data_9BYY
# 
_entry.id   9BYY 
# 
_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   9BYY         pdb_00009byy 10.2210/pdb9byy/pdb 
WWPDB D_1000284417 ?            ?                   
EMDB  EMD-45048    ?            ?                   
# 
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                        9BYY 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
EMDB .                                                                                            EMD-45037 'consensus EM volume'  
EMDB 'Class 9 model for turnover condition of Bacillus subtilis ribonucleotide reductase complex' EMD-45048 'associated EM volume' 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              nozomi.ando@cornell.edu 
_pdbx_contact_author.name_first         Nozomi 
_pdbx_contact_author.name_last          Ando 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7062-1644 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, D.'       1 0000-0002-3879-039X 
'Thomas, W.C.' 2 0000-0001-5490-4900 
'Burnim, A.A.' 3 0000-0002-9962-1397 
'Ando, N.'     4 0000-0001-7062-1644 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                2458 
_citation.page_last                 2458 
_citation.title                     
'Conformational landscapes of a class I ribonucleotide reductase complex during turnover reveal intrinsic dynamics and asymmetry.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-57735-4 
_citation.pdbx_database_id_PubMed   40075098 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Xu, D.'       1 ? 
primary 'Thomas, W.C.' 2 ? 
primary 'Burnim, A.A.' 3 ? 
primary 'Ando, N.'     4 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Ribonucleoside-diphosphate reductase subunit alpha' 80791.469 2 1.17.4.1 ? ? ? 
2 polymer     man 'Ribonucleoside-diphosphate reductase subunit beta'  40720.992 2 1.17.4.1 ? ? ? 
3 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"                          507.181   2 ?        ? ? ? 
4 non-polymer syn "GUANOSINE-5'-DIPHOSPHATE"                           443.201   2 ?        ? ? ? 
5 non-polymer syn "THYMIDINE-5'-TRIPHOSPHATE"                          482.168   2 ?        ? ? ? 
6 non-polymer syn 'MAGNESIUM ION'                                      24.305    2 ?        ? ? ? 
7 non-polymer syn 'MANGANESE (II) ION'                                 54.938    4 ?        ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Ribonucleotide reductase large subunit' 
2 'Ribonucleotide reductase small subunit' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MSQNQVPKWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTVFFHNLKEKLDYLVENQYYEEEFLSLYSFEDIKEV
FKTAYAKKFRFPSFMSAFKFYNDYALKTNDKKKILERYEDRISIVALFFANGDTEKAKEYVNLMINQEYQPSTPTFLNAG
RKRRGELVSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSKLRAKGEAIKDVENATKGVVGVMKLLDNAFRYADQM
GQRQGSGAAYLNIFHRDINDFLDTKKISADEDVRVKTLSIGVVIPDKFVELAREDKAAYVFYPHTIYKEYGQHMDEMDMN
EMYDKFVDNPRVKKEKINPRKLLEKLAMLRSESGYPYIMFQDNVNKVHANNHISKVKFSNLCSEVLQASQVSSYTDYDEE
DEIGLDISCNLGSLNILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVRRANKAMKSIGLGAMNLHGYLAQNGIAYE
SPEARDFANTFFMMVNFYSIQRSAEIAKEKGETFDQYEGSTYATGEYFDKYVSTDFSPKYEKIANLFEGMHIPTTEDWKK
LKAFVAEHGMYHSYRLCIAPTGSISYVQSSTASVMPIMERIEERTYGNSKTYYPMPGLASNNWFFYKEAYDMDMFKVVDM
IATIQQHIDQGISFTLFLKDTMTTRDLNRIDLYAHHRGIKTIYYARTKDTGQDSCLSCVV
;
;MSQNQVPKWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTVFFHNLKEKLDYLVENQYYEEEFLSLYSFEDIKEV
FKTAYAKKFRFPSFMSAFKFYNDYALKTNDKKKILERYEDRISIVALFFANGDTEKAKEYVNLMINQEYQPSTPTFLNAG
RKRRGELVSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSKLRAKGEAIKDVENATKGVVGVMKLLDNAFRYADQM
GQRQGSGAAYLNIFHRDINDFLDTKKISADEDVRVKTLSIGVVIPDKFVELAREDKAAYVFYPHTIYKEYGQHMDEMDMN
EMYDKFVDNPRVKKEKINPRKLLEKLAMLRSESGYPYIMFQDNVNKVHANNHISKVKFSNLCSEVLQASQVSSYTDYDEE
DEIGLDISCNLGSLNILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVRRANKAMKSIGLGAMNLHGYLAQNGIAYE
SPEARDFANTFFMMVNFYSIQRSAEIAKEKGETFDQYEGSTYATGEYFDKYVSTDFSPKYEKIANLFEGMHIPTTEDWKK
LKAFVAEHGMYHSYRLCIAPTGSISYVQSSTASVMPIMERIEERTYGNSKTYYPMPGLASNNWFFYKEAYDMDMFKVVDM
IATIQQHIDQGISFTLFLKDTMTTRDLNRIDLYAHHRGIKTIYYARTKDTGQDSCLSCVV
;
A,B ? 
2 'polypeptide(L)' no no 
;MGSSHHHHHHSSGLVPRGSHMMTKIYDAANWSKHEDDFTQMFYNQNVKQFWLPEEIALNGDLLTWKYLGKNEQDTYMKVL
AGLTLLDTEQGNTGMPIVAEHVDGHQRKAVLNFMAMMENAVHAKSYSNIFMTLAPTETINEVFEWVKQNKYLQKKAQMIV
GLYKAIQKDDEISLFKAMVASVYLESFLFYSGFYYPLYFYGQGKLMQSGEIINLILRDEAIHGVYVGLLAQEIYNKQTEE
KKAELREFAIDLLNQLYENELEYTEDLYDQVGLSHDVKKFIRYNANKALMNLGFDPYFEEEDINPIVLNGLNTKTKSHDF
FSMKGNGYKKATVEPLKDDDFYFEDEKEQI
;
;MGSSHHHHHHSSGLVPRGSHMMTKIYDAANWSKHEDDFTQMFYNQNVKQFWLPEEIALNGDLLTWKYLGKNEQDTYMKVL
AGLTLLDTEQGNTGMPIVAEHVDGHQRKAVLNFMAMMENAVHAKSYSNIFMTLAPTETINEVFEWVKQNKYLQKKAQMIV
GLYKAIQKDDEISLFKAMVASVYLESFLFYSGFYYPLYFYGQGKLMQSGEIINLILRDEAIHGVYVGLLAQEIYNKQTEE
KKAELREFAIDLLNQLYENELEYTEDLYDQVGLSHDVKKFIRYNANKALMNLGFDPYFEEEDINPIVLNGLNTKTKSHDF
FSMKGNGYKKATVEPLKDDDFYFEDEKEQI
;
C,D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
4 "GUANOSINE-5'-DIPHOSPHATE"  GDP 
5 "THYMIDINE-5'-TRIPHOSPHATE" TTP 
6 'MAGNESIUM ION'             MG  
7 'MANGANESE (II) ION'        MN  
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   GLN n 
1 4   ASN n 
1 5   GLN n 
1 6   VAL n 
1 7   PRO n 
1 8   LYS n 
1 9   TRP n 
1 10  ILE n 
1 11  GLN n 
1 12  LEU n 
1 13  ASN n 
1 14  ASN n 
1 15  GLU n 
1 16  ILE n 
1 17  MET n 
1 18  ILE n 
1 19  GLN n 
1 20  LYS n 
1 21  ASP n 
1 22  GLY n 
1 23  LYS n 
1 24  PHE n 
1 25  GLN n 
1 26  PHE n 
1 27  ASP n 
1 28  LYS n 
1 29  ASP n 
1 30  LYS n 
1 31  GLU n 
1 32  ALA n 
1 33  VAL n 
1 34  HIS n 
1 35  SER n 
1 36  TYR n 
1 37  PHE n 
1 38  VAL n 
1 39  ASP n 
1 40  TYR n 
1 41  ILE n 
1 42  ASN n 
1 43  GLN n 
1 44  ASN n 
1 45  THR n 
1 46  VAL n 
1 47  PHE n 
1 48  PHE n 
1 49  HIS n 
1 50  ASN n 
1 51  LEU n 
1 52  LYS n 
1 53  GLU n 
1 54  LYS n 
1 55  LEU n 
1 56  ASP n 
1 57  TYR n 
1 58  LEU n 
1 59  VAL n 
1 60  GLU n 
1 61  ASN n 
1 62  GLN n 
1 63  TYR n 
1 64  TYR n 
1 65  GLU n 
1 66  GLU n 
1 67  GLU n 
1 68  PHE n 
1 69  LEU n 
1 70  SER n 
1 71  LEU n 
1 72  TYR n 
1 73  SER n 
1 74  PHE n 
1 75  GLU n 
1 76  ASP n 
1 77  ILE n 
1 78  LYS n 
1 79  GLU n 
1 80  VAL n 
1 81  PHE n 
1 82  LYS n 
1 83  THR n 
1 84  ALA n 
1 85  TYR n 
1 86  ALA n 
1 87  LYS n 
1 88  LYS n 
1 89  PHE n 
1 90  ARG n 
1 91  PHE n 
1 92  PRO n 
1 93  SER n 
1 94  PHE n 
1 95  MET n 
1 96  SER n 
1 97  ALA n 
1 98  PHE n 
1 99  LYS n 
1 100 PHE n 
1 101 TYR n 
1 102 ASN n 
1 103 ASP n 
1 104 TYR n 
1 105 ALA n 
1 106 LEU n 
1 107 LYS n 
1 108 THR n 
1 109 ASN n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 ILE n 
1 115 LEU n 
1 116 GLU n 
1 117 ARG n 
1 118 TYR n 
1 119 GLU n 
1 120 ASP n 
1 121 ARG n 
1 122 ILE n 
1 123 SER n 
1 124 ILE n 
1 125 VAL n 
1 126 ALA n 
1 127 LEU n 
1 128 PHE n 
1 129 PHE n 
1 130 ALA n 
1 131 ASN n 
1 132 GLY n 
1 133 ASP n 
1 134 THR n 
1 135 GLU n 
1 136 LYS n 
1 137 ALA n 
1 138 LYS n 
1 139 GLU n 
1 140 TYR n 
1 141 VAL n 
1 142 ASN n 
1 143 LEU n 
1 144 MET n 
1 145 ILE n 
1 146 ASN n 
1 147 GLN n 
1 148 GLU n 
1 149 TYR n 
1 150 GLN n 
1 151 PRO n 
1 152 SER n 
1 153 THR n 
1 154 PRO n 
1 155 THR n 
1 156 PHE n 
1 157 LEU n 
1 158 ASN n 
1 159 ALA n 
1 160 GLY n 
1 161 ARG n 
1 162 LYS n 
1 163 ARG n 
1 164 ARG n 
1 165 GLY n 
1 166 GLU n 
1 167 LEU n 
1 168 VAL n 
1 169 SER n 
1 170 CYS n 
1 171 PHE n 
1 172 LEU n 
1 173 LEU n 
1 174 GLU n 
1 175 VAL n 
1 176 ASN n 
1 177 ASP n 
1 178 SER n 
1 179 LEU n 
1 180 ASN n 
1 181 ASP n 
1 182 ILE n 
1 183 SER n 
1 184 ARG n 
1 185 ALA n 
1 186 ILE n 
1 187 ASP n 
1 188 ILE n 
1 189 SER n 
1 190 MET n 
1 191 GLN n 
1 192 LEU n 
1 193 SER n 
1 194 LYS n 
1 195 LEU n 
1 196 GLY n 
1 197 GLY n 
1 198 GLY n 
1 199 VAL n 
1 200 SER n 
1 201 LEU n 
1 202 ASN n 
1 203 LEU n 
1 204 SER n 
1 205 LYS n 
1 206 LEU n 
1 207 ARG n 
1 208 ALA n 
1 209 LYS n 
1 210 GLY n 
1 211 GLU n 
1 212 ALA n 
1 213 ILE n 
1 214 LYS n 
1 215 ASP n 
1 216 VAL n 
1 217 GLU n 
1 218 ASN n 
1 219 ALA n 
1 220 THR n 
1 221 LYS n 
1 222 GLY n 
1 223 VAL n 
1 224 VAL n 
1 225 GLY n 
1 226 VAL n 
1 227 MET n 
1 228 LYS n 
1 229 LEU n 
1 230 LEU n 
1 231 ASP n 
1 232 ASN n 
1 233 ALA n 
1 234 PHE n 
1 235 ARG n 
1 236 TYR n 
1 237 ALA n 
1 238 ASP n 
1 239 GLN n 
1 240 MET n 
1 241 GLY n 
1 242 GLN n 
1 243 ARG n 
1 244 GLN n 
1 245 GLY n 
1 246 SER n 
1 247 GLY n 
1 248 ALA n 
1 249 ALA n 
1 250 TYR n 
1 251 LEU n 
1 252 ASN n 
1 253 ILE n 
1 254 PHE n 
1 255 HIS n 
1 256 ARG n 
1 257 ASP n 
1 258 ILE n 
1 259 ASN n 
1 260 ASP n 
1 261 PHE n 
1 262 LEU n 
1 263 ASP n 
1 264 THR n 
1 265 LYS n 
1 266 LYS n 
1 267 ILE n 
1 268 SER n 
1 269 ALA n 
1 270 ASP n 
1 271 GLU n 
1 272 ASP n 
1 273 VAL n 
1 274 ARG n 
1 275 VAL n 
1 276 LYS n 
1 277 THR n 
1 278 LEU n 
1 279 SER n 
1 280 ILE n 
1 281 GLY n 
1 282 VAL n 
1 283 VAL n 
1 284 ILE n 
1 285 PRO n 
1 286 ASP n 
1 287 LYS n 
1 288 PHE n 
1 289 VAL n 
1 290 GLU n 
1 291 LEU n 
1 292 ALA n 
1 293 ARG n 
1 294 GLU n 
1 295 ASP n 
1 296 LYS n 
1 297 ALA n 
1 298 ALA n 
1 299 TYR n 
1 300 VAL n 
1 301 PHE n 
1 302 TYR n 
1 303 PRO n 
1 304 HIS n 
1 305 THR n 
1 306 ILE n 
1 307 TYR n 
1 308 LYS n 
1 309 GLU n 
1 310 TYR n 
1 311 GLY n 
1 312 GLN n 
1 313 HIS n 
1 314 MET n 
1 315 ASP n 
1 316 GLU n 
1 317 MET n 
1 318 ASP n 
1 319 MET n 
1 320 ASN n 
1 321 GLU n 
1 322 MET n 
1 323 TYR n 
1 324 ASP n 
1 325 LYS n 
1 326 PHE n 
1 327 VAL n 
1 328 ASP n 
1 329 ASN n 
1 330 PRO n 
1 331 ARG n 
1 332 VAL n 
1 333 LYS n 
1 334 LYS n 
1 335 GLU n 
1 336 LYS n 
1 337 ILE n 
1 338 ASN n 
1 339 PRO n 
1 340 ARG n 
1 341 LYS n 
1 342 LEU n 
1 343 LEU n 
1 344 GLU n 
1 345 LYS n 
1 346 LEU n 
1 347 ALA n 
1 348 MET n 
1 349 LEU n 
1 350 ARG n 
1 351 SER n 
1 352 GLU n 
1 353 SER n 
1 354 GLY n 
1 355 TYR n 
1 356 PRO n 
1 357 TYR n 
1 358 ILE n 
1 359 MET n 
1 360 PHE n 
1 361 GLN n 
1 362 ASP n 
1 363 ASN n 
1 364 VAL n 
1 365 ASN n 
1 366 LYS n 
1 367 VAL n 
1 368 HIS n 
1 369 ALA n 
1 370 ASN n 
1 371 ASN n 
1 372 HIS n 
1 373 ILE n 
1 374 SER n 
1 375 LYS n 
1 376 VAL n 
1 377 LYS n 
1 378 PHE n 
1 379 SER n 
1 380 ASN n 
1 381 LEU n 
1 382 CYS n 
1 383 SER n 
1 384 GLU n 
1 385 VAL n 
1 386 LEU n 
1 387 GLN n 
1 388 ALA n 
1 389 SER n 
1 390 GLN n 
1 391 VAL n 
1 392 SER n 
1 393 SER n 
1 394 TYR n 
1 395 THR n 
1 396 ASP n 
1 397 TYR n 
1 398 ASP n 
1 399 GLU n 
1 400 GLU n 
1 401 ASP n 
1 402 GLU n 
1 403 ILE n 
1 404 GLY n 
1 405 LEU n 
1 406 ASP n 
1 407 ILE n 
1 408 SER n 
1 409 CYS n 
1 410 ASN n 
1 411 LEU n 
1 412 GLY n 
1 413 SER n 
1 414 LEU n 
1 415 ASN n 
1 416 ILE n 
1 417 LEU n 
1 418 ASN n 
1 419 VAL n 
1 420 MET n 
1 421 GLU n 
1 422 HIS n 
1 423 LYS n 
1 424 SER n 
1 425 ILE n 
1 426 GLU n 
1 427 LYS n 
1 428 THR n 
1 429 VAL n 
1 430 LYS n 
1 431 LEU n 
1 432 ALA n 
1 433 THR n 
1 434 ASP n 
1 435 SER n 
1 436 LEU n 
1 437 THR n 
1 438 HIS n 
1 439 VAL n 
1 440 SER n 
1 441 GLU n 
1 442 THR n 
1 443 THR n 
1 444 ASP n 
1 445 ILE n 
1 446 ARG n 
1 447 ASN n 
1 448 ALA n 
1 449 PRO n 
1 450 ALA n 
1 451 VAL n 
1 452 ARG n 
1 453 ARG n 
1 454 ALA n 
1 455 ASN n 
1 456 LYS n 
1 457 ALA n 
1 458 MET n 
1 459 LYS n 
1 460 SER n 
1 461 ILE n 
1 462 GLY n 
1 463 LEU n 
1 464 GLY n 
1 465 ALA n 
1 466 MET n 
1 467 ASN n 
1 468 LEU n 
1 469 HIS n 
1 470 GLY n 
1 471 TYR n 
1 472 LEU n 
1 473 ALA n 
1 474 GLN n 
1 475 ASN n 
1 476 GLY n 
1 477 ILE n 
1 478 ALA n 
1 479 TYR n 
1 480 GLU n 
1 481 SER n 
1 482 PRO n 
1 483 GLU n 
1 484 ALA n 
1 485 ARG n 
1 486 ASP n 
1 487 PHE n 
1 488 ALA n 
1 489 ASN n 
1 490 THR n 
1 491 PHE n 
1 492 PHE n 
1 493 MET n 
1 494 MET n 
1 495 VAL n 
1 496 ASN n 
1 497 PHE n 
1 498 TYR n 
1 499 SER n 
1 500 ILE n 
1 501 GLN n 
1 502 ARG n 
1 503 SER n 
1 504 ALA n 
1 505 GLU n 
1 506 ILE n 
1 507 ALA n 
1 508 LYS n 
1 509 GLU n 
1 510 LYS n 
1 511 GLY n 
1 512 GLU n 
1 513 THR n 
1 514 PHE n 
1 515 ASP n 
1 516 GLN n 
1 517 TYR n 
1 518 GLU n 
1 519 GLY n 
1 520 SER n 
1 521 THR n 
1 522 TYR n 
1 523 ALA n 
1 524 THR n 
1 525 GLY n 
1 526 GLU n 
1 527 TYR n 
1 528 PHE n 
1 529 ASP n 
1 530 LYS n 
1 531 TYR n 
1 532 VAL n 
1 533 SER n 
1 534 THR n 
1 535 ASP n 
1 536 PHE n 
1 537 SER n 
1 538 PRO n 
1 539 LYS n 
1 540 TYR n 
1 541 GLU n 
1 542 LYS n 
1 543 ILE n 
1 544 ALA n 
1 545 ASN n 
1 546 LEU n 
1 547 PHE n 
1 548 GLU n 
1 549 GLY n 
1 550 MET n 
1 551 HIS n 
1 552 ILE n 
1 553 PRO n 
1 554 THR n 
1 555 THR n 
1 556 GLU n 
1 557 ASP n 
1 558 TRP n 
1 559 LYS n 
1 560 LYS n 
1 561 LEU n 
1 562 LYS n 
1 563 ALA n 
1 564 PHE n 
1 565 VAL n 
1 566 ALA n 
1 567 GLU n 
1 568 HIS n 
1 569 GLY n 
1 570 MET n 
1 571 TYR n 
1 572 HIS n 
1 573 SER n 
1 574 TYR n 
1 575 ARG n 
1 576 LEU n 
1 577 CYS n 
1 578 ILE n 
1 579 ALA n 
1 580 PRO n 
1 581 THR n 
1 582 GLY n 
1 583 SER n 
1 584 ILE n 
1 585 SER n 
1 586 TYR n 
1 587 VAL n 
1 588 GLN n 
1 589 SER n 
1 590 SER n 
1 591 THR n 
1 592 ALA n 
1 593 SER n 
1 594 VAL n 
1 595 MET n 
1 596 PRO n 
1 597 ILE n 
1 598 MET n 
1 599 GLU n 
1 600 ARG n 
1 601 ILE n 
1 602 GLU n 
1 603 GLU n 
1 604 ARG n 
1 605 THR n 
1 606 TYR n 
1 607 GLY n 
1 608 ASN n 
1 609 SER n 
1 610 LYS n 
1 611 THR n 
1 612 TYR n 
1 613 TYR n 
1 614 PRO n 
1 615 MET n 
1 616 PRO n 
1 617 GLY n 
1 618 LEU n 
1 619 ALA n 
1 620 SER n 
1 621 ASN n 
1 622 ASN n 
1 623 TRP n 
1 624 PHE n 
1 625 PHE n 
1 626 TYR n 
1 627 LYS n 
1 628 GLU n 
1 629 ALA n 
1 630 TYR n 
1 631 ASP n 
1 632 MET n 
1 633 ASP n 
1 634 MET n 
1 635 PHE n 
1 636 LYS n 
1 637 VAL n 
1 638 VAL n 
1 639 ASP n 
1 640 MET n 
1 641 ILE n 
1 642 ALA n 
1 643 THR n 
1 644 ILE n 
1 645 GLN n 
1 646 GLN n 
1 647 HIS n 
1 648 ILE n 
1 649 ASP n 
1 650 GLN n 
1 651 GLY n 
1 652 ILE n 
1 653 SER n 
1 654 PHE n 
1 655 THR n 
1 656 LEU n 
1 657 PHE n 
1 658 LEU n 
1 659 LYS n 
1 660 ASP n 
1 661 THR n 
1 662 MET n 
1 663 THR n 
1 664 THR n 
1 665 ARG n 
1 666 ASP n 
1 667 LEU n 
1 668 ASN n 
1 669 ARG n 
1 670 ILE n 
1 671 ASP n 
1 672 LEU n 
1 673 TYR n 
1 674 ALA n 
1 675 HIS n 
1 676 HIS n 
1 677 ARG n 
1 678 GLY n 
1 679 ILE n 
1 680 LYS n 
1 681 THR n 
1 682 ILE n 
1 683 TYR n 
1 684 TYR n 
1 685 ALA n 
1 686 ARG n 
1 687 THR n 
1 688 LYS n 
1 689 ASP n 
1 690 THR n 
1 691 GLY n 
1 692 GLN n 
1 693 ASP n 
1 694 SER n 
1 695 CYS n 
1 696 LEU n 
1 697 SER n 
1 698 CYS n 
1 699 VAL n 
1 700 VAL n 
2 1   MET n 
2 2   GLY n 
2 3   SER n 
2 4   SER n 
2 5   HIS n 
2 6   HIS n 
2 7   HIS n 
2 8   HIS n 
2 9   HIS n 
2 10  HIS n 
2 11  SER n 
2 12  SER n 
2 13  GLY n 
2 14  LEU n 
2 15  VAL n 
2 16  PRO n 
2 17  ARG n 
2 18  GLY n 
2 19  SER n 
2 20  HIS n 
2 21  MET n 
2 22  MET n 
2 23  THR n 
2 24  LYS n 
2 25  ILE n 
2 26  TYR n 
2 27  ASP n 
2 28  ALA n 
2 29  ALA n 
2 30  ASN n 
2 31  TRP n 
2 32  SER n 
2 33  LYS n 
2 34  HIS n 
2 35  GLU n 
2 36  ASP n 
2 37  ASP n 
2 38  PHE n 
2 39  THR n 
2 40  GLN n 
2 41  MET n 
2 42  PHE n 
2 43  TYR n 
2 44  ASN n 
2 45  GLN n 
2 46  ASN n 
2 47  VAL n 
2 48  LYS n 
2 49  GLN n 
2 50  PHE n 
2 51  TRP n 
2 52  LEU n 
2 53  PRO n 
2 54  GLU n 
2 55  GLU n 
2 56  ILE n 
2 57  ALA n 
2 58  LEU n 
2 59  ASN n 
2 60  GLY n 
2 61  ASP n 
2 62  LEU n 
2 63  LEU n 
2 64  THR n 
2 65  TRP n 
2 66  LYS n 
2 67  TYR n 
2 68  LEU n 
2 69  GLY n 
2 70  LYS n 
2 71  ASN n 
2 72  GLU n 
2 73  GLN n 
2 74  ASP n 
2 75  THR n 
2 76  TYR n 
2 77  MET n 
2 78  LYS n 
2 79  VAL n 
2 80  LEU n 
2 81  ALA n 
2 82  GLY n 
2 83  LEU n 
2 84  THR n 
2 85  LEU n 
2 86  LEU n 
2 87  ASP n 
2 88  THR n 
2 89  GLU n 
2 90  GLN n 
2 91  GLY n 
2 92  ASN n 
2 93  THR n 
2 94  GLY n 
2 95  MET n 
2 96  PRO n 
2 97  ILE n 
2 98  VAL n 
2 99  ALA n 
2 100 GLU n 
2 101 HIS n 
2 102 VAL n 
2 103 ASP n 
2 104 GLY n 
2 105 HIS n 
2 106 GLN n 
2 107 ARG n 
2 108 LYS n 
2 109 ALA n 
2 110 VAL n 
2 111 LEU n 
2 112 ASN n 
2 113 PHE n 
2 114 MET n 
2 115 ALA n 
2 116 MET n 
2 117 MET n 
2 118 GLU n 
2 119 ASN n 
2 120 ALA n 
2 121 VAL n 
2 122 HIS n 
2 123 ALA n 
2 124 LYS n 
2 125 SER n 
2 126 TYR n 
2 127 SER n 
2 128 ASN n 
2 129 ILE n 
2 130 PHE n 
2 131 MET n 
2 132 THR n 
2 133 LEU n 
2 134 ALA n 
2 135 PRO n 
2 136 THR n 
2 137 GLU n 
2 138 THR n 
2 139 ILE n 
2 140 ASN n 
2 141 GLU n 
2 142 VAL n 
2 143 PHE n 
2 144 GLU n 
2 145 TRP n 
2 146 VAL n 
2 147 LYS n 
2 148 GLN n 
2 149 ASN n 
2 150 LYS n 
2 151 TYR n 
2 152 LEU n 
2 153 GLN n 
2 154 LYS n 
2 155 LYS n 
2 156 ALA n 
2 157 GLN n 
2 158 MET n 
2 159 ILE n 
2 160 VAL n 
2 161 GLY n 
2 162 LEU n 
2 163 TYR n 
2 164 LYS n 
2 165 ALA n 
2 166 ILE n 
2 167 GLN n 
2 168 LYS n 
2 169 ASP n 
2 170 ASP n 
2 171 GLU n 
2 172 ILE n 
2 173 SER n 
2 174 LEU n 
2 175 PHE n 
2 176 LYS n 
2 177 ALA n 
2 178 MET n 
2 179 VAL n 
2 180 ALA n 
2 181 SER n 
2 182 VAL n 
2 183 TYR n 
2 184 LEU n 
2 185 GLU n 
2 186 SER n 
2 187 PHE n 
2 188 LEU n 
2 189 PHE n 
2 190 TYR n 
2 191 SER n 
2 192 GLY n 
2 193 PHE n 
2 194 TYR n 
2 195 TYR n 
2 196 PRO n 
2 197 LEU n 
2 198 TYR n 
2 199 PHE n 
2 200 TYR n 
2 201 GLY n 
2 202 GLN n 
2 203 GLY n 
2 204 LYS n 
2 205 LEU n 
2 206 MET n 
2 207 GLN n 
2 208 SER n 
2 209 GLY n 
2 210 GLU n 
2 211 ILE n 
2 212 ILE n 
2 213 ASN n 
2 214 LEU n 
2 215 ILE n 
2 216 LEU n 
2 217 ARG n 
2 218 ASP n 
2 219 GLU n 
2 220 ALA n 
2 221 ILE n 
2 222 HIS n 
2 223 GLY n 
2 224 VAL n 
2 225 TYR n 
2 226 VAL n 
2 227 GLY n 
2 228 LEU n 
2 229 LEU n 
2 230 ALA n 
2 231 GLN n 
2 232 GLU n 
2 233 ILE n 
2 234 TYR n 
2 235 ASN n 
2 236 LYS n 
2 237 GLN n 
2 238 THR n 
2 239 GLU n 
2 240 GLU n 
2 241 LYS n 
2 242 LYS n 
2 243 ALA n 
2 244 GLU n 
2 245 LEU n 
2 246 ARG n 
2 247 GLU n 
2 248 PHE n 
2 249 ALA n 
2 250 ILE n 
2 251 ASP n 
2 252 LEU n 
2 253 LEU n 
2 254 ASN n 
2 255 GLN n 
2 256 LEU n 
2 257 TYR n 
2 258 GLU n 
2 259 ASN n 
2 260 GLU n 
2 261 LEU n 
2 262 GLU n 
2 263 TYR n 
2 264 THR n 
2 265 GLU n 
2 266 ASP n 
2 267 LEU n 
2 268 TYR n 
2 269 ASP n 
2 270 GLN n 
2 271 VAL n 
2 272 GLY n 
2 273 LEU n 
2 274 SER n 
2 275 HIS n 
2 276 ASP n 
2 277 VAL n 
2 278 LYS n 
2 279 LYS n 
2 280 PHE n 
2 281 ILE n 
2 282 ARG n 
2 283 TYR n 
2 284 ASN n 
2 285 ALA n 
2 286 ASN n 
2 287 LYS n 
2 288 ALA n 
2 289 LEU n 
2 290 MET n 
2 291 ASN n 
2 292 LEU n 
2 293 GLY n 
2 294 PHE n 
2 295 ASP n 
2 296 PRO n 
2 297 TYR n 
2 298 PHE n 
2 299 GLU n 
2 300 GLU n 
2 301 GLU n 
2 302 ASP n 
2 303 ILE n 
2 304 ASN n 
2 305 PRO n 
2 306 ILE n 
2 307 VAL n 
2 308 LEU n 
2 309 ASN n 
2 310 GLY n 
2 311 LEU n 
2 312 ASN n 
2 313 THR n 
2 314 LYS n 
2 315 THR n 
2 316 LYS n 
2 317 SER n 
2 318 HIS n 
2 319 ASP n 
2 320 PHE n 
2 321 PHE n 
2 322 SER n 
2 323 MET n 
2 324 LYS n 
2 325 GLY n 
2 326 ASN n 
2 327 GLY n 
2 328 TYR n 
2 329 LYS n 
2 330 LYS n 
2 331 ALA n 
2 332 THR n 
2 333 VAL n 
2 334 GLU n 
2 335 PRO n 
2 336 LEU n 
2 337 LYS n 
2 338 ASP n 
2 339 ASP n 
2 340 ASP n 
2 341 PHE n 
2 342 TYR n 
2 343 PHE n 
2 344 GLU n 
2 345 ASP n 
2 346 GLU n 
2 347 LYS n 
2 348 GLU n 
2 349 GLN n 
2 350 ILE n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 700 ? ? 'nrdE, nrdA, BSU17380' ? ? ? ? ? ? 'Bacillus subtilis' 1423 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 350 ? ? 'nrdF, BSU17390'       ? ? ? ? ? ? 'Bacillus subtilis' 1423 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                     ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                    ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ? 'C4 H7 N O4'        133.103 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
GDP 'RNA linking'       n "GUANOSINE-5'-DIPHOSPHATE"  ? 'C10 H15 N5 O11 P2' 443.201 
GLN 'L-peptide linking' y GLUTAMINE                   ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                     ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                   ? 'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE                  ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                     ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                      ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                  ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
MN  non-polymer         . 'MANGANESE (II) ION'        ? 'Mn 2'              54.938  
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TTP non-polymer         . "THYMIDINE-5'-TRIPHOSPHATE" ? 'C10 H17 N2 O14 P3' 482.168 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   GLN 3   3   ?   ?   ?   A . n 
A 1 4   ASN 4   4   ?   ?   ?   A . n 
A 1 5   GLN 5   5   ?   ?   ?   A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   PRO 7   7   7   PRO PRO A . n 
A 1 8   LYS 8   8   8   LYS LYS A . n 
A 1 9   TRP 9   9   9   TRP TRP A . n 
A 1 10  ILE 10  10  10  ILE ILE A . n 
A 1 11  GLN 11  11  11  GLN GLN A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  ASN 14  14  14  ASN ASN A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  PHE 24  24  24  PHE PHE A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  ASP 29  29  29  ASP ASP A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  GLU 31  31  31  GLU GLU A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  HIS 34  34  34  HIS HIS A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  TYR 36  36  36  TYR TYR A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ILE 41  41  41  ILE ILE A . n 
A 1 42  ASN 42  42  42  ASN ASN A . n 
A 1 43  GLN 43  43  43  GLN GLN A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  PHE 47  47  47  PHE PHE A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  HIS 49  49  49  HIS HIS A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  LYS 52  52  52  LYS LYS A . n 
A 1 53  GLU 53  53  53  GLU GLU A . n 
A 1 54  LYS 54  54  54  LYS LYS A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  TYR 57  57  57  TYR TYR A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  TYR 63  63  63  TYR TYR A . n 
A 1 64  TYR 64  64  64  TYR TYR A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  PHE 68  68  68  PHE PHE A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  TYR 72  72  72  TYR TYR A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  PHE 74  74  74  PHE PHE A . n 
A 1 75  GLU 75  75  75  GLU GLU A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  ILE 77  77  77  ILE ILE A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  GLU 79  79  79  GLU GLU A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  PHE 81  81  81  PHE PHE A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  THR 83  83  83  THR THR A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  PHE 89  89  89  PHE PHE A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  PHE 91  91  91  PHE PHE A . n 
A 1 92  PRO 92  92  92  PRO PRO A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  PHE 94  94  94  PHE PHE A . n 
A 1 95  MET 95  95  95  MET MET A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 PHE 100 100 100 PHE PHE A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 TYR 104 104 104 TYR TYR A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 ILE 114 114 114 ILE ILE A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 ARG 117 117 117 ARG ARG A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 GLU 119 119 119 GLU GLU A . n 
A 1 120 ASP 120 120 120 ASP ASP A . n 
A 1 121 ARG 121 121 121 ARG ARG A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 PHE 129 129 129 PHE PHE A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 ASP 133 133 133 ASP ASP A . n 
A 1 134 THR 134 134 134 THR THR A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 TYR 140 140 140 TYR TYR A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 MET 144 144 144 MET MET A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 ASN 146 146 146 ASN ASN A . n 
A 1 147 GLN 147 147 147 GLN GLN A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 TYR 149 149 149 TYR TYR A . n 
A 1 150 GLN 150 150 150 GLN GLN A . n 
A 1 151 PRO 151 151 151 PRO PRO A . n 
A 1 152 SER 152 152 152 SER SER A . n 
A 1 153 THR 153 153 153 THR THR A . n 
A 1 154 PRO 154 154 154 PRO PRO A . n 
A 1 155 THR 155 155 155 THR THR A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 ASN 158 158 158 ASN ASN A . n 
A 1 159 ALA 159 159 159 ALA ALA A . n 
A 1 160 GLY 160 160 160 GLY GLY A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 CYS 170 170 170 CYS CYS A . n 
A 1 171 PHE 171 171 171 PHE PHE A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 GLU 174 174 174 GLU GLU A . n 
A 1 175 VAL 175 175 175 VAL VAL A . n 
A 1 176 ASN 176 176 176 ASN ASN A . n 
A 1 177 ASP 177 177 177 ASP ASP A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 ASP 181 181 181 ASP ASP A . n 
A 1 182 ILE 182 182 182 ILE ILE A . n 
A 1 183 SER 183 183 183 SER SER A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ILE 188 188 188 ILE ILE A . n 
A 1 189 SER 189 189 189 SER SER A . n 
A 1 190 MET 190 190 190 MET MET A . n 
A 1 191 GLN 191 191 191 GLN GLN A . n 
A 1 192 LEU 192 192 192 LEU LEU A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 GLY 197 197 197 GLY GLY A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 SER 200 200 200 SER SER A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 ASN 202 202 202 ASN ASN A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 SER 204 204 204 SER SER A . n 
A 1 205 LYS 205 205 205 LYS LYS A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 ARG 207 207 207 ARG ARG A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 LYS 209 209 209 LYS LYS A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 GLU 211 211 211 GLU GLU A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 LYS 214 214 214 LYS LYS A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 GLU 217 217 217 GLU GLU A . n 
A 1 218 ASN 218 218 218 ASN ASN A . n 
A 1 219 ALA 219 219 219 ALA ALA A . n 
A 1 220 THR 220 220 220 THR THR A . n 
A 1 221 LYS 221 221 221 LYS LYS A . n 
A 1 222 GLY 222 222 222 GLY GLY A . n 
A 1 223 VAL 223 223 223 VAL VAL A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 GLY 225 225 225 GLY GLY A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 MET 227 227 227 MET MET A . n 
A 1 228 LYS 228 228 228 LYS LYS A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 ASP 231 231 231 ASP ASP A . n 
A 1 232 ASN 232 232 232 ASN ASN A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 PHE 234 234 234 PHE PHE A . n 
A 1 235 ARG 235 235 235 ARG ARG A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 GLN 239 239 239 GLN GLN A . n 
A 1 240 MET 240 240 240 MET MET A . n 
A 1 241 GLY 241 241 241 GLY GLY A . n 
A 1 242 GLN 242 242 242 GLN GLN A . n 
A 1 243 ARG 243 243 243 ARG ARG A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 GLY 245 245 245 GLY GLY A . n 
A 1 246 SER 246 246 246 SER SER A . n 
A 1 247 GLY 247 247 247 GLY GLY A . n 
A 1 248 ALA 248 248 248 ALA ALA A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 TYR 250 250 250 TYR TYR A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 ILE 253 253 253 ILE ILE A . n 
A 1 254 PHE 254 254 254 PHE PHE A . n 
A 1 255 HIS 255 255 255 HIS HIS A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 ASP 257 257 257 ASP ASP A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 ASN 259 259 259 ASN ASN A . n 
A 1 260 ASP 260 260 260 ASP ASP A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 THR 264 264 264 THR THR A . n 
A 1 265 LYS 265 265 265 LYS LYS A . n 
A 1 266 LYS 266 266 266 LYS LYS A . n 
A 1 267 ILE 267 267 267 ILE ILE A . n 
A 1 268 SER 268 268 268 SER SER A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 ASP 270 270 270 ASP ASP A . n 
A 1 271 GLU 271 271 271 GLU GLU A . n 
A 1 272 ASP 272 272 272 ASP ASP A . n 
A 1 273 VAL 273 273 273 VAL VAL A . n 
A 1 274 ARG 274 274 274 ARG ARG A . n 
A 1 275 VAL 275 275 275 VAL VAL A . n 
A 1 276 LYS 276 276 276 LYS LYS A . n 
A 1 277 THR 277 277 277 THR THR A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 SER 279 279 279 SER SER A . n 
A 1 280 ILE 280 280 280 ILE ILE A . n 
A 1 281 GLY 281 281 281 GLY GLY A . n 
A 1 282 VAL 282 282 282 VAL VAL A . n 
A 1 283 VAL 283 283 283 VAL VAL A . n 
A 1 284 ILE 284 284 284 ILE ILE A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 ASP 286 286 286 ASP ASP A . n 
A 1 287 LYS 287 287 287 LYS LYS A . n 
A 1 288 PHE 288 288 288 PHE PHE A . n 
A 1 289 VAL 289 289 289 VAL VAL A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 LEU 291 291 291 LEU LEU A . n 
A 1 292 ALA 292 292 292 ALA ALA A . n 
A 1 293 ARG 293 293 293 ARG ARG A . n 
A 1 294 GLU 294 294 294 GLU GLU A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 LYS 296 296 296 LYS LYS A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 ALA 298 298 298 ALA ALA A . n 
A 1 299 TYR 299 299 299 TYR TYR A . n 
A 1 300 VAL 300 300 300 VAL VAL A . n 
A 1 301 PHE 301 301 301 PHE PHE A . n 
A 1 302 TYR 302 302 302 TYR TYR A . n 
A 1 303 PRO 303 303 303 PRO PRO A . n 
A 1 304 HIS 304 304 304 HIS HIS A . n 
A 1 305 THR 305 305 305 THR THR A . n 
A 1 306 ILE 306 306 306 ILE ILE A . n 
A 1 307 TYR 307 307 307 TYR TYR A . n 
A 1 308 LYS 308 308 308 LYS LYS A . n 
A 1 309 GLU 309 309 309 GLU GLU A . n 
A 1 310 TYR 310 310 310 TYR TYR A . n 
A 1 311 GLY 311 311 311 GLY GLY A . n 
A 1 312 GLN 312 312 312 GLN GLN A . n 
A 1 313 HIS 313 313 313 HIS HIS A . n 
A 1 314 MET 314 314 314 MET MET A . n 
A 1 315 ASP 315 315 315 ASP ASP A . n 
A 1 316 GLU 316 316 316 GLU GLU A . n 
A 1 317 MET 317 317 317 MET MET A . n 
A 1 318 ASP 318 318 318 ASP ASP A . n 
A 1 319 MET 319 319 319 MET MET A . n 
A 1 320 ASN 320 320 320 ASN ASN A . n 
A 1 321 GLU 321 321 321 GLU GLU A . n 
A 1 322 MET 322 322 322 MET MET A . n 
A 1 323 TYR 323 323 323 TYR TYR A . n 
A 1 324 ASP 324 324 324 ASP ASP A . n 
A 1 325 LYS 325 325 325 LYS LYS A . n 
A 1 326 PHE 326 326 326 PHE PHE A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 ASP 328 328 328 ASP ASP A . n 
A 1 329 ASN 329 329 329 ASN ASN A . n 
A 1 330 PRO 330 330 330 PRO PRO A . n 
A 1 331 ARG 331 331 331 ARG ARG A . n 
A 1 332 VAL 332 332 332 VAL VAL A . n 
A 1 333 LYS 333 333 333 LYS LYS A . n 
A 1 334 LYS 334 334 334 LYS LYS A . n 
A 1 335 GLU 335 335 335 GLU GLU A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 ILE 337 337 337 ILE ILE A . n 
A 1 338 ASN 338 338 338 ASN ASN A . n 
A 1 339 PRO 339 339 339 PRO PRO A . n 
A 1 340 ARG 340 340 340 ARG ARG A . n 
A 1 341 LYS 341 341 341 LYS LYS A . n 
A 1 342 LEU 342 342 342 LEU LEU A . n 
A 1 343 LEU 343 343 343 LEU LEU A . n 
A 1 344 GLU 344 344 344 GLU GLU A . n 
A 1 345 LYS 345 345 345 LYS LYS A . n 
A 1 346 LEU 346 346 346 LEU LEU A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 MET 348 348 348 MET MET A . n 
A 1 349 LEU 349 349 349 LEU LEU A . n 
A 1 350 ARG 350 350 350 ARG ARG A . n 
A 1 351 SER 351 351 351 SER SER A . n 
A 1 352 GLU 352 352 352 GLU GLU A . n 
A 1 353 SER 353 353 353 SER SER A . n 
A 1 354 GLY 354 354 354 GLY GLY A . n 
A 1 355 TYR 355 355 355 TYR TYR A . n 
A 1 356 PRO 356 356 356 PRO PRO A . n 
A 1 357 TYR 357 357 357 TYR TYR A . n 
A 1 358 ILE 358 358 358 ILE ILE A . n 
A 1 359 MET 359 359 359 MET MET A . n 
A 1 360 PHE 360 360 360 PHE PHE A . n 
A 1 361 GLN 361 361 361 GLN GLN A . n 
A 1 362 ASP 362 362 362 ASP ASP A . n 
A 1 363 ASN 363 363 363 ASN ASN A . n 
A 1 364 VAL 364 364 364 VAL VAL A . n 
A 1 365 ASN 365 365 365 ASN ASN A . n 
A 1 366 LYS 366 366 366 LYS LYS A . n 
A 1 367 VAL 367 367 367 VAL VAL A . n 
A 1 368 HIS 368 368 368 HIS HIS A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 ASN 370 370 370 ASN ASN A . n 
A 1 371 ASN 371 371 371 ASN ASN A . n 
A 1 372 HIS 372 372 372 HIS HIS A . n 
A 1 373 ILE 373 373 373 ILE ILE A . n 
A 1 374 SER 374 374 374 SER SER A . n 
A 1 375 LYS 375 375 375 LYS LYS A . n 
A 1 376 VAL 376 376 376 VAL VAL A . n 
A 1 377 LYS 377 377 377 LYS LYS A . n 
A 1 378 PHE 378 378 378 PHE PHE A . n 
A 1 379 SER 379 379 379 SER SER A . n 
A 1 380 ASN 380 380 380 ASN ASN A . n 
A 1 381 LEU 381 381 381 LEU LEU A . n 
A 1 382 CYS 382 382 382 CYS CYS A . n 
A 1 383 SER 383 383 383 SER SER A . n 
A 1 384 GLU 384 384 384 GLU GLU A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 LEU 386 386 386 LEU LEU A . n 
A 1 387 GLN 387 387 387 GLN GLN A . n 
A 1 388 ALA 388 388 388 ALA ALA A . n 
A 1 389 SER 389 389 389 SER SER A . n 
A 1 390 GLN 390 390 390 GLN GLN A . n 
A 1 391 VAL 391 391 391 VAL VAL A . n 
A 1 392 SER 392 392 392 SER SER A . n 
A 1 393 SER 393 393 393 SER SER A . n 
A 1 394 TYR 394 394 394 TYR TYR A . n 
A 1 395 THR 395 395 395 THR THR A . n 
A 1 396 ASP 396 396 396 ASP ASP A . n 
A 1 397 TYR 397 397 397 TYR TYR A . n 
A 1 398 ASP 398 398 398 ASP ASP A . n 
A 1 399 GLU 399 399 399 GLU GLU A . n 
A 1 400 GLU 400 400 400 GLU GLU A . n 
A 1 401 ASP 401 401 401 ASP ASP A . n 
A 1 402 GLU 402 402 402 GLU GLU A . n 
A 1 403 ILE 403 403 403 ILE ILE A . n 
A 1 404 GLY 404 404 404 GLY GLY A . n 
A 1 405 LEU 405 405 405 LEU LEU A . n 
A 1 406 ASP 406 406 406 ASP ASP A . n 
A 1 407 ILE 407 407 407 ILE ILE A . n 
A 1 408 SER 408 408 408 SER SER A . n 
A 1 409 CYS 409 409 409 CYS CYS A . n 
A 1 410 ASN 410 410 410 ASN ASN A . n 
A 1 411 LEU 411 411 411 LEU LEU A . n 
A 1 412 GLY 412 412 412 GLY GLY A . n 
A 1 413 SER 413 413 413 SER SER A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 ASN 415 415 415 ASN ASN A . n 
A 1 416 ILE 416 416 416 ILE ILE A . n 
A 1 417 LEU 417 417 417 LEU LEU A . n 
A 1 418 ASN 418 418 418 ASN ASN A . n 
A 1 419 VAL 419 419 419 VAL VAL A . n 
A 1 420 MET 420 420 420 MET MET A . n 
A 1 421 GLU 421 421 421 GLU GLU A . n 
A 1 422 HIS 422 422 422 HIS HIS A . n 
A 1 423 LYS 423 423 423 LYS LYS A . n 
A 1 424 SER 424 424 424 SER SER A . n 
A 1 425 ILE 425 425 425 ILE ILE A . n 
A 1 426 GLU 426 426 426 GLU GLU A . n 
A 1 427 LYS 427 427 427 LYS LYS A . n 
A 1 428 THR 428 428 428 THR THR A . n 
A 1 429 VAL 429 429 429 VAL VAL A . n 
A 1 430 LYS 430 430 430 LYS LYS A . n 
A 1 431 LEU 431 431 431 LEU LEU A . n 
A 1 432 ALA 432 432 432 ALA ALA A . n 
A 1 433 THR 433 433 433 THR THR A . n 
A 1 434 ASP 434 434 434 ASP ASP A . n 
A 1 435 SER 435 435 435 SER SER A . n 
A 1 436 LEU 436 436 436 LEU LEU A . n 
A 1 437 THR 437 437 437 THR THR A . n 
A 1 438 HIS 438 438 438 HIS HIS A . n 
A 1 439 VAL 439 439 439 VAL VAL A . n 
A 1 440 SER 440 440 440 SER SER A . n 
A 1 441 GLU 441 441 441 GLU GLU A . n 
A 1 442 THR 442 442 442 THR THR A . n 
A 1 443 THR 443 443 443 THR THR A . n 
A 1 444 ASP 444 444 444 ASP ASP A . n 
A 1 445 ILE 445 445 445 ILE ILE A . n 
A 1 446 ARG 446 446 446 ARG ARG A . n 
A 1 447 ASN 447 447 447 ASN ASN A . n 
A 1 448 ALA 448 448 448 ALA ALA A . n 
A 1 449 PRO 449 449 449 PRO PRO A . n 
A 1 450 ALA 450 450 450 ALA ALA A . n 
A 1 451 VAL 451 451 451 VAL VAL A . n 
A 1 452 ARG 452 452 452 ARG ARG A . n 
A 1 453 ARG 453 453 453 ARG ARG A . n 
A 1 454 ALA 454 454 454 ALA ALA A . n 
A 1 455 ASN 455 455 455 ASN ASN A . n 
A 1 456 LYS 456 456 456 LYS LYS A . n 
A 1 457 ALA 457 457 457 ALA ALA A . n 
A 1 458 MET 458 458 458 MET MET A . n 
A 1 459 LYS 459 459 459 LYS LYS A . n 
A 1 460 SER 460 460 460 SER SER A . n 
A 1 461 ILE 461 461 461 ILE ILE A . n 
A 1 462 GLY 462 462 462 GLY GLY A . n 
A 1 463 LEU 463 463 463 LEU LEU A . n 
A 1 464 GLY 464 464 464 GLY GLY A . n 
A 1 465 ALA 465 465 465 ALA ALA A . n 
A 1 466 MET 466 466 466 MET MET A . n 
A 1 467 ASN 467 467 467 ASN ASN A . n 
A 1 468 LEU 468 468 468 LEU LEU A . n 
A 1 469 HIS 469 469 469 HIS HIS A . n 
A 1 470 GLY 470 470 470 GLY GLY A . n 
A 1 471 TYR 471 471 471 TYR TYR A . n 
A 1 472 LEU 472 472 472 LEU LEU A . n 
A 1 473 ALA 473 473 473 ALA ALA A . n 
A 1 474 GLN 474 474 474 GLN GLN A . n 
A 1 475 ASN 475 475 475 ASN ASN A . n 
A 1 476 GLY 476 476 476 GLY GLY A . n 
A 1 477 ILE 477 477 477 ILE ILE A . n 
A 1 478 ALA 478 478 478 ALA ALA A . n 
A 1 479 TYR 479 479 479 TYR TYR A . n 
A 1 480 GLU 480 480 480 GLU GLU A . n 
A 1 481 SER 481 481 481 SER SER A . n 
A 1 482 PRO 482 482 482 PRO PRO A . n 
A 1 483 GLU 483 483 483 GLU GLU A . n 
A 1 484 ALA 484 484 484 ALA ALA A . n 
A 1 485 ARG 485 485 485 ARG ARG A . n 
A 1 486 ASP 486 486 486 ASP ASP A . n 
A 1 487 PHE 487 487 487 PHE PHE A . n 
A 1 488 ALA 488 488 488 ALA ALA A . n 
A 1 489 ASN 489 489 489 ASN ASN A . n 
A 1 490 THR 490 490 490 THR THR A . n 
A 1 491 PHE 491 491 491 PHE PHE A . n 
A 1 492 PHE 492 492 492 PHE PHE A . n 
A 1 493 MET 493 493 493 MET MET A . n 
A 1 494 MET 494 494 494 MET MET A . n 
A 1 495 VAL 495 495 495 VAL VAL A . n 
A 1 496 ASN 496 496 496 ASN ASN A . n 
A 1 497 PHE 497 497 497 PHE PHE A . n 
A 1 498 TYR 498 498 498 TYR TYR A . n 
A 1 499 SER 499 499 499 SER SER A . n 
A 1 500 ILE 500 500 500 ILE ILE A . n 
A 1 501 GLN 501 501 501 GLN GLN A . n 
A 1 502 ARG 502 502 502 ARG ARG A . n 
A 1 503 SER 503 503 503 SER SER A . n 
A 1 504 ALA 504 504 504 ALA ALA A . n 
A 1 505 GLU 505 505 505 GLU GLU A . n 
A 1 506 ILE 506 506 506 ILE ILE A . n 
A 1 507 ALA 507 507 507 ALA ALA A . n 
A 1 508 LYS 508 508 508 LYS LYS A . n 
A 1 509 GLU 509 509 509 GLU GLU A . n 
A 1 510 LYS 510 510 510 LYS LYS A . n 
A 1 511 GLY 511 511 511 GLY GLY A . n 
A 1 512 GLU 512 512 512 GLU GLU A . n 
A 1 513 THR 513 513 513 THR THR A . n 
A 1 514 PHE 514 514 514 PHE PHE A . n 
A 1 515 ASP 515 515 515 ASP ASP A . n 
A 1 516 GLN 516 516 516 GLN GLN A . n 
A 1 517 TYR 517 517 517 TYR TYR A . n 
A 1 518 GLU 518 518 518 GLU GLU A . n 
A 1 519 GLY 519 519 519 GLY GLY A . n 
A 1 520 SER 520 520 520 SER SER A . n 
A 1 521 THR 521 521 521 THR THR A . n 
A 1 522 TYR 522 522 522 TYR TYR A . n 
A 1 523 ALA 523 523 523 ALA ALA A . n 
A 1 524 THR 524 524 524 THR THR A . n 
A 1 525 GLY 525 525 525 GLY GLY A . n 
A 1 526 GLU 526 526 526 GLU GLU A . n 
A 1 527 TYR 527 527 527 TYR TYR A . n 
A 1 528 PHE 528 528 528 PHE PHE A . n 
A 1 529 ASP 529 529 529 ASP ASP A . n 
A 1 530 LYS 530 530 530 LYS LYS A . n 
A 1 531 TYR 531 531 531 TYR TYR A . n 
A 1 532 VAL 532 532 532 VAL VAL A . n 
A 1 533 SER 533 533 533 SER SER A . n 
A 1 534 THR 534 534 534 THR THR A . n 
A 1 535 ASP 535 535 535 ASP ASP A . n 
A 1 536 PHE 536 536 536 PHE PHE A . n 
A 1 537 SER 537 537 537 SER SER A . n 
A 1 538 PRO 538 538 538 PRO PRO A . n 
A 1 539 LYS 539 539 539 LYS LYS A . n 
A 1 540 TYR 540 540 540 TYR TYR A . n 
A 1 541 GLU 541 541 541 GLU GLU A . n 
A 1 542 LYS 542 542 542 LYS LYS A . n 
A 1 543 ILE 543 543 543 ILE ILE A . n 
A 1 544 ALA 544 544 544 ALA ALA A . n 
A 1 545 ASN 545 545 545 ASN ASN A . n 
A 1 546 LEU 546 546 546 LEU LEU A . n 
A 1 547 PHE 547 547 547 PHE PHE A . n 
A 1 548 GLU 548 548 548 GLU GLU A . n 
A 1 549 GLY 549 549 549 GLY GLY A . n 
A 1 550 MET 550 550 550 MET MET A . n 
A 1 551 HIS 551 551 551 HIS HIS A . n 
A 1 552 ILE 552 552 552 ILE ILE A . n 
A 1 553 PRO 553 553 553 PRO PRO A . n 
A 1 554 THR 554 554 554 THR THR A . n 
A 1 555 THR 555 555 555 THR THR A . n 
A 1 556 GLU 556 556 556 GLU GLU A . n 
A 1 557 ASP 557 557 557 ASP ASP A . n 
A 1 558 TRP 558 558 558 TRP TRP A . n 
A 1 559 LYS 559 559 559 LYS LYS A . n 
A 1 560 LYS 560 560 560 LYS LYS A . n 
A 1 561 LEU 561 561 561 LEU LEU A . n 
A 1 562 LYS 562 562 562 LYS LYS A . n 
A 1 563 ALA 563 563 563 ALA ALA A . n 
A 1 564 PHE 564 564 564 PHE PHE A . n 
A 1 565 VAL 565 565 565 VAL VAL A . n 
A 1 566 ALA 566 566 566 ALA ALA A . n 
A 1 567 GLU 567 567 567 GLU GLU A . n 
A 1 568 HIS 568 568 568 HIS HIS A . n 
A 1 569 GLY 569 569 569 GLY GLY A . n 
A 1 570 MET 570 570 570 MET MET A . n 
A 1 571 TYR 571 571 571 TYR TYR A . n 
A 1 572 HIS 572 572 572 HIS HIS A . n 
A 1 573 SER 573 573 573 SER SER A . n 
A 1 574 TYR 574 574 574 TYR TYR A . n 
A 1 575 ARG 575 575 575 ARG ARG A . n 
A 1 576 LEU 576 576 576 LEU LEU A . n 
A 1 577 CYS 577 577 577 CYS CYS A . n 
A 1 578 ILE 578 578 578 ILE ILE A . n 
A 1 579 ALA 579 579 579 ALA ALA A . n 
A 1 580 PRO 580 580 580 PRO PRO A . n 
A 1 581 THR 581 581 581 THR THR A . n 
A 1 582 GLY 582 582 582 GLY GLY A . n 
A 1 583 SER 583 583 583 SER SER A . n 
A 1 584 ILE 584 584 584 ILE ILE A . n 
A 1 585 SER 585 585 585 SER SER A . n 
A 1 586 TYR 586 586 586 TYR TYR A . n 
A 1 587 VAL 587 587 587 VAL VAL A . n 
A 1 588 GLN 588 588 588 GLN GLN A . n 
A 1 589 SER 589 589 589 SER SER A . n 
A 1 590 SER 590 590 590 SER SER A . n 
A 1 591 THR 591 591 591 THR THR A . n 
A 1 592 ALA 592 592 592 ALA ALA A . n 
A 1 593 SER 593 593 593 SER SER A . n 
A 1 594 VAL 594 594 594 VAL VAL A . n 
A 1 595 MET 595 595 595 MET MET A . n 
A 1 596 PRO 596 596 596 PRO PRO A . n 
A 1 597 ILE 597 597 597 ILE ILE A . n 
A 1 598 MET 598 598 598 MET MET A . n 
A 1 599 GLU 599 599 599 GLU GLU A . n 
A 1 600 ARG 600 600 600 ARG ARG A . n 
A 1 601 ILE 601 601 601 ILE ILE A . n 
A 1 602 GLU 602 602 602 GLU GLU A . n 
A 1 603 GLU 603 603 603 GLU GLU A . n 
A 1 604 ARG 604 604 604 ARG ARG A . n 
A 1 605 THR 605 605 605 THR THR A . n 
A 1 606 TYR 606 606 606 TYR TYR A . n 
A 1 607 GLY 607 607 607 GLY GLY A . n 
A 1 608 ASN 608 608 608 ASN ASN A . n 
A 1 609 SER 609 609 609 SER SER A . n 
A 1 610 LYS 610 610 610 LYS LYS A . n 
A 1 611 THR 611 611 611 THR THR A . n 
A 1 612 TYR 612 612 612 TYR TYR A . n 
A 1 613 TYR 613 613 613 TYR TYR A . n 
A 1 614 PRO 614 614 614 PRO PRO A . n 
A 1 615 MET 615 615 615 MET MET A . n 
A 1 616 PRO 616 616 616 PRO PRO A . n 
A 1 617 GLY 617 617 617 GLY GLY A . n 
A 1 618 LEU 618 618 618 LEU LEU A . n 
A 1 619 ALA 619 619 619 ALA ALA A . n 
A 1 620 SER 620 620 620 SER SER A . n 
A 1 621 ASN 621 621 621 ASN ASN A . n 
A 1 622 ASN 622 622 622 ASN ASN A . n 
A 1 623 TRP 623 623 623 TRP TRP A . n 
A 1 624 PHE 624 624 624 PHE PHE A . n 
A 1 625 PHE 625 625 625 PHE PHE A . n 
A 1 626 TYR 626 626 626 TYR TYR A . n 
A 1 627 LYS 627 627 627 LYS LYS A . n 
A 1 628 GLU 628 628 628 GLU GLU A . n 
A 1 629 ALA 629 629 629 ALA ALA A . n 
A 1 630 TYR 630 630 630 TYR TYR A . n 
A 1 631 ASP 631 631 631 ASP ASP A . n 
A 1 632 MET 632 632 632 MET MET A . n 
A 1 633 ASP 633 633 633 ASP ASP A . n 
A 1 634 MET 634 634 634 MET MET A . n 
A 1 635 PHE 635 635 635 PHE PHE A . n 
A 1 636 LYS 636 636 636 LYS LYS A . n 
A 1 637 VAL 637 637 637 VAL VAL A . n 
A 1 638 VAL 638 638 638 VAL VAL A . n 
A 1 639 ASP 639 639 639 ASP ASP A . n 
A 1 640 MET 640 640 640 MET MET A . n 
A 1 641 ILE 641 641 641 ILE ILE A . n 
A 1 642 ALA 642 642 642 ALA ALA A . n 
A 1 643 THR 643 643 643 THR THR A . n 
A 1 644 ILE 644 644 644 ILE ILE A . n 
A 1 645 GLN 645 645 645 GLN GLN A . n 
A 1 646 GLN 646 646 646 GLN GLN A . n 
A 1 647 HIS 647 647 647 HIS HIS A . n 
A 1 648 ILE 648 648 648 ILE ILE A . n 
A 1 649 ASP 649 649 649 ASP ASP A . n 
A 1 650 GLN 650 650 650 GLN GLN A . n 
A 1 651 GLY 651 651 651 GLY GLY A . n 
A 1 652 ILE 652 652 652 ILE ILE A . n 
A 1 653 SER 653 653 653 SER SER A . n 
A 1 654 PHE 654 654 654 PHE PHE A . n 
A 1 655 THR 655 655 655 THR THR A . n 
A 1 656 LEU 656 656 656 LEU LEU A . n 
A 1 657 PHE 657 657 657 PHE PHE A . n 
A 1 658 LEU 658 658 658 LEU LEU A . n 
A 1 659 LYS 659 659 659 LYS LYS A . n 
A 1 660 ASP 660 660 660 ASP ASP A . n 
A 1 661 THR 661 661 661 THR THR A . n 
A 1 662 MET 662 662 662 MET MET A . n 
A 1 663 THR 663 663 663 THR THR A . n 
A 1 664 THR 664 664 664 THR THR A . n 
A 1 665 ARG 665 665 665 ARG ARG A . n 
A 1 666 ASP 666 666 666 ASP ASP A . n 
A 1 667 LEU 667 667 667 LEU LEU A . n 
A 1 668 ASN 668 668 668 ASN ASN A . n 
A 1 669 ARG 669 669 669 ARG ARG A . n 
A 1 670 ILE 670 670 670 ILE ILE A . n 
A 1 671 ASP 671 671 671 ASP ASP A . n 
A 1 672 LEU 672 672 672 LEU LEU A . n 
A 1 673 TYR 673 673 673 TYR TYR A . n 
A 1 674 ALA 674 674 674 ALA ALA A . n 
A 1 675 HIS 675 675 675 HIS HIS A . n 
A 1 676 HIS 676 676 676 HIS HIS A . n 
A 1 677 ARG 677 677 677 ARG ARG A . n 
A 1 678 GLY 678 678 678 GLY GLY A . n 
A 1 679 ILE 679 679 679 ILE ILE A . n 
A 1 680 LYS 680 680 680 LYS LYS A . n 
A 1 681 THR 681 681 681 THR THR A . n 
A 1 682 ILE 682 682 682 ILE ILE A . n 
A 1 683 TYR 683 683 683 TYR TYR A . n 
A 1 684 TYR 684 684 684 TYR TYR A . n 
A 1 685 ALA 685 685 685 ALA ALA A . n 
A 1 686 ARG 686 686 686 ARG ARG A . n 
A 1 687 THR 687 687 687 THR THR A . n 
A 1 688 LYS 688 688 688 LYS LYS A . n 
A 1 689 ASP 689 689 ?   ?   ?   A . n 
A 1 690 THR 690 690 ?   ?   ?   A . n 
A 1 691 GLY 691 691 ?   ?   ?   A . n 
A 1 692 GLN 692 692 ?   ?   ?   A . n 
A 1 693 ASP 693 693 ?   ?   ?   A . n 
A 1 694 SER 694 694 ?   ?   ?   A . n 
A 1 695 CYS 695 695 ?   ?   ?   A . n 
A 1 696 LEU 696 696 ?   ?   ?   A . n 
A 1 697 SER 697 697 ?   ?   ?   A . n 
A 1 698 CYS 698 698 ?   ?   ?   A . n 
A 1 699 VAL 699 699 ?   ?   ?   A . n 
A 1 700 VAL 700 700 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   GLN 3   3   ?   ?   ?   B . n 
B 1 4   ASN 4   4   ?   ?   ?   B . n 
B 1 5   GLN 5   5   ?   ?   ?   B . n 
B 1 6   VAL 6   6   6   VAL VAL B . n 
B 1 7   PRO 7   7   7   PRO PRO B . n 
B 1 8   LYS 8   8   8   LYS LYS B . n 
B 1 9   TRP 9   9   9   TRP TRP B . n 
B 1 10  ILE 10  10  10  ILE ILE B . n 
B 1 11  GLN 11  11  11  GLN GLN B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  ASN 13  13  13  ASN ASN B . n 
B 1 14  ASN 14  14  14  ASN ASN B . n 
B 1 15  GLU 15  15  15  GLU GLU B . n 
B 1 16  ILE 16  16  16  ILE ILE B . n 
B 1 17  MET 17  17  17  MET MET B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  GLN 19  19  19  GLN GLN B . n 
B 1 20  LYS 20  20  20  LYS LYS B . n 
B 1 21  ASP 21  21  21  ASP ASP B . n 
B 1 22  GLY 22  22  22  GLY GLY B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  PHE 24  24  24  PHE PHE B . n 
B 1 25  GLN 25  25  25  GLN GLN B . n 
B 1 26  PHE 26  26  26  PHE PHE B . n 
B 1 27  ASP 27  27  27  ASP ASP B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  ASP 29  29  29  ASP ASP B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  GLU 31  31  31  GLU GLU B . n 
B 1 32  ALA 32  32  32  ALA ALA B . n 
B 1 33  VAL 33  33  33  VAL VAL B . n 
B 1 34  HIS 34  34  34  HIS HIS B . n 
B 1 35  SER 35  35  35  SER SER B . n 
B 1 36  TYR 36  36  36  TYR TYR B . n 
B 1 37  PHE 37  37  37  PHE PHE B . n 
B 1 38  VAL 38  38  38  VAL VAL B . n 
B 1 39  ASP 39  39  39  ASP ASP B . n 
B 1 40  TYR 40  40  40  TYR TYR B . n 
B 1 41  ILE 41  41  41  ILE ILE B . n 
B 1 42  ASN 42  42  42  ASN ASN B . n 
B 1 43  GLN 43  43  43  GLN GLN B . n 
B 1 44  ASN 44  44  44  ASN ASN B . n 
B 1 45  THR 45  45  45  THR THR B . n 
B 1 46  VAL 46  46  46  VAL VAL B . n 
B 1 47  PHE 47  47  47  PHE PHE B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  HIS 49  49  49  HIS HIS B . n 
B 1 50  ASN 50  50  50  ASN ASN B . n 
B 1 51  LEU 51  51  51  LEU LEU B . n 
B 1 52  LYS 52  52  52  LYS LYS B . n 
B 1 53  GLU 53  53  53  GLU GLU B . n 
B 1 54  LYS 54  54  54  LYS LYS B . n 
B 1 55  LEU 55  55  55  LEU LEU B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  TYR 57  57  57  TYR TYR B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  VAL 59  59  59  VAL VAL B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  ASN 61  61  61  ASN ASN B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  TYR 63  63  63  TYR TYR B . n 
B 1 64  TYR 64  64  64  TYR TYR B . n 
B 1 65  GLU 65  65  65  GLU GLU B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  GLU 67  67  67  GLU GLU B . n 
B 1 68  PHE 68  68  68  PHE PHE B . n 
B 1 69  LEU 69  69  69  LEU LEU B . n 
B 1 70  SER 70  70  70  SER SER B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  TYR 72  72  72  TYR TYR B . n 
B 1 73  SER 73  73  73  SER SER B . n 
B 1 74  PHE 74  74  74  PHE PHE B . n 
B 1 75  GLU 75  75  75  GLU GLU B . n 
B 1 76  ASP 76  76  76  ASP ASP B . n 
B 1 77  ILE 77  77  77  ILE ILE B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  GLU 79  79  79  GLU GLU B . n 
B 1 80  VAL 80  80  80  VAL VAL B . n 
B 1 81  PHE 81  81  81  PHE PHE B . n 
B 1 82  LYS 82  82  82  LYS LYS B . n 
B 1 83  THR 83  83  83  THR THR B . n 
B 1 84  ALA 84  84  84  ALA ALA B . n 
B 1 85  TYR 85  85  85  TYR TYR B . n 
B 1 86  ALA 86  86  86  ALA ALA B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  PHE 89  89  89  PHE PHE B . n 
B 1 90  ARG 90  90  90  ARG ARG B . n 
B 1 91  PHE 91  91  91  PHE PHE B . n 
B 1 92  PRO 92  92  92  PRO PRO B . n 
B 1 93  SER 93  93  93  SER SER B . n 
B 1 94  PHE 94  94  94  PHE PHE B . n 
B 1 95  MET 95  95  95  MET MET B . n 
B 1 96  SER 96  96  96  SER SER B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  PHE 98  98  98  PHE PHE B . n 
B 1 99  LYS 99  99  99  LYS LYS B . n 
B 1 100 PHE 100 100 100 PHE PHE B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 ASN 102 102 102 ASN ASN B . n 
B 1 103 ASP 103 103 103 ASP ASP B . n 
B 1 104 TYR 104 104 104 TYR TYR B . n 
B 1 105 ALA 105 105 105 ALA ALA B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 LYS 107 107 107 LYS LYS B . n 
B 1 108 THR 108 108 108 THR THR B . n 
B 1 109 ASN 109 109 109 ASN ASN B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 LYS 112 112 112 LYS LYS B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 ILE 114 114 114 ILE ILE B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 GLU 116 116 116 GLU GLU B . n 
B 1 117 ARG 117 117 117 ARG ARG B . n 
B 1 118 TYR 118 118 118 TYR TYR B . n 
B 1 119 GLU 119 119 119 GLU GLU B . n 
B 1 120 ASP 120 120 120 ASP ASP B . n 
B 1 121 ARG 121 121 121 ARG ARG B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 ILE 124 124 124 ILE ILE B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 ALA 126 126 126 ALA ALA B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 PHE 128 128 128 PHE PHE B . n 
B 1 129 PHE 129 129 129 PHE PHE B . n 
B 1 130 ALA 130 130 130 ALA ALA B . n 
B 1 131 ASN 131 131 131 ASN ASN B . n 
B 1 132 GLY 132 132 132 GLY GLY B . n 
B 1 133 ASP 133 133 133 ASP ASP B . n 
B 1 134 THR 134 134 134 THR THR B . n 
B 1 135 GLU 135 135 135 GLU GLU B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 ALA 137 137 137 ALA ALA B . n 
B 1 138 LYS 138 138 138 LYS LYS B . n 
B 1 139 GLU 139 139 139 GLU GLU B . n 
B 1 140 TYR 140 140 140 TYR TYR B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 MET 144 144 144 MET MET B . n 
B 1 145 ILE 145 145 145 ILE ILE B . n 
B 1 146 ASN 146 146 146 ASN ASN B . n 
B 1 147 GLN 147 147 147 GLN GLN B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 TYR 149 149 149 TYR TYR B . n 
B 1 150 GLN 150 150 150 GLN GLN B . n 
B 1 151 PRO 151 151 151 PRO PRO B . n 
B 1 152 SER 152 152 152 SER SER B . n 
B 1 153 THR 153 153 153 THR THR B . n 
B 1 154 PRO 154 154 154 PRO PRO B . n 
B 1 155 THR 155 155 155 THR THR B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 LEU 157 157 157 LEU LEU B . n 
B 1 158 ASN 158 158 158 ASN ASN B . n 
B 1 159 ALA 159 159 159 ALA ALA B . n 
B 1 160 GLY 160 160 160 GLY GLY B . n 
B 1 161 ARG 161 161 161 ARG ARG B . n 
B 1 162 LYS 162 162 162 LYS LYS B . n 
B 1 163 ARG 163 163 163 ARG ARG B . n 
B 1 164 ARG 164 164 164 ARG ARG B . n 
B 1 165 GLY 165 165 165 GLY GLY B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 LEU 167 167 167 LEU LEU B . n 
B 1 168 VAL 168 168 168 VAL VAL B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 CYS 170 170 170 CYS CYS B . n 
B 1 171 PHE 171 171 171 PHE PHE B . n 
B 1 172 LEU 172 172 172 LEU LEU B . n 
B 1 173 LEU 173 173 173 LEU LEU B . n 
B 1 174 GLU 174 174 174 GLU GLU B . n 
B 1 175 VAL 175 175 175 VAL VAL B . n 
B 1 176 ASN 176 176 176 ASN ASN B . n 
B 1 177 ASP 177 177 177 ASP ASP B . n 
B 1 178 SER 178 178 178 SER SER B . n 
B 1 179 LEU 179 179 179 LEU LEU B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 ASP 181 181 181 ASP ASP B . n 
B 1 182 ILE 182 182 182 ILE ILE B . n 
B 1 183 SER 183 183 183 SER SER B . n 
B 1 184 ARG 184 184 184 ARG ARG B . n 
B 1 185 ALA 185 185 185 ALA ALA B . n 
B 1 186 ILE 186 186 186 ILE ILE B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 ILE 188 188 188 ILE ILE B . n 
B 1 189 SER 189 189 189 SER SER B . n 
B 1 190 MET 190 190 190 MET MET B . n 
B 1 191 GLN 191 191 191 GLN GLN B . n 
B 1 192 LEU 192 192 192 LEU LEU B . n 
B 1 193 SER 193 193 193 SER SER B . n 
B 1 194 LYS 194 194 194 LYS LYS B . n 
B 1 195 LEU 195 195 195 LEU LEU B . n 
B 1 196 GLY 196 196 196 GLY GLY B . n 
B 1 197 GLY 197 197 197 GLY GLY B . n 
B 1 198 GLY 198 198 198 GLY GLY B . n 
B 1 199 VAL 199 199 199 VAL VAL B . n 
B 1 200 SER 200 200 200 SER SER B . n 
B 1 201 LEU 201 201 201 LEU LEU B . n 
B 1 202 ASN 202 202 202 ASN ASN B . n 
B 1 203 LEU 203 203 203 LEU LEU B . n 
B 1 204 SER 204 204 204 SER SER B . n 
B 1 205 LYS 205 205 205 LYS LYS B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 ARG 207 207 207 ARG ARG B . n 
B 1 208 ALA 208 208 208 ALA ALA B . n 
B 1 209 LYS 209 209 209 LYS LYS B . n 
B 1 210 GLY 210 210 210 GLY GLY B . n 
B 1 211 GLU 211 211 211 GLU GLU B . n 
B 1 212 ALA 212 212 212 ALA ALA B . n 
B 1 213 ILE 213 213 213 ILE ILE B . n 
B 1 214 LYS 214 214 214 LYS LYS B . n 
B 1 215 ASP 215 215 215 ASP ASP B . n 
B 1 216 VAL 216 216 216 VAL VAL B . n 
B 1 217 GLU 217 217 217 GLU GLU B . n 
B 1 218 ASN 218 218 218 ASN ASN B . n 
B 1 219 ALA 219 219 219 ALA ALA B . n 
B 1 220 THR 220 220 220 THR THR B . n 
B 1 221 LYS 221 221 221 LYS LYS B . n 
B 1 222 GLY 222 222 222 GLY GLY B . n 
B 1 223 VAL 223 223 223 VAL VAL B . n 
B 1 224 VAL 224 224 224 VAL VAL B . n 
B 1 225 GLY 225 225 225 GLY GLY B . n 
B 1 226 VAL 226 226 226 VAL VAL B . n 
B 1 227 MET 227 227 227 MET MET B . n 
B 1 228 LYS 228 228 228 LYS LYS B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 LEU 230 230 230 LEU LEU B . n 
B 1 231 ASP 231 231 231 ASP ASP B . n 
B 1 232 ASN 232 232 232 ASN ASN B . n 
B 1 233 ALA 233 233 233 ALA ALA B . n 
B 1 234 PHE 234 234 234 PHE PHE B . n 
B 1 235 ARG 235 235 235 ARG ARG B . n 
B 1 236 TYR 236 236 236 TYR TYR B . n 
B 1 237 ALA 237 237 237 ALA ALA B . n 
B 1 238 ASP 238 238 238 ASP ASP B . n 
B 1 239 GLN 239 239 239 GLN GLN B . n 
B 1 240 MET 240 240 240 MET MET B . n 
B 1 241 GLY 241 241 241 GLY GLY B . n 
B 1 242 GLN 242 242 242 GLN GLN B . n 
B 1 243 ARG 243 243 243 ARG ARG B . n 
B 1 244 GLN 244 244 244 GLN GLN B . n 
B 1 245 GLY 245 245 245 GLY GLY B . n 
B 1 246 SER 246 246 246 SER SER B . n 
B 1 247 GLY 247 247 247 GLY GLY B . n 
B 1 248 ALA 248 248 248 ALA ALA B . n 
B 1 249 ALA 249 249 249 ALA ALA B . n 
B 1 250 TYR 250 250 250 TYR TYR B . n 
B 1 251 LEU 251 251 251 LEU LEU B . n 
B 1 252 ASN 252 252 252 ASN ASN B . n 
B 1 253 ILE 253 253 253 ILE ILE B . n 
B 1 254 PHE 254 254 254 PHE PHE B . n 
B 1 255 HIS 255 255 255 HIS HIS B . n 
B 1 256 ARG 256 256 256 ARG ARG B . n 
B 1 257 ASP 257 257 257 ASP ASP B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 ASN 259 259 259 ASN ASN B . n 
B 1 260 ASP 260 260 260 ASP ASP B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ASP 263 263 263 ASP ASP B . n 
B 1 264 THR 264 264 264 THR THR B . n 
B 1 265 LYS 265 265 265 LYS LYS B . n 
B 1 266 LYS 266 266 266 LYS LYS B . n 
B 1 267 ILE 267 267 267 ILE ILE B . n 
B 1 268 SER 268 268 268 SER SER B . n 
B 1 269 ALA 269 269 269 ALA ALA B . n 
B 1 270 ASP 270 270 270 ASP ASP B . n 
B 1 271 GLU 271 271 271 GLU GLU B . n 
B 1 272 ASP 272 272 272 ASP ASP B . n 
B 1 273 VAL 273 273 273 VAL VAL B . n 
B 1 274 ARG 274 274 274 ARG ARG B . n 
B 1 275 VAL 275 275 275 VAL VAL B . n 
B 1 276 LYS 276 276 276 LYS LYS B . n 
B 1 277 THR 277 277 277 THR THR B . n 
B 1 278 LEU 278 278 278 LEU LEU B . n 
B 1 279 SER 279 279 279 SER SER B . n 
B 1 280 ILE 280 280 280 ILE ILE B . n 
B 1 281 GLY 281 281 281 GLY GLY B . n 
B 1 282 VAL 282 282 282 VAL VAL B . n 
B 1 283 VAL 283 283 283 VAL VAL B . n 
B 1 284 ILE 284 284 284 ILE ILE B . n 
B 1 285 PRO 285 285 285 PRO PRO B . n 
B 1 286 ASP 286 286 286 ASP ASP B . n 
B 1 287 LYS 287 287 287 LYS LYS B . n 
B 1 288 PHE 288 288 288 PHE PHE B . n 
B 1 289 VAL 289 289 289 VAL VAL B . n 
B 1 290 GLU 290 290 290 GLU GLU B . n 
B 1 291 LEU 291 291 291 LEU LEU B . n 
B 1 292 ALA 292 292 292 ALA ALA B . n 
B 1 293 ARG 293 293 293 ARG ARG B . n 
B 1 294 GLU 294 294 294 GLU GLU B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 LYS 296 296 296 LYS LYS B . n 
B 1 297 ALA 297 297 297 ALA ALA B . n 
B 1 298 ALA 298 298 298 ALA ALA B . n 
B 1 299 TYR 299 299 299 TYR TYR B . n 
B 1 300 VAL 300 300 300 VAL VAL B . n 
B 1 301 PHE 301 301 301 PHE PHE B . n 
B 1 302 TYR 302 302 302 TYR TYR B . n 
B 1 303 PRO 303 303 303 PRO PRO B . n 
B 1 304 HIS 304 304 304 HIS HIS B . n 
B 1 305 THR 305 305 305 THR THR B . n 
B 1 306 ILE 306 306 306 ILE ILE B . n 
B 1 307 TYR 307 307 307 TYR TYR B . n 
B 1 308 LYS 308 308 308 LYS LYS B . n 
B 1 309 GLU 309 309 309 GLU GLU B . n 
B 1 310 TYR 310 310 310 TYR TYR B . n 
B 1 311 GLY 311 311 311 GLY GLY B . n 
B 1 312 GLN 312 312 312 GLN GLN B . n 
B 1 313 HIS 313 313 313 HIS HIS B . n 
B 1 314 MET 314 314 314 MET MET B . n 
B 1 315 ASP 315 315 315 ASP ASP B . n 
B 1 316 GLU 316 316 316 GLU GLU B . n 
B 1 317 MET 317 317 317 MET MET B . n 
B 1 318 ASP 318 318 318 ASP ASP B . n 
B 1 319 MET 319 319 319 MET MET B . n 
B 1 320 ASN 320 320 320 ASN ASN B . n 
B 1 321 GLU 321 321 321 GLU GLU B . n 
B 1 322 MET 322 322 322 MET MET B . n 
B 1 323 TYR 323 323 323 TYR TYR B . n 
B 1 324 ASP 324 324 324 ASP ASP B . n 
B 1 325 LYS 325 325 325 LYS LYS B . n 
B 1 326 PHE 326 326 326 PHE PHE B . n 
B 1 327 VAL 327 327 327 VAL VAL B . n 
B 1 328 ASP 328 328 328 ASP ASP B . n 
B 1 329 ASN 329 329 329 ASN ASN B . n 
B 1 330 PRO 330 330 330 PRO PRO B . n 
B 1 331 ARG 331 331 331 ARG ARG B . n 
B 1 332 VAL 332 332 332 VAL VAL B . n 
B 1 333 LYS 333 333 333 LYS LYS B . n 
B 1 334 LYS 334 334 334 LYS LYS B . n 
B 1 335 GLU 335 335 335 GLU GLU B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 ILE 337 337 337 ILE ILE B . n 
B 1 338 ASN 338 338 338 ASN ASN B . n 
B 1 339 PRO 339 339 339 PRO PRO B . n 
B 1 340 ARG 340 340 340 ARG ARG B . n 
B 1 341 LYS 341 341 341 LYS LYS B . n 
B 1 342 LEU 342 342 342 LEU LEU B . n 
B 1 343 LEU 343 343 343 LEU LEU B . n 
B 1 344 GLU 344 344 344 GLU GLU B . n 
B 1 345 LYS 345 345 345 LYS LYS B . n 
B 1 346 LEU 346 346 346 LEU LEU B . n 
B 1 347 ALA 347 347 347 ALA ALA B . n 
B 1 348 MET 348 348 348 MET MET B . n 
B 1 349 LEU 349 349 349 LEU LEU B . n 
B 1 350 ARG 350 350 350 ARG ARG B . n 
B 1 351 SER 351 351 351 SER SER B . n 
B 1 352 GLU 352 352 352 GLU GLU B . n 
B 1 353 SER 353 353 353 SER SER B . n 
B 1 354 GLY 354 354 354 GLY GLY B . n 
B 1 355 TYR 355 355 355 TYR TYR B . n 
B 1 356 PRO 356 356 356 PRO PRO B . n 
B 1 357 TYR 357 357 357 TYR TYR B . n 
B 1 358 ILE 358 358 358 ILE ILE B . n 
B 1 359 MET 359 359 359 MET MET B . n 
B 1 360 PHE 360 360 360 PHE PHE B . n 
B 1 361 GLN 361 361 361 GLN GLN B . n 
B 1 362 ASP 362 362 362 ASP ASP B . n 
B 1 363 ASN 363 363 363 ASN ASN B . n 
B 1 364 VAL 364 364 364 VAL VAL B . n 
B 1 365 ASN 365 365 365 ASN ASN B . n 
B 1 366 LYS 366 366 366 LYS LYS B . n 
B 1 367 VAL 367 367 367 VAL VAL B . n 
B 1 368 HIS 368 368 368 HIS HIS B . n 
B 1 369 ALA 369 369 369 ALA ALA B . n 
B 1 370 ASN 370 370 370 ASN ASN B . n 
B 1 371 ASN 371 371 371 ASN ASN B . n 
B 1 372 HIS 372 372 372 HIS HIS B . n 
B 1 373 ILE 373 373 373 ILE ILE B . n 
B 1 374 SER 374 374 374 SER SER B . n 
B 1 375 LYS 375 375 375 LYS LYS B . n 
B 1 376 VAL 376 376 376 VAL VAL B . n 
B 1 377 LYS 377 377 377 LYS LYS B . n 
B 1 378 PHE 378 378 378 PHE PHE B . n 
B 1 379 SER 379 379 379 SER SER B . n 
B 1 380 ASN 380 380 380 ASN ASN B . n 
B 1 381 LEU 381 381 381 LEU LEU B . n 
B 1 382 CYS 382 382 382 CYS CYS B . n 
B 1 383 SER 383 383 383 SER SER B . n 
B 1 384 GLU 384 384 384 GLU GLU B . n 
B 1 385 VAL 385 385 385 VAL VAL B . n 
B 1 386 LEU 386 386 386 LEU LEU B . n 
B 1 387 GLN 387 387 387 GLN GLN B . n 
B 1 388 ALA 388 388 388 ALA ALA B . n 
B 1 389 SER 389 389 389 SER SER B . n 
B 1 390 GLN 390 390 390 GLN GLN B . n 
B 1 391 VAL 391 391 391 VAL VAL B . n 
B 1 392 SER 392 392 392 SER SER B . n 
B 1 393 SER 393 393 393 SER SER B . n 
B 1 394 TYR 394 394 394 TYR TYR B . n 
B 1 395 THR 395 395 395 THR THR B . n 
B 1 396 ASP 396 396 396 ASP ASP B . n 
B 1 397 TYR 397 397 397 TYR TYR B . n 
B 1 398 ASP 398 398 398 ASP ASP B . n 
B 1 399 GLU 399 399 399 GLU GLU B . n 
B 1 400 GLU 400 400 400 GLU GLU B . n 
B 1 401 ASP 401 401 401 ASP ASP B . n 
B 1 402 GLU 402 402 402 GLU GLU B . n 
B 1 403 ILE 403 403 403 ILE ILE B . n 
B 1 404 GLY 404 404 404 GLY GLY B . n 
B 1 405 LEU 405 405 405 LEU LEU B . n 
B 1 406 ASP 406 406 406 ASP ASP B . n 
B 1 407 ILE 407 407 407 ILE ILE B . n 
B 1 408 SER 408 408 408 SER SER B . n 
B 1 409 CYS 409 409 409 CYS CYS B . n 
B 1 410 ASN 410 410 410 ASN ASN B . n 
B 1 411 LEU 411 411 411 LEU LEU B . n 
B 1 412 GLY 412 412 412 GLY GLY B . n 
B 1 413 SER 413 413 413 SER SER B . n 
B 1 414 LEU 414 414 414 LEU LEU B . n 
B 1 415 ASN 415 415 415 ASN ASN B . n 
B 1 416 ILE 416 416 416 ILE ILE B . n 
B 1 417 LEU 417 417 417 LEU LEU B . n 
B 1 418 ASN 418 418 418 ASN ASN B . n 
B 1 419 VAL 419 419 419 VAL VAL B . n 
B 1 420 MET 420 420 420 MET MET B . n 
B 1 421 GLU 421 421 421 GLU GLU B . n 
B 1 422 HIS 422 422 422 HIS HIS B . n 
B 1 423 LYS 423 423 423 LYS LYS B . n 
B 1 424 SER 424 424 424 SER SER B . n 
B 1 425 ILE 425 425 425 ILE ILE B . n 
B 1 426 GLU 426 426 426 GLU GLU B . n 
B 1 427 LYS 427 427 427 LYS LYS B . n 
B 1 428 THR 428 428 428 THR THR B . n 
B 1 429 VAL 429 429 429 VAL VAL B . n 
B 1 430 LYS 430 430 430 LYS LYS B . n 
B 1 431 LEU 431 431 431 LEU LEU B . n 
B 1 432 ALA 432 432 432 ALA ALA B . n 
B 1 433 THR 433 433 433 THR THR B . n 
B 1 434 ASP 434 434 434 ASP ASP B . n 
B 1 435 SER 435 435 435 SER SER B . n 
B 1 436 LEU 436 436 436 LEU LEU B . n 
B 1 437 THR 437 437 437 THR THR B . n 
B 1 438 HIS 438 438 438 HIS HIS B . n 
B 1 439 VAL 439 439 439 VAL VAL B . n 
B 1 440 SER 440 440 440 SER SER B . n 
B 1 441 GLU 441 441 441 GLU GLU B . n 
B 1 442 THR 442 442 442 THR THR B . n 
B 1 443 THR 443 443 443 THR THR B . n 
B 1 444 ASP 444 444 444 ASP ASP B . n 
B 1 445 ILE 445 445 445 ILE ILE B . n 
B 1 446 ARG 446 446 446 ARG ARG B . n 
B 1 447 ASN 447 447 447 ASN ASN B . n 
B 1 448 ALA 448 448 448 ALA ALA B . n 
B 1 449 PRO 449 449 449 PRO PRO B . n 
B 1 450 ALA 450 450 450 ALA ALA B . n 
B 1 451 VAL 451 451 451 VAL VAL B . n 
B 1 452 ARG 452 452 452 ARG ARG B . n 
B 1 453 ARG 453 453 453 ARG ARG B . n 
B 1 454 ALA 454 454 454 ALA ALA B . n 
B 1 455 ASN 455 455 455 ASN ASN B . n 
B 1 456 LYS 456 456 456 LYS LYS B . n 
B 1 457 ALA 457 457 457 ALA ALA B . n 
B 1 458 MET 458 458 458 MET MET B . n 
B 1 459 LYS 459 459 459 LYS LYS B . n 
B 1 460 SER 460 460 460 SER SER B . n 
B 1 461 ILE 461 461 461 ILE ILE B . n 
B 1 462 GLY 462 462 462 GLY GLY B . n 
B 1 463 LEU 463 463 463 LEU LEU B . n 
B 1 464 GLY 464 464 464 GLY GLY B . n 
B 1 465 ALA 465 465 465 ALA ALA B . n 
B 1 466 MET 466 466 466 MET MET B . n 
B 1 467 ASN 467 467 467 ASN ASN B . n 
B 1 468 LEU 468 468 468 LEU LEU B . n 
B 1 469 HIS 469 469 469 HIS HIS B . n 
B 1 470 GLY 470 470 470 GLY GLY B . n 
B 1 471 TYR 471 471 471 TYR TYR B . n 
B 1 472 LEU 472 472 472 LEU LEU B . n 
B 1 473 ALA 473 473 473 ALA ALA B . n 
B 1 474 GLN 474 474 474 GLN GLN B . n 
B 1 475 ASN 475 475 475 ASN ASN B . n 
B 1 476 GLY 476 476 476 GLY GLY B . n 
B 1 477 ILE 477 477 477 ILE ILE B . n 
B 1 478 ALA 478 478 478 ALA ALA B . n 
B 1 479 TYR 479 479 479 TYR TYR B . n 
B 1 480 GLU 480 480 480 GLU GLU B . n 
B 1 481 SER 481 481 481 SER SER B . n 
B 1 482 PRO 482 482 482 PRO PRO B . n 
B 1 483 GLU 483 483 483 GLU GLU B . n 
B 1 484 ALA 484 484 484 ALA ALA B . n 
B 1 485 ARG 485 485 485 ARG ARG B . n 
B 1 486 ASP 486 486 486 ASP ASP B . n 
B 1 487 PHE 487 487 487 PHE PHE B . n 
B 1 488 ALA 488 488 488 ALA ALA B . n 
B 1 489 ASN 489 489 489 ASN ASN B . n 
B 1 490 THR 490 490 490 THR THR B . n 
B 1 491 PHE 491 491 491 PHE PHE B . n 
B 1 492 PHE 492 492 492 PHE PHE B . n 
B 1 493 MET 493 493 493 MET MET B . n 
B 1 494 MET 494 494 494 MET MET B . n 
B 1 495 VAL 495 495 495 VAL VAL B . n 
B 1 496 ASN 496 496 496 ASN ASN B . n 
B 1 497 PHE 497 497 497 PHE PHE B . n 
B 1 498 TYR 498 498 498 TYR TYR B . n 
B 1 499 SER 499 499 499 SER SER B . n 
B 1 500 ILE 500 500 500 ILE ILE B . n 
B 1 501 GLN 501 501 501 GLN GLN B . n 
B 1 502 ARG 502 502 502 ARG ARG B . n 
B 1 503 SER 503 503 503 SER SER B . n 
B 1 504 ALA 504 504 504 ALA ALA B . n 
B 1 505 GLU 505 505 505 GLU GLU B . n 
B 1 506 ILE 506 506 506 ILE ILE B . n 
B 1 507 ALA 507 507 507 ALA ALA B . n 
B 1 508 LYS 508 508 508 LYS LYS B . n 
B 1 509 GLU 509 509 509 GLU GLU B . n 
B 1 510 LYS 510 510 510 LYS LYS B . n 
B 1 511 GLY 511 511 511 GLY GLY B . n 
B 1 512 GLU 512 512 512 GLU GLU B . n 
B 1 513 THR 513 513 513 THR THR B . n 
B 1 514 PHE 514 514 514 PHE PHE B . n 
B 1 515 ASP 515 515 515 ASP ASP B . n 
B 1 516 GLN 516 516 516 GLN GLN B . n 
B 1 517 TYR 517 517 517 TYR TYR B . n 
B 1 518 GLU 518 518 518 GLU GLU B . n 
B 1 519 GLY 519 519 519 GLY GLY B . n 
B 1 520 SER 520 520 520 SER SER B . n 
B 1 521 THR 521 521 521 THR THR B . n 
B 1 522 TYR 522 522 522 TYR TYR B . n 
B 1 523 ALA 523 523 523 ALA ALA B . n 
B 1 524 THR 524 524 524 THR THR B . n 
B 1 525 GLY 525 525 525 GLY GLY B . n 
B 1 526 GLU 526 526 526 GLU GLU B . n 
B 1 527 TYR 527 527 527 TYR TYR B . n 
B 1 528 PHE 528 528 528 PHE PHE B . n 
B 1 529 ASP 529 529 529 ASP ASP B . n 
B 1 530 LYS 530 530 530 LYS LYS B . n 
B 1 531 TYR 531 531 531 TYR TYR B . n 
B 1 532 VAL 532 532 532 VAL VAL B . n 
B 1 533 SER 533 533 533 SER SER B . n 
B 1 534 THR 534 534 534 THR THR B . n 
B 1 535 ASP 535 535 535 ASP ASP B . n 
B 1 536 PHE 536 536 536 PHE PHE B . n 
B 1 537 SER 537 537 537 SER SER B . n 
B 1 538 PRO 538 538 538 PRO PRO B . n 
B 1 539 LYS 539 539 539 LYS LYS B . n 
B 1 540 TYR 540 540 540 TYR TYR B . n 
B 1 541 GLU 541 541 541 GLU GLU B . n 
B 1 542 LYS 542 542 542 LYS LYS B . n 
B 1 543 ILE 543 543 543 ILE ILE B . n 
B 1 544 ALA 544 544 544 ALA ALA B . n 
B 1 545 ASN 545 545 545 ASN ASN B . n 
B 1 546 LEU 546 546 546 LEU LEU B . n 
B 1 547 PHE 547 547 547 PHE PHE B . n 
B 1 548 GLU 548 548 548 GLU GLU B . n 
B 1 549 GLY 549 549 549 GLY GLY B . n 
B 1 550 MET 550 550 550 MET MET B . n 
B 1 551 HIS 551 551 551 HIS HIS B . n 
B 1 552 ILE 552 552 552 ILE ILE B . n 
B 1 553 PRO 553 553 553 PRO PRO B . n 
B 1 554 THR 554 554 554 THR THR B . n 
B 1 555 THR 555 555 555 THR THR B . n 
B 1 556 GLU 556 556 556 GLU GLU B . n 
B 1 557 ASP 557 557 557 ASP ASP B . n 
B 1 558 TRP 558 558 558 TRP TRP B . n 
B 1 559 LYS 559 559 559 LYS LYS B . n 
B 1 560 LYS 560 560 560 LYS LYS B . n 
B 1 561 LEU 561 561 561 LEU LEU B . n 
B 1 562 LYS 562 562 562 LYS LYS B . n 
B 1 563 ALA 563 563 563 ALA ALA B . n 
B 1 564 PHE 564 564 564 PHE PHE B . n 
B 1 565 VAL 565 565 565 VAL VAL B . n 
B 1 566 ALA 566 566 566 ALA ALA B . n 
B 1 567 GLU 567 567 567 GLU GLU B . n 
B 1 568 HIS 568 568 568 HIS HIS B . n 
B 1 569 GLY 569 569 569 GLY GLY B . n 
B 1 570 MET 570 570 570 MET MET B . n 
B 1 571 TYR 571 571 571 TYR TYR B . n 
B 1 572 HIS 572 572 572 HIS HIS B . n 
B 1 573 SER 573 573 573 SER SER B . n 
B 1 574 TYR 574 574 574 TYR TYR B . n 
B 1 575 ARG 575 575 575 ARG ARG B . n 
B 1 576 LEU 576 576 576 LEU LEU B . n 
B 1 577 CYS 577 577 577 CYS CYS B . n 
B 1 578 ILE 578 578 578 ILE ILE B . n 
B 1 579 ALA 579 579 579 ALA ALA B . n 
B 1 580 PRO 580 580 580 PRO PRO B . n 
B 1 581 THR 581 581 581 THR THR B . n 
B 1 582 GLY 582 582 582 GLY GLY B . n 
B 1 583 SER 583 583 583 SER SER B . n 
B 1 584 ILE 584 584 584 ILE ILE B . n 
B 1 585 SER 585 585 585 SER SER B . n 
B 1 586 TYR 586 586 586 TYR TYR B . n 
B 1 587 VAL 587 587 587 VAL VAL B . n 
B 1 588 GLN 588 588 588 GLN GLN B . n 
B 1 589 SER 589 589 589 SER SER B . n 
B 1 590 SER 590 590 590 SER SER B . n 
B 1 591 THR 591 591 591 THR THR B . n 
B 1 592 ALA 592 592 592 ALA ALA B . n 
B 1 593 SER 593 593 593 SER SER B . n 
B 1 594 VAL 594 594 594 VAL VAL B . n 
B 1 595 MET 595 595 595 MET MET B . n 
B 1 596 PRO 596 596 596 PRO PRO B . n 
B 1 597 ILE 597 597 597 ILE ILE B . n 
B 1 598 MET 598 598 598 MET MET B . n 
B 1 599 GLU 599 599 599 GLU GLU B . n 
B 1 600 ARG 600 600 600 ARG ARG B . n 
B 1 601 ILE 601 601 601 ILE ILE B . n 
B 1 602 GLU 602 602 602 GLU GLU B . n 
B 1 603 GLU 603 603 603 GLU GLU B . n 
B 1 604 ARG 604 604 604 ARG ARG B . n 
B 1 605 THR 605 605 605 THR THR B . n 
B 1 606 TYR 606 606 606 TYR TYR B . n 
B 1 607 GLY 607 607 607 GLY GLY B . n 
B 1 608 ASN 608 608 608 ASN ASN B . n 
B 1 609 SER 609 609 609 SER SER B . n 
B 1 610 LYS 610 610 610 LYS LYS B . n 
B 1 611 THR 611 611 611 THR THR B . n 
B 1 612 TYR 612 612 612 TYR TYR B . n 
B 1 613 TYR 613 613 613 TYR TYR B . n 
B 1 614 PRO 614 614 614 PRO PRO B . n 
B 1 615 MET 615 615 615 MET MET B . n 
B 1 616 PRO 616 616 616 PRO PRO B . n 
B 1 617 GLY 617 617 617 GLY GLY B . n 
B 1 618 LEU 618 618 618 LEU LEU B . n 
B 1 619 ALA 619 619 619 ALA ALA B . n 
B 1 620 SER 620 620 620 SER SER B . n 
B 1 621 ASN 621 621 621 ASN ASN B . n 
B 1 622 ASN 622 622 622 ASN ASN B . n 
B 1 623 TRP 623 623 623 TRP TRP B . n 
B 1 624 PHE 624 624 624 PHE PHE B . n 
B 1 625 PHE 625 625 625 PHE PHE B . n 
B 1 626 TYR 626 626 626 TYR TYR B . n 
B 1 627 LYS 627 627 627 LYS LYS B . n 
B 1 628 GLU 628 628 628 GLU GLU B . n 
B 1 629 ALA 629 629 629 ALA ALA B . n 
B 1 630 TYR 630 630 630 TYR TYR B . n 
B 1 631 ASP 631 631 631 ASP ASP B . n 
B 1 632 MET 632 632 632 MET MET B . n 
B 1 633 ASP 633 633 633 ASP ASP B . n 
B 1 634 MET 634 634 634 MET MET B . n 
B 1 635 PHE 635 635 635 PHE PHE B . n 
B 1 636 LYS 636 636 636 LYS LYS B . n 
B 1 637 VAL 637 637 637 VAL VAL B . n 
B 1 638 VAL 638 638 638 VAL VAL B . n 
B 1 639 ASP 639 639 639 ASP ASP B . n 
B 1 640 MET 640 640 640 MET MET B . n 
B 1 641 ILE 641 641 641 ILE ILE B . n 
B 1 642 ALA 642 642 642 ALA ALA B . n 
B 1 643 THR 643 643 643 THR THR B . n 
B 1 644 ILE 644 644 644 ILE ILE B . n 
B 1 645 GLN 645 645 645 GLN GLN B . n 
B 1 646 GLN 646 646 646 GLN GLN B . n 
B 1 647 HIS 647 647 647 HIS HIS B . n 
B 1 648 ILE 648 648 648 ILE ILE B . n 
B 1 649 ASP 649 649 649 ASP ASP B . n 
B 1 650 GLN 650 650 650 GLN GLN B . n 
B 1 651 GLY 651 651 651 GLY GLY B . n 
B 1 652 ILE 652 652 652 ILE ILE B . n 
B 1 653 SER 653 653 653 SER SER B . n 
B 1 654 PHE 654 654 654 PHE PHE B . n 
B 1 655 THR 655 655 655 THR THR B . n 
B 1 656 LEU 656 656 656 LEU LEU B . n 
B 1 657 PHE 657 657 657 PHE PHE B . n 
B 1 658 LEU 658 658 658 LEU LEU B . n 
B 1 659 LYS 659 659 659 LYS LYS B . n 
B 1 660 ASP 660 660 660 ASP ASP B . n 
B 1 661 THR 661 661 661 THR THR B . n 
B 1 662 MET 662 662 662 MET MET B . n 
B 1 663 THR 663 663 663 THR THR B . n 
B 1 664 THR 664 664 664 THR THR B . n 
B 1 665 ARG 665 665 665 ARG ARG B . n 
B 1 666 ASP 666 666 666 ASP ASP B . n 
B 1 667 LEU 667 667 667 LEU LEU B . n 
B 1 668 ASN 668 668 668 ASN ASN B . n 
B 1 669 ARG 669 669 669 ARG ARG B . n 
B 1 670 ILE 670 670 670 ILE ILE B . n 
B 1 671 ASP 671 671 671 ASP ASP B . n 
B 1 672 LEU 672 672 672 LEU LEU B . n 
B 1 673 TYR 673 673 673 TYR TYR B . n 
B 1 674 ALA 674 674 674 ALA ALA B . n 
B 1 675 HIS 675 675 675 HIS HIS B . n 
B 1 676 HIS 676 676 676 HIS HIS B . n 
B 1 677 ARG 677 677 677 ARG ARG B . n 
B 1 678 GLY 678 678 678 GLY GLY B . n 
B 1 679 ILE 679 679 679 ILE ILE B . n 
B 1 680 LYS 680 680 680 LYS LYS B . n 
B 1 681 THR 681 681 681 THR THR B . n 
B 1 682 ILE 682 682 682 ILE ILE B . n 
B 1 683 TYR 683 683 683 TYR TYR B . n 
B 1 684 TYR 684 684 684 TYR TYR B . n 
B 1 685 ALA 685 685 685 ALA ALA B . n 
B 1 686 ARG 686 686 686 ARG ARG B . n 
B 1 687 THR 687 687 687 THR THR B . n 
B 1 688 LYS 688 688 688 LYS LYS B . n 
B 1 689 ASP 689 689 ?   ?   ?   B . n 
B 1 690 THR 690 690 ?   ?   ?   B . n 
B 1 691 GLY 691 691 ?   ?   ?   B . n 
B 1 692 GLN 692 692 ?   ?   ?   B . n 
B 1 693 ASP 693 693 ?   ?   ?   B . n 
B 1 694 SER 694 694 ?   ?   ?   B . n 
B 1 695 CYS 695 695 ?   ?   ?   B . n 
B 1 696 LEU 696 696 ?   ?   ?   B . n 
B 1 697 SER 697 697 ?   ?   ?   B . n 
B 1 698 CYS 698 698 ?   ?   ?   B . n 
B 1 699 VAL 699 699 ?   ?   ?   B . n 
B 1 700 VAL 700 700 ?   ?   ?   B . n 
C 2 1   MET 1   -20 ?   ?   ?   C . n 
C 2 2   GLY 2   -19 ?   ?   ?   C . n 
C 2 3   SER 3   -18 ?   ?   ?   C . n 
C 2 4   SER 4   -17 ?   ?   ?   C . n 
C 2 5   HIS 5   -16 ?   ?   ?   C . n 
C 2 6   HIS 6   -15 ?   ?   ?   C . n 
C 2 7   HIS 7   -14 ?   ?   ?   C . n 
C 2 8   HIS 8   -13 ?   ?   ?   C . n 
C 2 9   HIS 9   -12 ?   ?   ?   C . n 
C 2 10  HIS 10  -11 ?   ?   ?   C . n 
C 2 11  SER 11  -10 ?   ?   ?   C . n 
C 2 12  SER 12  -9  ?   ?   ?   C . n 
C 2 13  GLY 13  -8  ?   ?   ?   C . n 
C 2 14  LEU 14  -7  ?   ?   ?   C . n 
C 2 15  VAL 15  -6  ?   ?   ?   C . n 
C 2 16  PRO 16  -5  ?   ?   ?   C . n 
C 2 17  ARG 17  -4  ?   ?   ?   C . n 
C 2 18  GLY 18  -3  ?   ?   ?   C . n 
C 2 19  SER 19  -2  ?   ?   ?   C . n 
C 2 20  HIS 20  -1  ?   ?   ?   C . n 
C 2 21  MET 21  0   ?   ?   ?   C . n 
C 2 22  MET 22  1   ?   ?   ?   C . n 
C 2 23  THR 23  2   ?   ?   ?   C . n 
C 2 24  LYS 24  3   ?   ?   ?   C . n 
C 2 25  ILE 25  4   ?   ?   ?   C . n 
C 2 26  TYR 26  5   ?   ?   ?   C . n 
C 2 27  ASP 27  6   ?   ?   ?   C . n 
C 2 28  ALA 28  7   ?   ?   ?   C . n 
C 2 29  ALA 29  8   ?   ?   ?   C . n 
C 2 30  ASN 30  9   ?   ?   ?   C . n 
C 2 31  TRP 31  10  ?   ?   ?   C . n 
C 2 32  SER 32  11  ?   ?   ?   C . n 
C 2 33  LYS 33  12  ?   ?   ?   C . n 
C 2 34  HIS 34  13  ?   ?   ?   C . n 
C 2 35  GLU 35  14  ?   ?   ?   C . n 
C 2 36  ASP 36  15  ?   ?   ?   C . n 
C 2 37  ASP 37  16  16  ASP ASP C . n 
C 2 38  PHE 38  17  17  PHE PHE C . n 
C 2 39  THR 39  18  18  THR THR C . n 
C 2 40  GLN 40  19  19  GLN GLN C . n 
C 2 41  MET 41  20  20  MET MET C . n 
C 2 42  PHE 42  21  21  PHE PHE C . n 
C 2 43  TYR 43  22  22  TYR TYR C . n 
C 2 44  ASN 44  23  23  ASN ASN C . n 
C 2 45  GLN 45  24  24  GLN GLN C . n 
C 2 46  ASN 46  25  25  ASN ASN C . n 
C 2 47  VAL 47  26  26  VAL VAL C . n 
C 2 48  LYS 48  27  27  LYS LYS C . n 
C 2 49  GLN 49  28  28  GLN GLN C . n 
C 2 50  PHE 50  29  29  PHE PHE C . n 
C 2 51  TRP 51  30  30  TRP TRP C . n 
C 2 52  LEU 52  31  31  LEU LEU C . n 
C 2 53  PRO 53  32  32  PRO PRO C . n 
C 2 54  GLU 54  33  33  GLU GLU C . n 
C 2 55  GLU 55  34  34  GLU GLU C . n 
C 2 56  ILE 56  35  35  ILE ILE C . n 
C 2 57  ALA 57  36  36  ALA ALA C . n 
C 2 58  LEU 58  37  37  LEU LEU C . n 
C 2 59  ASN 59  38  38  ASN ASN C . n 
C 2 60  GLY 60  39  39  GLY GLY C . n 
C 2 61  ASP 61  40  40  ASP ASP C . n 
C 2 62  LEU 62  41  41  LEU LEU C . n 
C 2 63  LEU 63  42  42  LEU LEU C . n 
C 2 64  THR 64  43  43  THR THR C . n 
C 2 65  TRP 65  44  44  TRP TRP C . n 
C 2 66  LYS 66  45  45  LYS LYS C . n 
C 2 67  TYR 67  46  46  TYR TYR C . n 
C 2 68  LEU 68  47  47  LEU LEU C . n 
C 2 69  GLY 69  48  48  GLY GLY C . n 
C 2 70  LYS 70  49  49  LYS LYS C . n 
C 2 71  ASN 71  50  50  ASN ASN C . n 
C 2 72  GLU 72  51  51  GLU GLU C . n 
C 2 73  GLN 73  52  52  GLN GLN C . n 
C 2 74  ASP 74  53  53  ASP ASP C . n 
C 2 75  THR 75  54  54  THR THR C . n 
C 2 76  TYR 76  55  55  TYR TYR C . n 
C 2 77  MET 77  56  56  MET MET C . n 
C 2 78  LYS 78  57  57  LYS LYS C . n 
C 2 79  VAL 79  58  58  VAL VAL C . n 
C 2 80  LEU 80  59  59  LEU LEU C . n 
C 2 81  ALA 81  60  60  ALA ALA C . n 
C 2 82  GLY 82  61  61  GLY GLY C . n 
C 2 83  LEU 83  62  62  LEU LEU C . n 
C 2 84  THR 84  63  63  THR THR C . n 
C 2 85  LEU 85  64  64  LEU LEU C . n 
C 2 86  LEU 86  65  65  LEU LEU C . n 
C 2 87  ASP 87  66  66  ASP ASP C . n 
C 2 88  THR 88  67  67  THR THR C . n 
C 2 89  GLU 89  68  68  GLU GLU C . n 
C 2 90  GLN 90  69  69  GLN GLN C . n 
C 2 91  GLY 91  70  70  GLY GLY C . n 
C 2 92  ASN 92  71  71  ASN ASN C . n 
C 2 93  THR 93  72  72  THR THR C . n 
C 2 94  GLY 94  73  73  GLY GLY C . n 
C 2 95  MET 95  74  74  MET MET C . n 
C 2 96  PRO 96  75  75  PRO PRO C . n 
C 2 97  ILE 97  76  76  ILE ILE C . n 
C 2 98  VAL 98  77  77  VAL VAL C . n 
C 2 99  ALA 99  78  78  ALA ALA C . n 
C 2 100 GLU 100 79  79  GLU GLU C . n 
C 2 101 HIS 101 80  80  HIS HIS C . n 
C 2 102 VAL 102 81  81  VAL VAL C . n 
C 2 103 ASP 103 82  82  ASP ASP C . n 
C 2 104 GLY 104 83  83  GLY GLY C . n 
C 2 105 HIS 105 84  84  HIS HIS C . n 
C 2 106 GLN 106 85  85  GLN GLN C . n 
C 2 107 ARG 107 86  86  ARG ARG C . n 
C 2 108 LYS 108 87  87  LYS LYS C . n 
C 2 109 ALA 109 88  88  ALA ALA C . n 
C 2 110 VAL 110 89  89  VAL VAL C . n 
C 2 111 LEU 111 90  90  LEU LEU C . n 
C 2 112 ASN 112 91  91  ASN ASN C . n 
C 2 113 PHE 113 92  92  PHE PHE C . n 
C 2 114 MET 114 93  93  MET MET C . n 
C 2 115 ALA 115 94  94  ALA ALA C . n 
C 2 116 MET 116 95  95  MET MET C . n 
C 2 117 MET 117 96  96  MET MET C . n 
C 2 118 GLU 118 97  97  GLU GLU C . n 
C 2 119 ASN 119 98  98  ASN ASN C . n 
C 2 120 ALA 120 99  99  ALA ALA C . n 
C 2 121 VAL 121 100 100 VAL VAL C . n 
C 2 122 HIS 122 101 101 HIS HIS C . n 
C 2 123 ALA 123 102 102 ALA ALA C . n 
C 2 124 LYS 124 103 103 LYS LYS C . n 
C 2 125 SER 125 104 104 SER SER C . n 
C 2 126 TYR 126 105 105 TYR TYR C . n 
C 2 127 SER 127 106 106 SER SER C . n 
C 2 128 ASN 128 107 107 ASN ASN C . n 
C 2 129 ILE 129 108 108 ILE ILE C . n 
C 2 130 PHE 130 109 109 PHE PHE C . n 
C 2 131 MET 131 110 110 MET MET C . n 
C 2 132 THR 132 111 111 THR THR C . n 
C 2 133 LEU 133 112 112 LEU LEU C . n 
C 2 134 ALA 134 113 113 ALA ALA C . n 
C 2 135 PRO 135 114 114 PRO PRO C . n 
C 2 136 THR 136 115 115 THR THR C . n 
C 2 137 GLU 137 116 116 GLU GLU C . n 
C 2 138 THR 138 117 117 THR THR C . n 
C 2 139 ILE 139 118 118 ILE ILE C . n 
C 2 140 ASN 140 119 119 ASN ASN C . n 
C 2 141 GLU 141 120 120 GLU GLU C . n 
C 2 142 VAL 142 121 121 VAL VAL C . n 
C 2 143 PHE 143 122 122 PHE PHE C . n 
C 2 144 GLU 144 123 123 GLU GLU C . n 
C 2 145 TRP 145 124 124 TRP TRP C . n 
C 2 146 VAL 146 125 125 VAL VAL C . n 
C 2 147 LYS 147 126 126 LYS LYS C . n 
C 2 148 GLN 148 127 127 GLN GLN C . n 
C 2 149 ASN 149 128 128 ASN ASN C . n 
C 2 150 LYS 150 129 129 LYS LYS C . n 
C 2 151 TYR 151 130 130 TYR TYR C . n 
C 2 152 LEU 152 131 131 LEU LEU C . n 
C 2 153 GLN 153 132 132 GLN GLN C . n 
C 2 154 LYS 154 133 133 LYS LYS C . n 
C 2 155 LYS 155 134 134 LYS LYS C . n 
C 2 156 ALA 156 135 135 ALA ALA C . n 
C 2 157 GLN 157 136 136 GLN GLN C . n 
C 2 158 MET 158 137 137 MET MET C . n 
C 2 159 ILE 159 138 138 ILE ILE C . n 
C 2 160 VAL 160 139 139 VAL VAL C . n 
C 2 161 GLY 161 140 140 GLY GLY C . n 
C 2 162 LEU 162 141 141 LEU LEU C . n 
C 2 163 TYR 163 142 142 TYR TYR C . n 
C 2 164 LYS 164 143 143 LYS LYS C . n 
C 2 165 ALA 165 144 144 ALA ALA C . n 
C 2 166 ILE 166 145 145 ILE ILE C . n 
C 2 167 GLN 167 146 146 GLN GLN C . n 
C 2 168 LYS 168 147 147 LYS LYS C . n 
C 2 169 ASP 169 148 148 ASP ASP C . n 
C 2 170 ASP 170 149 149 ASP ASP C . n 
C 2 171 GLU 171 150 150 GLU GLU C . n 
C 2 172 ILE 172 151 151 ILE ILE C . n 
C 2 173 SER 173 152 152 SER SER C . n 
C 2 174 LEU 174 153 153 LEU LEU C . n 
C 2 175 PHE 175 154 154 PHE PHE C . n 
C 2 176 LYS 176 155 155 LYS LYS C . n 
C 2 177 ALA 177 156 156 ALA ALA C . n 
C 2 178 MET 178 157 157 MET MET C . n 
C 2 179 VAL 179 158 158 VAL VAL C . n 
C 2 180 ALA 180 159 159 ALA ALA C . n 
C 2 181 SER 181 160 160 SER SER C . n 
C 2 182 VAL 182 161 161 VAL VAL C . n 
C 2 183 TYR 183 162 162 TYR TYR C . n 
C 2 184 LEU 184 163 163 LEU LEU C . n 
C 2 185 GLU 185 164 164 GLU GLU C . n 
C 2 186 SER 186 165 165 SER SER C . n 
C 2 187 PHE 187 166 166 PHE PHE C . n 
C 2 188 LEU 188 167 167 LEU LEU C . n 
C 2 189 PHE 189 168 168 PHE PHE C . n 
C 2 190 TYR 190 169 169 TYR TYR C . n 
C 2 191 SER 191 170 170 SER SER C . n 
C 2 192 GLY 192 171 171 GLY GLY C . n 
C 2 193 PHE 193 172 172 PHE PHE C . n 
C 2 194 TYR 194 173 173 TYR TYR C . n 
C 2 195 TYR 195 174 174 TYR TYR C . n 
C 2 196 PRO 196 175 175 PRO PRO C . n 
C 2 197 LEU 197 176 176 LEU LEU C . n 
C 2 198 TYR 198 177 177 TYR TYR C . n 
C 2 199 PHE 199 178 178 PHE PHE C . n 
C 2 200 TYR 200 179 179 TYR TYR C . n 
C 2 201 GLY 201 180 180 GLY GLY C . n 
C 2 202 GLN 202 181 181 GLN GLN C . n 
C 2 203 GLY 203 182 182 GLY GLY C . n 
C 2 204 LYS 204 183 183 LYS LYS C . n 
C 2 205 LEU 205 184 184 LEU LEU C . n 
C 2 206 MET 206 185 185 MET MET C . n 
C 2 207 GLN 207 186 186 GLN GLN C . n 
C 2 208 SER 208 187 187 SER SER C . n 
C 2 209 GLY 209 188 188 GLY GLY C . n 
C 2 210 GLU 210 189 189 GLU GLU C . n 
C 2 211 ILE 211 190 190 ILE ILE C . n 
C 2 212 ILE 212 191 191 ILE ILE C . n 
C 2 213 ASN 213 192 192 ASN ASN C . n 
C 2 214 LEU 214 193 193 LEU LEU C . n 
C 2 215 ILE 215 194 194 ILE ILE C . n 
C 2 216 LEU 216 195 195 LEU LEU C . n 
C 2 217 ARG 217 196 196 ARG ARG C . n 
C 2 218 ASP 218 197 197 ASP ASP C . n 
C 2 219 GLU 219 198 198 GLU GLU C . n 
C 2 220 ALA 220 199 199 ALA ALA C . n 
C 2 221 ILE 221 200 200 ILE ILE C . n 
C 2 222 HIS 222 201 201 HIS HIS C . n 
C 2 223 GLY 223 202 202 GLY GLY C . n 
C 2 224 VAL 224 203 203 VAL VAL C . n 
C 2 225 TYR 225 204 204 TYR TYR C . n 
C 2 226 VAL 226 205 205 VAL VAL C . n 
C 2 227 GLY 227 206 206 GLY GLY C . n 
C 2 228 LEU 228 207 207 LEU LEU C . n 
C 2 229 LEU 229 208 208 LEU LEU C . n 
C 2 230 ALA 230 209 209 ALA ALA C . n 
C 2 231 GLN 231 210 210 GLN GLN C . n 
C 2 232 GLU 232 211 211 GLU GLU C . n 
C 2 233 ILE 233 212 212 ILE ILE C . n 
C 2 234 TYR 234 213 213 TYR TYR C . n 
C 2 235 ASN 235 214 214 ASN ASN C . n 
C 2 236 LYS 236 215 215 LYS LYS C . n 
C 2 237 GLN 237 216 216 GLN GLN C . n 
C 2 238 THR 238 217 217 THR THR C . n 
C 2 239 GLU 239 218 218 GLU GLU C . n 
C 2 240 GLU 240 219 219 GLU GLU C . n 
C 2 241 LYS 241 220 220 LYS LYS C . n 
C 2 242 LYS 242 221 221 LYS LYS C . n 
C 2 243 ALA 243 222 222 ALA ALA C . n 
C 2 244 GLU 244 223 223 GLU GLU C . n 
C 2 245 LEU 245 224 224 LEU LEU C . n 
C 2 246 ARG 246 225 225 ARG ARG C . n 
C 2 247 GLU 247 226 226 GLU GLU C . n 
C 2 248 PHE 248 227 227 PHE PHE C . n 
C 2 249 ALA 249 228 228 ALA ALA C . n 
C 2 250 ILE 250 229 229 ILE ILE C . n 
C 2 251 ASP 251 230 230 ASP ASP C . n 
C 2 252 LEU 252 231 231 LEU LEU C . n 
C 2 253 LEU 253 232 232 LEU LEU C . n 
C 2 254 ASN 254 233 233 ASN ASN C . n 
C 2 255 GLN 255 234 234 GLN GLN C . n 
C 2 256 LEU 256 235 235 LEU LEU C . n 
C 2 257 TYR 257 236 236 TYR TYR C . n 
C 2 258 GLU 258 237 237 GLU GLU C . n 
C 2 259 ASN 259 238 238 ASN ASN C . n 
C 2 260 GLU 260 239 239 GLU GLU C . n 
C 2 261 LEU 261 240 240 LEU LEU C . n 
C 2 262 GLU 262 241 241 GLU GLU C . n 
C 2 263 TYR 263 242 242 TYR TYR C . n 
C 2 264 THR 264 243 243 THR THR C . n 
C 2 265 GLU 265 244 244 GLU GLU C . n 
C 2 266 ASP 266 245 245 ASP ASP C . n 
C 2 267 LEU 267 246 246 LEU LEU C . n 
C 2 268 TYR 268 247 247 TYR TYR C . n 
C 2 269 ASP 269 248 248 ASP ASP C . n 
C 2 270 GLN 270 249 249 GLN GLN C . n 
C 2 271 VAL 271 250 250 VAL VAL C . n 
C 2 272 GLY 272 251 251 GLY GLY C . n 
C 2 273 LEU 273 252 252 LEU LEU C . n 
C 2 274 SER 274 253 253 SER SER C . n 
C 2 275 HIS 275 254 254 HIS HIS C . n 
C 2 276 ASP 276 255 255 ASP ASP C . n 
C 2 277 VAL 277 256 256 VAL VAL C . n 
C 2 278 LYS 278 257 257 LYS LYS C . n 
C 2 279 LYS 279 258 258 LYS LYS C . n 
C 2 280 PHE 280 259 259 PHE PHE C . n 
C 2 281 ILE 281 260 260 ILE ILE C . n 
C 2 282 ARG 282 261 261 ARG ARG C . n 
C 2 283 TYR 283 262 262 TYR TYR C . n 
C 2 284 ASN 284 263 263 ASN ASN C . n 
C 2 285 ALA 285 264 264 ALA ALA C . n 
C 2 286 ASN 286 265 265 ASN ASN C . n 
C 2 287 LYS 287 266 266 LYS LYS C . n 
C 2 288 ALA 288 267 267 ALA ALA C . n 
C 2 289 LEU 289 268 268 LEU LEU C . n 
C 2 290 MET 290 269 269 MET MET C . n 
C 2 291 ASN 291 270 270 ASN ASN C . n 
C 2 292 LEU 292 271 271 LEU LEU C . n 
C 2 293 GLY 293 272 272 GLY GLY C . n 
C 2 294 PHE 294 273 273 PHE PHE C . n 
C 2 295 ASP 295 274 274 ASP ASP C . n 
C 2 296 PRO 296 275 275 PRO PRO C . n 
C 2 297 TYR 297 276 276 TYR TYR C . n 
C 2 298 PHE 298 277 277 PHE PHE C . n 
C 2 299 GLU 299 278 278 GLU GLU C . n 
C 2 300 GLU 300 279 279 GLU GLU C . n 
C 2 301 GLU 301 280 280 GLU GLU C . n 
C 2 302 ASP 302 281 281 ASP ASP C . n 
C 2 303 ILE 303 282 282 ILE ILE C . n 
C 2 304 ASN 304 283 283 ASN ASN C . n 
C 2 305 PRO 305 284 284 PRO PRO C . n 
C 2 306 ILE 306 285 285 ILE ILE C . n 
C 2 307 VAL 307 286 286 VAL VAL C . n 
C 2 308 LEU 308 287 287 LEU LEU C . n 
C 2 309 ASN 309 288 288 ASN ASN C . n 
C 2 310 GLY 310 289 289 GLY GLY C . n 
C 2 311 LEU 311 290 290 LEU LEU C . n 
C 2 312 ASN 312 291 ?   ?   ?   C . n 
C 2 313 THR 313 292 ?   ?   ?   C . n 
C 2 314 LYS 314 293 ?   ?   ?   C . n 
C 2 315 THR 315 294 ?   ?   ?   C . n 
C 2 316 LYS 316 295 ?   ?   ?   C . n 
C 2 317 SER 317 296 ?   ?   ?   C . n 
C 2 318 HIS 318 297 ?   ?   ?   C . n 
C 2 319 ASP 319 298 ?   ?   ?   C . n 
C 2 320 PHE 320 299 ?   ?   ?   C . n 
C 2 321 PHE 321 300 ?   ?   ?   C . n 
C 2 322 SER 322 301 ?   ?   ?   C . n 
C 2 323 MET 323 302 ?   ?   ?   C . n 
C 2 324 LYS 324 303 ?   ?   ?   C . n 
C 2 325 GLY 325 304 ?   ?   ?   C . n 
C 2 326 ASN 326 305 ?   ?   ?   C . n 
C 2 327 GLY 327 306 ?   ?   ?   C . n 
C 2 328 TYR 328 307 ?   ?   ?   C . n 
C 2 329 LYS 329 308 ?   ?   ?   C . n 
C 2 330 LYS 330 309 309 LYS LYS C . n 
C 2 331 ALA 331 310 310 ALA ALA C . n 
C 2 332 THR 332 311 311 THR THR C . n 
C 2 333 VAL 333 312 312 VAL VAL C . n 
C 2 334 GLU 334 313 313 GLU GLU C . n 
C 2 335 PRO 335 314 314 PRO PRO C . n 
C 2 336 LEU 336 315 315 LEU LEU C . n 
C 2 337 LYS 337 316 316 LYS LYS C . n 
C 2 338 ASP 338 317 317 ASP ASP C . n 
C 2 339 ASP 339 318 318 ASP ASP C . n 
C 2 340 ASP 340 319 319 ASP ASP C . n 
C 2 341 PHE 341 320 320 PHE PHE C . n 
C 2 342 TYR 342 321 321 TYR TYR C . n 
C 2 343 PHE 343 322 322 PHE PHE C . n 
C 2 344 GLU 344 323 ?   ?   ?   C . n 
C 2 345 ASP 345 324 ?   ?   ?   C . n 
C 2 346 GLU 346 325 ?   ?   ?   C . n 
C 2 347 LYS 347 326 ?   ?   ?   C . n 
C 2 348 GLU 348 327 ?   ?   ?   C . n 
C 2 349 GLN 349 328 ?   ?   ?   C . n 
C 2 350 ILE 350 329 ?   ?   ?   C . n 
D 2 1   MET 1   -20 ?   ?   ?   D . n 
D 2 2   GLY 2   -19 ?   ?   ?   D . n 
D 2 3   SER 3   -18 ?   ?   ?   D . n 
D 2 4   SER 4   -17 ?   ?   ?   D . n 
D 2 5   HIS 5   -16 ?   ?   ?   D . n 
D 2 6   HIS 6   -15 ?   ?   ?   D . n 
D 2 7   HIS 7   -14 ?   ?   ?   D . n 
D 2 8   HIS 8   -13 ?   ?   ?   D . n 
D 2 9   HIS 9   -12 ?   ?   ?   D . n 
D 2 10  HIS 10  -11 ?   ?   ?   D . n 
D 2 11  SER 11  -10 ?   ?   ?   D . n 
D 2 12  SER 12  -9  ?   ?   ?   D . n 
D 2 13  GLY 13  -8  ?   ?   ?   D . n 
D 2 14  LEU 14  -7  ?   ?   ?   D . n 
D 2 15  VAL 15  -6  ?   ?   ?   D . n 
D 2 16  PRO 16  -5  ?   ?   ?   D . n 
D 2 17  ARG 17  -4  ?   ?   ?   D . n 
D 2 18  GLY 18  -3  ?   ?   ?   D . n 
D 2 19  SER 19  -2  ?   ?   ?   D . n 
D 2 20  HIS 20  -1  ?   ?   ?   D . n 
D 2 21  MET 21  0   ?   ?   ?   D . n 
D 2 22  MET 22  1   ?   ?   ?   D . n 
D 2 23  THR 23  2   ?   ?   ?   D . n 
D 2 24  LYS 24  3   ?   ?   ?   D . n 
D 2 25  ILE 25  4   ?   ?   ?   D . n 
D 2 26  TYR 26  5   ?   ?   ?   D . n 
D 2 27  ASP 27  6   ?   ?   ?   D . n 
D 2 28  ALA 28  7   ?   ?   ?   D . n 
D 2 29  ALA 29  8   ?   ?   ?   D . n 
D 2 30  ASN 30  9   ?   ?   ?   D . n 
D 2 31  TRP 31  10  ?   ?   ?   D . n 
D 2 32  SER 32  11  ?   ?   ?   D . n 
D 2 33  LYS 33  12  ?   ?   ?   D . n 
D 2 34  HIS 34  13  ?   ?   ?   D . n 
D 2 35  GLU 35  14  ?   ?   ?   D . n 
D 2 36  ASP 36  15  ?   ?   ?   D . n 
D 2 37  ASP 37  16  16  ASP ASP D . n 
D 2 38  PHE 38  17  17  PHE PHE D . n 
D 2 39  THR 39  18  18  THR THR D . n 
D 2 40  GLN 40  19  19  GLN GLN D . n 
D 2 41  MET 41  20  20  MET MET D . n 
D 2 42  PHE 42  21  21  PHE PHE D . n 
D 2 43  TYR 43  22  22  TYR TYR D . n 
D 2 44  ASN 44  23  23  ASN ASN D . n 
D 2 45  GLN 45  24  24  GLN GLN D . n 
D 2 46  ASN 46  25  25  ASN ASN D . n 
D 2 47  VAL 47  26  26  VAL VAL D . n 
D 2 48  LYS 48  27  27  LYS LYS D . n 
D 2 49  GLN 49  28  28  GLN GLN D . n 
D 2 50  PHE 50  29  29  PHE PHE D . n 
D 2 51  TRP 51  30  30  TRP TRP D . n 
D 2 52  LEU 52  31  31  LEU LEU D . n 
D 2 53  PRO 53  32  32  PRO PRO D . n 
D 2 54  GLU 54  33  33  GLU GLU D . n 
D 2 55  GLU 55  34  34  GLU GLU D . n 
D 2 56  ILE 56  35  35  ILE ILE D . n 
D 2 57  ALA 57  36  36  ALA ALA D . n 
D 2 58  LEU 58  37  37  LEU LEU D . n 
D 2 59  ASN 59  38  38  ASN ASN D . n 
D 2 60  GLY 60  39  39  GLY GLY D . n 
D 2 61  ASP 61  40  40  ASP ASP D . n 
D 2 62  LEU 62  41  41  LEU LEU D . n 
D 2 63  LEU 63  42  42  LEU LEU D . n 
D 2 64  THR 64  43  43  THR THR D . n 
D 2 65  TRP 65  44  44  TRP TRP D . n 
D 2 66  LYS 66  45  45  LYS LYS D . n 
D 2 67  TYR 67  46  46  TYR TYR D . n 
D 2 68  LEU 68  47  47  LEU LEU D . n 
D 2 69  GLY 69  48  48  GLY GLY D . n 
D 2 70  LYS 70  49  49  LYS LYS D . n 
D 2 71  ASN 71  50  50  ASN ASN D . n 
D 2 72  GLU 72  51  51  GLU GLU D . n 
D 2 73  GLN 73  52  52  GLN GLN D . n 
D 2 74  ASP 74  53  53  ASP ASP D . n 
D 2 75  THR 75  54  54  THR THR D . n 
D 2 76  TYR 76  55  55  TYR TYR D . n 
D 2 77  MET 77  56  56  MET MET D . n 
D 2 78  LYS 78  57  57  LYS LYS D . n 
D 2 79  VAL 79  58  58  VAL VAL D . n 
D 2 80  LEU 80  59  59  LEU LEU D . n 
D 2 81  ALA 81  60  60  ALA ALA D . n 
D 2 82  GLY 82  61  61  GLY GLY D . n 
D 2 83  LEU 83  62  62  LEU LEU D . n 
D 2 84  THR 84  63  63  THR THR D . n 
D 2 85  LEU 85  64  64  LEU LEU D . n 
D 2 86  LEU 86  65  65  LEU LEU D . n 
D 2 87  ASP 87  66  66  ASP ASP D . n 
D 2 88  THR 88  67  67  THR THR D . n 
D 2 89  GLU 89  68  68  GLU GLU D . n 
D 2 90  GLN 90  69  69  GLN GLN D . n 
D 2 91  GLY 91  70  70  GLY GLY D . n 
D 2 92  ASN 92  71  71  ASN ASN D . n 
D 2 93  THR 93  72  72  THR THR D . n 
D 2 94  GLY 94  73  73  GLY GLY D . n 
D 2 95  MET 95  74  74  MET MET D . n 
D 2 96  PRO 96  75  75  PRO PRO D . n 
D 2 97  ILE 97  76  76  ILE ILE D . n 
D 2 98  VAL 98  77  77  VAL VAL D . n 
D 2 99  ALA 99  78  78  ALA ALA D . n 
D 2 100 GLU 100 79  79  GLU GLU D . n 
D 2 101 HIS 101 80  80  HIS HIS D . n 
D 2 102 VAL 102 81  81  VAL VAL D . n 
D 2 103 ASP 103 82  82  ASP ASP D . n 
D 2 104 GLY 104 83  83  GLY GLY D . n 
D 2 105 HIS 105 84  84  HIS HIS D . n 
D 2 106 GLN 106 85  85  GLN GLN D . n 
D 2 107 ARG 107 86  86  ARG ARG D . n 
D 2 108 LYS 108 87  87  LYS LYS D . n 
D 2 109 ALA 109 88  88  ALA ALA D . n 
D 2 110 VAL 110 89  89  VAL VAL D . n 
D 2 111 LEU 111 90  90  LEU LEU D . n 
D 2 112 ASN 112 91  91  ASN ASN D . n 
D 2 113 PHE 113 92  92  PHE PHE D . n 
D 2 114 MET 114 93  93  MET MET D . n 
D 2 115 ALA 115 94  94  ALA ALA D . n 
D 2 116 MET 116 95  95  MET MET D . n 
D 2 117 MET 117 96  96  MET MET D . n 
D 2 118 GLU 118 97  97  GLU GLU D . n 
D 2 119 ASN 119 98  98  ASN ASN D . n 
D 2 120 ALA 120 99  99  ALA ALA D . n 
D 2 121 VAL 121 100 100 VAL VAL D . n 
D 2 122 HIS 122 101 101 HIS HIS D . n 
D 2 123 ALA 123 102 102 ALA ALA D . n 
D 2 124 LYS 124 103 103 LYS LYS D . n 
D 2 125 SER 125 104 104 SER SER D . n 
D 2 126 TYR 126 105 105 TYR TYR D . n 
D 2 127 SER 127 106 106 SER SER D . n 
D 2 128 ASN 128 107 107 ASN ASN D . n 
D 2 129 ILE 129 108 108 ILE ILE D . n 
D 2 130 PHE 130 109 109 PHE PHE D . n 
D 2 131 MET 131 110 110 MET MET D . n 
D 2 132 THR 132 111 111 THR THR D . n 
D 2 133 LEU 133 112 112 LEU LEU D . n 
D 2 134 ALA 134 113 113 ALA ALA D . n 
D 2 135 PRO 135 114 114 PRO PRO D . n 
D 2 136 THR 136 115 115 THR THR D . n 
D 2 137 GLU 137 116 116 GLU GLU D . n 
D 2 138 THR 138 117 117 THR THR D . n 
D 2 139 ILE 139 118 118 ILE ILE D . n 
D 2 140 ASN 140 119 119 ASN ASN D . n 
D 2 141 GLU 141 120 120 GLU GLU D . n 
D 2 142 VAL 142 121 121 VAL VAL D . n 
D 2 143 PHE 143 122 122 PHE PHE D . n 
D 2 144 GLU 144 123 123 GLU GLU D . n 
D 2 145 TRP 145 124 124 TRP TRP D . n 
D 2 146 VAL 146 125 125 VAL VAL D . n 
D 2 147 LYS 147 126 126 LYS LYS D . n 
D 2 148 GLN 148 127 127 GLN GLN D . n 
D 2 149 ASN 149 128 128 ASN ASN D . n 
D 2 150 LYS 150 129 129 LYS LYS D . n 
D 2 151 TYR 151 130 130 TYR TYR D . n 
D 2 152 LEU 152 131 131 LEU LEU D . n 
D 2 153 GLN 153 132 132 GLN GLN D . n 
D 2 154 LYS 154 133 133 LYS LYS D . n 
D 2 155 LYS 155 134 134 LYS LYS D . n 
D 2 156 ALA 156 135 135 ALA ALA D . n 
D 2 157 GLN 157 136 136 GLN GLN D . n 
D 2 158 MET 158 137 137 MET MET D . n 
D 2 159 ILE 159 138 138 ILE ILE D . n 
D 2 160 VAL 160 139 139 VAL VAL D . n 
D 2 161 GLY 161 140 140 GLY GLY D . n 
D 2 162 LEU 162 141 141 LEU LEU D . n 
D 2 163 TYR 163 142 142 TYR TYR D . n 
D 2 164 LYS 164 143 143 LYS LYS D . n 
D 2 165 ALA 165 144 144 ALA ALA D . n 
D 2 166 ILE 166 145 145 ILE ILE D . n 
D 2 167 GLN 167 146 146 GLN GLN D . n 
D 2 168 LYS 168 147 147 LYS LYS D . n 
D 2 169 ASP 169 148 148 ASP ASP D . n 
D 2 170 ASP 170 149 149 ASP ASP D . n 
D 2 171 GLU 171 150 150 GLU GLU D . n 
D 2 172 ILE 172 151 151 ILE ILE D . n 
D 2 173 SER 173 152 152 SER SER D . n 
D 2 174 LEU 174 153 153 LEU LEU D . n 
D 2 175 PHE 175 154 154 PHE PHE D . n 
D 2 176 LYS 176 155 155 LYS LYS D . n 
D 2 177 ALA 177 156 156 ALA ALA D . n 
D 2 178 MET 178 157 157 MET MET D . n 
D 2 179 VAL 179 158 158 VAL VAL D . n 
D 2 180 ALA 180 159 159 ALA ALA D . n 
D 2 181 SER 181 160 160 SER SER D . n 
D 2 182 VAL 182 161 161 VAL VAL D . n 
D 2 183 TYR 183 162 162 TYR TYR D . n 
D 2 184 LEU 184 163 163 LEU LEU D . n 
D 2 185 GLU 185 164 164 GLU GLU D . n 
D 2 186 SER 186 165 165 SER SER D . n 
D 2 187 PHE 187 166 166 PHE PHE D . n 
D 2 188 LEU 188 167 167 LEU LEU D . n 
D 2 189 PHE 189 168 168 PHE PHE D . n 
D 2 190 TYR 190 169 169 TYR TYR D . n 
D 2 191 SER 191 170 170 SER SER D . n 
D 2 192 GLY 192 171 171 GLY GLY D . n 
D 2 193 PHE 193 172 172 PHE PHE D . n 
D 2 194 TYR 194 173 173 TYR TYR D . n 
D 2 195 TYR 195 174 174 TYR TYR D . n 
D 2 196 PRO 196 175 175 PRO PRO D . n 
D 2 197 LEU 197 176 176 LEU LEU D . n 
D 2 198 TYR 198 177 177 TYR TYR D . n 
D 2 199 PHE 199 178 178 PHE PHE D . n 
D 2 200 TYR 200 179 179 TYR TYR D . n 
D 2 201 GLY 201 180 180 GLY GLY D . n 
D 2 202 GLN 202 181 181 GLN GLN D . n 
D 2 203 GLY 203 182 182 GLY GLY D . n 
D 2 204 LYS 204 183 183 LYS LYS D . n 
D 2 205 LEU 205 184 184 LEU LEU D . n 
D 2 206 MET 206 185 185 MET MET D . n 
D 2 207 GLN 207 186 186 GLN GLN D . n 
D 2 208 SER 208 187 187 SER SER D . n 
D 2 209 GLY 209 188 188 GLY GLY D . n 
D 2 210 GLU 210 189 189 GLU GLU D . n 
D 2 211 ILE 211 190 190 ILE ILE D . n 
D 2 212 ILE 212 191 191 ILE ILE D . n 
D 2 213 ASN 213 192 192 ASN ASN D . n 
D 2 214 LEU 214 193 193 LEU LEU D . n 
D 2 215 ILE 215 194 194 ILE ILE D . n 
D 2 216 LEU 216 195 195 LEU LEU D . n 
D 2 217 ARG 217 196 196 ARG ARG D . n 
D 2 218 ASP 218 197 197 ASP ASP D . n 
D 2 219 GLU 219 198 198 GLU GLU D . n 
D 2 220 ALA 220 199 199 ALA ALA D . n 
D 2 221 ILE 221 200 200 ILE ILE D . n 
D 2 222 HIS 222 201 201 HIS HIS D . n 
D 2 223 GLY 223 202 202 GLY GLY D . n 
D 2 224 VAL 224 203 203 VAL VAL D . n 
D 2 225 TYR 225 204 204 TYR TYR D . n 
D 2 226 VAL 226 205 205 VAL VAL D . n 
D 2 227 GLY 227 206 206 GLY GLY D . n 
D 2 228 LEU 228 207 207 LEU LEU D . n 
D 2 229 LEU 229 208 208 LEU LEU D . n 
D 2 230 ALA 230 209 209 ALA ALA D . n 
D 2 231 GLN 231 210 210 GLN GLN D . n 
D 2 232 GLU 232 211 211 GLU GLU D . n 
D 2 233 ILE 233 212 212 ILE ILE D . n 
D 2 234 TYR 234 213 213 TYR TYR D . n 
D 2 235 ASN 235 214 214 ASN ASN D . n 
D 2 236 LYS 236 215 215 LYS LYS D . n 
D 2 237 GLN 237 216 216 GLN GLN D . n 
D 2 238 THR 238 217 217 THR THR D . n 
D 2 239 GLU 239 218 218 GLU GLU D . n 
D 2 240 GLU 240 219 219 GLU GLU D . n 
D 2 241 LYS 241 220 220 LYS LYS D . n 
D 2 242 LYS 242 221 221 LYS LYS D . n 
D 2 243 ALA 243 222 222 ALA ALA D . n 
D 2 244 GLU 244 223 223 GLU GLU D . n 
D 2 245 LEU 245 224 224 LEU LEU D . n 
D 2 246 ARG 246 225 225 ARG ARG D . n 
D 2 247 GLU 247 226 226 GLU GLU D . n 
D 2 248 PHE 248 227 227 PHE PHE D . n 
D 2 249 ALA 249 228 228 ALA ALA D . n 
D 2 250 ILE 250 229 229 ILE ILE D . n 
D 2 251 ASP 251 230 230 ASP ASP D . n 
D 2 252 LEU 252 231 231 LEU LEU D . n 
D 2 253 LEU 253 232 232 LEU LEU D . n 
D 2 254 ASN 254 233 233 ASN ASN D . n 
D 2 255 GLN 255 234 234 GLN GLN D . n 
D 2 256 LEU 256 235 235 LEU LEU D . n 
D 2 257 TYR 257 236 236 TYR TYR D . n 
D 2 258 GLU 258 237 237 GLU GLU D . n 
D 2 259 ASN 259 238 238 ASN ASN D . n 
D 2 260 GLU 260 239 239 GLU GLU D . n 
D 2 261 LEU 261 240 240 LEU LEU D . n 
D 2 262 GLU 262 241 241 GLU GLU D . n 
D 2 263 TYR 263 242 242 TYR TYR D . n 
D 2 264 THR 264 243 243 THR THR D . n 
D 2 265 GLU 265 244 244 GLU GLU D . n 
D 2 266 ASP 266 245 245 ASP ASP D . n 
D 2 267 LEU 267 246 246 LEU LEU D . n 
D 2 268 TYR 268 247 247 TYR TYR D . n 
D 2 269 ASP 269 248 248 ASP ASP D . n 
D 2 270 GLN 270 249 249 GLN GLN D . n 
D 2 271 VAL 271 250 250 VAL VAL D . n 
D 2 272 GLY 272 251 251 GLY GLY D . n 
D 2 273 LEU 273 252 252 LEU LEU D . n 
D 2 274 SER 274 253 253 SER SER D . n 
D 2 275 HIS 275 254 254 HIS HIS D . n 
D 2 276 ASP 276 255 255 ASP ASP D . n 
D 2 277 VAL 277 256 256 VAL VAL D . n 
D 2 278 LYS 278 257 257 LYS LYS D . n 
D 2 279 LYS 279 258 258 LYS LYS D . n 
D 2 280 PHE 280 259 259 PHE PHE D . n 
D 2 281 ILE 281 260 260 ILE ILE D . n 
D 2 282 ARG 282 261 261 ARG ARG D . n 
D 2 283 TYR 283 262 262 TYR TYR D . n 
D 2 284 ASN 284 263 263 ASN ASN D . n 
D 2 285 ALA 285 264 264 ALA ALA D . n 
D 2 286 ASN 286 265 265 ASN ASN D . n 
D 2 287 LYS 287 266 266 LYS LYS D . n 
D 2 288 ALA 288 267 267 ALA ALA D . n 
D 2 289 LEU 289 268 268 LEU LEU D . n 
D 2 290 MET 290 269 269 MET MET D . n 
D 2 291 ASN 291 270 270 ASN ASN D . n 
D 2 292 LEU 292 271 271 LEU LEU D . n 
D 2 293 GLY 293 272 272 GLY GLY D . n 
D 2 294 PHE 294 273 273 PHE PHE D . n 
D 2 295 ASP 295 274 274 ASP ASP D . n 
D 2 296 PRO 296 275 275 PRO PRO D . n 
D 2 297 TYR 297 276 276 TYR TYR D . n 
D 2 298 PHE 298 277 277 PHE PHE D . n 
D 2 299 GLU 299 278 278 GLU GLU D . n 
D 2 300 GLU 300 279 279 GLU GLU D . n 
D 2 301 GLU 301 280 280 GLU GLU D . n 
D 2 302 ASP 302 281 281 ASP ASP D . n 
D 2 303 ILE 303 282 282 ILE ILE D . n 
D 2 304 ASN 304 283 283 ASN ASN D . n 
D 2 305 PRO 305 284 284 PRO PRO D . n 
D 2 306 ILE 306 285 285 ILE ILE D . n 
D 2 307 VAL 307 286 286 VAL VAL D . n 
D 2 308 LEU 308 287 287 LEU LEU D . n 
D 2 309 ASN 309 288 288 ASN ASN D . n 
D 2 310 GLY 310 289 289 GLY GLY D . n 
D 2 311 LEU 311 290 290 LEU LEU D . n 
D 2 312 ASN 312 291 ?   ?   ?   D . n 
D 2 313 THR 313 292 ?   ?   ?   D . n 
D 2 314 LYS 314 293 ?   ?   ?   D . n 
D 2 315 THR 315 294 ?   ?   ?   D . n 
D 2 316 LYS 316 295 ?   ?   ?   D . n 
D 2 317 SER 317 296 ?   ?   ?   D . n 
D 2 318 HIS 318 297 ?   ?   ?   D . n 
D 2 319 ASP 319 298 ?   ?   ?   D . n 
D 2 320 PHE 320 299 ?   ?   ?   D . n 
D 2 321 PHE 321 300 ?   ?   ?   D . n 
D 2 322 SER 322 301 ?   ?   ?   D . n 
D 2 323 MET 323 302 ?   ?   ?   D . n 
D 2 324 LYS 324 303 ?   ?   ?   D . n 
D 2 325 GLY 325 304 ?   ?   ?   D . n 
D 2 326 ASN 326 305 ?   ?   ?   D . n 
D 2 327 GLY 327 306 ?   ?   ?   D . n 
D 2 328 TYR 328 307 ?   ?   ?   D . n 
D 2 329 LYS 329 308 ?   ?   ?   D . n 
D 2 330 LYS 330 309 309 LYS LYS D . n 
D 2 331 ALA 331 310 310 ALA ALA D . n 
D 2 332 THR 332 311 311 THR THR D . n 
D 2 333 VAL 333 312 312 VAL VAL D . n 
D 2 334 GLU 334 313 313 GLU GLU D . n 
D 2 335 PRO 335 314 314 PRO PRO D . n 
D 2 336 LEU 336 315 315 LEU LEU D . n 
D 2 337 LYS 337 316 316 LYS LYS D . n 
D 2 338 ASP 338 317 317 ASP ASP D . n 
D 2 339 ASP 339 318 318 ASP ASP D . n 
D 2 340 ASP 340 319 319 ASP ASP D . n 
D 2 341 PHE 341 320 320 PHE PHE D . n 
D 2 342 TYR 342 321 321 TYR TYR D . n 
D 2 343 PHE 343 322 322 PHE PHE D . n 
D 2 344 GLU 344 323 ?   ?   ?   D . n 
D 2 345 ASP 345 324 ?   ?   ?   D . n 
D 2 346 GLU 346 325 ?   ?   ?   D . n 
D 2 347 LYS 347 326 ?   ?   ?   D . n 
D 2 348 GLU 348 327 ?   ?   ?   D . n 
D 2 349 GLN 349 328 ?   ?   ?   D . n 
D 2 350 ILE 350 329 ?   ?   ?   D . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ATP ? ? ATP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 GDP ? ? GDP ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
4 MN  ? ? MN  ? ? 'SUBJECT OF INVESTIGATION' ? 
5 TTP ? ? TTP ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 ATP 1 801 701 ATP ATP A . 
F 4 GDP 1 802 702 GDP GDP A . 
G 5 TTP 1 803 703 TTP TTP A . 
H 6 MG  1 804 704 MG  MG  A . 
I 5 TTP 1 801 701 TTP TTP B . 
J 6 MG  1 802 702 MG  MG  B . 
K 3 ATP 1 803 703 ATP ATP B . 
L 4 GDP 1 804 704 GDP GDP B . 
M 7 MN  1 401 401 MN  MN  C . 
N 7 MN  1 402 402 MN  MN  C . 
O 7 MN  1 401 401 MN  MN  D . 
P 7 MN  1 402 402 MN  MN  D . 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BYY 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BYY 
_struct.title                        'Class 9 model for turnover condition of Bacillus subtilis ribonucleotide reductase complex' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BYY 
_struct_keywords.text            'Ribonucleotide Reductase, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 5 ? 
J N N 6 ? 
K N N 3 ? 
L N N 4 ? 
M N N 7 ? 
N N N 7 ? 
O N N 7 ? 
P N N 7 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP RIR1_BACSU P50620 ? 1 
;MSQNQVPKWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTVFFHNLKEKLDYLVENQYYEEEFLSLYSFEDIKEV
FKTAYAKKFRFPSFMSAFKFYNDYALKTNDKKKILERYEDRISIVALFFANGDTEKAKEYVNLMINQEYQPSTPTFLNAG
RKRRGELVSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSKLRAKGEAIKDVENATKGVVGVMKLLDNAFRYADQM
GQRQGSGAAYLNIFHRDINDFLDTKKISADEDVRVKTLSIGVVIPDKFVELAREDKAAYVFYPHTIYKEYGQHMDEMDMN
EMYDKFVDNPRVKKEKINPRKLLEKLAMLRSESGYPYIMFQDNVNKVHANNHISKVKFSNLCSEVLQASQVSSYTDYDEE
DEIGLDISCNLGSLNILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVRRANKAMKSIGLGAMNLHGYLAQNGIAYE
SPEARDFANTFFMMVNFYSIQRSAEIAKEKGETFDQYEGSTYATGEYFDKYVSTDFSPKYEKIANLFEGMHIPTTEDWKK
LKAFVAEHGMYHSYRLCIAPTGSISYVQSSTASVMPIMERIEERTYGNSKTYYPMPGLASNNWFFYKEAYDMDMFKVVDM
IATIQQHIDQGISFTLFLKDTMTTRDLNRIDLYAHHRGIKTIYYARTKDTGQDSCLSCVV
;
1 
2 UNP RIR2_BACSU P50621 ? 2 
;MTKIYDAANWSKHEDDFTQMFYNQNVKQFWLPEEIALNGDLLTWKYLGKNEQDTYMKVLAGLTLLDTEQGNTGMPIVAEH
VDGHQRKAVLNFMAMMENAVHAKSYSNIFMTLAPTETINEVFEWVKQNKYLQKKAQMIVGLYKAIQKDDEISLFKAMVAS
VYLESFLFYSGFYYPLYFYGQGKLMQSGEIINLILRDEAIHGVYVGLLAQEIYNKQTEEKKAELREFAIDLLNQLYENEL
EYTEDLYDQVGLSHDVKKFIRYNANKALMNLGFDPYFEEEDINPIVLNGLNTKTKSHDFFSMKGNGYKKATVEPLKDDDF
YFEDEKEQI
;
1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9BYY A 1  ? 700 ? P50620 1 ? 700 ? 1 700 
2 1 9BYY B 1  ? 700 ? P50620 1 ? 700 ? 1 700 
3 2 9BYY C 22 ? 350 ? P50621 1 ? 329 ? 1 329 
4 2 9BYY 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 9BYY MET C 1  ? UNP P50621 ? ? 'initiating methionine' -20 1  
3 9BYY GLY C 2  ? UNP P50621 ? ? 'expression tag'        -19 2  
3 9BYY SER C 3  ? UNP P50621 ? ? 'expression tag'        -18 3  
3 9BYY SER C 4  ? UNP P50621 ? ? 'expression tag'        -17 4  
3 9BYY HIS C 5  ? UNP P50621 ? ? 'expression tag'        -16 5  
3 9BYY HIS C 6  ? UNP P50621 ? ? 'expression tag'        -15 6  
3 9BYY HIS C 7  ? UNP P50621 ? ? 'expression tag'        -14 7  
3 9BYY HIS C 8  ? UNP P50621 ? ? 'expression tag'        -13 8  
3 9BYY HIS C 9  ? UNP P50621 ? ? 'expression tag'        -12 9  
3 9BYY HIS C 10 ? UNP P50621 ? ? 'expression tag'        -11 10 
3 9BYY SER C 11 ? UNP P50621 ? ? 'expression tag'        -10 11 
3 9BYY SER C 12 ? UNP P50621 ? ? 'expression tag'        -9  12 
3 9BYY GLY C 13 ? UNP P50621 ? ? 'expression tag'        -8  13 
3 9BYY LEU C 14 ? UNP P50621 ? ? 'expression tag'        -7  14 
3 9BYY VAL C 15 ? UNP P50621 ? ? 'expression tag'        -6  15 
3 9BYY PRO C 16 ? UNP P50621 ? ? 'expression tag'        -5  16 
3 9BYY ARG C 17 ? UNP P50621 ? ? 'expression tag'        -4  17 
3 9BYY GLY C 18 ? UNP P50621 ? ? 'expression tag'        -3  18 
3 9BYY SER C 19 ? UNP P50621 ? ? 'expression tag'        -2  19 
3 9BYY HIS C 20 ? UNP P50621 ? ? 'expression tag'        -1  20 
3 9BYY MET C 21 ? UNP P50621 ? ? 'expression tag'        0   21 
4 9BYY MET D 1  ? UNP P50621 ? ? 'initiating methionine' -20 22 
4 9BYY GLY D 2  ? UNP P50621 ? ? 'expression tag'        -19 23 
4 9BYY SER D 3  ? UNP P50621 ? ? 'expression tag'        -18 24 
4 9BYY SER D 4  ? UNP P50621 ? ? 'expression tag'        -17 25 
4 9BYY HIS D 5  ? UNP P50621 ? ? 'expression tag'        -16 26 
4 9BYY HIS D 6  ? UNP P50621 ? ? 'expression tag'        -15 27 
4 9BYY HIS D 7  ? UNP P50621 ? ? 'expression tag'        -14 28 
4 9BYY HIS D 8  ? UNP P50621 ? ? 'expression tag'        -13 29 
4 9BYY HIS D 9  ? UNP P50621 ? ? 'expression tag'        -12 30 
4 9BYY HIS D 10 ? UNP P50621 ? ? 'expression tag'        -11 31 
4 9BYY SER D 11 ? UNP P50621 ? ? 'expression tag'        -10 32 
4 9BYY SER D 12 ? UNP P50621 ? ? 'expression tag'        -9  33 
4 9BYY GLY D 13 ? UNP P50621 ? ? 'expression tag'        -8  34 
4 9BYY LEU D 14 ? UNP P50621 ? ? 'expression tag'        -7  35 
4 9BYY VAL D 15 ? UNP P50621 ? ? 'expression tag'        -6  36 
4 9BYY PRO D 16 ? UNP P50621 ? ? 'expression tag'        -5  37 
4 9BYY ARG D 17 ? UNP P50621 ? ? 'expression tag'        -4  38 
4 9BYY GLY D 18 ? UNP P50621 ? ? 'expression tag'        -3  39 
4 9BYY SER D 19 ? UNP P50621 ? ? 'expression tag'        -2  40 
4 9BYY HIS D 20 ? UNP P50621 ? ? 'expression tag'        -1  41 
4 9BYY MET D 21 ? UNP P50621 ? ? 'expression tag'        0   42 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 7   ? GLU A 15  ? PRO A 7   GLU A 15  1 ? 9  
HELX_P HELX_P2  AA2 GLN A 25  ? ASP A 39  ? GLN A 25  ASP A 39  1 ? 15 
HELX_P HELX_P3  AA3 ASN A 50  ? ASN A 61  ? ASN A 50  ASN A 61  1 ? 12 
HELX_P HELX_P4  AA4 GLU A 65  ? LEU A 71  ? GLU A 65  LEU A 71  1 ? 7  
HELX_P HELX_P5  AA5 SER A 73  ? LYS A 87  ? SER A 73  LYS A 87  1 ? 15 
HELX_P HELX_P6  AA6 SER A 93  ? TYR A 104 ? SER A 93  TYR A 104 1 ? 12 
HELX_P HELX_P7  AA7 ARG A 117 ? ASN A 131 ? ARG A 117 ASN A 131 1 ? 15 
HELX_P HELX_P8  AA8 ASP A 133 ? ASN A 146 ? ASP A 133 ASN A 146 1 ? 14 
HELX_P HELX_P9  AA9 SER A 152 ? ALA A 159 ? SER A 152 ALA A 159 1 ? 8  
HELX_P HELX_P10 AB1 SER A 178 ? LEU A 195 ? SER A 178 LEU A 195 1 ? 18 
HELX_P HELX_P11 AB2 LYS A 221 ? ALA A 237 ? LYS A 221 ALA A 237 1 ? 17 
HELX_P HELX_P12 AB3 ASP A 257 ? THR A 264 ? ASP A 257 THR A 264 1 ? 8  
HELX_P HELX_P13 AB4 PRO A 285 ? GLU A 294 ? PRO A 285 GLU A 294 1 ? 10 
HELX_P HELX_P14 AB5 TYR A 302 ? GLY A 311 ? TYR A 302 GLY A 311 1 ? 10 
HELX_P HELX_P15 AB6 HIS A 313 ? MET A 317 ? HIS A 313 MET A 317 5 ? 5  
HELX_P HELX_P16 AB7 ASP A 318 ? ASN A 329 ? ASP A 318 ASN A 329 1 ? 12 
HELX_P HELX_P17 AB8 ASN A 338 ? GLY A 354 ? ASN A 338 GLY A 354 1 ? 17 
HELX_P HELX_P18 AB9 GLN A 361 ? LYS A 366 ? GLN A 361 LYS A 366 1 ? 6  
HELX_P HELX_P19 AC1 ILE A 416 ? HIS A 422 ? ILE A 416 HIS A 422 1 ? 7  
HELX_P HELX_P20 AC2 SER A 424 ? THR A 442 ? SER A 424 THR A 442 1 ? 19 
HELX_P HELX_P21 AC3 ALA A 448 ? LYS A 459 ? ALA A 448 LYS A 459 1 ? 12 
HELX_P HELX_P22 AC4 ASN A 467 ? ASN A 475 ? ASN A 467 ASN A 475 1 ? 9  
HELX_P HELX_P23 AC5 SER A 481 ? GLY A 511 ? SER A 481 GLY A 511 1 ? 31 
HELX_P HELX_P24 AC6 SER A 520 ? GLY A 525 ? SER A 520 GLY A 525 1 ? 6  
HELX_P HELX_P25 AC7 PHE A 528 ? THR A 534 ? PHE A 528 THR A 534 1 ? 7  
HELX_P HELX_P26 AC8 TYR A 540 ? PHE A 547 ? TYR A 540 PHE A 547 1 ? 8  
HELX_P HELX_P27 AC9 THR A 554 ? GLY A 569 ? THR A 554 GLY A 569 1 ? 16 
HELX_P HELX_P28 AD1 SER A 583 ? GLN A 588 ? SER A 583 GLN A 588 1 ? 6  
HELX_P HELX_P29 AD2 ASP A 633 ? GLN A 646 ? ASP A 633 GLN A 646 1 ? 14 
HELX_P HELX_P30 AD3 THR A 663 ? GLY A 678 ? THR A 663 GLY A 678 1 ? 16 
HELX_P HELX_P31 AD4 PRO B 7   ? GLU B 15  ? PRO B 7   GLU B 15  1 ? 9  
HELX_P HELX_P32 AD5 GLN B 25  ? TYR B 40  ? GLN B 25  TYR B 40  1 ? 16 
HELX_P HELX_P33 AD6 TYR B 40  ? THR B 45  ? TYR B 40  THR B 45  1 ? 6  
HELX_P HELX_P34 AD7 ASN B 50  ? ASN B 61  ? ASN B 50  ASN B 61  1 ? 12 
HELX_P HELX_P35 AD8 GLU B 65  ? LEU B 71  ? GLU B 65  LEU B 71  1 ? 7  
HELX_P HELX_P36 AD9 SER B 73  ? LYS B 87  ? SER B 73  LYS B 87  1 ? 15 
HELX_P HELX_P37 AE1 SER B 93  ? TYR B 104 ? SER B 93  TYR B 104 1 ? 12 
HELX_P HELX_P38 AE2 ARG B 117 ? ASN B 131 ? ARG B 117 ASN B 131 1 ? 15 
HELX_P HELX_P39 AE3 ASP B 133 ? ASN B 146 ? ASP B 133 ASN B 146 1 ? 14 
HELX_P HELX_P40 AE4 SER B 152 ? ALA B 159 ? SER B 152 ALA B 159 1 ? 8  
HELX_P HELX_P41 AE5 SER B 178 ? LEU B 195 ? SER B 178 LEU B 195 1 ? 18 
HELX_P HELX_P42 AE6 LYS B 221 ? ALA B 237 ? LYS B 221 ALA B 237 1 ? 17 
HELX_P HELX_P43 AE7 ASP B 238 ? GLN B 242 ? ASP B 238 GLN B 242 5 ? 5  
HELX_P HELX_P44 AE8 ASP B 257 ? THR B 264 ? ASP B 257 THR B 264 1 ? 8  
HELX_P HELX_P45 AE9 PRO B 285 ? ASP B 295 ? PRO B 285 ASP B 295 1 ? 11 
HELX_P HELX_P46 AF1 TYR B 302 ? GLY B 311 ? TYR B 302 GLY B 311 1 ? 10 
HELX_P HELX_P47 AF2 HIS B 313 ? MET B 317 ? HIS B 313 MET B 317 5 ? 5  
HELX_P HELX_P48 AF3 ASP B 318 ? ASN B 329 ? ASP B 318 ASN B 329 1 ? 12 
HELX_P HELX_P49 AF4 ASN B 338 ? GLY B 354 ? ASN B 338 GLY B 354 1 ? 17 
HELX_P HELX_P50 AF5 GLN B 361 ? LYS B 366 ? GLN B 361 LYS B 366 1 ? 6  
HELX_P HELX_P51 AF6 ILE B 416 ? HIS B 422 ? ILE B 416 HIS B 422 1 ? 7  
HELX_P HELX_P52 AF7 SER B 424 ? THR B 442 ? SER B 424 THR B 442 1 ? 19 
HELX_P HELX_P53 AF8 ALA B 448 ? LYS B 459 ? ALA B 448 LYS B 459 1 ? 12 
HELX_P HELX_P54 AF9 ASN B 467 ? ASN B 475 ? ASN B 467 ASN B 475 1 ? 9  
HELX_P HELX_P55 AG1 SER B 481 ? GLY B 511 ? SER B 481 GLY B 511 1 ? 31 
HELX_P HELX_P56 AG2 GLN B 516 ? GLY B 519 ? GLN B 516 GLY B 519 5 ? 4  
HELX_P HELX_P57 AG3 SER B 520 ? GLY B 525 ? SER B 520 GLY B 525 1 ? 6  
HELX_P HELX_P58 AG4 PHE B 528 ? THR B 534 ? PHE B 528 THR B 534 1 ? 7  
HELX_P HELX_P59 AG5 TYR B 540 ? PHE B 547 ? TYR B 540 PHE B 547 1 ? 8  
HELX_P HELX_P60 AG6 THR B 554 ? GLY B 569 ? THR B 554 GLY B 569 1 ? 16 
HELX_P HELX_P61 AG7 SER B 583 ? GLN B 588 ? SER B 583 GLN B 588 1 ? 6  
HELX_P HELX_P62 AG8 ASP B 633 ? GLN B 646 ? ASP B 633 GLN B 646 1 ? 14 
HELX_P HELX_P63 AG9 THR B 663 ? GLY B 678 ? THR B 663 GLY B 678 1 ? 16 
HELX_P HELX_P64 AH1 PHE C 38  ? GLN C 49  ? PHE C 17  GLN C 28  1 ? 12 
HELX_P HELX_P65 AH2 LEU C 52  ? ILE C 56  ? LEU C 31  ILE C 35  5 ? 5  
HELX_P HELX_P66 AH3 LEU C 58  ? GLY C 60  ? LEU C 37  GLY C 39  5 ? 3  
HELX_P HELX_P67 AH4 ASP C 61  ? TYR C 67  ? ASP C 40  TYR C 46  1 ? 7  
HELX_P HELX_P68 AH5 GLY C 69  ? THR C 93  ? GLY C 48  THR C 72  1 ? 25 
HELX_P HELX_P69 AH6 THR C 93  ? VAL C 102 ? THR C 72  VAL C 81  1 ? 10 
HELX_P HELX_P70 AH7 GLY C 104 ? VAL C 121 ? GLY C 83  VAL C 100 1 ? 18 
HELX_P HELX_P71 AH8 VAL C 121 ? ALA C 134 ? VAL C 100 ALA C 113 1 ? 14 
HELX_P HELX_P72 AH9 PRO C 135 ? ASN C 149 ? PRO C 114 ASN C 128 1 ? 15 
HELX_P HELX_P73 AI1 ASN C 149 ? ALA C 165 ? ASN C 128 ALA C 144 1 ? 17 
HELX_P HELX_P74 AI2 ASP C 170 ? PHE C 187 ? ASP C 149 PHE C 166 1 ? 18 
HELX_P HELX_P75 AI3 PHE C 189 ? GLY C 201 ? PHE C 168 GLY C 180 1 ? 13 
HELX_P HELX_P76 AI4 LEU C 205 ? ASN C 235 ? LEU C 184 ASN C 214 1 ? 31 
HELX_P HELX_P77 AI5 THR C 238 ? ASP C 269 ? THR C 217 ASP C 248 1 ? 32 
HELX_P HELX_P78 AI6 GLN C 270 ? GLY C 272 ? GLN C 249 GLY C 251 5 ? 3  
HELX_P HELX_P79 AI7 LEU C 273 ? LEU C 292 ? LEU C 252 LEU C 271 1 ? 20 
HELX_P HELX_P80 AI8 ASN C 304 ? GLY C 310 ? ASN C 283 GLY C 289 1 ? 7  
HELX_P HELX_P81 AI9 LYS C 337 ? TYR C 342 ? LYS C 316 TYR C 321 5 ? 6  
HELX_P HELX_P82 AJ1 PHE D 38  ? GLN D 49  ? PHE D 17  GLN D 28  1 ? 12 
HELX_P HELX_P83 AJ2 LEU D 52  ? ILE D 56  ? LEU D 31  ILE D 35  5 ? 5  
HELX_P HELX_P84 AJ3 LEU D 58  ? GLY D 60  ? LEU D 37  GLY D 39  5 ? 3  
HELX_P HELX_P85 AJ4 ASP D 61  ? LYS D 66  ? ASP D 40  LYS D 45  1 ? 6  
HELX_P HELX_P86 AJ5 GLY D 69  ? THR D 93  ? GLY D 48  THR D 72  1 ? 25 
HELX_P HELX_P87 AJ6 THR D 93  ? VAL D 102 ? THR D 72  VAL D 81  1 ? 10 
HELX_P HELX_P88 AJ7 GLY D 104 ? VAL D 121 ? GLY D 83  VAL D 100 1 ? 18 
HELX_P HELX_P89 AJ8 VAL D 121 ? ALA D 134 ? VAL D 100 ALA D 113 1 ? 14 
HELX_P HELX_P90 AJ9 PRO D 135 ? ASN D 149 ? PRO D 114 ASN D 128 1 ? 15 
HELX_P HELX_P91 AK1 ASN D 149 ? ALA D 165 ? ASN D 128 ALA D 144 1 ? 17 
HELX_P HELX_P92 AK2 ASP D 170 ? PHE D 187 ? ASP D 149 PHE D 166 1 ? 18 
HELX_P HELX_P93 AK3 PHE D 189 ? GLY D 201 ? PHE D 168 GLY D 180 1 ? 13 
HELX_P HELX_P94 AK4 LEU D 205 ? ASN D 235 ? LEU D 184 ASN D 214 1 ? 31 
HELX_P HELX_P95 AK5 THR D 238 ? ASP D 269 ? THR D 217 ASP D 248 1 ? 32 
HELX_P HELX_P96 AK6 GLN D 270 ? GLY D 272 ? GLN D 249 GLY D 251 5 ? 3  
HELX_P HELX_P97 AK7 LEU D 273 ? LEU D 292 ? LEU D 252 LEU D 271 1 ? 20 
HELX_P HELX_P98 AK8 ASN D 304 ? LEU D 311 ? ASN D 283 LEU D 290 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? G TTP .   O2A ? ? ? 1_555 H MG . MG ? ? A TTP 803 A MG 804 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
metalc2  metalc ? ? G TTP .   O1B ? ? ? 1_555 H MG . MG ? ? A TTP 803 A MG 804 1_555 ? ? ? ? ? ? ? 2.849 ? ? 
metalc3  metalc ? ? G TTP .   O1G ? ? ? 1_555 H MG . MG ? ? A TTP 803 A MG 804 1_555 ? ? ? ? ? ? ? 2.374 ? ? 
metalc4  metalc ? ? I TTP .   O2A ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
metalc5  metalc ? ? I TTP .   O1B ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.501 ? ? 
metalc6  metalc ? ? I TTP .   O3G ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.179 ? ? 
metalc7  metalc ? ? C ASP 87  OD1 ? ? ? 1_555 N MN . MN ? ? C ASP 66  C MN 402 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc8  metalc ? ? C GLU 118 OE2 ? ? ? 1_555 M MN . MN ? ? C GLU 97  C MN 401 1_555 ? ? ? ? ? ? ? 1.961 ? ? 
metalc9  metalc ? ? C GLU 118 OE1 ? ? ? 1_555 N MN . MN ? ? C GLU 97  C MN 402 1_555 ? ? ? ? ? ? ? 2.113 ? ? 
metalc10 metalc ? ? C HIS 122 ND1 ? ? ? 1_555 N MN . MN ? ? C HIS 101 C MN 402 1_555 ? ? ? ? ? ? ? 2.177 ? ? 
metalc11 metalc ? ? C GLU 185 OE1 ? ? ? 1_555 M MN . MN ? ? C GLU 164 C MN 401 1_555 ? ? ? ? ? ? ? 2.129 ? ? 
metalc12 metalc ? ? C GLU 185 OE2 ? ? ? 1_555 M MN . MN ? ? C GLU 164 C MN 401 1_555 ? ? ? ? ? ? ? 1.965 ? ? 
metalc13 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 M MN . MN ? ? C GLU 198 C MN 401 1_555 ? ? ? ? ? ? ? 2.173 ? ? 
metalc14 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 N MN . MN ? ? C GLU 198 C MN 402 1_555 ? ? ? ? ? ? ? 2.710 ? ? 
metalc15 metalc ? ? C GLU 219 OE2 ? ? ? 1_555 N MN . MN ? ? C GLU 198 C MN 402 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc16 metalc ? ? C HIS 222 ND1 ? ? ? 1_555 M MN . MN ? ? C HIS 201 C MN 401 1_555 ? ? ? ? ? ? ? 2.409 ? ? 
metalc17 metalc ? ? D ASP 87  OD1 ? ? ? 1_555 P MN . MN ? ? D ASP 66  D MN 402 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc18 metalc ? ? D ASP 87  OD2 ? ? ? 1_555 P MN . MN ? ? D ASP 66  D MN 402 1_555 ? ? ? ? ? ? ? 2.157 ? ? 
metalc19 metalc ? ? D GLU 118 OE2 ? ? ? 1_555 O MN . MN ? ? D GLU 97  D MN 401 1_555 ? ? ? ? ? ? ? 1.912 ? ? 
metalc20 metalc ? ? D GLU 118 OE1 ? ? ? 1_555 P MN . MN ? ? D GLU 97  D MN 402 1_555 ? ? ? ? ? ? ? 1.991 ? ? 
metalc21 metalc ? ? D HIS 122 ND1 ? ? ? 1_555 P MN . MN ? ? D HIS 101 D MN 402 1_555 ? ? ? ? ? ? ? 2.147 ? ? 
metalc22 metalc ? ? D GLU 185 OE1 ? ? ? 1_555 O MN . MN ? ? D GLU 164 D MN 401 1_555 ? ? ? ? ? ? ? 2.304 ? ? 
metalc23 metalc ? ? D GLU 185 OE2 ? ? ? 1_555 O MN . MN ? ? D GLU 164 D MN 401 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc24 metalc ? ? D GLU 219 OE1 ? ? ? 1_555 O MN . MN ? ? D GLU 198 D MN 401 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc25 metalc ? ? D GLU 219 OE2 ? ? ? 1_555 P MN . MN ? ? D GLU 198 D MN 402 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
metalc26 metalc ? ? D HIS 222 ND1 ? ? ? 1_555 O MN . MN ? ? D HIS 201 D MN 401 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O2A ? G TTP .   ? A TTP 803 ? 1_555 MG ? H MG . ? A MG 804 ? 1_555 O1B ? G TTP .   ? A TTP 803 ? 1_555 65.6  ? 
2  O2A ? G TTP .   ? A TTP 803 ? 1_555 MG ? H MG . ? A MG 804 ? 1_555 O1G ? G TTP .   ? A TTP 803 ? 1_555 111.2 ? 
3  O1B ? G TTP .   ? A TTP 803 ? 1_555 MG ? H MG . ? A MG 804 ? 1_555 O1G ? G TTP .   ? A TTP 803 ? 1_555 64.8  ? 
4  O2A ? I TTP .   ? B TTP 801 ? 1_555 MG ? J MG . ? B MG 802 ? 1_555 O1B ? I TTP .   ? B TTP 801 ? 1_555 71.7  ? 
5  O2A ? I TTP .   ? B TTP 801 ? 1_555 MG ? J MG . ? B MG 802 ? 1_555 O3G ? I TTP .   ? B TTP 801 ? 1_555 88.0  ? 
6  O1B ? I TTP .   ? B TTP 801 ? 1_555 MG ? J MG . ? B MG 802 ? 1_555 O3G ? I TTP .   ? B TTP 801 ? 1_555 74.3  ? 
7  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE1 ? C GLU 118 ? C GLU 97  ? 1_555 89.6  ? 
8  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 120.6 ? 
9  OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 90.1  ? 
10 OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 138.4 ? 
11 OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 85.1  ? 
12 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 100.7 ? 
13 OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 117.3 ? 
14 OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 137.9 ? 
15 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 101.2 ? 
16 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 53.0  ? 
17 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 141.6 ? 
18 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 87.2  ? 
19 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 64.8  ? 
20 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 120.1 ? 
21 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 78.3  ? 
22 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 142.1 ? 
23 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 97.1  ? 
24 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 114.2 ? 
25 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 103.9 ? 
26 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 98.4  ? 
27 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 58.6  ? 
28 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 93.4  ? 
29 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 119.5 ? 
30 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 165.6 ? 
31 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 107.0 ? 
32 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 93.7  ? 
33 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 90.2  ? 
34 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 111.3 ? 
35 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 122.1 ? 
36 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 96.5  ? 
37 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 153.4 ? 
38 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 99.7  ? 
39 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 55.6  ? 
40 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 121.6 ? 
41 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 81.3  ? 
42 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 136.7 ? 
43 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 91.4  ? 
44 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 103.0 ? 
45 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 102.6 ? 
46 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 89.6  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 355 A . ? TYR 355 A PRO 356 A ? PRO 356 A 1 0.38 
2 TYR 355 B . ? TYR 355 B PRO 356 B ? PRO 356 B 1 0.72 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 6 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 3 ? 
AA8 ? 8 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
AB2 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? parallel      
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? parallel      
AA8 4 5 ? parallel      
AA8 5 6 ? parallel      
AA8 6 7 ? parallel      
AA8 7 8 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLN A 19  ? LYS A 20  ? GLN A 19  LYS A 20  
AA1 2 LYS A 23  ? PHE A 24  ? LYS A 23  PHE A 24  
AA2 1 TYR A 149 ? PRO A 151 ? TYR A 149 PRO A 151 
AA2 2 LEU A 411 ? ASN A 415 ? LEU A 411 ASN A 415 
AA2 3 GLY A 462 ? MET A 466 ? GLY A 462 MET A 466 
AA3 1 CYS A 170 ? GLU A 174 ? CYS A 170 GLU A 174 
AA3 2 GLY A 198 ? ASN A 202 ? GLY A 198 ASN A 202 
AA3 3 GLY A 247 ? ASN A 252 ? GLY A 247 ASN A 252 
AA3 4 LEU A 278 ? ILE A 284 ? LEU A 278 ILE A 284 
AA3 5 TYR A 357 ? PHE A 360 ? TYR A 357 PHE A 360 
AA3 6 THR A 681 ? ILE A 682 ? THR A 681 ILE A 682 
AA4 1 ALA A 298 ? PHE A 301 ? ALA A 298 PHE A 301 
AA4 2 LYS A 334 ? ILE A 337 ? LYS A 334 ILE A 337 
AA5 1 ILE A 601 ? TYR A 606 ? ILE A 601 TYR A 606 
AA5 2 SER A 609 ? PRO A 614 ? SER A 609 PRO A 614 
AA6 1 LEU A 656 ? LEU A 658 ? LEU A 656 LEU A 658 
AA6 2 ALA A 685 ? THR A 687 ? ALA A 685 THR A 687 
AA7 1 TYR B 149 ? PRO B 151 ? TYR B 149 PRO B 151 
AA7 2 SER B 408 ? ASN B 415 ? SER B 408 ASN B 415 
AA7 3 ILE B 461 ? MET B 466 ? ILE B 461 MET B 466 
AA8 1 TYR B 149 ? PRO B 151 ? TYR B 149 PRO B 151 
AA8 2 SER B 408 ? ASN B 415 ? SER B 408 ASN B 415 
AA8 3 CYS B 170 ? GLU B 174 ? CYS B 170 GLU B 174 
AA8 4 GLY B 198 ? ASN B 202 ? GLY B 198 ASN B 202 
AA8 5 GLY B 247 ? ASN B 252 ? GLY B 247 ASN B 252 
AA8 6 LEU B 278 ? ILE B 284 ? LEU B 278 ILE B 284 
AA8 7 TYR B 357 ? PHE B 360 ? TYR B 357 PHE B 360 
AA8 8 THR B 681 ? ILE B 682 ? THR B 681 ILE B 682 
AA9 1 ALA B 298 ? PHE B 301 ? ALA B 298 PHE B 301 
AA9 2 LYS B 334 ? ILE B 337 ? LYS B 334 ILE B 337 
AB1 1 ILE B 601 ? TYR B 606 ? ILE B 601 TYR B 606 
AB1 2 SER B 609 ? PRO B 614 ? SER B 609 PRO B 614 
AB2 1 LEU B 656 ? LYS B 659 ? LEU B 656 LYS B 659 
AB2 2 ALA B 685 ? LYS B 688 ? ALA B 685 LYS B 688 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LYS A 20  ? N LYS A 20  O LYS A 23  ? O LYS A 23  
AA2 1 2 N GLN A 150 ? N GLN A 150 O SER A 413 ? O SER A 413 
AA2 2 3 N GLY A 412 ? N GLY A 412 O GLY A 464 ? O GLY A 464 
AA3 1 2 N LEU A 173 ? N LEU A 173 O SER A 200 ? O SER A 200 
AA3 2 3 N LEU A 201 ? N LEU A 201 O TYR A 250 ? O TYR A 250 
AA3 3 4 N GLY A 247 ? N GLY A 247 O SER A 279 ? O SER A 279 
AA3 4 5 N VAL A 282 ? N VAL A 282 O TYR A 357 ? O TYR A 357 
AA3 5 6 N ILE A 358 ? N ILE A 358 O ILE A 682 ? O ILE A 682 
AA4 1 2 N ALA A 298 ? N ALA A 298 O ILE A 337 ? O ILE A 337 
AA5 1 2 N GLU A 602 ? N GLU A 602 O TYR A 613 ? O TYR A 613 
AA6 1 2 N LEU A 656 ? N LEU A 656 O ARG A 686 ? O ARG A 686 
AA7 1 2 N GLN B 150 ? N GLN B 150 O SER B 413 ? O SER B 413 
AA7 2 3 N GLY B 412 ? N GLY B 412 O GLY B 464 ? O GLY B 464 
AA8 1 2 N GLN B 150 ? N GLN B 150 O SER B 413 ? O SER B 413 
AA8 2 3 O CYS B 409 ? O CYS B 409 N CYS B 170 ? N CYS B 170 
AA8 3 4 N LEU B 173 ? N LEU B 173 O SER B 200 ? O SER B 200 
AA8 4 5 N LEU B 201 ? N LEU B 201 O TYR B 250 ? O TYR B 250 
AA8 5 6 N GLY B 247 ? N GLY B 247 O SER B 279 ? O SER B 279 
AA8 6 7 N VAL B 282 ? N VAL B 282 O TYR B 357 ? O TYR B 357 
AA8 7 8 N ILE B 358 ? N ILE B 358 O ILE B 682 ? O ILE B 682 
AA9 1 2 N ALA B 298 ? N ALA B 298 O ILE B 337 ? O ILE B 337 
AB1 1 2 N ARG B 604 ? N ARG B 604 O THR B 611 ? O THR B 611 
AB2 1 2 N LEU B 658 ? N LEU B 658 O ARG B 686 ? O ARG B 686 
# 
_pdbx_entry_details.entry_id                   9BYY 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OG1 A THR 108 ? ? OD1 A ASP 110 ? ? 2.01 
2 1 O   A PRO 616 ? ? OH  A TYR 626 ? ? 2.13 
3 1 O   B PRO 616 ? ? OH  B TYR 626 ? ? 2.14 
4 1 NH2 D ARG 86  ? ? OE1 D GLU 211 ? ? 2.18 
5 1 NE2 B HIS 372 ? ? O   B GLN 516 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 257 ? ? -69.45  2.74    
2  1 ASP A 398 ? ? 39.43   35.64   
3  1 SER A 593 ? ? 56.65   -153.81 
4  1 ASP B 215 ? ? 74.78   -2.78   
5  1 SER B 593 ? ? 60.64   -154.24 
6  1 THR C 72  ? ? -128.08 -59.03  
7  1 ASP C 148 ? ? 58.15   15.67   
8  1 PHE C 166 ? ? -125.67 -60.81  
9  1 THR D 72  ? ? -128.17 -58.46  
10 1 PHE D 166 ? ? -144.15 -61.09  
11 1 ASP D 317 ? ? 64.29   164.43  
12 1 ASP D 318 ? ? 66.34   -1.37   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BYY 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'RIGID BODY FIT' 
# 
loop_
_em_3d_fitting_list.id 
_em_3d_fitting_list.3d_fitting_id 
_em_3d_fitting_list.pdb_entry_id 
_em_3d_fitting_list.pdb_chain_id 
_em_3d_fitting_list.pdb_chain_residue_range 
_em_3d_fitting_list.details 
_em_3d_fitting_list.chain_id 
_em_3d_fitting_list.chain_residue_range 
_em_3d_fitting_list.source_name 
_em_3d_fitting_list.type 
_em_3d_fitting_list.accession_code 
_em_3d_fitting_list.initial_refinement_model_id 
1 1 9BYH ? ?      'Rigid-body docking of consensus model 9BYH containing alpha subunits and beta C-terminal tails' ? ?      PDB 
'experimental model' 9BYH 1 
2 1 4DR0 ? 16-290 'Rigid-body docking of residues 16-290 from beta dimer model 4DR0'                               ? 16-290 PDB 
'experimental model' 4DR0 2 
# 
_em_3d_reconstruction.entry_id                    9BYY 
_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                  4.07 
_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               23000 
_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                        9BYY 
_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              9BYY 
_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                9BYY 
_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              9BYY 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? A MET 1   
2   1 Y 1 A SER 2   ? A SER 2   
3   1 Y 1 A GLN 3   ? A GLN 3   
4   1 Y 1 A ASN 4   ? A ASN 4   
5   1 Y 1 A GLN 5   ? A GLN 5   
6   1 Y 1 A ASP 689 ? A ASP 689 
7   1 Y 1 A THR 690 ? A THR 690 
8   1 Y 1 A GLY 691 ? A GLY 691 
9   1 Y 1 A GLN 692 ? A GLN 692 
10  1 Y 1 A ASP 693 ? A ASP 693 
11  1 Y 1 A SER 694 ? A SER 694 
12  1 Y 1 A CYS 695 ? A CYS 695 
13  1 Y 1 A LEU 696 ? A LEU 696 
14  1 Y 1 A SER 697 ? A SER 697 
15  1 Y 1 A CYS 698 ? A CYS 698 
16  1 Y 1 A VAL 699 ? A VAL 699 
17  1 Y 1 A VAL 700 ? A VAL 700 
18  1 Y 1 B MET 1   ? B MET 1   
19  1 Y 1 B SER 2   ? B SER 2   
20  1 Y 1 B GLN 3   ? B GLN 3   
21  1 Y 1 B ASN 4   ? B ASN 4   
22  1 Y 1 B GLN 5   ? B GLN 5   
23  1 Y 1 B ASP 689 ? B ASP 689 
24  1 Y 1 B THR 690 ? B THR 690 
25  1 Y 1 B GLY 691 ? B GLY 691 
26  1 Y 1 B GLN 692 ? B GLN 692 
27  1 Y 1 B ASP 693 ? B ASP 693 
28  1 Y 1 B SER 694 ? B SER 694 
29  1 Y 1 B CYS 695 ? B CYS 695 
30  1 Y 1 B LEU 696 ? B LEU 696 
31  1 Y 1 B SER 697 ? B SER 697 
32  1 Y 1 B CYS 698 ? B CYS 698 
33  1 Y 1 B VAL 699 ? B VAL 699 
34  1 Y 1 B VAL 700 ? B VAL 700 
35  1 Y 1 C MET -20 ? C MET 1   
36  1 Y 1 C GLY -19 ? C GLY 2   
37  1 Y 1 C SER -18 ? C SER 3   
38  1 Y 1 C SER -17 ? C SER 4   
39  1 Y 1 C HIS -16 ? C HIS 5   
40  1 Y 1 C HIS -15 ? C HIS 6   
41  1 Y 1 C HIS -14 ? C HIS 7   
42  1 Y 1 C HIS -13 ? C HIS 8   
43  1 Y 1 C HIS -12 ? C HIS 9   
44  1 Y 1 C HIS -11 ? C HIS 10  
45  1 Y 1 C SER -10 ? C SER 11  
46  1 Y 1 C SER -9  ? C SER 12  
47  1 Y 1 C GLY -8  ? C GLY 13  
48  1 Y 1 C LEU -7  ? C LEU 14  
49  1 Y 1 C VAL -6  ? C VAL 15  
50  1 Y 1 C PRO -5  ? C PRO 16  
51  1 Y 1 C ARG -4  ? C ARG 17  
52  1 Y 1 C GLY -3  ? C GLY 18  
53  1 Y 1 C SER -2  ? C SER 19  
54  1 Y 1 C HIS -1  ? C HIS 20  
55  1 Y 1 C MET 0   ? C MET 21  
56  1 Y 1 C MET 1   ? C MET 22  
57  1 Y 1 C THR 2   ? C THR 23  
58  1 Y 1 C LYS 3   ? C LYS 24  
59  1 Y 1 C ILE 4   ? C ILE 25  
60  1 Y 1 C TYR 5   ? C TYR 26  
61  1 Y 1 C ASP 6   ? C ASP 27  
62  1 Y 1 C ALA 7   ? C ALA 28  
63  1 Y 1 C ALA 8   ? C ALA 29  
64  1 Y 1 C ASN 9   ? C ASN 30  
65  1 Y 1 C TRP 10  ? C TRP 31  
66  1 Y 1 C SER 11  ? C SER 32  
67  1 Y 1 C LYS 12  ? C LYS 33  
68  1 Y 1 C HIS 13  ? C HIS 34  
69  1 Y 1 C GLU 14  ? C GLU 35  
70  1 Y 1 C ASP 15  ? C ASP 36  
71  1 Y 1 C ASN 291 ? C ASN 312 
72  1 Y 1 C THR 292 ? C THR 313 
73  1 Y 1 C LYS 293 ? C LYS 314 
74  1 Y 1 C THR 294 ? C THR 315 
75  1 Y 1 C LYS 295 ? C LYS 316 
76  1 Y 1 C SER 296 ? C SER 317 
77  1 Y 1 C HIS 297 ? C HIS 318 
78  1 Y 1 C ASP 298 ? C ASP 319 
79  1 Y 1 C PHE 299 ? C PHE 320 
80  1 Y 1 C PHE 300 ? C PHE 321 
81  1 Y 1 C SER 301 ? C SER 322 
82  1 Y 1 C MET 302 ? C MET 323 
83  1 Y 1 C LYS 303 ? C LYS 324 
84  1 Y 1 C GLY 304 ? C GLY 325 
85  1 Y 1 C ASN 305 ? C ASN 326 
86  1 Y 1 C GLY 306 ? C GLY 327 
87  1 Y 1 C TYR 307 ? C TYR 328 
88  1 Y 1 C LYS 308 ? C LYS 329 
89  1 Y 1 C GLU 323 ? C GLU 344 
90  1 Y 1 C ASP 324 ? C ASP 345 
91  1 Y 1 C GLU 325 ? C GLU 346 
92  1 Y 1 C LYS 326 ? C LYS 347 
93  1 Y 1 C GLU 327 ? C GLU 348 
94  1 Y 1 C GLN 328 ? C GLN 349 
95  1 Y 1 C ILE 329 ? C ILE 350 
96  1 Y 1 D MET -20 ? D MET 1   
97  1 Y 1 D GLY -19 ? D GLY 2   
98  1 Y 1 D SER -18 ? D SER 3   
99  1 Y 1 D SER -17 ? D SER 4   
100 1 Y 1 D HIS -16 ? D HIS 5   
101 1 Y 1 D HIS -15 ? D HIS 6   
102 1 Y 1 D HIS -14 ? D HIS 7   
103 1 Y 1 D HIS -13 ? D HIS 8   
104 1 Y 1 D HIS -12 ? D HIS 9   
105 1 Y 1 D HIS -11 ? D HIS 10  
106 1 Y 1 D SER -10 ? D SER 11  
107 1 Y 1 D SER -9  ? D SER 12  
108 1 Y 1 D GLY -8  ? D GLY 13  
109 1 Y 1 D LEU -7  ? D LEU 14  
110 1 Y 1 D VAL -6  ? D VAL 15  
111 1 Y 1 D PRO -5  ? D PRO 16  
112 1 Y 1 D ARG -4  ? D ARG 17  
113 1 Y 1 D GLY -3  ? D GLY 18  
114 1 Y 1 D SER -2  ? D SER 19  
115 1 Y 1 D HIS -1  ? D HIS 20  
116 1 Y 1 D MET 0   ? D MET 21  
117 1 Y 1 D MET 1   ? D MET 22  
118 1 Y 1 D THR 2   ? D THR 23  
119 1 Y 1 D LYS 3   ? D LYS 24  
120 1 Y 1 D ILE 4   ? D ILE 25  
121 1 Y 1 D TYR 5   ? D TYR 26  
122 1 Y 1 D ASP 6   ? D ASP 27  
123 1 Y 1 D ALA 7   ? D ALA 28  
124 1 Y 1 D ALA 8   ? D ALA 29  
125 1 Y 1 D ASN 9   ? D ASN 30  
126 1 Y 1 D TRP 10  ? D TRP 31  
127 1 Y 1 D SER 11  ? D SER 32  
128 1 Y 1 D LYS 12  ? D LYS 33  
129 1 Y 1 D HIS 13  ? D HIS 34  
130 1 Y 1 D GLU 14  ? D GLU 35  
131 1 Y 1 D ASP 15  ? D ASP 36  
132 1 Y 1 D ASN 291 ? D ASN 312 
133 1 Y 1 D THR 292 ? D THR 313 
134 1 Y 1 D LYS 293 ? D LYS 314 
135 1 Y 1 D THR 294 ? D THR 315 
136 1 Y 1 D LYS 295 ? D LYS 316 
137 1 Y 1 D SER 296 ? D SER 317 
138 1 Y 1 D HIS 297 ? D HIS 318 
139 1 Y 1 D ASP 298 ? D ASP 319 
140 1 Y 1 D PHE 299 ? D PHE 320 
141 1 Y 1 D PHE 300 ? D PHE 321 
142 1 Y 1 D SER 301 ? D SER 322 
143 1 Y 1 D MET 302 ? D MET 323 
144 1 Y 1 D LYS 303 ? D LYS 324 
145 1 Y 1 D GLY 304 ? D GLY 325 
146 1 Y 1 D ASN 305 ? D ASN 326 
147 1 Y 1 D GLY 306 ? D GLY 327 
148 1 Y 1 D TYR 307 ? D TYR 328 
149 1 Y 1 D LYS 308 ? D LYS 329 
150 1 Y 1 D GLU 323 ? D GLU 344 
151 1 Y 1 D ASP 324 ? D ASP 345 
152 1 Y 1 D GLU 325 ? D GLU 346 
153 1 Y 1 D LYS 326 ? D LYS 347 
154 1 Y 1 D GLU 327 ? D GLU 348 
155 1 Y 1 D GLN 328 ? D GLN 349 
156 1 Y 1 D ILE 329 ? D ILE 350 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
ATP PG     P  N N 74  
ATP O1G    O  N N 75  
ATP O2G    O  N N 76  
ATP O3G    O  N N 77  
ATP PB     P  N R 78  
ATP O1B    O  N N 79  
ATP O2B    O  N N 80  
ATP O3B    O  N N 81  
ATP PA     P  N R 82  
ATP O1A    O  N N 83  
ATP O2A    O  N N 84  
ATP O3A    O  N N 85  
ATP "O5'"  O  N N 86  
ATP "C5'"  C  N N 87  
ATP "C4'"  C  N R 88  
ATP "O4'"  O  N N 89  
ATP "C3'"  C  N S 90  
ATP "O3'"  O  N N 91  
ATP "C2'"  C  N R 92  
ATP "O2'"  O  N N 93  
ATP "C1'"  C  N R 94  
ATP N9     N  Y N 95  
ATP C8     C  Y N 96  
ATP N7     N  Y N 97  
ATP C5     C  Y N 98  
ATP C6     C  Y N 99  
ATP N6     N  N N 100 
ATP N1     N  Y N 101 
ATP C2     C  Y N 102 
ATP N3     N  Y N 103 
ATP C4     C  Y N 104 
ATP HOG2   H  N N 105 
ATP HOG3   H  N N 106 
ATP HOB2   H  N N 107 
ATP HOA2   H  N N 108 
ATP "H5'1" H  N N 109 
ATP "H5'2" H  N N 110 
ATP "H4'"  H  N N 111 
ATP "H3'"  H  N N 112 
ATP "HO3'" H  N N 113 
ATP "H2'"  H  N N 114 
ATP "HO2'" H  N N 115 
ATP "H1'"  H  N N 116 
ATP H8     H  N N 117 
ATP HN61   H  N N 118 
ATP HN62   H  N N 119 
ATP H2     H  N N 120 
CYS N      N  N N 121 
CYS CA     C  N R 122 
CYS C      C  N N 123 
CYS O      O  N N 124 
CYS CB     C  N N 125 
CYS SG     S  N N 126 
CYS OXT    O  N N 127 
CYS H      H  N N 128 
CYS H2     H  N N 129 
CYS HA     H  N N 130 
CYS HB2    H  N N 131 
CYS HB3    H  N N 132 
CYS HG     H  N N 133 
CYS HXT    H  N N 134 
GDP PB     P  N N 135 
GDP O1B    O  N N 136 
GDP O2B    O  N N 137 
GDP O3B    O  N N 138 
GDP O3A    O  N N 139 
GDP PA     P  N N 140 
GDP O1A    O  N N 141 
GDP O2A    O  N N 142 
GDP "O5'"  O  N N 143 
GDP "C5'"  C  N N 144 
GDP "C4'"  C  N R 145 
GDP "O4'"  O  N N 146 
GDP "C3'"  C  N S 147 
GDP "O3'"  O  N N 148 
GDP "C2'"  C  N R 149 
GDP "O2'"  O  N N 150 
GDP "C1'"  C  N R 151 
GDP N9     N  Y N 152 
GDP C8     C  Y N 153 
GDP N7     N  Y N 154 
GDP C5     C  Y N 155 
GDP C6     C  N N 156 
GDP O6     O  N N 157 
GDP N1     N  N N 158 
GDP C2     C  N N 159 
GDP N2     N  N N 160 
GDP N3     N  N N 161 
GDP C4     C  Y N 162 
GDP HOB2   H  N N 163 
GDP HOB3   H  N N 164 
GDP HOA2   H  N N 165 
GDP "H5'"  H  N N 166 
GDP "H5''" H  N N 167 
GDP "H4'"  H  N N 168 
GDP "H3'"  H  N N 169 
GDP "HO3'" H  N N 170 
GDP "H2'"  H  N N 171 
GDP "HO2'" H  N N 172 
GDP "H1'"  H  N N 173 
GDP H8     H  N N 174 
GDP HN1    H  N N 175 
GDP HN21   H  N N 176 
GDP HN22   H  N N 177 
GLN N      N  N N 178 
GLN CA     C  N S 179 
GLN C      C  N N 180 
GLN O      O  N N 181 
GLN CB     C  N N 182 
GLN CG     C  N N 183 
GLN CD     C  N N 184 
GLN OE1    O  N N 185 
GLN NE2    N  N N 186 
GLN OXT    O  N N 187 
GLN H      H  N N 188 
GLN H2     H  N N 189 
GLN HA     H  N N 190 
GLN HB2    H  N N 191 
GLN HB3    H  N N 192 
GLN HG2    H  N N 193 
GLN HG3    H  N N 194 
GLN HE21   H  N N 195 
GLN HE22   H  N N 196 
GLN HXT    H  N N 197 
GLU N      N  N N 198 
GLU CA     C  N S 199 
GLU C      C  N N 200 
GLU O      O  N N 201 
GLU CB     C  N N 202 
GLU CG     C  N N 203 
GLU CD     C  N N 204 
GLU OE1    O  N N 205 
GLU OE2    O  N N 206 
GLU OXT    O  N N 207 
GLU H      H  N N 208 
GLU H2     H  N N 209 
GLU HA     H  N N 210 
GLU HB2    H  N N 211 
GLU HB3    H  N N 212 
GLU HG2    H  N N 213 
GLU HG3    H  N N 214 
GLU HE2    H  N N 215 
GLU HXT    H  N N 216 
GLY N      N  N N 217 
GLY CA     C  N N 218 
GLY C      C  N N 219 
GLY O      O  N N 220 
GLY OXT    O  N N 221 
GLY H      H  N N 222 
GLY H2     H  N N 223 
GLY HA2    H  N N 224 
GLY HA3    H  N N 225 
GLY HXT    H  N N 226 
HIS N      N  N N 227 
HIS CA     C  N S 228 
HIS C      C  N N 229 
HIS O      O  N N 230 
HIS CB     C  N N 231 
HIS CG     C  Y N 232 
HIS ND1    N  Y N 233 
HIS CD2    C  Y N 234 
HIS CE1    C  Y N 235 
HIS NE2    N  Y N 236 
HIS OXT    O  N N 237 
HIS H      H  N N 238 
HIS H2     H  N N 239 
HIS HA     H  N N 240 
HIS HB2    H  N N 241 
HIS HB3    H  N N 242 
HIS HD1    H  N N 243 
HIS HD2    H  N N 244 
HIS HE1    H  N N 245 
HIS HE2    H  N N 246 
HIS HXT    H  N N 247 
ILE N      N  N N 248 
ILE CA     C  N S 249 
ILE C      C  N N 250 
ILE O      O  N N 251 
ILE CB     C  N S 252 
ILE CG1    C  N N 253 
ILE CG2    C  N N 254 
ILE CD1    C  N N 255 
ILE OXT    O  N N 256 
ILE H      H  N N 257 
ILE H2     H  N N 258 
ILE HA     H  N N 259 
ILE HB     H  N N 260 
ILE HG12   H  N N 261 
ILE HG13   H  N N 262 
ILE HG21   H  N N 263 
ILE HG22   H  N N 264 
ILE HG23   H  N N 265 
ILE HD11   H  N N 266 
ILE HD12   H  N N 267 
ILE HD13   H  N N 268 
ILE HXT    H  N N 269 
LEU N      N  N N 270 
LEU CA     C  N S 271 
LEU C      C  N N 272 
LEU O      O  N N 273 
LEU CB     C  N N 274 
LEU CG     C  N N 275 
LEU CD1    C  N N 276 
LEU CD2    C  N N 277 
LEU OXT    O  N N 278 
LEU H      H  N N 279 
LEU H2     H  N N 280 
LEU HA     H  N N 281 
LEU HB2    H  N N 282 
LEU HB3    H  N N 283 
LEU HG     H  N N 284 
LEU HD11   H  N N 285 
LEU HD12   H  N N 286 
LEU HD13   H  N N 287 
LEU HD21   H  N N 288 
LEU HD22   H  N N 289 
LEU HD23   H  N N 290 
LEU HXT    H  N N 291 
LYS N      N  N N 292 
LYS CA     C  N S 293 
LYS C      C  N N 294 
LYS O      O  N N 295 
LYS CB     C  N N 296 
LYS CG     C  N N 297 
LYS CD     C  N N 298 
LYS CE     C  N N 299 
LYS NZ     N  N N 300 
LYS OXT    O  N N 301 
LYS H      H  N N 302 
LYS H2     H  N N 303 
LYS HA     H  N N 304 
LYS HB2    H  N N 305 
LYS HB3    H  N N 306 
LYS HG2    H  N N 307 
LYS HG3    H  N N 308 
LYS HD2    H  N N 309 
LYS HD3    H  N N 310 
LYS HE2    H  N N 311 
LYS HE3    H  N N 312 
LYS HZ1    H  N N 313 
LYS HZ2    H  N N 314 
LYS HZ3    H  N N 315 
LYS HXT    H  N N 316 
MET N      N  N N 317 
MET CA     C  N S 318 
MET C      C  N N 319 
MET O      O  N N 320 
MET CB     C  N N 321 
MET CG     C  N N 322 
MET SD     S  N N 323 
MET CE     C  N N 324 
MET OXT    O  N N 325 
MET H      H  N N 326 
MET H2     H  N N 327 
MET HA     H  N N 328 
MET HB2    H  N N 329 
MET HB3    H  N N 330 
MET HG2    H  N N 331 
MET HG3    H  N N 332 
MET HE1    H  N N 333 
MET HE2    H  N N 334 
MET HE3    H  N N 335 
MET HXT    H  N N 336 
MG  MG     MG N N 337 
MN  MN     MN N N 338 
PHE N      N  N N 339 
PHE CA     C  N S 340 
PHE C      C  N N 341 
PHE O      O  N N 342 
PHE CB     C  N N 343 
PHE CG     C  Y N 344 
PHE CD1    C  Y N 345 
PHE CD2    C  Y N 346 
PHE CE1    C  Y N 347 
PHE CE2    C  Y N 348 
PHE CZ     C  Y N 349 
PHE OXT    O  N N 350 
PHE H      H  N N 351 
PHE H2     H  N N 352 
PHE HA     H  N N 353 
PHE HB2    H  N N 354 
PHE HB3    H  N N 355 
PHE HD1    H  N N 356 
PHE HD2    H  N N 357 
PHE HE1    H  N N 358 
PHE HE2    H  N N 359 
PHE HZ     H  N N 360 
PHE HXT    H  N N 361 
PRO N      N  N N 362 
PRO CA     C  N S 363 
PRO C      C  N N 364 
PRO O      O  N N 365 
PRO CB     C  N N 366 
PRO CG     C  N N 367 
PRO CD     C  N N 368 
PRO OXT    O  N N 369 
PRO H      H  N N 370 
PRO HA     H  N N 371 
PRO HB2    H  N N 372 
PRO HB3    H  N N 373 
PRO HG2    H  N N 374 
PRO HG3    H  N N 375 
PRO HD2    H  N N 376 
PRO HD3    H  N N 377 
PRO HXT    H  N N 378 
SER N      N  N N 379 
SER CA     C  N S 380 
SER C      C  N N 381 
SER O      O  N N 382 
SER CB     C  N N 383 
SER OG     O  N N 384 
SER OXT    O  N N 385 
SER H      H  N N 386 
SER H2     H  N N 387 
SER HA     H  N N 388 
SER HB2    H  N N 389 
SER HB3    H  N N 390 
SER HG     H  N N 391 
SER HXT    H  N N 392 
THR N      N  N N 393 
THR CA     C  N S 394 
THR C      C  N N 395 
THR O      O  N N 396 
THR CB     C  N R 397 
THR OG1    O  N N 398 
THR CG2    C  N N 399 
THR OXT    O  N N 400 
THR H      H  N N 401 
THR H2     H  N N 402 
THR HA     H  N N 403 
THR HB     H  N N 404 
THR HG1    H  N N 405 
THR HG21   H  N N 406 
THR HG22   H  N N 407 
THR HG23   H  N N 408 
THR HXT    H  N N 409 
TRP N      N  N N 410 
TRP CA     C  N S 411 
TRP C      C  N N 412 
TRP O      O  N N 413 
TRP CB     C  N N 414 
TRP CG     C  Y N 415 
TRP CD1    C  Y N 416 
TRP CD2    C  Y N 417 
TRP NE1    N  Y N 418 
TRP CE2    C  Y N 419 
TRP CE3    C  Y N 420 
TRP CZ2    C  Y N 421 
TRP CZ3    C  Y N 422 
TRP CH2    C  Y N 423 
TRP OXT    O  N N 424 
TRP H      H  N N 425 
TRP H2     H  N N 426 
TRP HA     H  N N 427 
TRP HB2    H  N N 428 
TRP HB3    H  N N 429 
TRP HD1    H  N N 430 
TRP HE1    H  N N 431 
TRP HE3    H  N N 432 
TRP HZ2    H  N N 433 
TRP HZ3    H  N N 434 
TRP HH2    H  N N 435 
TRP HXT    H  N N 436 
TTP PA     P  N S 437 
TTP O1A    O  N N 438 
TTP O2A    O  N N 439 
TTP O3A    O  N N 440 
TTP PB     P  N S 441 
TTP O1B    O  N N 442 
TTP O2B    O  N N 443 
TTP O3B    O  N N 444 
TTP PG     P  N N 445 
TTP O1G    O  N N 446 
TTP O2G    O  N N 447 
TTP O3G    O  N N 448 
TTP "O5'"  O  N N 449 
TTP "C5'"  C  N N 450 
TTP "C4'"  C  N R 451 
TTP "O4'"  O  N N 452 
TTP "C3'"  C  N S 453 
TTP "O3'"  O  N N 454 
TTP "C2'"  C  N N 455 
TTP "C1'"  C  N R 456 
TTP N1     N  N N 457 
TTP C2     C  N N 458 
TTP O2     O  N N 459 
TTP N3     N  N N 460 
TTP C4     C  N N 461 
TTP O4     O  N N 462 
TTP C5     C  N N 463 
TTP C5M    C  N N 464 
TTP C6     C  N N 465 
TTP HOA2   H  N N 466 
TTP HOB2   H  N N 467 
TTP HOG2   H  N N 468 
TTP HOG3   H  N N 469 
TTP "H5'1" H  N N 470 
TTP "H5'2" H  N N 471 
TTP "H4'"  H  N N 472 
TTP "H3'"  H  N N 473 
TTP "HO3'" H  N N 474 
TTP "H2'1" H  N N 475 
TTP "H2'2" H  N N 476 
TTP "H1'"  H  N N 477 
TTP HN3    H  N N 478 
TTP HM51   H  N N 479 
TTP HM52   H  N N 480 
TTP HM53   H  N N 481 
TTP H6     H  N N 482 
TYR N      N  N N 483 
TYR CA     C  N S 484 
TYR C      C  N N 485 
TYR O      O  N N 486 
TYR CB     C  N N 487 
TYR CG     C  Y N 488 
TYR CD1    C  Y N 489 
TYR CD2    C  Y N 490 
TYR CE1    C  Y N 491 
TYR CE2    C  Y N 492 
TYR CZ     C  Y N 493 
TYR OH     O  N N 494 
TYR OXT    O  N N 495 
TYR H      H  N N 496 
TYR H2     H  N N 497 
TYR HA     H  N N 498 
TYR HB2    H  N N 499 
TYR HB3    H  N N 500 
TYR HD1    H  N N 501 
TYR HD2    H  N N 502 
TYR HE1    H  N N 503 
TYR HE2    H  N N 504 
TYR HH     H  N N 505 
TYR HXT    H  N N 506 
VAL N      N  N N 507 
VAL CA     C  N S 508 
VAL C      C  N N 509 
VAL O      O  N N 510 
VAL CB     C  N N 511 
VAL CG1    C  N N 512 
VAL CG2    C  N N 513 
VAL OXT    O  N N 514 
VAL H      H  N N 515 
VAL H2     H  N N 516 
VAL HA     H  N N 517 
VAL HB     H  N N 518 
VAL HG11   H  N N 519 
VAL HG12   H  N N 520 
VAL HG13   H  N N 521 
VAL HG21   H  N N 522 
VAL HG22   H  N N 523 
VAL HG23   H  N N 524 
VAL HXT    H  N N 525 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
ATP PG    O1G    doub N N 70  
ATP PG    O2G    sing N N 71  
ATP PG    O3G    sing N N 72  
ATP PG    O3B    sing N N 73  
ATP O2G   HOG2   sing N N 74  
ATP O3G   HOG3   sing N N 75  
ATP PB    O1B    doub N N 76  
ATP PB    O2B    sing N N 77  
ATP PB    O3B    sing N N 78  
ATP PB    O3A    sing N N 79  
ATP O2B   HOB2   sing N N 80  
ATP PA    O1A    doub N N 81  
ATP PA    O2A    sing N N 82  
ATP PA    O3A    sing N N 83  
ATP PA    "O5'"  sing N N 84  
ATP O2A   HOA2   sing N N 85  
ATP "O5'" "C5'"  sing N N 86  
ATP "C5'" "C4'"  sing N N 87  
ATP "C5'" "H5'1" sing N N 88  
ATP "C5'" "H5'2" sing N N 89  
ATP "C4'" "O4'"  sing N N 90  
ATP "C4'" "C3'"  sing N N 91  
ATP "C4'" "H4'"  sing N N 92  
ATP "O4'" "C1'"  sing N N 93  
ATP "C3'" "O3'"  sing N N 94  
ATP "C3'" "C2'"  sing N N 95  
ATP "C3'" "H3'"  sing N N 96  
ATP "O3'" "HO3'" sing N N 97  
ATP "C2'" "O2'"  sing N N 98  
ATP "C2'" "C1'"  sing N N 99  
ATP "C2'" "H2'"  sing N N 100 
ATP "O2'" "HO2'" sing N N 101 
ATP "C1'" N9     sing N N 102 
ATP "C1'" "H1'"  sing N N 103 
ATP N9    C8     sing Y N 104 
ATP N9    C4     sing Y N 105 
ATP C8    N7     doub Y N 106 
ATP C8    H8     sing N N 107 
ATP N7    C5     sing Y N 108 
ATP C5    C6     sing Y N 109 
ATP C5    C4     doub Y N 110 
ATP C6    N6     sing N N 111 
ATP C6    N1     doub Y N 112 
ATP N6    HN61   sing N N 113 
ATP N6    HN62   sing N N 114 
ATP N1    C2     sing Y N 115 
ATP C2    N3     doub Y N 116 
ATP C2    H2     sing N N 117 
ATP N3    C4     sing Y N 118 
CYS N     CA     sing N N 119 
CYS N     H      sing N N 120 
CYS N     H2     sing N N 121 
CYS CA    C      sing N N 122 
CYS CA    CB     sing N N 123 
CYS CA    HA     sing N N 124 
CYS C     O      doub N N 125 
CYS C     OXT    sing N N 126 
CYS CB    SG     sing N N 127 
CYS CB    HB2    sing N N 128 
CYS CB    HB3    sing N N 129 
CYS SG    HG     sing N N 130 
CYS OXT   HXT    sing N N 131 
GDP PB    O1B    doub N N 132 
GDP PB    O2B    sing N N 133 
GDP PB    O3B    sing N N 134 
GDP PB    O3A    sing N N 135 
GDP O2B   HOB2   sing N N 136 
GDP O3B   HOB3   sing N N 137 
GDP O3A   PA     sing N N 138 
GDP PA    O1A    doub N N 139 
GDP PA    O2A    sing N N 140 
GDP PA    "O5'"  sing N N 141 
GDP O2A   HOA2   sing N N 142 
GDP "O5'" "C5'"  sing N N 143 
GDP "C5'" "C4'"  sing N N 144 
GDP "C5'" "H5'"  sing N N 145 
GDP "C5'" "H5''" sing N N 146 
GDP "C4'" "O4'"  sing N N 147 
GDP "C4'" "C3'"  sing N N 148 
GDP "C4'" "H4'"  sing N N 149 
GDP "O4'" "C1'"  sing N N 150 
GDP "C3'" "O3'"  sing N N 151 
GDP "C3'" "C2'"  sing N N 152 
GDP "C3'" "H3'"  sing N N 153 
GDP "O3'" "HO3'" sing N N 154 
GDP "C2'" "O2'"  sing N N 155 
GDP "C2'" "C1'"  sing N N 156 
GDP "C2'" "H2'"  sing N N 157 
GDP "O2'" "HO2'" sing N N 158 
GDP "C1'" N9     sing N N 159 
GDP "C1'" "H1'"  sing N N 160 
GDP N9    C8     sing Y N 161 
GDP N9    C4     sing Y N 162 
GDP C8    N7     doub Y N 163 
GDP C8    H8     sing N N 164 
GDP N7    C5     sing Y N 165 
GDP C5    C6     sing N N 166 
GDP C5    C4     doub Y N 167 
GDP C6    O6     doub N N 168 
GDP C6    N1     sing N N 169 
GDP N1    C2     sing N N 170 
GDP N1    HN1    sing N N 171 
GDP C2    N2     sing N N 172 
GDP C2    N3     doub N N 173 
GDP N2    HN21   sing N N 174 
GDP N2    HN22   sing N N 175 
GDP N3    C4     sing N N 176 
GLN N     CA     sing N N 177 
GLN N     H      sing N N 178 
GLN N     H2     sing N N 179 
GLN CA    C      sing N N 180 
GLN CA    CB     sing N N 181 
GLN CA    HA     sing N N 182 
GLN C     O      doub N N 183 
GLN C     OXT    sing N N 184 
GLN CB    CG     sing N N 185 
GLN CB    HB2    sing N N 186 
GLN CB    HB3    sing N N 187 
GLN CG    CD     sing N N 188 
GLN CG    HG2    sing N N 189 
GLN CG    HG3    sing N N 190 
GLN CD    OE1    doub N N 191 
GLN CD    NE2    sing N N 192 
GLN NE2   HE21   sing N N 193 
GLN NE2   HE22   sing N N 194 
GLN OXT   HXT    sing N N 195 
GLU N     CA     sing N N 196 
GLU N     H      sing N N 197 
GLU N     H2     sing N N 198 
GLU CA    C      sing N N 199 
GLU CA    CB     sing N N 200 
GLU CA    HA     sing N N 201 
GLU C     O      doub N N 202 
GLU C     OXT    sing N N 203 
GLU CB    CG     sing N N 204 
GLU CB    HB2    sing N N 205 
GLU CB    HB3    sing N N 206 
GLU CG    CD     sing N N 207 
GLU CG    HG2    sing N N 208 
GLU CG    HG3    sing N N 209 
GLU CD    OE1    doub N N 210 
GLU CD    OE2    sing N N 211 
GLU OE2   HE2    sing N N 212 
GLU OXT   HXT    sing N N 213 
GLY N     CA     sing N N 214 
GLY N     H      sing N N 215 
GLY N     H2     sing N N 216 
GLY CA    C      sing N N 217 
GLY CA    HA2    sing N N 218 
GLY CA    HA3    sing N N 219 
GLY C     O      doub N N 220 
GLY C     OXT    sing N N 221 
GLY OXT   HXT    sing N N 222 
HIS N     CA     sing N N 223 
HIS N     H      sing N N 224 
HIS N     H2     sing N N 225 
HIS CA    C      sing N N 226 
HIS CA    CB     sing N N 227 
HIS CA    HA     sing N N 228 
HIS C     O      doub N N 229 
HIS C     OXT    sing N N 230 
HIS CB    CG     sing N N 231 
HIS CB    HB2    sing N N 232 
HIS CB    HB3    sing N N 233 
HIS CG    ND1    sing Y N 234 
HIS CG    CD2    doub Y N 235 
HIS ND1   CE1    doub Y N 236 
HIS ND1   HD1    sing N N 237 
HIS CD2   NE2    sing Y N 238 
HIS CD2   HD2    sing N N 239 
HIS CE1   NE2    sing Y N 240 
HIS CE1   HE1    sing N N 241 
HIS NE2   HE2    sing N N 242 
HIS OXT   HXT    sing N N 243 
ILE N     CA     sing N N 244 
ILE N     H      sing N N 245 
ILE N     H2     sing N N 246 
ILE CA    C      sing N N 247 
ILE CA    CB     sing N N 248 
ILE CA    HA     sing N N 249 
ILE C     O      doub N N 250 
ILE C     OXT    sing N N 251 
ILE CB    CG1    sing N N 252 
ILE CB    CG2    sing N N 253 
ILE CB    HB     sing N N 254 
ILE CG1   CD1    sing N N 255 
ILE CG1   HG12   sing N N 256 
ILE CG1   HG13   sing N N 257 
ILE CG2   HG21   sing N N 258 
ILE CG2   HG22   sing N N 259 
ILE CG2   HG23   sing N N 260 
ILE CD1   HD11   sing N N 261 
ILE CD1   HD12   sing N N 262 
ILE CD1   HD13   sing N N 263 
ILE OXT   HXT    sing N N 264 
LEU N     CA     sing N N 265 
LEU N     H      sing N N 266 
LEU N     H2     sing N N 267 
LEU CA    C      sing N N 268 
LEU CA    CB     sing N N 269 
LEU CA    HA     sing N N 270 
LEU C     O      doub N N 271 
LEU C     OXT    sing N N 272 
LEU CB    CG     sing N N 273 
LEU CB    HB2    sing N N 274 
LEU CB    HB3    sing N N 275 
LEU CG    CD1    sing N N 276 
LEU CG    CD2    sing N N 277 
LEU CG    HG     sing N N 278 
LEU CD1   HD11   sing N N 279 
LEU CD1   HD12   sing N N 280 
LEU CD1   HD13   sing N N 281 
LEU CD2   HD21   sing N N 282 
LEU CD2   HD22   sing N N 283 
LEU CD2   HD23   sing N N 284 
LEU OXT   HXT    sing N N 285 
LYS N     CA     sing N N 286 
LYS N     H      sing N N 287 
LYS N     H2     sing N N 288 
LYS CA    C      sing N N 289 
LYS CA    CB     sing N N 290 
LYS CA    HA     sing N N 291 
LYS C     O      doub N N 292 
LYS C     OXT    sing N N 293 
LYS CB    CG     sing N N 294 
LYS CB    HB2    sing N N 295 
LYS CB    HB3    sing N N 296 
LYS CG    CD     sing N N 297 
LYS CG    HG2    sing N N 298 
LYS CG    HG3    sing N N 299 
LYS CD    CE     sing N N 300 
LYS CD    HD2    sing N N 301 
LYS CD    HD3    sing N N 302 
LYS CE    NZ     sing N N 303 
LYS CE    HE2    sing N N 304 
LYS CE    HE3    sing N N 305 
LYS NZ    HZ1    sing N N 306 
LYS NZ    HZ2    sing N N 307 
LYS NZ    HZ3    sing N N 308 
LYS OXT   HXT    sing N N 309 
MET N     CA     sing N N 310 
MET N     H      sing N N 311 
MET N     H2     sing N N 312 
MET CA    C      sing N N 313 
MET CA    CB     sing N N 314 
MET CA    HA     sing N N 315 
MET C     O      doub N N 316 
MET C     OXT    sing N N 317 
MET CB    CG     sing N N 318 
MET CB    HB2    sing N N 319 
MET CB    HB3    sing N N 320 
MET CG    SD     sing N N 321 
MET CG    HG2    sing N N 322 
MET CG    HG3    sing N N 323 
MET SD    CE     sing N N 324 
MET CE    HE1    sing N N 325 
MET CE    HE2    sing N N 326 
MET CE    HE3    sing N N 327 
MET OXT   HXT    sing N N 328 
PHE N     CA     sing N N 329 
PHE N     H      sing N N 330 
PHE N     H2     sing N N 331 
PHE CA    C      sing N N 332 
PHE CA    CB     sing N N 333 
PHE CA    HA     sing N N 334 
PHE C     O      doub N N 335 
PHE C     OXT    sing N N 336 
PHE CB    CG     sing N N 337 
PHE CB    HB2    sing N N 338 
PHE CB    HB3    sing N N 339 
PHE CG    CD1    doub Y N 340 
PHE CG    CD2    sing Y N 341 
PHE CD1   CE1    sing Y N 342 
PHE CD1   HD1    sing N N 343 
PHE CD2   CE2    doub Y N 344 
PHE CD2   HD2    sing N N 345 
PHE CE1   CZ     doub Y N 346 
PHE CE1   HE1    sing N N 347 
PHE CE2   CZ     sing Y N 348 
PHE CE2   HE2    sing N N 349 
PHE CZ    HZ     sing N N 350 
PHE OXT   HXT    sing N N 351 
PRO N     CA     sing N N 352 
PRO N     CD     sing N N 353 
PRO N     H      sing N N 354 
PRO CA    C      sing N N 355 
PRO CA    CB     sing N N 356 
PRO CA    HA     sing N N 357 
PRO C     O      doub N N 358 
PRO C     OXT    sing N N 359 
PRO CB    CG     sing N N 360 
PRO CB    HB2    sing N N 361 
PRO CB    HB3    sing N N 362 
PRO CG    CD     sing N N 363 
PRO CG    HG2    sing N N 364 
PRO CG    HG3    sing N N 365 
PRO CD    HD2    sing N N 366 
PRO CD    HD3    sing N N 367 
PRO OXT   HXT    sing N N 368 
SER N     CA     sing N N 369 
SER N     H      sing N N 370 
SER N     H2     sing N N 371 
SER CA    C      sing N N 372 
SER CA    CB     sing N N 373 
SER CA    HA     sing N N 374 
SER C     O      doub N N 375 
SER C     OXT    sing N N 376 
SER CB    OG     sing N N 377 
SER CB    HB2    sing N N 378 
SER CB    HB3    sing N N 379 
SER OG    HG     sing N N 380 
SER OXT   HXT    sing N N 381 
THR N     CA     sing N N 382 
THR N     H      sing N N 383 
THR N     H2     sing N N 384 
THR CA    C      sing N N 385 
THR CA    CB     sing N N 386 
THR CA    HA     sing N N 387 
THR C     O      doub N N 388 
THR C     OXT    sing N N 389 
THR CB    OG1    sing N N 390 
THR CB    CG2    sing N N 391 
THR CB    HB     sing N N 392 
THR OG1   HG1    sing N N 393 
THR CG2   HG21   sing N N 394 
THR CG2   HG22   sing N N 395 
THR CG2   HG23   sing N N 396 
THR OXT   HXT    sing N N 397 
TRP N     CA     sing N N 398 
TRP N     H      sing N N 399 
TRP N     H2     sing N N 400 
TRP CA    C      sing N N 401 
TRP CA    CB     sing N N 402 
TRP CA    HA     sing N N 403 
TRP C     O      doub N N 404 
TRP C     OXT    sing N N 405 
TRP CB    CG     sing N N 406 
TRP CB    HB2    sing N N 407 
TRP CB    HB3    sing N N 408 
TRP CG    CD1    doub Y N 409 
TRP CG    CD2    sing Y N 410 
TRP CD1   NE1    sing Y N 411 
TRP CD1   HD1    sing N N 412 
TRP CD2   CE2    doub Y N 413 
TRP CD2   CE3    sing Y N 414 
TRP NE1   CE2    sing Y N 415 
TRP NE1   HE1    sing N N 416 
TRP CE2   CZ2    sing Y N 417 
TRP CE3   CZ3    doub Y N 418 
TRP CE3   HE3    sing N N 419 
TRP CZ2   CH2    doub Y N 420 
TRP CZ2   HZ2    sing N N 421 
TRP CZ3   CH2    sing Y N 422 
TRP CZ3   HZ3    sing N N 423 
TRP CH2   HH2    sing N N 424 
TRP OXT   HXT    sing N N 425 
TTP PA    O1A    doub N N 426 
TTP PA    O2A    sing N N 427 
TTP PA    O3A    sing N N 428 
TTP PA    "O5'"  sing N N 429 
TTP O2A   HOA2   sing N N 430 
TTP O3A   PB     sing N N 431 
TTP PB    O1B    doub N N 432 
TTP PB    O2B    sing N N 433 
TTP PB    O3B    sing N N 434 
TTP O2B   HOB2   sing N N 435 
TTP O3B   PG     sing N N 436 
TTP PG    O1G    doub N N 437 
TTP PG    O2G    sing N N 438 
TTP PG    O3G    sing N N 439 
TTP O2G   HOG2   sing N N 440 
TTP O3G   HOG3   sing N N 441 
TTP "O5'" "C5'"  sing N N 442 
TTP "C5'" "C4'"  sing N N 443 
TTP "C5'" "H5'1" sing N N 444 
TTP "C5'" "H5'2" sing N N 445 
TTP "C4'" "O4'"  sing N N 446 
TTP "C4'" "C3'"  sing N N 447 
TTP "C4'" "H4'"  sing N N 448 
TTP "O4'" "C1'"  sing N N 449 
TTP "C3'" "O3'"  sing N N 450 
TTP "C3'" "C2'"  sing N N 451 
TTP "C3'" "H3'"  sing N N 452 
TTP "O3'" "HO3'" sing N N 453 
TTP "C2'" "C1'"  sing N N 454 
TTP "C2'" "H2'1" sing N N 455 
TTP "C2'" "H2'2" sing N N 456 
TTP "C1'" N1     sing N N 457 
TTP "C1'" "H1'"  sing N N 458 
TTP N1    C2     sing N N 459 
TTP N1    C6     sing N N 460 
TTP C2    O2     doub N N 461 
TTP C2    N3     sing N N 462 
TTP N3    C4     sing N N 463 
TTP N3    HN3    sing N N 464 
TTP C4    O4     doub N N 465 
TTP C4    C5     sing N N 466 
TTP C5    C5M    sing N N 467 
TTP C5    C6     doub N N 468 
TTP C5M   HM51   sing N N 469 
TTP C5M   HM52   sing N N 470 
TTP C5M   HM53   sing N N 471 
TTP C6    H6     sing N N 472 
TYR N     CA     sing N N 473 
TYR N     H      sing N N 474 
TYR N     H2     sing N N 475 
TYR CA    C      sing N N 476 
TYR CA    CB     sing N N 477 
TYR CA    HA     sing N N 478 
TYR C     O      doub N N 479 
TYR C     OXT    sing N N 480 
TYR CB    CG     sing N N 481 
TYR CB    HB2    sing N N 482 
TYR CB    HB3    sing N N 483 
TYR CG    CD1    doub Y N 484 
TYR CG    CD2    sing Y N 485 
TYR CD1   CE1    sing Y N 486 
TYR CD1   HD1    sing N N 487 
TYR CD2   CE2    doub Y N 488 
TYR CD2   HD2    sing N N 489 
TYR CE1   CZ     doub Y N 490 
TYR CE1   HE1    sing N N 491 
TYR CE2   CZ     sing Y N 492 
TYR CE2   HE2    sing N N 493 
TYR CZ    OH     sing N N 494 
TYR OH    HH     sing N N 495 
TYR OXT   HXT    sing N N 496 
VAL N     CA     sing N N 497 
VAL N     H      sing N N 498 
VAL N     H2     sing N N 499 
VAL CA    C      sing N N 500 
VAL CA    CB     sing N N 501 
VAL CA    HA     sing N N 502 
VAL C     O      doub N N 503 
VAL C     OXT    sing N N 504 
VAL CB    CG1    sing N N 505 
VAL CB    CG2    sing N N 506 
VAL CB    HB     sing N N 507 
VAL CG1   HG11   sing N N 508 
VAL CG1   HG12   sing N N 509 
VAL CG1   HG13   sing N N 510 
VAL CG2   HG21   sing N N 511 
VAL CG2   HG22   sing N N 512 
VAL CG2   HG23   sing N N 513 
VAL OXT   HXT    sing N N 514 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-24 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BYY 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              'Class 9 model for turnover condition of Bacillus subtilis ribonucleotide reductase complex' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          1423 
_em_entity_assembly_naturalsource.organism             'Bacillus subtilis' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       COUNTING 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    20 
_em_imaging_optics.energyfilter_name          ? 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                ? 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ?               ? 
'IMAGE ACQUISITION'        ? 2  ? ? ? ?               ? 
MASKING                    ? 3  ? ? ? ?               ? 
'CTF CORRECTION'           ? 4  1 ? ? ?               ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ?               ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?               ? 
'MODEL FITTING'            ? 7  ? 1 ? 'UCSF ChimeraX' ? 
OTHER                      ? 8  ? ? ? ?               ? 
'INITIAL EULER ASSIGNMENT' ? 9  1 ? ? RELION          ? 
'FINAL EULER ASSIGNMENT'   ? 10 1 ? ? RELION          ? 
CLASSIFICATION             ? 11 1 ? ? ?               ? 
RECONSTRUCTION             ? 12 1 ? ? RELION          ? 
