 
ATOM   10334 C  CA    . ILE B 1 597 ? 126.630 129.329 167.860 1.00 28.60 ?  597 ILE B CA    1 
ATOM   10335 C  C     . ILE B 1 597 ? 126.099 128.071 167.188 1.00 37.55 ?  597 ILE B C     1 
ATOM   10336 O  O     . ILE B 1 597 ? 125.083 127.498 167.602 1.00 40.72 ?  597 ILE B O     1 
ATOM   10337 C  CB    . ILE B 1 597 ? 127.507 128.986 169.077 1.00 33.65 ?  597 ILE B CB    1 
ATOM   10338 C  CG1   . ILE B 1 597 ? 126.687 128.268 170.149 1.00 34.53 ?  597 ILE B CG1   1 
ATOM   10339 C  CG2   . ILE B 1 597 ? 128.129 130.244 169.645 1.00 31.62 ?  597 ILE B CG2   1 
ATOM   10340 C  CD1   . ILE B 1 597 ? 127.497 127.339 171.011 1.00 33.96 ?  597 ILE B CD1   1 
ATOM   10341 N  N     . MET B 1 598 ? 126.784 127.644 166.126 1.00 44.87 ?  598 MET B N     1 
ATOM   10342 C  CA    . MET B 1 598 ? 126.411 126.406 165.452 1.00 41.70 ?  598 MET B CA    1 
ATOM   10343 C  C     . MET B 1 598 ? 126.805 125.192 166.282 1.00 38.38 ?  598 MET B C     1 
ATOM   10344 O  O     . MET B 1 598 ? 126.018 124.253 166.443 1.00 46.97 ?  598 MET B O     1 
ATOM   10345 C  CB    . MET B 1 598 ? 127.062 126.348 164.071 1.00 40.80 ?  598 MET B CB    1 
ATOM   10346 C  CG    . MET B 1 598 ? 126.710 127.513 163.171 1.00 39.04 ?  598 MET B CG    1 
ATOM   10347 S  SD    . MET B 1 598 ? 127.044 127.167 161.435 1.00 59.89 ?  598 MET B SD    1 
ATOM   10348 C  CE    . MET B 1 598 ? 128.471 128.211 161.159 1.00 42.97 ?  598 MET B CE    1 
ATOM   10349 N  N     . GLU B 1 599 ? 128.024 125.194 166.817 1.00 42.37 ?  599 GLU B N     1 
ATOM   10350 C  CA    . GLU B 1 599 ? 128.541 124.100 167.624 1.00 42.26 ?  599 GLU B CA    1 
ATOM   10351 C  C     . GLU B 1 599 ? 129.141 124.657 168.903 1.00 40.25 ?  599 GLU B C     1 
ATOM   10352 O  O     . GLU B 1 599 ? 129.655 125.778 168.928 1.00 46.11 ?  599 GLU B O     1 
ATOM   10353 C  CB    . GLU B 1 599 ? 129.605 123.290 166.870 1.00 44.07 ?  599 GLU B CB    1 
ATOM   10354 C  CG    . GLU B 1 599 ? 129.503 123.369 165.357 1.00 43.73 ?  599 GLU B CG    1 
ATOM   10355 C  CD    . GLU B 1 599 ? 130.671 122.703 164.660 1.00 50.12 ?  599 GLU B CD    1 
ATOM   10356 O  OE1   . GLU B 1 599 ? 131.094 121.618 165.110 1.00 49.97 ?  599 GLU B OE1   1 
ATOM   10357 O  OE2   . GLU B 1 599 ? 131.167 123.266 163.661 1.00 48.55 -1 599 GLU B OE2   1 
ATOM   10358 N  N     . ARG B 1 600 ? 129.071 123.867 169.974 1.00 43.29 ?  600 ARG B N     1 
ATOM   10359 C  CA    . ARG B 1 600 ? 129.692 124.279 171.229 1.00 35.78 ?  600 ARG B CA    1 
ATOM   10360 C  C     . ARG B 1 600 ? 131.210 124.246 171.122 1.00 37.20 ?  600 ARG B C     1 
ATOM   10361 O  O     . ARG B 1 600 ? 131.895 125.179 171.558 1.00 41.36 ?  600 ARG B O     1 
ATOM   10362 C  CB    . ARG B 1 600 ? 129.211 123.392 172.373 1.00 38.87 ?  600 ARG B CB    1 
ATOM   10363 C  CG    . ARG B 1 600 ? 127.891 123.832 172.961 1.00 39.64 ?  600 ARG B CG    1 
ATOM   10364 C  CD    . ARG B 1 600 ? 127.611 123.125 174.265 1.00 36.65 ?  600 ARG B CD    1 
ATOM   10365 N  NE    . ARG B 1 600 ? 126.296 123.456 174.798 1.00 36.86 ?  600 ARG B NE    1 
ATOM   10366 C  CZ    . ARG B 1 600 ? 125.167 122.873 174.420 1.00 40.58 ?  600 ARG B CZ    1 
ATOM   10367 N  NH1   . ARG B 1 600 ? 125.155 121.929 173.494 1.00 39.73 1  600 ARG B NH1   1 
ATOM   10368 N  NH2   . ARG B 1 600 ? 124.024 123.246 174.985 1.00 41.50 ?  600 ARG B NH2   1 
ATOM   10369 N  N     . ILE B 1 601 ? 131.754 123.178 170.548 1.00 49.15 ?  601 ILE B N     1 
ATOM   10370 C  CA    . ILE B 1 601 ? 133.183 123.052 170.300 1.00 43.12 ?  601 ILE B CA    1 
ATOM   10371 C  C     . ILE B 1 601 ? 133.379 122.810 168.813 1.00 43.56 ?  601 ILE B C     1 
ATOM   10372 O  O     . ILE B 1 601 ? 132.775 121.896 168.241 1.00 46.37 ?  601 ILE B O     1 
ATOM   10373 C  CB    . ILE B 1 601 ? 133.811 121.922 171.134 1.00 40.56 ?  601 ILE B CB    1 
ATOM   10374 C  CG1   . ILE B 1 601 ? 133.522 122.147 172.619 1.00 42.38 ?  601 ILE B CG1   1 
ATOM   10375 C  CG2   . ILE B 1 601 ? 135.304 121.859 170.885 1.00 41.67 ?  601 ILE B CG2   1 
ATOM   10376 C  CD1   . ILE B 1 601 ? 133.685 120.919 173.472 1.00 44.89 ?  601 ILE B CD1   1 
ATOM   10377 N  N     . GLU B 1 602 ? 134.219 123.628 168.192 1.00 53.69 ?  602 GLU B N     1 
ATOM   10378 C  CA    . GLU B 1 602 ? 134.383 123.645 166.746 1.00 50.17 ?  602 GLU B CA    1 
ATOM   10379 C  C     . GLU B 1 602 ? 135.529 122.720 166.356 1.00 53.61 ?  602 GLU B C     1 
ATOM   10380 O  O     . GLU B 1 602 ? 136.674 122.940 166.763 1.00 57.39 ?  602 GLU B O     1 
ATOM   10381 C  CB    . GLU B 1 602 ? 134.644 125.071 166.265 1.00 50.44 ?  602 GLU B CB    1 
ATOM   10382 C  CG    . GLU B 1 602 ? 134.307 125.323 164.819 1.00 50.20 ?  602 GLU B CG    1 
ATOM   10383 C  CD    . GLU B 1 602 ? 134.332 126.796 164.472 1.00 56.99 ?  602 GLU B CD    1 
ATOM   10384 O  OE1   . GLU B 1 602 ? 133.527 127.557 165.049 1.00 55.91 ?  602 GLU B OE1   1 
ATOM   10385 O  OE2   . GLU B 1 602 ? 135.159 127.193 163.627 1.00 58.72 -1 602 GLU B OE2   1 
ATOM   10386 N  N     . GLU B 1 603 ? 135.219 121.690 165.573 1.00 56.22 ?  603 GLU B N     1 
ATOM   10387 C  CA    . GLU B 1 603 ? 136.211 120.737 165.093 1.00 55.13 ?  603 GLU B CA    1 
ATOM   10388 C  C     . GLU B 1 603 ? 136.570 121.079 163.652 1.00 57.66 ?  603 GLU B C     1 
ATOM   10389 O  O     . GLU B 1 603 ? 135.717 120.998 162.761 1.00 59.08 ?  603 GLU B O     1 
ATOM   10390 C  CB    . GLU B 1 603 ? 135.687 119.303 165.184 1.00 58.25 ?  603 GLU B CB    1 
ATOM   10391 C  CG    . GLU B 1 603 ? 135.145 118.913 166.548 1.00 60.56 ?  603 GLU B CG    1 
ATOM   10392 C  CD    . GLU B 1 603 ? 133.641 119.083 166.653 1.00 60.85 ?  603 GLU B CD    1 
ATOM   10393 O  OE1   . GLU B 1 603 ? 132.981 119.220 165.601 1.00 54.69 ?  603 GLU B OE1   1 
ATOM   10394 O  OE2   . GLU B 1 603 ? 133.119 119.075 167.788 1.00 59.56 -1 603 GLU B OE2   1 
ATOM   10395 N  N     . ARG B 1 604 ? 137.825 121.459 163.428 1.00 60.93 ?  604 ARG B N     1 
ATOM   10396 C  CA    . ARG B 1 604 ? 138.314 121.826 162.108 1.00 61.64 ?  604 ARG B CA    1 
ATOM   10397 C  C     . ARG B 1 604 ? 139.678 121.201 161.861 1.00 62.36 ?  604 ARG B C     1 
ATOM   10398 O  O     . ARG B 1 604 ? 140.430 120.917 162.796 1.00 61.58 ?  604 ARG B O     1 
ATOM   10399 C  CB    . ARG B 1 604 ? 138.398 123.349 161.943 1.00 61.50 ?  604 ARG B CB    1 
ATOM   10400 C  CG    . ARG B 1 604 ? 137.061 124.056 162.052 1.00 61.72 ?  604 ARG B CG    1 
ATOM   10401 C  CD    . ARG B 1 604 ? 136.378 124.096 160.691 1.00 61.06 ?  604 ARG B CD    1 
ATOM   10402 N  NE    . ARG B 1 604 ? 135.344 125.120 160.611 1.00 64.58 ?  604 ARG B NE    1 
ATOM   10403 C  CZ    . ARG B 1 604 ? 134.186 125.073 161.255 1.00 62.16 ?  604 ARG B CZ    1 
ATOM   10404 N  NH1   . ARG B 1 604 ? 133.832 124.016 161.966 1.00 59.27 1  604 ARG B NH1   1 
ATOM   10405 N  NH2   . ARG B 1 604 ? 133.352 126.105 161.164 1.00 60.26 ?  604 ARG B NH2   1 
ATOM   10406 N  N     . THR B 1 605 ? 139.984 120.990 160.585 1.00 68.88 ?  605 THR B N     1 
ATOM   10407 C  CA    . THR B 1 605 ? 141.249 120.408 160.156 1.00 69.05 ?  605 THR B CA    1 
ATOM   10408 C  C     . THR B 1 605 ? 142.027 121.447 159.363 1.00 68.94 ?  605 THR B C     1 
ATOM   10409 O  O     . THR B 1 605 ? 141.526 121.973 158.362 1.00 68.34 ?  605 THR B O     1 
ATOM   10410 C  CB    . THR B 1 605 ? 141.018 119.155 159.311 1.00 68.77 ?  605 THR B CB    1 
ATOM   10411 O  OG1   . THR B 1 605 ? 140.362 118.155 160.100 1.00 68.65 ?  605 THR B OG1   1 
ATOM   10412 C  CG2   . THR B 1 605 ? 142.341 118.606 158.802 1.00 69.06 ?  605 THR B CG2   1 
ATOM   10413 N  N     . TYR B 1 606 ? 143.244 121.741 159.809 1.00 70.93 ?  606 TYR B N     1 
ATOM   10414 C  CA    . TYR B 1 606 ? 144.142 122.654 159.114 1.00 72.42 ?  606 TYR B CA    1 
ATOM   10415 C  C     . TYR B 1 606 ? 145.396 121.883 158.731 1.00 73.83 ?  606 TYR B C     1 
ATOM   10416 O  O     . TYR B 1 606 ? 146.064 121.311 159.599 1.00 71.71 ?  606 TYR B O     1 
ATOM   10417 C  CB    . TYR B 1 606 ? 144.481 123.863 159.987 1.00 70.45 ?  606 TYR B CB    1 
ATOM   10418 C  CG    . TYR B 1 606 ? 143.281 124.727 160.292 1.00 71.00 ?  606 TYR B CG    1 
ATOM   10419 C  CD1   . TYR B 1 606 ? 142.811 125.648 159.366 1.00 68.19 ?  606 TYR B CD1   1 
ATOM   10420 C  CD2   . TYR B 1 606 ? 142.610 124.614 161.502 1.00 71.01 ?  606 TYR B CD2   1 
ATOM   10421 C  CE1   . TYR B 1 606 ? 141.711 126.436 159.639 1.00 69.99 ?  606 TYR B CE1   1 
ATOM   10422 C  CE2   . TYR B 1 606 ? 141.510 125.396 161.783 1.00 68.85 ?  606 TYR B CE2   1 
ATOM   10423 C  CZ    . TYR B 1 606 ? 141.065 126.306 160.849 1.00 72.54 ?  606 TYR B CZ    1 
ATOM   10424 O  OH    . TYR B 1 606 ? 139.967 127.087 161.127 1.00 74.18 ?  606 TYR B OH    1 
ATOM   10425 N  N     . GLY B 1 607 ? 145.714 121.877 157.441 1.00 79.93 ?  607 GLY B N     1 
ATOM   10426 C  CA    . GLY B 1 607 ? 146.773 121.004 156.966 1.00 79.31 ?  607 GLY B CA    1 
ATOM   10427 C  C     . GLY B 1 607 ? 146.380 119.555 157.175 1.00 79.82 ?  607 GLY B C     1 
ATOM   10428 O  O     . GLY B 1 607 ? 145.273 119.130 156.825 1.00 79.29 ?  607 GLY B O     1 
ATOM   10429 N  N     . ASN B 1 608 ? 147.293 118.779 157.757 1.00 81.39 ?  608 ASN B N     1 
ATOM   10430 C  CA    . ASN B 1 608 ? 147.035 117.382 158.075 1.00 82.54 ?  608 ASN B CA    1 
ATOM   10431 C  C     . ASN B 1 608 ? 146.672 117.176 159.540 1.00 83.77 ?  608 ASN B C     1 
ATOM   10432 O  O     . ASN B 1 608 ? 146.465 116.034 159.963 1.00 83.08 ?  608 ASN B O     1 
ATOM   10433 C  CB    . ASN B 1 608 ? 148.247 116.525 157.705 1.00 83.72 ?  608 ASN B CB    1 
ATOM   10434 C  CG    . ASN B 1 608 ? 148.552 116.556 156.219 1.00 84.36 ?  608 ASN B CG    1 
ATOM   10435 O  OD1   . ASN B 1 608 ? 147.751 117.041 155.420 1.00 82.31 ?  608 ASN B OD1   1 
ATOM   10436 N  ND2   . ASN B 1 608 ? 149.713 116.035 155.841 1.00 83.01 ?  608 ASN B ND2   1 
ATOM   10437 N  N     . SER B 1 609 ? 146.583 118.250 160.319 1.00 76.85 ?  609 SER B N     1 
ATOM   10438 C  CA    . SER B 1 609 ? 146.291 118.171 161.742 1.00 76.36 ?  609 SER B CA    1 
ATOM   10439 C  C     . SER B 1 609 ? 144.922 118.772 162.031 1.00 74.44 ?  609 SER B C     1 
ATOM   10440 O  O     . SER B 1 609 ? 144.576 119.838 161.510 1.00 74.33 ?  609 SER B O     1 
ATOM   10441 C  CB    . SER B 1 609 ? 147.363 118.895 162.562 1.00 73.85 ?  609 SER B CB    1 
ATOM   10442 O  OG    . SER B 1 609 ? 147.386 120.279 162.262 1.00 73.50 ?  609 SER B OG    1 
ATOM   10443 N  N     . LYS B 1 610 ? 144.146 118.081 162.860 1.00 64.40 ?  610 LYS B N     1 
ATOM   10444 C  CA    . LYS B 1 610 ? 142.816 118.531 163.241 1.00 63.80 ?  610 LYS B CA    1 
ATOM   10445 C  C     . LYS B 1 610 ? 142.881 119.386 164.500 1.00 63.31 ?  610 LYS B C     1 
ATOM   10446 O  O     . LYS B 1 610 ? 143.672 119.121 165.410 1.00 64.06 ?  610 LYS B O     1 
ATOM   10447 C  CB    . LYS B 1 610 ? 141.888 117.327 163.433 1.00 64.70 ?  610 LYS B CB    1 
ATOM   10448 C  CG    . LYS B 1 610 ? 141.807 116.769 164.843 1.00 63.25 ?  610 LYS B CG    1 
ATOM   10449 C  CD    . LYS B 1 610 ? 141.245 115.354 164.822 1.00 64.78 ?  610 LYS B CD    1 
ATOM   10450 C  CE    . LYS B 1 610 ? 141.883 114.477 165.888 1.00 64.56 ?  610 LYS B CE    1 
ATOM   10451 N  NZ    . LYS B 1 610 ? 141.424 114.810 167.261 1.00 64.14 1  610 LYS B NZ    1 
ATOM   10452 N  N     . THR B 1 611 ? 142.066 120.437 164.528 1.00 63.68 ?  611 THR B N     1 
ATOM   10453 C  CA    . THR B 1 611 ? 142.068 121.413 165.606 1.00 61.02 ?  611 THR B CA    1 
ATOM   10454 C  C     . THR B 1 611 ? 140.690 121.487 166.247 1.00 56.76 ?  611 THR B C     1 
ATOM   10455 O  O     . THR B 1 611 ? 139.673 121.202 165.607 1.00 60.25 ?  611 THR B O     1 
ATOM   10456 C  CB    . THR B 1 611 ? 142.476 122.803 165.101 1.00 61.00 ?  611 THR B CB    1 
ATOM   10457 O  OG1   . THR B 1 611 ? 143.450 122.669 164.058 1.00 61.18 ?  611 THR B OG1   1 
ATOM   10458 C  CG2   . THR B 1 611 ? 143.076 123.613 166.228 1.00 60.84 ?  611 THR B CG2   1 
ATOM   10459 N  N     . TYR B 1 612 ? 140.664 121.871 167.520 1.00 51.00 ?  612 TYR B N     1 
ATOM   10460 C  CA    . TYR B 1 612 ? 139.436 121.982 168.293 1.00 52.40 ?  612 TYR B CA    1 
ATOM   10461 C  C     . TYR B 1 612 ? 139.309 123.398 168.830 1.00 54.60 ?  612 TYR B C     1 
ATOM   10462 O  O     . TYR B 1 612 ? 140.254 123.928 169.424 1.00 53.52 ?  612 TYR B O     1 
ATOM   10463 C  CB    . TYR B 1 612 ? 139.427 120.972 169.439 1.00 54.04 ?  612 TYR B CB    1 
ATOM   10464 C  CG    . TYR B 1 612 ? 139.380 119.545 168.956 1.00 57.49 ?  612 TYR B CG    1 
ATOM   10465 C  CD1   . TYR B 1 612 ? 138.299 119.075 168.225 1.00 55.55 ?  612 TYR B CD1   1 
ATOM   10466 C  CD2   . TYR B 1 612 ? 140.432 118.676 169.202 1.00 56.40 ?  612 TYR B CD2   1 
ATOM   10467 C  CE1   . TYR B 1 612 ? 138.256 117.774 167.772 1.00 54.86 ?  612 TYR B CE1   1 
ATOM   10468 C  CE2   . TYR B 1 612 ? 140.400 117.375 168.751 1.00 59.31 ?  612 TYR B CE2   1 
ATOM   10469 C  CZ    . TYR B 1 612 ? 139.309 116.928 168.038 1.00 59.22 ?  612 TYR B CZ    1 
ATOM   10470 O  OH    . TYR B 1 612 ? 139.271 115.629 167.588 1.00 60.84 ?  612 TYR B OH    1 
ATOM   10471 N  N     . TYR B 1 613 ? 138.146 124.007 168.621 1.00 51.35 ?  613 TYR B N     1 
ATOM   10472 C  CA    . TYR B 1 613 ? 137.889 125.379 169.053 1.00 45.38 ?  613 TYR B CA    1 
ATOM   10473 C  C     . TYR B 1 613 ? 136.616 125.436 169.885 1.00 43.07 ?  613 TYR B C     1 
ATOM   10474 O  O     . TYR B 1 613 ? 135.510 125.514 169.325 1.00 43.80 ?  613 TYR B O     1 
ATOM   10475 C  CB    . TYR B 1 613 ? 137.790 126.322 167.862 1.00 42.88 ?  613 TYR B CB    1 
ATOM   10476 C  CG    . TYR B 1 613 ? 137.488 127.751 168.247 1.00 43.43 ?  613 TYR B CG    1 
ATOM   10477 C  CD1   . TYR B 1 613 ? 138.247 128.405 169.208 1.00 42.09 ?  613 TYR B CD1   1 
ATOM   10478 C  CD2   . TYR B 1 613 ? 136.445 128.446 167.652 1.00 45.50 ?  613 TYR B CD2   1 
ATOM   10479 C  CE1   . TYR B 1 613 ? 137.976 129.709 169.563 1.00 44.64 ?  613 TYR B CE1   1 
ATOM   10480 C  CE2   . TYR B 1 613 ? 136.167 129.750 168.001 1.00 45.24 ?  613 TYR B CE2   1 
ATOM   10481 C  CZ    . TYR B 1 613 ? 136.935 130.377 168.956 1.00 48.46 ?  613 TYR B CZ    1 
ATOM   10482 O  OH    . TYR B 1 613 ? 136.661 131.678 169.306 1.00 47.39 ?  613 TYR B OH    1 
ATOM   10483 N  N     . PRO B 1 614 ? 136.723 125.394 171.208 1.00 39.22 ?  614 PRO B N     1 
ATOM   10484 C  CA    . PRO B 1 614 ? 135.549 125.658 172.042 1.00 42.67 ?  614 PRO B CA    1 
ATOM   10485 C  C     . PRO B 1 614 ? 135.089 127.095 171.869 1.00 41.86 ?  614 PRO B C     1 
ATOM   10486 O  O     . PRO B 1 614 ? 135.885 127.999 171.602 1.00 42.89 ?  614 PRO B O     1 
ATOM   10487 C  CB    . PRO B 1 614 ? 136.051 125.403 173.470 1.00 39.16 ?  614 PRO B CB    1 
ATOM   10488 C  CG    . PRO B 1 614 ? 137.371 124.712 173.316 1.00 42.11 ?  614 PRO B CG    1 
ATOM   10489 C  CD    . PRO B 1 614 ? 137.931 125.163 172.013 1.00 40.31 ?  614 PRO B CD    1 
ATOM   10490 N  N     . MET B 1 615 ? 133.786 127.302 172.014 1.00 40.49 ?  615 MET B N     1 
ATOM   10491 C  CA    . MET B 1 615 ? 133.249 128.645 171.887 1.00 40.16 ?  615 MET B CA    1 
ATOM   10492 C  C     . MET B 1 615 ? 133.802 129.532 173.001 1.00 44.34 ?  615 MET B C     1 
ATOM   10493 O  O     . MET B 1 615 ? 134.038 129.052 174.116 1.00 42.90 ?  615 MET B O     1 
ATOM   10494 C  CB    . MET B 1 615 ? 131.721 128.623 171.919 1.00 38.52 ?  615 MET B CB    1 
ATOM   10495 C  CG    . MET B 1 615 ? 131.112 128.238 170.581 1.00 41.18 ?  615 MET B CG    1 
ATOM   10496 S  SD    . MET B 1 615 ? 132.184 128.733 169.217 1.00 52.06 ?  615 MET B SD    1 
ATOM   10497 C  CE    . MET B 1 615 ? 131.215 128.242 167.798 1.00 41.46 ?  615 MET B CE    1 
ATOM   10498 N  N     . PRO B 1 616 ? 134.043 130.812 172.729 1.00 45.96 ?  616 PRO B N     1 
ATOM   10499 C  CA    . PRO B 1 616 ? 134.726 131.665 173.712 1.00 39.83 ?  616 PRO B CA    1 
ATOM   10500 C  C     . PRO B 1 616 ? 133.941 131.768 175.010 1.00 41.31 ?  616 PRO B C     1 
ATOM   10501 O  O     . PRO B 1 616 ? 132.764 132.134 175.017 1.00 42.63 ?  616 PRO B O     1 
ATOM   10502 C  CB    . PRO B 1 616 ? 134.819 133.019 173.000 1.00 36.23 ?  616 PRO B CB    1 
ATOM   10503 C  CG    . PRO B 1 616 ? 134.641 132.707 171.553 1.00 41.50 ?  616 PRO B CG    1 
ATOM   10504 C  CD    . PRO B 1 616 ? 133.725 131.540 171.490 1.00 40.52 ?  616 PRO B CD    1 
ATOM   10505 N  N     . GLY B 1 617 ? 134.611 131.452 176.113 1.00 40.43 ?  617 GLY B N     1 
ATOM   10506 C  CA    . GLY B 1 617 ? 133.982 131.448 177.413 1.00 36.58 ?  617 GLY B CA    1 
ATOM   10507 C  C     . GLY B 1 617 ? 133.248 130.176 177.768 1.00 41.88 ?  617 GLY B C     1 
ATOM   10508 O  O     . GLY B 1 617 ? 132.608 130.129 178.825 1.00 45.55 ?  617 GLY B O     1 
ATOM   10509 N  N     . LEU B 1 618 ? 133.314 129.150 176.925 1.00 44.70 ?  618 LEU B N     1 
ATOM   10510 C  CA    . LEU B 1 618 ? 132.660 127.886 177.231 1.00 38.50 ?  618 LEU B CA    1 
ATOM   10511 C  C     . LEU B 1 618 ? 133.321 127.221 178.429 1.00 39.94 ?  618 LEU B C     1 
ATOM   10512 O  O     . LEU B 1 618 ? 134.549 127.167 178.534 1.00 44.64 ?  618 LEU B O     1 
ATOM   10513 C  CB    . LEU B 1 618 ? 132.706 126.953 176.022 1.00 38.04 ?  618 LEU B CB    1 
ATOM   10514 C  CG    . LEU B 1 618 ? 131.971 125.619 176.141 1.00 40.00 ?  618 LEU B CG    1 
ATOM   10515 C  CD1   . LEU B 1 618 ? 130.492 125.840 176.386 1.00 41.29 ?  618 LEU B CD1   1 
ATOM   10516 C  CD2   . LEU B 1 618 ? 132.188 124.784 174.895 1.00 40.82 ?  618 LEU B CD2   1 
ATOM   10517 N  N     . ALA B 1 619 ? 132.494 126.714 179.336 1.00 47.78 ?  619 ALA B N     1 
ATOM   10518 C  CA    . ALA B 1 619 ? 132.965 126.037 180.533 1.00 47.23 ?  619 ALA B CA    1 
ATOM   10519 C  C     . ALA B 1 619 ? 131.879 125.072 180.986 1.00 49.90 ?  619 ALA B C     1 
ATOM   10520 O  O     . ALA B 1 619 ? 130.924 124.797 180.254 1.00 54.00 ?  619 ALA B O     1 
ATOM   10521 C  CB    . ALA B 1 619 ? 133.336 127.052 181.621 1.00 46.77 ?  619 ALA B CB    1 
ATOM   10522 N  N     . SER B 1 620 ? 132.029 124.545 182.200 1.00 56.15 ?  620 SER B N     1 
ATOM   10523 C  CA    . SER B 1 620 ? 131.013 123.654 182.746 1.00 55.66 ?  620 SER B CA    1 
ATOM   10524 C  C     . SER B 1 620 ? 129.796 124.428 183.240 1.00 55.44 ?  620 SER B C     1 
ATOM   10525 O  O     . SER B 1 620 ? 128.662 123.954 183.108 1.00 57.57 ?  620 SER B O     1 
ATOM   10526 C  CB    . SER B 1 620 ? 131.608 122.816 183.877 1.00 57.26 ?  620 SER B CB    1 
ATOM   10527 O  OG    . SER B 1 620 ? 132.830 122.224 183.476 1.00 59.15 ?  620 SER B OG    1 
ATOM   10528 N  N     . ASN B 1 621 ? 130.012 125.617 183.806 1.00 50.85 ?  621 ASN B N     1 
ATOM   10529 C  CA    . ASN B 1 621 ? 128.905 126.374 184.384 1.00 52.15 ?  621 ASN B CA    1 
ATOM   10530 C  C     . ASN B 1 621 ? 127.991 126.946 183.306 1.00 54.39 ?  621 ASN B C     1 
ATOM   10531 O  O     . ASN B 1 621 ? 126.770 127.011 183.494 1.00 56.25 ?  621 ASN B O     1 
ATOM   10532 C  CB    . ASN B 1 621 ? 129.444 127.487 185.283 1.00 53.65 ?  621 ASN B CB    1 
ATOM   10533 C  CG    . ASN B 1 621 ? 130.221 128.537 184.513 1.00 57.66 ?  621 ASN B CG    1 
ATOM   10534 O  OD1   . ASN B 1 621 ? 131.253 128.245 183.910 1.00 59.16 ?  621 ASN B OD1   1 
ATOM   10535 N  ND2   . ASN B 1 621 ? 129.729 129.771 184.532 1.00 55.87 ?  621 ASN B ND2   1 
ATOM   10536 N  N     . ASN B 1 622 ? 128.555 127.365 182.173 1.00 46.91 ?  622 ASN B N     1 
ATOM   10537 C  CA    . ASN B 1 622 ? 127.782 127.971 181.096 1.00 45.83 ?  622 ASN B CA    1 
ATOM   10538 C  C     . ASN B 1 622 ? 127.648 127.053 179.886 1.00 47.47 ?  622 ASN B C     1 
ATOM   10539 O  O     . ASN B 1 622 ? 127.420 127.532 178.773 1.00 53.86 ?  622 ASN B O     1 
ATOM   10540 C  CB    . ASN B 1 622 ? 128.397 129.315 180.691 1.00 46.81 ?  622 ASN B CB    1 
ATOM   10541 C  CG    . ASN B 1 622 ? 129.814 129.185 180.151 1.00 46.56 ?  622 ASN B CG    1 
ATOM   10542 O  OD1   . ASN B 1 622 ? 130.281 128.095 179.827 1.00 52.25 ?  622 ASN B OD1   1 
ATOM   10543 N  ND2   . ASN B 1 622 ? 130.508 130.312 180.058 1.00 43.47 ?  622 ASN B ND2   1 
ATOM   10544 N  N     . TRP B 1 623 ? 127.796 125.742 180.084 1.00 41.95 ?  623 TRP B N     1 
ATOM   10545 C  CA    . TRP B 1 623 ? 127.748 124.813 178.960 1.00 40.84 ?  623 TRP B CA    1 
ATOM   10546 C  C     . TRP B 1 623 ? 126.383 124.825 178.283 1.00 42.27 ?  623 TRP B C     1 
ATOM   10547 O  O     . TRP B 1 623 ? 126.296 124.831 177.049 1.00 42.30 ?  623 TRP B O     1 
ATOM   10548 C  CB    . TRP B 1 623 ? 128.097 123.402 179.433 1.00 45.73 ?  623 TRP B CB    1 
ATOM   10549 C  CG    . TRP B 1 623 ? 127.890 122.343 178.395 1.00 43.63 ?  623 TRP B CG    1 
ATOM   10550 C  CD1   . TRP B 1 623 ? 126.749 121.635 178.162 1.00 40.76 ?  623 TRP B CD1   1 
ATOM   10551 C  CD2   . TRP B 1 623 ? 128.855 121.869 177.449 1.00 42.24 ?  623 TRP B CD2   1 
ATOM   10552 N  NE1   . TRP B 1 623 ? 126.941 120.752 177.130 1.00 42.99 ?  623 TRP B NE1   1 
ATOM   10553 C  CE2   . TRP B 1 623 ? 128.227 120.874 176.676 1.00 40.39 ?  623 TRP B CE2   1 
ATOM   10554 C  CE3   . TRP B 1 623 ? 130.190 122.189 177.183 1.00 39.81 ?  623 TRP B CE3   1 
ATOM   10555 C  CZ2   . TRP B 1 623 ? 128.887 120.198 175.653 1.00 38.39 ?  623 TRP B CZ2   1 
ATOM   10556 C  CZ3   . TRP B 1 623 ? 130.840 121.517 176.166 1.00 42.86 ?  623 TRP B CZ3   1 
ATOM   10557 C  CH2   . TRP B 1 623 ? 130.190 120.534 175.414 1.00 42.62 ?  623 TRP B CH2   1 
ATOM   10558 N  N     . PHE B 1 624 ? 125.308 124.830 179.067 1.00 48.20 ?  624 PHE B N     1 
ATOM   10559 C  CA    . PHE B 1 624 ? 123.969 124.746 178.505 1.00 45.50 ?  624 PHE B CA    1 
ATOM   10560 C  C     . PHE B 1 624 ? 123.393 126.100 178.114 1.00 45.25 ?  624 PHE B C     1 
ATOM   10561 O  O     . PHE B 1 624 ? 122.348 126.143 177.458 1.00 52.40 ?  624 PHE B O     1 
ATOM   10562 C  CB    . PHE B 1 624 ? 123.029 124.044 179.490 1.00 49.11 ?  624 PHE B CB    1 
ATOM   10563 C  CG    . PHE B 1 624 ? 123.230 122.557 179.546 1.00 50.34 ?  624 PHE B CG    1 
ATOM   10564 C  CD1   . PHE B 1 624 ? 122.832 121.752 178.492 1.00 44.39 ?  624 PHE B CD1   1 
ATOM   10565 C  CD2   . PHE B 1 624 ? 123.831 121.966 180.645 1.00 48.19 ?  624 PHE B CD2   1 
ATOM   10566 C  CE1   . PHE B 1 624 ? 123.020 120.386 178.536 1.00 44.64 ?  624 PHE B CE1   1 
ATOM   10567 C  CE2   . PHE B 1 624 ? 124.023 120.599 180.694 1.00 49.33 ?  624 PHE B CE2   1 
ATOM   10568 C  CZ    . PHE B 1 624 ? 123.616 119.807 179.639 1.00 48.15 ?  624 PHE B CZ    1 
ATOM   10569 N  N     . PHE B 1 625 ? 124.043 127.200 178.493 1.00 39.83 ?  625 PHE B N     1 
ATOM   10570 C  CA    . PHE B 1 625 ? 123.698 128.492 177.919 1.00 37.08 ?  625 PHE B CA    1 
ATOM   10571 C  C     . PHE B 1 625 ? 124.278 128.667 176.526 1.00 36.39 ?  625 PHE B C     1 
ATOM   10572 O  O     . PHE B 1 625 ? 123.804 129.522 175.772 1.00 41.33 ?  625 PHE B O     1 
ATOM   10573 C  CB    . PHE B 1 625 ? 124.171 129.627 178.826 1.00 32.77 ?  625 PHE B CB    1 
ATOM   10574 C  CG    . PHE B 1 625 ? 123.370 129.766 180.085 1.00 35.96 ?  625 PHE B CG    1 
ATOM   10575 C  CD1   . PHE B 1 625 ? 122.042 130.149 180.035 1.00 37.62 ?  625 PHE B CD1   1 
ATOM   10576 C  CD2   . PHE B 1 625 ? 123.944 129.516 181.320 1.00 37.97 ?  625 PHE B CD2   1 
ATOM   10577 C  CE1   . PHE B 1 625 ? 121.301 130.280 181.190 1.00 40.00 ?  625 PHE B CE1   1 
ATOM   10578 C  CE2   . PHE B 1 625 ? 123.207 129.647 182.479 1.00 37.58 ?  625 PHE B CE2   1 
ATOM   10579 C  CZ    . PHE B 1 625 ? 121.884 130.030 182.414 1.00 40.99 ?  625 PHE B CZ    1 
ATOM   10580 N  N     . TYR B 1 626 ? 125.287 127.878 176.170 1.00 29.50 ?  626 TYR B N     1 
ATOM   10581 C  CA    . TYR B 1 626 ? 125.825 127.859 174.814 1.00 33.44 ?  626 TYR B CA    1 
ATOM   10582 C  C     . TYR B 1 626 ? 125.057 126.873 173.942 1.00 30.15 ?  626 TYR B C     1 
ATOM   10583 O  O     . TYR B 1 626 ? 125.631 126.005 173.291 1.00 36.11 ?  626 TYR B O     1 
ATOM   10584 C  CB    . TYR B 1 626 ? 127.309 127.516 174.848 1.00 32.29 ?  626 TYR B CB    1 
ATOM   10585 C  CG    . TYR B 1 626 ? 128.207 128.720 174.992 1.00 34.18 ?  626 TYR B CG    1 
ATOM   10586 C  CD1   . TYR B 1 626 ? 128.463 129.551 173.912 1.00 35.39 ?  626 TYR B CD1   1 
ATOM   10587 C  CD2   . TYR B 1 626 ? 128.797 129.024 176.210 1.00 34.34 ?  626 TYR B CD2   1 
ATOM   10588 C  CE1   . TYR B 1 626 ? 129.283 130.651 174.041 1.00 35.36 ?  626 TYR B CE1   1 
ATOM   10589 C  CE2   . TYR B 1 626 ? 129.617 130.122 176.348 1.00 31.69 ?  626 TYR B CE2   1 
ATOM   10590 C  CZ    . TYR B 1 626 ? 129.857 130.931 175.260 1.00 30.87 ?  626 TYR B CZ    1 
ATOM   10591 O  OH    . TYR B 1 626 ? 130.671 132.027 175.391 1.00 38.82 ?  626 TYR B OH    1 
ATOM   10592 N  N     . LYS B 1 627 ? 123.735 127.011 173.936 1.00 33.87 ?  627 LYS B N     1 
ATOM   10593 C  CA    . LYS B 1 627 ? 122.888 126.116 173.163 1.00 34.18 ?  627 LYS B CA    1 
ATOM   10594 C  C     . LYS B 1 627 ? 123.194 126.252 171.678 1.00 37.69 ?  627 LYS B C     1 
ATOM   10595 O  O     . LYS B 1 627 ? 123.322 127.363 171.157 1.00 44.50 ?  627 LYS B O     1 
ATOM   10596 C  CB    . LYS B 1 627 ? 121.419 126.428 173.444 1.00 37.36 ?  627 LYS B CB    1 
ATOM   10597 C  CG    . LYS B 1 627 ? 120.427 125.484 172.801 1.00 37.26 ?  627 LYS B CG    1 
ATOM   10598 C  CD    . LYS B 1 627 ? 119.032 125.732 173.350 1.00 32.29 ?  627 LYS B CD    1 
ATOM   10599 C  CE    . LYS B 1 627 ? 118.007 124.836 172.690 1.00 39.91 ?  627 LYS B CE    1 
ATOM   10600 N  NZ    . LYS B 1 627 ? 116.642 125.075 173.232 1.00 41.71 1  627 LYS B NZ    1 
ATOM   10601 N  N     . GLU B 1 628 ? 123.331 125.118 170.999 1.00 39.03 ?  628 GLU B N     1 
ATOM   10602 C  CA    . GLU B 1 628 ? 123.640 125.142 169.578 1.00 35.29 ?  628 GLU B CA    1 
ATOM   10603 C  C     . GLU B 1 628 ? 122.459 125.689 168.786 1.00 40.27 ?  628 GLU B C     1 
ATOM   10604 O  O     . GLU B 1 628 ? 121.297 125.532 169.170 1.00 45.56 ?  628 GLU B O     1 
ATOM   10605 C  CB    . GLU B 1 628 ? 124.013 123.747 169.086 1.00 39.70 ?  628 GLU B CB    1 
ATOM   10606 C  CG    . GLU B 1 628 ? 125.165 123.118 169.850 1.00 41.43 ?  628 GLU B CG    1 
ATOM   10607 C  CD    . GLU B 1 628 ? 125.905 122.077 169.037 1.00 47.84 ?  628 GLU B CD    1 
ATOM   10608 O  OE1   . GLU B 1 628 ? 125.385 121.670 167.977 1.00 43.73 ?  628 GLU B OE1   1 
ATOM   10609 O  OE2   . GLU B 1 628 ? 127.008 121.667 169.455 1.00 45.74 -1 628 GLU B OE2   1 
ATOM   10610 N  N     . ALA B 1 629 ? 122.776 126.347 167.668 1.00 41.50 ?  629 ALA B N     1 
ATOM   10611 C  CA    . ALA B 1 629 ? 121.747 127.015 166.878 1.00 32.10 ?  629 ALA B CA    1 
ATOM   10612 C  C     . ALA B 1 629 ? 120.723 126.026 166.337 1.00 37.00 ?  629 ALA B C     1 
ATOM   10613 O  O     . ALA B 1 629 ? 119.527 126.331 166.280 1.00 44.16 ?  629 ALA B O     1 
ATOM   10614 C  CB    . ALA B 1 629 ? 122.397 127.795 165.736 1.00 30.45 ?  629 ALA B CB    1 
ATOM   10615 N  N     . TYR B 1 630 ? 121.174 124.840 165.926 1.00 40.68 ?  630 TYR B N     1 
ATOM   10616 C  CA    . TYR B 1 630 ? 120.251 123.849 165.381 1.00 39.14 ?  630 TYR B CA    1 
ATOM   10617 C  C     . TYR B 1 630 ? 119.273 123.346 166.435 1.00 42.65 ?  630 TYR B C     1 
ATOM   10618 O  O     . TYR B 1 630 ? 118.119 123.042 166.112 1.00 49.05 ?  630 TYR B O     1 
ATOM   10619 C  CB    . TYR B 1 630 ? 121.033 122.687 164.777 1.00 37.55 ?  630 TYR B CB    1 
ATOM   10620 C  CG    . TYR B 1 630 ? 122.008 123.115 163.707 1.00 37.64 ?  630 TYR B CG    1 
ATOM   10621 C  CD1   . TYR B 1 630 ? 121.584 123.334 162.405 1.00 38.02 ?  630 TYR B CD1   1 
ATOM   10622 C  CD2   . TYR B 1 630 ? 123.349 123.311 164.001 1.00 37.73 ?  630 TYR B CD2   1 
ATOM   10623 C  CE1   . TYR B 1 630 ? 122.469 123.728 161.424 1.00 38.57 ?  630 TYR B CE1   1 
ATOM   10624 C  CE2   . TYR B 1 630 ? 124.241 123.705 163.026 1.00 40.36 ?  630 TYR B CE2   1 
ATOM   10625 C  CZ    . TYR B 1 630 ? 123.795 123.913 161.740 1.00 45.55 ?  630 TYR B CZ    1 
ATOM   10626 O  OH    . TYR B 1 630 ? 124.680 124.305 160.764 1.00 51.53 ?  630 TYR B OH    1 
ATOM   10627 N  N     . ASP B 1 631 ? 119.708 123.251 167.692 1.00 42.26 ?  631 ASP B N     1 
ATOM   10628 C  CA    . ASP B 1 631 ? 118.816 122.849 168.771 1.00 37.01 ?  631 ASP B CA    1 
ATOM   10629 C  C     . ASP B 1 631 ? 117.817 123.934 169.145 1.00 43.14 ?  631 ASP B C     1 
ATOM   10630 O  O     . ASP B 1 631 ? 116.895 123.663 169.921 1.00 47.63 ?  631 ASP B O     1 
ATOM   10631 C  CB    . ASP B 1 631 ? 119.628 122.457 170.006 1.00 41.58 ?  631 ASP B CB    1 
ATOM   10632 C  CG    . ASP B 1 631 ? 120.611 121.339 169.727 1.00 48.57 ?  631 ASP B CG    1 
ATOM   10633 O  OD1   . ASP B 1 631 ? 120.285 120.445 168.920 1.00 49.25 ?  631 ASP B OD1   1 
ATOM   10634 O  OD2   . ASP B 1 631 ? 121.712 121.355 170.317 1.00 50.10 -1 631 ASP B OD2   1 
ATOM   10635 N  N     . MET B 1 632 ? 117.971 125.141 168.615 1.00 37.56 ?  632 MET B N     1 
ATOM   10636 C  CA    . MET B 1 632 ? 117.147 126.274 169.001 1.00 38.15 ?  632 MET B CA    1 
ATOM   10637 C  C     . MET B 1 632 ? 115.850 126.312 168.204 1.00 37.21 ?  632 MET B C     1 
ATOM   10638 O  O     . MET B 1 632 ? 115.720 125.698 167.143 1.00 36.18 ?  632 MET B O     1 
ATOM   10639 C  CB    . MET B 1 632 ? 117.908 127.582 168.797 1.00 36.52 ?  632 MET B CB    1 
ATOM   10640 C  CG    . MET B 1 632 ? 118.562 128.121 170.046 1.00 35.34 ?  632 MET B CG    1 
ATOM   10641 S  SD    . MET B 1 632 ? 119.953 129.190 169.680 1.00 45.68 ?  632 MET B SD    1 
ATOM   10642 C  CE    . MET B 1 632 ? 120.770 129.221 171.268 1.00 33.51 ?  632 MET B CE    1 
ATOM   10643 N  N     . ASP B 1 633 ? 114.883 127.052 168.737 1.00 37.50 ?  633 ASP B N     1 
ATOM   10644 C  CA    . ASP B 1 633 ? 113.649 127.336 168.020 1.00 33.40 ?  633 ASP B CA    1 
ATOM   10645 C  C     . ASP B 1 633 ? 113.887 128.515 167.086 1.00 36.19 ?  633 ASP B C     1 
ATOM   10646 O  O     . ASP B 1 633 ? 114.171 129.627 167.546 1.00 43.42 ?  633 ASP B O     1 
ATOM   10647 C  CB    . ASP B 1 633 ? 112.519 127.640 169.000 1.00 30.86 ?  633 ASP B CB    1 
ATOM   10648 C  CG    . ASP B 1 633 ? 111.176 127.802 168.315 1.00 40.37 ?  633 ASP B CG    1 
ATOM   10649 O  OD1   . ASP B 1 633 ? 111.072 127.476 167.114 1.00 43.37 ?  633 ASP B OD1   1 
ATOM   10650 O  OD2   . ASP B 1 633 ? 110.223 128.258 168.979 1.00 41.05 -1 633 ASP B OD2   1 
ATOM   10651 N  N     . MET B 1 634 ? 113.778 128.274 165.778 1.00 30.22 ?  634 MET B N     1 
ATOM   10652 C  CA    . MET B 1 634 ? 114.034 129.335 164.811 1.00 23.54 ?  634 MET B CA    1 
ATOM   10653 C  C     . MET B 1 634 ? 113.051 130.489 164.941 1.00 26.50 ?  634 MET B C     1 
ATOM   10654 O  O     . MET B 1 634 ? 113.374 131.605 164.526 1.00 31.39 ?  634 MET B O     1 
ATOM   10655 C  CB    . MET B 1 634 ? 113.997 128.775 163.389 1.00 26.08 ?  634 MET B CB    1 
ATOM   10656 C  CG    . MET B 1 634 ? 115.292 128.111 162.962 1.00 31.31 ?  634 MET B CG    1 
ATOM   10657 S  SD    . MET B 1 634 ? 116.724 129.189 163.174 1.00 43.09 ?  634 MET B SD    1 
ATOM   10658 C  CE    . MET B 1 634 ? 117.575 128.371 164.521 1.00 29.75 ?  634 MET B CE    1 
ATOM   10659 N  N     . PHE B 1 635 ? 111.865 130.251 165.502 1.00 26.09 ?  635 PHE B N     1 
ATOM   10660 C  CA    . PHE B 1 635 ? 110.944 131.353 165.757 1.00 23.44 ?  635 PHE B CA    1 
ATOM   10661 C  C     . PHE B 1 635 ? 111.517 132.319 166.786 1.00 21.59 ?  635 PHE B C     1 
ATOM   10662 O  O     . PHE B 1 635 ? 111.401 133.540 166.636 1.00 26.28 ?  635 PHE B O     1 
ATOM   10663 C  CB    . PHE B 1 635 ? 109.591 130.812 166.217 1.00 27.07 ?  635 PHE B CB    1 
ATOM   10664 C  CG    . PHE B 1 635 ? 108.625 130.568 165.094 1.00 30.07 ?  635 PHE B CG    1 
ATOM   10665 C  CD1   . PHE B 1 635 ? 109.042 129.949 163.929 1.00 26.06 ?  635 PHE B CD1   1 
ATOM   10666 C  CD2   . PHE B 1 635 ? 107.303 130.958 165.203 1.00 25.64 ?  635 PHE B CD2   1 
ATOM   10667 C  CE1   . PHE B 1 635 ? 108.159 129.723 162.894 1.00 24.41 ?  635 PHE B CE1   1 
ATOM   10668 C  CE2   . PHE B 1 635 ? 106.414 130.734 164.170 1.00 28.30 ?  635 PHE B CE2   1 
ATOM   10669 C  CZ    . PHE B 1 635 ? 106.843 130.114 163.015 1.00 25.18 ?  635 PHE B CZ    1 
ATOM   10670 N  N     . LYS B 1 636 ? 112.154 131.793 167.832 1.00 27.48 ?  636 LYS B N     1 
ATOM   10671 C  CA    . LYS B 1 636 ? 112.756 132.660 168.838 1.00 30.38 ?  636 LYS B CA    1 
ATOM   10672 C  C     . LYS B 1 636 ? 113.990 133.374 168.300 1.00 26.86 ?  636 LYS B C     1 
ATOM   10673 O  O     . LYS B 1 636 ? 114.260 134.518 168.682 1.00 36.77 ?  636 LYS B O     1 
ATOM   10674 C  CB    . LYS B 1 636 ? 113.101 131.849 170.084 1.00 30.54 ?  636 LYS B CB    1 
ATOM   10675 C  CG    . LYS B 1 636 ? 111.903 131.152 170.704 1.00 29.29 ?  636 LYS B CG    1 
ATOM   10676 C  CD    . LYS B 1 636 ? 111.417 131.889 171.938 1.00 34.76 ?  636 LYS B CD    1 
ATOM   10677 C  CE    . LYS B 1 636 ? 109.948 131.611 172.205 1.00 33.40 ?  636 LYS B CE    1 
ATOM   10678 N  NZ    . LYS B 1 636 ? 109.174 132.867 172.401 1.00 35.79 1  636 LYS B NZ    1 
ATOM   10679 N  N     . VAL B 1 637 ? 114.744 132.727 167.411 1.00 24.28 ?  637 VAL B N     1 
ATOM   10680 C  CA    . VAL B 1 637 ? 115.859 133.407 166.758 1.00 17.58 ?  637 VAL B CA    1 
ATOM   10681 C  C     . VAL B 1 637 ? 115.343 134.528 165.866 1.00 27.32 ?  637 VAL B C     1 
ATOM   10682 O  O     . VAL B 1 637 ? 115.937 135.612 165.797 1.00 31.76 ?  637 VAL B O     1 
ATOM   10683 C  CB    . VAL B 1 637 ? 116.712 132.395 165.972 1.00 21.70 ?  637 VAL B CB    1 
ATOM   10684 C  CG1   . VAL B 1 637 ? 117.895 133.088 165.323 1.00 22.34 ?  637 VAL B CG1   1 
ATOM   10685 C  CG2   . VAL B 1 637 ? 117.178 131.277 166.888 1.00 23.89 ?  637 VAL B CG2   1 
ATOM   10686 N  N     . VAL B 1 638 ? 114.228 134.287 165.171 1.00 25.42 ?  638 VAL B N     1 
ATOM   10687 C  CA    . VAL B 1 638 ? 113.588 135.341 164.389 1.00 22.70 ?  638 VAL B CA    1 
ATOM   10688 C  C     . VAL B 1 638 ? 113.169 136.488 165.297 1.00 19.58 ?  638 VAL B C     1 
ATOM   10689 O  O     . VAL B 1 638 ? 113.328 137.663 164.952 1.00 30.46 ?  638 VAL B O     1 
ATOM   10690 C  CB    . VAL B 1 638 ? 112.385 134.778 163.609 1.00 24.93 ?  638 VAL B CB    1 
ATOM   10691 C  CG1   . VAL B 1 638 ? 111.488 135.905 163.132 1.00 14.67 ?  638 VAL B CG1   1 
ATOM   10692 C  CG2   . VAL B 1 638 ? 112.844 133.935 162.436 1.00 23.91 ?  638 VAL B CG2   1 
ATOM   10693 N  N     . ASP B 1 639 ? 112.617 136.163 166.466 1.00 17.63 ?  639 ASP B N     1 
ATOM   10694 C  CA    . ASP B 1 639 ? 112.217 137.195 167.417 1.00 21.91 ?  639 ASP B CA    1 
ATOM   10695 C  C     . ASP B 1 639 ? 113.412 138.029 167.858 1.00 26.76 ?  639 ASP B C     1 
ATOM   10696 O  O     . ASP B 1 639 ? 113.329 139.260 167.931 1.00 34.74 ?  639 ASP B O     1 
ATOM   10697 C  CB    . ASP B 1 639 ? 111.540 136.553 168.627 1.00 25.22 ?  639 ASP B CB    1 
ATOM   10698 C  CG    . ASP B 1 639 ? 110.080 136.244 168.383 1.00 36.03 ?  639 ASP B CG    1 
ATOM   10699 O  OD1   . ASP B 1 639 ? 109.440 136.969 167.594 1.00 33.39 ?  639 ASP B OD1   1 
ATOM   10700 O  OD2   . ASP B 1 639 ? 109.571 135.274 168.981 1.00 39.17 -1 639 ASP B OD2   1 
ATOM   10701 N  N     . MET B 1 640 ? 114.537 137.372 168.146 1.00 24.69 ?  640 MET B N     1 
ATOM   10702 C  CA    . MET B 1 640 ? 115.745 138.091 168.538 1.00 17.97 ?  640 MET B CA    1 
ATOM   10703 C  C     . MET B 1 640 ? 116.236 139.007 167.421 1.00 23.27 ?  640 MET B C     1 
ATOM   10704 O  O     . MET B 1 640 ? 116.553 140.180 167.656 1.00 32.90 ?  640 MET B O     1 
ATOM   10705 C  CB    . MET B 1 640 ? 116.837 137.096 168.929 1.00 22.73 ?  640 MET B CB    1 
ATOM   10706 C  CG    . MET B 1 640 ? 118.235 137.680 168.919 1.00 28.17 ?  640 MET B CG    1 
ATOM   10707 S  SD    . MET B 1 640 ? 118.542 138.731 170.345 1.00 39.52 ?  640 MET B SD    1 
ATOM   10708 C  CE    . MET B 1 640 ? 118.897 137.499 171.587 1.00 26.08 ?  640 MET B CE    1 
ATOM   10709 N  N     . ILE B 1 641 ? 116.303 138.485 166.195 1.00 28.94 ?  641 ILE B N     1 
ATOM   10710 C  CA    . ILE B 1 641 ? 116.825 139.280 165.090 1.00 21.13 ?  641 ILE B CA    1 
ATOM   10711 C  C     . ILE B 1 641 ? 115.894 140.440 164.768 1.00 19.87 ?  641 ILE B C     1 
ATOM   10712 O  O     . ILE B 1 641 ? 116.353 141.531 164.410 1.00 29.61 ?  641 ILE B O     1 
ATOM   10713 C  CB    . ILE B 1 641 ? 117.080 138.388 163.862 1.00 25.85 ?  641 ILE B CB    1 
ATOM   10714 C  CG1   . ILE B 1 641 ? 118.080 137.289 164.213 1.00 18.83 ?  641 ILE B CG1   1 
ATOM   10715 C  CG2   . ILE B 1 641 ? 117.616 139.210 162.702 1.00 18.72 ?  641 ILE B CG2   1 
ATOM   10716 C  CD1   . ILE B 1 641 ? 119.299 137.792 164.953 1.00 20.70 ?  641 ILE B CD1   1 
ATOM   10717 N  N     . ALA B 1 642 ? 114.581 140.240 164.898 1.00 17.45 ?  642 ALA B N     1 
ATOM   10718 C  CA    . ALA B 1 642 ? 113.639 141.332 164.693 1.00 20.38 ?  642 ALA B CA    1 
ATOM   10719 C  C     . ALA B 1 642 ? 113.736 142.364 165.806 1.00 21.19 ?  642 ALA B C     1 
ATOM   10720 O  O     . ALA B 1 642 ? 113.515 143.557 165.564 1.00 25.52 ?  642 ALA B O     1 
ATOM   10721 C  CB    . ALA B 1 642 ? 112.215 140.788 164.594 1.00 15.88 ?  642 ALA B CB    1 
ATOM   10722 N  N     . THR B 1 643 ? 114.044 141.928 167.027 1.00 21.94 ?  643 THR B N     1 
ATOM   10723 C  CA    . THR B 1 643 ? 114.321 142.877 168.099 1.00 18.28 ?  643 THR B CA    1 
ATOM   10724 C  C     . THR B 1 643 ? 115.546 143.721 167.775 1.00 24.19 ?  643 THR B C     1 
ATOM   10725 O  O     . THR B 1 643 ? 115.552 144.937 167.999 1.00 26.56 ?  643 THR B O     1 
ATOM   10726 C  CB    . THR B 1 643 ? 114.516 142.134 169.418 1.00 17.26 ?  643 THR B CB    1 
ATOM   10727 O  OG1   . THR B 1 643 ? 113.353 141.345 169.697 1.00 22.86 ?  643 THR B OG1   1 
ATOM   10728 C  CG2   . THR B 1 643 ? 114.740 143.113 170.550 1.00 17.83 ?  643 THR B CG2   1 
ATOM   10729 N  N     . ILE B 1 644 ? 116.598 143.090 167.253 1.00 22.78 ?  644 ILE B N     1 
ATOM   10730 C  CA    . ILE B 1 644 ? 117.784 143.840 166.853 1.00 10.33 ?  644 ILE B CA    1 
ATOM   10731 C  C     . ILE B 1 644 ? 117.502 144.674 165.609 1.00 16.72 ?  644 ILE B C     1 
ATOM   10732 O  O     . ILE B 1 644 ? 117.954 145.820 165.499 1.00 22.18 ?  644 ILE B O     1 
ATOM   10733 C  CB    . ILE B 1 644 ? 118.972 142.887 166.635 1.00 12.86 ?  644 ILE B CB    1 
ATOM   10734 C  CG1   . ILE B 1 644 ? 119.232 142.057 167.891 1.00 16.38 ?  644 ILE B CG1   1 
ATOM   10735 C  CG2   . ILE B 1 644 ? 120.212 143.668 166.256 1.00 8.54  ?  644 ILE B CG2   1 
ATOM   10736 C  CD1   . ILE B 1 644 ? 120.053 140.820 167.632 1.00 22.52 ?  644 ILE B CD1   1 
ATOM   10737 N  N     . GLN B 1 645 ? 116.748 144.116 164.655 1.00 12.43 ?  645 GLN B N     1 
ATOM   10738 C  CA    . GLN B 1 645 ? 116.551 144.773 163.366 1.00 13.88 ?  645 GLN B CA    1 
ATOM   10739 C  C     . GLN B 1 645 ? 115.854 146.120 163.505 1.00 17.48 ?  645 GLN B C     1 
ATOM   10740 O  O     . GLN B 1 645 ? 116.047 147.006 162.665 1.00 29.59 ?  645 GLN B O     1 
ATOM   10741 C  CB    . GLN B 1 645 ? 115.753 143.861 162.434 1.00 12.98 ?  645 GLN B CB    1 
ATOM   10742 C  CG    . GLN B 1 645 ? 115.592 144.391 161.022 1.00 3.84  ?  645 GLN B CG    1 
ATOM   10743 C  CD    . GLN B 1 645 ? 116.864 144.280 160.213 1.00 19.17 ?  645 GLN B CD    1 
ATOM   10744 O  OE1   . GLN B 1 645 ? 117.663 145.211 160.163 1.00 13.42 ?  645 GLN B OE1   1 
ATOM   10745 N  NE2   . GLN B 1 645 ? 117.057 143.136 159.570 1.00 16.27 ?  645 GLN B NE2   1 
ATOM   10746 N  N     . GLN B 1 646 ? 115.054 146.302 164.553 1.00 19.98 ?  646 GLN B N     1 
ATOM   10747 C  CA    . GLN B 1 646 ? 114.345 147.563 164.724 1.00 11.37 ?  646 GLN B CA    1 
ATOM   10748 C  C     . GLN B 1 646 ? 115.268 148.717 165.092 1.00 11.49 ?  646 GLN B C     1 
ATOM   10749 O  O     . GLN B 1 646 ? 114.823 149.867 165.077 1.00 15.53 ?  646 GLN B O     1 
ATOM   10750 C  CB    . GLN B 1 646 ? 113.249 147.410 165.777 1.00 19.79 ?  646 GLN B CB    1 
ATOM   10751 C  CG    . GLN B 1 646 ? 113.743 147.435 167.203 1.00 22.80 ?  646 GLN B CG    1 
ATOM   10752 C  CD    . GLN B 1 646 ? 112.641 147.142 168.196 1.00 27.77 ?  646 GLN B CD    1 
ATOM   10753 O  OE1   . GLN B 1 646 ? 112.697 146.156 168.928 1.00 26.85 ?  646 GLN B OE1   1 
ATOM   10754 N  NE2   . GLN B 1 646 ? 111.630 148.001 168.227 1.00 23.34 ?  646 GLN B NE2   1 
ATOM   10755 N  N     . HIS B 1 647 ? 116.531 148.447 165.412 1.00 29.18 ?  647 HIS B N     1 
ATOM   10756 C  CA    . HIS B 1 647 ? 117.501 149.493 165.695 1.00 12.41 ?  647 HIS B CA    1 
ATOM   10757 C  C     . HIS B 1 647 ? 118.626 149.551 164.673 1.00 13.61 ?  647 HIS B C     1 
ATOM   10758 O  O     . HIS B 1 647 ? 119.531 150.380 164.817 1.00 27.00 ?  647 HIS B O     1 
ATOM   10759 C  CB    . HIS B 1 647 ? 118.093 149.307 167.099 1.00 5.67  ?  647 HIS B CB    1 
ATOM   10760 C  CG    . HIS B 1 647 ? 117.063 149.138 168.170 1.00 14.52 ?  647 HIS B CG    1 
ATOM   10761 N  ND1   . HIS B 1 647 ? 116.157 150.124 168.494 1.00 18.16 ?  647 HIS B ND1   1 
ATOM   10762 C  CD2   . HIS B 1 647 ? 116.796 148.098 168.994 1.00 12.29 ?  647 HIS B CD2   1 
ATOM   10763 C  CE1   . HIS B 1 647 ? 115.375 149.698 169.469 1.00 20.52 ?  647 HIS B CE1   1 
ATOM   10764 N  NE2   . HIS B 1 647 ? 115.744 148.472 169.791 1.00 15.87 ?  647 HIS B NE2   1 
ATOM   10765 N  N     . ILE B 1 648 ? 118.595 148.704 163.650 1.00 14.96 ?  648 ILE B N     1 
ATOM   10766 C  CA    . ILE B 1 648 ? 119.612 148.666 162.608 1.00 16.22 ?  648 ILE B CA    1 
ATOM   10767 C  C     . ILE B 1 648 ? 118.988 149.235 161.341 1.00 14.31 ?  648 ILE B C     1 
ATOM   10768 O  O     . ILE B 1 648 ? 117.948 148.746 160.885 1.00 28.02 ?  648 ILE B O     1 
ATOM   10769 C  CB    . ILE B 1 648 ? 120.131 147.236 162.384 1.00 10.01 ?  648 ILE B CB    1 
ATOM   10770 C  CG1   . ILE B 1 648 ? 120.711 146.666 163.681 1.00 10.50 ?  648 ILE B CG1   1 
ATOM   10771 C  CG2   . ILE B 1 648 ? 121.173 147.203 161.285 1.00 3.67  ?  648 ILE B CG2   1 
ATOM   10772 C  CD1   . ILE B 1 648 ? 121.863 147.462 164.242 1.00 4.55  ?  648 ILE B CD1   1 
ATOM   10773 N  N     . ASP B 1 649 ? 119.613 150.271 160.775 1.00 7.88  ?  649 ASP B N     1 
ATOM   10774 C  CA    . ASP B 1 649 ? 119.025 150.922 159.607 1.00 9.36  ?  649 ASP B CA    1 
ATOM   10775 C  C     . ASP B 1 649 ? 119.167 150.070 158.354 1.00 7.99  ?  649 ASP B C     1 
ATOM   10776 O  O     . ASP B 1 649 ? 118.276 150.080 157.497 1.00 32.55 ?  649 ASP B O     1 
ATOM   10777 C  CB    . ASP B 1 649 ? 119.645 152.305 159.394 1.00 21.54 ?  649 ASP B CB    1 
ATOM   10778 C  CG    . ASP B 1 649 ? 121.159 152.279 159.383 1.00 16.61 ?  649 ASP B CG    1 
ATOM   10779 O  OD1   . ASP B 1 649 ? 121.764 152.537 160.442 1.00 20.43 ?  649 ASP B OD1   1 
ATOM   10780 O  OD2   . ASP B 1 649 ? 121.746 152.011 158.317 1.00 28.60 -1 649 ASP B OD2   1 
ATOM   10781 N  N     . GLN B 1 650 ? 120.267 149.342 158.223 1.00 10.05 ?  650 GLN B N     1 
ATOM   10782 C  CA    . GLN B 1 650 ? 120.430 148.355 157.167 1.00 2.07  ?  650 GLN B CA    1 
ATOM   10783 C  C     . GLN B 1 650 ? 119.957 147.000 157.692 1.00 5.15  ?  650 GLN B C     1 
ATOM   10784 O  O     . GLN B 1 650 ? 119.277 146.923 158.718 1.00 22.73 ?  650 GLN B O     1 
ATOM   10785 C  CB    . GLN B 1 650 ? 121.878 148.340 156.680 1.00 9.86  ?  650 GLN B CB    1 
ATOM   10786 C  CG    . GLN B 1 650 ? 122.337 149.655 156.095 1.00 8.84  ?  650 GLN B CG    1 
ATOM   10787 C  CD    . GLN B 1 650 ? 123.709 149.562 155.482 1.00 14.00 ?  650 GLN B CD    1 
ATOM   10788 O  OE1   . GLN B 1 650 ? 123.896 148.918 154.453 1.00 17.40 ?  650 GLN B OE1   1 
ATOM   10789 N  NE2   . GLN B 1 650 ? 124.683 150.211 156.107 1.00 8.23  ?  650 GLN B NE2   1 
ATOM   10790 N  N     . GLY B 1 651 ? 120.278 145.918 156.987 1.00 12.16 ?  651 GLY B N     1 
ATOM   10791 C  CA    . GLY B 1 651 ? 119.835 144.600 157.383 1.00 13.22 ?  651 GLY B CA    1 
ATOM   10792 C  C     . GLY B 1 651 ? 120.827 143.873 158.272 1.00 7.23  ?  651 GLY B C     1 
ATOM   10793 O  O     . GLY B 1 651 ? 121.864 144.396 158.674 1.00 12.16 ?  651 GLY B O     1 
ATOM   10794 N  N     . ILE B 1 652 ? 120.472 142.630 158.586 1.00 20.05 ?  652 ILE B N     1 
ATOM   10795 C  CA    . ILE B 1 652 ? 121.278 141.737 159.406 1.00 4.72  ?  652 ILE B CA    1 
ATOM   10796 C  C     . ILE B 1 652 ? 121.419 140.420 158.660 1.00 13.37 ?  652 ILE B C     1 
ATOM   10797 O  O     . ILE B 1 652 ? 120.435 139.901 158.122 1.00 24.03 ?  652 ILE B O     1 
ATOM   10798 C  CB    . ILE B 1 652 ? 120.647 141.502 160.793 1.00 2.58  ?  652 ILE B CB    1 
ATOM   10799 C  CG1   . ILE B 1 652 ? 120.439 142.825 161.527 1.00 3.36  ?  652 ILE B CG1   1 
ATOM   10800 C  CG2   . ILE B 1 652 ? 121.495 140.554 161.620 1.00 7.53  ?  652 ILE B CG2   1 
ATOM   10801 C  CD1   . ILE B 1 652 ? 119.642 142.686 162.796 1.00 8.68  ?  652 ILE B CD1   1 
ATOM   10802 N  N     . SER B 1 653 ? 122.633 139.882 158.621 1.00 14.90 ?  653 SER B N     1 
ATOM   10803 C  CA    . SER B 1 653 ? 122.867 138.580 158.002 1.00 13.87 ?  653 SER B CA    1 
ATOM   10804 C  C     . SER B 1 653 ? 122.221 137.509 158.871 1.00 20.31 ?  653 SER B C     1 
ATOM   10805 O  O     . SER B 1 653 ? 122.768 137.110 159.901 1.00 26.45 ?  653 SER B O     1 
ATOM   10806 C  CB    . SER B 1 653 ? 124.360 138.330 157.831 1.00 16.66 ?  653 SER B CB    1 
ATOM   10807 O  OG    . SER B 1 653 ? 124.775 138.643 156.516 1.00 22.31 ?  653 SER B OG    1 
ATOM   10808 N  N     . PHE B 1 654 ? 121.050 137.040 158.455 1.00 23.30 ?  654 PHE B N     1 
ATOM   10809 C  CA    . PHE B 1 654 ? 120.232 136.123 159.240 1.00 6.98  ?  654 PHE B CA    1 
ATOM   10810 C  C     . PHE B 1 654 ? 120.303 134.738 158.608 1.00 18.15 ?  654 PHE B C     1 
ATOM   10811 O  O     . PHE B 1 654 ? 119.665 134.483 157.582 1.00 27.86 ?  654 PHE B O     1 
ATOM   10812 C  CB    . PHE B 1 654 ? 118.792 136.626 159.314 1.00 13.53 ?  654 PHE B CB    1 
ATOM   10813 C  CG    . PHE B 1 654 ? 117.914 135.836 160.243 1.00 17.85 ?  654 PHE B CG    1 
ATOM   10814 C  CD1   . PHE B 1 654 ? 118.458 134.960 161.165 1.00 21.93 ?  654 PHE B CD1   1 
ATOM   10815 C  CD2   . PHE B 1 654 ? 116.543 135.979 160.195 1.00 20.97 ?  654 PHE B CD2   1 
ATOM   10816 C  CE1   . PHE B 1 654 ? 117.653 134.238 162.013 1.00 18.47 ?  654 PHE B CE1   1 
ATOM   10817 C  CE2   . PHE B 1 654 ? 115.732 135.261 161.044 1.00 24.46 ?  654 PHE B CE2   1 
ATOM   10818 C  CZ    . PHE B 1 654 ? 116.289 134.389 161.954 1.00 16.24 ?  654 PHE B CZ    1 
ATOM   10819 N  N     . THR B 1 655 ? 121.061 133.845 159.235 1.00 22.48 ?  655 THR B N     1 
ATOM   10820 C  CA    . THR B 1 655 ? 121.184 132.469 158.778 1.00 19.91 ?  655 THR B CA    1 
ATOM   10821 C  C     . THR B 1 655 ? 120.151 131.601 159.484 1.00 20.63 ?  655 THR B C     1 
ATOM   10822 O  O     . THR B 1 655 ? 120.010 131.664 160.708 1.00 29.03 ?  655 THR B O     1 
ATOM   10823 C  CB    . THR B 1 655 ? 122.593 131.938 159.047 1.00 29.28 ?  655 THR B CB    1 
ATOM   10824 O  OG1   . THR B 1 655 ? 123.542 132.688 158.280 1.00 35.51 ?  655 THR B OG1   1 
ATOM   10825 C  CG2   . THR B 1 655 ? 122.696 130.470 158.667 1.00 29.23 ?  655 THR B CG2   1 
ATOM   10826 N  N     . LEU B 1 656 ? 119.425 130.802 158.708 1.00 31.41 ?  656 LEU B N     1 
ATOM   10827 C  CA    . LEU B 1 656 ? 118.496 129.827 159.260 1.00 31.82 ?  656 LEU B CA    1 
ATOM   10828 C  C     . LEU B 1 656 ? 119.238 128.533 159.548 1.00 28.18 ?  656 LEU B C     1 
ATOM   10829 O  O     . LEU B 1 656 ? 119.914 127.988 158.671 1.00 33.03 ?  656 LEU B O     1 
ATOM   10830 C  CB    . LEU B 1 656 ? 117.339 129.567 158.295 1.00 34.25 ?  656 LEU B CB    1 
ATOM   10831 C  CG    . LEU B 1 656 ? 116.437 130.754 157.966 1.00 34.34 ?  656 LEU B CG    1 
ATOM   10832 C  CD1   . LEU B 1 656 ? 115.188 130.281 157.240 1.00 29.57 ?  656 LEU B CD1   1 
ATOM   10833 C  CD2   . LEU B 1 656 ? 116.075 131.525 159.224 1.00 25.37 ?  656 LEU B CD2   1 
ATOM   10834 N  N     . PHE B 1 657 ? 119.116 128.048 160.776 1.00 30.01 ?  657 PHE B N     1 
ATOM   10835 C  CA    . PHE B 1 657 ? 119.754 126.810 161.207 1.00 27.17 ?  657 PHE B CA    1 
ATOM   10836 C  C     . PHE B 1 657 ? 118.666 125.760 161.362 1.00 36.86 ?  657 PHE B C     1 
ATOM   10837 O  O     . PHE B 1 657 ? 117.840 125.843 162.276 1.00 39.95 ?  657 PHE B O     1 
ATOM   10838 C  CB    . PHE B 1 657 ? 120.525 127.023 162.505 1.00 31.39 ?  657 PHE B CB    1 
ATOM   10839 C  CG    . PHE B 1 657 ? 121.518 128.143 162.437 1.00 38.03 ?  657 PHE B CG    1 
ATOM   10840 C  CD1   . PHE B 1 657 ? 122.788 127.928 161.930 1.00 32.64 ?  657 PHE B CD1   1 
ATOM   10841 C  CD2   . PHE B 1 657 ? 121.180 129.412 162.872 1.00 35.57 ?  657 PHE B CD2   1 
ATOM   10842 C  CE1   . PHE B 1 657 ? 123.702 128.956 161.863 1.00 34.17 ?  657 PHE B CE1   1 
ATOM   10843 C  CE2   . PHE B 1 657 ? 122.092 130.444 162.807 1.00 34.07 ?  657 PHE B CE2   1 
ATOM   10844 C  CZ    . PHE B 1 657 ? 123.355 130.216 162.302 1.00 38.39 ?  657 PHE B CZ    1 
ATOM   10845 N  N     . LEU B 1 658 ? 118.669 124.775 160.470 1.00 40.65 ?  658 LEU B N     1 
ATOM   10846 C  CA    . LEU B 1 658 ? 117.592 123.805 160.368 1.00 41.19 ?  658 LEU B CA    1 
ATOM   10847 C  C     . LEU B 1 658 ? 118.106 122.407 160.677 1.00 45.56 ?  658 LEU B C     1 
ATOM   10848 O  O     . LEU B 1 658 ? 119.274 122.088 160.440 1.00 48.21 ?  658 LEU B O     1 
ATOM   10849 C  CB    . LEU B 1 658 ? 116.971 123.821 158.968 1.00 41.13 ?  658 LEU B CB    1 
ATOM   10850 C  CG    . LEU B 1 658 ? 116.861 125.193 158.303 1.00 40.87 ?  658 LEU B CG    1 
ATOM   10851 C  CD1   . LEU B 1 658 ? 116.785 125.044 156.797 1.00 38.06 ?  658 LEU B CD1   1 
ATOM   10852 C  CD2   . LEU B 1 658 ? 115.655 125.950 158.833 1.00 41.11 ?  658 LEU B CD2   1 
ATOM   10853 N  N     . LYS B 1 659 ? 117.223 121.581 161.222 1.00 49.14 ?  659 LYS B N     1 
ATOM   10854 C  CA    . LYS B 1 659 ? 117.507 120.168 161.404 1.00 50.62 ?  659 LYS B CA    1 
ATOM   10855 C  C     . LYS B 1 659 ? 117.190 119.404 160.123 1.00 52.29 ?  659 LYS B C     1 
ATOM   10856 O  O     . LYS B 1 659 ? 116.496 119.896 159.232 1.00 52.44 ?  659 LYS B O     1 
ATOM   10857 C  CB    . LYS B 1 659 ? 116.704 119.601 162.574 1.00 49.58 ?  659 LYS B CB    1 
ATOM   10858 C  CG    . LYS B 1 659 ? 117.053 120.219 163.913 1.00 52.09 ?  659 LYS B CG    1 
ATOM   10859 C  CD    . LYS B 1 659 ? 116.489 119.409 165.066 1.00 52.73 ?  659 LYS B CD    1 
ATOM   10860 C  CE    . LYS B 1 659 ? 116.925 119.983 166.405 1.00 51.17 ?  659 LYS B CE    1 
ATOM   10861 N  NZ    . LYS B 1 659 ? 116.756 119.006 167.515 1.00 53.28 1  659 LYS B NZ    1 
ATOM   10862 N  N     . ASP B 1 660 ? 117.724 118.184 160.036 1.00 57.27 ?  660 ASP B N     1 
ATOM   10863 C  CA    . ASP B 1 660 ? 117.432 117.341 158.881 1.00 56.83 ?  660 ASP B CA    1 
ATOM   10864 C  C     . ASP B 1 660 ? 115.970 116.916 158.853 1.00 55.41 ?  660 ASP B C     1 
ATOM   10865 O  O     . ASP B 1 660 ? 115.420 116.660 157.777 1.00 55.37 ?  660 ASP B O     1 
ATOM   10866 C  CB    . ASP B 1 660 ? 118.343 116.114 158.878 1.00 57.50 ?  660 ASP B CB    1 
ATOM   10867 C  CG    . ASP B 1 660 ? 118.298 115.348 160.187 1.00 58.83 ?  660 ASP B CG    1 
ATOM   10868 O  OD1   . ASP B 1 660 ? 117.838 115.919 161.199 1.00 57.20 ?  660 ASP B OD1   1 
ATOM   10869 O  OD2   . ASP B 1 660 ? 118.725 114.174 160.204 1.00 59.06 -1 660 ASP B OD2   1 
ATOM   10870 N  N     . THR B 1 661 ? 115.327 116.841 160.019 1.00 52.39 ?  661 THR B N     1 
ATOM   10871 C  CA    . THR B 1 661 ? 113.931 116.436 160.091 1.00 53.63 ?  661 THR B CA    1 
ATOM   10872 C  C     . THR B 1 661 ? 112.972 117.529 159.641 1.00 56.03 ?  661 THR B C     1 
ATOM   10873 O  O     . THR B 1 661 ? 111.803 117.232 159.366 1.00 54.76 ?  661 THR B O     1 
ATOM   10874 C  CB    . THR B 1 661 ? 113.580 116.011 161.518 1.00 54.73 ?  661 THR B CB    1 
ATOM   10875 O  OG1   . THR B 1 661 ? 113.850 117.094 162.417 1.00 52.56 ?  661 THR B OG1   1 
ATOM   10876 C  CG2   . THR B 1 661 ? 114.403 114.803 161.927 1.00 54.63 ?  661 THR B CG2   1 
ATOM   10877 N  N     . MET B 1 662 ? 113.429 118.774 159.561 1.00 55.39 ?  662 MET B N     1 
ATOM   10878 C  CA    . MET B 1 662 ? 112.553 119.867 159.167 1.00 51.19 ?  662 MET B CA    1 
ATOM   10879 C  C     . MET B 1 662 ? 112.153 119.731 157.703 1.00 52.53 ?  662 MET B C     1 
ATOM   10880 O  O     . MET B 1 662 ? 112.979 119.414 156.842 1.00 53.26 ?  662 MET B O     1 
ATOM   10881 C  CB    . MET B 1 662 ? 113.240 121.210 159.407 1.00 51.81 ?  662 MET B CB    1 
ATOM   10882 C  CG    . MET B 1 662 ? 112.843 121.872 160.715 1.00 51.85 ?  662 MET B CG    1 
ATOM   10883 S  SD    . MET B 1 662 ? 113.856 123.304 161.119 1.00 60.76 ?  662 MET B SD    1 
ATOM   10884 C  CE    . MET B 1 662 ? 112.754 124.196 162.212 1.00 51.82 ?  662 MET B CE    1 
ATOM   10885 N  N     . THR B 1 663 ? 110.875 119.971 157.428 1.00 48.30 ?  663 THR B N     1 
ATOM   10886 C  CA    . THR B 1 663 ? 110.329 119.812 156.092 1.00 45.04 ?  663 THR B CA    1 
ATOM   10887 C  C     . THR B 1 663 ? 110.397 121.131 155.325 1.00 46.54 ?  663 THR B C     1 
ATOM   10888 O  O     . THR B 1 663 ? 110.883 122.150 155.819 1.00 49.48 ?  663 THR B O     1 
ATOM   10889 C  CB    . THR B 1 663 ? 108.888 119.309 156.162 1.00 41.89 ?  663 THR B CB    1 
ATOM   10890 O  OG1   . THR B 1 663 ? 108.208 119.954 157.245 1.00 42.37 ?  663 THR B OG1   1 
ATOM   10891 C  CG2   . THR B 1 663 ? 108.858 117.808 156.387 1.00 44.20 ?  663 THR B CG2   1 
ATOM   10892 N  N     . THR B 1 664 ? 109.903 121.103 154.086 1.00 41.28 ?  664 THR B N     1 
ATOM   10893 C  CA    . THR B 1 664 ? 109.746 122.333 153.319 1.00 38.99 ?  664 THR B CA    1 
ATOM   10894 C  C     . THR B 1 664 ? 108.744 123.266 153.990 1.00 38.44 ?  664 THR B C     1 
ATOM   10895 O  O     . THR B 1 664 ? 108.941 124.488 154.021 1.00 41.92 ?  664 THR B O     1 
ATOM   10896 C  CB    . THR B 1 664 ? 109.313 121.995 151.889 1.00 41.98 ?  664 THR B CB    1 
ATOM   10897 O  OG1   . THR B 1 664 ? 110.455 121.575 151.129 1.00 40.54 ?  664 THR B OG1   1 
ATOM   10898 C  CG2   . THR B 1 664 ? 108.658 123.183 151.205 1.00 41.48 ?  664 THR B CG2   1 
ATOM   10899 N  N     . ARG B 1 665 ? 107.674 122.703 154.553 1.00 39.22 ?  665 ARG B N     1 
ATOM   10900 C  CA    . ARG B 1 665 ? 106.671 123.518 155.229 1.00 38.75 ?  665 ARG B CA    1 
ATOM   10901 C  C     . ARG B 1 665 ? 107.263 124.245 156.428 1.00 41.96 ?  665 ARG B C     1 
ATOM   10902 O  O     . ARG B 1 665 ? 106.891 125.387 156.708 1.00 47.88 ?  665 ARG B O     1 
ATOM   10903 C  CB    . ARG B 1 665 ? 105.492 122.649 155.664 1.00 40.49 ?  665 ARG B CB    1 
ATOM   10904 C  CG    . ARG B 1 665 ? 104.211 123.428 155.902 1.00 37.78 ?  665 ARG B CG    1 
ATOM   10905 C  CD    . ARG B 1 665 ? 103.273 122.674 156.825 1.00 41.85 ?  665 ARG B CD    1 
ATOM   10906 N  NE    . ARG B 1 665 ? 103.548 122.957 158.228 1.00 46.72 ?  665 ARG B NE    1 
ATOM   10907 C  CZ    . ARG B 1 665 ? 102.726 122.664 159.226 1.00 48.71 ?  665 ARG B CZ    1 
ATOM   10908 N  NH1   . ARG B 1 665 ? 101.565 122.067 159.013 1.00 43.92 1  665 ARG B NH1   1 
ATOM   10909 N  NH2   . ARG B 1 665 ? 103.079 122.978 160.470 1.00 46.34 ?  665 ARG B NH2   1 
ATOM   10910 N  N     . ASP B 1 666 ? 108.181 123.602 157.152 1.00 39.87 ?  666 ASP B N     1 
ATOM   10911 C  CA    . ASP B 1 666 ? 108.793 124.255 158.306 1.00 35.12 ?  666 ASP B CA    1 
ATOM   10912 C  C     . ASP B 1 666 ? 109.669 125.428 157.884 1.00 40.01 ?  666 ASP B C     1 
ATOM   10913 O  O     . ASP B 1 666 ? 109.641 126.491 158.518 1.00 42.48 ?  666 ASP B O     1 
ATOM   10914 C  CB    . ASP B 1 666 ? 109.600 123.241 159.114 1.00 42.29 ?  666 ASP B CB    1 
ATOM   10915 C  CG    . ASP B 1 666 ? 108.730 122.166 159.728 1.00 49.42 ?  666 ASP B CG    1 
ATOM   10916 O  OD1   . ASP B 1 666 ? 107.610 122.492 160.174 1.00 46.16 ?  666 ASP B OD1   1 
ATOM   10917 O  OD2   . ASP B 1 666 ? 109.164 120.996 159.768 1.00 50.89 -1 666 ASP B OD2   1 
ATOM   10918 N  N     . LEU B 1 667 ? 110.453 125.260 156.816 1.00 35.25 ?  667 LEU B N     1 
ATOM   10919 C  CA    . LEU B 1 667 ? 111.258 126.366 156.312 1.00 28.35 ?  667 LEU B CA    1 
ATOM   10920 C  C     . LEU B 1 667 ? 110.372 127.506 155.828 1.00 30.94 ?  667 LEU B C     1 
ATOM   10921 O  O     . LEU B 1 667 ? 110.664 128.683 156.078 1.00 32.33 ?  667 LEU B O     1 
ATOM   10922 C  CB    . LEU B 1 667 ? 112.172 125.878 155.188 1.00 31.84 ?  667 LEU B CB    1 
ATOM   10923 C  CG    . LEU B 1 667 ? 113.577 126.476 155.085 1.00 33.11 ?  667 LEU B CG    1 
ATOM   10924 C  CD1   . LEU B 1 667 ? 114.391 125.716 154.055 1.00 33.42 ?  667 LEU B CD1   1 
ATOM   10925 C  CD2   . LEU B 1 667 ? 113.542 127.953 154.741 1.00 38.02 ?  667 LEU B CD2   1 
ATOM   10926 N  N     . ASN B 1 668 ? 109.280 127.177 155.135 1.00 36.62 ?  668 ASN B N     1 
ATOM   10927 C  CA    . ASN B 1 668 ? 108.348 128.207 154.690 1.00 23.50 ?  668 ASN B CA    1 
ATOM   10928 C  C     . ASN B 1 668 ? 107.715 128.925 155.873 1.00 22.91 ?  668 ASN B C     1 
ATOM   10929 O  O     . ASN B 1 668 ? 107.516 130.143 155.834 1.00 31.40 ?  668 ASN B O     1 
ATOM   10930 C  CB    . ASN B 1 668 ? 107.273 127.591 153.798 1.00 28.51 ?  668 ASN B CB    1 
ATOM   10931 C  CG    . ASN B 1 668 ? 107.713 127.474 152.358 1.00 33.12 ?  668 ASN B CG    1 
ATOM   10932 O  OD1   . ASN B 1 668 ? 107.412 126.491 151.684 1.00 40.18 ?  668 ASN B OD1   1 
ATOM   10933 N  ND2   . ASN B 1 668 ? 108.431 128.481 151.875 1.00 30.35 ?  668 ASN B ND2   1 
ATOM   10934 N  N     . ARG B 1 669 ? 107.380 128.186 156.931 1.00 31.32 ?  669 ARG B N     1 
ATOM   10935 C  CA    . ARG B 1 669 ? 106.822 128.805 158.126 1.00 32.98 ?  669 ARG B CA    1 
ATOM   10936 C  C     . ARG B 1 669 ? 107.822 129.751 158.772 1.00 29.08 ?  669 ARG B C     1 
ATOM   10937 O  O     . ARG B 1 669 ? 107.453 130.840 159.225 1.00 28.03 ?  669 ARG B O     1 
ATOM   10938 C  CB    . ARG B 1 669 ? 106.386 127.729 159.119 1.00 32.09 ?  669 ARG B CB    1 
ATOM   10939 C  CG    . ARG B 1 669 ? 104.889 127.524 159.185 1.00 28.78 ?  669 ARG B CG    1 
ATOM   10940 C  CD    . ARG B 1 669 ? 104.514 126.555 160.293 1.00 33.13 ?  669 ARG B CD    1 
ATOM   10941 N  NE    . ARG B 1 669 ? 104.483 127.191 161.605 1.00 35.06 ?  669 ARG B NE    1 
ATOM   10942 C  CZ    . ARG B 1 669 ? 103.590 128.096 161.985 1.00 36.71 ?  669 ARG B CZ    1 
ATOM   10943 N  NH1   . ARG B 1 669 ? 102.621 128.495 161.178 1.00 35.18 1  669 ARG B NH1   1 
ATOM   10944 N  NH2   . ARG B 1 669 ? 103.667 128.609 163.209 1.00 38.29 ?  669 ARG B NH2   1 
ATOM   10945 N  N     . ILE B 1 670 ? 109.094 129.352 158.827 1.00 25.86 ?  670 ILE B N     1 
ATOM   10946 C  CA    . ILE B 1 670 ? 110.122 130.234 159.374 1.00 25.29 ?  670 ILE B CA    1 
ATOM   10947 C  C     . ILE B 1 670 ? 110.241 131.499 158.533 1.00 24.13 ?  670 ILE B C     1 
ATOM   10948 O  O     . ILE B 1 670 ? 110.326 132.610 159.068 1.00 27.90 ?  670 ILE B O     1 
ATOM   10949 C  CB    . ILE B 1 670 ? 111.469 129.496 159.481 1.00 32.05 ?  670 ILE B CB    1 
ATOM   10950 C  CG1   . ILE B 1 670 ? 111.372 128.341 160.476 1.00 31.60 ?  670 ILE B CG1   1 
ATOM   10951 C  CG2   . ILE B 1 670 ? 112.569 130.455 159.901 1.00 28.90 ?  670 ILE B CG2   1 
ATOM   10952 C  CD1   . ILE B 1 670 ? 112.385 127.249 160.232 1.00 27.50 ?  670 ILE B CD1   1 
ATOM   10953 N  N     . ASP B 1 671 ? 110.240 131.352 157.205 1.00 25.07 ?  671 ASP B N     1 
ATOM   10954 C  CA    . ASP B 1 671 ? 110.335 132.519 156.329 1.00 20.62 ?  671 ASP B CA    1 
ATOM   10955 C  C     . ASP B 1 671 ? 109.136 133.446 156.499 1.00 21.54 ?  671 ASP B C     1 
ATOM   10956 O  O     . ASP B 1 671 ? 109.289 134.671 156.539 1.00 30.77 ?  671 ASP B O     1 
ATOM   10957 C  CB    . ASP B 1 671 ? 110.464 132.076 154.872 1.00 21.88 ?  671 ASP B CB    1 
ATOM   10958 C  CG    . ASP B 1 671 ? 111.658 131.172 154.639 1.00 40.20 ?  671 ASP B CG    1 
ATOM   10959 O  OD1   . ASP B 1 671 ? 112.587 131.185 155.473 1.00 39.79 ?  671 ASP B OD1   1 
ATOM   10960 O  OD2   . ASP B 1 671 ? 111.667 130.446 153.622 1.00 39.34 -1 671 ASP B OD2   1 
ATOM   10961 N  N     . LEU B 1 672 ? 107.934 132.878 156.606 1.00 21.76 ?  672 LEU B N     1 
ATOM   10962 C  CA    . LEU B 1 672 ? 106.736 133.697 156.741 1.00 16.89 ?  672 LEU B CA    1 
ATOM   10963 C  C     . LEU B 1 672 ? 106.658 134.365 158.106 1.00 18.59 ?  672 LEU B C     1 
ATOM   10964 O  O     . LEU B 1 672 ? 106.141 135.482 158.217 1.00 24.78 ?  672 LEU B O     1 
ATOM   10965 C  CB    . LEU B 1 672 ? 105.489 132.852 156.492 1.00 24.55 ?  672 LEU B CB    1 
ATOM   10966 C  CG    . LEU B 1 672 ? 105.327 132.328 155.065 1.00 24.78 ?  672 LEU B CG    1 
ATOM   10967 C  CD1   . LEU B 1 672 ? 104.333 131.182 155.025 1.00 20.61 ?  672 LEU B CD1   1 
ATOM   10968 C  CD2   . LEU B 1 672 ? 104.911 133.448 154.126 1.00 23.39 ?  672 LEU B CD2   1 
ATOM   10969 N  N     . TYR B 1 673 ? 107.154 133.708 159.155 1.00 22.69 ?  673 TYR B N     1 
ATOM   10970 C  CA    . TYR B 1 673 ? 107.200 134.348 160.464 1.00 14.92 ?  673 TYR B CA    1 
ATOM   10971 C  C     . TYR B 1 673 ? 108.253 135.447 160.497 1.00 18.79 ?  673 TYR B C     1 
ATOM   10972 O  O     . TYR B 1 673 ? 108.067 136.473 161.162 1.00 25.74 ?  673 TYR B O     1 
ATOM   10973 C  CB    . TYR B 1 673 ? 107.471 133.313 161.551 1.00 19.00 ?  673 TYR B CB    1 
ATOM   10974 C  CG    . TYR B 1 673 ? 107.499 133.898 162.943 1.00 20.29 ?  673 TYR B CG    1 
ATOM   10975 C  CD1   . TYR B 1 673 ? 106.367 134.479 163.494 1.00 22.11 ?  673 TYR B CD1   1 
ATOM   10976 C  CD2   . TYR B 1 673 ? 108.657 133.869 163.704 1.00 15.22 ?  673 TYR B CD2   1 
ATOM   10977 C  CE1   . TYR B 1 673 ? 106.387 135.013 164.763 1.00 20.83 ?  673 TYR B CE1   1 
ATOM   10978 C  CE2   . TYR B 1 673 ? 108.688 134.400 164.973 1.00 24.30 ?  673 TYR B CE2   1 
ATOM   10979 C  CZ    . TYR B 1 673 ? 107.551 134.970 165.499 1.00 25.45 ?  673 TYR B CZ    1 
ATOM   10980 O  OH    . TYR B 1 673 ? 107.579 135.503 166.766 1.00 29.84 ?  673 TYR B OH    1 
ATOM   10981 N  N     . ALA B 1 674 ? 109.371 135.245 159.798 1.00 21.72 ?  674 ALA B N     1 
ATOM   10982 C  CA    . ALA B 1 674 ? 110.356 136.310 159.658 1.00 12.28 ?  674 ALA B CA    1 
ATOM   10983 C  C     . ALA B 1 674 ? 109.759 137.508 158.932 1.00 17.86 ?  674 ALA B C     1 
ATOM   10984 O  O     . ALA B 1 674 ? 109.947 138.655 159.351 1.00 30.35 ?  674 ALA B O     1 
ATOM   10985 C  CB    . ALA B 1 674 ? 111.587 135.786 158.921 1.00 10.16 ?  674 ALA B CB    1 
ATOM   10986 N  N     . HIS B 1 675 ? 109.020 137.257 157.853 1.00 15.42 ?  675 HIS B N     1 
ATOM   10987 C  CA    . HIS B 1 675 ? 108.335 138.340 157.154 1.00 16.56 ?  675 HIS B CA    1 
ATOM   10988 C  C     . HIS B 1 675 ? 107.327 139.032 158.065 1.00 21.20 ?  675 HIS B C     1 
ATOM   10989 O  O     . HIS B 1 675 ? 107.205 140.261 158.048 1.00 26.90 ?  675 HIS B O     1 
ATOM   10990 C  CB    . HIS B 1 675 ? 107.647 137.798 155.903 1.00 18.38 ?  675 HIS B CB    1 
ATOM   10991 C  CG    . HIS B 1 675 ? 106.785 138.803 155.206 1.00 21.58 ?  675 HIS B CG    1 
ATOM   10992 N  ND1   . HIS B 1 675 ? 105.435 138.926 155.457 1.00 27.58 ?  675 HIS B ND1   1 
ATOM   10993 C  CD2   . HIS B 1 675 ? 107.079 139.735 154.271 1.00 15.77 ?  675 HIS B CD2   1 
ATOM   10994 C  CE1   . HIS B 1 675 ? 104.936 139.890 154.707 1.00 25.50 ?  675 HIS B CE1   1 
ATOM   10995 N  NE2   . HIS B 1 675 ? 105.913 140.397 153.977 1.00 29.27 ?  675 HIS B NE2   1 
ATOM   10996 N  N     . HIS B 1 676 ? 106.595 138.254 158.862 1.00 22.09 ?  676 HIS B N     1 
ATOM   10997 C  CA    . HIS B 1 676 ? 105.596 138.821 159.761 1.00 20.05 ?  676 HIS B CA    1 
ATOM   10998 C  C     . HIS B 1 676 ? 106.240 139.677 160.844 1.00 26.00 ?  676 HIS B C     1 
ATOM   10999 O  O     . HIS B 1 676 ? 105.685 140.706 161.242 1.00 25.33 ?  676 HIS B O     1 
ATOM   11000 C  CB    . HIS B 1 676 ? 104.769 137.698 160.385 1.00 24.17 ?  676 HIS B CB    1 
ATOM   11001 C  CG    . HIS B 1 676 ? 103.840 138.158 161.466 1.00 22.97 ?  676 HIS B CG    1 
ATOM   11002 N  ND1   . HIS B 1 676 ? 102.800 139.032 161.233 1.00 21.33 ?  676 HIS B ND1   1 
ATOM   11003 C  CD2   . HIS B 1 676 ? 103.794 137.863 162.786 1.00 25.21 ?  676 HIS B CD2   1 
ATOM   11004 C  CE1   . HIS B 1 676 ? 102.154 139.254 162.362 1.00 28.69 ?  676 HIS B CE1   1 
ATOM   11005 N  NE2   . HIS B 1 676 ? 102.738 138.558 163.320 1.00 27.27 ?  676 HIS B NE2   1 
ATOM   11006 N  N     . ARG B 1 677 ? 107.409 139.270 161.330 1.00 24.54 ?  677 ARG B N     1 
ATOM   11007 C  CA    . ARG B 1 677 ? 108.071 139.944 162.437 1.00 19.48 ?  677 ARG B CA    1 
ATOM   11008 C  C     . ARG B 1 677 ? 108.926 141.123 161.996 1.00 23.24 ?  677 ARG B C     1 
ATOM   11009 O  O     . ARG B 1 677 ? 109.566 141.754 162.843 1.00 30.96 ?  677 ARG B O     1 
ATOM   11010 C  CB    . ARG B 1 677 ? 108.931 138.949 163.217 1.00 19.00 ?  677 ARG B CB    1 
ATOM   11011 C  CG    . ARG B 1 677 ? 108.150 138.101 164.196 1.00 19.85 ?  677 ARG B CG    1 
ATOM   11012 C  CD    . ARG B 1 677 ? 107.612 138.937 165.340 1.00 23.48 ?  677 ARG B CD    1 
ATOM   11013 N  NE    . ARG B 1 677 ? 108.609 139.120 166.387 1.00 30.10 ?  677 ARG B NE    1 
ATOM   11014 C  CZ    . ARG B 1 677 ? 109.040 140.300 166.809 1.00 34.53 ?  677 ARG B CZ    1 
ATOM   11015 N  NH1   . ARG B 1 677 ? 108.581 141.428 166.294 1.00 29.29 1  677 ARG B NH1   1 
ATOM   11016 N  NH2   . ARG B 1 677 ? 109.958 140.349 167.769 1.00 29.06 ?  677 ARG B NH2   1 
ATOM   11017 N  N     . GLY B 1 678 ? 108.957 141.435 160.706 1.00 22.05 ?  678 GLY B N     1 
ATOM   11018 C  CA    . GLY B 1 678 ? 109.725 142.558 160.218 1.00 12.98 ?  678 GLY B CA    1 
ATOM   11019 C  C     . GLY B 1 678 ? 111.143 142.245 159.807 1.00 16.33 ?  678 GLY B C     1 
ATOM   11020 O  O     . GLY B 1 678 ? 111.942 143.175 159.650 1.00 24.40 ?  678 GLY B O     1 
ATOM   11021 N  N     . ILE B 1 679 ? 111.487 140.968 159.634 1.00 18.05 ?  679 ILE B N     1 
ATOM   11022 C  CA    . ILE B 1 679 ? 112.821 140.613 159.170 1.00 15.19 ?  679 ILE B CA    1 
ATOM   11023 C  C     . ILE B 1 679 ? 113.003 141.124 157.750 1.00 21.06 ?  679 ILE B C     1 
ATOM   11024 O  O     . ILE B 1 679 ? 112.126 140.955 156.894 1.00 28.13 ?  679 ILE B O     1 
ATOM   11025 C  CB    . ILE B 1 679 ? 113.033 139.095 159.261 1.00 13.44 ?  679 ILE B CB    1 
ATOM   11026 C  CG1   . ILE B 1 679 ? 113.080 138.645 160.724 1.00 13.99 ?  679 ILE B CG1   1 
ATOM   11027 C  CG2   . ILE B 1 679 ? 114.291 138.673 158.524 1.00 15.28 ?  679 ILE B CG2   1 
ATOM   11028 C  CD1   . ILE B 1 679 ? 114.203 139.251 161.507 1.00 18.66 ?  679 ILE B CD1   1 
ATOM   11029 N  N     . LYS B 1 680 ? 114.137 141.770 157.498 1.00 10.64 ?  680 LYS B N     1 
ATOM   11030 C  CA    . LYS B 1 680 ? 114.393 142.371 156.197 1.00 5.62  ?  680 LYS B CA    1 
ATOM   11031 C  C     . LYS B 1 680 ? 114.984 141.373 155.207 1.00 0.15  ?  680 LYS B C     1 
ATOM   11032 O  O     . LYS B 1 680 ? 114.551 141.307 154.056 1.00 19.15 ?  680 LYS B O     1 
ATOM   11033 C  CB    . LYS B 1 680 ? 115.325 143.573 156.352 1.00 11.81 ?  680 LYS B CB    1 
ATOM   11034 C  CG    . LYS B 1 680 ? 114.740 144.719 157.148 1.00 0.00  ?  680 LYS B CG    1 
ATOM   11035 C  CD    . LYS B 1 680 ? 115.670 145.913 157.127 1.00 2.10  ?  680 LYS B CD    1 
ATOM   11036 C  CE    . LYS B 1 680 ? 115.254 146.950 158.146 1.00 12.27 ?  680 LYS B CE    1 
ATOM   11037 N  NZ    . LYS B 1 680 ? 116.110 148.162 158.091 1.00 15.62 1  680 LYS B NZ    1 
ATOM   11038 N  N     . THR B 1 681 ? 115.978 140.601 155.636 1.00 6.84  ?  681 THR B N     1 
ATOM   11039 C  CA    . THR B 1 681 ? 116.641 139.647 154.763 1.00 7.07  ?  681 THR B CA    1 
ATOM   11040 C  C     . THR B 1 681 ? 116.859 138.340 155.507 1.00 12.62 ?  681 THR B C     1 
ATOM   11041 O  O     . THR B 1 681 ? 116.980 138.317 156.734 1.00 25.64 ?  681 THR B O     1 
ATOM   11042 C  CB    . THR B 1 681 ? 117.992 140.177 154.248 1.00 13.07 ?  681 THR B CB    1 
ATOM   11043 O  OG1   . THR B 1 681 ? 118.751 140.710 155.340 1.00 29.37 ?  681 THR B OG1   1 
ATOM   11044 C  CG2   . THR B 1 681 ? 117.791 141.261 153.205 1.00 7.92  ?  681 THR B CG2   1 
ATOM   11045 N  N     . ILE B 1 682 ? 116.907 137.248 154.750 1.00 13.30 ?  682 ILE B N     1 
ATOM   11046 C  CA    . ILE B 1 682 ? 117.278 135.937 155.265 1.00 8.69  ?  682 ILE B CA    1 
ATOM   11047 C  C     . ILE B 1 682 ? 118.491 135.456 154.482 1.00 17.51 ?  682 ILE B C     1 
ATOM   11048 O  O     . ILE B 1 682 ? 118.452 135.385 153.249 1.00 13.41 ?  682 ILE B O     1 
ATOM   11049 C  CB    . ILE B 1 682 ? 116.120 134.930 155.160 1.00 11.16 ?  682 ILE B CB    1 
ATOM   11050 C  CG1   . ILE B 1 682 ? 114.879 135.471 155.870 1.00 19.69 ?  682 ILE B CG1   1 
ATOM   11051 C  CG2   . ILE B 1 682 ? 116.528 133.609 155.764 1.00 18.50 ?  682 ILE B CG2   1 
ATOM   11052 C  CD1   . ILE B 1 682 ? 113.752 134.472 155.976 1.00 21.11 ?  682 ILE B CD1   1 
ATOM   11053 N  N     . TYR B 1 683 ? 119.567 135.131 155.198 1.00 23.45 ?  683 TYR B N     1 
ATOM   11054 C  CA    . TYR B 1 683 ? 120.841 134.847 154.539 1.00 18.72 ?  683 TYR B CA    1 
ATOM   11055 C  C     . TYR B 1 683 ? 120.922 133.409 154.036 1.00 21.31 ?  683 TYR B C     1 
ATOM   11056 O  O     . TYR B 1 683 ? 120.967 133.161 152.830 1.00 36.30 ?  683 TYR B O     1 
ATOM   11057 C  CB    . TYR B 1 683 ? 121.993 135.149 155.501 1.00 18.95 ?  683 TYR B CB    1 
ATOM   11058 C  CG    . TYR B 1 683 ? 123.364 135.114 154.873 1.00 13.76 ?  683 TYR B CG    1 
ATOM   11059 C  CD1   . TYR B 1 683 ? 123.530 135.307 153.509 1.00 10.60 ?  683 TYR B CD1   1 
ATOM   11060 C  CD2   . TYR B 1 683 ? 124.496 134.895 155.645 1.00 10.01 ?  683 TYR B CD2   1 
ATOM   11061 C  CE1   . TYR B 1 683 ? 124.778 135.278 152.934 1.00 19.38 ?  683 TYR B CE1   1 
ATOM   11062 C  CE2   . TYR B 1 683 ? 125.751 134.866 155.076 1.00 19.11 ?  683 TYR B CE2   1 
ATOM   11063 C  CZ    . TYR B 1 683 ? 125.886 135.060 153.720 1.00 21.30 ?  683 TYR B CZ    1 
ATOM   11064 O  OH    . TYR B 1 683 ? 127.134 135.031 153.143 1.00 23.65 ?  683 TYR B OH    1 
ATOM   11065 N  N     . TYR B 1 684 ? 120.914 132.444 154.947 1.00 29.13 ?  684 TYR B N     1 
ATOM   11066 C  CA    . TYR B 1 684 ? 121.256 131.080 154.585 1.00 22.22 ?  684 TYR B CA    1 
ATOM   11067 C  C     . TYR B 1 684 ? 120.337 130.108 155.301 1.00 37.02 ?  684 TYR B C     1 
ATOM   11068 O  O     . TYR B 1 684 ? 119.860 130.377 156.405 1.00 37.92 ?  684 TYR B O     1 
ATOM   11069 C  CB    . TYR B 1 684 ? 122.712 130.752 154.939 1.00 24.34 ?  684 TYR B CB    1 
ATOM   11070 C  CG    . TYR B 1 684 ? 123.675 130.873 153.785 1.00 25.68 ?  684 TYR B CG    1 
ATOM   11071 C  CD1   . TYR B 1 684 ? 123.322 130.448 152.513 1.00 26.99 ?  684 TYR B CD1   1 
ATOM   11072 C  CD2   . TYR B 1 684 ? 124.940 131.408 153.971 1.00 30.41 ?  684 TYR B CD2   1 
ATOM   11073 C  CE1   . TYR B 1 684 ? 124.203 130.556 151.456 1.00 33.90 ?  684 TYR B CE1   1 
ATOM   11074 C  CE2   . TYR B 1 684 ? 125.828 131.521 152.922 1.00 25.07 ?  684 TYR B CE2   1 
ATOM   11075 C  CZ    . TYR B 1 684 ? 125.455 131.094 151.667 1.00 30.64 ?  684 TYR B CZ    1 
ATOM   11076 O  OH    . TYR B 1 684 ? 126.338 131.204 150.618 1.00 35.44 ?  684 TYR B OH    1 
ATOM   11077 N  N     . ALA B 1 685 ? 120.101 128.974 154.657 1.00 37.12 ?  685 ALA B N     1 
ATOM   11078 C  CA    . ALA B 1 685 ? 119.401 127.847 155.259 1.00 33.67 ?  685 ALA B CA    1 
ATOM   11079 C  C     . ALA B 1 685 ? 120.451 126.763 155.491 1.00 34.24 ?  685 ALA B C     1 
ATOM   11080 O  O     . ALA B 1 685 ? 120.787 125.998 154.586 1.00 42.25 ?  685 ALA B O     1 
ATOM   11081 C  CB    . ALA B 1 685 ? 118.265 127.363 154.370 1.00 31.43 ?  685 ALA B CB    1 
ATOM   11082 N  N     . ARG B 1 686 ? 120.973 126.709 156.712 1.00 32.67 ?  686 ARG B N     1 
ATOM   11083 C  CA    . ARG B 1 686 ? 121.980 125.723 157.080 1.00 38.58 ?  686 ARG B CA    1 
ATOM   11084 C  C     . ARG B 1 686 ? 121.298 124.545 157.760 1.00 41.88 ?  686 ARG B C     1 
ATOM   11085 O  O     . ARG B 1 686 ? 120.632 124.714 158.788 1.00 42.46 ?  686 ARG B O     1 
ATOM   11086 C  CB    . ARG B 1 686 ? 123.034 126.341 157.997 1.00 40.04 ?  686 ARG B CB    1 
ATOM   11087 C  CG    . ARG B 1 686 ? 124.125 127.090 157.260 1.00 40.60 ?  686 ARG B CG    1 
ATOM   11088 C  CD    . ARG B 1 686 ? 125.370 127.232 158.118 1.00 44.30 ?  686 ARG B CD    1 
ATOM   11089 N  NE    . ARG B 1 686 ? 126.205 126.039 158.073 1.00 46.43 ?  686 ARG B NE    1 
ATOM   11090 C  CZ    . ARG B 1 686 ? 127.531 126.054 158.031 1.00 48.20 ?  686 ARG B CZ    1 
ATOM   11091 N  NH1   . ARG B 1 686 ? 128.208 127.191 158.007 1.00 43.79 1  686 ARG B NH1   1 
ATOM   11092 N  NH2   . ARG B 1 686 ? 128.194 124.902 158.009 1.00 47.81 ?  686 ARG B NH2   1 
ATOM   11093 N  N     . THR B 1 687 ? 121.463 123.356 157.190 1.00 46.89 ?  687 THR B N     1 
ATOM   11094 C  CA    . THR B 1 687 ? 120.832 122.146 157.692 1.00 50.40 ?  687 THR B CA    1 
ATOM   11095 C  C     . THR B 1 687 ? 121.871 121.254 158.358 1.00 49.85 ?  687 THR B C     1 
ATOM   11096 O  O     . THR B 1 687 ? 122.992 121.112 157.861 1.00 51.44 ?  687 THR B O     1 
ATOM   11097 C  CB    . THR B 1 687 ? 120.132 121.382 156.565 1.00 47.33 ?  687 THR B CB    1 
ATOM   11098 O  OG1   . THR B 1 687 ? 119.510 122.311 155.669 1.00 44.31 ?  687 THR B OG1   1 
ATOM   11099 C  CG2   . THR B 1 687 ? 119.075 120.451 157.131 1.00 45.39 ?  687 THR B CG2   1 
ATOM   11100 N  N     . LYS B 1 688 ? 121.492 120.660 159.484 1.00 47.38 ?  688 LYS B N     1 
ATOM   11101 C  CA    . LYS B 1 688 ? 122.379 119.760 160.211 1.00 49.75 ?  688 LYS B CA    1 
ATOM   11102 C  C     . LYS B 1 688 ? 122.185 118.319 159.754 1.00 54.70 ?  688 LYS B C     1 
ATOM   11103 O  O     . LYS B 1 688 ? 121.057 117.864 159.569 1.00 55.57 ?  688 LYS B O     1 
ATOM   11104 C  CB    . LYS B 1 688 ? 122.138 119.869 161.717 1.00 47.73 ?  688 LYS B CB    1 
ATOM   11105 C  CG    . LYS B 1 688 ? 123.199 119.187 162.561 1.00 49.97 ?  688 LYS B CG    1 
ATOM   11106 C  CD    . LYS B 1 688 ? 123.175 119.694 163.990 1.00 50.55 ?  688 LYS B CD    1 
ATOM   11107 C  CE    . LYS B 1 688 ? 124.372 119.185 164.775 1.00 52.82 ?  688 LYS B CE    1 
ATOM   11108 N  NZ    . LYS B 1 688 ? 124.415 119.759 166.148 1.00 54.26 ?  688 LYS B NZ    1 
ATOM   11109 N  N     . ASP C 2 37  ? 135.964 81.753  114.417 1.00 45.99 ?  16  ASP C N     1 
ATOM   11110 C  CA    . ASP C 2 37  ? 136.089 82.286  113.056 1.00 45.47 ?  16  ASP C CA    1 
ATOM   11111 C  C     . ASP C 2 37  ? 135.412 83.640  112.841 1.00 44.13 ?  16  ASP C C     1 
ATOM   11112 O  O     . ASP C 2 37  ? 135.535 84.228  111.765 1.00 44.46 ?  16  ASP C O     1 
ATOM   11113 C  CB    . ASP C 2 37  ? 135.527 81.278  112.052 1.00 45.90 ?  16  ASP C CB    1 
ATOM   11114 C  CG    . ASP C 2 37  ? 136.072 79.886  112.265 1.00 47.25 ?  16  ASP C CG    1 
ATOM   11115 O  OD1   . ASP C 2 37  ? 137.276 79.756  112.574 1.00 47.99 ?  16  ASP C OD1   1 
ATOM   11116 O  OD2   . ASP C 2 37  ? 135.291 78.923  112.125 1.00 49.50 -1 16  ASP C OD2   1 
ATOM   11117 N  N     . PHE C 2 38  ? 134.706 84.136  113.853 1.00 42.17 ?  17  PHE C N     1 
ATOM   11118 C  CA    . PHE C 2 38  ? 133.840 85.305  113.659 1.00 40.67 ?  17  PHE C CA    1 
ATOM   11119 C  C     . PHE C 2 38  ? 133.922 86.426  114.701 1.00 39.46 ?  17  PHE C C     1 
ATOM   11120 O  O     . PHE C 2 38  ? 133.585 87.572  114.393 1.00 39.17 ?  17  PHE C O     1 
ATOM   11121 C  CB    . PHE C 2 38  ? 132.378 84.856  113.481 1.00 40.24 ?  17  PHE C CB    1 
ATOM   11122 C  CG    . PHE C 2 38  ? 131.858 83.987  114.603 1.00 39.58 ?  17  PHE C CG    1 
ATOM   11123 C  CD1   . PHE C 2 38  ? 131.304 84.559  115.748 1.00 38.78 ?  17  PHE C CD1   1 
ATOM   11124 C  CD2   . PHE C 2 38  ? 131.908 82.596  114.507 1.00 39.43 ?  17  PHE C CD2   1 
ATOM   11125 C  CE1   . PHE C 2 38  ? 130.812 83.763  116.783 1.00 38.07 ?  17  PHE C CE1   1 
ATOM   11126 C  CE2   . PHE C 2 38  ? 131.419 81.788  115.538 1.00 39.10 ?  17  PHE C CE2   1 
ATOM   11127 C  CZ    . PHE C 2 38  ? 130.871 82.375  116.680 1.00 38.63 ?  17  PHE C CZ    1 
ATOM   11128 N  N     . THR C 2 39  ? 134.356 86.107  115.922 1.00 38.22 ?  18  THR C N     1 
ATOM   11129 C  CA    . THR C 2 39  ? 134.326 87.089  117.020 1.00 37.09 ?  18  THR C CA    1 
ATOM   11130 C  C     . THR C 2 39  ? 135.097 88.379  116.695 1.00 36.84 ?  18  THR C C     1 
ATOM   11131 O  O     . THR C 2 39  ? 134.587 89.486  116.930 1.00 36.13 ?  18  THR C O     1 
ATOM   11132 C  CB    . THR C 2 39  ? 134.741 86.479  118.391 1.00 36.59 ?  18  THR C CB    1 
ATOM   11133 O  OG1   . THR C 2 39  ? 133.676 85.657  118.877 1.00 36.50 ?  18  THR C OG1   1 
ATOM   11134 C  CG2   . THR C 2 39  ? 134.989 87.563  119.421 1.00 36.06 ?  18  THR C CG2   1 
ATOM   11135 N  N     . GLN C 2 40  ? 136.304 88.234  116.138 1.00 37.01 ?  19  GLN C N     1 
ATOM   11136 C  CA    . GLN C 2 40  ? 137.138 89.396  115.799 1.00 37.33 ?  19  GLN C CA    1 
ATOM   11137 C  C     . GLN C 2 40  ? 136.461 90.359  114.839 1.00 36.63 ?  19  GLN C C     1 
ATOM   11138 O  O     . GLN C 2 40  ? 136.527 91.573  115.028 1.00 36.10 ?  19  GLN C O     1 
ATOM   11139 C  CB    . GLN C 2 40  ? 138.503 88.983  115.249 1.00 38.24 ?  19  GLN C CB    1 
ATOM   11140 C  CG    . GLN C 2 40  ? 139.499 88.655  116.338 1.00 41.33 ?  19  GLN C CG    1 
ATOM   11141 C  CD    . GLN C 2 40  ? 140.917 89.069  115.995 1.00 45.15 ?  19  GLN C CD    1 
ATOM   11142 O  OE1   . GLN C 2 40  ? 141.332 89.028  114.830 1.00 47.33 ?  19  GLN C OE1   1 
ATOM   11143 N  NE2   . GLN C 2 40  ? 141.675 89.470  117.014 1.00 46.51 ?  19  GLN C NE2   1 
ATOM   11144 N  N     . MET C 2 41  ? 135.799 89.816  113.821 1.00 36.23 ?  20  MET C N     1 
ATOM   11145 C  CA    . MET C 2 41  ? 135.085 90.657  112.870 1.00 36.40 ?  20  MET C CA    1 
ATOM   11146 C  C     . MET C 2 41  ? 133.837 91.306  113.498 1.00 34.93 ?  20  MET C C     1 
ATOM   11147 O  O     . MET C 2 41  ? 133.510 92.445  113.174 1.00 34.20 ?  20  MET C O     1 
ATOM   11148 C  CB    . MET C 2 41  ? 134.818 89.924  111.537 1.00 37.35 ?  20  MET C CB    1 
ATOM   11149 C  CG    . MET C 2 41  ? 133.559 89.085  111.432 1.00 40.49 ?  20  MET C CG    1 
ATOM   11150 S  SD    . MET C 2 41  ? 133.322 88.497  109.725 1.00 48.68 ?  20  MET C SD    1 
ATOM   11151 C  CE    . MET C 2 41  ? 134.297 86.987  109.728 1.00 47.17 ?  20  MET C CE    1 
ATOM   11152 N  N     . PHE C 2 42  ? 133.180 90.605  114.426 1.00 33.75 ?  21  PHE C N     1 
ATOM   11153 C  CA    . PHE C 2 42  ? 132.083 91.216  115.192 1.00 32.62 ?  21  PHE C CA    1 
ATOM   11154 C  C     . PHE C 2 42  ? 132.582 92.285  116.158 1.00 32.59 ?  21  PHE C C     1 
ATOM   11155 O  O     . PHE C 2 42  ? 131.944 93.329  116.318 1.00 32.23 ?  21  PHE C O     1 
ATOM   11156 C  CB    . PHE C 2 42  ? 131.244 90.164  115.916 1.00 32.12 ?  21  PHE C CB    1 
ATOM   11157 C  CG    . PHE C 2 42  ? 130.218 89.510  115.039 1.00 31.04 ?  21  PHE C CG    1 
ATOM   11158 C  CD1   . PHE C 2 42  ? 128.911 89.995  114.992 1.00 30.75 ?  21  PHE C CD1   1 
ATOM   11159 C  CD2   . PHE C 2 42  ? 130.554 88.415  114.251 1.00 30.99 ?  21  PHE C CD2   1 
ATOM   11160 C  CE1   . PHE C 2 42  ? 127.951 89.392  114.172 1.00 30.30 ?  21  PHE C CE1   1 
ATOM   11161 C  CE2   . PHE C 2 42  ? 129.601 87.801  113.422 1.00 30.74 ?  21  PHE C CE2   1 
ATOM   11162 C  CZ    . PHE C 2 42  ? 128.300 88.291  113.384 1.00 30.48 ?  21  PHE C CZ    1 
ATOM   11163 N  N     . TYR C 2 43  ? 133.727 92.025  116.788 1.00 32.33 ?  22  TYR C N     1 
ATOM   11164 C  CA    . TYR C 2 43  ? 134.365 93.022  117.643 1.00 32.50 ?  22  TYR C CA    1 
ATOM   11165 C  C     . TYR C 2 43  ? 134.612 94.312  116.864 1.00 33.01 ?  22  TYR C C     1 
ATOM   11166 O  O     . TYR C 2 43  ? 134.226 95.396  117.311 1.00 32.50 ?  22  TYR C O     1 
ATOM   11167 C  CB    . TYR C 2 43  ? 135.674 92.497  118.265 1.00 32.53 ?  22  TYR C CB    1 
ATOM   11168 C  CG    . TYR C 2 43  ? 136.467 93.596  118.950 1.00 33.27 ?  22  TYR C CG    1 
ATOM   11169 C  CD1   . TYR C 2 43  ? 136.142 94.018  120.242 1.00 32.34 ?  22  TYR C CD1   1 
ATOM   11170 C  CD2   . TYR C 2 43  ? 137.514 94.241  118.288 1.00 33.71 ?  22  TYR C CD2   1 
ATOM   11171 C  CE1   . TYR C 2 43  ? 136.854 95.042  120.866 1.00 33.58 ?  22  TYR C CE1   1 
ATOM   11172 C  CE2   . TYR C 2 43  ? 138.231 95.272  118.897 1.00 35.12 ?  22  TYR C CE2   1 
ATOM   11173 C  CZ    . TYR C 2 43  ? 137.898 95.664  120.188 1.00 35.30 ?  22  TYR C CZ    1 
ATOM   11174 O  OH    . TYR C 2 43  ? 138.607 96.680  120.789 1.00 36.54 ?  22  TYR C OH    1 
ATOM   11175 N  N     . ASN C 2 44  ? 135.240 94.182  115.692 1.00 33.80 ?  23  ASN C N     1 
ATOM   11176 C  CA    . ASN C 2 44  ? 135.559 95.330  114.854 1.00 34.80 ?  23  ASN C CA    1 
ATOM   11177 C  C     . ASN C 2 44  ? 134.304 96.057  114.374 1.00 34.40 ?  23  ASN C C     1 
ATOM   11178 O  O     . ASN C 2 44  ? 134.256 97.282  114.387 1.00 33.99 ?  23  ASN C O     1 
ATOM   11179 C  CB    . ASN C 2 44  ? 136.442 94.920  113.665 1.00 35.46 ?  23  ASN C CB    1 
ATOM   11180 C  CG    . ASN C 2 44  ? 137.811 94.371  114.095 1.00 38.28 ?  23  ASN C CG    1 
ATOM   11181 O  OD1   . ASN C 2 44  ? 138.314 94.662  115.190 1.00 41.01 ?  23  ASN C OD1   1 
ATOM   11182 N  ND2   . ASN C 2 44  ? 138.423 93.576  113.218 1.00 39.13 ?  23  ASN C ND2   1 
ATOM   11183 N  N     . GLN C 2 45  ? 133.287 95.294  113.968 1.00 34.49 ?  24  GLN C N     1 
ATOM   11184 C  CA    . GLN C 2 45  ? 132.028 95.874  113.513 1.00 34.81 ?  24  GLN C CA    1 
ATOM   11185 C  C     . GLN C 2 45  ? 131.305 96.616  114.644 1.00 34.68 ?  24  GLN C C     1 
ATOM   11186 O  O     . GLN C 2 45  ? 130.826 97.736  114.449 1.00 34.59 ?  24  GLN C O     1 
ATOM   11187 C  CB    . GLN C 2 45  ? 131.130 94.802  112.887 1.00 34.83 ?  24  GLN C CB    1 
ATOM   11188 C  CG    . GLN C 2 45  ? 129.972 95.351  112.048 1.00 36.14 ?  24  GLN C CG    1 
ATOM   11189 C  CD    . GLN C 2 45  ? 130.428 96.185  110.848 1.00 38.04 ?  24  GLN C CD    1 
ATOM   11190 O  OE1   . GLN C 2 45  ? 131.508 95.973  110.291 1.00 38.57 ?  24  GLN C OE1   1 
ATOM   11191 N  NE2   . GLN C 2 45  ? 129.595 97.148  110.450 1.00 38.67 ?  24  GLN C NE2   1 
ATOM   11192 N  N     . ASN C 2 46  ? 131.243 96.006  115.824 1.00 34.71 ?  25  ASN C N     1 
ATOM   11193 C  CA    . ASN C 2 46  ? 130.588 96.646  116.966 1.00 34.99 ?  25  ASN C CA    1 
ATOM   11194 C  C     . ASN C 2 46  ? 131.252 97.961  117.369 1.00 35.69 ?  25  ASN C C     1 
ATOM   11195 O  O     . ASN C 2 46  ? 130.576 98.981  117.538 1.00 35.41 ?  25  ASN C O     1 
ATOM   11196 C  CB    . ASN C 2 46  ? 130.477 95.689  118.159 1.00 34.64 ?  25  ASN C CB    1 
ATOM   11197 C  CG    . ASN C 2 46  ? 129.298 94.747  118.035 1.00 34.71 ?  25  ASN C CG    1 
ATOM   11198 O  OD1   . ASN C 2 46  ? 128.216 95.040  118.534 1.00 35.68 ?  25  ASN C OD1   1 
ATOM   11199 N  ND2   . ASN C 2 46  ? 129.490 93.625  117.334 1.00 34.71 ?  25  ASN C ND2   1 
ATOM   11200 N  N     . VAL C 2 47  ? 132.576 97.952  117.496 1.00 36.69 ?  26  VAL C N     1 
ATOM   11201 C  CA    . VAL C 2 47  ? 133.283 99.162  117.919 1.00 38.00 ?  26  VAL C CA    1 
ATOM   11202 C  C     . VAL C 2 47  ? 133.269 100.266 116.852 1.00 38.90 ?  26  VAL C C     1 
ATOM   11203 O  O     . VAL C 2 47  ? 133.271 101.445 117.191 1.00 39.46 ?  26  VAL C O     1 
ATOM   11204 C  CB    . VAL C 2 47  ? 134.719 98.886  118.439 1.00 38.16 ?  26  VAL C CB    1 
ATOM   11205 C  CG1   . VAL C 2 47  ? 134.675 97.917  119.605 1.00 37.75 ?  26  VAL C CG1   1 
ATOM   11206 C  CG2   . VAL C 2 47  ? 135.631 98.374  117.326 1.00 38.81 ?  26  VAL C CG2   1 
ATOM   11207 N  N     . LYS C 2 48  ? 133.221 99.885  115.575 1.00 39.67 ?  27  LYS C N     1 
ATOM   11208 C  CA    . LYS C 2 48  ? 133.155 100.873 114.496 1.00 40.50 ?  27  LYS C CA    1 
ATOM   11209 C  C     . LYS C 2 48  ? 131.744 101.457 114.343 1.00 40.02 ?  27  LYS C C     1 
ATOM   11210 O  O     . LYS C 2 48  ? 131.553 102.483 113.687 1.00 40.55 ?  27  LYS C O     1 
ATOM   11211 C  CB    . LYS C 2 48  ? 133.665 100.290 113.165 1.00 41.23 ?  27  LYS C CB    1 
ATOM   11212 C  CG    . LYS C 2 48  ? 132.630 99.498  112.367 1.00 42.50 ?  27  LYS C CG    1 
ATOM   11213 C  CD    . LYS C 2 48  ? 133.177 99.000  111.021 1.00 44.92 ?  27  LYS C CD    1 
ATOM   11214 C  CE    . LYS C 2 48  ? 133.166 100.092 109.953 1.00 46.66 ?  27  LYS C CE    1 
ATOM   11215 N  NZ    . LYS C 2 48  ? 131.790 100.600 109.680 1.00 47.26 1  27  LYS C NZ    1 
ATOM   11216 N  N     . GLN C 2 49  ? 130.759 100.796 114.940 1.00 39.10 ?  28  GLN C N     1 
ATOM   11217 C  CA    . GLN C 2 49  ? 129.398 101.288 114.902 1.00 38.22 ?  28  GLN C CA    1 
ATOM   11218 C  C     . GLN C 2 49  ? 129.084 102.184 116.099 1.00 37.23 ?  28  GLN C C     1 
ATOM   11219 O  O     . GLN C 2 49  ? 127.969 102.692 116.198 1.00 37.40 ?  28  GLN C O     1 
ATOM   11220 C  CB    . GLN C 2 49  ? 128.391 100.129 114.795 1.00 38.69 ?  28  GLN C CB    1 
ATOM   11221 C  CG    . GLN C 2 49  ? 128.341 99.470  113.408 1.00 39.57 ?  28  GLN C CG    1 
ATOM   11222 C  CD    . GLN C 2 49  ? 127.211 98.456  113.247 1.00 41.20 ?  28  GLN C CD    1 
ATOM   11223 O  OE1   . GLN C 2 49  ? 127.108 97.801  112.209 1.00 42.94 ?  28  GLN C OE1   1 
ATOM   11224 N  NE2   . GLN C 2 49  ? 126.360 98.323  114.269 1.00 41.23 ?  28  GLN C NE2   1 
ATOM   11225 N  N     . PHE C 2 50  ? 130.062 102.396 116.987 1.00 35.83 ?  29  PHE C N     1 
ATOM   11226 C  CA    . PHE C 2 50  ? 129.826 103.176 118.210 1.00 34.51 ?  29  PHE C CA    1 
ATOM   11227 C  C     . PHE C 2 50  ? 129.246 104.567 117.935 1.00 33.81 ?  29  PHE C C     1 
ATOM   11228 O  O     . PHE C 2 50  ? 129.725 105.280 117.054 1.00 33.66 ?  29  PHE C O     1 
ATOM   11229 C  CB    . PHE C 2 50  ? 131.080 103.292 119.081 1.00 34.59 ?  29  PHE C CB    1 
ATOM   11230 C  CG    . PHE C 2 50  ? 130.855 104.064 120.368 1.00 34.59 ?  29  PHE C CG    1 
ATOM   11231 C  CD1   . PHE C 2 50  ? 130.118 103.506 121.419 1.00 34.34 ?  29  PHE C CD1   1 
ATOM   11232 C  CD2   . PHE C 2 50  ? 131.360 105.355 120.521 1.00 35.49 ?  29  PHE C CD2   1 
ATOM   11233 C  CE1   . PHE C 2 50  ? 129.899 104.217 122.608 1.00 33.88 ?  29  PHE C CE1   1 
ATOM   11234 C  CE2   . PHE C 2 50  ? 131.146 106.082 121.707 1.00 34.12 ?  29  PHE C CE2   1 
ATOM   11235 C  CZ    . PHE C 2 50  ? 130.416 105.513 122.750 1.00 33.87 ?  29  PHE C CZ    1 
ATOM   11236 N  N     . TRP C 2 51  ? 128.219 104.933 118.705 1.00 32.24 ?  30  TRP C N     1 
ATOM   11237 C  CA    . TRP C 2 51  ? 127.537 106.217 118.557 1.00 31.28 ?  30  TRP C CA    1 
ATOM   11238 C  C     . TRP C 2 51  ? 126.903 106.677 119.871 1.00 31.12 ?  30  TRP C C     1 
ATOM   11239 O  O     . TRP C 2 51  ? 126.755 105.881 120.805 1.00 30.71 ?  30  TRP C O     1 
ATOM   11240 C  CB    . TRP C 2 51  ? 126.481 106.140 117.446 1.00 30.85 ?  30  TRP C CB    1 
ATOM   11241 C  CG    . TRP C 2 51  ? 125.375 105.148 117.713 1.00 29.31 ?  30  TRP C CG    1 
ATOM   11242 C  CD1   . TRP C 2 51  ? 125.408 103.798 117.491 1.00 29.07 ?  30  TRP C CD1   1 
ATOM   11243 C  CD2   . TRP C 2 51  ? 124.088 105.430 118.270 1.00 28.33 ?  30  TRP C CD2   1 
ATOM   11244 N  NE1   . TRP C 2 51  ? 124.218 103.226 117.867 1.00 28.01 ?  30  TRP C NE1   1 
ATOM   11245 C  CE2   . TRP C 2 51  ? 123.388 104.203 118.348 1.00 27.67 ?  30  TRP C CE2   1 
ATOM   11246 C  CE3   . TRP C 2 51  ? 123.456 106.599 118.717 1.00 27.27 ?  30  TRP C CE3   1 
ATOM   11247 C  CZ2   . TRP C 2 51  ? 122.091 104.113 118.852 1.00 26.54 ?  30  TRP C CZ2   1 
ATOM   11248 C  CZ3   . TRP C 2 51  ? 122.161 106.511 119.209 1.00 27.07 ?  30  TRP C CZ3   1 
ATOM   11249 C  CH2   . TRP C 2 51  ? 121.495 105.273 119.280 1.00 26.52 ?  30  TRP C CH2   1 
ATOM   11250 N  N     . LEU C 2 52  ? 126.538 107.961 119.931 1.00 30.65 ?  31  LEU C N     1 
ATOM   11251 C  CA    . LEU C 2 52  ? 125.793 108.540 121.053 1.00 30.38 ?  31  LEU C CA    1 
ATOM   11252 C  C     . LEU C 2 52  ? 124.617 109.353 120.520 1.00 30.51 ?  31  LEU C C     1 
ATOM   11253 O  O     . LEU C 2 52  ? 124.758 110.022 119.495 1.00 30.77 ?  31  LEU C O     1 
ATOM   11254 C  CB    . LEU C 2 52  ? 126.702 109.438 121.908 1.00 30.45 ?  31  LEU C CB    1 
ATOM   11255 C  CG    . LEU C 2 52  ? 127.851 108.729 122.631 1.00 30.29 ?  31  LEU C CG    1 
ATOM   11256 C  CD1   . LEU C 2 52  ? 128.958 109.703 123.060 1.00 30.69 ?  31  LEU C CD1   1 
ATOM   11257 C  CD2   . LEU C 2 52  ? 127.331 107.906 123.820 1.00 29.91 ?  31  LEU C CD2   1 
ATOM   11258 N  N     . PRO C 2 53  ? 123.455 109.310 121.211 1.00 30.73 ?  32  PRO C N     1 
ATOM   11259 C  CA    . PRO C 2 53  ? 122.269 110.039 120.732 1.00 31.17 ?  32  PRO C CA    1 
ATOM   11260 C  C     . PRO C 2 53  ? 122.503 111.538 120.555 1.00 32.18 ?  32  PRO C C     1 
ATOM   11261 O  O     . PRO C 2 53  ? 121.888 112.154 119.669 1.00 32.66 ?  32  PRO C O     1 
ATOM   11262 C  CB    . PRO C 2 53  ? 121.226 109.794 121.829 1.00 30.99 ?  32  PRO C CB    1 
ATOM   11263 C  CG    . PRO C 2 53  ? 122.007 109.295 123.022 1.00 30.50 ?  32  PRO C CG    1 
ATOM   11264 C  CD    . PRO C 2 53  ? 123.165 108.555 122.446 1.00 30.46 ?  32  PRO C CD    1 
ATOM   11265 N  N     . GLU C 2 54  ? 123.392 112.108 121.372 1.00 32.62 ?  33  GLU C N     1 
ATOM   11266 C  CA    . GLU C 2 54  ? 123.725 113.540 121.304 1.00 33.44 ?  33  GLU C CA    1 
ATOM   11267 C  C     . GLU C 2 54  ? 124.344 113.967 119.967 1.00 33.59 ?  33  GLU C C     1 
ATOM   11268 O  O     . GLU C 2 54  ? 124.394 115.157 119.666 1.00 34.05 ?  33  GLU C O     1 
ATOM   11269 C  CB    . GLU C 2 54  ? 124.647 113.960 122.463 1.00 33.72 ?  33  GLU C CB    1 
ATOM   11270 C  CG    . GLU C 2 54  ? 123.972 114.011 123.847 1.00 34.53 ?  33  GLU C CG    1 
ATOM   11271 C  CD    . GLU C 2 54  ? 123.720 112.627 124.445 1.00 35.09 ?  33  GLU C CD    1 
ATOM   11272 O  OE1   . GLU C 2 54  ? 124.412 111.655 124.047 1.00 34.38 ?  33  GLU C OE1   1 
ATOM   11273 O  OE2   . GLU C 2 54  ? 122.826 112.513 125.315 1.00 35.53 -1 33  GLU C OE2   1 
ATOM   11274 N  N     . GLU C 2 55  ? 124.813 112.999 119.176 1.00 33.82 ?  34  GLU C N     1 
ATOM   11275 C  CA    . GLU C 2 55  ? 125.333 113.270 117.833 1.00 34.19 ?  34  GLU C CA    1 
ATOM   11276 C  C     . GLU C 2 55  ? 124.224 113.738 116.880 1.00 33.83 ?  34  GLU C C     1 
ATOM   11277 O  O     . GLU C 2 55  ? 124.502 114.366 115.860 1.00 33.93 ?  34  GLU C O     1 
ATOM   11278 C  CB    . GLU C 2 55  ? 126.016 112.026 117.235 1.00 34.52 ?  34  GLU C CB    1 
ATOM   11279 C  CG    . GLU C 2 55  ? 127.244 111.512 117.982 1.00 36.50 ?  34  GLU C CG    1 
ATOM   11280 C  CD    . GLU C 2 55  ? 128.012 110.464 117.181 1.00 40.03 ?  34  GLU C CD    1 
ATOM   11281 O  OE1   . GLU C 2 55  ? 128.854 110.844 116.337 1.00 42.43 ?  34  GLU C OE1   1 
ATOM   11282 O  OE2   . GLU C 2 55  ? 127.784 109.258 117.398 1.00 39.35 -1 34  GLU C OE2   1 
ATOM   11283 N  N     . ILE C 2 56  ? 122.979 113.398 117.215 1.00 33.31 ?  35  ILE C N     1 
ATOM   11284 C  CA    . ILE C 2 56  ? 121.800 113.711 116.406 1.00 33.14 ?  35  ILE C CA    1 
ATOM   11285 C  C     . ILE C 2 56  ? 120.993 114.812 117.103 1.00 32.58 ?  35  ILE C C     1 
ATOM   11286 O  O     . ILE C 2 56  ? 120.506 114.611 118.210 1.00 32.12 ?  35  ILE C O     1 
ATOM   11287 C  CB    . ILE C 2 56  ? 120.886 112.449 116.227 1.00 33.03 ?  35  ILE C CB    1 
ATOM   11288 C  CG1   . ILE C 2 56  ? 121.682 111.226 115.724 1.00 34.76 ?  35  ILE C CG1   1 
ATOM   11289 C  CG2   . ILE C 2 56  ? 119.674 112.750 115.336 1.00 33.61 ?  35  ILE C CG2   1 
ATOM   11290 C  CD1   . ILE C 2 56  ? 122.225 111.326 114.296 1.00 36.75 ?  35  ILE C CD1   1 
ATOM   11291 N  N     . ALA C 2 57  ? 120.863 115.972 116.463 1.00 32.36 ?  36  ALA C N     1 
ATOM   11292 C  CA    . ALA C 2 57  ? 120.035 117.054 117.004 1.00 32.17 ?  36  ALA C CA    1 
ATOM   11293 C  C     . ALA C 2 57  ? 118.554 116.759 116.741 1.00 31.76 ?  36  ALA C C     1 
ATOM   11294 O  O     . ALA C 2 57  ? 118.173 116.414 115.621 1.00 31.95 ?  36  ALA C O     1 
ATOM   11295 C  CB    . ALA C 2 57  ? 120.434 118.386 116.390 1.00 33.01 ?  36  ALA C CB    1 
ATOM   11296 N  N     . LEU C 2 58  ? 117.722 116.896 117.769 1.00 30.68 ?  37  LEU C N     1 
ATOM   11297 C  CA    . LEU C 2 58  ? 116.346 116.408 117.693 1.00 30.14 ?  37  LEU C CA    1 
ATOM   11298 C  C     . LEU C 2 58  ? 115.285 117.487 117.514 1.00 30.21 ?  37  LEU C C     1 
ATOM   11299 O  O     . LEU C 2 58  ? 114.125 117.175 117.215 1.00 29.91 ?  37  LEU C O     1 
ATOM   11300 C  CB    . LEU C 2 58  ? 116.024 115.534 118.912 1.00 29.46 ?  37  LEU C CB    1 
ATOM   11301 C  CG    . LEU C 2 58  ? 116.780 114.201 118.991 1.00 29.08 ?  37  LEU C CG    1 
ATOM   11302 C  CD1   . LEU C 2 58  ? 116.519 113.511 120.318 1.00 29.23 ?  37  LEU C CD1   1 
ATOM   11303 C  CD2   . LEU C 2 58  ? 116.410 113.279 117.830 1.00 28.84 ?  37  LEU C CD2   1 
ATOM   11304 N  N     . ASN C 2 59  ? 115.684 118.746 117.671 1.00 30.50 ?  38  ASN C N     1 
ATOM   11305 C  CA    . ASN C 2 59  ? 114.747 119.868 117.575 1.00 31.23 ?  38  ASN C CA    1 
ATOM   11306 C  C     . ASN C 2 59  ? 114.069 120.003 116.201 1.00 31.03 ?  38  ASN C C     1 
ATOM   11307 O  O     . ASN C 2 59  ? 113.012 120.615 116.088 1.00 30.82 ?  38  ASN C O     1 
ATOM   11308 C  CB    . ASN C 2 59  ? 115.403 121.187 118.028 1.00 31.98 ?  38  ASN C CB    1 
ATOM   11309 C  CG    . ASN C 2 59  ? 116.642 121.544 117.224 1.00 33.59 ?  38  ASN C CG    1 
ATOM   11310 O  OD1   . ASN C 2 59  ? 117.588 120.752 117.124 1.00 36.48 ?  38  ASN C OD1   1 
ATOM   11311 N  ND2   . ASN C 2 59  ? 116.653 122.747 116.657 1.00 34.77 ?  38  ASN C ND2   1 
ATOM   11312 N  N     . GLY C 2 60  ? 114.668 119.397 115.178 1.00 30.88 ?  39  GLY C N     1 
ATOM   11313 C  CA    . GLY C 2 60  ? 114.072 119.325 113.839 1.00 31.37 ?  39  GLY C CA    1 
ATOM   11314 C  C     . GLY C 2 60  ? 112.784 118.517 113.734 1.00 31.05 ?  39  GLY C C     1 
ATOM   11315 O  O     . GLY C 2 60  ? 111.974 118.781 112.855 1.00 31.21 ?  39  GLY C O     1 
ATOM   11316 N  N     . ASP C 2 61  ? 112.587 117.544 114.627 1.00 30.63 ?  40  ASP C N     1 
ATOM   11317 C  CA    . ASP C 2 61  ? 111.324 116.783 114.697 1.00 30.65 ?  40  ASP C CA    1 
ATOM   11318 C  C     . ASP C 2 61  ? 110.165 117.515 115.380 1.00 31.00 ?  40  ASP C C     1 
ATOM   11319 O  O     . ASP C 2 61  ? 109.036 117.022 115.354 1.00 30.91 ?  40  ASP C O     1 
ATOM   11320 C  CB    . ASP C 2 61  ? 111.523 115.451 115.430 1.00 30.00 ?  40  ASP C CB    1 
ATOM   11321 C  CG    . ASP C 2 61  ? 112.406 114.485 114.678 1.00 30.88 ?  40  ASP C CG    1 
ATOM   11322 O  OD1   . ASP C 2 61  ? 112.904 114.826 113.579 1.00 30.42 ?  40  ASP C OD1   1 
ATOM   11323 O  OD2   . ASP C 2 61  ? 112.607 113.369 115.205 1.00 31.17 -1 40  ASP C OD2   1 
ATOM   11324 N  N     . LEU C 2 62  ? 110.438 118.663 116.000 1.00 31.54 ?  41  LEU C N     1 
ATOM   11325 C  CA    . LEU C 2 62  ? 109.438 119.356 116.828 1.00 32.47 ?  41  LEU C CA    1 
ATOM   11326 C  C     . LEU C 2 62  ? 108.120 119.637 116.114 1.00 33.21 ?  41  LEU C C     1 
ATOM   11327 O  O     . LEU C 2 62  ? 107.044 119.464 116.695 1.00 32.84 ?  41  LEU C O     1 
ATOM   11328 C  CB    . LEU C 2 62  ? 109.998 120.656 117.409 1.00 33.14 ?  41  LEU C CB    1 
ATOM   11329 C  CG    . LEU C 2 62  ? 110.803 120.562 118.704 1.00 34.44 ?  41  LEU C CG    1 
ATOM   11330 C  CD1   . LEU C 2 62  ? 111.530 121.875 118.960 1.00 35.04 ?  41  LEU C CD1   1 
ATOM   11331 C  CD2   . LEU C 2 62  ? 109.895 120.196 119.885 1.00 35.52 ?  41  LEU C CD2   1 
ATOM   11332 N  N     . LEU C 2 63  ? 108.211 120.064 114.856 1.00 33.75 ?  42  LEU C N     1 
ATOM   11333 C  CA    . LEU C 2 63  ? 107.017 120.391 114.088 1.00 34.79 ?  42  LEU C CA    1 
ATOM   11334 C  C     . LEU C 2 63  ? 106.232 119.188 113.569 1.00 34.66 ?  42  LEU C C     1 
ATOM   11335 O  O     . LEU C 2 63  ? 105.011 119.167 113.710 1.00 34.67 ?  42  LEU C O     1 
ATOM   11336 C  CB    . LEU C 2 63  ? 107.326 121.380 112.961 1.00 35.27 ?  42  LEU C CB    1 
ATOM   11337 C  CG    . LEU C 2 63  ? 107.371 122.842 113.422 1.00 36.82 ?  42  LEU C CG    1 
ATOM   11338 C  CD1   . LEU C 2 63  ? 107.726 123.741 112.243 1.00 37.93 ?  42  LEU C CD1   1 
ATOM   11339 C  CD2   . LEU C 2 63  ? 106.049 123.290 114.044 1.00 37.85 ?  42  LEU C CD2   1 
ATOM   11340 N  N     . THR C 2 64  ? 106.904 118.196 112.978 1.00 34.70 ?  43  THR C N     1 
ATOM   11341 C  CA    . THR C 2 64  ? 106.183 116.992 112.530 1.00 35.10 ?  43  THR C CA    1 
ATOM   11342 C  C     . THR C 2 64  ? 105.548 116.233 113.706 1.00 34.78 ?  43  THR C C     1 
ATOM   11343 O  O     . THR C 2 64  ? 104.546 115.550 113.527 1.00 35.04 ?  43  THR C O     1 
ATOM   11344 C  CB    . THR C 2 64  ? 107.018 116.041 111.616 1.00 35.30 ?  43  THR C CB    1 
ATOM   11345 O  OG1   . THR C 2 64  ? 108.236 115.651 112.268 1.00 36.01 ?  43  THR C OG1   1 
ATOM   11346 C  CG2   . THR C 2 64  ? 107.334 116.706 110.277 1.00 35.96 ?  43  THR C CG2   1 
ATOM   11347 N  N     . TRP C 2 65  ? 106.113 116.383 114.906 1.00 34.63 ?  44  TRP C N     1 
ATOM   11348 C  CA    . TRP C 2 65  ? 105.536 115.795 116.121 1.00 34.37 ?  44  TRP C CA    1 
ATOM   11349 C  C     . TRP C 2 65  ? 104.269 116.536 116.547 1.00 35.13 ?  44  TRP C C     1 
ATOM   11350 O  O     . TRP C 2 65  ? 103.225 115.921 116.803 1.00 34.98 ?  44  TRP C O     1 
ATOM   11351 C  CB    . TRP C 2 65  ? 106.554 115.811 117.260 1.00 33.95 ?  44  TRP C CB    1 
ATOM   11352 C  CG    . TRP C 2 65  ? 105.984 115.427 118.589 1.00 33.26 ?  44  TRP C CG    1 
ATOM   11353 C  CD1   . TRP C 2 65  ? 105.663 116.266 119.620 1.00 32.51 ?  44  TRP C CD1   1 
ATOM   11354 C  CD2   . TRP C 2 65  ? 105.672 114.101 119.036 1.00 30.93 ?  44  TRP C CD2   1 
ATOM   11355 N  NE1   . TRP C 2 65  ? 105.174 115.542 120.686 1.00 31.66 ?  44  TRP C NE1   1 
ATOM   11356 C  CE2   . TRP C 2 65  ? 105.167 114.211 120.353 1.00 30.39 ?  44  TRP C CE2   1 
ATOM   11357 C  CE3   . TRP C 2 65  ? 105.773 112.830 118.453 1.00 30.36 ?  44  TRP C CE3   1 
ATOM   11358 C  CZ2   . TRP C 2 65  ? 104.757 113.100 121.094 1.00 29.16 ?  44  TRP C CZ2   1 
ATOM   11359 C  CZ3   . TRP C 2 65  ? 105.367 111.719 119.193 1.00 28.84 ?  44  TRP C CZ3   1 
ATOM   11360 C  CH2   . TRP C 2 65  ? 104.871 111.863 120.501 1.00 29.34 ?  44  TRP C CH2   1 
ATOM   11361 N  N     . LYS C 2 66  ? 104.383 117.860 116.636 1.00 35.69 ?  45  LYS C N     1 
ATOM   11362 C  CA    . LYS C 2 66  ? 103.263 118.736 116.946 1.00 36.38 ?  45  LYS C CA    1 
ATOM   11363 C  C     . LYS C 2 66  ? 102.043 118.450 116.064 1.00 36.24 ?  45  LYS C C     1 
ATOM   11364 O  O     . LYS C 2 66  ? 100.915 118.567 116.529 1.00 36.78 ?  45  LYS C O     1 
ATOM   11365 C  CB    . LYS C 2 66  ? 103.708 120.190 116.775 1.00 37.14 ?  45  LYS C CB    1 
ATOM   11366 C  CG    . LYS C 2 66  ? 102.661 121.238 117.109 1.00 38.91 ?  45  LYS C CG    1 
ATOM   11367 C  CD    . LYS C 2 66  ? 103.132 122.622 116.660 1.00 41.12 ?  45  LYS C CD    1 
ATOM   11368 C  CE    . LYS C 2 66  ? 102.283 123.720 117.280 1.00 43.00 ?  45  LYS C CE    1 
ATOM   11369 N  NZ    . LYS C 2 66  ? 102.140 123.532 118.756 1.00 44.38 1  45  LYS C NZ    1 
ATOM   11370 N  N     . TYR C 2 67  ? 102.291 118.041 114.816 1.00 36.03 ?  46  TYR C N     1 
ATOM   11371 C  CA    . TYR C 2 67  ? 101.259 117.855 113.783 1.00 36.03 ?  46  TYR C CA    1 
ATOM   11372 C  C     . TYR C 2 67  ? 100.540 116.500 113.811 1.00 35.25 ?  46  TYR C C     1 
ATOM   11373 O  O     . TYR C 2 67  ? 99.528  116.314 113.127 1.00 35.32 ?  46  TYR C O     1 
ATOM   11374 C  CB    . TYR C 2 67  ? 101.863 118.049 112.380 1.00 36.60 ?  46  TYR C CB    1 
ATOM   11375 C  CG    . TYR C 2 67  ? 102.431 119.433 112.092 1.00 37.85 ?  46  TYR C CG    1 
ATOM   11376 C  CD1   . TYR C 2 67  ? 102.134 120.520 112.914 1.00 38.97 ?  46  TYR C CD1   1 
ATOM   11377 C  CD2   . TYR C 2 67  ? 103.255 119.652 110.979 1.00 40.06 ?  46  TYR C CD2   1 
ATOM   11378 C  CE1   . TYR C 2 67  ? 102.657 121.786 112.660 1.00 40.36 ?  46  TYR C CE1   1 
ATOM   11379 C  CE2   . TYR C 2 67  ? 103.784 120.925 110.710 1.00 40.53 ?  46  TYR C CE2   1 
ATOM   11380 C  CZ    . TYR C 2 67  ? 103.474 121.987 111.559 1.00 41.43 ?  46  TYR C CZ    1 
ATOM   11381 O  OH    . TYR C 2 67  ? 103.969 123.256 111.318 1.00 41.48 ?  46  TYR C OH    1 
ATOM   11382 N  N     . LEU C 2 68  ? 101.072 115.551 114.576 1.00 33.80 ?  47  LEU C N     1 
ATOM   11383 C  CA    . LEU C 2 68  ? 100.450 114.236 114.692 1.00 32.77 ?  47  LEU C CA    1 
ATOM   11384 C  C     . LEU C 2 68  ? 99.206  114.317 115.568 1.00 31.84 ?  47  LEU C C     1 
ATOM   11385 O  O     . LEU C 2 68  ? 99.138  115.135 116.482 1.00 31.90 ?  47  LEU C O     1 
ATOM   11386 C  CB    . LEU C 2 68  ? 101.427 113.223 115.292 1.00 32.39 ?  47  LEU C CB    1 
ATOM   11387 C  CG    . LEU C 2 68  ? 102.710 112.823 114.561 1.00 32.68 ?  47  LEU C CG    1 
ATOM   11388 C  CD1   . LEU C 2 68  ? 103.479 111.814 115.409 1.00 33.03 ?  47  LEU C CD1   1 
ATOM   11389 C  CD2   . LEU C 2 68  ? 102.438 112.254 113.164 1.00 32.78 ?  47  LEU C CD2   1 
ATOM   11390 N  N     . GLY C 2 69  ? 98.235  113.453 115.299 1.00 30.99 ?  48  GLY C N     1 
ATOM   11391 C  CA    . GLY C 2 69  ? 97.061  113.333 116.162 1.00 30.58 ?  48  GLY C CA    1 
ATOM   11392 C  C     . GLY C 2 69  ? 97.413  112.826 117.554 1.00 29.87 ?  48  GLY C C     1 
ATOM   11393 O  O     . GLY C 2 69  ? 98.481  112.252 117.763 1.00 28.79 ?  48  GLY C O     1 
ATOM   11394 N  N     . LYS C 2 70  ? 96.518  113.049 118.512 1.00 29.89 ?  49  LYS C N     1 
ATOM   11395 C  CA    . LYS C 2 70  ? 96.737  112.584 119.881 1.00 29.49 ?  49  LYS C CA    1 
ATOM   11396 C  C     . LYS C 2 70  ? 96.920  111.057 119.953 1.00 28.74 ?  49  LYS C C     1 
ATOM   11397 O  O     . LYS C 2 70  ? 97.772  110.568 120.707 1.00 27.27 ?  49  LYS C O     1 
ATOM   11398 C  CB    . LYS C 2 70  ? 95.620  113.072 120.809 1.00 30.67 ?  49  LYS C CB    1 
ATOM   11399 C  CG    . LYS C 2 70  ? 95.796  114.549 121.242 1.00 33.73 ?  49  LYS C CG    1 
ATOM   11400 C  CD    . LYS C 2 70  ? 94.509  115.169 121.814 1.00 38.93 ?  49  LYS C CD    1 
ATOM   11401 C  CE    . LYS C 2 70  ? 94.230  114.758 123.265 1.00 41.04 ?  49  LYS C CE    1 
ATOM   11402 N  NZ    . LYS C 2 70  ? 95.152  115.394 124.252 1.00 42.21 1  49  LYS C NZ    1 
ATOM   11403 N  N     . ASN C 2 71  ? 96.136  110.326 119.154 1.00 27.54 ?  50  ASN C N     1 
ATOM   11404 C  CA    . ASN C 2 71  ? 96.265  108.871 119.041 1.00 27.00 ?  50  ASN C CA    1 
ATOM   11405 C  C     . ASN C 2 71  ? 97.652  108.440 118.562 1.00 26.19 ?  50  ASN C C     1 
ATOM   11406 O  O     . ASN C 2 71  ? 98.238  107.472 119.091 1.00 25.38 ?  50  ASN C O     1 
ATOM   11407 C  CB    . ASN C 2 71  ? 95.177  108.285 118.113 1.00 27.08 ?  50  ASN C CB    1 
ATOM   11408 C  CG    . ASN C 2 71  ? 95.229  108.843 116.671 1.00 28.69 ?  50  ASN C CG    1 
ATOM   11409 O  OD1   . ASN C 2 71  ? 95.391  110.057 116.442 1.00 30.45 ?  50  ASN C OD1   1 
ATOM   11410 N  ND2   . ASN C 2 71  ? 95.059  107.944 115.689 1.00 29.42 ?  50  ASN C ND2   1 
ATOM   11411 N  N     . GLU C 2 72  ? 98.167  109.160 117.567 1.00 24.91 ?  51  GLU C N     1 
ATOM   11412 C  CA    . GLU C 2 72  ? 99.466  108.851 116.983 1.00 24.97 ?  51  GLU C CA    1 
ATOM   11413 C  C     . GLU C 2 72  ? 100.603 109.104 117.980 1.00 24.45 ?  51  GLU C C     1 
ATOM   11414 O  O     . GLU C 2 72  ? 101.513 108.274 118.123 1.00 23.90 ?  51  GLU C O     1 
ATOM   11415 C  CB    . GLU C 2 72  ? 99.679  109.657 115.701 1.00 25.27 ?  51  GLU C CB    1 
ATOM   11416 C  CG    . GLU C 2 72  ? 98.725  109.286 114.568 1.00 26.16 ?  51  GLU C CG    1 
ATOM   11417 C  CD    . GLU C 2 72  ? 98.944  110.151 113.334 1.00 28.70 ?  51  GLU C CD    1 
ATOM   11418 O  OE1   . GLU C 2 72  ? 98.503  111.319 113.341 1.00 28.70 ?  51  GLU C OE1   1 
ATOM   11419 O  OE2   . GLU C 2 72  ? 99.555  109.665 112.356 1.00 28.92 -1 51  GLU C OE2   1 
ATOM   11420 N  N     . GLN C 2 73  ? 100.527 110.237 118.677 1.00 23.75 ?  52  GLN C N     1 
ATOM   11421 C  CA    . GLN C 2 73  ? 101.526 110.586 119.684 1.00 23.94 ?  52  GLN C CA    1 
ATOM   11422 C  C     . GLN C 2 73  ? 101.516 109.584 120.841 1.00 23.36 ?  52  GLN C C     1 
ATOM   11423 O  O     . GLN C 2 73  ? 102.568 109.222 121.354 1.00 22.95 ?  52  GLN C O     1 
ATOM   11424 C  CB    . GLN C 2 73  ? 101.288 112.001 120.231 1.00 24.28 ?  52  GLN C CB    1 
ATOM   11425 C  CG    . GLN C 2 73  ? 101.645 113.149 119.267 1.00 25.22 ?  52  GLN C CG    1 
ATOM   11426 C  CD    . GLN C 2 73  ? 101.480 114.538 119.897 1.00 29.02 ?  52  GLN C CD    1 
ATOM   11427 O  OE1   . GLN C 2 73  ? 101.086 114.664 121.055 1.00 32.08 ?  52  GLN C OE1   1 
ATOM   11428 N  NE2   . GLN C 2 73  ? 101.784 115.578 119.130 1.00 29.13 ?  52  GLN C NE2   1 
ATOM   11429 N  N     . ASP C 2 74  ? 100.317 109.171 121.257 1.00 23.02 ?  53  ASP C N     1 
ATOM   11430 C  CA    . ASP C 2 74  ? 100.155 108.210 122.340 1.00 23.44 ?  53  ASP C CA    1 
ATOM   11431 C  C     . ASP C 2 74  ? 100.816 106.873 121.980 1.00 23.00 ?  53  ASP C C     1 
ATOM   11432 O  O     . ASP C 2 74  ? 101.587 106.332 122.767 1.00 22.96 ?  53  ASP C O     1 
ATOM   11433 C  CB    . ASP C 2 74  ? 98.668  107.992 122.653 1.00 23.31 ?  53  ASP C CB    1 
ATOM   11434 C  CG    . ASP C 2 74  ? 98.450  107.135 123.884 1.00 25.80 ?  53  ASP C CG    1 
ATOM   11435 O  OD1   . ASP C 2 74  ? 98.894  107.533 124.991 1.00 27.95 ?  53  ASP C OD1   1 
ATOM   11436 O  OD2   . ASP C 2 74  ? 97.824  106.066 123.744 1.00 26.30 -1 53  ASP C OD2   1 
ATOM   11437 N  N     . THR C 2 75  ? 100.496 106.351 120.798 1.00 22.20 ?  54  THR C N     1 
ATOM   11438 C  CA    . THR C 2 75  ? 101.069 105.097 120.327 1.00 21.84 ?  54  THR C CA    1 
ATOM   11439 C  C     . THR C 2 75  ? 102.585 105.213 120.215 1.00 22.09 ?  54  THR C C     1 
ATOM   11440 O  O     . THR C 2 75  ? 103.307 104.324 120.652 1.00 21.88 ?  54  THR C O     1 
ATOM   11441 C  CB    . THR C 2 75  ? 100.439 104.638 118.982 1.00 21.74 ?  54  THR C CB    1 
ATOM   11442 O  OG1   . THR C 2 75  ? 99.062  104.329 119.204 1.00 22.09 ?  54  THR C OG1   1 
ATOM   11443 C  CG2   . THR C 2 75  ? 101.127 103.374 118.450 1.00 19.76 ?  54  THR C CG2   1 
ATOM   11444 N  N     . TYR C 2 76  ? 103.059 106.316 119.644 1.00 22.38 ?  55  TYR C N     1 
ATOM   11445 C  CA    . TYR C 2 76  ? 104.495 106.544 119.504 1.00 22.85 ?  55  TYR C CA    1 
ATOM   11446 C  C     . TYR C 2 76  ? 105.239 106.528 120.851 1.00 22.56 ?  55  TYR C C     1 
ATOM   11447 O  O     . TYR C 2 76  ? 106.267 105.866 120.970 1.00 21.97 ?  55  TYR C O     1 
ATOM   11448 C  CB    . TYR C 2 76  ? 104.754 107.852 118.769 1.00 23.57 ?  55  TYR C CB    1 
ATOM   11449 C  CG    . TYR C 2 76  ? 106.156 108.009 118.219 1.00 25.59 ?  55  TYR C CG    1 
ATOM   11450 C  CD1   . TYR C 2 76  ? 106.466 107.603 116.916 1.00 27.49 ?  55  TYR C CD1   1 
ATOM   11451 C  CD2   . TYR C 2 76  ? 107.163 108.595 118.985 1.00 27.70 ?  55  TYR C CD2   1 
ATOM   11452 C  CE1   . TYR C 2 76  ? 107.755 107.771 116.396 1.00 30.28 ?  55  TYR C CE1   1 
ATOM   11453 C  CE2   . TYR C 2 76  ? 108.459 108.763 118.478 1.00 30.38 ?  55  TYR C CE2   1 
ATOM   11454 C  CZ    . TYR C 2 76  ? 108.745 108.347 117.183 1.00 31.39 ?  55  TYR C CZ    1 
ATOM   11455 O  OH    . TYR C 2 76  ? 110.019 108.524 116.678 1.00 32.67 ?  55  TYR C OH    1 
ATOM   11456 N  N     . MET C 2 77  ? 104.726 107.257 121.845 1.00 23.14 ?  56  MET C N     1 
ATOM   11457 C  CA    . MET C 2 77  ? 105.343 107.310 123.184 1.00 23.90 ?  56  MET C CA    1 
ATOM   11458 C  C     . MET C 2 77  ? 105.408 105.921 123.807 1.00 23.24 ?  56  MET C C     1 
ATOM   11459 O  O     . MET C 2 77  ? 106.415 105.532 124.411 1.00 22.47 ?  56  MET C O     1 
ATOM   11460 C  CB    . MET C 2 77  ? 104.543 108.213 124.129 1.00 24.38 ?  56  MET C CB    1 
ATOM   11461 C  CG    . MET C 2 77  ? 104.499 109.691 123.768 1.00 28.52 ?  56  MET C CG    1 
ATOM   11462 S  SD    . MET C 2 77  ? 106.027 110.543 124.136 1.00 34.32 ?  56  MET C SD    1 
ATOM   11463 C  CE    . MET C 2 77  ? 106.077 110.448 125.929 1.00 33.84 ?  56  MET C CE    1 
ATOM   11464 N  N     . LYS C 2 78  ? 104.311 105.182 123.660 1.00 23.25 ?  57  LYS C N     1 
ATOM   11465 C  CA    . LYS C 2 78  ? 104.165 103.896 124.329 1.00 22.98 ?  57  LYS C CA    1 
ATOM   11466 C  C     . LYS C 2 78  ? 105.085 102.868 123.687 1.00 22.77 ?  57  LYS C C     1 
ATOM   11467 O  O     . LYS C 2 78  ? 105.748 102.103 124.381 1.00 22.56 ?  57  LYS C O     1 
ATOM   11468 C  CB    . LYS C 2 78  ? 102.696 103.458 124.332 1.00 22.99 ?  57  LYS C CB    1 
ATOM   11469 C  CG    . LYS C 2 78  ? 101.857 104.220 125.361 1.00 24.86 ?  57  LYS C CG    1 
ATOM   11470 C  CD    . LYS C 2 78  ? 100.362 103.926 125.234 1.00 27.37 ?  57  LYS C CD    1 
ATOM   11471 C  CE    . LYS C 2 78  ? 99.586  104.505 126.423 1.00 28.99 ?  57  LYS C CE    1 
ATOM   11472 N  NZ    . LYS C 2 78  ? 98.118  104.382 126.179 1.00 29.82 1  57  LYS C NZ    1 
ATOM   11473 N  N     . VAL C 2 79  ? 105.124 102.887 122.356 1.00 22.70 ?  58  VAL C N     1 
ATOM   11474 C  CA    . VAL C 2 79  ? 106.017 102.058 121.549 1.00 23.48 ?  58  VAL C CA    1 
ATOM   11475 C  C     . VAL C 2 79  ? 107.492 102.220 121.989 1.00 23.04 ?  58  VAL C C     1 
ATOM   11476 O  O     . VAL C 2 79  ? 108.184 101.223 122.276 1.00 22.83 ?  58  VAL C O     1 
ATOM   11477 C  CB    . VAL C 2 79  ? 105.764 102.382 120.043 1.00 24.24 ?  58  VAL C CB    1 
ATOM   11478 C  CG1   . VAL C 2 79  ? 107.027 102.343 119.201 1.00 25.71 ?  58  VAL C CG1   1 
ATOM   11479 C  CG2   . VAL C 2 79  ? 104.641 101.480 119.485 1.00 25.04 ?  58  VAL C CG2   1 
ATOM   11480 N  N     . LEU C 2 80  ? 107.950 103.464 122.094 1.00 22.84 ?  59  LEU C N     1 
ATOM   11481 C  CA    . LEU C 2 80  ? 109.330 103.733 122.504 1.00 23.35 ?  59  LEU C CA    1 
ATOM   11482 C  C     . LEU C 2 80  ? 109.569 103.351 123.969 1.00 22.75 ?  59  LEU C C     1 
ATOM   11483 O  O     . LEU C 2 80  ? 110.660 102.906 124.318 1.00 22.75 ?  59  LEU C O     1 
ATOM   11484 C  CB    . LEU C 2 80  ? 109.725 105.197 122.264 1.00 23.91 ?  59  LEU C CB    1 
ATOM   11485 C  CG    . LEU C 2 80  ? 109.859 105.800 120.851 1.00 26.63 ?  59  LEU C CG    1 
ATOM   11486 C  CD1   . LEU C 2 80  ? 110.672 107.083 120.907 1.00 26.99 ?  59  LEU C CD1   1 
ATOM   11487 C  CD2   . LEU C 2 80  ? 110.484 104.844 119.848 1.00 27.23 ?  59  LEU C CD2   1 
ATOM   11488 N  N     . ALA C 2 81  ? 108.542 103.500 124.810 1.00 22.28 ?  60  ALA C N     1 
ATOM   11489 C  CA    . ALA C 2 81  ? 108.626 103.101 126.218 1.00 22.21 ?  60  ALA C CA    1 
ATOM   11490 C  C     . ALA C 2 81  ? 108.798 101.585 126.361 1.00 22.07 ?  60  ALA C C     1 
ATOM   11491 O  O     . ALA C 2 81  ? 109.598 101.137 127.177 1.00 21.97 ?  60  ALA C O     1 
ATOM   11492 C  CB    . ALA C 2 81  ? 107.404 103.612 127.010 1.00 22.38 ?  60  ALA C CB    1 
ATOM   11493 N  N     . GLY C 2 82  ? 108.078 100.817 125.535 1.00 21.67 ?  61  GLY C N     1 
ATOM   11494 C  CA    . GLY C 2 82  ? 108.212 99.364  125.468 1.00 21.74 ?  61  GLY C CA    1 
ATOM   11495 C  C     . GLY C 2 82  ? 109.605 98.943  125.030 1.00 21.79 ?  61  GLY C C     1 
ATOM   11496 O  O     . GLY C 2 82  ? 110.173 97.972  125.553 1.00 21.93 ?  61  GLY C O     1 
ATOM   11497 N  N     . LEU C 2 83  ? 110.162 99.694  124.081 1.00 21.54 ?  62  LEU C N     1 
ATOM   11498 C  CA    . LEU C 2 83  ? 111.537 99.487  123.630 1.00 21.12 ?  62  LEU C CA    1 
ATOM   11499 C  C     . LEU C 2 83  ? 112.529 99.798  124.742 1.00 20.89 ?  62  LEU C C     1 
ATOM   11500 O  O     . LEU C 2 83  ? 113.489 99.049  124.935 1.00 20.84 ?  62  LEU C O     1 
ATOM   11501 C  CB    . LEU C 2 83  ? 111.859 100.345 122.401 1.00 21.23 ?  62  LEU C CB    1 
ATOM   11502 C  CG    . LEU C 2 83  ? 111.129 100.066 121.080 1.00 21.98 ?  62  LEU C CG    1 
ATOM   11503 C  CD1   . LEU C 2 83  ? 111.465 101.126 120.028 1.00 24.12 ?  62  LEU C CD1   1 
ATOM   11504 C  CD2   . LEU C 2 83  ? 111.439 98.684  120.538 1.00 22.03 ?  62  LEU C CD2   1 
ATOM   11505 N  N     . THR C 2 84  ? 112.293 100.898 125.459 1.00 19.93 ?  63  THR C N     1 
ATOM   11506 C  CA    . THR C 2 84  ? 113.161 101.302 126.563 1.00 19.71 ?  63  THR C CA    1 
ATOM   11507 C  C     . THR C 2 84  ? 113.244 100.206 127.614 1.00 19.63 ?  63  THR C C     1 
ATOM   11508 O  O     . THR C 2 84  ? 114.327 99.924  128.133 1.00 19.62 ?  63  THR C O     1 
ATOM   11509 C  CB    . THR C 2 84  ? 112.675 102.615 127.225 1.00 20.22 ?  63  THR C CB    1 
ATOM   11510 O  OG1   . THR C 2 84  ? 112.466 103.619 126.216 1.00 19.37 ?  63  THR C OG1   1 
ATOM   11511 C  CG2   . THR C 2 84  ? 113.680 103.100 128.241 1.00 19.45 ?  63  THR C CG2   1 
ATOM   11512 N  N     . LEU C 2 85  ? 112.102 99.600  127.929 1.00 19.66 ?  64  LEU C N     1 
ATOM   11513 C  CA    . LEU C 2 85  ? 112.046 98.530  128.921 1.00 20.51 ?  64  LEU C CA    1 
ATOM   11514 C  C     . LEU C 2 85  ? 112.896 97.332  128.484 1.00 20.84 ?  64  LEU C C     1 
ATOM   11515 O  O     . LEU C 2 85  ? 113.727 96.844  129.252 1.00 21.30 ?  64  LEU C O     1 
ATOM   11516 C  CB    . LEU C 2 85  ? 110.597 98.108  129.219 1.00 20.03 ?  64  LEU C CB    1 
ATOM   11517 C  CG    . LEU C 2 85  ? 110.471 96.952  130.238 1.00 21.43 ?  64  LEU C CG    1 
ATOM   11518 C  CD1   . LEU C 2 85  ? 110.958 97.360  131.649 1.00 21.61 ?  64  LEU C CD1   1 
ATOM   11519 C  CD2   . LEU C 2 85  ? 109.054 96.390  130.314 1.00 20.99 ?  64  LEU C CD2   1 
ATOM   11520 N  N     . LEU C 2 86  ? 112.691 96.883  127.252 1.00 21.37 ?  65  LEU C N     1 
ATOM   11521 C  CA    . LEU C 2 86  ? 113.469 95.782  126.678 1.00 21.92 ?  65  LEU C CA    1 
ATOM   11522 C  C     . LEU C 2 86  ? 114.985 96.031  126.731 1.00 21.76 ?  65  LEU C C     1 
ATOM   11523 O  O     . LEU C 2 86  ? 115.738 95.157  127.162 1.00 21.72 ?  65  LEU C O     1 
ATOM   11524 C  CB    . LEU C 2 86  ? 113.029 95.497  125.234 1.00 22.42 ?  65  LEU C CB    1 
ATOM   11525 C  CG    . LEU C 2 86  ? 111.638 94.900  124.931 1.00 24.26 ?  65  LEU C CG    1 
ATOM   11526 C  CD1   . LEU C 2 86  ? 111.417 94.850  123.420 1.00 24.67 ?  65  LEU C CD1   1 
ATOM   11527 C  CD2   . LEU C 2 86  ? 111.480 93.513  125.530 1.00 25.60 ?  65  LEU C CD2   1 
ATOM   11528 N  N     . ASP C 2 87  ? 115.426 97.213  126.294 1.00 21.75 ?  66  ASP C N     1 
ATOM   11529 C  CA    . ASP C 2 87  ? 116.854 97.583  126.347 1.00 21.99 ?  66  ASP C CA    1 
ATOM   11530 C  C     . ASP C 2 87  ? 117.408 97.729  127.769 1.00 21.76 ?  66  ASP C C     1 
ATOM   11531 O  O     . ASP C 2 87  ? 118.584 97.429  128.020 1.00 21.65 ?  66  ASP C O     1 
ATOM   11532 C  CB    . ASP C 2 87  ? 117.111 98.888  125.589 1.00 22.23 ?  66  ASP C CB    1 
ATOM   11533 C  CG    . ASP C 2 87  ? 117.531 98.657  124.164 1.00 24.59 ?  66  ASP C CG    1 
ATOM   11534 O  OD1   . ASP C 2 87  ? 118.359 97.751  123.915 1.00 27.46 ?  66  ASP C OD1   1 
ATOM   11535 O  OD2   . ASP C 2 87  ? 117.036 99.397  123.290 1.00 27.98 -1 66  ASP C OD2   1 
ATOM   11536 N  N     . THR C 2 88  ? 116.573 98.224  128.679 1.00 21.50 ?  67  THR C N     1 
ATOM   11537 C  CA    . THR C 2 88  ? 116.935 98.297  130.090 1.00 21.80 ?  67  THR C CA    1 
ATOM   11538 C  C     . THR C 2 88  ? 117.328 96.905  130.621 1.00 22.04 ?  67  THR C C     1 
ATOM   11539 O  O     . THR C 2 88  ? 118.381 96.747  131.255 1.00 22.21 ?  67  THR C O     1 
ATOM   11540 C  CB    . THR C 2 88  ? 115.797 98.912  130.923 1.00 22.15 ?  67  THR C CB    1 
ATOM   11541 O  OG1   . THR C 2 88  ? 115.530 100.232 130.444 1.00 22.23 ?  67  THR C OG1   1 
ATOM   11542 C  CG2   . THR C 2 88  ? 116.162 98.992  132.409 1.00 21.19 ?  67  THR C CG2   1 
ATOM   11543 N  N     . GLU C 2 89  ? 116.502 95.905  130.329 1.00 21.55 ?  68  GLU C N     1 
ATOM   11544 C  CA    . GLU C 2 89  ? 116.748 94.559  130.830 1.00 21.81 ?  68  GLU C CA    1 
ATOM   11545 C  C     . GLU C 2 89  ? 117.843 93.832  130.032 1.00 21.35 ?  68  GLU C C     1 
ATOM   11546 O  O     . GLU C 2 89  ? 118.621 93.068  130.598 1.00 21.34 ?  68  GLU C O     1 
ATOM   11547 C  CB    . GLU C 2 89  ? 115.442 93.761  130.912 1.00 22.25 ?  68  GLU C CB    1 
ATOM   11548 C  CG    . GLU C 2 89  ? 114.596 94.119  132.169 1.00 24.02 ?  68  GLU C CG    1 
ATOM   11549 C  CD    . GLU C 2 89  ? 115.396 94.017  133.469 1.00 25.78 ?  68  GLU C CD    1 
ATOM   11550 O  OE1   . GLU C 2 89  ? 116.118 93.016  133.663 1.00 26.69 ?  68  GLU C OE1   1 
ATOM   11551 O  OE2   . GLU C 2 89  ? 115.303 94.942  134.310 1.00 28.98 -1 68  GLU C OE2   1 
ATOM   11552 N  N     . GLN C 2 90  ? 117.932 94.116  128.734 1.00 20.82 ?  69  GLN C N     1 
ATOM   11553 C  CA    . GLN C 2 90  ? 118.991 93.552  127.904 1.00 21.28 ?  69  GLN C CA    1 
ATOM   11554 C  C     . GLN C 2 90  ? 120.365 94.065  128.349 1.00 21.24 ?  69  GLN C C     1 
ATOM   11555 O  O     . GLN C 2 90  ? 121.342 93.311  128.346 1.00 20.99 ?  69  GLN C O     1 
ATOM   11556 C  CB    . GLN C 2 90  ? 118.741 93.843  126.414 1.00 21.86 ?  69  GLN C CB    1 
ATOM   11557 C  CG    . GLN C 2 90  ? 119.605 92.994  125.454 1.00 24.29 ?  69  GLN C CG    1 
ATOM   11558 C  CD    . GLN C 2 90  ? 119.213 91.512  125.445 1.00 27.14 ?  69  GLN C CD    1 
ATOM   11559 O  OE1   . GLN C 2 90  ? 118.590 91.016  126.388 1.00 27.13 ?  69  GLN C OE1   1 
ATOM   11560 N  NE2   . GLN C 2 90  ? 119.593 90.801  124.381 1.00 27.69 ?  69  GLN C NE2   1 
ATOM   11561 N  N     . GLY C 2 91  ? 120.419 95.334  128.762 1.00 20.62 ?  70  GLY C N     1 
ATOM   11562 C  CA    . GLY C 2 91  ? 121.662 95.955  129.230 1.00 22.00 ?  70  GLY C CA    1 
ATOM   11563 C  C     . GLY C 2 91  ? 122.007 95.616  130.667 1.00 22.45 ?  70  GLY C C     1 
ATOM   11564 O  O     . GLY C 2 91  ? 123.161 95.313  130.960 1.00 23.53 ?  70  GLY C O     1 
ATOM   11565 N  N     . ASN C 2 92  ? 121.012 95.666  131.556 1.00 22.79 ?  71  ASN C N     1 
ATOM   11566 C  CA    . ASN C 2 92  ? 121.215 95.390  132.987 1.00 23.85 ?  71  ASN C CA    1 
ATOM   11567 C  C     . ASN C 2 92  ? 121.477 93.916  133.270 1.00 24.33 ?  71  ASN C C     1 
ATOM   11568 O  O     . ASN C 2 92  ? 122.249 93.582  134.176 1.00 24.17 ?  71  ASN C O     1 
ATOM   11569 C  CB    . ASN C 2 92  ? 119.988 95.802  133.811 1.00 23.74 ?  71  ASN C CB    1 
ATOM   11570 C  CG    . ASN C 2 92  ? 119.782 97.305  133.884 1.00 24.38 ?  71  ASN C CG    1 
ATOM   11571 O  OD1   . ASN C 2 92  ? 120.528 98.097  133.295 1.00 25.16 ?  71  ASN C OD1   1 
ATOM   11572 N  ND2   . ASN C 2 92  ? 118.751 97.704  134.610 1.00 24.07 ?  71  ASN C ND2   1 
ATOM   11573 N  N     . THR C 2 93  ? 120.835 93.042  132.493 1.00 23.97 ?  72  THR C N     1 
ATOM   11574 C  CA    . THR C 2 93  ? 120.716 91.628  132.879 1.00 24.97 ?  72  THR C CA    1 
ATOM   11575 C  C     . THR C 2 93  ? 121.169 90.678  131.780 1.00 24.52 ?  72  THR C C     1 
ATOM   11576 O  O     . THR C 2 93  ? 122.086 89.893  131.989 1.00 25.39 ?  72  THR C O     1 
ATOM   11577 C  CB    . THR C 2 93  ? 119.262 91.275  133.294 1.00 24.54 ?  72  THR C CB    1 
ATOM   11578 O  OG1   . THR C 2 93  ? 118.819 92.177  134.317 1.00 26.43 ?  72  THR C OG1   1 
ATOM   11579 C  CG2   . THR C 2 93  ? 119.172 89.852  133.822 1.00 26.83 ?  72  THR C CG2   1 
ATOM   11580 N  N     . GLY C 2 94  ? 120.527 90.765  130.625 1.00 24.37 ?  73  GLY C N     1 
ATOM   11581 C  CA    . GLY C 2 94  ? 120.699 89.794  129.534 1.00 24.24 ?  73  GLY C CA    1 
ATOM   11582 C  C     . GLY C 2 94  ? 122.115 89.682  129.011 1.00 24.94 ?  73  GLY C C     1 
ATOM   11583 O  O     . GLY C 2 94  ? 122.728 88.611  129.077 1.00 25.86 ?  73  GLY C O     1 
ATOM   11584 N  N     . MET C 2 95  ? 122.641 90.784  128.489 1.00 24.07 ?  74  MET C N     1 
ATOM   11585 C  CA    . MET C 2 95  ? 123.994 90.766  127.948 1.00 24.35 ?  74  MET C CA    1 
ATOM   11586 C  C     . MET C 2 95  ? 125.102 90.491  128.983 1.00 23.52 ?  74  MET C C     1 
ATOM   11587 O  O     . MET C 2 95  ? 125.981 89.688  128.689 1.00 23.40 ?  74  MET C O     1 
ATOM   11588 C  CB    . MET C 2 95  ? 124.280 92.011  127.108 1.00 24.38 ?  74  MET C CB    1 
ATOM   11589 C  CG    . MET C 2 95  ? 123.525 92.050  125.779 1.00 27.47 ?  74  MET C CG    1 
ATOM   11590 S  SD    . MET C 2 95  ? 124.016 90.665  124.715 1.00 32.54 ?  74  MET C SD    1 
ATOM   11591 C  CE    . MET C 2 95  ? 125.639 91.164  124.259 1.00 34.32 ?  74  MET C CE    1 
ATOM   11592 N  N     . PRO C 2 96  ? 125.064 91.140  130.181 1.00 23.36 ?  75  PRO C N     1 
ATOM   11593 C  CA    . PRO C 2 96  ? 126.066 90.826  131.223 1.00 23.27 ?  75  PRO C CA    1 
ATOM   11594 C  C     . PRO C 2 96  ? 126.057 89.373  131.685 1.00 23.77 ?  75  PRO C C     1 
ATOM   11595 O  O     . PRO C 2 96  ? 127.124 88.793  131.881 1.00 23.46 ?  75  PRO C O     1 
ATOM   11596 C  CB    . PRO C 2 96  ? 125.657 91.727  132.401 1.00 23.55 ?  75  PRO C CB    1 
ATOM   11597 C  CG    . PRO C 2 96  ? 124.954 92.877  131.767 1.00 23.85 ?  75  PRO C CG    1 
ATOM   11598 C  CD    . PRO C 2 96  ? 124.204 92.269  130.592 1.00 22.76 ?  75  PRO C CD    1 
ATOM   11599 N  N     . ILE C 2 97  ? 124.870 88.794  131.880 1.00 23.81 ?  76  ILE C N     1 
ATOM   11600 C  CA    . ILE C 2 97  ? 124.772 87.399  132.318 1.00 24.52 ?  76  ILE C CA    1 
ATOM   11601 C  C     . ILE C 2 97  ? 125.280 86.395  131.261 1.00 23.92 ?  76  ILE C C     1 
ATOM   11602 O  O     . ILE C 2 97  ? 125.995 85.438  131.591 1.00 23.99 ?  76  ILE C O     1 
ATOM   11603 C  CB    . ILE C 2 97  ? 123.349 87.047  132.837 1.00 24.49 ?  76  ILE C CB    1 
ATOM   11604 C  CG1   . ILE C 2 97  ? 123.403 85.843  133.775 1.00 27.08 ?  76  ILE C CG1   1 
ATOM   11605 C  CG2   . ILE C 2 97  ? 122.354 86.791  131.686 1.00 26.06 ?  76  ILE C CG2   1 
ATOM   11606 C  CD1   . ILE C 2 97  ? 122.243 85.807  134.758 1.00 31.37 ?  76  ILE C CD1   1 
ATOM   11607 N  N     . VAL C 2 98  ? 124.942 86.628  129.996 1.00 23.97 ?  77  VAL C N     1 
ATOM   11608 C  CA    . VAL C 2 98  ? 125.488 85.812  128.903 1.00 24.01 ?  77  VAL C CA    1 
ATOM   11609 C  C     . VAL C 2 98  ? 127.021 85.986  128.832 1.00 25.23 ?  77  VAL C C     1 
ATOM   11610 O  O     . VAL C 2 98  ? 127.757 85.003  128.706 1.00 25.77 ?  77  VAL C O     1 
ATOM   11611 C  CB    . VAL C 2 98  ? 124.802 86.133  127.551 1.00 23.98 ?  77  VAL C CB    1 
ATOM   11612 C  CG1   . VAL C 2 98  ? 125.553 85.496  126.384 1.00 23.17 ?  77  VAL C CG1   1 
ATOM   11613 C  CG2   . VAL C 2 98  ? 123.346 85.650  127.579 1.00 22.55 ?  77  VAL C CG2   1 
ATOM   11614 N  N     . ALA C 2 99  ? 127.497 87.225  128.972 1.00 25.42 ?  78  ALA C N     1 
ATOM   11615 C  CA    . ALA C 2 99  ? 128.947 87.482  129.005 1.00 26.72 ?  78  ALA C CA    1 
ATOM   11616 C  C     . ALA C 2 99  ? 129.636 86.660  130.099 1.00 27.46 ?  78  ALA C C     1 
ATOM   11617 O  O     . ALA C 2 99  ? 130.701 86.088  129.871 1.00 28.07 ?  78  ALA C O     1 
ATOM   11618 C  CB    . ALA C 2 99  ? 129.236 88.959  129.191 1.00 26.52 ?  78  ALA C CB    1 
ATOM   11619 N  N     . GLU C 2 100 ? 129.000 86.574  131.266 1.00 28.33 ?  79  GLU C N     1 
ATOM   11620 C  CA    . GLU C 2 100 ? 129.561 85.843  132.406 1.00 29.60 ?  79  GLU C CA    1 
ATOM   11621 C  C     . GLU C 2 100 ? 129.781 84.360  132.099 1.00 29.64 ?  79  GLU C C     1 
ATOM   11622 O  O     . GLU C 2 100 ? 130.772 83.764  132.537 1.00 29.72 ?  79  GLU C O     1 
ATOM   11623 C  CB    . GLU C 2 100 ? 128.674 86.011  133.640 1.00 29.70 ?  79  GLU C CB    1 
ATOM   11624 C  CG    . GLU C 2 100 ? 129.226 85.345  134.900 1.00 33.58 ?  79  GLU C CG    1 
ATOM   11625 C  CD    . GLU C 2 100 ? 128.282 85.405  136.085 1.00 37.83 ?  79  GLU C CD    1 
ATOM   11626 O  OE1   . GLU C 2 100 ? 127.241 86.103  136.020 1.00 40.64 ?  79  GLU C OE1   1 
ATOM   11627 O  OE2   . GLU C 2 100 ? 128.584 84.736  137.097 1.00 41.40 -1 79  GLU C OE2   1 
ATOM   11628 N  N     . HIS C 2 101 ? 128.868 83.771  131.330 1.00 29.43 ?  80  HIS C N     1 
ATOM   11629 C  CA    . HIS C 2 101 ? 128.878 82.330  131.115 1.00 29.74 ?  80  HIS C CA    1 
ATOM   11630 C  C     . HIS C 2 101 ? 129.587 81.869  129.841 1.00 30.18 ?  80  HIS C C     1 
ATOM   11631 O  O     . HIS C 2 101 ? 129.920 80.697  129.711 1.00 30.30 ?  80  HIS C O     1 
ATOM   11632 C  CB    . HIS C 2 101 ? 127.453 81.765  131.233 1.00 29.21 ?  80  HIS C CB    1 
ATOM   11633 C  CG    . HIS C 2 101 ? 126.921 81.803  132.632 1.00 29.60 ?  80  HIS C CG    1 
ATOM   11634 N  ND1   . HIS C 2 101 ? 126.197 82.868  133.128 1.00 30.06 ?  80  HIS C ND1   1 
ATOM   11635 C  CD2   . HIS C 2 101 ? 127.046 80.926  133.656 1.00 29.49 ?  80  HIS C CD2   1 
ATOM   11636 C  CE1   . HIS C 2 101 ? 125.888 82.639  134.394 1.00 29.56 ?  80  HIS C CE1   1 
ATOM   11637 N  NE2   . HIS C 2 101 ? 126.389 81.467  134.737 1.00 30.20 ?  80  HIS C NE2   1 
ATOM   11638 N  N     . VAL C 2 102 ? 129.830 82.794  128.917 1.00 30.70 ?  81  VAL C N     1 
ATOM   11639 C  CA    . VAL C 2 102 ? 130.527 82.489  127.670 1.00 31.47 ?  81  VAL C CA    1 
ATOM   11640 C  C     . VAL C 2 102 ? 132.035 82.569  127.894 1.00 32.45 ?  81  VAL C C     1 
ATOM   11641 O  O     . VAL C 2 102 ? 132.526 83.552  128.464 1.00 32.50 ?  81  VAL C O     1 
ATOM   11642 C  CB    . VAL C 2 102 ? 130.106 83.445  126.522 1.00 31.18 ?  81  VAL C CB    1 
ATOM   11643 C  CG1   . VAL C 2 102 ? 130.991 83.251  125.288 1.00 31.20 ?  81  VAL C CG1   1 
ATOM   11644 C  CG2   . VAL C 2 102 ? 128.649 83.217  126.149 1.00 31.28 ?  81  VAL C CG2   1 
ATOM   11645 N  N     . ASP C 2 103 ? 132.755 81.542  127.437 1.00 33.38 ?  82  ASP C N     1 
ATOM   11646 C  CA    . ASP C 2 103 ? 134.209 81.458  127.607 1.00 34.82 ?  82  ASP C CA    1 
ATOM   11647 C  C     . ASP C 2 103 ? 134.985 82.174  126.508 1.00 34.74 ?  82  ASP C C     1 
ATOM   11648 O  O     . ASP C 2 103 ? 134.603 82.130  125.332 1.00 35.00 ?  82  ASP C O     1 
ATOM   11649 C  CB    . ASP C 2 103 ? 134.662 79.993  127.689 1.00 35.82 ?  82  ASP C CB    1 
ATOM   11650 C  CG    . ASP C 2 103 ? 134.297 79.335  129.016 1.00 38.29 ?  82  ASP C CG    1 
ATOM   11651 O  OD1   . ASP C 2 103 ? 134.269 80.030  130.061 1.00 41.49 ?  82  ASP C OD1   1 
ATOM   11652 O  OD2   . ASP C 2 103 ? 134.039 78.116  129.017 1.00 41.10 -1 82  ASP C OD2   1 
ATOM   11653 N  N     . GLY C 2 104 ? 136.078 82.826  126.904 1.00 34.89 ?  83  GLY C N     1 
ATOM   11654 C  CA    . GLY C 2 104 ? 136.984 83.496  125.965 1.00 35.11 ?  83  GLY C CA    1 
ATOM   11655 C  C     . GLY C 2 104 ? 136.940 85.008  126.081 1.00 34.96 ?  83  GLY C C     1 
ATOM   11656 O  O     . GLY C 2 104 ? 135.875 85.612  125.930 1.00 34.57 ?  83  GLY C O     1 
ATOM   11657 N  N     . HIS C 2 105 ? 138.101 85.617  126.332 1.00 35.02 ?  84  HIS C N     1 
ATOM   11658 C  CA    . HIS C 2 105 ? 138.198 87.062  126.581 1.00 34.83 ?  84  HIS C CA    1 
ATOM   11659 C  C     . HIS C 2 105 ? 137.675 87.930  125.444 1.00 33.77 ?  84  HIS C C     1 
ATOM   11660 O  O     . HIS C 2 105 ? 137.088 88.986  125.689 1.00 33.25 ?  84  HIS C O     1 
ATOM   11661 C  CB    . HIS C 2 105 ? 139.626 87.473  126.955 1.00 36.09 ?  84  HIS C CB    1 
ATOM   11662 C  CG    . HIS C 2 105 ? 140.011 87.096  128.353 1.00 39.17 ?  84  HIS C CG    1 
ATOM   11663 N  ND1   . HIS C 2 105 ? 141.297 86.738  128.703 1.00 43.00 ?  84  HIS C ND1   1 
ATOM   11664 C  CD2   . HIS C 2 105 ? 139.273 87.000  129.487 1.00 41.84 ?  84  HIS C CD2   1 
ATOM   11665 C  CE1   . HIS C 2 105 ? 141.335 86.447  129.993 1.00 43.47 ?  84  HIS C CE1   1 
ATOM   11666 N  NE2   . HIS C 2 105 ? 140.120 86.599  130.492 1.00 43.10 ?  84  HIS C NE2   1 
ATOM   11667 N  N     . GLN C 2 106 ? 137.867 87.482  124.209 1.00 32.84 ?  85  GLN C N     1 
ATOM   11668 C  CA    . GLN C 2 106 ? 137.368 88.237  123.063 1.00 32.29 ?  85  GLN C CA    1 
ATOM   11669 C  C     . GLN C 2 106 ? 135.844 88.142  122.924 1.00 30.88 ?  85  GLN C C     1 
ATOM   11670 O  O     . GLN C 2 106 ? 135.185 89.143  122.619 1.00 30.44 ?  85  GLN C O     1 
ATOM   11671 C  CB    . GLN C 2 106 ? 138.054 87.796  121.779 1.00 32.85 ?  85  GLN C CB    1 
ATOM   11672 C  CG    . GLN C 2 106 ? 139.544 88.110  121.747 1.00 35.55 ?  85  GLN C CG    1 
ATOM   11673 C  CD    . GLN C 2 106 ? 140.211 87.564  120.511 1.00 38.12 ?  85  GLN C CD    1 
ATOM   11674 O  OE1   . GLN C 2 106 ? 139.632 87.576  119.425 1.00 39.96 ?  85  GLN C OE1   1 
ATOM   11675 N  NE2   . GLN C 2 106 ? 141.442 87.080  120.666 1.00 40.39 ?  85  GLN C NE2   1 
ATOM   11676 N  N     . ARG C 2 107 ? 135.294 86.948  123.140 1.00 29.75 ?  86  ARG C N     1 
ATOM   11677 C  CA    . ARG C 2 107 ? 133.837 86.770  123.133 1.00 28.87 ?  86  ARG C CA    1 
ATOM   11678 C  C     . ARG C 2 107 ? 133.215 87.617  124.235 1.00 28.16 ?  86  ARG C C     1 
ATOM   11679 O  O     . ARG C 2 107 ? 132.195 88.268  124.016 1.00 27.55 ?  86  ARG C O     1 
ATOM   11680 C  CB    . ARG C 2 107 ? 133.450 85.304  123.313 1.00 28.48 ?  86  ARG C CB    1 
ATOM   11681 C  CG    . ARG C 2 107 ? 133.742 84.450  122.092 1.00 29.86 ?  86  ARG C CG    1 
ATOM   11682 C  CD    . ARG C 2 107 ? 133.384 82.990  122.311 1.00 30.23 ?  86  ARG C CD    1 
ATOM   11683 N  NE    . ARG C 2 107 ? 133.251 82.336  121.015 1.00 33.04 ?  86  ARG C NE    1 
ATOM   11684 C  CZ    . ARG C 2 107 ? 132.617 81.195  120.803 1.00 31.54 ?  86  ARG C CZ    1 
ATOM   11685 N  NH1   . ARG C 2 107 ? 132.055 80.540  121.809 1.00 31.85 1  86  ARG C NH1   1 
ATOM   11686 N  NH2   . ARG C 2 107 ? 132.556 80.712  119.573 1.00 34.74 ?  86  ARG C NH2   1 
ATOM   11687 N  N     . LYS C 2 108 ? 133.844 87.618  125.409 1.00 27.65 ?  87  LYS C N     1 
ATOM   11688 C  CA    . LYS C 2 108 ? 133.371 88.441  126.527 1.00 27.96 ?  87  LYS C CA    1 
ATOM   11689 C  C     . LYS C 2 108 ? 133.447 89.933  126.234 1.00 27.75 ?  87  LYS C C     1 
ATOM   11690 O  O     . LYS C 2 108 ? 132.563 90.684  126.645 1.00 28.29 ?  87  LYS C O     1 
ATOM   11691 C  CB    . LYS C 2 108 ? 134.126 88.129  127.819 1.00 27.80 ?  87  LYS C CB    1 
ATOM   11692 C  CG    . LYS C 2 108 ? 133.817 86.762  128.392 1.00 29.04 ?  87  LYS C CG    1 
ATOM   11693 C  CD    . LYS C 2 108 ? 134.588 86.555  129.688 1.00 31.15 ?  87  LYS C CD    1 
ATOM   11694 C  CE    . LYS C 2 108 ? 134.476 85.123  130.177 1.00 32.05 ?  87  LYS C CE    1 
ATOM   11695 N  NZ    . LYS C 2 108 ? 133.160 84.886  130.820 1.00 30.88 1  87  LYS C NZ    1 
ATOM   11696 N  N     . ALA C 2 109 ? 134.493 90.361  125.527 1.00 27.69 ?  88  ALA C N     1 
ATOM   11697 C  CA    . ALA C 2 109 ? 134.637 91.773  125.150 1.00 27.46 ?  88  ALA C CA    1 
ATOM   11698 C  C     . ALA C 2 109 ? 133.525 92.249  124.211 1.00 26.87 ?  88  ALA C C     1 
ATOM   11699 O  O     . ALA C 2 109 ? 133.037 93.371  124.342 1.00 26.47 ?  88  ALA C O     1 
ATOM   11700 C  CB    . ALA C 2 109 ? 135.994 92.025  124.526 1.00 27.98 ?  88  ALA C CB    1 
ATOM   11701 N  N     . VAL C 2 110 ? 133.145 91.400  123.258 1.00 25.98 ?  89  VAL C N     1 
ATOM   11702 C  CA    . VAL C 2 110 ? 132.044 91.703  122.339 1.00 25.46 ?  89  VAL C CA    1 
ATOM   11703 C  C     . VAL C 2 110 ? 130.729 91.801  123.119 1.00 24.57 ?  89  VAL C C     1 
ATOM   11704 O  O     . VAL C 2 110 ? 129.992 92.784  122.989 1.00 23.62 ?  89  VAL C O     1 
ATOM   11705 C  CB    . VAL C 2 110 ? 131.940 90.648  121.210 1.00 25.80 ?  89  VAL C CB    1 
ATOM   11706 C  CG1   . VAL C 2 110 ? 130.650 90.822  120.396 1.00 25.44 ?  89  VAL C CG1   1 
ATOM   11707 C  CG2   . VAL C 2 110 ? 133.165 90.723  120.300 1.00 26.23 ?  89  VAL C CG2   1 
ATOM   11708 N  N     . LEU C 2 111 ? 130.460 90.799  123.953 1.00 24.33 ?  90  LEU C N     1 
ATOM   11709 C  CA    . LEU C 2 111 ? 129.226 90.785  124.739 1.00 23.93 ?  90  LEU C CA    1 
ATOM   11710 C  C     . LEU C 2 111 ? 129.136 91.943  125.733 1.00 23.77 ?  90  LEU C C     1 
ATOM   11711 O  O     . LEU C 2 111 ? 128.058 92.505  125.925 1.00 23.04 ?  90  LEU C O     1 
ATOM   11712 C  CB    . LEU C 2 111 ? 129.021 89.438  125.437 1.00 23.73 ?  90  LEU C CB    1 
ATOM   11713 C  CG    . LEU C 2 111 ? 128.834 88.248  124.491 1.00 24.50 ?  90  LEU C CG    1 
ATOM   11714 C  CD1   . LEU C 2 111 ? 129.109 86.935  125.206 1.00 24.02 ?  90  LEU C CD1   1 
ATOM   11715 C  CD2   . LEU C 2 111 ? 127.441 88.244  123.856 1.00 25.38 ?  90  LEU C CD2   1 
ATOM   11716 N  N     . ASN C 2 112 ? 130.262 92.288  126.368 1.00 24.24 ?  91  ASN C N     1 
ATOM   11717 C  CA    . ASN C 2 112 ? 130.325 93.475  127.235 1.00 24.95 ?  91  ASN C CA    1 
ATOM   11718 C  C     . ASN C 2 112 ? 130.052 94.780  126.491 1.00 24.25 ?  91  ASN C C     1 
ATOM   11719 O  O     . ASN C 2 112 ? 129.375 95.663  127.016 1.00 23.99 ?  91  ASN C O     1 
ATOM   11720 C  CB    . ASN C 2 112 ? 131.681 93.582  127.939 1.00 25.81 ?  91  ASN C CB    1 
ATOM   11721 C  CG    . ASN C 2 112 ? 131.728 92.791  129.218 1.00 29.96 ?  91  ASN C CG    1 
ATOM   11722 O  OD1   . ASN C 2 112 ? 131.423 93.318  130.289 1.00 35.44 ?  91  ASN C OD1   1 
ATOM   11723 N  ND2   . ASN C 2 112 ? 132.108 91.517  129.123 1.00 32.37 ?  91  ASN C ND2   1 
ATOM   11724 N  N     . PHE C 2 113 ? 130.611 94.908  125.289 1.00 23.60 ?  92  PHE C N     1 
ATOM   11725 C  CA    . PHE C 2 113 ? 130.358 96.076  124.452 1.00 23.32 ?  92  PHE C CA    1 
ATOM   11726 C  C     . PHE C 2 113 ? 128.872 96.182  124.078 1.00 22.63 ?  92  PHE C C     1 
ATOM   11727 O  O     . PHE C 2 113 ? 128.288 97.263  124.159 1.00 21.94 ?  92  PHE C O     1 
ATOM   11728 C  CB    . PHE C 2 113 ? 131.194 96.037  123.166 1.00 23.27 ?  92  PHE C CB    1 
ATOM   11729 C  CG    . PHE C 2 113 ? 131.159 97.327  122.393 1.00 24.66 ?  92  PHE C CG    1 
ATOM   11730 C  CD1   . PHE C 2 113 ? 132.091 98.340  122.659 1.00 25.72 ?  92  PHE C CD1   1 
ATOM   11731 C  CD2   . PHE C 2 113 ? 130.185 97.547  121.423 1.00 25.36 ?  92  PHE C CD2   1 
ATOM   11732 C  CE1   . PHE C 2 113 ? 132.052 99.547  121.960 1.00 25.92 ?  92  PHE C CE1   1 
ATOM   11733 C  CE2   . PHE C 2 113 ? 130.135 98.755  120.715 1.00 25.82 ?  92  PHE C CE2   1 
ATOM   11734 C  CZ    . PHE C 2 113 ? 131.068 99.758  120.989 1.00 25.80 ?  92  PHE C CZ    1 
ATOM   11735 N  N     . MET C 2 114 ? 128.288 95.061  123.647 1.00 22.03 ?  93  MET C N     1 
ATOM   11736 C  CA    . MET C 2 114 ? 126.854 95.004  123.327 1.00 22.14 ?  93  MET C CA    1 
ATOM   11737 C  C     . MET C 2 114 ? 125.976 95.389  124.530 1.00 21.64 ?  93  MET C C     1 
ATOM   11738 O  O     . MET C 2 114 ? 125.012 96.146  124.376 1.00 21.59 ?  93  MET C O     1 
ATOM   11739 C  CB    . MET C 2 114 ? 126.475 93.622  122.805 1.00 22.46 ?  93  MET C CB    1 
ATOM   11740 C  CG    . MET C 2 114 ? 127.066 93.300  121.441 1.00 23.80 ?  93  MET C CG    1 
ATOM   11741 S  SD    . MET C 2 114 ? 126.753 91.591  120.946 1.00 28.07 ?  93  MET C SD    1 
ATOM   11742 C  CE    . MET C 2 114 ? 127.258 91.686  119.209 1.00 26.42 ?  93  MET C CE    1 
ATOM   11743 N  N     . ALA C 2 115 ? 126.332 94.895  125.721 1.00 20.98 ?  94  ALA C N     1 
ATOM   11744 C  CA    . ALA C 2 115 ? 125.648 95.271  126.973 1.00 20.58 ?  94  ALA C CA    1 
ATOM   11745 C  C     . ALA C 2 115 ? 125.674 96.775  127.237 1.00 21.01 ?  94  ALA C C     1 
ATOM   11746 O  O     . ALA C 2 115 ? 124.661 97.373  127.646 1.00 21.06 ?  94  ALA C O     1 
ATOM   11747 C  CB    . ALA C 2 115 ? 126.262 94.506  128.169 1.00 20.83 ?  94  ALA C CB    1 
ATOM   11748 N  N     . MET C 2 116 ? 126.842 97.383  127.042 1.00 20.36 ?  95  MET C N     1 
ATOM   11749 C  CA    . MET C 2 116 ? 126.991 98.817  127.213 1.00 20.83 ?  95  MET C CA    1 
ATOM   11750 C  C     . MET C 2 116 ? 126.067 99.572  126.244 1.00 20.55 ?  95  MET C C     1 
ATOM   11751 O  O     . MET C 2 116 ? 125.376 100.509 126.639 1.00 20.70 ?  95  MET C O     1 
ATOM   11752 C  CB    . MET C 2 116 ? 128.461 99.216  127.022 1.00 20.64 ?  95  MET C CB    1 
ATOM   11753 C  CG    . MET C 2 116 ? 128.740 100.719 127.052 1.00 21.42 ?  95  MET C CG    1 
ATOM   11754 S  SD    . MET C 2 116 ? 128.355 101.518 125.481 1.00 22.51 ?  95  MET C SD    1 
ATOM   11755 C  CE    . MET C 2 116 ? 129.463 100.663 124.359 1.00 20.66 ?  95  MET C CE    1 
ATOM   11756 N  N     . MET C 2 117 ? 126.045 99.142  124.987 1.00 20.50 ?  96  MET C N     1 
ATOM   11757 C  CA    . MET C 2 117 ? 125.188 99.767  123.988 1.00 21.22 ?  96  MET C CA    1 
ATOM   11758 C  C     . MET C 2 117 ? 123.721 99.737  124.415 1.00 21.11 ?  96  MET C C     1 
ATOM   11759 O  O     . MET C 2 117 ? 123.025 100.747 124.292 1.00 20.71 ?  96  MET C O     1 