'MODEL REFINEMENT'         ? 13 ? 1 ? ?               ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Science Foundation (NSF, United States)' 'United States' MCB-1942668 1 
'National Science Foundation (NSF, United States)' 'United States' DMR-1719875 2 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
1 'experimental model' PDB 9BYH 
2 'experimental model' PDB 4DR0 
# 
_atom_sites.entry_id                    9BYY 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
MN 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . VAL A 1 6   ? 105.997 118.255 97.917  1.00 61.20 ?  6   VAL A N     1 
ATOM   2     C  CA    . VAL A 1 6   ? 107.069 118.998 97.269  1.00 61.32 ?  6   VAL A CA    1 
ATOM   3     C  C     . VAL A 1 6   ? 106.494 119.983 96.250  1.00 62.07 ?  6   VAL A C     1 
ATOM   4     O  O     . VAL A 1 6   ? 105.691 119.609 95.395  1.00 60.69 ?  6   VAL A O     1 
ATOM   5     C  CB    . VAL A 1 6   ? 108.093 118.038 96.617  1.00 61.34 ?  6   VAL A CB    1 
ATOM   6     C  CG1   . VAL A 1 6   ? 107.406 117.068 95.663  1.00 61.29 ?  6   VAL A CG1   1 
ATOM   7     C  CG2   . VAL A 1 6   ? 109.181 118.820 95.901  1.00 59.53 ?  6   VAL A CG2   1 
ATOM   8     N  N     . PRO A 1 7   ? 106.887 121.250 96.358  1.00 58.51 ?  7   PRO A N     1 
ATOM   9     C  CA    . PRO A 1 7   ? 106.378 122.262 95.426  1.00 54.85 ?  7   PRO A CA    1 
ATOM   10    C  C     . PRO A 1 7   ? 106.954 122.080 94.030  1.00 54.57 ?  7   PRO A C     1 
ATOM   11    O  O     . PRO A 1 7   ? 108.015 121.487 93.833  1.00 55.81 ?  7   PRO A O     1 
ATOM   12    C  CB    . PRO A 1 7   ? 106.824 123.595 96.038  1.00 53.42 ?  7   PRO A CB    1 
ATOM   13    C  CG    . PRO A 1 7   ? 107.597 123.276 97.263  1.00 53.02 ?  7   PRO A CG    1 
ATOM   14    C  CD    . PRO A 1 7   ? 107.781 121.806 97.386  1.00 55.87 ?  7   PRO A CD    1 
ATOM   15    N  N     . LYS A 1 8   ? 106.224 122.620 93.049  1.00 54.03 ?  8   LYS A N     1 
ATOM   16    C  CA    . LYS A 1 8   ? 106.583 122.417 91.648  1.00 53.45 ?  8   LYS A CA    1 
ATOM   17    C  C     . LYS A 1 8   ? 107.948 123.012 91.324  1.00 55.16 ?  8   LYS A C     1 
ATOM   18    O  O     . LYS A 1 8   ? 108.744 122.399 90.600  1.00 57.31 ?  8   LYS A O     1 
ATOM   19    C  CB    . LYS A 1 8   ? 105.507 123.019 90.743  1.00 55.50 ?  8   LYS A CB    1 
ATOM   20    C  CG    . LYS A 1 8   ? 105.854 122.998 89.264  1.00 55.15 ?  8   LYS A CG    1 
ATOM   21    C  CD    . LYS A 1 8   ? 104.909 123.881 88.465  1.00 55.42 ?  8   LYS A CD    1 
ATOM   22    C  CE    . LYS A 1 8   ? 105.339 123.976 87.010  1.00 55.63 ?  8   LYS A CE    1 
ATOM   23    N  NZ    . LYS A 1 8   ? 104.613 125.054 86.285  1.00 56.86 1  8   LYS A NZ    1 
ATOM   24    N  N     . TRP A 1 9   ? 108.237 124.209 91.841  1.00 54.44 ?  9   TRP A N     1 
ATOM   25    C  CA    . TRP A 1 9   ? 109.526 124.830 91.558  1.00 52.69 ?  9   TRP A CA    1 
ATOM   26    C  C     . TRP A 1 9   ? 110.671 124.019 92.147  1.00 51.63 ?  9   TRP A C     1 
ATOM   27    O  O     . TRP A 1 9   ? 111.754 123.954 91.556  1.00 53.76 ?  9   TRP A O     1 
ATOM   28    C  CB    . TRP A 1 9   ? 109.559 126.265 92.085  1.00 52.54 ?  9   TRP A CB    1 
ATOM   29    C  CG    . TRP A 1 9   ? 109.332 126.397 93.560  1.00 49.94 ?  9   TRP A CG    1 
ATOM   30    C  CD1   . TRP A 1 9   ? 110.275 126.320 94.541  1.00 49.74 ?  9   TRP A CD1   1 
ATOM   31    C  CD2   . TRP A 1 9   ? 108.088 126.654 94.220  1.00 51.38 ?  9   TRP A CD2   1 
ATOM   32    N  NE1   . TRP A 1 9   ? 109.697 126.501 95.773  1.00 49.45 ?  9   TRP A NE1   1 
ATOM   33    C  CE2   . TRP A 1 9   ? 108.354 126.709 95.603  1.00 51.17 ?  9   TRP A CE2   1 
ATOM   34    C  CE3   . TRP A 1 9   ? 106.775 126.836 93.779  1.00 49.58 ?  9   TRP A CE3   1 
ATOM   35    C  CZ2   . TRP A 1 9   ? 107.356 126.940 96.546  1.00 49.84 ?  9   TRP A CZ2   1 
ATOM   36    C  CZ3   . TRP A 1 9   ? 105.786 127.063 94.717  1.00 51.27 ?  9   TRP A CZ3   1 
ATOM   37    C  CH2   . TRP A 1 9   ? 106.081 127.111 96.084  1.00 51.47 ?  9   TRP A CH2   1 
ATOM   38    N  N     . ILE A 1 10  ? 110.448 123.377 93.295  1.00 54.01 ?  10  ILE A N     1 
ATOM   39    C  CA    . ILE A 1 10  ? 111.494 122.554 93.891  1.00 53.77 ?  10  ILE A CA    1 
ATOM   40    C  C     . ILE A 1 10  ? 111.741 121.307 93.048  1.00 53.66 ?  10  ILE A C     1 
ATOM   41    O  O     . ILE A 1 10  ? 112.887 120.875 92.884  1.00 56.41 ?  10  ILE A O     1 
ATOM   42    C  CB    . ILE A 1 10  ? 111.135 122.209 95.347  1.00 54.66 ?  10  ILE A CB    1 
ATOM   43    C  CG1   . ILE A 1 10  ? 111.240 123.464 96.216  1.00 54.34 ?  10  ILE A CG1   1 
ATOM   44    C  CG2   . ILE A 1 10  ? 112.050 121.121 95.883  1.00 54.60 ?  10  ILE A CG2   1 
ATOM   45    C  CD1   . ILE A 1 10  ? 111.209 123.195 97.699  1.00 55.93 ?  10  ILE A CD1   1 
ATOM   46    N  N     . GLN A 1 11  ? 110.682 120.712 92.494  1.00 57.00 ?  11  GLN A N     1 
ATOM   47    C  CA    . GLN A 1 11  ? 110.879 119.595 91.573  1.00 57.95 ?  11  GLN A CA    1 
ATOM   48    C  C     . GLN A 1 11  ? 111.638 120.035 90.328  1.00 57.73 ?  11  GLN A C     1 
ATOM   49    O  O     . GLN A 1 11  ? 112.549 119.336 89.867  1.00 59.00 ?  11  GLN A O     1 
ATOM   50    C  CB    . GLN A 1 11  ? 109.538 118.972 91.184  1.00 57.52 ?  11  GLN A CB    1 
ATOM   51    C  CG    . GLN A 1 11  ? 108.555 118.811 92.327  1.00 58.92 ?  11  GLN A CG    1 
ATOM   52    C  CD    . GLN A 1 11  ? 107.112 118.859 91.863  1.00 60.78 ?  11  GLN A CD    1 
ATOM   53    O  OE1   . GLN A 1 11  ? 106.834 118.909 90.666  1.00 58.86 ?  11  GLN A OE1   1 
ATOM   54    N  NE2   . GLN A 1 11  ? 106.185 118.844 92.814  1.00 58.93 ?  11  GLN A NE2   1 
ATOM   55    N  N     . LEU A 1 12  ? 111.282 121.196 89.774  1.00 53.91 ?  12  LEU A N     1 
ATOM   56    C  CA    . LEU A 1 12  ? 111.985 121.693 88.595  1.00 52.66 ?  12  LEU A CA    1 
ATOM   57    C  C     . LEU A 1 12  ? 113.445 122.001 88.901  1.00 54.69 ?  12  LEU A C     1 
ATOM   58    O  O     . LEU A 1 12  ? 114.305 121.868 88.023  1.00 56.24 ?  12  LEU A O     1 
ATOM   59    C  CB    . LEU A 1 12  ? 111.280 122.933 88.047  1.00 52.80 ?  12  LEU A CB    1 
ATOM   60    C  CG    . LEU A 1 12  ? 110.118 122.679 87.085  1.00 53.51 ?  12  LEU A CG    1 
ATOM   61    C  CD1   . LEU A 1 12  ? 109.326 123.954 86.846  1.00 55.35 ?  12  LEU A CD1   1 
ATOM   62    C  CD2   . LEU A 1 12  ? 110.628 122.108 85.772  1.00 52.97 ?  12  LEU A CD2   1 
ATOM   63    N  N     . ASN A 1 13  ? 113.743 122.416 90.133  1.00 53.32 ?  13  ASN A N     1 
ATOM   64    C  CA    . ASN A 1 13  ? 115.125 122.670 90.523  1.00 51.61 ?  13  ASN A CA    1 
ATOM   65    C  C     . ASN A 1 13  ? 115.900 121.372 90.724  1.00 53.33 ?  13  ASN A C     1 
ATOM   66    O  O     . ASN A 1 13  ? 117.056 121.266 90.301  1.00 57.21 ?  13  ASN A O     1 
ATOM   67    C  CB    . ASN A 1 13  ? 115.161 123.518 91.795  1.00 52.13 ?  13  ASN A CB    1 
ATOM   68    C  CG    . ASN A 1 13  ? 116.571 123.841 92.240  1.00 51.95 ?  13  ASN A CG    1 
ATOM   69    O  OD1   . ASN A 1 13  ? 117.126 123.179 93.115  1.00 52.22 ?  13  ASN A OD1   1 
ATOM   70    N  ND2   . ASN A 1 13  ? 117.159 124.868 91.637  1.00 53.37 ?  13  ASN A ND2   1 
ATOM   71    N  N     . ASN A 1 14  ? 115.285 120.378 91.369  1.00 56.37 ?  14  ASN A N     1 
ATOM   72    C  CA    . ASN A 1 14  ? 115.937 119.085 91.548  1.00 55.27 ?  14  ASN A CA    1 
ATOM   73    C  C     . ASN A 1 14  ? 116.074 118.319 90.242  1.00 55.96 ?  14  ASN A C     1 
ATOM   74    O  O     . ASN A 1 14  ? 116.869 117.376 90.171  1.00 59.84 ?  14  ASN A O     1 
ATOM   75    C  CB    . ASN A 1 14  ? 115.177 118.245 92.574  1.00 55.43 ?  14  ASN A CB    1 
ATOM   76    C  CG    . ASN A 1 14  ? 115.177 118.872 93.955  1.00 58.93 ?  14  ASN A CG    1 
ATOM   77    O  OD1   . ASN A 1 14  ? 115.179 120.093 94.096  1.00 59.21 ?  14  ASN A OD1   1 
ATOM   78    N  ND2   . ASN A 1 14  ? 115.173 118.033 94.983  1.00 59.70 ?  14  ASN A ND2   1 
ATOM   79    N  N     . GLU A 1 15  ? 115.322 118.698 89.208  1.00 57.11 ?  15  GLU A N     1 
ATOM   80    C  CA    . GLU A 1 15  ? 115.494 118.077 87.901  1.00 58.53 ?  15  GLU A CA    1 
ATOM   81    C  C     . GLU A 1 15  ? 116.814 118.450 87.237  1.00 58.60 ?  15  GLU A C     1 
ATOM   82    O  O     . GLU A 1 15  ? 117.143 117.874 86.195  1.00 61.66 ?  15  GLU A O     1 
ATOM   83    C  CB    . GLU A 1 15  ? 114.325 118.445 86.984  1.00 58.15 ?  15  GLU A CB    1 
ATOM   84    C  CG    . GLU A 1 15  ? 113.069 117.624 87.234  1.00 58.81 ?  15  GLU A CG    1 
ATOM   85    C  CD    . GLU A 1 15  ? 111.873 118.121 86.444  1.00 61.24 ?  15  GLU A CD    1 
ATOM   86    O  OE1   . GLU A 1 15  ? 112.076 118.691 85.353  1.00 60.87 ?  15  GLU A OE1   1 
ATOM   87    O  OE2   . GLU A 1 15  ? 110.731 117.941 86.915  1.00 59.03 -1 15  GLU A OE2   1 
ATOM   88    N  N     . ILE A 1 16  ? 117.564 119.401 87.800  1.00 58.15 ?  16  ILE A N     1 
ATOM   89    C  CA    . ILE A 1 16  ? 118.869 119.757 87.244  1.00 58.69 ?  16  ILE A CA    1 
ATOM   90    C  C     . ILE A 1 16  ? 119.815 118.566 87.304  1.00 57.58 ?  16  ILE A C     1 
ATOM   91    O  O     . ILE A 1 16  ? 120.499 118.241 86.326  1.00 58.61 ?  16  ILE A O     1 
ATOM   92    C  CB    . ILE A 1 16  ? 119.457 120.969 87.989  1.00 57.30 ?  16  ILE A CB    1 
ATOM   93    C  CG1   . ILE A 1 16  ? 118.713 122.250 87.620  1.00 56.73 ?  16  ILE A CG1   1 
ATOM   94    C  CG2   . ILE A 1 16  ? 120.943 121.115 87.689  1.00 57.89 ?  16  ILE A CG2   1 
ATOM   95    C  CD1   . ILE A 1 16  ? 118.827 123.320 88.672  1.00 56.64 ?  16  ILE A CD1   1 
ATOM   96    N  N     . MET A 1 17  ? 119.866 117.894 88.458  1.00 57.91 ?  17  MET A N     1 
ATOM   97    C  CA    . MET A 1 17  ? 120.797 116.784 88.630  1.00 60.77 ?  17  MET A CA    1 
ATOM   98    C  C     . MET A 1 17  ? 120.449 115.608 87.730  1.00 60.83 ?  17  MET A C     1 
ATOM   99    O  O     . MET A 1 17  ? 121.334 114.824 87.370  1.00 61.69 ?  17  MET A O     1 
ATOM   100   C  CB    . MET A 1 17  ? 120.820 116.339 90.091  1.00 60.42 ?  17  MET A CB    1 
ATOM   101   C  CG    . MET A 1 17  ? 121.194 117.437 91.071  1.00 59.88 ?  17  MET A CG    1 
ATOM   102   S  SD    . MET A 1 17  ? 122.232 118.741 90.385  1.00 62.45 ?  17  MET A SD    1 
ATOM   103   C  CE    . MET A 1 17  ? 123.814 117.906 90.315  1.00 58.33 ?  17  MET A CE    1 
ATOM   104   N  N     . ILE A 1 18  ? 119.177 115.462 87.364  1.00 63.10 ?  18  ILE A N     1 
ATOM   105   C  CA    . ILE A 1 18  ? 118.766 114.398 86.452  1.00 63.93 ?  18  ILE A CA    1 
ATOM   106   C  C     . ILE A 1 18  ? 119.414 114.679 85.100  1.00 64.49 ?  18  ILE A C     1 
ATOM   107   O  O     . ILE A 1 18  ? 119.146 115.707 84.473  1.00 66.32 ?  18  ILE A O     1 
ATOM   108   C  CB    . ILE A 1 18  ? 117.238 114.297 86.336  1.00 63.43 ?  18  ILE A CB    1 
ATOM   109   C  CG1   . ILE A 1 18  ? 116.615 113.511 87.503  1.00 64.00 ?  18  ILE A CG1   1 
ATOM   110   C  CG2   . ILE A 1 18  ? 116.842 113.637 85.023  1.00 63.67 ?  18  ILE A CG2   1 
ATOM   111   C  CD1   . ILE A 1 18  ? 117.145 113.814 88.891  1.00 63.77 ?  18  ILE A CD1   1 
ATOM   112   N  N     . GLN A 1 19  ? 120.282 113.774 84.657  1.00 67.59 ?  19  GLN A N     1 
ATOM   113   C  CA    . GLN A 1 19  ? 121.090 114.019 83.473  1.00 69.12 ?  19  GLN A CA    1 
ATOM   114   C  C     . GLN A 1 19  ? 120.370 113.538 82.220  1.00 70.12 ?  19  GLN A C     1 
ATOM   115   O  O     . GLN A 1 19  ? 119.917 112.391 82.152  1.00 70.79 ?  19  GLN A O     1 
ATOM   116   C  CB    . GLN A 1 19  ? 122.445 113.324 83.605  1.00 70.18 ?  19  GLN A CB    1 
ATOM   117   C  CG    . GLN A 1 19  ? 123.403 114.022 84.558  1.00 68.31 ?  19  GLN A CG    1 
ATOM   118   C  CD    . GLN A 1 19  ? 124.850 113.648 84.311  1.00 70.65 ?  19  GLN A CD    1 
ATOM   119   O  OE1   . GLN A 1 19  ? 125.179 113.034 83.297  1.00 71.53 ?  19  GLN A OE1   1 
ATOM   120   N  NE2   . GLN A 1 19  ? 125.724 114.018 85.239  1.00 69.08 ?  19  GLN A NE2   1 
ATOM   121   N  N     . LYS A 1 20  ? 120.265 114.420 81.232  1.00 72.27 ?  20  LYS A N     1 
ATOM   122   C  CA    . LYS A 1 20  ? 119.707 114.092 79.928  1.00 73.91 ?  20  LYS A CA    1 
ATOM   123   C  C     . LYS A 1 20  ? 120.818 114.175 78.891  1.00 76.01 ?  20  LYS A C     1 
ATOM   124   O  O     . LYS A 1 20  ? 121.489 115.207 78.779  1.00 75.81 ?  20  LYS A O     1 
ATOM   125   C  CB    . LYS A 1 20  ? 118.557 115.036 79.569  1.00 71.70 ?  20  LYS A CB    1 
ATOM   126   C  CG    . LYS A 1 20  ? 118.267 115.142 78.080  1.00 73.05 ?  20  LYS A CG    1 
ATOM   127   C  CD    . LYS A 1 20  ? 118.716 116.482 77.519  1.00 74.70 ?  20  LYS A CD    1 
ATOM   128   C  CE    . LYS A 1 20  ? 118.986 116.394 76.025  1.00 74.77 ?  20  LYS A CE    1 
ATOM   129   N  NZ    . LYS A 1 20  ? 118.921 117.731 75.370  1.00 74.65 1  20  LYS A NZ    1 
ATOM   130   N  N     . ASP A 1 21  ? 121.009 113.086 78.145  1.00 77.71 ?  21  ASP A N     1 
ATOM   131   C  CA    . ASP A 1 21  ? 122.096 112.975 77.170  1.00 78.08 ?  21  ASP A CA    1 
ATOM   132   C  C     . ASP A 1 21  ? 123.454 113.203 77.831  1.00 78.21 ?  21  ASP A C     1 
ATOM   133   O  O     . ASP A 1 21  ? 124.362 113.798 77.245  1.00 77.84 ?  21  ASP A O     1 
ATOM   134   C  CB    . ASP A 1 21  ? 121.890 113.936 75.996  1.00 78.03 ?  21  ASP A CB    1 
ATOM   135   C  CG    . ASP A 1 21  ? 122.672 113.527 74.762  1.00 79.20 ?  21  ASP A CG    1 
ATOM   136   O  OD1   . ASP A 1 21  ? 122.696 112.318 74.448  1.00 77.85 ?  21  ASP A OD1   1 
ATOM   137   O  OD2   . ASP A 1 21  ? 123.264 114.412 74.110  1.00 77.64 -1 21  ASP A OD2   1 
ATOM   138   N  N     . GLY A 1 22  ? 123.594 112.730 79.066  1.00 74.06 ?  22  GLY A N     1 
ATOM   139   C  CA    . GLY A 1 22  ? 124.840 112.883 79.789  1.00 72.25 ?  22  GLY A CA    1 
ATOM   140   C  C     . GLY A 1 22  ? 125.174 114.300 80.190  1.00 73.50 ?  22  GLY A C     1 
ATOM   141   O  O     . GLY A 1 22  ? 126.342 114.598 80.454  1.00 74.68 ?  22  GLY A O     1 
ATOM   142   N  N     . LYS A 1 23  ? 124.184 115.187 80.246  1.00 69.34 ?  23  LYS A N     1 
ATOM   143   C  CA    . LYS A 1 23  ? 124.404 116.580 80.602  1.00 67.22 ?  23  LYS A CA    1 
ATOM   144   C  C     . LYS A 1 23  ? 123.381 117.019 81.639  1.00 68.95 ?  23  LYS A C     1 
ATOM   145   O  O     . LYS A 1 23  ? 122.232 116.569 81.634  1.00 70.38 ?  23  LYS A O     1 
ATOM   146   C  CB    . LYS A 1 23  ? 124.318 117.497 79.374  1.00 68.25 ?  23  LYS A CB    1 
ATOM   147   C  CG    . LYS A 1 23  ? 125.407 117.262 78.343  1.00 68.58 ?  23  LYS A CG    1 
ATOM   148   C  CD    . LYS A 1 23  ? 125.141 118.056 77.076  1.00 68.77 ?  23  LYS A CD    1 
ATOM   149   C  CE    . LYS A 1 23  ? 126.097 117.659 75.966  1.00 71.00 ?  23  LYS A CE    1 
ATOM   150   N  NZ    . LYS A 1 23  ? 125.722 118.272 74.663  1.00 69.00 1  23  LYS A NZ    1 
ATOM   151   N  N     . PHE A 1 24  ? 123.813 117.905 82.531  1.00 62.03 ?  24  PHE A N     1 
ATOM   152   C  CA    . PHE A 1 24  ? 122.912 118.461 83.529  1.00 59.31 ?  24  PHE A CA    1 
ATOM   153   C  C     . PHE A 1 24  ? 121.906 119.394 82.869  1.00 59.62 ?  24  PHE A C     1 
ATOM   154   O  O     . PHE A 1 24  ? 122.245 120.158 81.963  1.00 59.64 ?  24  PHE A O     1 
ATOM   155   C  CB    . PHE A 1 24  ? 123.702 119.213 84.598  1.00 57.58 ?  24  PHE A CB    1 
ATOM   156   C  CG    . PHE A 1 24  ? 124.581 118.331 85.436  1.00 59.16 ?  24  PHE A CG    1 
ATOM   157   C  CD1   . PHE A 1 24  ? 124.050 117.576 86.465  1.00 60.30 ?  24  PHE A CD1   1 
ATOM   158   C  CD2   . PHE A 1 24  ? 125.943 118.259 85.193  1.00 60.20 ?  24  PHE A CD2   1 
ATOM   159   C  CE1   . PHE A 1 24  ? 124.859 116.764 87.233  1.00 61.28 ?  24  PHE A CE1   1 
ATOM   160   C  CE2   . PHE A 1 24  ? 126.756 117.450 85.960  1.00 58.77 ?  24  PHE A CE2   1 
ATOM   161   C  CZ    . PHE A 1 24  ? 126.213 116.703 86.983  1.00 59.24 ?  24  PHE A CZ    1 
ATOM   162   N  N     . GLN A 1 25  ? 120.656 119.325 83.328  1.00 59.49 ?  25  GLN A N     1 
ATOM   163   C  CA    . GLN A 1 25  ? 119.590 120.175 82.799  1.00 61.28 ?  25  GLN A CA    1 
ATOM   164   C  C     . GLN A 1 25  ? 119.632 121.515 83.528  1.00 60.68 ?  25  GLN A C     1 
ATOM   165   O  O     . GLN A 1 25  ? 118.812 121.822 84.397  1.00 62.38 ?  25  GLN A O     1 
ATOM   166   C  CB    . GLN A 1 25  ? 118.235 119.494 82.943  1.00 61.69 ?  25  GLN A CB    1 
ATOM   167   C  CG    . GLN A 1 25  ? 118.072 118.253 82.084  1.00 60.60 ?  25  GLN A CG    1 
ATOM   168   C  CD    . GLN A 1 25  ? 116.816 117.476 82.420  1.00 61.28 ?  25  GLN A CD    1 
ATOM   169   O  OE1   . GLN A 1 25  ? 115.742 117.752 81.888  1.00 60.75 ?  25  GLN A OE1   1 
ATOM   170   N  NE2   . GLN A 1 25  ? 116.947 116.497 83.306  1.00 60.63 ?  25  GLN A NE2   1 
ATOM   171   N  N     . PHE A 1 26  ? 120.628 122.326 83.163  1.00 56.32 ?  26  PHE A N     1 
ATOM   172   C  CA    . PHE A 1 26  ? 120.779 123.642 83.775  1.00 54.81 ?  26  PHE A CA    1 
ATOM   173   C  C     . PHE A 1 26  ? 119.609 124.553 83.427  1.00 56.40 ?  26  PHE A C     1 
ATOM   174   O  O     . PHE A 1 26  ? 119.114 125.292 84.288  1.00 56.54 ?  26  PHE A O     1 
ATOM   175   C  CB    . PHE A 1 26  ? 122.099 124.273 83.335  1.00 51.71 ?  26  PHE A CB    1 
ATOM   176   C  CG    . PHE A 1 26  ? 123.315 123.548 83.836  1.00 54.69 ?  26  PHE A CG    1 
ATOM   177   C  CD1   . PHE A 1 26  ? 123.463 123.266 85.183  1.00 52.92 ?  26  PHE A CD1   1 
ATOM   178   C  CD2   . PHE A 1 26  ? 124.308 123.147 82.960  1.00 52.64 ?  26  PHE A CD2   1 
ATOM   179   C  CE1   . PHE A 1 26  ? 124.579 122.600 85.647  1.00 52.85 ?  26  PHE A CE1   1 
ATOM   180   C  CE2   . PHE A 1 26  ? 125.426 122.479 83.417  1.00 50.88 ?  26  PHE A CE2   1 
ATOM   181   C  CZ    . PHE A 1 26  ? 125.563 122.207 84.763  1.00 52.70 ?  26  PHE A CZ    1 
ATOM   182   N  N     . ASP A 1 27  ? 119.152 124.509 82.172  1.00 58.64 ?  27  ASP A N     1 
ATOM   183   C  CA    . ASP A 1 27  ? 118.064 125.381 81.739  1.00 58.79 ?  27  ASP A CA    1 
ATOM   184   C  C     . ASP A 1 27  ? 116.797 125.154 82.552  1.00 59.03 ?  27  ASP A C     1 
ATOM   185   O  O     . ASP A 1 27  ? 115.997 126.083 82.725  1.00 59.44 ?  27  ASP A O     1 
ATOM   186   C  CB    . ASP A 1 27  ? 117.790 125.173 80.248  1.00 59.79 ?  27  ASP A CB    1 
ATOM   187   C  CG    . ASP A 1 27  ? 117.451 123.732 79.908  1.00 62.16 ?  27  ASP A CG    1 
ATOM   188   O  OD1   . ASP A 1 27  ? 116.382 123.246 80.332  1.00 62.25 ?  27  ASP A OD1   1 
ATOM   189   O  OD2   . ASP A 1 27  ? 118.258 123.082 79.212  1.00 62.20 -1 27  ASP A OD2   1 
ATOM   190   N  N     . LYS A 1 28  ? 116.604 123.936 83.068  1.00 56.53 ?  28  LYS A N     1 
ATOM   191   C  CA    . LYS A 1 28  ? 115.439 123.659 83.901  1.00 58.97 ?  28  LYS A CA    1 
ATOM   192   C  C     . LYS A 1 28  ? 115.372 124.601 85.093  1.00 59.60 ?  28  LYS A C     1 
ATOM   193   O  O     . LYS A 1 28  ? 114.275 124.980 85.522  1.00 59.48 ?  28  LYS A O     1 
ATOM   194   C  CB    . LYS A 1 28  ? 115.463 122.206 84.372  1.00 58.52 ?  28  LYS A CB    1 
ATOM   195   C  CG    . LYS A 1 28  ? 114.961 121.212 83.340  1.00 60.37 ?  28  LYS A CG    1 
ATOM   196   C  CD    . LYS A 1 28  ? 113.497 120.880 83.562  1.00 59.68 ?  28  LYS A CD    1 
ATOM   197   C  CE    . LYS A 1 28  ? 112.827 120.453 82.269  1.00 58.32 ?  28  LYS A CE    1 
ATOM   198   N  NZ    . LYS A 1 28  ? 112.915 121.511 81.225  1.00 59.76 1  28  LYS A NZ    1 
ATOM   199   N  N     . ASP A 1 29  ? 116.532 125.005 85.623  1.00 57.46 ?  29  ASP A N     1 
ATOM   200   C  CA    . ASP A 1 29  ? 116.551 125.966 86.722  1.00 54.95 ?  29  ASP A CA    1 
ATOM   201   C  C     . ASP A 1 29  ? 115.757 127.212 86.371  1.00 53.98 ?  29  ASP A C     1 
ATOM   202   O  O     . ASP A 1 29  ? 114.954 127.692 87.181  1.00 56.72 ?  29  ASP A O     1 
ATOM   203   C  CB    . ASP A 1 29  ? 117.990 126.336 87.076  1.00 55.38 ?  29  ASP A CB    1 
ATOM   204   C  CG    . ASP A 1 29  ? 118.151 126.721 88.533  1.00 56.18 ?  29  ASP A CG    1 
ATOM   205   O  OD1   . ASP A 1 29  ? 117.348 126.251 89.367  1.00 55.71 ?  29  ASP A OD1   1 
ATOM   206   O  OD2   . ASP A 1 29  ? 119.083 127.491 88.846  1.00 55.40 -1 29  ASP A OD2   1 
ATOM   207   N  N     . LYS A 1 30  ? 115.941 127.730 85.153  1.00 54.92 ?  30  LYS A N     1 
ATOM   208   C  CA    . LYS A 1 30  ? 115.176 128.894 84.718  1.00 56.30 ?  30  LYS A CA    1 
ATOM   209   C  C     . LYS A 1 30  ? 113.682 128.638 84.854  1.00 55.88 ?  30  LYS A C     1 
ATOM   210   O  O     . LYS A 1 30  ? 112.949 129.454 85.426  1.00 58.29 ?  30  LYS A O     1 
ATOM   211   C  CB    . LYS A 1 30  ? 115.535 129.248 83.275  1.00 57.24 ?  30  LYS A CB    1 
ATOM   212   C  CG    . LYS A 1 30  ? 116.992 129.629 83.072  1.00 59.30 ?  30  LYS A CG    1 
ATOM   213   C  CD    . LYS A 1 30  ? 117.283 129.946 81.613  1.00 59.58 ?  30  LYS A CD    1 
ATOM   214   C  CE    . LYS A 1 30  ? 118.778 130.049 81.359  1.00 58.77 ?  30  LYS A CE    1 
ATOM   215   N  NZ    . LYS A 1 30  ? 119.133 129.731 79.948  1.00 58.18 1  30  LYS A NZ    1 
ATOM   216   N  N     . GLU A 1 31  ? 113.223 127.477 84.376  1.00 57.35 ?  31  GLU A N     1 
ATOM   217   C  CA    . GLU A 1 31  ? 111.813 127.133 84.513  1.00 56.70 ?  31  GLU A CA    1 
ATOM   218   C  C     . GLU A 1 31  ? 111.390 127.165 85.973  1.00 56.29 ?  31  GLU A C     1 
ATOM   219   O  O     . GLU A 1 31  ? 110.328 127.708 86.307  1.00 58.26 ?  31  GLU A O     1 
ATOM   220   C  CB    . GLU A 1 31  ? 111.544 125.754 83.903  1.00 56.01 ?  31  GLU A CB    1 
ATOM   221   C  CG    . GLU A 1 31  ? 112.282 125.445 82.593  1.00 58.50 ?  31  GLU A CG    1 
ATOM   222   C  CD    . GLU A 1 31  ? 111.882 126.337 81.419  1.00 61.13 ?  31  GLU A CD    1 
ATOM   223   O  OE1   . GLU A 1 31  ? 111.897 127.579 81.545  1.00 60.18 ?  31  GLU A OE1   1 
ATOM   224   O  OE2   . GLU A 1 31  ? 111.547 125.779 80.353  1.00 59.93 -1 31  GLU A OE2   1 
ATOM   225   N  N     . ALA A 1 32  ? 112.234 126.631 86.860  1.00 50.08 ?  32  ALA A N     1 
ATOM   226   C  CA    . ALA A 1 32  ? 111.934 126.660 88.286  1.00 48.71 ?  32  ALA A CA    1 
ATOM   227   C  C     . ALA A 1 32  ? 111.635 128.078 88.745  1.00 52.68 ?  32  ALA A C     1 
ATOM   228   O  O     . ALA A 1 32  ? 110.635 128.321 89.434  1.00 55.36 ?  32  ALA A O     1 
ATOM   229   C  CB    . ALA A 1 32  ? 113.099 126.066 89.080  1.00 47.76 ?  32  ALA A CB    1 
ATOM   230   N  N     . VAL A 1 33  ? 112.462 129.040 88.321  1.00 50.76 ?  33  VAL A N     1 
ATOM   231   C  CA    . VAL A 1 33  ? 112.239 130.430 88.711  1.00 49.52 ?  33  VAL A CA    1 
ATOM   232   C  C     . VAL A 1 33  ? 110.834 130.853 88.318  1.00 50.65 ?  33  VAL A C     1 
ATOM   233   O  O     . VAL A 1 33  ? 110.075 131.388 89.136  1.00 52.98 ?  33  VAL A O     1 
ATOM   234   C  CB    . VAL A 1 33  ? 113.293 131.354 88.075  1.00 50.41 ?  33  VAL A CB    1 
ATOM   235   C  CG1   . VAL A 1 33  ? 113.401 132.653 88.863  1.00 48.62 ?  33  VAL A CG1   1 
ATOM   236   C  CG2   . VAL A 1 33  ? 114.627 130.662 87.984  1.00 50.88 ?  33  VAL A CG2   1 
ATOM   237   N  N     . HIS A 1 34  ? 110.451 130.565 87.071  1.00 47.66 ?  34  HIS A N     1 
ATOM   238   C  CA    . HIS A 1 34  ? 109.110 130.899 86.614  1.00 47.52 ?  34  HIS A CA    1 
ATOM   239   C  C     . HIS A 1 34  ? 108.069 130.297 87.543  1.00 50.23 ?  34  HIS A C     1 
ATOM   240   O  O     . HIS A 1 34  ? 107.176 130.997 88.035  1.00 54.05 ?  34  HIS A O     1 
ATOM   241   C  CB    . HIS A 1 34  ? 108.916 130.411 85.180  1.00 50.92 ?  34  HIS A CB    1 
ATOM   242   C  CG    . HIS A 1 34  ? 107.990 131.264 84.370  1.00 50.54 ?  34  HIS A CG    1 
ATOM   243   N  ND1   . HIS A 1 34  ? 106.690 131.519 84.749  1.00 53.04 ?  34  HIS A ND1   1 
ATOM   244   C  CD2   . HIS A 1 34  ? 108.179 131.926 83.205  1.00 51.78 ?  34  HIS A CD2   1 
ATOM   245   C  CE1   . HIS A 1 34  ? 106.117 132.297 83.849  1.00 54.94 ?  34  HIS A CE1   1 
ATOM   246   N  NE2   . HIS A 1 34  ? 106.999 132.559 82.902  1.00 54.28 ?  34  HIS A NE2   1 
ATOM   247   N  N     . SER A 1 35  ? 108.214 129.005 87.852  1.00 48.83 ?  35  SER A N     1 
ATOM   248   C  CA    . SER A 1 35  ? 107.291 128.367 88.780  1.00 49.75 ?  35  SER A CA    1 
ATOM   249   C  C     . SER A 1 35  ? 107.319 129.072 90.126  1.00 50.04 ?  35  SER A C     1 
ATOM   250   O  O     . SER A 1 35  ? 106.269 129.412 90.685  1.00 52.60 ?  35  SER A O     1 
ATOM   251   C  CB    . SER A 1 35  ? 107.639 126.886 88.931  1.00 50.64 ?  35  SER A CB    1 
ATOM   252   O  OG    . SER A 1 35  ? 106.868 126.282 89.955  1.00 52.65 ?  35  SER A OG    1 
ATOM   253   N  N     . TYR A 1 36  ? 108.523 129.362 90.630  1.00 47.40 ?  36  TYR A N     1 
ATOM   254   C  CA    . TYR A 1 36  ? 108.644 130.011 91.930  1.00 48.30 ?  36  TYR A CA    1 
ATOM   255   C  C     . TYR A 1 36  ? 107.944 131.361 91.937  1.00 46.43 ?  36  TYR A C     1 
ATOM   256   O  O     . TYR A 1 36  ? 107.537 131.843 92.999  1.00 46.71 ?  36  TYR A O     1 
ATOM   257   C  CB    . TYR A 1 36  ? 110.116 130.169 92.306  1.00 46.66 ?  36  TYR A CB    1 
ATOM   258   C  CG    . TYR A 1 36  ? 110.340 130.708 93.700  1.00 45.89 ?  36  TYR A CG    1 
ATOM   259   C  CD1   . TYR A 1 36  ? 109.854 130.034 94.812  1.00 46.40 ?  36  TYR A CD1   1 
ATOM   260   C  CD2   . TYR A 1 36  ? 111.041 131.887 93.905  1.00 45.04 ?  36  TYR A CD2   1 
ATOM   261   C  CE1   . TYR A 1 36  ? 110.059 130.521 96.088  1.00 44.74 ?  36  TYR A CE1   1 
ATOM   262   C  CE2   . TYR A 1 36  ? 111.251 132.381 95.177  1.00 44.92 ?  36  TYR A CE2   1 
ATOM   263   C  CZ    . TYR A 1 36  ? 110.758 131.695 96.264  1.00 45.50 ?  36  TYR A CZ    1 
ATOM   264   O  OH    . TYR A 1 36  ? 110.966 132.186 97.532  1.00 47.43 ?  36  TYR A OH    1 
ATOM   265   N  N     . PHE A 1 37  ? 107.779 131.974 90.767  1.00 48.48 ?  37  PHE A N     1 
ATOM   266   C  CA    . PHE A 1 37  ? 107.036 133.220 90.671  1.00 49.98 ?  37  PHE A CA    1 
ATOM   267   C  C     . PHE A 1 37  ? 105.586 133.015 90.266  1.00 52.80 ?  37  PHE A C     1 
ATOM   268   O  O     . PHE A 1 37  ? 104.732 133.822 90.641  1.00 56.29 ?  37  PHE A O     1 
ATOM   269   C  CB    . PHE A 1 37  ? 107.717 134.170 89.681  1.00 51.07 ?  37  PHE A CB    1 
ATOM   270   C  CG    . PHE A 1 37  ? 108.891 134.899 90.263  1.00 51.02 ?  37  PHE A CG    1 
ATOM   271   C  CD1   . PHE A 1 37  ? 108.715 136.099 90.931  1.00 50.72 ?  37  PHE A CD1   1 
ATOM   272   C  CD2   . PHE A 1 37  ? 110.167 134.377 90.160  1.00 50.97 ?  37  PHE A CD2   1 
ATOM   273   C  CE1   . PHE A 1 37  ? 109.793 136.767 91.475  1.00 50.45 ?  37  PHE A CE1   1 
ATOM   274   C  CE2   . PHE A 1 37  ? 111.247 135.041 90.701  1.00 50.90 ?  37  PHE A CE2   1 
ATOM   275   C  CZ    . PHE A 1 37  ? 111.060 136.236 91.362  1.00 49.87 ?  37  PHE A CZ    1 
ATOM   276   N  N     . VAL A 1 38  ? 105.284 131.948 89.523  1.00 54.56 ?  38  VAL A N     1 
ATOM   277   C  CA    . VAL A 1 38  ? 103.905 131.733 89.099  1.00 53.41 ?  38  VAL A CA    1 
ATOM   278   C  C     . VAL A 1 38  ? 103.089 131.109 90.222  1.00 53.94 ?  38  VAL A C     1 
ATOM   279   O  O     . VAL A 1 38  ? 101.899 131.409 90.379  1.00 55.77 ?  38  VAL A O     1 
ATOM   280   C  CB    . VAL A 1 38  ? 103.874 130.882 87.815  1.00 53.67 ?  38  VAL A CB    1 
ATOM   281   C  CG1   . VAL A 1 38  ? 102.592 130.069 87.721  1.00 56.03 ?  38  VAL A CG1   1 
ATOM   282   C  CG2   . VAL A 1 38  ? 104.016 131.776 86.598  1.00 52.77 ?  38  VAL A CG2   1 
ATOM   283   N  N     . ASP A 1 39  ? 103.710 130.260 91.038  1.00 52.80 ?  39  ASP A N     1 
ATOM   284   C  CA    . ASP A 1 39  ? 103.003 129.523 92.076  1.00 53.63 ?  39  ASP A CA    1 
ATOM   285   C  C     . ASP A 1 39  ? 103.085 130.176 93.448  1.00 57.33 ?  39  ASP A C     1 
ATOM   286   O  O     . ASP A 1 39  ? 102.104 130.146 94.197  1.00 58.77 ?  39  ASP A O     1 
ATOM   287   C  CB    . ASP A 1 39  ? 103.547 128.094 92.164  1.00 55.81 ?  39  ASP A CB    1 
ATOM   288   C  CG    . ASP A 1 39  ? 103.652 127.426 90.809  1.00 57.71 ?  39  ASP A CG    1 
ATOM   289   O  OD1   . ASP A 1 39  ? 102.780 127.677 89.952  1.00 56.94 ?  39  ASP A OD1   1 
ATOM   290   O  OD2   . ASP A 1 39  ? 104.608 126.650 90.600  1.00 58.02 -1 39  ASP A OD2   1 
ATOM   291   N  N     . TYR A 1 40  ? 104.225 130.767 93.808  1.00 55.98 ?  40  TYR A N     1 
ATOM   292   C  CA    . TYR A 1 40  ? 104.445 131.233 95.172  1.00 53.64 ?  40  TYR A CA    1 
ATOM   293   C  C     . TYR A 1 40  ? 104.575 132.747 95.279  1.00 58.23 ?  40  TYR A C     1 
ATOM   294   O  O     . TYR A 1 40  ? 103.821 133.375 96.027  1.00 60.63 ?  40  TYR A O     1 
ATOM   295   C  CB    . TYR A 1 40  ? 105.690 130.556 95.757  1.00 53.89 ?  40  TYR A CB    1 
ATOM   296   C  CG    . TYR A 1 40  ? 105.830 130.731 97.253  1.00 54.81 ?  40  TYR A CG    1 
ATOM   297   C  CD1   . TYR A 1 40  ? 106.503 131.823 97.784  1.00 53.49 ?  40  TYR A CD1   1 
ATOM   298   C  CD2   . TYR A 1 40  ? 105.283 129.807 98.132  1.00 55.81 ?  40  TYR A CD2   1 
ATOM   299   C  CE1   . TYR A 1 40  ? 106.631 131.988 99.149  1.00 55.23 ?  40  TYR A CE1   1 
ATOM   300   C  CE2   . TYR A 1 40  ? 105.406 129.964 99.499  1.00 57.31 ?  40  TYR A CE2   1 
ATOM   301   C  CZ    . TYR A 1 40  ? 106.080 131.055 100.001 1.00 58.22 ?  40  TYR A CZ    1 
ATOM   302   O  OH    . TYR A 1 40  ? 106.204 131.214 101.362 1.00 57.01 ?  40  TYR A OH    1 
ATOM   303   N  N     . ILE A 1 41  ? 105.518 133.356 94.557  1.00 55.03 ?  41  ILE A N     1 
ATOM   304   C  CA    . ILE A 1 41  ? 105.870 134.748 94.829  1.00 51.74 ?  41  ILE A CA    1 
ATOM   305   C  C     . ILE A 1 41  ? 104.703 135.675 94.511  1.00 50.75 ?  41  ILE A C     1 
ATOM   306   O  O     . ILE A 1 41  ? 104.332 136.529 95.325  1.00 53.01 ?  41  ILE A O     1 
ATOM   307   C  CB    . ILE A 1 41  ? 107.137 135.148 94.054  1.00 49.42 ?  41  ILE A CB    1 
ATOM   308   C  CG1   . ILE A 1 41  ? 108.359 134.422 94.620  1.00 48.58 ?  41  ILE A CG1   1 
ATOM   309   C  CG2   . ILE A 1 41  ? 107.351 136.648 94.133  1.00 48.07 ?  41  ILE A CG2   1 
ATOM   310   C  CD1   . ILE A 1 41  ? 108.527 134.583 96.112  1.00 46.20 ?  41  ILE A CD1   1 
ATOM   311   N  N     . ASN A 1 42  ? 104.097 135.516 93.332  1.00 51.13 ?  42  ASN A N     1 
ATOM   312   C  CA    . ASN A 1 42  ? 102.988 136.389 92.960  1.00 51.45 ?  42  ASN A CA    1 
ATOM   313   C  C     . ASN A 1 42  ? 101.766 136.158 93.839  1.00 55.41 ?  42  ASN A C     1 
ATOM   314   O  O     . ASN A 1 42  ? 101.029 137.106 94.134  1.00 56.50 ?  42  ASN A O     1 
ATOM   315   C  CB    . ASN A 1 42  ? 102.635 136.192 91.486  1.00 52.87 ?  42  ASN A CB    1 
ATOM   316   C  CG    . ASN A 1 42  ? 103.754 136.619 90.558  1.00 53.98 ?  42  ASN A CG    1 
ATOM   317   O  OD1   . ASN A 1 42  ? 104.699 137.287 90.974  1.00 57.56 ?  42  ASN A OD1   1 
ATOM   318   N  ND2   . ASN A 1 42  ? 103.652 136.234 89.292  1.00 54.07 ?  42  ASN A ND2   1 
ATOM   319   N  N     . GLN A 1 43  ? 101.530 134.914 94.261  1.00 57.91 ?  43  GLN A N     1 
ATOM   320   C  CA    . GLN A 1 43  ? 100.383 134.625 95.115  1.00 55.47 ?  43  GLN A CA    1 
ATOM   321   C  C     . GLN A 1 43  ? 100.526 135.279 96.485  1.00 55.81 ?  43  GLN A C     1 
ATOM   322   O  O     . GLN A 1 43  ? 99.544  135.783 97.043  1.00 56.47 ?  43  GLN A O     1 
ATOM   323   C  CB    . GLN A 1 43  ? 100.206 133.114 95.258  1.00 55.39 ?  43  GLN A CB    1 
ATOM   324   C  CG    . GLN A 1 43  ? 99.284  132.491 94.221  1.00 57.56 ?  43  GLN A CG    1 
ATOM   325   C  CD    . GLN A 1 43  ? 99.835  132.587 92.811  1.00 58.38 ?  43  GLN A CD    1 
ATOM   326   O  OE1   . GLN A 1 43  ? 101.032 132.789 92.612  1.00 57.94 ?  43  GLN A OE1   1 
ATOM   327   N  NE2   . GLN A 1 43  ? 98.959  132.444 91.824  1.00 56.72 ?  43  GLN A NE2   1 
ATOM   328   N  N     . ASN A 1 44  ? 101.736 135.281 97.042  1.00 54.90 ?  44  ASN A N     1 
ATOM   329   C  CA    . ASN A 1 44  ? 101.982 135.800 98.380  1.00 55.01 ?  44  ASN A CA    1 
ATOM   330   C  C     . ASN A 1 44  ? 102.549 137.215 98.379  1.00 54.27 ?  44  ASN A C     1 
ATOM   331   O  O     . ASN A 1 44  ? 103.039 137.672 99.415  1.00 54.47 ?  44  ASN A O     1 
ATOM   332   C  CB    . ASN A 1 44  ? 102.915 134.860 99.147  1.00 53.41 ?  44  ASN A CB    1 
ATOM   333   C  CG    . ASN A 1 44  ? 102.369 133.447 99.241  1.00 55.83 ?  44  ASN A CG    1 
ATOM   334   O  OD1   . ASN A 1 44  ? 101.945 133.002 100.306 1.00 56.75 ?  44  ASN A OD1   1 
ATOM   335   N  ND2   . ASN A 1 44  ? 102.381 132.734 98.121  1.00 56.44 ?  44  ASN A ND2   1 
ATOM   336   N  N     . THR A 1 45  ? 102.497 137.914 97.250  1.00 54.15 ?  45  THR A N     1 
ATOM   337   C  CA    . THR A 1 45  ? 102.959 139.294 97.164  1.00 55.09 ?  45  THR A CA    1 
ATOM   338   C  C     . THR A 1 45  ? 101.773 140.234 97.321  1.00 55.66 ?  45  THR A C     1 
ATOM   339   O  O     . THR A 1 45  ? 100.787 140.128 96.582  1.00 56.05 ?  45  THR A O     1 
ATOM   340   C  CB    . THR A 1 45  ? 103.669 139.557 95.833  1.00 55.01 ?  45  THR A CB    1 
ATOM   341   O  OG1   . THR A 1 45  ? 105.007 139.047 95.897  1.00 57.88 ?  45  THR A OG1   1 
ATOM   342   C  CG2   . THR A 1 45  ? 103.721 141.049 95.536  1.00 53.39 ?  45  THR A CG2   1 
ATOM   343   N  N     . VAL A 1 46  ? 101.868 141.149 98.284  1.00 55.46 ?  46  VAL A N     1 
ATOM   344   C  CA    . VAL A 1 46  ? 100.797 142.111 98.517  1.00 55.19 ?  46  VAL A CA    1 
ATOM   345   C  C     . VAL A 1 46  ? 100.821 143.151 97.405  1.00 55.73 ?  46  VAL A C     1 
ATOM   346   O  O     . VAL A 1 46  ? 101.853 143.778 97.145  1.00 58.54 ?  46  VAL A O     1 
ATOM   347   C  CB    . VAL A 1 46  ? 100.939 142.769 99.896  1.00 55.20 ?  46  VAL A CB    1 
ATOM   348   C  CG1   . VAL A 1 46  ? 99.910  143.872 100.064 1.00 54.96 ?  46  VAL A CG1   1 
ATOM   349   C  CG2   . VAL A 1 46  ? 100.793 141.735 100.992 1.00 54.62 ?  46  VAL A CG2   1 
ATOM   350   N  N     . PHE A 1 47  ? 99.683  143.340 96.748  1.00 59.11 ?  47  PHE A N     1 
ATOM   351   C  CA    . PHE A 1 47  ? 99.555  144.304 95.668  1.00 59.69 ?  47  PHE A CA    1 
ATOM   352   C  C     . PHE A 1 47  ? 98.631  145.439 96.083  1.00 61.94 ?  47  PHE A C     1 
ATOM   353   O  O     . PHE A 1 47  ? 97.669  145.242 96.831  1.00 63.68 ?  47  PHE A O     1 
ATOM   354   C  CB    . PHE A 1 47  ? 99.028  143.644 94.391  1.00 60.14 ?  47  PHE A CB    1 
ATOM   355   C  CG    . PHE A 1 47  ? 99.385  144.387 93.136  1.00 62.75 ?  47  PHE A CG    1 
ATOM   356   C  CD1   . PHE A 1 47  ? 100.654 144.288 92.595  1.00 61.43 ?  47  PHE A CD1   1 
ATOM   357   C  CD2   . PHE A 1 47  ? 98.452  145.190 92.502  1.00 62.25 ?  47  PHE A CD2   1 
ATOM   358   C  CE1   . PHE A 1 47  ? 100.988 144.973 91.442  1.00 61.54 ?  47  PHE A CE1   1 
ATOM   359   C  CE2   . PHE A 1 47  ? 98.779  145.879 91.348  1.00 61.58 ?  47  PHE A CE2   1 
ATOM   360   C  CZ    . PHE A 1 47  ? 100.048 145.769 90.818  1.00 61.77 ?  47  PHE A CZ    1 
ATOM   361   N  N     . PHE A 1 48  ? 98.936  146.632 95.585  1.00 57.51 ?  48  PHE A N     1 
ATOM   362   C  CA    . PHE A 1 48  ? 98.183  147.837 95.889  1.00 57.86 ?  48  PHE A CA    1 
ATOM   363   C  C     . PHE A 1 48  ? 97.676  148.462 94.596  1.00 58.93 ?  48  PHE A C     1 
ATOM   364   O  O     . PHE A 1 48  ? 98.216  148.223 93.513  1.00 61.11 ?  48  PHE A O     1 
ATOM   365   C  CB    . PHE A 1 48  ? 99.037  148.846 96.665  1.00 57.18 ?  48  PHE A CB    1 
ATOM   366   C  CG    . PHE A 1 48  ? 99.527  148.338 97.993  1.00 56.27 ?  48  PHE A CG    1 
ATOM   367   C  CD1   . PHE A 1 48  ? 100.675 147.568 98.077  1.00 56.87 ?  48  PHE A CD1   1 
ATOM   368   C  CD2   . PHE A 1 48  ? 98.847  148.643 99.159  1.00 58.06 ?  48  PHE A CD2   1 
ATOM   369   C  CE1   . PHE A 1 48  ? 101.130 147.107 99.297  1.00 57.84 ?  48  PHE A CE1   1 
ATOM   370   C  CE2   . PHE A 1 48  ? 99.296  148.182 100.382 1.00 58.40 ?  48  PHE A CE2   1 
ATOM   371   C  CZ    . PHE A 1 48  ? 100.439 147.413 100.450 1.00 57.22 ?  48  PHE A CZ    1 
ATOM   372   N  N     . HIS A 1 49  ? 96.618  149.266 94.724  1.00 63.64 ?  49  HIS A N     1 
ATOM   373   C  CA    . HIS A 1 49  ? 96.034  149.907 93.551  1.00 66.40 ?  49  HIS A CA    1 
ATOM   374   C  C     . HIS A 1 49  ? 97.019  150.857 92.882  1.00 67.18 ?  49  HIS A C     1 
ATOM   375   O  O     . HIS A 1 49  ? 97.006  151.002 91.654  1.00 67.16 ?  49  HIS A O     1 
ATOM   376   C  CB    . HIS A 1 49  ? 94.755  150.650 93.941  1.00 67.54 ?  49  HIS A CB    1 
ATOM   377   C  CG    . HIS A 1 49  ? 94.024  151.244 92.778  1.00 69.46 ?  49  HIS A CG    1 
ATOM   378   N  ND1   . HIS A 1 49  ? 93.644  150.503 91.680  1.00 68.49 ?  49  HIS A ND1   1 
ATOM   379   C  CD2   . HIS A 1 49  ? 93.599  152.508 92.543  1.00 67.80 ?  49  HIS A CD2   1 
ATOM   380   C  CE1   . HIS A 1 49  ? 93.019  151.284 90.818  1.00 68.74 ?  49  HIS A CE1   1 
ATOM   381   N  NE2   . HIS A 1 49  ? 92.978  152.507 91.317  1.00 69.21 ?  49  HIS A NE2   1 
ATOM   382   N  N     . ASN A 1 50  ? 97.874  151.508 93.666  1.00 64.74 ?  50  ASN A N     1 
ATOM   383   C  CA    . ASN A 1 50  ? 98.899  152.390 93.130  1.00 63.49 ?  50  ASN A CA    1 
ATOM   384   C  C     . ASN A 1 50  ? 100.049 152.462 94.124  1.00 62.85 ?  50  ASN A C     1 
ATOM   385   O  O     . ASN A 1 50  ? 99.932  152.031 95.274  1.00 61.77 ?  50  ASN A O     1 
ATOM   386   C  CB    . ASN A 1 50  ? 98.333  153.782 92.810  1.00 62.57 ?  50  ASN A CB    1 
ATOM   387   C  CG    . ASN A 1 50  ? 97.945  154.564 94.053  1.00 64.44 ?  50  ASN A CG    1 
ATOM   388   O  OD1   . ASN A 1 50  ? 97.803  154.004 95.139  1.00 64.51 ?  50  ASN A OD1   1 
ATOM   389   N  ND2   . ASN A 1 50  ? 97.772  155.870 93.894  1.00 63.77 ?  50  ASN A ND2   1 
ATOM   390   N  N     . LEU A 1 51  ? 101.176 153.009 93.661  1.00 57.68 ?  51  LEU A N     1 
ATOM   391   C  CA    . LEU A 1 51  ? 102.359 153.093 94.510  1.00 56.20 ?  51  LEU A CA    1 
ATOM   392   C  C     . LEU A 1 51  ? 102.138 154.018 95.699  1.00 57.94 ?  51  LEU A C     1 
ATOM   393   O  O     . LEU A 1 51  ? 102.767 153.836 96.747  1.00 59.15 ?  51  LEU A O     1 
ATOM   394   C  CB    . LEU A 1 51  ? 103.560 153.560 93.692  1.00 55.60 ?  51  LEU A CB    1 
ATOM   395   C  CG    . LEU A 1 51  ? 104.912 153.636 94.401  1.00 55.06 ?  51  LEU A CG    1 
ATOM   396   C  CD1   . LEU A 1 51  ? 105.376 152.254 94.830  1.00 54.14 ?  51  LEU A CD1   1 
ATOM   397   C  CD2   . LEU A 1 51  ? 105.939 154.297 93.503  1.00 54.35 ?  51  LEU A CD2   1 
ATOM   398   N  N     . LYS A 1 52  ? 101.264 155.017 95.556  1.00 57.99 ?  52  LYS A N     1 
ATOM   399   C  CA    . LYS A 1 52  ? 100.973 155.910 96.673  1.00 57.65 ?  52  LYS A CA    1 
ATOM   400   C  C     . LYS A 1 52  ? 100.371 155.137 97.841  1.00 58.88 ?  52  LYS A C     1 
ATOM   401   O  O     . LYS A 1 52  ? 100.765 155.328 98.997  1.00 59.30 ?  52  LYS A O     1 
ATOM   402   C  CB    . LYS A 1 52  ? 100.033 157.026 96.215  1.00 57.85 ?  52  LYS A CB    1 
ATOM   403   C  CG    . LYS A 1 52  ? 100.347 158.395 96.801  1.00 58.85 ?  52  LYS A CG    1 
ATOM   404   C  CD    . LYS A 1 52  ? 99.959  158.485 98.264  1.00 59.24 ?  52  LYS A CD    1 
ATOM   405   C  CE    . LYS A 1 52  ? 100.141 159.896 98.795  1.00 59.48 ?  52  LYS A CE    1 
ATOM   406   N  NZ    . LYS A 1 52  ? 100.326 159.912 100.272 1.00 59.50 1  52  LYS A NZ    1 
ATOM   407   N  N     . GLU A 1 53  ? 99.420  154.247 97.549  1.00 60.58 ?  53  GLU A N     1 
ATOM   408   C  CA    . GLU A 1 53  ? 98.819  153.430 98.598  1.00 60.45 ?  53  GLU A CA    1 
ATOM   409   C  C     . GLU A 1 53  ? 99.846  152.502 99.231  1.00 60.19 ?  53  GLU A C     1 
ATOM   410   O  O     . GLU A 1 53  ? 99.850  152.310 100.452 1.00 60.00 ?  53  GLU A O     1 
ATOM   411   C  CB    . GLU A 1 53  ? 97.650  152.626 98.030  1.00 61.07 ?  53  GLU A CB    1 
ATOM   412   C  CG    . GLU A 1 53  ? 96.840  151.875 99.074  1.00 62.36 ?  53  GLU A CG    1 
ATOM   413   C  CD    . GLU A 1 53  ? 95.862  150.896 98.457  1.00 63.76 ?  53  GLU A CD    1 
ATOM   414   O  OE1   . GLU A 1 53  ? 95.836  149.725 98.890  1.00 62.97 ?  53  GLU A OE1   1 
ATOM   415   O  OE2   . GLU A 1 53  ? 95.119  151.296 97.535  1.00 62.77 -1 53  GLU A OE2   1 
ATOM   416   N  N     . LYS A 1 54  ? 100.724 151.914 98.415  1.00 58.66 ?  54  LYS A N     1 
ATOM   417   C  CA    . LYS A 1 54  ? 101.755 151.027 98.945  1.00 54.61 ?  54  LYS A CA    1 
ATOM   418   C  C     . LYS A 1 54  ? 102.689 151.773 99.889  1.00 52.64 ?  54  LYS A C     1 
ATOM   419   O  O     . LYS A 1 54  ? 102.998 151.293 100.987 1.00 55.36 ?  54  LYS A O     1 
ATOM   420   C  CB    . LYS A 1 54  ? 102.545 150.403 97.796  1.00 54.10 ?  54  LYS A CB    1 
ATOM   421   C  CG    . LYS A 1 54  ? 103.801 149.674 98.236  1.00 57.14 ?  54  LYS A CG    1 
ATOM   422   C  CD    . LYS A 1 54  ? 104.283 148.714 97.167  1.00 55.57 ?  54  LYS A CD    1 
ATOM   423   C  CE    . LYS A 1 54  ? 105.505 147.945 97.627  1.00 55.37 ?  54  LYS A CE    1 
ATOM   424   N  NZ    . LYS A 1 54  ? 105.708 146.705 96.830  1.00 55.79 1  54  LYS A NZ    1 
ATOM   425   N  N     . LEU A 1 55  ? 103.145 152.956 99.475  1.00 53.92 ?  55  LEU A N     1 
ATOM   426   C  CA    . LEU A 1 55  ? 104.048 153.737 100.313 1.00 55.07 ?  55  LEU A CA    1 
ATOM   427   C  C     . LEU A 1 55  ? 103.356 154.197 101.588 1.00 57.40 ?  55  LEU A C     1 
ATOM   428   O  O     . LEU A 1 55  ? 103.960 154.179 102.665 1.00 58.63 ?  55  LEU A O     1 
ATOM   429   C  CB    . LEU A 1 55  ? 104.590 154.930 99.530  1.00 55.64 ?  55  LEU A CB    1 
ATOM   430   C  CG    . LEU A 1 55  ? 105.506 154.597 98.351  1.00 56.12 ?  55  LEU A CG    1 
ATOM   431   C  CD1   . LEU A 1 55  ? 105.812 155.848 97.548  1.00 56.83 ?  55  LEU A CD1   1 
ATOM   432   C  CD2   . LEU A 1 55  ? 106.787 153.929 98.824  1.00 53.50 ?  55  LEU A CD2   1 
ATOM   433   N  N     . ASP A 1 56  ? 102.087 154.606 101.488 1.00 60.10 ?  56  ASP A N     1 
ATOM   434   C  CA    . ASP A 1 56  ? 101.350 155.009 102.681 1.00 59.38 ?  56  ASP A CA    1 
ATOM   435   C  C     . ASP A 1 56  ? 101.189 153.844 103.648 1.00 57.92 ?  56  ASP A C     1 
ATOM   436   O  O     . ASP A 1 56  ? 101.363 154.007 104.860 1.00 57.64 ?  56  ASP A O     1 
ATOM   437   C  CB    . ASP A 1 56  ? 99.984  155.571 102.289 1.00 60.22 ?  56  ASP A CB    1 
ATOM   438   C  CG    . ASP A 1 56  ? 100.075 156.968 101.713 1.00 62.26 ?  56  ASP A CG    1 
ATOM   439   O  OD1   . ASP A 1 56  ? 99.061  157.453 101.168 1.00 62.19 ?  56  ASP A OD1   1 
ATOM   440   O  OD2   . ASP A 1 56  ? 101.159 157.581 101.805 1.00 61.30 -1 56  ASP A OD2   1 
ATOM   441   N  N     . TYR A 1 57  ? 100.861 152.657 103.131 1.00 52.63 ?  57  TYR A N     1 
ATOM   442   C  CA    . TYR A 1 57  ? 100.705 151.493 103.996 1.00 54.65 ?  57  TYR A CA    1 
ATOM   443   C  C     . TYR A 1 57  ? 102.023 151.111 104.654 1.00 56.13 ?  57  TYR A C     1 
ATOM   444   O  O     . TYR A 1 57  ? 102.050 150.759 105.839 1.00 57.38 ?  57  TYR A O     1 
ATOM   445   C  CB    . TYR A 1 57  ? 100.144 150.317 103.196 1.00 53.46 ?  57  TYR A CB    1 
ATOM   446   C  CG    . TYR A 1 57  ? 100.069 149.028 103.981 1.00 55.24 ?  57  TYR A CG    1 
ATOM   447   C  CD1   . TYR A 1 57  ? 99.004  148.773 104.834 1.00 54.93 ?  57  TYR A CD1   1 
ATOM   448   C  CD2   . TYR A 1 57  ? 101.064 148.064 103.867 1.00 55.44 ?  57  TYR A CD2   1 
ATOM   449   C  CE1   . TYR A 1 57  ? 98.934  147.595 105.554 1.00 55.25 ?  57  TYR A CE1   1 
ATOM   450   C  CE2   . TYR A 1 57  ? 101.001 146.887 104.583 1.00 55.86 ?  57  TYR A CE2   1 
ATOM   451   C  CZ    . TYR A 1 57  ? 99.934  146.656 105.424 1.00 55.58 ?  57  TYR A CZ    1 
ATOM   452   O  OH    . TYR A 1 57  ? 99.868  145.482 106.137 1.00 56.63 ?  57  TYR A OH    1 
ATOM   453   N  N     . LEU A 1 58  ? 103.124 151.166 103.903 1.00 51.42 ?  58  LEU A N     1 
ATOM   454   C  CA    . LEU A 1 58  ? 104.412 150.773 104.465 1.00 50.27 ?  58  LEU A CA    1 
ATOM   455   C  C     . LEU A 1 58  ? 104.904 151.786 105.493 1.00 51.95 ?  58  LEU A C     1 
ATOM   456   O  O     . LEU A 1 58  ? 105.487 151.406 106.514 1.00 52.72 ?  58  LEU A O     1 
ATOM   457   C  CB    . LEU A 1 58  ? 105.435 150.586 103.346 1.00 49.61 ?  58  LEU A CB    1 
ATOM   458   C  CG    . LEU A 1 58  ? 105.172 149.375 102.444 1.00 50.58 ?  58  LEU A CG    1 
ATOM   459   C  CD1   . LEU A 1 58  ? 105.995 149.446 101.171 1.00 51.28 ?  58  LEU A CD1   1 
ATOM   460   C  CD2   . LEU A 1 58  ? 105.445 148.079 103.188 1.00 51.20 ?  58  LEU A CD2   1 
ATOM   461   N  N     . VAL A 1 59  ? 104.676 153.077 105.247 1.00 53.73 ?  59  VAL A N     1 
ATOM   462   C  CA    . VAL A 1 59  ? 105.103 154.098 106.199 1.00 54.61 ?  59  VAL A CA    1 
ATOM   463   C  C     . VAL A 1 59  ? 104.244 154.053 107.458 1.00 57.60 ?  59  VAL A C     1 
ATOM   464   O  O     . VAL A 1 59  ? 104.757 154.104 108.582 1.00 56.54 ?  59  VAL A O     1 
ATOM   465   C  CB    . VAL A 1 59  ? 105.064 155.487 105.539 1.00 54.59 ?  59  VAL A CB    1 
ATOM   466   C  CG1   . VAL A 1 59  ? 105.046 156.576 106.594 1.00 53.14 ?  59  VAL A CG1   1 
ATOM   467   C  CG2   . VAL A 1 59  ? 106.254 155.662 104.611 1.00 54.08 ?  59  VAL A CG2   1 
ATOM   468   N  N     . GLU A 1 60  ? 102.923 153.948 107.288 1.00 60.48 ?  60  GLU A N     1 
ATOM   469   C  CA    . GLU A 1 60  ? 102.017 153.988 108.431 1.00 58.01 ?  60  GLU A CA    1 
ATOM   470   C  C     . GLU A 1 60  ? 102.195 152.772 109.331 1.00 57.85 ?  60  GLU A C     1 
ATOM   471   O  O     . GLU A 1 60  ? 102.130 152.888 110.560 1.00 58.08 ?  60  GLU A O     1 
ATOM   472   C  CB    . GLU A 1 60  ? 100.571 154.097 107.947 1.00 58.23 ?  60  GLU A CB    1 
ATOM   473   C  CG    . GLU A 1 60  ? 100.191 155.481 107.445 1.00 59.63 ?  60  GLU A CG    1 
ATOM   474   C  CD    . GLU A 1 60  ? 98.994  155.457 106.514 1.00 61.74 ?  60  GLU A CD    1 
ATOM   475   O  OE1   . GLU A 1 60  ? 98.352  154.391 106.394 1.00 59.38 ?  60  GLU A OE1   1 
ATOM   476   O  OE2   . GLU A 1 60  ? 98.696  156.503 105.899 1.00 61.31 -1 60  GLU A OE2   1 
ATOM   477   N  N     . ASN A 1 61  ? 102.420 151.598 108.742 1.00 53.71 ?  61  ASN A N     1 
ATOM   478   C  CA    . ASN A 1 61  ? 102.594 150.368 109.504 1.00 52.50 ?  61  ASN A CA    1 
ATOM   479   C  C     . ASN A 1 61  ? 104.019 150.180 110.010 1.00 54.36 ?  61  ASN A C     1 
ATOM   480   O  O     . ASN A 1 61  ? 104.395 149.053 110.360 1.00 54.46 ?  61  ASN A O     1 
ATOM   481   C  CB    . ASN A 1 61  ? 102.172 149.163 108.661 1.00 53.45 ?  61  ASN A CB    1 
ATOM   482   C  CG    . ASN A 1 61  ? 100.668 149.023 108.560 1.00 56.30 ?  61  ASN A CG    1 
ATOM   483   O  OD1   . ASN A 1 61  ? 99.951  150.008 108.390 1.00 54.48 ?  61  ASN A OD1   1 
ATOM   484   N  ND2   . ASN A 1 61  ? 100.180 147.792 108.664 1.00 55.68 ?  61  ASN A ND2   1 
ATOM   485   N  N     . GLN A 1 62  ? 104.810 151.254 110.051 1.00 53.25 ?  62  GLN A N     1 
ATOM   486   C  CA    . GLN A 1 62  ? 106.167 151.243 110.600 1.00 52.66 ?  62  GLN A CA    1 
ATOM   487   C  C     . GLN A 1 62  ? 107.083 150.271 109.860 1.00 52.40 ?  62  GLN A C     1 
ATOM   488   O  O     . GLN A 1 62  ? 107.983 149.676 110.457 1.00 53.31 ?  62  GLN A O     1 
ATOM   489   C  CB    . GLN A 1 62  ? 106.159 150.931 112.101 1.00 51.98 ?  62  GLN A CB    1 
ATOM   490   C  CG    . GLN A 1 62  ? 105.074 151.657 112.883 1.00 51.77 ?  62  GLN A CG    1 
ATOM   491   C  CD    . GLN A 1 62  ? 105.186 153.165 112.779 1.00 54.59 ?  62  GLN A CD    1 
ATOM   492   O  OE1   . GLN A 1 62  ? 106.103 153.770 113.333 1.00 54.15 ?  62  GLN A OE1   1 
ATOM   493   N  NE2   . GLN A 1 62  ? 104.251 153.779 112.066 1.00 54.94 ?  62  GLN A NE2   1 
ATOM   494   N  N     . TYR A 1 63  ? 106.861 150.097 108.558 1.00 50.12 ?  63  TYR A N     1 
ATOM   495   C  CA    . TYR A 1 63  ? 107.783 149.325 107.733 1.00 46.66 ?  63  TYR A CA    1 
ATOM   496   C  C     . TYR A 1 63  ? 108.929 150.190 107.221 1.00 48.34 ?  63  TYR A C     1 
ATOM   497   O  O     . TYR A 1 63  ? 110.091 149.779 107.272 1.00 49.61 ?  63  TYR A O     1 
ATOM   498   C  CB    . TYR A 1 63  ? 107.043 148.687 106.552 1.00 47.01 ?  63  TYR A CB    1 
ATOM   499   C  CG    . TYR A 1 63  ? 106.102 147.571 106.936 1.00 49.24 ?  63  TYR A CG    1 
ATOM   500   C  CD1   . TYR A 1 63  ? 106.573 146.422 107.554 1.00 48.39 ?  63  TYR A CD1   1 
ATOM   501   C  CD2   . TYR A 1 63  ? 104.744 147.662 106.669 1.00 50.04 ?  63  TYR A CD2   1 
ATOM   502   C  CE1   . TYR A 1 63  ? 105.716 145.399 107.901 1.00 48.45 ?  63  TYR A CE1   1 
ATOM   503   C  CE2   . TYR A 1 63  ? 103.880 146.644 107.011 1.00 50.57 ?  63  TYR A CE2   1 
ATOM   504   C  CZ    . TYR A 1 63  ? 104.370 145.516 107.629 1.00 50.75 ?  63  TYR A CZ    1 
ATOM   505   O  OH    . TYR A 1 63  ? 103.507 144.502 107.971 1.00 53.58 ?  63  TYR A OH    1 
ATOM   506   N  N     . TYR A 1 64  ? 108.613 151.383 106.728 1.00 47.25 ?  64  TYR A N     1 
ATOM   507   C  CA    . TYR A 1 64  ? 109.593 152.307 106.177 1.00 43.93 ?  64  TYR A CA    1 
ATOM   508   C  C     . TYR A 1 64  ? 109.824 153.473 107.128 1.00 46.86 ?  64  TYR A C     1 
ATOM   509   O  O     . TYR A 1 64  ? 109.135 153.636 108.137 1.00 49.91 ?  64  TYR A O     1 
ATOM   510   C  CB    . TYR A 1 64  ? 109.138 152.836 104.813 1.00 45.49 ?  64  TYR A CB    1 
ATOM   511   C  CG    . TYR A 1 64  ? 109.286 151.851 103.682 1.00 45.64 ?  64  TYR A CG    1 
ATOM   512   C  CD1   . TYR A 1 64  ? 109.923 150.631 103.874 1.00 42.74 ?  64  TYR A CD1   1 
ATOM   513   C  CD2   . TYR A 1 64  ? 108.795 152.143 102.421 1.00 47.43 ?  64  TYR A CD2   1 
ATOM   514   C  CE1   . TYR A 1 64  ? 110.058 149.730 102.840 1.00 40.32 ?  64  TYR A CE1   1 
ATOM   515   C  CE2   . TYR A 1 64  ? 108.926 151.252 101.382 1.00 46.63 ?  64  TYR A CE2   1 
ATOM   516   C  CZ    . TYR A 1 64  ? 109.557 150.047 101.596 1.00 44.90 ?  64  TYR A CZ    1 
ATOM   517   O  OH    . TYR A 1 64  ? 109.686 149.159 100.556 1.00 44.35 ?  64  TYR A OH    1 
ATOM   518   N  N     . GLU A 1 65  ? 110.815 154.289 106.783 1.00 52.27 ?  65  GLU A N     1 
ATOM   519   C  CA    . GLU A 1 65  ? 111.067 155.540 107.479 1.00 50.80 ?  65  GLU A CA    1 
ATOM   520   C  C     . GLU A 1 65  ? 110.458 156.697 106.700 1.00 53.51 ?  65  GLU A C     1 
ATOM   521   O  O     . GLU A 1 65  ? 110.491 156.717 105.466 1.00 54.80 ?  65  GLU A O     1 
ATOM   522   C  CB    . GLU A 1 65  ? 112.568 155.767 107.667 1.00 50.17 ?  65  GLU A CB    1 
ATOM   523   C  CG    . GLU A 1 65  ? 113.182 154.996 108.822 1.00 51.49 ?  65  GLU A CG    1 
ATOM   524   C  CD    . GLU A 1 65  ? 114.660 154.728 108.624 1.00 52.41 ?  65  GLU A CD    1 
ATOM   525   O  OE1   . GLU A 1 65  ? 115.297 155.454 107.832 1.00 53.30 ?  65  GLU A OE1   1 
ATOM   526   O  OE2   . GLU A 1 65  ? 115.190 153.800 109.268 1.00 52.68 -1 65  GLU A OE2   1 
ATOM   527   N  N     . GLU A 1 66  ? 109.892 157.659 107.431 1.00 54.86 ?  66  GLU A N     1 
ATOM   528   C  CA    . GLU A 1 66  ? 109.296 158.827 106.794 1.00 54.45 ?  66  GLU A CA    1 
ATOM   529   C  C     . GLU A 1 66  ? 110.347 159.808 106.292 1.00 56.09 ?  66  GLU A C     1 
ATOM   530   O  O     . GLU A 1 66  ? 110.109 160.510 105.304 1.00 56.40 ?  66  GLU A O     1 
ATOM   531   C  CB    . GLU A 1 66  ? 108.357 159.538 107.773 1.00 55.78 ?  66  GLU A CB    1 
ATOM   532   C  CG    . GLU A 1 66  ? 106.854 159.509 107.443 1.00 57.32 ?  66  GLU A CG    1 
ATOM   533   C  CD    . GLU A 1 66  ? 106.462 160.118 106.093 1.00 58.41 ?  66  GLU A CD    1 
ATOM   534   O  OE1   . GLU A 1 66  ? 107.327 160.366 105.228 1.00 58.37 ?  66  GLU A OE1   1 
ATOM   535   O  OE2   . GLU A 1 66  ? 105.251 160.354 105.899 1.00 55.35 -1 66  GLU A OE2   1 
ATOM   536   N  N     . GLU A 1 67  ? 111.503 159.871 106.956 1.00 54.76 ?  67  GLU A N     1 
ATOM   537   C  CA    . GLU A 1 67  ? 112.470 160.929 106.675 1.00 55.13 ?  67  GLU A CA    1 
ATOM   538   C  C     . GLU A 1 67  ? 113.027 160.821 105.260 1.00 55.53 ?  67  GLU A C     1 
ATOM   539   O  O     . GLU A 1 67  ? 113.080 161.816 104.526 1.00 55.42 ?  67  GLU A O     1 
ATOM   540   C  CB    . GLU A 1 67  ? 113.601 160.887 107.703 1.00 56.55 ?  67  GLU A CB    1 
ATOM   541   C  CG    . GLU A 1 67  ? 113.124 160.840 109.146 1.00 57.39 ?  67  GLU A CG    1 
ATOM   542   C  CD    . GLU A 1 67  ? 113.122 159.435 109.714 1.00 60.75 ?  67  GLU A CD    1 
ATOM   543   O  OE1   . GLU A 1 67  ? 114.209 158.936 110.074 1.00 59.46 ?  67  GLU A OE1   1 
ATOM   544   O  OE2   . GLU A 1 67  ? 112.033 158.829 109.802 1.00 57.42 -1 67  GLU A OE2   1 
ATOM   545   N  N     . PHE A 1 68  ? 113.447 159.620 104.854 1.00 48.39 ?  68  PHE A N     1 
ATOM   546   C  CA    . PHE A 1 68  ? 114.094 159.485 103.553 1.00 44.87 ?  68  PHE A CA    1 
ATOM   547   C  C     . PHE A 1 68  ? 113.091 159.586 102.410 1.00 44.22 ?  68  PHE A C     1 
ATOM   548   O  O     . PHE A 1 68  ? 113.448 160.040 101.317 1.00 47.66 ?  68  PHE A O     1 
ATOM   549   C  CB    . PHE A 1 68  ? 114.877 158.171 103.486 1.00 46.19 ?  68  PHE A CB    1 
ATOM   550   C  CG    . PHE A 1 68  ? 114.074 156.997 103.002 1.00 44.21 ?  68  PHE A CG    1 
ATOM   551   C  CD1   . PHE A 1 68  ? 113.231 156.314 103.861 1.00 44.39 ?  68  PHE A CD1   1 
ATOM   552   C  CD2   . PHE A 1 68  ? 114.188 156.557 101.693 1.00 39.83 ?  68  PHE A CD2   1 
ATOM   553   C  CE1   . PHE A 1 68  ? 112.500 155.229 103.418 1.00 42.62 ?  68  PHE A CE1   1 
ATOM   554   C  CE2   . PHE A 1 68  ? 113.461 155.473 101.246 1.00 43.07 ?  68  PHE A CE2   1 
ATOM   555   C  CZ    . PHE A 1 68  ? 112.618 154.806 102.110 1.00 45.52 ?  68  PHE A CZ    1 
ATOM   556   N  N     . LEU A 1 69  ? 111.843 159.174 102.635 1.00 46.25 ?  69  LEU A N     1 
ATOM   557   C  CA    . LEU A 1 69  ? 110.825 159.325 101.601 1.00 46.48 ?  69  LEU A CA    1 
ATOM   558   C  C     . LEU A 1 69  ? 110.321 160.758 101.499 1.00 48.21 ?  69  LEU A C     1 
ATOM   559   O  O     . LEU A 1 69  ? 109.885 161.180 100.422 1.00 45.42 ?  69  LEU A O     1 
ATOM   560   C  CB    . LEU A 1 69  ? 109.656 158.376 101.867 1.00 45.84 ?  69  LEU A CB    1 
ATOM   561   C  CG    . LEU A 1 69  ? 109.892 156.912 101.486 1.00 43.33 ?  69  LEU A CG    1 
ATOM   562   C  CD1   . LEU A 1 69  ? 108.700 156.051 101.869 1.00 43.30 ?  69  LEU A CD1   1 
ATOM   563   C  CD2   . LEU A 1 69  ? 110.199 156.781 100.003 1.00 42.58 ?  69  LEU A CD2   1 
ATOM   564   N  N     . SER A 1 70  ? 110.374 161.517 102.596 1.00 50.75 ?  70  SER A N     1 
ATOM   565   C  CA    . SER A 1 70  ? 109.893 162.893 102.579 1.00 49.04 ?  70  SER A CA    1 
ATOM   566   C  C     . SER A 1 70  ? 110.801 163.822 101.786 1.00 49.55 ?  70  SER A C     1 
ATOM   567   O  O     . SER A 1 70  ? 110.373 164.923 101.423 1.00 51.31 ?  70  SER A O     1 
ATOM   568   C  CB    . SER A 1 70  ? 109.742 163.412 104.010 1.00 50.83 ?  70  SER A CB    1 
ATOM   569   O  OG    . SER A 1 70  ? 111.006 163.681 104.589 1.00 52.71 ?  70  SER A OG    1 
ATOM   570   N  N     . LEU A 1 71  ? 112.040 163.410 101.508 1.00 44.06 ?  71  LEU A N     1 
ATOM   571   C  CA    . LEU A 1 71  ? 112.955 164.244 100.740 1.00 43.61 ?  71  LEU A CA    1 
ATOM   572   C  C     . LEU A 1 71  ? 112.582 164.328 99.266  1.00 44.26 ?  71  LEU A C     1 
ATOM   573   O  O     . LEU A 1 71  ? 113.110 165.194 98.561  1.00 44.16 ?  71  LEU A O     1 
ATOM   574   C  CB    . LEU A 1 71  ? 114.385 163.720 100.875 1.00 45.70 ?  71  LEU A CB    1 
ATOM   575   C  CG    . LEU A 1 71  ? 114.891 163.488 102.298 1.00 47.64 ?  71  LEU A CG    1 
ATOM   576   C  CD1   . LEU A 1 71  ? 116.002 162.452 102.306 1.00 47.24 ?  71  LEU A CD1   1 
ATOM   577   C  CD2   . LEU A 1 71  ? 115.367 164.794 102.911 1.00 45.83 ?  71  LEU A CD2   1 
ATOM   578   N  N     . TYR A 1 72  ? 111.697 163.460 98.788  1.00 44.00 ?  72  TYR A N     1 
ATOM   579   C  CA    . TYR A 1 72  ? 111.267 163.456 97.400  1.00 44.48 ?  72  TYR A CA    1 
ATOM   580   C  C     . TYR A 1 72  ? 109.776 163.740 97.318  1.00 46.44 ?  72  TYR A C     1 
ATOM   581   O  O     . TYR A 1 72  ? 109.008 163.389 98.219  1.00 47.83 ?  72  TYR A O     1 
ATOM   582   C  CB    . TYR A 1 72  ? 111.548 162.108 96.716  1.00 43.94 ?  72  TYR A CB    1 
ATOM   583   C  CG    . TYR A 1 72  ? 112.930 161.543 96.939  1.00 41.73 ?  72  TYR A CG    1 
ATOM   584   C  CD1   . TYR A 1 72  ? 113.238 160.847 98.101  1.00 42.19 ?  72  TYR A CD1   1 
ATOM   585   C  CD2   . TYR A 1 72  ? 113.920 161.681 95.977  1.00 40.29 ?  72  TYR A CD2   1 
ATOM   586   C  CE1   . TYR A 1 72  ? 114.496 160.324 98.306  1.00 41.19 ?  72  TYR A CE1   1 
ATOM   587   C  CE2   . TYR A 1 72  ? 115.181 161.157 96.172  1.00 40.28 ?  72  TYR A CE2   1 
ATOM   588   C  CZ    . TYR A 1 72  ? 115.462 160.481 97.339  1.00 40.85 ?  72  TYR A CZ    1 
ATOM   589   O  OH    . TYR A 1 72  ? 116.716 159.959 97.542  1.00 43.51 ?  72  TYR A OH    1 
ATOM   590   N  N     . SER A 1 73  ? 109.372 164.385 96.230  1.00 51.19 ?  73  SER A N     1 
ATOM   591   C  CA    . SER A 1 73  ? 107.962 164.414 95.886  1.00 50.58 ?  73  SER A CA    1 
ATOM   592   C  C     . SER A 1 73  ? 107.524 163.024 95.434  1.00 52.96 ?  73  SER A C     1 
ATOM   593   O  O     . SER A 1 73  ? 108.338 162.195 95.019  1.00 52.97 ?  73  SER A O     1 
ATOM   594   C  CB    . SER A 1 73  ? 107.693 165.445 94.791  1.00 50.80 ?  73  SER A CB    1 
ATOM   595   O  OG    . SER A 1 73  ? 108.078 164.951 93.520  1.00 50.85 ?  73  SER A OG    1 
ATOM   596   N  N     . PHE A 1 74  ? 106.219 162.764 95.532  1.00 55.14 ?  74  PHE A N     1 
ATOM   597   C  CA    . PHE A 1 74  ? 105.720 161.450 95.144  1.00 53.82 ?  74  PHE A CA    1 
ATOM   598   C  C     . PHE A 1 74  ? 105.964 161.169 93.667  1.00 55.08 ?  74  PHE A C     1 
ATOM   599   O  O     . PHE A 1 74  ? 106.141 160.010 93.278  1.00 56.91 ?  74  PHE A O     1 
ATOM   600   C  CB    . PHE A 1 74  ? 104.232 161.318 95.466  1.00 54.87 ?  74  PHE A CB    1 
ATOM   601   C  CG    . PHE A 1 74  ? 103.592 160.108 94.849  1.00 56.02 ?  74  PHE A CG    1 
ATOM   602   C  CD1   . PHE A 1 74  ? 103.885 158.842 95.327  1.00 54.35 ?  74  PHE A CD1   1 
ATOM   603   C  CD2   . PHE A 1 74  ? 102.711 160.231 93.788  1.00 56.03 ?  74  PHE A CD2   1 
ATOM   604   C  CE1   . PHE A 1 74  ? 103.310 157.723 94.763  1.00 56.64 ?  74  PHE A CE1   1 
ATOM   605   C  CE2   . PHE A 1 74  ? 102.130 159.113 93.220  1.00 56.94 ?  74  PHE A CE2   1 
ATOM   606   C  CZ    . PHE A 1 74  ? 102.431 157.858 93.709  1.00 57.05 ?  74  PHE A CZ    1 
ATOM   607   N  N     . GLU A 1 75  ? 105.976 162.211 92.830  1.00 54.57 ?  75  GLU A N     1 
ATOM   608   C  CA    . GLU A 1 75  ? 106.263 162.014 91.413  1.00 55.54 ?  75  GLU A CA    1 
ATOM   609   C  C     . GLU A 1 75  ? 107.677 161.482 91.208  1.00 57.99 ?  75  GLU A C     1 
ATOM   610   O  O     . GLU A 1 75  ? 107.900 160.589 90.384  1.00 58.35 ?  75  GLU A O     1 
ATOM   611   C  CB    . GLU A 1 75  ? 106.058 163.323 90.642  1.00 54.90 ?  75  GLU A CB    1 
ATOM   612   C  CG    . GLU A 1 75  ? 104.673 164.027 90.753  1.00 55.52 ?  75  GLU A CG    1 
ATOM   613   C  CD    . GLU A 1 75  ? 103.431 163.121 90.650  1.00 58.83 ?  75  GLU A CD    1 
ATOM   614   O  OE1   . GLU A 1 75  ? 103.529 161.881 90.622  1.00 59.31 ?  75  GLU A OE1   1 
ATOM   615   O  OE2   . GLU A 1 75  ? 102.312 163.682 90.601  1.00 57.49 -1 75  GLU A OE2   1 
ATOM   616   N  N     . ASP A 1 76  ? 108.643 162.011 91.961  1.00 52.85 ?  76  ASP A N     1 
ATOM   617   C  CA    . ASP A 1 76  ? 110.019 161.536 91.845  1.00 49.88 ?  76  ASP A CA    1 
ATOM   618   C  C     . ASP A 1 76  ? 110.156 160.091 92.317  1.00 49.23 ?  76  ASP A C     1 
ATOM   619   O  O     . ASP A 1 76  ? 110.863 159.294 91.692  1.00 53.95 ?  76  ASP A O     1 
ATOM   620   C  CB    . ASP A 1 76  ? 110.952 162.455 92.631  1.00 52.85 ?  76  ASP A CB    1 
ATOM   621   C  CG    . ASP A 1 76  ? 111.083 163.826 91.998  1.00 55.11 ?  76  ASP A CG    1 
ATOM   622   O  OD1   . ASP A 1 76  ? 110.381 164.091 91.000  1.00 54.60 ?  76  ASP A OD1   1 
ATOM   623   O  OD2   . ASP A 1 76  ? 111.895 164.635 92.492  1.00 53.49 -1 76  ASP A OD2   1 
ATOM   624   N  N     . ILE A 1 77  ? 109.488 159.736 93.419  1.00 44.02 ?  77  ILE A N     1 
ATOM   625   C  CA    . ILE A 1 77  ? 109.531 158.358 93.904  1.00 45.79 ?  77  ILE A CA    1 
ATOM   626   C  C     . ILE A 1 77  ? 108.898 157.415 92.889  1.00 44.53 ?  77  ILE A C     1 
ATOM   627   O  O     . ILE A 1 77  ? 109.409 156.318 92.628  1.00 47.23 ?  77  ILE A O     1 
ATOM   628   C  CB    . ILE A 1 77  ? 108.844 158.254 95.279  1.00 46.81 ?  77  ILE A CB    1 
ATOM   629   C  CG1   . ILE A 1 77  ? 109.570 159.129 96.299  1.00 46.87 ?  77  ILE A CG1   1 
ATOM   630   C  CG2   . ILE A 1 77  ? 108.808 156.811 95.752  1.00 44.75 ?  77  ILE A CG2   1 
ATOM   631   C  CD1   . ILE A 1 77  ? 108.844 159.265 97.614  1.00 45.19 ?  77  ILE A CD1   1 
ATOM   632   N  N     . LYS A 1 78  ? 107.768 157.824 92.307  1.00 48.26 ?  78  LYS A N     1 
ATOM   633   C  CA    . LYS A 1 78  ? 107.122 157.010 91.284  1.00 49.51 ?  78  LYS A CA    1 
ATOM   634   C  C     . LYS A 1 78  ? 108.015 156.856 90.061  1.00 49.50 ?  78  LYS A C     1 
ATOM   635   O  O     . LYS A 1 78  ? 108.070 155.779 89.459  1.00 51.38 ?  78  LYS A O     1 
ATOM   636   C  CB    . LYS A 1 78  ? 105.776 157.626 90.900  1.00 51.36 ?  78  LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 78  ? 104.954 156.788 89.937  1.00 50.07 ?  78  LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 78  ? 103.589 157.410 89.705  1.00 51.85 ?  78  LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 78  ? 102.904 156.796 88.500  1.00 53.23 ?  78  LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 78  ? 101.803 157.664 88.003  1.00 50.53 1  78  LYS A NZ    1 
ATOM   641   N  N     . GLU A 1 79  ? 108.721 157.921 89.676  1.00 50.11 ?  79  GLU A N     1 
ATOM   642   C  CA    . GLU A 1 79  ? 109.644 157.829 88.549  1.00 50.50 ?  79  GLU A CA    1 
ATOM   643   C  C     . GLU A 1 79  ? 110.796 156.879 88.851  1.00 48.79 ?  79  GLU A C     1 
ATOM   644   O  O     . GLU A 1 79  ? 111.229 156.122 87.975  1.00 48.81 ?  79  GLU A O     1 
ATOM   645   C  CB    . GLU A 1 79  ? 110.173 159.218 88.183  1.00 50.57 ?  79  GLU A CB    1 
ATOM   646   C  CG    . GLU A 1 79  ? 109.618 159.846 86.886  1.00 51.59 ?  79  GLU A CG    1 
ATOM   647   C  CD    . GLU A 1 79  ? 109.859 159.034 85.605  1.00 55.08 ?  79  GLU A CD    1 
ATOM   648   O  OE1   . GLU A 1 79  ? 109.836 159.655 84.521  1.00 55.04 ?  79  GLU A OE1   1 
ATOM   649   O  OE2   . GLU A 1 79  ? 110.075 157.806 85.651  1.00 54.19 -1 79  GLU A OE2   1 
ATOM   650   N  N     . VAL A 1 80  ? 111.308 156.906 90.081  1.00 44.57 ?  80  VAL A N     1 
ATOM   651   C  CA    . VAL A 1 80  ? 112.376 155.983 90.459  1.00 41.51 ?  80  VAL A CA    1 
ATOM   652   C  C     . VAL A 1 80  ? 111.881 154.539 90.414  1.00 45.35 ?  80  VAL A C     1 
ATOM   653   O  O     . VAL A 1 80  ? 112.570 153.644 89.904  1.00 46.84 ?  80  VAL A O     1 
ATOM   654   C  CB    . VAL A 1 80  ? 112.928 156.357 91.844  1.00 40.87 ?  80  VAL A CB    1 
ATOM   655   C  CG1   . VAL A 1 80  ? 113.861 155.278 92.357  1.00 41.66 ?  80  VAL A CG1   1 
ATOM   656   C  CG2   . VAL A 1 80  ? 113.649 157.691 91.776  1.00 40.91 ?  80  VAL A CG2   1 
ATOM   657   N  N     . PHE A 1 81  ? 110.679 154.290 90.939  1.00 41.17 ?  81  PHE A N     1 
ATOM   658   C  CA    . PHE A 1 81  ? 110.114 152.943 90.890  1.00 39.00 ?  81  PHE A CA    1 
ATOM   659   C  C     . PHE A 1 81  ? 109.876 152.495 89.453  1.00 43.72 ?  81  PHE A C     1 
ATOM   660   O  O     . PHE A 1 81  ? 110.101 151.327 89.110  1.00 47.44 ?  81  PHE A O     1 
ATOM   661   C  CB    . PHE A 1 81  ? 108.814 152.889 91.691  1.00 40.74 ?  81  PHE A CB    1 
ATOM   662   C  CG    . PHE A 1 81  ? 109.003 152.542 93.140  1.00 39.06 ?  81  PHE A CG    1 
ATOM   663   C  CD1   . PHE A 1 81  ? 109.356 153.517 94.060  1.00 40.39 ?  81  PHE A CD1   1 
ATOM   664   C  CD2   . PHE A 1 81  ? 108.829 151.244 93.585  1.00 38.70 ?  81  PHE A CD2   1 
ATOM   665   C  CE1   . PHE A 1 81  ? 109.529 153.202 95.393  1.00 41.25 ?  81  PHE A CE1   1 
ATOM   666   C  CE2   . PHE A 1 81  ? 109.000 150.924 94.918  1.00 39.22 ?  81  PHE A CE2   1 
ATOM   667   C  CZ    . PHE A 1 81  ? 109.351 151.905 95.823  1.00 39.43 ?  81  PHE A CZ    1 
ATOM   668   N  N     . LYS A 1 82  ? 109.412 153.408 88.597  1.00 45.50 ?  82  LYS A N     1 
ATOM   669   C  CA    . LYS A 1 82  ? 109.202 153.080 87.192  1.00 44.86 ?  82  LYS A CA    1 
ATOM   670   C  C     . LYS A 1 82  ? 110.521 152.766 86.499  1.00 44.10 ?  82  LYS A C     1 
ATOM   671   O  O     . LYS A 1 82  ? 110.583 151.867 85.657  1.00 46.58 ?  82  LYS A O     1 
ATOM   672   C  CB    . LYS A 1 82  ? 108.484 154.231 86.489  1.00 46.41 ?  82  LYS A CB    1 
ATOM   673   C  CG    . LYS A 1 82  ? 106.983 154.249 86.709  1.00 47.69 ?  82  LYS A CG    1 
ATOM   674   C  CD    . LYS A 1 82  ? 106.302 155.230 85.771  1.00 49.23 ?  82  LYS A CD    1 
ATOM   675   C  CE    . LYS A 1 82  ? 104.922 154.739 85.373  1.00 48.47 ?  82  LYS A CE    1 
ATOM   676   N  NZ    . LYS A 1 82  ? 104.861 153.252 85.324  1.00 48.61 1  82  LYS A NZ    1 
ATOM   677   N  N     . THR A 1 83  ? 111.580 153.504 86.830  1.00 41.81 ?  83  THR A N     1 
ATOM   678   C  CA    . THR A 1 83  ? 112.897 153.196 86.283  1.00 42.61 ?  83  THR A CA    1 
ATOM   679   C  C     . THR A 1 83  ? 113.365 151.819 86.733  1.00 44.80 ?  83  THR A C     1 
ATOM   680   O  O     . THR A 1 83  ? 113.967 151.072 85.952  1.00 47.02 ?  83  THR A O     1 
ATOM   681   C  CB    . THR A 1 83  ? 113.906 154.268 86.700  1.00 42.16 ?  83  THR A CB    1 
ATOM   682   O  OG1   . THR A 1 83  ? 113.417 155.560 86.317  1.00 47.88 ?  83  THR A OG1   1 
ATOM   683   C  CG2   . THR A 1 83  ? 115.248 154.029 86.030  1.00 43.17 ?  83  THR A CG2   1 
ATOM   684   N  N     . ALA A 1 84  ? 113.099 151.468 87.993  1.00 38.43 ?  84  ALA A N     1 
ATOM   685   C  CA    . ALA A 1 84  ? 113.458 150.138 88.477  1.00 35.86 ?  84  ALA A CA    1 
ATOM   686   C  C     . ALA A 1 84  ? 112.691 149.049 87.738  1.00 39.07 ?  84  ALA A C     1 
ATOM   687   O  O     . ALA A 1 84  ? 113.263 148.018 87.366  1.00 42.31 ?  84  ALA A O     1 
ATOM   688   C  CB    . ALA A 1 84  ? 113.211 150.040 89.979  1.00 36.56 ?  84  ALA A CB    1 
ATOM   689   N  N     . TYR A 1 85  ? 111.394 149.256 87.518  1.00 44.03 ?  85  TYR A N     1 
ATOM   690   C  CA    . TYR A 1 85  ? 110.565 148.243 86.876  1.00 39.83 ?  85  TYR A CA    1 
ATOM   691   C  C     . TYR A 1 85  ? 110.710 148.210 85.360  1.00 40.48 ?  85  TYR A C     1 
ATOM   692   O  O     . TYR A 1 85  ? 110.299 147.223 84.740  1.00 41.84 ?  85  TYR A O     1 
ATOM   693   C  CB    . TYR A 1 85  ? 109.095 148.459 87.242  1.00 41.64 ?  85  TYR A CB    1 
ATOM   694   C  CG    . TYR A 1 85  ? 108.700 147.867 88.575  1.00 41.09 ?  85  TYR A CG    1 
ATOM   695   C  CD1   . TYR A 1 85  ? 108.247 146.559 88.667  1.00 39.31 ?  85  TYR A CD1   1 
ATOM   696   C  CD2   . TYR A 1 85  ? 108.779 148.615 89.742  1.00 42.16 ?  85  TYR A CD2   1 
ATOM   697   C  CE1   . TYR A 1 85  ? 107.884 146.011 89.880  1.00 41.12 ?  85  TYR A CE1   1 
ATOM   698   C  CE2   . TYR A 1 85  ? 108.417 148.076 90.961  1.00 42.11 ?  85  TYR A CE2   1 
ATOM   699   C  CZ    . TYR A 1 85  ? 107.970 146.774 91.024  1.00 43.05 ?  85  TYR A CZ    1 
ATOM   700   O  OH    . TYR A 1 85  ? 107.609 146.232 92.233  1.00 43.05 ?  85  TYR A OH    1 
ATOM   701   N  N     . ALA A 1 86  ? 111.279 149.251 84.748  1.00 40.35 ?  86  ALA A N     1 
ATOM   702   C  CA    . ALA A 1 86  ? 111.443 149.267 83.301  1.00 40.94 ?  86  ALA A CA    1 
ATOM   703   C  C     . ALA A 1 86  ? 112.486 148.270 82.822  1.00 45.40 ?  86  ALA A C     1 
ATOM   704   O  O     . ALA A 1 86  ? 112.447 147.861 81.658  1.00 45.64 ?  86  ALA A O     1 
ATOM   705   C  CB    . ALA A 1 86  ? 111.815 150.673 82.829  1.00 39.65 ?  86  ALA A CB    1 
ATOM   706   N  N     . LYS A 1 87  ? 113.419 147.875 83.691  1.00 43.91 ?  87  LYS A N     1 
ATOM   707   C  CA    . LYS A 1 87  ? 114.411 146.879 83.308  1.00 41.44 ?  87  LYS A CA    1 
ATOM   708   C  C     . LYS A 1 87  ? 113.770 145.522 83.048  1.00 42.51 ?  87  LYS A C     1 
ATOM   709   O  O     . LYS A 1 87  ? 114.291 144.735 82.248  1.00 44.65 ?  87  LYS A O     1 
ATOM   710   C  CB    . LYS A 1 87  ? 115.486 146.773 84.392  1.00 41.57 ?  87  LYS A CB    1 
ATOM   711   C  CG    . LYS A 1 87  ? 116.443 145.603 84.231  1.00 43.60 ?  87  LYS A CG    1 
ATOM   712   C  CD    . LYS A 1 87  ? 117.853 146.074 83.935  1.00 40.15 ?  87  LYS A CD    1 
ATOM   713   C  CE    . LYS A 1 87  ? 118.800 144.899 83.758  1.00 40.86 ?  87  LYS A CE    1 
ATOM   714   N  NZ    . LYS A 1 87  ? 119.680 145.073 82.570  1.00 42.63 1  87  LYS A NZ    1 
ATOM   715   N  N     . LYS A 1 88  ? 112.629 145.249 83.684  1.00 43.17 ?  88  LYS A N     1 
ATOM   716   C  CA    . LYS A 1 88  ? 111.985 143.936 83.631  1.00 41.87 ?  88  LYS A CA    1 
ATOM   717   C  C     . LYS A 1 88  ? 112.957 142.851 84.086  1.00 40.24 ?  88  LYS A C     1 
ATOM   718   O  O     . LYS A 1 88  ? 113.113 141.808 83.446  1.00 43.96 ?  88  LYS A O     1 
ATOM   719   C  CB    . LYS A 1 88  ? 111.437 143.639 82.232  1.00 43.41 ?  88  LYS A CB    1 
ATOM   720   C  CG    . LYS A 1 88  ? 110.005 144.101 82.011  1.00 44.06 ?  88  LYS A CG    1 
ATOM   721   C  CD    . LYS A 1 88  ? 109.960 145.414 81.244  1.00 44.79 ?  88  LYS A CD    1 
ATOM   722   C  CE    . LYS A 1 88  ? 108.829 146.303 81.733  1.00 45.47 ?  88  LYS A CE    1 
ATOM   723   N  NZ    . LYS A 1 88  ? 108.873 147.656 81.108  1.00 43.81 1  88  LYS A NZ    1 
ATOM   724   N  N     . PHE A 1 89  ? 113.627 143.117 85.206  1.00 39.10 ?  89  PHE A N     1 
ATOM   725   C  CA    . PHE A 1 89  ? 114.636 142.202 85.717  1.00 33.63 ?  89  PHE A CA    1 
ATOM   726   C  C     . PHE A 1 89  ? 114.020 140.852 86.053  1.00 40.27 ?  89  PHE A C     1 
ATOM   727   O  O     . PHE A 1 89  ? 112.950 140.769 86.662  1.00 42.10 ?  89  PHE A O     1 
ATOM   728   C  CB    . PHE A 1 89  ? 115.309 142.792 86.958  1.00 34.46 ?  89  PHE A CB    1 
ATOM   729   C  CG    . PHE A 1 89  ? 116.266 141.852 87.631  1.00 34.23 ?  89  PHE A CG    1 
ATOM   730   C  CD1   . PHE A 1 89  ? 117.564 141.721 87.171  1.00 34.64 ?  89  PHE A CD1   1 
ATOM   731   C  CD2   . PHE A 1 89  ? 115.869 141.094 88.719  1.00 35.69 ?  89  PHE A CD2   1 
ATOM   732   C  CE1   . PHE A 1 89  ? 118.446 140.855 87.783  1.00 37.08 ?  89  PHE A CE1   1 
ATOM   733   C  CE2   . PHE A 1 89  ? 116.747 140.224 89.333  1.00 32.64 ?  89  PHE A CE2   1 
ATOM   734   C  CZ    . PHE A 1 89  ? 118.036 140.106 88.867  1.00 35.02 ?  89  PHE A CZ    1 
ATOM   735   N  N     . ARG A 1 90  ? 114.708 139.788 85.648  1.00 41.70 ?  90  ARG A N     1 
ATOM   736   C  CA    . ARG A 1 90  ? 114.296 138.425 85.943  1.00 40.07 ?  90  ARG A CA    1 
ATOM   737   C  C     . ARG A 1 90  ? 115.454 137.696 86.601  1.00 39.11 ?  90  ARG A C     1 
ATOM   738   O  O     . ARG A 1 90  ? 116.585 137.747 86.108  1.00 40.65 ?  90  ARG A O     1 
ATOM   739   C  CB    . ARG A 1 90  ? 113.858 137.687 84.672  1.00 39.99 ?  90  ARG A CB    1 
ATOM   740   C  CG    . ARG A 1 90  ? 112.770 138.393 83.884  1.00 41.43 ?  90  ARG A CG    1 
ATOM   741   C  CD    . ARG A 1 90  ? 111.437 138.346 84.610  1.00 42.63 ?  90  ARG A CD    1 
ATOM   742   N  NE    . ARG A 1 90  ? 110.464 139.256 84.019  1.00 44.13 ?  90  ARG A NE    1 
ATOM   743   C  CZ    . ARG A 1 90  ? 109.892 140.264 84.664  1.00 45.93 ?  90  ARG A CZ    1 
ATOM   744   N  NH1   . ARG A 1 90  ? 110.166 140.515 85.934  1.00 45.56 1  90  ARG A NH1   1 
ATOM   745   N  NH2   . ARG A 1 90  ? 109.024 141.037 84.020  1.00 43.70 ?  90  ARG A NH2   1 
ATOM   746   N  N     . PHE A 1 91  ? 115.176 137.033 87.714  1.00 36.18 ?  91  PHE A N     1 
ATOM   747   C  CA    . PHE A 1 91  ? 116.191 136.216 88.360  1.00 37.86 ?  91  PHE A CA    1 
ATOM   748   C  C     . PHE A 1 91  ? 116.540 135.039 87.457  1.00 43.33 ?  91  PHE A C     1 
ATOM   749   O  O     . PHE A 1 91  ? 115.645 134.296 87.042  1.00 44.55 ?  91  PHE A O     1 
ATOM   750   C  CB    . PHE A 1 91  ? 115.698 135.720 89.717  1.00 35.06 ?  91  PHE A CB    1 
ATOM   751   C  CG    . PHE A 1 91  ? 115.592 136.800 90.755  1.00 39.65 ?  91  PHE A CG    1 
ATOM   752   C  CD1   . PHE A 1 91  ? 116.705 137.194 91.480  1.00 41.67 ?  91  PHE A CD1   1 
ATOM   753   C  CD2   . PHE A 1 91  ? 114.383 137.423 91.005  1.00 38.52 ?  91  PHE A CD2   1 
ATOM   754   C  CE1   . PHE A 1 91  ? 116.611 138.187 92.436  1.00 39.51 ?  91  PHE A CE1   1 
ATOM   755   C  CE2   . PHE A 1 91  ? 114.283 138.416 91.960  1.00 38.91 ?  91  PHE A CE2   1 
ATOM   756   C  CZ    . PHE A 1 91  ? 115.399 138.798 92.675  1.00 38.48 ?  91  PHE A CZ    1 
ATOM   757   N  N     . PRO A 1 92  ? 117.820 134.835 87.127  1.00 43.39 ?  92  PRO A N     1 
ATOM   758   C  CA    . PRO A 1 92  ? 118.170 133.752 86.199  1.00 42.30 ?  92  PRO A CA    1 
ATOM   759   C  C     . PRO A 1 92  ? 118.147 132.372 86.828  1.00 43.13 ?  92  PRO A C     1 
ATOM   760   O  O     . PRO A 1 92  ? 118.052 131.380 86.093  1.00 44.76 ?  92  PRO A O     1 
ATOM   761   C  CB    . PRO A 1 92  ? 119.585 134.129 85.749  1.00 42.75 ?  92  PRO A CB    1 
ATOM   762   C  CG    . PRO A 1 92  ? 120.158 134.826 86.939  1.00 43.24 ?  92  PRO A CG    1 
ATOM   763   C  CD    . PRO A 1 92  ? 119.013 135.550 87.616  1.00 40.50 ?  92  PRO A CD    1 
ATOM   764   N  N     . SER A 1 93  ? 118.229 132.276 88.152  1.00 42.55 ?  93  SER A N     1 
ATOM   765   C  CA    . SER A 1 93  ? 118.251 131.001 88.848  1.00 41.96 ?  93  SER A CA    1 
ATOM   766   C  C     . SER A 1 93  ? 117.250 131.038 89.993  1.00 44.09 ?  93  SER A C     1 
ATOM   767   O  O     . SER A 1 93  ? 116.916 132.102 90.520  1.00 47.27 ?  93  SER A O     1 
ATOM   768   C  CB    . SER A 1 93  ? 119.653 130.674 89.378  1.00 43.27 ?  93  SER A CB    1 
ATOM   769   O  OG    . SER A 1 93  ? 119.862 131.251 90.654  1.00 45.05 ?  93  SER A OG    1 
ATOM   770   N  N     . PHE A 1 94  ? 116.761 129.852 90.363  1.00 43.75 ?  94  PHE A N     1 
ATOM   771   C  CA    . PHE A 1 94  ? 115.772 129.763 91.431  1.00 40.05 ?  94  PHE A CA    1 
ATOM   772   C  C     . PHE A 1 94  ? 116.348 130.237 92.759  1.00 42.38 ?  94  PHE A C     1 
ATOM   773   O  O     . PHE A 1 94  ? 115.658 130.903 93.540  1.00 44.10 ?  94  PHE A O     1 
ATOM   774   C  CB    . PHE A 1 94  ? 115.253 128.331 91.556  1.00 40.38 ?  94  PHE A CB    1 
ATOM   775   C  CG    . PHE A 1 94  ? 114.696 128.008 92.913  1.00 41.40 ?  94  PHE A CG    1 
ATOM   776   C  CD1   . PHE A 1 94  ? 113.482 128.533 93.319  1.00 41.31 ?  94  PHE A CD1   1 
ATOM   777   C  CD2   . PHE A 1 94  ? 115.389 127.184 93.783  1.00 44.07 ?  94  PHE A CD2   1 
ATOM   778   C  CE1   . PHE A 1 94  ? 112.972 128.244 94.568  1.00 41.35 ?  94  PHE A CE1   1 
ATOM   779   C  CE2   . PHE A 1 94  ? 114.881 126.891 95.033  1.00 45.35 ?  94  PHE A CE2   1 
ATOM   780   C  CZ    . PHE A 1 94  ? 113.670 127.421 95.425  1.00 41.55 ?  94  PHE A CZ    1 
ATOM   781   N  N     . MET A 1 95  ? 117.609 129.898 93.036  1.00 41.51 ?  95  MET A N     1 
ATOM   782   C  CA    . MET A 1 95  ? 118.195 130.241 94.326  1.00 39.30 ?  95  MET A CA    1 
ATOM   783   C  C     . MET A 1 95  ? 118.337 131.745 94.509  1.00 41.31 ?  95  MET A C     1 
ATOM   784   O  O     . MET A 1 95  ? 118.231 132.233 95.636  1.00 42.06 ?  95  MET A O     1 
ATOM   785   C  CB    . MET A 1 95  ? 119.551 129.553 94.490  1.00 40.51 ?  95  MET A CB    1 
ATOM   786   C  CG    . MET A 1 95  ? 120.175 129.677 95.881  1.00 43.89 ?  95  MET A CG    1 
ATOM   787   S  SD    . MET A 1 95  ? 119.308 128.926 97.283  1.00 54.57 ?  95  MET A SD    1 
ATOM   788   C  CE    . MET A 1 95  ? 118.318 127.648 96.512  1.00 45.92 ?  95  MET A CE    1 
ATOM   789   N  N     . SER A 1 96  ? 118.559 132.496 93.429  1.00 38.56 ?  96  SER A N     1 
ATOM   790   C  CA    . SER A 1 96  ? 118.641 133.949 93.548  1.00 34.14 ?  96  SER A CA    1 
ATOM   791   C  C     . SER A 1 96  ? 117.340 134.528 94.093  1.00 38.41 ?  96  SER A C     1 
ATOM   792   O  O     . SER A 1 96  ? 117.333 135.253 95.099  1.00 40.40 ?  96  SER A O     1 
ATOM   793   C  CB    . SER A 1 96  ? 118.970 134.560 92.187  1.00 32.01 ?  96  SER A CB    1 
ATOM   794   O  OG    . SER A 1 96  ? 119.978 133.820 91.527  1.00 36.90 ?  96  SER A OG    1 
ATOM   795   N  N     . ALA A 1 97  ? 116.221 134.192 93.449  1.00 38.59 ?  97  ALA A N     1 
ATOM   796   C  CA    . ALA A 1 97  ? 114.925 134.690 93.891  1.00 34.80 ?  97  ALA A CA    1 
ATOM   797   C  C     . ALA A 1 97  ? 114.564 134.145 95.264  1.00 35.83 ?  97  ALA A C     1 
ATOM   798   O  O     . ALA A 1 97  ? 114.001 134.867 96.094  1.00 41.87 ?  97  ALA A O     1 
ATOM   799   C  CB    . ALA A 1 97  ? 113.850 134.326 92.870  1.00 36.02 ?  97  ALA A CB    1 
ATOM   800   N  N     . PHE A 1 98  ? 114.871 132.872 95.519  1.00 37.46 ?  98  PHE A N     1 
ATOM   801   C  CA    . PHE A 1 98  ? 114.563 132.289 96.819  1.00 37.31 ?  98  PHE A CA    1 
ATOM   802   C  C     . PHE A 1 98  ? 115.315 133.004 97.932  1.00 37.48 ?  98  PHE A C     1 
ATOM   803   O  O     . PHE A 1 98  ? 114.730 133.347 98.964  1.00 46.19 ?  98  PHE A O     1 
ATOM   804   C  CB    . PHE A 1 98  ? 114.894 130.798 96.820  1.00 41.86 ?  98  PHE A CB    1 
ATOM   805   C  CG    . PHE A 1 98  ? 114.651 130.128 98.140  1.00 42.40 ?  98  PHE A CG    1 
ATOM   806   C  CD1   . PHE A 1 98  ? 113.371 129.756 98.515  1.00 42.56 ?  98  PHE A CD1   1 
ATOM   807   C  CD2   . PHE A 1 98  ? 115.698 129.876 99.010  1.00 41.56 ?  98  PHE A CD2   1 
ATOM   808   C  CE1   . PHE A 1 98  ? 113.142 129.142 99.729  1.00 43.31 ?  98  PHE A CE1   1 
ATOM   809   C  CE2   . PHE A 1 98  ? 115.474 129.263 100.226 1.00 42.84 ?  98  PHE A CE2   1 
ATOM   810   C  CZ    . PHE A 1 98  ? 114.194 128.896 100.587 1.00 44.36 ?  98  PHE A CZ    1 
ATOM   811   N  N     . LYS A 1 99  ? 116.610 133.254 97.733  1.00 38.45 ?  99  LYS A N     1 
ATOM   812   C  CA    . LYS A 1 99  ? 117.405 133.937 98.744  1.00 36.82 ?  99  LYS A CA    1 
ATOM   813   C  C     . LYS A 1 99  ? 116.926 135.366 98.948  1.00 38.12 ?  99  LYS A C     1 
ATOM   814   O  O     . LYS A 1 99  ? 116.862 135.843 100.087 1.00 43.28 ?  99  LYS A O     1 
ATOM   815   C  CB    . LYS A 1 99  ? 118.882 133.913 98.355  1.00 37.70 ?  99  LYS A CB    1 
ATOM   816   C  CG    . LYS A 1 99  ? 119.567 132.584 98.618  1.00 39.76 ?  99  LYS A CG    1 
ATOM   817   C  CD    . LYS A 1 99  ? 119.276 132.071 100.016 1.00 41.23 ?  99  LYS A CD    1 
ATOM   818   C  CE    . LYS A 1 99  ? 120.539 131.570 100.693 1.00 39.84 ?  99  LYS A CE    1 
ATOM   819   N  NZ    . LYS A 1 99  ? 120.353 131.432 102.163 1.00 43.67 1  99  LYS A NZ    1 
ATOM   820   N  N     . PHE A 1 100 ? 116.577 136.068 97.866  1.00 33.98 ?  100 PHE A N     1 
ATOM   821   C  CA    . PHE A 1 100 ? 116.088 137.431 98.042  1.00 32.03 ?  100 PHE A CA    1 
ATOM   822   C  C     . PHE A 1 100 ? 114.769 137.454 98.804  1.00 35.49 ?  100 PHE A C     1 
ATOM   823   O  O     . PHE A 1 100 ? 114.612 138.213 99.768  1.00 40.64 ?  100 PHE A O     1 
ATOM   824   C  CB    . PHE A 1 100 ? 115.921 138.142 96.702  1.00 29.77 ?  100 PHE A CB    1 
ATOM   825   C  CG    . PHE A 1 100 ? 115.255 139.478 96.834  1.00 36.38 ?  100 PHE A CG    1 
ATOM   826   C  CD1   . PHE A 1 100 ? 115.944 140.555 97.369  1.00 36.19 ?  100 PHE A CD1   1 
ATOM   827   C  CD2   . PHE A 1 100 ? 113.930 139.649 96.477  1.00 35.11 ?  100 PHE A CD2   1 
ATOM   828   C  CE1   . PHE A 1 100 ? 115.332 141.781 97.517  1.00 35.16 ?  100 PHE A CE1   1 
ATOM   829   C  CE2   . PHE A 1 100 ? 113.313 140.872 96.627  1.00 35.41 ?  100 PHE A CE2   1 
ATOM   830   C  CZ    . PHE A 1 100 ? 114.016 141.940 97.147  1.00 35.14 ?  100 PHE A CZ    1 
ATOM   831   N  N     . TYR A 1 101 ? 113.806 136.632 98.390  1.00 38.04 ?  101 TYR A N     1 
ATOM   832   C  CA    . TYR A 1 101 ? 112.479 136.677 98.986  1.00 37.60 ?  101 TYR A CA    1 
ATOM   833   C  C     . TYR A 1 101 ? 112.400 135.953 100.323 1.00 38.38 ?  101 TYR A C     1 
ATOM   834   O  O     . TYR A 1 101 ? 111.368 136.044 100.995 1.00 44.60 ?  101 TYR A O     1 
ATOM   835   C  CB    . TYR A 1 101 ? 111.449 136.103 98.011  1.00 36.13 ?  101 TYR A CB    1 
ATOM   836   C  CG    . TYR A 1 101 ? 111.125 137.047 96.876  1.00 32.59 ?  101 TYR A CG    1 
ATOM   837   C  CD1   . TYR A 1 101 ? 110.321 138.159 97.081  1.00 36.94 ?  101 TYR A CD1   1 
ATOM   838   C  CD2   . TYR A 1 101 ? 111.636 136.837 95.603  1.00 34.18 ?  101 TYR A CD2   1 
ATOM   839   C  CE1   . TYR A 1 101 ? 110.030 139.029 96.052  1.00 38.04 ?  101 TYR A CE1   1 
ATOM   840   C  CE2   . TYR A 1 101 ? 111.350 137.700 94.567  1.00 36.49 ?  101 TYR A CE2   1 
ATOM   841   C  CZ    . TYR A 1 101 ? 110.546 138.795 94.796  1.00 38.47 ?  101 TYR A CZ    1 
ATOM   842   O  OH    . TYR A 1 101 ? 110.259 139.659 93.765  1.00 41.93 ?  101 TYR A OH    1 
ATOM   843   N  N     . ASN A 1 102 ? 113.455 135.244 100.724 1.00 41.74 ?  102 ASN A N     1 
ATOM   844   C  CA    . ASN A 1 102 ? 113.514 134.645 102.048 1.00 45.03 ?  102 ASN A CA    1 
ATOM   845   C  C     . ASN A 1 102 ? 114.387 135.426 103.019 1.00 45.97 ?  102 ASN A C     1 
ATOM   846   O  O     . ASN A 1 102 ? 114.207 135.287 104.234 1.00 48.30 ?  102 ASN A O     1 
ATOM   847   C  CB    . ASN A 1 102 ? 114.038 133.206 101.954 1.00 42.99 ?  102 ASN A CB    1 
ATOM   848   C  CG    . ASN A 1 102 ? 112.926 132.177 101.980 1.00 46.78 ?  102 ASN A CG    1 
ATOM   849   O  OD1   . ASN A 1 102 ? 112.106 132.107 101.065 1.00 48.92 ?  102 ASN A OD1   1 
ATOM   850   N  ND2   . ASN A 1 102 ? 112.895 131.368 103.032 1.00 44.50 ?  102 ASN A ND2   1 
ATOM   851   N  N     . ASP A 1 103 ? 115.321 136.236 102.521 1.00 41.29 ?  103 ASP A N     1 
ATOM   852   C  CA    . ASP A 1 103 ? 116.253 136.954 103.378 1.00 41.46 ?  103 ASP A CA    1 
ATOM   853   C  C     . ASP A 1 103 ? 116.119 138.466 103.314 1.00 40.82 ?  103 ASP A C     1 
ATOM   854   O  O     . ASP A 1 103 ? 116.291 139.125 104.341 1.00 45.01 ?  103 ASP A O     1 
ATOM   855   C  CB    . ASP A 1 103 ? 117.697 136.580 103.022 1.00 44.47 ?  103 ASP A CB    1 
ATOM   856   C  CG    . ASP A 1 103 ? 118.033 135.148 103.377 1.00 48.51 ?  103 ASP A CG    1 
ATOM   857   O  OD1   . ASP A 1 103 ? 117.189 134.476 104.006 1.00 47.69 ?  103 ASP A OD1   1 
ATOM   858   O  OD2   . ASP A 1 103 ? 119.140 134.692 103.023 1.00 50.67 -1 103 ASP A OD2   1 
ATOM   859   N  N     . TYR A 1 104 ? 115.815 139.035 102.151 1.00 34.75 ?  104 TYR A N     1 
ATOM   860   C  CA    . TYR A 1 104 ? 115.877 140.478 101.967 1.00 38.48 ?  104 TYR A CA    1 
ATOM   861   C  C     . TYR A 1 104 ? 114.542 141.133 101.657 1.00 39.62 ?  104 TYR A C     1 
ATOM   862   O  O     . TYR A 1 104 ? 114.360 142.304 101.996 1.00 43.43 ?  104 TYR A O     1 
ATOM   863   C  CB    . TYR A 1 104 ? 116.873 140.827 100.848 1.00 38.18 ?  104 TYR A CB    1 
ATOM   864   C  CG    . TYR A 1 104 ? 118.270 140.321 101.118 1.00 40.21 ?  104 TYR A CG    1 
ATOM   865   C  CD1   . TYR A 1 104 ? 119.157 141.054 101.895 1.00 37.87 ?  104 TYR A CD1   1 
ATOM   866   C  CD2   . TYR A 1 104 ? 118.699 139.105 100.605 1.00 35.30 ?  104 TYR A CD2   1 
ATOM   867   C  CE1   . TYR A 1 104 ? 120.431 140.593 102.148 1.00 36.61 ?  104 TYR A CE1   1 
ATOM   868   C  CE2   . TYR A 1 104 ? 119.971 138.635 100.854 1.00 35.79 ?  104 TYR A CE2   1 
ATOM   869   C  CZ    . TYR A 1 104 ? 120.833 139.383 101.626 1.00 39.06 ?  104 TYR A CZ    1 
ATOM   870   O  OH    . TYR A 1 104 ? 122.103 138.917 101.875 1.00 40.64 ?  104 TYR A OH    1 
ATOM   871   N  N     . ALA A 1 105 ? 113.610 140.427 101.021 1.00 40.76 ?  105 ALA A N     1 
ATOM   872   C  CA    . ALA A 1 105 ? 112.320 141.025 100.706 1.00 38.14 ?  105 ALA A CA    1 
ATOM   873   C  C     . ALA A 1 105 ? 111.551 141.337 101.984 1.00 42.98 ?  105 ALA A C     1 
ATOM   874   O  O     . ALA A 1 105 ? 111.498 140.525 102.912 1.00 44.65 ?  105 ALA A O     1 
ATOM   875   C  CB    . ALA A 1 105 ? 111.503 140.094 99.813  1.00 37.75 ?  105 ALA A CB    1 
ATOM   876   N  N     . LEU A 1 106 ? 110.958 142.526 102.029 1.00 44.74 ?  106 LEU A N     1 
ATOM   877   C  CA    . LEU A 1 106 ? 110.198 142.937 103.201 1.00 40.94 ?  106 LEU A CA    1 
ATOM   878   C  C     . LEU A 1 106 ? 108.912 142.128 103.305 1.00 45.24 ?  106 LEU A C     1 
ATOM   879   O  O     . LEU A 1 106 ? 108.154 142.016 102.338 1.00 46.46 ?  106 LEU A O     1 
ATOM   880   C  CB    . LEU A 1 106 ? 109.882 144.429 103.134 1.00 44.43 ?  106 LEU A CB    1 
ATOM   881   C  CG    . LEU A 1 106 ? 109.120 145.015 104.324 1.00 43.46 ?  106 LEU A CG    1 
ATOM   882   C  CD1   . LEU A 1 106 ? 109.965 144.959 105.585 1.00 42.46 ?  106 LEU A CD1   1 
ATOM   883   C  CD2   . LEU A 1 106 ? 108.685 146.440 104.029 1.00 43.80 ?  106 LEU A CD2   1 
ATOM   884   N  N     . LYS A 1 107 ? 108.668 141.570 104.485 1.00 50.99 ?  107 LYS A N     1 
ATOM   885   C  CA    . LYS A 1 107 ? 107.482 140.774 104.753 1.00 50.88 ?  107 LYS A CA    1 
ATOM   886   C  C     . LYS A 1 107 ? 106.656 141.435 105.847 1.00 54.09 ?  107 LYS A C     1 
ATOM   887   O  O     . LYS A 1 107 ? 107.151 142.265 106.614 1.00 54.52 ?  107 LYS A O     1 
ATOM   888   C  CB    . LYS A 1 107 ? 107.851 139.343 105.164 1.00 51.63 ?  107 LYS A CB    1 
ATOM   889   C  CG    . LYS A 1 107 ? 109.012 138.750 104.384 1.00 50.31 ?  107 LYS A CG    1 
ATOM   890   C  CD    . LYS A 1 107 ? 108.527 137.764 103.336 1.00 50.99 ?  107 LYS A CD    1 
ATOM   891   C  CE    . LYS A 1 107 ? 109.273 136.444 103.434 1.00 54.46 ?  107 LYS A CE    1 
ATOM   892   N  NZ    . LYS A 1 107 ? 109.031 135.576 102.248 1.00 51.38 1  107 LYS A NZ    1 
ATOM   893   N  N     . THR A 1 108 ? 105.382 141.057 105.906 1.00 58.40 ?  108 THR A N     1 
ATOM   894   C  CA    . THR A 1 108 ? 104.493 141.569 106.935 1.00 57.21 ?  108 THR A CA    1 
ATOM   895   C  C     . THR A 1 108 ? 104.952 141.102 108.317 1.00 59.00 ?  108 THR A C     1 
ATOM   896   O  O     . THR A 1 108 ? 105.834 140.251 108.457 1.00 59.19 ?  108 THR A O     1 
ATOM   897   C  CB    . THR A 1 108 ? 103.057 141.120 106.673 1.00 57.88 ?  108 THR A CB    1 
ATOM   898   O  OG1   . THR A 1 108 ? 103.011 139.689 106.596 1.00 63.02 ?  108 THR A OG1   1 
ATOM   899   C  CG2   . THR A 1 108 ? 102.549 141.706 105.365 1.00 57.15 ?  108 THR A CG2   1 
ATOM   900   N  N     . ASN A 1 109 ? 104.339 141.680 109.353 1.00 60.83 ?  109 ASN A N     1 
ATOM   901   C  CA    . ASN A 1 109 ? 104.690 141.305 110.720 1.00 62.67 ?  109 ASN A CA    1 
ATOM   902   C  C     . ASN A 1 109 ? 104.409 139.834 110.990 1.00 64.04 ?  109 ASN A C     1 
ATOM   903   O  O     . ASN A 1 109 ? 105.084 139.214 111.819 1.00 64.25 ?  109 ASN A O     1 
ATOM   904   C  CB    . ASN A 1 109 ? 103.932 142.180 111.719 1.00 62.17 ?  109 ASN A CB    1 
ATOM   905   C  CG    . ASN A 1 109 ? 104.230 143.655 111.545 1.00 61.16 ?  109 ASN A CG    1 
ATOM   906   O  OD1   . ASN A 1 109 ? 104.410 144.135 110.427 1.00 60.42 ?  109 ASN A OD1   1 
ATOM   907   N  ND2   . ASN A 1 109 ? 104.285 144.383 112.653 1.00 61.63 ?  109 ASN A ND2   1 
ATOM   908   N  N     . ASP A 1 110 ? 103.424 139.261 110.305 1.00 65.81 ?  110 ASP A N     1 
ATOM   909   C  CA    . ASP A 1 110 ? 103.091 137.849 110.431 1.00 64.93 ?  110 ASP A CA    1 
ATOM   910   C  C     . ASP A 1 110 ? 103.933 136.954 109.531 1.00 67.09 ?  110 ASP A C     1 
ATOM   911   O  O     . ASP A 1 110 ? 103.788 135.728 109.593 1.00 67.07 ?  110 ASP A O     1 
ATOM   912   C  CB    . ASP A 1 110 ? 101.601 137.644 110.140 1.00 67.12 ?  110 ASP A CB    1 
ATOM   913   C  CG    . ASP A 1 110 ? 101.222 138.069 108.734 1.00 68.83 ?  110 ASP A CG    1 
ATOM   914   O  OD1   . ASP A 1 110 ? 102.099 138.591 108.014 1.00 68.34 ?  110 ASP A OD1   1 
ATOM   915   O  OD2   . ASP A 1 110 ? 100.049 137.891 108.349 1.00 66.30 -1 110 ASP A OD2   1 
ATOM   916   N  N     . LYS A 1 111 ? 104.805 137.537 108.702 1.00 66.76 ?  111 LYS A N     1 
ATOM   917   C  CA    . LYS A 1 111 ? 105.770 136.793 107.889 1.00 65.22 ?  111 LYS A CA    1 
ATOM   918   C  C     . LYS A 1 111 ? 105.098 135.786 106.957 1.00 67.30 ?  111 LYS A C     1 
ATOM   919   O  O     . LYS A 1 111 ? 105.638 134.707 106.705 1.00 68.62 ?  111 LYS A O     1 
ATOM   920   C  CB    . LYS A 1 111 ? 106.807 136.083 108.766 1.00 66.02 ?  111 LYS A CB    1 
ATOM   921   C  CG    . LYS A 1 111 ? 107.388 136.939 109.881 1.00 66.12 ?  111 LYS A CG    1 
ATOM   922   C  CD    . LYS A 1 111 ? 108.088 138.169 109.327 1.00 67.95 ?  111 LYS A CD    1 
ATOM   923   C  CE    . LYS A 1 111 ? 109.314 137.790 108.513 1.00 68.19 ?  111 LYS A CE    1 
ATOM   924   N  NZ    . LYS A 1 111 ? 110.044 138.991 108.017 1.00 65.71 1  111 LYS A NZ    1 
ATOM   925   N  N     . LYS A 1 112 ? 103.921 136.123 106.431 1.00 65.38 ?  112 LYS A N     1 
ATOM   926   C  CA    . LYS A 1 112 ? 103.237 135.260 105.479 1.00 66.35 ?  112 LYS A CA    1 
ATOM   927   C  C     . LYS A 1 112 ? 103.008 135.918 104.127 1.00 66.89 ?  112 LYS A C     1 
ATOM   928   O  O     . LYS A 1 112 ? 102.643 135.223 103.174 1.00 68.20 ?  112 LYS A O     1 
ATOM   929   C  CB    . LYS A 1 112 ? 101.885 134.797 106.042 1.00 67.22 ?  112 LYS A CB    1 
ATOM   930   C  CG    . LYS A 1 112 ? 100.777 135.825 105.909 1.00 67.45 ?  112 LYS A CG    1 
ATOM   931   C  CD    . LYS A 1 112 ? 99.409  135.200 106.127 1.00 67.24 ?  112 LYS A CD    1 
ATOM   932   C  CE    . LYS A 1 112 ? 99.365  134.406 107.422 1.00 69.30 ?  112 LYS A CE    1 
ATOM   933   N  NZ    . LYS A 1 112 ? 99.794  135.223 108.591 1.00 66.57 1  112 LYS A NZ    1 
ATOM   934   N  N     . LYS A 1 113 ? 103.210 137.228 104.019 1.00 59.81 ?  113 LYS A N     1 
ATOM   935   C  CA    . LYS A 1 113 ? 102.997 137.953 102.779 1.00 58.38 ?  113 LYS A CA    1 
ATOM   936   C  C     . LYS A 1 113 ? 104.252 138.737 102.428 1.00 59.83 ?  113 LYS A C     1 
ATOM   937   O  O     . LYS A 1 113 ? 105.049 139.088 103.302 1.00 60.10 ?  113 LYS A O     1 
ATOM   938   C  CB    . LYS A 1 113 ? 101.798 138.902 102.883 1.00 58.07 ?  113 LYS A CB    1 
ATOM   939   C  CG    . LYS A 1 113 ? 100.455 138.237 102.635 1.00 58.53 ?  113 LYS A CG    1 
ATOM   940   C  CD    . LYS A 1 113 ? 100.259 137.916 101.164 1.00 59.74 ?  113 LYS A CD    1 
ATOM   941   C  CE    . LYS A 1 113 ? 98.869  137.361 100.901 1.00 58.90 ?  113 LYS A CE    1 
ATOM   942   N  NZ    . LYS A 1 113 ? 98.678  136.991 99.472  1.00 60.00 1  113 LYS A NZ    1 
ATOM   943   N  N     . ILE A 1 114 ? 104.421 139.005 101.137 1.00 53.46 ?  114 ILE A N     1 
ATOM   944   C  CA    . ILE A 1 114 ? 105.591 139.700 100.616 1.00 51.44 ?  114 ILE A CA    1 
ATOM   945   C  C     . ILE A 1 114 ? 105.176 141.121 100.265 1.00 49.75 ?  114 ILE A C     1 
ATOM   946   O  O     . ILE A 1 114 ? 104.311 141.330 99.405  1.00 52.17 ?  114 ILE A O     1 
ATOM   947   C  CB    . ILE A 1 114 ? 106.183 138.977 99.398  1.00 51.20 ?  114 ILE A CB    1 
ATOM   948   C  CG1   . ILE A 1 114 ? 106.933 137.721 99.842  1.00 50.03 ?  114 ILE A CG1   1 
ATOM   949   C  CG2   . ILE A 1 114 ? 107.106 139.900 98.621  1.00 48.71 ?  114 ILE A CG2   1 
ATOM   950   C  CD1   . ILE A 1 114 ? 107.077 136.685 98.755  1.00 50.18 ?  114 ILE A CD1   1 
ATOM   951   N  N     . LEU A 1 115 ? 105.789 142.097 100.932 1.00 46.17 ?  115 LEU A N     1 
ATOM   952   C  CA    . LEU A 1 115 ? 105.498 143.499 100.671 1.00 46.36 ?  115 LEU A CA    1 
ATOM   953   C  C     . LEU A 1 115 ? 106.429 144.113 99.637  1.00 47.43 ?  115 LEU A C     1 
ATOM   954   O  O     . LEU A 1 115 ? 106.029 145.049 98.935  1.00 49.19 ?  115 LEU A O     1 
ATOM   955   C  CB    . LEU A 1 115 ? 105.584 144.306 101.968 1.00 47.39 ?  115 LEU A CB    1 
ATOM   956   C  CG    . LEU A 1 115 ? 104.534 143.987 103.032 1.00 48.80 ?  115 LEU A CG    1 
ATOM   957   C  CD1   . LEU A 1 115 ? 105.031 144.402 104.404 1.00 46.26 ?  115 LEU A CD1   1 
ATOM   958   C  CD2   . LEU A 1 115 ? 103.217 144.671 102.704 1.00 45.93 ?  115 LEU A CD2   1 
ATOM   959   N  N     . GLU A 1 116 ? 107.655 143.610 99.522  1.00 45.75 ?  116 GLU A N     1 
ATOM   960   C  CA    . GLU A 1 116 ? 108.665 144.189 98.649  1.00 42.66 ?  116 GLU A CA    1 
ATOM   961   C  C     . GLU A 1 116 ? 109.079 143.186 97.584  1.00 42.32 ?  116 GLU A C     1 
ATOM   962   O  O     . GLU A 1 116 ? 109.424 142.043 97.902  1.00 46.46 ?  116 GLU A O     1 
ATOM   963   C  CB    . GLU A 1 116 ? 109.896 144.625 99.447  1.00 43.84 ?  116 GLU A CB    1 
ATOM   964   C  CG    . GLU A 1 116 ? 109.997 146.119 99.669  1.00 44.60 ?  116 GLU A CG    1 
ATOM   965   C  CD    . GLU A 1 116 ? 111.229 146.503 100.463 1.00 43.95 ?  116 GLU A CD    1 
ATOM   966   O  OE1   . GLU A 1 116 ? 111.942 145.593 100.933 1.00 42.41 ?  116 GLU A OE1   1 
ATOM   967   O  OE2   . GLU A 1 116 ? 111.482 147.716 100.617 1.00 46.49 -1 116 GLU A OE2   1 
ATOM   968   N  N     . ARG A 1 117 ? 109.045 143.618 96.327  1.00 41.40 ?  117 ARG A N     1 
ATOM   969   C  CA    . ARG A 1 117 ? 109.684 142.882 95.252  1.00 42.35 ?  117 ARG A CA    1 
ATOM   970   C  C     . ARG A 1 117 ? 111.154 143.288 95.172  1.00 42.07 ?  117 ARG A C     1 
ATOM   971   O  O     . ARG A 1 117 ? 111.643 144.103 95.957  1.00 45.43 ?  117 ARG A O     1 
ATOM   972   C  CB    . ARG A 1 117 ? 108.963 143.135 93.930  1.00 42.96 ?  117 ARG A CB    1 
ATOM   973   C  CG    . ARG A 1 117 ? 107.498 142.729 93.929  1.00 43.74 ?  117 ARG A CG    1 
ATOM   974   C  CD    . ARG A 1 117 ? 107.016 142.403 92.527  1.00 46.22 ?  117 ARG A CD    1 
ATOM   975   N  NE    . ARG A 1 117 ? 107.141 140.984 92.220  1.00 47.84 ?  117 ARG A NE    1 
ATOM   976   C  CZ    . ARG A 1 117 ? 106.121 140.139 92.148  1.00 44.68 ?  117 ARG A CZ    1 
ATOM   977   N  NH1   . ARG A 1 117 ? 104.878 140.538 92.361  1.00 45.48 1  117 ARG A NH1   1 
ATOM   978   N  NH2   . ARG A 1 117 ? 106.355 138.864 91.853  1.00 45.28 ?  117 ARG A NH2   1 
ATOM   979   N  N     . TYR A 1 118 ? 111.877 142.707 94.213  1.00 35.82 ?  118 TYR A N     1 
ATOM   980   C  CA    . TYR A 1 118 ? 113.261 143.120 94.002  1.00 33.09 ?  118 TYR A CA    1 
ATOM   981   C  C     . TYR A 1 118 ? 113.334 144.574 93.556  1.00 35.83 ?  118 TYR A C     1 
ATOM   982   O  O     . TYR A 1 118 ? 114.170 145.343 94.046  1.00 36.46 ?  118 TYR A O     1 
ATOM   983   C  CB    . TYR A 1 118 ? 113.933 142.207 92.979  1.00 33.04 ?  118 TYR A CB    1 
ATOM   984   C  CG    . TYR A 1 118 ? 115.441 142.282 93.001  1.00 34.61 ?  118 TYR A CG    1 
ATOM   985   C  CD1   . TYR A 1 118 ? 116.140 142.220 94.197  1.00 34.13 ?  118 TYR A CD1   1 
ATOM   986   C  CD2   . TYR A 1 118 ? 116.164 142.419 91.827  1.00 32.57 ?  118 TYR A CD2   1 
ATOM   987   C  CE1   . TYR A 1 118 ? 117.516 142.287 94.222  1.00 32.21 ?  118 TYR A CE1   1 
ATOM   988   C  CE2   . TYR A 1 118 ? 117.542 142.486 91.841  1.00 28.54 ?  118 TYR A CE2   1 
ATOM   989   C  CZ    . TYR A 1 118 ? 118.213 142.420 93.041  1.00 33.42 ?  118 TYR A CZ    1 
ATOM   990   O  OH    . TYR A 1 118 ? 119.585 142.489 93.058  1.00 41.14 ?  118 TYR A OH    1 
ATOM   991   N  N     . GLU A 1 119 ? 112.451 144.970 92.638  1.00 38.05 ?  119 GLU A N     1 
ATOM   992   C  CA    . GLU A 1 119 ? 112.442 146.350 92.167  1.00 33.51 ?  119 GLU A CA    1 
ATOM   993   C  C     . GLU A 1 119 ? 112.053 147.313 93.282  1.00 34.98 ?  119 GLU A C     1 
ATOM   994   O  O     . GLU A 1 119 ? 112.605 148.413 93.372  1.00 41.26 ?  119 GLU A O     1 
ATOM   995   C  CB    . GLU A 1 119 ? 111.498 146.489 90.974  1.00 34.53 ?  119 GLU A CB    1 
ATOM   996   C  CG    . GLU A 1 119 ? 111.975 145.775 89.719  1.00 33.42 ?  119 GLU A CG    1 
ATOM   997   C  CD    . GLU A 1 119 ? 111.456 144.354 89.621  1.00 38.33 ?  119 GLU A CD    1 
ATOM   998   O  OE1   . GLU A 1 119 ? 111.214 143.729 90.675  1.00 40.04 ?  119 GLU A OE1   1 
ATOM   999   O  OE2   . GLU A 1 119 ? 111.292 143.860 88.487  1.00 39.80 -1 119 GLU A OE2   1 
ATOM   1000  N  N     . ASP A 1 120 ? 111.114 146.918 94.144  1.00 38.34 ?  120 ASP A N     1 
ATOM   1001  C  CA    . ASP A 1 120 ? 110.718 147.781 95.253  1.00 35.32 ?  120 ASP A CA    1 
ATOM   1002  C  C     . ASP A 1 120 ? 111.872 147.997 96.224  1.00 36.45 ?  120 ASP A C     1 
ATOM   1003  O  O     . ASP A 1 120 ? 112.144 149.131 96.639  1.00 37.89 ?  120 ASP A O     1 
ATOM   1004  C  CB    . ASP A 1 120 ? 109.515 147.186 95.984  1.00 39.27 ?  120 ASP A CB    1 
ATOM   1005  C  CG    . ASP A 1 120 ? 108.351 146.915 95.062  1.00 44.42 ?  120 ASP A CG    1 
ATOM   1006  O  OD1   . ASP A 1 120 ? 108.065 147.773 94.203  1.00 42.64 ?  120 ASP A OD1   1 
ATOM   1007  O  OD2   . ASP A 1 120 ? 107.719 145.847 95.197  1.00 48.92 -1 120 ASP A OD2   1 
ATOM   1008  N  N     . ARG A 1 121 ? 112.556 146.916 96.604  1.00 35.02 ?  121 ARG A N     1 
ATOM   1009  C  CA    . ARG A 1 121 ? 113.687 147.041 97.516  1.00 32.20 ?  121 ARG A CA    1 
ATOM   1010  C  C     . ARG A 1 121 ? 114.799 147.872 96.894  1.00 33.06 ?  121 ARG A C     1 
ATOM   1011  O  O     . ARG A 1 121 ? 115.400 148.721 97.562  1.00 38.75 ?  121 ARG A O     1 
ATOM   1012  C  CB    . ARG A 1 121 ? 114.202 145.656 97.905  1.00 30.88 ?  121 ARG A CB    1 
ATOM   1013  C  CG    . ARG A 1 121 ? 115.482 145.671 98.727  1.00 30.04 ?  121 ARG A CG    1 
ATOM   1014  C  CD    . ARG A 1 121 ? 115.191 145.410 100.195 1.00 29.75 ?  121 ARG A CD    1 
ATOM   1015  N  NE    . ARG A 1 121 ? 114.442 146.499 100.811 1.00 37.01 ?  121 ARG A NE    1 
ATOM   1016  C  CZ    . ARG A 1 121 ? 114.984 147.476 101.523 1.00 36.31 ?  121 ARG A CZ    1 
ATOM   1017  N  NH1   . ARG A 1 121 ? 116.286 147.526 101.751 1.00 34.61 1  121 ARG A NH1   1 
ATOM   1018  N  NH2   . ARG A 1 121 ? 114.199 148.426 102.026 1.00 33.20 ?  121 ARG A NH2   1 
ATOM   1019  N  N     . ILE A 1 122 ? 115.082 147.647 95.609  1.00 30.77 ?  122 ILE A N     1 
ATOM   1020  C  CA    . ILE A 1 122 ? 116.130 148.408 94.937  1.00 28.80 ?  122 ILE A CA    1 
ATOM   1021  C  C     . ILE A 1 122 ? 115.764 149.886 94.872  1.00 30.77 ?  122 ILE A C     1 
ATOM   1022  O  O     . ILE A 1 122 ? 116.609 150.755 95.106  1.00 34.25 ?  122 ILE A O     1 
ATOM   1023  C  CB    . ILE A 1 122 ? 116.399 147.816 93.541  1.00 30.30 ?  122 ILE A CB    1 
ATOM   1024  C  CG1   . ILE A 1 122 ? 117.272 146.567 93.665  1.00 26.40 ?  122 ILE A CG1   1 
ATOM   1025  C  CG2   . ILE A 1 122 ? 117.054 148.845 92.629  1.00 28.94 ?  122 ILE A CG2   1 
ATOM   1026  C  CD1   . ILE A 1 122 ? 117.703 145.990 92.348  1.00 28.85 ?  122 ILE A CD1   1 
ATOM   1027  N  N     . SER A 1 123 ? 114.501 150.195 94.565  1.00 31.33 ?  123 SER A N     1 
ATOM   1028  C  CA    . SER A 1 123 ? 114.064 151.587 94.517  1.00 32.29 ?  123 SER A CA    1 
ATOM   1029  C  C     . SER A 1 123 ? 114.174 152.247 95.884  1.00 30.43 ?  123 SER A C     1 
ATOM   1030  O  O     . SER A 1 123 ? 114.597 153.403 95.990  1.00 32.18 ?  123 SER A O     1 
ATOM   1031  C  CB    . SER A 1 123 ? 112.626 151.670 94.008  1.00 28.37 ?  123 SER A CB    1 
ATOM   1032  O  OG    . SER A 1 123 ? 112.422 150.806 92.910  1.00 32.84 ?  123 SER A OG    1 
ATOM   1033  N  N     . ILE A 1 124 ? 113.790 151.531 96.942  1.00 30.02 ?  124 ILE A N     1 
ATOM   1034  C  CA    . ILE A 1 124 ? 113.873 152.099 98.284  1.00 32.25 ?  124 ILE A CA    1 
ATOM   1035  C  C     . ILE A 1 124 ? 115.323 152.358 98.667  1.00 32.94 ?  124 ILE A C     1 
ATOM   1036  O  O     . ILE A 1 124 ? 115.654 153.416 99.221  1.00 38.22 ?  124 ILE A O     1 
ATOM   1037  C  CB    . ILE A 1 124 ? 113.165 151.178 99.292  1.00 36.78 ?  124 ILE A CB    1 
ATOM   1038  C  CG1   . ILE A 1 124 ? 111.650 151.286 99.122  1.00 37.74 ?  124 ILE A CG1   1 
ATOM   1039  C  CG2   . ILE A 1 124 ? 113.570 151.520 100.717 1.00 29.38 ?  124 ILE A CG2   1 
ATOM   1040  C  CD1   . ILE A 1 124 ? 111.141 152.712 99.072  1.00 32.41 ?  124 ILE A CD1   1 
ATOM   1041  N  N     . VAL A 1 125 ? 116.216 151.409 98.369  1.00 30.55 ?  125 VAL A N     1 
ATOM   1042  C  CA    . VAL A 1 125 ? 117.627 151.594 98.693  1.00 29.88 ?  125 VAL A CA    1 
ATOM   1043  C  C     . VAL A 1 125 ? 118.212 152.751 97.890  1.00 24.99 ?  125 VAL A C     1 
ATOM   1044  O  O     . VAL A 1 125 ? 119.022 153.532 98.400  1.00 32.24 ?  125 VAL A O     1 
ATOM   1045  C  CB    . VAL A 1 125 ? 118.407 150.285 98.466  1.00 30.99 ?  125 VAL A CB    1 
ATOM   1046  C  CG1   . VAL A 1 125 ? 119.885 150.496 98.716  1.00 30.65 ?  125 VAL A CG1   1 
ATOM   1047  C  CG2   . VAL A 1 125 ? 117.884 149.198 99.382  1.00 25.85 ?  125 VAL A CG2   1 
ATOM   1048  N  N     . ALA A 1 126 ? 117.805 152.886 96.625  1.00 23.57 ?  126 ALA A N     1 
ATOM   1049  C  CA    . ALA A 1 126 ? 118.281 153.994 95.801  1.00 22.17 ?  126 ALA A CA    1 
ATOM   1050  C  C     . ALA A 1 126 ? 117.799 155.337 96.336  1.00 29.36 ?  126 ALA A C     1 
ATOM   1051  O  O     . ALA A 1 126 ? 118.566 156.307 96.377  1.00 33.76 ?  126 ALA A O     1 
ATOM   1052  C  CB    . ALA A 1 126 ? 117.824 153.802 94.357  1.00 29.36 ?  126 ALA A CB    1 
ATOM   1053  N  N     . LEU A 1 127 ? 116.530 155.414 96.737  1.00 31.34 ?  127 LEU A N     1 
ATOM   1054  C  CA    . LEU A 1 127 ? 116.002 156.655 97.296  1.00 27.26 ?  127 LEU A CA    1 
ATOM   1055  C  C     . LEU A 1 127 ? 116.702 157.006 98.601  1.00 30.16 ?  127 LEU A C     1 
ATOM   1056  O  O     . LEU A 1 127 ? 116.957 158.183 98.881  1.00 36.11 ?  127 LEU A O     1 
ATOM   1057  C  CB    . LEU A 1 127 ? 114.493 156.536 97.506  1.00 32.59 ?  127 LEU A CB    1 
ATOM   1058  C  CG    . LEU A 1 127 ? 113.638 156.474 96.240  1.00 30.20 ?  127 LEU A CG    1 
ATOM   1059  C  CD1   . LEU A 1 127 ? 112.283 155.860 96.541  1.00 35.03 ?  127 LEU A CD1   1 
ATOM   1060  C  CD2   . LEU A 1 127 ? 113.478 157.854 95.625  1.00 31.61 ?  127 LEU A CD2   1 
ATOM   1061  N  N     . PHE A 1 128 ? 117.011 155.998 99.417  1.00 29.65 ?  128 PHE A N     1 
ATOM   1062  C  CA    . PHE A 1 128 ? 117.783 156.245 100.629 1.00 27.44 ?  128 PHE A CA    1 
ATOM   1063  C  C     . PHE A 1 128 ? 119.187 156.740 100.298 1.00 27.67 ?  128 PHE A C     1 
ATOM   1064  O  O     . PHE A 1 128 ? 119.701 157.653 100.954 1.00 39.06 ?  128 PHE A O     1 
ATOM   1065  C  CB    . PHE A 1 128 ? 117.846 154.975 101.475 1.00 27.29 ?  128 PHE A CB    1 
ATOM   1066  C  CG    . PHE A 1 128 ? 118.788 155.070 102.637 1.00 32.64 ?  128 PHE A CG    1 
ATOM   1067  C  CD1   . PHE A 1 128 ? 120.038 154.478 102.582 1.00 28.84 ?  128 PHE A CD1   1 
ATOM   1068  C  CD2   . PHE A 1 128 ? 118.420 155.746 103.787 1.00 32.00 ?  128 PHE A CD2   1 
ATOM   1069  C  CE1   . PHE A 1 128 ? 120.905 154.567 103.648 1.00 31.85 ?  128 PHE A CE1   1 
ATOM   1070  C  CE2   . PHE A 1 128 ? 119.284 155.834 104.859 1.00 35.22 ?  128 PHE A CE2   1 
ATOM   1071  C  CZ    . PHE A 1 128 ? 120.527 155.244 104.789 1.00 33.47 ?  128 PHE A CZ    1 
ATOM   1072  N  N     . PHE A 1 129 ? 119.821 156.143 99.285  1.00 24.44 ?  129 PHE A N     1 
ATOM   1073  C  CA    . PHE A 1 129 ? 121.171 156.539 98.900  1.00 22.14 ?  129 PHE A CA    1 
ATOM   1074  C  C     . PHE A 1 129 ? 121.214 157.980 98.410  1.00 28.86 ?  129 PHE A C     1 
ATOM   1075  O  O     . PHE A 1 129 ? 122.110 158.746 98.782  1.00 28.00 ?  129 PHE A O     1 
ATOM   1076  C  CB    . PHE A 1 129 ? 121.699 155.609 97.810  1.00 22.02 ?  129 PHE A CB    1 
ATOM   1077  C  CG    . PHE A 1 129 ? 122.204 154.292 98.315  1.00 23.96 ?  129 PHE A CG    1 
ATOM   1078  C  CD1   . PHE A 1 129 ? 122.447 154.092 99.660  1.00 24.20 ?  129 PHE A CD1   1 
ATOM   1079  C  CD2   . PHE A 1 129 ? 122.447 153.255 97.432  1.00 22.46 ?  129 PHE A CD2   1 
ATOM   1080  C  CE1   . PHE A 1 129 ? 122.914 152.877 100.114 1.00 24.48 ?  129 PHE A CE1   1 
ATOM   1081  C  CE2   . PHE A 1 129 ? 122.917 152.041 97.882  1.00 24.48 ?  129 PHE A CE2   1 
ATOM   1082  C  CZ    . PHE A 1 129 ? 123.152 151.851 99.225  1.00 26.83 ?  129 PHE A CZ    1 
ATOM   1083  N  N     . ALA A 1 130 ? 120.255 158.365 97.565  1.00 30.83 ?  130 ALA A N     1 
ATOM   1084  C  CA    . ALA A 1 130 ? 120.334 159.658 96.894  1.00 31.96 ?  130 ALA A CA    1 
ATOM   1085  C  C     . ALA A 1 130 ? 120.106 160.820 97.852  1.00 40.33 ?  130 ALA A C     1 
ATOM   1086  O  O     . ALA A 1 130 ? 120.598 161.927 97.603  1.00 42.45 ?  130 ALA A O     1 
ATOM   1087  C  CB    . ALA A 1 130 ? 119.331 159.713 95.748  1.00 32.00 ?  130 ALA A CB    1 
ATOM   1088  N  N     . ASN A 1 131 ? 119.362 160.593 98.936  1.00 40.41 ?  131 ASN A N     1 
ATOM   1089  C  CA    . ASN A 1 131 ? 119.132 161.606 99.969  1.00 38.34 ?  131 ASN A CA    1 
ATOM   1090  C  C     . ASN A 1 131 ? 118.470 162.860 99.396  1.00 41.21 ?  131 ASN A C     1 
ATOM   1091  O  O     . ASN A 1 131 ? 118.802 163.985 99.772  1.00 46.33 ?  131 ASN A O     1 
ATOM   1092  C  CB    . ASN A 1 131 ? 120.435 161.962 100.689 1.00 34.85 ?  131 ASN A CB    1 
ATOM   1093  C  CG    . ASN A 1 131 ? 120.209 162.402 102.120 1.00 43.68 ?  131 ASN A CG    1 
ATOM   1094  O  OD1   . ASN A 1 131 ? 119.239 161.998 102.760 1.00 43.08 ?  131 ASN A OD1   1 
ATOM   1095  N  ND2   . ASN A 1 131 ? 121.109 163.236 102.631 1.00 44.19 ?  131 ASN A ND2   1 
ATOM   1096  N  N     . GLY A 1 132 ? 117.525 162.666 98.479  1.00 39.55 ?  132 GLY A N     1 
ATOM   1097  C  CA    . GLY A 1 132 ? 116.725 163.753 97.948  1.00 39.30 ?  132 GLY A CA    1 
ATOM   1098  C  C     . GLY A 1 132 ? 116.940 164.069 96.484  1.00 43.26 ?  132 GLY A C     1 
ATOM   1099  O  O     . GLY A 1 132 ? 116.205 164.902 95.939  1.00 45.37 ?  132 GLY A O     1 
ATOM   1100  N  N     . ASP A 1 133 ? 117.912 163.442 95.826  1.00 43.29 ?  133 ASP A N     1 
ATOM   1101  C  CA    . ASP A 1 133 ? 118.206 163.702 94.420  1.00 41.14 ?  133 ASP A CA    1 
ATOM   1102  C  C     . ASP A 1 133 ? 117.530 162.632 93.570  1.00 42.99 ?  133 ASP A C     1 
ATOM   1103  O  O     . ASP A 1 133 ? 117.932 161.465 93.596  1.00 47.06 ?  133 ASP A O     1 
ATOM   1104  C  CB    . ASP A 1 133 ? 119.713 163.727 94.179  1.00 43.53 ?  133 ASP A CB    1 
ATOM   1105  C  CG    . ASP A 1 133 ? 120.089 164.443 92.897  1.00 46.21 ?  133 ASP A CG    1 
ATOM   1106  O  OD1   . ASP A 1 133 ? 119.183 164.742 92.091  1.00 48.02 ?  133 ASP A OD1   1 
ATOM   1107  O  OD2   . ASP A 1 133 ? 121.293 164.703 92.693  1.00 46.08 -1 133 ASP A OD2   1 
ATOM   1108  N  N     . THR A 1 134 ? 116.505 163.031 92.812  1.00 45.97 ?  134 THR A N     1 
ATOM   1109  C  CA    . THR A 1 134 ? 115.769 162.065 92.003  1.00 41.92 ?  134 THR A CA    1 
ATOM   1110  C  C     . THR A 1 134 ? 116.639 161.478 90.894  1.00 43.76 ?  134 THR A C     1 
ATOM   1111  O  O     . THR A 1 134 ? 116.561 160.279 90.609  1.00 44.74 ?  134 THR A O     1 
ATOM   1112  C  CB    . THR A 1 134 ? 114.509 162.712 91.421  1.00 45.87 ?  134 THR A CB    1 
ATOM   1113  O  OG1   . THR A 1 134 ? 113.906 161.825 90.471  1.00 48.16 ?  134 THR A OG1   1 
ATOM   1114  C  CG2   . THR A 1 134 ? 114.834 164.042 90.750  1.00 46.73 ?  134 THR A CG2   1 
ATOM   1115  N  N     . GLU A 1 135 ? 117.472 162.306 90.257  1.00 42.46 ?  135 GLU A N     1 
ATOM   1116  C  CA    . GLU A 1 135 ? 118.359 161.794 89.215  1.00 43.05 ?  135 GLU A CA    1 
ATOM   1117  C  C     . GLU A 1 135 ? 119.402 160.847 89.793  1.00 43.92 ?  135 GLU A C     1 
ATOM   1118  O  O     . GLU A 1 135 ? 119.701 159.804 89.199  1.00 43.52 ?  135 GLU A O     1 
ATOM   1119  C  CB    . GLU A 1 135 ? 119.030 162.953 88.480  1.00 43.57 ?  135 GLU A CB    1 
ATOM   1120  C  CG    . GLU A 1 135 ? 118.129 163.658 87.479  1.00 44.06 ?  135 GLU A CG    1 
ATOM   1121  C  CD    . GLU A 1 135 ? 117.046 162.751 86.927  1.00 47.86 ?  135 GLU A CD    1 
ATOM   1122  O  OE1   . GLU A 1 135 ? 117.340 161.972 85.997  1.00 47.89 ?  135 GLU A OE1   1 
ATOM   1123  O  OE2   . GLU A 1 135 ? 115.899 162.822 87.417  1.00 48.27 -1 135 GLU A OE2   1 
ATOM   1124  N  N     . LYS A 1 136 ? 119.964 161.190 90.954  1.00 35.81 ?  136 LYS A N     1 
ATOM   1125  C  CA    . LYS A 1 136 ? 120.897 160.288 91.619  1.00 32.22 ?  136 LYS A CA    1 
ATOM   1126  C  C     . LYS A 1 136 ? 120.206 158.994 92.030  1.00 33.99 ?  136 LYS A C     1 
ATOM   1127  O  O     . LYS A 1 136 ? 120.797 157.910 91.947  1.00 39.30 ?  136 LYS A O     1 
ATOM   1128  C  CB    . LYS A 1 136 ? 121.516 160.983 92.831  1.00 38.68 ?  136 LYS A CB    1 
ATOM   1129  C  CG    . LYS A 1 136 ? 122.673 160.237 93.464  1.00 37.05 ?  136 LYS A CG    1 
ATOM   1130  C  CD    . LYS A 1 136 ? 123.987 160.563 92.779  1.00 36.18 ?  136 LYS A CD    1 
ATOM   1131  C  CE    . LYS A 1 136 ? 125.167 160.123 93.627  1.00 38.80 ?  136 LYS A CE    1 
ATOM   1132  N  NZ    . LYS A 1 136 ? 126.459 160.620 93.083  1.00 39.04 1  136 LYS A NZ    1 
ATOM   1133  N  N     . ALA A 1 137 ? 118.952 159.087 92.478  1.00 33.83 ?  137 ALA A N     1 
ATOM   1134  C  CA    . ALA A 1 137 ? 118.196 157.888 92.824  1.00 30.50 ?  137 ALA A CA    1 
ATOM   1135  C  C     . ALA A 1 137 ? 117.980 157.003 91.603  1.00 31.42 ?  137 ALA A C     1 
ATOM   1136  O  O     . ALA A 1 137 ? 118.082 155.776 91.693  1.00 33.06 ?  137 ALA A O     1 
ATOM   1137  C  CB    . ALA A 1 137 ? 116.858 158.271 93.453  1.00 29.01 ?  137 ALA A CB    1 
ATOM   1138  N  N     . LYS A 1 138 ? 117.677 157.608 90.453  1.00 35.80 ?  138 LYS A N     1 
ATOM   1139  C  CA    . LYS A 1 138 ? 117.516 156.825 89.232  1.00 34.99 ?  138 LYS A CA    1 
ATOM   1140  C  C     . LYS A 1 138 ? 118.836 156.199 88.798  1.00 31.55 ?  138 LYS A C     1 
ATOM   1141  O  O     . LYS A 1 138 ? 118.858 155.074 88.289  1.00 33.93 ?  138 LYS A O     1 
ATOM   1142  C  CB    . LYS A 1 138 ? 116.940 157.698 88.117  1.00 39.13 ?  138 LYS A CB    1 
ATOM   1143  C  CG    . LYS A 1 138 ? 115.471 158.040 88.300  1.00 39.27 ?  138 LYS A CG    1 
ATOM   1144  C  CD    . LYS A 1 138 ? 115.130 159.370 87.653  1.00 37.78 ?  138 LYS A CD    1 
ATOM   1145  C  CE    . LYS A 1 138 ? 114.767 159.192 86.188  1.00 37.18 ?  138 LYS A CE    1 
ATOM   1146  N  NZ    . LYS A 1 138 ? 114.729 160.492 85.466  1.00 39.98 1  138 LYS A NZ    1 
ATOM   1147  N  N     . GLU A 1 139 ? 119.948 156.914 88.992  1.00 36.22 ?  139 GLU A N     1 
ATOM   1148  C  CA    . GLU A 1 139 ? 121.256 156.333 88.702  1.00 32.63 ?  139 GLU A CA    1 
ATOM   1149  C  C     . GLU A 1 139 ? 121.532 155.129 89.593  1.00 32.19 ?  139 GLU A C     1 
ATOM   1150  O  O     . GLU A 1 139 ? 122.032 154.100 89.123  1.00 40.53 ?  139 GLU A O     1 
ATOM   1151  C  CB    . GLU A 1 139 ? 122.352 157.383 88.873  1.00 33.71 ?  139 GLU A CB    1 
ATOM   1152  C  CG    . GLU A 1 139 ? 122.298 158.516 87.867  1.00 36.98 ?  139 GLU A CG    1 
ATOM   1153  C  CD    . GLU A 1 139 ? 123.408 159.526 88.073  1.00 45.18 ?  139 GLU A CD    1 
ATOM   1154  O  OE1   . GLU A 1 139 ? 124.550 159.106 88.352  1.00 43.35 ?  139 GLU A OE1   1 
ATOM   1155  O  OE2   . GLU A 1 139 ? 123.139 160.740 87.956  1.00 41.43 -1 139 GLU A OE2   1 
ATOM   1156  N  N     . TYR A 1 140 ? 121.208 155.235 90.883  1.00 23.52 ?  140 TYR A N     1 
ATOM   1157  C  CA    . TYR A 1 140 ? 121.380 154.103 91.788  1.00 27.69 ?  140 TYR A CA    1 
ATOM   1158  C  C     . TYR A 1 140 ? 120.477 152.941 91.396  1.00 28.10 ?  140 TYR A C     1 
ATOM   1159  O  O     . TYR A 1 140 ? 120.876 151.773 91.486  1.00 33.30 ?  140 TYR A O     1 
ATOM   1160  C  CB    . TYR A 1 140 ? 121.097 154.528 93.227  1.00 28.73 ?  140 TYR A CB    1 
ATOM   1161  C  CG    . TYR A 1 140 ? 122.220 155.283 93.891  1.00 30.16 ?  140 TYR A CG    1 
ATOM   1162  C  CD1   . TYR A 1 140 ? 123.490 154.734 93.988  1.00 28.80 ?  140 TYR A CD1   1 
ATOM   1163  C  CD2   . TYR A 1 140 ? 122.007 156.540 94.434  1.00 30.41 ?  140 TYR A CD2   1 
ATOM   1164  C  CE1   . TYR A 1 140 ? 124.517 155.421 94.598  1.00 29.52 ?  140 TYR A CE1   1 
ATOM   1165  C  CE2   . TYR A 1 140 ? 123.025 157.233 95.047  1.00 30.02 ?  140 TYR A CE2   1 
ATOM   1166  C  CZ    . TYR A 1 140 ? 124.277 156.671 95.127  1.00 25.73 ?  140 TYR A CZ    1 
ATOM   1167  O  OH    . TYR A 1 140 ? 125.289 157.365 95.740  1.00 31.30 ?  140 TYR A OH    1 
ATOM   1168  N  N     . VAL A 1 141 ? 119.246 153.242 90.980  1.00 32.97 ?  141 VAL A N     1 
ATOM   1169  C  CA    . VAL A 1 141 ? 118.321 152.197 90.553  1.00 30.44 ?  141 VAL A CA    1 
ATOM   1170  C  C     . VAL A 1 141 ? 118.860 151.480 89.322  1.00 29.32 ?  141 VAL A C     1 
ATOM   1171  O  O     . VAL A 1 141 ? 118.792 150.250 89.227  1.00 34.54 ?  141 VAL A O     1 
ATOM   1172  C  CB    . VAL A 1 141 ? 116.920 152.789 90.310  1.00 32.31 ?  141 VAL A CB    1 
ATOM   1173  C  CG1   . VAL A 1 141 ? 116.293 152.214 89.054  1.00 28.92 ?  141 VAL A CG1   1 
ATOM   1174  C  CG2   . VAL A 1 141 ? 116.027 152.516 91.501  1.00 32.26 ?  141 VAL A CG2   1 
ATOM   1175  N  N     . ASN A 1 142 ? 119.401 152.233 88.363  1.00 27.50 ?  142 ASN A N     1 
ATOM   1176  C  CA    . ASN A 1 142 ? 119.991 151.604 87.187  1.00 29.40 ?  142 ASN A CA    1 
ATOM   1177  C  C     . ASN A 1 142 ? 121.238 150.810 87.548  1.00 29.06 ?  142 ASN A C     1 
ATOM   1178  O  O     . ASN A 1 142 ? 121.525 149.788 86.914  1.00 36.97 ?  142 ASN A O     1 
ATOM   1179  C  CB    . ASN A 1 142 ? 120.319 152.660 86.134  1.00 29.77 ?  142 ASN A CB    1 
ATOM   1180  C  CG    . ASN A 1 142 ? 119.088 153.159 85.409  1.00 32.97 ?  142 ASN A CG    1 
ATOM   1181  O  OD1   . ASN A 1 142 ? 118.184 152.385 85.095  1.00 32.44 ?  142 ASN A OD1   1 
ATOM   1182  N  ND2   . ASN A 1 142 ? 119.045 154.457 85.138  1.00 33.88 ?  142 ASN A ND2   1 
ATOM   1183  N  N     . LEU A 1 143 ? 121.987 151.263 88.553  1.00 28.20 ?  143 LEU A N     1 
ATOM   1184  C  CA    . LEU A 1 143 ? 123.168 150.531 88.994  1.00 25.80 ?  143 LEU A CA    1 
ATOM   1185  C  C     . LEU A 1 143 ? 122.795 149.193 89.621  1.00 25.05 ?  143 LEU A C     1 
ATOM   1186  O  O     . LEU A 1 143 ? 123.429 148.170 89.340  1.00 28.27 ?  143 LEU A O     1 
ATOM   1187  C  CB    . LEU A 1 143 ? 123.957 151.382 89.986  1.00 23.48 ?  143 LEU A CB    1 
ATOM   1188  C  CG    . LEU A 1 143 ? 125.428 151.032 90.189  1.00 28.00 ?  143 LEU A CG    1 
ATOM   1189  C  CD1   . LEU A 1 143 ? 126.222 151.393 88.952  1.00 28.70 ?  143 LEU A CD1   1 
ATOM   1190  C  CD2   . LEU A 1 143 ? 125.969 151.754 91.408  1.00 29.39 ?  143 LEU A CD2   1 
ATOM   1191  N  N     . MET A 1 144 ? 121.774 149.183 90.476  1.00 28.78 ?  144 MET A N     1 
ATOM   1192  C  CA    . MET A 1 144 ? 121.401 147.974 91.202  1.00 23.13 ?  144 MET A CA    1 
ATOM   1193  C  C     . MET A 1 144 ? 120.506 147.035 90.404  1.00 25.40 ?  144 MET A C     1 
ATOM   1194  O  O     . MET A 1 144 ? 120.534 145.823 90.642  1.00 29.77 ?  144 MET A O     1 
ATOM   1195  C  CB    . MET A 1 144 ? 120.709 148.343 92.515  1.00 23.68 ?  144 MET A CB    1 
ATOM   1196  C  CG    . MET A 1 144 ? 121.494 149.321 93.363  1.00 26.24 ?  144 MET A CG    1 
ATOM   1197  S  SD    . MET A 1 144 ? 120.989 149.301 95.087  1.00 33.43 ?  144 MET A SD    1 
ATOM   1198  C  CE    . MET A 1 144 ? 120.210 150.907 95.195  1.00 28.66 ?  144 MET A CE    1 
ATOM   1199  N  N     . ILE A 1 145 ? 119.712 147.555 89.471  1.00 29.37 ?  145 ILE A N     1 
ATOM   1200  C  CA    . ILE A 1 145 ? 118.874 146.695 88.646  1.00 28.87 ?  145 ILE A CA    1 
ATOM   1201  C  C     . ILE A 1 145 ? 119.671 146.086 87.495  1.00 31.49 ?  145 ILE A C     1 
ATOM   1202  O  O     . ILE A 1 145 ? 119.328 145.002 87.013  1.00 35.53 ?  145 ILE A O     1 
ATOM   1203  C  CB    . ILE A 1 145 ? 117.640 147.463 88.137  1.00 27.96 ?  145 ILE A CB    1 
ATOM   1204  C  CG1   . ILE A 1 145 ? 116.470 146.504 87.907  1.00 30.70 ?  145 ILE A CG1   1 
ATOM   1205  C  CG2   . ILE A 1 145 ? 117.953 148.242 86.866  1.00 32.52 ?  145 ILE A CG2   1 
ATOM   1206  C  CD1   . ILE A 1 145 ? 115.992 145.804 89.156  1.00 28.51 ?  145 ILE A CD1   1 
ATOM   1207  N  N     . ASN A 1 146 ? 120.733 146.759 87.046  1.00 23.60 ?  146 ASN A N     1 
ATOM   1208  C  CA    . ASN A 1 146 ? 121.730 146.110 86.209  1.00 26.02 ?  146 ASN A CA    1 
ATOM   1209  C  C     . ASN A 1 146 ? 122.610 145.166 87.012  1.00 25.75 ?  146 ASN A C     1 
ATOM   1210  O  O     . ASN A 1 146 ? 123.403 144.427 86.420  1.00 30.46 ?  146 ASN A O     1 
ATOM   1211  C  CB    . ASN A 1 146 ? 122.600 147.152 85.506  1.00 25.53 ?  146 ASN A CB    1 
ATOM   1212  C  CG    . ASN A 1 146 ? 121.837 147.940 84.462  1.00 30.32 ?  146 ASN A CG    1 
ATOM   1213  O  OD1   . ASN A 1 146 ? 120.760 147.537 84.028  1.00 35.31 ?  146 ASN A OD1   1 
ATOM   1214  N  ND2   . ASN A 1 146 ? 122.396 149.072 84.050  1.00 30.38 ?  146 ASN A ND2   1 
ATOM   1215  N  N     . GLN A 1 147 ? 122.486 145.191 88.340  1.00 23.38 ?  147 GLN A N     1 
ATOM   1216  C  CA    . GLN A 1 147 ? 123.247 144.329 89.241  1.00 20.38 ?  147 GLN A CA    1 
ATOM   1217  C  C     . GLN A 1 147 ? 124.748 144.544 89.075  1.00 26.35 ?  147 GLN A C     1 
ATOM   1218  O  O     . GLN A 1 147 ? 125.545 143.617 89.220  1.00 35.68 ?  147 GLN A O     1 
ATOM   1219  C  CB    . GLN A 1 147 ? 122.874 142.858 89.047  1.00 24.70 ?  147 GLN A CB    1 
ATOM   1220  C  CG    . GLN A 1 147 ? 121.495 142.507 89.580  1.00 23.57 ?  147 GLN A CG    1 
ATOM   1221  C  CD    . GLN A 1 147 ? 121.354 141.038 89.910  1.00 26.46 ?  147 GLN A CD    1 
ATOM   1222  O  OE1   . GLN A 1 147 ? 120.723 140.671 90.901  1.00 28.11 ?  147 GLN A OE1   1 
ATOM   1223  N  NE2   . GLN A 1 147 ? 121.944 140.187 89.081  1.00 35.92 ?  147 GLN A NE2   1 
ATOM   1224  N  N     . GLU A 1 148 ? 125.134 145.781 88.762  1.00 25.21 ?  148 GLU A N     1 
ATOM   1225  C  CA    . GLU A 1 148 ? 126.549 146.129 88.710  1.00 22.94 ?  148 GLU A CA    1 
ATOM   1226  C  C     . GLU A 1 148 ? 127.123 146.314 90.107  1.00 24.69 ?  148 GLU A C     1 
ATOM   1227  O  O     . GLU A 1 148 ? 128.263 145.920 90.373  1.00 29.83 ?  148 GLU A O     1 
ATOM   1228  C  CB    . GLU A 1 148 ? 126.747 147.397 87.880  1.00 20.80 ?  148 GLU A CB    1 
ATOM   1229  C  CG    . GLU A 1 148 ? 126.268 147.280 86.445  1.00 24.20 ?  148 GLU A CG    1 
ATOM   1230  C  CD    . GLU A 1 148 ? 126.131 148.626 85.767  1.00 33.09 ?  148 GLU A CD    1 
ATOM   1231  O  OE1   . GLU A 1 148 ? 125.111 149.308 85.996  1.00 36.31 ?  148 GLU A OE1   1 
ATOM   1232  O  OE2   . GLU A 1 148 ? 127.044 149.005 85.005  1.00 36.13 -1 148 GLU A OE2   1 
ATOM   1233  N  N     . TYR A 1 149 ? 126.349 146.905 91.010  1.00 18.43 ?  149 TYR A N     1 
ATOM   1234  C  CA    . TYR A 1 149 ? 126.767 147.123 92.385  1.00 20.58 ?  149 TYR A CA    1 
ATOM   1235  C  C     . TYR A 1 149 ? 125.716 146.560 93.324  1.00 22.59 ?  149 TYR A C     1 
ATOM   1236  O  O     . TYR A 1 149 ? 124.515 146.650 93.053  1.00 30.54 ?  149 TYR A O     1 
ATOM   1237  C  CB    . TYR A 1 149 ? 126.987 148.610 92.671  1.00 22.04 ?  149 TYR A CB    1 
ATOM   1238  C  CG    . TYR A 1 149 ? 127.146 148.935 94.137  1.00 21.96 ?  149 TYR A CG    1 
ATOM   1239  C  CD1   . TYR A 1 149 ? 128.239 148.475 94.857  1.00 17.07 ?  149 TYR A CD1   1 
ATOM   1240  C  CD2   . TYR A 1 149 ? 126.199 149.703 94.803  1.00 19.77 ?  149 TYR A CD2   1 
ATOM   1241  C  CE1   . TYR A 1 149 ? 128.386 148.772 96.197  1.00 22.13 ?  149 TYR A CE1   1 
ATOM   1242  C  CE2   . TYR A 1 149 ? 126.337 150.005 96.140  1.00 17.50 ?  149 TYR A CE2   1 
ATOM   1243  C  CZ    . TYR A 1 149 ? 127.432 149.536 96.833  1.00 19.19 ?  149 TYR A CZ    1 
ATOM   1244  O  OH    . TYR A 1 149 ? 127.574 149.834 98.168  1.00 20.73 ?  149 TYR A OH    1 
ATOM   1245  N  N     . GLN A 1 150 ? 126.172 145.979 94.425  1.00 19.43 ?  150 GLN A N     1 
ATOM   1246  C  CA    . GLN A 1 150 ? 125.294 145.381 95.425  1.00 14.05 ?  150 GLN A CA    1 
ATOM   1247  C  C     . GLN A 1 150 ? 125.684 145.930 96.788  1.00 17.22 ?  150 GLN A C     1 
ATOM   1248  O  O     . GLN A 1 150 ? 126.815 145.675 97.252  1.00 18.47 ?  150 GLN A O     1 
ATOM   1249  C  CB    . GLN A 1 150 ? 125.395 143.859 95.391  1.00 19.49 ?  150 GLN A CB    1 
ATOM   1250  C  CG    . GLN A 1 150 ? 124.692 143.142 96.527  1.00 20.50 ?  150 GLN A CG    1 
ATOM   1251  C  CD    . GLN A 1 150 ? 123.227 143.509 96.633  1.00 17.04 ?  150 GLN A CD    1 
ATOM   1252  O  OE1   . GLN A 1 150 ? 122.432 143.200 95.747  1.00 22.92 ?  150 GLN A OE1   1 
ATOM   1253  N  NE2   . GLN A 1 150 ? 122.863 144.168 97.723  1.00 19.47 ?  150 GLN A NE2   1 
ATOM   1254  N  N     . PRO A 1 151 ? 124.819 146.701 97.441  1.00 24.37 ?  151 PRO A N     1 
ATOM   1255  C  CA    . PRO A 1 151 ? 125.075 147.060 98.838  1.00 10.14 ?  151 PRO A CA    1 
ATOM   1256  C  C     . PRO A 1 151 ? 125.104 145.810 99.701  1.00 13.12 ?  151 PRO A C     1 
ATOM   1257  O  O     . PRO A 1 151 ? 124.464 144.803 99.395  1.00 25.36 ?  151 PRO A O     1 
ATOM   1258  C  CB    . PRO A 1 151 ? 123.894 147.969 99.199  1.00 19.55 ?  151 PRO A CB    1 
ATOM   1259  C  CG    . PRO A 1 151 ? 123.365 148.454 97.890  1.00 19.21 ?  151 PRO A CG    1 
ATOM   1260  C  CD    . PRO A 1 151 ? 123.607 147.346 96.914  1.00 19.61 ?  151 PRO A CD    1 
ATOM   1261  N  N     . SER A 1 152 ? 125.875 145.879 100.783 1.00 23.35 ?  152 SER A N     1 
ATOM   1262  C  CA    . SER A 1 152 ? 126.028 144.734 101.664 1.00 19.59 ?  152 SER A CA    1 
ATOM   1263  C  C     . SER A 1 152 ? 124.677 144.311 102.239 1.00 22.03 ?  152 SER A C     1 
ATOM   1264  O  O     . SER A 1 152 ? 123.677 145.025 102.151 1.00 27.11 ?  152 SER A O     1 
ATOM   1265  C  CB    . SER A 1 152 ? 127.002 145.058 102.792 1.00 19.84 ?  152 SER A CB    1 
ATOM   1266  O  OG    . SER A 1 152 ? 126.490 146.084 103.622 1.00 23.90 ?  152 SER A OG    1 
ATOM   1267  N  N     . THR A 1 153 ? 124.664 143.121 102.835 1.00 26.99 ?  153 THR A N     1 
ATOM   1268  C  CA    . THR A 1 153 ? 123.448 142.617 103.466 1.00 21.18 ?  153 THR A CA    1 
ATOM   1269  C  C     . THR A 1 153 ? 122.839 143.595 104.466 1.00 30.64 ?  153 THR A C     1 
ATOM   1270  O  O     . THR A 1 153 ? 121.615 143.802 104.406 1.00 32.29 ?  153 THR A O     1 
ATOM   1271  C  CB    . THR A 1 153 ? 123.733 141.260 104.129 1.00 26.27 ?  153 THR A CB    1 
ATOM   1272  O  OG1   . THR A 1 153 ? 123.926 140.262 103.119 1.00 31.38 ?  153 THR A OG1   1 
ATOM   1273  C  CG2   . THR A 1 153 ? 122.581 140.845 105.032 1.00 25.56 ?  153 THR A CG2   1 
ATOM   1274  N  N     . PRO A 1 154 ? 123.593 144.232 105.372 1.00 28.10 ?  154 PRO A N     1 
ATOM   1275  C  CA    . PRO A 1 154 ? 122.961 145.247 106.236 1.00 20.25 ?  154 PRO A CA    1 
ATOM   1276  C  C     . PRO A 1 154 ? 122.347 146.394 105.454 1.00 20.45 ?  154 PRO A C     1 
ATOM   1277  O  O     . PRO A 1 154 ? 121.179 146.738 105.676 1.00 28.25 ?  154 PRO A O     1 
ATOM   1278  C  CB    . PRO A 1 154 ? 124.121 145.719 107.123 1.00 22.33 ?  154 PRO A CB    1 
ATOM   1279  C  CG    . PRO A 1 154 ? 125.101 144.627 107.083 1.00 18.21 ?  154 PRO A CG    1 
ATOM   1280  C  CD    . PRO A 1 154 ? 125.007 144.021 105.734 1.00 19.76 ?  154 PRO A CD    1 
ATOM   1281  N  N     . THR A 1 155 ? 123.106 146.995 104.537 1.00 21.90 ?  155 THR A N     1 
ATOM   1282  C  CA    . THR A 1 155 ? 122.590 148.123 103.770 1.00 22.24 ?  155 THR A CA    1 
ATOM   1283  C  C     . THR A 1 155 ? 121.419 147.701 102.890 1.00 24.01 ?  155 THR A C     1 
ATOM   1284  O  O     . THR A 1 155 ? 120.370 148.352 102.882 1.00 25.79 ?  155 THR A O     1 
ATOM   1285  C  CB    . THR A 1 155 ? 123.704 148.735 102.921 1.00 20.44 ?  155 THR A CB    1 
ATOM   1286  O  OG1   . THR A 1 155 ? 124.853 148.977 103.741 1.00 26.23 ?  155 THR A OG1   1 
ATOM   1287  C  CG2   . THR A 1 155 ? 123.242 150.045 102.310 1.00 15.83 ?  155 THR A CG2   1 
ATOM   1288  N  N     . PHE A 1 156 ? 121.578 146.604 102.148 1.00 26.18 ?  156 PHE A N     1 
ATOM   1289  C  CA    . PHE A 1 156 ? 120.525 146.177 101.232 1.00 22.55 ?  156 PHE A CA    1 
ATOM   1290  C  C     . PHE A 1 156 ? 119.253 145.804 101.981 1.00 29.74 ?  156 PHE A C     1 
ATOM   1291  O  O     . PHE A 1 156 ? 118.144 146.124 101.535 1.00 25.60 ?  156 PHE A O     1 
ATOM   1292  C  CB    . PHE A 1 156 ? 121.010 145.002 100.385 1.00 21.93 ?  156 PHE A CB    1 
ATOM   1293  C  CG    . PHE A 1 156 ? 120.166 144.743 99.173  1.00 27.63 ?  156 PHE A CG    1 
ATOM   1294  C  CD1   . PHE A 1 156 ? 119.942 145.743 98.244  1.00 24.70 ?  156 PHE A CD1   1 
ATOM   1295  C  CD2   . PHE A 1 156 ? 119.594 143.499 98.964  1.00 23.84 ?  156 PHE A CD2   1 
ATOM   1296  C  CE1   . PHE A 1 156 ? 119.166 145.509 97.128  1.00 24.94 ?  156 PHE A CE1   1 
ATOM   1297  C  CE2   . PHE A 1 156 ? 118.817 143.260 97.850  1.00 25.17 ?  156 PHE A CE2   1 
ATOM   1298  C  CZ    . PHE A 1 156 ? 118.602 144.266 96.931  1.00 29.02 ?  156 PHE A CZ    1 
ATOM   1299  N  N     . LEU A 1 157 ? 119.389 145.124 103.119 1.00 29.89 ?  157 LEU A N     1 
ATOM   1300  C  CA    . LEU A 1 157 ? 118.223 144.660 103.861 1.00 24.18 ?  157 LEU A CA    1 
ATOM   1301  C  C     . LEU A 1 157 ? 117.540 145.787 104.627 1.00 27.71 ?  157 LEU A C     1 
ATOM   1302  O  O     . LEU A 1 157 ? 116.307 145.836 104.687 1.00 38.07 ?  157 LEU A O     1 
ATOM   1303  C  CB    . LEU A 1 157 ? 118.636 143.539 104.816 1.00 29.60 ?  157 LEU A CB    1 
ATOM   1304  C  CG    . LEU A 1 157 ? 117.632 143.126 105.892 1.00 30.16 ?  157 LEU A CG    1 
ATOM   1305  C  CD1   . LEU A 1 157 ? 116.630 142.137 105.332 1.00 31.34 ?  157 LEU A CD1   1 
ATOM   1306  C  CD2   . LEU A 1 157 ? 118.353 142.536 107.093 1.00 25.42 ?  157 LEU A CD2   1 
ATOM   1307  N  N     . ASN A 1 158 ? 118.312 146.706 105.207 1.00 29.43 ?  158 ASN A N     1 
ATOM   1308  C  CA    . ASN A 1 158 ? 117.776 147.633 106.192 1.00 28.29 ?  158 ASN A CA    1 
ATOM   1309  C  C     . ASN A 1 158 ? 117.581 149.053 105.675 1.00 29.21 ?  158 ASN A C     1 
ATOM   1310  O  O     . ASN A 1 158 ? 116.950 149.856 106.368 1.00 35.75 ?  158 ASN A O     1 
ATOM   1311  C  CB    . ASN A 1 158 ? 118.688 147.670 107.422 1.00 28.05 ?  158 ASN A CB    1 
ATOM   1312  C  CG    . ASN A 1 158 ? 118.726 146.348 108.158 1.00 33.65 ?  158 ASN A CG    1 
ATOM   1313  O  OD1   . ASN A 1 158 ? 117.692 145.725 108.391 1.00 37.04 ?  158 ASN A OD1   1 
ATOM   1314  N  ND2   . ASN A 1 158 ? 119.924 145.910 108.522 1.00 34.74 ?  158 ASN A ND2   1 
ATOM   1315  N  N     . ALA A 1 159 ? 118.098 149.389 104.496 1.00 27.74 ?  159 ALA A N     1 
ATOM   1316  C  CA    . ALA A 1 159 ? 117.983 150.759 104.008 1.00 27.63 ?  159 ALA A CA    1 
ATOM   1317  C  C     . ALA A 1 159 ? 116.521 151.128 103.804 1.00 33.43 ?  159 ALA A C     1 
ATOM   1318  O  O     . ALA A 1 159 ? 115.791 150.442 103.082 1.00 39.61 ?  159 ALA A O     1 
ATOM   1319  C  CB    . ALA A 1 159 ? 118.760 150.934 102.705 1.00 29.21 ?  159 ALA A CB    1 
ATOM   1320  N  N     . GLY A 1 160 ? 116.098 152.216 104.443 1.00 36.32 ?  160 GLY A N     1 
ATOM   1321  C  CA    . GLY A 1 160 ? 114.741 152.695 104.320 1.00 36.92 ?  160 GLY A CA    1 
ATOM   1322  C  C     . GLY A 1 160 ? 113.722 152.009 105.202 1.00 39.04 ?  160 GLY A C     1 
ATOM   1323  O  O     . GLY A 1 160 ? 112.528 152.297 105.071 1.00 44.26 ?  160 GLY A O     1 
ATOM   1324  N  N     . ARG A 1 161 ? 114.145 151.117 106.093 1.00 41.42 ?  161 ARG A N     1 
ATOM   1325  C  CA    . ARG A 1 161 ? 113.234 150.376 106.956 1.00 41.58 ?  161 ARG A CA    1 
ATOM   1326  C  C     . ARG A 1 161 ? 113.309 150.919 108.377 1.00 43.09 ?  161 ARG A C     1 
ATOM   1327  O  O     . ARG A 1 161 ? 114.404 151.134 108.905 1.00 45.61 ?  161 ARG A O     1 
ATOM   1328  C  CB    . ARG A 1 161 ? 113.567 148.884 106.946 1.00 37.99 ?  161 ARG A CB    1 
ATOM   1329  C  CG    . ARG A 1 161 ? 113.292 148.195 105.623 1.00 40.07 ?  161 ARG A CG    1 
ATOM   1330  C  CD    . ARG A 1 161 ? 113.236 146.688 105.793 1.00 39.67 ?  161 ARG A CD    1 
ATOM   1331  N  NE    . ARG A 1 161 ? 113.263 145.994 104.512 1.00 42.62 ?  161 ARG A NE    1 
ATOM   1332  C  CZ    . ARG A 1 161 ? 113.450 144.688 104.372 1.00 43.82 ?  161 ARG A CZ    1 
ATOM   1333  N  NH1   . ARG A 1 161 ? 113.619 143.898 105.419 1.00 39.86 1  161 ARG A NH1   1 
ATOM   1334  N  NH2   . ARG A 1 161 ? 113.470 144.164 103.151 1.00 43.40 ?  161 ARG A NH2   1 
ATOM   1335  N  N     . LYS A 1 162 ? 112.144 151.142 108.989 1.00 48.38 ?  162 LYS A N     1 
ATOM   1336  C  CA    . LYS A 1 162 ? 112.115 151.646 110.359 1.00 50.04 ?  162 LYS A CA    1 
ATOM   1337  C  C     . LYS A 1 162 ? 112.540 150.569 111.352 1.00 49.96 ?  162 LYS A C     1 
ATOM   1338  O  O     . LYS A 1 162 ? 113.337 150.828 112.261 1.00 51.28 ?  162 LYS A O     1 
ATOM   1339  C  CB    . LYS A 1 162 ? 110.720 152.173 110.698 1.00 49.53 ?  162 LYS A CB    1 
ATOM   1340  C  CG    . LYS A 1 162 ? 110.658 152.959 111.999 1.00 48.91 ?  162 LYS A CG    1 
ATOM   1341  C  CD    . LYS A 1 162 ? 109.945 154.290 111.819 1.00 49.75 ?  162 LYS A CD    1 
ATOM   1342  C  CE    . LYS A 1 162 ? 108.550 154.099 111.249 1.00 52.02 ?  162 LYS A CE    1 
ATOM   1343  N  NZ    . LYS A 1 162 ? 108.147 155.234 110.374 1.00 52.03 1  162 LYS A NZ    1 
ATOM   1344  N  N     . ARG A 1 163 ? 112.017 149.356 111.194 1.00 49.65 ?  163 ARG A N     1 
ATOM   1345  C  CA    . ARG A 1 163 ? 112.397 148.225 112.041 1.00 51.16 ?  163 ARG A CA    1 
ATOM   1346  C  C     . ARG A 1 163 ? 113.646 147.603 111.433 1.00 52.31 ?  163 ARG A C     1 
ATOM   1347  O  O     . ARG A 1 163 ? 113.576 146.713 110.585 1.00 53.52 ?  163 ARG A O     1 
ATOM   1348  C  CB    . ARG A 1 163 ? 111.255 147.222 112.149 1.00 53.63 ?  163 ARG A CB    1 
ATOM   1349  C  CG    . ARG A 1 163 ? 111.126 146.548 113.509 1.00 52.96 ?  163 ARG A CG    1 
ATOM   1350  C  CD    . ARG A 1 163 ? 112.276 145.593 113.790 1.00 52.96 ?  163 ARG A CD    1 
ATOM   1351  N  NE    . ARG A 1 163 ? 112.568 144.729 112.652 1.00 53.32 ?  163 ARG A NE    1 
ATOM   1352  C  CZ    . ARG A 1 163 ? 113.768 144.235 112.375 1.00 53.85 ?  163 ARG A CZ    1 
ATOM   1353  N  NH1   . ARG A 1 163 ? 114.817 144.503 113.135 1.00 53.22 1  163 ARG A NH1   1 
ATOM   1354  N  NH2   . ARG A 1 163 ? 113.917 143.455 111.310 1.00 52.27 ?  163 ARG A NH2   1 
ATOM   1355  N  N     . ARG A 1 164 ? 114.808 148.081 111.871 1.00 50.24 ?  164 ARG A N     1 
ATOM   1356  C  CA    . ARG A 1 164 ? 116.061 147.711 111.234 1.00 50.56 ?  164 ARG A CA    1 
ATOM   1357  C  C     . ARG A 1 164 ? 117.198 147.791 112.240 1.00 49.30 ?  164 ARG A C     1 
ATOM   1358  O  O     . ARG A 1 164 ? 117.101 148.457 113.273 1.00 50.46 ?  164 ARG A O     1 
ATOM   1359  C  CB    . ARG A 1 164 ? 116.367 148.619 110.040 1.00 46.90 ?  164 ARG A CB    1 
ATOM   1360  C  CG    . ARG A 1 164 ? 116.908 149.984 110.446 1.00 43.57 ?  164 ARG A CG    1 
ATOM   1361  C  CD    . ARG A 1 164 ? 117.607 150.674 109.290 1.00 46.79 ?  164 ARG A CD    1 
ATOM   1362  N  NE    . ARG A 1 164 ? 118.026 152.032 109.619 1.00 46.54 ?  164 ARG A NE    1 
ATOM   1363  C  CZ    . ARG A 1 164 ? 119.080 152.333 110.363 1.00 49.60 ?  164 ARG A CZ    1 
ATOM   1364  N  NH1   . ARG A 1 164 ? 119.851 151.393 110.885 1.00 48.82 1  164 ARG A NH1   1 
ATOM   1365  N  NH2   . ARG A 1 164 ? 119.370 153.611 110.589 1.00 47.91 ?  164 ARG A NH2   1 
ATOM   1366  N  N     . GLY A 1 165 ? 118.284 147.090 111.919 1.00 43.35 ?  165 GLY A N     1 
ATOM   1367  C  CA    . GLY A 1 165 ? 119.550 147.276 112.592 1.00 42.46 ?  165 GLY A CA    1 
ATOM   1368  C  C     . GLY A 1 165 ? 120.383 148.337 111.900 1.00 45.44 ?  165 GLY A C     1 
ATOM   1369  O  O     . GLY A 1 165 ? 119.933 149.032 110.988 1.00 46.28 ?  165 GLY A O     1 
ATOM   1370  N  N     . GLU A 1 166 ? 121.629 148.456 112.345 1.00 39.87 ?  166 GLU A N     1 
ATOM   1371  C  CA    . GLU A 1 166 ? 122.527 149.409 111.717 1.00 37.89 ?  166 GLU A CA    1 
ATOM   1372  C  C     . GLU A 1 166 ? 122.955 148.912 110.337 1.00 38.58 ?  166 GLU A C     1 
ATOM   1373  O  O     . GLU A 1 166 ? 122.976 147.712 110.055 1.00 36.64 ?  166 GLU A O     1 
ATOM   1374  C  CB    . GLU A 1 166 ? 123.755 149.657 112.595 1.00 35.65 ?  166 GLU A CB    1 
ATOM   1375  C  CG    . GLU A 1 166 ? 123.712 150.966 113.374 1.00 38.87 ?  166 GLU A CG    1 
ATOM   1376  C  CD    . GLU A 1 166 ? 123.607 152.196 112.483 1.00 45.97 ?  166 GLU A CD    1 
ATOM   1377  O  OE1   . GLU A 1 166 ? 123.964 152.113 111.288 1.00 48.15 ?  166 GLU A OE1   1 
ATOM   1378  O  OE2   . GLU A 1 166 ? 123.163 153.251 112.981 1.00 43.24 -1 166 GLU A OE2   1 
ATOM   1379  N  N     . LEU A 1 167 ? 123.298 149.865 109.470 1.00 30.76 ?  167 LEU A N     1 
ATOM   1380  C  CA    . LEU A 1 167 ? 123.748 149.539 108.124 1.00 25.60 ?  167 LEU A CA    1 
ATOM   1381  C  C     . LEU A 1 167 ? 125.192 149.063 108.084 1.00 28.67 ?  167 LEU A C     1 
ATOM   1382  O  O     . LEU A 1 167 ? 125.642 148.587 107.037 1.00 30.69 ?  167 LEU A O     1 
ATOM   1383  C  CB    . LEU A 1 167 ? 123.583 150.752 107.209 1.00 26.21 ?  167 LEU A CB    1 
ATOM   1384  C  CG    . LEU A 1 167 ? 122.153 151.236 106.974 1.00 25.34 ?  167 LEU A CG    1 
ATOM   1385  C  CD1   . LEU A 1 167 ? 122.117 152.203 105.816 1.00 27.51 ?  167 LEU A CD1   1 
ATOM   1386  C  CD2   . LEU A 1 167 ? 121.230 150.065 106.714 1.00 27.01 ?  167 LEU A CD2   1 
ATOM   1387  N  N     . VAL A 1 168 ? 125.920 149.184 109.188 1.00 29.92 ?  168 VAL A N     1 
ATOM   1388  C  CA    . VAL A 1 168 ? 127.282 148.679 109.306 1.00 20.10 ?  168 VAL A CA    1 
ATOM   1389  C  C     . VAL A 1 168 ? 127.246 147.440 110.184 1.00 25.75 ?  168 VAL A C     1 
ATOM   1390  O  O     . VAL A 1 168 ? 126.594 147.436 111.237 1.00 33.49 ?  168 VAL A O     1 
ATOM   1391  C  CB    . VAL A 1 168 ? 128.222 149.745 109.894 1.00 24.69 ?  168 VAL A CB    1 
ATOM   1392  C  CG1   . VAL A 1 168 ? 129.647 149.221 109.956 1.00 29.31 ?  168 VAL A CG1   1 
ATOM   1393  C  CG2   . VAL A 1 168 ? 128.154 151.024 109.075 1.00 27.55 ?  168 VAL A CG2   1 
ATOM   1394  N  N     . SER A 1 169 ? 127.926 146.380 109.751 1.00 26.07 ?  169 SER A N     1 
ATOM   1395  C  CA    . SER A 1 169 ? 127.994 145.153 110.529 1.00 29.38 ?  169 SER A CA    1 
ATOM   1396  C  C     . SER A 1 169 ? 129.410 144.674 110.800 1.00 32.50 ?  169 SER A C     1 
ATOM   1397  O  O     . SER A 1 169 ? 129.578 143.613 111.410 1.00 38.92 ?  169 SER A O     1 
ATOM   1398  C  CB    . SER A 1 169 ? 127.202 144.032 109.845 1.00 30.68 ?  169 SER A CB    1 
ATOM   1399  O  OG    . SER A 1 169 ? 125.813 144.191 110.073 1.00 38.06 ?  169 SER A OG    1 
ATOM   1400  N  N     . CYS A 1 170 ? 130.429 145.407 110.368 1.00 26.32 ?  170 CYS A N     1 
ATOM   1401  C  CA    . CYS A 1 170 ? 131.807 145.102 110.723 1.00 24.16 ?  170 CYS A CA    1 
ATOM   1402  C  C     . CYS A 1 170 ? 132.310 146.191 111.662 1.00 23.58 ?  170 CYS A C     1 
ATOM   1403  O  O     . CYS A 1 170 ? 132.351 147.370 111.293 1.00 26.85 ?  170 CYS A O     1 
ATOM   1404  C  CB    . CYS A 1 170 ? 132.689 144.963 109.478 1.00 30.30 ?  170 CYS A CB    1 
ATOM   1405  S  SG    . CYS A 1 170 ? 133.072 146.473 108.561 1.00 48.74 ?  170 CYS A SG    1 
ATOM   1406  N  N     . PHE A 1 171 ? 132.651 145.797 112.885 1.00 23.10 ?  171 PHE A N     1 
ATOM   1407  C  CA    . PHE A 1 171 ? 133.128 146.716 113.907 1.00 10.69 ?  171 PHE A CA    1 
ATOM   1408  C  C     . PHE A 1 171 ? 134.406 146.164 114.507 1.00 15.01 ?  171 PHE A C     1 
ATOM   1409  O  O     . PHE A 1 171 ? 134.475 144.981 114.851 1.00 22.56 ?  171 PHE A O     1 
ATOM   1410  C  CB    . PHE A 1 171 ? 132.078 146.928 115.001 1.00 15.76 ?  171 PHE A CB    1 
ATOM   1411  C  CG    . PHE A 1 171 ? 130.783 147.484 114.495 1.00 17.29 ?  171 PHE A CG    1 
ATOM   1412  C  CD1   . PHE A 1 171 ? 130.686 148.813 114.130 1.00 19.36 ?  171 PHE A CD1   1 
ATOM   1413  C  CD2   . PHE A 1 171 ? 129.662 146.680 114.386 1.00 15.63 ?  171 PHE A CD2   1 
ATOM   1414  C  CE1   . PHE A 1 171 ? 129.500 149.329 113.659 1.00 14.98 ?  171 PHE A CE1   1 
ATOM   1415  C  CE2   . PHE A 1 171 ? 128.471 147.193 113.920 1.00 16.79 ?  171 PHE A CE2   1 
ATOM   1416  C  CZ    . PHE A 1 171 ? 128.391 148.520 113.556 1.00 16.17 ?  171 PHE A CZ    1 
ATOM   1417  N  N     . LEU A 1 172 ? 135.415 147.019 114.628 1.00 14.71 ?  172 LEU A N     1 
ATOM   1418  C  CA    . LEU A 1 172 ? 136.685 146.657 115.235 1.00 9.06  ?  172 LEU A CA    1 
ATOM   1419  C  C     . LEU A 1 172 ? 136.882 147.506 116.479 1.00 13.65 ?  172 LEU A C     1 
ATOM   1420  O  O     . LEU A 1 172 ? 136.845 148.738 116.403 1.00 16.89 ?  172 LEU A O     1 
ATOM   1421  C  CB    . LEU A 1 172 ? 137.845 146.859 114.259 1.00 14.71 ?  172 LEU A CB    1 
ATOM   1422  C  CG    . LEU A 1 172 ? 137.985 145.869 113.104 1.00 6.10  ?  172 LEU A CG    1 
ATOM   1423  C  CD1   . LEU A 1 172 ? 137.012 146.202 111.986 1.00 8.62  ?  172 LEU A CD1   1 
ATOM   1424  C  CD2   . LEU A 1 172 ? 139.409 145.870 112.590 1.00 13.30 ?  172 LEU A CD2   1 
ATOM   1425  N  N     . LEU A 1 173 ? 137.091 146.852 117.615 1.00 16.08 ?  173 LEU A N     1 
ATOM   1426  C  CA    . LEU A 1 173 ? 137.250 147.532 118.889 1.00 12.47 ?  173 LEU A CA    1 
ATOM   1427  C  C     . LEU A 1 173 ? 138.656 147.324 119.428 1.00 11.97 ?  173 LEU A C     1 
ATOM   1428  O  O     . LEU A 1 173 ? 139.202 146.219 119.361 1.00 16.59 ?  173 LEU A O     1 
ATOM   1429  C  CB    . LEU A 1 173 ? 136.232 147.033 119.917 1.00 16.96 ?  173 LEU A CB    1 
ATOM   1430  C  CG    . LEU A 1 173 ? 134.757 147.025 119.527 1.00 20.16 ?  173 LEU A CG    1 
ATOM   1431  C  CD1   . LEU A 1 173 ? 133.915 146.621 120.723 1.00 19.08 ?  173 LEU A CD1   1 
ATOM   1432  C  CD2   . LEU A 1 173 ? 134.324 148.379 118.990 1.00 16.49 ?  173 LEU A CD2   1 
ATOM   1433  N  N     . GLU A 1 174 ? 139.238 148.395 119.952 1.00 25.98 ?  174 GLU A N     1 
ATOM   1434  C  CA    . GLU A 1 174 ? 140.479 148.312 120.704 1.00 23.68 ?  174 GLU A CA    1 
ATOM   1435  C  C     . GLU A 1 174 ? 140.161 148.250 122.190 1.00 20.40 ?  174 GLU A C     1 
ATOM   1436  O  O     . GLU A 1 174 ? 139.387 149.063 122.704 1.00 29.43 ?  174 GLU A O     1 
ATOM   1437  C  CB    . GLU A 1 174 ? 141.373 149.516 120.407 1.00 26.29 ?  174 GLU A CB    1 
ATOM   1438  C  CG    . GLU A 1 174 ? 141.859 149.596 118.973 1.00 22.14 ?  174 GLU A CG    1 
ATOM   1439  C  CD    . GLU A 1 174 ? 143.274 149.085 118.813 1.00 25.00 ?  174 GLU A CD    1 
ATOM   1440  O  OE1   . GLU A 1 174 ? 143.918 148.781 119.838 1.00 28.05 ?  174 GLU A OE1   1 
ATOM   1441  O  OE2   . GLU A 1 174 ? 143.745 148.986 117.661 1.00 28.48 -1 174 GLU A OE2   1 
ATOM   1442  N  N     . VAL A 1 175 ? 140.756 147.282 122.876 1.00 19.84 ?  175 VAL A N     1 
ATOM   1443  C  CA    . VAL A 1 175 ? 140.539 147.080 124.304 1.00 20.81 ?  175 VAL A CA    1 
ATOM   1444  C  C     . VAL A 1 175 ? 141.821 147.450 125.034 1.00 18.94 ?  175 VAL A C     1 
ATOM   1445  O  O     . VAL A 1 175 ? 142.876 146.849 124.796 1.00 26.83 ?  175 VAL A O     1 
ATOM   1446  C  CB    . VAL A 1 175 ? 140.120 145.636 124.618 1.00 22.21 ?  175 VAL A CB    1 
ATOM   1447  C  CG1   . VAL A 1 175 ? 139.600 145.531 126.043 1.00 14.41 ?  175 VAL A CG1   1 
ATOM   1448  C  CG2   . VAL A 1 175 ? 139.074 145.159 123.623 1.00 19.87 ?  175 VAL A CG2   1 
ATOM   1449  N  N     . ASN A 1 176 ? 141.731 148.437 125.920 1.00 18.41 ?  176 ASN A N     1 
ATOM   1450  C  CA    . ASN A 1 176 ? 142.875 148.836 126.719 1.00 20.00 ?  176 ASN A CA    1 
ATOM   1451  C  C     . ASN A 1 176 ? 143.009 147.935 127.942 1.00 23.60 ?  176 ASN A C     1 
ATOM   1452  O  O     . ASN A 1 176 ? 142.060 147.270 128.367 1.00 24.22 ?  176 ASN A O     1 
ATOM   1453  C  CB    . ASN A 1 176 ? 142.751 150.298 127.142 1.00 18.83 ?  176 ASN A CB    1 
ATOM   1454  C  CG    . ASN A 1 176 ? 144.084 151.012 127.171 1.00 21.31 ?  176 ASN A CG    1 
ATOM   1455  O  OD1   . ASN A 1 176 ? 145.130 150.389 127.350 1.00 27.96 ?  176 ASN A OD1   1 
ATOM   1456  N  ND2   . ASN A 1 176 ? 144.055 152.326 126.991 1.00 20.44 ?  176 ASN A ND2   1 
ATOM   1457  N  N     . ASP A 1 177 ? 144.212 147.925 128.517 1.00 23.65 ?  177 ASP A N     1 
ATOM   1458  C  CA    . ASP A 1 177 ? 144.554 147.005 129.601 1.00 20.06 ?  177 ASP A CA    1 
ATOM   1459  C  C     . ASP A 1 177 ? 144.051 147.570 130.928 1.00 24.85 ?  177 ASP A C     1 
ATOM   1460  O  O     . ASP A 1 177 ? 144.807 148.092 131.752 1.00 35.39 ?  177 ASP A O     1 
ATOM   1461  C  CB    . ASP A 1 177 ? 146.055 146.756 129.630 1.00 19.80 ?  177 ASP A CB    1 
ATOM   1462  C  CG    . ASP A 1 177 ? 146.440 145.644 130.577 1.00 25.30 ?  177 ASP A CG    1 
ATOM   1463  O  OD1   . ASP A 1 177 ? 145.725 144.621 130.619 1.00 28.44 ?  177 ASP A OD1   1 
ATOM   1464  O  OD2   . ASP A 1 177 ? 147.461 145.792 131.279 1.00 31.09 -1 177 ASP A OD2   1 
ATOM   1465  N  N     . SER A 1 178 ? 142.742 147.456 131.134 1.00 20.57 ?  178 SER A N     1 
ATOM   1466  C  CA    . SER A 1 178 ? 142.128 147.866 132.388 1.00 17.37 ?  178 SER A CA    1 
ATOM   1467  C  C     . SER A 1 178 ? 140.784 147.170 132.525 1.00 17.74 ?  178 SER A C     1 
ATOM   1468  O  O     . SER A 1 178 ? 140.188 146.732 131.538 1.00 27.43 ?  178 SER A O     1 
ATOM   1469  C  CB    . SER A 1 178 ? 141.960 149.388 132.465 1.00 16.60 ?  178 SER A CB    1 
ATOM   1470  O  OG    . SER A 1 178 ? 140.694 149.788 131.977 1.00 20.62 ?  178 SER A OG    1 
ATOM   1471  N  N     . LEU A 1 179 ? 140.316 147.068 133.771 1.00 22.74 ?  179 LEU A N     1 
ATOM   1472  C  CA    . LEU A 1 179 ? 139.003 146.479 134.015 1.00 19.48 ?  179 LEU A CA    1 
ATOM   1473  C  C     . LEU A 1 179 ? 137.891 147.373 133.484 1.00 18.74 ?  179 LEU A C     1 
ATOM   1474  O  O     . LEU A 1 179 ? 136.892 146.880 132.951 1.00 22.22 ?  179 LEU A O     1 
ATOM   1475  C  CB    . LEU A 1 179 ? 138.809 146.217 135.508 1.00 26.25 ?  179 LEU A CB    1 
ATOM   1476  C  CG    . LEU A 1 179 ? 137.585 145.369 135.859 1.00 18.81 ?  179 LEU A CG    1 
ATOM   1477  C  CD1   . LEU A 1 179 ? 137.829 143.910 135.508 1.00 21.68 ?  179 LEU A CD1   1 
ATOM   1478  C  CD2   . LEU A 1 179 ? 137.222 145.521 137.325 1.00 18.45 ?  179 LEU A CD2   1 
ATOM   1479  N  N     . ASN A 1 180 ? 138.045 148.692 133.628 1.00 21.73 ?  180 ASN A N     1 
ATOM   1480  C  CA    . ASN A 1 180 ? 137.071 149.618 133.061 1.00 19.79 ?  180 ASN A CA    1 
ATOM   1481  C  C     . ASN A 1 180 ? 136.995 149.469 131.548 1.00 20.72 ?  180 ASN A C     1 
ATOM   1482  O  O     . ASN A 1 180 ? 135.901 149.430 130.972 1.00 24.18 ?  180 ASN A O     1 
ATOM   1483  C  CB    . ASN A 1 180 ? 137.433 151.054 133.436 1.00 21.19 ?  180 ASN A CB    1 
ATOM   1484  C  CG    . ASN A 1 180 ? 137.005 151.417 134.840 1.00 26.79 ?  180 ASN A CG    1 
ATOM   1485  O  OD1   . ASN A 1 180 ? 136.026 150.884 135.362 1.00 33.12 ?  180 ASN A OD1   1 
ATOM   1486  N  ND2   . ASN A 1 180 ? 137.739 152.330 135.462 1.00 26.38 ?  180 ASN A ND2   1 
ATOM   1487  N  N     . ASP A 1 181 ? 138.151 149.369 130.891 1.00 21.75 ?  181 ASP A N     1 
ATOM   1488  C  CA    . ASP A 1 181 ? 138.170 149.222 129.441 1.00 12.47 ?  181 ASP A CA    1 
ATOM   1489  C  C     . ASP A 1 181 ? 137.617 147.869 129.012 1.00 18.69 ?  181 ASP A C     1 
ATOM   1490  O  O     . ASP A 1 181 ? 136.940 147.772 127.987 1.00 26.03 ?  181 ASP A O     1 
ATOM   1491  C  CB    . ASP A 1 181 ? 139.590 149.420 128.915 1.00 20.67 ?  181 ASP A CB    1 
ATOM   1492  C  CG    . ASP A 1 181 ? 140.075 150.844 129.082 1.00 28.75 ?  181 ASP A CG    1 
ATOM   1493  O  OD1   . ASP A 1 181 ? 139.498 151.745 128.443 1.00 31.69 ?  181 ASP A OD1   1 
ATOM   1494  O  OD2   . ASP A 1 181 ? 141.035 151.063 129.850 1.00 29.88 -1 181 ASP A OD2   1 
ATOM   1495  N  N     . ILE A 1 182 ? 137.885 146.816 129.783 1.00 20.59 ?  182 ILE A N     1 
ATOM   1496  C  CA    . ILE A 1 182 ? 137.346 145.500 129.452 1.00 17.82 ?  182 ILE A CA    1 
ATOM   1497  C  C     . ILE A 1 182 ? 135.827 145.492 129.582 1.00 19.62 ?  182 ILE A C     1 
ATOM   1498  O  O     . ILE A 1 182 ? 135.116 144.964 128.716 1.00 25.76 ?  182 ILE A O     1 
ATOM   1499  C  CB    . ILE A 1 182 ? 138.004 144.422 130.332 1.00 18.58 ?  182 ILE A CB    1 
ATOM   1500  C  CG1   . ILE A 1 182 ? 139.396 144.093 129.796 1.00 20.04 ?  182 ILE A CG1   1 
ATOM   1501  C  CG2   . ILE A 1 182 ? 137.143 143.170 130.396 1.00 21.02 ?  182 ILE A CG2   1 
ATOM   1502  C  CD1   . ILE A 1 182 ? 140.252 143.336 130.766 1.00 21.69 ?  182 ILE A CD1   1 
ATOM   1503  N  N     . SER A 1 183 ? 135.303 146.079 130.660 1.00 20.91 ?  183 SER A N     1 
ATOM   1504  C  CA    . SER A 1 183 ? 133.856 146.154 130.831 1.00 19.31 ?  183 SER A CA    1 
ATOM   1505  C  C     . SER A 1 183 ? 133.214 147.005 129.744 1.00 23.27 ?  183 SER A C     1 
ATOM   1506  O  O     . SER A 1 183 ? 132.146 146.661 129.225 1.00 25.87 ?  183 SER A O     1 
ATOM   1507  C  CB    . SER A 1 183 ? 133.521 146.704 132.216 1.00 19.40 ?  183 SER A CB    1 
ATOM   1508  O  OG    . SER A 1 183 ? 133.970 148.039 132.356 1.00 29.39 ?  183 SER A OG    1 
ATOM   1509  N  N     . ARG A 1 184 ? 133.854 148.120 129.382 1.00 25.20 ?  184 ARG A N     1 
ATOM   1510  C  CA    . ARG A 1 184 ? 133.333 148.949 128.301 1.00 19.46 ?  184 ARG A CA    1 
ATOM   1511  C  C     . ARG A 1 184 ? 133.366 148.208 126.972 1.00 23.51 ?  184 ARG A C     1 
ATOM   1512  O  O     . ARG A 1 184 ? 132.455 148.355 126.155 1.00 28.66 ?  184 ARG A O     1 
ATOM   1513  C  CB    . ARG A 1 184 ? 134.120 150.254 128.212 1.00 15.25 ?  184 ARG A CB    1 
ATOM   1514  C  CG    . ARG A 1 184 ? 133.612 151.205 127.145 1.00 24.35 ?  184 ARG A CG    1 
ATOM   1515  C  CD    . ARG A 1 184 ? 132.133 151.489 127.313 1.00 24.56 ?  184 ARG A CD    1 
ATOM   1516  N  NE    . ARG A 1 184 ? 131.891 152.553 128.279 1.00 32.26 ?  184 ARG A NE    1 
ATOM   1517  C  CZ    . ARG A 1 184 ? 130.794 152.659 129.014 1.00 29.75 ?  184 ARG A CZ    1 
ATOM   1518  N  NH1   . ARG A 1 184 ? 129.813 151.776 128.924 1.00 25.23 1  184 ARG A NH1   1 
ATOM   1519  N  NH2   . ARG A 1 184 ? 130.677 153.677 129.862 1.00 26.89 ?  184 ARG A NH2   1 
ATOM   1520  N  N     . ALA A 1 185 ? 134.410 147.411 126.733 1.00 24.15 ?  185 ALA A N     1 
ATOM   1521  C  CA    . ALA A 1 185 ? 134.476 146.617 125.513 1.00 16.96 ?  185 ALA A CA    1 
ATOM   1522  C  C     . ALA A 1 185 ? 133.361 145.583 125.470 1.00 20.26 ?  185 ALA A C     1 
ATOM   1523  O  O     . ALA A 1 185 ? 132.748 145.367 124.421 1.00 23.61 ?  185 ALA A O     1 
ATOM   1524  C  CB    . ALA A 1 185 ? 135.840 145.938 125.401 1.00 16.52 ?  185 ALA A CB    1 
ATOM   1525  N  N     . ILE A 1 186 ? 133.082 144.937 126.605 1.00 23.68 ?  186 ILE A N     1 
ATOM   1526  C  CA    . ILE A 1 186 ? 131.973 143.986 126.670 1.00 20.75 ?  186 ILE A CA    1 
ATOM   1527  C  C     . ILE A 1 186 ? 130.654 144.691 126.374 1.00 20.06 ?  186 ILE A C     1 
ATOM   1528  O  O     . ILE A 1 186 ? 129.818 144.198 125.603 1.00 27.89 ?  186 ILE A O     1 
ATOM   1529  C  CB    . ILE A 1 186 ? 131.943 143.289 128.042 1.00 26.09 ?  186 ILE A CB    1 
ATOM   1530  C  CG1   . ILE A 1 186 ? 133.159 142.377 128.211 1.00 24.61 ?  186 ILE A CG1   1 
ATOM   1531  C  CG2   . ILE A 1 186 ? 130.655 142.499 128.220 1.00 24.04 ?  186 ILE A CG2   1 
ATOM   1532  C  CD1   . ILE A 1 186 ? 133.517 142.111 129.654 1.00 23.67 ?  186 ILE A CD1   1 
ATOM   1533  N  N     . ASP A 1 187 ? 130.453 145.864 126.979 1.00 21.52 ?  187 ASP A N     1 
ATOM   1534  C  CA    . ASP A 1 187 ? 129.224 146.620 126.759 1.00 19.03 ?  187 ASP A CA    1 
ATOM   1535  C  C     . ASP A 1 187 ? 129.073 147.018 125.294 1.00 23.82 ?  187 ASP A C     1 
ATOM   1536  O  O     . ASP A 1 187 ? 127.996 146.871 124.708 1.00 28.16 ?  187 ASP A O     1 
ATOM   1537  C  CB    . ASP A 1 187 ? 129.206 147.857 127.655 1.00 17.96 ?  187 ASP A CB    1 
ATOM   1538  C  CG    . ASP A 1 187 ? 128.267 148.932 127.148 1.00 28.50 ?  187 ASP A CG    1 
ATOM   1539  O  OD1   . ASP A 1 187 ? 127.068 148.637 126.958 1.00 30.94 ?  187 ASP A OD1   1 
ATOM   1540  O  OD2   . ASP A 1 187 ? 128.728 150.072 126.935 1.00 34.22 -1 187 ASP A OD2   1 
ATOM   1541  N  N     . ILE A 1 188 ? 130.149 147.527 124.689 1.00 22.45 ?  188 ILE A N     1 
ATOM   1542  C  CA    . ILE A 1 188 ? 130.088 147.969 123.300 1.00 21.59 ?  188 ILE A CA    1 
ATOM   1543  C  C     . ILE A 1 188 ? 129.868 146.785 122.370 1.00 23.18 ?  188 ILE A C     1 
ATOM   1544  O  O     . ILE A 1 188 ? 129.136 146.886 121.381 1.00 27.73 ?  188 ILE A O     1 
ATOM   1545  C  CB    . ILE A 1 188 ? 131.361 148.756 122.933 1.00 22.36 ?  188 ILE A CB    1 
ATOM   1546  C  CG1   . ILE A 1 188 ? 131.452 150.044 123.751 1.00 22.66 ?  188 ILE A CG1   1 
ATOM   1547  C  CG2   . ILE A 1 188 ? 131.372 149.104 121.461 1.00 21.91 ?  188 ILE A CG2   1 
ATOM   1548  C  CD1   . ILE A 1 188 ? 132.754 150.787 123.566 1.00 22.60 ?  188 ILE A CD1   1 
ATOM   1549  N  N     . SER A 1 189 ? 130.496 145.645 122.667 1.00 18.21 ?  189 SER A N     1 
ATOM   1550  C  CA    . SER A 1 189 ? 130.262 144.444 121.875 1.00 12.23 ?  189 SER A CA    1 
ATOM   1551  C  C     . SER A 1 189 ? 128.803 144.023 121.944 1.00 19.79 ?  189 SER A C     1 
ATOM   1552  O  O     . SER A 1 189 ? 128.205 143.660 120.925 1.00 28.18 ?  189 SER A O     1 
ATOM   1553  C  CB    . SER A 1 189 ? 131.169 143.314 122.360 1.00 20.99 ?  189 SER A CB    1 
ATOM   1554  O  OG    . SER A 1 189 ? 132.525 143.716 122.372 1.00 27.35 ?  189 SER A OG    1 
ATOM   1555  N  N     . MET A 1 190 ? 128.211 144.076 123.139 1.00 25.42 ?  190 MET A N     1 
ATOM   1556  C  CA    . MET A 1 190 ? 126.797 143.745 123.278 1.00 22.32 ?  190 MET A CA    1 
ATOM   1557  C  C     . MET A 1 190 ? 125.920 144.718 122.500 1.00 18.68 ?  190 MET A C     1 
ATOM   1558  O  O     . MET A 1 190 ? 124.964 144.308 121.832 1.00 22.42 ?  190 MET A O     1 
ATOM   1559  C  CB    . MET A 1 190 ? 126.406 143.747 124.753 1.00 25.23 ?  190 MET A CB    1 
ATOM   1560  C  CG    . MET A 1 190 ? 126.749 142.472 125.486 1.00 18.79 ?  190 MET A CG    1 
ATOM   1561  S  SD    . MET A 1 190 ? 126.793 142.740 127.263 1.00 37.97 ?  190 MET A SD    1 
ATOM   1562  C  CE    . MET A 1 190 ? 125.580 141.544 127.790 1.00 27.75 ?  190 MET A CE    1 
ATOM   1563  N  N     . GLN A 1 191 ? 126.231 146.014 122.573 1.00 21.05 ?  191 GLN A N     1 
ATOM   1564  C  CA    . GLN A 1 191 ? 125.421 147.012 121.882 1.00 22.57 ?  191 GLN A CA    1 
ATOM   1565  C  C     . GLN A 1 191 ? 125.522 146.864 120.370 1.00 24.99 ?  191 GLN A C     1 
ATOM   1566  O  O     . GLN A 1 191 ? 124.531 147.049 119.655 1.00 30.62 ?  191 GLN A O     1 
ATOM   1567  C  CB    . GLN A 1 191 ? 125.836 148.421 122.307 1.00 22.31 ?  191 GLN A CB    1 
ATOM   1568  C  CG    . GLN A 1 191 ? 125.695 148.700 123.792 1.00 21.20 ?  191 GLN A CG    1 
ATOM   1569  C  CD    . GLN A 1 191 ? 124.252 148.763 124.246 1.00 27.26 ?  191 GLN A CD    1 
ATOM   1570  O  OE1   . GLN A 1 191 ? 123.343 148.980 123.444 1.00 28.28 ?  191 GLN A OE1   1 
ATOM   1571  N  NE2   . GLN A 1 191 ? 124.033 148.579 125.542 1.00 25.51 ?  191 GLN A NE2   1 
ATOM   1572  N  N     . LEU A 1 192 ? 126.712 146.541 119.861 1.00 24.46 ?  192 LEU A N     1 
ATOM   1573  C  CA    . LEU A 1 192 ? 126.887 146.399 118.422 1.00 19.42 ?  192 LEU A CA    1 
ATOM   1574  C  C     . LEU A 1 192 ? 126.320 145.085 117.903 1.00 23.47 ?  192 LEU A C     1 
ATOM   1575  O  O     . LEU A 1 192 ? 125.830 145.037 116.769 1.00 33.19 ?  192 LEU A O     1 
ATOM   1576  C  CB    . LEU A 1 192 ? 128.365 146.523 118.056 1.00 20.09 ?  192 LEU A CB    1 
ATOM   1577  C  CG    . LEU A 1 192 ? 129.022 147.872 118.353 1.00 18.88 ?  192 LEU A CG    1 
ATOM   1578  C  CD1   . LEU A 1 192 ? 130.531 147.761 118.236 1.00 18.46 ?  192 LEU A CD1   1 
ATOM   1579  C  CD2   . LEU A 1 192 ? 128.483 148.962 117.443 1.00 16.55 ?  192 LEU A CD2   1 
ATOM   1580  N  N     . SER A 1 193 ? 126.378 144.014 118.698 1.00 19.30 ?  193 SER A N     1 
ATOM   1581  C  CA    . SER A 1 193 ? 125.692 142.784 118.323 1.00 21.10 ?  193 SER A CA    1 
ATOM   1582  C  C     . SER A 1 193 ? 124.182 142.973 118.356 1.00 30.66 ?  193 SER A C     1 
ATOM   1583  O  O     . SER A 1 193 ? 123.455 142.367 117.561 1.00 35.65 ?  193 SER A O     1 
ATOM   1584  C  CB    . SER A 1 193 ? 126.115 141.643 119.245 1.00 23.76 ?  193 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 193 ? 127.518 141.642 119.434 1.00 29.24 ?  193 SER A OG    1 
ATOM   1586  N  N     . LYS A 1 194 ? 123.696 143.807 119.277 1.00 28.35 ?  194 LYS A N     1 
ATOM   1587  C  CA    . LYS A 1 194 ? 122.282 144.166 119.292 1.00 26.81 ?  194 LYS A CA    1 
ATOM   1588  C  C     . LYS A 1 194 ? 121.886 144.869 118.000 1.00 33.98 ?  194 LYS A C     1 
ATOM   1589  O  O     . LYS A 1 194 ? 120.797 144.634 117.464 1.00 37.52 ?  194 LYS A O     1 
ATOM   1590  C  CB    . LYS A 1 194 ? 121.989 145.047 120.506 1.00 25.61 ?  194 LYS A CB    1 
ATOM   1591  C  CG    . LYS A 1 194 ? 120.632 145.720 120.488 1.00 31.84 ?  194 LYS A CG    1 
ATOM   1592  C  CD    . LYS A 1 194 ? 120.497 146.714 121.629 1.00 34.30 ?  194 LYS A CD    1 
ATOM   1593  C  CE    . LYS A 1 194 ? 119.064 147.195 121.773 1.00 30.41 ?  194 LYS A CE    1 
ATOM   1594  N  NZ    . LYS A 1 194 ? 118.927 148.210 122.851 1.00 33.10 1  194 LYS A NZ    1 
ATOM   1595  N  N     . LEU A 1 195 ? 122.760 145.734 117.485 1.00 34.63 ?  195 LEU A N     1 
ATOM   1596  C  CA    . LEU A 1 195 ? 122.526 146.396 116.208 1.00 32.10 ?  195 LEU A CA    1 
ATOM   1597  C  C     . LEU A 1 195 ? 122.656 145.448 115.023 1.00 34.27 ?  195 LEU A C     1 
ATOM   1598  O  O     . LEU A 1 195 ? 122.329 145.844 113.899 1.00 37.81 ?  195 LEU A O     1 
ATOM   1599  C  CB    . LEU A 1 195 ? 123.497 147.565 116.038 1.00 32.31 ?  195 LEU A CB    1 
ATOM   1600  C  CG    . LEU A 1 195 ? 123.313 148.741 116.998 1.00 35.80 ?  195 LEU A CG    1 
ATOM   1601  C  CD1   . LEU A 1 195 ? 124.417 149.766 116.802 1.00 35.62 ?  195 LEU A CD1   1 
ATOM   1602  C  CD2   . LEU A 1 195 ? 121.946 149.374 116.808 1.00 33.64 ?  195 LEU A CD2   1 
ATOM   1603  N  N     . GLY A 1 196 ? 123.127 144.225 115.242 1.00 34.97 ?  196 GLY A N     1 
ATOM   1604  C  CA    . GLY A 1 196 ? 123.282 143.266 114.172 1.00 33.07 ?  196 GLY A CA    1 
ATOM   1605  C  C     . GLY A 1 196 ? 124.659 143.201 113.556 1.00 37.29 ?  196 GLY A C     1 
ATOM   1606  O  O     . GLY A 1 196 ? 124.817 142.574 112.502 1.00 40.02 ?  196 GLY A O     1 
ATOM   1607  N  N     . GLY A 1 197 ? 125.658 143.819 114.175 1.00 34.21 ?  197 GLY A N     1 
ATOM   1608  C  CA    . GLY A 1 197 ? 126.986 143.860 113.605 1.00 24.52 ?  197 GLY A CA    1 
ATOM   1609  C  C     . GLY A 1 197 ? 127.930 142.822 114.183 1.00 23.86 ?  197 GLY A C     1 
ATOM   1610  O  O     . GLY A 1 197 ? 127.815 142.418 115.336 1.00 33.65 ?  197 GLY A O     1 
ATOM   1611  N  N     . GLY A 1 198 ? 128.873 142.388 113.348 1.00 17.12 ?  198 GLY A N     1 
ATOM   1612  C  CA    . GLY A 1 198 ? 129.946 141.525 113.811 1.00 16.73 ?  198 GLY A CA    1 
ATOM   1613  C  C     . GLY A 1 198 ? 131.054 142.362 114.418 1.00 17.59 ?  198 GLY A C     1 
ATOM   1614  O  O     . GLY A 1 198 ? 131.517 143.334 113.813 1.00 18.46 ?  198 GLY A O     1 
ATOM   1615  N  N     . VAL A 1 199 ? 131.483 141.985 115.618 1.00 21.76 ?  199 VAL A N     1 
ATOM   1616  C  CA    . VAL A 1 199 ? 132.398 142.788 116.418 1.00 13.39 ?  199 VAL A CA    1 
ATOM   1617  C  C     . VAL A 1 199 ? 133.724 142.057 116.536 1.00 11.65 ?  199 VAL A C     1 
ATOM   1618  O  O     . VAL A 1 199 ? 133.763 140.887 116.930 1.00 16.01 ?  199 VAL A O     1 
ATOM   1619  C  CB    . VAL A 1 199 ? 131.812 143.082 117.809 1.00 13.59 ?  199 VAL A CB    1 
ATOM   1620  C  CG1   . VAL A 1 199 ? 132.740 143.991 118.589 1.00 15.15 ?  199 VAL A CG1   1 
ATOM   1621  C  CG2   . VAL A 1 199 ? 130.436 143.694 117.678 1.00 18.65 ?  199 VAL A CG2   1 
ATOM   1622  N  N     . SER A 1 200 ? 134.807 142.749 116.203 1.00 15.20 ?  200 SER A N     1 
ATOM   1623  C  CA    . SER A 1 200 ? 136.160 142.245 116.379 1.00 3.66  ?  200 SER A CA    1 
ATOM   1624  C  C     . SER A 1 200 ? 136.857 143.079 117.442 1.00 11.73 ?  200 SER A C     1 
ATOM   1625  O  O     . SER A 1 200 ? 136.787 144.312 117.413 1.00 21.37 ?  200 SER A O     1 
ATOM   1626  C  CB    . SER A 1 200 ? 136.940 142.291 115.067 1.00 9.17  ?  200 SER A CB    1 
ATOM   1627  O  OG    . SER A 1 200 ? 138.145 141.554 115.163 1.00 16.25 ?  200 SER A OG    1 
ATOM   1628  N  N     . LEU A 1 201 ? 137.517 142.410 118.381 1.00 16.66 ?  201 LEU A N     1 
ATOM   1629  C  CA    . LEU A 1 201 ? 138.189 143.068 119.490 1.00 9.22  ?  201 LEU A CA    1 
ATOM   1630  C  C     . LEU A 1 201 ? 139.666 142.711 119.474 1.00 7.69  ?  201 LEU A C     1 
ATOM   1631  O  O     . LEU A 1 201 ? 140.024 141.538 119.327 1.00 9.39  ?  201 LEU A O     1 
ATOM   1632  C  CB    . LEU A 1 201 ? 137.563 142.666 120.829 1.00 16.07 ?  201 LEU A CB    1 
ATOM   1633  C  CG    . LEU A 1 201 ? 136.089 143.027 121.010 1.00 14.03 ?  201 LEU A CG    1 
ATOM   1634  C  CD1   . LEU A 1 201 ? 135.210 141.806 120.799 1.00 14.27 ?  201 LEU A CD1   1 
ATOM   1635  C  CD2   . LEU A 1 201 ? 135.849 143.636 122.379 1.00 15.95 ?  201 LEU A CD2   1 
ATOM   1636  N  N     . ASN A 1 202 ? 140.515 143.721 119.632 1.00 13.18 ?  202 ASN A N     1 
ATOM   1637  C  CA    . ASN A 1 202 ? 141.952 143.522 119.756 1.00 7.05  ?  202 ASN A CA    1 
ATOM   1638  C  C     . ASN A 1 202 ? 142.289 143.305 121.225 1.00 13.85 ?  202 ASN A C     1 
ATOM   1639  O  O     . ASN A 1 202 ? 142.021 144.172 122.063 1.00 25.93 ?  202 ASN A O     1 
ATOM   1640  C  CB    . ASN A 1 202 ? 142.711 144.723 119.197 1.00 8.39  ?  202 ASN A CB    1 
ATOM   1641  C  CG    . ASN A 1 202 ? 144.196 144.463 119.060 1.00 11.78 ?  202 ASN A CG    1 
ATOM   1642  O  OD1   . ASN A 1 202 ? 144.627 143.320 118.915 1.00 17.73 ?  202 ASN A OD1   1 
ATOM   1643  N  ND2   . ASN A 1 202 ? 144.987 145.527 119.103 1.00 14.87 ?  202 ASN A ND2   1 
ATOM   1644  N  N     . LEU A 1 203 ? 142.873 142.150 121.537 1.00 8.33  ?  203 LEU A N     1 
ATOM   1645  C  CA    . LEU A 1 203 ? 143.210 141.795 122.909 1.00 9.55  ?  203 LEU A CA    1 
ATOM   1646  C  C     . LEU A 1 203 ? 144.709 141.823 123.170 1.00 12.58 ?  203 LEU A C     1 
ATOM   1647  O  O     . LEU A 1 203 ? 145.153 141.357 124.224 1.00 14.59 ?  203 LEU A O     1 
ATOM   1648  C  CB    . LEU A 1 203 ? 142.642 140.417 123.252 1.00 15.42 ?  203 LEU A CB    1 
ATOM   1649  C  CG    . LEU A 1 203 ? 141.126 140.250 123.132 1.00 15.72 ?  203 LEU A CG    1 
ATOM   1650  C  CD1   . LEU A 1 203 ? 140.678 139.011 123.880 1.00 14.37 ?  203 LEU A CD1   1 
ATOM   1651  C  CD2   . LEU A 1 203 ? 140.389 141.479 123.641 1.00 12.05 ?  203 LEU A CD2   1 
ATOM   1652  N  N     . SER A 1 204 ? 145.499 142.365 122.240 1.00 17.27 ?  204 SER A N     1 
ATOM   1653  C  CA    . SER A 1 204 ? 146.948 142.365 122.399 1.00 15.28 ?  204 SER A CA    1 
ATOM   1654  C  C     . SER A 1 204 ? 147.411 143.328 123.484 1.00 17.32 ?  204 SER A C     1 
ATOM   1655  O  O     . SER A 1 204 ? 148.424 143.068 124.142 1.00 27.44 ?  204 SER A O     1 
ATOM   1656  C  CB    . SER A 1 204 ? 147.619 142.713 121.071 1.00 12.39 ?  204 SER A CB    1 
ATOM   1657  O  OG    . SER A 1 204 ? 147.163 141.862 120.035 1.00 20.84 ?  204 SER A OG    1 
ATOM   1658  N  N     . LYS A 1 205 ? 146.695 144.435 123.685 1.00 18.64 ?  205 LYS A N     1 
ATOM   1659  C  CA    . LYS A 1 205 ? 147.065 145.372 124.738 1.00 21.79 ?  205 LYS A CA    1 
ATOM   1660  C  C     . LYS A 1 205 ? 146.790 144.816 126.127 1.00 22.02 ?  205 LYS A C     1 
ATOM   1661  O  O     . LYS A 1 205 ? 147.390 145.286 127.099 1.00 28.08 ?  205 LYS A O     1 
ATOM   1662  C  CB    . LYS A 1 205 ? 146.323 146.694 124.552 1.00 22.28 ?  205 LYS A CB    1 
ATOM   1663  C  CG    . LYS A 1 205 ? 146.773 147.472 123.337 1.00 21.54 ?  205 LYS A CG    1 
ATOM   1664  C  CD    . LYS A 1 205 ? 146.040 148.790 123.224 1.00 25.34 ?  205 LYS A CD    1 
ATOM   1665  C  CE    . LYS A 1 205 ? 146.640 149.643 122.124 1.00 28.62 ?  205 LYS A CE    1 
ATOM   1666  N  NZ    . LYS A 1 205 ? 146.547 148.985 120.793 1.00 24.12 1  205 LYS A NZ    1 
ATOM   1667  N  N     . LEU A 1 206 ? 145.904 143.832 126.240 1.00 18.83 ?  206 LEU A N     1 
ATOM   1668  C  CA    . LEU A 1 206 ? 145.609 143.228 127.530 1.00 12.03 ?  206 LEU A CA    1 
ATOM   1669  C  C     . LEU A 1 206 ? 146.808 142.432 128.029 1.00 18.40 ?  206 LEU A C     1 
ATOM   1670  O  O     . LEU A 1 206 ? 147.434 141.684 127.275 1.00 24.65 ?  206 LEU A O     1 
ATOM   1671  C  CB    . LEU A 1 206 ? 144.387 142.322 127.417 1.00 16.39 ?  206 LEU A CB    1 
ATOM   1672  C  CG    . LEU A 1 206 ? 143.073 143.032 127.094 1.00 21.56 ?  206 LEU A CG    1 
ATOM   1673  C  CD1   . LEU A 1 206 ? 141.943 142.029 127.007 1.00 19.17 ?  206 LEU A CD1   1 
ATOM   1674  C  CD2   . LEU A 1 206 ? 142.771 144.097 128.131 1.00 21.52 ?  206 LEU A CD2   1 
ATOM   1675  N  N     . ARG A 1 207 ? 147.124 142.597 129.309 1.00 25.76 ?  207 ARG A N     1 
ATOM   1676  C  CA    . ARG A 1 207 ? 148.271 141.911 129.880 1.00 22.21 ?  207 ARG A CA    1 
ATOM   1677  C  C     . ARG A 1 207 ? 147.987 140.420 130.031 1.00 27.34 ?  207 ARG A C     1 
ATOM   1678  O  O     . ARG A 1 207 ? 146.844 139.994 130.208 1.00 33.02 ?  207 ARG A O     1 
ATOM   1679  C  CB    . ARG A 1 207 ? 148.651 142.532 131.224 1.00 25.46 ?  207 ARG A CB    1 
ATOM   1680  C  CG    . ARG A 1 207 ? 147.604 142.426 132.310 1.00 20.93 ?  207 ARG A CG    1 
ATOM   1681  C  CD    . ARG A 1 207 ? 148.009 143.250 133.520 1.00 21.04 ?  207 ARG A CD    1 
ATOM   1682  N  NE    . ARG A 1 207 ? 147.631 144.650 133.372 1.00 29.59 ?  207 ARG A NE    1 
ATOM   1683  C  CZ    . ARG A 1 207 ? 147.672 145.545 134.349 1.00 23.85 ?  207 ARG A CZ    1 
ATOM   1684  N  NH1   . ARG A 1 207 ? 148.088 145.224 135.562 1.00 28.40 1  207 ARG A NH1   1 
ATOM   1685  N  NH2   . ARG A 1 207 ? 147.283 146.792 134.102 1.00 19.28 ?  207 ARG A NH2   1 
ATOM   1686  N  N     . ALA A 1 208 ? 149.051 139.624 129.954 1.00 28.20 ?  208 ALA A N     1 
ATOM   1687  C  CA    . ALA A 1 208 ? 148.931 138.178 129.877 1.00 25.93 ?  208 ALA A CA    1 
ATOM   1688  C  C     . ALA A 1 208 ? 148.573 137.590 131.240 1.00 31.00 ?  208 ALA A C     1 
ATOM   1689  O  O     . ALA A 1 208 ? 148.444 138.295 132.243 1.00 33.88 ?  208 ALA A O     1 
ATOM   1690  C  CB    . ALA A 1 208 ? 150.222 137.568 129.337 1.00 27.47 ?  208 ALA A CB    1 
ATOM   1691  N  N     . LYS A 1 209 ? 148.398 136.273 131.271 1.00 30.80 ?  209 LYS A N     1 
ATOM   1692  C  CA    . LYS A 1 209 ? 148.070 135.590 132.515 1.00 25.81 ?  209 LYS A CA    1 
ATOM   1693  C  C     . LYS A 1 209 ? 149.296 135.531 133.418 1.00 33.73 ?  209 LYS A C     1 
ATOM   1694  O  O     . LYS A 1 209 ? 150.405 135.235 132.960 1.00 34.47 ?  209 LYS A O     1 
ATOM   1695  C  CB    . LYS A 1 209 ? 147.550 134.184 132.231 1.00 28.85 ?  209 LYS A CB    1 
ATOM   1696  C  CG    . LYS A 1 209 ? 147.095 133.432 133.469 1.00 32.40 ?  209 LYS A CG    1 
ATOM   1697  C  CD    . LYS A 1 209 ? 147.023 131.934 133.230 1.00 32.56 ?  209 LYS A CD    1 
ATOM   1698  C  CE    . LYS A 1 209 ? 148.163 131.445 132.352 1.00 35.58 ?  209 LYS A CE    1 
ATOM   1699  N  NZ    . LYS A 1 209 ? 148.044 129.992 132.054 1.00 35.06 1  209 LYS A NZ    1 
ATOM   1700  N  N     . GLY A 1 210 ? 149.093 135.802 134.704 1.00 37.65 ?  210 GLY A N     1 
ATOM   1701  C  CA    . GLY A 1 210 ? 150.189 135.837 135.647 1.00 32.83 ?  210 GLY A CA    1 
ATOM   1702  C  C     . GLY A 1 210 ? 150.866 137.178 135.793 1.00 35.30 ?  210 GLY A C     1 
ATOM   1703  O  O     . GLY A 1 210 ? 151.996 137.232 136.291 1.00 40.60 ?  210 GLY A O     1 
ATOM   1704  N  N     . GLU A 1 211 ? 150.221 138.260 135.371 1.00 33.92 ?  211 GLU A N     1 
ATOM   1705  C  CA    . GLU A 1 211 ? 150.765 139.601 135.506 1.00 31.71 ?  211 GLU A CA    1 
ATOM   1706  C  C     . GLU A 1 211 ? 150.216 140.271 136.761 1.00 34.75 ?  211 GLU A C     1 
ATOM   1707  O  O     . GLU A 1 211 ? 149.323 139.756 137.437 1.00 36.62 ?  211 GLU A O     1 
ATOM   1708  C  CB    . GLU A 1 211 ? 150.451 140.437 134.263 1.00 30.32 ?  211 GLU A CB    1 
ATOM   1709  C  CG    . GLU A 1 211 ? 151.128 139.925 133.009 1.00 33.60 ?  211 GLU A CG    1 
ATOM   1710  C  CD    . GLU A 1 211 ? 151.896 141.004 132.278 1.00 36.43 ?  211 GLU A CD    1 
ATOM   1711  O  OE1   . GLU A 1 211 ? 152.887 141.513 132.841 1.00 39.07 ?  211 GLU A OE1   1 
ATOM   1712  O  OE2   . GLU A 1 211 ? 151.522 141.334 131.134 1.00 30.88 -1 211 GLU A OE2   1 
ATOM   1713  N  N     . ALA A 1 212 ? 150.766 141.442 137.067 1.00 33.78 ?  212 ALA A N     1 
ATOM   1714  C  CA    . ALA A 1 212 ? 150.462 142.133 138.311 1.00 33.97 ?  212 ALA A CA    1 
ATOM   1715  C  C     . ALA A 1 212 ? 149.327 143.131 138.128 1.00 39.38 ?  212 ALA A C     1 
ATOM   1716  O  O     . ALA A 1 212 ? 149.273 143.858 137.132 1.00 41.12 ?  212 ALA A O     1 
ATOM   1717  C  CB    . ALA A 1 212 ? 151.702 142.850 138.842 1.00 35.82 ?  212 ALA A CB    1 
ATOM   1718  N  N     . ILE A 1 213 ? 148.418 143.157 139.101 1.00 32.09 ?  213 ILE A N     1 
ATOM   1719  C  CA    . ILE A 1 213 ? 147.363 144.160 139.188 1.00 34.78 ?  213 ILE A CA    1 
ATOM   1720  C  C     . ILE A 1 213 ? 147.600 144.943 140.471 1.00 36.14 ?  213 ILE A C     1 
ATOM   1721  O  O     . ILE A 1 213 ? 147.473 144.392 141.572 1.00 40.58 ?  213 ILE A O     1 
ATOM   1722  C  CB    . ILE A 1 213 ? 145.962 143.534 139.175 1.00 34.49 ?  213 ILE A CB    1 