ATOM   11760 C  CB    . MET C 2 117 ? 125.376 99.122  122.608 1.00 21.35 ?  96  MET C CB    1 
ATOM   11761 C  CG    . MET C 2 117 ? 126.725 99.460  121.898 1.00 22.54 ?  96  MET C CG    1 
ATOM   11762 S  SD    . MET C 2 117 ? 127.098 101.219 121.706 1.00 24.89 ?  96  MET C SD    1 
ATOM   11763 C  CE    . MET C 2 117 ? 125.988 101.668 120.373 1.00 24.95 ?  96  MET C CE    1 
ATOM   11764 N  N     . GLU C 2 118 ? 123.273 98.593  124.933 1.00 21.18 ?  97  GLU C N     1 
ATOM   11765 C  CA    . GLU C 2 118 ? 121.883 98.420  125.370 1.00 21.99 ?  97  GLU C CA    1 
ATOM   11766 C  C     . GLU C 2 118 ? 121.441 99.488  126.372 1.00 22.10 ?  97  GLU C C     1 
ATOM   11767 O  O     . GLU C 2 118 ? 120.446 100.181 126.145 1.00 22.22 ?  97  GLU C O     1 
ATOM   11768 C  CB    . GLU C 2 118 ? 121.633 97.024  125.963 1.00 22.01 ?  97  GLU C CB    1 
ATOM   11769 C  CG    . GLU C 2 118 ? 122.033 95.815  125.107 1.00 24.38 ?  97  GLU C CG    1 
ATOM   11770 C  CD    . GLU C 2 118 ? 121.324 95.712  123.751 1.00 26.32 ?  97  GLU C CD    1 
ATOM   11771 O  OE1   . GLU C 2 118 ? 120.984 96.736  123.142 1.00 29.86 ?  97  GLU C OE1   1 
ATOM   11772 O  OE2   . GLU C 2 118 ? 121.151 94.583  123.262 1.00 29.19 -1 97  GLU C OE2   1 
ATOM   11773 N  N     . ASN C 2 119 ? 122.170 99.626  127.477 1.00 22.26 ?  98  ASN C N     1 
ATOM   11774 C  CA    . ASN C 2 119 ? 121.714 100.532 128.532 1.00 21.91 ?  98  ASN C CA    1 
ATOM   11775 C  C     . ASN C 2 119 ? 122.348 101.930 128.570 1.00 22.41 ?  98  ASN C C     1 
ATOM   11776 O  O     . ASN C 2 119 ? 121.710 102.883 129.015 1.00 23.07 ?  98  ASN C O     1 
ATOM   11777 C  CB    . ASN C 2 119 ? 121.646 99.846  129.914 1.00 21.93 ?  98  ASN C CB    1 
ATOM   11778 C  CG    . ASN C 2 119 ? 122.992 99.379  130.424 1.00 21.31 ?  98  ASN C CG    1 
ATOM   11779 O  OD1   . ASN C 2 119 ? 124.018 99.518  129.755 1.00 21.88 ?  98  ASN C OD1   1 
ATOM   11780 N  ND2   . ASN C 2 119 ? 122.996 98.827  131.636 1.00 21.73 ?  98  ASN C ND2   1 
ATOM   11781 N  N     . ALA C 2 120 ? 123.594 102.049 128.118 1.00 22.75 ?  99  ALA C N     1 
ATOM   11782 C  CA    . ALA C 2 120 ? 124.279 103.340 128.089 1.00 23.12 ?  99  ALA C CA    1 
ATOM   11783 C  C     . ALA C 2 120 ? 123.995 104.131 126.827 1.00 23.60 ?  99  ALA C C     1 
ATOM   11784 O  O     . ALA C 2 120 ? 124.117 105.360 126.838 1.00 24.14 ?  99  ALA C O     1 
ATOM   11785 C  CB    . ALA C 2 120 ? 125.799 103.179 128.298 1.00 23.28 ?  99  ALA C CB    1 
ATOM   11786 N  N     . VAL C 2 121 ? 123.612 103.444 125.744 1.00 23.23 ?  100 VAL C N     1 
ATOM   11787 C  CA    . VAL C 2 121 ? 123.324 104.144 124.478 1.00 23.74 ?  100 VAL C CA    1 
ATOM   11788 C  C     . VAL C 2 121 ? 121.863 104.044 124.039 1.00 23.62 ?  100 VAL C C     1 
ATOM   11789 O  O     . VAL C 2 121 ? 121.206 105.068 123.879 1.00 24.51 ?  100 VAL C O     1 
ATOM   11790 C  CB    . VAL C 2 121 ? 124.264 103.706 123.334 1.00 23.19 ?  100 VAL C CB    1 
ATOM   11791 C  CG1   . VAL C 2 121 ? 123.898 104.421 122.021 1.00 24.10 ?  100 VAL C CG1   1 
ATOM   11792 C  CG2   . VAL C 2 121 ? 125.727 103.990 123.712 1.00 23.48 ?  100 VAL C CG2   1 
ATOM   11793 N  N     . HIS C 2 122 ? 121.366 102.823 123.856 1.00 23.45 ?  101 HIS C N     1 
ATOM   11794 C  CA    . HIS C 2 122 ? 120.014 102.613 123.331 1.00 23.81 ?  101 HIS C CA    1 
ATOM   11795 C  C     . HIS C 2 122 ? 118.924 103.083 124.271 1.00 24.33 ?  101 HIS C C     1 
ATOM   11796 O  O     . HIS C 2 122 ? 118.095 103.910 123.881 1.00 24.80 ?  101 HIS C O     1 
ATOM   11797 C  CB    . HIS C 2 122 ? 119.762 101.150 122.978 1.00 23.30 ?  101 HIS C CB    1 
ATOM   11798 C  CG    . HIS C 2 122 ? 120.654 100.621 121.901 1.00 22.96 ?  101 HIS C CG    1 
ATOM   11799 N  ND1   . HIS C 2 122 ? 120.666 99.291  121.535 1.00 22.78 ?  101 HIS C ND1   1 
ATOM   11800 C  CD2   . HIS C 2 122 ? 121.589 101.234 121.136 1.00 23.25 ?  101 HIS C CD2   1 
ATOM   11801 C  CE1   . HIS C 2 122 ? 121.558 99.113  120.579 1.00 22.57 ?  101 HIS C CE1   1 
ATOM   11802 N  NE2   . HIS C 2 122 ? 122.131 100.274 120.318 1.00 21.75 ?  101 HIS C NE2   1 
ATOM   11803 N  N     . ALA C 2 123 ? 118.903 102.535 125.490 1.00 24.40 ?  102 ALA C N     1 
ATOM   11804 C  CA    . ALA C 2 123 ? 117.865 102.884 126.461 1.00 24.00 ?  102 ALA C CA    1 
ATOM   11805 C  C     . ALA C 2 123 ? 117.856 104.393 126.718 1.00 24.05 ?  102 ALA C C     1 
ATOM   11806 O  O     . ALA C 2 123 ? 116.791 104.996 126.820 1.00 23.89 ?  102 ALA C O     1 
ATOM   11807 C  CB    . ALA C 2 123 ? 118.042 102.103 127.761 1.00 23.73 ?  102 ALA C CB    1 
ATOM   11808 N  N     . LYS C 2 124 ? 119.042 104.994 126.799 1.00 24.36 ?  103 LYS C N     1 
ATOM   11809 C  CA    . LYS C 2 124 ? 119.170 106.437 127.039 1.00 24.31 ?  103 LYS C CA    1 
ATOM   11810 C  C     . LYS C 2 124 ? 118.668 107.312 125.885 1.00 23.84 ?  103 LYS C C     1 
ATOM   11811 O  O     . LYS C 2 124 ? 118.048 108.356 126.125 1.00 24.21 ?  103 LYS C O     1 
ATOM   11812 C  CB    . LYS C 2 124 ? 120.597 106.821 127.439 1.00 24.93 ?  103 LYS C CB    1 
ATOM   11813 C  CG    . LYS C 2 124 ? 120.716 108.277 127.914 1.00 26.37 ?  103 LYS C CG    1 
ATOM   11814 C  CD    . LYS C 2 124 ? 122.092 108.589 128.477 1.00 29.42 ?  103 LYS C CD    1 
ATOM   11815 C  CE    . LYS C 2 124 ? 122.231 110.085 128.777 1.00 31.51 ?  103 LYS C CE    1 
ATOM   11816 N  NZ    . LYS C 2 124 ? 122.168 110.919 127.540 1.00 32.37 1  103 LYS C NZ    1 
ATOM   11817 N  N     . SER C 2 125 ? 118.922 106.887 124.645 1.00 23.52 ?  104 SER C N     1 
ATOM   11818 C  CA    . SER C 2 125 ? 118.456 107.606 123.454 0.50 23.23 ?  104 SER C CA    1 
ATOM   11819 C  C     . SER C 2 125 ? 116.948 107.854 123.482 1.00 22.91 ?  104 SER C C     1 
ATOM   11820 O  O     . SER C 2 125 ? 116.473 108.884 123.022 1.00 22.33 ?  104 SER C O     1 
ATOM   11821 C  CB    . SER C 2 125 ? 118.817 106.838 122.177 0.50 23.25 ?  104 SER C CB    1 
ATOM   11822 O  OG    . SER C 2 125 ? 120.215 106.659 122.056 0.50 24.57 ?  104 SER C OG    1 
ATOM   11823 N  N     . TYR C 2 126 ? 116.189 106.896 124.009 1.00 22.72 ?  105 TYR C N     1 
ATOM   11824 C  CA    . TYR C 2 126 ? 114.737 107.067 124.072 1.00 23.34 ?  105 TYR C CA    1 
ATOM   11825 C  C     . TYR C 2 126 ? 114.351 108.219 124.970 1.00 23.32 ?  105 TYR C C     1 
ATOM   11826 O  O     . TYR C 2 126 ? 113.394 108.918 124.673 1.00 23.17 ?  105 TYR C O     1 
ATOM   11827 C  CB    . TYR C 2 126 ? 114.008 105.799 124.522 1.00 23.45 ?  105 TYR C CB    1 
ATOM   11828 C  CG    . TYR C 2 126 ? 114.290 104.587 123.666 1.00 25.16 ?  105 TYR C CG    1 
ATOM   11829 C  CD1   . TYR C 2 126 ? 113.958 104.564 122.314 1.00 26.75 ?  105 TYR C CD1   1 
ATOM   11830 C  CD2   . TYR C 2 126 ? 114.892 103.457 124.219 1.00 26.36 ?  105 TYR C CD2   1 
ATOM   11831 C  CE1   . TYR C 2 126 ? 114.237 103.441 121.526 1.00 28.22 ?  105 TYR C CE1   1 
ATOM   11832 C  CE2   . TYR C 2 126 ? 115.175 102.341 123.448 1.00 27.17 ?  105 TYR C CE2   1 
ATOM   11833 C  CZ    . TYR C 2 126 ? 114.832 102.333 122.108 1.00 29.26 ?  105 TYR C CZ    1 
ATOM   11834 O  OH    . TYR C 2 126 ? 115.101 101.213 121.345 1.00 30.76 ?  105 TYR C OH    1 
ATOM   11835 N  N     . SER C 2 127 ? 115.100 108.407 126.060 1.00 23.61 ?  106 SER C N     1 
ATOM   11836 C  CA    . SER C 2 127 ? 114.880 109.539 126.951 1.00 24.40 ?  106 SER C CA    1 
ATOM   11837 C  C     . SER C 2 127 ? 115.225 110.856 126.270 1.00 24.55 ?  106 SER C C     1 
ATOM   11838 O  O     . SER C 2 127 ? 114.588 111.862 126.543 1.00 24.74 ?  106 SER C O     1 
ATOM   11839 C  CB    . SER C 2 127 ? 115.656 109.397 128.260 1.00 24.54 ?  106 SER C CB    1 
ATOM   11840 O  OG    . SER C 2 127 ? 115.011 108.477 129.135 1.00 24.69 ?  106 SER C OG    1 
ATOM   11841 N  N     . ASN C 2 128 ? 116.233 110.849 125.398 1.00 25.28 ?  107 ASN C N     1 
ATOM   11842 C  CA    . ASN C 2 128 ? 116.566 112.040 124.610 1.00 25.88 ?  107 ASN C CA    1 
ATOM   11843 C  C     . ASN C 2 128 ? 115.391 112.409 123.714 1.00 25.48 ?  107 ASN C C     1 
ATOM   11844 O  O     . ASN C 2 128 ? 115.012 113.575 123.618 1.00 25.23 ?  107 ASN C O     1 
ATOM   11845 C  CB    . ASN C 2 128 ? 117.827 111.830 123.763 1.00 26.40 ?  107 ASN C CB    1 
ATOM   11846 C  CG    . ASN C 2 128 ? 119.114 111.916 124.574 1.00 27.90 ?  107 ASN C CG    1 
ATOM   11847 O  OD1   . ASN C 2 128 ? 119.149 111.572 125.757 1.00 30.62 ?  107 ASN C OD1   1 
ATOM   11848 N  ND2   . ASN C 2 128 ? 120.185 112.363 123.927 1.00 27.91 ?  107 ASN C ND2   1 
ATOM   11849 N  N     . ILE C 2 129 ? 114.812 111.402 123.068 1.00 25.44 ?  108 ILE C N     1 
ATOM   11850 C  CA    . ILE C 2 129 ? 113.626 111.622 122.240 1.00 25.48 ?  108 ILE C CA    1 
ATOM   11851 C  C     . ILE C 2 129 ? 112.458 112.139 123.096 1.00 25.93 ?  108 ILE C C     1 
ATOM   11852 O  O     . ILE C 2 129 ? 111.866 113.171 122.763 1.00 25.54 ?  108 ILE C O     1 
ATOM   11853 C  CB    . ILE C 2 129 ? 113.251 110.375 121.398 1.00 25.21 ?  108 ILE C CB    1 
ATOM   11854 C  CG1   . ILE C 2 129 ? 114.399 110.036 120.431 1.00 25.96 ?  108 ILE C CG1   1 
ATOM   11855 C  CG2   . ILE C 2 129 ? 111.930 110.610 120.633 1.00 24.43 ?  108 ILE C CG2   1 
ATOM   11856 C  CD1   . ILE C 2 129 ? 114.290 108.678 119.739 1.00 26.11 ?  108 ILE C CD1   1 
ATOM   11857 N  N     . PHE C 2 130 ? 112.146 111.445 124.195 1.00 26.04 ?  109 PHE C N     1 
ATOM   11858 C  CA    . PHE C 2 130 ? 111.058 111.867 125.098 1.00 26.66 ?  109 PHE C CA    1 
ATOM   11859 C  C     . PHE C 2 130 ? 111.234 113.304 125.596 1.00 27.38 ?  109 PHE C C     1 
ATOM   11860 O  O     . PHE C 2 130 ? 110.275 114.092 125.605 1.00 27.22 ?  109 PHE C O     1 
ATOM   11861 C  CB    . PHE C 2 130 ? 110.949 110.937 126.327 1.00 26.98 ?  109 PHE C CB    1 
ATOM   11862 C  CG    . PHE C 2 130 ? 110.419 109.556 126.029 1.00 27.46 ?  109 PHE C CG    1 
ATOM   11863 C  CD1   . PHE C 2 130 ? 109.542 109.328 124.975 1.00 28.57 ?  109 PHE C CD1   1 
ATOM   11864 C  CD2   . PHE C 2 130 ? 110.790 108.478 126.833 1.00 28.51 ?  109 PHE C CD2   1 
ATOM   11865 C  CE1   . PHE C 2 130 ? 109.058 108.048 124.712 1.00 29.17 ?  109 PHE C CE1   1 
ATOM   11866 C  CE2   . PHE C 2 130 ? 110.304 107.187 126.583 1.00 29.27 ?  109 PHE C CE2   1 
ATOM   11867 C  CZ    . PHE C 2 130 ? 109.434 106.970 125.526 1.00 28.83 ?  109 PHE C CZ    1 
ATOM   11868 N  N     . MET C 2 131 ? 112.455 113.648 126.008 1.00 27.52 ?  110 MET C N     1 
ATOM   11869 C  CA    . MET C 2 131 ? 112.717 114.965 126.601 1.00 29.07 ?  110 MET C CA    1 
ATOM   11870 C  C     . MET C 2 131 ? 112.583 116.107 125.608 1.00 29.58 ?  110 MET C C     1 
ATOM   11871 O  O     . MET C 2 131 ? 112.287 117.237 125.996 1.00 30.07 ?  110 MET C O     1 
ATOM   11872 C  CB    . MET C 2 131 ? 114.084 115.015 127.278 1.00 28.96 ?  110 MET C CB    1 
ATOM   11873 C  CG    . MET C 2 131 ? 114.089 114.382 128.654 1.00 31.09 ?  110 MET C CG    1 
ATOM   11874 S  SD    . MET C 2 131 ? 115.710 114.385 129.455 1.00 35.43 ?  110 MET C SD    1 
ATOM   11875 C  CE    . MET C 2 131 ? 116.655 113.285 128.405 1.00 33.13 ?  110 MET C CE    1 
ATOM   11876 N  N     . THR C 2 132 ? 112.796 115.800 124.335 1.00 30.25 ?  111 THR C N     1 
ATOM   11877 C  CA    . THR C 2 132 ? 112.616 116.763 123.253 1.00 30.97 ?  111 THR C CA    1 
ATOM   11878 C  C     . THR C 2 132 ? 111.134 116.982 122.932 1.00 31.36 ?  111 THR C C     1 
ATOM   11879 O  O     . THR C 2 132 ? 110.652 118.123 122.905 1.00 31.60 ?  111 THR C O     1 
ATOM   11880 C  CB    . THR C 2 132 ? 113.384 116.297 121.983 1.00 30.88 ?  111 THR C CB    1 
ATOM   11881 O  OG1   . THR C 2 132 ? 114.784 116.239 122.279 1.00 29.86 ?  111 THR C OG1   1 
ATOM   11882 C  CG2   . THR C 2 132 ? 113.165 117.252 120.799 1.00 31.44 ?  111 THR C CG2   1 
ATOM   11883 N  N     . LEU C 2 133 ? 110.417 115.886 122.702 1.00 31.34 ?  112 LEU C N     1 
ATOM   11884 C  CA    . LEU C 2 133 ? 109.052 115.947 122.179 1.00 31.68 ?  112 LEU C CA    1 
ATOM   11885 C  C     . LEU C 2 133 ? 107.938 116.147 123.211 1.00 31.96 ?  112 LEU C C     1 
ATOM   11886 O  O     . LEU C 2 133 ? 106.911 116.752 122.908 1.00 31.69 ?  112 LEU C O     1 
ATOM   11887 C  CB    . LEU C 2 133 ? 108.754 114.697 121.357 1.00 31.35 ?  112 LEU C CB    1 
ATOM   11888 C  CG    . LEU C 2 133 ? 109.738 114.339 120.238 1.00 32.14 ?  112 LEU C CG    1 
ATOM   11889 C  CD1   . LEU C 2 133 ? 109.310 113.040 119.596 1.00 32.15 ?  112 LEU C CD1   1 
ATOM   11890 C  CD2   . LEU C 2 133 ? 109.837 115.458 119.204 1.00 32.39 ?  112 LEU C CD2   1 
ATOM   11891 N  N     . ALA C 2 134 ? 108.140 115.639 124.423 1.00 32.12 ?  113 ALA C N     1 
ATOM   11892 C  CA    . ALA C 2 134 ? 107.053 115.542 125.388 1.00 32.53 ?  113 ALA C CA    1 
ATOM   11893 C  C     . ALA C 2 134 ? 107.304 116.323 126.671 1.00 33.15 ?  113 ALA C C     1 
ATOM   11894 O  O     . ALA C 2 134 ? 108.444 116.435 127.115 1.00 32.47 ?  113 ALA C O     1 
ATOM   11895 C  CB    . ALA C 2 134 ? 106.760 114.071 125.707 1.00 32.20 ?  113 ALA C CB    1 
ATOM   11896 N  N     . PRO C 2 135 ? 106.224 116.854 127.280 1.00 34.27 ?  114 PRO C N     1 
ATOM   11897 C  CA    . PRO C 2 135 ? 106.337 117.477 128.592 1.00 35.35 ?  114 PRO C CA    1 
ATOM   11898 C  C     . PRO C 2 135 ? 106.531 116.418 129.672 1.00 36.17 ?  114 PRO C C     1 
ATOM   11899 O  O     . PRO C 2 135 ? 106.146 115.262 129.481 1.00 35.92 ?  114 PRO C O     1 
ATOM   11900 C  CB    . PRO C 2 135 ? 104.999 118.208 128.761 1.00 35.48 ?  114 PRO C CB    1 
ATOM   11901 C  CG    . PRO C 2 135 ? 104.049 117.509 127.868 1.00 34.94 ?  114 PRO C CG    1 
ATOM   11902 C  CD    . PRO C 2 135 ? 104.842 116.878 126.761 1.00 34.50 ?  114 PRO C CD    1 
ATOM   11903 N  N     . THR C 2 136 ? 107.136 116.817 130.786 1.00 37.30 ?  115 THR C N     1 
ATOM   11904 C  CA    . THR C 2 136 ? 107.496 115.901 131.874 1.00 38.49 ?  115 THR C CA    1 
ATOM   11905 C  C     . THR C 2 136 ? 106.363 114.982 132.351 1.00 38.48 ?  115 THR C C     1 
ATOM   11906 O  O     . THR C 2 136 ? 106.609 113.810 132.657 1.00 38.74 ?  115 THR C O     1 
ATOM   11907 C  CB    . THR C 2 136 ? 108.070 116.680 133.075 1.00 38.95 ?  115 THR C CB    1 
ATOM   11908 O  OG1   . THR C 2 136 ? 109.122 117.533 132.614 1.00 40.08 ?  115 THR C OG1   1 
ATOM   11909 C  CG2   . THR C 2 136 ? 108.623 115.734 134.142 1.00 39.82 ?  115 THR C CG2   1 
ATOM   11910 N  N     . GLU C 2 137 ? 105.139 115.510 132.409 1.00 38.89 ?  116 GLU C N     1 
ATOM   11911 C  CA    . GLU C 2 137 ? 103.982 114.752 132.908 1.00 38.65 ?  116 GLU C CA    1 
ATOM   11912 C  C     . GLU C 2 137 ? 103.626 113.589 131.989 1.00 37.38 ?  116 GLU C C     1 
ATOM   11913 O  O     . GLU C 2 137 ? 103.260 112.512 132.456 1.00 37.22 ?  116 GLU C O     1 
ATOM   11914 C  CB    . GLU C 2 137 ? 102.754 115.654 133.159 1.00 39.52 ?  116 GLU C CB    1 
ATOM   11915 C  CG    . GLU C 2 137 ? 102.052 116.228 131.906 1.00 41.90 ?  116 GLU C CG    1 
ATOM   11916 C  CD    . GLU C 2 137 ? 102.029 117.765 131.850 1.00 46.43 ?  116 GLU C CD    1 
ATOM   11917 O  OE1   . GLU C 2 137 ? 102.739 118.426 132.646 1.00 47.84 ?  116 GLU C OE1   1 
ATOM   11918 O  OE2   . GLU C 2 137 ? 101.289 118.316 130.998 1.00 47.52 -1 116 GLU C OE2   1 
ATOM   11919 N  N     . THR C 2 138 ? 103.748 113.817 130.684 1.00 36.05 ?  117 THR C N     1 
ATOM   11920 C  CA    . THR C 2 138 ? 103.499 112.786 129.689 1.00 34.88 ?  117 THR C CA    1 
ATOM   11921 C  C     . THR C 2 138 ? 104.595 111.727 129.758 1.00 33.58 ?  117 THR C C     1 
ATOM   11922 O  O     . THR C 2 138 ? 104.316 110.534 129.606 1.00 33.61 ?  117 THR C O     1 
ATOM   11923 C  CB    . THR C 2 138 ? 103.414 113.382 128.277 1.00 34.85 ?  117 THR C CB    1 
ATOM   11924 O  OG1   . THR C 2 138 ? 102.475 114.464 128.285 1.00 35.98 ?  117 THR C OG1   1 
ATOM   11925 C  CG2   . THR C 2 138 ? 102.961 112.334 127.270 1.00 34.92 ?  117 THR C CG2   1 
ATOM   11926 N  N     . ILE C 2 139 ? 105.830 112.168 129.991 1.00 32.29 ?  118 ILE C N     1 
ATOM   11927 C  CA    . ILE C 2 139 ? 106.952 111.253 130.191 1.00 31.19 ?  118 ILE C CA    1 
ATOM   11928 C  C     . ILE C 2 139 ? 106.735 110.396 131.452 1.00 30.85 ?  118 ILE C C     1 
ATOM   11929 O  O     . ILE C 2 139 ? 106.859 109.172 131.394 1.00 29.77 ?  118 ILE C O     1 
ATOM   11930 C  CB    . ILE C 2 139 ? 108.327 111.985 130.234 1.00 31.25 ?  118 ILE C CB    1 
ATOM   11931 C  CG1   . ILE C 2 139 ? 108.576 112.777 128.938 1.00 30.12 ?  118 ILE C CG1   1 
ATOM   11932 C  CG2   . ILE C 2 139 ? 109.474 110.990 130.471 1.00 30.21 ?  118 ILE C CG2   1 
ATOM   11933 C  CD1   . ILE C 2 139 ? 109.848 113.645 128.972 1.00 29.41 ?  118 ILE C CD1   1 
ATOM   11934 N  N     . ASN C 2 140 ? 106.394 111.040 132.573 1.00 31.17 ?  119 ASN C N     1 
ATOM   11935 C  CA    . ASN C 2 140 ? 106.097 110.328 133.827 1.00 31.76 ?  119 ASN C CA    1 
ATOM   11936 C  C     . ASN C 2 140 ? 104.983 109.290 133.651 1.00 31.25 ?  119 ASN C C     1 
ATOM   11937 O  O     . ASN C 2 140 ? 105.113 108.153 134.108 1.00 31.47 ?  119 ASN C O     1 
ATOM   11938 C  CB    . ASN C 2 140 ? 105.705 111.297 134.953 1.00 32.65 ?  119 ASN C CB    1 
ATOM   11939 C  CG    . ASN C 2 140 ? 106.876 112.124 135.474 1.00 35.14 ?  119 ASN C CG    1 
ATOM   11940 O  OD1   . ASN C 2 140 ? 108.040 111.716 135.407 1.00 36.75 ?  119 ASN C OD1   1 
ATOM   11941 N  ND2   . ASN C 2 140 ? 106.556 113.297 136.030 1.00 38.05 ?  119 ASN C ND2   1 
ATOM   11942 N  N     . GLU C 2 141 ? 103.908 109.693 132.977 1.00 30.96 ?  120 GLU C N     1 
ATOM   11943 C  CA    . GLU C 2 141 ? 102.758 108.829 132.715 1.00 30.36 ?  120 GLU C CA    1 
ATOM   11944 C  C     . GLU C 2 141 ? 103.122 107.600 131.879 1.00 28.60 ?  120 GLU C C     1 
ATOM   11945 O  O     . GLU C 2 141 ? 102.665 106.499 132.176 1.00 27.94 ?  120 GLU C O     1 
ATOM   11946 C  CB    . GLU C 2 141 ? 101.638 109.611 132.023 1.00 30.86 ?  120 GLU C CB    1 
ATOM   11947 C  CG    . GLU C 2 141 ? 100.833 110.520 132.945 1.00 34.89 ?  120 GLU C CG    1 
ATOM   11948 C  CD    . GLU C 2 141 ? 99.870  111.421 132.184 1.00 39.82 ?  120 GLU C CD    1 
ATOM   11949 O  OE1   . GLU C 2 141 ? 99.618  111.166 130.980 1.00 41.95 ?  120 GLU C OE1   1 
ATOM   11950 O  OE2   . GLU C 2 141 ? 99.357  112.385 132.789 1.00 41.94 -1 120 GLU C OE2   1 
ATOM   11951 N  N     . VAL C 2 142 ? 103.935 107.777 130.841 1.00 27.29 ?  121 VAL C N     1 
ATOM   11952 C  CA    . VAL C 2 142 ? 104.291 106.619 129.993 1.00 25.89 ?  121 VAL C CA    1 
ATOM   11953 C  C     . VAL C 2 142 ? 105.179 105.605 130.724 1.00 25.11 ?  121 VAL C C     1 
ATOM   11954 O  O     . VAL C 2 142 ? 105.064 104.401 130.500 1.00 24.23 ?  121 VAL C O     1 
ATOM   11955 C  CB    . VAL C 2 142 ? 104.853 107.019 128.585 1.00 25.99 ?  121 VAL C CB    1 
ATOM   11956 C  CG1   . VAL C 2 142 ? 106.360 107.291 128.610 1.00 25.21 ?  121 VAL C CG1   1 
ATOM   11957 C  CG2   . VAL C 2 142 ? 104.547 105.932 127.567 1.00 25.78 ?  121 VAL C CG2   1 
ATOM   11958 N  N     . PHE C 2 143 ? 106.051 106.079 131.608 1.00 24.69 ?  122 PHE C N     1 
ATOM   11959 C  CA    . PHE C 2 143 ? 106.863 105.153 132.411 1.00 24.77 ?  122 PHE C CA    1 
ATOM   11960 C  C     . PHE C 2 143 ? 106.016 104.428 133.472 1.00 24.99 ?  122 PHE C C     1 
ATOM   11961 O  O     . PHE C 2 143 ? 106.258 103.262 133.784 1.00 24.73 ?  122 PHE C O     1 
ATOM   11962 C  CB    . PHE C 2 143 ? 108.097 105.845 133.003 1.00 24.83 ?  122 PHE C CB    1 
ATOM   11963 C  CG    . PHE C 2 143 ? 109.214 106.029 131.998 1.00 25.12 ?  122 PHE C CG    1 
ATOM   11964 C  CD1   . PHE C 2 143 ? 109.976 104.942 131.576 1.00 26.58 ?  122 PHE C CD1   1 
ATOM   11965 C  CD2   . PHE C 2 143 ? 109.488 107.279 131.463 1.00 24.49 ?  122 PHE C CD2   1 
ATOM   11966 C  CE1   . PHE C 2 143 ? 111.000 105.107 130.634 1.00 26.96 ?  122 PHE C CE1   1 
ATOM   11967 C  CE2   . PHE C 2 143 ? 110.502 107.454 130.532 1.00 25.79 ?  122 PHE C CE2   1 
ATOM   11968 C  CZ    . PHE C 2 143 ? 111.262 106.367 130.110 1.00 26.45 ?  122 PHE C CZ    1 
ATOM   11969 N  N     . GLU C 2 144 ? 105.008 105.116 134.004 1.00 25.22 ?  123 GLU C N     1 
ATOM   11970 C  CA    . GLU C 2 144 ? 104.021 104.461 134.867 1.00 25.72 ?  123 GLU C CA    1 
ATOM   11971 C  C     . GLU C 2 144 ? 103.227 103.417 134.084 1.00 25.08 ?  123 GLU C C     1 
ATOM   11972 O  O     . GLU C 2 144 ? 102.955 102.326 134.588 1.00 24.67 ?  123 GLU C O     1 
ATOM   11973 C  CB    . GLU C 2 144 ? 103.096 105.485 135.520 1.00 26.23 ?  123 GLU C CB    1 
ATOM   11974 C  CG    . GLU C 2 144 ? 103.794 106.300 136.596 1.00 29.96 ?  123 GLU C CG    1 
ATOM   11975 C  CD    . GLU C 2 144 ? 104.470 105.421 137.635 1.00 33.82 ?  123 GLU C CD    1 
ATOM   11976 O  OE1   . GLU C 2 144 ? 103.748 104.707 138.364 1.00 36.54 ?  123 GLU C OE1   1 
ATOM   11977 O  OE2   . GLU C 2 144 ? 105.717 105.429 137.712 1.00 35.84 -1 123 GLU C OE2   1 
ATOM   11978 N  N     . TRP C 2 145 ? 102.886 103.752 132.842 1.00 24.21 ?  124 TRP C N     1 
ATOM   11979 C  CA    . TRP C 2 145 ? 102.174 102.835 131.954 1.00 23.99 ?  124 TRP C CA    1 
ATOM   11980 C  C     . TRP C 2 145 ? 102.951 101.545 131.651 1.00 23.95 ?  124 TRP C C     1 
ATOM   11981 O  O     . TRP C 2 145 ? 102.341 100.462 131.578 1.00 23.31 ?  124 TRP C O     1 
ATOM   11982 C  CB    . TRP C 2 145 ? 101.767 103.544 130.652 1.00 24.13 ?  124 TRP C CB    1 
ATOM   11983 C  CG    . TRP C 2 145 ? 101.295 102.598 129.572 1.00 24.37 ?  124 TRP C CG    1 
ATOM   11984 C  CD1   . TRP C 2 145 ? 100.013 102.148 129.363 1.00 24.76 ?  124 TRP C CD1   1 
ATOM   11985 C  CD2   . TRP C 2 145 ? 102.104 101.994 128.555 1.00 23.31 ?  124 TRP C CD2   1 
ATOM   11986 N  NE1   . TRP C 2 145 ? 99.985  101.293 128.277 1.00 24.97 ?  124 TRP C NE1   1 
ATOM   11987 C  CE2   . TRP C 2 145 ? 101.252 101.184 127.763 1.00 24.20 ?  124 TRP C CE2   1 
ATOM   11988 C  CE3   . TRP C 2 145 ? 103.469 102.048 128.240 1.00 23.76 ?  124 TRP C CE3   1 
ATOM   11989 C  CZ2   . TRP C 2 145 ? 101.724 100.439 126.674 1.00 23.41 ?  124 TRP C CZ2   1 
ATOM   11990 C  CZ3   . TRP C 2 145 ? 103.939 101.304 127.159 1.00 23.29 ?  124 TRP C CZ3   1 
ATOM   11991 C  CH2   . TRP C 2 145 ? 103.063 100.515 126.386 1.00 22.93 ?  124 TRP C CH2   1 
ATOM   11992 N  N     . VAL C 2 146 ? 104.272 101.630 131.466 1.00 23.35 ?  125 VAL C N     1 
ATOM   11993 C  CA    . VAL C 2 146 ? 105.036 100.370 131.272 1.00 23.53 ?  125 VAL C CA    1 
ATOM   11994 C  C     . VAL C 2 146 ? 104.932 99.433  132.481 1.00 23.73 ?  125 VAL C C     1 
ATOM   11995 O  O     . VAL C 2 146 ? 104.768 98.235  132.305 1.00 23.03 ?  125 VAL C O     1 
ATOM   11996 C  CB    . VAL C 2 146 ? 106.518 100.514 130.684 1.00 23.63 ?  125 VAL C CB    1 
ATOM   11997 C  CG1   . VAL C 2 146 ? 106.891 101.920 130.300 1.00 24.40 ?  125 VAL C CG1   1 
ATOM   11998 C  CG2   . VAL C 2 146 ? 107.600 99.830  131.541 1.00 22.97 ?  125 VAL C CG2   1 
ATOM   11999 N  N     . LYS C 2 147 ? 104.968 99.994  133.693 1.00 24.06 ?  126 LYS C N     1 
ATOM   12000 C  CA    . LYS C 2 147 ? 104.905 99.186  134.923 1.00 25.41 ?  126 LYS C CA    1 
ATOM   12001 C  C     . LYS C 2 147 ? 103.611 98.381  135.060 1.00 25.82 ?  126 LYS C C     1 
ATOM   12002 O  O     . LYS C 2 147 ? 103.623 97.285  135.625 1.00 26.08 ?  126 LYS C O     1 
ATOM   12003 C  CB    . LYS C 2 147 ? 105.072 100.065 136.165 1.00 25.49 ?  126 LYS C CB    1 
ATOM   12004 C  CG    . LYS C 2 147 ? 106.445 100.679 136.342 1.00 27.52 ?  126 LYS C CG    1 
ATOM   12005 C  CD    . LYS C 2 147 ? 106.433 101.591 137.563 1.00 30.43 ?  126 LYS C CD    1 
ATOM   12006 C  CE    . LYS C 2 147 ? 107.647 102.495 137.600 1.00 33.10 ?  126 LYS C CE    1 
ATOM   12007 N  NZ    . LYS C 2 147 ? 107.539 103.452 138.737 1.00 34.86 1  126 LYS C NZ    1 
ATOM   12008 N  N     . GLN C 2 148 ? 102.507 98.926  134.549 1.00 26.45 ?  127 GLN C N     1 
ATOM   12009 C  CA    . GLN C 2 148 ? 101.186 98.318  134.728 1.00 26.85 ?  127 GLN C CA    1 
ATOM   12010 C  C     . GLN C 2 148 ? 100.641 97.602  133.490 1.00 26.01 ?  127 GLN C C     1 
ATOM   12011 O  O     . GLN C 2 148 ? 99.589  96.965  133.564 1.00 26.12 ?  127 GLN C O     1 
ATOM   12012 C  CB    . GLN C 2 148 ? 100.166 99.352  135.244 1.00 28.08 ?  127 GLN C CB    1 
ATOM   12013 C  CG    . GLN C 2 148 ? 99.892  100.529 134.302 1.00 30.69 ?  127 GLN C CG    1 
ATOM   12014 C  CD    . GLN C 2 148 ? 99.010  100.159 133.113 1.00 34.64 ?  127 GLN C CD    1 
ATOM   12015 O  OE1   . GLN C 2 148 ? 99.456  100.195 131.952 1.00 33.80 ?  127 GLN C OE1   1 
ATOM   12016 N  NE2   . GLN C 2 148 ? 97.754  99.788  133.393 1.00 36.24 ?  127 GLN C NE2   1 
ATOM   12017 N  N     . ASN C 2 149 ? 101.344 97.712  132.359 1.00 24.97 ?  128 ASN C N     1 
ATOM   12018 C  CA    . ASN C 2 149 ? 100.912 97.060  131.126 1.00 24.03 ?  128 ASN C CA    1 
ATOM   12019 C  C     . ASN C 2 149 ? 101.192 95.566  131.181 1.00 24.13 ?  128 ASN C C     1 
ATOM   12020 O  O     . ASN C 2 149 ? 102.353 95.169  131.311 1.00 22.93 ?  128 ASN C O     1 
ATOM   12021 C  CB    . ASN C 2 149 ? 101.637 97.652  129.928 1.00 23.97 ?  128 ASN C CB    1 
ATOM   12022 C  CG    . ASN C 2 149 ? 101.122 97.105  128.619 1.00 23.94 ?  128 ASN C CG    1 
ATOM   12023 O  OD1   . ASN C 2 149 ? 101.608 96.089  128.123 1.00 24.85 ?  128 ASN C OD1   1 
ATOM   12024 N  ND2   . ASN C 2 149 ? 100.098 97.746  128.073 1.00 24.76 ?  128 ASN C ND2   1 
ATOM   12025 N  N     . LYS C 2 150 ? 100.145 94.747  131.053 1.00 24.32 ?  129 LYS C N     1 
ATOM   12026 C  CA    . LYS C 2 150 ? 100.276 93.296  131.294 1.00 24.77 ?  129 LYS C CA    1 
ATOM   12027 C  C     . LYS C 2 150 ? 101.101 92.529  130.258 1.00 24.54 ?  129 LYS C C     1 
ATOM   12028 O  O     . LYS C 2 150 ? 101.762 91.547  130.600 1.00 24.17 ?  129 LYS C O     1 
ATOM   12029 C  CB    . LYS C 2 150 ? 98.912  92.633  131.521 1.00 25.27 ?  129 LYS C CB    1 
ATOM   12030 C  CG    . LYS C 2 150 ? 97.945  92.699  130.356 1.00 28.72 ?  129 LYS C CG    1 
ATOM   12031 C  CD    . LYS C 2 150 ? 96.793  91.719  130.585 1.00 33.40 ?  129 LYS C CD    1 
ATOM   12032 C  CE    . LYS C 2 150 ? 95.573  92.100  129.768 1.00 36.77 ?  129 LYS C CE    1 
ATOM   12033 N  NZ    . LYS C 2 150 ? 94.400  91.264  130.169 1.00 39.66 1  129 LYS C NZ    1 
ATOM   12034 N  N     . TYR C 2 151 ? 101.056 92.973  128.997 1.00 23.92 ?  130 TYR C N     1 
ATOM   12035 C  CA    . TYR C 2 151 ? 101.824 92.329  127.923 1.00 24.12 ?  130 TYR C CA    1 
ATOM   12036 C  C     . TYR C 2 151 ? 103.313 92.616  128.027 1.00 23.54 ?  130 TYR C C     1 
ATOM   12037 O  O     . TYR C 2 151 ? 104.150 91.733  127.783 1.00 23.32 ?  130 TYR C O     1 
ATOM   12038 C  CB    . TYR C 2 151 ? 101.274 92.744  126.546 1.00 24.53 ?  130 TYR C CB    1 
ATOM   12039 C  CG    . TYR C 2 151 ? 99.762  92.708  126.498 1.00 25.83 ?  130 TYR C CG    1 
ATOM   12040 C  CD1   . TYR C 2 151 ? 99.072  91.505  126.648 1.00 26.57 ?  130 TYR C CD1   1 
ATOM   12041 C  CD2   . TYR C 2 151 ? 99.019  93.885  126.348 1.00 27.87 ?  130 TYR C CD2   1 
ATOM   12042 C  CE1   . TYR C 2 151 ? 97.682  91.461  126.628 1.00 29.65 ?  130 TYR C CE1   1 
ATOM   12043 C  CE2   . TYR C 2 151 ? 97.619  93.854  126.330 1.00 29.91 ?  130 TYR C CE2   1 
ATOM   12044 C  CZ    . TYR C 2 151 ? 96.963  92.639  126.472 1.00 31.19 ?  130 TYR C CZ    1 
ATOM   12045 O  OH    . TYR C 2 151 ? 95.584  92.588  126.455 1.00 34.44 ?  130 TYR C OH    1 
ATOM   12046 N  N     . LEU C 2 152 ? 103.640 93.852  128.389 1.00 23.38 ?  131 LEU C N     1 
ATOM   12047 C  CA    . LEU C 2 152 ? 105.020 94.263  128.570 1.00 23.43 ?  131 LEU C CA    1 
ATOM   12048 C  C     . LEU C 2 152 ? 105.609 93.584  129.811 1.00 23.37 ?  131 LEU C C     1 
ATOM   12049 O  O     . LEU C 2 152 ? 106.749 93.109  129.777 1.00 23.05 ?  131 LEU C O     1 
ATOM   12050 C  CB    . LEU C 2 152 ? 105.077 95.786  128.686 1.00 23.73 ?  131 LEU C CB    1 
ATOM   12051 C  CG    . LEU C 2 152 ? 106.081 96.678  127.966 1.00 24.71 ?  131 LEU C CG    1 
ATOM   12052 C  CD1   . LEU C 2 152 ? 106.773 96.041  126.749 1.00 21.63 ?  131 LEU C CD1   1 
ATOM   12053 C  CD2   . LEU C 2 152 ? 105.387 97.961  127.572 1.00 26.87 ?  131 LEU C CD2   1 
ATOM   12054 N  N     . GLN C 2 153 ? 104.842 93.534  130.904 1.00 22.80 ?  132 GLN C N     1 
ATOM   12055 C  CA    . GLN C 2 153 ? 105.282 92.770  132.083 1.00 22.70 ?  132 GLN C CA    1 
ATOM   12056 C  C     . GLN C 2 153 ? 105.455 91.275  131.802 1.00 22.54 ?  132 GLN C C     1 
ATOM   12057 O  O     . GLN C 2 153 ? 106.456 90.678  132.227 1.00 21.73 ?  132 GLN C O     1 
ATOM   12058 C  CB    . GLN C 2 153 ? 104.383 93.014  133.298 1.00 23.07 ?  132 GLN C CB    1 
ATOM   12059 C  CG    . GLN C 2 153 ? 104.426 94.463  133.785 1.00 21.83 ?  132 GLN C CG    1 
ATOM   12060 C  CD    . GLN C 2 153 ? 105.831 94.935  134.165 1.00 22.34 ?  132 GLN C CD    1 
ATOM   12061 O  OE1   . GLN C 2 153 ? 106.559 94.251  134.889 1.00 24.07 ?  132 GLN C OE1   1 
ATOM   12062 N  NE2   . GLN C 2 153 ? 106.207 96.114  133.689 1.00 22.26 ?  132 GLN C NE2   1 
ATOM   12063 N  N     . LYS C 2 154 ? 104.500 90.674  131.086 1.00 22.53 ?  133 LYS C N     1 
ATOM   12064 C  CA    . LYS C 2 154 ? 104.626 89.262  130.726 1.00 22.84 ?  133 LYS C CA    1 
ATOM   12065 C  C     . LYS C 2 154 ? 105.886 88.985  129.904 1.00 22.42 ?  133 LYS C C     1 
ATOM   12066 O  O     . LYS C 2 154 ? 106.598 88.030  130.193 1.00 21.90 ?  133 LYS C O     1 
ATOM   12067 C  CB    . LYS C 2 154 ? 103.365 88.707  130.022 1.00 22.96 ?  133 LYS C CB    1 
ATOM   12068 C  CG    . LYS C 2 154 ? 103.448 87.191  129.664 1.00 23.45 ?  133 LYS C CG    1 
ATOM   12069 C  CD    . LYS C 2 154 ? 103.531 86.271  130.902 1.00 26.74 ?  133 LYS C CD    1 
ATOM   12070 C  CE    . LYS C 2 154 ? 103.566 84.789  130.501 1.00 27.93 ?  133 LYS C CE    1 
ATOM   12071 N  NZ    . LYS C 2 154 ? 103.851 83.875  131.639 1.00 27.86 1  133 LYS C NZ    1 
ATOM   12072 N  N     . LYS C 2 155 ? 106.179 89.819  128.902 1.00 22.77 ?  134 LYS C N     1 
ATOM   12073 C  CA    . LYS C 2 155 ? 107.330 89.533  128.039 1.00 22.87 ?  134 LYS C CA    1 
ATOM   12074 C  C     . LYS C 2 155 ? 108.650 89.702  128.784 1.00 22.30 ?  134 LYS C C     1 
ATOM   12075 O  O     . LYS C 2 155 ? 109.557 88.866  128.630 1.00 21.89 ?  134 LYS C O     1 
ATOM   12076 C  CB    . LYS C 2 155 ? 107.285 90.285  126.688 1.00 23.33 ?  134 LYS C CB    1 
ATOM   12077 C  CG    . LYS C 2 155 ? 107.638 91.751  126.700 1.00 24.25 ?  134 LYS C CG    1 
ATOM   12078 C  CD    . LYS C 2 155 ? 107.562 92.352  125.286 1.00 26.87 ?  134 LYS C CD    1 
ATOM   12079 C  CE    . LYS C 2 155 ? 106.140 92.785  124.943 1.00 28.26 ?  134 LYS C CE    1 
ATOM   12080 N  NZ    . LYS C 2 155 ? 106.139 93.644  123.720 1.00 28.97 1  134 LYS C NZ    1 
ATOM   12081 N  N     . ALA C 2 156 ? 108.734 90.739  129.617 1.00 21.96 ?  135 ALA C N     1 
ATOM   12082 C  CA    . ALA C 2 156 ? 109.873 90.914  130.539 1.00 22.43 ?  135 ALA C CA    1 
ATOM   12083 C  C     . ALA C 2 156 ? 110.024 89.751  131.522 1.00 22.02 ?  135 ALA C C     1 
ATOM   12084 O  O     . ALA C 2 156 ? 111.135 89.283  131.753 1.00 22.60 ?  135 ALA C O     1 
ATOM   12085 C  CB    . ALA C 2 156 ? 109.765 92.243  131.318 1.00 22.05 ?  135 ALA C CB    1 
ATOM   12086 N  N     . GLN C 2 157 ? 108.916 89.304  132.113 1.00 21.97 ?  136 GLN C N     1 
ATOM   12087 C  CA    . GLN C 2 157 ? 108.946 88.167  133.043 1.00 22.10 ?  136 GLN C CA    1 
ATOM   12088 C  C     . GLN C 2 157 ? 109.542 86.939  132.386 1.00 21.87 ?  136 GLN C C     1 
ATOM   12089 O  O     . GLN C 2 157 ? 110.363 86.250  132.989 1.00 21.75 ?  136 GLN C O     1 
ATOM   12090 C  CB    . GLN C 2 157 ? 107.544 87.801  133.530 1.00 22.50 ?  136 GLN C CB    1 
ATOM   12091 C  CG    . GLN C 2 157 ? 106.998 88.680  134.644 1.00 23.55 ?  136 GLN C CG    1 
ATOM   12092 C  CD    . GLN C 2 157 ? 105.490 88.540  134.751 1.00 26.93 ?  136 GLN C CD    1 
ATOM   12093 O  OE1   . GLN C 2 157 ? 104.929 87.527  134.337 1.00 26.36 ?  136 GLN C OE1   1 
ATOM   12094 N  NE2   . GLN C 2 157 ? 104.826 89.563  135.277 1.00 28.09 ?  136 GLN C NE2   1 
ATOM   12095 N  N     . MET C 2 158 ? 109.104 86.669  131.157 1.00 21.38 ?  137 MET C N     1 
ATOM   12096 C  CA    . MET C 2 158 ? 109.514 85.475  130.432 1.00 22.08 ?  137 MET C CA    1 
ATOM   12097 C  C     . MET C 2 158 ? 110.979 85.526  130.015 1.00 21.70 ?  137 MET C C     1 
ATOM   12098 O  O     . MET C 2 158 ? 111.709 84.541  130.136 1.00 21.83 ?  137 MET C O     1 
ATOM   12099 C  CB    . MET C 2 158 ? 108.656 85.292  129.185 1.00 22.05 ?  137 MET C CB    1 
ATOM   12100 C  CG    . MET C 2 158 ? 107.235 84.784  129.461 1.00 23.93 ?  137 MET C CG    1 
ATOM   12101 S  SD    . MET C 2 158 ? 106.260 84.824  127.943 1.00 27.75 ?  137 MET C SD    1 
ATOM   12102 C  CE    . MET C 2 158 ? 107.073 83.507  127.025 1.00 26.00 ?  137 MET C CE    1 
ATOM   12103 N  N     . ILE C 2 159 ? 111.394 86.668  129.485 1.00 20.90 ?  138 ILE C N     1 
ATOM   12104 C  CA    . ILE C 2 159 ? 112.749 86.795  128.975 1.00 20.60 ?  138 ILE C CA    1 
ATOM   12105 C  C     . ILE C 2 159 ? 113.752 86.823  130.132 1.00 20.36 ?  138 ILE C C     1 
ATOM   12106 O  O     . ILE C 2 159 ? 114.725 86.067  130.123 1.00 19.65 ?  138 ILE C O     1 
ATOM   12107 C  CB    . ILE C 2 159 ? 112.898 88.028  128.036 1.00 20.17 ?  138 ILE C CB    1 
ATOM   12108 C  CG1   . ILE C 2 159 ? 112.071 87.837  126.751 1.00 20.66 ?  138 ILE C CG1   1 
ATOM   12109 C  CG2   . ILE C 2 159 ? 114.379 88.347  127.772 1.00 20.62 ?  138 ILE C CG2   1 
ATOM   12110 C  CD1   . ILE C 2 159 ? 112.488 86.695  125.820 1.00 22.17 ?  138 ILE C CD1   1 
ATOM   12111 N  N     . VAL C 2 160 ? 113.496 87.671  131.129 1.00 19.58 ?  139 VAL C N     1 
ATOM   12112 C  CA    . VAL C 2 160 ? 114.401 87.823  132.273 1.00 19.88 ?  139 VAL C CA    1 
ATOM   12113 C  C     . VAL C 2 160 ? 114.430 86.543  133.112 1.00 19.44 ?  139 VAL C C     1 
ATOM   12114 O  O     . VAL C 2 160 ? 115.449 86.207  133.707 1.00 19.88 ?  139 VAL C O     1 
ATOM   12115 C  CB    . VAL C 2 160 ? 114.032 89.055  133.177 1.00 19.52 ?  139 VAL C CB    1 
ATOM   12116 C  CG1   . VAL C 2 160 ? 114.946 89.126  134.414 1.00 20.75 ?  139 VAL C CG1   1 
ATOM   12117 C  CG2   . VAL C 2 160 ? 114.156 90.357  132.394 1.00 20.03 ?  139 VAL C CG2   1 
ATOM   12118 N  N     . GLY C 2 161 ? 113.312 85.824  133.152 1.00 19.13 ?  140 GLY C N     1 
ATOM   12119 C  CA    . GLY C 2 161 ? 113.265 84.571  133.888 1.00 18.05 ?  140 GLY C CA    1 
ATOM   12120 C  C     . GLY C 2 161 ? 114.263 83.591  133.327 1.00 17.86 ?  140 GLY C C     1 
ATOM   12121 O  O     . GLY C 2 161 ? 114.995 82.929  134.071 1.00 17.47 ?  140 GLY C O     1 
ATOM   12122 N  N     . LEU C 2 162 ? 114.287 83.486  132.003 1.00 17.92 ?  141 LEU C N     1 
ATOM   12123 C  CA    . LEU C 2 162 ? 115.246 82.618  131.330 1.00 18.32 ?  141 LEU C CA    1 
ATOM   12124 C  C     . LEU C 2 162 ? 116.711 83.058  131.551 1.00 18.55 ?  141 LEU C C     1 
ATOM   12125 O  O     . LEU C 2 162 ? 117.576 82.216  131.786 1.00 18.49 ?  141 LEU C O     1 
ATOM   12126 C  CB    . LEU C 2 162 ? 114.909 82.521  129.837 1.00 18.50 ?  141 LEU C CB    1 
ATOM   12127 C  CG    . LEU C 2 162 ? 113.632 81.729  129.540 1.00 19.32 ?  141 LEU C CG    1 
ATOM   12128 C  CD1   . LEU C 2 162 ? 113.154 81.999  128.117 1.00 20.38 ?  141 LEU C CD1   1 
ATOM   12129 C  CD2   . LEU C 2 162 ? 113.844 80.232  129.779 1.00 19.94 ?  141 LEU C CD2   1 
ATOM   12130 N  N     . TYR C 2 163 ? 116.980 84.360  131.512 1.00 19.16 ?  142 TYR C N     1 
ATOM   12131 C  CA    . TYR C 2 163 ? 118.326 84.871  131.845 1.00 20.16 ?  142 TYR C CA    1 
ATOM   12132 C  C     . TYR C 2 163 ? 118.764 84.462  133.239 1.00 20.78 ?  142 TYR C C     1 
ATOM   12133 O  O     . TYR C 2 163 ? 119.911 84.060  133.456 1.00 20.36 ?  142 TYR C O     1 
ATOM   12134 C  CB    . TYR C 2 163 ? 118.393 86.406  131.755 1.00 20.34 ?  142 TYR C CB    1 
ATOM   12135 C  CG    . TYR C 2 163 ? 118.195 86.982  130.361 1.00 22.46 ?  142 TYR C CG    1 
ATOM   12136 C  CD1   . TYR C 2 163 ? 118.454 86.228  129.221 1.00 23.88 ?  142 TYR C CD1   1 
ATOM   12137 C  CD2   . TYR C 2 163 ? 117.758 88.291  130.191 1.00 22.41 ?  142 TYR C CD2   1 
ATOM   12138 C  CE1   . TYR C 2 163 ? 118.266 86.769  127.936 1.00 25.93 ?  142 TYR C CE1   1 
ATOM   12139 C  CE2   . TYR C 2 163 ? 117.574 88.835  128.923 1.00 22.07 ?  142 TYR C CE2   1 
ATOM   12140 C  CZ    . TYR C 2 163 ? 117.837 88.077  127.807 1.00 25.19 ?  142 TYR C CZ    1 
ATOM   12141 O  OH    . TYR C 2 163 ? 117.644 88.641  126.562 1.00 27.43 ?  142 TYR C OH    1 
ATOM   12142 N  N     . LYS C 2 164 ? 117.844 84.562  134.191 1.00 21.39 ?  143 LYS C N     1 
ATOM   12143 C  CA    . LYS C 2 164 ? 118.200 84.304  135.577 1.00 22.49 ?  143 LYS C CA    1 
ATOM   12144 C  C     . LYS C 2 164 ? 118.208 82.816  135.918 1.00 22.49 ?  143 LYS C C     1 
ATOM   12145 O  O     . LYS C 2 164 ? 118.707 82.427  136.968 1.00 22.45 ?  143 LYS C O     1 
ATOM   12146 C  CB    . LYS C 2 164 ? 117.344 85.137  136.528 1.00 23.16 ?  143 LYS C CB    1 
ATOM   12147 C  CG    . LYS C 2 164 ? 117.662 86.625  136.405 1.00 26.08 ?  143 LYS C CG    1 
ATOM   12148 C  CD    . LYS C 2 164 ? 117.270 87.397  137.631 1.00 30.38 ?  143 LYS C CD    1 
ATOM   12149 C  CE    . LYS C 2 164 ? 117.770 88.819  137.553 1.00 32.69 ?  143 LYS C CE    1 
ATOM   12150 N  NZ    . LYS C 2 164 ? 117.333 89.586  138.752 1.00 35.60 1  143 LYS C NZ    1 
ATOM   12151 N  N     . ALA C 2 165 ? 117.724 81.988  134.991 1.00 22.02 ?  144 ALA C N     1 
ATOM   12152 C  CA    . ALA C 2 165 ? 117.762 80.549  135.173 1.00 22.69 ?  144 ALA C CA    1 
ATOM   12153 C  C     . ALA C 2 165 ? 119.084 79.915  134.707 1.00 23.20 ?  144 ALA C C     1 
ATOM   12154 O  O     . ALA C 2 165 ? 119.309 78.732  134.931 1.00 23.80 ?  144 ALA C O     1 
ATOM   12155 C  CB    . ALA C 2 165 ? 116.548 79.881  134.481 1.00 21.79 ?  144 ALA C CB    1 
ATOM   12156 N  N     . ILE C 2 166 ? 119.959 80.689  134.061 1.00 23.97 ?  145 ILE C N     1 
ATOM   12157 C  CA    . ILE C 2 166 ? 121.247 80.148  133.611 1.00 24.29 ?  145 ILE C CA    1 
ATOM   12158 C  C     . ILE C 2 166 ? 122.034 79.587  134.798 1.00 25.49 ?  145 ILE C C     1 
ATOM   12159 O  O     . ILE C 2 166 ? 122.146 80.233  135.836 1.00 25.82 ?  145 ILE C O     1 
ATOM   12160 C  CB    . ILE C 2 166 ? 122.117 81.195  132.858 1.00 24.22 ?  145 ILE C CB    1 
ATOM   12161 C  CG1   . ILE C 2 166 ? 121.403 81.710  131.612 1.00 23.45 ?  145 ILE C CG1   1 
ATOM   12162 C  CG2   . ILE C 2 166 ? 123.466 80.591  132.464 1.00 23.42 ?  145 ILE C CG2   1 
ATOM   12163 C  CD1   . ILE C 2 166 ? 122.060 82.972  130.996 1.00 21.99 ?  145 ILE C CD1   1 
ATOM   12164 N  N     . GLN C 2 167 ? 122.525 78.365  134.649 1.00 26.83 ?  146 GLN C N     1 
ATOM   12165 C  CA    . GLN C 2 167 ? 123.331 77.729  135.682 1.00 28.85 ?  146 GLN C CA    1 
ATOM   12166 C  C     . GLN C 2 167 ? 124.756 77.629  135.172 1.00 29.77 ?  146 GLN C C     1 
ATOM   12167 O  O     . GLN C 2 167 ? 124.981 77.287  134.007 1.00 29.74 ?  146 GLN C O     1 
ATOM   12168 C  CB    . GLN C 2 167 ? 122.793 76.334  136.033 1.00 28.99 ?  146 GLN C CB    1 
ATOM   12169 C  CG    . GLN C 2 167 ? 121.479 76.334  136.815 1.00 30.30 ?  146 GLN C CG    1 
ATOM   12170 C  CD    . GLN C 2 167 ? 121.638 76.826  138.248 1.00 33.32 ?  146 GLN C CD    1 
ATOM   12171 O  OE1   . GLN C 2 167 ? 122.757 76.995  138.737 1.00 34.63 ?  146 GLN C OE1   1 
ATOM   12172 N  NE2   . GLN C 2 167 ? 120.517 77.036  138.934 1.00 32.32 ?  146 GLN C NE2   1 
ATOM   12173 N  N     . LYS C 2 168 ? 125.710 77.933  136.043 1.00 31.29 ?  147 LYS C N     1 
ATOM   12174 C  CA    . LYS C 2 168 ? 127.128 77.863  135.690 1.00 33.14 ?  147 LYS C CA    1 
ATOM   12175 C  C     . LYS C 2 168 ? 127.444 76.480  135.136 1.00 33.79 ?  147 LYS C C     1 
ATOM   12176 O  O     . LYS C 2 168 ? 126.916 75.471  135.615 1.00 34.06 ?  147 LYS C O     1 
ATOM   12177 C  CB    . LYS C 2 168 ? 127.997 78.183  136.903 1.00 33.44 ?  147 LYS C CB    1 
ATOM   12178 C  CG    . LYS C 2 168 ? 129.421 78.636  136.590 1.00 35.61 ?  147 LYS C CG    1 
ATOM   12179 C  CD    . LYS C 2 168 ? 130.152 78.966  137.887 1.00 38.40 ?  147 LYS C CD    1 
ATOM   12180 C  CE    . LYS C 2 168 ? 131.468 79.689  137.651 1.00 40.48 ?  147 LYS C CE    1 
ATOM   12181 N  NZ    . LYS C 2 168 ? 132.608 78.734  137.679 1.00 41.56 1  147 LYS C NZ    1 
ATOM   12182 N  N     . ASP C 2 169 ? 128.268 76.451  134.093 1.00 35.10 ?  148 ASP C N     1 
ATOM   12183 C  CA    . ASP C 2 169 ? 128.686 75.202  133.435 1.00 36.27 ?  148 ASP C CA    1 
ATOM   12184 C  C     . ASP C 2 169 ? 127.545 74.341  132.888 1.00 36.29 ?  148 ASP C C     1 
ATOM   12185 O  O     . ASP C 2 169 ? 127.740 73.163  132.587 1.00 36.95 ?  148 ASP C O     1 
ATOM   12186 C  CB    . ASP C 2 169 ? 129.555 74.364  134.379 1.00 37.15 ?  148 ASP C CB    1 
ATOM   12187 C  CG    . ASP C 2 169 ? 130.907 74.977  134.622 1.00 38.94 ?  148 ASP C CG    1 
ATOM   12188 O  OD1   . ASP C 2 169 ? 131.357 75.798  133.788 1.00 41.71 ?  148 ASP C OD1   1 
ATOM   12189 O  OD2   . ASP C 2 169 ? 131.522 74.636  135.653 1.00 41.64 -1 148 ASP C OD2   1 
ATOM   12190 N  N     . ASP C 2 170 ? 126.357 74.920  132.763 1.00 35.87 ?  149 ASP C N     1 
ATOM   12191 C  CA    . ASP C 2 170 ? 125.225 74.193  132.206 1.00 35.24 ?  149 ASP C CA    1 
ATOM   12192 C  C     . ASP C 2 170 ? 124.849 74.858  130.890 1.00 34.12 ?  149 ASP C C     1 
ATOM   12193 O  O     . ASP C 2 170 ? 124.191 75.917  130.859 1.00 33.52 ?  149 ASP C O     1 
ATOM   12194 C  CB    . ASP C 2 170 ? 124.061 74.142  133.203 1.00 36.09 ?  149 ASP C CB    1 
ATOM   12195 C  CG    . ASP C 2 170 ? 122.781 73.559  132.605 1.00 38.39 ?  149 ASP C CG    1 
ATOM   12196 O  OD1   . ASP C 2 170 ? 122.816 72.928  131.522 1.00 42.06 ?  149 ASP C OD1   1 
ATOM   12197 O  OD2   . ASP C 2 170 ? 121.721 73.727  133.238 1.00 42.21 -1 149 ASP C OD2   1 
ATOM   12198 N  N     . GLU C 2 171 ? 125.297 74.227  129.809 1.00 32.48 ?  150 GLU C N     1 
ATOM   12199 C  CA    . GLU C 2 171 ? 125.184 74.784  128.472 1.00 30.93 ?  150 GLU C CA    1 
ATOM   12200 C  C     . GLU C 2 171 ? 123.736 74.845  127.977 1.00 29.37 ?  150 GLU C C     1 
ATOM   12201 O  O     . GLU C 2 171 ? 123.398 75.705  127.163 1.00 28.99 ?  150 GLU C O     1 
ATOM   12202 C  CB    . GLU C 2 171 ? 126.094 74.028  127.485 1.00 31.30 ?  150 GLU C CB    1 
ATOM   12203 C  CG    . GLU C 2 171 ? 125.659 72.592  127.105 1.00 33.64 ?  150 GLU C CG    1 
ATOM   12204 C  CD    . GLU C 2 171 ? 126.751 71.780  126.366 1.00 36.40 ?  150 GLU C CD    1 
ATOM   12205 O  OE1   . GLU C 2 171 ? 127.848 72.318  126.100 1.00 38.62 ?  150 GLU C OE1   1 
ATOM   12206 O  OE2   . GLU C 2 171 ? 126.511 70.593  126.051 1.00 37.42 -1 150 GLU C OE2   1 
ATOM   12207 N  N     . ILE C 2 172 ? 122.890 73.936  128.463 1.00 27.68 ?  151 ILE C N     1 
ATOM   12208 C  CA    . ILE C 2 172 ? 121.485 73.911  128.046 1.00 26.26 ?  151 ILE C CA    1 
ATOM   12209 C  C     . ILE C 2 172 ? 120.726 75.128  128.582 1.00 24.85 ?  151 ILE C C     1 
ATOM   12210 O  O     . ILE C 2 172 ? 119.974 75.751  127.835 1.00 23.53 ?  151 ILE C O     1 
ATOM   12211 C  CB    . ILE C 2 172 ? 120.775 72.583  128.424 1.00 26.53 ?  151 ILE C CB    1 
ATOM   12212 C  CG1   . ILE C 2 172 ? 121.452 71.388  127.731 1.00 27.59 ?  151 ILE C CG1   1 
ATOM   12213 C  CG2   . ILE C 2 172 ? 119.266 72.641  128.118 1.00 26.51 ?  151 ILE C CG2   1 
ATOM   12214 C  CD1   . ILE C 2 172 ? 121.320 71.350  126.202 1.00 26.91 ?  151 ILE C CD1   1 
ATOM   12215 N  N     . SER C 2 173 ? 120.928 75.476  129.855 1.00 23.58 ?  152 SER C N     1 
ATOM   12216 C  CA    . SER C 2 173 ? 120.272 76.665  130.394 1.00 22.36 ?  152 SER C CA    1 
ATOM   12217 C  C     . SER C 2 173 ? 120.775 77.922  129.682 1.00 21.79 ?  152 SER C C     1 
ATOM   12218 O  O     . SER C 2 173 ? 120.014 78.876  129.477 1.00 20.91 ?  152 SER C O     1 
ATOM   12219 C  CB    . SER C 2 173 ? 120.426 76.773  131.917 1.00 22.43 ?  152 SER C CB    1 
ATOM   12220 O  OG    . SER C 2 173 ? 121.788 76.867  132.302 1.00 24.02 ?  152 SER C OG    1 
ATOM   12221 N  N     . LEU C 2 174 ? 122.055 77.913  129.308 1.00 21.65 ?  153 LEU C N     1 
ATOM   12222 C  CA    . LEU C 2 174 ? 122.653 79.024  128.573 1.00 21.86 ?  153 LEU C CA    1 
ATOM   12223 C  C     . LEU C 2 174 ? 122.037 79.155  127.178 1.00 21.98 ?  153 LEU C C     1 
ATOM   12224 O  O     . LEU C 2 174 ? 121.676 80.262  126.773 1.00 21.64 ?  153 LEU C O     1 
ATOM   12225 C  CB    . LEU C 2 174 ? 124.190 78.907  128.506 1.00 21.71 ?  153 LEU C CB    1 
ATOM   12226 C  CG    . LEU C 2 174 ? 124.984 79.993  127.753 1.00 22.04 ?  153 LEU C CG    1 
ATOM   12227 C  CD1   . LEU C 2 174 ? 124.637 81.407  128.217 1.00 21.99 ?  153 LEU C CD1   1 
ATOM   12228 C  CD2   . LEU C 2 174 ? 126.488 79.735  127.899 1.00 23.37 ?  153 LEU C CD2   1 
ATOM   12229 N  N     . PHE C 2 175 ? 121.911 78.032  126.463 1.00 22.17 ?  154 PHE C N     1 
ATOM   12230 C  CA    . PHE C 2 175 ? 121.244 78.000  125.142 1.00 22.02 ?  154 PHE C CA    1 
ATOM   12231 C  C     . PHE C 2 175 ? 119.845 78.601  125.194 1.00 21.86 ?  154 PHE C C     1 
ATOM   12232 O  O     . PHE C 2 175 ? 119.450 79.370  124.309 1.00 21.62 ?  154 PHE C O     1 
ATOM   12233 C  CB    . PHE C 2 175 ? 121.137 76.560  124.616 1.00 22.08 ?  154 PHE C CB    1 
ATOM   12234 C  CG    . PHE C 2 175 ? 120.317 76.427  123.348 1.00 21.99 ?  154 PHE C CG    1 
ATOM   12235 C  CD1   . PHE C 2 175 ? 120.891 76.676  122.098 1.00 20.87 ?  154 PHE C CD1   1 
ATOM   12236 C  CD2   . PHE C 2 175 ? 118.962 76.067  123.408 1.00 20.82 ?  154 PHE C CD2   1 
ATOM   12237 C  CE1   . PHE C 2 175 ? 120.136 76.585  120.928 1.00 20.27 ?  154 PHE C CE1   1 
ATOM   12238 C  CE2   . PHE C 2 175 ? 118.194 75.960  122.245 1.00 20.19 ?  154 PHE C CE2   1 
ATOM   12239 C  CZ    . PHE C 2 175 ? 118.784 76.214  120.994 1.00 20.93 ?  154 PHE C CZ    1 
ATOM   12240 N  N     . LYS C 2 176 ? 119.083 78.208  126.216 1.00 21.98 ?  155 LYS C N     1 
ATOM   12241 C  CA    . LYS C 2 176 ? 117.708 78.686  126.376 1.00 21.79 ?  155 LYS C CA    1 
ATOM   12242 C  C     . LYS C 2 176 ? 117.661 80.209  126.542 1.00 21.70 ?  155 LYS C C     1 
ATOM   12243 O  O     . LYS C 2 176 ? 116.821 80.883  125.929 1.00 21.10 ?  155 LYS C O     1 
ATOM   12244 C  CB    . LYS C 2 176 ? 117.022 77.969  127.546 1.00 22.00 ?  155 LYS C CB    1 
ATOM   12245 C  CG    . LYS C 2 176 ? 116.799 76.480  127.314 1.00 21.93 ?  155 LYS C CG    1 
ATOM   12246 C  CD    . LYS C 2 176 ? 116.181 75.807  128.527 1.00 23.06 ?  155 LYS C CD    1 
ATOM   12247 C  CE    . LYS C 2 176 ? 115.902 74.341  128.266 1.00 24.91 ?  155 LYS C CE    1 
ATOM   12248 N  NZ    . LYS C 2 176 ? 115.607 73.605  129.541 1.00 25.16 1  155 LYS C NZ    1 
ATOM   12249 N  N     . ALA C 2 177 ? 118.567 80.745  127.366 1.00 21.49 ?  156 ALA C N     1 
ATOM   12250 C  CA    . ALA C 2 177 ? 118.688 82.192  127.519 1.00 20.60 ?  156 ALA C CA    1 
ATOM   12251 C  C     . ALA C 2 177 ? 119.145 82.905  126.227 1.00 20.37 ?  156 ALA C C     1 
ATOM   12252 O  O     . ALA C 2 177 ? 118.686 84.002  125.938 1.00 19.61 ?  156 ALA C O     1 
ATOM   12253 C  CB    . ALA C 2 177 ? 119.608 82.546  128.683 1.00 20.88 ?  156 ALA C CB    1 
ATOM   12254 N  N     . MET C 2 178 ? 120.030 82.275  125.455 1.00 20.70 ?  157 MET C N     1 
ATOM   12255 C  CA    . MET C 2 178 ? 120.473 82.843  124.170 1.00 21.06 ?  157 MET C CA    1 
ATOM   12256 C  C     . MET C 2 178 ? 119.354 82.862  123.147 1.00 20.83 ?  157 MET C C     1 
ATOM   12257 O  O     . MET C 2 178 ? 119.301 83.763  122.303 1.00 21.28 ?  157 MET C O     1 
ATOM   12258 C  CB    . MET C 2 178 ? 121.672 82.074  123.585 1.00 20.68 ?  157 MET C CB    1 
ATOM   12259 C  CG    . MET C 2 178 ? 122.989 82.214  124.345 1.00 21.61 ?  157 MET C CG    1 
ATOM   12260 S  SD    . MET C 2 178 ? 124.225 81.069  123.692 1.00 24.32 ?  157 MET C SD    1 
ATOM   12261 C  CE    . MET C 2 178 ? 125.719 81.699  124.485 1.00 23.64 ?  157 MET C CE    1 
ATOM   12262 N  N     . VAL C 2 179 ? 118.481 81.855  123.184 1.00 20.76 ?  158 VAL C N     1 
ATOM   12263 C  CA    . VAL C 2 179 ? 117.300 81.842  122.312 1.00 20.14 ?  158 VAL C CA    1 
ATOM   12264 C  C     . VAL C 2 179 ? 116.393 83.017  122.691 1.00 20.35 ?  158 VAL C C     1 
ATOM   12265 O  O     . VAL C 2 179 ? 115.905 83.750  121.827 1.00 19.82 ?  158 VAL C O     1 
ATOM   12266 C  CB    . VAL C 2 179 ? 116.502 80.515  122.425 1.00 20.07 ?  158 VAL C CB    1 
ATOM   12267 C  CG1   . VAL C 2 179 ? 115.155 80.634  121.708 1.00 20.07 ?  158 VAL C CG1   1 
ATOM   12268 C  CG2   . VAL C 2 179 ? 117.307 79.355  121.849 1.00 20.57 ?  158 VAL C CG2   1 
ATOM   12269 N  N     . ALA C 2 180 ? 116.184 83.183  123.994 1.00 19.89 ?  159 ALA C N     1 
ATOM   12270 C  CA    . ALA C 2 180 ? 115.388 84.290  124.524 1.00 20.50 ?  159 ALA C CA    1 
ATOM   12271 C  C     . ALA C 2 180 ? 115.972 85.640  124.074 1.00 20.67 ?  159 ALA C C     1 
ATOM   12272 O  O     . ALA C 2 180 ? 115.234 86.519  123.625 1.00 21.27 ?  159 ALA C O     1 
ATOM   12273 C  CB    . ALA C 2 180 ? 115.345 84.212  126.034 1.00 20.03 ?  159 ALA C CB    1 
ATOM   12274 N  N     . SER C 2 181 ? 117.292 85.786  124.186 1.00 20.78 ?  160 SER C N     1 
ATOM   12275 C  CA    . SER C 2 181 ? 117.992 86.997  123.746 1.00 21.26 ?  160 SER C CA    1 
ATOM   12276 C  C     . SER C 2 181 ? 117.848 87.243  122.236 1.00 21.19 ?  160 SER C C     1 
ATOM   12277 O  O     . SER C 2 181 ? 117.553 88.358  121.821 1.00 20.89 ?  160 SER C O     1 
ATOM   12278 C  CB    . SER C 2 181 ? 119.473 86.953  124.152 1.00 21.42 ?  160 SER C CB    1 
ATOM   12279 O  OG    . SER C 2 181 ? 120.137 88.161  123.808 1.00 23.69 ?  160 SER C OG    1 
ATOM   12280 N  N     . VAL C 2 182 ? 118.055 86.209  121.413 1.00 20.99 ?  161 VAL C N     1 
ATOM   12281 C  CA    . VAL C 2 182 ? 117.803 86.368  119.977 1.00 21.18 ?  161 VAL C CA    1 
ATOM   12282 C  C     . VAL C 2 182 ? 116.350 86.801  119.716 1.00 21.15 ?  161 VAL C C     1 
ATOM   12283 O  O     . VAL C 2 182 ? 116.103 87.704  118.899 1.00 21.18 ?  161 VAL C O     1 
ATOM   12284 C  CB    . VAL C 2 182 ? 118.167 85.091  119.154 1.00 21.11 ?  161 VAL C CB    1 
ATOM   12285 C  CG1   . VAL C 2 182 ? 117.699 85.230  117.707 1.00 21.75 ?  161 VAL C CG1   1 
ATOM   12286 C  CG2   . VAL C 2 182 ? 119.673 84.837  119.201 1.00 20.98 ?  161 VAL C CG2   1 
ATOM   12287 N  N     . TYR C 2 183 ? 115.385 86.183  120.410 1.00 21.10 ?  162 TYR C N     1 
ATOM   12288 C  CA    . TYR C 2 183 ? 113.978 86.577  120.245 1.00 21.21 ?  162 TYR C CA    1 
ATOM   12289 C  C     . TYR C 2 183 ? 113.711 88.023  120.659 1.00 21.38 ?  162 TYR C C     1 
ATOM   12290 O  O     . TYR C 2 183 ? 112.871 88.692  120.067 1.00 20.97 ?  162 TYR C O     1 
ATOM   12291 C  CB    . TYR C 2 183 ? 113.004 85.633  120.979 1.00 21.50 ?  162 TYR C CB    1 
ATOM   12292 C  CG    . TYR C 2 183 ? 112.873 84.272  120.350 1.00 22.20 ?  162 TYR C CG    1 
ATOM   12293 C  CD1   . TYR C 2 183 ? 113.222 84.063  119.017 1.00 23.80 ?  162 TYR C CD1   1 
ATOM   12294 C  CD2   . TYR C 2 183 ? 112.378 83.188  121.083 1.00 23.71 ?  162 TYR C CD2   1 
ATOM   12295 C  CE1   . TYR C 2 183 ? 113.102 82.798  118.429 1.00 25.52 ?  162 TYR C CE1   1 
ATOM   12296 C  CE2   . TYR C 2 183 ? 112.250 81.933  120.509 1.00 24.01 ?  162 TYR C CE2   1 
ATOM   12297 C  CZ    . TYR C 2 183 ? 112.621 81.740  119.189 1.00 25.47 ?  162 TYR C CZ    1 
ATOM   12298 O  OH    . TYR C 2 183 ? 112.512 80.489  118.617 1.00 25.37 ?  162 TYR C OH    1 
ATOM   12299 N  N     . LEU C 2 184 ? 114.413 88.489  121.681 1.00 22.12 ?  163 LEU C N     1 
ATOM   12300 C  CA    . LEU C 2 184 ? 114.335 89.909  122.078 1.00 23.80 ?  163 LEU C CA    1 
ATOM   12301 C  C     . LEU C 2 184 ? 114.962 90.802  120.999 1.00 24.21 ?  163 LEU C C     1 
ATOM   12302 O  O     . LEU C 2 184 ? 114.363 91.782  120.608 1.00 24.72 ?  163 LEU C O     1 
ATOM   12303 C  CB    . LEU C 2 184 ? 115.005 90.138  123.437 1.00 23.52 ?  163 LEU C CB    1 
ATOM   12304 C  CG    . LEU C 2 184 ? 114.961 91.529  124.101 1.00 24.91 ?  163 LEU C CG    1 
ATOM   12305 C  CD1   . LEU C 2 184 ? 114.906 91.374  125.600 1.00 24.81 ?  163 LEU C CD1   1 
ATOM   12306 C  CD2   . LEU C 2 184 ? 116.138 92.431  123.702 1.00 26.39 ?  163 LEU C CD2   1 
ATOM   12307 N  N     . GLU C 2 185 ? 116.157 90.440  120.512 1.00 25.17 ?  164 GLU C N     1 
ATOM   12308 C  CA    . GLU C 2 185 ? 116.899 91.273  119.553 1.00 25.30 ?  164 GLU C CA    1 
ATOM   12309 C  C     . GLU C 2 185 ? 116.219 91.377  118.177 1.00 25.07 ?  164 GLU C C     1 
ATOM   12310 O  O     . GLU C 2 185 ? 116.149 92.461  117.574 1.00 24.49 ?  164 GLU C O     1 
ATOM   12311 C  CB    . GLU C 2 185 ? 118.332 90.730  119.342 1.00 26.17 ?  164 GLU C CB    1 
ATOM   12312 C  CG    . GLU C 2 185 ? 119.252 90.808  120.580 1.00 27.05 ?  164 GLU C CG    1 
ATOM   12313 C  CD    . GLU C 2 185 ? 119.802 92.215  120.839 1.00 29.23 ?  164 GLU C CD    1 
ATOM   12314 O  OE1   . GLU C 2 185 ? 119.480 93.172  120.077 1.00 28.79 ?  164 GLU C OE1   1 
ATOM   12315 O  OE2   . GLU C 2 185 ? 120.598 92.376  121.793 1.00 28.65 -1 164 GLU C OE2   1 
ATOM   12316 N  N     . SER C 2 186 ? 115.749 90.235  117.692 1.00 24.23 ?  165 SER C N     1 
ATOM   12317 C  CA    . SER C 2 186 ? 115.409 90.054  116.286 1.00 24.71 ?  165 SER C CA    1 
ATOM   12318 C  C     . SER C 2 186 ? 113.913 89.904  116.031 1.00 24.51 ?  165 SER C C     1 
ATOM   12319 O  O     . SER C 2 186 ? 113.485 89.899  114.879 1.00 24.87 ?  165 SER C O     1 
ATOM   12320 C  CB    . SER C 2 186 ? 116.139 88.823  115.733 1.00 25.06 ?  165 SER C CB    1 
ATOM   12321 O  OG    . SER C 2 186 ? 117.543 88.945  115.875 1.00 26.29 ?  165 SER C OG    1 
ATOM   12322 N  N     . PHE C 2 187 ? 113.131 89.766  117.099 1.00 24.71 ?  166 PHE C N     1 
ATOM   12323 C  CA    . PHE C 2 187 ? 111.681 89.609  116.995 1.00 25.69 ?  166 PHE C CA    1 
ATOM   12324 C  C     . PHE C 2 187 ? 110.918 90.648  117.833 1.00 25.87 ?  166 PHE C C     1 
ATOM   12325 O  O     . PHE C 2 187 ? 110.164 91.442  117.269 1.00 26.03 ?  166 PHE C O     1 
ATOM   12326 C  CB    . PHE C 2 187 ? 111.249 88.177  117.367 1.00 25.54 ?  166 PHE C CB    1 
ATOM   12327 C  CG    . PHE C 2 187 ? 109.754 88.005  117.543 1.00 26.64 ?  166 PHE C CG    1 
ATOM   12328 C  CD1   . PHE C 2 187 ? 108.872 88.241  116.481 1.00 25.90 ?  166 PHE C CD1   1 
ATOM   12329 C  CD2   . PHE C 2 187 ? 109.229 87.594  118.772 1.00 27.45 ?  166 PHE C CD2   1 
ATOM   12330 C  CE1   . PHE C 2 187 ? 107.482 88.085  116.644 1.00 25.64 ?  166 PHE C CE1   1 
ATOM   12331 C  CE2   . PHE C 2 187 ? 107.834 87.430  118.949 1.00 26.52 ?  166 PHE C CE2   1 
ATOM   12332 C  CZ    . PHE C 2 187 ? 106.966 87.675  117.882 1.00 27.18 ?  166 PHE C CZ    1 
ATOM   12333 N  N     . LEU C 2 188 ? 111.132 90.642  119.151 1.00 26.13 ?  167 LEU C N     1 
ATOM   12334 C  CA    . LEU C 2 188 ? 110.340 91.464  120.103 1.00 27.13 ?  167 LEU C CA    1 
ATOM   12335 C  C     . LEU C 2 188 ? 110.456 92.991  119.939 1.00 27.22 ?  167 LEU C C     1 
ATOM   12336 O  O     . LEU C 2 188 ? 109.502 93.723  120.238 1.00 28.03 ?  167 LEU C O     1 
ATOM   12337 C  CB    . LEU C 2 188 ? 110.679 91.105  121.559 1.00 26.89 ?  167 LEU C CB    1 
ATOM   12338 C  CG    . LEU C 2 188 ? 110.355 89.730  122.164 1.00 28.64 ?  167 LEU C CG    1 
ATOM   12339 C  CD1   . LEU C 2 188 ? 110.849 89.660  123.607 1.00 28.34 ?  167 LEU C CD1   1 
ATOM   12340 C  CD2   . LEU C 2 188 ? 108.872 89.404  122.106 1.00 27.90 ?  167 LEU C CD2   1 
ATOM   12341 N  N     . PHE C 2 189 ? 111.620 93.470  119.515 1.00 26.79 ?  168 PHE C N     1 
ATOM   12342 C  CA    . PHE C 2 189 ? 111.811 94.903  119.303 1.00 26.90 ?  168 PHE C CA    1 
ATOM   12343 C  C     . PHE C 2 189 ? 110.931 95.419  118.158 1.00 26.52 ?  168 PHE C C     1 
ATOM   12344 O  O     . PHE C 2 189 ? 110.655 96.623  118.070 1.00 26.02 ?  168 PHE C O     1 
ATOM   12345 C  CB    . PHE C 2 189 ? 113.280 95.231  118.968 1.00 27.03 ?  168 PHE C CB    1 
ATOM   12346 C  CG    . PHE C 2 189 ? 114.183 95.444  120.181 1.00 28.09 ?  168 PHE C CG    1 
ATOM   12347 C  CD1   . PHE C 2 189 ? 113.876 96.393  121.158 1.00 28.69 ?  168 PHE C CD1   1 
ATOM   12348 C  CD2   . PHE C 2 189 ? 115.378 94.745  120.297 1.00 29.15 ?  168 PHE C CD2   1 
ATOM   12349 C  CE1   . PHE C 2 189 ? 114.718 96.604  122.261 1.00 28.50 ?  168 PHE C CE1   1 
ATOM   12350 C  CE2   . PHE C 2 189 ? 116.234 94.944  121.396 1.00 30.19 ?  168 PHE C CE2   1 
ATOM   12351 C  CZ    . PHE C 2 189 ? 115.895 95.884  122.386 1.00 29.81 ?  168 PHE C CZ    1 
ATOM   12352 N  N     . TYR C 2 190 ? 110.509 94.520  117.269 1.00 26.18 ?  169 TYR C N     1 
ATOM   12353 C  CA    . TYR C 2 190 ? 109.984 94.968  115.984 1.00 26.24 ?  169 TYR C CA    1 
ATOM   12354 C  C     . TYR C 2 190 ? 108.549 95.516  115.982 1.00 25.94 ?  169 TYR C C     1 
ATOM   12355 O  O     . TYR C 2 190 ? 108.190 96.322  115.123 1.00 25.71 ?  169 TYR C O     1 
ATOM   12356 C  CB    . TYR C 2 190 ? 110.282 93.938  114.893 1.00 27.13 ?  169 TYR C CB    1 
ATOM   12357 C  CG    . TYR C 2 190 ? 111.740 94.030  114.496 1.00 28.07 ?  169 TYR C CG    1 
ATOM   12358 C  CD1   . TYR C 2 190 ? 112.728 93.354  115.223 1.00 29.54 ?  169 TYR C CD1   1 
ATOM   12359 C  CD2   . TYR C 2 190 ? 112.143 94.848  113.441 1.00 29.31 ?  169 TYR C CD2   1 
ATOM   12360 C  CE1   . TYR C 2 190 ? 114.078 93.463  114.879 1.00 30.44 ?  169 TYR C CE1   1 
ATOM   12361 C  CE2   . TYR C 2 190 ? 113.496 94.963  113.087 1.00 30.64 ?  169 TYR C CE2   1 
ATOM   12362 C  CZ    . TYR C 2 190 ? 114.455 94.271  113.814 1.00 30.40 ?  169 TYR C CZ    1 
ATOM   12363 O  OH    . TYR C 2 190 ? 115.785 94.388  113.477 1.00 28.85 ?  169 TYR C OH    1 
ATOM   12364 N  N     . SER C 2 191 ? 107.757 95.125  116.977 1.00 25.17 ?  170 SER C N     1 
ATOM   12365 C  CA    . SER C 2 191 ? 106.431 95.707  117.166 1.00 25.10 ?  170 SER C CA    1 
ATOM   12366 C  C     . SER C 2 191 ? 106.590 97.191  117.518 1.00 25.16 ?  170 SER C C     1 
ATOM   12367 O  O     . SER C 2 191 ? 105.722 98.008  117.195 1.00 25.30 ?  170 SER C O     1 
ATOM   12368 C  CB    . SER C 2 191 ? 105.654 94.960  118.251 1.00 24.56 ?  170 SER C CB    1 
ATOM   12369 O  OG    . SER C 2 191 ? 106.274 95.098  119.515 1.00 24.98 ?  170 SER C OG    1 
ATOM   12370 N  N     . GLY C 2 192 ? 107.715 97.508  118.171 1.00 24.32 ?  171 GLY C N     1 
ATOM   12371 C  CA    . GLY C 2 192 ? 108.108 98.870  118.508 1.00 23.97 ?  171 GLY C CA    1 
ATOM   12372 C  C     . GLY C 2 192 ? 108.755 99.620  117.356 1.00 23.85 ?  171 GLY C C     1 
ATOM   12373 O  O     . GLY C 2 192 ? 108.334 100.736 117.049 1.00 23.99 ?  171 GLY C O     1 
ATOM   12374 N  N     . PHE C 2 193 ? 109.752 99.011  116.711 1.00 23.28 ?  172 PHE C N     1 
ATOM   12375 C  CA    . PHE C 2 193 ? 110.460 99.636  115.578 1.00 23.85 ?  172 PHE C CA    1 
ATOM   12376 C  C     . PHE C 2 193 ? 109.554 100.035 114.413 1.00 23.72 ?  172 PHE C C     1 
ATOM   12377 O  O     . PHE C 2 193 ? 109.876 100.966 113.677 1.00 23.92 ?  172 PHE C O     1 
ATOM   12378 C  CB    . PHE C 2 193 ? 111.558 98.726  115.014 1.00 23.47 ?  172 PHE C CB    1 
ATOM   12379 C  CG    . PHE C 2 193 ? 112.789 98.615  115.885 1.00 24.32 ?  172 PHE C CG    1 
ATOM   12380 C  CD1   . PHE C 2 193 ? 113.122 99.614  116.801 1.00 22.28 ?  172 PHE C CD1   1 
ATOM   12381 C  CD2   . PHE C 2 193 ? 113.634 97.510  115.762 1.00 23.82 ?  172 PHE C CD2   1 
ATOM   12382 C  CE1   . PHE C 2 193 ? 114.263 99.509  117.606 1.00 23.41 ?  172 PHE C CE1   1 
ATOM   12383 C  CE2   . PHE C 2 193 ? 114.785 97.387  116.559 1.00 24.70 ?  172 PHE C CE2   1 
ATOM   12384 C  CZ    . PHE C 2 193 ? 115.103 98.395  117.483 1.00 24.87 ?  172 PHE C CZ    1 
ATOM   12385 N  N     . TYR C 2 194 ? 108.446 99.313  114.229 1.00 23.31 ?  173 TYR C N     1 
ATOM   12386 C  CA    . TYR C 2 194 ? 107.553 99.547  113.091 1.00 23.26 ?  173 TYR C CA    1 
ATOM   12387 C  C     . TYR C 2 194 ? 107.193 101.027 112.942 1.00 23.04 ?  173 TYR C C     1 
ATOM   12388 O  O     . TYR C 2 194 ? 107.257 101.584 111.843 1.00 23.47 ?  173 TYR C O     1 
ATOM   12389 C  CB    . TYR C 2 194 ? 106.261 98.716  113.197 1.00 23.13 ?  173 TYR C CB    1 
ATOM   12390 C  CG    . TYR C 2 194 ? 105.357 98.853  111.979 1.00 24.10 ?  173 TYR C CG    1 
ATOM   12391 C  CD1   . TYR C 2 194 ? 105.431 97.934  110.930 1.00 25.72 ?  173 TYR C CD1   1 
ATOM   12392 C  CD2   . TYR C 2 194 ? 104.451 99.909  111.865 1.00 27.04 ?  173 TYR C CD2   1 
ATOM   12393 C  CE1   . TYR C 2 194 ? 104.606 98.053  109.803 1.00 28.94 ?  173 TYR C CE1   1 
ATOM   12394 C  CE2   . TYR C 2 194 ? 103.627 100.044 110.732 1.00 27.84 ?  173 TYR C CE2   1 
ATOM   12395 C  CZ    . TYR C 2 194 ? 103.716 99.110  109.712 1.00 29.97 ?  173 TYR C CZ    1 
ATOM   12396 O  OH    . TYR C 2 194 ? 102.921 99.229  108.585 1.00 34.34 ?  173 TYR C OH    1 
ATOM   12397 N  N     . TYR C 2 195 ? 106.810 101.650 114.047 1.00 22.51 ?  174 TYR C N     1 
ATOM   12398 C  CA    . TYR C 2 195 ? 106.183 102.966 113.992 1.00 22.60 ?  174 TYR C CA    1 
ATOM   12399 C  C     . TYR C 2 195 ? 107.168 104.103 113.660 1.00 22.64 ?  174 TYR C C     1 
ATOM   12400 O  O     . TYR C 2 195 ? 106.866 104.914 112.778 1.00 22.39 ?  174 TYR C O     1 
ATOM   12401 C  CB    . TYR C 2 195 ? 105.378 103.227 115.265 1.00 22.32 ?  174 TYR C CB    1 
ATOM   12402 C  CG    . TYR C 2 195 ? 104.165 104.118 115.080 1.00 23.39 ?  174 TYR C CG    1 
ATOM   12403 C  CD1   . TYR C 2 195 ? 103.433 104.117 113.883 1.00 22.84 ?  174 TYR C CD1   1 
ATOM   12404 C  CD2   . TYR C 2 195 ? 103.728 104.933 116.122 1.00 22.23 ?  174 TYR C CD2   1 
ATOM   12405 C  CE1   . TYR C 2 195 ? 102.307 104.936 113.727 1.00 24.05 ?  174 TYR C CE1   1 
ATOM   12406 C  CE2   . TYR C 2 195 ? 102.598 105.742 115.983 1.00 24.11 ?  174 TYR C CE2   1 
ATOM   12407 C  CZ    . TYR C 2 195 ? 101.896 105.736 114.789 1.00 23.92 ?  174 TYR C CZ    1 
ATOM   12408 O  OH    . TYR C 2 195 ? 100.805 106.553 114.661 1.00 25.00 ?  174 TYR C OH    1 
ATOM   12409 N  N     . PRO C 2 196 ? 108.350 104.155 114.343 1.00 22.25 ?  175 PRO C N     1 
ATOM   12410 C  CA    . PRO C 2 196 ? 109.367 105.125 113.905 1.00 22.45 ?  175 PRO C CA    1 
ATOM   12411 C  C     . PRO C 2 196 ? 109.779 104.937 112.444 1.00 22.59 ?  175 PRO C C     1 
ATOM   12412 O  O     . PRO C 2 196 ? 109.997 105.933 111.745 1.00 22.19 ?  175 PRO C O     1 
ATOM   12413 C  CB    . PRO C 2 196 ? 110.563 104.854 114.830 1.00 22.25 ?  175 PRO C CB    1 
ATOM   12414 C  CG    . PRO C 2 196 ? 110.000 104.159 116.026 1.00 22.22 ?  175 PRO C CG    1 
ATOM   12415 C  CD    . PRO C 2 196 ? 108.780 103.411 115.549 1.00 22.32 ?  175 PRO C CD    1 
ATOM   12416 N  N     . LEU C 2 197 ? 109.873 103.684 111.990 1.00 21.92 ?  176 LEU C N     1 
ATOM   12417 C  CA    . LEU C 2 197 ? 110.216 103.400 110.594 1.00 22.35 ?  176 LEU C CA    1 
ATOM   12418 C  C     . LEU C 2 197 ? 109.101 103.848 109.643 1.00 22.60 ?  176 LEU C C     1 
ATOM   12419 O  O     . LEU C 2 197 ? 109.365 104.367 108.555 1.00 22.41 ?  176 LEU C O     1 
ATOM   12420 C  CB    . LEU C 2 197 ? 110.498 101.914 110.380 1.00 22.69 ?  176 LEU C CB    1 
ATOM   12421 C  CG    . LEU C 2 197 ? 111.693 101.241 111.069 1.00 23.68 ?  176 LEU C CG    1 
ATOM   12422 C  CD1   . LEU C 2 197 ? 111.721 99.748  110.705 1.00 23.70 ?  176 LEU C CD1   1 
ATOM   12423 C  CD2   . LEU C 2 197 ? 113.004 101.915 110.679 1.00 23.09 ?  176 LEU C CD2   1 
ATOM   12424 N  N     . TYR C 2 198 ? 107.858 103.640 110.070 1.00 22.64 ?  177 TYR C N     1 
ATOM   12425 C  CA    . TYR C 2 198 ? 106.684 104.009 109.291 1.00 22.92 ?  177 TYR C CA    1 
ATOM   12426 C  C     . TYR C 2 198 ? 106.669 105.532 109.064 1.00 23.68 ?  177 TYR C C     1 
ATOM   12427 O  O     . TYR C 2 198 ? 106.412 106.003 107.954 1.00 23.81 ?  177 TYR C O     1 
ATOM   12428 C  CB    . TYR C 2 198 ? 105.442 103.523 110.032 1.00 22.73 ?  177 TYR C CB    1 
ATOM   12429 C  CG    . TYR C 2 198 ? 104.105 103.843 109.420 1.00 22.91 ?  177 TYR C CG    1 
ATOM   12430 C  CD1   . TYR C 2 198 ? 103.646 103.147 108.301 1.00 23.49 ?  177 TYR C CD1   1 
ATOM   12431 C  CD2   . TYR C 2 198 ? 103.268 104.796 110.001 1.00 21.97 ?  177 TYR C CD2   1 
ATOM   12432 C  CE1   . TYR C 2 198 ? 102.394 103.417 107.747 1.00 23.57 ?  177 TYR C CE1   1 
ATOM   12433 C  CE2   . TYR C 2 198 ? 102.002 105.074 109.456 1.00 22.54 ?  177 TYR C CE2   1 
ATOM   12434 C  CZ    . TYR C 2 198 ? 101.580 104.383 108.330 1.00 22.88 ?  177 TYR C CZ    1 
ATOM   12435 O  OH    . TYR C 2 198 ? 100.335 104.633 107.782 1.00 23.17 ?  177 TYR C OH    1 
ATOM   12436 N  N     . PHE C 2 199 ? 106.992 106.295 110.102 1.00 23.50 ?  178 PHE C N     1 
ATOM   12437 C  CA    . PHE C 2 199 ? 107.101 107.748 109.959 1.00 24.60 ?  178 PHE C CA    1 
ATOM   12438 C  C     . PHE C 2 199 ? 108.314 108.212 109.141 1.00 24.72 ?  178 PHE C C     1 
ATOM   12439 O  O     . PHE C 2 199 ? 108.187 109.063 108.262 1.00 24.19 ?  178 PHE C O     1 
ATOM   12440 C  CB    . PHE C 2 199 ? 107.069 108.432 111.328 1.00 24.35 ?  178 PHE C CB    1 
ATOM   12441 C  CG    . PHE C 2 199 ? 105.700 108.485 111.937 1.00 26.36 ?  178 PHE C CG    1 
ATOM   12442 C  CD1   . PHE C 2 199 ? 104.596 108.867 111.175 1.00 28.53 ?  178 PHE C CD1   1 
ATOM   12443 C  CD2   . PHE C 2 199 ? 105.507 108.172 113.275 1.00 28.23 ?  178 PHE C CD2   1 
ATOM   12444 C  CE1   . PHE C 2 199 ? 103.317 108.913 111.738 1.00 29.37 ?  178 PHE C CE1   1 
ATOM   12445 C  CE2   . PHE C 2 199 ? 104.225 108.229 113.848 1.00 28.69 ?  178 PHE C CE2   1 
ATOM   12446 C  CZ    . PHE C 2 199 ? 103.139 108.596 113.081 1.00 28.43 ?  178 PHE C CZ    1 
ATOM   12447 N  N     . TYR C 2 200 ? 109.480 107.641 109.436 1.00 25.36 ?  179 TYR C N     1 
ATOM   12448 C  CA    . TYR C 2 200 ? 110.718 107.938 108.705 1.00 26.02 ?  179 TYR C CA    1 
ATOM   12449 C  C     . TYR C 2 200 ? 110.489 107.791 107.200 1.00 26.57 ?  179 TYR C C     1 
ATOM   12450 O  O     . TYR C 2 200 ? 110.892 108.649 106.408 1.00 26.30 ?  179 TYR C O     1 
ATOM   12451 C  CB    . TYR C 2 200 ? 111.835 106.986 109.154 1.00 26.19 ?  179 TYR C CB    1 
ATOM   12452 C  CG    . TYR C 2 200 ? 113.211 107.334 108.630 1.00 27.82 ?  179 TYR C CG    1 
ATOM   12453 C  CD1   . TYR C 2 200 ? 113.759 106.644 107.544 1.00 30.77 ?  179 TYR C CD1   1 
ATOM   12454 C  CD2   . TYR C 2 200 ? 113.971 108.345 109.223 1.00 29.20 ?  179 TYR C CD2   1 
ATOM   12455 C  CE1   . TYR C 2 200 ? 115.023 106.957 107.059 1.00 31.82 ?  179 TYR C CE1   1 
ATOM   12456 C  CE2   . TYR C 2 200 ? 115.234 108.668 108.748 1.00 30.44 ?  179 TYR C CE2   1 
ATOM   12457 C  CZ    . TYR C 2 200 ? 115.754 107.968 107.664 1.00 32.74 ?  179 TYR C CZ    1 
ATOM   12458 O  OH    . TYR C 2 200 ? 116.999 108.278 107.174 1.00 34.58 ?  179 TYR C OH    1 
ATOM   12459 N  N     . GLY C 2 201 ? 109.814 106.707 106.825 1.00 26.71 ?  180 GLY C N     1 
ATOM   12460 C  CA    . GLY C 2 201 ? 109.519 106.412 105.430 1.00 27.38 ?  180 GLY C CA    1 
ATOM   12461 C  C     . GLY C 2 201 ? 108.592 107.406 104.748 1.00 27.62 ?  180 GLY C C     1 
ATOM   12462 O  O     . GLY C 2 201 ? 108.547 107.449 103.530 1.00 28.25 ?  180 GLY C O     1 
ATOM   12463 N  N     . GLN C 2 202 ? 107.862 108.198 105.533 1.00 27.60 ?  181 GLN C N     1 
ATOM   12464 C  CA    . GLN C 2 202 ? 106.975 109.250 105.005 1.00 28.24 ?  181 GLN C CA    1 
ATOM   12465 C  C     . GLN C 2 202 ? 107.606 110.629 105.125 1.00 28.30 ?  181 GLN C C     1 
ATOM   12466 O  O     . GLN C 2 202 ? 106.945 111.633 104.849 1.00 27.98 ?  181 GLN C O     1 
ATOM   12467 C  CB    . GLN C 2 202 ? 105.658 109.302 105.784 1.00 27.90 ?  181 GLN C CB    1 
ATOM   12468 C  CG    . GLN C 2 202 ? 104.817 108.068 105.736 1.00 29.54 ?  181 GLN C CG    1 
ATOM   12469 C  CD    . GLN C 2 202 ? 103.608 108.185 106.637 1.00 31.54 ?  181 GLN C CD    1 
ATOM   12470 O  OE1   . GLN C 2 202 ? 102.684 108.956 106.361 1.00 32.11 ?  181 GLN C OE1   1 
ATOM   12471 N  NE2   . GLN C 2 202 ? 103.608 107.429 107.726 1.00 31.29 ?  181 GLN C NE2   1 
ATOM   12472 N  N     . GLY C 2 203 ? 108.857 110.674 105.582 1.00 28.14 ?  182 GLY C N     1 
ATOM   12473 C  CA    . GLY C 2 203 ? 109.568 111.925 105.791 1.00 28.38 ?  182 GLY C CA    1 
ATOM   12474 C  C     . GLY C 2 203 ? 109.132 112.654 107.045 1.00 28.71 ?  182 GLY C C     1 
ATOM   12475 O  O     . GLY C 2 203 ? 109.174 113.879 107.094 1.00 28.80 ?  182 GLY C O     1 
ATOM   12476 N  N     . LYS C 2 204 ? 108.697 111.895 108.051 1.00 28.24 ?  183 LYS C N     1 
ATOM   12477 C  CA    . LYS C 2 204 ? 108.232 112.465 109.305 1.00 28.48 ?  183 LYS C CA    1 
ATOM   12478 C  C     . LYS C 2 204 ? 109.061 111.932 110.470 1.00 27.82 ?  183 LYS C C     1 
ATOM   12479 O  O     . LYS C 2 204 ? 109.463 110.760 110.475 1.00 26.73 ?  183 LYS C O     1 
ATOM   12480 C  CB    . LYS C 2 204 ? 106.751 112.155 109.529 1.00 29.13 ?  183 LYS C CB    1 
ATOM   12481 C  CG    . LYS C 2 204 ? 105.814 112.811 108.514 1.00 30.41 ?  183 LYS C CG    1 
ATOM   12482 C  CD    . LYS C 2 204 ? 104.494 112.058 108.428 1.00 33.74 ?  183 LYS C CD    1 
ATOM   12483 C  CE    . LYS C 2 204 ? 103.520 112.760 107.468 1.00 36.26 ?  183 LYS C CE    1 
ATOM   12484 N  NZ    . LYS C 2 204 ? 102.220 112.031 107.417 1.00 39.17 1  183 LYS C NZ    1 
ATOM   12485 N  N     . LEU C 2 205 ? 109.307 112.801 111.449 1.00 27.77 ?  184 LEU C N     1 
ATOM   12486 C  CA    . LEU C 2 205 ? 110.111 112.465 112.630 1.00 27.79 ?  184 LEU C CA    1 
ATOM   12487 C  C     . LEU C 2 205 ? 111.448 111.831 112.236 1.00 27.85 ?  184 LEU C C     1 
ATOM   12488 O  O     . LEU C 2 205 ? 111.842 110.767 112.735 1.00 27.07 ?  184 LEU C O     1 
ATOM   12489 C  CB    . LEU C 2 205 ? 109.317 111.559 113.594 1.00 27.76 ?  184 LEU C CB    1 
ATOM   12490 C  CG    . LEU C 2 205 ? 107.968 112.113 114.070 1.00 28.62 ?  184 LEU C CG    1 
ATOM   12491 C  CD1   . LEU C 2 205 ? 107.223 111.089 114.902 1.00 29.18 ?  184 LEU C CD1   1 
ATOM   12492 C  CD2   . LEU C 2 205 ? 108.147 113.403 114.858 1.00 28.43 ?  184 LEU C CD2   1 
ATOM   12493 N  N     . MET C 2 206 ? 112.160 112.502 111.343 1.00 28.15 ?  185 MET C N     1 
ATOM   12494 C  CA    . MET C 2 206 ? 113.319 111.888 110.737 1.00 28.80 ?  185 MET C CA    1 
ATOM   12495 C  C     . MET C 2 206 ? 114.568 111.873 111.607 1.00 28.77 ?  185 MET C C     1 
ATOM   12496 O  O     . MET C 2 206 ? 115.432 111.020 111.415 1.00 28.79 ?  185 MET C O     1 
ATOM   12497 C  CB    . MET C 2 206 ? 113.570 112.495 109.369 1.00 29.96 ?  185 MET C CB    1 
ATOM   12498 C  CG    . MET C 2 206 ? 112.454 112.129 108.386 1.00 31.23 ?  185 MET C CG    1 
ATOM   12499 S  SD    . MET C 2 206 ? 112.994 112.381 106.717 1.00 40.10 ?  185 MET C SD    1 
ATOM   12500 C  CE    . MET C 2 206 ? 114.136 111.032 106.491 1.00 35.10 ?  185 MET C CE    1 
ATOM   12501 N  N     . GLN C 2 207 ? 114.655 112.783 112.572 1.00 28.62 ?  186 GLN C N     1 
ATOM   12502 C  CA    . GLN C 2 207 ? 115.798 112.799 113.491 1.00 29.10 ?  186 GLN C CA    1 
ATOM   12503 C  C     . GLN C 2 207 ? 115.685 111.668 114.517 1.00 28.52 ?  186 GLN C C     1 
ATOM   12504 O  O     . GLN C 2 207 ? 116.643 110.924 114.716 1.00 28.28 ?  186 GLN C O     1 
ATOM   12505 C  CB    . GLN C 2 207 ? 115.959 114.159 114.179 1.00 29.21 ?  186 GLN C CB    1 
ATOM   12506 C  CG    . GLN C 2 207 ? 116.270 115.310 113.221 1.00 31.41 ?  186 GLN C CG    1 
ATOM   12507 C  CD    . GLN C 2 207 ? 117.610 115.149 112.534 1.00 34.70 ?  186 GLN C CD    1 
ATOM   12508 O  OE1   . GLN C 2 207 ? 117.696 114.582 111.449 1.00 37.69 ?  186 GLN C OE1   1 
ATOM   12509 N  NE2   . GLN C 2 207 ? 118.671 115.621 113.179 1.00 34.75 ?  186 GLN C NE2   1 
ATOM   12510 N  N     . SER C 2 208 ? 114.511 111.548 115.150 1.00 28.38 ?  187 SER C N     1 
ATOM   12511 C  CA    . SER C 2 208 ? 114.177 110.400 116.002 1.00 28.25 ?  187 SER C CA    1 
ATOM   12512 C  C     . SER C 2 208 ? 114.356 109.107 115.215 1.00 28.00 ?  187 SER C C     1 
ATOM   12513 O  O     . SER C 2 208 ? 114.883 108.125 115.740 1.00 27.90 ?  187 SER C O     1 
ATOM   12514 C  CB    . SER C 2 208 ? 112.722 110.473 116.471 1.00 27.88 ?  187 SER C CB    1 
ATOM   12515 O  OG    . SER C 2 208 ? 112.482 111.624 117.253 1.00 30.27 ?  187 SER C OG    1 
ATOM   12516 N  N     . GLY C 2 209 ? 113.898 109.122 113.959 1.00 27.31 ?  188 GLY C N     1 
ATOM   12517 C  CA    . GLY C 2 209 ? 114.012 107.976 113.060 1.00 27.86 ?  188 GLY C CA    1 
ATOM   12518 C  C     . GLY C 2 209 ? 115.446 107.574 112.773 1.00 27.96 ?  188 GLY C C     1 
ATOM   12519 O  O     . GLY C 2 209 ? 115.747 106.383 112.633 1.00 27.84 ?  188 GLY C O     1 
ATOM   12520 N  N     . GLU C 2 210 ? 116.332 108.567 112.681 1.00 28.21 ?  189 GLU C N     1 
ATOM   12521 C  CA    . GLU C 2 210 ? 117.757 108.317 112.491 1.00 29.15 ?  189 GLU C CA    1 
ATOM   12522 C  C     . GLU C 2 210 ? 118.348 107.568 113.702 1.00 28.02 ?  189 GLU C C     1 
ATOM   12523 O  O     . GLU C 2 210 ? 119.125 106.622 113.549 1.00 27.15 ?  189 GLU C O     1 
ATOM   12524 C  CB    . GLU C 2 210 ? 118.495 109.638 112.253 1.00 30.17 ?  189 GLU C CB    1 
ATOM   12525 C  CG    . GLU C 2 210 ? 119.407 109.635 111.036 1.00 35.68 ?  189 GLU C CG    1 
ATOM   12526 C  CD    . GLU C 2 210 ? 118.645 109.810 109.719 1.00 40.25 ?  189 GLU C CD    1 
ATOM   12527 O  OE1   . GLU C 2 210 ? 117.994 110.862 109.510 1.00 42.98 ?  189 GLU C OE1   1 
ATOM   12528 O  OE2   . GLU C 2 210 ? 118.706 108.893 108.878 1.00 43.59 -1 189 GLU C OE2   1 
ATOM   12529 N  N     . ILE C 2 211 ? 117.972 107.997 114.905 1.00 27.57 ?  190 ILE C N     1 
ATOM   12530 C  CA    . ILE C 2 211 ? 118.364 107.297 116.133 1.00 27.47 ?  190 ILE C CA    1 
ATOM   12531 C  C     . ILE C 2 211 ? 117.898 105.838 116.116 1.00 26.69 ?  190 ILE C C     1 
ATOM   12532 O  O     . ILE C 2 211 ? 118.682 104.909 116.348 1.00 26.56 ?  190 ILE C O     1 
ATOM   12533 C  CB    . ILE C 2 211 ? 117.845 108.044 117.398 1.00 27.84 ?  190 ILE C CB    1 
ATOM   12534 C  CG1   . ILE C 2 211 ? 118.631 109.351 117.587 1.00 28.56 ?  190 ILE C CG1   1 
ATOM   12535 C  CG2   . ILE C 2 211 ? 117.930 107.133 118.644 1.00 27.27 ?  190 ILE C CG2   1 
ATOM   12536 C  CD1   . ILE C 2 211 ? 118.246 110.147 118.829 1.00 30.09 ?  190 ILE C CD1   1 
ATOM   12537 N  N     . ILE C 2 212 ? 116.623 105.642 115.800 1.00 26.33 ?  191 ILE C N     1 
ATOM   12538 C  CA    . ILE C 2 212 ? 116.024 104.312 115.754 1.00 25.96 ?  191 ILE C CA    1 
ATOM   12539 C  C     . ILE C 2 212 ? 116.722 103.396 114.739 1.00 25.46 ?  191 ILE C C     1 
ATOM   12540 O  O     . ILE C 2 212 ? 116.941 102.222 115.028 1.00 24.84 ?  191 ILE C O     1 
ATOM   12541 C  CB    . ILE C 2 212 ? 114.487 104.391 115.499 1.00 26.00 ?  191 ILE C CB    1 
ATOM   12542 C  CG1   . ILE C 2 212 ? 113.779 105.073 116.681 1.00 27.16 ?  191 ILE C CG1   1 
ATOM   12543 C  CG2   . ILE C 2 212 ? 113.883 103.018 115.237 1.00 26.87 ?  191 ILE C CG2   1 
ATOM   12544 C  CD1   . ILE C 2 212 ? 113.873 104.331 118.001 1.00 29.84 ?  191 ILE C CD1   1 
ATOM   12545 N  N     . ASN C 2 213 ? 117.070 103.930 113.566 1.00 25.35 ?  192 ASN C N     1 
ATOM   12546 C  CA    . ASN C 2 213 ? 117.807 103.163 112.556 1.00 25.60 ?  192 ASN C CA    1 
ATOM   12547 C  C     . ASN C 2 213 ? 119.185 102.725 113.042 1.00 25.14 ?  192 ASN C C     1 
ATOM   12548 O  O     . ASN C 2 213 ? 119.650 101.619 112.727 1.00 25.61 ?  192 ASN C O     1 
ATOM   12549 C  CB    . ASN C 2 213 ? 117.945 103.945 111.243 1.00 26.55 ?  192 ASN C CB    1 
ATOM   12550 C  CG    . ASN C 2 213 ? 116.760 103.749 110.324 1.00 28.10 ?  192 ASN C CG    1 
ATOM   12551 O  OD1   . ASN C 2 213 ? 116.485 102.636 109.865 1.00 31.67 ?  192 ASN C OD1   1 
ATOM   12552 N  ND2   . ASN C 2 213 ? 116.057 104.830 110.039 1.00 30.36 ?  192 ASN C ND2   1 
ATOM   12553 N  N     . LEU C 2 214 ? 119.837 103.588 113.811 1.00 24.54 ?  193 LEU C N     1 
ATOM   12554 C  CA    . LEU C 2 214 ? 121.124 103.232 114.415 1.00 24.40 ?  193 LEU C CA    1 
ATOM   12555 C  C     . LEU C 2 214 ? 120.956 102.118 115.450 1.00 23.55 ?  193 LEU C C     1 
ATOM   12556 O  O     . LEU C 2 214 ? 121.735 101.160 115.463 1.00 23.09 ?  193 LEU C O     1 
ATOM   12557 C  CB    . LEU C 2 214 ? 121.815 104.461 115.000 1.00 24.00 ?  193 LEU C CB    1 
ATOM   12558 C  CG    . LEU C 2 214 ? 122.385 105.459 113.968 1.00 25.69 ?  193 LEU C CG    1 
ATOM   12559 C  CD1   . LEU C 2 214 ? 122.789 106.779 114.625 1.00 26.28 ?  193 LEU C CD1   1 
ATOM   12560 C  CD2   . LEU C 2 214 ? 123.579 104.876 113.210 1.00 26.05 ?  193 LEU C CD2   1 
ATOM   12561 N  N     . ILE C 2 215 ? 119.934 102.239 116.300 1.00 23.19 ?  194 ILE C N     1 
ATOM   12562 C  CA    . ILE C 2 215 ? 119.581 101.183 117.256 1.00 22.88 ?  194 ILE C CA    1 
ATOM   12563 C  C     . ILE C 2 215 ? 119.302 99.874  116.500 1.00 23.81 ?  194 ILE C C     1 
ATOM   12564 O  O     . ILE C 2 215 ? 119.834 98.822  116.858 1.00 23.83 ?  194 ILE C O     1 
ATOM   12565 C  CB    . ILE C 2 215 ? 118.366 101.577 118.143 1.00 22.92 ?  194 ILE C CB    1 
ATOM   12566 C  CG1   . ILE C 2 215 ? 118.682 102.828 118.966 1.00 21.11 ?  194 ILE C CG1   1 
ATOM   12567 C  CG2   . ILE C 2 215 ? 117.931 100.421 119.056 1.00 21.89 ?  194 ILE C CG2   1 
ATOM   12568 C  CD1   . ILE C 2 215 ? 117.541 103.301 119.843 1.00 22.26 ?  194 ILE C CD1   1 
ATOM   12569 N  N     . LEU C 2 216 ? 118.506 99.945  115.432 1.00 24.23 ?  195 LEU C N     1 
ATOM   12570 C  CA    . LEU C 2 216 ? 118.136 98.743  114.675 1.00 25.41 ?  195 LEU C CA    1 
ATOM   12571 C  C     . LEU C 2 216 ? 119.352 98.083  114.021 1.00 25.63 ?  195 LEU C C     1 
ATOM   12572 O  O     . LEU C 2 216 ? 119.486 96.850  114.044 1.00 25.46 ?  195 LEU C O     1 
ATOM   12573 C  CB    . LEU C 2 216 ? 117.056 99.069  113.625 1.00 26.03 ?  195 LEU C CB    1 
ATOM   12574 C  CG    . LEU C 2 216 ? 116.466 97.961  112.740 1.00 28.00 ?  195 LEU C CG    1 
ATOM   12575 C  CD1   . LEU C 2 216 ? 115.118 98.420  112.211 1.00 31.45 ?  195 LEU C CD1   1 
ATOM   12576 C  CD2   . LEU C 2 216 ? 117.397 97.577  111.584 1.00 29.83 ?  195 LEU C CD2   1 
ATOM   12577 N  N     . ARG C 2 217 ? 120.230 98.903  113.451 1.00 25.98 ?  196 ARG C N     1 
ATOM   12578 C  CA    . ARG C 2 217 ? 121.485 98.427  112.878 1.00 26.73 ?  196 ARG C CA    1 
ATOM   12579 C  C     . ARG C 2 217 ? 122.305 97.634  113.926 1.00 25.95 ?  196 ARG C C     1 
ATOM   12580 O  O     . ARG C 2 217 ? 122.830 96.562  113.606 1.00 25.75 ?  196 ARG C O     1 
ATOM   12581 C  CB    . ARG C 2 217 ? 122.289 99.607  112.327 1.00 27.29 ?  196 ARG C CB    1 
ATOM   12582 C  CG    . ARG C 2 217 ? 123.497 99.237  111.455 1.00 30.12 ?  196 ARG C CG    1 
ATOM   12583 C  CD    . ARG C 2 217 ? 124.572 100.298 111.602 1.00 35.40 ?  196 ARG C CD    1 
ATOM   12584 N  NE    . ARG C 2 217 ? 124.718 100.619 113.022 1.00 39.87 ?  196 ARG C NE    1 
ATOM   12585 C  CZ    . ARG C 2 217 ? 125.388 101.648 113.525 1.00 40.55 ?  196 ARG C CZ    1 
ATOM   12586 N  NH1   . ARG C 2 217 ? 126.024 102.509 112.732 1.00 40.77 1  196 ARG C NH1   1 
ATOM   12587 N  NH2   . ARG C 2 217 ? 125.411 101.808 114.843 1.00 41.10 ?  196 ARG C NH2   1 
ATOM   12588 N  N     . ASP C 2 218 ? 122.392 98.154  115.156 1.00 24.70 ?  197 ASP C N     1 
ATOM   12589 C  CA    . ASP C 2 218 ? 123.046 97.445  116.275 1.00 24.55 ?  197 ASP C CA    1 
ATOM   12590 C  C     . ASP C 2 218 ? 122.339 96.116  116.607 1.00 24.23 ?  197 ASP C C     1 
ATOM   12591 O  O     . ASP C 2 218 ? 122.994 95.072  116.687 1.00 23.69 ?  197 ASP C O     1 
ATOM   12592 C  CB    . ASP C 2 218 ? 123.126 98.302  117.555 1.00 24.50 ?  197 ASP C CB    1 
ATOM   12593 C  CG    . ASP C 2 218 ? 124.051 99.526  117.426 1.00 25.84 ?  197 ASP C CG    1 
ATOM   12594 O  OD1   . ASP C 2 218 ? 124.981 99.539  116.590 1.00 26.91 ?  197 ASP C OD1   1 
ATOM   12595 O  OD2   . ASP C 2 218 ? 123.852 100.485 118.197 1.00 25.72 -1 197 ASP C OD2   1 
ATOM   12596 N  N     . GLU C 2 219 ? 121.013 96.145  116.774 1.00 23.92 ?  198 GLU C N     1 
ATOM   12597 C  CA    . GLU C 2 219 ? 120.301 94.928  117.200 1.00 24.20 ?  198 GLU C CA    1 
ATOM   12598 C  C     . GLU C 2 219 ? 120.429 93.815  116.176 1.00 24.02 ?  198 GLU C C     1 
ATOM   12599 O  O     . GLU C 2 219 ? 120.507 92.652  116.554 1.00 24.24 ?  198 GLU C O     1 
ATOM   12600 C  CB    . GLU C 2 219 ? 118.821 95.162  117.513 1.00 24.05 ?  198 GLU C CB    1 
ATOM   12601 C  CG    . GLU C 2 219 ? 118.464 96.450  118.232 1.00 25.03 ?  198 GLU C CG    1 
ATOM   12602 C  CD    . GLU C 2 219 ? 118.882 96.543  119.713 1.00 26.31 ?  198 GLU C CD    1 
ATOM   12603 O  OE1   . GLU C 2 219 ? 119.840 95.862  120.182 1.00 27.65 ?  198 GLU C OE1   1 
ATOM   12604 O  OE2   . GLU C 2 219 ? 118.230 97.365  120.415 1.00 26.87 -1 198 GLU C OE2   1 
ATOM   12605 N  N     . ALA C 2 220 ? 120.447 94.169  114.889 1.00 24.00 ?  199 ALA C N     1 
ATOM   12606 C  CA    . ALA C 2 220 ? 120.613 93.177  113.832 1.00 24.72 ?  199 ALA C CA    1 
ATOM   12607 C  C     . ALA C 2 220 ? 121.914 92.374  113.995 1.00 24.80 ?  199 ALA C C     1 
ATOM   12608 O  O     . ALA C 2 220 ? 121.901 91.145  113.887 1.00 25.04 ?  199 ALA C O     1 
ATOM   12609 C  CB    . ALA C 2 220 ? 120.535 93.830  112.429 1.00 24.66 ?  199 ALA C CB    1 
ATOM   12610 N  N     . ILE C 2 221 ? 123.022 93.062  114.264 1.00 24.85 ?  200 ILE C N     1 
ATOM   12611 C  CA    . ILE C 2 221 ? 124.306 92.374  114.487 1.00 25.07 ?  200 ILE C CA    1 
ATOM   12612 C  C     . ILE C 2 221 ? 124.360 91.660  115.846 1.00 23.86 ?  200 ILE C C     1 
ATOM   12613 O  O     . ILE C 2 221 ? 124.983 90.601  115.958 1.00 23.72 ?  200 ILE C O     1 
ATOM   12614 C  CB    . ILE C 2 221 ? 125.567 93.284  114.261 1.00 25.71 ?  200 ILE C CB    1 
ATOM   12615 C  CG1   . ILE C 2 221 ? 125.751 94.294  115.398 1.00 27.10 ?  200 ILE C CG1   1 
ATOM   12616 C  CG2   . ILE C 2 221 ? 125.517 93.955  112.874 1.00 27.18 ?  200 ILE C CG2   1 
ATOM   12617 C  CD1   . ILE C 2 221 ? 127.061 95.089  115.355 1.00 29.63 ?  200 ILE C CD1   1 
ATOM   12618 N  N     . HIS C 2 222 ? 123.698 92.223  116.857 1.00 22.79 ?  201 HIS C N     1 
ATOM   12619 C  CA    . HIS C 2 222 ? 123.585 91.558  118.175 1.00 22.48 ?  201 HIS C CA    1 
ATOM   12620 C  C     . HIS C 2 222 ? 122.842 90.228  118.064 1.00 22.04 ?  201 HIS C C     1 
ATOM   12621 O  O     . HIS C 2 222 ? 123.252 89.244  118.666 1.00 22.06 ?  201 HIS C O     1 
ATOM   12622 C  CB    . HIS C 2 222 ? 122.825 92.413  119.191 1.00 21.77 ?  201 HIS C CB    1 
ATOM   12623 C  CG    . HIS C 2 222 ? 123.512 93.679  119.578 1.00 21.76 ?  201 HIS C CG    1 
ATOM   12624 N  ND1   . HIS C 2 222 ? 123.017 94.512  120.557 1.00 20.70 ?  201 HIS C ND1   1 
ATOM   12625 C  CD2   . HIS C 2 222 ? 124.651 94.258  119.133 1.00 22.07 ?  201 HIS C CD2   1 
ATOM   12626 C  CE1   . HIS C 2 222 ? 123.814 95.555  120.691 1.00 22.26 ?  201 HIS C CE1   1 
ATOM   12627 N  NE2   . HIS C 2 222 ? 124.809 95.429  119.833 1.00 22.52 ?  201 HIS C NE2   1 
ATOM   12628 N  N     . GLY C 2 223 ? 121.731 90.223  117.325 1.00 22.35 ?  202 GLY C N     1 
ATOM   12629 C  CA    . GLY C 2 223 ? 120.936 89.007  117.090 1.00 22.01 ?  202 GLY C CA    1 
ATOM   12630 C  C     . GLY C 2 223 ? 121.691 87.929  116.317 1.00 22.73 ?  202 GLY C C     1 
ATOM   12631 O  O     . GLY C 2 223 ? 121.583 86.732  116.630 1.00 21.99 ?  202 GLY C O     1 
ATOM   12632 N  N     . VAL C 2 224 ? 122.463 88.344  115.310 1.00 22.45 ?  203 VAL C N     1 
ATOM   12633 C  CA    . VAL C 2 224 ? 123.292 87.400  114.557 1.00 22.54 ?  203 VAL C CA    1 
ATOM   12634 C  C     . VAL C 2 224 ? 124.363 86.782  115.459 1.00 22.28 ?  203 VAL C C     1 
ATOM   12635 O  O     . VAL C 2 224 ? 124.505 85.562  115.508 1.00 22.44 ?  203 VAL C O     1 
ATOM   12636 C  CB    . VAL C 2 224 ? 123.955 88.049  113.295 1.00 23.00 ?  203 VAL C CB    1 
ATOM   12637 C  CG1   . VAL C 2 224 ? 124.980 87.088  112.667 1.00 23.10 ?  203 VAL C CG1   1 
ATOM   12638 C  CG2   . VAL C 2 224 ? 122.883 88.442  112.242 1.00 23.14 ?  203 VAL C CG2   1 
ATOM   12639 N  N     . TYR C 2 225 ? 125.084 87.626  116.193 1.00 22.41 ?  204 TYR C N     1 
ATOM   12640 C  CA    . TYR C 2 225 ? 126.164 87.161  117.063 1.00 22.03 ?  204 TYR C CA    1 
ATOM   12641 C  C     . TYR C 2 225 ? 125.686 86.172  118.124 1.00 21.66 ?  204 TYR C C     1 
ATOM   12642 O  O     . TYR C 2 225 ? 126.231 85.064  118.236 1.00 21.72 ?  204 TYR C O     1 
ATOM   12643 C  CB    . TYR C 2 225 ? 126.911 88.335  117.716 1.00 22.22 ?  204 TYR C CB    1 
ATOM   12644 C  CG    . TYR C 2 225 ? 128.167 87.895  118.441 1.00 21.92 ?  204 TYR C CG    1 
ATOM   12645 C  CD1   . TYR C 2 225 ? 129.270 87.418  117.732 1.00 22.36 ?  204 TYR C CD1   1 
ATOM   12646 C  CD2   . TYR C 2 225 ? 128.246 87.948  119.834 1.00 21.43 ?  204 TYR C CD2   1 
ATOM   12647 C  CE1   . TYR C 2 225 ? 130.423 86.996  118.394 1.00 23.82 ?  204 TYR C CE1   1 
ATOM   12648 C  CE2   . TYR C 2 225 ? 129.398 87.537  120.511 1.00 21.49 ?  204 TYR C CE2   1 
ATOM   12649 C  CZ    . TYR C 2 225 ? 130.475 87.065  119.785 1.00 23.58 ?  204 TYR C CZ    1 
ATOM   12650 O  OH    . TYR C 2 225 ? 131.604 86.661  120.447 1.00 25.42 ?  204 TYR C OH    1 
ATOM   12651 N  N     . VAL C 2 226 ? 124.668 86.560  118.896 1.00 20.95 ?  205 VAL C N     1 
ATOM   12652 C  CA    . VAL C 2 226 ? 124.103 85.662  119.911 1.00 20.49 ?  205 VAL C CA    1 
ATOM   12653 C  C     . VAL C 2 226 ? 123.545 84.382  119.261 1.00 20.84 ?  205 VAL C C     1 
ATOM   12654 O  O     . VAL C 2 226 ? 123.721 83.277  119.791 1.00 21.10 ?  205 VAL C O     1 
ATOM   12655 C  CB    . VAL C 2 226 ? 123.064 86.373  120.821 1.00 20.57 ?  205 VAL C CB    1 
ATOM   12656 C  CG1   . VAL C 2 226 ? 122.470 85.391  121.831 1.00 20.35 ?  205 VAL C CG1   1 
ATOM   12657 C  CG2   . VAL C 2 226 ? 123.734 87.542  121.559 1.00 19.60 ?  205 VAL C CG2   1 
ATOM   12658 N  N     . GLY C 2 227 ? 122.924 84.528  118.095 1.00 21.08 ?  206 GLY C N     1 
ATOM   12659 C  CA    . GLY C 2 227 ? 122.486 83.365  117.308 1.00 21.43 ?  206 GLY C CA    1 
ATOM   12660 C  C     . GLY C 2 227 ? 123.598 82.370  117.004 1.00 21.95 ?  206 GLY C C     1 
ATOM   12661 O  O     . GLY C 2 227 ? 123.408 81.147  117.127 1.00 21.84 ?  206 GLY C O     1 
ATOM   12662 N  N     . LEU C 2 228 ? 124.766 82.881  116.614 1.00 22.09 ?  207 LEU C N     1 
ATOM   12663 C  CA    . LEU C 2 228 ? 125.913 82.011  116.338 1.00 22.96 ?  207 LEU C CA    1 
ATOM   12664 C  C     . LEU C 2 228 ? 126.403 81.275  117.594 1.00 22.60 ?  207 LEU C C     1 
ATOM   12665 O  O     . LEU C 2 228 ? 126.753 80.092  117.529 1.00 22.04 ?  207 LEU C O     1 
ATOM   12666 C  CB    . LEU C 2 228 ? 127.052 82.779  115.656 1.00 23.39 ?  207 LEU C CB    1 
ATOM   12667 C  CG    . LEU C 2 228 ? 126.801 83.318  114.235 1.00 24.35 ?  207 LEU C CG    1 
ATOM   12668 C  CD1   . LEU C 2 228 ? 127.839 84.395  113.891 1.00 25.01 ?  207 LEU C CD1   1 
ATOM   12669 C  CD2   . LEU C 2 228 ? 126.816 82.213  113.184 1.00 25.11 ?  207 LEU C CD2   1 
ATOM   12670 N  N     . LEU C 2 229 ? 126.398 81.957  118.737 1.00 22.37 ?  208 LEU C N     1 
ATOM   12671 C  CA    . LEU C 2 229 ? 126.756 81.308  120.013 1.00 22.62 ?  208 LEU C CA    1 
ATOM   12672 C  C     . LEU C 2 229 ? 125.760 80.213  120.411 1.00 22.77 ?  208 LEU C C     1 
ATOM   12673 O  O     . LEU C 2 229 ? 126.159 79.133  120.881 1.00 22.57 ?  208 LEU C O     1 
ATOM   12674 C  CB    . LEU C 2 229 ? 126.922 82.337  121.135 1.00 22.44 ?  208 LEU C CB    1 
ATOM   12675 C  CG    . LEU C 2 229 ? 127.961 83.441  120.886 1.00 23.54 ?  208 LEU C CG    1 
ATOM   12676 C  CD1   . LEU C 2 229 ? 127.954 84.452  122.030 1.00 23.37 ?  208 LEU C CD1   1 
ATOM   12677 C  CD2   . LEU C 2 229 ? 129.370 82.859  120.678 1.00 23.91 ?  208 LEU C CD2   1 
ATOM   12678 N  N     . ALA C 2 230 ? 124.471 80.488  120.212 1.00 22.42 ?  209 ALA C N     1 
ATOM   12679 C  CA    . ALA C 2 230 ? 123.422 79.501  120.465 1.00 22.02 ?  209 ALA C CA    1 
ATOM   12680 C  C     . ALA C 2 230 ? 123.599 78.259  119.585 1.00 22.58 ?  209 ALA C C     1 
ATOM   12681 O  O     . ALA C 2 230 ? 123.510 77.139  120.071 1.00 22.14 ?  209 ALA C O     1 
ATOM   12682 C  CB    . ALA C 2 230 ? 122.056 80.110  120.245 1.00 22.04 ?  209 ALA C CB    1 
ATOM   12683 N  N     . GLN C 2 231 ? 123.871 78.472  118.300 1.00 22.96 ?  210 GLN C N     1 
ATOM   12684 C  CA    . GLN C 2 231 ? 124.121 77.357  117.368 1.00 24.30 ?  210 GLN C CA    1 
ATOM   12685 C  C     . GLN C 2 231 ? 125.306 76.498  117.770 1.00 25.11 ?  210 GLN C C     1 
ATOM   12686 O  O     . GLN C 2 231 ? 125.284 75.278  117.569 1.00 24.97 ?  210 GLN C O     1 
ATOM   12687 C  CB    . GLN C 2 231 ? 124.315 77.872  115.946 1.00 24.38 ?  210 GLN C CB    1 
ATOM   12688 C  CG    . GLN C 2 231 ? 123.028 78.457  115.339 1.00 25.12 ?  210 GLN C CG    1 
ATOM   12689 C  CD    . GLN C 2 231 ? 123.237 78.961  113.927 1.00 28.08 ?  210 GLN C CD    1 
ATOM   12690 O  OE1   . GLN C 2 231 ? 123.698 78.221  113.057 1.00 27.83 ?  210 GLN C OE1   1 
ATOM   12691 N  NE2   . GLN C 2 231 ? 122.914 80.235  113.692 1.00 26.38 ?  210 GLN C NE2   1 
ATOM   12692 N  N     . GLU C 2 232 ? 126.341 77.127  118.332 1.00 25.80 ?  211 GLU C N     1 
ATOM   12693 C  CA    . GLU C 2 232 ? 127.493 76.383  118.849 1.00 27.16 ?  211 GLU C CA    1 
ATOM   12694 C  C     . GLU C 2 232 ? 127.061 75.347  119.882 1.00 26.47 ?  211 GLU C C     1 
ATOM   12695 O  O     . GLU C 2 232 ? 127.510 74.195  119.848 1.00 26.10 ?  211 GLU C O     1 
ATOM   12696 C  CB    . GLU C 2 232 ? 128.494 77.319  119.514 1.00 27.59 ?  211 GLU C CB    1 
ATOM   12697 C  CG    . GLU C 2 232 ? 129.556 77.856  118.604 1.00 32.55 ?  211 GLU C CG    1 
ATOM   12698 C  CD    . GLU C 2 232 ? 130.875 78.084  119.332 1.00 36.72 ?  211 GLU C CD    1 
ATOM   12699 O  OE1   . GLU C 2 232 ? 130.929 77.910  120.573 1.00 38.32 ?  211 GLU C OE1   1 
ATOM   12700 O  OE2   . GLU C 2 232 ? 131.861 78.432  118.653 1.00 40.62 -1 211 GLU C OE2   1 
ATOM   12701 N  N     . ILE C 2 233 ? 126.203 75.769  120.809 1.00 25.55 ?  212 ILE C N     1 
ATOM   12702 C  CA    . ILE C 2 233 ? 125.736 74.887  121.879 1.00 25.32 ?  212 ILE C CA    1 
ATOM   12703 C  C     . ILE C 2 233 ? 124.808 73.805  121.341 1.00 25.48 ?  212 ILE C C     1 
ATOM   12704 O  O     . ILE C 2 233 ? 124.982 72.623  121.644 1.00 25.82 ?  212 ILE C O     1 
ATOM   12705 C  CB    . ILE C 2 233 ? 125.057 75.672  123.023 1.00 25.39 ?  212 ILE C CB    1 
ATOM   12706 C  CG1   . ILE C 2 233 ? 126.097 76.538  123.739 1.00 24.37 ?  212 ILE C CG1   1 
ATOM   12707 C  CG2   . ILE C 2 233 ? 124.365 74.712  123.996 1.00 24.86 ?  212 ILE C CG2   1 
ATOM   12708 C  CD1   . ILE C 2 233 ? 125.490 77.641  124.592 1.00 25.10 ?  212 ILE C CD1   1 
ATOM   12709 N  N     . TYR C 2 234 ? 123.842 74.214  120.523 1.00 25.27 ?  213 TYR C N     1 
ATOM   12710 C  CA    . TYR C 2 234 ? 122.932 73.288  119.844 1.00 25.77 ?  213 TYR C CA    1 
ATOM   12711 C  C     . TYR C 2 234 ? 123.686 72.192  119.070 1.00 26.44 ?  213 TYR C C     1 
ATOM   12712 O  O     . TYR C 2 234 ? 123.310 71.018  119.110 1.00 26.29 ?  213 TYR C O     1 
ATOM   12713 C  CB    . TYR C 2 234 ? 122.015 74.083  118.902 1.00 25.67 ?  213 TYR C CB    1 
ATOM   12714 C  CG    . TYR C 2 234 ? 121.039 73.286  118.062 1.00 25.65 ?  213 TYR C CG    1 
ATOM   12715 C  CD1   . TYR C 2 234 ? 119.740 73.039  118.515 1.00 25.02 ?  213 TYR C CD1   1 
ATOM   12716 C  CD2   . TYR C 2 234 ? 121.395 72.827  116.784 1.00 26.59 ?  213 TYR C CD2   1 
ATOM   12717 C  CE1   . TYR C 2 234 ? 118.830 72.332  117.737 1.00 26.52 ?  213 TYR C CE1   1 
ATOM   12718 C  CE2   . TYR C 2 234 ? 120.493 72.110  115.996 1.00 27.00 ?  213 TYR C CE2   1 
ATOM   12719 C  CZ    . TYR C 2 234 ? 119.215 71.866  116.484 1.00 27.79 ?  213 TYR C CZ    1 
ATOM   12720 O  OH    . TYR C 2 234 ? 118.319 71.180  115.714 1.00 29.00 ?  213 TYR C OH    1 
ATOM   12721 N  N     . ASN C 2 235 ? 124.748 72.576  118.365 1.00 26.96 ?  214 ASN C N     1 
ATOM   12722 C  CA    . ASN C 2 235 ? 125.485 71.620  117.540 1.00 28.05 ?  214 ASN C CA    1 
ATOM   12723 C  C     . ASN C 2 235 ? 126.262 70.565  118.322 1.00 28.24 ?  214 ASN C C     1 
ATOM   12724 O  O     . ASN C 2 235 ? 126.672 69.560  117.751 1.00 28.63 ?  214 ASN C O     1 
ATOM   12725 C  CB    . ASN C 2 235 ? 126.379 72.335  116.515 1.00 28.38 ?  214 ASN C CB    1 
ATOM   12726 C  CG    . ASN C 2 235 ? 125.572 73.073  115.453 1.00 31.14 ?  214 ASN C CG    1 
ATOM   12727 O  OD1   . ASN C 2 235 ? 124.475 72.649  115.078 1.00 34.16 ?  214 ASN C OD1   1 
ATOM   12728 N  ND2   . ASN C 2 235 ? 126.112 74.185  114.968 1.00 32.42 ?  214 ASN C ND2   1 
ATOM   12729 N  N     . LYS C 2 236 ? 126.439 70.784  119.624 1.00 27.91 ?  215 LYS C N     1 
ATOM   12730 C  CA    . LYS C 2 236 ? 127.089 69.812  120.505 1.00 28.49 ?  215 LYS C CA    1 
ATOM   12731 C  C     . LYS C 2 236 ? 126.161 68.678  120.954 1.00 28.50 ?  215 LYS C C     1 
ATOM   12732 O  O     . LYS C 2 236 ? 126.620 67.668  121.493 1.00 28.98 ?  215 LYS C O     1 
ATOM   12733 C  CB    . LYS C 2 236 ? 127.669 70.506  121.742 1.00 28.10 ?  215 LYS C CB    1 
ATOM   12734 C  CG    . LYS C 2 236 ? 128.786 71.495  121.441 1.00 29.25 ?  215 LYS C CG    1 
ATOM   12735 C  CD    . LYS C 2 236 ? 129.326 72.129  122.713 1.00 30.19 ?  215 LYS C CD    1 
ATOM   12736 C  CE    . LYS C 2 236 ? 130.198 73.313  122.370 1.00 32.63 ?  215 LYS C CE    1 
ATOM   12737 N  NZ    . LYS C 2 236 ? 130.736 73.962  123.588 1.00 35.39 1  215 LYS C NZ    1 
ATOM   12738 N  N     . GLN C 2 237 ? 124.862 68.830  120.718 1.00 28.25 ?  216 GLN C N     1 
ATOM   12739 C  CA    . GLN C 2 237 ? 123.884 67.905  121.293 1.00 28.34 ?  216 GLN C CA    1 
ATOM   12740 C  C     . GLN C 2 237 ? 123.636 66.647  120.443 1.00 28.92 ?  216 GLN C C     1 
ATOM   12741 O  O     . GLN C 2 237 ? 123.922 66.628  119.246 1.00 28.53 ?  216 GLN C O     1 
ATOM   12742 C  CB    . GLN C 2 237 ? 122.572 68.648  121.582 1.00 27.68 ?  216 GLN C CB    1 
ATOM   12743 C  CG    . GLN C 2 237 ? 122.745 69.959  122.387 1.00 26.67 ?  216 GLN C CG    1 
ATOM   12744 C  CD    . GLN C 2 237 ? 123.574 69.798  123.657 1.00 25.32 ?  216 GLN C CD    1 
ATOM   12745 O  OE1   . GLN C 2 237 ? 123.397 68.844  124.418 1.00 25.49 ?  216 GLN C OE1   1 
ATOM   12746 N  NE2   . GLN C 2 237 ? 124.484 70.740  123.894 1.00 23.63 ?  216 GLN C NE2   1 
ATOM   12747 N  N     . THR C 2 238 ? 123.100 65.603  121.076 1.00 29.53 ?  217 THR C N     1 
ATOM   12748 C  CA    . THR C 2 238 ? 122.578 64.442  120.349 1.00 30.73 ?  217 THR C CA    1 
ATOM   12749 C  C     . THR C 2 238 ? 121.378 64.878  119.500 1.00 31.13 ?  217 THR C C     1 
ATOM   12750 O  O     . THR C 2 238 ? 120.801 65.957  119.728 1.00 30.17 ?  217 THR C O     1 
ATOM   12751 C  CB    . THR C 2 238 ? 122.086 63.336  121.299 1.00 30.79 ?  217 THR C CB    1 
ATOM   12752 O  OG1   . THR C 2 238 ? 120.915 63.793  121.989 1.00 31.16 ?  217 THR C OG1   1 
ATOM   12753 C  CG2   . THR C 2 238 ? 123.165 62.943  122.314 1.00 31.22 ?  217 THR C CG2   1 
ATOM   12754 N  N     . GLU C 2 239 ? 120.985 64.032  118.545 1.00 31.67 ?  218 GLU C N     1 
ATOM   12755 C  CA    . GLU C 2 239 ? 119.811 64.323  117.721 1.00 32.25 ?  218 GLU C CA    1 
ATOM   12756 C  C     . GLU C 2 239 ? 118.533 64.431  118.560 1.00 31.86 ?  218 GLU C C     1 
ATOM   12757 O  O     . GLU C 2 239 ? 117.684 65.291  118.307 1.00 31.09 ?  218 GLU C O     1 
ATOM   12758 C  CB    . GLU C 2 239 ? 119.663 63.296  116.585 1.00 33.29 ?  218 GLU C CB    1 
ATOM   12759 C  CG    . GLU C 2 239 ? 120.769 63.402  115.517 1.00 35.65 ?  218 GLU C CG    1 
ATOM   12760 C  CD    . GLU C 2 239 ? 120.826 64.780  114.848 1.00 39.17 ?  218 GLU C CD    1 
ATOM   12761 O  OE1   . GLU C 2 239 ? 119.754 65.311  114.459 1.00 41.08 ?  218 GLU C OE1   1 
ATOM   12762 O  OE2   . GLU C 2 239 ? 121.941 65.341  114.716 1.00 39.64 -1 218 GLU C OE2   1 
ATOM   12763 N  N     . GLU C 2 240 ? 118.428 63.578  119.579 1.00 31.72 ?  219 GLU C N     1 
ATOM   12764 C  CA    . GLU C 2 240 ? 117.296 63.583  120.497 1.00 31.76 ?  219 GLU C CA    1 
ATOM   12765 C  C     . GLU C 2 240 ? 117.216 64.903  121.278 1.00 30.21 ?  219 GLU C C     1 
ATOM   12766 O  O     . GLU C 2 240 ? 116.137 65.500  121.403 1.00 29.63 ?  219 GLU C O     1 
ATOM   12767 C  CB    . GLU C 2 240 ? 117.396 62.383  121.442 1.00 32.58 ?  219 GLU C CB    1 
ATOM   12768 C  CG    . GLU C 2 240 ? 116.162 62.136  122.295 1.00 36.93 ?  219 GLU C CG    1 
ATOM   12769 C  CD    . GLU C 2 240 ? 116.155 60.743  122.916 1.00 42.06 ?  219 GLU C CD    1 
ATOM   12770 O  OE1   . GLU C 2 240 ? 116.254 60.639  124.159 1.00 44.09 ?  219 GLU C OE1   1 
ATOM   12771 O  OE2   . GLU C 2 240 ? 116.057 59.749  122.158 1.00 44.45 -1 219 GLU C OE2   1 
ATOM   12772 N  N     . LYS C 2 241 ? 118.363 65.353  121.785 1.00 28.91 ?  220 LYS C N     1 
ATOM   12773 C  CA    . LYS C 2 241 ? 118.452 66.609  122.517 1.00 28.14 ?  220 LYS C CA    1 
ATOM   12774 C  C     . LYS C 2 241 ? 118.136 67.815  121.630 1.00 27.03 ?  220 LYS C C     1 
ATOM   12775 O  O     . LYS C 2 241 ? 117.436 68.737  122.061 1.00 26.72 ?  220 LYS C O     1 
ATOM   12776 C  CB    . LYS C 2 241 ? 119.828 66.772  123.169 1.00 27.83 ?  220 LYS C CB    1 
ATOM   12777 C  CG    . LYS C 2 241 ? 119.947 68.021  124.052 1.00 29.68 ?  220 LYS C CG    1 
ATOM   12778 C  CD    . LYS C 2 241 ? 119.738 67.707  125.527 1.00 33.58 ?  220 LYS C CD    1 
ATOM   12779 C  CE    . LYS C 2 241 ? 118.282 67.659  125.896 1.00 33.71 ?  220 LYS C CE    1 
ATOM   12780 N  NZ    . LYS C 2 241 ? 118.066 67.191  127.305 1.00 34.69 1  220 LYS C NZ    1 
ATOM   12781 N  N     . LYS C 2 242 ? 118.663 67.800  120.404 1.00 26.38 ?  221 LYS C N     1 
ATOM   12782 C  CA    . LYS C 2 242 ? 118.375 68.822  119.394 1.00 25.87 ?  221 LYS C CA    1 
ATOM   12783 C  C     . LYS C 2 242 ? 116.887 68.956  119.127 1.00 25.72 ?  221 LYS C C     1 
ATOM   12784 O  O     . LYS C 2 242 ? 116.366 70.077  119.047 1.00 24.52 ?  221 LYS C O     1 
ATOM   12785 C  CB    . LYS C 2 242 ? 119.093 68.521  118.076 1.00 25.83 ?  221 LYS C CB    1 
ATOM   12786 C  CG    . LYS C 2 242 ? 120.575 68.820  118.074 1.00 26.76 ?  221 LYS C CG    1 
ATOM   12787 C  CD    . LYS C 2 242 ? 121.142 68.608  116.674 1.00 28.40 ?  221 LYS C CD    1 
ATOM   12788 C  CE    . LYS C 2 242 ? 122.643 68.669  116.667 1.00 29.84 ?  221 LYS C CE    1 
ATOM   12789 N  NZ    . LYS C 2 242 ? 123.177 68.243  115.351 1.00 30.96 1  221 LYS C NZ    1 
ATOM   12790 N  N     . ALA C 2 243 ? 116.216 67.810  118.979 1.00 25.97 ?  222 ALA C N     1 
ATOM   12791 C  CA    . ALA C 2 243 ? 114.764 67.781  118.784 1.00 25.79 ?  222 ALA C CA    1 
ATOM   12792 C  C     . ALA C 2 243 ? 114.025 68.470  119.932 1.00 25.24 ?  222 ALA C C     1 
ATOM   12793 O  O     . ALA C 2 243 ? 113.068 69.221  119.695 1.00 25.37 ?  222 ALA C O     1 
ATOM   12794 C  CB    . ALA C 2 243 ? 114.271 66.346  118.588 1.00 26.17 ?  222 ALA C CB    1 
ATOM   12795 N  N     . GLU C 2 244 ? 114.478 68.248  121.164 1.00 25.02 ?  223 GLU C N     1 
ATOM   12796 C  CA    . GLU C 2 244 ? 113.900 68.933  122.330 1.00 25.08 ?  223 GLU C CA    1 
ATOM   12797 C  C     . GLU C 2 244 ? 114.180 70.447  122.324 1.00 24.70 ?  223 GLU C C     1 
ATOM   12798 O  O     . GLU C 2 244 ? 113.311 71.253  122.687 1.00 24.20 ?  223 GLU C O     1 
ATOM   12799 C  CB    . GLU C 2 244 ? 114.387 68.306  123.641 1.00 25.35 ?  223 GLU C CB    1 
ATOM   12800 C  CG    . GLU C 2 244 ? 113.762 68.951  124.890 1.00 26.67 ?  223 GLU C CG    1 
ATOM   12801 C  CD    . GLU C 2 244 ? 114.444 68.540  126.181 1.00 28.29 ?  223 GLU C CD    1 
ATOM   12802 O  OE1   . GLU C 2 244 ? 115.076 67.467  126.222 1.00 29.51 ?  223 GLU C OE1   1 
ATOM   12803 O  OE2   . GLU C 2 244 ? 114.348 69.299  127.163 1.00 29.09 -1 223 GLU C OE2   1 
ATOM   12804 N  N     . LEU C 2 245 ? 115.389 70.825  121.923 1.00 24.27 ?  224 LEU C N     1 
ATOM   12805 C  CA    . LEU C 2 245 ? 115.759 72.240  121.862 1.00 24.54 ?  224 LEU C CA    1 
ATOM   12806 C  C     . LEU C 2 245 ? 114.954 73.020  120.812 1.00 24.42 ?  224 LEU C C     1 
ATOM   12807 O  O     . LEU C 2 245 ? 114.579 74.171  121.045 1.00 24.10 ?  224 LEU C O     1 
ATOM   12808 C  CB    . LEU C 2 245 ? 117.277 72.406  121.664 1.00 23.86 ?  224 LEU C CB    1 
ATOM   12809 C  CG    . LEU C 2 245 ? 118.153 71.951  122.840 1.00 24.78 ?  224 LEU C CG    1 
ATOM   12810 C  CD1   . LEU C 2 245 ? 119.635 72.216  122.554 1.00 25.54 ?  224 LEU C CD1   1 
ATOM   12811 C  CD2   . LEU C 2 245 ? 117.740 72.610  124.164 1.00 25.29 ?  224 LEU C CD2   1 
ATOM   12812 N  N     . ARG C 2 246 ? 114.681 72.384  119.674 1.00 25.26 ?  225 ARG C N     1 
ATOM   12813 C  CA    . ARG C 2 246 ? 113.806 72.965  118.645 1.00 25.97 ?  225 ARG C CA    1 
ATOM   12814 C  C     . ARG C 2 246 ? 112.397 73.143  119.194 1.00 25.85 ?  225 ARG C C     1 
ATOM   12815 O  O     . ARG C 2 246 ? 111.769 74.178  118.964 1.00 25.01 ?  225 ARG C O     1 
ATOM   12816 C  CB    . ARG C 2 246 ? 113.783 72.112  117.359 1.00 26.65 ?  225 ARG C CB    1 
ATOM   12817 C  CG    . ARG C 2 246 ? 115.116 72.082  116.614 1.00 28.90 ?  225 ARG C CG    1 
ATOM   12818 C  CD    . ARG C 2 246 ? 114.996 71.569  115.159 1.00 31.26 ?  225 ARG C CD    1 
ATOM   12819 N  NE    . ARG C 2 246 ? 114.457 70.209  115.073 1.00 34.01 ?  225 ARG C NE    1 
ATOM   12820 C  CZ    . ARG C 2 246 ? 115.144 69.097  115.335 1.00 35.64 ?  225 ARG C CZ    1 
ATOM   12821 N  NH1   . ARG C 2 246 ? 116.415 69.155  115.710 1.00 36.11 1  225 ARG C NH1   1 
ATOM   12822 N  NH2   . ARG C 2 246 ? 114.550 67.914  115.221 1.00 37.05 ?  225 ARG C NH2   1 
ATOM   12823 N  N     . GLU C 2 247 ? 111.908 72.140  119.929 1.00 26.01 ?  226 GLU C N     1 
ATOM   12824 C  CA    . GLU C 2 247 ? 110.607 72.237  120.601 1.00 26.48 ?  226 GLU C CA    1 
ATOM   12825 C  C     . GLU C 2 247 ? 110.577 73.422  121.564 1.00 25.72 ?  226 GLU C C     1 
ATOM   12826 O  O     . GLU C 2 247 ? 109.622 74.212  121.556 1.00 25.16 ?  226 GLU C O     1 
ATOM   12827 C  CB    . GLU C 2 247 ? 110.268 70.955  121.367 1.00 27.18 ?  226 GLU C CB    1 
ATOM   12828 C  CG    . GLU C 2 247 ? 108.788 70.845  121.713 1.00 30.38 ?  226 GLU C CG    1 
ATOM   12829 C  CD    . GLU C 2 247 ? 108.506 70.211  123.063 1.00 35.77 ?  226 GLU C CD    1 
ATOM   12830 O  OE1   . GLU C 2 247 ? 109.302 69.373  123.539 1.00 38.02 ?  226 GLU C OE1   1 
ATOM   12831 O  OE2   . GLU C 2 247 ? 107.462 70.555  123.657 1.00 40.39 -1 226 GLU C OE2   1 
ATOM   12832 N  N     . PHE C 2 248 ? 111.622 73.544  122.385 1.00 24.71 ?  227 PHE C N     1 
ATOM   12833 C  CA    . PHE C 2 248 ? 111.735 74.673  123.307 1.00 23.71 ?  227 PHE C CA    1 
ATOM   12834 C  C     . PHE C 2 248 ? 111.661 75.996  122.543 1.00 23.14 ?  227 PHE C C     1 
ATOM   12835 O  O     . PHE C 2 248 ? 110.897 76.887  122.920 1.00 22.40 ?  227 PHE C O     1 
ATOM   12836 C  CB    . PHE C 2 248 ? 113.029 74.621  124.140 1.00 23.85 ?  227 PHE C CB    1 
ATOM   12837 C  CG    . PHE C 2 248 ? 113.340 75.924  124.832 1.00 23.64 ?  227 PHE C CG    1 
ATOM   12838 C  CD1   . PHE C 2 248 ? 112.728 76.241  126.047 1.00 23.07 ?  227 PHE C CD1   1 
ATOM   12839 C  CD2   . PHE C 2 248 ? 114.191 76.867  124.230 1.00 23.04 ?  227 PHE C CD2   1 
ATOM   12840 C  CE1   . PHE C 2 248 ? 112.985 77.454  126.683 1.00 22.73 ?  227 PHE C CE1   1 
ATOM   12841 C  CE2   . PHE C 2 248 ? 114.453 78.090  124.850 1.00 23.31 ?  227 PHE C CE2   1 
ATOM   12842 C  CZ    . PHE C 2 248 ? 113.851 78.387  126.085 1.00 21.51 ?  227 PHE C CZ    1 
ATOM   12843 N  N     . ALA C 2 249 ? 112.450 76.108  121.473 1.00 22.95 ?  228 ALA C N     1 
ATOM   12844 C  CA    . ALA C 2 249 ? 112.569 77.361  120.716 1.00 22.96 ?  228 ALA C CA    1 
ATOM   12845 C  C     . ALA C 2 249 ? 111.248 77.748  120.055 1.00 23.31 ?  228 ALA C C     1 
ATOM   12846 O  O     . ALA C 2 249 ? 110.846 78.913  120.086 1.00 22.63 ?  228 ALA C O     1 
ATOM   12847 C  CB    . ALA C 2 249 ? 113.679 77.257  119.673 1.00 22.40 ?  228 ALA C CB    1 
ATOM   12848 N  N     . ILE C 2 250 ? 110.585 76.762  119.462 1.00 23.66 ?  229 ILE C N     1 
ATOM   12849 C  CA    . ILE C 2 250 ? 109.309 76.983  118.780 1.00 25.00 ?  229 ILE C CA    1 
ATOM   12850 C  C     . ILE C 2 250 ? 108.167 77.255  119.769 1.00 24.64 ?  229 ILE C C     1 
ATOM   12851 O  O     . ILE C 2 250 ? 107.369 78.177  119.556 1.00 24.26 ?  229 ILE C O     1 
ATOM   12852 C  CB    . ILE C 2 250 ? 108.992 75.836  117.771 1.00 25.43 ?  229 ILE C CB    1 
ATOM   12853 C  CG1   . ILE C 2 250 ? 109.944 75.944  116.570 1.00 27.27 ?  229 ILE C CG1   1 
ATOM   12854 C  CG2   . ILE C 2 250 ? 107.532 75.939  117.252 1.00 27.62 ?  229 ILE C CG2   1 
ATOM   12855 C  CD1   . ILE C 2 250 ? 110.395 74.603  115.975 1.00 31.32 ?  229 ILE C CD1   1 
ATOM   12856 N  N     . ASP C 2 251 ? 108.105 76.489  120.859 1.00 24.78 ?  230 ASP C N     1 
ATOM   12857 C  CA    . ASP C 2 251 ? 107.124 76.763  121.925 1.00 25.20 ?  230 ASP C CA    1 
ATOM   12858 C  C     . ASP C 2 251 ? 107.294 78.163  122.514 1.00 24.08 ?  230 ASP C C     1 
ATOM   12859 O  O     . ASP C 2 251 ? 106.307 78.871  122.769 1.00 23.34 ?  230 ASP C O     1 
ATOM   12860 C  CB    . ASP C 2 251 ? 107.238 75.751  123.074 1.00 25.73 ?  230 ASP C CB    1 
ATOM   12861 C  CG    . ASP C 2 251 ? 106.649 74.402  122.736 1.00 28.78 ?  230 ASP C CG    1 
ATOM   12862 O  OD1   . ASP C 2 251 ? 106.046 74.244  121.649 1.00 29.99 ?  230 ASP C OD1   1 
ATOM   12863 O  OD2   . ASP C 2 251 ? 106.800 73.489  123.575 1.00 33.31 -1 230 ASP C OD2   1 
ATOM   12864 N  N     . LEU C 2 252 ? 108.545 78.554  122.744 1.00 22.98 ?  231 LEU C N     1 
ATOM   12865 C  CA    . LEU C 2 252 ? 108.823 79.878  123.302 1.00 21.63 ?  231 LEU C CA    1 
ATOM   12866 C  C     . LEU C 2 252 ? 108.426 80.966  122.310 1.00 21.66 ?  231 LEU C C     1 
ATOM   12867 O  O     . LEU C 2 252 ? 107.835 81.981  122.682 1.00 19.41 ?  231 LEU C O     1 
ATOM   12868 C  CB    . LEU C 2 252 ? 110.299 80.026  123.669 1.00 21.89 ?  231 LEU C CB    1 
ATOM   12869 C  CG    . LEU C 2 252 ? 110.762 81.401  124.186 1.00 21.33 ?  231 LEU C CG    1 
ATOM   12870 C  CD1   . LEU C 2 252 ? 109.983 81.833  125.447 1.00 20.89 ?  231 LEU C CD1   1 
ATOM   12871 C  CD2   . LEU C 2 252 ? 112.271 81.358  124.445 1.00 20.31 ?  231 LEU C CD2   1 
ATOM   12872 N  N     . LEU C 2 253 ? 108.765 80.748  121.042 1.00 22.28 ?  232 LEU C N     1 
ATOM   12873 C  CA    . LEU C 2 253 ? 108.435 81.727  120.012 1.00 23.05 ?  232 LEU C CA    1 
ATOM   12874 C  C     . LEU C 2 253 ? 106.925 81.931  119.924 1.00 23.36 ?  232 LEU C C     1 
ATOM   12875 O  O     . LEU C 2 253 ? 106.452 83.080  119.942 1.00 22.96 ?  232 LEU C O     1 
ATOM   12876 C  CB    . LEU C 2 253 ? 109.017 81.326  118.656 1.00 23.53 ?  232 LEU C CB    1 
ATOM   12877 C  CG    . LEU C 2 253 ? 108.713 82.321  117.530 1.00 25.63 ?  232 LEU C CG    1 
ATOM   12878 C  CD1   . LEU C 2 253 ? 109.366 83.680  117.784 1.00 25.88 ?  232 LEU C CD1   1 
ATOM   12879 C  CD2   . LEU C 2 253 ? 109.169 81.742  116.200 1.00 27.67 ?  232 LEU C CD2   1 
ATOM   12880 N  N     . ASN C 2 254 ? 106.178 80.825  119.848 1.00 23.55 ?  233 ASN C N     1 
ATOM   12881 C  CA    . ASN C 2 254 ? 104.706 80.886  119.819 1.00 24.61 ?  233 ASN C CA    1 
ATOM   12882 C  C     . ASN C 2 254 ? 104.096 81.584  121.037 1.00 23.57 ?  233 ASN C C     1 
ATOM   12883 O  O     . ASN C 2 254 ? 103.166 82.377  120.908 1.00 23.52 ?  233 ASN C O     1 
ATOM   12884 C  CB    . ASN C 2 254 ? 104.097 79.493  119.642 1.00 24.99 ?  233 ASN C CB    1 
ATOM   12885 C  CG    . ASN C 2 254 ? 104.021 79.068  118.180 1.00 28.92 ?  233 ASN C CG    1 
ATOM   12886 O  OD1   . ASN C 2 254 ? 103.413 79.745  117.349 1.00 33.75 ?  233 ASN C OD1   1 
ATOM   12887 N  ND2   . ASN C 2 254 ? 104.635 77.943  117.867 1.00 30.99 ?  233 ASN C ND2   1 
ATOM   12888 N  N     . GLN C 2 255 ? 104.625 81.290  122.222 1.00 23.22 ?  234 GLN C N     1 
ATOM   12889 C  CA    . GLN C 2 255 ? 104.142 81.936  123.434 1.00 22.54 ?  234 GLN C CA    1 
ATOM   12890 C  C     . GLN C 2 255 ? 104.400 83.457  123.410 1.00 22.00 ?  234 GLN C C     1 
ATOM   12891 O  O     . GLN C 2 255 ? 103.514 84.260  123.752 1.00 21.73 ?  234 GLN C O     1 
ATOM   12892 C  CB    . GLN C 2 255 ? 104.773 81.294  124.669 1.00 22.85 ?  234 GLN C CB    1 
ATOM   12893 C  CG    . GLN C 2 255 ? 104.101 81.697  125.965 1.00 23.87 ?  234 GLN C CG    1 
ATOM   12894 C  CD    . GLN C 2 255 ? 104.754 81.079  127.196 1.00 24.95 ?  234 GLN C CD    1 
ATOM   12895 O  OE1   . GLN C 2 255 ? 105.619 80.203  127.088 1.00 24.21 ?  234 GLN C OE1   1 
ATOM   12896 N  NE2   . GLN C 2 255 ? 104.356 81.558  128.376 1.00 25.97 ?  234 GLN C NE2   1 
ATOM   12897 N  N     . LEU C 2 256 ? 105.604 83.845  123.007 1.00 21.27 ?  235 LEU C N     1 
ATOM   12898 C  CA    . LEU C 2 256 ? 105.947 85.257  122.874 1.00 21.37 ?  235 LEU C CA    1 
ATOM   12899 C  C     . LEU C 2 256 ? 105.114 85.921  121.774 1.00 21.21 ?  235 LEU C C     1 
ATOM   12900 O  O     . LEU C 2 256 ? 104.662 87.055  121.920 1.00 20.75 ?  235 LEU C O     1 
ATOM   12901 C  CB    . LEU C 2 256 ? 107.442 85.409  122.561 1.00 20.93 ?  235 LEU C CB    1 
ATOM   12902 C  CG    . LEU C 2 256 ? 108.461 85.121  123.666 1.00 21.74 ?  235 LEU C CG    1 
ATOM   12903 C  CD1   . LEU C 2 256 ? 109.886 85.209  123.098 1.00 20.15 ?  235 LEU C CD1   1 
ATOM   12904 C  CD2   . LEU C 2 256 ? 108.298 86.061  124.860 1.00 20.90 ?  235 LEU C CD2   1 
ATOM   12905 N  N     . TYR C 2 257 ? 104.938 85.201  120.671 1.00 21.68 ?  236 TYR C N     1 
ATOM   12906 C  CA    . TYR C 2 257 ? 104.170 85.685  119.524 1.00 22.40 ?  236 TYR C CA    1 
ATOM   12907 C  C     . TYR C 2 257 ? 102.720 86.016  119.915 1.00 23.31 ?  236 TYR C C     1 
ATOM   12908 O  O     . TYR C 2 257 ? 102.232 87.127  119.630 1.00 22.99 ?  236 TYR C O     1 
ATOM   12909 C  CB    . TYR C 2 257 ? 104.224 84.663  118.384 1.00 22.81 ?  236 TYR C CB    1 
ATOM   12910 C  CG    . TYR C 2 257 ? 103.349 84.986  117.189 1.00 23.76 ?  236 TYR C CG    1 
ATOM   12911 C  CD1   . TYR C 2 257 ? 103.626 86.086  116.372 1.00 24.05 ?  236 TYR C CD1   1 
ATOM   12912 C  CD2   . TYR C 2 257 ? 102.240 84.201  116.886 1.00 24.04 ?  236 TYR C CD2   1 
ATOM   12913 C  CE1   . TYR C 2 257 ? 102.819 86.395  115.283 1.00 24.40 ?  236 TYR C CE1   1 
ATOM   12914 C  CE2   . TYR C 2 257 ? 101.428 84.501  115.793 1.00 26.30 ?  236 TYR C CE2   1 
ATOM   12915 C  CZ    . TYR C 2 257 ? 101.733 85.591  114.999 1.00 25.80 ?  236 TYR C CZ    1 
ATOM   12916 O  OH    . TYR C 2 257 ? 100.940 85.877  113.924 1.00 28.42 ?  236 TYR C OH    1 
ATOM   12917 N  N     . GLU C 2 258 ? 102.057 85.079  120.601 1.00 22.99 ?  237 GLU C N     1 
ATOM   12918 C  CA    . GLU C 2 258 ? 100.663 85.269  121.018 1.00 24.46 ?  237 GLU C CA    1 
ATOM   12919 C  C     . GLU C 2 258 ? 100.504 86.476  121.927 1.00 23.86 ?  237 GLU C C     1 
ATOM   12920 O  O     . GLU C 2 258 ? 99.554  87.246  121.782 1.00 24.01 ?  237 GLU C O     1 
ATOM   12921 C  CB    . GLU C 2 258 ? 100.086 84.000  121.671 1.00 25.21 ?  237 GLU C CB    1 
ATOM   12922 C  CG    . GLU C 2 258 ? 99.887  82.829  120.681 1.00 30.12 ?  237 GLU C CG    1 
ATOM   12923 C  CD    . GLU C 2 258 ? 98.820  83.115  119.620 1.00 35.29 ?  237 GLU C CD    1 
ATOM   12924 O  OE1   . GLU C 2 258 ? 97.872  83.885  119.895 1.00 37.71 ?  237 GLU C OE1   1 
ATOM   12925 O  OE2   . GLU C 2 258 ? 98.928  82.559  118.501 1.00 39.07 -1 237 GLU C OE2   1 
ATOM   12926 N  N     . ASN C 2 259 ? 101.453 86.659  122.844 1.00 23.25 ?  238 ASN C N     1 
ATOM   12927 C  CA    . ASN C 2 259 ? 101.474 87.844  123.697 1.00 23.10 ?  238 ASN C CA    1 
ATOM   12928 C  C     . ASN C 2 259 ? 101.722 89.128  122.882 1.00 22.68 ?  238 ASN C C     1 
ATOM   12929 O  O     . ASN C 2 259 ? 101.087 90.160  123.118 1.00 22.73 ?  238 ASN C O     1 
ATOM   12930 C  CB    . ASN C 2 259 ? 102.522 87.674  124.800 1.00 23.22 ?  238 ASN C CB    1 
ATOM   12931 C  CG    . ASN C 2 259 ? 102.569 88.855  125.747 1.00 24.46 ?  238 ASN C CG    1 
ATOM   12932 O  OD1   . ASN C 2 259 ? 101.647 89.074  126.538 1.00 26.28 ?  238 ASN C OD1   1 
ATOM   12933 N  ND2   . ASN C 2 259 ? 103.648 89.626  125.673 1.00 24.93 ?  238 ASN C ND2   1 
ATOM   12934 N  N     . GLU C 2 260 ? 102.624 89.053  121.906 1.00 22.64 ?  239 GLU C N     1 
ATOM   12935 C  CA    . GLU C 2 260 ? 102.959 90.219  121.086 1.00 23.18 ?  239 GLU C CA    1 
ATOM   12936 C  C     . GLU C 2 260 ? 101.771 90.672  120.221 1.00 23.40 ?  239 GLU C C     1 
ATOM   12937 O  O     . GLU C 2 260 ? 101.584 91.876  119.986 1.00 23.57 ?  239 GLU C O     1 
ATOM   12938 C  CB    . GLU C 2 260 ? 104.199 89.948  120.223 1.00 23.19 ?  239 GLU C CB    1 
ATOM   12939 C  CG    . GLU C 2 260 ? 105.007 91.218  119.863 1.00 24.33 ?  239 GLU C CG    1 
ATOM   12940 C  CD    . GLU C 2 260 ? 105.636 91.912  121.085 1.00 27.99 ?  239 GLU C CD    1 
ATOM   12941 O  OE1   . GLU C 2 260 ? 105.593 91.367  122.209 1.00 27.36 ?  239 GLU C OE1   1 
ATOM   12942 O  OE2   . GLU C 2 260 ? 106.175 93.029  120.920 1.00 28.98 -1 239 GLU C OE2   1 
ATOM   12943 N  N     . LEU C 2 261 ? 100.969 89.710  119.761 1.00 23.35 ?  240 LEU C N     1 
ATOM   12944 C  CA    . LEU C 2 261 ? 99.729  90.022  119.033 1.00 23.74 ?  240 LEU C CA    1 
ATOM   12945 C  C     . LEU C 2 261 ? 98.787  90.912  119.849 1.00 23.80 ?  240 LEU C C     1 
ATOM   12946 O  O     . LEU C 2 261 ? 98.279  91.929  119.348 1.00 23.33 ?  240 LEU C O     1 
ATOM   12947 C  CB    . LEU C 2 261 ? 98.998  88.744  118.615 1.00 24.09 ?  240 LEU C CB    1 
ATOM   12948 C  CG    . LEU C 2 261 ? 99.649  87.891  117.525 1.00 24.07 ?  240 LEU C CG    1 
ATOM   12949 C  CD1   . LEU C 2 261 ? 98.794  86.660  117.256 1.00 24.77 ?  240 LEU C CD1   1 
ATOM   12950 C  CD2   . LEU C 2 261 ? 99.865  88.707  116.235 1.00 24.38 ?  240 LEU C CD2   1 
ATOM   12951 N  N     . GLU C 2 262 ? 98.555  90.522  121.096 1.00 23.41 ?  241 GLU C N     1 
ATOM   12952 C  CA    . GLU C 2 262 ? 97.705  91.294  122.000 1.00 24.02 ?  241 GLU C CA    1 
ATOM   12953 C  C     . GLU C 2 262 ? 98.291  92.684  122.296 1.00 22.91 ?  241 GLU C C     1 
ATOM   12954 O  O     . GLU C 2 262 ? 97.562  93.667  122.321 1.00 22.94 ?  241 GLU C O     1 
ATOM   12955 C  CB    . GLU C 2 262 ? 97.487  90.518  123.300 1.00 24.92 ?  241 GLU C CB    1 
ATOM   12956 C  CG    . GLU C 2 262 ? 96.695  89.231  123.136 1.00 27.82 ?  241 GLU C CG    1 
ATOM   12957 C  CD    . GLU C 2 262 ? 96.480  88.514  124.457 1.00 33.08 ?  241 GLU C CD    1 
ATOM   12958 O  OE1   . GLU C 2 262 ? 97.396  87.796  124.920 1.00 36.94 ?  241 GLU C OE1   1 
ATOM   12959 O  OE2   . GLU C 2 262 ? 95.387  88.661  125.032 1.00 37.48 -1 241 GLU C OE2   1 
ATOM   12960 N  N     . TYR C 2 263 ? 99.604  92.745  122.526 1.00 21.84 ?  242 TYR C N     1 
ATOM   12961 C  CA    . TYR C 2 263 ? 100.332 93.999  122.709 1.00 21.66 ?  242 TYR C CA    1 
ATOM   12962 C  C     . TYR C 2 263 ? 100.189 94.895  121.486 1.00 21.28 ?  242 TYR C C     1 
ATOM   12963 O  O     . TYR C 2 263 ? 99.938  96.102  121.613 1.00 21.14 ?  242 TYR C O     1 
ATOM   12964 C  CB    . TYR C 2 263 ? 101.823 93.705  122.939 1.00 21.44 ?  242 TYR C CB    1 
ATOM   12965 C  CG    . TYR C 2 263 ? 102.718 94.915  123.172 1.00 21.89 ?  242 TYR C CG    1 
ATOM   12966 C  CD1   . TYR C 2 263 ? 102.635 95.654  124.353 1.00 22.52 ?  242 TYR C CD1   1 
ATOM   12967 C  CD2   . TYR C 2 263 ? 103.674 95.293  122.226 1.00 22.58 ?  242 TYR C CD2   1 
ATOM   12968 C  CE1   . TYR C 2 263 ? 103.471 96.748  124.579 1.00 22.67 ?  242 TYR C CE1   1 
ATOM   12969 C  CE2   . TYR C 2 263 ? 104.521 96.386  122.444 1.00 24.03 ?  242 TYR C CE2   1 
ATOM   12970 C  CZ    . TYR C 2 263 ? 104.415 97.100  123.632 1.00 23.75 ?  242 TYR C CZ    1 
ATOM   12971 O  OH    . TYR C 2 263 ? 105.236 98.186  123.866 1.00 26.82 ?  242 TYR C OH    1 
ATOM   12972 N  N     . THR C 2 264 ? 100.355 94.302  120.306 1.00 20.66 ?  243 THR C N     1 
ATOM   12973 C  CA    . THR C 2 264 ? 100.271 95.045  119.041 1.00 20.99 ?  243 THR C CA    1 
ATOM   12974 C  C     . THR C 2 264 ? 98.873  95.643  118.849 1.00 21.22 ?  243 THR C C     1 
ATOM   12975 O  O     . THR C 2 264 ? 98.739  96.831  118.516 1.00 20.95 ?  243 THR C O     1 
ATOM   12976 C  CB    . THR C 2 264 ? 100.661 94.148  117.834 1.00 20.58 ?  243 THR C CB    1 
ATOM   12977 O  OG1   . THR C 2 264 ? 102.041 93.790  117.945 1.00 20.84 ?  243 THR C OG1   1 
ATOM   12978 C  CG2   . THR C 2 264 ? 100.446 94.874  116.504 1.00 20.90 ?  243 THR C CG2   1 
ATOM   12979 N  N     . GLU C 2 265 ? 97.838  94.834  119.087 1.00 21.62 ?  244 GLU C N     1 
ATOM   12980 C  CA    . GLU C 2 265 ? 96.463  95.318  118.965 1.00 23.46 ?  244 GLU C CA    1 
ATOM   12981 C  C     . GLU C 2 265 ? 96.181  96.437  119.949 1.00 23.33 ?  244 GLU C C     1 
ATOM   12982 O  O     . GLU C 2 265 ? 95.567  97.447  119.605 1.00 22.86 ?  244 GLU C O     1 
ATOM   12983 C  CB    . GLU C 2 265 ? 95.449  94.189  119.154 1.00 24.31 ?  244 GLU C CB    1 
ATOM   12984 C  CG    . GLU C 2 265 ? 95.402  93.212  117.984 1.00 27.63 ?  244 GLU C CG    1 
ATOM   12985 C  CD    . GLU C 2 265 ? 94.377  92.100  118.190 1.00 33.27 ?  244 GLU C CD    1 
ATOM   12986 O  OE1   . GLU C 2 265 ? 93.356  92.338  118.874 1.00 35.56 ?  244 GLU C OE1   1 
ATOM   12987 O  OE2   . GLU C 2 265 ? 94.590  90.988  117.656 1.00 35.96 -1 244 GLU C OE2   1 
ATOM   12988 N  N     . ASP C 2 266 ? 96.645  96.252  121.176 1.00 23.36 ?  245 ASP C N     1 
ATOM   12989 C  CA    . ASP C 2 266 ? 96.467  97.250  122.216 1.00 24.18 ?  245 ASP C CA    1 
ATOM   12990 C  C     . ASP C 2 266 ? 97.064  98.616  121.826 1.00 23.96 ?  245 ASP C C     1 
ATOM   12991 O  O     . ASP C 2 266 ? 96.461  99.657  122.078 1.00 24.19 ?  245 ASP C O     1 
ATOM   12992 C  CB    . ASP C 2 266 ? 97.098  96.745  123.511 1.00 25.14 ?  245 ASP C CB    1 
ATOM   12993 C  CG    . ASP C 2 266 ? 96.745  97.598  124.691 1.00 27.35 ?  245 ASP C CG    1 
ATOM   12994 O  OD1   . ASP C 2 266 ? 95.537  97.784  124.948 1.00 28.45 ?  245 ASP C OD1   1 
ATOM   12995 O  OD2   . ASP C 2 266 ? 97.683  98.083  125.359 1.00 31.99 -1 245 ASP C OD2   1 
ATOM   12996 N  N     . LEU C 2 267 ? 98.232  98.605  121.196 1.00 23.34 ?  246 LEU C N     1 
ATOM   12997 C  CA    . LEU C 2 267 ? 98.902  99.851  120.809 1.00 23.53 ?  246 LEU C CA    1 
ATOM   12998 C  C     . LEU C 2 267 ? 98.435  100.439 119.486 1.00 22.94 ?  246 LEU C C     1 
ATOM   12999 O  O     . LEU C 2 267 ? 98.277  101.655 119.367 1.00 23.14 ?  246 LEU C O     1 
ATOM   13000 C  CB    . LEU C 2 267 ? 100.412 99.640  120.747 1.00 23.37 ?  246 LEU C CB    1 
ATOM   13001 C  CG    . LEU C 2 267 ? 101.152 99.469  122.075 1.00 26.17 ?  246 LEU C CG    1 
ATOM   13002 C  CD1   . LEU C 2 267 ? 102.626 99.298  121.782 1.00 27.31 ?  246 LEU C CD1   1 
ATOM   13003 C  CD2   . LEU C 2 267 ? 100.933 100.677 122.980 1.00 28.08 ?  246 LEU C CD2   1 
ATOM   13004 N  N     . TYR C 2 268 ? 98.242  99.578  118.491 1.00 22.46 ?  247 TYR C N     1 
ATOM   13005 C  CA    . TYR C 2 268 ? 98.032  100.041 117.122 1.00 22.00 ?  247 TYR C CA    1 
ATOM   13006 C  C     . TYR C 2 268 ? 96.601  100.173 116.629 1.00 22.26 ?  247 TYR C C     1 
ATOM   13007 O  O     . TYR C 2 268 ? 96.385  100.821 115.604 1.00 22.17 ?  247 TYR C O     1 
ATOM   13008 C  CB    . TYR C 2 268 ? 98.835  99.182  116.136 1.00 21.73 ?  247 TYR C CB    1 
ATOM   13009 C  CG    . TYR C 2 268 ? 100.325 99.414  116.211 1.00 21.49 ?  247 TYR C CG    1 
ATOM   13010 C  CD1   . TYR C 2 268 ? 101.153 98.527  116.905 1.00 19.45 ?  247 TYR C CD1   1 
ATOM   13011 C  CD2   . TYR C 2 268 ? 100.905 100.531 115.601 1.00 22.71 ?  247 TYR C CD2   1 
ATOM   13012 C  CE1   . TYR C 2 268 ? 102.532 98.745  116.984 1.00 20.30 ?  247 TYR C CE1   1 
ATOM   13013 C  CE2   . TYR C 2 268 ? 102.290 100.762 115.667 1.00 21.69 ?  247 TYR C CE2   1 
ATOM   13014 C  CZ    . TYR C 2 268 ? 103.090 99.857  116.348 1.00 21.40 ?  247 TYR C CZ    1 
ATOM   13015 O  OH    . TYR C 2 268 ? 104.442 100.076 116.406 1.00 22.11 ?  247 TYR C OH    1 
ATOM   13016 N  N     . ASP C 2 269 ? 95.629  99.558  117.311 1.00 22.40 ?  248 ASP C N     1 
ATOM   13017 C  CA    . ASP C 2 269 ? 94.226  99.692  116.879 1.00 22.75 ?  248 ASP C CA    1 
ATOM   13018 C  C     . ASP C 2 269 ? 93.795  101.157 116.783 1.00 22.55 ?  248 ASP C C     1 
ATOM   13019 O  O     . ASP C 2 269 ? 93.067  101.529 115.854 1.00 22.22 ?  248 ASP C O     1 
ATOM   13020 C  CB    . ASP C 2 269 ? 93.253  98.901  117.774 1.00 23.03 ?  248 ASP C CB    1 
ATOM   13021 C  CG    . ASP C 2 269 ? 93.198  97.423  117.426 1.00 25.02 ?  248 ASP C CG    1 
ATOM   13022 O  OD1   . ASP C 2 269 ? 93.742  97.009  116.380 1.00 26.85 ?  248 ASP C OD1   1 
ATOM   13023 O  OD2   . ASP C 2 269 ? 92.594  96.660  118.208 1.00 28.74 -1 248 ASP C OD2   1 
ATOM   13024 N  N     . GLN C 2 270 ? 94.255  101.985 117.725 1.00 22.21 ?  249 GLN C N     1 
ATOM   13025 C  CA    . GLN C 2 270 ? 93.880  103.418 117.728 1.00 22.39 ?  249 GLN C CA    1 
ATOM   13026 C  C     . GLN C 2 270 ? 94.484  104.237 116.579 1.00 21.65 ?  249 GLN C C     1 
ATOM   13027 O  O     . GLN C 2 270 ? 94.061  105.369 116.343 1.00 21.70 ?  249 GLN C O     1 
ATOM   13028 C  CB    . GLN C 2 270 ? 94.172  104.084 119.081 1.00 22.53 ?  249 GLN C CB    1 
ATOM   13029 C  CG    . GLN C 2 270 ? 95.659  104.105 119.518 1.00 22.73 ?  249 GLN C CG    1 
ATOM   13030 C  CD    . GLN C 2 270 ? 95.839  104.784 120.861 1.00 25.39 ?  249 GLN C CD    1 
ATOM   13031 O  OE1   . GLN C 2 270 ? 94.875  104.970 121.605 1.00 27.88 ?  249 GLN C OE1   1 
ATOM   13032 N  NE2   . GLN C 2 270 ? 97.072  105.168 121.179 1.00 24.88 ?  249 GLN C NE2   1 
ATOM   13033 N  N     . VAL C 2 271 ? 95.466  103.667 115.877 1.00 20.91 ?  250 VAL C N     1 
ATOM   13034 C  CA    . VAL C 2 271 ? 96.078  104.328 114.701 1.00 20.62 ?  250 VAL C CA    1 
ATOM   13035 C  C     . VAL C 2 271 ? 95.841  103.533 113.404 1.00 20.53 ?  250 VAL C C     1 
ATOM   13036 O  O     . VAL C 2 271 ? 96.308  103.923 112.321 1.00 20.05 ?  250 VAL C O     1 
ATOM   13037 C  CB    . VAL C 2 271 ? 97.600  104.674 114.909 1.00 20.32 ?  250 VAL C CB    1 
ATOM   13038 C  CG1   . VAL C 2 271 ? 97.778  105.699 116.024 1.00 20.35 ?  250 VAL C CG1   1 
ATOM   13039 C  CG2   . VAL C 2 271 ? 98.445  103.425 115.205 1.00 19.32 ?  250 VAL C CG2   1 
ATOM   13040 N  N     . GLY C 2 272 ? 95.105  102.427 113.527 1.00 20.29 ?  251 GLY C N     1 
ATOM   13041 C  CA    . GLY C 2 272 ? 94.630  101.659 112.373 1.00 20.51 ?  251 GLY C CA    1 
ATOM   13042 C  C     . GLY C 2 272 ? 95.648  100.745 111.709 1.00 20.99 ?  251 GLY C C     1 
ATOM   13043 O  O     . GLY C 2 272 ? 95.481  100.373 110.536 1.00 20.22 ?  251 GLY C O     1 
ATOM   13044 N  N     . LEU C 2 273 ? 96.703  100.379 112.444 1.00 20.76 ?  252 LEU C N     1 
ATOM   13045 C  CA    . LEU C 2 273 ? 97.846  99.705  111.821 1.00 21.38 ?  252 LEU C CA    1 
ATOM   13046 C  C     . LEU C 2 273 ? 98.140  98.288  112.307 1.00 21.86 ?  252 LEU C C     1 
ATOM   13047 O  O     . LEU C 2 273 ? 99.140  97.695  111.904 1.00 22.45 ?  252 LEU C O     1 
ATOM   13048 C  CB    . LEU C 2 273 ? 99.111  100.575 111.922 1.00 21.44 ?  252 LEU C CB    1 
ATOM   13049 C  CG    . LEU C 2 273 ? 99.089  101.978 111.312 1.00 22.02 ?  252 LEU C CG    1 
ATOM   13050 C  CD1   . LEU C 2 273 ? 100.414 102.678 111.597 1.00 22.86 ?  252 LEU C CD1   1 
ATOM   13051 C  CD2   . LEU C 2 273 ? 98.803  101.926 109.795 1.00 23.88 ?  252 LEU C CD2   1 
ATOM   13052 N  N     . SER C 2 274 ? 97.270  97.730  113.147 1.00 22.19 ?  253 SER C N     1 
ATOM   13053 C  CA    . SER C 2 274 ? 97.583  96.482  113.838 1.00 22.47 ?  253 SER C CA    1 
ATOM   13054 C  C     . SER C 2 274 ? 97.905  95.326  112.890 1.00 22.94 ?  253 SER C C     1 
ATOM   13055 O  O     . SER C 2 274 ? 98.877  94.607  113.095 1.00 22.07 ?  253 SER C O     1 
ATOM   13056 C  CB    . SER C 2 274 ? 96.444  96.092  114.785 1.00 22.91 ?  253 SER C CB    1 
ATOM   13057 O  OG    . SER C 2 274 ? 96.378  97.014  115.855 1.00 24.25 ?  253 SER C OG    1 
ATOM   13058 N  N     . HIS C 2 275 ? 97.108  95.180  111.834 1.00 24.59 ?  254 HIS C N     1 
ATOM   13059 C  CA    . HIS C 2 275 ? 97.301  94.094  110.867 1.00 25.66 ?  254 HIS C CA    1 
ATOM   13060 C  C     . HIS C 2 275 ? 98.649  94.208  110.136 1.00 26.01 ?  254 HIS C C     1 
ATOM   13061 O  O     . HIS C 2 275 ? 99.339  93.200  109.903 1.00 26.23 ?  254 HIS C O     1 
ATOM   13062 C  CB    . HIS C 2 275 ? 96.141  94.064  109.863 1.00 26.89 ?  254 HIS C CB    1 
ATOM   13063 C  CG    . HIS C 2 275 ? 96.207  92.921  108.899 1.00 29.10 ?  254 HIS C CG    1 
ATOM   13064 N  ND1   . HIS C 2 275 ? 96.313  91.607  109.306 1.00 32.70 ?  254 HIS C ND1   1 
ATOM   13065 C  CD2   . HIS C 2 275 ? 96.179  92.892  107.546 1.00 31.68 ?  254 HIS C CD2   1 
ATOM   13066 C  CE1   . HIS C 2 275 ? 96.352  90.820  108.246 1.00 33.55 ?  254 HIS C CE1   1 
ATOM   13067 N  NE2   . HIS C 2 275 ? 96.256  91.574  107.166 1.00 33.71 ?  254 HIS C NE2   1 
ATOM   13068 N  N     . ASP C 2 276 ? 99.010  95.435  109.778 1.00 25.93 ?  255 ASP C N     1 
ATOM   13069 C  CA    . ASP C 2 276 ? 100.283 95.719  109.124 1.00 26.65 ?  255 ASP C CA    1 
ATOM   13070 C  C     . ASP C 2 276 ? 101.480 95.379  110.015 1.00 25.61 ?  255 ASP C C     1 
ATOM   13071 O  O     . ASP C 2 276 ? 102.436 94.742  109.554 1.00 25.34 ?  255 ASP C O     1 
ATOM   13072 C  CB    . ASP C 2 276 ? 100.348 97.185  108.690 1.00 27.44 ?  255 ASP C CB    1 
ATOM   13073 C  CG    . ASP C 2 276 ? 100.354 97.341  107.186 1.00 32.09 ?  255 ASP C CG    1 
ATOM   13074 O  OD1   . ASP C 2 276 ? 101.096 96.584  106.513 1.00 36.67 ?  255 ASP C OD1   1 
ATOM   13075 O  OD2   . ASP C 2 276 ? 99.610  98.208  106.670 1.00 36.30 -1 255 ASP C OD2   1 
ATOM   13076 N  N     . VAL C 2 277 ? 101.414 95.805  111.281 1.00 24.17 ?  256 VAL C N     1 
ATOM   13077 C  CA    . VAL C 2 277 ? 102.470 95.514  112.260 1.00 23.71 ?  256 VAL C CA    1 
ATOM   13078 C  C     . VAL C 2 277 ? 102.613 94.005  112.475 1.00 23.48 ?  256 VAL C C     1 
ATOM   13079 O  O     . VAL C 2 277 ? 103.729 93.491  112.562 1.00 23.08 ?  256 VAL C O     1 
ATOM   13080 C  CB    . VAL C 2 277 ? 102.223 96.211  113.627 1.00 23.27 ?  256 VAL C CB    1 
ATOM   13081 C  CG1   . VAL C 2 277 ? 103.346 95.887  114.617 1.00 24.02 ?  256 VAL C CG1   1 
ATOM   13082 C  CG2   . VAL C 2 277 ? 102.095 97.719  113.457 1.00 23.35 ?  256 VAL C CG2   1 
ATOM   13083 N  N     . LYS C 2 278 ? 101.486 93.303  112.560 1.00 23.36 ?  257 LYS C N     1 
ATOM   13084 C  CA    . LYS C 2 278 ? 101.492 91.849  112.714 1.00 24.12 ?  257 LYS C CA    1 
ATOM   13085 C  C     . LYS C 2 278 ? 102.260 91.140  111.601 1.00 24.30 ?  257 LYS C C     1 
ATOM   13086 O  O     . LYS C 2 278 ? 103.010 90.188  111.859 1.00 24.37 ?  257 LYS C O     1 
ATOM   13087 C  CB    . LYS C 2 278 ? 100.069 91.298  112.807 1.00 24.22 ?  257 LYS C CB    1 
ATOM   13088 C  CG    . LYS C 2 278 ? 99.386  91.572  114.136 1.00 24.96 ?  257 LYS C CG    1 
ATOM   13089 C  CD    . LYS C 2 278 ? 97.936  91.115  114.067 1.00 26.34 ?  257 LYS C CD    1 
ATOM   13090 C  CE    . LYS C 2 278 ? 97.203  91.404  115.348 1.00 27.16 ?  257 LYS C CE    1 
ATOM   13091 N  NZ    . LYS C 2 278 ? 95.794  90.925  115.218 1.00 29.60 1  257 LYS C NZ    1 
ATOM   13092 N  N     . LYS C 2 279 ? 102.081 91.604  110.365 1.00 24.55 ?  258 LYS C N     1 
ATOM   13093 C  CA    . LYS C 2 279 ? 102.837 91.059  109.241 1.00 24.85 ?  258 LYS C CA    1 
ATOM   13094 C  C     . LYS C 2 279 ? 104.333 91.298  109.438 1.00 24.57 ?  258 LYS C C     1 
ATOM   13095 O  O     . LYS C 2 279 ? 105.144 90.416  109.160 1.00 24.07 ?  258 LYS C O     1 
ATOM   13096 C  CB    . LYS C 2 279 ? 102.376 91.682  107.924 1.00 25.30 ?  258 LYS C CB    1 
ATOM   13097 C  CG    . LYS C 2 279 ? 100.924 91.418  107.592 1.00 26.63 ?  258 LYS C CG    1 
ATOM   13098 C  CD    . LYS C 2 279 ? 100.575 92.087  106.269 1.00 29.30 ?  258 LYS C CD    1 
ATOM   13099 C  CE    . LYS C 2 279 ? 99.190  91.715  105.833 1.00 31.79 ?  258 LYS C CE    1 
ATOM   13100 N  NZ    . LYS C 2 279 ? 98.751  92.633  104.752 1.00 33.80 1  258 LYS C NZ    1 
ATOM   13101 N  N     . PHE C 2 280 ? 104.679 92.482  109.946 1.00 24.29 ?  259 PHE C N     1 
ATOM   13102 C  CA    . PHE C 2 280 ? 106.076 92.868  110.182 1.00 24.90 ?  259 PHE C CA    1 
ATOM   13103 C  C     . PHE C 2 280 ? 106.749 91.998  111.260 1.00 24.86 ?  259 PHE C C     1 
ATOM   13104 O  O     . PHE C 2 280 ? 107.894 91.565  111.093 1.00 24.68 ?  259 PHE C O     1 
ATOM   13105 C  CB    . PHE C 2 280 ? 106.138 94.361  110.538 1.00 24.70 ?  259 PHE C CB    1 
ATOM   13106 C  CG    . PHE C 2 280 ? 107.530 94.947  110.574 1.00 25.70 ?  259 PHE C CG    1 
ATOM   13107 C  CD1   . PHE C 2 280 ? 108.355 94.913  109.449 1.00 26.86 ?  259 PHE C CD1   1 
ATOM   13108 C  CD2   . PHE C 2 280 ? 108.000 95.581  111.732 1.00 26.19 ?  259 PHE C CD2   1 
ATOM   13109 C  CE1   . PHE C 2 280 ? 109.638 95.479  109.476 1.00 26.66 ?  259 PHE C CE1   1 
ATOM   13110 C  CE2   . PHE C 2 280 ? 109.274 96.155  111.767 1.00 26.52 ?  259 PHE C CE2   1 
ATOM   13111 C  CZ    . PHE C 2 280 ? 110.098 96.099  110.635 1.00 26.23 ?  259 PHE C CZ    1 
ATOM   13112 N  N     . ILE C 2 281 ? 106.034 91.737  112.355 1.00 25.53 ?  260 ILE C N     1 
ATOM   13113 C  CA    . ILE C 2 281 ? 106.596 90.921  113.434 1.00 26.21 ?  260 ILE C CA    1 
ATOM   13114 C  C     . ILE C 2 281 ? 106.776 89.455  113.016 1.00 26.47 ?  260 ILE C C     1 
ATOM   13115 O  O     . ILE C 2 281 ? 107.732 88.810  113.436 1.00 26.52 ?  260 ILE C O     1 
ATOM   13116 C  CB    . ILE C 2 281 ? 105.842 91.077  114.800 1.00 26.27 ?  260 ILE C CB    1 
ATOM   13117 C  CG1   . ILE C 2 281 ? 104.537 90.278  114.830 1.00 27.37 ?  260 ILE C CG1   1 
ATOM   13118 C  CG2   . ILE C 2 281 ? 105.630 92.571  115.134 1.00 26.92 ?  260 ILE C CG2   1 
ATOM   13119 C  CD1   . ILE C 2 281 ? 103.794 90.337  116.166 1.00 29.51 ?  260 ILE C CD1   1 
ATOM   13120 N  N     . ARG C 2 282 ? 105.886 88.952  112.158 1.00 26.57 ?  261 ARG C N     1 
ATOM   13121 C  CA    . ARG C 2 282 ? 106.032 87.597  111.617 1.00 26.84 ?  261 ARG C CA    1 
ATOM   13122 C  C     . ARG C 2 282 ? 107.265 87.498  110.719 1.00 27.34 ?  261 ARG C C     1 
ATOM   13123 O  O     . ARG C 2 282 ? 108.030 86.542  110.815 1.00 27.54 ?  261 ARG C O     1 
ATOM   13124 C  CB    . ARG C 2 282 ? 104.773 87.148  110.871 1.00 26.98 ?  261 ARG C CB    1 
ATOM   13125 C  CG    . ARG C 2 282 ? 103.644 86.685  111.770 1.00 26.53 ?  261 ARG C CG    1 
ATOM   13126 C  CD    . ARG C 2 282 ? 102.529 85.981  110.970 1.00 27.77 ?  261 ARG C CD    1 
ATOM   13127 N  NE    . ARG C 2 282 ? 101.771 86.900  110.125 1.00 28.67 ?  261 ARG C NE    1 
ATOM   13128 C  CZ    . ARG C 2 282 ? 100.727 87.622  110.537 1.00 29.68 ?  261 ARG C CZ    1 
ATOM   13129 N  NH1   . ARG C 2 282 ? 100.296 87.542  111.795 1.00 28.31 1  261 ARG C NH1   1 
ATOM   13130 N  NH2   . ARG C 2 282 ? 100.104 88.421  109.686 1.00 29.15 ?  261 ARG C NH2   1 
ATOM   13131 N  N     . TYR C 2 283 ? 107.446 88.501  109.863 1.00 27.78 ?  262 TYR C N     1 
ATOM   13132 C  CA    . TYR C 2 283 ? 108.640 88.641  109.032 1.00 28.18 ?  262 TYR C CA    1 
ATOM   13133 C  C     . TYR C 2 283 ? 109.922 88.563  109.881 1.00 27.08 ?  262 TYR C C     1 
ATOM   13134 O  O     . TYR C 2 283 ? 110.851 87.796  109.581 1.00 26.51 ?  262 TYR C O     1 
ATOM   13135 C  CB    . TYR C 2 283 ? 108.579 89.976  108.279 1.00 29.11 ?  262 TYR C CB    1 
ATOM   13136 C  CG    . TYR C 2 283 ? 109.748 90.242  107.362 1.00 32.56 ?  262 TYR C CG    1 
ATOM   13137 C  CD1   . TYR C 2 283 ? 109.855 89.589  106.133 1.00 36.59 ?  262 TYR C CD1   1 
ATOM   13138 C  CD2   . TYR C 2 283 ? 110.743 91.160  107.714 1.00 36.34 ?  262 TYR C CD2   1 
ATOM   13139 C  CE1   . TYR C 2 283 ? 110.931 89.832  105.274 1.00 39.47 ?  262 TYR C CE1   1 
ATOM   13140 C  CE2   . TYR C 2 283 ? 111.828 91.417  106.854 1.00 39.23 ?  262 TYR C CE2   1 
ATOM   13141 C  CZ    . TYR C 2 283 ? 111.910 90.744  105.639 1.00 40.48 ?  262 TYR C CZ    1 
ATOM   13142 O  OH    . TYR C 2 283 ? 112.965 90.977  104.785 1.00 44.00 ?  262 TYR C OH    1 
ATOM   13143 N  N     . ASN C 2 284 ? 109.953 89.339  110.955 1.00 26.08 ?  263 ASN C N     1 
ATOM   13144 C  CA    . ASN C 2 284 ? 111.113 89.360  111.833 1.00 25.73 ?  263 ASN C CA    1 
ATOM   13145 C  C     . ASN C 2 284 ? 111.278 88.119  112.713 1.00 25.24 ?  263 ASN C C     1 
ATOM   13146 O  O     . ASN C 2 284 ? 112.413 87.721  113.007 1.00 25.56 ?  263 ASN C O     1 
ATOM   13147 C  CB    . ASN C 2 284 ? 111.151 90.664  112.630 1.00 25.69 ?  263 ASN C CB    1 
ATOM   13148 C  CG    . ASN C 2 284 ? 111.581 91.835  111.777 1.00 26.39 ?  263 ASN C CG    1 
ATOM   13149 O  OD1   . ASN C 2 284 ? 112.764 91.985  111.459 1.00 26.91 ?  263 ASN C OD1   1 
ATOM   13150 N  ND2   . ASN C 2 284 ? 110.626 92.669  111.390 1.00 27.56 ?  263 ASN C ND2   1 
ATOM   13151 N  N     . ALA C 2 285 ? 110.168 87.489  113.106 1.00 24.51 ?  264 ALA C N     1 
ATOM   13152 C  CA    . ALA C 2 285 ? 110.233 86.165  113.754 1.00 24.19 ?  264 ALA C CA    1 
ATOM   13153 C  C     . ALA C 2 285 ? 111.017 85.143  112.907 1.00 24.63 ?  264 ALA C C     1 
ATOM   13154 O  O     . ALA C 2 285 ? 111.834 84.390  113.434 1.00 24.01 ?  264 ALA C O     1 
ATOM   13155 C  CB    . ALA C 2 285 ? 108.845 85.633  114.059 1.00 23.63 ?  264 ALA C CB    1 
ATOM   13156 N  N     . ASN C 2 286 ? 110.763 85.128  111.599 1.00 24.66 ?  265 ASN C N     1 
ATOM   13157 C  CA    . ASN C 2 286 ? 111.513 84.274  110.678 1.00 25.24 ?  265 ASN C CA    1 
ATOM   13158 C  C     . ASN C 2 286 ? 113.010 84.562  110.644 1.00 25.09 ?  265 ASN C C     1 
ATOM   13159 O  O     . ASN C 2 286 ? 113.816 83.627  110.512 1.00 24.14 ?  265 ASN C O     1 
ATOM   13160 C  CB    . ASN C 2 286 ? 110.935 84.346  109.252 1.00 25.62 ?  265 ASN C CB    1 
ATOM   13161 C  CG    . ASN C 2 286 ? 109.624 83.588  109.118 1.00 26.46 ?  265 ASN C CG    1 
ATOM   13162 O  OD1   . ASN C 2 286 ? 109.239 82.822  110.005 1.00 27.14 ?  265 ASN C OD1   1 
ATOM   13163 N  ND2   . ASN C 2 286 ? 108.919 83.813  108.007 1.00 27.89 ?  265 ASN C ND2   1 
ATOM   13164 N  N     . LYS C 2 287 ? 113.366 85.846  110.745 1.00 24.99 ?  266 LYS C N     1 
ATOM   13165 C  CA    . LYS C 2 287 ? 114.762 86.282  110.816 1.00 25.91 ?  266 LYS C CA    1 
ATOM   13166 C  C     . LYS C 2 287 ? 115.416 85.821  112.115 1.00 25.23 ?  266 LYS C C     1 
ATOM   13167 O  O     . LYS C 2 287 ? 116.580 85.415  112.115 1.00 25.34 ?  266 LYS C O     1 
ATOM   13168 C  CB    . LYS C 2 287 ? 114.880 87.804  110.726 1.00 25.96 ?  266 LYS C CB    1 
ATOM   13169 C  CG    . LYS C 2 287 ? 114.668 88.404  109.345 1.00 29.60 ?  266 LYS C CG    1 
ATOM   13170 C  CD    . LYS C 2 287 ? 115.080 89.882  109.381 1.00 34.20 ?  266 LYS C CD    1 
ATOM   13171 C  CE    . LYS C 2 287 ? 114.997 90.538  108.025 1.00 37.67 ?  266 LYS C CE    1 
ATOM   13172 N  NZ    . LYS C 2 287 ? 115.544 91.933  108.097 1.00 39.48 1  266 LYS C NZ    1 
ATOM   13173 N  N     . ALA C 2 288 ? 114.674 85.899  113.217 1.00 24.87 ?  267 ALA C N     1 
ATOM   13174 C  CA    . ALA C 2 288 ? 115.155 85.374  114.509 1.00 24.23 ?  267 ALA C CA    1 
ATOM   13175 C  C     . ALA C 2 288 ? 115.416 83.863  114.436 1.00 24.24 ?  267 ALA C C     1 
ATOM   13176 O  O     . ALA C 2 288 ? 116.465 83.388  114.875 1.00 23.96 ?  267 ALA C O     1 
ATOM   13177 C  CB    . ALA C 2 288 ? 114.170 85.692  115.618 1.00 24.23 ?  267 ALA C CB    1 
ATOM   13178 N  N     . LEU C 2 289 ? 114.467 83.113  113.878 1.00 24.63 ?  268 LEU C N     1 
ATOM   13179 C  CA    . LEU C 2 289 ? 114.657 81.673  113.686 1.00 25.14 ?  268 LEU C CA    1 
ATOM   13180 C  C     . LEU C 2 289 ? 115.889 81.403  112.837 1.00 25.58 ?  268 LEU C C     1 
ATOM   13181 O  O     . LEU C 2 289 ? 116.691 80.536  113.166 1.00 25.42 ?  268 LEU C O     1 
ATOM   13182 C  CB    . LEU C 2 289 ? 113.419 81.008  113.064 1.00 25.28 ?  268 LEU C CB    1 
ATOM   13183 C  CG    . LEU C 2 289 ? 112.221 80.844  114.005 1.00 25.93 ?  268 LEU C CG    1 
ATOM   13184 C  CD1   . LEU C 2 289 ? 110.945 80.616  113.220 1.00 26.50 ?  268 LEU C CD1   1 
ATOM   13185 C  CD2   . LEU C 2 289 ? 112.443 79.735  115.051 1.00 25.20 ?  268 LEU C CD2   1 