ATOM   1723  C  CG1   . ILE A 1 213 ? 145.831 142.529 138.030 1.00 34.39 ?  213 ILE A CG1   1 
ATOM   1724  C  CG2   . ILE A 1 213 ? 144.899 144.614 139.064 1.00 29.79 ?  213 ILE A CG2   1 
ATOM   1725  C  CD1   . ILE A 1 213 ? 144.611 141.644 138.138 1.00 30.50 ?  213 ILE A CD1   1 
ATOM   1726  N  N     . LYS A 1 214 ? 147.933 146.228 140.332 1.00 41.13 ?  214 LYS A N     1 
ATOM   1727  C  CA    . LYS A 1 214 ? 148.267 147.087 141.470 1.00 40.28 ?  214 LYS A CA    1 
ATOM   1728  C  C     . LYS A 1 214 ? 149.386 146.479 142.311 1.00 46.68 ?  214 LYS A C     1 
ATOM   1729  O  O     . LYS A 1 214 ? 149.330 146.463 143.543 1.00 49.91 ?  214 LYS A O     1 
ATOM   1730  C  CB    . LYS A 1 214 ? 147.033 147.382 142.325 1.00 40.44 ?  214 LYS A CB    1 
ATOM   1731  C  CG    . LYS A 1 214 ? 146.175 148.518 141.795 1.00 40.01 ?  214 LYS A CG    1 
ATOM   1732  C  CD    . LYS A 1 214 ? 144.969 148.770 142.683 1.00 42.30 ?  214 LYS A CD    1 
ATOM   1733  C  CE    . LYS A 1 214 ? 144.267 150.063 142.297 1.00 44.11 ?  214 LYS A CE    1 
ATOM   1734  N  NZ    . LYS A 1 214 ? 143.066 150.319 143.137 1.00 42.67 1  214 LYS A NZ    1 
ATOM   1735  N  N     . ASP A 1 215 ? 150.408 145.963 141.628 1.00 47.70 ?  215 ASP A N     1 
ATOM   1736  C  CA    . ASP A 1 215 ? 151.631 145.462 142.263 1.00 49.79 ?  215 ASP A CA    1 
ATOM   1737  C  C     . ASP A 1 215 ? 151.359 144.279 143.191 1.00 48.44 ?  215 ASP A C     1 
ATOM   1738  O  O     . ASP A 1 215 ? 151.999 144.127 144.233 1.00 48.37 ?  215 ASP A O     1 
ATOM   1739  C  CB    . ASP A 1 215 ? 152.364 146.581 143.007 1.00 48.76 ?  215 ASP A CB    1 
ATOM   1740  C  CG    . ASP A 1 215 ? 152.692 147.760 142.111 1.00 52.47 ?  215 ASP A CG    1 
ATOM   1741  O  OD1   . ASP A 1 215 ? 153.084 147.531 140.948 1.00 51.00 ?  215 ASP A OD1   1 
ATOM   1742  O  OD2   . ASP A 1 215 ? 152.561 148.914 142.569 1.00 51.63 -1 215 ASP A OD2   1 
ATOM   1743  N  N     . VAL A 1 216 ? 150.405 143.431 142.815 1.00 43.69 ?  216 VAL A N     1 
ATOM   1744  C  CA    . VAL A 1 216 ? 150.233 142.117 143.424 1.00 45.86 ?  216 VAL A CA    1 
ATOM   1745  C  C     . VAL A 1 216 ? 150.446 141.079 142.329 1.00 46.94 ?  216 VAL A C     1 
ATOM   1746  O  O     . VAL A 1 216 ? 149.917 141.217 141.220 1.00 49.98 ?  216 VAL A O     1 
ATOM   1747  C  CB    . VAL A 1 216 ? 148.863 141.970 144.127 1.00 44.85 ?  216 VAL A CB    1 
ATOM   1748  C  CG1   . VAL A 1 216 ? 148.302 143.337 144.502 1.00 43.90 ?  216 VAL A CG1   1 
ATOM   1749  C  CG2   . VAL A 1 216 ? 147.858 141.173 143.303 1.00 43.37 ?  216 VAL A CG2   1 
ATOM   1750  N  N     . GLU A 1 217 ? 151.278 140.083 142.616 1.00 48.48 ?  217 GLU A N     1 
ATOM   1751  C  CA    . GLU A 1 217 ? 151.806 139.218 141.571 1.00 48.13 ?  217 GLU A CA    1 
ATOM   1752  C  C     . GLU A 1 217 ? 150.846 138.077 141.245 1.00 49.28 ?  217 GLU A C     1 
ATOM   1753  O  O     . GLU A 1 217 ? 150.018 137.668 142.064 1.00 51.39 ?  217 GLU A O     1 
ATOM   1754  C  CB    . GLU A 1 217 ? 153.166 138.652 141.982 1.00 50.28 ?  217 GLU A CB    1 
ATOM   1755  C  CG    . GLU A 1 217 ? 154.168 139.686 142.486 1.00 50.51 ?  217 GLU A CG    1 
ATOM   1756  C  CD    . GLU A 1 217 ? 154.050 141.024 141.777 1.00 52.26 ?  217 GLU A CD    1 
ATOM   1757  O  OE1   . GLU A 1 217 ? 154.610 141.162 140.670 1.00 53.56 ?  217 GLU A OE1   1 
ATOM   1758  O  OE2   . GLU A 1 217 ? 153.407 141.940 142.332 1.00 49.24 -1 217 GLU A OE2   1 
ATOM   1759  N  N     . ASN A 1 218 ? 150.980 137.562 140.019 1.00 44.02 ?  218 ASN A N     1 
ATOM   1760  C  CA    . ASN A 1 218 ? 150.221 136.402 139.542 1.00 44.04 ?  218 ASN A CA    1 
ATOM   1761  C  C     . ASN A 1 218 ? 148.717 136.613 139.698 1.00 47.82 ?  218 ASN A C     1 
ATOM   1762  O  O     . ASN A 1 218 ? 147.987 135.718 140.128 1.00 46.76 ?  218 ASN A O     1 
ATOM   1763  C  CB    . ASN A 1 218 ? 150.668 135.124 140.253 1.00 43.02 ?  218 ASN A CB    1 
ATOM   1764  C  CG    . ASN A 1 218 ? 150.718 133.927 139.324 1.00 48.15 ?  218 ASN A CG    1 
ATOM   1765  O  OD1   . ASN A 1 218 ? 151.253 134.007 138.218 1.00 50.06 ?  218 ASN A OD1   1 
ATOM   1766  N  ND2   . ASN A 1 218 ? 150.158 132.809 139.769 1.00 47.54 ?  218 ASN A ND2   1 
ATOM   1767  N  N     . ALA A 1 219 ? 148.249 137.806 139.341 1.00 38.03 ?  219 ALA A N     1 
ATOM   1768  C  CA    . ALA A 1 219 ? 146.861 138.187 139.561 1.00 33.65 ?  219 ALA A CA    1 
ATOM   1769  C  C     . ALA A 1 219 ? 146.018 138.191 138.297 1.00 35.31 ?  219 ALA A C     1 
ATOM   1770  O  O     . ALA A 1 219 ? 144.819 137.903 138.367 1.00 36.61 ?  219 ALA A O     1 
ATOM   1771  C  CB    . ALA A 1 219 ? 146.795 139.574 140.206 1.00 35.87 ?  219 ALA A CB    1 
ATOM   1772  N  N     . THR A 1 220 ? 146.606 138.510 137.148 1.00 36.45 ?  220 THR A N     1 
ATOM   1773  C  CA    . THR A 1 220 ? 145.829 138.637 135.924 1.00 30.45 ?  220 THR A CA    1 
ATOM   1774  C  C     . THR A 1 220 ? 145.388 137.270 135.417 1.00 34.14 ?  220 THR A C     1 
ATOM   1775  O  O     . THR A 1 220 ? 146.142 136.294 135.469 1.00 35.22 ?  220 THR A O     1 
ATOM   1776  C  CB    . THR A 1 220 ? 146.648 139.355 134.851 1.00 27.27 ?  220 THR A CB    1 
ATOM   1777  O  OG1   . THR A 1 220 ? 147.179 140.572 135.388 1.00 35.48 ?  220 THR A OG1   1 
ATOM   1778  C  CG2   . THR A 1 220 ? 145.780 139.682 133.649 1.00 29.46 ?  220 THR A CG2   1 
ATOM   1779  N  N     . LYS A 1 221 ? 144.151 137.205 134.923 1.00 35.92 ?  221 LYS A N     1 
ATOM   1780  C  CA    . LYS A 1 221 ? 143.637 135.993 134.302 1.00 30.05 ?  221 LYS A CA    1 
ATOM   1781  C  C     . LYS A 1 221 ? 144.060 135.852 132.847 1.00 33.95 ?  221 LYS A C     1 
ATOM   1782  O  O     . LYS A 1 221 ? 143.816 134.800 132.247 1.00 40.03 ?  221 LYS A O     1 
ATOM   1783  C  CB    . LYS A 1 221 ? 142.110 135.961 134.392 1.00 29.97 ?  221 LYS A CB    1 
ATOM   1784  C  CG    . LYS A 1 221 ? 141.580 135.731 135.791 1.00 32.25 ?  221 LYS A CG    1 
ATOM   1785  C  CD    . LYS A 1 221 ? 140.278 134.953 135.762 1.00 33.02 ?  221 LYS A CD    1 
ATOM   1786  C  CE    . LYS A 1 221 ? 139.953 134.383 137.129 1.00 33.42 ?  221 LYS A CE    1 
ATOM   1787  N  NZ    . LYS A 1 221 ? 138.827 133.411 137.070 1.00 36.29 1  221 LYS A NZ    1 
ATOM   1788  N  N     . GLY A 1 222 ? 144.682 136.874 132.273 1.00 31.76 ?  222 GLY A N     1 
ATOM   1789  C  CA    . GLY A 1 222 ? 145.087 136.828 130.889 1.00 26.99 ?  222 GLY A CA    1 
ATOM   1790  C  C     . GLY A 1 222 ? 143.962 137.218 129.949 1.00 27.61 ?  222 GLY A C     1 
ATOM   1791  O  O     . GLY A 1 222 ? 142.893 137.683 130.352 1.00 33.53 ?  222 GLY A O     1 
ATOM   1792  N  N     . VAL A 1 223 ? 144.226 137.020 128.658 1.00 25.41 ?  223 VAL A N     1 
ATOM   1793  C  CA    . VAL A 1 223 ? 143.219 137.330 127.652 1.00 24.51 ?  223 VAL A CA    1 
ATOM   1794  C  C     . VAL A 1 223 ? 142.161 136.243 127.544 1.00 18.93 ?  223 VAL A C     1 
ATOM   1795  O  O     . VAL A 1 223 ? 141.107 136.483 126.948 1.00 22.69 ?  223 VAL A O     1 
ATOM   1796  C  CB    . VAL A 1 223 ? 143.864 137.572 126.276 1.00 22.73 ?  223 VAL A CB    1 
ATOM   1797  C  CG1   . VAL A 1 223 ? 145.067 138.484 126.409 1.00 20.06 ?  223 VAL A CG1   1 
ATOM   1798  C  CG2   . VAL A 1 223 ? 144.254 136.254 125.627 1.00 20.14 ?  223 VAL A CG2   1 
ATOM   1799  N  N     . VAL A 1 224 ? 142.399 135.058 128.108 1.00 27.29 ?  224 VAL A N     1 
ATOM   1800  C  CA    . VAL A 1 224 ? 141.418 133.982 127.999 1.00 23.25 ?  224 VAL A CA    1 
ATOM   1801  C  C     . VAL A 1 224 ? 140.176 134.273 128.838 1.00 27.16 ?  224 VAL A C     1 
ATOM   1802  O  O     . VAL A 1 224 ? 139.054 133.971 128.415 1.00 29.49 ?  224 VAL A O     1 
ATOM   1803  C  CB    . VAL A 1 224 ? 142.061 132.638 128.381 1.00 30.45 ?  224 VAL A CB    1 
ATOM   1804  C  CG1   . VAL A 1 224 ? 141.037 131.518 128.327 1.00 28.30 ?  224 VAL A CG1   1 
ATOM   1805  C  CG2   . VAL A 1 224 ? 143.223 132.337 127.453 1.00 28.17 ?  224 VAL A CG2   1 
ATOM   1806  N  N     . GLY A 1 225 ? 140.339 134.860 130.025 1.00 26.05 ?  225 GLY A N     1 
ATOM   1807  C  CA    . GLY A 1 225 ? 139.174 135.266 130.797 1.00 23.64 ?  225 GLY A CA    1 
ATOM   1808  C  C     . GLY A 1 225 ? 138.372 136.348 130.102 1.00 21.95 ?  225 GLY A C     1 
ATOM   1809  O  O     . GLY A 1 225 ? 137.136 136.341 130.127 1.00 29.10 ?  225 GLY A O     1 
ATOM   1810  N  N     . VAL A 1 226 ? 139.066 137.293 129.463 1.00 22.04 ?  226 VAL A N     1 
ATOM   1811  C  CA    . VAL A 1 226 ? 138.385 138.318 128.681 1.00 21.14 ?  226 VAL A CA    1 
ATOM   1812  C  C     . VAL A 1 226 ? 137.655 137.689 127.503 1.00 19.41 ?  226 VAL A C     1 
ATOM   1813  O  O     . VAL A 1 226 ? 136.560 138.121 127.132 1.00 22.12 ?  226 VAL A O     1 
ATOM   1814  C  CB    . VAL A 1 226 ? 139.386 139.392 128.221 1.00 19.03 ?  226 VAL A CB    1 
ATOM   1815  C  CG1   . VAL A 1 226 ? 138.656 140.549 127.558 1.00 26.23 ?  226 VAL A CG1   1 
ATOM   1816  C  CG2   . VAL A 1 226 ? 140.211 139.878 129.396 1.00 16.46 ?  226 VAL A CG2   1 
ATOM   1817  N  N     . MET A 1 227 ? 138.252 136.661 126.897 1.00 21.13 ?  227 MET A N     1 
ATOM   1818  C  CA    . MET A 1 227 ? 137.583 135.957 125.807 1.00 23.66 ?  227 MET A CA    1 
ATOM   1819  C  C     . MET A 1 227 ? 136.339 135.237 126.300 1.00 23.17 ?  227 MET A C     1 
ATOM   1820  O  O     . MET A 1 227 ? 135.330 135.187 125.595 1.00 28.48 ?  227 MET A O     1 
ATOM   1821  C  CB    . MET A 1 227 ? 138.533 134.968 125.137 1.00 20.13 ?  227 MET A CB    1 
ATOM   1822  C  CG    . MET A 1 227 ? 139.683 135.606 124.398 1.00 17.73 ?  227 MET A CG    1 
ATOM   1823  S  SD    . MET A 1 227 ? 140.961 134.407 124.008 1.00 36.51 ?  227 MET A SD    1 
ATOM   1824  C  CE    . MET A 1 227 ? 140.102 133.417 122.793 1.00 24.79 ?  227 MET A CE    1 
ATOM   1825  N  N     . LYS A 1 228 ? 136.398 134.650 127.496 1.00 21.26 ?  228 LYS A N     1 
ATOM   1826  C  CA    . LYS A 1 228 ? 135.209 134.023 128.067 1.00 22.96 ?  228 LYS A CA    1 
ATOM   1827  C  C     . LYS A 1 228 ? 134.110 135.051 128.302 1.00 21.81 ?  228 LYS A C     1 
ATOM   1828  O  O     . LYS A 1 228 ? 132.934 134.804 127.995 1.00 24.62 ?  228 LYS A O     1 
ATOM   1829  C  CB    . LYS A 1 228 ? 135.561 133.314 129.374 1.00 24.81 ?  228 LYS A CB    1 
ATOM   1830  C  CG    . LYS A 1 228 ? 136.203 131.952 129.199 1.00 27.57 ?  228 LYS A CG    1 
ATOM   1831  C  CD    . LYS A 1 228 ? 136.763 131.448 130.520 1.00 30.30 ?  228 LYS A CD    1 
ATOM   1832  C  CE    . LYS A 1 228 ? 138.257 131.700 130.621 1.00 31.49 ?  228 LYS A CE    1 
ATOM   1833  N  NZ    . LYS A 1 228 ? 138.709 131.893 132.027 1.00 27.84 1  228 LYS A NZ    1 
ATOM   1834  N  N     . LEU A 1 229 ? 134.477 136.215 128.843 1.00 20.71 ?  229 LEU A N     1 
ATOM   1835  C  CA    . LEU A 1 229 ? 133.502 137.282 129.051 1.00 18.79 ?  229 LEU A CA    1 
ATOM   1836  C  C     . LEU A 1 229 ? 132.890 137.733 127.730 1.00 20.13 ?  229 LEU A C     1 
ATOM   1837  O  O     . LEU A 1 229 ? 131.671 137.914 127.623 1.00 18.55 ?  229 LEU A O     1 
ATOM   1838  C  CB    . LEU A 1 229 ? 134.162 138.461 129.761 1.00 20.16 ?  229 LEU A CB    1 
ATOM   1839  C  CG    . LEU A 1 229 ? 134.448 138.327 131.255 1.00 18.98 ?  229 LEU A CG    1 
ATOM   1840  C  CD1   . LEU A 1 229 ? 135.296 139.495 131.719 1.00 21.66 ?  229 LEU A CD1   1 
ATOM   1841  C  CD2   . LEU A 1 229 ? 133.151 138.266 132.036 1.00 18.33 ?  229 LEU A CD2   1 
ATOM   1842  N  N     . LEU A 1 230 ? 133.729 137.921 126.710 1.00 24.97 ?  230 LEU A N     1 
ATOM   1843  C  CA    . LEU A 1 230 ? 133.240 138.354 125.406 1.00 16.02 ?  230 LEU A CA    1 
ATOM   1844  C  C     . LEU A 1 230 ? 132.366 137.289 124.759 1.00 15.64 ?  230 LEU A C     1 
ATOM   1845  O  O     . LEU A 1 230 ? 131.370 137.611 124.109 1.00 30.75 ?  230 LEU A O     1 
ATOM   1846  C  CB    . LEU A 1 230 ? 134.415 138.709 124.497 1.00 23.37 ?  230 LEU A CB    1 
ATOM   1847  C  CG    . LEU A 1 230 ? 135.165 139.994 124.848 1.00 22.41 ?  230 LEU A CG    1 
ATOM   1848  C  CD1   . LEU A 1 230 ? 136.435 140.114 124.019 1.00 23.43 ?  230 LEU A CD1   1 
ATOM   1849  C  CD2   . LEU A 1 230 ? 134.271 141.207 124.651 1.00 16.74 ?  230 LEU A CD2   1 
ATOM   1850  N  N     . ASP A 1 231 ? 132.732 136.017 124.914 1.00 23.35 ?  231 ASP A N     1 
ATOM   1851  C  CA    . ASP A 1 231 ? 131.922 134.936 124.368 1.00 23.77 ?  231 ASP A CA    1 
ATOM   1852  C  C     . ASP A 1 231 ? 130.551 134.897 125.026 1.00 22.03 ?  231 ASP A C     1 
ATOM   1853  O  O     . ASP A 1 231 ? 129.537 134.712 124.346 1.00 29.84 ?  231 ASP A O     1 
ATOM   1854  C  CB    . ASP A 1 231 ? 132.649 133.602 124.544 1.00 23.08 ?  231 ASP A CB    1 
ATOM   1855  C  CG    . ASP A 1 231 ? 131.802 132.415 124.134 1.00 36.05 ?  231 ASP A CG    1 
ATOM   1856  O  OD1   . ASP A 1 231 ? 131.330 132.391 122.978 1.00 42.35 ?  231 ASP A OD1   1 
ATOM   1857  O  OD2   . ASP A 1 231 ? 131.613 131.504 124.967 1.00 33.33 -1 231 ASP A OD2   1 
ATOM   1858  N  N     . ASN A 1 232 ? 130.499 135.085 126.346 1.00 27.62 ?  232 ASN A N     1 
ATOM   1859  C  CA    . ASN A 1 232 ? 129.204 135.163 127.018 1.00 25.45 ?  232 ASN A CA    1 
ATOM   1860  C  C     . ASN A 1 232 ? 128.406 136.372 126.544 1.00 21.44 ?  232 ASN A C     1 
ATOM   1861  O  O     . ASN A 1 232 ? 127.189 136.281 126.342 1.00 28.17 ?  232 ASN A O     1 
ATOM   1862  C  CB    . ASN A 1 232 ? 129.394 135.200 128.532 1.00 26.42 ?  232 ASN A CB    1 
ATOM   1863  C  CG    . ASN A 1 232 ? 128.521 134.192 129.247 1.00 32.00 ?  232 ASN A CG    1 
ATOM   1864  O  OD1   . ASN A 1 232 ? 127.297 134.317 129.261 1.00 34.71 ?  232 ASN A OD1   1 
ATOM   1865  N  ND2   . ASN A 1 232 ? 129.141 133.175 129.827 1.00 34.25 ?  232 ASN A ND2   1 
ATOM   1866  N  N     . ALA A 1 233 ? 129.075 137.513 126.363 1.00 17.49 ?  233 ALA A N     1 
ATOM   1867  C  CA    . ALA A 1 233 ? 128.388 138.710 125.892 1.00 19.25 ?  233 ALA A CA    1 
ATOM   1868  C  C     . ALA A 1 233 ? 127.818 138.510 124.493 1.00 27.61 ?  233 ALA A C     1 
ATOM   1869  O  O     . ALA A 1 233 ? 126.708 138.966 124.195 1.00 27.48 ?  233 ALA A O     1 
ATOM   1870  C  CB    . ALA A 1 233 ? 129.342 139.904 125.920 1.00 19.50 ?  233 ALA A CB    1 
ATOM   1871  N  N     . PHE A 1 234 ? 128.568 137.837 123.618 1.00 25.88 ?  234 PHE A N     1 
ATOM   1872  C  CA    . PHE A 1 234 ? 128.101 137.607 122.257 1.00 18.99 ?  234 PHE A CA    1 
ATOM   1873  C  C     . PHE A 1 234 ? 127.007 136.550 122.208 1.00 22.17 ?  234 PHE A C     1 
ATOM   1874  O  O     . PHE A 1 234 ? 126.111 136.629 121.361 1.00 29.06 ?  234 PHE A O     1 
ATOM   1875  C  CB    . PHE A 1 234 ? 129.269 137.209 121.356 1.00 24.21 ?  234 PHE A CB    1 
ATOM   1876  C  CG    . PHE A 1 234 ? 130.143 138.362 120.954 1.00 22.59 ?  234 PHE A CG    1 
ATOM   1877  C  CD1   . PHE A 1 234 ? 129.614 139.449 120.283 1.00 21.43 ?  234 PHE A CD1   1 
ATOM   1878  C  CD2   . PHE A 1 234 ? 131.495 138.358 121.245 1.00 21.36 ?  234 PHE A CD2   1 
ATOM   1879  C  CE1   . PHE A 1 234 ? 130.416 140.511 119.917 1.00 20.43 ?  234 PHE A CE1   1 
ATOM   1880  C  CE2   . PHE A 1 234 ? 132.300 139.417 120.883 1.00 22.33 ?  234 PHE A CE2   1 
ATOM   1881  C  CZ    . PHE A 1 234 ? 131.761 140.494 120.216 1.00 22.81 ?  234 PHE A CZ    1 
ATOM   1882  N  N     . ARG A 1 235 ? 127.063 135.554 123.094 1.00 24.66 ?  235 ARG A N     1 
ATOM   1883  C  CA    . ARG A 1 235 ? 125.959 134.607 123.196 1.00 25.84 ?  235 ARG A CA    1 
ATOM   1884  C  C     . ARG A 1 235 ? 124.691 135.302 123.668 1.00 31.07 ?  235 ARG A C     1 
ATOM   1885  O  O     . ARG A 1 235 ? 123.595 135.013 123.177 1.00 39.35 ?  235 ARG A O     1 
ATOM   1886  C  CB    . ARG A 1 235 ? 126.326 133.462 124.139 1.00 26.56 ?  235 ARG A CB    1 
ATOM   1887  C  CG    . ARG A 1 235 ? 127.394 132.531 123.601 1.00 32.06 ?  235 ARG A CG    1 
ATOM   1888  C  CD    . ARG A 1 235 ? 127.425 131.222 124.367 1.00 31.55 ?  235 ARG A CD    1 
ATOM   1889  N  NE    . ARG A 1 235 ? 128.677 131.054 125.095 1.00 33.93 ?  235 ARG A NE    1 
ATOM   1890  C  CZ    . ARG A 1 235 ? 128.868 131.440 126.349 1.00 35.96 ?  235 ARG A CZ    1 
ATOM   1891  N  NH1   . ARG A 1 235 ? 127.905 132.015 127.049 1.00 35.78 1  235 ARG A NH1   1 
ATOM   1892  N  NH2   . ARG A 1 235 ? 130.058 131.246 126.913 1.00 33.53 ?  235 ARG A NH2   1 
ATOM   1893  N  N     . TYR A 1 236 ? 124.822 136.225 124.623 1.00 25.37 ?  236 TYR A N     1 
ATOM   1894  C  CA    . TYR A 1 236 ? 123.654 136.933 125.134 1.00 21.11 ?  236 TYR A CA    1 
ATOM   1895  C  C     . TYR A 1 236 ? 123.048 137.844 124.071 1.00 24.21 ?  236 TYR A C     1 
ATOM   1896  O  O     . TYR A 1 236 ? 121.828 137.859 123.874 1.00 24.55 ?  236 TYR A O     1 
ATOM   1897  C  CB    . TYR A 1 236 ? 124.031 137.736 126.377 1.00 19.94 ?  236 TYR A CB    1 
ATOM   1898  C  CG    . TYR A 1 236 ? 122.847 138.359 127.069 1.00 23.99 ?  236 TYR A CG    1 
ATOM   1899  C  CD1   . TYR A 1 236 ? 121.979 137.584 127.823 1.00 21.35 ?  236 TYR A CD1   1 
ATOM   1900  C  CD2   . TYR A 1 236 ? 122.593 139.720 126.966 1.00 24.85 ?  236 TYR A CD2   1 
ATOM   1901  C  CE1   . TYR A 1 236 ? 120.895 138.144 128.458 1.00 24.71 ?  236 TYR A CE1   1 
ATOM   1902  C  CE2   . TYR A 1 236 ? 121.508 140.289 127.599 1.00 16.98 ?  236 TYR A CE2   1 
ATOM   1903  C  CZ    . TYR A 1 236 ? 120.664 139.495 128.343 1.00 21.52 ?  236 TYR A CZ    1 
ATOM   1904  O  OH    . TYR A 1 236 ? 119.582 140.048 128.978 1.00 25.78 ?  236 TYR A OH    1 
ATOM   1905  N  N     . ALA A 1 237 ? 123.885 138.613 123.378 1.00 30.61 ?  237 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 237 ? 123.431 139.556 122.356 1.00 30.91 ?  237 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 237 ? 123.469 138.842 121.010 1.00 35.59 ?  237 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 237 ? 124.506 138.772 120.350 1.00 39.55 ?  237 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 237 ? 124.292 140.813 122.358 1.00 30.89 ?  237 ALA A CB    1 
ATOM   1910  N  N     . ASP A 1 238 ? 122.320 138.313 120.597 1.00 50.35 ?  238 ASP A N     1 
ATOM   1911  C  CA    . ASP A 1 238 ? 122.210 137.488 119.398 1.00 54.69 ?  238 ASP A CA    1 
ATOM   1912  C  C     . ASP A 1 238 ? 121.082 137.990 118.501 1.00 59.58 ?  238 ASP A C     1 
ATOM   1913  O  O     . ASP A 1 238 ? 120.243 137.221 118.025 1.00 59.96 ?  238 ASP A O     1 
ATOM   1914  C  CB    . ASP A 1 238 ? 122.002 136.025 119.774 1.00 52.63 ?  238 ASP A CB    1 
ATOM   1915  C  CG    . ASP A 1 238 ? 120.856 135.829 120.743 1.00 55.48 ?  238 ASP A CG    1 
ATOM   1916  O  OD1   . ASP A 1 238 ? 120.366 136.835 121.299 1.00 55.79 ?  238 ASP A OD1   1 
ATOM   1917  O  OD2   . ASP A 1 238 ? 120.443 134.669 120.953 1.00 56.24 -1 238 ASP A OD2   1 
ATOM   1918  N  N     . GLN A 1 239 ? 121.055 139.305 118.263 1.00 65.05 ?  239 GLN A N     1 
ATOM   1919  C  CA    . GLN A 1 239 ? 120.089 139.935 117.358 1.00 64.51 ?  239 GLN A CA    1 
ATOM   1920  C  C     . GLN A 1 239 ? 118.650 139.598 117.740 1.00 64.87 ?  239 GLN A C     1 
ATOM   1921  O  O     . GLN A 1 239 ? 117.834 139.219 116.896 1.00 64.37 ?  239 GLN A O     1 
ATOM   1922  C  CB    . GLN A 1 239 ? 120.364 139.552 115.902 1.00 64.27 ?  239 GLN A CB    1 
ATOM   1923  C  CG    . GLN A 1 239 ? 121.394 140.416 115.205 1.00 63.60 ?  239 GLN A CG    1 
ATOM   1924  C  CD    . GLN A 1 239 ? 121.096 140.586 113.726 1.00 65.72 ?  239 GLN A CD    1 
ATOM   1925  O  OE1   . GLN A 1 239 ? 119.961 140.859 113.338 1.00 65.94 ?  239 GLN A OE1   1 
ATOM   1926  N  NE2   . GLN A 1 239 ? 122.116 140.416 112.893 1.00 64.99 ?  239 GLN A NE2   1 
ATOM   1927  N  N     . MET A 1 240 ? 118.339 139.743 119.029 1.00 68.51 ?  240 MET A N     1 
ATOM   1928  C  CA    . MET A 1 240 ? 117.001 139.460 119.551 1.00 68.14 ?  240 MET A CA    1 
ATOM   1929  C  C     . MET A 1 240 ? 116.578 138.025 119.244 1.00 69.94 ?  240 MET A C     1 
ATOM   1930  O  O     . MET A 1 240 ? 115.428 137.759 118.885 1.00 68.89 ?  240 MET A O     1 
ATOM   1931  C  CB    . MET A 1 240 ? 115.973 140.457 119.009 1.00 66.92 ?  240 MET A CB    1 
ATOM   1932  C  CG    . MET A 1 240 ? 116.114 141.870 119.551 1.00 68.38 ?  240 MET A CG    1 
ATOM   1933  S  SD    . MET A 1 240 ? 117.804 142.493 119.488 1.00 73.97 ?  240 MET A SD    1 
ATOM   1934  C  CE    . MET A 1 240 ? 117.500 144.257 119.486 1.00 65.29 ?  240 MET A CE    1 
ATOM   1935  N  N     . GLY A 1 241 ? 117.514 137.093 119.382 1.00 69.79 ?  241 GLY A N     1 
ATOM   1936  C  CA    . GLY A 1 241 ? 117.229 135.692 119.127 1.00 68.54 ?  241 GLY A CA    1 
ATOM   1937  C  C     . GLY A 1 241 ? 116.924 135.358 117.681 1.00 70.57 ?  241 GLY A C     1 
ATOM   1938  O  O     . GLY A 1 241 ? 116.017 134.560 117.413 1.00 71.99 ?  241 GLY A O     1 
ATOM   1939  N  N     . GLN A 1 242 ? 117.660 135.948 116.741 1.00 72.20 ?  242 GLN A N     1 
ATOM   1940  C  CA    . GLN A 1 242 ? 117.495 135.659 115.322 1.00 72.85 ?  242 GLN A CA    1 
ATOM   1941  C  C     . GLN A 1 242 ? 118.712 134.948 114.744 1.00 73.98 ?  242 GLN A C     1 
ATOM   1942  O  O     . GLN A 1 242 ? 118.578 133.881 114.138 1.00 74.28 ?  242 GLN A O     1 
ATOM   1943  C  CB    . GLN A 1 242 ? 117.210 136.955 114.550 1.00 72.37 ?  242 GLN A CB    1 
ATOM   1944  C  CG    . GLN A 1 242 ? 115.888 137.611 114.913 1.00 73.86 ?  242 GLN A CG    1 
ATOM   1945  C  CD    . GLN A 1 242 ? 115.434 138.619 113.878 1.00 75.01 ?  242 GLN A CD    1 
ATOM   1946  O  OE1   . GLN A 1 242 ? 116.003 138.709 112.789 1.00 75.76 ?  242 GLN A OE1   1 
ATOM   1947  N  NE2   . GLN A 1 242 ? 114.405 139.388 114.212 1.00 73.28 ?  242 GLN A NE2   1 
ATOM   1948  N  N     . ARG A 1 243 ? 119.904 135.514 114.918 1.00 64.01 ?  243 ARG A N     1 
ATOM   1949  C  CA    . ARG A 1 243 ? 121.144 134.899 114.472 1.00 63.58 ?  243 ARG A CA    1 
ATOM   1950  C  C     . ARG A 1 243 ? 122.068 134.705 115.666 1.00 62.97 ?  243 ARG A C     1 
ATOM   1951  O  O     . ARG A 1 243 ? 121.966 135.416 116.670 1.00 61.17 ?  243 ARG A O     1 
ATOM   1952  C  CB    . ARG A 1 243 ? 121.823 135.749 113.366 1.00 62.81 ?  243 ARG A CB    1 
ATOM   1953  C  CG    . ARG A 1 243 ? 122.289 137.166 113.758 1.00 63.98 ?  243 ARG A CG    1 
ATOM   1954  C  CD    . ARG A 1 243 ? 123.606 137.179 114.528 1.00 64.32 ?  243 ARG A CD    1 
ATOM   1955  N  NE    . ARG A 1 243 ? 124.018 138.515 114.942 1.00 65.06 ?  243 ARG A NE    1 
ATOM   1956  C  CZ    . ARG A 1 243 ? 124.954 139.232 114.336 1.00 64.23 ?  243 ARG A CZ    1 
ATOM   1957  N  NH1   . ARG A 1 243 ? 125.593 138.778 113.270 1.00 63.32 1  243 ARG A NH1   1 
ATOM   1958  N  NH2   . ARG A 1 243 ? 125.261 140.434 114.815 1.00 60.04 ?  243 ARG A NH2   1 
ATOM   1959  N  N     . GLN A 1 244 ? 122.972 133.735 115.552 1.00 64.35 ?  244 GLN A N     1 
ATOM   1960  C  CA    . GLN A 1 244 ? 123.937 133.491 116.616 1.00 62.85 ?  244 GLN A CA    1 
ATOM   1961  C  C     . GLN A 1 244 ? 124.935 134.640 116.692 1.00 62.96 ?  244 GLN A C     1 
ATOM   1962  O  O     . GLN A 1 244 ? 125.535 135.018 115.682 1.00 60.03 ?  244 GLN A O     1 
ATOM   1963  C  CB    . GLN A 1 244 ? 124.670 132.172 116.379 1.00 60.75 ?  244 GLN A CB    1 
ATOM   1964  C  CG    . GLN A 1 244 ? 123.863 130.934 116.730 1.00 62.26 ?  244 GLN A CG    1 
ATOM   1965  C  CD    . GLN A 1 244 ? 124.743 129.738 117.036 1.00 64.17 ?  244 GLN A CD    1 
ATOM   1966  O  OE1   . GLN A 1 244 ? 125.747 129.502 116.363 1.00 64.37 ?  244 GLN A OE1   1 
ATOM   1967  N  NE2   . GLN A 1 244 ? 124.372 128.977 118.059 1.00 61.33 ?  244 GLN A NE2   1 
ATOM   1968  N  N     . GLY A 1 245 ? 125.117 135.186 117.892 1.00 50.20 ?  245 GLY A N     1 
ATOM   1969  C  CA    . GLY A 1 245 ? 126.037 136.290 118.089 1.00 46.90 ?  245 GLY A CA    1 
ATOM   1970  C  C     . GLY A 1 245 ? 127.451 135.950 117.670 1.00 45.73 ?  245 GLY A C     1 
ATOM   1971  O  O     . GLY A 1 245 ? 128.046 134.996 118.180 1.00 43.83 ?  245 GLY A O     1 
ATOM   1972  N  N     . SER A 1 246 ? 128.001 136.729 116.744 1.00 40.73 ?  246 SER A N     1 
ATOM   1973  C  CA    . SER A 1 246 ? 129.294 136.445 116.136 1.00 32.62 ?  246 SER A CA    1 
ATOM   1974  C  C     . SER A 1 246 ? 130.300 137.496 116.579 1.00 31.43 ?  246 SER A C     1 
ATOM   1975  O  O     . SER A 1 246 ? 130.072 138.697 116.396 1.00 30.78 ?  246 SER A O     1 
ATOM   1976  C  CB    . SER A 1 246 ? 129.185 136.414 114.613 1.00 32.71 ?  246 SER A CB    1 
ATOM   1977  O  OG    . SER A 1 246 ? 128.361 135.346 114.180 1.00 44.32 ?  246 SER A OG    1 
ATOM   1978  N  N     . GLY A 1 247 ? 131.409 137.042 117.155 1.00 28.96 ?  247 GLY A N     1 
ATOM   1979  C  CA    . GLY A 1 247 ? 132.471 137.936 117.557 1.00 13.13 ?  247 GLY A CA    1 
ATOM   1980  C  C     . GLY A 1 247 ? 133.822 137.333 117.235 1.00 15.41 ?  247 GLY A C     1 
ATOM   1981  O  O     . GLY A 1 247 ? 133.969 136.117 117.089 1.00 23.68 ?  247 GLY A O     1 
ATOM   1982  N  N     . ALA A 1 248 ? 134.810 138.211 117.122 1.00 17.67 ?  248 ALA A N     1 
ATOM   1983  C  CA    . ALA A 1 248 ? 136.177 137.818 116.832 1.00 14.46 ?  248 ALA A CA    1 
ATOM   1984  C  C     . ALA A 1 248 ? 137.114 138.472 117.833 1.00 12.56 ?  248 ALA A C     1 
ATOM   1985  O  O     . ALA A 1 248 ? 136.887 139.599 118.276 1.00 16.39 ?  248 ALA A O     1 
ATOM   1986  C  CB    . ALA A 1 248 ? 136.589 138.200 115.404 1.00 8.12  ?  248 ALA A CB    1 
ATOM   1987  N  N     . ALA A 1 249 ? 138.170 137.750 118.187 1.00 16.30 ?  249 ALA A N     1 
ATOM   1988  C  CA    . ALA A 1 249 ? 139.217 138.255 119.064 1.00 5.45  ?  249 ALA A CA    1 
ATOM   1989  C  C     . ALA A 1 249 ? 140.555 138.095 118.362 1.00 11.13 ?  249 ALA A C     1 
ATOM   1990  O  O     . ALA A 1 249 ? 140.861 137.018 117.842 1.00 19.26 ?  249 ALA A O     1 
ATOM   1991  C  CB    . ALA A 1 249 ? 139.222 137.519 120.406 1.00 13.03 ?  249 ALA A CB    1 
ATOM   1992  N  N     . TYR A 1 250 ? 141.343 139.161 118.340 1.00 15.80 ?  250 TYR A N     1 
ATOM   1993  C  CA    . TYR A 1 250 ? 142.653 139.149 117.707 1.00 9.77  ?  250 TYR A CA    1 
ATOM   1994  C  C     . TYR A 1 250 ? 143.731 139.336 118.761 1.00 6.64  ?  250 TYR A C     1 
ATOM   1995  O  O     . TYR A 1 250 ? 143.621 140.216 119.621 1.00 17.12 ?  250 TYR A O     1 
ATOM   1996  C  CB    . TYR A 1 250 ? 142.759 140.237 116.640 1.00 10.64 ?  250 TYR A CB    1 
ATOM   1997  C  CG    . TYR A 1 250 ? 142.200 139.829 115.299 1.00 17.03 ?  250 TYR A CG    1 
ATOM   1998  C  CD1   . TYR A 1 250 ? 140.832 139.830 115.069 1.00 11.39 ?  250 TYR A CD1   1 
ATOM   1999  C  CD2   . TYR A 1 250 ? 143.038 139.437 114.265 1.00 13.62 ?  250 TYR A CD2   1 
ATOM   2000  C  CE1   . TYR A 1 250 ? 140.314 139.458 113.849 1.00 5.03  ?  250 TYR A CE1   1 
ATOM   2001  C  CE2   . TYR A 1 250 ? 142.528 139.061 113.040 1.00 9.66  ?  250 TYR A CE2   1 
ATOM   2002  C  CZ    . TYR A 1 250 ? 141.166 139.074 112.837 1.00 8.96  ?  250 TYR A CZ    1 
ATOM   2003  O  OH    . TYR A 1 250 ? 140.651 138.704 111.618 1.00 16.52 ?  250 TYR A OH    1 
ATOM   2004  N  N     . LEU A 1 251 ? 144.762 138.504 118.693 1.00 11.05 ?  251 LEU A N     1 
ATOM   2005  C  CA    . LEU A 1 251 ? 145.900 138.585 119.591 1.00 13.94 ?  251 LEU A CA    1 
ATOM   2006  C  C     . LEU A 1 251 ? 147.181 138.553 118.777 1.00 11.63 ?  251 LEU A C     1 
ATOM   2007  O  O     . LEU A 1 251 ? 147.297 137.784 117.819 1.00 16.73 ?  251 LEU A O     1 
ATOM   2008  C  CB    . LEU A 1 251 ? 145.899 137.437 120.603 1.00 17.48 ?  251 LEU A CB    1 
ATOM   2009  C  CG    . LEU A 1 251 ? 146.746 137.657 121.856 1.00 12.99 ?  251 LEU A CG    1 
ATOM   2010  C  CD1   . LEU A 1 251 ? 146.046 138.606 122.807 1.00 18.08 ?  251 LEU A CD1   1 
ATOM   2011  C  CD2   . LEU A 1 251 ? 147.048 136.336 122.536 1.00 13.39 ?  251 LEU A CD2   1 
ATOM   2012  N  N     . ASN A 1 252 ? 148.137 139.394 119.157 1.00 15.94 ?  252 ASN A N     1 
ATOM   2013  C  CA    . ASN A 1 252 ? 149.450 139.347 118.535 1.00 12.87 ?  252 ASN A CA    1 
ATOM   2014  C  C     . ASN A 1 252 ? 150.149 138.046 118.902 1.00 14.42 ?  252 ASN A C     1 
ATOM   2015  O  O     . ASN A 1 252 ? 150.013 137.541 120.019 1.00 25.53 ?  252 ASN A O     1 
ATOM   2016  C  CB    . ASN A 1 252 ? 150.289 140.546 118.969 1.00 15.10 ?  252 ASN A CB    1 
ATOM   2017  C  CG    . ASN A 1 252 ? 151.381 140.877 117.976 1.00 20.40 ?  252 ASN A CG    1 
ATOM   2018  O  OD1   . ASN A 1 252 ? 152.416 140.214 117.929 1.00 25.03 ?  252 ASN A OD1   1 
ATOM   2019  N  ND2   . ASN A 1 252 ? 151.150 141.900 117.164 1.00 17.33 ?  252 ASN A ND2   1 
ATOM   2020  N  N     . ILE A 1 253 ? 150.901 137.494 117.946 1.00 13.59 ?  253 ILE A N     1 
ATOM   2021  C  CA    . ILE A 1 253 ? 151.558 136.214 118.174 1.00 20.79 ?  253 ILE A CA    1 
ATOM   2022  C  C     . ILE A 1 253 ? 152.679 136.325 119.200 1.00 23.63 ?  253 ILE A C     1 
ATOM   2023  O  O     . ILE A 1 253 ? 153.113 135.305 119.747 1.00 25.79 ?  253 ILE A O     1 
ATOM   2024  C  CB    . ILE A 1 253 ? 152.075 135.635 116.843 1.00 19.47 ?  253 ILE A CB    1 
ATOM   2025  C  CG1   . ILE A 1 253 ? 152.212 134.115 116.943 1.00 23.14 ?  253 ILE A CG1   1 
ATOM   2026  C  CG2   . ILE A 1 253 ? 153.394 136.281 116.448 1.00 13.69 ?  253 ILE A CG2   1 
ATOM   2027  C  CD1   . ILE A 1 253 ? 152.044 133.398 115.631 1.00 21.73 ?  253 ILE A CD1   1 
ATOM   2028  N  N     . PHE A 1 254 ? 153.156 137.533 119.486 1.00 22.21 ?  254 PHE A N     1 
ATOM   2029  C  CA    . PHE A 1 254 ? 154.177 137.737 120.503 1.00 15.92 ?  254 PHE A CA    1 
ATOM   2030  C  C     . PHE A 1 254 ? 153.587 137.984 121.885 1.00 21.42 ?  254 PHE A C     1 
ATOM   2031  O  O     . PHE A 1 254 ? 154.342 138.078 122.859 1.00 29.46 ?  254 PHE A O     1 
ATOM   2032  C  CB    . PHE A 1 254 ? 155.094 138.897 120.102 1.00 22.92 ?  254 PHE A CB    1 
ATOM   2033  C  CG    . PHE A 1 254 ? 156.113 138.523 119.063 1.00 26.00 ?  254 PHE A CG    1 
ATOM   2034  C  CD1   . PHE A 1 254 ? 157.141 137.646 119.366 1.00 25.65 ?  254 PHE A CD1   1 
ATOM   2035  C  CD2   . PHE A 1 254 ? 156.032 139.030 117.778 1.00 23.77 ?  254 PHE A CD2   1 
ATOM   2036  C  CE1   . PHE A 1 254 ? 158.076 137.294 118.412 1.00 28.02 ?  254 PHE A CE1   1 
ATOM   2037  C  CE2   . PHE A 1 254 ? 156.963 138.679 116.819 1.00 26.10 ?  254 PHE A CE2   1 
ATOM   2038  C  CZ    . PHE A 1 254 ? 157.986 137.811 117.138 1.00 27.05 ?  254 PHE A CZ    1 
ATOM   2039  N  N     . HIS A 1 255 ? 152.266 138.102 121.988 1.00 26.58 ?  255 HIS A N     1 
ATOM   2040  C  CA    . HIS A 1 255 ? 151.608 138.073 123.287 1.00 17.25 ?  255 HIS A CA    1 
ATOM   2041  C  C     . HIS A 1 255 ? 151.819 136.707 123.924 1.00 19.54 ?  255 HIS A C     1 
ATOM   2042  O  O     . HIS A 1 255 ? 151.800 135.680 123.241 1.00 28.90 ?  255 HIS A O     1 
ATOM   2043  C  CB    . HIS A 1 255 ? 150.117 138.365 123.121 1.00 19.06 ?  255 HIS A CB    1 
ATOM   2044  C  CG    . HIS A 1 255 ? 149.412 138.707 124.397 1.00 23.16 ?  255 HIS A CG    1 
ATOM   2045  N  ND1   . HIS A 1 255 ? 149.152 137.778 125.380 1.00 21.46 ?  255 HIS A ND1   1 
ATOM   2046  C  CD2   . HIS A 1 255 ? 148.888 139.875 124.836 1.00 15.99 ?  255 HIS A CD2   1 
ATOM   2047  C  CE1   . HIS A 1 255 ? 148.512 138.363 126.377 1.00 16.84 ?  255 HIS A CE1   1 
ATOM   2048  N  NE2   . HIS A 1 255 ? 148.339 139.636 126.071 1.00 13.24 ?  255 HIS A NE2   1 
ATOM   2049  N  N     . ARG A 1 256 ? 152.029 136.691 125.241 1.00 21.55 ?  256 ARG A N     1 
ATOM   2050  C  CA    . ARG A 1 256 ? 152.383 135.435 125.893 1.00 21.81 ?  256 ARG A CA    1 
ATOM   2051  C  C     . ARG A 1 256 ? 151.207 134.468 125.907 1.00 27.23 ?  256 ARG A C     1 
ATOM   2052  O  O     . ARG A 1 256 ? 151.398 133.248 125.843 1.00 30.87 ?  256 ARG A O     1 
ATOM   2053  C  CB    . ARG A 1 256 ? 152.866 135.689 127.313 1.00 24.98 ?  256 ARG A CB    1 
ATOM   2054  C  CG    . ARG A 1 256 ? 153.541 134.482 127.919 1.00 29.78 ?  256 ARG A CG    1 
ATOM   2055  C  CD    . ARG A 1 256 ? 153.072 134.221 129.326 1.00 30.42 ?  256 ARG A CD    1 
ATOM   2056  N  NE    . ARG A 1 256 ? 151.622 134.275 129.451 1.00 29.67 ?  256 ARG A NE    1 
ATOM   2057  C  CZ    . ARG A 1 256 ? 150.864 133.214 129.688 1.00 31.62 ?  256 ARG A CZ    1 
ATOM   2058  N  NH1   . ARG A 1 256 ? 151.391 132.010 129.838 1.00 32.60 1  256 ARG A NH1   1 
ATOM   2059  N  NH2   . ARG A 1 256 ? 149.548 133.365 129.787 1.00 33.08 ?  256 ARG A NH2   1 
ATOM   2060  N  N     . ASP A 1 257 ? 149.987 134.988 125.987 1.00 22.54 ?  257 ASP A N     1 
ATOM   2061  C  CA    . ASP A 1 257 ? 148.777 134.170 126.005 1.00 19.25 ?  257 ASP A CA    1 
ATOM   2062  C  C     . ASP A 1 257 ? 148.496 133.493 124.684 1.00 24.96 ?  257 ASP A C     1 
ATOM   2063  O  O     . ASP A 1 257 ? 147.470 132.800 124.615 1.00 32.70 ?  257 ASP A O     1 
ATOM   2064  C  CB    . ASP A 1 257 ? 147.569 135.021 126.396 1.00 21.68 ?  257 ASP A CB    1 
ATOM   2065  C  CG    . ASP A 1 257 ? 147.524 135.334 127.873 1.00 30.64 ?  257 ASP A CG    1 
ATOM   2066  O  OD1   . ASP A 1 257 ? 148.169 134.612 128.658 1.00 28.10 ?  257 ASP A OD1   1 
ATOM   2067  O  OD2   . ASP A 1 257 ? 146.830 136.299 128.251 1.00 34.69 -1 257 ASP A OD2   1 
ATOM   2068  N  N     . ILE A 1 258 ? 149.370 133.651 123.686 1.00 26.12 ?  258 ILE A N     1 
ATOM   2069  C  CA    . ILE A 1 258 ? 149.053 133.220 122.328 1.00 25.64 ?  258 ILE A CA    1 
ATOM   2070  C  C     . ILE A 1 258 ? 148.712 131.735 122.298 1.00 23.84 ?  258 ILE A C     1 
ATOM   2071  O  O     . ILE A 1 258 ? 147.803 131.310 121.578 1.00 32.27 ?  258 ILE A O     1 
ATOM   2072  C  CB    . ILE A 1 258 ? 150.208 133.567 121.368 1.00 22.86 ?  258 ILE A CB    1 
ATOM   2073  C  CG1   . ILE A 1 258 ? 149.812 133.265 119.921 1.00 25.32 ?  258 ILE A CG1   1 
ATOM   2074  C  CG2   . ILE A 1 258 ? 151.493 132.842 121.753 1.00 19.03 ?  258 ILE A CG2   1 
ATOM   2075  C  CD1   . ILE A 1 258 ? 148.596 134.034 119.460 1.00 18.76 ?  258 ILE A CD1   1 
ATOM   2076  N  N     . ASN A 1 259 ? 149.423 130.925 123.085 1.00 23.42 ?  259 ASN A N     1 
ATOM   2077  C  CA    . ASN A 1 259 ? 149.099 129.505 123.145 1.00 23.87 ?  259 ASN A CA    1 
ATOM   2078  C  C     . ASN A 1 259 ? 147.732 129.287 123.780 1.00 27.63 ?  259 ASN A C     1 
ATOM   2079  O  O     . ASN A 1 259 ? 146.867 128.619 123.198 1.00 29.97 ?  259 ASN A O     1 
ATOM   2080  C  CB    . ASN A 1 259 ? 150.184 128.755 123.917 1.00 25.62 ?  259 ASN A CB    1 
ATOM   2081  C  CG    . ASN A 1 259 ? 151.461 128.598 123.117 1.00 30.57 ?  259 ASN A CG    1 
ATOM   2082  O  OD1   . ASN A 1 259 ? 151.498 127.879 122.119 1.00 31.68 ?  259 ASN A OD1   1 
ATOM   2083  N  ND2   . ASN A 1 259 ? 152.516 129.278 123.550 1.00 27.56 ?  259 ASN A ND2   1 
ATOM   2084  N  N     . ASP A 1 260 ? 147.500 129.887 124.951 1.00 26.94 ?  260 ASP A N     1 
ATOM   2085  C  CA    . ASP A 1 260 ? 146.210 129.737 125.617 1.00 26.40 ?  260 ASP A CA    1 
ATOM   2086  C  C     . ASP A 1 260 ? 145.090 130.283 124.745 1.00 21.16 ?  260 ASP A C     1 
ATOM   2087  O  O     . ASP A 1 260 ? 144.036 129.653 124.600 1.00 27.71 ?  260 ASP A O     1 
ATOM   2088  C  CB    . ASP A 1 260 ? 146.235 130.441 126.974 1.00 26.24 ?  260 ASP A CB    1 
ATOM   2089  C  CG    . ASP A 1 260 ? 147.506 130.169 127.751 1.00 36.42 ?  260 ASP A CG    1 
ATOM   2090  O  OD1   . ASP A 1 260 ? 147.946 131.063 128.504 1.00 35.80 ?  260 ASP A OD1   1 
ATOM   2091  O  OD2   . ASP A 1 260 ? 148.064 129.061 127.612 1.00 35.91 -1 260 ASP A OD2   1 
ATOM   2092  N  N     . PHE A 1 261 ? 145.311 131.459 124.153 1.00 26.31 ?  261 PHE A N     1 
ATOM   2093  C  CA    . PHE A 1 261 ? 144.466 131.978 123.086 1.00 23.74 ?  261 PHE A CA    1 
ATOM   2094  C  C     . PHE A 1 261 ? 144.123 130.882 122.085 1.00 20.08 ?  261 PHE A C     1 
ATOM   2095  O  O     . PHE A 1 261 ? 142.952 130.524 121.902 1.00 21.56 ?  261 PHE A O     1 
ATOM   2096  C  CB    . PHE A 1 261 ? 145.199 133.142 122.406 1.00 16.16 ?  261 PHE A CB    1 
ATOM   2097  C  CG    . PHE A 1 261 ? 144.383 133.882 121.388 1.00 22.45 ?  261 PHE A CG    1 
ATOM   2098  C  CD1   . PHE A 1 261 ? 143.437 134.810 121.780 1.00 18.74 ?  261 PHE A CD1   1 
ATOM   2099  C  CD2   . PHE A 1 261 ? 144.594 133.679 120.036 1.00 23.64 ?  261 PHE A CD2   1 
ATOM   2100  C  CE1   . PHE A 1 261 ? 142.696 135.501 120.846 1.00 13.75 ?  261 PHE A CE1   1 
ATOM   2101  C  CE2   . PHE A 1 261 ? 143.858 134.370 119.097 1.00 15.00 ?  261 PHE A CE2   1 
ATOM   2102  C  CZ    . PHE A 1 261 ? 142.909 135.283 119.503 1.00 18.00 ?  261 PHE A CZ    1 
ATOM   2103  N  N     . LEU A 1 262 ? 145.156 130.296 121.473 1.00 26.08 ?  262 LEU A N     1 
ATOM   2104  C  CA    . LEU A 1 262 ? 144.931 129.228 120.506 1.00 23.94 ?  262 LEU A CA    1 
ATOM   2105  C  C     . LEU A 1 262 ? 144.264 128.029 121.162 1.00 29.96 ?  262 LEU A C     1 
ATOM   2106  O  O     . LEU A 1 262 ? 143.416 127.366 120.551 1.00 28.96 ?  262 LEU A O     1 
ATOM   2107  C  CB    . LEU A 1 262 ? 146.255 128.825 119.860 1.00 23.93 ?  262 LEU A CB    1 
ATOM   2108  C  CG    . LEU A 1 262 ? 146.927 129.875 118.977 1.00 25.30 ?  262 LEU A CG    1 
ATOM   2109  C  CD1   . LEU A 1 262 ? 148.241 129.346 118.435 1.00 27.68 ?  262 LEU A CD1   1 
ATOM   2110  C  CD2   . LEU A 1 262 ? 146.005 130.302 117.851 1.00 23.46 ?  262 LEU A CD2   1 
ATOM   2111  N  N     . ASP A 1 263 ? 144.606 127.760 122.424 1.00 35.28 ?  263 ASP A N     1 
ATOM   2112  C  CA    . ASP A 1 263 ? 144.014 126.631 123.128 1.00 29.88 ?  263 ASP A CA    1 
ATOM   2113  C  C     . ASP A 1 263 ? 142.512 126.793 123.304 1.00 31.41 ?  263 ASP A C     1 
ATOM   2114  O  O     . ASP A 1 263 ? 141.829 125.814 123.621 1.00 39.37 ?  263 ASP A O     1 
ATOM   2115  C  CB    . ASP A 1 263 ? 144.682 126.449 124.491 1.00 33.59 ?  263 ASP A CB    1 
ATOM   2116  C  CG    . ASP A 1 263 ? 146.073 125.859 124.382 1.00 38.24 ?  263 ASP A CG    1 
ATOM   2117  O  OD1   . ASP A 1 263 ? 146.391 125.277 123.324 1.00 38.59 ?  263 ASP A OD1   1 
ATOM   2118  O  OD2   . ASP A 1 263 ? 146.846 125.975 125.355 1.00 38.50 -1 263 ASP A OD2   1 
ATOM   2119  N  N     . THR A 1 264 ? 141.982 128.003 123.110 1.00 34.25 ?  264 THR A N     1 
ATOM   2120  C  CA    . THR A 1 264 ? 140.540 128.183 123.192 1.00 32.61 ?  264 THR A CA    1 
ATOM   2121  C  C     . THR A 1 264 ? 139.807 127.521 122.033 1.00 37.29 ?  264 THR A C     1 
ATOM   2122  O  O     . THR A 1 264 ? 138.592 127.320 122.122 1.00 40.05 ?  264 THR A O     1 
ATOM   2123  C  CB    . THR A 1 264 ? 140.193 129.671 123.240 1.00 35.07 ?  264 THR A CB    1 
ATOM   2124  O  OG1   . THR A 1 264 ? 140.706 130.319 122.069 1.00 39.96 ?  264 THR A OG1   1 
ATOM   2125  C  CG2   . THR A 1 264 ? 140.794 130.314 124.479 1.00 31.28 ?  264 THR A CG2   1 
ATOM   2126  N  N     . LYS A 1 265 ? 140.509 127.176 120.953 1.00 36.99 ?  265 LYS A N     1 
ATOM   2127  C  CA    . LYS A 1 265 ? 139.877 126.560 119.794 1.00 36.97 ?  265 LYS A CA    1 
ATOM   2128  C  C     . LYS A 1 265 ? 140.152 125.069 119.672 1.00 39.83 ?  265 LYS A C     1 
ATOM   2129  O  O     . LYS A 1 265 ? 139.643 124.437 118.740 1.00 43.53 ?  265 LYS A O     1 
ATOM   2130  C  CB    . LYS A 1 265 ? 140.318 127.269 118.509 1.00 37.82 ?  265 LYS A CB    1 
ATOM   2131  C  CG    . LYS A 1 265 ? 139.558 128.547 118.224 1.00 37.62 ?  265 LYS A CG    1 
ATOM   2132  C  CD    . LYS A 1 265 ? 138.066 128.352 118.409 1.00 39.31 ?  265 LYS A CD    1 
ATOM   2133  C  CE    . LYS A 1 265 ? 137.313 129.649 118.199 1.00 36.10 ?  265 LYS A CE    1 
ATOM   2134  N  NZ    . LYS A 1 265 ? 135.888 129.529 118.605 1.00 37.78 1  265 LYS A NZ    1 
ATOM   2135  N  N     . LYS A 1 266 ? 140.936 124.490 120.574 1.00 45.49 ?  266 LYS A N     1 
ATOM   2136  C  CA    . LYS A 1 266 ? 141.170 123.054 120.532 1.00 46.34 ?  266 LYS A CA    1 
ATOM   2137  C  C     . LYS A 1 266 ? 139.932 122.298 121.000 1.00 50.98 ?  266 LYS A C     1 
ATOM   2138  O  O     . LYS A 1 266 ? 139.200 122.744 121.887 1.00 50.36 ?  266 LYS A O     1 
ATOM   2139  C  CB    . LYS A 1 266 ? 142.376 122.681 121.392 1.00 44.07 ?  266 LYS A CB    1 
ATOM   2140  C  CG    . LYS A 1 266 ? 143.710 122.916 120.705 1.00 47.04 ?  266 LYS A CG    1 
ATOM   2141  C  CD    . LYS A 1 266 ? 144.871 122.416 121.547 1.00 48.02 ?  266 LYS A CD    1 
ATOM   2142  C  CE    . LYS A 1 266 ? 146.172 122.460 120.760 1.00 48.71 ?  266 LYS A CE    1 
ATOM   2143  N  NZ    . LYS A 1 266 ? 147.362 122.253 121.631 1.00 47.04 1  266 LYS A NZ    1 
ATOM   2144  N  N     . ILE A 1 267 ? 139.697 121.142 120.378 1.00 57.94 ?  267 ILE A N     1 
ATOM   2145  C  CA    . ILE A 1 267 ? 138.552 120.317 120.754 1.00 59.55 ?  267 ILE A CA    1 
ATOM   2146  C  C     . ILE A 1 267 ? 138.741 119.747 122.153 1.00 59.12 ?  267 ILE A C     1 
ATOM   2147  O  O     . ILE A 1 267 ? 137.779 119.607 122.918 1.00 57.17 ?  267 ILE A O     1 
ATOM   2148  C  CB    . ILE A 1 267 ? 138.330 119.205 119.713 1.00 59.00 ?  267 ILE A CB    1 
ATOM   2149  C  CG1   . ILE A 1 267 ? 137.939 119.808 118.361 1.00 59.81 ?  267 ILE A CG1   1 
ATOM   2150  C  CG2   . ILE A 1 267 ? 137.265 118.232 120.196 1.00 57.14 ?  267 ILE A CG2   1 
ATOM   2151  C  CD1   . ILE A 1 267 ? 139.085 119.895 117.374 1.00 59.86 ?  267 ILE A CD1   1 
ATOM   2152  N  N     . SER A 1 268 ? 139.981 119.409 122.513 1.00 60.20 ?  268 SER A N     1 
ATOM   2153  C  CA    . SER A 1 268 ? 140.271 118.846 123.826 1.00 63.53 ?  268 SER A CA    1 
ATOM   2154  C  C     . SER A 1 268 ? 140.187 119.874 124.948 1.00 64.19 ?  268 SER A C     1 
ATOM   2155  O  O     . SER A 1 268 ? 140.280 119.490 126.119 1.00 63.68 ?  268 SER A O     1 
ATOM   2156  C  CB    . SER A 1 268 ? 141.659 118.203 123.824 1.00 63.60 ?  268 SER A CB    1 
ATOM   2157  O  OG    . SER A 1 268 ? 142.658 119.149 123.486 1.00 62.10 ?  268 SER A OG    1 
ATOM   2158  N  N     . ALA A 1 269 ? 140.025 121.155 124.624 1.00 66.10 ?  269 ALA A N     1 
ATOM   2159  C  CA    . ALA A 1 269 ? 139.963 122.188 125.648 1.00 65.74 ?  269 ALA A CA    1 
ATOM   2160  C  C     . ALA A 1 269 ? 138.746 121.990 126.546 1.00 66.79 ?  269 ALA A C     1 
ATOM   2161  O  O     . ALA A 1 269 ? 137.680 121.555 126.103 1.00 64.71 ?  269 ALA A O     1 
ATOM   2162  C  CB    . ALA A 1 269 ? 139.915 123.574 125.004 1.00 61.65 ?  269 ALA A CB    1 
ATOM   2163  N  N     . ASP A 1 270 ? 138.919 122.316 127.824 1.00 73.17 ?  270 ASP A N     1 
ATOM   2164  C  CA    . ASP A 1 270 ? 137.849 122.164 128.795 1.00 73.06 ?  270 ASP A CA    1 
ATOM   2165  C  C     . ASP A 1 270 ? 136.789 123.248 128.601 1.00 73.22 ?  270 ASP A C     1 
ATOM   2166  O  O     . ASP A 1 270 ? 136.942 124.177 127.802 1.00 73.93 ?  270 ASP A O     1 
ATOM   2167  C  CB    . ASP A 1 270 ? 138.404 122.213 130.218 1.00 73.27 ?  270 ASP A CB    1 
ATOM   2168  C  CG    . ASP A 1 270 ? 139.684 121.417 130.371 1.00 74.95 ?  270 ASP A CG    1 
ATOM   2169  O  OD1   . ASP A 1 270 ? 139.846 120.406 129.656 1.00 74.46 ?  270 ASP A OD1   1 
ATOM   2170  O  OD2   . ASP A 1 270 ? 140.528 121.801 131.209 1.00 73.37 -1 270 ASP A OD2   1 
ATOM   2171  N  N     . GLU A 1 271 ? 135.694 123.117 129.354 1.00 74.54 ?  271 GLU A N     1 
ATOM   2172  C  CA    . GLU A 1 271 ? 134.590 124.064 129.233 1.00 75.66 ?  271 GLU A CA    1 
ATOM   2173  C  C     . GLU A 1 271 ? 134.970 125.449 129.741 1.00 75.28 ?  271 GLU A C     1 
ATOM   2174  O  O     . GLU A 1 271 ? 134.408 126.449 129.282 1.00 74.37 ?  271 GLU A O     1 
ATOM   2175  C  CB    . GLU A 1 271 ? 133.366 123.540 129.983 1.00 74.59 ?  271 GLU A CB    1 
ATOM   2176  C  CG    . GLU A 1 271 ? 132.881 122.178 129.509 1.00 75.40 ?  271 GLU A CG    1 
ATOM   2177  C  CD    . GLU A 1 271 ? 132.815 122.073 127.997 1.00 76.58 ?  271 GLU A CD    1 
ATOM   2178  O  OE1   . GLU A 1 271 ? 132.212 122.963 127.360 1.00 75.75 ?  271 GLU A OE1   1 
ATOM   2179  O  OE2   . GLU A 1 271 ? 133.367 121.099 127.443 1.00 74.84 -1 271 GLU A OE2   1 
ATOM   2180  N  N     . ASP A 1 272 ? 135.909 125.531 130.679 1.00 69.39 ?  272 ASP A N     1 
ATOM   2181  C  CA    . ASP A 1 272 ? 136.375 126.810 131.197 1.00 70.33 ?  272 ASP A CA    1 
ATOM   2182  C  C     . ASP A 1 272 ? 137.494 127.413 130.357 1.00 70.67 ?  272 ASP A C     1 
ATOM   2183  O  O     . ASP A 1 272 ? 138.018 128.471 130.717 1.00 68.52 ?  272 ASP A O     1 
ATOM   2184  C  CB    . ASP A 1 272 ? 136.842 126.658 132.649 1.00 70.43 ?  272 ASP A CB    1 
ATOM   2185  C  CG    . ASP A 1 272 ? 138.076 125.786 132.780 1.00 71.48 ?  272 ASP A CG    1 
ATOM   2186  O  OD1   . ASP A 1 272 ? 138.301 124.932 131.897 1.00 70.47 ?  272 ASP A OD1   1 
ATOM   2187  O  OD2   . ASP A 1 272 ? 138.823 125.955 133.766 1.00 70.07 -1 272 ASP A OD2   1 
ATOM   2188  N  N     . VAL A 1 273 ? 137.876 126.761 129.258 1.00 65.21 ?  273 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 273 ? 138.927 127.244 128.376 1.00 64.67 ?  273 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 273 ? 138.395 127.570 126.987 1.00 62.53 ?  273 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 273 ? 138.768 128.591 126.397 1.00 65.25 ?  273 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 273 ? 140.086 126.226 128.288 1.00 66.28 ?  273 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 273 ? 141.048 126.592 127.168 1.00 63.57 ?  273 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 273 ? 140.816 126.137 129.618 1.00 64.79 ?  273 VAL A CG2   1 
ATOM   2195  N  N     . ARG A 1 274 ? 137.508 126.735 126.455 1.00 60.44 ?  274 ARG A N     1 
ATOM   2196  C  CA    . ARG A 1 274 ? 137.055 126.870 125.078 1.00 59.82 ?  274 ARG A CA    1 
ATOM   2197  C  C     . ARG A 1 274 ? 135.967 127.931 124.961 1.00 58.10 ?  274 ARG A C     1 
ATOM   2198  O  O     . ARG A 1 274 ? 135.036 127.971 125.770 1.00 58.12 ?  274 ARG A O     1 
ATOM   2199  C  CB    . ARG A 1 274 ? 136.536 125.528 124.561 1.00 59.95 ?  274 ARG A CB    1 
ATOM   2200  C  CG    . ARG A 1 274 ? 135.600 125.634 123.368 1.00 58.60 ?  274 ARG A CG    1 
ATOM   2201  C  CD    . ARG A 1 274 ? 135.632 124.374 122.520 1.00 58.80 ?  274 ARG A CD    1 
ATOM   2202  N  NE    . ARG A 1 274 ? 135.580 123.162 123.331 1.00 62.16 ?  274 ARG A NE    1 
ATOM   2203  C  CZ    . ARG A 1 274 ? 134.484 122.694 123.912 1.00 63.53 ?  274 ARG A CZ    1 
ATOM   2204  N  NH1   . ARG A 1 274 ? 133.319 123.310 123.789 1.00 62.50 1  274 ARG A NH1   1 
ATOM   2205  N  NH2   . ARG A 1 274 ? 134.557 121.577 124.631 1.00 63.03 ?  274 ARG A NH2   1 
ATOM   2206  N  N     . VAL A 1 275 ? 136.090 128.789 123.950 1.00 47.64 ?  275 VAL A N     1 
ATOM   2207  C  CA    . VAL A 1 275 ? 135.054 129.745 123.577 1.00 44.89 ?  275 VAL A CA    1 
ATOM   2208  C  C     . VAL A 1 275 ? 134.471 129.300 122.243 1.00 45.72 ?  275 VAL A C     1 
ATOM   2209  O  O     . VAL A 1 275 ? 135.212 129.047 121.286 1.00 47.61 ?  275 VAL A O     1 
ATOM   2210  C  CB    . VAL A 1 275 ? 135.606 131.181 123.501 1.00 44.54 ?  275 VAL A CB    1 
ATOM   2211  C  CG1   . VAL A 1 275 ? 135.838 131.731 124.899 1.00 42.69 ?  275 VAL A CG1   1 
ATOM   2212  C  CG2   . VAL A 1 275 ? 136.899 131.224 122.703 1.00 44.81 ?  275 VAL A CG2   1 
ATOM   2213  N  N     . LYS A 1 276 ? 133.145 129.186 122.183 1.00 46.73 ?  276 LYS A N     1 
ATOM   2214  C  CA    . LYS A 1 276 ? 132.486 128.580 121.033 1.00 47.97 ?  276 LYS A CA    1 
ATOM   2215  C  C     . LYS A 1 276 ? 131.965 129.587 120.018 1.00 47.05 ?  276 LYS A C     1 
ATOM   2216  O  O     . LYS A 1 276 ? 132.033 129.322 118.814 1.00 52.80 ?  276 LYS A O     1 
ATOM   2217  C  CB    . LYS A 1 276 ? 131.325 127.691 121.497 1.00 49.01 ?  276 LYS A CB    1 
ATOM   2218  C  CG    . LYS A 1 276 ? 130.370 128.367 122.469 1.00 52.48 ?  276 LYS A CG    1 
ATOM   2219  C  CD    . LYS A 1 276 ? 129.420 127.363 123.107 1.00 50.48 ?  276 LYS A CD    1 
ATOM   2220  C  CE    . LYS A 1 276 ? 130.164 126.137 123.614 1.00 49.46 ?  276 LYS A CE    1 
ATOM   2221  N  NZ    . LYS A 1 276 ? 131.226 126.496 124.595 1.00 48.12 1  276 LYS A NZ    1 
ATOM   2222  N  N     . THR A 1 277 ? 131.449 130.731 120.461 1.00 38.15 ?  277 THR A N     1 
ATOM   2223  C  CA    . THR A 1 277 ? 130.909 131.739 119.560 1.00 38.69 ?  277 THR A CA    1 
ATOM   2224  C  C     . THR A 1 277 ? 131.866 132.900 119.335 1.00 42.36 ?  277 THR A C     1 
ATOM   2225  O  O     . THR A 1 277 ? 131.456 133.932 118.796 1.00 41.83 ?  277 THR A O     1 
ATOM   2226  C  CB    . THR A 1 277 ? 129.570 132.260 120.087 1.00 41.43 ?  277 THR A CB    1 
ATOM   2227  O  OG1   . THR A 1 277 ? 129.799 133.162 121.177 1.00 35.00 ?  277 THR A OG1   1 
ATOM   2228  C  CG2   . THR A 1 277 ? 128.700 131.104 120.556 1.00 41.22 ?  277 THR A CG2   1 
ATOM   2229  N  N     . LEU A 1 278 ? 133.125 132.760 119.737 1.00 33.87 ?  278 LEU A N     1 
ATOM   2230  C  CA    . LEU A 1 278 ? 134.129 133.805 119.577 1.00 31.20 ?  278 LEU A CA    1 
ATOM   2231  C  C     . LEU A 1 278 ? 135.193 133.313 118.605 1.00 25.43 ?  278 LEU A C     1 
ATOM   2232  O  O     . LEU A 1 278 ? 136.008 132.454 118.952 1.00 34.43 ?  278 LEU A O     1 
ATOM   2233  C  CB    . LEU A 1 278 ? 134.750 134.176 120.921 1.00 28.77 ?  278 LEU A CB    1 
ATOM   2234  C  CG    . LEU A 1 278 ? 135.531 135.489 120.965 1.00 25.02 ?  278 LEU A CG    1 
ATOM   2235  C  CD1   . LEU A 1 278 ? 134.586 136.671 121.068 1.00 24.11 ?  278 LEU A CD1   1 
ATOM   2236  C  CD2   . LEU A 1 278 ? 136.515 135.487 122.120 1.00 31.95 ?  278 LEU A CD2   1 
ATOM   2237  N  N     . SER A 1 279 ? 135.181 133.856 117.392 1.00 26.11 ?  279 SER A N     1 
ATOM   2238  C  CA    . SER A 1 279 ? 136.254 133.595 116.448 1.00 21.19 ?  279 SER A CA    1 
ATOM   2239  C  C     . SER A 1 279 ? 137.556 134.197 116.961 1.00 20.60 ?  279 SER A C     1 
ATOM   2240  O  O     . SER A 1 279 ? 137.557 135.164 117.726 1.00 33.10 ?  279 SER A O     1 
ATOM   2241  C  CB    . SER A 1 279 ? 135.913 134.174 115.077 1.00 17.65 ?  279 SER A CB    1 
ATOM   2242  O  OG    . SER A 1 279 ? 134.853 133.458 114.469 1.00 25.68 ?  279 SER A OG    1 
ATOM   2243  N  N     . ILE A 1 280 ? 138.673 133.609 116.549 1.00 18.70 ?  280 ILE A N     1 
ATOM   2244  C  CA    . ILE A 1 280 ? 139.983 134.076 116.979 1.00 22.67 ?  280 ILE A CA    1 
ATOM   2245  C  C     . ILE A 1 280 ? 140.844 134.347 115.756 1.00 23.14 ?  280 ILE A C     1 
ATOM   2246  O  O     . ILE A 1 280 ? 140.770 133.625 114.755 1.00 26.18 ?  280 ILE A O     1 
ATOM   2247  C  CB    . ILE A 1 280 ? 140.680 133.077 117.929 1.00 17.83 ?  280 ILE A CB    1 
ATOM   2248  C  CG1   . ILE A 1 280 ? 140.946 131.743 117.234 1.00 23.84 ?  280 ILE A CG1   1 
ATOM   2249  C  CG2   . ILE A 1 280 ? 139.851 132.876 119.185 1.00 20.13 ?  280 ILE A CG2   1 
ATOM   2250  C  CD1   . ILE A 1 280 ? 142.119 130.989 117.824 1.00 18.96 ?  280 ILE A CD1   1 
ATOM   2251  N  N     . GLY A 1 281 ? 141.632 135.409 115.828 1.00 13.73 ?  281 GLY A N     1 
ATOM   2252  C  CA    . GLY A 1 281 ? 142.620 135.696 114.812 1.00 4.47  ?  281 GLY A CA    1 
ATOM   2253  C  C     . GLY A 1 281 ? 143.953 136.009 115.457 1.00 10.46 ?  281 GLY A C     1 
ATOM   2254  O  O     . GLY A 1 281 ? 144.021 136.543 116.562 1.00 18.34 ?  281 GLY A O     1 
ATOM   2255  N  N     . VAL A 1 282 ? 145.020 135.658 114.748 1.00 15.23 ?  282 VAL A N     1 
ATOM   2256  C  CA    . VAL A 1 282 ? 146.382 135.850 115.230 1.00 12.71 ?  282 VAL A CA    1 
ATOM   2257  C  C     . VAL A 1 282 ? 147.085 136.835 114.310 1.00 13.55 ?  282 VAL A C     1 
ATOM   2258  O  O     . VAL A 1 282 ? 147.047 136.687 113.082 1.00 17.64 ?  282 VAL A O     1 
ATOM   2259  C  CB    . VAL A 1 282 ? 147.147 134.517 115.308 1.00 14.51 ?  282 VAL A CB    1 
ATOM   2260  C  CG1   . VAL A 1 282 ? 148.627 134.764 115.519 1.00 19.00 ?  282 VAL A CG1   1 
ATOM   2261  C  CG2   . VAL A 1 282 ? 146.595 133.671 116.435 1.00 19.47 ?  282 VAL A CG2   1 
ATOM   2262  N  N     . VAL A 1 283 ? 147.712 137.844 114.904 1.00 12.13 ?  283 VAL A N     1 
ATOM   2263  C  CA    . VAL A 1 283 ? 148.493 138.828 114.166 1.00 11.66 ?  283 VAL A CA    1 
ATOM   2264  C  C     . VAL A 1 283 ? 149.951 138.395 114.200 1.00 16.58 ?  283 VAL A C     1 
ATOM   2265  O  O     . VAL A 1 283 ? 150.538 138.249 115.277 1.00 25.42 ?  283 VAL A O     1 
ATOM   2266  C  CB    . VAL A 1 283 ? 148.316 140.232 114.761 1.00 11.36 ?  283 VAL A CB    1 
ATOM   2267  C  CG1   . VAL A 1 283 ? 148.944 141.271 113.858 1.00 9.15  ?  283 VAL A CG1   1 
ATOM   2268  C  CG2   . VAL A 1 283 ? 146.840 140.522 114.976 1.00 14.54 ?  283 VAL A CG2   1 
ATOM   2269  N  N     . ILE A 1 284 ? 150.535 138.191 113.028 1.00 14.52 ?  284 ILE A N     1 
ATOM   2270  C  CA    . ILE A 1 284 ? 151.879 137.649 112.893 1.00 14.52 ?  284 ILE A CA    1 
ATOM   2271  C  C     . ILE A 1 284 ? 152.768 138.713 112.262 1.00 18.20 ?  284 ILE A C     1 
ATOM   2272  O  O     . ILE A 1 284 ? 152.717 138.943 111.054 1.00 20.15 ?  284 ILE A O     1 
ATOM   2273  C  CB    . ILE A 1 284 ? 151.885 136.356 112.059 1.00 16.43 ?  284 ILE A CB    1 
ATOM   2274  C  CG1   . ILE A 1 284 ? 150.968 135.311 112.697 1.00 16.93 ?  284 ILE A CG1   1 
ATOM   2275  C  CG2   . ILE A 1 284 ? 153.298 135.815 111.923 1.00 17.23 ?  284 ILE A CG2   1 
ATOM   2276  C  CD1   . ILE A 1 284 ? 151.031 133.956 112.032 1.00 19.37 ?  284 ILE A CD1   1 
ATOM   2277  N  N     . PRO A 1 285 ? 153.597 139.387 113.054 1.00 27.08 ?  285 PRO A N     1 
ATOM   2278  C  CA    . PRO A 1 285 ? 154.571 140.320 112.480 1.00 25.81 ?  285 PRO A CA    1 
ATOM   2279  C  C     . PRO A 1 285 ? 155.652 139.579 111.707 1.00 23.52 ?  285 PRO A C     1 
ATOM   2280  O  O     . PRO A 1 285 ? 155.831 138.366 111.833 1.00 25.24 ?  285 PRO A O     1 
ATOM   2281  C  CB    . PRO A 1 285 ? 155.154 141.033 113.706 1.00 19.49 ?  285 PRO A CB    1 
ATOM   2282  C  CG    . PRO A 1 285 ? 154.185 140.766 114.814 1.00 17.59 ?  285 PRO A CG    1 
ATOM   2283  C  CD    . PRO A 1 285 ? 153.602 139.423 114.524 1.00 21.54 ?  285 PRO A CD    1 
ATOM   2284  N  N     . ASP A 1 286 ? 156.379 140.340 110.883 1.00 26.51 ?  286 ASP A N     1 
ATOM   2285  C  CA    . ASP A 1 286 ? 157.461 139.751 110.101 1.00 24.40 ?  286 ASP A CA    1 
ATOM   2286  C  C     . ASP A 1 286 ? 158.548 139.168 110.992 1.00 29.80 ?  286 ASP A C     1 
ATOM   2287  O  O     . ASP A 1 286 ? 159.263 138.251 110.573 1.00 32.08 ?  286 ASP A O     1 
ATOM   2288  C  CB    . ASP A 1 286 ? 158.063 140.792 109.158 1.00 24.91 ?  286 ASP A CB    1 
ATOM   2289  C  CG    . ASP A 1 286 ? 157.498 140.704 107.758 1.00 36.92 ?  286 ASP A CG    1 
ATOM   2290  O  OD1   . ASP A 1 286 ? 156.456 140.041 107.578 1.00 36.04 ?  286 ASP A OD1   1 
ATOM   2291  O  OD2   . ASP A 1 286 ? 158.094 141.301 106.836 1.00 39.10 -1 286 ASP A OD2   1 
ATOM   2292  N  N     . LYS A 1 287 ? 158.693 139.685 112.215 1.00 30.46 ?  287 LYS A N     1 
ATOM   2293  C  CA    . LYS A 1 287 ? 159.721 139.177 113.117 1.00 28.00 ?  287 LYS A CA    1 
ATOM   2294  C  C     . LYS A 1 287 ? 159.477 137.715 113.467 1.00 29.31 ?  287 LYS A C     1 
ATOM   2295  O  O     . LYS A 1 287 ? 160.422 136.921 113.535 1.00 36.10 ?  287 LYS A O     1 
ATOM   2296  C  CB    . LYS A 1 287 ? 159.777 140.030 114.383 1.00 31.50 ?  287 LYS A CB    1 
ATOM   2297  C  CG    . LYS A 1 287 ? 160.989 139.748 115.253 1.00 27.46 ?  287 LYS A CG    1 
ATOM   2298  C  CD    . LYS A 1 287 ? 162.262 139.764 114.425 1.00 30.56 ?  287 LYS A CD    1 
ATOM   2299  C  CE    . LYS A 1 287 ? 163.497 139.686 115.301 1.00 31.46 ?  287 LYS A CE    1 
ATOM   2300  N  NZ    . LYS A 1 287 ? 164.747 139.813 114.504 1.00 34.93 1  287 LYS A NZ    1 
ATOM   2301  N  N     . PHE A 1 288 ? 158.217 137.340 113.697 1.00 24.06 ?  288 PHE A N     1 
ATOM   2302  C  CA    . PHE A 1 288 ? 157.907 135.944 113.989 1.00 24.02 ?  288 PHE A CA    1 
ATOM   2303  C  C     . PHE A 1 288 ? 158.248 135.045 112.808 1.00 24.75 ?  288 PHE A C     1 
ATOM   2304  O  O     . PHE A 1 288 ? 158.777 133.941 112.989 1.00 36.24 ?  288 PHE A O     1 
ATOM   2305  C  CB    . PHE A 1 288 ? 156.432 135.800 114.363 1.00 25.06 ?  288 PHE A CB    1 
ATOM   2306  C  CG    . PHE A 1 288 ? 156.041 134.403 114.755 1.00 26.56 ?  288 PHE A CG    1 
ATOM   2307  C  CD1   . PHE A 1 288 ? 156.252 133.949 116.046 1.00 27.58 ?  288 PHE A CD1   1 
ATOM   2308  C  CD2   . PHE A 1 288 ? 155.465 133.546 113.833 1.00 22.72 ?  288 PHE A CD2   1 
ATOM   2309  C  CE1   . PHE A 1 288 ? 155.895 132.666 116.409 1.00 26.22 ?  288 PHE A CE1   1 
ATOM   2310  C  CE2   . PHE A 1 288 ? 155.107 132.262 114.191 1.00 24.98 ?  288 PHE A CE2   1 
ATOM   2311  C  CZ    . PHE A 1 288 ? 155.321 131.822 115.480 1.00 29.33 ?  288 PHE A CZ    1 
ATOM   2312  N  N     . VAL A 1 289 ? 157.953 135.501 111.589 1.00 24.93 ?  289 VAL A N     1 
ATOM   2313  C  CA    . VAL A 1 289 ? 158.255 134.701 110.409 1.00 28.22 ?  289 VAL A CA    1 
ATOM   2314  C  C     . VAL A 1 289 ? 159.762 134.573 110.223 1.00 29.88 ?  289 VAL A C     1 
ATOM   2315  O  O     . VAL A 1 289 ? 160.262 133.517 109.822 1.00 33.12 ?  289 VAL A O     1 
ATOM   2316  C  CB    . VAL A 1 289 ? 157.576 135.304 109.166 1.00 31.83 ?  289 VAL A CB    1 
ATOM   2317  C  CG1   . VAL A 1 289 ? 157.659 134.339 107.996 1.00 25.97 ?  289 VAL A CG1   1 
ATOM   2318  C  CG2   . VAL A 1 289 ? 156.129 135.656 109.473 1.00 26.24 ?  289 VAL A CG2   1 
ATOM   2319  N  N     . GLU A 1 290 ? 160.510 135.644 110.506 1.00 33.29 ?  290 GLU A N     1 
ATOM   2320  C  CA    . GLU A 1 290 ? 161.966 135.568 110.429 1.00 32.38 ?  290 GLU A CA    1 
ATOM   2321  C  C     . GLU A 1 290 ? 162.524 134.603 111.467 1.00 35.00 ?  290 GLU A C     1 
ATOM   2322  O  O     . GLU A 1 290 ? 163.447 133.833 111.178 1.00 41.47 ?  290 GLU A O     1 
ATOM   2323  C  CB    . GLU A 1 290 ? 162.581 136.956 110.605 1.00 33.41 ?  290 GLU A CB    1 
ATOM   2324  C  CG    . GLU A 1 290 ? 162.548 137.822 109.358 1.00 38.34 ?  290 GLU A CG    1 
ATOM   2325  C  CD    . GLU A 1 290 ? 161.937 139.186 109.605 1.00 39.81 ?  290 GLU A CD    1 
ATOM   2326  O  OE1   . GLU A 1 290 ? 161.171 139.661 108.741 1.00 38.86 ?  290 GLU A OE1   1 
ATOM   2327  O  OE2   . GLU A 1 290 ? 162.219 139.784 110.665 1.00 40.07 -1 290 GLU A OE2   1 
ATOM   2328  N  N     . LEU A 1 291 ? 161.983 134.637 112.687 1.00 32.62 ?  291 LEU A N     1 
ATOM   2329  C  CA    . LEU A 1 291 ? 162.449 133.731 113.731 1.00 29.33 ?  291 LEU A CA    1 
ATOM   2330  C  C     . LEU A 1 291 ? 162.149 132.279 113.380 1.00 32.32 ?  291 LEU A C     1 
ATOM   2331  O  O     . LEU A 1 291 ? 162.991 131.399 113.592 1.00 39.75 ?  291 LEU A O     1 
ATOM   2332  C  CB    . LEU A 1 291 ? 161.813 134.103 115.071 1.00 31.03 ?  291 LEU A CB    1 
ATOM   2333  C  CG    . LEU A 1 291 ? 162.274 135.425 115.683 1.00 32.77 ?  291 LEU A CG    1 
ATOM   2334  C  CD1   . LEU A 1 291 ? 161.264 135.926 116.701 1.00 27.11 ?  291 LEU A CD1   1 
ATOM   2335  C  CD2   . LEU A 1 291 ? 163.647 135.273 116.312 1.00 32.96 ?  291 LEU A CD2   1 
ATOM   2336  N  N     . ALA A 1 292 ? 160.955 132.010 112.851 1.00 33.22 ?  292 ALA A N     1 
ATOM   2337  C  CA    . ALA A 1 292 ? 160.620 130.650 112.439 1.00 31.63 ?  292 ALA A CA    1 
ATOM   2338  C  C     . ALA A 1 292 ? 161.481 130.200 111.265 1.00 32.39 ?  292 ALA A C     1 
ATOM   2339  O  O     . ALA A 1 292 ? 161.899 129.038 111.204 1.00 37.80 ?  292 ALA A O     1 
ATOM   2340  C  CB    . ALA A 1 292 ? 159.137 130.559 112.087 1.00 30.62 ?  292 ALA A CB    1 
ATOM   2341  N  N     . ARG A 1 293 ? 161.750 131.106 110.323 1.00 34.05 ?  293 ARG A N     1 
ATOM   2342  C  CA    . ARG A 1 293 ? 162.548 130.762 109.151 1.00 33.45 ?  293 ARG A CA    1 
ATOM   2343  C  C     . ARG A 1 293 ? 163.968 130.371 109.537 1.00 39.26 ?  293 ARG A C     1 
ATOM   2344  O  O     . ARG A 1 293 ? 164.518 129.400 109.004 1.00 43.88 ?  293 ARG A O     1 
ATOM   2345  C  CB    . ARG A 1 293 ? 162.557 131.939 108.177 1.00 34.13 ?  293 ARG A CB    1 
ATOM   2346  C  CG    . ARG A 1 293 ? 163.414 131.741 106.943 1.00 34.36 ?  293 ARG A CG    1 
ATOM   2347  C  CD    . ARG A 1 293 ? 163.561 133.046 106.182 1.00 38.71 ?  293 ARG A CD    1 
ATOM   2348  N  NE    . ARG A 1 293 ? 162.291 133.757 106.091 1.00 40.23 ?  293 ARG A NE    1 
ATOM   2349  C  CZ    . ARG A 1 293 ? 162.131 135.043 106.373 1.00 39.33 ?  293 ARG A CZ    1 
ATOM   2350  N  NH1   . ARG A 1 293 ? 163.147 135.800 106.752 1.00 37.97 1  293 ARG A NH1   1 
ATOM   2351  N  NH2   . ARG A 1 293 ? 160.919 135.582 106.272 1.00 35.71 ?  293 ARG A NH2   1 
ATOM   2352  N  N     . GLU A 1 294 ? 164.576 131.111 110.459 1.00 41.45 ?  294 GLU A N     1 
ATOM   2353  C  CA    . GLU A 1 294 ? 165.930 130.820 110.910 1.00 39.06 ?  294 GLU A CA    1 
ATOM   2354  C  C     . GLU A 1 294 ? 165.972 129.785 112.024 1.00 40.16 ?  294 GLU A C     1 
ATOM   2355  O  O     . GLU A 1 294 ? 167.065 129.456 112.498 1.00 42.64 ?  294 GLU A O     1 
ATOM   2356  C  CB    . GLU A 1 294 ? 166.612 132.108 111.378 1.00 39.21 ?  294 GLU A CB    1 
ATOM   2357  C  CG    . GLU A 1 294 ? 167.047 133.025 110.248 1.00 41.33 ?  294 GLU A CG    1 
ATOM   2358  C  CD    . GLU A 1 294 ? 166.488 134.426 110.390 1.00 44.89 ?  294 GLU A CD    1 
ATOM   2359  O  OE1   . GLU A 1 294 ? 166.310 134.883 111.538 1.00 45.92 ?  294 GLU A OE1   1 
ATOM   2360  O  OE2   . GLU A 1 294 ? 166.224 135.070 109.353 1.00 46.51 -1 294 GLU A OE2   1 
ATOM   2361  N  N     . ASP A 1 295 ? 164.816 129.285 112.459 1.00 38.72 ?  295 ASP A N     1 
ATOM   2362  C  CA    . ASP A 1 295 ? 164.674 128.288 113.516 1.00 37.97 ?  295 ASP A CA    1 
ATOM   2363  C  C     . ASP A 1 295 ? 165.167 128.782 114.870 1.00 44.50 ?  295 ASP A C     1 
ATOM   2364  O  O     . ASP A 1 295 ? 165.289 127.985 115.807 1.00 44.19 ?  295 ASP A O     1 
ATOM   2365  C  CB    . ASP A 1 295 ? 165.381 126.974 113.155 1.00 40.78 ?  295 ASP A CB    1 
ATOM   2366  C  CG    . ASP A 1 295 ? 164.560 125.752 113.515 1.00 44.89 ?  295 ASP A CG    1 
ATOM   2367  O  OD1   . ASP A 1 295 ? 163.589 125.893 114.288 1.00 46.03 ?  295 ASP A OD1   1 
ATOM   2368  O  OD2   . ASP A 1 295 ? 164.886 124.650 113.026 1.00 42.65 -1 295 ASP A OD2   1 
ATOM   2369  N  N     . LYS A 1 296 ? 165.457 130.074 115.003 1.00 43.47 ?  296 LYS A N     1 
ATOM   2370  C  CA    . LYS A 1 296 ? 165.812 130.627 116.301 1.00 41.60 ?  296 LYS A CA    1 
ATOM   2371  C  C     . LYS A 1 296 ? 164.604 130.599 117.226 1.00 41.53 ?  296 LYS A C     1 
ATOM   2372  O  O     . LYS A 1 296 ? 163.479 130.886 116.810 1.00 45.89 ?  296 LYS A O     1 
ATOM   2373  C  CB    . LYS A 1 296 ? 166.325 132.059 116.159 1.00 42.27 ?  296 LYS A CB    1 
ATOM   2374  C  CG    . LYS A 1 296 ? 167.414 132.244 115.121 1.00 44.14 ?  296 LYS A CG    1 
ATOM   2375  C  CD    . LYS A 1 296 ? 167.364 133.641 114.527 1.00 42.91 ?  296 LYS A CD    1 
ATOM   2376  C  CE    . LYS A 1 296 ? 168.752 134.245 114.415 1.00 43.56 ?  296 LYS A CE    1 
ATOM   2377  N  NZ    . LYS A 1 296 ? 169.623 133.467 113.492 1.00 44.16 1  296 LYS A NZ    1 
ATOM   2378  N  N     . ALA A 1 297 ? 164.840 130.247 118.486 1.00 40.88 ?  297 ALA A N     1 
ATOM   2379  C  CA    . ALA A 1 297 ? 163.763 130.243 119.464 1.00 42.43 ?  297 ALA A CA    1 
ATOM   2380  C  C     . ALA A 1 297 ? 163.272 131.662 119.714 1.00 40.42 ?  297 ALA A C     1 
ATOM   2381  O  O     . ALA A 1 297 ? 164.066 132.592 119.878 1.00 41.09 ?  297 ALA A O     1 
ATOM   2382  C  CB    . ALA A 1 297 ? 164.234 129.608 120.769 1.00 37.53 ?  297 ALA A CB    1 
ATOM   2383  N  N     . ALA A 1 298 ? 161.954 131.825 119.744 1.00 35.05 ?  298 ALA A N     1 
ATOM   2384  C  CA    . ALA A 1 298 ? 161.340 133.130 119.896 1.00 34.96 ?  298 ALA A CA    1 
ATOM   2385  C  C     . ALA A 1 298 ? 160.941 133.355 121.351 1.00 35.60 ?  298 ALA A C     1 
ATOM   2386  O  O     . ALA A 1 298 ? 161.014 132.459 122.194 1.00 39.04 ?  298 ALA A O     1 
ATOM   2387  C  CB    . ALA A 1 298 ? 160.132 133.265 118.967 1.00 33.74 ?  298 ALA A CB    1 
ATOM   2388  N  N     . TYR A 1 299 ? 160.502 134.575 121.643 1.00 33.59 ?  299 TYR A N     1 
ATOM   2389  C  CA    . TYR A 1 299 ? 160.050 134.942 122.976 1.00 27.91 ?  299 TYR A CA    1 
ATOM   2390  C  C     . TYR A 1 299 ? 158.670 135.568 122.877 1.00 29.08 ?  299 TYR A C     1 
ATOM   2391  O  O     . TYR A 1 299 ? 158.449 136.464 122.057 1.00 30.35 ?  299 TYR A O     1 
ATOM   2392  C  CB    . TYR A 1 299 ? 161.027 135.914 123.644 1.00 29.77 ?  299 TYR A CB    1 
ATOM   2393  C  CG    . TYR A 1 299 ? 162.301 135.263 124.125 1.00 31.98 ?  299 TYR A CG    1 
ATOM   2394  C  CD1   . TYR A 1 299 ? 162.343 134.584 125.336 1.00 34.99 ?  299 TYR A CD1   1 
ATOM   2395  C  CD2   . TYR A 1 299 ? 163.460 135.320 123.365 1.00 32.52 ?  299 TYR A CD2   1 
ATOM   2396  C  CE1   . TYR A 1 299 ? 163.506 133.985 125.777 1.00 35.03 ?  299 TYR A CE1   1 
ATOM   2397  C  CE2   . TYR A 1 299 ? 164.626 134.725 123.797 1.00 33.28 ?  299 TYR A CE2   1 
ATOM   2398  C  CZ    . TYR A 1 299 ? 164.645 134.058 125.003 1.00 35.74 ?  299 TYR A CZ    1 
ATOM   2399  O  OH    . TYR A 1 299 ? 165.806 133.463 125.438 1.00 39.40 ?  299 TYR A OH    1 
ATOM   2400  N  N     . VAL A 1 300 ? 157.747 135.092 123.705 1.00 32.74 ?  300 VAL A N     1 
ATOM   2401  C  CA    . VAL A 1 300 ? 156.437 135.713 123.861 1.00 27.48 ?  300 VAL A CA    1 
ATOM   2402  C  C     . VAL A 1 300 ? 156.485 136.580 125.110 1.00 28.99 ?  300 VAL A C     1 
ATOM   2403  O  O     . VAL A 1 300 ? 156.901 136.120 126.179 1.00 35.40 ?  300 VAL A O     1 
ATOM   2404  C  CB    . VAL A 1 300 ? 155.319 134.660 123.946 1.00 25.59 ?  300 VAL A CB    1 
ATOM   2405  C  CG1   . VAL A 1 300 ? 154.974 134.143 122.559 1.00 26.29 ?  300 VAL A CG1   1 
ATOM   2406  C  CG2   . VAL A 1 300 ? 155.719 133.518 124.863 1.00 28.34 ?  300 VAL A CG2   1 
ATOM   2407  N  N     . PHE A 1 301 ? 156.078 137.834 124.976 1.00 22.22 ?  301 PHE A N     1 
ATOM   2408  C  CA    . PHE A 1 301 ? 156.314 138.832 126.006 1.00 24.64 ?  301 PHE A CA    1 
ATOM   2409  C  C     . PHE A 1 301 ? 155.064 139.114 126.828 1.00 29.79 ?  301 PHE A C     1 
ATOM   2410  O  O     . PHE A 1 301 ? 153.934 138.979 126.352 1.00 32.59 ?  301 PHE A O     1 
ATOM   2411  C  CB    . PHE A 1 301 ? 156.828 140.131 125.384 1.00 23.17 ?  301 PHE A CB    1 
ATOM   2412  C  CG    . PHE A 1 301 ? 158.018 139.939 124.495 1.00 28.71 ?  301 PHE A CG    1 
ATOM   2413  C  CD1   . PHE A 1 301 ? 159.281 139.803 125.040 1.00 27.45 ?  301 PHE A CD1   1 
ATOM   2414  C  CD2   . PHE A 1 301 ? 157.875 139.878 123.120 1.00 27.89 ?  301 PHE A CD2   1 
ATOM   2415  C  CE1   . PHE A 1 301 ? 160.382 139.617 124.235 1.00 27.89 ?  301 PHE A CE1   1 
ATOM   2416  C  CE2   . PHE A 1 301 ? 158.976 139.694 122.308 1.00 26.73 ?  301 PHE A CE2   1 
ATOM   2417  C  CZ    . PHE A 1 301 ? 160.232 139.564 122.868 1.00 29.84 ?  301 PHE A CZ    1 
ATOM   2418  N  N     . TYR A 1 302 ? 155.290 139.500 128.081 1.00 27.90 ?  302 TYR A N     1 
ATOM   2419  C  CA    . TYR A 1 302 ? 154.230 139.983 128.952 1.00 24.69 ?  302 TYR A CA    1 
ATOM   2420  C  C     . TYR A 1 302 ? 153.969 141.447 128.626 1.00 28.70 ?  302 TYR A C     1 
ATOM   2421  O  O     . TYR A 1 302 ? 154.851 142.294 128.810 1.00 30.11 ?  302 TYR A O     1 
ATOM   2422  C  CB    . TYR A 1 302 ? 154.609 139.811 130.422 1.00 25.69 ?  302 TYR A CB    1 
ATOM   2423  C  CG    . TYR A 1 302 ? 154.590 138.378 130.902 1.00 28.28 ?  302 TYR A CG    1 
ATOM   2424  C  CD1   . TYR A 1 302 ? 155.568 137.478 130.507 1.00 27.90 ?  302 TYR A CD1   1 
ATOM   2425  C  CD2   . TYR A 1 302 ? 153.592 137.927 131.751 1.00 29.97 ?  302 TYR A CD2   1 
ATOM   2426  C  CE1   . TYR A 1 302 ? 155.552 136.170 130.946 1.00 26.48 ?  302 TYR A CE1   1 
ATOM   2427  C  CE2   . TYR A 1 302 ? 153.566 136.623 132.197 1.00 30.24 ?  302 TYR A CE2   1 
ATOM   2428  C  CZ    . TYR A 1 302 ? 154.551 135.749 131.797 1.00 33.79 ?  302 TYR A CZ    1 
ATOM   2429  O  OH    . TYR A 1 302 ? 154.526 134.447 132.236 1.00 34.01 ?  302 TYR A OH    1 
ATOM   2430  N  N     . PRO A 1 303 ? 152.779 141.775 128.122 1.00 24.50 ?  303 PRO A N     1 
ATOM   2431  C  CA    . PRO A 1 303 ? 152.533 143.147 127.649 1.00 21.46 ?  303 PRO A CA    1 
ATOM   2432  C  C     . PRO A 1 303 ? 152.653 144.208 128.726 1.00 28.11 ?  303 PRO A C     1 
ATOM   2433  O  O     . PRO A 1 303 ? 153.109 145.320 128.434 1.00 32.36 ?  303 PRO A O     1 
ATOM   2434  C  CB    . PRO A 1 303 ? 151.102 143.069 127.099 1.00 24.61 ?  303 PRO A CB    1 
ATOM   2435  C  CG    . PRO A 1 303 ? 150.886 141.628 126.812 1.00 26.14 ?  303 PRO A CG    1 
ATOM   2436  C  CD    . PRO A 1 303 ? 151.634 140.889 127.865 1.00 25.81 ?  303 PRO A CD    1 
ATOM   2437  N  N     . HIS A 1 304 ? 152.255 143.906 129.964 1.00 29.80 ?  304 HIS A N     1 
ATOM   2438  C  CA    . HIS A 1 304 ? 152.264 144.932 130.999 1.00 24.97 ?  304 HIS A CA    1 
ATOM   2439  C  C     . HIS A 1 304 ? 153.681 145.310 131.402 1.00 28.58 ?  304 HIS A C     1 
ATOM   2440  O  O     . HIS A 1 304 ? 153.940 146.475 131.714 1.00 36.19 ?  304 HIS A O     1 
ATOM   2441  C  CB    . HIS A 1 304 ? 151.472 144.468 132.219 1.00 28.66 ?  304 HIS A CB    1 
ATOM   2442  C  CG    . HIS A 1 304 ? 151.247 145.545 133.234 1.00 30.65 ?  304 HIS A CG    1 
ATOM   2443  N  ND1   . HIS A 1 304 ? 151.429 145.346 134.585 1.00 33.01 ?  304 HIS A ND1   1 
ATOM   2444  C  CD2   . HIS A 1 304 ? 150.857 146.834 133.093 1.00 29.10 ?  304 HIS A CD2   1 
ATOM   2445  C  CE1   . HIS A 1 304 ? 151.158 146.465 135.234 1.00 32.39 ?  304 HIS A CE1   1 
ATOM   2446  N  NE2   . HIS A 1 304 ? 150.809 147.384 134.351 1.00 30.65 ?  304 HIS A NE2   1 
ATOM   2447  N  N     . THR A 1 305 ? 154.607 144.348 131.410 1.00 29.10 ?  305 THR A N     1 
ATOM   2448  C  CA    . THR A 1 305 ? 156.000 144.673 131.700 1.00 32.57 ?  305 THR A CA    1 
ATOM   2449  C  C     . THR A 1 305 ? 156.585 145.580 130.625 1.00 27.80 ?  305 THR A C     1 
ATOM   2450  O  O     . THR A 1 305 ? 157.316 146.530 130.931 1.00 33.42 ?  305 THR A O     1 
ATOM   2451  C  CB    . THR A 1 305 ? 156.826 143.394 131.839 1.00 31.42 ?  305 THR A CB    1 
ATOM   2452  O  OG1   . THR A 1 305 ? 157.043 142.811 130.548 1.00 31.84 ?  305 THR A OG1   1 
ATOM   2453  C  CG2   . THR A 1 305 ? 156.105 142.393 132.724 1.00 29.19 ?  305 THR A CG2   1 
ATOM   2454  N  N     . ILE A 1 306 ? 156.266 145.308 129.358 1.00 32.77 ?  306 ILE A N     1 
ATOM   2455  C  CA    . ILE A 1 306 ? 156.713 146.176 128.273 1.00 32.57 ?  306 ILE A CA    1 
ATOM   2456  C  C     . ILE A 1 306 ? 156.110 147.567 128.423 1.00 31.32 ?  306 ILE A C     1 
ATOM   2457  O  O     . ILE A 1 306 ? 156.791 148.581 128.223 1.00 32.80 ?  306 ILE A O     1 
ATOM   2458  C  CB    . ILE A 1 306 ? 156.365 145.545 126.913 1.00 28.41 ?  306 ILE A CB    1 
ATOM   2459  C  CG1   . ILE A 1 306 ? 157.370 144.444 126.568 1.00 32.43 ?  306 ILE A CG1   1 
ATOM   2460  C  CG2   . ILE A 1 306 ? 156.317 146.601 125.821 1.00 31.73 ?  306 ILE A CG2   1 
ATOM   2461  C  CD1   . ILE A 1 306 ? 157.086 143.747 125.268 1.00 31.27 ?  306 ILE A CD1   1 
ATOM   2462  N  N     . TYR A 1 307 ? 154.825 147.640 128.774 1.00 31.91 ?  307 TYR A N     1 
ATOM   2463  C  CA    . TYR A 1 307 ? 154.180 148.936 128.958 1.00 31.01 ?  307 TYR A CA    1 
ATOM   2464  C  C     . TYR A 1 307 ? 154.814 149.712 130.105 1.00 33.45 ?  307 TYR A C     1 
ATOM   2465  O  O     . TYR A 1 307 ? 155.008 150.929 130.010 1.00 36.52 ?  307 TYR A O     1 
ATOM   2466  C  CB    . TYR A 1 307 ? 152.681 148.749 129.199 1.00 28.97 ?  307 TYR A CB    1 
ATOM   2467  C  CG    . TYR A 1 307 ? 151.920 150.048 129.300 1.00 30.60 ?  307 TYR A CG    1 
ATOM   2468  C  CD1   . TYR A 1 307 ? 151.562 150.752 128.159 1.00 30.65 ?  307 TYR A CD1   1 
ATOM   2469  C  CD2   . TYR A 1 307 ? 151.567 150.575 130.534 1.00 33.18 ?  307 TYR A CD2   1 
ATOM   2470  C  CE1   . TYR A 1 307 ? 150.873 151.939 128.244 1.00 33.00 ?  307 TYR A CE1   1 
ATOM   2471  C  CE2   . TYR A 1 307 ? 150.877 151.763 130.628 1.00 33.13 ?  307 TYR A CE2   1 
ATOM   2472  C  CZ    . TYR A 1 307 ? 150.532 152.439 129.479 1.00 34.63 ?  307 TYR A CZ    1 
ATOM   2473  O  OH    . TYR A 1 307 ? 149.843 153.625 129.558 1.00 36.39 ?  307 TYR A OH    1 
ATOM   2474  N  N     . LYS A 1 308 ? 155.132 149.026 131.203 1.00 34.52 ?  308 LYS A N     1 
ATOM   2475  C  CA    . LYS A 1 308 ? 155.775 149.685 132.334 1.00 32.72 ?  308 LYS A CA    1 
ATOM   2476  C  C     . LYS A 1 308 ? 157.173 150.168 131.971 1.00 32.52 ?  308 LYS A C     1 
ATOM   2477  O  O     . LYS A 1 308 ? 157.590 151.252 132.392 1.00 38.35 ?  308 LYS A O     1 
ATOM   2478  C  CB    . LYS A 1 308 ? 155.829 148.737 133.531 1.00 33.87 ?  308 LYS A CB    1 
ATOM   2479  C  CG    . LYS A 1 308 ? 154.488 148.522 134.212 1.00 33.26 ?  308 LYS A CG    1 
ATOM   2480  C  CD    . LYS A 1 308 ? 154.640 147.717 135.491 1.00 36.34 ?  308 LYS A CD    1 
ATOM   2481  C  CE    . LYS A 1 308 ? 155.306 146.378 135.224 1.00 37.36 ?  308 LYS A CE    1 
ATOM   2482  N  NZ    . LYS A 1 308 ? 154.359 145.242 135.394 1.00 37.78 1  308 LYS A NZ    1 
ATOM   2483  N  N     . GLU A 1 309 ? 157.913 149.376 131.191 1.00 32.39 ?  309 GLU A N     1 
ATOM   2484  C  CA    . GLU A 1 309 ? 159.287 149.740 130.866 1.00 33.46 ?  309 GLU A CA    1 
ATOM   2485  C  C     . GLU A 1 309 ? 159.349 150.873 129.848 1.00 36.40 ?  309 GLU A C     1 
ATOM   2486  O  O     . GLU A 1 309 ? 160.167 151.790 129.983 1.00 37.54 ?  309 GLU A O     1 
ATOM   2487  C  CB    . GLU A 1 309 ? 160.042 148.516 130.350 1.00 31.64 ?  309 GLU A CB    1 
ATOM   2488  C  CG    . GLU A 1 309 ? 161.439 148.821 129.840 1.00 37.48 ?  309 GLU A CG    1 
ATOM   2489  C  CD    . GLU A 1 309 ? 162.389 149.246 130.941 1.00 42.65 ?  309 GLU A CD    1 
ATOM   2490  O  OE1   . GLU A 1 309 ? 162.083 148.994 132.125 1.00 41.25 ?  309 GLU A OE1   1 
ATOM   2491  O  OE2   . GLU A 1 309 ? 163.442 149.835 130.622 1.00 41.78 -1 309 GLU A OE2   1 
ATOM   2492  N  N     . TYR A 1 310 ? 158.492 150.835 128.827 1.00 37.05 ?  310 TYR A N     1 
ATOM   2493  C  CA    . TYR A 1 310 ? 158.595 151.755 127.703 1.00 36.10 ?  310 TYR A CA    1 
ATOM   2494  C  C     . TYR A 1 310 ? 157.473 152.781 127.634 1.00 33.12 ?  310 TYR A C     1 
ATOM   2495  O  O     . TYR A 1 310 ? 157.584 153.737 126.860 1.00 38.26 ?  310 TYR A O     1 
ATOM   2496  C  CB    . TYR A 1 310 ? 158.640 150.968 126.384 1.00 37.36 ?  310 TYR A CB    1 
ATOM   2497  C  CG    . TYR A 1 310 ? 159.792 149.993 126.300 1.00 33.85 ?  310 TYR A CG    1 
ATOM   2498  C  CD1   . TYR A 1 310 ? 161.042 150.403 125.859 1.00 34.94 ?  310 TYR A CD1   1 
ATOM   2499  C  CD2   . TYR A 1 310 ? 159.631 148.664 126.666 1.00 32.11 ?  310 TYR A CD2   1 
ATOM   2500  C  CE1   . TYR A 1 310 ? 162.099 149.519 125.783 1.00 36.55 ?  310 TYR A CE1   1 
ATOM   2501  C  CE2   . TYR A 1 310 ? 160.683 147.772 126.595 1.00 33.23 ?  310 TYR A CE2   1 
ATOM   2502  C  CZ    . TYR A 1 310 ? 161.913 148.205 126.151 1.00 37.01 ?  310 TYR A CZ    1 
ATOM   2503  O  OH    . TYR A 1 310 ? 162.963 147.319 126.078 1.00 41.12 ?  310 TYR A OH    1 
ATOM   2504  N  N     . GLY A 1 311 ? 156.407 152.620 128.414 1.00 27.93 ?  311 GLY A N     1 
ATOM   2505  C  CA    . GLY A 1 311 ? 155.301 153.552 128.369 1.00 31.03 ?  311 GLY A CA    1 
ATOM   2506  C  C     . GLY A 1 311 ? 154.355 153.367 127.205 1.00 36.06 ?  311 GLY A C     1 
ATOM   2507  O  O     . GLY A 1 311 ? 153.416 154.160 127.061 1.00 39.00 ?  311 GLY A O     1 
ATOM   2508  N  N     . GLN A 1 312 ? 154.574 152.355 126.370 1.00 35.59 ?  312 GLN A N     1 
ATOM   2509  C  CA    . GLN A 1 312 ? 153.714 152.061 125.235 1.00 32.40 ?  312 GLN A CA    1 
ATOM   2510  C  C     . GLN A 1 312 ? 153.385 150.576 125.231 1.00 34.00 ?  312 GLN A C     1 
ATOM   2511  O  O     . GLN A 1 312 ? 154.137 149.751 125.757 1.00 38.82 ?  312 GLN A O     1 
ATOM   2512  C  CB    . GLN A 1 312 ? 154.368 152.453 123.902 1.00 31.89 ?  312 GLN A CB    1 
ATOM   2513  C  CG    . GLN A 1 312 ? 155.453 153.510 124.014 1.00 34.46 ?  312 GLN A CG    1 
ATOM   2514  C  CD    . GLN A 1 312 ? 156.193 153.725 122.711 1.00 39.73 ?  312 GLN A CD    1 
ATOM   2515  O  OE1   . GLN A 1 312 ? 155.582 153.871 121.653 1.00 38.64 ?  312 GLN A OE1   1 
ATOM   2516  N  NE2   . GLN A 1 312 ? 157.519 153.743 122.779 1.00 38.75 ?  312 GLN A NE2   1 
ATOM   2517  N  N     . HIS A 1 313 ? 152.250 150.242 124.627 1.00 31.83 ?  313 HIS A N     1 
ATOM   2518  C  CA    . HIS A 1 313 ? 151.832 148.854 124.547 1.00 28.38 ?  313 HIS A CA    1 
ATOM   2519  C  C     . HIS A 1 313 ? 152.715 148.084 123.567 1.00 33.15 ?  313 HIS A C     1 
ATOM   2520  O  O     . HIS A 1 313 ? 153.333 148.654 122.665 1.00 35.26 ?  313 HIS A O     1 
ATOM   2521  C  CB    . HIS A 1 313 ? 150.366 148.757 124.126 1.00 28.95 ?  313 HIS A CB    1 
ATOM   2522  C  CG    . HIS A 1 313 ? 149.423 149.446 125.061 1.00 33.95 ?  313 HIS A CG    1 
ATOM   2523  N  ND1   . HIS A 1 313 ? 148.969 148.864 126.225 1.00 30.64 ?  313 HIS A ND1   1 
ATOM   2524  C  CD2   . HIS A 1 313 ? 148.843 150.668 125.002 1.00 32.84 ?  313 HIS A CD2   1 
ATOM   2525  C  CE1   . HIS A 1 313 ? 148.153 149.697 126.844 1.00 28.85 ?  313 HIS A CE1   1 
ATOM   2526  N  NE2   . HIS A 1 313 ? 148.059 150.800 126.123 1.00 30.06 ?  313 HIS A NE2   1 
ATOM   2527  N  N     . MET A 1 314 ? 152.768 146.764 123.764 1.00 34.61 ?  314 MET A N     1 
ATOM   2528  C  CA    . MET A 1 314 ? 153.612 145.921 122.924 1.00 27.28 ?  314 MET A CA    1 
ATOM   2529  C  C     . MET A 1 314 ? 153.170 145.966 121.466 1.00 31.93 ?  314 MET A C     1 
ATOM   2530  O  O     . MET A 1 314 ? 154.006 145.977 120.557 1.00 36.58 ?  314 MET A O     1 
ATOM   2531  C  CB    . MET A 1 314 ? 153.599 144.485 123.448 1.00 27.70 ?  314 MET A CB    1 
ATOM   2532  C  CG    . MET A 1 314 ? 154.530 143.542 122.707 1.00 28.99 ?  314 MET A CG    1 
ATOM   2533  S  SD    . MET A 1 314 ? 154.159 141.808 123.026 1.00 41.60 ?  314 MET A SD    1 
ATOM   2534  C  CE    . MET A 1 314 ? 152.370 141.842 123.030 1.00 30.84 ?  314 MET A CE    1 
ATOM   2535  N  N     . ASP A 1 315 ? 151.862 145.989 121.222 1.00 33.57 ?  315 ASP A N     1 
ATOM   2536  C  CA    . ASP A 1 315 ? 151.345 146.020 119.861 1.00 36.36 ?  315 ASP A CA    1 
ATOM   2537  C  C     . ASP A 1 315 ? 151.358 147.415 119.245 1.00 33.16 ?  315 ASP A C     1 
ATOM   2538  O  O     . ASP A 1 315 ? 151.024 147.553 118.064 1.00 35.57 ?  315 ASP A O     1 
ATOM   2539  C  CB    . ASP A 1 315 ? 149.925 145.447 119.824 1.00 27.80 ?  315 ASP A CB    1 
ATOM   2540  C  CG    . ASP A 1 315 ? 148.917 146.342 120.513 1.00 34.50 ?  315 ASP A CG    1 
ATOM   2541  O  OD1   . ASP A 1 315 ? 149.317 147.094 121.426 1.00 36.88 ?  315 ASP A OD1   1 
ATOM   2542  O  OD2   . ASP A 1 315 ? 147.726 146.294 120.141 1.00 31.81 -1 315 ASP A OD2   1 
ATOM   2543  N  N     . GLU A 1 316 ? 151.731 148.442 120.002 1.00 30.94 ?  316 GLU A N     1 
ATOM   2544  C  CA    . GLU A 1 316 ? 151.777 149.807 119.492 1.00 31.82 ?  316 GLU A CA    1 
ATOM   2545  C  C     . GLU A 1 316 ? 153.128 150.189 118.903 1.00 34.22 ?  316 GLU A C     1 
ATOM   2546  O  O     . GLU A 1 316 ? 153.244 151.266 118.311 1.00 36.40 ?  316 GLU A O     1 
ATOM   2547  C  CB    . GLU A 1 316 ? 151.413 150.796 120.602 1.00 34.66 ?  316 GLU A CB    1 
ATOM   2548  C  CG    . GLU A 1 316 ? 149.985 150.681 121.092 1.00 35.61 ?  316 GLU A CG    1 
ATOM   2549  C  CD    . GLU A 1 316 ? 149.064 151.674 120.418 1.00 39.42 ?  316 GLU A CD    1 
ATOM   2550  O  OE1   . GLU A 1 316 ? 149.204 151.880 119.194 1.00 36.52 ?  316 GLU A OE1   1 
ATOM   2551  O  OE2   . GLU A 1 316 ? 148.206 152.257 121.114 1.00 45.88 -1 316 GLU A OE2   1 
ATOM   2552  N  N     . MET A 1 317 ? 154.147 149.346 119.047 1.00 40.57 ?  317 MET A N     1 
ATOM   2553  C  CA    . MET A 1 317 ? 155.465 149.618 118.498 1.00 41.21 ?  317 MET A CA    1 
ATOM   2554  C  C     . MET A 1 317 ? 155.856 148.525 117.512 1.00 42.05 ?  317 MET A C     1 
ATOM   2555  O  O     . MET A 1 317 ? 155.307 147.421 117.523 1.00 38.59 ?  317 MET A O     1 
ATOM   2556  C  CB    . MET A 1 317 ? 156.526 149.730 119.599 1.00 40.57 ?  317 MET A CB    1 
ATOM   2557  C  CG    . MET A 1 317 ? 156.020 150.307 120.904 1.00 42.12 ?  317 MET A CG    1 
ATOM   2558  S  SD    . MET A 1 317 ? 157.286 150.283 122.184 1.00 51.18 ?  317 MET A SD    1 
ATOM   2559  C  CE    . MET A 1 317 ? 156.467 149.321 123.447 1.00 35.61 ?  317 MET A CE    1 
ATOM   2560  N  N     . ASP A 1 318 ? 156.827 148.848 116.661 1.00 43.69 ?  318 ASP A N     1 
ATOM   2561  C  CA    . ASP A 1 318 ? 157.288 147.931 115.623 1.00 41.03 ?  318 ASP A CA    1 
ATOM   2562  C  C     . ASP A 1 318 ? 158.120 146.833 116.268 1.00 40.87 ?  318 ASP A C     1 
ATOM   2563  O  O     . ASP A 1 318 ? 159.210 147.093 116.788 1.00 43.57 ?  318 ASP A O     1 
ATOM   2564  C  CB    . ASP A 1 318 ? 158.094 148.682 114.568 1.00 41.27 ?  318 ASP A CB    1 
ATOM   2565  C  CG    . ASP A 1 318 ? 158.721 147.755 113.547 1.00 47.77 ?  318 ASP A CG    1 
ATOM   2566  O  OD1   . ASP A 1 318 ? 158.039 146.804 113.110 1.00 46.74 ?  318 ASP A OD1   1 
ATOM   2567  O  OD2   . ASP A 1 318 ? 159.895 147.978 113.182 1.00 49.13 -1 318 ASP A OD2   1 
ATOM   2568  N  N     . MET A 1 319 ? 157.609 145.600 116.233 1.00 42.96 ?  319 MET A N     1 
ATOM   2569  C  CA    . MET A 1 319 ? 158.319 144.475 116.827 1.00 36.29 ?  319 MET A CA    1 
ATOM   2570  C  C     . MET A 1 319 ? 159.614 144.153 116.091 1.00 36.71 ?  319 MET A C     1 
ATOM   2571  O  O     . MET A 1 319 ? 160.528 143.590 116.696 1.00 41.37 ?  319 MET A O     1 
ATOM   2572  C  CB    . MET A 1 319 ? 157.401 143.248 116.864 1.00 33.84 ?  319 MET A CB    1 
ATOM   2573  C  CG    . MET A 1 319 ? 158.079 141.954 117.287 1.00 38.01 ?  319 MET A CG    1 
ATOM   2574  S  SD    . MET A 1 319 ? 158.111 141.693 119.074 1.00 45.80 ?  319 MET A SD    1 
ATOM   2575  C  CE    . MET A 1 319 ? 156.713 142.675 119.607 1.00 34.85 ?  319 MET A CE    1 
ATOM   2576  N  N     . ASN A 1 320 ? 159.729 144.527 114.816 1.00 38.02 ?  320 ASN A N     1 
ATOM   2577  C  CA    . ASN A 1 320 ? 160.953 144.241 114.077 1.00 41.12 ?  320 ASN A CA    1 
ATOM   2578  C  C     . ASN A 1 320 ? 162.154 144.942 114.700 1.00 41.90 ?  320 ASN A C     1 
ATOM   2579  O  O     . ASN A 1 320 ? 163.240 144.358 114.801 1.00 41.32 ?  320 ASN A O     1 
ATOM   2580  C  CB    . ASN A 1 320 ? 160.791 144.649 112.613 1.00 41.65 ?  320 ASN A CB    1 
ATOM   2581  C  CG    . ASN A 1 320 ? 160.171 143.552 111.773 1.00 43.37 ?  320 ASN A CG    1 
ATOM   2582  O  OD1   . ASN A 1 320 ? 158.963 143.325 111.820 1.00 38.61 ?  320 ASN A OD1   1 
ATOM   2583  N  ND2   . ASN A 1 320 ? 160.999 142.863 110.995 1.00 40.60 ?  320 ASN A ND2   1 
ATOM   2584  N  N     . GLU A 1 321 ? 161.980 146.190 115.128 1.00 42.91 ?  321 GLU A N     1 
ATOM   2585  C  CA    . GLU A 1 321 ? 163.048 146.936 115.780 1.00 44.57 ?  321 GLU A CA    1 
ATOM   2586  C  C     . GLU A 1 321 ? 162.997 146.851 117.300 1.00 42.96 ?  321 GLU A C     1 
ATOM   2587  O  O     . GLU A 1 321 ? 163.963 147.254 117.958 1.00 44.36 ?  321 GLU A O     1 
ATOM   2588  C  CB    . GLU A 1 321 ? 163.000 148.406 115.353 1.00 44.39 ?  321 GLU A CB    1 
ATOM   2589  C  CG    . GLU A 1 321 ? 161.781 149.157 115.861 1.00 47.17 ?  321 GLU A CG    1 
ATOM   2590  C  CD    . GLU A 1 321 ? 162.097 150.587 116.250 1.00 49.00 ?  321 GLU A CD    1 
ATOM   2591  O  OE1   . GLU A 1 321 ? 163.188 150.827 116.807 1.00 46.69 ?  321 GLU A OE1   1 
ATOM   2592  O  OE2   . GLU A 1 321 ? 161.252 151.472 115.998 1.00 47.46 -1 321 GLU A OE2   1 
ATOM   2593  N  N     . MET A 1 322 ? 161.908 146.339 117.871 1.00 41.35 ?  322 MET A N     1 
ATOM   2594  C  CA    . MET A 1 322 ? 161.735 146.296 119.316 1.00 35.79 ?  322 MET A CA    1 
ATOM   2595  C  C     . MET A 1 322 ? 161.993 144.922 119.921 1.00 33.07 ?  322 MET A C     1 
ATOM   2596  O  O     . MET A 1 322 ? 162.123 144.823 121.143 1.00 41.00 ?  322 MET A O     1 
ATOM   2597  C  CB    . MET A 1 322 ? 160.315 146.739 119.691 1.00 34.29 ?  322 MET A CB    1 
ATOM   2598  C  CG    . MET A 1 322 ? 160.165 148.219 120.003 1.00 39.93 ?  322 MET A CG    1 
ATOM   2599  S  SD    . MET A 1 322 ? 161.481 148.875 121.041 1.00 48.26 ?  322 MET A SD    1 
ATOM   2600  C  CE    . MET A 1 322 ? 162.253 150.021 119.902 1.00 39.75 ?  322 MET A CE    1 
ATOM   2601  N  N     . TYR A 1 323 ? 162.054 143.867 119.105 1.00 31.27 ?  323 TYR A N     1 
ATOM   2602  C  CA    . TYR A 1 323 ? 162.136 142.511 119.640 1.00 32.27 ?  323 TYR A CA    1 
ATOM   2603  C  C     . TYR A 1 323 ? 163.454 142.277 120.366 1.00 36.70 ?  323 TYR A C     1 
ATOM   2604  O  O     . TYR A 1 323 ? 163.480 141.703 121.460 1.00 38.05 ?  323 TYR A O     1 
ATOM   2605  C  CB    . TYR A 1 323 ? 161.952 141.496 118.512 1.00 30.02 ?  323 TYR A CB    1 
ATOM   2606  C  CG    . TYR A 1 323 ? 162.114 140.059 118.945 1.00 35.95 ?  323 TYR A CG    1 
ATOM   2607  C  CD1   . TYR A 1 323 ? 161.055 139.362 119.510 1.00 31.23 ?  323 TYR A CD1   1 
ATOM   2608  C  CD2   . TYR A 1 323 ? 163.324 139.397 118.789 1.00 33.51 ?  323 TYR A CD2   1 
ATOM   2609  C  CE1   . TYR A 1 323 ? 161.198 138.050 119.907 1.00 28.78 ?  323 TYR A CE1   1 
ATOM   2610  C  CE2   . TYR A 1 323 ? 163.476 138.086 119.183 1.00 26.53 ?  323 TYR A CE2   1 
ATOM   2611  C  CZ    . TYR A 1 323 ? 162.410 137.417 119.742 1.00 31.76 ?  323 TYR A CZ    1 
ATOM   2612  O  OH    . TYR A 1 323 ? 162.559 136.110 120.136 1.00 34.72 ?  323 TYR A OH    1 
ATOM   2613  N  N     . ASP A 1 324 ? 164.565 142.705 119.762 1.00 38.06 ?  324 ASP A N     1 
ATOM   2614  C  CA    . ASP A 1 324 ? 165.864 142.522 120.397 1.00 37.16 ?  324 ASP A CA    1 
ATOM   2615  C  C     . ASP A 1 324 ? 165.956 143.315 121.693 1.00 39.55 ?  324 ASP A C     1 
ATOM   2616  O  O     . ASP A 1 324 ? 166.516 142.835 122.685 1.00 45.08 ?  324 ASP A O     1 
ATOM   2617  C  CB    . ASP A 1 324 ? 166.981 142.927 119.437 1.00 40.36 ?  324 ASP A CB    1 
ATOM   2618  C  CG    . ASP A 1 324 ? 167.095 141.993 118.251 1.00 43.01 ?  324 ASP A CG    1 
ATOM   2619  O  OD1   . ASP A 1 324 ? 166.921 140.770 118.436 1.00 43.21 ?  324 ASP A OD1   1 
ATOM   2620  O  OD2   . ASP A 1 324 ? 167.360 142.480 117.132 1.00 43.38 -1 324 ASP A OD2   1 
ATOM   2621  N  N     . LYS A 1 325 ? 165.410 144.532 121.704 1.00 37.78 ?  325 LYS A N     1 
ATOM   2622  C  CA    . LYS A 1 325 ? 165.428 145.337 122.920 1.00 37.22 ?  325 LYS A CA    1 
ATOM   2623  C  C     . LYS A 1 325 ? 164.556 144.720 124.006 1.00 37.32 ?  325 LYS A C     1 
ATOM   2624  O  O     . LYS A 1 325 ? 164.908 144.768 125.188 1.00 44.63 ?  325 LYS A O     1 
ATOM   2625  C  CB    . LYS A 1 325 ? 164.983 146.765 122.607 1.00 40.71 ?  325 LYS A CB    1 
ATOM   2626  C  CG    . LYS A 1 325 ? 165.917 147.495 121.657 1.00 40.43 ?  325 LYS A CG    1 
ATOM   2627  C  CD    . LYS A 1 325 ? 165.395 148.877 121.313 1.00 40.26 ?  325 LYS A CD    1 
ATOM   2628  C  CE    . LYS A 1 325 ? 166.237 149.529 120.228 1.00 41.23 ?  325 LYS A CE    1 
ATOM   2629  N  NZ    . LYS A 1 325 ? 165.537 150.681 119.598 1.00 45.47 1  325 LYS A NZ    1 
ATOM   2630  N  N     . PHE A 1 326 ? 163.414 144.144 123.627 1.00 37.17 ?  326 PHE A N     1 
ATOM   2631  C  CA    . PHE A 1 326 ? 162.581 143.442 124.598 1.00 36.58 ?  326 PHE A CA    1 
ATOM   2632  C  C     . PHE A 1 326 ? 163.319 142.244 125.182 1.00 34.61 ?  326 PHE A C     1 
ATOM   2633  O  O     . PHE A 1 326 ? 163.295 142.016 126.396 1.00 41.38 ?  326 PHE A O     1 
ATOM   2634  C  CB    . PHE A 1 326 ? 161.273 142.987 123.946 1.00 34.54 ?  326 PHE A CB    1 
ATOM   2635  C  CG    . PHE A 1 326 ? 160.366 144.110 123.533 1.00 34.95 ?  326 PHE A CG    1 
ATOM   2636  C  CD1   . PHE A 1 326 ? 160.479 145.365 124.105 1.00 36.22 ?  326 PHE A CD1   1 
ATOM   2637  C  CD2   . PHE A 1 326 ? 159.394 143.906 122.570 1.00 34.82 ?  326 PHE A CD2   1 
ATOM   2638  C  CE1   . PHE A 1 326 ? 159.639 146.393 123.721 1.00 36.18 ?  326 PHE A CE1   1 
ATOM   2639  C  CE2   . PHE A 1 326 ? 158.552 144.929 122.185 1.00 36.20 ?  326 PHE A CE2   1 
ATOM   2640  C  CZ    . PHE A 1 326 ? 158.675 146.174 122.761 1.00 38.81 ?  326 PHE A CZ    1 
ATOM   2641  N  N     . VAL A 1 327 ? 163.980 141.465 124.324 1.00 38.25 ?  327 VAL A N     1 
ATOM   2642  C  CA    . VAL A 1 327 ? 164.681 140.270 124.784 1.00 39.48 ?  327 VAL A CA    1 
ATOM   2643  C  C     . VAL A 1 327 ? 165.841 140.645 125.700 1.00 42.72 ?  327 VAL A C     1 
ATOM   2644  O  O     . VAL A 1 327 ? 166.054 140.015 126.743 1.00 44.58 ?  327 VAL A O     1 
ATOM   2645  C  CB    . VAL A 1 327 ? 165.151 139.433 123.580 1.00 37.45 ?  327 VAL A CB    1 
ATOM   2646  C  CG1   . VAL A 1 327 ? 166.085 138.323 124.033 1.00 40.17 ?  327 VAL A CG1   1 
ATOM   2647  C  CG2   . VAL A 1 327 ? 163.957 138.855 122.842 1.00 32.45 ?  327 VAL A CG2   1 
ATOM   2648  N  N     . ASP A 1 328 ? 166.601 141.675 125.333 1.00 40.53 ?  328 ASP A N     1 
ATOM   2649  C  CA    . ASP A 1 328 ? 167.758 142.089 126.117 1.00 39.72 ?  328 ASP A CA    1 
ATOM   2650  C  C     . ASP A 1 328 ? 167.388 142.906 127.347 1.00 43.46 ?  328 ASP A C     1 
ATOM   2651  O  O     . ASP A 1 328 ? 168.270 143.200 128.159 1.00 47.01 ?  328 ASP A O     1 
ATOM   2652  C  CB    . ASP A 1 328 ? 168.722 142.893 125.242 1.00 41.20 ?  328 ASP A CB    1 
ATOM   2653  C  CG    . ASP A 1 328 ? 169.345 142.057 124.141 1.00 48.04 ?  328 ASP A CG    1 
ATOM   2654  O  OD1   . ASP A 1 328 ? 168.920 140.896 123.961 1.00 46.00 ?  328 ASP A OD1   1 
ATOM   2655  O  OD2   . ASP A 1 328 ? 170.260 142.560 123.456 1.00 47.87 -1 328 ASP A OD2   1 
ATOM   2656  N  N     . ASN A 1 329 ? 166.120 143.280 127.505 1.00 40.52 ?  329 ASN A N     1 
ATOM   2657  C  CA    . ASN A 1 329 ? 165.701 144.073 128.653 1.00 40.00 ?  329 ASN A CA    1 
ATOM   2658  C  C     . ASN A 1 329 ? 165.364 143.153 129.817 1.00 43.33 ?  329 ASN A C     1 
ATOM   2659  O  O     . ASN A 1 329 ? 164.433 142.345 129.702 1.00 43.25 ?  329 ASN A O     1 
ATOM   2660  C  CB    . ASN A 1 329 ? 164.496 144.929 128.303 1.00 36.36 ?  329 ASN A CB    1 
ATOM   2661  C  CG    . ASN A 1 329 ? 164.316 146.097 129.250 1.00 38.87 ?  329 ASN A CG    1 
ATOM   2662  O  OD1   . ASN A 1 329 ? 164.359 145.936 130.469 1.00 45.50 ?  329 ASN A OD1   1 
ATOM   2663  N  ND2   . ASN A 1 329 ? 164.119 147.283 128.691 1.00 36.20 ?  329 ASN A ND2   1 
ATOM   2664  N  N     . PRO A 1 330 ? 166.085 143.228 130.939 1.00 43.62 ?  330 PRO A N     1 
ATOM   2665  C  CA    . PRO A 1 330 ? 165.741 142.369 132.082 1.00 38.70 ?  330 PRO A CA    1 
ATOM   2666  C  C     . PRO A 1 330 ? 164.399 142.705 132.706 1.00 38.18 ?  330 PRO A C     1 
ATOM   2667  O  O     . PRO A 1 330 ? 163.765 141.820 133.294 1.00 41.07 ?  330 PRO A O     1 
ATOM   2668  C  CB    . PRO A 1 330 ? 166.897 142.612 133.062 1.00 40.51 ?  330 PRO A CB    1 
ATOM   2669  C  CG    . PRO A 1 330 ? 167.398 143.972 132.715 1.00 38.95 ?  330 PRO A CG    1 
ATOM   2670  C  CD    . PRO A 1 330 ? 167.234 144.104 131.227 1.00 40.23 ?  330 PRO A CD    1 
ATOM   2671  N  N     . ARG A 1 331 ? 163.944 143.953 132.597 1.00 37.03 ?  331 ARG A N     1 
ATOM   2672  C  CA    . ARG A 1 331 ? 162.675 144.358 133.188 1.00 38.27 ?  331 ARG A CA    1 
ATOM   2673  C  C     . ARG A 1 331 ? 161.473 143.962 132.344 1.00 39.55 ?  331 ARG A C     1 
ATOM   2674  O  O     . ARG A 1 331 ? 160.335 144.160 132.784 1.00 38.55 ?  331 ARG A O     1 
ATOM   2675  C  CB    . ARG A 1 331 ? 162.669 145.870 133.427 1.00 36.84 ?  331 ARG A CB    1 
ATOM   2676  C  CG    . ARG A 1 331 ? 163.581 146.308 134.561 1.00 38.30 ?  331 ARG A CG    1 
ATOM   2677  C  CD    . ARG A 1 331 ? 163.839 147.805 134.527 1.00 38.69 ?  331 ARG A CD    1 
ATOM   2678  N  NE    . ARG A 1 331 ? 164.373 148.244 133.244 1.00 41.16 ?  331 ARG A NE    1 
ATOM   2679  C  CZ    . ARG A 1 331 ? 165.611 148.015 132.826 1.00 40.35 ?  331 ARG A CZ    1 
ATOM   2680  N  NH1   . ARG A 1 331 ? 166.483 147.356 133.571 1.00 42.22 1  331 ARG A NH1   1 
ATOM   2681  N  NH2   . ARG A 1 331 ? 165.984 148.460 131.630 1.00 35.96 ?  331 ARG A NH2   1 
ATOM   2682  N  N     . VAL A 1 332 ? 161.693 143.417 131.152 1.00 35.93 ?  332 VAL A N     1 
ATOM   2683  C  CA    . VAL A 1 332 ? 160.626 142.882 130.316 1.00 34.17 ?  332 VAL A CA    1 
ATOM   2684  C  C     . VAL A 1 332 ? 160.580 141.377 130.534 1.00 37.50 ?  332 VAL A C     1 
ATOM   2685  O  O     . VAL A 1 332 ? 161.573 140.678 130.302 1.00 37.78 ?  332 VAL A O     1 
ATOM   2686  C  CB    . VAL A 1 332 ? 160.848 143.223 128.835 1.00 34.74 ?  332 VAL A CB    1 
ATOM   2687  C  CG1   . VAL A 1 332 ? 159.995 142.329 127.949 1.00 34.04 ?  332 VAL A CG1   1 
ATOM   2688  C  CG2   . VAL A 1 332 ? 160.541 144.688 128.575 1.00 35.22 ?  332 VAL A CG2   1 
ATOM   2689  N  N     . LYS A 1 333 ? 159.436 140.876 130.987 1.00 33.45 ?  333 LYS A N     1 
ATOM   2690  C  CA    . LYS A 1 333 ? 159.269 139.455 131.247 1.00 31.89 ?  333 LYS A CA    1 
ATOM   2691  C  C     . LYS A 1 333 ? 158.819 138.746 129.977 1.00 32.22 ?  333 LYS A C     1 
ATOM   2692  O  O     . LYS A 1 333 ? 157.949 139.236 129.253 1.00 36.70 ?  333 LYS A O     1 
ATOM   2693  C  CB    . LYS A 1 333 ? 158.257 139.228 132.372 1.00 29.77 ?  333 LYS A CB    1 
ATOM   2694  C  CG    . LYS A 1 333 ? 158.129 137.782 132.814 1.00 32.83 ?  333 LYS A CG    1 
ATOM   2695  C  CD    . LYS A 1 333 ? 157.334 137.670 134.103 1.00 33.72 ?  333 LYS A CD    1 
ATOM   2696  C  CE    . LYS A 1 333 ? 157.429 136.273 134.691 1.00 36.46 ?  333 LYS A CE    1 
ATOM   2697  N  NZ    . LYS A 1 333 ? 156.099 135.767 135.129 1.00 38.82 1  333 LYS A NZ    1 
ATOM   2698  N  N     . LYS A 1 334 ? 159.422 137.589 129.712 1.00 35.19 ?  334 LYS A N     1 
ATOM   2699  C  CA    . LYS A 1 334 ? 159.167 136.866 128.476 1.00 33.26 ?  334 LYS A CA    1 
ATOM   2700  C  C     . LYS A 1 334 ? 159.296 135.372 128.726 1.00 37.91 ?  334 LYS A C     1 
ATOM   2701  O  O     . LYS A 1 334 ? 159.917 134.934 129.698 1.00 40.87 ?  334 LYS A O     1 
ATOM   2702  C  CB    . LYS A 1 334 ? 160.132 137.300 127.367 1.00 31.87 ?  334 LYS A CB    1 
ATOM   2703  C  CG    . LYS A 1 334 ? 161.593 137.117 127.726 1.00 34.69 ?  334 LYS A CG    1 
ATOM   2704  C  CD    . LYS A 1 334 ? 162.476 138.076 126.956 1.00 33.81 ?  334 LYS A CD    1 
ATOM   2705  C  CE    . LYS A 1 334 ? 162.968 139.199 127.850 1.00 35.60 ?  334 LYS A CE    1 
ATOM   2706  N  NZ    . LYS A 1 334 ? 163.878 138.706 128.918 1.00 37.49 1  334 LYS A NZ    1 
ATOM   2707  N  N     . GLU A 1 335 ? 158.695 134.592 127.832 1.00 35.08 ?  335 GLU A N     1 
ATOM   2708  C  CA    . GLU A 1 335 ? 158.759 133.139 127.875 1.00 35.23 ?  335 GLU A CA    1 
ATOM   2709  C  C     . GLU A 1 335 ? 159.286 132.605 126.551 1.00 39.41 ?  335 GLU A C     1 
ATOM   2710  O  O     . GLU A 1 335 ? 158.926 133.100 125.479 1.00 44.34 ?  335 GLU A O     1 
ATOM   2711  C  CB    . GLU A 1 335 ? 157.388 132.526 128.180 1.00 34.11 ?  335 GLU A CB    1 
ATOM   2712  C  CG    . GLU A 1 335 ? 156.675 133.166 129.358 1.00 43.30 ?  335 GLU A CG    1 
ATOM   2713  C  CD    . GLU A 1 335 ? 156.492 132.207 130.519 1.00 43.64 ?  335 GLU A CD    1 
ATOM   2714  O  OE1   . GLU A 1 335 ? 157.484 131.562 130.921 1.00 40.96 ?  335 GLU A OE1   1 
ATOM   2715  O  OE2   . GLU A 1 335 ? 155.359 132.099 131.031 1.00 38.15 -1 335 GLU A OE2   1 
ATOM   2716  N  N     . LYS A 1 336 ? 160.146 131.594 126.643 1.00 38.66 ?  336 LYS A N     1 
ATOM   2717  C  CA    . LYS A 1 336 ? 160.742 130.964 125.474 1.00 34.38 ?  336 LYS A CA    1 
ATOM   2718  C  C     . LYS A 1 336 ? 159.716 130.094 124.757 1.00 38.68 ?  336 LYS A C     1 
ATOM   2719  O  O     . LYS A 1 336 ? 158.997 129.317 125.393 1.00 41.63 ?  336 LYS A O     1 
ATOM   2720  C  CB    . LYS A 1 336 ? 161.944 130.122 125.900 1.00 40.52 ?  336 LYS A CB    1 
ATOM   2721  C  CG    . LYS A 1 336 ? 163.122 130.134 124.946 1.00 42.05 ?  336 LYS A CG    1 
ATOM   2722  C  CD    . LYS A 1 336 ? 164.073 128.992 125.282 1.00 41.51 ?  336 LYS A CD    1 
ATOM   2723  C  CE    . LYS A 1 336 ? 164.916 128.587 124.088 1.00 40.22 ?  336 LYS A CE    1 
ATOM   2724  N  NZ    . LYS A 1 336 ? 165.573 127.267 124.290 1.00 41.73 1  336 LYS A NZ    1 
ATOM   2725  N  N     . ILE A 1 337 ? 159.650 130.225 123.430 1.00 36.69 ?  337 ILE A N     1 
ATOM   2726  C  CA    . ILE A 1 337 ? 158.789 129.396 122.596 1.00 33.68 ?  337 ILE A CA    1 
ATOM   2727  C  C     . ILE A 1 337 ? 159.556 129.009 121.340 1.00 32.64 ?  337 ILE A C     1 
ATOM   2728  O  O     . ILE A 1 337 ? 160.581 129.603 120.999 1.00 36.49 ?  337 ILE A O     1 
ATOM   2729  C  CB    . ILE A 1 337 ? 157.470 130.104 122.209 1.00 34.61 ?  337 ILE A CB    1 
ATOM   2730  C  CG1   . ILE A 1 337 ? 157.766 131.444 121.533 1.00 33.71 ?  337 ILE A CG1   1 
ATOM   2731  C  CG2   . ILE A 1 337 ? 156.573 130.284 123.425 1.00 35.33 ?  337 ILE A CG2   1 
ATOM   2732  C  CD1   . ILE A 1 337 ? 156.874 131.739 120.352 1.00 31.06 ?  337 ILE A CD1   1 
ATOM   2733  N  N     . ASN A 1 338 ? 159.042 127.994 120.647 1.00 33.74 ?  338 ASN A N     1 
ATOM   2734  C  CA    . ASN A 1 338 ? 159.583 127.614 119.353 1.00 35.16 ?  338 ASN A CA    1 
ATOM   2735  C  C     . ASN A 1 338 ? 158.663 128.151 118.269 1.00 32.98 ?  338 ASN A C     1 
ATOM   2736  O  O     . ASN A 1 338 ? 157.523 127.677 118.151 1.00 34.04 ?  338 ASN A O     1 
ATOM   2737  C  CB    . ASN A 1 338 ? 159.718 126.098 119.240 1.00 35.34 ?  338 ASN A CB    1 
ATOM   2738  C  CG    . ASN A 1 338 ? 160.473 125.673 117.995 1.00 36.98 ?  338 ASN A CG    1 
ATOM   2739  O  OD1   . ASN A 1 338 ? 160.110 124.703 117.334 1.00 37.66 ?  338 ASN A OD1   1 
ATOM   2740  N  ND2   . ASN A 1 338 ? 161.532 126.406 117.670 1.00 37.68 ?  338 ASN A ND2   1 
ATOM   2741  N  N     . PRO A 1 339 ? 159.091 129.136 117.475 1.00 35.25 ?  339 PRO A N     1 
ATOM   2742  C  CA    . PRO A 1 339 ? 158.191 129.698 116.456 1.00 31.07 ?  339 PRO A CA    1 
ATOM   2743  C  C     . PRO A 1 339 ? 157.727 128.687 115.422 1.00 32.75 ?  339 PRO A C     1 
ATOM   2744  O  O     . PRO A 1 339 ? 156.595 128.792 114.937 1.00 37.31 ?  339 PRO A O     1 
ATOM   2745  C  CB    . PRO A 1 339 ? 159.033 130.813 115.820 1.00 31.83 ?  339 PRO A CB    1 
ATOM   2746  C  CG    . PRO A 1 339 ? 160.442 130.462 116.139 1.00 34.70 ?  339 PRO A CG    1 
ATOM   2747  C  CD    . PRO A 1 339 ? 160.411 129.785 117.470 1.00 33.83 ?  339 PRO A CD    1 
ATOM   2748  N  N     . ARG A 1 340 ? 158.564 127.712 115.062 1.00 32.40 ?  340 ARG A N     1 
ATOM   2749  C  CA    . ARG A 1 340 ? 158.127 126.684 114.124 1.00 27.98 ?  340 ARG A CA    1 
ATOM   2750  C  C     . ARG A 1 340 ? 157.062 125.790 114.745 1.00 31.44 ?  340 ARG A C     1 
ATOM   2751  O  O     . ARG A 1 340 ? 156.102 125.398 114.072 1.00 37.96 ?  340 ARG A O     1 
ATOM   2752  C  CB    . ARG A 1 340 ? 159.323 125.860 113.650 1.00 30.71 ?  340 ARG A CB    1 
ATOM   2753  C  CG    . ARG A 1 340 ? 160.197 126.588 112.647 1.00 30.19 ?  340 ARG A CG    1 
ATOM   2754  C  CD    . ARG A 1 340 ? 161.098 125.637 111.885 1.00 27.86 ?  340 ARG A CD    1 
ATOM   2755  N  NE    . ARG A 1 340 ? 161.966 126.356 110.961 1.00 30.37 ?  340 ARG A NE    1 
ATOM   2756  C  CZ    . ARG A 1 340 ? 162.909 125.789 110.222 1.00 32.54 ?  340 ARG A CZ    1 
ATOM   2757  N  NH1   . ARG A 1 340 ? 163.136 124.487 110.271 1.00 32.83 1  340 ARG A NH1   1 
ATOM   2758  N  NH2   . ARG A 1 340 ? 163.643 126.548 109.412 1.00 32.68 ?  340 ARG A NH2   1 
ATOM   2759  N  N     . LYS A 1 341 ? 157.209 125.465 116.031 1.00 33.69 ?  341 LYS A N     1 
ATOM   2760  C  CA    . LYS A 1 341 ? 156.162 124.725 116.726 1.00 32.33 ?  341 LYS A CA    1 
ATOM   2761  C  C     . LYS A 1 341 ? 154.869 125.527 116.777 1.00 31.94 ?  341 LYS A C     1 
ATOM   2762  O  O     . LYS A 1 341 ? 153.778 124.968 116.633 1.00 35.86 ?  341 LYS A O     1 
ATOM   2763  C  CB    . LYS A 1 341 ? 156.621 124.357 118.137 1.00 35.30 ?  341 LYS A CB    1 
ATOM   2764  C  CG    . LYS A 1 341 ? 157.480 123.107 118.206 1.00 37.81 ?  341 LYS A CG    1 
ATOM   2765  C  CD    . LYS A 1 341 ? 156.846 121.951 117.451 1.00 36.37 ?  341 LYS A CD    1 
ATOM   2766  C  CE    . LYS A 1 341 ? 157.900 121.085 116.784 1.00 38.19 ?  341 LYS A CE    1 
ATOM   2767  N  NZ    . LYS A 1 341 ? 158.753 121.871 115.850 1.00 38.23 1  341 LYS A NZ    1 
ATOM   2768  N  N     . LEU A 1 342 ? 154.971 126.841 116.984 1.00 29.81 ?  342 LEU A N     1 
ATOM   2769  C  CA    . LEU A 1 342 ? 153.778 127.682 116.997 1.00 27.23 ?  342 LEU A CA    1 
ATOM   2770  C  C     . LEU A 1 342 ? 153.118 127.726 115.623 1.00 29.81 ?  342 LEU A C     1 
ATOM   2771  O  O     . LEU A 1 342 ? 151.886 127.708 115.520 1.00 36.01 ?  342 LEU A O     1 
ATOM   2772  C  CB    . LEU A 1 342 ? 154.138 129.088 117.477 1.00 28.01 ?  342 LEU A CB    1 
ATOM   2773  C  CG    . LEU A 1 342 ? 152.986 130.008 117.878 1.00 27.34 ?  342 LEU A CG    1 
ATOM   2774  C  CD1   . LEU A 1 342 ? 151.925 129.238 118.642 1.00 26.87 ?  342 LEU A CD1   1 
ATOM   2775  C  CD2   . LEU A 1 342 ? 153.508 131.165 118.712 1.00 28.36 ?  342 LEU A CD2   1 
ATOM   2776  N  N     . LEU A 1 343 ? 153.919 127.787 114.557 1.00 28.68 ?  343 LEU A N     1 
ATOM   2777  C  CA    . LEU A 1 343 ? 153.364 127.748 113.206 1.00 24.60 ?  343 LEU A CA    1 
ATOM   2778  C  C     . LEU A 1 343 ? 152.670 126.420 112.933 1.00 31.50 ?  343 LEU A C     1 
ATOM   2779  O  O     . LEU A 1 343 ? 151.595 126.384 112.321 1.00 36.23 ?  343 LEU A O     1 
ATOM   2780  C  CB    . LEU A 1 343 ? 154.468 127.995 112.180 1.00 28.60 ?  343 LEU A CB    1 
ATOM   2781  C  CG    . LEU A 1 343 ? 154.817 129.452 111.878 1.00 31.05 ?  343 LEU A CG    1 
ATOM   2782  C  CD1   . LEU A 1 343 ? 155.804 129.534 110.727 1.00 27.29 ?  343 LEU A CD1   1 
ATOM   2783  C  CD2   . LEU A 1 343 ? 153.562 130.250 111.568 1.00 30.62 ?  343 LEU A CD2   1 
ATOM   2784  N  N     . GLU A 1 344 ? 153.278 125.316 113.372 1.00 34.59 ?  344 GLU A N     1 
ATOM   2785  C  CA    . GLU A 1 344 ? 152.646 124.011 113.203 1.00 30.94 ?  344 GLU A CA    1 
ATOM   2786  C  C     . GLU A 1 344 ? 151.354 123.923 114.002 1.00 30.40 ?  344 GLU A C     1 
ATOM   2787  O  O     . GLU A 1 344 ? 150.378 123.315 113.550 1.00 39.33 ?  344 GLU A O     1 
ATOM   2788  C  CB    . GLU A 1 344 ? 153.614 122.900 113.611 1.00 31.41 ?  344 GLU A CB    1 
ATOM   2789  C  CG    . GLU A 1 344 ? 154.829 122.781 112.707 1.00 33.61 ?  344 GLU A CG    1 
ATOM   2790  C  CD    . GLU A 1 344 ? 155.954 121.994 113.347 1.00 40.44 ?  344 GLU A CD    1 
ATOM   2791  O  OE1   . GLU A 1 344 ? 155.696 121.290 114.345 1.00 41.47 ?  344 GLU A OE1   1 
ATOM   2792  O  OE2   . GLU A 1 344 ? 157.098 122.082 112.854 1.00 40.14 -1 344 GLU A OE2   1 
ATOM   2793  N  N     . LYS A 1 345 ? 151.328 124.519 115.195 1.00 29.13 ?  345 LYS A N     1 
ATOM   2794  C  CA    . LYS A 1 345 ? 150.099 124.562 115.981 1.00 29.09 ?  345 LYS A CA    1 
ATOM   2795  C  C     . LYS A 1 345 ? 149.020 125.371 115.274 1.00 29.83 ?  345 LYS A C     1 
ATOM   2796  O  O     . LYS A 1 345 ? 147.847 124.982 115.273 1.00 31.83 ?  345 LYS A O     1 
ATOM   2797  C  CB    . LYS A 1 345 ? 150.384 125.139 117.368 1.00 26.73 ?  345 LYS A CB    1 
ATOM   2798  C  CG    . LYS A 1 345 ? 149.170 125.178 118.280 1.00 29.26 ?  345 LYS A CG    1 
ATOM   2799  C  CD    . LYS A 1 345 ? 149.520 125.729 119.649 1.00 30.18 ?  345 LYS A CD    1 
ATOM   2800  C  CE    . LYS A 1 345 ? 148.291 125.799 120.540 1.00 32.03 ?  345 LYS A CE    1 
ATOM   2801  N  NZ    . LYS A 1 345 ? 148.596 126.387 121.871 1.00 31.82 1  345 LYS A NZ    1 
ATOM   2802  N  N     . LEU A 1 346 ? 149.396 126.502 114.671 1.00 32.88 ?  346 LEU A N     1 
ATOM   2803  C  CA    . LEU A 1 346 ? 148.438 127.287 113.899 1.00 25.13 ?  346 LEU A CA    1 
ATOM   2804  C  C     . LEU A 1 346 ? 147.879 126.480 112.737 1.00 26.69 ?  346 LEU A C     1 
ATOM   2805  O  O     . LEU A 1 346 ? 146.667 126.487 112.491 1.00 32.19 ?  346 LEU A O     1 
ATOM   2806  C  CB    . LEU A 1 346 ? 149.095 128.567 113.379 1.00 24.17 ?  346 LEU A CB    1 
ATOM   2807  C  CG    . LEU A 1 346 ? 149.593 129.612 114.377 1.00 26.88 ?  346 LEU A CG    1 
ATOM   2808  C  CD1   . LEU A 1 346 ? 150.558 130.565 113.695 1.00 27.67 ?  346 LEU A CD1   1 
ATOM   2809  C  CD2   . LEU A 1 346 ? 148.433 130.375 114.972 1.00 28.49 ?  346 LEU A CD2   1 
ATOM   2810  N  N     . ALA A 1 347 ? 148.750 125.775 112.010 1.00 25.65 ?  347 ALA A N     1 
ATOM   2811  C  CA    . ALA A 1 347 ? 148.296 124.969 110.882 1.00 26.16 ?  347 ALA A CA    1 
ATOM   2812  C  C     . ALA A 1 347 ? 147.386 123.835 111.339 1.00 29.62 ?  347 ALA A C     1 
ATOM   2813  O  O     . ALA A 1 347 ? 146.367 123.554 110.698 1.00 35.76 ?  347 ALA A O     1 
ATOM   2814  C  CB    . ALA A 1 347 ? 149.496 124.418 110.113 1.00 26.21 ?  347 ALA A CB    1 
ATOM   2815  N  N     . MET A 1 348 ? 147.733 123.175 112.447 1.00 31.30 ?  348 MET A N     1 
ATOM   2816  C  CA    . MET A 1 348 ? 146.898 122.098 112.964 1.00 34.50 ?  348 MET A CA    1 
ATOM   2817  C  C     . MET A 1 348 ? 145.534 122.618 113.395 1.00 31.34 ?  348 MET A C     1 
ATOM   2818  O  O     . MET A 1 348 ? 144.504 121.999 113.105 1.00 36.47 ?  348 MET A O     1 
ATOM   2819  C  CB    . MET A 1 348 ? 147.606 121.405 114.130 1.00 32.72 ?  348 MET A CB    1 
ATOM   2820  C  CG    . MET A 1 348 ? 146.701 120.545 114.995 1.00 37.45 ?  348 MET A CG    1 
ATOM   2821  S  SD    . MET A 1 348 ? 146.434 121.246 116.635 1.00 55.87 ?  348 MET A SD    1 
ATOM   2822  C  CE    . MET A 1 348 ? 148.105 121.257 117.276 1.00 38.89 ?  348 MET A CE    1 
ATOM   2823  N  N     . LEU A 1 349 ? 145.505 123.763 114.082 1.00 27.73 ?  349 LEU A N     1 
ATOM   2824  C  CA    . LEU A 1 349 ? 144.236 124.335 114.515 1.00 22.99 ?  349 LEU A CA    1 
ATOM   2825  C  C     . LEU A 1 349 ? 143.384 124.753 113.325 1.00 28.25 ?  349 LEU A C     1 
ATOM   2826  O  O     . LEU A 1 349 ? 142.159 124.586 113.342 1.00 30.06 ?  349 LEU A O     1 
ATOM   2827  C  CB    . LEU A 1 349 ? 144.489 125.522 115.440 1.00 26.16 ?  349 LEU A CB    1 
ATOM   2828  C  CG    . LEU A 1 349 ? 144.535 125.184 116.928 1.00 32.55 ?  349 LEU A CG    1 
ATOM   2829  C  CD1   . LEU A 1 349 ? 145.333 126.231 117.670 1.00 30.67 ?  349 LEU A CD1   1 
ATOM   2830  C  CD2   . LEU A 1 349 ? 143.132 125.071 117.498 1.00 34.59 ?  349 LEU A CD2   1 
ATOM   2831  N  N     . ARG A 1 350 ? 144.010 125.311 112.287 1.00 29.88 ?  350 ARG A N     1 
ATOM   2832  C  CA    . ARG A 1 350 ? 143.263 125.666 111.087 1.00 24.31 ?  350 ARG A CA    1 
ATOM   2833  C  C     . ARG A 1 350 ? 142.737 124.430 110.370 1.00 30.19 ?  350 ARG A C     1 
ATOM   2834  O  O     . ARG A 1 350 ? 141.649 124.471 109.785 1.00 34.35 ?  350 ARG A O     1 
ATOM   2835  C  CB    . ARG A 1 350 ? 144.137 126.500 110.152 1.00 26.02 ?  350 ARG A CB    1 
ATOM   2836  C  CG    . ARG A 1 350 ? 144.337 127.932 110.618 1.00 24.05 ?  350 ARG A CG    1 
ATOM   2837  C  CD    . ARG A 1 350 ? 145.459 128.613 109.856 1.00 23.05 ?  350 ARG A CD    1 
ATOM   2838  N  NE    . ARG A 1 350 ? 145.109 128.812 108.456 1.00 34.27 ?  350 ARG A NE    1 
ATOM   2839  C  CZ    . ARG A 1 350 ? 144.300 129.765 108.010 1.00 31.39 ?  350 ARG A CZ    1 
ATOM   2840  N  NH1   . ARG A 1 350 ? 143.748 130.644 108.831 1.00 24.59 1  350 ARG A NH1   1 
ATOM   2841  N  NH2   . ARG A 1 350 ? 144.037 129.836 106.709 1.00 28.80 ?  350 ARG A NH2   1 
ATOM   2842  N  N     . SER A 1 351 ? 143.492 123.331 110.391 1.00 33.50 ?  351 SER A N     1 
ATOM   2843  C  CA    . SER A 1 351 ? 142.990 122.085 109.824 1.00 30.16 ?  351 SER A CA    1 
ATOM   2844  C  C     . SER A 1 351 ? 141.786 121.570 110.603 1.00 31.45 ?  351 SER A C     1 
ATOM   2845  O  O     . SER A 1 351 ? 140.804 121.111 110.010 1.00 38.80 ?  351 SER A O     1 
ATOM   2846  C  CB    . SER A 1 351 ? 144.101 121.037 109.798 1.00 30.96 ?  351 SER A CB    1 
ATOM   2847  O  OG    . SER A 1 351 ? 145.045 121.318 108.780 1.00 39.77 ?  351 SER A OG    1 
ATOM   2848  N  N     . GLU A 1 352 ? 141.844 121.639 111.935 1.00 29.70 ?  352 GLU A N     1 
ATOM   2849  C  CA    . GLU A 1 352 ? 140.748 121.118 112.749 1.00 30.98 ?  352 GLU A CA    1 
ATOM   2850  C  C     . GLU A 1 352 ? 139.496 121.981 112.633 1.00 34.19 ?  352 GLU A C     1 
ATOM   2851  O  O     . GLU A 1 352 ? 138.390 121.460 112.446 1.00 39.10 ?  352 GLU A O     1 
ATOM   2852  C  CB    . GLU A 1 352 ? 141.178 120.996 114.213 1.00 33.49 ?  352 GLU A CB    1 
ATOM   2853  C  CG    . GLU A 1 352 ? 142.447 120.196 114.439 1.00 33.65 ?  352 GLU A CG    1 
ATOM   2854  C  CD    . GLU A 1 352 ? 142.947 120.290 115.868 1.00 42.38 ?  352 GLU A CD    1 
ATOM   2855  O  OE1   . GLU A 1 352 ? 143.694 119.387 116.299 1.00 41.46 ?  352 GLU A OE1   1 
ATOM   2856  O  OE2   . GLU A 1 352 ? 142.591 121.267 116.560 1.00 41.70 -1 352 GLU A OE2   1 
ATOM   2857  N  N     . SER A 1 353 ? 139.642 123.304 112.743 1.00 34.69 ?  353 SER A N     1 
ATOM   2858  C  CA    . SER A 1 353 ? 138.486 124.182 112.864 1.00 34.74 ?  353 SER A CA    1 
ATOM   2859  C  C     . SER A 1 353 ? 138.514 125.406 111.958 1.00 30.47 ?  353 SER A C     1 
ATOM   2860  O  O     . SER A 1 353 ? 137.550 126.178 111.969 1.00 31.06 ?  353 SER A O     1 
ATOM   2861  C  CB    . SER A 1 353 ? 138.331 124.651 114.318 1.00 34.34 ?  353 SER A CB    1 
ATOM   2862  O  OG    . SER A 1 353 ? 139.440 125.434 114.724 1.00 32.37 ?  353 SER A OG    1 
ATOM   2863  N  N     . GLY A 1 354 ? 139.574 125.613 111.182 1.00 27.70 ?  354 GLY A N     1 
ATOM   2864  C  CA    . GLY A 1 354 ? 139.676 126.796 110.354 1.00 27.40 ?  354 GLY A CA    1 
ATOM   2865  C  C     . GLY A 1 354 ? 140.159 128.034 111.070 1.00 21.81 ?  354 GLY A C     1 
ATOM   2866  O  O     . GLY A 1 354 ? 140.279 129.089 110.435 1.00 25.58 ?  354 GLY A O     1 
ATOM   2867  N  N     . TYR A 1 355 ? 140.446 127.943 112.363 1.00 22.77 ?  355 TYR A N     1 
ATOM   2868  C  CA    . TYR A 1 355 ? 140.922 129.038 113.184 1.00 17.75 ?  355 TYR A CA    1 
ATOM   2869  C  C     . TYR A 1 355 ? 142.397 128.843 113.519 1.00 22.19 ?  355 TYR A C     1 
ATOM   2870  O  O     . TYR A 1 355 ? 142.881 127.708 113.563 1.00 28.86 ?  355 TYR A O     1 
ATOM   2871  C  CB    . TYR A 1 355 ? 140.113 129.139 114.482 1.00 23.82 ?  355 TYR A CB    1 
ATOM   2872  C  CG    . TYR A 1 355 ? 138.696 129.621 114.283 1.00 26.78 ?  355 TYR A CG    1 
ATOM   2873  C  CD1   . TYR A 1 355 ? 138.437 130.836 113.666 1.00 20.43 ?  355 TYR A CD1   1 
ATOM   2874  C  CD2   . TYR A 1 355 ? 137.617 128.860 114.712 1.00 25.91 ?  355 TYR A CD2   1 
ATOM   2875  C  CE1   . TYR A 1 355 ? 137.144 131.280 113.482 1.00 27.50 ?  355 TYR A CE1   1 
ATOM   2876  C  CE2   . TYR A 1 355 ? 136.320 129.296 114.532 1.00 26.03 ?  355 TYR A CE2   1 
ATOM   2877  C  CZ    . TYR A 1 355 ? 136.090 130.505 113.916 1.00 30.59 ?  355 TYR A CZ    1 
ATOM   2878  O  OH    . TYR A 1 355 ? 134.799 130.945 113.735 1.00 31.21 ?  355 TYR A OH    1 
ATOM   2879  N  N     . PRO A 1 356 ? 143.142 129.923 113.770 1.00 22.84 ?  356 PRO A N     1 
ATOM   2880  C  CA    . PRO A 1 356 ? 142.737 131.333 113.780 1.00 17.73 ?  356 PRO A CA    1 
ATOM   2881  C  C     . PRO A 1 356 ? 142.839 132.006 112.421 1.00 15.52 ?  356 PRO A C     1 
ATOM   2882  O  O     . PRO A 1 356 ? 143.440 131.471 111.496 1.00 19.50 ?  356 PRO A O     1 
ATOM   2883  C  CB    . PRO A 1 356 ? 143.728 131.948 114.770 1.00 18.27 ?  356 PRO A CB    1 
ATOM   2884  C  CG    . PRO A 1 356 ? 144.988 131.180 114.502 1.00 17.73 ?  356 PRO A CG    1 
ATOM   2885  C  CD    . PRO A 1 356 ? 144.548 129.769 114.185 1.00 13.52 ?  356 PRO A CD    1 
ATOM   2886  N  N     . TYR A 1 357 ? 142.251 133.190 112.274 1.00 18.54 ?  357 TYR A N     1 
ATOM   2887  C  CA    . TYR A 1 357 ? 142.593 134.043 111.148 1.00 11.30 ?  357 TYR A CA    1 
ATOM   2888  C  C     . TYR A 1 357 ? 144.035 134.513 111.291 1.00 16.15 ?  357 TYR A C     1 
ATOM   2889  O  O     . TYR A 1 357 ? 144.530 134.742 112.397 1.00 25.34 ?  357 TYR A O     1 
ATOM   2890  C  CB    . TYR A 1 357 ? 141.657 135.250 111.068 1.00 15.07 ?  357 TYR A CB    1 
ATOM   2891  C  CG    . TYR A 1 357 ? 140.191 134.953 111.297 1.00 18.99 ?  357 TYR A CG    1 
ATOM   2892  C  CD1   . TYR A 1 357 ? 139.622 133.768 110.856 1.00 14.29 ?  357 TYR A CD1   1 
ATOM   2893  C  CD2   . TYR A 1 357 ? 139.375 135.863 111.952 1.00 18.46 ?  357 TYR A CD2   1 
ATOM   2894  C  CE1   . TYR A 1 357 ? 138.288 133.496 111.058 1.00 14.64 ?  357 TYR A CE1   1 
ATOM   2895  C  CE2   . TYR A 1 357 ? 138.037 135.600 112.162 1.00 17.60 ?  357 TYR A CE2   1 
ATOM   2896  C  CZ    . TYR A 1 357 ? 137.499 134.414 111.713 1.00 21.97 ?  357 TYR A CZ    1 
ATOM   2897  O  OH    . TYR A 1 357 ? 136.167 134.142 111.915 1.00 26.52 ?  357 TYR A OH    1 
ATOM   2898  N  N     . ILE A 1 358 ? 144.716 134.648 110.159 1.00 14.85 ?  358 ILE A N     1 
ATOM   2899  C  CA    . ILE A 1 358 ? 146.116 135.045 110.129 1.00 13.71 ?  358 ILE A CA    1 
ATOM   2900  C  C     . ILE A 1 358 ? 146.204 136.457 109.571 1.00 16.73 ?  358 ILE A C     1 
ATOM   2901  O  O     . ILE A 1 358 ? 145.729 136.723 108.461 1.00 25.12 ?  358 ILE A O     1 
ATOM   2902  C  CB    . ILE A 1 358 ? 146.965 134.073 109.293 1.00 18.73 ?  358 ILE A CB    1 
ATOM   2903  C  CG1   . ILE A 1 358 ? 146.720 132.629 109.736 1.00 21.88 ?  358 ILE A CG1   1 
ATOM   2904  C  CG2   . ILE A 1 358 ? 148.437 134.427 109.402 1.00 17.24 ?  358 ILE A CG2   1 
ATOM   2905  C  CD1   . ILE A 1 358 ? 147.189 132.333 111.140 1.00 18.48 ?  358 ILE A CD1   1 
ATOM   2906  N  N     . MET A 1 359 ? 146.805 137.359 110.340 1.00 10.67 ?  359 MET A N     1 
ATOM   2907  C  CA    . MET A 1 359 ? 147.091 138.713 109.887 1.00 8.82  ?  359 MET A CA    1 
ATOM   2908  C  C     . MET A 1 359 ? 148.600 138.885 109.824 1.00 10.43 ?  359 MET A C     1 
ATOM   2909  O  O     . MET A 1 359 ? 149.284 138.783 110.848 1.00 21.36 ?  359 MET A O     1 
ATOM   2910  C  CB    . MET A 1 359 ? 146.472 139.759 110.814 1.00 11.87 ?  359 MET A CB    1 
ATOM   2911  C  CG    . MET A 1 359 ? 145.844 140.926 110.074 1.00 12.10 ?  359 MET A CG    1 
ATOM   2912  S  SD    . MET A 1 359 ? 145.840 142.485 110.976 1.00 33.65 ?  359 MET A SD    1 
ATOM   2913  C  CE    . MET A 1 359 ? 147.575 142.907 110.954 1.00 12.22 ?  359 MET A CE    1 
ATOM   2914  N  N     . PHE A 1 360 ? 149.116 139.139 108.626 1.00 10.78 ?  360 PHE A N     1 
ATOM   2915  C  CA    . PHE A 1 360 ? 150.534 139.424 108.436 1.00 11.58 ?  360 PHE A CA    1 
ATOM   2916  C  C     . PHE A 1 360 ? 150.719 140.924 108.622 1.00 15.89 ?  360 PHE A C     1 
ATOM   2917  O  O     . PHE A 1 360 ? 150.465 141.711 107.707 1.00 25.75 ?  360 PHE A O     1 
ATOM   2918  C  CB    . PHE A 1 360 ? 150.998 138.944 107.066 1.00 9.13  ?  360 PHE A CB    1 
ATOM   2919  C  CG    . PHE A 1 360 ? 150.907 137.455 106.894 1.00 17.71 ?  360 PHE A CG    1 
ATOM   2920  C  CD1   . PHE A 1 360 ? 151.591 136.605 107.745 1.00 16.06 ?  360 PHE A CD1   1 
ATOM   2921  C  CD2   . PHE A 1 360 ? 150.129 136.904 105.890 1.00 13.68 ?  360 PHE A CD2   1 
ATOM   2922  C  CE1   . PHE A 1 360 ? 151.506 135.235 107.596 1.00 11.57 ?  360 PHE A CE1   1 
ATOM   2923  C  CE2   . PHE A 1 360 ? 150.041 135.537 105.736 1.00 17.28 ?  360 PHE A CE2   1 
ATOM   2924  C  CZ    . PHE A 1 360 ? 150.731 134.701 106.590 1.00 15.05 ?  360 PHE A CZ    1 
ATOM   2925  N  N     . GLN A 1 361 ? 151.164 141.314 109.819 1.00 11.68 ?  361 GLN A N     1 
ATOM   2926  C  CA    . GLN A 1 361 ? 151.153 142.720 110.213 1.00 11.92 ?  361 GLN A CA    1 
ATOM   2927  C  C     . GLN A 1 361 ? 151.983 143.577 109.266 1.00 15.94 ?  361 GLN A C     1 
ATOM   2928  O  O     . GLN A 1 361 ? 151.546 144.654 108.840 1.00 20.44 ?  361 GLN A O     1 
ATOM   2929  C  CB    . GLN A 1 361 ? 151.669 142.857 111.646 1.00 23.22 ?  361 GLN A CB    1 
ATOM   2930  C  CG    . GLN A 1 361 ? 151.399 144.211 112.274 1.00 17.97 ?  361 GLN A CG    1 
ATOM   2931  C  CD    . GLN A 1 361 ? 151.053 144.113 113.742 1.00 20.29 ?  361 GLN A CD    1 
ATOM   2932  O  OE1   . GLN A 1 361 ? 151.542 143.235 114.448 1.00 24.15 ?  361 GLN A OE1   1 
ATOM   2933  N  NE2   . GLN A 1 361 ? 150.208 145.023 114.210 1.00 23.91 ?  361 GLN A NE2   1 
ATOM   2934  N  N     . ASP A 1 362 ? 153.189 143.121 108.930 1.00 18.11 ?  362 ASP A N     1 
ATOM   2935  C  CA    . ASP A 1 362 ? 154.057 143.928 108.081 1.00 17.14 ?  362 ASP A CA    1 
ATOM   2936  C  C     . ASP A 1 362 ? 153.566 143.966 106.641 1.00 18.27 ?  362 ASP A C     1 
ATOM   2937  O  O     . ASP A 1 362 ? 153.748 144.978 105.959 1.00 19.69 ?  362 ASP A O     1 
ATOM   2938  C  CB    . ASP A 1 362 ? 155.491 143.412 108.153 1.00 18.97 ?  362 ASP A CB    1 
ATOM   2939  C  CG    . ASP A 1 362 ? 156.045 143.442 109.561 1.00 30.49 ?  362 ASP A CG    1 
ATOM   2940  O  OD1   . ASP A 1 362 ? 155.355 142.959 110.484 1.00 27.74 ?  362 ASP A OD1   1 
ATOM   2941  O  OD2   . ASP A 1 362 ? 157.169 143.951 109.747 1.00 34.52 -1 362 ASP A OD2   1 
ATOM   2942  N  N     . ASN A 1 363 ? 152.929 142.893 106.169 1.00 18.08 ?  363 ASN A N     1 
ATOM   2943  C  CA    . ASN A 1 363 ? 152.319 142.929 104.844 1.00 10.98 ?  363 ASN A CA    1 
ATOM   2944  C  C     . ASN A 1 363 ? 151.220 143.981 104.778 1.00 13.44 ?  363 ASN A C     1 
ATOM   2945  O  O     . ASN A 1 363 ? 151.047 144.649 103.752 1.00 21.41 ?  363 ASN A O     1 
ATOM   2946  C  CB    . ASN A 1 363 ? 151.768 141.551 104.479 1.00 11.67 ?  363 ASN A CB    1 
ATOM   2947  C  CG    . ASN A 1 363 ? 152.843 140.606 103.986 1.00 18.13 ?  363 ASN A CG    1 
ATOM   2948  O  OD1   . ASN A 1 363 ? 153.973 141.016 103.724 1.00 19.36 ?  363 ASN A OD1   1 
ATOM   2949  N  ND2   . ASN A 1 363 ? 152.496 139.333 103.856 1.00 18.77 ?  363 ASN A ND2   1 
ATOM   2950  N  N     . VAL A 1 364 ? 150.460 144.137 105.862 1.00 9.09  ?  364 VAL A N     1 
ATOM   2951  C  CA    . VAL A 1 364 ? 149.427 145.167 105.907 1.00 10.59 ?  364 VAL A CA    1 
ATOM   2952  C  C     . VAL A 1 364 ? 150.056 146.552 105.987 1.00 17.38 ?  364 VAL A C     1 
ATOM   2953  O  O     . VAL A 1 364 ? 149.640 147.483 105.288 1.00 16.12 ?  364 VAL A O     1 
ATOM   2954  C  CB    . VAL A 1 364 ? 148.475 144.919 107.090 1.00 1.48  ?  364 VAL A CB    1 
ATOM   2955  C  CG1   . VAL A 1 364 ? 147.354 145.942 107.085 1.00 4.43  ?  364 VAL A CG1   1 
ATOM   2956  C  CG2   . VAL A 1 364 ? 147.920 143.510 107.046 1.00 8.10  ?  364 VAL A CG2   1 
ATOM   2957  N  N     . ASN A 1 365 ? 151.070 146.710 106.837 1.00 21.00 ?  365 ASN A N     1 
ATOM   2958  C  CA    . ASN A 1 365 ? 151.566 148.031 107.197 1.00 11.91 ?  365 ASN A CA    1 
ATOM   2959  C  C     . ASN A 1 365 ? 152.639 148.571 106.259 1.00 15.26 ?  365 ASN A C     1 
ATOM   2960  O  O     . ASN A 1 365 ? 152.942 149.767 106.327 1.00 21.76 ?  365 ASN A O     1 
ATOM   2961  C  CB    . ASN A 1 365 ? 152.103 148.011 108.631 1.00 13.85 ?  365 ASN A CB    1 
ATOM   2962  C  CG    . ASN A 1 365 ? 150.997 147.957 109.661 1.00 15.71 ?  365 ASN A CG    1 
ATOM   2963  O  OD1   . ASN A 1 365 ? 150.097 148.797 109.667 1.00 12.41 ?  365 ASN A OD1   1 
ATOM   2964  N  ND2   . ASN A 1 365 ? 151.052 146.964 110.537 1.00 18.99 ?  365 ASN A ND2   1 
ATOM   2965  N  N     . LYS A 1 366 ? 153.217 147.743 105.389 1.00 19.00 ?  366 LYS A N     1 
ATOM   2966  C  CA    . LYS A 1 366 ? 154.166 148.251 104.410 1.00 15.84 ?  366 LYS A CA    1 
ATOM   2967  C  C     . LYS A 1 366 ? 153.480 148.959 103.251 1.00 19.99 ?  366 LYS A C     1 
ATOM   2968  O  O     . LYS A 1 366 ? 154.144 149.693 102.512 1.00 29.30 ?  366 LYS A O     1 
ATOM   2969  C  CB    . LYS A 1 366 ? 155.041 147.111 103.882 1.00 13.23 ?  366 LYS A CB    1 
ATOM   2970  C  CG    . LYS A 1 366 ? 154.412 146.298 102.768 1.00 19.82 ?  366 LYS A CG    1 
ATOM   2971  C  CD    . LYS A 1 366 ? 154.983 144.889 102.735 1.00 23.35 ?  366 LYS A CD    1 
ATOM   2972  C  CE    . LYS A 1 366 ? 154.260 144.020 101.719 1.00 26.32 ?  366 LYS A CE    1 
ATOM   2973  N  NZ    . LYS A 1 366 ? 152.795 144.286 101.692 1.00 25.54 1  366 LYS A NZ    1 
ATOM   2974  N  N     . VAL A 1 367 ? 152.176 148.755 103.083 1.00 25.26 ?  367 VAL A N     1 
ATOM   2975  C  CA    . VAL A 1 367 ? 151.374 149.471 102.103 1.00 15.02 ?  367 VAL A CA    1 
ATOM   2976  C  C     . VAL A 1 367 ? 150.264 150.279 102.750 1.00 14.05 ?  367 VAL A C     1 
ATOM   2977  O  O     . VAL A 1 367 ? 149.453 150.878 102.038 1.00 18.32 ?  367 VAL A O     1 
ATOM   2978  C  CB    . VAL A 1 367 ? 150.791 148.509 101.048 1.00 13.12 ?  367 VAL A CB    1 
ATOM   2979  C  CG1   . VAL A 1 367 ? 151.860 148.121 100.041 1.00 17.27 ?  367 VAL A CG1   1 
ATOM   2980  C  CG2   . VAL A 1 367 ? 150.227 147.276 101.723 1.00 4.98  ?  367 VAL A CG2   1 
ATOM   2981  N  N     . HIS A 1 368 ? 150.202 150.311 104.079 1.00 14.46 ?  368 HIS A N     1 
ATOM   2982  C  CA    . HIS A 1 368 ? 149.190 151.090 104.776 1.00 6.03  ?  368 HIS A CA    1 
ATOM   2983  C  C     . HIS A 1 368 ? 149.436 152.578 104.562 1.00 15.52 ?  368 HIS A C     1 
ATOM   2984  O  O     . HIS A 1 368 ? 150.547 153.073 104.771 1.00 25.03 ?  368 HIS A O     1 
ATOM   2985  C  CB    . HIS A 1 368 ? 149.209 150.756 106.266 1.00 12.53 ?  368 HIS A CB    1 
ATOM   2986  C  CG    . HIS A 1 368 ? 148.072 151.349 107.035 1.00 8.17  ?  368 HIS A CG    1 
ATOM   2987  N  ND1   . HIS A 1 368 ? 148.213 151.822 108.322 1.00 13.52 ?  368 HIS A ND1   1 
ATOM   2988  C  CD2   . HIS A 1 368 ? 146.775 151.545 106.703 1.00 10.74 ?  368 HIS A CD2   1 
ATOM   2989  C  CE1   . HIS A 1 368 ? 147.051 152.284 108.748 1.00 15.09 ?  368 HIS A CE1   1 
ATOM   2990  N  NE2   . HIS A 1 368 ? 146.162 152.127 107.785 1.00 7.25  ?  368 HIS A NE2   1 
ATOM   2991  N  N     . ALA A 1 369 ? 148.391 153.292 104.144 1.00 18.25 ?  369 ALA A N     1 
ATOM   2992  C  CA    . ALA A 1 369 ? 148.525 154.709 103.846 1.00 12.50 ?  369 ALA A CA    1 
ATOM   2993  C  C     . ALA A 1 369 ? 148.420 155.592 105.080 1.00 17.79 ?  369 ALA A C     1 
ATOM   2994  O  O     . ALA A 1 369 ? 148.824 156.757 105.024 1.00 25.01 ?  369 ALA A O     1 
ATOM   2995  C  CB    . ALA A 1 369 ? 147.466 155.131 102.828 1.00 8.96  ?  369 ALA A CB    1 
ATOM   2996  N  N     . ASN A 1 370 ? 147.905 155.070 106.189 1.00 17.23 ?  370 ASN A N     1 
ATOM   2997  C  CA    . ASN A 1 370 ? 147.644 155.862 107.383 1.00 12.34 ?  370 ASN A CA    1 
ATOM   2998  C  C     . ASN A 1 370 ? 148.420 155.329 108.580 1.00 12.14 ?  370 ASN A C     1 
ATOM   2999  O  O     . ASN A 1 370 ? 147.888 155.212 109.686 1.00 21.21 ?  370 ASN A O     1 
ATOM   3000  C  CB    . ASN A 1 370 ? 146.149 155.903 107.686 1.00 12.21 ?  370 ASN A CB    1 
ATOM   3001  C  CG    . ASN A 1 370 ? 145.340 156.464 106.538 1.00 10.47 ?  370 ASN A CG    1 
ATOM   3002  O  OD1   . ASN A 1 370 ? 145.544 157.602 106.119 1.00 26.58 ?  370 ASN A OD1   1 
ATOM   3003  N  ND2   . ASN A 1 370 ? 144.419 155.666 106.017 1.00 12.40 ?  370 ASN A ND2   1 
ATOM   3004  N  N     . ASN A 1 371 ? 149.696 154.998 108.373 1.00 14.37 ?  371 ASN A N     1 
ATOM   3005  C  CA    . ASN A 1 371 ? 150.540 154.567 109.480 1.00 11.15 ?  371 ASN A CA    1 
ATOM   3006  C  C     . ASN A 1 371 ? 150.809 155.690 110.471 1.00 16.52 ?  371 ASN A C     1 
ATOM   3007  O  O     . ASN A 1 371 ? 151.101 155.411 111.638 1.00 19.08 ?  371 ASN A O     1 
ATOM   3008  C  CB    . ASN A 1 371 ? 151.861 154.010 108.953 1.00 8.50  ?  371 ASN A CB    1 
ATOM   3009  C  CG    . ASN A 1 371 ? 151.766 152.547 108.578 1.00 16.56 ?  371 ASN A CG    1 
ATOM   3010  O  OD1   . ASN A 1 371 ? 150.909 151.822 109.079 1.00 20.95 ?  371 ASN A OD1   1 
ATOM   3011  N  ND2   . ASN A 1 371 ? 152.649 152.105 107.692 1.00 18.37 ?  371 ASN A ND2   1 
ATOM   3012  N  N     . HIS A 1 372 ? 150.730 156.947 110.029 1.00 19.53 ?  372 HIS A N     1 
ATOM   3013  C  CA    . HIS A 1 372 ? 150.910 158.068 110.947 1.00 15.92 ?  372 HIS A CA    1 
ATOM   3014  C  C     . HIS A 1 372 ? 149.815 158.094 112.006 1.00 16.49 ?  372 HIS A C     1 
ATOM   3015  O  O     . HIS A 1 372 ? 150.088 158.359 113.183 1.00 25.78 ?  372 HIS A O     1 
ATOM   3016  C  CB    . HIS A 1 372 ? 150.937 159.382 110.167 1.00 18.05 ?  372 HIS A CB    1 
ATOM   3017  C  CG    . HIS A 1 372 ? 149.634 159.723 109.515 1.00 18.35 ?  372 HIS A CG    1 
ATOM   3018  N  ND1   . HIS A 1 372 ? 149.058 158.934 108.544 1.00 23.68 ?  372 HIS A ND1   1 
ATOM   3019  C  CD2   . HIS A 1 372 ? 148.789 160.764 109.703 1.00 18.43 ?  372 HIS A CD2   1 
ATOM   3020  C  CE1   . HIS A 1 372 ? 147.916 159.474 108.161 1.00 17.06 ?  372 HIS A CE1   1 
ATOM   3021  N  NE2   . HIS A 1 372 ? 147.731 160.587 108.846 1.00 17.38 ?  372 HIS A NE2   1 
ATOM   3022  N  N     . ILE A 1 373 ? 148.569 157.836 111.605 1.00 16.32 ?  373 ILE A N     1 
ATOM   3023  C  CA    . ILE A 1 373 ? 147.482 157.739 112.576 1.00 18.68 ?  373 ILE A CA    1 
ATOM   3024  C  C     . ILE A 1 373 ? 147.720 156.563 113.509 1.00 15.16 ?  373 ILE A C     1 
ATOM   3025  O  O     . ILE A 1 373 ? 147.697 156.701 114.738 1.00 28.13 ?  373 ILE A O     1 
ATOM   3026  C  CB    . ILE A 1 373 ? 146.129 157.612 111.853 1.00 19.22 ?  373 ILE A CB    1 
ATOM   3027  C  CG1   . ILE A 1 373 ? 145.889 158.816 110.946 1.00 15.45 ?  373 ILE A CG1   1 
ATOM   3028  C  CG2   . ILE A 1 373 ? 144.998 157.456 112.858 1.00 19.60 ?  373 ILE A CG2   1 
ATOM   3029  C  CD1   . ILE A 1 373 ? 144.743 158.632 109.982 1.00 15.20 ?  373 ILE A CD1   1 
ATOM   3030  N  N     . SER A 1 374 ? 147.978 155.391 112.931 1.00 16.92 ?  374 SER A N     1 
ATOM   3031  C  CA    . SER A 1 374 ? 148.236 154.165 113.670 1.00 12.66 ?  374 SER A CA    1 
ATOM   3032  C  C     . SER A 1 374 ? 148.595 153.057 112.693 1.00 14.27 ?  374 SER A C     1 
ATOM   3033  O  O     . SER A 1 374 ? 148.197 153.103 111.525 1.00 21.20 ?  374 SER A O     1 
ATOM   3034  C  CB    . SER A 1 374 ? 147.020 153.760 114.503 1.00 19.05 ?  374 SER A CB    1 
ATOM   3035  O  OG    . SER A 1 374 ? 147.352 152.737 115.422 1.00 24.05 ?  374 SER A OG    1 
ATOM   3036  N  N     . LYS A 1 375 ? 149.344 152.062 113.148 1.00 22.39 ?  375 LYS A N     1 
ATOM   3037  C  CA    . LYS A 1 375 ? 149.535 150.867 112.345 1.00 19.34 ?  375 LYS A CA    1 
ATOM   3038  C  C     . LYS A 1 375 ? 148.358 149.922 112.544 1.00 15.28 ?  375 LYS A C     1 
ATOM   3039  O  O     . LYS A 1 375 ? 147.746 149.873 113.614 1.00 22.44 ?  375 LYS A O     1 
ATOM   3040  C  CB    . LYS A 1 375 ? 150.847 150.172 112.708 1.00 12.06 ?  375 LYS A CB    1 
ATOM   3041  C  CG    . LYS A 1 375 ? 152.073 150.859 112.132 1.00 16.85 ?  375 LYS A CG    1 
ATOM   3042  C  CD    . LYS A 1 375 ? 153.271 149.930 112.103 1.00 24.65 ?  375 LYS A CD    1 
ATOM   3043  C  CE    . LYS A 1 375 ? 154.433 150.567 111.363 1.00 24.19 ?  375 LYS A CE    1 
ATOM   3044  N  NZ    . LYS A 1 375 ? 155.562 149.617 111.174 1.00 29.43 1  375 LYS A NZ    1 
ATOM   3045  N  N     . VAL A 1 376 ? 148.030 149.179 111.490 1.00 15.10 ?  376 VAL A N     1 
ATOM   3046  C  CA    . VAL A 1 376 ? 146.930 148.223 111.555 1.00 15.74 ?  376 VAL A CA    1 
ATOM   3047  C  C     . VAL A 1 376 ? 147.353 147.082 112.476 1.00 13.96 ?  376 VAL A C     1 
ATOM   3048  O  O     . VAL A 1 376 ? 148.263 146.315 112.150 1.00 20.44 ?  376 VAL A O     1 
ATOM   3049  C  CB    . VAL A 1 376 ? 146.545 147.709 110.165 1.00 10.94 ?  376 VAL A CB    1 
ATOM   3050  C  CG1   . VAL A 1 376 ? 145.354 146.776 110.259 1.00 8.26  ?  376 VAL A CG1   1 
ATOM   3051  C  CG2   . VAL A 1 376 ? 146.247 148.873 109.236 1.00 3.91  ?  376 VAL A CG2   1 
ATOM   3052  N  N     . LYS A 1 377 ? 146.699 146.973 113.631 1.00 12.77 ?  377 LYS A N     1 
ATOM   3053  C  CA    . LYS A 1 377 ? 147.064 145.978 114.627 1.00 11.43 ?  377 LYS A CA    1 
ATOM   3054  C  C     . LYS A 1 377 ? 146.225 144.713 114.556 1.00 10.48 ?  377 LYS A C     1 
ATOM   3055  O  O     . LYS A 1 377 ? 146.661 143.676 115.062 1.00 24.90 ?  377 LYS A O     1 
ATOM   3056  C  CB    . LYS A 1 377 ? 146.947 146.563 116.038 1.00 15.92 ?  377 LYS A CB    1 
ATOM   3057  C  CG    . LYS A 1 377 ? 147.692 147.862 116.246 1.00 12.28 ?  377 LYS A CG    1 
ATOM   3058  C  CD    . LYS A 1 377 ? 146.982 148.706 117.283 1.00 21.26 ?  377 LYS A CD    1 
ATOM   3059  C  CE    . LYS A 1 377 ? 147.388 150.159 117.190 1.00 23.69 ?  377 LYS A CE    1 
ATOM   3060  N  NZ    . LYS A 1 377 ? 146.389 151.049 117.843 1.00 26.00 1  377 LYS A NZ    1 
ATOM   3061  N  N     . PHE A 1 378 ? 145.040 144.773 113.956 1.00 8.60  ?  378 PHE A N     1 
ATOM   3062  C  CA    . PHE A 1 378 ? 144.156 143.619 113.896 1.00 7.85  ?  378 PHE A CA    1 
ATOM   3063  C  C     . PHE A 1 378 ? 143.140 143.840 112.787 1.00 8.00  ?  378 PHE A C     1 
ATOM   3064  O  O     . PHE A 1 378 ? 143.068 144.913 112.185 1.00 15.64 ?  378 PHE A O     1 
ATOM   3065  C  CB    . PHE A 1 378 ? 143.475 143.363 115.247 1.00 6.52  ?  378 PHE A CB    1 
ATOM   3066  C  CG    . PHE A 1 378 ? 142.436 144.384 115.621 1.00 8.31  ?  378 PHE A CG    1 
ATOM   3067  C  CD1   . PHE A 1 378 ? 142.771 145.721 115.762 1.00 9.59  ?  378 PHE A CD1   1 
ATOM   3068  C  CD2   . PHE A 1 378 ? 141.128 144.001 115.856 1.00 5.15  ?  378 PHE A CD2   1 
ATOM   3069  C  CE1   . PHE A 1 378 ? 141.821 146.655 116.112 1.00 4.02  ?  378 PHE A CE1   1 
ATOM   3070  C  CE2   . PHE A 1 378 ? 140.174 144.931 116.207 1.00 9.56  ?  378 PHE A CE2   1 
ATOM   3071  C  CZ    . PHE A 1 378 ? 140.522 146.259 116.336 1.00 11.53 ?  378 PHE A CZ    1 
ATOM   3072  N  N     . SER A 1 379 ? 142.356 142.802 112.521 1.00 3.31  ?  379 SER A N     1 
ATOM   3073  C  CA    . SER A 1 379 ? 141.373 142.800 111.447 1.00 4.14  ?  379 SER A CA    1 
ATOM   3074  C  C     . SER A 1 379 ? 139.979 142.579 112.032 1.00 5.96  ?  379 SER A C     1 
ATOM   3075  O  O     . SER A 1 379 ? 139.785 142.571 113.249 1.00 12.37 ?  379 SER A O     1 
ATOM   3076  C  CB    . SER A 1 379 ? 141.724 141.740 110.402 1.00 5.03  ?  379 SER A CB    1 
ATOM   3077  O  OG    . SER A 1 379 ? 141.188 142.081 109.137 1.00 8.38  ?  379 SER A OG    1 
ATOM   3078  N  N     . ASN A 1 380 ? 139.003 142.402 111.147 1.00 11.92 ?  380 ASN A N     1 
ATOM   3079  C  CA    . ASN A 1 380 ? 137.613 142.261 111.537 1.00 9.17  ?  380 ASN A CA    1 
ATOM   3080  C  C     . ASN A 1 380 ? 137.247 140.785 111.673 1.00 9.46  ?  380 ASN A C     1 
ATOM   3081  O  O     . ASN A 1 380 ? 138.100 139.896 111.610 1.00 9.92  ?  380 ASN A O     1 
ATOM   3082  C  CB    . ASN A 1 380 ? 136.708 142.975 110.532 1.00 2.71  ?  380 ASN A CB    1 
ATOM   3083  C  CG    . ASN A 1 380 ? 136.664 142.280 109.190 1.00 3.90  ?  380 ASN A CG    1 
ATOM   3084  O  OD1   . ASN A 1 380 ? 137.699 141.976 108.599 1.00 12.64 ?  380 ASN A OD1   1 
ATOM   3085  N  ND2   . ASN A 1 380 ? 135.459 142.021 108.700 1.00 10.73 ?  380 ASN A ND2   1 
ATOM   3086  N  N     . LEU A 1 381 ? 135.954 140.521 111.870 1.00 17.84 ?  381 LEU A N     1 
ATOM   3087  C  CA    . LEU A 1 381 ? 135.461 139.154 111.974 1.00 6.52  ?  381 LEU A CA    1 
ATOM   3088  C  C     . LEU A 1 381 ? 135.635 138.377 110.675 1.00 6.70  ?  381 LEU A C     1 
ATOM   3089  O  O     . LEU A 1 381 ? 135.769 137.150 110.714 1.00 15.30 ?  381 LEU A O     1 
ATOM   3090  C  CB    . LEU A 1 381 ? 133.990 139.174 112.394 1.00 11.71 ?  381 LEU A CB    1 
ATOM   3091  C  CG    . LEU A 1 381 ? 133.188 137.873 112.429 1.00 20.37 ?  381 LEU A CG    1 
ATOM   3092  C  CD1   . LEU A 1 381 ? 133.723 136.923 113.484 1.00 14.47 ?  381 LEU A CD1   1 
ATOM   3093  C  CD2   . LEU A 1 381 ? 131.720 138.173 112.669 1.00 15.89 ?  381 LEU A CD2   1 
ATOM   3094  N  N     . CYS A 1 382 ? 135.645 139.058 109.532 1.00 8.83  ?  382 CYS A N     1 
ATOM   3095  C  CA    . CYS A 1 382 ? 135.856 138.419 108.242 1.00 6.39  ?  382 CYS A CA    1 
ATOM   3096  C  C     . CYS A 1 382 ? 137.283 138.572 107.735 1.00 10.63 ?  382 CYS A C     1 
ATOM   3097  O  O     . CYS A 1 382 ? 137.589 138.099 106.635 1.00 17.01 ?  382 CYS A O     1 
ATOM   3098  C  CB    . CYS A 1 382 ? 134.873 138.980 107.209 1.00 15.57 ?  382 CYS A CB    1 
ATOM   3099  S  SG    . CYS A 1 382 ? 133.135 138.857 107.693 1.00 35.34 ?  382 CYS A SG    1 
ATOM   3100  N  N     . SER A 1 383 ? 138.157 139.217 108.510 1.00 11.05 ?  383 SER A N     1 
ATOM   3101  C  CA    . SER A 1 383 ? 139.583 139.335 108.198 1.00 8.94  ?  383 SER A CA    1 
ATOM   3102  C  C     . SER A 1 383 ? 139.820 140.005 106.846 1.00 12.51 ?  383 SER A C     1 
ATOM   3103  O  O     . SER A 1 383 ? 140.630 139.544 106.040 1.00 22.80 ?  383 SER A O     1 
ATOM   3104  C  CB    . SER A 1 383 ? 140.274 137.971 108.253 1.00 12.13 ?  383 SER A CB    1 
ATOM   3105  O  OG    . SER A 1 383 ? 139.976 137.206 107.101 1.00 20.92 ?  383 SER A OG    1 
ATOM   3106  N  N     . GLU A 1 384 ? 139.109 141.101 106.587 1.00 8.02  ?  384 GLU A N     1 
ATOM   3107  C  CA    . GLU A 1 384 ? 139.373 141.909 105.405 1.00 11.46 ?  384 GLU A CA    1 
ATOM   3108  C  C     . GLU A 1 384 ? 139.436 143.403 105.687 1.00 13.32 ?  384 GLU A C     1 
ATOM   3109  O  O     . GLU A 1 384 ? 139.931 144.149 104.836 1.00 22.51 ?  384 GLU A O     1 
ATOM   3110  C  CB    . GLU A 1 384 ? 138.323 141.636 104.313 1.00 6.55  ?  384 GLU A CB    1 
ATOM   3111  C  CG    . GLU A 1 384 ? 137.266 142.710 104.111 1.00 7.25  ?  384 GLU A CG    1 
ATOM   3112  C  CD    . GLU A 1 384 ? 136.132 142.616 105.106 1.00 16.76 ?  384 GLU A CD    1 
ATOM   3113  O  OE1   . GLU A 1 384 ? 135.994 141.558 105.751 1.00 19.97 ?  384 GLU A OE1   1 
ATOM   3114  O  OE2   . GLU A 1 384 ? 135.366 143.592 105.228 1.00 21.02 -1 384 GLU A OE2   1 
ATOM   3115  N  N     . VAL A 1 385 ? 138.980 143.860 106.847 1.00 13.29 ?  385 VAL A N     1 
ATOM   3116  C  CA    . VAL A 1 385 ? 139.079 145.265 107.222 1.00 3.12  ?  385 VAL A CA    1 
ATOM   3117  C  C     . VAL A 1 385 ? 140.423 145.484 107.899 1.00 15.14 ?  385 VAL A C     1 
ATOM   3118  O  O     . VAL A 1 385 ? 140.715 144.873 108.932 1.00 19.40 ?  385 VAL A O     1 
ATOM   3119  C  CB    . VAL A 1 385 ? 137.924 145.681 108.143 1.00 3.77  ?  385 VAL A CB    1 
ATOM   3120  C  CG1   . VAL A 1 385 ? 138.031 147.150 108.471 1.00 10.14 ?  385 VAL A CG1   1 
ATOM   3121  C  CG2   . VAL A 1 385 ? 136.595 145.382 107.492 1.00 8.54  ?  385 VAL A CG2   1 
ATOM   3122  N  N     . LEU A 1 386 ? 141.245 146.355 107.318 1.00 16.86 ?  386 LEU A N     1 
ATOM   3123  C  CA    . LEU A 1 386 ? 142.584 146.642 107.825 1.00 3.54  ?  386 LEU A CA    1 
ATOM   3124  C  C     . LEU A 1 386 ? 142.760 148.156 107.866 1.00 7.34  ?  386 LEU A C     1 
ATOM   3125  O  O     . LEU A 1 386 ? 143.085 148.779 106.852 1.00 8.00  ?  386 LEU A O     1 
ATOM   3126  C  CB    . LEU A 1 386 ? 143.648 145.979 106.961 1.00 3.17  ?  386 LEU A CB    1 
ATOM   3127  C  CG    . LEU A 1 386 ? 143.572 144.455 106.957 1.00 7.86  ?  386 LEU A CG    1 
ATOM   3128  C  CD1   . LEU A 1 386 ? 144.513 143.892 105.931 1.00 9.37  ?  386 LEU A CD1   1 
ATOM   3129  C  CD2   . LEU A 1 386 ? 143.890 143.907 108.336 1.00 6.77  ?  386 LEU A CD2   1 
ATOM   3130  N  N     . GLN A 1 387 ? 142.548 148.742 109.041 1.00 14.69 ?  387 GLN A N     1 
ATOM   3131  C  CA    . GLN A 1 387 ? 142.556 150.187 109.195 1.00 4.40  ?  387 GLN A CA    1 
ATOM   3132  C  C     . GLN A 1 387 ? 143.317 150.571 110.453 1.00 6.85  ?  387 GLN A C     1 
ATOM   3133  O  O     . GLN A 1 387 ? 143.515 149.762 111.362 1.00 18.95 ?  387 GLN A O     1 
ATOM   3134  C  CB    . GLN A 1 387 ? 141.133 150.754 109.256 1.00 6.31  ?  387 GLN A CB    1 
ATOM   3135  C  CG    . GLN A 1 387 ? 140.275 150.384 108.070 1.00 8.48  ?  387 GLN A CG    1 
ATOM   3136  C  CD    . GLN A 1 387 ? 138.970 151.135 108.053 1.00 6.84  ?  387 GLN A CD    1 
ATOM   3137  O  OE1   . GLN A 1 387 ? 138.764 152.059 108.834 1.00 19.59 ?  387 GLN A OE1   1 
ATOM   3138  N  NE2   . GLN A 1 387 ? 138.083 150.750 107.150 1.00 8.43  ?  387 GLN A NE2   1 
ATOM   3139  N  N     . ALA A 1 388 ? 143.758 151.825 110.484 1.00 10.17 ?  388 ALA A N     1 
ATOM   3140  C  CA    . ALA A 1 388 ? 144.384 152.371 111.678 1.00 9.47  ?  388 ALA A CA    1 
ATOM   3141  C  C     . ALA A 1 388 ? 143.356 152.525 112.790 1.00 14.32 ?  388 ALA A C     1 
ATOM   3142  O  O     . ALA A 1 388 ? 142.232 152.980 112.562 1.00 25.46 ?  388 ALA A O     1 
ATOM   3143  C  CB    . ALA A 1 388 ? 145.029 153.721 111.368 1.00 12.02 ?  388 ALA A CB    1 
ATOM   3144  N  N     . SER A 1 389 ? 143.744 152.134 114.001 1.00 17.96 ?  389 SER A N     1 
ATOM   3145  C  CA    . SER A 1 389 ? 142.877 152.255 115.163 1.00 8.83  ?  389 SER A CA    1 
ATOM   3146  C  C     . SER A 1 389 ? 143.682 152.781 116.339 1.00 13.12 ?  389 SER A C     1 
ATOM   3147  O  O     . SER A 1 389 ? 144.844 152.412 116.521 1.00 24.46 ?  389 SER A O     1 
ATOM   3148  C  CB    . SER A 1 389 ? 142.235 150.912 115.526 1.00 16.70 ?  389 SER A CB    1 
ATOM   3149  O  OG    . SER A 1 389 ? 143.177 149.858 115.452 1.00 21.83 ?  389 SER A OG    1 
ATOM   3150  N  N     . GLN A 1 390 ? 143.055 153.641 117.135 1.00 17.64 ?  390 GLN A N     1 
ATOM   3151  C  CA    . GLN A 1 390 ? 143.651 154.171 118.353 1.00 14.92 ?  390 GLN A CA    1 
ATOM   3152  C  C     . GLN A 1 390 ? 142.828 153.701 119.541 1.00 13.36 ?  390 GLN A C     1 
ATOM   3153  O  O     . GLN A 1 390 ? 141.601 153.830 119.540 1.00 17.32 ?  390 GLN A O     1 
ATOM   3154  C  CB    . GLN A 1 390 ? 143.721 155.699 118.319 1.00 10.33 ?  390 GLN A CB    1 
ATOM   3155  C  CG    . GLN A 1 390 ? 144.775 156.246 117.372 1.00 15.85 ?  390 GLN A CG    1 
ATOM   3156  C  CD    . GLN A 1 390 ? 144.626 157.733 117.128 1.00 25.93 ?  390 GLN A CD    1 
ATOM   3157  O  OE1   . GLN A 1 390 ? 143.656 158.351 117.565 1.00 24.72 ?  390 GLN A OE1   1 
ATOM   3158  N  NE2   . GLN A 1 390 ? 145.589 158.316 116.424 1.00 21.61 ?  390 GLN A NE2   1 
ATOM   3159  N  N     . VAL A 1 391 ? 143.507 153.150 120.549 1.00 24.05 ?  391 VAL A N     1 
ATOM   3160  C  CA    . VAL A 1 391 ? 142.810 152.634 121.718 1.00 20.62 ?  391 VAL A CA    1 
ATOM   3161  C  C     . VAL A 1 391 ? 142.208 153.787 122.513 1.00 22.62 ?  391 VAL A C     1 
ATOM   3162  O  O     . VAL A 1 391 ? 142.708 154.921 122.496 1.00 24.03 ?  391 VAL A O     1 
ATOM   3163  C  CB    . VAL A 1 391 ? 143.758 151.785 122.586 1.00 19.09 ?  391 VAL A CB    1 
ATOM   3164  C  CG1   . VAL A 1 391 ? 144.644 152.668 123.452 1.00 20.19 ?  391 VAL A CG1   1 
ATOM   3165  C  CG2   . VAL A 1 391 ? 142.967 150.805 123.439 1.00 17.61 ?  391 VAL A CG2   1 
ATOM   3166  N  N     . SER A 1 392 ? 141.108 153.501 123.198 1.00 27.56 ?  392 SER A N     1 
ATOM   3167  C  CA    . SER A 1 392 ? 140.435 154.475 124.041 1.00 19.89 ?  392 SER A CA    1 
ATOM   3168  C  C     . SER A 1 392 ? 140.736 154.190 125.506 1.00 29.15 ?  392 SER A C     1 
ATOM   3169  O  O     . SER A 1 392 ? 140.896 153.038 125.916 1.00 29.80 ?  392 SER A O     1 
ATOM   3170  C  CB    . SER A 1 392 ? 138.924 154.452 123.807 1.00 20.67 ?  392 SER A CB    1 
ATOM   3171  O  OG    . SER A 1 392 ? 138.612 154.708 122.450 1.00 27.89 ?  392 SER A OG    1 
ATOM   3172  N  N     . SER A 1 393 ? 140.818 155.257 126.292 1.00 31.70 ?  393 SER A N     1 
ATOM   3173  C  CA    . SER A 1 393 ? 141.049 155.165 127.731 1.00 28.10 ?  393 SER A CA    1 
ATOM   3174  C  C     . SER A 1 393 ? 139.719 155.440 128.424 1.00 30.16 ?  393 SER A C     1 
ATOM   3175  O  O     . SER A 1 393 ? 139.382 156.586 128.726 1.00 34.98 ?  393 SER A O     1 
ATOM   3176  C  CB    . SER A 1 393 ? 142.130 156.141 128.181 1.00 30.37 ?  393 SER A CB    1 
ATOM   3177  O  OG    . SER A 1 393 ? 143.419 155.668 127.832 1.00 36.82 ?  393 SER A OG    1 
ATOM   3178  N  N     . TYR A 1 394 ? 138.958 154.377 128.666 1.00 29.20 ?  394 TYR A N     1 
ATOM   3179  C  CA    . TYR A 1 394 ? 137.694 154.486 129.382 1.00 28.90 ?  394 TYR A CA    1 
ATOM   3180  C  C     . TYR A 1 394 ? 137.988 154.483 130.877 1.00 28.85 ?  394 TYR A C     1 
ATOM   3181  O  O     . TYR A 1 394 ? 138.353 153.450 131.443 1.00 33.55 ?  394 TYR A O     1 
ATOM   3182  C  CB    . TYR A 1 394 ? 136.760 153.345 128.994 1.00 24.98 ?  394 TYR A CB    1 
ATOM   3183  C  CG    . TYR A 1 394 ? 136.252 153.436 127.574 1.00 28.24 ?  394 TYR A CG    1 
ATOM   3184  C  CD1   . TYR A 1 394 ? 135.289 154.371 127.219 1.00 29.50 ?  394 TYR A CD1   1 
ATOM   3185  C  CD2   . TYR A 1 394 ? 136.742 152.592 126.586 1.00 26.55 ?  394 TYR A CD2   1 
ATOM   3186  C  CE1   . TYR A 1 394 ? 134.822 154.456 125.923 1.00 28.34 ?  394 TYR A CE1   1 
ATOM   3187  C  CE2   . TYR A 1 394 ? 136.281 152.670 125.288 1.00 27.08 ?  394 TYR A CE2   1 
ATOM   3188  C  CZ    . TYR A 1 394 ? 135.322 153.604 124.961 1.00 36.10 ?  394 TYR A CZ    1 
ATOM   3189  O  OH    . TYR A 1 394 ? 134.862 153.687 123.667 1.00 38.36 ?  394 TYR A OH    1 
ATOM   3190  N  N     . THR A 1 395 ? 137.833 155.639 131.512 1.00 35.82 ?  395 THR A N     1 
ATOM   3191  C  CA    . THR A 1 395 ? 138.189 155.812 132.911 1.00 37.45 ?  395 THR A CA    1 
ATOM   3192  C  C     . THR A 1 395 ? 137.020 155.398 133.804 1.00 38.54 ?  395 THR A C     1 
ATOM   3193  O  O     . THR A 1 395 ? 136.047 154.788 133.353 1.00 38.57 ?  395 THR A O     1 
ATOM   3194  C  CB    . THR A 1 395 ? 138.613 157.256 133.166 1.00 36.92 ?  395 THR A CB    1 
ATOM   3195  O  OG1   . THR A 1 395 ? 137.546 158.139 132.797 1.00 38.62 ?  395 THR A OG1   1 
ATOM   3196  C  CG2   . THR A 1 395 ? 139.849 157.597 132.349 1.00 35.25 ?  395 THR A CG2   1 
ATOM   3197  N  N     . ASP A 1 396 ? 137.112 155.723 135.091 1.00 36.30 ?  396 ASP A N     1 
ATOM   3198  C  CA    . ASP A 1 396 ? 136.047 155.419 136.033 1.00 36.61 ?  396 ASP A CA    1 
ATOM   3199  C  C     . ASP A 1 396 ? 134.816 156.269 135.725 1.00 38.06 ?  396 ASP A C     1 
ATOM   3200  O  O     . ASP A 1 396 ? 134.800 157.085 134.799 1.00 42.28 ?  396 ASP A O     1 
ATOM   3201  C  CB    . ASP A 1 396 ? 136.520 155.657 137.465 1.00 38.06 ?  396 ASP A CB    1 
ATOM   3202  C  CG    . ASP A 1 396 ? 137.783 154.890 137.803 1.00 42.51 ?  396 ASP A CG    1 
ATOM   3203  O  OD1   . ASP A 1 396 ? 138.038 153.845 137.167 1.00 43.52 ?  396 ASP A OD1   1 
ATOM   3204  O  OD2   . ASP A 1 396 ? 138.518 155.330 138.709 1.00 44.02 -1 396 ASP A OD2   1 
ATOM   3205  N  N     . TYR A 1 397 ? 133.765 156.071 136.517 1.00 37.44 ?  397 TYR A N     1 
ATOM   3206  C  CA    . TYR A 1 397 ? 132.589 156.915 136.403 1.00 34.06 ?  397 TYR A CA    1 
ATOM   3207  C  C     . TYR A 1 397 ? 132.953 158.358 136.752 1.00 37.34 ?  397 TYR A C     1 
ATOM   3208  O  O     . TYR A 1 397 ? 134.042 158.645 137.247 1.00 39.74 ?  397 TYR A O     1 
ATOM   3209  C  CB    . TYR A 1 397 ? 131.469 156.399 137.305 1.00 33.65 ?  397 TYR A CB    1 
ATOM   3210  C  CG    . TYR A 1 397 ? 130.084 156.784 136.835 1.00 33.80 ?  397 TYR A CG    1 
ATOM   3211  C  CD1   . TYR A 1 397 ? 129.424 156.031 135.873 1.00 36.07 ?  397 TYR A CD1   1 
ATOM   3212  C  CD2   . TYR A 1 397 ? 129.436 157.897 137.355 1.00 34.56 ?  397 TYR A CD2   1 
ATOM   3213  C  CE1   . TYR A 1 397 ? 128.160 156.378 135.440 1.00 33.88 ?  397 TYR A CE1   1 
ATOM   3214  C  CE2   . TYR A 1 397 ? 128.174 158.251 136.927 1.00 31.84 ?  397 TYR A CE2   1 
ATOM   3215  C  CZ    . TYR A 1 397 ? 127.540 157.489 135.972 1.00 34.09 ?  397 TYR A CZ    1 
ATOM   3216  O  OH    . TYR A 1 397 ? 126.281 157.838 135.545 1.00 39.73 ?  397 TYR A OH    1 
ATOM   3217  N  N     . ASP A 1 398 ? 132.035 159.270 136.416 1.00 41.00 ?  398 ASP A N     1 
ATOM   3218  C  CA    . ASP A 1 398 ? 132.127 160.722 136.587 1.00 42.01 ?  398 ASP A CA    1 
ATOM   3219  C  C     . ASP A 1 398 ? 133.531 161.238 136.277 1.00 44.08 ?  398 ASP A C     1 
ATOM   3220  O  O     . ASP A 1 398 ? 134.012 162.198 136.889 1.00 41.83 ?  398 ASP A O     1 
ATOM   3221  C  CB    . ASP A 1 398 ? 131.618 161.160 137.981 1.00 41.67 ?  398 ASP A CB    1 
ATOM   3222  C  CG    . ASP A 1 398 ? 132.625 160.971 139.126 1.00 44.94 ?  398 ASP A CG    1 
ATOM   3223  O  OD1   . ASP A 1 398 ? 132.342 161.504 140.218 1.00 45.96 ?  398 ASP A OD1   1 
ATOM   3224  O  OD2   . ASP A 1 398 ? 133.680 160.334 138.978 1.00 42.18 -1 398 ASP A OD2   1 
ATOM   3225  N  N     . GLU A 1 399 ? 134.173 160.616 135.290 1.00 48.02 ?  399 GLU A N     1 
ATOM   3226  C  CA    . GLU A 1 399 ? 135.495 160.989 134.817 1.00 43.95 ?  399 GLU A CA    1 
ATOM   3227  C  C     . GLU A 1 399 ? 135.495 160.908 133.299 1.00 44.55 ?  399 GLU A C     1 
ATOM   3228  O  O     . GLU A 1 399 ? 134.958 159.958 132.722 1.00 42.49 ?  399 GLU A O     1 
ATOM   3229  C  CB    . GLU A 1 399 ? 136.578 160.073 135.401 1.00 39.19 ?  399 GLU A CB    1 
ATOM   3230  C  CG    . GLU A 1 399 ? 137.907 160.761 135.654 1.00 42.93 ?  399 GLU A CG    1 
ATOM   3231  C  CD    . GLU A 1 399 ? 139.051 159.778 135.815 1.00 48.39 ?  399 GLU A CD    1 
ATOM   3232  O  OE1   . GLU A 1 399 ? 138.825 158.686 136.377 1.00 47.56 ?  399 GLU A OE1   1 
ATOM   3233  O  OE2   . GLU A 1 399 ? 140.177 160.098 135.379 1.00 47.06 -1 399 GLU A OE2   1 
ATOM   3234  N  N     . GLU A 1 400 ? 136.092 161.908 132.656 1.00 44.73 ?  400 GLU A N     1 
ATOM   3235  C  CA    . GLU A 1 400 ? 136.036 161.995 131.204 1.00 40.43 ?  400 GLU A CA    1 
ATOM   3236  C  C     . GLU A 1 400 ? 136.878 160.898 130.565 1.00 43.83 ?  400 GLU A C     1 
ATOM   3237  O  O     . GLU A 1 400 ? 138.048 160.712 130.914 1.00 43.14 ?  400 GLU A O     1 
ATOM   3238  C  CB    . GLU A 1 400 ? 136.513 163.369 130.739 1.00 40.22 ?  400 GLU A CB    1 
ATOM   3239  C  CG    . GLU A 1 400 ? 135.664 163.981 129.636 1.00 45.83 ?  400 GLU A CG    1 
ATOM   3240  C  CD    . GLU A 1 400 ? 134.203 164.116 130.027 1.00 48.85 ?  400 GLU A CD    1 
ATOM   3241  O  OE1   . GLU A 1 400 ? 133.925 164.454 131.196 1.00 46.49 ?  400 GLU A OE1   1 
ATOM   3242  O  OE2   . GLU A 1 400 ? 133.332 163.885 129.162 1.00 47.21 -1 400 GLU A OE2   1 
ATOM   3243  N  N     . ASP A 1 401 ? 136.278 160.174 129.624 1.00 35.69 ?  401 ASP A N     1 
ATOM   3244  C  CA    . ASP A 1 401 ? 136.992 159.149 128.880 1.00 33.74 ?  401 ASP A CA    1 
ATOM   3245  C  C     . ASP A 1 401 ? 137.802 159.775 127.753 1.00 34.42 ?  401 ASP A C     1 
ATOM   3246  O  O     . ASP A 1 401 ? 137.446 160.826 127.213 1.00 38.08 ?  401 ASP A O     1 
ATOM   3247  C  CB    . ASP A 1 401 ? 136.018 158.122 128.303 1.00 32.53 ?  401 ASP A CB    1 
ATOM   3248  C  CG    . ASP A 1 401 ? 135.097 157.533 129.350 1.00 37.68 ?  401 ASP A CG    1 
ATOM   3249  O  OD1   . ASP A 1 401 ? 135.603 156.954 130.333 1.00 42.07 ?  401 ASP A OD1   1 
ATOM   3250  O  OD2   . ASP A 1 401 ? 133.864 157.648 129.188 1.00 38.40 -1 401 ASP A OD2   1 
ATOM   3251  N  N     . GLU A 1 402 ? 138.902 159.117 127.399 1.00 31.60 ?  402 GLU A N     1 
ATOM   3252  C  CA    . GLU A 1 402 ? 139.706 159.504 126.244 1.00 29.37 ?  402 GLU A CA    1 
ATOM   3253  C  C     . GLU A 1 402 ? 139.247 158.615 125.094 1.00 24.85 ?  402 GLU A C     1 
ATOM   3254  O  O     . GLU A 1 402 ? 139.574 157.428 125.041 1.00 30.34 ?  402 GLU A O     1 
ATOM   3255  C  CB    . GLU A 1 402 ? 141.199 159.363 126.536 1.00 31.18 ?  402 GLU A CB    1 
ATOM   3256  C  CG    . GLU A 1 402 ? 142.115 159.430 125.313 1.00 36.78 ?  402 GLU A CG    1 
ATOM   3257  C  CD    . GLU A 1 402 ? 142.410 158.073 124.696 1.00 40.42 ?  402 GLU A CD    1 
ATOM   3258  O  OE1   . GLU A 1 402 ? 143.092 157.255 125.347 1.00 35.31 ?  402 GLU A OE1   1 
ATOM   3259  O  OE2   . GLU A 1 402 ? 141.965 157.828 123.556 1.00 34.93 -1 402 GLU A OE2   1 
ATOM   3260  N  N     . ILE A 1 403 ? 138.457 159.185 124.191 1.00 27.50 ?  403 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 403 ? 137.864 158.416 123.104 1.00 26.57 ?  403 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 403 ? 138.861 158.317 121.958 1.00 28.07 ?  403 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 403 ? 139.363 159.333 121.464 1.00 28.44 ?  403 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 403 ? 136.544 159.054 122.643 1.00 24.55 ?  403 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 403 ? 135.543 159.102 123.798 1.00 24.49 ?  403 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 403 ? 135.964 158.289 121.467 1.00 20.31 ?  403 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 403 ? 135.358 157.780 124.507 1.00 26.84 ?  403 ILE A CD1   1 
ATOM   3268  N  N     . GLY A 1 404 ? 139.153 157.094 121.539 1.00 23.34 ?  404 GLY A N     1 
ATOM   3269  C  CA    . GLY A 1 404 ? 140.050 156.821 120.439 1.00 9.27  ?  404 GLY A CA    1 
ATOM   3270  C  C     . GLY A 1 404 ? 139.312 156.579 119.140 1.00 19.17 ?  404 GLY A C     1 
ATOM   3271  O  O     . GLY A 1 404 ? 138.240 157.145 118.891 1.00 31.31 ?  404 GLY A O     1 
ATOM   3272  N  N     . LEU A 1 405 ? 139.890 155.728 118.298 1.00 22.22 ?  405 LEU A N     1 
ATOM   3273  C  CA    . LEU A 1 405 ? 139.317 155.388 117.002 1.00 7.02  ?  405 LEU A CA    1 
ATOM   3274  C  C     . LEU A 1 405 ? 139.072 153.888 116.949 1.00 8.34  ?  405 LEU A C     1 
ATOM   3275  O  O     . LEU A 1 405 ? 140.010 153.098 117.087 1.00 18.34 ?  405 LEU A O     1 
ATOM   3276  C  CB    . LEU A 1 405 ? 140.242 155.820 115.863 1.00 17.23 ?  405 LEU A CB    1 
ATOM   3277  C  CG    . LEU A 1 405 ? 140.567 157.312 115.770 1.00 18.22 ?  405 LEU A CG    1 
ATOM   3278  C  CD1   . LEU A 1 405 ? 141.617 157.567 114.702 1.00 21.75 ?  405 LEU A CD1   1 
ATOM   3279  C  CD2   . LEU A 1 405 ? 139.312 158.121 115.498 1.00 15.48 ?  405 LEU A CD2   1 
ATOM   3280  N  N     . ASP A 1 406 ? 137.816 153.502 116.746 1.00 22.38 ?  406 ASP A N     1 
ATOM   3281  C  CA    . ASP A 1 406 ? 137.434 152.110 116.557 1.00 17.43 ?  406 ASP A CA    1 
ATOM   3282  C  C     . ASP A 1 406 ? 136.884 151.938 115.149 1.00 19.13 ?  406 ASP A C     1 
ATOM   3283  O  O     . ASP A 1 406 ? 135.986 152.676 114.734 1.00 31.28 ?  406 ASP A O     1 
ATOM   3284  C  CB    . ASP A 1 406 ? 136.399 151.675 117.595 1.00 18.37 ?  406 ASP A CB    1 
ATOM   3285  C  CG    . ASP A 1 406 ? 137.030 151.228 118.899 1.00 29.15 ?  406 ASP A CG    1 
ATOM   3286  O  OD1   . ASP A 1 406 ? 138.269 151.321 119.029 1.00 32.47 ?  406 ASP A OD1   1 
ATOM   3287  O  OD2   . ASP A 1 406 ? 136.286 150.788 119.799 1.00 28.37 -1 406 ASP A OD2   1 
ATOM   3288  N  N     . ILE A 1 407 ? 137.411 150.958 114.432 1.00 21.24 ?  407 ILE A N     1 
ATOM   3289  C  CA    . ILE A 1 407 ? 137.155 150.828 113.004 1.00 15.66 ?  407 ILE A CA    1 
ATOM   3290  C  C     . ILE A 1 407 ? 135.737 150.332 112.764 1.00 14.81 ?  407 ILE A C     1 
ATOM   3291  O  O     . ILE A 1 407 ? 135.255 149.412 113.435 1.00 21.70 ?  407 ILE A O     1 
ATOM   3292  C  CB    . ILE A 1 407 ? 138.187 149.885 112.363 1.00 10.60 ?  407 ILE A CB    1 
ATOM   3293  C  CG1   . ILE A 1 407 ? 139.601 150.428 112.556 1.00 6.69  ?  407 ILE A CG1   1 
ATOM   3294  C  CG2   . ILE A 1 407 ? 137.881 149.688 110.900 1.00 16.52 ?  407 ILE A CG2   1 
ATOM   3295  C  CD1   . ILE A 1 407 ? 140.632 149.349 112.731 1.00 10.78 ?  407 ILE A CD1   1 
ATOM   3296  N  N     . SER A 1 408 ? 135.062 150.953 111.798 1.00 25.69 ?  408 SER A N     1 
ATOM   3297  C  CA    . SER A 1 408 ? 133.772 150.473 111.314 1.00 21.75 ?  408 SER A CA    1 
ATOM   3298  C  C     . SER A 1 408 ? 133.638 150.931 109.870 1.00 24.54 ?  408 SER A C     1 
ATOM   3299  O  O     . SER A 1 408 ? 133.259 152.080 109.621 1.00 30.62 ?  408 SER A O     1 
ATOM   3300  C  CB    . SER A 1 408 ? 132.626 151.007 112.168 1.00 26.05 ?  408 SER A CB    1 
ATOM   3301  O  OG    . SER A 1 408 ? 132.559 152.420 112.097 1.00 29.29 ?  408 SER A OG    1 
ATOM   3302  N  N     . CYS A 1 409 ? 133.943 150.048 108.927 1.00 20.52 ?  409 CYS A N     1 
ATOM   3303  C  CA    . CYS A 1 409 ? 133.904 150.409 107.518 1.00 26.32 ?  409 CYS A CA    1 
ATOM   3304  C  C     . CYS A 1 409 ? 132.582 149.984 106.891 1.00 30.59 ?  409 CYS A C     1 
ATOM   3305  O  O     . CYS A 1 409 ? 131.830 149.173 107.437 1.00 25.65 ?  409 CYS A O     1 
ATOM   3306  C  CB    . CYS A 1 409 ? 135.079 149.791 106.755 1.00 23.24 ?  409 CYS A CB    1 
ATOM   3307  S  SG    . CYS A 1 409 ? 134.770 148.181 106.018 1.00 41.88 ?  409 CYS A SG    1 
ATOM   3308  N  N     . ASN A 1 410 ? 132.315 150.552 105.723 1.00 30.01 ?  410 ASN A N     1 
ATOM   3309  C  CA    . ASN A 1 410 ? 131.031 150.444 105.047 1.00 18.67 ?  410 ASN A CA    1 
ATOM   3310  C  C     . ASN A 1 410 ? 131.183 149.519 103.847 1.00 21.72 ?  410 ASN A C     1 
ATOM   3311  O  O     . ASN A 1 410 ? 131.980 149.799 102.948 1.00 29.59 ?  410 ASN A O     1 
ATOM   3312  C  CB    . ASN A 1 410 ? 130.562 151.829 104.612 1.00 26.98 ?  410 ASN A CB    1 
ATOM   3313  C  CG    . ASN A 1 410 ? 129.102 151.871 104.277 1.00 32.40 ?  410 ASN A CG    1 
ATOM   3314  O  OD1   . ASN A 1 410 ? 128.375 150.894 104.452 1.00 35.72 ?  410 ASN A OD1   1 
ATOM   3315  N  ND2   . ASN A 1 410 ? 128.659 153.011 103.783 1.00 34.49 ?  410 ASN A ND2   1 
ATOM   3316  N  N     . LEU A 1 411 ? 130.412 148.435 103.827 1.00 21.50 ?  411 LEU A N     1 
ATOM   3317  C  CA    . LEU A 1 411 ? 130.594 147.382 102.838 1.00 11.76 ?  411 LEU A CA    1 
ATOM   3318  C  C     . LEU A 1 411 ? 129.700 147.587 101.619 1.00 16.12 ?  411 LEU A C     1 
ATOM   3319  O  O     . LEU A 1 411 ? 128.586 148.106 101.715 1.00 26.82 ?  411 LEU A O     1 
ATOM   3320  C  CB    . LEU A 1 411 ? 130.307 146.011 103.452 1.00 19.14 ?  411 LEU A CB    1 
ATOM   3321  C  CG    . LEU A 1 411 ? 131.485 145.123 103.856 1.00 20.45 ?  411 LEU A CG    1 
ATOM   3322  C  CD1   . LEU A 1 411 ? 132.543 145.927 104.579 1.00 19.01 ?  411 LEU A CD1   1 
ATOM   3323  C  CD2   . LEU A 1 411 ? 131.005 143.965 104.715 1.00 18.70 ?  411 LEU A CD2   1 
ATOM   3324  N  N     . GLY A 1 412 ? 130.210 147.159 100.466 1.00 22.65 ?  412 GLY A N     1 
ATOM   3325  C  CA    . GLY A 1 412 ? 129.492 147.186 99.206  1.00 13.61 ?  412 GLY A CA    1 
ATOM   3326  C  C     . GLY A 1 412 ? 130.336 146.541 98.125  1.00 13.30 ?  412 GLY A C     1 
ATOM   3327  O  O     . GLY A 1 412 ? 131.546 146.779 98.076  1.00 23.34 ?  412 GLY A O     1 
ATOM   3328  N  N     . SER A 1 413 ? 129.736 145.730 97.255  1.00 14.80 ?  413 SER A N     1 
ATOM   3329  C  CA    . SER A 1 413 ? 130.499 144.892 96.338  1.00 10.91 ?  413 SER A CA    1 
ATOM   3330  C  C     . SER A 1 413 ? 130.126 145.179 94.892  1.00 17.65 ?  413 SER A C     1 
ATOM   3331  O  O     . SER A 1 413 ? 128.943 145.237 94.548  1.00 21.51 ?  413 SER A O     1 
ATOM   3332  C  CB    . SER A 1 413 ? 130.279 143.411 96.645  1.00 9.74  ?  413 SER A CB    1 
ATOM   3333  O  OG    . SER A 1 413 ? 130.793 143.083 97.922  1.00 32.49 ?  413 SER A OG    1 
ATOM   3334  N  N     . LEU A 1 414 ? 131.140 145.342 94.048  1.00 18.32 ?  414 LEU A N     1 
ATOM   3335  C  CA    . LEU A 1 414 ? 130.927 145.394 92.611  1.00 12.54 ?  414 LEU A CA    1 
ATOM   3336  C  C     . LEU A 1 414 ? 130.762 143.984 92.061  1.00 19.08 ?  414 LEU A C     1 
ATOM   3337  O  O     . LEU A 1 414 ? 131.464 143.057 92.470  1.00 24.42 ?  414 LEU A O     1 
ATOM   3338  C  CB    . LEU A 1 414 ? 132.103 146.083 91.919  1.00 17.56 ?  414 LEU A CB    1 
ATOM   3339  C  CG    . LEU A 1 414 ? 132.603 147.392 92.526  1.00 20.23 ?  414 LEU A CG    1 
ATOM   3340  C  CD1   . LEU A 1 414 ? 133.950 147.762 91.935  1.00 22.49 ?  414 LEU A CD1   1 
ATOM   3341  C  CD2   . LEU A 1 414 ? 131.594 148.502 92.301  1.00 20.11 ?  414 LEU A CD2   1 
ATOM   3342  N  N     . ASN A 1 415 ? 129.825 143.823 91.133  1.00 25.67 ?  415 ASN A N     1 
ATOM   3343  C  CA    . ASN A 1 415 ? 129.669 142.567 90.404  1.00 24.25 ?  415 ASN A CA    1 
ATOM   3344  C  C     . ASN A 1 415 ? 130.544 142.663 89.163  1.00 22.60 ?  415 ASN A C     1 
ATOM   3345  O  O     . ASN A 1 415 ? 130.197 143.344 88.196  1.00 27.33 ?  415 ASN A O     1 
ATOM   3346  C  CB    . ASN A 1 415 ? 128.206 142.317 90.060  1.00 20.70 ?  415 ASN A CB    1 
ATOM   3347  C  CG    . ASN A 1 415 ? 127.934 140.879 89.663  1.00 25.69 ?  415 ASN A CG    1 
ATOM   3348  O  OD1   . ASN A 1 415 ? 128.601 140.324 88.792  1.00 33.28 ?  415 ASN A OD1   1 
ATOM   3349  N  ND2   . ASN A 1 415 ? 126.949 140.266 90.308  1.00 29.90 ?  415 ASN A ND2   1 
ATOM   3350  N  N     . ILE A 1 416 ? 131.688 141.974 89.192  1.00 21.84 ?  416 ILE A N     1 
ATOM   3351  C  CA    . ILE A 1 416 ? 132.702 142.147 88.155  1.00 24.00 ?  416 ILE A CA    1 
ATOM   3352  C  C     . ILE A 1 416 ? 132.148 141.780 86.787  1.00 26.98 ?  416 ILE A C     1 
ATOM   3353  O  O     . ILE A 1 416 ? 132.412 142.463 85.791  1.00 29.35 ?  416 ILE A O     1 
ATOM   3354  C  CB    . ILE A 1 416 ? 133.961 141.328 88.497  1.00 20.69 ?  416 ILE A CB    1 
ATOM   3355  C  CG1   . ILE A 1 416 ? 134.600 141.849 89.783  1.00 18.38 ?  416 ILE A CG1   1 
ATOM   3356  C  CG2   . ILE A 1 416 ? 134.956 141.367 87.352  1.00 14.34 ?  416 ILE A CG2   1 
ATOM   3357  C  CD1   . ILE A 1 416 ? 135.696 140.966 90.318  1.00 19.31 ?  416 ILE A CD1   1 
ATOM   3358  N  N     . LEU A 1 417 ? 131.365 140.702 86.714  1.00 20.94 ?  417 LEU A N     1 
ATOM   3359  C  CA    . LEU A 1 417 ? 130.781 140.303 85.439  1.00 22.96 ?  417 LEU A CA    1 
ATOM   3360  C  C     . LEU A 1 417 ? 129.849 141.382 84.903  1.00 23.58 ?  417 LEU A C     1 
ATOM   3361  O  O     . LEU A 1 417 ? 129.987 141.828 83.757  1.00 34.84 ?  417 LEU A O     1 
ATOM   3362  C  CB    . LEU A 1 417 ? 130.046 138.972 85.598  1.00 25.83 ?  417 LEU A CB    1 
ATOM   3363  C  CG    . LEU A 1 417 ? 129.332 138.409 84.368  1.00 28.56 ?  417 LEU A CG    1 
ATOM   3364  C  CD1   . LEU A 1 417 ? 129.747 136.970 84.136  1.00 25.37 ?  417 LEU A CD1   1 
ATOM   3365  C  CD2   . LEU A 1 417 ? 127.826 138.506 84.531  1.00 28.76 ?  417 LEU A CD2   1 
ATOM   3366  N  N     . ASN A 1 418 ? 128.903 141.832 85.732  1.00 25.55 ?  418 ASN A N     1 
ATOM   3367  C  CA    . ASN A 1 418 ? 127.940 142.835 85.290  1.00 25.79 ?  418 ASN A CA    1 
ATOM   3368  C  C     . ASN A 1 418 ? 128.608 144.182 85.045  1.00 27.32 ?  418 ASN A C     1 
ATOM   3369  O  O     . ASN A 1 418 ? 128.239 144.901 84.110  1.00 29.87 ?  418 ASN A O     1 
ATOM   3370  C  CB    . ASN A 1 418 ? 126.815 142.966 86.316  1.00 25.54 ?  418 ASN A CB    1 
ATOM   3371  C  CG    . ASN A 1 418 ? 125.970 141.712 86.413  1.00 29.11 ?  418 ASN A CG    1 
ATOM   3372  O  OD1   . ASN A 1 418 ? 125.699 141.059 85.408  1.00 29.68 ?  418 ASN A OD1   1 
ATOM   3373  N  ND2   . ASN A 1 418 ? 125.552 141.368 87.624  1.00 29.21 ?  418 ASN A ND2   1 
ATOM   3374  N  N     . VAL A 1 419 ? 129.587 144.543 85.878  1.00 31.03 ?  419 VAL A N     1 
ATOM   3375  C  CA    . VAL A 1 419 ? 130.290 145.810 85.693  1.00 28.81 ?  419 VAL A CA    1 
ATOM   3376  C  C     . VAL A 1 419 ? 131.065 145.807 84.383  1.00 29.87 ?  419 VAL A C     1 
ATOM   3377  O  O     . VAL A 1 419 ? 131.037 146.785 83.627  1.00 32.16 ?  419 VAL A O     1 
ATOM   3378  C  CB    . VAL A 1 419 ? 131.209 146.093 86.897  1.00 26.42 ?  419 VAL A CB    1 
ATOM   3379  C  CG1   . VAL A 1 419 ? 132.216 147.169 86.557  1.00 27.47 ?  419 VAL A CG1   1 
ATOM   3380  C  CG2   . VAL A 1 419 ? 130.387 146.525 88.091  1.00 28.81 ?  419 VAL A CG2   1 
ATOM   3381  N  N     . MET A 1 420 ? 131.764 144.710 84.084  1.00 32.84 ?  420 MET A N     1 
ATOM   3382  C  CA    . MET A 1 420 ? 132.618 144.706 82.904  1.00 33.42 ?  420 MET A CA    1 
ATOM   3383  C  C     . MET A 1 420 ? 131.829 144.489 81.619  1.00 30.71 ?  420 MET A C     1 
ATOM   3384  O  O     . MET A 1 420 ? 132.232 144.994 80.566  1.00 35.76 ?  420 MET A O     1 
ATOM   3385  C  CB    . MET A 1 420 ? 133.715 143.651 83.042  1.00 31.20 ?  420 MET A CB    1 
ATOM   3386  C  CG    . MET A 1 420 ? 134.951 144.183 83.757  1.00 26.08 ?  420 MET A CG    1 
ATOM   3387  S  SD    . MET A 1 420 ? 136.268 144.781 82.682  1.00 47.11 ?  420 MET A SD    1 
ATOM   3388  C  CE    . MET A 1 420 ? 136.426 143.447 81.509  1.00 33.81 ?  420 MET A CE    1 
ATOM   3389  N  N     . GLU A 1 421 ? 130.716 143.751 81.668  1.00 32.30 ?  421 GLU A N     1 
ATOM   3390  C  CA    . GLU A 1 421 ? 129.910 143.601 80.461  1.00 37.53 ?  421 GLU A CA    1 
ATOM   3391  C  C     . GLU A 1 421 ? 129.186 144.890 80.099  1.00 37.35 ?  421 GLU A C     1 
ATOM   3392  O  O     . GLU A 1 421 ? 128.839 145.085 78.930  1.00 40.20 ?  421 GLU A O     1 
ATOM   3393  C  CB    . GLU A 1 421 ? 128.896 142.465 80.616  1.00 34.43 ?  421 GLU A CB    1 
ATOM   3394  C  CG    . GLU A 1 421 ? 127.845 142.695 81.683  1.00 39.15 ?  421 GLU A CG    1 
ATOM   3395  C  CD    . GLU A 1 421 ? 126.768 141.629 81.674  1.00 43.34 ?  421 GLU A CD    1 
ATOM   3396  O  OE1   . GLU A 1 421 ? 126.650 140.912 80.658  1.00 44.06 ?  421 GLU A OE1   1 
ATOM   3397  O  OE2   . GLU A 1 421 ? 126.039 141.507 82.680  1.00 40.29 -1 421 GLU A OE2   1 
ATOM   3398  N  N     . HIS A 1 422 ? 128.957 145.769 81.070  1.00 35.77 ?  422 HIS A N     1 
ATOM   3399  C  CA    . HIS A 1 422 ? 128.384 147.085 80.824  1.00 35.28 ?  422 HIS A CA    1 
ATOM   3400  C  C     . HIS A 1 422 ? 129.443 148.140 80.539  1.00 39.14 ?  422 HIS A C     1 
ATOM   3401  O  O     . HIS A 1 422 ? 129.087 149.283 80.237  1.00 39.84 ?  422 HIS A O     1 
ATOM   3402  C  CB    . HIS A 1 422 ? 127.537 147.526 82.022  1.00 32.46 ?  422 HIS A CB    1 
ATOM   3403  C  CG    . HIS A 1 422 ? 126.211 146.838 82.110  1.00 36.58 ?  422 HIS A CG    1 
ATOM   3404  N  ND1   . HIS A 1 422 ? 126.016 145.691 82.849  1.00 36.83 ?  422 HIS A ND1   1 
ATOM   3405  C  CD2   . HIS A 1 422 ? 125.013 147.134 81.554  1.00 36.85 ?  422 HIS A CD2   1 
ATOM   3406  C  CE1   . HIS A 1 422 ? 124.756 145.310 82.745  1.00 38.65 ?  422 HIS A CE1   1 
ATOM   3407  N  NE2   . HIS A 1 422 ? 124.126 146.168 81.964  1.00 39.61 ?  422 HIS A NE2   1 
ATOM   3408  N  N     . LYS A 1 423 ? 130.724 147.779 80.625  1.00 40.10 ?  423 LYS A N     1 
ATOM   3409  C  CA    . LYS A 1 423 ? 131.835 148.700 80.382  1.00 39.49 ?  423 LYS A CA    1 
ATOM   3410  C  C     . LYS A 1 423 ? 131.705 149.955 81.241  1.00 42.48 ?  423 LYS A C     1 
ATOM   3411  O  O     . LYS A 1 423 ? 131.895 151.083 80.780  1.00 42.19 ?  423 LYS A O     1 
ATOM   3412  C  CB    . LYS A 1 423 ? 131.935 149.054 78.898  1.00 37.95 ?  423 LYS A CB    1 
ATOM   3413  C  CG    . LYS A 1 423 ? 132.241 147.868 78.000  1.00 38.37 ?  423 LYS A CG    1 
ATOM   3414  C  CD    . LYS A 1 423 ? 132.116 148.238 76.532  1.00 40.56 ?  423 LYS A CD    1 
ATOM   3415  C  CE    . LYS A 1 423 ? 132.169 147.007 75.647  1.00 40.10 ?  423 LYS A CE    1 
ATOM   3416  N  NZ    . LYS A 1 423 ? 133.294 146.106 76.022  1.00 43.35 1  423 LYS A NZ    1 
ATOM   3417  N  N     . SER A 1 424 ? 131.379 149.748 82.514  1.00 32.26 ?  424 SER A N     1 
ATOM   3418  C  CA    . SER A 1 424 ? 131.051 150.830 83.434  1.00 29.82 ?  424 SER A CA    1 
ATOM   3419  C  C     . SER A 1 424 ? 131.806 150.675 84.747  1.00 32.67 ?  424 SER A C     1 
ATOM   3420  O  O     . SER A 1 424 ? 131.229 150.750 85.832  1.00 32.96 ?  424 SER A O     1 
ATOM   3421  C  CB    . SER A 1 424 ? 129.547 150.879 83.687  1.00 34.00 ?  424 SER A CB    1 
ATOM   3422  O  OG    . SER A 1 424 ? 129.134 149.788 84.489  1.00 31.39 ?  424 SER A OG    1 
ATOM   3423  N  N     . ILE A 1 425 ? 133.118 150.447 84.669  1.00 31.72 ?  425 ILE A N     1 
ATOM   3424  C  CA    . ILE A 1 425 ? 133.922 150.387 85.887  1.00 23.87 ?  425 ILE A CA    1 
ATOM   3425  C  C     . ILE A 1 425 ? 133.913 151.737 86.595  1.00 29.13 ?  425 ILE A C     1 
ATOM   3426  O  O     . ILE A 1 425 ? 133.668 151.819 87.804  1.00 37.02 ?  425 ILE A O     1 
ATOM   3427  C  CB    . ILE A 1 425 ? 135.357 149.929 85.570  1.00 26.96 ?  425 ILE A CB    1 
ATOM   3428  C  CG1   . ILE A 1 425 ? 135.391 148.434 85.253  1.00 31.42 ?  425 ILE A CG1   1 
ATOM   3429  C  CG2   . ILE A 1 425 ? 136.286 150.235 86.734  1.00 27.22 ?  425 ILE A CG2   1 
ATOM   3430  C  CD1   . ILE A 1 425 ? 136.751 147.941 84.812  1.00 29.41 ?  425 ILE A CD1   1 
ATOM   3431  N  N     . GLU A 1 426 ? 134.155 152.815 85.846  1.00 25.95 ?  426 GLU A N     1 
ATOM   3432  C  CA    . GLU A 1 426 ? 134.250 154.141 86.452  1.00 26.36 ?  426 GLU A CA    1 
ATOM   3433  C  C     . GLU A 1 426 ? 132.933 154.559 87.092  1.00 27.33 ?  426 GLU A C     1 
ATOM   3434  O  O     . GLU A 1 426 ? 132.895 154.953 88.264  1.00 32.66 ?  426 GLU A O     1 
ATOM   3435  C  CB    . GLU A 1 426 ? 134.680 155.162 85.400  1.00 26.18 ?  426 GLU A CB    1 
ATOM   3436  C  CG    . GLU A 1 426 ? 134.394 156.602 85.783  1.00 28.32 ?  426 GLU A CG    1 
ATOM   3437  C  CD    . GLU A 1 426 ? 134.859 157.585 84.729  1.00 36.93 ?  426 GLU A CD    1 
ATOM   3438  O  OE1   . GLU A 1 426 ? 135.300 157.137 83.650  1.00 34.16 ?  426 GLU A OE1   1 
ATOM   3439  O  OE2   . GLU A 1 426 ? 134.783 158.806 84.979  1.00 37.58 -1 426 GLU A OE2   1 
ATOM   3440  N  N     . LYS A 1 427 ? 131.839 154.487 86.329  1.00 27.52 ?  427 LYS A N     1 
ATOM   3441  C  CA    . LYS A 1 427 ? 130.550 154.942 86.837  1.00 24.47 ?  427 LYS A CA    1 
ATOM   3442  C  C     . LYS A 1 427 ? 130.098 154.106 88.026  1.00 26.33 ?  427 LYS A C     1 
ATOM   3443  O  O     . LYS A 1 427 ? 129.622 154.648 89.030  1.00 31.77 ?  427 LYS A O     1 
ATOM   3444  C  CB    . LYS A 1 427 ? 129.508 154.908 85.719  1.00 31.26 ?  427 LYS A CB    1 
ATOM   3445  C  CG    . LYS A 1 427 ? 128.066 154.921 86.200  1.00 28.72 ?  427 LYS A CG    1 
ATOM   3446  C  CD    . LYS A 1 427 ? 127.171 154.107 85.279  1.00 32.81 ?  427 LYS A CD    1 
ATOM   3447  C  CE    . LYS A 1 427 ? 127.125 152.649 85.698  1.00 32.53 ?  427 LYS A CE    1 
ATOM   3448  N  NZ    . LYS A 1 427 ? 126.138 151.867 84.902  1.00 29.00 1  427 LYS A NZ    1 
ATOM   3449  N  N     . THR A 1 428 ? 130.249 152.783 87.935  1.00 26.39 ?  428 THR A N     1 