ATOM   13186 N  N     . MET C 2 290 ? 116.050 82.162  111.753 1.00 26.32 ?  269 MET C N     1 
ATOM   13187 C  CA    . MET C 2 290 ? 117.215 81.980  110.892 1.00 27.41 ?  269 MET C CA    1 
ATOM   13188 C  C     . MET C 2 290 ? 118.532 82.277  111.605 1.00 26.66 ?  269 MET C C     1 
ATOM   13189 O  O     . MET C 2 290 ? 119.518 81.566  111.396 1.00 26.69 ?  269 MET C O     1 
ATOM   13190 C  CB    . MET C 2 290 ? 117.073 82.768  109.595 1.00 28.28 ?  269 MET C CB    1 
ATOM   13191 C  CG    . MET C 2 290 ? 116.407 81.931  108.503 1.00 32.91 ?  269 MET C CG    1 
ATOM   13192 S  SD    . MET C 2 290 ? 115.909 82.902  107.077 1.00 42.49 ?  269 MET C SD    1 
ATOM   13193 C  CE    . MET C 2 290 ? 114.131 82.950  107.296 1.00 38.74 ?  269 MET C CE    1 
ATOM   13194 N  N     . ASN C 2 291 ? 118.536 83.296  112.465 1.00 25.48 ?  270 ASN C N     1 
ATOM   13195 C  CA    . ASN C 2 291 ? 119.706 83.619  113.298 1.00 25.39 ?  270 ASN C CA    1 
ATOM   13196 C  C     . ASN C 2 291 ? 120.098 82.455  114.223 1.00 25.18 ?  270 ASN C C     1 
ATOM   13197 O  O     . ASN C 2 291 ? 121.270 82.310  114.602 1.00 24.73 ?  270 ASN C O     1 
ATOM   13198 C  CB    . ASN C 2 291 ? 119.456 84.892  114.117 1.00 24.83 ?  270 ASN C CB    1 
ATOM   13199 C  CG    . ASN C 2 291 ? 119.539 86.168  113.270 1.00 25.58 ?  270 ASN C CG    1 
ATOM   13200 O  OD1   . ASN C 2 291 ? 120.010 86.151  112.138 1.00 25.58 ?  270 ASN C OD1   1 
ATOM   13201 N  ND2   . ASN C 2 291 ? 119.077 87.275  113.830 1.00 24.32 ?  270 ASN C ND2   1 
ATOM   13202 N  N     . LEU C 2 292 ? 119.104 81.623  114.548 1.00 25.09 ?  271 LEU C N     1 
ATOM   13203 C  CA    . LEU C 2 292 ? 119.279 80.410  115.359 1.00 25.46 ?  271 LEU C CA    1 
ATOM   13204 C  C     . LEU C 2 292 ? 119.548 79.135  114.543 1.00 26.18 ?  271 LEU C C     1 
ATOM   13205 O  O     . LEU C 2 292 ? 119.688 78.034  115.107 1.00 26.06 ?  271 LEU C O     1 
ATOM   13206 C  CB    . LEU C 2 292 ? 118.059 80.221  116.270 1.00 25.19 ?  271 LEU C CB    1 
ATOM   13207 C  CG    . LEU C 2 292 ? 117.865 81.300  117.349 1.00 25.03 ?  271 LEU C CG    1 
ATOM   13208 C  CD1   . LEU C 2 292 ? 116.494 81.182  117.976 1.00 24.50 ?  271 LEU C CD1   1 
ATOM   13209 C  CD2   . LEU C 2 292 ? 118.968 81.199  118.415 1.00 25.64 ?  271 LEU C CD2   1 
ATOM   13210 N  N     . GLY C 2 293 ? 119.626 79.282  113.221 1.00 26.71 ?  272 GLY C N     1 
ATOM   13211 C  CA    . GLY C 2 293 ? 119.862 78.147  112.321 1.00 28.06 ?  272 GLY C CA    1 
ATOM   13212 C  C     . GLY C 2 293 ? 118.643 77.280  112.046 1.00 29.34 ?  272 GLY C C     1 
ATOM   13213 O  O     . GLY C 2 293 ? 118.777 76.110  111.657 1.00 29.73 ?  272 GLY C O     1 
ATOM   13214 N  N     . PHE C 2 294 ? 117.454 77.846  112.246 1.00 29.88 ?  273 PHE C N     1 
ATOM   13215 C  CA    . PHE C 2 294 ? 116.199 77.132  112.030 1.00 31.24 ?  273 PHE C CA    1 
ATOM   13216 C  C     . PHE C 2 294 ? 115.471 77.653  110.783 1.00 32.42 ?  273 PHE C C     1 
ATOM   13217 O  O     . PHE C 2 294 ? 115.702 78.787  110.341 1.00 32.30 ?  273 PHE C O     1 
ATOM   13218 C  CB    . PHE C 2 294 ? 115.290 77.235  113.261 1.00 30.82 ?  273 PHE C CB    1 
ATOM   13219 C  CG    . PHE C 2 294 ? 115.886 76.646  114.523 1.00 30.93 ?  273 PHE C CG    1 
ATOM   13220 C  CD1   . PHE C 2 294 ? 116.462 75.376  114.523 1.00 30.85 ?  273 PHE C CD1   1 
ATOM   13221 C  CD2   . PHE C 2 294 ? 115.856 77.359  115.712 1.00 30.30 ?  273 PHE C CD2   1 
ATOM   13222 C  CE1   . PHE C 2 294 ? 117.014 74.840  115.685 1.00 30.75 ?  273 PHE C CE1   1 
ATOM   13223 C  CE2   . PHE C 2 294 ? 116.391 76.827  116.888 1.00 30.41 ?  273 PHE C CE2   1 
ATOM   13224 C  CZ    . PHE C 2 294 ? 116.967 75.563  116.875 1.00 30.88 ?  273 PHE C CZ    1 
ATOM   13225 N  N     . ASP C 2 295 ? 114.609 76.810  110.217 1.00 33.81 ?  274 ASP C N     1 
ATOM   13226 C  CA    . ASP C 2 295 ? 113.784 77.178  109.062 1.00 35.32 ?  274 ASP C CA    1 
ATOM   13227 C  C     . ASP C 2 295 ? 112.718 78.223  109.436 1.00 35.36 ?  274 ASP C C     1 
ATOM   13228 O  O     . ASP C 2 295 ? 112.232 78.226  110.564 1.00 34.78 ?  274 ASP C O     1 
ATOM   13229 C  CB    . ASP C 2 295 ? 113.086 75.935  108.495 1.00 35.95 ?  274 ASP C CB    1 
ATOM   13230 C  CG    . ASP C 2 295 ? 114.062 74.899  107.945 1.00 37.98 ?  274 ASP C CG    1 
ATOM   13231 O  OD1   . ASP C 2 295 ? 115.177 75.265  107.513 1.00 39.83 ?  274 ASP C OD1   1 
ATOM   13232 O  OD2   . ASP C 2 295 ? 113.701 73.702  107.945 1.00 40.03 -1 274 ASP C OD2   1 
ATOM   13233 N  N     . PRO C 2 296 ? 112.346 79.105  108.487 1.00 36.33 ?  275 PRO C N     1 
ATOM   13234 C  CA    . PRO C 2 296 ? 111.237 80.053  108.729 1.00 36.92 ?  275 PRO C CA    1 
ATOM   13235 C  C     . PRO C 2 296 ? 109.927 79.350  109.120 1.00 37.68 ?  275 PRO C C     1 
ATOM   13236 O  O     . PRO C 2 296 ? 109.637 78.261  108.616 1.00 38.07 ?  275 PRO C O     1 
ATOM   13237 C  CB    . PRO C 2 296 ? 111.082 80.775  107.381 1.00 36.82 ?  275 PRO C CB    1 
ATOM   13238 C  CG    . PRO C 2 296 ? 111.882 79.952  106.381 1.00 37.42 ?  275 PRO C CG    1 
ATOM   13239 C  CD    . PRO C 2 296 ? 112.980 79.323  107.174 1.00 36.41 ?  275 PRO C CD    1 
ATOM   13240 N  N     . TYR C 2 297 ? 109.153 79.971  110.010 1.00 38.10 ?  276 TYR C N     1 
ATOM   13241 C  CA    . TYR C 2 297 ? 107.941 79.361  110.576 1.00 38.96 ?  276 TYR C CA    1 
ATOM   13242 C  C     . TYR C 2 297 ? 106.650 79.981  110.027 1.00 39.71 ?  276 TYR C C     1 
ATOM   13243 O  O     . TYR C 2 297 ? 105.611 79.315  109.965 1.00 40.18 ?  276 TYR C O     1 
ATOM   13244 C  CB    . TYR C 2 297 ? 107.977 79.496  112.102 1.00 38.94 ?  276 TYR C CB    1 
ATOM   13245 C  CG    . TYR C 2 297 ? 106.863 78.835  112.887 1.00 39.64 ?  276 TYR C CG    1 
ATOM   13246 C  CD1   . TYR C 2 297 ? 106.906 77.472  113.194 1.00 40.43 ?  276 TYR C CD1   1 
ATOM   13247 C  CD2   . TYR C 2 297 ? 105.798 79.582  113.378 1.00 41.04 ?  276 TYR C CD2   1 
ATOM   13248 C  CE1   . TYR C 2 297 ? 105.890 76.867  113.935 1.00 41.69 ?  276 TYR C CE1   1 
ATOM   13249 C  CE2   . TYR C 2 297 ? 104.775 78.990  114.119 1.00 41.60 ?  276 TYR C CE2   1 
ATOM   13250 C  CZ    . TYR C 2 297 ? 104.830 77.635  114.398 1.00 41.92 ?  276 TYR C CZ    1 
ATOM   13251 O  OH    . TYR C 2 297 ? 103.822 77.056  115.138 1.00 42.52 ?  276 TYR C OH    1 
ATOM   13252 N  N     . PHE C 2 298 ? 106.711 81.251  109.645 1.00 39.85 ?  277 PHE C N     1 
ATOM   13253 C  CA    . PHE C 2 298 ? 105.538 81.944  109.123 1.00 40.77 ?  277 PHE C CA    1 
ATOM   13254 C  C     . PHE C 2 298 ? 105.647 82.121  107.616 1.00 41.95 ?  277 PHE C C     1 
ATOM   13255 O  O     . PHE C 2 298 ? 106.749 82.250  107.086 1.00 41.91 ?  277 PHE C O     1 
ATOM   13256 C  CB    . PHE C 2 298 ? 105.372 83.306  109.805 1.00 39.94 ?  277 PHE C CB    1 
ATOM   13257 C  CG    . PHE C 2 298 ? 105.119 83.222  111.285 1.00 39.09 ?  277 PHE C CG    1 
ATOM   13258 C  CD1   . PHE C 2 298 ? 106.113 83.562  112.194 1.00 37.84 ?  277 PHE C CD1   1 
ATOM   13259 C  CD2   . PHE C 2 298 ? 103.878 82.817  111.772 1.00 38.97 ?  277 PHE C CD2   1 
ATOM   13260 C  CE1   . PHE C 2 298 ? 105.886 83.494  113.566 1.00 37.46 ?  277 PHE C CE1   1 
ATOM   13261 C  CE2   . PHE C 2 298 ? 103.638 82.744  113.139 1.00 38.20 ?  277 PHE C CE2   1 
ATOM   13262 C  CZ    . PHE C 2 298 ? 104.645 83.084  114.040 1.00 37.91 ?  277 PHE C CZ    1 
ATOM   13263 N  N     . GLU C 2 299 ? 104.510 82.122  106.921 1.00 43.74 ?  278 GLU C N     1 
ATOM   13264 C  CA    . GLU C 2 299 ? 104.521 82.336  105.470 1.00 45.61 ?  278 GLU C CA    1 
ATOM   13265 C  C     . GLU C 2 299 ? 104.832 83.797  105.143 1.00 46.04 ?  278 GLU C C     1 
ATOM   13266 O  O     . GLU C 2 299 ? 104.505 84.699  105.915 1.00 45.88 ?  278 GLU C O     1 
ATOM   13267 C  CB    . GLU C 2 299 ? 103.198 81.913  104.821 1.00 46.43 ?  278 GLU C CB    1 
ATOM   13268 C  CG    . GLU C 2 299 ? 103.363 81.408  103.377 1.00 48.82 ?  278 GLU C CG    1 
ATOM   13269 C  CD    . GLU C 2 299 ? 102.078 81.460  102.564 1.00 51.86 ?  278 GLU C CD    1 
ATOM   13270 O  OE1   . GLU C 2 299 ? 102.120 81.083  101.371 1.00 53.35 ?  278 GLU C OE1   1 
ATOM   13271 O  OE2   . GLU C 2 299 ? 101.027 81.878  103.105 1.00 53.10 -1 278 GLU C OE2   1 
ATOM   13272 N  N     . GLU C 2 300 ? 105.479 84.015  104.000 1.00 47.16 ?  279 GLU C N     1 
ATOM   13273 C  CA    . GLU C 2 300 ? 105.833 85.360  103.533 1.00 47.75 ?  279 GLU C CA    1 
ATOM   13274 C  C     . GLU C 2 300 ? 104.600 86.215  103.202 1.00 47.71 ?  279 GLU C C     1 
ATOM   13275 O  O     . GLU C 2 300 ? 103.614 85.710  102.654 1.00 47.77 ?  279 GLU C O     1 
ATOM   13276 C  CB    . GLU C 2 300 ? 106.785 85.274  102.326 1.00 48.42 ?  279 GLU C CB    1 
ATOM   13277 C  CG    . GLU C 2 300 ? 106.312 84.350  101.199 1.00 50.63 ?  279 GLU C CG    1 
ATOM   13278 C  CD    . GLU C 2 300 ? 107.453 83.848  100.313 1.00 53.06 ?  279 GLU C CD    1 
ATOM   13279 O  OE1   . GLU C 2 300 ? 108.224 84.684  99.785  1.00 54.35 ?  279 GLU C OE1   1 
ATOM   13280 O  OE2   . GLU C 2 300 ? 107.568 82.613  100.137 1.00 53.32 -1 279 GLU C OE2   1 
ATOM   13281 N  N     . GLU C 2 301 ? 104.667 87.497  103.560 1.00 47.40 ?  280 GLU C N     1 
ATOM   13282 C  CA    . GLU C 2 301 ? 103.599 88.469  103.291 1.00 47.46 ?  280 GLU C CA    1 
ATOM   13283 C  C     . GLU C 2 301 ? 104.191 89.805  102.828 1.00 47.31 ?  280 GLU C C     1 
ATOM   13284 O  O     . GLU C 2 301 ? 105.351 90.108  103.123 1.00 47.21 ?  280 GLU C O     1 
ATOM   13285 C  CB    . GLU C 2 301 ? 102.746 88.704  104.546 1.00 47.19 ?  280 GLU C CB    1 
ATOM   13286 C  CG    . GLU C 2 301 ? 102.020 87.477  105.100 1.00 47.14 ?  280 GLU C CG    1 
ATOM   13287 C  CD    . GLU C 2 301 ? 101.635 87.643  106.568 1.00 47.21 ?  280 GLU C CD    1 
ATOM   13288 O  OE1   . GLU C 2 301 ? 100.434 87.835  106.848 1.00 46.97 ?  280 GLU C OE1   1 
ATOM   13289 O  OE2   . GLU C 2 301 ? 102.536 87.592  107.440 1.00 46.13 -1 280 GLU C OE2   1 
ATOM   13290 N  N     . ASP C 2 302 ? 103.397 90.600  102.111 1.00 47.15 ?  281 ASP C N     1 
ATOM   13291 C  CA    . ASP C 2 302 ? 103.833 91.928  101.668 1.00 47.04 ?  281 ASP C CA    1 
ATOM   13292 C  C     . ASP C 2 302 ? 103.827 92.920  102.836 1.00 46.05 ?  281 ASP C C     1 
ATOM   13293 O  O     . ASP C 2 302 ? 102.778 93.177  103.437 1.00 46.10 ?  281 ASP C O     1 
ATOM   13294 C  CB    . ASP C 2 302 ? 102.947 92.459  100.525 1.00 47.66 ?  281 ASP C CB    1 
ATOM   13295 C  CG    . ASP C 2 302 ? 103.199 91.752  99.190  1.00 49.53 ?  281 ASP C CG    1 
ATOM   13296 O  OD1   . ASP C 2 302 ? 104.356 91.370  98.906  1.00 50.58 ?  281 ASP C OD1   1 
ATOM   13297 O  OD2   . ASP C 2 302 ? 102.229 91.603  98.408  1.00 51.14 -1 281 ASP C OD2   1 
ATOM   13298 N  N     . ILE C 2 303 ? 105.002 93.456  103.157 1.00 44.96 ?  282 ILE C N     1 
ATOM   13299 C  CA    . ILE C 2 303 ? 105.153 94.474  104.202 1.00 43.99 ?  282 ILE C CA    1 
ATOM   13300 C  C     . ILE C 2 303 ? 104.880 95.861  103.613 1.00 43.53 ?  282 ILE C C     1 
ATOM   13301 O  O     . ILE C 2 303 ? 105.180 96.105  102.443 1.00 43.52 ?  282 ILE C O     1 
ATOM   13302 C  CB    . ILE C 2 303 ? 106.577 94.435  104.831 1.00 43.84 ?  282 ILE C CB    1 
ATOM   13303 C  CG1   . ILE C 2 303 ? 106.920 93.027  105.354 1.00 43.91 ?  282 ILE C CG1   1 
ATOM   13304 C  CG2   . ILE C 2 303 ? 106.746 95.508  105.921 1.00 43.55 ?  282 ILE C CG2   1 
ATOM   13305 C  CD1   . ILE C 2 303 ? 105.967 92.472  106.417 1.00 42.76 ?  282 ILE C CD1   1 
ATOM   13306 N  N     . ASN C 2 304 ? 104.303 96.756  104.417 1.00 42.51 ?  283 ASN C N     1 
ATOM   13307 C  CA    . ASN C 2 304 ? 104.044 98.132  103.990 1.00 41.93 ?  283 ASN C CA    1 
ATOM   13308 C  C     . ASN C 2 304 ? 105.309 98.749  103.372 1.00 41.78 ?  283 ASN C C     1 
ATOM   13309 O  O     . ASN C 2 304 ? 106.350 98.816  104.039 1.00 41.13 ?  283 ASN C O     1 
ATOM   13310 C  CB    . ASN C 2 304 ? 103.555 98.975  105.178 1.00 41.83 ?  283 ASN C CB    1 
ATOM   13311 C  CG    . ASN C 2 304 ? 102.811 100.239 104.749 1.00 41.27 ?  283 ASN C CG    1 
ATOM   13312 O  OD1   . ASN C 2 304 ? 103.241 100.965 103.855 1.00 41.28 ?  283 ASN C OD1   1 
ATOM   13313 N  ND2   . ASN C 2 304 ? 101.690 100.506 105.402 1.00 40.67 ?  283 ASN C ND2   1 
ATOM   13314 N  N     . PRO C 2 305 ? 105.230 99.183  102.090 1.00 41.74 ?  284 PRO C N     1 
ATOM   13315 C  CA    . PRO C 2 305 ? 106.421 99.714  101.408 1.00 41.82 ?  284 PRO C CA    1 
ATOM   13316 C  C     . PRO C 2 305 ? 106.974 100.983 102.064 1.00 41.56 ?  284 PRO C C     1 
ATOM   13317 O  O     . PRO C 2 305 ? 108.155 101.296 101.898 1.00 41.46 ?  284 PRO C O     1 
ATOM   13318 C  CB    . PRO C 2 305 ? 105.928 99.995  99.975  1.00 42.14 ?  284 PRO C CB    1 
ATOM   13319 C  CG    . PRO C 2 305 ? 104.450 100.092 100.079 1.00 42.59 ?  284 PRO C CG    1 
ATOM   13320 C  CD    . PRO C 2 305 ? 104.050 99.167  101.202 1.00 42.05 ?  284 PRO C CD    1 
ATOM   13321 N  N     . ILE C 2 306 ? 106.129 101.689 102.811 1.00 41.19 ?  285 ILE C N     1 
ATOM   13322 C  CA    . ILE C 2 306 ? 106.550 102.854 103.591 1.00 41.47 ?  285 ILE C CA    1 
ATOM   13323 C  C     . ILE C 2 306 ? 107.616 102.449 104.617 1.00 41.71 ?  285 ILE C C     1 
ATOM   13324 O  O     . ILE C 2 306 ? 108.645 103.111 104.748 1.00 41.38 ?  285 ILE C O     1 
ATOM   13325 C  CB    . ILE C 2 306 ? 105.349 103.515 104.319 1.00 41.22 ?  285 ILE C CB    1 
ATOM   13326 C  CG1   . ILE C 2 306 ? 104.317 104.031 103.308 1.00 41.27 ?  285 ILE C CG1   1 
ATOM   13327 C  CG2   . ILE C 2 306 ? 105.821 104.631 105.248 1.00 40.37 ?  285 ILE C CG2   1 
ATOM   13328 C  CD1   . ILE C 2 306 ? 102.961 104.346 103.922 1.00 41.85 ?  285 ILE C CD1   1 
ATOM   13329 N  N     . VAL C 2 307 ? 107.352 101.357 105.333 1.00 42.33 ?  286 VAL C N     1 
ATOM   13330 C  CA    . VAL C 2 307 ? 108.281 100.817 106.332 1.00 43.36 ?  286 VAL C CA    1 
ATOM   13331 C  C     . VAL C 2 307 ? 109.596 100.344 105.698 1.00 44.51 ?  286 VAL C C     1 
ATOM   13332 O  O     . VAL C 2 307 ? 110.658 100.485 106.302 1.00 44.57 ?  286 VAL C O     1 
ATOM   13333 C  CB    . VAL C 2 307 ? 107.609 99.703  107.171 1.00 42.97 ?  286 VAL C CB    1 
ATOM   13334 C  CG1   . VAL C 2 307 ? 108.642 98.888  107.966 1.00 42.86 ?  286 VAL C CG1   1 
ATOM   13335 C  CG2   . VAL C 2 307 ? 106.583 100.324 108.100 1.00 41.93 ?  286 VAL C CG2   1 
ATOM   13336 N  N     . LEU C 2 308 ? 109.509 99.812  104.480 1.00 46.21 ?  287 LEU C N     1 
ATOM   13337 C  CA    . LEU C 2 308 ? 110.680 99.386  103.700 1.00 47.66 ?  287 LEU C CA    1 
ATOM   13338 C  C     . LEU C 2 308 ? 111.536 100.569 103.247 1.00 48.82 ?  287 LEU C C     1 
ATOM   13339 O  O     . LEU C 2 308 ? 112.768 100.464 103.186 1.00 49.02 ?  287 LEU C O     1 
ATOM   13340 C  CB    . LEU C 2 308 ? 110.248 98.537  102.496 1.00 47.95 ?  287 LEU C CB    1 
ATOM   13341 C  CG    . LEU C 2 308 ? 110.150 97.011  102.670 1.00 48.23 ?  287 LEU C CG    1 
ATOM   13342 C  CD1   . LEU C 2 308 ? 109.879 96.565  104.114 1.00 48.10 ?  287 LEU C CD1   1 
ATOM   13343 C  CD2   . LEU C 2 308 ? 109.123 96.413  101.712 1.00 48.81 ?  287 LEU C CD2   1 
ATOM   13344 N  N     . ASN C 2 309 ? 110.877 101.685 102.930 1.00 49.80 ?  288 ASN C N     1 
ATOM   13345 C  CA    . ASN C 2 309 ? 111.563 102.954 102.703 1.00 51.09 ?  288 ASN C CA    1 
ATOM   13346 C  C     . ASN C 2 309 ? 112.133 103.553 103.993 1.00 51.08 ?  288 ASN C C     1 
ATOM   13347 O  O     . ASN C 2 309 ? 113.091 104.325 103.950 1.00 51.41 ?  288 ASN C O     1 
ATOM   13348 C  CB    . ASN C 2 309 ? 110.649 103.957 101.995 1.00 51.37 ?  288 ASN C CB    1 
ATOM   13349 C  CG    . ASN C 2 309 ? 110.584 103.726 100.498 1.00 53.22 ?  288 ASN C CG    1 
ATOM   13350 O  OD1   . ASN C 2 309 ? 110.420 102.592 100.034 1.00 54.39 ?  288 ASN C OD1   1 
ATOM   13351 N  ND2   . ASN C 2 309 ? 110.715 104.802 99.730  1.00 54.70 ?  288 ASN C ND2   1 
ATOM   13352 N  N     . GLY C 2 310 ? 111.541 103.192 105.131 1.00 51.25 ?  289 GLY C N     1 
ATOM   13353 C  CA    . GLY C 2 310 ? 112.061 103.568 106.447 1.00 51.35 ?  289 GLY C CA    1 
ATOM   13354 C  C     . GLY C 2 310 ? 113.409 102.934 106.766 1.00 51.86 ?  289 GLY C C     1 
ATOM   13355 O  O     . GLY C 2 310 ? 114.149 103.432 107.622 1.00 51.49 ?  289 GLY C O     1 
ATOM   13356 N  N     . LEU C 2 311 ? 113.726 101.834 106.082 1.00 52.45 ?  290 LEU C N     1 
ATOM   13357 C  CA    . LEU C 2 311 ? 115.013 101.152 106.238 1.00 52.99 ?  290 LEU C CA    1 
ATOM   13358 C  C     . LEU C 2 311 ? 116.075 101.742 105.307 1.00 53.65 ?  290 LEU C C     1 
ATOM   13359 O  O     . LEU C 2 311 ? 116.025 101.570 104.083 1.00 54.22 ?  290 LEU C O     1 
ATOM   13360 C  CB    . LEU C 2 311 ? 114.863 99.647  105.986 1.00 53.08 ?  290 LEU C CB    1 
ATOM   13361 C  CG    . LEU C 2 311 ? 114.149 98.783  107.028 1.00 53.33 ?  290 LEU C CG    1 
ATOM   13362 C  CD1   . LEU C 2 311 ? 113.778 97.433  106.431 1.00 53.79 ?  290 LEU C CD1   1 
ATOM   13363 C  CD2   . LEU C 2 311 ? 115.001 98.600  108.286 1.00 53.22 ?  290 LEU C CD2   1 
ATOM   13364 N  N     . LYS C 2 330 ? 139.006 109.247 114.854 1.00 57.38 ?  309 LYS C N     1 
ATOM   13365 C  CA    . LYS C 2 330 ? 140.238 110.001 114.653 1.00 58.57 ?  309 LYS C CA    1 
ATOM   13366 C  C     . LYS C 2 330 ? 140.958 109.554 113.386 1.00 57.73 ?  309 LYS C C     1 
ATOM   13367 O  O     . LYS C 2 330 ? 140.773 108.431 112.919 1.00 59.72 ?  309 LYS C O     1 
ATOM   13368 C  CB    . LYS C 2 330 ? 141.167 109.843 115.859 1.00 55.66 ?  309 LYS C CB    1 
ATOM   13369 C  CG    . LYS C 2 330 ? 140.886 110.804 117.001 1.00 56.05 ?  309 LYS C CG    1 
ATOM   13370 C  CD    . LYS C 2 330 ? 142.025 110.797 118.009 1.00 57.52 ?  309 LYS C CD    1 
ATOM   13371 C  CE    . LYS C 2 330 ? 141.738 111.720 119.181 1.00 58.27 ?  309 LYS C CE    1 
ATOM   13372 N  NZ    . LYS C 2 330 ? 140.922 111.048 120.230 1.00 57.81 1  309 LYS C NZ    1 
ATOM   13373 N  N     . ALA C 2 331 ? 141.780 110.441 112.834 1.00 46.74 ?  310 ALA C N     1 
ATOM   13374 C  CA    . ALA C 2 331 ? 142.622 110.101 111.700 1.00 47.69 ?  310 ALA C CA    1 
ATOM   13375 C  C     . ALA C 2 331 ? 143.939 109.517 112.193 1.00 44.34 ?  310 ALA C C     1 
ATOM   13376 O  O     . ALA C 2 331 ? 144.455 109.900 113.246 1.00 44.88 ?  310 ALA C O     1 
ATOM   13377 C  CB    . ALA C 2 331 ? 142.885 111.328 110.826 1.00 44.94 ?  310 ALA C CB    1 
ATOM   13378 N  N     . THR C 2 332 ? 144.473 108.573 111.422 1.00 40.86 ?  311 THR C N     1 
ATOM   13379 C  CA    . THR C 2 332 ? 145.696 107.881 111.808 1.00 38.81 ?  311 THR C CA    1 
ATOM   13380 C  C     . THR C 2 332 ? 146.847 108.862 111.962 1.00 36.15 ?  311 THR C C     1 
ATOM   13381 O  O     . THR C 2 332 ? 147.070 109.716 111.100 1.00 43.30 ?  311 THR C O     1 
ATOM   13382 C  CB    . THR C 2 332 ? 146.046 106.810 110.771 1.00 39.78 ?  311 THR C CB    1 
ATOM   13383 O  OG1   . THR C 2 332 ? 144.987 105.846 110.702 1.00 41.99 ?  311 THR C OG1   1 
ATOM   13384 C  CG2   . THR C 2 332 ? 147.342 106.108 111.143 1.00 37.37 ?  311 THR C CG2   1 
ATOM   13385 N  N     . VAL C 2 333 ? 147.575 108.736 113.066 1.00 29.00 ?  312 VAL C N     1 
ATOM   13386 C  CA    . VAL C 2 333 ? 148.695 109.627 113.353 1.00 27.73 ?  312 VAL C CA    1 
ATOM   13387 C  C     . VAL C 2 333 ? 149.972 108.996 112.815 1.00 34.73 ?  312 VAL C C     1 
ATOM   13388 O  O     . VAL C 2 333 ? 150.354 107.895 113.224 1.00 34.24 ?  312 VAL C O     1 
ATOM   13389 C  CB    . VAL C 2 333 ? 148.805 109.905 114.858 1.00 29.67 ?  312 VAL C CB    1 
ATOM   13390 C  CG1   . VAL C 2 333 ? 150.098 110.644 115.167 1.00 33.09 ?  312 VAL C CG1   1 
ATOM   13391 C  CG2   . VAL C 2 333 ? 147.602 110.700 115.337 1.00 33.00 ?  312 VAL C CG2   1 
ATOM   13392 N  N     . GLU C 2 334 ? 150.631 109.692 111.893 1.00 31.99 ?  313 GLU C N     1 
ATOM   13393 C  CA    . GLU C 2 334 ? 151.879 109.238 111.315 1.00 30.19 ?  313 GLU C CA    1 
ATOM   13394 C  C     . GLU C 2 334 ? 152.951 110.296 111.537 1.00 35.47 ?  313 GLU C C     1 
ATOM   13395 O  O     . GLU C 2 334 ? 152.736 111.468 111.191 1.00 39.91 ?  313 GLU C O     1 
ATOM   13396 C  CB    . GLU C 2 334 ? 151.718 108.953 109.814 1.00 31.98 ?  313 GLU C CB    1 
ATOM   13397 C  CG    . GLU C 2 334 ? 152.755 107.999 109.249 1.00 30.40 ?  313 GLU C CG    1 
ATOM   13398 C  CD    . GLU C 2 334 ? 152.778 107.989 107.734 1.00 36.69 ?  313 GLU C CD    1 
ATOM   13399 O  OE1   . GLU C 2 334 ? 151.691 107.976 107.122 1.00 35.22 ?  313 GLU C OE1   1 
ATOM   13400 O  OE2   . GLU C 2 334 ? 153.884 107.975 107.154 1.00 37.50 -1 313 GLU C OE2   1 
ATOM   13401 N  N     . PRO C 2 335 ? 154.097 109.941 112.111 1.00 33.23 ?  314 PRO C N     1 
ATOM   13402 C  CA    . PRO C 2 335 ? 155.110 110.955 112.422 1.00 32.48 ?  314 PRO C CA    1 
ATOM   13403 C  C     . PRO C 2 335 ? 155.681 111.595 111.168 1.00 32.75 ?  314 PRO C C     1 
ATOM   13404 O  O     . PRO C 2 335 ? 155.782 110.972 110.109 1.00 33.62 ?  314 PRO C O     1 
ATOM   13405 C  CB    . PRO C 2 335 ? 156.182 110.162 113.177 1.00 27.14 ?  314 PRO C CB    1 
ATOM   13406 C  CG    . PRO C 2 335 ? 156.028 108.767 112.677 1.00 33.25 ?  314 PRO C CG    1 
ATOM   13407 C  CD    . PRO C 2 335 ? 154.552 108.583 112.456 1.00 31.97 ?  314 PRO C CD    1 
ATOM   13408 N  N     . LEU C 2 336 ? 156.054 112.865 111.304 1.00 31.37 ?  315 LEU C N     1 
ATOM   13409 C  CA    . LEU C 2 336 ? 156.664 113.602 110.209 1.00 25.32 ?  315 LEU C CA    1 
ATOM   13410 C  C     . LEU C 2 336 ? 158.104 113.158 110.005 1.00 30.05 ?  315 LEU C C     1 
ATOM   13411 O  O     . LEU C 2 336 ? 158.863 112.995 110.965 1.00 28.04 ?  315 LEU C O     1 
ATOM   13412 C  CB    . LEU C 2 336 ? 156.625 115.104 110.489 1.00 24.68 ?  315 LEU C CB    1 
ATOM   13413 C  CG    . LEU C 2 336 ? 155.418 115.906 110.010 1.00 29.53 ?  315 LEU C CG    1 
ATOM   13414 C  CD1   . LEU C 2 336 ? 155.361 117.233 110.747 1.00 23.58 ?  315 LEU C CD1   1 
ATOM   13415 C  CD2   . LEU C 2 336 ? 155.474 116.127 108.510 1.00 23.76 ?  315 LEU C CD2   1 
ATOM   13416 N  N     . LYS C 2 337 ? 158.482 112.968 108.747 1.00 29.08 ?  316 LYS C N     1 
ATOM   13417 C  CA    . LYS C 2 337 ? 159.857 112.653 108.404 1.00 24.90 ?  316 LYS C CA    1 
ATOM   13418 C  C     . LYS C 2 337 ? 160.634 113.933 108.108 1.00 25.51 ?  316 LYS C C     1 
ATOM   13419 O  O     . LYS C 2 337 ? 160.066 115.012 107.934 1.00 33.13 ?  316 LYS C O     1 
ATOM   13420 C  CB    . LYS C 2 337 ? 159.914 111.706 107.205 1.00 29.23 ?  316 LYS C CB    1 
ATOM   13421 C  CG    . LYS C 2 337 ? 158.997 110.502 107.308 1.00 29.66 ?  316 LYS C CG    1 
ATOM   13422 C  CD    . LYS C 2 337 ? 159.429 109.406 106.346 1.00 30.93 ?  316 LYS C CD    1 
ATOM   13423 C  CE    . LYS C 2 337 ? 158.842 108.059 106.735 1.00 33.14 ?  316 LYS C CE    1 
ATOM   13424 N  NZ    . LYS C 2 337 ? 157.482 108.196 107.326 1.00 33.67 1  316 LYS C NZ    1 
ATOM   13425 N  N     . ASP C 2 338 ? 161.960 113.802 108.061 1.00 26.51 ?  317 ASP C N     1 
ATOM   13426 C  CA    . ASP C 2 338 ? 162.795 114.938 107.693 1.00 29.94 ?  317 ASP C CA    1 
ATOM   13427 C  C     . ASP C 2 338 ? 162.538 115.361 106.253 1.00 29.65 ?  317 ASP C C     1 
ATOM   13428 O  O     . ASP C 2 338 ? 162.492 116.557 105.947 1.00 24.94 ?  317 ASP C O     1 
ATOM   13429 C  CB    . ASP C 2 338 ? 164.271 114.597 107.899 1.00 32.12 ?  317 ASP C CB    1 
ATOM   13430 C  CG    . ASP C 2 338 ? 164.748 114.904 109.304 1.00 35.61 ?  317 ASP C CG    1 
ATOM   13431 O  OD1   . ASP C 2 338 ? 164.553 114.054 110.199 1.00 36.45 ?  317 ASP C OD1   1 
ATOM   13432 O  OD2   . ASP C 2 338 ? 165.319 115.995 109.516 1.00 32.88 -1 317 ASP C OD2   1 
ATOM   13433 N  N     . ASP C 2 339 ? 162.357 114.390 105.356 1.00 31.98 ?  318 ASP C N     1 
ATOM   13434 C  CA    . ASP C 2 339 ? 162.122 114.686 103.948 1.00 23.82 ?  318 ASP C CA    1 
ATOM   13435 C  C     . ASP C 2 339 ? 160.769 115.337 103.693 1.00 21.90 ?  318 ASP C C     1 
ATOM   13436 O  O     . ASP C 2 339 ? 160.548 115.848 102.590 1.00 29.62 ?  318 ASP C O     1 
ATOM   13437 C  CB    . ASP C 2 339 ? 162.242 113.406 103.118 1.00 24.61 ?  318 ASP C CB    1 
ATOM   13438 C  CG    . ASP C 2 339 ? 163.675 112.927 102.990 1.00 36.61 ?  318 ASP C CG    1 
ATOM   13439 O  OD1   . ASP C 2 339 ? 164.590 113.777 102.986 1.00 34.94 ?  318 ASP C OD1   1 
ATOM   13440 O  OD2   . ASP C 2 339 ? 163.886 111.699 102.894 1.00 37.02 -1 318 ASP C OD2   1 
ATOM   13441 N  N     . ASP C 2 340 ? 159.862 115.326 104.671 1.00 21.75 ?  319 ASP C N     1 
ATOM   13442 C  CA    . ASP C 2 340 ? 158.568 115.978 104.510 1.00 12.52 ?  319 ASP C CA    1 
ATOM   13443 C  C     . ASP C 2 340 ? 158.669 117.496 104.508 1.00 11.68 ?  319 ASP C C     1 
ATOM   13444 O  O     . ASP C 2 340 ? 157.723 118.161 104.073 1.00 29.94 ?  319 ASP C O     1 
ATOM   13445 C  CB    . ASP C 2 340 ? 157.616 115.534 105.620 1.00 15.38 ?  319 ASP C CB    1 
ATOM   13446 C  CG    . ASP C 2 340 ? 157.130 114.115 105.436 1.00 27.80 ?  319 ASP C CG    1 
ATOM   13447 O  OD1   . ASP C 2 340 ? 156.426 113.609 106.333 1.00 35.11 ?  319 ASP C OD1   1 
ATOM   13448 O  OD2   . ASP C 2 340 ? 157.450 113.504 104.394 1.00 32.85 -1 319 ASP C OD2   1 
ATOM   13449 N  N     . PHE C 2 341 ? 159.779 118.054 104.981 1.00 19.10 ?  320 PHE C N     1 
ATOM   13450 C  CA    . PHE C 2 341 ? 159.954 119.495 105.087 1.00 9.08  ?  320 PHE C CA    1 
ATOM   13451 C  C     . PHE C 2 341 ? 160.635 120.104 103.871 1.00 17.46 ?  320 PHE C C     1 
ATOM   13452 O  O     . PHE C 2 341 ? 160.833 121.322 103.835 1.00 21.47 ?  320 PHE C O     1 
ATOM   13453 C  CB    . PHE C 2 341 ? 160.753 119.830 106.348 1.00 14.57 ?  320 PHE C CB    1 
ATOM   13454 C  CG    . PHE C 2 341 ? 159.989 119.618 107.620 1.00 10.84 ?  320 PHE C CG    1 
ATOM   13455 C  CD1   . PHE C 2 341 ? 159.270 120.652 108.191 1.00 9.48  ?  320 PHE C CD1   1 
ATOM   13456 C  CD2   . PHE C 2 341 ? 159.981 118.381 108.242 1.00 12.36 ?  320 PHE C CD2   1 
ATOM   13457 C  CE1   . PHE C 2 341 ? 158.564 120.459 109.360 1.00 7.91  ?  320 PHE C CE1   1 
ATOM   13458 C  CE2   . PHE C 2 341 ? 159.275 118.183 109.409 1.00 13.16 ?  320 PHE C CE2   1 
ATOM   13459 C  CZ    . PHE C 2 341 ? 158.566 119.223 109.969 1.00 4.56  ?  320 PHE C CZ    1 
ATOM   13460 N  N     . TYR C 2 342 ? 160.998 119.297 102.878 1.00 9.53  ?  321 TYR C N     1 
ATOM   13461 C  CA    . TYR C 2 342 ? 161.611 119.791 101.656 1.00 17.23 ?  321 TYR C CA    1 
ATOM   13462 C  C     . TYR C 2 342 ? 160.798 119.335 100.455 1.00 16.10 ?  321 TYR C C     1 
ATOM   13463 O  O     . TYR C 2 342 ? 160.226 118.242 100.445 1.00 16.88 ?  321 TYR C O     1 
ATOM   13464 C  CB    . TYR C 2 342 ? 163.079 119.338 101.503 1.00 17.88 ?  321 TYR C CB    1 
ATOM   13465 C  CG    . TYR C 2 342 ? 163.906 119.400 102.770 1.00 13.83 ?  321 TYR C CG    1 
ATOM   13466 C  CD1   . TYR C 2 342 ? 163.748 118.467 103.786 1.00 18.12 ?  321 TYR C CD1   1 
ATOM   13467 C  CD2   . TYR C 2 342 ? 164.843 120.406 102.951 1.00 16.03 ?  321 TYR C CD2   1 
ATOM   13468 C  CE1   . TYR C 2 342 ? 164.506 118.533 104.939 1.00 15.48 ?  321 TYR C CE1   1 
ATOM   13469 C  CE2   . TYR C 2 342 ? 165.603 120.480 104.101 1.00 17.80 ?  321 TYR C CE2   1 
ATOM   13470 C  CZ    . TYR C 2 342 ? 165.430 119.542 105.091 1.00 19.62 ?  321 TYR C CZ    1 
ATOM   13471 O  OH    . TYR C 2 342 ? 166.186 119.610 106.239 1.00 28.71 ?  321 TYR C OH    1 
ATOM   13472 N  N     . PHE C 2 343 ? 160.752 120.195 99.443  1.00 7.71  ?  322 PHE C N     1 
ATOM   13473 C  CA    . PHE C 2 343 ? 159.907 119.976 98.278  1.00 20.35 ?  322 PHE C CA    1 
ATOM   13474 C  C     . PHE C 2 343 ? 160.665 120.277 96.990  1.00 25.47 ?  322 PHE C C     1 
ATOM   13475 O  O     . PHE C 2 343 ? 161.643 121.023 96.991  1.00 26.11 ?  322 PHE C O     1 
ATOM   13476 C  CB    . PHE C 2 343 ? 158.651 120.844 98.374  1.00 15.28 ?  322 PHE C CB    1 
ATOM   13477 C  CG    . PHE C 2 343 ? 157.873 120.641 99.641  1.00 13.74 ?  322 PHE C CG    1 
ATOM   13478 C  CD1   . PHE C 2 343 ? 156.969 119.601 99.755  1.00 17.31 ?  322 PHE C CD1   1 
ATOM   13479 C  CD2   . PHE C 2 343 ? 158.063 121.477 100.725 1.00 4.75  ?  322 PHE C CD2   1 
ATOM   13480 C  CE1   . PHE C 2 343 ? 156.260 119.409 100.922 1.00 16.31 ?  322 PHE C CE1   1 
ATOM   13481 C  CE2   . PHE C 2 343 ? 157.360 121.288 101.894 1.00 5.64  ?  322 PHE C CE2   1 
ATOM   13482 C  CZ    . PHE C 2 343 ? 156.456 120.254 101.993 1.00 10.19 ?  322 PHE C CZ    1 
ATOM   13483 N  N     . ASP D 2 37  ? 122.963 112.327 142.888 1.00 32.44 ?  16  ASP D N     1 
ATOM   13484 C  CA    . ASP D 2 37  ? 123.506 113.665 142.634 1.00 32.83 ?  16  ASP D CA    1 
ATOM   13485 C  C     . ASP D 2 37  ? 124.634 113.694 141.604 1.00 31.65 ?  16  ASP D C     1 
ATOM   13486 O  O     . ASP D 2 37  ? 125.090 114.777 141.230 1.00 32.65 ?  16  ASP D O     1 
ATOM   13487 C  CB    . ASP D 2 37  ? 124.048 114.285 143.931 1.00 33.73 ?  16  ASP D CB    1 
ATOM   13488 C  CG    . ASP D 2 37  ? 122.966 114.551 144.967 1.00 36.81 ?  16  ASP D CG    1 
ATOM   13489 O  OD1   . ASP D 2 37  ? 123.330 114.706 146.158 1.00 39.69 ?  16  ASP D OD1   1 
ATOM   13490 O  OD2   . ASP D 2 37  ? 121.767 114.600 144.609 1.00 39.67 -1 16  ASP D OD2   1 
ATOM   13491 N  N     . PHE D 2 38  ? 125.091 112.529 141.150 1.00 29.55 ?  17  PHE D N     1 
ATOM   13492 C  CA    . PHE D 2 38  ? 126.370 112.478 140.441 1.00 27.75 ?  17  PHE D CA    1 
ATOM   13493 C  C     . PHE D 2 38  ? 126.463 111.567 139.206 1.00 26.21 ?  17  PHE D C     1 
ATOM   13494 O  O     . PHE D 2 38  ? 127.360 111.740 138.389 1.00 25.93 ?  17  PHE D O     1 
ATOM   13495 C  CB    . PHE D 2 38  ? 127.498 112.140 141.443 1.00 27.37 ?  17  PHE D CB    1 
ATOM   13496 C  CG    . PHE D 2 38  ? 127.309 110.820 142.142 1.00 27.32 ?  17  PHE D CG    1 
ATOM   13497 C  CD1   . PHE D 2 38  ? 127.730 109.636 141.544 1.00 27.01 ?  17  PHE D CD1   1 
ATOM   13498 C  CD2   . PHE D 2 38  ? 126.712 110.757 143.395 1.00 28.02 ?  17  PHE D CD2   1 
ATOM   13499 C  CE1   . PHE D 2 38  ? 127.552 108.410 142.183 1.00 27.66 ?  17  PHE D CE1   1 
ATOM   13500 C  CE2   . PHE D 2 38  ? 126.526 109.538 144.034 1.00 27.68 ?  17  PHE D CE2   1 
ATOM   13501 C  CZ    . PHE D 2 38  ? 126.949 108.360 143.425 1.00 27.47 ?  17  PHE D CZ    1 
ATOM   13502 N  N     . THR D 2 39  ? 125.553 110.607 139.071 1.00 24.88 ?  18  THR D N     1 
ATOM   13503 C  CA    . THR D 2 39  ? 125.672 109.582 138.021 1.00 23.81 ?  18  THR D CA    1 
ATOM   13504 C  C     . THR D 2 39  ? 125.595 110.130 136.585 1.00 23.56 ?  18  THR D C     1 
ATOM   13505 O  O     . THR D 2 39  ? 126.364 109.723 135.714 1.00 23.02 ?  18  THR D O     1 
ATOM   13506 C  CB    . THR D 2 39  ? 124.699 108.401 138.261 1.00 23.40 ?  18  THR D CB    1 
ATOM   13507 O  OG1   . THR D 2 39  ? 125.238 107.553 139.283 1.00 23.77 ?  18  THR D OG1   1 
ATOM   13508 C  CG2   . THR D 2 39  ? 124.511 107.565 137.006 1.00 22.31 ?  18  THR D CG2   1 
ATOM   13509 N  N     . GLN D 2 40  ? 124.686 111.062 136.333 1.00 23.78 ?  19  GLN D N     1 
ATOM   13510 C  CA    . GLN D 2 40  ? 124.601 111.641 134.989 1.00 23.88 ?  19  GLN D CA    1 
ATOM   13511 C  C     . GLN D 2 40  ? 125.855 112.439 134.623 1.00 24.09 ?  19  GLN D C     1 
ATOM   13512 O  O     . GLN D 2 40  ? 126.352 112.339 133.509 1.00 23.15 ?  19  GLN D O     1 
ATOM   13513 C  CB    . GLN D 2 40  ? 123.326 112.468 134.813 1.00 24.53 ?  19  GLN D CB    1 
ATOM   13514 C  CG    . GLN D 2 40  ? 122.077 111.602 134.829 1.00 24.06 ?  19  GLN D CG    1 
ATOM   13515 C  CD    . GLN D 2 40  ? 120.869 112.278 134.223 1.00 25.83 ?  19  GLN D CD    1 
ATOM   13516 O  OE1   . GLN D 2 40  ? 120.990 113.314 133.571 1.00 25.90 ?  19  GLN D OE1   1 
ATOM   13517 N  NE2   . GLN D 2 40  ? 119.694 111.681 134.417 1.00 23.56 ?  19  GLN D NE2   1 
ATOM   13518 N  N     . MET D 2 41  ? 126.390 113.191 135.576 1.00 24.07 ?  20  MET D N     1 
ATOM   13519 C  CA    . MET D 2 41  ? 127.664 113.881 135.367 1.00 25.53 ?  20  MET D CA    1 
ATOM   13520 C  C     . MET D 2 41  ? 128.814 112.910 135.029 1.00 24.24 ?  20  MET D C     1 
ATOM   13521 O  O     . MET D 2 41  ? 129.604 113.171 134.117 1.00 23.16 ?  20  MET D O     1 
ATOM   13522 C  CB    . MET D 2 41  ? 128.007 114.732 136.594 1.00 26.79 ?  20  MET D CB    1 
ATOM   13523 C  CG    . MET D 2 41  ? 129.326 115.475 136.506 1.00 32.62 ?  20  MET D CG    1 
ATOM   13524 S  SD    . MET D 2 41  ? 129.761 116.155 138.124 1.00 44.01 ?  20  MET D SD    1 
ATOM   13525 C  CE    . MET D 2 41  ? 131.547 116.275 137.981 1.00 41.93 ?  20  MET D CE    1 
ATOM   13526 N  N     . PHE D 2 42  ? 128.899 111.789 135.748 1.00 23.31 ?  21  PHE D N     1 
ATOM   13527 C  CA    . PHE D 2 42  ? 129.943 110.804 135.467 1.00 23.44 ?  21  PHE D CA    1 
ATOM   13528 C  C     . PHE D 2 42  ? 129.705 110.077 134.159 1.00 23.55 ?  21  PHE D C     1 
ATOM   13529 O  O     . PHE D 2 42  ? 130.654 109.734 133.462 1.00 23.74 ?  21  PHE D O     1 
ATOM   13530 C  CB    . PHE D 2 42  ? 130.116 109.816 136.622 1.00 22.97 ?  21  PHE D CB    1 
ATOM   13531 C  CG    . PHE D 2 42  ? 131.039 110.316 137.677 1.00 23.86 ?  21  PHE D CG    1 
ATOM   13532 C  CD1   . PHE D 2 42  ? 132.385 109.959 137.667 1.00 24.55 ?  21  PHE D CD1   1 
ATOM   13533 C  CD2   . PHE D 2 42  ? 130.582 111.178 138.656 1.00 24.06 ?  21  PHE D CD2   1 
ATOM   13534 C  CE1   . PHE D 2 42  ? 133.258 110.444 138.644 1.00 25.78 ?  21  PHE D CE1   1 
ATOM   13535 C  CE2   . PHE D 2 42  ? 131.448 111.669 139.637 1.00 25.25 ?  21  PHE D CE2   1 
ATOM   13536 C  CZ    . PHE D 2 42  ? 132.780 111.308 139.628 1.00 25.79 ?  21  PHE D CZ    1 
ATOM   13537 N  N     . TYR D 2 43  ? 128.433 109.864 133.826 1.00 24.08 ?  22  TYR D N     1 
ATOM   13538 C  CA    . TYR D 2 43  ? 128.071 109.313 132.531 1.00 24.74 ?  22  TYR D CA    1 
ATOM   13539 C  C     . TYR D 2 43  ? 128.694 110.165 131.423 1.00 25.72 ?  22  TYR D C     1 
ATOM   13540 O  O     . TYR D 2 43  ? 129.358 109.642 130.522 1.00 25.56 ?  22  TYR D O     1 
ATOM   13541 C  CB    . TYR D 2 43  ? 126.547 109.230 132.348 1.00 24.90 ?  22  TYR D CB    1 
ATOM   13542 C  CG    . TYR D 2 43  ? 126.168 108.817 130.933 1.00 24.38 ?  22  TYR D CG    1 
ATOM   13543 C  CD1   . TYR D 2 43  ? 126.027 107.476 130.596 1.00 23.96 ?  22  TYR D CD1   1 
ATOM   13544 C  CD2   . TYR D 2 43  ? 126.010 109.770 129.924 1.00 24.73 ?  22  TYR D CD2   1 
ATOM   13545 C  CE1   . TYR D 2 43  ? 125.715 107.090 129.291 1.00 23.42 ?  22  TYR D CE1   1 
ATOM   13546 C  CE2   . TYR D 2 43  ? 125.685 109.401 128.617 1.00 26.65 ?  22  TYR D CE2   1 
ATOM   13547 C  CZ    . TYR D 2 43  ? 125.544 108.058 128.312 1.00 25.68 ?  22  TYR D CZ    1 
ATOM   13548 O  OH    . TYR D 2 43  ? 125.226 107.688 127.025 1.00 26.57 ?  22  TYR D OH    1 
ATOM   13549 N  N     . ASN D 2 44  ? 128.466 111.474 131.503 1.00 26.77 ?  23  ASN D N     1 
ATOM   13550 C  CA    . ASN D 2 44  ? 128.971 112.418 130.514 1.00 28.57 ?  23  ASN D CA    1 
ATOM   13551 C  C     . ASN D 2 44  ? 130.482 112.372 130.387 1.00 28.70 ?  23  ASN D C     1 
ATOM   13552 O  O     . ASN D 2 44  ? 131.007 112.215 129.282 1.00 28.99 ?  23  ASN D O     1 
ATOM   13553 C  CB    . ASN D 2 44  ? 128.477 113.835 130.822 1.00 29.62 ?  23  ASN D CB    1 
ATOM   13554 C  CG    . ASN D 2 44  ? 126.980 113.988 130.582 1.00 32.44 ?  23  ASN D CG    1 
ATOM   13555 O  OD1   . ASN D 2 44  ? 126.376 113.215 129.828 1.00 34.30 ?  23  ASN D OD1   1 
ATOM   13556 N  ND2   . ASN D 2 44  ? 126.373 114.983 131.224 1.00 35.17 ?  23  ASN D ND2   1 
ATOM   13557 N  N     . GLN D 2 45  ? 131.172 112.462 131.522 1.00 28.97 ?  24  GLN D N     1 
ATOM   13558 C  CA    . GLN D 2 45  ? 132.630 112.443 131.532 1.00 29.99 ?  24  GLN D CA    1 
ATOM   13559 C  C     . GLN D 2 45  ? 133.202 111.122 130.997 1.00 29.69 ?  24  GLN D C     1 
ATOM   13560 O  O     . GLN D 2 45  ? 134.189 111.126 130.263 1.00 30.01 ?  24  GLN D O     1 
ATOM   13561 C  CB    . GLN D 2 45  ? 133.175 112.754 132.932 1.00 30.27 ?  24  GLN D CB    1 
ATOM   13562 C  CG    . GLN D 2 45  ? 134.702 112.982 132.971 1.00 32.29 ?  24  GLN D CG    1 
ATOM   13563 C  CD    . GLN D 2 45  ? 135.152 114.188 132.156 1.00 35.95 ?  24  GLN D CD    1 
ATOM   13564 O  OE1   . GLN D 2 45  ? 134.400 115.150 131.973 1.00 36.72 ?  24  GLN D OE1   1 
ATOM   13565 N  NE2   . GLN D 2 45  ? 136.385 114.141 131.663 1.00 37.05 ?  24  GLN D NE2   1 
ATOM   13566 N  N     . ASN D 2 46  ? 132.565 110.004 131.342 1.00 28.93 ?  25  ASN D N     1 
ATOM   13567 C  CA    . ASN D 2 46  ? 132.985 108.705 130.846 1.00 28.70 ?  25  ASN D CA    1 
ATOM   13568 C  C     . ASN D 2 46  ? 132.874 108.561 129.334 1.00 29.05 ?  25  ASN D C     1 
ATOM   13569 O  O     . ASN D 2 46  ? 133.845 108.179 128.675 1.00 28.51 ?  25  ASN D O     1 
ATOM   13570 C  CB    . ASN D 2 46  ? 132.227 107.569 131.546 1.00 28.36 ?  25  ASN D CB    1 
ATOM   13571 C  CG    . ASN D 2 46  ? 132.901 107.129 132.827 1.00 28.45 ?  25  ASN D CG    1 
ATOM   13572 O  OD1   . ASN D 2 46  ? 133.653 106.157 132.829 1.00 28.03 ?  25  ASN D OD1   1 
ATOM   13573 N  ND2   . ASN D 2 46  ? 132.662 107.857 133.917 1.00 26.53 ?  25  ASN D ND2   1 
ATOM   13574 N  N     . VAL D 2 47  ? 131.705 108.889 128.783 1.00 29.66 ?  26  VAL D N     1 
ATOM   13575 C  CA    . VAL D 2 47  ? 131.466 108.677 127.355 1.00 31.15 ?  26  VAL D CA    1 
ATOM   13576 C  C     . VAL D 2 47  ? 132.260 109.657 126.498 1.00 32.39 ?  26  VAL D C     1 
ATOM   13577 O  O     . VAL D 2 47  ? 132.655 109.328 125.381 1.00 32.80 ?  26  VAL D O     1 
ATOM   13578 C  CB    . VAL D 2 47  ? 129.950 108.663 126.963 1.00 31.08 ?  26  VAL D CB    1 
ATOM   13579 C  CG1   . VAL D 2 47  ? 129.191 107.619 127.774 1.00 31.09 ?  26  VAL D CG1   1 
ATOM   13580 C  CG2   . VAL D 2 47  ? 129.308 110.051 127.103 1.00 30.81 ?  26  VAL D CG2   1 
ATOM   13581 N  N     . LYS D 2 48  ? 132.526 110.849 127.021 1.00 33.28 ?  27  LYS D N     1 
ATOM   13582 C  CA    . LYS D 2 48  ? 133.321 111.794 126.253 1.00 34.87 ?  27  LYS D CA    1 
ATOM   13583 C  C     . LYS D 2 48  ? 134.829 111.472 126.258 1.00 34.91 ?  27  LYS D C     1 
ATOM   13584 O  O     . LYS D 2 48  ? 135.585 112.032 125.469 1.00 34.92 ?  27  LYS D O     1 
ATOM   13585 C  CB    . LYS D 2 48  ? 133.010 113.245 126.651 1.00 35.45 ?  27  LYS D CB    1 
ATOM   13586 C  CG    . LYS D 2 48  ? 133.771 113.797 127.833 1.00 37.41 ?  27  LYS D CG    1 
ATOM   13587 C  CD    . LYS D 2 48  ? 133.652 115.330 127.857 1.00 40.91 ?  27  LYS D CD    1 
ATOM   13588 C  CE    . LYS D 2 48  ? 134.710 115.951 128.773 1.00 42.46 ?  27  LYS D CE    1 
ATOM   13589 N  NZ    . LYS D 2 48  ? 134.731 117.443 128.707 1.00 45.13 1  27  LYS D NZ    1 
ATOM   13590 N  N     . GLN D 2 49  ? 135.242 110.554 127.136 1.00 34.66 ?  28  GLN D N     1 
ATOM   13591 C  CA    . GLN D 2 49  ? 136.621 110.077 127.204 1.00 34.64 ?  28  GLN D CA    1 
ATOM   13592 C  C     . GLN D 2 49  ? 136.826 108.817 126.366 1.00 34.20 ?  28  GLN D C     1 
ATOM   13593 O  O     . GLN D 2 49  ? 137.890 108.200 126.438 1.00 34.53 ?  28  GLN D O     1 
ATOM   13594 C  CB    . GLN D 2 49  ? 137.028 109.784 128.662 1.00 34.89 ?  28  GLN D CB    1 
ATOM   13595 C  CG    . GLN D 2 49  ? 137.578 110.982 129.433 1.00 36.47 ?  28  GLN D CG    1 
ATOM   13596 C  CD    . GLN D 2 49  ? 137.787 110.706 130.924 1.00 38.37 ?  28  GLN D CD    1 
ATOM   13597 O  OE1   . GLN D 2 49  ? 137.656 111.611 131.748 1.00 40.68 ?  28  GLN D OE1   1 
ATOM   13598 N  NE2   . GLN D 2 49  ? 138.108 109.460 131.274 1.00 38.57 ?  28  GLN D NE2   1 
ATOM   13599 N  N     . PHE D 2 50  ? 135.820 108.425 125.583 1.00 33.42 ?  29  PHE D N     1 
ATOM   13600 C  CA    . PHE D 2 50  ? 135.906 107.183 124.815 1.00 32.57 ?  29  PHE D CA    1 
ATOM   13601 C  C     . PHE D 2 50  ? 137.057 107.256 123.811 1.00 32.60 ?  29  PHE D C     1 
ATOM   13602 O  O     . PHE D 2 50  ? 137.278 108.290 123.175 1.00 32.39 ?  29  PHE D O     1 
ATOM   13603 C  CB    . PHE D 2 50  ? 134.580 106.848 124.115 1.00 32.77 ?  29  PHE D CB    1 
ATOM   13604 C  CG    . PHE D 2 50  ? 134.609 105.550 123.332 1.00 32.24 ?  29  PHE D CG    1 
ATOM   13605 C  CD1   . PHE D 2 50  ? 134.558 104.322 123.986 1.00 31.50 ?  29  PHE D CD1   1 
ATOM   13606 C  CD2   . PHE D 2 50  ? 134.692 105.561 121.945 1.00 33.60 ?  29  PHE D CD2   1 
ATOM   13607 C  CE1   . PHE D 2 50  ? 134.588 103.132 123.276 1.00 33.02 ?  29  PHE D CE1   1 
ATOM   13608 C  CE2   . PHE D 2 50  ? 134.727 104.369 121.217 1.00 33.78 ?  29  PHE D CE2   1 
ATOM   13609 C  CZ    . PHE D 2 50  ? 134.667 103.154 121.882 1.00 33.13 ?  29  PHE D CZ    1 
ATOM   13610 N  N     . TRP D 2 51  ? 137.787 106.155 123.690 1.00 31.95 ?  30  TRP D N     1 
ATOM   13611 C  CA    . TRP D 2 51  ? 138.930 106.063 122.781 1.00 32.03 ?  30  TRP D CA    1 
ATOM   13612 C  C     . TRP D 2 51  ? 139.136 104.610 122.376 1.00 33.03 ?  30  TRP D C     1 
ATOM   13613 O  O     . TRP D 2 51  ? 138.546 103.701 122.966 1.00 32.54 ?  30  TRP D O     1 
ATOM   13614 C  CB    . TRP D 2 51  ? 140.199 106.647 123.420 1.00 31.19 ?  30  TRP D CB    1 
ATOM   13615 C  CG    . TRP D 2 51  ? 140.639 105.935 124.684 1.00 28.11 ?  30  TRP D CG    1 
ATOM   13616 C  CD1   . TRP D 2 51  ? 140.115 106.089 125.930 1.00 26.51 ?  30  TRP D CD1   1 
ATOM   13617 C  CD2   . TRP D 2 51  ? 141.684 104.958 124.806 1.00 25.93 ?  30  TRP D CD2   1 
ATOM   13618 N  NE1   . TRP D 2 51  ? 140.772 105.273 126.828 1.00 24.52 ?  30  TRP D NE1   1 
ATOM   13619 C  CE2   . TRP D 2 51  ? 141.736 104.567 126.165 1.00 24.42 ?  30  TRP D CE2   1 
ATOM   13620 C  CE3   . TRP D 2 51  ? 142.587 104.379 123.902 1.00 25.37 ?  30  TRP D CE3   1 
ATOM   13621 C  CZ2   . TRP D 2 51  ? 142.659 103.626 126.643 1.00 24.00 ?  30  TRP D CZ2   1 
ATOM   13622 C  CZ3   . TRP D 2 51  ? 143.500 103.436 124.378 1.00 24.99 ?  30  TRP D CZ3   1 
ATOM   13623 C  CH2   . TRP D 2 51  ? 143.526 103.070 125.735 1.00 23.72 ?  30  TRP D CH2   1 
ATOM   13624 N  N     . LEU D 2 52  ? 139.963 104.404 121.356 1.00 34.81 ?  31  LEU D N     1 
ATOM   13625 C  CA    . LEU D 2 52  ? 140.254 103.080 120.829 1.00 36.58 ?  31  LEU D CA    1 
ATOM   13626 C  C     . LEU D 2 52  ? 141.759 102.910 120.644 1.00 37.80 ?  31  LEU D C     1 
ATOM   13627 O  O     . LEU D 2 52  ? 142.451 103.876 120.335 1.00 37.92 ?  31  LEU D O     1 
ATOM   13628 C  CB    . LEU D 2 52  ? 139.517 102.856 119.498 1.00 36.95 ?  31  LEU D CB    1 
ATOM   13629 C  CG    . LEU D 2 52  ? 138.038 102.456 119.527 1.00 38.15 ?  31  LEU D CG    1 
ATOM   13630 C  CD1   . LEU D 2 52  ? 137.604 101.950 118.156 1.00 39.50 ?  31  LEU D CD1   1 
ATOM   13631 C  CD2   . LEU D 2 52  ? 137.754 101.388 120.577 1.00 37.94 ?  31  LEU D CD2   1 
ATOM   13632 N  N     . PRO D 2 53  ? 142.275 101.678 120.826 1.00 39.26 ?  32  PRO D N     1 
ATOM   13633 C  CA    . PRO D 2 53  ? 143.716 101.394 120.694 1.00 40.41 ?  32  PRO D CA    1 
ATOM   13634 C  C     . PRO D 2 53  ? 144.311 101.837 119.350 1.00 41.91 ?  32  PRO D C     1 
ATOM   13635 O  O     . PRO D 2 53  ? 145.388 102.443 119.318 1.00 42.52 ?  32  PRO D O     1 
ATOM   13636 C  CB    . PRO D 2 53  ? 143.784 99.867  120.807 1.00 40.42 ?  32  PRO D CB    1 
ATOM   13637 C  CG    . PRO D 2 53  ? 142.539 99.472  121.493 1.00 40.01 ?  32  PRO D CG    1 
ATOM   13638 C  CD    . PRO D 2 53  ? 141.496 100.456 121.098 1.00 39.30 ?  32  PRO D CD    1 
ATOM   13639 N  N     . GLU D 2 54  ? 143.599 101.553 118.263 1.00 43.27 ?  33  GLU D N     1 
ATOM   13640 C  CA    . GLU D 2 54  ? 144.034 101.865 116.892 1.00 45.17 ?  33  GLU D CA    1 
ATOM   13641 C  C     . GLU D 2 54  ? 144.428 103.330 116.644 1.00 45.57 ?  33  GLU D C     1 
ATOM   13642 O  O     . GLU D 2 54  ? 145.160 103.626 115.695 1.00 46.08 ?  33  GLU D O     1 
ATOM   13643 C  CB    . GLU D 2 54  ? 142.943 101.453 115.892 1.00 45.55 ?  33  GLU D CB    1 
ATOM   13644 C  CG    . GLU D 2 54  ? 142.933 99.967  115.526 1.00 48.19 ?  33  GLU D CG    1 
ATOM   13645 C  CD    . GLU D 2 54  ? 142.629 99.048  116.702 1.00 50.61 ?  33  GLU D CD    1 
ATOM   13646 O  OE1   . GLU D 2 54  ? 141.655 99.318  117.443 1.00 51.10 ?  33  GLU D OE1   1 
ATOM   13647 O  OE2   . GLU D 2 54  ? 143.375 98.056  116.883 1.00 52.64 -1 33  GLU D OE2   1 
ATOM   13648 N  N     . GLU D 2 55  ? 143.943 104.234 117.495 1.00 45.74 ?  34  GLU D N     1 
ATOM   13649 C  CA    . GLU D 2 55  ? 144.190 105.673 117.342 1.00 46.28 ?  34  GLU D CA    1 
ATOM   13650 C  C     . GLU D 2 55  ? 145.662 106.060 117.532 1.00 46.49 ?  34  GLU D C     1 
ATOM   13651 O  O     . GLU D 2 55  ? 146.137 107.031 116.934 1.00 46.73 ?  34  GLU D O     1 
ATOM   13652 C  CB    . GLU D 2 55  ? 143.304 106.483 118.294 1.00 46.17 ?  34  GLU D CB    1 
ATOM   13653 C  CG    . GLU D 2 55  ? 141.799 106.356 118.041 1.00 47.10 ?  34  GLU D CG    1 
ATOM   13654 C  CD    . GLU D 2 55  ? 140.975 107.231 118.983 1.00 48.43 ?  34  GLU D CD    1 
ATOM   13655 O  OE1   . GLU D 2 55  ? 141.110 108.473 118.921 1.00 49.62 ?  34  GLU D OE1   1 
ATOM   13656 O  OE2   . GLU D 2 55  ? 140.192 106.679 119.784 1.00 47.11 -1 34  GLU D OE2   1 
ATOM   13657 N  N     . ILE D 2 56  ? 146.374 105.305 118.368 1.00 46.23 ?  35  ILE D N     1 
ATOM   13658 C  CA    . ILE D 2 56  ? 147.794 105.546 118.611 1.00 46.25 ?  35  ILE D CA    1 
ATOM   13659 C  C     . ILE D 2 56  ? 148.623 104.520 117.840 1.00 46.30 ?  35  ILE D C     1 
ATOM   13660 O  O     . ILE D 2 56  ? 148.483 103.312 118.054 1.00 46.36 ?  35  ILE D O     1 
ATOM   13661 C  CB    . ILE D 2 56  ? 148.151 105.471 120.137 1.00 45.84 ?  35  ILE D CB    1 
ATOM   13662 C  CG1   . ILE D 2 56  ? 147.096 106.170 121.020 1.00 46.15 ?  35  ILE D CG1   1 
ATOM   13663 C  CG2   . ILE D 2 56  ? 149.580 105.987 120.403 1.00 45.72 ?  35  ILE D CG2   1 
ATOM   13664 C  CD1   . ILE D 2 56  ? 146.931 107.669 120.802 1.00 47.27 ?  35  ILE D CD1   1 
ATOM   13665 N  N     . ALA D 2 57  ? 149.474 104.999 116.938 1.00 46.51 ?  36  ALA D N     1 
ATOM   13666 C  CA    . ALA D 2 57  ? 150.415 104.130 116.226 1.00 46.56 ?  36  ALA D CA    1 
ATOM   13667 C  C     . ALA D 2 57  ? 151.575 103.772 117.160 1.00 46.08 ?  36  ALA D C     1 
ATOM   13668 O  O     . ALA D 2 57  ? 152.216 104.662 117.716 1.00 45.70 ?  36  ALA D O     1 
ATOM   13669 C  CB    . ALA D 2 57  ? 150.929 104.812 114.961 1.00 47.10 ?  36  ALA D CB    1 
ATOM   13670 N  N     . LEU D 2 58  ? 151.845 102.477 117.315 1.00 45.66 ?  37  LEU D N     1 
ATOM   13671 C  CA    . LEU D 2 58  ? 152.831 102.012 118.303 1.00 45.27 ?  37  LEU D CA    1 
ATOM   13672 C  C     . LEU D 2 58  ? 154.248 101.765 117.790 1.00 45.25 ?  37  LEU D C     1 
ATOM   13673 O  O     . LEU D 2 58  ? 155.201 101.760 118.577 1.00 44.82 ?  37  LEU D O     1 
ATOM   13674 C  CB    . LEU D 2 58  ? 152.322 100.759 119.015 1.00 45.05 ?  37  LEU D CB    1 
ATOM   13675 C  CG    . LEU D 2 58  ? 151.292 101.021 120.111 1.00 45.41 ?  37  LEU D CG    1 
ATOM   13676 C  CD1   . LEU D 2 58  ? 150.814 99.705  120.694 1.00 45.40 ?  37  LEU D CD1   1 
ATOM   13677 C  CD2   . LEU D 2 58  ? 151.872 101.920 121.202 1.00 44.70 ?  37  LEU D CD2   1 
ATOM   13678 N  N     . ASN D 2 59  ? 154.392 101.575 116.482 1.00 45.33 ?  38  ASN D N     1 
ATOM   13679 C  CA    . ASN D 2 59  ? 155.659 101.102 115.916 1.00 45.22 ?  38  ASN D CA    1 
ATOM   13680 C  C     . ASN D 2 59  ? 156.883 101.987 116.191 1.00 44.39 ?  38  ASN D C     1 
ATOM   13681 O  O     . ASN D 2 59  ? 157.999 101.474 116.336 1.00 44.33 ?  38  ASN D O     1 
ATOM   13682 C  CB    . ASN D 2 59  ? 155.508 100.835 114.421 1.00 46.22 ?  38  ASN D CB    1 
ATOM   13683 C  CG    . ASN D 2 59  ? 156.330 99.645  113.957 1.00 47.90 ?  38  ASN D CG    1 
ATOM   13684 O  OD1   . ASN D 2 59  ? 157.230 99.783  113.130 1.00 49.28 ?  38  ASN D OD1   1 
ATOM   13685 N  ND2   . ASN D 2 59  ? 156.019 98.462  114.491 1.00 49.18 ?  38  ASN D ND2   1 
ATOM   13686 N  N     . GLY D 2 60  ? 156.666 103.301 116.284 1.00 43.45 ?  39  GLY D N     1 
ATOM   13687 C  CA    . GLY D 2 60  ? 157.737 104.264 116.559 1.00 42.42 ?  39  GLY D CA    1 
ATOM   13688 C  C     . GLY D 2 60  ? 158.390 104.165 117.936 1.00 41.55 ?  39  GLY D C     1 
ATOM   13689 O  O     . GLY D 2 60  ? 159.391 104.837 118.205 1.00 41.29 ?  39  GLY D O     1 
ATOM   13690 N  N     . ASP D 2 61  ? 157.826 103.339 118.814 1.00 40.35 ?  40  ASP D N     1 
ATOM   13691 C  CA    . ASP D 2 61  ? 158.434 103.075 120.123 1.00 39.53 ?  40  ASP D CA    1 
ATOM   13692 C  C     . ASP D 2 61  ? 159.699 102.232 120.036 1.00 39.38 ?  40  ASP D C     1 
ATOM   13693 O  O     . ASP D 2 61  ? 160.545 102.281 120.926 1.00 38.90 ?  40  ASP D O     1 
ATOM   13694 C  CB    . ASP D 2 61  ? 157.439 102.386 121.045 1.00 38.93 ?  40  ASP D CB    1 
ATOM   13695 C  CG    . ASP D 2 61  ? 156.550 103.359 121.765 1.00 38.21 ?  40  ASP D CG    1 
ATOM   13696 O  OD1   . ASP D 2 61  ? 156.706 104.586 121.576 1.00 38.79 ?  40  ASP D OD1   1 
ATOM   13697 O  OD2   . ASP D 2 61  ? 155.694 102.891 122.533 1.00 38.02 -1 40  ASP D OD2   1 
ATOM   13698 N  N     . LEU D 2 62  ? 159.818 101.461 118.960 1.00 39.82 ?  41  LEU D N     1 
ATOM   13699 C  CA    . LEU D 2 62  ? 160.968 100.590 118.750 1.00 40.22 ?  41  LEU D CA    1 
ATOM   13700 C  C     . LEU D 2 62  ? 162.265 101.387 118.612 1.00 40.40 ?  41  LEU D C     1 
ATOM   13701 O  O     . LEU D 2 62  ? 163.352 100.847 118.820 1.00 40.91 ?  41  LEU D O     1 
ATOM   13702 C  CB    . LEU D 2 62  ? 160.735 99.693  117.532 1.00 40.52 ?  41  LEU D CB    1 
ATOM   13703 C  CG    . LEU D 2 62  ? 159.597 98.673  117.654 1.00 41.03 ?  41  LEU D CG    1 
ATOM   13704 C  CD1   . LEU D 2 62  ? 159.410 97.918  116.345 1.00 42.53 ?  41  LEU D CD1   1 
ATOM   13705 C  CD2   . LEU D 2 62  ? 159.832 97.702  118.819 1.00 41.89 ?  41  LEU D CD2   1 
ATOM   13706 N  N     . LEU D 2 63  ? 162.129 102.675 118.284 1.00 40.20 ?  42  LEU D N     1 
ATOM   13707 C  CA    . LEU D 2 63  ? 163.253 103.598 118.129 1.00 39.85 ?  42  LEU D CA    1 
ATOM   13708 C  C     . LEU D 2 63  ? 163.849 104.065 119.470 1.00 38.90 ?  42  LEU D C     1 
ATOM   13709 O  O     . LEU D 2 63  ? 164.960 104.609 119.509 1.00 39.48 ?  42  LEU D O     1 
ATOM   13710 C  CB    . LEU D 2 63  ? 162.812 104.801 117.280 1.00 40.50 ?  42  LEU D CB    1 
ATOM   13711 C  CG    . LEU D 2 63  ? 163.774 105.528 116.327 1.00 41.98 ?  42  LEU D CG    1 
ATOM   13712 C  CD1   . LEU D 2 63  ? 164.417 104.585 115.315 1.00 43.07 ?  42  LEU D CD1   1 
ATOM   13713 C  CD2   . LEU D 2 63  ? 163.024 106.622 115.588 1.00 43.17 ?  42  LEU D CD2   1 
ATOM   13714 N  N     . THR D 2 64  ? 163.121 103.873 120.567 1.00 37.28 ?  43  THR D N     1 
ATOM   13715 C  CA    . THR D 2 64  ? 163.688 104.140 121.898 1.00 35.53 ?  43  THR D CA    1 
ATOM   13716 C  C     . THR D 2 64  ? 163.844 102.866 122.720 1.00 34.57 ?  43  THR D C     1 
ATOM   13717 O  O     . THR D 2 64  ? 164.734 102.775 123.570 1.00 34.23 ?  43  THR D O     1 
ATOM   13718 C  CB    . THR D 2 64  ? 162.904 105.202 122.701 1.00 35.18 ?  43  THR D CB    1 
ATOM   13719 O  OG1   . THR D 2 64  ? 161.503 104.913 122.676 1.00 34.59 ?  43  THR D OG1   1 
ATOM   13720 C  CG2   . THR D 2 64  ? 163.141 106.573 122.131 1.00 35.48 ?  43  THR D CG2   1 
ATOM   13721 N  N     . TRP D 2 65  ? 162.980 101.888 122.449 1.00 33.62 ?  44  TRP D N     1 
ATOM   13722 C  CA    . TRP D 2 65  ? 163.011 100.580 123.123 1.00 32.87 ?  44  TRP D CA    1 
ATOM   13723 C  C     . TRP D 2 65  ? 164.366 99.881  122.954 1.00 33.46 ?  44  TRP D C     1 
ATOM   13724 O  O     . TRP D 2 65  ? 164.914 99.336  123.913 1.00 32.58 ?  44  TRP D O     1 
ATOM   13725 C  CB    . TRP D 2 65  ? 161.877 99.691  122.587 1.00 32.09 ?  44  TRP D CB    1 
ATOM   13726 C  CG    . TRP D 2 65  ? 161.842 98.299  123.153 1.00 30.42 ?  44  TRP D CG    1 
ATOM   13727 C  CD1   . TRP D 2 65  ? 162.204 97.147  122.511 1.00 29.35 ?  44  TRP D CD1   1 
ATOM   13728 C  CD2   . TRP D 2 65  ? 161.415 97.909  124.468 1.00 28.04 ?  44  TRP D CD2   1 
ATOM   13729 N  NE1   . TRP D 2 65  ? 162.030 96.066  123.342 1.00 28.44 ?  44  TRP D NE1   1 
ATOM   13730 C  CE2   . TRP D 2 65  ? 161.551 96.505  124.549 1.00 28.14 ?  44  TRP D CE2   1 
ATOM   13731 C  CE3   . TRP D 2 65  ? 160.940 98.608  125.585 1.00 27.11 ?  44  TRP D CE3   1 
ATOM   13732 C  CZ2   . TRP D 2 65  ? 161.221 95.781  125.703 1.00 27.21 ?  44  TRP D CZ2   1 
ATOM   13733 C  CZ3   . TRP D 2 65  ? 160.603 97.886  126.734 1.00 27.45 ?  44  TRP D CZ3   1 
ATOM   13734 C  CH2   . TRP D 2 65  ? 160.742 96.485  126.777 1.00 27.25 ?  44  TRP D CH2   1 
ATOM   13735 N  N     . LYS D 2 66  ? 164.890 99.917  121.729 1.00 34.52 ?  45  LYS D N     1 
ATOM   13736 C  CA    . LYS D 2 66  ? 166.180 99.321  121.396 1.00 36.41 ?  45  LYS D CA    1 
ATOM   13737 C  C     . LYS D 2 66  ? 167.356 99.911  122.174 1.00 36.26 ?  45  LYS D C     1 
ATOM   13738 O  O     . LYS D 2 66  ? 168.399 99.268  122.291 1.00 36.52 ?  45  LYS D O     1 
ATOM   13739 C  CB    . LYS D 2 66  ? 166.447 99.423  119.888 1.00 36.98 ?  45  LYS D CB    1 
ATOM   13740 C  CG    . LYS D 2 66  ? 166.201 98.123  119.126 1.00 40.03 ?  45  LYS D CG    1 
ATOM   13741 C  CD    . LYS D 2 66  ? 164.713 97.764  119.038 1.00 43.70 ?  45  LYS D CD    1 
ATOM   13742 C  CE    . LYS D 2 66  ? 164.494 96.488  118.219 1.00 45.57 ?  45  LYS D CE    1 
ATOM   13743 N  NZ    . LYS D 2 66  ? 164.950 96.621  116.804 1.00 46.59 1  45  LYS D NZ    1 
ATOM   13744 N  N     . TYR D 2 67  ? 167.178 101.114 122.712 1.00 36.26 ?  46  TYR D N     1 
ATOM   13745 C  CA    . TYR D 2 67  ? 168.254 101.777 123.457 1.00 36.90 ?  46  TYR D CA    1 
ATOM   13746 C  C     . TYR D 2 67  ? 168.203 101.587 124.974 1.00 36.28 ?  46  TYR D C     1 
ATOM   13747 O  O     . TYR D 2 67  ? 169.075 102.083 125.681 1.00 36.44 ?  46  TYR D O     1 
ATOM   13748 C  CB    . TYR D 2 67  ? 168.343 103.265 123.101 1.00 37.15 ?  46  TYR D CB    1 
ATOM   13749 C  CG    . TYR D 2 67  ? 168.548 103.524 121.627 1.00 39.40 ?  46  TYR D CG    1 
ATOM   13750 C  CD1   . TYR D 2 67  ? 169.459 102.766 120.885 1.00 41.26 ?  46  TYR D CD1   1 
ATOM   13751 C  CD2   . TYR D 2 67  ? 167.855 104.541 120.978 1.00 41.06 ?  46  TYR D CD2   1 
ATOM   13752 C  CE1   . TYR D 2 67  ? 169.651 102.998 119.524 1.00 43.03 ?  46  TYR D CE1   1 
ATOM   13753 C  CE2   . TYR D 2 67  ? 168.046 104.788 119.616 1.00 43.05 ?  46  TYR D CE2   1 
ATOM   13754 C  CZ    . TYR D 2 67  ? 168.944 104.016 118.896 1.00 43.80 ?  46  TYR D CZ    1 
ATOM   13755 O  OH    . TYR D 2 67  ? 169.127 104.260 117.547 1.00 45.18 ?  46  TYR D OH    1 
ATOM   13756 N  N     . LEU D 2 68  ? 167.190 100.884 125.476 1.00 35.71 ?  47  LEU D N     1 
ATOM   13757 C  CA    . LEU D 2 68  ? 167.115 100.595 126.909 1.00 34.92 ?  47  LEU D CA    1 
ATOM   13758 C  C     . LEU D 2 68  ? 167.984 99.384  127.265 1.00 34.32 ?  47  LEU D C     1 
ATOM   13759 O  O     . LEU D 2 68  ? 168.141 98.463  126.459 1.00 34.50 ?  47  LEU D O     1 
ATOM   13760 C  CB    . LEU D 2 68  ? 165.666 100.363 127.362 1.00 35.00 ?  47  LEU D CB    1 
ATOM   13761 C  CG    . LEU D 2 68  ? 164.586 101.403 127.016 1.00 35.82 ?  47  LEU D CG    1 
ATOM   13762 C  CD1   . LEU D 2 68  ? 163.240 100.960 127.569 1.00 35.95 ?  47  LEU D CD1   1 
ATOM   13763 C  CD2   . LEU D 2 68  ? 164.931 102.807 127.513 1.00 35.97 ?  47  LEU D CD2   1 
ATOM   13764 N  N     . GLY D 2 69  ? 168.543 99.397  128.473 1.00 33.50 ?  48  GLY D N     1 
ATOM   13765 C  CA    . GLY D 2 69  ? 169.257 98.245  129.018 1.00 32.41 ?  48  GLY D CA    1 
ATOM   13766 C  C     . GLY D 2 69  ? 168.339 97.062  129.292 1.00 32.15 ?  48  GLY D C     1 
ATOM   13767 O  O     . GLY D 2 69  ? 167.109 97.199  129.294 1.00 30.98 ?  48  GLY D O     1 
ATOM   13768 N  N     . LYS D 2 70  ? 168.942 95.901  129.536 1.00 32.14 ?  49  LYS D N     1 
ATOM   13769 C  CA    . LYS D 2 70  ? 168.193 94.682  129.827 1.00 32.25 ?  49  LYS D CA    1 
ATOM   13770 C  C     . LYS D 2 70  ? 167.316 94.816  131.070 1.00 31.24 ?  49  LYS D C     1 
ATOM   13771 O  O     . LYS D 2 70  ? 166.171 94.370  131.052 1.00 31.34 ?  49  LYS D O     1 
ATOM   13772 C  CB    . LYS D 2 70  ? 169.132 93.482  129.969 1.00 33.07 ?  49  LYS D CB    1 
ATOM   13773 C  CG    . LYS D 2 70  ? 169.914 93.159  128.705 1.00 35.74 ?  49  LYS D CG    1 
ATOM   13774 C  CD    . LYS D 2 70  ? 171.021 92.154  129.011 1.00 39.67 ?  49  LYS D CD    1 
ATOM   13775 C  CE    . LYS D 2 70  ? 172.015 92.057  127.864 1.00 40.96 ?  49  LYS D CE    1 
ATOM   13776 N  NZ    . LYS D 2 70  ? 173.224 91.316  128.300 1.00 42.55 1  49  LYS D NZ    1 
ATOM   13777 N  N     . ASN D 2 71  ? 167.845 95.432  132.132 1.00 29.92 ?  50  ASN D N     1 
ATOM   13778 C  CA    . ASN D 2 71  ? 167.081 95.630  133.369 1.00 29.37 ?  50  ASN D CA    1 
ATOM   13779 C  C     . ASN D 2 71  ? 165.873 96.536  133.152 1.00 28.35 ?  50  ASN D C     1 
ATOM   13780 O  O     . ASN D 2 71  ? 164.795 96.273  133.700 1.00 27.64 ?  50  ASN D O     1 
ATOM   13781 C  CB    . ASN D 2 71  ? 167.948 96.179  134.518 1.00 29.38 ?  50  ASN D CB    1 
ATOM   13782 C  CG    . ASN D 2 71  ? 168.854 95.119  135.142 1.00 31.22 ?  50  ASN D CG    1 
ATOM   13783 O  OD1   . ASN D 2 71  ? 168.524 93.932  135.179 1.00 33.03 ?  50  ASN D OD1   1 
ATOM   13784 N  ND2   . ASN D 2 71  ? 170.003 95.554  135.649 1.00 31.97 ?  50  ASN D ND2   1 
ATOM   13785 N  N     . GLU D 2 72  ? 166.054 97.586  132.347 1.00 27.72 ?  51  GLU D N     1 
ATOM   13786 C  CA    . GLU D 2 72  ? 164.952 98.502  132.014 1.00 27.70 ?  51  GLU D CA    1 
ATOM   13787 C  C     . GLU D 2 72  ? 163.857 97.796  131.212 1.00 27.62 ?  51  GLU D C     1 
ATOM   13788 O  O     . GLU D 2 72  ? 162.663 97.985  131.468 1.00 27.56 ?  51  GLU D O     1 
ATOM   13789 C  CB    . GLU D 2 72  ? 165.454 99.722  131.234 1.00 27.55 ?  51  GLU D CB    1 
ATOM   13790 C  CG    . GLU D 2 72  ? 166.500 100.574 131.963 1.00 28.77 ?  51  GLU D CG    1 
ATOM   13791 C  CD    . GLU D 2 72  ? 166.850 101.825 131.177 1.00 31.18 ?  51  GLU D CD    1 
ATOM   13792 O  OE1   . GLU D 2 72  ? 167.533 101.706 130.138 1.00 33.17 ?  51  GLU D OE1   1 
ATOM   13793 O  OE2   . GLU D 2 72  ? 166.432 102.923 131.594 1.00 31.66 -1 51  GLU D OE2   1 
ATOM   13794 N  N     . GLN D 2 73  ? 164.271 96.984  130.244 1.00 27.32 ?  52  GLN D N     1 
ATOM   13795 C  CA    . GLN D 2 73  ? 163.334 96.241  129.406 1.00 27.33 ?  52  GLN D CA    1 
ATOM   13796 C  C     . GLN D 2 73  ? 162.601 95.186  130.239 1.00 26.85 ?  52  GLN D C     1 
ATOM   13797 O  O     . GLN D 2 73  ? 161.387 95.011  130.100 1.00 26.24 ?  52  GLN D O     1 
ATOM   13798 C  CB    . GLN D 2 73  ? 164.054 95.602  128.225 1.00 27.65 ?  52  GLN D CB    1 
ATOM   13799 C  CG    . GLN D 2 73  ? 164.488 96.588  127.123 1.00 29.66 ?  52  GLN D CG    1 
ATOM   13800 C  CD    . GLN D 2 73  ? 165.028 95.891  125.875 1.00 32.60 ?  52  GLN D CD    1 
ATOM   13801 O  OE1   . GLN D 2 73  ? 165.439 94.735  125.924 1.00 34.76 ?  52  GLN D OE1   1 
ATOM   13802 N  NE2   . GLN D 2 73  ? 165.044 96.603  124.758 1.00 33.42 ?  52  GLN D NE2   1 
ATOM   13803 N  N     . ASP D 2 74  ? 163.344 94.525  131.124 1.00 26.26 ?  53  ASP D N     1 
ATOM   13804 C  CA    . ASP D 2 74  ? 162.802 93.512  132.038 1.00 26.50 ?  53  ASP D CA    1 
ATOM   13805 C  C     . ASP D 2 74  ? 161.778 94.115  132.988 1.00 25.81 ?  53  ASP D C     1 
ATOM   13806 O  O     . ASP D 2 74  ? 160.689 93.570  133.152 1.00 26.12 ?  53  ASP D O     1 
ATOM   13807 C  CB    . ASP D 2 74  ? 163.944 92.873  132.841 1.00 26.84 ?  53  ASP D CB    1 
ATOM   13808 C  CG    . ASP D 2 74  ? 163.490 91.701  133.711 1.00 29.50 ?  53  ASP D CG    1 
ATOM   13809 O  OD1   . ASP D 2 74  ? 163.032 90.673  133.168 1.00 32.08 ?  53  ASP D OD1   1 
ATOM   13810 O  OD2   . ASP D 2 74  ? 163.637 91.792  134.947 1.00 33.52 -1 53  ASP D OD2   1 
ATOM   13811 N  N     . THR D 2 75  ? 162.121 95.239  133.615 1.00 25.10 ?  54  THR D N     1 
ATOM   13812 C  CA    . THR D 2 75  ? 161.197 95.898  134.542 1.00 24.11 ?  54  THR D CA    1 
ATOM   13813 C  C     . THR D 2 75  ? 159.922 96.328  133.812 1.00 23.82 ?  54  THR D C     1 
ATOM   13814 O  O     . THR D 2 75  ? 158.815 96.065  134.283 1.00 23.81 ?  54  THR D O     1 
ATOM   13815 C  CB    . THR D 2 75  ? 161.859 97.090  135.262 1.00 23.80 ?  54  THR D CB    1 
ATOM   13816 O  OG1   . THR D 2 75  ? 162.947 96.606  136.061 1.00 24.62 ?  54  THR D OG1   1 
ATOM   13817 C  CG2   . THR D 2 75  ? 160.850 97.813  136.171 1.00 23.25 ?  54  THR D CG2   1 
ATOM   13818 N  N     . TYR D 2 76  ? 160.087 96.994  132.678 1.00 24.06 ?  55  TYR D N     1 
ATOM   13819 C  CA    . TYR D 2 76  ? 158.953 97.419  131.862 1.00 24.76 ?  55  TYR D CA    1 
ATOM   13820 C  C     . TYR D 2 76  ? 158.008 96.261  131.510 1.00 24.85 ?  55  TYR D C     1 
ATOM   13821 O  O     . TYR D 2 76  ? 156.792 96.377  131.690 1.00 24.83 ?  55  TYR D O     1 
ATOM   13822 C  CB    . TYR D 2 76  ? 159.428 98.112  130.585 1.00 24.78 ?  55  TYR D CB    1 
ATOM   13823 C  CG    . TYR D 2 76  ? 158.367 98.993  129.959 1.00 26.19 ?  55  TYR D CG    1 
ATOM   13824 C  CD1   . TYR D 2 76  ? 158.273 100.341 130.307 1.00 27.81 ?  55  TYR D CD1   1 
ATOM   13825 C  CD2   . TYR D 2 76  ? 157.449 98.483  129.035 1.00 28.03 ?  55  TYR D CD2   1 
ATOM   13826 C  CE1   . TYR D 2 76  ? 157.307 101.166 129.746 1.00 29.32 ?  55  TYR D CE1   1 
ATOM   13827 C  CE2   . TYR D 2 76  ? 156.467 99.306  128.464 1.00 29.01 ?  55  TYR D CE2   1 
ATOM   13828 C  CZ    . TYR D 2 76  ? 156.409 100.646 128.830 1.00 30.76 ?  55  TYR D CZ    1 
ATOM   13829 O  OH    . TYR D 2 76  ? 155.466 101.487 128.287 1.00 34.50 ?  55  TYR D OH    1 
ATOM   13830 N  N     . MET D 2 77  ? 158.568 95.161  131.010 1.00 25.76 ?  56  MET D N     1 
ATOM   13831 C  CA    . MET D 2 77  ? 157.777 93.971  130.677 1.00 26.81 ?  56  MET D CA    1 
ATOM   13832 C  C     . MET D 2 77  ? 156.991 93.453  131.886 1.00 26.23 ?  56  MET D C     1 
ATOM   13833 O  O     . MET D 2 77  ? 155.799 93.157  131.782 1.00 25.00 ?  56  MET D O     1 
ATOM   13834 C  CB    . MET D 2 77  ? 158.671 92.860  130.128 1.00 28.11 ?  56  MET D CB    1 
ATOM   13835 C  CG    . MET D 2 77  ? 159.267 93.128  128.741 1.00 32.52 ?  56  MET D CG    1 
ATOM   13836 S  SD    . MET D 2 77  ? 158.076 93.016  127.395 1.00 42.68 ?  56  MET D SD    1 
ATOM   13837 C  CE    . MET D 2 77  ? 157.376 94.665  127.355 1.00 38.97 ?  56  MET D CE    1 
ATOM   13838 N  N     . LYS D 2 78  ? 157.677 93.342  133.024 1.00 26.01 ?  57  LYS D N     1 
ATOM   13839 C  CA    . LYS D 2 78  ? 157.070 92.816  134.250 1.00 26.07 ?  57  LYS D CA    1 
ATOM   13840 C  C     . LYS D 2 78  ? 155.965 93.724  134.787 1.00 25.69 ?  57  LYS D C     1 
ATOM   13841 O  O     . LYS D 2 78  ? 154.922 93.244  135.248 1.00 25.58 ?  57  LYS D O     1 
ATOM   13842 C  CB    . LYS D 2 78  ? 158.132 92.567  135.329 1.00 26.08 ?  57  LYS D CB    1 
ATOM   13843 C  CG    . LYS D 2 78  ? 159.075 91.397  135.011 1.00 27.64 ?  57  LYS D CG    1 
ATOM   13844 C  CD    . LYS D 2 78  ? 160.212 91.304  136.021 1.00 29.47 ?  57  LYS D CD    1 
ATOM   13845 C  CE    . LYS D 2 78  ? 161.006 90.024  135.817 1.00 31.69 ?  57  LYS D CE    1 
ATOM   13846 N  NZ    . LYS D 2 78  ? 162.113 89.885  136.801 1.00 33.36 1  57  LYS D NZ    1 
ATOM   13847 N  N     . VAL D 2 79  ? 156.202 95.033  134.726 1.00 25.32 ?  58  VAL D N     1 
ATOM   13848 C  CA    . VAL D 2 79  ? 155.221 96.030  135.169 1.00 25.47 ?  58  VAL D CA    1 
ATOM   13849 C  C     . VAL D 2 79  ? 153.989 95.952  134.272 1.00 25.09 ?  58  VAL D C     1 
ATOM   13850 O  O     . VAL D 2 79  ? 152.853 95.906  134.751 1.00 24.46 ?  58  VAL D O     1 
ATOM   13851 C  CB    . VAL D 2 79  ? 155.845 97.454  135.133 1.00 25.83 ?  58  VAL D CB    1 
ATOM   13852 C  CG1   . VAL D 2 79  ? 154.791 98.520  134.932 1.00 27.35 ?  58  VAL D CG1   1 
ATOM   13853 C  CG2   . VAL D 2 79  ? 156.670 97.696  136.396 1.00 26.42 ?  58  VAL D CG2   1 
ATOM   13854 N  N     . LEU D 2 80  ? 154.238 95.888  132.966 1.00 25.27 ?  59  LEU D N     1 
ATOM   13855 C  CA    . LEU D 2 80  ? 153.179 95.852  131.983 1.00 25.55 ?  59  LEU D CA    1 
ATOM   13856 C  C     . LEU D 2 80  ? 152.296 94.623  132.196 1.00 24.94 ?  59  LEU D C     1 
ATOM   13857 O  O     . LEU D 2 80  ? 151.072 94.729  132.156 1.00 24.82 ?  59  LEU D O     1 
ATOM   13858 C  CB    . LEU D 2 80  ? 153.772 95.842  130.572 1.00 25.80 ?  59  LEU D CB    1 
ATOM   13859 C  CG    . LEU D 2 80  ? 153.416 96.913  129.534 1.00 28.76 ?  59  LEU D CG    1 
ATOM   13860 C  CD1   . LEU D 2 80  ? 153.478 96.273  128.147 1.00 30.25 ?  59  LEU D CD1   1 
ATOM   13861 C  CD2   . LEU D 2 80  ? 152.066 97.577  129.749 1.00 27.79 ?  59  LEU D CD2   1 
ATOM   13862 N  N     . ALA D 2 81  ? 152.924 93.470  132.428 1.00 24.86 ?  60  ALA D N     1 
ATOM   13863 C  CA    . ALA D 2 81  ? 152.194 92.215  132.659 1.00 24.60 ?  60  ALA D CA    1 
ATOM   13864 C  C     . ALA D 2 81  ? 151.387 92.292  133.952 1.00 23.80 ?  60  ALA D C     1 
ATOM   13865 O  O     . ALA D 2 81  ? 150.269 91.796  134.024 1.00 24.07 ?  60  ALA D O     1 
ATOM   13866 C  CB    . ALA D 2 81  ? 153.158 91.031  132.700 1.00 24.48 ?  60  ALA D CB    1 
ATOM   13867 N  N     . GLY D 2 82  ? 151.962 92.925  134.968 1.00 23.54 ?  61  GLY D N     1 
ATOM   13868 C  CA    . GLY D 2 82  ? 151.266 93.160  136.228 1.00 22.53 ?  61  GLY D CA    1 
ATOM   13869 C  C     . GLY D 2 82  ? 149.990 93.950  136.020 1.00 22.23 ?  61  GLY D C     1 
ATOM   13870 O  O     . GLY D 2 82  ? 148.925 93.559  136.497 1.00 21.27 ?  61  GLY D O     1 
ATOM   13871 N  N     . LEU D 2 83  ? 150.095 95.064  135.298 1.00 22.36 ?  62  LEU D N     1 
ATOM   13872 C  CA    . LEU D 2 83  ? 148.922 95.895  134.997 1.00 22.42 ?  62  LEU D CA    1 
ATOM   13873 C  C     . LEU D 2 83  ? 147.889 95.121  134.191 1.00 22.91 ?  62  LEU D C     1 
ATOM   13874 O  O     . LEU D 2 83  ? 146.686 95.194  134.478 1.00 22.99 ?  62  LEU D O     1 
ATOM   13875 C  CB    . LEU D 2 83  ? 149.322 97.166  134.237 1.00 22.19 ?  62  LEU D CB    1 
ATOM   13876 C  CG    . LEU D 2 83  ? 150.196 98.179  134.993 1.00 22.17 ?  62  LEU D CG    1 
ATOM   13877 C  CD1   . LEU D 2 83  ? 150.788 99.195  134.006 1.00 21.55 ?  62  LEU D CD1   1 
ATOM   13878 C  CD2   . LEU D 2 83  ? 149.371 98.874  136.062 1.00 22.42 ?  62  LEU D CD2   1 
ATOM   13879 N  N     . THR D 2 84  ? 148.360 94.366  133.204 1.00 23.39 ?  63  THR D N     1 
ATOM   13880 C  CA    . THR D 2 84  ? 147.472 93.600  132.333 1.00 24.42 ?  63  THR D CA    1 
ATOM   13881 C  C     . THR D 2 84  ? 146.653 92.589  133.138 1.00 24.55 ?  63  THR D C     1 
ATOM   13882 O  O     . THR D 2 84  ? 145.428 92.523  133.008 1.00 23.68 ?  63  THR D O     1 
ATOM   13883 C  CB    . THR D 2 84  ? 148.253 92.866  131.214 1.00 24.70 ?  63  THR D CB    1 
ATOM   13884 O  OG1   . THR D 2 84  ? 148.968 93.824  130.423 1.00 25.57 ?  63  THR D OG1   1 
ATOM   13885 C  CG2   . THR D 2 84  ? 147.296 92.110  130.308 1.00 25.36 ?  63  THR D CG2   1 
ATOM   13886 N  N     . LEU D 2 85  ? 147.351 91.817  133.965 1.00 25.38 ?  64  LEU D N     1 
ATOM   13887 C  CA    . LEU D 2 85  ? 146.721 90.790  134.784 1.00 26.44 ?  64  LEU D CA    1 
ATOM   13888 C  C     . LEU D 2 85  ? 145.698 91.373  135.763 1.00 25.96 ?  64  LEU D C     1 
ATOM   13889 O  O     . LEU D 2 85  ? 144.571 90.864  135.844 1.00 25.83 ?  64  LEU D O     1 
ATOM   13890 C  CB    . LEU D 2 85  ? 147.776 89.909  135.472 1.00 26.65 ?  64  LEU D CB    1 
ATOM   13891 C  CG    . LEU D 2 85  ? 148.423 88.898  134.505 1.00 29.62 ?  64  LEU D CG    1 
ATOM   13892 C  CD1   . LEU D 2 85  ? 149.789 88.444  134.984 1.00 31.57 ?  64  LEU D CD1   1 
ATOM   13893 C  CD2   . LEU D 2 85  ? 147.519 87.676  134.257 1.00 30.96 ?  64  LEU D CD2   1 
ATOM   13894 N  N     . LEU D 2 86  ? 146.057 92.454  136.459 1.00 25.63 ?  65  LEU D N     1 
ATOM   13895 C  CA    . LEU D 2 86  ? 145.104 93.100  137.365 1.00 25.59 ?  65  LEU D CA    1 
ATOM   13896 C  C     . LEU D 2 86  ? 143.890 93.691  136.648 1.00 25.60 ?  65  LEU D C     1 
ATOM   13897 O  O     . LEU D 2 86  ? 142.768 93.632  137.159 1.00 25.47 ?  65  LEU D O     1 
ATOM   13898 C  CB    . LEU D 2 86  ? 145.777 94.165  138.252 1.00 25.76 ?  65  LEU D CB    1 
ATOM   13899 C  CG    . LEU D 2 86  ? 146.747 93.641  139.319 1.00 26.71 ?  65  LEU D CG    1 
ATOM   13900 C  CD1   . LEU D 2 86  ? 147.592 94.765  139.912 1.00 28.01 ?  65  LEU D CD1   1 
ATOM   13901 C  CD2   . LEU D 2 86  ? 146.015 92.911  140.421 1.00 28.01 ?  65  LEU D CD2   1 
ATOM   13902 N  N     . ASP D 2 87  ? 144.110 94.269  135.473 1.00 25.49 ?  66  ASP D N     1 
ATOM   13903 C  CA    . ASP D 2 87  ? 143.026 94.914  134.751 1.00 25.83 ?  66  ASP D CA    1 
ATOM   13904 C  C     . ASP D 2 87  ? 142.018 93.901  134.191 1.00 26.20 ?  66  ASP D C     1 
ATOM   13905 O  O     . ASP D 2 87  ? 140.833 94.195  134.083 1.00 25.99 ?  66  ASP D O     1 
ATOM   13906 C  CB    . ASP D 2 87  ? 143.573 95.810  133.648 1.00 25.50 ?  66  ASP D CB    1 
ATOM   13907 C  CG    . ASP D 2 87  ? 142.697 97.005  133.401 1.00 25.76 ?  66  ASP D CG    1 
ATOM   13908 O  OD1   . ASP D 2 87  ? 142.007 97.439  134.355 1.00 26.91 ?  66  ASP D OD1   1 
ATOM   13909 O  OD2   . ASP D 2 87  ? 142.690 97.517  132.265 1.00 23.11 -1 66  ASP D OD2   1 
ATOM   13910 N  N     . THR D 2 88  ? 142.502 92.705  133.864 1.00 27.12 ?  67  THR D N     1 
ATOM   13911 C  CA    . THR D 2 88  ? 141.653 91.608  133.421 1.00 28.40 ?  67  THR D CA    1 
ATOM   13912 C  C     . THR D 2 88  ? 140.694 91.172  134.516 1.00 28.28 ?  67  THR D C     1 
ATOM   13913 O  O     . THR D 2 88  ? 139.521 90.920  134.248 1.00 28.10 ?  67  THR D O     1 
ATOM   13914 C  CB    . THR D 2 88  ? 142.489 90.404  132.944 1.00 29.04 ?  67  THR D CB    1 
ATOM   13915 O  OG1   . THR D 2 88  ? 143.326 90.821  131.864 1.00 31.00 ?  67  THR D OG1   1 
ATOM   13916 C  CG2   . THR D 2 88  ? 141.582 89.279  132.450 1.00 30.16 ?  67  THR D CG2   1 
ATOM   13917 N  N     . GLU D 2 89  ? 141.185 91.087  135.752 1.00 28.28 ?  68  GLU D N     1 
ATOM   13918 C  CA    . GLU D 2 89  ? 140.310 90.778  136.877 1.00 29.16 ?  68  GLU D CA    1 
ATOM   13919 C  C     . GLU D 2 89  ? 139.217 91.839  136.995 1.00 28.65 ?  68  GLU D C     1 
ATOM   13920 O  O     . GLU D 2 89  ? 138.063 91.514  137.232 1.00 28.44 ?  68  GLU D O     1 
ATOM   13921 C  CB    . GLU D 2 89  ? 141.091 90.675  138.195 1.00 29.32 ?  68  GLU D CB    1 
ATOM   13922 C  CG    . GLU D 2 89  ? 142.172 89.586  138.215 1.00 31.95 ?  68  GLU D CG    1 
ATOM   13923 C  CD    . GLU D 2 89  ? 141.625 88.167  138.086 1.00 35.19 ?  68  GLU D CD    1 
ATOM   13924 O  OE1   . GLU D 2 89  ? 140.409 87.944  138.283 1.00 35.47 ?  68  GLU D OE1   1 
ATOM   13925 O  OE2   . GLU D 2 89  ? 142.429 87.264  137.778 1.00 38.06 -1 68  GLU D OE2   1 
ATOM   13926 N  N     . GLN D 2 90  ? 139.588 93.103  136.811 1.00 28.45 ?  69  GLN D N     1 
ATOM   13927 C  CA    . GLN D 2 90  ? 138.622 94.197  136.925 1.00 28.47 ?  69  GLN D CA    1 
ATOM   13928 C  C     . GLN D 2 90  ? 137.554 94.137  135.824 1.00 28.97 ?  69  GLN D C     1 
ATOM   13929 O  O     . GLN D 2 90  ? 136.381 94.400  136.084 1.00 28.84 ?  69  GLN D O     1 
ATOM   13930 C  CB    . GLN D 2 90  ? 139.336 95.552  136.948 1.00 28.21 ?  69  GLN D CB    1 
ATOM   13931 C  CG    . GLN D 2 90  ? 138.488 96.708  137.477 1.00 27.75 ?  69  GLN D CG    1 
ATOM   13932 C  CD    . GLN D 2 90  ? 138.235 96.655  138.980 1.00 28.91 ?  69  GLN D CD    1 
ATOM   13933 O  OE1   . GLN D 2 90  ? 138.327 95.596  139.615 1.00 27.62 ?  69  GLN D OE1   1 
ATOM   13934 N  NE2   . GLN D 2 90  ? 137.889 97.808  139.554 1.00 28.23 ?  69  GLN D NE2   1 
ATOM   13935 N  N     . GLY D 2 91  ? 137.961 93.766  134.610 1.00 29.62 ?  70  GLY D N     1 
ATOM   13936 C  CA    . GLY D 2 91  ? 137.030 93.616  133.490 1.00 30.43 ?  70  GLY D CA    1 
ATOM   13937 C  C     . GLY D 2 91  ? 136.119 92.396  133.570 1.00 31.11 ?  70  GLY D C     1 
ATOM   13938 O  O     . GLY D 2 91  ? 134.931 92.468  133.240 1.00 30.77 ?  70  GLY D O     1 
ATOM   13939 N  N     . ASN D 2 92  ? 136.672 91.270  133.995 1.00 31.69 ?  71  ASN D N     1 
ATOM   13940 C  CA    . ASN D 2 92  ? 135.885 90.045  134.070 1.00 32.72 ?  71  ASN D CA    1 
ATOM   13941 C  C     . ASN D 2 92  ? 135.031 89.900  135.322 1.00 32.60 ?  71  ASN D C     1 
ATOM   13942 O  O     . ASN D 2 92  ? 133.977 89.261  135.271 1.00 33.12 ?  71  ASN D O     1 
ATOM   13943 C  CB    . ASN D 2 92  ? 136.777 88.824  133.892 1.00 33.68 ?  71  ASN D CB    1 
ATOM   13944 C  CG    . ASN D 2 92  ? 137.265 88.671  132.467 1.00 35.15 ?  71  ASN D CG    1 
ATOM   13945 O  OD1   . ASN D 2 92  ? 138.319 88.093  132.232 1.00 40.21 ?  71  ASN D OD1   1 
ATOM   13946 N  ND2   . ASN D 2 92  ? 136.504 89.201  131.507 1.00 36.91 ?  71  ASN D ND2   1 
ATOM   13947 N  N     . THR D 2 93  ? 135.474 90.505  136.425 1.00 31.76 ?  72  THR D N     1 
ATOM   13948 C  CA    . THR D 2 93  ? 134.813 90.329  137.712 1.00 31.47 ?  72  THR D CA    1 
ATOM   13949 C  C     . THR D 2 93  ? 134.465 91.640  138.414 1.00 30.62 ?  72  THR D C     1 
ATOM   13950 O  O     . THR D 2 93  ? 133.298 91.891  138.702 1.00 30.71 ?  72  THR D O     1 
ATOM   13951 C  CB    . THR D 2 93  ? 135.658 89.461  138.641 1.00 31.60 ?  72  THR D CB    1 
ATOM   13952 O  OG1   . THR D 2 93  ? 135.935 88.215  137.987 1.00 33.14 ?  72  THR D OG1   1 
ATOM   13953 C  CG2   . THR D 2 93  ? 134.926 89.198  139.947 1.00 31.89 ?  72  THR D CG2   1 
ATOM   13954 N  N     . GLY D 2 94  ? 135.476 92.466  138.677 1.00 29.61 ?  73  GLY D N     1 
ATOM   13955 C  CA    . GLY D 2 94  ? 135.309 93.679  139.479 1.00 28.47 ?  73  GLY D CA    1 
ATOM   13956 C  C     . GLY D 2 94  ? 134.189 94.607  139.053 1.00 27.90 ?  73  GLY D C     1 
ATOM   13957 O  O     . GLY D 2 94  ? 133.309 94.951  139.854 1.00 28.27 ?  73  GLY D O     1 
ATOM   13958 N  N     . MET D 2 95  ? 134.217 95.045  137.802 1.00 26.67 ?  74  MET D N     1 
ATOM   13959 C  CA    . MET D 2 95  ? 133.167 95.955  137.352 1.00 26.00 ?  74  MET D CA    1 
ATOM   13960 C  C     . MET D 2 95  ? 131.839 95.235  137.145 1.00 25.25 ?  74  MET D C     1 
ATOM   13961 O  O     . MET D 2 95  ? 130.809 95.758  137.548 1.00 24.97 ?  74  MET D O     1 
ATOM   13962 C  CB    . MET D 2 95  ? 133.565 96.752  136.104 1.00 26.00 ?  74  MET D CB    1 
ATOM   13963 C  CG    . MET D 2 95  ? 134.464 97.930  136.393 1.00 26.40 ?  74  MET D CG    1 
ATOM   13964 S  SD    . MET D 2 95  ? 133.721 99.176  137.476 1.00 28.10 ?  74  MET D SD    1 
ATOM   13965 C  CE    . MET D 2 95  ? 135.141 100.240 137.702 1.00 28.95 ?  74  MET D CE    1 
ATOM   13966 N  N     . PRO D 2 96  ? 131.853 94.046  136.511 1.00 24.98 ?  75  PRO D N     1 
ATOM   13967 C  CA    . PRO D 2 96  ? 130.536 93.412  136.319 1.00 24.59 ?  75  PRO D CA    1 
ATOM   13968 C  C     . PRO D 2 96  ? 129.847 92.994  137.615 1.00 23.90 ?  75  PRO D C     1 
ATOM   13969 O  O     . PRO D 2 96  ? 128.622 93.020  137.670 1.00 23.45 ?  75  PRO D O     1 
ATOM   13970 C  CB    . PRO D 2 96  ? 130.851 92.174  135.470 1.00 24.80 ?  75  PRO D CB    1 
ATOM   13971 C  CG    . PRO D 2 96  ? 132.131 92.527  134.746 1.00 25.75 ?  75  PRO D CG    1 
ATOM   13972 C  CD    . PRO D 2 96  ? 132.908 93.375  135.720 1.00 25.07 ?  75  PRO D CD    1 
ATOM   13973 N  N     . ILE D 2 97  ? 130.612 92.603  138.638 1.00 23.36 ?  76  ILE D N     1 
ATOM   13974 C  CA    . ILE D 2 97  ? 130.000 92.165  139.888 1.00 23.48 ?  76  ILE D CA    1 
ATOM   13975 C  C     . ILE D 2 97  ? 129.380 93.341  140.625 1.00 23.30 ?  76  ILE D C     1 
ATOM   13976 O  O     . ILE D 2 97  ? 128.317 93.203  141.225 1.00 23.45 ?  76  ILE D O     1 
ATOM   13977 C  CB    . ILE D 2 97  ? 130.979 91.366  140.795 1.00 23.96 ?  76  ILE D CB    1 
ATOM   13978 C  CG1   . ILE D 2 97  ? 130.212 90.425  141.718 1.00 24.71 ?  76  ILE D CG1   1 
ATOM   13979 C  CG2   . ILE D 2 97  ? 131.923 92.292  141.600 1.00 24.02 ?  76  ILE D CG2   1 
ATOM   13980 C  CD1   . ILE D 2 97  ? 130.985 89.114  142.003 1.00 29.17 ?  76  ILE D CD1   1 
ATOM   13981 N  N     . VAL D 2 98  ? 130.038 94.499  140.568 1.00 22.71 ?  77  VAL D N     1 
ATOM   13982 C  CA    . VAL D 2 98  ? 129.499 95.715  141.198 1.00 22.78 ?  77  VAL D CA    1 
ATOM   13983 C  C     . VAL D 2 98  ? 128.250 96.191  140.453 1.00 22.89 ?  77  VAL D C     1 
ATOM   13984 O  O     . VAL D 2 98  ? 127.249 96.552  141.073 1.00 23.72 ?  77  VAL D O     1 
ATOM   13985 C  CB    . VAL D 2 98  ? 130.580 96.826  141.318 1.00 22.49 ?  77  VAL D CB    1 
ATOM   13986 C  CG1   . VAL D 2 98  ? 129.969 98.168  141.760 1.00 21.91 ?  77  VAL D CG1   1 
ATOM   13987 C  CG2   . VAL D 2 98  ? 131.648 96.394  142.309 1.00 23.02 ?  77  VAL D CG2   1 
ATOM   13988 N  N     . ALA D 2 99  ? 128.296 96.156  139.122 1.00 23.19 ?  78  ALA D N     1 
ATOM   13989 C  CA    . ALA D 2 99  ? 127.126 96.516  138.308 1.00 23.05 ?  78  ALA D CA    1 
ATOM   13990 C  C     . ALA D 2 99  ? 125.928 95.622  138.642 1.00 23.52 ?  78  ALA D C     1 
ATOM   13991 O  O     . ALA D 2 99  ? 124.780 96.078  138.681 1.00 23.68 ?  78  ALA D O     1 
ATOM   13992 C  CB    . ALA D 2 99  ? 127.466 96.439  136.829 1.00 22.81 ?  78  ALA D CB    1 
ATOM   13993 N  N     . GLU D 2 100 ? 126.197 94.344  138.893 1.00 23.68 ?  79  GLU D N     1 
ATOM   13994 C  CA    . GLU D 2 100 ? 125.143 93.398  139.250 1.00 24.14 ?  79  GLU D CA    1 
ATOM   13995 C  C     . GLU D 2 100 ? 124.425 93.726  140.570 1.00 23.66 ?  79  GLU D C     1 
ATOM   13996 O  O     . GLU D 2 100 ? 123.198 93.624  140.660 1.00 22.94 ?  79  GLU D O     1 
ATOM   13997 C  CB    . GLU D 2 100 ? 125.720 91.984  139.300 1.00 24.47 ?  79  GLU D CB    1 
ATOM   13998 C  CG    . GLU D 2 100 ? 124.673 90.894  139.429 1.00 27.90 ?  79  GLU D CG    1 
ATOM   13999 C  CD    . GLU D 2 100 ? 125.283 89.522  139.654 1.00 32.30 ?  79  GLU D CD    1 
ATOM   14000 O  OE1   . GLU D 2 100 ? 126.442 89.298  139.237 1.00 32.88 ?  79  GLU D OE1   1 
ATOM   14001 O  OE2   . GLU D 2 100 ? 124.597 88.671  140.257 1.00 34.74 -1 79  GLU D OE2   1 
ATOM   14002 N  N     . HIS D 2 101 ? 125.187 94.109  141.594 1.00 23.62 ?  80  HIS D N     1 
ATOM   14003 C  CA    . HIS D 2 101 ? 124.614 94.343  142.932 1.00 23.99 ?  80  HIS D CA    1 
ATOM   14004 C  C     . HIS D 2 101 ? 124.138 95.771  143.229 1.00 24.35 ?  80  HIS D C     1 
ATOM   14005 O  O     . HIS D 2 101 ? 123.366 95.979  144.167 1.00 24.21 ?  80  HIS D O     1 
ATOM   14006 C  CB    . HIS D 2 101 ? 125.579 93.849  144.020 1.00 24.13 ?  80  HIS D CB    1 
ATOM   14007 C  CG    . HIS D 2 101 ? 125.782 92.363  144.004 1.00 24.76 ?  80  HIS D CG    1 
ATOM   14008 N  ND1   . HIS D 2 101 ? 125.040 91.501  144.785 1.00 25.68 ?  80  HIS D ND1   1 
ATOM   14009 C  CD2   . HIS D 2 101 ? 126.625 91.586  143.284 1.00 25.75 ?  80  HIS D CD2   1 
ATOM   14010 C  CE1   . HIS D 2 101 ? 125.423 90.257  144.548 1.00 26.21 ?  80  HIS D CE1   1 
ATOM   14011 N  NE2   . HIS D 2 101 ? 126.383 90.281  143.643 1.00 25.35 ?  80  HIS D NE2   1 
ATOM   14012 N  N     . VAL D 2 102 ? 124.599 96.750  142.453 1.00 24.50 ?  81  VAL D N     1 
ATOM   14013 C  CA    . VAL D 2 102 ? 124.160 98.135  142.622 1.00 25.50 ?  81  VAL D CA    1 
ATOM   14014 C  C     . VAL D 2 102 ? 122.747 98.317  142.045 1.00 26.14 ?  81  VAL D C     1 
ATOM   14015 O  O     . VAL D 2 102 ? 122.469 97.850  140.943 1.00 26.96 ?  81  VAL D O     1 
ATOM   14016 C  CB    . VAL D 2 102 ? 125.153 99.128  141.951 1.00 25.30 ?  81  VAL D CB    1 
ATOM   14017 C  CG1   . VAL D 2 102 ? 124.570 100.520 141.882 1.00 27.08 ?  81  VAL D CG1   1 
ATOM   14018 C  CG2   . VAL D 2 102 ? 126.462 99.165  142.722 1.00 25.41 ?  81  VAL D CG2   1 
ATOM   14019 N  N     . ASP D 2 103 ? 121.868 98.975  142.796 1.00 26.45 ?  82  ASP D N     1 
ATOM   14020 C  CA    . ASP D 2 103 ? 120.526 99.307  142.311 1.00 27.15 ?  82  ASP D CA    1 
ATOM   14021 C  C     . ASP D 2 103 ? 120.526 100.664 141.622 1.00 26.39 ?  82  ASP D C     1 
ATOM   14022 O  O     . ASP D 2 103 ? 121.199 101.602 142.068 1.00 26.40 ?  82  ASP D O     1 
ATOM   14023 C  CB    . ASP D 2 103 ? 119.508 99.320  143.457 1.00 27.72 ?  82  ASP D CB    1 
ATOM   14024 C  CG    . ASP D 2 103 ? 119.346 97.962  144.130 1.00 31.46 ?  82  ASP D CG    1 
ATOM   14025 O  OD1   . ASP D 2 103 ? 119.483 96.904  143.458 1.00 34.26 ?  82  ASP D OD1   1 
ATOM   14026 O  OD2   . ASP D 2 103 ? 119.068 97.952  145.351 1.00 35.52 -1 82  ASP D OD2   1 
ATOM   14027 N  N     . GLY D 2 104 ? 119.752 100.766 140.546 1.00 25.52 ?  83  GLY D N     1 
ATOM   14028 C  CA    . GLY D 2 104 ? 119.618 102.019 139.806 1.00 24.31 ?  83  GLY D CA    1 
ATOM   14029 C  C     . GLY D 2 104 ? 119.996 101.789 138.348 1.00 23.27 ?  83  GLY D C     1 
ATOM   14030 O  O     . GLY D 2 104 ? 121.093 101.318 138.050 1.00 22.38 ?  83  GLY D O     1 
ATOM   14031 N  N     . HIS D 2 105 ? 119.079 102.106 137.438 1.00 22.46 ?  84  HIS D N     1 
ATOM   14032 C  CA    . HIS D 2 105 ? 119.333 101.914 136.009 1.00 22.17 ?  84  HIS D CA    1 
ATOM   14033 C  C     . HIS D 2 105 ? 120.497 102.739 135.485 1.00 21.13 ?  84  HIS D C     1 
ATOM   14034 O  O     . HIS D 2 105 ? 121.277 102.256 134.667 1.00 20.91 ?  84  HIS D O     1 
ATOM   14035 C  CB    . HIS D 2 105 ? 118.068 102.204 135.190 1.00 22.07 ?  84  HIS D CB    1 
ATOM   14036 C  CG    . HIS D 2 105 ? 116.914 101.329 135.565 1.00 23.85 ?  84  HIS D CG    1 
ATOM   14037 N  ND1   . HIS D 2 105 ? 117.020 99.956  135.621 1.00 24.86 ?  84  HIS D ND1   1 
ATOM   14038 C  CD2   . HIS D 2 105 ? 115.649 101.628 135.937 1.00 25.19 ?  84  HIS D CD2   1 
ATOM   14039 C  CE1   . HIS D 2 105 ? 115.860 99.444  135.993 1.00 24.94 ?  84  HIS D CE1   1 
ATOM   14040 N  NE2   . HIS D 2 105 ? 115.014 100.438 136.196 1.00 26.41 ?  84  HIS D NE2   1 
ATOM   14041 N  N     . GLN D 2 106 ? 120.612 103.974 135.951 1.00 20.66 ?  85  GLN D N     1 
ATOM   14042 C  CA    . GLN D 2 106 ? 121.628 104.873 135.410 1.00 20.70 ?  85  GLN D CA    1 
ATOM   14043 C  C     . GLN D 2 106 ? 123.012 104.466 135.912 1.00 20.46 ?  85  GLN D C     1 
ATOM   14044 O  O     . GLN D 2 106 ? 123.982 104.508 135.155 1.00 20.72 ?  85  GLN D O     1 
ATOM   14045 C  CB    . GLN D 2 106 ? 121.279 106.345 135.685 1.00 20.60 ?  85  GLN D CB    1 
ATOM   14046 C  CG    . GLN D 2 106 ? 119.943 106.779 135.024 1.00 20.74 ?  85  GLN D CG    1 
ATOM   14047 C  CD    . GLN D 2 106 ? 119.457 108.175 135.436 1.00 22.11 ?  85  GLN D CD    1 
ATOM   14048 O  OE1   . GLN D 2 106 ? 120.250 109.051 135.764 1.00 22.88 ?  85  GLN D OE1   1 
ATOM   14049 N  NE2   . GLN D 2 106 ? 118.143 108.381 135.403 1.00 21.64 ?  85  GLN D NE2   1 
ATOM   14050 N  N     . ARG D 2 107 ? 123.085 104.023 137.169 1.00 20.17 ?  86  ARG D N     1 
ATOM   14051 C  CA    . ARG D 2 107 ? 124.338 103.524 137.740 1.00 20.29 ?  86  ARG D CA    1 
ATOM   14052 C  C     . ARG D 2 107 ? 124.789 102.260 137.028 1.00 20.07 ?  86  ARG D C     1 
ATOM   14053 O  O     . ARG D 2 107 ? 125.967 102.103 136.737 1.00 19.53 ?  86  ARG D O     1 
ATOM   14054 C  CB    . ARG D 2 107 ? 124.182 103.227 139.230 1.00 20.88 ?  86  ARG D CB    1 
ATOM   14055 C  CG    . ARG D 2 107 ? 123.762 104.422 140.022 1.00 22.56 ?  86  ARG D CG    1 
ATOM   14056 C  CD    . ARG D 2 107 ? 123.305 104.015 141.400 1.00 27.21 ?  86  ARG D CD    1 
ATOM   14057 N  NE    . ARG D 2 107 ? 123.416 105.193 142.240 1.00 31.70 ?  86  ARG D NE    1 
ATOM   14058 C  CZ    . ARG D 2 107 ? 123.491 105.185 143.554 1.00 32.23 ?  86  ARG D CZ    1 
ATOM   14059 N  NH1   . ARG D 2 107 ? 123.454 104.038 144.231 1.00 34.27 1  86  ARG D NH1   1 
ATOM   14060 N  NH2   . ARG D 2 107 ? 123.610 106.342 144.180 1.00 33.79 ?  86  ARG D NH2   1 
ATOM   14061 N  N     . LYS D 2 108 ? 123.848 101.351 136.765 1.00 19.61 ?  87  LYS D N     1 
ATOM   14062 C  CA    . LYS D 2 108 ? 124.177 100.131 136.030 1.00 19.92 ?  87  LYS D CA    1 
ATOM   14063 C  C     . LYS D 2 108 ? 124.728 100.442 134.634 1.00 20.08 ?  87  LYS D C     1 
ATOM   14064 O  O     . LYS D 2 108 ? 125.607 99.730  134.137 1.00 20.38 ?  87  LYS D O     1 
ATOM   14065 C  CB    . LYS D 2 108 ? 122.983 99.178  135.942 1.00 19.54 ?  87  LYS D CB    1 
ATOM   14066 C  CG    . LYS D 2 108 ? 122.557 98.587  137.273 1.00 20.55 ?  87  LYS D CG    1 
ATOM   14067 C  CD    . LYS D 2 108 ? 121.379 97.625  137.105 1.00 21.09 ?  87  LYS D CD    1 
ATOM   14068 C  CE    . LYS D 2 108 ? 120.964 96.989  138.427 1.00 22.98 ?  87  LYS D CE    1 
ATOM   14069 N  NZ    . LYS D 2 108 ? 121.987 95.974  138.886 1.00 22.30 1  87  LYS D NZ    1 
ATOM   14070 N  N     . ALA D 2 109 ? 124.207 101.494 134.004 1.00 19.72 ?  88  ALA D N     1 
ATOM   14071 C  CA    . ALA D 2 109 ? 124.665 101.877 132.674 1.00 19.83 ?  88  ALA D CA    1 
ATOM   14072 C  C     . ALA D 2 109 ? 126.097 102.414 132.711 1.00 19.84 ?  88  ALA D C     1 
ATOM   14073 O  O     . ALA D 2 109 ? 126.934 102.025 131.889 1.00 19.96 ?  88  ALA D O     1 
ATOM   14074 C  CB    . ALA D 2 109 ? 123.703 102.892 132.033 1.00 19.65 ?  88  ALA D CB    1 
ATOM   14075 N  N     . VAL D 2 110 ? 126.383 103.285 133.676 1.00 19.33 ?  89  VAL D N     1 
ATOM   14076 C  CA    . VAL D 2 110 ? 127.737 103.835 133.836 1.00 19.22 ?  89  VAL D CA    1 
ATOM   14077 C  C     . VAL D 2 110 ? 128.714 102.685 134.139 1.00 19.45 ?  89  VAL D C     1 
ATOM   14078 O  O     . VAL D 2 110 ? 129.737 102.524 133.459 1.00 18.97 ?  89  VAL D O     1 
ATOM   14079 C  CB    . VAL D 2 110 ? 127.762 104.966 134.904 1.00 19.01 ?  89  VAL D CB    1 
ATOM   14080 C  CG1   . VAL D 2 110 ? 129.213 105.427 135.229 1.00 19.90 ?  89  VAL D CG1   1 
ATOM   14081 C  CG2   . VAL D 2 110 ? 126.954 106.144 134.409 1.00 19.69 ?  89  VAL D CG2   1 
ATOM   14082 N  N     . LEU D 2 111 ? 128.354 101.843 135.109 1.00 19.27 ?  90  LEU D N     1 
ATOM   14083 C  CA    . LEU D 2 111 ? 129.180 100.678 135.436 1.00 19.96 ?  90  LEU D CA    1 
ATOM   14084 C  C     . LEU D 2 111 ? 129.416 99.742  134.244 1.00 20.30 ?  90  LEU D C     1 
ATOM   14085 O  O     . LEU D 2 111 ? 130.536 99.264  134.048 1.00 19.88 ?  90  LEU D O     1 
ATOM   14086 C  CB    . LEU D 2 111 ? 128.632 99.930  136.659 1.00 19.87 ?  90  LEU D CB    1 
ATOM   14087 C  CG    . LEU D 2 111 ? 128.734 100.737 137.955 1.00 20.24 ?  90  LEU D CG    1 
ATOM   14088 C  CD1   . LEU D 2 111 ? 127.884 100.151 139.094 1.00 21.85 ?  90  LEU D CD1   1 
ATOM   14089 C  CD2   . LEU D 2 111 ? 130.204 100.909 138.386 1.00 20.29 ?  90  LEU D CD2   1 
ATOM   14090 N  N     . ASN D 2 112 ? 128.376 99.503  133.441 1.00 20.92 ?  91  ASN D N     1 
ATOM   14091 C  CA    . ASN D 2 112 ? 128.530 98.746  132.177 1.00 20.70 ?  91  ASN D CA    1 
ATOM   14092 C  C     . ASN D 2 112 ? 129.517 99.386  131.216 1.00 20.57 ?  91  ASN D C     1 
ATOM   14093 O  O     . ASN D 2 112 ? 130.264 98.686  130.513 1.00 20.45 ?  91  ASN D O     1 
ATOM   14094 C  CB    . ASN D 2 112 ? 127.202 98.637  131.427 1.00 21.16 ?  91  ASN D CB    1 
ATOM   14095 C  CG    . ASN D 2 112 ? 126.465 97.343  131.707 1.00 21.98 ?  91  ASN D CG    1 
ATOM   14096 O  OD1   . ASN D 2 112 ? 126.877 96.530  132.540 1.00 25.37 ?  91  ASN D OD1   1 
ATOM   14097 N  ND2   . ASN D 2 112 ? 125.349 97.156  131.025 1.00 21.12 ?  91  ASN D ND2   1 
ATOM   14098 N  N     . PHE D 2 113 ? 129.456 100.712 131.122 1.00 19.70 ?  92  PHE D N     1 
ATOM   14099 C  CA    . PHE D 2 113 ? 130.375 101.436 130.271 1.00 20.02 ?  92  PHE D CA    1 
ATOM   14100 C  C     . PHE D 2 113 ? 131.824 101.250 130.749 1.00 19.97 ?  92  PHE D C     1 
ATOM   14101 O  O     . PHE D 2 113 ? 132.725 100.996 129.942 1.00 19.22 ?  92  PHE D O     1 
ATOM   14102 C  CB    . PHE D 2 113 ? 130.014 102.928 130.163 1.00 20.09 ?  92  PHE D CB    1 
ATOM   14103 C  CG    . PHE D 2 113 ? 130.841 103.650 129.158 1.00 20.54 ?  92  PHE D CG    1 
ATOM   14104 C  CD1   . PHE D 2 113 ? 130.433 103.720 127.825 1.00 20.14 ?  92  PHE D CD1   1 
ATOM   14105 C  CD2   . PHE D 2 113 ? 132.065 104.210 129.527 1.00 20.77 ?  92  PHE D CD2   1 
ATOM   14106 C  CE1   . PHE D 2 113 ? 131.224 104.364 126.877 1.00 20.54 ?  92  PHE D CE1   1 
ATOM   14107 C  CE2   . PHE D 2 113 ? 132.866 104.850 128.582 1.00 21.23 ?  92  PHE D CE2   1 
ATOM   14108 C  CZ    . PHE D 2 113 ? 132.438 104.921 127.250 1.00 20.92 ?  92  PHE D CZ    1 
ATOM   14109 N  N     . MET D 2 114 ? 132.033 101.366 132.057 1.00 19.67 ?  93  MET D N     1 
ATOM   14110 C  CA    . MET D 2 114 ? 133.353 101.143 132.633 1.00 20.55 ?  93  MET D CA    1 
ATOM   14111 C  C     . MET D 2 114 ? 133.856 99.717  132.398 1.00 20.82 ?  93  MET D C     1 
ATOM   14112 O  O     . MET D 2 114 ? 135.019 99.549  132.056 1.00 20.43 ?  93  MET D O     1 
ATOM   14113 C  CB    . MET D 2 114 ? 133.364 101.481 134.120 1.00 20.24 ?  93  MET D CB    1 
ATOM   14114 C  CG    . MET D 2 114 ? 132.937 102.915 134.362 1.00 22.05 ?  93  MET D CG    1 
ATOM   14115 S  SD    . MET D 2 114 ? 132.732 103.343 136.075 1.00 25.85 ?  93  MET D SD    1 
ATOM   14116 C  CE    . MET D 2 114 ? 132.957 105.125 135.963 1.00 27.57 ?  93  MET D CE    1 
ATOM   14117 N  N     . ALA D 2 115 ? 132.984 98.714  132.576 1.00 21.19 ?  94  ALA D N     1 
ATOM   14118 C  CA    . ALA D 2 115 ? 133.349 97.311  132.298 1.00 21.53 ?  94  ALA D CA    1 
ATOM   14119 C  C     . ALA D 2 115 ? 133.743 97.133  130.833 1.00 21.75 ?  94  ALA D C     1 
ATOM   14120 O  O     . ALA D 2 115 ? 134.737 96.470  130.536 1.00 22.18 ?  94  ALA D O     1 
ATOM   14121 C  CB    . ALA D 2 115 ? 132.215 96.352  132.677 1.00 21.32 ?  94  ALA D CB    1 
ATOM   14122 N  N     . MET D 2 116 ? 132.980 97.751  129.927 1.00 21.47 ?  95  MET D N     1 
ATOM   14123 C  CA    . MET D 2 116 ? 133.308 97.744  128.504 1.00 21.83 ?  95  MET D CA    1 
ATOM   14124 C  C     . MET D 2 116 ? 134.728 98.281  128.241 1.00 22.15 ?  95  MET D C     1 
ATOM   14125 O  O     . MET D 2 116 ? 135.491 97.670  127.495 1.00 22.09 ?  95  MET D O     1 
ATOM   14126 C  CB    . MET D 2 116 ? 132.262 98.540  127.704 1.00 21.72 ?  95  MET D CB    1 
ATOM   14127 C  CG    . MET D 2 116 ? 132.563 98.685  126.204 1.00 22.57 ?  95  MET D CG    1 
ATOM   14128 S  SD    . MET D 2 116 ? 133.788 99.958  125.800 1.00 22.75 ?  95  MET D SD    1 
ATOM   14129 C  CE    . MET D 2 116 ? 132.919 101.457 126.258 1.00 22.96 ?  95  MET D CE    1 
ATOM   14130 N  N     . MET D 2 117 ? 135.070 99.415  128.854 1.00 22.04 ?  96  MET D N     1 
ATOM   14131 C  CA    . MET D 2 117 ? 136.401 100.021 128.677 1.00 22.45 ?  96  MET D CA    1 
ATOM   14132 C  C     . MET D 2 117 ? 137.524 99.068  129.123 1.00 22.39 ?  96  MET D C     1 
ATOM   14133 O  O     . MET D 2 117 ? 138.560 98.970  128.463 1.00 21.88 ?  96  MET D O     1 
ATOM   14134 C  CB    . MET D 2 117 ? 136.501 101.375 129.409 1.00 22.00 ?  96  MET D CB    1 
ATOM   14135 C  CG    . MET D 2 117 ? 135.686 102.510 128.736 1.00 23.25 ?  96  MET D CG    1 
ATOM   14136 S  SD    . MET D 2 117 ? 136.162 102.834 127.022 1.00 24.28 ?  96  MET D SD    1 
ATOM   14137 C  CE    . MET D 2 117 ? 137.743 103.644 127.232 1.00 24.59 ?  96  MET D CE    1 
ATOM   14138 N  N     . GLU D 2 118 ? 137.304 98.354  130.227 1.00 22.66 ?  97  GLU D N     1 
ATOM   14139 C  CA    . GLU D 2 118 ? 138.283 97.371  130.707 1.00 23.52 ?  97  GLU D CA    1 
ATOM   14140 C  C     . GLU D 2 118 ? 138.523 96.275  129.684 1.00 24.25 ?  97  GLU D C     1 
ATOM   14141 O  O     . GLU D 2 118 ? 139.673 95.994  129.340 1.00 25.05 ?  97  GLU D O     1 
ATOM   14142 C  CB    . GLU D 2 118 ? 137.868 96.732  132.053 1.00 23.11 ?  97  GLU D CB    1 
ATOM   14143 C  CG    . GLU D 2 118 ? 137.331 97.688  133.126 1.00 23.08 ?  97  GLU D CG    1 
ATOM   14144 C  CD    . GLU D 2 118 ? 138.373 98.628  133.710 1.00 24.08 ?  97  GLU D CD    1 
ATOM   14145 O  OE1   . GLU D 2 118 ? 139.448 98.786  133.110 1.00 26.39 ?  97  GLU D OE1   1 
ATOM   14146 O  OE2   . GLU D 2 118 ? 138.104 99.238  134.766 1.00 27.52 -1 97  GLU D OE2   1 
ATOM   14147 N  N     . ASN D 2 119 ? 137.438 95.684  129.189 1.00 25.47 ?  98  ASN D N     1 
ATOM   14148 C  CA    . ASN D 2 119 ? 137.489 94.475  128.342 1.00 26.32 ?  98  ASN D CA    1 
ATOM   14149 C  C     . ASN D 2 119 ? 137.738 94.731  126.859 1.00 26.22 ?  98  ASN D C     1 
ATOM   14150 O  O     . ASN D 2 119 ? 138.447 93.953  126.188 1.00 26.54 ?  98  ASN D O     1 
ATOM   14151 C  CB    . ASN D 2 119 ? 136.196 93.656  128.502 1.00 26.72 ?  98  ASN D CB    1 
ATOM   14152 C  CG    . ASN D 2 119 ? 136.037 93.085  129.911 1.00 29.12 ?  98  ASN D CG    1 
ATOM   14153 O  OD1   . ASN D 2 119 ? 136.932 92.406  130.426 1.00 32.07 ?  98  ASN D OD1   1 
ATOM   14154 N  ND2   . ASN D 2 119 ? 134.911 93.386  130.548 1.00 29.12 ?  98  ASN D ND2   1 
ATOM   14155 N  N     . ALA D 2 120 ? 137.134 95.801  126.350 1.00 25.46 ?  99  ALA D N     1 
ATOM   14156 C  CA    . ALA D 2 120 ? 137.174 96.106  124.921 1.00 25.77 ?  99  ALA D CA    1 
ATOM   14157 C  C     . ALA D 2 120 ? 138.290 97.073  124.539 1.00 25.51 ?  99  ALA D C     1 
ATOM   14158 O  O     . ALA D 2 120 ? 138.769 97.044  123.402 1.00 26.64 ?  99  ALA D O     1 
ATOM   14159 C  CB    . ALA D 2 120 ? 135.816 96.649  124.446 1.00 25.75 ?  99  ALA D CB    1 
ATOM   14160 N  N     . VAL D 2 121 ? 138.697 97.930  125.469 1.00 24.40 ?  100 VAL D N     1 
ATOM   14161 C  CA    . VAL D 2 121 ? 139.647 98.986  125.138 1.00 24.15 ?  100 VAL D CA    1 
ATOM   14162 C  C     . VAL D 2 121 ? 140.993 98.780  125.838 1.00 23.94 ?  100 VAL D C     1 
ATOM   14163 O  O     . VAL D 2 121 ? 142.026 98.637  125.177 1.00 23.75 ?  100 VAL D O     1 
ATOM   14164 C  CB    . VAL D 2 121 ? 139.061 100.402 125.422 1.00 23.68 ?  100 VAL D CB    1 
ATOM   14165 C  CG1   . VAL D 2 121 ? 140.058 101.491 125.029 1.00 23.76 ?  100 VAL D CG1   1 
ATOM   14166 C  CG2   . VAL D 2 121 ? 137.750 100.593 124.653 1.00 23.99 ?  100 VAL D CG2   1 
ATOM   14167 N  N     . HIS D 2 122 ? 140.972 98.760  127.169 1.00 23.68 ?  101 HIS D N     1 
ATOM   14168 C  CA    . HIS D 2 122 ? 142.196 98.592  127.955 1.00 24.02 ?  101 HIS D CA    1 
ATOM   14169 C  C     . HIS D 2 122 ? 142.912 97.283  127.666 1.00 24.39 ?  101 HIS D C     1 
ATOM   14170 O  O     . HIS D 2 122 ? 144.122 97.284  127.455 1.00 24.71 ?  101 HIS D O     1 
ATOM   14171 C  CB    . HIS D 2 122 ? 141.936 98.732  129.460 1.00 23.20 ?  101 HIS D CB    1 
ATOM   14172 C  CG    . HIS D 2 122 ? 141.460 100.091 129.869 1.00 22.82 ?  101 HIS D CG    1 
ATOM   14173 N  ND1   . HIS D 2 122 ? 141.112 100.394 131.167 1.00 20.48 ?  101 HIS D ND1   1 
ATOM   14174 C  CD2   . HIS D 2 122 ? 141.248 101.220 129.149 1.00 21.03 ?  101 HIS D CD2   1 
ATOM   14175 C  CE1   . HIS D 2 122 ? 140.722 101.654 131.233 1.00 19.88 ?  101 HIS D CE1   1 
ATOM   14176 N  NE2   . HIS D 2 122 ? 140.797 102.179 130.022 1.00 21.62 ?  101 HIS D NE2   1 
ATOM   14177 N  N     . ALA D 2 123 ? 142.174 96.174  127.644 1.00 25.30 ?  102 ALA D N     1 
ATOM   14178 C  CA    . ALA D 2 123 ? 142.800 94.857  127.450 1.00 25.77 ?  102 ALA D CA    1 
ATOM   14179 C  C     . ALA D 2 123 ? 143.467 94.727  126.078 1.00 26.37 ?  102 ALA D C     1 
ATOM   14180 O  O     . ALA D 2 123 ? 144.557 94.153  125.956 1.00 25.87 ?  102 ALA D O     1 
ATOM   14181 C  CB    . ALA D 2 123 ? 141.784 93.728  127.673 1.00 26.43 ?  102 ALA D CB    1 
ATOM   14182 N  N     . LYS D 2 124 ? 142.808 95.265  125.051 1.00 26.51 ?  103 LYS D N     1 
ATOM   14183 C  CA    . LYS D 2 124 ? 143.353 95.264  123.701 1.00 27.22 ?  103 LYS D CA    1 
ATOM   14184 C  C     . LYS D 2 124 ? 144.587 96.174  123.616 1.00 26.63 ?  103 LYS D C     1 
ATOM   14185 O  O     . LYS D 2 124 ? 145.543 95.855  122.908 1.00 26.07 ?  103 LYS D O     1 
ATOM   14186 C  CB    . LYS D 2 124 ? 142.277 95.687  122.680 1.00 27.51 ?  103 LYS D CB    1 
ATOM   14187 C  CG    . LYS D 2 124 ? 142.759 95.810  121.218 1.00 30.58 ?  103 LYS D CG    1 
ATOM   14188 C  CD    . LYS D 2 124 ? 143.141 94.464  120.620 1.00 35.72 ?  103 LYS D CD    1 
ATOM   14189 C  CE    . LYS D 2 124 ? 143.648 94.591  119.181 1.00 37.33 ?  103 LYS D CE    1 
ATOM   14190 N  NZ    . LYS D 2 124 ? 142.559 95.052  118.280 1.00 40.73 1  103 LYS D NZ    1 
ATOM   14191 N  N     . SER D 2 125 ? 144.558 97.285  124.356 1.00 26.02 ?  104 SER D N     1 
ATOM   14192 C  CA    . SER D 2 125 ? 145.656 98.254  124.378 1.00 26.16 ?  104 SER D CA    1 
ATOM   14193 C  C     . SER D 2 125 ? 146.932 97.671  124.986 1.00 26.18 ?  104 SER D C     1 
ATOM   14194 O  O     . SER D 2 125 ? 148.027 97.877  124.450 1.00 26.06 ?  104 SER D O     1 
ATOM   14195 C  CB    . SER D 2 125 ? 145.255 99.526  125.129 1.00 26.10 ?  104 SER D CB    1 
ATOM   14196 O  OG    . SER D 2 125 ? 144.222 100.201 124.433 1.00 26.58 ?  104 SER D OG    1 
ATOM   14197 N  N     . TYR D 2 126 ? 146.782 96.950  126.095 1.00 25.68 ?  105 TYR D N     1 
ATOM   14198 C  CA    . TYR D 2 126 ? 147.915 96.280  126.746 1.00 26.12 ?  105 TYR D CA    1 
ATOM   14199 C  C     . TYR D 2 126 ? 148.505 95.203  125.830 1.00 26.38 ?  105 TYR D C     1 
ATOM   14200 O  O     . TYR D 2 126 ? 149.725 95.093  125.689 1.00 26.83 ?  105 TYR D O     1 
ATOM   14201 C  CB    . TYR D 2 126 ? 147.499 95.652  128.090 1.00 25.35 ?  105 TYR D CB    1 
ATOM   14202 C  CG    . TYR D 2 126 ? 147.381 96.625  129.248 1.00 25.46 ?  105 TYR D CG    1 
ATOM   14203 C  CD1   . TYR D 2 126 ? 148.453 97.444  129.605 1.00 25.41 ?  105 TYR D CD1   1 
ATOM   14204 C  CD2   . TYR D 2 126 ? 146.207 96.704  130.012 1.00 24.77 ?  105 TYR D CD2   1 
ATOM   14205 C  CE1   . TYR D 2 126 ? 148.358 98.339  130.669 1.00 25.89 ?  105 TYR D CE1   1 
ATOM   14206 C  CE2   . TYR D 2 126 ? 146.102 97.603  131.085 1.00 23.11 ?  105 TYR D CE2   1 
ATOM   14207 C  CZ    . TYR D 2 126 ? 147.187 98.404  131.414 1.00 25.38 ?  105 TYR D CZ    1 
ATOM   14208 O  OH    . TYR D 2 126 ? 147.121 99.296  132.462 1.00 23.31 ?  105 TYR D OH    1 
ATOM   14209 N  N     . SER D 2 127 ? 147.632 94.428  125.196 1.00 27.16 ?  106 SER D N     1 
ATOM   14210 C  CA    . SER D 2 127 ? 148.055 93.391  124.248 1.00 27.83 ?  106 SER D CA    1 
ATOM   14211 C  C     . SER D 2 127 ? 148.855 93.997  123.086 1.00 28.21 ?  106 SER D C     1 
ATOM   14212 O  O     . SER D 2 127 ? 149.933 93.493  122.744 1.00 28.30 ?  106 SER D O     1 
ATOM   14213 C  CB    . SER D 2 127 ? 146.840 92.599  123.738 1.00 28.37 ?  106 SER D CB    1 
ATOM   14214 O  OG    . SER D 2 127 ? 147.213 91.659  122.733 1.00 29.33 ?  106 SER D OG    1 
ATOM   14215 N  N     . ASN D 2 128 ? 148.325 95.075  122.499 1.00 28.27 ?  107 ASN D N     1 
ATOM   14216 C  CA    . ASN D 2 128 ? 149.000 95.833  121.432 1.00 28.79 ?  107 ASN D CA    1 
ATOM   14217 C  C     . ASN D 2 128 ? 150.395 96.321  121.810 1.00 28.53 ?  107 ASN D C     1 
ATOM   14218 O  O     . ASN D 2 128 ? 151.330 96.199  121.011 1.00 28.03 ?  107 ASN D O     1 
ATOM   14219 C  CB    . ASN D 2 128 ? 148.154 97.034  120.969 1.00 29.05 ?  107 ASN D CB    1 
ATOM   14220 C  CG    . ASN D 2 128 ? 146.901 96.616  120.194 1.00 30.48 ?  107 ASN D CG    1 
ATOM   14221 O  OD1   . ASN D 2 128 ? 146.742 95.455  119.823 1.00 32.19 ?  107 ASN D OD1   1 
ATOM   14222 N  ND2   . ASN D 2 128 ? 146.001 97.567  119.967 1.00 31.59 ?  107 ASN D ND2   1 
ATOM   14223 N  N     . ILE D 2 129 ? 150.531 96.897  123.006 1.00 28.21 ?  108 ILE D N     1 
ATOM   14224 C  CA    . ILE D 2 129 ? 151.848 97.329  123.492 1.00 28.76 ?  108 ILE D CA    1 
ATOM   14225 C  C     . ILE D 2 129 ? 152.824 96.141  123.557 1.00 29.83 ?  108 ILE D C     1 
ATOM   14226 O  O     . ILE D 2 129 ? 153.956 96.227  123.061 1.00 29.99 ?  108 ILE D O     1 
ATOM   14227 C  CB    . ILE D 2 129 ? 151.774 98.070  124.866 1.00 28.28 ?  108 ILE D CB    1 
ATOM   14228 C  CG1   . ILE D 2 129 ? 150.965 99.370  124.744 1.00 27.94 ?  108 ILE D CG1   1 
ATOM   14229 C  CG2   . ILE D 2 129 ? 153.184 98.384  125.386 1.00 27.52 ?  108 ILE D CG2   1 
ATOM   14230 C  CD1   . ILE D 2 129 ? 150.532 99.964  126.079 1.00 27.98 ?  108 ILE D CD1   1 
ATOM   14231 N  N     . PHE D 2 130 ? 152.386 95.040  124.162 1.00 30.86 ?  109 PHE D N     1 
ATOM   14232 C  CA    . PHE D 2 130 ? 153.208 93.837  124.254 1.00 32.76 ?  109 PHE D CA    1 
ATOM   14233 C  C     . PHE D 2 130 ? 153.670 93.312  122.891 1.00 34.37 ?  109 PHE D C     1 
ATOM   14234 O  O     . PHE D 2 130 ? 154.862 93.104  122.681 1.00 34.61 ?  109 PHE D O     1 
ATOM   14235 C  CB    . PHE D 2 130 ? 152.474 92.732  125.010 1.00 32.81 ?  109 PHE D CB    1 
ATOM   14236 C  CG    . PHE D 2 130 ? 152.818 92.661  126.470 1.00 33.84 ?  109 PHE D CG    1 
ATOM   14237 C  CD1   . PHE D 2 130 ? 154.089 92.266  126.880 1.00 34.61 ?  109 PHE D CD1   1 
ATOM   14238 C  CD2   . PHE D 2 130 ? 151.862 92.956  127.434 1.00 35.74 ?  109 PHE D CD2   1 
ATOM   14239 C  CE1   . PHE D 2 130 ? 154.413 92.186  128.234 1.00 36.99 ?  109 PHE D CE1   1 
ATOM   14240 C  CE2   . PHE D 2 130 ? 152.172 92.881  128.798 1.00 36.96 ?  109 PHE D CE2   1 
ATOM   14241 C  CZ    . PHE D 2 130 ? 153.450 92.495  129.199 1.00 36.91 ?  109 PHE D CZ    1 
ATOM   14242 N  N     . MET D 2 131 ? 152.719 93.119  121.976 1.00 35.90 ?  110 MET D N     1 
ATOM   14243 C  CA    . MET D 2 131 ? 152.995 92.583  120.642 1.00 37.94 ?  110 MET D CA    1 
ATOM   14244 C  C     . MET D 2 131 ? 153.956 93.460  119.852 1.00 38.05 ?  110 MET D C     1 
ATOM   14245 O  O     . MET D 2 131 ? 154.684 92.962  119.000 1.00 38.20 ?  110 MET D O     1 
ATOM   14246 C  CB    . MET D 2 131 ? 151.698 92.377  119.844 1.00 38.63 ?  110 MET D CB    1 
ATOM   14247 C  CG    . MET D 2 131 ? 150.783 91.263  120.380 1.00 42.34 ?  110 MET D CG    1 
ATOM   14248 S  SD    . MET D 2 131 ? 149.251 91.014  119.425 1.00 50.15 ?  110 MET D SD    1 
ATOM   14249 C  CE    . MET D 2 131 ? 148.307 92.500  119.787 1.00 48.14 ?  110 MET D CE    1 
ATOM   14250 N  N     . THR D 2 132 ? 153.953 94.761  120.138 1.00 38.12 ?  111 THR D N     1 
ATOM   14251 C  CA    . THR D 2 132 ? 154.863 95.696  119.475 1.00 38.79 ?  111 THR D CA    1 
ATOM   14252 C  C     . THR D 2 132 ? 156.311 95.559  119.981 1.00 38.81 ?  111 THR D C     1 
ATOM   14253 O  O     . THR D 2 132 ? 157.251 95.579  119.180 1.00 39.26 ?  111 THR D O     1 
ATOM   14254 C  CB    . THR D 2 132 ? 154.375 97.152  119.623 1.00 38.78 ?  111 THR D CB    1 
ATOM   14255 O  OG1   . THR D 2 132 ? 153.048 97.263  119.096 1.00 39.32 ?  111 THR D OG1   1 
ATOM   14256 C  CG2   . THR D 2 132 ? 155.278 98.115  118.860 1.00 39.75 ?  111 THR D CG2   1 
ATOM   14257 N  N     . LEU D 2 133 ? 156.473 95.405  121.296 1.00 38.34 ?  112 LEU D N     1 
ATOM   14258 C  CA    . LEU D 2 133 ? 157.787 95.444  121.945 1.00 38.36 ?  112 LEU D CA    1 
ATOM   14259 C  C     . LEU D 2 133 ? 158.489 94.092  122.081 1.00 38.94 ?  112 LEU D C     1 
ATOM   14260 O  O     . LEU D 2 133 ? 159.718 94.030  122.062 1.00 39.14 ?  112 LEU D O     1 
ATOM   14261 C  CB    . LEU D 2 133 ? 157.682 96.097  123.334 1.00 37.62 ?  112 LEU D CB    1 
ATOM   14262 C  CG    . LEU D 2 133 ? 157.064 97.494  123.440 1.00 36.50 ?  112 LEU D CG    1 
ATOM   14263 C  CD1   . LEU D 2 133 ? 156.822 97.860  124.908 1.00 35.80 ?  112 LEU D CD1   1 
ATOM   14264 C  CD2   . LEU D 2 133 ? 157.908 98.550  122.747 1.00 35.32 ?  112 LEU D CD2   1 
ATOM   14265 N  N     . ALA D 2 134 ? 157.729 93.015  122.232 1.00 39.41 ?  113 ALA D N     1 
ATOM   14266 C  CA    . ALA D 2 134 ? 158.350 91.701  122.436 1.00 40.33 ?  113 ALA D CA    1 
ATOM   14267 C  C     . ALA D 2 134 ? 157.870 90.660  121.430 1.00 41.05 ?  113 ALA D C     1 
ATOM   14268 O  O     . ALA D 2 134 ? 156.740 90.743  120.962 1.00 40.81 ?  113 ALA D O     1 
ATOM   14269 C  CB    . ALA D 2 134 ? 158.107 91.222  123.855 1.00 40.15 ?  113 ALA D CB    1 
ATOM   14270 N  N     . PRO D 2 135 ? 158.733 89.681  121.083 1.00 42.21 ?  114 PRO D N     1 
ATOM   14271 C  CA    . PRO D 2 135 ? 158.247 88.560  120.269 1.00 43.27 ?  114 PRO D CA    1 
ATOM   14272 C  C     . PRO D 2 135 ? 157.346 87.628  121.092 1.00 43.89 ?  114 PRO D C     1 
ATOM   14273 O  O     . PRO D 2 135 ? 157.407 87.640  122.324 1.00 43.31 ?  114 PRO D O     1 
ATOM   14274 C  CB    . PRO D 2 135 ? 159.532 87.840  119.852 1.00 43.69 ?  114 PRO D CB    1 
ATOM   14275 C  CG    . PRO D 2 135 ? 160.507 88.167  120.918 1.00 43.01 ?  114 PRO D CG    1 
ATOM   14276 C  CD    . PRO D 2 135 ? 160.170 89.554  121.393 1.00 42.16 ?  114 PRO D CD    1 
ATOM   14277 N  N     . THR D 2 136 ? 156.532 86.827  120.404 1.00 45.26 ?  115 THR D N     1 
ATOM   14278 C  CA    . THR D 2 136 ? 155.521 85.969  121.043 1.00 46.11 ?  115 THR D CA    1 
ATOM   14279 C  C     . THR D 2 136 ? 156.072 85.135  122.203 1.00 46.35 ?  115 THR D C     1 
ATOM   14280 O  O     . THR D 2 136 ? 155.461 85.086  123.276 1.00 46.25 ?  115 THR D O     1 
ATOM   14281 C  CB    . THR D 2 136 ? 154.799 85.060  120.010 1.00 46.59 ?  115 THR D CB    1 
ATOM   14282 O  OG1   . THR D 2 136 ? 154.277 85.868  118.951 1.00 47.80 ?  115 THR D OG1   1 
ATOM   14283 C  CG2   . THR D 2 136 ? 153.634 84.305  120.647 1.00 46.94 ?  115 THR D CG2   1 
ATOM   14284 N  N     . GLU D 2 137 ? 157.229 84.506  121.997 1.00 46.92 ?  116 GLU D N     1 
ATOM   14285 C  CA    . GLU D 2 137 ? 157.834 83.654  123.021 1.00 47.37 ?  116 GLU D CA    1 
ATOM   14286 C  C     . GLU D 2 137 ? 158.205 84.417  124.294 1.00 46.64 ?  116 GLU D C     1 
ATOM   14287 O  O     . GLU D 2 137 ? 158.037 83.893  125.397 1.00 46.89 ?  116 GLU D O     1 
ATOM   14288 C  CB    . GLU D 2 137 ? 159.048 82.891  122.467 1.00 48.04 ?  116 GLU D CB    1 
ATOM   14289 C  CG    . GLU D 2 137 ? 159.670 81.874  123.441 1.00 49.86 ?  116 GLU D CG    1 
ATOM   14290 C  CD    . GLU D 2 137 ? 158.805 80.629  123.688 1.00 52.40 ?  116 GLU D CD    1 
ATOM   14291 O  OE1   . GLU D 2 137 ? 157.617 80.766  124.057 1.00 52.97 ?  116 GLU D OE1   1 
ATOM   14292 O  OE2   . GLU D 2 137 ? 159.328 79.500  123.536 1.00 54.12 -1 116 GLU D OE2   1 
ATOM   14293 N  N     . THR D 2 138 ? 158.701 85.643  124.136 1.00 46.09 ?  117 THR D N     1 
ATOM   14294 C  CA    . THR D 2 138 ? 159.045 86.511  125.272 1.00 45.30 ?  117 THR D CA    1 
ATOM   14295 C  C     . THR D 2 138 ? 157.804 86.933  126.070 1.00 44.63 ?  117 THR D C     1 
ATOM   14296 O  O     . THR D 2 138 ? 157.837 86.972  127.303 1.00 44.51 ?  117 THR D O     1 
ATOM   14297 C  CB    . THR D 2 138 ? 159.828 87.764  124.812 1.00 45.20 ?  117 THR D CB    1 
ATOM   14298 O  OG1   . THR D 2 138 ? 161.000 87.357  124.097 1.00 45.69 ?  117 THR D OG1   1 
ATOM   14299 C  CG2   . THR D 2 138 ? 160.251 88.628  125.999 1.00 44.67 ?  117 THR D CG2   1 
ATOM   14300 N  N     . ILE D 2 139 ? 156.714 87.237  125.365 1.00 44.24 ?  118 ILE D N     1 
ATOM   14301 C  CA    . ILE D 2 139 ? 155.450 87.596  126.011 1.00 43.65 ?  118 ILE D CA    1 
ATOM   14302 C  C     . ILE D 2 139 ? 154.937 86.437  126.879 1.00 43.87 ?  118 ILE D C     1 
ATOM   14303 O  O     . ILE D 2 139 ? 154.602 86.632  128.051 1.00 43.36 ?  118 ILE D O     1 
ATOM   14304 C  CB    . ILE D 2 139 ? 154.390 88.056  124.977 1.00 43.68 ?  118 ILE D CB    1 
ATOM   14305 C  CG1   . ILE D 2 139 ? 154.821 89.385  124.336 1.00 43.30 ?  118 ILE D CG1   1 
ATOM   14306 C  CG2   . ILE D 2 139 ? 153.000 88.192  125.625 1.00 43.11 ?  118 ILE D CG2   1 
ATOM   14307 C  CD1   . ILE D 2 139 ? 154.096 89.745  123.046 1.00 43.41 ?  118 ILE D CD1   1 
ATOM   14308 N  N     . ASN D 2 140 ? 154.909 85.235  126.307 1.00 44.52 ?  119 ASN D N     1 
ATOM   14309 C  CA    . ASN D 2 140 ? 154.474 84.034  127.029 1.00 45.00 ?  119 ASN D CA    1 
ATOM   14310 C  C     . ASN D 2 140 ? 155.296 83.764  128.307 1.00 44.99 ?  119 ASN D C     1 
ATOM   14311 O  O     . ASN D 2 140 ? 154.735 83.395  129.346 1.00 44.61 ?  119 ASN D O     1 
ATOM   14312 C  CB    . ASN D 2 140 ? 154.472 82.807  126.100 1.00 45.74 ?  119 ASN D CB    1 
ATOM   14313 C  CG    . ASN D 2 140 ? 153.513 82.957  124.913 1.00 46.40 ?  119 ASN D CG    1 
ATOM   14314 O  OD1   . ASN D 2 140 ? 152.638 83.829  124.896 1.00 46.85 ?  119 ASN D OD1   1 
ATOM   14315 N  ND2   . ASN D 2 140 ? 153.676 82.090  123.916 1.00 48.16 ?  119 ASN D ND2   1 
ATOM   14316 N  N     . GLU D 2 141 ? 156.612 83.978  128.232 1.00 45.09 ?  120 GLU D N     1 
ATOM   14317 C  CA    . GLU D 2 141 ? 157.502 83.769  129.378 1.00 45.27 ?  120 GLU D CA    1 
ATOM   14318 C  C     . GLU D 2 141 ? 157.317 84.803  130.498 1.00 44.75 ?  120 GLU D C     1 
ATOM   14319 O  O     . GLU D 2 141 ? 157.312 84.449  131.682 1.00 44.37 ?  120 GLU D O     1 
ATOM   14320 C  CB    . GLU D 2 141 ? 158.965 83.727  128.935 1.00 45.75 ?  120 GLU D CB    1 
ATOM   14321 C  CG    . GLU D 2 141 ? 159.328 82.496  128.103 1.00 48.17 ?  120 GLU D CG    1 
ATOM   14322 C  CD    . GLU D 2 141 ? 160.795 82.444  127.726 1.00 50.15 ?  120 GLU D CD    1 
ATOM   14323 O  OE1   . GLU D 2 141 ? 161.655 82.601  128.618 1.00 50.90 ?  120 GLU D OE1   1 
ATOM   14324 O  OE2   . GLU D 2 141 ? 161.090 82.238  126.530 1.00 52.25 -1 120 GLU D OE2   1 
ATOM   14325 N  N     . VAL D 2 142 ? 157.182 86.074  130.117 1.00 44.31 ?  121 VAL D N     1 
ATOM   14326 C  CA    . VAL D 2 142 ? 156.931 87.152  131.076 1.00 43.91 ?  121 VAL D CA    1 
ATOM   14327 C  C     . VAL D 2 142 ? 155.621 86.908  131.831 1.00 43.71 ?  121 VAL D C     1 
ATOM   14328 O  O     . VAL D 2 142 ? 155.561 87.075  133.048 1.00 43.44 ?  121 VAL D O     1 
ATOM   14329 C  CB    . VAL D 2 142 ? 156.917 88.547  130.393 1.00 43.65 ?  121 VAL D CB    1 
ATOM   14330 C  CG1   . VAL D 2 142 ? 156.524 89.638  131.388 1.00 43.40 ?  121 VAL D CG1   1 
ATOM   14331 C  CG2   . VAL D 2 142 ? 158.284 88.861  129.794 1.00 43.96 ?  121 VAL D CG2   1 
ATOM   14332 N  N     . PHE D 2 143 ? 154.582 86.500  131.106 1.00 44.03 ?  122 PHE D N     1 
ATOM   14333 C  CA    . PHE D 2 143 ? 153.298 86.210  131.734 1.00 44.42 ?  122 PHE D CA    1 
ATOM   14334 C  C     . PHE D 2 143 ? 153.339 84.976  132.628 1.00 45.38 ?  122 PHE D C     1 
ATOM   14335 O  O     . PHE D 2 143 ? 152.693 84.953  133.672 1.00 45.50 ?  122 PHE D O     1 
ATOM   14336 C  CB    . PHE D 2 143 ? 152.167 86.138  130.706 1.00 44.27 ?  122 PHE D CB    1 
ATOM   14337 C  CG    . PHE D 2 143 ? 151.558 87.475  130.412 1.00 43.28 ?  122 PHE D CG    1 
ATOM   14338 C  CD1   . PHE D 2 143 ? 150.592 88.013  131.259 1.00 42.17 ?  122 PHE D CD1   1 
ATOM   14339 C  CD2   . PHE D 2 143 ? 151.972 88.216  129.313 1.00 42.76 ?  122 PHE D CD2   1 
ATOM   14340 C  CE1   . PHE D 2 143 ? 150.034 89.261  131.008 1.00 42.16 ?  122 PHE D CE1   1 
ATOM   14341 C  CE2   . PHE D 2 143 ? 151.422 89.465  129.051 1.00 42.77 ?  122 PHE D CE2   1 
ATOM   14342 C  CZ    . PHE D 2 143 ? 150.449 89.991  129.900 1.00 42.28 ?  122 PHE D CZ    1 
ATOM   14343 N  N     . GLU D 2 144 ? 154.116 83.971  132.230 1.00 46.18 ?  123 GLU D N     1 
ATOM   14344 C  CA    . GLU D 2 144 ? 154.380 82.816  133.088 1.00 47.19 ?  123 GLU D CA    1 
ATOM   14345 C  C     . GLU D 2 144 ? 155.053 83.241  134.402 1.00 46.99 ?  123 GLU D C     1 
ATOM   14346 O  O     . GLU D 2 144 ? 154.650 82.781  135.475 1.00 46.94 ?  123 GLU D O     1 
ATOM   14347 C  CB    . GLU D 2 144 ? 155.239 81.783  132.346 1.00 47.80 ?  123 GLU D CB    1 
ATOM   14348 C  CG    . GLU D 2 144 ? 155.465 80.460  133.086 1.00 49.54 ?  123 GLU D CG    1 
ATOM   14349 C  CD    . GLU D 2 144 ? 156.423 79.519  132.349 1.00 52.37 ?  123 GLU D CD    1 
ATOM   14350 O  OE1   . GLU D 2 144 ? 157.493 79.978  131.884 1.00 52.92 ?  123 GLU D OE1   1 
ATOM   14351 O  OE2   . GLU D 2 144 ? 156.110 78.315  132.241 1.00 53.55 -1 123 GLU D OE2   1 
ATOM   14352 N  N     . TRP D 2 145 ? 156.063 84.114  134.307 1.00 47.02 ?  124 TRP D N     1 
ATOM   14353 C  CA    . TRP D 2 145 ? 156.806 84.621  135.475 1.00 46.93 ?  124 TRP D CA    1 
ATOM   14354 C  C     . TRP D 2 145 ? 155.910 85.441  136.393 1.00 46.55 ?  124 TRP D C     1 
ATOM   14355 O  O     . TRP D 2 145 ? 155.851 85.189  137.593 1.00 46.42 ?  124 TRP D O     1 
ATOM   14356 C  CB    . TRP D 2 145 ? 158.007 85.476  135.042 1.00 47.07 ?  124 TRP D CB    1 
ATOM   14357 C  CG    . TRP D 2 145 ? 158.960 85.881  136.171 1.00 47.82 ?  124 TRP D CG    1 
ATOM   14358 C  CD1   . TRP D 2 145 ? 160.092 85.217  136.564 1.00 48.78 ?  124 TRP D CD1   1 
ATOM   14359 C  CD2   . TRP D 2 145 ? 158.868 87.044  137.019 1.00 47.80 ?  124 TRP D CD2   1 
ATOM   14360 N  NE1   . TRP D 2 145 ? 160.703 85.884  137.603 1.00 49.06 ?  124 TRP D NE1   1 
ATOM   14361 C  CE2   . TRP D 2 145 ? 159.973 87.006  137.904 1.00 48.24 ?  124 TRP D CE2   1 
ATOM   14362 C  CE3   . TRP D 2 145 ? 157.959 88.106  137.122 1.00 47.65 ?  124 TRP D CE3   1 
ATOM   14363 C  CZ2   . TRP D 2 145 ? 160.192 87.991  138.881 1.00 47.74 ?  124 TRP D CZ2   1 
ATOM   14364 C  CZ3   . TRP D 2 145 ? 158.176 89.087  138.093 1.00 46.92 ?  124 TRP D CZ3   1 
ATOM   14365 C  CH2   . TRP D 2 145 ? 159.288 89.019  138.959 1.00 47.88 ?  124 TRP D CH2   1 
ATOM   14366 N  N     . VAL D 2 146 ? 155.218 86.423  135.822 1.00 46.09 ?  125 VAL D N     1 
ATOM   14367 C  CA    . VAL D 2 146 ? 154.381 87.322  136.607 1.00 45.36 ?  125 VAL D CA    1 
ATOM   14368 C  C     . VAL D 2 146 ? 153.184 86.563  137.202 1.00 45.28 ?  125 VAL D C     1 
ATOM   14369 O  O     . VAL D 2 146 ? 152.740 86.868  138.314 1.00 45.29 ?  125 VAL D O     1 
ATOM   14370 C  CB    . VAL D 2 146 ? 154.008 88.602  135.790 1.00 45.33 ?  125 VAL D CB    1 
ATOM   14371 C  CG1   . VAL D 2 146 ? 153.022 89.469  136.529 1.00 44.97 ?  125 VAL D CG1   1 
ATOM   14372 C  CG2   . VAL D 2 146 ? 155.267 89.419  135.495 1.00 44.52 ?  125 VAL D CG2   1 
ATOM   14373 N  N     . LYS D 2 147 ? 152.705 85.546  136.485 1.00 44.98 ?  126 LYS D N     1 
ATOM   14374 C  CA    . LYS D 2 147 ? 151.633 84.675  136.987 1.00 44.65 ?  126 LYS D CA    1 
ATOM   14375 C  C     . LYS D 2 147 ? 152.044 83.877  138.235 1.00 44.06 ?  126 LYS D C     1 
ATOM   14376 O  O     . LYS D 2 147 ? 151.204 83.549  139.074 1.00 44.65 ?  126 LYS D O     1 
ATOM   14377 C  CB    . LYS D 2 147 ? 151.150 83.710  135.901 1.00 45.31 ?  126 LYS D CB    1 
ATOM   14378 C  CG    . LYS D 2 147 ? 149.635 83.606  135.808 1.00 46.54 ?  126 LYS D CG    1 
ATOM   14379 C  CD    . LYS D 2 147 ? 149.150 82.168  135.619 1.00 49.06 ?  126 LYS D CD    1 
ATOM   14380 C  CE    . LYS D 2 147 ? 148.956 81.464  136.969 1.00 50.46 ?  126 LYS D CE    1 
ATOM   14381 N  NZ    . LYS D 2 147 ? 147.946 80.365  136.908 1.00 51.33 1  126 LYS D NZ    1 
ATOM   14382 N  N     . GLN D 2 148 ? 153.333 83.568  138.349 1.00 42.58 ?  127 GLN D N     1 
ATOM   14383 C  CA    . GLN D 2 148 ? 153.862 82.827  139.494 1.00 41.39 ?  127 GLN D CA    1 
ATOM   14384 C  C     . GLN D 2 148 ? 154.394 83.748  140.600 1.00 39.56 ?  127 GLN D C     1 
ATOM   14385 O  O     . GLN D 2 148 ? 154.604 83.304  141.727 1.00 39.77 ?  127 GLN D O     1 
ATOM   14386 C  CB    . GLN D 2 148 ? 154.936 81.830  139.015 1.00 42.11 ?  127 GLN D CB    1 
ATOM   14387 C  CG    . GLN D 2 148 ? 156.107 81.587  139.964 1.00 44.08 ?  127 GLN D CG    1 
ATOM   14388 C  CD    . GLN D 2 148 ? 157.351 82.410  139.621 1.00 46.12 ?  127 GLN D CD    1 
ATOM   14389 O  OE1   . GLN D 2 148 ? 157.265 83.597  139.281 1.00 46.47 ?  127 GLN D OE1   1 
ATOM   14390 N  NE2   . GLN D 2 148 ? 158.520 81.778  139.726 1.00 45.69 ?  127 GLN D NE2   1 
ATOM   14391 N  N     . ASN D 2 149 ? 154.596 85.027  140.270 1.00 36.99 ?  128 ASN D N     1 
ATOM   14392 C  CA    . ASN D 2 149 ? 155.159 86.001  141.205 1.00 34.54 ?  128 ASN D CA    1 
ATOM   14393 C  C     . ASN D 2 149 ? 154.340 86.189  142.485 1.00 33.13 ?  128 ASN D C     1 
ATOM   14394 O  O     . ASN D 2 149 ? 153.149 86.485  142.435 1.00 32.62 ?  128 ASN D O     1 
ATOM   14395 C  CB    . ASN D 2 149 ? 155.367 87.352  140.519 1.00 34.24 ?  128 ASN D CB    1 
ATOM   14396 C  CG    . ASN D 2 149 ? 156.058 88.354  141.423 1.00 33.83 ?  128 ASN D CG    1 
ATOM   14397 O  OD1   . ASN D 2 149 ? 155.413 89.219  142.018 1.00 32.21 ?  128 ASN D OD1   1 
ATOM   14398 N  ND2   . ASN D 2 149 ? 157.376 88.219  141.555 1.00 33.26 ?  128 ASN D ND2   1 
ATOM   14399 N  N     . LYS D 2 150 ? 155.008 86.045  143.626 1.00 31.49 ?  129 LYS D N     1 
ATOM   14400 C  CA    . LYS D 2 150 ? 154.363 86.065  144.937 1.00 30.68 ?  129 LYS D CA    1 
ATOM   14401 C  C     . LYS D 2 150 ? 153.631 87.388  145.271 1.00 28.95 ?  129 LYS D C     1 
ATOM   14402 O  O     . LYS D 2 150 ? 152.526 87.368  145.826 1.00 27.90 ?  129 LYS D O     1 
ATOM   14403 C  CB    . LYS D 2 150 ? 155.411 85.707  146.001 1.00 31.17 ?  129 LYS D CB    1 
ATOM   14404 C  CG    . LYS D 2 150 ? 155.069 86.003  147.447 1.00 33.66 ?  129 LYS D CG    1 
ATOM   14405 C  CD    . LYS D 2 150 ? 156.252 85.602  148.342 1.00 38.08 ?  129 LYS D CD    1 
ATOM   14406 C  CE    . LYS D 2 150 ? 156.282 86.397  149.653 1.00 40.20 ?  129 LYS D CE    1 
ATOM   14407 N  NZ    . LYS D 2 150 ? 155.553 85.708  150.753 1.00 42.60 1  129 LYS D NZ    1 
ATOM   14408 N  N     . TYR D 2 151 ? 154.245 88.522  144.940 1.00 27.36 ?  130 TYR D N     1 
ATOM   14409 C  CA    . TYR D 2 151 ? 153.687 89.833  145.318 1.00 26.56 ?  130 TYR D CA    1 
ATOM   14410 C  C     . TYR D 2 151 ? 152.536 90.253  144.417 1.00 25.66 ?  130 TYR D C     1 
ATOM   14411 O  O     . TYR D 2 151 ? 151.562 90.837  144.901 1.00 25.61 ?  130 TYR D O     1 
ATOM   14412 C  CB    . TYR D 2 151 ? 154.782 90.916  145.393 1.00 26.32 ?  130 TYR D CB    1 
ATOM   14413 C  CG    . TYR D 2 151 ? 156.010 90.426  146.135 1.00 27.20 ?  130 TYR D CG    1 
ATOM   14414 C  CD1   . TYR D 2 151 ? 155.969 90.209  147.513 1.00 27.31 ?  130 TYR D CD1   1 
ATOM   14415 C  CD2   . TYR D 2 151 ? 157.190 90.125  145.455 1.00 27.22 ?  130 TYR D CD2   1 
ATOM   14416 C  CE1   . TYR D 2 151 ? 157.080 89.727  148.201 1.00 29.65 ?  130 TYR D CE1   1 
ATOM   14417 C  CE2   . TYR D 2 151 ? 158.316 89.639  146.139 1.00 28.75 ?  130 TYR D CE2   1 
ATOM   14418 C  CZ    . TYR D 2 151 ? 158.242 89.455  147.522 1.00 29.17 ?  130 TYR D CZ    1 
ATOM   14419 O  OH    . TYR D 2 151 ? 159.321 88.981  148.234 1.00 30.61 ?  130 TYR D OH    1 
ATOM   14420 N  N     . LEU D 2 152 ? 152.649 89.954  143.121 1.00 24.87 ?  131 LEU D N     1 
ATOM   14421 C  CA    . LEU D 2 152 ? 151.544 90.183  142.196 1.00 24.37 ?  131 LEU D CA    1 
ATOM   14422 C  C     . LEU D 2 152 ? 150.345 89.305  142.574 1.00 24.18 ?  131 LEU D C     1 
ATOM   14423 O  O     . LEU D 2 152 ? 149.232 89.810  142.717 1.00 23.16 ?  131 LEU D O     1 
ATOM   14424 C  CB    . LEU D 2 152 ? 151.936 89.955  140.732 1.00 24.45 ?  131 LEU D CB    1 
ATOM   14425 C  CG    . LEU D 2 152 ? 150.681 90.285  139.905 1.00 26.33 ?  131 LEU D CG    1 
ATOM   14426 C  CD1   . LEU D 2 152 ? 150.450 91.801  139.839 1.00 25.00 ?  131 LEU D CD1   1 
ATOM   14427 C  CD2   . LEU D 2 152 ? 150.661 89.656  138.542 1.00 29.15 ?  131 LEU D CD2   1 
ATOM   14428 N  N     . GLN D 2 153 ? 150.584 88.006  142.766 1.00 24.07 ?  132 GLN D N     1 
ATOM   14429 C  CA    . GLN D 2 153 ? 149.508 87.088  143.198 1.00 24.99 ?  132 GLN D CA    1 
ATOM   14430 C  C     . GLN D 2 153 ? 148.851 87.490  144.515 1.00 24.24 ?  132 GLN D C     1 
ATOM   14431 O  O     . GLN D 2 153 ? 147.612 87.469  144.636 1.00 23.75 ?  132 GLN D O     1 
ATOM   14432 C  CB    . GLN D 2 153 ? 149.990 85.628  143.247 1.00 25.84 ?  132 GLN D CB    1 
ATOM   14433 C  CG    . GLN D 2 153 ? 150.238 85.008  141.846 1.00 28.48 ?  132 GLN D CG    1 
ATOM   14434 C  CD    . GLN D 2 153 ? 148.984 84.967  140.957 1.00 30.95 ?  132 GLN D CD    1 
ATOM   14435 O  OE1   . GLN D 2 153 ? 147.879 84.751  141.438 1.00 31.78 ?  132 GLN D OE1   1 
ATOM   14436 N  NE2   . GLN D 2 153 ? 149.169 85.162  139.650 1.00 32.81 ?  132 GLN D NE2   1 
ATOM   14437 N  N     . LYS D 2 154 ? 149.654 87.871  145.504 1.00 24.00 ?  133 LYS D N     1 
ATOM   14438 C  CA    . LYS D 2 154 ? 149.068 88.247  146.790 1.00 24.43 ?  133 LYS D CA    1 
ATOM   14439 C  C     . LYS D 2 154 ? 148.000 89.337  146.619 1.00 23.40 ?  133 LYS D C     1 
ATOM   14440 O  O     . LYS D 2 154 ? 146.862 89.174  147.066 1.00 22.68 ?  133 LYS D O     1 
ATOM   14441 C  CB    . LYS D 2 154 ? 150.115 88.702  147.813 1.00 24.64 ?  133 LYS D CB    1 
ATOM   14442 C  CG    . LYS D 2 154 ? 149.456 89.051  149.159 1.00 28.01 ?  133 LYS D CG    1 
ATOM   14443 C  CD    . LYS D 2 154 ? 150.434 89.340  150.273 1.00 32.56 ?  133 LYS D CD    1 
ATOM   14444 C  CE    . LYS D 2 154 ? 151.159 88.090  150.709 1.00 34.45 ?  133 LYS D CE    1 
ATOM   14445 N  NZ    . LYS D 2 154 ? 152.129 88.402  151.806 1.00 36.11 1  133 LYS D NZ    1 
ATOM   14446 N  N     . LYS D 2 155 ? 148.363 90.442  145.968 1.00 23.07 ?  134 LYS D N     1 
ATOM   14447 C  CA    . LYS D 2 155 ? 147.398 91.520  145.770 1.00 22.70 ?  134 LYS D CA    1 
ATOM   14448 C  C     . LYS D 2 155 ? 146.257 91.121  144.835 1.00 21.96 ?  134 LYS D C     1 
ATOM   14449 O  O     . LYS D 2 155 ? 145.105 91.424  145.127 1.00 22.25 ?  134 LYS D O     1 
ATOM   14450 C  CB    . LYS D 2 155 ? 148.066 92.841  145.346 1.00 22.70 ?  134 LYS D CB    1 
ATOM   14451 C  CG    . LYS D 2 155 ? 148.756 92.853  143.997 1.00 23.62 ?  134 LYS D CG    1 
ATOM   14452 C  CD    . LYS D 2 155 ? 149.287 94.257  143.718 1.00 25.32 ?  134 LYS D CD    1 
ATOM   14453 C  CE    . LYS D 2 155 ? 150.595 94.190  142.936 1.00 27.09 ?  134 LYS D CE    1 
ATOM   14454 N  NZ    . LYS D 2 155 ? 151.076 95.562  142.599 1.00 26.65 1  134 LYS D NZ    1 
ATOM   14455 N  N     . ALA D 2 156 ? 146.550 90.421  143.738 1.00 21.76 ?  135 ALA D N     1 
ATOM   14456 C  CA    . ALA D 2 156 ? 145.475 90.023  142.810 1.00 21.83 ?  135 ALA D CA    1 
ATOM   14457 C  C     . ALA D 2 156 ? 144.415 89.170  143.527 1.00 22.30 ?  135 ALA D C     1 
ATOM   14458 O  O     . ALA D 2 156 ? 143.212 89.422  143.397 1.00 21.92 ?  135 ALA D O     1 
ATOM   14459 C  CB    . ALA D 2 156 ? 146.037 89.277  141.587 1.00 22.30 ?  135 ALA D CB    1 
ATOM   14460 N  N     . GLN D 2 157 ? 144.862 88.182  144.304 1.00 22.15 ?  136 GLN D N     1 
ATOM   14461 C  CA    . GLN D 2 157 ? 143.927 87.289  144.997 1.00 22.38 ?  136 GLN D CA    1 
ATOM   14462 C  C     . GLN D 2 157 ? 143.199 87.947  146.176 1.00 21.59 ?  136 GLN D C     1 
ATOM   14463 O  O     . GLN D 2 157 ? 142.056 87.598  146.469 1.00 21.44 ?  136 GLN D O     1 
ATOM   14464 C  CB    . GLN D 2 157 ? 144.608 85.980  145.434 1.00 22.94 ?  136 GLN D CB    1 
ATOM   14465 C  CG    . GLN D 2 157 ? 145.240 85.164  144.294 1.00 25.31 ?  136 GLN D CG    1 
ATOM   14466 C  CD    . GLN D 2 157 ? 144.341 85.019  143.063 1.00 28.02 ?  136 GLN D CD    1 
ATOM   14467 O  OE1   . GLN D 2 157 ? 143.124 84.840  143.169 1.00 27.14 ?  136 GLN D OE1   1 
ATOM   14468 N  NE2   . GLN D 2 157 ? 144.954 85.088  141.882 1.00 29.47 ?  136 GLN D NE2   1 
ATOM   14469 N  N     . MET D 2 158 ? 143.851 88.884  146.855 1.00 21.52 ?  137 MET D N     1 
ATOM   14470 C  CA    . MET D 2 158 ? 143.182 89.651  147.921 1.00 22.20 ?  137 MET D CA    1 
ATOM   14471 C  C     . MET D 2 158 ? 141.971 90.427  147.391 1.00 21.84 ?  137 MET D C     1 
ATOM   14472 O  O     . MET D 2 158 ? 140.902 90.422  148.006 1.00 21.91 ?  137 MET D O     1 
ATOM   14473 C  CB    . MET D 2 158 ? 144.151 90.613  148.608 1.00 22.52 ?  137 MET D CB    1 
ATOM   14474 C  CG    . MET D 2 158 ? 145.098 89.932  149.606 1.00 25.81 ?  137 MET D CG    1 
ATOM   14475 S  SD    . MET D 2 158 ? 146.249 91.081  150.409 1.00 31.19 ?  137 MET D SD    1 
ATOM   14476 C  CE    . MET D 2 158 ? 145.064 92.080  151.272 1.00 23.91 ?  137 MET D CE    1 
ATOM   14477 N  N     . ILE D 2 159 ? 142.154 91.085  146.248 1.00 21.41 ?  138 ILE D N     1 
ATOM   14478 C  CA    . ILE D 2 159 ? 141.099 91.877  145.623 1.00 21.51 ?  138 ILE D CA    1 
ATOM   14479 C  C     . ILE D 2 159 ? 139.960 90.966  145.139 1.00 21.77 ?  138 ILE D C     1 
ATOM   14480 O  O     . ILE D 2 159 ? 138.782 91.221  145.437 1.00 21.44 ?  138 ILE D O     1 
ATOM   14481 C  CB    . ILE D 2 159 ? 141.691 92.774  144.466 1.00 21.49 ?  138 ILE D CB    1 
ATOM   14482 C  CG1   . ILE D 2 159 ? 142.714 93.782  145.011 1.00 21.16 ?  138 ILE D CG1   1 
ATOM   14483 C  CG2   . ILE D 2 159 ? 140.591 93.488  143.671 1.00 22.34 ?  138 ILE D CG2   1 
ATOM   14484 C  CD1   . ILE D 2 159 ? 142.151 94.806  146.019 1.00 23.85 ?  138 ILE D CD1   1 
ATOM   14485 N  N     . VAL D 2 160 ? 140.326 89.905  144.409 1.00 21.96 ?  139 VAL D N     1 
ATOM   14486 C  CA    . VAL D 2 160 ? 139.375 88.936  143.846 1.00 22.59 ?  139 VAL D CA    1 
ATOM   14487 C  C     . VAL D 2 160 ? 138.576 88.244  144.960 1.00 22.36 ?  139 VAL D C     1 
ATOM   14488 O  O     . VAL D 2 160 ? 137.378 87.989  144.804 1.00 21.64 ?  139 VAL D O     1 
ATOM   14489 C  CB    . VAL D 2 160 ? 140.102 87.889  142.936 1.00 23.08 ?  139 VAL D CB    1 
ATOM   14490 C  CG1   . VAL D 2 160 ? 139.225 86.656  142.644 1.00 24.33 ?  139 VAL D CG1   1 
ATOM   14491 C  CG2   . VAL D 2 160 ? 140.553 88.540  141.618 1.00 22.87 ?  139 VAL D CG2   1 
ATOM   14492 N  N     . GLY D 2 161 ? 139.246 87.953  146.079 1.00 22.21 ?  140 GLY D N     1 
ATOM   14493 C  CA    . GLY D 2 161 ? 138.589 87.363  147.243 1.00 22.50 ?  140 GLY D CA    1 
ATOM   14494 C  C     . GLY D 2 161 ? 137.422 88.208  147.744 1.00 22.88 ?  140 GLY D C     1 
ATOM   14495 O  O     . GLY D 2 161 ? 136.348 87.674  148.054 1.00 23.54 ?  140 GLY D O     1 
ATOM   14496 N  N     . LEU D 2 162 ? 137.620 89.524  147.811 1.00 22.25 ?  141 LEU D N     1 
ATOM   14497 C  CA    . LEU D 2 162 ? 136.550 90.429  148.244 1.00 22.48 ?  141 LEU D CA    1 
ATOM   14498 C  C     . LEU D 2 162 ? 135.400 90.526  147.238 1.00 22.27 ?  141 LEU D C     1 
ATOM   14499 O  O     . LEU D 2 162 ? 134.243 90.648  147.644 1.00 22.31 ?  141 LEU D O     1 
ATOM   14500 C  CB    . LEU D 2 162 ? 137.095 91.817  148.636 1.00 22.07 ?  141 LEU D CB    1 
ATOM   14501 C  CG    . LEU D 2 162 ? 137.829 91.841  149.995 1.00 22.81 ?  141 LEU D CG    1 
ATOM   14502 C  CD1   . LEU D 2 162 ? 138.771 93.037  150.120 1.00 21.65 ?  141 LEU D CD1   1 
ATOM   14503 C  CD2   . LEU D 2 162 ? 136.873 91.747  151.190 1.00 23.35 ?  141 LEU D CD2   1 
ATOM   14504 N  N     . TYR D 2 163 ? 135.706 90.476  145.940 1.00 22.63 ?  142 TYR D N     1 
ATOM   14505 C  CA    . TYR D 2 163 ? 134.650 90.423  144.908 1.00 23.30 ?  142 TYR D CA    1 
ATOM   14506 C  C     . TYR D 2 163 ? 133.826 89.146  145.004 1.00 23.40 ?  142 TYR D C     1 
ATOM   14507 O  O     . TYR D 2 163 ? 132.616 89.177  144.836 1.00 23.75 ?  142 TYR D O     1 
ATOM   14508 C  CB    . TYR D 2 163 ? 135.224 90.481  143.499 1.00 23.22 ?  142 TYR D CB    1 
ATOM   14509 C  CG    . TYR D 2 163 ? 135.989 91.726  143.145 1.00 24.01 ?  142 TYR D CG    1 
ATOM   14510 C  CD1   . TYR D 2 163 ? 135.782 92.918  143.827 1.00 24.47 ?  142 TYR D CD1   1 
ATOM   14511 C  CD2   . TYR D 2 163 ? 136.919 91.705  142.110 1.00 24.62 ?  142 TYR D CD2   1 
ATOM   14512 C  CE1   . TYR D 2 163 ? 136.485 94.058  143.496 1.00 26.33 ?  142 TYR D CE1   1 
ATOM   14513 C  CE2   . TYR D 2 163 ? 137.622 92.847  141.760 1.00 26.07 ?  142 TYR D CE2   1 
ATOM   14514 C  CZ    . TYR D 2 163 ? 137.392 94.023  142.462 1.00 26.65 ?  142 TYR D CZ    1 
ATOM   14515 O  OH    . TYR D 2 163 ? 138.087 95.165  142.140 1.00 31.13 ?  142 TYR D OH    1 
ATOM   14516 N  N     . LYS D 2 164 ? 134.486 88.025  145.263 1.00 23.70 ?  143 LYS D N     1 
ATOM   14517 C  CA    . LYS D 2 164 ? 133.791 86.735  145.398 1.00 24.47 ?  143 LYS D CA    1 
ATOM   14518 C  C     . LYS D 2 164 ? 132.931 86.629  146.668 1.00 24.55 ?  143 LYS D C     1 
ATOM   14519 O  O     . LYS D 2 164 ? 132.053 85.768  146.760 1.00 24.49 ?  143 LYS D O     1 
ATOM   14520 C  CB    . LYS D 2 164 ? 134.805 85.590  145.355 1.00 24.98 ?  143 LYS D CB    1 
ATOM   14521 C  CG    . LYS D 2 164 ? 135.362 85.279  143.957 1.00 27.10 ?  143 LYS D CG    1 
ATOM   14522 C  CD    . LYS D 2 164 ? 136.259 84.051  144.022 1.00 30.75 ?  143 LYS D CD    1 
ATOM   14523 C  CE    . LYS D 2 164 ? 136.770 83.619  142.649 1.00 32.81 ?  143 LYS D CE    1 
ATOM   14524 N  NZ    . LYS D 2 164 ? 137.746 82.461  142.746 1.00 33.68 1  143 LYS D NZ    1 
ATOM   14525 N  N     . ALA D 2 165 ? 133.193 87.492  147.646 1.00 24.18 ?  144 ALA D N     1 
ATOM   14526 C  CA    . ALA D 2 165 ? 132.489 87.445  148.930 1.00 25.04 ?  144 ALA D CA    1 
ATOM   14527 C  C     . ALA D 2 165 ? 131.228 88.317  149.000 1.00 25.00 ?  144 ALA D C     1 
ATOM   14528 O  O     . ALA D 2 165 ? 130.538 88.324  150.031 1.00 25.50 ?  144 ALA D O     1 
ATOM   14529 C  CB    . ALA D 2 165 ? 133.446 87.795  150.083 1.00 25.02 ?  144 ALA D CB    1 
ATOM   14530 N  N     . ILE D 2 166 ? 130.924 89.050  147.927 1.00 24.60 ?  145 ILE D N     1 
ATOM   14531 C  CA    . ILE D 2 166 ? 129.699 89.850  147.881 1.00 24.40 ?  145 ILE D CA    1 
ATOM   14532 C  C     . ILE D 2 166 ? 128.482 88.917  147.955 1.00 25.75 ?  145 ILE D C     1 
ATOM   14533 O  O     . ILE D 2 166 ? 128.419 87.903  147.251 1.00 25.84 ?  145 ILE D O     1 
ATOM   14534 C  CB    . ILE D 2 166 ? 129.585 90.725  146.600 1.00 24.15 ?  145 ILE D CB    1 
ATOM   14535 C  CG1   . ILE D 2 166 ? 130.855 91.544  146.377 1.00 23.15 ?  145 ILE D CG1   1 
ATOM   14536 C  CG2   . ILE D 2 166 ? 128.369 91.647  146.692 1.00 22.72 ?  145 ILE D CG2   1 
ATOM   14537 C  CD1   . ILE D 2 166 ? 130.908 92.239  145.032 1.00 21.70 ?  145 ILE D CD1   1 
ATOM   14538 N  N     . GLN D 2 167 ? 127.544 89.248  148.833 1.00 26.52 ?  146 GLN D N     1 
ATOM   14539 C  CA    . GLN D 2 167 ? 126.312 88.482  148.961 1.00 28.77 ?  146 GLN D CA    1 
ATOM   14540 C  C     . GLN D 2 167 ? 125.118 89.307  148.499 1.00 29.20 ?  146 GLN D C     1 
ATOM   14541 O  O     . GLN D 2 167 ? 125.048 90.517  148.758 1.00 28.89 ?  146 GLN D O     1 
ATOM   14542 C  CB    . GLN D 2 167 ? 126.114 88.034  150.406 1.00 29.04 ?  146 GLN D CB    1 
ATOM   14543 C  CG    . GLN D 2 167 ? 127.173 87.059  150.882 1.00 31.87 ?  146 GLN D CG    1 
ATOM   14544 C  CD    . GLN D 2 167 ? 127.662 87.387  152.267 1.00 35.35 ?  146 GLN D CD    1 
ATOM   14545 O  OE1   . GLN D 2 167 ? 126.925 87.252  153.247 1.00 36.91 ?  146 GLN D OE1   1 
ATOM   14546 N  NE2   . GLN D 2 167 ? 128.917 87.823  152.362 1.00 36.19 ?  146 GLN D NE2   1 
ATOM   14547 N  N     . LYS D 2 168 ? 124.182 88.648  147.820 1.00 30.29 ?  147 LYS D N     1 
ATOM   14548 C  CA    . LYS D 2 168 ? 122.954 89.303  147.374 1.00 31.24 ?  147 LYS D CA    1 
ATOM   14549 C  C     . LYS D 2 168 ? 122.270 90.042  148.524 1.00 31.73 ?  147 LYS D C     1 
ATOM   14550 O  O     . LYS D 2 168 ? 122.174 89.512  149.630 1.00 31.46 ?  147 LYS D O     1 
ATOM   14551 C  CB    . LYS D 2 168 ? 122.002 88.290  146.744 1.00 31.92 ?  147 LYS D CB    1 
ATOM   14552 C  CG    . LYS D 2 168 ? 120.736 88.917  146.179 1.00 33.23 ?  147 LYS D CG    1 
ATOM   14553 C  CD    . LYS D 2 168 ? 119.935 87.920  145.355 1.00 36.06 ?  147 LYS D CD    1 
ATOM   14554 C  CE    . LYS D 2 168 ? 118.643 88.533  144.858 1.00 35.46 ?  147 LYS D CE    1 
ATOM   14555 N  NZ    . LYS D 2 168 ? 118.874 89.551  143.799 1.00 38.24 1  147 LYS D NZ    1 
ATOM   14556 N  N     . ASP D 2 169 ? 121.822 91.272  148.254 1.00 32.28 ?  148 ASP D N     1 
ATOM   14557 C  CA    . ASP D 2 169 ? 121.135 92.120  149.244 1.00 33.45 ?  148 ASP D CA    1 
ATOM   14558 C  C     . ASP D 2 169 ? 121.909 92.392  150.534 1.00 33.30 ?  148 ASP D C     1 
ATOM   14559 O  O     . ASP D 2 169 ? 121.308 92.678  151.572 1.00 34.32 ?  148 ASP D O     1 
ATOM   14560 C  CB    . ASP D 2 169 ? 119.762 91.534  149.613 1.00 34.63 ?  148 ASP D CB    1 
ATOM   14561 C  CG    . ASP D 2 169 ? 118.735 91.687  148.512 1.00 36.09 ?  148 ASP D CG    1 
ATOM   14562 O  OD1   . ASP D 2 169 ? 118.964 92.447  147.547 1.00 37.80 ?  148 ASP D OD1   1 
ATOM   14563 O  OD2   . ASP D 2 169 ? 117.678 91.034  148.629 1.00 40.47 -1 148 ASP D OD2   1 
ATOM   14564 N  N     . ASP D 2 170 ? 123.228 92.284  150.492 1.00 32.58 ?  149 ASP D N     1 
ATOM   14565 C  CA    . ASP D 2 170 ? 124.034 92.647  151.655 1.00 32.01 ?  149 ASP D CA    1 
ATOM   14566 C  C     . ASP D 2 170 ? 124.962 93.793  151.271 1.00 30.59 ?  149 ASP D C     1 
ATOM   14567 O  O     . ASP D 2 170 ? 125.971 93.592  150.593 1.00 29.11 ?  149 ASP D O     1 
ATOM   14568 C  CB    . ASP D 2 170 ? 124.805 91.442  152.199 1.00 32.93 ?  149 ASP D CB    1 
ATOM   14569 C  CG    . ASP D 2 170 ? 125.840 91.822  153.249 1.00 35.05 ?  149 ASP D CG    1 
ATOM   14570 O  OD1   . ASP D 2 170 ? 125.667 92.826  153.975 1.00 39.25 ?  149 ASP D OD1   1 
ATOM   14571 O  OD2   . ASP D 2 170 ? 126.837 91.096  153.363 1.00 39.22 -1 149 ASP D OD2   1 
ATOM   14572 N  N     . GLU D 2 171 ? 124.593 94.994  151.708 1.00 29.34 ?  150 GLU D N     1 
ATOM   14573 C  CA    . GLU D 2 171 ? 125.314 96.210  151.345 1.00 28.51 ?  150 GLU D CA    1 
ATOM   14574 C  C     . GLU D 2 171 ? 126.685 96.334  152.024 1.00 27.27 ?  150 GLU D C     1 
ATOM   14575 O  O     . GLU D 2 171 ? 127.552 97.034  151.526 1.00 26.62 ?  150 GLU D O     1 
ATOM   14576 C  CB    . GLU D 2 171 ? 124.448 97.450  151.606 1.00 29.09 ?  150 GLU D CB    1 
ATOM   14577 C  CG    . GLU D 2 171 ? 124.189 97.773  153.076 1.00 30.68 ?  150 GLU D CG    1 
ATOM   14578 C  CD    . GLU D 2 171 ? 123.181 98.898  153.255 1.00 33.92 ?  150 GLU D CD    1 
ATOM   14579 O  OE1   . GLU D 2 171 ? 122.717 99.456  152.231 1.00 36.31 ?  150 GLU D OE1   1 
ATOM   14580 O  OE2   . GLU D 2 171 ? 122.852 99.237  154.413 1.00 34.02 -1 150 GLU D OE2   1 
ATOM   14581 N  N     . ILE D 2 172 ? 126.883 95.636  153.141 1.00 26.19 ?  151 ILE D N     1 
ATOM   14582 C  CA    . ILE D 2 172 ? 128.178 95.637  153.822 1.00 25.49 ?  151 ILE D CA    1 
ATOM   14583 C  C     . ILE D 2 172 ? 129.235 94.928  152.970 1.00 24.61 ?  151 ILE D C     1 
ATOM   14584 O  O     . ILE D 2 172 ? 130.333 95.459  152.760 1.00 24.09 ?  151 ILE D O     1 
ATOM   14585 C  CB    . ILE D 2 172 ? 128.091 95.024  155.249 1.00 25.98 ?  151 ILE D CB    1 
ATOM   14586 C  CG1   . ILE D 2 172 ? 127.179 95.862  156.146 1.00 26.86 ?  151 ILE D CG1   1 
ATOM   14587 C  CG2   . ILE D 2 172 ? 129.488 94.852  155.902 1.00 26.50 ?  151 ILE D CG2   1 
ATOM   14588 C  CD1   . ILE D 2 172 ? 127.639 97.299  156.343 1.00 27.81 ?  151 ILE D CD1   1 
ATOM   14589 N  N     . SER D 2 173 ? 128.888 93.748  152.465 1.00 23.71 ?  152 SER D N     1 
ATOM   14590 C  CA    . SER D 2 173 ? 129.791 92.986  151.605 1.00 23.38 ?  152 SER D CA    1 
ATOM   14591 C  C     . SER D 2 173 ? 130.031 93.715  150.270 1.00 22.41 ?  152 SER D C     1 
ATOM   14592 O  O     . SER D 2 173 ? 131.126 93.657  149.704 1.00 21.43 ?  152 SER D O     1 
ATOM   14593 C  CB    . SER D 2 173 ? 129.269 91.560  151.382 1.00 23.90 ?  152 SER D CB    1 
ATOM   14594 O  OG    . SER D 2 173 ? 128.105 91.508  150.559 1.00 23.74 ?  152 SER D OG    1 
ATOM   14595 N  N     . LEU D 2 174 ? 129.011 94.417  149.786 1.00 21.63 ?  153 LEU D N     1 
ATOM   14596 C  CA    . LEU D 2 174 ? 129.165 95.220  148.571 1.00 20.75 ?  153 LEU D CA    1 
ATOM   14597 C  C     . LEU D 2 174 ? 130.151 96.360  148.823 1.00 20.96 ?  153 LEU D C     1 
ATOM   14598 O  O     . LEU D 2 174 ? 131.031 96.616  148.001 1.00 20.41 ?  153 LEU D O     1 
ATOM   14599 C  CB    . LEU D 2 174 ? 127.809 95.769  148.084 1.00 20.62 ?  153 LEU D CB    1 
ATOM   14600 C  CG    . LEU D 2 174 ? 127.838 96.668  146.829 1.00 19.55 ?  153 LEU D CG    1 
ATOM   14601 C  CD1   . LEU D 2 174 ? 128.560 95.970  145.671 1.00 20.44 ?  153 LEU D CD1   1 
ATOM   14602 C  CD2   . LEU D 2 174 ? 126.408 97.065  146.434 1.00 20.99 ?  153 LEU D CD2   1 
ATOM   14603 N  N     . PHE D 2 175 ? 130.005 97.035  149.962 1.00 21.07 ?  154 PHE D N     1 
ATOM   14604 C  CA    . PHE D 2 175 ? 130.899 98.133  150.321 1.00 21.32 ?  154 PHE D CA    1 
ATOM   14605 C  C     . PHE D 2 175 ? 132.361 97.671  150.378 1.00 21.08 ?  154 PHE D C     1 
ATOM   14606 O  O     . PHE D 2 175 ? 133.254 98.340  149.856 1.00 20.85 ?  154 PHE D O     1 
ATOM   14607 C  CB    . PHE D 2 175 ? 130.487 98.745  151.664 1.00 21.20 ?  154 PHE D CB    1 
ATOM   14608 C  CG    . PHE D 2 175 ? 131.501 99.691  152.236 1.00 22.46 ?  154 PHE D CG    1 
ATOM   14609 C  CD1   . PHE D 2 175 ? 131.442 101.052 151.942 1.00 21.21 ?  154 PHE D CD1   1 
ATOM   14610 C  CD2   . PHE D 2 175 ? 132.516 99.229  153.079 1.00 22.53 ?  154 PHE D CD2   1 