ATOM   3450  C  CA    . THR A 1 428 ? 129.841 151.922 89.038  1.00 21.30 ?  428 THR A CA    1 
ATOM   3451  C  C     . THR A 1 428 ? 130.677 152.183 90.282  1.00 23.90 ?  428 THR A C     1 
ATOM   3452  O  O     . THR A 1 428 ? 130.136 152.263 91.389  1.00 31.41 ?  428 THR A O     1 
ATOM   3453  C  CB    . THR A 1 428 ? 129.937 150.453 88.635  1.00 25.35 ?  428 THR A CB    1 
ATOM   3454  O  OG1   . THR A 1 428 ? 129.269 150.256 87.384  1.00 29.04 ?  428 THR A OG1   1 
ATOM   3455  C  CG2   . THR A 1 428 ? 129.292 149.572 89.690  1.00 24.41 ?  428 THR A CG2   1 
ATOM   3456  N  N     . VAL A 1 429 ? 131.995 152.326 90.123  1.00 24.51 ?  429 VAL A N     1 
ATOM   3457  C  CA    . VAL A 1 429 ? 132.853 152.567 91.278  1.00 24.24 ?  429 VAL A CA    1 
ATOM   3458  C  C     . VAL A 1 429 ? 132.504 153.895 91.934  1.00 23.22 ?  429 VAL A C     1 
ATOM   3459  O  O     . VAL A 1 429 ? 132.401 153.987 93.162  1.00 26.22 ?  429 VAL A O     1 
ATOM   3460  C  CB    . VAL A 1 429 ? 134.338 152.505 90.870  1.00 21.22 ?  429 VAL A CB    1 
ATOM   3461  C  CG1   . VAL A 1 429 ? 135.205 153.164 91.927  1.00 18.94 ?  429 VAL A CG1   1 
ATOM   3462  C  CG2   . VAL A 1 429 ? 134.769 151.067 90.662  1.00 23.02 ?  429 VAL A CG2   1 
ATOM   3463  N  N     . LYS A 1 430 ? 132.299 154.942 91.130  1.00 22.34 ?  430 LYS A N     1 
ATOM   3464  C  CA    . LYS A 1 430 ? 131.998 156.251 91.704  1.00 20.97 ?  430 LYS A CA    1 
ATOM   3465  C  C     . LYS A 1 430 ? 130.634 156.268 92.383  1.00 23.22 ?  430 LYS A C     1 
ATOM   3466  O  O     . LYS A 1 430 ? 130.485 156.839 93.470  1.00 30.05 ?  430 LYS A O     1 
ATOM   3467  C  CB    . LYS A 1 430 ? 132.088 157.328 90.624  1.00 19.83 ?  430 LYS A CB    1 
ATOM   3468  C  CG    . LYS A 1 430 ? 133.488 157.497 90.061  1.00 23.31 ?  430 LYS A CG    1 
ATOM   3469  C  CD    . LYS A 1 430 ? 133.677 158.854 89.417  1.00 27.87 ?  430 LYS A CD    1 
ATOM   3470  C  CE    . LYS A 1 430 ? 135.137 159.099 89.086  1.00 28.43 ?  430 LYS A CE    1 
ATOM   3471  N  NZ    . LYS A 1 430 ? 135.361 160.467 88.547  1.00 30.72 1  430 LYS A NZ    1 
ATOM   3472  N  N     . LEU A 1 431 ? 129.625 155.642 91.772  1.00 26.98 ?  431 LEU A N     1 
ATOM   3473  C  CA    . LEU A 1 431 ? 128.306 155.605 92.394  1.00 22.52 ?  431 LEU A CA    1 
ATOM   3474  C  C     . LEU A 1 431 ? 128.317 154.768 93.667  1.00 21.71 ?  431 LEU A C     1 
ATOM   3475  O  O     . LEU A 1 431 ? 127.667 155.125 94.657  1.00 28.12 ?  431 LEU A O     1 
ATOM   3476  C  CB    . LEU A 1 431 ? 127.273 155.074 91.402  1.00 27.33 ?  431 LEU A CB    1 
ATOM   3477  C  CG    . LEU A 1 431 ? 126.540 156.122 90.564  1.00 30.18 ?  431 LEU A CG    1 
ATOM   3478  C  CD1   . LEU A 1 431 ? 125.820 155.466 89.398  1.00 26.87 ?  431 LEU A CD1   1 
ATOM   3479  C  CD2   . LEU A 1 431 ? 125.564 156.906 91.424  1.00 28.35 ?  431 LEU A CD2   1 
ATOM   3480  N  N     . ALA A 1 432 ? 129.049 153.652 93.663  1.00 20.35 ?  432 ALA A N     1 
ATOM   3481  C  CA    . ALA A 1 432 ? 129.175 152.842 94.867  1.00 19.22 ?  432 ALA A CA    1 
ATOM   3482  C  C     . ALA A 1 432 ? 129.898 153.606 95.967  1.00 24.76 ?  432 ALA A C     1 
ATOM   3483  O  O     . ALA A 1 432 ? 129.532 153.509 97.142  1.00 26.67 ?  432 ALA A O     1 
ATOM   3484  C  CB    . ALA A 1 432 ? 129.907 151.541 94.547  1.00 26.31 ?  432 ALA A CB    1 
ATOM   3485  N  N     . THR A 1 433 ? 130.929 154.371 95.602  1.00 22.76 ?  433 THR A N     1 
ATOM   3486  C  CA    . THR A 1 433 ? 131.623 155.201 96.579  1.00 17.94 ?  433 THR A CA    1 
ATOM   3487  C  C     . THR A 1 433 ? 130.690 156.251 97.167  1.00 22.72 ?  433 THR A C     1 
ATOM   3488  O  O     . THR A 1 433 ? 130.712 156.501 98.376  1.00 27.81 ?  433 THR A O     1 
ATOM   3489  C  CB    . THR A 1 433 ? 132.837 155.868 95.930  1.00 20.26 ?  433 THR A CB    1 
ATOM   3490  O  OG1   . THR A 1 433 ? 133.652 154.871 95.301  1.00 25.56 ?  433 THR A OG1   1 
ATOM   3491  C  CG2   . THR A 1 433 ? 133.663 156.609 96.969  1.00 24.42 ?  433 THR A CG2   1 
ATOM   3492  N  N     . ASP A 1 434 ? 129.864 156.875 96.325  1.00 20.19 ?  434 ASP A N     1 
ATOM   3493  C  CA    . ASP A 1 434 ? 128.909 157.861 96.823  1.00 15.86 ?  434 ASP A CA    1 
ATOM   3494  C  C     . ASP A 1 434 ? 127.893 157.226 97.768  1.00 19.40 ?  434 ASP A C     1 
ATOM   3495  O  O     . ASP A 1 434 ? 127.565 157.797 98.814  1.00 25.70 ?  434 ASP A O     1 
ATOM   3496  C  CB    . ASP A 1 434 ? 128.201 158.540 95.651  1.00 23.42 ?  434 ASP A CB    1 
ATOM   3497  C  CG    . ASP A 1 434 ? 129.136 159.388 94.819  1.00 31.37 ?  434 ASP A CG    1 
ATOM   3498  O  OD1   . ASP A 1 434 ? 130.143 159.879 95.370  1.00 29.06 ?  434 ASP A OD1   1 
ATOM   3499  O  OD2   . ASP A 1 434 ? 128.866 159.563 93.613  1.00 30.81 -1 434 ASP A OD2   1 
ATOM   3500  N  N     . SER A 1 435 ? 127.382 156.044 97.414  1.00 20.41 ?  435 SER A N     1 
ATOM   3501  C  CA    . SER A 1 435 ? 126.426 155.361 98.282  1.00 17.04 ?  435 SER A CA    1 
ATOM   3502  C  C     . SER A 1 435 ? 127.064 154.961 99.607  1.00 25.13 ?  435 SER A C     1 
ATOM   3503  O  O     . SER A 1 435 ? 126.441 155.089 100.669 1.00 34.54 ?  435 SER A O     1 
ATOM   3504  C  CB    . SER A 1 435 ? 125.858 154.134 97.570  1.00 19.28 ?  435 SER A CB    1 
ATOM   3505  O  OG    . SER A 1 435 ? 126.825 153.106 97.475  1.00 23.37 ?  435 SER A OG    1 
ATOM   3506  N  N     . LEU A 1 436 ? 128.303 154.466 99.563  1.00 18.68 ?  436 LEU A N     1 
ATOM   3507  C  CA    . LEU A 1 436 ? 129.000 154.097 100.788 1.00 13.11 ?  436 LEU A CA    1 
ATOM   3508  C  C     . LEU A 1 436 ? 129.272 155.318 101.655 1.00 15.45 ?  436 LEU A C     1 
ATOM   3509  O  O     . LEU A 1 436 ? 129.162 155.251 102.883 1.00 27.01 ?  436 LEU A O     1 
ATOM   3510  C  CB    . LEU A 1 436 ? 130.300 153.370 100.450 1.00 20.26 ?  436 LEU A CB    1 
ATOM   3511  C  CG    . LEU A 1 436 ? 130.133 151.968 99.866  1.00 17.84 ?  436 LEU A CG    1 
ATOM   3512  C  CD1   . LEU A 1 436 ? 131.470 151.398 99.428  1.00 17.53 ?  436 LEU A CD1   1 
ATOM   3513  C  CD2   . LEU A 1 436 ? 129.462 151.058 100.873 1.00 18.63 ?  436 LEU A CD2   1 
ATOM   3514  N  N     . THR A 1 437 ? 129.627 156.444 101.031 1.00 19.99 ?  437 THR A N     1 
ATOM   3515  C  CA    . THR A 1 437 ? 129.803 157.685 101.775 1.00 20.52 ?  437 THR A CA    1 
ATOM   3516  C  C     . THR A 1 437 ? 128.503 158.116 102.437 1.00 23.63 ?  437 THR A C     1 
ATOM   3517  O  O     . THR A 1 437 ? 128.499 158.540 103.597 1.00 25.90 ?  437 THR A O     1 
ATOM   3518  C  CB    . THR A 1 437 ? 130.317 158.782 100.843 1.00 18.17 ?  437 THR A CB    1 
ATOM   3519  O  OG1   . THR A 1 437 ? 131.519 158.341 100.203 1.00 17.98 ?  437 THR A OG1   1 
ATOM   3520  C  CG2   . THR A 1 437 ? 130.600 160.053 101.620 1.00 22.56 ?  437 THR A CG2   1 
ATOM   3521  N  N     . HIS A 1 438 ? 127.384 158.010 101.715 1.00 22.47 ?  438 HIS A N     1 
ATOM   3522  C  CA    . HIS A 1 438 ? 126.097 158.377 102.294 1.00 23.06 ?  438 HIS A CA    1 
ATOM   3523  C  C     . HIS A 1 438 ? 125.751 157.490 103.483 1.00 22.61 ?  438 HIS A C     1 
ATOM   3524  O  O     . HIS A 1 438 ? 125.293 157.983 104.521 1.00 26.43 ?  438 HIS A O     1 
ATOM   3525  C  CB    . HIS A 1 438 ? 124.999 158.296 101.236 1.00 26.74 ?  438 HIS A CB    1 
ATOM   3526  C  CG    . HIS A 1 438 ? 123.617 158.408 101.798 1.00 27.35 ?  438 HIS A CG    1 
ATOM   3527  N  ND1   . HIS A 1 438 ? 123.035 159.619 102.107 1.00 25.41 ?  438 HIS A ND1   1 
ATOM   3528  C  CD2   . HIS A 1 438 ? 122.706 157.461 102.118 1.00 23.58 ?  438 HIS A CD2   1 
ATOM   3529  C  CE1   . HIS A 1 438 ? 121.823 159.411 102.588 1.00 30.51 ?  438 HIS A CE1   1 
ATOM   3530  N  NE2   . HIS A 1 438 ? 121.598 158.111 102.605 1.00 29.10 ?  438 HIS A NE2   1 
ATOM   3531  N  N     . VAL A 1 439 ? 125.966 156.180 103.353 1.00 24.67 ?  439 VAL A N     1 
ATOM   3532  C  CA    . VAL A 1 439 ? 125.637 155.277 104.453 1.00 20.20 ?  439 VAL A CA    1 
ATOM   3533  C  C     . VAL A 1 439 ? 126.558 155.516 105.644 1.00 27.85 ?  439 VAL A C     1 
ATOM   3534  O  O     . VAL A 1 439 ? 126.119 155.448 106.799 1.00 36.63 ?  439 VAL A O     1 
ATOM   3535  C  CB    . VAL A 1 439 ? 125.682 153.815 103.975 1.00 20.52 ?  439 VAL A CB    1 
ATOM   3536  C  CG1   . VAL A 1 439 ? 125.685 152.857 105.156 1.00 21.99 ?  439 VAL A CG1   1 
ATOM   3537  C  CG2   . VAL A 1 439 ? 124.514 153.526 103.063 1.00 30.53 ?  439 VAL A CG2   1 
ATOM   3538  N  N     . SER A 1 440 ? 127.837 155.810 105.395 1.00 21.50 ?  440 SER A N     1 
ATOM   3539  C  CA    . SER A 1 440 ? 128.749 156.132 106.487 1.00 20.63 ?  440 SER A CA    1 
ATOM   3540  C  C     . SER A 1 440 ? 128.343 157.425 107.184 1.00 24.45 ?  440 SER A C     1 
ATOM   3541  O  O     . SER A 1 440 ? 128.446 157.533 108.412 1.00 26.57 ?  440 SER A O     1 
ATOM   3542  C  CB    . SER A 1 440 ? 130.181 156.228 105.960 1.00 25.67 ?  440 SER A CB    1 
ATOM   3543  O  OG    . SER A 1 440 ? 131.089 156.548 106.998 1.00 24.86 ?  440 SER A OG    1 
ATOM   3544  N  N     . GLU A 1 441 ? 127.886 158.418 106.418 1.00 26.21 ?  441 GLU A N     1 
ATOM   3545  C  CA    . GLU A 1 441 ? 127.474 159.685 107.012 1.00 23.41 ?  441 GLU A CA    1 
ATOM   3546  C  C     . GLU A 1 441 ? 126.168 159.550 107.783 1.00 30.31 ?  441 GLU A C     1 
ATOM   3547  O  O     . GLU A 1 441 ? 125.958 160.266 108.768 1.00 38.74 ?  441 GLU A O     1 
ATOM   3548  C  CB    . GLU A 1 441 ? 127.335 160.754 105.928 1.00 25.90 ?  441 GLU A CB    1 
ATOM   3549  C  CG    . GLU A 1 441 ? 128.653 161.264 105.380 1.00 29.16 ?  441 GLU A CG    1 
ATOM   3550  C  CD    . GLU A 1 441 ? 128.519 161.811 103.973 1.00 36.38 ?  441 GLU A CD    1 
ATOM   3551  O  OE1   . GLU A 1 441 ? 127.501 161.515 103.313 1.00 34.67 ?  441 GLU A OE1   1 
ATOM   3552  O  OE2   . GLU A 1 441 ? 129.431 162.539 103.526 1.00 36.67 -1 441 GLU A OE2   1 
ATOM   3553  N  N     . THR A 1 442 ? 125.283 158.653 107.356 1.00 30.88 ?  442 THR A N     1 
ATOM   3554  C  CA    . THR A 1 442 ? 124.003 158.462 108.024 1.00 29.96 ?  442 THR A CA    1 
ATOM   3555  C  C     . THR A 1 442 ? 124.075 157.468 109.174 1.00 30.74 ?  442 THR A C     1 
ATOM   3556  O  O     . THR A 1 442 ? 123.048 157.199 109.806 1.00 38.69 ?  442 THR A O     1 
ATOM   3557  C  CB    . THR A 1 442 ? 122.940 158.004 107.021 1.00 29.97 ?  442 THR A CB    1 
ATOM   3558  O  OG1   . THR A 1 442 ? 123.412 156.852 106.312 1.00 33.39 ?  442 THR A OG1   1 
ATOM   3559  C  CG2   . THR A 1 442 ? 122.627 159.113 106.031 1.00 29.67 ?  442 THR A CG2   1 
ATOM   3560  N  N     . THR A 1 443 ? 125.251 156.919 109.461 1.00 29.39 ?  443 THR A N     1 
ATOM   3561  C  CA    . THR A 1 443 ? 125.422 156.001 110.578 1.00 32.14 ?  443 THR A CA    1 
ATOM   3562  C  C     . THR A 1 443 ? 125.764 156.789 111.836 1.00 37.04 ?  443 THR A C     1 
ATOM   3563  O  O     . THR A 1 443 ? 126.718 157.574 111.844 1.00 39.75 ?  443 THR A O     1 
ATOM   3564  C  CB    . THR A 1 443 ? 126.517 154.978 110.281 1.00 32.36 ?  443 THR A CB    1 
ATOM   3565  O  OG1   . THR A 1 443 ? 126.105 154.136 109.196 1.00 36.65 ?  443 THR A OG1   1 
ATOM   3566  C  CG2   . THR A 1 443 ? 126.791 154.120 111.504 1.00 26.65 ?  443 THR A CG2   1 
ATOM   3567  N  N     . ASP A 1 444 ? 124.982 156.579 112.892 1.00 43.45 ?  444 ASP A N     1 
ATOM   3568  C  CA    . ASP A 1 444 ? 125.182 157.268 114.167 1.00 42.13 ?  444 ASP A CA    1 
ATOM   3569  C  C     . ASP A 1 444 ? 124.921 156.261 115.282 1.00 41.49 ?  444 ASP A C     1 
ATOM   3570  O  O     . ASP A 1 444 ? 123.766 155.939 115.578 1.00 42.15 ?  444 ASP A O     1 
ATOM   3571  C  CB    . ASP A 1 444 ? 124.272 158.484 114.288 1.00 43.52 ?  444 ASP A CB    1 
ATOM   3572  C  CG    . ASP A 1 444 ? 125.014 159.723 114.743 1.00 47.76 ?  444 ASP A CG    1 
ATOM   3573  O  OD1   . ASP A 1 444 ? 126.261 159.686 114.794 1.00 46.38 ?  444 ASP A OD1   1 
ATOM   3574  O  OD2   . ASP A 1 444 ? 124.350 160.737 115.047 1.00 47.26 -1 444 ASP A OD2   1 
ATOM   3575  N  N     . ILE A 1 445 ? 125.992 155.772 115.898 1.00 34.72 ?  445 ILE A N     1 
ATOM   3576  C  CA    . ILE A 1 445 ? 125.908 154.782 116.963 1.00 37.80 ?  445 ILE A CA    1 
ATOM   3577  C  C     . ILE A 1 445 ? 126.155 155.488 118.288 1.00 38.51 ?  445 ILE A C     1 
ATOM   3578  O  O     . ILE A 1 445 ? 127.240 156.035 118.519 1.00 39.84 ?  445 ILE A O     1 
ATOM   3579  C  CB    . ILE A 1 445 ? 126.909 153.637 116.744 1.00 36.80 ?  445 ILE A CB    1 
ATOM   3580  C  CG1   . ILE A 1 445 ? 126.565 152.886 115.458 1.00 34.86 ?  445 ILE A CG1   1 
ATOM   3581  C  CG2   . ILE A 1 445 ? 126.904 152.692 117.932 1.00 37.90 ?  445 ILE A CG2   1 
ATOM   3582  C  CD1   . ILE A 1 445 ? 127.623 151.913 115.019 1.00 34.17 ?  445 ILE A CD1   1 
ATOM   3583  N  N     . ARG A 1 446 ? 125.150 155.474 119.159 1.00 40.85 ?  446 ARG A N     1 
ATOM   3584  C  CA    . ARG A 1 446 ? 125.171 156.241 120.396 1.00 46.28 ?  446 ARG A CA    1 
ATOM   3585  C  C     . ARG A 1 446 ? 125.702 155.449 121.585 1.00 44.95 ?  446 ARG A C     1 
ATOM   3586  O  O     . ARG A 1 446 ? 125.748 155.988 122.695 1.00 41.08 ?  446 ARG A O     1 
ATOM   3587  C  CB    . ARG A 1 446 ? 123.764 156.761 120.713 1.00 44.76 ?  446 ARG A CB    1 
ATOM   3588  C  CG    . ARG A 1 446 ? 122.851 156.869 119.500 1.00 43.05 ?  446 ARG A CG    1 
ATOM   3589  C  CD    . ARG A 1 446 ? 123.282 157.989 118.560 1.00 45.48 ?  446 ARG A CD    1 
ATOM   3590  N  NE    . ARG A 1 446 ? 122.838 159.300 119.019 1.00 47.02 ?  446 ARG A NE    1 
ATOM   3591  C  CZ    . ARG A 1 446 ? 121.595 159.751 118.906 1.00 47.76 ?  446 ARG A CZ    1 
ATOM   3592  N  NH1   . ARG A 1 446 ? 120.640 159.017 118.360 1.00 43.40 1  446 ARG A NH1   1 
ATOM   3593  N  NH2   . ARG A 1 446 ? 121.305 160.970 119.352 1.00 47.17 ?  446 ARG A NH2   1 
ATOM   3594  N  N     . ASN A 1 447 ? 126.103 154.195 121.384 1.00 34.40 ?  447 ASN A N     1 
ATOM   3595  C  CA    . ASN A 1 447 ? 126.636 153.371 122.458 1.00 29.03 ?  447 ASN A CA    1 
ATOM   3596  C  C     . ASN A 1 447 ? 128.064 152.913 122.204 1.00 32.18 ?  447 ASN A C     1 
ATOM   3597  O  O     . ASN A 1 447 ? 128.635 152.215 123.049 1.00 35.53 ?  447 ASN A O     1 
ATOM   3598  C  CB    . ASN A 1 447 ? 125.737 152.150 122.686 1.00 32.55 ?  447 ASN A CB    1 
ATOM   3599  C  CG    . ASN A 1 447 ? 124.633 152.419 123.684 1.00 29.77 ?  447 ASN A CG    1 
ATOM   3600  O  OD1   . ASN A 1 447 ? 124.804 153.200 124.618 1.00 28.36 ?  447 ASN A OD1   1 
ATOM   3601  N  ND2   . ASN A 1 447 ? 123.487 151.781 123.484 1.00 32.26 ?  447 ASN A ND2   1 
ATOM   3602  N  N     . ALA A 1 448 ? 128.653 153.281 121.066 1.00 34.16 ?  448 ALA A N     1 
ATOM   3603  C  CA    . ALA A 1 448 ? 130.047 152.986 120.745 1.00 29.31 ?  448 ALA A CA    1 
ATOM   3604  C  C     . ALA A 1 448 ? 130.734 154.312 120.449 1.00 29.15 ?  448 ALA A C     1 
ATOM   3605  O  O     . ALA A 1 448 ? 130.709 154.792 119.304 1.00 29.10 ?  448 ALA A O     1 
ATOM   3606  C  CB    . ALA A 1 448 ? 130.155 152.022 119.568 1.00 24.41 ?  448 ALA A CB    1 
ATOM   3607  N  N     . PRO A 1 449 ? 131.351 154.945 121.450 1.00 28.77 ?  449 PRO A N     1 
ATOM   3608  C  CA    . PRO A 1 449 ? 131.902 156.291 121.222 1.00 22.93 ?  449 PRO A CA    1 
ATOM   3609  C  C     . PRO A 1 449 ? 133.062 156.307 120.247 1.00 27.34 ?  449 PRO A C     1 
ATOM   3610  O  O     . PRO A 1 449 ? 133.125 157.190 119.381 1.00 22.25 ?  449 PRO A O     1 
ATOM   3611  C  CB    . PRO A 1 449 ? 132.336 156.740 122.627 1.00 19.14 ?  449 PRO A CB    1 
ATOM   3612  C  CG    . PRO A 1 449 ? 131.795 155.714 123.577 1.00 25.18 ?  449 PRO A CG    1 
ATOM   3613  C  CD    . PRO A 1 449 ? 131.621 154.456 122.809 1.00 23.69 ?  449 PRO A CD    1 
ATOM   3614  N  N     . ALA A 1 450 ? 133.986 155.350 120.357 1.00 25.81 ?  450 ALA A N     1 
ATOM   3615  C  CA    . ALA A 1 450 ? 135.130 155.327 119.455 1.00 16.45 ?  450 ALA A CA    1 
ATOM   3616  C  C     . ALA A 1 450 ? 134.722 154.933 118.041 1.00 22.90 ?  450 ALA A C     1 
ATOM   3617  O  O     . ALA A 1 450 ? 135.283 155.456 117.073 1.00 26.91 ?  450 ALA A O     1 
ATOM   3618  C  CB    . ALA A 1 450 ? 136.203 154.381 119.990 1.00 19.28 ?  450 ALA A CB    1 
ATOM   3619  N  N     . VAL A 1 451 ? 133.743 154.037 117.901 1.00 28.04 ?  451 VAL A N     1 
ATOM   3620  C  CA    . VAL A 1 451 ? 133.240 153.685 116.575 1.00 18.02 ?  451 VAL A CA    1 
ATOM   3621  C  C     . VAL A 1 451 ? 132.633 154.908 115.900 1.00 21.83 ?  451 VAL A C     1 
ATOM   3622  O  O     . VAL A 1 451 ? 132.899 155.191 114.728 1.00 30.56 ?  451 VAL A O     1 
ATOM   3623  C  CB    . VAL A 1 451 ? 132.223 152.533 116.674 1.00 21.98 ?  451 VAL A CB    1 
ATOM   3624  C  CG1   . VAL A 1 451 ? 131.395 152.439 115.402 1.00 23.76 ?  451 VAL A CG1   1 
ATOM   3625  C  CG2   . VAL A 1 451 ? 132.929 151.218 116.948 1.00 22.51 ?  451 VAL A CG2   1 
ATOM   3626  N  N     . ARG A 1 452 ? 131.810 155.657 116.639 1.00 20.50 ?  452 ARG A N     1 
ATOM   3627  C  CA    . ARG A 1 452 ? 131.193 156.856 116.083 1.00 22.77 ?  452 ARG A CA    1 
ATOM   3628  C  C     . ARG A 1 452 ? 132.238 157.912 115.740 1.00 23.83 ?  452 ARG A C     1 
ATOM   3629  O  O     . ARG A 1 452 ? 132.167 158.549 114.680 1.00 33.52 ?  452 ARG A O     1 
ATOM   3630  C  CB    . ARG A 1 452 ? 130.169 157.413 117.071 1.00 21.08 ?  452 ARG A CB    1 
ATOM   3631  C  CG    . ARG A 1 452 ? 129.646 158.793 116.729 1.00 26.53 ?  452 ARG A CG    1 
ATOM   3632  C  CD    . ARG A 1 452 ? 128.574 159.223 117.713 1.00 27.26 ?  452 ARG A CD    1 
ATOM   3633  N  NE    . ARG A 1 452 ? 128.975 158.963 119.091 1.00 38.94 ?  452 ARG A NE    1 
ATOM   3634  C  CZ    . ARG A 1 452 ? 128.221 159.217 120.152 1.00 41.10 ?  452 ARG A CZ    1 
ATOM   3635  N  NH1   . ARG A 1 452 ? 127.011 159.737 120.032 1.00 34.44 1  452 ARG A NH1   1 
ATOM   3636  N  NH2   . ARG A 1 452 ? 128.695 158.941 121.364 1.00 29.62 ?  452 ARG A NH2   1 
ATOM   3637  N  N     . ARG A 1 453 ? 133.221 158.107 116.623 1.00 21.78 ?  453 ARG A N     1 
ATOM   3638  C  CA    . ARG A 1 453 ? 134.257 159.102 116.367 1.00 20.91 ?  453 ARG A CA    1 
ATOM   3639  C  C     . ARG A 1 453 ? 135.080 158.737 115.140 1.00 25.75 ?  453 ARG A C     1 
ATOM   3640  O  O     . ARG A 1 453 ? 135.383 159.599 114.308 1.00 29.91 ?  453 ARG A O     1 
ATOM   3641  C  CB    . ARG A 1 453 ? 135.155 159.252 117.597 1.00 20.33 ?  453 ARG A CB    1 
ATOM   3642  C  CG    . ARG A 1 453 ? 136.490 159.918 117.310 1.00 23.78 ?  453 ARG A CG    1 
ATOM   3643  C  CD    . ARG A 1 453 ? 137.098 160.523 118.563 1.00 21.86 ?  453 ARG A CD    1 
ATOM   3644  N  NE    . ARG A 1 453 ? 138.438 160.009 118.818 1.00 21.77 ?  453 ARG A NE    1 
ATOM   3645  C  CZ    . ARG A 1 453 ? 139.544 160.508 118.284 1.00 23.79 ?  453 ARG A CZ    1 
ATOM   3646  N  NH1   . ARG A 1 453 ? 139.509 161.537 117.455 1.00 24.12 1  453 ARG A NH1   1 
ATOM   3647  N  NH2   . ARG A 1 453 ? 140.716 159.956 118.586 1.00 25.71 ?  453 ARG A NH2   1 
ATOM   3648  N  N     . ALA A 1 454 ? 135.438 157.458 114.998 1.00 23.64 ?  454 ALA A N     1 
ATOM   3649  C  CA    . ALA A 1 454 ? 136.214 157.033 113.841 1.00 18.39 ?  454 ALA A CA    1 
ATOM   3650  C  C     . ALA A 1 454 ? 135.387 157.065 112.564 1.00 18.15 ?  454 ALA A C     1 
ATOM   3651  O  O     . ALA A 1 454 ? 135.932 157.319 111.487 1.00 23.75 ?  454 ALA A O     1 
ATOM   3652  C  CB    . ALA A 1 454 ? 136.783 155.636 114.072 1.00 20.65 ?  454 ALA A CB    1 
ATOM   3653  N  N     . ASN A 1 455 ? 134.081 156.810 112.653 1.00 20.68 ?  455 ASN A N     1 
ATOM   3654  C  CA    . ASN A 1 455 ? 133.232 156.946 111.476 1.00 21.99 ?  455 ASN A CA    1 
ATOM   3655  C  C     . ASN A 1 455 ? 133.152 158.399 111.028 1.00 25.45 ?  455 ASN A C     1 
ATOM   3656  O  O     . ASN A 1 455 ? 133.191 158.689 109.827 1.00 30.27 ?  455 ASN A O     1 
ATOM   3657  C  CB    . ASN A 1 455 ? 131.838 156.391 111.763 1.00 19.31 ?  455 ASN A CB    1 
ATOM   3658  C  CG    . ASN A 1 455 ? 130.926 156.456 110.556 1.00 27.04 ?  455 ASN A CG    1 
ATOM   3659  O  OD1   . ASN A 1 455 ? 131.238 155.908 109.499 1.00 31.25 ?  455 ASN A OD1   1 
ATOM   3660  N  ND2   . ASN A 1 455 ? 129.792 157.129 110.705 1.00 26.78 ?  455 ASN A ND2   1 
ATOM   3661  N  N     . LYS A 1 456 ? 133.038 159.327 111.982 1.00 24.12 ?  456 LYS A N     1 
ATOM   3662  C  CA    . LYS A 1 456 ? 132.993 160.743 111.629 1.00 25.23 ?  456 LYS A CA    1 
ATOM   3663  C  C     . LYS A 1 456 ? 134.330 161.228 111.080 1.00 23.97 ?  456 LYS A C     1 
ATOM   3664  O  O     . LYS A 1 456 ? 134.367 162.027 110.138 1.00 29.54 ?  456 LYS A O     1 
ATOM   3665  C  CB    . LYS A 1 456 ? 132.582 161.574 112.843 1.00 27.55 ?  456 LYS A CB    1 
ATOM   3666  C  CG    . LYS A 1 456 ? 131.130 162.028 112.827 1.00 30.26 ?  456 LYS A CG    1 
ATOM   3667  C  CD    . LYS A 1 456 ? 130.484 161.925 114.205 1.00 33.55 ?  456 LYS A CD    1 
ATOM   3668  C  CE    . LYS A 1 456 ? 131.496 162.131 115.324 1.00 33.77 ?  456 LYS A CE    1 
ATOM   3669  N  NZ    . LYS A 1 456 ? 130.896 161.930 116.671 1.00 31.84 1  456 LYS A NZ    1 
ATOM   3670  N  N     . ALA A 1 457 ? 135.438 160.758 111.656 1.00 19.17 ?  457 ALA A N     1 
ATOM   3671  C  CA    . ALA A 1 457 ? 136.752 161.283 111.301 1.00 17.96 ?  457 ALA A CA    1 
ATOM   3672  C  C     . ALA A 1 457 ? 137.321 160.605 110.059 1.00 24.71 ?  457 ALA A C     1 
ATOM   3673  O  O     . ALA A 1 457 ? 137.617 161.264 109.057 1.00 29.05 ?  457 ALA A O     1 
ATOM   3674  C  CB    . ALA A 1 457 ? 137.710 161.118 112.485 1.00 15.33 ?  457 ALA A CB    1 
ATOM   3675  N  N     . MET A 1 458 ? 137.486 159.285 110.116 1.00 23.82 ?  458 MET A N     1 
ATOM   3676  C  CA    . MET A 1 458 ? 138.137 158.545 109.042 1.00 19.43 ?  458 MET A CA    1 
ATOM   3677  C  C     . MET A 1 458 ? 137.292 158.485 107.776 1.00 23.77 ?  458 MET A C     1 
ATOM   3678  O  O     . MET A 1 458 ? 137.848 158.504 106.672 1.00 30.03 ?  458 MET A O     1 
ATOM   3679  C  CB    . MET A 1 458 ? 138.468 157.132 109.519 1.00 22.61 ?  458 MET A CB    1 
ATOM   3680  C  CG    . MET A 1 458 ? 139.358 157.090 110.749 1.00 14.51 ?  458 MET A CG    1 
ATOM   3681  S  SD    . MET A 1 458 ? 141.030 157.666 110.411 1.00 33.37 ?  458 MET A SD    1 
ATOM   3682  C  CE    . MET A 1 458 ? 141.904 156.107 110.298 1.00 22.54 ?  458 MET A CE    1 
ATOM   3683  N  N     . LYS A 1 459 ? 135.967 158.405 107.913 1.00 18.14 ?  459 LYS A N     1 
ATOM   3684  C  CA    . LYS A 1 459 ? 135.063 158.277 106.768 1.00 21.43 ?  459 LYS A CA    1 
ATOM   3685  C  C     . LYS A 1 459 ? 135.455 157.089 105.894 1.00 21.56 ?  459 LYS A C     1 
ATOM   3686  O  O     . LYS A 1 459 ? 135.409 157.149 104.664 1.00 27.81 ?  459 LYS A O     1 
ATOM   3687  C  CB    . LYS A 1 459 ? 135.019 159.565 105.943 1.00 22.37 ?  459 LYS A CB    1 
ATOM   3688  C  CG    . LYS A 1 459 ? 134.621 160.801 106.725 1.00 24.94 ?  459 LYS A CG    1 
ATOM   3689  C  CD    . LYS A 1 459 ? 135.614 161.928 106.506 1.00 25.12 ?  459 LYS A CD    1 
ATOM   3690  C  CE    . LYS A 1 459 ? 134.965 163.282 106.728 1.00 27.52 ?  459 LYS A CE    1 
ATOM   3691  N  NZ    . LYS A 1 459 ? 133.776 163.187 107.620 1.00 30.30 1  459 LYS A NZ    1 
ATOM   3692  N  N     . SER A 1 460 ? 135.849 155.998 106.540 1.00 20.55 ?  460 SER A N     1 
ATOM   3693  C  CA    . SER A 1 460 ? 136.351 154.835 105.825 1.00 11.16 ?  460 SER A CA    1 
ATOM   3694  C  C     . SER A 1 460 ? 135.200 153.985 105.305 1.00 15.54 ?  460 SER A C     1 
ATOM   3695  O  O     . SER A 1 460 ? 134.227 153.724 106.017 1.00 26.00 ?  460 SER A O     1 
ATOM   3696  C  CB    . SER A 1 460 ? 137.251 154.001 106.734 1.00 13.25 ?  460 SER A CB    1 
ATOM   3697  O  OG    . SER A 1 460 ? 136.544 152.903 107.277 1.00 13.78 ?  460 SER A OG    1 
ATOM   3698  N  N     . ILE A 1 461 ? 135.321 153.559 104.050 1.00 17.07 ?  461 ILE A N     1 
ATOM   3699  C  CA    . ILE A 1 461 ? 134.343 152.696 103.409 1.00 11.44 ?  461 ILE A CA    1 
ATOM   3700  C  C     . ILE A 1 461 ? 135.076 151.494 102.832 1.00 18.03 ?  461 ILE A C     1 
ATOM   3701  O  O     . ILE A 1 461 ? 136.281 151.535 102.577 1.00 18.23 ?  461 ILE A O     1 
ATOM   3702  C  CB    . ILE A 1 461 ? 133.555 153.427 102.301 1.00 13.11 ?  461 ILE A CB    1 
ATOM   3703  C  CG1   . ILE A 1 461 ? 134.512 153.946 101.228 1.00 8.92  ?  461 ILE A CG1   1 
ATOM   3704  C  CG2   . ILE A 1 461 ? 132.740 154.568 102.892 1.00 13.75 ?  461 ILE A CG2   1 
ATOM   3705  C  CD1   . ILE A 1 461 ? 133.824 154.462 99.992  1.00 8.18  ?  461 ILE A CD1   1 
ATOM   3706  N  N     . GLY A 1 462 ? 134.339 150.404 102.654 1.00 17.97 ?  462 GLY A N     1 
ATOM   3707  C  CA    . GLY A 1 462 ? 134.892 149.251 101.977 1.00 8.19  ?  462 GLY A CA    1 
ATOM   3708  C  C     . GLY A 1 462 ? 134.137 148.901 100.714 1.00 5.51  ?  462 GLY A C     1 
ATOM   3709  O  O     . GLY A 1 462 ? 133.013 148.399 100.777 1.00 19.62 ?  462 GLY A O     1 
ATOM   3710  N  N     . LEU A 1 463 ? 134.748 149.142 99.561  1.00 11.37 ?  463 LEU A N     1 
ATOM   3711  C  CA    . LEU A 1 463 ? 134.158 148.796 98.274  1.00 9.14  ?  463 LEU A CA    1 
ATOM   3712  C  C     . LEU A 1 463 ? 134.797 147.500 97.795  1.00 11.19 ?  463 LEU A C     1 
ATOM   3713  O  O     . LEU A 1 463 ? 135.977 147.480 97.432  1.00 20.03 ?  463 LEU A O     1 
ATOM   3714  C  CB    . LEU A 1 463 ? 134.353 149.919 97.260  1.00 18.61 ?  463 LEU A CB    1 
ATOM   3715  C  CG    . LEU A 1 463 ? 133.771 149.672 95.866  1.00 18.85 ?  463 LEU A CG    1 
ATOM   3716  C  CD1   . LEU A 1 463 ? 132.327 149.216 95.962  1.00 9.23  ?  463 LEU A CD1   1 
ATOM   3717  C  CD2   . LEU A 1 463 ? 133.886 150.921 95.009  1.00 15.50 ?  463 LEU A CD2   1 
ATOM   3718  N  N     . GLY A 1 464 ? 134.018 146.419 97.798  1.00 12.27 ?  464 GLY A N     1 
ATOM   3719  C  CA    . GLY A 1 464 ? 134.503 145.120 97.397  1.00 8.91  ?  464 GLY A CA    1 
ATOM   3720  C  C     . GLY A 1 464 ? 134.092 144.751 95.980  1.00 14.99 ?  464 GLY A C     1 
ATOM   3721  O  O     . GLY A 1 464 ? 133.460 145.513 95.253  1.00 21.90 ?  464 GLY A O     1 
ATOM   3722  N  N     . ALA A 1 465 ? 134.480 143.541 95.595  1.00 14.56 ?  465 ALA A N     1 
ATOM   3723  C  CA    . ALA A 1 465 ? 134.132 142.990 94.297  1.00 10.65 ?  465 ALA A CA    1 
ATOM   3724  C  C     . ALA A 1 465 ? 133.735 141.533 94.468  1.00 13.06 ?  465 ALA A C     1 
ATOM   3725  O  O     . ALA A 1 465 ? 134.162 140.864 95.413  1.00 22.50 ?  465 ALA A O     1 
ATOM   3726  C  CB    . ALA A 1 465 ? 135.290 143.111 93.300  1.00 16.40 ?  465 ALA A CB    1 
ATOM   3727  N  N     . MET A 1 466 ? 132.906 141.051 93.548  1.00 13.84 ?  466 MET A N     1 
ATOM   3728  C  CA    . MET A 1 466 ? 132.476 139.663 93.554  1.00 20.15 ?  466 MET A CA    1 
ATOM   3729  C  C     . MET A 1 466 ? 132.286 139.210 92.114  1.00 20.70 ?  466 MET A C     1 
ATOM   3730  O  O     . MET A 1 466 ? 132.407 139.998 91.174  1.00 27.41 ?  466 MET A O     1 
ATOM   3731  C  CB    . MET A 1 466 ? 131.189 139.476 94.363  1.00 25.63 ?  466 MET A CB    1 
ATOM   3732  C  CG    . MET A 1 466 ? 129.996 140.196 93.777  1.00 21.84 ?  466 MET A CG    1 
ATOM   3733  S  SD    . MET A 1 466 ? 128.557 140.168 94.853  1.00 34.17 ?  466 MET A SD    1 
ATOM   3734  C  CE    . MET A 1 466 ? 127.529 141.362 94.016  1.00 25.31 ?  466 MET A CE    1 
ATOM   3735  N  N     . ASN A 1 467 ? 131.986 137.920 91.958  1.00 13.45 ?  467 ASN A N     1 
ATOM   3736  C  CA    . ASN A 1 467 ? 131.799 137.292 90.650  1.00 16.31 ?  467 ASN A CA    1 
ATOM   3737  C  C     . ASN A 1 467 ? 133.074 137.331 89.814  1.00 18.38 ?  467 ASN A C     1 
ATOM   3738  O  O     . ASN A 1 467 ? 133.017 137.378 88.584  1.00 23.98 ?  467 ASN A O     1 
ATOM   3739  C  CB    . ASN A 1 467 ? 130.640 137.928 89.876  1.00 20.54 ?  467 ASN A CB    1 
ATOM   3740  C  CG    . ASN A 1 467 ? 129.836 136.912 89.094  1.00 23.54 ?  467 ASN A CG    1 
ATOM   3741  O  OD1   . ASN A 1 467 ? 130.057 135.708 89.209  1.00 31.27 ?  467 ASN A OD1   1 
ATOM   3742  N  ND2   . ASN A 1 467 ? 128.896 137.393 88.292  1.00 23.37 ?  467 ASN A ND2   1 
ATOM   3743  N  N     . LEU A 1 468 ? 134.234 137.320 90.471  1.00 18.69 ?  468 LEU A N     1 
ATOM   3744  C  CA    . LEU A 1 468 ? 135.491 137.250 89.734  1.00 13.32 ?  468 LEU A CA    1 
ATOM   3745  C  C     . LEU A 1 468 ? 135.633 135.907 89.033  1.00 20.58 ?  468 LEU A C     1 
ATOM   3746  O  O     . LEU A 1 468 ? 135.895 135.847 87.826  1.00 21.33 ?  468 LEU A O     1 
ATOM   3747  C  CB    . LEU A 1 468 ? 136.670 137.489 90.676  1.00 22.42 ?  468 LEU A CB    1 
ATOM   3748  C  CG    . LEU A 1 468 ? 138.057 137.247 90.077  1.00 19.10 ?  468 LEU A CG    1 
ATOM   3749  C  CD1   . LEU A 1 468 ? 138.390 138.302 89.035  1.00 16.67 ?  468 LEU A CD1   1 
ATOM   3750  C  CD2   . LEU A 1 468 ? 139.115 137.207 91.163  1.00 14.68 ?  468 LEU A CD2   1 
ATOM   3751  N  N     . HIS A 1 469 ? 135.442 134.814 89.775  1.00 25.22 ?  469 HIS A N     1 
ATOM   3752  C  CA    . HIS A 1 469 ? 135.539 133.492 89.171  1.00 16.21 ?  469 HIS A CA    1 
ATOM   3753  C  C     . HIS A 1 469 ? 134.412 133.259 88.178  1.00 25.21 ?  469 HIS A C     1 
ATOM   3754  O  O     . HIS A 1 469 ? 134.620 132.635 87.135  1.00 33.67 ?  469 HIS A O     1 
ATOM   3755  C  CB    . HIS A 1 469 ? 135.533 132.408 90.246  1.00 17.64 ?  469 HIS A CB    1 
ATOM   3756  C  CG    . HIS A 1 469 ? 135.931 131.059 89.736  1.00 22.56 ?  469 HIS A CG    1 
ATOM   3757  N  ND1   . HIS A 1 469 ? 135.813 129.912 90.488  1.00 27.87 ?  469 HIS A ND1   1 
ATOM   3758  C  CD2   . HIS A 1 469 ? 136.449 130.676 88.544  1.00 23.49 ?  469 HIS A CD2   1 
ATOM   3759  C  CE1   . HIS A 1 469 ? 136.238 128.879 89.782  1.00 23.94 ?  469 HIS A CE1   1 
ATOM   3760  N  NE2   . HIS A 1 469 ? 136.630 129.316 88.599  1.00 28.10 ?  469 HIS A NE2   1 
ATOM   3761  N  N     . GLY A 1 470 ? 133.209 133.745 88.486  1.00 24.88 ?  470 GLY A N     1 
ATOM   3762  C  CA    . GLY A 1 470 ? 132.123 133.643 87.526  1.00 20.72 ?  470 GLY A CA    1 
ATOM   3763  C  C     . GLY A 1 470 ? 132.442 134.352 86.226  1.00 18.09 ?  470 GLY A C     1 
ATOM   3764  O  O     . GLY A 1 470 ? 132.267 133.794 85.141  1.00 35.24 ?  470 GLY A O     1 
ATOM   3765  N  N     . TYR A 1 471 ? 132.944 135.585 86.321  1.00 17.42 ?  471 TYR A N     1 
ATOM   3766  C  CA    . TYR A 1 471 ? 133.291 136.332 85.118  1.00 21.95 ?  471 TYR A CA    1 
ATOM   3767  C  C     . TYR A 1 471 ? 134.392 135.628 84.334  1.00 25.73 ?  471 TYR A C     1 
ATOM   3768  O  O     . TYR A 1 471 ? 134.339 135.548 83.102  1.00 28.80 ?  471 TYR A O     1 
ATOM   3769  C  CB    . TYR A 1 471 ? 133.727 137.753 85.475  1.00 22.09 ?  471 TYR A CB    1 
ATOM   3770  C  CG    . TYR A 1 471 ? 134.257 138.510 84.282  1.00 19.48 ?  471 TYR A CG    1 
ATOM   3771  C  CD1   . TYR A 1 471 ? 133.388 139.091 83.369  1.00 23.38 ?  471 TYR A CD1   1 
ATOM   3772  C  CD2   . TYR A 1 471 ? 135.621 138.616 84.045  1.00 18.44 ?  471 TYR A CD2   1 
ATOM   3773  C  CE1   . TYR A 1 471 ? 133.860 139.773 82.269  1.00 25.73 ?  471 TYR A CE1   1 
ATOM   3774  C  CE2   . TYR A 1 471 ? 136.102 139.293 82.943  1.00 22.96 ?  471 TYR A CE2   1 
ATOM   3775  C  CZ    . TYR A 1 471 ? 135.216 139.870 82.060  1.00 25.21 ?  471 TYR A CZ    1 
ATOM   3776  O  OH    . TYR A 1 471 ? 135.687 140.545 80.961  1.00 31.66 ?  471 TYR A OH    1 
ATOM   3777  N  N     . LEU A 1 472 ? 135.413 135.130 85.034  1.00 27.82 ?  472 LEU A N     1 
ATOM   3778  C  CA    . LEU A 1 472 ? 136.524 134.469 84.353  1.00 24.74 ?  472 LEU A CA    1 
ATOM   3779  C  C     . LEU A 1 472 ? 136.080 133.173 83.686  1.00 27.35 ?  472 LEU A C     1 
ATOM   3780  O  O     . LEU A 1 472 ? 136.517 132.862 82.573  1.00 32.46 ?  472 LEU A O     1 
ATOM   3781  C  CB    . LEU A 1 472 ? 137.663 134.208 85.340  1.00 25.71 ?  472 LEU A CB    1 
ATOM   3782  C  CG    . LEU A 1 472 ? 138.383 135.439 85.893  1.00 24.59 ?  472 LEU A CG    1 
ATOM   3783  C  CD1   . LEU A 1 472 ? 139.247 135.066 87.086  1.00 23.05 ?  472 LEU A CD1   1 
ATOM   3784  C  CD2   . LEU A 1 472 ? 139.216 136.104 84.810  1.00 23.35 ?  472 LEU A CD2   1 
ATOM   3785  N  N     . ALA A 1 473 ? 135.218 132.401 84.351  1.00 26.73 ?  473 ALA A N     1 
ATOM   3786  C  CA    . ALA A 1 473 ? 134.770 131.132 83.792  1.00 24.56 ?  473 ALA A CA    1 
ATOM   3787  C  C     . ALA A 1 473 ? 133.835 131.343 82.607  1.00 35.21 ?  473 ALA A C     1 
ATOM   3788  O  O     . ALA A 1 473 ? 133.918 130.615 81.611  1.00 42.98 ?  473 ALA A O     1 
ATOM   3789  C  CB    . ALA A 1 473 ? 134.091 130.297 84.876  1.00 27.08 ?  473 ALA A CB    1 
ATOM   3790  N  N     . GLN A 1 474 ? 132.941 132.332 82.690  1.00 29.14 ?  474 GLN A N     1 
ATOM   3791  C  CA    . GLN A 1 474 ? 132.068 132.631 81.561  1.00 29.13 ?  474 GLN A CA    1 
ATOM   3792  C  C     . GLN A 1 474 ? 132.804 133.285 80.400  1.00 32.16 ?  474 GLN A C     1 
ATOM   3793  O  O     . GLN A 1 474 ? 132.213 133.447 79.328  1.00 36.34 ?  474 GLN A O     1 
ATOM   3794  C  CB    . GLN A 1 474 ? 130.905 133.522 82.000  1.00 28.84 ?  474 GLN A CB    1 
ATOM   3795  C  CG    . GLN A 1 474 ? 130.115 132.986 83.177  1.00 30.82 ?  474 GLN A CG    1 
ATOM   3796  C  CD    . GLN A 1 474 ? 128.684 133.474 83.184  1.00 32.74 ?  474 GLN A CD    1 
ATOM   3797  O  OE1   . GLN A 1 474 ? 128.042 133.564 82.138  1.00 37.49 ?  474 GLN A OE1   1 
ATOM   3798  N  NE2   . GLN A 1 474 ? 128.174 133.800 84.366  1.00 31.46 ?  474 GLN A NE2   1 
ATOM   3799  N  N     . ASN A 1 475 ? 134.069 133.666 80.584  1.00 33.08 ?  475 ASN A N     1 
ATOM   3800  C  CA    . ASN A 1 475 ? 134.883 134.230 79.516  1.00 35.90 ?  475 ASN A CA    1 
ATOM   3801  C  C     . ASN A 1 475 ? 136.004 133.290 79.090  1.00 35.04 ?  475 ASN A C     1 
ATOM   3802  O  O     . ASN A 1 475 ? 136.945 133.717 78.414  1.00 33.44 ?  475 ASN A O     1 
ATOM   3803  C  CB    . ASN A 1 475 ? 135.452 135.582 79.945  1.00 32.28 ?  475 ASN A CB    1 
ATOM   3804  C  CG    . ASN A 1 475 ? 134.409 136.679 79.933  1.00 31.54 ?  475 ASN A CG    1 
ATOM   3805  O  OD1   . ASN A 1 475 ? 134.209 137.350 78.922  1.00 33.91 ?  475 ASN A OD1   1 
ATOM   3806  N  ND2   . ASN A 1 475 ? 133.727 136.856 81.057  1.00 29.10 ?  475 ASN A ND2   1 
ATOM   3807  N  N     . GLY A 1 476 ? 135.918 132.018 79.469  1.00 29.82 ?  476 GLY A N     1 
ATOM   3808  C  CA    . GLY A 1 476 ? 136.922 131.042 79.076  1.00 29.15 ?  476 GLY A CA    1 
ATOM   3809  C  C     . GLY A 1 476 ? 138.299 131.306 79.645  1.00 35.07 ?  476 GLY A C     1 
ATOM   3810  O  O     . GLY A 1 476 ? 139.299 131.175 78.929  1.00 37.01 ?  476 GLY A O     1 
ATOM   3811  N  N     . ILE A 1 477 ? 138.375 131.677 80.920  1.00 31.50 ?  477 ILE A N     1 
ATOM   3812  C  CA    . ILE A 1 477 ? 139.641 131.956 81.586  1.00 26.83 ?  477 ILE A CA    1 
ATOM   3813  C  C     . ILE A 1 477 ? 139.696 131.159 82.880  1.00 31.18 ?  477 ILE A C     1 
ATOM   3814  O  O     . ILE A 1 477 ? 138.793 131.262 83.718  1.00 34.93 ?  477 ILE A O     1 
ATOM   3815  C  CB    . ILE A 1 477 ? 139.820 133.459 81.871  1.00 27.36 ?  477 ILE A CB    1 
ATOM   3816  C  CG1   . ILE A 1 477 ? 139.857 134.247 80.563  1.00 30.88 ?  477 ILE A CG1   1 
ATOM   3817  C  CG2   . ILE A 1 477 ? 141.087 133.700 82.667  1.00 28.51 ?  477 ILE A CG2   1 
ATOM   3818  C  CD1   . ILE A 1 477 ? 139.621 135.721 80.741  1.00 30.35 ?  477 ILE A CD1   1 
ATOM   3819  N  N     . ALA A 1 478 ? 140.752 130.366 83.042  1.00 31.04 ?  478 ALA A N     1 
ATOM   3820  C  CA    . ALA A 1 478 ? 140.945 129.621 84.276  1.00 27.78 ?  478 ALA A CA    1 
ATOM   3821  C  C     . ALA A 1 478 ? 141.354 130.563 85.401  1.00 30.47 ?  478 ALA A C     1 
ATOM   3822  O  O     . ALA A 1 478 ? 142.130 131.499 85.196  1.00 31.20 ?  478 ALA A O     1 
ATOM   3823  C  CB    . ALA A 1 478 ? 142.005 128.537 84.085  1.00 28.28 ?  478 ALA A CB    1 
ATOM   3824  N  N     . TYR A 1 479 ? 140.824 130.306 86.600  1.00 29.75 ?  479 TYR A N     1 
ATOM   3825  C  CA    . TYR A 1 479 ? 141.111 131.169 87.742  1.00 22.93 ?  479 TYR A CA    1 
ATOM   3826  C  C     . TYR A 1 479 ? 142.596 131.186 88.078  1.00 27.34 ?  479 TYR A C     1 
ATOM   3827  O  O     . TYR A 1 479 ? 143.116 132.209 88.535  1.00 33.22 ?  479 TYR A O     1 
ATOM   3828  C  CB    . TYR A 1 479 ? 140.292 130.714 88.950  1.00 21.32 ?  479 TYR A CB    1 
ATOM   3829  C  CG    . TYR A 1 479 ? 140.379 131.620 90.159  1.00 28.50 ?  479 TYR A CG    1 
ATOM   3830  C  CD1   . TYR A 1 479 ? 141.361 131.433 91.124  1.00 26.50 ?  479 TYR A CD1   1 
ATOM   3831  C  CD2   . TYR A 1 479 ? 139.468 132.650 90.344  1.00 22.04 ?  479 TYR A CD2   1 
ATOM   3832  C  CE1   . TYR A 1 479 ? 141.440 132.252 92.230  1.00 22.41 ?  479 TYR A CE1   1 
ATOM   3833  C  CE2   . TYR A 1 479 ? 139.538 133.474 91.449  1.00 22.90 ?  479 TYR A CE2   1 
ATOM   3834  C  CZ    . TYR A 1 479 ? 140.526 133.271 92.388  1.00 29.54 ?  479 TYR A CZ    1 
ATOM   3835  O  OH    . TYR A 1 479 ? 140.598 134.091 93.491  1.00 31.36 ?  479 TYR A OH    1 
ATOM   3836  N  N     . GLU A 1 480 ? 143.292 130.075 87.861  1.00 30.91 ?  480 GLU A N     1 
ATOM   3837  C  CA    . GLU A 1 480 ? 144.715 129.983 88.155  1.00 29.89 ?  480 GLU A CA    1 
ATOM   3838  C  C     . GLU A 1 480 ? 145.595 130.417 86.993  1.00 32.47 ?  480 GLU A C     1 
ATOM   3839  O  O     . GLU A 1 480 ? 146.822 130.426 87.135  1.00 37.66 ?  480 GLU A O     1 
ATOM   3840  C  CB    . GLU A 1 480 ? 145.077 128.552 88.555  1.00 29.48 ?  480 GLU A CB    1 
ATOM   3841  C  CG    . GLU A 1 480 ? 144.288 128.005 89.725  1.00 30.62 ?  480 GLU A CG    1 
ATOM   3842  C  CD    . GLU A 1 480 ? 144.176 126.497 89.683  1.00 37.66 ?  480 GLU A CD    1 
ATOM   3843  O  OE1   . GLU A 1 480 ? 143.322 125.984 88.931  1.00 38.85 ?  480 GLU A OE1   1 
ATOM   3844  O  OE2   . GLU A 1 480 ? 144.948 125.823 90.397  1.00 38.05 -1 480 GLU A OE2   1 
ATOM   3845  N  N     . SER A 1 481 ? 145.008 130.772 85.855  1.00 30.10 ?  481 SER A N     1 
ATOM   3846  C  CA    . SER A 1 481 ? 145.798 131.138 84.694  1.00 27.49 ?  481 SER A CA    1 
ATOM   3847  C  C     . SER A 1 481 ? 146.440 132.512 84.887  1.00 31.91 ?  481 SER A C     1 
ATOM   3848  O  O     . SER A 1 481 ? 145.909 133.358 85.611  1.00 32.24 ?  481 SER A O     1 
ATOM   3849  C  CB    . SER A 1 481 ? 144.931 131.144 83.440  1.00 29.10 ?  481 SER A CB    1 
ATOM   3850  O  OG    . SER A 1 481 ? 144.289 132.394 83.272  1.00 33.68 ?  481 SER A OG    1 
ATOM   3851  N  N     . PRO A 1 482 ? 147.594 132.752 84.258  1.00 37.78 ?  482 PRO A N     1 
ATOM   3852  C  CA    . PRO A 1 482 ? 148.175 134.104 84.297  1.00 30.91 ?  482 PRO A CA    1 
ATOM   3853  C  C     . PRO A 1 482 ? 147.276 135.157 83.677  1.00 29.86 ?  482 PRO A C     1 
ATOM   3854  O  O     . PRO A 1 482 ? 147.361 136.331 84.056  1.00 34.98 ?  482 PRO A O     1 
ATOM   3855  C  CB    . PRO A 1 482 ? 149.486 133.944 83.514  1.00 30.41 ?  482 PRO A CB    1 
ATOM   3856  C  CG    . PRO A 1 482 ? 149.793 132.486 83.571  1.00 32.89 ?  482 PRO A CG    1 
ATOM   3857  C  CD    . PRO A 1 482 ? 148.468 131.794 83.564  1.00 31.72 ?  482 PRO A CD    1 
ATOM   3858  N  N     . GLU A 1 483 ? 146.420 134.772 82.728  1.00 36.10 ?  483 GLU A N     1 
ATOM   3859  C  CA    . GLU A 1 483 ? 145.473 135.720 82.150  1.00 32.70 ?  483 GLU A CA    1 
ATOM   3860  C  C     . GLU A 1 483 ? 144.464 136.195 83.188  1.00 31.18 ?  483 GLU A C     1 
ATOM   3861  O  O     . GLU A 1 483 ? 144.075 137.368 83.191  1.00 35.55 ?  483 GLU A O     1 
ATOM   3862  C  CB    . GLU A 1 483 ? 144.756 135.086 80.958  1.00 33.67 ?  483 GLU A CB    1 
ATOM   3863  C  CG    . GLU A 1 483 ? 145.617 134.955 79.715  1.00 36.84 ?  483 GLU A CG    1 
ATOM   3864  C  CD    . GLU A 1 483 ? 146.412 133.664 79.687  1.00 39.71 ?  483 GLU A CD    1 
ATOM   3865  O  OE1   . GLU A 1 483 ? 146.497 132.992 80.735  1.00 37.12 ?  483 GLU A OE1   1 
ATOM   3866  O  OE2   . GLU A 1 483 ? 146.954 133.324 78.616  1.00 41.10 -1 483 GLU A OE2   1 
ATOM   3867  N  N     . ALA A 1 484 ? 144.021 135.295 84.068  1.00 26.19 ?  484 ALA A N     1 
ATOM   3868  C  CA    . ALA A 1 484 ? 143.108 135.694 85.134  1.00 25.77 ?  484 ALA A CA    1 
ATOM   3869  C  C     . ALA A 1 484 ? 143.760 136.703 86.070  1.00 25.99 ?  484 ALA A C     1 
ATOM   3870  O  O     . ALA A 1 484 ? 143.128 137.683 86.477  1.00 25.65 ?  484 ALA A O     1 
ATOM   3871  C  CB    . ALA A 1 484 ? 142.641 134.468 85.913  1.00 20.79 ?  484 ALA A CB    1 
ATOM   3872  N  N     . ARG A 1 485 ? 145.027 136.477 86.426  1.00 27.55 ?  485 ARG A N     1 
ATOM   3873  C  CA    . ARG A 1 485 ? 145.731 137.430 87.274  1.00 21.77 ?  485 ARG A CA    1 
ATOM   3874  C  C     . ARG A 1 485 ? 145.961 138.753 86.556  1.00 22.14 ?  485 ARG A C     1 
ATOM   3875  O  O     . ARG A 1 485 ? 145.897 139.813 87.185  1.00 30.74 ?  485 ARG A O     1 
ATOM   3876  C  CB    . ARG A 1 485 ? 147.059 136.840 87.743  1.00 24.49 ?  485 ARG A CB    1 
ATOM   3877  C  CG    . ARG A 1 485 ? 146.906 135.748 88.784  1.00 25.08 ?  485 ARG A CG    1 
ATOM   3878  C  CD    . ARG A 1 485 ? 148.247 135.364 89.376  1.00 26.67 ?  485 ARG A CD    1 
ATOM   3879  N  NE    . ARG A 1 485 ? 149.159 134.832 88.371  1.00 27.79 ?  485 ARG A NE    1 
ATOM   3880  C  CZ    . ARG A 1 485 ? 149.170 133.571 87.966  1.00 29.59 ?  485 ARG A CZ    1 
ATOM   3881  N  NH1   . ARG A 1 485 ? 148.323 132.680 88.453  1.00 27.74 1  485 ARG A NH1   1 
ATOM   3882  N  NH2   . ARG A 1 485 ? 150.056 133.193 87.049  1.00 25.12 ?  485 ARG A NH2   1 
ATOM   3883  N  N     . ASP A 1 486 ? 146.229 138.713 85.251  1.00 29.60 ?  486 ASP A N     1 
ATOM   3884  C  CA    . ASP A 1 486 ? 146.349 139.942 84.473  1.00 28.93 ?  486 ASP A CA    1 
ATOM   3885  C  C     . ASP A 1 486 ? 145.045 140.731 84.491  1.00 29.97 ?  486 ASP A C     1 
ATOM   3886  O  O     . ASP A 1 486 ? 145.043 141.956 84.683  1.00 35.68 ?  486 ASP A O     1 
ATOM   3887  C  CB    . ASP A 1 486 ? 146.759 139.600 83.042  1.00 33.99 ?  486 ASP A CB    1 
ATOM   3888  C  CG    . ASP A 1 486 ? 147.092 140.824 82.222  1.00 39.53 ?  486 ASP A CG    1 
ATOM   3889  O  OD1   . ASP A 1 486 ? 147.980 141.598 82.634  1.00 38.33 ?  486 ASP A OD1   1 
ATOM   3890  O  OD2   . ASP A 1 486 ? 146.464 141.005 81.159  1.00 40.45 -1 486 ASP A OD2   1 
ATOM   3891  N  N     . PHE A 1 487 ? 143.922 140.038 84.296  1.00 27.52 ?  487 PHE A N     1 
ATOM   3892  C  CA    . PHE A 1 487 ? 142.630 140.709 84.352  1.00 24.06 ?  487 PHE A CA    1 
ATOM   3893  C  C     . PHE A 1 487 ? 142.366 141.285 85.733  1.00 23.48 ?  487 PHE A C     1 
ATOM   3894  O  O     . PHE A 1 487 ? 141.858 142.402 85.854  1.00 28.50 ?  487 PHE A O     1 
ATOM   3895  C  CB    . PHE A 1 487 ? 141.497 139.760 83.972  1.00 23.47 ?  487 PHE A CB    1 
ATOM   3896  C  CG    . PHE A 1 487 ? 140.149 140.262 84.394  1.00 24.82 ?  487 PHE A CG    1 
ATOM   3897  C  CD1   . PHE A 1 487 ? 139.516 141.259 83.672  1.00 22.38 ?  487 PHE A CD1   1 
ATOM   3898  C  CD2   . PHE A 1 487 ? 139.530 139.770 85.531  1.00 24.88 ?  487 PHE A CD2   1 
ATOM   3899  C  CE1   . PHE A 1 487 ? 138.288 141.742 84.063  1.00 24.63 ?  487 PHE A CE1   1 
ATOM   3900  C  CE2   . PHE A 1 487 ? 138.301 140.251 85.927  1.00 25.98 ?  487 PHE A CE2   1 
ATOM   3901  C  CZ    . PHE A 1 487 ? 137.679 141.238 85.192  1.00 24.61 ?  487 PHE A CZ    1 
ATOM   3902  N  N     . ALA A 1 488 ? 142.661 140.521 86.785  1.00 20.43 ?  488 ALA A N     1 
ATOM   3903  C  CA    . ALA A 1 488 ? 142.441 141.021 88.136  1.00 16.31 ?  488 ALA A CA    1 
ATOM   3904  C  C     . ALA A 1 488 ? 143.292 142.253 88.400  1.00 23.39 ?  488 ALA A C     1 
ATOM   3905  O  O     . ALA A 1 488 ? 142.806 143.247 88.954  1.00 28.14 ?  488 ALA A O     1 
ATOM   3906  C  CB    . ALA A 1 488 ? 142.741 139.928 89.159  1.00 22.74 ?  488 ALA A CB    1 
ATOM   3907  N  N     . ASN A 1 489 ? 144.558 142.217 87.979  1.00 25.91 ?  489 ASN A N     1 
ATOM   3908  C  CA    . ASN A 1 489 ? 145.437 143.369 88.127  1.00 21.39 ?  489 ASN A CA    1 
ATOM   3909  C  C     . ASN A 1 489 ? 144.842 144.597 87.457  1.00 20.60 ?  489 ASN A C     1 
ATOM   3910  O  O     . ASN A 1 489 ? 144.689 145.649 88.089  1.00 23.98 ?  489 ASN A O     1 
ATOM   3911  C  CB    . ASN A 1 489 ? 146.810 143.047 87.534  1.00 17.63 ?  489 ASN A CB    1 
ATOM   3912  C  CG    . ASN A 1 489 ? 147.841 144.108 87.836  1.00 25.69 ?  489 ASN A CG    1 
ATOM   3913  O  OD1   . ASN A 1 489 ? 147.939 144.593 88.961  1.00 31.29 ?  489 ASN A OD1   1 
ATOM   3914  N  ND2   . ASN A 1 489 ? 148.625 144.470 86.829  1.00 28.39 ?  489 ASN A ND2   1 
ATOM   3915  N  N     . THR A 1 490 ? 144.468 144.473 86.181  1.00 22.74 ?  490 THR A N     1 
ATOM   3916  C  CA    . THR A 1 490 ? 143.952 145.631 85.459  1.00 21.31 ?  490 THR A CA    1 
ATOM   3917  C  C     . THR A 1 490 ? 142.636 146.119 86.057  1.00 22.67 ?  490 THR A C     1 
ATOM   3918  O  O     . THR A 1 490 ? 142.462 147.318 86.307  1.00 24.89 ?  490 THR A O     1 
ATOM   3919  C  CB    . THR A 1 490 ? 143.776 145.299 83.979  1.00 28.93 ?  490 THR A CB    1 
ATOM   3920  O  OG1   . THR A 1 490 ? 144.991 144.739 83.467  1.00 33.78 ?  490 THR A OG1   1 
ATOM   3921  C  CG2   . THR A 1 490 ? 143.432 146.556 83.197  1.00 22.59 ?  490 THR A CG2   1 
ATOM   3922  N  N     . PHE A 1 491 ? 141.702 145.199 86.304  1.00 19.82 ?  491 PHE A N     1 
ATOM   3923  C  CA    . PHE A 1 491 ? 140.377 145.576 86.784  1.00 17.95 ?  491 PHE A CA    1 
ATOM   3924  C  C     . PHE A 1 491 ? 140.460 146.262 88.138  1.00 22.82 ?  491 PHE A C     1 
ATOM   3925  O  O     . PHE A 1 491 ? 139.838 147.306 88.355  1.00 22.93 ?  491 PHE A O     1 
ATOM   3926  C  CB    . PHE A 1 491 ? 139.480 144.338 86.859  1.00 22.92 ?  491 PHE A CB    1 
ATOM   3927  C  CG    . PHE A 1 491 ? 138.140 144.593 87.492  1.00 19.23 ?  491 PHE A CG    1 
ATOM   3928  C  CD1   . PHE A 1 491 ? 137.075 145.034 86.729  1.00 17.23 ?  491 PHE A CD1   1 
ATOM   3929  C  CD2   . PHE A 1 491 ? 137.943 144.383 88.848  1.00 17.98 ?  491 PHE A CD2   1 
ATOM   3930  C  CE1   . PHE A 1 491 ? 135.844 145.273 87.303  1.00 15.75 ?  491 PHE A CE1   1 
ATOM   3931  C  CE2   . PHE A 1 491 ? 136.715 144.621 89.428  1.00 17.31 ?  491 PHE A CE2   1 
ATOM   3932  C  CZ    . PHE A 1 491 ? 135.663 145.066 88.653  1.00 19.56 ?  491 PHE A CZ    1 
ATOM   3933  N  N     . PHE A 1 492 ? 141.238 145.700 89.063  1.00 23.17 ?  492 PHE A N     1 
ATOM   3934  C  CA    . PHE A 1 492 ? 141.321 146.296 90.384  1.00 12.41 ?  492 PHE A CA    1 
ATOM   3935  C  C     . PHE A 1 492 ? 142.203 147.534 90.413  1.00 14.90 ?  492 PHE A C     1 
ATOM   3936  O  O     . PHE A 1 492 ? 141.996 148.394 91.271  1.00 20.08 ?  492 PHE A O     1 
ATOM   3937  C  CB    . PHE A 1 492 ? 141.797 145.252 91.391  1.00 19.66 ?  492 PHE A CB    1 
ATOM   3938  C  CG    . PHE A 1 492 ? 140.733 144.262 91.765  1.00 16.33 ?  492 PHE A CG    1 
ATOM   3939  C  CD1   . PHE A 1 492 ? 139.743 144.605 92.669  1.00 11.74 ?  492 PHE A CD1   1 
ATOM   3940  C  CD2   . PHE A 1 492 ? 140.699 143.004 91.190  1.00 16.15 ?  492 PHE A CD2   1 
ATOM   3941  C  CE1   . PHE A 1 492 ? 138.755 143.705 93.008  1.00 12.40 ?  492 PHE A CE1   1 
ATOM   3942  C  CE2   . PHE A 1 492 ? 139.711 142.099 91.525  1.00 14.11 ?  492 PHE A CE2   1 
ATOM   3943  C  CZ    . PHE A 1 492 ? 138.738 142.451 92.436  1.00 16.69 ?  492 PHE A CZ    1 
ATOM   3944  N  N     . MET A 1 493 ? 143.139 147.685 89.471  1.00 19.05 ?  493 MET A N     1 
ATOM   3945  C  CA    . MET A 1 493 ? 143.830 148.963 89.362  1.00 16.78 ?  493 MET A CA    1 
ATOM   3946  C  C     . MET A 1 493 ? 142.872 150.048 88.894  1.00 16.20 ?  493 MET A C     1 
ATOM   3947  O  O     . MET A 1 493 ? 142.916 151.173 89.398  1.00 22.30 ?  493 MET A O     1 
ATOM   3948  C  CB    . MET A 1 493 ? 145.050 148.823 88.441  1.00 17.19 ?  493 MET A CB    1 
ATOM   3949  C  CG    . MET A 1 493 ? 145.643 150.090 87.773  1.00 17.53 ?  493 MET A CG    1 
ATOM   3950  S  SD    . MET A 1 493 ? 144.652 151.174 86.719  1.00 32.83 ?  493 MET A SD    1 
ATOM   3951  C  CE    . MET A 1 493 ? 144.638 150.222 85.208  1.00 21.93 ?  493 MET A CE    1 
ATOM   3952  N  N     . MET A 1 494 ? 141.995 149.735 87.933  1.00 20.52 ?  494 MET A N     1 
ATOM   3953  C  CA    . MET A 1 494 ? 140.979 150.710 87.538  1.00 19.50 ?  494 MET A CA    1 
ATOM   3954  C  C     . MET A 1 494 ? 140.016 151.005 88.681  1.00 21.79 ?  494 MET A C     1 
ATOM   3955  O  O     . MET A 1 494 ? 139.599 152.155 88.869  1.00 24.82 ?  494 MET A O     1 
ATOM   3956  C  CB    . MET A 1 494 ? 140.205 150.234 86.307  1.00 17.94 ?  494 MET A CB    1 
ATOM   3957  C  CG    . MET A 1 494 ? 141.053 149.685 85.181  1.00 22.98 ?  494 MET A CG    1 
ATOM   3958  S  SD    . MET A 1 494 ? 140.191 149.628 83.599  1.00 39.60 ?  494 MET A SD    1 
ATOM   3959  C  CE    . MET A 1 494 ? 138.937 150.882 83.840  1.00 24.17 ?  494 MET A CE    1 
ATOM   3960  N  N     . VAL A 1 495 ? 139.641 149.978 89.447  1.00 19.25 ?  495 VAL A N     1 
ATOM   3961  C  CA    . VAL A 1 495 ? 138.757 150.190 90.591  1.00 14.86 ?  495 VAL A CA    1 
ATOM   3962  C  C     . VAL A 1 495 ? 139.414 151.120 91.601  1.00 21.00 ?  495 VAL A C     1 
ATOM   3963  O  O     . VAL A 1 495 ? 138.787 152.057 92.105  1.00 32.06 ?  495 VAL A O     1 
ATOM   3964  C  CB    . VAL A 1 495 ? 138.369 148.844 91.231  1.00 19.73 ?  495 VAL A CB    1 
ATOM   3965  C  CG1   . VAL A 1 495 ? 137.700 149.071 92.577  1.00 13.65 ?  495 VAL A CG1   1 
ATOM   3966  C  CG2   . VAL A 1 495 ? 137.447 148.067 90.312  1.00 14.21 ?  495 VAL A CG2   1 
ATOM   3967  N  N     . ASN A 1 496 ? 140.693 150.883 91.902  1.00 18.39 ?  496 ASN A N     1 
ATOM   3968  C  CA    . ASN A 1 496 ? 141.419 151.754 92.819  1.00 11.72 ?  496 ASN A CA    1 
ATOM   3969  C  C     . ASN A 1 496 ? 141.534 153.168 92.264  1.00 16.27 ?  496 ASN A C     1 
ATOM   3970  O  O     . ASN A 1 496 ? 141.374 154.146 93.002  1.00 26.76 ?  496 ASN A O     1 
ATOM   3971  C  CB    . ASN A 1 496 ? 142.805 151.174 93.101  1.00 17.45 ?  496 ASN A CB    1 
ATOM   3972  C  CG    . ASN A 1 496 ? 143.428 151.739 94.359  1.00 18.49 ?  496 ASN A CG    1 
ATOM   3973  O  OD1   . ASN A 1 496 ? 142.727 152.119 95.294  1.00 24.08 ?  496 ASN A OD1   1 
ATOM   3974  N  ND2   . ASN A 1 496 ? 144.751 151.796 94.388  1.00 18.71 ?  496 ASN A ND2   1 
ATOM   3975  N  N     . PHE A 1 497 ? 141.808 153.294 90.964  1.00 18.94 ?  497 PHE A N     1 
ATOM   3976  C  CA    . PHE A 1 497 ? 141.938 154.609 90.347  1.00 14.12 ?  497 PHE A CA    1 
ATOM   3977  C  C     . PHE A 1 497 ? 140.646 155.403 90.479  1.00 19.38 ?  497 PHE A C     1 
ATOM   3978  O  O     . PHE A 1 497 ? 140.655 156.562 90.908  1.00 24.23 ?  497 PHE A O     1 
ATOM   3979  C  CB    . PHE A 1 497 ? 142.329 154.452 88.875  1.00 17.00 ?  497 PHE A CB    1 
ATOM   3980  C  CG    . PHE A 1 497 ? 142.486 155.753 88.139  1.00 20.91 ?  497 PHE A CG    1 
ATOM   3981  C  CD1   . PHE A 1 497 ? 141.406 156.339 87.499  1.00 20.09 ?  497 PHE A CD1   1 
ATOM   3982  C  CD2   . PHE A 1 497 ? 143.717 156.382 88.072  1.00 25.45 ?  497 PHE A CD2   1 
ATOM   3983  C  CE1   . PHE A 1 497 ? 141.549 157.532 86.821  1.00 22.74 ?  497 PHE A CE1   1 
ATOM   3984  C  CE2   . PHE A 1 497 ? 143.865 157.576 87.393  1.00 23.32 ?  497 PHE A CE2   1 
ATOM   3985  C  CZ    . PHE A 1 497 ? 142.780 158.150 86.767  1.00 22.22 ?  497 PHE A CZ    1 
ATOM   3986  N  N     . TYR A 1 498 ? 139.518 154.786 90.130  1.00 25.25 ?  498 TYR A N     1 
ATOM   3987  C  CA    . TYR A 1 498 ? 138.256 155.512 90.169  1.00 18.22 ?  498 TYR A CA    1 
ATOM   3988  C  C     . TYR A 1 498 ? 137.764 155.713 91.596  1.00 23.26 ?  498 TYR A C     1 
ATOM   3989  O  O     . TYR A 1 498 ? 137.097 156.711 91.878  1.00 29.58 ?  498 TYR A O     1 
ATOM   3990  C  CB    . TYR A 1 498 ? 137.214 154.794 89.314  1.00 19.42 ?  498 TYR A CB    1 
ATOM   3991  C  CG    . TYR A 1 498 ? 137.539 154.864 87.842  1.00 22.71 ?  498 TYR A CG    1 
ATOM   3992  C  CD1   . TYR A 1 498 ? 137.731 156.089 87.216  1.00 23.96 ?  498 TYR A CD1   1 
ATOM   3993  C  CD2   . TYR A 1 498 ? 137.678 153.711 87.082  1.00 23.81 ?  498 TYR A CD2   1 
ATOM   3994  C  CE1   . TYR A 1 498 ? 138.039 156.163 85.872  1.00 19.02 ?  498 TYR A CE1   1 
ATOM   3995  C  CE2   . TYR A 1 498 ? 137.987 153.776 85.739  1.00 26.18 ?  498 TYR A CE2   1 
ATOM   3996  C  CZ    . TYR A 1 498 ? 138.165 155.004 85.139  1.00 27.69 ?  498 TYR A CZ    1 
ATOM   3997  O  OH    . TYR A 1 498 ? 138.471 155.073 83.800  1.00 33.10 ?  498 TYR A OH    1 
ATOM   3998  N  N     . SER A 1 499 ? 138.112 154.810 92.515  1.00 21.40 ?  499 SER A N     1 
ATOM   3999  C  CA    . SER A 1 499 ? 137.778 155.020 93.919  1.00 7.93  ?  499 SER A CA    1 
ATOM   4000  C  C     . SER A 1 499 ? 138.546 156.206 94.489  1.00 13.95 ?  499 SER A C     1 
ATOM   4001  O  O     . SER A 1 499 ? 137.977 157.045 95.195  1.00 20.78 ?  499 SER A O     1 
ATOM   4002  C  CB    . SER A 1 499 ? 138.067 153.750 94.718  1.00 10.95 ?  499 SER A CB    1 
ATOM   4003  O  OG    . SER A 1 499 ? 137.349 153.737 95.937  1.00 23.91 ?  499 SER A OG    1 
ATOM   4004  N  N     . ILE A 1 500 ? 139.842 156.298 94.179  1.00 13.96 ?  500 ILE A N     1 
ATOM   4005  C  CA    . ILE A 1 500 ? 140.636 157.440 94.620  1.00 17.91 ?  500 ILE A CA    1 
ATOM   4006  C  C     . ILE A 1 500 ? 140.127 158.721 93.977  1.00 18.43 ?  500 ILE A C     1 
ATOM   4007  O  O     . ILE A 1 500 ? 140.049 159.769 94.627  1.00 27.23 ?  500 ILE A O     1 
ATOM   4008  C  CB    . ILE A 1 500 ? 142.127 157.207 94.312  1.00 20.89 ?  500 ILE A CB    1 
ATOM   4009  C  CG1   . ILE A 1 500 ? 142.683 156.076 95.173  1.00 17.96 ?  500 ILE A CG1   1 
ATOM   4010  C  CG2   . ILE A 1 500 ? 142.927 158.470 94.552  1.00 14.38 ?  500 ILE A CG2   1 
ATOM   4011  C  CD1   . ILE A 1 500 ? 143.969 155.493 94.646  1.00 17.65 ?  500 ILE A CD1   1 
ATOM   4012  N  N     . GLN A 1 501 ? 139.775 158.661 92.691  1.00 21.74 ?  501 GLN A N     1 
ATOM   4013  C  CA    . GLN A 1 501 ? 139.256 159.839 92.009  1.00 21.17 ?  501 GLN A CA    1 
ATOM   4014  C  C     . GLN A 1 501 ? 137.948 160.308 92.632  1.00 23.95 ?  501 GLN A C     1 
ATOM   4015  O  O     . GLN A 1 501 ? 137.752 161.507 92.845  1.00 33.02 ?  501 GLN A O     1 
ATOM   4016  C  CB    . GLN A 1 501 ? 139.070 159.542 90.522  1.00 26.40 ?  501 GLN A CB    1 
ATOM   4017  C  CG    . GLN A 1 501 ? 139.282 160.743 89.619  1.00 26.12 ?  501 GLN A CG    1 
ATOM   4018  C  CD    . GLN A 1 501 ? 139.069 160.415 88.158  1.00 29.50 ?  501 GLN A CD    1 
ATOM   4019  O  OE1   . GLN A 1 501 ? 138.042 159.852 87.780  1.00 30.35 ?  501 GLN A OE1   1 
ATOM   4020  N  NE2   . GLN A 1 501 ? 140.042 160.763 87.325  1.00 31.13 ?  501 GLN A NE2   1 
ATOM   4021  N  N     . ARG A 1 502 ? 137.045 159.375 92.943  1.00 22.64 ?  502 ARG A N     1 
ATOM   4022  C  CA    . ARG A 1 502 ? 135.783 159.747 93.574  1.00 21.00 ?  502 ARG A CA    1 
ATOM   4023  C  C     . ARG A 1 502 ? 136.005 160.289 94.980  1.00 21.54 ?  502 ARG A C     1 
ATOM   4024  O  O     . ARG A 1 502 ? 135.336 161.240 95.392  1.00 25.89 ?  502 ARG A O     1 
ATOM   4025  C  CB    . ARG A 1 502 ? 134.836 158.549 93.603  1.00 19.91 ?  502 ARG A CB    1 
ATOM   4026  C  CG    . ARG A 1 502 ? 133.411 158.910 93.976  1.00 22.74 ?  502 ARG A CG    1 
ATOM   4027  C  CD    . ARG A 1 502 ? 132.875 160.017 93.087  1.00 23.43 ?  502 ARG A CD    1 
ATOM   4028  N  NE    . ARG A 1 502 ? 131.769 160.729 93.714  1.00 26.60 ?  502 ARG A NE    1 
ATOM   4029  C  CZ    . ARG A 1 502 ? 131.529 162.024 93.562  1.00 25.59 ?  502 ARG A CZ    1 
ATOM   4030  N  NH1   . ARG A 1 502 ? 132.294 162.783 92.796  1.00 29.04 1  502 ARG A NH1   1 
ATOM   4031  N  NH2   . ARG A 1 502 ? 130.495 162.570 94.193  1.00 26.36 ?  502 ARG A NH2   1 
ATOM   4032  N  N     . SER A 1 503 ? 136.933 159.694 95.735  1.00 19.21 ?  503 SER A N     1 
ATOM   4033  C  CA    . SER A 1 503 ? 137.233 160.202 97.070  1.00 20.41 ?  503 SER A CA    1 
ATOM   4034  C  C     . SER A 1 503 ? 137.778 161.622 97.005  1.00 23.19 ?  503 SER A C     1 
ATOM   4035  O  O     . SER A 1 503 ? 137.377 162.489 97.790  1.00 26.02 ?  503 SER A O     1 
ATOM   4036  C  CB    . SER A 1 503 ? 138.226 159.274 97.769  1.00 19.03 ?  503 SER A CB    1 
ATOM   4037  O  OG    . SER A 1 503 ? 138.217 159.474 99.171  1.00 23.30 ?  503 SER A OG    1 
ATOM   4038  N  N     . ALA A 1 504 ? 138.680 161.885 96.057  1.00 24.12 ?  504 ALA A N     1 
ATOM   4039  C  CA    . ALA A 1 504 ? 139.227 163.227 95.901  1.00 21.09 ?  504 ALA A CA    1 
ATOM   4040  C  C     . ALA A 1 504 ? 138.163 164.208 95.423  1.00 28.52 ?  504 ALA A C     1 
ATOM   4041  O  O     . ALA A 1 504 ? 138.148 165.369 95.845  1.00 37.22 ?  504 ALA A O     1 
ATOM   4042  C  CB    . ALA A 1 504 ? 140.409 163.201 94.934  1.00 24.49 ?  504 ALA A CB    1 
ATOM   4043  N  N     . GLU A 1 505 ? 137.260 163.760 94.549  1.00 26.33 ?  505 GLU A N     1 
ATOM   4044  C  CA    . GLU A 1 505 ? 136.178 164.623 94.091  1.00 26.93 ?  505 GLU A CA    1 
ATOM   4045  C  C     . GLU A 1 505 ? 135.228 164.971 95.229  1.00 29.67 ?  505 GLU A C     1 
ATOM   4046  O  O     . GLU A 1 505 ? 134.777 166.115 95.338  1.00 35.60 ?  505 GLU A O     1 
ATOM   4047  C  CB    . GLU A 1 505 ? 135.421 163.950 92.946  1.00 26.49 ?  505 GLU A CB    1 
ATOM   4048  C  CG    . GLU A 1 505 ? 136.150 163.976 91.614  1.00 27.33 ?  505 GLU A CG    1 
ATOM   4049  C  CD    . GLU A 1 505 ? 135.733 162.840 90.700  1.00 33.62 ?  505 GLU A CD    1 
ATOM   4050  O  OE1   . GLU A 1 505 ? 134.857 162.046 91.098  1.00 34.56 ?  505 GLU A OE1   1 
ATOM   4051  O  OE2   . GLU A 1 505 ? 136.284 162.741 89.583  1.00 35.30 -1 505 GLU A OE2   1 
ATOM   4052  N  N     . ILE A 1 506 ? 134.915 164.000 96.087  1.00 26.44 ?  506 ILE A N     1 
ATOM   4053  C  CA    . ILE A 1 506 ? 134.066 164.271 97.243  1.00 24.78 ?  506 ILE A CA    1 
ATOM   4054  C  C     . ILE A 1 506 ? 134.768 165.214 98.211  1.00 28.62 ?  506 ILE A C     1 
ATOM   4055  O  O     . ILE A 1 506 ? 134.145 166.117 98.780  1.00 34.21 ?  506 ILE A O     1 
ATOM   4056  C  CB    . ILE A 1 506 ? 133.654 162.952 97.925  1.00 23.01 ?  506 ILE A CB    1 
ATOM   4057  C  CG1   . ILE A 1 506 ? 132.760 162.128 96.998  1.00 26.55 ?  506 ILE A CG1   1 
ATOM   4058  C  CG2   . ILE A 1 506 ? 132.936 163.226 99.236  1.00 23.61 ?  506 ILE A CG2   1 
ATOM   4059  C  CD1   . ILE A 1 506 ? 132.595 160.690 97.431  1.00 21.55 ?  506 ILE A CD1   1 
ATOM   4060  N  N     . ALA A 1 507 ? 136.076 165.025 98.409  1.00 30.57 ?  507 ALA A N     1 
ATOM   4061  C  CA    . ALA A 1 507 ? 136.832 165.934 99.265  1.00 28.17 ?  507 ALA A CA    1 
ATOM   4062  C  C     . ALA A 1 507 ? 136.818 167.355 98.711  1.00 30.16 ?  507 ALA A C     1 
ATOM   4063  O  O     . ALA A 1 507 ? 136.680 168.322 99.468  1.00 33.75 ?  507 ALA A O     1 
ATOM   4064  C  CB    . ALA A 1 507 ? 138.268 165.435 99.422  1.00 24.00 ?  507 ALA A CB    1 
ATOM   4065  N  N     . LYS A 1 508 ? 136.968 167.498 97.394  1.00 34.66 ?  508 LYS A N     1 
ATOM   4066  C  CA    . LYS A 1 508 ? 136.926 168.818 96.774  1.00 32.34 ?  508 LYS A CA    1 
ATOM   4067  C  C     . LYS A 1 508 ? 135.540 169.443 96.887  1.00 37.17 ?  508 LYS A C     1 
ATOM   4068  O  O     . LYS A 1 508 ? 135.415 170.641 97.170  1.00 43.61 ?  508 LYS A O     1 
ATOM   4069  C  CB    . LYS A 1 508 ? 137.354 168.714 95.310  1.00 34.75 ?  508 LYS A CB    1 
ATOM   4070  C  CG    . LYS A 1 508 ? 137.102 169.966 94.490  1.00 36.97 ?  508 LYS A CG    1 
ATOM   4071  C  CD    . LYS A 1 508 ? 137.277 169.691 93.007  1.00 38.51 ?  508 LYS A CD    1 
ATOM   4072  C  CE    . LYS A 1 508 ? 137.068 170.950 92.184  1.00 37.16 ?  508 LYS A CE    1 
ATOM   4073  N  NZ    . LYS A 1 508 ? 137.906 170.956 90.954  1.00 40.86 1  508 LYS A NZ    1 
ATOM   4074  N  N     . GLU A 1 509 ? 134.488 168.652 96.665  1.00 35.71 ?  509 GLU A N     1 
ATOM   4075  C  CA    . GLU A 1 509 ? 133.128 169.179 96.722  1.00 34.30 ?  509 GLU A CA    1 
ATOM   4076  C  C     . GLU A 1 509 ? 132.767 169.623 98.134  1.00 37.22 ?  509 GLU A C     1 
ATOM   4077  O  O     . GLU A 1 509 ? 132.274 170.738 98.339  1.00 41.97 ?  509 GLU A O     1 
ATOM   4078  C  CB    . GLU A 1 509 ? 132.138 168.126 96.222  1.00 33.13 ?  509 GLU A CB    1 
ATOM   4079  C  CG    . GLU A 1 509 ? 132.170 167.906 94.719  1.00 40.38 ?  509 GLU A CG    1 
ATOM   4080  C  CD    . GLU A 1 509 ? 131.753 166.501 94.328  1.00 43.69 ?  509 GLU A CD    1 
ATOM   4081  O  OE1   . GLU A 1 509 ? 131.257 165.761 95.203  1.00 42.01 ?  509 GLU A OE1   1 
ATOM   4082  O  OE2   . GLU A 1 509 ? 131.925 166.137 93.146  1.00 40.06 -1 509 GLU A OE2   1 
ATOM   4083  N  N     . LYS A 1 510 ? 133.006 168.762 99.122  1.00 33.73 ?  510 LYS A N     1 
ATOM   4084  C  CA    . LYS A 1 510 ? 132.690 169.086 100.506 1.00 30.44 ?  510 LYS A CA    1 
ATOM   4085  C  C     . LYS A 1 510 ? 133.748 169.954 101.171 1.00 32.19 ?  510 LYS A C     1 
ATOM   4086  O  O     . LYS A 1 510 ? 133.493 170.490 102.254 1.00 38.71 ?  510 LYS A O     1 
ATOM   4087  C  CB    . LYS A 1 510 ? 132.497 167.799 101.313 1.00 29.73 ?  510 LYS A CB    1 
ATOM   4088  C  CG    . LYS A 1 510 ? 131.468 166.852 100.720 1.00 29.83 ?  510 LYS A CG    1 
ATOM   4089  C  CD    . LYS A 1 510 ? 131.231 165.655 101.620 1.00 30.57 ?  510 LYS A CD    1 
ATOM   4090  C  CE    . LYS A 1 510 ? 129.793 165.171 101.528 1.00 35.93 ?  510 LYS A CE    1 
ATOM   4091  N  NZ    . LYS A 1 510 ? 129.711 163.691 101.386 1.00 35.29 1  510 LYS A NZ    1 
ATOM   4092  N  N     . GLY A 1 511 ? 134.919 170.105 100.556 1.00 31.46 ?  511 GLY A N     1 
ATOM   4093  C  CA    . GLY A 1 511 ? 135.964 170.923 101.133 1.00 28.76 ?  511 GLY A CA    1 
ATOM   4094  C  C     . GLY A 1 511 ? 136.666 170.319 102.325 1.00 36.85 ?  511 GLY A C     1 
ATOM   4095  O  O     . GLY A 1 511 ? 137.407 171.028 103.013 1.00 40.96 ?  511 GLY A O     1 
ATOM   4096  N  N     . GLU A 1 512 ? 136.459 169.032 102.594 1.00 29.37 ?  512 GLU A N     1 
ATOM   4097  C  CA    . GLU A 1 512 ? 137.049 168.381 103.753 1.00 27.23 ?  512 GLU A CA    1 
ATOM   4098  C  C     . GLU A 1 512 ? 137.582 167.011 103.361 1.00 29.79 ?  512 GLU A C     1 
ATOM   4099  O  O     . GLU A 1 512 ? 137.008 166.320 102.517 1.00 29.31 ?  512 GLU A O     1 
ATOM   4100  C  CB    . GLU A 1 512 ? 136.033 168.237 104.895 1.00 29.38 ?  512 GLU A CB    1 
ATOM   4101  C  CG    . GLU A 1 512 ? 134.757 167.513 104.500 1.00 31.17 ?  512 GLU A CG    1 
ATOM   4102  C  CD    . GLU A 1 512 ? 134.048 166.893 105.686 1.00 33.54 ?  512 GLU A CD    1 
ATOM   4103  O  OE1   . GLU A 1 512 ? 134.734 166.527 106.663 1.00 31.95 ?  512 GLU A OE1   1 
ATOM   4104  O  OE2   . GLU A 1 512 ? 132.806 166.771 105.643 1.00 30.20 -1 512 GLU A OE2   1 
ATOM   4105  N  N     . THR A 1 513 ? 138.691 166.631 103.985 1.00 31.54 ?  513 THR A N     1 
ATOM   4106  C  CA    . THR A 1 513 ? 139.281 165.311 103.859 1.00 24.41 ?  513 THR A CA    1 
ATOM   4107  C  C     . THR A 1 513 ? 139.023 164.531 105.145 1.00 26.94 ?  513 THR A C     1 
ATOM   4108  O  O     . THR A 1 513 ? 138.337 165.007 106.057 1.00 31.85 ?  513 THR A O     1 
ATOM   4109  C  CB    . THR A 1 513 ? 140.774 165.428 103.552 1.00 26.12 ?  513 THR A CB    1 
ATOM   4110  O  OG1   . THR A 1 513 ? 141.471 165.855 104.728 1.00 35.94 ?  513 THR A OG1   1 
ATOM   4111  C  CG2   . THR A 1 513 ? 141.008 166.437 102.441 1.00 25.68 ?  513 THR A CG2   1 
ATOM   4112  N  N     . PHE A 1 514 ? 139.572 163.323 105.225 1.00 23.23 ?  514 PHE A N     1 
ATOM   4113  C  CA    . PHE A 1 514 ? 139.480 162.574 106.467 1.00 23.53 ?  514 PHE A CA    1 
ATOM   4114  C  C     . PHE A 1 514 ? 140.507 163.096 107.463 1.00 19.94 ?  514 PHE A C     1 
ATOM   4115  O  O     . PHE A 1 514 ? 141.521 163.690 107.086 1.00 28.21 ?  514 PHE A O     1 
ATOM   4116  C  CB    . PHE A 1 514 ? 139.665 161.073 106.228 1.00 16.82 ?  514 PHE A CB    1 
ATOM   4117  C  CG    . PHE A 1 514 ? 141.029 160.685 105.725 1.00 18.74 ?  514 PHE A CG    1 
ATOM   4118  C  CD1   . PHE A 1 514 ? 141.306 160.674 104.370 1.00 18.81 ?  514 PHE A CD1   1 
ATOM   4119  C  CD2   . PHE A 1 514 ? 142.021 160.293 106.607 1.00 19.05 ?  514 PHE A CD2   1 
ATOM   4120  C  CE1   . PHE A 1 514 ? 142.550 160.301 103.907 1.00 12.80 ?  514 PHE A CE1   1 
ATOM   4121  C  CE2   . PHE A 1 514 ? 143.267 159.921 106.149 1.00 16.19 ?  514 PHE A CE2   1 
ATOM   4122  C  CZ    . PHE A 1 514 ? 143.532 159.926 104.797 1.00 15.17 ?  514 PHE A CZ    1 
ATOM   4123  N  N     . ASP A 1 515 ? 140.222 162.888 108.745 1.00 22.86 ?  515 ASP A N     1 
ATOM   4124  C  CA    . ASP A 1 515 ? 141.085 163.418 109.792 1.00 26.17 ?  515 ASP A CA    1 
ATOM   4125  C  C     . ASP A 1 515 ? 142.488 162.835 109.680 1.00 27.64 ?  515 ASP A C     1 
ATOM   4126  O  O     . ASP A 1 515 ? 142.666 161.640 109.432 1.00 32.62 ?  515 ASP A O     1 
ATOM   4127  C  CB    . ASP A 1 515 ? 140.496 163.118 111.170 1.00 27.91 ?  515 ASP A CB    1 
ATOM   4128  C  CG    . ASP A 1 515 ? 139.330 164.025 111.512 1.00 30.13 ?  515 ASP A CG    1 
ATOM   4129  O  OD1   . ASP A 1 515 ? 138.732 164.603 110.580 1.00 30.97 ?  515 ASP A OD1   1 
ATOM   4130  O  OD2   . ASP A 1 515 ? 139.013 164.163 112.712 1.00 31.63 -1 515 ASP A OD2   1 
ATOM   4131  N  N     . GLN A 1 516 ? 143.486 163.702 109.859 1.00 29.29 ?  516 GLN A N     1 
ATOM   4132  C  CA    . GLN A 1 516 ? 144.898 163.341 109.737 1.00 27.02 ?  516 GLN A CA    1 
ATOM   4133  C  C     . GLN A 1 516 ? 145.233 162.824 108.341 1.00 24.74 ?  516 GLN A C     1 
ATOM   4134  O  O     . GLN A 1 516 ? 146.060 161.925 108.184 1.00 31.63 ?  516 GLN A O     1 
ATOM   4135  C  CB    . GLN A 1 516 ? 145.307 162.314 110.797 1.00 23.58 ?  516 GLN A CB    1 
ATOM   4136  C  CG    . GLN A 1 516 ? 145.080 162.765 112.228 1.00 27.32 ?  516 GLN A CG    1 
ATOM   4137  C  CD    . GLN A 1 516 ? 145.328 161.655 113.230 1.00 28.96 ?  516 GLN A CD    1 
ATOM   4138  O  OE1   . GLN A 1 516 ? 146.473 161.294 113.503 1.00 24.45 ?  516 GLN A OE1   1 
ATOM   4139  N  NE2   . GLN A 1 516 ? 144.254 161.105 113.783 1.00 30.70 ?  516 GLN A NE2   1 
ATOM   4140  N  N     . TYR A 1 517 ? 144.592 163.382 107.312 1.00 21.14 ?  517 TYR A N     1 
ATOM   4141  C  CA    . TYR A 1 517 ? 144.942 163.011 105.945 1.00 19.39 ?  517 TYR A CA    1 
ATOM   4142  C  C     . TYR A 1 517 ? 146.311 163.547 105.551 1.00 29.46 ?  517 TYR A C     1 
ATOM   4143  O  O     . TYR A 1 517 ? 147.020 162.911 104.764 1.00 36.04 ?  517 TYR A O     1 
ATOM   4144  C  CB    . TYR A 1 517 ? 143.880 163.511 104.965 1.00 18.68 ?  517 TYR A CB    1 
ATOM   4145  C  CG    . TYR A 1 517 ? 144.422 163.798 103.582 1.00 27.03 ?  517 TYR A CG    1 
ATOM   4146  C  CD1   . TYR A 1 517 ? 144.621 162.774 102.667 1.00 23.94 ?  517 TYR A CD1   1 
ATOM   4147  C  CD2   . TYR A 1 517 ? 144.739 165.095 103.193 1.00 29.69 ?  517 TYR A CD2   1 
ATOM   4148  C  CE1   . TYR A 1 517 ? 145.122 163.029 101.406 1.00 27.36 ?  517 TYR A CE1   1 
ATOM   4149  C  CE2   . TYR A 1 517 ? 145.243 165.358 101.936 1.00 25.86 ?  517 TYR A CE2   1 
ATOM   4150  C  CZ    . TYR A 1 517 ? 145.431 164.323 101.048 1.00 29.69 ?  517 TYR A CZ    1 
ATOM   4151  O  OH    . TYR A 1 517 ? 145.928 164.584 99.793  1.00 34.33 ?  517 TYR A OH    1 
ATOM   4152  N  N     . GLU A 1 518 ? 146.694 164.710 106.084 1.00 31.48 ?  518 GLU A N     1 
ATOM   4153  C  CA    . GLU A 1 518 ? 147.933 165.357 105.667 1.00 33.30 ?  518 GLU A CA    1 
ATOM   4154  C  C     . GLU A 1 518 ? 149.149 164.481 105.931 1.00 37.36 ?  518 GLU A C     1 
ATOM   4155  O  O     . GLU A 1 518 ? 150.145 164.566 105.203 1.00 39.66 ?  518 GLU A O     1 
ATOM   4156  C  CB    . GLU A 1 518 ? 148.095 166.710 106.370 1.00 32.58 ?  518 GLU A CB    1 
ATOM   4157  C  CG    . GLU A 1 518 ? 146.913 167.681 106.243 1.00 34.94 ?  518 GLU A CG    1 
ATOM   4158  C  CD    . GLU A 1 518 ? 145.669 167.232 106.992 1.00 42.69 ?  518 GLU A CD    1 
ATOM   4159  O  OE1   . GLU A 1 518 ? 144.552 167.588 106.561 1.00 41.60 ?  518 GLU A OE1   1 
ATOM   4160  O  OE2   . GLU A 1 518 ? 145.810 166.523 108.011 1.00 40.31 -1 518 GLU A OE2   1 
ATOM   4161  N  N     . GLY A 1 519 ? 149.095 163.638 106.961 1.00 26.93 ?  519 GLY A N     1 
ATOM   4162  C  CA    . GLY A 1 519 ? 150.182 162.717 107.220 1.00 23.56 ?  519 GLY A CA    1 
ATOM   4163  C  C     . GLY A 1 519 ? 150.140 161.432 106.424 1.00 23.79 ?  519 GLY A C     1 
ATOM   4164  O  O     . GLY A 1 519 ? 151.091 160.648 106.490 1.00 28.85 ?  519 GLY A O     1 
ATOM   4165  N  N     . SER A 1 520 ? 149.067 161.201 105.671 1.00 22.77 ?  520 SER A N     1 
ATOM   4166  C  CA    . SER A 1 520 ? 148.920 159.958 104.933 1.00 24.37 ?  520 SER A CA    1 
ATOM   4167  C  C     . SER A 1 520 ? 149.803 159.952 103.689 1.00 22.49 ?  520 SER A C     1 
ATOM   4168  O  O     . SER A 1 520 ? 150.272 160.991 103.216 1.00 31.54 ?  520 SER A O     1 
ATOM   4169  C  CB    . SER A 1 520 ? 147.460 159.738 104.538 1.00 19.01 ?  520 SER A CB    1 
ATOM   4170  O  OG    . SER A 1 520 ? 147.009 160.756 103.663 1.00 21.50 ?  520 SER A OG    1 
ATOM   4171  N  N     . THR A 1 521 ? 150.030 158.748 103.159 1.00 20.34 ?  521 THR A N     1 
ATOM   4172  C  CA    . THR A 1 521 ? 150.812 158.606 101.938 1.00 21.16 ?  521 THR A CA    1 
ATOM   4173  C  C     . THR A 1 521 ? 150.082 159.157 100.720 1.00 23.54 ?  521 THR A C     1 
ATOM   4174  O  O     . THR A 1 521 ? 150.725 159.426 99.700  1.00 24.52 ?  521 THR A O     1 
ATOM   4175  C  CB    . THR A 1 521 ? 151.176 157.139 101.710 1.00 22.76 ?  521 THR A CB    1 
ATOM   4176  O  OG1   . THR A 1 521 ? 150.000 156.401 101.357 1.00 23.73 ?  521 THR A OG1   1 
ATOM   4177  C  CG2   . THR A 1 521 ? 151.782 156.541 102.968 1.00 19.65 ?  521 THR A CG2   1 
ATOM   4178  N  N     . TYR A 1 522 ? 148.758 159.315 100.797 1.00 26.55 ?  522 TYR A N     1 
ATOM   4179  C  CA    . TYR A 1 522 ? 148.036 160.012 99.738  1.00 18.97 ?  522 TYR A CA    1 
ATOM   4180  C  C     . TYR A 1 522 ? 148.489 161.463 99.643  1.00 23.87 ?  522 TYR A C     1 
ATOM   4181  O  O     . TYR A 1 522 ? 148.727 161.985 98.548  1.00 25.62 ?  522 TYR A O     1 
ATOM   4182  C  CB    . TYR A 1 522 ? 146.530 159.945 99.990  1.00 17.28 ?  522 TYR A CB    1 
ATOM   4183  C  CG    . TYR A 1 522 ? 145.949 158.550 100.018 1.00 17.83 ?  522 TYR A CG    1 
ATOM   4184  C  CD1   . TYR A 1 522 ? 145.918 157.765 98.873  1.00 19.28 ?  522 TYR A CD1   1 
ATOM   4185  C  CD2   . TYR A 1 522 ? 145.412 158.026 101.185 1.00 21.38 ?  522 TYR A CD2   1 
ATOM   4186  C  CE1   . TYR A 1 522 ? 145.382 156.494 98.895  1.00 18.02 ?  522 TYR A CE1   1 
ATOM   4187  C  CE2   . TYR A 1 522 ? 144.870 156.757 101.215 1.00 18.03 ?  522 TYR A CE2   1 
ATOM   4188  C  CZ    . TYR A 1 522 ? 144.860 155.995 100.069 1.00 19.92 ?  522 TYR A CZ    1 
ATOM   4189  O  OH    . TYR A 1 522 ? 144.325 154.730 100.096 1.00 25.93 ?  522 TYR A OH    1 
ATOM   4190  N  N     . ALA A 1 523 ? 148.615 162.131 100.793 1.00 25.50 ?  523 ALA A N     1 
ATOM   4191  C  CA    . ALA A 1 523 ? 149.018 163.533 100.801 1.00 26.43 ?  523 ALA A CA    1 
ATOM   4192  C  C     . ALA A 1 523 ? 150.456 163.700 100.329 1.00 31.21 ?  523 ALA A C     1 
ATOM   4193  O  O     . ALA A 1 523 ? 150.766 164.637 99.584  1.00 32.89 ?  523 ALA A O     1 
ATOM   4194  C  CB    . ALA A 1 523 ? 148.838 164.119 102.200 1.00 25.19 ?  523 ALA A CB    1 
ATOM   4195  N  N     . THR A 1 524 ? 151.348 162.806 100.753 1.00 24.86 ?  524 THR A N     1 
ATOM   4196  C  CA    . THR A 1 524 ? 152.747 162.880 100.357 1.00 24.67 ?  524 THR A CA    1 
ATOM   4197  C  C     . THR A 1 524 ? 152.998 162.333 98.959  1.00 30.74 ?  524 THR A C     1 
ATOM   4198  O  O     . THR A 1 524 ? 154.105 162.505 98.436  1.00 36.80 ?  524 THR A O     1 
ATOM   4199  C  CB    . THR A 1 524 ? 153.621 162.125 101.362 1.00 28.88 ?  524 THR A CB    1 
ATOM   4200  O  OG1   . THR A 1 524 ? 153.469 160.714 101.168 1.00 30.78 ?  524 THR A OG1   1 
ATOM   4201  C  CG2   . THR A 1 524 ? 153.222 162.480 102.785 1.00 26.81 ?  524 THR A CG2   1 
ATOM   4202  N  N     . GLY A 1 525 ? 152.012 161.683 98.345  1.00 26.63 ?  525 GLY A N     1 
ATOM   4203  C  CA    . GLY A 1 525 ? 152.167 161.126 97.021  1.00 24.39 ?  525 GLY A CA    1 
ATOM   4204  C  C     . GLY A 1 525 ? 152.886 159.798 96.961  1.00 29.59 ?  525 GLY A C     1 
ATOM   4205  O  O     . GLY A 1 525 ? 153.079 159.268 95.860  1.00 32.79 ?  525 GLY A O     1 
ATOM   4206  N  N     . GLU A 1 526 ? 153.291 159.244 98.106  1.00 29.06 ?  526 GLU A N     1 
ATOM   4207  C  CA    . GLU A 1 526 ? 153.980 157.957 98.108  1.00 29.80 ?  526 GLU A CA    1 
ATOM   4208  C  C     . GLU A 1 526 ? 153.065 156.840 97.624  1.00 31.92 ?  526 GLU A C     1 
ATOM   4209  O  O     . GLU A 1 526 ? 153.507 155.927 96.916  1.00 37.13 ?  526 GLU A O     1 
ATOM   4210  C  CB    . GLU A 1 526 ? 154.511 157.656 99.510  1.00 30.68 ?  526 GLU A CB    1 
ATOM   4211  C  CG    . GLU A 1 526 ? 154.917 156.210 99.734  1.00 31.72 ?  526 GLU A CG    1 
ATOM   4212  C  CD    . GLU A 1 526 ? 155.021 155.858 101.205 1.00 36.24 ?  526 GLU A CD    1 
ATOM   4213  O  OE1   . GLU A 1 526 ? 155.085 156.787 102.036 1.00 35.08 ?  526 GLU A OE1   1 
ATOM   4214  O  OE2   . GLU A 1 526 ? 155.037 154.652 101.530 1.00 34.53 -1 526 GLU A OE2   1 
ATOM   4215  N  N     . TYR A 1 527 ? 151.781 156.905 97.989  1.00 31.75 ?  527 TYR A N     1 
ATOM   4216  C  CA    . TYR A 1 527 ? 150.828 155.866 97.607  1.00 22.45 ?  527 TYR A CA    1 
ATOM   4217  C  C     . TYR A 1 527 ? 150.803 155.655 96.099  1.00 24.31 ?  527 TYR A C     1 
ATOM   4218  O  O     . TYR A 1 527 ? 150.647 154.525 95.623  1.00 30.71 ?  527 TYR A O     1 
ATOM   4219  C  CB    . TYR A 1 527 ? 149.432 156.230 98.116  1.00 18.46 ?  527 TYR A CB    1 
ATOM   4220  C  CG    . TYR A 1 527 ? 148.381 155.179 97.844  1.00 25.45 ?  527 TYR A CG    1 
ATOM   4221  C  CD1   . TYR A 1 527 ? 147.671 155.168 96.650  1.00 23.33 ?  527 TYR A CD1   1 
ATOM   4222  C  CD2   . TYR A 1 527 ? 148.094 154.201 98.785  1.00 24.14 ?  527 TYR A CD2   1 
ATOM   4223  C  CE1   . TYR A 1 527 ? 146.713 154.208 96.400  1.00 20.19 ?  527 TYR A CE1   1 
ATOM   4224  C  CE2   . TYR A 1 527 ? 147.137 153.240 98.544  1.00 22.64 ?  527 TYR A CE2   1 
ATOM   4225  C  CZ    . TYR A 1 527 ? 146.449 153.249 97.351  1.00 23.29 ?  527 TYR A CZ    1 
ATOM   4226  O  OH    . TYR A 1 527 ? 145.493 152.290 97.108  1.00 29.93 ?  527 TYR A OH    1 
ATOM   4227  N  N     . PHE A 1 528 ? 150.960 156.730 95.333  1.00 26.54 ?  528 PHE A N     1 
ATOM   4228  C  CA    . PHE A 1 528 ? 150.883 156.674 93.881  1.00 27.56 ?  528 PHE A CA    1 
ATOM   4229  C  C     . PHE A 1 528 ? 152.199 156.283 93.224  1.00 31.65 ?  528 PHE A C     1 
ATOM   4230  O  O     . PHE A 1 528 ? 152.252 156.206 91.993  1.00 37.05 ?  528 PHE A O     1 
ATOM   4231  C  CB    . PHE A 1 528 ? 150.418 158.025 93.330  1.00 28.67 ?  528 PHE A CB    1 
ATOM   4232  C  CG    . PHE A 1 528 ? 149.116 158.498 93.907  1.00 31.81 ?  528 PHE A CG    1 
ATOM   4233  C  CD1   . PHE A 1 528 ? 147.915 158.147 93.313  1.00 27.01 ?  528 PHE A CD1   1 
ATOM   4234  C  CD2   . PHE A 1 528 ? 149.089 159.288 95.043  1.00 29.35 ?  528 PHE A CD2   1 
ATOM   4235  C  CE1   . PHE A 1 528 ? 146.714 158.577 93.840  1.00 27.38 ?  528 PHE A CE1   1 
ATOM   4236  C  CE2   . PHE A 1 528 ? 147.892 159.720 95.575  1.00 29.22 ?  528 PHE A CE2   1 
ATOM   4237  C  CZ    . PHE A 1 528 ? 146.703 159.363 94.972  1.00 28.09 ?  528 PHE A CZ    1 
ATOM   4238  N  N     . ASP A 1 529 ? 153.251 156.033 94.009  1.00 30.61 ?  529 ASP A N     1 
ATOM   4239  C  CA    . ASP A 1 529 ? 154.563 155.730 93.444  1.00 29.55 ?  529 ASP A CA    1 
ATOM   4240  C  C     . ASP A 1 529 ? 154.486 154.579 92.446  1.00 33.50 ?  529 ASP A C     1 
ATOM   4241  O  O     . ASP A 1 529 ? 154.762 154.750 91.252  1.00 35.83 ?  529 ASP A O     1 
ATOM   4242  C  CB    . ASP A 1 529 ? 155.548 155.407 94.569  1.00 32.37 ?  529 ASP A CB    1 
ATOM   4243  C  CG    . ASP A 1 529 ? 156.095 156.650 95.238  1.00 39.19 ?  529 ASP A CG    1 
ATOM   4244  O  OD1   . ASP A 1 529 ? 155.787 157.766 94.768  1.00 36.61 ?  529 ASP A OD1   1 
ATOM   4245  O  OD2   . ASP A 1 529 ? 156.834 156.513 96.237  1.00 39.06 -1 529 ASP A OD2   1 
ATOM   4246  N  N     . LYS A 1 530 ? 154.065 153.402 92.916  1.00 34.90 ?  530 LYS A N     1 
ATOM   4247  C  CA    . LYS A 1 530 ? 153.957 152.245 92.035  1.00 32.53 ?  530 LYS A CA    1 
ATOM   4248  C  C     . LYS A 1 530 ? 152.977 152.481 90.896  1.00 32.70 ?  530 LYS A C     1 
ATOM   4249  O  O     . LYS A 1 530 ? 153.036 151.776 89.884  1.00 34.96 ?  530 LYS A O     1 
ATOM   4250  C  CB    . LYS A 1 530 ? 153.534 151.012 92.833  1.00 31.49 ?  530 LYS A CB    1 
ATOM   4251  C  CG    . LYS A 1 530 ? 152.046 150.726 92.774  1.00 29.76 ?  530 LYS A CG    1 
ATOM   4252  C  CD    . LYS A 1 530 ? 151.638 149.678 93.784  1.00 31.93 ?  530 LYS A CD    1 
ATOM   4253  C  CE    . LYS A 1 530 ? 150.188 149.288 93.594  1.00 27.82 ?  530 LYS A CE    1 
ATOM   4254  N  NZ    . LYS A 1 530 ? 149.437 149.348 94.875  1.00 33.29 1  530 LYS A NZ    1 
ATOM   4255  N  N     . TYR A 1 531 ? 152.082 153.455 91.036  1.00 30.64 ?  531 TYR A N     1 
ATOM   4256  C  CA    . TYR A 1 531 ? 151.131 153.767 89.983  1.00 28.11 ?  531 TYR A CA    1 
ATOM   4257  C  C     . TYR A 1 531 ? 151.673 154.762 88.969  1.00 26.93 ?  531 TYR A C     1 
ATOM   4258  O  O     . TYR A 1 531 ? 151.189 154.788 87.832  1.00 32.56 ?  531 TYR A O     1 
ATOM   4259  C  CB    . TYR A 1 531 ? 149.836 154.306 90.592  1.00 27.82 ?  531 TYR A CB    1 
ATOM   4260  C  CG    . TYR A 1 531 ? 148.989 153.240 91.243  1.00 28.79 ?  531 TYR A CG    1 
ATOM   4261  C  CD1   . TYR A 1 531 ? 148.588 152.117 90.533  1.00 23.74 ?  531 TYR A CD1   1 
ATOM   4262  C  CD2   . TYR A 1 531 ? 148.590 153.355 92.568  1.00 25.66 ?  531 TYR A CD2   1 
ATOM   4263  C  CE1   . TYR A 1 531 ? 147.814 151.139 91.121  1.00 29.88 ?  531 TYR A CE1   1 
ATOM   4264  C  CE2   . TYR A 1 531 ? 147.814 152.382 93.164  1.00 25.40 ?  531 TYR A CE2   1 
ATOM   4265  C  CZ    . TYR A 1 531 ? 147.430 151.277 92.436  1.00 28.75 ?  531 TYR A CZ    1 
ATOM   4266  O  OH    . TYR A 1 531 ? 146.658 150.305 93.026  1.00 26.64 ?  531 TYR A OH    1 
ATOM   4267  N  N     . VAL A 1 532 ? 152.662 155.580 89.346  1.00 36.73 ?  532 VAL A N     1 
ATOM   4268  C  CA    . VAL A 1 532 ? 153.247 156.527 88.403  1.00 35.08 ?  532 VAL A CA    1 
ATOM   4269  C  C     . VAL A 1 532 ? 154.486 155.970 87.720  1.00 36.69 ?  532 VAL A C     1 
ATOM   4270  O  O     . VAL A 1 532 ? 155.083 156.657 86.881  1.00 41.15 ?  532 VAL A O     1 
ATOM   4271  C  CB    . VAL A 1 532 ? 153.585 157.867 89.090  1.00 35.29 ?  532 VAL A CB    1 
ATOM   4272  C  CG1   . VAL A 1 532 ? 152.339 158.474 89.714  1.00 34.97 ?  532 VAL A CG1   1 
ATOM   4273  C  CG2   . VAL A 1 532 ? 154.673 157.680 90.130  1.00 33.74 ?  532 VAL A CG2   1 
ATOM   4274  N  N     . SER A 1 533 ? 154.888 154.745 88.048  1.00 37.31 ?  533 SER A N     1 
ATOM   4275  C  CA    . SER A 1 533 ? 156.048 154.111 87.442  1.00 39.93 ?  533 SER A CA    1 
ATOM   4276  C  C     . SER A 1 533 ? 155.737 152.794 86.750  1.00 40.94 ?  533 SER A C     1 
ATOM   4277  O  O     . SER A 1 533 ? 156.397 152.466 85.761  1.00 43.31 ?  533 SER A O     1 
ATOM   4278  C  CB    . SER A 1 533 ? 157.135 153.867 88.501  1.00 41.14 ?  533 SER A CB    1 
ATOM   4279  O  OG    . SER A 1 533 ? 156.764 152.818 89.378  1.00 44.41 ?  533 SER A OG    1 
ATOM   4280  N  N     . THR A 1 534 ? 154.757 152.037 87.233  1.00 40.28 ?  534 THR A N     1 
ATOM   4281  C  CA    . THR A 1 534 ? 154.397 150.747 86.661  1.00 38.86 ?  534 THR A CA    1 
ATOM   4282  C  C     . THR A 1 534 ? 153.081 150.875 85.908  1.00 38.19 ?  534 THR A C     1 
ATOM   4283  O  O     . THR A 1 534 ? 152.096 151.384 86.453  1.00 43.56 ?  534 THR A O     1 
ATOM   4284  C  CB    . THR A 1 534 ? 154.276 149.677 87.750  1.00 39.36 ?  534 THR A CB    1 
ATOM   4285  O  OG1   . THR A 1 534 ? 155.560 149.450 88.345  1.00 42.76 ?  534 THR A OG1   1 
ATOM   4286  C  CG2   . THR A 1 534 ? 153.756 148.373 87.165  1.00 38.66 ?  534 THR A CG2   1 
ATOM   4287  N  N     . ASP A 1 535 ? 153.072 150.418 84.660  1.00 40.64 ?  535 ASP A N     1 
ATOM   4288  C  CA    . ASP A 1 535 ? 151.863 150.404 83.850  1.00 39.74 ?  535 ASP A CA    1 
ATOM   4289  C  C     . ASP A 1 535 ? 151.098 149.112 84.111  1.00 41.84 ?  535 ASP A C     1 
ATOM   4290  O  O     . ASP A 1 535 ? 151.661 148.018 84.007  1.00 42.89 ?  535 ASP A O     1 
ATOM   4291  C  CB    . ASP A 1 535 ? 152.206 150.531 82.366  1.00 38.68 ?  535 ASP A CB    1 
ATOM   4292  C  CG    . ASP A 1 535 ? 151.022 150.968 81.529  1.00 44.50 ?  535 ASP A CG    1 
ATOM   4293  O  OD1   . ASP A 1 535 ? 150.576 152.124 81.684  1.00 45.74 ?  535 ASP A OD1   1 
ATOM   4294  O  OD2   . ASP A 1 535 ? 150.540 150.155 80.714  1.00 45.92 -1 535 ASP A OD2   1 
ATOM   4295  N  N     . PHE A 1 536 ? 149.817 149.244 84.453  1.00 34.20 ?  536 PHE A N     1 
ATOM   4296  C  CA    . PHE A 1 536 ? 148.984 148.102 84.805  1.00 26.98 ?  536 PHE A CA    1 
ATOM   4297  C  C     . PHE A 1 536 ? 148.004 147.738 83.695  1.00 31.33 ?  536 PHE A C     1 
ATOM   4298  O  O     . PHE A 1 536 ? 146.983 147.094 83.959  1.00 37.66 ?  536 PHE A O     1 
ATOM   4299  C  CB    . PHE A 1 536 ? 148.241 148.376 86.112  1.00 29.06 ?  536 PHE A CB    1 
ATOM   4300  C  CG    . PHE A 1 536 ? 149.139 148.436 87.315  1.00 27.91 ?  536 PHE A CG    1 
ATOM   4301  C  CD1   . PHE A 1 536 ? 149.490 147.283 87.992  1.00 27.98 ?  536 PHE A CD1   1 
ATOM   4302  C  CD2   . PHE A 1 536 ? 149.638 149.646 87.764  1.00 27.54 ?  536 PHE A CD2   1 
ATOM   4303  C  CE1   . PHE A 1 536 ? 150.318 147.334 89.096  1.00 28.05 ?  536 PHE A CE1   1 
ATOM   4304  C  CE2   . PHE A 1 536 ? 150.468 149.703 88.868  1.00 32.24 ?  536 PHE A CE2   1 
ATOM   4305  C  CZ    . PHE A 1 536 ? 150.806 148.546 89.535  1.00 28.77 ?  536 PHE A CZ    1 
ATOM   4306  N  N     . SER A 1 537 ? 148.294 148.143 82.462  1.00 37.02 ?  537 SER A N     1 
ATOM   4307  C  CA    . SER A 1 537 ? 147.501 147.714 81.325  1.00 33.64 ?  537 SER A CA    1 
ATOM   4308  C  C     . SER A 1 537 ? 147.670 146.210 81.114  1.00 38.82 ?  537 SER A C     1 
ATOM   4309  O  O     . SER A 1 537 ? 148.710 145.642 81.459  1.00 39.19 ?  537 SER A O     1 
ATOM   4310  C  CB    . SER A 1 537 ? 147.921 148.476 80.071  1.00 37.25 ?  537 SER A CB    1 
ATOM   4311  O  OG    . SER A 1 537 ? 147.533 147.803 78.887  1.00 44.12 ?  537 SER A OG    1 
ATOM   4312  N  N     . PRO A 1 538 ? 146.653 145.538 80.572  1.00 37.27 ?  538 PRO A N     1 
ATOM   4313  C  CA    . PRO A 1 538 ? 146.751 144.085 80.388  1.00 34.32 ?  538 PRO A CA    1 
ATOM   4314  C  C     . PRO A 1 538 ? 147.922 143.702 79.494  1.00 39.19 ?  538 PRO A C     1 
ATOM   4315  O  O     . PRO A 1 538 ? 148.192 144.346 78.479  1.00 39.38 ?  538 PRO A O     1 
ATOM   4316  C  CB    . PRO A 1 538 ? 145.411 143.720 79.743  1.00 37.31 ?  538 PRO A CB    1 
ATOM   4317  C  CG    . PRO A 1 538 ? 144.488 144.814 80.145  1.00 34.46 ?  538 PRO A CG    1 
ATOM   4318  C  CD    . PRO A 1 538 ? 145.330 146.050 80.181  1.00 33.65 ?  538 PRO A CD    1 
ATOM   4319  N  N     . LYS A 1 539 ? 148.616 142.635 79.888  1.00 44.39 ?  539 LYS A N     1 
ATOM   4320  C  CA    . LYS A 1 539 ? 149.726 142.101 79.113  1.00 44.62 ?  539 LYS A CA    1 
ATOM   4321  C  C     . LYS A 1 539 ? 149.293 141.030 78.124  1.00 44.99 ?  539 LYS A C     1 
ATOM   4322  O  O     . LYS A 1 539 ? 150.113 140.592 77.309  1.00 47.43 ?  539 LYS A O     1 
ATOM   4323  C  CB    . LYS A 1 539 ? 150.794 141.527 80.049  1.00 43.77 ?  539 LYS A CB    1 
ATOM   4324  C  CG    . LYS A 1 539 ? 151.187 142.455 81.185  1.00 42.84 ?  539 LYS A CG    1 
ATOM   4325  C  CD    . LYS A 1 539 ? 152.278 143.422 80.756  1.00 45.68 ?  539 LYS A CD    1 
ATOM   4326  C  CE    . LYS A 1 539 ? 152.477 144.519 81.789  1.00 45.50 ?  539 LYS A CE    1 
ATOM   4327  N  NZ    . LYS A 1 539 ? 151.730 145.757 81.435  1.00 44.13 1  539 LYS A NZ    1 
ATOM   4328  N  N     . TYR A 1 540 ? 148.035 140.604 78.172  1.00 42.49 ?  540 TYR A N     1 
ATOM   4329  C  CA    . TYR A 1 540 ? 147.503 139.589 77.277  1.00 41.58 ?  540 TYR A CA    1 
ATOM   4330  C  C     . TYR A 1 540 ? 146.444 140.208 76.377  1.00 42.99 ?  540 TYR A C     1 
ATOM   4331  O  O     . TYR A 1 540 ? 145.668 141.065 76.813  1.00 44.81 ?  540 TYR A O     1 
ATOM   4332  C  CB    . TYR A 1 540 ? 146.911 138.417 78.064  1.00 42.66 ?  540 TYR A CB    1 
ATOM   4333  C  CG    . TYR A 1 540 ? 147.939 137.626 78.837  1.00 44.40 ?  540 TYR A CG    1 
ATOM   4334  C  CD1   . TYR A 1 540 ? 148.289 137.984 80.132  1.00 42.75 ?  540 TYR A CD1   1 
ATOM   4335  C  CD2   . TYR A 1 540 ? 148.566 136.525 78.269  1.00 45.61 ?  540 TYR A CD2   1 
ATOM   4336  C  CE1   . TYR A 1 540 ? 149.231 137.265 80.841  1.00 45.50 ?  540 TYR A CE1   1 
ATOM   4337  C  CE2   . TYR A 1 540 ? 149.509 135.801 78.971  1.00 40.60 ?  540 TYR A CE2   1 
ATOM   4338  C  CZ    . TYR A 1 540 ? 149.838 136.175 80.256  1.00 45.33 ?  540 TYR A CZ    1 
ATOM   4339  O  OH    . TYR A 1 540 ? 150.777 135.455 80.955  1.00 46.48 ?  540 TYR A OH    1 
ATOM   4340  N  N     . GLU A 1 541 ? 146.422 139.773 75.114  1.00 47.04 ?  541 GLU A N     1 
ATOM   4341  C  CA    . GLU A 1 541 ? 145.479 140.333 74.151  1.00 47.04 ?  541 GLU A CA    1 
ATOM   4342  C  C     . GLU A 1 541 ? 144.038 140.021 74.537  1.00 47.07 ?  541 GLU A C     1 
ATOM   4343  O  O     . GLU A 1 541 ? 143.139 140.841 74.318  1.00 44.24 ?  541 GLU A O     1 
ATOM   4344  C  CB    . GLU A 1 541 ? 145.784 139.804 72.750  1.00 45.13 ?  541 GLU A CB    1 
ATOM   4345  C  CG    . GLU A 1 541 ? 145.307 140.708 71.627  1.00 46.40 ?  541 GLU A CG    1 
ATOM   4346  C  CD    . GLU A 1 541 ? 145.253 139.994 70.291  1.00 52.19 ?  541 GLU A CD    1 
ATOM   4347  O  OE1   . GLU A 1 541 ? 145.277 138.746 70.282  1.00 52.67 ?  541 GLU A OE1   1 
ATOM   4348  O  OE2   . GLU A 1 541 ? 145.188 140.681 69.249  1.00 50.07 -1 541 GLU A OE2   1 
ATOM   4349  N  N     . LYS A 1 542 ? 143.799 138.837 75.104  1.00 42.45 ?  542 LYS A N     1 
ATOM   4350  C  CA    . LYS A 1 542 ? 142.444 138.465 75.498  1.00 41.73 ?  542 LYS A CA    1 
ATOM   4351  C  C     . LYS A 1 542 ? 141.903 139.400 76.574  1.00 43.05 ?  542 LYS A C     1 
ATOM   4352  O  O     . LYS A 1 542 ? 140.751 139.843 76.502  1.00 41.93 ?  542 LYS A O     1 
ATOM   4353  C  CB    . LYS A 1 542 ? 142.424 137.016 75.984  1.00 40.93 ?  542 LYS A CB    1 
ATOM   4354  C  CG    . LYS A 1 542 ? 141.042 136.477 76.295  1.00 43.00 ?  542 LYS A CG    1 
ATOM   4355  C  CD    . LYS A 1 542 ? 141.113 135.032 76.758  1.00 39.38 ?  542 LYS A CD    1 
ATOM   4356  C  CE    . LYS A 1 542 ? 139.729 134.432 76.914  1.00 41.15 ?  542 LYS A CE    1 
ATOM   4357  N  NZ    . LYS A 1 542 ? 139.790 132.978 77.226  1.00 42.60 1  542 LYS A NZ    1 
ATOM   4358  N  N     . ILE A 1 543 ? 142.729 139.728 77.568  1.00 38.22 ?  543 ILE A N     1 
ATOM   4359  C  CA    . ILE A 1 543 ? 142.284 140.623 78.632  1.00 36.34 ?  543 ILE A CA    1 
ATOM   4360  C  C     . ILE A 1 543 ? 142.071 142.032 78.088  1.00 38.94 ?  543 ILE A C     1 
ATOM   4361  O  O     . ILE A 1 543 ? 141.125 142.729 78.480  1.00 41.41 ?  543 ILE A O     1 
ATOM   4362  C  CB    . ILE A 1 543 ? 143.287 140.606 79.799  1.00 35.88 ?  543 ILE A CB    1 
ATOM   4363  C  CG1   . ILE A 1 543 ? 143.426 139.199 80.387  1.00 39.31 ?  543 ILE A CG1   1 
ATOM   4364  C  CG2   . ILE A 1 543 ? 142.844 141.561 80.887  1.00 37.77 ?  543 ILE A CG2   1 
ATOM   4365  C  CD1   . ILE A 1 543 ? 142.144 138.391 80.406  1.00 37.09 ?  543 ILE A CD1   1 
ATOM   4366  N  N     . ALA A 1 544 ? 142.941 142.471 77.175  1.00 37.81 ?  544 ALA A N     1 
ATOM   4367  C  CA    . ALA A 1 544 ? 142.769 143.782 76.559  1.00 40.47 ?  544 ALA A CA    1 
ATOM   4368  C  C     . ALA A 1 544 ? 141.466 143.856 75.773  1.00 42.32 ?  544 ALA A C     1 
ATOM   4369  O  O     . ALA A 1 544 ? 140.767 144.874 75.809  1.00 42.94 ?  544 ALA A O     1 
ATOM   4370  C  CB    . ALA A 1 544 ? 143.961 144.098 75.658  1.00 40.60 ?  544 ALA A CB    1 
ATOM   4371  N  N     . ASN A 1 545 ? 141.125 142.785 75.053  1.00 43.74 ?  545 ASN A N     1 
ATOM   4372  C  CA    . ASN A 1 545 ? 139.841 142.739 74.361  1.00 44.64 ?  545 ASN A CA    1 
ATOM   4373  C  C     . ASN A 1 545 ? 138.681 142.700 75.346  1.00 44.81 ?  545 ASN A C     1 
ATOM   4374  O  O     . ASN A 1 545 ? 137.601 143.227 75.053  1.00 47.71 ?  545 ASN A O     1 
ATOM   4375  C  CB    . ASN A 1 545 ? 139.787 141.531 73.426  1.00 44.57 ?  545 ASN A CB    1 
ATOM   4376  C  CG    . ASN A 1 545 ? 140.871 141.564 72.370  1.00 47.93 ?  545 ASN A CG    1 
ATOM   4377  O  OD1   . ASN A 1 545 ? 141.386 142.628 72.027  1.00 47.94 ?  545 ASN A OD1   1 
ATOM   4378  N  ND2   . ASN A 1 545 ? 141.227 140.395 71.850  1.00 47.29 ?  545 ASN A ND2   1 
ATOM   4379  N  N     . LEU A 1 546 ? 138.878 142.072 76.507  1.00 40.52 ?  546 LEU A N     1 
ATOM   4380  C  CA    . LEU A 1 546 ? 137.864 142.127 77.555  1.00 38.34 ?  546 LEU A CA    1 
ATOM   4381  C  C     . LEU A 1 546 ? 137.634 143.559 78.018  1.00 38.77 ?  546 LEU A C     1 
ATOM   4382  O  O     . LEU A 1 546 ? 136.491 143.968 78.258  1.00 40.95 ?  546 LEU A O     1 
ATOM   4383  C  CB    . LEU A 1 546 ? 138.274 141.246 78.734  1.00 35.29 ?  546 LEU A CB    1 
ATOM   4384  C  CG    . LEU A 1 546 ? 138.131 139.737 78.550  1.00 38.57 ?  546 LEU A CG    1 
ATOM   4385  C  CD1   . LEU A 1 546 ? 138.461 139.026 79.848  1.00 36.37 ?  546 LEU A CD1   1 
ATOM   4386  C  CD2   . LEU A 1 546 ? 136.730 139.387 78.084  1.00 34.75 ?  546 LEU A CD2   1 
ATOM   4387  N  N     . PHE A 1 547 ? 138.706 144.338 78.146  1.00 37.80 ?  547 PHE A N     1 
ATOM   4388  C  CA    . PHE A 1 547 ? 138.613 145.728 78.571  1.00 36.82 ?  547 PHE A CA    1 
ATOM   4389  C  C     . PHE A 1 547 ? 138.312 146.682 77.423  1.00 37.34 ?  547 PHE A C     1 
ATOM   4390  O  O     . PHE A 1 547 ? 138.382 147.900 77.615  1.00 38.01 ?  547 PHE A O     1 
ATOM   4391  C  CB    . PHE A 1 547 ? 139.906 146.155 79.269  1.00 35.38 ?  547 PHE A CB    1 
ATOM   4392  C  CG    . PHE A 1 547 ? 140.010 145.685 80.687  1.00 35.44 ?  547 PHE A CG    1 
ATOM   4393  C  CD1   . PHE A 1 547 ? 139.394 146.385 81.708  1.00 34.89 ?  547 PHE A CD1   1 
ATOM   4394  C  CD2   . PHE A 1 547 ? 140.724 144.543 81.000  1.00 32.16 ?  547 PHE A CD2   1 
ATOM   4395  C  CE1   . PHE A 1 547 ? 139.488 145.954 83.016  1.00 31.83 ?  547 PHE A CE1   1 
ATOM   4396  C  CE2   . PHE A 1 547 ? 140.821 144.108 82.305  1.00 34.52 ?  547 PHE A CE2   1 
ATOM   4397  C  CZ    . PHE A 1 547 ? 140.201 144.814 83.313  1.00 33.71 ?  547 PHE A CZ    1 
ATOM   4398  N  N     . GLU A 1 548 ? 137.987 146.164 76.241  1.00 43.65 ?  548 GLU A N     1 
ATOM   4399  C  CA    . GLU A 1 548 ? 137.682 147.025 75.106  1.00 46.68 ?  548 GLU A CA    1 
ATOM   4400  C  C     . GLU A 1 548 ? 136.440 147.863 75.384  1.00 47.86 ?  548 GLU A C     1 
ATOM   4401  O  O     . GLU A 1 548 ? 135.477 147.394 75.997  1.00 47.21 ?  548 GLU A O     1 
ATOM   4402  C  CB    . GLU A 1 548 ? 137.481 146.188 73.842  1.00 45.30 ?  548 GLU A CB    1 
ATOM   4403  C  CG    . GLU A 1 548 ? 138.206 146.731 72.623  1.00 46.87 ?  548 GLU A CG    1 
ATOM   4404  C  CD    . GLU A 1 548 ? 139.711 146.719 72.790  1.00 49.11 ?  548 GLU A CD    1 
ATOM   4405  O  OE1   . GLU A 1 548 ? 140.328 145.658 72.559  1.00 48.26 ?  548 GLU A OE1   1 
ATOM   4406  O  OE2   . GLU A 1 548 ? 140.279 147.771 73.154  1.00 47.53 -1 548 GLU A OE2   1 
ATOM   4407  N  N     . GLY A 1 549 ? 136.468 149.112 74.925  1.00 44.32 ?  549 GLY A N     1 
ATOM   4408  C  CA    . GLY A 1 549 ? 135.396 150.048 75.175  1.00 40.96 ?  549 GLY A CA    1 
ATOM   4409  C  C     . GLY A 1 549 ? 135.507 150.812 76.475  1.00 43.69 ?  549 GLY A C     1 
ATOM   4410  O  O     . GLY A 1 549 ? 134.636 151.644 76.761  1.00 44.76 ?  549 GLY A O     1 
ATOM   4411  N  N     . MET A 1 550 ? 136.545 150.558 77.269  1.00 43.09 ?  550 MET A N     1 
ATOM   4412  C  CA    . MET A 1 550 ? 136.747 151.217 78.551  1.00 40.92 ?  550 MET A CA    1 
ATOM   4413  C  C     . MET A 1 550 ? 138.149 151.801 78.589  1.00 41.67 ?  550 MET A C     1 
ATOM   4414  O  O     . MET A 1 550 ? 139.112 151.131 78.200  1.00 42.25 ?  550 MET A O     1 
ATOM   4415  C  CB    . MET A 1 550 ? 136.559 150.237 79.711  1.00 38.56 ?  550 MET A CB    1 
ATOM   4416  C  CG    . MET A 1 550 ? 135.296 150.451 80.514  1.00 42.56 ?  550 MET A CG    1 
ATOM   4417  S  SD    . MET A 1 550 ? 135.169 149.258 81.852  1.00 55.69 ?  550 MET A SD    1 
ATOM   4418  C  CE    . MET A 1 550 ? 135.253 147.720 80.939  1.00 41.52 ?  550 MET A CE    1 
ATOM   4419  N  N     . HIS A 1 551 ? 138.267 153.040 79.058  1.00 38.98 ?  551 HIS A N     1 
ATOM   4420  C  CA    . HIS A 1 551 ? 139.574 153.672 79.166  1.00 38.16 ?  551 HIS A CA    1 
ATOM   4421  C  C     . HIS A 1 551 ? 140.330 153.092 80.355  1.00 38.90 ?  551 HIS A C     1 
ATOM   4422  O  O     . HIS A 1 551 ? 139.849 153.141 81.491  1.00 40.01 ?  551 HIS A O     1 
ATOM   4423  C  CB    . HIS A 1 551 ? 139.426 155.184 79.309  1.00 39.46 ?  551 HIS A CB    1 
ATOM   4424  C  CG    . HIS A 1 551 ? 140.710 155.887 79.620  1.00 41.61 ?  551 HIS A CG    1 
ATOM   4425  N  ND1   . HIS A 1 551 ? 141.801 155.850 78.778  1.00 42.78 ?  551 HIS A ND1   1 
ATOM   4426  C  CD2   . HIS A 1 551 ? 141.080 156.643 80.681  1.00 42.39 ?  551 HIS A CD2   1 
ATOM   4427  C  CE1   . HIS A 1 551 ? 142.786 156.554 79.305  1.00 40.85 ?  551 HIS A CE1   1 
ATOM   4428  N  NE2   . HIS A 1 551 ? 142.375 157.045 80.460  1.00 41.74 ?  551 HIS A NE2   1 
ATOM   4429  N  N     . ILE A 1 552 ? 141.509 152.542 80.091  1.00 35.62 ?  552 ILE A N     1 
ATOM   4430  C  CA    . ILE A 1 552 ? 142.356 151.963 81.129  1.00 31.64 ?  552 ILE A CA    1 
ATOM   4431  C  C     . ILE A 1 552 ? 143.326 153.044 81.598  1.00 33.24 ?  552 ILE A C     1 
ATOM   4432  O  O     . ILE A 1 552 ? 144.105 153.554 80.778  1.00 36.10 ?  552 ILE A O     1 
ATOM   4433  C  CB    . ILE A 1 552 ? 143.111 150.733 80.615  1.00 33.70 ?  552 ILE A CB    1 
ATOM   4434  C  CG1   . ILE A 1 552 ? 142.122 149.630 80.233  1.00 32.99 ?  552 ILE A CG1   1 
ATOM   4435  C  CG2   . ILE A 1 552 ? 144.097 150.236 81.655  1.00 34.38 ?  552 ILE A CG2   1 
ATOM   4436  C  CD1   . ILE A 1 552 ? 142.759 148.465 79.519  1.00 34.55 ?  552 ILE A CD1   1 
ATOM   4437  N  N     . PRO A 1 553 ? 143.304 153.427 82.874  1.00 38.28 ?  553 PRO A N     1 
ATOM   4438  C  CA    . PRO A 1 553 ? 144.197 154.496 83.341  1.00 32.24 ?  553 PRO A CA    1 
ATOM   4439  C  C     . PRO A 1 553 ? 145.661 154.123 83.152  1.00 35.19 ?  553 PRO A C     1 
ATOM   4440  O  O     . PRO A 1 553 ? 146.096 153.030 83.521  1.00 36.48 ?  553 PRO A O     1 
ATOM   4441  C  CB    . PRO A 1 553 ? 143.835 154.636 84.824  1.00 31.02 ?  553 PRO A CB    1 
ATOM   4442  C  CG    . PRO A 1 553 ? 142.451 154.079 84.929  1.00 30.52 ?  553 PRO A CG    1 
ATOM   4443  C  CD    . PRO A 1 553 ? 142.391 152.967 83.931  1.00 32.28 ?  553 PRO A CD    1 
ATOM   4444  N  N     . THR A 1 554 ? 146.419 155.046 82.574  1.00 39.01 ?  554 THR A N     1 
ATOM   4445  C  CA    . THR A 1 554 ? 147.834 154.862 82.316  1.00 38.97 ?  554 THR A CA    1 
ATOM   4446  C  C     . THR A 1 554 ? 148.649 155.518 83.427  1.00 37.81 ?  554 THR A C     1 
ATOM   4447  O  O     . THR A 1 554 ? 148.111 155.969 84.443  1.00 39.91 ?  554 THR A O     1 
ATOM   4448  C  CB    . THR A 1 554 ? 148.196 155.428 80.941  1.00 37.93 ?  554 THR A CB    1 
ATOM   4449  O  OG1   . THR A 1 554 ? 148.064 156.854 80.960  1.00 40.49 ?  554 THR A OG1   1 
ATOM   4450  C  CG2   . THR A 1 554 ? 147.279 154.855 79.872  1.00 35.01 ?  554 THR A CG2   1 
ATOM   4451  N  N     . THR A 1 555 ? 149.969 155.572 83.239  1.00 38.74 ?  555 THR A N     1 
ATOM   4452  C  CA    . THR A 1 555 ? 150.822 156.242 84.214  1.00 36.20 ?  555 THR A CA    1 
ATOM   4453  C  C     . THR A 1 555 ? 150.592 157.746 84.220  1.00 38.34 ?  555 THR A C     1 
ATOM   4454  O  O     . THR A 1 555 ? 150.680 158.379 85.276  1.00 40.28 ?  555 THR A O     1 
ATOM   4455  C  CB    . THR A 1 555 ? 152.292 155.931 83.935  1.00 38.61 ?  555 THR A CB    1 
ATOM   4456  O  OG1   . THR A 1 555 ? 152.564 156.100 82.537  1.00 41.79 ?  555 THR A OG1   1 
ATOM   4457  C  CG2   . THR A 1 555 ? 152.620 154.502 84.343  1.00 37.28 ?  555 THR A CG2   1 
ATOM   4458  N  N     . GLU A 1 556 ? 150.302 158.338 83.058  1.00 39.91 ?  556 GLU A N     1 
ATOM   4459  C  CA    . GLU A 1 556 ? 149.984 159.761 83.012  1.00 39.82 ?  556 GLU A CA    1 
ATOM   4460  C  C     . GLU A 1 556 ? 148.672 160.056 83.731  1.00 38.55 ?  556 GLU A C     1 
ATOM   4461  O  O     . GLU A 1 556 ? 148.559 161.059 84.447  1.00 40.13 ?  556 GLU A O     1 
ATOM   4462  C  CB    . GLU A 1 556 ? 149.923 160.238 81.561  1.00 40.74 ?  556 GLU A CB    1 
ATOM   4463  C  CG    . GLU A 1 556 ? 149.877 161.748 81.408  1.00 43.25 ?  556 GLU A CG    1 
ATOM   4464  C  CD    . GLU A 1 556 ? 151.060 162.436 82.060  1.00 44.78 ?  556 GLU A CD    1 
ATOM   4465  O  OE1   . GLU A 1 556 ? 152.191 161.915 81.947  1.00 41.96 ?  556 GLU A OE1   1 
ATOM   4466  O  OE2   . GLU A 1 556 ? 150.861 163.497 82.688  1.00 44.90 -1 556 GLU A OE2   1 
ATOM   4467  N  N     . ASP A 1 557 ? 147.669 159.196 83.546  1.00 40.02 ?  557 ASP A N     1 
ATOM   4468  C  CA    . ASP A 1 557 ? 146.413 159.358 84.268  1.00 36.22 ?  557 ASP A CA    1 
ATOM   4469  C  C     . ASP A 1 557 ? 146.627 159.234 85.770  1.00 36.15 ?  557 ASP A C     1 
ATOM   4470  O  O     . ASP A 1 557 ? 146.024 159.972 86.556  1.00 37.41 ?  557 ASP A O     1 
ATOM   4471  C  CB    . ASP A 1 557 ? 145.391 158.330 83.783  1.00 35.10 ?  557 ASP A CB    1 
ATOM   4472  C  CG    . ASP A 1 557 ? 144.763 158.715 82.460  1.00 40.32 ?  557 ASP A CG    1 
ATOM   4473  O  OD1   . ASP A 1 557 ? 144.588 159.927 82.213  1.00 43.55 ?  557 ASP A OD1   1 
ATOM   4474  O  OD2   . ASP A 1 557 ? 144.447 157.806 81.664  1.00 42.22 -1 557 ASP A OD2   1 
ATOM   4475  N  N     . TRP A 1 558 ? 147.489 158.304 86.188  1.00 29.19 ?  558 TRP A N     1 
ATOM   4476  C  CA    . TRP A 1 558 ? 147.791 158.167 87.607  1.00 27.33 ?  558 TRP A CA    1 
ATOM   4477  C  C     . TRP A 1 558 ? 148.553 159.372 88.142  1.00 29.30 ?  558 TRP A C     1 
ATOM   4478  O  O     . TRP A 1 558 ? 148.343 159.770 89.291  1.00 33.21 ?  558 TRP A O     1 
ATOM   4479  C  CB    . TRP A 1 558 ? 148.576 156.882 87.853  1.00 29.55 ?  558 TRP A CB    1 
ATOM   4480  C  CG    . TRP A 1 558 ? 147.704 155.694 88.105  1.00 27.37 ?  558 TRP A CG    1 
ATOM   4481  C  CD1   . TRP A 1 558 ? 147.463 154.658 87.253  1.00 27.28 ?  558 TRP A CD1   1 
ATOM   4482  C  CD2   . TRP A 1 558 ? 146.956 155.418 89.295  1.00 28.16 ?  558 TRP A CD2   1 
ATOM   4483  N  NE1   . TRP A 1 558 ? 146.613 153.752 87.838  1.00 30.85 ?  558 TRP A NE1   1 
ATOM   4484  C  CE2   . TRP A 1 558 ? 146.289 154.194 89.093  1.00 28.47 ?  558 TRP A CE2   1 
ATOM   4485  C  CE3   . TRP A 1 558 ? 146.791 156.082 90.513  1.00 30.88 ?  558 TRP A CE3   1 
ATOM   4486  C  CZ2   . TRP A 1 558 ? 145.469 153.624 90.062  1.00 26.24 ?  558 TRP A CZ2   1 
ATOM   4487  C  CZ3   . TRP A 1 558 ? 145.976 155.515 91.474  1.00 26.03 ?  558 TRP A CZ3   1 
ATOM   4488  C  CH2   . TRP A 1 558 ? 145.326 154.299 91.242  1.00 22.82 ?  558 TRP A CH2   1 
ATOM   4489  N  N     . LYS A 1 559 ? 149.437 159.964 87.335  1.00 36.33 ?  559 LYS A N     1 
ATOM   4490  C  CA    . LYS A 1 559 ? 150.112 161.190 87.751  1.00 32.59 ?  559 LYS A CA    1 
ATOM   4491  C  C     . LYS A 1 559 ? 149.117 162.333 87.916  1.00 31.12 ?  559 LYS A C     1 
ATOM   4492  O  O     . LYS A 1 559 ? 149.204 163.114 88.872  1.00 34.31 ?  559 LYS A O     1 
ATOM   4493  C  CB    . LYS A 1 559 ? 151.189 161.567 86.735  1.00 36.36 ?  559 LYS A CB    1 
ATOM   4494  C  CG    . LYS A 1 559 ? 152.511 160.847 86.925  1.00 38.00 ?  559 LYS A CG    1 
ATOM   4495  C  CD    . LYS A 1 559 ? 153.213 160.637 85.595  1.00 39.16 ?  559 LYS A CD    1 
ATOM   4496  C  CE    . LYS A 1 559 ? 154.401 159.703 85.735  1.00 37.84 ?  559 LYS A CE    1 
ATOM   4497  N  NZ    . LYS A 1 559 ? 155.509 160.077 84.815  1.00 39.17 1  559 LYS A NZ    1 
ATOM   4498  N  N     . LYS A 1 560 ? 148.165 162.444 86.988  1.00 33.31 ?  560 LYS A N     1 
ATOM   4499  C  CA    . LYS A 1 560 ? 147.127 163.462 87.108  1.00 32.75 ?  560 LYS A CA    1 
ATOM   4500  C  C     . LYS A 1 560 ? 146.277 163.235 88.352  1.00 36.91 ?  560 LYS A C     1 
ATOM   4501  O  O     . LYS A 1 560 ? 145.922 164.189 89.051  1.00 36.57 ?  560 LYS A O     1 
ATOM   4502  C  CB    . LYS A 1 560 ? 146.252 163.473 85.856  1.00 32.44 ?  560 LYS A CB    1 
ATOM   4503  C  CG    . LYS A 1 560 ? 146.966 163.944 84.602  1.00 37.98 ?  560 LYS A CG    1 
ATOM   4504  C  CD    . LYS A 1 560 ? 146.072 163.814 83.381  1.00 38.81 ?  560 LYS A CD    1 
ATOM   4505  C  CE    . LYS A 1 560 ? 146.860 163.996 82.096  1.00 35.97 ?  560 LYS A CE    1 
ATOM   4506  N  NZ    . LYS A 1 560 ? 146.111 163.492 80.914  1.00 38.72 1  560 LYS A NZ    1 
ATOM   4507  N  N     . LEU A 1 561 ? 145.941 161.976 88.642  1.00 35.84 ?  561 LEU A N     1 
ATOM   4508  C  CA    . LEU A 1 561 ? 145.183 161.669 89.851  1.00 28.48 ?  561 LEU A CA    1 
ATOM   4509  C  C     . LEU A 1 561 ? 145.986 161.992 91.106  1.00 28.17 ?  561 LEU A C     1 
ATOM   4510  O  O     . LEU A 1 561 ? 145.430 162.472 92.098  1.00 30.26 ?  561 LEU A O     1 
ATOM   4511  C  CB    . LEU A 1 561 ? 144.758 160.202 89.850  1.00 28.29 ?  561 LEU A CB    1 
ATOM   4512  C  CG    . LEU A 1 561 ? 143.926 159.774 91.061  1.00 29.77 ?  561 LEU A CG    1 
ATOM   4513  C  CD1   . LEU A 1 561 ? 142.684 160.638 91.175  1.00 26.57 ?  561 LEU A CD1   1 
ATOM   4514  C  CD2   . LEU A 1 561 ? 143.553 158.306 90.980  1.00 24.71 ?  561 LEU A CD2   1 
ATOM   4515  N  N     . LYS A 1 562 ? 147.292 161.720 91.085  1.00 29.68 ?  562 LYS A N     1 
ATOM   4516  C  CA    . LYS A 1 562 ? 148.145 162.063 92.218  1.00 30.82 ?  562 LYS A CA    1 
ATOM   4517  C  C     . LYS A 1 562 ? 148.175 163.568 92.448  1.00 35.47 ?  562 LYS A C     1 
ATOM   4518  O  O     . LYS A 1 562 ? 148.083 164.032 93.590  1.00 35.60 ?  562 LYS A O     1 
ATOM   4519  C  CB    . LYS A 1 562 ? 149.556 161.524 91.984  1.00 28.95 ?  562 LYS A CB    1 
ATOM   4520  C  CG    . LYS A 1 562 ? 150.584 161.964 93.007  1.00 29.87 ?  562 LYS A CG    1 
ATOM   4521  C  CD    . LYS A 1 562 ? 151.982 161.569 92.564  1.00 30.17 ?  562 LYS A CD    1 
ATOM   4522  C  CE    . LYS A 1 562 ? 153.029 161.977 93.583  1.00 32.22 ?  562 LYS A CE    1 
ATOM   4523  N  NZ    . LYS A 1 562 ? 154.291 161.211 93.405  1.00 34.97 1  562 LYS A NZ    1 
ATOM   4524  N  N     . ALA A 1 563 ? 148.293 164.346 91.370  1.00 34.18 ?  563 ALA A N     1 
ATOM   4525  C  CA    . ALA A 1 563 ? 148.254 165.800 91.501  1.00 31.91 ?  563 ALA A CA    1 
ATOM   4526  C  C     . ALA A 1 563 ? 146.897 166.272 92.013  1.00 31.32 ?  563 ALA A C     1 
ATOM   4527  O  O     . ALA A 1 563 ? 146.820 167.190 92.839  1.00 37.17 ?  563 ALA A O     1 
ATOM   4528  C  CB    . ALA A 1 563 ? 148.583 166.457 90.161  1.00 33.30 ?  563 ALA A CB    1 
ATOM   4529  N  N     . PHE A 1 564 ? 145.816 165.655 91.530  1.00 33.10 ?  564 PHE A N     1 
ATOM   4530  C  CA    . PHE A 1 564 ? 144.479 166.016 91.987  1.00 30.55 ?  564 PHE A CA    1 
ATOM   4531  C  C     . PHE A 1 564 ? 144.306 165.729 93.473  1.00 31.17 ?  564 PHE A C     1 
ATOM   4532  O  O     . PHE A 1 564 ? 143.706 166.526 94.202  1.00 35.80 ?  564 PHE A O     1 
ATOM   4533  C  CB    . PHE A 1 564 ? 143.436 165.260 91.163  1.00 30.41 ?  564 PHE A CB    1 
ATOM   4534  C  CG    . PHE A 1 564 ? 142.043 165.799 91.298  1.00 30.40 ?  564 PHE A CG    1 
ATOM   4535  C  CD1   . PHE A 1 564 ? 141.613 166.852 90.509  1.00 32.82 ?  564 PHE A CD1   1 
ATOM   4536  C  CD2   . PHE A 1 564 ? 141.155 165.243 92.202  1.00 33.53 ?  564 PHE A CD2   1 
ATOM   4537  C  CE1   . PHE A 1 564 ? 140.329 167.345 90.628  1.00 38.30 ?  564 PHE A CE1   1 
ATOM   4538  C  CE2   . PHE A 1 564 ? 139.871 165.732 92.326  1.00 34.07 ?  564 PHE A CE2   1 
ATOM   4539  C  CZ    . PHE A 1 564 ? 139.457 166.784 91.538  1.00 36.68 ?  564 PHE A CZ    1 
ATOM   4540  N  N     . VAL A 1 565 ? 144.820 164.589 93.937  1.00 32.53 ?  565 VAL A N     1 
ATOM   4541  C  CA    . VAL A 1 565 ? 144.743 164.252 95.355  1.00 27.22 ?  565 VAL A CA    1 
ATOM   4542  C  C     . VAL A 1 565 ? 145.595 165.210 96.178  1.00 31.96 ?  565 VAL A C     1 
ATOM   4543  O  O     . VAL A 1 565 ? 145.204 165.622 97.276  1.00 36.49 ?  565 VAL A O     1 
ATOM   4544  C  CB    . VAL A 1 565 ? 145.159 162.785 95.573  1.00 26.89 ?  565 VAL A CB    1 
ATOM   4545  C  CG1   . VAL A 1 565 ? 145.429 162.509 97.043  1.00 28.44 ?  565 VAL A CG1   1 
ATOM   4546  C  CG2   . VAL A 1 565 ? 144.083 161.856 95.049  1.00 30.95 ?  565 VAL A CG2   1 
ATOM   4547  N  N     . ALA A 1 566 ? 146.766 165.587 95.661  1.00 35.27 ?  566 ALA A N     1 
ATOM   4548  C  CA    . ALA A 1 566 ? 147.606 166.548 96.365  1.00 33.21 ?  566 ALA A CA    1 
ATOM   4549  C  C     . ALA A 1 566 ? 146.906 167.895 96.502  1.00 36.36 ?  566 ALA A C     1 
ATOM   4550  O  O     . ALA A 1 566 ? 146.988 168.543 97.553  1.00 36.75 ?  566 ALA A O     1 
ATOM   4551  C  CB    . ALA A 1 566 ? 148.941 166.708 95.640  1.00 32.08 ?  566 ALA A CB    1 
ATOM   4552  N  N     . GLU A 1 567 ? 146.212 168.333 95.451  1.00 36.78 ?  567 GLU A N     1 
ATOM   4553  C  CA    . GLU A 1 567 ? 145.550 169.633 95.493  1.00 35.42 ?  567 GLU A CA    1 
ATOM   4554  C  C     . GLU A 1 567 ? 144.293 169.605 96.359  1.00 38.61 ?  567 GLU A C     1 
ATOM   4555  O  O     . GLU A 1 567 ? 144.039 170.547 97.117  1.00 41.33 ?  567 GLU A O     1 
ATOM   4556  C  CB    . GLU A 1 567 ? 145.212 170.096 94.077  1.00 37.27 ?  567 GLU A CB    1 
ATOM   4557  C  CG    . GLU A 1 567 ? 146.222 171.069 93.484  1.00 42.63 ?  567 GLU A CG    1 
ATOM   4558  C  CD    . GLU A 1 567 ? 147.590 170.447 93.287  1.00 45.29 ?  567 GLU A CD    1 
ATOM   4559  O  OE1   . GLU A 1 567 ? 148.480 170.682 94.131  1.00 42.73 ?  567 GLU A OE1   1 
ATOM   4560  O  OE2   . GLU A 1 567 ? 147.780 169.731 92.281  1.00 42.47 -1 567 GLU A OE2   1 
ATOM   4561  N  N     . HIS A 1 568 ? 143.498 168.537 96.266  1.00 39.00 ?  568 HIS A N     1 
ATOM   4562  C  CA    . HIS A 1 568 ? 142.175 168.512 96.873  1.00 36.41 ?  568 HIS A CA    1 
ATOM   4563  C  C     . HIS A 1 568 ? 142.044 167.568 98.060  1.00 35.41 ?  568 HIS A C     1 
ATOM   4564  O  O     . HIS A 1 568 ? 141.069 167.680 98.808  1.00 41.18 ?  568 HIS A O     1 
ATOM   4565  C  CB    . HIS A 1 568 ? 141.123 168.134 95.820  1.00 33.87 ?  568 HIS A CB    1 
ATOM   4566  C  CG    . HIS A 1 568 ? 140.909 169.185 94.777  1.00 38.50 ?  568 HIS A CG    1 
ATOM   4567  N  ND1   . HIS A 1 568 ? 140.555 170.480 95.088  1.00 36.84 ?  568 HIS A ND1   1 
ATOM   4568  C  CD2   . HIS A 1 568 ? 141.003 169.135 93.427  1.00 37.26 ?  568 HIS A CD2   1 
ATOM   4569  C  CE1   . HIS A 1 568 ? 140.438 171.182 93.975  1.00 40.24 ?  568 HIS A CE1   1 
ATOM   4570  N  NE2   . HIS A 1 568 ? 140.704 170.390 92.953  1.00 40.01 ?  568 HIS A NE2   1 
ATOM   4571  N  N     . GLY A 1 569 ? 142.984 166.653 98.258  1.00 28.17 ?  569 GLY A N     1 
ATOM   4572  C  CA    . GLY A 1 569 ? 142.867 165.701 99.339  1.00 28.04 ?  569 GLY A CA    1 
ATOM   4573  C  C     . GLY A 1 569 ? 142.009 164.506 98.969  1.00 28.41 ?  569 GLY A C     1 
ATOM   4574  O  O     . GLY A 1 569 ? 141.591 164.322 97.824  1.00 34.15 ?  569 GLY A O     1 
ATOM   4575  N  N     . MET A 1 570 ? 141.750 163.675 99.974  1.00 25.27 ?  570 MET A N     1 
ATOM   4576  C  CA    . MET A 1 570 ? 140.943 162.473 99.811  1.00 25.78 ?  570 MET A CA    1 
ATOM   4577  C  C     . MET A 1 570 ? 139.940 162.397 100.951 1.00 24.58 ?  570 MET A C     1 
ATOM   4578  O  O     . MET A 1 570 ? 140.311 162.549 102.118 1.00 27.32 ?  570 MET A O     1 
ATOM   4579  C  CB    . MET A 1 570 ? 141.823 161.219 99.777  1.00 24.02 ?  570 MET A CB    1 
ATOM   4580  C  CG    . MET A 1 570 ? 142.346 160.877 98.390  1.00 20.26 ?  570 MET A CG    1 
ATOM   4581  S  SD    . MET A 1 570 ? 142.725 159.131 98.170  1.00 39.13 ?  570 MET A SD    1 
ATOM   4582  C  CE    . MET A 1 570 ? 141.639 158.390 99.379  1.00 25.71 ?  570 MET A CE    1 
ATOM   4583  N  N     . TYR A 1 571 ? 138.672 162.164 100.610 1.00 21.91 ?  571 TYR A N     1 
ATOM   4584  C  CA    . TYR A 1 571 ? 137.615 162.176 101.615 1.00 14.14 ?  571 TYR A CA    1 
ATOM   4585  C  C     . TYR A 1 571 ? 137.630 160.935 102.497 1.00 20.21 ?  571 TYR A C     1 
ATOM   4586  O  O     . TYR A 1 571 ? 137.334 161.030 103.692 1.00 24.53 ?  571 TYR A O     1 
ATOM   4587  C  CB    . TYR A 1 571 ? 136.250 162.314 100.941 1.00 22.96 ?  571 TYR A CB    1 
ATOM   4588  C  CG    . TYR A 1 571 ? 135.119 162.571 101.909 1.00 24.15 ?  571 TYR A CG    1 
ATOM   4589  C  CD1   . TYR A 1 571 ? 134.909 163.836 102.439 1.00 23.12 ?  571 TYR A CD1   1 
ATOM   4590  C  CD2   . TYR A 1 571 ? 134.265 161.547 102.297 1.00 18.53 ?  571 TYR A CD2   1 
ATOM   4591  C  CE1   . TYR A 1 571 ? 133.879 164.075 103.324 1.00 22.43 ?  571 TYR A CE1   1 
ATOM   4592  C  CE2   . TYR A 1 571 ? 133.234 161.778 103.183 1.00 19.81 ?  571 TYR A CE2   1 
ATOM   4593  C  CZ    . TYR A 1 571 ? 133.044 163.043 103.692 1.00 25.46 ?  571 TYR A CZ    1 
ATOM   4594  O  OH    . TYR A 1 571 ? 132.017 163.280 104.575 1.00 28.14 ?  571 TYR A OH    1 
ATOM   4595  N  N     . HIS A 1 572 ? 137.966 159.776 101.940 1.00 22.73 ?  572 HIS A N     1 
ATOM   4596  C  CA    . HIS A 1 572 ? 137.923 158.517 102.672 1.00 13.70 ?  572 HIS A CA    1 
ATOM   4597  C  C     . HIS A 1 572 ? 139.331 158.086 103.050 1.00 10.41 ?  572 HIS A C     1 
ATOM   4598  O  O     . HIS A 1 572 ? 140.230 158.074 102.205 1.00 22.35 ?  572 HIS A O     1 
ATOM   4599  C  CB    . HIS A 1 572 ? 137.250 157.422 101.842 1.00 14.68 ?  572 HIS A CB    1 
ATOM   4600  C  CG    . HIS A 1 572 ? 135.944 157.834 101.240 1.00 15.57 ?  572 HIS A CG    1 
ATOM   4601  N  ND1   . HIS A 1 572 ? 135.846 158.387 99.982  1.00 16.85 ?  572 HIS A ND1   1 
ATOM   4602  C  CD2   . HIS A 1 572 ? 134.679 157.770 101.721 1.00 9.72  ?  572 HIS A CD2   1 
ATOM   4603  C  CE1   . HIS A 1 572 ? 134.580 158.648 99.715  1.00 16.23 ?  572 HIS A CE1   1 
ATOM   4604  N  NE2   . HIS A 1 572 ? 133.851 158.284 100.754 1.00 23.78 ?  572 HIS A NE2   1 
ATOM   4605  N  N     . SER A 1 573 ? 139.519 157.741 104.325 1.00 5.57  ?  573 SER A N     1 
ATOM   4606  C  CA    . SER A 1 573 ? 140.787 157.159 104.747 1.00 7.60  ?  573 SER A CA    1 
ATOM   4607  C  C     . SER A 1 573 ? 141.006 155.800 104.099 1.00 11.79 ?  573 SER A C     1 
ATOM   4608  O  O     . SER A 1 573 ? 142.133 155.456 103.723 1.00 19.77 ?  573 SER A O     1 
ATOM   4609  C  CB    . SER A 1 573 ? 140.828 157.043 106.269 1.00 15.52 ?  573 SER A CB    1 
ATOM   4610  O  OG    . SER A 1 573 ? 139.714 156.314 106.745 1.00 22.99 ?  573 SER A OG    1 
ATOM   4611  N  N     . TYR A 1 574 ? 139.941 155.012 103.968 1.00 12.39 ?  574 TYR A N     1 
ATOM   4612  C  CA    . TYR A 1 574 ? 139.990 153.713 103.316 1.00 1.15  ?  574 TYR A CA    1 
ATOM   4613  C  C     . TYR A 1 574 ? 138.789 153.591 102.394 1.00 8.90  ?  574 TYR A C     1 
ATOM   4614  O  O     . TYR A 1 574 ? 137.701 154.077 102.716 1.00 16.56 ?  574 TYR A O     1 
ATOM   4615  C  CB    . TYR A 1 574 ? 140.007 152.576 104.343 1.00 11.68 ?  574 TYR A CB    1 
ATOM   4616  C  CG    . TYR A 1 574 ? 141.105 152.725 105.370 1.00 8.23  ?  574 TYR A CG    1 
ATOM   4617  C  CD1   . TYR A 1 574 ? 140.902 153.466 106.525 1.00 10.27 ?  574 TYR A CD1   1 
ATOM   4618  C  CD2   . TYR A 1 574 ? 142.346 152.134 105.180 1.00 8.46  ?  574 TYR A CD2   1 
ATOM   4619  C  CE1   . TYR A 1 574 ? 141.899 153.617 107.459 1.00 6.62  ?  574 TYR A CE1   1 
ATOM   4620  C  CE2   . TYR A 1 574 ? 143.350 152.277 106.114 1.00 11.12 ?  574 TYR A CE2   1 
ATOM   4621  C  CZ    . TYR A 1 574 ? 143.120 153.019 107.252 1.00 5.82  ?  574 TYR A CZ    1 
ATOM   4622  O  OH    . TYR A 1 574 ? 144.114 153.165 108.188 1.00 18.04 ?  574 TYR A OH    1 
ATOM   4623  N  N     . ARG A 1 575 ? 138.989 152.950 101.248 1.00 11.09 ?  575 ARG A N     1 
ATOM   4624  C  CA    . ARG A 1 575 ? 137.962 152.882 100.217 1.00 4.65  ?  575 ARG A CA    1 
ATOM   4625  C  C     . ARG A 1 575 ? 137.579 151.466 99.825  1.00 9.69  ?  575 ARG A C     1 
ATOM   4626  O  O     . ARG A 1 575 ? 136.395 151.190 99.622  1.00 19.78 ?  575 ARG A O     1 
ATOM   4627  C  CB    . ARG A 1 575 ? 138.428 153.633 98.963  1.00 17.10 ?  575 ARG A CB    1 
ATOM   4628  C  CG    . ARG A 1 575 ? 138.676 155.112 99.169  1.00 11.51 ?  575 ARG A CG    1 
ATOM   4629  C  CD    . ARG A 1 575 ? 139.681 155.627 98.155  1.00 11.59 ?  575 ARG A CD    1 
ATOM   4630  N  NE    . ARG A 1 575 ? 141.018 155.104 98.409  1.00 16.30 ?  575 ARG A NE    1 
ATOM   4631  C  CZ    . ARG A 1 575 ? 141.586 154.126 97.716  1.00 14.92 ?  575 ARG A CZ    1 
ATOM   4632  N  NH1   . ARG A 1 575 ? 140.964 153.545 96.705  1.00 12.79 1  575 ARG A NH1   1 
ATOM   4633  N  NH2   . ARG A 1 575 ? 142.809 153.724 98.046  1.00 14.91 ?  575 ARG A NH2   1 
ATOM   4634  N  N     . LEU A 1 576 ? 138.545 150.559 99.709  1.00 19.64 ?  576 LEU A N     1 
ATOM   4635  C  CA    . LEU A 1 576 ? 138.319 149.247 99.122  1.00 12.26 ?  576 LEU A CA    1 
ATOM   4636  C  C     . LEU A 1 576 ? 138.627 148.158 100.136 1.00 3.41  ?  576 LEU A C     1 
ATOM   4637  O  O     . LEU A 1 576 ? 139.707 148.151 100.736 1.00 19.60 ?  576 LEU A O     1 
ATOM   4638  C  CB    . LEU A 1 576 ? 139.184 149.053 97.874  1.00 4.91  ?  576 LEU A CB    1 
ATOM   4639  C  CG    . LEU A 1 576 ? 139.154 150.167 96.827  1.00 8.38  ?  576 LEU A CG    1 
ATOM   4640  C  CD1   . LEU A 1 576 ? 140.204 149.913 95.761  1.00 11.87 ?  576 LEU A CD1   1 
ATOM   4641  C  CD2   . LEU A 1 576 ? 137.776 150.292 96.204  1.00 10.83 ?  576 LEU A CD2   1 
ATOM   4642  N  N     . CYS A 1 577 ? 137.679 147.244 100.325 1.00 1.85  ?  577 CYS A N     1 
ATOM   4643  C  CA    . CYS A 1 577 ? 137.916 146.013 101.066 1.00 6.52  ?  577 CYS A CA    1 
ATOM   4644  C  C     . CYS A 1 577 ? 136.987 144.954 100.497 1.00 16.04 ?  577 CYS A C     1 
ATOM   4645  O  O     . CYS A 1 577 ? 135.810 145.230 100.249 1.00 21.38 ?  577 CYS A O     1 
ATOM   4646  C  CB    . CYS A 1 577 ? 137.691 146.197 102.574 1.00 5.82  ?  577 CYS A CB    1 
ATOM   4647  S  SG    . CYS A 1 577 ? 135.979 146.099 103.151 1.00 27.63 ?  577 CYS A SG    1 
ATOM   4648  N  N     . ILE A 1 578 ? 137.517 143.758 100.271 1.00 8.13  ?  578 ILE A N     1 
ATOM   4649  C  CA    . ILE A 1 578 ? 136.778 142.686 99.615  1.00 11.51 ?  578 ILE A CA    1 
ATOM   4650  C  C     . ILE A 1 578 ? 136.251 141.758 100.703 1.00 8.57  ?  578 ILE A C     1 
ATOM   4651  O  O     . ILE A 1 578 ? 136.992 140.949 101.264 1.00 10.89 ?  578 ILE A O     1 
ATOM   4652  C  CB    . ILE A 1 578 ? 137.644 141.943 98.595  1.00 12.84 ?  578 ILE A CB    1 
ATOM   4653  C  CG1   . ILE A 1 578 ? 138.241 142.936 97.595  1.00 0.32  ?  578 ILE A CG1   1 
ATOM   4654  C  CG2   . ILE A 1 578 ? 136.822 140.897 97.866  1.00 8.42  ?  578 ILE A CG2   1 
ATOM   4655  C  CD1   . ILE A 1 578 ? 138.827 142.288 96.371  1.00 9.81  ?  578 ILE A CD1   1 
ATOM   4656  N  N     . ALA A 1 579 ? 134.962 141.877 100.995 1.00 16.56 ?  579 ALA A N     1 
ATOM   4657  C  CA    . ALA A 1 579 ? 134.241 141.085 101.977 1.00 8.89  ?  579 ALA A CA    1 
ATOM   4658  C  C     . ALA A 1 579 ? 133.828 139.744 101.383 1.00 16.81 ?  579 ALA A C     1 
ATOM   4659  O  O     . ALA A 1 579 ? 133.798 139.577 100.161 1.00 21.14 ?  579 ALA A O     1 
ATOM   4660  C  CB    . ALA A 1 579 ? 133.013 141.853 102.460 1.00 13.01 ?  579 ALA A CB    1 
ATOM   4661  N  N     . PRO A 1 580 ? 133.527 138.751 102.227 1.00 24.08 ?  580 PRO A N     1 
ATOM   4662  C  CA    . PRO A 1 580 ? 133.118 137.439 101.694 1.00 20.95 ?  580 PRO A CA    1 
ATOM   4663  C  C     . PRO A 1 580 ? 131.858 137.473 100.841 1.00 25.56 ?  580 PRO A C     1 
ATOM   4664  O  O     . PRO A 1 580 ? 131.739 136.659 99.915  1.00 31.34 ?  580 PRO A O     1 
ATOM   4665  C  CB    . PRO A 1 580 ? 132.919 136.590 102.960 1.00 17.28 ?  580 PRO A CB    1 
ATOM   4666  C  CG    . PRO A 1 580 ? 132.877 137.561 104.095 1.00 20.67 ?  580 PRO A CG    1 
ATOM   4667  C  CD    . PRO A 1 580 ? 133.731 138.705 103.683 1.00 20.22 ?  580 PRO A CD    1 
ATOM   4668  N  N     . THR A 1 581 ? 130.917 138.376 101.120 1.00 21.90 ?  581 THR A N     1 
ATOM   4669  C  CA    . THR A 1 581 ? 129.662 138.496 100.373 1.00 27.67 ?  581 THR A CA    1 
ATOM   4670  C  C     . THR A 1 581 ? 128.900 137.167 100.367 1.00 31.22 ?  581 THR A C     1 
ATOM   4671  O  O     . THR A 1 581 ? 128.715 136.518 99.338  1.00 32.14 ?  581 THR A O     1 
ATOM   4672  C  CB    . THR A 1 581 ? 129.902 138.987 98.940  1.00 27.73 ?  581 THR A CB    1 
ATOM   4673  O  OG1   . THR A 1 581 ? 130.346 137.898 98.122  1.00 23.00 ?  581 THR A OG1   1 
ATOM   4674  C  CG2   . THR A 1 581 ? 130.935 140.097 98.914  1.00 28.64 ?  581 THR A CG2   1 
ATOM   4675  N  N     . GLY A 1 582 ? 128.460 136.781 101.562 1.00 28.49 ?  582 GLY A N     1 
ATOM   4676  C  CA    . GLY A 1 582 ? 127.840 135.486 101.766 1.00 31.03 ?  582 GLY A CA    1 
ATOM   4677  C  C     . GLY A 1 582 ? 126.561 135.234 100.993 1.00 34.80 ?  582 GLY A C     1 
ATOM   4678  O  O     . GLY A 1 582 ? 126.539 134.393 100.089 1.00 33.60 ?  582 GLY A O     1 
ATOM   4679  N  N     . SER A 1 583 ? 125.488 135.950 101.328 1.00 34.42 ?  583 SER A N     1 
ATOM   4680  C  CA    . SER A 1 583 ? 124.179 135.677 100.748 1.00 38.66 ?  583 SER A CA    1 
ATOM   4681  C  C     . SER A 1 583 ? 123.798 136.622 99.619  1.00 35.70 ?  583 SER A C     1 
ATOM   4682  O  O     . SER A 1 583 ? 122.951 136.264 98.794  1.00 34.27 ?  583 SER A O     1 
ATOM   4683  C  CB    . SER A 1 583 ? 123.095 135.735 101.831 1.00 40.58 ?  583 SER A CB    1 
ATOM   4684  O  OG    . SER A 1 583 ? 123.149 134.591 102.665 1.00 41.67 ?  583 SER A OG    1 
ATOM   4685  N  N     . ILE A 1 584 ? 124.391 137.816 99.556  1.00 32.67 ?  584 ILE A N     1 
ATOM   4686  C  CA    . ILE A 1 584 ? 124.085 138.729 98.462  1.00 26.88 ?  584 ILE A CA    1 
ATOM   4687  C  C     . ILE A 1 584 ? 124.599 138.202 97.130  1.00 29.09 ?  584 ILE A C     1 
ATOM   4688  O  O     . ILE A 1 584 ? 124.104 138.612 96.075  1.00 36.37 ?  584 ILE A O     1 
ATOM   4689  C  CB    . ILE A 1 584 ? 124.655 140.133 98.742  1.00 33.33 ?  584 ILE A CB    1 
ATOM   4690  C  CG1   . ILE A 1 584 ? 126.162 140.062 98.999  1.00 34.20 ?  584 ILE A CG1   1 
ATOM   4691  C  CG2   . ILE A 1 584 ? 123.921 140.785 99.904  1.00 34.09 ?  584 ILE A CG2   1 
ATOM   4692  C  CD1   . ILE A 1 584 ? 126.734 141.302 99.653  1.00 28.91 ?  584 ILE A CD1   1 
ATOM   4693  N  N     . SER A 1 585 ? 125.585 137.304 97.149  1.00 30.54 ?  585 SER A N     1 
ATOM   4694  C  CA    . SER A 1 585 ? 126.065 136.709 95.905  1.00 27.64 ?  585 SER A CA    1 
ATOM   4695  C  C     . SER A 1 585 ? 125.002 135.830 95.262  1.00 26.77 ?  585 SER A C     1 
ATOM   4696  O  O     . SER A 1 585 ? 124.981 135.682 94.035  1.00 27.43 ?  585 SER A O     1 
ATOM   4697  C  CB    . SER A 1 585 ? 127.338 135.905 96.164  1.00 24.39 ?  585 SER A CB    1 
ATOM   4698  O  OG    . SER A 1 585 ? 127.113 134.888 97.123  1.00 31.13 ?  585 SER A OG    1 
ATOM   4699  N  N     . TYR A 1 586 ? 124.122 135.231 96.068  1.00 34.80 ?  586 TYR A N     1 
ATOM   4700  C  CA    . TYR A 1 586 ? 123.010 134.466 95.517  1.00 33.30 ?  586 TYR A CA    1 
ATOM   4701  C  C     . TYR A 1 586 ? 122.038 135.375 94.778  1.00 31.89 ?  586 TYR A C     1 
ATOM   4702  O  O     . TYR A 1 586 ? 121.677 135.110 93.627  1.00 35.40 ?  586 TYR A O     1 
ATOM   4703  C  CB    . TYR A 1 586 ? 122.284 133.715 96.633  1.00 32.22 ?  586 TYR A CB    1 
ATOM   4704  C  CG    . TYR A 1 586 ? 123.030 132.524 97.183  1.00 30.72 ?  586 TYR A CG    1 
ATOM   4705  C  CD1   . TYR A 1 586 ? 123.426 132.488 98.513  1.00 33.44 ?  586 TYR A CD1   1 
ATOM   4706  C  CD2   . TYR A 1 586 ? 123.329 131.432 96.381  1.00 34.07 ?  586 TYR A CD2   1 
ATOM   4707  C  CE1   . TYR A 1 586 ? 124.106 131.402 99.026  1.00 35.12 ?  586 TYR A CE1   1 
ATOM   4708  C  CE2   . TYR A 1 586 ? 124.009 130.341 96.887  1.00 34.78 ?  586 TYR A CE2   1 
ATOM   4709  C  CZ    . TYR A 1 586 ? 124.393 130.331 98.210  1.00 36.82 ?  586 TYR A CZ    1 
ATOM   4710  O  OH    . TYR A 1 586 ? 125.071 129.249 98.720  1.00 38.57 ?  586 TYR A OH    1 
ATOM   4711  N  N     . VAL A 1 587 ? 121.616 136.463 95.427  1.00 29.42 ?  587 VAL A N     1 
ATOM   4712  C  CA    . VAL A 1 587 ? 120.630 137.368 94.840  1.00 27.19 ?  587 VAL A CA    1 
ATOM   4713  C  C     . VAL A 1 587 ? 121.167 137.986 93.557  1.00 29.12 ?  587 VAL A C     1 
ATOM   4714  O  O     . VAL A 1 587 ? 120.425 138.186 92.587  1.00 34.89 ?  587 VAL A O     1 
ATOM   4715  C  CB    . VAL A 1 587 ? 120.225 138.445 95.862  1.00 31.21 ?  587 VAL A CB    1 
ATOM   4716  C  CG1   . VAL A 1 587 ? 119.157 139.353 95.286  1.00 31.59 ?  587 VAL A CG1   1 
ATOM   4717  C  CG2   . VAL A 1 587 ? 119.746 137.797 97.150  1.00 33.64 ?  587 VAL A CG2   1 
ATOM   4718  N  N     . GLN A 1 588 ? 122.460 138.293 93.529  1.00 31.49 ?  588 GLN A N     1 
ATOM   4719  C  CA    . GLN A 1 588 ? 123.085 138.869 92.348  1.00 26.60 ?  588 GLN A CA    1 
ATOM   4720  C  C     . GLN A 1 588 ? 123.466 137.822 91.313  1.00 28.18 ?  588 GLN A C     1 
ATOM   4721  O  O     . GLN A 1 588 ? 123.985 138.190 90.252  1.00 29.80 ?  588 GLN A O     1 
ATOM   4722  C  CB    . GLN A 1 588 ? 124.325 139.670 92.750  1.00 24.80 ?  588 GLN A CB    1 
ATOM   4723  C  CG    . GLN A 1 588 ? 124.013 140.935 93.524  1.00 23.53 ?  588 GLN A CG    1 
ATOM   4724  C  CD    . GLN A 1 588 ? 123.990 142.160 92.637  1.00 26.75 ?  588 GLN A CD    1 
ATOM   4725  O  OE1   . GLN A 1 588 ? 124.791 142.285 91.712  1.00 24.74 ?  588 GLN A OE1   1 
ATOM   4726  N  NE2   . GLN A 1 588 ? 123.070 143.075 92.916  1.00 32.10 ?  588 GLN A NE2   1 
ATOM   4727  N  N     . SER A 1 589 ? 123.212 136.544 91.590  1.00 29.68 ?  589 SER A N     1 
ATOM   4728  C  CA    . SER A 1 589 ? 123.622 135.437 90.730  1.00 26.27 ?  589 SER A CA    1 
ATOM   4729  C  C     . SER A 1 589 ? 125.109 135.553 90.396  1.00 28.13 ?  589 SER A C     1 
ATOM   4730  O  O     . SER A 1 589 ? 125.516 135.688 89.241  1.00 30.35 ?  589 SER A O     1 
ATOM   4731  C  CB    . SER A 1 589 ? 122.763 135.374 89.464  1.00 28.07 ?  589 SER A CB    1 
ATOM   4732  O  OG    . SER A 1 589 ? 123.184 136.329 88.506  1.00 34.21 ?  589 SER A OG    1 
ATOM   4733  N  N     . SER A 1 590 ? 125.917 135.506 91.450  1.00 27.77 ?  590 SER A N     1 
ATOM   4734  C  CA    . SER A 1 590 ? 127.347 135.734 91.343  1.00 22.98 ?  590 SER A CA    1 
ATOM   4735  C  C     . SER A 1 590 ? 128.082 134.770 92.258  1.00 24.82 ?  590 SER A C     1 
ATOM   4736  O  O     . SER A 1 590 ? 127.529 134.265 93.238  1.00 29.39 ?  590 SER A O     1 
ATOM   4737  C  CB    . SER A 1 590 ? 127.706 137.181 91.705  1.00 22.09 ?  590 SER A CB    1 
ATOM   4738  O  OG    . SER A 1 590 ? 128.043 137.294 93.074  1.00 29.32 ?  590 SER A OG    1 
ATOM   4739  N  N     . THR A 1 591 ? 129.341 134.507 91.920  1.00 23.96 ?  591 THR A N     1 
ATOM   4740  C  CA    . THR A 1 591 ? 130.209 133.753 92.807  1.00 24.18 ?  591 THR A CA    1 
ATOM   4741  C  C     . THR A 1 591 ? 130.657 134.636 93.965  1.00 23.05 ?  591 THR A C     1 
ATOM   4742  O  O     . THR A 1 591 ? 130.796 135.855 93.827  1.00 17.67 ?  591 THR A O     1 
ATOM   4743  C  CB    . THR A 1 591 ? 131.422 133.211 92.048  1.00 26.23 ?  591 THR A CB    1 
ATOM   4744  O  OG1   . THR A 1 591 ? 132.312 134.285 91.728  1.00 30.00 ?  591 THR A OG1   1 
ATOM   4745  C  CG2   . THR A 1 591 ? 130.977 132.533 90.764  1.00 25.88 ?  591 THR A CG2   1 
ATOM   4746  N  N     . ALA A 1 592 ? 130.874 134.010 95.118  1.00 22.30 ?  592 ALA A N     1 
ATOM   4747  C  CA    . ALA A 1 592 ? 131.121 134.764 96.339  1.00 22.38 ?  592 ALA A CA    1 
ATOM   4748  C  C     . ALA A 1 592 ? 132.505 135.398 96.317  1.00 22.73 ?  592 ALA A C     1 
ATOM   4749  O  O     . ALA A 1 592 ? 133.513 134.706 96.149  1.00 27.19 ?  592 ALA A O     1 
ATOM   4750  C  CB    . ALA A 1 592 ? 130.975 133.856 97.559  1.00 24.34 ?  592 ALA A CB    1 
ATOM   4751  N  N     . SER A 1 593 ? 132.543 136.713 96.492  1.00 24.21 ?  593 SER A N     1 
ATOM   4752  C  CA    . SER A 1 593 ? 133.774 137.493 96.641  1.00 16.30 ?  593 SER A CA    1 
ATOM   4753  C  C     . SER A 1 593 ? 134.676 137.259 95.428  1.00 15.94 ?  593 SER A C     1 
ATOM   4754  O  O     . SER A 1 593 ? 134.203 136.943 94.332  1.00 23.75 ?  593 SER A O     1 
ATOM   4755  C  CB    . SER A 1 593 ? 134.409 137.153 97.978  1.00 25.18 ?  593 SER A CB    1 
ATOM   4756  O  OG    . SER A 1 593 ? 135.432 138.070 98.310  1.00 24.78 ?  593 SER A OG    1 
ATOM   4757  N  N     . VAL A 1 594 ? 135.986 137.423 95.612  1.00 21.63 ?  594 VAL A N     1 
ATOM   4758  C  CA    . VAL A 1 594 ? 136.965 137.068 94.595  1.00 19.48 ?  594 VAL A CA    1 
ATOM   4759  C  C     . VAL A 1 594 ? 137.472 135.644 94.782  1.00 18.95 ?  594 VAL A C     1 
ATOM   4760  O  O     . VAL A 1 594 ? 138.420 135.230 94.108  1.00 18.36 ?  594 VAL A O     1 
ATOM   4761  C  CB    . VAL A 1 594 ? 138.133 138.067 94.580  1.00 21.54 ?  594 VAL A CB    1 
ATOM   4762  C  CG1   . VAL A 1 594 ? 137.650 139.438 94.134  1.00 9.11  ?  594 VAL A CG1   1 
ATOM   4763  C  CG2   . VAL A 1 594 ? 138.782 138.142 95.950  1.00 17.90 ?  594 VAL A CG2   1 
ATOM   4764  N  N     . MET A 1 595 ? 136.862 134.887 95.689  1.00 25.45 ?  595 MET A N     1 
ATOM   4765  C  CA    . MET A 1 595 ? 137.257 133.510 95.915  1.00 18.76 ?  595 MET A CA    1 
ATOM   4766  C  C     . MET A 1 595 ? 136.839 132.637 94.734  1.00 24.58 ?  595 MET A C     1 
ATOM   4767  O  O     . MET A 1 595 ? 135.851 132.925 94.054  1.00 32.18 ?  595 MET A O     1 
ATOM   4768  C  CB    . MET A 1 595 ? 136.613 132.975 97.192  1.00 22.37 ?  595 MET A CB    1 
ATOM   4769  C  CG    . MET A 1 595 ? 137.277 133.306 98.546  1.00 25.47 ?  595 MET A CG    1 
ATOM   4770  S  SD    . MET A 1 595 ? 139.077 133.248 98.757  1.00 31.61 ?  595 MET A SD    1 
ATOM   4771  C  CE    . MET A 1 595 ? 139.641 134.735 97.937  1.00 18.71 ?  595 MET A CE    1 
ATOM   4772  N  N     . PRO A 1 596 ? 137.581 131.567 94.464  1.00 27.55 ?  596 PRO A N     1 
ATOM   4773  C  CA    . PRO A 1 596 ? 137.096 130.556 93.522  1.00 22.18 ?  596 PRO A CA    1 
ATOM   4774  C  C     . PRO A 1 596 ? 135.932 129.777 94.116  1.00 27.22 ?  596 PRO A C     1 
ATOM   4775  O  O     . PRO A 1 596 ? 135.763 129.685 95.334  1.00 31.05 ?  596 PRO A O     1 
ATOM   4776  C  CB    . PRO A 1 596 ? 138.316 129.657 93.299  1.00 23.92 ?  596 PRO A CB    1 
ATOM   4777  C  CG    . PRO A 1 596 ? 139.154 129.851 94.517  1.00 28.34 ?  596 PRO A CG    1 
ATOM   4778  C  CD    . PRO A 1 596 ? 138.934 131.264 94.961  1.00 28.46 ?  596 PRO A CD    1 
ATOM   4779  N  N     . ILE A 1 597 ? 135.115 129.212 93.226  1.00 29.21 ?  597 ILE A N     1 
ATOM   4780  C  CA    . ILE A 1 597 ? 133.921 128.501 93.663  1.00 31.33 ?  597 ILE A CA    1 
ATOM   4781  C  C     . ILE A 1 597 ? 134.312 127.222 94.396  1.00 34.65 ?  597 ILE A C     1 
ATOM   4782  O  O     . ILE A 1 597 ? 135.276 126.534 94.034  1.00 36.12 ?  597 ILE A O     1 
ATOM   4783  C  CB    . ILE A 1 597 ? 132.997 128.198 92.469  1.00 32.00 ?  597 ILE A CB    1 
ATOM   4784  C  CG1   . ILE A 1 597 ? 133.672 127.233 91.490  1.00 31.16 ?  597 ILE A CG1   1 
ATOM   4785  C  CG2   . ILE A 1 597 ? 132.613 129.481 91.761  1.00 31.63 ?  597 ILE A CG2   1 
ATOM   4786  C  CD1   . ILE A 1 597 ? 132.702 126.439 90.651  1.00 31.93 ?  597 ILE A CD1   1 
ATOM   4787  N  N     . MET A 1 598 ? 133.561 126.909 95.452  1.00 39.86 ?  598 MET A N     1 
ATOM   4788  C  CA    . MET A 1 598 ? 133.809 125.681 96.196  1.00 38.55 ?  598 MET A CA    1 
ATOM   4789  C  C     . MET A 1 598 ? 133.239 124.468 95.474  1.00 38.59 ?  598 MET A C     1 
ATOM   4790  O  O     . MET A 1 598 ? 133.893 123.423 95.394  1.00 44.29 ?  598 MET A O     1 
ATOM   4791  C  CB    . MET A 1 598 ? 133.217 125.792 97.600  1.00 37.06 ?  598 MET A CB    1 
ATOM   4792  C  CG    . MET A 1 598 ? 134.126 126.474 98.603  1.00 35.00 ?  598 MET A CG    1 
ATOM   4793  S  SD    . MET A 1 598 ? 133.303 126.812 100.170 1.00 53.18 ?  598 MET A SD    1 
ATOM   4794  C  CE    . MET A 1 598 ? 132.089 128.022 99.656  1.00 39.51 ?  598 MET A CE    1 
ATOM   4795  N  N     . GLU A 1 599 ? 132.022 124.589 94.951  1.00 38.15 ?  599 GLU A N     1 
ATOM   4796  C  CA    . GLU A 1 599 ? 131.365 123.527 94.206  1.00 37.01 ?  599 GLU A CA    1 
ATOM   4797  C  C     . GLU A 1 599 ? 130.763 124.108 92.936  1.00 36.30 ?  599 GLU A C     1 
ATOM   4798  O  O     . GLU A 1 599 ? 130.358 125.272 92.902  1.00 40.49 ?  599 GLU A O     1 
ATOM   4799  C  CB    . GLU A 1 599 ? 130.264 122.848 95.035  1.00 38.85 ?  599 GLU A CB    1 
ATOM   4800  C  CG    . GLU A 1 599 ? 130.634 122.591 96.488  1.00 39.53 ?  599 GLU A CG    1 
ATOM   4801  C  CD    . GLU A 1 599 ? 129.425 122.557 97.401  1.00 43.17 ?  599 GLU A CD    1 
ATOM   4802  O  OE1   . GLU A 1 599 ? 128.921 123.640 97.764  1.00 40.97 ?  599 GLU A OE1   1 
ATOM   4803  O  OE2   . GLU A 1 599 ? 128.979 121.447 97.758  1.00 45.94 -1 599 GLU A OE2   1 
ATOM   4804  N  N     . ARG A 1 600 ? 130.714 123.291 91.883  1.00 38.66 ?  600 ARG A N     1 
ATOM   4805  C  CA    . ARG A 1 600 ? 130.059 123.729 90.655  1.00 35.38 ?  600 ARG A CA    1 
ATOM   4806  C  C     . ARG A 1 600 ? 128.552 123.824 90.850  1.00 34.16 ?  600 ARG A C     1 
ATOM   4807  O  O     . ARG A 1 600 ? 127.924 124.815 90.463  1.00 37.87 ?  600 ARG A O     1 
ATOM   4808  C  CB    . ARG A 1 600 ? 130.398 122.779 89.510  1.00 34.71 ?  600 ARG A CB    1 
ATOM   4809  C  CG    . ARG A 1 600 ? 131.761 123.022 88.905  1.00 35.12 ?  600 ARG A CG    1 
ATOM   4810  C  CD    . ARG A 1 600 ? 131.980 122.149 87.692  1.00 34.48 ?  600 ARG A CD    1 
ATOM   4811  N  NE    . ARG A 1 600 ? 133.296 122.352 87.098  1.00 34.15 ?  600 ARG A NE    1 
ATOM   4812  C  CZ    . ARG A 1 600 ? 134.399 121.739 87.502  1.00 37.48 ?  600 ARG A CZ    1 
ATOM   4813  N  NH1   . ARG A 1 600 ? 134.384 120.883 88.510  1.00 36.61 1  600 ARG A NH1   1 
ATOM   4814  N  NH2   . ARG A 1 600 ? 135.546 121.993 86.879  1.00 37.83 ?  600 ARG A NH2   1 
ATOM   4815  N  N     . ILE A 1 601 ? 127.957 122.794 91.444  1.00 39.12 ?  601 ILE A N     1 
ATOM   4816  C  CA    . ILE A 1 601 ? 126.557 122.802 91.845  1.00 41.28 ?  601 ILE A CA    1 
ATOM   4817  C  C     . ILE A 1 601 ? 126.516 122.487 93.332  1.00 40.35 ?  601 ILE A C     1 
ATOM   4818  O  O     . ILE A 1 601 ? 127.053 121.462 93.769  1.00 41.59 ?  601 ILE A O     1 
ATOM   4819  C  CB    . ILE A 1 601 ? 125.722 121.790 91.047  1.00 40.71 ?  601 ILE A CB    1 
ATOM   4820  C  CG1   . ILE A 1 601 ? 125.912 122.004 89.545  1.00 41.03 ?  601 ILE A CG1   1 
ATOM   4821  C  CG2   . ILE A 1 601 ? 124.253 121.906 91.416  1.00 37.03 ?  601 ILE A CG2   1 
ATOM   4822  C  CD1   . ILE A 1 601 ? 125.336 120.898 88.695  1.00 39.55 ?  601 ILE A CD1   1 
ATOM   4823  N  N     . GLU A 1 602 ? 125.887 123.363 94.107  1.00 45.16 ?  602 GLU A N     1 
ATOM   4824  C  CA    . GLU A 1 602 ? 125.800 123.196 95.549  1.00 47.44 ?  602 GLU A CA    1 
ATOM   4825  C  C     . GLU A 1 602 ? 124.422 122.681 95.942  1.00 48.63 ?  602 GLU A C     1 
ATOM   4826  O  O     . GLU A 1 602 ? 123.397 123.157 95.444  1.00 48.67 ?  602 GLU A O     1 
ATOM   4827  C  CB    . GLU A 1 602 ? 126.104 124.509 96.276  1.00 45.19 ?  602 GLU A CB    1 
ATOM   4828  C  CG    . GLU A 1 602 ? 125.292 125.697 95.807  1.00 47.09 ?  602 GLU A CG    1 
ATOM   4829  C  CD    . GLU A 1 602 ? 125.478 126.912 96.693  1.00 50.58 ?  602 GLU A CD    1 
ATOM   4830  O  OE1   . GLU A 1 602 ? 126.528 127.577 96.579  1.00 50.27 ?  602 GLU A OE1   1 
ATOM   4831  O  OE2   . GLU A 1 602 ? 124.573 127.202 97.504  1.00 51.85 -1 602 GLU A OE2   1 
ATOM   4832  N  N     . GLU A 1 603 ? 124.413 121.693 96.830  1.00 56.87 ?  603 GLU A N     1 
ATOM   4833  C  CA    . GLU A 1 603 ? 123.193 121.086 97.341  1.00 57.73 ?  603 GLU A CA    1 
ATOM   4834  C  C     . GLU A 1 603 ? 122.888 121.652 98.720  1.00 57.59 ?  603 GLU A C     1 
ATOM   4835  O  O     . GLU A 1 603 ? 123.737 121.605 99.617  1.00 57.50 ?  603 GLU A O     1 
ATOM   4836  C  CB    . GLU A 1 603 ? 123.339 119.566 97.414  1.00 57.17 ?  603 GLU A CB    1 
ATOM   4837  C  CG    . GLU A 1 603 ? 122.113 118.841 97.930  1.00 58.95 ?  603 GLU A CG    1 
ATOM   4838  C  CD    . GLU A 1 603 ? 122.465 117.577 98.689  1.00 60.15 ?  603 GLU A CD    1 
ATOM   4839  O  OE1   . GLU A 1 603 ? 122.789 117.676 99.891  1.00 60.48 ?  603 GLU A OE1   1 
ATOM   4840  O  OE2   . GLU A 1 603 ? 122.417 116.487 98.084  1.00 59.56 -1 603 GLU A OE2   1 
ATOM   4841  N  N     . ARG A 1 604 ? 121.680 122.184 98.889  1.00 58.62 ?  604 ARG A N     1 
ATOM   4842  C  CA    . ARG A 1 604 ? 121.267 122.768 100.155 1.00 59.06 ?  604 ARG A CA    1 
ATOM   4843  C  C     . ARG A 1 604 ? 119.958 122.138 100.609 1.00 59.92 ?  604 ARG A C     1 
ATOM   4844  O  O     . ARG A 1 604 ? 119.182 121.628 99.799  1.00 59.33 ?  604 ARG A O     1 
ATOM   4845  C  CB    . ARG A 1 604 ? 121.111 124.289 100.053 1.00 58.99 ?  604 ARG A CB    1 
ATOM   4846  C  CG    . ARG A 1 604 ? 122.369 125.007 99.597  1.00 58.38 ?  604 ARG A CG    1 
ATOM   4847  C  CD    . ARG A 1 604 ? 123.212 125.446 100.782 1.00 58.50 ?  604 ARG A CD    1 
ATOM   4848  N  NE    . ARG A 1 604 ? 124.324 124.536 101.025 1.00 58.72 ?  604 ARG A NE    1 
ATOM   4849  C  CZ    . ARG A 1 604 ? 125.533 124.672 100.497 1.00 59.29 ?  604 ARG A CZ    1 
ATOM   4850  N  NH1   . ARG A 1 604 ? 125.824 125.676 99.686  1.00 57.85 1  604 ARG A NH1   1 
ATOM   4851  N  NH2   . ARG A 1 604 ? 126.473 123.777 100.789 1.00 57.26 ?  604 ARG A NH2   1 
ATOM   4852  N  N     . THR A 1 605 ? 119.732 122.165 101.919 1.00 65.73 ?  605 THR A N     1 
ATOM   4853  C  CA    . THR A 1 605 ? 118.521 121.620 102.524 1.00 66.61 ?  605 THR A CA    1 
ATOM   4854  C  C     . THR A 1 605 ? 117.793 122.748 103.240 1.00 66.54 ?  605 THR A C     1 
ATOM   4855  O  O     . THR A 1 605 ? 118.280 123.265 104.251 1.00 65.70 ?  605 THR A O     1 
ATOM   4856  C  CB    . THR A 1 605 ? 118.852 120.484 103.492 1.00 66.19 ?  605 THR A CB    1 
ATOM   4857  O  OG1   . THR A 1 605 ? 119.627 119.486 102.817 1.00 66.36 ?  605 THR A OG1   1 
ATOM   4858  C  CG2   . THR A 1 605 ? 117.576 119.852 104.026 1.00 66.87 ?  605 THR A CG2   1 
ATOM   4859  N  N     . TYR A 1 606 ? 116.632 123.132 102.719 1.00 66.48 ?  606 TYR A N     1 
ATOM   4860  C  CA    . TYR A 1 606 ? 115.781 124.133 103.346 1.00 68.28 ?  606 TYR A CA    1 
ATOM   4861  C  C     . TYR A 1 606 ? 114.495 123.465 103.807 1.00 70.28 ?  606 TYR A C     1 
ATOM   4862  O  O     . TYR A 1 606 ? 113.802 122.823 103.007 1.00 69.13 ?  606 TYR A O     1 
ATOM   4863  C  CB    . TYR A 1 606 ? 115.477 125.286 102.387 1.00 66.57 ?  606 TYR A CB    1 
ATOM   4864  C  CG    . TYR A 1 606 ? 116.696 126.095 102.005 1.00 68.29 ?  606 TYR A CG    1 
ATOM   4865  C  CD1   . TYR A 1 606 ? 117.380 126.846 102.951 1.00 66.92 ?  606 TYR A CD1   1 
ATOM   4866  C  CD2   . TYR A 1 606 ? 117.161 126.109 100.699 1.00 67.97 ?  606 TYR A CD2   1 
ATOM   4867  C  CE1   . TYR A 1 606 ? 118.495 127.588 102.605 1.00 66.54 ?  606 TYR A CE1   1 
ATOM   4868  C  CE2   . TYR A 1 606 ? 118.274 126.847 100.344 1.00 65.78 ?  606 TYR A CE2   1 
ATOM   4869  C  CZ    . TYR A 1 606 ? 118.937 127.583 101.299 1.00 67.46 ?  606 TYR A CZ    1 
ATOM   4870  O  OH    . TYR A 1 606 ? 120.045 128.318 100.946 1.00 66.96 ?  606 TYR A OH    1 
ATOM   4871  N  N     . GLY A 1 607 ? 114.177 123.622 105.089 1.00 75.36 ?  607 GLY A N     1 
ATOM   4872  C  CA    . GLY A 1 607 ? 113.070 122.869 105.655 1.00 74.97 ?  607 GLY A CA    1 
ATOM   4873  C  C     . GLY A 1 607 ? 113.344 121.386 105.528 1.00 75.53 ?  607 GLY A C     1 
ATOM   4874  O  O     . GLY A 1 607 ? 114.394 120.886 105.946 1.00 75.04 ?  607 GLY A O     1 
ATOM   4875  N  N     . ASN A 1 608 ? 112.391 120.665 104.939 1.00 78.59 ?  608 ASN A N     1 
ATOM   4876  C  CA    . ASN A 1 608 ? 112.562 119.254 104.622 1.00 80.29 ?  608 ASN A CA    1 
ATOM   4877  C  C     . ASN A 1 608 ? 112.743 119.025 103.126 1.00 79.21 ?  608 ASN A C     1 
ATOM   4878  O  O     . ASN A 1 608 ? 112.517 117.913 102.639 1.00 78.37 ?  608 ASN A O     1 
ATOM   4879  C  CB    . ASN A 1 608 ? 111.377 118.442 105.148 1.00 79.45 ?  608 ASN A CB    1 
ATOM   4880  C  CG    . ASN A 1 608 ? 111.433 118.239 106.650 1.00 79.47 ?  608 ASN A CG    1 
ATOM   4881  O  OD1   . ASN A 1 608 ? 112.453 118.506 107.286 1.00 79.06 ?  608 ASN A OD1   1 
ATOM   4882  N  ND2   . ASN A 1 608 ? 110.335 117.763 107.225 1.00 78.01 ?  608 ASN A ND2   1 
ATOM   4883  N  N     . SER A 1 609 ? 113.148 120.057 102.390 1.00 73.08 ?  609 SER A N     1 
ATOM   4884  C  CA    . SER A 1 609 ? 113.276 119.992 100.944 1.00 72.48 ?  609 SER A CA    1 
ATOM   4885  C  C     . SER A 1 609 ? 114.722 120.222 100.528 1.00 73.03 ?  609 SER A C     1 
ATOM   4886  O  O     . SER A 1 609 ? 115.481 120.925 101.204 1.00 72.83 ?  609 SER A O     1 
ATOM   4887  C  CB    . SER A 1 609 ? 112.371 121.025 100.264 1.00 71.53 ?  609 SER A CB    1 
ATOM   4888  O  OG    . SER A 1 609 ? 112.729 122.343 100.640 1.00 70.80 ?  609 SER A OG    1 
ATOM   4889  N  N     . LYS A 1 610 ? 115.099 119.609 99.410  1.00 65.08 ?  610 LYS A N     1 
ATOM   4890  C  CA    . LYS A 1 610 ? 116.436 119.737 98.852  1.00 62.96 ?  610 LYS A CA    1 
ATOM   4891  C  C     . LYS A 1 610 ? 116.403 120.678 97.655  1.00 63.45 ?  610 LYS A C     1 
ATOM   4892  O  O     . LYS A 1 610 ? 115.430 120.700 96.896  1.00 64.05 ?  610 LYS A O     1 
ATOM   4893  C  CB    . LYS A 1 610 ? 116.984 118.372 98.431  1.00 62.17 ?  610 LYS A CB    1 
ATOM   4894  C  CG    . LYS A 1 610 ? 118.499 118.306 98.355  1.00 63.41 ?  610 LYS A CG    1 
ATOM   4895  C  CD    . LYS A 1 610 ? 119.022 117.031 99.002  1.00 64.78 ?  610 LYS A CD    1 
ATOM   4896  C  CE    . LYS A 1 610 ? 119.125 117.172 100.514 1.00 64.27 ?  610 LYS A CE    1 
ATOM   4897  N  NZ    . LYS A 1 610 ? 120.322 117.951 100.931 1.00 62.54 1  610 LYS A NZ    1 
ATOM   4898  N  N     . THR A 1 611 ? 117.470 121.456 97.494  1.00 61.72 ?  611 THR A N     1 
ATOM   4899  C  CA    . THR A 1 611 ? 117.565 122.417 96.407  1.00 58.73 ?  611 THR A CA    1 
ATOM   4900  C  C     . THR A 1 611 ? 118.980 122.403 95.849  1.00 57.57 ?  611 THR A C     1 
ATOM   4901  O  O     . THR A 1 611 ? 119.944 122.053 96.536  1.00 56.69 ?  611 THR A O     1 
ATOM   4902  C  CB    . THR A 1 611 ? 117.185 123.830 96.865  1.00 58.99 ?  611 THR A CB    1 
ATOM   4903  O  OG1   . THR A 1 611 ? 117.221 124.721 95.745  1.00 61.87 ?  611 THR A OG1   1 
ATOM   4904  C  CG2   . THR A 1 611 ? 118.149 124.315 97.926  1.00 59.35 ?  611 THR A CG2   1 
ATOM   4905  N  N     . TYR A 1 612 ? 119.090 122.801 94.584  1.00 53.41 ?  612 TYR A N     1 
ATOM   4906  C  CA    . TYR A 1 612 ? 120.323 122.679 93.818  1.00 51.64 ?  612 TYR A CA    1 
ATOM   4907  C  C     . TYR A 1 612 ? 120.626 124.020 93.172  1.00 54.03 ?  612 TYR A C     1 
ATOM   4908  O  O     . TYR A 1 612 ? 119.809 124.536 92.402  1.00 56.09 ?  612 TYR A O     1 
ATOM   4909  C  CB    . TYR A 1 612 ? 120.177 121.586 92.756  1.00 53.90 ?  612 TYR A CB    1 
ATOM   4910  C  CG    . TYR A 1 612 ? 120.145 120.190 93.332  1.00 55.12 ?  612 TYR A CG    1 
ATOM   4911  C  CD1   . TYR A 1 612 ? 121.141 119.745 94.186  1.00 54.59 ?  612 TYR A CD1   1 
ATOM   4912  C  CD2   . TYR A 1 612 ? 119.083 119.337 93.064  1.00 54.58 ?  612 TYR A CD2   1 
ATOM   4913  C  CE1   . TYR A 1 612 ? 121.104 118.473 94.720  1.00 55.95 ?  612 TYR A CE1   1 
ATOM   4914  C  CE2   . TYR A 1 612 ? 119.032 118.066 93.602  1.00 55.96 ?  612 TYR A CE2   1 
ATOM   4915  C  CZ    . TYR A 1 612 ? 120.046 117.639 94.429  1.00 57.43 ?  612 TYR A CZ    1 
ATOM   4916  O  OH    . TYR A 1 612 ? 120.006 116.374 94.969  1.00 58.99 ?  612 TYR A OH    1 
ATOM   4917  N  N     . TYR A 1 613 ? 121.789 124.586 93.482  1.00 46.07 ?  613 TYR A N     1 
ATOM   4918  C  CA    . TYR A 1 613 ? 122.221 125.851 92.889  1.00 40.41 ?  613 TYR A CA    1 
ATOM   4919  C  C     . TYR A 1 613 ? 123.477 125.639 92.060  1.00 39.86 ?  613 TYR A C     1 
ATOM   4920  O  O     . TYR A 1 613 ? 124.571 125.460 92.622  1.00 39.39 ?  613 TYR A O     1 
ATOM   4921  C  CB    . TYR A 1 613 ? 122.469 126.907 93.964  1.00 40.96 ?  613 TYR A CB    1 
ATOM   4922  C  CG    . TYR A 1 613 ? 122.913 128.240 93.404  1.00 37.21 ?  613 TYR A CG    1 
ATOM   4923  C  CD1   . TYR A 1 613 ? 122.159 128.895 92.439  1.00 37.85 ?  613 TYR A CD1   1 
ATOM   4924  C  CD2   . TYR A 1 613 ? 124.088 128.841 93.835  1.00 37.53 ?  613 TYR A CD2   1 
ATOM   4925  C  CE1   . TYR A 1 613 ? 122.559 130.113 91.925  1.00 41.31 ?  613 TYR A CE1   1 
ATOM   4926  C  CE2   . TYR A 1 613 ? 124.496 130.059 93.325  1.00 39.98 ?  613 TYR A CE2   1 
ATOM   4927  C  CZ    . TYR A 1 613 ? 123.728 130.689 92.371  1.00 44.91 ?  613 TYR A CZ    1 
ATOM   4928  O  OH    . TYR A 1 613 ? 124.129 131.902 91.859  1.00 41.53 ?  613 TYR A OH    1 
ATOM   4929  N  N     . PRO A 1 614 ? 123.373 125.610 90.736  1.00 41.29 ?  614 PRO A N     1 
ATOM   4930  C  CA    . PRO A 1 614 ? 124.582 125.661 89.910  1.00 38.89 ?  614 PRO A CA    1 
ATOM   4931  C  C     . PRO A 1 614 ? 125.212 127.040 89.978  1.00 39.14 ?  614 PRO A C     1 
ATOM   4932  O  O     . PRO A 1 614 ? 124.538 128.046 90.212  1.00 37.77 ?  614 PRO A O     1 
ATOM   4933  C  CB    . PRO A 1 614 ? 124.070 125.349 88.498  1.00 35.09 ?  614 PRO A CB    1 
ATOM   4934  C  CG    . PRO A 1 614 ? 122.670 124.834 88.678  1.00 39.46 ?  614 PRO A CG    1 
ATOM   4935  C  CD    . PRO A 1 614 ? 122.156 125.471 89.924  1.00 39.99 ?  614 PRO A CD    1 
ATOM   4936  N  N     . MET A 1 615 ? 126.525 127.081 89.776  1.00 37.84 ?  615 MET A N     1 
ATOM   4937  C  CA    . MET A 1 615 ? 127.212 128.359 89.735  1.00 35.62 ?  615 MET A CA    1 
ATOM   4938  C  C     . MET A 1 615 ? 126.727 129.173 88.536  1.00 38.19 ?  615 MET A C     1 
ATOM   4939  O  O     . MET A 1 615 ? 126.359 128.610 87.502  1.00 40.78 ?  615 MET A O     1 
ATOM   4940  C  CB    . MET A 1 615 ? 128.723 128.153 89.682  1.00 36.41 ?  615 MET A CB    1 
ATOM   4941  C  CG    . MET A 1 615 ? 129.330 127.920 91.055  1.00 37.79 ?  615 MET A CG    1 
ATOM   4942  S  SD    . MET A 1 615 ? 128.358 128.744 92.334  1.00 44.79 ?  615 MET A SD    1 
ATOM   4943  C  CE    . MET A 1 615 ? 128.862 127.857 93.801  1.00 37.65 ?  615 MET A CE    1 
ATOM   4944  N  N     . PRO A 1 616 ? 126.683 130.498 88.663  1.00 38.31 ?  616 PRO A N     1 
ATOM   4945  C  CA    . PRO A 1 616 ? 126.072 131.324 87.613  1.00 35.48 ?  616 PRO A CA    1 
ATOM   4946  C  C     . PRO A 1 616 ? 126.781 131.156 86.277  1.00 36.21 ?  616 PRO A C     1 
ATOM   4947  O  O     . PRO A 1 616 ? 128.009 131.201 86.194  1.00 38.12 ?  616 PRO A O     1 
ATOM   4948  C  CB    . PRO A 1 616 ? 126.222 132.750 88.155  1.00 36.48 ?  616 PRO A CB    1 
ATOM   4949  C  CG    . PRO A 1 616 ? 126.404 132.578 89.629  1.00 35.50 ?  616 PRO A CG    1 
ATOM   4950  C  CD    . PRO A 1 616 ? 127.152 131.305 89.801  1.00 35.95 ?  616 PRO A CD    1 
ATOM   4951  N  N     . GLY A 1 617 ? 125.989 130.968 85.225  1.00 37.13 ?  617 GLY A N     1 
ATOM   4952  C  CA    . GLY A 1 617 ? 126.537 130.772 83.900  1.00 36.09 ?  617 GLY A CA    1 
ATOM   4953  C  C     . GLY A 1 617 ? 127.164 129.420 83.658  1.00 40.13 ?  617 GLY A C     1 
ATOM   4954  O  O     . GLY A 1 617 ? 127.830 129.239 82.634  1.00 42.08 ?  617 GLY A O     1 
ATOM   4955  N  N     . LEU A 1 618 ? 126.977 128.464 84.565  1.00 41.11 ?  618 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 618 ? 127.568 127.144 84.392  1.00 37.11 ?  618 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 618 ? 126.860 126.389 83.275  1.00 39.55 ?  618 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 618 ? 125.629 126.334 83.227  1.00 44.58 ?  618 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 618 ? 127.497 126.351 85.695  1.00 37.34 ?  618 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 618 ? 128.111 124.951 85.675  1.00 38.46 ?  618 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 618 ? 129.578 125.011 85.292  1.00 38.88 ?  618 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 618 ? 127.936 124.270 87.022  1.00 39.00 ?  618 LEU A CD2   1 
ATOM   4963  N  N     . ALA A 1 619 ? 127.648 125.805 82.377  1.00 45.15 ?  619 ALA A N     1 
ATOM   4964  C  CA    . ALA A 1 619 ? 127.125 125.016 81.274  1.00 45.77 ?  619 ALA A CA    1 
ATOM   4965  C  C     . ALA A 1 619 ? 128.156 123.954 80.922  1.00 49.12 ?  619 ALA A C     1 
ATOM   4966  O  O     . ALA A 1 619 ? 129.163 123.785 81.614  1.00 51.63 ?  619 ALA A O     1 
ATOM   4967  C  CB    . ALA A 1 619 ? 126.788 125.901 80.070  1.00 44.64 ?  619 ALA A CB    1 
ATOM   4968  N  N     . SER A 1 620 ? 127.897 123.230 79.832  1.00 50.10 ?  620 SER A N     1 
ATOM   4969  C  CA    . SER A 1 620 ? 128.842 122.212 79.390  1.00 49.28 ?  620 SER A CA    1 
ATOM   4970  C  C     . SER A 1 620 ? 130.116 122.841 78.841  1.00 49.15 ?  620 SER A C     1 
ATOM   4971  O  O     . SER A 1 620 ? 131.210 122.287 79.007  1.00 51.61 ?  620 SER A O     1 
ATOM   4972  C  CB    . SER A 1 620 ? 128.188 121.314 78.340  1.00 52.72 ?  620 SER A CB    1 
ATOM   4973  O  OG    . SER A 1 620 ? 126.968 120.777 78.819  1.00 54.05 ?  620 SER A OG    1 
ATOM   4974  N  N     . ASN A 1 621 ? 129.998 123.998 78.186  1.00 47.90 ?  621 ASN A N     1 
ATOM   4975  C  CA    . ASN A 1 621 ? 131.166 124.627 77.579  1.00 50.30 ?  621 ASN A CA    1 
ATOM   4976  C  C     . ASN A 1 621 ? 132.119 125.179 78.634  1.00 50.21 ?  621 ASN A C     1 
ATOM   4977  O  O     . ASN A 1 621 ? 133.342 125.090 78.478  1.00 50.40 ?  621 ASN A O     1 
ATOM   4978  C  CB    . ASN A 1 621 ? 130.726 125.733 76.621  1.00 49.26 ?  621 ASN A CB    1 
ATOM   4979  C  CG    . ASN A 1 621 ? 129.465 126.433 77.079  1.00 51.92 ?  621 ASN A CG    1 
ATOM   4980  O  OD1   . ASN A 1 621 ? 129.416 126.996 78.172  1.00 50.98 ?  621 ASN A OD1   1 
ATOM   4981  N  ND2   . ASN A 1 621 ? 128.433 126.400 76.245  1.00 51.57 ?  621 ASN A ND2   1 
ATOM   4982  N  N     . ASN A 1 622 ? 131.582 125.750 79.712  1.00 40.26 ?  622 ASN A N     1 
ATOM   4983  C  CA    . ASN A 1 622 ? 132.399 126.347 80.762  1.00 39.73 ?  622 ASN A CA    1 
ATOM   4984  C  C     . ASN A 1 622 ? 132.436 125.495 82.027  1.00 43.21 ?  622 ASN A C     1 
ATOM   4985  O  O     . ASN A 1 622 ? 132.774 126.003 83.101  1.00 47.91 ?  622 ASN A O     1 
ATOM   4986  C  CB    . ASN A 1 622 ? 131.910 127.762 81.079  1.00 40.12 ?  622 ASN A CB    1 
ATOM   4987  C  CG    . ASN A 1 622 ? 130.436 127.811 81.434  1.00 41.94 ?  622 ASN A CG    1 
ATOM   4988  O  OD1   . ASN A 1 622 ? 129.816 126.789 81.724  1.00 47.40 ?  622 ASN A OD1   1 
ATOM   4989  N  ND2   . ASN A 1 622 ? 129.865 129.009 81.411  1.00 38.35 ?  622 ASN A ND2   1 
ATOM   4990  N  N     . TRP A 1 623 ? 132.087 124.211 81.923  1.00 40.70 ?  623 TRP A N     1 
ATOM   4991  C  CA    . TRP A 1 623 ? 132.170 123.327 83.080  1.00 40.55 ?  623 TRP A CA    1 
ATOM   4992  C  C     . TRP A 1 623 ? 133.612 123.170 83.548  1.00 41.55 ?  623 TRP A C     1 
ATOM   4993  O  O     . TRP A 1 623 ? 133.884 123.144 84.754  1.00 40.00 ?  623 TRP A O     1 
ATOM   4994  C  CB    . TRP A 1 623 ? 131.559 121.965 82.744  1.00 41.25 ?  623 TRP A CB    1 
ATOM   4995  C  CG    . TRP A 1 623 ? 131.696 120.941 83.832  1.00 40.04 ?  623 TRP A CG    1 
ATOM   4996  C  CD1   . TRP A 1 623 ? 132.764 120.124 84.062  1.00 37.86 ?  623 TRP A CD1   1 
ATOM   4997  C  CD2   . TRP A 1 623 ? 130.725 120.622 84.836  1.00 39.38 ?  623 TRP A CD2   1 
ATOM   4998  N  NE1   . TRP A 1 623 ? 132.520 119.319 85.147  1.00 37.74 ?  623 TRP A NE1   1 
ATOM   4999  C  CE2   . TRP A 1 623 ? 131.274 119.604 85.638  1.00 37.65 ?  623 TRP A CE2   1 
ATOM   5000  C  CE3   . TRP A 1 623 ? 129.445 121.099 85.132  1.00 38.03 ?  623 TRP A CE3   1 
ATOM   5001  C  CZ2   . TRP A 1 623 ? 130.589 119.056 86.722  1.00 38.90 ?  623 TRP A CZ2   1 
ATOM   5002  C  CZ3   . TRP A 1 623 ? 128.767 120.554 86.206  1.00 39.91 ?  623 TRP A CZ3   1 
ATOM   5003  C  CH2   . TRP A 1 623 ? 129.339 119.544 86.988  1.00 39.28 ?  623 TRP A CH2   1 
ATOM   5004  N  N     . PHE A 1 624 ? 134.551 123.063 82.605  1.00 43.25 ?  624 PHE A N     1 
ATOM   5005  C  CA    . PHE A 1 624 ? 135.955 122.914 82.965  1.00 43.02 ?  624 PHE A CA    1 
ATOM   5006  C  C     . PHE A 1 624 ? 136.537 124.201 83.536  1.00 41.73 ?  624 PHE A C     1 
ATOM   5007  O  O     . PHE A 1 624 ? 137.374 124.146 84.442  1.00 45.72 ?  624 PHE A O     1 
ATOM   5008  C  CB    . PHE A 1 624 ? 136.752 122.431 81.746  1.00 41.79 ?  624 PHE A CB    1 
ATOM   5009  C  CG    . PHE A 1 624 ? 138.178 122.918 81.702  1.00 45.02 ?  624 PHE A CG    1 
ATOM   5010  C  CD1   . PHE A 1 624 ? 138.500 124.140 81.126  1.00 42.97 ?  624 PHE A CD1   1 
ATOM   5011  C  CD2   . PHE A 1 624 ? 139.197 122.150 82.239  1.00 44.13 ?  624 PHE A CD2   1 
ATOM   5012  C  CE1   . PHE A 1 624 ? 139.808 124.581 81.087  1.00 43.88 ?  624 PHE A CE1   1 
ATOM   5013  C  CE2   . PHE A 1 624 ? 140.508 122.587 82.202  1.00 43.74 ?  624 PHE A CE2   1 
ATOM   5014  C  CZ    . PHE A 1 624 ? 140.812 123.804 81.626  1.00 44.28 ?  624 PHE A CZ    1 
ATOM   5015  N  N     . PHE A 1 625 ? 136.111 125.359 83.025  1.00 35.51 ?  625 PHE A N     1 
ATOM   5016  C  CA    . PHE A 1 625 ? 136.612 126.625 83.545  1.00 34.02 ?  625 PHE A CA    1 
ATOM   5017  C  C     . PHE A 1 625 ? 136.056 126.944 84.925  1.00 33.14 ?  625 PHE A C     1 
ATOM   5018  O  O     . PHE A 1 625 ? 136.657 127.743 85.650  1.00 35.40 ?  625 PHE A O     1 
ATOM   5019  C  CB    . PHE A 1 625 ? 136.287 127.762 82.575  1.00 32.94 ?  625 PHE A CB    1 
ATOM   5020  C  CG    . PHE A 1 625 ? 137.097 127.728 81.313  1.00 34.92 ?  625 PHE A CG    1 
ATOM   5021  C  CD1   . PHE A 1 625 ? 138.437 128.077 81.324  1.00 33.87 ?  625 PHE A CD1   1 
ATOM   5022  C  CD2   . PHE A 1 625 ? 136.520 127.345 80.114  1.00 34.90 ?  625 PHE A CD2   1 
ATOM   5023  C  CE1   . PHE A 1 625 ? 139.186 128.046 80.163  1.00 35.98 ?  625 PHE A CE1   1 
ATOM   5024  C  CE2   . PHE A 1 625 ? 137.262 127.312 78.951  1.00 36.21 ?  625 PHE A CE2   1 
ATOM   5025  C  CZ    . PHE A 1 625 ? 138.597 127.662 78.975  1.00 38.49 ?  625 PHE A CZ    1 
ATOM   5026  N  N     . TYR A 1 626 ? 134.932 126.339 85.306  1.00 29.63 ?  626 TYR A N     1 
ATOM   5027  C  CA    . TYR A 1 626 ? 134.405 126.513 86.653  1.00 32.34 ?  626 TYR A CA    1 
ATOM   5028  C  C     . TYR A 1 626 ? 135.050 125.515 87.603  1.00 31.25 ?  626 TYR A C     1 
ATOM   5029  O  O     . TYR A 1 626 ? 134.355 124.776 88.306  1.00 34.79 ?  626 TYR A O     1 
ATOM   5030  C  CB    . TYR A 1 626 ? 132.884 126.357 86.669  1.00 32.25 ?  626 TYR A CB    1 
ATOM   5031  C  CG    . TYR A 1 626 ? 132.146 127.671 86.589  1.00 31.54 ?  626 TYR A CG    1 
ATOM   5032  C  CD1   . TYR A 1 626 ? 132.146 128.552 87.661  1.00 34.40 ?  626 TYR A CD1   1 
ATOM   5033  C  CD2   . TYR A 1 626 ? 131.449 128.030 85.445  1.00 30.33 ?  626 TYR A CD2   1 
ATOM   5034  C  CE1   . TYR A 1 626 ? 131.478 129.754 87.595  1.00 34.43 ?  626 TYR A CE1   1 
ATOM   5035  C  CE2   . TYR A 1 626 ? 130.775 129.231 85.370  1.00 32.29 ?  626 TYR A CE2   1 
ATOM   5036  C  CZ    . TYR A 1 626 ? 130.794 130.088 86.448  1.00 33.86 ?  626 TYR A CZ    1 
ATOM   5037  O  OH    . TYR A 1 626 ? 130.126 131.287 86.381  1.00 36.02 ?  626 TYR A OH    1 
ATOM   5038  N  N     . LYS A 1 627 ? 136.380 125.493 87.629  1.00 31.15 ?  627 LYS A N     1 
ATOM   5039  C  CA    . LYS A 1 627 ? 137.104 124.564 88.484  1.00 30.24 ?  627 LYS A CA    1 
ATOM   5040  C  C     . LYS A 1 627 ? 136.794 124.836 89.949  1.00 34.65 ?  627 LYS A C     1 
ATOM   5041  O  O     . LYS A 1 627 ? 136.688 125.988 90.376  1.00 40.73 ?  627 LYS A O     1 
ATOM   5042  C  CB    . LYS A 1 627 ? 138.605 124.685 88.226  1.00 35.22 ?  627 LYS A CB    1 
ATOM   5043  C  CG    . LYS A 1 627 ? 139.457 123.641 88.916  1.00 34.08 ?  627 LYS A CG    1 
ATOM   5044  C  CD    . LYS A 1 627 ? 140.889 123.710 88.418  1.00 31.12 ?  627 LYS A CD    1 
ATOM   5045  C  CE    . LYS A 1 627 ? 141.797 122.788 89.207  1.00 36.23 ?  627 LYS A CE    1 
ATOM   5046  N  NZ    . LYS A 1 627 ? 143.228 123.002 88.860  1.00 36.73 1  627 LYS A NZ    1 
ATOM   5047  N  N     . GLU A 1 628 ? 136.629 123.766 90.720  1.00 38.83 ?  628 GLU A N     1 
ATOM   5048  C  CA    . GLU A 1 628 ? 136.351 123.917 92.139  1.00 36.13 ?  628 GLU A CA    1 
ATOM   5049  C  C     . GLU A 1 628 ? 137.594 124.395 92.879  1.00 38.43 ?  628 GLU A C     1 
ATOM   5050  O  O     . GLU A 1 628 ? 138.729 124.117 92.481  1.00 40.81 ?  628 GLU A O     1 
ATOM   5051  C  CB    . GLU A 1 628 ? 135.848 122.601 92.729  1.00 37.33 ?  628 GLU A CB    1 
ATOM   5052  C  CG    . GLU A 1 628 ? 134.412 122.276 92.353  1.00 39.57 ?  628 GLU A CG    1 
ATOM   5053  C  CD    . GLU A 1 628 ? 133.995 120.886 92.780  1.00 43.19 ?  628 GLU A CD    1 
ATOM   5054  O  OE1   . GLU A 1 628 ? 134.744 120.247 93.549  1.00 45.12 ?  628 GLU A OE1   1 
ATOM   5055  O  OE2   . GLU A 1 628 ? 132.916 120.430 92.347  1.00 39.83 -1 628 GLU A OE2   1 
ATOM   5056  N  N     . ALA A 1 629 ? 137.365 125.132 93.969  1.00 39.43 ?  629 ALA A N     1 
ATOM   5057  C  CA    . ALA A 1 629 ? 138.469 125.744 94.702  1.00 33.25 ?  629 ALA A CA    1 
ATOM   5058  C  C     . ALA A 1 629 ? 139.393 124.696 95.305  1.00 35.69 ?  629 ALA A C     1 
ATOM   5059  O  O     . ALA A 1 629 ? 140.615 124.884 95.344  1.00 42.03 ?  629 ALA A O     1 
ATOM   5060  C  CB    . ALA A 1 629 ? 137.924 126.667 95.790  1.00 30.29 ?  629 ALA A CB    1 
ATOM   5061  N  N     . TYR A 1 630 ? 138.829 123.589 95.794  1.00 40.56 ?  630 TYR A N     1 
ATOM   5062  C  CA    . TYR A 1 630 ? 139.650 122.563 96.428  1.00 36.66 ?  630 TYR A CA    1 
ATOM   5063  C  C     . TYR A 1 630 ? 140.583 121.888 95.432  1.00 41.15 ?  630 TYR A C     1 
ATOM   5064  O  O     . TYR A 1 630 ? 141.705 121.516 95.792  1.00 44.81 ?  630 TYR A O     1 
ATOM   5065  C  CB    . TYR A 1 630 ? 138.757 121.529 97.110  1.00 35.20 ?  630 TYR A CB    1 
ATOM   5066  C  CG    . TYR A 1 630 ? 137.825 122.122 98.139  1.00 36.69 ?  630 TYR A CG    1 
ATOM   5067  C  CD1   . TYR A 1 630 ? 138.277 122.439 99.413  1.00 34.53 ?  630 TYR A CD1   1 
ATOM   5068  C  CD2   . TYR A 1 630 ? 136.493 122.368 97.838  1.00 37.62 ?  630 TYR A CD2   1 
ATOM   5069  C  CE1   . TYR A 1 630 ? 137.429 122.981 100.356 1.00 37.48 ?  630 TYR A CE1   1 
ATOM   5070  C  CE2   . TYR A 1 630 ? 135.638 122.910 98.775  1.00 38.03 ?  630 TYR A CE2   1 
ATOM   5071  C  CZ    . TYR A 1 630 ? 136.112 123.216 100.032 1.00 44.44 ?  630 TYR A CZ    1 
ATOM   5072  O  OH    . TYR A 1 630 ? 135.262 123.756 100.969 1.00 44.97 ?  630 TYR A OH    1 
ATOM   5073  N  N     . ASP A 1 631 ? 140.146 121.722 94.185  1.00 38.93 ?  631 ASP A N     1 
ATOM   5074  C  CA    . ASP A 1 631 ? 140.990 121.133 93.154  1.00 38.97 ?  631 ASP A CA    1 
ATOM   5075  C  C     . ASP A 1 631 ? 142.092 122.070 92.682  1.00 41.98 ?  631 ASP A C     1 
ATOM   5076  O  O     . ASP A 1 631 ? 143.012 121.619 91.991  1.00 43.81 ?  631 ASP A O     1 
ATOM   5077  C  CB    . ASP A 1 631 ? 140.137 120.709 91.956  1.00 39.94 ?  631 ASP A CB    1 
ATOM   5078  C  CG    . ASP A 1 631 ? 139.023 119.758 92.342  1.00 45.71 ?  631 ASP A CG    1 
ATOM   5079  O  OD1   . ASP A 1 631 ? 139.222 118.952 93.274  1.00 46.44 ?  631 ASP A OD1   1 
ATOM   5080  O  OD2   . ASP A 1 631 ? 137.945 119.818 91.713  1.00 43.66 -1 631 ASP A OD2   1 
ATOM   5081  N  N     . MET A 1 632 ? 142.027 123.349 93.039  1.00 35.51 ?  632 MET A N     1 
ATOM   5082  C  CA    . MET A 1 632 ? 142.983 124.329 92.552  1.00 32.76 ?  632 MET A CA    1 
ATOM   5083  C  C     . MET A 1 632 ? 144.268 124.300 93.374  1.00 37.18 ?  632 MET A C     1 
ATOM   5084  O  O     . MET A 1 632 ? 144.294 123.866 94.529  1.00 35.27 ?  632 MET A O     1 
ATOM   5085  C  CB    . MET A 1 632 ? 142.382 125.732 92.593  1.00 31.39 ?  632 MET A CB    1 
ATOM   5086  C  CG    . MET A 1 632 ? 141.314 125.981 91.551  1.00 35.86 ?  632 MET A CG    1 
ATOM   5087  S  SD    . MET A 1 632 ? 140.732 127.683 91.571  1.00 39.76 ?  632 MET A SD    1 
ATOM   5088  C  CE    . MET A 1 632 ? 139.421 127.589 90.362  1.00 33.94 ?  632 MET A CE    1 
ATOM   5089  N  N     . ASP A 1 633 ? 145.343 124.777 92.755  1.00 33.46 ?  633 ASP A N     1 
ATOM   5090  C  CA    . ASP A 1 633 ? 146.607 124.973 93.452  1.00 31.47 ?  633 ASP A CA    1 
ATOM   5091  C  C     . ASP A 1 633 ? 146.502 126.223 94.315  1.00 31.69 ?  633 ASP A C     1 
ATOM   5092  O  O     . ASP A 1 633 ? 146.259 127.319 93.799  1.00 35.01 ?  633 ASP A O     1 
ATOM   5093  C  CB    . ASP A 1 633 ? 147.754 125.096 92.452  1.00 29.78 ?  633 ASP A CB    1 
ATOM   5094  C  CG    . ASP A 1 633 ? 149.116 125.077 93.118  1.00 36.13 ?  633 ASP A CG    1 
ATOM   5095  O  OD1   . ASP A 1 633 ? 149.184 124.846 94.343  1.00 38.03 ?  633 ASP A OD1   1 
ATOM   5096  O  OD2   . ASP A 1 633 ? 150.123 125.298 92.413  1.00 37.92 -1 633 ASP A OD2   1 
ATOM   5097  N  N     . MET A 1 634 ? 146.679 126.061 95.627  1.00 27.77 ?  634 MET A N     1 
ATOM   5098  C  CA    . MET A 1 634 ? 146.538 127.192 96.535  1.00 25.57 ?  634 MET A CA    1 
ATOM   5099  C  C     . MET A 1 634 ? 147.613 128.249 96.325  1.00 27.47 ?  634 MET A C     1 
ATOM   5100  O  O     . MET A 1 634 ? 147.394 129.409 96.684  1.00 26.26 ?  634 MET A O     1 
ATOM   5101  C  CB    . MET A 1 634 ? 146.554 126.710 97.985  1.00 27.41 ?  634 MET A CB    1 
ATOM   5102  C  CG    . MET A 1 634 ? 145.190 126.292 98.503  1.00 28.92 ?  634 MET A CG    1 
ATOM   5103  S  SD    . MET A 1 634 ? 143.968 127.608 98.344  1.00 43.53 ?  634 MET A SD    1 
ATOM   5104  C  CE    . MET A 1 634 ? 142.835 126.877 97.165  1.00 28.34 ?  634 MET A CE    1 
ATOM   5105  N  N     . PHE A 1 635 ? 148.759 127.882 95.750  1.00 26.68 ?  635 PHE A N     1 
ATOM   5106  C  CA    . PHE A 1 635 ? 149.779 128.880 95.450  1.00 23.26 ?  635 PHE A CA    1 
ATOM   5107  C  C     . PHE A 1 635 ? 149.301 129.852 94.377  1.00 21.66 ?  635 PHE A C     1 
ATOM   5108  O  O     . PHE A 1 635 ? 149.546 131.059 94.471  1.00 25.79 ?  635 PHE A O     1 
ATOM   5109  C  CB    . PHE A 1 635 ? 151.077 128.196 95.021  1.00 23.22 ?  635 PHE A CB    1 
ATOM   5110  C  CG    . PHE A 1 635 ? 151.968 127.817 96.169  1.00 24.30 ?  635 PHE A CG    1 
ATOM   5111  C  CD1   . PHE A 1 635 ? 151.448 127.208 97.298  1.00 23.65 ?  635 PHE A CD1   1 
ATOM   5112  C  CD2   . PHE A 1 635 ? 153.327 128.071 96.119  1.00 27.13 ?  635 PHE A CD2   1 
ATOM   5113  C  CE1   . PHE A 1 635 ? 152.265 126.859 98.354  1.00 22.91 ?  635 PHE A CE1   1 
ATOM   5114  C  CE2   . PHE A 1 635 ? 154.150 127.725 97.173  1.00 29.75 ?  635 PHE A CE2   1 
ATOM   5115  C  CZ    . PHE A 1 635 ? 153.617 127.118 98.291  1.00 26.44 ?  635 PHE A CZ    1 
ATOM   5116  N  N     . LYS A 1 636 ? 148.601 129.350 93.360  1.00 23.36 ?  636 LYS A N     1 
ATOM   5117  C  CA    . LYS A 1 636 ? 148.090 130.233 92.317  1.00 26.62 ?  636 LYS A CA    1 
ATOM   5118  C  C     . LYS A 1 636 ? 146.916 131.069 92.815  1.00 27.24 ?  636 LYS A C     1 
ATOM   5119  O  O     . LYS A 1 636 ? 146.753 132.222 92.396  1.00 32.63 ?  636 LYS A O     1 
ATOM   5120  C  CB    . LYS A 1 636 ? 147.701 129.412 91.090  1.00 28.33 ?  636 LYS A CB    1 
ATOM   5121  C  CG    . LYS A 1 636 ? 148.899 128.785 90.393  1.00 28.04 ?  636 LYS A CG    1 
ATOM   5122  C  CD    . LYS A 1 636 ? 148.489 127.963 89.188  1.00 33.47 ?  636 LYS A CD    1 
ATOM   5123  C  CE    . LYS A 1 636 ? 149.650 127.138 88.659  1.00 32.60 ?  636 LYS A CE    1 
ATOM   5124  N  NZ    . LYS A 1 636 ? 149.203 126.146 87.644  1.00 33.68 1  636 LYS A NZ    1 
ATOM   5125  N  N     . VAL A 1 637 ? 146.101 130.519 93.717  1.00 23.94 ?  637 VAL A N     1 
ATOM   5126  C  CA    . VAL A 1 637 ? 145.064 131.319 94.363  1.00 16.29 ?  637 VAL A CA    1 
ATOM   5127  C  C     . VAL A 1 637 ? 145.697 132.432 95.190  1.00 23.84 ?  637 VAL A C     1 
ATOM   5128  O  O     . VAL A 1 637 ? 145.217 133.572 95.194  1.00 27.23 ?  637 VAL A O     1 
ATOM   5129  C  CB    . VAL A 1 637 ? 144.150 130.423 95.218  1.00 20.35 ?  637 VAL A CB    1 
ATOM   5130  C  CG1   . VAL A 1 637 ? 142.987 131.226 95.775  1.00 21.92 ?  637 VAL A CG1   1 
ATOM   5131  C  CG2   . VAL A 1 637 ? 143.645 129.250 94.397  1.00 25.87 ?  637 VAL A CG2   1 
ATOM   5132  N  N     . VAL A 1 638 ? 146.785 132.119 95.898  1.00 25.45 ?  638 VAL A N     1 
ATOM   5133  C  CA    . VAL A 1 638 ? 147.521 133.141 96.640  1.00 21.79 ?  638 VAL A CA    1 
ATOM   5134  C  C     . VAL A 1 638 ? 148.062 134.199 95.690  1.00 17.02 ?  638 VAL A C     1 
ATOM   5135  O  O     . VAL A 1 638 ? 148.035 135.397 95.992  1.00 25.22 ?  638 VAL A O     1 
ATOM   5136  C  CB    . VAL A 1 638 ? 148.650 132.495 97.466  1.00 20.12 ?  638 VAL A CB    1 
ATOM   5137  C  CG1   . VAL A 1 638 ? 149.677 133.537 97.876  1.00 15.90 ?  638 VAL A CG1   1 
ATOM   5138  C  CG2   . VAL A 1 638 ? 148.089 131.798 98.690  1.00 18.74 ?  638 VAL A CG2   1 
ATOM   5139  N  N     . ASP A 1 639 ? 148.573 133.774 94.534  1.00 20.16 ?  639 ASP A N     1 
ATOM   5140  C  CA    . ASP A 1 639 ? 149.096 134.725 93.557  1.00 17.42 ?  639 ASP A CA    1 
ATOM   5141  C  C     . ASP A 1 639 ? 148.004 135.667 93.064  1.00 23.65 ?  639 ASP A C     1 
ATOM   5142  O  O     . ASP A 1 639 ? 148.219 136.881 92.965  1.00 34.49 ?  639 ASP A O     1 
ATOM   5143  C  CB    . ASP A 1 639 ? 149.724 133.976 92.383  1.00 22.23 ?  639 ASP A CB    1 
ATOM   5144  C  CG    . ASP A 1 639 ? 151.096 133.427 92.709  1.00 30.93 ?  639 ASP A CG    1 
ATOM   5145  O  OD1   . ASP A 1 639 ? 151.851 134.105 93.436  1.00 31.40 ?  639 ASP A OD1   1 
ATOM   5146  O  OD2   . ASP A 1 639 ? 151.420 132.316 92.240  1.00 30.53 -1 639 ASP A OD2   1 
ATOM   5147  N  N     . MET A 1 640 ? 146.823 135.126 92.759  1.00 23.94 ?  640 MET A N     1 
ATOM   5148  C  CA    . MET A 1 640 ? 145.714 135.972 92.328  1.00 17.59 ?  640 MET A CA    1 
ATOM   5149  C  C     . MET A 1 640 ? 145.278 136.926 93.434  1.00 19.97 ?  640 MET A C     1 
ATOM   5150  O  O     . MET A 1 640 ? 145.010 138.110 93.180  1.00 30.73 ?  640 MET A O     1 
ATOM   5151  C  CB    . MET A 1 640 ? 144.536 135.111 91.875  1.00 23.08 ?  640 MET A CB    1 
ATOM   5152  C  CG    . MET A 1 640 ? 143.185 135.786 92.048  1.00 26.44 ?  640 MET A CG    1 
ATOM   5153  S  SD    . MET A 1 640 ? 142.597 136.589 90.547  1.00 31.92 ?  640 MET A SD    1 
ATOM   5154  C  CE    . MET A 1 640 ? 142.525 135.202 89.426  1.00 23.12 ?  640 MET A CE    1 
ATOM   5155  N  N     . ILE A 1 641 ? 145.195 136.431 94.670  1.00 15.77 ?  641 ILE A N     1 
ATOM   5156  C  CA    . ILE A 1 641 ? 144.753 137.286 95.764  1.00 18.94 ?  641 ILE A CA    1 
ATOM   5157  C  C     . ILE A 1 641 ? 145.774 138.381 96.038  1.00 19.32 ?  641 ILE A C     1 
ATOM   5158  O  O     . ILE A 1 641 ? 145.402 139.508 96.363  1.00 24.40 ?  641 ILE A O     1 
ATOM   5159  C  CB    . ILE A 1 641 ? 144.450 136.443 97.017  1.00 20.90 ?  641 ILE A CB    1 
ATOM   5160  C  CG1   . ILE A 1 641 ? 143.279 135.502 96.739  1.00 17.33 ?  641 ILE A CG1   1 
ATOM   5161  C  CG2   . ILE A 1 641 ? 144.102 137.334 98.197  1.00 16.43 ?  641 ILE A CG2   1 
ATOM   5162  C  CD1   . ILE A 1 641 ? 142.170 136.136 95.925  1.00 20.72 ?  641 ILE A CD1   1 
ATOM   5163  N  N     . ALA A 1 642 ? 147.067 138.086 95.889  1.00 15.52 ?  642 ALA A N     1 
ATOM   5164  C  CA    . ALA A 1 642 ? 148.089 139.119 96.039  1.00 16.76 ?  642 ALA A CA    1 
ATOM   5165  C  C     . ALA A 1 642 ? 148.021 140.132 94.905  1.00 19.56 ?  642 ALA A C     1 
ATOM   5166  O  O     . ALA A 1 642 ? 148.211 141.338 95.122  1.00 30.33 ?  642 ALA A O     1 
ATOM   5167  C  CB    . ALA A 1 642 ? 149.475 138.480 96.105  1.00 17.60 ?  642 ALA A CB    1 
ATOM   5168  N  N     . THR A 1 643 ? 147.753 139.659 93.686  1.00 16.40 ?  643 THR A N     1 
ATOM   5169  C  CA    . THR A 1 643 ? 147.582 140.563 92.556  1.00 16.82 ?  643 THR A CA    1 
ATOM   5170  C  C     . THR A 1 643 ? 146.434 141.532 92.805  1.00 20.72 ?  643 THR A C     1 
ATOM   5171  O  O     . THR A 1 643 ? 146.547 142.729 92.519  1.00 23.15 ?  643 THR A O     1 
ATOM   5172  C  CB    . THR A 1 643 ? 147.341 139.755 91.281  1.00 18.01 ?  643 THR A CB    1 
ATOM   5173  O  OG1   . THR A 1 643 ? 148.530 139.030 90.942  1.00 22.20 ?  643 THR A OG1   1 
ATOM   5174  C  CG2   . THR A 1 643 ? 146.968 140.664 90.134  1.00 14.96 ?  643 THR A CG2   1 
ATOM   5175  N  N     . ILE A 1 644 ? 145.323 141.034 93.345  1.00 17.72 ?  644 ILE A N     1 
ATOM   5176  C  CA    . ILE A 1 644 ? 144.217 141.921 93.696  1.00 11.61 ?  644 ILE A CA    1 
ATOM   5177  C  C     . ILE A 1 644 ? 144.600 142.825 94.864  1.00 15.14 ?  644 ILE A C     1 
ATOM   5178  O  O     . ILE A 1 644 ? 144.290 144.022 94.868  1.00 19.99 ?  644 ILE A O     1 
ATOM   5179  C  CB    . ILE A 1 644 ? 142.951 141.102 94.004  1.00 15.27 ?  644 ILE A CB    1 
ATOM   5180  C  CG1   . ILE A 1 644 ? 142.556 140.251 92.799  1.00 18.05 ?  644 ILE A CG1   1 
ATOM   5181  C  CG2   . ILE A 1 644 ? 141.812 142.022 94.399  1.00 9.24  ?  644 ILE A CG2   1 
ATOM   5182  C  CD1   . ILE A 1 644 ? 141.547 139.175 93.123  1.00 21.85 ?  644 ILE A CD1   1 
ATOM   5183  N  N     . GLN A 1 645 ? 145.288 142.270 95.866  1.00 13.04 ?  645 GLN A N     1 
ATOM   5184  C  CA    . GLN A 1 645 ? 145.603 143.001 97.087  1.00 14.10 ?  645 GLN A CA    1 
ATOM   5185  C  C     . GLN A 1 645 ? 146.532 144.174 96.825  1.00 15.57 ?  645 GLN A C     1 
ATOM   5186  O  O     . GLN A 1 645 ? 146.505 145.162 97.567  1.00 19.84 ?  645 GLN A O     1 
ATOM   5187  C  CB    . GLN A 1 645 ? 146.228 142.052 98.109  1.00 12.50 ?  645 GLN A CB    1 
ATOM   5188  C  CG    . GLN A 1 645 ? 146.477 142.667 99.472  1.00 8.73  ?  645 GLN A CG    1 
ATOM   5189  C  CD    . GLN A 1 645 ? 145.195 142.917 100.234 1.00 11.82 ?  645 GLN A CD    1 
ATOM   5190  O  OE1   . GLN A 1 645 ? 144.689 142.034 100.924 1.00 17.05 ?  645 GLN A OE1   1 
ATOM   5191  N  NE2   . GLN A 1 645 ? 144.661 144.125 100.114 1.00 6.56  ?  645 GLN A NE2   1 
ATOM   5192  N  N     . GLN A 1 646 ? 147.357 144.088 95.784  1.00 20.80 ?  646 GLN A N     1 
ATOM   5193  C  CA    . GLN A 1 646 ? 148.224 145.216 95.475  1.00 14.50 ?  646 GLN A CA    1 
ATOM   5194  C  C     . GLN A 1 646 ? 147.441 146.458 95.061  1.00 13.51 ?  646 GLN A C     1 
ATOM   5195  O  O     . GLN A 1 646 ? 148.016 147.549 95.036  1.00 17.75 ?  646 GLN A O     1 
ATOM   5196  C  CB    . GLN A 1 646 ? 149.224 144.831 94.384  1.00 17.94 ?  646 GLN A CB    1 
ATOM   5197  C  CG    . GLN A 1 646 ? 148.702 144.964 92.973  1.00 21.82 ?  646 GLN A CG    1 
ATOM   5198  C  CD    . GLN A 1 646 ? 149.641 144.357 91.952  1.00 26.95 ?  646 GLN A CD    1 
ATOM   5199  O  OE1   . GLN A 1 646 ? 150.761 144.828 91.766  1.00 25.36 ?  646 GLN A OE1   1 
ATOM   5200  N  NE2   . GLN A 1 646 ? 149.189 143.302 91.285  1.00 22.86 ?  646 GLN A NE2   1 
ATOM   5201  N  N     . HIS A 1 647 ? 146.149 146.324 94.754  1.00 21.28 ?  647 HIS A N     1 
ATOM   5202  C  CA    . HIS A 1 647 ? 145.303 147.459 94.407  1.00 14.87 ?  647 HIS A CA    1 
ATOM   5203  C  C     . HIS A 1 647 ? 144.212 147.720 95.437  1.00 11.61 ?  647 HIS A C     1 
ATOM   5204  O  O     . HIS A 1 647 ? 143.364 148.592 95.217  1.00 19.13 ?  647 HIS A O     1 
ATOM   5205  C  CB    . HIS A 1 647 ? 144.673 147.249 93.028  1.00 10.26 ?  647 HIS A CB    1 
ATOM   5206  C  CG    . HIS A 1 647 ? 145.670 146.971 91.950  1.00 15.52 ?  647 HIS A CG    1 
ATOM   5207  N  ND1   . HIS A 1 647 ? 146.625 147.889 91.568  1.00 16.09 ?  647 HIS A ND1   1 
ATOM   5208  C  CD2   . HIS A 1 647 ? 145.868 145.878 91.179  1.00 13.32 ?  647 HIS A CD2   1 
ATOM   5209  C  CE1   . HIS A 1 647 ? 147.366 147.374 90.605  1.00 18.02 ?  647 HIS A CE1   1 
ATOM   5210  N  NE2   . HIS A 1 647 ? 146.928 146.154 90.350  1.00 19.55 ?  647 HIS A NE2   1 
ATOM   5211  N  N     . ILE A 1 648 ? 144.207 146.993 96.549  1.00 11.14 ?  648 ILE A N     1 
ATOM   5212  C  CA    . ILE A 1 648 ? 143.216 147.158 97.607  1.00 13.31 ?  648 ILE A CA    1 
ATOM   5213  C  C     . ILE A 1 648 ? 143.929 147.711 98.834  1.00 13.02 ?  648 ILE A C     1 
ATOM   5214  O  O     . ILE A 1 648 ? 144.911 147.125 99.303  1.00 23.58 ?  648 ILE A O     1 
ATOM   5215  C  CB    . ILE A 1 648 ? 142.507 145.832 97.926  1.00 11.46 ?  648 ILE A CB    1 
ATOM   5216  C  CG1   . ILE A 1 648 ? 141.895 145.226 96.660  1.00 7.66  ?  648 ILE A CG1   1 
ATOM   5217  C  CG2   . ILE A 1 648 ? 141.437 146.037 98.982  1.00 9.21  ?  648 ILE A CG2   1 
ATOM   5218  C  CD1   . ILE A 1 648 ? 140.723 146.005 96.107  1.00 9.58  ?  648 ILE A CD1   1 
ATOM   5219  N  N     . ASP A 1 649 ? 143.441 148.844 99.346  1.00 6.66  ?  649 ASP A N     1 
ATOM   5220  C  CA    . ASP A 1 649 ? 144.093 149.471 100.492 1.00 11.95 ?  649 ASP A CA    1 
ATOM   5221  C  C     . ASP A 1 649 ? 143.874 148.664 101.764 1.00 9.56  ?  649 ASP A C     1 
ATOM   5222  O  O     . ASP A 1 649 ? 144.778 148.554 102.599 1.00 28.87 ?  649 ASP A O     1 
ATOM   5223  C  CB    . ASP A 1 649 ? 143.592 150.905 100.665 1.00 21.67 ?  649 ASP A CB    1 
ATOM   5224  C  CG    . ASP A 1 649 ? 142.101 151.029 100.456 1.00 18.65 ?  649 ASP A CG    1 
ATOM   5225  O  OD1   . ASP A 1 649 ? 141.548 150.253 99.652  1.00 24.11 ?  649 ASP A OD1   1 
ATOM   5226  O  OD2   . ASP A 1 649 ? 141.480 151.903 101.093 1.00 15.97 -1 649 ASP A OD2   1 
ATOM   5227  N  N     . GLN A 1 650 ? 142.685 148.101 101.936 1.00 10.05 ?  650 GLN A N     1 
ATOM   5228  C  CA    . GLN A 1 650 ? 142.407 147.206 103.047 1.00 6.55  ?  650 GLN A CA    1 
ATOM   5229  C  C     . GLN A 1 650 ? 142.688 145.770 102.601 1.00 5.55  ?  650 GLN A C     1 
ATOM   5230  O  O     . GLN A 1 650 ? 143.318 145.542 101.565 1.00 16.73 ?  650 GLN A O     1 
ATOM   5231  C  CB    . GLN A 1 650 ? 140.973 147.413 103.542 1.00 3.48  ?  650 GLN A CB    1 
ATOM   5232  C  CG    . GLN A 1 650 ? 140.683 148.822 104.023 1.00 4.86  ?  650 GLN A CG    1 
ATOM   5233  C  CD    . GLN A 1 650 ? 139.250 148.997 104.468 1.00 10.24 ?  650 GLN A CD    1 
ATOM   5234  O  OE1   . GLN A 1 650 ? 138.852 148.498 105.519 1.00 21.25 ?  650 GLN A OE1   1 
ATOM   5235  N  NE2   . GLN A 1 650 ? 138.465 149.707 103.670 1.00 5.10  ?  650 GLN A NE2   1 
ATOM   5236  N  N     . GLY A 1 651 ? 142.241 144.786 103.379 1.00 6.66  ?  651 GLY A N     1 
ATOM   5237  C  CA    . GLY A 1 651 ? 142.503 143.399 103.070 1.00 8.64  ?  651 GLY A CA    1 
ATOM   5238  C  C     . GLY A 1 651 ? 141.410 142.754 102.240 1.00 6.35  ?  651 GLY A C     1 
ATOM   5239  O  O     . GLY A 1 651 ? 140.399 143.359 101.889 1.00 9.60  ?  651 GLY A O     1 
ATOM   5240  N  N     . ILE A 1 652 ? 141.640 141.484 101.925 1.00 18.34 ?  652 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 652 ? 140.706 140.653 101.179 1.00 8.90  ?  652 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 652 ? 140.402 139.427 102.023 1.00 7.64  ?  652 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 652 ? 141.321 138.792 102.553 1.00 19.66 ?  652 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 652 ? 141.279 140.238 99.812  1.00 6.86  ?  652 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 652 ? 141.662 141.468 98.991  1.00 0.00  ?  652 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 652 ? 140.289 139.370 99.057  1.00 10.78 ?  652 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 652 ? 142.553 141.146 97.822  1.00 4.02  ?  652 ILE A CD1   1 
ATOM   5248  N  N     . SER A 1 653 ? 139.122 139.098 102.157 1.00 15.16 ?  653 SER A N     1 
ATOM   5249  C  CA    . SER A 1 653 ? 138.733 137.874 102.852 1.00 12.99 ?  653 SER A CA    1 
ATOM   5250  C  C     . SER A 1 653 ? 139.214 136.692 102.023 1.00 13.55 ?  653 SER A C     1 
ATOM   5251  O  O     . SER A 1 653 ? 138.617 136.344 101.003 1.00 26.18 ?  653 SER A O     1 
ATOM   5252  C  CB    . SER A 1 653 ? 137.227 137.830 103.069 1.00 12.53 ?  653 SER A CB    1 
ATOM   5253  O  OG    . SER A 1 653 ? 136.900 138.130 104.413 1.00 15.77 ?  653 SER A OG    1 
ATOM   5254  N  N     . PHE A 1 654 ? 140.302 136.073 102.464 1.00 18.67 ?  654 PHE A N     1 
ATOM   5255  C  CA    . PHE A 1 654 ? 141.003 135.043 101.702 1.00 9.68  ?  654 PHE A CA    1 
ATOM   5256  C  C     . PHE A 1 654 ? 140.871 133.725 102.456 1.00 15.65 ?  654 PHE A C     1 
ATOM   5257  O  O     . PHE A 1 654 ? 141.575 133.487 103.440 1.00 24.30 ?  654 PHE A O     1 
ATOM   5258  C  CB    . PHE A 1 654 ? 142.463 135.436 101.499 1.00 9.20  ?  654 PHE A CB    1 
ATOM   5259  C  CG    . PHE A 1 654 ? 143.248 134.474 100.651 1.00 16.73 ?  654 PHE A CG    1 
ATOM   5260  C  CD1   . PHE A 1 654 ? 142.611 133.580 99.807  1.00 22.93 ?  654 PHE A CD1   1 
ATOM   5261  C  CD2   . PHE A 1 654 ? 144.630 134.470 100.700 1.00 18.70 ?  654 PHE A CD2   1 
ATOM   5262  C  CE1   . PHE A 1 654 ? 143.336 132.700 99.033  1.00 14.90 ?  654 PHE A CE1   1 
ATOM   5263  C  CE2   . PHE A 1 654 ? 145.359 133.594 99.926  1.00 20.49 ?  654 PHE A CE2   1 
ATOM   5264  C  CZ    . PHE A 1 654 ? 144.711 132.707 99.093  1.00 15.99 ?  654 PHE A CZ    1 
ATOM   5265  N  N     . THR A 1 655 ? 139.975 132.868 101.979 1.00 20.69 ?  655 THR A N     1 
ATOM   5266  C  CA    . THR A 1 655 ? 139.784 131.545 102.552 1.00 16.46 ?  655 THR A CA    1 
ATOM   5267  C  C     . THR A 1 655 ? 140.655 130.538 101.812 1.00 23.11 ?  655 THR A C     1 
ATOM   5268  O  O     . THR A 1 655 ? 140.651 130.494 100.579 1.00 28.79 ?  655 THR A O     1 
ATOM   5269  C  CB    . THR A 1 655 ? 138.313 131.133 102.473 1.00 23.48 ?  655 THR A CB    1 
ATOM   5270  O  OG1   . THR A 1 655 ? 137.549 131.893 103.418 1.00 23.66 ?  655 THR A OG1   1 
ATOM   5271  C  CG2   . THR A 1 655 ? 138.149 129.651 102.770 1.00 24.36 ?  655 THR A CG2   1 
ATOM   5272  N  N     . LEU A 1 656 ? 141.413 129.748 102.568 1.00 31.95 ?  656 LEU A N     1 
ATOM   5273  C  CA    . LEU A 1 656 ? 142.158 128.643 101.987 1.00 28.61 ?  656 LEU A CA    1 
ATOM   5274  C  C     . LEU A 1 656 ? 141.231 127.455 101.776 1.00 27.54 ?  656 LEU A C     1 
ATOM   5275  O  O     . LEU A 1 656 ? 140.369 127.170 102.609 1.00 31.16 ?  656 LEU A O     1 
ATOM   5276  C  CB    . LEU A 1 656 ? 143.322 128.239 102.891 1.00 29.59 ?  656 LEU A CB    1 
ATOM   5277  C  CG    . LEU A 1 656 ? 144.396 129.299 103.128 1.00 30.46 ?  656 LEU A CG    1 
ATOM   5278  C  CD1   . LEU A 1 656 ? 145.595 128.695 103.840 1.00 26.80 ?  656 LEU A CD1   1 
ATOM   5279  C  CD2   . LEU A 1 656 ? 144.807 129.952 101.819 1.00 27.73 ?  656 LEU A CD2   1 
ATOM   5280  N  N     . PHE A 1 657 ? 141.402 126.771 100.650 1.00 26.53 ?  657 PHE A N     1 
ATOM   5281  C  CA    . PHE A 1 657 ? 140.591 125.607 100.308 1.00 28.20 ?  657 PHE A CA    1 
ATOM   5282  C  C     . PHE A 1 657 ? 141.515 124.404 100.206 1.00 36.33 ?  657 PHE A C     1 
ATOM   5283  O  O     . PHE A 1 657 ? 142.278 124.282 99.241  1.00 37.74 ?  657 PHE A O     1 
ATOM   5284  C  CB    . PHE A 1 657 ? 139.825 125.838 99.009  1.00 29.41 ?  657 PHE A CB    1 
ATOM   5285  C  CG    . PHE A 1 657 ? 138.990 127.083 99.018  1.00 32.69 ?  657 PHE A CG    1 
ATOM   5286  C  CD1   . PHE A 1 657 ? 137.717 127.075 99.558  1.00 30.22 ?  657 PHE A CD1   1 
ATOM   5287  C  CD2   . PHE A 1 657 ? 139.478 128.265 98.485  1.00 33.87 ?  657 PHE A CD2   1 
ATOM   5288  C  CE1   . PHE A 1 657 ? 136.949 128.221 99.569  1.00 32.64 ?  657 PHE A CE1   1 
ATOM   5289  C  CE2   . PHE A 1 657 ? 138.712 129.411 98.489  1.00 29.81 ?  657 PHE A CE2   1 
ATOM   5290  C  CZ    . PHE A 1 657 ? 137.447 129.390 99.034  1.00 32.98 ?  657 PHE A CZ    1 
ATOM   5291  N  N     . LEU A 1 658 ? 141.447 123.520 101.193 1.00 40.31 ?  658 LEU A N     1 
ATOM   5292  C  CA    . LEU A 1 658 ? 142.377 122.412 101.319 1.00 42.67 ?  658 LEU A CA    1 
ATOM   5293  C  C     . LEU A 1 658 ? 141.658 121.085 101.131 1.00 45.45 ?  658 LEU A C     1 
ATOM   5294  O  O     . LEU A 1 658 ? 140.460 120.960 101.400 1.00 46.68 ?  658 LEU A O     1 
ATOM   5295  C  CB    . LEU A 1 658 ? 143.063 122.432 102.686 1.00 40.37 ?  658 LEU A CB    1 
ATOM   5296  C  CG    . LEU A 1 658 ? 143.346 123.816 103.271 1.00 39.41 ?  658 LEU A CG    1 
ATOM   5297  C  CD1   . LEU A 1 658 ? 143.627 123.707 104.757 1.00 41.38 ?  658 LEU A CD1   1 
ATOM   5298  C  CD2   . LEU A 1 658 ? 144.501 124.489 102.548 1.00 42.05 ?  658 LEU A CD2   1 
ATOM   5299  N  N     . LYS A 1 659 ? 142.401 120.102 100.639 1.00 51.27 ?  659 LYS A N     1 
ATOM   5300  C  CA    . LYS A 1 659 ? 141.941 118.724 100.609 1.00 51.78 ?  659 LYS A CA    1 
ATOM   5301  C  C     . LYS A 1 659 ? 142.300 118.035 101.921 1.00 52.89 ?  659 LYS A C     1 
ATOM   5302  O  O     . LYS A 1 659 ? 143.214 118.447 102.638 1.00 54.58 ?  659 LYS A O     1 
ATOM   5303  C  CB    . LYS A 1 659 ? 142.559 117.973 99.429  1.00 54.80 ?  659 LYS A CB    1 
ATOM   5304  C  CG    . LYS A 1 659 ? 142.310 118.623 98.079  1.00 53.58 ?  659 LYS A CG    1 
ATOM   5305  C  CD    . LYS A 1 659 ? 142.757 117.719 96.941  1.00 53.18 ?  659 LYS A CD    1 
ATOM   5306  C  CE    . LYS A 1 659 ? 142.485 118.357 95.588  1.00 53.02 ?  659 LYS A CE    1 
ATOM   5307  N  NZ    . LYS A 1 659 ? 142.571 117.370 94.477  1.00 52.86 1  659 LYS A NZ    1 
ATOM   5308  N  N     . ASP A 1 660 ? 141.556 116.973 102.234 1.00 57.82 ?  660 ASP A N     1 
ATOM   5309  C  CA    . ASP A 1 660 ? 141.845 116.204 103.437 1.00 57.29 ?  660 ASP A CA    1 
ATOM   5310  C  C     . ASP A 1 660 ? 143.189 115.492 103.359 1.00 55.49 ?  660 ASP A C     1 
ATOM   5311  O  O     . ASP A 1 660 ? 143.730 115.098 104.397 1.00 56.14 ?  660 ASP A O     1 
ATOM   5312  C  CB    . ASP A 1 660 ? 140.728 115.192 103.698 1.00 58.51 ?  660 ASP A CB    1 
ATOM   5313  C  CG    . ASP A 1 660 ? 140.176 114.592 102.421 1.00 61.52 ?  660 ASP A CG    1 
ATOM   5314  O  OD1   . ASP A 1 660 ? 140.978 114.167 101.563 1.00 59.08 ?  660 ASP A OD1   1 
ATOM   5315  O  OD2   . ASP A 1 660 ? 138.936 114.547 102.273 1.00 61.60 -1 660 ASP A OD2   1 
ATOM   5316  N  N     . THR A 1 661 ? 143.738 115.321 102.154 1.00 53.18 ?  661 THR A N     1 
ATOM   5317  C  CA    . THR A 1 661 ? 145.004 114.610 102.012 1.00 55.32 ?  661 THR A CA    1 
ATOM   5318  C  C     . THR A 1 661 ? 146.180 115.457 102.484 1.00 54.64 ?  661 THR A C     1 
ATOM   5319  O  O     . THR A 1 661 ? 147.104 114.939 103.122 1.00 55.17 ?  661 THR A O     1 
ATOM   5320  C  CB    . THR A 1 661 ? 145.207 114.181 100.559 1.00 56.55 ?  661 THR A CB    1 
ATOM   5321  O  OG1   . THR A 1 661 ? 145.765 115.269 99.812  1.00 56.41 ?  661 THR A OG1   1 
ATOM   5322  C  CG2   . THR A 1 661 ? 143.883 113.770 99.935  1.00 54.38 ?  661 THR A CG2   1 
ATOM   5323  N  N     . MET A 1 662 ? 146.169 116.753 102.180 1.00 52.78 ?  662 MET A N     1 
ATOM   5324  C  CA    . MET A 1 662 ? 147.298 117.599 102.538 1.00 52.47 ?  662 MET A CA    1 
ATOM   5325  C  C     . MET A 1 662 ? 147.383 117.780 104.050 1.00 51.28 ?  662 MET A C     1 
ATOM   5326  O  O     . MET A 1 662 ? 146.375 117.791 104.762 1.00 49.11 ?  662 MET A O     1 
ATOM   5327  C  CB    . MET A 1 662 ? 147.208 118.955 101.833 1.00 50.11 ?  662 MET A CB    1 
ATOM   5328  C  CG    . MET A 1 662 ? 146.632 120.088 102.663 1.00 51.94 ?  662 MET A CG    1 
ATOM   5329  S  SD    . MET A 1 662 ? 146.499 121.602 101.695 1.00 62.99 ?  662 MET A SD    1 
ATOM   5330  C  CE    . MET A 1 662 ? 145.566 121.020 100.285 1.00 48.13 ?  662 MET A CE    1 
ATOM   5331  N  N     . THR A 1 663 ? 148.613 117.901 104.535 1.00 45.64 ?  663 THR A N     1 
ATOM   5332  C  CA    . THR A 1 663 ? 148.920 117.914 105.953 1.00 44.52 ?  663 THR A CA    1 
ATOM   5333  C  C     . THR A 1 663 ? 149.115 119.348 106.439 1.00 44.92 ?  663 THR A C     1 
ATOM   5334  O  O     . THR A 1 663 ? 148.906 120.314 105.700 1.00 46.43 ?  663 THR A O     1 
ATOM   5335  C  CB    . THR A 1 663 ? 150.156 117.054 106.214 1.00 43.39 ?  663 THR A CB    1 
ATOM   5336  O  OG1   . THR A 1 663 ? 151.335 117.852 106.052 1.00 42.25 ?  663 THR A OG1   1 
ATOM   5337  C  CG2   . THR A 1 663 ? 150.203 115.894 105.230 1.00 44.97 ?  663 THR A CG2   1 
ATOM   5338  N  N     . THR A 1 664 ? 149.521 119.495 107.703 1.00 39.16 ?  664 THR A N     1 
ATOM   5339  C  CA    . THR A 1 664 ? 149.780 120.821 108.247 1.00 38.73 ?  664 THR A CA    1 
ATOM   5340  C  C     . THR A 1 664 ? 151.009 121.469 107.628 1.00 37.04 ?  664 THR A C     1 
ATOM   5341  O  O     . THR A 1 664 ? 151.113 122.699 107.635 1.00 40.13 ?  664 THR A O     1 
ATOM   5342  C  CB    . THR A 1 664 ? 149.943 120.761 109.767 1.00 39.50 ?  664 THR A CB    1 
ATOM   5343  O  OG1   . THR A 1 664 ? 151.210 120.179 110.095 1.00 39.06 ?  664 THR A OG1   1 
ATOM   5344  C  CG2   . THR A 1 664 ? 148.825 119.942 110.393 1.00 36.70 ?  664 THR A CG2   1 
ATOM   5345  N  N     . ARG A 1 665 ? 151.943 120.675 107.098 1.00 37.74 ?  665 ARG A N     1 
ATOM   5346  C  CA    . ARG A 1 665 ? 153.077 121.253 106.385 1.00 34.74 ?  665 ARG A CA    1 
ATOM   5347  C  C     . ARG A 1 665 ? 152.615 122.001 105.143 1.00 39.12 ?  665 ARG A C     1 
ATOM   5348  O  O     . ARG A 1 665 ? 153.119 123.088 104.842 1.00 44.89 ?  665 ARG A O     1 
ATOM   5349  C  CB    . ARG A 1 665 ? 154.081 120.165 106.010 1.00 37.03 ?  665 ARG A CB    1 
ATOM   5350  C  CG    . ARG A 1 665 ? 155.061 120.578 104.924 1.00 35.80 ?  665 ARG A CG    1 
ATOM   5351  C  CD    . ARG A 1 665 ? 156.477 120.149 105.257 1.00 37.90 ?  665 ARG A CD    1 
ATOM   5352  N  NE    . ARG A 1 665 ? 157.404 120.443 104.172 1.00 40.76 ?  665 ARG A NE    1 
ATOM   5353  C  CZ    . ARG A 1 665 ? 157.703 119.602 103.191 1.00 42.19 ?  665 ARG A CZ    1 
ATOM   5354  N  NH1   . ARG A 1 665 ? 157.161 118.397 103.126 1.00 41.36 1  665 ARG A NH1   1 
ATOM   5355  N  NH2   . ARG A 1 665 ? 158.566 119.980 102.253 1.00 41.42 ?  665 ARG A NH2   1 
ATOM   5356  N  N     . ASP A 1 666 ? 151.652 121.438 104.411 1.00 37.63 ?  666 ASP A N     1 
ATOM   5357  C  CA    . ASP A 1 666 ? 151.121 122.122 103.237 1.00 36.14 ?  666 ASP A CA    1 
ATOM   5358  C  C     . ASP A 1 666 ? 150.392 123.404 103.625 1.00 39.97 ?  666 ASP A C     1 
ATOM   5359  O  O     . ASP A 1 666 ? 150.521 124.427 102.943 1.00 44.17 ?  666 ASP A O     1 
ATOM   5360  C  CB    . ASP A 1 666 ? 150.196 121.185 102.462 1.00 42.08 ?  666 ASP A CB    1 
ATOM   5361  C  CG    . ASP A 1 666 ? 150.920 119.966 101.930 1.00 46.23 ?  666 ASP A CG    1 
ATOM   5362  O  OD1   . ASP A 1 666 ? 151.962 120.138 101.266 1.00 44.32 ?  666 ASP A OD1   1 
ATOM   5363  O  OD2   . ASP A 1 666 ? 150.448 118.836 102.178 1.00 46.85 -1 666 ASP A OD2   1 
ATOM   5364  N  N     . LEU A 1 667 ? 149.622 123.366 104.714 1.00 33.15 ?  667 LEU A N     1 
ATOM   5365  C  CA    . LEU A 1 667 ? 148.946 124.570 105.186 1.00 30.35 ?  667 LEU A CA    1 
ATOM   5366  C  C     . LEU A 1 667 ? 149.953 125.644 105.576 1.00 30.18 ?  667 LEU A C     1 
ATOM   5367  O  O     . LEU A 1 667 ? 149.785 126.822 105.234 1.00 33.76 ?  667 LEU A O     1 
ATOM   5368  C  CB    . LEU A 1 667 ? 148.044 124.229 106.372 1.00 33.25 ?  667 LEU A CB    1 
ATOM   5369  C  CG    . LEU A 1 667 ? 146.707 124.959 106.505 1.00 35.96 ?  667 LEU A CG    1 
ATOM   5370  C  CD1   . LEU A 1 667 ? 145.842 124.264 107.539 1.00 35.10 ?  667 LEU A CD1   1 
ATOM   5371  C  CD2   . LEU A 1 667 ? 146.900 126.421 106.868 1.00 33.24 ?  667 LEU A CD2   1 
ATOM   5372  N  N     . ASN A 1 668 ? 151.009 125.255 106.293 1.00 30.42 ?  668 ASN A N     1 
ATOM   5373  C  CA    . ASN A 1 668 ? 152.042 126.210 106.672 1.00 27.03 ?  668 ASN A CA    1 
ATOM   5374  C  C     . ASN A 1 668 ? 152.760 126.758 105.448 1.00 27.13 ?  668 ASN A C     1 
ATOM   5375  O  O     . ASN A 1 668 ? 153.120 127.937 105.411 1.00 33.76 ?  668 ASN A O     1 
ATOM   5376  C  CB    . ASN A 1 668 ? 153.038 125.555 107.628 1.00 28.88 ?  668 ASN A CB    1 
ATOM   5377  C  CG    . ASN A 1 668 ? 152.605 125.648 109.075 1.00 31.15 ?  668 ASN A CG    1 
ATOM   5378  O  OD1   . ASN A 1 668 ? 152.876 124.751 109.872 1.00 39.82 ?  668 ASN A OD1   1 
ATOM   5379  N  ND2   . ASN A 1 668 ? 151.928 126.734 109.422 1.00 28.99 ?  668 ASN A ND2   1 
ATOM   5380  N  N     . ARG A 1 669 ? 152.987 125.915 104.439 1.00 29.15 ?  669 ARG A N     1 
ATOM   5381  C  CA    . ARG A 1 669 ? 153.614 126.383 103.208 1.00 30.94 ?  669 ARG A CA    1 
ATOM   5382  C  C     . ARG A 1 669 ? 152.736 127.397 102.492 1.00 28.85 ?  669 ARG A C     1 
ATOM   5383  O  O     . ARG A 1 669 ? 153.237 128.399 101.971 1.00 28.98 ?  669 ARG A O     1 
ATOM   5384  C  CB    . ARG A 1 669 ? 153.924 125.202 102.291 1.00 31.95 ?  669 ARG A CB    1 
ATOM   5385  C  CG    . ARG A 1 669 ? 155.398 124.863 102.196 1.00 29.86 ?  669 ARG A CG    1 
ATOM   5386  C  CD    . ARG A 1 669 ? 155.644 123.749 101.191 1.00 35.06 ?  669 ARG A CD    1 
ATOM   5387  N  NE    . ARG A 1 669 ? 155.750 124.249 99.826  1.00 33.74 ?  669 ARG A NE    1 
ATOM   5388  C  CZ    . ARG A 1 669 ? 156.783 124.931 99.348  1.00 34.89 ?  669 ARG A CZ    1 
ATOM   5389  N  NH1   . ARG A 1 669 ? 157.834 125.211 100.100 1.00 33.74 1  669 ARG A NH1   1 
ATOM   5390  N  NH2   . ARG A 1 669 ? 156.761 125.340 98.083  1.00 37.58 ?  669 ARG A NH2   1 
ATOM   5391  N  N     . ILE A 1 670 ? 151.424 127.152 102.449 1.00 25.18 ?  670 ILE A N     1 
ATOM   5392  C  CA    . ILE A 1 670 ? 150.514 128.122 101.845 1.00 25.57 ?  670 ILE A CA    1 
ATOM   5393  C  C     . ILE A 1 670 ? 150.536 129.431 102.625 1.00 27.89 ?  670 ILE A C     1 
ATOM   5394  O  O     . ILE A 1 670 ? 150.558 130.518 102.037 1.00 32.77 ?  670 ILE A O     1 
ATOM   5395  C  CB    . ILE A 1 670 ? 149.089 127.545 101.750 1.00 28.03 ?  670 ILE A CB    1 
ATOM   5396  C  CG1   . ILE A 1 670 ? 149.075 126.281 100.891 1.00 30.18 ?  670 ILE A CG1   1 
ATOM   5397  C  CG2   . ILE A 1 670 ? 148.138 128.576 101.171 1.00 25.40 ?  670 ILE A CG2   1 
ATOM   5398  C  CD1   . ILE A 1 670 ? 147.894 125.377 101.161 1.00 26.89 ?  670 ILE A CD1   1 
ATOM   5399  N  N     . ASP A 1 671 ? 150.534 129.348 103.957 1.00 24.47 ?  671 ASP A N     1 
ATOM   5400  C  CA    . ASP A 1 671 ? 150.581 130.560 104.773 1.00 21.06 ?  671 ASP A CA    1 
ATOM   5401  C  C     . ASP A 1 671 ? 151.875 131.335 104.548 1.00 25.88 ?  671 ASP A C     1 
ATOM   5402  O  O     . ASP A 1 671 ? 151.861 132.567 104.443 1.00 27.34 ?  671 ASP A O     1 
ATOM   5403  C  CB    . ASP A 1 671 ? 150.425 130.203 106.252 1.00 22.89 ?  671 ASP A CB    1 
ATOM   5404  C  CG    . ASP A 1 671 ? 149.097 129.539 106.554 1.00 34.47 ?  671 ASP A CG    1 
ATOM   5405  O  OD1   . ASP A 1 671 ? 148.153 129.704 105.754 1.00 34.26 ?  671 ASP A OD1   1 
ATOM   5406  O  OD2   . ASP A 1 671 ? 148.999 128.850 107.592 1.00 35.03 -1 671 ASP A OD2   1 
ATOM   5407  N  N     . LEU A 1 672 ? 153.004 130.630 104.469 1.00 23.57 ?  672 LEU A N     1 
ATOM   5408  C  CA    . LEU A 1 672 ? 154.287 131.297 104.275 1.00 19.62 ?  672 LEU A CA    1 
ATOM   5409  C  C     . LEU A 1 672 ? 154.421 131.868 102.871 1.00 18.97 ?  672 LEU A C     1 
ATOM   5410  O  O     . LEU A 1 672 ? 155.063 132.907 102.690 1.00 24.16 ?  672 LEU A O     1 
ATOM   5411  C  CB    . LEU A 1 672 ? 155.430 130.327 104.568 1.00 27.26 ?  672 LEU A CB    1 
ATOM   5412  C  CG    . LEU A 1 672 ? 155.546 129.856 106.018 1.00 23.67 ?  672 LEU A CG    1 
ATOM   5413  C  CD1   . LEU A 1 672 ? 156.463 128.650 106.113 1.00 21.82 ?  672 LEU A CD1   1 
ATOM   5414  C  CD2   . LEU A 1 672 ? 156.033 130.984 106.911 1.00 20.76 ?  672 LEU A CD2   1 
ATOM   5415  N  N     . TYR A 1 673 ? 153.835 131.210 101.870 1.00 21.31 ?  673 TYR A N     1 
ATOM   5416  C  CA    . TYR A 1 673 ? 153.834 131.769 100.524 1.00 18.01 ?  673 TYR A CA    1 
ATOM   5417  C  C     . TYR A 1 673 ? 152.921 132.985 100.440 1.00 21.32 ?  673 TYR A C     1 
ATOM   5418  O  O     . TYR A 1 673 ? 153.212 133.938 99.709  1.00 23.54 ?  673 TYR A O     1 
ATOM   5419  C  CB    . TYR A 1 673 ? 153.411 130.704 99.513  1.00 16.74 ?  673 TYR A CB    1 
ATOM   5420  C  CG    . TYR A 1 673 ? 153.477 131.167 98.078  1.00 22.24 ?  673 TYR A CG    1 
ATOM   5421  C  CD1   . TYR A 1 673 ? 154.692 131.483 97.489  1.00 23.24 ?  673 TYR A CD1   1 
ATOM   5422  C  CD2   . TYR A 1 673 ? 152.326 131.288 97.313  1.00 20.22 ?  673 TYR A CD2   1 
ATOM   5423  C  CE1   . TYR A 1 673 ? 154.760 131.907 96.178  1.00 18.97 ?  673 TYR A CE1   1 
ATOM   5424  C  CE2   . TYR A 1 673 ? 152.383 131.712 96.002  1.00 22.76 ?  673 TYR A CE2   1 
ATOM   5425  C  CZ    . TYR A 1 673 ? 153.602 132.018 95.440  1.00 21.41 ?  673 TYR A CZ    1 
ATOM   5426  O  OH    . TYR A 1 673 ? 153.666 132.442 94.133  1.00 26.15 ?  673 TYR A OH    1 
ATOM   5427  N  N     . ALA A 1 674 ? 151.808 132.964 101.176 1.00 21.02 ?  674 ALA A N     1 
ATOM   5428  C  CA    . ALA A 1 674 ? 150.955 134.142 101.270 1.00 16.37 ?  674 ALA A CA    1 
ATOM   5429  C  C     . ALA A 1 674 ? 151.699 135.301 101.918 1.00 16.90 ?  674 ALA A C     1 
ATOM   5430  O  O     . ALA A 1 674 ? 151.621 136.442 101.450 1.00 25.79 ?  674 ALA A O     1 
ATOM   5431  C  CB    . ALA A 1 674 ? 149.689 133.802 102.054 1.00 18.01 ?  674 ALA A CB    1 
ATOM   5432  N  N     . HIS A 1 675 ? 152.435 135.022 102.995 1.00 15.15 ?  675 HIS A N     1 
ATOM   5433  C  CA    . HIS A 1 675 ? 153.253 136.054 103.622 1.00 15.76 ?  675 HIS A CA    1 
ATOM   5434  C  C     . HIS A 1 675 ? 154.319 136.570 102.661 1.00 20.74 ?  675 HIS A C     1 
ATOM   5435  O  O     . HIS A 1 675 ? 154.588 137.775 102.608 1.00 27.09 ?  675 HIS A O     1 
ATOM   5436  C  CB    . HIS A 1 675 ? 153.894 135.507 104.897 1.00 12.33 ?  675 HIS A CB    1 
ATOM   5437  C  CG    . HIS A 1 675 ? 154.842 136.459 105.551 1.00 21.52 ?  675 HIS A CG    1 
ATOM   5438  N  ND1   . HIS A 1 675 ? 156.210 136.365 105.408 1.00 24.93 ?  675 HIS A ND1   1 
ATOM   5439  C  CD2   . HIS A 1 675 ? 154.621 137.530 106.350 1.00 19.57 ?  675 HIS A CD2   1 
ATOM   5440  C  CE1   . HIS A 1 675 ? 156.790 137.334 106.090 1.00 25.63 ?  675 HIS A CE1   1 
ATOM   5441  N  NE2   . HIS A 1 675 ? 155.849 138.055 106.671 1.00 22.92 ?  675 HIS A NE2   1 
ATOM   5442  N  N     . HIS A 1 676 ? 154.937 135.669 101.898 1.00 19.67 ?  676 HIS A N     1 
ATOM   5443  C  CA    . HIS A 1 676 ? 155.964 136.067 100.941 1.00 20.42 ?  676 HIS A CA    1 
ATOM   5444  C  C     . HIS A 1 676 ? 155.378 136.893 99.802  1.00 24.31 ?  676 HIS A C     1 
ATOM   5445  O  O     . HIS A 1 676 ? 156.003 137.855 99.340  1.00 25.05 ?  676 HIS A O     1 
ATOM   5446  C  CB    . HIS A 1 676 ? 156.671 134.828 100.395 1.00 23.92 ?  676 HIS A CB    1 
ATOM   5447  C  CG    . HIS A 1 676 ? 157.550 135.102 99.215  1.00 25.00 ?  676 HIS A CG    1 
ATOM   5448  N  ND1   . HIS A 1 676 ? 158.727 135.811 99.311  1.00 20.88 ?  676 HIS A ND1   1 
ATOM   5449  C  CD2   . HIS A 1 676 ? 157.423 134.760 97.911  1.00 19.79 ?  676 HIS A CD2   1 
ATOM   5450  C  CE1   . HIS A 1 676 ? 159.286 135.895 98.118  1.00 25.77 ?  676 HIS A CE1   1 
ATOM   5451  N  NE2   . HIS A 1 676 ? 158.515 135.266 97.251  1.00 28.82 ?  676 HIS A NE2   1 
ATOM   5452  N  N     . ARG A 1 677 ? 154.182 136.537 99.339  1.00 21.42 ?  677 ARG A N     1 
ATOM   5453  C  CA    . ARG A 1 677 ? 153.571 137.203 98.195  1.00 20.36 ?  677 ARG A CA    1 
ATOM   5454  C  C     . ARG A 1 677 ? 152.862 138.496 98.566  1.00 24.10 ?  677 ARG A C     1 
ATOM   5455  O  O     . ARG A 1 677 ? 152.313 139.157 97.677  1.00 25.29 ?  677 ARG A O     1 
ATOM   5456  C  CB    . ARG A 1 677 ? 152.587 136.257 97.502  1.00 18.85 ?  677 ARG A CB    1 
ATOM   5457  C  CG    . ARG A 1 677 ? 153.236 135.322 96.498  1.00 20.21 ?  677 ARG A CG    1 
ATOM   5458  C  CD    . ARG A 1 677 ? 153.759 136.082 95.292  1.00 20.22 ?  677 ARG A CD    1 
ATOM   5459  N  NE    . ARG A 1 677 ? 152.739 136.245 94.264  1.00 25.02 ?  677 ARG A NE    1 
ATOM   5460  C  CZ    . ARG A 1 677 ? 152.216 137.409 93.904  1.00 27.26 ?  677 ARG A CZ    1 
ATOM   5461  N  NH1   . ARG A 1 677 ? 152.597 138.542 94.472  1.00 21.21 1  677 ARG A NH1   1 
ATOM   5462  N  NH2   . ARG A 1 677 ? 151.289 137.437 92.952  1.00 22.30 ?  677 ARG A NH2   1 
ATOM   5463  N  N     . GLY A 1 678 ? 152.858 138.874 99.840  1.00 20.70 ?  678 GLY A N     1 
ATOM   5464  C  CA    . GLY A 1 678 ? 152.224 140.106 100.259 1.00 16.08 ?  678 GLY A CA    1 
ATOM   5465  C  C     . GLY A 1 678 ? 150.777 139.981 100.663 1.00 16.22 ?  678 GLY A C     1 
ATOM   5466  O  O     . GLY A 1 678 ? 150.081 141.000 100.737 1.00 23.71 ?  678 GLY A O     1 
ATOM   5467  N  N     . ILE A 1 679 ? 150.292 138.765 100.918 1.00 15.50 ?  679 ILE A N     1 
ATOM   5468  C  CA    . ILE A 1 679 ? 148.926 138.589 101.392 1.00 11.34 ?  679 ILE A CA    1 
ATOM   5469  C  C     . ILE A 1 679 ? 148.800 139.207 102.776 1.00 15.26 ?  679 ILE A C     1 
ATOM   5470  O  O     . ILE A 1 679 ? 149.630 138.964 103.662 1.00 23.09 ?  679 ILE A O     1 
ATOM   5471  C  CB    . ILE A 1 679 ? 148.545 137.103 101.409 1.00 15.65 ?  679 ILE A CB    1 
ATOM   5472  C  CG1   . ILE A 1 679 ? 148.490 136.547 99.986  1.00 15.46 ?  679 ILE A CG1   1 
ATOM   5473  C  CG2   . ILE A 1 679 ? 147.220 136.893 102.120 1.00 15.73 ?  679 ILE A CG2   1 
ATOM   5474  C  CD1   . ILE A 1 679 ? 147.575 137.306 99.085  1.00 13.41 ?  679 ILE A CD1   1 
ATOM   5475  N  N     . LYS A 1 680 ? 147.766 140.021 102.966 1.00 13.20 ?  680 LYS A N     1 
ATOM   5476  C  CA    . LYS A 1 680 ? 147.579 140.723 104.227 1.00 8.26  ?  680 LYS A CA    1 
ATOM   5477  C  C     . LYS A 1 680 ? 146.882 139.854 105.270 1.00 8.16  ?  680 LYS A C     1 
ATOM   5478  O  O     . LYS A 1 680 ? 147.310 139.806 106.426 1.00 16.91 ?  680 LYS A O     1 
ATOM   5479  C  CB    . LYS A 1 680 ? 146.787 142.010 103.994 1.00 8.86  ?  680 LYS A CB    1 
ATOM   5480  C  CG    . LYS A 1 680 ? 147.546 143.081 103.231 1.00 0.00  ?  680 LYS A CG    1 
ATOM   5481  C  CD    . LYS A 1 680 ? 146.702 144.330 103.065 1.00 6.45  ?  680 LYS A CD    1 
ATOM   5482  C  CE    . LYS A 1 680 ? 147.285 145.264 102.026 1.00 13.22 ?  680 LYS A CE    1 
ATOM   5483  N  NZ    . LYS A 1 680 ? 146.504 146.524 101.913 1.00 10.77 1  680 LYS A NZ    1 
ATOM   5484  N  N     . THR A 1 681 ? 145.813 139.166 104.881 1.00 15.71 ?  681 THR A N     1 
ATOM   5485  C  CA    . THR A 1 681 ? 145.040 138.343 105.797 1.00 8.89  ?  681 THR A CA    1 
ATOM   5486  C  C     . THR A 1 681 ? 144.704 137.009 105.148 1.00 15.33 ?  681 THR A C     1 
ATOM   5487  O  O     . THR A 1 681 ? 144.541 136.916 103.929 1.00 22.36 ?  681 THR A O     1 
ATOM   5488  C  CB    . THR A 1 681 ? 143.734 139.033 106.224 1.00 16.05 ?  681 THR A CB    1 
ATOM   5489  O  OG1   . THR A 1 681 ? 143.040 139.510 105.066 1.00 30.21 ?  681 THR A OG1   1 
ATOM   5490  C  CG2   . THR A 1 681 ? 144.013 140.197 107.151 1.00 3.10  ?  681 THR A CG2   1 
ATOM   5491  N  N     . ILE A 1 682 ? 144.599 135.977 105.980 1.00 15.27 ?  682 ILE A N     1 
ATOM   5492  C  CA    . ILE A 1 682 ? 144.085 134.676 105.576 1.00 9.32  ?  682 ILE A CA    1 
ATOM   5493  C  C     . ILE A 1 682 ? 142.858 134.380 106.425 1.00 13.63 ?  682 ILE A C     1 
ATOM   5494  O  O     . ILE A 1 682 ? 142.936 134.393 107.659 1.00 21.07 ?  682 ILE A O     1 
ATOM   5495  C  CB    . ILE A 1 682 ? 145.141 133.568 105.727 1.00 12.93 ?  682 ILE A CB    1 
ATOM   5496  C  CG1   . ILE A 1 682 ? 146.525 134.086 105.339 1.00 17.99 ?  682 ILE A CG1   1 
ATOM   5497  C  CG2   . ILE A 1 682 ? 144.778 132.389 104.860 1.00 20.80 ?  682 ILE A CG2   1 
ATOM   5498  C  CD1   . ILE A 1 682 ? 147.588 133.012 105.310 1.00 19.45 ?  682 ILE A CD1   1 
ATOM   5499  N  N     . TYR A 1 683 ? 141.727 134.126 105.767 1.00 18.77 ?  683 TYR A N     1 
ATOM   5500  C  CA    . TYR A 1 683 ? 140.457 134.041 106.488 1.00 12.07 ?  683 TYR A CA    1 
ATOM   5501  C  C     . TYR A 1 683 ? 140.228 132.654 107.084 1.00 19.43 ?  683 TYR A C     1 
ATOM   5502  O  O     . TYR A 1 683 ? 140.192 132.489 108.305 1.00 32.31 ?  683 TYR A O     1 
ATOM   5503  C  CB    . TYR A 1 683 ? 139.306 134.431 105.553 1.00 18.00 ?  683 TYR A CB    1 
ATOM   5504  C  CG    . TYR A 1 683 ? 137.960 134.552 106.231 1.00 16.18 ?  683 TYR A CG    1 
ATOM   5505  C  CD1   . TYR A 1 683 ? 137.865 134.783 107.598 1.00 12.18 ?  683 TYR A CD1   1 
ATOM   5506  C  CD2   . TYR A 1 683 ? 136.783 134.445 105.503 1.00 9.75  ?  683 TYR A CD2   1 
ATOM   5507  C  CE1   . TYR A 1 683 ? 136.640 134.896 108.218 1.00 15.88 ?  683 TYR A CE1   1 
ATOM   5508  C  CE2   . TYR A 1 683 ? 135.553 134.559 106.117 1.00 18.37 ?  683 TYR A CE2   1 
ATOM   5509  C  CZ    . TYR A 1 683 ? 135.488 134.785 107.474 1.00 19.26 ?  683 TYR A CZ    1 
ATOM   5510  O  OH    . TYR A 1 683 ? 134.264 134.898 108.091 1.00 26.27 ?  683 TYR A OH    1 
ATOM   5511  N  N     . TYR A 1 684 ? 140.093 131.641 106.237 1.00 29.27 ?  684 TYR A N     1 
ATOM   5512  C  CA    . TYR A 1 684 ? 139.649 130.338 106.701 1.00 25.72 ?  684 TYR A CA    1 
ATOM   5513  C  C     . TYR A 1 684 ? 140.430 129.243 105.996 1.00 32.85 ?  684 TYR A C     1 
ATOM   5514  O  O     . TYR A 1 684 ? 140.960 129.440 104.900 1.00 36.53 ?  684 TYR A O     1 
ATOM   5515  C  CB    . TYR A 1 684 ? 138.147 130.138 106.460 1.00 23.92 ?  684 TYR A CB    1 
ATOM   5516  C  CG    . TYR A 1 684 ? 137.287 130.409 107.672 1.00 22.24 ?  684 TYR A CG    1 
ATOM   5517  C  CD1   . TYR A 1 684 ? 137.506 129.739 108.868 1.00 26.54 ?  684 TYR A CD1   1 
ATOM   5518  C  CD2   . TYR A 1 684 ? 136.255 131.336 107.620 1.00 29.36 ?  684 TYR A CD2   1 
ATOM   5519  C  CE1   . TYR A 1 684 ? 136.719 129.983 109.978 1.00 30.37 ?  684 TYR A CE1   1 
ATOM   5520  C  CE2   . TYR A 1 684 ? 135.464 131.589 108.725 1.00 26.07 ?  684 TYR A CE2   1 
ATOM   5521  C  CZ    . TYR A 1 684 ? 135.701 130.910 109.900 1.00 29.63 ?  684 TYR A CZ    1 
ATOM   5522  O  OH    . TYR A 1 684 ? 134.916 131.158 111.001 1.00 32.26 ?  684 TYR A OH    1 
ATOM   5523  N  N     . ALA A 1 685 ? 140.495 128.084 106.644 1.00 31.03 ?  685 ALA A N     1 
ATOM   5524  C  CA    . ALA A 1 685 ? 141.077 126.874 106.075 1.00 32.41 ?  685 ALA A CA    1 
ATOM   5525  C  C     . ALA A 1 685 ? 139.954 125.845 105.998 1.00 36.55 ?  685 ALA A C     1 
ATOM   5526  O  O     . ALA A 1 685 ? 139.768 125.041 106.914 1.00 43.59 ?  685 ALA A O     1 
ATOM   5527  C  CB    . ALA A 1 685 ? 142.252 126.377 106.908 1.00 32.11 ?  685 ALA A CB    1 
ATOM   5528  N  N     . ARG A 1 686 ? 139.201 125.881 104.902 1.00 32.51 ?  686 ARG A N     1 
ATOM   5529  C  CA    . ARG A 1 686 ? 138.094 124.959 104.695 1.00 33.05 ?  686 ARG A CA    1 
ATOM   5530  C  C     . ARG A 1 686 ? 138.624 123.672 104.078 1.00 38.70 ?  686 ARG A C     1 
ATOM   5531  O  O     . ARG A 1 686 ? 139.160 123.688 102.965 1.00 40.64 ?  686 ARG A O     1 
ATOM   5532  C  CB    . ARG A 1 686 ? 137.039 125.595 103.793 1.00 38.13 ?  686 ARG A CB    1 
ATOM   5533  C  CG    . ARG A 1 686 ? 136.295 126.755 104.427 1.00 38.73 ?  686 ARG A CG    1 
ATOM   5534  C  CD    . ARG A 1 686 ? 135.015 127.065 103.671 1.00 39.90 ?  686 ARG A CD    1 
ATOM   5535  N  NE    . ARG A 1 686 ? 134.158 125.893 103.536 1.00 42.70 ?  686 ARG A NE    1 
ATOM   5536  C  CZ    . ARG A 1 686 ? 132.840 125.912 103.671 1.00 42.66 ?  686 ARG A CZ    1 
ATOM   5537  N  NH1   . ARG A 1 686 ? 132.189 127.032 103.942 1.00 41.77 1  686 ARG A NH1   1 
ATOM   5538  N  NH2   . ARG A 1 686 ? 132.156 124.780 103.529 1.00 42.47 ?  686 ARG A NH2   1 
ATOM   5539  N  N     . THR A 1 687 ? 138.478 122.565 104.798 1.00 48.40 ?  687 THR A N     1 
ATOM   5540  C  CA    . THR A 1 687 ? 138.930 121.263 104.332 1.00 46.64 ?  687 THR A CA    1 
ATOM   5541  C  C     . THR A 1 687 ? 137.762 120.504 103.716 1.00 47.93 ?  687 THR A C     1 
ATOM   5542  O  O     . THR A 1 687 ? 136.684 120.414 104.309 1.00 50.75 ?  687 THR A O     1 
ATOM   5543  C  CB    . THR A 1 687 ? 139.540 120.453 105.478 1.00 46.66 ?  687 THR A CB    1 
ATOM   5544  O  OG1   . THR A 1 687 ? 140.829 120.986 105.812 1.00 48.39 ?  687 THR A OG1   1 
ATOM   5545  C  CG2   . THR A 1 687 ? 139.693 118.990 105.085 1.00 47.30 ?  687 THR A CG2   1 
ATOM   5546  N  N     . LYS A 1 688 ? 137.985 119.963 102.524 1.00 48.04 ?  688 LYS A N     1 
ATOM   5547  C  CA    . LYS A 1 688 ? 136.950 119.219 101.818 1.00 48.98 ?  688 LYS A CA    1 
ATOM   5548  C  C     . LYS A 1 688 ? 136.844 117.795 102.352 1.00 53.36 ?  688 LYS A C     1 
ATOM   5549  O  O     . LYS A 1 688 ? 137.831 117.216 102.804 1.00 55.18 ?  688 LYS A O     1 
ATOM   5550  C  CB    . LYS A 1 688 ? 137.234 119.197 100.314 1.00 49.54 ?  688 LYS A CB    1 
ATOM   5551  C  CG    . LYS A 1 688 ? 136.116 118.594 99.483  1.00 48.07 ?  688 LYS A CG    1 
ATOM   5552  C  CD    . LYS A 1 688 ? 136.432 118.662 97.999  1.00 47.51 ?  688 LYS A CD    1 
ATOM   5553  C  CE    . LYS A 1 688 ? 135.286 118.111 97.168  1.00 51.68 ?  688 LYS A CE    1 
ATOM   5554  N  NZ    . LYS A 1 688 ? 135.569 118.195 95.709  1.00 52.23 ?  688 LYS A NZ    1 
ATOM   5555  N  N     . VAL B 1 6   ? 155.585 117.502 162.481 1.00 57.44 ?  6   VAL B N     1 
ATOM   5556  C  CA    . VAL B 1 6   ? 154.457 118.323 162.903 1.00 58.35 ?  6   VAL B CA    1 
ATOM   5557  C  C     . VAL B 1 6   ? 154.889 119.313 163.980 1.00 60.21 ?  6   VAL B C     1 
ATOM   5558  O  O     . VAL B 1 6   ? 155.727 118.994 164.823 1.00 58.78 ?  6   VAL B O     1 
ATOM   5559  C  CB    . VAL B 1 6   ? 153.290 117.449 163.400 1.00 58.16 ?  6   VAL B CB    1 
ATOM   5560  C  CG1   . VAL B 1 6   ? 152.626 116.741 162.231 1.00 58.66 ?  6   VAL B CG1   1 
ATOM   5561  C  CG2   . VAL B 1 6   ? 153.780 116.441 164.425 1.00 58.25 ?  6   VAL B CG2   1 
ATOM   5562  N  N     . PRO B 1 7   ? 154.324 120.517 163.941 1.00 57.76 ?  7   PRO B N     1 
ATOM   5563  C  CA    . PRO B 1 7   ? 154.685 121.537 164.931 1.00 53.33 ?  7   PRO B CA    1 
ATOM   5564  C  C     . PRO B 1 7   ? 154.229 121.153 166.331 1.00 52.92 ?  7   PRO B C     1 
ATOM   5565  O  O     . PRO B 1 7   ? 153.284 120.385 166.524 1.00 55.02 ?  7   PRO B O     1 
ATOM   5566  C  CB    . PRO B 1 7   ? 153.956 122.792 164.439 1.00 52.57 ?  7   PRO B CB    1 
ATOM   5567  C  CG    . PRO B 1 7   ? 153.608 122.520 163.014 1.00 52.52 ?  7   PRO B CG    1 
ATOM   5568  C  CD    . PRO B 1 7   ? 153.428 121.043 162.899 1.00 54.44 ?  7   PRO B CD    1 
ATOM   5569  N  N     . LYS B 1 8   ? 154.935 121.707 167.321 1.00 50.58 ?  8   LYS B N     1 
ATOM   5570  C  CA    . LYS B 1 8   ? 154.625 121.406 168.715 1.00 49.37 ?  8   LYS B CA    1 
ATOM   5571  C  C     . LYS B 1 8   ? 153.227 121.881 169.090 1.00 52.20 ?  8   LYS B C     1 
ATOM   5572  O  O     . LYS B 1 8   ? 152.481 121.165 169.770 1.00 54.02 ?  8   LYS B O     1 
ATOM   5573  C  CB    . LYS B 1 8   ? 155.672 122.038 169.631 1.00 51.24 ?  8   LYS B CB    1 
ATOM   5574  C  CG    . LYS B 1 8   ? 155.244 122.139 171.085 1.00 52.38 ?  8   LYS B CG    1 
ATOM   5575  C  CD    . LYS B 1 8   ? 156.443 122.164 172.016 1.00 51.18 ?  8   LYS B CD    1 
ATOM   5576  C  CE    . LYS B 1 8   ? 156.013 122.055 173.469 1.00 51.50 ?  8   LYS B CE    1 
ATOM   5577  N  NZ    . LYS B 1 8   ? 155.930 123.388 174.126 1.00 52.01 1  8   LYS B NZ    1 
ATOM   5578  N  N     . TRP B 1 9   ? 152.853 123.089 168.659 1.00 53.51 ?  9   TRP B N     1 
ATOM   5579  C  CA    . TRP B 1 9   ? 151.516 123.587 168.962 1.00 51.21 ?  9   TRP B CA    1 
ATOM   5580  C  C     . TRP B 1 9   ? 150.444 122.749 168.281 1.00 49.73 ?  9   TRP B C     1 
ATOM   5581  O  O     . TRP B 1 9   ? 149.350 122.584 168.829 1.00 51.44 ?  9   TRP B O     1 
ATOM   5582  C  CB    . TRP B 1 9   ? 151.380 125.055 168.555 1.00 51.68 ?  9   TRP B CB    1 
ATOM   5583  C  CG    . TRP B 1 9   ? 151.707 125.339 167.122 1.00 49.36 ?  9   TRP B CG    1 
ATOM   5584  C  CD1   . TRP B 1 9   ? 150.844 125.318 166.068 1.00 48.25 ?  9   TRP B CD1   1 
ATOM   5585  C  CD2   . TRP B 1 9   ? 152.983 125.711 166.589 1.00 49.96 ?  9   TRP B CD2   1 
ATOM   5586  N  NE1   . TRP B 1 9   ? 151.503 125.644 164.909 1.00 47.82 ?  9   TRP B NE1   1 
ATOM   5587  C  CE2   . TRP B 1 9   ? 152.817 125.892 165.202 1.00 49.58 ?  9   TRP B CE2   1 
ATOM   5588  C  CE3   . TRP B 1 9   ? 154.249 125.905 167.148 1.00 47.79 ?  9   TRP B CE3   1 
ATOM   5589  C  CZ2   . TRP B 1 9   ? 153.871 126.254 164.366 1.00 48.99 ?  9   TRP B CZ2   1 
ATOM   5590  C  CZ3   . TRP B 1 9   ? 155.292 126.265 166.317 1.00 49.28 ?  9   TRP B CZ3   1 
ATOM   5591  C  CH2   . TRP B 1 9   ? 155.097 126.434 164.942 1.00 50.26 ?  9   TRP B CH2   1 
ATOM   5592  N  N     . ILE B 1 10  ? 150.739 122.207 167.098 1.00 52.27 ?  10  ILE B N     1 
ATOM   5593  C  CA    . ILE B 1 10  ? 149.789 121.326 166.428 1.00 52.32 ?  10  ILE B CA    1 
ATOM   5594  C  C     . ILE B 1 10  ? 149.561 120.063 167.251 1.00 53.45 ?  10  ILE B C     1 
ATOM   5595  O  O     . ILE B 1 10  ? 148.421 119.611 167.416 1.00 55.24 ?  10  ILE B O     1 
ATOM   5596  C  CB    . ILE B 1 10  ? 150.284 121.000 165.008 1.00 52.71 ?  10  ILE B CB    1 
ATOM   5597  C  CG1   . ILE B 1 10  ? 150.117 122.219 164.095 1.00 52.31 ?  10  ILE B CG1   1 
ATOM   5598  C  CG2   . ILE B 1 10  ? 149.553 119.789 164.446 1.00 53.05 ?  10  ILE B CG2   1 
ATOM   5599  C  CD1   . ILE B 1 10  ? 148.805 122.266 163.355 1.00 53.46 ?  10  ILE B CD1   1 
ATOM   5600  N  N     . GLN B 1 11  ? 150.637 119.480 167.785 1.00 53.92 ?  11  GLN B N     1 
ATOM   5601  C  CA    . GLN B 1 11  ? 150.494 118.307 168.644 1.00 55.14 ?  11  GLN B CA    1 
ATOM   5602  C  C     . GLN B 1 11  ? 149.719 118.642 169.911 1.00 54.84 ?  11  GLN B C     1 
ATOM   5603  O  O     . GLN B 1 11  ? 148.865 117.862 170.351 1.00 57.06 ?  11  GLN B O     1 
ATOM   5604  C  CB    . GLN B 1 11  ? 151.870 117.743 168.997 1.00 56.03 ?  11  GLN B CB    1 
ATOM   5605  C  CG    . GLN B 1 11  ? 152.736 117.410 167.797 1.00 56.59 ?  11  GLN B CG    1 
ATOM   5606  C  CD    . GLN B 1 11  ? 154.214 117.415 168.130 1.00 58.95 ?  11  GLN B CD    1 
ATOM   5607  O  OE1   . GLN B 1 11  ? 155.054 117.689 167.275 1.00 58.89 ?  11  GLN B OE1   1 
ATOM   5608  N  NE2   . GLN B 1 11  ? 154.538 117.113 169.382 1.00 55.94 ?  11  GLN B NE2   1 
ATOM   5609  N  N     . LEU B 1 12  ? 150.001 119.799 170.514 1.00 51.73 ?  12  LEU B N     1 
ATOM   5610  C  CA    . LEU B 1 12  ? 149.284 120.186 171.725 1.00 50.64 ?  12  LEU B CA    1 
ATOM   5611  C  C     . LEU B 1 12  ? 147.800 120.397 171.446 1.00 51.29 ?  12  LEU B C     1 
ATOM   5612  O  O     . LEU B 1 12  ? 146.951 120.045 172.273 1.00 53.55 ?  12  LEU B O     1 
ATOM   5613  C  CB    . LEU B 1 12  ? 149.908 121.446 172.322 1.00 52.10 ?  12  LEU B CB    1 
ATOM   5614  C  CG    . LEU B 1 12  ? 151.157 121.211 173.172 1.00 52.39 ?  12  LEU B CG    1 
ATOM   5615  C  CD1   . LEU B 1 12  ? 151.921 122.510 173.382 1.00 52.91 ?  12  LEU B CD1   1 
ATOM   5616  C  CD2   . LEU B 1 12  ? 150.786 120.581 174.503 1.00 51.76 ?  12  LEU B CD2   1 
ATOM   5617  N  N     . ASN B 1 13  ? 147.469 120.974 170.289 1.00 51.33 ?  13  ASN B N     1 
ATOM   5618  C  CA    . ASN B 1 13  ? 146.069 121.165 169.926 1.00 49.42 ?  13  ASN B CA    1 
ATOM   5619  C  C     . ASN B 1 13  ? 145.386 119.836 169.630 1.00 52.08 ?  13  ASN B C     1 
ATOM   5620  O  O     . ASN B 1 13  ? 144.210 119.650 169.960 1.00 56.58 ?  13  ASN B O     1 
ATOM   5621  C  CB    . ASN B 1 13  ? 145.966 122.106 168.725 1.00 51.33 ?  13  ASN B CB    1 
ATOM   5622  C  CG    . ASN B 1 13  ? 144.542 122.281 168.245 1.00 50.05 ?  13  ASN B CG    1 
ATOM   5623  O  OD1   . ASN B 1 13  ? 144.160 121.764 167.197 1.00 50.41 ?  13  ASN B OD1   1 
ATOM   5624  N  ND2   . ASN B 1 13  ? 143.746 123.016 169.012 1.00 51.28 ?  13  ASN B ND2   1 
ATOM   5625  N  N     . ASN B 1 14  ? 146.100 118.900 169.001 1.00 53.76 ?  14  ASN B N     1 
ATOM   5626  C  CA    . ASN B 1 14  ? 145.534 117.578 168.764 1.00 52.32 ?  14  ASN B CA    1 
ATOM   5627  C  C     . ASN B 1 14  ? 145.406 116.772 170.049 1.00 53.34 ?  14  ASN B C     1 
ATOM   5628  O  O     . ASN B 1 14  ? 144.632 115.810 170.090 1.00 56.59 ?  14  ASN B O     1 
ATOM   5629  C  CB    . ASN B 1 14  ? 146.384 116.811 167.750 1.00 52.91 ?  14  ASN B CB    1 
ATOM   5630  C  CG    . ASN B 1 14  ? 146.309 117.409 166.363 1.00 55.92 ?  14  ASN B CG    1 
ATOM   5631  O  OD1   . ASN B 1 14  ? 145.517 118.315 166.109 1.00 58.01 ?  14  ASN B OD1   1 
ATOM   5632  N  ND2   . ASN B 1 14  ? 147.133 116.903 165.454 1.00 54.69 ?  14  ASN B ND2   1 
ATOM   5633  N  N     . GLU B 1 15  ? 146.147 117.145 171.092 1.00 56.23 ?  15  GLU B N     1 
ATOM   5634  C  CA    . GLU B 1 15  ? 146.035 116.475 172.383 1.00 56.56 ?  15  GLU B CA    1 
ATOM   5635  C  C     . GLU B 1 15  ? 144.694 116.717 173.066 1.00 57.08 ?  15  GLU B C     1 
ATOM   5636  O  O     . GLU B 1 15  ? 144.406 116.052 174.066 1.00 60.06 ?  15  GLU B O     1 
ATOM   5637  C  CB    . GLU B 1 15  ? 147.170 116.922 173.306 1.00 55.53 ?  15  GLU B CB    1 
ATOM   5638  C  CG    . GLU B 1 15  ? 148.354 115.970 173.334 1.00 57.49 ?  15  GLU B CG    1 
ATOM   5639  C  CD    . GLU B 1 15  ? 149.640 116.646 173.765 1.00 61.35 ?  15  GLU B CD    1 
ATOM   5640  O  OE1   . GLU B 1 15  ? 149.762 116.986 174.960 1.00 60.81 ?  15  GLU B OE1   1 
ATOM   5641  O  OE2   . GLU B 1 15  ? 150.530 116.837 172.909 1.00 60.08 -1 15  GLU B OE2   1 
ATOM   5642  N  N     . ILE B 1 16  ? 143.882 117.651 172.566 1.00 56.73 ?  16  ILE B N     1 
ATOM   5643  C  CA    . ILE B 1 16  ? 142.568 117.893 173.159 1.00 56.54 ?  16  ILE B CA    1 
ATOM   5644  C  C     . ILE B 1 16  ? 141.693 116.652 173.038 1.00 56.57 ?  16  ILE B C     1 
ATOM   5645  O  O     . ILE B 1 16  ? 141.042 116.230 174.001 1.00 54.26 ?  16  ILE B O     1 
ATOM   5646  C  CB    . ILE B 1 16  ? 141.894 119.110 172.500 1.00 55.92 ?  16  ILE B CB    1 
ATOM   5647  C  CG1   . ILE B 1 16  ? 142.724 120.374 172.706 1.00 55.42 ?  16  ILE B CG1   1 
ATOM   5648  C  CG2   . ILE B 1 16  ? 140.489 119.305 173.050 1.00 56.40 ?  16  ILE B CG2   1 
ATOM   5649  C  CD1   . ILE B 1 16  ? 142.344 121.488 171.763 1.00 54.74 ?  16  ILE B CD1   1 
ATOM   5650  N  N     . MET B 1 17  ? 141.670 116.046 171.850 1.00 56.33 ?  17  MET B N     1 
ATOM   5651  C  CA    . MET B 1 17  ? 140.790 114.912 171.600 1.00 56.69 ?  17  MET B CA    1 
ATOM   5652  C  C     . MET B 1 17  ? 141.269 113.632 172.266 1.00 57.42 ?  17  MET B C     1 
ATOM   5653  O  O     . MET B 1 17  ? 140.467 112.709 172.447 1.00 56.86 ?  17  MET B O     1 
ATOM   5654  C  CB    . MET B 1 17  ? 140.642 114.686 170.096 1.00 57.47 ?  17  MET B CB    1 
ATOM   5655  C  CG    . MET B 1 17  ? 140.242 115.933 169.339 1.00 57.59 ?  17  MET B CG    1 
ATOM   5656  S  SD    . MET B 1 17  ? 138.646 116.581 169.867 1.00 63.33 ?  17  MET B SD    1 
ATOM   5657  C  CE    . MET B 1 17  ? 137.563 115.879 168.627 1.00 55.92 ?  17  MET B CE    1 
ATOM   5658  N  N     . ILE B 1 18  ? 142.546 113.548 172.631 1.00 59.62 ?  18  ILE B N     1 
ATOM   5659  C  CA    . ILE B 1 18  ? 143.032 112.409 173.397 1.00 58.94 ?  18  ILE B CA    1 
ATOM   5660  C  C     . ILE B 1 18  ? 142.459 112.535 174.801 1.00 60.09 ?  18  ILE B C     1 
ATOM   5661  O  O     . ILE B 1 18  ? 142.912 113.363 175.600 1.00 59.84 ?  18  ILE B O     1 
ATOM   5662  C  CB    . ILE B 1 18  ? 144.569 112.339 173.411 1.00 60.01 ?  18  ILE B CB    1 
ATOM   5663  C  CG1   . ILE B 1 18  ? 145.092 111.977 172.019 1.00 60.22 ?  18  ILE B CG1   1 
ATOM   5664  C  CG2   . ILE B 1 18  ? 145.050 111.319 174.430 1.00 59.20 ?  18  ILE B CG2   1 
ATOM   5665  C  CD1   . ILE B 1 18  ? 146.173 112.902 171.511 1.00 60.47 ?  18  ILE B CD1   1 
ATOM   5666  N  N     . GLN B 1 19  ? 141.447 111.727 175.103 1.00 62.58 ?  19  GLN B N     1 
ATOM   5667  C  CA    . GLN B 1 19  ? 140.725 111.871 176.356 1.00 62.09 ?  19  GLN B CA    1 
ATOM   5668  C  C     . GLN B 1 19  ? 141.556 111.359 177.524 1.00 64.61 ?  19  GLN B C     1 
ATOM   5669  O  O     . GLN B 1 19  ? 142.242 110.339 177.424 1.00 66.56 ?  19  GLN B O     1 
ATOM   5670  C  CB    . GLN B 1 19  ? 139.394 111.123 176.289 1.00 64.69 ?  19  GLN B CB    1 
ATOM   5671  C  CG    . GLN B 1 19  ? 138.810 111.029 174.889 1.00 64.60 ?  19  GLN B CG    1 
ATOM   5672  C  CD    . GLN B 1 19  ? 137.305 111.203 174.871 1.00 64.39 ?  19  GLN B CD    1 
ATOM   5673  O  OE1   . GLN B 1 19  ? 136.611 110.812 175.810 1.00 64.88 ?  19  GLN B OE1   1 
ATOM   5674  N  NE2   . GLN B 1 19  ? 136.791 111.793 173.798 1.00 64.21 ?  19  GLN B NE2   1 
ATOM   5675  N  N     . LYS B 1 20  ? 141.490 112.082 178.639 1.00 67.86 ?  20  LYS B N     1 
ATOM   5676  C  CA    . LYS B 1 20  ? 142.125 111.680 179.888 1.00 69.26 ?  20  LYS B CA    1 
ATOM   5677  C  C     . LYS B 1 20  ? 141.032 111.518 180.934 1.00 69.23 ?  20  LYS B C     1 
ATOM   5678  O  O     . LYS B 1 20  ? 140.295 112.469 181.216 1.00 68.81 ?  20  LYS B O     1 
ATOM   5679  C  CB    . LYS B 1 20  ? 143.166 112.708 180.335 1.00 67.79 ?  20  LYS B CB    1 
ATOM   5680  C  CG    . LYS B 1 20  ? 143.451 112.704 181.827 1.00 68.45 ?  20  LYS B CG    1 
ATOM   5681  C  CD    . LYS B 1 20  ? 144.810 113.314 182.128 1.00 69.24 ?  20  LYS B CD    1 
ATOM   5682  C  CE    . LYS B 1 20  ? 144.676 114.754 182.593 1.00 69.19 ?  20  LYS B CE    1 
ATOM   5683  N  NZ    . LYS B 1 20  ? 145.985 115.463 182.594 1.00 68.51 1  20  LYS B NZ    1 
ATOM   5684  N  N     . ASP B 1 21  ? 140.930 110.314 181.499 1.00 71.38 ?  21  ASP B N     1 
ATOM   5685  C  CA    . ASP B 1 21  ? 139.873 109.973 182.454 1.00 71.25 ?  21  ASP B CA    1 
ATOM   5686  C  C     . ASP B 1 21  ? 138.488 110.206 181.853 1.00 72.08 ?  21  ASP B C     1 
ATOM   5687  O  O     . ASP B 1 21  ? 137.560 110.646 182.535 1.00 71.47 ?  21  ASP B O     1 
ATOM   5688  C  CB    . ASP B 1 21  ? 140.038 110.745 183.765 1.00 71.76 ?  21  ASP B CB    1 
ATOM   5689  C  CG    . ASP B 1 21  ? 141.474 110.767 184.251 1.00 73.48 ?  21  ASP B CG    1 
ATOM   5690  O  OD1   . ASP B 1 21  ? 142.150 109.721 184.161 1.00 72.23 ?  21  ASP B OD1   1 
ATOM   5691  O  OD2   . ASP B 1 21  ? 141.927 111.832 184.723 1.00 72.92 -1 21  ASP B OD2   1 
ATOM   5692  N  N     . GLY B 1 22  ? 138.348 109.909 180.563 1.00 68.63 ?  22  GLY B N     1 
ATOM   5693  C  CA    . GLY B 1 22  ? 137.075 110.029 179.885 1.00 66.05 ?  22  GLY B CA    1 
ATOM   5694  C  C     . GLY B 1 22  ? 136.644 111.438 179.547 1.00 67.44 ?  22  GLY B C     1 
ATOM   5695  O  O     . GLY B 1 22  ? 135.497 111.632 179.131 1.00 67.11 ?  22  GLY B O     1 
ATOM   5696  N  N     . LYS B 1 23  ? 137.520 112.426 179.708 1.00 66.70 ?  23  LYS B N     1 
ATOM   5697  C  CA    . LYS B 1 23  ? 137.187 113.819 179.457 1.00 63.82 ?  23  LYS B CA    1 
ATOM   5698  C  C     . LYS B 1 23  ? 138.169 114.424 178.463 1.00 63.01 ?  23  LYS B C     1 
ATOM   5699  O  O     . LYS B 1 23  ? 139.349 114.059 178.430 1.00 64.84 ?  23  LYS B O     1 
ATOM   5700  C  CB    . LYS B 1 23  ? 137.201 114.638 180.755 1.00 63.78 ?  23  LYS B CB    1 
ATOM   5701  C  CG    . LYS B 1 23  ? 136.589 113.925 181.946 1.00 65.44 ?  23  LYS B CG    1 
ATOM   5702  C  CD    . LYS B 1 23  ? 135.092 113.743 181.767 1.00 65.22 ?  23  LYS B CD    1 
ATOM   5703  C  CE    . LYS B 1 23  ? 134.351 115.041 182.030 1.00 64.91 ?  23  LYS B CE    1 
ATOM   5704  N  NZ    . LYS B 1 23  ? 135.009 115.839 183.099 1.00 63.67 1  23  LYS B NZ    1 
ATOM   5705  N  N     . PHE B 1 24  ? 137.668 115.352 177.652 1.00 59.23 ?  24  PHE B N     1 
ATOM   5706  C  CA    . PHE B 1 24  ? 138.518 116.050 176.697 1.00 57.17 ?  24  PHE B CA    1 
ATOM   5707  C  C     . PHE B 1 24  ? 139.523 116.932 177.426 1.00 56.29 ?  24  PHE B C     1 
ATOM   5708  O  O     . PHE B 1 24  ? 139.226 117.505 178.477 1.00 56.56 ?  24  PHE B O     1 
ATOM   5709  C  CB    . PHE B 1 24  ? 137.671 116.898 175.750 1.00 55.54 ?  24  PHE B CB    1 
ATOM   5710  C  CG    . PHE B 1 24  ? 136.990 116.110 174.667 1.00 55.27 ?  24  PHE B CG    1 
ATOM   5711  C  CD1   . PHE B 1 24  ? 137.696 115.678 173.558 1.00 57.16 ?  24  PHE B CD1   1 
ATOM   5712  C  CD2   . PHE B 1 24  ? 135.641 115.812 174.755 1.00 55.44 ?  24  PHE B CD2   1 
ATOM   5713  C  CE1   . PHE B 1 24  ? 137.070 114.955 172.560 1.00 56.09 ?  24  PHE B CE1   1 
ATOM   5714  C  CE2   . PHE B 1 24  ? 135.011 115.090 173.760 1.00 56.44 ?  24  PHE B CE2   1 
ATOM   5715  C  CZ    . PHE B 1 24  ? 135.727 114.663 172.661 1.00 55.50 ?  24  PHE B CZ    1 
ATOM   5716  N  N     . GLN B 1 25  ? 140.725 117.039 176.857 1.00 57.29 ?  25  GLN B N     1 
ATOM   5717  C  CA    . GLN B 1 25  ? 141.786 117.866 177.435 1.00 57.15 ?  25  GLN B CA    1 
ATOM   5718  C  C     . GLN B 1 25  ? 141.711 119.257 176.812 1.00 57.88 ?  25  GLN B C     1 
ATOM   5719  O  O     . GLN B 1 25  ? 142.511 119.639 175.955 1.00 59.45 ?  25  GLN B O     1 
ATOM   5720  C  CB    . GLN B 1 25  ? 143.148 117.218 177.220 1.00 57.43 ?  25  GLN B CB    1 
ATOM   5721  C  CG    . GLN B 1 25  ? 143.263 115.814 177.785 1.00 57.27 ?  25  GLN B CG    1 
ATOM   5722  C  CD    . GLN B 1 25  ? 144.635 115.211 177.567 1.00 58.27 ?  25  GLN B CD    1 
ATOM   5723  O  OE1   . GLN B 1 25  ? 145.497 115.270 178.443 1.00 58.75 ?  25  GLN B OE1   1 
ATOM   5724  N  NE2   . GLN B 1 25  ? 144.845 114.628 176.393 1.00 58.57 ?  25  GLN B NE2   1 
ATOM   5725  N  N     . PHE B 1 26  ? 140.717 120.025 177.261 1.00 51.55 ?  26  PHE B N     1 
ATOM   5726  C  CA    . PHE B 1 26  ? 140.524 121.372 176.732 1.00 52.93 ?  26  PHE B CA    1 
ATOM   5727  C  C     . PHE B 1 26  ? 141.685 122.287 177.106 1.00 53.51 ?  26  PHE B C     1 
ATOM   5728  O  O     . PHE B 1 26  ? 142.096 123.135 176.304 1.00 52.89 ?  26  PHE B O     1 
ATOM   5729  C  CB    . PHE B 1 26  ? 139.201 121.947 177.235 1.00 50.12 ?  26  PHE B CB    1 
ATOM   5730  C  CG    . PHE B 1 26  ? 137.992 121.204 176.744 1.00 51.96 ?  26  PHE B CG    1 
ATOM   5731  C  CD1   . PHE B 1 26  ? 137.768 121.040 175.387 1.00 51.08 ?  26  PHE B CD1   1 
ATOM   5732  C  CD2   . PHE B 1 26  ? 137.080 120.670 177.637 1.00 50.64 ?  26  PHE B CD2   1 
ATOM   5733  C  CE1   . PHE B 1 26  ? 136.658 120.358 174.931 1.00 49.46 ?  26  PHE B CE1   1 
ATOM   5734  C  CE2   . PHE B 1 26  ? 135.968 119.986 177.187 1.00 49.81 ?  26  PHE B CE2   1 
ATOM   5735  C  CZ    . PHE B 1 26  ? 135.756 119.831 175.833 1.00 49.40 ?  26  PHE B CZ    1 
ATOM   5736  N  N     . ASP B 1 27  ? 142.224 122.131 178.320 1.00 57.05 ?  27  ASP B N     1 
ATOM   5737  C  CA    . ASP B 1 27  ? 143.313 122.992 178.769 1.00 54.92 ?  27  ASP B CA    1 
ATOM   5738  C  C     . ASP B 1 27  ? 144.536 122.875 177.869 1.00 55.84 ?  27  ASP B C     1 
ATOM   5739  O  O     . ASP B 1 27  ? 145.295 123.843 177.728 1.00 55.38 ?  27  ASP B O     1 
ATOM   5740  C  CB    . ASP B 1 27  ? 143.682 122.657 180.214 1.00 55.14 ?  27  ASP B CB    1 
ATOM   5741  C  CG    . ASP B 1 27  ? 143.556 121.178 180.519 1.00 59.58 ?  27  ASP B CG    1 
ATOM   5742  O  OD1   . ASP B 1 27  ? 143.982 120.357 179.681 1.00 58.90 ?  27  ASP B OD1   1 
ATOM   5743  O  OD2   . ASP B 1 27  ? 143.028 120.835 181.598 1.00 60.21 -1 27  ASP B OD2   1 
ATOM   5744  N  N     . LYS B 1 28  ? 144.736 121.710 177.246 1.00 55.09 ?  28  LYS B N     1 
ATOM   5745  C  CA    . LYS B 1 28  ? 145.842 121.548 176.307 1.00 55.69 ?  28  LYS B CA    1 
ATOM   5746  C  C     . LYS B 1 28  ? 145.798 122.615 175.223 1.00 55.91 ?  28  LYS B C     1 
ATOM   5747  O  O     . LYS B 1 28  ? 146.846 123.110 174.786 1.00 58.39 ?  28  LYS B O     1 
ATOM   5748  C  CB    . LYS B 1 28  ? 145.803 120.153 175.685 1.00 56.35 ?  28  LYS B CB    1 
ATOM   5749  C  CG    . LYS B 1 28  ? 146.329 119.047 176.585 1.00 56.47 ?  28  LYS B CG    1 
ATOM   5750  C  CD    . LYS B 1 28  ? 147.834 119.144 176.759 1.00 56.20 ?  28  LYS B CD    1 
ATOM   5751  C  CE    . LYS B 1 28  ? 148.340 118.116 177.757 1.00 56.98 ?  28  LYS B CE    1 
ATOM   5752  N  NZ    . LYS B 1 28  ? 149.136 118.744 178.847 1.00 55.47 1  28  LYS B NZ    1 
ATOM   5753  N  N     . ASP B 1 29  ? 144.590 123.002 174.800 1.00 54.35 ?  29  ASP B N     1 
ATOM   5754  C  CA    . ASP B 1 29  ? 144.439 124.062 173.810 1.00 52.22 ?  29  ASP B CA    1 
ATOM   5755  C  C     . ASP B 1 29  ? 145.213 125.305 174.223 1.00 52.26 ?  29  ASP B C     1 
ATOM   5756  O  O     . ASP B 1 29  ? 145.972 125.868 173.427 1.00 52.34 ?  29  ASP B O     1 
ATOM   5757  C  CB    . ASP B 1 29  ? 142.959 124.395 173.623 1.00 52.42 ?  29  ASP B CB    1 
ATOM   5758  C  CG    . ASP B 1 29  ? 142.665 124.999 172.264 1.00 54.90 ?  29  ASP B CG    1 
ATOM   5759  O  OD1   . ASP B 1 29  ? 143.406 124.699 171.305 1.00 55.08 ?  29  ASP B OD1   1 
ATOM   5760  O  OD2   . ASP B 1 29  ? 141.691 125.772 172.157 1.00 52.90 -1 29  ASP B OD2   1 
ATOM   5761  N  N     . LYS B 1 30  ? 145.058 125.720 175.483 1.00 52.18 ?  30  LYS B N     1 
ATOM   5762  C  CA    . LYS B 1 30  ? 145.787 126.884 175.974 1.00 53.26 ?  30  LYS B CA    1 
ATOM   5763  C  C     . LYS B 1 30  ? 147.285 126.698 175.785 1.00 51.63 ?  30  LYS B C     1 
ATOM   5764  O  O     . LYS B 1 30  ? 147.972 127.579 175.251 1.00 55.03 ?  30  LYS B O     1 
ATOM   5765  C  CB    . LYS B 1 30  ? 145.454 127.127 177.447 1.00 52.12 ?  30  LYS B CB    1 
ATOM   5766  C  CG    . LYS B 1 30  ? 146.135 128.347 178.043 1.00 51.47 ?  30  LYS B CG    1 
ATOM   5767  C  CD    . LYS B 1 30  ? 145.713 128.565 179.486 1.00 53.30 ?  30  LYS B CD    1 
ATOM   5768  C  CE    . LYS B 1 30  ? 146.410 129.775 180.086 1.00 55.90 ?  30  LYS B CE    1 
ATOM   5769  N  NZ    . LYS B 1 30  ? 146.007 130.003 181.500 1.00 55.29 1  30  LYS B NZ    1 
ATOM   5770  N  N     . GLU B 1 31  ? 147.798 125.527 176.175 1.00 53.21 ?  31  GLU B N     1 
ATOM   5771  C  CA    . GLU B 1 31  ? 149.215 125.243 175.983 1.00 52.85 ?  31  GLU B CA    1 
ATOM   5772  C  C     . GLU B 1 31  ? 149.611 125.458 174.531 1.00 52.18 ?  31  GLU B C     1 
ATOM   5773  O  O     . GLU B 1 31  ? 150.633 126.095 174.245 1.00 54.46 ?  31  GLU B O     1 
ATOM   5774  C  CB    . GLU B 1 31  ? 149.526 123.812 176.422 1.00 52.70 ?  31  GLU B CB    1 
ATOM   5775  C  CG    . GLU B 1 31  ? 149.277 123.547 177.897 1.00 54.76 ?  31  GLU B CG    1 
ATOM   5776  C  CD    . GLU B 1 31  ? 149.336 122.072 178.241 1.00 57.88 ?  31  GLU B CD    1 
ATOM   5777  O  OE1   . GLU B 1 31  ? 150.161 121.354 177.640 1.00 59.45 ?  31  GLU B OE1   1 
ATOM   5778  O  OE2   . GLU B 1 31  ? 148.557 121.630 179.111 1.00 56.50 -1 31  GLU B OE2   1 
ATOM   5779  N  N     . ALA B 1 32  ? 148.772 124.988 173.604 1.00 43.56 ?  32  ALA B N     1 
ATOM   5780  C  CA    . ALA B 1 32  ? 149.062 125.146 172.185 1.00 44.58 ?  32  ALA B CA    1 
ATOM   5781  C  C     . ALA B 1 32  ? 149.321 126.605 171.844 1.00 48.74 ?  32  ALA B C     1 
ATOM   5782  O  O     . ALA B 1 32  ? 150.336 126.935 171.215 1.00 50.09 ?  32  ALA B O     1 
ATOM   5783  C  CB    . ALA B 1 32  ? 147.911 124.590 171.348 1.00 44.78 ?  32  ALA B CB    1 
ATOM   5784  N  N     . VAL B 1 33  ? 148.444 127.504 172.308 1.00 49.04 ?  33  VAL B N     1 
ATOM   5785  C  CA    . VAL B 1 33  ? 148.624 128.921 172.006 1.00 47.36 ?  33  VAL B CA    1 
ATOM   5786  C  C     . VAL B 1 33  ? 149.992 129.380 172.483 1.00 47.53 ?  33  VAL B C     1 
ATOM   5787  O  O     . VAL B 1 33  ? 150.745 130.021 171.739 1.00 49.67 ?  33  VAL B O     1 
ATOM   5788  C  CB    . VAL B 1 33  ? 147.499 129.769 172.626 1.00 45.21 ?  33  VAL B CB    1 
ATOM   5789  C  CG1   . VAL B 1 33  ? 147.090 130.877 171.670 1.00 45.04 ?  33  VAL B CG1   1 
ATOM   5790  C  CG2   . VAL B 1 33  ? 146.307 128.912 172.968 1.00 47.96 ?  33  VAL B CG2   1 
ATOM   5791  N  N     . HIS B 1 34  ? 150.353 129.007 173.715 1.00 44.02 ?  34  HIS B N     1 
ATOM   5792  C  CA    . HIS B 1 34  ? 151.671 129.359 174.226 1.00 45.18 ?  34  HIS B CA    1 
ATOM   5793  C  C     . HIS B 1 34  ? 152.753 128.882 173.271 1.00 45.96 ?  34  HIS B C     1 
ATOM   5794  O  O     . HIS B 1 34  ? 153.596 129.672 172.826 1.00 49.13 ?  34  HIS B O     1 
ATOM   5795  C  CB    . HIS B 1 34  ? 151.872 128.766 175.620 1.00 50.39 ?  34  HIS B CB    1 
ATOM   5796  C  CG    . HIS B 1 34  ? 152.829 129.540 176.470 1.00 49.36 ?  34  HIS B CG    1 
ATOM   5797  N  ND1   . HIS B 1 34  ? 154.123 129.124 176.703 1.00 48.47 ?  34  HIS B ND1   1 
ATOM   5798  C  CD2   . HIS B 1 34  ? 152.683 130.708 177.140 1.00 49.42 ?  34  HIS B CD2   1 
ATOM   5799  C  CE1   . HIS B 1 34  ? 154.731 130.001 177.481 1.00 50.02 ?  34  HIS B CE1   1 
ATOM   5800  N  NE2   . HIS B 1 34  ? 153.880 130.972 177.760 1.00 51.44 ?  34  HIS B NE2   1 
ATOM   5801  N  N     . SER B 1 35  ? 152.699 127.604 172.889 1.00 46.26 ?  35  SER B N     1 
ATOM   5802  C  CA    . SER B 1 35  ? 153.653 127.093 171.914 1.00 47.37 ?  35  SER B CA    1 
ATOM   5803  C  C     . SER B 1 35  ? 153.594 127.916 170.638 1.00 46.78 ?  35  SER B C     1 
ATOM   5804  O  O     . SER B 1 35  ? 154.620 128.415 170.158 1.00 50.48 ?  35  SER B O     1 
ATOM   5805  C  CB    . SER B 1 35  ? 153.373 125.618 171.626 1.00 48.20 ?  35  SER B CB    1 
ATOM   5806  O  OG    . SER B 1 35  ? 154.075 125.182 170.477 1.00 48.65 ?  35  SER B OG    1 
ATOM   5807  N  N     . TYR B 1 36  ? 152.378 128.143 170.126 1.00 47.40 ?  36  TYR B N     1 
ATOM   5808  C  CA    . TYR B 1 36  ? 152.218 128.871 168.875 1.00 45.60 ?  36  TYR B CA    1 
ATOM   5809  C  C     . TYR B 1 36  ? 152.842 130.254 168.959 1.00 46.42 ?  36  TYR B C     1 
ATOM   5810  O  O     . TYR B 1 36  ? 153.236 130.820 167.933 1.00 47.08 ?  36  TYR B O     1 
ATOM   5811  C  CB    . TYR B 1 36  ? 150.736 128.976 168.515 1.00 44.83 ?  36  TYR B CB    1 
ATOM   5812  C  CG    . TYR B 1 36  ? 150.468 129.607 167.169 1.00 45.26 ?  36  TYR B CG    1 
ATOM   5813  C  CD1   . TYR B 1 36  ? 150.978 129.049 166.004 1.00 44.63 ?  36  TYR B CD1   1 
ATOM   5814  C  CD2   . TYR B 1 36  ? 149.701 130.759 167.061 1.00 42.99 ?  36  TYR B CD2   1 
ATOM   5815  C  CE1   . TYR B 1 36  ? 150.732 129.619 164.772 1.00 43.22 ?  36  TYR B CE1   1 
ATOM   5816  C  CE2   . TYR B 1 36  ? 149.451 131.337 165.834 1.00 44.18 ?  36  TYR B CE2   1 
ATOM   5817  C  CZ    . TYR B 1 36  ? 149.969 130.764 164.692 1.00 44.46 ?  36  TYR B CZ    1 
ATOM   5818  O  OH    . TYR B 1 36  ? 149.723 131.338 163.466 1.00 43.59 ?  36  TYR B OH    1 
ATOM   5819  N  N     . PHE B 1 37  ? 152.959 130.804 170.165 1.00 49.89 ?  37  PHE B N     1 
ATOM   5820  C  CA    . PHE B 1 37  ? 153.603 132.098 170.319 1.00 49.17 ?  37  PHE B CA    1 
ATOM   5821  C  C     . PHE B 1 37  ? 155.080 131.971 170.662 1.00 51.17 ?  37  PHE B C     1 
ATOM   5822  O  O     . PHE B 1 37  ? 155.888 132.783 170.202 1.00 55.25 ?  37  PHE B O     1 
ATOM   5823  C  CB    . PHE B 1 37  ? 152.877 132.924 171.382 1.00 49.72 ?  37  PHE B CB    1 
ATOM   5824  C  CG    . PHE B 1 37  ? 151.674 133.647 170.855 1.00 50.79 ?  37  PHE B CG    1 
ATOM   5825  C  CD1   . PHE B 1 37  ? 151.809 134.874 170.230 1.00 51.43 ?  37  PHE B CD1   1 
ATOM   5826  C  CD2   . PHE B 1 37  ? 150.412 133.095 170.969 1.00 50.28 ?  37  PHE B CD2   1 
ATOM   5827  C  CE1   . PHE B 1 37  ? 150.706 135.540 169.738 1.00 50.45 ?  37  PHE B CE1   1 
ATOM   5828  C  CE2   . PHE B 1 37  ? 149.306 133.756 170.479 1.00 48.78 ?  37  PHE B CE2   1 
ATOM   5829  C  CZ    . PHE B 1 37  ? 149.454 134.979 169.861 1.00 48.83 ?  37  PHE B CZ    1 
ATOM   5830  N  N     . VAL B 1 38  ? 155.464 130.960 171.448 1.00 52.14 ?  38  VAL B N     1 
ATOM   5831  C  CA    . VAL B 1 38  ? 156.864 130.867 171.861 1.00 51.44 ?  38  VAL B CA    1 
ATOM   5832  C  C     . VAL B 1 38  ? 157.730 130.159 170.835 1.00 53.54 ?  38  VAL B C     1 
ATOM   5833  O  O     . VAL B 1 38  ? 158.955 130.110 171.003 1.00 56.53 ?  38  VAL B O     1 
ATOM   5834  C  CB    . VAL B 1 38  ? 157.024 130.157 173.219 1.00 50.73 ?  38  VAL B CB    1 
ATOM   5835  C  CG1   . VAL B 1 38  ? 156.184 130.849 174.285 1.00 50.91 ?  38  VAL B CG1   1 
ATOM   5836  C  CG2   . VAL B 1 38  ? 156.665 128.686 173.103 1.00 49.68 ?  38  VAL B CG2   1 
ATOM   5837  N  N     . ASP B 1 39  ? 157.135 129.615 169.778 1.00 50.18 ?  39  ASP B N     1 
ATOM   5838  C  CA    . ASP B 1 39  ? 157.884 128.923 168.743 1.00 51.31 ?  39  ASP B CA    1 
ATOM   5839  C  C     . ASP B 1 39  ? 157.677 129.485 167.346 1.00 53.35 ?  39  ASP B C     1 
ATOM   5840  O  O     . ASP B 1 39  ? 158.575 129.354 166.512 1.00 56.10 ?  39  ASP B O     1 
ATOM   5841  C  CB    . ASP B 1 39  ? 157.525 127.428 168.732 1.00 52.76 ?  39  ASP B CB    1 
ATOM   5842  C  CG    . ASP B 1 39  ? 157.631 126.793 170.104 1.00 54.28 ?  39  ASP B CG    1 
ATOM   5843  O  OD1   . ASP B 1 39  ? 158.543 127.171 170.867 1.00 54.59 ?  39  ASP B OD1   1 
ATOM   5844  O  OD2   . ASP B 1 39  ? 156.800 125.916 170.419 1.00 53.25 -1 39  ASP B OD2   1 
ATOM   5845  N  N     . TYR B 1 40  ? 156.528 130.100 167.060 1.00 53.18 ?  40  TYR B N     1 
ATOM   5846  C  CA    . TYR B 1 40  ? 156.257 130.617 165.723 1.00 53.04 ?  40  TYR B CA    1 
ATOM   5847  C  C     . TYR B 1 40  ? 156.053 132.126 165.701 1.00 55.10 ?  40  TYR B C     1 
ATOM   5848  O  O     . TYR B 1 40  ? 156.748 132.819 164.951 1.00 55.56 ?  40  TYR B O     1 
ATOM   5849  C  CB    . TYR B 1 40  ? 155.036 129.911 165.124 1.00 52.98 ?  40  TYR B CB    1 
ATOM   5850  C  CG    . TYR B 1 40  ? 154.901 130.099 163.630 1.00 52.53 ?  40  TYR B CG    1 
ATOM   5851  C  CD1   . TYR B 1 40  ? 155.670 129.355 162.746 1.00 53.26 ?  40  TYR B CD1   1 
ATOM   5852  C  CD2   . TYR B 1 40  ? 154.007 131.022 163.104 1.00 51.96 ?  40  TYR B CD2   1 
ATOM   5853  C  CE1   . TYR B 1 40  ? 155.552 129.523 161.380 1.00 55.40 ?  40  TYR B CE1   1 
ATOM   5854  C  CE2   . TYR B 1 40  ? 153.883 131.199 161.739 1.00 52.85 ?  40  TYR B CE2   1 
ATOM   5855  C  CZ    . TYR B 1 40  ? 154.658 130.446 160.882 1.00 56.50 ?  40  TYR B CZ    1 
ATOM   5856  O  OH    . TYR B 1 40  ? 154.538 130.616 159.522 1.00 57.66 ?  40  TYR B OH    1 
ATOM   5857  N  N     . ILE B 1 41  ? 155.126 132.662 166.497 1.00 55.05 ?  41  ILE B N     1 
ATOM   5858  C  CA    . ILE B 1 41  ? 154.731 134.059 166.332 1.00 53.28 ?  41  ILE B CA    1 
ATOM   5859  C  C     . ILE B 1 41  ? 155.847 134.996 166.777 1.00 52.04 ?  41  ILE B C     1 
ATOM   5860  O  O     . ILE B 1 41  ? 156.183 135.958 166.076 1.00 54.19 ?  41  ILE B O     1 
ATOM   5861  C  CB    . ILE B 1 41  ? 153.420 134.343 167.087 1.00 50.85 ?  41  ILE B CB    1 
ATOM   5862  C  CG1   . ILE B 1 41  ? 152.290 133.474 166.535 1.00 48.55 ?  41  ILE B CG1   1 
ATOM   5863  C  CG2   . ILE B 1 41  ? 153.052 135.814 166.979 1.00 49.09 ?  41  ILE B CG2   1 
ATOM   5864  C  CD1   . ILE B 1 41  ? 152.148 133.540 165.033 1.00 49.11 ?  41  ILE B CD1   1 
ATOM   5865  N  N     . ASN B 1 42  ? 156.442 134.733 167.943 1.00 50.52 ?  42  ASN B N     1 
ATOM   5866  C  CA    . ASN B 1 42  ? 157.496 135.614 168.435 1.00 51.96 ?  42  ASN B CA    1 
ATOM   5867  C  C     . ASN B 1 42  ? 158.745 135.536 167.568 1.00 54.31 ?  42  ASN B C     1 
ATOM   5868  O  O     . ASN B 1 42  ? 159.466 136.531 167.431 1.00 54.08 ?  42  ASN B O     1 
ATOM   5869  C  CB    . ASN B 1 42  ? 157.832 135.280 169.887 1.00 53.11 ?  42  ASN B CB    1 
ATOM   5870  C  CG    . ASN B 1 42  ? 156.693 135.597 170.836 1.00 53.45 ?  42  ASN B CG    1 
ATOM   5871  O  OD1   . ASN B 1 42  ? 155.714 136.238 170.455 1.00 56.58 ?  42  ASN B OD1   1 
ATOM   5872  N  ND2   . ASN B 1 42  ? 156.816 135.146 172.079 1.00 53.35 ?  42  ASN B ND2   1 
ATOM   5873  N  N     . GLN B 1 43  ? 159.022 134.371 166.981 1.00 58.65 ?  43  GLN B N     1 
ATOM   5874  C  CA    . GLN B 1 43  ? 160.169 134.245 166.089 1.00 57.83 ?  43  GLN B CA    1 
ATOM   5875  C  C     . GLN B 1 43  ? 159.894 134.868 164.725 1.00 56.26 ?  43  GLN B C     1 
ATOM   5876  O  O     . GLN B 1 43  ? 160.794 135.455 164.117 1.00 58.13 ?  43  GLN B O     1 
ATOM   5877  C  CB    . GLN B 1 43  ? 160.559 132.775 165.939 1.00 58.46 ?  43  GLN B CB    1 
ATOM   5878  C  CG    . GLN B 1 43  ? 161.597 132.308 166.944 1.00 58.98 ?  43  GLN B CG    1 
ATOM   5879  C  CD    . GLN B 1 43  ? 160.987 131.903 168.270 1.00 60.06 ?  43  GLN B CD    1 
ATOM   5880  O  OE1   . GLN B 1 43  ? 160.579 130.758 168.454 1.00 59.73 ?  43  GLN B OE1   1 
ATOM   5881  N  NE2   . GLN B 1 43  ? 160.923 132.845 169.205 1.00 59.72 ?  43  GLN B NE2   1 
ATOM   5882  N  N     . ASN B 1 44  ? 158.664 134.750 164.231 1.00 56.45 ?  44  ASN B N     1 
ATOM   5883  C  CA    . ASN B 1 44  ? 158.304 135.279 162.923 1.00 56.94 ?  44  ASN B CA    1 
ATOM   5884  C  C     . ASN B 1 44  ? 157.875 136.740 162.967 1.00 55.64 ?  44  ASN B C     1 
ATOM   5885  O  O     . ASN B 1 44  ? 157.648 137.335 161.909 1.00 56.35 ?  44  ASN B O     1 
ATOM   5886  C  CB    . ASN B 1 44  ? 157.186 134.438 162.299 1.00 55.57 ?  44  ASN B CB    1 
ATOM   5887  C  CG    . ASN B 1 44  ? 157.718 133.308 161.442 1.00 56.91 ?  44  ASN B CG    1 
ATOM   5888  O  OD1   . ASN B 1 44  ? 158.685 132.640 161.808 1.00 58.79 ?  44  ASN B OD1   1 
ATOM   5889  N  ND2   . ASN B 1 44  ? 157.087 133.087 160.295 1.00 58.76 ?  44  ASN B ND2   1 
ATOM   5890  N  N     . THR B 1 45  ? 157.755 137.329 164.151 1.00 55.50 ?  45  THR B N     1 
ATOM   5891  C  CA    . THR B 1 45  ? 157.413 138.738 164.249 1.00 56.66 ?  45  THR B CA    1 
ATOM   5892  C  C     . THR B 1 45  ? 158.638 139.601 163.968 1.00 57.37 ?  45  THR B C     1 
ATOM   5893  O  O     . THR B 1 45  ? 159.782 139.181 164.167 1.00 60.83 ?  45  THR B O     1 
ATOM   5894  C  CB    . THR B 1 45  ? 156.831 139.066 165.629 1.00 56.50 ?  45  THR B CB    1 
ATOM   5895  O  OG1   . THR B 1 45  ? 156.313 140.400 165.628 1.00 56.05 ?  45  THR B OG1   1 
ATOM   5896  C  CG2   . THR B 1 45  ? 157.887 138.938 166.720 1.00 55.69 ?  45  THR B CG2   1 
ATOM   5897  N  N     . VAL B 1 46  ? 158.388 140.806 163.467 1.00 56.32 ?  46  VAL B N     1 
ATOM   5898  C  CA    . VAL B 1 46  ? 159.440 141.770 163.173 1.00 57.35 ?  46  VAL B CA    1 
ATOM   5899  C  C     . VAL B 1 46  ? 159.409 142.840 164.255 1.00 57.06 ?  46  VAL B C     1 
ATOM   5900  O  O     . VAL B 1 46  ? 158.426 143.579 164.382 1.00 58.31 ?  46  VAL B O     1 
ATOM   5901  C  CB    . VAL B 1 46  ? 159.264 142.387 161.777 1.00 56.58 ?  46  VAL B CB    1 
ATOM   5902  C  CG1   . VAL B 1 46  ? 160.134 143.623 161.630 1.00 55.16 ?  46  VAL B CG1   1 
ATOM   5903  C  CG2   . VAL B 1 46  ? 159.603 141.370 160.705 1.00 55.55 ?  46  VAL B CG2   1 
ATOM   5904  N  N     . PHE B 1 47  ? 160.480 142.922 165.035 1.00 58.54 ?  47  PHE B N     1 
ATOM   5905  C  CA    . PHE B 1 47  ? 160.573 143.878 166.126 1.00 60.28 ?  47  PHE B CA    1 
ATOM   5906  C  C     . PHE B 1 47  ? 161.476 145.041 165.738 1.00 60.60 ?  47  PHE B C     1 
ATOM   5907  O  O     . PHE B 1 47  ? 162.491 144.869 165.061 1.00 61.43 ?  47  PHE B O     1 
ATOM   5908  C  CB    . PHE B 1 47  ? 161.103 143.212 167.397 1.00 60.54 ?  47  PHE B CB    1 
ATOM   5909  C  CG    . PHE B 1 47  ? 160.784 143.971 168.654 1.00 60.62 ?  47  PHE B CG    1 
ATOM   5910  C  CD1   . PHE B 1 47  ? 159.472 144.252 168.995 1.00 59.97 ?  47  PHE B CD1   1 
ATOM   5911  C  CD2   . PHE B 1 47  ? 161.798 144.406 169.492 1.00 60.05 ?  47  PHE B CD2   1 
ATOM   5912  C  CE1   . PHE B 1 47  ? 159.176 144.950 170.151 1.00 60.86 ?  47  PHE B CE1   1 
ATOM   5913  C  CE2   . PHE B 1 47  ? 161.508 145.104 170.649 1.00 60.57 ?  47  PHE B CE2   1 
ATOM   5914  C  CZ    . PHE B 1 47  ? 160.195 145.378 170.978 1.00 61.43 ?  47  PHE B CZ    1 
ATOM   5915  N  N     . PHE B 1 48  ? 161.089 146.234 166.178 1.00 56.81 ?  48  PHE B N     1 
ATOM   5916  C  CA    . PHE B 1 48  ? 161.847 147.450 165.945 1.00 56.47 ?  48  PHE B CA    1 
ATOM   5917  C  C     . PHE B 1 48  ? 162.333 148.002 167.277 1.00 59.30 ?  48  PHE B C     1 
ATOM   5918  O  O     . PHE B 1 48  ? 161.900 147.566 168.348 1.00 59.94 ?  48  PHE B O     1 
ATOM   5919  C  CB    . PHE B 1 48  ? 161.008 148.504 165.209 1.00 56.72 ?  48  PHE B CB    1 
ATOM   5920  C  CG    . PHE B 1 48  ? 160.511 148.057 163.862 1.00 57.71 ?  48  PHE B CG    1 
ATOM   5921  C  CD1   . PHE B 1 48  ? 159.426 147.201 163.753 1.00 56.37 ?  48  PHE B CD1   1 
ATOM   5922  C  CD2   . PHE B 1 48  ? 161.126 148.497 162.703 1.00 57.45 ?  48  PHE B CD2   1 
ATOM   5923  C  CE1   . PHE B 1 48  ? 158.968 146.794 162.516 1.00 56.89 ?  48  PHE B CE1   1 
ATOM   5924  C  CE2   . PHE B 1 48  ? 160.673 148.091 161.464 1.00 56.57 ?  48  PHE B CE2   1 
ATOM   5925  C  CZ    . PHE B 1 48  ? 159.593 147.239 161.370 1.00 56.22 ?  48  PHE B CZ    1 
ATOM   5926  N  N     . HIS B 1 49  ? 163.252 148.968 167.202 1.00 62.05 ?  49  HIS B N     1 
ATOM   5927  C  CA    . HIS B 1 49  ? 163.795 149.558 168.422 1.00 62.83 ?  49  HIS B CA    1 
ATOM   5928  C  C     . HIS B 1 49  ? 162.705 150.254 169.229 1.00 63.07 ?  49  HIS B C     1 
ATOM   5929  O  O     . HIS B 1 49  ? 162.654 150.125 170.457 1.00 64.37 ?  49  HIS B O     1 
ATOM   5930  C  CB    . HIS B 1 49  ? 164.919 150.536 168.080 1.00 64.35 ?  49  HIS B CB    1 
ATOM   5931  C  CG    . HIS B 1 49  ? 165.604 151.108 169.281 1.00 65.21 ?  49  HIS B CG    1 
ATOM   5932  N  ND1   . HIS B 1 49  ? 166.133 150.321 170.281 1.00 63.91 ?  49  HIS B ND1   1 
ATOM   5933  C  CD2   . HIS B 1 49  ? 165.843 152.390 169.646 1.00 63.74 ?  49  HIS B CD2   1 
ATOM   5934  C  CE1   . HIS B 1 49  ? 166.671 151.093 171.209 1.00 63.98 ?  49  HIS B CE1   1 
ATOM   5935  N  NE2   . HIS B 1 49  ? 166.508 152.353 170.847 1.00 63.41 ?  49  HIS B NE2   1 
ATOM   5936  N  N     . ASN B 1 50  ? 161.825 150.991 168.556 1.00 61.05 ?  50  ASN B N     1 
ATOM   5937  C  CA    . ASN B 1 50  ? 160.666 151.590 169.200 1.00 62.50 ?  50  ASN B CA    1 
ATOM   5938  C  C     . ASN B 1 50  ? 159.544 151.687 168.175 1.00 60.99 ?  50  ASN B C     1 
ATOM   5939  O  O     . ASN B 1 50  ? 159.682 151.250 167.029 1.00 58.84 ?  50  ASN B O     1 
ATOM   5940  C  CB    . ASN B 1 50  ? 161.003 152.956 169.809 1.00 61.56 ?  50  ASN B CB    1 
ATOM   5941  C  CG    . ASN B 1 50  ? 161.674 153.886 168.822 1.00 62.99 ?  50  ASN B CG    1 
ATOM   5942  O  OD1   . ASN B 1 50  ? 161.922 153.519 167.676 1.00 62.27 ?  50  ASN B OD1   1 
ATOM   5943  N  ND2   . ASN B 1 50  ? 161.969 155.103 169.262 1.00 63.03 ?  50  ASN B ND2   1 
ATOM   5944  N  N     . LEU B 1 51  ? 158.419 152.266 168.601 1.00 55.35 ?  51  LEU B N     1 
ATOM   5945  C  CA    . LEU B 1 51  ? 157.257 152.362 167.725 1.00 54.03 ?  51  LEU B CA    1 
ATOM   5946  C  C     . LEU B 1 51  ? 157.508 153.303 166.553 1.00 56.24 ?  51  LEU B C     1 
ATOM   5947  O  O     . LEU B 1 51  ? 156.893 153.146 165.491 1.00 56.85 ?  51  LEU B O     1 
ATOM   5948  C  CB    . LEU B 1 51  ? 156.039 152.820 168.527 1.00 55.44 ?  51  LEU B CB    1 
ATOM   5949  C  CG    . LEU B 1 51  ? 154.692 152.829 167.805 1.00 53.80 ?  51  LEU B CG    1 
ATOM   5950  C  CD1   . LEU B 1 51  ? 154.303 151.424 167.373 1.00 51.80 ?  51  LEU B CD1   1 
ATOM   5951  C  CD2   . LEU B 1 51  ? 153.623 153.437 168.692 1.00 53.40 ?  51  LEU B CD2   1 
ATOM   5952  N  N     . LYS B 1 52  ? 158.398 154.284 166.724 1.00 56.71 ?  52  LYS B N     1 
ATOM   5953  C  CA    . LYS B 1 52  ? 158.666 155.238 165.650 1.00 55.26 ?  52  LYS B CA    1 
ATOM   5954  C  C     . LYS B 1 52  ? 159.247 154.540 164.427 1.00 56.32 ?  52  LYS B C     1 
ATOM   5955  O  O     . LYS B 1 52  ? 158.809 154.779 163.296 1.00 57.80 ?  52  LYS B O     1 
ATOM   5956  C  CB    . LYS B 1 52  ? 159.613 156.331 166.145 1.00 56.33 ?  52  LYS B CB    1 
ATOM   5957  C  CG    . LYS B 1 52  ? 159.062 157.741 166.004 1.00 57.26 ?  52  LYS B CG    1 
ATOM   5958  C  CD    . LYS B 1 52  ? 158.944 158.150 164.547 1.00 58.35 ?  52  LYS B CD    1 
ATOM   5959  C  CE    . LYS B 1 52  ? 158.105 159.409 164.397 1.00 58.29 ?  52  LYS B CE    1 
ATOM   5960  N  NZ    . LYS B 1 52  ? 157.851 159.742 162.968 1.00 58.58 1  52  LYS B NZ    1 
ATOM   5961  N  N     . GLU B 1 53  ? 160.237 153.668 164.637 1.00 59.10 ?  53  GLU B N     1 
ATOM   5962  C  CA    . GLU B 1 53  ? 160.837 152.950 163.517 1.00 59.32 ?  53  GLU B CA    1 
ATOM   5963  C  C     . GLU B 1 53  ? 159.827 152.026 162.852 1.00 57.39 ?  53  GLU B C     1 
ATOM   5964  O  O     . GLU B 1 53  ? 159.802 151.907 161.623 1.00 59.82 ?  53  GLU B O     1 
ATOM   5965  C  CB    . GLU B 1 53  ? 162.060 152.162 163.985 1.00 59.95 ?  53  GLU B CB    1 
ATOM   5966  C  CG    . GLU B 1 53  ? 163.038 152.971 164.812 1.00 60.72 ?  53  GLU B CG    1 
ATOM   5967  C  CD    . GLU B 1 53  ? 164.482 152.660 164.475 1.00 62.00 ?  53  GLU B CD    1 
ATOM   5968  O  OE1   . GLU B 1 53  ? 164.901 151.498 164.663 1.00 62.82 ?  53  GLU B OE1   1 
ATOM   5969  O  OE2   . GLU B 1 53  ? 165.197 153.577 164.019 1.00 61.66 -1 53  GLU B OE2   1 
ATOM   5970  N  N     . LYS B 1 54  ? 158.984 151.365 163.647 1.00 54.54 ?  54  LYS B N     1 
ATOM   5971  C  CA    . LYS B 1 54  ? 157.963 150.489 163.083 1.00 54.20 ?  54  LYS B CA    1 
ATOM   5972  C  C     . LYS B 1 54  ? 156.995 151.270 162.204 1.00 52.54 ?  54  LYS B C     1 
ATOM   5973  O  O     . LYS B 1 54  ? 156.697 150.864 161.074 1.00 52.90 ?  54  LYS B O     1 
ATOM   5974  C  CB    . LYS B 1 54  ? 157.210 149.776 164.205 1.00 53.29 ?  54  LYS B CB    1 
ATOM   5975  C  CG    . LYS B 1 54  ? 155.994 149.002 163.733 1.00 54.25 ?  54  LYS B CG    1 
ATOM   5976  C  CD    . LYS B 1 54  ? 155.613 147.926 164.725 1.00 53.22 ?  54  LYS B CD    1 
ATOM   5977  C  CE    . LYS B 1 54  ? 154.429 147.118 164.236 1.00 53.86 ?  54  LYS B CE    1 
ATOM   5978  N  NZ    . LYS B 1 54  ? 154.393 145.766 164.857 1.00 54.25 1  54  LYS B NZ    1 
ATOM   5979  N  N     . LEU B 1 55  ? 156.497 152.399 162.711 1.00 52.77 ?  55  LEU B N     1 
ATOM   5980  C  CA    . LEU B 1 55  ? 155.554 153.201 161.939 1.00 53.11 ?  55  LEU B CA    1 
ATOM   5981  C  C     . LEU B 1 55  ? 156.203 153.758 160.681 1.00 56.57 ?  55  LEU B C     1 
ATOM   5982  O  O     . LEU B 1 55  ? 155.584 153.765 159.611 1.00 60.90 ?  55  LEU B O     1 
ATOM   5983  C  CB    . LEU B 1 55  ? 154.993 154.329 162.802 1.00 55.67 ?  55  LEU B CB    1 
ATOM   5984  C  CG    . LEU B 1 55  ? 153.827 153.959 163.720 1.00 55.50 ?  55  LEU B CG    1 
ATOM   5985  C  CD1   . LEU B 1 55  ? 153.022 155.199 164.051 1.00 56.44 ?  55  LEU B CD1   1 
ATOM   5986  C  CD2   . LEU B 1 55  ? 152.942 152.897 163.084 1.00 54.78 ?  55  LEU B CD2   1 
ATOM   5987  N  N     . ASP B 1 56  ? 157.450 154.227 160.782 1.00 56.68 ?  56  ASP B N     1 
ATOM   5988  C  CA    . ASP B 1 56  ? 158.137 154.742 159.603 1.00 56.24 ?  56  ASP B CA    1 
ATOM   5989  C  C     . ASP B 1 56  ? 158.338 153.648 158.561 1.00 57.03 ?  56  ASP B C     1 
ATOM   5990  O  O     . ASP B 1 56  ? 158.104 153.868 157.368 1.00 57.75 ?  56  ASP B O     1 
ATOM   5991  C  CB    . ASP B 1 56  ? 159.477 155.357 160.004 1.00 59.58 ?  56  ASP B CB    1 
ATOM   5992  C  CG    . ASP B 1 56  ? 159.316 156.567 160.903 1.00 60.61 ?  56  ASP B CG    1 
ATOM   5993  O  OD1   . ASP B 1 56  ? 158.168 157.016 161.098 1.00 61.48 ?  56  ASP B OD1   1 
ATOM   5994  O  OD2   . ASP B 1 56  ? 160.338 157.067 161.416 1.00 59.36 -1 56  ASP B OD2   1 
ATOM   5995  N  N     . TYR B 1 57  ? 158.760 152.457 158.994 1.00 55.74 ?  57  TYR B N     1 
ATOM   5996  C  CA    . TYR B 1 57  ? 158.962 151.359 158.057 1.00 56.06 ?  57  TYR B CA    1 
ATOM   5997  C  C     . TYR B 1 57  ? 157.654 150.965 157.387 1.00 56.30 ?  57  TYR B C     1 
ATOM   5998  O  O     . TYR B 1 57  ? 157.624 150.690 156.183 1.00 60.11 ?  57  TYR B O     1 
ATOM   5999  C  CB    . TYR B 1 57  ? 159.582 150.161 158.780 1.00 55.53 ?  57  TYR B CB    1 
ATOM   6000  C  CG    . TYR B 1 57  ? 159.653 148.898 157.949 1.00 56.81 ?  57  TYR B CG    1 
ATOM   6001  C  CD1   . TYR B 1 57  ? 160.733 148.659 157.110 1.00 57.13 ?  57  TYR B CD1   1 
ATOM   6002  C  CD2   . TYR B 1 57  ? 158.648 147.940 158.010 1.00 59.01 ?  57  TYR B CD2   1 
ATOM   6003  C  CE1   . TYR B 1 57  ? 160.806 147.508 156.349 1.00 57.09 ?  57  TYR B CE1   1 
ATOM   6004  C  CE2   . TYR B 1 57  ? 158.713 146.788 157.253 1.00 59.36 ?  57  TYR B CE2   1 
ATOM   6005  C  CZ    . TYR B 1 57  ? 159.794 146.575 156.426 1.00 59.35 ?  57  TYR B CZ    1 
ATOM   6006  O  OH    . TYR B 1 57  ? 159.862 145.426 155.670 1.00 59.74 ?  57  TYR B OH    1 
ATOM   6007  N  N     . LEU B 1 58  ? 156.559 150.932 158.149 1.00 53.38 ?  58  LEU B N     1 
ATOM   6008  C  CA    . LEU B 1 58  ? 155.275 150.565 157.564 1.00 52.61 ?  58  LEU B CA    1 
ATOM   6009  C  C     . LEU B 1 58  ? 154.729 151.663 156.658 1.00 51.55 ?  58  LEU B C     1 
ATOM   6010  O  O     . LEU B 1 58  ? 153.947 151.376 155.746 1.00 53.00 ?  58  LEU B O     1 
ATOM   6011  C  CB    . LEU B 1 58  ? 154.276 150.229 158.671 1.00 52.55 ?  58  LEU B CB    1 
ATOM   6012  C  CG    . LEU B 1 58  ? 154.617 148.973 159.476 1.00 52.17 ?  58  LEU B CG    1 
ATOM   6013  C  CD1   . LEU B 1 58  ? 153.846 148.932 160.783 1.00 52.11 ?  58  LEU B CD1   1 
ATOM   6014  C  CD2   . LEU B 1 58  ? 154.354 147.720 158.657 1.00 53.03 ?  58  LEU B CD2   1 
ATOM   6015  N  N     . VAL B 1 59  ? 155.125 152.914 156.885 1.00 55.47 ?  59  VAL B N     1 
ATOM   6016  C  CA    . VAL B 1 59  ? 154.615 154.007 156.065 1.00 56.82 ?  59  VAL B CA    1 
ATOM   6017  C  C     . VAL B 1 59  ? 155.383 154.106 154.751 1.00 57.98 ?  59  VAL B C     1 
ATOM   6018  O  O     . VAL B 1 59  ? 154.783 154.172 153.672 1.00 56.51 ?  59  VAL B O     1 
ATOM   6019  C  CB    . VAL B 1 59  ? 154.660 155.330 156.852 1.00 56.13 ?  59  VAL B CB    1 
ATOM   6020  C  CG1   . VAL B 1 59  ? 154.709 156.519 155.904 1.00 55.82 ?  59  VAL B CG1   1 
ATOM   6021  C  CG2   . VAL B 1 59  ? 153.460 155.432 157.779 1.00 55.43 ?  59  VAL B CG2   1 
ATOM   6022  N  N     . GLU B 1 60  ? 156.719 154.115 154.814 1.00 59.74 ?  60  GLU B N     1 
ATOM   6023  C  CA    . GLU B 1 60  ? 157.502 154.274 153.591 1.00 59.69 ?  60  GLU B CA    1 
ATOM   6024  C  C     . GLU B 1 60  ? 157.425 153.044 152.695 1.00 59.71 ?  60  GLU B C     1 
ATOM   6025  O  O     . GLU B 1 60  ? 157.527 153.171 151.469 1.00 61.21 ?  60  GLU B O     1 
ATOM   6026  C  CB    . GLU B 1 60  ? 158.961 154.599 153.914 1.00 59.21 ?  60  GLU B CB    1 
ATOM   6027  C  CG    . GLU B 1 60  ? 159.161 155.580 155.055 1.00 60.66 ?  60  GLU B CG    1 
ATOM   6028  C  CD    . GLU B 1 60  ? 160.363 155.235 155.912 1.00 62.93 ?  60  GLU B CD    1 
ATOM   6029  O  OE1   . GLU B 1 60  ? 160.785 156.090 156.719 1.00 59.92 ?  60  GLU B OE1   1 
ATOM   6030  O  OE2   . GLU B 1 60  ? 160.888 154.109 155.779 1.00 61.95 -1 60  GLU B OE2   1 
ATOM   6031  N  N     . ASN B 1 61  ? 157.254 151.856 153.271 1.00 55.81 ?  61  ASN B N     1 
ATOM   6032  C  CA    . ASN B 1 61  ? 157.165 150.628 152.494 1.00 56.10 ?  61  ASN B CA    1 
ATOM   6033  C  C     . ASN B 1 61  ? 155.757 150.360 151.977 1.00 56.29 ?  61  ASN B C     1 
ATOM   6034  O  O     . ASN B 1 61  ? 155.457 149.228 151.579 1.00 58.43 ?  61  ASN B O     1 
ATOM   6035  C  CB    . ASN B 1 61  ? 157.659 149.440 153.321 1.00 56.83 ?  61  ASN B CB    1 
ATOM   6036  C  CG    . ASN B 1 61  ? 159.162 149.452 153.514 1.00 58.89 ?  61  ASN B CG    1 
ATOM   6037  O  OD1   . ASN B 1 61  ? 159.898 148.792 152.782 1.00 58.92 ?  61  ASN B OD1   1 
ATOM   6038  N  ND2   . ASN B 1 61  ? 159.625 150.212 154.499 1.00 58.89 ?  61  ASN B ND2   1 
ATOM   6039  N  N     . GLN B 1 62  ? 154.893 151.378 151.976 1.00 55.77 ?  62  GLN B N     1 
ATOM   6040  C  CA    . GLN B 1 62  ? 153.543 151.290 151.415 1.00 57.06 ?  62  GLN B CA    1 
ATOM   6041  C  C     . GLN B 1 62  ? 152.721 150.190 152.083 1.00 55.48 ?  62  GLN B C     1 
ATOM   6042  O  O     . GLN B 1 62  ? 151.922 149.508 151.439 1.00 56.00 ?  62  GLN B O     1 
ATOM   6043  C  CB    . GLN B 1 62  ? 153.587 151.091 149.898 1.00 54.59 ?  62  GLN B CB    1 
ATOM   6044  C  CG    . GLN B 1 62  ? 154.515 152.054 149.173 1.00 55.59 ?  62  GLN B CG    1 
ATOM   6045  C  CD    . GLN B 1 62  ? 154.320 153.494 149.606 1.00 58.59 ?  62  GLN B CD    1 
ATOM   6046  O  OE1   . GLN B 1 62  ? 153.297 154.111 149.307 1.00 58.31 ?  62  GLN B OE1   1 
ATOM   6047  N  NE2   . GLN B 1 62  ? 155.303 154.038 150.312 1.00 57.60 ?  62  GLN B NE2   1 
ATOM   6048  N  N     . TYR B 1 63  ? 152.918 150.013 153.389 1.00 52.92 ?  63  TYR B N     1 
ATOM   6049  C  CA    . TYR B 1 63  ? 152.055 149.140 154.174 1.00 52.23 ?  63  TYR B CA    1 
ATOM   6050  C  C     . TYR B 1 63  ? 150.891 149.903 154.787 1.00 52.08 ?  63  TYR B C     1 
ATOM   6051  O  O     . TYR B 1 63  ? 149.772 149.384 154.851 1.00 51.06 ?  63  TYR B O     1 
ATOM   6052  C  CB    . TYR B 1 63  ? 152.853 148.449 155.283 1.00 51.41 ?  63  TYR B CB    1 
ATOM   6053  C  CG    . TYR B 1 63  ? 153.790 147.369 154.799 1.00 53.74 ?  63  TYR B CG    1 
ATOM   6054  C  CD1   . TYR B 1 63  ? 153.302 146.226 154.182 1.00 51.61 ?  63  TYR B CD1   1 
ATOM   6055  C  CD2   . TYR B 1 63  ? 155.161 147.489 154.970 1.00 53.83 ?  63  TYR B CD2   1 
ATOM   6056  C  CE1   . TYR B 1 63  ? 154.156 145.235 153.742 1.00 54.06 ?  63  TYR B CE1   1 
ATOM   6057  C  CE2   . TYR B 1 63  ? 156.022 146.505 154.534 1.00 52.91 ?  63  TYR B CE2   1 
ATOM   6058  C  CZ    . TYR B 1 63  ? 155.517 145.381 153.921 1.00 55.02 ?  63  TYR B CZ    1 
ATOM   6059  O  OH    . TYR B 1 63  ? 156.376 144.400 153.485 1.00 55.71 ?  63  TYR B OH    1 
ATOM   6060  N  N     . TYR B 1 64  ? 151.138 151.130 155.236 1.00 49.23 ?  64  TYR B N     1 
ATOM   6061  C  CA    . TYR B 1 64  ? 150.139 151.954 155.896 1.00 46.99 ?  64  TYR B CA    1 
ATOM   6062  C  C     . TYR B 1 64  ? 149.892 153.225 155.098 1.00 48.94 ?  64  TYR B C     1 
ATOM   6063  O  O     . TYR B 1 64  ? 150.800 153.763 154.458 1.00 50.62 ?  64  TYR B O     1 
ATOM   6064  C  CB    . TYR B 1 64  ? 150.579 152.335 157.312 1.00 47.69 ?  64  TYR B CB    1 
ATOM   6065  C  CG    . TYR B 1 64  ? 150.415 151.242 158.337 1.00 47.26 ?  64  TYR B CG    1 
ATOM   6066  C  CD1   . TYR B 1 64  ? 149.826 150.030 158.006 1.00 47.65 ?  64  TYR B CD1   1 
ATOM   6067  C  CD2   . TYR B 1 64  ? 150.855 151.425 159.639 1.00 47.78 ?  64  TYR B CD2   1 
ATOM   6068  C  CE1   . TYR B 1 64  ? 149.678 149.032 158.946 1.00 45.62 ?  64  TYR B CE1   1 
ATOM   6069  C  CE2   . TYR B 1 64  ? 150.712 150.435 160.581 1.00 48.04 ?  64  TYR B CE2   1 
ATOM   6070  C  CZ    . TYR B 1 64  ? 150.125 149.241 160.232 1.00 47.45 ?  64  TYR B CZ    1 
ATOM   6071  O  OH    . TYR B 1 64  ? 149.987 148.258 161.180 1.00 49.14 ?  64  TYR B OH    1 
ATOM   6072  N  N     . GLU B 1 65  ? 148.652 153.699 155.139 1.00 51.99 ?  65  GLU B N     1 
ATOM   6073  C  CA    . GLU B 1 65  ? 148.351 155.034 154.645 1.00 51.96 ?  65  GLU B CA    1 
ATOM   6074  C  C     . GLU B 1 65  ? 148.860 156.065 155.643 1.00 54.39 ?  65  GLU B C     1 
ATOM   6075  O  O     . GLU B 1 65  ? 148.605 155.957 156.846 1.00 55.86 ?  65  GLU B O     1 
ATOM   6076  C  CB    . GLU B 1 65  ? 146.849 155.196 154.423 1.00 50.39 ?  65  GLU B CB    1 
ATOM   6077  C  CG    . GLU B 1 65  ? 146.246 154.160 153.489 1.00 51.97 ?  65  GLU B CG    1 
ATOM   6078  C  CD    . GLU B 1 65  ? 144.741 154.291 153.366 1.00 55.50 ?  65  GLU B CD    1 
ATOM   6079  O  OE1   . GLU B 1 65  ? 144.094 154.689 154.357 1.00 54.42 ?  65  GLU B OE1   1 
ATOM   6080  O  OE2   . GLU B 1 65  ? 144.205 153.997 152.277 1.00 54.21 -1 65  GLU B OE2   1 
ATOM   6081  N  N     . GLU B 1 66  ? 149.593 157.061 155.149 1.00 52.84 ?  66  GLU B N     1 
ATOM   6082  C  CA    . GLU B 1 66  ? 150.171 158.060 156.038 1.00 54.72 ?  66  GLU B CA    1 
ATOM   6083  C  C     . GLU B 1 66  ? 149.173 159.136 156.444 1.00 54.99 ?  66  GLU B C     1 
ATOM   6084  O  O     . GLU B 1 66  ? 149.427 159.860 157.414 1.00 54.13 ?  66  GLU B O     1 
ATOM   6085  C  CB    . GLU B 1 66  ? 151.391 158.707 155.378 1.00 55.88 ?  66  GLU B CB    1 
ATOM   6086  C  CG    . GLU B 1 66  ? 151.059 159.813 154.394 1.00 55.41 ?  66  GLU B CG    1 
ATOM   6087  C  CD    . GLU B 1 66  ? 152.262 160.670 154.058 1.00 56.78 ?  66  GLU B CD    1 
ATOM   6088  O  OE1   . GLU B 1 66  ? 153.375 160.114 153.947 1.00 55.65 ?  66  GLU B OE1   1 
ATOM   6089  O  OE2   . GLU B 1 66  ? 152.096 161.898 153.905 1.00 56.59 -1 66  GLU B OE2   1 
ATOM   6090  N  N     . GLU B 1 67  ? 148.045 159.247 155.741 1.00 53.83 ?  67  GLU B N     1 
ATOM   6091  C  CA    . GLU B 1 67  ? 147.097 160.321 156.023 1.00 53.55 ?  67  GLU B CA    1 
ATOM   6092  C  C     . GLU B 1 67  ? 146.437 160.138 157.385 1.00 55.20 ?  67  GLU B C     1 
ATOM   6093  O  O     . GLU B 1 67  ? 146.348 161.087 158.171 1.00 55.05 ?  67  GLU B O     1 
ATOM   6094  C  CB    . GLU B 1 67  ? 146.038 160.407 154.919 1.00 54.00 ?  67  GLU B CB    1 
ATOM   6095  C  CG    . GLU B 1 67  ? 146.572 160.487 153.485 1.00 55.13 ?  67  GLU B CG    1 
ATOM   6096  C  CD    . GLU B 1 67  ? 147.139 159.175 152.974 1.00 58.09 ?  67  GLU B CD    1 
ATOM   6097  O  OE1   . GLU B 1 67  ? 148.309 159.162 152.538 1.00 57.11 ?  67  GLU B OE1   1 
ATOM   6098  O  OE2   . GLU B 1 67  ? 146.414 158.159 153.007 1.00 56.98 -1 67  GLU B OE2   1 
ATOM   6099  N  N     . PHE B 1 68  ? 145.964 158.925 157.682 1.00 50.07 ?  68  PHE B N     1 
ATOM   6100  C  CA    . PHE B 1 68  ? 145.271 158.708 158.948 1.00 46.19 ?  68  PHE B CA    1 
ATOM   6101  C  C     . PHE B 1 68  ? 146.230 158.768 160.130 1.00 46.50 ?  68  PHE B C     1 
ATOM   6102  O  O     . PHE B 1 68  ? 145.832 159.180 161.226 1.00 50.04 ?  68  PHE B O     1 
ATOM   6103  C  CB    . PHE B 1 68  ? 144.512 157.378 158.918 1.00 47.47 ?  68  PHE B CB    1 
ATOM   6104  C  CG    . PHE B 1 68  ? 145.292 156.207 159.447 1.00 47.17 ?  68  PHE B CG    1 
ATOM   6105  C  CD1   . PHE B 1 68  ? 146.165 155.514 158.630 1.00 45.17 ?  68  PHE B CD1   1 
ATOM   6106  C  CD2   . PHE B 1 68  ? 145.127 155.783 160.755 1.00 43.14 ?  68  PHE B CD2   1 
ATOM   6107  C  CE1   . PHE B 1 68  ? 146.877 154.435 159.112 1.00 44.22 ?  68  PHE B CE1   1 
ATOM   6108  C  CE2   . PHE B 1 68  ? 145.835 154.704 161.242 1.00 42.72 ?  68  PHE B CE2   1 
ATOM   6109  C  CZ    . PHE B 1 68  ? 146.709 154.027 160.418 1.00 44.93 ?  68  PHE B CZ    1 
ATOM   6110  N  N     . LEU B 1 69  ? 147.486 158.366 159.934 1.00 49.73 ?  69  LEU B N     1 
ATOM   6111  C  CA    . LEU B 1 69  ? 148.485 158.490 160.987 1.00 47.63 ?  69  LEU B CA    1 
ATOM   6112  C  C     . LEU B 1 69  ? 148.981 159.919 161.157 1.00 48.62 ?  69  LEU B C     1 
ATOM   6113  O  O     . LEU B 1 69  ? 149.475 160.263 162.236 1.00 52.37 ?  69  LEU B O     1 
ATOM   6114  C  CB    . LEU B 1 69  ? 149.672 157.568 160.703 1.00 47.53 ?  69  LEU B CB    1 
ATOM   6115  C  CG    . LEU B 1 69  ? 149.485 156.088 161.040 1.00 47.12 ?  69  LEU B CG    1 
ATOM   6116  C  CD1   . LEU B 1 69  ? 150.647 155.264 160.507 1.00 48.48 ?  69  LEU B CD1   1 
ATOM   6117  C  CD2   . LEU B 1 69  ? 149.325 155.891 162.538 1.00 47.04 ?  69  LEU B CD2   1 
ATOM   6118  N  N     . SER B 1 70  ? 148.863 160.754 160.122 1.00 48.36 ?  70  SER B N     1 
ATOM   6119  C  CA    . SER B 1 70  ? 149.332 162.131 160.221 1.00 47.28 ?  70  SER B CA    1 
ATOM   6120  C  C     . SER B 1 70  ? 148.407 163.004 161.060 1.00 49.11 ?  70  SER B C     1 
ATOM   6121  O  O     . SER B 1 70  ? 148.811 164.100 161.463 1.00 51.02 ?  70  SER B O     1 
ATOM   6122  C  CB    . SER B 1 70  ? 149.487 162.734 158.824 1.00 49.35 ?  70  SER B CB    1 
ATOM   6123  O  OG    . SER B 1 70  ? 148.232 163.117 158.291 1.00 49.06 ?  70  SER B OG    1 
ATOM   6124  N  N     . LEU B 1 71  ? 147.183 162.551 161.329 1.00 46.46 ?  71  LEU B N     1 
ATOM   6125  C  CA    . LEU B 1 71  ? 146.258 163.316 162.155 1.00 45.72 ?  71  LEU B CA    1 
ATOM   6126  C  C     . LEU B 1 71  ? 146.614 163.278 163.633 1.00 45.67 ?  71  LEU B C     1 
ATOM   6127  O  O     . LEU B 1 71  ? 146.035 164.043 164.412 1.00 46.85 ?  71  LEU B O     1 
ATOM   6128  C  CB    . LEU B 1 71  ? 144.828 162.804 161.963 1.00 44.59 ?  71  LEU B CB    1 
ATOM   6129  C  CG    . LEU B 1 71  ? 144.287 162.806 160.534 1.00 47.01 ?  71  LEU B CG    1 
ATOM   6130  C  CD1   . LEU B 1 71  ? 143.425 161.580 160.291 1.00 49.18 ?  71  LEU B CD1   1 
ATOM   6131  C  CD2   . LEU B 1 71  ? 143.503 164.078 160.262 1.00 45.72 ?  71  LEU B CD2   1 
ATOM   6132  N  N     . TYR B 1 72  ? 147.541 162.415 164.036 1.00 43.56 ?  72  TYR B N     1 
ATOM   6133  C  CA    . TYR B 1 72  ? 147.978 162.305 165.419 1.00 44.85 ?  72  TYR B CA    1 
ATOM   6134  C  C     . TYR B 1 72  ? 149.463 162.620 165.513 1.00 46.70 ?  72  TYR B C     1 
ATOM   6135  O  O     . TYR B 1 72  ? 150.245 162.236 164.637 1.00 48.51 ?  72  TYR B O     1 
ATOM   6136  C  CB    . TYR B 1 72  ? 147.737 160.901 165.987 1.00 45.55 ?  72  TYR B CB    1 
ATOM   6137  C  CG    . TYR B 1 72  ? 146.369 160.318 165.726 1.00 42.98 ?  72  TYR B CG    1 
ATOM   6138  C  CD1   . TYR B 1 72  ? 146.077 159.692 164.521 1.00 42.35 ?  72  TYR B CD1   1 
ATOM   6139  C  CD2   . TYR B 1 72  ? 145.379 160.366 166.695 1.00 42.77 ?  72  TYR B CD2   1 
ATOM   6140  C  CE1   . TYR B 1 72  ? 144.833 159.150 164.283 1.00 40.87 ?  72  TYR B CE1   1 
ATOM   6141  C  CE2   . TYR B 1 72  ? 144.131 159.825 166.468 1.00 42.72 ?  72  TYR B CE2   1 
ATOM   6142  C  CZ    . TYR B 1 72  ? 143.864 159.219 165.259 1.00 42.62 ?  72  TYR B CZ    1 
ATOM   6143  O  OH    . TYR B 1 72  ? 142.623 158.678 165.024 1.00 45.08 ?  72  TYR B OH    1 
ATOM   6144  N  N     . SER B 1 73  ? 149.847 163.318 166.577 1.00 52.19 ?  73  SER B N     1 
ATOM   6145  C  CA    . SER B 1 73  ? 151.255 163.397 166.930 1.00 52.49 ?  73  SER B CA    1 
ATOM   6146  C  C     . SER B 1 73  ? 151.740 162.021 167.368 1.00 51.86 ?  73  SER B C     1 
ATOM   6147  O  O     . SER B 1 73  ? 150.960 161.185 167.829 1.00 54.01 ?  73  SER B O     1 
ATOM   6148  C  CB    . SER B 1 73  ? 151.475 164.420 168.043 1.00 51.38 ?  73  SER B CB    1 
ATOM   6149  O  OG    . SER B 1 73  ? 151.102 163.890 169.303 1.00 50.60 ?  73  SER B OG    1 
ATOM   6150  N  N     . PHE B 1 74  ? 153.044 161.780 167.205 1.00 54.68 ?  74  PHE B N     1 
ATOM   6151  C  CA    . PHE B 1 74  ? 153.571 160.457 167.525 1.00 53.82 ?  74  PHE B CA    1 
ATOM   6152  C  C     . PHE B 1 74  ? 153.388 160.114 168.997 1.00 54.02 ?  74  PHE B C     1 
ATOM   6153  O  O     . PHE B 1 74  ? 153.289 158.933 169.347 1.00 55.52 ?  74  PHE B O     1 
ATOM   6154  C  CB    . PHE B 1 74  ? 155.047 160.347 167.148 1.00 54.59 ?  74  PHE B CB    1 
ATOM   6155  C  CG    . PHE B 1 74  ? 155.678 159.060 167.594 1.00 55.45 ?  74  PHE B CG    1 
ATOM   6156  C  CD1   . PHE B 1 74  ? 155.330 157.863 166.992 1.00 53.33 ?  74  PHE B CD1   1 
ATOM   6157  C  CD2   . PHE B 1 74  ? 156.594 159.042 168.631 1.00 55.41 ?  74  PHE B CD2   1 
ATOM   6158  C  CE1   . PHE B 1 74  ? 155.893 156.673 167.405 1.00 55.48 ?  74  PHE B CE1   1 
ATOM   6159  C  CE2   . PHE B 1 74  ? 157.162 157.854 169.049 1.00 55.10 ?  74  PHE B CE2   1 
ATOM   6160  C  CZ    . PHE B 1 74  ? 156.812 156.669 168.436 1.00 55.55 ?  74  PHE B CZ    1 
ATOM   6161  N  N     . GLU B 1 75  ? 153.341 161.121 169.871 1.00 54.99 ?  75  GLU B N     1 
ATOM   6162  C  CA    . GLU B 1 75  ? 153.072 160.851 171.280 1.00 56.01 ?  75  GLU B CA    1 
ATOM   6163  C  C     . GLU B 1 75  ? 151.687 160.242 171.463 1.00 56.55 ?  75  GLU B C     1 
ATOM   6164  O  O     . GLU B 1 75  ? 151.510 159.309 172.253 1.00 57.06 ?  75  GLU B O     1 
ATOM   6165  C  CB    . GLU B 1 75  ? 153.211 162.135 172.099 1.00 56.12 ?  75  GLU B CB    1 
ATOM   6166  C  CG    . GLU B 1 75  ? 154.604 162.373 172.663 1.00 56.08 ?  75  GLU B CG    1 
ATOM   6167  C  CD    . GLU B 1 75  ? 155.704 162.046 171.672 1.00 59.46 ?  75  GLU B CD    1 
ATOM   6168  O  OE1   . GLU B 1 75  ? 155.869 162.804 170.693 1.00 59.31 ?  75  GLU B OE1   1 
ATOM   6169  O  OE2   . GLU B 1 75  ? 156.406 161.032 171.874 1.00 59.07 -1 75  GLU B OE2   1 
ATOM   6170  N  N     . ASP B 1 76  ? 150.696 160.753 170.731 1.00 52.52 ?  76  ASP B N     1 
ATOM   6171  C  CA    . ASP B 1 76  ? 149.344 160.211 170.823 1.00 51.01 ?  76  ASP B CA    1 
ATOM   6172  C  C     . ASP B 1 76  ? 149.277 158.783 170.293 1.00 49.96 ?  76  ASP B C     1 
ATOM   6173  O  O     . ASP B 1 76  ? 148.604 157.928 170.880 1.00 53.31 ?  76  ASP B O     1 
ATOM   6174  C  CB    . ASP B 1 76  ? 148.374 161.116 170.068 1.00 52.34 ?  76  ASP B CB    1 
ATOM   6175  C  CG    . ASP B 1 76  ? 148.148 162.437 170.775 1.00 54.36 ?  76  ASP B CG    1 
ATOM   6176  O  OD1   . ASP B 1 76  ? 148.604 162.579 171.928 1.00 53.96 ?  76  ASP B OD1   1 
ATOM   6177  O  OD2   . ASP B 1 76  ? 147.513 163.332 170.177 1.00 53.46 -1 76  ASP B OD2   1 
ATOM   6178  N  N     . ILE B 1 77  ? 149.963 158.506 169.182 1.00 47.36 ?  77  ILE B N     1 
ATOM   6179  C  CA    . ILE B 1 77  ? 149.989 157.148 168.643 1.00 47.58 ?  77  ILE B CA    1 
ATOM   6180  C  C     . ILE B 1 77  ? 150.677 156.202 169.616 1.00 48.60 ?  77  ILE B C     1 
ATOM   6181  O  O     . ILE B 1 77  ? 150.242 155.059 169.812 1.00 50.21 ?  77  ILE B O     1 
ATOM   6182  C  CB    . ILE B 1 77  ? 150.673 157.132 167.264 1.00 49.12 ?  77  ILE B CB    1 
ATOM   6183  C  CG1   . ILE B 1 77  ? 149.953 158.075 166.301 1.00 48.20 ?  77  ILE B CG1   1 
ATOM   6184  C  CG2   . ILE B 1 77  ? 150.698 155.723 166.704 1.00 46.74 ?  77  ILE B CG2   1 
ATOM   6185  C  CD1   . ILE B 1 77  ? 150.718 158.344 165.027 1.00 45.94 ?  77  ILE B CD1   1 
ATOM   6186  N  N     . LYS B 1 78  ? 151.772 156.656 170.230 1.00 50.55 ?  78  LYS B N     1 
ATOM   6187  C  CA    . LYS B 1 78  ? 152.451 155.853 171.238 1.00 50.70 ?  78  LYS B CA    1 
ATOM   6188  C  C     . LYS B 1 78  ? 151.535 155.572 172.419 1.00 49.63 ?  78  LYS B C     1 
ATOM   6189  O  O     . LYS B 1 78  ? 151.515 154.455 172.944 1.00 50.68 ?  78  LYS B O     1 
ATOM   6190  C  CB    . LYS B 1 78  ? 153.721 156.565 171.706 1.00 53.57 ?  78  LYS B CB    1 
ATOM   6191  C  CG    . LYS B 1 78  ? 154.782 155.645 172.280 1.00 52.73 ?  78  LYS B CG    1 
ATOM   6192  C  CD    . LYS B 1 78  ? 155.663 156.390 173.270 1.00 53.81 ?  78  LYS B CD    1 
ATOM   6193  C  CE    . LYS B 1 78  ? 156.970 155.659 173.514 1.00 54.50 ?  78  LYS B CE    1 
ATOM   6194  N  NZ    . LYS B 1 78  ? 158.136 156.414 172.978 1.00 52.68 1  78  LYS B NZ    1 
ATOM   6195  N  N     . GLU B 1 79  ? 150.767 156.575 172.850 1.00 51.71 ?  79  GLU B N     1 
ATOM   6196  C  CA    . GLU B 1 79  ? 149.832 156.376 173.952 1.00 51.17 ?  79  GLU B CA    1 
ATOM   6197  C  C     . GLU B 1 79  ? 148.744 155.376 173.578 1.00 49.54 ?  79  GLU B C     1 
ATOM   6198  O  O     . GLU B 1 79  ? 148.349 154.542 174.400 1.00 51.83 ?  79  GLU B O     1 
ATOM   6199  C  CB    . GLU B 1 79  ? 149.224 157.718 174.360 1.00 49.44 ?  79  GLU B CB    1 
ATOM   6200  C  CG    . GLU B 1 79  ? 149.859 158.324 175.602 1.00 52.62 ?  79  GLU B CG    1 
ATOM   6201  C  CD    . GLU B 1 79  ? 148.952 159.316 176.300 1.00 56.12 ?  79  GLU B CD    1 
ATOM   6202  O  OE1   . GLU B 1 79  ? 149.310 159.773 177.406 1.00 54.05 ?  79  GLU B OE1   1 
ATOM   6203  O  OE2   . GLU B 1 79  ? 147.890 159.652 175.738 1.00 56.75 -1 79  GLU B OE2   1 
ATOM   6204  N  N     . VAL B 1 80  ? 148.254 155.438 172.339 1.00 43.97 ?  80  VAL B N     1 
ATOM   6205  C  CA    . VAL B 1 80  ? 147.241 154.488 171.884 1.00 41.94 ?  80  VAL B CA    1 
ATOM   6206  C  C     . VAL B 1 80  ? 147.801 153.068 171.863 1.00 46.28 ?  80  VAL B C     1 
ATOM   6207  O  O     . VAL B 1 80  ? 147.149 152.119 172.317 1.00 48.04 ?  80  VAL B O     1 
ATOM   6208  C  CB    . VAL B 1 80  ? 146.707 154.914 170.504 1.00 43.34 ?  80  VAL B CB    1 
ATOM   6209  C  CG1   . VAL B 1 80  ? 145.930 153.784 169.853 1.00 44.32 ?  80  VAL B CG1   1 
ATOM   6210  C  CG2   . VAL B 1 80  ? 145.840 156.154 170.634 1.00 44.52 ?  80  VAL B CG2   1 
ATOM   6211  N  N     . PHE B 1 81  ? 149.018 152.900 171.339 1.00 46.65 ?  81  PHE B N     1 
ATOM   6212  C  CA    . PHE B 1 81  ? 149.631 151.575 171.304 1.00 43.06 ?  81  PHE B CA    1 
ATOM   6213  C  C     . PHE B 1 81  ? 149.906 151.054 172.711 1.00 45.86 ?  81  PHE B C     1 
ATOM   6214  O  O     . PHE B 1 81  ? 149.746 149.857 172.982 1.00 48.13 ?  81  PHE B O     1 
ATOM   6215  C  CB    . PHE B 1 81  ? 150.918 151.615 170.481 1.00 40.92 ?  81  PHE B CB    1 
ATOM   6216  C  CG    . PHE B 1 81  ? 150.713 151.339 169.019 1.00 40.82 ?  81  PHE B CG    1 
ATOM   6217  C  CD1   . PHE B 1 81  ? 150.288 152.344 168.165 1.00 41.95 ?  81  PHE B CD1   1 
ATOM   6218  C  CD2   . PHE B 1 81  ? 150.943 150.079 168.498 1.00 42.08 ?  81  PHE B CD2   1 
ATOM   6219  C  CE1   . PHE B 1 81  ? 150.099 152.094 166.819 1.00 43.36 ?  81  PHE B CE1   1 
ATOM   6220  C  CE2   . PHE B 1 81  ? 150.755 149.825 167.153 1.00 42.11 ?  81  PHE B CE2   1 
ATOM   6221  C  CZ    . PHE B 1 81  ? 150.333 150.834 166.313 1.00 41.06 ?  81  PHE B CZ    1 
ATOM   6222  N  N     . LYS B 1 82  ? 150.330 151.937 173.617 1.00 47.33 ?  82  LYS B N     1 
ATOM   6223  C  CA    . LYS B 1 82  ? 150.546 151.536 175.002 1.00 46.06 ?  82  LYS B CA    1 
ATOM   6224  C  C     . LYS B 1 82  ? 149.238 151.127 175.665 1.00 44.98 ?  82  LYS B C     1 
ATOM   6225  O  O     . LYS B 1 82  ? 149.207 150.182 176.458 1.00 46.57 ?  82  LYS B O     1 
ATOM   6226  C  CB    . LYS B 1 82  ? 151.213 152.670 175.781 1.00 46.55 ?  82  LYS B CB    1 
ATOM   6227  C  CG    . LYS B 1 82  ? 152.687 152.853 175.469 1.00 47.41 ?  82  LYS B CG    1 
ATOM   6228  C  CD    . LYS B 1 82  ? 153.558 152.248 176.556 1.00 47.76 ?  82  LYS B CD    1 
ATOM   6229  C  CE    . LYS B 1 82  ? 153.227 152.838 177.917 1.00 49.18 ?  82  LYS B CE    1 
ATOM   6230  N  NZ    . LYS B 1 82  ? 153.800 154.202 178.084 1.00 48.24 1  82  LYS B NZ    1 
ATOM   6231  N  N     . THR B 1 83  ? 148.147 151.831 175.356 1.00 42.72 ?  83  THR B N     1 
ATOM   6232  C  CA    . THR B 1 83  ? 146.842 151.429 175.867 1.00 41.20 ?  83  THR B CA    1 
ATOM   6233  C  C     . THR B 1 83  ? 146.450 150.056 175.338 1.00 42.79 ?  83  THR B C     1 
ATOM   6234  O  O     . THR B 1 83  ? 145.881 149.237 176.068 1.00 45.00 ?  83  THR B O     1 
ATOM   6235  C  CB    . THR B 1 83  ? 145.788 152.471 175.491 1.00 41.20 ?  83  THR B CB    1 
ATOM   6236  O  OG1   . THR B 1 83  ? 146.167 153.746 176.024 1.00 46.81 ?  83  THR B OG1   1 
ATOM   6237  C  CG2   . THR B 1 83  ? 144.429 152.085 176.051 1.00 44.21 ?  83  THR B CG2   1 
ATOM   6238  N  N     . ALA B 1 84  ? 146.748 149.789 174.064 1.00 41.52 ?  84  ALA B N     1 
ATOM   6239  C  CA    . ALA B 1 84  ? 146.448 148.478 173.495 1.00 38.00 ?  84  ALA B CA    1 
ATOM   6240  C  C     . ALA B 1 84  ? 147.251 147.376 174.175 1.00 38.28 ?  84  ALA B C     1 
ATOM   6241  O  O     . ALA B 1 84  ? 146.716 146.302 174.473 1.00 43.99 ?  84  ALA B O     1 
ATOM   6242  C  CB    . ALA B 1 84  ? 146.714 148.483 171.992 1.00 39.60 ?  84  ALA B CB    1 
ATOM   6243  N  N     . TYR B 1 85  ? 148.536 147.621 174.422 1.00 45.05 ?  85  TYR B N     1 
ATOM   6244  C  CA    . TYR B 1 85  ? 149.396 146.604 175.020 1.00 43.36 ?  85  TYR B CA    1 
ATOM   6245  C  C     . TYR B 1 85  ? 149.260 146.507 176.535 1.00 44.29 ?  85  TYR B C     1 
ATOM   6246  O  O     . TYR B 1 85  ? 149.741 145.529 177.116 1.00 46.49 ?  85  TYR B O     1 
ATOM   6247  C  CB    . TYR B 1 85  ? 150.856 146.871 174.651 1.00 40.26 ?  85  TYR B CB    1 
ATOM   6248  C  CG    . TYR B 1 85  ? 151.238 146.363 173.280 1.00 41.59 ?  85  TYR B CG    1 
ATOM   6249  C  CD1   . TYR B 1 85  ? 151.691 145.064 173.105 1.00 43.79 ?  85  TYR B CD1   1 
ATOM   6250  C  CD2   . TYR B 1 85  ? 151.138 147.178 172.161 1.00 43.92 ?  85  TYR B CD2   1 
ATOM   6251  C  CE1   . TYR B 1 85  ? 152.040 144.591 171.858 1.00 44.17 ?  85  TYR B CE1   1 
ATOM   6252  C  CE2   . TYR B 1 85  ? 151.484 146.714 170.909 1.00 43.73 ?  85  TYR B CE2   1 
ATOM   6253  C  CZ    . TYR B 1 85  ? 151.935 145.420 170.763 1.00 43.21 ?  85  TYR B CZ    1 
ATOM   6254  O  OH    . TYR B 1 85  ? 152.281 144.951 169.519 1.00 45.29 ?  85  TYR B OH    1 
ATOM   6255  N  N     . ALA B 1 86  ? 148.624 147.483 177.185 1.00 43.66 ?  86  ALA B N     1 
ATOM   6256  C  CA    . ALA B 1 86  ? 148.477 147.429 178.635 1.00 42.01 ?  86  ALA B CA    1 
ATOM   6257  C  C     . ALA B 1 86  ? 147.500 146.346 179.067 1.00 45.48 ?  86  ALA B C     1 
ATOM   6258  O  O     . ALA B 1 86  ? 147.584 145.855 180.197 1.00 47.31 ?  86  ALA B O     1 
ATOM   6259  C  CB    . ALA B 1 86  ? 148.029 148.789 179.168 1.00 42.20 ?  86  ALA B CB    1 
ATOM   6260  N  N     . LYS B 1 87  ? 146.567 145.967 178.192 1.00 44.46 ?  87  LYS B N     1 
ATOM   6261  C  CA    . LYS B 1 87  ? 145.606 144.929 178.538 1.00 45.39 ?  87  LYS B CA    1 
ATOM   6262  C  C     . LYS B 1 87  ? 146.252 143.554 178.654 1.00 44.55 ?  87  LYS B C     1 
ATOM   6263  O  O     . LYS B 1 87  ? 145.672 142.669 179.293 1.00 46.37 ?  87  LYS B O     1 
ATOM   6264  C  CB    . LYS B 1 87  ? 144.482 144.886 177.502 1.00 43.93 ?  87  LYS B CB    1 
ATOM   6265  C  CG    . LYS B 1 87  ? 143.133 144.480 178.069 1.00 43.92 ?  87  LYS B CG    1 
ATOM   6266  C  CD    . LYS B 1 87  ? 142.594 143.240 177.377 1.00 44.50 ?  87  LYS B CD    1 
ATOM   6267  C  CE    . LYS B 1 87  ? 141.477 142.600 178.187 1.00 42.38 ?  87  LYS B CE    1 
ATOM   6268  N  NZ    . LYS B 1 87  ? 140.815 141.491 177.447 1.00 40.62 1  87  LYS B NZ    1 
ATOM   6269  N  N     . LYS B 1 88  ? 147.436 143.366 178.069 1.00 44.68 ?  88  LYS B N     1 
ATOM   6270  C  CA    . LYS B 1 88  ? 148.111 142.069 178.040 1.00 44.57 ?  88  LYS B CA    1 
ATOM   6271  C  C     . LYS B 1 88  ? 147.183 140.989 177.493 1.00 42.41 ?  88  LYS B C     1 
ATOM   6272  O  O     . LYS B 1 88  ? 147.016 139.917 178.079 1.00 43.90 ?  88  LYS B O     1 
ATOM   6273  C  CB    . LYS B 1 88  ? 148.643 141.688 179.423 1.00 45.79 ?  88  LYS B CB    1 
ATOM   6274  C  CG    . LYS B 1 88  ? 150.020 142.244 179.747 1.00 46.36 ?  88  LYS B CG    1 
ATOM   6275  C  CD    . LYS B 1 88  ? 149.940 143.641 180.335 1.00 45.95 ?  88  LYS B CD    1 
ATOM   6276  C  CE    . LYS B 1 88  ? 151.198 144.440 180.029 1.00 46.97 ?  88  LYS B CE    1 
ATOM   6277  N  NZ    . LYS B 1 88  ? 150.996 145.902 180.223 1.00 47.47 1  88  LYS B NZ    1 
ATOM   6278  N  N     . PHE B 1 89  ? 146.559 141.290 176.355 1.00 42.94 ?  89  PHE B N     1 
ATOM   6279  C  CA    . PHE B 1 89  ? 145.590 140.373 175.770 1.00 39.07 ?  89  PHE B CA    1 
ATOM   6280  C  C     . PHE B 1 89  ? 146.256 139.059 175.390 1.00 43.73 ?  89  PHE B C     1 
ATOM   6281  O  O     . PHE B 1 89  ? 147.321 139.041 174.766 1.00 46.25 ?  89  PHE B O     1 
ATOM   6282  C  CB    . PHE B 1 89  ? 144.933 141.004 174.541 1.00 37.31 ?  89  PHE B CB    1 
ATOM   6283  C  CG    . PHE B 1 89  ? 144.020 140.068 173.801 1.00 38.71 ?  89  PHE B CG    1 
ATOM   6284  C  CD1   . PHE B 1 89  ? 142.702 139.915 174.191 1.00 37.31 ?  89  PHE B CD1   1 
ATOM   6285  C  CD2   . PHE B 1 89  ? 144.482 139.335 172.720 1.00 38.40 ?  89  PHE B CD2   1 
ATOM   6286  C  CE1   . PHE B 1 89  ? 141.862 139.052 173.517 1.00 37.73 ?  89  PHE B CE1   1 
ATOM   6287  C  CE2   . PHE B 1 89  ? 143.645 138.469 172.044 1.00 34.60 ?  89  PHE B CE2   1 
ATOM   6288  C  CZ    . PHE B 1 89  ? 142.334 138.329 172.442 1.00 36.67 ?  89  PHE B CZ    1 
ATOM   6289  N  N     . ARG B 1 90  ? 145.618 137.956 175.766 1.00 42.62 ?  90  ARG B N     1 
ATOM   6290  C  CA    . ARG B 1 90  ? 146.085 136.618 175.440 1.00 40.51 ?  90  ARG B CA    1 
ATOM   6291  C  C     . ARG B 1 90  ? 144.983 135.878 174.698 1.00 41.89 ?  90  ARG B C     1 
ATOM   6292  O  O     . ARG B 1 90  ? 143.820 135.912 175.114 1.00 42.84 ?  90  ARG B O     1 
ATOM   6293  C  CB    . ARG B 1 90  ? 146.483 135.850 176.702 1.00 45.34 ?  90  ARG B CB    1 
ATOM   6294  C  CG    . ARG B 1 90  ? 147.609 136.494 177.492 1.00 42.68 ?  90  ARG B CG    1 
ATOM   6295  C  CD    . ARG B 1 90  ? 148.924 136.419 176.738 1.00 45.15 ?  90  ARG B CD    1 
ATOM   6296  N  NE    . ARG B 1 90  ? 149.952 137.250 177.354 1.00 45.79 ?  90  ARG B NE    1 
ATOM   6297  C  CZ    . ARG B 1 90  ? 150.345 138.424 176.882 1.00 44.67 ?  90  ARG B CZ    1 
ATOM   6298  N  NH1   . ARG B 1 90  ? 149.823 138.936 175.780 1.00 46.68 1  90  ARG B NH1   1 
ATOM   6299  N  NH2   . ARG B 1 90  ? 151.287 139.102 177.532 1.00 44.05 ?  90  ARG B NH2   1 
ATOM   6300  N  N     . PHE B 1 91  ? 145.346 135.224 173.608 1.00 39.25 ?  91  PHE B N     1 
ATOM   6301  C  CA    . PHE B 1 91  ? 144.392 134.401 172.881 1.00 38.08 ?  91  PHE B CA    1 
ATOM   6302  C  C     . PHE B 1 91  ? 144.112 133.140 173.688 1.00 43.46 ?  91  PHE B C     1 
ATOM   6303  O  O     . PHE B 1 91  ? 145.047 132.379 173.971 1.00 45.50 ?  91  PHE B O     1 
ATOM   6304  C  CB    . PHE B 1 91  ? 144.935 134.048 171.502 1.00 38.01 ?  91  PHE B CB    1 
ATOM   6305  C  CG    . PHE B 1 91  ? 144.872 135.181 170.518 1.00 39.78 ?  91  PHE B CG    1 
ATOM   6306  C  CD1   . PHE B 1 91  ? 143.680 135.518 169.901 1.00 40.90 ?  91  PHE B CD1   1 
ATOM   6307  C  CD2   . PHE B 1 91  ? 146.008 135.911 170.210 1.00 39.02 ?  91  PHE B CD2   1 
ATOM   6308  C  CE1   . PHE B 1 91  ? 143.622 136.559 168.996 1.00 39.44 ?  91  PHE B CE1   1 
ATOM   6309  C  CE2   . PHE B 1 91  ? 145.955 136.951 169.306 1.00 39.13 ?  91  PHE B CE2   1 
ATOM   6310  C  CZ    . PHE B 1 91  ? 144.759 137.276 168.699 1.00 39.68 ?  91  PHE B CZ    1 
ATOM   6311  N  N     . PRO B 1 92  ? 142.862 132.874 174.077 1.00 42.41 ?  92  PRO B N     1 
ATOM   6312  C  CA    . PRO B 1 92  ? 142.594 131.702 174.922 1.00 42.17 ?  92  PRO B CA    1 
ATOM   6313  C  C     . PRO B 1 92  ? 142.635 130.385 174.173 1.00 42.72 ?  92  PRO B C     1 
ATOM   6314  O  O     . PRO B 1 92  ? 142.727 129.331 174.817 1.00 43.37 ?  92  PRO B O     1 
ATOM   6315  C  CB    . PRO B 1 92  ? 141.189 131.983 175.468 1.00 41.94 ?  92  PRO B CB    1 
ATOM   6316  C  CG    . PRO B 1 92  ? 140.543 132.785 174.394 1.00 41.93 ?  92  PRO B CG    1 
ATOM   6317  C  CD    . PRO B 1 92  ? 141.631 133.619 173.758 1.00 40.90 ?  92  PRO B CD    1 
ATOM   6318  N  N     . SER B 1 93  ? 142.571 130.407 172.845 1.00 42.05 ?  93  SER B N     1 
ATOM   6319  C  CA    . SER B 1 93  ? 142.597 129.199 172.038 1.00 39.78 ?  93  SER B CA    1 
ATOM   6320  C  C     . SER B 1 93  ? 143.627 129.356 170.931 1.00 40.03 ?  93  SER B C     1 
ATOM   6321  O  O     . SER B 1 93  ? 143.918 130.469 170.485 1.00 44.07 ?  93  SER B O     1 
ATOM   6322  C  CB    . SER B 1 93  ? 141.218 128.897 171.435 1.00 42.98 ?  93  SER B CB    1 
ATOM   6323  O  OG    . SER B 1 93  ? 141.020 129.611 170.228 1.00 44.75 ?  93  SER B OG    1 
ATOM   6324  N  N     . PHE B 1 94  ? 144.188 128.224 170.501 1.00 40.58 ?  94  PHE B N     1 
ATOM   6325  C  CA    . PHE B 1 94  ? 145.181 128.254 169.433 1.00 41.09 ?  94  PHE B CA    1 
ATOM   6326  C  C     . PHE B 1 94  ? 144.577 128.767 168.134 1.00 41.10 ?  94  PHE B C     1 
ATOM   6327  O  O     . PHE B 1 94  ? 145.222 129.520 167.396 1.00 43.52 ?  94  PHE B O     1 
ATOM   6328  C  CB    . PHE B 1 94  ? 145.781 126.862 169.231 1.00 42.58 ?  94  PHE B CB    1 
ATOM   6329  C  CG    . PHE B 1 94  ? 146.343 126.641 167.856 1.00 39.39 ?  94  PHE B CG    1 
ATOM   6330  C  CD1   . PHE B 1 94  ? 147.502 127.282 167.455 1.00 41.36 ?  94  PHE B CD1   1 
ATOM   6331  C  CD2   . PHE B 1 94  ? 145.707 125.798 166.959 1.00 41.92 ?  94  PHE B CD2   1 
ATOM   6332  C  CE1   . PHE B 1 94  ? 148.018 127.087 166.190 1.00 41.54 ?  94  PHE B CE1   1 
ATOM   6333  C  CE2   . PHE B 1 94  ? 146.219 125.598 165.693 1.00 44.46 ?  94  PHE B CE2   1 
ATOM   6334  C  CZ    . PHE B 1 94  ? 147.376 126.243 165.308 1.00 41.24 ?  94  PHE B CZ    1 
ATOM   6335  N  N     . MET B 1 95  ? 143.340 128.365 167.835 1.00 38.90 ?  95  MET B N     1 
ATOM   6336  C  CA    . MET B 1 95  ? 142.735 128.725 166.559 1.00 36.29 ?  95  MET B CA    1 
ATOM   6337  C  C     . MET B 1 95  ? 142.472 130.221 166.451 1.00 38.72 ?  95  MET B C     1 
ATOM   6338  O  O     . MET B 1 95  ? 142.541 130.772 165.351 1.00 44.00 ?  95  MET B O     1 
ATOM   6339  C  CB    . MET B 1 95  ? 141.443 127.936 166.347 1.00 39.90 ?  95  MET B CB    1 
ATOM   6340  C  CG    . MET B 1 95  ? 140.753 128.200 165.015 1.00 42.25 ?  95  MET B CG    1 
ATOM   6341  S  SD    . MET B 1 95  ? 141.412 127.296 163.595 1.00 51.03 ?  95  MET B SD    1 
ATOM   6342  C  CE    . MET B 1 95  ? 142.404 126.027 164.379 1.00 43.73 ?  95  MET B CE    1 
ATOM   6343  N  N     . SER B 1 96  ? 142.184 130.896 167.565 1.00 33.31 ?  96  SER B N     1 
ATOM   6344  C  CA    . SER B 1 96  ? 141.987 132.343 167.516 1.00 30.40 ?  96  SER B CA    1 
ATOM   6345  C  C     . SER B 1 96  ? 143.241 133.049 167.015 1.00 32.32 ?  96  SER B C     1 
ATOM   6346  O  O     . SER B 1 96  ? 143.196 133.830 166.053 1.00 34.21 ?  96  SER B O     1 
ATOM   6347  C  CB    . SER B 1 96  ? 141.598 132.857 168.901 1.00 33.47 ?  96  SER B CB    1 
ATOM   6348  O  OG    . SER B 1 96  ? 140.504 132.128 169.427 1.00 38.67 ?  96  SER B OG    1 
ATOM   6349  N  N     . ALA B 1 97  ? 144.380 132.764 167.650 1.00 37.86 ?  97  ALA B N     1 
ATOM   6350  C  CA    . ALA B 1 97  ? 145.639 133.371 167.239 1.00 34.01 ?  97  ALA B CA    1 
ATOM   6351  C  C     . ALA B 1 97  ? 146.030 132.932 165.837 1.00 35.07 ?  97  ALA B C     1 
ATOM   6352  O  O     . ALA B 1 97  ? 146.531 133.737 165.045 1.00 42.03 ?  97  ALA B O     1 
ATOM   6353  C  CB    . ALA B 1 97  ? 146.738 133.018 168.239 1.00 36.35 ?  97  ALA B CB    1 
ATOM   6354  N  N     . PHE B 1 98  ? 145.821 131.654 165.516 1.00 33.42 ?  98  PHE B N     1 
ATOM   6355  C  CA    . PHE B 1 98  ? 146.166 131.161 164.187 1.00 32.89 ?  98  PHE B CA    1 
ATOM   6356  C  C     . PHE B 1 98  ? 145.370 131.889 163.114 1.00 35.95 ?  98  PHE B C     1 
ATOM   6357  O  O     . PHE B 1 98  ? 145.926 132.328 162.101 1.00 43.40 ?  98  PHE B O     1 
ATOM   6358  C  CB    . PHE B 1 98  ? 145.925 129.653 164.112 1.00 37.17 ?  98  PHE B CB    1 
ATOM   6359  C  CG    . PHE B 1 98  ? 146.136 129.073 162.744 1.00 39.18 ?  98  PHE B CG    1 
ATOM   6360  C  CD1   . PHE B 1 98  ? 147.408 128.744 162.308 1.00 39.78 ?  98  PHE B CD1   1 
ATOM   6361  C  CD2   . PHE B 1 98  ? 145.065 128.857 161.893 1.00 41.11 ?  98  PHE B CD2   1 
ATOM   6362  C  CE1   . PHE B 1 98  ? 147.607 128.212 161.052 1.00 37.68 ?  98  PHE B CE1   1 
ATOM   6363  C  CE2   . PHE B 1 98  ? 145.259 128.326 160.634 1.00 43.04 ?  98  PHE B CE2   1 
ATOM   6364  C  CZ    . PHE B 1 98  ? 146.532 128.002 160.213 1.00 40.72 ?  98  PHE B CZ    1 
ATOM   6365  N  N     . LYS B 1 99  ? 144.063 132.043 163.329 1.00 39.14 ?  99  LYS B N     1 
ATOM   6366  C  CA    . LYS B 1 99  ? 143.217 132.719 162.356 1.00 37.77 ?  99  LYS B CA    1 
ATOM   6367  C  C     . LYS B 1 99  ? 143.598 134.183 162.220 1.00 35.59 ?  99  LYS B C     1 
ATOM   6368  O  O     . LYS B 1 99  ? 143.636 134.714 161.104 1.00 41.58 ?  99  LYS B O     1 
ATOM   6369  C  CB    . LYS B 1 99  ? 141.747 132.578 162.749 1.00 36.70 ?  99  LYS B CB    1 
ATOM   6370  C  CG    . LYS B 1 99  ? 141.126 131.253 162.343 1.00 39.01 ?  99  LYS B CG    1 
ATOM   6371  C  CD    . LYS B 1 99  ? 141.453 130.907 160.902 1.00 42.01 ?  99  LYS B CD    1 
ATOM   6372  C  CE    . LYS B 1 99  ? 140.332 130.113 160.258 1.00 40.21 ?  99  LYS B CE    1 
ATOM   6373  N  NZ    . LYS B 1 99  ? 140.106 130.527 158.846 1.00 42.41 1  99  LYS B NZ    1 
ATOM   6374  N  N     . PHE B 1 100 ? 143.891 134.857 163.337 1.00 32.10 ?  100 PHE B N     1 
ATOM   6375  C  CA    . PHE B 1 100 ? 144.305 136.252 163.231 1.00 35.03 ?  100 PHE B CA    1 
ATOM   6376  C  C     . PHE B 1 100 ? 145.610 136.387 162.457 1.00 35.92 ?  100 PHE B C     1 
ATOM   6377  O  O     . PHE B 1 100 ? 145.716 137.203 161.534 1.00 41.09 ?  100 PHE B O     1 
ATOM   6378  C  CB    . PHE B 1 100 ? 144.459 136.894 164.605 1.00 33.33 ?  100 PHE B CB    1 
ATOM   6379  C  CG    . PHE B 1 100 ? 145.065 138.262 164.536 1.00 35.46 ?  100 PHE B CG    1 
ATOM   6380  C  CD1   . PHE B 1 100 ? 144.347 139.320 164.005 1.00 34.60 ?  100 PHE B CD1   1 
ATOM   6381  C  CD2   . PHE B 1 100 ? 146.369 138.478 164.937 1.00 34.53 ?  100 PHE B CD2   1 
ATOM   6382  C  CE1   . PHE B 1 100 ? 144.905 140.576 163.913 1.00 34.60 ?  100 PHE B CE1   1 
ATOM   6383  C  CE2   . PHE B 1 100 ? 146.934 139.731 164.843 1.00 35.28 ?  100 PHE B CE2   1 
ATOM   6384  C  CZ    . PHE B 1 100 ? 146.200 140.782 164.331 1.00 34.72 ?  100 PHE B CZ    1 
ATOM   6385  N  N     . TYR B 1 101 ? 146.617 135.593 162.816 1.00 36.51 ?  101 TYR B N     1 
ATOM   6386  C  CA    . TYR B 1 101 ? 147.937 135.752 162.222 1.00 35.32 ?  101 TYR B CA    1 
ATOM   6387  C  C     . TYR B 1 101 ? 148.044 135.138 160.835 1.00 37.20 ?  101 TYR B C     1 
ATOM   6388  O  O     . TYR B 1 101 ? 149.056 135.351 160.160 1.00 45.47 ?  101 TYR B O     1 
ATOM   6389  C  CB    . TYR B 1 101 ? 149.001 135.162 163.150 1.00 38.28 ?  101 TYR B CB    1 
ATOM   6390  C  CG    . TYR B 1 101 ? 149.260 136.025 164.365 1.00 37.54 ?  101 TYR B CG    1 
ATOM   6391  C  CD1   . TYR B 1 101 ? 149.920 137.240 164.248 1.00 36.80 ?  101 TYR B CD1   1 
ATOM   6392  C  CD2   . TYR B 1 101 ? 148.828 135.635 165.624 1.00 36.97 ?  101 TYR B CD2   1 
ATOM   6393  C  CE1   . TYR B 1 101 ? 150.151 138.037 165.351 1.00 36.63 ?  101 TYR B CE1   1 
ATOM   6394  C  CE2   . TYR B 1 101 ? 149.053 136.425 166.733 1.00 38.05 ?  101 TYR B CE2   1 
ATOM   6395  C  CZ    . TYR B 1 101 ? 149.715 137.625 166.591 1.00 39.59 ?  101 TYR B CZ    1 
ATOM   6396  O  OH    . TYR B 1 101 ? 149.942 138.414 167.694 1.00 42.17 ?  101 TYR B OH    1 
ATOM   6397  N  N     . ASN B 1 102 ? 147.034 134.392 160.390 1.00 40.40 ?  102 ASN B N     1 
ATOM   6398  C  CA    . ASN B 1 102 ? 147.012 133.882 159.028 1.00 41.86 ?  102 ASN B CA    1 
ATOM   6399  C  C     . ASN B 1 102 ? 146.105 134.676 158.101 1.00 43.32 ?  102 ASN B C     1 
ATOM   6400  O  O     . ASN B 1 102 ? 146.375 134.740 156.898 1.00 47.54 ?  102 ASN B O     1 
ATOM   6401  C  CB    . ASN B 1 102 ? 146.573 132.415 159.022 1.00 40.01 ?  102 ASN B CB    1 
ATOM   6402  C  CG    . ASN B 1 102 ? 147.682 131.472 159.440 1.00 43.14 ?  102 ASN B CG    1 
ATOM   6403  O  OD1   . ASN B 1 102 ? 148.297 131.647 160.492 1.00 45.88 ?  102 ASN B OD1   1 
ATOM   6404  N  ND2   . ASN B 1 102 ? 147.945 130.465 158.616 1.00 43.81 ?  102 ASN B ND2   1 
ATOM   6405  N  N     . ASP B 1 103 ? 145.039 135.286 158.625 1.00 38.59 ?  103 ASP B N     1 
ATOM   6406  C  CA    . ASP B 1 103 ? 144.074 135.992 157.794 1.00 40.61 ?  103 ASP B CA    1 
ATOM   6407  C  C     . ASP B 1 103 ? 144.070 137.500 157.984 1.00 40.98 ?  103 ASP B C     1 
ATOM   6408  O  O     . ASP B 1 103 ? 143.701 138.218 157.053 1.00 46.47 ?  103 ASP B O     1 
ATOM   6409  C  CB    . ASP B 1 103 ? 142.655 135.470 158.059 1.00 42.23 ?  103 ASP B CB    1 
ATOM   6410  C  CG    . ASP B 1 103 ? 142.573 133.955 158.050 1.00 45.37 ?  103 ASP B CG    1 
ATOM   6411  O  OD1   . ASP B 1 103 ? 143.499 133.305 157.521 1.00 44.78 ?  103 ASP B OD1   1 
ATOM   6412  O  OD2   . ASP B 1 103 ? 141.576 133.415 158.571 1.00 47.06 -1 103 ASP B OD2   1 
ATOM   6413  N  N     . TYR B 1 104 ? 144.461 138.004 159.155 1.00 31.95 ?  104 TYR B N     1 
ATOM   6414  C  CA    . TYR B 1 104 ? 144.292 139.421 159.457 1.00 35.66 ?  104 TYR B CA    1 
ATOM   6415  C  C     . TYR B 1 104 ? 145.563 140.147 159.870 1.00 38.78 ?  104 TYR B C     1 
ATOM   6416  O  O     . TYR B 1 104 ? 145.629 141.368 159.684 1.00 43.88 ?  104 TYR B O     1 
ATOM   6417  C  CB    . TYR B 1 104 ? 143.234 139.612 160.554 1.00 37.44 ?  104 TYR B CB    1 
ATOM   6418  C  CG    . TYR B 1 104 ? 141.923 138.934 160.235 1.00 36.15 ?  104 TYR B CG    1 
ATOM   6419  C  CD1   . TYR B 1 104 ? 140.942 139.589 159.501 1.00 34.65 ?  104 TYR B CD1   1 
ATOM   6420  C  CD2   . TYR B 1 104 ? 141.663 137.640 160.666 1.00 33.99 ?  104 TYR B CD2   1 
ATOM   6421  C  CE1   . TYR B 1 104 ? 139.745 138.971 159.199 1.00 36.14 ?  104 TYR B CE1   1 
ATOM   6422  C  CE2   . TYR B 1 104 ? 140.467 137.015 160.371 1.00 37.33 ?  104 TYR B CE2   1 
ATOM   6423  C  CZ    . TYR B 1 104 ? 139.512 137.685 159.636 1.00 38.90 ?  104 TYR B CZ    1 
ATOM   6424  O  OH    . TYR B 1 104 ? 138.319 137.066 159.343 1.00 38.34 ?  104 TYR B OH    1 
ATOM   6425  N  N     . ALA B 1 105 ? 146.560 139.464 160.424 1.00 40.73 ?  105 ALA B N     1 
ATOM   6426  C  CA    . ALA B 1 105 ? 147.803 140.133 160.778 1.00 40.00 ?  105 ALA B CA    1 
ATOM   6427  C  C     . ALA B 1 105 ? 148.561 140.541 159.521 1.00 43.61 ?  105 ALA B C     1 
ATOM   6428  O  O     . ALA B 1 105 ? 148.647 139.780 158.553 1.00 40.70 ?  105 ALA B O     1 
ATOM   6429  C  CB    . ALA B 1 105 ? 148.673 139.231 161.645 1.00 37.04 ?  105 ALA B CB    1 
ATOM   6430  N  N     . LEU B 1 106 ? 149.110 141.752 159.540 1.00 46.91 ?  106 LEU B N     1 
ATOM   6431  C  CA    . LEU B 1 106 ? 149.851 142.252 158.391 1.00 44.23 ?  106 LEU B CA    1 
ATOM   6432  C  C     . LEU B 1 106 ? 151.200 141.552 158.288 1.00 47.83 ?  106 LEU B C     1 
ATOM   6433  O  O     . LEU B 1 106 ? 151.948 141.470 159.266 1.00 46.99 ?  106 LEU B O     1 
ATOM   6434  C  CB    . LEU B 1 106 ? 150.044 143.763 158.498 1.00 46.87 ?  106 LEU B CB    1 
ATOM   6435  C  CG    . LEU B 1 106 ? 150.878 144.424 157.400 1.00 45.27 ?  106 LEU B CG    1 
ATOM   6436  C  CD1   . LEU B 1 106 ? 150.120 144.428 156.083 1.00 45.59 ?  106 LEU B CD1   1 
ATOM   6437  C  CD2   . LEU B 1 106 ? 151.266 145.836 157.802 1.00 46.37 ?  106 LEU B CD2   1 
ATOM   6438  N  N     . LYS B 1 107 ? 151.505 141.046 157.098 1.00 53.13 ?  107 LYS B N     1 
ATOM   6439  C  CA    . LYS B 1 107 ? 152.766 140.384 156.813 1.00 52.70 ?  107 LYS B CA    1 
ATOM   6440  C  C     . LYS B 1 107 ? 153.548 141.196 155.790 1.00 55.30 ?  107 LYS B C     1 
ATOM   6441  O  O     . LYS B 1 107 ? 153.052 142.173 155.223 1.00 56.79 ?  107 LYS B O     1 
ATOM   6442  C  CB    . LYS B 1 107 ? 152.541 138.956 156.302 1.00 52.84 ?  107 LYS B CB    1 
ATOM   6443  C  CG    . LYS B 1 107 ? 151.976 138.001 157.340 1.00 51.33 ?  107 LYS B CG    1 
ATOM   6444  C  CD    . LYS B 1 107 ? 151.700 136.636 156.732 1.00 54.71 ?  107 LYS B CD    1 
ATOM   6445  C  CE    . LYS B 1 107 ? 151.171 135.664 157.771 1.00 55.56 ?  107 LYS B CE    1 
ATOM   6446  N  NZ    . LYS B 1 107 ? 150.653 134.412 157.151 1.00 52.71 1  107 LYS B NZ    1 
ATOM   6447  N  N     . THR B 1 108 ? 154.789 140.777 155.556 1.00 59.23 ?  108 THR B N     1 
ATOM   6448  C  CA    . THR B 1 108 ? 155.643 141.452 154.593 1.00 59.39 ?  108 THR B CA    1 
ATOM   6449  C  C     . THR B 1 108 ? 155.156 141.172 153.172 1.00 61.88 ?  108 THR B C     1 
ATOM   6450  O  O     . THR B 1 108 ? 154.189 140.440 152.944 1.00 61.58 ?  108 THR B O     1 
ATOM   6451  C  CB    . THR B 1 108 ? 157.094 141.011 154.771 1.00 60.99 ?  108 THR B CB    1 
ATOM   6452  O  OG1   . THR B 1 108 ? 157.142 139.594 154.982 1.00 65.24 ?  108 THR B OG1   1 
ATOM   6453  C  CG2   . THR B 1 108 ? 157.719 141.714 155.966 1.00 58.11 ?  108 THR B CG2   1 
ATOM   6454  N  N     . ASN B 1 109 ? 155.840 141.778 152.197 1.00 63.97 ?  109 ASN B N     1 
ATOM   6455  C  CA    . ASN B 1 109 ? 155.468 141.581 150.799 1.00 61.95 ?  109 ASN B CA    1 
ATOM   6456  C  C     . ASN B 1 109 ? 155.608 140.121 150.390 1.00 64.82 ?  109 ASN B C     1 
ATOM   6457  O  O     . ASN B 1 109 ? 154.757 139.583 149.672 1.00 64.81 ?  109 ASN B O     1 
ATOM   6458  C  CB    . ASN B 1 109 ? 156.320 142.475 149.898 1.00 63.18 ?  109 ASN B CB    1 
ATOM   6459  C  CG    . ASN B 1 109 ? 156.160 143.946 150.219 1.00 63.25 ?  109 ASN B CG    1 
ATOM   6460  O  OD1   . ASN B 1 109 ? 155.280 144.333 150.985 1.00 61.63 ?  109 ASN B OD1   1 
ATOM   6461  N  ND2   . ASN B 1 109 ? 157.013 144.776 149.631 1.00 64.76 ?  109 ASN B ND2   1 
ATOM   6462  N  N     . ASP B 1 110 ? 156.676 139.462 150.836 1.00 66.37 ?  110 ASP B N     1 
ATOM   6463  C  CA    . ASP B 1 110 ? 156.882 138.047 150.556 1.00 66.12 ?  110 ASP B CA    1 
ATOM   6464  C  C     . ASP B 1 110 ? 156.168 137.137 151.548 1.00 66.70 ?  110 ASP B C     1 
ATOM   6465  O  O     . ASP B 1 110 ? 156.255 135.912 151.408 1.00 67.58 ?  110 ASP B O     1 
ATOM   6466  C  CB    . ASP B 1 110 ? 158.380 137.730 150.541 1.00 66.14 ?  110 ASP B CB    1 
ATOM   6467  C  CG    . ASP B 1 110 ? 159.089 138.204 151.793 1.00 67.51 ?  110 ASP B CG    1 
ATOM   6468  O  OD1   . ASP B 1 110 ? 158.475 138.952 152.581 1.00 67.34 ?  110 ASP B OD1   1 
ATOM   6469  O  OD2   . ASP B 1 110 ? 160.266 137.834 151.985 1.00 67.65 -1 110 ASP B OD2   1 
ATOM   6470  N  N     . LYS B 1 111 ? 155.472 137.708 152.535 1.00 62.24 ?  111 LYS B N     1 
ATOM   6471  C  CA    . LYS B 1 111 ? 154.706 136.945 153.523 1.00 63.06 ?  111 LYS B CA    1 
ATOM   6472  C  C     . LYS B 1 111 ? 155.586 135.940 154.264 1.00 64.05 ?  111 LYS B C     1 
ATOM   6473  O  O     . LYS B 1 111 ? 155.178 134.808 154.529 1.00 65.21 ?  111 LYS B O     1 
ATOM   6474  C  CB    . LYS B 1 111 ? 153.507 136.245 152.878 1.00 63.14 ?  111 LYS B CB    1 
ATOM   6475  C  CG    . LYS B 1 111 ? 152.768 137.087 151.848 1.00 63.13 ?  111 LYS B CG    1 
ATOM   6476  C  CD    . LYS B 1 111 ? 151.703 137.953 152.499 1.00 64.53 ?  111 LYS B CD    1 
ATOM   6477  C  CE    . LYS B 1 111 ? 151.420 139.196 151.673 1.00 64.19 ?  111 LYS B CE    1 
ATOM   6478  N  NZ    . LYS B 1 111 ? 151.498 138.920 150.212 1.00 63.59 1  111 LYS B NZ    1 
ATOM   6479  N  N     . LYS B 1 112 ? 156.806 136.357 154.603 1.00 64.60 ?  112 LYS B N     1 
ATOM   6480  C  CA    . LYS B 1 112 ? 157.714 135.518 155.372 1.00 64.95 ?  112 LYS B CA    1 
ATOM   6481  C  C     . LYS B 1 112 ? 157.783 135.901 156.842 1.00 64.12 ?  112 LYS B C     1 
ATOM   6482  O  O     . LYS B 1 112 ? 158.256 135.097 157.653 1.00 64.02 ?  112 LYS B O     1 
ATOM   6483  C  CB    . LYS B 1 112 ? 159.126 135.573 154.778 1.00 64.38 ?  112 LYS B CB    1 
ATOM   6484  C  CG    . LYS B 1 112 ? 159.917 136.809 155.175 1.00 65.17 ?  112 LYS B CG    1 
ATOM   6485  C  CD    . LYS B 1 112 ? 161.372 136.698 154.753 1.00 66.05 ?  112 LYS B CD    1 
ATOM   6486  C  CE    . LYS B 1 112 ? 162.138 137.969 155.084 1.00 64.52 ?  112 LYS B CE    1 
ATOM   6487  N  NZ    . LYS B 1 112 ? 161.300 139.186 154.896 1.00 64.63 1  112 LYS B NZ    1 
ATOM   6488  N  N     . LYS B 1 113 ? 157.327 137.098 157.204 1.00 59.57 ?  113 LYS B N     1 
ATOM   6489  C  CA    . LYS B 1 113 ? 157.411 137.579 158.574 1.00 59.62 ?  113 LYS B CA    1 
ATOM   6490  C  C     . LYS B 1 113 ? 156.117 138.293 158.934 1.00 57.88 ?  113 LYS B C     1 
ATOM   6491  O  O     . LYS B 1 113 ? 155.330 138.673 158.064 1.00 60.09 ?  113 LYS B O     1 
ATOM   6492  C  CB    . LYS B 1 113 ? 158.610 138.518 158.769 1.00 60.10 ?  113 LYS B CB    1 
ATOM   6493  C  CG    . LYS B 1 113 ? 159.962 137.821 158.740 1.00 58.77 ?  113 LYS B CG    1 
ATOM   6494  C  CD    . LYS B 1 113 ? 160.122 136.873 159.915 1.00 60.69 ?  113 LYS B CD    1 
ATOM   6495  C  CE    . LYS B 1 113 ? 161.480 136.195 159.898 1.00 61.41 ?  113 LYS B CE    1 
ATOM   6496  N  NZ    . LYS B 1 113 ? 161.571 135.114 160.917 1.00 60.18 1  113 LYS B NZ    1 
ATOM   6497  N  N     . ILE B 1 114 ? 155.907 138.472 160.234 1.00 52.57 ?  114 ILE B N     1 
ATOM   6498  C  CA    . ILE B 1 114 ? 154.704 139.101 160.766 1.00 52.15 ?  114 ILE B CA    1 
ATOM   6499  C  C     . ILE B 1 114 ? 155.064 140.510 161.209 1.00 53.20 ?  114 ILE B C     1 
ATOM   6500  O  O     . ILE B 1 114 ? 155.924 140.696 162.080 1.00 54.37 ?  114 ILE B O     1 
ATOM   6501  C  CB    . ILE B 1 114 ? 154.110 138.292 161.930 1.00 53.28 ?  114 ILE B CB    1 
ATOM   6502  C  CG1   . ILE B 1 114 ? 153.466 137.006 161.411 1.00 49.72 ?  114 ILE B CG1   1 
ATOM   6503  C  CG2   . ILE B 1 114 ? 153.097 139.125 162.696 1.00 51.69 ?  114 ILE B CG2   1 
ATOM   6504  C  CD1   . ILE B 1 114 ? 153.185 135.992 162.491 1.00 50.40 ?  114 ILE B CD1   1 
ATOM   6505  N  N     . LEU B 1 115 ? 154.410 141.503 160.611 1.00 49.76 ?  115 LEU B N     1 
ATOM   6506  C  CA    . LEU B 1 115 ? 154.648 142.894 160.972 1.00 48.02 ?  115 LEU B CA    1 
ATOM   6507  C  C     . LEU B 1 115 ? 153.663 143.414 162.007 1.00 49.77 ?  115 LEU B C     1 
ATOM   6508  O  O     . LEU B 1 115 ? 153.996 144.339 162.755 1.00 50.66 ?  115 LEU B O     1 
ATOM   6509  C  CB    . LEU B 1 115 ? 154.588 143.783 159.727 1.00 48.78 ?  115 LEU B CB    1 
ATOM   6510  C  CG    . LEU B 1 115 ? 155.788 143.719 158.784 1.00 48.87 ?  115 LEU B CG    1 
ATOM   6511  C  CD1   . LEU B 1 115 ? 155.425 144.302 157.430 1.00 48.97 ?  115 LEU B CD1   1 
ATOM   6512  C  CD2   . LEU B 1 115 ? 156.977 144.449 159.386 1.00 49.55 ?  115 LEU B CD2   1 
ATOM   6513  N  N     . GLU B 1 116 ? 152.462 142.845 162.072 1.00 49.06 ?  116 GLU B N     1 
ATOM   6514  C  CA    . GLU B 1 116 ? 151.407 143.335 162.948 1.00 45.44 ?  116 GLU B CA    1 
ATOM   6515  C  C     . GLU B 1 116 ? 151.053 142.284 163.988 1.00 45.77 ?  116 GLU B C     1 
ATOM   6516  O  O     . GLU B 1 116 ? 150.750 141.138 163.641 1.00 48.91 ?  116 GLU B O     1 
ATOM   6517  C  CB    . GLU B 1 116 ? 150.156 143.705 162.149 1.00 44.67 ?  116 GLU B CB    1 
ATOM   6518  C  CG    . GLU B 1 116 ? 149.961 145.191 161.945 1.00 44.82 ?  116 GLU B CG    1 
ATOM   6519  C  CD    . GLU B 1 116 ? 148.669 145.509 161.224 1.00 45.82 ?  116 GLU B CD    1 
ATOM   6520  O  OE1   . GLU B 1 116 ? 147.954 144.562 160.837 1.00 44.53 ?  116 GLU B OE1   1 
ATOM   6521  O  OE2   . GLU B 1 116 ? 148.365 146.707 161.042 1.00 47.68 -1 116 GLU B OE2   1 
ATOM   6522  N  N     . ARG B 1 117 ? 151.084 142.681 165.256 1.00 40.37 ?  117 ARG B N     1 
ATOM   6523  C  CA    . ARG B 1 117 ? 150.505 141.876 166.317 1.00 41.84 ?  117 ARG B CA    1 
ATOM   6524  C  C     . ARG B 1 117 ? 149.011 142.178 166.417 1.00 42.11 ?  117 ARG B C     1 
ATOM   6525  O  O     . ARG B 1 117 ? 148.470 143.012 165.685 1.00 44.85 ?  117 ARG B O     1 
ATOM   6526  C  CB    . ARG B 1 117 ? 151.218 142.146 167.639 1.00 43.52 ?  117 ARG B CB    1 
ATOM   6527  C  CG    . ARG B 1 117 ? 152.650 141.641 167.689 1.00 43.24 ?  117 ARG B CG    1 
ATOM   6528  C  CD    . ARG B 1 117 ? 152.737 140.184 167.264 1.00 45.76 ?  117 ARG B CD    1 
ATOM   6529  N  NE    . ARG B 1 117 ? 153.735 139.447 168.030 1.00 45.69 ?  117 ARG B NE    1 
ATOM   6530  C  CZ    . ARG B 1 117 ? 153.558 139.007 169.268 1.00 45.62 ?  117 ARG B CZ    1 
ATOM   6531  N  NH1   . ARG B 1 117 ? 152.424 139.210 169.919 1.00 44.83 1  117 ARG B NH1   1 
ATOM   6532  N  NH2   . ARG B 1 117 ? 154.543 138.345 169.869 1.00 48.06 ?  117 ARG B NH2   1 
ATOM   6533  N  N     . TYR B 1 118 ? 148.324 141.486 167.326 1.00 39.73 ?  118 TYR B N     1 
ATOM   6534  C  CA    . TYR B 1 118 ? 146.915 141.791 167.554 1.00 36.21 ?  118 TYR B CA    1 
ATOM   6535  C  C     . TYR B 1 118 ? 146.748 143.202 168.096 1.00 37.83 ?  118 TYR B C     1 
ATOM   6536  O  O     . TYR B 1 118 ? 145.859 143.946 167.661 1.00 41.14 ?  118 TYR B O     1 
ATOM   6537  C  CB    . TYR B 1 118 ? 146.298 140.768 168.505 1.00 34.13 ?  118 TYR B CB    1 
ATOM   6538  C  CG    . TYR B 1 118 ? 144.790 140.832 168.568 1.00 35.58 ?  118 TYR B CG    1 
ATOM   6539  C  CD1   . TYR B 1 118 ? 144.025 140.768 167.412 1.00 34.33 ?  118 TYR B CD1   1 
ATOM   6540  C  CD2   . TYR B 1 118 ? 144.132 140.960 169.782 1.00 35.30 ?  118 TYR B CD2   1 
ATOM   6541  C  CE1   . TYR B 1 118 ? 142.647 140.826 167.465 1.00 34.36 ?  118 TYR B CE1   1 
ATOM   6542  C  CE2   . TYR B 1 118 ? 142.756 141.016 169.846 1.00 30.65 ?  118 TYR B CE2   1 
ATOM   6543  C  CZ    . TYR B 1 118 ? 142.018 140.951 168.684 1.00 36.75 ?  118 TYR B CZ    1 
ATOM   6544  O  OH    . TYR B 1 118 ? 140.645 141.010 168.743 1.00 40.55 ?  118 TYR B OH    1 
ATOM   6545  N  N     . GLU B 1 119 ? 147.610 143.595 169.035 1.00 39.86 ?  119 GLU B N     1 
ATOM   6546  C  CA    . GLU B 1 119 ? 147.550 144.945 169.578 1.00 39.18 ?  119 GLU B CA    1 
ATOM   6547  C  C     . GLU B 1 119 ? 147.890 145.985 168.519 1.00 38.98 ?  119 GLU B C     1 
ATOM   6548  O  O     . GLU B 1 119 ? 147.284 147.058 168.486 1.00 43.90 ?  119 GLU B O     1 
ATOM   6549  C  CB    . GLU B 1 119 ? 148.484 145.068 170.780 1.00 36.58 ?  119 GLU B CB    1 
ATOM   6550  C  CG    . GLU B 1 119 ? 147.952 144.421 172.045 1.00 36.87 ?  119 GLU B CG    1 
ATOM   6551  C  CD    . GLU B 1 119 ? 148.519 143.036 172.276 1.00 44.14 ?  119 GLU B CD    1 
ATOM   6552  O  OE1   . GLU B 1 119 ? 148.853 142.355 171.283 1.00 43.47 ?  119 GLU B OE1   1 
ATOM   6553  O  OE2   . GLU B 1 119 ? 148.629 142.626 173.451 1.00 45.63 -1 119 GLU B OE2   1 
ATOM   6554  N  N     . ASP B 1 120 ? 148.853 145.688 167.643 1.00 40.51 ?  120 ASP B N     1 
ATOM   6555  C  CA    . ASP B 1 120 ? 149.199 146.628 166.579 1.00 37.36 ?  120 ASP B CA    1 
ATOM   6556  C  C     . ASP B 1 120 ? 148.032 146.827 165.620 1.00 35.98 ?  120 ASP B C     1 
ATOM   6557  O  O     . ASP B 1 120 ? 147.701 147.960 165.249 1.00 39.04 ?  120 ASP B O     1 
ATOM   6558  C  CB    . ASP B 1 120 ? 150.431 146.132 165.819 1.00 41.42 ?  120 ASP B CB    1 
ATOM   6559  C  CG    . ASP B 1 120 ? 151.618 145.895 166.725 1.00 45.25 ?  120 ASP B CG    1 
ATOM   6560  O  OD1   . ASP B 1 120 ? 151.727 146.588 167.757 1.00 45.23 ?  120 ASP B OD1   1 
ATOM   6561  O  OD2   . ASP B 1 120 ? 152.442 145.014 166.406 1.00 48.28 -1 120 ASP B OD2   1 
ATOM   6562  N  N     . ARG B 1 121 ? 147.395 145.729 165.209 1.00 33.62 ?  121 ARG B N     1 
ATOM   6563  C  CA    . ARG B 1 121 ? 146.245 145.823 164.317 1.00 33.76 ?  121 ARG B CA    1 
ATOM   6564  C  C     . ARG B 1 121 ? 145.104 146.589 164.974 1.00 36.24 ?  121 ARG B C     1 
ATOM   6565  O  O     . ARG B 1 121 ? 144.475 147.446 164.341 1.00 37.10 ?  121 ARG B O     1 
ATOM   6566  C  CB    . ARG B 1 121 ? 145.794 144.421 163.908 1.00 32.18 ?  121 ARG B CB    1 
ATOM   6567  C  CG    . ARG B 1 121 ? 144.505 144.372 163.108 1.00 30.15 ?  121 ARG B CG    1 
ATOM   6568  C  CD    . ARG B 1 121 ? 144.761 144.577 161.629 1.00 30.70 ?  121 ARG B CD    1 
ATOM   6569  N  NE    . ARG B 1 121 ? 144.246 145.859 161.168 1.00 37.96 ?  121 ARG B NE    1 
ATOM   6570  C  CZ    . ARG B 1 121 ? 144.854 146.640 160.288 1.00 34.88 ?  121 ARG B CZ    1 
ATOM   6571  N  NH1   . ARG B 1 121 ? 146.009 146.298 159.741 1.00 37.95 1  121 ARG B NH1   1 
ATOM   6572  N  NH2   . ARG B 1 121 ? 144.291 147.794 159.948 1.00 31.85 ?  121 ARG B NH2   1 
ATOM   6573  N  N     . ILE B 1 122 ? 144.835 146.303 166.249 1.00 33.71 ?  122 ILE B N     1 
ATOM   6574  C  CA    . ILE B 1 122 ? 143.757 146.989 166.952 1.00 26.54 ?  122 ILE B CA    1 
ATOM   6575  C  C     . ILE B 1 122 ? 144.065 148.474 167.091 1.00 30.87 ?  122 ILE B C     1 
ATOM   6576  O  O     . ILE B 1 122 ? 143.181 149.319 166.924 1.00 37.19 ?  122 ILE B O     1 
ATOM   6577  C  CB    . ILE B 1 122 ? 143.504 146.320 168.314 1.00 33.72 ?  122 ILE B CB    1 
ATOM   6578  C  CG1   . ILE B 1 122 ? 142.667 145.056 168.120 1.00 29.67 ?  122 ILE B CG1   1 
ATOM   6579  C  CG2   . ILE B 1 122 ? 142.814 147.280 169.275 1.00 31.03 ?  122 ILE B CG2   1 
ATOM   6580  C  CD1   . ILE B 1 122 ? 142.211 144.431 169.402 1.00 29.81 ?  122 ILE B CD1   1 
ATOM   6581  N  N     . SER B 1 123 ? 145.320 148.819 167.392 1.00 35.20 ?  123 SER B N     1 
ATOM   6582  C  CA    . SER B 1 123 ? 145.700 150.222 167.506 1.00 30.91 ?  123 SER B CA    1 
ATOM   6583  C  C     . SER B 1 123 ? 145.542 150.947 166.177 1.00 30.80 ?  123 SER B C     1 
ATOM   6584  O  O     . SER B 1 123 ? 145.057 152.081 166.137 1.00 39.32 ?  123 SER B O     1 
ATOM   6585  C  CB    . SER B 1 123 ? 147.140 150.342 168.001 1.00 32.46 ?  123 SER B CB    1 
ATOM   6586  O  OG    . SER B 1 123 ? 147.360 149.531 169.137 1.00 36.41 ?  123 SER B OG    1 
ATOM   6587  N  N     . ILE B 1 124 ? 145.956 150.311 165.079 1.00 30.84 ?  124 ILE B N     1 
ATOM   6588  C  CA    . ILE B 1 124 ? 145.830 150.948 163.772 1.00 31.07 ?  124 ILE B CA    1 
ATOM   6589  C  C     . ILE B 1 124 ? 144.363 151.152 163.416 1.00 34.58 ?  124 ILE B C     1 
ATOM   6590  O  O     . ILE B 1 124 ? 143.969 152.221 162.927 1.00 36.70 ?  124 ILE B O     1 
ATOM   6591  C  CB    . ILE B 1 124 ? 146.573 150.123 162.704 1.00 37.99 ?  124 ILE B CB    1 
ATOM   6592  C  CG1   . ILE B 1 124 ? 148.083 150.262 162.896 1.00 37.08 ?  124 ILE B CG1   1 
ATOM   6593  C  CG2   . ILE B 1 124 ? 146.168 150.559 161.306 1.00 34.09 ?  124 ILE B CG2   1 
ATOM   6594  C  CD1   . ILE B 1 124 ? 148.546 151.691 163.086 1.00 34.28 ?  124 ILE B CD1   1 
ATOM   6595  N  N     . VAL B 1 125 ? 143.529 150.141 163.669 1.00 33.80 ?  125 VAL B N     1 
ATOM   6596  C  CA    . VAL B 1 125 ? 142.105 150.264 163.372 1.00 27.57 ?  125 VAL B CA    1 
ATOM   6597  C  C     . VAL B 1 125 ? 141.471 151.354 164.230 1.00 24.37 ?  125 VAL B C     1 
ATOM   6598  O  O     . VAL B 1 125 ? 140.639 152.135 163.751 1.00 35.89 ?  125 VAL B O     1 
ATOM   6599  C  CB    . VAL B 1 125 ? 141.400 148.906 163.558 1.00 31.00 ?  125 VAL B CB    1 
ATOM   6600  C  CG1   . VAL B 1 125 ? 139.901 149.061 163.424 1.00 31.11 ?  125 VAL B CG1   1 
ATOM   6601  C  CG2   . VAL B 1 125 ? 141.911 147.906 162.537 1.00 28.16 ?  125 VAL B CG2   1 
ATOM   6602  N  N     . ALA B 1 126 ? 141.860 151.435 165.504 1.00 23.02 ?  126 ALA B N     1 
ATOM   6603  C  CA    . ALA B 1 126 ? 141.319 152.461 166.391 1.00 25.33 ?  126 ALA B CA    1 
ATOM   6604  C  C     . ALA B 1 126 ? 141.743 153.857 165.957 1.00 30.57 ?  126 ALA B C     1 
ATOM   6605  O  O     . ALA B 1 126 ? 140.940 154.797 165.999 1.00 35.12 ?  126 ALA B O     1 
ATOM   6606  C  CB    . ALA B 1 126 ? 141.763 152.193 167.825 1.00 31.54 ?  126 ALA B CB    1 
ATOM   6607  N  N     . LEU B 1 127 ? 143.006 154.016 165.555 1.00 33.87 ?  127 LEU B N     1 
ATOM   6608  C  CA    . LEU B 1 127 ? 143.477 155.314 165.090 1.00 29.95 ?  127 LEU B CA    1 
ATOM   6609  C  C     . LEU B 1 127 ? 142.773 155.723 163.806 1.00 30.74 ?  127 LEU B C     1 
ATOM   6610  O  O     . LEU B 1 127 ? 142.475 156.906 163.605 1.00 36.71 ?  127 LEU B O     1 
ATOM   6611  C  CB    . LEU B 1 127 ? 144.991 155.281 164.891 1.00 33.31 ?  127 LEU B CB    1 
ATOM   6612  C  CG    . LEU B 1 127 ? 145.840 155.233 166.162 1.00 32.21 ?  127 LEU B CG    1 
ATOM   6613  C  CD1   . LEU B 1 127 ? 147.246 154.761 165.843 1.00 36.25 ?  127 LEU B CD1   1 
ATOM   6614  C  CD2   . LEU B 1 127 ? 145.869 156.589 166.846 1.00 33.87 ?  127 LEU B CD2   1 
ATOM   6615  N  N     . PHE B 1 128 ? 142.506 154.762 162.919 1.00 29.85 ?  128 PHE B N     1 
ATOM   6616  C  CA    . PHE B 1 128 ? 141.720 155.067 161.727 1.00 29.40 ?  128 PHE B CA    1 
ATOM   6617  C  C     . PHE B 1 128 ? 140.297 155.470 162.097 1.00 28.36 ?  128 PHE B C     1 
ATOM   6618  O  O     . PHE B 1 128 ? 139.736 156.404 161.513 1.00 33.31 ?  128 PHE B O     1 
ATOM   6619  C  CB    . PHE B 1 128 ? 141.709 153.866 160.781 1.00 28.61 ?  128 PHE B CB    1 
ATOM   6620  C  CG    . PHE B 1 128 ? 140.615 153.919 159.756 1.00 33.12 ?  128 PHE B CG    1 
ATOM   6621  C  CD1   . PHE B 1 128 ? 140.733 154.732 158.643 1.00 31.02 ?  128 PHE B CD1   1 
ATOM   6622  C  CD2   . PHE B 1 128 ? 139.465 153.163 159.910 1.00 32.42 ?  128 PHE B CD2   1 
ATOM   6623  C  CE1   . PHE B 1 128 ? 139.729 154.790 157.700 1.00 31.53 ?  128 PHE B CE1   1 
ATOM   6624  C  CE2   . PHE B 1 128 ? 138.457 153.220 158.972 1.00 31.93 ?  128 PHE B CE2   1 
ATOM   6625  C  CZ    . PHE B 1 128 ? 138.589 154.034 157.865 1.00 31.58 ?  128 PHE B CZ    1 
ATOM   6626  N  N     . PHE B 1 129 ? 139.697 154.769 163.061 1.00 29.04 ?  129 PHE B N     1 
ATOM   6627  C  CA    . PHE B 1 129 ? 138.327 155.067 163.467 1.00 26.13 ?  129 PHE B CA    1 
ATOM   6628  C  C     . PHE B 1 129 ? 138.211 156.460 164.073 1.00 28.48 ?  129 PHE B C     1 
ATOM   6629  O  O     . PHE B 1 129 ? 137.265 157.199 163.776 1.00 32.18 ?  129 PHE B O     1 
ATOM   6630  C  CB    . PHE B 1 129 ? 137.838 154.024 164.470 1.00 28.98 ?  129 PHE B CB    1 
ATOM   6631  C  CG    . PHE B 1 129 ? 137.394 152.735 163.849 1.00 26.86 ?  129 PHE B CG    1 
ATOM   6632  C  CD1   . PHE B 1 129 ? 137.176 152.641 162.488 1.00 25.66 ?  129 PHE B CD1   1 
ATOM   6633  C  CD2   . PHE B 1 129 ? 137.182 151.617 164.636 1.00 25.26 ?  129 PHE B CD2   1 
ATOM   6634  C  CE1   . PHE B 1 129 ? 136.763 151.453 161.922 1.00 26.72 ?  129 PHE B CE1   1 
ATOM   6635  C  CE2   . PHE B 1 129 ? 136.766 150.428 164.077 1.00 28.32 ?  129 PHE B CE2   1 
ATOM   6636  C  CZ    . PHE B 1 129 ? 136.557 150.345 162.717 1.00 30.23 ?  129 PHE B CZ    1 
ATOM   6637  N  N     . ALA B 1 130 ? 139.161 156.832 164.932 1.00 33.69 ?  130 ALA B N     1 
ATOM   6638  C  CA    . ALA B 1 130 ? 139.020 158.063 165.704 1.00 35.78 ?  130 ALA B CA    1 
ATOM   6639  C  C     . ALA B 1 130 ? 139.155 159.306 164.836 1.00 40.17 ?  130 ALA B C     1 
ATOM   6640  O  O     . ALA B 1 130 ? 138.565 160.345 165.156 1.00 46.69 ?  130 ALA B O     1 
ATOM   6641  C  CB    . ALA B 1 130 ? 140.046 158.090 166.832 1.00 33.05 ?  130 ALA B CB    1 
ATOM   6642  N  N     . ASN B 1 131 ? 139.925 159.226 163.749 1.00 41.05 ?  131 ASN B N     1 
ATOM   6643  C  CA    . ASN B 1 131 ? 140.102 160.337 162.813 1.00 41.85 ?  131 ASN B CA    1 
ATOM   6644  C  C     . ASN B 1 131 ? 140.672 161.573 163.512 1.00 41.78 ?  131 ASN B C     1 
ATOM   6645  O  O     . ASN B 1 131 ? 140.160 162.685 163.377 1.00 44.86 ?  131 ASN B O     1 
ATOM   6646  C  CB    . ASN B 1 131 ? 138.788 160.667 162.098 1.00 38.10 ?  131 ASN B CB    1 
ATOM   6647  C  CG    . ASN B 1 131 ? 139.008 161.257 160.720 1.00 45.08 ?  131 ASN B CG    1 
ATOM   6648  O  OD1   . ASN B 1 131 ? 140.002 160.964 160.056 1.00 45.24 ?  131 ASN B OD1   1 
ATOM   6649  N  ND2   . ASN B 1 131 ? 138.074 162.092 160.279 1.00 43.88 ?  131 ASN B ND2   1 
ATOM   6650  N  N     . GLY B 1 132 ? 141.748 161.366 164.270 1.00 42.24 ?  132 GLY B N     1 
ATOM   6651  C  CA    . GLY B 1 132 ? 142.463 162.453 164.905 1.00 43.72 ?  132 GLY B CA    1 
ATOM   6652  C  C     . GLY B 1 132 ? 142.161 162.680 166.370 1.00 46.62 ?  132 GLY B C     1 
ATOM   6653  O  O     . GLY B 1 132 ? 142.748 163.589 166.967 1.00 49.36 ?  132 GLY B O     1 
ATOM   6654  N  N     . ASP B 1 133 ? 141.274 161.890 166.970 1.00 42.99 ?  133 ASP B N     1 
ATOM   6655  C  CA    . ASP B 1 133 ? 140.902 162.047 168.373 1.00 43.79 ?  133 ASP B CA    1 
ATOM   6656  C  C     . ASP B 1 133 ? 141.630 160.987 169.195 1.00 46.29 ?  133 ASP B C     1 
ATOM   6657  O  O     . ASP B 1 133 ? 141.331 159.794 169.086 1.00 48.43 ?  133 ASP B O     1 
ATOM   6658  C  CB    . ASP B 1 133 ? 139.390 161.938 168.546 1.00 45.24 ?  133 ASP B CB    1 
ATOM   6659  C  CG    . ASP B 1 133 ? 138.905 162.537 169.853 1.00 48.48 ?  133 ASP B CG    1 
ATOM   6660  O  OD1   . ASP B 1 133 ? 139.728 162.711 170.775 1.00 49.94 ?  133 ASP B OD1   1 
ATOM   6661  O  OD2   . ASP B 1 133 ? 137.696 162.833 169.958 1.00 49.76 -1 133 ASP B OD2   1 
ATOM   6662  N  N     . THR B 1 134 ? 142.585 161.425 170.017 1.00 46.10 ?  134 THR B N     1 
ATOM   6663  C  CA    . THR B 1 134 ? 143.370 160.480 170.806 1.00 45.62 ?  134 THR B CA    1 
ATOM   6664  C  C     . THR B 1 134 ? 142.510 159.760 171.837 1.00 45.11 ?  134 THR B C     1 
ATOM   6665  O  O     . THR B 1 134 ? 142.646 158.546 172.026 1.00 45.77 ?  134 THR B O     1 
ATOM   6666  C  CB    . THR B 1 134 ? 144.528 161.204 171.489 1.00 47.78 ?  134 THR B CB    1 
ATOM   6667  O  OG1   . THR B 1 134 ? 145.223 162.001 170.523 1.00 49.81 ?  134 THR B OG1   1 
ATOM   6668  C  CG2   . THR B 1 134 ? 145.492 160.201 172.105 1.00 46.42 ?  134 THR B CG2   1 
ATOM   6669  N  N     . GLU B 1 135 ? 141.623 160.489 172.519 1.00 43.87 ?  135 GLU B N     1 
ATOM   6670  C  CA    . GLU B 1 135 ? 140.753 159.857 173.505 1.00 42.72 ?  135 GLU B CA    1 
ATOM   6671  C  C     . GLU B 1 135 ? 139.792 158.876 172.846 1.00 44.61 ?  135 GLU B C     1 
ATOM   6672  O  O     . GLU B 1 135 ? 139.546 157.786 173.376 1.00 45.08 ?  135 GLU B O     1 
ATOM   6673  C  CB    . GLU B 1 135 ? 139.989 160.922 174.290 1.00 45.96 ?  135 GLU B CB    1 
ATOM   6674  C  CG    . GLU B 1 135 ? 140.877 161.784 175.168 1.00 46.64 ?  135 GLU B CG    1 
ATOM   6675  C  CD    . GLU B 1 135 ? 141.834 160.962 176.010 1.00 50.56 ?  135 GLU B CD    1 
ATOM   6676  O  OE1   . GLU B 1 135 ? 141.359 160.128 176.808 1.00 49.79 ?  135 GLU B OE1   1 
ATOM   6677  O  OE2   . GLU B 1 135 ? 143.061 161.148 175.870 1.00 49.37 -1 135 GLU B OE2   1 
ATOM   6678  N  N     . LYS B 1 136 ? 139.240 159.243 171.688 1.00 40.26 ?  136 LYS B N     1 
ATOM   6679  C  CA    . LYS B 1 136 ? 138.381 158.320 170.954 1.00 37.63 ?  136 LYS B CA    1 
ATOM   6680  C  C     . LYS B 1 136 ? 139.168 157.104 170.479 1.00 37.69 ?  136 LYS B C     1 
ATOM   6681  O  O     . LYS B 1 136 ? 138.648 155.982 170.470 1.00 41.90 ?  136 LYS B O     1 
ATOM   6682  C  CB    . LYS B 1 136 ? 137.729 159.038 169.775 1.00 42.81 ?  136 LYS B CB    1 
ATOM   6683  C  CG    . LYS B 1 136 ? 136.509 158.338 169.208 1.00 41.41 ?  136 LYS B CG    1 
ATOM   6684  C  CD    . LYS B 1 136 ? 135.238 158.792 169.902 1.00 41.96 ?  136 LYS B CD    1 
ATOM   6685  C  CE    . LYS B 1 136 ? 134.011 158.464 169.069 1.00 42.73 ?  136 LYS B CE    1 
ATOM   6686  N  NZ    . LYS B 1 136 ? 132.801 159.173 169.564 1.00 43.51 1  136 LYS B NZ    1 
ATOM   6687  N  N     . ALA B 1 137 ? 140.424 157.308 170.078 1.00 36.90 ?  137 ALA B N     1 
ATOM   6688  C  CA    . ALA B 1 137 ? 141.264 156.184 169.679 1.00 33.48 ?  137 ALA B CA    1 
ATOM   6689  C  C     . ALA B 1 137 ? 141.510 155.240 170.847 1.00 36.36 ?  137 ALA B C     1 
ATOM   6690  O  O     . ALA B 1 137 ? 141.485 154.016 170.681 1.00 39.45 ?  137 ALA B O     1 
ATOM   6691  C  CB    . ALA B 1 137 ? 142.587 156.692 169.107 1.00 33.49 ?  137 ALA B CB    1 
ATOM   6692  N  N     . LYS B 1 138 ? 141.739 155.791 172.041 1.00 38.61 ?  138 LYS B N     1 
ATOM   6693  C  CA    . LYS B 1 138 ? 141.901 154.950 173.223 1.00 36.74 ?  138 LYS B CA    1 
ATOM   6694  C  C     . LYS B 1 138 ? 140.609 154.221 173.566 1.00 37.49 ?  138 LYS B C     1 
ATOM   6695  O  O     . LYS B 1 138 ? 140.639 153.065 174.003 1.00 39.01 ?  138 LYS B O     1 
ATOM   6696  C  CB    . LYS B 1 138 ? 142.372 155.788 174.410 1.00 41.46 ?  138 LYS B CB    1 
ATOM   6697  C  CG    . LYS B 1 138 ? 143.723 156.443 174.210 1.00 41.35 ?  138 LYS B CG    1 
ATOM   6698  C  CD    . LYS B 1 138 ? 144.497 156.490 175.512 1.00 38.39 ?  138 LYS B CD    1 
ATOM   6699  C  CE    . LYS B 1 138 ? 145.452 157.665 175.536 1.00 41.44 ?  138 LYS B CE    1 
ATOM   6700  N  NZ    . LYS B 1 138 ? 144.753 158.951 175.266 1.00 43.43 1  138 LYS B NZ    1 
ATOM   6701  N  N     . GLU B 1 139 ? 139.464 154.883 173.390 1.00 37.44 ?  139 GLU B N     1 
ATOM   6702  C  CA    . GLU B 1 139 ? 138.185 154.219 173.623 1.00 37.33 ?  139 GLU B CA    1 
ATOM   6703  C  C     . GLU B 1 139 ? 137.991 153.048 172.666 1.00 36.11 ?  139 GLU B C     1 
ATOM   6704  O  O     . GLU B 1 139 ? 137.557 151.966 173.075 1.00 41.74 ?  139 GLU B O     1 
ATOM   6705  C  CB    . GLU B 1 139 ? 137.038 155.219 173.484 1.00 34.82 ?  139 GLU B CB    1 
ATOM   6706  C  CG    . GLU B 1 139 ? 136.970 156.244 174.603 1.00 38.00 ?  139 GLU B CG    1 
ATOM   6707  C  CD    . GLU B 1 139 ? 135.842 157.237 174.413 1.00 45.17 ?  139 GLU B CD    1 
ATOM   6708  O  OE1   . GLU B 1 139 ? 134.810 156.860 173.818 1.00 43.55 ?  139 GLU B OE1   1 
ATOM   6709  O  OE2   . GLU B 1 139 ? 135.986 158.395 174.857 1.00 44.22 -1 139 GLU B OE2   1 
ATOM   6710  N  N     . TYR B 1 140 ? 138.322 153.243 171.388 1.00 29.54 ?  140 TYR B N     1 
ATOM   6711  C  CA    . TYR B 1 140 ? 138.232 152.151 170.421 1.00 28.47 ?  140 TYR B CA    1 
ATOM   6712  C  C     . TYR B 1 140 ? 139.209 151.033 170.761 1.00 31.07 ?  140 TYR B C     1 
ATOM   6713  O  O     . TYR B 1 140 ? 138.891 149.847 170.600 1.00 35.49 ?  140 TYR B O     1 
ATOM   6714  C  CB    . TYR B 1 140 ? 138.495 152.673 169.010 1.00 29.36 ?  140 TYR B CB    1 
ATOM   6715  C  CG    . TYR B 1 140 ? 137.352 153.446 168.402 1.00 30.90 ?  140 TYR B CG    1 
ATOM   6716  C  CD1   . TYR B 1 140 ? 136.079 152.898 168.322 1.00 31.12 ?  140 TYR B CD1   1 
ATOM   6717  C  CD2   . TYR B 1 140 ? 137.548 154.723 167.901 1.00 32.00 ?  140 TYR B CD2   1 
ATOM   6718  C  CE1   . TYR B 1 140 ? 135.036 153.605 167.761 1.00 34.65 ?  140 TYR B CE1   1 
ATOM   6719  C  CE2   . TYR B 1 140 ? 136.513 155.436 167.343 1.00 30.75 ?  140 TYR B CE2   1 
ATOM   6720  C  CZ    . TYR B 1 140 ? 135.261 154.874 167.274 1.00 28.98 ?  140 TYR B CZ    1 
ATOM   6721  O  OH    . TYR B 1 140 ? 134.234 155.592 166.714 1.00 37.84 ?  140 TYR B OH    1 
ATOM   6722  N  N     . VAL B 1 141 ? 140.411 151.393 171.215 1.00 32.75 ?  141 VAL B N     1 
ATOM   6723  C  CA    . VAL B 1 141 ? 141.399 150.393 171.610 1.00 32.90 ?  141 VAL B CA    1 
ATOM   6724  C  C     . VAL B 1 141 ? 140.876 149.557 172.768 1.00 32.97 ?  141 VAL B C     1 
ATOM   6725  O  O     . VAL B 1 141 ? 140.996 148.329 172.773 1.00 38.73 ?  141 VAL B O     1 
ATOM   6726  C  CB    . VAL B 1 141 ? 142.735 151.072 171.962 1.00 35.19 ?  141 VAL B CB    1 
ATOM   6727  C  CG1   . VAL B 1 141 ? 143.493 150.250 172.974 1.00 33.55 ?  141 VAL B CG1   1 
ATOM   6728  C  CG2   . VAL B 1 141 ? 143.574 151.245 170.718 1.00 33.99 ?  141 VAL B CG2   1 
ATOM   6729  N  N     . ASN B 1 142 ? 140.292 150.212 173.772 1.00 32.61 ?  142 ASN B N     1 
ATOM   6730  C  CA    . ASN B 1 142 ? 139.738 149.477 174.902 1.00 30.80 ?  142 ASN B CA    1 
ATOM   6731  C  C     . ASN B 1 142 ? 138.542 148.635 174.485 1.00 31.55 ?  142 ASN B C     1 
ATOM   6732  O  O     . ASN B 1 142 ? 138.319 147.555 175.044 1.00 35.97 ?  142 ASN B O     1 
ATOM   6733  C  CB    . ASN B 1 142 ? 139.348 150.445 176.016 1.00 28.16 ?  142 ASN B CB    1 
ATOM   6734  C  CG    . ASN B 1 142 ? 140.551 151.009 176.742 1.00 32.27 ?  142 ASN B CG    1 
ATOM   6735  O  OD1   . ASN B 1 142 ? 141.397 150.265 177.237 1.00 32.50 ?  142 ASN B OD1   1 
ATOM   6736  N  ND2   . ASN B 1 142 ? 140.638 152.332 176.803 1.00 34.28 ?  142 ASN B ND2   1 
ATOM   6737  N  N     . LEU B 1 143 ? 137.766 149.109 173.509 1.00 31.52 ?  143 LEU B N     1 
ATOM   6738  C  CA    . LEU B 1 143 ? 136.606 148.358 173.047 1.00 25.88 ?  143 LEU B CA    1 
ATOM   6739  C  C     . LEU B 1 143 ? 137.017 147.102 172.287 1.00 30.44 ?  143 LEU B C     1 
ATOM   6740  O  O     . LEU B 1 143 ? 136.375 146.054 172.416 1.00 32.84 ?  143 LEU B O     1 
ATOM   6741  C  CB    . LEU B 1 143 ? 135.732 149.255 172.174 1.00 25.23 ?  143 LEU B CB    1 
ATOM   6742  C  CG    . LEU B 1 143 ? 134.255 148.891 172.055 1.00 28.76 ?  143 LEU B CG    1 
ATOM   6743  C  CD1   . LEU B 1 143 ? 133.522 149.301 173.316 1.00 31.58 ?  143 LEU B CD1   1 
ATOM   6744  C  CD2   . LEU B 1 143 ? 133.658 149.575 170.844 1.00 28.42 ?  143 LEU B CD2   1 
ATOM   6745  N  N     . MET B 1 144 ? 138.077 147.190 171.485 1.00 28.96 ?  144 MET B N     1 
ATOM   6746  C  CA    . MET B 1 144 ? 138.497 146.057 170.668 1.00 21.69 ?  144 MET B CA    1 
ATOM   6747  C  C     . MET B 1 144 ? 139.437 145.103 171.394 1.00 26.49 ?  144 MET B C     1 
ATOM   6748  O  O     . MET B 1 144 ? 139.389 143.894 171.143 1.00 30.49 ?  144 MET B O     1 
ATOM   6749  C  CB    . MET B 1 144 ? 139.163 146.552 169.382 1.00 24.86 ?  144 MET B CB    1 
ATOM   6750  C  CG    . MET B 1 144 ? 138.212 147.258 168.433 1.00 25.95 ?  144 MET B CG    1 
ATOM   6751  S  SD    . MET B 1 144 ? 138.969 147.629 166.843 1.00 37.66 ?  144 MET B SD    1 
ATOM   6752  C  CE    . MET B 1 144 ? 139.527 149.304 167.130 1.00 27.90 ?  144 MET B CE    1 
ATOM   6753  N  N     . ILE B 1 145 ? 140.301 145.613 172.274 1.00 29.57 ?  145 ILE B N     1 
ATOM   6754  C  CA    . ILE B 1 145 ? 141.189 144.741 173.036 1.00 30.47 ?  145 ILE B CA    1 
ATOM   6755  C  C     . ILE B 1 145 ? 140.410 143.969 174.098 1.00 31.16 ?  145 ILE B C     1 
ATOM   6756  O  O     . ILE B 1 145 ? 140.753 142.825 174.412 1.00 35.22 ?  145 ILE B O     1 
ATOM   6757  C  CB    . ILE B 1 145 ? 142.354 145.551 173.637 1.00 29.75 ?  145 ILE B CB    1 
ATOM   6758  C  CG1   . ILE B 1 145 ? 143.615 144.689 173.729 1.00 28.07 ?  145 ILE B CG1   1 
ATOM   6759  C  CG2   . ILE B 1 145 ? 141.997 146.137 174.998 1.00 31.72 ?  145 ILE B CG2   1 
ATOM   6760  C  CD1   . ILE B 1 145 ? 144.262 144.406 172.395 1.00 28.63 ?  145 ILE B CD1   1 
ATOM   6761  N  N     . ASN B 1 146 ? 139.355 144.567 174.660 1.00 28.14 ?  146 ASN B N     1 
ATOM   6762  C  CA    . ASN B 1 146 ? 138.415 143.812 175.477 1.00 28.75 ?  146 ASN B CA    1 
ATOM   6763  C  C     . ASN B 1 146 ? 137.550 142.891 174.635 1.00 30.68 ?  146 ASN B C     1 
ATOM   6764  O  O     . ASN B 1 146 ? 136.809 142.076 175.197 1.00 37.17 ?  146 ASN B O     1 
ATOM   6765  C  CB    . ASN B 1 146 ? 137.523 144.758 176.281 1.00 28.50 ?  146 ASN B CB    1 
ATOM   6766  C  CG    . ASN B 1 146 ? 138.288 145.525 177.337 1.00 31.95 ?  146 ASN B CG    1 
ATOM   6767  O  OD1   . ASN B 1 146 ? 139.384 145.133 177.734 1.00 33.23 ?  146 ASN B OD1   1 
ATOM   6768  N  ND2   . ASN B 1 146 ? 137.711 146.627 177.800 1.00 31.99 ?  146 ASN B ND2   1 
ATOM   6769  N  N     . GLN B 1 147 ? 137.622 143.018 173.309 1.00 27.45 ?  147 GLN B N     1 
ATOM   6770  C  CA    . GLN B 1 147 ? 136.852 142.205 172.374 1.00 23.39 ?  147 GLN B CA    1 
ATOM   6771  C  C     . GLN B 1 147 ? 135.353 142.370 172.586 1.00 23.64 ?  147 GLN B C     1 
ATOM   6772  O  O     . GLN B 1 147 ? 134.581 141.436 172.375 1.00 30.53 ?  147 GLN B O     1 
ATOM   6773  C  CB    . GLN B 1 147 ? 137.255 140.730 172.459 1.00 26.93 ?  147 GLN B CB    1 
ATOM   6774  C  CG    . GLN B 1 147 ? 138.690 140.469 172.044 1.00 20.38 ?  147 GLN B CG    1 
ATOM   6775  C  CD    . GLN B 1 147 ? 138.903 139.058 171.544 1.00 27.43 ?  147 GLN B CD    1 
ATOM   6776  O  OE1   . GLN B 1 147 ? 139.601 138.836 170.555 1.00 28.19 ?  147 GLN B OE1   1 
ATOM   6777  N  NE2   . GLN B 1 147 ? 138.303 138.093 172.228 1.00 34.56 ?  147 GLN B NE2   1 
ATOM   6778  N  N     . GLU B 1 148 ? 134.935 143.559 173.021 1.00 26.03 ?  148 GLU B N     1 
ATOM   6779  C  CA    . GLU B 1 148 ? 133.513 143.872 173.086 1.00 23.10 ?  148 GLU B CA    1 
ATOM   6780  C  C     . GLU B 1 148 ? 132.929 144.116 171.702 1.00 26.63 ?  148 GLU B C     1 
ATOM   6781  O  O     . GLU B 1 148 ? 131.781 143.740 171.440 1.00 32.90 ?  148 GLU B O     1 
ATOM   6782  C  CB    . GLU B 1 148 ? 133.284 145.098 173.969 1.00 21.39 ?  148 GLU B CB    1 
ATOM   6783  C  CG    . GLU B 1 148 ? 133.719 144.915 175.409 1.00 26.46 ?  148 GLU B CG    1 
ATOM   6784  C  CD    . GLU B 1 148 ? 133.706 146.214 176.185 1.00 32.26 ?  148 GLU B CD    1 
ATOM   6785  O  OE1   . GLU B 1 148 ? 134.686 146.980 176.084 1.00 33.54 ?  148 GLU B OE1   1 
ATOM   6786  O  OE2   . GLU B 1 148 ? 132.713 146.472 176.896 1.00 37.57 -1 148 GLU B OE2   1 
ATOM   6787  N  N     . TYR B 1 149 ? 133.700 144.734 170.814 1.00 23.60 ?  149 TYR B N     1 
ATOM   6788  C  CA    . TYR B 1 149 ? 133.270 145.027 169.457 1.00 19.15 ?  149 TYR B CA    1 
ATOM   6789  C  C     . TYR B 1 149 ? 134.323 144.542 168.477 1.00 22.53 ?  149 TYR B C     1 
ATOM   6790  O  O     . TYR B 1 149 ? 135.525 144.633 168.742 1.00 28.88 ?  149 TYR B O     1 
ATOM   6791  C  CB    . TYR B 1 149 ? 133.022 146.522 169.260 1.00 21.16 ?  149 TYR B CB    1 
ATOM   6792  C  CG    . TYR B 1 149 ? 132.807 146.922 167.820 1.00 21.61 ?  149 TYR B CG    1 
ATOM   6793  C  CD1   . TYR B 1 149 ? 131.696 146.481 167.114 1.00 13.92 ?  149 TYR B CD1   1 
ATOM   6794  C  CD2   . TYR B 1 149 ? 133.715 147.743 167.167 1.00 19.53 ?  149 TYR B CD2   1 
ATOM   6795  C  CE1   . TYR B 1 149 ? 131.497 146.846 165.797 1.00 17.41 ?  149 TYR B CE1   1 
ATOM   6796  C  CE2   . TYR B 1 149 ? 133.525 148.114 165.854 1.00 20.91 ?  149 TYR B CE2   1 
ATOM   6797  C  CZ    . TYR B 1 149 ? 132.414 147.664 165.173 1.00 20.04 ?  149 TYR B CZ    1 
ATOM   6798  O  OH    . TYR B 1 149 ? 132.225 148.033 163.862 1.00 18.44 ?  149 TYR B OH    1 
ATOM   6799  N  N     . GLN B 1 150 ? 133.863 144.026 167.348 1.00 17.68 ?  150 GLN B N     1 
ATOM   6800  C  CA    . GLN B 1 150 ? 134.739 143.523 166.297 1.00 10.71 ?  150 GLN B CA    1 
ATOM   6801  C  C     . GLN B 1 150 ? 134.333 144.141 164.970 1.00 20.38 ?  150 GLN B C     1 
ATOM   6802  O  O     . GLN B 1 150 ? 133.214 143.880 164.486 1.00 23.27 ?  150 GLN B O     1 
ATOM   6803  C  CB    . GLN B 1 150 ? 134.665 141.999 166.229 1.00 17.41 ?  150 GLN B CB    1 
ATOM   6804  C  CG    . GLN B 1 150 ? 135.507 141.387 165.139 1.00 18.97 ?  150 GLN B CG    1 
ATOM   6805  C  CD    . GLN B 1 150 ? 136.965 141.779 165.233 1.00 17.16 ?  150 GLN B CD    1 
ATOM   6806  O  OE1   . GLN B 1 150 ? 137.645 141.461 166.208 1.00 30.40 ?  150 GLN B OE1   1 
ATOM   6807  N  NE2   . GLN B 1 150 ? 137.457 142.471 164.214 1.00 15.84 ?  150 GLN B NE2   1 
ATOM   6808  N  N     . PRO B 1 151 ? 135.171 144.977 164.362 1.00 26.31 ?  151 PRO B N     1 
ATOM   6809  C  CA    . PRO B 1 151 ? 134.889 145.432 163.000 1.00 16.21 ?  151 PRO B CA    1 
ATOM   6810  C  C     . PRO B 1 151 ? 134.896 144.259 162.034 1.00 16.18 ?  151 PRO B C     1 
ATOM   6811  O  O     . PRO B 1 151 ? 135.561 143.245 162.261 1.00 21.62 ?  151 PRO B O     1 
ATOM   6812  C  CB    . PRO B 1 151 ? 136.030 146.412 162.704 1.00 18.71 ?  151 PRO B CB    1 
ATOM   6813  C  CG    . PRO B 1 151 ? 136.543 146.820 164.047 1.00 18.97 ?  151 PRO B CG    1 
ATOM   6814  C  CD    . PRO B 1 151 ? 136.359 145.632 164.934 1.00 21.62 ?  151 PRO B CD    1 
ATOM   6815  N  N     . SER B 1 152 ? 134.130 144.397 160.957 1.00 21.04 ?  152 SER B N     1 
ATOM   6816  C  CA    . SER B 1 152 ? 134.021 143.332 159.973 1.00 14.61 ?  152 SER B CA    1 
ATOM   6817  C  C     . SER B 1 152 ? 135.389 142.990 159.391 1.00 22.02 ?  152 SER B C     1 
ATOM   6818  O  O     . SER B 1 152 ? 136.359 143.741 159.523 1.00 25.96 ?  152 SER B O     1 
ATOM   6819  C  CB    . SER B 1 152 ? 133.067 143.732 158.852 1.00 20.91 ?  152 SER B CB    1 
ATOM   6820  O  OG    . SER B 1 152 ? 133.603 144.792 158.080 1.00 24.93 ?  152 SER B OG    1 
ATOM   6821  N  N     . THR B 1 153 ? 135.458 141.828 158.743 1.00 28.20 ?  153 THR B N     1 
ATOM   6822  C  CA    . THR B 1 153 ? 136.698 141.390 158.107 1.00 20.89 ?  153 THR B CA    1 
ATOM   6823  C  C     . THR B 1 153 ? 137.278 142.424 157.147 1.00 27.54 ?  153 THR B C     1 
ATOM   6824  O  O     . THR B 1 153 ? 138.487 142.689 157.230 1.00 27.63 ?  153 THR B O     1 
ATOM   6825  C  CB    . THR B 1 153 ? 136.461 140.043 157.408 1.00 25.86 ?  153 THR B CB    1 
ATOM   6826  O  OG1   . THR B 1 153 ? 136.351 139.006 158.389 1.00 29.62 ?  153 THR B OG1   1 
ATOM   6827  C  CG2   . THR B 1 153 ? 137.602 139.718 156.456 1.00 25.78 ?  153 THR B CG2   1 
ATOM   6828  N  N     . PRO B 1 154 ? 136.506 143.050 156.246 1.00 25.81 ?  154 PRO B N     1 
ATOM   6829  C  CA    . PRO B 1 154 ? 137.105 144.119 155.425 1.00 19.80 ?  154 PRO B CA    1 
ATOM   6830  C  C     . PRO B 1 154 ? 137.658 145.266 156.250 1.00 20.96 ?  154 PRO B C     1 
ATOM   6831  O  O     . PRO B 1 154 ? 138.792 145.706 156.019 1.00 26.68 ?  154 PRO B O     1 
ATOM   6832  C  CB    . PRO B 1 154 ? 135.939 144.563 154.531 1.00 21.37 ?  154 PRO B CB    1 
ATOM   6833  C  CG    . PRO B 1 154 ? 135.029 143.402 154.489 1.00 24.97 ?  154 PRO B CG    1 
ATOM   6834  C  CD    . PRO B 1 154 ? 135.117 142.776 155.839 1.00 19.97 ?  154 PRO B CD    1 
ATOM   6835  N  N     . THR B 1 155 ? 136.891 145.755 157.227 1.00 22.65 ?  155 THR B N     1 
ATOM   6836  C  CA    . THR B 1 155 ? 137.342 146.886 158.029 1.00 20.13 ?  155 THR B CA    1 
ATOM   6837  C  C     . THR B 1 155 ? 138.520 146.503 158.915 1.00 24.21 ?  155 THR B C     1 
ATOM   6838  O  O     . THR B 1 155 ? 139.531 147.212 158.961 1.00 29.73 ?  155 THR B O     1 
ATOM   6839  C  CB    . THR B 1 155 ? 136.188 147.425 158.875 1.00 22.59 ?  155 THR B CB    1 
ATOM   6840  O  OG1   . THR B 1 155 ? 135.060 147.694 158.033 1.00 23.45 ?  155 THR B OG1   1 
ATOM   6841  C  CG2   . THR B 1 155 ? 136.601 148.704 159.577 1.00 17.64 ?  155 THR B CG2   1 
ATOM   6842  N  N     . PHE B 1 156 ? 138.412 145.380 159.628 1.00 23.30 ?  156 PHE B N     1 
ATOM   6843  C  CA    . PHE B 1 156 ? 139.488 144.971 160.524 1.00 20.13 ?  156 PHE B CA    1 
ATOM   6844  C  C     . PHE B 1 156 ? 140.771 144.680 159.755 1.00 29.69 ?  156 PHE B C     1 
ATOM   6845  O  O     . PHE B 1 156 ? 141.866 145.039 160.200 1.00 29.95 ?  156 PHE B O     1 
ATOM   6846  C  CB    . PHE B 1 156 ? 139.063 143.747 161.336 1.00 23.60 ?  156 PHE B CB    1 
ATOM   6847  C  CG    . PHE B 1 156 ? 139.912 143.501 162.549 1.00 28.03 ?  156 PHE B CG    1 
ATOM   6848  C  CD1   . PHE B 1 156 ? 140.030 144.466 163.536 1.00 24.88 ?  156 PHE B CD1   1 
ATOM   6849  C  CD2   . PHE B 1 156 ? 140.594 142.307 162.703 1.00 23.77 ?  156 PHE B CD2   1 
ATOM   6850  C  CE1   . PHE B 1 156 ? 140.811 144.242 164.652 1.00 26.16 ?  156 PHE B CE1   1 
ATOM   6851  C  CE2   . PHE B 1 156 ? 141.376 142.078 163.817 1.00 22.91 ?  156 PHE B CE2   1 
ATOM   6852  C  CZ    . PHE B 1 156 ? 141.484 143.047 164.792 1.00 29.01 ?  156 PHE B CZ    1 
ATOM   6853  N  N     . LEU B 1 157 ? 140.654 144.029 158.598 1.00 30.11 ?  157 LEU B N     1 
ATOM   6854  C  CA    . LEU B 1 157 ? 141.831 143.637 157.834 1.00 26.59 ?  157 LEU B CA    1 
ATOM   6855  C  C     . LEU B 1 157 ? 142.454 144.814 157.092 1.00 31.97 ?  157 LEU B C     1 
ATOM   6856  O  O     . LEU B 1 157 ? 143.682 144.892 156.976 1.00 40.37 ?  157 LEU B O     1 
ATOM   6857  C  CB    . LEU B 1 157 ? 141.458 142.524 156.851 1.00 30.79 ?  157 LEU B CB    1 
ATOM   6858  C  CG    . LEU B 1 157 ? 142.492 142.116 155.802 1.00 29.61 ?  157 LEU B CG    1 
ATOM   6859  C  CD1   . LEU B 1 157 ? 143.708 141.492 156.459 1.00 32.68 ?  157 LEU B CD1   1 
ATOM   6860  C  CD2   . LEU B 1 157 ? 141.877 141.161 154.793 1.00 30.30 ?  157 LEU B CD2   1 
ATOM   6861  N  N     . ASN B 1 158 ? 141.639 145.745 156.595 1.00 30.57 ?  158 ASN B N     1 
ATOM   6862  C  CA    . ASN B 1 158 ? 142.112 146.737 155.642 1.00 29.15 ?  158 ASN B CA    1 
ATOM   6863  C  C     . ASN B 1 158 ? 142.219 148.151 156.195 1.00 32.44 ?  158 ASN B C     1 
ATOM   6864  O  O     . ASN B 1 158 ? 142.704 149.032 155.478 1.00 39.63 ?  158 ASN B O     1 
ATOM   6865  C  CB    . ASN B 1 158 ? 141.193 146.753 154.412 1.00 29.82 ?  158 ASN B CB    1 
ATOM   6866  C  CG    . ASN B 1 158 ? 141.178 145.428 153.679 1.00 35.71 ?  158 ASN B CG    1 
ATOM   6867  O  OD1   . ASN B 1 158 ? 142.152 144.677 153.713 1.00 40.03 ?  158 ASN B OD1   1 
ATOM   6868  N  ND2   . ASN B 1 158 ? 140.069 145.133 153.014 1.00 35.98 ?  158 ASN B ND2   1 
ATOM   6869  N  N     . ALA B 1 159 ? 141.784 148.402 157.428 1.00 31.90 ?  159 ALA B N     1 
ATOM   6870  C  CA    . ALA B 1 159 ? 141.821 149.762 157.955 1.00 33.22 ?  159 ALA B CA    1 
ATOM   6871  C  C     . ALA B 1 159 ? 143.258 150.255 158.070 1.00 38.83 ?  159 ALA B C     1 
ATOM   6872  O  O     . ALA B 1 159 ? 144.116 149.583 158.650 1.00 42.87 ?  159 ALA B O     1 
ATOM   6873  C  CB    . ALA B 1 159 ? 141.135 149.829 159.318 1.00 32.12 ?  159 ALA B CB    1 
ATOM   6874  N  N     . GLY B 1 160 ? 143.518 151.434 157.512 1.00 45.42 ?  160 GLY B N     1 
ATOM   6875  C  CA    . GLY B 1 160 ? 144.826 152.042 157.613 1.00 40.42 ?  160 GLY B CA    1 
ATOM   6876  C  C     . GLY B 1 160 ? 145.903 151.425 156.751 1.00 40.71 ?  160 GLY B C     1 
ATOM   6877  O  O     . GLY B 1 160 ? 147.080 151.743 156.944 1.00 45.57 ?  160 GLY B O     1 
ATOM   6878  N  N     . ARG B 1 161 ? 145.546 150.557 155.810 1.00 43.00 ?  161 ARG B N     1 
ATOM   6879  C  CA    . ARG B 1 161 ? 146.513 149.895 154.947 1.00 44.08 ?  161 ARG B CA    1 
ATOM   6880  C  C     . ARG B 1 161 ? 146.551 150.572 153.584 1.00 46.63 ?  161 ARG B C     1 
ATOM   6881  O  O     . ARG B 1 161 ? 145.516 150.976 153.048 1.00 46.53 ?  161 ARG B O     1 
ATOM   6882  C  CB    . ARG B 1 161 ? 146.176 148.413 154.781 1.00 38.66 ?  161 ARG B CB    1 
ATOM   6883  C  CG    . ARG B 1 161 ? 146.432 147.574 156.020 1.00 39.48 ?  161 ARG B CG    1 
ATOM   6884  C  CD    . ARG B 1 161 ? 146.513 146.096 155.680 1.00 40.50 ?  161 ARG B CD    1 
ATOM   6885  N  NE    . ARG B 1 161 ? 146.526 145.262 156.876 1.00 44.00 ?  161 ARG B NE    1 
ATOM   6886  C  CZ    . ARG B 1 161 ? 146.519 143.936 156.865 1.00 44.80 ?  161 ARG B CZ    1 
ATOM   6887  N  NH1   . ARG B 1 161 ? 146.509 143.253 155.733 1.00 44.14 1  161 ARG B NH1   1 
ATOM   6888  N  NH2   . ARG B 1 161 ? 146.521 143.279 158.021 1.00 43.06 ?  161 ARG B NH2   1 
ATOM   6889  N  N     . LYS B 1 162 ? 147.760 150.706 153.030 1.00 53.05 ?  162 LYS B N     1 
ATOM   6890  C  CA    . LYS B 1 162 ? 147.900 151.298 151.703 1.00 52.29 ?  162 LYS B CA    1 
ATOM   6891  C  C     . LYS B 1 162 ? 147.417 150.342 150.618 1.00 52.62 ?  162 LYS B C     1 
ATOM   6892  O  O     . LYS B 1 162 ? 146.702 150.751 149.696 1.00 52.82 ?  162 LYS B O     1 
ATOM   6893  C  CB    . LYS B 1 162 ? 149.353 151.702 151.460 1.00 52.13 ?  162 LYS B CB    1 
ATOM   6894  C  CG    . LYS B 1 162 ? 149.660 152.095 150.025 1.00 52.46 ?  162 LYS B CG    1 
ATOM   6895  C  CD    . LYS B 1 162 ? 149.440 153.583 149.797 1.00 54.30 ?  162 LYS B CD    1 
ATOM   6896  C  CE    . LYS B 1 162 ? 150.253 154.420 150.770 1.00 54.39 ?  162 LYS B CE    1 
ATOM   6897  N  NZ    . LYS B 1 162 ? 149.569 155.701 151.102 1.00 54.64 1  162 LYS B NZ    1 
ATOM   6898  N  N     . ARG B 1 163 ? 147.786 149.064 150.717 1.00 53.33 ?  163 ARG B N     1 
ATOM   6899  C  CA    . ARG B 1 163 ? 147.377 148.044 149.759 1.00 55.14 ?  163 ARG B CA    1 
ATOM   6900  C  C     . ARG B 1 163 ? 145.987 147.490 150.053 1.00 57.86 ?  163 ARG B C     1 
ATOM   6901  O  O     . ARG B 1 163 ? 145.646 146.394 149.590 1.00 56.49 ?  163 ARG B O     1 
ATOM   6902  C  CB    . ARG B 1 163 ? 148.406 146.909 149.732 1.00 56.25 ?  163 ARG B CB    1 
ATOM   6903  C  CG    . ARG B 1 163 ? 148.506 146.180 148.399 1.00 58.12 ?  163 ARG B CG    1 
ATOM   6904  C  CD    . ARG B 1 163 ? 148.920 144.727 148.586 1.00 56.45 ?  163 ARG B CD    1 