ATOM   14611 C  CE1   . PHE D 2 175 ? 132.363 101.933 152.472 1.00 22.11 ?  154 PHE D CE1   1 
ATOM   14612 C  CE2   . PHE D 2 175 ? 133.460 100.107 153.604 1.00 23.26 ?  154 PHE D CE2   1 
ATOM   14613 C  CZ    . PHE D 2 175 ? 133.383 101.463 153.306 1.00 22.08 ?  154 PHE D CZ    1 
ATOM   14614 N  N     . LYS D 2 176 ? 132.594 96.534  151.024 1.00 21.14 ?  155 LYS D N     1 
ATOM   14615 C  CA    . LYS D 2 176 ? 133.943 95.969  151.131 1.00 20.93 ?  155 LYS D CA    1 
ATOM   14616 C  C     . LYS D 2 176 ? 134.569 95.704  149.764 1.00 20.61 ?  155 LYS D C     1 
ATOM   14617 O  O     . LYS D 2 176 ? 135.749 95.996  149.541 1.00 20.62 ?  155 LYS D O     1 
ATOM   14618 C  CB    . LYS D 2 176 ? 133.905 94.695  151.961 1.00 21.27 ?  155 LYS D CB    1 
ATOM   14619 C  CG    . LYS D 2 176 ? 133.700 94.982  153.423 1.00 22.04 ?  155 LYS D CG    1 
ATOM   14620 C  CD    . LYS D 2 176 ? 133.555 93.719  154.255 1.00 25.24 ?  155 LYS D CD    1 
ATOM   14621 C  CE    . LYS D 2 176 ? 133.418 94.097  155.707 1.00 25.83 ?  155 LYS D CE    1 
ATOM   14622 N  NZ    . LYS D 2 176 ? 133.288 92.914  156.607 1.00 26.64 1  155 LYS D NZ    1 
ATOM   14623 N  N     . ALA D 2 177 ? 133.765 95.178  148.847 1.00 20.02 ?  156 ALA D N     1 
ATOM   14624 C  CA    . ALA D 2 177 ? 134.205 94.973  147.469 1.00 19.86 ?  156 ALA D CA    1 
ATOM   14625 C  C     . ALA D 2 177 ? 134.485 96.299  146.747 1.00 19.61 ?  156 ALA D C     1 
ATOM   14626 O  O     . ALA D 2 177 ? 135.397 96.389  145.922 1.00 19.69 ?  156 ALA D O     1 
ATOM   14627 C  CB    . ALA D 2 177 ? 133.171 94.187  146.730 1.00 19.99 ?  156 ALA D CB    1 
ATOM   14628 N  N     . MET D 2 178 ? 133.693 97.325  147.051 1.00 19.75 ?  157 MET D N     1 
ATOM   14629 C  CA    . MET D 2 178 ? 133.881 98.648  146.422 1.00 18.89 ?  157 MET D CA    1 
ATOM   14630 C  C     . MET D 2 178 ? 135.183 99.275  146.895 1.00 18.62 ?  157 MET D C     1 
ATOM   14631 O  O     . MET D 2 178 ? 135.905 99.895  146.106 1.00 18.10 ?  157 MET D O     1 
ATOM   14632 C  CB    . MET D 2 178 ? 132.705 99.571  146.731 1.00 18.82 ?  157 MET D CB    1 
ATOM   14633 C  CG    . MET D 2 178 ? 131.450 99.228  145.945 1.00 20.20 ?  157 MET D CG    1 
ATOM   14634 S  SD    . MET D 2 178 ? 130.081 100.264 146.480 1.00 23.78 ?  157 MET D SD    1 
ATOM   14635 C  CE    . MET D 2 178 ? 128.861 99.829  145.244 1.00 22.62 ?  157 MET D CE    1 
ATOM   14636 N  N     . VAL D 2 179 ? 135.484 99.085  148.181 1.00 18.34 ?  158 VAL D N     1 
ATOM   14637 C  CA    . VAL D 2 179 ? 136.749 99.522  148.753 1.00 18.75 ?  158 VAL D CA    1 
ATOM   14638 C  C     . VAL D 2 179 ? 137.913 98.850  148.036 1.00 18.86 ?  158 VAL D C     1 
ATOM   14639 O  O     . VAL D 2 179 ? 138.885 99.528  147.660 1.00 18.79 ?  158 VAL D O     1 
ATOM   14640 C  CB    . VAL D 2 179 ? 136.842 99.251  150.278 1.00 19.02 ?  158 VAL D CB    1 
ATOM   14641 C  CG1   . VAL D 2 179 ? 138.269 99.521  150.777 1.00 19.10 ?  158 VAL D CG1   1 
ATOM   14642 C  CG2   . VAL D 2 179 ? 135.821 100.104 151.046 1.00 18.94 ?  158 VAL D CG2   1 
ATOM   14643 N  N     . ALA D 2 180 ? 137.814 97.526  147.863 1.00 18.96 ?  159 ALA D N     1 
ATOM   14644 C  CA    . ALA D 2 180 ? 138.805 96.764  147.100 1.00 19.05 ?  159 ALA D CA    1 
ATOM   14645 C  C     . ALA D 2 180 ? 138.951 97.317  145.680 1.00 18.67 ?  159 ALA D C     1 
ATOM   14646 O  O     . ALA D 2 180 ? 140.074 97.515  145.199 1.00 17.72 ?  159 ALA D O     1 
ATOM   14647 C  CB    . ALA D 2 180 ? 138.441 95.269  147.067 1.00 19.43 ?  159 ALA D CB    1 
ATOM   14648 N  N     . SER D 2 181 ? 137.816 97.595  145.033 1.00 18.49 ?  160 SER D N     1 
ATOM   14649 C  CA    . SER D 2 181 ? 137.829 98.143  143.675 1.00 18.51 ?  160 SER D CA    1 
ATOM   14650 C  C     . SER D 2 181 ? 138.505 99.512  143.604 1.00 18.23 ?  160 SER D C     1 
ATOM   14651 O  O     . SER D 2 181 ? 139.336 99.751  142.738 1.00 18.18 ?  160 SER D O     1 
ATOM   14652 C  CB    . SER D 2 181 ? 136.413 98.234  143.099 1.00 18.51 ?  160 SER D CB    1 
ATOM   14653 O  OG    . SER D 2 181 ? 136.487 98.604  141.736 1.00 19.42 ?  160 SER D OG    1 
ATOM   14654 N  N     . VAL D 2 182 ? 138.149 100.406 144.524 1.00 18.43 ?  161 VAL D N     1 
ATOM   14655 C  CA    . VAL D 2 182 ? 138.797 101.720 144.590 1.00 18.09 ?  161 VAL D CA    1 
ATOM   14656 C  C     . VAL D 2 182 ? 140.303 101.584 144.839 1.00 18.41 ?  161 VAL D C     1 
ATOM   14657 O  O     . VAL D 2 182 ? 141.104 102.275 144.207 1.00 18.52 ?  161 VAL D O     1 
ATOM   14658 C  CB    . VAL D 2 182 ? 138.140 102.633 145.632 1.00 17.71 ?  161 VAL D CB    1 
ATOM   14659 C  CG1   . VAL D 2 182 ? 138.967 103.925 145.835 1.00 16.02 ?  161 VAL D CG1   1 
ATOM   14660 C  CG2   . VAL D 2 182 ? 136.714 102.979 145.180 1.00 17.78 ?  161 VAL D CG2   1 
ATOM   14661 N  N     . TYR D 2 183 ? 140.686 100.662 145.724 1.00 19.06 ?  162 TYR D N     1 
ATOM   14662 C  CA    . TYR D 2 183 ? 142.106 100.437 145.977 1.00 19.73 ?  162 TYR D CA    1 
ATOM   14663 C  C     . TYR D 2 183 ? 142.828 99.958  144.725 1.00 19.90 ?  162 TYR D C     1 
ATOM   14664 O  O     . TYR D 2 183 ? 143.967 100.334 144.503 1.00 20.73 ?  162 TYR D O     1 
ATOM   14665 C  CB    . TYR D 2 183 ? 142.357 99.482  147.159 1.00 19.84 ?  162 TYR D CB    1 
ATOM   14666 C  CG    . TYR D 2 183 ? 142.076 100.083 148.520 1.00 20.24 ?  162 TYR D CG    1 
ATOM   14667 C  CD1   . TYR D 2 183 ? 141.882 101.453 148.677 1.00 21.51 ?  162 TYR D CD1   1 
ATOM   14668 C  CD2   . TYR D 2 183 ? 142.024 99.277  149.664 1.00 20.45 ?  162 TYR D CD2   1 
ATOM   14669 C  CE1   . TYR D 2 183 ? 141.628 102.008 149.938 1.00 21.68 ?  162 TYR D CE1   1 
ATOM   14670 C  CE2   . TYR D 2 183 ? 141.792 99.826  150.933 1.00 19.97 ?  162 TYR D CE2   1 
ATOM   14671 C  CZ    . TYR D 2 183 ? 141.591 101.190 151.058 1.00 21.83 ?  162 TYR D CZ    1 
ATOM   14672 O  OH    . TYR D 2 183 ? 141.351 101.743 152.300 1.00 21.96 ?  162 TYR D OH    1 
ATOM   14673 N  N     . LEU D 2 184 ? 142.172 99.154  143.900 1.00 20.22 ?  163 LEU D N     1 
ATOM   14674 C  CA    . LEU D 2 184 ? 142.802 98.712  142.660 1.00 20.89 ?  163 LEU D CA    1 
ATOM   14675 C  C     . LEU D 2 184 ? 142.918 99.885  141.675 1.00 20.72 ?  163 LEU D C     1 
ATOM   14676 O  O     . LEU D 2 184 ? 144.011 100.194 141.208 1.00 21.07 ?  163 LEU D O     1 
ATOM   14677 C  CB    . LEU D 2 184 ? 142.075 97.494  142.055 1.00 21.16 ?  163 LEU D CB    1 
ATOM   14678 C  CG    . LEU D 2 184 ? 142.570 96.909  140.717 1.00 22.77 ?  163 LEU D CG    1 
ATOM   14679 C  CD1   . LEU D 2 184 ? 144.085 96.606  140.718 1.00 22.44 ?  163 LEU D CD1   1 
ATOM   14680 C  CD2   . LEU D 2 184 ? 141.786 95.663  140.335 1.00 24.75 ?  163 LEU D CD2   1 
ATOM   14681 N  N     . GLU D 2 185 ? 141.798 100.551 141.404 1.00 20.65 ?  164 GLU D N     1 
ATOM   14682 C  CA    . GLU D 2 185 ? 141.740 101.659 140.439 1.00 20.69 ?  164 GLU D CA    1 
ATOM   14683 C  C     . GLU D 2 185 ? 142.630 102.852 140.788 1.00 20.64 ?  164 GLU D C     1 
ATOM   14684 O  O     . GLU D 2 185 ? 143.247 103.460 139.901 1.00 20.25 ?  164 GLU D O     1 
ATOM   14685 C  CB    . GLU D 2 185 ? 140.297 102.165 140.295 1.00 21.03 ?  164 GLU D CB    1 
ATOM   14686 C  CG    . GLU D 2 185 ? 139.284 101.111 139.838 1.00 22.19 ?  164 GLU D CG    1 
ATOM   14687 C  CD    . GLU D 2 185 ? 139.244 100.906 138.326 1.00 24.19 ?  164 GLU D CD    1 
ATOM   14688 O  OE1   . GLU D 2 185 ? 140.053 101.492 137.586 1.00 27.97 ?  164 GLU D OE1   1 
ATOM   14689 O  OE2   . GLU D 2 185 ? 138.376 100.166 137.861 1.00 25.47 -1 164 GLU D OE2   1 
ATOM   14690 N  N     . SER D 2 186 ? 142.667 103.203 142.070 1.00 20.42 ?  165 SER D N     1 
ATOM   14691 C  CA    . SER D 2 186 ? 143.270 104.462 142.506 1.00 20.70 ?  165 SER D CA    1 
ATOM   14692 C  C     . SER D 2 186 ? 144.592 104.297 143.254 1.00 20.88 ?  165 SER D C     1 
ATOM   14693 O  O     . SER D 2 186 ? 145.190 105.288 143.675 1.00 21.21 ?  165 SER D O     1 
ATOM   14694 C  CB    . SER D 2 186 ? 142.284 105.259 143.378 1.00 21.25 ?  165 SER D CB    1 
ATOM   14695 O  OG    . SER D 2 186 ? 141.024 105.419 142.741 1.00 20.97 ?  165 SER D OG    1 
ATOM   14696 N  N     . PHE D 2 187 ? 145.063 103.061 143.420 1.00 20.94 ?  166 PHE D N     1 
ATOM   14697 C  CA    . PHE D 2 187 ? 146.219 102.833 144.276 1.00 21.19 ?  166 PHE D CA    1 
ATOM   14698 C  C     . PHE D 2 187 ? 147.128 101.724 143.746 1.00 21.22 ?  166 PHE D C     1 
ATOM   14699 O  O     . PHE D 2 187 ? 148.281 102.004 143.400 1.00 21.10 ?  166 PHE D O     1 
ATOM   14700 C  CB    . PHE D 2 187 ? 145.759 102.645 145.748 1.00 21.63 ?  166 PHE D CB    1 
ATOM   14701 C  CG    . PHE D 2 187 ? 146.748 101.945 146.644 1.00 24.05 ?  166 PHE D CG    1 
ATOM   14702 C  CD1   . PHE D 2 187 ? 148.029 102.458 146.847 1.00 25.52 ?  166 PHE D CD1   1 
ATOM   14703 C  CD2   . PHE D 2 187 ? 146.376 100.791 147.328 1.00 27.03 ?  166 PHE D CD2   1 
ATOM   14704 C  CE1   . PHE D 2 187 ? 148.923 101.816 147.695 1.00 26.73 ?  166 PHE D CE1   1 
ATOM   14705 C  CE2   . PHE D 2 187 ? 147.281 100.136 148.176 1.00 27.36 ?  166 PHE D CE2   1 
ATOM   14706 C  CZ    . PHE D 2 187 ? 148.549 100.651 148.352 1.00 27.87 ?  166 PHE D CZ    1 
ATOM   14707 N  N     . LEU D 2 188 ? 146.608 100.505 143.630 1.00 20.78 ?  167 LEU D N     1 
ATOM   14708 C  CA    . LEU D 2 188 ? 147.434 99.342  143.246 1.00 21.78 ?  167 LEU D CA    1 
ATOM   14709 C  C     . LEU D 2 188 ? 148.048 99.416  141.843 1.00 21.91 ?  167 LEU D C     1 
ATOM   14710 O  O     . LEU D 2 188 ? 149.143 98.898  141.625 1.00 22.87 ?  167 LEU D O     1 
ATOM   14711 C  CB    . LEU D 2 188 ? 146.650 98.039  143.392 1.00 22.32 ?  167 LEU D CB    1 
ATOM   14712 C  CG    . LEU D 2 188 ? 146.225 97.544  144.774 1.00 23.33 ?  167 LEU D CG    1 
ATOM   14713 C  CD1   . LEU D 2 188 ? 145.447 96.251  144.609 1.00 22.43 ?  167 LEU D CD1   1 
ATOM   14714 C  CD2   . LEU D 2 188 ? 147.414 97.343  145.724 1.00 25.71 ?  167 LEU D CD2   1 
ATOM   14715 N  N     . PHE D 2 189 ? 147.341 100.034 140.894 1.00 21.56 ?  168 PHE D N     1 
ATOM   14716 C  CA    . PHE D 2 189 ? 147.863 100.227 139.539 1.00 21.86 ?  168 PHE D CA    1 
ATOM   14717 C  C     . PHE D 2 189 ? 149.114 101.130 139.504 1.00 21.87 ?  168 PHE D C     1 
ATOM   14718 O  O     . PHE D 2 189 ? 149.914 101.061 138.567 1.00 21.79 ?  168 PHE D O     1 
ATOM   14719 C  CB    . PHE D 2 189 ? 146.802 100.864 138.622 1.00 21.79 ?  168 PHE D CB    1 
ATOM   14720 C  CG    . PHE D 2 189 ? 145.765 99.900  138.093 1.00 21.88 ?  168 PHE D CG    1 
ATOM   14721 C  CD1   . PHE D 2 189 ? 146.107 98.603  137.706 1.00 21.44 ?  168 PHE D CD1   1 
ATOM   14722 C  CD2   . PHE D 2 189 ? 144.441 100.314 137.951 1.00 22.82 ?  168 PHE D CD2   1 
ATOM   14723 C  CE1   . PHE D 2 189 ? 145.137 97.721  137.211 1.00 22.35 ?  168 PHE D CE1   1 
ATOM   14724 C  CE2   . PHE D 2 189 ? 143.462 99.451  137.457 1.00 22.08 ?  168 PHE D CE2   1 
ATOM   14725 C  CZ    . PHE D 2 189 ? 143.807 98.146  137.096 1.00 22.60 ?  168 PHE D CZ    1 
ATOM   14726 N  N     . TYR D 2 190 ? 149.270 101.990 140.505 1.00 21.91 ?  169 TYR D N     1 
ATOM   14727 C  CA    . TYR D 2 190 ? 150.249 103.082 140.392 1.00 22.52 ?  169 TYR D CA    1 
ATOM   14728 C  C     . TYR D 2 190 ? 151.715 102.694 140.593 1.00 22.75 ?  169 TYR D C     1 
ATOM   14729 O  O     . TYR D 2 190 ? 152.587 103.360 140.051 1.00 21.93 ?  169 TYR D O     1 
ATOM   14730 C  CB    . TYR D 2 190 ? 149.836 104.298 141.227 1.00 22.67 ?  169 TYR D CB    1 
ATOM   14731 C  CG    . TYR D 2 190 ? 148.714 105.056 140.547 1.00 24.77 ?  169 TYR D CG    1 
ATOM   14732 C  CD1   . TYR D 2 190 ? 147.403 104.569 140.562 1.00 25.65 ?  169 TYR D CD1   1 
ATOM   14733 C  CD2   . TYR D 2 190 ? 148.972 106.233 139.849 1.00 25.94 ?  169 TYR D CD2   1 
ATOM   14734 C  CE1   . TYR D 2 190 ? 146.374 105.253 139.906 1.00 26.62 ?  169 TYR D CE1   1 
ATOM   14735 C  CE2   . TYR D 2 190 ? 147.952 106.930 139.206 1.00 26.91 ?  169 TYR D CE2   1 
ATOM   14736 C  CZ    . TYR D 2 190 ? 146.662 106.437 139.235 1.00 27.39 ?  169 TYR D CZ    1 
ATOM   14737 O  OH    . TYR D 2 190 ? 145.665 107.140 138.585 1.00 27.50 ?  169 TYR D OH    1 
ATOM   14738 N  N     . SER D 2 191 ? 151.981 101.610 141.329 1.00 22.74 ?  170 SER D N     1 
ATOM   14739 C  CA    . SER D 2 191 ? 153.341 101.058 141.373 1.00 23.43 ?  170 SER D CA    1 
ATOM   14740 C  C     . SER D 2 191 ? 153.752 100.626 139.965 1.00 23.08 ?  170 SER D C     1 
ATOM   14741 O  O     . SER D 2 191 ? 154.920 100.654 139.618 1.00 23.67 ?  170 SER D O     1 
ATOM   14742 C  CB    . SER D 2 191 ? 153.456 99.881  142.353 1.00 23.39 ?  170 SER D CB    1 
ATOM   14743 O  OG    . SER D 2 191 ? 152.609 98.804  141.977 1.00 24.10 ?  170 SER D OG    1 
ATOM   14744 N  N     . GLY D 2 192 ? 152.768 100.265 139.151 1.00 22.82 ?  171 GLY D N     1 
ATOM   14745 C  CA    . GLY D 2 192 ? 152.991 99.888  137.761 1.00 22.08 ?  171 GLY D CA    1 
ATOM   14746 C  C     . GLY D 2 192 ? 153.043 101.072 136.810 1.00 22.12 ?  171 GLY D C     1 
ATOM   14747 O  O     . GLY D 2 192 ? 153.978 101.185 136.015 1.00 22.86 ?  171 GLY D O     1 
ATOM   14748 N  N     . PHE D 2 193 ? 152.049 101.956 136.889 1.00 21.48 ?  172 PHE D N     1 
ATOM   14749 C  CA    . PHE D 2 193 ? 151.993 103.156 136.033 1.00 21.06 ?  172 PHE D CA    1 
ATOM   14750 C  C     . PHE D 2 193 ? 153.262 104.003 136.131 1.00 21.13 ?  172 PHE D C     1 
ATOM   14751 O  O     . PHE D 2 193 ? 153.625 104.684 135.171 1.00 21.18 ?  172 PHE D O     1 
ATOM   14752 C  CB    . PHE D 2 193 ? 150.799 104.036 136.396 1.00 21.33 ?  172 PHE D CB    1 
ATOM   14753 C  CG    . PHE D 2 193 ? 149.456 103.476 135.989 1.00 20.93 ?  172 PHE D CG    1 
ATOM   14754 C  CD1   . PHE D 2 193 ? 149.317 102.652 134.873 1.00 20.88 ?  172 PHE D CD1   1 
ATOM   14755 C  CD2   . PHE D 2 193 ? 148.319 103.824 136.706 1.00 19.83 ?  172 PHE D CD2   1 
ATOM   14756 C  CE1   . PHE D 2 193 ? 148.059 102.160 134.505 1.00 22.31 ?  172 PHE D CE1   1 
ATOM   14757 C  CE2   . PHE D 2 193 ? 147.056 103.347 136.337 1.00 20.67 ?  172 PHE D CE2   1 
ATOM   14758 C  CZ    . PHE D 2 193 ? 146.928 102.514 135.235 1.00 21.00 ?  172 PHE D CZ    1 
ATOM   14759 N  N     . TYR D 2 194 ? 153.935 103.947 137.282 1.00 20.48 ?  173 TYR D N     1 
ATOM   14760 C  CA    . TYR D 2 194 ? 155.131 104.754 137.520 1.00 20.76 ?  173 TYR D CA    1 
ATOM   14761 C  C     . TYR D 2 194 ? 156.122 104.674 136.354 1.00 20.53 ?  173 TYR D C     1 
ATOM   14762 O  O     . TYR D 2 194 ? 156.588 105.692 135.835 1.00 19.89 ?  173 TYR D O     1 
ATOM   14763 C  CB    . TYR D 2 194 ? 155.827 104.349 138.844 1.00 20.94 ?  173 TYR D CB    1 
ATOM   14764 C  CG    . TYR D 2 194 ? 156.933 105.313 139.237 1.00 21.56 ?  173 TYR D CG    1 
ATOM   14765 C  CD1   . TYR D 2 194 ? 156.710 106.311 140.189 1.00 22.23 ?  173 TYR D CD1   1 
ATOM   14766 C  CD2   . TYR D 2 194 ? 158.197 105.242 138.640 1.00 22.00 ?  173 TYR D CD2   1 
ATOM   14767 C  CE1   . TYR D 2 194 ? 157.716 107.212 140.535 1.00 21.58 ?  173 TYR D CE1   1 
ATOM   14768 C  CE2   . TYR D 2 194 ? 159.202 106.127 138.983 1.00 20.52 ?  173 TYR D CE2   1 
ATOM   14769 C  CZ    . TYR D 2 194 ? 158.956 107.110 139.928 1.00 21.66 ?  173 TYR D CZ    1 
ATOM   14770 O  OH    . TYR D 2 194 ? 159.948 108.005 140.248 1.00 21.37 ?  173 TYR D OH    1 
ATOM   14771 N  N     . TYR D 2 195 ? 156.417 103.459 135.922 1.00 20.77 ?  174 TYR D N     1 
ATOM   14772 C  CA    . TYR D 2 195 ? 157.499 103.266 134.973 1.00 21.12 ?  174 TYR D CA    1 
ATOM   14773 C  C     . TYR D 2 195 ? 157.195 103.837 133.576 1.00 21.49 ?  174 TYR D C     1 
ATOM   14774 O  O     . TYR D 2 195 ? 158.006 104.608 133.055 1.00 21.60 ?  174 TYR D O     1 
ATOM   14775 C  CB    . TYR D 2 195 ? 157.938 101.799 134.955 1.00 21.23 ?  174 TYR D CB    1 
ATOM   14776 C  CG    . TYR D 2 195 ? 159.395 101.572 134.620 1.00 21.77 ?  174 TYR D CG    1 
ATOM   14777 C  CD1   . TYR D 2 195 ? 160.394 102.432 135.091 1.00 23.28 ?  174 TYR D CD1   1 
ATOM   14778 C  CD2   . TYR D 2 195 ? 159.780 100.477 133.849 1.00 22.87 ?  174 TYR D CD2   1 
ATOM   14779 C  CE1   . TYR D 2 195 ? 161.742 102.206 134.778 1.00 23.81 ?  174 TYR D CE1   1 
ATOM   14780 C  CE2   . TYR D 2 195 ? 161.118 100.243 133.543 1.00 24.09 ?  174 TYR D CE2   1 
ATOM   14781 C  CZ    . TYR D 2 195 ? 162.089 101.109 134.003 1.00 23.51 ?  174 TYR D CZ    1 
ATOM   14782 O  OH    . TYR D 2 195 ? 163.413 100.876 133.688 1.00 25.36 ?  174 TYR D OH    1 
ATOM   14783 N  N     . PRO D 2 196 ? 156.033 103.481 132.971 1.00 21.86 ?  175 PRO D N     1 
ATOM   14784 C  CA    . PRO D 2 196 ? 155.662 104.110 131.694 1.00 22.03 ?  175 PRO D CA    1 
ATOM   14785 C  C     . PRO D 2 196 ? 155.602 105.634 131.776 1.00 22.18 ?  175 PRO D C     1 
ATOM   14786 O  O     . PRO D 2 196 ? 156.013 106.305 130.826 1.00 23.00 ?  175 PRO D O     1 
ATOM   14787 C  CB    . PRO D 2 196 ? 154.262 103.554 131.403 1.00 21.50 ?  175 PRO D CB    1 
ATOM   14788 C  CG    . PRO D 2 196 ? 154.158 102.330 132.168 1.00 22.47 ?  175 PRO D CG    1 
ATOM   14789 C  CD    . PRO D 2 196 ? 155.142 102.354 133.300 1.00 20.91 ?  175 PRO D CD    1 
ATOM   14790 N  N     . LEU D 2 197 ? 155.110 106.175 132.893 1.00 21.70 ?  176 LEU D N     1 
ATOM   14791 C  CA    . LEU D 2 197 ? 155.087 107.631 133.095 1.00 22.40 ?  176 LEU D CA    1 
ATOM   14792 C  C     . LEU D 2 197 ? 156.492 108.229 133.205 1.00 22.58 ?  176 LEU D C     1 
ATOM   14793 O  O     . LEU D 2 197 ? 156.745 109.335 132.711 1.00 22.15 ?  176 LEU D O     1 
ATOM   14794 C  CB    . LEU D 2 197 ? 154.292 108.001 134.340 1.00 22.15 ?  176 LEU D CB    1 
ATOM   14795 C  CG    . LEU D 2 197 ? 152.766 107.840 134.333 1.00 23.08 ?  176 LEU D CG    1 
ATOM   14796 C  CD1   . LEU D 2 197 ? 152.271 107.921 135.767 1.00 21.62 ?  176 LEU D CD1   1 
ATOM   14797 C  CD2   . LEU D 2 197 ? 152.096 108.910 133.448 1.00 21.94 ?  176 LEU D CD2   1 
ATOM   14798 N  N     . TYR D 2 198 ? 157.386 107.487 133.863 1.00 22.76 ?  177 TYR D N     1 
ATOM   14799 C  CA    . TYR D 2 198 ? 158.799 107.849 133.990 1.00 23.23 ?  177 TYR D CA    1 
ATOM   14800 C  C     . TYR D 2 198 ? 159.470 107.939 132.619 1.00 23.91 ?  177 TYR D C     1 
ATOM   14801 O  O     . TYR D 2 198 ? 160.169 108.922 132.329 1.00 24.20 ?  177 TYR D O     1 
ATOM   14802 C  CB    . TYR D 2 198 ? 159.522 106.850 134.909 1.00 23.19 ?  177 TYR D CB    1 
ATOM   14803 C  CG    . TYR D 2 198 ? 160.990 107.129 135.165 1.00 23.52 ?  177 TYR D CG    1 
ATOM   14804 C  CD1   . TYR D 2 198 ? 161.391 108.245 135.886 1.00 24.85 ?  177 TYR D CD1   1 
ATOM   14805 C  CD2   . TYR D 2 198 ? 161.978 106.242 134.719 1.00 25.30 ?  177 TYR D CD2   1 
ATOM   14806 C  CE1   . TYR D 2 198 ? 162.742 108.496 136.141 1.00 26.05 ?  177 TYR D CE1   1 
ATOM   14807 C  CE2   . TYR D 2 198 ? 163.339 106.482 134.974 1.00 26.38 ?  177 TYR D CE2   1 
ATOM   14808 C  CZ    . TYR D 2 198 ? 163.704 107.610 135.685 1.00 26.68 ?  177 TYR D CZ    1 
ATOM   14809 O  OH    . TYR D 2 198 ? 165.030 107.868 135.952 1.00 30.01 ?  177 TYR D OH    1 
ATOM   14810 N  N     . PHE D 2 199 ? 159.258 106.936 131.768 1.00 24.84 ?  178 PHE D N     1 
ATOM   14811 C  CA    . PHE D 2 199 ? 159.760 107.014 130.392 1.00 25.81 ?  178 PHE D CA    1 
ATOM   14812 C  C     . PHE D 2 199 ? 159.108 108.127 129.581 1.00 26.23 ?  178 PHE D C     1 
ATOM   14813 O  O     . PHE D 2 199 ? 159.794 108.876 128.885 1.00 26.58 ?  178 PHE D O     1 
ATOM   14814 C  CB    . PHE D 2 199 ? 159.621 105.680 129.671 1.00 26.08 ?  178 PHE D CB    1 
ATOM   14815 C  CG    . PHE D 2 199 ? 160.638 104.663 130.092 1.00 28.71 ?  178 PHE D CG    1 
ATOM   14816 C  CD1   . PHE D 2 199 ? 161.979 105.007 130.205 1.00 32.03 ?  178 PHE D CD1   1 
ATOM   14817 C  CD2   . PHE D 2 199 ? 160.262 103.362 130.383 1.00 31.77 ?  178 PHE D CD2   1 
ATOM   14818 C  CE1   . PHE D 2 199 ? 162.938 104.066 130.611 1.00 32.29 ?  178 PHE D CE1   1 
ATOM   14819 C  CE2   . PHE D 2 199 ? 161.214 102.416 130.779 1.00 32.72 ?  178 PHE D CE2   1 
ATOM   14820 C  CZ    . PHE D 2 199 ? 162.553 102.776 130.890 1.00 31.91 ?  178 PHE D CZ    1 
ATOM   14821 N  N     . TYR D 2 200 ? 157.785 108.216 129.685 1.00 26.46 ?  179 TYR D N     1 
ATOM   14822 C  CA    . TYR D 2 200 ? 156.969 109.211 128.972 1.00 27.43 ?  179 TYR D CA    1 
ATOM   14823 C  C     . TYR D 2 200 ? 157.433 110.628 129.294 1.00 27.68 ?  179 TYR D C     1 
ATOM   14824 O  O     . TYR D 2 200 ? 157.492 111.482 128.411 1.00 28.71 ?  179 TYR D O     1 
ATOM   14825 C  CB    . TYR D 2 200 ? 155.516 109.029 129.397 1.00 27.27 ?  179 TYR D CB    1 
ATOM   14826 C  CG    . TYR D 2 200 ? 154.449 109.651 128.530 1.00 28.90 ?  179 TYR D CG    1 
ATOM   14827 C  CD1   . TYR D 2 200 ? 154.452 109.493 127.151 1.00 29.00 ?  179 TYR D CD1   1 
ATOM   14828 C  CD2   . TYR D 2 200 ? 153.387 110.347 129.115 1.00 30.14 ?  179 TYR D CD2   1 
ATOM   14829 C  CE1   . TYR D 2 200 ? 153.445 110.045 126.363 1.00 31.26 ?  179 TYR D CE1   1 
ATOM   14830 C  CE2   . TYR D 2 200 ? 152.374 110.892 128.345 1.00 31.86 ?  179 TYR D CE2   1 
ATOM   14831 C  CZ    . TYR D 2 200 ? 152.409 110.743 126.968 1.00 32.51 ?  179 TYR D CZ    1 
ATOM   14832 O  OH    . TYR D 2 200 ? 151.406 111.287 126.203 1.00 33.77 ?  179 TYR D OH    1 
ATOM   14833 N  N     . GLY D 2 201 ? 157.766 110.869 130.561 1.00 27.68 ?  180 GLY D N     1 
ATOM   14834 C  CA    . GLY D 2 201 ? 158.284 112.162 130.996 1.00 28.02 ?  180 GLY D CA    1 
ATOM   14835 C  C     . GLY D 2 201 ? 159.694 112.489 130.513 1.00 28.60 ?  180 GLY D C     1 
ATOM   14836 O  O     . GLY D 2 201 ? 160.117 113.634 130.602 1.00 28.44 ?  180 GLY D O     1 
ATOM   14837 N  N     . GLN D 2 202 ? 160.415 111.476 130.022 1.00 29.34 ?  181 GLN D N     1 
ATOM   14838 C  CA    . GLN D 2 202 ? 161.785 111.613 129.497 1.00 30.39 ?  181 GLN D CA    1 
ATOM   14839 C  C     . GLN D 2 202 ? 161.854 111.624 127.969 1.00 30.55 ?  181 GLN D C     1 
ATOM   14840 O  O     . GLN D 2 202 ? 162.944 111.748 127.402 1.00 31.23 ?  181 GLN D O     1 
ATOM   14841 C  CB    . GLN D 2 202 ? 162.638 110.413 129.913 1.00 30.31 ?  181 GLN D CB    1 
ATOM   14842 C  CG    . GLN D 2 202 ? 162.975 110.259 131.347 1.00 32.40 ?  181 GLN D CG    1 
ATOM   14843 C  CD    . GLN D 2 202 ? 163.811 109.014 131.559 1.00 33.85 ?  181 GLN D CD    1 
ATOM   14844 O  OE1   . GLN D 2 202 ? 163.328 108.002 132.060 1.00 33.94 ?  181 GLN D OE1   1 
ATOM   14845 N  NE2   . GLN D 2 202 ? 165.061 109.070 131.134 1.00 34.92 ?  181 GLN D NE2   1 
ATOM   14846 N  N     . GLY D 2 203 ? 160.723 111.423 127.303 1.00 30.57 ?  182 GLY D N     1 
ATOM   14847 C  CA    . GLY D 2 203 ? 160.703 111.348 125.841 1.00 30.83 ?  182 GLY D CA    1 
ATOM   14848 C  C     . GLY D 2 203 ? 160.927 109.950 125.285 1.00 30.80 ?  182 GLY D C     1 
ATOM   14849 O  O     . GLY D 2 203 ? 161.134 109.784 124.079 1.00 30.86 ?  182 GLY D O     1 
ATOM   14850 N  N     . LYS D 2 204 ? 160.880 108.944 126.159 1.00 30.14 ?  183 LYS D N     1 
ATOM   14851 C  CA    . LYS D 2 204 ? 161.045 107.547 125.747 1.00 30.35 ?  183 LYS D CA    1 
ATOM   14852 C  C     . LYS D 2 204 ? 159.712 106.801 125.721 1.00 29.52 ?  183 LYS D C     1 
ATOM   14853 O  O     . LYS D 2 204 ? 158.833 107.077 126.534 1.00 28.60 ?  183 LYS D O     1 
ATOM   14854 C  CB    . LYS D 2 204 ? 162.031 106.832 126.668 1.00 30.76 ?  183 LYS D CB    1 
ATOM   14855 C  CG    . LYS D 2 204 ? 163.461 107.373 126.573 1.00 32.95 ?  183 LYS D CG    1 
ATOM   14856 C  CD    . LYS D 2 204 ? 164.298 106.822 127.702 1.00 36.37 ?  183 LYS D CD    1 
ATOM   14857 C  CE    . LYS D 2 204 ? 165.729 107.327 127.653 1.00 38.47 ?  183 LYS D CE    1 
ATOM   14858 N  NZ    . LYS D 2 204 ? 166.405 106.941 128.928 1.00 40.21 1  183 LYS D NZ    1 
ATOM   14859 N  N     . LEU D 2 205 ? 159.579 105.853 124.790 1.00 29.47 ?  184 LEU D N     1 
ATOM   14860 C  CA    . LEU D 2 205 ? 158.356 105.052 124.626 1.00 29.06 ?  184 LEU D CA    1 
ATOM   14861 C  C     . LEU D 2 205 ? 157.085 105.921 124.729 1.00 28.96 ?  184 LEU D C     1 
ATOM   14862 O  O     . LEU D 2 205 ? 156.182 105.661 125.534 1.00 27.68 ?  184 LEU D O     1 
ATOM   14863 C  CB    . LEU D 2 205 ? 158.322 103.886 125.627 1.00 28.63 ?  184 LEU D CB    1 
ATOM   14864 C  CG    . LEU D 2 205 ? 159.500 102.899 125.623 1.00 29.00 ?  184 LEU D CG    1 
ATOM   14865 C  CD1   . LEU D 2 205 ? 159.326 101.861 126.734 1.00 28.90 ?  184 LEU D CD1   1 
ATOM   14866 C  CD2   . LEU D 2 205 ? 159.646 102.207 124.274 1.00 28.67 ?  184 LEU D CD2   1 
ATOM   14867 N  N     . MET D 2 206 ? 157.050 106.951 123.888 1.00 29.02 ?  185 MET D N     1 
ATOM   14868 C  CA    . MET D 2 206 ? 155.996 107.953 123.873 1.00 29.72 ?  185 MET D CA    1 
ATOM   14869 C  C     . MET D 2 206 ? 154.628 107.463 123.408 1.00 29.54 ?  185 MET D C     1 
ATOM   14870 O  O     . MET D 2 206 ? 153.610 107.961 123.882 1.00 29.47 ?  185 MET D O     1 
ATOM   14871 C  CB    . MET D 2 206 ? 156.432 109.150 123.018 1.00 30.69 ?  185 MET D CB    1 
ATOM   14872 C  CG    . MET D 2 206 ? 157.713 109.799 123.518 1.00 32.03 ?  185 MET D CG    1 
ATOM   14873 S  SD    . MET D 2 206 ? 157.540 110.370 125.219 1.00 36.63 ?  185 MET D SD    1 
ATOM   14874 C  CE    . MET D 2 206 ? 156.796 111.969 124.952 1.00 33.80 ?  185 MET D CE    1 
ATOM   14875 N  N     . GLN D 2 207 ? 154.605 106.516 122.471 1.00 29.56 ?  186 GLN D N     1 
ATOM   14876 C  CA    . GLN D 2 207 ? 153.345 105.992 121.934 1.00 29.17 ?  186 GLN D CA    1 
ATOM   14877 C  C     . GLN D 2 207 ? 152.645 105.112 122.965 1.00 28.26 ?  186 GLN D C     1 
ATOM   14878 O  O     . GLN D 2 207 ? 151.452 105.273 123.208 1.00 27.98 ?  186 GLN D O     1 
ATOM   14879 C  CB    . GLN D 2 207 ? 153.570 105.215 120.627 1.00 29.80 ?  186 GLN D CB    1 
ATOM   14880 C  CG    . GLN D 2 207 ? 154.318 105.991 119.544 1.00 31.75 ?  186 GLN D CG    1 
ATOM   14881 C  CD    . GLN D 2 207 ? 153.697 107.348 119.279 1.00 34.93 ?  186 GLN D CD    1 
ATOM   14882 O  OE1   . GLN D 2 207 ? 152.606 107.452 118.704 1.00 36.91 ?  186 GLN D OE1   1 
ATOM   14883 N  NE2   . GLN D 2 207 ? 154.384 108.400 119.710 1.00 36.09 ?  186 GLN D NE2   1 
ATOM   14884 N  N     . SER D 2 208 ? 153.386 104.187 123.571 0.50 27.75 ?  187 SER D N     1 
ATOM   14885 C  CA    . SER D 2 208 ? 152.823 103.334 124.611 0.50 27.12 ?  187 SER D CA    1 
ATOM   14886 C  C     . SER D 2 208 ? 152.538 104.138 125.875 0.50 26.72 ?  187 SER D C     1 
ATOM   14887 O  O     . SER D 2 208 ? 151.589 103.834 126.597 0.50 26.30 ?  187 SER D O     1 
ATOM   14888 C  CB    . SER D 2 208 ? 153.743 102.150 124.917 0.50 26.88 ?  187 SER D CB    1 
ATOM   14889 O  OG    . SER D 2 208 ? 155.055 102.595 125.184 0.50 26.59 ?  187 SER D OG    1 
ATOM   14890 N  N     . GLY D 2 209 ? 153.356 105.160 126.131 1.00 26.64 ?  188 GLY D N     1 
ATOM   14891 C  CA    . GLY D 2 209 ? 153.135 106.081 127.265 1.00 26.43 ?  188 GLY D CA    1 
ATOM   14892 C  C     . GLY D 2 209 ? 151.859 106.899 127.113 1.00 26.66 ?  188 GLY D C     1 
ATOM   14893 O  O     . GLY D 2 209 ? 151.167 107.180 128.092 1.00 26.57 ?  188 GLY D O     1 
ATOM   14894 N  N     . GLU D 2 210 ? 151.547 107.291 125.881 1.00 27.42 ?  189 GLU D N     1 
ATOM   14895 C  CA    . GLU D 2 210 ? 150.291 107.982 125.596 1.00 27.73 ?  189 GLU D CA    1 
ATOM   14896 C  C     . GLU D 2 210 ? 149.105 107.047 125.876 1.00 27.04 ?  189 GLU D C     1 
ATOM   14897 O  O     . GLU D 2 210 ? 148.136 107.440 126.527 1.00 26.57 ?  189 GLU D O     1 
ATOM   14898 C  CB    . GLU D 2 210 ? 150.261 108.509 124.150 1.00 28.28 ?  189 GLU D CB    1 
ATOM   14899 C  CG    . GLU D 2 210 ? 149.004 109.331 123.824 1.00 30.71 ?  189 GLU D CG    1 
ATOM   14900 C  CD    . GLU D 2 210 ? 149.069 110.080 122.495 1.00 35.43 ?  189 GLU D CD    1 
ATOM   14901 O  OE1   . GLU D 2 210 ? 150.020 109.868 121.702 1.00 36.89 ?  189 GLU D OE1   1 
ATOM   14902 O  OE2   . GLU D 2 210 ? 148.156 110.901 122.249 1.00 37.04 -1 189 GLU D OE2   1 
ATOM   14903 N  N     . ILE D 2 211 ? 149.197 105.812 125.395 1.00 26.80 ?  190 ILE D N     1 
ATOM   14904 C  CA    . ILE D 2 211 ? 148.186 104.800 125.687 1.00 26.92 ?  190 ILE D CA    1 
ATOM   14905 C  C     . ILE D 2 211 ? 148.011 104.615 127.188 1.00 26.45 ?  190 ILE D C     1 
ATOM   14906 O  O     . ILE D 2 211 ? 146.883 104.616 127.677 1.00 26.65 ?  190 ILE D O     1 
ATOM   14907 C  CB    . ILE D 2 211 ? 148.489 103.451 124.986 1.00 27.00 ?  190 ILE D CB    1 
ATOM   14908 C  CG1   . ILE D 2 211 ? 148.283 103.600 123.474 1.00 28.77 ?  190 ILE D CG1   1 
ATOM   14909 C  CG2   . ILE D 2 211 ? 147.588 102.334 125.538 1.00 26.82 ?  190 ILE D CG2   1 
ATOM   14910 C  CD1   . ILE D 2 211 ? 148.695 102.390 122.646 1.00 30.88 ?  190 ILE D CD1   1 
ATOM   14911 N  N     . ILE D 2 212 ? 149.119 104.486 127.924 1.00 26.49 ?  191 ILE D N     1 
ATOM   14912 C  CA    . ILE D 2 212 ? 149.043 104.258 129.367 1.00 25.73 ?  191 ILE D CA    1 
ATOM   14913 C  C     . ILE D 2 212 ? 148.378 105.443 130.071 1.00 25.48 ?  191 ILE D C     1 
ATOM   14914 O  O     . ILE D 2 212 ? 147.580 105.260 130.994 1.00 24.95 ?  191 ILE D O     1 
ATOM   14915 C  CB    . ILE D 2 212 ? 150.433 103.938 129.993 1.00 26.44 ?  191 ILE D CB    1 
ATOM   14916 C  CG1   . ILE D 2 212 ? 150.977 102.605 129.461 1.00 26.71 ?  191 ILE D CG1   1 
ATOM   14917 C  CG2   . ILE D 2 212 ? 150.363 103.929 131.536 1.00 26.01 ?  191 ILE D CG2   1 
ATOM   14918 C  CD1   . ILE D 2 212 ? 150.149 101.375 129.785 1.00 30.50 ?  191 ILE D CD1   1 
ATOM   14919 N  N     . ASN D 2 213 ? 148.693 106.650 129.612 1.00 24.79 ?  192 ASN D N     1 
ATOM   14920 C  CA    . ASN D 2 213 ? 148.097 107.855 130.172 1.00 24.80 ?  192 ASN D CA    1 
ATOM   14921 C  C     . ASN D 2 213 ? 146.567 107.904 129.977 1.00 24.44 ?  192 ASN D C     1 
ATOM   14922 O  O     . ASN D 2 213 ? 145.837 108.403 130.841 1.00 23.25 ?  192 ASN D O     1 
ATOM   14923 C  CB    . ASN D 2 213 ? 148.772 109.097 129.588 1.00 25.68 ?  192 ASN D CB    1 
ATOM   14924 C  CG    . ASN D 2 213 ? 148.935 110.208 130.608 1.00 27.89 ?  192 ASN D CG    1 
ATOM   14925 O  OD1   . ASN D 2 213 ? 149.085 109.961 131.802 1.00 31.05 ?  192 ASN D OD1   1 
ATOM   14926 N  ND2   . ASN D 2 213 ? 148.912 111.446 130.134 1.00 31.70 ?  192 ASN D ND2   1 
ATOM   14927 N  N     . LEU D 2 214 ? 146.090 107.372 128.851 1.00 23.60 ?  193 LEU D N     1 
ATOM   14928 C  CA    . LEU D 2 214 ? 144.652 107.326 128.582 1.00 23.84 ?  193 LEU D CA    1 
ATOM   14929 C  C     . LEU D 2 214 ? 143.986 106.295 129.476 1.00 23.48 ?  193 LEU D C     1 
ATOM   14930 O  O     . LEU D 2 214 ? 142.902 106.541 130.013 1.00 24.12 ?  193 LEU D O     1 
ATOM   14931 C  CB    . LEU D 2 214 ? 144.385 107.005 127.112 1.00 23.71 ?  193 LEU D CB    1 
ATOM   14932 C  CG    . LEU D 2 214 ? 144.671 108.144 126.125 1.00 25.29 ?  193 LEU D CG    1 
ATOM   14933 C  CD1   . LEU D 2 214 ? 144.510 107.657 124.684 1.00 25.41 ?  193 LEU D CD1   1 
ATOM   14934 C  CD2   . LEU D 2 214 ? 143.775 109.346 126.380 1.00 25.80 ?  193 LEU D CD2   1 
ATOM   14935 N  N     . ILE D 2 215 ? 144.646 105.148 129.636 1.00 22.89 ?  194 ILE D N     1 
ATOM   14936 C  CA    . ILE D 2 215 ? 144.170 104.093 130.519 1.00 22.25 ?  194 ILE D CA    1 
ATOM   14937 C  C     . ILE D 2 215 ? 144.087 104.634 131.943 1.00 22.55 ?  194 ILE D C     1 
ATOM   14938 O  O     . ILE D 2 215 ? 143.052 104.508 132.612 1.00 22.53 ?  194 ILE D O     1 
ATOM   14939 C  CB    . ILE D 2 215 ? 145.092 102.857 130.486 1.00 22.37 ?  194 ILE D CB    1 
ATOM   14940 C  CG1   . ILE D 2 215 ? 145.030 102.184 129.108 1.00 21.89 ?  194 ILE D CG1   1 
ATOM   14941 C  CG2   . ILE D 2 215 ? 144.725 101.878 131.619 1.00 20.25 ?  194 ILE D CG2   1 
ATOM   14942 C  CD1   . ILE D 2 215 ? 145.926 100.947 128.966 1.00 20.48 ?  194 ILE D CD1   1 
ATOM   14943 N  N     . LEU D 2 216 ? 145.175 105.251 132.395 1.00 22.35 ?  195 LEU D N     1 
ATOM   14944 C  CA    . LEU D 2 216 ? 145.255 105.774 133.756 1.00 22.51 ?  195 LEU D CA    1 
ATOM   14945 C  C     . LEU D 2 216 ? 144.141 106.794 134.004 1.00 22.30 ?  195 LEU D C     1 
ATOM   14946 O  O     . LEU D 2 216 ? 143.523 106.790 135.077 1.00 21.62 ?  195 LEU D O     1 
ATOM   14947 C  CB    . LEU D 2 216 ? 146.639 106.402 133.986 1.00 23.06 ?  195 LEU D CB    1 
ATOM   14948 C  CG    . LEU D 2 216 ? 147.030 107.155 135.267 1.00 23.98 ?  195 LEU D CG    1 
ATOM   14949 C  CD1   . LEU D 2 216 ? 148.531 107.277 135.299 1.00 24.44 ?  195 LEU D CD1   1 
ATOM   14950 C  CD2   . LEU D 2 216 ? 146.395 108.553 135.340 1.00 25.00 ?  195 LEU D CD2   1 
ATOM   14951 N  N     . ARG D 2 217 ? 143.897 107.663 133.017 1.00 21.64 ?  196 ARG D N     1 
ATOM   14952 C  CA    . ARG D 2 217 ? 142.825 108.661 133.107 1.00 22.49 ?  196 ARG D CA    1 
ATOM   14953 C  C     . ARG D 2 217 ? 141.437 107.995 133.277 1.00 21.56 ?  196 ARG D C     1 
ATOM   14954 O  O     . ARG D 2 217 ? 140.614 108.485 134.039 1.00 21.32 ?  196 ARG D O     1 
ATOM   14955 C  CB    . ARG D 2 217 ? 142.844 109.638 131.915 1.00 23.07 ?  196 ARG D CB    1 
ATOM   14956 C  CG    . ARG D 2 217 ? 141.851 110.813 132.049 1.00 25.64 ?  196 ARG D CG    1 
ATOM   14957 C  CD    . ARG D 2 217 ? 141.726 111.649 130.761 1.00 32.11 ?  196 ARG D CD    1 
ATOM   14958 N  NE    . ARG D 2 217 ? 141.285 110.845 129.613 1.00 35.06 ?  196 ARG D NE    1 
ATOM   14959 C  CZ    . ARG D 2 217 ? 140.891 111.341 128.445 1.00 37.65 ?  196 ARG D CZ    1 
ATOM   14960 N  NH1   . ARG D 2 217 ? 140.850 112.656 128.253 1.00 40.20 1  196 ARG D NH1   1 
ATOM   14961 N  NH2   . ARG D 2 217 ? 140.522 110.522 127.465 1.00 38.20 ?  196 ARG D NH2   1 
ATOM   14962 N  N     . ASP D 2 218 ? 141.189 106.887 132.577 1.00 21.34 ?  197 ASP D N     1 
ATOM   14963 C  CA    . ASP D 2 218 ? 139.976 106.086 132.804 1.00 21.09 ?  197 ASP D CA    1 
ATOM   14964 C  C     . ASP D 2 218 ? 139.938 105.490 134.226 1.00 20.65 ?  197 ASP D C     1 
ATOM   14965 O  O     . ASP D 2 218 ? 138.911 105.577 134.904 1.00 20.16 ?  197 ASP D O     1 
ATOM   14966 C  CB    . ASP D 2 218 ? 139.842 104.959 131.769 1.00 21.58 ?  197 ASP D CB    1 
ATOM   14967 C  CG    . ASP D 2 218 ? 139.593 105.472 130.351 1.00 22.60 ?  197 ASP D CG    1 
ATOM   14968 O  OD1   . ASP D 2 218 ? 139.091 106.607 130.177 1.00 24.72 ?  197 ASP D OD1   1 
ATOM   14969 O  OD2   . ASP D 2 218 ? 139.917 104.725 129.399 1.00 22.64 -1 197 ASP D OD2   1 
ATOM   14970 N  N     . GLU D 2 219 ? 141.037 104.885 134.682 1.00 20.59 ?  198 GLU D N     1 
ATOM   14971 C  CA    . GLU D 2 219 ? 141.037 104.260 136.024 1.00 20.66 ?  198 GLU D CA    1 
ATOM   14972 C  C     . GLU D 2 219 ? 140.795 105.290 137.130 1.00 20.45 ?  198 GLU D C     1 
ATOM   14973 O  O     . GLU D 2 219 ? 140.124 104.993 138.123 1.00 20.59 ?  198 GLU D O     1 
ATOM   14974 C  CB    . GLU D 2 219 ? 142.323 103.467 136.305 1.00 20.55 ?  198 GLU D CB    1 
ATOM   14975 C  CG    . GLU D 2 219 ? 142.867 102.594 135.132 1.00 21.99 ?  198 GLU D CG    1 
ATOM   14976 C  CD    . GLU D 2 219 ? 141.920 101.494 134.635 1.00 24.00 ?  198 GLU D CD    1 
ATOM   14977 O  OE1   . GLU D 2 219 ? 140.684 101.585 134.796 1.00 25.06 ?  198 GLU D OE1   1 
ATOM   14978 O  OE2   . GLU D 2 219 ? 142.419 100.525 134.039 1.00 24.49 -1 198 GLU D OE2   1 
ATOM   14979 N  N     . ALA D 2 220 ? 141.325 106.497 136.947 1.00 20.47 ?  199 ALA D N     1 
ATOM   14980 C  CA    . ALA D 2 220 ? 141.095 107.602 137.901 1.00 21.10 ?  199 ALA D CA    1 
ATOM   14981 C  C     . ALA D 2 220 ? 139.609 107.897 138.089 1.00 21.34 ?  199 ALA D C     1 
ATOM   14982 O  O     . ALA D 2 220 ? 139.119 107.885 139.217 1.00 21.19 ?  199 ALA D O     1 
ATOM   14983 C  CB    . ALA D 2 220 ? 141.857 108.863 137.487 1.00 21.09 ?  199 ALA D CB    1 
ATOM   14984 N  N     . ILE D 2 221 ? 138.892 108.131 136.988 1.00 21.31 ?  200 ILE D N     1 
ATOM   14985 C  CA    . ILE D 2 221 ? 137.448 108.337 137.069 1.00 21.80 ?  200 ILE D CA    1 
ATOM   14986 C  C     . ILE D 2 221 ? 136.674 107.097 137.566 1.00 20.90 ?  200 ILE D C     1 
ATOM   14987 O  O     . ILE D 2 221 ? 135.702 107.238 138.306 1.00 20.54 ?  200 ILE D O     1 
ATOM   14988 C  CB    . ILE D 2 221 ? 136.843 108.942 135.769 1.00 22.75 ?  200 ILE D CB    1 
ATOM   14989 C  CG1   . ILE D 2 221 ? 135.459 109.509 136.063 1.00 24.63 ?  200 ILE D CG1   1 
ATOM   14990 C  CG2   . ILE D 2 221 ? 136.745 107.904 134.653 1.00 23.38 ?  200 ILE D CG2   1 
ATOM   14991 C  CD1   . ILE D 2 221 ? 135.001 110.543 135.076 1.00 26.91 ?  200 ILE D CD1   1 
ATOM   14992 N  N     . HIS D 2 222 ? 137.123 105.890 137.200 1.00 20.31 ?  201 HIS D N     1 
ATOM   14993 C  CA    . HIS D 2 222 ? 136.505 104.673 137.733 1.00 20.25 ?  201 HIS D CA    1 
ATOM   14994 C  C     . HIS D 2 222 ? 136.599 104.654 139.257 1.00 20.51 ?  201 HIS D C     1 
ATOM   14995 O  O     . HIS D 2 222 ? 135.597 104.437 139.949 1.00 20.99 ?  201 HIS D O     1 
ATOM   14996 C  CB    . HIS D 2 222 ? 137.139 103.400 137.160 1.00 19.79 ?  201 HIS D CB    1 
ATOM   14997 C  CG    . HIS D 2 222 ? 137.002 103.247 135.676 1.00 19.25 ?  201 HIS D CG    1 
ATOM   14998 N  ND1   . HIS D 2 222 ? 137.647 102.247 134.980 1.00 18.35 ?  201 HIS D ND1   1 
ATOM   14999 C  CD2   . HIS D 2 222 ? 136.312 103.964 134.754 1.00 17.64 ?  201 HIS D CD2   1 
ATOM   15000 C  CE1   . HIS D 2 222 ? 137.351 102.342 133.695 1.00 18.28 ?  201 HIS D CE1   1 
ATOM   15001 N  NE2   . HIS D 2 222 ? 136.550 103.381 133.530 1.00 20.01 ?  201 HIS D NE2   1 
ATOM   15002 N  N     . GLY D 2 223 ? 137.803 104.907 139.775 1.00 20.33 ?  202 GLY D N     1 
ATOM   15003 C  CA    . GLY D 2 223 ? 138.039 104.969 141.223 1.00 19.94 ?  202 GLY D CA    1 
ATOM   15004 C  C     . GLY D 2 223 ? 137.187 106.011 141.938 1.00 19.80 ?  202 GLY D C     1 
ATOM   15005 O  O     . GLY D 2 223 ? 136.609 105.724 142.985 1.00 19.96 ?  202 GLY D O     1 
ATOM   15006 N  N     . VAL D 2 224 ? 137.080 107.211 141.364 1.00 19.49 ?  203 VAL D N     1 
ATOM   15007 C  CA    . VAL D 2 224 ? 136.249 108.273 141.955 1.00 18.88 ?  203 VAL D CA    1 
ATOM   15008 C  C     . VAL D 2 224 ? 134.766 107.880 141.999 1.00 18.55 ?  203 VAL D C     1 
ATOM   15009 O  O     . VAL D 2 224 ? 134.086 108.070 143.020 1.00 17.65 ?  203 VAL D O     1 
ATOM   15010 C  CB    . VAL D 2 224 ? 136.433 109.652 141.220 1.00 19.22 ?  203 VAL D CB    1 
ATOM   15011 C  CG1   . VAL D 2 224 ? 135.528 110.734 141.845 1.00 18.51 ?  203 VAL D CG1   1 
ATOM   15012 C  CG2   . VAL D 2 224 ? 137.907 110.105 141.267 1.00 19.69 ?  203 VAL D CG2   1 
ATOM   15013 N  N     . TYR D 2 225 ? 134.278 107.308 140.900 1.00 18.17 ?  204 TYR D N     1 
ATOM   15014 C  CA    . TYR D 2 225 ? 132.873 106.912 140.784 1.00 18.76 ?  204 TYR D CA    1 
ATOM   15015 C  C     . TYR D 2 225 ? 132.508 105.790 141.772 1.00 18.93 ?  204 TYR D C     1 
ATOM   15016 O  O     . TYR D 2 225 ? 131.547 105.911 142.544 1.00 18.77 ?  204 TYR D O     1 
ATOM   15017 C  CB    . TYR D 2 225 ? 132.527 106.497 139.340 1.00 18.96 ?  204 TYR D CB    1 
ATOM   15018 C  CG    . TYR D 2 225 ? 131.039 106.212 139.172 1.00 20.06 ?  204 TYR D CG    1 
ATOM   15019 C  CD1   . TYR D 2 225 ? 130.099 107.244 139.294 1.00 21.79 ?  204 TYR D CD1   1 
ATOM   15020 C  CD2   . TYR D 2 225 ? 130.572 104.917 138.927 1.00 19.51 ?  204 TYR D CD2   1 
ATOM   15021 C  CE1   . TYR D 2 225 ? 128.731 106.994 139.171 1.00 20.38 ?  204 TYR D CE1   1 
ATOM   15022 C  CE2   . TYR D 2 225 ? 129.190 104.657 138.795 1.00 19.38 ?  204 TYR D CE2   1 
ATOM   15023 C  CZ    . TYR D 2 225 ? 128.285 105.707 138.924 1.00 20.84 ?  204 TYR D CZ    1 
ATOM   15024 O  OH    . TYR D 2 225 ? 126.929 105.488 138.817 1.00 20.77 ?  204 TYR D OH    1 
ATOM   15025 N  N     . VAL D 2 226 ? 133.280 104.705 141.755 1.00 18.76 ?  205 VAL D N     1 
ATOM   15026 C  CA    . VAL D 2 226 ? 133.034 103.604 142.683 1.00 18.85 ?  205 VAL D CA    1 
ATOM   15027 C  C     . VAL D 2 226 ? 133.160 104.099 144.124 1.00 19.19 ?  205 VAL D C     1 
ATOM   15028 O  O     . VAL D 2 226 ? 132.400 103.667 144.992 1.00 19.87 ?  205 VAL D O     1 
ATOM   15029 C  CB    . VAL D 2 226 ? 133.954 102.407 142.411 1.00 19.28 ?  205 VAL D CB    1 
ATOM   15030 C  CG1   . VAL D 2 226 ? 133.719 101.279 143.451 1.00 18.22 ?  205 VAL D CG1   1 
ATOM   15031 C  CG2   . VAL D 2 226 ? 133.705 101.901 140.981 1.00 18.40 ?  205 VAL D CG2   1 
ATOM   15032 N  N     . GLY D 2 227 ? 134.095 105.022 144.358 1.00 18.53 ?  206 GLY D N     1 
ATOM   15033 C  CA    . GLY D 2 227 ? 134.239 105.675 145.673 1.00 18.74 ?  206 GLY D CA    1 
ATOM   15034 C  C     . GLY D 2 227 ? 132.980 106.368 146.165 1.00 19.17 ?  206 GLY D C     1 
ATOM   15035 O  O     . GLY D 2 227 ? 132.638 106.293 147.354 1.00 18.66 ?  206 GLY D O     1 
ATOM   15036 N  N     . LEU D 2 228 ? 132.296 107.062 145.258 1.00 19.00 ?  207 LEU D N     1 
ATOM   15037 C  CA    . LEU D 2 228 ? 131.044 107.737 145.611 1.00 19.73 ?  207 LEU D CA    1 
ATOM   15038 C  C     . LEU D 2 228 ? 129.943 106.720 145.940 1.00 19.76 ?  207 LEU D C     1 
ATOM   15039 O  O     . LEU D 2 228 ? 129.182 106.917 146.886 1.00 20.07 ?  207 LEU D O     1 
ATOM   15040 C  CB    . LEU D 2 228 ? 130.614 108.702 144.504 1.00 19.36 ?  207 LEU D CB    1 
ATOM   15041 C  CG    . LEU D 2 228 ? 131.500 109.946 144.334 1.00 20.50 ?  207 LEU D CG    1 
ATOM   15042 C  CD1   . LEU D 2 228 ? 131.147 110.683 143.055 1.00 19.87 ?  207 LEU D CD1   1 
ATOM   15043 C  CD2   . LEU D 2 228 ? 131.390 110.898 145.560 1.00 22.38 ?  207 LEU D CD2   1 
ATOM   15044 N  N     . LEU D 2 229 ? 129.889 105.619 145.191 1.00 19.27 ?  208 LEU D N     1 
ATOM   15045 C  CA    . LEU D 2 229 ? 128.945 104.527 145.497 1.00 19.47 ?  208 LEU D CA    1 
ATOM   15046 C  C     . LEU D 2 229 ? 129.212 103.874 146.858 1.00 19.67 ?  208 LEU D C     1 
ATOM   15047 O  O     . LEU D 2 229 ? 128.272 103.490 147.565 1.00 19.82 ?  208 LEU D O     1 
ATOM   15048 C  CB    . LEU D 2 229 ? 128.953 103.455 144.387 1.00 19.51 ?  208 LEU D CB    1 
ATOM   15049 C  CG    . LEU D 2 229 ? 128.558 103.846 142.953 1.00 19.48 ?  208 LEU D CG    1 
ATOM   15050 C  CD1   . LEU D 2 229 ? 128.791 102.663 141.996 1.00 20.14 ?  208 LEU D CD1   1 
ATOM   15051 C  CD2   . LEU D 2 229 ? 127.109 104.369 142.844 1.00 19.95 ?  208 LEU D CD2   1 
ATOM   15052 N  N     . ALA D 2 230 ? 130.488 103.738 147.224 1.00 19.43 ?  209 ALA D N     1 
ATOM   15053 C  CA    . ALA D 2 230 ? 130.866 103.220 148.545 1.00 20.29 ?  209 ALA D CA    1 
ATOM   15054 C  C     . ALA D 2 230 ? 130.476 104.176 149.673 1.00 21.17 ?  209 ALA D C     1 
ATOM   15055 O  O     . ALA D 2 230 ? 129.959 103.745 150.699 1.00 21.73 ?  209 ALA D O     1 
ATOM   15056 C  CB    . ALA D 2 230 ? 132.360 102.911 148.594 1.00 19.99 ?  209 ALA D CB    1 
ATOM   15057 N  N     . GLN D 2 231 ? 130.719 105.473 149.481 1.00 22.26 ?  210 GLN D N     1 
ATOM   15058 C  CA    . GLN D 2 231 ? 130.331 106.493 150.474 1.00 23.33 ?  210 GLN D CA    1 
ATOM   15059 C  C     . GLN D 2 231 ? 128.818 106.516 150.713 1.00 23.85 ?  210 GLN D C     1 
ATOM   15060 O  O     . GLN D 2 231 ? 128.371 106.717 151.839 1.00 24.91 ?  210 GLN D O     1 
ATOM   15061 C  CB    . GLN D 2 231 ? 130.798 107.889 150.048 1.00 23.49 ?  210 GLN D CB    1 
ATOM   15062 C  CG    . GLN D 2 231 ? 132.317 108.090 150.012 1.00 23.05 ?  210 GLN D CG    1 
ATOM   15063 C  CD    . GLN D 2 231 ? 132.693 109.497 149.553 1.00 24.65 ?  210 GLN D CD    1 
ATOM   15064 O  OE1   . GLN D 2 231 ? 132.187 110.483 150.089 1.00 25.85 ?  210 GLN D OE1   1 
ATOM   15065 N  NE2   . GLN D 2 231 ? 133.569 109.595 148.551 1.00 22.30 ?  210 GLN D NE2   1 
ATOM   15066 N  N     . GLU D 2 232 ? 128.038 106.331 149.652 1.00 24.36 ?  211 GLU D N     1 
ATOM   15067 C  CA    . GLU D 2 232 ? 126.587 106.205 149.773 1.00 24.83 ?  211 GLU D CA    1 
ATOM   15068 C  C     . GLU D 2 232 ? 126.188 105.085 150.740 1.00 24.34 ?  211 GLU D C     1 
ATOM   15069 O  O     . GLU D 2 232 ? 125.322 105.286 151.593 1.00 24.20 ?  211 GLU D O     1 
ATOM   15070 C  CB    . GLU D 2 232 ? 125.952 105.965 148.408 1.00 25.15 ?  211 GLU D CB    1 
ATOM   15071 C  CG    . GLU D 2 232 ? 124.451 106.085 148.402 1.00 28.55 ?  211 GLU D CG    1 
ATOM   15072 C  CD    . GLU D 2 232 ? 123.889 105.862 147.025 1.00 33.83 ?  211 GLU D CD    1 
ATOM   15073 O  OE1   . GLU D 2 232 ? 123.723 106.861 146.295 1.00 35.09 ?  211 GLU D OE1   1 
ATOM   15074 O  OE2   . GLU D 2 232 ? 123.657 104.689 146.657 1.00 35.51 -1 211 GLU D OE2   1 
ATOM   15075 N  N     . ILE D 2 233 ? 126.820 103.918 150.614 1.00 23.39 ?  212 ILE D N     1 
ATOM   15076 C  CA    . ILE D 2 233 ? 126.565 102.804 151.544 1.00 23.42 ?  212 ILE D CA    1 
ATOM   15077 C  C     . ILE D 2 233 ? 127.047 103.148 152.954 1.00 23.74 ?  212 ILE D C     1 
ATOM   15078 O  O     . ILE D 2 233 ? 126.312 102.986 153.927 1.00 24.61 ?  212 ILE D O     1 
ATOM   15079 C  CB    . ILE D 2 233 ? 127.189 101.469 151.054 1.00 22.81 ?  212 ILE D CB    1 
ATOM   15080 C  CG1   . ILE D 2 233 ? 126.503 100.999 149.763 1.00 22.94 ?  212 ILE D CG1   1 
ATOM   15081 C  CG2   . ILE D 2 233 ? 127.070 100.381 152.129 1.00 22.45 ?  212 ILE D CG2   1 
ATOM   15082 C  CD1   . ILE D 2 233 ? 127.270 99.889  149.012 1.00 22.21 ?  212 ILE D CD1   1 
ATOM   15083 N  N     . TYR D 2 234 ? 128.278 103.642 153.055 1.00 24.19 ?  213 TYR D N     1 
ATOM   15084 C  CA    . TYR D 2 234 ? 128.878 104.028 154.324 1.00 24.59 ?  213 TYR D CA    1 
ATOM   15085 C  C     . TYR D 2 234 ? 127.978 104.989 155.108 1.00 25.15 ?  213 TYR D C     1 
ATOM   15086 O  O     . TYR D 2 234 ? 127.815 104.833 156.321 1.00 24.94 ?  213 TYR D O     1 
ATOM   15087 C  CB    . TYR D 2 234 ? 130.243 104.673 154.074 1.00 24.41 ?  213 TYR D CB    1 
ATOM   15088 C  CG    . TYR D 2 234 ? 130.974 105.138 155.316 1.00 25.93 ?  213 TYR D CG    1 
ATOM   15089 C  CD1   . TYR D 2 234 ? 131.768 104.261 156.046 1.00 24.70 ?  213 TYR D CD1   1 
ATOM   15090 C  CD2   . TYR D 2 234 ? 130.876 106.466 155.755 1.00 26.11 ?  213 TYR D CD2   1 
ATOM   15091 C  CE1   . TYR D 2 234 ? 132.448 104.684 157.185 1.00 27.90 ?  213 TYR D CE1   1 
ATOM   15092 C  CE2   . TYR D 2 234 ? 131.556 106.896 156.886 1.00 27.70 ?  213 TYR D CE2   1 
ATOM   15093 C  CZ    . TYR D 2 234 ? 132.341 106.003 157.594 1.00 27.89 ?  213 TYR D CZ    1 
ATOM   15094 O  OH    . TYR D 2 234 ? 133.013 106.423 158.718 1.00 32.34 ?  213 TYR D OH    1 
ATOM   15095 N  N     . ASN D 2 235 ? 127.411 105.973 154.409 1.00 25.43 ?  214 ASN D N     1 
ATOM   15096 C  CA    . ASN D 2 235 ? 126.573 107.008 155.038 1.00 26.77 ?  214 ASN D CA    1 
ATOM   15097 C  C     . ASN D 2 235 ? 125.210 106.505 155.513 1.00 27.06 ?  214 ASN D C     1 
ATOM   15098 O  O     . ASN D 2 235 ? 124.511 107.197 156.247 1.00 27.42 ?  214 ASN D O     1 
ATOM   15099 C  CB    . ASN D 2 235 ? 126.361 108.196 154.097 1.00 26.80 ?  214 ASN D CB    1 
ATOM   15100 C  CG    . ASN D 2 235 ? 127.641 108.915 153.766 1.00 28.19 ?  214 ASN D CG    1 
ATOM   15101 O  OD1   . ASN D 2 235 ? 128.548 109.018 154.590 1.00 29.35 ?  214 ASN D OD1   1 
ATOM   15102 N  ND2   . ASN D 2 235 ? 127.719 109.431 152.550 1.00 30.84 ?  214 ASN D ND2   1 
ATOM   15103 N  N     . LYS D 2 236 ? 124.838 105.308 155.087 1.00 26.87 ?  215 LYS D N     1 
ATOM   15104 C  CA    . LYS D 2 236 ? 123.586 104.704 155.523 1.00 27.86 ?  215 LYS D CA    1 
ATOM   15105 C  C     . LYS D 2 236 ? 123.767 103.903 156.820 1.00 28.07 ?  215 LYS D C     1 
ATOM   15106 O  O     . LYS D 2 236 ? 122.803 103.364 157.362 1.00 28.22 ?  215 LYS D O     1 
ATOM   15107 C  CB    . LYS D 2 236 ? 123.008 103.815 154.420 1.00 27.52 ?  215 LYS D CB    1 
ATOM   15108 C  CG    . LYS D 2 236 ? 122.602 104.560 153.173 1.00 29.60 ?  215 LYS D CG    1 
ATOM   15109 C  CD    . LYS D 2 236 ? 121.521 103.822 152.401 1.00 34.24 ?  215 LYS D CD    1 
ATOM   15110 C  CE    . LYS D 2 236 ? 122.055 103.026 151.227 1.00 36.75 ?  215 LYS D CE    1 
ATOM   15111 N  NZ    . LYS D 2 236 ? 122.923 101.912 151.668 1.00 40.41 1  215 LYS D NZ    1 
ATOM   15112 N  N     . GLN D 2 237 ? 125.000 103.837 157.316 1.00 28.33 ?  216 GLN D N     1 
ATOM   15113 C  CA    . GLN D 2 237 ? 125.323 102.991 158.466 1.00 29.60 ?  216 GLN D CA    1 
ATOM   15114 C  C     . GLN D 2 237 ? 125.295 103.754 159.786 1.00 30.69 ?  216 GLN D C     1 
ATOM   15115 O  O     . GLN D 2 237 ? 125.418 104.983 159.805 1.00 30.85 ?  216 GLN D O     1 
ATOM   15116 C  CB    . GLN D 2 237 ? 126.702 102.320 158.292 1.00 29.08 ?  216 GLN D CB    1 
ATOM   15117 C  CG    . GLN D 2 237 ? 126.907 101.555 156.981 1.00 27.78 ?  216 GLN D CG    1 
ATOM   15118 C  CD    . GLN D 2 237 ? 125.780 100.586 156.664 1.00 28.38 ?  216 GLN D CD    1 
ATOM   15119 O  OE1   . GLN D 2 237 ? 125.394 99.769  157.499 1.00 29.30 ?  216 GLN D OE1   1 
ATOM   15120 N  NE2   . GLN D 2 237 ? 125.254 100.666 155.446 1.00 26.88 ?  216 GLN D NE2   1 
ATOM   15121 N  N     . THR D 2 238 ? 125.146 103.012 160.882 1.00 32.02 ?  217 THR D N     1 
ATOM   15122 C  CA    . THR D 2 238 ? 125.267 103.573 162.231 1.00 33.47 ?  217 THR D CA    1 
ATOM   15123 C  C     . THR D 2 238 ? 126.698 104.046 162.505 1.00 34.29 ?  217 THR D C     1 
ATOM   15124 O  O     . THR D 2 238 ? 127.627 103.758 161.732 1.00 33.78 ?  217 THR D O     1 
ATOM   15125 C  CB    . THR D 2 238 ? 124.862 102.536 163.316 1.00 34.00 ?  217 THR D CB    1 
ATOM   15126 O  OG1   . THR D 2 238 ? 125.794 101.444 163.315 1.00 34.33 ?  217 THR D OG1   1 
ATOM   15127 C  CG2   . THR D 2 238 ? 123.444 101.998 163.062 1.00 33.53 ?  217 THR D CG2   1 
ATOM   15128 N  N     . GLU D 2 239 ? 126.887 104.758 163.612 1.00 35.45 ?  218 GLU D N     1 
ATOM   15129 C  CA    . GLU D 2 239 ? 128.215 105.239 163.977 1.00 36.37 ?  218 GLU D CA    1 
ATOM   15130 C  C     . GLU D 2 239 ? 129.178 104.103 164.318 1.00 36.29 ?  218 GLU D C     1 
ATOM   15131 O  O     . GLU D 2 239 ? 130.351 104.150 163.937 1.00 36.18 ?  218 GLU D O     1 
ATOM   15132 C  CB    . GLU D 2 239 ? 128.144 106.271 165.106 1.00 37.27 ?  218 GLU D CB    1 
ATOM   15133 C  CG    . GLU D 2 239 ? 127.516 107.609 164.674 1.00 39.45 ?  218 GLU D CG    1 
ATOM   15134 C  CD    . GLU D 2 239 ? 128.227 108.254 163.485 1.00 41.22 ?  218 GLU D CD    1 
ATOM   15135 O  OE1   . GLU D 2 239 ? 129.475 108.322 163.485 1.00 42.62 ?  218 GLU D OE1   1 
ATOM   15136 O  OE2   . GLU D 2 239 ? 127.532 108.696 162.545 1.00 41.24 -1 218 GLU D OE2   1 
ATOM   15137 N  N     . GLU D 2 240 ? 128.680 103.081 165.011 1.00 36.66 ?  219 GLU D N     1 
ATOM   15138 C  CA    . GLU D 2 240 ? 129.504 101.919 165.351 1.00 37.01 ?  219 GLU D CA    1 
ATOM   15139 C  C     . GLU D 2 240 ? 129.890 101.135 164.097 1.00 35.85 ?  219 GLU D C     1 
ATOM   15140 O  O     . GLU D 2 240 ? 131.036 100.698 163.967 1.00 35.62 ?  219 GLU D O     1 
ATOM   15141 C  CB    . GLU D 2 240 ? 128.800 100.999 166.360 1.00 37.98 ?  219 GLU D CB    1 
ATOM   15142 C  CG    . GLU D 2 240 ? 129.677 99.824  166.820 1.00 40.87 ?  219 GLU D CG    1 
ATOM   15143 C  CD    . GLU D 2 240 ? 129.000 98.883  167.814 1.00 44.58 ?  219 GLU D CD    1 
ATOM   15144 O  OE1   . GLU D 2 240 ? 129.738 98.234  168.596 1.00 45.86 ?  219 GLU D OE1   1 
ATOM   15145 O  OE2   . GLU D 2 240 ? 127.749 98.784  167.817 1.00 45.75 -1 219 GLU D OE2   1 
ATOM   15146 N  N     . LYS D 2 241 ? 128.927 100.963 163.190 1.00 34.54 ?  220 LYS D N     1 
ATOM   15147 C  CA    . LYS D 2 241 ? 129.161 100.261 161.927 1.00 33.65 ?  220 LYS D CA    1 
ATOM   15148 C  C     . LYS D 2 241 ? 130.139 101.040 161.037 1.00 32.67 ?  220 LYS D C     1 
ATOM   15149 O  O     . LYS D 2 241 ? 130.982 100.435 160.381 1.00 32.05 ?  220 LYS D O     1 
ATOM   15150 C  CB    . LYS D 2 241 ? 127.842 99.989  161.195 1.00 33.30 ?  220 LYS D CB    1 
ATOM   15151 C  CG    . LYS D 2 241 ? 127.952 99.117  159.930 1.00 34.50 ?  220 LYS D CG    1 
ATOM   15152 C  CD    . LYS D 2 241 ? 128.509 97.716  160.212 1.00 36.30 ?  220 LYS D CD    1 
ATOM   15153 C  CE    . LYS D 2 241 ? 127.512 96.852  160.975 1.00 38.44 ?  220 LYS D CE    1 
ATOM   15154 N  NZ    . LYS D 2 241 ? 128.200 95.757  161.710 1.00 39.28 1  220 LYS D NZ    1 
ATOM   15155 N  N     . LYS D 2 242 ? 130.020 102.371 161.029 1.00 31.90 ?  221 LYS D N     1 
ATOM   15156 C  CA    . LYS D 2 242 ? 130.957 103.233 160.309 1.00 31.28 ?  221 LYS D CA    1 
ATOM   15157 C  C     . LYS D 2 242 ? 132.389 103.042 160.805 1.00 31.32 ?  221 LYS D C     1 
ATOM   15158 O  O     . LYS D 2 242 ? 133.292 102.837 160.003 1.00 30.72 ?  221 LYS D O     1 
ATOM   15159 C  CB    . LYS D 2 242 ? 130.563 104.713 160.422 1.00 31.38 ?  221 LYS D CB    1 
ATOM   15160 C  CG    . LYS D 2 242 ? 129.481 105.161 159.445 1.00 30.64 ?  221 LYS D CG    1 
ATOM   15161 C  CD    . LYS D 2 242 ? 129.175 106.646 159.638 1.00 32.51 ?  221 LYS D CD    1 
ATOM   15162 C  CE    . LYS D 2 242 ? 128.125 107.119 158.657 1.00 32.66 ?  221 LYS D CE    1 
ATOM   15163 N  NZ    . LYS D 2 242 ? 127.658 108.481 158.999 1.00 35.31 1  221 LYS D NZ    1 
ATOM   15164 N  N     . ALA D 2 243 ? 132.586 103.115 162.125 1.00 31.62 ?  222 ALA D N     1 
ATOM   15165 C  CA    . ALA D 2 243 ? 133.905 102.906 162.734 1.00 31.66 ?  222 ALA D CA    1 
ATOM   15166 C  C     . ALA D 2 243 ? 134.500 101.543 162.360 1.00 31.52 ?  222 ALA D C     1 
ATOM   15167 O  O     . ALA D 2 243 ? 135.711 101.414 162.160 1.00 31.41 ?  222 ALA D O     1 
ATOM   15168 C  CB    . ALA D 2 243 ? 133.822 103.067 164.257 1.00 31.89 ?  222 ALA D CB    1 
ATOM   15169 N  N     . GLU D 2 244 ? 133.627 100.546 162.247 1.00 31.35 ?  223 GLU D N     1 
ATOM   15170 C  CA    . GLU D 2 244 ? 133.992 99.188  161.880 1.00 31.54 ?  223 GLU D CA    1 
ATOM   15171 C  C     . GLU D 2 244 ? 134.405 99.089  160.394 1.00 30.63 ?  223 GLU D C     1 
ATOM   15172 O  O     . GLU D 2 244 ? 135.363 98.386  160.041 1.00 29.47 ?  223 GLU D O     1 
ATOM   15173 C  CB    . GLU D 2 244 ? 132.797 98.297  162.176 1.00 32.45 ?  223 GLU D CB    1 
ATOM   15174 C  CG    . GLU D 2 244 ? 133.035 96.818  162.167 1.00 35.31 ?  223 GLU D CG    1 
ATOM   15175 C  CD    . GLU D 2 244 ? 131.867 96.077  162.785 1.00 38.36 ?  223 GLU D CD    1 
ATOM   15176 O  OE1   . GLU D 2 244 ? 131.662 96.201  164.011 1.00 41.93 ?  223 GLU D OE1   1 
ATOM   15177 O  OE2   . GLU D 2 244 ? 131.142 95.378  162.050 1.00 39.37 -1 223 GLU D OE2   1 
ATOM   15178 N  N     . LEU D 2 245 ? 133.679 99.802  159.539 1.00 29.62 ?  224 LEU D N     1 
ATOM   15179 C  CA    . LEU D 2 245 ? 134.016 99.893  158.120 1.00 29.44 ?  224 LEU D CA    1 
ATOM   15180 C  C     . LEU D 2 245 ? 135.303 100.683 157.875 1.00 28.99 ?  224 LEU D C     1 
ATOM   15181 O  O     . LEU D 2 245 ? 136.060 100.350 156.968 1.00 28.63 ?  224 LEU D O     1 
ATOM   15182 C  CB    . LEU D 2 245 ? 132.850 100.490 157.325 1.00 29.06 ?  224 LEU D CB    1 
ATOM   15183 C  CG    . LEU D 2 245 ? 131.583 99.634  157.222 1.00 29.27 ?  224 LEU D CG    1 
ATOM   15184 C  CD1   . LEU D 2 245 ? 130.553 100.355 156.357 1.00 30.76 ?  224 LEU D CD1   1 
ATOM   15185 C  CD2   . LEU D 2 245 ? 131.873 98.251  156.648 1.00 28.11 ?  224 LEU D CD2   1 
ATOM   15186 N  N     . ARG D 2 246 ? 135.542 101.720 158.680 1.00 29.31 ?  225 ARG D N     1 
ATOM   15187 C  CA    . ARG D 2 246 ? 136.803 102.468 158.619 1.00 29.86 ?  225 ARG D CA    1 
ATOM   15188 C  C     . ARG D 2 246 ? 137.983 101.582 158.990 1.00 29.23 ?  225 ARG D C     1 
ATOM   15189 O  O     . ARG D 2 246 ? 139.012 101.611 158.329 1.00 28.95 ?  225 ARG D O     1 
ATOM   15190 C  CB    . ARG D 2 246 ? 136.797 103.687 159.550 1.00 30.56 ?  225 ARG D CB    1 
ATOM   15191 C  CG    . ARG D 2 246 ? 136.004 104.868 159.040 1.00 33.71 ?  225 ARG D CG    1 
ATOM   15192 C  CD    . ARG D 2 246 ? 136.449 106.195 159.685 1.00 37.42 ?  225 ARG D CD    1 
ATOM   15193 N  NE    . ARG D 2 246 ? 136.399 106.180 161.152 1.00 39.17 ?  225 ARG D NE    1 
ATOM   15194 C  CZ    . ARG D 2 246 ? 135.296 106.318 161.888 1.00 40.68 ?  225 ARG D CZ    1 
ATOM   15195 N  NH1   . ARG D 2 246 ? 134.104 106.473 161.318 1.00 40.28 1  225 ARG D NH1   1 
ATOM   15196 N  NH2   . ARG D 2 246 ? 135.386 106.289 163.214 1.00 41.65 ?  225 ARG D NH2   1 
ATOM   15197 N  N     . GLU D 2 247 ? 137.830 100.811 160.060 1.00 28.89 ?  226 GLU D N     1 
ATOM   15198 C  CA    . GLU D 2 247 ? 138.866 99.874  160.481 1.00 29.27 ?  226 GLU D CA    1 
ATOM   15199 C  C     . GLU D 2 247 ? 139.145 98.846  159.385 1.00 27.84 ?  226 GLU D C     1 
ATOM   15200 O  O     . GLU D 2 247 ? 140.310 98.548  159.111 1.00 27.37 ?  226 GLU D O     1 
ATOM   15201 C  CB    . GLU D 2 247 ? 138.497 99.188  161.808 1.00 30.21 ?  226 GLU D CB    1 
ATOM   15202 C  CG    . GLU D 2 247 ? 139.481 98.094  162.268 1.00 34.46 ?  226 GLU D CG    1 
ATOM   15203 C  CD    . GLU D 2 247 ? 140.903 98.612  162.467 1.00 40.77 ?  226 GLU D CD    1 
ATOM   15204 O  OE1   . GLU D 2 247 ? 141.102 99.480  163.350 1.00 44.03 ?  226 GLU D OE1   1 
ATOM   15205 O  OE2   . GLU D 2 247 ? 141.825 98.157  161.744 1.00 42.98 -1 226 GLU D OE2   1 
ATOM   15206 N  N     . PHE D 2 248 ? 138.086 98.325  158.759 1.00 26.73 ?  227 PHE D N     1 
ATOM   15207 C  CA    . PHE D 2 248 ? 138.230 97.415  157.616 1.00 26.15 ?  227 PHE D CA    1 
ATOM   15208 C  C     . PHE D 2 248 ? 139.075 98.039  156.502 1.00 25.33 ?  227 PHE D C     1 
ATOM   15209 O  O     . PHE D 2 248 ? 140.003 97.406  156.005 1.00 24.70 ?  227 PHE D O     1 
ATOM   15210 C  CB    . PHE D 2 248 ? 136.879 96.967  157.025 1.00 26.02 ?  227 PHE D CB    1 
ATOM   15211 C  CG    . PHE D 2 248 ? 137.002 96.346  155.634 1.00 25.61 ?  227 PHE D CG    1 
ATOM   15212 C  CD1   . PHE D 2 248 ? 137.288 94.993  155.482 1.00 26.51 ?  227 PHE D CD1   1 
ATOM   15213 C  CD2   . PHE D 2 248 ? 136.869 97.132  154.485 1.00 26.21 ?  227 PHE D CD2   1 
ATOM   15214 C  CE1   . PHE D 2 248 ? 137.429 94.421  154.217 1.00 26.16 ?  227 PHE D CE1   1 
ATOM   15215 C  CE2   . PHE D 2 248 ? 137.010 96.572  153.208 1.00 26.07 ?  227 PHE D CE2   1 
ATOM   15216 C  CZ    . PHE D 2 248 ? 137.294 95.209  153.079 1.00 25.82 ?  227 PHE D CZ    1 
ATOM   15217 N  N     . ALA D 2 249 ? 138.728 99.267  156.112 1.00 24.83 ?  228 ALA D N     1 
ATOM   15218 C  CA    . ALA D 2 249 ? 139.392 99.965  155.002 1.00 24.08 ?  228 ALA D CA    1 
ATOM   15219 C  C     . ALA D 2 249 ? 140.877 100.225 155.293 1.00 23.93 ?  228 ALA D C     1 
ATOM   15220 O  O     . ALA D 2 249 ? 141.730 100.025 154.426 1.00 22.51 ?  228 ALA D O     1 
ATOM   15221 C  CB    . ALA D 2 249 ? 138.671 101.286 154.709 1.00 24.18 ?  228 ALA D CB    1 
ATOM   15222 N  N     . ILE D 2 250 ? 141.173 100.676 156.512 1.00 24.20 ?  229 ILE D N     1 
ATOM   15223 C  CA    . ILE D 2 250 ? 142.551 100.965 156.913 1.00 24.86 ?  229 ILE D CA    1 
ATOM   15224 C  C     . ILE D 2 250 ? 143.372 99.675  157.023 1.00 24.68 ?  229 ILE D C     1 
ATOM   15225 O  O     . ILE D 2 250 ? 144.515 99.630  156.585 1.00 24.30 ?  229 ILE D O     1 
ATOM   15226 C  CB    . ILE D 2 250 ? 142.618 101.806 158.236 1.00 25.44 ?  229 ILE D CB    1 
ATOM   15227 C  CG1   . ILE D 2 250 ? 141.872 103.148 158.098 1.00 26.49 ?  229 ILE D CG1   1 
ATOM   15228 C  CG2   . ILE D 2 250 ? 144.066 102.038 158.688 1.00 27.13 ?  229 ILE D CG2   1 
ATOM   15229 C  CD1   . ILE D 2 250 ? 142.290 104.021 156.912 1.00 28.58 ?  229 ILE D CD1   1 
ATOM   15230 N  N     . ASP D 2 251 ? 142.780 98.631  157.605 1.00 24.90 ?  230 ASP D N     1 
ATOM   15231 C  CA    . ASP D 2 251 ? 143.432 97.332  157.720 1.00 25.04 ?  230 ASP D CA    1 
ATOM   15232 C  C     . ASP D 2 251 ? 143.762 96.757  156.331 1.00 24.25 ?  230 ASP D C     1 
ATOM   15233 O  O     . ASP D 2 251 ? 144.879 96.291  156.095 1.00 23.60 ?  230 ASP D O     1 
ATOM   15234 C  CB    . ASP D 2 251 ? 142.538 96.371  158.512 1.00 26.23 ?  230 ASP D CB    1 
ATOM   15235 C  CG    . ASP D 2 251 ? 143.086 94.961  158.565 1.00 28.91 ?  230 ASP D CG    1 
ATOM   15236 O  OD1   . ASP D 2 251 ? 144.131 94.735  159.211 1.00 32.03 ?  230 ASP D OD1   1 
ATOM   15237 O  OD2   . ASP D 2 251 ? 142.450 94.066  157.974 1.00 33.16 -1 230 ASP D OD2   1 
ATOM   15238 N  N     . LEU D 2 252 ? 142.786 96.790  155.427 1.00 23.43 ?  231 LEU D N     1 
ATOM   15239 C  CA    . LEU D 2 252 ? 143.003 96.355  154.050 1.00 22.79 ?  231 LEU D CA    1 
ATOM   15240 C  C     . LEU D 2 252 ? 144.106 97.177  153.377 1.00 22.71 ?  231 LEU D C     1 
ATOM   15241 O  O     . LEU D 2 252 ? 144.992 96.618  152.718 1.00 21.58 ?  231 LEU D O     1 
ATOM   15242 C  CB    . LEU D 2 252 ? 141.710 96.444  153.232 1.00 22.48 ?  231 LEU D CB    1 
ATOM   15243 C  CG    . LEU D 2 252 ? 141.822 96.004  151.760 1.00 21.05 ?  231 LEU D CG    1 
ATOM   15244 C  CD1   . LEU D 2 252 ? 142.323 94.549  151.631 1.00 22.94 ?  231 LEU D CD1   1 
ATOM   15245 C  CD2   . LEU D 2 252 ? 140.489 96.158  151.042 1.00 19.31 ?  231 LEU D CD2   1 
ATOM   15246 N  N     . LEU D 2 253 ? 144.044 98.499  153.541 1.00 22.90 ?  232 LEU D N     1 
ATOM   15247 C  CA    . LEU D 2 253 ? 145.064 99.379  152.953 1.00 23.78 ?  232 LEU D CA    1 
ATOM   15248 C  C     . LEU D 2 253 ? 146.466 99.001  153.443 1.00 23.75 ?  232 LEU D C     1 
ATOM   15249 O  O     . LEU D 2 253 ? 147.402 98.911  152.647 1.00 23.26 ?  232 LEU D O     1 
ATOM   15250 C  CB    . LEU D 2 253 ? 144.789 100.850 153.278 1.00 24.03 ?  232 LEU D CB    1 
ATOM   15251 C  CG    . LEU D 2 253 ? 145.930 101.812 152.901 1.00 26.46 ?  232 LEU D CG    1 
ATOM   15252 C  CD1   . LEU D 2 253 ? 146.001 101.972 151.400 1.00 26.52 ?  232 LEU D CD1   1 
ATOM   15253 C  CD2   . LEU D 2 253 ? 145.766 103.179 153.571 1.00 27.50 ?  232 LEU D CD2   1 
ATOM   15254 N  N     . ASN D 2 254 ? 146.598 98.808  154.756 1.00 24.63 ?  233 ASN D N     1 
ATOM   15255 C  CA    . ASN D 2 254 ? 147.861 98.378  155.362 1.00 25.49 ?  233 ASN D CA    1 
ATOM   15256 C  C     . ASN D 2 254 ? 148.417 97.073  154.773 1.00 24.94 ?  233 ASN D C     1 
ATOM   15257 O  O     . ASN D 2 254 ? 149.615 96.991  154.489 1.00 24.64 ?  233 ASN D O     1 
ATOM   15258 C  CB    . ASN D 2 254 ? 147.718 98.233  156.874 1.00 26.98 ?  233 ASN D CB    1 
ATOM   15259 C  CG    . ASN D 2 254 ? 147.941 99.538  157.607 1.00 29.94 ?  233 ASN D CG    1 
ATOM   15260 O  OD1   . ASN D 2 254 ? 148.834 100.322 157.261 1.00 34.55 ?  233 ASN D OD1   1 
ATOM   15261 N  ND2   . ASN D 2 254 ? 147.139 99.775  158.636 1.00 33.81 ?  233 ASN D ND2   1 
ATOM   15262 N  N     . GLN D 2 255 ? 147.557 96.068  154.607 1.00 24.08 ?  234 GLN D N     1 
ATOM   15263 C  CA    . GLN D 2 255 ? 147.986 94.785  154.044 1.00 24.35 ?  234 GLN D CA    1 
ATOM   15264 C  C     . GLN D 2 255 ? 148.494 94.981  152.628 1.00 23.26 ?  234 GLN D C     1 
ATOM   15265 O  O     . GLN D 2 255 ? 149.573 94.487  152.285 1.00 23.12 ?  234 GLN D O     1 
ATOM   15266 C  CB    . GLN D 2 255 ? 146.853 93.752  154.018 1.00 24.84 ?  234 GLN D CB    1 
ATOM   15267 C  CG    . GLN D 2 255 ? 146.448 93.179  155.357 1.00 27.45 ?  234 GLN D CG    1 
ATOM   15268 C  CD    . GLN D 2 255 ? 147.606 92.546  156.110 1.00 32.02 ?  234 GLN D CD    1 
ATOM   15269 O  OE1   . GLN D 2 255 ? 147.948 92.989  157.204 1.00 35.80 ?  234 GLN D OE1   1 
ATOM   15270 N  NE2   . GLN D 2 255 ? 148.211 91.507  155.532 1.00 32.12 ?  234 GLN D NE2   1 
ATOM   15271 N  N     . LEU D 2 256 ? 147.717 95.704  151.820 1.00 21.77 ?  235 LEU D N     1 
ATOM   15272 C  CA    . LEU D 2 256 ? 148.079 95.958  150.423 1.00 21.68 ?  235 LEU D CA    1 
ATOM   15273 C  C     . LEU D 2 256 ? 149.341 96.809  150.331 1.00 21.49 ?  235 LEU D C     1 
ATOM   15274 O  O     . LEU D 2 256 ? 150.204 96.549  149.500 1.00 20.89 ?  235 LEU D O     1 
ATOM   15275 C  CB    . LEU D 2 256 ? 146.931 96.640  149.652 1.00 20.49 ?  235 LEU D CB    1 
ATOM   15276 C  CG    . LEU D 2 256 ? 145.671 95.799  149.404 1.00 21.52 ?  235 LEU D CG    1 
ATOM   15277 C  CD1   . LEU D 2 256 ? 144.522 96.646  148.832 1.00 20.71 ?  235 LEU D CD1   1 
ATOM   15278 C  CD2   . LEU D 2 256 ? 145.953 94.619  148.484 1.00 20.74 ?  235 LEU D CD2   1 
ATOM   15279 N  N     . TYR D 2 257 ? 149.440 97.818  151.195 1.00 21.42 ?  236 TYR D N     1 
ATOM   15280 C  CA    . TYR D 2 257 ? 150.604 98.704  151.187 1.00 22.02 ?  236 TYR D CA    1 
ATOM   15281 C  C     . TYR D 2 257 ? 151.903 97.966  151.509 1.00 22.61 ?  236 TYR D C     1 
ATOM   15282 O  O     . TYR D 2 257 ? 152.921 98.180  150.850 1.00 22.19 ?  236 TYR D O     1 
ATOM   15283 C  CB    . TYR D 2 257 ? 150.402 99.886  152.129 1.00 22.06 ?  236 TYR D CB    1 
ATOM   15284 C  CG    . TYR D 2 257 ? 151.628 100.756 152.293 1.00 23.44 ?  236 TYR D CG    1 
ATOM   15285 C  CD1   . TYR D 2 257 ? 152.120 101.517 151.225 1.00 24.01 ?  236 TYR D CD1   1 
ATOM   15286 C  CD2   . TYR D 2 257 ? 152.289 100.825 153.517 1.00 25.22 ?  236 TYR D CD2   1 
ATOM   15287 C  CE1   . TYR D 2 257 ? 153.247 102.321 151.380 1.00 25.14 ?  236 TYR D CE1   1 
ATOM   15288 C  CE2   . TYR D 2 257 ? 153.422 101.618 153.679 1.00 26.71 ?  236 TYR D CE2   1 
ATOM   15289 C  CZ    . TYR D 2 257 ? 153.890 102.363 152.611 1.00 25.35 ?  236 TYR D CZ    1 
ATOM   15290 O  OH    . TYR D 2 257 ? 154.999 103.149 152.788 1.00 26.77 ?  236 TYR D OH    1 
ATOM   15291 N  N     . GLU D 2 258 ? 151.870 97.090  152.511 1.00 23.09 ?  237 GLU D N     1 
ATOM   15292 C  CA    . GLU D 2 258 ? 153.083 96.360  152.885 1.00 23.98 ?  237 GLU D CA    1 
ATOM   15293 C  C     . GLU D 2 258 ? 153.537 95.415  151.772 1.00 23.13 ?  237 GLU D C     1 
ATOM   15294 O  O     . GLU D 2 258 ? 154.731 95.288  151.515 1.00 23.02 ?  237 GLU D O     1 
ATOM   15295 C  CB    . GLU D 2 258 ? 152.915 95.633  154.227 1.00 25.20 ?  237 GLU D CB    1 
ATOM   15296 C  CG    . GLU D 2 258 ? 152.744 96.585  155.423 1.00 28.82 ?  237 GLU D CG    1 
ATOM   15297 C  CD    . GLU D 2 258 ? 154.014 97.362  155.799 1.00 34.48 ?  237 GLU D CD    1 
ATOM   15298 O  OE1   . GLU D 2 258 ? 155.146 96.860  155.569 1.00 37.75 ?  237 GLU D OE1   1 
ATOM   15299 O  OE2   . GLU D 2 258 ? 153.881 98.486  156.343 1.00 37.16 -1 237 GLU D OE2   1 
ATOM   15300 N  N     . ASN D 2 259 ? 152.583 94.786  151.098 1.00 22.12 ?  238 ASN D N     1 
ATOM   15301 C  CA    . ASN D 2 259 ? 152.880 93.985  149.910 1.00 22.35 ?  238 ASN D CA    1 
ATOM   15302 C  C     . ASN D 2 259 ? 153.381 94.826  148.706 1.00 22.11 ?  238 ASN D C     1 
ATOM   15303 O  O     . ASN D 2 259 ? 154.255 94.377  147.961 1.00 22.24 ?  238 ASN D O     1 
ATOM   15304 C  CB    . ASN D 2 259 ? 151.665 93.133  149.522 1.00 21.69 ?  238 ASN D CB    1 
ATOM   15305 C  CG    . ASN D 2 259 ? 151.937 92.242  148.323 1.00 23.38 ?  238 ASN D CG    1 
ATOM   15306 O  OD1   . ASN D 2 259 ? 152.667 91.244  148.420 1.00 23.95 ?  238 ASN D OD1   1 
ATOM   15307 N  ND2   . ASN D 2 259 ? 151.363 92.603  147.183 1.00 21.14 ?  238 ASN D ND2   1 
ATOM   15308 N  N     . GLU D 2 260 ? 152.831 96.033  148.527 1.00 21.95 ?  239 GLU D N     1 
ATOM   15309 C  CA    . GLU D 2 260 ? 153.301 96.968  147.485 1.00 22.50 ?  239 GLU D CA    1 
ATOM   15310 C  C     . GLU D 2 260 ? 154.768 97.354  147.670 1.00 22.03 ?  239 GLU D C     1 
ATOM   15311 O  O     . GLU D 2 260 ? 155.495 97.522  146.695 1.00 22.03 ?  239 GLU D O     1 
ATOM   15312 C  CB    . GLU D 2 260 ? 152.479 98.270  147.460 1.00 22.90 ?  239 GLU D CB    1 
ATOM   15313 C  CG    . GLU D 2 260 ? 151.160 98.226  146.670 1.00 25.84 ?  239 GLU D CG    1 
ATOM   15314 C  CD    . GLU D 2 260 ? 151.292 97.620  145.277 1.00 28.59 ?  239 GLU D CD    1 
ATOM   15315 O  OE1   . GLU D 2 260 ? 151.317 96.376  145.173 1.00 28.18 ?  239 GLU D OE1   1 
ATOM   15316 O  OE2   . GLU D 2 260 ? 151.329 98.384  144.284 1.00 30.32 -1 239 GLU D OE2   1 
ATOM   15317 N  N     . LEU D 2 261 ? 155.186 97.529  148.919 1.00 21.50 ?  240 LEU D N     1 
ATOM   15318 C  CA    . LEU D 2 261 ? 156.576 97.870  149.202 1.00 22.03 ?  240 LEU D CA    1 
ATOM   15319 C  C     . LEU D 2 261 ? 157.487 96.745  148.744 1.00 21.52 ?  240 LEU D C     1 
ATOM   15320 O  O     . LEU D 2 261 ? 158.517 97.000  148.118 1.00 21.44 ?  240 LEU D O     1 
ATOM   15321 C  CB    . LEU D 2 261 ? 156.798 98.164  150.683 1.00 21.57 ?  240 LEU D CB    1 
ATOM   15322 C  CG    . LEU D 2 261 ? 156.031 99.331  151.306 1.00 23.22 ?  240 LEU D CG    1 
ATOM   15323 C  CD1   . LEU D 2 261 ? 156.375 99.419  152.781 1.00 23.06 ?  240 LEU D CD1   1 