ATOM   6905  N  NE    . ARG B 1 163 ? 148.279 144.108 149.740 1.00 59.28 ?  163 ARG B NE    1 
ATOM   6906  C  CZ    . ARG B 1 163 ? 147.042 143.631 149.747 1.00 58.45 ?  163 ARG B CZ    1 
ATOM   6907  N  NH1   . ARG B 1 163 ? 146.274 143.683 148.671 1.00 56.93 1  163 ARG B NH1   1 
ATOM   6908  N  NH2   . ARG B 1 163 ? 146.563 143.084 150.862 1.00 56.83 ?  163 ARG B NH2   1 
ATOM   6909  N  N     . ARG B 1 164 ? 145.184 148.225 150.814 1.00 55.68 ?  164 ARG B N     1 
ATOM   6910  C  CA    . ARG B 1 164 ? 143.870 147.761 151.222 1.00 50.63 ?  164 ARG B CA    1 
ATOM   6911  C  C     . ARG B 1 164 ? 142.893 147.766 150.051 1.00 50.63 ?  164 ARG B C     1 
ATOM   6912  O  O     . ARG B 1 164 ? 143.123 148.385 149.008 1.00 50.44 ?  164 ARG B O     1 
ATOM   6913  C  CB    . ARG B 1 164 ? 143.322 148.640 152.343 1.00 48.84 ?  164 ARG B CB    1 
ATOM   6914  C  CG    . ARG B 1 164 ? 142.735 149.957 151.859 1.00 45.63 ?  164 ARG B CG    1 
ATOM   6915  C  CD    . ARG B 1 164 ? 141.727 150.513 152.849 1.00 48.21 ?  164 ARG B CD    1 
ATOM   6916  N  NE    . ARG B 1 164 ? 141.069 151.714 152.347 1.00 50.38 ?  164 ARG B NE    1 
ATOM   6917  C  CZ    . ARG B 1 164 ? 140.714 152.744 153.104 1.00 53.94 ?  164 ARG B CZ    1 
ATOM   6918  N  NH1   . ARG B 1 164 ? 140.946 152.757 154.405 1.00 51.60 1  164 ARG B NH1   1 
ATOM   6919  N  NH2   . ARG B 1 164 ? 140.112 153.787 152.538 1.00 53.54 ?  164 ARG B NH2   1 
ATOM   6920  N  N     . GLY B 1 165 ? 141.791 147.054 150.239 1.00 49.03 ?  165 GLY B N     1 
ATOM   6921  C  CA    . GLY B 1 165 ? 140.639 147.135 149.364 1.00 45.13 ?  165 GLY B CA    1 
ATOM   6922  C  C     . GLY B 1 165 ? 139.622 148.123 149.889 1.00 48.10 ?  165 GLY B C     1 
ATOM   6923  O  O     . GLY B 1 165 ? 139.961 149.228 150.326 1.00 48.97 ?  165 GLY B O     1 
ATOM   6924  N  N     . GLU B 1 166 ? 138.357 147.726 149.848 1.00 43.00 ?  166 GLU B N     1 
ATOM   6925  C  CA    . GLU B 1 166 ? 137.292 148.526 150.432 1.00 39.82 ?  166 GLU B CA    1 
ATOM   6926  C  C     . GLU B 1 166 ? 136.870 147.948 151.777 1.00 37.59 ?  166 GLU B C     1 
ATOM   6927  O  O     . GLU B 1 166 ? 136.924 146.736 152.000 1.00 33.46 ?  166 GLU B O     1 
ATOM   6928  C  CB    . GLU B 1 166 ? 136.087 148.603 149.494 1.00 36.97 ?  166 GLU B CB    1 
ATOM   6929  C  CG    . GLU B 1 166 ? 136.189 149.708 148.459 1.00 41.28 ?  166 GLU B CG    1 
ATOM   6930  C  CD    . GLU B 1 166 ? 136.215 151.091 149.079 1.00 42.78 ?  166 GLU B CD    1 
ATOM   6931  O  OE1   . GLU B 1 166 ? 135.568 151.286 150.130 1.00 47.42 ?  166 GLU B OE1   1 
ATOM   6932  O  OE2   . GLU B 1 166 ? 136.883 151.982 148.516 1.00 39.22 -1 166 GLU B OE2   1 
ATOM   6933  N  N     . LEU B 1 167 ? 136.453 148.837 152.679 1.00 30.71 ?  167 LEU B N     1 
ATOM   6934  C  CA    . LEU B 1 167 ? 136.011 148.424 154.003 1.00 23.73 ?  167 LEU B CA    1 
ATOM   6935  C  C     . LEU B 1 167 ? 134.574 147.925 154.021 1.00 29.03 ?  167 LEU B C     1 
ATOM   6936  O  O     . LEU B 1 167 ? 134.146 147.361 155.034 1.00 30.76 ?  167 LEU B O     1 
ATOM   6937  C  CB    . LEU B 1 167 ? 136.156 149.582 154.992 1.00 30.06 ?  167 LEU B CB    1 
ATOM   6938  C  CG    . LEU B 1 167 ? 137.544 150.204 155.157 1.00 26.48 ?  167 LEU B CG    1 
ATOM   6939  C  CD1   . LEU B 1 167 ? 137.603 150.983 156.450 1.00 27.89 ?  167 LEU B CD1   1 
ATOM   6940  C  CD2   . LEU B 1 167 ? 138.626 149.143 155.132 1.00 26.02 ?  167 LEU B CD2   1 
ATOM   6941  N  N     . VAL B 1 168 ? 133.825 148.116 152.941 1.00 29.42 ?  168 VAL B N     1 
ATOM   6942  C  CA    . VAL B 1 168 ? 132.443 147.657 152.879 1.00 22.91 ?  168 VAL B CA    1 
ATOM   6943  C  C     . VAL B 1 168 ? 132.424 146.197 152.454 1.00 26.85 ?  168 VAL B C     1 
ATOM   6944  O  O     . VAL B 1 168 ? 133.083 145.810 151.481 1.00 28.67 ?  168 VAL B O     1 
ATOM   6945  C  CB    . VAL B 1 168 ? 131.621 148.528 151.917 1.00 27.41 ?  168 VAL B CB    1 
ATOM   6946  C  CG1   . VAL B 1 168 ? 130.150 148.163 152.006 1.00 28.93 ?  168 VAL B CG1   1 
ATOM   6947  C  CG2   . VAL B 1 168 ? 131.828 149.997 152.230 1.00 27.27 ?  168 VAL B CG2   1 
ATOM   6948  N  N     . SER B 1 169 ? 131.667 145.379 153.187 1.00 35.86 ?  169 SER B N     1 
ATOM   6949  C  CA    . SER B 1 169 ? 131.640 143.946 152.923 1.00 37.59 ?  169 SER B CA    1 
ATOM   6950  C  C     . SER B 1 169 ? 130.708 143.603 151.765 1.00 36.82 ?  169 SER B C     1 
ATOM   6951  O  O     . SER B 1 169 ? 131.094 142.879 150.842 1.00 34.09 ?  169 SER B O     1 
ATOM   6952  C  CB    . SER B 1 169 ? 131.223 143.191 154.186 1.00 31.71 ?  169 SER B CB    1 
ATOM   6953  O  OG    . SER B 1 169 ? 131.267 141.789 153.982 1.00 34.78 ?  169 SER B OG    1 
ATOM   6954  N  N     . CYS B 1 170 ? 129.479 144.111 151.798 1.00 31.77 ?  170 CYS B N     1 
ATOM   6955  C  CA    . CYS B 1 170 ? 128.438 143.699 150.869 1.00 26.64 ?  170 CYS B CA    1 
ATOM   6956  C  C     . CYS B 1 170 ? 127.917 144.890 150.078 1.00 25.35 ?  170 CYS B C     1 
ATOM   6957  O  O     . CYS B 1 170 ? 127.826 146.006 150.599 1.00 24.91 ?  170 CYS B O     1 
ATOM   6958  C  CB    . CYS B 1 170 ? 127.282 143.026 151.615 1.00 34.42 ?  170 CYS B CB    1 
ATOM   6959  S  SG    . CYS B 1 170 ? 126.667 143.972 153.024 1.00 53.61 ?  170 CYS B SG    1 
ATOM   6960  N  N     . PHE B 1 171 ? 127.578 144.638 148.815 1.00 22.77 ?  171 PHE B N     1 
ATOM   6961  C  CA    . PHE B 1 171 ? 126.970 145.628 147.940 1.00 13.83 ?  171 PHE B CA    1 
ATOM   6962  C  C     . PHE B 1 171 ? 125.744 145.022 147.278 1.00 12.90 ?  171 PHE B C     1 
ATOM   6963  O  O     . PHE B 1 171 ? 125.753 143.848 146.894 1.00 24.47 ?  171 PHE B O     1 
ATOM   6964  C  CB    . PHE B 1 171 ? 127.948 146.111 146.868 1.00 16.07 ?  171 PHE B CB    1 
ATOM   6965  C  CG    . PHE B 1 171 ? 129.260 146.581 147.414 1.00 19.04 ?  171 PHE B CG    1 
ATOM   6966  C  CD1   . PHE B 1 171 ? 129.387 147.849 147.948 1.00 15.01 ?  171 PHE B CD1   1 
ATOM   6967  C  CD2   . PHE B 1 171 ? 130.370 145.755 147.387 1.00 18.02 ?  171 PHE B CD2   1 
ATOM   6968  C  CE1   . PHE B 1 171 ? 130.592 148.281 148.450 1.00 13.11 ?  171 PHE B CE1   1 
ATOM   6969  C  CE2   . PHE B 1 171 ? 131.578 146.186 147.886 1.00 15.58 ?  171 PHE B CE2   1 
ATOM   6970  C  CZ    . PHE B 1 171 ? 131.690 147.451 148.418 1.00 15.68 ?  171 PHE B CZ    1 
ATOM   6971  N  N     . LEU B 1 172 ? 124.692 145.823 147.147 1.00 13.06 ?  172 LEU B N     1 
ATOM   6972  C  CA    . LEU B 1 172 ? 123.436 145.387 146.550 1.00 10.19 ?  172 LEU B CA    1 
ATOM   6973  C  C     . LEU B 1 172 ? 123.112 146.303 145.381 1.00 11.41 ?  172 LEU B C     1 
ATOM   6974  O  O     . LEU B 1 172 ? 123.012 147.521 145.556 1.00 17.26 ?  172 LEU B O     1 
ATOM   6975  C  CB    . LEU B 1 172 ? 122.303 145.406 147.577 1.00 13.81 ?  172 LEU B CB    1 
ATOM   6976  C  CG    . LEU B 1 172 ? 122.343 144.400 148.727 1.00 8.92  ?  172 LEU B CG    1 
ATOM   6977  C  CD1   . LEU B 1 172 ? 123.230 144.895 149.858 1.00 10.47 ?  172 LEU B CD1   1 
ATOM   6978  C  CD2   . LEU B 1 172 ? 120.939 144.154 149.227 1.00 10.66 ?  172 LEU B CD2   1 
ATOM   6979  N  N     . LEU B 1 173 ? 122.943 145.720 144.199 1.00 17.95 ?  173 LEU B N     1 
ATOM   6980  C  CA    . LEU B 1 173 ? 122.701 146.474 142.978 1.00 9.04  ?  173 LEU B CA    1 
ATOM   6981  C  C     . LEU B 1 173 ? 121.304 146.193 142.443 1.00 14.71 ?  173 LEU B C     1 
ATOM   6982  O  O     . LEU B 1 173 ? 120.845 145.048 142.442 1.00 20.11 ?  173 LEU B O     1 
ATOM   6983  C  CB    . LEU B 1 173 ? 123.732 146.133 141.901 1.00 13.46 ?  173 LEU B CB    1 
ATOM   6984  C  CG    . LEU B 1 173 ? 125.213 146.195 142.269 1.00 18.36 ?  173 LEU B CG    1 
ATOM   6985  C  CD1   . LEU B 1 173 ? 126.054 145.841 141.056 1.00 21.69 ?  173 LEU B CD1   1 
ATOM   6986  C  CD2   . LEU B 1 173 ? 125.580 147.570 142.801 1.00 20.29 ?  173 LEU B CD2   1 
ATOM   6987  N  N     . GLU B 1 174 ? 120.635 147.249 141.992 1.00 23.41 ?  174 GLU B N     1 
ATOM   6988  C  CA    . GLU B 1 174 ? 119.378 147.124 141.270 1.00 20.21 ?  174 GLU B CA    1 
ATOM   6989  C  C     . GLU B 1 174 ? 119.659 147.198 139.776 1.00 18.27 ?  174 GLU B C     1 
ATOM   6990  O  O     . GLU B 1 174 ? 120.293 148.147 139.305 1.00 27.43 ?  174 GLU B O     1 
ATOM   6991  C  CB    . GLU B 1 174 ? 118.404 148.226 141.684 1.00 23.89 ?  174 GLU B CB    1 
ATOM   6992  C  CG    . GLU B 1 174 ? 117.759 148.016 143.041 1.00 18.30 ?  174 GLU B CG    1 
ATOM   6993  C  CD    . GLU B 1 174 ? 116.256 147.851 142.950 1.00 21.69 ?  174 GLU B CD    1 
ATOM   6994  O  OE1   . GLU B 1 174 ? 115.783 147.240 141.971 1.00 28.18 ?  174 GLU B OE1   1 
ATOM   6995  O  OE2   . GLU B 1 174 ? 115.549 148.334 143.857 1.00 24.53 -1 174 GLU B OE2   1 
ATOM   6996  N  N     . VAL B 1 175 ? 119.188 146.200 139.034 1.00 16.95 ?  175 VAL B N     1 
ATOM   6997  C  CA    . VAL B 1 175 ? 119.427 146.099 137.599 1.00 18.41 ?  175 VAL B CA    1 
ATOM   6998  C  C     . VAL B 1 175 ? 118.130 146.433 136.876 1.00 17.16 ?  175 VAL B C     1 
ATOM   6999  O  O     . VAL B 1 175 ? 117.131 145.717 137.012 1.00 13.81 ?  175 VAL B O     1 
ATOM   7000  C  CB    . VAL B 1 175 ? 119.932 144.703 137.206 1.00 19.90 ?  175 VAL B CB    1 
ATOM   7001  C  CG1   . VAL B 1 175 ? 120.568 144.735 135.824 1.00 14.27 ?  175 VAL B CG1   1 
ATOM   7002  C  CG2   . VAL B 1 175 ? 120.914 144.186 138.242 1.00 14.16 ?  175 VAL B CG2   1 
ATOM   7003  N  N     . ASN B 1 176 ? 118.147 147.518 136.107 1.00 18.38 ?  176 ASN B N     1 
ATOM   7004  C  CA    . ASN B 1 176 ? 116.990 147.895 135.314 1.00 19.52 ?  176 ASN B CA    1 
ATOM   7005  C  C     . ASN B 1 176 ? 116.908 147.040 134.052 1.00 20.93 ?  176 ASN B C     1 
ATOM   7006  O  O     . ASN B 1 176 ? 117.887 146.430 133.616 1.00 19.66 ?  176 ASN B O     1 
ATOM   7007  C  CB    . ASN B 1 176 ? 117.043 149.377 134.946 1.00 18.09 ?  176 ASN B CB    1 
ATOM   7008  C  CG    . ASN B 1 176 ? 115.682 150.032 134.976 1.00 19.52 ?  176 ASN B CG    1 
ATOM   7009  O  OD1   . ASN B 1 176 ? 114.655 149.357 134.968 1.00 27.15 ?  176 ASN B OD1   1 
ATOM   7010  N  ND2   . ASN B 1 176 ? 115.665 151.359 135.011 1.00 21.83 ?  176 ASN B ND2   1 
ATOM   7011  N  N     . ASP B 1 177 ? 115.714 147.011 133.461 1.00 25.27 ?  177 ASP B N     1 
ATOM   7012  C  CA    . ASP B 1 177 ? 115.427 146.147 132.317 1.00 22.19 ?  177 ASP B CA    1 
ATOM   7013  C  C     . ASP B 1 177 ? 115.882 146.841 131.035 1.00 23.70 ?  177 ASP B C     1 
ATOM   7014  O  O     . ASP B 1 177 ? 115.095 147.420 130.281 1.00 26.99 ?  177 ASP B O     1 
ATOM   7015  C  CB    . ASP B 1 177 ? 113.945 145.800 132.275 1.00 18.71 ?  177 ASP B CB    1 
ATOM   7016  C  CG    . ASP B 1 177 ? 113.590 144.896 131.119 1.00 26.22 ?  177 ASP B CG    1 
ATOM   7017  O  OD1   . ASP B 1 177 ? 114.401 144.007 130.786 1.00 30.83 ?  177 ASP B OD1   1 
ATOM   7018  O  OD2   . ASP B 1 177 ? 112.498 145.075 130.542 1.00 29.50 -1 177 ASP B OD2   1 
ATOM   7019  N  N     . SER B 1 178 ? 117.189 146.777 130.788 1.00 19.01 ?  178 SER B N     1 
ATOM   7020  C  CA    . SER B 1 178 ? 117.765 147.321 129.568 1.00 18.37 ?  178 SER B CA    1 
ATOM   7021  C  C     . SER B 1 178 ? 119.160 146.743 129.381 1.00 16.76 ?  178 SER B C     1 
ATOM   7022  O  O     . SER B 1 178 ? 119.810 146.337 130.347 1.00 23.35 ?  178 SER B O     1 
ATOM   7023  C  CB    . SER B 1 178 ? 117.820 148.852 129.599 1.00 14.28 ?  178 SER B CB    1 
ATOM   7024  O  OG    . SER B 1 178 ? 119.049 149.311 130.128 1.00 19.63 ?  178 SER B OG    1 
ATOM   7025  N  N     . LEU B 1 179 ? 119.605 146.703 128.123 1.00 23.99 ?  179 LEU B N     1 
ATOM   7026  C  CA    . LEU B 1 179 ? 120.951 146.219 127.831 1.00 19.15 ?  179 LEU B CA    1 
ATOM   7027  C  C     . LEU B 1 179 ? 122.009 147.136 128.429 1.00 14.42 ?  179 LEU B C     1 
ATOM   7028  O  O     . LEU B 1 179 ? 123.032 146.665 128.938 1.00 18.64 ?  179 LEU B O     1 
ATOM   7029  C  CB    . LEU B 1 179 ? 121.151 146.088 126.321 1.00 20.55 ?  179 LEU B CB    1 
ATOM   7030  C  CG    . LEU B 1 179 ? 122.487 145.485 125.886 1.00 17.53 ?  179 LEU B CG    1 
ATOM   7031  C  CD1   . LEU B 1 179 ? 122.602 144.042 126.359 1.00 14.12 ?  179 LEU B CD1   1 
ATOM   7032  C  CD2   . LEU B 1 179 ? 122.658 145.579 124.382 1.00 15.45 ?  179 LEU B CD2   1 
ATOM   7033  N  N     . ASN B 1 180 ? 121.786 148.451 128.364 1.00 18.45 ?  180 ASN B N     1 
ATOM   7034  C  CA    . ASN B 1 180 ? 122.714 149.390 128.982 1.00 19.17 ?  180 ASN B CA    1 
ATOM   7035  C  C     . ASN B 1 180 ? 122.810 149.152 130.482 1.00 19.71 ?  180 ASN B C     1 
ATOM   7036  O  O     . ASN B 1 180 ? 123.910 149.127 131.047 1.00 23.44 ?  180 ASN B O     1 
ATOM   7037  C  CB    . ASN B 1 180 ? 122.274 150.826 128.699 1.00 18.93 ?  180 ASN B CB    1 
ATOM   7038  C  CG    . ASN B 1 180 ? 122.647 151.288 127.308 1.00 24.64 ?  180 ASN B CG    1 
ATOM   7039  O  OD1   . ASN B 1 180 ? 123.553 150.741 126.681 1.00 31.55 ?  180 ASN B OD1   1 
ATOM   7040  N  ND2   . ASN B 1 180 ? 121.945 152.300 126.814 1.00 25.83 ?  180 ASN B ND2   1 
ATOM   7041  N  N     . ASP B 1 181 ? 121.666 148.957 131.137 1.00 19.83 ?  181 ASP B N     1 
ATOM   7042  C  CA    . ASP B 1 181 ? 121.663 148.714 132.574 1.00 15.41 ?  181 ASP B CA    1 
ATOM   7043  C  C     . ASP B 1 181 ? 122.289 147.367 132.913 1.00 14.51 ?  181 ASP B C     1 
ATOM   7044  O  O     . ASP B 1 181 ? 122.982 147.242 133.926 1.00 25.19 ?  181 ASP B O     1 
ATOM   7045  C  CB    . ASP B 1 181 ? 120.237 148.802 133.113 1.00 21.97 ?  181 ASP B CB    1 
ATOM   7046  C  CG    . ASP B 1 181 ? 119.689 150.215 133.073 1.00 24.91 ?  181 ASP B CG    1 
ATOM   7047  O  OD1   . ASP B 1 181 ? 120.172 151.061 133.854 1.00 24.60 ?  181 ASP B OD1   1 
ATOM   7048  O  OD2   . ASP B 1 181 ? 118.776 150.480 132.265 1.00 29.14 -1 181 ASP B OD2   1 
ATOM   7049  N  N     . ILE B 1 182 ? 122.062 146.351 132.080 1.00 15.82 ?  182 ILE B N     1 
ATOM   7050  C  CA    . ILE B 1 182 ? 122.666 145.042 132.322 1.00 17.64 ?  182 ILE B CA    1 
ATOM   7051  C  C     . ILE B 1 182 ? 124.185 145.123 132.205 1.00 17.43 ?  182 ILE B C     1 
ATOM   7052  O  O     . ILE B 1 182 ? 124.920 144.584 133.042 1.00 21.16 ?  182 ILE B O     1 
ATOM   7053  C  CB    . ILE B 1 182 ? 122.080 143.997 131.354 1.00 18.63 ?  182 ILE B CB    1 
ATOM   7054  C  CG1   . ILE B 1 182 ? 120.701 143.543 131.835 1.00 15.17 ?  182 ILE B CG1   1 
ATOM   7055  C  CG2   . ILE B 1 182 ? 123.011 142.804 131.214 1.00 20.80 ?  182 ILE B CG2   1 
ATOM   7056  C  CD1   . ILE B 1 182 ? 119.919 142.785 130.796 1.00 16.89 ?  182 ILE B CD1   1 
ATOM   7057  N  N     . SER B 1 183 ? 124.676 145.798 131.164 1.00 17.86 ?  183 SER B N     1 
ATOM   7058  C  CA    . SER B 1 183 ? 126.117 145.951 130.993 1.00 18.73 ?  183 SER B CA    1 
ATOM   7059  C  C     . SER B 1 183 ? 126.723 146.769 132.125 1.00 21.57 ?  183 SER B C     1 
ATOM   7060  O  O     . SER B 1 183 ? 127.810 146.446 132.620 1.00 28.03 ?  183 SER B O     1 
ATOM   7061  C  CB    . SER B 1 183 ? 126.416 146.592 129.640 1.00 15.98 ?  183 SER B CB    1 
ATOM   7062  O  OG    . SER B 1 183 ? 125.783 147.852 129.524 1.00 30.83 ?  183 SER B OG    1 
ATOM   7063  N  N     . ARG B 1 184 ? 126.033 147.829 132.555 1.00 18.88 ?  184 ARG B N     1 
ATOM   7064  C  CA    . ARG B 1 184 ? 126.523 148.612 133.683 1.00 16.57 ?  184 ARG B CA    1 
ATOM   7065  C  C     . ARG B 1 184 ? 126.539 147.786 134.962 1.00 25.25 ?  184 ARG B C     1 
ATOM   7066  O  O     . ARG B 1 184 ? 127.450 147.923 135.781 1.00 29.17 ?  184 ARG B O     1 
ATOM   7067  C  CB    . ARG B 1 184 ? 125.672 149.866 133.867 1.00 15.37 ?  184 ARG B CB    1 
ATOM   7068  C  CG    . ARG B 1 184 ? 126.274 150.865 134.839 1.00 24.71 ?  184 ARG B CG    1 
ATOM   7069  C  CD    . ARG B 1 184 ? 127.682 151.251 134.428 1.00 24.41 ?  184 ARG B CD    1 
ATOM   7070  N  NE    . ARG B 1 184 ? 127.681 152.289 133.406 1.00 31.42 ?  184 ARG B NE    1 
ATOM   7071  C  CZ    . ARG B 1 184 ? 128.769 152.903 132.961 1.00 33.23 ?  184 ARG B CZ    1 
ATOM   7072  N  NH1   . ARG B 1 184 ? 129.972 152.590 133.413 1.00 27.36 1  184 ARG B NH1   1 
ATOM   7073  N  NH2   . ARG B 1 184 ? 128.646 153.853 132.039 1.00 28.64 ?  184 ARG B NH2   1 
ATOM   7074  N  N     . ALA B 1 185 ? 125.535 146.928 135.154 1.00 22.10 ?  185 ALA B N     1 
ATOM   7075  C  CA    . ALA B 1 185 ? 125.514 146.060 136.324 1.00 11.35 ?  185 ALA B CA    1 
ATOM   7076  C  C     . ALA B 1 185 ? 126.676 145.080 136.301 1.00 15.81 ?  185 ALA B C     1 
ATOM   7077  O  O     . ALA B 1 185 ? 127.300 144.823 137.334 1.00 20.15 ?  185 ALA B O     1 
ATOM   7078  C  CB    . ALA B 1 185 ? 124.185 145.313 136.403 1.00 15.68 ?  185 ALA B CB    1 
ATOM   7079  N  N     . ILE B 1 186 ? 126.980 144.519 135.128 1.00 24.17 ?  186 ILE B N     1 
ATOM   7080  C  CA    . ILE B 1 186 ? 128.134 143.628 135.008 1.00 21.97 ?  186 ILE B CA    1 
ATOM   7081  C  C     . ILE B 1 186 ? 129.420 144.378 135.337 1.00 20.56 ?  186 ILE B C     1 
ATOM   7082  O  O     . ILE B 1 186 ? 130.284 143.876 136.073 1.00 26.55 ?  186 ILE B O     1 
ATOM   7083  C  CB    . ILE B 1 186 ? 128.186 143.009 133.599 1.00 26.98 ?  186 ILE B CB    1 
ATOM   7084  C  CG1   . ILE B 1 186 ? 126.989 142.088 133.370 1.00 20.24 ?  186 ILE B CG1   1 
ATOM   7085  C  CG2   . ILE B 1 186 ? 129.485 142.250 133.393 1.00 22.94 ?  186 ILE B CG2   1 
ATOM   7086  C  CD1   . ILE B 1 186 ? 126.665 141.876 131.910 1.00 23.18 ?  186 ILE B CD1   1 
ATOM   7087  N  N     . ASP B 1 187 ? 129.563 145.592 134.801 1.00 22.65 ?  187 ASP B N     1 
ATOM   7088  C  CA    . ASP B 1 187 ? 130.755 146.391 135.066 1.00 21.24 ?  187 ASP B CA    1 
ATOM   7089  C  C     . ASP B 1 187 ? 130.895 146.700 136.553 1.00 23.70 ?  187 ASP B C     1 
ATOM   7090  O  O     . ASP B 1 187 ? 131.978 146.559 137.128 1.00 29.52 ?  187 ASP B O     1 
ATOM   7091  C  CB    . ASP B 1 187 ? 130.704 147.684 134.252 1.00 21.82 ?  187 ASP B CB    1 
ATOM   7092  C  CG    . ASP B 1 187 ? 131.672 148.734 134.759 1.00 30.86 ?  187 ASP B CG    1 
ATOM   7093  O  OD1   . ASP B 1 187 ? 132.875 148.426 134.891 1.00 30.90 ?  187 ASP B OD1   1 
ATOM   7094  O  OD2   . ASP B 1 187 ? 131.230 149.870 135.028 1.00 35.86 -1 187 ASP B OD2   1 
ATOM   7095  N  N     . ILE B 1 188 ? 129.800 147.117 137.191 1.00 21.60 ?  188 ILE B N     1 
ATOM   7096  C  CA    . ILE B 1 188 ? 129.843 147.474 138.605 1.00 19.74 ?  188 ILE B CA    1 
ATOM   7097  C  C     . ILE B 1 188 ? 130.106 146.241 139.461 1.00 21.48 ?  188 ILE B C     1 
ATOM   7098  O  O     . ILE B 1 188 ? 130.804 146.315 140.477 1.00 28.68 ?  188 ILE B O     1 
ATOM   7099  C  CB    . ILE B 1 188 ? 128.541 148.188 139.014 1.00 21.13 ?  188 ILE B CB    1 
ATOM   7100  C  CG1   . ILE B 1 188 ? 128.411 149.522 138.278 1.00 22.43 ?  188 ILE B CG1   1 
ATOM   7101  C  CG2   . ILE B 1 188 ? 128.507 148.436 140.506 1.00 23.49 ?  188 ILE B CG2   1 
ATOM   7102  C  CD1   . ILE B 1 188 ? 127.055 150.170 138.428 1.00 18.85 ?  188 ILE B CD1   1 
ATOM   7103  N  N     . SER B 1 189 ? 129.556 145.090 139.068 1.00 17.21 ?  189 SER B N     1 
ATOM   7104  C  CA    . SER B 1 189 ? 129.831 143.856 139.791 1.00 10.40 ?  189 SER B CA    1 
ATOM   7105  C  C     . SER B 1 189 ? 131.308 143.499 139.720 1.00 22.08 ?  189 SER B C     1 
ATOM   7106  O  O     . SER B 1 189 ? 131.912 143.127 140.732 1.00 23.66 ?  189 SER B O     1 
ATOM   7107  C  CB    . SER B 1 189 ? 128.976 142.720 139.231 1.00 18.67 ?  189 SER B CB    1 
ATOM   7108  O  OG    . SER B 1 189 ? 127.603 143.054 139.266 1.00 25.30 ?  189 SER B OG    1 
ATOM   7109  N  N     . MET B 1 190 ? 131.912 143.615 138.533 1.00 27.49 ?  190 MET B N     1 
ATOM   7110  C  CA    . MET B 1 190 ? 133.345 143.359 138.420 1.00 19.93 ?  190 MET B CA    1 
ATOM   7111  C  C     . MET B 1 190 ? 134.152 144.360 139.238 1.00 19.96 ?  190 MET B C     1 
ATOM   7112  O  O     . MET B 1 190 ? 135.138 143.992 139.883 1.00 24.18 ?  190 MET B O     1 
ATOM   7113  C  CB    . MET B 1 190 ? 133.786 143.389 136.957 1.00 20.87 ?  190 MET B CB    1 
ATOM   7114  C  CG    . MET B 1 190 ? 133.206 142.277 136.109 1.00 22.70 ?  190 MET B CG    1 
ATOM   7115  S  SD    . MET B 1 190 ? 133.962 142.196 134.476 1.00 37.29 ?  190 MET B SD    1 
ATOM   7116  C  CE    . MET B 1 190 ? 132.958 143.371 133.574 1.00 24.55 ?  190 MET B CE    1 
ATOM   7117  N  N     . GLN B 1 191 ? 133.747 145.632 139.223 1.00 19.21 ?  191 GLN B N     1 
ATOM   7118  C  CA    . GLN B 1 191 ? 134.475 146.650 139.976 1.00 23.96 ?  191 GLN B CA    1 
ATOM   7119  C  C     . GLN B 1 191 ? 134.410 146.389 141.476 1.00 23.51 ?  191 GLN B C     1 
ATOM   7120  O  O     . GLN B 1 191 ? 135.412 146.541 142.183 1.00 29.80 ?  191 GLN B O     1 
ATOM   7121  C  CB    . GLN B 1 191 ? 133.925 148.040 139.657 1.00 21.47 ?  191 GLN B CB    1 
ATOM   7122  C  CG    . GLN B 1 191 ? 134.144 148.494 138.225 1.00 20.65 ?  191 GLN B CG    1 
ATOM   7123  C  CD    . GLN B 1 191 ? 135.610 148.649 137.875 1.00 26.80 ?  191 GLN B CD    1 
ATOM   7124  O  OE1   . GLN B 1 191 ? 136.454 148.844 138.749 1.00 30.50 ?  191 GLN B OE1   1 
ATOM   7125  N  NE2   . GLN B 1 191 ? 135.919 148.568 136.587 1.00 25.97 ?  191 GLN B NE2   1 
ATOM   7126  N  N     . LEU B 1 192 ? 133.239 146.002 141.980 1.00 23.86 ?  192 LEU B N     1 
ATOM   7127  C  CA    . LEU B 1 192 ? 133.083 145.777 143.412 1.00 18.39 ?  192 LEU B CA    1 
ATOM   7128  C  C     . LEU B 1 192 ? 133.696 144.458 143.860 1.00 22.39 ?  192 LEU B C     1 
ATOM   7129  O  O     . LEU B 1 192 ? 134.165 144.359 144.999 1.00 33.29 ?  192 LEU B O     1 
ATOM   7130  C  CB    . LEU B 1 192 ? 131.605 145.836 143.795 1.00 19.17 ?  192 LEU B CB    1 
ATOM   7131  C  CG    . LEU B 1 192 ? 130.936 147.204 143.648 1.00 20.72 ?  192 LEU B CG    1 
ATOM   7132  C  CD1   . LEU B 1 192 ? 129.428 147.074 143.745 1.00 20.16 ?  192 LEU B CD1   1 
ATOM   7133  C  CD2   . LEU B 1 192 ? 131.463 148.178 144.688 1.00 21.42 ?  192 LEU B CD2   1 
ATOM   7134  N  N     . SER B 1 193 ? 133.698 143.435 143.001 1.00 19.80 ?  193 SER B N     1 
ATOM   7135  C  CA    . SER B 1 193 ? 134.428 142.215 143.321 1.00 22.09 ?  193 SER B CA    1 
ATOM   7136  C  C     . SER B 1 193 ? 135.930 142.450 143.287 1.00 27.73 ?  193 SER B C     1 
ATOM   7137  O  O     . SER B 1 193 ? 136.675 141.816 144.042 1.00 36.62 ?  193 SER B O     1 
ATOM   7138  C  CB    . SER B 1 193 ? 134.041 141.099 142.356 1.00 24.90 ?  193 SER B CB    1 
ATOM   7139  O  OG    . SER B 1 193 ? 132.676 140.769 142.503 1.00 35.01 ?  193 SER B OG    1 
ATOM   7140  N  N     . LYS B 1 194 ? 136.387 143.346 142.413 1.00 29.29 ?  194 LYS B N     1 
ATOM   7141  C  CA    . LYS B 1 194 ? 137.777 143.779 142.444 1.00 29.16 ?  194 LYS B CA    1 
ATOM   7142  C  C     . LYS B 1 194 ? 138.105 144.445 143.774 1.00 35.14 ?  194 LYS B C     1 
ATOM   7143  O  O     . LYS B 1 194 ? 139.187 144.235 144.335 1.00 39.81 ?  194 LYS B O     1 
ATOM   7144  C  CB    . LYS B 1 194 ? 138.043 144.725 141.273 1.00 26.06 ?  194 LYS B CB    1 
ATOM   7145  C  CG    . LYS B 1 194 ? 139.318 145.532 141.374 1.00 33.46 ?  194 LYS B CG    1 
ATOM   7146  C  CD    . LYS B 1 194 ? 139.334 146.631 140.327 1.00 33.37 ?  194 LYS B CD    1 
ATOM   7147  C  CE    . LYS B 1 194 ? 140.690 147.309 140.251 1.00 34.95 ?  194 LYS B CE    1 
ATOM   7148  N  NZ    . LYS B 1 194 ? 140.699 148.416 139.256 1.00 35.12 1  194 LYS B NZ    1 
ATOM   7149  N  N     . LEU B 1 195 ? 137.175 145.246 144.298 1.00 30.45 ?  195 LEU B N     1 
ATOM   7150  C  CA    . LEU B 1 195 ? 137.336 145.856 145.611 1.00 29.84 ?  195 LEU B CA    1 
ATOM   7151  C  C     . LEU B 1 195 ? 137.200 144.852 146.747 1.00 31.64 ?  195 LEU B C     1 
ATOM   7152  O  O     . LEU B 1 195 ? 137.482 145.205 147.898 1.00 35.04 ?  195 LEU B O     1 
ATOM   7153  C  CB    . LEU B 1 195 ? 136.318 146.983 145.787 1.00 31.01 ?  195 LEU B CB    1 
ATOM   7154  C  CG    . LEU B 1 195 ? 136.493 148.171 144.837 1.00 32.60 ?  195 LEU B CG    1 
ATOM   7155  C  CD1   . LEU B 1 195 ? 135.351 149.161 144.988 1.00 32.68 ?  195 LEU B CD1   1 
ATOM   7156  C  CD2   . LEU B 1 195 ? 137.834 148.850 145.071 1.00 30.72 ?  195 LEU B CD2   1 
ATOM   7157  N  N     . GLY B 1 196 ? 136.772 143.622 146.461 1.00 31.68 ?  196 GLY B N     1 
ATOM   7158  C  CA    . GLY B 1 196 ? 136.703 142.571 147.451 1.00 32.64 ?  196 GLY B CA    1 
ATOM   7159  C  C     . GLY B 1 196 ? 135.333 142.333 148.051 1.00 33.71 ?  196 GLY B C     1 
ATOM   7160  O  O     . GLY B 1 196 ? 135.178 141.389 148.836 1.00 35.13 ?  196 GLY B O     1 
ATOM   7161  N  N     . GLY B 1 197 ? 134.340 143.148 147.710 1.00 30.62 ?  197 GLY B N     1 
ATOM   7162  C  CA    . GLY B 1 197 ? 133.037 143.016 148.325 1.00 26.25 ?  197 GLY B CA    1 
ATOM   7163  C  C     . GLY B 1 197 ? 132.128 142.050 147.588 1.00 22.65 ?  197 GLY B C     1 
ATOM   7164  O  O     . GLY B 1 197 ? 132.199 141.887 146.372 1.00 27.65 ?  197 GLY B O     1 
ATOM   7165  N  N     . GLY B 1 198 ? 131.255 141.398 148.354 1.00 19.98 ?  198 GLY B N     1 
ATOM   7166  C  CA    . GLY B 1 198 ? 130.243 140.535 147.770 1.00 16.72 ?  198 GLY B CA    1 
ATOM   7167  C  C     . GLY B 1 198 ? 129.119 141.368 147.184 1.00 17.83 ?  198 GLY B C     1 
ATOM   7168  O  O     . GLY B 1 198 ? 128.606 142.287 147.832 1.00 21.91 ?  198 GLY B O     1 
ATOM   7169  N  N     . VAL B 1 199 ? 128.733 141.050 145.953 1.00 20.11 ?  199 VAL B N     1 
ATOM   7170  C  CA    . VAL B 1 199 ? 127.781 141.847 145.190 1.00 12.78 ?  199 VAL B CA    1 
ATOM   7171  C  C     . VAL B 1 199 ? 126.492 141.055 145.033 1.00 7.15  ?  199 VAL B C     1 
ATOM   7172  O  O     . VAL B 1 199 ? 126.518 139.890 144.626 1.00 15.02 ?  199 VAL B O     1 
ATOM   7173  C  CB    . VAL B 1 199 ? 128.350 142.238 143.815 1.00 13.70 ?  199 VAL B CB    1 
ATOM   7174  C  CG1   . VAL B 1 199 ? 127.405 143.183 143.099 1.00 16.53 ?  199 VAL B CG1   1 
ATOM   7175  C  CG2   . VAL B 1 199 ? 129.725 142.855 143.969 1.00 11.69 ?  199 VAL B CG2   1 
ATOM   7176  N  N     . SER B 1 200 ? 125.369 141.690 145.355 1.00 13.20 ?  200 SER B N     1 
ATOM   7177  C  CA    . SER B 1 200 ? 124.046 141.122 145.154 1.00 3.98  ?  200 SER B CA    1 
ATOM   7178  C  C     . SER B 1 200 ? 123.291 141.968 144.140 1.00 13.16 ?  200 SER B C     1 
ATOM   7179  O  O     . SER B 1 200 ? 123.317 143.200 144.206 1.00 23.38 ?  200 SER B O     1 
ATOM   7180  C  CB    . SER B 1 200 ? 123.267 141.052 146.469 1.00 10.36 ?  200 SER B CB    1 
ATOM   7181  O  OG    . SER B 1 200 ? 122.164 140.171 146.362 1.00 15.93 ?  200 SER B OG    1 
ATOM   7182  N  N     . LEU B 1 201 ? 122.627 141.306 143.199 1.00 15.98 ?  201 LEU B N     1 
ATOM   7183  C  CA    . LEU B 1 201 ? 121.915 141.980 142.122 1.00 8.21  ?  201 LEU B CA    1 
ATOM   7184  C  C     . LEU B 1 201 ? 120.467 141.521 142.095 1.00 7.83  ?  201 LEU B C     1 
ATOM   7185  O  O     . LEU B 1 201 ? 120.191 140.318 142.106 1.00 14.96 ?  201 LEU B O     1 
ATOM   7186  C  CB    . LEU B 1 201 ? 122.580 141.709 140.771 1.00 14.50 ?  201 LEU B CB    1 
ATOM   7187  C  CG    . LEU B 1 201 ? 124.052 142.103 140.668 1.00 19.27 ?  201 LEU B CG    1 
ATOM   7188  C  CD1   . LEU B 1 201 ? 124.940 140.869 140.692 1.00 16.44 ?  201 LEU B CD1   1 
ATOM   7189  C  CD2   . LEU B 1 201 ? 124.297 142.928 139.417 1.00 17.08 ?  201 LEU B CD2   1 
ATOM   7190  N  N     . ASN B 1 202 ? 119.550 142.483 142.046 1.00 13.30 ?  202 ASN B N     1 
ATOM   7191  C  CA    . ASN B 1 202 ? 118.125 142.205 141.921 1.00 4.34  ?  202 ASN B CA    1 
ATOM   7192  C  C     . ASN B 1 202 ? 117.791 142.085 140.439 1.00 19.44 ?  202 ASN B C     1 
ATOM   7193  O  O     . ASN B 1 202 ? 117.873 143.066 139.695 1.00 25.78 ?  202 ASN B O     1 
ATOM   7194  C  CB    . ASN B 1 202 ? 117.300 143.304 142.583 1.00 8.57  ?  202 ASN B CB    1 
ATOM   7195  C  CG    . ASN B 1 202 ? 115.868 142.885 142.837 1.00 9.79  ?  202 ASN B CG    1 
ATOM   7196  O  OD1   . ASN B 1 202 ? 115.562 141.697 142.917 1.00 17.92 ?  202 ASN B OD1   1 
ATOM   7197  N  ND2   . ASN B 1 202 ? 114.979 143.862 142.963 1.00 12.16 ?  202 ASN B ND2   1 
ATOM   7198  N  N     . LEU B 1 203 ? 117.418 140.881 140.011 1.00 12.94 ?  203 LEU B N     1 
ATOM   7199  C  CA    . LEU B 1 203 ? 117.086 140.617 138.620 1.00 9.62  ?  203 LEU B CA    1 
ATOM   7200  C  C     . LEU B 1 203 ? 115.585 140.596 138.369 1.00 12.21 ?  203 LEU B C     1 
ATOM   7201  O  O     . LEU B 1 203 ? 115.153 140.174 137.292 1.00 17.15 ?  203 LEU B O     1 
ATOM   7202  C  CB    . LEU B 1 203 ? 117.711 139.293 138.175 1.00 15.46 ?  203 LEU B CB    1 
ATOM   7203  C  CG    . LEU B 1 203 ? 119.220 139.151 138.384 1.00 15.40 ?  203 LEU B CG    1 
ATOM   7204  C  CD1   . LEU B 1 203 ? 119.740 137.908 137.686 1.00 14.42 ?  203 LEU B CD1   1 
ATOM   7205  C  CD2   . LEU B 1 203 ? 119.957 140.387 137.896 1.00 15.77 ?  203 LEU B CD2   1 
ATOM   7206  N  N     . SER B 1 204 ? 114.782 141.047 139.335 1.00 15.54 ?  204 SER B N     1 
ATOM   7207  C  CA    . SER B 1 204 ? 113.333 140.975 139.208 1.00 10.71 ?  204 SER B CA    1 
ATOM   7208  C  C     . SER B 1 204 ? 112.773 141.977 138.207 1.00 20.34 ?  204 SER B C     1 
ATOM   7209  O  O     . SER B 1 204 ? 111.681 141.753 137.676 1.00 23.52 ?  204 SER B O     1 
ATOM   7210  C  CB    . SER B 1 204 ? 112.676 141.195 140.571 1.00 8.35  ?  204 SER B CB    1 
ATOM   7211  O  OG    . SER B 1 204 ? 113.162 140.267 141.523 1.00 20.64 ?  204 SER B OG    1 
ATOM   7212  N  N     . LYS B 1 205 ? 113.489 143.069 137.942 1.00 22.11 ?  205 LYS B N     1 
ATOM   7213  C  CA    . LYS B 1 205 ? 113.031 144.034 136.951 1.00 16.32 ?  205 LYS B CA    1 
ATOM   7214  C  C     . LYS B 1 205 ? 113.309 143.585 135.525 1.00 15.37 ?  205 LYS B C     1 
ATOM   7215  O  O     . LYS B 1 205 ? 112.606 144.021 134.608 1.00 26.69 ?  205 LYS B O     1 
ATOM   7216  C  CB    . LYS B 1 205 ? 113.681 145.395 137.200 1.00 18.23 ?  205 LYS B CB    1 
ATOM   7217  C  CG    . LYS B 1 205 ? 113.162 146.096 138.440 1.00 15.88 ?  205 LYS B CG    1 
ATOM   7218  C  CD    . LYS B 1 205 ? 113.784 147.468 138.601 1.00 21.18 ?  205 LYS B CD    1 
ATOM   7219  C  CE    . LYS B 1 205 ? 113.055 148.274 139.659 1.00 24.74 ?  205 LYS B CE    1 
ATOM   7220  N  NZ    . LYS B 1 205 ? 113.094 147.612 140.990 1.00 17.90 1  205 LYS B NZ    1 
ATOM   7221  N  N     . LEU B 1 206 ? 114.310 142.732 135.321 1.00 19.58 ?  206 LEU B N     1 
ATOM   7222  C  CA    . LEU B 1 206 ? 114.601 142.219 133.990 1.00 19.72 ?  206 LEU B CA    1 
ATOM   7223  C  C     . LEU B 1 206 ? 113.430 141.397 133.474 1.00 20.06 ?  206 LEU B C     1 
ATOM   7224  O  O     . LEU B 1 206 ? 112.879 140.559 134.195 1.00 24.64 ?  206 LEU B O     1 
ATOM   7225  C  CB    . LEU B 1 206 ? 115.868 141.368 134.020 1.00 19.51 ?  206 LEU B CB    1 
ATOM   7226  C  CG    . LEU B 1 206 ? 117.118 142.040 134.583 1.00 18.70 ?  206 LEU B CG    1 
ATOM   7227  C  CD1   . LEU B 1 206 ? 118.249 141.038 134.683 1.00 19.93 ?  206 LEU B CD1   1 
ATOM   7228  C  CD2   . LEU B 1 206 ? 117.518 143.217 133.718 1.00 22.12 ?  206 LEU B CD2   1 
ATOM   7229  N  N     . ARG B 1 207 ? 113.049 141.636 132.224 1.00 26.04 ?  207 ARG B N     1 
ATOM   7230  C  CA    . ARG B 1 207 ? 111.927 140.913 131.649 1.00 23.84 ?  207 ARG B CA    1 
ATOM   7231  C  C     . ARG B 1 207 ? 112.292 139.452 131.414 1.00 25.07 ?  207 ARG B C     1 
ATOM   7232  O  O     . ARG B 1 207 ? 113.452 139.104 131.175 1.00 30.59 ?  207 ARG B O     1 
ATOM   7233  C  CB    . ARG B 1 207 ? 111.472 141.569 130.346 1.00 22.30 ?  207 ARG B CB    1 
ATOM   7234  C  CG    . ARG B 1 207 ? 112.532 141.703 129.275 1.00 26.52 ?  207 ARG B CG    1 
ATOM   7235  C  CD    . ARG B 1 207 ? 112.021 142.573 128.138 1.00 24.61 ?  207 ARG B CD    1 
ATOM   7236  N  NE    . ARG B 1 207 ? 112.182 143.993 128.417 1.00 25.92 ?  207 ARG B NE    1 
ATOM   7237  C  CZ    . ARG B 1 207 ? 112.252 144.936 127.488 1.00 23.22 ?  207 ARG B CZ    1 
ATOM   7238  N  NH1   . ARG B 1 207 ? 112.158 144.647 126.201 1.00 26.34 1  207 ARG B NH1   1 
ATOM   7239  N  NH2   . ARG B 1 207 ? 112.419 146.202 127.859 1.00 20.80 ?  207 ARG B NH2   1 
ATOM   7240  N  N     . ALA B 1 208 ? 111.281 138.594 131.490 1.00 29.42 ?  208 ALA B N     1 
ATOM   7241  C  CA    . ALA B 1 208 ? 111.493 137.157 131.460 1.00 21.81 ?  208 ALA B CA    1 
ATOM   7242  C  C     . ALA B 1 208 ? 111.854 136.685 130.054 1.00 28.96 ?  208 ALA B C     1 
ATOM   7243  O  O     . ALA B 1 208 ? 111.894 137.456 129.092 1.00 34.82 ?  208 ALA B O     1 
ATOM   7244  C  CB    . ALA B 1 208 ? 110.252 136.426 131.963 1.00 23.95 ?  208 ALA B CB    1 
ATOM   7245  N  N     . LYS B 1 209 ? 112.131 135.388 129.950 1.00 28.19 ?  209 LYS B N     1 
ATOM   7246  C  CA    . LYS B 1 209 ? 112.430 134.782 128.662 1.00 24.45 ?  209 LYS B CA    1 
ATOM   7247  C  C     . LYS B 1 209 ? 111.193 134.793 127.773 1.00 31.93 ?  209 LYS B C     1 
ATOM   7248  O  O     . LYS B 1 209 ? 110.072 134.562 128.234 1.00 34.54 ?  209 LYS B O     1 
ATOM   7249  C  CB    . LYS B 1 209 ? 112.931 133.351 128.853 1.00 27.07 ?  209 LYS B CB    1 
ATOM   7250  C  CG    . LYS B 1 209 ? 113.611 132.764 127.629 1.00 32.28 ?  209 LYS B CG    1 
ATOM   7251  C  CD    . LYS B 1 209 ? 114.468 131.565 127.997 1.00 29.21 ?  209 LYS B CD    1 
ATOM   7252  C  CE    . LYS B 1 209 ? 113.615 130.351 128.328 1.00 32.67 ?  209 LYS B CE    1 
ATOM   7253  N  NZ    . LYS B 1 209 ? 112.387 130.287 127.489 1.00 33.89 1  209 LYS B NZ    1 
ATOM   7254  N  N     . GLY B 1 210 ? 111.404 135.063 126.487 1.00 35.25 ?  210 GLY B N     1 
ATOM   7255  C  CA    . GLY B 1 210 ? 110.301 135.124 125.553 1.00 34.69 ?  210 GLY B CA    1 
ATOM   7256  C  C     . GLY B 1 210 ? 109.556 136.438 125.534 1.00 35.24 ?  210 GLY B C     1 
ATOM   7257  O  O     . GLY B 1 210 ? 108.378 136.468 125.165 1.00 38.95 ?  210 GLY B O     1 
ATOM   7258  N  N     . GLU B 1 211 ? 110.204 137.528 125.927 1.00 33.78 ?  211 GLU B N     1 
ATOM   7259  C  CA    . GLU B 1 211 ? 109.610 138.853 125.865 1.00 33.10 ?  211 GLU B CA    1 
ATOM   7260  C  C     . GLU B 1 211 ? 110.142 139.613 124.652 1.00 37.21 ?  211 GLU B C     1 
ATOM   7261  O  O     . GLU B 1 211 ? 111.088 139.191 123.984 1.00 40.01 ?  211 GLU B O     1 
ATOM   7262  C  CB    . GLU B 1 211 ? 109.879 139.631 127.156 1.00 31.64 ?  211 GLU B CB    1 
ATOM   7263  C  CG    . GLU B 1 211 ? 109.219 139.023 128.378 1.00 33.93 ?  211 GLU B CG    1 
ATOM   7264  C  CD    . GLU B 1 211 ? 108.294 139.991 129.086 1.00 36.00 ?  211 GLU B CD    1 
ATOM   7265  O  OE1   . GLU B 1 211 ? 107.303 140.428 128.465 1.00 39.65 ?  211 GLU B OE1   1 
ATOM   7266  O  OE2   . GLU B 1 211 ? 108.547 140.305 130.266 1.00 32.33 -1 211 GLU B OE2   1 
ATOM   7267  N  N     . ALA B 1 212 ? 109.516 140.752 124.377 1.00 38.34 ?  212 ALA B N     1 
ATOM   7268  C  CA    . ALA B 1 212 ? 109.790 141.511 123.165 1.00 35.63 ?  212 ALA B CA    1 
ATOM   7269  C  C     . ALA B 1 212 ? 110.805 142.615 123.434 1.00 41.57 ?  212 ALA B C     1 
ATOM   7270  O  O     . ALA B 1 212 ? 110.686 143.353 124.417 1.00 44.34 ?  212 ALA B O     1 
ATOM   7271  C  CB    . ALA B 1 212 ? 108.500 142.110 122.606 1.00 38.46 ?  212 ALA B CB    1 
ATOM   7272  N  N     . ILE B 1 213 ? 111.802 142.717 122.560 1.00 40.74 ?  213 ILE B N     1 
ATOM   7273  C  CA    . ILE B 1 213 ? 112.753 143.822 122.561 1.00 43.49 ?  213 ILE B CA    1 
ATOM   7274  C  C     . ILE B 1 213 ? 112.408 144.698 121.363 1.00 41.50 ?  213 ILE B C     1 
ATOM   7275  O  O     . ILE B 1 213 ? 112.880 144.458 120.250 1.00 44.98 ?  213 ILE B O     1 
ATOM   7276  C  CB    . ILE B 1 213 ? 114.201 143.330 122.502 1.00 41.22 ?  213 ILE B CB    1 
ATOM   7277  C  CG1   . ILE B 1 213 ? 114.456 142.283 123.583 1.00 41.47 ?  213 ILE B CG1   1 
ATOM   7278  C  CG2   . ILE B 1 213 ? 115.166 144.497 122.649 1.00 38.15 ?  213 ILE B CG2   1 
ATOM   7279  C  CD1   . ILE B 1 213 ? 115.595 141.347 123.265 1.00 41.34 ?  213 ILE B CD1   1 
ATOM   7280  N  N     . LYS B 1 214 ? 111.591 145.723 121.595 1.00 46.02 ?  214 LYS B N     1 
ATOM   7281  C  CA    . LYS B 1 214 ? 111.119 146.630 120.547 1.00 46.63 ?  214 LYS B CA    1 
ATOM   7282  C  C     . LYS B 1 214 ? 110.362 145.875 119.454 1.00 52.94 ?  214 LYS B C     1 
ATOM   7283  O  O     . LYS B 1 214 ? 110.792 145.785 118.301 1.00 55.44 ?  214 LYS B O     1 
ATOM   7284  C  CB    . LYS B 1 214 ? 112.272 147.445 119.956 1.00 48.06 ?  214 LYS B CB    1 
ATOM   7285  C  CG    . LYS B 1 214 ? 112.360 148.863 120.495 1.00 49.74 ?  214 LYS B CG    1 
ATOM   7286  C  CD    . LYS B 1 214 ? 113.785 149.387 120.475 1.00 49.95 ?  214 LYS B CD    1 
ATOM   7287  C  CE    . LYS B 1 214 ? 114.544 148.909 119.247 1.00 48.13 ?  214 LYS B CE    1 
ATOM   7288  N  NZ    . LYS B 1 214 ? 116.017 148.928 119.461 1.00 51.60 1  214 LYS B NZ    1 
ATOM   7289  N  N     . ASP B 1 215 ? 109.230 145.294 119.861 1.00 54.72 ?  215 ASP B N     1 
ATOM   7290  C  CA    . ASP B 1 215 ? 108.190 144.802 118.961 1.00 56.27 ?  215 ASP B CA    1 
ATOM   7291  C  C     . ASP B 1 215 ? 108.546 143.500 118.250 1.00 55.86 ?  215 ASP B C     1 
ATOM   7292  O  O     . ASP B 1 215 ? 107.720 142.961 117.507 1.00 57.90 ?  215 ASP B O     1 
ATOM   7293  C  CB    . ASP B 1 215 ? 107.830 145.875 117.927 1.00 56.75 ?  215 ASP B CB    1 
ATOM   7294  C  CG    . ASP B 1 215 ? 106.864 146.909 118.472 1.00 58.77 ?  215 ASP B CG    1 
ATOM   7295  O  OD1   . ASP B 1 215 ? 105.685 146.562 118.694 1.00 57.83 ?  215 ASP B OD1   1 
ATOM   7296  O  OD2   . ASP B 1 215 ? 107.285 148.066 118.679 1.00 57.94 -1 215 ASP B OD2   1 
ATOM   7297  N  N     . VAL B 1 216 ? 109.752 142.977 118.460 1.00 49.80 ?  216 VAL B N     1 
ATOM   7298  C  CA    . VAL B 1 216 ? 110.084 141.636 117.978 1.00 49.24 ?  216 VAL B CA    1 
ATOM   7299  C  C     . VAL B 1 216 ? 109.960 140.702 119.180 1.00 51.37 ?  216 VAL B C     1 
ATOM   7300  O  O     . VAL B 1 216 ? 110.642 140.872 120.191 1.00 54.49 ?  216 VAL B O     1 
ATOM   7301  C  CB    . VAL B 1 216 ? 111.471 141.573 117.329 1.00 49.43 ?  216 VAL B CB    1 
ATOM   7302  C  CG1   . VAL B 1 216 ? 112.310 142.771 117.722 1.00 48.26 ?  216 VAL B CG1   1 
ATOM   7303  C  CG2   . VAL B 1 216 ? 112.184 140.258 117.649 1.00 49.08 ?  216 VAL B CG2   1 
ATOM   7304  N  N     . GLU B 1 217 ? 109.060 139.727 119.080 1.00 49.49 ?  217 GLU B N     1 
ATOM   7305  C  CA    . GLU B 1 217 ? 108.661 138.943 120.238 1.00 48.12 ?  217 GLU B CA    1 
ATOM   7306  C  C     . GLU B 1 217 ? 109.555 137.714 120.402 1.00 47.97 ?  217 GLU B C     1 
ATOM   7307  O  O     . GLU B 1 217 ? 110.282 137.307 119.491 1.00 49.55 ?  217 GLU B O     1 
ATOM   7308  C  CB    . GLU B 1 217 ? 107.198 138.522 120.113 1.00 49.89 ?  217 GLU B CB    1 
ATOM   7309  C  CG    . GLU B 1 217 ? 106.265 139.654 119.718 1.00 50.43 ?  217 GLU B CG    1 
ATOM   7310  C  CD    . GLU B 1 217 ? 105.845 140.502 120.900 1.00 53.17 ?  217 GLU B CD    1 
ATOM   7311  O  OE1   . GLU B 1 217 ? 105.946 140.017 122.047 1.00 52.28 ?  217 GLU B OE1   1 
ATOM   7312  O  OE2   . GLU B 1 217 ? 105.415 141.654 120.685 1.00 49.00 -1 217 GLU B OE2   1 
ATOM   7313  N  N     . ASN B 1 218 ? 109.477 137.120 121.592 1.00 43.64 ?  218 ASN B N     1 
ATOM   7314  C  CA    . ASN B 1 218 ? 110.246 135.928 121.952 1.00 41.92 ?  218 ASN B CA    1 
ATOM   7315  C  C     . ASN B 1 218 ? 111.733 136.139 121.693 1.00 45.22 ?  218 ASN B C     1 
ATOM   7316  O  O     . ASN B 1 218 ? 112.429 135.289 121.133 1.00 46.74 ?  218 ASN B O     1 
ATOM   7317  C  CB    . ASN B 1 218 ? 109.725 134.697 121.214 1.00 43.14 ?  218 ASN B CB    1 
ATOM   7318  C  CG    . ASN B 1 218 ? 108.782 133.868 122.060 1.00 46.85 ?  218 ASN B CG    1 
ATOM   7319  O  OD1   . ASN B 1 218 ? 107.740 134.351 122.503 1.00 45.77 ?  218 ASN B OD1   1 
ATOM   7320  N  ND2   . ASN B 1 218 ? 109.146 132.613 122.295 1.00 48.32 ?  218 ASN B ND2   1 
ATOM   7321  N  N     . ALA B 1 219 ? 112.223 137.298 122.121 1.00 37.53 ?  219 ALA B N     1 
ATOM   7322  C  CA    . ALA B 1 219 ? 113.586 137.730 121.843 1.00 35.07 ?  219 ALA B CA    1 
ATOM   7323  C  C     . ALA B 1 219 ? 114.495 137.709 123.060 1.00 37.31 ?  219 ALA B C     1 
ATOM   7324  O  O     . ALA B 1 219 ? 115.697 137.473 122.918 1.00 35.41 ?  219 ALA B O     1 
ATOM   7325  C  CB    . ALA B 1 219 ? 113.572 139.143 121.252 1.00 36.43 ?  219 ALA B CB    1 
ATOM   7326  N  N     . THR B 1 220 ? 113.957 137.950 124.251 1.00 34.97 ?  220 THR B N     1 
ATOM   7327  C  CA    . THR B 1 220 ? 114.781 138.045 125.446 1.00 31.02 ?  220 THR B CA    1 
ATOM   7328  C  C     . THR B 1 220 ? 115.268 136.672 125.890 1.00 34.50 ?  220 THR B C     1 
ATOM   7329  O  O     . THR B 1 220 ? 114.574 135.663 125.744 1.00 35.03 ?  220 THR B O     1 
ATOM   7330  C  CB    . THR B 1 220 ? 114.005 138.704 126.585 1.00 32.28 ?  220 THR B CB    1 
ATOM   7331  O  OG1   . THR B 1 220 ? 112.915 137.859 126.976 1.00 38.26 ?  220 THR B OG1   1 
ATOM   7332  C  CG2   . THR B 1 220 ? 113.458 140.039 126.139 1.00 32.74 ?  220 THR B CG2   1 
ATOM   7333  N  N     . LYS B 1 221 ? 116.481 136.649 126.436 1.00 32.78 ?  221 LYS B N     1 
ATOM   7334  C  CA    . LYS B 1 221 ? 117.033 135.450 127.047 1.00 29.71 ?  221 LYS B CA    1 
ATOM   7335  C  C     . LYS B 1 221 ? 116.573 135.257 128.483 1.00 31.82 ?  221 LYS B C     1 
ATOM   7336  O  O     . LYS B 1 221 ? 116.873 134.216 129.080 1.00 34.84 ?  221 LYS B O     1 
ATOM   7337  C  CB    . LYS B 1 221 ? 118.564 135.491 127.007 1.00 29.40 ?  221 LYS B CB    1 
ATOM   7338  C  CG    . LYS B 1 221 ? 119.147 135.290 125.626 1.00 30.09 ?  221 LYS B CG    1 
ATOM   7339  C  CD    . LYS B 1 221 ? 120.346 134.362 125.672 1.00 32.86 ?  221 LYS B CD    1 
ATOM   7340  C  CE    . LYS B 1 221 ? 120.803 133.996 124.274 1.00 35.04 ?  221 LYS B CE    1 
ATOM   7341  N  NZ    . LYS B 1 221 ? 119.751 134.283 123.262 1.00 32.52 1  221 LYS B NZ    1 
ATOM   7342  N  N     . GLY B 1 222 ? 115.858 136.223 129.046 1.00 31.02 ?  222 GLY B N     1 
ATOM   7343  C  CA    . GLY B 1 222 ? 115.409 136.126 130.413 1.00 27.64 ?  222 GLY B CA    1 
ATOM   7344  C  C     . GLY B 1 222 ? 116.510 136.447 131.404 1.00 28.06 ?  222 GLY B C     1 
ATOM   7345  O  O     . GLY B 1 222 ? 117.586 136.946 131.061 1.00 31.31 ?  222 GLY B O     1 
ATOM   7346  N  N     . VAL B 1 223 ? 116.220 136.149 132.672 1.00 27.28 ?  223 VAL B N     1 
ATOM   7347  C  CA    . VAL B 1 223 ? 117.191 136.407 133.726 1.00 25.17 ?  223 VAL B CA    1 
ATOM   7348  C  C     . VAL B 1 223 ? 118.320 135.389 133.717 1.00 20.16 ?  223 VAL B C     1 
ATOM   7349  O  O     . VAL B 1 223 ? 119.350 135.617 134.354 1.00 26.46 ?  223 VAL B O     1 
ATOM   7350  C  CB    . VAL B 1 223 ? 116.505 136.440 135.105 1.00 21.99 ?  223 VAL B CB    1 
ATOM   7351  C  CG1   . VAL B 1 223 ? 115.237 137.274 135.048 1.00 22.24 ?  223 VAL B CG1   1 
ATOM   7352  C  CG2   . VAL B 1 223 ? 116.206 135.030 135.593 1.00 22.98 ?  223 VAL B CG2   1 
ATOM   7353  N  N     . VAL B 1 224 ? 118.159 134.267 133.014 1.00 24.17 ?  224 VAL B N     1 
ATOM   7354  C  CA    . VAL B 1 224 ? 119.208 133.252 132.988 1.00 22.49 ?  224 VAL B CA    1 
ATOM   7355  C  C     . VAL B 1 224 ? 120.416 133.717 132.176 1.00 26.27 ?  224 VAL B C     1 
ATOM   7356  O  O     . VAL B 1 224 ? 121.562 133.437 132.548 1.00 30.84 ?  224 VAL B O     1 
ATOM   7357  C  CB    . VAL B 1 224 ? 118.643 131.923 132.458 1.00 27.68 ?  224 VAL B CB    1 
ATOM   7358  C  CG1   . VAL B 1 224 ? 119.755 130.907 132.256 1.00 27.23 ?  224 VAL B CG1   1 
ATOM   7359  C  CG2   . VAL B 1 224 ? 117.602 131.384 133.420 1.00 26.03 ?  224 VAL B CG2   1 
ATOM   7360  N  N     . GLY B 1 225 ? 120.197 134.426 131.067 1.00 22.82 ?  225 GLY B N     1 
ATOM   7361  C  CA    . GLY B 1 225 ? 121.323 134.966 130.318 1.00 18.39 ?  225 GLY B CA    1 
ATOM   7362  C  C     . GLY B 1 225 ? 122.103 136.000 131.109 1.00 21.88 ?  225 GLY B C     1 
ATOM   7363  O  O     . GLY B 1 225 ? 123.338 135.988 131.121 1.00 34.08 ?  225 GLY B O     1 
ATOM   7364  N  N     . VAL B 1 226 ? 121.391 136.904 131.784 1.00 19.13 ?  226 VAL B N     1 
ATOM   7365  C  CA    . VAL B 1 226 ? 122.048 137.869 132.658 1.00 19.93 ?  226 VAL B CA    1 
ATOM   7366  C  C     . VAL B 1 226 ? 122.751 137.155 133.799 1.00 19.06 ?  226 VAL B C     1 
ATOM   7367  O  O     . VAL B 1 226 ? 123.817 137.586 134.251 1.00 23.03 ?  226 VAL B O     1 
ATOM   7368  C  CB    . VAL B 1 226 ? 121.029 138.899 133.180 1.00 17.08 ?  226 VAL B CB    1 
ATOM   7369  C  CG1   . VAL B 1 226 ? 121.746 140.092 133.795 1.00 22.26 ?  226 VAL B CG1   1 
ATOM   7370  C  CG2   . VAL B 1 226 ? 120.109 139.338 132.061 1.00 16.72 ?  226 VAL B CG2   1 
ATOM   7371  N  N     . MET B 1 227 ? 122.169 136.057 134.284 1.00 22.71 ?  227 MET B N     1 
ATOM   7372  C  CA    . MET B 1 227 ? 122.810 135.262 135.324 1.00 21.23 ?  227 MET B CA    1 
ATOM   7373  C  C     . MET B 1 227 ? 124.129 134.681 134.840 1.00 21.57 ?  227 MET B C     1 
ATOM   7374  O  O     . MET B 1 227 ? 125.120 134.683 135.572 1.00 27.55 ?  227 MET B O     1 
ATOM   7375  C  CB    . MET B 1 227 ? 121.872 134.145 135.770 1.00 20.01 ?  227 MET B CB    1 
ATOM   7376  C  CG    . MET B 1 227 ? 120.932 134.527 136.886 1.00 16.03 ?  227 MET B CG    1 
ATOM   7377  S  SD    . MET B 1 227 ? 119.999 133.099 137.447 1.00 40.04 ?  227 MET B SD    1 
ATOM   7378  C  CE    . MET B 1 227 ? 120.820 132.795 138.999 1.00 24.27 ?  227 MET B CE    1 
ATOM   7379  N  N     . LYS B 1 228 ? 124.154 134.166 133.611 1.00 22.19 ?  228 LYS B N     1 
ATOM   7380  C  CA    . LYS B 1 228 ? 125.395 133.636 133.053 1.00 22.43 ?  228 LYS B CA    1 
ATOM   7381  C  C     . LYS B 1 228 ? 126.432 134.738 132.878 1.00 22.93 ?  228 LYS B C     1 
ATOM   7382  O  O     . LYS B 1 228 ? 127.621 134.540 133.169 1.00 23.93 ?  228 LYS B O     1 
ATOM   7383  C  CB    . LYS B 1 228 ? 125.117 132.946 131.719 1.00 24.69 ?  228 LYS B CB    1 
ATOM   7384  C  CG    . LYS B 1 228 ? 124.920 131.448 131.824 1.00 29.35 ?  228 LYS B CG    1 
ATOM   7385  C  CD    . LYS B 1 228 ? 123.526 131.057 131.372 1.00 29.88 ?  228 LYS B CD    1 
ATOM   7386  C  CE    . LYS B 1 228 ? 123.282 131.474 129.931 1.00 33.12 ?  228 LYS B CE    1 
ATOM   7387  N  NZ    . LYS B 1 228 ? 122.094 130.795 129.347 1.00 34.24 1  228 LYS B NZ    1 
ATOM   7388  N  N     . LEU B 1 229 ? 125.997 135.909 132.404 1.00 22.47 ?  229 LEU B N     1 
ATOM   7389  C  CA    . LEU B 1 229 ? 126.914 137.036 132.262 1.00 20.86 ?  229 LEU B CA    1 
ATOM   7390  C  C     . LEU B 1 229 ? 127.506 137.432 133.608 1.00 19.28 ?  229 LEU B C     1 
ATOM   7391  O  O     . LEU B 1 229 ? 128.716 137.654 133.729 1.00 25.07 ?  229 LEU B O     1 
ATOM   7392  C  CB    . LEU B 1 229 ? 126.192 138.226 131.634 1.00 23.23 ?  229 LEU B CB    1 
ATOM   7393  C  CG    . LEU B 1 229 ? 125.651 138.078 130.217 1.00 19.52 ?  229 LEU B CG    1 
ATOM   7394  C  CD1   . LEU B 1 229 ? 124.477 139.018 130.031 1.00 20.88 ?  229 LEU B CD1   1 
ATOM   7395  C  CD2   . LEU B 1 229 ? 126.742 138.364 129.203 1.00 17.63 ?  229 LEU B CD2   1 
ATOM   7396  N  N     . LEU B 1 230 ? 126.662 137.521 134.637 1.00 21.75 ?  230 LEU B N     1 
ATOM   7397  C  CA    . LEU B 1 230 ? 127.133 137.884 135.967 1.00 17.81 ?  230 LEU B CA    1 
ATOM   7398  C  C     . LEU B 1 230 ? 128.044 136.809 136.542 1.00 17.83 ?  230 LEU B C     1 
ATOM   7399  O  O     . LEU B 1 230 ? 129.020 137.121 137.228 1.00 28.53 ?  230 LEU B O     1 
ATOM   7400  C  CB    . LEU B 1 230 ? 125.945 138.135 136.894 1.00 19.03 ?  230 LEU B CB    1 
ATOM   7401  C  CG    . LEU B 1 230 ? 125.130 139.399 136.623 1.00 23.50 ?  230 LEU B CG    1 
ATOM   7402  C  CD1   . LEU B 1 230 ? 123.825 139.364 137.399 1.00 24.96 ?  230 LEU B CD1   1 
ATOM   7403  C  CD2   . LEU B 1 230 ? 125.935 140.638 136.974 1.00 20.05 ?  230 LEU B CD2   1 
ATOM   7404  N  N     . ASP B 1 231 ? 127.733 135.539 136.285 1.00 21.74 ?  231 ASP B N     1 
ATOM   7405  C  CA    . ASP B 1 231 ? 128.583 134.455 136.757 1.00 24.81 ?  231 ASP B CA    1 
ATOM   7406  C  C     . ASP B 1 231 ? 129.972 134.540 136.141 1.00 26.22 ?  231 ASP B C     1 
ATOM   7407  O  O     . ASP B 1 231 ? 130.981 134.389 136.840 1.00 32.42 ?  231 ASP B O     1 
ATOM   7408  C  CB    . ASP B 1 231 ? 127.932 133.110 136.437 1.00 26.44 ?  231 ASP B CB    1 
ATOM   7409  C  CG    . ASP B 1 231 ? 128.770 131.935 136.887 1.00 35.82 ?  231 ASP B CG    1 
ATOM   7410  O  OD1   . ASP B 1 231 ? 129.203 131.929 138.056 1.00 38.60 ?  231 ASP B OD1   1 
ATOM   7411  O  OD2   . ASP B 1 231 ? 128.995 131.017 136.072 1.00 35.57 -1 231 ASP B OD2   1 
ATOM   7412  N  N     . ASN B 1 232 ? 130.044 134.802 134.834 1.00 29.25 ?  232 ASN B N     1 
ATOM   7413  C  CA    . ASN B 1 232 ? 131.347 134.969 134.198 1.00 26.54 ?  232 ASN B CA    1 
ATOM   7414  C  C     . ASN B 1 232 ? 132.060 136.216 134.703 1.00 23.51 ?  232 ASN B C     1 
ATOM   7415  O  O     . ASN B 1 232 ? 133.288 136.215 134.858 1.00 31.02 ?  232 ASN B O     1 
ATOM   7416  C  CB    . ASN B 1 232 ? 131.194 135.009 132.679 1.00 29.57 ?  232 ASN B CB    1 
ATOM   7417  C  CG    . ASN B 1 232 ? 132.147 134.067 131.978 1.00 31.72 ?  232 ASN B CG    1 
ATOM   7418  O  OD1   . ASN B 1 232 ? 131.724 133.145 131.284 1.00 31.09 ?  232 ASN B OD1   1 
ATOM   7419  N  ND2   . ASN B 1 232 ? 133.442 134.305 132.139 1.00 30.58 ?  232 ASN B ND2   1 
ATOM   7420  N  N     . ALA B 1 233 ? 131.313 137.291 134.962 1.00 22.25 ?  233 ALA B N     1 
ATOM   7421  C  CA    . ALA B 1 233 ? 131.920 138.508 135.489 1.00 19.36 ?  233 ALA B CA    1 
ATOM   7422  C  C     . ALA B 1 233 ? 132.520 138.277 136.870 1.00 30.42 ?  233 ALA B C     1 
ATOM   7423  O  O     . ALA B 1 233 ? 133.623 138.752 137.165 1.00 37.00 ?  233 ALA B O     1 
ATOM   7424  C  CB    . ALA B 1 233 ? 130.883 139.629 135.534 1.00 21.32 ?  233 ALA B CB    1 
ATOM   7425  N  N     . PHE B 1 234 ? 131.806 137.550 137.731 1.00 26.24 ?  234 PHE B N     1 
ATOM   7426  C  CA    . PHE B 1 234 ? 132.317 137.256 139.065 1.00 18.46 ?  234 PHE B CA    1 
ATOM   7427  C  C     . PHE B 1 234 ? 133.468 136.262 139.014 1.00 23.57 ?  234 PHE B C     1 
ATOM   7428  O  O     . PHE B 1 234 ? 134.380 136.330 139.846 1.00 30.29 ?  234 PHE B O     1 
ATOM   7429  C  CB    . PHE B 1 234 ? 131.192 136.734 139.957 1.00 25.09 ?  234 PHE B CB    1 
ATOM   7430  C  CG    . PHE B 1 234 ? 130.258 137.807 140.440 1.00 21.29 ?  234 PHE B CG    1 
ATOM   7431  C  CD1   . PHE B 1 234 ? 130.725 138.845 141.221 1.00 22.20 ?  234 PHE B CD1   1 
ATOM   7432  C  CD2   . PHE B 1 234 ? 128.917 137.779 140.110 1.00 20.87 ?  234 PHE B CD2   1 
ATOM   7433  C  CE1   . PHE B 1 234 ? 129.872 139.835 141.662 1.00 20.21 ?  234 PHE B CE1   1 
ATOM   7434  C  CE2   . PHE B 1 234 ? 128.061 138.769 140.547 1.00 20.94 ?  234 PHE B CE2   1 
ATOM   7435  C  CZ    . PHE B 1 234 ? 128.539 139.795 141.324 1.00 20.90 ?  234 PHE B CZ    1 
ATOM   7436  N  N     . ARG B 1 235 ? 133.442 135.328 138.059 1.00 29.56 ?  235 ARG B N     1 
ATOM   7437  C  CA    . ARG B 1 235 ? 134.582 134.441 137.867 1.00 26.83 ?  235 ARG B CA    1 
ATOM   7438  C  C     . ARG B 1 235 ? 135.819 135.223 137.449 1.00 28.32 ?  235 ARG B C     1 
ATOM   7439  O  O     . ARG B 1 235 ? 136.926 134.951 137.927 1.00 36.66 ?  235 ARG B O     1 
ATOM   7440  C  CB    . ARG B 1 235 ? 134.251 133.373 136.825 1.00 24.84 ?  235 ARG B CB    1 
ATOM   7441  C  CG    . ARG B 1 235 ? 133.906 132.021 137.413 1.00 32.99 ?  235 ARG B CG    1 
ATOM   7442  C  CD    . ARG B 1 235 ? 133.667 130.987 136.326 1.00 30.46 ?  235 ARG B CD    1 
ATOM   7443  N  NE    . ARG B 1 235 ? 132.280 130.970 135.879 1.00 34.53 ?  235 ARG B NE    1 
ATOM   7444  C  CZ    . ARG B 1 235 ? 131.899 131.149 134.621 1.00 36.67 ?  235 ARG B CZ    1 
ATOM   7445  N  NH1   . ARG B 1 235 ? 132.778 131.369 133.658 1.00 35.53 1  235 ARG B NH1   1 
ATOM   7446  N  NH2   . ARG B 1 235 ? 130.604 131.104 134.323 1.00 32.65 ?  235 ARG B NH2   1 
ATOM   7447  N  N     . TYR B 1 236 ? 135.650 136.199 136.556 1.00 24.71 ?  236 TYR B N     1 
ATOM   7448  C  CA    . TYR B 1 236 ? 136.789 136.978 136.085 1.00 25.51 ?  236 TYR B CA    1 
ATOM   7449  C  C     . TYR B 1 236 ? 137.335 137.874 137.190 1.00 27.63 ?  236 TYR B C     1 
ATOM   7450  O  O     . TYR B 1 236 ? 138.550 137.929 137.416 1.00 28.35 ?  236 TYR B O     1 
ATOM   7451  C  CB    . TYR B 1 236 ? 136.384 137.808 134.869 1.00 22.47 ?  236 TYR B CB    1 
ATOM   7452  C  CG    . TYR B 1 236 ? 137.526 138.577 134.255 1.00 23.31 ?  236 TYR B CG    1 
ATOM   7453  C  CD1   . TYR B 1 236 ? 138.496 137.925 133.508 1.00 21.64 ?  236 TYR B CD1   1 
ATOM   7454  C  CD2   . TYR B 1 236 ? 137.637 139.950 134.420 1.00 24.88 ?  236 TYR B CD2   1 
ATOM   7455  C  CE1   . TYR B 1 236 ? 139.542 138.615 132.944 1.00 24.32 ?  236 TYR B CE1   1 
ATOM   7456  C  CE2   . TYR B 1 236 ? 138.683 140.650 133.856 1.00 17.73 ?  236 TYR B CE2   1 
ATOM   7457  C  CZ    . TYR B 1 236 ? 139.631 139.975 133.119 1.00 20.63 ?  236 TYR B CZ    1 
ATOM   7458  O  OH    . TYR B 1 236 ? 140.678 140.658 132.551 1.00 30.59 ?  236 TYR B OH    1 
ATOM   7459  N  N     . ALA B 1 237 ? 136.453 138.589 137.885 1.00 29.98 ?  237 ALA B N     1 
ATOM   7460  C  CA    . ALA B 1 237 ? 136.849 139.467 138.987 1.00 29.43 ?  237 ALA B CA    1 
ATOM   7461  C  C     . ALA B 1 237 ? 136.800 138.652 140.272 1.00 36.88 ?  237 ALA B C     1 
ATOM   7462  O  O     . ALA B 1 237 ? 135.783 138.602 140.965 1.00 39.03 ?  237 ALA B O     1 
ATOM   7463  C  CB    . ALA B 1 237 ? 135.947 140.692 139.053 1.00 30.69 ?  237 ALA B CB    1 
ATOM   7464  N  N     . ASP B 1 238 ? 137.919 138.007 140.595 1.00 50.17 ?  238 ASP B N     1 
ATOM   7465  C  CA    . ASP B 1 238 ? 137.981 137.117 141.748 1.00 53.56 ?  238 ASP B CA    1 
ATOM   7466  C  C     . ASP B 1 238 ? 139.043 137.568 142.744 1.00 57.82 ?  238 ASP B C     1 
ATOM   7467  O  O     . ASP B 1 238 ? 139.858 136.756 143.194 1.00 57.80 ?  238 ASP B O     1 
ATOM   7468  C  CB    . ASP B 1 238 ? 138.247 135.677 141.297 1.00 52.95 ?  238 ASP B CB    1 
ATOM   7469  C  CG    . ASP B 1 238 ? 139.504 135.549 140.459 1.00 57.45 ?  238 ASP B CG    1 
ATOM   7470  O  OD1   . ASP B 1 238 ? 139.953 136.568 139.894 1.00 57.54 ?  238 ASP B OD1   1 
ATOM   7471  O  OD2   . ASP B 1 238 ? 140.046 134.427 140.370 1.00 56.42 -1 238 ASP B OD2   1 
ATOM   7472  N  N     . GLN B 1 239 ? 139.047 138.859 143.078 1.00 63.48 ?  239 GLN B N     1 
ATOM   7473  C  CA    . GLN B 1 239 ? 139.976 139.425 144.060 1.00 64.82 ?  239 GLN B CA    1 
ATOM   7474  C  C     . GLN B 1 239 ? 141.424 139.095 143.708 1.00 67.35 ?  239 GLN B C     1 
ATOM   7475  O  O     . GLN B 1 239 ? 142.215 138.669 144.554 1.00 66.69 ?  239 GLN B O     1 
ATOM   7476  C  CB    . GLN B 1 239 ? 139.641 138.950 145.474 1.00 64.62 ?  239 GLN B CB    1 
ATOM   7477  C  CG    . GLN B 1 239 ? 138.588 139.777 146.183 1.00 63.82 ?  239 GLN B CG    1 
ATOM   7478  C  CD    . GLN B 1 239 ? 138.864 139.909 147.669 1.00 66.05 ?  239 GLN B CD    1 
ATOM   7479  O  OE1   . GLN B 1 239 ? 137.977 139.712 148.499 1.00 65.31 ?  239 GLN B OE1   1 
ATOM   7480  N  NE2   . GLN B 1 239 ? 140.101 140.247 148.012 1.00 65.72 ?  239 GLN B NE2   1 
ATOM   7481  N  N     . MET B 1 240 ? 141.766 139.296 142.434 1.00 69.45 ?  240 MET B N     1 
ATOM   7482  C  CA    . MET B 1 240 ? 143.106 139.015 141.918 1.00 68.65 ?  240 MET B CA    1 
ATOM   7483  C  C     . MET B 1 240 ? 143.509 137.560 142.146 1.00 69.19 ?  240 MET B C     1 
ATOM   7484  O  O     . MET B 1 240 ? 144.682 137.256 142.374 1.00 69.12 ?  240 MET B O     1 
ATOM   7485  C  CB    . MET B 1 240 ? 144.147 139.962 142.525 1.00 68.32 ?  240 MET B CB    1 
ATOM   7486  C  CG    . MET B 1 240 ? 143.963 141.425 142.146 1.00 68.69 ?  240 MET B CG    1 
ATOM   7487  S  SD    . MET B 1 240 ? 142.266 142.013 142.305 1.00 73.09 ?  240 MET B SD    1 
ATOM   7488  C  CE    . MET B 1 240 ? 142.468 143.742 141.889 1.00 67.85 ?  240 MET B CE    1 
ATOM   7489  N  N     . GLY B 1 241 ? 142.538 136.650 142.089 1.00 67.80 ?  241 GLY B N     1 
ATOM   7490  C  CA    . GLY B 1 241 ? 142.811 135.235 142.223 1.00 68.08 ?  241 GLY B CA    1 
ATOM   7491  C  C     . GLY B 1 241 ? 143.012 134.737 143.636 1.00 70.85 ?  241 GLY B C     1 
ATOM   7492  O  O     . GLY B 1 241 ? 143.374 133.569 143.814 1.00 70.98 ?  241 GLY B O     1 
ATOM   7493  N  N     . GLN B 1 242 ? 142.790 135.578 144.646 1.00 75.83 ?  242 GLN B N     1 
ATOM   7494  C  CA    . GLN B 1 242 ? 142.966 135.158 146.032 1.00 75.30 ?  242 GLN B CA    1 
ATOM   7495  C  C     . GLN B 1 242 ? 141.705 134.511 146.595 1.00 76.57 ?  242 GLN B C     1 
ATOM   7496  O  O     . GLN B 1 242 ? 141.746 133.369 147.062 1.00 76.27 ?  242 GLN B O     1 
ATOM   7497  C  CB    . GLN B 1 242 ? 143.378 136.354 146.895 1.00 74.11 ?  242 GLN B CB    1 
ATOM   7498  C  CG    . GLN B 1 242 ? 144.787 136.855 146.623 1.00 76.09 ?  242 GLN B CG    1 
ATOM   7499  C  CD    . GLN B 1 242 ? 145.333 137.706 147.751 1.00 77.11 ?  242 GLN B CD    1 
ATOM   7500  O  OE1   . GLN B 1 242 ? 144.746 137.778 148.832 1.00 76.41 ?  242 GLN B OE1   1 
ATOM   7501  N  NE2   . GLN B 1 242 ? 146.464 138.358 147.507 1.00 75.63 ?  242 GLN B NE2   1 
ATOM   7502  N  N     . ARG B 1 243 ? 140.583 135.224 146.557 1.00 64.77 ?  243 ARG B N     1 
ATOM   7503  C  CA    . ARG B 1 243 ? 139.297 134.708 147.003 1.00 64.67 ?  243 ARG B CA    1 
ATOM   7504  C  C     . ARG B 1 243 ? 138.363 134.631 145.805 1.00 63.62 ?  243 ARG B C     1 
ATOM   7505  O  O     . ARG B 1 243 ? 138.260 135.591 145.036 1.00 62.13 ?  243 ARG B O     1 
ATOM   7506  C  CB    . ARG B 1 243 ? 138.694 135.594 148.100 1.00 63.04 ?  243 ARG B CB    1 
ATOM   7507  C  CG    . ARG B 1 243 ? 137.171 135.617 148.130 1.00 63.91 ?  243 ARG B CG    1 
ATOM   7508  C  CD    . ARG B 1 243 ? 136.620 136.929 147.588 1.00 63.15 ?  243 ARG B CD    1 
ATOM   7509  N  NE    . ARG B 1 243 ? 135.245 137.165 148.013 1.00 65.04 ?  243 ARG B NE    1 
ATOM   7510  C  CZ    . ARG B 1 243 ? 134.479 138.147 147.557 1.00 62.89 ?  243 ARG B CZ    1 
ATOM   7511  N  NH1   . ARG B 1 243 ? 134.921 139.008 146.654 1.00 59.40 1  243 ARG B NH1   1 
ATOM   7512  N  NH2   . ARG B 1 243 ? 133.237 138.268 148.018 1.00 60.40 ?  243 ARG B NH2   1 
ATOM   7513  N  N     . GLN B 1 244 ? 137.692 133.491 145.649 1.00 61.88 ?  244 GLN B N     1 
ATOM   7514  C  CA    . GLN B 1 244 ? 136.783 133.307 144.525 1.00 62.67 ?  244 GLN B CA    1 
ATOM   7515  C  C     . GLN B 1 244 ? 135.708 134.385 144.527 1.00 61.97 ?  244 GLN B C     1 
ATOM   7516  O  O     . GLN B 1 244 ? 135.117 134.687 145.568 1.00 61.07 ?  244 GLN B O     1 
ATOM   7517  C  CB    . GLN B 1 244 ? 136.140 131.921 144.589 1.00 59.38 ?  244 GLN B CB    1 
ATOM   7518  C  CG    . GLN B 1 244 ? 137.096 130.774 144.310 1.00 59.03 ?  244 GLN B CG    1 
ATOM   7519  C  CD    . GLN B 1 244 ? 136.377 129.508 143.888 1.00 60.67 ?  244 GLN B CD    1 
ATOM   7520  O  OE1   . GLN B 1 244 ? 135.341 129.152 144.450 1.00 61.69 ?  244 GLN B OE1   1 
ATOM   7521  N  NE2   . GLN B 1 244 ? 136.924 128.819 142.894 1.00 59.63 ?  244 GLN B NE2   1 
ATOM   7522  N  N     . GLY B 1 245 ? 135.468 134.975 143.358 1.00 50.30 ?  245 GLY B N     1 
ATOM   7523  C  CA    . GLY B 1 245 ? 134.446 135.993 143.228 1.00 47.08 ?  245 GLY B CA    1 
ATOM   7524  C  C     . GLY B 1 245 ? 133.070 135.464 143.568 1.00 46.51 ?  245 GLY B C     1 
ATOM   7525  O  O     . GLY B 1 245 ? 132.598 134.504 142.953 1.00 46.35 ?  245 GLY B O     1 
ATOM   7526  N  N     . SER B 1 246 ? 132.418 136.082 144.547 1.00 41.79 ?  246 SER B N     1 
ATOM   7527  C  CA    . SER B 1 246 ? 131.130 135.624 145.048 1.00 37.18 ?  246 SER B CA    1 
ATOM   7528  C  C     . SER B 1 246 ? 130.061 136.644 144.682 1.00 35.91 ?  246 SER B C     1 
ATOM   7529  O  O     . SER B 1 246 ? 130.180 137.825 145.024 1.00 30.02 ?  246 SER B O     1 
ATOM   7530  C  CB    . SER B 1 246 ? 131.175 135.412 146.561 1.00 37.49 ?  246 SER B CB    1 
ATOM   7531  O  OG    . SER B 1 246 ? 131.997 134.309 146.897 1.00 43.74 ?  246 SER B OG    1 
ATOM   7532  N  N     . GLY B 1 247 ? 129.022 136.181 143.991 1.00 25.68 ?  247 GLY B N     1 
ATOM   7533  C  CA    . GLY B 1 247 ? 127.906 137.029 143.649 1.00 8.74  ?  247 GLY B CA    1 
ATOM   7534  C  C     . GLY B 1 247 ? 126.599 136.372 144.046 1.00 13.22 ?  247 GLY B C     1 
ATOM   7535  O  O     . GLY B 1 247 ? 126.515 135.161 144.246 1.00 20.58 ?  247 GLY B O     1 
ATOM   7536  N  N     . ALA B 1 248 ? 125.575 137.206 144.170 1.00 14.03 ?  248 ALA B N     1 
ATOM   7537  C  CA    . ALA B 1 248 ? 124.232 136.750 144.484 1.00 14.28 ?  248 ALA B CA    1 
ATOM   7538  C  C     . ALA B 1 248 ? 123.257 137.354 143.489 1.00 10.37 ?  248 ALA B C     1 
ATOM   7539  O  O     . ALA B 1 248 ? 123.374 138.526 143.126 1.00 17.81 ?  248 ALA B O     1 
ATOM   7540  C  CB    . ALA B 1 248 ? 123.828 137.125 145.913 1.00 9.00  ?  248 ALA B CB    1 
ATOM   7541  N  N     . ALA B 1 249 ? 122.308 136.543 143.037 1.00 12.61 ?  249 ALA B N     1 
ATOM   7542  C  CA    . ALA B 1 249 ? 121.210 137.002 142.202 1.00 12.36 ?  249 ALA B CA    1 
ATOM   7543  C  C     . ALA B 1 249 ? 119.911 136.776 142.956 1.00 8.88  ?  249 ALA B C     1 
ATOM   7544  O  O     . ALA B 1 249 ? 119.688 135.690 143.500 1.00 16.83 ?  249 ALA B O     1 
ATOM   7545  C  CB    . ALA B 1 249 ? 121.183 136.271 140.858 1.00 14.14 ?  249 ALA B CB    1 
ATOM   7546  N  N     . TYR B 1 250 ? 119.067 137.799 143.005 1.00 8.30  ?  250 TYR B N     1 
ATOM   7547  C  CA    . TYR B 1 250 ? 117.781 137.712 143.675 1.00 8.18  ?  250 TYR B CA    1 
ATOM   7548  C  C     . TYR B 1 250 ? 116.675 137.893 142.650 1.00 7.77  ?  250 TYR B C     1 
ATOM   7549  O  O     . TYR B 1 250 ? 116.733 138.806 141.820 1.00 13.56 ?  250 TYR B O     1 
ATOM   7550  C  CB    . TYR B 1 250 ? 117.661 138.759 144.782 1.00 7.54  ?  250 TYR B CB    1 
ATOM   7551  C  CG    . TYR B 1 250 ? 118.248 138.313 146.099 1.00 15.50 ?  250 TYR B CG    1 
ATOM   7552  C  CD1   . TYR B 1 250 ? 119.622 138.282 146.290 1.00 3.04  ?  250 TYR B CD1   1 
ATOM   7553  C  CD2   . TYR B 1 250 ? 117.432 137.924 147.151 1.00 12.49 ?  250 TYR B CD2   1 
ATOM   7554  C  CE1   . TYR B 1 250 ? 120.166 137.878 147.487 1.00 0.74  ?  250 TYR B CE1   1 
ATOM   7555  C  CE2   . TYR B 1 250 ? 117.968 137.515 148.355 1.00 7.28  ?  250 TYR B CE2   1 
ATOM   7556  C  CZ    . TYR B 1 250 ? 119.336 137.495 148.517 1.00 8.49  ?  250 TYR B CZ    1 
ATOM   7557  O  OH    . TYR B 1 250 ? 119.878 137.090 149.715 1.00 12.85 ?  250 TYR B OH    1 
ATOM   7558  N  N     . LEU B 1 251 ? 115.679 137.018 142.703 1.00 12.99 ?  251 LEU B N     1 
ATOM   7559  C  CA    . LEU B 1 251 ? 114.535 137.083 141.810 1.00 14.29 ?  251 LEU B CA    1 
ATOM   7560  C  C     . LEU B 1 251 ? 113.258 136.937 142.616 1.00 12.54 ?  251 LEU B C     1 
ATOM   7561  O  O     . LEU B 1 251 ? 113.185 136.115 143.535 1.00 15.58 ?  251 LEU B O     1 
ATOM   7562  C  CB    . LEU B 1 251 ? 114.602 135.994 140.737 1.00 15.25 ?  251 LEU B CB    1 
ATOM   7563  C  CG    . LEU B 1 251 ? 113.716 136.233 139.515 1.00 11.75 ?  251 LEU B CG    1 
ATOM   7564  C  CD1   . LEU B 1 251 ? 114.238 137.409 138.715 1.00 12.25 ?  251 LEU B CD1   1 
ATOM   7565  C  CD2   . LEU B 1 251 ? 113.637 134.989 138.655 1.00 7.68  ?  251 LEU B CD2   1 
ATOM   7566  N  N     . ASN B 1 252 ? 112.257 137.740 142.276 1.00 11.64 ?  252 ASN B N     1 
ATOM   7567  C  CA    . ASN B 1 252 ? 110.949 137.592 142.895 1.00 10.65 ?  252 ASN B CA    1 
ATOM   7568  C  C     . ASN B 1 252 ? 110.319 136.274 142.470 1.00 15.17 ?  252 ASN B C     1 
ATOM   7569  O  O     . ASN B 1 252 ? 110.480 135.828 141.331 1.00 23.08 ?  252 ASN B O     1 
ATOM   7570  C  CB    . ASN B 1 252 ? 110.042 138.762 142.519 1.00 12.48 ?  252 ASN B CB    1 
ATOM   7571  C  CG    . ASN B 1 252 ? 108.977 139.028 143.559 1.00 20.70 ?  252 ASN B CG    1 
ATOM   7572  O  OD1   . ASN B 1 252 ? 108.026 138.260 143.701 1.00 30.12 ?  252 ASN B OD1   1 
ATOM   7573  N  ND2   . ASN B 1 252 ? 109.134 140.115 144.303 1.00 20.44 ?  252 ASN B ND2   1 
ATOM   7574  N  N     . ILE B 1 253 ? 109.601 135.642 143.401 1.00 13.68 ?  253 ILE B N     1 
ATOM   7575  C  CA    . ILE B 1 253 ? 108.989 134.352 143.115 1.00 17.48 ?  253 ILE B CA    1 
ATOM   7576  C  C     . ILE B 1 253 ? 107.859 134.470 142.099 1.00 20.96 ?  253 ILE B C     1 
ATOM   7577  O  O     . ILE B 1 253 ? 107.442 133.459 141.521 1.00 23.60 ?  253 ILE B O     1 
ATOM   7578  C  CB    . ILE B 1 253 ? 108.495 133.696 144.419 1.00 16.66 ?  253 ILE B CB    1 
ATOM   7579  C  CG1   . ILE B 1 253 ? 108.410 132.177 144.254 1.00 16.22 ?  253 ILE B CG1   1 
ATOM   7580  C  CG2   . ILE B 1 253 ? 107.157 134.277 144.845 1.00 13.72 ?  253 ILE B CG2   1 
ATOM   7581  C  CD1   . ILE B 1 253 ? 108.636 131.413 145.530 1.00 16.69 ?  253 ILE B CD1   1 
ATOM   7582  N  N     . PHE B 1 254 ? 107.356 135.677 141.857 1.00 19.04 ?  254 PHE B N     1 
ATOM   7583  C  CA    . PHE B 1 254 ? 106.314 135.897 140.864 1.00 16.79 ?  254 PHE B CA    1 
ATOM   7584  C  C     . PHE B 1 254 ? 106.876 136.207 139.483 1.00 18.10 ?  254 PHE B C     1 
ATOM   7585  O  O     . PHE B 1 254 ? 106.101 136.399 138.542 1.00 25.04 ?  254 PHE B O     1 
ATOM   7586  C  CB    . PHE B 1 254 ? 105.387 137.025 141.321 1.00 23.09 ?  254 PHE B CB    1 
ATOM   7587  C  CG    . PHE B 1 254 ? 104.388 136.597 142.355 1.00 22.28 ?  254 PHE B CG    1 
ATOM   7588  C  CD1   . PHE B 1 254 ? 103.362 135.730 142.027 1.00 22.04 ?  254 PHE B CD1   1 
ATOM   7589  C  CD2   . PHE B 1 254 ? 104.488 137.043 143.661 1.00 26.07 ?  254 PHE B CD2   1 
ATOM   7590  C  CE1   . PHE B 1 254 ? 102.445 135.328 142.978 1.00 24.80 ?  254 PHE B CE1   1 
ATOM   7591  C  CE2   . PHE B 1 254 ? 103.576 136.644 144.617 1.00 27.48 ?  254 PHE B CE2   1 
ATOM   7592  C  CZ    . PHE B 1 254 ? 102.552 135.786 144.274 1.00 21.77 ?  254 PHE B CZ    1 
ATOM   7593  N  N     . HIS B 1 255 ? 108.196 136.270 139.347 1.00 25.56 ?  255 HIS B N     1 
ATOM   7594  C  CA    . HIS B 1 255 ? 108.819 136.376 138.036 1.00 14.87 ?  255 HIS B CA    1 
ATOM   7595  C  C     . HIS B 1 255 ? 108.590 135.092 137.249 1.00 18.41 ?  255 HIS B C     1 
ATOM   7596  O  O     . HIS B 1 255 ? 108.605 133.993 137.809 1.00 27.28 ?  255 HIS B O     1 
ATOM   7597  C  CB    . HIS B 1 255 ? 110.315 136.643 138.190 1.00 17.20 ?  255 HIS B CB    1 
ATOM   7598  C  CG    . HIS B 1 255 ? 110.948 137.283 136.997 1.00 19.61 ?  255 HIS B CG    1 
ATOM   7599  N  ND1   . HIS B 1 255 ? 111.169 136.606 135.818 1.00 17.88 ?  255 HIS B ND1   1 
ATOM   7600  C  CD2   . HIS B 1 255 ? 111.428 138.535 136.808 1.00 14.91 ?  255 HIS B CD2   1 
ATOM   7601  C  CE1   . HIS B 1 255 ? 111.747 137.415 134.950 1.00 16.46 ?  255 HIS B CE1   1 
ATOM   7602  N  NE2   . HIS B 1 255 ? 111.918 138.591 135.526 1.00 11.54 ?  255 HIS B NE2   1 
ATOM   7603  N  N     . ARG B 1 256 ? 108.369 135.233 135.940 1.00 21.76 ?  256 ARG B N     1 
ATOM   7604  C  CA    . ARG B 1 256 ? 108.110 134.058 135.113 1.00 22.18 ?  256 ARG B CA    1 
ATOM   7605  C  C     . ARG B 1 256 ? 109.321 133.134 135.056 1.00 23.41 ?  256 ARG B C     1 
ATOM   7606  O  O     . ARG B 1 256 ? 109.165 131.912 134.953 1.00 25.13 ?  256 ARG B O     1 
ATOM   7607  C  CB    . ARG B 1 256 ? 107.699 134.484 133.704 1.00 22.61 ?  256 ARG B CB    1 
ATOM   7608  C  CG    . ARG B 1 256 ? 107.459 133.321 132.756 1.00 23.62 ?  256 ARG B CG    1 
ATOM   7609  C  CD    . ARG B 1 256 ? 108.312 133.433 131.506 1.00 25.89 ?  256 ARG B CD    1 
ATOM   7610  N  NE    . ARG B 1 256 ? 109.588 132.741 131.634 1.00 27.83 ?  256 ARG B NE    1 
ATOM   7611  C  CZ    . ARG B 1 256 ? 109.736 131.425 131.579 1.00 29.95 ?  256 ARG B CZ    1 
ATOM   7612  N  NH1   . ARG B 1 256 ? 108.703 130.618 131.401 1.00 28.67 1  256 ARG B NH1   1 
ATOM   7613  N  NH2   . ARG B 1 256 ? 110.953 130.904 131.708 1.00 27.86 ?  256 ARG B NH2   1 
ATOM   7614  N  N     . ASP B 1 257 ? 110.524 133.692 135.139 1.00 14.82 ?  257 ASP B N     1 
ATOM   7615  C  CA    . ASP B 1 257 ? 111.753 132.915 135.056 1.00 19.17 ?  257 ASP B CA    1 
ATOM   7616  C  C     . ASP B 1 257 ? 112.103 132.208 136.358 1.00 18.74 ?  257 ASP B C     1 
ATOM   7617  O  O     . ASP B 1 257 ? 113.173 131.592 136.432 1.00 24.95 ?  257 ASP B O     1 
ATOM   7618  C  CB    . ASP B 1 257 ? 112.915 133.819 134.644 1.00 23.39 ?  257 ASP B CB    1 
ATOM   7619  C  CG    . ASP B 1 257 ? 112.892 134.160 133.173 1.00 26.85 ?  257 ASP B CG    1 
ATOM   7620  O  OD1   . ASP B 1 257 ? 112.159 133.491 132.415 1.00 27.01 ?  257 ASP B OD1   1 
ATOM   7621  O  OD2   . ASP B 1 257 ? 113.613 135.095 132.775 1.00 31.26 -1 257 ASP B OD2   1 
ATOM   7622  N  N     . ILE B 1 258 ? 111.223 132.259 137.363 1.00 19.61 ?  258 ILE B N     1 
ATOM   7623  C  CA    . ILE B 1 258 ? 111.578 131.783 138.698 1.00 21.87 ?  258 ILE B CA    1 
ATOM   7624  C  C     . ILE B 1 258 ? 111.989 130.317 138.656 1.00 23.00 ?  258 ILE B C     1 
ATOM   7625  O  O     . ILE B 1 258 ? 112.907 129.897 139.369 1.00 32.37 ?  258 ILE B O     1 
ATOM   7626  C  CB    . ILE B 1 258 ? 110.421 132.028 139.686 1.00 23.55 ?  258 ILE B CB    1 
ATOM   7627  C  CG1   . ILE B 1 258 ? 110.849 131.675 141.112 1.00 21.31 ?  258 ILE B CG1   1 
ATOM   7628  C  CG2   . ILE B 1 258 ? 109.176 131.247 139.290 1.00 20.68 ?  258 ILE B CG2   1 
ATOM   7629  C  CD1   . ILE B 1 258 ? 112.004 132.503 141.624 1.00 19.07 ?  258 ILE B CD1   1 
ATOM   7630  N  N     . ASN B 1 259 ? 111.330 129.518 137.816 1.00 26.15 ?  259 ASN B N     1 
ATOM   7631  C  CA    . ASN B 1 259 ? 111.733 128.123 137.674 1.00 24.53 ?  259 ASN B CA    1 
ATOM   7632  C  C     . ASN B 1 259 ? 113.113 128.020 137.039 1.00 23.29 ?  259 ASN B C     1 
ATOM   7633  O  O     . ASN B 1 259 ? 114.008 127.359 137.579 1.00 26.89 ?  259 ASN B O     1 
ATOM   7634  C  CB    . ASN B 1 259 ? 110.694 127.361 136.853 1.00 24.70 ?  259 ASN B CB    1 
ATOM   7635  C  CG    . ASN B 1 259 ? 109.527 126.885 137.693 1.00 24.50 ?  259 ASN B CG    1 
ATOM   7636  O  OD1   . ASN B 1 259 ? 109.671 125.989 138.523 1.00 26.50 ?  259 ASN B OD1   1 
ATOM   7637  N  ND2   . ASN B 1 259 ? 108.364 127.488 137.483 1.00 30.54 ?  259 ASN B ND2   1 
ATOM   7638  N  N     . ASP B 1 260 ? 113.317 128.708 135.911 1.00 27.76 ?  260 ASP B N     1 
ATOM   7639  C  CA    . ASP B 1 260 ? 114.613 128.667 135.241 1.00 24.59 ?  260 ASP B CA    1 
ATOM   7640  C  C     . ASP B 1 260 ? 115.708 129.183 136.164 1.00 19.53 ?  260 ASP B C     1 
ATOM   7641  O  O     . ASP B 1 260 ? 116.786 128.585 136.265 1.00 27.97 ?  260 ASP B O     1 
ATOM   7642  C  CB    . ASP B 1 260 ? 114.562 129.486 133.952 1.00 23.49 ?  260 ASP B CB    1 
ATOM   7643  C  CG    . ASP B 1 260 ? 113.604 128.908 132.931 1.00 32.69 ?  260 ASP B CG    1 
ATOM   7644  O  OD1   . ASP B 1 260 ? 113.425 127.671 132.913 1.00 33.48 ?  260 ASP B OD1   1 
ATOM   7645  O  OD2   . ASP B 1 260 ? 113.030 129.691 132.145 1.00 33.86 -1 260 ASP B OD2   1 
ATOM   7646  N  N     . PHE B 1 261 ? 115.438 130.299 136.845 1.00 26.81 ?  261 PHE B N     1 
ATOM   7647  C  CA    . PHE B 1 261 ? 116.269 130.782 137.938 1.00 22.12 ?  261 PHE B CA    1 
ATOM   7648  C  C     . PHE B 1 261 ? 116.677 129.639 138.862 1.00 16.07 ?  261 PHE B C     1 
ATOM   7649  O  O     . PHE B 1 261 ? 117.867 129.348 139.031 1.00 21.75 ?  261 PHE B O     1 
ATOM   7650  C  CB    . PHE B 1 261 ? 115.491 131.864 138.698 1.00 10.28 ?  261 PHE B CB    1 
ATOM   7651  C  CG    . PHE B 1 261 ? 116.287 132.582 139.747 1.00 22.77 ?  261 PHE B CG    1 
ATOM   7652  C  CD1   . PHE B 1 261 ? 117.181 133.579 139.398 1.00 20.56 ?  261 PHE B CD1   1 
ATOM   7653  C  CD2   . PHE B 1 261 ? 116.110 132.290 141.090 1.00 23.60 ?  261 PHE B CD2   1 
ATOM   7654  C  CE1   . PHE B 1 261 ? 117.902 134.251 140.364 1.00 15.18 ?  261 PHE B CE1   1 
ATOM   7655  C  CE2   . PHE B 1 261 ? 116.827 132.959 142.058 1.00 15.89 ?  261 PHE B CE2   1 
ATOM   7656  C  CZ    . PHE B 1 261 ? 117.725 133.941 141.694 1.00 15.76 ?  261 PHE B CZ    1 
ATOM   7657  N  N     . LEU B 1 262 ? 115.683 128.945 139.421 1.00 23.93 ?  262 LEU B N     1 
ATOM   7658  C  CA    . LEU B 1 262 ? 115.975 127.834 140.318 1.00 23.77 ?  262 LEU B CA    1 
ATOM   7659  C  C     . LEU B 1 262 ? 116.726 126.728 139.591 1.00 28.49 ?  262 LEU B C     1 
ATOM   7660  O  O     . LEU B 1 262 ? 117.612 126.084 140.165 1.00 30.74 ?  262 LEU B O     1 
ATOM   7661  C  CB    . LEU B 1 262 ? 114.684 127.295 140.928 1.00 27.44 ?  262 LEU B CB    1 
ATOM   7662  C  CG    . LEU B 1 262 ? 113.924 128.267 141.830 1.00 24.56 ?  262 LEU B CG    1 
ATOM   7663  C  CD1   . LEU B 1 262 ? 112.609 127.658 142.276 1.00 26.12 ?  262 LEU B CD1   1 
ATOM   7664  C  CD2   . LEU B 1 262 ? 114.774 128.670 143.022 1.00 23.89 ?  262 LEU B CD2   1 
ATOM   7665  N  N     . ASP B 1 263 ? 116.410 126.518 138.312 1.00 34.07 ?  263 ASP B N     1 
ATOM   7666  C  CA    . ASP B 1 263 ? 117.088 125.484 137.546 1.00 25.65 ?  263 ASP B CA    1 
ATOM   7667  C  C     . ASP B 1 263 ? 118.571 125.773 137.370 1.00 29.95 ?  263 ASP B C     1 
ATOM   7668  O  O     . ASP B 1 263 ? 119.315 124.869 136.978 1.00 38.33 ?  263 ASP B O     1 
ATOM   7669  C  CB    . ASP B 1 263 ? 116.422 125.320 136.180 1.00 30.81 ?  263 ASP B CB    1 
ATOM   7670  C  CG    . ASP B 1 263 ? 115.050 124.682 136.275 1.00 37.05 ?  263 ASP B CG    1 
ATOM   7671  O  OD1   . ASP B 1 263 ? 114.765 124.035 137.304 1.00 36.66 ?  263 ASP B OD1   1 
ATOM   7672  O  OD2   . ASP B 1 263 ? 114.259 124.828 135.320 1.00 35.56 -1 263 ASP B OD2   1 
ATOM   7673  N  N     . THR B 1 264 ? 119.016 127.002 137.646 1.00 33.51 ?  264 THR B N     1 
ATOM   7674  C  CA    . THR B 1 264 ? 120.446 127.281 137.616 1.00 32.04 ?  264 THR B CA    1 
ATOM   7675  C  C     . THR B 1 264 ? 121.199 126.548 138.718 1.00 36.16 ?  264 THR B C     1 
ATOM   7676  O  O     . THR B 1 264 ? 122.408 126.332 138.585 1.00 36.90 ?  264 THR B O     1 
ATOM   7677  C  CB    . THR B 1 264 ? 120.697 128.784 137.725 1.00 33.04 ?  264 THR B CB    1 
ATOM   7678  O  OG1   . THR B 1 264 ? 120.142 129.276 138.952 1.00 36.48 ?  264 THR B OG1   1 
ATOM   7679  C  CG2   . THR B 1 264 ? 120.060 129.516 136.555 1.00 30.51 ?  264 THR B CG2   1 
ATOM   7680  N  N     . LYS B 1 265 ? 120.519 126.158 139.797 1.00 32.38 ?  265 LYS B N     1 
ATOM   7681  C  CA    . LYS B 1 265 ? 121.165 125.495 140.922 1.00 34.15 ?  265 LYS B CA    1 
ATOM   7682  C  C     . LYS B 1 265 ? 120.884 124.000 140.991 1.00 36.53 ?  265 LYS B C     1 
ATOM   7683  O  O     . LYS B 1 265 ? 121.398 123.332 141.892 1.00 39.20 ?  265 LYS B O     1 
ATOM   7684  C  CB    . LYS B 1 265 ? 120.747 126.158 142.238 1.00 33.86 ?  265 LYS B CB    1 
ATOM   7685  C  CG    . LYS B 1 265 ? 121.458 127.467 142.516 1.00 32.96 ?  265 LYS B CG    1 
ATOM   7686  C  CD    . LYS B 1 265 ? 122.962 127.310 142.402 1.00 35.96 ?  265 LYS B CD    1 
ATOM   7687  C  CE    . LYS B 1 265 ? 123.661 128.650 142.500 1.00 34.47 ?  265 LYS B CE    1 
ATOM   7688  N  NZ    . LYS B 1 265 ? 125.100 128.552 142.138 1.00 37.38 1  265 LYS B NZ    1 
ATOM   7689  N  N     . LYS B 1 266 ? 120.085 123.461 140.075 1.00 45.03 ?  266 LYS B N     1 
ATOM   7690  C  CA    . LYS B 1 266 ? 119.863 122.022 140.049 1.00 44.08 ?  266 LYS B CA    1 
ATOM   7691  C  C     . LYS B 1 266 ? 121.149 121.299 139.672 1.00 48.90 ?  266 LYS B C     1 
ATOM   7692  O  O     . LYS B 1 266 ? 121.895 121.741 138.792 1.00 50.53 ?  266 LYS B O     1 
ATOM   7693  C  CB    . LYS B 1 266 ? 118.748 121.669 139.066 1.00 44.10 ?  266 LYS B CB    1 
ATOM   7694  C  CG    . LYS B 1 266 ? 117.350 121.812 139.645 1.00 46.71 ?  266 LYS B CG    1 
ATOM   7695  C  CD    . LYS B 1 266 ? 116.295 121.285 138.688 1.00 48.45 ?  266 LYS B CD    1 
ATOM   7696  C  CE    . LYS B 1 266 ? 114.987 121.009 139.415 1.00 47.44 ?  266 LYS B CE    1 
ATOM   7697  N  NZ    . LYS B 1 266 ? 113.879 120.698 138.472 1.00 49.34 1  266 LYS B NZ    1 
ATOM   7698  N  N     . ILE B 1 267 ? 121.413 120.180 140.351 1.00 56.82 ?  267 ILE B N     1 
ATOM   7699  C  CA    . ILE B 1 267 ? 122.650 119.445 140.113 1.00 59.40 ?  267 ILE B CA    1 
ATOM   7700  C  C     . ILE B 1 267 ? 122.651 118.744 138.760 1.00 59.98 ?  267 ILE B C     1 
ATOM   7701  O  O     . ILE B 1 267 ? 123.711 118.318 138.288 1.00 58.71 ?  267 ILE B O     1 
ATOM   7702  C  CB    . ILE B 1 267 ? 122.917 118.463 141.274 1.00 60.41 ?  267 ILE B CB    1 
ATOM   7703  C  CG1   . ILE B 1 267 ? 121.632 117.785 141.779 1.00 59.80 ?  267 ILE B CG1   1 
ATOM   7704  C  CG2   . ILE B 1 267 ? 123.618 119.179 142.421 1.00 58.18 ?  267 ILE B CG2   1 
ATOM   7705  C  CD1   . ILE B 1 267 ? 120.889 116.918 140.779 1.00 57.74 ?  267 ILE B CD1   1 
ATOM   7706  N  N     . SER B 1 268 ? 121.490 118.615 138.120 1.00 62.10 ?  268 SER B N     1 
ATOM   7707  C  CA    . SER B 1 268 ? 121.375 118.002 136.805 1.00 64.31 ?  268 SER B CA    1 
ATOM   7708  C  C     . SER B 1 268 ? 121.291 119.031 135.686 1.00 65.31 ?  268 SER B C     1 
ATOM   7709  O  O     . SER B 1 268 ? 121.043 118.661 134.534 1.00 66.20 ?  268 SER B O     1 
ATOM   7710  C  CB    . SER B 1 268 ? 120.153 117.083 136.761 1.00 67.03 ?  268 SER B CB    1 
ATOM   7711  O  OG    . SER B 1 268 ? 118.980 117.777 137.151 1.00 64.20 ?  268 SER B OG    1 
ATOM   7712  N  N     . ALA B 1 269 ? 121.486 120.309 136.000 1.00 66.97 ?  269 ALA B N     1 
ATOM   7713  C  CA    . ALA B 1 269 ? 121.348 121.362 135.004 1.00 67.58 ?  269 ALA B CA    1 
ATOM   7714  C  C     . ALA B 1 269 ? 122.444 121.270 133.949 1.00 67.63 ?  269 ALA B C     1 
ATOM   7715  O  O     . ALA B 1 269 ? 123.586 120.898 134.232 1.00 65.97 ?  269 ALA B O     1 
ATOM   7716  C  CB    . ALA B 1 269 ? 121.384 122.736 135.673 1.00 65.51 ?  269 ALA B CB    1 
ATOM   7717  N  N     . ASP B 1 270 ? 122.081 121.616 132.717 1.00 73.26 ?  270 ASP B N     1 
ATOM   7718  C  CA    . ASP B 1 270 ? 123.039 121.634 131.624 1.00 73.45 ?  270 ASP B CA    1 
ATOM   7719  C  C     . ASP B 1 270 ? 124.008 122.804 131.786 1.00 73.74 ?  270 ASP B C     1 
ATOM   7720  O  O     . ASP B 1 270 ? 123.748 123.767 132.512 1.00 74.05 ?  270 ASP B O     1 
ATOM   7721  C  CB    . ASP B 1 270 ? 122.315 121.728 130.280 1.00 73.73 ?  270 ASP B CB    1 
ATOM   7722  C  CG    . ASP B 1 270 ? 123.127 121.153 129.138 1.00 75.07 ?  270 ASP B CG    1 
ATOM   7723  O  OD1   . ASP B 1 270 ? 124.240 121.660 128.881 1.00 75.22 ?  270 ASP B OD1   1 
ATOM   7724  O  OD2   . ASP B 1 270 ? 122.653 120.192 128.496 1.00 74.14 -1 270 ASP B OD2   1 
ATOM   7725  N  N     . GLU B 1 271 ? 125.145 122.706 131.092 1.00 73.75 ?  271 GLU B N     1 
ATOM   7726  C  CA    . GLU B 1 271 ? 126.181 123.725 131.222 1.00 73.72 ?  271 GLU B CA    1 
ATOM   7727  C  C     . GLU B 1 271 ? 125.719 125.083 130.704 1.00 72.95 ?  271 GLU B C     1 
ATOM   7728  O  O     . GLU B 1 271 ? 126.178 126.118 131.197 1.00 72.44 ?  271 GLU B O     1 
ATOM   7729  C  CB    . GLU B 1 271 ? 127.448 123.283 130.490 1.00 72.64 ?  271 GLU B CB    1 
ATOM   7730  C  CG    . GLU B 1 271 ? 128.273 122.260 131.252 1.00 73.86 ?  271 GLU B CG    1 
ATOM   7731  C  CD    . GLU B 1 271 ? 128.803 122.800 132.567 1.00 74.42 ?  271 GLU B CD    1 
ATOM   7732  O  OE1   . GLU B 1 271 ? 129.163 123.994 132.619 1.00 73.57 ?  271 GLU B OE1   1 
ATOM   7733  O  OE2   . GLU B 1 271 ? 128.857 122.030 133.548 1.00 73.53 -1 271 GLU B OE2   1 
ATOM   7734  N  N     . ASP B 1 272 ? 124.818 125.103 129.721 1.00 69.22 ?  272 ASP B N     1 
ATOM   7735  C  CA    . ASP B 1 272 ? 124.313 126.369 129.202 1.00 70.00 ?  272 ASP B CA    1 
ATOM   7736  C  C     . ASP B 1 272 ? 123.340 127.051 130.155 1.00 69.56 ?  272 ASP B C     1 
ATOM   7737  O  O     . ASP B 1 272 ? 123.002 128.219 129.934 1.00 68.28 ?  272 ASP B O     1 
ATOM   7738  C  CB    . ASP B 1 272 ? 123.644 126.151 127.842 1.00 69.68 ?  272 ASP B CB    1 
ATOM   7739  C  CG    . ASP B 1 272 ? 122.305 125.448 127.954 1.00 72.04 ?  272 ASP B CG    1 
ATOM   7740  O  OD1   . ASP B 1 272 ? 122.127 124.639 128.889 1.00 71.80 ?  272 ASP B OD1   1 
ATOM   7741  O  OD2   . ASP B 1 272 ? 121.427 125.703 127.102 1.00 69.21 -1 272 ASP B OD2   1 
ATOM   7742  N  N     . VAL B 1 273 ? 122.880 126.356 131.196 1.00 62.08 ?  273 VAL B N     1 
ATOM   7743  C  CA    . VAL B 1 273 ? 121.974 126.917 132.186 1.00 62.78 ?  273 VAL B CA    1 
ATOM   7744  C  C     . VAL B 1 273 ? 122.615 126.987 133.566 1.00 61.16 ?  273 VAL B C     1 
ATOM   7745  O  O     . VAL B 1 273 ? 122.394 127.949 134.310 1.00 60.96 ?  273 VAL B O     1 
ATOM   7746  C  CB    . VAL B 1 273 ? 120.653 126.118 132.240 1.00 63.68 ?  273 VAL B CB    1 
ATOM   7747  C  CG1   . VAL B 1 273 ? 119.750 126.634 133.353 1.00 61.00 ?  273 VAL B CG1   1 
ATOM   7748  C  CG2   . VAL B 1 273 ? 119.940 126.182 130.899 1.00 62.41 ?  273 VAL B CG2   1 
ATOM   7749  N  N     . ARG B 1 274 ? 123.421 125.987 133.921 1.00 61.27 ?  274 ARG B N     1 
ATOM   7750  C  CA    . ARG B 1 274 ? 124.001 125.915 135.255 1.00 60.75 ?  274 ARG B CA    1 
ATOM   7751  C  C     . ARG B 1 274 ? 124.887 127.124 135.537 1.00 59.70 ?  274 ARG B C     1 
ATOM   7752  O  O     . ARG B 1 274 ? 125.689 127.542 134.697 1.00 62.45 ?  274 ARG B O     1 
ATOM   7753  C  CB    . ARG B 1 274 ? 124.811 124.625 135.408 1.00 62.89 ?  274 ARG B CB    1 
ATOM   7754  C  CG    . ARG B 1 274 ? 126.035 124.753 136.303 1.00 58.68 ?  274 ARG B CG    1 
ATOM   7755  C  CD    . ARG B 1 274 ? 126.265 123.495 137.123 1.00 61.77 ?  274 ARG B CD    1 
ATOM   7756  N  NE    . ARG B 1 274 ? 126.587 122.348 136.283 1.00 65.06 ?  274 ARG B NE    1 
ATOM   7757  C  CZ    . ARG B 1 274 ? 125.896 121.217 136.262 1.00 66.11 ?  274 ARG B CZ    1 
ATOM   7758  N  NH1   . ARG B 1 274 ? 124.835 121.040 137.033 1.00 63.75 1  274 ARG B NH1   1 
ATOM   7759  N  NH2   . ARG B 1 274 ? 126.278 120.237 135.448 1.00 63.75 ?  274 ARG B NH2   1 
ATOM   7760  N  N     . VAL B 1 275 ? 124.726 127.688 136.730 1.00 47.00 ?  275 VAL B N     1 
ATOM   7761  C  CA    . VAL B 1 275 ? 125.551 128.780 137.227 1.00 44.89 ?  275 VAL B CA    1 
ATOM   7762  C  C     . VAL B 1 275 ? 126.113 128.352 138.575 1.00 48.71 ?  275 VAL B C     1 
ATOM   7763  O  O     . VAL B 1 275 ? 125.358 127.912 139.451 1.00 51.14 ?  275 VAL B O     1 
ATOM   7764  C  CB    . VAL B 1 275 ? 124.744 130.085 137.352 1.00 45.84 ?  275 VAL B CB    1 
ATOM   7765  C  CG1   . VAL B 1 275 ? 125.489 131.076 138.202 1.00 45.29 ?  275 VAL B CG1   1 
ATOM   7766  C  CG2   . VAL B 1 275 ? 124.454 130.667 135.978 1.00 43.95 ?  275 VAL B CG2   1 
ATOM   7767  N  N     . LYS B 1 276 ? 127.432 128.476 138.746 1.00 46.32 ?  276 LYS B N     1 
ATOM   7768  C  CA    . LYS B 1 276 ? 128.105 127.857 139.878 1.00 47.39 ?  276 LYS B CA    1 
ATOM   7769  C  C     . LYS B 1 276 ? 128.777 128.823 140.847 1.00 45.61 ?  276 LYS B C     1 
ATOM   7770  O  O     . LYS B 1 276 ? 128.981 128.447 142.007 1.00 51.16 ?  276 LYS B O     1 
ATOM   7771  C  CB    . LYS B 1 276 ? 129.150 126.841 139.383 1.00 48.20 ?  276 LYS B CB    1 
ATOM   7772  C  CG    . LYS B 1 276 ? 130.473 127.444 138.955 1.00 47.46 ?  276 LYS B CG    1 
ATOM   7773  C  CD    . LYS B 1 276 ? 131.217 126.522 138.006 1.00 50.60 ?  276 LYS B CD    1 
ATOM   7774  C  CE    . LYS B 1 276 ? 130.443 126.339 136.712 1.00 49.82 ?  276 LYS B CE    1 
ATOM   7775  N  NZ    . LYS B 1 276 ? 129.946 127.640 136.187 1.00 48.35 1  276 LYS B NZ    1 
ATOM   7776  N  N     . THR B 1 277 ? 129.129 130.037 140.426 1.00 37.24 ?  277 THR B N     1 
ATOM   7777  C  CA    . THR B 1 277 ? 129.740 131.008 141.327 1.00 36.87 ?  277 THR B CA    1 
ATOM   7778  C  C     . THR B 1 277 ? 128.796 132.128 141.737 1.00 38.11 ?  277 THR B C     1 
ATOM   7779  O  O     . THR B 1 277 ? 129.236 133.085 142.383 1.00 42.20 ?  277 THR B O     1 
ATOM   7780  C  CB    . THR B 1 277 ? 131.000 131.620 140.698 1.00 39.89 ?  277 THR B CB    1 
ATOM   7781  O  OG1   . THR B 1 277 ? 130.643 132.774 139.928 1.00 37.56 ?  277 THR B OG1   1 
ATOM   7782  C  CG2   . THR B 1 277 ? 131.701 130.614 139.811 1.00 40.45 ?  277 THR B CG2   1 
ATOM   7783  N  N     . LEU B 1 278 ? 127.519 132.039 141.386 1.00 29.21 ?  278 LEU B N     1 
ATOM   7784  C  CA    . LEU B 1 278 ? 126.540 133.077 141.690 1.00 29.10 ?  278 LEU B CA    1 
ATOM   7785  C  C     . LEU B 1 278 ? 125.451 132.474 142.567 1.00 23.31 ?  278 LEU B C     1 
ATOM   7786  O  O     . LEU B 1 278 ? 124.666 131.640 142.105 1.00 29.21 ?  278 LEU B O     1 
ATOM   7787  C  CB    . LEU B 1 278 ? 125.958 133.662 140.405 1.00 26.18 ?  278 LEU B CB    1 
ATOM   7788  C  CG    . LEU B 1 278 ? 125.011 134.855 140.480 1.00 26.72 ?  278 LEU B CG    1 
ATOM   7789  C  CD1   . LEU B 1 278 ? 125.791 136.145 140.602 1.00 23.26 ?  278 LEU B CD1   1 
ATOM   7790  C  CD2   . LEU B 1 278 ? 124.123 134.881 139.249 1.00 23.82 ?  278 LEU B CD2   1 
ATOM   7791  N  N     . SER B 1 279 ? 125.409 132.894 143.827 1.00 23.24 ?  279 SER B N     1 
ATOM   7792  C  CA    . SER B 1 279 ? 124.350 132.461 144.727 1.00 18.49 ?  279 SER B CA    1 
ATOM   7793  C  C     . SER B 1 279 ? 123.007 132.999 144.252 1.00 19.07 ?  279 SER B C     1 
ATOM   7794  O  O     . SER B 1 279 ? 122.927 134.033 143.586 1.00 29.86 ?  279 SER B O     1 
ATOM   7795  C  CB    . SER B 1 279 ? 124.632 132.936 146.150 1.00 17.19 ?  279 SER B CB    1 
ATOM   7796  O  OG    . SER B 1 279 ? 125.866 132.427 146.622 1.00 23.76 ?  279 SER B OG    1 
ATOM   7797  N  N     . ILE B 1 280 ? 121.941 132.282 144.589 1.00 20.84 ?  280 ILE B N     1 
ATOM   7798  C  CA    . ILE B 1 280 ? 120.602 132.648 144.153 1.00 19.36 ?  280 ILE B CA    1 
ATOM   7799  C  C     . ILE B 1 280 ? 119.731 132.882 145.378 1.00 20.82 ?  280 ILE B C     1 
ATOM   7800  O  O     . ILE B 1 280 ? 119.854 132.180 146.388 1.00 24.93 ?  280 ILE B O     1 
ATOM   7801  C  CB    . ILE B 1 280 ? 119.983 131.585 143.220 1.00 16.70 ?  280 ILE B CB    1 
ATOM   7802  C  CG1   . ILE B 1 280 ? 119.642 130.301 143.971 1.00 22.49 ?  280 ILE B CG1   1 
ATOM   7803  C  CG2   . ILE B 1 280 ? 120.942 131.246 142.106 1.00 25.14 ?  280 ILE B CG2   1 
ATOM   7804  C  CD1   . ILE B 1 280 ? 118.608 129.455 143.260 1.00 21.68 ?  280 ILE B CD1   1 
ATOM   7805  N  N     . GLY B 1 281 ? 118.883 133.897 145.297 1.00 11.91 ?  281 GLY B N     1 
ATOM   7806  C  CA    . GLY B 1 281 ? 117.910 134.161 146.334 1.00 6.43  ?  281 GLY B CA    1 
ATOM   7807  C  C     . GLY B 1 281 ? 116.547 134.400 145.724 1.00 8.98  ?  281 GLY B C     1 
ATOM   7808  O  O     . GLY B 1 281 ? 116.420 134.924 144.618 1.00 18.68 ?  281 GLY B O     1 
ATOM   7809  N  N     . VAL B 1 282 ? 115.519 133.999 146.463 1.00 8.40  ?  282 VAL B N     1 
ATOM   7810  C  CA    . VAL B 1 282 ? 114.136 134.115 146.018 1.00 14.89 ?  282 VAL B CA    1 
ATOM   7811  C  C     . VAL B 1 282 ? 113.392 135.010 146.996 1.00 11.81 ?  282 VAL B C     1 
ATOM   7812  O  O     . VAL B 1 282 ? 113.449 134.795 148.212 1.00 18.21 ?  282 VAL B O     1 
ATOM   7813  C  CB    . VAL B 1 282 ? 113.460 132.736 145.902 1.00 13.09 ?  282 VAL B CB    1 
ATOM   7814  C  CG1   . VAL B 1 282 ? 111.958 132.889 145.788 1.00 15.57 ?  282 VAL B CG1   1 
ATOM   7815  C  CG2   . VAL B 1 282 ? 114.003 131.990 144.700 1.00 19.32 ?  282 VAL B CG2   1 
ATOM   7816  N  N     . VAL B 1 283 ? 112.706 136.016 146.464 1.00 7.35  ?  283 VAL B N     1 
ATOM   7817  C  CA    . VAL B 1 283 ? 111.924 136.952 147.260 1.00 10.05 ?  283 VAL B CA    1 
ATOM   7818  C  C     . VAL B 1 283 ? 110.465 136.529 147.181 1.00 12.37 ?  283 VAL B C     1 
ATOM   7819  O  O     . VAL B 1 283 ? 109.865 136.536 146.099 1.00 22.54 ?  283 VAL B O     1 
ATOM   7820  C  CB    . VAL B 1 283 ? 112.117 138.394 146.773 1.00 6.35  ?  283 VAL B CB    1 
ATOM   7821  C  CG1   . VAL B 1 283 ? 111.390 139.361 147.687 1.00 9.67  ?  283 VAL B CG1   1 
ATOM   7822  C  CG2   . VAL B 1 283 ? 113.597 138.724 146.704 1.00 8.67  ?  283 VAL B CG2   1 
ATOM   7823  N  N     . ILE B 1 284 ? 109.895 136.161 148.322 1.00 17.09 ?  284 ILE B N     1 
ATOM   7824  C  CA    . ILE B 1 284 ? 108.556 135.588 148.396 1.00 17.92 ?  284 ILE B CA    1 
ATOM   7825  C  C     . ILE B 1 284 ? 107.647 136.594 149.098 1.00 17.41 ?  284 ILE B C     1 
ATOM   7826  O  O     . ILE B 1 284 ? 107.769 136.795 150.316 1.00 19.60 ?  284 ILE B O     1 
ATOM   7827  C  CB    . ILE B 1 284 ? 108.559 134.240 149.129 1.00 12.85 ?  284 ILE B CB    1 
ATOM   7828  C  CG1   . ILE B 1 284 ? 109.637 133.323 148.552 1.00 13.68 ?  284 ILE B CG1   1 
ATOM   7829  C  CG2   . ILE B 1 284 ? 107.190 133.587 149.044 1.00 17.19 ?  284 ILE B CG2   1 
ATOM   7830  C  CD1   . ILE B 1 284 ? 109.615 131.923 149.115 1.00 15.71 ?  284 ILE B CD1   1 
ATOM   7831  N  N     . PRO B 1 285 ? 106.732 137.246 148.388 1.00 22.30 ?  285 PRO B N     1 
ATOM   7832  C  CA    . PRO B 1 285 ? 105.710 138.049 149.063 1.00 25.67 ?  285 PRO B CA    1 
ATOM   7833  C  C     . PRO B 1 285 ? 104.719 137.165 149.804 1.00 25.21 ?  285 PRO B C     1 
ATOM   7834  O  O     . PRO B 1 285 ? 104.648 135.951 149.600 1.00 24.82 ?  285 PRO B O     1 
ATOM   7835  C  CB    . PRO B 1 285 ? 105.029 138.805 147.916 1.00 23.16 ?  285 PRO B CB    1 
ATOM   7836  C  CG    . PRO B 1 285 ? 105.986 138.722 146.770 1.00 19.61 ?  285 PRO B CG    1 
ATOM   7837  C  CD    . PRO B 1 285 ? 106.690 137.414 146.927 1.00 16.49 ?  285 PRO B CD    1 
ATOM   7838  N  N     . ASP B 1 286 ? 103.947 137.799 150.690 1.00 29.11 ?  286 ASP B N     1 
ATOM   7839  C  CA    . ASP B 1 286 ? 102.915 137.076 151.425 1.00 23.66 ?  286 ASP B CA    1 
ATOM   7840  C  C     . ASP B 1 286 ? 101.844 136.509 150.505 1.00 30.67 ?  286 ASP B C     1 
ATOM   7841  O  O     . ASP B 1 286 ? 101.174 135.540 150.877 1.00 32.81 ?  286 ASP B O     1 
ATOM   7842  C  CB    . ASP B 1 286 ? 102.273 137.990 152.468 1.00 26.22 ?  286 ASP B CB    1 
ATOM   7843  C  CG    . ASP B 1 286 ? 102.795 137.735 153.867 1.00 37.25 ?  286 ASP B CG    1 
ATOM   7844  O  OD1   . ASP B 1 286 ? 104.008 137.477 154.012 1.00 38.58 ?  286 ASP B OD1   1 
ATOM   7845  O  OD2   . ASP B 1 286 ? 101.993 137.796 154.822 1.00 39.34 -1 286 ASP B OD2   1 
ATOM   7846  N  N     . LYS B 1 287 ? 101.668 137.095 149.317 1.00 33.03 ?  287 LYS B N     1 
ATOM   7847  C  CA    . LYS B 1 287 ? 100.678 136.584 148.375 1.00 25.93 ?  287 LYS B CA    1 
ATOM   7848  C  C     . LYS B 1 287 ? 101.006 135.160 147.942 1.00 26.93 ?  287 LYS B C     1 
ATOM   7849  O  O     . LYS B 1 287 ? 100.107 134.320 147.825 1.00 33.99 ?  287 LYS B O     1 
ATOM   7850  C  CB    . LYS B 1 287 ? 100.586 137.505 147.160 1.00 27.63 ?  287 LYS B CB    1 
ATOM   7851  C  CG    . LYS B 1 287 ? 99.408  137.205 146.251 1.00 27.80 ?  287 LYS B CG    1 
ATOM   7852  C  CD    . LYS B 1 287 ? 98.108  137.188 147.035 1.00 32.66 ?  287 LYS B CD    1 
ATOM   7853  C  CE    . LYS B 1 287 ? 96.910  137.022 146.120 1.00 31.91 ?  287 LYS B CE    1 
ATOM   7854  N  NZ    . LYS B 1 287 ? 95.629  137.158 146.863 1.00 33.82 1  287 LYS B NZ    1 
ATOM   7855  N  N     . PHE B 1 288 ? 102.284 134.873 147.689 1.00 26.58 ?  288 PHE B N     1 
ATOM   7856  C  CA    . PHE B 1 288 ? 102.666 133.525 147.276 1.00 23.20 ?  288 PHE B CA    1 
ATOM   7857  C  C     . PHE B 1 288 ? 102.392 132.510 148.377 1.00 22.50 ?  288 PHE B C     1 
ATOM   7858  O  O     . PHE B 1 288 ? 101.898 131.409 148.109 1.00 30.53 ?  288 PHE B O     1 
ATOM   7859  C  CB    . PHE B 1 288 ? 104.139 133.493 146.875 1.00 27.79 ?  288 PHE B CB    1 
ATOM   7860  C  CG    . PHE B 1 288 ? 104.584 132.169 146.325 1.00 26.67 ?  288 PHE B CG    1 
ATOM   7861  C  CD1   . PHE B 1 288 ? 104.376 131.855 144.994 1.00 23.90 ?  288 PHE B CD1   1 
ATOM   7862  C  CD2   . PHE B 1 288 ? 105.200 131.235 147.141 1.00 23.29 ?  288 PHE B CD2   1 
ATOM   7863  C  CE1   . PHE B 1 288 ? 104.778 130.638 144.484 1.00 28.59 ?  288 PHE B CE1   1 
ATOM   7864  C  CE2   . PHE B 1 288 ? 105.603 130.015 146.637 1.00 24.98 ?  288 PHE B CE2   1 
ATOM   7865  C  CZ    . PHE B 1 288 ? 105.394 129.717 145.307 1.00 26.34 ?  288 PHE B CZ    1 
ATOM   7866  N  N     . VAL B 1 289 ? 102.717 132.860 149.623 1.00 25.75 ?  289 VAL B N     1 
ATOM   7867  C  CA    . VAL B 1 289 ? 102.459 131.958 150.739 1.00 26.07 ?  289 VAL B CA    1 
ATOM   7868  C  C     . VAL B 1 289 ? 100.961 131.754 150.923 1.00 26.59 ?  289 VAL B C     1 
ATOM   7869  O  O     . VAL B 1 289 ? 100.506 130.651 151.240 1.00 29.88 ?  289 VAL B O     1 
ATOM   7870  C  CB    . VAL B 1 289 ? 103.122 132.492 152.021 1.00 31.81 ?  289 VAL B CB    1 
ATOM   7871  C  CG1   . VAL B 1 289 ? 103.008 131.474 153.143 1.00 23.07 ?  289 VAL B CG1   1 
ATOM   7872  C  CG2   . VAL B 1 289 ? 104.577 132.844 151.757 1.00 25.12 ?  289 VAL B CG2   1 
ATOM   7873  N  N     . GLU B 1 290 ? 100.173 132.813 150.730 1.00 34.76 ?  290 GLU B N     1 
ATOM   7874  C  CA    . GLU B 1 290 ? 98.722  132.686 150.822 1.00 30.92 ?  290 GLU B CA    1 
ATOM   7875  C  C     . GLU B 1 290 ? 98.176  131.766 149.736 1.00 34.54 ?  290 GLU B C     1 
ATOM   7876  O  O     . GLU B 1 290 ? 97.310  130.924 150.001 1.00 39.59 ?  290 GLU B O     1 
ATOM   7877  C  CB    . GLU B 1 290 ? 98.076  134.069 150.741 1.00 28.23 ?  290 GLU B CB    1 
ATOM   7878  C  CG    . GLU B 1 290 ? 96.693  134.087 150.114 1.00 37.04 ?  290 GLU B CG    1 
ATOM   7879  C  CD    . GLU B 1 290 ? 96.059  135.462 150.150 1.00 41.41 ?  290 GLU B CD    1 
ATOM   7880  O  OE1   . GLU B 1 290 ? 96.070  136.095 151.226 1.00 42.37 ?  290 GLU B OE1   1 
ATOM   7881  O  OE2   . GLU B 1 290 ? 95.551  135.912 149.101 1.00 38.39 -1 290 GLU B OE2   1 
ATOM   7882  N  N     . LEU B 1 291 ? 98.675  131.910 148.506 1.00 27.28 ?  291 LEU B N     1 
ATOM   7883  C  CA    . LEU B 1 291 ? 98.227  131.049 147.413 1.00 25.18 ?  291 LEU B CA    1 
ATOM   7884  C  C     . LEU B 1 291 ? 98.614  129.596 147.657 1.00 32.91 ?  291 LEU B C     1 
ATOM   7885  O  O     . LEU B 1 291 ? 97.817  128.686 147.400 1.00 37.34 ?  291 LEU B O     1 
ATOM   7886  C  CB    . LEU B 1 291 ? 98.804  131.539 146.085 1.00 29.43 ?  291 LEU B CB    1 
ATOM   7887  C  CG    . LEU B 1 291 ? 98.315  132.895 145.574 1.00 29.44 ?  291 LEU B CG    1 
ATOM   7888  C  CD1   . LEU B 1 291 ? 99.309  133.481 144.589 1.00 26.20 ?  291 LEU B CD1   1 
ATOM   7889  C  CD2   . LEU B 1 291 ? 96.942  132.768 144.942 1.00 32.36 ?  291 LEU B CD2   1 
ATOM   7890  N  N     . ALA B 1 292 ? 99.836  129.357 148.137 1.00 32.40 ?  292 ALA B N     1 
ATOM   7891  C  CA    . ALA B 1 292 ? 100.260 127.994 148.437 1.00 27.35 ?  292 ALA B CA    1 
ATOM   7892  C  C     . ALA B 1 292 ? 99.441  127.399 149.577 1.00 29.21 ?  292 ALA B C     1 
ATOM   7893  O  O     . ALA B 1 292 ? 99.098  126.212 149.549 1.00 36.30 ?  292 ALA B O     1 
ATOM   7894  C  CB    . ALA B 1 292 ? 101.750 127.968 148.774 1.00 27.19 ?  292 ALA B CB    1 
ATOM   7895  N  N     . ARG B 1 293 ? 99.126  128.210 150.589 1.00 28.11 ?  293 ARG B N     1 
ATOM   7896  C  CA    . ARG B 1 293 ? 98.336  127.730 151.717 1.00 28.07 ?  293 ARG B CA    1 
ATOM   7897  C  C     . ARG B 1 293 ? 96.941  127.306 151.277 1.00 35.25 ?  293 ARG B C     1 
ATOM   7898  O  O     . ARG B 1 293 ? 96.429  126.272 151.718 1.00 39.63 ?  293 ARG B O     1 
ATOM   7899  C  CB    . ARG B 1 293 ? 98.261  128.817 152.788 1.00 29.39 ?  293 ARG B CB    1 
ATOM   7900  C  CG    . ARG B 1 293 ? 97.180  128.615 153.833 1.00 31.61 ?  293 ARG B CG    1 
ATOM   7901  C  CD    . ARG B 1 293 ? 96.975  129.886 154.635 1.00 32.58 ?  293 ARG B CD    1 
ATOM   7902  N  NE    . ARG B 1 293 ? 98.246  130.465 155.053 1.00 38.76 ?  293 ARG B NE    1 
ATOM   7903  C  CZ    . ARG B 1 293 ? 98.606  131.722 154.831 1.00 37.05 ?  293 ARG B CZ    1 
ATOM   7904  N  NH1   . ARG B 1 293 ? 97.807  132.569 154.204 1.00 36.91 1  293 ARG B NH1   1 
ATOM   7905  N  NH2   . ARG B 1 293 ? 99.800  132.137 155.244 1.00 29.92 ?  293 ARG B NH2   1 
ATOM   7906  N  N     . GLU B 1 294 ? 96.315  128.089 150.402 1.00 44.02 ?  294 GLU B N     1 
ATOM   7907  C  CA    . GLU B 1 294 ? 94.980  127.787 149.906 1.00 41.02 ?  294 GLU B CA    1 
ATOM   7908  C  C     . GLU B 1 294 ? 94.986  126.798 148.749 1.00 42.10 ?  294 GLU B C     1 
ATOM   7909  O  O     . GLU B 1 294 ? 93.909  126.430 148.268 1.00 46.91 ?  294 GLU B O     1 
ATOM   7910  C  CB    . GLU B 1 294 ? 94.280  129.079 149.480 1.00 37.63 ?  294 GLU B CB    1 
ATOM   7911  C  CG    . GLU B 1 294 ? 94.146  130.102 150.597 1.00 42.57 ?  294 GLU B CG    1 
ATOM   7912  C  CD    . GLU B 1 294 ? 93.656  131.448 150.102 1.00 48.77 ?  294 GLU B CD    1 
ATOM   7913  O  OE1   . GLU B 1 294 ? 93.477  131.603 148.877 1.00 48.12 ?  294 GLU B OE1   1 
ATOM   7914  O  OE2   . GLU B 1 294 ? 93.451  132.351 150.939 1.00 45.21 -1 294 GLU B OE2   1 
ATOM   7915  N  N     . ASP B 1 295 ? 96.165  126.374 148.290 1.00 39.29 ?  295 ASP B N     1 
ATOM   7916  C  CA    . ASP B 1 295 ? 96.327  125.421 147.194 1.00 41.69 ?  295 ASP B CA    1 
ATOM   7917  C  C     . ASP B 1 295 ? 95.742  125.935 145.883 1.00 45.58 ?  295 ASP B C     1 
ATOM   7918  O  O     . ASP B 1 295 ? 95.506  125.153 144.955 1.00 46.25 ?  295 ASP B O     1 
ATOM   7919  C  CB    . ASP B 1 295 ? 95.720  124.056 147.543 1.00 45.70 ?  295 ASP B CB    1 
ATOM   7920  C  CG    . ASP B 1 295 ? 96.561  122.900 147.042 1.00 50.22 ?  295 ASP B CG    1 
ATOM   7921  O  OD1   . ASP B 1 295 ? 96.516  121.818 147.663 1.00 47.79 ?  295 ASP B OD1   1 
ATOM   7922  O  OD2   . ASP B 1 295 ? 97.269  123.074 146.028 1.00 47.83 -1 295 ASP B OD2   1 
ATOM   7923  N  N     . LYS B 1 296 ? 95.501  127.240 145.785 1.00 45.81 ?  296 LYS B N     1 
ATOM   7924  C  CA    . LYS B 1 296 ? 95.024  127.835 144.547 1.00 44.99 ?  296 LYS B CA    1 
ATOM   7925  C  C     . LYS B 1 296 ? 96.191  128.031 143.591 1.00 46.34 ?  296 LYS B C     1 
ATOM   7926  O  O     . LYS B 1 296 ? 97.250  128.527 143.988 1.00 48.28 ?  296 LYS B O     1 
ATOM   7927  C  CB    . LYS B 1 296 ? 94.335  129.170 144.829 1.00 45.13 ?  296 LYS B CB    1 
ATOM   7928  C  CG    . LYS B 1 296 ? 93.094  129.055 145.697 1.00 46.13 ?  296 LYS B CG    1 
ATOM   7929  C  CD    . LYS B 1 296 ? 92.493  130.420 145.989 1.00 46.16 ?  296 LYS B CD    1 
ATOM   7930  C  CE    . LYS B 1 296 ? 91.197  130.296 146.774 1.00 47.56 ?  296 LYS B CE    1 
ATOM   7931  N  NZ    . LYS B 1 296 ? 90.739  131.611 147.303 1.00 45.77 1  296 LYS B NZ    1 
ATOM   7932  N  N     . ALA B 1 297 ? 96.002  127.637 142.333 1.00 44.65 ?  297 ALA B N     1 
ATOM   7933  C  CA    . ALA B 1 297 ? 97.061  127.768 141.341 1.00 43.38 ?  297 ALA B CA    1 
ATOM   7934  C  C     . ALA B 1 297 ? 97.447  129.230 141.168 1.00 42.38 ?  297 ALA B C     1 
ATOM   7935  O  O     . ALA B 1 297 ? 96.587  130.100 141.003 1.00 44.72 ?  297 ALA B O     1 
ATOM   7936  C  CB    . ALA B 1 297 ? 96.613  127.174 140.007 1.00 42.71 ?  297 ALA B CB    1 
ATOM   7937  N  N     . ALA B 1 298 ? 98.748  129.498 141.207 1.00 34.57 ?  298 ALA B N     1 
ATOM   7938  C  CA    . ALA B 1 298 ? 99.249  130.859 141.136 1.00 33.18 ?  298 ALA B CA    1 
ATOM   7939  C  C     . ALA B 1 298 ? 99.664  131.199 139.710 1.00 35.87 ?  298 ALA B C     1 
ATOM   7940  O  O     . ALA B 1 298 ? 99.664  130.355 138.813 1.00 40.21 ?  298 ALA B O     1 
ATOM   7941  C  CB    . ALA B 1 298 ? 100.423 131.048 142.095 1.00 34.50 ?  298 ALA B CB    1 
ATOM   7942  N  N     . TYR B 1 299 ? 100.032 132.459 139.506 1.00 36.18 ?  299 TYR B N     1 
ATOM   7943  C  CA    . TYR B 1 299 ? 100.467 132.936 138.202 1.00 25.69 ?  299 TYR B CA    1 
ATOM   7944  C  C     . TYR B 1 299 ? 101.776 133.692 138.352 1.00 27.90 ?  299 TYR B C     1 
ATOM   7945  O  O     . TYR B 1 299 ? 101.869 134.626 139.155 1.00 34.61 ?  299 TYR B O     1 
ATOM   7946  C  CB    . TYR B 1 299 ? 99.408  133.836 137.562 1.00 30.33 ?  299 TYR B CB    1 
ATOM   7947  C  CG    . TYR B 1 299 ? 98.253  133.081 136.944 1.00 31.78 ?  299 TYR B CG    1 
ATOM   7948  C  CD1   . TYR B 1 299 ? 98.392  132.438 135.721 1.00 33.34 ?  299 TYR B CD1   1 
ATOM   7949  C  CD2   . TYR B 1 299 ? 97.020  133.020 137.579 1.00 32.79 ?  299 TYR B CD2   1 
ATOM   7950  C  CE1   . TYR B 1 299 ? 97.340  131.751 135.153 1.00 33.86 ?  299 TYR B CE1   1 
ATOM   7951  C  CE2   . TYR B 1 299 ? 95.960  132.335 137.018 1.00 33.08 ?  299 TYR B CE2   1 
ATOM   7952  C  CZ    . TYR B 1 299 ? 96.126  131.701 135.804 1.00 35.07 ?  299 TYR B CZ    1 
ATOM   7953  O  OH    . TYR B 1 299 ? 95.073  131.019 135.239 1.00 37.22 ?  299 TYR B OH    1 
ATOM   7954  N  N     . VAL B 1 300 ? 102.780 133.287 137.590 1.00 29.64 ?  300 VAL B N     1 
ATOM   7955  C  CA    . VAL B 1 300 ? 104.011 134.056 137.464 1.00 22.32 ?  300 VAL B CA    1 
ATOM   7956  C  C     . VAL B 1 300 ? 103.837 135.008 136.292 1.00 25.64 ?  300 VAL B C     1 
ATOM   7957  O  O     . VAL B 1 300 ? 103.092 134.726 135.353 1.00 30.12 ?  300 VAL B O     1 
ATOM   7958  C  CB    . VAL B 1 300 ? 105.241 133.142 137.285 1.00 24.45 ?  300 VAL B CB    1 
ATOM   7959  C  CG1   . VAL B 1 300 ? 105.599 132.479 138.603 1.00 23.16 ?  300 VAL B CG1   1 
ATOM   7960  C  CG2   . VAL B 1 300 ? 104.979 132.101 136.210 1.00 26.14 ?  300 VAL B CG2   1 
ATOM   7961  N  N     . PHE B 1 301 ? 104.516 136.147 136.340 1.00 25.84 ?  301 PHE B N     1 
ATOM   7962  C  CA    . PHE B 1 301 ? 104.213 137.235 135.427 1.00 20.81 ?  301 PHE B CA    1 
ATOM   7963  C  C     . PHE B 1 301 ? 105.428 137.620 134.596 1.00 28.11 ?  301 PHE B C     1 
ATOM   7964  O  O     . PHE B 1 301 ? 106.579 137.423 134.995 1.00 29.52 ?  301 PHE B O     1 
ATOM   7965  C  CB    . PHE B 1 301 ? 103.698 138.458 136.190 1.00 24.66 ?  301 PHE B CB    1 
ATOM   7966  C  CG    . PHE B 1 301 ? 102.468 138.184 136.999 1.00 27.51 ?  301 PHE B CG    1 
ATOM   7967  C  CD1   . PHE B 1 301 ? 101.244 138.005 136.380 1.00 26.92 ?  301 PHE B CD1   1 
ATOM   7968  C  CD2   . PHE B 1 301 ? 102.535 138.100 138.378 1.00 25.39 ?  301 PHE B CD2   1 
ATOM   7969  C  CE1   . PHE B 1 301 ? 100.112 137.745 137.119 1.00 27.62 ?  301 PHE B CE1   1 
ATOM   7970  C  CE2   . PHE B 1 301 ? 101.405 137.843 139.122 1.00 28.97 ?  301 PHE B CE2   1 
ATOM   7971  C  CZ    . PHE B 1 301 ? 100.191 137.667 138.492 1.00 28.06 ?  301 PHE B CZ    1 
ATOM   7972  N  N     . TYR B 1 302 ? 105.140 138.177 133.419 1.00 25.95 ?  302 TYR B N     1 
ATOM   7973  C  CA    . TYR B 1 302 ? 106.166 138.743 132.558 1.00 26.54 ?  302 TYR B CA    1 
ATOM   7974  C  C     . TYR B 1 302 ? 106.364 140.197 132.959 1.00 29.50 ?  302 TYR B C     1 
ATOM   7975  O  O     . TYR B 1 302 ? 105.426 140.997 132.823 1.00 30.63 ?  302 TYR B O     1 
ATOM   7976  C  CB    . TYR B 1 302 ? 105.756 138.642 131.096 1.00 25.74 ?  302 TYR B CB    1 
ATOM   7977  C  CG    . TYR B 1 302 ? 105.806 137.238 130.538 1.00 27.02 ?  302 TYR B CG    1 
ATOM   7978  C  CD1   . TYR B 1 302 ? 104.837 136.302 130.872 1.00 25.03 ?  302 TYR B CD1   1 
ATOM   7979  C  CD2   . TYR B 1 302 ? 106.820 136.850 129.676 1.00 27.54 ?  302 TYR B CD2   1 
ATOM   7980  C  CE1   . TYR B 1 302 ? 104.878 135.022 130.364 1.00 25.70 ?  302 TYR B CE1   1 
ATOM   7981  C  CE2   . TYR B 1 302 ? 106.869 135.572 129.161 1.00 26.81 ?  302 TYR B CE2   1 
ATOM   7982  C  CZ    . TYR B 1 302 ? 105.895 134.662 129.509 1.00 30.33 ?  302 TYR B CZ    1 
ATOM   7983  O  OH    . TYR B 1 302 ? 105.943 133.386 128.999 1.00 33.17 ?  302 TYR B OH    1 
ATOM   7984  N  N     . PRO B 1 303 ? 107.535 140.581 133.472 1.00 28.05 ?  303 PRO B N     1 
ATOM   7985  C  CA    . PRO B 1 303 ? 107.699 141.952 133.983 1.00 25.48 ?  303 PRO B CA    1 
ATOM   7986  C  C     . PRO B 1 303 ? 107.488 143.034 132.941 1.00 29.88 ?  303 PRO B C     1 
ATOM   7987  O  O     . PRO B 1 303 ? 106.979 144.110 133.280 1.00 30.10 ?  303 PRO B O     1 
ATOM   7988  C  CB    . PRO B 1 303 ? 109.141 141.957 134.508 1.00 23.10 ?  303 PRO B CB    1 
ATOM   7989  C  CG    . PRO B 1 303 ? 109.464 140.532 134.753 1.00 25.78 ?  303 PRO B CG    1 
ATOM   7990  C  CD    . PRO B 1 303 ? 108.727 139.754 133.712 1.00 22.71 ?  303 PRO B CD    1 
ATOM   7991  N  N     . HIS B 1 304 ? 107.865 142.790 131.684 1.00 29.63 ?  304 HIS B N     1 
ATOM   7992  C  CA    . HIS B 1 304 ? 107.798 143.853 130.687 1.00 29.90 ?  304 HIS B CA    1 
ATOM   7993  C  C     . HIS B 1 304 ? 106.358 144.191 130.328 1.00 31.79 ?  304 HIS B C     1 
ATOM   7994  O  O     . HIS B 1 304 ? 106.033 145.359 130.090 1.00 37.64 ?  304 HIS B O     1 
ATOM   7995  C  CB    . HIS B 1 304 ? 108.580 143.467 129.437 1.00 27.70 ?  304 HIS B CB    1 
ATOM   7996  C  CG    . HIS B 1 304 ? 108.697 144.574 128.439 1.00 28.80 ?  304 HIS B CG    1 
ATOM   7997  N  ND1   . HIS B 1 304 ? 108.958 145.877 128.804 1.00 27.07 ?  304 HIS B ND1   1 
ATOM   7998  C  CD2   . HIS B 1 304 ? 108.583 144.577 127.090 1.00 35.59 ?  304 HIS B CD2   1 
ATOM   7999  C  CE1   . HIS B 1 304 ? 109.003 146.634 127.723 1.00 30.15 ?  304 HIS B CE1   1 
ATOM   8000  N  NE2   . HIS B 1 304 ? 108.779 145.870 126.669 1.00 35.61 ?  304 HIS B NE2   1 
ATOM   8001  N  N     . THR B 1 305 ? 105.481 143.187 130.272 1.00 28.56 ?  305 THR B N     1 
ATOM   8002  C  CA    . THR B 1 305 ? 104.071 143.459 130.010 1.00 32.68 ?  305 THR B CA    1 
ATOM   8003  C  C     . THR B 1 305 ? 103.457 144.291 131.128 1.00 29.26 ?  305 THR B C     1 
ATOM   8004  O  O     . THR B 1 305 ? 102.693 145.229 130.871 1.00 34.96 ?  305 THR B O     1 
ATOM   8005  C  CB    . THR B 1 305 ? 103.308 142.147 129.835 1.00 30.45 ?  305 THR B CB    1 
ATOM   8006  O  OG1   . THR B 1 305 ? 103.332 141.411 131.064 1.00 28.12 ?  305 THR B OG1   1 
ATOM   8007  C  CG2   . THR B 1 305 ? 103.941 141.309 128.739 1.00 31.29 ?  305 THR B CG2   1 
ATOM   8008  N  N     . ILE B 1 306 ? 103.793 143.967 132.378 1.00 29.89 ?  306 ILE B N     1 
ATOM   8009  C  CA    . ILE B 1 306 ? 103.297 144.739 133.513 1.00 30.13 ?  306 ILE B CA    1 
ATOM   8010  C  C     . ILE B 1 306 ? 103.828 146.164 133.460 1.00 29.22 ?  306 ILE B C     1 
ATOM   8011  O  O     . ILE B 1 306 ? 103.096 147.126 133.728 1.00 34.03 ?  306 ILE B O     1 
ATOM   8012  C  CB    . ILE B 1 306 ? 103.671 144.039 134.831 1.00 26.76 ?  306 ILE B CB    1 
ATOM   8013  C  CG1   . ILE B 1 306 ? 102.845 142.766 135.006 1.00 26.49 ?  306 ILE B CG1   1 
ATOM   8014  C  CG2   . ILE B 1 306 ? 103.472 144.967 136.009 1.00 29.75 ?  306 ILE B CG2   1 
ATOM   8015  C  CD1   . ILE B 1 306 ? 103.196 141.987 136.239 1.00 28.94 ?  306 ILE B CD1   1 
ATOM   8016  N  N     . TYR B 1 307 ? 105.107 146.326 133.117 1.00 30.63 ?  307 TYR B N     1 
ATOM   8017  C  CA    . TYR B 1 307 ? 105.681 147.664 133.019 1.00 27.67 ?  307 TYR B CA    1 
ATOM   8018  C  C     . TYR B 1 307 ? 105.019 148.466 131.905 1.00 31.63 ?  307 TYR B C     1 
ATOM   8019  O  O     . TYR B 1 307 ? 104.769 149.666 132.061 1.00 35.31 ?  307 TYR B O     1 
ATOM   8020  C  CB    . TYR B 1 307 ? 107.193 147.571 132.807 1.00 24.46 ?  307 TYR B CB    1 
ATOM   8021  C  CG    . TYR B 1 307 ? 107.895 148.908 132.710 1.00 31.21 ?  307 TYR B CG    1 
ATOM   8022  C  CD1   . TYR B 1 307 ? 107.938 149.614 131.512 1.00 31.54 ?  307 TYR B CD1   1 
ATOM   8023  C  CD2   . TYR B 1 307 ? 108.502 149.473 133.823 1.00 26.86 ?  307 TYR B CD2   1 
ATOM   8024  C  CE1   . TYR B 1 307 ? 108.572 150.834 131.427 1.00 31.01 ?  307 TYR B CE1   1 
ATOM   8025  C  CE2   . TYR B 1 307 ? 109.137 150.693 133.746 1.00 29.82 ?  307 TYR B CE2   1 
ATOM   8026  C  CZ    . TYR B 1 307 ? 109.170 151.370 132.546 1.00 34.47 ?  307 TYR B CZ    1 
ATOM   8027  O  OH    . TYR B 1 307 ? 109.803 152.588 132.465 1.00 36.60 ?  307 TYR B OH    1 
ATOM   8028  N  N     . LYS B 1 308 ? 104.741 147.824 130.770 1.00 34.42 ?  308 LYS B N     1 
ATOM   8029  C  CA    . LYS B 1 308 ? 104.059 148.506 129.676 1.00 31.88 ?  308 LYS B CA    1 
ATOM   8030  C  C     . LYS B 1 308 ? 102.655 148.930 130.081 1.00 31.61 ?  308 LYS B C     1 
ATOM   8031  O  O     . LYS B 1 308 ? 102.220 150.045 129.770 1.00 36.40 ?  308 LYS B O     1 
ATOM   8032  C  CB    . LYS B 1 308 ? 104.008 147.599 128.447 1.00 32.36 ?  308 LYS B CB    1 
ATOM   8033  C  CG    . LYS B 1 308 ? 105.275 147.608 127.608 1.00 33.85 ?  308 LYS B CG    1 
ATOM   8034  C  CD    . LYS B 1 308 ? 105.495 146.282 126.885 1.00 35.89 ?  308 LYS B CD    1 
ATOM   8035  C  CE    . LYS B 1 308 ? 104.234 145.430 126.840 1.00 36.98 ?  308 LYS B CE    1 
ATOM   8036  N  NZ    . LYS B 1 308 ? 104.233 144.498 125.680 1.00 35.60 1  308 LYS B NZ    1 
ATOM   8037  N  N     . GLU B 1 309 ? 101.929 148.053 130.778 1.00 29.97 ?  309 GLU B N     1 
ATOM   8038  C  CA    . GLU B 1 309 ? 100.541 148.353 131.113 1.00 34.83 ?  309 GLU B CA    1 
ATOM   8039  C  C     . GLU B 1 309 ? 100.435 149.410 132.206 1.00 35.03 ?  309 GLU B C     1 
ATOM   8040  O  O     . GLU B 1 309 ? 99.604  150.321 132.115 1.00 37.16 ?  309 GLU B O     1 
ATOM   8041  C  CB    . GLU B 1 309 ? 99.818  147.075 131.536 1.00 32.85 ?  309 GLU B CB    1 
ATOM   8042  C  CG    . GLU B 1 309 ? 98.469  147.321 132.186 1.00 35.09 ?  309 GLU B CG    1 
ATOM   8043  C  CD    . GLU B 1 309 ? 97.439  147.879 131.223 1.00 40.22 ?  309 GLU B CD    1 
ATOM   8044  O  OE1   . GLU B 1 309 ? 97.636  147.759 129.996 1.00 40.62 ?  309 GLU B OE1   1 
ATOM   8045  O  OE2   . GLU B 1 309 ? 96.430  148.441 131.696 1.00 39.65 -1 309 GLU B OE2   1 
ATOM   8046  N  N     . TYR B 1 310 ? 101.265 149.314 133.245 1.00 33.44 ?  310 TYR B N     1 
ATOM   8047  C  CA    . TYR B 1 310 ? 101.119 150.157 134.422 1.00 33.04 ?  310 TYR B CA    1 
ATOM   8048  C  C     . TYR B 1 310 ? 102.171 151.251 134.535 1.00 31.90 ?  310 TYR B C     1 
ATOM   8049  O  O     . TYR B 1 310 ? 101.979 152.187 135.319 1.00 31.87 ?  310 TYR B O     1 
ATOM   8050  C  CB    . TYR B 1 310 ? 101.152 149.296 135.693 1.00 31.08 ?  310 TYR B CB    1 
ATOM   8051  C  CG    . TYR B 1 310 ? 100.058 148.255 135.749 1.00 32.59 ?  310 TYR B CG    1 
ATOM   8052  C  CD1   . TYR B 1 310 ? 98.797  148.570 136.237 1.00 31.36 ?  310 TYR B CD1   1 
ATOM   8053  C  CD2   . TYR B 1 310 ? 100.283 146.958 135.308 1.00 32.26 ?  310 TYR B CD2   1 
ATOM   8054  C  CE1   . TYR B 1 310 ? 97.794  147.623 136.288 1.00 33.04 ?  310 TYR B CE1   1 
ATOM   8055  C  CE2   . TYR B 1 310 ? 99.285  146.004 135.353 1.00 32.17 ?  310 TYR B CE2   1 
ATOM   8056  C  CZ    . TYR B 1 310 ? 98.044  146.342 135.846 1.00 33.62 ?  310 TYR B CZ    1 
ATOM   8057  O  OH    . TYR B 1 310 ? 97.048  145.396 135.895 1.00 34.39 ?  310 TYR B OH    1 
ATOM   8058  N  N     . GLY B 1 311 ? 103.263 151.168 133.782 1.00 29.63 ?  311 GLY B N     1 
ATOM   8059  C  CA    . GLY B 1 311 ? 104.329 152.140 133.891 1.00 29.67 ?  311 GLY B CA    1 
ATOM   8060  C  C     . GLY B 1 311 ? 105.297 151.900 135.026 1.00 34.53 ?  311 GLY B C     1 
ATOM   8061  O  O     . GLY B 1 311 ? 106.245 152.678 135.183 1.00 36.90 ?  311 GLY B O     1 
ATOM   8062  N  N     . GLN B 1 312 ? 105.091 150.853 135.821 1.00 31.52 ?  312 GLN B N     1 
ATOM   8063  C  CA    . GLN B 1 312 ? 105.969 150.520 136.930 1.00 29.78 ?  312 GLN B CA    1 
ATOM   8064  C  C     . GLN B 1 312 ? 106.368 149.055 136.835 1.00 32.31 ?  312 GLN B C     1 
ATOM   8065  O  O     . GLN B 1 312 ? 105.671 148.237 136.229 1.00 39.23 ?  312 GLN B O     1 
ATOM   8066  C  CB    . GLN B 1 312 ? 105.304 150.791 138.287 1.00 32.47 ?  312 GLN B CB    1 
ATOM   8067  C  CG    . GLN B 1 312 ? 104.223 151.857 138.257 1.00 31.94 ?  312 GLN B CG    1 
ATOM   8068  C  CD    . GLN B 1 312 ? 103.314 151.798 139.466 1.00 35.90 ?  312 GLN B CD    1 
ATOM   8069  O  OE1   . GLN B 1 312 ? 103.724 152.120 140.582 1.00 38.51 ?  312 GLN B OE1   1 
ATOM   8070  N  NE2   . GLN B 1 312 ? 102.071 151.384 139.253 1.00 33.65 ?  312 GLN B NE2   1 
ATOM   8071  N  N     . HIS B 1 313 ? 107.505 148.733 137.444 1.00 29.23 ?  313 HIS B N     1 
ATOM   8072  C  CA    . HIS B 1 313 ? 107.988 147.364 137.449 1.00 29.45 ?  313 HIS B CA    1 
ATOM   8073  C  C     . HIS B 1 313 ? 107.136 146.497 138.373 1.00 32.07 ?  313 HIS B C     1 
ATOM   8074  O  O     . HIS B 1 313 ? 106.470 146.984 139.290 1.00 32.39 ?  313 HIS B O     1 
ATOM   8075  C  CB    . HIS B 1 313 ? 109.454 147.318 137.876 1.00 26.13 ?  313 HIS B CB    1 
ATOM   8076  C  CG    . HIS B 1 313 ? 110.361 148.122 136.998 1.00 27.87 ?  313 HIS B CG    1 
ATOM   8077  N  ND1   . HIS B 1 313 ? 110.850 147.645 135.800 1.00 30.95 ?  313 HIS B ND1   1 
ATOM   8078  C  CD2   . HIS B 1 313 ? 110.865 149.370 137.138 1.00 29.49 ?  313 HIS B CD2   1 
ATOM   8079  C  CE1   . HIS B 1 313 ? 111.617 148.564 135.243 1.00 28.56 ?  313 HIS B CE1   1 
ATOM   8080  N  NE2   . HIS B 1 313 ? 111.642 149.621 136.035 1.00 30.09 ?  313 HIS B NE2   1 
ATOM   8081  N  N     . MET B 1 314 ? 107.162 145.187 138.111 1.00 35.31 ?  314 MET B N     1 
ATOM   8082  C  CA    . MET B 1 314 ? 106.354 144.259 138.897 1.00 30.43 ?  314 MET B CA    1 
ATOM   8083  C  C     . MET B 1 314 ? 106.780 144.254 140.360 1.00 37.07 ?  314 MET B C     1 
ATOM   8084  O  O     . MET B 1 314 ? 105.933 144.206 141.260 1.00 39.69 ?  314 MET B O     1 
ATOM   8085  C  CB    . MET B 1 314 ? 106.445 142.852 138.309 1.00 28.98 ?  314 MET B CB    1 
ATOM   8086  C  CG    . MET B 1 314 ? 105.533 141.850 138.993 1.00 29.54 ?  314 MET B CG    1 
ATOM   8087  S  SD    . MET B 1 314 ? 106.110 140.145 138.917 1.00 45.32 ?  314 MET B SD    1 
ATOM   8088  C  CE    . MET B 1 314 ? 107.218 140.218 137.517 1.00 30.08 ?  314 MET B CE    1 
ATOM   8089  N  N     . ASP B 1 315 ? 108.084 144.303 140.619 1.00 30.29 ?  315 ASP B N     1 
ATOM   8090  C  CA    . ASP B 1 315 ? 108.588 144.335 141.986 1.00 34.42 ?  315 ASP B CA    1 
ATOM   8091  C  C     . ASP B 1 315 ? 108.575 145.733 142.587 1.00 30.20 ?  315 ASP B C     1 
ATOM   8092  O  O     . ASP B 1 315 ? 108.956 145.893 143.751 1.00 36.93 ?  315 ASP B O     1 
ATOM   8093  C  CB    . ASP B 1 315 ? 110.006 143.759 142.039 1.00 33.18 ?  315 ASP B CB    1 
ATOM   8094  C  CG    . ASP B 1 315 ? 111.001 144.590 141.259 1.00 32.79 ?  315 ASP B CG    1 
ATOM   8095  O  OD1   . ASP B 1 315 ? 110.583 145.265 140.295 1.00 36.65 ?  315 ASP B OD1   1 
ATOM   8096  O  OD2   . ASP B 1 315 ? 112.198 144.569 141.608 1.00 29.78 -1 315 ASP B OD2   1 
ATOM   8097  N  N     . GLU B 1 316 ? 108.150 146.743 141.827 1.00 28.38 ?  316 GLU B N     1 
ATOM   8098  C  CA    . GLU B 1 316 ? 108.067 148.106 142.333 1.00 29.96 ?  316 GLU B CA    1 
ATOM   8099  C  C     . GLU B 1 316 ? 106.777 148.382 143.095 1.00 35.54 ?  316 GLU B C     1 
ATOM   8100  O  O     . GLU B 1 316 ? 106.673 149.433 143.736 1.00 39.07 ?  316 GLU B O     1 
ATOM   8101  C  CB    . GLU B 1 316 ? 108.191 149.102 141.177 1.00 36.44 ?  316 GLU B CB    1 
ATOM   8102  C  CG    . GLU B 1 316 ? 109.602 149.608 140.923 1.00 34.69 ?  316 GLU B CG    1 
ATOM   8103  C  CD    . GLU B 1 316 ? 110.397 149.809 142.196 1.00 36.36 ?  316 GLU B CD    1 
ATOM   8104  O  OE1   . GLU B 1 316 ? 109.946 150.580 143.070 1.00 38.09 ?  316 GLU B OE1   1 
ATOM   8105  O  OE2   . GLU B 1 316 ? 111.478 149.199 142.321 1.00 41.39 -1 316 GLU B OE2   1 
ATOM   8106  N  N     . MET B 1 317 ? 105.802 147.480 143.040 1.00 38.06 ?  317 MET B N     1 
ATOM   8107  C  CA    . MET B 1 317 ? 104.520 147.678 143.698 1.00 38.40 ?  317 MET B CA    1 
ATOM   8108  C  C     . MET B 1 317 ? 104.142 146.434 144.491 1.00 37.91 ?  317 MET B C     1 
ATOM   8109  O  O     . MET B 1 317 ? 104.771 145.379 144.382 1.00 37.39 ?  317 MET B O     1 
ATOM   8110  C  CB    . MET B 1 317 ? 103.417 148.030 142.690 1.00 40.05 ?  317 MET B CB    1 
ATOM   8111  C  CG    . MET B 1 317 ? 103.559 147.359 141.338 1.00 34.68 ?  317 MET B CG    1 
ATOM   8112  S  SD    . MET B 1 317 ? 102.871 148.391 140.031 1.00 48.10 ?  317 MET B SD    1 
ATOM   8113  C  CE    . MET B 1 317 ? 103.210 147.389 138.591 1.00 33.99 ?  317 MET B CE    1 
ATOM   8114  N  N     . ASP B 1 318 ? 103.089 146.578 145.294 1.00 40.30 ?  318 ASP B N     1 
ATOM   8115  C  CA    . ASP B 1 318 ? 102.669 145.541 146.231 1.00 38.45 ?  318 ASP B CA    1 
ATOM   8116  C  C     . ASP B 1 318 ? 101.915 144.452 145.480 1.00 38.44 ?  318 ASP B C     1 
ATOM   8117  O  O     . ASP B 1 318 ? 100.867 144.710 144.880 1.00 41.14 ?  318 ASP B O     1 
ATOM   8118  C  CB    . ASP B 1 318 ? 101.803 146.151 147.330 1.00 37.95 ?  318 ASP B CB    1 
ATOM   8119  C  CG    . ASP B 1 318 ? 101.347 145.129 148.350 1.00 46.03 ?  318 ASP B CG    1 
ATOM   8120  O  OD1   . ASP B 1 318 ? 102.191 144.652 149.139 1.00 42.17 ?  318 ASP B OD1   1 
ATOM   8121  O  OD2   . ASP B 1 318 ? 100.142 144.804 148.364 1.00 44.77 -1 318 ASP B OD2   1 
ATOM   8122  N  N     . MET B 1 319 ? 102.451 143.229 145.508 1.00 39.69 ?  319 MET B N     1 
ATOM   8123  C  CA    . MET B 1 319 ? 101.767 142.107 144.874 1.00 35.15 ?  319 MET B CA    1 
ATOM   8124  C  C     . MET B 1 319 ? 100.513 141.703 145.638 1.00 36.04 ?  319 MET B C     1 
ATOM   8125  O  O     . MET B 1 319 ? 99.561  141.203 145.032 1.00 38.25 ?  319 MET B O     1 
ATOM   8126  C  CB    . MET B 1 319 ? 102.713 140.913 144.745 1.00 36.87 ?  319 MET B CB    1 
ATOM   8127  C  CG    . MET B 1 319 ? 102.214 139.824 143.803 1.00 37.09 ?  319 MET B CG    1 
ATOM   8128  S  SD    . MET B 1 319 ? 102.582 140.091 142.056 1.00 44.18 ?  319 MET B SD    1 
ATOM   8129  C  CE    . MET B 1 319 ? 103.883 141.316 142.143 1.00 38.47 ?  319 MET B CE    1 
ATOM   8130  N  N     . ASN B 1 320 ? 100.485 141.923 146.954 1.00 38.47 ?  320 ASN B N     1 
ATOM   8131  C  CA    . ASN B 1 320 ? 99.325  141.525 147.745 1.00 38.98 ?  320 ASN B CA    1 
ATOM   8132  C  C     . ASN B 1 320 ? 98.068  142.268 147.316 1.00 40.89 ?  320 ASN B C     1 
ATOM   8133  O  O     . ASN B 1 320 ? 96.955  141.764 147.503 1.00 41.47 ?  320 ASN B O     1 
ATOM   8134  C  CB    . ASN B 1 320 ? 99.599  141.758 149.230 1.00 37.46 ?  320 ASN B CB    1 
ATOM   8135  C  CG    . ASN B 1 320 ? 100.723 140.891 149.755 1.00 42.30 ?  320 ASN B CG    1 
ATOM   8136  O  OD1   . ASN B 1 320 ? 101.842 140.925 149.242 1.00 37.80 ?  320 ASN B OD1   1 
ATOM   8137  N  ND2   . ASN B 1 320 ? 100.431 140.106 150.783 1.00 41.25 ?  320 ASN B ND2   1 
ATOM   8138  N  N     . GLU B 1 321 ? 98.221  143.460 146.742 1.00 42.19 ?  321 GLU B N     1 
ATOM   8139  C  CA    . GLU B 1 321 ? 97.089  144.248 146.280 1.00 40.34 ?  321 GLU B CA    1 
ATOM   8140  C  C     . GLU B 1 321 ? 96.969  144.311 144.765 1.00 40.01 ?  321 GLU B C     1 
ATOM   8141  O  O     . GLU B 1 321 ? 95.914  144.719 144.264 1.00 46.31 ?  321 GLU B O     1 
ATOM   8142  C  CB    . GLU B 1 321 ? 97.178  145.678 146.838 1.00 42.72 ?  321 GLU B CB    1 
ATOM   8143  C  CG    . GLU B 1 321 ? 97.915  146.652 145.933 1.00 39.85 ?  321 GLU B CG    1 
ATOM   8144  C  CD    . GLU B 1 321 ? 98.587  147.769 146.703 1.00 45.15 ?  321 GLU B CD    1 
ATOM   8145  O  OE1   . GLU B 1 321 ? 98.577  147.723 147.950 1.00 45.47 ?  321 GLU B OE1   1 
ATOM   8146  O  OE2   . GLU B 1 321 ? 99.134  148.691 146.061 1.00 45.61 -1 321 GLU B OE2   1 
ATOM   8147  N  N     . MET B 1 322 ? 98.001  143.916 144.022 1.00 34.71 ?  322 MET B N     1 
ATOM   8148  C  CA    . MET B 1 322 ? 97.996  144.040 142.572 1.00 32.82 ?  322 MET B CA    1 
ATOM   8149  C  C     . MET B 1 322 ? 98.016  142.697 141.856 1.00 33.10 ?  322 MET B C     1 
ATOM   8150  O  O     . MET B 1 322 ? 97.979  142.672 140.622 1.00 39.54 ?  322 MET B O     1 
ATOM   8151  C  CB    . MET B 1 322 ? 99.190  144.883 142.110 1.00 33.39 ?  322 MET B CB    1 
ATOM   8152  C  CG    . MET B 1 322 ? 99.036  146.381 142.354 1.00 35.60 ?  322 MET B CG    1 
ATOM   8153  S  SD    . MET B 1 322 ? 98.111  147.303 141.110 1.00 45.22 ?  322 MET B SD    1 
ATOM   8154  C  CE    . MET B 1 322 ? 98.309  146.268 139.668 1.00 36.56 ?  322 MET B CE    1 
ATOM   8155  N  N     . TYR B 1 323 ? 98.084  141.581 142.590 1.00 32.48 ?  323 TYR B N     1 
ATOM   8156  C  CA    . TYR B 1 323 ? 98.133  140.269 141.951 1.00 28.69 ?  323 TYR B CA    1 
ATOM   8157  C  C     . TYR B 1 323 ? 96.845  139.969 141.195 1.00 29.49 ?  323 TYR B C     1 
ATOM   8158  O  O     . TYR B 1 323 ? 96.884  139.459 140.068 1.00 33.38 ?  323 TYR B O     1 
ATOM   8159  C  CB    . TYR B 1 323 ? 98.405  139.189 143.000 1.00 32.87 ?  323 TYR B CB    1 
ATOM   8160  C  CG    . TYR B 1 323 ? 98.360  137.778 142.459 1.00 30.91 ?  323 TYR B CG    1 
ATOM   8161  C  CD1   . TYR B 1 323 ? 99.479  137.202 141.878 1.00 27.40 ?  323 TYR B CD1   1 
ATOM   8162  C  CD2   . TYR B 1 323 ? 97.198  137.021 142.534 1.00 30.40 ?  323 TYR B CD2   1 
ATOM   8163  C  CE1   . TYR B 1 323 ? 99.441  135.915 141.381 1.00 29.80 ?  323 TYR B CE1   1 
ATOM   8164  C  CE2   . TYR B 1 323 ? 97.151  135.735 142.041 1.00 25.97 ?  323 TYR B CE2   1 
ATOM   8165  C  CZ    . TYR B 1 323 ? 98.275  135.187 141.467 1.00 31.28 ?  323 TYR B CZ    1 
ATOM   8166  O  OH    . TYR B 1 323 ? 98.234  133.906 140.973 1.00 30.96 ?  323 TYR B OH    1 
ATOM   8167  N  N     . ASP B 1 324 ? 95.697  140.268 141.802 1.00 36.10 ?  324 ASP B N     1 
ATOM   8168  C  CA    . ASP B 1 324 ? 94.425  140.030 141.131 1.00 34.38 ?  324 ASP B CA    1 
ATOM   8169  C  C     . ASP B 1 324 ? 94.278  140.918 139.901 1.00 38.34 ?  324 ASP B C     1 
ATOM   8170  O  O     . ASP B 1 324 ? 93.737  140.485 138.877 1.00 41.12 ?  324 ASP B O     1 
ATOM   8171  C  CB    . ASP B 1 324 ? 93.270  140.252 142.104 1.00 38.72 ?  324 ASP B CB    1 
ATOM   8172  C  CG    . ASP B 1 324 ? 93.043  139.060 143.014 1.00 40.69 ?  324 ASP B CG    1 
ATOM   8173  O  OD1   . ASP B 1 324 ? 93.408  137.934 142.619 1.00 40.70 ?  324 ASP B OD1   1 
ATOM   8174  O  OD2   . ASP B 1 324 ? 92.501  139.250 144.123 1.00 42.71 -1 324 ASP B OD2   1 
ATOM   8175  N  N     . LYS B 1 325 ? 94.749  142.164 139.986 1.00 33.53 ?  325 LYS B N     1 
ATOM   8176  C  CA    . LYS B 1 325 ? 94.715  143.047 138.824 1.00 31.34 ?  325 LYS B CA    1 
ATOM   8177  C  C     . LYS B 1 325 ? 95.624  142.534 137.712 1.00 32.90 ?  325 LYS B C     1 
ATOM   8178  O  O     . LYS B 1 325 ? 95.268  142.609 136.532 1.00 40.84 ?  325 LYS B O     1 
ATOM   8179  C  CB    . LYS B 1 325 ? 95.106  144.464 139.234 1.00 36.26 ?  325 LYS B CB    1 
ATOM   8180  C  CG    . LYS B 1 325 ? 94.126  145.106 140.200 1.00 34.78 ?  325 LYS B CG    1 
ATOM   8181  C  CD    . LYS B 1 325 ? 94.713  146.347 140.841 1.00 34.18 ?  325 LYS B CD    1 
ATOM   8182  C  CE    . LYS B 1 325 ? 93.622  147.277 141.338 1.00 36.84 ?  325 LYS B CE    1 
ATOM   8183  N  NZ    . LYS B 1 325 ? 92.319  146.572 141.482 1.00 36.00 1  325 LYS B NZ    1 
ATOM   8184  N  N     . PHE B 1 326 ? 96.799  142.011 138.071 1.00 35.11 ?  326 PHE B N     1 
ATOM   8185  C  CA    . PHE B 1 326 ? 97.669  141.383 137.080 1.00 33.24 ?  326 PHE B CA    1 
ATOM   8186  C  C     . PHE B 1 326 ? 96.985  140.195 136.416 1.00 29.94 ?  326 PHE B C     1 
ATOM   8187  O  O     . PHE B 1 326 ? 97.069  140.023 135.194 1.00 36.57 ?  326 PHE B O     1 
ATOM   8188  C  CB    . PHE B 1 326 ? 98.976  140.929 137.733 1.00 30.23 ?  326 PHE B CB    1 
ATOM   8189  C  CG    . PHE B 1 326 ? 99.875  142.050 138.161 1.00 30.01 ?  326 PHE B CG    1 
ATOM   8190  C  CD1   . PHE B 1 326 ? 99.736  143.318 137.629 1.00 33.25 ?  326 PHE B CD1   1 
ATOM   8191  C  CD2   . PHE B 1 326 ? 100.865 141.830 139.104 1.00 33.29 ?  326 PHE B CD2   1 
ATOM   8192  C  CE1   . PHE B 1 326 ? 100.573 144.342 138.023 1.00 30.86 ?  326 PHE B CE1   1 
ATOM   8193  C  CE2   . PHE B 1 326 ? 101.699 142.852 139.505 1.00 33.97 ?  326 PHE B CE2   1 
ATOM   8194  C  CZ    . PHE B 1 326 ? 101.553 144.110 138.965 1.00 35.34 ?  326 PHE B CZ    1 
ATOM   8195  N  N     . VAL B 1 327 ? 96.312  139.359 137.208 1.00 31.40 ?  327 VAL B N     1 
ATOM   8196  C  CA    . VAL B 1 327 ? 95.703  138.149 136.665 1.00 34.99 ?  327 VAL B CA    1 
ATOM   8197  C  C     . VAL B 1 327 ? 94.526  138.494 135.758 1.00 36.86 ?  327 VAL B C     1 
ATOM   8198  O  O     . VAL B 1 327 ? 94.366  137.914 134.678 1.00 41.34 ?  327 VAL B O     1 
ATOM   8199  C  CB    . VAL B 1 327 ? 95.286  137.205 137.807 1.00 32.98 ?  327 VAL B CB    1 
ATOM   8200  C  CG1   . VAL B 1 327 ? 94.384  136.098 137.286 1.00 35.22 ?  327 VAL B CG1   1 
ATOM   8201  C  CG2   . VAL B 1 327 ? 96.516  136.619 138.481 1.00 29.82 ?  327 VAL B CG2   1 
ATOM   8202  N  N     . ASP B 1 328 ? 93.693  139.449 136.171 1.00 36.62 ?  328 ASP B N     1 
ATOM   8203  C  CA    . ASP B 1 328 ? 92.510  139.814 135.403 1.00 36.77 ?  328 ASP B CA    1 
ATOM   8204  C  C     . ASP B 1 328 ? 92.817  140.732 134.227 1.00 40.53 ?  328 ASP B C     1 
ATOM   8205  O  O     . ASP B 1 328 ? 91.915  141.008 133.430 1.00 43.97 ?  328 ASP B O     1 
ATOM   8206  C  CB    . ASP B 1 328 ? 91.481  140.483 136.318 1.00 38.73 ?  328 ASP B CB    1 
ATOM   8207  C  CG    . ASP B 1 328 ? 91.051  139.587 137.461 1.00 45.21 ?  328 ASP B CG    1 
ATOM   8208  O  OD1   . ASP B 1 328 ? 90.448  140.102 138.426 1.00 46.00 ?  328 ASP B OD1   1 
ATOM   8209  O  OD2   . ASP B 1 328 ? 91.318  138.368 137.396 1.00 44.15 -1 328 ASP B OD2   1 
ATOM   8210  N  N     . ASN B 1 329 ? 94.053  141.207 134.100 1.00 36.19 ?  329 ASN B N     1 
ATOM   8211  C  CA    . ASN B 1 329 ? 94.415  142.120 133.024 1.00 35.52 ?  329 ASN B CA    1 
ATOM   8212  C  C     . ASN B 1 329 ? 94.827  141.313 131.799 1.00 39.38 ?  329 ASN B C     1 
ATOM   8213  O  O     . ASN B 1 329 ? 95.831  140.591 131.858 1.00 39.32 ?  329 ASN B O     1 
ATOM   8214  C  CB    . ASN B 1 329 ? 95.552  143.029 133.462 1.00 35.64 ?  329 ASN B CB    1 
ATOM   8215  C  CG    . ASN B 1 329 ? 95.695  144.266 132.595 1.00 39.66 ?  329 ASN B CG    1 
ATOM   8216  O  OD1   . ASN B 1 329 ? 96.275  145.260 133.023 1.00 37.91 ?  329 ASN B OD1   1 
ATOM   8217  N  ND2   . ASN B 1 329 ? 95.170  144.216 131.380 1.00 42.21 ?  329 ASN B ND2   1 
ATOM   8218  N  N     . PRO B 1 330 ? 94.094  141.397 130.683 1.00 43.55 ?  330 PRO B N     1 
ATOM   8219  C  CA    . PRO B 1 330 ? 94.510  140.647 129.487 1.00 40.99 ?  330 PRO B CA    1 
ATOM   8220  C  C     . PRO B 1 330 ? 95.796  141.165 128.867 1.00 37.31 ?  330 PRO B C     1 
ATOM   8221  O  O     . PRO B 1 330 ? 96.487  140.401 128.182 1.00 39.57 ?  330 PRO B O     1 
ATOM   8222  C  CB    . PRO B 1 330 ? 93.316  140.814 128.539 1.00 41.98 ?  330 PRO B CB    1 
ATOM   8223  C  CG    . PRO B 1 330 ? 92.669  142.084 128.974 1.00 37.44 ?  330 PRO B CG    1 
ATOM   8224  C  CD    . PRO B 1 330 ? 92.844  142.143 130.464 1.00 40.19 ?  330 PRO B CD    1 
ATOM   8225  N  N     . ARG B 1 331 ? 96.141  142.434 129.082 1.00 38.79 ?  331 ARG B N     1 
ATOM   8226  C  CA    . ARG B 1 331 ? 97.369  142.992 128.530 1.00 42.17 ?  331 ARG B CA    1 
ATOM   8227  C  C     . ARG B 1 331 ? 98.607  142.593 129.320 1.00 40.20 ?  331 ARG B C     1 
ATOM   8228  O  O     . ARG B 1 331 ? 99.722  142.913 128.896 1.00 38.14 ?  331 ARG B O     1 
ATOM   8229  C  CB    . ARG B 1 331 ? 97.267  144.517 128.455 1.00 39.65 ?  331 ARG B CB    1 
ATOM   8230  C  CG    . ARG B 1 331 ? 96.300  145.014 127.393 1.00 38.38 ?  331 ARG B CG    1 
ATOM   8231  C  CD    . ARG B 1 331 ? 95.878  146.454 127.640 1.00 40.13 ?  331 ARG B CD    1 
ATOM   8232  N  NE    . ARG B 1 331 ? 95.164  146.621 128.901 1.00 42.43 ?  331 ARG B NE    1 
ATOM   8233  C  CZ    . ARG B 1 331 ? 93.935  146.179 129.136 1.00 42.33 ?  331 ARG B CZ    1 
ATOM   8234  N  NH1   . ARG B 1 331 ? 93.243  145.531 128.214 1.00 41.73 1  331 ARG B NH1   1 
ATOM   8235  N  NH2   . ARG B 1 331 ? 93.385  146.399 130.327 1.00 40.55 ?  331 ARG B NH2   1 
ATOM   8236  N  N     . VAL B 1 332 ? 98.438  141.914 130.449 1.00 38.10 ?  332 VAL B N     1 
ATOM   8237  C  CA    . VAL B 1 332 ? 99.546  141.376 131.227 1.00 33.72 ?  332 VAL B CA    1 
ATOM   8238  C  C     . VAL B 1 332 ? 99.694  139.902 130.883 1.00 34.64 ?  332 VAL B C     1 
ATOM   8239  O  O     . VAL B 1 332 ? 98.712  139.150 130.912 1.00 37.29 ?  332 VAL B O     1 
ATOM   8240  C  CB    . VAL B 1 332 ? 99.314  141.572 132.736 1.00 33.18 ?  332 VAL B CB    1 
ATOM   8241  C  CG1   . VAL B 1 332 ? 100.266 140.701 133.541 1.00 33.55 ?  332 VAL B CG1   1 
ATOM   8242  C  CG2   . VAL B 1 332 ? 99.474  143.037 133.109 1.00 33.28 ?  332 VAL B CG2   1 
ATOM   8243  N  N     . LYS B 1 333 ? 100.909 139.491 130.537 1.00 31.25 ?  333 LYS B N     1 
ATOM   8244  C  CA    . LYS B 1 333 ? 101.186 138.102 130.203 1.00 31.37 ?  333 LYS B CA    1 
ATOM   8245  C  C     . LYS B 1 333 ? 101.607 137.342 131.454 1.00 33.26 ?  333 LYS B C     1 
ATOM   8246  O  O     . LYS B 1 333 ? 102.394 137.843 132.263 1.00 34.81 ?  333 LYS B O     1 
ATOM   8247  C  CB    . LYS B 1 333 ? 102.276 138.010 129.135 1.00 26.23 ?  333 LYS B CB    1 
ATOM   8248  C  CG    . LYS B 1 333 ? 102.298 136.694 128.378 1.00 32.17 ?  333 LYS B CG    1 
ATOM   8249  C  CD    . LYS B 1 333 ? 103.466 136.639 127.408 1.00 34.40 ?  333 LYS B CD    1 
ATOM   8250  C  CE    . LYS B 1 333 ? 103.596 135.263 126.777 1.00 35.85 ?  333 LYS B CE    1 
ATOM   8251  N  NZ    . LYS B 1 333 ? 104.738 135.196 125.825 1.00 37.67 1  333 LYS B NZ    1 
ATOM   8252  N  N     . LYS B 1 334 ? 101.080 136.130 131.609 1.00 32.05 ?  334 LYS B N     1 
ATOM   8253  C  CA    . LYS B 1 334 ? 101.354 135.338 132.798 1.00 29.36 ?  334 LYS B CA    1 
ATOM   8254  C  C     . LYS B 1 334 ? 101.315 133.858 132.451 1.00 33.55 ?  334 LYS B C     1 
ATOM   8255  O  O     . LYS B 1 334 ? 100.749 133.448 131.435 1.00 35.10 ?  334 LYS B O     1 
ATOM   8256  C  CB    . LYS B 1 334 ? 100.354 135.642 133.920 1.00 31.14 ?  334 LYS B CB    1 
ATOM   8257  C  CG    . LYS B 1 334 ? 98.947  135.147 133.648 1.00 35.88 ?  334 LYS B CG    1 
ATOM   8258  C  CD    . LYS B 1 334 ? 97.906  136.130 134.144 1.00 32.50 ?  334 LYS B CD    1 
ATOM   8259  C  CE    . LYS B 1 334 ? 97.700  137.252 133.148 1.00 33.97 ?  334 LYS B CE    1 
ATOM   8260  N  NZ    . LYS B 1 334 ? 96.333  137.830 133.228 1.00 34.33 1  334 LYS B NZ    1 
ATOM   8261  N  N     . GLU B 1 335 ? 101.932 133.061 133.320 1.00 33.86 ?  335 GLU B N     1 
ATOM   8262  C  CA    . GLU B 1 335 ? 101.968 131.612 133.199 1.00 33.23 ?  335 GLU B CA    1 
ATOM   8263  C  C     . GLU B 1 335 ? 101.444 130.984 134.481 1.00 34.05 ?  335 GLU B C     1 
ATOM   8264  O  O     . GLU B 1 335 ? 101.715 131.476 135.580 1.00 40.53 ?  335 GLU B O     1 
ATOM   8265  C  CB    . GLU B 1 335 ? 103.388 131.106 132.918 1.00 29.97 ?  335 GLU B CB    1 
ATOM   8266  C  CG    . GLU B 1 335 ? 104.160 131.938 131.913 1.00 37.48 ?  335 GLU B CG    1 
ATOM   8267  C  CD    . GLU B 1 335 ? 104.976 131.090 130.958 1.00 41.55 ?  335 GLU B CD    1 
ATOM   8268  O  OE1   . GLU B 1 335 ? 105.943 130.443 131.414 1.00 36.02 ?  335 GLU B OE1   1 
ATOM   8269  O  OE2   . GLU B 1 335 ? 104.650 131.071 129.753 1.00 36.24 -1 335 GLU B OE2   1 
ATOM   8270  N  N     . LYS B 1 336 ? 100.699 129.893 134.333 1.00 33.34 ?  336 LYS B N     1 
ATOM   8271  C  CA    . LYS B 1 336 ? 100.154 129.187 135.483 1.00 29.33 ?  336 LYS B CA    1 
ATOM   8272  C  C     . LYS B 1 336 ? 101.223 128.324 136.138 1.00 35.73 ?  336 LYS B C     1 
ATOM   8273  O  O     . LYS B 1 336 ? 101.988 127.633 135.461 1.00 37.25 ?  336 LYS B O     1 
ATOM   8274  C  CB    . LYS B 1 336 ? 98.970  128.316 135.061 1.00 37.44 ?  336 LYS B CB    1 
ATOM   8275  C  CG    . LYS B 1 336 ? 97.935  128.102 136.152 1.00 41.25 ?  336 LYS B CG    1 
ATOM   8276  C  CD    . LYS B 1 336 ? 96.799  127.218 135.667 1.00 38.03 ?  336 LYS B CD    1 
ATOM   8277  C  CE    . LYS B 1 336 ? 95.450  127.881 135.884 1.00 39.22 ?  336 LYS B CE    1 
ATOM   8278  N  NZ    . LYS B 1 336 ? 95.367  128.549 137.211 1.00 39.13 1  336 LYS B NZ    1 
ATOM   8279  N  N     . ILE B 1 337 ? 101.276 128.373 137.471 1.00 36.47 ?  337 ILE B N     1 
ATOM   8280  C  CA    . ILE B 1 337 ? 102.185 127.556 138.260 1.00 34.68 ?  337 ILE B CA    1 
ATOM   8281  C  C     . ILE B 1 337 ? 101.426 127.013 139.462 1.00 35.24 ?  337 ILE B C     1 
ATOM   8282  O  O     . ILE B 1 337 ? 100.361 127.513 139.832 1.00 39.38 ?  337 ILE B O     1 
ATOM   8283  C  CB    . ILE B 1 337 ? 103.432 128.336 138.738 1.00 33.50 ?  337 ILE B CB    1 
ATOM   8284  C  CG1   . ILE B 1 337 ? 103.012 129.572 139.536 1.00 33.10 ?  337 ILE B CG1   1 
ATOM   8285  C  CG2   . ILE B 1 337 ? 104.315 128.720 137.562 1.00 35.27 ?  337 ILE B CG2   1 
ATOM   8286  C  CD1   . ILE B 1 337 ? 103.912 129.874 140.710 1.00 31.75 ?  337 ILE B CD1   1 
ATOM   8287  N  N     . ASN B 1 338 ? 101.987 125.972 140.069 1.00 35.06 ?  338 ASN B N     1 
ATOM   8288  C  CA    . ASN B 1 338 ? 101.467 125.461 141.326 1.00 34.44 ?  338 ASN B CA    1 
ATOM   8289  C  C     . ASN B 1 338 ? 102.325 126.008 142.453 1.00 34.15 ?  338 ASN B C     1 
ATOM   8290  O  O     . ASN B 1 338 ? 103.494 125.612 142.574 1.00 37.77 ?  338 ASN B O     1 
ATOM   8291  C  CB    . ASN B 1 338 ? 101.473 123.934 141.338 1.00 32.16 ?  338 ASN B CB    1 
ATOM   8292  C  CG    . ASN B 1 338 ? 100.569 123.354 142.410 1.00 35.79 ?  338 ASN B CG    1 
ATOM   8293  O  OD1   . ASN B 1 338 ? 100.534 122.142 142.618 1.00 38.49 ?  338 ASN B OD1   1 
ATOM   8294  N  ND2   . ASN B 1 338 ? 99.829  124.219 143.092 1.00 37.38 ?  338 ASN B ND2   1 
ATOM   8295  N  N     . PRO B 1 339 ? 101.814 126.921 143.284 1.00 33.80 ?  339 PRO B N     1 
ATOM   8296  C  CA    . PRO B 1 339 ? 102.653 127.485 144.354 1.00 28.56 ?  339 PRO B CA    1 
ATOM   8297  C  C     . PRO B 1 339 ? 103.167 126.448 145.335 1.00 32.53 ?  339 PRO B C     1 
ATOM   8298  O  O     . PRO B 1 339 ? 104.288 126.591 145.838 1.00 35.56 ?  339 PRO B O     1 
ATOM   8299  C  CB    . PRO B 1 339 ? 101.720 128.498 145.034 1.00 29.85 ?  339 PRO B CB    1 
ATOM   8300  C  CG    . PRO B 1 339 ? 100.343 128.076 144.651 1.00 33.77 ?  339 PRO B CG    1 
ATOM   8301  C  CD    . PRO B 1 339 ? 100.460 127.493 143.281 1.00 33.82 ?  339 PRO B CD    1 
ATOM   8302  N  N     . ARG B 1 340 ? 102.387 125.403 145.623 1.00 31.45 ?  340 ARG B N     1 
ATOM   8303  C  CA    . ARG B 1 340 ? 102.879 124.343 146.497 1.00 28.07 ?  340 ARG B CA    1 
ATOM   8304  C  C     . ARG B 1 340 ? 103.996 123.553 145.828 1.00 31.70 ?  340 ARG B C     1 
ATOM   8305  O  O     . ARG B 1 340 ? 104.973 123.174 146.483 1.00 34.63 ?  340 ARG B O     1 
ATOM   8306  C  CB    . ARG B 1 340 ? 101.732 123.423 146.909 1.00 31.53 ?  340 ARG B CB    1 
ATOM   8307  C  CG    . ARG B 1 340 ? 100.822 124.032 147.956 1.00 29.55 ?  340 ARG B CG    1 
ATOM   8308  C  CD    . ARG B 1 340 ? 100.079 122.977 148.752 1.00 28.13 ?  340 ARG B CD    1 
ATOM   8309  N  NE    . ARG B 1 340 ? 99.119  123.586 149.665 1.00 31.78 ?  340 ARG B NE    1 
ATOM   8310  C  CZ    . ARG B 1 340 ? 98.312  122.909 150.469 1.00 34.23 ?  340 ARG B CZ    1 
ATOM   8311  N  NH1   . ARG B 1 340 ? 98.324  121.587 150.507 1.00 34.73 1  340 ARG B NH1   1 
ATOM   8312  N  NH2   . ARG B 1 340 ? 97.472  123.575 151.255 1.00 34.57 ?  340 ARG B NH2   1 
ATOM   8313  N  N     . LYS B 1 341 ? 103.872 123.298 144.524 1.00 30.60 ?  341 LYS B N     1 
ATOM   8314  C  CA    . LYS B 1 341 ? 104.959 122.646 143.802 1.00 27.34 ?  341 LYS B CA    1 
ATOM   8315  C  C     . LYS B 1 341 ? 106.204 123.521 143.766 1.00 30.08 ?  341 LYS B C     1 
ATOM   8316  O  O     . LYS B 1 341 ? 107.322 123.009 143.860 1.00 29.73 ?  341 LYS B O     1 
ATOM   8317  C  CB    . LYS B 1 341 ? 104.520 122.289 142.381 1.00 35.91 ?  341 LYS B CB    1 
ATOM   8318  C  CG    . LYS B 1 341 ? 103.581 121.091 142.275 1.00 37.10 ?  341 LYS B CG    1 
ATOM   8319  C  CD    . LYS B 1 341 ? 103.622 120.208 143.512 1.00 34.20 ?  341 LYS B CD    1 
ATOM   8320  C  CE    . LYS B 1 341 ? 103.245 118.774 143.178 1.00 36.14 ?  341 LYS B CE    1 
ATOM   8321  N  NZ    . LYS B 1 341 ? 101.894 118.681 142.557 1.00 33.97 1  341 LYS B NZ    1 
ATOM   8322  N  N     . LEU B 1 342 ? 106.032 124.838 143.636 1.00 29.26 ?  342 LEU B N     1 
ATOM   8323  C  CA    . LEU B 1 342 ? 107.179 125.738 143.676 1.00 26.52 ?  342 LEU B CA    1 
ATOM   8324  C  C     . LEU B 1 342 ? 107.833 125.738 145.054 1.00 30.91 ?  342 LEU B C     1 
ATOM   8325  O  O     . LEU B 1 342 ? 109.063 125.772 145.162 1.00 37.75 ?  342 LEU B O     1 
ATOM   8326  C  CB    . LEU B 1 342 ? 106.753 127.149 143.278 1.00 30.07 ?  342 LEU B CB    1 
ATOM   8327  C  CG    . LEU B 1 342 ? 107.876 128.117 142.900 1.00 27.23 ?  342 LEU B CG    1 
ATOM   8328  C  CD1   . LEU B 1 342 ? 108.912 127.425 142.031 1.00 25.62 ?  342 LEU B CD1   1 
ATOM   8329  C  CD2   . LEU B 1 342 ? 107.311 129.337 142.193 1.00 26.81 ?  342 LEU B CD2   1 
ATOM   8330  N  N     . LEU B 1 343 ? 107.028 125.698 146.118 1.00 29.53 ?  343 LEU B N     1 
ATOM   8331  C  CA    . LEU B 1 343 ? 107.580 125.598 147.466 1.00 26.59 ?  343 LEU B CA    1 
ATOM   8332  C  C     . LEU B 1 343 ? 108.348 124.295 147.653 1.00 28.70 ?  343 LEU B C     1 
ATOM   8333  O  O     . LEU B 1 343 ? 109.425 124.280 148.261 1.00 33.74 ?  343 LEU B O     1 
ATOM   8334  C  CB    . LEU B 1 343 ? 106.461 125.708 148.499 1.00 30.61 ?  343 LEU B CB    1 
ATOM   8335  C  CG    . LEU B 1 343 ? 106.208 127.090 149.096 1.00 30.70 ?  343 LEU B CG    1 
ATOM   8336  C  CD1   . LEU B 1 343 ? 105.182 127.001 150.211 1.00 27.27 ?  343 LEU B CD1   1 
ATOM   8337  C  CD2   . LEU B 1 343 ? 107.505 127.701 149.598 1.00 30.33 ?  343 LEU B CD2   1 
ATOM   8338  N  N     . GLU B 1 344 ? 107.800 123.188 147.149 1.00 30.95 ?  344 GLU B N     1 
ATOM   8339  C  CA    . GLU B 1 344 ? 108.497 121.910 147.242 1.00 28.52 ?  344 GLU B CA    1 
ATOM   8340  C  C     . GLU B 1 344 ? 109.790 121.929 146.437 1.00 29.40 ?  344 GLU B C     1 
ATOM   8341  O  O     . GLU B 1 344 ? 110.792 121.338 146.850 1.00 34.84 ?  344 GLU B O     1 
ATOM   8342  C  CB    . GLU B 1 344 ? 107.585 120.777 146.777 1.00 30.80 ?  344 GLU B CB    1 
ATOM   8343  C  CG    . GLU B 1 344 ? 106.403 120.523 147.698 1.00 33.67 ?  344 GLU B CG    1 
ATOM   8344  C  CD    . GLU B 1 344 ? 105.312 119.710 147.034 1.00 38.15 ?  344 GLU B CD    1 
ATOM   8345  O  OE1   . GLU B 1 344 ? 105.548 119.202 145.918 1.00 39.86 ?  344 GLU B OE1   1 
ATOM   8346  O  OE2   . GLU B 1 344 ? 104.220 119.582 147.625 1.00 37.98 -1 344 GLU B OE2   1 
ATOM   8347  N  N     . LYS B 1 345 ? 109.785 122.600 145.283 1.00 29.24 ?  345 LYS B N     1 
ATOM   8348  C  CA    . LYS B 1 345 ? 111.012 122.758 144.510 1.00 27.16 ?  345 LYS B CA    1 
ATOM   8349  C  C     . LYS B 1 345 ? 112.043 123.574 145.278 1.00 30.72 ?  345 LYS B C     1 
ATOM   8350  O  O     . LYS B 1 345 ? 113.237 123.258 145.254 1.00 32.03 ?  345 LYS B O     1 
ATOM   8351  C  CB    . LYS B 1 345 ? 110.705 123.411 143.163 1.00 26.14 ?  345 LYS B CB    1 
ATOM   8352  C  CG    . LYS B 1 345 ? 111.919 123.576 142.268 1.00 29.85 ?  345 LYS B CG    1 
ATOM   8353  C  CD    . LYS B 1 345 ? 111.542 124.151 140.916 1.00 30.37 ?  345 LYS B CD    1 
ATOM   8354  C  CE    . LYS B 1 345 ? 112.760 124.269 140.015 1.00 30.62 ?  345 LYS B CE    1 
ATOM   8355  N  NZ    . LYS B 1 345 ? 112.423 124.860 138.692 1.00 31.25 1  345 LYS B NZ    1 
ATOM   8356  N  N     . LEU B 1 346 ? 111.600 124.633 145.961 1.00 29.75 ?  346 LEU B N     1 
ATOM   8357  C  CA    . LEU B 1 346 ? 112.507 125.413 146.797 1.00 23.48 ?  346 LEU B CA    1 
ATOM   8358  C  C     . LEU B 1 346 ? 113.116 124.548 147.891 1.00 27.62 ?  346 LEU B C     1 
ATOM   8359  O  O     . LEU B 1 346 ? 114.326 124.600 148.142 1.00 30.54 ?  346 LEU B O     1 
ATOM   8360  C  CB    . LEU B 1 346 ? 111.767 126.600 147.417 1.00 24.10 ?  346 LEU B CB    1 
ATOM   8361  C  CG    . LEU B 1 346 ? 111.213 127.704 146.517 1.00 26.77 ?  346 LEU B CG    1 
ATOM   8362  C  CD1   . LEU B 1 346 ? 110.412 128.696 147.341 1.00 28.15 ?  346 LEU B CD1   1 
ATOM   8363  C  CD2   . LEU B 1 346 ? 112.331 128.408 145.784 1.00 26.32 ?  346 LEU B CD2   1 
ATOM   8364  N  N     . ALA B 1 347 ? 112.286 123.742 148.554 1.00 26.89 ?  347 ALA B N     1 
ATOM   8365  C  CA    . ALA B 1 347 ? 112.782 122.880 149.624 1.00 20.29 ?  347 ALA B CA    1 
ATOM   8366  C  C     . ALA B 1 347 ? 113.760 121.839 149.093 1.00 29.91 ?  347 ALA B C     1 
ATOM   8367  O  O     . ALA B 1 347 ? 114.795 121.578 149.717 1.00 35.16 ?  347 ALA B O     1 
ATOM   8368  C  CB    . ALA B 1 347 ? 111.613 122.204 150.338 1.00 22.69 ?  347 ALA B CB    1 
ATOM   8369  N  N     . MET B 1 348 ? 113.451 121.237 147.943 1.00 31.69 ?  348 MET B N     1 
ATOM   8370  C  CA    . MET B 1 348 ? 114.355 120.259 147.347 1.00 29.01 ?  348 MET B CA    1 
ATOM   8371  C  C     . MET B 1 348 ? 115.680 120.898 146.956 1.00 31.20 ?  348 MET B C     1 
ATOM   8372  O  O     . MET B 1 348 ? 116.749 120.323 147.193 1.00 35.64 ?  348 MET B O     1 
ATOM   8373  C  CB    . MET B 1 348 ? 113.691 119.610 146.133 1.00 31.96 ?  348 MET B CB    1 
ATOM   8374  C  CG    . MET B 1 348 ? 114.647 118.864 145.215 1.00 38.36 ?  348 MET B CG    1 
ATOM   8375  S  SD    . MET B 1 348 ? 114.861 119.687 143.625 1.00 53.07 ?  348 MET B SD    1 
ATOM   8376  C  CE    . MET B 1 348 ? 113.183 119.669 143.005 1.00 37.32 ?  348 MET B CE    1 
ATOM   8377  N  N     . LEU B 1 349 ? 115.632 122.091 146.362 1.00 28.67 ?  349 LEU B N     1 
ATOM   8378  C  CA    . LEU B 1 349 ? 116.857 122.784 145.982 1.00 25.58 ?  349 LEU B CA    1 
ATOM   8379  C  C     . LEU B 1 349 ? 117.695 123.130 147.203 1.00 25.72 ?  349 LEU B C     1 
ATOM   8380  O  O     . LEU B 1 349 ? 118.925 123.008 147.175 1.00 30.40 ?  349 LEU B O     1 
ATOM   8381  C  CB    . LEU B 1 349 ? 116.519 124.048 145.193 1.00 30.48 ?  349 LEU B CB    1 
ATOM   8382  C  CG    . LEU B 1 349 ? 116.875 124.068 143.709 1.00 31.43 ?  349 LEU B CG    1 
ATOM   8383  C  CD1   . LEU B 1 349 ? 115.812 123.356 142.889 1.00 31.89 ?  349 LEU B CD1   1 
ATOM   8384  C  CD2   . LEU B 1 349 ? 117.052 125.500 143.244 1.00 28.13 ?  349 LEU B CD2   1 
ATOM   8385  N  N     . ARG B 1 350 ? 117.051 123.580 148.282 1.00 25.07 ?  350 ARG B N     1 
ATOM   8386  C  CA    . ARG B 1 350 ? 117.792 123.903 149.496 1.00 25.84 ?  350 ARG B CA    1 
ATOM   8387  C  C     . ARG B 1 350 ? 118.376 122.656 150.146 1.00 28.68 ?  350 ARG B C     1 
ATOM   8388  O  O     . ARG B 1 350 ? 119.466 122.714 150.725 1.00 33.54 ?  350 ARG B O     1 
ATOM   8389  C  CB    . ARG B 1 350 ? 116.893 124.654 150.476 1.00 22.89 ?  350 ARG B CB    1 
ATOM   8390  C  CG    . ARG B 1 350 ? 116.492 126.041 150.002 1.00 23.30 ?  350 ARG B CG    1 
ATOM   8391  C  CD    . ARG B 1 350 ? 115.417 126.644 150.886 1.00 23.06 ?  350 ARG B CD    1 
ATOM   8392  N  NE    . ARG B 1 350 ? 115.835 126.701 152.281 1.00 34.99 ?  350 ARG B NE    1 
ATOM   8393  C  CZ    . ARG B 1 350 ? 116.684 127.592 152.776 1.00 31.12 ?  350 ARG B CZ    1 
ATOM   8394  N  NH1   . ARG B 1 350 ? 117.223 128.531 152.016 1.00 26.96 1  350 ARG B NH1   1 
ATOM   8395  N  NH2   . ARG B 1 350 ? 117.001 127.538 154.065 1.00 27.93 ?  350 ARG B NH2   1 
ATOM   8396  N  N     . SER B 1 351 ? 117.670 121.528 150.073 1.00 28.79 ?  351 SER B N     1 
ATOM   8397  C  CA    . SER B 1 351 ? 118.233 120.277 150.569 1.00 29.95 ?  351 SER B CA    1 
ATOM   8398  C  C     . SER B 1 351 ? 119.446 119.854 149.750 1.00 33.63 ?  351 SER B C     1 
ATOM   8399  O  O     . SER B 1 351 ? 120.454 119.406 150.307 1.00 40.76 ?  351 SER B O     1 
ATOM   8400  C  CB    . SER B 1 351 ? 117.170 119.181 150.559 1.00 31.21 ?  351 SER B CB    1 
ATOM   8401  O  OG    . SER B 1 351 ? 116.027 119.571 151.298 1.00 36.59 ?  351 SER B OG    1 
ATOM   8402  N  N     . GLU B 1 352 ? 119.369 119.993 148.425 1.00 31.55 ?  352 GLU B N     1 
ATOM   8403  C  CA    . GLU B 1 352 ? 120.459 119.530 147.570 1.00 30.05 ?  352 GLU B CA    1 
ATOM   8404  C  C     . GLU B 1 352 ? 121.683 120.436 147.665 1.00 35.96 ?  352 GLU B C     1 
ATOM   8405  O  O     . GLU B 1 352 ? 122.812 119.945 147.780 1.00 39.68 ?  352 GLU B O     1 
ATOM   8406  C  CB    . GLU B 1 352 ? 119.984 119.425 146.121 1.00 34.33 ?  352 GLU B CB    1 
ATOM   8407  C  CG    . GLU B 1 352 ? 118.862 118.425 145.903 1.00 36.76 ?  352 GLU B CG    1 
ATOM   8408  C  CD    . GLU B 1 352 ? 118.314 118.463 144.491 1.00 41.55 ?  352 GLU B CD    1 
ATOM   8409  O  OE1   . GLU B 1 352 ? 118.361 119.541 143.862 1.00 38.58 ?  352 GLU B OE1   1 
ATOM   8410  O  OE2   . GLU B 1 352 ? 117.835 117.415 144.010 1.00 41.64 -1 352 GLU B OE2   1 
ATOM   8411  N  N     . SER B 1 353 ? 121.487 121.757 147.621 1.00 34.01 ?  353 SER B N     1 
ATOM   8412  C  CA    . SER B 1 353 ? 122.604 122.684 147.507 1.00 35.75 ?  353 SER B CA    1 
ATOM   8413  C  C     . SER B 1 353 ? 122.567 123.853 148.482 1.00 31.83 ?  353 SER B C     1 
ATOM   8414  O  O     . SER B 1 353 ? 123.506 124.655 148.488 1.00 34.71 ?  353 SER B O     1 
ATOM   8415  C  CB    . SER B 1 353 ? 122.688 123.237 146.076 1.00 35.48 ?  353 SER B CB    1 
ATOM   8416  O  OG    . SER B 1 353 ? 121.558 124.036 145.773 1.00 36.62 ?  353 SER B OG    1 
ATOM   8417  N  N     . GLY B 1 354 ? 121.523 123.981 149.298 1.00 22.19 ?  354 GLY B N     1 
ATOM   8418  C  CA    . GLY B 1 354 ? 121.418 125.101 150.209 1.00 23.41 ?  354 GLY B CA    1 
ATOM   8419  C  C     . GLY B 1 354 ? 120.867 126.373 149.604 1.00 21.72 ?  354 GLY B C     1 
ATOM   8420  O  O     . GLY B 1 354 ? 120.738 127.373 150.319 1.00 28.76 ?  354 GLY B O     1 
ATOM   8421  N  N     . TYR B 1 355 ? 120.539 126.366 148.321 1.00 25.60 ?  355 TYR B N     1 
ATOM   8422  C  CA    . TYR B 1 355 ? 119.973 127.495 147.607 1.00 17.85 ?  355 TYR B CA    1 
ATOM   8423  C  C     . TYR B 1 355 ? 118.523 127.209 147.246 1.00 20.21 ?  355 TYR B C     1 
ATOM   8424  O  O     . TYR B 1 355 ? 118.124 126.048 147.127 1.00 28.32 ?  355 TYR B O     1 
ATOM   8425  C  CB    . TYR B 1 355 ? 120.782 127.778 146.334 1.00 22.73 ?  355 TYR B CB    1 
ATOM   8426  C  CG    . TYR B 1 355 ? 122.168 128.310 146.600 1.00 25.91 ?  355 TYR B CG    1 
ATOM   8427  C  CD1   . TYR B 1 355 ? 122.360 129.429 147.398 1.00 23.53 ?  355 TYR B CD1   1 
ATOM   8428  C  CD2   . TYR B 1 355 ? 123.287 127.693 146.056 1.00 26.75 ?  355 TYR B CD2   1 
ATOM   8429  C  CE1   . TYR B 1 355 ? 123.624 129.918 147.646 1.00 26.24 ?  355 TYR B CE1   1 
ATOM   8430  C  CE2   . TYR B 1 355 ? 124.555 128.176 146.299 1.00 28.07 ?  355 TYR B CE2   1 
ATOM   8431  C  CZ    . TYR B 1 355 ? 124.718 129.290 147.094 1.00 29.17 ?  355 TYR B CZ    1 
ATOM   8432  O  OH    . TYR B 1 355 ? 125.980 129.777 147.341 1.00 30.83 ?  355 TYR B OH    1 
ATOM   8433  N  N     . PRO B 1 356 ? 117.696 128.244 147.050 1.00 21.44 ?  356 PRO B N     1 
ATOM   8434  C  CA    . PRO B 1 356 ? 117.974 129.684 147.116 1.00 17.78 ?  356 PRO B CA    1 
ATOM   8435  C  C     . PRO B 1 356 ? 117.917 130.278 148.515 1.00 17.32 ?  356 PRO B C     1 
ATOM   8436  O  O     . PRO B 1 356 ? 117.419 129.664 149.453 1.00 20.04 ?  356 PRO B O     1 
ATOM   8437  C  CB    . PRO B 1 356 ? 116.862 130.270 146.243 1.00 16.77 ?  356 PRO B CB    1 
ATOM   8438  C  CG    . PRO B 1 356 ? 115.702 129.372 146.528 1.00 19.79 ?  356 PRO B CG    1 
ATOM   8439  C  CD    . PRO B 1 356 ? 116.299 127.990 146.658 1.00 17.79 ?  356 PRO B CD    1 
ATOM   8440  N  N     . TYR B 1 357 ? 118.439 131.490 148.669 1.00 23.57 ?  357 TYR B N     1 
ATOM   8441  C  CA    . TYR B 1 357 ? 118.089 132.301 149.822 1.00 11.38 ?  357 TYR B CA    1 
ATOM   8442  C  C     . TYR B 1 357 ? 116.610 132.650 149.750 1.00 17.94 ?  357 TYR B C     1 
ATOM   8443  O  O     . TYR B 1 357 ? 116.068 132.898 148.670 1.00 26.55 ?  357 TYR B O     1 
ATOM   8444  C  CB    . TYR B 1 357 ? 118.927 133.580 149.864 1.00 16.41 ?  357 TYR B CB    1 
ATOM   8445  C  CG    . TYR B 1 357 ? 120.417 133.370 149.722 1.00 21.16 ?  357 TYR B CG    1 
ATOM   8446  C  CD1   . TYR B 1 357 ? 121.027 132.231 150.218 1.00 15.33 ?  357 TYR B CD1   1 
ATOM   8447  C  CD2   . TYR B 1 357 ? 121.214 134.315 149.090 1.00 20.38 ?  357 TYR B CD2   1 
ATOM   8448  C  CE1   . TYR B 1 357 ? 122.385 132.034 150.097 1.00 20.34 ?  357 TYR B CE1   1 
ATOM   8449  C  CE2   . TYR B 1 357 ? 122.574 134.128 148.960 1.00 15.32 ?  357 TYR B CE2   1 
ATOM   8450  C  CZ    . TYR B 1 357 ? 123.155 132.984 149.466 1.00 21.33 ?  357 TYR B CZ    1 
ATOM   8451  O  OH    . TYR B 1 357 ? 124.510 132.789 149.343 1.00 31.57 ?  357 TYR B OH    1 
ATOM   8452  N  N     . ILE B 1 358 ? 115.950 132.662 150.901 1.00 15.26 ?  358 ILE B N     1 
ATOM   8453  C  CA    . ILE B 1 358 ? 114.527 132.963 150.980 1.00 14.09 ?  358 ILE B CA    1 
ATOM   8454  C  C     . ILE B 1 358 ? 114.373 134.313 151.660 1.00 15.26 ?  358 ILE B C     1 
ATOM   8455  O  O     . ILE B 1 358 ? 114.837 134.504 152.789 1.00 24.51 ?  358 ILE B O     1 
ATOM   8456  C  CB    . ILE B 1 358 ? 113.756 131.872 151.737 1.00 23.12 ?  358 ILE B CB    1 
ATOM   8457  C  CG1   . ILE B 1 358 ? 113.863 130.534 151.004 1.00 15.21 ?  358 ILE B CG1   1 
ATOM   8458  C  CG2   . ILE B 1 358 ? 112.300 132.272 151.899 1.00 16.12 ?  358 ILE B CG2   1 
ATOM   8459  C  CD1   . ILE B 1 358 ? 113.322 130.567 149.594 1.00 19.53 ?  358 ILE B CD1   1 
ATOM   8460  N  N     . MET B 1 359 ? 113.728 135.250 150.970 1.00 17.72 ?  359 MET B N     1 
ATOM   8461  C  CA    . MET B 1 359 ? 113.430 136.570 151.514 1.00 7.28  ?  359 MET B CA    1 
ATOM   8462  C  C     . MET B 1 359 ? 111.918 136.736 151.549 1.00 9.30  ?  359 MET B C     1 
ATOM   8463  O  O     . MET B 1 359 ? 111.272 136.816 150.499 1.00 20.49 ?  359 MET B O     1 
ATOM   8464  C  CB    . MET B 1 359 ? 114.080 137.674 150.683 1.00 8.65  ?  359 MET B CB    1 
ATOM   8465  C  CG    . MET B 1 359 ? 113.954 139.055 151.302 1.00 9.10  ?  359 MET B CG    1 
ATOM   8466  S  SD    . MET B 1 359 ? 113.868 140.371 150.079 1.00 32.53 ?  359 MET B SD    1 
ATOM   8467  C  CE    . MET B 1 359 ? 112.852 141.562 150.939 1.00 9.56  ?  359 MET B CE    1 
ATOM   8468  N  N     . PHE B 1 360 ? 111.355 136.781 152.751 1.00 10.36 ?  360 PHE B N     1 
ATOM   8469  C  CA    . PHE B 1 360 ? 109.922 137.004 152.921 1.00 10.65 ?  360 PHE B CA    1 
ATOM   8470  C  C     . PHE B 1 360 ? 109.679 138.503 152.833 1.00 16.04 ?  360 PHE B C     1 
ATOM   8471  O  O     . PHE B 1 360 ? 109.847 139.231 153.814 1.00 19.76 ?  360 PHE B O     1 
ATOM   8472  C  CB    . PHE B 1 360 ? 109.445 136.419 154.242 1.00 12.02 ?  360 PHE B CB    1 
ATOM   8473  C  CG    . PHE B 1 360 ? 109.570 134.925 154.314 1.00 15.34 ?  360 PHE B CG    1 
ATOM   8474  C  CD1   . PHE B 1 360 ? 108.868 134.114 153.439 1.00 15.19 ?  360 PHE B CD1   1 
ATOM   8475  C  CD2   . PHE B 1 360 ? 110.404 134.331 155.246 1.00 14.96 ?  360 PHE B CD2   1 
ATOM   8476  C  CE1   . PHE B 1 360 ? 108.989 132.739 153.499 1.00 13.79 ?  360 PHE B CE1   1 
ATOM   8477  C  CE2   . PHE B 1 360 ? 110.529 132.959 155.310 1.00 14.37 ?  360 PHE B CE2   1 
ATOM   8478  C  CZ    . PHE B 1 360 ? 109.819 132.162 154.436 1.00 17.05 ?  360 PHE B CZ    1 
ATOM   8479  N  N     . GLN B 1 361 ? 109.271 138.961 151.646 1.00 16.85 ?  361 GLN B N     1 
ATOM   8480  C  CA    . GLN B 1 361 ? 109.220 140.393 151.359 1.00 9.93  ?  361 GLN B CA    1 
ATOM   8481  C  C     . GLN B 1 361 ? 108.276 141.127 152.302 1.00 13.61 ?  361 GLN B C     1 
ATOM   8482  O  O     . GLN B 1 361 ? 108.599 142.215 152.793 1.00 15.15 ?  361 GLN B O     1 
ATOM   8483  C  CB    . GLN B 1 361 ? 108.797 140.610 149.906 1.00 15.59 ?  361 GLN B CB    1 
ATOM   8484  C  CG    . GLN B 1 361 ? 108.808 142.056 149.457 1.00 15.46 ?  361 GLN B CG    1 
ATOM   8485  C  CD    . GLN B 1 361 ? 108.948 142.192 147.958 1.00 17.89 ?  361 GLN B CD    1 
ATOM   8486  O  OE1   . GLN B 1 361 ? 108.389 141.403 147.198 1.00 27.70 ?  361 GLN B OE1   1 
ATOM   8487  N  NE2   . GLN B 1 361 ? 109.701 143.193 147.520 1.00 18.34 ?  361 GLN B NE2   1 
ATOM   8488  N  N     . ASP B 1 362 ? 107.100 140.553 152.562 1.00 20.04 ?  362 ASP B N     1 
ATOM   8489  C  CA    . ASP B 1 362 ? 106.140 141.223 153.430 1.00 15.90 ?  362 ASP B CA    1 
ATOM   8490  C  C     . ASP B 1 362 ? 106.620 141.264 154.874 1.00 16.17 ?  362 ASP B C     1 
ATOM   8491  O  O     . ASP B 1 362 ? 106.366 142.245 155.578 1.00 23.66 ?  362 ASP B O     1 
ATOM   8492  C  CB    . ASP B 1 362 ? 104.779 140.540 153.336 1.00 22.13 ?  362 ASP B CB    1 
ATOM   8493  C  CG    . ASP B 1 362 ? 104.003 140.963 152.107 1.00 29.34 ?  362 ASP B CG    1 
ATOM   8494  O  OD1   . ASP B 1 362 ? 104.337 140.491 151.000 1.00 29.39 ?  362 ASP B OD1   1 
ATOM   8495  O  OD2   . ASP B 1 362 ? 103.060 141.769 152.246 1.00 30.44 -1 362 ASP B OD2   1 
ATOM   8496  N  N     . ASN B 1 363 ? 107.320 140.222 155.329 1.00 21.55 ?  363 ASN B N     1 
ATOM   8497  C  CA    . ASN B 1 363 ? 107.913 140.261 156.661 1.00 10.88 ?  363 ASN B CA    1 
ATOM   8498  C  C     . ASN B 1 363 ? 108.950 141.368 156.774 1.00 14.86 ?  363 ASN B C     1 
ATOM   8499  O  O     . ASN B 1 363 ? 109.087 141.988 157.834 1.00 25.42 ?  363 ASN B O     1 
ATOM   8500  C  CB    . ASN B 1 363 ? 108.544 138.910 156.997 1.00 12.50 ?  363 ASN B CB    1 
ATOM   8501  C  CG    . ASN B 1 363 ? 107.514 137.854 157.333 1.00 16.62 ?  363 ASN B CG    1 
ATOM   8502  O  OD1   . ASN B 1 363 ? 106.385 138.169 157.703 1.00 21.40 ?  363 ASN B OD1   1 
ATOM   8503  N  ND2   . ASN B 1 363 ? 107.898 136.591 157.206 1.00 15.52 ?  363 ASN B ND2   1 
ATOM   8504  N  N     . VAL B 1 364 ? 109.695 141.623 155.697 1.00 14.12 ?  364 VAL B N     1 
ATOM   8505  C  CA    . VAL B 1 364 ? 110.673 142.704 155.703 1.00 9.03  ?  364 VAL B CA    1 
ATOM   8506  C  C     . VAL B 1 364 ? 109.978 144.059 155.705 1.00 16.84 ?  364 VAL B C     1 
ATOM   8507  O  O     . VAL B 1 364 ? 110.377 144.974 156.435 1.00 18.99 ?  364 VAL B O     1 
ATOM   8508  C  CB    . VAL B 1 364 ? 111.627 142.565 154.504 1.00 2.44  ?  364 VAL B CB    1 
ATOM   8509  C  CG1   . VAL B 1 364 ? 112.693 143.642 154.550 1.00 6.38  ?  364 VAL B CG1   1 
ATOM   8510  C  CG2   . VAL B 1 364 ? 112.260 141.189 154.488 1.00 9.06  ?  364 VAL B CG2   1 
ATOM   8511  N  N     . ASN B 1 365 ? 108.931 144.214 154.896 1.00 18.91 ?  365 ASN B N     1 
ATOM   8512  C  CA    . ASN B 1 365 ? 108.350 145.526 154.652 1.00 7.74  ?  365 ASN B CA    1 
ATOM   8513  C  C     . ASN B 1 365 ? 107.236 145.901 155.621 1.00 15.37 ?  365 ASN B C     1 
ATOM   8514  O  O     . ASN B 1 365 ? 106.813 147.062 155.620 1.00 22.95 ?  365 ASN B O     1 
ATOM   8515  C  CB    . ASN B 1 365 ? 107.820 145.607 153.218 1.00 11.88 ?  365 ASN B CB    1 
ATOM   8516  C  CG    . ASN B 1 365 ? 108.931 145.687 152.195 1.00 13.44 ?  365 ASN B CG    1 
ATOM   8517  O  OD1   . ASN B 1 365 ? 109.832 146.518 152.304 1.00 15.79 ?  365 ASN B OD1   1 
ATOM   8518  N  ND2   . ASN B 1 365 ? 108.876 144.823 151.193 1.00 19.25 ?  365 ASN B ND2   1 
ATOM   8519  N  N     . LYS B 1 366 ? 106.749 144.970 156.441 1.00 15.39 ?  366 LYS B N     1 
ATOM   8520  C  CA    . LYS B 1 366 ? 105.755 145.333 157.442 1.00 17.04 ?  366 LYS B CA    1 
ATOM   8521  C  C     . LYS B 1 366 ? 106.367 146.084 158.614 1.00 19.24 ?  366 LYS B C     1 
ATOM   8522  O  O     . LYS B 1 366 ? 105.647 146.793 159.325 1.00 26.94 ?  366 LYS B O     1 
ATOM   8523  C  CB    . LYS B 1 366 ? 105.025 144.086 157.947 1.00 18.92 ?  366 LYS B CB    1 
ATOM   8524  C  CG    . LYS B 1 366 ? 105.921 143.064 158.627 1.00 22.26 ?  366 LYS B CG    1 
ATOM   8525  C  CD    . LYS B 1 366 ? 105.123 142.135 159.533 1.00 24.45 ?  366 LYS B CD    1 
ATOM   8526  C  CE    . LYS B 1 366 ? 103.785 141.752 158.916 1.00 24.01 ?  366 LYS B CE    1 
ATOM   8527  N  NZ    . LYS B 1 366 ? 103.936 140.768 157.809 1.00 24.16 1  366 LYS B NZ    1 
ATOM   8528  N  N     . VAL B 1 367 ? 107.673 145.945 158.828 1.00 24.11 ?  367 VAL B N     1 
ATOM   8529  C  CA    . VAL B 1 367 ? 108.395 146.686 159.851 1.00 14.42 ?  367 VAL B CA    1 
ATOM   8530  C  C     . VAL B 1 367 ? 109.493 147.557 159.266 1.00 16.80 ?  367 VAL B C     1 
ATOM   8531  O  O     . VAL B 1 367 ? 110.242 148.182 160.024 1.00 22.49 ?  367 VAL B O     1 
ATOM   8532  C  CB    . VAL B 1 367 ? 108.977 145.742 160.923 1.00 12.46 ?  367 VAL B CB    1 
ATOM   8533  C  CG1   . VAL B 1 367 ? 107.857 145.022 161.655 1.00 19.88 ?  367 VAL B CG1   1 
ATOM   8534  C  CG2   . VAL B 1 367 ? 109.925 144.746 160.288 1.00 9.76  ?  367 VAL B CG2   1 
ATOM   8535  N  N     . HIS B 1 368 ? 109.615 147.611 157.942 1.00 20.92 ?  368 HIS B N     1 
ATOM   8536  C  CA    . HIS B 1 368 ? 110.611 148.456 157.301 1.00 5.32  ?  368 HIS B CA    1 
ATOM   8537  C  C     . HIS B 1 368 ? 110.309 149.923 157.576 1.00 15.48 ?  368 HIS B C     1 
ATOM   8538  O  O     . HIS B 1 368 ? 109.185 150.388 157.363 1.00 25.96 ?  368 HIS B O     1 
ATOM   8539  C  CB    . HIS B 1 368 ? 110.632 148.184 155.799 1.00 13.01 ?  368 HIS B CB    1 
ATOM   8540  C  CG    . HIS B 1 368 ? 111.691 148.937 155.058 1.00 10.56 ?  368 HIS B CG    1 
ATOM   8541  N  ND1   . HIS B 1 368 ? 111.514 149.391 153.770 1.00 14.86 ?  368 HIS B ND1   1 
ATOM   8542  C  CD2   . HIS B 1 368 ? 112.940 149.310 155.421 1.00 7.35  ?  368 HIS B CD2   1 
ATOM   8543  C  CE1   . HIS B 1 368 ? 112.608 150.014 153.371 1.00 14.41 ?  368 HIS B CE1   1 
ATOM   8544  N  NE2   . HIS B 1 368 ? 113.489 149.978 154.354 1.00 10.81 ?  368 HIS B NE2   1 
ATOM   8545  N  N     . ALA B 1 369 ? 111.318 150.653 158.048 1.00 20.22 ?  369 ALA B N     1 
ATOM   8546  C  CA    . ALA B 1 369 ? 111.131 152.038 158.452 1.00 10.07 ?  369 ALA B CA    1 
ATOM   8547  C  C     . ALA B 1 369 ? 111.231 153.025 157.299 1.00 17.57 ?  369 ALA B C     1 
ATOM   8548  O  O     . ALA B 1 369 ? 110.871 154.192 157.477 1.00 26.04 ?  369 ALA B O     1 
ATOM   8549  C  CB    . ALA B 1 369 ? 112.154 152.408 159.527 1.00 10.84 ?  369 ALA B CB    1 
ATOM   8550  N  N     . ASN B 1 370 ? 111.698 152.596 156.130 1.00 16.15 ?  370 ASN B N     1 
ATOM   8551  C  CA    . ASN B 1 370 ? 111.938 153.487 155.004 1.00 14.72 ?  370 ASN B CA    1 
ATOM   8552  C  C     . ASN B 1 370 ? 111.183 153.029 153.763 1.00 12.00 ?  370 ASN B C     1 
ATOM   8553  O  O     . ASN B 1 370 ? 111.708 153.054 152.649 1.00 18.38 ?  370 ASN B O     1 
ATOM   8554  C  CB    . ASN B 1 370 ? 113.432 153.601 154.715 1.00 11.27 ?  370 ASN B CB    1 
ATOM   8555  C  CG    . ASN B 1 370 ? 114.213 154.136 155.897 1.00 11.90 ?  370 ASN B CG    1 
ATOM   8556  O  OD1   . ASN B 1 370 ? 113.961 155.243 156.370 1.00 26.54 ?  370 ASN B OD1   1 
ATOM   8557  N  ND2   . ASN B 1 370 ? 115.162 153.349 156.385 1.00 16.28 ?  370 ASN B ND2   1 
ATOM   8558  N  N     . ASN B 1 371 ? 109.932 152.600 153.945 1.00 20.31 ?  371 ASN B N     1 
ATOM   8559  C  CA    . ASN B 1 371 ? 109.105 152.212 152.810 1.00 10.79 ?  371 ASN B CA    1 
ATOM   8560  C  C     . ASN B 1 371 ? 108.795 153.386 151.892 1.00 16.41 ?  371 ASN B C     1 
ATOM   8561  O  O     . ASN B 1 371 ? 108.524 153.175 150.707 1.00 19.64 ?  371 ASN B O     1 
ATOM   8562  C  CB    . ASN B 1 371 ? 107.802 151.578 153.297 1.00 6.58  ?  371 ASN B CB    1 
ATOM   8563  C  CG    . ASN B 1 371 ? 107.944 150.099 153.579 1.00 16.28 ?  371 ASN B CG    1 
ATOM   8564  O  OD1   . ASN B 1 371 ? 108.823 149.434 153.032 1.00 20.36 ?  371 ASN B OD1   1 
ATOM   8565  N  ND2   . ASN B 1 371 ? 107.076 149.574 154.433 1.00 19.92 ?  371 ASN B ND2   1 
ATOM   8566  N  N     . HIS B 1 372 ? 108.821 154.613 152.418 1.00 21.65 ?  372 HIS B N     1 
ATOM   8567  C  CA    . HIS B 1 372 ? 108.580 155.787 151.586 1.00 17.77 ?  372 HIS B CA    1 
ATOM   8568  C  C     . HIS B 1 372 ? 109.654 155.935 150.516 1.00 20.25 ?  372 HIS B C     1 
ATOM   8569  O  O     . HIS B 1 372 ? 109.350 156.255 149.361 1.00 26.17 ?  372 HIS B O     1 
ATOM   8570  C  CB    . HIS B 1 372 ? 108.515 157.038 152.460 1.00 19.55 ?  372 HIS B CB    1 
ATOM   8571  C  CG    . HIS B 1 372 ? 109.809 157.367 153.136 1.00 19.08 ?  372 HIS B CG    1 
ATOM   8572  N  ND1   . HIS B 1 372 ? 110.418 156.516 154.033 1.00 22.10 ?  372 HIS B ND1   1 
ATOM   8573  C  CD2   . HIS B 1 372 ? 110.615 158.450 153.038 1.00 20.71 ?  372 HIS B CD2   1 
ATOM   8574  C  CE1   . HIS B 1 372 ? 111.543 157.061 154.459 1.00 17.13 ?  372 HIS B CE1   1 
ATOM   8575  N  NE2   . HIS B 1 372 ? 111.683 158.236 153.873 1.00 24.73 ?  372 HIS B NE2   1 
ATOM   8576  N  N     . ILE B 1 373 ? 110.920 155.717 150.883 1.00 16.01 ?  373 ILE B N     1 
ATOM   8577  C  CA    . ILE B 1 373 ? 111.997 155.758 149.899 1.00 18.41 ?  373 ILE B CA    1 
ATOM   8578  C  C     . ILE B 1 373 ? 111.812 154.645 148.878 1.00 18.51 ?  373 ILE B C     1 
ATOM   8579  O  O     . ILE B 1 373 ? 111.812 154.882 147.663 1.00 28.73 ?  373 ILE B O     1 
ATOM   8580  C  CB    . ILE B 1 373 ? 113.364 155.650 150.599 1.00 20.64 ?  373 ILE B CB    1 
ATOM   8581  C  CG1   . ILE B 1 373 ? 113.564 156.821 151.558 1.00 18.92 ?  373 ILE B CG1   1 
ATOM   8582  C  CG2   . ILE B 1 373 ? 114.488 155.591 149.575 1.00 19.25 ?  373 ILE B CG2   1 
ATOM   8583  C  CD1   . ILE B 1 373 ? 114.723 156.645 152.503 1.00 14.77 ?  373 ILE B CD1   1 
ATOM   8584  N  N     . SER B 1 374 ? 111.627 153.421 149.364 1.00 17.14 ?  374 SER B N     1 
ATOM   8585  C  CA    . SER B 1 374 ? 111.420 152.246 148.530 1.00 6.86  ?  374 SER B CA    1 
ATOM   8586  C  C     . SER B 1 374 ? 111.139 151.046 149.420 1.00 13.56 ?  374 SER B C     1 
ATOM   8587  O  O     . SER B 1 374 ? 111.559 151.019 150.581 1.00 16.95 ?  374 SER B O     1 
ATOM   8588  C  CB    . SER B 1 374 ? 112.641 151.978 147.650 1.00 18.97 ?  374 SER B CB    1 
ATOM   8589  O  OG    . SER B 1 374 ? 112.303 151.162 146.545 1.00 32.64 ?  374 SER B OG    1 
ATOM   8590  N  N     . LYS B 1 375 ? 110.427 150.056 148.899 1.00 24.02 ?  375 LYS B N     1 
ATOM   8591  C  CA    . LYS B 1 375 ? 110.298 148.792 149.601 1.00 14.13 ?  375 LYS B CA    1 
ATOM   8592  C  C     . LYS B 1 375 ? 111.553 147.958 149.391 1.00 15.05 ?  375 LYS B C     1 
ATOM   8593  O  O     . LYS B 1 375 ? 112.248 148.088 148.381 1.00 23.95 ?  375 LYS B O     1 
ATOM   8594  C  CB    . LYS B 1 375 ? 109.070 148.021 149.117 1.00 11.94 ?  375 LYS B CB    1 
ATOM   8595  C  CG    . LYS B 1 375 ? 107.759 148.752 149.320 1.00 17.96 ?  375 LYS B CG    1 
ATOM   8596  C  CD    . LYS B 1 375 ? 106.933 148.103 150.415 1.00 17.81 ?  375 LYS B CD    1 
ATOM   8597  C  CE    . LYS B 1 375 ? 105.595 148.800 150.577 1.00 16.98 ?  375 LYS B CE    1 
ATOM   8598  N  NZ    . LYS B 1 375 ? 105.708 150.269 150.372 1.00 23.96 1  375 LYS B NZ    1 
ATOM   8599  N  N     . VAL B 1 376 ? 111.850 147.102 150.362 1.00 9.75  ?  376 VAL B N     1 
ATOM   8600  C  CA    . VAL B 1 376 ? 112.985 146.195 150.239 1.00 13.73 ?  376 VAL B CA    1 
ATOM   8601  C  C     . VAL B 1 376 ? 112.591 145.068 149.294 1.00 16.12 ?  376 VAL B C     1 
ATOM   8602  O  O     . VAL B 1 376 ? 111.679 144.288 149.590 1.00 23.12 ?  376 VAL B O     1 
ATOM   8603  C  CB    . VAL B 1 376 ? 113.416 145.652 151.606 1.00 11.90 ?  376 VAL B CB    1 
ATOM   8604  C  CG1   . VAL B 1 376 ? 114.634 144.761 151.454 1.00 10.55 ?  376 VAL B CG1   1 
ATOM   8605  C  CG2   . VAL B 1 376 ? 113.704 146.793 152.563 1.00 6.92  ?  376 VAL B CG2   1 
ATOM   8606  N  N     . LYS B 1 377 ? 113.271 144.984 148.152 1.00 14.55 ?  377 LYS B N     1 
ATOM   8607  C  CA    . LYS B 1 377 ? 112.920 144.011 147.129 1.00 9.58  ?  377 LYS B CA    1 
ATOM   8608  C  C     . LYS B 1 377 ? 113.872 142.829 147.060 1.00 9.63  ?  377 LYS B C     1 
ATOM   8609  O  O     . LYS B 1 377 ? 113.542 141.833 146.412 1.00 24.47 ?  377 LYS B O     1 
ATOM   8610  C  CB    . LYS B 1 377 ? 112.866 144.676 145.750 1.00 13.22 ?  377 LYS B CB    1 
ATOM   8611  C  CG    . LYS B 1 377 ? 112.094 145.973 145.714 1.00 9.80  ?  377 LYS B CG    1 
ATOM   8612  C  CD    . LYS B 1 377 ? 112.734 146.935 144.740 1.00 18.20 ?  377 LYS B CD    1 
ATOM   8613  C  CE    . LYS B 1 377 ? 112.536 148.367 145.173 1.00 20.76 ?  377 LYS B CE    1 
ATOM   8614  N  NZ    . LYS B 1 377 ? 113.431 149.289 144.423 1.00 19.82 1  377 LYS B NZ    1 
ATOM   8615  N  N     . PHE B 1 378 ? 115.038 142.915 147.692 1.00 11.14 ?  378 PHE B N     1 
ATOM   8616  C  CA    . PHE B 1 378 ? 116.004 141.825 147.672 1.00 8.11  ?  378 PHE B CA    1 
ATOM   8617  C  C     . PHE B 1 378 ? 116.978 142.024 148.825 1.00 7.41  ?  378 PHE B C     1 
ATOM   8618  O  O     . PHE B 1 378 ? 116.950 143.043 149.521 1.00 16.36 ?  378 PHE B O     1 
ATOM   8619  C  CB    . PHE B 1 378 ? 116.715 141.738 146.317 1.00 4.29  ?  378 PHE B CB    1 
ATOM   8620  C  CG    . PHE B 1 378 ? 117.708 142.837 146.067 1.00 4.17  ?  378 PHE B CG    1 
ATOM   8621  C  CD1   . PHE B 1 378 ? 117.307 144.160 146.026 1.00 10.59 ?  378 PHE B CD1   1 
ATOM   8622  C  CD2   . PHE B 1 378 ? 119.041 142.540 145.849 1.00 3.19  ?  378 PHE B CD2   1 
ATOM   8623  C  CE1   . PHE B 1 378 ? 118.217 145.166 145.789 1.00 7.65  ?  378 PHE B CE1   1 
ATOM   8624  C  CE2   . PHE B 1 378 ? 119.954 143.543 145.610 1.00 10.18 ?  378 PHE B CE2   1 
ATOM   8625  C  CZ    . PHE B 1 378 ? 119.540 144.858 145.578 1.00 11.71 ?  378 PHE B CZ    1 
ATOM   8626  N  N     . SER B 1 379 ? 117.839 141.034 149.028 1.00 2.13  ?  379 SER B N     1 
ATOM   8627  C  CA    . SER B 1 379 ? 118.815 141.037 150.108 1.00 0.54  ?  379 SER B CA    1 
ATOM   8628  C  C     . SER B 1 379 ? 120.221 140.920 149.524 1.00 4.59  ?  379 SER B C     1 
ATOM   8629  O  O     . SER B 1 379 ? 120.416 140.949 148.306 1.00 7.64  ?  379 SER B O     1 
ATOM   8630  C  CB    . SER B 1 379 ? 118.519 139.911 151.101 1.00 10.27 ?  379 SER B CB    1 
ATOM   8631  O  OG    . SER B 1 379 ? 118.940 140.267 152.404 1.00 10.56 ?  379 SER B OG    1 
ATOM   8632  N  N     . ASN B 1 380 ? 121.206 140.800 150.406 1.00 11.08 ?  380 ASN B N     1 
ATOM   8633  C  CA    . ASN B 1 380 ? 122.603 140.752 150.016 1.00 7.33  ?  380 ASN B CA    1 
ATOM   8634  C  C     . ASN B 1 380 ? 123.053 139.301 149.854 1.00 13.50 ?  380 ASN B C     1 
ATOM   8635  O  O     . ASN B 1 380 ? 122.247 138.366 149.879 1.00 16.85 ?  380 ASN B O     1 
ATOM   8636  C  CB    . ASN B 1 380 ? 123.459 141.505 151.036 1.00 8.68  ?  380 ASN B CB    1 
ATOM   8637  C  CG    . ASN B 1 380 ? 123.509 140.816 152.380 1.00 6.85  ?  380 ASN B CG    1 
ATOM   8638  O  OD1   . ASN B 1 380 ? 122.485 140.394 152.913 1.00 19.12 ?  380 ASN B OD1   1 
ATOM   8639  N  ND2   . ASN B 1 380 ? 124.706 140.699 152.938 1.00 13.32 ?  380 ASN B ND2   1 
ATOM   8640  N  N     . LEU B 1 381 ? 124.360 139.109 149.672 1.00 18.23 ?  381 LEU B N     1 
ATOM   8641  C  CA    . LEU B 1 381 ? 124.912 137.774 149.484 1.00 11.49 ?  381 LEU B CA    1 
ATOM   8642  C  C     . LEU B 1 381 ? 124.770 136.908 150.730 1.00 7.62  ?  381 LEU B C     1 
ATOM   8643  O  O     . LEU B 1 381 ? 124.716 135.680 150.614 1.00 18.28 ?  381 LEU B O     1 
ATOM   8644  C  CB    . LEU B 1 381 ? 126.382 137.883 149.071 1.00 17.87 ?  381 LEU B CB    1 
ATOM   8645  C  CG    . LEU B 1 381 ? 127.222 136.613 148.915 1.00 19.37 ?  381 LEU B CG    1 
ATOM   8646  C  CD1   . LEU B 1 381 ? 126.765 135.798 147.719 1.00 15.88 ?  381 LEU B CD1   1 
ATOM   8647  C  CD2   . LEU B 1 381 ? 128.691 136.970 148.793 1.00 17.74 ?  381 LEU B CD2   1 
ATOM   8648  N  N     . CYS B 1 382 ? 124.694 137.515 151.912 1.00 11.63 ?  382 CYS B N     1 
ATOM   8649  C  CA    . CYS B 1 382 ? 124.479 136.783 153.150 1.00 5.10  ?  382 CYS B CA    1 
ATOM   8650  C  C     . CYS B 1 382 ? 123.044 136.882 153.648 1.00 8.11  ?  382 CYS B C     1 
ATOM   8651  O  O     . CYS B 1 382 ? 122.742 136.371 154.730 1.00 17.87 ?  382 CYS B O     1 
ATOM   8652  C  CB    . CYS B 1 382 ? 125.444 137.276 154.230 1.00 16.37 ?  382 CYS B CB    1 
ATOM   8653  S  SG    . CYS B 1 382 ? 127.174 137.345 153.711 1.00 31.70 ?  382 CYS B SG    1 
ATOM   8654  N  N     . SER B 1 383 ? 122.159 137.525 152.884 1.00 10.35 ?  383 SER B N     1 
ATOM   8655  C  CA    . SER B 1 383 ? 120.725 137.591 153.178 1.00 9.66  ?  383 SER B CA    1 
ATOM   8656  C  C     . SER B 1 383 ? 120.449 138.157 154.568 1.00 12.91 ?  383 SER B C     1 
ATOM   8657  O  O     . SER B 1 383 ? 119.616 137.645 155.317 1.00 23.55 ?  383 SER B O     1 
ATOM   8658  C  CB    . SER B 1 383 ? 120.064 136.221 153.012 1.00 13.23 ?  383 SER B CB    1 
ATOM   8659  O  OG    . SER B 1 383 ? 120.611 135.273 153.905 1.00 18.79 ?  383 SER B OG    1 
ATOM   8660  N  N     . GLU B 1 384 ? 121.162 139.225 154.925 1.00 7.46  ?  384 GLU B N     1 
ATOM   8661  C  CA    . GLU B 1 384 ? 120.879 139.948 156.155 1.00 8.37  ?  384 GLU B CA    1 
ATOM   8662  C  C     . GLU B 1 384 ? 120.724 141.447 155.953 1.00 13.49 ?  384 GLU B C     1 
ATOM   8663  O  O     . GLU B 1 384 ? 120.227 142.124 156.861 1.00 23.85 ?  384 GLU B O     1 
ATOM   8664  C  CB    . GLU B 1 384 ? 121.970 139.683 157.207 1.00 6.60  ?  384 GLU B CB    1 
ATOM   8665  C  CG    . GLU B 1 384 ? 122.985 140.798 157.410 1.00 10.32 ?  384 GLU B CG    1 
ATOM   8666  C  CD    . GLU B 1 384 ? 124.078 140.793 156.367 1.00 19.47 ?  384 GLU B CD    1 
ATOM   8667  O  OE1   . GLU B 1 384 ? 124.208 139.783 155.650 1.00 13.01 ?  384 GLU B OE1   1 
ATOM   8668  O  OE2   . GLU B 1 384 ? 124.818 141.793 156.277 1.00 26.60 -1 384 GLU B OE2   1 
ATOM   8669  N  N     . VAL B 1 385 ? 121.109 141.984 154.802 1.00 10.47 ?  385 VAL B N     1 
ATOM   8670  C  CA    . VAL B 1 385 ? 120.933 143.398 154.503 1.00 6.73  ?  385 VAL B CA    1 
ATOM   8671  C  C     . VAL B 1 385 ? 119.586 143.578 153.818 1.00 15.55 ?  385 VAL B C     1 
ATOM   8672  O  O     . VAL B 1 385 ? 119.339 142.996 152.756 1.00 24.31 ?  385 VAL B O     1 
ATOM   8673  C  CB    . VAL B 1 385 ? 122.073 143.926 153.623 1.00 6.60  ?  385 VAL B CB    1 
ATOM   8674  C  CG1   . VAL B 1 385 ? 121.778 145.339 153.188 1.00 6.70  ?  385 VAL B CG1   1 
ATOM   8675  C  CG2   . VAL B 1 385 ? 123.380 143.867 154.374 1.00 11.92 ?  385 VAL B CG2   1 
ATOM   8676  N  N     . LEU B 1 386 ? 118.715 144.381 154.425 1.00 12.50 ?  386 LEU B N     1 
ATOM   8677  C  CA    . LEU B 1 386 ? 117.358 144.611 153.926 1.00 2.08  ?  386 LEU B CA    1 
ATOM   8678  C  C     . LEU B 1 386 ? 117.089 146.111 153.981 1.00 5.19  ?  386 LEU B C     1 
ATOM   8679  O  O     . LEU B 1 386 ? 116.647 146.636 155.006 1.00 11.17 ?  386 LEU B O     1 
ATOM   8680  C  CB    . LEU B 1 386 ? 116.344 143.818 154.734 1.00 5.06  ?  386 LEU B CB    1 
ATOM   8681  C  CG    . LEU B 1 386 ? 116.494 142.304 154.594 1.00 5.85  ?  386 LEU B CG    1 
ATOM   8682  C  CD1   . LEU B 1 386 ? 115.698 141.601 155.659 1.00 10.23 ?  386 LEU B CD1   1 
ATOM   8683  C  CD2   . LEU B 1 386 ? 116.063 141.848 153.210 1.00 8.67  ?  386 LEU B CD2   1 
ATOM   8684  N  N     . GLN B 1 387 ? 117.356 146.794 152.872 1.00 11.72 ?  387 GLN B N     1 
ATOM   8685  C  CA    . GLN B 1 387 ? 117.279 148.244 152.818 1.00 9.78  ?  387 GLN B CA    1 
ATOM   8686  C  C     . GLN B 1 387 ? 116.543 148.677 151.560 1.00 11.25 ?  387 GLN B C     1 
ATOM   8687  O  O     . GLN B 1 387 ? 116.421 147.923 150.592 1.00 19.86 ?  387 GLN B O     1 
ATOM   8688  C  CB    . GLN B 1 387 ? 118.674 148.880 152.855 1.00 4.43  ?  387 GLN B CB    1 
ATOM   8689  C  CG    . GLN B 1 387 ? 119.521 148.437 154.029 1.00 6.44  ?  387 GLN B CG    1 
ATOM   8690  C  CD    . GLN B 1 387 ? 120.859 149.129 154.063 1.00 10.27 ?  387 GLN B CD    1 
ATOM   8691  O  OE1   . GLN B 1 387 ? 121.061 150.137 153.390 1.00 21.83 ?  387 GLN B OE1   1 
ATOM   8692  N  NE2   . GLN B 1 387 ? 121.784 148.595 154.848 1.00 10.90 ?  387 GLN B NE2   1 
ATOM   8693  N  N     . ALA B 1 388 ? 116.038 149.907 151.594 1.00 13.59 ?  388 ALA B N     1 
ATOM   8694  C  CA    . ALA B 1 388 ? 115.391 150.487 150.428 1.00 10.79 ?  388 ALA B CA    1 
ATOM   8695  C  C     . ALA B 1 388 ? 116.407 150.735 149.322 1.00 17.73 ?  388 ALA B C     1 
ATOM   8696  O  O     . ALA B 1 388 ? 117.520 151.206 149.570 1.00 23.67 ?  388 ALA B O     1 
ATOM   8697  C  CB    . ALA B 1 388 ? 114.696 151.795 150.802 1.00 9.43  ?  388 ALA B CB    1 
ATOM   8698  N  N     . SER B 1 389 ? 116.020 150.412 148.091 1.00 21.15 ?  389 SER B N     1 
ATOM   8699  C  CA    . SER B 1 389 ? 116.865 150.643 146.931 1.00 8.55  ?  389 SER B CA    1 
ATOM   8700  C  C     . SER B 1 389 ? 116.022 151.194 145.796 1.00 16.13 ?  389 SER B C     1 
ATOM   8701  O  O     . SER B 1 389 ? 114.892 150.749 145.575 1.00 23.96 ?  389 SER B O     1 
ATOM   8702  C  CB    . SER B 1 389 ? 117.570 149.359 146.480 1.00 14.47 ?  389 SER B CB    1 
ATOM   8703  O  OG    . SER B 1 389 ? 116.644 148.300 146.308 1.00 24.83 ?  389 SER B OG    1 
ATOM   8704  N  N     . GLN B 1 390 ? 116.575 152.167 145.081 1.00 17.90 ?  390 GLN B N     1 
ATOM   8705  C  CA    . GLN B 1 390 ? 115.955 152.730 143.892 1.00 11.04 ?  390 GLN B CA    1 
ATOM   8706  C  C     . GLN B 1 390 ? 116.802 152.365 142.684 1.00 12.59 ?  390 GLN B C     1 
ATOM   8707  O  O     . GLN B 1 390 ? 118.021 152.567 142.693 1.00 26.82 ?  390 GLN B O     1 
ATOM   8708  C  CB    . GLN B 1 390 ? 115.809 154.248 144.015 1.00 16.03 ?  390 GLN B CB    1 
ATOM   8709  C  CG    . GLN B 1 390 ? 114.803 154.683 145.070 1.00 18.30 ?  390 GLN B CG    1 
ATOM   8710  C  CD    . GLN B 1 390 ? 114.825 156.175 145.325 1.00 22.91 ?  390 GLN B CD    1 
ATOM   8711  O  OE1   . GLN B 1 390 ? 115.688 156.891 144.818 1.00 25.83 ?  390 GLN B OE1   1 
ATOM   8712  N  NE2   . GLN B 1 390 ? 113.871 156.654 146.116 1.00 18.30 ?  390 GLN B NE2   1 
ATOM   8713  N  N     . VAL B 1 391 ? 116.159 151.815 141.654 1.00 22.98 ?  391 VAL B N     1 
ATOM   8714  C  CA    . VAL B 1 391 ? 116.892 151.371 140.476 1.00 20.87 ?  391 VAL B CA    1 
ATOM   8715  C  C     . VAL B 1 391 ? 117.447 152.579 139.729 1.00 23.00 ?  391 VAL B C     1 
ATOM   8716  O  O     . VAL B 1 391 ? 116.876 153.678 139.753 1.00 21.34 ?  391 VAL B O     1 
ATOM   8717  C  CB    . VAL B 1 391 ? 115.995 150.507 139.570 1.00 15.39 ?  391 VAL B CB    1 
ATOM   8718  C  CG1   . VAL B 1 391 ? 115.043 151.370 138.756 1.00 20.83 ?  391 VAL B CG1   1 
ATOM   8719  C  CG2   . VAL B 1 391 ? 116.841 149.627 138.663 1.00 17.46 ?  391 VAL B CG2   1 
ATOM   8720  N  N     . SER B 1 392 ? 118.587 152.379 139.077 1.00 28.78 ?  392 SER B N     1 
ATOM   8721  C  CA    . SER B 1 392 ? 119.236 153.423 138.300 1.00 21.82 ?  392 SER B CA    1 
ATOM   8722  C  C     . SER B 1 392 ? 118.899 153.264 136.824 1.00 28.18 ?  392 SER B C     1 
ATOM   8723  O  O     . SER B 1 392 ? 118.728 152.150 136.323 1.00 31.29 ?  392 SER B O     1 
ATOM   8724  C  CB    . SER B 1 392 ? 120.754 153.387 138.492 1.00 20.84 ?  392 SER B CB    1 
ATOM   8725  O  OG    . SER B 1 392 ? 121.101 153.552 139.855 1.00 30.03 ?  392 SER B OG    1 
ATOM   8726  N  N     . SER B 1 393 ? 118.802 154.393 136.133 1.00 25.65 ?  393 SER B N     1 
ATOM   8727  C  CA    . SER B 1 393 ? 118.547 154.423 134.696 1.00 23.85 ?  393 SER B CA    1 
ATOM   8728  C  C     . SER B 1 393 ? 119.864 154.773 134.009 1.00 25.99 ?  393 SER B C     1 
ATOM   8729  O  O     . SER B 1 393 ? 120.170 155.943 133.778 1.00 31.14 ?  393 SER B O     1 
ATOM   8730  C  CB    . SER B 1 393 ? 117.448 155.421 134.349 1.00 28.94 ?  393 SER B CB    1 
ATOM   8731  O  OG    . SER B 1 393 ? 116.311 155.236 135.175 1.00 31.30 ?  393 SER B OG    1 
ATOM   8732  N  N     . TYR B 1 394 ? 120.647 153.745 133.695 1.00 28.75 ?  394 TYR B N     1 
ATOM   8733  C  CA    . TYR B 1 394 ? 121.890 153.927 132.954 1.00 26.75 ?  394 TYR B CA    1 
ATOM   8734  C  C     . TYR B 1 394 ? 121.546 154.038 131.475 1.00 26.39 ?  394 TYR B C     1 
ATOM   8735  O  O     . TYR B 1 394 ? 121.123 153.059 130.852 1.00 29.18 ?  394 TYR B O     1 
ATOM   8736  C  CB    . TYR B 1 394 ? 122.848 152.773 133.220 1.00 24.95 ?  394 TYR B CB    1 
ATOM   8737  C  CG    . TYR B 1 394 ? 123.274 152.659 134.667 1.00 23.85 ?  394 TYR B CG    1 
ATOM   8738  C  CD1   . TYR B 1 394 ? 124.064 153.635 135.257 1.00 23.65 ?  394 TYR B CD1   1 
ATOM   8739  C  CD2   . TYR B 1 394 ? 122.878 151.579 135.444 1.00 25.91 ?  394 TYR B CD2   1 
ATOM   8740  C  CE1   . TYR B 1 394 ? 124.453 153.536 136.579 1.00 28.58 ?  394 TYR B CE1   1 
ATOM   8741  C  CE2   . TYR B 1 394 ? 123.261 151.470 136.765 1.00 26.75 ?  394 TYR B CE2   1 
ATOM   8742  C  CZ    . TYR B 1 394 ? 124.048 152.452 137.327 1.00 30.68 ?  394 TYR B CZ    1 
ATOM   8743  O  OH    . TYR B 1 394 ? 124.433 152.349 138.645 1.00 34.71 ?  394 TYR B OH    1 
ATOM   8744  N  N     . THR B 1 395 ? 121.716 155.228 130.915 1.00 31.26 ?  395 THR B N     1 
ATOM   8745  C  CA    . THR B 1 395 ? 121.296 155.523 129.558 1.00 30.91 ?  395 THR B CA    1 
ATOM   8746  C  C     . THR B 1 395 ? 122.445 155.274 128.585 1.00 32.44 ?  395 THR B C     1 
ATOM   8747  O  O     . THR B 1 395 ? 123.494 154.728 128.945 1.00 32.19 ?  395 THR B O     1 
ATOM   8748  C  CB    . THR B 1 395 ? 120.781 156.960 129.479 1.00 30.55 ?  395 THR B CB    1 
ATOM   8749  O  OG1   . THR B 1 395 ? 121.804 157.860 129.925 1.00 32.79 ?  395 THR B OG1   1 
ATOM   8750  C  CG2   . THR B 1 395 ? 119.552 157.130 130.356 1.00 30.29 ?  395 THR B CG2   1 
ATOM   8751  N  N     . ASP B 1 396 ? 122.249 155.674 127.333 1.00 33.29 ?  396 ASP B N     1 
ATOM   8752  C  CA    . ASP B 1 396 ? 123.273 155.507 126.316 1.00 31.68 ?  396 ASP B CA    1 
ATOM   8753  C  C     . ASP B 1 396 ? 124.467 156.410 126.604 1.00 34.49 ?  396 ASP B C     1 
ATOM   8754  O  O     . ASP B 1 396 ? 124.407 157.327 127.428 1.00 40.59 ?  396 ASP B O     1 
ATOM   8755  C  CB    . ASP B 1 396 ? 122.714 155.818 124.929 1.00 33.18 ?  396 ASP B CB    1 
ATOM   8756  C  CG    . ASP B 1 396 ? 121.628 154.852 124.504 1.00 36.09 ?  396 ASP B CG    1 
ATOM   8757  O  OD1   . ASP B 1 396 ? 121.587 153.725 125.039 1.00 39.61 ?  396 ASP B OD1   1 
ATOM   8758  O  OD2   . ASP B 1 396 ? 120.816 155.219 123.629 1.00 36.46 -1 396 ASP B OD2   1 
ATOM   8759  N  N     . TYR B 1 397 ? 125.571 156.132 125.916 1.00 32.92 ?  397 TYR B N     1 
ATOM   8760  C  CA    . TYR B 1 397 ? 126.735 156.999 126.004 1.00 32.88 ?  397 TYR B CA    1 
ATOM   8761  C  C     . TYR B 1 397 ? 126.389 158.387 125.478 1.00 38.23 ?  397 TYR B C     1 
ATOM   8762  O  O     . TYR B 1 397 ? 125.560 158.544 124.577 1.00 43.77 ?  397 TYR B O     1 
ATOM   8763  C  CB    . TYR B 1 397 ? 127.906 156.407 125.220 1.00 31.40 ?  397 TYR B CB    1 
ATOM   8764  C  CG    . TYR B 1 397 ? 129.259 156.882 125.695 1.00 31.29 ?  397 TYR B CG    1 
ATOM   8765  C  CD1   . TYR B 1 397 ? 129.800 158.073 125.230 1.00 34.49 ?  397 TYR B CD1   1 
ATOM   8766  C  CD2   . TYR B 1 397 ? 129.994 156.141 126.609 1.00 32.36 ?  397 TYR B CD2   1 
ATOM   8767  C  CE1   . TYR B 1 397 ? 131.035 158.511 125.661 1.00 33.49 ?  397 TYR B CE1   1 
ATOM   8768  C  CE2   . TYR B 1 397 ? 131.231 156.571 127.045 1.00 29.46 ?  397 TYR B CE2   1 
ATOM   8769  C  CZ    . TYR B 1 397 ? 131.746 157.756 126.569 1.00 31.74 ?  397 TYR B CZ    1 
ATOM   8770  O  OH    . TYR B 1 397 ? 132.977 158.190 127.000 1.00 35.13 ?  397 TYR B OH    1 
ATOM   8771  N  N     . ASP B 1 398 ? 127.021 159.401 126.072 1.00 35.77 ?  398 ASP B N     1 
ATOM   8772  C  CA    . ASP B 1 398 ? 126.765 160.818 125.825 1.00 40.56 ?  398 ASP B CA    1 
ATOM   8773  C  C     . ASP B 1 398 ? 125.398 161.258 126.328 1.00 41.34 ?  398 ASP B C     1 
ATOM   8774  O  O     . ASP B 1 398 ? 124.951 162.366 126.004 1.00 39.21 ?  398 ASP B O     1 
ATOM   8775  C  CB    . ASP B 1 398 ? 126.908 161.186 124.342 1.00 39.07 ?  398 ASP B CB    1 
ATOM   8776  C  CG    . ASP B 1 398 ? 128.200 161.920 124.046 1.00 44.22 ?  398 ASP B CG    1 
ATOM   8777  O  OD1   . ASP B 1 398 ? 128.294 162.548 122.970 1.00 42.46 ?  398 ASP B OD1   1 
ATOM   8778  O  OD2   . ASP B 1 398 ? 129.122 161.869 124.888 1.00 45.23 -1 398 ASP B OD2   1 
ATOM   8779  N  N     . GLU B 1 399 ? 124.719 160.424 127.111 1.00 44.70 ?  399 GLU B N     1 
ATOM   8780  C  CA    . GLU B 1 399 ? 123.453 160.770 127.740 1.00 41.11 ?  399 GLU B CA    1 
ATOM   8781  C  C     . GLU B 1 399 ? 123.607 160.666 129.250 1.00 44.21 ?  399 GLU B C     1 
ATOM   8782  O  O     . GLU B 1 399 ? 124.282 159.764 129.754 1.00 39.66 ?  399 GLU B O     1 
ATOM   8783  C  CB    . GLU B 1 399 ? 122.322 159.853 127.262 1.00 37.86 ?  399 GLU B CB    1 
ATOM   8784  C  CG    . GLU B 1 399 ? 122.013 159.968 125.779 1.00 43.97 ?  399 GLU B CG    1 
ATOM   8785  C  CD    . GLU B 1 399 ? 121.356 161.286 125.421 1.00 47.43 ?  399 GLU B CD    1 
ATOM   8786  O  OE1   . GLU B 1 399 ? 120.475 161.740 126.181 1.00 47.85 ?  399 GLU B OE1   1 
ATOM   8787  O  OE2   . GLU B 1 399 ? 121.722 161.870 124.379 1.00 46.53 -1 399 GLU B OE2   1 
ATOM   8788  N  N     . GLU B 1 400 ? 122.984 161.596 129.968 1.00 45.70 ?  400 GLU B N     1 
ATOM   8789  C  CA    . GLU B 1 400 ? 123.070 161.596 131.422 1.00 39.54 ?  400 GLU B CA    1 
ATOM   8790  C  C     . GLU B 1 400 ? 122.313 160.406 131.997 1.00 40.22 ?  400 GLU B C     1 
ATOM   8791  O  O     . GLU B 1 400 ? 121.195 160.101 131.570 1.00 39.36 ?  400 GLU B O     1 
ATOM   8792  C  CB    . GLU B 1 400 ? 122.515 162.901 131.987 1.00 40.02 ?  400 GLU B CB    1 
ATOM   8793  C  CG    . GLU B 1 400 ? 123.513 164.046 131.992 1.00 44.35 ?  400 GLU B CG    1 
ATOM   8794  C  CD    . GLU B 1 400 ? 124.829 163.669 132.640 1.00 47.31 ?  400 GLU B CD    1 
ATOM   8795  O  OE1   . GLU B 1 400 ? 124.824 163.315 133.837 1.00 46.59 ?  400 GLU B OE1   1 
ATOM   8796  O  OE2   . GLU B 1 400 ? 125.869 163.725 131.953 1.00 45.60 -1 400 GLU B OE2   1 
ATOM   8797  N  N     . ASP B 1 401 ? 122.926 159.734 132.967 1.00 35.64 ?  401 ASP B N     1 
ATOM   8798  C  CA    . ASP B 1 401 ? 122.305 158.601 133.634 1.00 31.88 ?  401 ASP B CA    1 
ATOM   8799  C  C     . ASP B 1 401 ? 121.541 159.068 134.864 1.00 32.92 ?  401 ASP B C     1 
ATOM   8800  O  O     . ASP B 1 401 ? 121.986 159.967 135.582 1.00 38.51 ?  401 ASP B O     1 
ATOM   8801  C  CB    . ASP B 1 401 ? 123.357 157.567 134.039 1.00 31.73 ?  401 ASP B CB    1 
ATOM   8802  C  CG    . ASP B 1 401 ? 124.184 157.084 132.867 1.00 36.42 ?  401 ASP B CG    1 
ATOM   8803  O  OD1   . ASP B 1 401 ? 123.727 157.224 131.713 1.00 38.79 ?  401 ASP B OD1   1 
ATOM   8804  O  OD2   . ASP B 1 401 ? 125.294 156.563 133.099 1.00 38.06 -1 401 ASP B OD2   1 
ATOM   8805  N  N     . GLU B 1 402 ? 120.385 158.452 135.101 1.00 29.52 ?  402 GLU B N     1 
ATOM   8806  C  CA    . GLU B 1 402 ? 119.605 158.703 136.311 1.00 27.64 ?  402 GLU B CA    1 
ATOM   8807  C  C     . GLU B 1 402 ? 120.104 157.742 137.382 1.00 29.15 ?  402 GLU B C     1 
ATOM   8808  O  O     . GLU B 1 402 ? 119.796 156.550 137.357 1.00 30.97 ?  402 GLU B O     1 
ATOM   8809  C  CB    . GLU B 1 402 ? 118.115 158.530 136.045 1.00 29.73 ?  402 GLU B CB    1 
ATOM   8810  C  CG    . GLU B 1 402 ? 117.507 159.620 135.179 1.00 33.82 ?  402 GLU B CG    1 
ATOM   8811  C  CD    . GLU B 1 402 ? 117.979 161.008 135.567 1.00 39.10 ?  402 GLU B CD    1 
ATOM   8812  O  OE1   . GLU B 1 402 ? 117.579 161.494 136.646 1.00 35.36 ?  402 GLU B OE1   1 
ATOM   8813  O  OE2   . GLU B 1 402 ? 118.752 161.613 134.795 1.00 36.60 -1 402 GLU B OE2   1 
ATOM   8814  N  N     . ILE B 1 403 ? 120.879 158.265 138.325 1.00 29.66 ?  403 ILE B N     1 
ATOM   8815  C  CA    . ILE B 1 403 ? 121.528 157.450 139.345 1.00 24.05 ?  403 ILE B CA    1 
ATOM   8816  C  C     . ILE B 1 403 ? 120.548 157.220 140.488 1.00 25.63 ?  403 ILE B C     1 
ATOM   8817  O  O     . ILE B 1 403 ? 120.033 158.175 141.080 1.00 30.61 ?  403 ILE B O     1 
ATOM   8818  C  CB    . ILE B 1 403 ? 122.817 158.115 139.847 1.00 21.38 ?  403 ILE B CB    1 
ATOM   8819  C  CG1   . ILE B 1 403 ? 123.853 158.181 138.723 1.00 23.71 ?  403 ILE B CG1   1 
ATOM   8820  C  CG2   . ILE B 1 403 ? 123.372 157.366 141.043 1.00 20.95 ?  403 ILE B CG2   1 
ATOM   8821  C  CD1   . ILE B 1 403 ? 124.095 156.857 138.037 1.00 27.98 ?  403 ILE B CD1   1 
ATOM   8822  N  N     . GLY B 1 404 ? 120.294 155.957 140.798 1.00 22.24 ?  404 GLY B N     1 
ATOM   8823  C  CA    . GLY B 1 404 ? 119.416 155.576 141.885 1.00 10.85 ?  404 GLY B CA    1 
ATOM   8824  C  C     . GLY B 1 404 ? 120.171 155.310 143.167 1.00 19.17 ?  404 GLY B C     1 
ATOM   8825  O  O     . GLY B 1 404 ? 121.219 155.904 143.438 1.00 26.62 ?  404 GLY B O     1 
ATOM   8826  N  N     . LEU B 1 405 ? 119.632 154.399 143.971 1.00 23.93 ?  405 LEU B N     1 
ATOM   8827  C  CA    . LEU B 1 405 ? 120.221 154.028 145.250 1.00 10.66 ?  405 LEU B CA    1 
ATOM   8828  C  C     . LEU B 1 405 ? 120.522 152.536 145.241 1.00 13.07 ?  405 LEU B C     1 
ATOM   8829  O  O     . LEU B 1 405 ? 119.604 151.717 145.127 1.00 14.56 ?  405 LEU B O     1 
ATOM   8830  C  CB    . LEU B 1 405 ? 119.285 154.380 146.408 1.00 17.18 ?  405 LEU B CB    1 
ATOM   8831  C  CG    . LEU B 1 405 ? 118.906 155.853 146.559 1.00 17.59 ?  405 LEU B CG    1 
ATOM   8832  C  CD1   . LEU B 1 405 ? 117.713 156.002 147.484 1.00 20.83 ?  405 LEU B CD1   1 
ATOM   8833  C  CD2   . LEU B 1 405 ? 120.082 156.669 147.067 1.00 16.71 ?  405 LEU B CD2   1 
ATOM   8834  N  N     . ASP B 1 406 ? 121.799 152.188 145.363 1.00 24.08 ?  406 ASP B N     1 
ATOM   8835  C  CA    . ASP B 1 406 ? 122.234 150.802 145.467 1.00 17.26 ?  406 ASP B CA    1 
ATOM   8836  C  C     . ASP B 1 406 ? 122.751 150.552 146.876 1.00 18.11 ?  406 ASP B C     1 
ATOM   8837  O  O     . ASP B 1 406 ? 123.650 151.254 147.347 1.00 27.75 ?  406 ASP B O     1 
ATOM   8838  C  CB    . ASP B 1 406 ? 123.316 150.480 144.437 1.00 17.89 ?  406 ASP B CB    1 
ATOM   8839  C  CG    . ASP B 1 406 ? 122.742 150.072 143.095 1.00 29.59 ?  406 ASP B CG    1 
ATOM   8840  O  OD1   . ASP B 1 406 ? 121.527 149.788 143.025 1.00 31.46 ?  406 ASP B OD1   1 
ATOM   8841  O  OD2   . ASP B 1 406 ? 123.506 150.031 142.109 1.00 31.03 -1 406 ASP B OD2   1 
ATOM   8842  N  N     . ILE B 1 407 ? 122.193 149.536 147.534 1.00 18.55 ?  407 ILE B N     1 
ATOM   8843  C  CA    . ILE B 1 407 ? 122.426 149.341 148.957 1.00 14.68 ?  407 ILE B CA    1 
ATOM   8844  C  C     . ILE B 1 407 ? 123.886 148.990 149.224 1.00 15.53 ?  407 ILE B C     1 
ATOM   8845  O  O     . ILE B 1 407 ? 124.534 148.265 148.456 1.00 21.25 ?  407 ILE B O     1 
ATOM   8846  C  CB    . ILE B 1 407 ? 121.486 148.251 149.502 1.00 15.58 ?  407 ILE B CB    1 
ATOM   8847  C  CG1   . ILE B 1 407 ? 120.028 148.595 149.199 1.00 3.84  ?  407 ILE B CG1   1 
ATOM   8848  C  CG2   . ILE B 1 407 ? 121.686 148.068 150.983 1.00 13.32 ?  407 ILE B CG2   1 
ATOM   8849  C  CD1   . ILE B 1 407 ? 119.157 147.382 149.020 1.00 11.74 ?  407 ILE B CD1   1 
ATOM   8850  N  N     . SER B 1 408 ? 124.408 149.520 150.328 1.00 26.34 ?  408 SER B N     1 
ATOM   8851  C  CA    . SER B 1 408 ? 125.746 149.203 150.810 1.00 23.56 ?  408 SER B CA    1 
ATOM   8852  C  C     . SER B 1 408 ? 125.829 149.635 152.265 1.00 27.78 ?  408 SER B C     1 
ATOM   8853  O  O     . SER B 1 408 ? 125.529 150.789 152.583 1.00 38.28 ?  408 SER B O     1 
ATOM   8854  C  CB    . SER B 1 408 ? 126.819 149.910 149.975 1.00 29.16 ?  408 SER B CB    1 
ATOM   8855  O  OG    . SER B 1 408 ? 127.944 150.242 150.767 1.00 27.58 ?  408 SER B OG    1 
ATOM   8856  N  N     . CYS B 1 409 ? 126.219 148.715 153.143 1.00 23.83 ?  409 CYS B N     1 
ATOM   8857  C  CA    . CYS B 1 409 ? 126.356 149.021 154.559 1.00 30.39 ?  409 CYS B CA    1 
ATOM   8858  C  C     . CYS B 1 409 ? 127.645 148.415 155.096 1.00 28.90 ?  409 CYS B C     1 
ATOM   8859  O  O     . CYS B 1 409 ? 128.177 147.442 154.554 1.00 26.96 ?  409 CYS B O     1 
ATOM   8860  C  CB    . CYS B 1 409 ? 125.155 148.517 155.373 1.00 25.10 ?  409 CYS B CB    1 
ATOM   8861  S  SG    . CYS B 1 409 ? 125.135 146.741 155.689 1.00 45.46 ?  409 CYS B SG    1 
ATOM   8862  N  N     . ASN B 1 410 ? 128.140 149.013 156.174 1.00 22.93 ?  410 ASN B N     1 
ATOM   8863  C  CA    . ASN B 1 410 ? 129.365 148.580 156.831 1.00 20.91 ?  410 ASN B CA    1 
ATOM   8864  C  C     . ASN B 1 410 ? 129.010 147.678 158.002 1.00 25.91 ?  410 ASN B C     1 
ATOM   8865  O  O     . ASN B 1 410 ? 128.109 147.995 158.785 1.00 28.35 ?  410 ASN B O     1 
ATOM   8866  C  CB    . ASN B 1 410 ? 130.175 149.782 157.312 1.00 24.20 ?  410 ASN B CB    1 
ATOM   8867  C  CG    . ASN B 1 410 ? 129.935 151.010 156.469 1.00 32.33 ?  410 ASN B CG    1 
ATOM   8868  O  OD1   . ASN B 1 410 ? 129.328 151.976 156.925 1.00 34.43 ?  410 ASN B OD1   1 
ATOM   8869  N  ND2   . ASN B 1 410 ? 130.407 150.980 155.228 1.00 34.92 ?  410 ASN B ND2   1 
ATOM   8870  N  N     . LEU B 1 411 ? 129.716 146.562 158.119 1.00 19.65 ?  411 LEU B N     1 
ATOM   8871  C  CA    . LEU B 1 411 ? 129.411 145.550 159.117 1.00 10.94 ?  411 LEU B CA    1 
ATOM   8872  C  C     . LEU B 1 411 ? 130.296 145.716 160.346 1.00 11.69 ?  411 LEU B C     1 
ATOM   8873  O  O     . LEU B 1 411 ? 131.457 146.123 160.254 1.00 22.88 ?  411 LEU B O     1 
ATOM   8874  C  CB    . LEU B 1 411 ? 129.590 144.145 158.539 1.00 19.20 ?  411 LEU B CB    1 
ATOM   8875  C  CG    . LEU B 1 411 ? 128.438 143.503 157.765 1.00 17.67 ?  411 LEU B CG    1 
ATOM   8876  C  CD1   . LEU B 1 411 ? 128.146 144.241 156.472 1.00 18.06 ?  411 LEU B CD1   1 
ATOM   8877  C  CD2   . LEU B 1 411 ? 128.769 142.050 157.481 1.00 23.52 ?  411 LEU B CD2   1 
ATOM   8878  N  N     . GLY B 1 412 ? 129.723 145.403 161.501 1.00 17.26 ?  412 GLY B N     1 
ATOM   8879  C  CA    . GLY B 1 412 ? 130.444 145.377 162.757 1.00 11.56 ?  412 GLY B CA    1 
ATOM   8880  C  C     . GLY B 1 412 ? 129.647 144.596 163.777 1.00 10.58 ?  412 GLY B C     1 
ATOM   8881  O  O     . GLY B 1 412 ? 128.431 144.776 163.871 1.00 27.55 ?  412 GLY B O     1 
ATOM   8882  N  N     . SER B 1 413 ? 130.297 143.723 164.538 1.00 11.05 ?  413 SER B N     1 
ATOM   8883  C  CA    . SER B 1 413 ? 129.591 142.805 165.418 1.00 11.98 ?  413 SER B CA    1 
ATOM   8884  C  C     . SER B 1 413 ? 129.939 143.064 166.876 1.00 19.09 ?  413 SER B C     1 
ATOM   8885  O  O     . SER B 1 413 ? 131.109 143.236 167.227 1.00 20.96 ?  413 SER B O     1 
ATOM   8886  C  CB    . SER B 1 413 ? 129.917 141.354 165.064 1.00 13.26 ?  413 SER B CB    1 
ATOM   8887  O  OG    . SER B 1 413 ? 129.407 141.022 163.786 1.00 31.25 ?  413 SER B OG    1 
ATOM   8888  N  N     . LEU B 1 414 ? 128.919 143.077 167.723 1.00 20.36 ?  414 LEU B N     1 
ATOM   8889  C  CA    . LEU B 1 414 ? 129.120 143.087 169.161 1.00 13.08 ?  414 LEU B CA    1 
ATOM   8890  C  C     . LEU B 1 414 ? 129.360 141.667 169.645 1.00 21.50 ?  414 LEU B C     1 
ATOM   8891  O  O     . LEU B 1 414 ? 128.657 140.736 169.247 1.00 25.61 ?  414 LEU B O     1 
ATOM   8892  C  CB    . LEU B 1 414 ? 127.908 143.680 169.879 1.00 22.88 ?  414 LEU B CB    1 
ATOM   8893  C  CG    . LEU B 1 414 ? 127.362 145.011 169.372 1.00 21.75 ?  414 LEU B CG    1 
ATOM   8894  C  CD1   . LEU B 1 414 ? 126.087 145.355 170.112 1.00 22.36 ?  414 LEU B CD1   1 
ATOM   8895  C  CD2   . LEU B 1 414 ? 128.394 146.110 169.544 1.00 24.62 ?  414 LEU B CD2   1 
ATOM   8896  N  N     . ASN B 1 415 ? 130.363 141.502 170.500 1.00 29.80 ?  415 ASN B N     1 
ATOM   8897  C  CA    . ASN B 1 415 ? 130.584 140.226 171.169 1.00 27.12 ?  415 ASN B CA    1 
ATOM   8898  C  C     . ASN B 1 415 ? 129.710 140.202 172.414 1.00 25.14 ?  415 ASN B C     1 
ATOM   8899  O  O     . ASN B 1 415 ? 130.004 140.883 173.401 1.00 29.23 ?  415 ASN B O     1 
ATOM   8900  C  CB    . ASN B 1 415 ? 132.059 140.048 171.511 1.00 22.71 ?  415 ASN B CB    1 
ATOM   8901  C  CG    . ASN B 1 415 ? 132.411 138.619 171.869 1.00 28.99 ?  415 ASN B CG    1 
ATOM   8902  O  OD1   . ASN B 1 415 ? 131.685 137.951 172.602 1.00 34.87 ?  415 ASN B OD1   1 
ATOM   8903  N  ND2   . ASN B 1 415 ? 133.534 138.142 171.349 1.00 29.53 ?  415 ASN B ND2   1 
ATOM   8904  N  N     . ILE B 1 416 ? 128.631 139.417 172.366 1.00 20.40 ?  416 ILE B N     1 
ATOM   8905  C  CA    . ILE B 1 416 ? 127.615 139.470 173.414 1.00 23.03 ?  416 ILE B CA    1 
ATOM   8906  C  C     . ILE B 1 416 ? 128.207 139.082 174.762 1.00 30.00 ?  416 ILE B C     1 
ATOM   8907  O  O     . ILE B 1 416 ? 127.924 139.717 175.785 1.00 30.28 ?  416 ILE B O     1 
ATOM   8908  C  CB    . ILE B 1 416 ? 126.418 138.578 173.033 1.00 22.35 ?  416 ILE B CB    1 
ATOM   8909  C  CG1   . ILE B 1 416 ? 125.673 139.185 171.843 1.00 22.82 ?  416 ILE B CG1   1 
ATOM   8910  C  CG2   . ILE B 1 416 ? 125.479 138.408 174.210 1.00 17.29 ?  416 ILE B CG2   1 
ATOM   8911  C  CD1   . ILE B 1 416 ? 124.569 138.315 171.295 1.00 21.61 ?  416 ILE B CD1   1 
ATOM   8912  N  N     . LEU B 1 417 ? 129.046 138.045 174.786 1.00 24.98 ?  417 LEU B N     1 
ATOM   8913  C  CA    . LEU B 1 417 ? 129.652 137.613 176.041 1.00 27.55 ?  417 LEU B CA    1 
ATOM   8914  C  C     . LEU B 1 417 ? 130.526 138.707 176.639 1.00 28.75 ?  417 LEU B C     1 
ATOM   8915  O  O     . LEU B 1 417 ? 130.426 139.016 177.832 1.00 34.00 ?  417 LEU B O     1 
ATOM   8916  C  CB    . LEU B 1 417 ? 130.466 136.339 175.818 1.00 28.61 ?  417 LEU B CB    1 
ATOM   8917  C  CG    . LEU B 1 417 ? 131.094 135.726 177.070 1.00 29.91 ?  417 LEU B CG    1 
ATOM   8918  C  CD1   . LEU B 1 417 ? 130.570 134.323 177.290 1.00 27.31 ?  417 LEU B CD1   1 
ATOM   8919  C  CD2   . LEU B 1 417 ? 132.609 135.724 176.961 1.00 32.64 ?  417 LEU B CD2   1 
ATOM   8920  N  N     . ASN B 1 418 ? 131.384 139.318 175.819 1.00 34.08 ?  418 ASN B N     1 
ATOM   8921  C  CA    . ASN B 1 418 ? 132.275 140.354 176.326 1.00 29.41 ?  418 ASN B CA    1 
ATOM   8922  C  C     . ASN B 1 418 ? 131.524 141.641 176.639 1.00 29.20 ?  418 ASN B C     1 
ATOM   8923  O  O     . ASN B 1 418 ? 131.873 142.344 177.594 1.00 35.03 ?  418 ASN B O     1 
ATOM   8924  C  CB    . ASN B 1 418 ? 133.395 140.616 175.322 1.00 27.06 ?  418 ASN B CB    1 
ATOM   8925  C  CG    . ASN B 1 418 ? 134.347 139.446 175.200 1.00 28.65 ?  418 ASN B CG    1 
ATOM   8926  O  OD1   . ASN B 1 418 ? 134.686 138.803 176.193 1.00 36.71 ?  418 ASN B OD1   1 
ATOM   8927  N  ND2   . ASN B 1 418 ? 134.782 139.159 173.980 1.00 30.28 ?  418 ASN B ND2   1 
ATOM   8928  N  N     . VAL B 1 419 ? 130.501 141.970 175.848 1.00 31.16 ?  419 VAL B N     1 
ATOM   8929  C  CA    . VAL B 1 419 ? 129.716 143.173 176.108 1.00 31.46 ?  419 VAL B CA    1 
ATOM   8930  C  C     . VAL B 1 419 ? 128.965 143.049 177.428 1.00 29.36 ?  419 VAL B C     1 
ATOM   8931  O  O     . VAL B 1 419 ? 128.950 143.981 178.241 1.00 36.08 ?  419 VAL B O     1 
ATOM   8932  C  CB    . VAL B 1 419 ? 128.760 143.452 174.933 1.00 26.47 ?  419 VAL B CB    1 
ATOM   8933  C  CG1   . VAL B 1 419 ? 127.660 144.396 175.355 1.00 28.15 ?  419 VAL B CG1   1 
ATOM   8934  C  CG2   . VAL B 1 419 ? 129.525 144.035 173.762 1.00 25.84 ?  419 VAL B CG2   1 
ATOM   8935  N  N     . MET B 1 420 ? 128.339 141.895 177.671 1.00 31.99 ?  420 MET B N     1 
ATOM   8936  C  CA    . MET B 1 420 ? 127.577 141.724 178.902 1.00 34.66 ?  420 MET B CA    1 
ATOM   8937  C  C     . MET B 1 420 ? 128.474 141.490 180.111 1.00 33.26 ?  420 MET B C     1 
ATOM   8938  O  O     . MET B 1 420 ? 128.105 141.867 181.228 1.00 35.93 ?  420 MET B O     1 
ATOM   8939  C  CB    . MET B 1 420 ? 126.576 140.578 178.756 1.00 32.45 ?  420 MET B CB    1 
ATOM   8940  C  CG    . MET B 1 420 ? 125.516 140.829 177.701 1.00 30.51 ?  420 MET B CG    1 
ATOM   8941  S  SD    . MET B 1 420 ? 123.967 141.423 178.403 1.00 43.53 ?  420 MET B SD    1 
ATOM   8942  C  CE    . MET B 1 420 ? 123.805 140.376 179.843 1.00 31.04 ?  420 MET B CE    1 
ATOM   8943  N  N     . GLU B 1 421 ? 129.641 140.871 179.916 1.00 37.77 ?  421 GLU B N     1 
ATOM   8944  C  CA    . GLU B 1 421 ? 130.585 140.718 181.019 1.00 34.78 ?  421 GLU B CA    1 
ATOM   8945  C  C     . GLU B 1 421 ? 131.083 142.073 181.501 1.00 38.51 ?  421 GLU B C     1 
ATOM   8946  O  O     . GLU B 1 421 ? 131.230 142.299 182.708 1.00 41.72 ?  421 GLU B O     1 
ATOM   8947  C  CB    . GLU B 1 421 ? 131.752 139.831 180.588 1.00 34.46 ?  421 GLU B CB    1 
ATOM   8948  C  CG    . GLU B 1 421 ? 132.991 139.958 181.456 1.00 42.35 ?  421 GLU B CG    1 
ATOM   8949  C  CD    . GLU B 1 421 ? 134.267 140.022 180.641 1.00 44.83 ?  421 GLU B CD    1 
ATOM   8950  O  OE1   . GLU B 1 421 ? 134.182 139.942 179.397 1.00 43.17 ?  421 GLU B OE1   1 
ATOM   8951  O  OE2   . GLU B 1 421 ? 135.353 140.153 181.243 1.00 41.27 -1 421 GLU B OE2   1 
ATOM   8952  N  N     . HIS B 1 422 ? 131.336 142.993 180.573 1.00 34.24 ?  422 HIS B N     1 
ATOM   8953  C  CA    . HIS B 1 422 ? 131.763 144.342 180.917 1.00 35.44 ?  422 HIS B CA    1 
ATOM   8954  C  C     . HIS B 1 422 ? 130.599 145.256 181.278 1.00 38.64 ?  422 HIS B C     1 
ATOM   8955  O  O     . HIS B 1 422 ? 130.841 146.404 181.665 1.00 41.12 ?  422 HIS B O     1 
ATOM   8956  C  CB    . HIS B 1 422 ? 132.556 144.951 179.757 1.00 32.69 ?  422 HIS B CB    1 
ATOM   8957  C  CG    . HIS B 1 422 ? 133.882 144.296 179.524 1.00 35.81 ?  422 HIS B CG    1 
ATOM   8958  N  ND1   . HIS B 1 422 ? 134.037 143.204 178.698 1.00 36.57 ?  422 HIS B ND1   1 
ATOM   8959  C  CD2   . HIS B 1 422 ? 135.113 144.577 180.011 1.00 37.01 ?  422 HIS B CD2   1 
ATOM   8960  C  CE1   . HIS B 1 422 ? 135.307 142.841 178.686 1.00 39.80 ?  422 HIS B CE1   1 
ATOM   8961  N  NE2   . HIS B 1 422 ? 135.981 143.657 179.474 1.00 39.81 ?  422 HIS B NE2   1 
ATOM   8962  N  N     . LYS B 1 423 ? 129.359 144.776 181.164 1.00 40.97 ?  423 LYS B N     1 
ATOM   8963  C  CA    . LYS B 1 423 ? 128.167 145.565 181.482 1.00 42.37 ?  423 LYS B CA    1 
ATOM   8964  C  C     . LYS B 1 423 ? 128.163 146.885 180.717 1.00 43.69 ?  423 LYS B C     1 
ATOM   8965  O  O     . LYS B 1 423 ? 127.869 147.948 181.267 1.00 46.33 ?  423 LYS B O     1 
ATOM   8966  C  CB    . LYS B 1 423 ? 128.057 145.807 182.988 1.00 40.41 ?  423 LYS B CB    1 
ATOM   8967  C  CG    . LYS B 1 423 ? 127.570 144.607 183.779 1.00 42.43 ?  423 LYS B CG    1 
ATOM   8968  C  CD    . LYS B 1 423 ? 127.670 144.858 185.274 1.00 43.32 ?  423 LYS B CD    1 
ATOM   8969  C  CE    . LYS B 1 423 ? 128.852 144.116 185.880 1.00 45.85 ?  423 LYS B CE    1 
ATOM   8970  N  NZ    . LYS B 1 423 ? 128.424 143.128 186.908 1.00 43.92 1  423 LYS B NZ    1 
ATOM   8971  N  N     . SER B 1 424 ? 128.490 146.814 179.430 1.00 31.73 ?  424 SER B N     1 
ATOM   8972  C  CA    . SER B 1 424 ? 128.722 147.997 178.610 1.00 33.97 ?  424 SER B CA    1 
ATOM   8973  C  C     . SER B 1 424 ? 127.983 147.893 177.285 1.00 34.09 ?  424 SER B C     1 
ATOM   8974  O  O     . SER B 1 424 ? 128.550 148.117 176.215 1.00 32.55 ?  424 SER B O     1 
ATOM   8975  C  CB    . SER B 1 424 ? 130.214 148.196 178.371 1.00 35.65 ?  424 SER B CB    1 
ATOM   8976  O  OG    . SER B 1 424 ? 130.720 147.196 177.505 1.00 32.02 ?  424 SER B OG    1 
ATOM   8977  N  N     . ILE B 1 425 ? 126.697 147.542 177.335 1.00 33.46 ?  425 ILE B N     1 
ATOM   8978  C  CA    . ILE B 1 425 ? 125.895 147.525 176.114 1.00 26.93 ?  425 ILE B CA    1 
ATOM   8979  C  C     . ILE B 1 425 ? 125.842 148.918 175.500 1.00 32.03 ?  425 ILE B C     1 
ATOM   8980  O  O     . ILE B 1 425 ? 126.079 149.098 174.301 1.00 35.69 ?  425 ILE B O     1 
ATOM   8981  C  CB    . ILE B 1 425 ? 124.482 146.984 176.398 1.00 32.10 ?  425 ILE B CB    1 
ATOM   8982  C  CG1   . ILE B 1 425 ? 124.507 145.466 176.576 1.00 32.37 ?  425 ILE B CG1   1 
ATOM   8983  C  CG2   . ILE B 1 425 ? 123.530 147.357 175.273 1.00 27.48 ?  425 ILE B CG2   1 
ATOM   8984  C  CD1   . ILE B 1 425 ? 123.178 144.887 177.001 1.00 33.35 ?  425 ILE B CD1   1 
ATOM   8985  N  N     . GLU B 1 426 ? 125.556 149.927 176.325 1.00 27.69 ?  426 GLU B N     1 
ATOM   8986  C  CA    . GLU B 1 426 ? 125.396 151.285 175.814 1.00 23.51 ?  426 GLU B CA    1 
ATOM   8987  C  C     . GLU B 1 426 ? 126.688 151.805 175.198 1.00 26.23 ?  426 GLU B C     1 
ATOM   8988  O  O     . GLU B 1 426 ? 126.699 152.268 174.052 1.00 34.59 ?  426 GLU B O     1 
ATOM   8989  C  CB    . GLU B 1 426 ? 124.928 152.210 176.937 1.00 26.59 ?  426 GLU B CB    1 
ATOM   8990  C  CG    . GLU B 1 426 ? 125.102 153.686 176.631 1.00 29.01 ?  426 GLU B CG    1 
ATOM   8991  C  CD    . GLU B 1 426 ? 124.606 154.576 177.752 1.00 33.93 ?  426 GLU B CD    1 
ATOM   8992  O  OE1   . GLU B 1 426 ? 124.263 154.046 178.828 1.00 33.66 ?  426 GLU B OE1   1 
ATOM   8993  O  OE2   . GLU B 1 426 ? 124.560 155.809 177.556 1.00 36.80 -1 426 GLU B OE2   1 
ATOM   8994  N  N     . LYS B 1 427 ? 127.790 151.738 175.948 1.00 33.18 ?  427 LYS B N     1 
ATOM   8995  C  CA    . LYS B 1 427 ? 129.049 152.293 175.464 1.00 27.99 ?  427 LYS B CA    1 
ATOM   8996  C  C     . LYS B 1 427 ? 129.534 151.561 174.220 1.00 28.32 ?  427 LYS B C     1 
ATOM   8997  O  O     . LYS B 1 427 ? 129.970 152.192 173.249 1.00 32.78 ?  427 LYS B O     1 
ATOM   8998  C  CB    . LYS B 1 427 ? 130.104 152.242 176.568 1.00 28.87 ?  427 LYS B CB    1 
ATOM   8999  C  CG    . LYS B 1 427 ? 131.517 152.534 176.094 1.00 32.24 ?  427 LYS B CG    1 
ATOM   9000  C  CD    . LYS B 1 427 ? 132.536 152.287 177.194 1.00 33.02 ?  427 LYS B CD    1 
ATOM   9001  C  CE    . LYS B 1 427 ? 132.569 150.826 177.608 1.00 31.84 ?  427 LYS B CE    1 
ATOM   9002  N  NZ    . LYS B 1 427 ? 132.512 149.908 176.438 1.00 33.99 1  427 LYS B NZ    1 
ATOM   9003  N  N     . THR B 1 428 ? 129.455 150.228 174.227 1.00 30.09 ?  428 THR B N     1 
ATOM   9004  C  CA    . THR B 1 428 ? 129.894 149.459 173.069 1.00 24.75 ?  428 THR B CA    1 
ATOM   9005  C  C     . THR B 1 428 ? 129.039 149.764 171.849 1.00 24.98 ?  428 THR B C     1 
ATOM   9006  O  O     . THR B 1 428 ? 129.566 149.929 170.744 1.00 32.34 ?  428 THR B O     1 
ATOM   9007  C  CB    . THR B 1 428 ? 129.862 147.964 173.378 1.00 24.64 ?  428 THR B CB    1 
ATOM   9008  O  OG1   . THR B 1 428 ? 130.507 147.720 174.633 1.00 26.31 ?  428 THR B OG1   1 
ATOM   9009  C  CG2   . THR B 1 428 ? 130.576 147.187 172.288 1.00 25.22 ?  428 THR B CG2   1 
ATOM   9010  N  N     . VAL B 1 429 ? 127.718 149.848 172.027 1.00 23.05 ?  429 VAL B N     1 
ATOM   9011  C  CA    . VAL B 1 429 ? 126.839 150.128 170.896 1.00 22.40 ?  429 VAL B CA    1 
ATOM   9012  C  C     . VAL B 1 429 ? 127.131 151.507 170.320 1.00 27.00 ?  429 VAL B C     1 
ATOM   9013  O  O     . VAL B 1 429 ? 127.225 151.675 169.098 1.00 28.05 ?  429 VAL B O     1 
ATOM   9014  C  CB    . VAL B 1 429 ? 125.363 149.985 171.311 1.00 25.19 ?  429 VAL B CB    1 
ATOM   9015  C  CG1   . VAL B 1 429 ? 124.464 150.663 170.297 1.00 22.74 ?  429 VAL B CG1   1 
ATOM   9016  C  CG2   . VAL B 1 429 ? 124.988 148.522 171.431 1.00 26.03 ?  429 VAL B CG2   1 
ATOM   9017  N  N     . LYS B 1 430 ? 127.286 152.515 171.183 1.00 25.79 ?  430 LYS B N     1 
ATOM   9018  C  CA    . LYS B 1 430 ? 127.540 153.865 170.685 1.00 20.82 ?  430 LYS B CA    1 
ATOM   9019  C  C     . LYS B 1 430 ? 128.892 153.960 169.985 1.00 23.73 ?  430 LYS B C     1 
ATOM   9020  O  O     . LYS B 1 430 ? 129.000 154.579 168.919 1.00 30.67 ?  430 LYS B O     1 
ATOM   9021  C  CB    . LYS B 1 430 ? 127.449 154.877 171.827 1.00 23.66 ?  430 LYS B CB    1 
ATOM   9022  C  CG    . LYS B 1 430 ? 126.131 154.838 172.580 1.00 25.85 ?  430 LYS B CG    1 
ATOM   9023  C  CD    . LYS B 1 430 ? 125.404 156.165 172.538 1.00 27.12 ?  430 LYS B CD    1 
ATOM   9024  C  CE    . LYS B 1 430 ? 124.262 156.188 173.538 1.00 29.17 ?  430 LYS B CE    1 
ATOM   9025  N  NZ    . LYS B 1 430 ? 123.745 157.564 173.765 1.00 32.65 1  430 LYS B NZ    1 
ATOM   9026  N  N     . LEU B 1 431 ? 129.931 153.347 170.557 1.00 25.57 ?  431 LEU B N     1 
ATOM   9027  C  CA    . LEU B 1 431 ? 131.245 153.393 169.923 1.00 21.63 ?  431 LEU B CA    1 
ATOM   9028  C  C     . LEU B 1 431 ? 131.254 152.632 168.603 1.00 24.56 ?  431 LEU B C     1 
ATOM   9029  O  O     . LEU B 1 431 ? 131.885 153.069 167.633 1.00 28.94 ?  431 LEU B O     1 
ATOM   9030  C  CB    . LEU B 1 431 ? 132.303 152.841 170.874 1.00 26.72 ?  431 LEU B CB    1 
ATOM   9031  C  CG    . LEU B 1 431 ? 132.991 153.857 171.783 1.00 29.74 ?  431 LEU B CG    1 
ATOM   9032  C  CD1   . LEU B 1 431 ? 133.878 153.150 172.792 1.00 27.85 ?  431 LEU B CD1   1 
ATOM   9033  C  CD2   . LEU B 1 431 ? 133.793 154.853 170.962 1.00 28.68 ?  431 LEU B CD2   1 
ATOM   9034  N  N     . ALA B 1 432 ? 130.562 151.491 168.544 1.00 26.78 ?  432 ALA B N     1 
ATOM   9035  C  CA    . ALA B 1 432 ? 130.465 150.745 167.295 1.00 15.82 ?  432 ALA B CA    1 
ATOM   9036  C  C     . ALA B 1 432 ? 129.700 151.533 166.242 1.00 25.44 ?  432 ALA B C     1 
ATOM   9037  O  O     . ALA B 1 432 ? 130.061 151.514 165.060 1.00 27.92 ?  432 ALA B O     1 
ATOM   9038  C  CB    . ALA B 1 432 ? 129.795 149.396 167.546 1.00 17.76 ?  432 ALA B CB    1 
ATOM   9039  N  N     . THR B 1 433 ? 128.636 152.227 166.651 1.00 25.72 ?  433 THR B N     1 
ATOM   9040  C  CA    . THR B 1 433 ? 127.903 153.074 165.718 1.00 19.97 ?  433 THR B CA    1 
ATOM   9041  C  C     . THR B 1 433 ? 128.789 154.191 165.186 1.00 23.21 ?  433 THR B C     1 
ATOM   9042  O  O     . THR B 1 433 ? 128.753 154.505 163.992 1.00 32.64 ?  433 THR B O     1 
ATOM   9043  C  CB    . THR B 1 433 ? 126.661 153.651 166.401 1.00 22.90 ?  433 THR B CB    1 
ATOM   9044  O  OG1   . THR B 1 433 ? 125.848 152.581 166.897 1.00 31.80 ?  433 THR B OG1   1 
ATOM   9045  C  CG2   . THR B 1 433 ? 125.847 154.484 165.422 1.00 22.05 ?  433 THR B CG2   1 
ATOM   9046  N  N     . ASP B 1 434 ? 129.600 154.795 166.057 1.00 23.10 ?  434 ASP B N     1 
ATOM   9047  C  CA    . ASP B 1 434 ? 130.525 155.832 165.608 1.00 23.64 ?  434 ASP B CA    1 
ATOM   9048  C  C     . ASP B 1 434 ? 131.555 155.277 164.631 1.00 20.53 ?  434 ASP B C     1 
ATOM   9049  O  O     . ASP B 1 434 ? 131.871 155.915 163.620 1.00 25.07 ?  434 ASP B O     1 
ATOM   9050  C  CB    . ASP B 1 434 ? 131.216 156.473 166.810 1.00 26.42 ?  434 ASP B CB    1 
ATOM   9051  C  CG    . ASP B 1 434 ? 130.260 157.256 167.680 1.00 32.91 ?  434 ASP B CG    1 
ATOM   9052  O  OD1   . ASP B 1 434 ? 129.319 157.863 167.128 1.00 34.35 ?  434 ASP B OD1   1 
ATOM   9053  O  OD2   . ASP B 1 434 ? 130.446 157.265 168.914 1.00 33.39 -1 434 ASP B OD2   1 
ATOM   9054  N  N     . SER B 1 435 ? 132.095 154.091 164.920 1.00 23.60 ?  435 SER B N     1 
ATOM   9055  C  CA    . SER B 1 435 ? 133.077 153.487 164.025 1.00 18.43 ?  435 SER B CA    1 
ATOM   9056  C  C     . SER B 1 435 ? 132.465 153.153 162.668 1.00 22.69 ?  435 SER B C     1 
ATOM   9057  O  O     . SER B 1 435 ? 133.092 153.376 161.625 1.00 32.06 ?  435 SER B O     1 
ATOM   9058  C  CB    . SER B 1 435 ? 133.671 152.234 164.667 1.00 22.49 ?  435 SER B CB    1 
ATOM   9059  O  OG    . SER B 1 435 ? 132.739 151.168 164.663 1.00 23.75 ?  435 SER B OG    1 
ATOM   9060  N  N     . LEU B 1 436 ? 131.241 152.625 162.660 1.00 21.95 ?  436 LEU B N     1 
ATOM   9061  C  CA    . LEU B 1 436 ? 130.579 152.310 161.397 1.00 13.09 ?  436 LEU B CA    1 
ATOM   9062  C  C     . LEU B 1 436 ? 130.232 153.578 160.627 1.00 18.56 ?  436 LEU B C     1 
ATOM   9063  O  O     . LEU B 1 436 ? 130.308 153.602 159.393 1.00 23.01 ?  436 LEU B O     1 
ATOM   9064  C  CB    . LEU B 1 436 ? 129.330 151.471 161.658 1.00 22.43 ?  436 LEU B CB    1 
ATOM   9065  C  CG    . LEU B 1 436 ? 129.577 150.075 162.234 1.00 21.08 ?  436 LEU B CG    1 
ATOM   9066  C  CD1   . LEU B 1 436 ? 128.298 149.491 162.807 1.00 18.38 ?  436 LEU B CD1   1 
ATOM   9067  C  CD2   . LEU B 1 436 ? 130.165 149.158 161.179 1.00 18.57 ?  436 LEU B CD2   1 
ATOM   9068  N  N     . THR B 1 437 ? 129.854 154.641 161.338 1.00 21.16 ?  437 THR B N     1 
ATOM   9069  C  CA    . THR B 1 437 ? 129.621 155.925 160.687 1.00 20.15 ?  437 THR B CA    1 
ATOM   9070  C  C     . THR B 1 437 ? 130.898 156.449 160.046 1.00 22.83 ?  437 THR B C     1 
ATOM   9071  O  O     . THR B 1 437 ? 130.872 156.974 158.928 1.00 29.74 ?  437 THR B O     1 
ATOM   9072  C  CB    . THR B 1 437 ? 129.078 156.933 161.700 1.00 20.41 ?  437 THR B CB    1 
ATOM   9073  O  OG1   . THR B 1 437 ? 127.933 156.379 162.357 1.00 23.40 ?  437 THR B OG1   1 
ATOM   9074  C  CG2   . THR B 1 437 ? 128.687 158.224 161.012 1.00 20.77 ?  437 THR B CG2   1 
ATOM   9075  N  N     . HIS B 1 438 ? 132.028 156.314 160.742 1.00 21.30 ?  438 HIS B N     1 
ATOM   9076  C  CA    . HIS B 1 438 ? 133.305 156.719 160.163 1.00 21.63 ?  438 HIS B CA    1 
ATOM   9077  C  C     . HIS B 1 438 ? 133.636 155.893 158.926 1.00 23.01 ?  438 HIS B C     1 
ATOM   9078  O  O     . HIS B 1 438 ? 134.098 156.435 157.913 1.00 32.46 ?  438 HIS B O     1 
ATOM   9079  C  CB    . HIS B 1 438 ? 134.416 156.594 161.205 1.00 26.49 ?  438 HIS B CB    1 
ATOM   9080  C  CG    . HIS B 1 438 ? 135.781 156.891 160.667 1.00 27.67 ?  438 HIS B CG    1 
ATOM   9081  N  ND1   . HIS B 1 438 ? 136.251 158.176 160.503 1.00 25.54 ?  438 HIS B ND1   1 
ATOM   9082  C  CD2   . HIS B 1 438 ? 136.772 156.071 160.248 1.00 28.00 ?  438 HIS B CD2   1 
ATOM   9083  C  CE1   . HIS B 1 438 ? 137.477 158.134 160.012 1.00 30.66 ?  438 HIS B CE1   1 
ATOM   9084  N  NE2   . HIS B 1 438 ? 137.816 156.868 159.847 1.00 31.16 ?  438 HIS B NE2   1 
ATOM   9085  N  N     . VAL B 1 439 ? 133.405 154.580 158.989 1.00 21.40 ?  439 VAL B N     1 
ATOM   9086  C  CA    . VAL B 1 439 ? 133.689 153.719 157.842 1.00 19.11 ?  439 VAL B CA    1 
ATOM   9087  C  C     . VAL B 1 439 ? 132.829 154.119 156.651 1.00 28.84 ?  439 VAL B C     1 
ATOM   9088  O  O     . VAL B 1 439 ? 133.300 154.149 155.508 1.00 32.53 ?  439 VAL B O     1 
ATOM   9089  C  CB    . VAL B 1 439 ? 133.486 152.240 158.217 1.00 23.77 ?  439 VAL B CB    1 
ATOM   9090  C  CG1   . VAL B 1 439 ? 133.547 151.360 156.977 1.00 20.70 ?  439 VAL B CG1   1 
ATOM   9091  C  CG2   . VAL B 1 439 ? 134.531 151.805 159.220 1.00 21.77 ?  439 VAL B CG2   1 
ATOM   9092  N  N     . SER B 1 440 ? 131.556 154.434 156.898 1.00 24.41 ?  440 SER B N     1 
ATOM   9093  C  CA    . SER B 1 440 ? 130.689 154.908 155.824 1.00 20.03 ?  440 SER B CA    1 
ATOM   9094  C  C     . SER B 1 440 ? 131.181 156.237 155.263 1.00 25.90 ?  440 SER B C     1 
ATOM   9095  O  O     . SER B 1 440 ? 131.186 156.442 154.044 1.00 31.54 ?  440 SER B O     1 
ATOM   9096  C  CB    . SER B 1 440 ? 129.252 155.038 156.327 1.00 22.41 ?  440 SER B CB    1 
ATOM   9097  O  OG    . SER B 1 440 ? 128.356 155.288 155.258 1.00 31.27 ?  440 SER B OG    1 
ATOM   9098  N  N     . GLU B 1 441 ? 131.596 157.154 156.140 1.00 26.70 ?  441 GLU B N     1 
ATOM   9099  C  CA    . GLU B 1 441 ? 132.002 158.485 155.696 1.00 24.82 ?  441 GLU B CA    1 
ATOM   9100  C  C     . GLU B 1 441 ? 133.269 158.437 154.851 1.00 32.63 ?  441 GLU B C     1 
ATOM   9101  O  O     . GLU B 1 441 ? 133.380 159.157 153.853 1.00 40.05 ?  441 GLU B O     1 
ATOM   9102  C  CB    . GLU B 1 441 ? 132.196 159.402 156.901 1.00 27.11 ?  441 GLU B CB    1 
ATOM   9103  C  CG    . GLU B 1 441 ? 130.904 160.006 157.424 1.00 27.69 ?  441 GLU B CG    1 
ATOM   9104  C  CD    . GLU B 1 441 ? 130.966 160.333 158.902 1.00 35.39 ?  441 GLU B CD    1 
ATOM   9105  O  OE1   . GLU B 1 441 ? 131.999 160.038 159.539 1.00 37.20 ?  441 GLU B OE1   1 
ATOM   9106  O  OE2   . GLU B 1 441 ? 129.977 160.884 159.428 1.00 36.45 -1 441 GLU B OE2   1 
ATOM   9107  N  N     . THR B 1 442 ? 134.235 157.600 155.227 1.00 31.61 ?  442 THR B N     1 
ATOM   9108  C  CA    . THR B 1 442 ? 135.478 157.501 154.473 1.00 30.94 ?  442 THR B CA    1 
ATOM   9109  C  C     . THR B 1 442 ? 135.390 156.545 153.290 1.00 29.64 ?  442 THR B C     1 
ATOM   9110  O  O     . THR B 1 442 ? 136.392 156.349 152.597 1.00 34.42 ?  442 THR B O     1 
ATOM   9111  C  CB    . THR B 1 442 ? 136.636 157.076 155.385 1.00 29.54 ?  442 THR B CB    1 
ATOM   9112  O  OG1   . THR B 1 442 ? 136.596 155.659 155.595 1.00 31.14 ?  442 THR B OG1   1 
ATOM   9113  C  CG2   . THR B 1 442 ? 136.576 157.807 156.711 1.00 31.60 ?  442 THR B CG2   1 
ATOM   9114  N  N     . THR B 1 443 ? 134.227 155.949 153.042 1.00 30.24 ?  443 THR B N     1 
ATOM   9115  C  CA    . THR B 1 443 ? 134.034 155.094 151.880 1.00 34.71 ?  443 THR B CA    1 
ATOM   9116  C  C     . THR B 1 443 ? 133.611 155.940 150.687 1.00 35.60 ?  443 THR B C     1 
ATOM   9117  O  O     . THR B 1 443 ? 132.622 156.675 150.757 1.00 36.53 ?  443 THR B O     1 
ATOM   9118  C  CB    . THR B 1 443 ? 132.984 154.019 152.161 1.00 33.90 ?  443 THR B CB    1 
ATOM   9119  O  OG1   . THR B 1 443 ? 133.498 153.084 153.117 1.00 39.26 ?  443 THR B OG1   1 
ATOM   9120  C  CG2   . THR B 1 443 ? 132.627 153.282 150.880 1.00 27.95 ?  443 THR B CG2   1 
ATOM   9121  N  N     . ASP B 1 444 ? 134.365 155.833 149.594 1.00 39.02 ?  444 ASP B N     1 
ATOM   9122  C  CA    . ASP B 1 444 ? 134.059 156.546 148.357 1.00 38.94 ?  444 ASP B CA    1 
ATOM   9123  C  C     . ASP B 1 444 ? 134.428 155.637 147.193 1.00 39.94 ?  444 ASP B C     1 
ATOM   9124  O  O     . ASP B 1 444 ? 135.614 155.435 146.913 1.00 40.16 ?  444 ASP B O     1 
ATOM   9125  C  CB    . ASP B 1 444 ? 134.813 157.874 148.278 1.00 41.00 ?  444 ASP B CB    1 
ATOM   9126  C  CG    . ASP B 1 444 ? 134.072 158.916 147.465 1.00 46.45 ?  444 ASP B CG    1 
ATOM   9127  O  OD1   . ASP B 1 444 ? 132.929 159.259 147.833 1.00 44.63 ?  444 ASP B OD1   1 
ATOM   9128  O  OD2   . ASP B 1 444 ? 134.635 159.397 146.458 1.00 43.46 -1 444 ASP B OD2   1 
ATOM   9129  N  N     . ILE B 1 445 ? 133.421 155.092 146.520 1.00 37.64 ?  445 ILE B N     1 
ATOM   9130  C  CA    . ILE B 1 445 ? 133.618 154.160 145.417 1.00 36.46 ?  445 ILE B CA    1 
ATOM   9131  C  C     . ILE B 1 445 ? 133.392 154.913 144.114 1.00 37.15 ?  445 ILE B C     1 
ATOM   9132  O  O     . ILE B 1 445 ? 132.300 155.440 143.872 1.00 42.66 ?  445 ILE B O     1 
ATOM   9133  C  CB    . ILE B 1 445 ? 132.680 152.950 145.534 1.00 32.65 ?  445 ILE B CB    1 
ATOM   9134  C  CG1   . ILE B 1 445 ? 133.140 152.045 146.675 1.00 33.55 ?  445 ILE B CG1   1 
ATOM   9135  C  CG2   . ILE B 1 445 ? 132.650 152.173 144.229 1.00 35.35 ?  445 ILE B CG2   1 
ATOM   9136  C  CD1   . ILE B 1 445 ? 132.072 151.118 147.177 1.00 35.02 ?  445 ILE B CD1   1 
ATOM   9137  N  N     . ARG B 1 446 ? 134.422 154.959 143.274 1.00 36.82 ?  446 ARG B N     1 
ATOM   9138  C  CA    . ARG B 1 446 ? 134.423 155.805 142.089 1.00 39.43 ?  446 ARG B CA    1 
ATOM   9139  C  C     . ARG B 1 446 ? 133.904 155.102 140.841 1.00 40.16 ?  446 ARG B C     1 
ATOM   9140  O  O     . ARG B 1 446 ? 133.842 155.730 139.780 1.00 37.10 ?  446 ARG B O     1 
ATOM   9141  C  CB    . ARG B 1 446 ? 135.838 156.334 141.828 1.00 37.35 ?  446 ARG B CB    1 
ATOM   9142  C  CG    . ARG B 1 446 ? 136.693 156.436 143.081 1.00 37.48 ?  446 ARG B CG    1 
ATOM   9143  C  CD    . ARG B 1 446 ? 136.357 157.676 143.894 1.00 39.79 ?  446 ARG B CD    1 
ATOM   9144  N  NE    . ARG B 1 446 ? 136.187 158.858 143.060 1.00 40.67 ?  446 ARG B NE    1 
ATOM   9145  C  CZ    . ARG B 1 446 ? 136.278 160.105 143.503 1.00 40.52 ?  446 ARG B CZ    1 
ATOM   9146  N  NH1   . ARG B 1 446 ? 136.535 160.369 144.774 1.00 37.72 1  446 ARG B NH1   1 
ATOM   9147  N  NH2   . ARG B 1 446 ? 136.103 161.112 142.651 1.00 39.59 ?  446 ARG B NH2   1 
ATOM   9148  N  N     . ASN B 1 447 ? 133.525 153.827 140.936 1.00 33.35 ?  447 ASN B N     1 
ATOM   9149  C  CA    . ASN B 1 447 ? 133.022 153.089 139.788 1.00 25.93 ?  447 ASN B CA    1 
ATOM   9150  C  C     . ASN B 1 447 ? 131.614 152.550 139.988 1.00 30.51 ?  447 ASN B C     1 
ATOM   9151  O  O     . ASN B 1 447 ? 131.063 151.942 139.063 1.00 37.20 ?  447 ASN B O     1 
ATOM   9152  C  CB    . ASN B 1 447 ? 133.968 151.932 139.441 1.00 31.43 ?  447 ASN B CB    1 
ATOM   9153  C  CG    . ASN B 1 447 ? 135.017 152.328 138.426 1.00 30.80 ?  447 ASN B CG    1 
ATOM   9154  O  OD1   . ASN B 1 447 ? 134.696 152.680 137.293 1.00 34.38 ?  447 ASN B OD1   1 
ATOM   9155  N  ND2   . ASN B 1 447 ? 136.280 152.275 138.828 1.00 29.87 ?  447 ASN B ND2   1 
ATOM   9156  N  N     . ALA B 1 448 ? 131.018 152.751 141.162 1.00 31.55 ?  448 ALA B N     1 
ATOM   9157  C  CA    . ALA B 1 448 ? 129.626 152.394 141.431 1.00 26.92 ?  448 ALA B CA    1 
ATOM   9158  C  C     . ALA B 1 448 ? 128.902 153.671 141.833 1.00 27.73 ?  448 ALA B C     1 
ATOM   9159  O  O     . ALA B 1 448 ? 128.953 154.082 143.003 1.00 29.36 ?  448 ALA B O     1 
ATOM   9160  C  CB    . ALA B 1 448 ? 129.525 151.325 142.515 1.00 26.31 ?  448 ALA B CB    1 
ATOM   9161  N  N     . PRO B 1 449 ? 128.224 154.337 140.895 1.00 27.20 ?  449 PRO B N     1 
ATOM   9162  C  CA    . PRO B 1 449 ? 127.619 155.636 141.231 1.00 24.21 ?  449 PRO B CA    1 
ATOM   9163  C  C     . PRO B 1 449 ? 126.428 155.514 142.160 1.00 24.86 ?  449 PRO B C     1 
ATOM   9164  O  O     . PRO B 1 449 ? 126.281 156.326 143.082 1.00 21.81 ?  449 PRO B O     1 
ATOM   9165  C  CB    . PRO B 1 449 ? 127.211 156.203 139.862 1.00 21.18 ?  449 PRO B CB    1 
ATOM   9166  C  CG    . PRO B 1 449 ? 127.749 155.245 138.836 1.00 25.67 ?  449 PRO B CG    1 
ATOM   9167  C  CD    . PRO B 1 449 ? 127.948 153.938 139.508 1.00 25.18 ?  449 PRO B CD    1 
ATOM   9168  N  N     . ALA B 1 450 ? 125.563 154.524 141.936 1.00 28.94 ?  450 ALA B N     1 
ATOM   9169  C  CA    . ALA B 1 450 ? 124.413 154.338 142.813 1.00 19.52 ?  450 ALA B CA    1 
ATOM   9170  C  C     . ALA B 1 450 ? 124.851 153.930 144.212 1.00 23.03 ?  450 ALA B C     1 
ATOM   9171  O  O     . ALA B 1 450 ? 124.265 154.376 145.204 1.00 24.84 ?  450 ALA B O     1 
ATOM   9172  C  CB    . ALA B 1 450 ? 123.460 153.306 142.216 1.00 19.72 ?  450 ALA B CB    1 
ATOM   9173  N  N     . VAL B 1 451 ? 125.885 153.093 144.314 1.00 26.08 ?  451 VAL B N     1 
ATOM   9174  C  CA    . VAL B 1 451 ? 126.415 152.719 145.622 1.00 19.47 ?  451 VAL B CA    1 
ATOM   9175  C  C     . VAL B 1 451 ? 126.966 153.942 146.343 1.00 19.53 ?  451 VAL B C     1 
ATOM   9176  O  O     . VAL B 1 451 ? 126.729 154.133 147.540 1.00 26.05 ?  451 VAL B O     1 
ATOM   9177  C  CB    . VAL B 1 451 ? 127.484 151.619 145.477 1.00 22.52 ?  451 VAL B CB    1 
ATOM   9178  C  CG1   . VAL B 1 451 ? 128.196 151.385 146.799 1.00 25.41 ?  451 VAL B CG1   1 
ATOM   9179  C  CG2   . VAL B 1 451 ? 126.857 150.330 144.979 1.00 19.90 ?  451 VAL B CG2   1 
ATOM   9180  N  N     . ARG B 1 452 ? 127.708 154.790 145.628 1.00 21.20 ?  452 ARG B N     1 
ATOM   9181  C  CA    . ARG B 1 452 ? 128.260 155.995 146.240 1.00 23.42 ?  452 ARG B CA    1 
ATOM   9182  C  C     . ARG B 1 452 ? 127.152 156.930 146.710 1.00 24.60 ?  452 ARG B C     1 
ATOM   9183  O  O     . ARG B 1 452 ? 127.197 157.455 147.832 1.00 30.17 ?  452 ARG B O     1 
ATOM   9184  C  CB    . ARG B 1 452 ? 129.180 156.707 145.247 1.00 20.90 ?  452 ARG B CB    1 
ATOM   9185  C  CG    . ARG B 1 452 ? 129.660 158.066 145.719 1.00 24.84 ?  452 ARG B CG    1 
ATOM   9186  C  CD    . ARG B 1 452 ? 131.070 158.356 145.239 1.00 27.79 ?  452 ARG B CD    1 
ATOM   9187  N  NE    . ARG B 1 452 ? 131.073 159.248 144.087 1.00 33.94 ?  452 ARG B NE    1 
ATOM   9188  C  CZ    . ARG B 1 452 ? 132.078 159.360 143.229 1.00 38.90 ?  452 ARG B CZ    1 
ATOM   9189  N  NH1   . ARG B 1 452 ? 133.184 158.648 143.364 1.00 31.79 1  452 ARG B NH1   1 
ATOM   9190  N  NH2   . ARG B 1 452 ? 131.971 160.209 142.212 1.00 34.38 ?  452 ARG B NH2   1 
ATOM   9191  N  N     . ARG B 1 453 ? 126.143 157.146 145.864 1.00 22.40 ?  453 ARG B N     1 
ATOM   9192  C  CA    . ARG B 1 453 ? 125.048 158.039 146.229 1.00 20.83 ?  453 ARG B CA    1 
ATOM   9193  C  C     . ARG B 1 453 ? 124.265 157.494 147.417 1.00 23.25 ?  453 ARG B C     1 
ATOM   9194  O  O     . ARG B 1 453 ? 123.888 158.250 148.319 1.00 25.88 ?  453 ARG B O     1 
ATOM   9195  C  CB    . ARG B 1 453 ? 124.130 158.258 145.026 1.00 20.64 ?  453 ARG B CB    1 
ATOM   9196  C  CG    . ARG B 1 453 ? 122.765 158.821 145.373 1.00 20.05 ?  453 ARG B CG    1 
ATOM   9197  C  CD    . ARG B 1 453 ? 122.083 159.413 144.153 1.00 20.46 ?  453 ARG B CD    1 
ATOM   9198  N  NE    . ARG B 1 453 ? 120.745 158.871 143.962 1.00 22.82 ?  453 ARG B NE    1 
ATOM   9199  C  CZ    . ARG B 1 453 ? 119.654 159.348 144.545 1.00 26.10 ?  453 ARG B CZ    1 
ATOM   9200  N  NH1   . ARG B 1 453 ? 119.705 160.383 145.367 1.00 28.13 1  453 ARG B NH1   1 
ATOM   9201  N  NH2   . ARG B 1 453 ? 118.481 158.770 144.299 1.00 25.07 ?  453 ARG B NH2   1 
ATOM   9202  N  N     . ALA B 1 454 ? 124.015 156.182 147.439 1.00 23.91 ?  454 ALA B N     1 
ATOM   9203  C  CA    . ALA B 1 454 ? 123.292 155.586 148.556 1.00 17.46 ?  454 ALA B CA    1 
ATOM   9204  C  C     . ALA B 1 454 ? 124.110 155.634 149.839 1.00 21.92 ?  454 ALA B C     1 
ATOM   9205  O  O     . ALA B 1 454 ? 123.555 155.833 150.922 1.00 24.78 ?  454 ALA B O     1 
ATOM   9206  C  CB    . ALA B 1 454 ? 122.901 154.149 148.219 1.00 19.55 ?  454 ALA B CB    1 
ATOM   9207  N  N     . ASN B 1 455 ? 125.426 155.442 149.747 1.00 23.90 ?  455 ASN B N     1 
ATOM   9208  C  CA    . ASN B 1 455 ? 126.268 155.574 150.930 1.00 20.72 ?  455 ASN B CA    1 
ATOM   9209  C  C     . ASN B 1 455 ? 126.234 156.999 151.464 1.00 26.36 ?  455 ASN B C     1 
ATOM   9210  O  O     . ASN B 1 455 ? 126.179 157.215 152.680 1.00 30.59 ?  455 ASN B O     1 
ATOM   9211  C  CB    . ASN B 1 455 ? 127.701 155.154 150.606 1.00 20.52 ?  455 ASN B CB    1 
ATOM   9212  C  CG    . ASN B 1 455 ? 128.581 155.097 151.836 1.00 24.75 ?  455 ASN B CG    1 
ATOM   9213  O  OD1   . ASN B 1 455 ? 128.472 154.181 152.648 1.00 30.97 ?  455 ASN B OD1   1 
ATOM   9214  N  ND2   . ASN B 1 455 ? 129.458 156.082 151.982 1.00 27.07 ?  455 ASN B ND2   1 
ATOM   9215  N  N     . LYS B 1 456 ? 126.264 157.986 150.566 1.00 27.25 ?  456 LYS B N     1 
ATOM   9216  C  CA    . LYS B 1 456 ? 126.251 159.378 150.999 1.00 25.06 ?  456 LYS B CA    1 
ATOM   9217  C  C     . LYS B 1 456 ? 124.898 159.791 151.566 1.00 23.96 ?  456 LYS B C     1 
ATOM   9218  O  O     . LYS B 1 456 ? 124.841 160.618 152.482 1.00 32.65 ?  456 LYS B O     1 
ATOM   9219  C  CB    . LYS B 1 456 ? 126.636 160.292 149.835 1.00 26.81 ?  456 LYS B CB    1 
ATOM   9220  C  CG    . LYS B 1 456 ? 127.747 161.275 150.155 1.00 30.51 ?  456 LYS B CG    1 
ATOM   9221  C  CD    . LYS B 1 456 ? 128.271 161.946 148.896 1.00 33.74 ?  456 LYS B CD    1 
ATOM   9222  C  CE    . LYS B 1 456 ? 128.789 160.923 147.899 1.00 33.23 ?  456 LYS B CE    1 
ATOM   9223  N  NZ    . LYS B 1 456 ? 130.065 160.300 148.347 1.00 28.20 1  456 LYS B NZ    1 
ATOM   9224  N  N     . ALA B 1 457 ? 123.805 159.237 151.041 1.00 24.59 ?  457 ALA B N     1 
ATOM   9225  C  CA    . ALA B 1 457 ? 122.465 159.677 151.421 1.00 18.66 ?  457 ALA B CA    1 
ATOM   9226  C  C     . ALA B 1 457 ? 121.886 158.848 152.565 1.00 26.26 ?  457 ALA B C     1 
ATOM   9227  O  O     . ALA B 1 457 ? 121.504 159.394 153.605 1.00 32.54 ?  457 ALA B O     1 
ATOM   9228  C  CB    . ALA B 1 457 ? 121.540 159.622 150.200 1.00 18.26 ?  457 ALA B CB    1 
ATOM   9229  N  N     . MET B 1 458 ? 121.799 157.531 152.374 1.00 24.94 ?  458 MET B N     1 
ATOM   9230  C  CA    . MET B 1 458 ? 121.229 156.652 153.388 1.00 16.55 ?  458 MET B CA    1 
ATOM   9231  C  C     . MET B 1 458 ? 122.058 156.656 154.666 1.00 21.35 ?  458 MET B C     1 
ATOM   9232  O  O     . MET B 1 458 ? 121.503 156.624 155.770 1.00 30.53 ?  458 MET B O     1 
ATOM   9233  C  CB    . MET B 1 458 ? 121.115 155.230 152.836 1.00 22.58 ?  458 MET B CB    1 
ATOM   9234  C  CG    . MET B 1 458 ? 120.469 155.138 151.465 1.00 21.89 ?  458 MET B CG    1 
ATOM   9235  S  SD    . MET B 1 458 ? 118.901 156.014 151.379 1.00 29.65 ?  458 MET B SD    1 
ATOM   9236  C  CE    . MET B 1 458 ? 117.895 154.968 152.424 1.00 23.61 ?  458 MET B CE    1 
ATOM   9237  N  N     . LYS B 1 459 ? 123.386 156.675 154.534 1.00 19.92 ?  459 LYS B N     1 
ATOM   9238  C  CA    . LYS B 1 459 ? 124.299 156.572 155.675 1.00 17.97 ?  459 LYS B CA    1 
ATOM   9239  C  C     . LYS B 1 459 ? 124.037 155.295 156.469 1.00 20.01 ?  459 LYS B C     1 
ATOM   9240  O  O     . LYS B 1 459 ? 124.172 155.262 157.693 1.00 26.61 ?  459 LYS B O     1 
ATOM   9241  C  CB    . LYS B 1 459 ? 124.207 157.801 156.582 1.00 20.12 ?  459 LYS B CB    1 
ATOM   9242  C  CG    . LYS B 1 459 ? 124.721 159.083 155.958 1.00 24.69 ?  459 LYS B CG    1 
ATOM   9243  C  CD    . LYS B 1 459 ? 123.920 160.280 156.436 1.00 25.09 ?  459 LYS B CD    1 
ATOM   9244  C  CE    . LYS B 1 459 ? 124.059 161.452 155.484 1.00 25.13 ?  459 LYS B CE    1 
ATOM   9245  N  NZ    . LYS B 1 459 ? 125.480 161.859 155.313 1.00 27.84 1  459 LYS B NZ    1 
ATOM   9246  N  N     . SER B 1 460 ? 123.659 154.234 155.764 1.00 24.04 ?  460 SER B N     1 
ATOM   9247  C  CA    . SER B 1 460 ? 123.278 152.988 156.407 1.00 13.89 ?  460 SER B CA    1 
ATOM   9248  C  C     . SER B 1 460 ? 124.501 152.243 156.922 1.00 13.09 ?  460 SER B C     1 
ATOM   9249  O  O     . SER B 1 460 ? 125.531 152.162 156.249 1.00 26.30 ?  460 SER B O     1 
ATOM   9250  C  CB    . SER B 1 460 ? 122.505 152.102 155.433 1.00 15.88 ?  460 SER B CB    1 
ATOM   9251  O  OG    . SER B 1 460 ? 122.738 150.735 155.708 1.00 26.50 ?  460 SER B OG    1 
ATOM   9252  N  N     . ILE B 1 461 ? 124.377 151.695 158.131 1.00 10.69 ?  461 ILE B N     1 
ATOM   9253  C  CA    . ILE B 1 461 ? 125.418 150.885 158.742 1.00 19.56 ?  461 ILE B CA    1 
ATOM   9254  C  C     . ILE B 1 461 ? 124.787 149.587 159.226 1.00 16.81 ?  461 ILE B C     1 
ATOM   9255  O  O     . ILE B 1 461 ? 123.572 149.486 159.402 1.00 20.02 ?  461 ILE B O     1 
ATOM   9256  C  CB    . ILE B 1 461 ? 126.119 151.610 159.911 1.00 14.38 ?  461 ILE B CB    1 
ATOM   9257  C  CG1   . ILE B 1 461 ? 125.122 151.898 161.033 1.00 10.83 ?  461 ILE B CG1   1 
ATOM   9258  C  CG2   . ILE B 1 461 ? 126.777 152.894 159.429 1.00 17.22 ?  461 ILE B CG2   1 
ATOM   9259  C  CD1   . ILE B 1 461 ? 125.755 152.435 162.293 1.00 14.55 ?  461 ILE B CD1   1 
ATOM   9260  N  N     . GLY B 1 462 ? 125.632 148.580 159.419 1.00 15.87 ?  462 GLY B N     1 
ATOM   9261  C  CA    . GLY B 1 462 ? 125.167 147.329 159.980 1.00 6.58  ?  462 GLY B CA    1 
ATOM   9262  C  C     . GLY B 1 462 ? 125.911 146.946 161.240 1.00 11.82 ?  462 GLY B C     1 
ATOM   9263  O  O     . GLY B 1 462 ? 127.094 146.602 161.187 1.00 26.95 ?  462 GLY B O     1 
ATOM   9264  N  N     . LEU B 1 463 ? 125.227 146.993 162.378 1.00 12.36 ?  463 LEU B N     1 
ATOM   9265  C  CA    . LEU B 1 463 ? 125.812 146.618 163.659 1.00 11.25 ?  463 LEU B CA    1 
ATOM   9266  C  C     . LEU B 1 463 ? 125.246 145.261 164.057 1.00 13.98 ?  463 LEU B C     1 
ATOM   9267  O  O     . LEU B 1 463 ? 124.082 145.157 164.455 1.00 25.51 ?  463 LEU B O     1 
ATOM   9268  C  CB    . LEU B 1 463 ? 125.524 147.674 164.724 1.00 19.67 ?  463 LEU B CB    1 
ATOM   9269  C  CG    . LEU B 1 463 ? 126.022 147.371 166.139 1.00 18.45 ?  463 LEU B CG    1 
ATOM   9270  C  CD1   . LEU B 1 463 ? 127.484 146.967 166.116 1.00 6.51  ?  463 LEU B CD1   1 
ATOM   9271  C  CD2   . LEU B 1 463 ? 125.806 148.567 167.050 1.00 14.56 ?  463 LEU B CD2   1 
ATOM   9272  N  N     . GLY B 1 464 ? 126.071 144.221 163.942 1.00 14.85 ?  464 GLY B N     1 
ATOM   9273  C  CA    . GLY B 1 464 ? 125.662 142.870 164.250 1.00 13.86 ?  464 GLY B CA    1 
ATOM   9274  C  C     . GLY B 1 464 ? 126.022 142.459 165.665 1.00 13.07 ?  464 GLY B C     1 
ATOM   9275  O  O     . GLY B 1 464 ? 126.397 143.270 166.513 1.00 15.05 ?  464 GLY B O     1 
ATOM   9276  N  N     . ALA B 1 465 ? 125.900 141.158 165.913 1.00 15.16 ?  465 ALA B N     1 
ATOM   9277  C  CA    . ALA B 1 465 ? 126.225 140.588 167.209 1.00 12.37 ?  465 ALA B CA    1 
ATOM   9278  C  C     . ALA B 1 465 ? 126.747 139.175 167.009 1.00 14.17 ?  465 ALA B C     1 
ATOM   9279  O  O     . ALA B 1 465 ? 126.297 138.462 166.107 1.00 28.53 ?  465 ALA B O     1 
ATOM   9280  C  CB    . ALA B 1 465 ? 125.010 140.580 168.143 1.00 19.00 ?  465 ALA B CB    1 
ATOM   9281  N  N     . MET B 1 466 ? 127.701 138.783 167.846 1.00 20.66 ?  466 MET B N     1 
ATOM   9282  C  CA    . MET B 1 466 ? 128.267 137.444 167.838 1.00 20.75 ?  466 MET B CA    1 
ATOM   9283  C  C     . MET B 1 466 ? 128.267 136.898 169.257 1.00 20.58 ?  466 MET B C     1 
ATOM   9284  O  O     . MET B 1 466 ? 128.035 137.626 170.227 1.00 26.81 ?  466 MET B O     1 
ATOM   9285  C  CB    . MET B 1 466 ? 129.691 137.434 167.261 1.00 27.19 ?  466 MET B CB    1 
ATOM   9286  C  CG    . MET B 1 466 ? 130.619 138.464 167.884 1.00 22.89 ?  466 MET B CG    1 
ATOM   9287  S  SD    . MET B 1 466 ? 132.291 138.431 167.210 1.00 38.02 ?  466 MET B SD    1 
ATOM   9288  C  CE    . MET B 1 466 ? 131.962 138.398 165.452 1.00 29.36 ?  466 MET B CE    1 
ATOM   9289  N  N     . ASN B 1 467 ? 128.516 135.592 169.367 1.00 19.96 ?  467 ASN B N     1 
ATOM   9290  C  CA    . ASN B 1 467 ? 128.665 134.908 170.654 1.00 19.55 ?  467 ASN B CA    1 
ATOM   9291  C  C     . ASN B 1 467 ? 127.369 134.919 171.462 1.00 20.51 ?  467 ASN B C     1 
ATOM   9292  O  O     . ASN B 1 467 ? 127.393 135.029 172.688 1.00 27.46 ?  467 ASN B O     1 
ATOM   9293  C  CB    . ASN B 1 467 ? 129.810 135.503 171.476 1.00 21.54 ?  467 ASN B CB    1 
ATOM   9294  C  CG    . ASN B 1 467 ? 130.630 134.446 172.182 1.00 24.57 ?  467 ASN B CG    1 
ATOM   9295  O  OD1   . ASN B 1 467 ? 130.464 133.251 171.939 1.00 28.94 ?  467 ASN B OD1   1 
ATOM   9296  N  ND2   . ASN B 1 467 ? 131.523 134.879 173.060 1.00 28.00 ?  467 ASN B ND2   1 
ATOM   9297  N  N     . LEU B 1 468 ? 126.228 134.816 170.779 1.00 19.53 ?  468 LEU B N     1 
ATOM   9298  C  CA    . LEU B 1 468 ? 124.973 134.617 171.496 1.00 18.12 ?  468 LEU B CA    1 
ATOM   9299  C  C     . LEU B 1 468 ? 124.930 133.233 172.128 1.00 22.01 ?  468 LEU B C     1 
ATOM   9300  O  O     . LEU B 1 468 ? 124.664 133.091 173.329 1.00 25.58 ?  468 LEU B O     1 
ATOM   9301  C  CB    . LEU B 1 468 ? 123.787 134.811 170.554 1.00 24.55 ?  468 LEU B CB    1 
ATOM   9302  C  CG    . LEU B 1 468 ? 122.431 134.417 171.143 1.00 20.38 ?  468 LEU B CG    1 
ATOM   9303  C  CD1   . LEU B 1 468 ? 122.067 135.325 172.305 1.00 17.94 ?  468 LEU B CD1   1 
ATOM   9304  C  CD2   . LEU B 1 468 ? 121.343 134.431 170.084 1.00 15.41 ?  468 LEU B CD2   1 
ATOM   9305  N  N     . HIS B 1 469 ? 125.219 132.199 171.337 1.00 25.31 ?  469 HIS B N     1 
ATOM   9306  C  CA    . HIS B 1 469 ? 125.210 130.840 171.864 1.00 16.96 ?  469 HIS B CA    1 
ATOM   9307  C  C     . HIS B 1 469 ? 126.342 130.632 172.860 1.00 26.08 ?  469 HIS B C     1 
ATOM   9308  O  O     . HIS B 1 469 ? 126.178 129.908 173.844 1.00 38.87 ?  469 HIS B O     1 
ATOM   9309  C  CB    . HIS B 1 469 ? 125.306 129.825 170.727 1.00 20.40 ?  469 HIS B CB    1 
ATOM   9310  C  CG    . HIS B 1 469 ? 124.912 128.438 171.129 1.00 24.73 ?  469 HIS B CG    1 
ATOM   9311  N  ND1   . HIS B 1 469 ? 125.080 127.348 170.304 1.00 28.72 ?  469 HIS B ND1   1 
ATOM   9312  C  CD2   . HIS B 1 469 ? 124.360 127.964 172.271 1.00 25.30 ?  469 HIS B CD2   1 
ATOM   9313  C  CE1   . HIS B 1 469 ? 124.647 126.262 170.919 1.00 22.84 ?  469 HIS B CE1   1 
ATOM   9314  N  NE2   . HIS B 1 469 ? 124.206 126.608 172.114 1.00 25.44 ?  469 HIS B NE2   1 
ATOM   9315  N  N     . GLY B 1 470 ? 127.497 131.251 172.617 1.00 21.78 ?  470 GLY B N     1 
ATOM   9316  C  CA    . GLY B 1 470 ? 128.583 131.158 173.579 1.00 18.71 ?  470 GLY B CA    1 
ATOM   9317  C  C     . GLY B 1 470 ? 128.210 131.746 174.924 1.00 19.99 ?  470 GLY B C     1 
ATOM   9318  O  O     . GLY B 1 470 ? 128.457 131.142 175.971 1.00 34.01 ?  470 GLY B O     1 
ATOM   9319  N  N     . TYR B 1 471 ? 127.593 132.930 174.913 1.00 22.88 ?  471 TYR B N     1 
ATOM   9320  C  CA    . TYR B 1 471 ? 127.161 133.547 176.162 1.00 25.52 ?  471 TYR B CA    1 
ATOM   9321  C  C     . TYR B 1 471 ? 126.097 132.705 176.852 1.00 27.96 ?  471 TYR B C     1 
ATOM   9322  O  O     . TYR B 1 471 ? 126.132 132.528 178.076 1.00 32.88 ?  471 TYR B O     1 
ATOM   9323  C  CB    . TYR B 1 471 ? 126.636 134.958 175.905 1.00 24.23 ?  471 TYR B CB    1 
ATOM   9324  C  CG    . TYR B 1 471 ? 126.236 135.686 177.168 1.00 26.56 ?  471 TYR B CG    1 
ATOM   9325  C  CD1   . TYR B 1 471 ? 127.198 136.143 178.060 1.00 28.31 ?  471 TYR B CD1   1 
ATOM   9326  C  CD2   . TYR B 1 471 ? 124.901 135.892 177.483 1.00 18.57 ?  471 TYR B CD2   1 
ATOM   9327  C  CE1   . TYR B 1 471 ? 126.842 136.803 179.217 1.00 28.21 ?  471 TYR B CE1   1 
ATOM   9328  C  CE2   . TYR B 1 471 ? 124.536 136.548 178.642 1.00 21.27 ?  471 TYR B CE2   1 
ATOM   9329  C  CZ    . TYR B 1 471 ? 125.511 137.001 179.503 1.00 27.48 ?  471 TYR B CZ    1 
ATOM   9330  O  OH    . TYR B 1 471 ? 125.155 137.653 180.660 1.00 32.99 ?  471 TYR B OH    1 
ATOM   9331  N  N     . LEU B 1 472 ? 125.136 132.180 176.086 1.00 26.27 ?  472 LEU B N     1 
ATOM   9332  C  CA    . LEU B 1 472 ? 124.064 131.396 176.690 1.00 23.87 ?  472 LEU B CA    1 
ATOM   9333  C  C     . LEU B 1 472 ? 124.587 130.092 177.282 1.00 25.52 ?  472 LEU B C     1 
ATOM   9334  O  O     . LEU B 1 472 ? 124.176 129.695 178.378 1.00 31.23 ?  472 LEU B O     1 
ATOM   9335  C  CB    . LEU B 1 472 ? 122.970 131.118 175.660 1.00 28.13 ?  472 LEU B CB    1 
ATOM   9336  C  CG    . LEU B 1 472 ? 122.204 132.329 175.128 1.00 27.42 ?  472 LEU B CG    1 
ATOM   9337  C  CD1   . LEU B 1 472 ? 121.359 131.940 173.925 1.00 24.49 ?  472 LEU B CD1   1 
ATOM   9338  C  CD2   . LEU B 1 472 ? 121.344 132.947 176.218 1.00 19.86 ?  472 LEU B CD2   1 
ATOM   9339  N  N     . ALA B 1 473 ? 125.489 129.409 176.573 1.00 25.93 ?  473 ALA B N     1 
ATOM   9340  C  CA    . ALA B 1 473 ? 126.010 128.137 177.058 1.00 26.31 ?  473 ALA B CA    1 
ATOM   9341  C  C     . ALA B 1 473 ? 126.960 128.336 178.231 1.00 33.22 ?  473 ALA B C     1 
ATOM   9342  O  O     . ALA B 1 473 ? 126.979 127.525 179.164 1.00 38.99 ?  473 ALA B O     1 
ATOM   9343  C  CB    . ALA B 1 473 ? 126.705 127.391 175.921 1.00 26.76 ?  473 ALA B CB    1 
ATOM   9344  N  N     . GLN B 1 474 ? 127.757 129.403 178.205 1.00 27.75 ?  474 GLN B N     1 
ATOM   9345  C  CA    . GLN B 1 474 ? 128.663 129.687 179.309 1.00 28.56 ?  474 GLN B CA    1 
ATOM   9346  C  C     . GLN B 1 474 ? 127.943 130.224 180.537 1.00 29.18 ?  474 GLN B C     1 
ATOM   9347  O  O     . GLN B 1 474 ? 128.561 130.324 181.602 1.00 36.85 ?  474 GLN B O     1 
ATOM   9348  C  CB    . GLN B 1 474 ? 129.739 130.679 178.862 1.00 28.71 ?  474 GLN B CB    1 
ATOM   9349  C  CG    . GLN B 1 474 ? 130.800 130.060 177.969 1.00 28.77 ?  474 GLN B CG    1 
ATOM   9350  C  CD    . GLN B 1 474 ? 131.762 131.084 177.410 1.00 33.70 ?  474 GLN B CD    1 
ATOM   9351  O  OE1   . GLN B 1 474 ? 132.557 131.671 178.143 1.00 36.08 ?  474 GLN B OE1   1 
ATOM   9352  N  NE2   . GLN B 1 474 ? 131.697 131.306 176.102 1.00 33.97 ?  474 GLN B NE2   1 
ATOM   9353  N  N     . ASN B 1 475 ? 126.663 130.572 180.416 1.00 31.43 ?  475 ASN B N     1 
ATOM   9354  C  CA    . ASN B 1 475 ? 125.855 131.018 181.541 1.00 31.52 ?  475 ASN B CA    1 
ATOM   9355  C  C     . ASN B 1 475 ? 124.785 130.004 181.922 1.00 31.77 ?  475 ASN B C     1 
ATOM   9356  O  O     . ASN B 1 475 ? 123.875 130.336 182.687 1.00 34.96 ?  475 ASN B O     1 
ATOM   9357  C  CB    . ASN B 1 475 ? 125.213 132.370 181.224 1.00 30.74 ?  475 ASN B CB    1 
ATOM   9358  C  CG    . ASN B 1 475 ? 126.211 133.506 181.262 1.00 30.26 ?  475 ASN B CG    1 
ATOM   9359  O  OD1   . ASN B 1 475 ? 126.390 134.158 182.290 1.00 38.24 ?  475 ASN B OD1   1 
ATOM   9360  N  ND2   . ASN B 1 475 ? 126.878 133.741 180.141 1.00 28.97 ?  475 ASN B ND2   1 
ATOM   9361  N  N     . GLY B 1 476 ? 124.873 128.781 181.409 1.00 31.06 ?  476 GLY B N     1 
ATOM   9362  C  CA    . GLY B 1 476 ? 123.915 127.743 181.742 1.00 30.18 ?  476 GLY B CA    1 
ATOM   9363  C  C     . GLY B 1 476 ? 122.508 127.993 181.245 1.00 35.17 ?  476 GLY B C     1 
ATOM   9364  O  O     . GLY B 1 476 ? 121.543 127.731 181.973 1.00 37.39 ?  476 GLY B O     1 
ATOM   9365  N  N     . ILE B 1 477 ? 122.364 128.498 180.023 1.00 32.15 ?  477 ILE B N     1 
ATOM   9366  C  CA    . ILE B 1 477 ? 121.063 128.736 179.411 1.00 27.50 ?  477 ILE B CA    1 
ATOM   9367  C  C     . ILE B 1 477 ? 121.016 127.977 178.093 1.00 31.33 ?  477 ILE B C     1 
ATOM   9368  O  O     . ILE B 1 477 ? 121.880 128.173 177.228 1.00 36.33 ?  477 ILE B O     1 
ATOM   9369  C  CB    . ILE B 1 477 ? 120.794 130.231 179.191 1.00 26.02 ?  477 ILE B CB    1 
ATOM   9370  C  CG1   . ILE B 1 477 ? 120.908 130.998 180.509 1.00 29.49 ?  477 ILE B CG1   1 
ATOM   9371  C  CG2   . ILE B 1 477 ? 119.421 130.438 178.579 1.00 30.20 ?  477 ILE B CG2   1 
ATOM   9372  C  CD1   . ILE B 1 477 ? 121.150 132.473 180.328 1.00 32.35 ?  477 ILE B CD1   1 
ATOM   9373  N  N     . ALA B 1 478 ? 120.015 127.114 177.942 1.00 33.41 ?  478 ALA B N     1 
ATOM   9374  C  CA    . ALA B 1 478 ? 119.835 126.391 176.691 1.00 27.28 ?  478 ALA B CA    1 
ATOM   9375  C  C     . ALA B 1 478 ? 119.395 127.353 175.595 1.00 32.74 ?  478 ALA B C     1 
ATOM   9376  O  O     . ALA B 1 478 ? 118.522 128.197 175.813 1.00 34.41 ?  478 ALA B O     1 
ATOM   9377  C  CB    . ALA B 1 478 ? 118.807 125.275 176.866 1.00 27.73 ?  478 ALA B CB    1 
ATOM   9378  N  N     . TYR B 1 479 ? 120.003 127.221 174.413 1.00 30.56 ?  479 TYR B N     1 
ATOM   9379  C  CA    . TYR B 1 479 ? 119.705 128.132 173.312 1.00 23.51 ?  479 TYR B CA    1 
ATOM   9380  C  C     . TYR B 1 479 ? 118.236 128.071 172.911 1.00 26.65 ?  479 TYR B C     1 
ATOM   9381  O  O     . TYR B 1 479 ? 117.665 129.084 172.495 1.00 32.90 ?  479 TYR B O     1 
ATOM   9382  C  CB    . TYR B 1 479 ? 120.606 127.809 172.120 1.00 18.58 ?  479 TYR B CB    1 
ATOM   9383  C  CG    . TYR B 1 479 ? 120.462 128.729 170.925 1.00 26.64 ?  479 TYR B CG    1 
ATOM   9384  C  CD1   . TYR B 1 479 ? 119.512 128.484 169.941 1.00 24.92 ?  479 TYR B CD1   1 
ATOM   9385  C  CD2   . TYR B 1 479 ? 121.292 129.832 170.773 1.00 25.29 ?  479 TYR B CD2   1 
ATOM   9386  C  CE1   . TYR B 1 479 ? 119.384 129.320 168.848 1.00 22.84 ?  479 TYR B CE1   1 
ATOM   9387  C  CE2   . TYR B 1 479 ? 121.172 130.672 169.683 1.00 22.12 ?  479 TYR B CE2   1 
ATOM   9388  C  CZ    . TYR B 1 479 ? 120.218 130.411 168.724 1.00 28.95 ?  479 TYR B CZ    1 
ATOM   9389  O  OH    . TYR B 1 479 ? 120.097 131.247 167.638 1.00 29.93 ?  479 TYR B OH    1 
ATOM   9390  N  N     . GLU B 1 480 ? 117.610 126.902 173.027 1.00 28.98 ?  480 GLU B N     1 
ATOM   9391  C  CA    . GLU B 1 480 ? 116.202 126.753 172.687 1.00 28.27 ?  480 GLU B CA    1 
ATOM   9392  C  C     . GLU B 1 480 ? 115.268 127.119 173.831 1.00 27.46 ?  480 GLU B C     1 
ATOM   9393  O  O     . GLU B 1 480 ? 114.050 127.159 173.625 1.00 33.76 ?  480 GLU B O     1 
ATOM   9394  C  CB    . GLU B 1 480 ? 115.909 125.315 172.251 1.00 30.32 ?  480 GLU B CB    1 
ATOM   9395  C  CG    . GLU B 1 480 ? 116.646 124.865 171.006 1.00 28.24 ?  480 GLU B CG    1 
ATOM   9396  C  CD    . GLU B 1 480 ? 116.508 123.375 170.772 1.00 36.35 ?  480 GLU B CD    1 
ATOM   9397  O  OE1   . GLU B 1 480 ? 115.400 122.930 170.406 1.00 36.92 ?  480 GLU B OE1   1 
ATOM   9398  O  OE2   . GLU B 1 480 ? 117.502 122.645 170.963 1.00 36.74 -1 480 GLU B OE2   1 
ATOM   9399  N  N     . SER B 1 481 ? 115.800 127.386 175.019 1.00 26.14 ?  481 SER B N     1 
ATOM   9400  C  CA    . SER B 1 481 ? 114.956 127.650 176.171 1.00 26.98 ?  481 SER B CA    1 
ATOM   9401  C  C     . SER B 1 481 ? 114.267 129.008 176.038 1.00 28.79 ?  481 SER B C     1 
ATOM   9402  O  O     . SER B 1 481 ? 114.771 129.906 175.358 1.00 29.80 ?  481 SER B O     1 
ATOM   9403  C  CB    . SER B 1 481 ? 115.781 127.612 177.453 1.00 28.32 ?  481 SER B CB    1 
ATOM   9404  O  OG    . SER B 1 481 ? 116.335 128.883 177.739 1.00 32.20 ?  481 SER B OG    1 
ATOM   9405  N  N     . PRO B 1 482 ? 113.101 129.175 176.667 1.00 36.02 ?  482 PRO B N     1 
ATOM   9406  C  CA    . PRO B 1 482 ? 112.479 130.508 176.702 1.00 32.05 ?  482 PRO B CA    1 
ATOM   9407  C  C     . PRO B 1 482 ? 113.333 131.549 177.401 1.00 31.69 ?  482 PRO B C     1 
ATOM   9408  O  O     . PRO B 1 482 ? 113.213 132.740 177.092 1.00 31.35 ?  482 PRO B O     1 
ATOM   9409  C  CB    . PRO B 1 482 ? 111.162 130.259 177.450 1.00 30.81 ?  482 PRO B CB    1 
ATOM   9410  C  CG    . PRO B 1 482 ? 110.897 128.804 177.286 1.00 31.49 ?  482 PRO B CG    1 
ATOM   9411  C  CD    . PRO B 1 482 ? 112.240 128.146 177.272 1.00 33.90 ?  482 PRO B CD    1 
ATOM   9412  N  N     . GLU B 1 483 ? 114.183 131.137 178.345 1.00 34.74 ?  483 GLU B N     1 
ATOM   9413  C  CA    . GLU B 1 483 ? 115.077 132.085 179.004 1.00 33.51 ?  483 GLU B CA    1 
ATOM   9414  C  C     . GLU B 1 483 ? 116.070 132.684 178.016 1.00 33.18 ?  483 GLU B C     1 
ATOM   9415  O  O     . GLU B 1 483 ? 116.390 133.876 178.093 1.00 38.65 ?  483 GLU B O     1 
ATOM   9416  C  CB    . GLU B 1 483 ? 115.813 131.400 180.154 1.00 36.12 ?  483 GLU B CB    1 
ATOM   9417  C  CG    . GLU B 1 483 ? 114.957 131.162 181.382 1.00 37.22 ?  483 GLU B CG    1 
ATOM   9418  C  CD    . GLU B 1 483 ? 114.356 129.772 181.411 1.00 41.25 ?  483 GLU B CD    1 
ATOM   9419  O  OE1   . GLU B 1 483 ? 113.969 129.267 180.336 1.00 39.62 ?  483 GLU B OE1   1 
ATOM   9420  O  OE2   . GLU B 1 483 ? 114.269 129.184 182.510 1.00 40.92 -1 483 GLU B OE2   1 
ATOM   9421  N  N     . ALA B 1 484 ? 116.574 131.869 177.089 1.00 26.92 ?  484 ALA B N     1 
ATOM   9422  C  CA    . ALA B 1 484 ? 117.478 132.380 176.066 1.00 25.36 ?  484 ALA B CA    1 
ATOM   9423  C  C     . ALA B 1 484 ? 116.782 133.394 175.168 1.00 27.63 ?  484 ALA B C     1 
ATOM   9424  O  O     . ALA B 1 484 ? 117.366 134.426 174.815 1.00 27.44 ?  484 ALA B O     1 
ATOM   9425  C  CB    . ALA B 1 484 ? 118.036 131.223 175.241 1.00 24.44 ?  484 ALA B CB    1 
ATOM   9426  N  N     . ARG B 1 485 ? 115.535 133.117 174.782 1.00 29.59 ?  485 ARG B N     1 
ATOM   9427  C  CA    . ARG B 1 485 ? 114.790 134.073 173.969 1.00 22.93 ?  485 ARG B CA    1 
ATOM   9428  C  C     . ARG B 1 485 ? 114.490 135.349 174.744 1.00 23.94 ?  485 ARG B C     1 
ATOM   9429  O  O     . ARG B 1 485 ? 114.506 136.439 174.166 1.00 33.77 ?  485 ARG B O     1 
ATOM   9430  C  CB    . ARG B 1 485 ? 113.499 133.439 173.458 1.00 28.90 ?  485 ARG B CB    1 
ATOM   9431  C  CG    . ARG B 1 485 ? 113.721 132.330 172.446 1.00 27.03 ?  485 ARG B CG    1 
ATOM   9432  C  CD    . ARG B 1 485 ? 112.417 131.903 171.802 1.00 27.04 ?  485 ARG B CD    1 
ATOM   9433  N  NE    . ARG B 1 485 ? 111.436 131.462 172.786 1.00 27.22 ?  485 ARG B NE    1 
ATOM   9434  C  CZ    . ARG B 1 485 ? 111.328 130.218 173.231 1.00 27.87 ?  485 ARG B CZ    1 
ATOM   9435  N  NH1   . ARG B 1 485 ? 112.139 129.261 172.810 1.00 25.07 1  485 ARG B NH1   1 
ATOM   9436  N  NH2   . ARG B 1 485 ? 110.384 129.928 174.120 1.00 30.16 ?  485 ARG B NH2   1 
ATOM   9437  N  N     . ASP B 1 486 ? 114.220 135.233 176.045 1.00 30.99 ?  486 ASP B N     1 
ATOM   9438  C  CA    . ASP B 1 486 ? 114.040 136.418 176.878 1.00 27.43 ?  486 ASP B CA    1 
ATOM   9439  C  C     . ASP B 1 486 ? 115.312 137.254 176.931 1.00 26.61 ?  486 ASP B C     1 
ATOM   9440  O  O     . ASP B 1 486 ? 115.265 138.489 176.823 1.00 33.37 ?  486 ASP B O     1 
ATOM   9441  C  CB    . ASP B 1 486 ? 113.611 135.994 178.283 1.00 32.56 ?  486 ASP B CB    1 
ATOM   9442  C  CG    . ASP B 1 486 ? 113.258 137.167 179.167 1.00 40.37 ?  486 ASP B CG    1 
ATOM   9443  O  OD1   . ASP B 1 486 ? 112.443 138.012 178.743 1.00 37.86 ?  486 ASP B OD1   1 
ATOM   9444  O  OD2   . ASP B 1 486 ? 113.793 137.234 180.291 1.00 37.16 -1 486 ASP B OD2   1 
ATOM   9445  N  N     . PHE B 1 487 ? 116.462 136.596 177.091 1.00 25.12 ?  487 PHE B N     1 
ATOM   9446  C  CA    . PHE B 1 487 ? 117.729 137.317 177.082 1.00 24.05 ?  487 PHE B CA    1 
ATOM   9447  C  C     . PHE B 1 487 ? 117.956 138.006 175.746 1.00 23.70 ?  487 PHE B C     1 
ATOM   9448  O  O     . PHE B 1 487 ? 118.406 139.153 175.700 1.00 29.55 ?  487 PHE B O     1 
ATOM   9449  C  CB    . PHE B 1 487 ? 118.896 136.382 177.382 1.00 25.33 ?  487 PHE B CB    1 
ATOM   9450  C  CG    . PHE B 1 487 ? 120.221 136.956 176.978 1.00 27.57 ?  487 PHE B CG    1 
ATOM   9451  C  CD1   . PHE B 1 487 ? 120.823 137.932 177.750 1.00 22.50 ?  487 PHE B CD1   1 
ATOM   9452  C  CD2   . PHE B 1 487 ? 120.841 136.558 175.805 1.00 29.01 ?  487 PHE B CD2   1 
ATOM   9453  C  CE1   . PHE B 1 487 ? 122.026 138.484 177.376 1.00 24.30 ?  487 PHE B CE1   1 
ATOM   9454  C  CE2   . PHE B 1 487 ? 122.046 137.108 175.426 1.00 25.24 ?  487 PHE B CE2   1 
ATOM   9455  C  CZ    . PHE B 1 487 ? 122.639 138.073 176.214 1.00 27.43 ?  487 PHE B CZ    1 
ATOM   9456  N  N     . ALA B 1 488 ? 117.687 137.302 174.646 1.00 24.45 ?  488 ALA B N     1 
ATOM   9457  C  CA    . ALA B 1 488 ? 117.873 137.902 173.330 1.00 19.89 ?  488 ALA B CA    1 
ATOM   9458  C  C     . ALA B 1 488 ? 116.959 139.105 173.150 1.00 26.39 ?  488 ALA B C     1 
ATOM   9459  O  O     . ALA B 1 488 ? 117.388 140.152 172.654 1.00 31.88 ?  488 ALA B O     1 
ATOM   9460  C  CB    . ALA B 1 488 ? 117.623 136.866 172.237 1.00 20.17 ?  488 ALA B CB    1 
ATOM   9461  N  N     . ASN B 1 489 ? 115.701 138.978 173.575 1.00 25.22 ?  489 ASN B N     1 
ATOM   9462  C  CA    . ASN B 1 489 ? 114.761 140.090 173.499 1.00 24.36 ?  489 ASN B CA    1 
ATOM   9463  C  C     . ASN B 1 489 ? 115.296 141.306 174.237 1.00 23.95 ?  489 ASN B C     1 
ATOM   9464  O  O     . ASN B 1 489 ? 115.382 142.402 173.672 1.00 24.39 ?  489 ASN B O     1 
ATOM   9465  C  CB    . ASN B 1 489 ? 113.411 139.660 174.074 1.00 21.91 ?  489 ASN B CB    1 
ATOM   9466  C  CG    . ASN B 1 489 ? 112.319 140.670 173.815 1.00 27.14 ?  489 ASN B CG    1 
ATOM   9467  O  OD1   . ASN B 1 489 ? 112.181 141.182 172.707 1.00 33.77 ?  489 ASN B OD1   1 
ATOM   9468  N  ND2   . ASN B 1 489 ? 111.528 140.958 174.840 1.00 30.58 ?  489 ASN B ND2   1 
ATOM   9469  N  N     . THR B 1 490 ? 115.691 141.125 175.499 1.00 27.27 ?  490 THR B N     1 
ATOM   9470  C  CA    . THR B 1 490 ? 116.156 142.260 176.289 1.00 22.97 ?  490 THR B CA    1 
ATOM   9471  C  C     . THR B 1 490 ? 117.446 142.845 175.723 1.00 24.75 ?  490 THR B C     1 
ATOM   9472  O  O     . THR B 1 490 ? 117.569 144.066 175.563 1.00 25.78 ?  490 THR B O     1 
ATOM   9473  C  CB    . THR B 1 490 ? 116.353 141.845 177.746 1.00 28.98 ?  490 THR B CB    1 
ATOM   9474  O  OG1   . THR B 1 490 ? 115.141 141.267 178.247 1.00 32.64 ?  490 THR B OG1   1 
ATOM   9475  C  CG2   . THR B 1 490 ? 116.726 143.051 178.591 1.00 26.06 ?  490 THR B CG2   1 
ATOM   9476  N  N     . PHE B 1 491 ? 118.417 141.985 175.404 1.00 24.63 ?  491 PHE B N     1 
ATOM   9477  C  CA    . PHE B 1 491 ? 119.716 142.457 174.939 1.00 19.07 ?  491 PHE B CA    1 
ATOM   9478  C  C     . PHE B 1 491 ? 119.592 143.214 173.627 1.00 19.39 ?  491 PHE B C     1 
ATOM   9479  O  O     . PHE B 1 491 ? 120.194 144.281 173.459 1.00 28.67 ?  491 PHE B O     1 
ATOM   9480  C  CB    . PHE B 1 491 ? 120.675 141.275 174.788 1.00 25.23 ?  491 PHE B CB    1 
ATOM   9481  C  CG    . PHE B 1 491 ? 121.989 141.635 174.153 1.00 23.98 ?  491 PHE B CG    1 
ATOM   9482  C  CD1   . PHE B 1 491 ? 123.034 142.112 174.924 1.00 19.94 ?  491 PHE B CD1   1 
ATOM   9483  C  CD2   . PHE B 1 491 ? 122.183 141.491 172.788 1.00 19.44 ?  491 PHE B CD2   1 
ATOM   9484  C  CE1   . PHE B 1 491 ? 124.243 142.444 174.348 1.00 16.87 ?  491 PHE B CE1   1 
ATOM   9485  C  CE2   . PHE B 1 491 ? 123.387 141.825 172.208 1.00 17.20 ?  491 PHE B CE2   1 
ATOM   9486  C  CZ    . PHE B 1 491 ? 124.419 142.302 172.990 1.00 23.78 ?  491 PHE B CZ    1 
ATOM   9487  N  N     . PHE B 1 492 ? 118.817 142.687 172.681 1.00 17.42 ?  492 PHE B N     1 
ATOM   9488  C  CA    . PHE B 1 492 ? 118.703 143.351 171.395 1.00 12.24 ?  492 PHE B CA    1 
ATOM   9489  C  C     . PHE B 1 492 ? 117.763 144.546 171.436 1.00 13.03 ?  492 PHE B C     1 
ATOM   9490  O  O     . PHE B 1 492 ? 117.934 145.468 170.637 1.00 24.31 ?  492 PHE B O     1 
ATOM   9491  C  CB    . PHE B 1 492 ? 118.281 142.341 170.331 1.00 17.91 ?  492 PHE B CB    1 
ATOM   9492  C  CG    . PHE B 1 492 ? 119.390 141.411 169.932 1.00 20.42 ?  492 PHE B CG    1 
ATOM   9493  C  CD1   . PHE B 1 492 ? 120.413 141.848 169.109 1.00 14.94 ?  492 PHE B CD1   1 
ATOM   9494  C  CD2   . PHE B 1 492 ? 119.433 140.115 170.411 1.00 19.18 ?  492 PHE B CD2   1 
ATOM   9495  C  CE1   . PHE B 1 492 ? 121.443 141.002 168.754 1.00 10.03 ?  492 PHE B CE1   1 
ATOM   9496  C  CE2   . PHE B 1 492 ? 120.461 139.264 170.060 1.00 15.06 ?  492 PHE B CE2   1 
ATOM   9497  C  CZ    . PHE B 1 492 ? 121.466 139.709 169.229 1.00 15.00 ?  492 PHE B CZ    1 
ATOM   9498  N  N     . MET B 1 493 ? 116.812 144.588 172.374 1.00 16.96 ?  493 MET B N     1 
ATOM   9499  C  CA    . MET B 1 493 ? 116.090 145.834 172.602 1.00 17.53 ?  493 MET B CA    1 
ATOM   9500  C  C     . MET B 1 493 ? 117.029 146.910 173.131 1.00 17.63 ?  493 MET B C     1 
ATOM   9501  O  O     . MET B 1 493 ? 116.945 148.069 172.717 1.00 26.01 ?  493 MET B O     1 
ATOM   9502  C  CB    . MET B 1 493 ? 114.915 145.597 173.556 1.00 17.60 ?  493 MET B CB    1 
ATOM   9503  C  CG    . MET B 1 493 ? 114.257 146.855 174.130 1.00 20.72 ?  493 MET B CG    1 
ATOM   9504  S  SD    . MET B 1 493 ? 115.084 147.586 175.559 1.00 30.63 ?  493 MET B SD    1 
ATOM   9505  C  CE    . MET B 1 493 ? 115.096 146.192 176.679 1.00 24.03 ?  493 MET B CE    1 
ATOM   9506  N  N     . MET B 1 494 ? 117.933 146.543 174.045 1.00 21.86 ?  494 MET B N     1 
ATOM   9507  C  CA    . MET B 1 494 ? 118.941 147.492 174.517 1.00 16.39 ?  494 MET B CA    1 
ATOM   9508  C  C     . MET B 1 494 ? 119.841 147.957 173.378 1.00 19.03 ?  494 MET B C     1 
ATOM   9509  O  O     . MET B 1 494 ? 120.156 149.150 173.268 1.00 22.87 ?  494 MET B O     1 
ATOM   9510  C  CB    . MET B 1 494 ? 119.782 146.859 175.625 1.00 20.19 ?  494 MET B CB    1 
ATOM   9511  C  CG    . MET B 1 494 ? 119.023 146.508 176.890 1.00 20.19 ?  494 MET B CG    1 
ATOM   9512  S  SD    . MET B 1 494 ? 120.129 146.352 178.304 1.00 37.53 ?  494 MET B SD    1 
ATOM   9513  C  CE    . MET B 1 494 ? 120.511 148.066 178.637 1.00 30.33 ?  494 MET B CE    1 
ATOM   9514  N  N     . VAL B 1 495 ? 120.273 147.022 172.531 1.00 19.01 ?  495 VAL B N     1 
ATOM   9515  C  CA    . VAL B 1 495 ? 121.129 147.371 171.402 1.00 17.66 ?  495 VAL B CA    1 
ATOM   9516  C  C     . VAL B 1 495 ? 120.407 148.324 170.459 1.00 17.55 ?  495 VAL B C     1 
ATOM   9517  O  O     . VAL B 1 495 ? 120.978 149.321 170.010 1.00 28.72 ?  495 VAL B O     1 
ATOM   9518  C  CB    . VAL B 1 495 ? 121.600 146.099 170.673 1.00 15.28 ?  495 VAL B CB    1 
ATOM   9519  C  CG1   . VAL B 1 495 ? 122.255 146.454 169.349 1.00 10.14 ?  495 VAL B CG1   1 
ATOM   9520  C  CG2   . VAL B 1 495 ? 122.562 145.316 171.545 1.00 19.24 ?  495 VAL B CG2   1 
ATOM   9521  N  N     . ASN B 1 496 ? 119.140 148.035 170.148 1.00 19.18 ?  496 ASN B N     1 
ATOM   9522  C  CA    . ASN B 1 496 ? 118.366 148.918 169.282 1.00 12.13 ?  496 ASN B CA    1 
ATOM   9523  C  C     . ASN B 1 496 ? 118.173 150.287 169.916 1.00 19.26 ?  496 ASN B C     1 
ATOM   9524  O  O     . ASN B 1 496 ? 118.288 151.314 169.239 1.00 30.91 ?  496 ASN B O     1 
ATOM   9525  C  CB    . ASN B 1 496 ? 117.013 148.282 168.962 1.00 16.23 ?  496 ASN B CB    1 
ATOM   9526  C  CG    . ASN B 1 496 ? 116.343 148.915 167.763 1.00 16.08 ?  496 ASN B CG    1 
ATOM   9527  O  OD1   . ASN B 1 496 ? 117.009 149.411 166.856 1.00 24.74 ?  496 ASN B OD1   1 
ATOM   9528  N  ND2   . ASN B 1 496 ? 115.017 148.904 167.752 1.00 15.35 ?  496 ASN B ND2   1 
ATOM   9529  N  N     . PHE B 1 497 ? 117.882 150.323 171.218 1.00 20.27 ?  497 PHE B N     1 
ATOM   9530  C  CA    . PHE B 1 497 ? 117.684 151.591 171.910 1.00 15.60 ?  497 PHE B CA    1 
ATOM   9531  C  C     . PHE B 1 497 ? 118.934 152.452 171.830 1.00 19.24 ?  497 PHE B C     1 
ATOM   9532  O  O     . PHE B 1 497 ? 118.870 153.632 171.472 1.00 26.32 ?  497 PHE B O     1 
ATOM   9533  C  CB    . PHE B 1 497 ? 117.301 151.328 173.367 1.00 17.84 ?  497 PHE B CB    1 
ATOM   9534  C  CG    . PHE B 1 497 ? 117.124 152.573 174.189 1.00 20.97 ?  497 PHE B CG    1 
ATOM   9535  C  CD1   . PHE B 1 497 ? 118.195 153.134 174.867 1.00 21.66 ?  497 PHE B CD1   1 
ATOM   9536  C  CD2   . PHE B 1 497 ? 115.884 153.177 174.295 1.00 21.23 ?  497 PHE B CD2   1 
ATOM   9537  C  CE1   . PHE B 1 497 ? 118.033 154.276 175.622 1.00 22.63 ?  497 PHE B CE1   1 
ATOM   9538  C  CE2   . PHE B 1 497 ? 115.716 154.320 175.051 1.00 20.87 ?  497 PHE B CE2   1 
ATOM   9539  C  CZ    . PHE B 1 497 ? 116.793 154.868 175.716 1.00 23.33 ?  497 PHE B CZ    1 
ATOM   9540  N  N     . TYR B 1 498 ? 120.089 151.870 172.146 1.00 26.89 ?  498 TYR B N     1 
ATOM   9541  C  CA    . TYR B 1 498 ? 121.310 152.664 172.164 1.00 18.43 ?  498 TYR B CA    1 
ATOM   9542  C  C     . TYR B 1 498 ? 121.806 152.979 170.759 1.00 18.27 ?  498 TYR B C     1 
ATOM   9543  O  O     . TYR B 1 498 ? 122.422 154.028 170.553 1.00 26.71 ?  498 TYR B O     1 
ATOM   9544  C  CB    . TYR B 1 498 ? 122.379 151.954 172.992 1.00 18.97 ?  498 TYR B CB    1 
ATOM   9545  C  CG    . TYR B 1 498 ? 122.057 151.988 174.468 1.00 22.61 ?  498 TYR B CG    1 
ATOM   9546  C  CD1   . TYR B 1 498 ? 121.873 153.198 175.125 1.00 23.34 ?  498 TYR B CD1   1 
ATOM   9547  C  CD2   . TYR B 1 498 ? 121.911 150.818 175.199 1.00 26.29 ?  498 TYR B CD2   1 
ATOM   9548  C  CE1   . TYR B 1 498 ? 121.566 153.242 176.468 1.00 24.09 ?  498 TYR B CE1   1 
ATOM   9549  C  CE2   . TYR B 1 498 ? 121.605 150.852 176.545 1.00 25.24 ?  498 TYR B CE2   1 
ATOM   9550  C  CZ    . TYR B 1 498 ? 121.433 152.067 177.174 1.00 29.24 ?  498 TYR B CZ    1 
ATOM   9551  O  OH    . TYR B 1 498 ? 121.130 152.109 178.515 1.00 35.73 ?  498 TYR B OH    1 
ATOM   9552  N  N     . SER B 1 499 ? 121.513 152.123 169.776 1.00 19.26 ?  499 SER B N     1 
ATOM   9553  C  CA    . SER B 1 499 ? 121.844 152.451 168.395 1.00 13.36 ?  499 SER B CA    1 
ATOM   9554  C  C     . SER B 1 499 ? 121.004 153.618 167.891 1.00 18.33 ?  499 SER B C     1 
ATOM   9555  O  O     . SER B 1 499 ? 121.525 154.521 167.229 1.00 20.27 ?  499 SER B O     1 
ATOM   9556  C  CB    . SER B 1 499 ? 121.653 151.224 167.505 1.00 14.93 ?  499 SER B CB    1 
ATOM   9557  O  OG    . SER B 1 499 ? 122.328 151.380 166.271 1.00 19.27 ?  499 SER B OG    1 
ATOM   9558  N  N     . ILE B 1 500 ? 119.706 153.621 168.203 1.00 18.14 ?  500 ILE B N     1 
ATOM   9559  C  CA    . ILE B 1 500 ? 118.851 154.745 167.831 1.00 20.90 ?  500 ILE B CA    1 
ATOM   9560  C  C     . ILE B 1 500 ? 119.301 156.010 168.546 1.00 19.50 ?  500 ILE B C     1 
ATOM   9561  O  O     . ILE B 1 500 ? 119.323 157.099 167.959 1.00 26.97 ?  500 ILE B O     1 
ATOM   9562  C  CB    . ILE B 1 500 ? 117.376 154.420 168.131 1.00 23.62 ?  500 ILE B CB    1 
ATOM   9563  C  CG1   . ILE B 1 500 ? 116.875 153.306 167.218 1.00 18.38 ?  500 ILE B CG1   1 
ATOM   9564  C  CG2   . ILE B 1 500 ? 116.507 155.653 167.968 1.00 18.21 ?  500 ILE B CG2   1 
ATOM   9565  C  CD1   . ILE B 1 500 ? 115.579 152.702 167.675 1.00 22.35 ?  500 ILE B CD1   1 
ATOM   9566  N  N     . GLN B 1 501 ? 119.664 155.889 169.825 1.00 20.82 ?  501 GLN B N     1 
ATOM   9567  C  CA    . GLN B 1 501 ? 120.136 157.048 170.572 1.00 22.83 ?  501 GLN B CA    1 
ATOM   9568  C  C     . GLN B 1 501 ? 121.412 157.615 169.963 1.00 24.83 ?  501 GLN B C     1 
ATOM   9569  O  O     . GLN B 1 501 ? 121.539 158.833 169.803 1.00 30.68 ?  501 GLN B O     1 
ATOM   9570  C  CB    . GLN B 1 501 ? 120.357 156.673 172.035 1.00 27.35 ?  501 GLN B CB    1 
ATOM   9571  C  CG    . GLN B 1 501 ? 120.253 157.845 172.994 1.00 24.19 ?  501 GLN B CG    1 
ATOM   9572  C  CD    . GLN B 1 501 ? 120.201 157.406 174.441 1.00 28.90 ?  501 GLN B CD    1 
ATOM   9573  O  OE1   . GLN B 1 501 ? 121.022 156.611 174.892 1.00 34.53 ?  501 GLN B OE1   1 
ATOM   9574  N  NE2   . GLN B 1 501 ? 119.227 157.924 175.180 1.00 31.97 ?  501 GLN B NE2   1 
ATOM   9575  N  N     . ARG B 1 502 ? 122.364 156.749 169.609 1.00 23.90 ?  502 ARG B N     1 
ATOM   9576  C  CA    . ARG B 1 502 ? 123.596 157.222 168.990 1.00 20.10 ?  502 ARG B CA    1 
ATOM   9577  C  C     . ARG B 1 502 ? 123.334 157.831 167.618 1.00 22.90 ?  502 ARG B C     1 
ATOM   9578  O  O     . ARG B 1 502 ? 123.952 158.835 167.257 1.00 30.30 ?  502 ARG B O     1 
ATOM   9579  C  CB    . ARG B 1 502 ? 124.610 156.085 168.884 1.00 23.30 ?  502 ARG B CB    1 
ATOM   9580  C  CG    . ARG B 1 502 ? 126.015 156.565 168.563 1.00 26.41 ?  502 ARG B CG    1 
ATOM   9581  C  CD    . ARG B 1 502 ? 126.421 157.707 169.476 1.00 26.01 ?  502 ARG B CD    1 
ATOM   9582  N  NE    . ARG B 1 502 ? 127.633 158.372 169.012 1.00 24.91 ?  502 ARG B NE    1 
ATOM   9583  C  CZ    . ARG B 1 502 ? 127.861 159.673 169.121 1.00 23.93 ?  502 ARG B CZ    1 
ATOM   9584  N  NH1   . ARG B 1 502 ? 126.982 160.484 169.685 1.00 30.63 1  502 ARG B NH1   1 
ATOM   9585  N  NH2   . ARG B 1 502 ? 129.001 160.173 168.653 1.00 28.82 ?  502 ARG B NH2   1 
ATOM   9586  N  N     . SER B 1 503 ? 122.434 157.232 166.835 1.00 23.38 ?  503 SER B N     1 
ATOM   9587  C  CA    . SER B 1 503 ? 122.107 157.793 165.529 1.00 22.11 ?  503 SER B CA    1 
ATOM   9588  C  C     . SER B 1 503 ? 121.497 159.181 165.668 1.00 23.05 ?  503 SER B C     1 
ATOM   9589  O  O     . SER B 1 503 ? 121.860 160.107 164.933 1.00 28.92 ?  503 SER B O     1 
ATOM   9590  C  CB    . SER B 1 503 ? 121.159 156.855 164.783 1.00 18.74 ?  503 SER B CB    1 
ATOM   9591  O  OG    . SER B 1 503 ? 121.255 157.032 163.382 1.00 24.69 ?  503 SER B OG    1 
ATOM   9592  N  N     . ALA B 1 504 ? 120.583 159.349 166.626 1.00 23.24 ?  504 ALA B N     1 
ATOM   9593  C  CA    . ALA B 1 504 ? 119.981 160.657 166.857 1.00 25.89 ?  504 ALA B CA    1 
ATOM   9594  C  C     . ALA B 1 504 ? 121.005 161.656 167.380 1.00 27.48 ?  504 ALA B C     1 
ATOM   9595  O  O     . ALA B 1 504 ? 120.967 162.836 167.015 1.00 34.08 ?  504 ALA B O     1 
ATOM   9596  C  CB    . ALA B 1 504 ? 118.807 160.525 167.825 1.00 26.38 ?  504 ALA B CB    1 
ATOM   9597  N  N     . GLU B 1 505 ? 121.931 161.206 168.229 1.00 25.13 ?  505 GLU B N     1 
ATOM   9598  C  CA    . GLU B 1 505 ? 122.970 162.098 168.736 1.00 25.65 ?  505 GLU B CA    1 
ATOM   9599  C  C     . GLU B 1 505 ? 123.910 162.544 167.624 1.00 26.97 ?  505 GLU B C     1 
ATOM   9600  O  O     . GLU B 1 505 ? 124.331 163.705 167.589 1.00 31.65 ?  505 GLU B O     1 
ATOM   9601  C  CB    . GLU B 1 505 ? 123.749 161.412 169.856 1.00 26.13 ?  505 GLU B CB    1 
ATOM   9602  C  CG    . GLU B 1 505 ? 122.996 161.327 171.171 1.00 27.47 ?  505 GLU B CG    1 
ATOM   9603  C  CD    . GLU B 1 505 ? 123.544 160.252 172.085 1.00 32.39 ?  505 GLU B CD    1 
ATOM   9604  O  OE1   . GLU B 1 505 ? 124.559 159.623 171.720 1.00 31.08 ?  505 GLU B OE1   1 
ATOM   9605  O  OE2   . GLU B 1 505 ? 122.963 160.036 173.168 1.00 34.66 -1 505 GLU B OE2   1 
ATOM   9606  N  N     . ILE B 1 506 ? 124.258 161.635 166.712 1.00 26.20 ?  506 ILE B N     1 
ATOM   9607  C  CA    . ILE B 1 506 ? 125.081 162.004 165.565 1.00 26.19 ?  506 ILE B CA    1 
ATOM   9608  C  C     . ILE B 1 506 ? 124.334 162.979 164.666 1.00 26.67 ?  506 ILE B C     1 
ATOM   9609  O  O     . ILE B 1 506 ? 124.913 163.948 164.161 1.00 33.16 ?  506 ILE B O     1 
ATOM   9610  C  CB    . ILE B 1 506 ? 125.528 160.746 164.797 1.00 25.49 ?  506 ILE B CB    1 
ATOM   9611  C  CG1   . ILE B 1 506 ? 126.430 159.877 165.672 1.00 28.34 ?  506 ILE B CG1   1 
ATOM   9612  C  CG2   . ILE B 1 506 ? 126.254 161.125 163.520 1.00 24.77 ?  506 ILE B CG2   1 
ATOM   9613  C  CD1   . ILE B 1 506 ? 126.676 158.496 165.111 1.00 21.69 ?  506 ILE B CD1   1 
ATOM   9614  N  N     . ALA B 1 507 ? 123.037 162.744 164.452 1.00 26.64 ?  507 ALA B N     1 
ATOM   9615  C  CA    . ALA B 1 507 ? 122.240 163.674 163.658 1.00 28.48 ?  507 ALA B CA    1 
ATOM   9616  C  C     . ALA B 1 507 ? 122.196 165.054 164.306 1.00 32.25 ?  507 ALA B C     1 
ATOM   9617  O  O     . ALA B 1 507 ? 122.248 166.076 163.614 1.00 36.65 ?  507 ALA B O     1 
ATOM   9618  C  CB    . ALA B 1 507 ? 120.827 163.124 163.469 1.00 24.25 ?  507 ALA B CB    1 
ATOM   9619  N  N     . LYS B 1 508 ? 122.090 165.097 165.635 1.00 32.69 ?  508 LYS B N     1 
ATOM   9620  C  CA    . LYS B 1 508 ? 122.086 166.371 166.347 1.00 30.69 ?  508 LYS B CA    1 
ATOM   9621  C  C     . LYS B 1 508 ? 123.436 167.072 166.248 1.00 36.95 ?  508 LYS B C     1 
ATOM   9622  O  O     . LYS B 1 508 ? 123.496 168.285 166.016 1.00 43.58 ?  508 LYS B O     1 
ATOM   9623  C  CB    . LYS B 1 508 ? 121.707 166.140 167.809 1.00 34.62 ?  508 LYS B CB    1 
ATOM   9624  C  CG    . LYS B 1 508 ? 121.792 167.373 168.688 1.00 35.60 ?  508 LYS B CG    1 
ATOM   9625  C  CD    . LYS B 1 508 ? 121.676 166.998 170.157 1.00 34.74 ?  508 LYS B CD    1 
ATOM   9626  C  CE    . LYS B 1 508 ? 121.456 168.220 171.029 1.00 36.44 ?  508 LYS B CE    1 
ATOM   9627  N  NZ    . LYS B 1 508 ? 120.667 167.894 172.249 1.00 38.05 1  508 LYS B NZ    1 
ATOM   9628  N  N     . GLU B 1 509 ? 124.528 166.325 166.422 1.00 34.40 ?  509 GLU B N     1 
ATOM   9629  C  CA    . GLU B 1 509 ? 125.855 166.934 166.428 1.00 35.15 ?  509 GLU B CA    1 
ATOM   9630  C  C     . GLU B 1 509 ? 126.288 167.366 165.034 1.00 36.28 ?  509 GLU B C     1 
ATOM   9631  O  O     . GLU B 1 509 ? 127.095 168.292 164.898 1.00 39.64 ?  509 GLU B O     1 
ATOM   9632  C  CB    . GLU B 1 509 ? 126.869 165.963 167.037 1.00 35.08 ?  509 GLU B CB    1 
ATOM   9633  C  CG    . GLU B 1 509 ? 127.686 165.175 166.027 1.00 32.91 ?  509 GLU B CG    1 
ATOM   9634  C  CD    . GLU B 1 509 ? 128.305 163.926 166.624 1.00 41.57 ?  509 GLU B CD    1 
ATOM   9635  O  OE1   . GLU B 1 509 ? 128.246 163.764 167.862 1.00 40.77 ?  509 GLU B OE1   1 
ATOM   9636  O  OE2   . GLU B 1 509 ? 128.848 163.105 165.856 1.00 40.46 -1 509 GLU B OE2   1 
ATOM   9637  N  N     . LYS B 1 510 ? 125.770 166.717 163.991 1.00 32.33 ?  510 LYS B N     1 
ATOM   9638  C  CA    . LYS B 1 510 ? 126.090 167.085 162.620 1.00 31.26 ?  510 LYS B CA    1 
ATOM   9639  C  C     . LYS B 1 510 ? 125.008 167.930 161.962 1.00 35.37 ?  510 LYS B C     1 
ATOM   9640  O  O     . LYS B 1 510 ? 125.236 168.450 160.864 1.00 39.87 ?  510 LYS B O     1 
ATOM   9641  C  CB    . LYS B 1 510 ? 126.336 165.828 161.778 1.00 30.84 ?  510 LYS B CB    1 
ATOM   9642  C  CG    . LYS B 1 510 ? 127.413 164.917 162.337 1.00 32.21 ?  510 LYS B CG    1 
ATOM   9643  C  CD    . LYS B 1 510 ? 127.887 163.915 161.303 1.00 31.73 ?  510 LYS B CD    1 
ATOM   9644  C  CE    . LYS B 1 510 ? 129.048 163.090 161.832 1.00 33.69 ?  510 LYS B CE    1 
ATOM   9645  N  NZ    . LYS B 1 510 ? 130.031 162.767 160.764 1.00 32.53 1  510 LYS B NZ    1 
ATOM   9646  N  N     . GLY B 1 511 ? 123.849 168.079 162.599 1.00 32.71 ?  511 GLY B N     1 
ATOM   9647  C  CA    . GLY B 1 511 ? 122.773 168.862 162.029 1.00 32.43 ?  511 GLY B CA    1 
ATOM   9648  C  C     . GLY B 1 511 ? 122.148 168.282 160.783 1.00 36.03 ?  511 GLY B C     1 
ATOM   9649  O  O     . GLY B 1 511 ? 121.403 168.987 160.098 1.00 39.42 ?  511 GLY B O     1 
ATOM   9650  N  N     . GLU B 1 512 ? 122.427 167.020 160.465 1.00 33.04 ?  512 GLU B N     1 
ATOM   9651  C  CA    . GLU B 1 512 ? 121.913 166.386 159.261 1.00 29.38 ?  512 GLU B CA    1 
ATOM   9652  C  C     . GLU B 1 512 ? 121.411 164.988 159.580 1.00 31.47 ?  512 GLU B C     1 
ATOM   9653  O  O     . GLU B 1 512 ? 121.991 164.281 160.410 1.00 32.91 ?  512 GLU B O     1 
ATOM   9654  C  CB    . GLU B 1 512 ? 122.987 166.316 158.166 1.00 31.29 ?  512 GLU B CB    1 
ATOM   9655  C  CG    . GLU B 1 512 ? 124.292 165.679 158.611 1.00 31.45 ?  512 GLU B CG    1 
ATOM   9656  C  CD    . GLU B 1 512 ? 125.076 165.090 157.454 1.00 36.04 ?  512 GLU B CD    1 
ATOM   9657  O  OE1   . GLU B 1 512 ? 124.444 164.614 156.489 1.00 32.30 ?  512 GLU B OE1   1 
ATOM   9658  O  OE2   . GLU B 1 512 ? 126.324 165.102 157.511 1.00 36.73 -1 512 GLU B OE2   1 
ATOM   9659  N  N     . THR B 1 513 ? 120.327 164.600 158.921 1.00 31.96 ?  513 THR B N     1 
ATOM   9660  C  CA    . THR B 1 513 ? 119.777 163.256 158.982 1.00 26.26 ?  513 THR B CA    1 
ATOM   9661  C  C     . THR B 1 513 ? 120.054 162.545 157.662 1.00 27.02 ?  513 THR B C     1 
ATOM   9662  O  O     . THR B 1 513 ? 120.652 163.108 156.742 1.00 34.08 ?  513 THR B O     1 
ATOM   9663  C  CB    . THR B 1 513 ? 118.277 163.302 159.284 1.00 27.27 ?  513 THR B CB    1 
ATOM   9664  O  OG1   . THR B 1 513 ? 117.594 163.958 158.209 1.00 29.20 ?  513 THR B OG1   1 
ATOM   9665  C  CG2   . THR B 1 513 ? 118.019 164.060 160.573 1.00 24.46 ?  513 THR B CG2   1 
ATOM   9666  N  N     . PHE B 1 514 ? 119.616 161.293 157.569 1.00 21.67 ?  514 PHE B N     1 
ATOM   9667  C  CA    . PHE B 1 514 ? 119.737 160.608 156.295 1.00 22.78 ?  514 PHE B CA    1 
ATOM   9668  C  C     . PHE B 1 514 ? 118.671 161.115 155.329 1.00 22.05 ?  514 PHE B C     1 
ATOM   9669  O  O     . PHE B 1 514 ? 117.644 161.668 155.732 1.00 26.25 ?  514 PHE B O     1 
ATOM   9670  C  CB    . PHE B 1 514 ? 119.642 159.088 156.468 1.00 19.13 ?  514 PHE B CB    1 
ATOM   9671  C  CG    . PHE B 1 514 ? 118.310 158.599 156.966 1.00 19.25 ?  514 PHE B CG    1 
ATOM   9672  C  CD1   . PHE B 1 514 ? 118.055 158.500 158.322 1.00 17.52 ?  514 PHE B CD1   1 
ATOM   9673  C  CD2   . PHE B 1 514 ? 117.325 158.205 156.075 1.00 19.76 ?  514 PHE B CD2   1 
ATOM   9674  C  CE1   . PHE B 1 514 ? 116.840 158.035 158.779 1.00 20.16 ?  514 PHE B CE1   1 
ATOM   9675  C  CE2   . PHE B 1 514 ? 116.108 157.741 156.528 1.00 14.93 ?  514 PHE B CE2   1 
ATOM   9676  C  CZ    . PHE B 1 514 ? 115.865 157.656 157.881 1.00 21.93 ?  514 PHE B CZ    1 
ATOM   9677  N  N     . ASP B 1 515 ? 118.936 160.934 154.039 1.00 25.10 ?  515 ASP B N     1 
ATOM   9678  C  CA    . ASP B 1 515 ? 118.050 161.473 153.018 1.00 26.53 ?  515 ASP B CA    1 
ATOM   9679  C  C     . ASP B 1 515 ? 116.664 160.854 153.121 1.00 31.04 ?  515 ASP B C     1 
ATOM   9680  O  O     . ASP B 1 515 ? 116.517 159.646 153.325 1.00 40.44 ?  515 ASP B O     1 
ATOM   9681  C  CB    . ASP B 1 515 ? 118.635 161.231 151.627 1.00 29.27 ?  515 ASP B CB    1 
ATOM   9682  C  CG    . ASP B 1 515 ? 119.560 162.345 151.184 1.00 33.63 ?  515 ASP B CG    1 
ATOM   9683  O  OD1   . ASP B 1 515 ? 120.003 163.130 152.049 1.00 32.53 ?  515 ASP B OD1   1 
ATOM   9684  O  OD2   . ASP B 1 515 ? 119.845 162.437 149.973 1.00 38.46 -1 515 ASP B OD2   1 
ATOM   9685  N  N     . GLN B 1 516 ? 115.642 161.702 152.983 1.00 28.92 ?  516 GLN B N     1 
ATOM   9686  C  CA    . GLN B 1 516 ? 114.241 161.296 153.067 1.00 26.49 ?  516 GLN B CA    1 
ATOM   9687  C  C     . GLN B 1 516 ? 113.901 160.701 154.431 1.00 27.05 ?  516 GLN B C     1 
ATOM   9688  O  O     . GLN B 1 516 ? 113.057 159.810 154.536 1.00 32.99 ?  516 GLN B O     1 
ATOM   9689  C  CB    . GLN B 1 516 ? 113.876 160.311 151.954 1.00 26.22 ?  516 GLN B CB    1 
ATOM   9690  C  CG    . GLN B 1 516 ? 114.107 160.831 150.549 1.00 29.62 ?  516 GLN B CG    1 
ATOM   9691  C  CD    . GLN B 1 516 ? 113.968 159.744 149.503 1.00 32.34 ?  516 GLN B CD    1 
ATOM   9692  O  OE1   . GLN B 1 516 ? 112.861 159.304 149.192 1.00 29.80 ?  516 GLN B OE1   1 
ATOM   9693  N  NE2   . GLN B 1 516 ? 115.093 159.301 148.956 1.00 32.48 ?  516 GLN B NE2   1 
ATOM   9694  N  N     . TYR B 1 517 ? 114.554 161.185 155.490 1.00 24.80 ?  517 TYR B N     1 
ATOM   9695  C  CA    . TYR B 1 517 ? 114.217 160.713 156.828 1.00 22.80 ?  517 TYR B CA    1 
ATOM   9696  C  C     . TYR B 1 517 ? 112.822 161.162 157.246 1.00 29.59 ?  517 TYR B C     1 
ATOM   9697  O  O     . TYR B 1 517 ? 112.160 160.474 158.033 1.00 35.82 ?  517 TYR B O     1 
ATOM   9698  C  CB    . TYR B 1 517 ? 115.255 161.198 157.842 1.00 18.52 ?  517 TYR B CB    1 
ATOM   9699  C  CG    . TYR B 1 517 ? 114.695 161.399 159.233 1.00 28.00 ?  517 TYR B CG    1 
ATOM   9700  C  CD1   . TYR B 1 517 ? 114.548 160.327 160.105 1.00 23.79 ?  517 TYR B CD1   1 
ATOM   9701  C  CD2   . TYR B 1 517 ? 114.306 162.659 159.673 1.00 29.52 ?  517 TYR B CD2   1 
ATOM   9702  C  CE1   . TYR B 1 517 ? 114.031 160.504 161.371 1.00 27.50 ?  517 TYR B CE1   1 
ATOM   9703  C  CE2   . TYR B 1 517 ? 113.787 162.843 160.936 1.00 24.93 ?  517 TYR B CE2   1 
ATOM   9704  C  CZ    . TYR B 1 517 ? 113.650 161.763 161.781 1.00 27.75 ?  517 TYR B CZ    1 
ATOM   9705  O  OH    . TYR B 1 517 ? 113.136 161.946 163.043 1.00 36.93 ?  517 TYR B OH    1 
ATOM   9706  N  N     . GLU B 1 518 ? 112.357 162.300 156.726 1.00 28.16 ?  518 GLU B N     1 
ATOM   9707  C  CA    . GLU B 1 518 ? 111.102 162.882 157.191 1.00 30.08 ?  518 GLU B CA    1 
ATOM   9708  C  C     . GLU B 1 518 ? 109.911 161.975 156.909 1.00 34.42 ?  518 GLU B C     1 
ATOM   9709  O  O     . GLU B 1 518 ? 108.938 161.981 157.671 1.00 35.10 ?  518 GLU B O     1 
ATOM   9710  C  CB    . GLU B 1 518 ? 110.888 164.252 156.547 1.00 29.58 ?  518 GLU B CB    1 
ATOM   9711  C  CG    . GLU B 1 518 ? 111.947 165.290 156.898 1.00 34.09 ?  518 GLU B CG    1 
ATOM   9712  C  CD    . GLU B 1 518 ? 113.233 165.112 156.109 1.00 41.01 ?  518 GLU B CD    1 
ATOM   9713  O  OE1   . GLU B 1 518 ? 113.161 164.652 154.950 1.00 38.63 ?  518 GLU B OE1   1 
ATOM   9714  O  OE2   . GLU B 1 518 ? 114.313 165.432 156.649 1.00 38.53 -1 518 GLU B OE2   1 
ATOM   9715  N  N     . GLY B 1 519 ? 109.961 161.200 155.832 1.00 23.98 ?  519 GLY B N     1 
ATOM   9716  C  CA    . GLY B 1 519 ? 108.910 160.256 155.525 1.00 20.26 ?  519 GLY B CA    1 
ATOM   9717  C  C     . GLY B 1 519 ? 109.029 158.917 156.210 1.00 19.74 ?  519 GLY B C     1 
ATOM   9718  O  O     . GLY B 1 519 ? 108.132 158.079 156.071 1.00 28.28 ?  519 GLY B O     1 
ATOM   9719  N  N     . SER B 1 520 ? 110.109 158.685 156.948 1.00 21.17 ?  520 SER B N     1 
ATOM   9720  C  CA    . SER B 1 520 ? 110.337 157.404 157.594 1.00 22.77 ?  520 SER B CA    1 
ATOM   9721  C  C     . SER B 1 520 ? 109.476 157.264 158.845 1.00 22.36 ?  520 SER B C     1 
ATOM   9722  O  O     . SER B 1 520 ? 108.932 158.237 159.375 1.00 24.18 ?  520 SER B O     1 
ATOM   9723  C  CB    . SER B 1 520 ? 111.813 157.238 157.954 1.00 18.69 ?  520 SER B CB    1 
ATOM   9724  O  OG    . SER B 1 520 ? 112.222 158.217 158.890 1.00 23.96 ?  520 SER B OG    1 
ATOM   9725  N  N     . THR B 1 521 ? 109.353 156.020 159.314 1.00 21.97 ?  521 THR B N     1 
ATOM   9726  C  CA    . THR B 1 521 ? 108.617 155.759 160.544 1.00 18.95 ?  521 THR B CA    1 
ATOM   9727  C  C     . THR B 1 521 ? 109.357 156.268 161.773 1.00 25.21 ?  521 THR B C     1 
ATOM   9728  O  O     . THR B 1 521 ? 108.743 156.406 162.836 1.00 26.86 ?  521 THR B O     1 
ATOM   9729  C  CB    . THR B 1 521 ? 108.336 154.263 160.685 1.00 24.09 ?  521 THR B CB    1 
ATOM   9730  O  OG1   . THR B 1 521 ? 109.546 153.574 161.019 1.00 29.44 ?  521 THR B OG1   1 
ATOM   9731  C  CG2   . THR B 1 521 ? 107.786 153.704 159.386 1.00 15.63 ?  521 THR B CG2   1 
ATOM   9732  N  N     . TYR B 1 522 ? 110.659 156.540 161.656 1.00 25.01 ?  522 TYR B N     1 
ATOM   9733  C  CA    . TYR B 1 522 ? 111.376 157.192 162.746 1.00 20.83 ?  522 TYR B CA    1 
ATOM   9734  C  C     . TYR B 1 522 ? 110.871 158.613 162.958 1.00 25.33 ?  522 TYR B C     1 
ATOM   9735  O  O     . TYR B 1 522 ? 110.702 159.056 164.099 1.00 24.25 ?  522 TYR B O     1 
ATOM   9736  C  CB    . TYR B 1 522 ? 112.877 157.204 162.460 1.00 18.01 ?  522 TYR B CB    1 
ATOM   9737  C  CG    . TYR B 1 522 ? 113.521 155.839 162.409 1.00 24.21 ?  522 TYR B CG    1 
ATOM   9738  C  CD1   . TYR B 1 522 ? 113.588 155.037 163.541 1.00 24.70 ?  522 TYR B CD1   1 
ATOM   9739  C  CD2   . TYR B 1 522 ? 114.078 155.358 161.233 1.00 22.12 ?  522 TYR B CD2   1 
ATOM   9740  C  CE1   . TYR B 1 522 ? 114.182 153.792 163.497 1.00 24.61 ?  522 TYR B CE1   1 
ATOM   9741  C  CE2   . TYR B 1 522 ? 114.674 154.116 161.181 1.00 20.99 ?  522 TYR B CE2   1 
ATOM   9742  C  CZ    . TYR B 1 522 ? 114.722 153.337 162.316 1.00 22.49 ?  522 TYR B CZ    1 
ATOM   9743  O  OH    . TYR B 1 522 ? 115.315 152.098 162.266 1.00 28.05 ?  522 TYR B OH    1 
ATOM   9744  N  N     . ALA B 1 523 ? 110.625 159.342 161.866 1.00 27.79 ?  523 ALA B N     1 
ATOM   9745  C  CA    . ALA B 1 523 ? 110.175 160.725 161.977 1.00 30.41 ?  523 ALA B CA    1 
ATOM   9746  C  C     . ALA B 1 523 ? 108.736 160.804 162.470 1.00 29.48 ?  523 ALA B C     1 
ATOM   9747  O  O     . ALA B 1 523 ? 108.396 161.684 163.270 1.00 28.29 ?  523 ALA B O     1 
ATOM   9748  C  CB    . ALA B 1 523 ? 110.321 161.431 160.631 1.00 27.66 ?  523 ALA B CB    1 
ATOM   9749  N  N     . THR B 1 524 ? 107.878 159.898 162.004 1.00 26.48 ?  524 THR B N     1 
ATOM   9750  C  CA    . THR B 1 524 ? 106.475 159.907 162.393 1.00 27.99 ?  524 THR B CA    1 
ATOM   9751  C  C     . THR B 1 524 ? 106.232 159.293 163.766 1.00 33.26 ?  524 THR B C     1 
ATOM   9752  O  O     . THR B 1 524 ? 105.124 159.429 164.297 1.00 38.05 ?  524 THR B O     1 
ATOM   9753  C  CB    . THR B 1 524 ? 105.633 159.166 161.350 1.00 28.49 ?  524 THR B CB    1 
ATOM   9754  O  OG1   . THR B 1 524 ? 105.939 157.768 161.391 1.00 32.57 ?  524 THR B OG1   1 
ATOM   9755  C  CG2   . THR B 1 524 ? 105.920 159.703 159.957 1.00 27.48 ?  524 THR B CG2   1 
ATOM   9756  N  N     . GLY B 1 525 ? 107.226 158.628 164.348 1.00 25.50 ?  525 GLY B N     1 
ATOM   9757  C  CA    . GLY B 1 525 ? 107.073 157.998 165.641 1.00 23.63 ?  525 GLY B CA    1 
ATOM   9758  C  C     . GLY B 1 525 ? 106.434 156.629 165.618 1.00 26.91 ?  525 GLY B C     1 
ATOM   9759  O  O     . GLY B 1 525 ? 106.285 156.016 166.682 1.00 31.03 ?  525 GLY B O     1 
ATOM   9760  N  N     . GLU B 1 526 ? 106.050 156.129 164.441 1.00 31.40 ?  526 GLU B N     1 
ATOM   9761  C  CA    . GLU B 1 526 ? 105.432 154.809 164.360 1.00 30.90 ?  526 GLU B CA    1 
ATOM   9762  C  C     . GLU B 1 526 ? 106.412 153.715 164.762 1.00 31.91 ?  526 GLU B C     1 
ATOM   9763  O  O     . GLU B 1 526 ? 106.027 152.734 165.411 1.00 36.63 ?  526 GLU B O     1 
ATOM   9764  C  CB    . GLU B 1 526 ? 104.901 154.575 162.945 1.00 29.22 ?  526 GLU B CB    1 
ATOM   9765  C  CG    . GLU B 1 526 ? 104.533 153.134 162.637 1.00 33.58 ?  526 GLU B CG    1 
ATOM   9766  C  CD    . GLU B 1 526 ? 104.401 152.874 161.151 1.00 39.33 ?  526 GLU B CD    1 
ATOM   9767  O  OE1   . GLU B 1 526 ? 103.849 153.740 160.440 1.00 39.85 ?  526 GLU B OE1   1 
ATOM   9768  O  OE2   . GLU B 1 526 ? 104.853 151.804 160.690 1.00 35.42 -1 526 GLU B OE2   1 
ATOM   9769  N  N     . TYR B 1 527 ? 107.689 153.876 164.399 1.00 33.11 ?  527 TYR B N     1 
ATOM   9770  C  CA    . TYR B 1 527 ? 108.693 152.856 164.684 1.00 22.71 ?  527 TYR B CA    1 
ATOM   9771  C  C     . TYR B 1 527 ? 108.760 152.531 166.170 1.00 25.58 ?  527 TYR B C     1 
ATOM   9772  O  O     . TYR B 1 527 ? 109.007 151.383 166.554 1.00 30.15 ?  527 TYR B O     1 
ATOM   9773  C  CB    . TYR B 1 527 ? 110.062 153.320 164.185 1.00 18.10 ?  527 TYR B CB    1 
ATOM   9774  C  CG    . TYR B 1 527 ? 111.173 152.326 164.435 1.00 26.66 ?  527 TYR B CG    1 
ATOM   9775  C  CD1   . TYR B 1 527 ? 111.461 151.337 163.506 1.00 26.45 ?  527 TYR B CD1   1 
ATOM   9776  C  CD2   . TYR B 1 527 ? 111.928 152.372 165.599 1.00 24.18 ?  527 TYR B CD2   1 
ATOM   9777  C  CE1   . TYR B 1 527 ? 112.470 150.425 163.725 1.00 23.64 ?  527 TYR B CE1   1 
ATOM   9778  C  CE2   . TYR B 1 527 ? 112.937 151.461 165.828 1.00 19.65 ?  527 TYR B CE2   1 
ATOM   9779  C  CZ    . TYR B 1 527 ? 113.204 150.492 164.888 1.00 20.98 ?  527 TYR B CZ    1 
ATOM   9780  O  OH    . TYR B 1 527 ? 114.211 149.582 165.111 1.00 30.81 ?  527 TYR B OH    1 
ATOM   9781  N  N     . PHE B 1 528 ? 108.546 153.529 167.020 1.00 29.04 ?  528 PHE B N     1 
ATOM   9782  C  CA    . PHE B 1 528 ? 108.659 153.364 168.461 1.00 26.61 ?  528 PHE B CA    1 
ATOM   9783  C  C     . PHE B 1 528 ? 107.386 152.834 169.105 1.00 33.94 ?  528 PHE B C     1 
ATOM   9784  O  O     . PHE B 1 528 ? 107.354 152.684 170.330 1.00 38.82 ?  528 PHE B O     1 
ATOM   9785  C  CB    . PHE B 1 528 ? 109.043 154.696 169.112 1.00 27.80 ?  528 PHE B CB    1 
ATOM   9786  C  CG    . PHE B 1 528 ? 110.291 155.310 168.548 1.00 29.99 ?  528 PHE B CG    1 
ATOM   9787  C  CD1   . PHE B 1 528 ? 111.531 154.999 169.077 1.00 26.60 ?  528 PHE B CD1   1 
ATOM   9788  C  CD2   . PHE B 1 528 ? 110.224 156.200 167.489 1.00 25.41 ?  528 PHE B CD2   1 
ATOM   9789  C  CE1   . PHE B 1 528 ? 112.681 155.562 168.561 1.00 28.91 ?  528 PHE B CE1   1 
ATOM   9790  C  CE2   . PHE B 1 528 ? 111.370 156.765 166.969 1.00 27.68 ?  528 PHE B CE2   1 
ATOM   9791  C  CZ    . PHE B 1 528 ? 112.600 156.445 167.506 1.00 27.60 ?  528 PHE B CZ    1 
ATOM   9792  N  N     . ASP B 1 529 ? 106.348 152.546 168.313 1.00 31.57 ?  529 ASP B N     1 
ATOM   9793  C  CA    . ASP B 1 529 ? 105.061 152.135 168.869 1.00 31.29 ?  529 ASP B CA    1 
ATOM   9794  C  C     . ASP B 1 529 ? 105.215 150.960 169.829 1.00 32.79 ?  529 ASP B C     1 
ATOM   9795  O  O     . ASP B 1 529 ? 104.932 151.077 171.029 1.00 37.04 ?  529 ASP B O     1 
ATOM   9796  C  CB    . ASP B 1 529 ? 104.100 151.779 167.733 1.00 31.85 ?  529 ASP B CB    1 
ATOM   9797  C  CG    . ASP B 1 529 ? 103.467 153.002 167.103 1.00 33.93 ?  529 ASP B CG    1 
ATOM   9798  O  OD1   . ASP B 1 529 ? 103.669 154.115 167.631 1.00 36.54 ?  529 ASP B OD1   1 
ATOM   9799  O  OD2   . ASP B 1 529 ? 102.770 152.849 166.078 1.00 36.46 -1 529 ASP B OD2   1 
ATOM   9800  N  N     . LYS B 1 530 ? 105.701 149.824 169.323 1.00 34.54 ?  530 LYS B N     1 
ATOM   9801  C  CA    . LYS B 1 530 ? 105.872 148.649 170.168 1.00 34.43 ?  530 LYS B CA    1 
ATOM   9802  C  C     . LYS B 1 530 ? 106.852 148.897 171.304 1.00 36.06 ?  530 LYS B C     1 
ATOM   9803  O  O     . LYS B 1 530 ? 106.840 148.157 172.293 1.00 36.80 ?  530 LYS B O     1 
ATOM   9804  C  CB    . LYS B 1 530 ? 106.341 147.459 169.331 1.00 33.22 ?  530 LYS B CB    1 
ATOM   9805  C  CG    . LYS B 1 530 ? 107.849 147.279 169.302 1.00 31.06 ?  530 LYS B CG    1 
ATOM   9806  C  CD    . LYS B 1 530 ? 108.278 146.358 168.180 1.00 32.94 ?  530 LYS B CD    1 
ATOM   9807  C  CE    . LYS B 1 530 ? 109.770 146.107 168.229 1.00 31.12 ?  530 LYS B CE    1 
ATOM   9808  N  NZ    . LYS B 1 530 ? 110.407 146.323 166.901 1.00 37.43 1  530 LYS B NZ    1 
ATOM   9809  N  N     . TYR B 1 531 ? 107.697 149.919 171.190 1.00 35.29 ?  531 TYR B N     1 
ATOM   9810  C  CA    . TYR B 1 531 ? 108.643 150.237 172.246 1.00 28.42 ?  531 TYR B CA    1 
ATOM   9811  C  C     . TYR B 1 531 ? 108.072 151.179 173.293 1.00 29.68 ?  531 TYR B C     1 
ATOM   9812  O  O     . TYR B 1 531 ? 108.625 151.263 174.395 1.00 33.16 ?  531 TYR B O     1 
ATOM   9813  C  CB    . TYR B 1 531 ? 109.912 150.845 171.646 1.00 27.04 ?  531 TYR B CB    1 
ATOM   9814  C  CG    . TYR B 1 531 ? 110.798 149.836 170.956 1.00 28.11 ?  531 TYR B CG    1 
ATOM   9815  C  CD1   . TYR B 1 531 ? 111.275 148.725 171.635 1.00 25.95 ?  531 TYR B CD1   1 
ATOM   9816  C  CD2   . TYR B 1 531 ? 111.158 149.996 169.625 1.00 27.49 ?  531 TYR B CD2   1 
ATOM   9817  C  CE1   . TYR B 1 531 ? 112.087 147.801 171.011 1.00 28.69 ?  531 TYR B CE1   1 
ATOM   9818  C  CE2   . TYR B 1 531 ? 111.969 149.076 168.992 1.00 23.66 ?  531 TYR B CE2   1 
ATOM   9819  C  CZ    . TYR B 1 531 ? 112.430 147.981 169.690 1.00 28.29 ?  531 TYR B CZ    1 
ATOM   9820  O  OH    . TYR B 1 531 ? 113.237 147.063 169.064 1.00 32.32 ?  531 TYR B OH    1 
ATOM   9821  N  N     . VAL B 1 532 ? 106.980 151.885 172.984 1.00 33.72 ?  532 VAL B N     1 
ATOM   9822  C  CA    . VAL B 1 532 ? 106.359 152.782 173.952 1.00 31.71 ?  532 VAL B CA    1 
ATOM   9823  C  C     . VAL B 1 532 ? 105.108 152.186 174.573 1.00 34.87 ?  532 VAL B C     1 
ATOM   9824  O  O     . VAL B 1 532 ? 104.415 152.875 175.334 1.00 40.13 ?  532 VAL B O     1 
ATOM   9825  C  CB    . VAL B 1 532 ? 106.040 154.154 173.319 1.00 34.38 ?  532 VAL B CB    1 
ATOM   9826  C  CG1   . VAL B 1 532 ? 107.310 154.810 172.803 1.00 32.64 ?  532 VAL B CG1   1 
ATOM   9827  C  CG2   . VAL B 1 532 ? 105.013 154.010 172.208 1.00 34.61 ?  532 VAL B CG2   1 
ATOM   9828  N  N     . SER B 1 533 ? 104.798 150.924 174.277 1.00 40.20 ?  533 SER B N     1 
ATOM   9829  C  CA    . SER B 1 533 ? 103.606 150.283 174.813 1.00 39.75 ?  533 SER B CA    1 
ATOM   9830  C  C     . SER B 1 533 ? 103.944 148.933 175.432 1.00 40.09 ?  533 SER B C     1 
ATOM   9831  O  O     . SER B 1 533 ? 103.236 148.459 176.327 1.00 44.55 ?  533 SER B O     1 
ATOM   9832  C  CB    . SER B 1 533 ? 102.554 150.116 173.715 1.00 41.09 ?  533 SER B CB    1 
ATOM   9833  O  OG    . SER B 1 533 ? 102.943 149.118 172.788 1.00 42.45 ?  533 SER B OG    1 
ATOM   9834  N  N     . THR B 1 534 ? 105.019 148.309 174.964 1.00 39.24 ?  534 THR B N     1 
ATOM   9835  C  CA    . THR B 1 534 ? 105.442 147.000 175.440 1.00 38.89 ?  534 THR B CA    1 
ATOM   9836  C  C     . THR B 1 534 ? 106.767 147.119 176.180 1.00 37.46 ?  534 THR B C     1 
ATOM   9837  O  O     . THR B 1 534 ? 107.682 147.814 175.727 1.00 43.15 ?  534 THR B O     1 
ATOM   9838  C  CB    . THR B 1 534 ? 105.581 146.007 174.282 1.00 39.21 ?  534 THR B CB    1 
ATOM   9839  O  OG1   . THR B 1 534 ? 104.403 146.051 173.468 1.00 40.92 ?  534 THR B OG1   1 
ATOM   9840  C  CG2   . THR B 1 534 ? 105.777 144.592 174.807 1.00 40.55 ?  534 THR B CG2   1 
ATOM   9841  N  N     . ASP B 1 535 ? 106.861 146.439 177.318 1.00 42.63 ?  535 ASP B N     1 
ATOM   9842  C  CA    . ASP B 1 535 ? 108.079 146.419 178.113 1.00 41.49 ?  535 ASP B CA    1 
ATOM   9843  C  C     . ASP B 1 535 ? 108.908 145.195 177.746 1.00 41.07 ?  535 ASP B C     1 
ATOM   9844  O  O     . ASP B 1 535 ? 108.396 144.071 177.736 1.00 42.97 ?  535 ASP B O     1 
ATOM   9845  C  CB    . ASP B 1 535 ? 107.744 146.411 179.606 1.00 38.42 ?  535 ASP B CB    1 
ATOM   9846  C  CG    . ASP B 1 535 ? 108.967 146.220 180.476 1.00 44.29 ?  535 ASP B CG    1 
ATOM   9847  O  OD1   . ASP B 1 535 ? 109.649 147.222 180.776 1.00 47.58 ?  535 ASP B OD1   1 
ATOM   9848  O  OD2   . ASP B 1 535 ? 109.240 145.065 180.863 1.00 46.27 -1 535 ASP B OD2   1 
ATOM   9849  N  N     . PHE B 1 536 ? 110.186 145.417 177.444 1.00 32.24 ?  536 PHE B N     1 
ATOM   9850  C  CA    . PHE B 1 536 ? 111.084 144.351 177.020 1.00 32.66 ?  536 PHE B CA    1 
ATOM   9851  C  C     . PHE B 1 536 ? 112.107 143.997 178.094 1.00 33.90 ?  536 PHE B C     1 
ATOM   9852  O  O     . PHE B 1 536 ? 113.162 143.436 177.781 1.00 35.05 ?  536 PHE B O     1 
ATOM   9853  C  CB    . PHE B 1 536 ? 111.782 144.736 175.716 1.00 29.99 ?  536 PHE B CB    1 
ATOM   9854  C  CG    . PHE B 1 536 ? 110.845 144.879 174.552 1.00 27.01 ?  536 PHE B CG    1 
ATOM   9855  C  CD1   . PHE B 1 536 ? 110.543 143.791 173.751 1.00 28.60 ?  536 PHE B CD1   1 
ATOM   9856  C  CD2   . PHE B 1 536 ? 110.257 146.099 174.263 1.00 30.83 ?  536 PHE B CD2   1 
ATOM   9857  C  CE1   . PHE B 1 536 ? 109.679 143.917 172.682 1.00 30.63 ?  536 PHE B CE1   1 
ATOM   9858  C  CE2   . PHE B 1 536 ? 109.391 146.231 173.196 1.00 35.58 ?  536 PHE B CE2   1 
ATOM   9859  C  CZ    . PHE B 1 536 ? 109.102 145.139 172.404 1.00 32.38 ?  536 PHE B CZ    1 
ATOM   9860  N  N     . SER B 1 537 ? 111.816 144.316 179.351 1.00 35.74 ?  537 SER B N     1 
ATOM   9861  C  CA    . SER B 1 537 ? 112.661 143.875 180.445 1.00 33.49 ?  537 SER B CA    1 
ATOM   9862  C  C     . SER B 1 537 ? 112.551 142.359 180.603 1.00 37.92 ?  537 SER B C     1 
ATOM   9863  O  O     . SER B 1 537 ? 111.533 141.764 180.240 1.00 39.77 ?  537 SER B O     1 
ATOM   9864  C  CB    . SER B 1 537 ? 112.260 144.569 181.744 1.00 35.62 ?  537 SER B CB    1 
ATOM   9865  O  OG    . SER B 1 537 ? 112.289 145.978 181.596 1.00 41.80 ?  537 SER B OG    1 
ATOM   9866  N  N     . PRO B 1 538 ? 113.591 141.709 181.123 1.00 35.53 ?  538 PRO B N     1 
ATOM   9867  C  CA    . PRO B 1 538 ? 113.559 140.246 181.235 1.00 34.54 ?  538 PRO B CA    1 
ATOM   9868  C  C     . PRO B 1 538 ? 112.411 139.766 182.112 1.00 38.77 ?  538 PRO B C     1 
ATOM   9869  O  O     . PRO B 1 538 ? 112.127 140.336 183.167 1.00 41.83 ?  538 PRO B O     1 
ATOM   9870  C  CB    . PRO B 1 538 ? 114.920 139.908 181.856 1.00 36.06 ?  538 PRO B CB    1 
ATOM   9871  C  CG    . PRO B 1 538 ? 115.780 141.087 181.562 1.00 37.65 ?  538 PRO B CG    1 
ATOM   9872  C  CD    . PRO B 1 538 ? 114.866 142.267 181.602 1.00 35.67 ?  538 PRO B CD    1 
ATOM   9873  N  N     . LYS B 1 539 ? 111.753 138.701 181.659 1.00 41.02 ?  539 LYS B N     1 
ATOM   9874  C  CA    . LYS B 1 539 ? 110.667 138.081 182.404 1.00 41.05 ?  539 LYS B CA    1 
ATOM   9875  C  C     . LYS B 1 539 ? 111.144 136.995 183.357 1.00 44.29 ?  539 LYS B C     1 
ATOM   9876  O  O     . LYS B 1 539 ? 110.351 136.519 184.175 1.00 47.25 ?  539 LYS B O     1 
ATOM   9877  C  CB    . LYS B 1 539 ? 109.634 137.490 181.439 1.00 42.03 ?  539 LYS B CB    1 
ATOM   9878  C  CG    . LYS B 1 539 ? 109.410 138.320 180.188 1.00 42.44 ?  539 LYS B CG    1 
ATOM   9879  C  CD    . LYS B 1 539 ? 108.183 139.205 180.327 1.00 42.09 ?  539 LYS B CD    1 
ATOM   9880  C  CE    . LYS B 1 539 ? 107.945 140.018 179.066 1.00 44.54 ?  539 LYS B CE    1 
ATOM   9881  N  NZ    . LYS B 1 539 ? 109.195 140.671 178.585 1.00 45.96 1  539 LYS B NZ    1 
ATOM   9882  N  N     . TYR B 1 540 ? 112.409 136.597 183.272 1.00 42.27 ?  540 TYR B N     1 
ATOM   9883  C  CA    . TYR B 1 540 ? 112.977 135.569 184.129 1.00 39.72 ?  540 TYR B CA    1 
ATOM   9884  C  C     . TYR B 1 540 ? 113.999 136.192 185.068 1.00 46.19 ?  540 TYR B C     1 
ATOM   9885  O  O     . TYR B 1 540 ? 114.724 137.116 184.688 1.00 47.07 ?  540 TYR B O     1 
ATOM   9886  C  CB    . TYR B 1 540 ? 113.626 134.459 183.298 1.00 41.89 ?  540 TYR B CB    1 
ATOM   9887  C  CG    . TYR B 1 540 ? 112.640 133.664 182.474 1.00 45.05 ?  540 TYR B CG    1 
ATOM   9888  C  CD1   . TYR B 1 540 ? 112.285 134.073 181.195 1.00 42.64 ?  540 TYR B CD1   1 
ATOM   9889  C  CD2   . TYR B 1 540 ? 112.056 132.510 182.978 1.00 45.24 ?  540 TYR B CD2   1 
ATOM   9890  C  CE1   . TYR B 1 540 ? 111.380 133.351 180.440 1.00 42.42 ?  540 TYR B CE1   1 
ATOM   9891  C  CE2   . TYR B 1 540 ? 111.152 131.782 182.231 1.00 42.26 ?  540 TYR B CE2   1 
ATOM   9892  C  CZ    . TYR B 1 540 ? 110.818 132.206 180.963 1.00 43.92 ?  540 TYR B CZ    1 
ATOM   9893  O  OH    . TYR B 1 540 ? 109.916 131.483 180.217 1.00 46.28 ?  540 TYR B OH    1 
ATOM   9894  N  N     . GLU B 1 541 ? 114.045 135.683 186.302 1.00 49.66 ?  541 GLU B N     1 
ATOM   9895  C  CA    . GLU B 1 541 ? 114.952 136.241 187.300 1.00 45.98 ?  541 GLU B CA    1 
ATOM   9896  C  C     . GLU B 1 541 ? 116.409 136.034 186.905 1.00 46.37 ?  541 GLU B C     1 
ATOM   9897  O  O     . GLU B 1 541 ? 117.255 136.898 187.159 1.00 45.04 ?  541 GLU B O     1 
ATOM   9898  C  CB    . GLU B 1 541 ? 114.675 135.620 188.669 1.00 46.69 ?  541 GLU B CB    1 
ATOM   9899  C  CG    . GLU B 1 541 ? 115.333 136.358 189.822 1.00 48.66 ?  541 GLU B CG    1 
ATOM   9900  C  CD    . GLU B 1 541 ? 115.122 137.857 189.751 1.00 50.84 ?  541 GLU B CD    1 
ATOM   9901  O  OE1   . GLU B 1 541 ? 113.954 138.293 189.702 1.00 50.80 ?  541 GLU B OE1   1 
ATOM   9902  O  OE2   . GLU B 1 541 ? 116.126 138.600 189.738 1.00 52.89 -1 541 GLU B OE2   1 
ATOM   9903  N  N     . LYS B 1 542 ? 116.724 134.889 186.295 1.00 42.48 ?  542 LYS B N     1 
ATOM   9904  C  CA    . LYS B 1 542 ? 118.100 134.623 185.884 1.00 39.80 ?  542 LYS B CA    1 
ATOM   9905  C  C     . LYS B 1 542 ? 118.573 135.633 184.847 1.00 42.82 ?  542 LYS B C     1 
ATOM   9906  O  O     . LYS B 1 542 ? 119.698 136.139 184.928 1.00 44.21 ?  542 LYS B O     1 
ATOM   9907  C  CB    . LYS B 1 542 ? 118.215 133.198 185.342 1.00 38.45 ?  542 LYS B CB    1 
ATOM   9908  C  CG    . LYS B 1 542 ? 119.626 132.788 184.958 1.00 43.63 ?  542 LYS B CG    1 
ATOM   9909  C  CD    . LYS B 1 542 ? 119.676 131.332 184.529 1.00 42.93 ?  542 LYS B CD    1 
ATOM   9910  C  CE    . LYS B 1 542 ? 121.106 130.876 184.295 1.00 43.45 ?  542 LYS B CE    1 
ATOM   9911  N  NZ    . LYS B 1 542 ? 121.195 129.406 184.082 1.00 41.95 1  542 LYS B NZ    1 
ATOM   9912  N  N     . ILE B 1 543 ? 117.722 135.951 183.871 1.00 39.40 ?  543 ILE B N     1 
ATOM   9913  C  CA    . ILE B 1 543 ? 118.094 136.927 182.851 1.00 37.20 ?  543 ILE B CA    1 
ATOM   9914  C  C     . ILE B 1 543 ? 118.228 138.317 183.461 1.00 36.34 ?  543 ILE B C     1 
ATOM   9915  O  O     . ILE B 1 543 ? 119.136 139.081 183.109 1.00 39.33 ?  543 ILE B O     1 
ATOM   9916  C  CB    . ILE B 1 543 ? 117.073 136.905 181.701 1.00 36.93 ?  543 ILE B CB    1 
ATOM   9917  C  CG1   . ILE B 1 543 ? 116.865 135.473 181.200 1.00 36.34 ?  543 ILE B CG1   1 
ATOM   9918  C  CG2   . ILE B 1 543 ? 117.533 137.801 180.573 1.00 35.21 ?  543 ILE B CG2   1 
ATOM   9919  C  CD1   . ILE B 1 543 ? 118.146 134.768 180.804 1.00 34.56 ?  543 ILE B CD1   1 
ATOM   9920  N  N     . ALA B 1 544 ? 117.326 138.672 184.381 1.00 37.78 ?  544 ALA B N     1 
ATOM   9921  C  CA    . ALA B 1 544 ? 117.424 139.964 185.052 1.00 40.15 ?  544 ALA B CA    1 
ATOM   9922  C  C     . ALA B 1 544 ? 118.725 140.078 185.836 1.00 39.96 ?  544 ALA B C     1 
ATOM   9923  O  O     . ALA B 1 544 ? 119.367 141.135 185.837 1.00 42.67 ?  544 ALA B O     1 
ATOM   9924  C  CB    . ALA B 1 544 ? 116.221 140.170 185.972 1.00 41.98 ?  544 ALA B CB    1 
ATOM   9925  N  N     . ASN B 1 545 ? 119.129 139.000 186.511 1.00 43.77 ?  545 ASN B N     1 
ATOM   9926  C  CA    . ASN B 1 545 ? 120.420 138.989 187.190 1.00 47.64 ?  545 ASN B CA    1 
ATOM   9927  C  C     . ASN B 1 545 ? 121.564 139.117 186.193 1.00 45.05 ?  545 ASN B C     1 
ATOM   9928  O  O     . ASN B 1 545 ? 122.566 139.787 186.468 1.00 46.84 ?  545 ASN B O     1 
ATOM   9929  C  CB    . ASN B 1 545 ? 120.568 137.712 188.018 1.00 44.49 ?  545 ASN B CB    1 
ATOM   9930  C  CG    . ASN B 1 545 ? 119.586 137.649 189.168 1.00 47.52 ?  545 ASN B CG    1 
ATOM   9931  O  OD1   . ASN B 1 545 ? 119.085 138.676 189.628 1.00 49.39 ?  545 ASN B OD1   1 
ATOM   9932  N  ND2   . ASN B 1 545 ? 119.303 136.441 189.639 1.00 44.45 ?  545 ASN B ND2   1 
ATOM   9933  N  N     . LEU B 1 546 ? 121.437 138.466 185.034 1.00 38.60 ?  546 LEU B N     1 
ATOM   9934  C  CA    . LEU B 1 546 ? 122.431 138.625 183.979 1.00 39.55 ?  546 LEU B CA    1 
ATOM   9935  C  C     . LEU B 1 546 ? 122.555 140.078 183.542 1.00 39.47 ?  546 LEU B C     1 
ATOM   9936  O  O     . LEU B 1 546 ? 123.653 140.533 183.203 1.00 39.00 ?  546 LEU B O     1 
ATOM   9937  C  CB    . LEU B 1 546 ? 122.071 137.743 182.784 1.00 36.75 ?  546 LEU B CB    1 
ATOM   9938  C  CG    . LEU B 1 546 ? 122.507 136.280 182.846 1.00 39.09 ?  546 LEU B CG    1 
ATOM   9939  C  CD1   . LEU B 1 546 ? 122.485 135.669 181.458 1.00 37.33 ?  546 LEU B CD1   1 
ATOM   9940  C  CD2   . LEU B 1 546 ? 123.889 136.155 183.468 1.00 38.77 ?  546 LEU B CD2   1 
ATOM   9941  N  N     . PHE B 1 547 ? 121.449 140.818 183.549 1.00 40.07 ?  547 PHE B N     1 
ATOM   9942  C  CA    . PHE B 1 547 ? 121.443 142.219 183.154 1.00 37.64 ?  547 PHE B CA    1 
ATOM   9943  C  C     . PHE B 1 547 ? 121.658 143.173 184.323 1.00 39.81 ?  547 PHE B C     1 
ATOM   9944  O  O     . PHE B 1 547 ? 121.444 144.379 184.165 1.00 43.53 ?  547 PHE B O     1 
ATOM   9945  C  CB    . PHE B 1 547 ? 120.130 142.562 182.447 1.00 35.49 ?  547 PHE B CB    1 
ATOM   9946  C  CG    . PHE B 1 547 ? 120.080 142.125 181.015 1.00 36.65 ?  547 PHE B CG    1 
ATOM   9947  C  CD1   . PHE B 1 547 ? 120.717 142.860 180.032 1.00 35.91 ?  547 PHE B CD1   1 
ATOM   9948  C  CD2   . PHE B 1 547 ? 119.396 140.979 180.649 1.00 35.72 ?  547 PHE B CD2   1 
ATOM   9949  C  CE1   . PHE B 1 547 ? 120.673 142.462 178.713 1.00 34.64 ?  547 PHE B CE1   1 
ATOM   9950  C  CE2   . PHE B 1 547 ? 119.350 140.577 179.332 1.00 36.03 ?  547 PHE B CE2   1 
ATOM   9951  C  CZ    . PHE B 1 547 ? 119.990 141.318 178.363 1.00 35.01 ?  547 PHE B CZ    1 
ATOM   9952  N  N     . GLU B 1 548 ? 122.068 142.669 185.483 1.00 47.04 ?  548 GLU B N     1 
ATOM   9953  C  CA    . GLU B 1 548 ? 122.303 143.535 186.630 1.00 47.44 ?  548 GLU B CA    1 
ATOM   9954  C  C     . GLU B 1 548 ? 123.502 144.445 186.386 1.00 47.26 ?  548 GLU B C     1 
ATOM   9955  O  O     . GLU B 1 548 ? 124.447 144.091 185.676 1.00 50.56 ?  548 GLU B O     1 
ATOM   9956  C  CB    . GLU B 1 548 ? 122.524 142.710 187.897 1.00 46.82 ?  548 GLU B CB    1 
ATOM   9957  C  CG    . GLU B 1 548 ? 121.243 142.217 188.550 1.00 48.12 ?  548 GLU B CG    1 
ATOM   9958  C  CD    . GLU B 1 548 ? 120.318 143.346 188.970 1.00 50.79 ?  548 GLU B CD    1 
ATOM   9959  O  OE1   . GLU B 1 548 ? 120.809 144.465 189.228 1.00 48.80 ?  548 GLU B OE1   1 
ATOM   9960  O  OE2   . GLU B 1 548 ? 119.094 143.111 189.044 1.00 50.91 -1 548 GLU B OE2   1 
ATOM   9961  N  N     . GLY B 1 549 ? 123.452 145.630 186.988 1.00 45.31 ?  549 GLY B N     1 
ATOM   9962  C  CA    . GLY B 1 549 ? 124.463 146.639 186.769 1.00 44.97 ?  549 GLY B CA    1 
ATOM   9963  C  C     . GLY B 1 549 ? 124.293 147.437 185.499 1.00 46.10 ?  549 GLY B C     1 
ATOM   9964  O  O     . GLY B 1 549 ? 125.157 148.267 185.187 1.00 47.53 ?  549 GLY B O     1 
ATOM   9965  N  N     . MET B 1 550 ? 123.211 147.215 184.757 1.00 45.44 ?  550 MET B N     1 
ATOM   9966  C  CA    . MET B 1 550 ? 122.954 147.900 183.499 1.00 44.20 ?  550 MET B CA    1 
ATOM   9967  C  C     . MET B 1 550 ? 121.514 148.385 183.491 1.00 44.33 ?  550 MET B C     1 
ATOM   9968  O  O     . MET B 1 550 ? 120.605 147.642 183.875 1.00 46.15 ?  550 MET B O     1 
ATOM   9969  C  CB    . MET B 1 550 ? 123.214 146.971 182.310 1.00 43.15 ?  550 MET B CB    1 
ATOM   9970  C  CG    . MET B 1 550 ? 124.455 147.321 181.517 1.00 48.10 ?  550 MET B CG    1 
ATOM   9971  S  SD    . MET B 1 550 ? 124.531 146.441 179.950 1.00 54.89 ?  550 MET B SD    1 
ATOM   9972  C  CE    . MET B 1 550 ? 124.544 144.741 180.510 1.00 44.40 ?  550 MET B CE    1 
ATOM   9973  N  N     . HIS B 1 551 ? 121.306 149.624 183.054 1.00 40.63 ?  551 HIS B N     1 
ATOM   9974  C  CA    . HIS B 1 551 ? 119.975 150.221 183.043 1.00 40.60 ?  551 HIS B CA    1 
ATOM   9975  C  C     . HIS B 1 551 ? 119.213 149.741 181.814 1.00 40.33 ?  551 HIS B C     1 
ATOM   9976  O  O     . HIS B 1 551 ? 119.453 150.218 180.701 1.00 41.37 ?  551 HIS B O     1 
ATOM   9977  C  CB    . HIS B 1 551 ? 120.067 151.743 183.061 1.00 39.84 ?  551 HIS B CB    1 
ATOM   9978  C  CG    . HIS B 1 551 ? 118.770 152.424 182.754 1.00 41.55 ?  551 HIS B CG    1 
ATOM   9979  N  ND1   . HIS B 1 551 ? 117.696 152.402 183.616 1.00 44.88 ?  551 HIS B ND1   1 
ATOM   9980  C  CD2   . HIS B 1 551 ? 118.372 153.137 181.674 1.00 41.27 ?  551 HIS B CD2   1 
ATOM   9981  C  CE1   . HIS B 1 551 ? 116.693 153.075 183.083 1.00 43.33 ?  551 HIS B CE1   1 
ATOM   9982  N  NE2   . HIS B 1 551 ? 117.076 153.531 181.904 1.00 40.71 ?  551 HIS B NE2   1 
ATOM   9983  N  N     . ILE B 1 552 ? 118.285 148.812 182.017 1.00 35.98 ?  552 ILE B N     1 
ATOM   9984  C  CA    . ILE B 1 552 ? 117.447 148.301 180.936 1.00 32.38 ?  552 ILE B CA    1 
ATOM   9985  C  C     . ILE B 1 552 ? 116.414 149.363 180.581 1.00 33.83 ?  552 ILE B C     1 
ATOM   9986  O  O     . ILE B 1 552 ? 115.642 149.789 181.453 1.00 38.54 ?  552 ILE B O     1 
ATOM   9987  C  CB    . ILE B 1 552 ? 116.772 146.979 181.335 1.00 35.25 ?  552 ILE B CB    1 
ATOM   9988  C  CG1   . ILE B 1 552 ? 117.826 145.947 181.736 1.00 34.38 ?  552 ILE B CG1   1 
ATOM   9989  C  CG2   . ILE B 1 552 ? 115.914 146.455 180.198 1.00 35.00 ?  552 ILE B CG2   1 
ATOM   9990  C  CD1   . ILE B 1 552 ? 117.274 144.801 182.543 1.00 33.66 ?  552 ILE B CD1   1 
ATOM   9991  N  N     . PRO B 1 553 ? 116.370 149.828 179.332 1.00 37.53 ?  553 PRO B N     1 
ATOM   9992  C  CA    . PRO B 1 553 ? 115.405 150.873 178.969 1.00 34.70 ?  553 PRO B CA    1 
ATOM   9993  C  C     . PRO B 1 553 ? 113.971 150.396 179.144 1.00 35.12 ?  553 PRO B C     1 
ATOM   9994  O  O     . PRO B 1 553 ? 113.622 149.267 178.794 1.00 37.86 ?  553 PRO B O     1 
ATOM   9995  C  CB    . PRO B 1 553 ? 115.726 151.158 177.498 1.00 32.01 ?  553 PRO B CB    1 
ATOM   9996  C  CG    . PRO B 1 553 ? 117.123 150.666 177.306 1.00 30.36 ?  553 PRO B CG    1 
ATOM   9997  C  CD    . PRO B 1 553 ? 117.262 149.487 178.213 1.00 32.54 ?  553 PRO B CD    1 
ATOM   9998  N  N     . THR B 1 554 ? 113.140 151.274 179.690 1.00 39.81 ?  554 THR B N     1 
ATOM   9999  C  CA    . THR B 1 554 ? 111.728 151.007 179.886 1.00 38.48 ?  554 THR B CA    1 
ATOM   10000 C  C     . THR B 1 554 ? 110.920 151.759 178.832 1.00 36.43 ?  554 THR B C     1 
ATOM   10001 O  O     . THR B 1 554 ? 111.471 152.356 177.902 1.00 36.73 ?  554 THR B O     1 
ATOM   10002 C  CB    . THR B 1 554 ? 111.311 151.390 181.307 1.00 38.13 ?  554 THR B CB    1 
ATOM   10003 O  OG1   . THR B 1 554 ? 111.506 152.795 181.501 1.00 37.11 ?  554 THR B OG1   1 
ATOM   10004 C  CG2   . THR B 1 554 ? 112.138 150.623 182.329 1.00 36.24 ?  554 THR B CG2   1 
ATOM   10005 N  N     . THR B 1 555 ? 109.592 151.731 178.969 1.00 39.09 ?  555 THR B N     1 
ATOM   10006 C  CA    . THR B 1 555 ? 108.748 152.469 178.037 1.00 36.65 ?  555 THR B CA    1 
ATOM   10007 C  C     . THR B 1 555 ? 108.957 153.973 178.161 1.00 39.53 ?  555 THR B C     1 
ATOM   10008 O  O     . THR B 1 555 ? 108.800 154.699 177.174 1.00 40.35 ?  555 THR B O     1 
ATOM   10009 C  CB    . THR B 1 555 ? 107.276 152.120 178.261 1.00 38.95 ?  555 THR B CB    1 
ATOM   10010 O  OG1   . THR B 1 555 ? 106.927 152.363 179.629 1.00 44.10 ?  555 THR B OG1   1 
ATOM   10011 C  CG2   . THR B 1 555 ? 107.021 150.658 177.926 1.00 39.39 ?  555 THR B CG2   1 
ATOM   10012 N  N     . GLU B 1 556 ? 109.310 154.458 179.354 1.00 37.71 ?  556 GLU B N     1 
ATOM   10013 C  CA    . GLU B 1 556 ? 109.572 155.884 179.523 1.00 37.73 ?  556 GLU B CA    1 
ATOM   10014 C  C     . GLU B 1 556 ? 110.860 156.298 178.819 1.00 40.49 ?  556 GLU B C     1 
ATOM   10015 O  O     . GLU B 1 556 ? 110.908 157.352 178.171 1.00 41.86 ?  556 GLU B O     1 
ATOM   10016 C  CB    . GLU B 1 556 ? 109.638 156.231 181.009 1.00 39.97 ?  556 GLU B CB    1 
ATOM   10017 C  CG    . GLU B 1 556 ? 108.292 156.204 181.713 1.00 41.23 ?  556 GLU B CG    1 
ATOM   10018 C  CD    . GLU B 1 556 ? 107.182 156.803 180.873 1.00 44.19 ?  556 GLU B CD    1 
ATOM   10019 O  OE1   . GLU B 1 556 ? 107.199 158.032 180.652 1.00 42.40 ?  556 GLU B OE1   1 
ATOM   10020 O  OE2   . GLU B 1 556 ? 106.291 156.045 180.434 1.00 44.24 -1 556 GLU B OE2   1 
ATOM   10021 N  N     . ASP B 1 557 ? 111.913 155.488 178.939 1.00 40.06 ?  557 ASP B N     1 
ATOM   10022 C  CA    . ASP B 1 557 ? 113.148 155.772 178.215 1.00 34.63 ?  557 ASP B CA    1 
ATOM   10023 C  C     . ASP B 1 557 ? 112.919 155.731 176.712 1.00 36.07 ?  557 ASP B C     1 
ATOM   10024 O  O     . ASP B 1 557 ? 113.475 156.545 175.967 1.00 38.98 ?  557 ASP B O     1 
ATOM   10025 C  CB    . ASP B 1 557 ? 114.239 154.780 178.620 1.00 32.74 ?  557 ASP B CB    1 
ATOM   10026 C  CG    . ASP B 1 557 ? 114.239 154.488 180.105 1.00 41.14 ?  557 ASP B CG    1 
ATOM   10027 O  OD1   . ASP B 1 557 ? 113.200 154.028 180.621 1.00 44.16 ?  557 ASP B OD1   1 
ATOM   10028 O  OD2   . ASP B 1 557 ? 115.280 154.718 180.757 1.00 42.26 -1 557 ASP B OD2   1 
ATOM   10029 N  N     . TRP B 1 558 ? 112.097 154.788 176.247 1.00 32.21 ?  558 TRP B N     1 
ATOM   10030 C  CA    . TRP B 1 558 ? 111.785 154.718 174.825 1.00 26.34 ?  558 TRP B CA    1 
ATOM   10031 C  C     . TRP B 1 558 ? 110.959 155.916 174.373 1.00 31.81 ?  558 TRP B C     1 
ATOM   10032 O  O     . TRP B 1 558 ? 111.134 156.403 173.253 1.00 38.07 ?  558 TRP B O     1 
ATOM   10033 C  CB    . TRP B 1 558 ? 111.061 153.411 174.515 1.00 27.19 ?  558 TRP B CB    1 
ATOM   10034 C  CG    . TRP B 1 558 ? 111.986 152.298 174.144 1.00 27.01 ?  558 TRP B CG    1 
ATOM   10035 C  CD1   . TRP B 1 558 ? 112.304 151.209 174.899 1.00 26.33 ?  558 TRP B CD1   1 
ATOM   10036 C  CD2   . TRP B 1 558 ? 112.710 152.161 172.916 1.00 27.89 ?  558 TRP B CD2   1 
ATOM   10037 N  NE1   . TRP B 1 558 ? 113.182 150.403 174.219 1.00 30.65 ?  558 TRP B NE1   1 
ATOM   10038 C  CE2   . TRP B 1 558 ? 113.446 150.963 172.998 1.00 28.06 ?  558 TRP B CE2   1 
ATOM   10039 C  CE3   . TRP B 1 558 ? 112.803 152.931 171.754 1.00 31.92 ?  558 TRP B CE3   1 
ATOM   10040 C  CZ2   . TRP B 1 558 ? 114.265 150.521 171.963 1.00 25.09 ?  558 TRP B CZ2   1 
ATOM   10041 C  CZ3   . TRP B 1 558 ? 113.618 152.491 170.729 1.00 26.96 ?  558 TRP B CZ3   1 
ATOM   10042 C  CH2   . TRP B 1 558 ? 114.338 151.297 170.840 1.00 21.83 ?  558 TRP B CH2   1 
ATOM   10043 N  N     . LYS B 1 559 ? 110.054 156.406 175.223 1.00 36.75 ?  559 LYS B N     1 
ATOM   10044 C  CA    . LYS B 1 559 ? 109.309 157.617 174.890 1.00 31.12 ?  559 LYS B CA    1 
ATOM   10045 C  C     . LYS B 1 559 ? 110.233 158.826 174.801 1.00 34.26 ?  559 LYS B C     1 
ATOM   10046 O  O     . LYS B 1 559 ? 110.097 159.660 173.897 1.00 34.78 ?  559 LYS B O     1 
ATOM   10047 C  CB    . LYS B 1 559 ? 108.211 157.859 175.926 1.00 35.39 ?  559 LYS B CB    1 
ATOM   10048 C  CG    . LYS B 1 559 ? 106.970 157.007 175.731 1.00 37.52 ?  559 LYS B CG    1 
ATOM   10049 C  CD    . LYS B 1 559 ? 106.087 157.032 176.966 1.00 36.46 ?  559 LYS B CD    1 
ATOM   10050 C  CE    . LYS B 1 559 ? 105.154 155.834 177.004 1.00 37.55 ?  559 LYS B CE    1 
ATOM   10051 N  NZ    . LYS B 1 559 ? 104.692 155.535 178.388 1.00 36.41 1  559 LYS B NZ    1 
ATOM   10052 N  N     . LYS B 1 560 ? 111.182 158.934 175.734 1.00 31.68 ?  560 LYS B N     1 
ATOM   10053 C  CA    . LYS B 1 560 ? 112.157 160.017 175.677 1.00 30.42 ?  560 LYS B CA    1 
ATOM   10054 C  C     . LYS B 1 560 ? 113.010 159.920 174.419 1.00 34.62 ?  560 LYS B C     1 
ATOM   10055 O  O     . LYS B 1 560 ? 113.306 160.935 173.779 1.00 36.67 ?  560 LYS B O     1 
ATOM   10056 C  CB    . LYS B 1 560 ? 113.034 160.002 176.928 1.00 30.64 ?  560 LYS B CB    1 
ATOM   10057 C  CG    . LYS B 1 560 ? 112.344 160.519 178.177 1.00 35.01 ?  560 LYS B CG    1 
ATOM   10058 C  CD    . LYS B 1 560 ? 113.300 160.555 179.357 1.00 37.36 ?  560 LYS B CD    1 
ATOM   10059 C  CE    . LYS B 1 560 ? 112.550 160.583 180.677 1.00 35.42 ?  560 LYS B CE    1 
ATOM   10060 N  NZ    . LYS B 1 560 ? 111.935 159.264 180.996 1.00 37.29 1  560 LYS B NZ    1 
ATOM   10061 N  N     . LEU B 1 561 ? 113.413 158.703 174.048 1.00 31.74 ?  561 LEU B N     1 
ATOM   10062 C  CA    . LEU B 1 561 ? 114.186 158.516 172.825 1.00 27.68 ?  561 LEU B CA    1 
ATOM   10063 C  C     . LEU B 1 561 ? 113.363 158.860 171.590 1.00 31.16 ?  561 LEU B C     1 
ATOM   10064 O  O     . LEU B 1 561 ? 113.888 159.421 170.625 1.00 33.36 ?  561 LEU B O     1 
ATOM   10065 C  CB    . LEU B 1 561 ? 114.700 157.079 172.743 1.00 29.77 ?  561 LEU B CB    1 
ATOM   10066 C  CG    . LEU B 1 561 ? 115.519 156.743 171.496 1.00 28.99 ?  561 LEU B CG    1 
ATOM   10067 C  CD1   . LEU B 1 561 ? 116.672 157.720 171.342 1.00 25.20 ?  561 LEU B CD1   1 
ATOM   10068 C  CD2   . LEU B 1 561 ? 116.027 155.317 171.552 1.00 26.50 ?  561 LEU B CD2   1 
ATOM   10069 N  N     . LYS B 1 562 ? 112.073 158.520 171.598 1.00 31.63 ?  562 LYS B N     1 
ATOM   10070 C  CA    . LYS B 1 562 ? 111.198 158.878 170.488 1.00 29.39 ?  562 LYS B CA    1 
ATOM   10071 C  C     . LYS B 1 562 ? 111.081 160.389 170.348 1.00 31.00 ?  562 LYS B C     1 
ATOM   10072 O  O     . LYS B 1 562 ? 111.132 160.925 169.235 1.00 35.93 ?  562 LYS B O     1 
ATOM   10073 C  CB    . LYS B 1 562 ? 109.823 158.241 170.688 1.00 27.01 ?  562 LYS B CB    1 
ATOM   10074 C  CG    . LYS B 1 562 ? 108.748 158.737 169.738 1.00 29.64 ?  562 LYS B CG    1 
ATOM   10075 C  CD    . LYS B 1 562 ? 107.397 158.138 170.092 1.00 30.78 ?  562 LYS B CD    1 
ATOM   10076 C  CE    . LYS B 1 562 ? 106.300 158.656 169.178 1.00 32.17 ?  562 LYS B CE    1 
ATOM   10077 N  NZ    . LYS B 1 562 ? 105.085 157.798 169.234 1.00 32.25 1  562 LYS B NZ    1 
ATOM   10078 N  N     . ALA B 1 563 ? 110.929 161.094 171.471 1.00 31.70 ?  563 ALA B N     1 
ATOM   10079 C  CA    . ALA B 1 563 ? 110.890 162.554 171.426 1.00 32.22 ?  563 ALA B CA    1 
ATOM   10080 C  C     . ALA B 1 563 ? 112.215 163.125 170.934 1.00 32.55 ?  563 ALA B C     1 
ATOM   10081 O  O     . ALA B 1 563 ? 112.238 164.083 170.151 1.00 36.45 ?  563 ALA B O     1 
ATOM   10082 C  CB    . ALA B 1 563 ? 110.541 163.113 172.805 1.00 32.53 ?  563 ALA B CB    1 
ATOM   10083 N  N     . PHE B 1 564 ? 113.331 162.546 171.383 1.00 32.33 ?  564 PHE B N     1 
ATOM   10084 C  CA    . PHE B 1 564 ? 114.646 163.005 170.948 1.00 27.46 ?  564 PHE B CA    1 
ATOM   10085 C  C     . PHE B 1 564 ? 114.828 162.812 169.447 1.00 30.75 ?  564 PHE B C     1 
ATOM   10086 O  O     . PHE B 1 564 ? 115.378 163.682 168.763 1.00 33.53 ?  564 PHE B O     1 
ATOM   10087 C  CB    . PHE B 1 564 ? 115.729 162.258 171.727 1.00 28.79 ?  564 PHE B CB    1 
ATOM   10088 C  CG    . PHE B 1 564 ? 117.099 162.853 171.591 1.00 32.18 ?  564 PHE B CG    1 
ATOM   10089 C  CD1   . PHE B 1 564 ? 117.484 163.924 172.378 1.00 31.86 ?  564 PHE B CD1   1 
ATOM   10090 C  CD2   . PHE B 1 564 ? 118.008 162.333 170.686 1.00 33.00 ?  564 PHE B CD2   1 
ATOM   10091 C  CE1   . PHE B 1 564 ? 118.747 164.469 172.259 1.00 34.64 ?  564 PHE B CE1   1 
ATOM   10092 C  CE2   . PHE B 1 564 ? 119.271 162.874 170.562 1.00 32.71 ?  564 PHE B CE2   1 
ATOM   10093 C  CZ    . PHE B 1 564 ? 119.642 163.943 171.349 1.00 34.29 ?  564 PHE B CZ    1 
ATOM   10094 N  N     . VAL B 1 565 ? 114.375 161.674 168.919 1.00 31.07 ?  565 VAL B N     1 
ATOM   10095 C  CA    . VAL B 1 565 ? 114.456 161.422 167.484 1.00 27.20 ?  565 VAL B CA    1 
ATOM   10096 C  C     . VAL B 1 565 ? 113.561 162.388 166.719 1.00 32.84 ?  565 VAL B C     1 
ATOM   10097 O  O     . VAL B 1 565 ? 113.952 162.921 165.675 1.00 34.16 ?  565 VAL B O     1 
ATOM   10098 C  CB    . VAL B 1 565 ? 114.102 159.956 167.180 1.00 27.17 ?  565 VAL B CB    1 
ATOM   10099 C  CG1   . VAL B 1 565 ? 113.925 159.748 165.686 1.00 27.37 ?  565 VAL B CG1   1 
ATOM   10100 C  CG2   . VAL B 1 565 ? 115.181 159.034 167.714 1.00 29.85 ?  565 VAL B CG2   1 
ATOM   10101 N  N     . ALA B 1 566 ? 112.350 162.632 167.223 1.00 34.96 ?  566 ALA B N     1 
ATOM   10102 C  CA    . ALA B 1 566 ? 111.459 163.580 166.566 1.00 34.18 ?  566 ALA B CA    1 
ATOM   10103 C  C     . ALA B 1 566 ? 112.073 164.973 166.524 1.00 36.19 ?  566 ALA B C     1 
ATOM   10104 O  O     . ALA B 1 566 ? 111.908 165.705 165.541 1.00 38.31 ?  566 ALA B O     1 
ATOM   10105 C  CB    . ALA B 1 566 ? 110.106 163.609 167.276 1.00 33.11 ?  566 ALA B CB    1 
ATOM   10106 N  N     . GLU B 1 567 ? 112.787 165.357 167.583 1.00 36.81 ?  567 GLU B N     1 
ATOM   10107 C  CA    . GLU B 1 567 ? 113.398 166.681 167.619 1.00 35.87 ?  567 GLU B CA    1 
ATOM   10108 C  C     . GLU B 1 567 ? 114.624 166.761 166.713 1.00 38.64 ?  567 GLU B C     1 
ATOM   10109 O  O     . GLU B 1 567 ? 114.804 167.752 165.993 1.00 44.38 ?  567 GLU B O     1 
ATOM   10110 C  CB    . GLU B 1 567 ? 113.764 167.047 169.057 1.00 34.73 ?  567 GLU B CB    1 
ATOM   10111 C  CG    . GLU B 1 567 ? 114.975 167.955 169.184 1.00 37.84 ?  567 GLU B CG    1 
ATOM   10112 C  CD    . GLU B 1 567 ? 114.866 168.910 170.355 1.00 42.89 ?  567 GLU B CD    1 
ATOM   10113 O  OE1   . GLU B 1 567 ? 115.790 169.728 170.543 1.00 42.59 ?  567 GLU B OE1   1 
ATOM   10114 O  OE2   . GLU B 1 567 ? 113.855 168.844 171.085 1.00 42.45 -1 567 GLU B OE2   1 
ATOM   10115 N  N     . HIS B 1 568 ? 115.474 165.731 166.722 1.00 34.94 ?  568 HIS B N     1 
ATOM   10116 C  CA    . HIS B 1 568 ? 116.767 165.799 166.054 1.00 31.70 ?  568 HIS B CA    1 
ATOM   10117 C  C     . HIS B 1 568 ? 116.891 164.919 164.820 1.00 32.49 ?  568 HIS B C     1 
ATOM   10118 O  O     . HIS B 1 568 ? 117.764 165.181 163.987 1.00 37.18 ?  568 HIS B O     1 
ATOM   10119 C  CB    . HIS B 1 568 ? 117.889 165.424 167.033 1.00 31.46 ?  568 HIS B CB    1 
ATOM   10120 C  CG    . HIS B 1 568 ? 118.060 166.397 168.156 1.00 35.80 ?  568 HIS B CG    1 
ATOM   10121 N  ND1   . HIS B 1 568 ? 117.945 166.034 169.479 1.00 36.83 ?  568 HIS B ND1   1 
ATOM   10122 C  CD2   . HIS B 1 568 ? 118.336 167.722 168.151 1.00 34.09 ?  568 HIS B CD2   1 
ATOM   10123 C  CE1   . HIS B 1 568 ? 118.144 167.093 170.243 1.00 32.59 ?  568 HIS B CE1   1 
ATOM   10124 N  NE2   . HIS B 1 568 ? 118.383 168.131 169.463 1.00 39.37 ?  568 HIS B NE2   1 
ATOM   10125 N  N     . GLY B 1 569 ? 116.060 163.896 164.677 1.00 28.65 ?  569 GLY B N     1 
ATOM   10126 C  CA    . GLY B 1 569 ? 116.185 162.994 163.553 1.00 27.61 ?  569 GLY B CA    1 
ATOM   10127 C  C     . GLY B 1 569 ? 117.189 161.887 163.808 1.00 29.72 ?  569 GLY B C     1 
ATOM   10128 O  O     . GLY B 1 569 ? 117.746 161.741 164.898 1.00 33.19 ?  569 GLY B O     1 
ATOM   10129 N  N     . MET B 1 570 ? 117.412 161.085 162.769 1.00 26.84 ?  570 MET B N     1 
ATOM   10130 C  CA    . MET B 1 570 ? 118.363 159.984 162.822 1.00 24.33 ?  570 MET B CA    1 
ATOM   10131 C  C     . MET B 1 570 ? 119.380 160.133 161.703 1.00 26.64 ?  570 MET B C     1 
ATOM   10132 O  O     . MET B 1 570 ? 119.021 160.440 160.562 1.00 30.44 ?  570 MET B O     1 
ATOM   10133 C  CB    . MET B 1 570 ? 117.665 158.627 162.707 1.00 25.96 ?  570 MET B CB    1 
ATOM   10134 C  CG    . MET B 1 570 ? 116.721 158.310 163.848 1.00 23.78 ?  570 MET B CG    1 
ATOM   10135 S  SD    . MET B 1 570 ? 117.112 156.734 164.620 1.00 38.72 ?  570 MET B SD    1 
ATOM   10136 C  CE    . MET B 1 570 ? 117.176 155.666 163.188 1.00 28.81 ?  570 MET B CE    1 
ATOM   10137 N  N     . TYR B 1 571 ? 120.651 159.910 162.035 1.00 19.73 ?  571 TYR B N     1 
ATOM   10138 C  CA    . TYR B 1 571 ? 121.708 160.017 161.037 1.00 11.33 ?  571 TYR B CA    1 
ATOM   10139 C  C     . TYR B 1 571 ? 121.738 158.823 160.093 1.00 18.37 ?  571 TYR B C     1 
ATOM   10140 O  O     . TYR B 1 571 ? 122.123 158.971 158.929 1.00 22.60 ?  571 TYR B O     1 
ATOM   10141 C  CB    . TYR B 1 571 ? 123.065 160.166 161.721 1.00 19.31 ?  571 TYR B CB    1 
ATOM   10142 C  CG    . TYR B 1 571 ? 124.167 160.596 160.783 1.00 20.16 ?  571 TYR B CG    1 
ATOM   10143 C  CD1   . TYR B 1 571 ? 124.220 161.894 160.295 1.00 23.18 ?  571 TYR B CD1   1 
ATOM   10144 C  CD2   . TYR B 1 571 ? 125.150 159.703 160.378 1.00 18.13 ?  571 TYR B CD2   1 
ATOM   10145 C  CE1   . TYR B 1 571 ? 125.223 162.292 159.436 1.00 23.37 ?  571 TYR B CE1   1 
ATOM   10146 C  CE2   . TYR B 1 571 ? 126.156 160.093 159.518 1.00 22.50 ?  571 TYR B CE2   1 
ATOM   10147 C  CZ    . TYR B 1 571 ? 126.188 161.389 159.050 1.00 27.73 ?  571 TYR B CZ    1 
ATOM   10148 O  OH    . TYR B 1 571 ? 127.190 161.782 158.194 1.00 26.73 ?  571 TYR B OH    1 
ATOM   10149 N  N     . HIS B 1 572 ? 121.344 157.644 160.565 1.00 20.02 ?  572 HIS B N     1 
ATOM   10150 C  CA    . HIS B 1 572 ? 121.453 156.413 159.796 1.00 13.85 ?  572 HIS B CA    1 
ATOM   10151 C  C     . HIS B 1 572 ? 120.067 155.905 159.431 1.00 22.03 ?  572 HIS B C     1 
ATOM   10152 O  O     . HIS B 1 572 ? 119.200 155.773 160.301 1.00 26.66 ?  572 HIS B O     1 
ATOM   10153 C  CB    . HIS B 1 572 ? 122.210 155.341 160.583 1.00 13.30 ?  572 HIS B CB    1 
ATOM   10154 C  CG    . HIS B 1 572 ? 123.486 155.829 161.194 1.00 14.70 ?  572 HIS B CG    1 
ATOM   10155 N  ND1   . HIS B 1 572 ? 123.557 156.309 162.483 1.00 18.30 ?  572 HIS B ND1   1 
ATOM   10156 C  CD2   . HIS B 1 572 ? 124.741 155.911 160.693 1.00 16.96 ?  572 HIS B CD2   1 
ATOM   10157 C  CE1   . HIS B 1 572 ? 124.801 156.665 162.750 1.00 19.14 ?  572 HIS B CE1   1 
ATOM   10158 N  NE2   . HIS B 1 572 ? 125.539 156.433 161.681 1.00 26.58 ?  572 HIS B NE2   1 
ATOM   10159 N  N     . SER B 1 573 ? 119.864 155.624 158.143 1.00 13.21 ?  573 SER B N     1 
ATOM   10160 C  CA    . SER B 1 573 ? 118.623 154.992 157.712 1.00 7.91  ?  573 SER B CA    1 
ATOM   10161 C  C     . SER B 1 573 ? 118.506 153.581 158.271 1.00 14.44 ?  573 SER B C     1 
ATOM   10162 O  O     . SER B 1 573 ? 117.413 153.144 158.651 1.00 21.39 ?  573 SER B O     1 
ATOM   10163 C  CB    . SER B 1 573 ? 118.546 154.974 156.187 1.00 14.15 ?  573 SER B CB    1 
ATOM   10164 O  OG    . SER B 1 573 ? 119.758 154.503 155.628 1.00 22.11 ?  573 SER B OG    1 
ATOM   10165 N  N     . TYR B 1 574 ? 119.619 152.854 158.321 1.00 14.03 ?  574 TYR B N     1 
ATOM   10166 C  CA    . TYR B 1 574 ? 119.658 151.500 158.848 1.00 7.35  ?  574 TYR B CA    1 
ATOM   10167 C  C     . TYR B 1 574 ? 120.872 151.373 159.752 1.00 8.48  ?  574 TYR B C     1 
ATOM   10168 O  O     . TYR B 1 574 ? 121.943 151.900 159.440 1.00 18.38 ?  574 TYR B O     1 
ATOM   10169 C  CB    . TYR B 1 574 ? 119.712 150.464 157.720 1.00 10.15 ?  574 TYR B CB    1 
ATOM   10170 C  CG    . TYR B 1 574 ? 118.597 150.617 156.714 1.00 7.41  ?  574 TYR B CG    1 
ATOM   10171 C  CD1   . TYR B 1 574 ? 118.727 151.477 155.632 1.00 9.48  ?  574 TYR B CD1   1 
ATOM   10172 C  CD2   . TYR B 1 574 ? 117.409 149.910 156.848 1.00 7.15  ?  574 TYR B CD2   1 
ATOM   10173 C  CE1   . TYR B 1 574 ? 117.710 151.631 154.716 1.00 9.78  ?  574 TYR B CE1   1 
ATOM   10174 C  CE2   . TYR B 1 574 ? 116.388 150.056 155.934 1.00 9.31  ?  574 TYR B CE2   1 
ATOM   10175 C  CZ    . TYR B 1 574 ? 116.544 150.917 154.870 1.00 4.50  ?  574 TYR B CZ    1 
ATOM   10176 O  OH    . TYR B 1 574 ? 115.531 151.064 153.954 1.00 17.16 ?  574 TYR B OH    1 
ATOM   10177 N  N     . ARG B 1 575 ? 120.700 150.681 160.872 1.00 10.32 ?  575 ARG B N     1 
ATOM   10178 C  CA    . ARG B 1 575 ? 121.736 150.615 161.895 1.00 4.99  ?  575 ARG B CA    1 
ATOM   10179 C  C     . ARG B 1 575 ? 122.172 149.202 162.239 1.00 12.76 ?  575 ARG B C     1 
ATOM   10180 O  O     . ARG B 1 575 ? 123.368 148.960 162.407 1.00 18.56 ?  575 ARG B O     1 
ATOM   10181 C  CB    . ARG B 1 575 ? 121.250 151.313 163.171 1.00 13.95 ?  575 ARG B CB    1 
ATOM   10182 C  CG    . ARG B 1 575 ? 120.907 152.777 162.988 1.00 6.32  ?  575 ARG B CG    1 
ATOM   10183 C  CD    . ARG B 1 575 ? 119.899 153.229 164.027 1.00 13.67 ?  575 ARG B CD    1 
ATOM   10184 N  NE    . ARG B 1 575 ? 118.594 152.610 163.827 1.00 18.22 ?  575 ARG B NE    1 
ATOM   10185 C  CZ    . ARG B 1 575 ? 118.130 151.591 164.537 1.00 13.40 ?  575 ARG B CZ    1 
ATOM   10186 N  NH1   . ARG B 1 575 ? 118.845 151.040 165.503 1.00 12.95 1  575 ARG B NH1   1 
ATOM   10187 N  NH2   . ARG B 1 575 ? 116.919 151.112 164.270 1.00 11.24 ?  575 ARG B NH2   1 
ATOM   10188 N  N     . LEU B 1 576 ? 121.241 148.260 162.347 1.00 20.40 ?  576 LEU B N     1 
ATOM   10189 C  CA    . LEU B 1 576 ? 121.532 146.926 162.850 1.00 10.53 ?  576 LEU B CA    1 
ATOM   10190 C  C     . LEU B 1 576 ? 121.286 145.891 161.764 1.00 5.36  ?  576 LEU B C     1 
ATOM   10191 O  O     . LEU B 1 576 ? 120.193 145.829 161.196 1.00 15.05 ?  576 LEU B O     1 
ATOM   10192 C  CB    . LEU B 1 576 ? 120.675 146.607 164.078 1.00 6.04  ?  576 LEU B CB    1 
ATOM   10193 C  CG    . LEU B 1 576 ? 120.692 147.626 165.217 1.00 7.13  ?  576 LEU B CG    1 
ATOM   10194 C  CD1   . LEU B 1 576 ? 119.687 147.239 166.287 1.00 13.51 ?  576 LEU B CD1   1 
ATOM   10195 C  CD2   . LEU B 1 576 ? 122.081 147.748 165.806 1.00 10.43 ?  576 LEU B CD2   1 
ATOM   10196 N  N     . CYS B 1 577 ? 122.306 145.085 161.480 1.00 14.04 ?  577 CYS B N     1 
ATOM   10197 C  CA    . CYS B 1 577 ? 122.167 143.914 160.627 1.00 8.07  ?  577 CYS B CA    1 
ATOM   10198 C  C     . CYS B 1 577 ? 123.137 142.861 161.138 1.00 14.92 ?  577 CYS B C     1 
ATOM   10199 O  O     . CYS B 1 577 ? 124.303 143.165 161.403 1.00 21.80 ?  577 CYS B O     1 
ATOM   10200 C  CB    . CYS B 1 577 ? 122.427 144.250 159.150 1.00 5.93  ?  577 CYS B CB    1 
ATOM   10201 S  SG    . CYS B 1 577 ? 124.138 144.141 158.570 1.00 35.18 ?  577 CYS B SG    1 
ATOM   10202 N  N     . ILE B 1 578 ? 122.648 141.637 161.303 1.00 16.01 ?  578 ILE B N     1 
ATOM   10203 C  CA    . ILE B 1 578 ? 123.416 140.563 161.921 1.00 12.46 ?  578 ILE B CA    1 
ATOM   10204 C  C     . ILE B 1 578 ? 123.984 139.698 160.800 1.00 9.65  ?  578 ILE B C     1 
ATOM   10205 O  O     . ILE B 1 578 ? 123.295 138.839 160.245 1.00 18.17 ?  578 ILE B O     1 
ATOM   10206 C  CB    . ILE B 1 578 ? 122.567 139.752 162.902 1.00 9.77  ?  578 ILE B CB    1 
ATOM   10207 C  CG1   . ILE B 1 578 ? 122.015 140.670 163.994 1.00 8.00  ?  578 ILE B CG1   1 
ATOM   10208 C  CG2   . ILE B 1 578 ? 123.387 138.644 163.528 1.00 9.50  ?  578 ILE B CG2   1 
ATOM   10209 C  CD1   . ILE B 1 578 ? 121.325 139.939 165.111 1.00 8.95  ?  578 ILE B CD1   1 
ATOM   10210 N  N     . ALA B 1 579 ? 125.249 139.934 160.470 1.00 17.09 ?  579 ALA B N     1 
ATOM   10211 C  CA    . ALA B 1 579 ? 125.965 139.188 159.452 1.00 7.33  ?  579 ALA B CA    1 
ATOM   10212 C  C     . ALA B 1 579 ? 126.384 137.818 159.980 1.00 21.03 ?  579 ALA B C     1 
ATOM   10213 O  O     . ALA B 1 579 ? 126.378 137.582 161.189 1.00 28.62 ?  579 ALA B O     1 
ATOM   10214 C  CB    . ALA B 1 579 ? 127.187 139.979 158.998 1.00 11.73 ?  579 ALA B CB    1 
ATOM   10215 N  N     . PRO B 1 580 ? 126.727 136.883 159.087 1.00 25.04 ?  580 PRO B N     1 
ATOM   10216 C  CA    . PRO B 1 580 ? 127.190 135.565 159.555 1.00 22.61 ?  580 PRO B CA    1 
ATOM   10217 C  C     . PRO B 1 580 ? 128.452 135.614 160.404 1.00 25.92 ?  580 PRO B C     1 
ATOM   10218 O  O     . PRO B 1 580 ? 128.603 134.774 161.301 1.00 32.85 ?  580 PRO B O     1 
ATOM   10219 C  CB    . PRO B 1 580 ? 127.417 134.785 158.251 1.00 22.52 ?  580 PRO B CB    1 
ATOM   10220 C  CG    . PRO B 1 580 ? 127.410 135.805 157.160 1.00 21.75 ?  580 PRO B CG    1 
ATOM   10221 C  CD    . PRO B 1 580 ? 126.529 136.906 157.629 1.00 19.76 ?  580 PRO B CD    1 
ATOM   10222 N  N     . THR B 1 581 ? 129.355 136.565 160.156 1.00 21.55 ?  581 THR B N     1 
ATOM   10223 C  CA    . THR B 1 581 ? 130.617 136.699 160.893 1.00 29.18 ?  581 THR B CA    1 
ATOM   10224 C  C     . THR B 1 581 ? 131.388 135.374 160.909 1.00 28.51 ?  581 THR B C     1 
ATOM   10225 O  O     . THR B 1 581 ? 131.605 134.750 161.946 1.00 27.81 ?  581 THR B O     1 
ATOM   10226 C  CB    . THR B 1 581 ? 130.390 137.206 162.322 1.00 28.11 ?  581 THR B CB    1 
ATOM   10227 O  OG1   . THR B 1 581 ? 130.160 136.097 163.200 1.00 27.66 ?  581 THR B OG1   1 
ATOM   10228 C  CG2   . THR B 1 581 ? 129.218 138.171 162.389 1.00 30.44 ?  581 THR B CG2   1 
ATOM   10229 N  N     . GLY B 1 582 ? 131.802 134.966 159.712 1.00 31.48 ?  582 GLY B N     1 
ATOM   10230 C  CA    . GLY B 1 582 ? 132.396 133.658 159.524 1.00 33.44 ?  582 GLY B CA    1 
ATOM   10231 C  C     . GLY B 1 582 ? 133.738 133.438 160.193 1.00 37.00 ?  582 GLY B C     1 
ATOM   10232 O  O     . GLY B 1 582 ? 133.839 132.645 161.134 1.00 38.24 ?  582 GLY B O     1 
ATOM   10233 N  N     . SER B 1 583 ? 134.778 134.131 159.727 1.00 31.25 ?  583 SER B N     1 
ATOM   10234 C  CA    . SER B 1 583 ? 136.134 133.854 160.184 1.00 33.74 ?  583 SER B CA    1 
ATOM   10235 C  C     . SER B 1 583 ? 136.620 134.797 161.275 1.00 35.09 ?  583 SER B C     1 
ATOM   10236 O  O     . SER B 1 583 ? 137.520 134.422 162.034 1.00 37.38 ?  583 SER B O     1 
ATOM   10237 C  CB    . SER B 1 583 ? 137.112 133.912 159.004 1.00 37.87 ?  583 SER B CB    1 
ATOM   10238 O  OG    . SER B 1 583 ? 137.154 132.670 158.322 1.00 41.00 ?  583 SER B OG    1 
ATOM   10239 N  N     . ILE B 1 584 ? 136.054 136.001 161.376 1.00 33.94 ?  584 ILE B N     1 
ATOM   10240 C  CA    . ILE B 1 584 ? 136.466 136.918 162.429 1.00 27.57 ?  584 ILE B CA    1 
ATOM   10241 C  C     . ILE B 1 584 ? 135.927 136.491 163.788 1.00 26.21 ?  584 ILE B C     1 
ATOM   10242 O  O     . ILE B 1 584 ? 136.381 137.000 164.819 1.00 29.85 ?  584 ILE B O     1 
ATOM   10243 C  CB    . ILE B 1 584 ? 136.033 138.355 162.083 1.00 31.69 ?  584 ILE B CB    1 
ATOM   10244 C  CG1   . ILE B 1 584 ? 136.959 139.366 162.760 1.00 28.37 ?  584 ILE B CG1   1 
ATOM   10245 C  CG2   . ILE B 1 584 ? 134.586 138.593 162.485 1.00 29.13 ?  584 ILE B CG2   1 
ATOM   10246 C  CD1   . ILE B 1 584 ? 138.417 139.183 162.449 1.00 31.61 ?  584 ILE B CD1   1 
ATOM   10247 N  N     . SER B 1 585 ? 134.967 135.563 163.820 1.00 31.58 ?  585 SER B N     1 
ATOM   10248 C  CA    . SER B 1 585 ? 134.495 135.039 165.096 1.00 30.22 ?  585 SER B CA    1 
ATOM   10249 C  C     . SER B 1 585 ? 135.552 134.170 165.763 1.00 28.05 ?  585 SER B C     1 
ATOM   10250 O  O     . SER B 1 585 ? 135.540 134.013 166.989 1.00 26.72 ?  585 SER B O     1 
ATOM   10251 C  CB    . SER B 1 585 ? 133.202 134.248 164.896 1.00 25.61 ?  585 SER B CB    1 
ATOM   10252 O  OG    . SER B 1 585 ? 133.411 133.140 164.039 1.00 30.23 ?  585 SER B OG    1 
ATOM   10253 N  N     . TYR B 1 586 ? 136.462 133.594 164.975 1.00 31.10 ?  586 TYR B N     1 
ATOM   10254 C  CA    . TYR B 1 586 ? 137.561 132.821 165.541 1.00 32.10 ?  586 TYR B CA    1 
ATOM   10255 C  C     . TYR B 1 586 ? 138.471 133.703 166.385 1.00 31.26 ?  586 TYR B C     1 
ATOM   10256 O  O     . TYR B 1 586 ? 138.841 133.340 167.507 1.00 34.53 ?  586 TYR B O     1 
ATOM   10257 C  CB    . TYR B 1 586 ? 138.359 132.159 164.418 1.00 28.08 ?  586 TYR B CB    1 
ATOM   10258 C  CG    . TYR B 1 586 ? 137.696 130.945 163.817 1.00 31.07 ?  586 TYR B CG    1 
ATOM   10259 C  CD1   . TYR B 1 586 ? 137.425 129.823 164.587 1.00 31.09 ?  586 TYR B CD1   1 
ATOM   10260 C  CD2   . TYR B 1 586 ? 137.339 130.923 162.477 1.00 31.81 ?  586 TYR B CD2   1 
ATOM   10261 C  CE1   . TYR B 1 586 ? 136.819 128.714 164.037 1.00 33.96 ?  586 TYR B CE1   1 
ATOM   10262 C  CE2   . TYR B 1 586 ? 136.731 129.819 161.918 1.00 30.57 ?  586 TYR B CE2   1 
ATOM   10263 C  CZ    . TYR B 1 586 ? 136.474 128.717 162.702 1.00 34.73 ?  586 TYR B CZ    1 
ATOM   10264 O  OH    . TYR B 1 586 ? 135.868 127.614 162.148 1.00 37.76 ?  586 TYR B OH    1 
ATOM   10265 N  N     . VAL B 1 587 ? 138.832 134.876 165.858 1.00 28.11 ?  587 VAL B N     1 
ATOM   10266 C  CA    . VAL B 1 587 ? 139.767 135.761 166.548 1.00 24.65 ?  587 VAL B CA    1 
ATOM   10267 C  C     . VAL B 1 587 ? 139.171 136.256 167.858 1.00 29.14 ?  587 VAL B C     1 
ATOM   10268 O  O     . VAL B 1 587 ? 139.877 136.403 168.863 1.00 35.72 ?  587 VAL B O     1 
ATOM   10269 C  CB    . VAL B 1 587 ? 140.163 136.932 165.631 1.00 30.15 ?  587 VAL B CB    1 
ATOM   10270 C  CG1   . VAL B 1 587 ? 141.280 137.747 166.259 1.00 30.11 ?  587 VAL B CG1   1 
ATOM   10271 C  CG2   . VAL B 1 587 ? 140.573 136.418 164.260 1.00 28.67 ?  587 VAL B CG2   1 
ATOM   10272 N  N     . GLN B 1 588 ? 137.867 136.513 167.873 1.00 31.14 ?  588 GLN B N     1 
ATOM   10273 C  CA    . GLN B 1 588 ? 137.196 137.023 169.059 1.00 24.26 ?  588 GLN B CA    1 
ATOM   10274 C  C     . GLN B 1 588 ? 136.853 135.933 170.063 1.00 25.55 ?  588 GLN B C     1 
ATOM   10275 O  O     . GLN B 1 588 ? 136.310 136.251 171.127 1.00 32.76 ?  588 GLN B O     1 
ATOM   10276 C  CB    . GLN B 1 588 ? 135.921 137.769 168.660 1.00 25.03 ?  588 GLN B CB    1 
ATOM   10277 C  CG    . GLN B 1 588 ? 136.170 139.128 168.035 1.00 28.82 ?  588 GLN B CG    1 
ATOM   10278 C  CD    . GLN B 1 588 ? 136.045 140.256 169.039 1.00 24.32 ?  588 GLN B CD    1 
ATOM   10279 O  OE1   . GLN B 1 588 ? 135.086 140.314 169.806 1.00 29.94 ?  588 GLN B OE1   1 
ATOM   10280 N  NE2   . GLN B 1 588 ? 137.015 141.161 169.037 1.00 26.90 ?  588 GLN B NE2   1 
ATOM   10281 N  N     . SER B 1 589 ? 137.164 134.674 169.757 1.00 30.06 ?  589 SER B N     1 
ATOM   10282 C  CA    . SER B 1 589 ? 136.794 133.533 170.591 1.00 27.12 ?  589 SER B CA    1 
ATOM   10283 C  C     . SER B 1 589 ? 135.293 133.550 170.868 1.00 26.93 ?  589 SER B C     1 
ATOM   10284 O  O     . SER B 1 589 ? 134.833 133.573 172.010 1.00 28.72 ?  589 SER B O     1 
ATOM   10285 C  CB    . SER B 1 589 ? 137.602 133.514 171.891 1.00 32.57 ?  589 SER B CB    1 
ATOM   10286 O  OG    . SER B 1 589 ? 138.981 133.334 171.626 1.00 36.64 ?  589 SER B OG    1 
ATOM   10287 N  N     . SER B 1 590 ? 134.530 133.550 169.778 1.00 25.89 ?  590 SER B N     1 
ATOM   10288 C  CA    . SER B 1 590 ? 133.089 133.715 169.838 1.00 22.92 ?  590 SER B CA    1 
ATOM   10289 C  C     . SER B 1 590 ? 132.425 132.756 168.864 1.00 25.94 ?  590 SER B C     1 
ATOM   10290 O  O     . SER B 1 590 ? 133.005 132.380 167.843 1.00 29.51 ?  590 SER B O     1 
ATOM   10291 C  CB    . SER B 1 590 ? 132.684 135.157 169.511 1.00 21.98 ?  590 SER B CB    1 
ATOM   10292 O  OG    . SER B 1 590 ? 132.428 135.313 168.128 1.00 31.28 ?  590 SER B OG    1 
ATOM   10293 N  N     . THR B 1 591 ? 131.200 132.357 169.195 1.00 25.52 ?  591 THR B N     1 
ATOM   10294 C  CA    . THR B 1 591 ? 130.396 131.583 168.264 1.00 21.76 ?  591 THR B CA    1 
ATOM   10295 C  C     . THR B 1 591 ? 129.907 132.475 167.130 1.00 24.15 ?  591 THR B C     1 
ATOM   10296 O  O     . THR B 1 591 ? 129.664 133.671 167.309 1.00 22.75 ?  591 THR B O     1 
ATOM   10297 C  CB    . THR B 1 591 ? 129.211 130.938 168.979 1.00 22.02 ?  591 THR B CB    1 
ATOM   10298 O  OG1   . THR B 1 591 ? 128.238 131.940 169.299 1.00 29.69 ?  591 THR B OG1   1 
ATOM   10299 C  CG2   . THR B 1 591 ? 129.673 130.261 170.256 1.00 20.22 ?  591 THR B CG2   1 
ATOM   10300 N  N     . ALA B 1 592 ? 129.767 131.879 165.949 1.00 22.71 ?  592 ALA B N     1 
ATOM   10301 C  CA    . ALA B 1 592 ? 129.460 132.642 164.747 1.00 20.11 ?  592 ALA B CA    1 
ATOM   10302 C  C     . ALA B 1 592 ? 128.064 133.247 164.837 1.00 19.32 ?  592 ALA B C     1 
ATOM   10303 O  O     . ALA B 1 592 ? 127.067 132.520 164.872 1.00 27.49 ?  592 ALA B O     1 
ATOM   10304 C  CB    . ALA B 1 592 ? 129.577 131.749 163.515 1.00 24.99 ?  592 ALA B CB    1 
ATOM   10305 N  N     . SER B 1 593 ? 128.004 134.574 164.882 1.00 25.09 ?  593 SER B N     1 
ATOM   10306 C  CA    . SER B 1 593 ? 126.753 135.338 164.780 1.00 14.55 ?  593 SER B CA    1 
ATOM   10307 C  C     . SER B 1 593 ? 125.831 134.944 165.937 1.00 16.18 ?  593 SER B C     1 
ATOM   10308 O  O     . SER B 1 593 ? 126.294 134.509 166.999 1.00 27.98 ?  593 SER B O     1 
ATOM   10309 C  CB    . SER B 1 593 ? 126.158 135.136 163.399 1.00 27.06 ?  593 SER B CB    1 
ATOM   10310 O  OG    . SER B 1 593 ? 125.086 136.028 163.163 1.00 23.36 ?  593 SER B OG    1 
ATOM   10311 N  N     . VAL B 1 594 ? 124.521 135.099 165.742 1.00 19.65 ?  594 VAL B N     1 
ATOM   10312 C  CA    . VAL B 1 594 ? 123.529 134.646 166.705 1.00 19.52 ?  594 VAL B CA    1 
ATOM   10313 C  C     . VAL B 1 594 ? 123.067 133.223 166.407 1.00 18.59 ?  594 VAL B C     1 
ATOM   10314 O  O     . VAL B 1 594 ? 122.147 132.722 167.060 1.00 18.18 ?  594 VAL B O     1 
ATOM   10315 C  CB    . VAL B 1 594 ? 122.332 135.609 166.764 1.00 17.07 ?  594 VAL B CB    1 
ATOM   10316 C  CG1   . VAL B 1 594 ? 122.782 136.982 167.234 1.00 12.24 ?  594 VAL B CG1   1 
ATOM   10317 C  CG2   . VAL B 1 594 ? 121.658 135.702 165.406 1.00 19.04 ?  594 VAL B CG2   1 
ATOM   10318 N  N     . MET B 1 595 ? 123.685 132.564 165.432 1.00 23.61 ?  595 MET B N     1 
ATOM   10319 C  CA    . MET B 1 595 ? 123.343 131.190 165.117 1.00 19.01 ?  595 MET B CA    1 
ATOM   10320 C  C     . MET B 1 595 ? 123.869 130.250 166.200 1.00 26.69 ?  595 MET B C     1 
ATOM   10321 O  O     . MET B 1 595 ? 124.884 130.534 166.843 1.00 29.65 ?  595 MET B O     1 
ATOM   10322 C  CB    . MET B 1 595 ? 123.930 130.787 163.767 1.00 18.08 ?  595 MET B CB    1 
ATOM   10323 C  CG    . MET B 1 595 ? 123.105 131.184 162.551 1.00 24.07 ?  595 MET B CG    1 
ATOM   10324 S  SD    . MET B 1 595 ? 121.335 131.294 162.864 1.00 29.78 ?  595 MET B SD    1 
ATOM   10325 C  CE    . MET B 1 595 ? 121.128 133.070 162.906 1.00 22.55 ?  595 MET B CE    1 
ATOM   10326 N  N     . PRO B 1 596 ? 123.195 129.127 166.426 1.00 29.56 ?  596 PRO B N     1 
ATOM   10327 C  CA    . PRO B 1 596 ? 123.754 128.101 167.308 1.00 19.09 ?  596 PRO B CA    1 
ATOM   10328 C  C     . PRO B 1 596 ? 124.938 127.403 166.656 1.00 25.93 ?  596 PRO B C     1 
ATOM   10329 O  O     . PRO B 1 596 ? 125.079 127.362 165.432 1.00 30.62 ?  596 PRO B O     1 
ATOM   10330 C  CB    . PRO B 1 596 ? 122.584 127.137 167.523 1.00 20.74 ?  596 PRO B CB    1 
ATOM   10331 C  CG    . PRO B 1 596 ? 121.726 127.316 166.322 1.00 23.25 ?  596 PRO B CG    1 
ATOM   10332 C  CD    . PRO B 1 596 ? 121.874 128.748 165.895 1.00 25.77 ?  596 PRO B CD    1 
ATOM   10333 N  N     . ILE B 1 597 ? 125.805 126.850 167.506 1.00 28.44 ?  597 ILE B N     1 
ATOM   10334 C  CA    . ILE B 1 597 ? 127.044 126.248 167.032 1.00 31.03 ?  597 ILE B CA    1 
ATOM   10335 C  C     . ILE B 1 597 ? 126.739 125.021 166.184 1.00 34.42 ?  597 ILE B C     1 
ATOM   10336 O  O     . ILE B 1 597 ? 125.829 124.237 166.488 1.00 37.08 ?  597 ILE B O     1 
ATOM   10337 C  CB    . ILE B 1 597 ? 127.959 125.893 168.215 1.00 32.17 ?  597 ILE B CB    1 
ATOM   10338 C  CG1   . ILE B 1 597 ? 127.291 124.859 169.122 1.00 30.45 ?  597 ILE B CG1   1 
ATOM   10339 C  CG2   . ILE B 1 597 ? 128.314 127.140 169.000 1.00 29.22 ?  597 ILE B CG2   1 
ATOM   10340 C  CD1   . ILE B 1 597 ? 128.260 123.933 169.811 1.00 29.18 ?  597 ILE B CD1   1 
ATOM   10341 N  N     . MET B 1 598 ? 127.494 124.860 165.096 1.00 40.22 ?  598 MET B N     1 
ATOM   10342 C  CA    . MET B 1 598 ? 127.340 123.675 164.261 1.00 38.65 ?  598 MET B CA    1 
ATOM   10343 C  C     . MET B 1 598 ? 127.871 122.434 164.965 1.00 36.48 ?  598 MET B C     1 
ATOM   10344 O  O     . MET B 1 598 ? 127.244 121.369 164.921 1.00 42.09 ?  598 MET B O     1 
ATOM   10345 C  CB    . MET B 1 598 ? 128.053 123.879 162.925 1.00 38.14 ?  598 MET B CB    1 
ATOM   10346 C  CG    . MET B 1 598 ? 127.240 124.646 161.901 1.00 35.63 ?  598 MET B CG    1 
ATOM   10347 S  SD    . MET B 1 598 ? 128.260 125.446 160.650 1.00 53.34 ?  598 MET B SD    1 
ATOM   10348 C  CE    . MET B 1 598 ? 129.387 126.383 161.679 1.00 40.76 ?  598 MET B CE    1 
ATOM   10349 N  N     . GLU B 1 599 ? 129.023 122.551 165.622 1.00 37.86 ?  599 GLU B N     1 
ATOM   10350 C  CA    . GLU B 1 599 ? 129.631 121.434 166.327 1.00 37.80 ?  599 GLU B CA    1 
ATOM   10351 C  C     . GLU B 1 599 ? 130.357 121.963 167.552 1.00 34.97 ?  599 GLU B C     1 
ATOM   10352 O  O     . GLU B 1 599 ? 130.801 123.114 167.578 1.00 40.23 ?  599 GLU B O     1 
ATOM   10353 C  CB    . GLU B 1 599 ? 130.600 120.663 165.425 1.00 39.85 ?  599 GLU B CB    1 
ATOM   10354 C  CG    . GLU B 1 599 ? 131.581 121.551 164.682 1.00 37.81 ?  599 GLU B CG    1 
ATOM   10355 C  CD    . GLU B 1 599 ? 131.861 121.065 163.276 1.00 43.29 ?  599 GLU B CD    1 
ATOM   10356 O  OE1   . GLU B 1 599 ? 131.754 119.845 163.035 1.00 44.64 ?  599 GLU B OE1   1 
ATOM   10357 O  OE2   . GLU B 1 599 ? 132.191 121.904 162.411 1.00 43.83 -1 599 GLU B OE2   1 
ATOM   10358 N  N     . ARG B 1 600 ? 130.471 121.111 168.572 1.00 36.52 ?  600 ARG B N     1 
ATOM   10359 C  CA    . ARG B 1 600 ? 131.168 121.508 169.790 1.00 32.88 ?  600 ARG B CA    1 
ATOM   10360 C  C     . ARG B 1 600 ? 132.660 121.670 169.540 1.00 33.71 ?  600 ARG B C     1 