ATOM   15324 C  CD2   . LEU D 2 261 ? 156.349 100.647 150.595 1.00 23.52 ?  240 LEU D CD2   1 
ATOM   15325 N  N     . GLU D 2 262 ? 157.091 95.506  149.037 1.00 21.69 ?  241 GLU D N     1 
ATOM   15326 C  CA    . GLU D 2 262 ? 157.855 94.329  148.593 1.00 22.31 ?  241 GLU D CA    1 
ATOM   15327 C  C     . GLU D 2 262 ? 157.821 94.170  147.072 1.00 21.69 ?  241 GLU D C     1 
ATOM   15328 O  O     . GLU D 2 262 ? 158.843 93.881  146.445 1.00 21.75 ?  241 GLU D O     1 
ATOM   15329 C  CB    . GLU D 2 262 ? 157.330 93.049  149.253 1.00 22.46 ?  241 GLU D CB    1 
ATOM   15330 C  CG    . GLU D 2 262 ? 157.424 93.001  150.780 1.00 25.63 ?  241 GLU D CG    1 
ATOM   15331 C  CD    . GLU D 2 262 ? 156.968 91.651  151.317 1.00 29.83 ?  241 GLU D CD    1 
ATOM   15332 O  OE1   . GLU D 2 262 ? 155.744 91.423  151.413 1.00 33.22 ?  241 GLU D OE1   1 
ATOM   15333 O  OE2   . GLU D 2 262 ? 157.829 90.804  151.617 1.00 33.36 -1 241 GLU D OE2   1 
ATOM   15334 N  N     . TYR D 2 263 ? 156.637 94.339  146.485 1.00 21.42 ?  242 TYR D N     1 
ATOM   15335 C  CA    . TYR D 2 263 ? 156.458 94.305  145.029 1.00 21.04 ?  242 TYR D CA    1 
ATOM   15336 C  C     . TYR D 2 263 ? 157.384 95.330  144.361 1.00 21.15 ?  242 TYR D C     1 
ATOM   15337 O  O     . TYR D 2 263 ? 158.010 95.050  143.338 1.00 20.32 ?  242 TYR D O     1 
ATOM   15338 C  CB    . TYR D 2 263 ? 154.992 94.614  144.687 1.00 20.95 ?  242 TYR D CB    1 
ATOM   15339 C  CG    . TYR D 2 263 ? 154.667 94.715  143.208 1.00 21.86 ?  242 TYR D CG    1 
ATOM   15340 C  CD1   . TYR D 2 263 ? 154.466 93.567  142.440 1.00 23.53 ?  242 TYR D CD1   1 
ATOM   15341 C  CD2   . TYR D 2 263 ? 154.560 95.957  142.575 1.00 21.20 ?  242 TYR D CD2   1 
ATOM   15342 C  CE1   . TYR D 2 263 ? 154.167 93.652  141.088 1.00 23.34 ?  242 TYR D CE1   1 
ATOM   15343 C  CE2   . TYR D 2 263 ? 154.260 96.051  141.220 1.00 23.11 ?  242 TYR D CE2   1 
ATOM   15344 C  CZ    . TYR D 2 263 ? 154.071 94.893  140.484 1.00 23.27 ?  242 TYR D CZ    1 
ATOM   15345 O  OH    . TYR D 2 263 ? 153.773 94.980  139.141 1.00 27.07 ?  242 TYR D OH    1 
ATOM   15346 N  N     . THR D 2 264 ? 157.438 96.520  144.955 1.00 21.12 ?  243 THR D N     1 
ATOM   15347 C  CA    . THR D 2 264 ? 158.214 97.642  144.436 1.00 21.98 ?  243 THR D CA    1 
ATOM   15348 C  C     . THR D 2 264 ? 159.710 97.335  144.437 1.00 22.32 ?  243 THR D C     1 
ATOM   15349 O  O     . THR D 2 264 ? 160.369 97.483  143.410 1.00 21.78 ?  243 THR D O     1 
ATOM   15350 C  CB    . THR D 2 264 ? 157.902 98.938  145.216 1.00 21.68 ?  243 THR D CB    1 
ATOM   15351 O  OG1   . THR D 2 264 ? 156.542 99.308  144.974 1.00 23.29 ?  243 THR D OG1   1 
ATOM   15352 C  CG2   . THR D 2 264 ? 158.829 100.101 144.808 1.00 23.16 ?  243 THR D CG2   1 
ATOM   15353 N  N     . GLU D 2 265 ? 160.235 96.885  145.576 1.00 22.48 ?  244 GLU D N     1 
ATOM   15354 C  CA    . GLU D 2 265 ? 161.657 96.539  145.652 1.00 23.73 ?  244 GLU D CA    1 
ATOM   15355 C  C     . GLU D 2 265 ? 162.012 95.426  144.678 1.00 23.85 ?  244 GLU D C     1 
ATOM   15356 O  O     . GLU D 2 265 ? 163.050 95.487  144.032 1.00 24.40 ?  244 GLU D O     1 
ATOM   15357 C  CB    . GLU D 2 265 ? 162.052 96.149  147.068 1.00 23.19 ?  244 GLU D CB    1 
ATOM   15358 C  CG    . GLU D 2 265 ? 162.120 97.343  147.982 1.00 25.08 ?  244 GLU D CG    1 
ATOM   15359 C  CD    . GLU D 2 265 ? 162.340 96.969  149.433 1.00 27.30 ?  244 GLU D CD    1 
ATOM   15360 O  OE1   . GLU D 2 265 ? 162.645 95.795  149.720 1.00 27.77 ?  244 GLU D OE1   1 
ATOM   15361 O  OE2   . GLU D 2 265 ? 162.206 97.864  150.288 1.00 28.63 -1 244 GLU D OE2   1 
ATOM   15362 N  N     . ASP D 2 266 ? 161.124 94.438  144.558 1.00 24.13 ?  245 ASP D N     1 
ATOM   15363 C  CA    . ASP D 2 266 ? 161.317 93.291  143.666 1.00 25.22 ?  245 ASP D CA    1 
ATOM   15364 C  C     . ASP D 2 266 ? 161.506 93.708  142.191 1.00 24.84 ?  245 ASP D C     1 
ATOM   15365 O  O     . ASP D 2 266 ? 162.301 93.100  141.468 1.00 25.64 ?  245 ASP D O     1 
ATOM   15366 C  CB    . ASP D 2 266 ? 160.132 92.325  143.819 1.00 25.79 ?  245 ASP D CB    1 
ATOM   15367 C  CG    . ASP D 2 266 ? 160.307 91.031  143.035 1.00 27.71 ?  245 ASP D CG    1 
ATOM   15368 O  OD1   . ASP D 2 266 ? 161.319 90.345  143.240 1.00 31.57 ?  245 ASP D OD1   1 
ATOM   15369 O  OD2   . ASP D 2 266 ? 159.418 90.685  142.228 1.00 30.29 -1 245 ASP D OD2   1 
ATOM   15370 N  N     . LEU D 2 267 ? 160.796 94.748  141.762 1.00 24.07 ?  246 LEU D N     1 
ATOM   15371 C  CA    . LEU D 2 267 ? 160.832 95.201  140.370 1.00 23.98 ?  246 LEU D CA    1 
ATOM   15372 C  C     . LEU D 2 267 ? 161.796 96.357  140.099 1.00 22.83 ?  246 LEU D C     1 
ATOM   15373 O  O     . LEU D 2 267 ? 162.449 96.385  139.049 1.00 23.00 ?  246 LEU D O     1 
ATOM   15374 C  CB    . LEU D 2 267 ? 159.426 95.613  139.896 1.00 23.82 ?  246 LEU D CB    1 
ATOM   15375 C  CG    . LEU D 2 267 ? 158.400 94.485  139.725 1.00 26.05 ?  246 LEU D CG    1 
ATOM   15376 C  CD1   . LEU D 2 267 ? 157.174 94.988  139.014 1.00 26.74 ?  246 LEU D CD1   1 
ATOM   15377 C  CD2   . LEU D 2 267 ? 158.982 93.306  138.967 1.00 28.00 ?  246 LEU D CD2   1 
ATOM   15378 N  N     . TYR D 2 268 ? 161.873 97.300  141.039 1.00 21.68 ?  247 TYR D N     1 
ATOM   15379 C  CA    . TYR D 2 268 ? 162.546 98.579  140.799 1.00 20.95 ?  247 TYR D CA    1 
ATOM   15380 C  C     . TYR D 2 268 ? 163.956 98.744  141.380 1.00 21.43 ?  247 TYR D C     1 
ATOM   15381 O  O     . TYR D 2 268 ? 164.671 99.657  140.967 1.00 20.73 ?  247 TYR D O     1 
ATOM   15382 C  CB    . TYR D 2 268 ? 161.672 99.748  141.266 1.00 20.27 ?  247 TYR D CB    1 
ATOM   15383 C  CG    . TYR D 2 268 ? 160.444 100.002 140.410 1.00 19.54 ?  247 TYR D CG    1 
ATOM   15384 C  CD1   . TYR D 2 268 ? 159.187 99.573  140.822 1.00 18.52 ?  247 TYR D CD1   1 
ATOM   15385 C  CD2   . TYR D 2 268 ? 160.549 100.670 139.181 1.00 20.62 ?  247 TYR D CD2   1 
ATOM   15386 C  CE1   . TYR D 2 268 ? 158.032 99.816  140.033 1.00 18.33 ?  247 TYR D CE1   1 
ATOM   15387 C  CE2   . TYR D 2 268 ? 159.407 100.918 138.384 1.00 20.79 ?  247 TYR D CE2   1 
ATOM   15388 C  CZ    . TYR D 2 268 ? 158.161 100.495 138.826 1.00 20.23 ?  247 TYR D CZ    1 
ATOM   15389 O  OH    . TYR D 2 268 ? 157.054 100.742 138.038 1.00 20.50 ?  247 TYR D OH    1 
ATOM   15390 N  N     . ASP D 2 269 ? 164.358 97.899  142.335 1.00 21.65 ?  248 ASP D N     1 
ATOM   15391 C  CA    . ASP D 2 269 ? 165.743 97.963  142.815 1.00 22.30 ?  248 ASP D CA    1 
ATOM   15392 C  C     . ASP D 2 269 ? 166.778 97.815  141.675 1.00 22.54 ?  248 ASP D C     1 
ATOM   15393 O  O     . ASP D 2 269 ? 167.807 98.496  141.683 1.00 22.49 ?  248 ASP D O     1 
ATOM   15394 C  CB    . ASP D 2 269 ? 166.013 96.941  143.922 1.00 22.83 ?  248 ASP D CB    1 
ATOM   15395 C  CG    . ASP D 2 269 ? 165.536 97.416  145.291 1.00 23.55 ?  248 ASP D CG    1 
ATOM   15396 O  OD1   . ASP D 2 269 ? 165.138 98.590  145.421 1.00 24.95 ?  248 ASP D OD1   1 
ATOM   15397 O  OD2   . ASP D 2 269 ? 165.560 96.605  146.245 1.00 24.47 -1 248 ASP D OD2   1 
ATOM   15398 N  N     . GLN D 2 270 ? 166.499 96.942  140.704 1.00 22.79 ?  249 GLN D N     1 
ATOM   15399 C  CA    . GLN D 2 270 ? 167.433 96.698  139.597 1.00 23.41 ?  249 GLN D CA    1 
ATOM   15400 C  C     . GLN D 2 270 ? 167.613 97.901  138.665 1.00 22.83 ?  249 GLN D C     1 
ATOM   15401 O  O     . GLN D 2 270 ? 168.562 97.939  137.885 1.00 23.75 ?  249 GLN D O     1 
ATOM   15402 C  CB    . GLN D 2 270 ? 167.044 95.454  138.791 1.00 24.02 ?  249 GLN D CB    1 
ATOM   15403 C  CG    . GLN D 2 270 ? 165.761 95.600  137.953 1.00 25.40 ?  249 GLN D CG    1 
ATOM   15404 C  CD    . GLN D 2 270 ? 165.252 94.268  137.429 1.00 29.23 ?  249 GLN D CD    1 
ATOM   15405 O  OE1   . GLN D 2 270 ? 165.428 93.230  138.068 1.00 31.31 ?  249 GLN D OE1   1 
ATOM   15406 N  NE2   . GLN D 2 270 ? 164.603 94.292  136.267 1.00 30.04 ?  249 GLN D NE2   1 
ATOM   15407 N  N     . VAL D 2 271 ? 166.696 98.866  138.736 1.00 21.93 ?  250 VAL D N     1 
ATOM   15408 C  CA    . VAL D 2 271 ? 166.829 100.110 137.970 1.00 21.29 ?  250 VAL D CA    1 
ATOM   15409 C  C     . VAL D 2 271 ? 166.938 101.348 138.880 1.00 21.16 ?  250 VAL D C     1 
ATOM   15410 O  O     . VAL D 2 271 ? 166.838 102.485 138.409 1.00 21.54 ?  250 VAL D O     1 
ATOM   15411 C  CB    . VAL D 2 271 ? 165.682 100.260 136.918 1.00 21.62 ?  250 VAL D CB    1 
ATOM   15412 C  CG1   . VAL D 2 271 ? 165.775 99.155  135.868 1.00 21.36 ?  250 VAL D CG1   1 
ATOM   15413 C  CG2   . VAL D 2 271 ? 164.298 100.259 137.593 1.00 21.17 ?  250 VAL D CG2   1 
ATOM   15414 N  N     . GLY D 2 272 ? 167.119 101.116 140.186 1.00 20.92 ?  251 GLY D N     1 
ATOM   15415 C  CA    . GLY D 2 272 ? 167.425 102.176 141.166 1.00 20.61 ?  251 GLY D CA    1 
ATOM   15416 C  C     . GLY D 2 272 ? 166.334 103.192 141.494 1.00 20.77 ?  251 GLY D C     1 
ATOM   15417 O  O     . GLY D 2 272 ? 166.632 104.321 141.914 1.00 20.28 ?  251 GLY D O     1 
ATOM   15418 N  N     . LEU D 2 273 ? 165.074 102.798 141.331 1.00 19.85 ?  252 LEU D N     1 
ATOM   15419 C  CA    . LEU D 2 273 ? 163.976 103.761 141.435 1.00 20.09 ?  252 LEU D CA    1 
ATOM   15420 C  C     . LEU D 2 273 ? 163.048 103.606 142.643 1.00 19.88 ?  252 LEU D C     1 
ATOM   15421 O  O     . LEU D 2 273 ? 162.167 104.437 142.837 1.00 20.04 ?  252 LEU D O     1 
ATOM   15422 C  CB    . LEU D 2 273 ? 163.128 103.709 140.153 1.00 19.97 ?  252 LEU D CB    1 
ATOM   15423 C  CG    . LEU D 2 273 ? 163.840 104.008 138.842 1.00 20.26 ?  252 LEU D CG    1 
ATOM   15424 C  CD1   . LEU D 2 273 ? 162.806 104.009 137.739 1.00 18.98 ?  252 LEU D CD1   1 
ATOM   15425 C  CD2   . LEU D 2 273 ? 164.603 105.362 138.888 1.00 21.03 ?  252 LEU D CD2   1 
ATOM   15426 N  N     . SER D 2 274 ? 163.261 102.562 143.445 0.50 19.54 ?  253 SER D N     1 
ATOM   15427 C  CA    . SER D 2 274 ? 162.292 102.148 144.472 0.50 19.34 ?  253 SER D CA    1 
ATOM   15428 C  C     . SER D 2 274 ? 161.886 103.243 145.466 0.50 20.05 ?  253 SER D C     1 
ATOM   15429 O  O     . SER D 2 274 ? 160.709 103.358 145.807 0.50 20.31 ?  253 SER D O     1 
ATOM   15430 C  CB    . SER D 2 274 ? 162.775 100.897 145.217 0.50 18.97 ?  253 SER D CB    1 
ATOM   15431 O  OG    . SER D 2 274 ? 163.045 99.835  144.320 0.50 15.35 ?  253 SER D OG    1 
ATOM   15432 N  N     . HIS D 2 275 ? 162.855 104.029 145.933 1.00 20.77 ?  254 HIS D N     1 
ATOM   15433 C  CA    . HIS D 2 275 ? 162.574 105.149 146.855 1.00 21.18 ?  254 HIS D CA    1 
ATOM   15434 C  C     . HIS D 2 275 ? 161.486 106.091 146.310 1.00 21.50 ?  254 HIS D C     1 
ATOM   15435 O  O     . HIS D 2 275 ? 160.512 106.407 147.013 1.00 19.88 ?  254 HIS D O     1 
ATOM   15436 C  CB    . HIS D 2 275 ? 163.848 105.941 147.191 1.00 21.60 ?  254 HIS D CB    1 
ATOM   15437 C  CG    . HIS D 2 275 ? 163.591 107.163 148.020 1.00 22.43 ?  254 HIS D CG    1 
ATOM   15438 N  ND1   . HIS D 2 275 ? 163.568 107.140 149.400 1.00 22.77 ?  254 HIS D ND1   1 
ATOM   15439 C  CD2   . HIS D 2 275 ? 163.328 108.444 147.659 1.00 22.50 ?  254 HIS D CD2   1 
ATOM   15440 C  CE1   . HIS D 2 275 ? 163.308 108.355 149.852 1.00 24.05 ?  254 HIS D CE1   1 
ATOM   15441 N  NE2   . HIS D 2 275 ? 163.151 109.163 148.816 1.00 23.22 ?  254 HIS D NE2   1 
ATOM   15442 N  N     . ASP D 2 276 ? 161.654 106.518 145.057 1.00 22.34 ?  255 ASP D N     1 
ATOM   15443 C  CA    . ASP D 2 276 ? 160.700 107.427 144.426 1.00 23.19 ?  255 ASP D CA    1 
ATOM   15444 C  C     . ASP D 2 276 ? 159.367 106.758 144.123 1.00 22.17 ?  255 ASP D C     1 
ATOM   15445 O  O     . ASP D 2 276 ? 158.331 107.403 144.204 1.00 21.87 ?  255 ASP D O     1 
ATOM   15446 C  CB    . ASP D 2 276 ? 161.272 108.040 143.137 1.00 24.33 ?  255 ASP D CB    1 
ATOM   15447 C  CG    . ASP D 2 276 ? 162.079 109.317 143.386 1.00 27.58 ?  255 ASP D CG    1 
ATOM   15448 O  OD1   . ASP D 2 276 ? 161.857 110.003 144.409 1.00 31.10 ?  255 ASP D OD1   1 
ATOM   15449 O  OD2   . ASP D 2 276 ? 162.948 109.631 142.541 1.00 29.88 -1 255 ASP D OD2   1 
ATOM   15450 N  N     . VAL D 2 277 ? 159.397 105.482 143.738 1.00 21.21 ?  256 VAL D N     1 
ATOM   15451 C  CA    . VAL D 2 277 ? 158.156 104.737 143.502 1.00 20.51 ?  256 VAL D CA    1 
ATOM   15452 C  C     . VAL D 2 277 ? 157.319 104.633 144.782 1.00 20.32 ?  256 VAL D C     1 
ATOM   15453 O  O     . VAL D 2 277 ? 156.101 104.781 144.738 1.00 19.81 ?  256 VAL D O     1 
ATOM   15454 C  CB    . VAL D 2 277 ? 158.413 103.323 142.907 1.00 20.30 ?  256 VAL D CB    1 
ATOM   15455 C  CG1   . VAL D 2 277 ? 157.106 102.564 142.749 1.00 21.16 ?  256 VAL D CG1   1 
ATOM   15456 C  CG2   . VAL D 2 277 ? 159.112 103.431 141.564 1.00 19.06 ?  256 VAL D CG2   1 
ATOM   15457 N  N     . LYS D 2 278 ? 157.987 104.400 145.912 1.00 19.84 ?  257 LYS D N     1 
ATOM   15458 C  CA    . LYS D 2 278 ? 157.316 104.334 147.210 1.00 20.27 ?  257 LYS D CA    1 
ATOM   15459 C  C     . LYS D 2 278 ? 156.578 105.632 147.559 1.00 20.16 ?  257 LYS D C     1 
ATOM   15460 O  O     . LYS D 2 278 ? 155.456 105.576 148.056 1.00 19.88 ?  257 LYS D O     1 
ATOM   15461 C  CB    . LYS D 2 278 ? 158.290 103.928 148.320 1.00 20.20 ?  257 LYS D CB    1 
ATOM   15462 C  CG    . LYS D 2 278 ? 158.680 102.455 148.267 1.00 21.60 ?  257 LYS D CG    1 
ATOM   15463 C  CD    . LYS D 2 278 ? 159.846 102.143 149.197 1.00 21.53 ?  257 LYS D CD    1 
ATOM   15464 C  CE    . LYS D 2 278 ? 160.303 100.720 148.986 1.00 24.52 ?  257 LYS D CE    1 
ATOM   15465 N  NZ    . LYS D 2 278 ? 161.427 100.379 149.919 1.00 26.32 1  257 LYS D NZ    1 
ATOM   15466 N  N     . LYS D 2 279 ? 157.193 106.785 147.273 1.00 19.67 ?  258 LYS D N     1 
ATOM   15467 C  CA    . LYS D 2 279 ? 156.517 108.077 147.466 1.00 20.10 ?  258 LYS D CA    1 
ATOM   15468 C  C     . LYS D 2 279 ? 155.241 108.166 146.620 1.00 19.12 ?  258 LYS D C     1 
ATOM   15469 O  O     . LYS D 2 279 ? 154.218 108.664 147.093 1.00 18.59 ?  258 LYS D O     1 
ATOM   15470 C  CB    . LYS D 2 279 ? 157.446 109.266 147.151 1.00 20.54 ?  258 LYS D CB    1 
ATOM   15471 C  CG    . LYS D 2 279 ? 158.694 109.358 148.027 1.00 22.84 ?  258 LYS D CG    1 
ATOM   15472 C  CD    . LYS D 2 279 ? 159.266 110.793 148.089 1.00 24.16 ?  258 LYS D CD    1 
ATOM   15473 C  CE    . LYS D 2 279 ? 159.813 111.268 146.746 1.00 25.61 ?  258 LYS D CE    1 
ATOM   15474 N  NZ    . LYS D 2 279 ? 160.377 112.673 146.818 1.00 24.70 1  258 LYS D NZ    1 
ATOM   15475 N  N     . PHE D 2 280 ? 155.316 107.661 145.385 1.00 19.04 ?  259 PHE D N     1 
ATOM   15476 C  CA    . PHE D 2 280 ? 154.188 107.665 144.433 1.00 19.31 ?  259 PHE D CA    1 
ATOM   15477 C  C     . PHE D 2 280 ? 153.039 106.747 144.864 1.00 19.25 ?  259 PHE D C     1 
ATOM   15478 O  O     . PHE D 2 280 ? 151.861 107.087 144.698 1.00 19.71 ?  259 PHE D O     1 
ATOM   15479 C  CB    . PHE D 2 280 ? 154.682 107.255 143.046 1.00 19.04 ?  259 PHE D CB    1 
ATOM   15480 C  CG    . PHE D 2 280 ? 153.731 107.590 141.912 1.00 20.15 ?  259 PHE D CG    1 
ATOM   15481 C  CD1   . PHE D 2 280 ? 153.289 108.888 141.709 1.00 21.63 ?  259 PHE D CD1   1 
ATOM   15482 C  CD2   . PHE D 2 280 ? 153.329 106.596 141.018 1.00 19.95 ?  259 PHE D CD2   1 
ATOM   15483 C  CE1   . PHE D 2 280 ? 152.436 109.198 140.627 1.00 22.56 ?  259 PHE D CE1   1 
ATOM   15484 C  CE2   . PHE D 2 280 ? 152.488 106.884 139.944 1.00 20.29 ?  259 PHE D CE2   1 
ATOM   15485 C  CZ    . PHE D 2 280 ? 152.037 108.190 139.749 1.00 21.30 ?  259 PHE D CZ    1 
ATOM   15486 N  N     . ILE D 2 281 ? 153.378 105.580 145.403 1.00 19.36 ?  260 ILE D N     1 
ATOM   15487 C  CA    . ILE D 2 281 ? 152.385 104.686 146.005 1.00 19.45 ?  260 ILE D CA    1 
ATOM   15488 C  C     . ILE D 2 281 ? 151.603 105.361 147.151 1.00 19.61 ?  260 ILE D C     1 
ATOM   15489 O  O     . ILE D 2 281 ? 150.372 105.287 147.181 1.00 19.72 ?  260 ILE D O     1 
ATOM   15490 C  CB    . ILE D 2 281 ? 153.066 103.376 146.480 1.00 19.49 ?  260 ILE D CB    1 
ATOM   15491 C  CG1   . ILE D 2 281 ? 153.590 102.599 145.268 1.00 20.10 ?  260 ILE D CG1   1 
ATOM   15492 C  CG2   . ILE D 2 281 ? 152.139 102.516 147.367 1.00 20.53 ?  260 ILE D CG2   1 
ATOM   15493 C  CD1   . ILE D 2 281 ? 154.561 101.483 145.665 1.00 21.17 ?  260 ILE D CD1   1 
ATOM   15494 N  N     . ARG D 2 282 ? 152.309 106.020 148.073 1.00 19.75 ?  261 ARG D N     1 
ATOM   15495 C  CA    . ARG D 2 282 ? 151.663 106.655 149.238 1.00 20.34 ?  261 ARG D CA    1 
ATOM   15496 C  C     . ARG D 2 282 ? 150.762 107.814 148.828 1.00 21.18 ?  261 ARG D C     1 
ATOM   15497 O  O     . ARG D 2 282 ? 149.660 107.991 149.366 1.00 21.68 ?  261 ARG D O     1 
ATOM   15498 C  CB    . ARG D 2 282 ? 152.701 107.117 150.270 1.00 20.20 ?  261 ARG D CB    1 
ATOM   15499 C  CG    . ARG D 2 282 ? 153.376 105.979 151.014 1.00 20.57 ?  261 ARG D CG    1 
ATOM   15500 C  CD    . ARG D 2 282 ? 154.270 106.504 152.140 1.00 23.15 ?  261 ARG D CD    1 
ATOM   15501 N  NE    . ARG D 2 282 ? 155.515 107.112 151.665 1.00 23.46 ?  261 ARG D NE    1 
ATOM   15502 C  CZ    . ARG D 2 282 ? 156.650 106.447 151.451 1.00 22.84 ?  261 ARG D CZ    1 
ATOM   15503 N  NH1   . ARG D 2 282 ? 156.709 105.134 151.630 1.00 23.37 1  261 ARG D NH1   1 
ATOM   15504 N  NH2   . ARG D 2 282 ? 157.729 107.101 151.043 1.00 22.27 ?  261 ARG D NH2   1 
ATOM   15505 N  N     . TYR D 2 283 ? 151.253 108.610 147.884 1.00 21.46 ?  262 TYR D N     1 
ATOM   15506 C  CA    . TYR D 2 283 ? 150.492 109.723 147.320 1.00 22.97 ?  262 TYR D CA    1 
ATOM   15507 C  C     . TYR D 2 283 ? 149.178 109.212 146.688 1.00 22.12 ?  262 TYR D C     1 
ATOM   15508 O  O     . TYR D 2 283 ? 148.112 109.800 146.886 1.00 22.00 ?  262 TYR D O     1 
ATOM   15509 C  CB    . TYR D 2 283 ? 151.385 110.463 146.317 1.00 23.37 ?  262 TYR D CB    1 
ATOM   15510 C  CG    . TYR D 2 283 ? 150.697 111.424 145.375 1.00 27.31 ?  262 TYR D CG    1 
ATOM   15511 C  CD1   . TYR D 2 283 ? 150.472 112.750 145.743 1.00 30.79 ?  262 TYR D CD1   1 
ATOM   15512 C  CD2   . TYR D 2 283 ? 150.313 111.016 144.098 1.00 30.31 ?  262 TYR D CD2   1 
ATOM   15513 C  CE1   . TYR D 2 283 ? 149.840 113.647 144.866 1.00 33.18 ?  262 TYR D CE1   1 
ATOM   15514 C  CE2   . TYR D 2 283 ? 149.693 111.901 143.211 1.00 33.20 ?  262 TYR D CE2   1 
ATOM   15515 C  CZ    . TYR D 2 283 ? 149.467 113.215 143.602 1.00 34.74 ?  262 TYR D CZ    1 
ATOM   15516 O  OH    . TYR D 2 283 ? 148.861 114.089 142.721 1.00 37.63 ?  262 TYR D OH    1 
ATOM   15517 N  N     . ASN D 2 284 ? 149.247 108.090 145.976 1.00 21.63 ?  263 ASN D N     1 
ATOM   15518 C  CA    . ASN D 2 284 ? 148.051 107.526 145.356 1.00 21.41 ?  263 ASN D CA    1 
ATOM   15519 C  C     . ASN D 2 284 ? 147.142 106.784 146.340 1.00 20.86 ?  263 ASN D C     1 
ATOM   15520 O  O     . ASN D 2 284 ? 145.929 106.773 146.163 1.00 20.92 ?  263 ASN D O     1 
ATOM   15521 C  CB    . ASN D 2 284 ? 148.406 106.679 144.132 1.00 21.15 ?  263 ASN D CB    1 
ATOM   15522 C  CG    . ASN D 2 284 ? 148.792 107.539 142.936 1.00 22.59 ?  263 ASN D CG    1 
ATOM   15523 O  OD1   . ASN D 2 284 ? 147.940 108.190 142.326 1.00 22.35 ?  263 ASN D OD1   1 
ATOM   15524 N  ND2   . ASN D 2 284 ? 150.080 107.558 142.605 1.00 22.93 ?  263 ASN D ND2   1 
ATOM   15525 N  N     . ALA D 2 285 ? 147.727 106.180 147.374 1.00 20.92 ?  264 ALA D N     1 
ATOM   15526 C  CA    . ALA D 2 285 ? 146.948 105.635 148.499 1.00 20.77 ?  264 ALA D CA    1 
ATOM   15527 C  C     . ALA D 2 285 ? 146.066 106.707 149.150 1.00 21.13 ?  264 ALA D C     1 
ATOM   15528 O  O     . ALA D 2 285 ? 144.891 106.457 149.446 1.00 19.92 ?  264 ALA D O     1 
ATOM   15529 C  CB    . ALA D 2 285 ? 147.871 104.985 149.541 1.00 20.68 ?  264 ALA D CB    1 
ATOM   15530 N  N     . ASN D 2 286 ? 146.639 107.897 149.361 1.00 21.38 ?  265 ASN D N     1 
ATOM   15531 C  CA    . ASN D 2 286 ? 145.898 109.042 149.896 1.00 21.94 ?  265 ASN D CA    1 
ATOM   15532 C  C     . ASN D 2 286 ? 144.737 109.469 148.979 1.00 22.13 ?  265 ASN D C     1 
ATOM   15533 O  O     . ASN D 2 286 ? 143.665 109.814 149.460 1.00 21.95 ?  265 ASN D O     1 
ATOM   15534 C  CB    . ASN D 2 286 ? 146.828 110.233 150.135 1.00 22.22 ?  265 ASN D CB    1 
ATOM   15535 C  CG    . ASN D 2 286 ? 147.640 110.118 151.422 1.00 22.80 ?  265 ASN D CG    1 
ATOM   15536 O  OD1   . ASN D 2 286 ? 147.374 109.280 152.291 1.00 22.57 ?  265 ASN D OD1   1 
ATOM   15537 N  ND2   . ASN D 2 286 ? 148.650 110.973 151.539 1.00 23.91 ?  265 ASN D ND2   1 
ATOM   15538 N  N     . LYS D 2 287 ? 144.953 109.438 147.666 1.00 22.51 ?  266 LYS D N     1 
ATOM   15539 C  CA    . LYS D 2 287 ? 143.875 109.749 146.716 1.00 22.91 ?  266 LYS D CA    1 
ATOM   15540 C  C     . LYS D 2 287 ? 142.739 108.723 146.808 1.00 22.33 ?  266 LYS D C     1 
ATOM   15541 O  O     . LYS D 2 287 ? 141.572 109.094 146.791 1.00 22.24 ?  266 LYS D O     1 
ATOM   15542 C  CB    . LYS D 2 287 ? 144.404 109.840 145.278 1.00 23.65 ?  266 LYS D CB    1 
ATOM   15543 C  CG    . LYS D 2 287 ? 145.191 111.118 144.989 1.00 26.50 ?  266 LYS D CG    1 
ATOM   15544 C  CD    . LYS D 2 287 ? 145.675 111.142 143.527 1.00 31.30 ?  266 LYS D CD    1 
ATOM   15545 C  CE    . LYS D 2 287 ? 145.996 112.564 143.101 1.00 35.08 ?  266 LYS D CE    1 
ATOM   15546 N  NZ    . LYS D 2 287 ? 146.439 112.679 141.679 1.00 37.66 1  266 LYS D NZ    1 
ATOM   15547 N  N     . ALA D 2 288 ? 143.097 107.443 146.920 1.00 21.41 ?  267 ALA D N     1 
ATOM   15548 C  CA    . ALA D 2 288 ? 142.136 106.349 147.067 1.00 21.53 ?  267 ALA D CA    1 
ATOM   15549 C  C     . ALA D 2 288 ? 141.286 106.509 148.340 1.00 21.77 ?  267 ALA D C     1 
ATOM   15550 O  O     . ALA D 2 288 ? 140.054 106.345 148.317 1.00 21.59 ?  267 ALA D O     1 
ATOM   15551 C  CB    . ALA D 2 288 ? 142.861 104.996 147.058 1.00 21.33 ?  267 ALA D CB    1 
ATOM   15552 N  N     . LEU D 2 289 ? 141.942 106.852 149.441 1.00 21.71 ?  268 LEU D N     1 
ATOM   15553 C  CA    . LEU D 2 289 ? 141.231 107.137 150.681 1.00 22.36 ?  268 LEU D CA    1 
ATOM   15554 C  C     . LEU D 2 289 ? 140.290 108.323 150.514 1.00 23.01 ?  268 LEU D C     1 
ATOM   15555 O  O     . LEU D 2 289 ? 139.128 108.261 150.924 1.00 23.14 ?  268 LEU D O     1 
ATOM   15556 C  CB    . LEU D 2 289 ? 142.210 107.357 151.841 1.00 22.61 ?  268 LEU D CB    1 
ATOM   15557 C  CG    . LEU D 2 289 ? 142.961 106.097 152.322 1.00 21.22 ?  268 LEU D CG    1 
ATOM   15558 C  CD1   . LEU D 2 289 ? 144.117 106.471 153.238 1.00 20.77 ?  268 LEU D CD1   1 
ATOM   15559 C  CD2   . LEU D 2 289 ? 142.018 105.092 153.020 1.00 21.40 ?  268 LEU D CD2   1 
ATOM   15560 N  N     . MET D 2 290 ? 140.767 109.395 149.890 1.00 23.87 ?  269 MET D N     1 
ATOM   15561 C  CA    . MET D 2 290 ? 139.894 110.545 149.672 1.00 25.26 ?  269 MET D CA    1 
ATOM   15562 C  C     . MET D 2 290 ? 138.686 110.189 148.787 1.00 24.37 ?  269 MET D C     1 
ATOM   15563 O  O     . MET D 2 290 ? 137.583 110.652 149.060 1.00 23.97 ?  269 MET D O     1 
ATOM   15564 C  CB    . MET D 2 290 ? 140.681 111.760 149.191 1.00 25.94 ?  269 MET D CB    1 
ATOM   15565 C  CG    . MET D 2 290 ? 141.396 112.456 150.366 1.00 31.08 ?  269 MET D CG    1 
ATOM   15566 S  SD    . MET D 2 290 ? 142.384 113.894 149.895 1.00 41.28 ?  269 MET D SD    1 
ATOM   15567 C  CE    . MET D 2 290 ? 141.178 114.872 148.963 1.00 38.56 ?  269 MET D CE    1 
ATOM   15568 N  N     . ASN D 2 291 ? 138.884 109.334 147.779 1.00 23.66 ?  270 ASN D N     1 
ATOM   15569 C  CA    . ASN D 2 291 ? 137.755 108.798 146.982 1.00 23.17 ?  270 ASN D CA    1 
ATOM   15570 C  C     . ASN D 2 291 ? 136.679 108.089 147.811 1.00 23.22 ?  270 ASN D C     1 
ATOM   15571 O  O     . ASN D 2 291 ? 135.505 108.090 147.442 1.00 22.68 ?  270 ASN D O     1 
ATOM   15572 C  CB    . ASN D 2 291 ? 138.241 107.850 145.874 1.00 22.41 ?  270 ASN D CB    1 
ATOM   15573 C  CG    . ASN D 2 291 ? 138.989 108.572 144.777 1.00 21.93 ?  270 ASN D CG    1 
ATOM   15574 O  OD1   . ASN D 2 291 ? 138.950 109.803 144.686 1.00 20.94 ?  270 ASN D OD1   1 
ATOM   15575 N  ND2   . ASN D 2 291 ? 139.678 107.810 143.932 1.00 19.20 ?  270 ASN D ND2   1 
ATOM   15576 N  N     . LEU D 2 292 ? 137.100 107.488 148.922 1.00 23.53 ?  271 LEU D N     1 
ATOM   15577 C  CA    . LEU D 2 292 ? 136.198 106.786 149.838 1.00 24.21 ?  271 LEU D CA    1 
ATOM   15578 C  C     . LEU D 2 292 ? 135.714 107.691 150.976 1.00 25.14 ?  271 LEU D C     1 
ATOM   15579 O  O     . LEU D 2 292 ? 135.093 107.220 151.943 1.00 25.14 ?  271 LEU D O     1 
ATOM   15580 C  CB    . LEU D 2 292 ? 136.880 105.519 150.397 1.00 23.71 ?  271 LEU D CB    1 
ATOM   15581 C  CG    . LEU D 2 292 ? 137.242 104.408 149.400 1.00 23.37 ?  271 LEU D CG    1 
ATOM   15582 C  CD1   . LEU D 2 292 ? 138.247 103.429 150.012 1.00 23.28 ?  271 LEU D CD1   1 
ATOM   15583 C  CD2   . LEU D 2 292 ? 135.990 103.663 148.897 1.00 23.06 ?  271 LEU D CD2   1 
ATOM   15584 N  N     . GLY D 2 293 ? 135.991 108.990 150.850 1.00 25.82 ?  272 GLY D N     1 
ATOM   15585 C  CA    . GLY D 2 293 ? 135.587 109.976 151.844 1.00 27.13 ?  272 GLY D CA    1 
ATOM   15586 C  C     . GLY D 2 293 ? 136.353 109.905 153.149 1.00 27.99 ?  272 GLY D C     1 
ATOM   15587 O  O     . GLY D 2 293 ? 135.891 110.423 154.162 1.00 27.97 ?  272 GLY D O     1 
ATOM   15588 N  N     . PHE D 2 294 ? 137.524 109.262 153.127 1.00 28.02 ?  273 PHE D N     1 
ATOM   15589 C  CA    . PHE D 2 294 ? 138.373 109.130 154.319 1.00 28.75 ?  273 PHE D CA    1 
ATOM   15590 C  C     . PHE D 2 294 ? 139.552 110.110 154.308 1.00 29.00 ?  273 PHE D C     1 
ATOM   15591 O  O     . PHE D 2 294 ? 139.935 110.617 153.255 1.00 28.74 ?  273 PHE D O     1 
ATOM   15592 C  CB    . PHE D 2 294 ? 138.906 107.693 154.442 1.00 28.32 ?  273 PHE D CB    1 
ATOM   15593 C  CG    . PHE D 2 294 ? 137.836 106.662 154.675 1.00 28.66 ?  273 PHE D CG    1 
ATOM   15594 C  CD1   . PHE D 2 294 ? 136.784 106.910 155.557 1.00 30.23 ?  273 PHE D CD1   1 
ATOM   15595 C  CD2   . PHE D 2 294 ? 137.890 105.436 154.025 1.00 26.94 ?  273 PHE D CD2   1 
ATOM   15596 C  CE1   . PHE D 2 294 ? 135.790 105.950 155.775 1.00 31.04 ?  273 PHE D CE1   1 
ATOM   15597 C  CE2   . PHE D 2 294 ? 136.914 104.471 154.236 1.00 27.39 ?  273 PHE D CE2   1 
ATOM   15598 C  CZ    . PHE D 2 294 ? 135.863 104.719 155.110 1.00 29.80 ?  273 PHE D CZ    1 
ATOM   15599 N  N     . ASP D 2 295 ? 140.119 110.370 155.485 1.00 29.60 ?  274 ASP D N     1 
ATOM   15600 C  CA    . ASP D 2 295 ? 141.289 111.234 155.614 1.00 30.40 ?  274 ASP D CA    1 
ATOM   15601 C  C     . ASP D 2 295 ? 142.551 110.571 155.029 1.00 29.58 ?  274 ASP D C     1 
ATOM   15602 O  O     . ASP D 2 295 ? 142.657 109.344 155.012 1.00 28.68 ?  274 ASP D O     1 
ATOM   15603 C  CB    . ASP D 2 295 ? 141.535 111.600 157.083 1.00 31.44 ?  274 ASP D CB    1 
ATOM   15604 C  CG    . ASP D 2 295 ? 140.421 112.452 157.680 1.00 34.27 ?  274 ASP D CG    1 
ATOM   15605 O  OD1   . ASP D 2 295 ? 139.755 113.210 156.935 1.00 36.43 ?  274 ASP D OD1   1 
ATOM   15606 O  OD2   . ASP D 2 295 ? 140.220 112.360 158.911 1.00 38.03 -1 274 ASP D OD2   1 
ATOM   15607 N  N     . PRO D 2 296 ? 143.516 111.386 154.559 1.00 29.59 ?  275 PRO D N     1 
ATOM   15608 C  CA    . PRO D 2 296 ? 144.770 110.793 154.084 1.00 29.09 ?  275 PRO D CA    1 
ATOM   15609 C  C     . PRO D 2 296 ? 145.487 110.058 155.215 1.00 29.26 ?  275 PRO D C     1 
ATOM   15610 O  O     . PRO D 2 296 ? 145.422 110.477 156.371 1.00 29.36 ?  275 PRO D O     1 
ATOM   15611 C  CB    . PRO D 2 296 ? 145.592 112.004 153.624 1.00 29.49 ?  275 PRO D CB    1 
ATOM   15612 C  CG    . PRO D 2 296 ? 144.956 113.198 154.282 1.00 30.28 ?  275 PRO D CG    1 
ATOM   15613 C  CD    . PRO D 2 296 ? 143.507 112.856 154.433 1.00 29.63 ?  275 PRO D CD    1 
ATOM   15614 N  N     . TYR D 2 297 ? 146.146 108.958 154.882 1.00 28.97 ?  276 TYR D N     1 
ATOM   15615 C  CA    . TYR D 2 297 ? 146.833 108.140 155.875 1.00 29.63 ?  276 TYR D CA    1 
ATOM   15616 C  C     . TYR D 2 297 ? 148.310 108.542 156.008 1.00 29.55 ?  276 TYR D C     1 
ATOM   15617 O  O     . TYR D 2 297 ? 148.893 108.486 157.099 1.00 30.12 ?  276 TYR D O     1 
ATOM   15618 C  CB    . TYR D 2 297 ? 146.725 106.673 155.461 1.00 29.49 ?  276 TYR D CB    1 
ATOM   15619 C  CG    . TYR D 2 297 ? 147.100 105.674 156.523 1.00 31.19 ?  276 TYR D CG    1 
ATOM   15620 C  CD1   . TYR D 2 297 ? 146.373 105.591 157.715 1.00 31.93 ?  276 TYR D CD1   1 
ATOM   15621 C  CD2   . TYR D 2 297 ? 148.163 104.790 156.330 1.00 31.98 ?  276 TYR D CD2   1 
ATOM   15622 C  CE1   . TYR D 2 297 ? 146.706 104.667 158.697 1.00 33.86 ?  276 TYR D CE1   1 
ATOM   15623 C  CE2   . TYR D 2 297 ? 148.501 103.853 157.308 1.00 33.88 ?  276 TYR D CE2   1 
ATOM   15624 C  CZ    . TYR D 2 297 ? 147.761 103.800 158.483 1.00 34.42 ?  276 TYR D CZ    1 
ATOM   15625 O  OH    . TYR D 2 297 ? 148.082 102.892 159.460 1.00 37.63 ?  276 TYR D OH    1 
ATOM   15626 N  N     . PHE D 2 298 ? 148.896 108.942 154.885 1.00 29.10 ?  277 PHE D N     1 
ATOM   15627 C  CA    . PHE D 2 298 ? 150.323 109.227 154.780 1.00 28.97 ?  277 PHE D CA    1 
ATOM   15628 C  C     . PHE D 2 298 ? 150.575 110.737 154.709 1.00 29.77 ?  277 PHE D C     1 
ATOM   15629 O  O     . PHE D 2 298 ? 149.753 111.486 154.173 1.00 29.07 ?  277 PHE D O     1 
ATOM   15630 C  CB    . PHE D 2 298 ? 150.902 108.553 153.532 1.00 27.99 ?  277 PHE D CB    1 
ATOM   15631 C  CG    . PHE D 2 298 ? 150.777 107.048 153.529 1.00 27.61 ?  277 PHE D CG    1 
ATOM   15632 C  CD1   . PHE D 2 298 ? 149.873 106.413 152.688 1.00 25.91 ?  277 PHE D CD1   1 
ATOM   15633 C  CD2   . PHE D 2 298 ? 151.584 106.266 154.358 1.00 27.32 ?  277 PHE D CD2   1 
ATOM   15634 C  CE1   . PHE D 2 298 ? 149.764 105.033 152.679 1.00 26.65 ?  277 PHE D CE1   1 
ATOM   15635 C  CE2   . PHE D 2 298 ? 151.488 104.886 154.358 1.00 25.38 ?  277 PHE D CE2   1 
ATOM   15636 C  CZ    . PHE D 2 298 ? 150.575 104.263 153.528 1.00 26.20 ?  277 PHE D CZ    1 
ATOM   15637 N  N     . GLU D 2 299 ? 151.710 111.171 155.258 1.00 31.10 ?  278 GLU D N     1 
ATOM   15638 C  CA    . GLU D 2 299 ? 152.147 112.565 155.148 1.00 32.86 ?  278 GLU D CA    1 
ATOM   15639 C  C     . GLU D 2 299 ? 152.357 112.931 153.673 1.00 33.04 ?  278 GLU D C     1 
ATOM   15640 O  O     . GLU D 2 299 ? 152.693 112.072 152.853 1.00 32.23 ?  278 GLU D O     1 
ATOM   15641 C  CB    . GLU D 2 299 ? 153.436 112.798 155.956 1.00 33.45 ?  278 GLU D CB    1 
ATOM   15642 C  CG    . GLU D 2 299 ? 154.629 111.964 155.466 1.00 36.27 ?  278 GLU D CG    1 
ATOM   15643 C  CD    . GLU D 2 299 ? 155.947 112.277 156.158 1.00 40.47 ?  278 GLU D CD    1 
ATOM   15644 O  OE1   . GLU D 2 299 ? 155.964 112.483 157.393 1.00 41.72 ?  278 GLU D OE1   1 
ATOM   15645 O  OE2   . GLU D 2 299 ? 156.979 112.283 155.451 1.00 42.65 -1 278 GLU D OE2   1 
ATOM   15646 N  N     . GLU D 2 300 ? 152.148 114.207 153.353 1.00 34.09 ?  279 GLU D N     1 
ATOM   15647 C  CA    . GLU D 2 300 ? 152.330 114.722 152.003 1.00 35.06 ?  279 GLU D CA    1 
ATOM   15648 C  C     . GLU D 2 300 ? 153.807 114.671 151.609 1.00 34.97 ?  279 GLU D C     1 
ATOM   15649 O  O     . GLU D 2 300 ? 154.682 115.034 152.396 1.00 34.96 ?  279 GLU D O     1 
ATOM   15650 C  CB    . GLU D 2 300 ? 151.786 116.159 151.907 1.00 35.81 ?  279 GLU D CB    1 
ATOM   15651 C  CG    . GLU D 2 300 ? 151.754 116.727 150.486 1.00 38.58 ?  279 GLU D CG    1 
ATOM   15652 C  CD    . GLU D 2 300 ? 150.719 117.836 150.306 1.00 43.09 ?  279 GLU D CD    1 
ATOM   15653 O  OE1   . GLU D 2 300 ? 149.849 117.695 149.416 1.00 44.69 ?  279 GLU D OE1   1 
ATOM   15654 O  OE2   . GLU D 2 300 ? 150.767 118.839 151.054 1.00 44.94 -1 279 GLU D OE2   1 
ATOM   15655 N  N     . GLU D 2 301 ? 154.065 114.190 150.397 1.00 34.73 ?  280 GLU D N     1 
ATOM   15656 C  CA    . GLU D 2 301 ? 155.415 114.107 149.854 1.00 35.16 ?  280 GLU D CA    1 
ATOM   15657 C  C     . GLU D 2 301 ? 155.413 114.666 148.441 1.00 35.23 ?  280 GLU D C     1 
ATOM   15658 O  O     . GLU D 2 301 ? 154.390 114.623 147.750 1.00 34.92 ?  280 GLU D O     1 
ATOM   15659 C  CB    . GLU D 2 301 ? 155.894 112.650 149.824 1.00 35.10 ?  280 GLU D CB    1 
ATOM   15660 C  CG    . GLU D 2 301 ? 156.415 112.116 151.156 1.00 36.62 ?  280 GLU D CG    1 
ATOM   15661 C  CD    . GLU D 2 301 ? 156.622 110.601 151.150 1.00 37.59 ?  280 GLU D CD    1 
ATOM   15662 O  OE1   . GLU D 2 301 ? 155.657 109.859 150.873 1.00 38.10 ?  280 GLU D OE1   1 
ATOM   15663 O  OE2   . GLU D 2 301 ? 157.745 110.150 151.447 1.00 38.93 -1 280 GLU D OE2   1 
ATOM   15664 N  N     . ASP D 2 302 ? 156.554 115.188 148.008 1.00 35.60 ?  281 ASP D N     1 
ATOM   15665 C  CA    . ASP D 2 302 ? 156.687 115.639 146.628 1.00 35.96 ?  281 ASP D CA    1 
ATOM   15666 C  C     . ASP D 2 302 ? 156.940 114.424 145.745 1.00 35.01 ?  281 ASP D C     1 
ATOM   15667 O  O     . ASP D 2 302 ? 157.469 113.416 146.213 1.00 35.52 ?  281 ASP D O     1 
ATOM   15668 C  CB    . ASP D 2 302 ? 157.791 116.703 146.489 1.00 36.82 ?  281 ASP D CB    1 
ATOM   15669 C  CG    . ASP D 2 302 ? 159.196 116.177 146.837 1.00 39.01 ?  281 ASP D CG    1 
ATOM   15670 O  OD1   . ASP D 2 302 ? 159.337 115.154 147.552 1.00 40.83 ?  281 ASP D OD1   1 
ATOM   15671 O  OD2   . ASP D 2 302 ? 160.172 116.821 146.401 1.00 41.13 -1 281 ASP D OD2   1 
ATOM   15672 N  N     . ILE D 2 303 ? 156.530 114.495 144.486 1.00 33.94 ?  282 ILE D N     1 
ATOM   15673 C  CA    . ILE D 2 303 ? 156.714 113.374 143.567 1.00 33.00 ?  282 ILE D CA    1 
ATOM   15674 C  C     . ILE D 2 303 ? 157.832 113.638 142.549 1.00 31.59 ?  282 ILE D C     1 
ATOM   15675 O  O     . ILE D 2 303 ? 158.110 114.790 142.208 1.00 31.14 ?  282 ILE D O     1 
ATOM   15676 C  CB    . ILE D 2 303 ? 155.366 112.962 142.893 1.00 33.44 ?  282 ILE D CB    1 
ATOM   15677 C  CG1   . ILE D 2 303 ? 155.579 112.378 141.491 1.00 34.29 ?  282 ILE D CG1   1 
ATOM   15678 C  CG2   . ILE D 2 303 ? 154.398 114.133 142.865 1.00 35.47 ?  282 ILE D CG2   1 
ATOM   15679 C  CD1   . ILE D 2 303 ? 154.300 112.148 140.712 1.00 36.30 ?  282 ILE D CD1   1 
ATOM   15680 N  N     . ASN D 2 304 ? 158.483 112.567 142.095 1.00 29.53 ?  283 ASN D N     1 
ATOM   15681 C  CA    . ASN D 2 304 ? 159.507 112.661 141.058 1.00 28.49 ?  283 ASN D CA    1 
ATOM   15682 C  C     . ASN D 2 304 ? 159.048 113.557 139.888 1.00 27.87 ?  283 ASN D C     1 
ATOM   15683 O  O     . ASN D 2 304 ? 157.992 113.316 139.304 1.00 27.02 ?  283 ASN D O     1 
ATOM   15684 C  CB    . ASN D 2 304 ? 159.869 111.263 140.553 1.00 28.20 ?  283 ASN D CB    1 
ATOM   15685 C  CG    . ASN D 2 304 ? 160.988 111.287 139.547 1.00 28.17 ?  283 ASN D CG    1 
ATOM   15686 O  OD1   . ASN D 2 304 ? 160.756 111.484 138.358 1.00 29.01 ?  283 ASN D OD1   1 
ATOM   15687 N  ND2   . ASN D 2 304 ? 162.211 111.088 140.013 1.00 27.24 ?  283 ASN D ND2   1 
ATOM   15688 N  N     . PRO D 2 305 ? 159.835 114.602 139.556 1.00 28.00 ?  284 PRO D N     1 
ATOM   15689 C  CA    . PRO D 2 305 ? 159.409 115.570 138.533 1.00 27.58 ?  284 PRO D CA    1 
ATOM   15690 C  C     . PRO D 2 305 ? 159.305 114.999 137.117 1.00 27.01 ?  284 PRO D C     1 
ATOM   15691 O  O     . PRO D 2 305 ? 158.555 115.527 136.302 1.00 26.66 ?  284 PRO D O     1 
ATOM   15692 C  CB    . PRO D 2 305 ? 160.490 116.657 138.592 1.00 28.21 ?  284 PRO D CB    1 
ATOM   15693 C  CG    . PRO D 2 305 ? 161.648 116.031 139.236 1.00 28.80 ?  284 PRO D CG    1 
ATOM   15694 C  CD    . PRO D 2 305 ? 161.082 115.029 140.217 1.00 28.11 ?  284 PRO D CD    1 
ATOM   15695 N  N     . ILE D 2 306 ? 160.044 113.931 136.831 1.00 26.52 ?  285 ILE D N     1 
ATOM   15696 C  CA    . ILE D 2 306 ? 159.964 113.287 135.526 1.00 26.50 ?  285 ILE D CA    1 
ATOM   15697 C  C     . ILE D 2 306 ? 158.609 112.583 135.371 1.00 26.43 ?  285 ILE D C     1 
ATOM   15698 O  O     . ILE D 2 306 ? 157.911 112.750 134.360 1.00 26.00 ?  285 ILE D O     1 
ATOM   15699 C  CB    . ILE D 2 306 ? 161.156 112.328 135.281 1.00 26.88 ?  285 ILE D CB    1 
ATOM   15700 C  CG1   . ILE D 2 306 ? 162.477 113.115 135.336 1.00 26.98 ?  285 ILE D CG1   1 
ATOM   15701 C  CG2   . ILE D 2 306 ? 160.978 111.603 133.947 1.00 24.94 ?  285 ILE D CG2   1 
ATOM   15702 C  CD1   . ILE D 2 306 ? 163.724 112.274 135.300 1.00 26.65 ?  285 ILE D CD1   1 
ATOM   15703 N  N     . VAL D 2 307 ? 158.230 111.827 136.396 1.00 26.36 ?  286 VAL D N     1 
ATOM   15704 C  CA    . VAL D 2 307 ? 156.901 111.232 136.463 1.00 26.71 ?  286 VAL D CA    1 
ATOM   15705 C  C     . VAL D 2 307 ? 155.802 112.299 136.439 1.00 27.68 ?  286 VAL D C     1 
ATOM   15706 O  O     . VAL D 2 307 ? 154.807 112.127 135.735 1.00 27.92 ?  286 VAL D O     1 
ATOM   15707 C  CB    . VAL D 2 307 ? 156.766 110.266 137.671 1.00 26.37 ?  286 VAL D CB    1 
ATOM   15708 C  CG1   . VAL D 2 307 ? 155.306 109.835 137.890 1.00 25.48 ?  286 VAL D CG1   1 
ATOM   15709 C  CG2   . VAL D 2 307 ? 157.617 109.061 137.429 1.00 25.55 ?  286 VAL D CG2   1 
ATOM   15710 N  N     . LEU D 2 308 ? 155.989 113.407 137.163 1.00 28.80 ?  287 LEU D N     1 
ATOM   15711 C  CA    . LEU D 2 308 ? 155.033 114.523 137.084 1.00 30.07 ?  287 LEU D CA    1 
ATOM   15712 C  C     . LEU D 2 308 ? 154.879 115.067 135.660 1.00 30.38 ?  287 LEU D C     1 
ATOM   15713 O  O     . LEU D 2 308 ? 153.766 115.359 135.210 1.00 30.71 ?  287 LEU D O     1 
ATOM   15714 C  CB    . LEU D 2 308 ? 155.408 115.657 138.042 1.00 30.86 ?  287 LEU D CB    1 
ATOM   15715 C  CG    . LEU D 2 308 ? 154.924 115.497 139.487 1.00 32.62 ?  287 LEU D CG    1 
ATOM   15716 C  CD1   . LEU D 2 308 ? 155.526 116.563 140.375 1.00 33.97 ?  287 LEU D CD1   1 
ATOM   15717 C  CD2   . LEU D 2 308 ? 153.387 115.519 139.574 1.00 34.73 ?  287 LEU D CD2   1 
ATOM   15718 N  N     . ASN D 2 309 ? 155.993 115.193 134.947 1.00 30.81 ?  288 ASN D N     1 
ATOM   15719 C  CA    . ASN D 2 309 ? 155.952 115.654 133.563 1.00 31.25 ?  288 ASN D CA    1 
ATOM   15720 C  C     . ASN D 2 309 ? 155.203 114.671 132.662 1.00 31.83 ?  288 ASN D C     1 
ATOM   15721 O  O     . ASN D 2 309 ? 154.523 115.080 131.716 1.00 31.73 ?  288 ASN D O     1 
ATOM   15722 C  CB    . ASN D 2 309 ? 157.357 115.941 133.023 1.00 31.21 ?  288 ASN D CB    1 
ATOM   15723 C  CG    . ASN D 2 309 ? 157.324 116.610 131.658 1.00 31.41 ?  288 ASN D CG    1 
ATOM   15724 O  OD1   . ASN D 2 309 ? 156.539 117.537 131.429 1.00 31.88 ?  288 ASN D OD1   1 
ATOM   15725 N  ND2   . ASN D 2 309 ? 158.168 116.141 130.745 1.00 29.12 ?  288 ASN D ND2   1 
ATOM   15726 N  N     . GLY D 2 310 ? 155.329 113.379 132.967 1.00 32.04 ?  289 GLY D N     1 
ATOM   15727 C  CA    . GLY D 2 310 ? 154.554 112.341 132.296 1.00 33.04 ?  289 GLY D CA    1 
ATOM   15728 C  C     . GLY D 2 310 ? 153.067 112.475 132.597 1.00 33.85 ?  289 GLY D C     1 
ATOM   15729 O  O     . GLY D 2 310 ? 152.243 112.434 131.683 1.00 34.05 ?  289 GLY D O     1 
ATOM   15730 N  N     . LEU D 2 311 ? 152.730 112.638 133.875 1.00 34.33 ?  290 LEU D N     1 
ATOM   15731 C  CA    . LEU D 2 311 ? 151.340 112.760 134.323 1.00 35.77 ?  290 LEU D CA    1 
ATOM   15732 C  C     . LEU D 2 311 ? 150.621 113.972 133.740 1.00 37.01 ?  290 LEU D C     1 
ATOM   15733 O  O     . LEU D 2 311 ? 149.450 113.886 133.369 1.00 37.18 ?  290 LEU D O     1 
ATOM   15734 C  CB    . LEU D 2 311 ? 151.271 112.841 135.854 1.00 35.50 ?  290 LEU D CB    1 
ATOM   15735 C  CG    . LEU D 2 311 ? 151.136 111.591 136.717 1.00 35.45 ?  290 LEU D CG    1 
ATOM   15736 C  CD1   . LEU D 2 311 ? 151.286 111.981 138.196 1.00 35.28 ?  290 LEU D CD1   1 
ATOM   15737 C  CD2   . LEU D 2 311 ? 149.806 110.867 136.488 1.00 34.16 ?  290 LEU D CD2   1 
ATOM   15738 N  N     . LYS D 2 330 ? 117.370 117.741 149.633 1.00 61.72 ?  309 LYS D N     1 
ATOM   15739 C  CA    . LYS D 2 330 ? 116.070 117.082 149.621 1.00 61.83 ?  309 LYS D CA    1 
ATOM   15740 C  C     . LYS D 2 330 ? 115.715 116.558 151.005 1.00 62.21 ?  309 LYS D C     1 
ATOM   15741 O  O     . LYS D 2 330 ? 115.959 115.387 151.303 1.00 61.32 ?  309 LYS D O     1 
ATOM   15742 C  CB    . LYS D 2 330 ? 116.057 115.921 148.623 1.00 59.60 ?  309 LYS D CB    1 
ATOM   15743 C  CG    . LYS D 2 330 ? 116.645 116.234 147.260 1.00 60.95 ?  309 LYS D CG    1 
ATOM   15744 C  CD    . LYS D 2 330 ? 115.631 115.990 146.153 1.00 60.77 ?  309 LYS D CD    1 
ATOM   15745 C  CE    . LYS D 2 330 ? 116.063 116.648 144.854 1.00 61.40 ?  309 LYS D CE    1 
ATOM   15746 N  NZ    . LYS D 2 330 ? 115.256 117.859 144.544 1.00 62.04 1  309 LYS D NZ    1 
ATOM   15747 N  N     . ALA D 2 331 ? 115.150 117.406 151.864 1.00 57.72 ?  310 ALA D N     1 
ATOM   15748 C  CA    . ALA D 2 331 ? 114.753 116.932 153.182 1.00 58.04 ?  310 ALA D CA    1 
ATOM   15749 C  C     . ALA D 2 331 ? 113.397 116.239 153.164 1.00 58.14 ?  310 ALA D C     1 
ATOM   15750 O  O     . ALA D 2 331 ? 113.329 115.018 153.333 1.00 58.87 ?  310 ALA D O     1 
ATOM   15751 C  CB    . ALA D 2 331 ? 114.731 118.100 154.175 1.00 56.57 ?  310 ALA D CB    1 
ATOM   15752 N  N     . THR D 2 332 ? 112.315 116.994 152.955 1.00 46.15 ?  311 THR D N     1 
ATOM   15753 C  CA    . THR D 2 332 ? 111.003 116.446 152.624 1.00 42.78 ?  311 THR D CA    1 
ATOM   15754 C  C     . THR D 2 332 ? 110.056 117.557 152.178 1.00 42.27 ?  311 THR D C     1 
ATOM   15755 O  O     . THR D 2 332 ? 109.727 118.449 152.967 1.00 45.09 ?  311 THR D O     1 
ATOM   15756 C  CB    . THR D 2 332 ? 110.420 115.660 153.805 1.00 46.86 ?  311 THR D CB    1 
ATOM   15757 O  OG1   . THR D 2 332 ? 109.238 114.959 153.395 1.00 46.97 ?  311 THR D OG1   1 
ATOM   15758 C  CG2   . THR D 2 332 ? 110.131 116.565 154.987 1.00 43.65 ?  311 THR D CG2   1 
ATOM   15759 N  N     . VAL D 2 333 ? 109.609 117.516 150.925 1.00 39.49 ?  312 VAL D N     1 
ATOM   15760 C  CA    . VAL D 2 333 ? 108.670 118.510 150.417 1.00 35.97 ?  312 VAL D CA    1 
ATOM   15761 C  C     . VAL D 2 333 ? 107.323 118.333 151.108 1.00 40.19 ?  312 VAL D C     1 
ATOM   15762 O  O     . VAL D 2 333 ? 106.746 117.239 151.093 1.00 43.38 ?  312 VAL D O     1 
ATOM   15763 C  CB    . VAL D 2 333 ? 108.523 118.412 148.887 1.00 38.60 ?  312 VAL D CB    1 
ATOM   15764 C  CG1   . VAL D 2 333 ? 107.197 119.009 148.434 1.00 39.63 ?  312 VAL D CG1   1 
ATOM   15765 C  CG2   . VAL D 2 333 ? 109.686 119.104 148.197 1.00 39.03 ?  312 VAL D CG2   1 
ATOM   15766 N  N     . GLU D 2 334 ? 106.818 119.400 151.723 1.00 39.20 ?  313 GLU D N     1 
ATOM   15767 C  CA    . GLU D 2 334 ? 105.487 119.403 152.322 1.00 36.81 ?  313 GLU D CA    1 
ATOM   15768 C  C     . GLU D 2 334 ? 104.781 120.684 151.898 1.00 37.73 ?  313 GLU D C     1 
ATOM   15769 O  O     . GLU D 2 334 ? 105.372 121.778 152.005 1.00 40.12 ?  313 GLU D O     1 
ATOM   15770 C  CB    . GLU D 2 334 ? 105.548 119.291 153.847 1.00 34.61 ?  313 GLU D CB    1 
ATOM   15771 C  CG    . GLU D 2 334 ? 104.180 119.118 154.490 1.00 37.90 ?  313 GLU D CG    1 
ATOM   15772 C  CD    . GLU D 2 334 ? 104.239 118.981 155.997 1.00 39.43 ?  313 GLU D CD    1 
ATOM   15773 O  OE1   . GLU D 2 334 ? 105.353 118.901 156.546 1.00 37.54 ?  313 GLU D OE1   1 
ATOM   15774 O  OE2   . GLU D 2 334 ? 103.166 118.950 156.634 1.00 39.69 -1 313 GLU D OE2   1 
ATOM   15775 N  N     . PRO D 2 335 ? 103.545 120.610 151.413 1.00 38.18 ?  314 PRO D N     1 
ATOM   15776 C  CA    . PRO D 2 335 ? 102.855 121.824 150.965 1.00 40.62 ?  314 PRO D CA    1 
ATOM   15777 C  C     . PRO D 2 335 ? 102.455 122.718 152.127 1.00 40.02 ?  314 PRO D C     1 
ATOM   15778 O  O     . PRO D 2 335 ? 102.290 122.270 153.263 1.00 41.11 ?  314 PRO D O     1 
ATOM   15779 C  CB    . PRO D 2 335 ? 101.622 121.278 150.238 1.00 37.91 ?  314 PRO D CB    1 
ATOM   15780 C  CG    . PRO D 2 335 ? 101.368 119.963 150.895 1.00 34.58 ?  314 PRO D CG    1 
ATOM   15781 C  CD    . PRO D 2 335 ? 102.727 119.403 151.206 1.00 36.60 ?  314 PRO D CD    1 
ATOM   15782 N  N     . LEU D 2 336 ? 102.308 124.006 151.825 1.00 34.57 ?  315 LEU D N     1 
ATOM   15783 C  CA    . LEU D 2 336 ? 101.752 124.954 152.779 1.00 30.08 ?  315 LEU D CA    1 
ATOM   15784 C  C     . LEU D 2 336 ? 100.236 124.801 152.810 1.00 33.20 ?  315 LEU D C     1 
ATOM   15785 O  O     . LEU D 2 336 ? 99.563  125.011 151.797 1.00 37.22 ?  315 LEU D O     1 
ATOM   15786 C  CB    . LEU D 2 336 ? 102.137 126.383 152.398 1.00 28.04 ?  315 LEU D CB    1 
ATOM   15787 C  CG    . LEU D 2 336 ? 103.553 126.839 152.750 1.00 27.76 ?  315 LEU D CG    1 
ATOM   15788 C  CD1   . LEU D 2 336 ? 103.993 127.967 151.832 1.00 24.11 ?  315 LEU D CD1   1 
ATOM   15789 C  CD2   . LEU D 2 336 ? 103.624 127.271 154.202 1.00 29.08 ?  315 LEU D CD2   1 
ATOM   15790 N  N     . LYS D 2 337 ? 99.700  124.437 153.974 1.00 36.25 ?  316 LYS D N     1 
ATOM   15791 C  CA    . LYS D 2 337 ? 98.293  124.082 154.109 1.00 47.76 ?  316 LYS D CA    1 
ATOM   15792 C  C     . LYS D 2 337 ? 97.491  125.187 154.789 1.00 47.26 ?  316 LYS D C     1 
ATOM   15793 O  O     . LYS D 2 337 ? 96.563  124.905 155.550 1.00 51.37 ?  316 LYS D O     1 
ATOM   15794 C  CB    . LYS D 2 337 ? 98.142  122.769 154.875 1.00 44.37 ?  316 LYS D CB    1 
ATOM   15795 C  CG    . LYS D 2 337 ? 99.094  122.632 156.052 1.00 46.03 ?  316 LYS D CG    1 
ATOM   15796 C  CD    . LYS D 2 337 ? 99.527  121.190 156.253 1.00 46.40 ?  316 LYS D CD    1 
ATOM   15797 C  CE    . LYS D 2 337 ? 100.072 120.596 154.965 1.00 45.29 ?  316 LYS D CE    1 
ATOM   15798 N  NZ    . LYS D 2 337 ? 100.915 119.398 155.219 1.00 42.09 1  316 LYS D NZ    1 
ATOM   15799 N  N     . ASP D 2 338 ? 97.848  126.445 154.521 1.00 29.55 ?  317 ASP D N     1 
ATOM   15800 C  CA    . ASP D 2 338 ? 97.206  127.614 155.116 1.00 32.48 ?  317 ASP D CA    1 
ATOM   15801 C  C     . ASP D 2 338 ? 97.363  127.632 156.633 1.00 37.94 ?  317 ASP D C     1 
ATOM   15802 O  O     . ASP D 2 338 ? 97.814  126.650 157.232 1.00 40.84 ?  317 ASP D O     1 
ATOM   15803 C  CB    . ASP D 2 338 ? 95.727  127.682 154.731 1.00 36.01 ?  317 ASP D CB    1 
ATOM   15804 C  CG    . ASP D 2 338 ? 95.202  129.102 154.697 1.00 38.86 ?  317 ASP D CG    1 
ATOM   15805 O  OD1   . ASP D 2 338 ? 96.002  130.032 154.934 1.00 36.19 ?  317 ASP D OD1   1 
ATOM   15806 O  OD2   . ASP D 2 338 ? 93.996  129.288 154.436 1.00 34.94 -1 317 ASP D OD2   1 
ATOM   15807 N  N     . ASP D 2 339 ? 97.041  128.773 157.249 1.00 32.37 ?  318 ASP D N     1 
ATOM   15808 C  CA    . ASP D 2 339 ? 97.226  129.011 158.680 1.00 28.49 ?  318 ASP D CA    1 
ATOM   15809 C  C     . ASP D 2 339 ? 98.710  129.055 159.026 1.00 28.80 ?  318 ASP D C     1 
ATOM   15810 O  O     . ASP D 2 339 ? 99.081  129.321 160.173 1.00 36.28 ?  318 ASP D O     1 
ATOM   15811 C  CB    . ASP D 2 339 ? 96.501  127.958 159.523 1.00 30.55 ?  318 ASP D CB    1 
ATOM   15812 C  CG    . ASP D 2 339 ? 95.638  128.575 160.607 1.00 37.05 ?  318 ASP D CG    1 
ATOM   15813 O  OD1   . ASP D 2 339 ? 96.007  129.652 161.121 1.00 32.14 ?  318 ASP D OD1   1 
ATOM   15814 O  OD2   . ASP D 2 339 ? 94.590  127.984 160.944 1.00 39.30 -1 318 ASP D OD2   1 
ATOM   15815 N  N     . ASP D 2 340 ? 99.564  128.794 158.037 1.00 24.72 ?  319 ASP D N     1 
ATOM   15816 C  CA    . ASP D 2 340 ? 100.992 129.037 158.141 1.00 24.52 ?  319 ASP D CA    1 
ATOM   15817 C  C     . ASP D 2 340 ? 101.355 130.469 157.782 1.00 21.51 ?  319 ASP D C     1 
ATOM   15818 O  O     . ASP D 2 340 ? 102.492 130.886 158.019 1.00 32.71 ?  319 ASP D O     1 
ATOM   15819 C  CB    . ASP D 2 340 ? 101.760 128.070 157.234 1.00 23.05 ?  319 ASP D CB    1 
ATOM   15820 C  CG    . ASP D 2 340 ? 101.656 126.630 157.696 1.00 28.00 ?  319 ASP D CG    1 
ATOM   15821 O  OD1   . ASP D 2 340 ? 101.541 126.401 158.918 1.00 34.28 ?  319 ASP D OD1   1 
ATOM   15822 O  OD2   . ASP D 2 340 ? 101.687 125.726 156.836 1.00 31.08 -1 319 ASP D OD2   1 
ATOM   15823 N  N     . PHE D 2 341 ? 100.413 131.219 157.215 1.00 10.52 ?  320 PHE D N     1 
ATOM   15824 C  CA    . PHE D 2 341 ? 100.583 132.630 156.913 1.00 15.27 ?  320 PHE D CA    1 
ATOM   15825 C  C     . PHE D 2 341 ? 100.023 133.524 158.007 1.00 12.85 ?  320 PHE D C     1 
ATOM   15826 O  O     . PHE D 2 341 ? 100.070 134.750 157.874 1.00 22.40 ?  320 PHE D O     1 
ATOM   15827 C  CB    . PHE D 2 341 ? 99.907  132.966 155.579 1.00 21.01 ?  320 PHE D CB    1 
ATOM   15828 C  CG    . PHE D 2 341 ? 100.482 132.230 154.402 1.00 15.79 ?  320 PHE D CG    1 
ATOM   15829 C  CD1   . PHE D 2 341 ? 100.047 130.954 154.090 1.00 11.88 ?  320 PHE D CD1   1 
ATOM   15830 C  CD2   . PHE D 2 341 ? 101.447 132.815 153.604 1.00 9.87  ?  320 PHE D CD2   1 
ATOM   15831 C  CE1   . PHE D 2 341 ? 100.571 130.275 153.010 1.00 13.02 ?  320 PHE D CE1   1 
ATOM   15832 C  CE2   . PHE D 2 341 ? 101.973 132.140 152.521 1.00 10.78 ?  320 PHE D CE2   1 
ATOM   15833 C  CZ    . PHE D 2 341 ? 101.535 130.868 152.225 1.00 4.79  ?  320 PHE D CZ    1 
ATOM   15834 N  N     . TYR D 2 342 ? 99.496  132.939 159.078 1.00 12.46 ?  321 TYR D N     1 
ATOM   15835 C  CA    . TYR D 2 342 ? 98.895  133.681 160.175 1.00 17.95 ?  321 TYR D CA    1 
ATOM   15836 C  C     . TYR D 2 342 ? 99.574  133.279 161.473 1.00 22.41 ?  321 TYR D C     1 
ATOM   15837 O  O     . TYR D 2 342 ? 99.889  132.104 161.681 1.00 24.04 ?  321 TYR D O     1 
ATOM   15838 C  CB    . TYR D 2 342 ? 97.390  133.415 160.262 1.00 13.28 ?  321 TYR D CB    1 
ATOM   15839 C  CG    . TYR D 2 342 ? 96.624  133.870 159.042 1.00 11.63 ?  321 TYR D CG    1 
ATOM   15840 C  CD1   . TYR D 2 342 ? 96.212  135.189 158.907 1.00 16.81 ?  321 TYR D CD1   1 
ATOM   15841 C  CD2   . TYR D 2 342 ? 96.319  132.980 158.021 1.00 15.94 ?  321 TYR D CD2   1 
ATOM   15842 C  CE1   . TYR D 2 342 ? 95.514  135.607 157.791 1.00 20.80 ?  321 TYR D CE1   1 
ATOM   15843 C  CE2   . TYR D 2 342 ? 95.622  133.389 156.902 1.00 15.55 ?  321 TYR D CE2   1 
ATOM   15844 C  CZ    . TYR D 2 342 ? 95.222  134.703 156.792 1.00 24.69 ?  321 TYR D CZ    1 
ATOM   15845 O  OH    . TYR D 2 342 ? 94.526  135.117 155.679 1.00 21.45 ?  321 TYR D OH    1 
ATOM   15846 N  N     . PHE D 2 343 ? 99.806  134.258 162.339 1.00 12.93 ?  322 PHE D N     1 
ATOM   15847 C  CA    . PHE D 2 343 ? 100.516 134.018 163.590 1.00 18.66 ?  322 PHE D CA    1 
ATOM   15848 C  C     . PHE D 2 343 ? 99.846  134.745 164.750 1.00 24.79 ?  322 PHE D C     1 
ATOM   15849 O  O     . PHE D 2 343 ? 99.535  135.931 164.659 1.00 23.91 ?  322 PHE D O     1 
ATOM   15850 C  CB    . PHE D 2 343 ? 101.980 134.457 163.464 1.00 13.99 ?  322 PHE D CB    1 
ATOM   15851 C  CG    . PHE D 2 343 ? 102.634 134.021 162.184 1.00 14.21 ?  322 PHE D CG    1 
ATOM   15852 C  CD1   . PHE D 2 343 ? 102.600 134.828 161.060 1.00 13.48 ?  322 PHE D CD1   1 
ATOM   15853 C  CD2   . PHE D 2 343 ? 103.281 132.801 162.104 1.00 16.65 ?  322 PHE D CD2   1 
ATOM   15854 C  CE1   . PHE D 2 343 ? 103.196 134.424 159.884 1.00 9.34  ?  322 PHE D CE1   1 
ATOM   15855 C  CE2   . PHE D 2 343 ? 103.878 132.395 160.930 1.00 9.50  ?  322 PHE D CE2   1 
ATOM   15856 C  CZ    . PHE D 2 343 ? 103.835 133.208 159.820 1.00 5.03  ?  322 PHE D CZ    1 
HETATM 15857 P  PA    . TTP E 3 .   ? 146.016 143.826 134.611 1.00 19.37 ?  801 TTP A PA    1 
HETATM 15858 O  O1A   . TTP E 3 .   ? 144.597 144.315 134.502 1.00 21.91 -1 801 TTP A O1A   1 
HETATM 15859 O  O2A   . TTP E 3 .   ? 146.924 144.611 133.699 1.00 26.56 ?  801 TTP A O2A   1 
HETATM 15860 O  O3A   . TTP E 3 .   ? 146.506 143.839 136.141 1.00 35.02 ?  801 TTP A O3A   1 
HETATM 15861 P  PB    . TTP E 3 .   ? 147.615 144.875 136.671 1.00 29.77 ?  801 TTP A PB    1 
HETATM 15862 O  O1B   . TTP E 3 .   ? 147.263 145.321 138.066 1.00 33.96 -1 801 TTP A O1B   1 
HETATM 15863 O  O2B   . TTP E 3 .   ? 147.783 146.071 135.770 1.00 25.37 ?  801 TTP A O2B   1 
HETATM 15864 O  O3B   . TTP E 3 .   ? 148.916 143.931 136.675 1.00 28.38 ?  801 TTP A O3B   1 
HETATM 15865 P  PG    . TTP E 3 .   ? 150.281 144.353 135.936 1.00 32.16 ?  801 TTP A PG    1 
HETATM 15866 O  O1G   . TTP E 3 .   ? 149.981 144.888 134.557 1.00 33.52 ?  801 TTP A O1G   1 
HETATM 15867 O  O2G   . TTP E 3 .   ? 151.160 143.136 135.815 1.00 23.47 -1 801 TTP A O2G   1 
HETATM 15868 O  O3G   . TTP E 3 .   ? 150.998 145.409 136.738 1.00 34.78 ?  801 TTP A O3G   1 
HETATM 15869 O  "O5'" . TTP E 3 .   ? 146.111 142.265 134.261 1.00 18.77 ?  801 TTP A "O5'" 1 
HETATM 15870 C  "C5'" . TTP E 3 .   ? 147.031 141.850 133.259 1.00 25.04 ?  801 TTP A "C5'" 1 
HETATM 15871 C  "C4'" . TTP E 3 .   ? 146.794 140.393 132.905 1.00 26.93 ?  801 TTP A "C4'" 1 
HETATM 15872 O  "O4'" . TTP E 3 .   ? 146.449 139.657 134.077 1.00 30.38 ?  801 TTP A "O4'" 1 
HETATM 15873 C  "C3'" . TTP E 3 .   ? 145.638 140.254 131.936 1.00 25.75 ?  801 TTP A "C3'" 1 
HETATM 15874 O  "O3'" . TTP E 3 .   ? 146.121 139.920 130.633 1.00 30.86 ?  801 TTP A "O3'" 1 
HETATM 15875 C  "C2'" . TTP E 3 .   ? 144.788 139.124 132.476 1.00 28.56 ?  801 TTP A "C2'" 1 
HETATM 15876 C  "C1'" . TTP E 3 .   ? 145.442 138.691 133.778 1.00 25.58 ?  801 TTP A "C1'" 1 
HETATM 15877 N  N1    . TTP E 3 .   ? 144.448 138.655 134.849 1.00 26.58 ?  801 TTP A N1    1 
HETATM 15878 C  C2    . TTP E 3 .   ? 143.852 137.425 135.205 1.00 30.61 ?  801 TTP A C2    1 
HETATM 15879 O  O2    . TTP E 3 .   ? 144.189 136.387 134.601 1.00 27.38 ?  801 TTP A O2    1 
HETATM 15880 N  N3    . TTP E 3 .   ? 142.940 137.347 136.181 1.00 28.52 ?  801 TTP A N3    1 
HETATM 15881 C  C4    . TTP E 3 .   ? 142.565 138.442 136.844 1.00 31.97 ?  801 TTP A C4    1 
HETATM 15882 O  O4    . TTP E 3 .   ? 141.713 138.371 137.754 1.00 33.14 ?  801 TTP A O4    1 
HETATM 15883 C  C5    . TTP E 3 .   ? 143.173 139.744 136.487 1.00 26.42 ?  801 TTP A C5    1 
HETATM 15884 C  C5M   . TTP E 3 .   ? 142.778 141.000 137.213 1.00 26.94 ?  801 TTP A C5M   1 
HETATM 15885 C  C6    . TTP E 3 .   ? 144.115 139.787 135.473 1.00 25.12 ?  801 TTP A C6    1 
HETATM 15886 MG MG    . MG  F 4 .   ? 148.224 146.153 133.340 1.00 24.14 ?  802 MG  A MG    1 
HETATM 15887 P  PG    . ATP G 5 .   ? 108.947 133.236 78.038  1.00 73.57 ?  803 ATP A PG    1 
HETATM 15888 O  O1G   . ATP G 5 .   ? 109.426 134.138 76.951  1.00 63.77 ?  803 ATP A O1G   1 
HETATM 15889 O  O2G   . ATP G 5 .   ? 108.418 131.890 77.532  1.00 64.13 -1 803 ATP A O2G   1 
HETATM 15890 O  O3G   . ATP G 5 .   ? 109.989 132.986 79.133  1.00 61.47 ?  803 ATP A O3G   1 
HETATM 15891 P  PB    . ATP G 5 .   ? 107.395 134.717 80.131  1.00 71.75 ?  803 ATP A PB    1 
HETATM 15892 O  O1B   . ATP G 5 .   ? 108.210 135.946 80.216  1.00 63.94 -1 803 ATP A O1B   1 
HETATM 15893 O  O2B   . ATP G 5 .   ? 105.882 134.929 80.189  1.00 62.90 ?  803 ATP A O2B   1 
HETATM 15894 O  O3B   . ATP G 5 .   ? 107.707 133.892 78.807  1.00 66.82 ?  803 ATP A O3B   1 
HETATM 15895 P  PA    . ATP G 5 .   ? 107.010 132.586 82.155  1.00 70.68 ?  803 ATP A PA    1 
HETATM 15896 O  O1A   . ATP G 5 .   ? 107.651 131.259 82.067  1.00 64.00 -1 803 ATP A O1A   1 
HETATM 15897 O  O2A   . ATP G 5 .   ? 105.540 132.613 81.738  1.00 62.49 ?  803 ATP A O2A   1 
HETATM 15898 O  O3A   . ATP G 5 .   ? 107.775 133.667 81.267  1.00 63.22 ?  803 ATP A O3A   1 
HETATM 15899 O  "O5'" . ATP G 5 .   ? 107.123 133.190 83.609  1.00 62.47 ?  803 ATP A "O5'" 1 
HETATM 15900 C  "C5'" . ATP G 5 .   ? 106.244 134.247 84.049  1.00 61.67 ?  803 ATP A "C5'" 1 
HETATM 15901 C  "C4'" . ATP G 5 .   ? 106.951 135.067 85.099  1.00 61.88 ?  803 ATP A "C4'" 1 
HETATM 15902 O  "O4'" . ATP G 5 .   ? 107.429 134.200 86.149  1.00 63.84 ?  803 ATP A "O4'" 1 
HETATM 15903 C  "C3'" . ATP G 5 .   ? 108.183 135.821 84.614  1.00 60.84 ?  803 ATP A "C3'" 1 
HETATM 15904 O  "O3'" . ATP G 5 .   ? 107.826 137.092 84.082  1.00 63.01 ?  803 ATP A "O3'" 1 
HETATM 15905 C  "C2'" . ATP G 5 .   ? 109.002 135.961 85.897  1.00 62.28 ?  803 ATP A "C2'" 1 
HETATM 15906 O  "O2'" . ATP G 5 .   ? 108.561 137.059 86.686  1.00 61.13 ?  803 ATP A "O2'" 1 
HETATM 15907 C  "C1'" . ATP G 5 .   ? 108.700 134.635 86.603  1.00 61.93 ?  803 ATP A "C1'" 1 
HETATM 15908 N  N9    . ATP G 5 .   ? 109.672 133.581 86.336  1.00 60.22 ?  803 ATP A N9    1 
HETATM 15909 C  C8    . ATP G 5 .   ? 109.430 132.358 85.767  1.00 60.42 ?  803 ATP A C8    1 
HETATM 15910 N  N7    . ATP G 5 .   ? 110.494 131.602 85.647  1.00 60.85 ?  803 ATP A N7    1 
HETATM 15911 C  C5    . ATP G 5 .   ? 111.510 132.382 86.178  1.00 61.63 ?  803 ATP A C5    1 
HETATM 15912 C  C6    . ATP G 5 .   ? 112.890 132.157 86.349  1.00 58.03 ?  803 ATP A C6    1 
HETATM 15913 N  N6    . ATP G 5 .   ? 113.512 131.032 85.986  1.00 57.72 ?  803 ATP A N6    1 
HETATM 15914 N  N1    . ATP G 5 .   ? 113.620 133.142 86.915  1.00 58.44 ?  803 ATP A N1    1 
HETATM 15915 C  C2    . ATP G 5 .   ? 113.008 134.273 87.276  1.00 58.37 ?  803 ATP A C2    1 
HETATM 15916 N  N3    . ATP G 5 .   ? 111.718 134.595 87.168  1.00 61.94 ?  803 ATP A N3    1 
HETATM 15917 C  C4    . ATP G 5 .   ? 111.018 133.604 86.608  1.00 62.47 ?  803 ATP A C4    1 
HETATM 15918 O  O1B   . DGI H 6 .   ? 105.043 150.353 83.816  1.00 65.79 ?  804 DGI A O1B   1 
HETATM 15919 P  PB    . DGI H 6 .   ? 105.171 151.824 84.140  1.00 74.95 ?  804 DGI A PB    1 
HETATM 15920 O  O2B   . DGI H 6 .   ? 103.843 152.554 84.115  1.00 66.56 -1 804 DGI A O2B   1 
HETATM 15921 O  O3B   . DGI H 6 .   ? 106.238 152.521 83.322  1.00 66.82 ?  804 DGI A O3B   1 
HETATM 15922 O  O3A   . DGI H 6 .   ? 105.680 151.834 85.685  1.00 67.64 ?  804 DGI A O3A   1 
HETATM 15923 P  PA    . DGI H 6 .   ? 105.565 151.003 87.047  1.00 72.66 ?  804 DGI A PA    1 
HETATM 15924 O  O1A   . DGI H 6 .   ? 105.696 151.929 88.191  1.00 65.42 -1 804 DGI A O1A   1 
HETATM 15925 O  O2A   . DGI H 6 .   ? 104.382 150.113 86.968  1.00 66.08 ?  804 DGI A O2A   1 
HETATM 15926 O  "O5'" . DGI H 6 .   ? 106.892 150.119 86.985  1.00 64.30 ?  804 DGI A "O5'" 1 
HETATM 15927 C  "C5'" . DGI H 6 .   ? 108.160 150.748 86.708  1.00 63.95 ?  804 DGI A "C5'" 1 
HETATM 15928 C  "C4'" . DGI H 6 .   ? 109.270 149.770 86.998  1.00 63.55 ?  804 DGI A "C4'" 1 
HETATM 15929 O  "O4'" . DGI H 6 .   ? 109.190 149.340 88.376  1.00 62.06 ?  804 DGI A "O4'" 1 
HETATM 15930 C  "C3'" . DGI H 6 .   ? 109.254 148.500 86.139  1.00 64.87 ?  804 DGI A "C3'" 1 
HETATM 15931 O  "O3'" . DGI H 6 .   ? 110.560 148.230 85.629  1.00 62.86 ?  804 DGI A "O3'" 1 
HETATM 15932 C  "C2'" . DGI H 6 .   ? 108.824 147.413 87.117  1.00 62.93 ?  804 DGI A "C2'" 1 
HETATM 15933 C  "C1'" . DGI H 6 .   ? 109.351 147.939 88.436  1.00 59.66 ?  804 DGI A "C1'" 1 
HETATM 15934 N  N9    . DGI H 6 .   ? 108.624 147.443 89.620  1.00 62.34 ?  804 DGI A N9    1 
HETATM 15935 C  C8    . DGI H 6 .   ? 109.157 146.819 90.716  1.00 63.25 ?  804 DGI A C8    1 
HETATM 15936 N  N7    . DGI H 6 .   ? 108.257 146.475 91.606  1.00 62.94 ?  804 DGI A N7    1 
HETATM 15937 C  C5    . DGI H 6 .   ? 107.057 146.900 91.062  1.00 64.85 ?  804 DGI A C5    1 
HETATM 15938 C  C4    . DGI H 6 .   ? 107.266 147.499 89.838  1.00 64.28 ?  804 DGI A C4    1 
HETATM 15939 N  N3    . DGI H 6 .   ? 106.355 148.038 89.009  1.00 64.32 ?  804 DGI A N3    1 
HETATM 15940 C  C2    . DGI H 6 .   ? 105.115 147.952 89.483  1.00 62.71 ?  804 DGI A C2    1 
HETATM 15941 N  N2    . DGI H 6 .   ? 104.099 148.445 88.773  1.00 63.01 ?  804 DGI A N2    1 
HETATM 15942 N  N1    . DGI H 6 .   ? 104.807 147.375 90.686  1.00 63.42 ?  804 DGI A N1    1 
HETATM 15943 C  C6    . DGI H 6 .   ? 105.721 146.814 91.557  1.00 64.23 ?  804 DGI A C6    1 
HETATM 15944 O  O6    . DGI H 6 .   ? 105.350 146.314 92.619  1.00 64.17 ?  804 DGI A O6    1 
HETATM 15945 P  PA    . TTP I 3 .   ? 119.631 146.683 124.211 1.00 22.87 ?  801 TTP B PA    1 
HETATM 15946 O  O1A   . TTP I 3 .   ? 120.993 146.191 123.797 1.00 21.90 -1 801 TTP B O1A   1 
HETATM 15947 O  O2A   . TTP I 3 .   ? 119.714 148.081 124.768 1.00 27.07 ?  801 TTP B O2A   1 
HETATM 15948 O  O3A   . TTP I 3 .   ? 118.586 146.626 122.991 1.00 36.80 ?  801 TTP B O3A   1 
HETATM 15949 P  PB    . TTP I 3 .   ? 118.563 147.731 121.824 1.00 32.44 ?  801 TTP B PB    1 
HETATM 15950 O  O1B   . TTP I 3 .   ? 119.396 147.289 120.650 1.00 35.04 -1 801 TTP B O1B   1 
HETATM 15951 O  O2B   . TTP I 3 .   ? 119.012 149.084 122.311 1.00 28.12 ?  801 TTP B O2B   1 
HETATM 15952 O  O3B   . TTP I 3 .   ? 117.005 147.758 121.435 1.00 37.21 ?  801 TTP B O3B   1 
HETATM 15953 P  PG    . TTP I 3 .   ? 115.898 148.031 122.570 1.00 30.08 ?  801 TTP B PG    1 
HETATM 15954 O  O1G   . TTP I 3 .   ? 115.412 146.708 123.101 1.00 20.36 ?  801 TTP B O1G   1 
HETATM 15955 O  O2G   . TTP I 3 .   ? 114.726 148.777 121.984 1.00 33.83 -1 801 TTP B O2G   1 
HETATM 15956 O  O3G   . TTP I 3 .   ? 116.505 148.833 123.696 1.00 27.09 ?  801 TTP B O3G   1 
HETATM 15957 O  "O5'" . TTP I 3 .   ? 118.955 145.686 125.273 1.00 24.10 ?  801 TTP B "O5'" 1 
HETATM 15958 C  "C5'" . TTP I 3 .   ? 118.204 144.569 124.812 1.00 22.09 ?  801 TTP B "C5'" 1 
HETATM 15959 C  "C4'" . TTP I 3 .   ? 118.084 143.545 125.928 1.00 23.21 ?  801 TTP B "C4'" 1 
HETATM 15960 O  "O4'" . TTP I 3 .   ? 118.147 142.248 125.338 1.00 35.77 ?  801 TTP B "O4'" 1 
HETATM 15961 C  "C3'" . TTP I 3 .   ? 119.239 143.672 126.902 1.00 25.49 ?  801 TTP B "C3'" 1 
HETATM 15962 O  "O3'" . TTP I 3 .   ? 118.742 143.810 128.234 1.00 27.76 ?  801 TTP B "O3'" 1 
HETATM 15963 C  "C2'" . TTP I 3 .   ? 120.032 142.389 126.788 1.00 25.02 ?  801 TTP B "C2'" 1 
HETATM 15964 C  "C1'" . TTP I 3 .   ? 119.231 141.483 125.866 1.00 28.60 ?  801 TTP B "C1'" 1 
HETATM 15965 N  N1    . TTP I 3 .   ? 120.068 141.012 124.765 1.00 27.06 ?  801 TTP B N1    1 
HETATM 15966 C  C2    . TTP I 3 .   ? 120.192 139.626 124.522 1.00 29.68 ?  801 TTP B C2    1 
HETATM 15967 O  O2    . TTP I 3 .   ? 119.584 138.819 125.255 1.00 27.86 ?  801 TTP B O2    1 
HETATM 15968 N  N3    . TTP I 3 .   ? 120.949 139.160 123.522 1.00 27.67 ?  801 TTP B N3    1 
HETATM 15969 C  C4    . TTP I 3 .   ? 121.610 140.001 122.723 1.00 32.29 ?  801 TTP B C4    1 
HETATM 15970 O  O4    . TTP I 3 .   ? 122.315 139.565 121.790 1.00 35.26 ?  801 TTP B O4    1 
HETATM 15971 C  C5    . TTP I 3 .   ? 121.495 141.460 122.958 1.00 27.29 ?  801 TTP B C5    1 
HETATM 15972 C  C5M   . TTP I 3 .   ? 122.223 142.440 122.081 1.00 27.10 ?  801 TTP B C5M   1 
HETATM 15973 C  C6    . TTP I 3 .   ? 120.703 141.905 124.002 1.00 25.61 ?  801 TTP B C6    1 
HETATM 15974 MG MG    . MG  J 4 .   ? 117.909 149.537 125.095 1.00 27.32 ?  802 MG  B MG    1 
HETATM 15975 P  PG    . ATP K 5 .   ? 154.755 138.023 179.709 1.00 78.28 ?  803 ATP B PG    1 
HETATM 15976 O  O1G   . ATP K 5 .   ? 154.534 138.530 181.093 1.00 64.48 ?  803 ATP B O1G   1 
HETATM 15977 O  O2G   . ATP K 5 .   ? 153.467 137.893 178.889 1.00 66.98 -1 803 ATP B O2G   1 
HETATM 15978 O  O3G   . ATP K 5 .   ? 155.776 138.838 178.909 1.00 64.37 ?  803 ATP B O3G   1 
HETATM 15979 P  PB    . ATP K 5 .   ? 156.708 135.793 180.119 1.00 74.62 ?  803 ATP B PB    1 
HETATM 15980 O  O1B   . ATP K 5 .   ? 157.854 136.290 179.332 1.00 63.94 -1 803 ATP B O1B   1 
HETATM 15981 O  O2B   . ATP K 5 .   ? 156.859 135.872 181.638 1.00 65.48 ?  803 ATP B O2B   1 
HETATM 15982 O  O3B   . ATP K 5 .   ? 155.360 136.545 179.742 1.00 67.90 ?  803 ATP B O3B   1 
HETATM 15983 P  PA    . ATP K 5 .   ? 155.593 133.524 178.585 1.00 74.99 ?  803 ATP B PA    1 
HETATM 15984 O  O1A   . ATP K 5 .   ? 154.239 133.108 179.003 1.00 65.28 -1 803 ATP B O1A   1 
HETATM 15985 O  O2A   . ATP K 5 .   ? 156.507 132.389 178.128 1.00 66.62 ?  803 ATP B O2A   1 
HETATM 15986 O  O3A   . ATP K 5 .   ? 156.348 134.286 179.758 1.00 66.93 ?  803 ATP B O3A   1 
HETATM 15987 O  "O5'" . ATP K 5 .   ? 155.534 134.606 177.438 1.00 63.34 ?  803 ATP B "O5'" 1 
HETATM 15988 C  "C5'" . ATP K 5 .   ? 156.582 134.710 176.452 1.00 62.23 ?  803 ATP B "C5'" 1 
HETATM 15989 C  "C4'" . ATP K 5 .   ? 156.116 135.611 175.338 1.00 64.37 ?  803 ATP B "C4'" 1 
HETATM 15990 O  "O4'" . ATP K 5 .   ? 155.356 134.842 174.381 1.00 66.78 ?  803 ATP B "O4'" 1 
HETATM 15991 C  "C3'" . ATP K 5 .   ? 155.190 136.745 175.762 1.00 61.93 ?  803 ATP B "C3'" 1 
HETATM 15992 O  "O3'" . ATP K 5 .   ? 155.934 137.887 176.167 1.00 65.20 ?  803 ATP B "O3'" 1 
HETATM 15993 C  "C2'" . ATP K 5 .   ? 154.400 137.016 174.481 1.00 61.89 ?  803 ATP B "C2'" 1 
HETATM 15994 O  "O2'" . ATP K 5 .   ? 155.117 137.858 173.587 1.00 64.23 ?  803 ATP B "O2'" 1 
HETATM 15995 C  "C1'" . ATP K 5 .   ? 154.264 135.607 173.895 1.00 63.64 ?  803 ATP B "C1'" 1 
HETATM 15996 N  N9    . ATP K 5 .   ? 153.026 134.924 174.254 1.00 61.39 ?  803 ATP B N9    1 
HETATM 15997 C  C8    . ATP K 5 .   ? 152.894 133.766 174.975 1.00 60.31 ?  803 ATP B C8    1 
HETATM 15998 N  N7    . ATP K 5 .   ? 151.654 133.377 175.144 1.00 61.85 ?  803 ATP B N7    1 
HETATM 15999 C  C5    . ATP K 5 .   ? 150.914 134.347 174.485 1.00 64.90 ?  803 ATP B C5    1 
HETATM 16000 C  C6    . ATP K 5 .   ? 149.531 134.520 174.290 1.00 60.15 ?  803 ATP B C6    1 
HETATM 16001 N  N6    . ATP K 5 .   ? 148.602 133.683 174.762 1.00 59.38 ?  803 ATP B N6    1 
HETATM 16002 N  N1    . ATP K 5 .   ? 149.125 135.597 173.584 1.00 59.56 ?  803 ATP B N1    1 
HETATM 16003 C  C2    . ATP K 5 .   ? 150.045 136.441 173.112 1.00 58.45 ?  803 ATP B C2    1 
HETATM 16004 N  N3    . ATP K 5 .   ? 151.373 136.381 173.230 1.00 61.55 ?  803 ATP B N3    1 
HETATM 16005 C  C4    . ATP K 5 .   ? 151.747 135.307 173.931 1.00 64.32 ?  803 ATP B C4    1 
HETATM 16006 O  O1B   . DGI L 6 .   ? 162.317 153.037 173.788 1.00 62.73 -1 804 DGI B O1B   1 
HETATM 16007 P  PB    . DGI L 6 .   ? 162.544 151.561 173.528 1.00 78.16 ?  804 DGI B PB    1 
HETATM 16008 O  O2B   . DGI L 6 .   ? 163.987 151.229 173.221 1.00 66.34 ?  804 DGI B O2B   1 
HETATM 16009 O  O3B   . DGI L 6 .   ? 161.948 150.679 174.604 1.00 63.38 ?  804 DGI B O3B   1 
HETATM 16010 O  O3A   . DGI L 6 .   ? 161.763 151.202 172.145 1.00 65.58 ?  804 DGI B O3A   1 
HETATM 16011 P  PA    . DGI L 6 .   ? 161.787 150.166 170.926 1.00 72.25 ?  804 DGI B PA    1 
HETATM 16012 O  O1A   . DGI L 6 .   ? 162.640 149.013 171.297 1.00 65.11 ?  804 DGI B O1A   1 
HETATM 16013 O  O2A   . DGI L 6 .   ? 162.071 150.902 169.677 1.00 63.88 -1 804 DGI B O2A   1 
HETATM 16014 O  "O5'" . DGI L 6 .   ? 160.261 149.701 170.880 1.00 64.69 ?  804 DGI B "O5'" 1 
HETATM 16015 C  "C5'" . DGI L 6 .   ? 159.210 150.689 170.913 1.00 61.37 ?  804 DGI B "C5'" 1 
HETATM 16016 C  "C4'" . DGI L 6 .   ? 157.876 149.997 170.782 1.00 62.25 ?  804 DGI B "C4'" 1 
HETATM 16017 O  "O4'" . DGI L 6 .   ? 157.817 149.292 169.522 1.00 62.79 ?  804 DGI B "O4'" 1 
HETATM 16018 C  "C3'" . DGI L 6 .   ? 157.565 148.972 171.878 1.00 63.26 ?  804 DGI B "C3'" 1 
HETATM 16019 O  "O3'" . DGI L 6 .   ? 156.250 149.179 172.392 1.00 62.44 ?  804 DGI B "O3'" 1 
HETATM 16020 C  "C2'" . DGI L 6 .   ? 157.657 147.634 171.153 1.00 58.79 ?  804 DGI B "C2'" 1 
HETATM 16021 C  "C1'" . DGI L 6 .   ? 157.274 148.007 169.734 1.00 58.08 ?  804 DGI B "C1'" 1 
HETATM 16022 N  N9    . DGI L 6 .   ? 157.814 147.102 168.699 1.00 59.64 ?  804 DGI B N9    1 
HETATM 16023 C  C8    . DGI L 6 .   ? 157.111 146.471 167.709 1.00 62.54 ?  804 DGI B C8    1 
HETATM 16024 N  N7    . DGI L 6 .   ? 157.862 145.725 166.935 1.00 61.46 ?  804 DGI B N7    1 
HETATM 16025 C  C5    . DGI L 6 .   ? 159.139 145.873 167.447 1.00 64.08 ?  804 DGI B C5    1 
HETATM 16026 C  C4    . DGI L 6 .   ? 159.126 146.720 168.535 1.00 62.76 ?  804 DGI B C4    1 
HETATM 16027 N  N3    . DGI L 6 .   ? 160.164 147.108 169.299 1.00 63.02 ?  804 DGI B N3    1 
HETATM 16028 C  C2    . DGI L 6 .   ? 161.319 146.574 168.906 1.00 61.32 ?  804 DGI B C2    1 
HETATM 16029 N  N2    . DGI L 6 .   ? 162.440 146.861 169.572 1.00 62.38 ?  804 DGI B N2    1 
HETATM 16030 N  N1    . DGI L 6 .   ? 161.430 145.723 167.839 1.00 60.59 ?  804 DGI B N1    1 
HETATM 16031 C  C6    . DGI L 6 .   ? 160.384 145.309 167.038 1.00 62.82 ?  804 DGI B C6    1 
HETATM 16032 O  O6    . DGI L 6 .   ? 160.581 144.541 166.097 1.00 61.55 ?  804 DGI B O6    1 
HETATM 16033 MN MN    . MN  M 7 .   ? 120.759 94.287  121.364 0.85 25.05 ?  401 MN  C MN    1 
HETATM 16034 MN MN    . MN  N 7 .   ? 119.363 97.661  122.152 0.85 26.37 ?  402 MN  C MN    1 
HETATM 16035 MN MN    . MN  O 7 .   ? 139.103 100.575 135.698 1.00 22.51 ?  401 MN  D MN    1 
HETATM 16036 MN MN    . MN  P 7 .   ? 141.394 99.129  132.878 1.00 24.72 ?  402 MN  D MN    1 
# 