ATOM   10361 O  O     . ARG B 1 600 ? 133.262 122.677 169.930 1.00 39.87 ?  600 ARG B O     1 
ATOM   10362 C  CB    . ARG B 1 600 ? 130.910 120.485 170.894 1.00 35.62 ?  600 ARG B CB    1 
ATOM   10363 C  CG    . ARG B 1 600 ? 129.528 120.583 171.499 1.00 33.67 ?  600 ARG B CG    1 
ATOM   10364 C  CD    . ARG B 1 600 ? 129.414 119.733 172.742 1.00 31.09 ?  600 ARG B CD    1 
ATOM   10365 N  NE    . ARG B 1 600 ? 128.056 119.710 173.267 1.00 32.40 ?  600 ARG B NE    1 
ATOM   10366 C  CZ    . ARG B 1 600 ? 127.083 118.944 172.794 1.00 34.59 ?  600 ARG B CZ    1 
ATOM   10367 N  NH1   . ARG B 1 600 ? 127.281 118.131 171.769 1.00 33.92 1  600 ARG B NH1   1 
ATOM   10368 N  NH2   . ARG B 1 600 ? 125.882 118.996 173.362 1.00 35.08 ?  600 ARG B NH2   1 
ATOM   10369 N  N     . ILE B 1 601 ? 133.276 120.686 168.893 1.00 38.78 ?  601 ILE B N     1 
ATOM   10370 C  CA    . ILE B 1 601 ? 134.674 120.750 168.485 1.00 37.26 ?  601 ILE B CA    1 
ATOM   10371 C  C     . ILE B 1 601 ? 134.718 120.531 166.981 1.00 37.70 ?  601 ILE B C     1 
ATOM   10372 O  O     . ILE B 1 601 ? 134.234 119.505 166.485 1.00 42.98 ?  601 ILE B O     1 
ATOM   10373 C  CB    . ILE B 1 601 ? 135.537 119.710 169.216 1.00 39.69 ?  601 ILE B CB    1 
ATOM   10374 C  CG1   . ILE B 1 601 ? 135.243 119.727 170.716 1.00 40.45 ?  601 ILE B CG1   1 
ATOM   10375 C  CG2   . ILE B 1 601 ? 137.012 119.970 168.961 1.00 37.99 ?  601 ILE B CG2   1 
ATOM   10376 C  CD1   . ILE B 1 601 ? 135.890 118.593 171.479 1.00 39.25 ?  601 ILE B CD1   1 
ATOM   10377 N  N     . GLU B 1 602 ? 135.293 121.485 166.258 1.00 45.48 ?  602 GLU B N     1 
ATOM   10378 C  CA    . GLU B 1 602 ? 135.370 121.412 164.807 1.00 46.01 ?  602 GLU B CA    1 
ATOM   10379 C  C     . GLU B 1 602 ? 136.776 121.025 164.373 1.00 47.78 ?  602 GLU B C     1 
ATOM   10380 O  O     . GLU B 1 602 ? 137.763 121.612 164.824 1.00 47.96 ?  602 GLU B O     1 
ATOM   10381 C  CB    . GLU B 1 602 ? 134.977 122.744 164.168 1.00 44.80 ?  602 GLU B CB    1 
ATOM   10382 C  CG    . GLU B 1 602 ? 135.509 123.964 164.889 1.00 47.22 ?  602 GLU B CG    1 
ATOM   10383 C  CD    . GLU B 1 602 ? 135.499 125.200 164.017 1.00 50.05 ?  602 GLU B CD    1 
ATOM   10384 O  OE1   . GLU B 1 602 ? 134.402 125.731 163.746 1.00 48.81 ?  602 GLU B OE1   1 
ATOM   10385 O  OE2   . GLU B 1 602 ? 136.590 125.637 163.597 1.00 49.61 -1 602 GLU B OE2   1 
ATOM   10386 N  N     . GLU B 1 603 ? 136.861 120.031 163.492 1.00 53.84 ?  603 GLU B N     1 
ATOM   10387 C  CA    . GLU B 1 603 ? 138.132 119.553 162.961 1.00 54.70 ?  603 GLU B CA    1 
ATOM   10388 C  C     . GLU B 1 603 ? 138.344 120.182 161.589 1.00 53.81 ?  603 GLU B C     1 
ATOM   10389 O  O     . GLU B 1 603 ? 137.600 119.897 160.644 1.00 54.77 ?  603 GLU B O     1 
ATOM   10390 C  CB    . GLU B 1 603 ? 138.149 118.028 162.881 1.00 54.03 ?  603 GLU B CB    1 
ATOM   10391 C  CG    . GLU B 1 603 ? 139.431 117.449 162.308 1.00 56.11 ?  603 GLU B CG    1 
ATOM   10392 C  CD    . GLU B 1 603 ? 139.275 116.004 161.876 1.00 58.17 ?  603 GLU B CD    1 
ATOM   10393 O  OE1   . GLU B 1 603 ? 139.240 115.119 162.757 1.00 57.94 ?  603 GLU B OE1   1 
ATOM   10394 O  OE2   . GLU B 1 603 ? 139.186 115.753 160.656 1.00 56.54 -1 603 GLU B OE2   1 
ATOM   10395 N  N     . ARG B 1 604 ? 139.359 121.036 161.483 1.00 55.14 ?  604 ARG B N     1 
ATOM   10396 C  CA    . ARG B 1 604 ? 139.673 121.743 160.251 1.00 55.62 ?  604 ARG B CA    1 
ATOM   10397 C  C     . ARG B 1 604 ? 141.076 121.369 159.796 1.00 56.99 ?  604 ARG B C     1 
ATOM   10398 O  O     . ARG B 1 604 ? 142.008 121.314 160.604 1.00 58.94 ?  604 ARG B O     1 
ATOM   10399 C  CB    . ARG B 1 604 ? 139.573 123.260 160.446 1.00 57.20 ?  604 ARG B CB    1 
ATOM   10400 C  CG    . ARG B 1 604 ? 138.152 123.801 160.467 1.00 57.77 ?  604 ARG B CG    1 
ATOM   10401 C  CD    . ARG B 1 604 ? 137.279 123.136 159.418 1.00 56.81 ?  604 ARG B CD    1 
ATOM   10402 N  NE    . ARG B 1 604 ? 136.266 122.275 160.016 1.00 59.20 ?  604 ARG B NE    1 
ATOM   10403 C  CZ    . ARG B 1 604 ? 135.103 122.702 160.487 1.00 59.01 ?  604 ARG B CZ    1 
ATOM   10404 N  NH1   . ARG B 1 604 ? 134.771 123.982 160.453 1.00 56.40 1  604 ARG B NH1   1 
ATOM   10405 N  NH2   . ARG B 1 604 ? 134.250 121.822 161.005 1.00 56.67 ?  604 ARG B NH2   1 
ATOM   10406 N  N     . THR B 1 605 ? 141.228 121.122 158.499 1.00 63.74 ?  605 THR B N     1 
ATOM   10407 C  CA    . THR B 1 605 ? 142.507 120.726 157.928 1.00 64.57 ?  605 THR B CA    1 
ATOM   10408 C  C     . THR B 1 605 ? 143.198 121.952 157.342 1.00 64.75 ?  605 THR B C     1 
ATOM   10409 O  O     . THR B 1 605 ? 142.657 122.603 156.441 1.00 64.19 ?  605 THR B O     1 
ATOM   10410 C  CB    . THR B 1 605 ? 142.319 119.654 156.855 1.00 64.44 ?  605 THR B CB    1 
ATOM   10411 O  OG1   . THR B 1 605 ? 141.711 118.495 157.437 1.00 64.01 ?  605 THR B OG1   1 
ATOM   10412 C  CG2   . THR B 1 605 ? 143.660 119.266 156.253 1.00 64.39 ?  605 THR B CG2   1 
ATOM   10413 N  N     . TYR B 1 606 ? 144.385 122.261 157.855 1.00 64.82 ?  606 TYR B N     1 
ATOM   10414 C  CA    . TYR B 1 606 ? 145.212 123.347 157.347 1.00 66.48 ?  606 TYR B CA    1 
ATOM   10415 C  C     . TYR B 1 606 ? 146.548 122.772 156.905 1.00 67.41 ?  606 TYR B C     1 
ATOM   10416 O  O     . TYR B 1 606 ? 147.216 122.076 157.679 1.00 65.23 ?  606 TYR B O     1 
ATOM   10417 C  CB    . TYR B 1 606 ? 145.413 124.434 158.406 1.00 64.43 ?  606 TYR B CB    1 
ATOM   10418 C  CG    . TYR B 1 606 ? 144.123 125.063 158.881 1.00 65.10 ?  606 TYR B CG    1 
ATOM   10419 C  CD1   . TYR B 1 606 ? 143.409 125.930 158.064 1.00 64.08 ?  606 TYR B CD1   1 
ATOM   10420 C  CD2   . TYR B 1 606 ? 143.618 124.791 160.146 1.00 63.67 ?  606 TYR B CD2   1 
ATOM   10421 C  CE1   . TYR B 1 606 ? 142.230 126.506 158.491 1.00 64.22 ?  606 TYR B CE1   1 
ATOM   10422 C  CE2   . TYR B 1 606 ? 142.439 125.363 160.582 1.00 62.41 ?  606 TYR B CE2   1 
ATOM   10423 C  CZ    . TYR B 1 606 ? 141.749 126.219 159.750 1.00 65.40 ?  606 TYR B CZ    1 
ATOM   10424 O  OH    . TYR B 1 606 ? 140.573 126.792 160.180 1.00 66.17 ?  606 TYR B OH    1 
ATOM   10425 N  N     . GLY B 1 607 ? 146.933 123.064 155.666 1.00 74.58 ?  607 GLY B N     1 
ATOM   10426 C  CA    . GLY B 1 607 ? 148.124 122.446 155.108 1.00 74.32 ?  607 GLY B CA    1 
ATOM   10427 C  C     . GLY B 1 607 ? 147.974 120.938 155.097 1.00 75.00 ?  607 GLY B C     1 
ATOM   10428 O  O     . GLY B 1 607 ? 146.956 120.394 154.656 1.00 73.95 ?  607 GLY B O     1 
ATOM   10429 N  N     . ASN B 1 608 ? 148.998 120.247 155.590 1.00 78.45 ?  608 ASN B N     1 
ATOM   10430 C  CA    . ASN B 1 608 ? 148.949 118.804 155.773 1.00 78.79 ?  608 ASN B CA    1 
ATOM   10431 C  C     . ASN B 1 608 ? 148.586 118.413 157.199 1.00 78.89 ?  608 ASN B C     1 
ATOM   10432 O  O     . ASN B 1 608 ? 148.575 117.221 157.522 1.00 79.13 ?  608 ASN B O     1 
ATOM   10433 C  CB    . ASN B 1 608 ? 150.287 118.175 155.380 1.00 78.58 ?  608 ASN B CB    1 
ATOM   10434 C  CG    . ASN B 1 608 ? 151.431 118.646 156.257 1.00 79.08 ?  608 ASN B CG    1 
ATOM   10435 O  OD1   . ASN B 1 608 ? 151.295 119.614 157.006 1.00 78.71 ?  608 ASN B OD1   1 
ATOM   10436 N  ND2   . ASN B 1 608 ? 152.567 117.965 156.166 1.00 78.97 ?  608 ASN B ND2   1 
ATOM   10437 N  N     . SER B 1 609 ? 148.288 119.386 158.055 1.00 72.52 ?  609 SER B N     1 
ATOM   10438 C  CA    . SER B 1 609 ? 147.962 119.137 159.449 1.00 71.89 ?  609 SER B CA    1 
ATOM   10439 C  C     . SER B 1 609 ? 146.469 119.317 159.686 1.00 70.62 ?  609 SER B C     1 
ATOM   10440 O  O     . SER B 1 609 ? 145.757 119.932 158.888 1.00 71.68 ?  609 SER B O     1 
ATOM   10441 C  CB    . SER B 1 609 ? 148.753 120.069 160.371 1.00 69.93 ?  609 SER B CB    1 
ATOM   10442 O  OG    . SER B 1 609 ? 148.343 121.416 160.205 1.00 69.72 ?  609 SER B OG    1 
ATOM   10443 N  N     . LYS B 1 610 ? 145.999 118.762 160.798 1.00 61.32 ?  610 LYS B N     1 
ATOM   10444 C  CA    . LYS B 1 610 ? 144.615 118.899 161.222 1.00 61.43 ?  610 LYS B CA    1 
ATOM   10445 C  C     . LYS B 1 610 ? 144.575 119.515 162.613 1.00 61.84 ?  610 LYS B C     1 
ATOM   10446 O  O     . LYS B 1 610 ? 145.411 119.202 163.466 1.00 59.72 ?  610 LYS B O     1 
ATOM   10447 C  CB    . LYS B 1 610 ? 143.891 117.547 161.203 1.00 62.88 ?  610 LYS B CB    1 
ATOM   10448 C  CG    . LYS B 1 610 ? 144.394 116.536 162.221 1.00 61.41 ?  610 LYS B CG    1 
ATOM   10449 C  CD    . LYS B 1 610 ? 143.460 115.339 162.334 1.00 61.32 ?  610 LYS B CD    1 
ATOM   10450 C  CE    . LYS B 1 610 ? 142.715 115.073 161.033 1.00 61.36 ?  610 LYS B CE    1 
ATOM   10451 N  NZ    . LYS B 1 610 ? 141.752 113.946 161.162 1.00 60.10 1  610 LYS B NZ    1 
ATOM   10452 N  N     . THR B 1 611 ? 143.617 120.413 162.827 1.00 60.71 ?  611 THR B N     1 
ATOM   10453 C  CA    . THR B 1 611 ? 143.469 121.124 164.085 1.00 57.67 ?  611 THR B CA    1 
ATOM   10454 C  C     . THR B 1 611 ? 142.040 120.979 164.579 1.00 54.85 ?  611 THR B C     1 
ATOM   10455 O  O     . THR B 1 611 ? 141.104 120.833 163.787 1.00 57.03 ?  611 THR B O     1 
ATOM   10456 C  CB    . THR B 1 611 ? 143.811 122.613 163.940 1.00 58.17 ?  611 THR B CB    1 
ATOM   10457 O  OG1   . THR B 1 611 ? 142.952 123.204 162.959 1.00 58.82 ?  611 THR B OG1   1 
ATOM   10458 C  CG2   . THR B 1 611 ? 145.256 122.792 163.511 1.00 55.74 ?  611 THR B CG2   1 
ATOM   10459 N  N     . TYR B 1 612 ? 141.876 121.010 165.897 1.00 49.86 ?  612 TYR B N     1 
ATOM   10460 C  CA    . TYR B 1 612 ? 140.563 120.933 166.521 1.00 50.17 ?  612 TYR B CA    1 
ATOM   10461 C  C     . TYR B 1 612 ? 140.308 122.215 167.296 1.00 50.25 ?  612 TYR B C     1 
ATOM   10462 O  O     . TYR B 1 612 ? 141.088 122.575 168.185 1.00 51.80 ?  612 TYR B O     1 
ATOM   10463 C  CB    . TYR B 1 612 ? 140.439 119.713 167.438 1.00 52.03 ?  612 TYR B CB    1 
ATOM   10464 C  CG    . TYR B 1 612 ? 140.810 118.398 166.786 1.00 54.51 ?  612 TYR B CG    1 
ATOM   10465 C  CD1   . TYR B 1 612 ? 142.137 118.055 166.559 1.00 53.62 ?  612 TYR B CD1   1 
ATOM   10466 C  CD2   . TYR B 1 612 ? 139.825 117.515 166.367 1.00 54.03 ?  612 TYR B CD2   1 
ATOM   10467 C  CE1   . TYR B 1 612 ? 142.471 116.857 165.958 1.00 55.62 ?  612 TYR B CE1   1 
ATOM   10468 C  CE2   . TYR B 1 612 ? 140.149 116.315 165.767 1.00 54.22 ?  612 TYR B CE2   1 
ATOM   10469 C  CZ    . TYR B 1 612 ? 141.472 115.992 165.564 1.00 55.61 ?  612 TYR B CZ    1 
ATOM   10470 O  OH    . TYR B 1 612 ? 141.795 114.798 164.964 1.00 55.81 ?  612 TYR B OH    1 
ATOM   10471 N  N     . TYR B 1 613 ? 139.221 122.897 166.956 1.00 42.10 ?  613 TYR B N     1 
ATOM   10472 C  CA    . TYR B 1 613 ? 138.799 124.105 167.652 1.00 38.05 ?  613 TYR B CA    1 
ATOM   10473 C  C     . TYR B 1 613 ? 137.580 123.794 168.503 1.00 38.01 ?  613 TYR B C     1 
ATOM   10474 O  O     . TYR B 1 613 ? 136.498 123.533 167.951 1.00 36.70 ?  613 TYR B O     1 
ATOM   10475 C  CB    . TYR B 1 613 ? 138.484 125.223 166.658 1.00 38.76 ?  613 TYR B CB    1 
ATOM   10476 C  CG    . TYR B 1 613 ? 137.953 126.484 167.302 1.00 35.14 ?  613 TYR B CG    1 
ATOM   10477 C  CD1   . TYR B 1 613 ? 138.705 127.178 168.239 1.00 36.58 ?  613 TYR B CD1   1 
ATOM   10478 C  CD2   . TYR B 1 613 ? 136.701 126.983 166.970 1.00 36.96 ?  613 TYR B CD2   1 
ATOM   10479 C  CE1   . TYR B 1 613 ? 138.228 128.330 168.827 1.00 38.78 ?  613 TYR B CE1   1 
ATOM   10480 C  CE2   . TYR B 1 613 ? 136.214 128.135 167.553 1.00 39.76 ?  613 TYR B CE2   1 
ATOM   10481 C  CZ    . TYR B 1 613 ? 136.982 128.805 168.481 1.00 41.14 ?  613 TYR B CZ    1 
ATOM   10482 O  OH    . TYR B 1 613 ? 136.505 129.954 169.065 1.00 40.64 ?  613 TYR B OH    1 
ATOM   10483 N  N     . PRO B 1 614 ? 137.708 123.746 169.826 1.00 35.86 ?  614 PRO B N     1 
ATOM   10484 C  CA    . PRO B 1 614 ? 136.518 123.665 170.675 1.00 34.87 ?  614 PRO B CA    1 
ATOM   10485 C  C     . PRO B 1 614 ? 135.778 124.991 170.691 1.00 38.36 ?  614 PRO B C     1 
ATOM   10486 O  O     . PRO B 1 614 ? 136.363 126.058 170.488 1.00 39.87 ?  614 PRO B O     1 
ATOM   10487 C  CB    . PRO B 1 614 ? 137.085 123.327 172.061 1.00 33.93 ?  614 PRO B CB    1 
ATOM   10488 C  CG    . PRO B 1 614 ? 138.517 122.931 171.827 1.00 36.88 ?  614 PRO B CG    1 
ATOM   10489 C  CD    . PRO B 1 614 ? 138.951 123.670 170.608 1.00 35.12 ?  614 PRO B CD    1 
ATOM   10490 N  N     . MET B 1 615 ? 134.475 124.913 170.929 1.00 32.85 ?  615 MET B N     1 
ATOM   10491 C  CA    . MET B 1 615 ? 133.684 126.126 171.046 1.00 29.77 ?  615 MET B CA    1 
ATOM   10492 C  C     . MET B 1 615 ? 134.154 126.935 172.252 1.00 36.44 ?  615 MET B C     1 
ATOM   10493 O  O     . MET B 1 615 ? 134.588 126.357 173.255 1.00 40.66 ?  615 MET B O     1 
ATOM   10494 C  CB    . MET B 1 615 ? 132.198 125.788 171.169 1.00 30.91 ?  615 MET B CB    1 
ATOM   10495 C  CG    . MET B 1 615 ? 131.510 125.462 169.846 1.00 35.52 ?  615 MET B CG    1 
ATOM   10496 S  SD    . MET B 1 615 ? 132.138 126.368 168.413 1.00 41.17 ?  615 MET B SD    1 
ATOM   10497 C  CE    . MET B 1 615 ? 133.292 125.195 167.700 1.00 34.86 ?  615 MET B CE    1 
ATOM   10498 N  N     . PRO B 1 616 ? 134.100 128.265 172.184 1.00 37.15 ?  616 PRO B N     1 
ATOM   10499 C  CA    . PRO B 1 616 ? 134.653 129.092 173.269 1.00 33.00 ?  616 PRO B CA    1 
ATOM   10500 C  C     . PRO B 1 616 ? 133.960 128.821 174.594 1.00 35.01 ?  616 PRO B C     1 
ATOM   10501 O  O     . PRO B 1 616 ? 132.743 128.961 174.720 1.00 37.07 ?  616 PRO B O     1 
ATOM   10502 C  CB    . PRO B 1 616 ? 134.402 130.522 172.780 1.00 34.26 ?  616 PRO B CB    1 
ATOM   10503 C  CG    . PRO B 1 616 ? 134.229 130.398 171.303 1.00 33.99 ?  616 PRO B CG    1 
ATOM   10504 C  CD    . PRO B 1 616 ? 133.576 129.081 171.078 1.00 33.29 ?  616 PRO B CD    1 
ATOM   10505 N  N     . GLY B 1 617 ? 134.752 128.441 175.592 1.00 35.39 ?  617 GLY B N     1 
ATOM   10506 C  CA    . GLY B 1 617 ? 134.219 128.126 176.898 1.00 33.60 ?  617 GLY B CA    1 
ATOM   10507 C  C     . GLY B 1 617 ? 133.674 126.726 177.050 1.00 38.16 ?  617 GLY B C     1 
ATOM   10508 O  O     . GLY B 1 617 ? 133.078 126.424 178.090 1.00 41.04 ?  617 GLY B O     1 
ATOM   10509 N  N     . LEU B 1 618 ? 133.849 125.866 176.049 1.00 38.93 ?  618 LEU B N     1 
ATOM   10510 C  CA    . LEU B 1 618 ? 133.376 124.493 176.155 1.00 33.74 ?  618 LEU B CA    1 
ATOM   10511 C  C     . LEU B 1 618 ? 134.134 123.754 177.249 1.00 36.51 ?  618 LEU B C     1 
ATOM   10512 O  O     . LEU B 1 618 ? 135.359 123.858 177.359 1.00 38.95 ?  618 LEU B O     1 
ATOM   10513 C  CB    . LEU B 1 618 ? 133.537 123.772 174.816 1.00 30.87 ?  618 LEU B CB    1 
ATOM   10514 C  CG    . LEU B 1 618 ? 133.064 122.318 174.749 1.00 35.47 ?  618 LEU B CG    1 
ATOM   10515 C  CD1   . LEU B 1 618 ? 131.568 122.222 174.998 1.00 36.01 ?  618 LEU B CD1   1 
ATOM   10516 C  CD2   . LEU B 1 618 ? 133.429 121.700 173.410 1.00 35.81 ?  618 LEU B CD2   1 
ATOM   10517 N  N     . ALA B 1 619 ? 133.398 123.006 178.060 1.00 42.84 ?  619 ALA B N     1 
ATOM   10518 C  CA    . ALA B 1 619 ? 133.971 122.268 179.177 1.00 42.21 ?  619 ALA B CA    1 
ATOM   10519 C  C     . ALA B 1 619 ? 133.004 121.150 179.551 1.00 43.92 ?  619 ALA B C     1 
ATOM   10520 O  O     . ALA B 1 619 ? 132.008 120.912 178.859 1.00 49.67 ?  619 ALA B O     1 
ATOM   10521 C  CB    . ALA B 1 619 ? 134.263 123.200 180.357 1.00 41.95 ?  619 ALA B CB    1 
ATOM   10522 N  N     . SER B 1 620 ? 133.303 120.456 180.650 1.00 47.85 ?  620 SER B N     1 
ATOM   10523 C  CA    . SER B 1 620 ? 132.443 119.361 181.088 1.00 49.40 ?  620 SER B CA    1 
ATOM   10524 C  C     . SER B 1 620 ? 131.112 119.876 181.623 1.00 49.40 ?  620 SER B C     1 
ATOM   10525 O  O     . SER B 1 620 ? 130.061 119.281 181.363 1.00 51.23 ?  620 SER B O     1 
ATOM   10526 C  CB    . SER B 1 620 ? 133.159 118.527 182.149 1.00 50.49 ?  620 SER B CB    1 
ATOM   10527 O  OG    . SER B 1 620 ? 134.550 118.454 181.887 1.00 53.13 ?  620 SER B OG    1 
ATOM   10528 N  N     . ASN B 1 621 ? 131.135 120.981 182.371 1.00 47.53 ?  621 ASN B N     1 
ATOM   10529 C  CA    . ASN B 1 621 ? 129.917 121.475 183.002 1.00 49.06 ?  621 ASN B CA    1 
ATOM   10530 C  C     . ASN B 1 621 ? 128.960 122.122 182.009 1.00 50.49 ?  621 ASN B C     1 
ATOM   10531 O  O     . ASN B 1 621 ? 127.755 122.167 182.274 1.00 51.11 ?  621 ASN B O     1 
ATOM   10532 C  CB    . ASN B 1 621 ? 130.265 122.472 184.109 1.00 48.58 ?  621 ASN B CB    1 
ATOM   10533 C  CG    . ASN B 1 621 ? 131.163 123.591 183.625 1.00 51.79 ?  621 ASN B CG    1 
ATOM   10534 O  OD1   . ASN B 1 621 ? 131.963 123.407 182.708 1.00 54.59 ?  621 ASN B OD1   1 
ATOM   10535 N  ND2   . ASN B 1 621 ? 131.035 124.760 184.240 1.00 50.11 ?  621 ASN B ND2   1 
ATOM   10536 N  N     . ASN B 1 622 ? 129.460 122.618 180.878 1.00 42.43 ?  622 ASN B N     1 
ATOM   10537 C  CA    . ASN B 1 622 ? 128.621 123.257 179.872 1.00 42.64 ?  622 ASN B CA    1 
ATOM   10538 C  C     . ASN B 1 622 ? 128.673 122.512 178.541 1.00 45.50 ?  622 ASN B C     1 
ATOM   10539 O  O     . ASN B 1 622 ? 128.463 123.107 177.482 1.00 48.48 ?  622 ASN B O     1 
ATOM   10540 C  CB    . ASN B 1 622 ? 129.012 124.725 179.688 1.00 42.25 ?  622 ASN B CB    1 
ATOM   10541 C  CG    . ASN B 1 622 ? 130.464 124.905 179.275 1.00 43.85 ?  622 ASN B CG    1 
ATOM   10542 O  OD1   . ASN B 1 622 ? 131.161 123.942 178.959 1.00 45.91 ?  622 ASN B OD1   1 
ATOM   10543 N  ND2   . ASN B 1 622 ? 130.925 126.149 179.279 1.00 41.49 ?  622 ASN B ND2   1 
ATOM   10544 N  N     . TRP B 1 623 ? 128.964 121.210 178.583 1.00 40.13 ?  623 TRP B N     1 
ATOM   10545 C  CA    . TRP B 1 623 ? 129.008 120.427 177.352 1.00 38.16 ?  623 TRP B CA    1 
ATOM   10546 C  C     . TRP B 1 623 ? 127.632 120.333 176.706 1.00 39.87 ?  623 TRP B C     1 
ATOM   10547 O  O     . TRP B 1 623 ? 127.497 120.512 175.490 1.00 42.48 ?  623 TRP B O     1 
ATOM   10548 C  CB    . TRP B 1 623 ? 129.565 119.032 177.636 1.00 42.24 ?  623 TRP B CB    1 
ATOM   10549 C  CG    . TRP B 1 623 ? 129.512 118.106 176.456 1.00 40.48 ?  623 TRP B CG    1 
ATOM   10550 C  CD1   . TRP B 1 623 ? 128.471 117.304 176.090 1.00 39.05 ?  623 TRP B CD1   1 
ATOM   10551 C  CD2   . TRP B 1 623 ? 130.546 117.889 175.488 1.00 39.60 ?  623 TRP B CD2   1 
ATOM   10552 N  NE1   . TRP B 1 623 ? 128.791 116.601 174.955 1.00 40.20 ?  623 TRP B NE1   1 
ATOM   10553 C  CE2   . TRP B 1 623 ? 130.060 116.940 174.566 1.00 39.80 ?  623 TRP B CE2   1 
ATOM   10554 C  CE3   . TRP B 1 623 ? 131.833 118.402 175.312 1.00 40.04 ?  623 TRP B CE3   1 
ATOM   10555 C  CZ2   . TRP B 1 623 ? 130.815 116.498 173.483 1.00 39.15 ?  623 TRP B CZ2   1 
ATOM   10556 C  CZ3   . TRP B 1 623 ? 132.582 117.960 174.237 1.00 39.84 ?  623 TRP B CZ3   1 
ATOM   10557 C  CH2   . TRP B 1 623 ? 132.071 117.018 173.336 1.00 39.02 ?  623 TRP B CH2   1 
ATOM   10558 N  N     . PHE B 1 624 ? 126.598 120.056 177.500 1.00 44.42 ?  624 PHE B N     1 
ATOM   10559 C  CA    . PHE B 1 624 ? 125.255 119.900 176.958 1.00 44.06 ?  624 PHE B CA    1 
ATOM   10560 C  C     . PHE B 1 624 ? 124.537 121.224 176.745 1.00 41.51 ?  624 PHE B C     1 
ATOM   10561 O  O     . PHE B 1 624 ? 123.527 121.252 176.034 1.00 46.26 ?  624 PHE B O     1 
ATOM   10562 C  CB    . PHE B 1 624 ? 124.425 118.994 177.868 1.00 42.66 ?  624 PHE B CB    1 
ATOM   10563 C  CG    . PHE B 1 624 ? 124.868 117.560 177.851 1.00 44.84 ?  624 PHE B CG    1 
ATOM   10564 C  CD1   . PHE B 1 624 ? 124.476 116.716 176.826 1.00 42.91 ?  624 PHE B CD1   1 
ATOM   10565 C  CD2   . PHE B 1 624 ? 125.685 117.059 178.850 1.00 45.60 ?  624 PHE B CD2   1 
ATOM   10566 C  CE1   . PHE B 1 624 ? 124.884 115.397 176.803 1.00 42.49 ?  624 PHE B CE1   1 
ATOM   10567 C  CE2   . PHE B 1 624 ? 126.097 115.741 178.831 1.00 45.60 ?  624 PHE B CE2   1 
ATOM   10568 C  CZ    . PHE B 1 624 ? 125.695 114.909 177.806 1.00 45.64 ?  624 PHE B CZ    1 
ATOM   10569 N  N     . PHE B 1 625 ? 125.023 122.316 177.337 1.00 37.19 ?  625 PHE B N     1 
ATOM   10570 C  CA    . PHE B 1 625 ? 124.507 123.631 176.980 1.00 32.73 ?  625 PHE B CA    1 
ATOM   10571 C  C     . PHE B 1 625 ? 125.021 124.086 175.624 1.00 30.95 ?  625 PHE B C     1 
ATOM   10572 O  O     . PHE B 1 625 ? 124.377 124.916 174.975 1.00 33.43 ?  625 PHE B O     1 
ATOM   10573 C  CB    . PHE B 1 625 ? 124.869 124.654 178.057 1.00 29.88 ?  625 PHE B CB    1 
ATOM   10574 C  CG    . PHE B 1 625 ? 124.020 124.557 179.290 1.00 32.89 ?  625 PHE B CG    1 
ATOM   10575 C  CD1   . PHE B 1 625 ? 122.664 124.831 179.235 1.00 33.41 ?  625 PHE B CD1   1 
ATOM   10576 C  CD2   . PHE B 1 625 ? 124.575 124.188 180.504 1.00 33.39 ?  625 PHE B CD2   1 
ATOM   10577 C  CE1   . PHE B 1 625 ? 121.879 124.742 180.367 1.00 33.55 ?  625 PHE B CE1   1 
ATOM   10578 C  CE2   . PHE B 1 625 ? 123.794 124.098 181.638 1.00 35.07 ?  625 PHE B CE2   1 
ATOM   10579 C  CZ    . PHE B 1 625 ? 122.444 124.376 181.570 1.00 35.94 ?  625 PHE B CZ    1 
ATOM   10580 N  N     . TYR B 1 626 ? 126.159 123.558 175.184 1.00 29.75 ?  626 TYR B N     1 
ATOM   10581 C  CA    . TYR B 1 626 ? 126.665 123.795 173.834 1.00 29.27 ?  626 TYR B CA    1 
ATOM   10582 C  C     . TYR B 1 626 ? 126.061 122.805 172.845 1.00 32.33 ?  626 TYR B C     1 
ATOM   10583 O  O     . TYR B 1 626 ? 126.763 122.123 172.101 1.00 35.80 ?  626 TYR B O     1 
ATOM   10584 C  CB    . TYR B 1 626 ? 128.186 123.720 173.827 1.00 31.54 ?  626 TYR B CB    1 
ATOM   10585 C  CG    . TYR B 1 626 ? 128.857 125.067 173.909 1.00 29.75 ?  626 TYR B CG    1 
ATOM   10586 C  CD1   . TYR B 1 626 ? 128.776 125.967 172.856 1.00 33.90 ?  626 TYR B CD1   1 
ATOM   10587 C  CD2   . TYR B 1 626 ? 129.572 125.440 175.038 1.00 28.57 ?  626 TYR B CD2   1 
ATOM   10588 C  CE1   . TYR B 1 626 ? 129.385 127.201 172.924 1.00 30.73 ?  626 TYR B CE1   1 
ATOM   10589 C  CE2   . TYR B 1 626 ? 130.185 126.673 175.116 1.00 31.89 ?  626 TYR B CE2   1 
ATOM   10590 C  CZ    . TYR B 1 626 ? 130.089 127.548 174.055 1.00 33.56 ?  626 TYR B CZ    1 
ATOM   10591 O  OH    . TYR B 1 626 ? 130.697 128.778 174.123 1.00 36.80 ?  626 TYR B OH    1 
ATOM   10592 N  N     . LYS B 1 627 ? 124.733 122.725 172.845 1.00 33.36 ?  627 LYS B N     1 
ATOM   10593 C  CA    . LYS B 1 627 ? 124.032 121.801 171.966 1.00 31.32 ?  627 LYS B CA    1 
ATOM   10594 C  C     . LYS B 1 627 ? 124.286 122.159 170.508 1.00 31.42 ?  627 LYS B C     1 
ATOM   10595 O  O     . LYS B 1 627 ? 124.242 123.329 170.121 1.00 34.42 ?  627 LYS B O     1 
ATOM   10596 C  CB    . LYS B 1 627 ? 122.535 121.833 172.269 1.00 32.93 ?  627 LYS B CB    1 
ATOM   10597 C  CG    . LYS B 1 627 ? 121.710 120.805 171.522 1.00 33.39 ?  627 LYS B CG    1 
ATOM   10598 C  CD    . LYS B 1 627 ? 120.272 120.822 172.007 1.00 30.93 ?  627 LYS B CD    1 
ATOM   10599 C  CE    . LYS B 1 627 ? 119.409 119.848 171.229 1.00 36.51 ?  627 LYS B CE    1 
ATOM   10600 N  NZ    . LYS B 1 627 ? 117.980 119.941 171.635 1.00 36.73 1  627 LYS B NZ    1 
ATOM   10601 N  N     . GLU B 1 628 ? 124.562 121.140 169.699 1.00 33.49 ?  628 GLU B N     1 
ATOM   10602 C  CA    . GLU B 1 628 ? 124.820 121.369 168.287 1.00 33.47 ?  628 GLU B CA    1 
ATOM   10603 C  C     . GLU B 1 628 ? 123.543 121.792 167.572 1.00 35.41 ?  628 GLU B C     1 
ATOM   10604 O  O     . GLU B 1 628 ? 122.437 121.372 167.923 1.00 39.24 ?  628 GLU B O     1 
ATOM   10605 C  CB    . GLU B 1 628 ? 125.404 120.114 167.640 1.00 35.21 ?  628 GLU B CB    1 
ATOM   10606 C  CG    . GLU B 1 628 ? 126.831 119.822 168.068 1.00 33.53 ?  628 GLU B CG    1 
ATOM   10607 C  CD    . GLU B 1 628 ? 127.431 118.637 167.341 1.00 41.02 ?  628 GLU B CD    1 
ATOM   10608 O  OE1   . GLU B 1 628 ? 126.829 118.181 166.346 1.00 41.66 ?  628 GLU B OE1   1 
ATOM   10609 O  OE2   . GLU B 1 628 ? 128.506 118.163 167.762 1.00 38.10 -1 628 GLU B OE2   1 
ATOM   10610 N  N     . ALA B 1 629 ? 123.710 122.643 166.558 1.00 33.48 ?  629 ALA B N     1 
ATOM   10611 C  CA    . ALA B 1 629 ? 122.562 123.222 165.868 1.00 28.50 ?  629 ALA B CA    1 
ATOM   10612 C  C     . ALA B 1 629 ? 121.727 122.155 165.172 1.00 33.82 ?  629 ALA B C     1 
ATOM   10613 O  O     . ALA B 1 629 ? 120.493 122.236 165.158 1.00 41.85 ?  629 ALA B O     1 
ATOM   10614 C  CB    . ALA B 1 629 ? 123.034 124.271 164.865 1.00 29.76 ?  629 ALA B CB    1 
ATOM   10615 N  N     . TYR B 1 630 ? 122.380 121.153 164.580 1.00 39.39 ?  630 TYR B N     1 
ATOM   10616 C  CA    . TYR B 1 630 ? 121.646 120.112 163.868 1.00 37.06 ?  630 TYR B CA    1 
ATOM   10617 C  C     . TYR B 1 630 ? 120.766 119.298 164.807 1.00 39.49 ?  630 TYR B C     1 
ATOM   10618 O  O     . TYR B 1 630 ? 119.704 118.818 164.395 1.00 42.63 ?  630 TYR B O     1 
ATOM   10619 C  CB    . TYR B 1 630 ? 122.620 119.201 163.124 1.00 34.90 ?  630 TYR B CB    1 
ATOM   10620 C  CG    . TYR B 1 630 ? 123.498 119.934 162.138 1.00 37.14 ?  630 TYR B CG    1 
ATOM   10621 C  CD1   . TYR B 1 630 ? 123.013 120.307 160.892 1.00 33.86 ?  630 TYR B CD1   1 
ATOM   10622 C  CD2   . TYR B 1 630 ? 124.810 120.254 162.453 1.00 37.66 ?  630 TYR B CD2   1 
ATOM   10623 C  CE1   . TYR B 1 630 ? 123.810 120.979 159.989 1.00 37.39 ?  630 TYR B CE1   1 
ATOM   10624 C  CE2   . TYR B 1 630 ? 125.616 120.925 161.555 1.00 36.27 ?  630 TYR B CE2   1 
ATOM   10625 C  CZ    . TYR B 1 630 ? 125.111 121.285 160.325 1.00 39.87 ?  630 TYR B CZ    1 
ATOM   10626 O  OH    . TYR B 1 630 ? 125.908 121.953 159.426 1.00 43.03 ?  630 TYR B OH    1 
ATOM   10627 N  N     . ASP B 1 631 ? 121.180 119.138 166.063 1.00 36.75 ?  631 ASP B N     1 
ATOM   10628 C  CA    . ASP B 1 631 ? 120.379 118.419 167.043 1.00 32.70 ?  631 ASP B CA    1 
ATOM   10629 C  C     . ASP B 1 631 ? 119.236 119.255 167.603 1.00 37.19 ?  631 ASP B C     1 
ATOM   10630 O  O     . ASP B 1 631 ? 118.398 118.719 168.335 1.00 39.80 ?  631 ASP B O     1 
ATOM   10631 C  CB    . ASP B 1 631 ? 121.266 117.936 168.193 1.00 34.41 ?  631 ASP B CB    1 
ATOM   10632 C  CG    . ASP B 1 631 ? 122.388 117.032 167.723 1.00 41.11 ?  631 ASP B CG    1 
ATOM   10633 O  OD1   . ASP B 1 631 ? 122.136 116.166 166.860 1.00 43.19 ?  631 ASP B OD1   1 
ATOM   10634 O  OD2   . ASP B 1 631 ? 123.525 117.188 168.217 1.00 42.19 -1 631 ASP B OD2   1 
ATOM   10635 N  N     . MET B 1 632 ? 119.180 120.542 167.276 1.00 36.47 ?  632 MET B N     1 
ATOM   10636 C  CA    . MET B 1 632 ? 118.190 121.446 167.838 1.00 32.57 ?  632 MET B CA    1 
ATOM   10637 C  C     . MET B 1 632 ? 116.913 121.442 167.010 1.00 34.91 ?  632 MET B C     1 
ATOM   10638 O  O     . MET B 1 632 ? 116.920 121.134 165.815 1.00 34.50 ?  632 MET B O     1 
ATOM   10639 C  CB    . MET B 1 632 ? 118.741 122.870 167.907 1.00 31.54 ?  632 MET B CB    1 
ATOM   10640 C  CG    . MET B 1 632 ? 119.877 123.049 168.888 1.00 36.57 ?  632 MET B CG    1 
ATOM   10641 S  SD    . MET B 1 632 ? 120.467 124.745 168.938 1.00 39.71 ?  632 MET B SD    1 
ATOM   10642 C  CE    . MET B 1 632 ? 121.297 124.752 170.520 1.00 30.53 ?  632 MET B CE    1 
ATOM   10643 N  N     . ASP B 1 633 ? 115.809 121.791 167.664 1.00 33.36 ?  633 ASP B N     1 
ATOM   10644 C  CA    . ASP B 1 633 ? 114.551 122.004 166.964 1.00 26.12 ?  633 ASP B CA    1 
ATOM   10645 C  C     . ASP B 1 633 ? 114.630 123.304 166.176 1.00 31.27 ?  633 ASP B C     1 
ATOM   10646 O  O     . ASP B 1 633 ? 114.835 124.376 166.755 1.00 37.33 ?  633 ASP B O     1 
ATOM   10647 C  CB    . ASP B 1 633 ? 113.394 122.046 167.958 1.00 28.86 ?  633 ASP B CB    1 
ATOM   10648 C  CG    . ASP B 1 633 ? 112.039 122.024 167.280 1.00 36.59 ?  633 ASP B CG    1 
ATOM   10649 O  OD1   . ASP B 1 633 ? 111.988 121.825 166.049 1.00 39.85 ?  633 ASP B OD1   1 
ATOM   10650 O  OD2   . ASP B 1 633 ? 111.022 122.208 167.980 1.00 35.97 -1 633 ASP B OD2   1 
ATOM   10651 N  N     . MET B 1 634 ? 114.474 123.213 164.854 1.00 28.97 ?  634 MET B N     1 
ATOM   10652 C  CA    . MET B 1 634 ? 114.550 124.406 164.021 1.00 19.79 ?  634 MET B CA    1 
ATOM   10653 C  C     . MET B 1 634 ? 113.423 125.387 164.309 1.00 23.83 ?  634 MET B C     1 
ATOM   10654 O  O     . MET B 1 634 ? 113.572 126.578 164.024 1.00 30.66 ?  634 MET B O     1 
ATOM   10655 C  CB    . MET B 1 634 ? 114.539 124.022 162.541 1.00 24.77 ?  634 MET B CB    1 
ATOM   10656 C  CG    . MET B 1 634 ? 115.918 123.931 161.899 1.00 26.45 ?  634 MET B CG    1 
ATOM   10657 S  SD    . MET B 1 634 ? 117.064 125.209 162.451 1.00 40.68 ?  634 MET B SD    1 
ATOM   10658 C  CE    . MET B 1 634 ? 118.140 124.266 163.530 1.00 27.98 ?  634 MET B CE    1 
ATOM   10659 N  N     . PHE B 1 635 ? 112.306 124.918 164.869 1.00 22.81 ?  635 PHE B N     1 
ATOM   10660 C  CA    . PHE B 1 635 ? 111.217 125.829 165.213 1.00 23.82 ?  635 PHE B CA    1 
ATOM   10661 C  C     . PHE B 1 635 ? 111.615 126.758 166.353 1.00 20.23 ?  635 PHE B C     1 
ATOM   10662 O  O     . PHE B 1 635 ? 111.297 127.952 166.331 1.00 23.00 ?  635 PHE B O     1 
ATOM   10663 C  CB    . PHE B 1 635 ? 109.966 125.032 165.576 1.00 22.81 ?  635 PHE B CB    1 
ATOM   10664 C  CG    . PHE B 1 635 ? 109.083 124.725 164.400 1.00 23.55 ?  635 PHE B CG    1 
ATOM   10665 C  CD1   . PHE B 1 635 ? 109.631 124.315 163.197 1.00 25.61 ?  635 PHE B CD1   1 
ATOM   10666 C  CD2   . PHE B 1 635 ? 107.708 124.845 164.499 1.00 24.32 ?  635 PHE B CD2   1 
ATOM   10667 C  CE1   . PHE B 1 635 ? 108.825 124.031 162.112 1.00 22.74 ?  635 PHE B CE1   1 
ATOM   10668 C  CE2   . PHE B 1 635 ? 106.897 124.562 163.417 1.00 25.49 ?  635 PHE B CE2   1 
ATOM   10669 C  CZ    . PHE B 1 635 ? 107.456 124.155 162.222 1.00 23.57 ?  635 PHE B CZ    1 
ATOM   10670 N  N     . LYS B 1 636 ? 112.330 126.236 167.351 1.00 26.75 ?  636 LYS B N     1 
ATOM   10671 C  CA    . LYS B 1 636 ? 112.786 127.079 168.449 1.00 29.79 ?  636 LYS B CA    1 
ATOM   10672 C  C     . LYS B 1 636 ? 113.918 128.006 168.020 1.00 26.40 ?  636 LYS B C     1 
ATOM   10673 O  O     . LYS B 1 636 ? 114.021 129.130 168.525 1.00 29.33 ?  636 LYS B O     1 
ATOM   10674 C  CB    . LYS B 1 636 ? 113.215 126.207 169.628 1.00 27.22 ?  636 LYS B CB    1 
ATOM   10675 C  CG    . LYS B 1 636 ? 112.080 125.366 170.192 1.00 27.67 ?  636 LYS B CG    1 
ATOM   10676 C  CD    . LYS B 1 636 ? 112.477 124.675 171.482 1.00 33.78 ?  636 LYS B CD    1 
ATOM   10677 C  CE    . LYS B 1 636 ? 111.380 123.744 171.969 1.00 33.82 ?  636 LYS B CE    1 
ATOM   10678 N  NZ    . LYS B 1 636 ? 111.820 122.933 173.136 1.00 35.15 1  636 LYS B NZ    1 
ATOM   10679 N  N     . VAL B 1 637 ? 114.757 127.568 167.080 1.00 22.60 ?  637 VAL B N     1 
ATOM   10680 C  CA    . VAL B 1 637 ? 115.744 128.473 166.502 1.00 19.51 ?  637 VAL B CA    1 
ATOM   10681 C  C     . VAL B 1 637 ? 115.048 129.586 165.727 1.00 25.77 ?  637 VAL B C     1 
ATOM   10682 O  O     . VAL B 1 637 ? 115.475 130.746 165.766 1.00 26.46 ?  637 VAL B O     1 
ATOM   10683 C  CB    . VAL B 1 637 ? 116.732 127.692 165.618 1.00 19.65 ?  637 VAL B CB    1 
ATOM   10684 C  CG1   . VAL B 1 637 ? 117.864 128.596 165.160 1.00 20.23 ?  637 VAL B CG1   1 
ATOM   10685 C  CG2   . VAL B 1 637 ? 117.282 126.494 166.372 1.00 24.93 ?  637 VAL B CG2   1 
ATOM   10686 N  N     . VAL B 1 638 ? 113.966 129.256 165.018 1.00 20.68 ?  638 VAL B N     1 
ATOM   10687 C  CA    . VAL B 1 638 ? 113.171 130.276 164.339 1.00 20.02 ?  638 VAL B CA    1 
ATOM   10688 C  C     . VAL B 1 638 ? 112.579 131.247 165.352 1.00 20.80 ?  638 VAL B C     1 
ATOM   10689 O  O     . VAL B 1 638 ? 112.532 132.460 165.119 1.00 28.07 ?  638 VAL B O     1 
ATOM   10690 C  CB    . VAL B 1 638 ? 112.072 129.618 163.481 1.00 22.27 ?  638 VAL B CB    1 
ATOM   10691 C  CG1   . VAL B 1 638 ? 110.998 130.628 163.120 1.00 16.86 ?  638 VAL B CG1   1 
ATOM   10692 C  CG2   . VAL B 1 638 ? 112.664 129.007 162.226 1.00 18.92 ?  638 VAL B CG2   1 
ATOM   10693 N  N     . ASP B 1 639 ? 112.106 130.726 166.486 1.00 21.40 ?  639 ASP B N     1 
ATOM   10694 C  CA    . ASP B 1 639 ? 111.579 131.589 167.538 1.00 16.39 ?  639 ASP B CA    1 
ATOM   10695 C  C     . ASP B 1 639 ? 112.646 132.547 168.053 1.00 22.64 ?  639 ASP B C     1 
ATOM   10696 O  O     . ASP B 1 639 ? 112.384 133.742 168.234 1.00 31.87 ?  639 ASP B O     1 
ATOM   10697 C  CB    . ASP B 1 639 ? 111.028 130.741 168.683 1.00 20.16 ?  639 ASP B CB    1 
ATOM   10698 C  CG    . ASP B 1 639 ? 109.670 130.156 168.373 1.00 30.99 ?  639 ASP B CG    1 
ATOM   10699 O  OD1   . ASP B 1 639 ? 108.865 130.841 167.707 1.00 30.17 ?  639 ASP B OD1   1 
ATOM   10700 O  OD2   . ASP B 1 639 ? 109.403 129.013 168.797 1.00 33.70 -1 639 ASP B OD2   1 
ATOM   10701 N  N     . MET B 1 640 ? 113.858 132.038 168.290 1.00 20.10 ?  640 MET B N     1 
ATOM   10702 C  CA    . MET B 1 640 ? 114.960 132.899 168.712 1.00 16.85 ?  640 MET B CA    1 
ATOM   10703 C  C     . MET B 1 640 ? 115.263 133.968 167.671 1.00 18.80 ?  640 MET B C     1 
ATOM   10704 O  O     . MET B 1 640 ? 115.455 135.145 168.004 1.00 24.56 ?  640 MET B O     1 
ATOM   10705 C  CB    . MET B 1 640 ? 116.210 132.065 168.983 1.00 18.97 ?  640 MET B CB    1 
ATOM   10706 C  CG    . MET B 1 640 ? 117.403 132.907 169.402 1.00 23.29 ?  640 MET B CG    1 
ATOM   10707 S  SD    . MET B 1 640 ? 117.361 133.441 171.116 1.00 26.94 ?  640 MET B SD    1 
ATOM   10708 C  CE    . MET B 1 640 ? 118.291 132.121 171.872 1.00 20.08 ?  640 MET B CE    1 
ATOM   10709 N  N     . ILE B 1 641 ? 115.327 133.571 166.400 1.00 22.96 ?  641 ILE B N     1 
ATOM   10710 C  CA    . ILE B 1 641 ? 115.700 134.519 165.359 1.00 18.61 ?  641 ILE B CA    1 
ATOM   10711 C  C     . ILE B 1 641 ? 114.619 135.577 165.188 1.00 17.77 ?  641 ILE B C     1 
ATOM   10712 O  O     . ILE B 1 641 ? 114.920 136.745 164.946 1.00 25.68 ?  641 ILE B O     1 
ATOM   10713 C  CB    . ILE B 1 641 ? 116.009 133.786 164.040 1.00 23.86 ?  641 ILE B CB    1 
ATOM   10714 C  CG1   . ILE B 1 641 ? 117.182 132.825 164.234 1.00 22.05 ?  641 ILE B CG1   1 
ATOM   10715 C  CG2   . ILE B 1 641 ? 116.362 134.778 162.948 1.00 13.33 ?  641 ILE B CG2   1 
ATOM   10716 C  CD1   . ILE B 1 641 ? 118.311 133.397 165.061 1.00 20.77 ?  641 ILE B CD1   1 
ATOM   10717 N  N     . ALA B 1 642 ? 113.348 135.194 165.334 1.00 9.77  ?  642 ALA B N     1 
ATOM   10718 C  CA    . ALA B 1 642 ? 112.266 136.174 165.275 1.00 17.35 ?  642 ALA B CA    1 
ATOM   10719 C  C     . ALA B 1 642 ? 112.310 137.121 166.468 1.00 19.47 ?  642 ALA B C     1 
ATOM   10720 O  O     . ALA B 1 642 ? 112.065 138.329 166.325 1.00 29.13 ?  642 ALA B O     1 
ATOM   10721 C  CB    . ALA B 1 642 ? 110.917 135.461 165.205 1.00 23.44 ?  642 ALA B CB    1 
ATOM   10722 N  N     . THR B 1 643 ? 112.622 136.591 167.654 1.00 13.83 ?  643 THR B N     1 
ATOM   10723 C  CA    . THR B 1 643 ? 112.754 137.436 168.835 1.00 15.50 ?  643 THR B CA    1 
ATOM   10724 C  C     . THR B 1 643 ? 113.859 138.466 168.651 1.00 18.38 ?  643 THR B C     1 
ATOM   10725 O  O     . THR B 1 643 ? 113.698 139.635 169.020 1.00 22.78 ?  643 THR B O     1 
ATOM   10726 C  CB    . THR B 1 643 ? 113.027 136.570 170.065 1.00 18.85 ?  643 THR B CB    1 
ATOM   10727 O  OG1   . THR B 1 643 ? 111.959 135.631 170.238 1.00 23.42 ?  643 THR B OG1   1 
ATOM   10728 C  CG2   . THR B 1 643 ? 113.141 137.429 171.308 1.00 17.01 ?  643 THR B CG2   1 
ATOM   10729 N  N     . ILE B 1 644 ? 114.992 138.051 168.085 1.00 16.84 ?  644 ILE B N     1 
ATOM   10730 C  CA    . ILE B 1 644 ? 116.060 139.003 167.797 1.00 12.86 ?  644 ILE B CA    1 
ATOM   10731 C  C     . ILE B 1 644 ? 115.641 139.960 166.686 1.00 16.93 ?  644 ILE B C     1 
ATOM   10732 O  O     . ILE B 1 644 ? 115.926 141.162 166.740 1.00 23.05 ?  644 ILE B O     1 
ATOM   10733 C  CB    . ILE B 1 644 ? 117.359 138.259 167.443 1.00 14.99 ?  644 ILE B CB    1 
ATOM   10734 C  CG1   . ILE B 1 644 ? 117.769 137.328 168.583 1.00 15.83 ?  644 ILE B CG1   1 
ATOM   10735 C  CG2   . ILE B 1 644 ? 118.466 139.246 167.139 1.00 10.19 ?  644 ILE B CG2   1 
ATOM   10736 C  CD1   . ILE B 1 644 ? 118.840 136.339 168.198 1.00 18.65 ?  644 ILE B CD1   1 
ATOM   10737 N  N     . GLN B 1 645 ? 114.944 139.444 165.670 1.00 7.72  ?  645 GLN B N     1 
ATOM   10738 C  CA    . GLN B 1 645 ? 114.607 140.217 164.484 1.00 14.27 ?  645 GLN B CA    1 
ATOM   10739 C  C     . GLN B 1 645 ? 113.639 141.344 164.800 1.00 20.95 ?  645 GLN B C     1 
ATOM   10740 O  O     . GLN B 1 645 ? 113.655 142.382 164.127 1.00 28.01 ?  645 GLN B O     1 
ATOM   10741 C  CB    . GLN B 1 645 ? 114.011 139.289 163.426 1.00 12.79 ?  645 GLN B CB    1 
ATOM   10742 C  CG    . GLN B 1 645 ? 113.668 139.959 162.114 1.00 10.57 ?  645 GLN B CG    1 
ATOM   10743 C  CD    . GLN B 1 645 ? 114.878 140.115 161.223 1.00 15.11 ?  645 GLN B CD    1 
ATOM   10744 O  OE1   . GLN B 1 645 ? 115.554 141.137 161.258 1.00 8.69  ?  645 GLN B OE1   1 
ATOM   10745 N  NE2   . GLN B 1 645 ? 115.157 139.098 160.418 1.00 17.69 ?  645 GLN B NE2   1 
ATOM   10746 N  N     . GLN B 1 646 ? 112.790 141.161 165.811 1.00 18.85 ?  646 GLN B N     1 
ATOM   10747 C  CA    . GLN B 1 646 ? 111.864 142.226 166.177 1.00 16.53 ?  646 GLN B CA    1 
ATOM   10748 C  C     . GLN B 1 646 ? 112.588 143.494 166.619 1.00 13.75 ?  646 GLN B C     1 
ATOM   10749 O  O     . GLN B 1 646 ? 111.988 144.573 166.595 1.00 21.39 ?  646 GLN B O     1 
ATOM   10750 C  CB    . GLN B 1 646 ? 110.913 141.739 167.272 1.00 19.98 ?  646 GLN B CB    1 
ATOM   10751 C  CG    . GLN B 1 646 ? 111.467 141.830 168.673 1.00 21.39 ?  646 GLN B CG    1 
ATOM   10752 C  CD    . GLN B 1 646 ? 110.524 141.248 169.704 1.00 27.82 ?  646 GLN B CD    1 
ATOM   10753 O  OE1   . GLN B 1 646 ? 110.838 140.253 170.357 1.00 25.23 ?  646 GLN B OE1   1 
ATOM   10754 N  NE2   . GLN B 1 646 ? 109.359 141.865 169.855 1.00 27.04 ?  646 GLN B NE2   1 
ATOM   10755 N  N     . HIS B 1 647 ? 113.862 143.397 166.997 1.00 22.19 ?  647 HIS B N     1 
ATOM   10756 C  CA    . HIS B 1 647 ? 114.653 144.554 167.396 1.00 19.27 ?  647 HIS B CA    1 
ATOM   10757 C  C     . HIS B 1 647 ? 115.718 144.938 166.379 1.00 16.97 ?  647 HIS B C     1 
ATOM   10758 O  O     . HIS B 1 647 ? 116.466 145.891 166.617 1.00 22.98 ?  647 HIS B O     1 
ATOM   10759 C  CB    . HIS B 1 647 ? 115.317 144.298 168.753 1.00 13.76 ?  647 HIS B CB    1 
ATOM   10760 C  CG    . HIS B 1 647 ? 114.358 143.888 169.826 1.00 17.51 ?  647 HIS B CG    1 
ATOM   10761 N  ND1   . HIS B 1 647 ? 113.375 144.727 170.303 1.00 13.19 ?  647 HIS B ND1   1 
ATOM   10762 C  CD2   . HIS B 1 647 ? 114.233 142.729 170.513 1.00 16.95 ?  647 HIS B CD2   1 
ATOM   10763 C  CE1   . HIS B 1 647 ? 112.685 144.102 171.239 1.00 19.01 ?  647 HIS B CE1   1 
ATOM   10764 N  NE2   . HIS B 1 647 ? 113.184 142.889 171.386 1.00 21.98 ?  647 HIS B NE2   1 
ATOM   10765 N  N     . ILE B 1 648 ? 115.810 144.230 165.256 1.00 12.68 ?  648 ILE B N     1 
ATOM   10766 C  CA    . ILE B 1 648 ? 116.796 144.504 164.218 1.00 11.44 ?  648 ILE B CA    1 
ATOM   10767 C  C     . ILE B 1 648 ? 116.067 145.088 163.016 1.00 16.81 ?  648 ILE B C     1 
ATOM   10768 O  O     . ILE B 1 648 ? 115.119 144.480 162.504 1.00 27.46 ?  648 ILE B O     1 
ATOM   10769 C  CB    . ILE B 1 648 ? 117.574 143.233 163.833 1.00 13.28 ?  648 ILE B CB    1 
ATOM   10770 C  CG1   . ILE B 1 648 ? 118.235 142.614 165.065 1.00 16.65 ?  648 ILE B CG1   1 
ATOM   10771 C  CG2   . ILE B 1 648 ? 118.617 143.541 162.777 1.00 5.40  ?  648 ILE B CG2   1 
ATOM   10772 C  CD1   . ILE B 1 648 ? 119.266 143.502 165.719 1.00 8.73  ?  648 ILE B CD1   1 
ATOM   10773 N  N     . ASP B 1 649 ? 116.503 146.269 162.572 1.00 12.87 ?  649 ASP B N     1 
ATOM   10774 C  CA    . ASP B 1 649 ? 115.820 146.941 161.469 1.00 7.33  ?  649 ASP B CA    1 
ATOM   10775 C  C     . ASP B 1 649 ? 116.102 146.264 160.133 1.00 10.36 ?  649 ASP B C     1 
ATOM   10776 O  O     . ASP B 1 649 ? 115.214 146.180 159.279 1.00 29.65 ?  649 ASP B O     1 
ATOM   10777 C  CB    . ASP B 1 649 ? 116.218 148.416 161.422 1.00 16.59 ?  649 ASP B CB    1 
ATOM   10778 C  CG    . ASP B 1 649 ? 117.698 148.628 161.639 1.00 16.75 ?  649 ASP B CG    1 
ATOM   10779 O  OD1   . ASP B 1 649 ? 118.242 148.047 162.598 1.00 20.57 ?  649 ASP B OD1   1 
ATOM   10780 O  OD2   . ASP B 1 649 ? 118.315 149.379 160.860 1.00 15.48 -1 649 ASP B OD2   1 
ATOM   10781 N  N     . GLN B 1 650 ? 117.324 145.788 159.931 1.00 12.34 ?  650 GLN B N     1 
ATOM   10782 C  CA    . GLN B 1 650 ? 117.649 144.978 158.766 1.00 3.46  ?  650 GLN B CA    1 
ATOM   10783 C  C     . GLN B 1 650 ? 117.437 143.508 159.127 1.00 7.97  ?  650 GLN B C     1 
ATOM   10784 O  O     . GLN B 1 650 ? 116.814 143.195 160.144 1.00 18.13 ?  650 GLN B O     1 
ATOM   10785 C  CB    . GLN B 1 650 ? 119.071 145.283 158.291 1.00 7.16  ?  650 GLN B CB    1 
ATOM   10786 C  CG    . GLN B 1 650 ? 119.299 146.732 157.922 1.00 8.51  ?  650 GLN B CG    1 
ATOM   10787 C  CD    . GLN B 1 650 ? 120.705 146.982 157.425 1.00 13.48 ?  650 GLN B CD    1 
ATOM   10788 O  OE1   . GLN B 1 650 ? 121.056 146.604 156.310 1.00 18.42 ?  650 GLN B OE1   1 
ATOM   10789 N  NE2   . GLN B 1 650 ? 121.517 147.627 158.252 1.00 6.77  ?  650 GLN B NE2   1 
ATOM   10790 N  N     . GLY B 1 651 ? 117.930 142.591 158.300 1.00 7.27  ?  651 GLY B N     1 
ATOM   10791 C  CA    . GLY B 1 651 ? 117.715 141.179 158.522 1.00 8.37  ?  651 GLY B CA    1 
ATOM   10792 C  C     . GLY B 1 651 ? 118.829 140.518 159.311 1.00 7.98  ?  651 GLY B C     1 
ATOM   10793 O  O     . GLY B 1 651 ? 119.790 141.143 159.756 1.00 12.97 ?  651 GLY B O     1 
ATOM   10794 N  N     . ILE B 1 652 ? 118.673 139.209 159.486 1.00 12.55 ?  652 ILE B N     1 
ATOM   10795 C  CA    . ILE B 1 652 ? 119.636 138.362 160.175 1.00 11.63 ?  652 ILE B CA    1 
ATOM   10796 C  C     . ILE B 1 652 ? 119.953 137.190 159.261 1.00 14.25 ?  652 ILE B C     1 
ATOM   10797 O  O     . ILE B 1 652 ? 119.040 136.567 158.710 1.00 25.45 ?  652 ILE B O     1 
ATOM   10798 C  CB    . ILE B 1 652 ? 119.094 137.857 161.525 1.00 6.36  ?  652 ILE B CB    1 
ATOM   10799 C  CG1   . ILE B 1 652 ? 118.634 139.025 162.396 1.00 6.35  ?  652 ILE B CG1   1 
ATOM   10800 C  CG2   . ILE B 1 652 ? 120.137 137.021 162.244 1.00 10.09 ?  652 ILE B CG2   1 
ATOM   10801 C  CD1   . ILE B 1 652 ? 117.831 138.595 163.598 1.00 9.76  ?  652 ILE B CD1   1 
ATOM   10802 N  N     . SER B 1 653 ? 121.237 136.888 159.100 1.00 5.70  ?  653 SER B N     1 
ATOM   10803 C  CA    . SER B 1 653 ? 121.641 135.750 158.281 1.00 12.44 ?  653 SER B CA    1 
ATOM   10804 C  C     . SER B 1 653 ? 121.269 134.476 159.025 1.00 19.34 ?  653 SER B C     1 
ATOM   10805 O  O     . SER B 1 653 ? 122.014 133.996 159.881 1.00 23.48 ?  653 SER B O     1 
ATOM   10806 C  CB    . SER B 1 653 ? 123.133 135.804 157.981 1.00 12.43 ?  653 SER B CB    1 
ATOM   10807 O  OG    . SER B 1 653 ? 123.390 136.622 156.854 1.00 21.12 ?  653 SER B OG    1 
ATOM   10808 N  N     . PHE B 1 654 ? 120.104 133.928 158.698 1.00 19.33 ?  654 PHE B N     1 
ATOM   10809 C  CA    . PHE B 1 654 ? 119.529 132.792 159.409 1.00 12.91 ?  654 PHE B CA    1 
ATOM   10810 C  C     . PHE B 1 654 ? 119.798 131.531 158.595 1.00 16.26 ?  654 PHE B C     1 
ATOM   10811 O  O     . PHE B 1 654 ? 119.142 131.277 157.583 1.00 25.36 ?  654 PHE B O     1 
ATOM   10812 C  CB    . PHE B 1 654 ? 118.038 133.013 159.637 1.00 13.27 ?  654 PHE B CB    1 
ATOM   10813 C  CG    . PHE B 1 654 ? 117.374 131.931 160.436 1.00 16.91 ?  654 PHE B CG    1 
ATOM   10814 C  CD1   . PHE B 1 654 ? 118.110 131.087 161.249 1.00 18.96 ?  654 PHE B CD1   1 
ATOM   10815 C  CD2   . PHE B 1 654 ? 116.004 131.762 160.373 1.00 17.86 ?  654 PHE B CD2   1 
ATOM   10816 C  CE1   . PHE B 1 654 ? 117.494 130.095 161.977 1.00 19.71 ?  654 PHE B CE1   1 
ATOM   10817 C  CE2   . PHE B 1 654 ? 115.383 130.773 161.101 1.00 17.55 ?  654 PHE B CE2   1 
ATOM   10818 C  CZ    . PHE B 1 654 ? 116.128 129.939 161.905 1.00 16.60 ?  654 PHE B CZ    1 
ATOM   10819 N  N     . THR B 1 655 ? 120.762 130.738 159.050 1.00 21.60 ?  655 THR B N     1 
ATOM   10820 C  CA    . THR B 1 655 ? 121.069 129.458 158.435 1.00 22.15 ?  655 THR B CA    1 
ATOM   10821 C  C     . THR B 1 655 ? 120.236 128.366 159.093 1.00 22.47 ?  655 THR B C     1 
ATOM   10822 O  O     . THR B 1 655 ? 120.190 128.269 160.323 1.00 27.99 ?  655 THR B O     1 
ATOM   10823 C  CB    . THR B 1 655 ? 122.559 129.139 158.566 1.00 24.56 ?  655 THR B CB    1 
ATOM   10824 O  OG1   . THR B 1 655 ? 123.321 130.082 157.802 1.00 31.42 ?  655 THR B OG1   1 
ATOM   10825 C  CG2   . THR B 1 655 ? 122.857 127.734 158.068 1.00 24.12 ?  655 THR B CG2   1 
ATOM   10826 N  N     . LEU B 1 656 ? 119.568 127.560 158.275 1.00 28.74 ?  656 LEU B N     1 
ATOM   10827 C  CA    . LEU B 1 656 ? 118.829 126.406 158.766 1.00 31.33 ?  656 LEU B CA    1 
ATOM   10828 C  C     . LEU B 1 656 ? 119.774 125.219 158.869 1.00 24.98 ?  656 LEU B C     1 
ATOM   10829 O  O     . LEU B 1 656 ? 120.573 124.975 157.960 1.00 30.77 ?  656 LEU B O     1 
ATOM   10830 C  CB    . LEU B 1 656 ? 117.654 126.077 157.846 1.00 28.54 ?  656 LEU B CB    1 
ATOM   10831 C  CG    . LEU B 1 656 ? 116.544 127.127 157.797 1.00 29.96 ?  656 LEU B CG    1 
ATOM   10832 C  CD1   . LEU B 1 656 ? 115.389 126.647 156.938 1.00 27.74 ?  656 LEU B CD1   1 
ATOM   10833 C  CD2   . LEU B 1 656 ? 116.068 127.477 159.199 1.00 26.15 ?  656 LEU B CD2   1 
ATOM   10834 N  N     . PHE B 1 657 ? 119.700 124.503 159.984 1.00 25.49 ?  657 PHE B N     1 
ATOM   10835 C  CA    . PHE B 1 657 ? 120.564 123.358 160.251 1.00 29.93 ?  657 PHE B CA    1 
ATOM   10836 C  C     . PHE B 1 657 ? 119.689 122.115 160.279 1.00 34.81 ?  657 PHE B C     1 
ATOM   10837 O  O     . PHE B 1 657 ? 118.910 121.918 161.218 1.00 38.68 ?  657 PHE B O     1 
ATOM   10838 C  CB    . PHE B 1 657 ? 121.321 123.550 161.562 1.00 28.95 ?  657 PHE B CB    1 
ATOM   10839 C  CG    . PHE B 1 657 ? 122.127 124.814 161.608 1.00 33.74 ?  657 PHE B CG    1 
ATOM   10840 C  CD1   . PHE B 1 657 ? 123.399 124.860 161.064 1.00 32.30 ?  657 PHE B CD1   1 
ATOM   10841 C  CD2   . PHE B 1 657 ? 121.609 125.962 162.185 1.00 33.75 ?  657 PHE B CD2   1 
ATOM   10842 C  CE1   . PHE B 1 657 ? 124.139 126.026 161.100 1.00 32.19 ?  657 PHE B CE1   1 
ATOM   10843 C  CE2   . PHE B 1 657 ? 122.346 127.127 162.228 1.00 31.68 ?  657 PHE B CE2   1 
ATOM   10844 C  CZ    . PHE B 1 657 ? 123.613 127.159 161.684 1.00 31.73 ?  657 PHE B CZ    1 
ATOM   10845 N  N     . LEU B 1 658 ? 119.817 121.279 159.255 1.00 35.52 ?  658 LEU B N     1 
ATOM   10846 C  CA    . LEU B 1 658 ? 118.894 120.185 159.017 1.00 38.84 ?  658 LEU B CA    1 
ATOM   10847 C  C     . LEU B 1 658 ? 119.611 118.849 159.159 1.00 42.86 ?  658 LEU B C     1 
ATOM   10848 O  O     . LEU B 1 658 ? 120.823 118.750 158.952 1.00 42.45 ?  658 LEU B O     1 
ATOM   10849 C  CB    . LEU B 1 658 ? 118.284 120.292 157.618 1.00 38.92 ?  658 LEU B CB    1 
ATOM   10850 C  CG    . LEU B 1 658 ? 117.706 121.658 157.241 1.00 36.73 ?  658 LEU B CG    1 
ATOM   10851 C  CD1   . LEU B 1 658 ? 117.782 121.848 155.737 1.00 36.74 ?  658 LEU B CD1   1 
ATOM   10852 C  CD2   . LEU B 1 658 ? 116.289 121.857 157.744 1.00 34.53 ?  658 LEU B CD2   1 
ATOM   10853 N  N     . LYS B 1 659 ? 118.850 117.827 159.534 1.00 46.82 ?  659 LYS B N     1 
ATOM   10854 C  CA    . LYS B 1 659 ? 119.346 116.461 159.544 1.00 45.01 ?  659 LYS B CA    1 
ATOM   10855 C  C     . LYS B 1 659 ? 119.035 115.784 158.216 1.00 47.48 ?  659 LYS B C     1 
ATOM   10856 O  O     . LYS B 1 659 ? 118.098 116.161 157.508 1.00 49.57 ?  659 LYS B O     1 
ATOM   10857 C  CB    . LYS B 1 659 ? 118.733 115.664 160.694 1.00 45.65 ?  659 LYS B CB    1 
ATOM   10858 C  CG    . LYS B 1 659 ? 119.110 116.169 162.075 1.00 46.86 ?  659 LYS B CG    1 
ATOM   10859 C  CD    . LYS B 1 659 ? 118.615 115.223 163.158 1.00 49.12 ?  659 LYS B CD    1 
ATOM   10860 C  CE    . LYS B 1 659 ? 119.038 115.693 164.539 1.00 46.79 ?  659 LYS B CE    1 
ATOM   10861 N  NZ    . LYS B 1 659 ? 118.856 114.634 165.570 1.00 49.98 1  659 LYS B NZ    1 
ATOM   10862 N  N     . ASP B 1 660 ? 119.843 114.777 157.879 1.00 53.65 ?  660 ASP B N     1 
ATOM   10863 C  CA    . ASP B 1 660 ? 119.633 114.037 156.640 1.00 52.62 ?  660 ASP B CA    1 
ATOM   10864 C  C     . ASP B 1 660 ? 118.333 113.244 156.652 1.00 51.96 ?  660 ASP B C     1 
ATOM   10865 O  O     . ASP B 1 660 ? 117.771 112.981 155.583 1.00 51.23 ?  660 ASP B O     1 
ATOM   10866 C  CB    . ASP B 1 660 ? 120.813 113.096 156.387 1.00 53.34 ?  660 ASP B CB    1 
ATOM   10867 C  CG    . ASP B 1 660 ? 121.760 113.620 155.326 1.00 55.56 ?  660 ASP B CG    1 
ATOM   10868 O  OD1   . ASP B 1 660 ? 121.306 114.380 154.446 1.00 54.48 ?  660 ASP B OD1   1 
ATOM   10869 O  OD2   . ASP B 1 660 ? 122.959 113.273 155.372 1.00 53.90 -1 660 ASP B OD2   1 
ATOM   10870 N  N     . THR B 1 661 ? 117.844 112.860 157.833 1.00 52.85 ?  661 THR B N     1 
ATOM   10871 C  CA    . THR B 1 661 ? 116.647 112.028 157.908 1.00 52.27 ?  661 THR B CA    1 
ATOM   10872 C  C     . THR B 1 661 ? 115.400 112.797 157.489 1.00 52.80 ?  661 THR B C     1 
ATOM   10873 O  O     . THR B 1 661 ? 114.491 112.228 156.874 1.00 55.96 ?  661 THR B O     1 
ATOM   10874 C  CB    . THR B 1 661 ? 116.479 111.478 159.324 1.00 53.12 ?  661 THR B CB    1 
ATOM   10875 O  OG1   . THR B 1 661 ? 116.499 112.559 160.265 1.00 54.39 ?  661 THR B OG1   1 
ATOM   10876 C  CG2   . THR B 1 661 ? 117.601 110.505 159.654 1.00 52.13 ?  661 THR B CG2   1 
ATOM   10877 N  N     . MET B 1 662 ? 115.335 114.085 157.813 1.00 51.33 ?  662 MET B N     1 
ATOM   10878 C  CA    . MET B 1 662 ? 114.133 114.862 157.546 1.00 52.61 ?  662 MET B CA    1 
ATOM   10879 C  C     . MET B 1 662 ? 113.961 115.110 156.051 1.00 51.05 ?  662 MET B C     1 
ATOM   10880 O  O     . MET B 1 662 ? 114.923 115.113 155.279 1.00 52.14 ?  662 MET B O     1 
ATOM   10881 C  CB    . MET B 1 662 ? 114.177 116.184 158.311 1.00 51.42 ?  662 MET B CB    1 
ATOM   10882 C  CG    . MET B 1 662 ? 114.956 117.289 157.632 1.00 49.54 ?  662 MET B CG    1 
ATOM   10883 S  SD    . MET B 1 662 ? 114.947 118.791 158.623 1.00 59.95 ?  662 MET B SD    1 
ATOM   10884 C  CE    . MET B 1 662 ? 114.946 118.112 160.281 1.00 49.08 ?  662 MET B CE    1 
ATOM   10885 N  N     . THR B 1 663 ? 112.710 115.314 155.648 1.00 43.99 ?  663 THR B N     1 
ATOM   10886 C  CA    . THR B 1 663 ? 112.330 115.405 154.249 1.00 44.61 ?  663 THR B CA    1 
ATOM   10887 C  C     . THR B 1 663 ? 112.211 116.867 153.821 1.00 44.35 ?  663 THR B C     1 
ATOM   10888 O  O     . THR B 1 663 ? 112.388 117.793 154.613 1.00 47.40 ?  663 THR B O     1 
ATOM   10889 C  CB    . THR B 1 663 ? 111.013 114.663 154.011 1.00 44.65 ?  663 THR B CB    1 
ATOM   10890 O  OG1   . THR B 1 663 ? 109.974 115.276 154.782 1.00 46.81 ?  663 THR B OG1   1 
ATOM   10891 C  CG2   . THR B 1 663 ? 111.144 113.209 154.428 1.00 45.09 ?  663 THR B CG2   1 
ATOM   10892 N  N     . THR B 1 664 ? 111.909 117.069 152.534 1.00 36.56 ?  664 THR B N     1 
ATOM   10893 C  CA    . THR B 1 664 ? 111.668 118.420 152.039 1.00 37.93 ?  664 THR B CA    1 
ATOM   10894 C  C     . THR B 1 664 ? 110.410 119.020 152.651 1.00 36.91 ?  664 THR B C     1 
ATOM   10895 O  O     . THR B 1 664 ? 110.275 120.246 152.717 1.00 39.76 ?  664 THR B O     1 
ATOM   10896 C  CB    . THR B 1 664 ? 111.559 118.421 150.513 1.00 37.84 ?  664 THR B CB    1 
ATOM   10897 O  OG1   . THR B 1 664 ? 110.380 117.710 150.116 1.00 38.33 ?  664 THR B OG1   1 
ATOM   10898 C  CG2   . THR B 1 664 ? 112.780 117.762 149.890 1.00 37.08 ?  664 THR B CG2   1 
ATOM   10899 N  N     . ARG B 1 665 ? 109.477 118.175 153.095 1.00 39.50 ?  665 ARG B N     1 
ATOM   10900 C  CA    . ARG B 1 665 ? 108.290 118.671 153.781 1.00 37.27 ?  665 ARG B CA    1 
ATOM   10901 C  C     . ARG B 1 665 ? 108.654 119.321 155.109 1.00 40.60 ?  665 ARG B C     1 
ATOM   10902 O  O     . ARG B 1 665 ? 108.068 120.338 155.488 1.00 42.67 ?  665 ARG B O     1 
ATOM   10903 C  CB    . ARG B 1 665 ? 107.297 117.528 153.984 1.00 39.03 ?  665 ARG B CB    1 
ATOM   10904 C  CG    . ARG B 1 665 ? 105.961 117.924 154.592 1.00 36.25 ?  665 ARG B CG    1 
ATOM   10905 C  CD    . ARG B 1 665 ? 105.787 117.291 155.962 1.00 39.06 ?  665 ARG B CD    1 
ATOM   10906 N  NE    . ARG B 1 665 ? 104.390 116.988 156.249 1.00 42.59 ?  665 ARG B NE    1 
ATOM   10907 C  CZ    . ARG B 1 665 ? 103.762 117.318 157.369 1.00 42.49 ?  665 ARG B CZ    1 
ATOM   10908 N  NH1   . ARG B 1 665 ? 104.382 117.960 158.344 1.00 43.20 1  665 ARG B NH1   1 
ATOM   10909 N  NH2   . ARG B 1 665 ? 102.481 116.993 157.515 1.00 41.16 ?  665 ARG B NH2   1 
ATOM   10910 N  N     . ASP B 1 666 ? 109.626 118.753 155.827 1.00 40.52 ?  666 ASP B N     1 
ATOM   10911 C  CA    . ASP B 1 666 ? 110.096 119.378 157.059 1.00 36.31 ?  666 ASP B CA    1 
ATOM   10912 C  C     . ASP B 1 666 ? 110.754 120.724 156.778 1.00 40.69 ?  666 ASP B C     1 
ATOM   10913 O  O     . ASP B 1 666 ? 110.555 121.687 157.528 1.00 43.81 ?  666 ASP B O     1 
ATOM   10914 C  CB    . ASP B 1 666 ? 111.065 118.444 157.782 1.00 39.39 ?  666 ASP B CB    1 
ATOM   10915 C  CG    . ASP B 1 666 ? 110.396 117.176 158.270 1.00 46.56 ?  666 ASP B CG    1 
ATOM   10916 O  OD1   . ASP B 1 666 ? 109.334 117.275 158.920 1.00 46.49 ?  666 ASP B OD1   1 
ATOM   10917 O  OD2   . ASP B 1 666 ? 110.928 116.079 158.003 1.00 46.36 -1 666 ASP B OD2   1 
ATOM   10918 N  N     . LEU B 1 667 ? 111.542 120.808 155.705 1.00 34.44 ?  667 LEU B N     1 
ATOM   10919 C  CA    . LEU B 1 667 ? 112.152 122.079 155.328 1.00 29.98 ?  667 LEU B CA    1 
ATOM   10920 C  C     . LEU B 1 667 ? 111.092 123.113 154.969 1.00 28.63 ?  667 LEU B C     1 
ATOM   10921 O  O     . LEU B 1 667 ? 111.198 124.284 155.355 1.00 35.33 ?  667 LEU B O     1 
ATOM   10922 C  CB    . LEU B 1 667 ? 113.115 121.863 154.160 1.00 33.52 ?  667 LEU B CB    1 
ATOM   10923 C  CG    . LEU B 1 667 ? 114.025 123.026 153.768 1.00 32.74 ?  667 LEU B CG    1 
ATOM   10924 C  CD1   . LEU B 1 667 ? 114.599 123.694 155.002 1.00 34.04 ?  667 LEU B CD1   1 
ATOM   10925 C  CD2   . LEU B 1 667 ? 115.137 122.537 152.858 1.00 31.27 ?  667 LEU B CD2   1 
ATOM   10926 N  N     . ASN B 1 668 ? 110.059 122.697 154.234 1.00 29.56 ?  668 ASN B N     1 
ATOM   10927 C  CA    . ASN B 1 668 ? 108.971 123.609 153.900 1.00 24.89 ?  668 ASN B CA    1 
ATOM   10928 C  C     . ASN B 1 668 ? 108.222 124.056 155.148 1.00 26.58 ?  668 ASN B C     1 
ATOM   10929 O  O     . ASN B 1 668 ? 107.828 125.221 155.255 1.00 28.91 ?  668 ASN B O     1 
ATOM   10930 C  CB    . ASN B 1 668 ? 108.015 122.950 152.907 1.00 28.31 ?  668 ASN B CB    1 
ATOM   10931 C  CG    . ASN B 1 668 ? 108.408 123.199 151.467 1.00 32.47 ?  668 ASN B CG    1 
ATOM   10932 O  OD1   . ASN B 1 668 ? 109.020 124.217 151.146 1.00 33.33 ?  668 ASN B OD1   1 
ATOM   10933 N  ND2   . ASN B 1 668 ? 108.059 122.267 150.590 1.00 33.17 ?  668 ASN B ND2   1 
ATOM   10934 N  N     . ARG B 1 669 ? 108.011 123.144 156.099 1.00 30.84 ?  669 ARG B N     1 
ATOM   10935 C  CA    . ARG B 1 669 ? 107.359 123.514 157.351 1.00 33.19 ?  669 ARG B CA    1 
ATOM   10936 C  C     . ARG B 1 669 ? 108.192 124.521 158.128 1.00 27.48 ?  669 ARG B C     1 
ATOM   10937 O  O     . ARG B 1 669 ? 107.651 125.469 158.706 1.00 28.14 ?  669 ARG B O     1 
ATOM   10938 C  CB    . ARG B 1 669 ? 107.101 122.272 158.201 1.00 31.40 ?  669 ARG B CB    1 
ATOM   10939 C  CG    . ARG B 1 669 ? 105.642 121.884 158.306 1.00 30.10 ?  669 ARG B CG    1 
ATOM   10940 C  CD    . ARG B 1 669 ? 105.431 120.838 159.390 1.00 32.17 ?  669 ARG B CD    1 
ATOM   10941 N  NE    . ARG B 1 669 ? 105.352 121.423 160.724 1.00 31.03 ?  669 ARG B NE    1 
ATOM   10942 C  CZ    . ARG B 1 669 ? 104.324 122.128 161.179 1.00 34.14 ?  669 ARG B CZ    1 
ATOM   10943 N  NH1   . ARG B 1 669 ? 103.257 122.358 160.431 1.00 33.10 1  669 ARG B NH1   1 
ATOM   10944 N  NH2   . ARG B 1 669 ? 104.366 122.610 162.417 1.00 34.56 ?  669 ARG B NH2   1 
ATOM   10945 N  N     . ILE B 1 670 ? 109.511 124.328 158.162 1.00 24.89 ?  670 ILE B N     1 
ATOM   10946 C  CA    . ILE B 1 670 ? 110.383 125.285 158.839 1.00 28.67 ?  670 ILE B CA    1 
ATOM   10947 C  C     . ILE B 1 670 ? 110.313 126.644 158.155 1.00 27.42 ?  670 ILE B C     1 
ATOM   10948 O  O     . ILE B 1 670 ? 110.238 127.686 158.817 1.00 27.35 ?  670 ILE B O     1 
ATOM   10949 C  CB    . ILE B 1 670 ? 111.826 124.752 158.901 1.00 28.82 ?  670 ILE B CB    1 
ATOM   10950 C  CG1   . ILE B 1 670 ? 111.899 123.512 159.796 1.00 28.87 ?  670 ILE B CG1   1 
ATOM   10951 C  CG2   . ILE B 1 670 ? 112.769 125.822 159.418 1.00 26.47 ?  670 ILE B CG2   1 
ATOM   10952 C  CD1   . ILE B 1 670 ? 113.091 122.628 159.513 1.00 28.03 ?  670 ILE B CD1   1 
ATOM   10953 N  N     . ASP B 1 671 ? 110.328 126.655 156.819 1.00 27.88 ?  671 ASP B N     1 
ATOM   10954 C  CA    . ASP B 1 671 ? 110.237 127.914 156.084 1.00 21.61 ?  671 ASP B CA    1 
ATOM   10955 C  C     . ASP B 1 671 ? 108.914 128.623 156.357 1.00 22.57 ?  671 ASP B C     1 
ATOM   10956 O  O     . ASP B 1 671 ? 108.881 129.844 156.555 1.00 26.72 ?  671 ASP B O     1 
ATOM   10957 C  CB    . ASP B 1 671 ? 110.400 127.656 154.585 1.00 22.56 ?  671 ASP B CB    1 
ATOM   10958 C  CG    . ASP B 1 671 ? 111.811 127.252 154.212 1.00 32.56 ?  671 ASP B CG    1 
ATOM   10959 O  OD1   . ASP B 1 671 ? 112.749 127.591 154.961 1.00 35.53 ?  671 ASP B OD1   1 
ATOM   10960 O  OD2   . ASP B 1 671 ? 111.982 126.590 153.166 1.00 33.40 -1 671 ASP B OD2   1 
ATOM   10961 N  N     . LEU B 1 672 ? 107.812 127.871 156.375 1.00 22.25 ?  672 LEU B N     1 
ATOM   10962 C  CA    . LEU B 1 672 ? 106.506 128.474 156.611 1.00 20.71 ?  672 LEU B CA    1 
ATOM   10963 C  C     . LEU B 1 672 ? 106.356 128.954 158.047 1.00 21.52 ?  672 LEU B C     1 
ATOM   10964 O  O     . LEU B 1 672 ? 105.687 129.962 158.292 1.00 26.69 ?  672 LEU B O     1 
ATOM   10965 C  CB    . LEU B 1 672 ? 105.400 127.482 156.259 1.00 24.45 ?  672 LEU B CB    1 
ATOM   10966 C  CG    . LEU B 1 672 ? 105.324 127.096 154.781 1.00 23.66 ?  672 LEU B CG    1 
ATOM   10967 C  CD1   . LEU B 1 672 ? 104.533 125.811 154.602 1.00 22.52 ?  672 LEU B CD1   1 
ATOM   10968 C  CD2   . LEU B 1 672 ? 104.733 128.228 153.957 1.00 20.82 ?  672 LEU B CD2   1 
ATOM   10969 N  N     . TYR B 1 673 ? 106.958 128.250 159.006 1.00 21.13 ?  673 TYR B N     1 
ATOM   10970 C  CA    . TYR B 1 673 ? 106.949 128.728 160.384 1.00 18.26 ?  673 TYR B CA    1 
ATOM   10971 C  C     . TYR B 1 673 ? 107.790 129.987 160.530 1.00 19.58 ?  673 TYR B C     1 
ATOM   10972 O  O     . TYR B 1 673 ? 107.434 130.894 161.290 1.00 27.13 ?  673 TYR B O     1 
ATOM   10973 C  CB    . TYR B 1 673 ? 107.451 127.634 161.325 1.00 18.99 ?  673 TYR B CB    1 
ATOM   10974 C  CG    . TYR B 1 673 ? 107.376 128.013 162.785 1.00 23.24 ?  673 TYR B CG    1 
ATOM   10975 C  CD1   . TYR B 1 673 ? 106.154 128.266 163.392 1.00 22.65 ?  673 TYR B CD1   1 
ATOM   10976 C  CD2   . TYR B 1 673 ? 108.524 128.120 163.555 1.00 16.57 ?  673 TYR B CD2   1 
ATOM   10977 C  CE1   . TYR B 1 673 ? 106.079 128.612 164.724 1.00 18.82 ?  673 TYR B CE1   1 
ATOM   10978 C  CE2   . TYR B 1 673 ? 108.459 128.466 164.888 1.00 19.29 ?  673 TYR B CE2   1 
ATOM   10979 C  CZ    . TYR B 1 673 ? 107.234 128.710 165.467 1.00 20.46 ?  673 TYR B CZ    1 
ATOM   10980 O  OH    . TYR B 1 673 ? 107.163 129.056 166.797 1.00 28.40 ?  673 TYR B OH    1 
ATOM   10981 N  N     . ALA B 1 674 ? 108.917 130.054 159.818 1.00 18.23 ?  674 ALA B N     1 
ATOM   10982 C  CA    . ALA B 1 674 ? 109.722 131.268 159.810 1.00 14.78 ?  674 ALA B CA    1 
ATOM   10983 C  C     . ALA B 1 674 ? 108.932 132.439 159.244 1.00 19.33 ?  674 ALA B C     1 
ATOM   10984 O  O     . ALA B 1 674 ? 108.945 133.542 159.801 1.00 23.74 ?  674 ALA B O     1 
ATOM   10985 C  CB    . ALA B 1 674 ? 111.002 131.037 159.007 1.00 13.81 ?  674 ALA B CB    1 
ATOM   10986 N  N     . HIS B 1 675 ? 108.223 132.209 158.138 1.00 18.20 ?  675 HIS B N     1 
ATOM   10987 C  CA    . HIS B 1 675 ? 107.379 133.256 157.571 1.00 19.37 ?  675 HIS B CA    1 
ATOM   10988 C  C     . HIS B 1 675 ? 106.278 133.660 158.545 1.00 18.72 ?  675 HIS B C     1 
ATOM   10989 O  O     . HIS B 1 675 ? 105.958 134.847 158.676 1.00 26.02 ?  675 HIS B O     1 
ATOM   10990 C  CB    . HIS B 1 675 ? 106.780 132.784 156.248 1.00 19.31 ?  675 HIS B CB    1 
ATOM   10991 C  CG    . HIS B 1 675 ? 105.714 133.688 155.715 1.00 17.26 ?  675 HIS B CG    1 
ATOM   10992 N  ND1   . HIS B 1 675 ? 104.370 133.454 155.914 1.00 24.61 ?  675 HIS B ND1   1 
ATOM   10993 C  CD2   . HIS B 1 675 ? 105.794 134.831 154.995 1.00 13.15 ?  675 HIS B CD2   1 
ATOM   10994 C  CE1   . HIS B 1 675 ? 103.669 134.412 155.336 1.00 22.93 ?  675 HIS B CE1   1 
ATOM   10995 N  NE2   . HIS B 1 675 ? 104.509 135.261 154.772 1.00 27.16 ?  675 HIS B NE2   1 
ATOM   10996 N  N     . HIS B 1 676 ? 105.683 132.683 159.231 1.00 18.21 ?  676 HIS B N     1 
ATOM   10997 C  CA    . HIS B 1 676 ? 104.630 132.971 160.198 1.00 18.52 ?  676 HIS B CA    1 
ATOM   10998 C  C     . HIS B 1 676 ? 105.161 133.770 161.381 1.00 23.94 ?  676 HIS B C     1 
ATOM   10999 O  O     . HIS B 1 676 ? 104.480 134.667 161.891 1.00 25.31 ?  676 HIS B O     1 
ATOM   11000 C  CB    . HIS B 1 676 ? 103.993 131.665 160.672 1.00 19.23 ?  676 HIS B CB    1 
ATOM   11001 C  CG    . HIS B 1 676 ? 103.150 131.811 161.899 1.00 20.47 ?  676 HIS B CG    1 
ATOM   11002 N  ND1   . HIS B 1 676 ? 101.932 132.457 161.895 1.00 25.04 ?  676 HIS B ND1   1 
ATOM   11003 C  CD2   . HIS B 1 676 ? 103.350 131.396 163.172 1.00 21.47 ?  676 HIS B CD2   1 
ATOM   11004 C  CE1   . HIS B 1 676 ? 101.418 132.431 163.111 1.00 26.61 ?  676 HIS B CE1   1 
ATOM   11005 N  NE2   . HIS B 1 676 ? 102.259 131.793 163.905 1.00 26.42 ?  676 HIS B NE2   1 
ATOM   11006 N  N     . ARG B 1 677 ? 106.375 133.461 161.831 1.00 22.89 ?  677 ARG B N     1 
ATOM   11007 C  CA    . ARG B 1 677 ? 106.949 134.104 163.005 1.00 19.61 ?  677 ARG B CA    1 
ATOM   11008 C  C     . ARG B 1 677 ? 107.577 135.457 162.701 1.00 21.29 ?  677 ARG B C     1 
ATOM   11009 O  O     . ARG B 1 677 ? 108.078 136.108 163.624 1.00 29.33 ?  677 ARG B O     1 
ATOM   11010 C  CB    . ARG B 1 677 ? 107.993 133.188 163.647 1.00 19.71 ?  677 ARG B CB    1 
ATOM   11011 C  CG    . ARG B 1 677 ? 107.400 131.997 164.370 1.00 23.45 ?  677 ARG B CG    1 
ATOM   11012 C  CD    . ARG B 1 677 ? 106.795 132.405 165.701 1.00 21.42 ?  677 ARG B CD    1 
ATOM   11013 N  NE    . ARG B 1 677 ? 107.809 132.849 166.649 1.00 28.85 ?  677 ARG B NE    1 
ATOM   11014 C  CZ    . ARG B 1 677 ? 107.948 134.100 167.068 1.00 35.20 ?  677 ARG B CZ    1 
ATOM   11015 N  NH1   . ARG B 1 677 ? 107.146 135.064 166.644 1.00 30.86 1  677 ARG B NH1   1 
ATOM   11016 N  NH2   . ARG B 1 677 ? 108.916 134.390 167.932 1.00 26.43 ?  677 ARG B NH2   1 
ATOM   11017 N  N     . GLY B 1 678 ? 107.564 135.894 161.447 1.00 20.57 ?  678 GLY B N     1 
ATOM   11018 C  CA    . GLY B 1 678 ? 108.122 137.178 161.090 1.00 13.88 ?  678 GLY B CA    1 
ATOM   11019 C  C     . GLY B 1 678 ? 109.564 137.157 160.644 1.00 12.96 ?  678 GLY B C     1 
ATOM   11020 O  O     . GLY B 1 678 ? 110.186 138.224 160.577 1.00 18.02 ?  678 GLY B O     1 
ATOM   11021 N  N     . ILE B 1 679 ? 110.121 135.982 160.346 1.00 15.56 ?  679 ILE B N     1 
ATOM   11022 C  CA    . ILE B 1 679 ? 111.494 135.913 159.868 1.00 15.82 ?  679 ILE B CA    1 
ATOM   11023 C  C     . ILE B 1 679 ? 111.589 136.619 158.526 1.00 13.14 ?  679 ILE B C     1 
ATOM   11024 O  O     . ILE B 1 679 ? 110.788 136.372 157.616 1.00 26.35 ?  679 ILE B O     1 
ATOM   11025 C  CB    . ILE B 1 679 ? 111.959 134.453 159.767 1.00 16.76 ?  679 ILE B CB    1 
ATOM   11026 C  CG1   . ILE B 1 679 ? 111.998 133.809 161.153 1.00 11.88 ?  679 ILE B CG1   1 
ATOM   11027 C  CG2   . ILE B 1 679 ? 113.317 134.368 159.091 1.00 14.34 ?  679 ILE B CG2   1 
ATOM   11028 C  CD1   . ILE B 1 679 ? 112.920 134.494 162.106 1.00 13.38 ?  679 ILE B CD1   1 
ATOM   11029 N  N     . LYS B 1 680 ? 112.567 137.513 158.401 1.00 9.64  ?  680 LYS B N     1 
ATOM   11030 C  CA    . LYS B 1 680 ? 112.695 138.295 157.179 1.00 9.10  ?  680 LYS B CA    1 
ATOM   11031 C  C     . LYS B 1 680 ? 113.395 137.503 156.081 1.00 6.32  ?  680 LYS B C     1 
ATOM   11032 O  O     . LYS B 1 680 ? 112.914 137.447 154.945 1.00 19.51 ?  680 LYS B O     1 
ATOM   11033 C  CB    . LYS B 1 680 ? 113.445 139.592 157.471 1.00 6.44  ?  680 LYS B CB    1 
ATOM   11034 C  CG    . LYS B 1 680 ? 112.657 140.588 158.297 1.00 0.00  ?  680 LYS B CG    1 
ATOM   11035 C  CD    . LYS B 1 680 ? 113.442 141.866 158.511 1.00 8.90  ?  680 LYS B CD    1 
ATOM   11036 C  CE    . LYS B 1 680 ? 112.820 142.717 159.596 1.00 9.68  ?  680 LYS B CE    1 
ATOM   11037 N  NZ    . LYS B 1 680 ? 113.577 143.975 159.820 1.00 17.63 1  680 LYS B NZ    1 
ATOM   11038 N  N     . THR B 1 681 ? 114.527 136.882 156.401 1.00 14.09 ?  681 THR B N     1 
ATOM   11039 C  CA    . THR B 1 681 ? 115.310 136.153 155.416 1.00 7.46  ?  681 THR B CA    1 
ATOM   11040 C  C     . THR B 1 681 ? 115.802 134.845 156.013 1.00 12.18 ?  681 THR B C     1 
ATOM   11041 O  O     . THR B 1 681 ? 115.990 134.726 157.226 1.00 19.65 ?  681 THR B O     1 
ATOM   11042 C  CB    . THR B 1 681 ? 116.515 136.970 154.922 1.00 12.38 ?  681 THR B CB    1 
ATOM   11043 O  OG1   . THR B 1 681 ? 117.237 137.492 156.046 1.00 23.17 ?  681 THR B OG1   1 
ATOM   11044 C  CG2   . THR B 1 681 ? 116.064 138.120 154.040 1.00 8.64  ?  681 THR B CG2   1 
ATOM   11045 N  N     . ILE B 1 682 ? 116.011 133.862 155.141 1.00 12.38 ?  682 ILE B N     1 
ATOM   11046 C  CA    . ILE B 1 682 ? 116.615 132.586 155.500 1.00 9.09  ?  682 ILE B CA    1 
ATOM   11047 C  C     . ILE B 1 682 ? 117.870 132.416 154.656 1.00 15.98 ?  682 ILE B C     1 
ATOM   11048 O  O     . ILE B 1 682 ? 117.813 132.521 153.426 1.00 19.54 ?  682 ILE B O     1 
ATOM   11049 C  CB    . ILE B 1 682 ? 115.643 131.413 155.286 1.00 11.04 ?  682 ILE B CB    1 
ATOM   11050 C  CG1   . ILE B 1 682 ? 114.292 131.720 155.931 1.00 17.16 ?  682 ILE B CG1   1 
ATOM   11051 C  CG2   . ILE B 1 682 ? 116.223 130.145 155.863 1.00 19.66 ?  682 ILE B CG2   1 
ATOM   11052 C  CD1   . ILE B 1 682 ? 113.261 130.640 155.736 1.00 18.91 ?  682 ILE B CD1   1 
ATOM   11053 N  N     . TYR B 1 683 ? 119.002 132.167 155.316 1.00 13.01 ?  683 TYR B N     1 
ATOM   11054 C  CA    . TYR B 1 683 ? 120.284 132.177 154.612 1.00 12.37 ?  683 TYR B CA    1 
ATOM   11055 C  C     . TYR B 1 683 ? 120.572 130.845 153.925 1.00 20.43 ?  683 TYR B C     1 
ATOM   11056 O  O     . TYR B 1 683 ? 120.612 130.764 152.695 1.00 33.65 ?  683 TYR B O     1 
ATOM   11057 C  CB    . TYR B 1 683 ? 121.406 132.534 155.592 1.00 19.94 ?  683 TYR B CB    1 
ATOM   11058 C  CG    . TYR B 1 683 ? 122.757 132.751 154.949 1.00 16.76 ?  683 TYR B CG    1 
ATOM   11059 C  CD1   . TYR B 1 683 ? 122.866 133.081 153.604 1.00 10.05 ?  683 TYR B CD1   1 
ATOM   11060 C  CD2   . TYR B 1 683 ? 123.923 132.638 155.691 1.00 14.57 ?  683 TYR B CD2   1 
ATOM   11061 C  CE1   . TYR B 1 683 ? 124.095 133.282 153.017 1.00 17.35 ?  683 TYR B CE1   1 
ATOM   11062 C  CE2   . TYR B 1 683 ? 125.159 132.839 155.111 1.00 20.79 ?  683 TYR B CE2   1 
ATOM   11063 C  CZ    . TYR B 1 683 ? 125.239 133.162 153.774 1.00 21.07 ?  683 TYR B CZ    1 
ATOM   11064 O  OH    . TYR B 1 683 ? 126.468 133.363 153.194 1.00 18.47 ?  683 TYR B OH    1 
ATOM   11065 N  N     . TYR B 1 684 ? 120.749 129.785 154.702 1.00 28.72 ?  684 TYR B N     1 
ATOM   11066 C  CA    . TYR B 1 684 ? 121.240 128.533 154.151 1.00 22.47 ?  684 TYR B CA    1 
ATOM   11067 C  C     . TYR B 1 684 ? 120.475 127.366 154.748 1.00 33.54 ?  684 TYR B C     1 
ATOM   11068 O  O     . TYR B 1 684 ? 119.952 127.446 155.862 1.00 33.94 ?  684 TYR B O     1 
ATOM   11069 C  CB    . TYR B 1 684 ? 122.740 128.347 154.416 1.00 23.90 ?  684 TYR B CB    1 
ATOM   11070 C  CG    . TYR B 1 684 ? 123.627 128.745 153.260 1.00 25.15 ?  684 TYR B CG    1 
ATOM   11071 C  CD1   . TYR B 1 684 ? 123.436 128.209 151.995 1.00 28.20 ?  684 TYR B CD1   1 
ATOM   11072 C  CD2   . TYR B 1 684 ? 124.661 129.654 153.438 1.00 27.14 ?  684 TYR B CD2   1 
ATOM   11073 C  CE1   . TYR B 1 684 ? 124.248 128.570 150.936 1.00 30.33 ?  684 TYR B CE1   1 
ATOM   11074 C  CE2   . TYR B 1 684 ? 125.477 130.022 152.388 1.00 27.12 ?  684 TYR B CE2   1 
ATOM   11075 C  CZ    . TYR B 1 684 ? 125.267 129.478 151.139 1.00 30.90 ?  684 TYR B CZ    1 
ATOM   11076 O  OH    . TYR B 1 684 ? 126.080 129.843 150.092 1.00 33.34 ?  684 TYR B OH    1 
ATOM   11077 N  N     . ALA B 1 685 ? 120.417 126.283 153.987 1.00 32.23 ?  685 ALA B N     1 
ATOM   11078 C  CA    . ALA B 1 685 ? 119.902 125.003 154.454 1.00 31.89 ?  685 ALA B CA    1 
ATOM   11079 C  C     . ALA B 1 685 ? 121.082 124.036 154.454 1.00 34.11 ?  685 ALA B C     1 
ATOM   11080 O  O     . ALA B 1 685 ? 121.312 123.312 153.484 1.00 41.93 ?  685 ALA B O     1 
ATOM   11081 C  CB    . ALA B 1 685 ? 118.761 124.515 153.573 1.00 30.04 ?  685 ALA B CB    1 
ATOM   11082 N  N     . ARG B 1 686 ? 121.838 124.038 155.549 1.00 31.14 ?  686 ARG B N     1 
ATOM   11083 C  CA    . ARG B 1 686 ? 122.986 123.154 155.692 1.00 35.59 ?  686 ARG B CA    1 
ATOM   11084 C  C     . ARG B 1 686 ? 122.526 121.835 156.295 1.00 40.36 ?  686 ARG B C     1 
ATOM   11085 O  O     . ARG B 1 686 ? 121.972 121.812 157.399 1.00 39.37 ?  686 ARG B O     1 
ATOM   11086 C  CB    . ARG B 1 686 ? 124.051 123.804 156.572 1.00 35.54 ?  686 ARG B CB    1 
ATOM   11087 C  CG    . ARG B 1 686 ? 124.701 125.031 155.964 1.00 39.12 ?  686 ARG B CG    1 
ATOM   11088 C  CD    . ARG B 1 686 ? 125.832 125.542 156.840 1.00 40.12 ?  686 ARG B CD    1 
ATOM   11089 N  NE    . ARG B 1 686 ? 126.471 124.467 157.589 1.00 42.56 ?  686 ARG B NE    1 
ATOM   11090 C  CZ    . ARG B 1 686 ? 127.696 124.016 157.353 1.00 41.73 ?  686 ARG B CZ    1 
ATOM   11091 N  NH1   . ARG B 1 686 ? 128.446 124.527 156.391 1.00 40.57 1  686 ARG B NH1   1 
ATOM   11092 N  NH2   . ARG B 1 686 ? 128.180 123.029 158.102 1.00 38.17 ?  686 ARG B NH2   1 
ATOM   11093 N  N     . THR B 1 687 ? 122.760 120.740 155.580 1.00 42.20 ?  687 THR B N     1 
ATOM   11094 C  CA    . THR B 1 687 ? 122.346 119.417 156.017 1.00 45.25 ?  687 THR B CA    1 
ATOM   11095 C  C     . THR B 1 687 ? 123.545 118.660 156.571 1.00 45.70 ?  687 THR B C     1 
ATOM   11096 O  O     . THR B 1 687 ? 124.621 118.654 155.967 1.00 45.26 ?  687 THR B O     1 
ATOM   11097 C  CB    . THR B 1 687 ? 121.713 118.629 154.867 1.00 43.73 ?  687 THR B CB    1 
ATOM   11098 O  OG1   . THR B 1 687 ? 120.808 119.475 154.148 1.00 43.79 ?  687 THR B OG1   1 
ATOM   11099 C  CG2   . THR B 1 687 ? 120.950 117.432 155.407 1.00 42.22 ?  687 THR B CG2   1 
ATOM   11100 N  N     . LYS B 1 688 ? 123.350 118.027 157.722 1.00 40.87 ?  688 LYS B N     1 
ATOM   11101 C  CA    . LYS B 1 688 ? 124.425 117.301 158.387 1.00 43.33 ?  688 LYS B CA    1 
ATOM   11102 C  C     . LYS B 1 688 ? 124.752 116.007 157.649 1.00 48.17 ?  688 LYS B C     1 
ATOM   11103 O  O     . LYS B 1 688 ? 123.971 115.057 157.664 1.00 48.97 ?  688 LYS B O     1 
ATOM   11104 C  CB    . LYS B 1 688 ? 124.048 117.002 159.839 1.00 42.70 ?  688 LYS B CB    1 
ATOM   11105 C  CG    . LYS B 1 688 ? 125.142 116.319 160.638 1.00 41.41 ?  688 LYS B CG    1 
ATOM   11106 C  CD    . LYS B 1 688 ? 124.760 116.200 162.102 1.00 44.48 ?  688 LYS B CD    1 
ATOM   11107 C  CE    . LYS B 1 688 ? 125.923 115.688 162.935 1.00 46.73 ?  688 LYS B CE    1 
ATOM   11108 N  NZ    . LYS B 1 688 ? 125.572 115.601 164.378 1.00 44.27 ?  688 LYS B NZ    1 
ATOM   11109 N  N     . ASP C 2 37  ? 142.334 85.715  110.556 1.00 45.99 ?  16  ASP C N     1 
ATOM   11110 C  CA    . ASP C 2 37  ? 142.376 86.444  109.285 1.00 45.47 ?  16  ASP C CA    1 
ATOM   11111 C  C     . ASP C 2 37  ? 141.452 87.661  109.221 1.00 44.13 ?  16  ASP C C     1 
ATOM   11112 O  O     . ASP C 2 37  ? 141.477 88.404  108.238 1.00 44.46 ?  16  ASP C O     1 
ATOM   11113 C  CB    . ASP C 2 37  ? 142.039 85.496  108.133 1.00 45.90 ?  16  ASP C CB    1 
ATOM   11114 C  CG    . ASP C 2 37  ? 142.841 84.218  108.183 1.00 47.25 ?  16  ASP C CG    1 
ATOM   11115 O  OD1   . ASP C 2 37  ? 144.042 84.279  108.525 1.00 47.99 ?  16  ASP C OD1   1 
ATOM   11116 O  OD2   . ASP C 2 37  ? 142.266 83.152  107.884 1.00 49.50 -1 16  ASP C OD2   1 
ATOM   11117 N  N     . PHE C 2 38  ? 140.645 87.869  110.258 1.00 42.17 ?  17  PHE C N     1 
ATOM   11118 C  CA    . PHE C 2 38  ? 139.572 88.866  110.182 1.00 40.67 ?  17  PHE C CA    1 
ATOM   11119 C  C     . PHE C 2 38  ? 139.416 89.828  111.365 1.00 39.46 ?  17  PHE C C     1 
ATOM   11120 O  O     . PHE C 2 38  ? 138.867 90.920  111.197 1.00 39.17 ?  17  PHE C O     1 
ATOM   11121 C  CB    . PHE C 2 38  ? 138.228 88.176  109.883 1.00 40.24 ?  17  PHE C CB    1 
ATOM   11122 C  CG    . PHE C 2 38  ? 137.869 87.077  110.856 1.00 39.58 ?  17  PHE C CG    1 
ATOM   11123 C  CD1   . PHE C 2 38  ? 137.194 87.369  112.042 1.00 38.78 ?  17  PHE C CD1   1 
ATOM   11124 C  CD2   . PHE C 2 38  ? 138.191 85.748  110.579 1.00 39.43 ?  17  PHE C CD2   1 
ATOM   11125 C  CE1   . PHE C 2 38  ? 136.849 86.359  112.939 1.00 38.07 ?  17  PHE C CE1   1 
ATOM   11126 C  CE2   . PHE C 2 38  ? 137.851 84.727  111.473 1.00 39.10 ?  17  PHE C CE2   1 
ATOM   11127 C  CZ    . PHE C 2 38  ? 137.179 85.036  112.657 1.00 38.63 ?  17  PHE C CZ    1 
ATOM   11128 N  N     . THR C 2 39  ? 139.882 89.432  112.552 1.00 38.22 ?  18  THR C N     1 
ATOM   11129 C  CA    . THR C 2 39  ? 139.642 90.229  113.767 1.00 37.09 ?  18  THR C CA    1 
ATOM   11130 C  C     . THR C 2 39  ? 140.153 91.675  113.649 1.00 36.84 ?  18  THR C C     1 
ATOM   11131 O  O     . THR C 2 39  ? 139.432 92.621  114.006 1.00 36.13 ?  18  THR C O     1 
ATOM   11132 C  CB    . THR C 2 39  ? 140.144 89.526  115.062 1.00 36.59 ?  18  THR C CB    1 
ATOM   11133 O  OG1   . THR C 2 39  ? 139.252 88.457  115.388 1.00 36.50 ?  18  THR C OG1   1 
ATOM   11134 C  CG2   . THR C 2 39  ? 140.158 90.485  116.236 1.00 36.06 ?  18  THR C CG2   1 
ATOM   11135 N  N     . GLN C 2 40  ? 141.374 91.841  113.131 1.00 37.01 ?  19  GLN C N     1 
ATOM   11136 C  CA    . GLN C 2 40  ? 141.972 93.176  112.986 1.00 37.33 ?  19  GLN C CA    1 
ATOM   11137 C  C     . GLN C 2 40  ? 141.136 94.116  112.132 1.00 36.63 ?  19  GLN C C     1 
ATOM   11138 O  O     . GLN C 2 40  ? 140.961 95.282  112.482 1.00 36.10 ?  19  GLN C O     1 
ATOM   11139 C  CB    . GLN C 2 40  ? 143.400 93.111  112.446 1.00 38.24 ?  19  GLN C CB    1 
ATOM   11140 C  CG    . GLN C 2 40  ? 144.422 92.832  113.525 1.00 41.33 ?  19  GLN C CG    1 
ATOM   11141 C  CD    . GLN C 2 40  ? 145.738 93.552  113.302 1.00 45.15 ?  19  GLN C CD    1 
ATOM   11142 O  OE1   . GLN C 2 40  ? 146.172 93.752  112.161 1.00 47.33 ?  19  GLN C OE1   1 
ATOM   11143 N  NE2   . GLN C 2 40  ? 146.385 93.946  114.397 1.00 46.51 ?  19  GLN C NE2   1 
ATOM   11144 N  N     . MET C 2 41  ? 140.611 93.602  111.023 1.00 36.23 ?  20  MET C N     1 
ATOM   11145 C  CA    . MET C 2 41  ? 139.763 94.414  110.161 1.00 36.40 ?  20  MET C CA    1 
ATOM   11146 C  C     . MET C 2 41  ? 138.402 94.720  110.814 1.00 34.93 ?  20  MET C C     1 
ATOM   11147 O  O     . MET C 2 41  ? 137.864 95.810  110.630 1.00 34.20 ?  20  MET C O     1 
ATOM   11148 C  CB    . MET C 2 41  ? 139.667 93.835  108.733 1.00 37.35 ?  20  MET C CB    1 
ATOM   11149 C  CG    . MET C 2 41  ? 138.598 92.793  108.463 1.00 40.49 ?  20  MET C CG    1 
ATOM   11150 S  SD    . MET C 2 41  ? 138.509 92.413  106.685 1.00 48.68 ?  20  MET C SD    1 
ATOM   11151 C  CE    . MET C 2 41  ? 139.760 91.130  106.531 1.00 47.17 ?  20  MET C CE    1 
ATOM   11152 N  N     . PHE C 2 42  ? 137.878 93.786  111.612 1.00 33.75 ?  21  PHE C N     1 
ATOM   11153 C  CA    . PHE C 2 42  ? 136.670 94.064  112.403 1.00 32.62 ?  21  PHE C CA    1 
ATOM   11154 C  C     . PHE C 2 42  ? 136.934 95.065  113.522 1.00 32.59 ?  21  PHE C C     1 
ATOM   11155 O  O     . PHE C 2 42  ? 136.102 95.936  113.792 1.00 32.23 ?  21  PHE C O     1 
ATOM   11156 C  CB    . PHE C 2 42  ? 136.040 92.782  112.945 1.00 32.12 ?  21  PHE C CB    1 
ATOM   11157 C  CG    . PHE C 2 42  ? 135.176 92.071  111.945 1.00 31.04 ?  21  PHE C CG    1 
ATOM   11158 C  CD1   . PHE C 2 42  ? 133.801 92.300  111.906 1.00 30.75 ?  21  PHE C CD1   1 
ATOM   11159 C  CD2   . PHE C 2 42  ? 135.733 91.180  111.035 1.00 30.99 ?  21  PHE C CD2   1 
ATOM   11160 C  CE1   . PHE C 2 42  ? 132.991 91.644  110.972 1.00 30.30 ?  21  PHE C CE1   1 
ATOM   11161 C  CE2   . PHE C 2 42  ? 134.933 90.516  110.091 1.00 30.74 ?  21  PHE C CE2   1 
ATOM   11162 C  CZ    . PHE C 2 42  ? 133.561 90.749  110.061 1.00 30.48 ?  21  PHE C CZ    1 
ATOM   11163 N  N     . TYR C 2 43  ? 138.096 94.944  114.163 1.00 32.33 ?  22  TYR C N     1 
ATOM   11164 C  CA    . TYR C 2 43  ? 138.513 95.917  115.169 1.00 32.50 ?  22  TYR C CA    1 
ATOM   11165 C  C     . TYR C 2 43  ? 138.517 97.325  114.578 1.00 33.01 ?  22  TYR C C     1 
ATOM   11166 O  O     . TYR C 2 43  ? 137.920 98.243  115.147 1.00 32.50 ?  22  TYR C O     1 
ATOM   11167 C  CB    . TYR C 2 43  ? 139.888 95.570  115.772 1.00 32.53 ?  22  TYR C CB    1 
ATOM   11168 C  CG    . TYR C 2 43  ? 140.439 96.695  116.631 1.00 33.27 ?  22  TYR C CG    1 
ATOM   11169 C  CD1   . TYR C 2 43  ? 140.016 96.865  117.952 1.00 32.34 ?  22  TYR C CD1   1 
ATOM   11170 C  CD2   . TYR C 2 43  ? 141.352 97.613  116.106 1.00 33.71 ?  22  TYR C CD2   1 
ATOM   11171 C  CE1   . TYR C 2 43  ? 140.504 97.910  118.736 1.00 33.58 ?  22  TYR C CE1   1 
ATOM   11172 C  CE2   . TYR C 2 43  ? 141.844 98.668  116.877 1.00 35.12 ?  22  TYR C CE2   1 
ATOM   11173 C  CZ    . TYR C 2 43  ? 141.418 98.807  118.192 1.00 35.30 ?  22  TYR C CZ    1 
ATOM   11174 O  OH    . TYR C 2 43  ? 141.906 99.848  118.953 1.00 36.54 ?  22  TYR C OH    1 
ATOM   11175 N  N     . ASN C 2 44  ? 139.179 97.480  113.428 1.00 33.80 ?  23  ASN C N     1 
ATOM   11176 C  CA    . ASN C 2 44  ? 139.282 98.773  112.764 1.00 34.80 ?  23  ASN C CA    1 
ATOM   11177 C  C     . ASN C 2 44  ? 137.918 99.306  112.329 1.00 34.40 ?  23  ASN C C     1 
ATOM   11178 O  O     . ASN C 2 44  ? 137.632 100.486 112.502 1.00 33.99 ?  23  ASN C O     1 
ATOM   11179 C  CB    . ASN C 2 44  ? 140.249 98.706  111.571 1.00 35.46 ?  23  ASN C CB    1 
ATOM   11180 C  CG    . ASN C 2 44  ? 141.691 98.375  111.984 1.00 38.28 ?  23  ASN C CG    1 
ATOM   11181 O  OD1   . ASN C 2 44  ? 142.108 98.603  113.129 1.00 41.01 ?  23  ASN C OD1   1 
ATOM   11182 N  ND2   . ASN C 2 44  ? 142.461 97.840  111.037 1.00 39.13 ?  23  ASN C ND2   1 
ATOM   11183 N  N     . GLN C 2 45  ? 137.077 98.427  111.782 1.00 34.49 ?  24  GLN C N     1 
ATOM   11184 C  CA    . GLN C 2 45  ? 135.737 98.813  111.353 1.00 34.81 ?  24  GLN C CA    1 
ATOM   11185 C  C     . GLN C 2 45  ? 134.864 99.240  112.539 1.00 34.68 ?  24  GLN C C     1 
ATOM   11186 O  O     . GLN C 2 45  ? 134.179 100.264 112.473 1.00 34.59 ?  24  GLN C O     1 
ATOM   11187 C  CB    . GLN C 2 45  ? 135.076 97.686  110.552 1.00 34.83 ?  24  GLN C CB    1 
ATOM   11188 C  CG    . GLN C 2 45  ? 133.848 98.114  109.744 1.00 36.14 ?  24  GLN C CG    1 
ATOM   11189 C  CD    . GLN C 2 45  ? 134.153 99.178  108.685 1.00 38.04 ?  24  GLN C CD    1 
ATOM   11190 O  OE1   . GLN C 2 45  ? 135.264 99.254  108.152 1.00 38.57 ?  24  GLN C OE1   1 
ATOM   11191 N  NE2   . GLN C 2 45  ? 133.156 100.009 108.382 1.00 38.67 ?  24  GLN C NE2   1 
ATOM   11192 N  N     . ASN C 2 46  ? 134.901 98.472  113.625 1.00 34.71 ?  25  ASN C N     1 
ATOM   11193 C  CA    . ASN C 2 46  ? 134.114 98.812  114.811 1.00 34.99 ?  25  ASN C CA    1 
ATOM   11194 C  C     . ASN C 2 46  ? 134.502 100.161 115.413 1.00 35.69 ?  25  ASN C C     1 
ATOM   11195 O  O     . ASN C 2 46  ? 133.637 101.000 115.686 1.00 35.41 ?  25  ASN C O     1 
ATOM   11196 C  CB    . ASN C 2 46  ? 134.171 97.695  115.862 1.00 34.64 ?  25  ASN C CB    1 
ATOM   11197 C  CG    . ASN C 2 46  ? 133.201 96.573  115.563 1.00 34.71 ?  25  ASN C CG    1 
ATOM   11198 O  OD1   . ASN C 2 46  ? 132.074 96.582  116.049 1.00 35.68 ?  25  ASN C OD1   1 
ATOM   11199 N  ND2   . ASN C 2 46  ? 133.620 95.616  114.729 1.00 34.71 ?  25  ASN C ND2   1 
ATOM   11200 N  N     . VAL C 2 47  ? 135.800 100.387 115.595 1.00 36.69 ?  26  VAL C N     1 
ATOM   11201 C  CA    . VAL C 2 47  ? 136.250 101.640 116.205 1.00 38.00 ?  26  VAL C CA    1 
ATOM   11202 C  C     . VAL C 2 47  ? 136.040 102.857 115.294 1.00 38.90 ?  26  VAL C C     1 
ATOM   11203 O  O     . VAL C 2 47  ? 135.806 103.957 115.785 1.00 39.46 ?  26  VAL C O     1 
ATOM   11204 C  CB    . VAL C 2 47  ? 137.703 101.574 116.746 1.00 38.16 ?  26  VAL C CB    1 
ATOM   11205 C  CG1   . VAL C 2 47  ? 137.828 100.463 117.771 1.00 37.75 ?  26  VAL C CG1   1 
ATOM   11206 C  CG2   . VAL C 2 47  ? 138.717 101.403 115.617 1.00 38.81 ?  26  VAL C CG2   1 
ATOM   11207 N  N     . LYS C 2 48  ? 136.089 102.654 113.977 1.00 39.67 ?  27  LYS C N     1 
ATOM   11208 C  CA    . LYS C 2 48  ? 135.850 103.751 113.036 1.00 40.50 ?  27  LYS C CA    1 
ATOM   11209 C  C     . LYS C 2 48  ? 134.356 104.070 112.900 1.00 40.02 ?  27  LYS C C     1 
ATOM   11210 O  O     . LYS C 2 48  ? 133.980 105.122 112.377 1.00 40.55 ?  27  LYS C O     1 
ATOM   11211 C  CB    . LYS C 2 48  ? 136.488 103.465 111.663 1.00 41.23 ?  27  LYS C CB    1 
ATOM   11212 C  CG    . LYS C 2 48  ? 135.641 102.608 110.723 1.00 42.50 ?  27  LYS C CG    1 
ATOM   11213 C  CD    . LYS C 2 48  ? 136.297 102.414 109.348 1.00 44.92 ?  27  LYS C CD    1 
ATOM   11214 C  CE    . LYS C 2 48  ? 136.093 103.621 108.434 1.00 46.66 ?  27  LYS C CE    1 
ATOM   11215 N  NZ    . LYS C 2 48  ? 134.649 103.889 108.171 1.00 47.26 1  27  LYS C NZ    1 
ATOM   11216 N  N     . GLN C 2 49  ? 133.508 103.158 113.360 1.00 39.10 ?  28  GLN C N     1 
ATOM   11217 C  CA    . GLN C 2 49  ? 132.078 103.381 113.328 1.00 38.22 ?  28  GLN C CA    1 
ATOM   11218 C  C     . GLN C 2 49  ? 131.575 104.027 114.618 1.00 37.23 ?  28  GLN C C     1 
ATOM   11219 O  O     . GLN C 2 49  ? 130.381 104.294 114.734 1.00 37.40 ?  28  GLN C O     1 
ATOM   11220 C  CB    . GLN C 2 49  ? 131.318 102.078 113.026 1.00 38.69 ?  28  GLN C CB    1 
ATOM   11221 C  CG    . GLN C 2 49  ? 131.422 101.619 111.563 1.00 39.57 ?  28  GLN C CG    1 
ATOM   11222 C  CD    . GLN C 2 49  ? 130.514 100.440 111.220 1.00 41.20 ?  28  GLN C CD    1 
ATOM   11223 O  OE1   . GLN C 2 49  ? 130.559 99.927  110.101 1.00 42.94 ?  28  GLN C OE1   1 
ATOM   11224 N  NE2   . GLN C 2 49  ? 129.688 100.008 112.177 1.00 41.23 ?  28  GLN C NE2   1 
ATOM   11225 N  N     . PHE C 2 50  ? 132.477 104.297 115.568 1.00 35.83 ?  29  PHE C N     1 
ATOM   11226 C  CA    . PHE C 2 50  ? 132.072 104.841 116.872 1.00 34.51 ?  29  PHE C CA    1 
ATOM   11227 C  C     . PHE C 2 50  ? 131.237 106.120 116.758 1.00 33.81 ?  29  PHE C C     1 
ATOM   11228 O  O     . PHE C 2 50  ? 131.583 107.026 116.000 1.00 33.66 ?  29  PHE C O     1 
ATOM   11229 C  CB    . PHE C 2 50  ? 133.265 105.073 117.804 1.00 34.59 ?  29  PHE C CB    1 
ATOM   11230 C  CG    . PHE C 2 50  ? 132.871 105.603 119.172 1.00 34.59 ?  29  PHE C CG    1 
ATOM   11231 C  CD1   . PHE C 2 50  ? 132.239 104.775 120.106 1.00 34.34 ?  29  PHE C CD1   1 
ATOM   11232 C  CD2   . PHE C 2 50  ? 133.112 106.933 119.515 1.00 35.49 ?  29  PHE C CD2   1 
ATOM   11233 C  CE1   . PHE C 2 50  ? 131.865 105.260 121.368 1.00 33.88 ?  29  PHE C CE1   1 
ATOM   11234 C  CE2   . PHE C 2 50  ? 132.740 107.435 120.776 1.00 34.12 ?  29  PHE C CE2   1 
ATOM   11235 C  CZ    . PHE C 2 50  ? 132.117 106.598 121.702 1.00 33.87 ?  29  PHE C CZ    1 
ATOM   11236 N  N     . TRP C 2 51  ? 130.145 106.174 117.524 1.00 32.24 ?  30  TRP C N     1 
ATOM   11237 C  CA    . TRP C 2 51  ? 129.229 107.312 117.517 1.00 31.28 ?  30  TRP C CA    1 
ATOM   11238 C  C     . TRP C 2 51  ? 128.495 107.457 118.851 1.00 31.12 ?  30  TRP C C     1 
ATOM   11239 O  O     . TRP C 2 51  ? 128.489 106.526 119.665 1.00 30.71 ?  30  TRP C O     1 
ATOM   11240 C  CB    . TRP C 2 51  ? 128.227 107.189 116.360 1.00 30.85 ?  30  TRP C CB    1 
ATOM   11241 C  CG    . TRP C 2 51  ? 127.332 105.978 116.445 1.00 29.31 ?  30  TRP C CG    1 
ATOM   11242 C  CD1   . TRP C 2 51  ? 127.631 104.703 116.049 1.00 29.07 ?  30  TRP C CD1   1 
ATOM   11243 C  CD2   . TRP C 2 51  ? 126.005 105.929 116.978 1.00 28.33 ?  30  TRP C CD2   1 
ATOM   11244 N  NE1   . TRP C 2 51  ? 126.569 103.867 116.293 1.00 28.01 ?  30  TRP C NE1   1 
ATOM   11245 C  CE2   . TRP C 2 51  ? 125.556 104.593 116.863 1.00 27.67 ?  30  TRP C CE2   1 
ATOM   11246 C  CE3   . TRP C 2 51  ? 125.150 106.883 117.547 1.00 27.27 ?  30  TRP C CE3   1 
ATOM   11247 C  CZ2   . TRP C 2 51  ? 124.294 104.188 117.293 1.00 26.54 ?  30  TRP C CZ2   1 
ATOM   11248 C  CZ3   . TRP C 2 51  ? 123.889 106.482 117.966 1.00 27.07 ?  30  TRP C CZ3   1 
ATOM   11249 C  CH2   . TRP C 2 51  ? 123.475 105.142 117.843 1.00 26.52 ?  30  TRP C CH2   1 
ATOM   11250 N  N     . LEU C 2 52  ? 127.885 108.627 119.065 1.00 30.65 ?  31  LEU C N     1 
ATOM   11251 C  CA    . LEU C 2 52  ? 127.023 108.893 120.219 1.00 30.38 ?  31  LEU C CA    1 
ATOM   11252 C  C     . LEU C 2 52  ? 125.720 109.532 119.747 1.00 30.51 ?  31  LEU C C     1 
ATOM   11253 O  O     . LEU C 2 52  ? 125.745 110.350 118.826 1.00 30.77 ?  31  LEU C O     1 
ATOM   11254 C  CB    . LEU C 2 52  ? 127.724 109.821 121.224 1.00 30.45 ?  31  LEU C CB    1 
ATOM   11255 C  CG    . LEU C 2 52  ? 128.976 109.251 121.897 1.00 30.29 ?  31  LEU C CG    1 
ATOM   11256 C  CD1   . LEU C 2 52  ? 129.864 110.350 122.498 1.00 30.69 ?  31  LEU C CD1   1 
ATOM   11257 C  CD2   . LEU C 2 52  ? 128.606 108.188 122.943 1.00 29.91 ?  31  LEU C CD2   1 
ATOM   11258 N  N     . PRO C 2 53  ? 124.577 109.174 120.375 1.00 30.73 ?  32  PRO C N     1 
ATOM   11259 C  CA    . PRO C 2 53  ? 123.280 109.722 119.945 1.00 31.17 ?  32  PRO C CA    1 
ATOM   11260 C  C     . PRO C 2 53  ? 123.220 111.248 119.977 1.00 32.18 ?  32  PRO C C     1 
ATOM   11261 O  O     . PRO C 2 53  ? 122.512 111.851 119.154 1.00 32.66 ?  32  PRO C O     1 
ATOM   11262 C  CB    . PRO C 2 53  ? 122.286 109.133 120.953 1.00 30.99 ?  32  PRO C CB    1 
ATOM   11263 C  CG    . PRO C 2 53  ? 123.128 108.633 122.103 1.00 30.50 ?  32  PRO C CG    1 
ATOM   11264 C  CD    . PRO C 2 53  ? 124.418 108.214 121.486 1.00 30.46 ?  32  PRO C CD    1 
ATOM   11265 N  N     . GLU C 2 54  ? 123.967 111.859 120.901 1.00 32.62 ?  33  GLU C N     1 
ATOM   11266 C  CA    . GLU C 2 54  ? 124.015 113.324 121.037 1.00 33.44 ?  33  GLU C CA    1 
ATOM   11267 C  C     . GLU C 2 54  ? 124.563 114.041 119.797 1.00 33.59 ?  33  GLU C C     1 
ATOM   11268 O  O     . GLU C 2 54  ? 124.385 115.248 119.658 1.00 34.05 ?  33  GLU C O     1 
ATOM   11269 C  CB    . GLU C 2 54  ? 124.818 113.747 122.280 1.00 33.72 ?  33  GLU C CB    1 
ATOM   11270 C  CG    . GLU C 2 54  ? 124.122 113.478 123.628 1.00 34.53 ?  33  GLU C CG    1 
ATOM   11271 C  CD    . GLU C 2 54  ? 124.134 112.001 124.027 1.00 35.09 ?  33  GLU C CD    1 
ATOM   11272 O  OE1   . GLU C 2 54  ? 125.009 111.244 123.535 1.00 34.38 ?  33  GLU C OE1   1 
ATOM   11273 O  OE2   . GLU C 2 54  ? 123.264 111.600 124.834 1.00 35.53 -1 33  GLU C OE2   1 
ATOM   11274 N  N     . GLU C 2 55  ? 125.224 113.298 118.906 1.00 33.82 ?  34  GLU C N     1 
ATOM   11275 C  CA    . GLU C 2 55  ? 125.706 113.846 117.635 1.00 34.19 ?  34  GLU C CA    1 
ATOM   11276 C  C     . GLU C 2 55  ? 124.543 114.222 116.704 1.00 33.83 ?  34  GLU C C     1 
ATOM   11277 O  O     . GLU C 2 55  ? 124.711 115.025 115.789 1.00 33.93 ?  34  GLU C O     1 
ATOM   11278 C  CB    . GLU C 2 55  ? 126.628 112.851 116.908 1.00 34.52 ?  34  GLU C CB    1 
ATOM   11279 C  CG    . GLU C 2 55  ? 127.919 112.481 117.633 1.00 36.50 ?  34  GLU C CG    1 
ATOM   11280 C  CD    . GLU C 2 55  ? 128.891 111.720 116.736 1.00 40.03 ?  34  GLU C CD    1 
ATOM   11281 O  OE1   . GLU C 2 55  ? 129.657 112.366 115.987 1.00 42.43 ?  34  GLU C OE1   1 
ATOM   11282 O  OE2   . GLU C 2 55  ? 128.898 110.475 116.781 1.00 39.35 -1 34  GLU C OE2   1 
ATOM   11283 N  N     . ILE C 2 56  ? 123.383 113.607 116.937 1.00 33.31 ?  35  ILE C N     1 
ATOM   11284 C  CA    . ILE C 2 56  ? 122.179 113.798 116.125 1.00 33.14 ?  35  ILE C CA    1 
ATOM   11285 C  C     . ILE C 2 56  ? 121.161 114.618 116.925 1.00 32.58 ?  35  ILE C C     1 
ATOM   11286 O  O     . ILE C 2 56  ? 120.704 114.177 117.974 1.00 32.12 ?  35  ILE C O     1 
ATOM   11287 C  CB    . ILE C 2 56  ? 121.532 112.422 115.742 1.00 33.03 ?  35  ILE C CB    1 
ATOM   11288 C  CG1   . ILE C 2 56  ? 122.560 111.454 115.116 1.00 34.76 ?  35  ILE C CG1   1 
ATOM   11289 C  CG2   . ILE C 2 56  ? 120.301 112.606 114.846 1.00 33.61 ?  35  ILE C CG2   1 
ATOM   11290 C  CD1   . ILE C 2 56  ? 123.098 111.852 113.739 1.00 36.75 ?  35  ILE C CD1   1 
ATOM   11291 N  N     . ALA C 2 57  ? 120.818 115.809 116.439 1.00 32.36 ?  36  ALA C N     1 
ATOM   11292 C  CA    . ALA C 2 57  ? 119.786 116.628 117.081 1.00 32.17 ?  36  ALA C CA    1 
ATOM   11293 C  C     . ALA C 2 57  ? 118.396 116.095 116.717 1.00 31.76 ?  36  ALA C C     1 
ATOM   11294 O  O     . ALA C 2 57  ? 118.109 115.842 115.546 1.00 31.95 ?  36  ALA C O     1 
ATOM   11295 C  CB    . ALA C 2 57  ? 119.929 118.084 116.666 1.00 33.01 ?  36  ALA C CB    1 
ATOM   11296 N  N     . LEU C 2 58  ? 117.535 115.928 117.717 1.00 30.68 ?  37  LEU C N     1 
ATOM   11297 C  CA    . LEU C 2 58  ? 116.283 115.201 117.517 1.00 30.14 ?  37  LEU C CA    1 
ATOM   11298 C  C     . LEU C 2 58  ? 115.035 116.073 117.435 1.00 30.21 ?  37  LEU C C     1 
ATOM   11299 O  O     . LEU C 2 58  ? 113.963 115.589 117.048 1.00 29.91 ?  37  LEU C O     1 
ATOM   11300 C  CB    . LEU C 2 58  ? 116.116 114.123 118.594 1.00 29.46 ?  37  LEU C CB    1 
ATOM   11301 C  CG    . LEU C 2 58  ? 117.116 112.960 118.530 1.00 29.08 ?  37  LEU C CG    1 
ATOM   11302 C  CD1   . LEU C 2 58  ? 116.972 112.056 119.741 1.00 29.23 ?  37  LEU C CD1   1 
ATOM   11303 C  CD2   . LEU C 2 58  ? 116.953 112.153 117.242 1.00 28.84 ?  37  LEU C CD2   1 
ATOM   11304 N  N     . ASN C 2 59  ? 115.178 117.350 117.775 1.00 30.50 ?  38  ASN C N     1 
ATOM   11305 C  CA    . ASN C 2 59  ? 114.042 118.275 117.787 1.00 31.23 ?  38  ASN C CA    1 
ATOM   11306 C  C     . ASN C 2 59  ? 113.375 118.467 116.414 1.00 31.03 ?  38  ASN C C     1 
ATOM   11307 O  O     . ASN C 2 59  ? 112.220 118.876 116.338 1.00 30.82 ?  38  ASN C O     1 
ATOM   11308 C  CB    . ASN C 2 59  ? 114.420 119.619 118.438 1.00 31.98 ?  38  ASN C CB    1 
ATOM   11309 C  CG    . ASN C 2 59  ? 115.580 120.314 117.743 1.00 33.59 ?  38  ASN C CG    1 
ATOM   11310 O  OD1   . ASN C 2 59  ? 116.663 119.738 117.581 1.00 36.48 ?  38  ASN C OD1   1 
ATOM   11311 N  ND2   . ASN C 2 59  ? 115.366 121.563 117.341 1.00 34.77 ?  38  ASN C ND2   1 
ATOM   11312 N  N     . GLY C 2 60  ? 114.098 118.133 115.348 1.00 30.88 ?  39  GLY C N     1 
ATOM   11313 C  CA    . GLY C 2 60  ? 113.551 118.134 113.986 1.00 31.37 ?  39  GLY C CA    1 
ATOM   11314 C  C     . GLY C 2 60  ? 112.447 117.118 113.719 1.00 31.05 ?  39  GLY C C     1 
ATOM   11315 O  O     . GLY C 2 60  ? 111.617 117.341 112.848 1.00 31.21 ?  39  GLY C O     1 
ATOM   11316 N  N     . ASP C 2 61  ? 112.428 116.011 114.466 1.00 30.63 ?  40  ASP C N     1 
ATOM   11317 C  CA    . ASP C 2 61  ? 111.337 115.021 114.380 1.00 30.65 ?  40  ASP C CA    1 
ATOM   11318 C  C     . ASP C 2 61  ? 110.045 115.418 115.102 1.00 31.00 ?  40  ASP C C     1 
ATOM   11319 O  O     . ASP C 2 61  ? 109.035 114.727 114.962 1.00 30.91 ?  40  ASP C O     1 
ATOM   11320 C  CB    . ASP C 2 61  ? 111.778 113.663 114.939 1.00 30.00 ?  40  ASP C CB    1 
ATOM   11321 C  CG    . ASP C 2 61  ? 112.846 112.996 114.105 1.00 30.88 ?  40  ASP C CG    1 
ATOM   11322 O  OD1   . ASP C 2 61  ? 113.287 113.575 113.083 1.00 30.42 ?  40  ASP C OD1   1 
ATOM   11323 O  OD2   . ASP C 2 61  ? 113.251 111.878 114.488 1.00 31.17 -1 40  ASP C OD2   1 
ATOM   11324 N  N     . LEU C 2 62  ? 110.079 116.499 115.880 1.00 31.54 ?  41  LEU C N     1 
ATOM   11325 C  CA    . LEU C 2 62  ? 108.948 116.868 116.748 1.00 32.47 ?  41  LEU C CA    1 
ATOM   11326 C  C     . LEU C 2 62  ? 107.614 116.988 116.019 1.00 33.21 ?  41  LEU C C     1 
ATOM   11327 O  O     . LEU C 2 62  ? 106.582 116.535 116.525 1.00 32.84 ?  41  LEU C O     1 
ATOM   11328 C  CB    . LEU C 2 62  ? 109.234 118.158 117.518 1.00 33.14 ?  41  LEU C CB    1 
ATOM   11329 C  CG    . LEU C 2 62  ? 110.020 118.042 118.824 1.00 34.44 ?  41  LEU C CG    1 
ATOM   11330 C  CD1   . LEU C 2 62  ? 110.472 119.421 119.283 1.00 35.04 ?  41  LEU C CD1   1 
ATOM   11331 C  CD2   . LEU C 2 62  ? 109.180 117.350 119.905 1.00 35.52 ?  41  LEU C CD2   1 
ATOM   11332 N  N     . LEU C 2 63  ? 107.641 117.594 114.834 1.00 33.75 ?  42  LEU C N     1 
ATOM   11333 C  CA    . LEU C 2 63  ? 106.420 117.790 114.064 1.00 34.79 ?  42  LEU C CA    1 
ATOM   11334 C  C     . LEU C 2 63  ? 105.894 116.543 113.358 1.00 34.66 ?  42  LEU C C     1 
ATOM   11335 O  O     . LEU C 2 63  ? 104.698 116.270 113.441 1.00 34.67 ?  42  LEU C O     1 
ATOM   11336 C  CB    . LEU C 2 63  ? 106.550 118.966 113.093 1.00 35.27 ?  42  LEU C CB    1 
ATOM   11337 C  CG    . LEU C 2 63  ? 106.301 120.332 113.744 1.00 36.82 ?  42  LEU C CG    1 
ATOM   11338 C  CD1   . LEU C 2 63  ? 106.495 121.436 112.711 1.00 37.93 ?  42  LEU C CD1   1 
ATOM   11339 C  CD2   . LEU C 2 63  ? 104.907 120.429 114.361 1.00 37.85 ?  42  LEU C CD2   1 
ATOM   11340 N  N     . THR C 2 64  ? 106.756 115.788 112.670 1.00 34.70 ?  43  THR C N     1 
ATOM   11341 C  CA    . THR C 2 64  ? 106.292 114.543 112.036 1.00 35.10 ?  43  THR C CA    1 
ATOM   11342 C  C     . THR C 2 64  ? 105.797 113.521 113.073 1.00 34.78 ?  43  THR C C     1 
ATOM   11343 O  O     . THR C 2 64  ? 104.950 112.691 112.762 1.00 35.04 ?  43  THR C O     1 
ATOM   11344 C  CB    . THR C 2 64  ? 107.312 113.903 111.042 1.00 35.30 ?  43  THR C CB    1 
ATOM   11345 O  OG1   . THR C 2 64  ? 108.572 113.667 111.690 1.00 36.01 ?  43  THR C OG1   1 
ATOM   11346 C  CG2   . THR C 2 64  ? 107.515 114.795 109.818 1.00 35.96 ?  43  THR C CG2   1 
ATOM   11347 N  N     . TRP C 2 65  ? 106.301 113.610 114.306 1.00 34.63 ?  44  TRP C N     1 
ATOM   11348 C  CA    . TRP C 2 65  ? 105.828 112.760 115.407 1.00 34.37 ?  44  TRP C CA    1 
ATOM   11349 C  C     . TRP C 2 65  ? 104.434 113.180 115.871 1.00 35.13 ?  44  TRP C C     1 
ATOM   11350 O  O     . TRP C 2 65  ? 103.526 112.348 115.997 1.00 34.98 ?  44  TRP C O     1 
ATOM   11351 C  CB    . TRP C 2 65  ? 106.804 112.812 116.581 1.00 33.95 ?  44  TRP C CB    1 
ATOM   11352 C  CG    . TRP C 2 65  ? 106.297 112.148 117.821 1.00 33.26 ?  44  TRP C CG    1 
ATOM   11353 C  CD1   . TRP C 2 65  ? 105.801 112.759 118.939 1.00 32.51 ?  44  TRP C CD1   1 
ATOM   11354 C  CD2   . TRP C 2 65  ? 106.241 110.737 118.075 1.00 30.93 ?  44  TRP C CD2   1 
ATOM   11355 N  NE1   . TRP C 2 65  ? 105.444 111.815 119.878 1.00 31.66 ?  44  TRP C NE1   1 
ATOM   11356 C  CE2   . TRP C 2 65  ? 105.703 110.566 119.372 1.00 30.39 ?  44  TRP C CE2   1 
ATOM   11357 C  CE3   . TRP C 2 65  ? 106.599 109.602 117.334 1.00 30.36 ?  44  TRP C CE3   1 
ATOM   11358 C  CZ2   . TRP C 2 65  ? 105.503 109.306 119.941 1.00 29.16 ?  44  TRP C CZ2   1 
ATOM   11359 C  CZ3   . TRP C 2 65  ? 106.404 108.342 117.903 1.00 28.84 ?  44  TRP C CZ3   1 
ATOM   11360 C  CH2   . TRP C 2 65  ? 105.867 108.208 119.196 1.00 29.34 ?  44  TRP C CH2   1 
ATOM   11361 N  N     . LYS C 2 66  ? 104.287 114.476 116.138 1.00 35.69 ?  45  LYS C N     1 
ATOM   11362 C  CA    . LYS C 2 66  ? 103.012 115.071 116.512 1.00 36.38 ?  45  LYS C CA    1 
ATOM   11363 C  C     . LYS C 2 66  ? 101.886 114.682 115.547 1.00 36.24 ?  45  LYS C C     1 
ATOM   11364 O  O     . LYS C 2 66  ? 100.749 114.516 115.974 1.00 36.78 ?  45  LYS C O     1 
ATOM   11365 C  CB    . LYS C 2 66  ? 103.167 116.592 116.554 1.00 37.14 ?  45  LYS C CB    1 
ATOM   11366 C  CG    . LYS C 2 66  ? 101.931 117.365 116.977 1.00 38.91 ?  45  LYS C CG    1 
ATOM   11367 C  CD    . LYS C 2 66  ? 102.130 118.862 116.736 1.00 41.12 ?  45  LYS C CD    1 
ATOM   11368 C  CE    . LYS C 2 66  ? 101.073 119.682 117.458 1.00 43.00 ?  45  LYS C CE    1 
ATOM   11369 N  NZ    . LYS C 2 66  ? 100.944 119.268 118.889 1.00 44.38 1  45  LYS C NZ    1 
ATOM   11370 N  N     . TYR C 2 67  ? 102.231 114.504 114.269 1.00 36.03 ?  46  TYR C N     1 
ATOM   11371 C  CA    . TYR C 2 67  ? 101.274 114.269 113.175 1.00 36.03 ?  46  TYR C CA    1 
ATOM   11372 C  C     . TYR C 2 67  ? 100.832 112.811 112.993 1.00 35.25 ?  46  TYR C C     1 
ATOM   11373 O  O     . TYR C 2 67  ? 99.887  112.531 112.247 1.00 35.32 ?  46  TYR C O     1 
ATOM   11374 C  CB    . TYR C 2 67  ? 101.853 114.766 111.838 1.00 36.60 ?  46  TYR C CB    1 
ATOM   11375 C  CG    . TYR C 2 67  ? 102.144 116.259 111.761 1.00 37.85 ?  46  TYR C CG    1 
ATOM   11376 C  CD1   . TYR C 2 67  ? 101.627 117.146 112.705 1.00 38.97 ?  46  TYR C CD1   1 
ATOM   11377 C  CD2   . TYR C 2 67  ? 102.929 116.783 110.724 1.00 40.06 ?  46  TYR C CD2   1 
ATOM   11378 C  CE1   . TYR C 2 67  ? 101.897 118.512 112.644 1.00 40.36 ?  46  TYR C CE1   1 
ATOM   11379 C  CE2   . TYR C 2 67  ? 103.204 118.158 110.648 1.00 40.53 ?  46  TYR C CE2   1 
ATOM   11380 C  CZ    . TYR C 2 67  ? 102.678 119.014 111.615 1.00 41.43 ?  46  TYR C CZ    1 
ATOM   11381 O  OH    . TYR C 2 67  ? 102.921 120.375 111.566 1.00 41.48 ?  46  TYR C OH    1 
ATOM   11382 N  N     . LEU C 2 68  ? 101.525 111.884 113.649 1.00 33.80 ?  47  LEU C N     1 
ATOM   11383 C  CA    . LEU C 2 68  ? 101.169 110.472 113.563 1.00 32.77 ?  47  LEU C CA    1 
ATOM   11384 C  C     . LEU C 2 68  ? 99.919  110.192 114.387 1.00 31.84 ?  47  LEU C C     1 
ATOM   11385 O  O     . LEU C 2 68  ? 99.677  110.848 115.397 1.00 31.90 ?  47  LEU C O     1 
ATOM   11386 C  CB    . LEU C 2 68  ? 102.315 109.591 114.066 1.00 32.39 ?  47  LEU C CB    1 
ATOM   11387 C  CG    . LEU C 2 68  ? 103.664 109.548 113.346 1.00 32.68 ?  47  LEU C CG    1 
ATOM   11388 C  CD1   . LEU C 2 68  ? 104.599 108.597 114.086 1.00 33.03 ?  47  LEU C CD1   1 
ATOM   11389 C  CD2   . LEU C 2 68  ? 103.532 109.136 111.876 1.00 32.78 ?  47  LEU C CD2   1 
ATOM   11390 N  N     . GLY C 2 69  ? 99.139  109.204 113.963 1.00 30.99 ?  48  GLY C N     1 
ATOM   11391 C  CA    . GLY C 2 69  ? 97.997  108.745 114.751 1.00 30.58 ?  48  GLY C CA    1 
ATOM   11392 C  C     . GLY C 2 69  ? 98.416  108.127 116.079 1.00 29.87 ?  48  GLY C C     1 
ATOM   11393 O  O     . GLY C 2 69  ? 99.572  107.745 116.256 1.00 28.79 ?  48  GLY C O     1 
ATOM   11394 N  N     . LYS C 2 70  ? 97.479  108.041 117.017 1.00 29.89 ?  49  LYS C N     1 
ATOM   11395 C  CA    . LYS C 2 70  ? 97.760  107.442 118.321 1.00 29.49 ?  49  LYS C CA    1 
ATOM   11396 C  C     . LYS C 2 70  ? 98.237  105.983 118.198 1.00 28.74 ?  49  LYS C C     1 
ATOM   11397 O  O     . LYS C 2 70  ? 99.154  105.567 118.918 1.00 27.27 ?  49  LYS C O     1 
ATOM   11398 C  CB    . LYS C 2 70  ? 96.554  107.575 119.256 1.00 30.67 ?  49  LYS C CB    1 
ATOM   11399 C  CG    . LYS C 2 70  ? 96.431  108.984 119.887 1.00 33.73 ?  49  LYS C CG    1 
ATOM   11400 C  CD    . LYS C 2 70  ? 95.038  109.263 120.479 1.00 38.93 ?  49  LYS C CD    1 
ATOM   11401 C  CE    . LYS C 2 70  ? 94.819  108.610 121.850 1.00 41.04 ?  49  LYS C CE    1 
ATOM   11402 N  NZ    . LYS C 2 70  ? 95.583  109.268 122.951 1.00 42.21 1  49  LYS C NZ    1 
ATOM   11403 N  N     . ASN C 2 71  ? 97.623  105.233 117.277 1.00 27.54 ?  50  ASN C N     1 
ATOM   11404 C  CA    . ASN C 2 71  ? 98.036  103.860 116.978 1.00 27.00 ?  50  ASN C CA    1 
ATOM   11405 C  C     . ASN C 2 71  ? 99.488  103.771 116.508 1.00 26.19 ?  50  ASN C C     1 
ATOM   11406 O  O     . ASN C 2 71  ? 100.242 102.869 116.929 1.00 25.38 ?  50  ASN C O     1 
ATOM   11407 C  CB    . ASN C 2 71  ? 97.099  103.210 115.935 1.00 27.08 ?  50  ASN C CB    1 
ATOM   11408 C  CG    . ASN C 2 71  ? 97.066  103.961 114.582 1.00 28.69 ?  50  ASN C CG    1 
ATOM   11409 O  OD1   . ASN C 2 71  ? 96.992  105.204 114.523 1.00 30.45 ?  50  ASN C OD1   1 
ATOM   11410 N  ND2   . ASN C 2 71  ? 97.092  103.191 113.484 1.00 29.42 ?  50  ASN C ND2   1 
ATOM   11411 N  N     . GLU C 2 72  ? 99.870  104.706 115.640 1.00 24.91 ?  51  GLU C N     1 
ATOM   11412 C  CA    . GLU C 2 72  ? 101.215 104.734 115.078 1.00 24.97 ?  51  GLU C CA    1 
ATOM   11413 C  C     . GLU C 2 72  ? 102.263 105.060 116.148 1.00 24.45 ?  51  GLU C C     1 
ATOM   11414 O  O     . GLU C 2 72  ? 103.315 104.407 116.220 1.00 23.90 ?  51  GLU C O     1 
ATOM   11415 C  CB    . GLU C 2 72  ? 101.289 105.735 113.924 1.00 25.27 ?  51  GLU C CB    1 
ATOM   11416 C  CG    . GLU C 2 72  ? 100.445 105.349 112.711 1.00 26.16 ?  51  GLU C CG    1 
ATOM   11417 C  CD    . GLU C 2 72  ? 100.512 106.402 111.613 1.00 28.70 ?  51  GLU C CD    1 
ATOM   11418 O  OE1   . GLU C 2 72  ? 99.853  107.452 111.755 1.00 28.70 ?  51  GLU C OE1   1 
ATOM   11419 O  OE2   . GLU C 2 72  ? 101.224 106.181 110.608 1.00 28.92 -1 51  GLU C OE2   1 
ATOM   11420 N  N     . GLN C 2 73  ? 101.956 106.050 116.985 1.00 23.75 ?  52  GLN C N     1 
ATOM   11421 C  CA    . GLN C 2 73  ? 102.850 106.441 118.072 1.00 23.94 ?  52  GLN C CA    1 
ATOM   11422 C  C     . GLN C 2 73  ? 103.015 105.306 119.084 1.00 23.36 ?  52  GLN C C     1 
ATOM   11423 O  O     . GLN C 2 73  ? 104.108 105.084 119.591 1.00 22.95 ?  52  GLN C O     1 
ATOM   11424 C  CB    . GLN C 2 73  ? 102.331 107.696 118.790 1.00 24.28 ?  52  GLN C CB    1 
ATOM   11425 C  CG    . GLN C 2 73  ? 102.474 109.013 118.002 1.00 25.22 ?  52  GLN C CG    1 
ATOM   11426 C  CD    . GLN C 2 73  ? 102.030 110.243 118.802 1.00 29.02 ?  52  GLN C CD    1 
ATOM   11427 O  OE1   . GLN C 2 73  ? 101.599 110.131 119.948 1.00 32.08 ?  52  GLN C OE1   1 
ATOM   11428 N  NE2   . GLN C 2 73  ? 102.139 111.418 118.194 1.00 29.13 ?  52  GLN C NE2   1 
ATOM   11429 N  N     . ASP C 2 74  ? 101.913 104.618 119.390 1.00 23.02 ?  53  ASP C N     1 
ATOM   11430 C  CA    . ASP C 2 74  ? 101.923 103.504 120.328 1.00 23.44 ?  53  ASP C CA    1 
ATOM   11431 C  C     . ASP C 2 74  ? 102.838 102.381 119.824 1.00 23.00 ?  53  ASP C C     1 
ATOM   11432 O  O     . ASP C 2 74  ? 103.685 101.893 120.566 1.00 22.96 ?  53  ASP C O     1 
ATOM   11433 C  CB    . ASP C 2 74  ? 100.501 102.965 120.545 1.00 23.31 ?  53  ASP C CB    1 
ATOM   11434 C  CG    . ASP C 2 74  ? 100.434 101.921 121.640 1.00 25.80 ?  53  ASP C CG    1 
ATOM   11435 O  OD1   . ASP C 2 74  ? 100.772 102.240 122.809 1.00 27.95 ?  53  ASP C OD1   1 
ATOM   11436 O  OD2   . ASP C 2 74  ? 100.030 100.782 121.334 1.00 26.30 -1 53  ASP C OD2   1 
ATOM   11437 N  N     . THR C 2 75  ? 102.646 101.975 118.571 1.00 22.20 ?  54  THR C N     1 
ATOM   11438 C  CA    . THR C 2 75  ? 103.460 100.930 117.964 1.00 21.84 ?  54  THR C CA    1 
ATOM   11439 C  C     . THR C 2 75  ? 104.926 101.348 117.935 1.00 22.09 ?  54  THR C C     1 
ATOM   11440 O  O     . THR C 2 75  ? 105.801 100.561 118.282 1.00 21.88 ?  54  THR C O     1 
ATOM   11441 C  CB    . THR C 2 75  ? 102.955 100.550 116.544 1.00 21.74 ?  54  THR C CB    1 
ATOM   11442 O  OG1   . THR C 2 75  ? 101.661 99.956  116.662 1.00 22.09 ?  54  THR C OG1   1 
ATOM   11443 C  CG2   . THR C 2 75  ? 103.886 99.526  115.881 1.00 19.76 ?  54  THR C CG2   1 
ATOM   11444 N  N     . TYR C 2 76  ? 105.186 102.589 117.536 1.00 22.38 ?  55  TYR C N     1 
ATOM   11445 C  CA    . TYR C 2 76  ? 106.553 103.104 117.490 1.00 22.85 ?  55  TYR C CA    1 
ATOM   11446 C  C     . TYR C 2 76  ? 107.262 103.045 118.855 1.00 22.56 ?  55  TYR C C     1 
ATOM   11447 O  O     . TYR C 2 76  ? 108.397 102.581 118.930 1.00 21.97 ?  55  TYR C O     1 
ATOM   11448 C  CB    . TYR C 2 76  ? 106.564 104.525 116.946 1.00 23.57 ?  55  TYR C CB    1 
ATOM   11449 C  CG    . TYR C 2 76  ? 107.918 105.022 116.483 1.00 25.59 ?  55  TYR C CG    1 
ATOM   11450 C  CD1   . TYR C 2 76  ? 108.324 104.866 115.153 1.00 27.49 ?  55  TYR C CD1   1 
ATOM   11451 C  CD2   . TYR C 2 76  ? 108.778 105.678 117.363 1.00 27.70 ?  55  TYR C CD2   1 
ATOM   11452 C  CE1   . TYR C 2 76  ? 109.564 105.347 114.717 1.00 30.28 ?  55  TYR C CE1   1 
ATOM   11453 C  CE2   . TYR C 2 76  ? 110.025 106.158 116.940 1.00 30.38 ?  55  TYR C CE2   1 
ATOM   11454 C  CZ    . TYR C 2 76  ? 110.409 105.987 115.615 1.00 31.39 ?  55  TYR C CZ    1 
ATOM   11455 O  OH    . TYR C 2 76  ? 111.633 106.472 115.194 1.00 32.67 ?  55  TYR C OH    1 
ATOM   11456 N  N     . MET C 2 77  ? 106.599 103.518 119.913 1.00 23.14 ?  56  MET C N     1 
ATOM   11457 C  CA    . MET C 2 77  ? 107.171 103.502 121.273 1.00 23.90 ?  56  MET C CA    1 
ATOM   11458 C  C     . MET C 2 77  ? 107.494 102.079 121.708 1.00 23.24 ?  56  MET C C     1 
ATOM   11459 O  O     . MET C 2 77  ? 108.547 101.809 122.300 1.00 22.47 ?  56  MET C O     1 
ATOM   11460 C  CB    . MET C 2 77  ? 106.194 104.097 122.293 1.00 24.38 ?  56  MET C CB    1 
ATOM   11461 C  CG    . MET C 2 77  ? 105.869 105.574 122.127 1.00 28.52 ?  56  MET C CG    1 
ATOM   11462 S  SD    . MET C 2 77  ? 107.195 106.643 122.672 1.00 34.32 ?  56  MET C SD    1 
ATOM   11463 C  CE    . MET C 2 77  ? 107.231 106.313 124.437 1.00 33.84 ?  56  MET C CE    1 
ATOM   11464 N  N     . LYS C 2 78  ? 106.565 101.172 121.418 1.00 23.25 ?  57  LYS C N     1 
ATOM   11465 C  CA    . LYS C 2 78  ? 106.662 99.801  121.904 1.00 22.98 ?  57  LYS C CA    1 
ATOM   11466 C  C     . LYS C 2 78  ? 107.775 99.066  121.172 1.00 22.77 ?  57  LYS C C     1 
ATOM   11467 O  O     . LYS C 2 78  ? 108.563 98.354  121.788 1.00 22.56 ?  57  LYS C O     1 
ATOM   11468 C  CB    . LYS C 2 78  ? 105.306 99.095  121.785 1.00 22.99 ?  57  LYS C CB    1 
ATOM   11469 C  CG    . LYS C 2 78  ? 104.317 99.533  122.868 1.00 24.86 ?  57  LYS C CG    1 
ATOM   11470 C  CD    . LYS C 2 78  ? 102.911 98.980  122.638 1.00 27.37 ?  57  LYS C CD    1 
ATOM   11471 C  CE    . LYS C 2 78  ? 102.016 99.231  123.858 1.00 28.99 ?  57  LYS C CE    1 
ATOM   11472 N  NZ    . LYS C 2 78  ? 100.605 98.865  123.536 1.00 29.82 1  57  LYS C NZ    1 
ATOM   11473 N  N     . VAL C 2 79  ? 107.833 99.276  119.859 1.00 22.70 ?  58  VAL C N     1 
ATOM   11474 C  CA    . VAL C 2 79  ? 108.884 98.752  118.990 1.00 23.48 ?  58  VAL C CA    1 
ATOM   11475 C  C     . VAL C 2 79  ? 110.291 99.131  119.511 1.00 23.04 ?  58  VAL C C     1 
ATOM   11476 O  O     . VAL C 2 79  ? 111.160 98.253  119.693 1.00 22.83 ?  58  VAL C O     1 
ATOM   11477 C  CB    . VAL C 2 79  ? 108.599 99.226  117.530 1.00 24.24 ?  58  VAL C CB    1 
ATOM   11478 C  CG1   . VAL C 2 79  ? 109.860 99.546  116.746 1.00 25.71 ?  58  VAL C CG1   1 
ATOM   11479 C  CG2   . VAL C 2 79  ? 107.683 98.213  116.809 1.00 25.04 ?  58  VAL C CG2   1 
ATOM   11480 N  N     . LEU C 2 80  ? 110.496 100.413 119.799 1.00 22.84 ?  59  LEU C N     1 
ATOM   11481 C  CA    . LEU C 2 80  ? 111.790 100.881 120.301 1.00 23.35 ?  59  LEU C CA    1 
ATOM   11482 C  C     . LEU C 2 80  ? 112.073 100.352 121.712 1.00 22.75 ?  59  LEU C C     1 
ATOM   11483 O  O     . LEU C 2 80  ? 113.223 100.080 122.046 1.00 22.75 ?  59  LEU C O     1 
ATOM   11484 C  CB    . LEU C 2 80  ? 111.896 102.412 120.274 1.00 23.91 ?  59  LEU C CB    1 
ATOM   11485 C  CG    . LEU C 2 80  ? 111.934 103.218 118.960 1.00 26.63 ?  59  LEU C CG    1 
ATOM   11486 C  CD1   . LEU C 2 80  ? 112.480 104.612 119.221 1.00 26.99 ?  59  LEU C CD1   1 
ATOM   11487 C  CD2   . LEU C 2 80  ? 112.751 102.547 117.868 1.00 27.23 ?  59  LEU C CD2   1 
ATOM   11488 N  N     . ALA C 2 81  ? 111.022 100.185 122.519 1.00 22.28 ?  60  ALA C N     1 
ATOM   11489 C  CA    . ALA C 2 81  ? 111.159 99.619  123.865 1.00 22.21 ?  60  ALA C CA    1 
ATOM   11490 C  C     . ALA C 2 81  ? 111.620 98.159  123.814 1.00 22.07 ?  60  ALA C C     1 
ATOM   11491 O  O     . ALA C 2 81  ? 112.477 97.764  124.597 1.00 21.97 ?  60  ALA C O     1 
ATOM   11492 C  CB    . ALA C 2 81  ? 109.847 99.773  124.663 1.00 22.38 ?  60  ALA C CB    1 
ATOM   11493 N  N     . GLY C 2 82  ? 111.078 97.389  122.863 1.00 21.67 ?  61  GLY C N     1 
ATOM   11494 C  CA    . GLY C 2 82  ? 111.494 96.012  122.610 1.00 21.74 ?  61  GLY C CA    1 
ATOM   11495 C  C     . GLY C 2 82  ? 112.949 95.929  122.183 1.00 21.79 ?  61  GLY C C     1 
ATOM   11496 O  O     . GLY C 2 82  ? 113.687 95.022  122.597 1.00 21.93 ?  61  GLY C O     1 
ATOM   11497 N  N     . LEU C 2 83  ? 113.366 96.895  121.366 1.00 21.54 ?  62  LEU C N     1 
ATOM   11498 C  CA    . LEU C 2 83  ? 114.763 97.019  120.952 1.00 21.12 ?  62  LEU C CA    1 
ATOM   11499 C  C     . LEU C 2 83  ? 115.655 97.357  122.138 1.00 20.89 ?  62  LEU C C     1 
ATOM   11500 O  O     . LEU C 2 83  ? 116.739 96.786  122.272 1.00 20.84 ?  62  LEU C O     1 
ATOM   11501 C  CB    . LEU C 2 83  ? 114.932 98.084  119.862 1.00 21.23 ?  62  LEU C CB    1 
ATOM   11502 C  CG    . LEU C 2 83  ? 114.293 97.856  118.485 1.00 21.98 ?  62  LEU C CG    1 
ATOM   11503 C  CD1   . LEU C 2 83  ? 114.435 99.096  117.598 1.00 24.12 ?  62  LEU C CD1   1 
ATOM   11504 C  CD2   . LEU C 2 83  ? 114.876 96.647  117.780 1.00 22.03 ?  62  LEU C CD2   1 
ATOM   11505 N  N     . THR C 2 84  ? 115.197 98.282  122.983 1.00 19.93 ?  63  THR C N     1 
ATOM   11506 C  CA    . THR C 2 84  ? 115.951 98.688  124.167 1.00 19.71 ?  63  THR C CA    1 
ATOM   11507 C  C     . THR C 2 84  ? 116.227 97.494  125.067 1.00 19.63 ?  63  THR C C     1 
ATOM   11508 O  O     . THR C 2 84  ? 117.336 97.355  125.591 1.00 19.62 ?  63  THR C O     1 
ATOM   11509 C  CB    . THR C 2 84  ? 115.207 99.781  124.975 1.00 20.22 ?  63  THR C CB    1 
ATOM   11510 O  OG1   . THR C 2 84  ? 114.824 100.855 124.099 1.00 19.37 ?  63  THR C OG1   1 
ATOM   11511 C  CG2   . THR C 2 84  ? 116.080 100.303 126.089 1.00 19.45 ?  63  THR C CG2   1 
ATOM   11512 N  N     . LEU C 2 85  ? 115.220 96.644  125.249 1.00 19.66 ?  64  LEU C N     1 
ATOM   11513 C  CA    . LEU C 2 85  ? 115.357 95.456  126.088 1.00 20.51 ?  64  LEU C CA    1 
ATOM   11514 C  C     . LEU C 2 85  ? 116.431 94.514  125.534 1.00 20.84 ?  64  LEU C C     1 
ATOM   11515 O  O     . LEU C 2 85  ? 117.328 94.092  126.266 1.00 21.30 ?  64  LEU C O     1 
ATOM   11516 C  CB    . LEU C 2 85  ? 114.012 94.729  126.264 1.00 20.03 ?  64  LEU C CB    1 
ATOM   11517 C  CG    . LEU C 2 85  ? 114.097 93.441  127.115 1.00 21.43 ?  64  LEU C CG    1 
ATOM   11518 C  CD1   . LEU C 2 85  ? 114.471 93.735  128.587 1.00 21.61 ?  64  LEU C CD1   1 
ATOM   11519 C  CD2   . LEU C 2 85  ? 112.815 92.614  127.054 1.00 20.99 ?  64  LEU C CD2   1 
ATOM   11520 N  N     . LEU C 2 86  ? 116.339 94.209  124.245 1.00 21.37 ?  65  LEU C N     1 
ATOM   11521 C  CA    . LEU C 2 86  ? 117.326 93.366  123.567 1.00 21.92 ?  65  LEU C CA    1 
ATOM   11522 C  C     . LEU C 2 86  ? 118.764 93.891  123.718 1.00 21.76 ?  65  LEU C C     1 
ATOM   11523 O  O     . LEU C 2 86  ? 119.665 93.125  124.062 1.00 21.72 ?  65  LEU C O     1 
ATOM   11524 C  CB    . LEU C 2 86  ? 116.975 93.204  122.079 1.00 22.42 ?  65  LEU C CB    1 
ATOM   11525 C  CG    . LEU C 2 86  ? 115.733 92.401  121.640 1.00 24.26 ?  65  LEU C CG    1 
ATOM   11526 C  CD1   . LEU C 2 86  ? 115.552 92.519  120.127 1.00 24.67 ?  65  LEU C CD1   1 
ATOM   11527 C  CD2   . LEU C 2 86  ? 115.838 90.940  122.042 1.00 25.60 ?  65  LEU C CD2   1 
ATOM   11528 N  N     . ASP C 2 87  ? 118.973 95.183  123.460 1.00 21.75 ?  66  ASP C N     1 
ATOM   11529 C  CA    . ASP C 2 87  ? 120.301 95.808  123.625 1.00 21.99 ?  66  ASP C CA    1 
ATOM   11530 C  C     . ASP C 2 87  ? 120.791 95.860  125.076 1.00 21.76 ?  66  ASP C C     1 
ATOM   11531 O  O     . ASP C 2 87  ? 121.998 95.758  125.336 1.00 21.65 ?  66  ASP C O     1 
ATOM   11532 C  CB    . ASP C 2 87  ? 120.311 97.230  123.057 1.00 22.23 ?  66  ASP C CB    1 
ATOM   11533 C  CG    . ASP C 2 87  ? 120.793 97.282  121.634 1.00 24.59 ?  66  ASP C CG    1 
ATOM   11534 O  OD1   . ASP C 2 87  ? 121.786 96.594  121.303 1.00 27.46 ?  66  ASP C OD1   1 
ATOM   11535 O  OD2   . ASP C 2 87  ? 120.179 98.028  120.845 1.00 27.98 -1 66  ASP C OD2   1 
ATOM   11536 N  N     . THR C 2 88  ? 119.860 96.056  126.006 1.00 21.50 ?  67  THR C N     1 
ATOM   11537 C  CA    . THR C 2 88  ? 120.176 96.001  127.429 1.00 21.80 ?  67  THR C CA    1 
ATOM   11538 C  C     . THR C 2 88  ? 120.824 94.650  127.787 1.00 22.04 ?  67  THR C C     1 
ATOM   11539 O  O     . THR C 2 88  ? 121.876 94.610  128.441 1.00 22.21 ?  67  THR C O     1 
ATOM   11540 C  CB    . THR C 2 88  ? 118.926 96.267  128.285 1.00 22.15 ?  67  THR C CB    1 
ATOM   11541 O  OG1   . THR C 2 88  ? 118.414 97.565  127.973 1.00 22.23 ?  67  THR C OG1   1 
ATOM   11542 C  CG2   . THR C 2 88  ? 119.242 96.209  129.783 1.00 21.19 ?  67  THR C CG2   1 
ATOM   11543 N  N     . GLU C 2 89  ? 120.214 93.560  127.331 1.00 21.55 ?  68  GLU C N     1 
ATOM   11544 C  CA    . GLU C 2 89  ? 120.709 92.230  127.659 1.00 21.81 ?  68  GLU C CA    1 
ATOM   11545 C  C     . GLU C 2 89  ? 121.937 91.843  126.822 1.00 21.35 ?  68  GLU C C     1 
ATOM   11546 O  O     . GLU C 2 89  ? 122.840 91.170  127.315 1.00 21.34 ?  68  GLU C O     1 
ATOM   11547 C  CB    . GLU C 2 89  ? 119.582 91.194  127.579 1.00 22.25 ?  68  GLU C CB    1 
ATOM   11548 C  CG    . GLU C 2 89  ? 118.661 91.207  128.833 1.00 24.02 ?  68  GLU C CG    1 
ATOM   11549 C  CD    . GLU C 2 89  ? 119.443 91.082  130.143 1.00 25.78 ?  68  GLU C CD    1 
ATOM   11550 O  OE1   . GLU C 2 89  ? 120.343 90.220  130.234 1.00 26.69 ?  68  GLU C OE1   1 
ATOM   11551 O  OE2   . GLU C 2 89  ? 119.157 91.847  131.093 1.00 28.98 -1 68  GLU C OE2   1 
ATOM   11552 N  N     . GLN C 2 90  ? 121.993 92.315  125.577 1.00 20.82 ?  69  GLN C N     1 
ATOM   11553 C  CA    . GLN C 2 90  ? 123.155 92.084  124.728 1.00 21.28 ?  69  GLN C CA    1 
ATOM   11554 C  C     . GLN C 2 90  ? 124.395 92.783  125.296 1.00 21.24 ?  69  GLN C C     1 
ATOM   11555 O  O     . GLN C 2 90  ? 125.500 92.236  125.236 1.00 20.99 ?  69  GLN C O     1 
ATOM   11556 C  CB    . GLN C 2 90  ? 122.879 92.524  123.279 1.00 21.86 ?  69  GLN C CB    1 
ATOM   11557 C  CG    . GLN C 2 90  ? 123.909 91.996  122.254 1.00 24.29 ?  69  GLN C CG    1 
ATOM   11558 C  CD    . GLN C 2 90  ? 123.813 90.483  122.032 1.00 27.14 ?  69  GLN C CD    1 
ATOM   11559 O  OE1   . GLN C 2 90  ? 123.283 89.752  122.874 1.00 27.13 ?  69  GLN C OE1   1 
ATOM   11560 N  NE2   . GLN C 2 90  ? 124.343 90.010  120.901 1.00 27.69 ?  69  GLN C NE2   1 
ATOM   11561 N  N     . GLY C 2 91  ? 124.194 93.969  125.875 1.00 20.62 ?  70  GLY C N     1 
ATOM   11562 C  CA    . GLY C 2 91  ? 125.283 94.745  126.475 1.00 22.00 ?  70  GLY C CA    1 
ATOM   11563 C  C     . GLY C 2 91  ? 125.662 94.284  127.868 1.00 22.45 ?  70  GLY C C     1 
ATOM   11564 O  O     . GLY C 2 91  ? 126.848 94.169  128.168 1.00 23.53 ?  70  GLY C O     1 
ATOM   11565 N  N     . ASN C 2 92  ? 124.661 94.020  128.711 1.00 22.79 ?  71  ASN C N     1 
ATOM   11566 C  CA    . ASN C 2 92  ? 124.889 93.593  130.101 1.00 23.85 ?  71  ASN C CA    1 
ATOM   11567 C  C     . ASN C 2 92  ? 125.429 92.171  130.198 1.00 24.33 ?  71  ASN C C     1 
ATOM   11568 O  O     . ASN C 2 92  ? 126.236 91.868  131.085 1.00 24.17 ?  71  ASN C O     1 
ATOM   11569 C  CB    . ASN C 2 92  ? 123.592 93.645  130.918 1.00 23.74 ?  71  ASN C CB    1 
ATOM   11570 C  CG    . ASN C 2 92  ? 123.096 95.057  131.180 1.00 24.38 ?  71  ASN C CG    1 
ATOM   11571 O  OD1   . ASN C 2 92  ? 123.683 96.050  130.733 1.00 25.16 ?  71  ASN C OD1   1 
ATOM   11572 N  ND2   . ASN C 2 92  ? 121.994 95.148  131.906 1.00 24.07 ?  71  ASN C ND2   1 
ATOM   11573 N  N     . THR C 2 93  ? 124.984 91.306  129.285 1.00 23.97 ?  72  THR C N     1 
ATOM   11574 C  CA    . THR C 2 93  ? 125.136 89.856  129.475 1.00 24.97 ?  72  THR C CA    1 
ATOM   11575 C  C     . THR C 2 93  ? 125.784 89.171  128.282 1.00 24.52 ?  72  THR C C     1 
ATOM   11576 O  O     . THR C 2 93  ? 126.833 88.554  128.425 1.00 25.39 ?  72  THR C O     1 
ATOM   11577 C  CB    . THR C 2 93  ? 123.772 89.178  129.777 1.00 24.54 ?  72  THR C CB    1 
ATOM   11578 O  OG1   . THR C 2 93  ? 123.144 89.829  130.889 1.00 26.43 ?  72  THR C OG1   1 
ATOM   11579 C  CG2   . THR C 2 93  ? 123.951 87.705  130.108 1.00 26.83 ?  72  THR C CG2   1 
ATOM   11580 N  N     . GLY C 2 94  ? 125.158 89.293  127.121 1.00 24.37 ?  73  GLY C N     1 
ATOM   11581 C  CA    . GLY C 2 94  ? 125.535 88.532  125.920 1.00 24.24 ?  73  GLY C CA    1 
ATOM   11582 C  C     . GLY C 2 94  ? 126.954 88.766  125.449 1.00 24.94 ?  73  GLY C C     1 
ATOM   11583 O  O     . GLY C 2 94  ? 127.763 87.832  125.400 1.00 25.86 ?  73  GLY C O     1 
ATOM   11584 N  N     . MET C 2 95  ? 127.264 90.009  125.101 1.00 24.07 ?  74  MET C N     1 
ATOM   11585 C  CA    . MET C 2 95  ? 128.604 90.324  124.622 1.00 24.35 ?  74  MET C CA    1 
ATOM   11586 C  C     . MET C 2 95  ? 129.726 90.125  125.659 1.00 23.52 ?  74  MET C C     1 
ATOM   11587 O  O     . MET C 2 95  ? 130.750 89.553  125.301 1.00 23.40 ?  74  MET C O     1 
ATOM   11588 C  CB    . MET C 2 95  ? 128.656 91.704  123.967 1.00 24.38 ?  74  MET C CB    1 
ATOM   11589 C  CG    . MET C 2 95  ? 127.931 91.781  122.623 1.00 27.47 ?  74  MET C CG    1 
ATOM   11590 S  SD    . MET C 2 95  ? 128.701 90.676  121.408 1.00 32.54 ?  74  MET C SD    1 
ATOM   11591 C  CE    . MET C 2 95  ? 130.203 91.533  121.094 1.00 34.32 ?  74  MET C CE    1 
ATOM   11592 N  N     . PRO C 2 96  ? 129.541 90.583  126.930 1.00 23.36 ?  75  PRO C N     1 
ATOM   11593 C  CA    . PRO C 2 96  ? 130.567 90.326  127.964 1.00 23.27 ?  75  PRO C CA    1 
ATOM   11594 C  C     . PRO C 2 96  ? 130.833 88.848  128.229 1.00 23.77 ?  75  PRO C C     1 
ATOM   11595 O  O     . PRO C 2 96  ? 131.990 88.461  128.394 1.00 23.46 ?  75  PRO C O     1 
ATOM   11596 C  CB    . PRO C 2 96  ? 129.970 90.961  129.231 1.00 23.55 ?  75  PRO C CB    1 
ATOM   11597 C  CG    . PRO C 2 96  ? 129.067 92.032  128.725 1.00 23.85 ?  75  PRO C CG    1 
ATOM   11598 C  CD    . PRO C 2 96  ? 128.471 91.460  127.448 1.00 22.76 ?  75  PRO C CD    1 
ATOM   11599 N  N     . ILE C 2 97  ? 129.779 88.031  128.294 1.00 23.81 ?  76  ILE C N     1 
ATOM   11600 C  CA    . ILE C 2 97  ? 129.948 86.597  128.539 1.00 24.52 ?  76  ILE C CA    1 
ATOM   11601 C  C     . ILE C 2 97  ? 130.660 85.864  127.382 1.00 23.92 ?  76  ILE C C     1 
ATOM   11602 O  O     . ILE C 2 97  ? 131.541 85.025  127.613 1.00 23.99 ?  76  ILE C O     1 
ATOM   11603 C  CB    . ILE C 2 97  ? 128.612 85.912  128.945 1.00 24.49 ?  76  ILE C CB    1 
ATOM   11604 C  CG1   . ILE C 2 97  ? 128.883 84.622  129.717 1.00 27.08 ?  76  ILE C CG1   1 
ATOM   11605 C  CG2   . ILE C 2 97  ? 127.706 85.632  127.727 1.00 26.06 ?  76  ILE C CG2   1 
ATOM   11606 C  CD1   . ILE C 2 97  ? 127.735 84.230  130.635 1.00 31.37 ?  76  ILE C CD1   1 
ATOM   11607 N  N     . VAL C 2 98  ? 130.304 86.200  126.146 1.00 23.97 ?  77  VAL C N     1 
ATOM   11608 C  CA    . VAL C 2 98  ? 131.018 85.662  124.979 1.00 24.01 ?  77  VAL C CA    1 
ATOM   11609 C  C     . VAL C 2 98  ? 132.488 86.134  124.999 1.00 25.23 ?  77  VAL C C     1 
ATOM   11610 O  O     . VAL C 2 98  ? 133.404 85.336  124.776 1.00 25.77 ?  77  VAL C O     1 
ATOM   11611 C  CB    . VAL C 2 98  ? 130.306 86.030  123.652 1.00 23.98 ?  77  VAL C CB    1 
ATOM   11612 C  CG1   . VAL C 2 98  ? 131.188 85.715  122.446 1.00 23.17 ?  77  VAL C CG1   1 
ATOM   11613 C  CG2   . VAL C 2 98  ? 128.972 85.279  123.553 1.00 22.55 ?  77  VAL C CG2   1 
ATOM   11614 N  N     . ALA C 2 99  ? 132.711 87.409  125.322 1.00 25.42 ?  78  ALA C N     1 
ATOM   11615 C  CA    . ALA C 2 99  ? 134.083 87.931  125.452 1.00 26.72 ?  78  ALA C CA    1 
ATOM   11616 C  C     . ALA C 2 99  ? 134.900 87.113  126.457 1.00 27.46 ?  78  ALA C C     1 
ATOM   11617 O  O     . ALA C 2 99  ? 136.060 86.792  126.202 1.00 28.07 ?  78  ALA C O     1 
ATOM   11618 C  CB    . ALA C 2 99  ? 134.075 89.397  125.844 1.00 26.52 ?  78  ALA C CB    1 
ATOM   11619 N  N     . GLU C 2 100 ? 134.273 86.747  127.573 1.00 28.33 ?  79  GLU C N     1 
ATOM   11620 C  CA    . GLU C 2 100 ? 134.945 85.987  128.630 1.00 29.60 ?  79  GLU C CA    1 
ATOM   11621 C  C     . GLU C 2 100 ? 135.456 84.629  128.140 1.00 29.64 ?  79  GLU C C     1 
ATOM   11622 O  O     . GLU C 2 100 ? 136.536 84.178  128.539 1.00 29.72 ?  79  GLU C O     1 
ATOM   11623 C  CB    . GLU C 2 100 ? 134.021 85.810  129.836 1.00 29.70 ?  79  GLU C CB    1 
ATOM   11624 C  CG    . GLU C 2 100 ? 134.671 85.094  131.020 1.00 33.58 ?  79  GLU C CG    1 
ATOM   11625 C  CD    . GLU C 2 100 ? 133.713 84.809  132.160 1.00 37.83 ?  79  GLU C CD    1 
ATOM   11626 O  OE1   . GLU C 2 100 ? 132.557 85.298  132.142 1.00 40.64 ?  79  GLU C OE1   1 
ATOM   11627 O  OE2   . GLU C 2 100 ? 134.122 84.077  133.087 1.00 41.40 -1 79  GLU C OE2   1 
ATOM   11628 N  N     . HIS C 2 101 ? 134.688 83.989  127.261 1.00 29.43 ?  80  HIS C N     1 
ATOM   11629 C  CA    . HIS C 2 101 ? 134.983 82.620  126.859 1.00 29.74 ?  80  HIS C CA    1 
ATOM   11630 C  C     . HIS C 2 101 ? 135.791 82.483  125.567 1.00 30.18 ?  80  HIS C C     1 
ATOM   11631 O  O     . HIS C 2 101 ? 136.347 81.425  125.298 1.00 30.30 ?  80  HIS C O     1 
ATOM   11632 C  CB    . HIS C 2 101 ? 133.693 81.782  126.839 1.00 29.21 ?  80  HIS C CB    1 
ATOM   11633 C  CG    . HIS C 2 101 ? 133.140 81.525  128.206 1.00 29.60 ?  80  HIS C CG    1 
ATOM   11634 N  ND1   . HIS C 2 101 ? 132.214 82.354  128.806 1.00 30.06 ?  80  HIS C ND1   1 
ATOM   11635 C  CD2   . HIS C 2 101 ? 133.416 80.555  129.109 1.00 29.49 ?  80  HIS C CD2   1 
ATOM   11636 C  CE1   . HIS C 2 101 ? 131.934 81.897  130.015 1.00 29.56 ?  80  HIS C CE1   1 
ATOM   11637 N  NE2   . HIS C 2 101 ? 132.648 80.806  130.222 1.00 30.20 ?  80  HIS C NE2   1 
ATOM   11638 N  N     . VAL C 2 102 ? 135.864 83.556  124.784 1.00 30.70 ?  81  VAL C N     1 
ATOM   11639 C  CA    . VAL C 2 102 ? 136.629 83.564  123.540 1.00 31.47 ?  81  VAL C CA    1 
ATOM   11640 C  C     . VAL C 2 102 ? 138.088 83.899  123.839 1.00 32.45 ?  81  VAL C C     1 
ATOM   11641 O  O     . VAL C 2 102 ? 138.368 84.869  124.554 1.00 32.50 ?  81  VAL C O     1 
ATOM   11642 C  CB    . VAL C 2 102 ? 136.050 84.571  122.511 1.00 31.18 ?  81  VAL C CB    1 
ATOM   11643 C  CG1   . VAL C 2 102 ? 136.976 84.722  121.302 1.00 31.20 ?  81  VAL C CG1   1 
ATOM   11644 C  CG2   . VAL C 2 102 ? 134.672 84.123  122.048 1.00 31.28 ?  81  VAL C CG2   1 
ATOM   11645 N  N     . ASP C 2 103 ? 139.002 83.101  123.282 1.00 33.38 ?  82  ASP C N     1 
ATOM   11646 C  CA    . ASP C 2 103 ? 140.441 83.274  123.503 1.00 34.82 ?  82  ASP C CA    1 
ATOM   11647 C  C     . ASP C 2 103 ? 141.082 84.269  122.543 1.00 34.74 ?  82  ASP C C     1 
ATOM   11648 O  O     . ASP C 2 103 ? 140.737 84.315  121.355 1.00 35.00 ?  82  ASP C O     1 
ATOM   11649 C  CB    . ASP C 2 103 ? 141.170 81.925  123.410 1.00 35.82 ?  82  ASP C CB    1 
ATOM   11650 C  CG    . ASP C 2 103 ? 140.918 81.032  124.622 1.00 38.29 ?  82  ASP C CG    1 
ATOM   11651 O  OD1   . ASP C 2 103 ? 140.737 81.558  125.747 1.00 41.49 ?  82  ASP C OD1   1 
ATOM   11652 O  OD2   . ASP C 2 103 ? 140.902 79.798  124.450 1.00 41.10 -1 82  ASP C OD2   1 
ATOM   11653 N  N     . GLY C 2 104 ? 142.021 85.056  123.069 1.00 34.89 ?  83  GLY C N     1 
ATOM   11654 C  CA    . GLY C 2 104 ? 142.794 86.010  122.267 1.00 35.11 ?  83  GLY C CA    1 
ATOM   11655 C  C     . GLY C 2 104 ? 142.454 87.455  122.579 1.00 34.96 ?  83  GLY C C     1 
ATOM   11656 O  O     . GLY C 2 104 ? 141.295 87.859  122.464 1.00 34.57 ?  83  GLY C O     1 
ATOM   11657 N  N     . HIS C 2 105 ? 143.470 88.233  122.959 1.00 35.02 ?  84  HIS C N     1 
ATOM   11658 C  CA    . HIS C 2 105 ? 143.278 89.622  123.401 1.00 34.83 ?  84  HIS C CA    1 
ATOM   11659 C  C     . HIS C 2 105 ? 142.616 90.523  122.367 1.00 33.77 ?  84  HIS C C     1 
ATOM   11660 O  O     . HIS C 2 105 ? 141.831 91.403  122.723 1.00 33.25 ?  84  HIS C O     1 
ATOM   11661 C  CB    . HIS C 2 105 ? 144.593 90.243  123.888 1.00 36.09 ?  84  HIS C CB    1 
ATOM   11662 C  CG    . HIS C 2 105 ? 145.019 89.757  125.240 1.00 39.17 ?  84  HIS C CG    1 
ATOM   11663 N  ND1   . HIS C 2 105 ? 146.345 89.605  125.595 1.00 43.00 ?  84  HIS C ND1   1 
ATOM   11664 C  CD2   . HIS C 2 105 ? 144.294 89.366  126.317 1.00 41.84 ?  84  HIS C CD2   1 
ATOM   11665 C  CE1   . HIS C 2 105 ? 146.416 89.152  126.836 1.00 43.47 ?  84  HIS C CE1   1 
ATOM   11666 N  NE2   . HIS C 2 105 ? 145.187 88.999  127.297 1.00 43.10 ?  84  HIS C NE2   1 
ATOM   11667 N  N     . GLN C 2 106 ? 142.913 90.294  121.093 1.00 32.84 ?  85  GLN C N     1 
ATOM   11668 C  CA    . GLN C 2 106 ? 142.297 91.091  120.036 1.00 32.29 ?  85  GLN C CA    1 
ATOM   11669 C  C     . GLN C 2 106 ? 140.823 90.728  119.819 1.00 30.88 ?  85  GLN C C     1 
ATOM   11670 O  O     . GLN C 2 106 ? 139.987 91.616  119.620 1.00 30.44 ?  85  GLN C O     1 
ATOM   11671 C  CB    . GLN C 2 106 ? 143.078 90.971  118.736 1.00 32.85 ?  85  GLN C CB    1 
ATOM   11672 C  CG    . GLN C 2 106 ? 144.479 91.564  118.811 1.00 35.55 ?  85  GLN C CG    1 
ATOM   11673 C  CD    . GLN C 2 106 ? 145.261 91.332  117.544 1.00 38.12 ?  85  GLN C CD    1 
ATOM   11674 O  OE1   . GLN C 2 106 ? 144.709 91.383  116.445 1.00 39.96 ?  85  GLN C OE1   1 
ATOM   11675 N  NE2   . GLN C 2 106 ? 146.559 91.075  117.688 1.00 40.39 ?  85  GLN C NE2   1 
ATOM   11676 N  N     . ARG C 2 107 ? 140.513 89.432  119.851 1.00 29.75 ?  86  ARG C N     1 
ATOM   11677 C  CA    . ARG C 2 107 ? 139.119 88.983  119.757 1.00 28.87 ?  86  ARG C CA    1 
ATOM   11678 C  C     . ARG C 2 107 ? 138.325 89.535  120.933 1.00 28.16 ?  86  ARG C C     1 
ATOM   11679 O  O     . ARG C 2 107 ? 137.201 90.003  120.757 1.00 27.55 ?  86  ARG C O     1 
ATOM   11680 C  CB    . ARG C 2 107 ? 139.022 87.459  119.725 1.00 28.48 ?  86  ARG C CB    1 
ATOM   11681 C  CG    . ARG C 2 107 ? 139.496 86.853  118.416 1.00 29.86 ?  86  ARG C CG    1 
ATOM   11682 C  CD    . ARG C 2 107 ? 139.426 85.335  118.425 1.00 30.23 ?  86  ARG C CD    1 
ATOM   11683 N  NE    . ARG C 2 107 ? 139.446 84.853  117.049 1.00 33.04 ?  86  ARG C NE    1 
ATOM   11684 C  CZ    . ARG C 2 107 ? 139.049 83.653  116.660 1.00 31.54 ?  86  ARG C CZ    1 
ATOM   11685 N  NH1   . ARG C 2 107 ? 138.609 82.770  117.545 1.00 31.85 1  86  ARG C NH1   1 
ATOM   11686 N  NH2   . ARG C 2 107 ? 139.105 83.341  115.376 1.00 34.74 ?  86  ARG C NH2   1 
ATOM   11687 N  N     . LYS C 2 108 ? 138.921 89.493  122.123 1.00 27.65 ?  87  LYS C N     1 
ATOM   11688 C  CA    . LYS C 2 108 ? 138.277 90.049  123.318 1.00 27.96 ?  87  LYS C CA    1 
ATOM   11689 C  C     . LYS C 2 108 ? 138.066 91.554  123.229 1.00 27.75 ?  87  LYS C C     1 
ATOM   11690 O  O     . LYS C 2 108 ? 137.046 92.058  123.696 1.00 28.29 ?  87  LYS C O     1 
ATOM   11691 C  CB    . LYS C 2 108 ? 139.056 89.712  124.590 1.00 27.80 ?  87  LYS C CB    1 
ATOM   11692 C  CG    . LYS C 2 108 ? 139.009 88.245  124.963 1.00 29.04 ?  87  LYS C CG    1 
ATOM   11693 C  CD    . LYS C 2 108 ? 139.783 88.012  126.253 1.00 31.15 ?  87  LYS C CD    1 
ATOM   11694 C  CE    . LYS C 2 108 ? 139.944 86.532  126.543 1.00 32.05 ?  87  LYS C CE    1 
ATOM   11695 N  NZ    . LYS C 2 108 ? 138.689 85.961  127.091 1.00 30.88 1  87  LYS C NZ    1 
ATOM   11696 N  N     . ALA C 2 109 ? 139.020 92.267  122.631 1.00 27.69 ?  88  ALA C N     1 
ATOM   11697 C  CA    . ALA C 2 109 ? 138.893 93.719  122.450 1.00 27.46 ?  88  ALA C CA    1 
ATOM   11698 C  C     . ALA C 2 109 ? 137.726 94.099  121.534 1.00 26.87 ?  88  ALA C C     1 
ATOM   11699 O  O     . ALA C 2 109 ? 137.027 95.078  121.790 1.00 26.47 ?  88  ALA C O     1 
ATOM   11700 C  CB    . ALA C 2 109 ? 140.186 94.309  121.924 1.00 27.98 ?  88  ALA C CB    1 
ATOM   11701 N  N     . VAL C 2 110 ? 137.535 93.333  120.461 1.00 25.98 ?  89  VAL C N     1 
ATOM   11702 C  CA    . VAL C 2 110 ? 136.413 93.544  119.544 1.00 25.46 ?  89  VAL C CA    1 
ATOM   11703 C  C     . VAL C 2 110 ? 135.090 93.281  120.271 1.00 24.57 ?  89  VAL C C     1 
ATOM   11704 O  O     . VAL C 2 110 ? 134.179 94.113  120.240 1.00 23.62 ?  89  VAL C O     1 
ATOM   11705 C  CB    . VAL C 2 110 ? 136.535 92.655  118.282 1.00 25.80 ?  89  VAL C CB    1 
ATOM   11706 C  CG1   . VAL C 2 110 ? 135.252 92.690  117.442 1.00 25.44 ?  89  VAL C CG1   1 
ATOM   11707 C  CG2   . VAL C 2 110 ? 137.739 93.087  117.444 1.00 26.23 ?  89  VAL C CG2   1 
ATOM   11708 N  N     . LEU C 2 111 ? 135.007 92.141  120.953 1.00 24.33 ?  90  LEU C N     1 
ATOM   11709 C  CA    . LEU C 2 111 ? 133.786 91.783  121.676 1.00 23.93 ?  90  LEU C CA    1 
ATOM   11710 C  C     . LEU C 2 111 ? 133.455 92.754  122.809 1.00 23.77 ?  90  LEU C C     1 
ATOM   11711 O  O     . LEU C 2 111 ? 132.285 93.068  123.027 1.00 23.04 ?  90  LEU C O     1 
ATOM   11712 C  CB    . LEU C 2 111 ? 133.836 90.338  122.180 1.00 23.73 ?  90  LEU C CB    1 
ATOM   11713 C  CG    . LEU C 2 111 ? 133.901 89.277  121.078 1.00 24.50 ?  90  LEU C CG    1 
ATOM   11714 C  CD1   . LEU C 2 111 ? 134.414 87.954  121.625 1.00 24.02 ?  90  LEU C CD1   1 
ATOM   11715 C  CD2   . LEU C 2 111 ? 132.547 89.095  120.388 1.00 25.38 ?  90  LEU C CD2   1 
ATOM   11716 N  N     . ASN C 2 112 ? 134.481 93.217  123.532 1.00 24.24 ?  91  ASN C N     1 
ATOM   11717 C  CA    . ASN C 2 112 ? 134.297 94.263  124.550 1.00 24.95 ?  91  ASN C CA    1 
ATOM   11718 C  C     . ASN C 2 112 ? 133.787 95.581  123.975 1.00 24.25 ?  91  ASN C C     1 
ATOM   11719 O  O     . ASN C 2 112 ? 132.942 96.238  124.581 1.00 23.99 ?  91  ASN C O     1 
ATOM   11720 C  CB    . ASN C 2 112 ? 135.594 94.529  125.321 1.00 25.81 ?  91  ASN C CB    1 
ATOM   11721 C  CG    . ASN C 2 112 ? 135.772 93.592  126.485 1.00 29.96 ?  91  ASN C CG    1 
ATOM   11722 O  OD1   . ASN C 2 112 ? 135.351 93.898  127.602 1.00 35.44 ?  91  ASN C OD1   1 
ATOM   11723 N  ND2   . ASN C 2 112 ? 136.394 92.439  126.240 1.00 32.37 ?  91  ASN C ND2   1 
ATOM   11724 N  N     . PHE C 2 113 ? 134.332 95.979  122.825 1.00 23.60 ?  92  PHE C N     1 
ATOM   11725 C  CA    . PHE C 2 113 ? 133.870 97.181  122.140 1.00 23.32 ?  92  PHE C CA    1 
ATOM   11726 C  C     . PHE C 2 113 ? 132.399 97.052  121.718 1.00 22.63 ?  92  PHE C C     1 
ATOM   11727 O  O     . PHE C 2 113 ? 131.614 97.981  121.915 1.00 21.94 ?  92  PHE C O     1 
ATOM   11728 C  CB    . PHE C 2 113 ? 134.720 97.480  120.897 1.00 23.27 ?  92  PHE C CB    1 
ATOM   11729 C  CG    . PHE C 2 113 ? 134.447 98.834  120.301 1.00 24.66 ?  92  PHE C CG    1 
ATOM   11730 C  CD1   . PHE C 2 113 ? 135.160 99.960  120.739 1.00 25.72 ?  92  PHE C CD1   1 
ATOM   11731 C  CD2   . PHE C 2 113 ? 133.466 98.996  119.326 1.00 25.36 ?  92  PHE C CD2   1 
ATOM   11732 C  CE1   . PHE C 2 113 ? 134.898 101.221 120.203 1.00 25.92 ?  92  PHE C CE1   1 
ATOM   11733 C  CE2   . PHE C 2 113 ? 133.194 100.258 118.783 1.00 25.82 ?  92  PHE C CE2   1 
ATOM   11734 C  CZ    . PHE C 2 113 ? 133.908 101.373 119.227 1.00 25.80 ?  92  PHE C CZ    1 
ATOM   11735 N  N     . MET C 2 114 ? 132.052 95.911  121.118 1.00 22.03 ?  93  MET C N     1 
ATOM   11736 C  CA    . MET C 2 114 ? 130.663 95.626  120.730 1.00 22.14 ?  93  MET C CA    1 
ATOM   11737 C  C     . MET C 2 114 ? 129.705 95.666  121.934 1.00 21.64 ?  93  MET C C     1 
ATOM   11738 O  O     . MET C 2 114 ? 128.616 96.240  121.839 1.00 21.59 ?  93  MET C O     1 
ATOM   11739 C  CB    . MET C 2 114 ? 130.569 94.283  120.015 1.00 22.46 ?  93  MET C CB    1 
ATOM   11740 C  CG    . MET C 2 114 ? 131.235 94.270  118.647 1.00 23.80 ?  93  MET C CG    1 
ATOM   11741 S  SD    . MET C 2 114 ? 131.270 92.618  117.918 1.00 28.07 ?  93  MET C SD    1 
ATOM   11742 C  CE    . MET C 2 114 ? 131.777 93.047  116.232 1.00 26.42 ?  93  MET C CE    1 
ATOM   11743 N  N     . ALA C 2 115 ? 130.130 95.090  123.064 1.00 20.98 ?  94  ALA C N     1 
ATOM   11744 C  CA    . ALA C 2 115 ? 129.364 95.152  124.323 1.00 20.58 ?  94  ALA C CA    1 
ATOM   11745 C  C     . ALA C 2 115 ? 129.092 96.583  124.785 1.00 21.01 ?  94  ALA C C     1 
ATOM   11746 O  O     . ALA C 2 115 ? 127.975 96.915  125.224 1.00 21.06 ?  94  ALA C O     1 
ATOM   11747 C  CB    . ALA C 2 115 ? 130.095 94.361  125.434 1.00 20.83 ?  94  ALA C CB    1 
ATOM   11748 N  N     . MET C 2 116 ? 130.123 97.424  124.723 1.00 20.36 ?  95  MET C N     1 
ATOM   11749 C  CA    . MET C 2 116 ? 129.986 98.822  125.088 1.00 20.83 ?  95  MET C CA    1 
ATOM   11750 C  C     . MET C 2 116 ? 128.949 99.513  124.187 1.00 20.55 ?  95  MET C C     1 
ATOM   11751 O  O     . MET C 2 116 ? 128.082 100.237 124.672 1.00 20.70 ?  95  MET C O     1 
ATOM   11752 C  CB    . MET C 2 116 ? 131.353 99.516  125.016 1.00 20.64 ?  95  MET C CB    1 
ATOM   11753 C  CG    . MET C 2 116 ? 131.333 101.026 125.256 1.00 21.42 ?  95  MET C CG    1 
ATOM   11754 S  SD    . MET C 2 116 ? 130.827 101.946 123.790 1.00 22.51 ?  95  MET C SD    1 
ATOM   11755 C  CE    . MET C 2 116 ? 132.100 101.481 122.614 1.00 20.66 ?  95  MET C CE    1 
ATOM   11756 N  N     . MET C 2 117 ? 129.033 99.264  122.885 1.00 20.50 ?  96  MET C N     1 
ATOM   11757 C  CA    . MET C 2 117 ? 128.089 99.846  121.941 1.00 21.22 ?  96  MET C CA    1 
ATOM   11758 C  C     . MET C 2 117 ? 126.649 99.478  122.296 1.00 21.11 ?  96  MET C C     1 
ATOM   11759 O  O     . MET C 2 117 ? 125.772 100.344 122.277 1.00 20.71 ?  96  MET C O     1 
ATOM   11760 C  CB    . MET C 2 117 ? 128.423 99.446  120.498 1.00 21.35 ?  96  MET C CB    1 
ATOM   11761 C  CG    . MET C 2 117 ? 129.692 100.130 119.898 1.00 22.54 ?  96  MET C CG    1 
ATOM   11762 S  SD    . MET C 2 117 ? 129.718 101.936 119.957 1.00 24.89 ?  96  MET C SD    1 
ATOM   11763 C  CE    . MET C 2 117 ? 128.565 102.345 118.647 1.00 24.95 ?  96  MET C CE    1 
ATOM   11764 N  N     . GLU C 2 118 ? 126.423 98.209  122.638 1.00 21.18 ?  97  GLU C N     1 
ATOM   11765 C  CA    . GLU C 2 118 ? 125.086 97.716  122.987 1.00 21.99 ?  97  GLU C CA    1 
ATOM   11766 C  C     . GLU C 2 118 ? 124.427 98.531  124.101 1.00 22.10 ?  97  GLU C C     1 
ATOM   11767 O  O     . GLU C 2 118 ? 123.320 99.046  123.924 1.00 22.22 ?  97  GLU C O     1 
ATOM   11768 C  CB    . GLU C 2 118 ? 125.103 96.229  123.379 1.00 22.01 ?  97  GLU C CB    1 
ATOM   11769 C  CG    . GLU C 2 118 ? 125.746 95.249  122.390 1.00 24.38 ?  97  GLU C CG    1 
ATOM   11770 C  CD    . GLU C 2 118 ? 125.094 95.200  121.002 1.00 26.32 ?  97  GLU C CD    1 
ATOM   11771 O  OE1   . GLU C 2 118 ? 124.572 96.215  120.519 1.00 29.86 ?  97  GLU C OE1   1 
ATOM   11772 O  OE2   . GLU C 2 118 ? 125.153 94.137  120.361 1.00 29.19 -1 97  GLU C OE2   1 
ATOM   11773 N  N     . ASN C 2 119 ? 125.096 98.652  125.246 1.00 22.26 ?  98  ASN C N     1 
ATOM   11774 C  CA    . ASN C 2 119 ? 124.454 99.300  126.390 1.00 21.91 ?  98  ASN C CA    1 
ATOM   11775 C  C     . ASN C 2 119 ? 124.802 100.775 126.639 1.00 22.41 ?  98  ASN C C     1 
ATOM   11776 O  O     . ASN C 2 119 ? 123.983 101.517 127.178 1.00 23.07 ?  98  ASN C O     1 
ATOM   11777 C  CB    . ASN C 2 119 ? 124.496 98.429  127.665 1.00 21.93 ?  98  ASN C CB    1 
ATOM   11778 C  CG    . ASN C 2 119 ? 125.899 98.162  128.167 1.00 21.31 ?  98  ASN C CG    1 
ATOM   11779 O  OD1   . ASN C 2 119 ? 126.890 98.585  127.568 1.00 21.88 ?  98  ASN C OD1   1 
ATOM   11780 N  ND2   . ASN C 2 119 ? 125.989 97.459  129.294 1.00 21.73 ?  98  ASN C ND2   1 
ATOM   11781 N  N     . ALA C 2 120 ? 126.009 101.190 126.263 1.00 22.75 ?  99  ALA C N     1 
ATOM   11782 C  CA    . ALA C 2 120 ? 126.430 102.580 126.434 1.00 23.12 ?  99  ALA C CA    1 
ATOM   11783 C  C     . ALA C 2 120 ? 126.019 103.468 125.276 1.00 23.60 ?  99  ALA C C     1 
ATOM   11784 O  O     . ALA C 2 120 ? 125.899 104.684 125.455 1.00 24.14 ?  99  ALA C O     1 
ATOM   11785 C  CB    . ALA C 2 120 ? 127.948 102.684 126.686 1.00 23.28 ?  99  ALA C CB    1 
ATOM   11786 N  N     . VAL C 2 121 ? 125.796 102.877 124.097 1.00 23.23 ?  100 VAL C N     1 
ATOM   11787 C  CA    . VAL C 2 121 ? 125.399 103.677 122.923 1.00 23.74 ?  100 VAL C CA    1 
ATOM   11788 C  C     . VAL C 2 121 ? 123.994 103.362 122.410 1.00 23.62 ?  100 VAL C C     1 
ATOM   11789 O  O     . VAL C 2 121 ? 123.152 104.254 122.358 1.00 24.51 ?  100 VAL C O     1 
ATOM   11790 C  CB    . VAL C 2 121 ? 126.426 103.589 121.773 1.00 23.19 ?  100 VAL C CB    1 
ATOM   11791 C  CG1   . VAL C 2 121 ? 125.950 104.394 120.550 1.00 24.10 ?  100 VAL C CG1   1 
ATOM   11792 C  CG2   . VAL C 2 121 ? 127.799 104.091 122.249 1.00 23.48 ?  100 VAL C CG2   1 
ATOM   11793 N  N     . HIS C 2 122 ? 123.747 102.105 122.047 1.00 23.45 ?  101 HIS C N     1 
ATOM   11794 C  CA    . HIS C 2 122 ? 122.472 101.715 121.440 1.00 23.81 ?  101 HIS C CA    1 
ATOM   11795 C  C     . HIS C 2 122 ? 121.295 101.835 122.385 1.00 24.33 ?  101 HIS C C     1 
ATOM   11796 O  O     . HIS C 2 122 ? 120.327 102.534 122.072 1.00 24.80 ?  101 HIS C O     1 
ATOM   11797 C  CB    . HIS C 2 122 ? 122.515 100.294 120.886 1.00 23.30 ?  101 HIS C CB    1 
ATOM   11798 C  CG    . HIS C 2 122 ? 123.512 100.099 119.789 1.00 22.96 ?  101 HIS C CG    1 
ATOM   11799 N  ND1   . HIS C 2 122 ? 123.789 98.860  119.251 1.00 22.78 ?  101 HIS C ND1   1 
ATOM   11800 C  CD2   . HIS C 2 122 ? 124.322 100.979 119.153 1.00 23.25 ?  101 HIS C CD2   1 
ATOM   11801 C  CE1   . HIS C 2 122 ? 124.715 98.988  118.320 1.00 22.57 ?  101 HIS C CE1   1 
ATOM   11802 N  NE2   . HIS C 2 122 ? 125.056 100.262 118.240 1.00 21.75 ?  101 HIS C NE2   1 
ATOM   11803 N  N     . ALA C 2 123 ? 121.360 101.130 123.519 1.00 24.40 ?  102 ALA C N     1 
ATOM   11804 C  CA    . ALA C 2 123 ? 120.256 101.138 124.481 1.00 24.00 ?  102 ALA C CA    1 
ATOM   11805 C  C     . ALA C 2 123 ? 119.950 102.566 124.934 1.00 24.05 ?  102 ALA C C     1 
ATOM   11806 O  O     . ALA C 2 123 ? 118.785 102.936 125.068 1.00 23.89 ?  102 ALA C O     1 
ATOM   11807 C  CB    . ALA C 2 123 ? 120.560 100.232 125.673 1.00 23.73 ?  102 ALA C CB    1 
ATOM   11808 N  N     . LYS C 2 124 ? 120.994 103.366 125.145 1.00 24.36 ?  103 LYS C N     1 
ATOM   11809 C  CA    . LYS C 2 124 ? 120.834 104.759 125.579 1.00 24.31 ?  103 LYS C CA    1 
ATOM   11810 C  C     . LYS C 2 124 ? 120.191 105.674 124.530 1.00 23.84 ?  103 LYS C C     1 
ATOM   11811 O  O     . LYS C 2 124 ? 119.375 106.537 124.879 1.00 24.21 ?  103 LYS C O     1 
ATOM   11812 C  CB    . LYS C 2 124 ? 122.152 105.350 126.089 1.00 24.93 ?  103 LYS C CB    1 
ATOM   11813 C  CG    . LYS C 2 124 ? 121.976 106.722 126.756 1.00 26.37 ?  103 LYS C CG    1 
ATOM   11814 C  CD    . LYS C 2 124 ? 123.255 107.210 127.415 1.00 29.42 ?  103 LYS C CD    1 
ATOM   11815 C  CE    . LYS C 2 124 ? 123.094 108.649 127.916 1.00 31.51 ?  103 LYS C CE    1 
ATOM   11816 N  NZ    . LYS C 2 124 ? 122.891 109.618 126.799 1.00 32.37 1  103 LYS C NZ    1 
ATOM   11817 N  N     . SER C 2 125 ? 120.544 105.480 123.257 1.00 23.52 ?  104 SER C N     1 
ATOM   11818 C  CA    . SER C 2 125 ? 119.968 106.254 122.153 0.50 23.23 ?  104 SER C CA    1 
ATOM   11819 C  C     . SER C 2 125 ? 118.440 106.204 122.147 1.00 22.91 ?  104 SER C C     1 
ATOM   11820 O  O     . SER C 2 125 ? 117.782 107.178 121.806 1.00 22.33 ?  104 SER C O     1 
ATOM   11821 C  CB    . SER C 2 125 ? 120.494 105.753 120.802 0.50 23.25 ?  104 SER C CB    1 
ATOM   11822 O  OG    . SER C 2 125 ? 121.902 105.862 120.720 0.50 24.57 ?  104 SER C OG    1 
ATOM   11823 N  N     . TYR C 2 126 ? 117.873 105.055 122.509 1.00 22.72 ?  105 TYR C N     1 
ATOM   11824 C  CA    . TYR C 2 126 ? 116.415 104.936 122.530 1.00 23.34 ?  105 TYR C CA    1 
ATOM   11825 C  C     . TYR C 2 126 ? 115.797 105.858 123.555 1.00 23.32 ?  105 TYR C C     1 
ATOM   11826 O  O     . TYR C 2 126 ? 114.727 106.396 123.311 1.00 23.17 ?  105 TYR C O     1 
ATOM   11827 C  CB    . TYR C 2 126 ? 115.939 103.502 122.777 1.00 23.45 ?  105 TYR C CB    1 
ATOM   11828 C  CG    . TYR C 2 126 ? 116.467 102.496 121.781 1.00 25.16 ?  105 TYR C CG    1 
ATOM   11829 C  CD1   . TYR C 2 126 ? 116.170 102.597 120.425 1.00 26.75 ?  105 TYR C CD1   1 
ATOM   11830 C  CD2   . TYR C 2 126 ? 117.269 101.437 122.207 1.00 26.36 ?  105 TYR C CD2   1 
ATOM   11831 C  CE1   . TYR C 2 126 ? 116.676 101.668 119.508 1.00 28.22 ?  105 TYR C CE1   1 
ATOM   11832 C  CE2   . TYR C 2 126 ? 117.776 100.512 121.307 1.00 27.17 ?  105 TYR C CE2   1 
ATOM   11833 C  CZ    . TYR C 2 126 ? 117.466 100.624 119.965 1.00 29.26 ?  105 TYR C CZ    1 
ATOM   11834 O  OH    . TYR C 2 126 ? 117.961 99.692  119.073 1.00 30.76 ?  105 TYR C OH    1 
ATOM   11835 N  N     . SER C 2 127 ? 116.475 106.032 124.692 1.00 23.61 ?  106 SER C N     1 
ATOM   11836 C  CA    . SER C 2 127 ? 116.024 106.968 125.714 1.00 24.40 ?  106 SER C CA    1 
ATOM   11837 C  C     . SER C 2 127 ? 116.117 108.408 125.229 1.00 24.55 ?  106 SER C C     1 
ATOM   11838 O  O     . SER C 2 127 ? 115.291 109.226 125.604 1.00 24.74 ?  106 SER C O     1 
ATOM   11839 C  CB    . SER C 2 127 ? 116.789 106.797 127.026 1.00 24.54 ?  106 SER C CB    1 
ATOM   11840 O  OG    . SER C 2 127 ? 116.321 105.660 127.742 1.00 24.69 ?  106 SER C OG    1 
ATOM   11841 N  N     . ASN C 2 128 ? 117.122 108.714 124.408 1.00 25.28 ?  107 ASN C N     1 
ATOM   11842 C  CA    . ASN C 2 128 ? 117.230 110.044 123.800 1.00 25.88 ?  107 ASN C CA    1 
ATOM   11843 C  C     . ASN C 2 128 ? 116.021 110.301 122.909 1.00 25.48 ?  107 ASN C C     1 
ATOM   11844 O  O     . ASN C 2 128 ? 115.424 111.375 122.952 1.00 25.23 ?  107 ASN C O     1 
ATOM   11845 C  CB    . ASN C 2 128 ? 118.522 110.197 122.988 1.00 26.40 ?  107 ASN C CB    1 
ATOM   11846 C  CG    . ASN C 2 128 ? 119.753 110.414 123.859 1.00 27.90 ?  107 ASN C CG    1 
ATOM   11847 O  OD1   . ASN C 2 128 ? 119.834 109.923 124.987 1.00 30.62 ?  107 ASN C OD1   1 
ATOM   11848 N  ND2   . ASN C 2 128 ? 120.728 111.142 123.325 1.00 27.91 ?  107 ASN C ND2   1 
ATOM   11849 N  N     . ILE C 2 129 ? 115.661 109.301 122.112 1.00 25.44 ?  108 ILE C N     1 
ATOM   11850 C  CA    . ILE C 2 129 ? 114.469 109.403 121.269 1.00 25.48 ?  108 ILE C CA    1 
ATOM   11851 C  C     . ILE C 2 129 ? 113.208 109.565 122.134 1.00 25.93 ?  108 ILE C C     1 
ATOM   11852 O  O     . ILE C 2 129 ? 112.432 110.501 121.915 1.00 25.54 ?  108 ILE C O     1 
ATOM   11853 C  CB    . ILE C 2 129 ? 114.359 108.236 120.254 1.00 25.21 ?  108 ILE C CB    1 
ATOM   11854 C  CG1   . ILE C 2 129 ? 115.568 108.259 119.303 1.00 25.96 ?  108 ILE C CG1   1 
ATOM   11855 C  CG2   . ILE C 2 129 ? 113.032 108.318 119.470 1.00 24.43 ?  108 ILE C CG2   1 
ATOM   11856 C  CD1   . ILE C 2 129 ? 115.738 107.014 118.433 1.00 26.11 ?  108 ILE C CD1   1 
ATOM   11857 N  N     . PHE C 2 130 ? 113.018 108.679 123.117 1.00 26.04 ?  109 PHE C N     1 
ATOM   11858 C  CA    . PHE C 2 130 ? 111.854 108.757 124.019 1.00 26.66 ?  109 PHE C CA    1 
ATOM   11859 C  C     . PHE C 2 130 ? 111.738 110.119 124.710 1.00 27.38 ?  109 PHE C C     1 
ATOM   11860 O  O     . PHE C 2 130 ? 110.643 110.701 124.781 1.00 27.22 ?  109 PHE C O     1 
ATOM   11861 C  CB    . PHE C 2 130 ? 111.907 107.663 125.108 1.00 26.98 ?  109 PHE C CB    1 
ATOM   11862 C  CG    . PHE C 2 130 ? 111.661 106.261 124.609 1.00 27.46 ?  109 PHE C CG    1 
ATOM   11863 C  CD1   . PHE C 2 130 ? 110.864 106.018 123.496 1.00 28.57 ?  109 PHE C CD1   1 
ATOM   11864 C  CD2   . PHE C 2 130 ? 112.222 105.173 125.278 1.00 28.51 ?  109 PHE C CD2   1 
ATOM   11865 C  CE1   . PHE C 2 130 ? 110.644 104.717 123.045 1.00 29.17 ?  109 PHE C CE1   1 
ATOM   11866 C  CE2   . PHE C 2 130 ? 112.001 103.860 124.839 1.00 29.27 ?  109 PHE C CE2   1 
ATOM   11867 C  CZ    . PHE C 2 130 ? 111.209 103.629 123.725 1.00 28.83 ?  109 PHE C CZ    1 
ATOM   11868 N  N     . MET C 2 131 ? 112.861 110.629 125.217 1.00 27.52 ?  110 MET C N     1 
ATOM   11869 C  CA    . MET C 2 131 ? 112.850 111.877 125.989 1.00 29.07 ?  110 MET C CA    1 
ATOM   11870 C  C     . MET C 2 131 ? 112.514 113.098 125.151 1.00 29.58 ?  110 MET C C     1 
ATOM   11871 O  O     . MET C 2 131 ? 111.997 114.087 125.671 1.00 30.07 ?  110 MET C O     1 
ATOM   11872 C  CB    . MET C 2 131 ? 114.169 112.093 126.726 1.00 28.96 ?  110 MET C CB    1 
ATOM   11873 C  CG    . MET C 2 131 ? 114.274 111.289 128.005 1.00 31.09 ?  110 MET C CG    1 
ATOM   11874 S  SD    . MET C 2 131 ? 115.850 111.491 128.870 1.00 35.43 ?  110 MET C SD    1 
ATOM   11875 C  CE    . MET C 2 131 ? 117.009 110.747 127.726 1.00 33.13 ?  110 MET C CE    1 
ATOM   11876 N  N     . THR C 2 132 ? 112.805 113.016 123.859 1.00 30.25 ?  111 THR C N     1 
ATOM   11877 C  CA    . THR C 2 132 ? 112.459 114.067 122.906 1.00 30.97 ?  111 THR C CA    1 
ATOM   11878 C  C     . THR C 2 132 ? 110.969 114.042 122.552 1.00 31.36 ?  111 THR C C     1 
ATOM   11879 O  O     . THR C 2 132 ? 110.274 115.063 122.656 1.00 31.60 ?  111 THR C O     1 
ATOM   11880 C  CB    . THR C 2 132 ? 113.326 113.937 121.621 1.00 30.88 ?  111 THR C CB    1 
ATOM   11881 O  OG1   . THR C 2 132 ? 114.704 114.106 121.968 1.00 29.86 ?  111 THR C OG1   1 
ATOM   11882 C  CG2   . THR C 2 132 ? 112.945 114.986 120.566 1.00 31.44 ?  111 THR C CG2   1 
ATOM   11883 N  N     . LEU C 2 133 ? 110.483 112.872 122.149 1.00 31.34 ?  112 LEU C N     1 
ATOM   11884 C  CA    . LEU C 2 133 ? 109.141 112.743 121.579 1.00 31.68 ?  112 LEU C CA    1 
ATOM   11885 C  C     . LEU C 2 133 ? 107.993 112.582 122.579 1.00 31.96 ?  112 LEU C C     1 
ATOM   11886 O  O     . LEU C 2 133 ? 106.873 113.016 122.313 1.00 31.69 ?  112 LEU C O     1 
ATOM   11887 C  CB    . LEU C 2 133 ? 109.108 111.584 120.587 1.00 31.35 ?  112 LEU C CB    1 
ATOM   11888 C  CG    . LEU C 2 133 ? 110.162 111.578 119.475 1.00 32.14 ?  112 LEU C CG    1 
ATOM   11889 C  CD1   . LEU C 2 133 ? 110.006 110.323 118.650 1.00 32.15 ?  112 LEU C CD1   1 
ATOM   11890 C  CD2   . LEU C 2 133 ? 110.058 112.828 118.603 1.00 32.39 ?  112 LEU C CD2   1 
ATOM   11891 N  N     . ALA C 2 134 ? 108.269 111.959 123.721 1.00 32.12 ?  113 ALA C N     1 
ATOM   11892 C  CA    . ALA C 2 134 ? 107.205 111.525 124.616 1.00 32.53 ?  113 ALA C CA    1 
ATOM   11893 C  C     . ALA C 2 134 ? 107.276 112.155 126.001 1.00 33.15 ?  113 ALA C C     1 
ATOM   11894 O  O     . ALA C 2 134 ? 108.365 112.420 126.505 1.00 32.47 ?  113 ALA C O     1 
ATOM   11895 C  CB    . ALA C 2 134 ? 107.199 109.995 124.725 1.00 32.20 ?  113 ALA C CB    1 
ATOM   11896 N  N     . PRO C 2 135 ? 106.103 112.380 126.627 1.00 34.27 ?  114 PRO C N     1 
ATOM   11897 C  CA    . PRO C 2 135 ? 106.070 112.827 128.014 1.00 35.35 ?  114 PRO C CA    1 
ATOM   11898 C  C     . PRO C 2 135 ? 106.448 111.686 128.952 1.00 36.17 ?  114 PRO C C     1 
ATOM   11899 O  O     . PRO C 2 135 ? 106.299 110.515 128.593 1.00 35.92 ?  114 PRO C O     1 
ATOM   11900 C  CB    . PRO C 2 135 ? 104.612 113.258 128.219 1.00 35.48 ?  114 PRO C CB    1 
ATOM   11901 C  CG    . PRO C 2 135 ? 103.833 112.521 127.200 1.00 34.94 ?  114 PRO C CG    1 
ATOM   11902 C  CD    . PRO C 2 135 ? 104.752 112.212 126.056 1.00 34.50 ?  114 PRO C CD    1 
ATOM   11903 N  N     . THR C 2 136 ? 106.944 112.035 130.134 1.00 37.30 ?  115 THR C N     1 
ATOM   11904 C  CA    . THR C 2 136 ? 107.457 111.064 131.106 1.00 38.49 ?  115 THR C CA    1 
ATOM   11905 C  C     . THR C 2 136 ? 106.516 109.888 131.408 1.00 38.48 ?  115 THR C C     1 
ATOM   11906 O  O     . THR C 2 136 ? 106.981 108.754 131.567 1.00 38.74 ?  115 THR C O     1 
ATOM   11907 C  CB    . THR C 2 136 ? 107.847 111.764 132.423 1.00 38.95 ?  115 THR C CB    1 
ATOM   11908 O  OG1   . THR C 2 136 ? 108.720 112.858 132.126 1.00 40.08 ?  115 THR C OG1   1 
ATOM   11909 C  CG2   . THR C 2 136 ? 108.555 110.803 133.380 1.00 39.82 ?  115 THR C CG2   1 
ATOM   11910 N  N     . GLU C 2 137 ? 105.212 110.160 131.481 1.00 38.89 ?  116 GLU C N     1 
ATOM   11911 C  CA    . GLU C 2 137 ? 104.217 109.134 131.824 1.00 38.65 ?  116 GLU C CA    1 
ATOM   11912 C  C     . GLU C 2 137 ? 104.110 108.062 130.745 1.00 37.38 ?  116 GLU C C     1 
ATOM   11913 O  O     . GLU C 2 137 ? 103.953 106.881 131.050 1.00 37.22 ?  116 GLU C O     1 
ATOM   11914 C  CB    . GLU C 2 137 ? 102.832 109.741 132.138 1.00 39.52 ?  116 GLU C CB    1 
ATOM   11915 C  CG    . GLU C 2 137 ? 102.054 110.339 130.943 1.00 41.90 ?  116 GLU C CG    1 
ATOM   11916 C  CD    . GLU C 2 137 ? 101.732 111.836 131.089 1.00 46.43 ?  116 GLU C CD    1 
ATOM   11917 O  OE1   . GLU C 2 137 ? 102.286 112.503 131.996 1.00 47.84 ?  116 GLU C OE1   1 
ATOM   11918 O  OE2   . GLU C 2 137 ? 100.914 112.347 130.286 1.00 47.52 -1 116 GLU C OE2   1 
ATOM   11919 N  N     . THR C 2 138 ? 104.209 108.487 129.489 1.00 36.05 ?  117 THR C N     1 
ATOM   11920 C  CA    . THR C 2 138 ? 104.183 107.575 128.356 1.00 34.88 ?  117 THR C CA    1 
ATOM   11921 C  C     . THR C 2 138 ? 105.462 106.745 128.332 1.00 33.58 ?  117 THR C C     1 
ATOM   11922 O  O     . THR C 2 138 ? 105.424 105.554 128.012 1.00 33.61 ?  117 THR C O     1 
ATOM   11923 C  CB    . THR C 2 138 ? 104.007 108.332 127.033 1.00 34.85 ?  117 THR C CB    1 
ATOM   11924 O  OG1   . THR C 2 138 ? 102.876 109.204 127.142 1.00 35.98 ?  117 THR C OG1   1 
ATOM   11925 C  CG2   . THR C 2 138 ? 103.784 107.367 125.878 1.00 34.92 ?  117 THR C CG2   1 
ATOM   11926 N  N     . ILE C 2 139 ? 106.583 107.378 128.676 1.00 32.29 ?  118 ILE C N     1 
ATOM   11927 C  CA    . ILE C 2 139 ? 107.859 106.674 128.802 1.00 31.19 ?  118 ILE C CA    1 
ATOM   11928 C  C     . ILE C 2 139 ? 107.791 105.626 129.928 1.00 30.85 ?  118 ILE C C     1 
ATOM   11929 O  O     . ILE C 2 139 ? 108.152 104.468 129.715 1.00 29.77 ?  118 ILE C O     1 
ATOM   11930 C  CB    . ILE C 2 139 ? 109.064 107.643 129.001 1.00 31.25 ?  118 ILE C CB    1 
ATOM   11931 C  CG1   . ILE C 2 139 ? 109.176 108.638 127.834 1.00 30.12 ?  118 ILE C CG1   1 
ATOM   11932 C  CG2   . ILE C 2 139 ? 110.378 106.861 129.155 1.00 30.21 ?  118 ILE C CG2   1 
ATOM   11933 C  CD1   . ILE C 2 139 ? 110.253 109.720 128.038 1.00 29.41 ?  118 ILE C CD1   1 
ATOM   11934 N  N     . ASN C 2 140 ? 107.311 106.033 131.109 1.00 31.17 ?  119 ASN C N     1 
ATOM   11935 C  CA    . ASN C 2 140 ? 107.137 105.111 132.243 1.00 31.76 ?  119 ASN C CA    1 
ATOM   11936 C  C     . ASN C 2 140 ? 106.251 103.913 131.883 1.00 31.25 ?  119 ASN C C     1 
ATOM   11937 O  O     . ASN C 2 140 ? 106.592 102.771 132.191 1.00 31.47 ?  119 ASN C O     1 
ATOM   11938 C  CB    . ASN C 2 140 ? 106.544 105.823 133.469 1.00 32.65 ?  119 ASN C CB    1 
ATOM   11939 C  CG    . ASN C 2 140 ? 107.522 106.778 134.146 1.00 35.14 ?  119 ASN C CG    1 
ATOM   11940 O  OD1   . ASN C 2 140 ? 108.745 106.613 134.076 1.00 36.75 ?  119 ASN C OD1   1 
ATOM   11941 N  ND2   . ASN C 2 140 ? 106.971 107.780 134.837 1.00 38.05 ?  119 ASN C ND2   1 
ATOM   11942 N  N     . GLU C 2 141 ? 105.129 104.193 131.222 1.00 30.96 ?  120 GLU C N     1 
ATOM   11943 C  CA    . GLU C 2 141 ? 104.174 103.170 130.798 1.00 30.36 ?  120 GLU C CA    1 
ATOM   11944 C  C     . GLU C 2 141 ? 104.786 102.160 129.824 1.00 28.60 ?  120 GLU C C     1 
ATOM   11945 O  O     . GLU C 2 141 ? 104.546 100.962 129.952 1.00 27.94 ?  120 GLU C O     1 
ATOM   11946 C  CB    . GLU C 2 141 ? 102.936 103.813 130.167 1.00 30.86 ?  120 GLU C CB    1 
ATOM   11947 C  CG    . GLU C 2 141 ? 101.953 104.415 131.165 1.00 34.89 ?  120 GLU C CG    1 
ATOM   11948 C  CD    . GLU C 2 141 ? 100.846 105.212 130.488 1.00 39.82 ?  120 GLU C CD    1 
ATOM   11949 O  OE1   . GLU C 2 141 ? 100.670 105.082 129.251 1.00 41.95 ?  120 GLU C OE1   1 
ATOM   11950 O  OE2   . GLU C 2 141 ? 100.144 105.967 131.192 1.00 41.94 -1 120 GLU C OE2   1 
ATOM   11951 N  N     . VAL C 2 142 ? 105.567 102.631 128.855 1.00 27.29 ?  121 VAL C N     1 
ATOM   11952 C  CA    . VAL C 2 142 ? 106.156 101.691 127.877 1.00 25.89 ?  121 VAL C CA    1 
ATOM   11953 C  C     . VAL C 2 142 ? 107.212 100.774 128.506 1.00 25.11 ?  121 VAL C C     1 
ATOM   11954 O  O     . VAL C 2 142 ? 107.338 99.612  128.121 1.00 24.23 ?  121 VAL C O     1 
ATOM   11955 C  CB    . VAL C 2 142 ? 106.654 102.381 126.560 1.00 25.99 ?  121 VAL C CB    1 
ATOM   11956 C  CG1   . VAL C 2 142 ? 108.078 102.929 126.687 1.00 25.21 ?  121 VAL C CG1   1 
ATOM   11957 C  CG2   . VAL C 2 142 ? 106.583 101.406 125.396 1.00 25.78 ?  121 VAL C CG2   1 
ATOM   11958 N  N     . PHE C 2 143 ? 107.959 101.279 129.483 1.00 24.69 ?  122 PHE C N     1 
ATOM   11959 C  CA    . PHE C 2 143 ? 108.922 100.422 130.191 1.00 24.77 ?  122 PHE C CA    1 
ATOM   11960 C  C     . PHE C 2 143 ? 108.214 99.411  131.109 1.00 24.99 ?  122 PHE C C     1 
ATOM   11961 O  O     . PHE C 2 143 ? 108.674 98.280  131.275 1.00 24.73 ?  122 PHE C O     1 
ATOM   11962 C  CB    . PHE C 2 143 ? 109.987 101.249 130.923 1.00 24.83 ?  122 PHE C CB    1 
ATOM   11963 C  CG    . PHE C 2 143 ? 111.064 101.780 130.001 1.00 25.12 ?  122 PHE C CG    1 
ATOM   11964 C  CD1   . PHE C 2 143 ? 112.030 100.927 129.472 1.00 26.58 ?  122 PHE C CD1   1 
ATOM   11965 C  CD2   . PHE C 2 143 ? 111.098 103.120 129.648 1.00 24.49 ?  122 PHE C CD2   1 
ATOM   11966 C  CE1   . PHE C 2 143 ? 113.019 101.412 128.606 1.00 26.96 ?  122 PHE C CE1   1 
ATOM   11967 C  CE2   . PHE C 2 143 ? 112.074 103.612 128.793 1.00 25.79 ?  122 PHE C CE2   1 
ATOM   11968 C  CZ    . PHE C 2 143 ? 113.039 102.759 128.266 1.00 26.45 ?  122 PHE C CZ    1 
ATOM   11969 N  N     . GLU C 2 144 ? 107.083 99.813  131.683 1.00 25.22 ?  123 GLU C N     1 
ATOM   11970 C  CA    . GLU C 2 144 ? 106.227 98.869  132.408 1.00 25.72 ?  123 GLU C CA    1 
ATOM   11971 C  C     . GLU C 2 144 ? 105.665 97.811  131.460 1.00 25.08 ?  123 GLU C C     1 
ATOM   11972 O  O     . GLU C 2 144 ? 105.603 96.630  131.803 1.00 24.67 ?  123 GLU C O     1 
ATOM   11973 C  CB    . GLU C 2 144 ? 105.110 99.598  133.149 1.00 26.23 ?  123 GLU C CB    1 
ATOM   11974 C  CG    . GLU C 2 144 ? 105.616 100.375 134.353 1.00 29.96 ?  123 GLU C CG    1 
ATOM   11975 C  CD    . GLU C 2 144 ? 106.432 99.506  135.295 1.00 33.82 ?  123 GLU C CD    1 
ATOM   11976 O  OE1   . GLU C 2 144 ? 105.852 98.573  135.891 1.00 36.54 ?  123 GLU C OE1   1 
ATOM   11977 O  OE2   . GLU C 2 144 ? 107.652 99.741  135.427 1.00 35.84 -1 123 GLU C OE2   1 
ATOM   11978 N  N     . TRP C 2 145 ? 105.287 98.243  130.260 1.00 24.21 ?  124 TRP C N     1 
ATOM   11979 C  CA    . TRP C 2 145 ? 104.783 97.338  129.227 1.00 23.99 ?  124 TRP C CA    1 
ATOM   11980 C  C     . TRP C 2 145 ? 105.802 96.275  128.792 1.00 23.95 ?  124 TRP C C     1 
ATOM   11981 O  O     . TRP C 2 145 ? 105.416 95.116  128.549 1.00 23.31 ?  124 TRP C O     1 
ATOM   11982 C  CB    . TRP C 2 145 ? 104.269 98.129  128.014 1.00 24.13 ?  124 TRP C CB    1 
ATOM   11983 C  CG    . TRP C 2 145 ? 104.009 97.269  126.799 1.00 24.37 ?  124 TRP C CG    1 
ATOM   11984 C  CD1   . TRP C 2 145 ? 102.843 96.616  126.476 1.00 24.76 ?  124 TRP C CD1   1 
ATOM   11985 C  CD2   . TRP C 2 145 ? 104.938 96.977  125.747 1.00 23.31 ?  124 TRP C CD2   1 
ATOM   11986 N  NE1   . TRP C 2 145 ? 103.002 95.929  125.287 1.00 24.97 ?  124 TRP C NE1   1 
ATOM   11987 C  CE2   . TRP C 2 145 ? 104.274 96.136  124.819 1.00 24.20 ?  124 TRP C CE2   1 
ATOM   11988 C  CE3   . TRP C 2 145 ? 106.271 97.333  125.502 1.00 23.76 ?  124 TRP C CE3   1 
ATOM   11989 C  CZ2   . TRP C 2 145 ? 104.901 95.652  123.663 1.00 23.41 ?  124 TRP C CZ2   1 
ATOM   11990 C  CZ3   . TRP C 2 145 ? 106.896 96.849  124.354 1.00 23.29 ?  124 TRP C CZ3   1 
ATOM   11991 C  CH2   . TRP C 2 145 ? 106.204 96.022  123.446 1.00 22.93 ?  124 TRP C CH2   1 
ATOM   11992 N  N     . VAL C 2 146 ? 107.084 96.635  128.677 1.00 23.35 ?  125 VAL C N     1 
ATOM   11993 C  CA    . VAL C 2 146 ? 108.083 95.583  128.352 1.00 23.53 ?  125 VAL C CA    1 
ATOM   11994 C  C     . VAL C 2 146 ? 108.142 94.485  129.421 1.00 23.73 ?  125 VAL C C     1 
ATOM   11995 O  O     . VAL C 2 146 ? 108.218 93.314  129.081 1.00 23.03 ?  125 VAL C O     1 
ATOM   11996 C  CB    . VAL C 2 146 ? 109.518 96.086  127.854 1.00 23.63 ?  125 VAL C CB    1 
ATOM   11997 C  CG1   . VAL C 2 146 ? 109.616 97.577  127.675 1.00 24.40 ?  125 VAL C CG1   1 
ATOM   11998 C  CG2   . VAL C 2 146 ? 110.698 95.510  128.660 1.00 22.97 ?  125 VAL C CG2   1 
ATOM   11999 N  N     . LYS C 2 147 ? 108.047 94.870  130.697 1.00 24.06 ?  126 LYS C N     1 
ATOM   12000 C  CA    . LYS C 2 147 ? 108.122 93.903  131.806 1.00 25.41 ?  126 LYS C CA    1 
ATOM   12001 C  C     . LYS C 2 147 ? 107.007 92.855  131.779 1.00 25.82 ?  126 LYS C C     1 
ATOM   12002 O  O     . LYS C 2 147 ? 107.223 91.714  132.193 1.00 26.08 ?  126 LYS C O     1 
ATOM   12003 C  CB    . LYS C 2 147 ? 108.092 94.618  133.159 1.00 25.49 ?  126 LYS C CB    1 
ATOM   12004 C  CG    . LYS C 2 147 ? 109.317 95.453  133.476 1.00 27.52 ?  126 LYS C CG    1 
ATOM   12005 C  CD    . LYS C 2 147 ? 109.105 96.168  134.804 1.00 30.43 ?  126 LYS C CD    1 
ATOM   12006 C  CE    . LYS C 2 147 ? 110.119 97.273  135.014 1.00 33.10 ?  126 LYS C CE    1 
ATOM   12007 N  NZ    . LYS C 2 147 ? 109.807 98.025  136.261 1.00 34.86 1  126 LYS C NZ    1 
ATOM   12008 N  N     . GLN C 2 148 ? 105.827 93.245  131.296 1.00 26.45 ?  127 GLN C N     1 
ATOM   12009 C  CA    . GLN C 2 148 ? 104.647 92.378  131.335 1.00 26.85 ?  127 GLN C CA    1 
ATOM   12010 C  C     . GLN C 2 148 ? 104.274 91.749  129.991 1.00 26.01 ?  127 GLN C C     1 
ATOM   12011 O  O     . GLN C 2 148 ? 103.365 90.918  129.934 1.00 26.12 ?  127 GLN C O     1 
ATOM   12012 C  CB    . GLN C 2 148 ? 103.437 93.117  131.938 1.00 28.08 ?  127 GLN C CB    1 
ATOM   12013 C  CG    . GLN C 2 148 ? 102.955 94.338  131.149 1.00 30.69 ?  127 GLN C CG    1 
ATOM   12014 C  CD    . GLN C 2 148 ? 102.182 93.974  129.883 1.00 34.64 ?  127 GLN C CD    1 
ATOM   12015 O  OE1   . GLN C 2 148 ? 102.632 94.255  128.758 1.00 33.80 ?  127 GLN C OE1   1 
ATOM   12016 N  NE2   . GLN C 2 148 ? 101.018 93.336  130.057 1.00 36.24 ?  127 GLN C NE2   1 
ATOM   12017 N  N     . ASN C 2 149 ? 104.961 92.145  128.916 1.00 24.97 ?  128 ASN C N     1 
ATOM   12018 C  CA    . ASN C 2 149 ? 104.687 91.599  127.590 1.00 24.03 ?  128 ASN C CA    1 
ATOM   12019 C  C     . ASN C 2 149 ? 105.251 90.193  127.460 1.00 24.13 ?  128 ASN C C     1 
ATOM   12020 O  O     . ASN C 2 149 ? 106.465 90.011  127.587 1.00 22.93 ?  128 ASN C O     1 
ATOM   12021 C  CB    . ASN C 2 149 ? 105.303 92.478  126.514 1.00 23.97 ?  128 ASN C CB    1 
ATOM   12022 C  CG    . ASN C 2 149 ? 104.927 92.029  125.122 1.00 23.94 ?  128 ASN C CG    1 
ATOM   12023 O  OD1   . ASN C 2 149 ? 105.610 91.203  124.519 1.00 24.85 ?  128 ASN C OD1   1 
ATOM   12024 N  ND2   . ASN C 2 149 ? 103.807 92.532  124.622 1.00 24.76 ?  128 ASN C ND2   1 
ATOM   12025 N  N     . LYS C 2 150 ? 104.387 89.215  127.179 1.00 24.32 ?  129 LYS C N     1 
ATOM   12026 C  CA    . LYS C 2 150 ? 104.793 87.797  127.232 1.00 24.77 ?  129 LYS C CA    1 
ATOM   12027 C  C     . LYS C 2 150 ? 105.769 87.351  126.140 1.00 24.54 ?  129 LYS C C     1 
ATOM   12028 O  O     . LYS C 2 150 ? 106.603 86.476  126.379 1.00 24.17 ?  129 LYS C O     1 
ATOM   12029 C  CB    . LYS C 2 150 ? 103.581 86.860  127.309 1.00 25.27 ?  129 LYS C CB    1 
ATOM   12030 C  CG    . LYS C 2 150 ? 102.640 86.901  126.123 1.00 28.72 ?  129 LYS C CG    1 
ATOM   12031 C  CD    . LYS C 2 150 ? 101.697 85.697  126.169 1.00 33.40 ?  129 LYS C CD    1 
ATOM   12032 C  CE    . LYS C 2 150 ? 100.441 85.948  125.357 1.00 36.77 ?  129 LYS C CE    1 
ATOM   12033 N  NZ    . LYS C 2 150 ? 99.446  84.856  125.592 1.00 39.66 1  129 LYS C NZ    1 
ATOM   12034 N  N     . TYR C 2 151 ? 105.661 87.949  124.949 1.00 23.92 ?  130 TYR C N     1 
ATOM   12035 C  CA    . TYR C 2 151 ? 106.558 87.617  123.834 1.00 24.12 ?  130 TYR C CA    1 
ATOM   12036 C  C     . TYR C 2 151 ? 107.961 88.166  124.040 1.00 23.54 ?  130 TYR C C     1 
ATOM   12037 O  O     . TYR C 2 151 ? 108.957 87.501  123.719 1.00 23.32 ?  130 TYR C O     1 
ATOM   12038 C  CB    . TYR C 2 151 ? 105.962 88.106  122.500 1.00 24.53 ?  130 TYR C CB    1 
ATOM   12039 C  CG    . TYR C 2 151 ? 104.486 87.789  122.382 1.00 25.83 ?  130 TYR C CG    1 
ATOM   12040 C  CD1   . TYR C 2 151 ? 104.043 86.467  122.342 1.00 26.57 ?  130 TYR C CD1   1 
ATOM   12041 C  CD2   . TYR C 2 151 ? 103.532 88.812  122.356 1.00 27.87 ?  130 TYR C CD2   1 
ATOM   12042 C  CE1   . TYR C 2 151 ? 102.688 86.162  122.255 1.00 29.65 ?  130 TYR C CE1   1 
ATOM   12043 C  CE2   . TYR C 2 151 ? 102.165 88.517  122.273 1.00 29.91 ?  130 TYR C CE2   1 
ATOM   12044 C  CZ    . TYR C 2 151 ? 101.756 87.191  122.225 1.00 31.19 ?  130 TYR C CZ    1 
ATOM   12045 O  OH    . TYR C 2 151 ? 100.414 86.881  122.142 1.00 34.44 ?  130 TYR C OH    1 
ATOM   12046 N  N     . LEU C 2 152 ? 108.034 89.380  124.576 1.00 23.38 ?  131 LEU C N     1 
ATOM   12047 C  CA    . LEU C 2 152 ? 109.304 90.018  124.870 1.00 23.43 ?  131 LEU C CA    1 
ATOM   12048 C  C     . LEU C 2 152 ? 109.993 89.299  126.034 1.00 23.37 ?  131 LEU C C     1 
ATOM   12049 O  O     . LEU C 2 152 ? 111.203 89.059  125.988 1.00 23.05 ?  131 LEU C O     1 
ATOM   12050 C  CB    . LEU C 2 152 ? 109.061 91.492  125.188 1.00 23.73 ?  131 LEU C CB    1 
ATOM   12051 C  CG    . LEU C 2 152 ? 109.884 92.650  124.637 1.00 24.71 ?  131 LEU C CG    1 
ATOM   12052 C  CD1   . LEU C 2 152 ? 110.708 92.331  123.378 1.00 21.63 ?  131 LEU C CD1   1 
ATOM   12053 C  CD2   . LEU C 2 152 ? 108.960 93.819  124.385 1.00 26.87 ?  131 LEU C CD2   1 
ATOM   12054 N  N     . GLN C 2 153 ? 109.232 88.953  127.077 1.00 22.80 ?  132 GLN C N     1 
ATOM   12055 C  CA    . GLN C 2 153 ? 109.791 88.132  128.162 1.00 22.70 ?  132 GLN C CA    1 
ATOM   12056 C  C     . GLN C 2 153 ? 110.257 86.750  127.695 1.00 22.54 ?  132 GLN C C     1 
ATOM   12057 O  O     . GLN C 2 153 ? 111.348 86.302  128.080 1.00 21.73 ?  132 GLN C O     1 
ATOM   12058 C  CB    . GLN C 2 153 ? 108.841 88.030  129.359 1.00 23.07 ?  132 GLN C CB    1 
ATOM   12059 C  CG    . GLN C 2 153 ? 108.592 89.378  130.034 1.00 21.83 ?  132 GLN C CG    1 
ATOM   12060 C  CD    . GLN C 2 153 ? 109.872 90.053  130.535 1.00 22.34 ?  132 GLN C CD    1 
ATOM   12061 O  OE1   . GLN C 2 153 ? 110.707 89.427  131.193 1.00 24.07 ?  132 GLN C OE1   1 
ATOM   12062 N  NE2   . GLN C 2 153 ? 110.018 91.337  130.235 1.00 22.26 ?  132 GLN C NE2   1 
ATOM   12063 N  N     . LYS C 2 154 ? 109.451 86.083  126.865 1.00 22.53 ?  133 LYS C N     1 
ATOM   12064 C  CA    . LYS C 2 154 ? 109.855 84.784  126.328 1.00 22.84 ?  133 LYS C CA    1 
ATOM   12065 C  C     . LYS C 2 154 ? 111.159 84.869  125.532 1.00 22.42 ?  133 LYS C C     1 
ATOM   12066 O  O     . LYS C 2 154 ? 112.039 84.037  125.723 1.00 21.90 ?  133 LYS C O     1 
ATOM   12067 C  CB    . LYS C 2 154 ? 108.739 84.101  125.502 1.00 22.96 ?  133 LYS C CB    1 
ATOM   12068 C  CG    . LYS C 2 154 ? 109.122 82.693  124.951 1.00 23.45 ?  133 LYS C CG    1 
ATOM   12069 C  CD    . LYS C 2 154 ? 109.362 81.644  126.059 1.00 26.74 ?  133 LYS C CD    1 
ATOM   12070 C  CE    . LYS C 2 154 ? 109.691 80.266  125.468 1.00 27.93 ?  133 LYS C CE    1 
ATOM   12071 N  NZ    . LYS C 2 154 ? 110.130 79.274  126.487 1.00 27.86 1  133 LYS C NZ    1 
ATOM   12072 N  N     . LYS C 2 155 ? 111.302 85.874  124.662 1.00 22.77 ?  134 LYS C N     1 
ATOM   12073 C  CA    . LYS C 2 155 ? 112.501 85.934  123.820 1.00 22.87 ?  134 LYS C CA    1 
ATOM   12074 C  C     . LYS C 2 155 ? 113.750 86.247  124.638 1.00 22.30 ?  134 LYS C C     1 
ATOM   12075 O  O     . LYS C 2 155 ? 114.804 85.629  124.415 1.00 21.89 ?  134 LYS C O     1 
ATOM   12076 C  CB    . LYS C 2 155 ? 112.334 86.843  122.580 1.00 23.33 ?  134 LYS C CB    1 
ATOM   12077 C  CG    . LYS C 2 155 ? 112.393 88.334  122.801 1.00 24.25 ?  134 LYS C CG    1 
ATOM   12078 C  CD    . LYS C 2 155 ? 112.226 89.098  121.476 1.00 26.87 ?  134 LYS C CD    1 
ATOM   12079 C  CE    . LYS C 2 155 ? 110.754 89.295  121.132 1.00 28.26 ?  134 LYS C CE    1 
ATOM   12080 N  NZ    . LYS C 2 155 ? 110.606 90.298  120.033 1.00 28.97 1  134 LYS C NZ    1 
ATOM   12081 N  N     . ALA C 2 156 ? 113.615 87.156  125.604 1.00 21.96 ?  135 ALA C N     1 
ATOM   12082 C  CA    . ALA C 2 156 ? 114.682 87.416  126.590 1.00 22.43 ?  135 ALA C CA    1 
ATOM   12083 C  C     . ALA C 2 156 ? 115.040 86.180  127.416 1.00 22.02 ?  135 ALA C C     1 
ATOM   12084 O  O     . ALA C 2 156 ? 116.217 85.904  127.631 1.00 22.60 ?  135 ALA C O     1 
ATOM   12085 C  CB    . ALA C 2 156 ? 114.304 88.580  127.531 1.00 22.05 ?  135 ALA C CB    1 
ATOM   12086 N  N     . GLN C 2 157 ? 114.030 85.452  127.894 1.00 21.97 ?  136 GLN C N     1 
ATOM   12087 C  CA    . GLN C 2 157 ? 114.265 84.225  128.667 1.00 22.10 ?  136 GLN C CA    1 
ATOM   12088 C  C     . GLN C 2 157 ? 115.100 83.235  127.879 1.00 21.87 ?  136 GLN C C     1 
ATOM   12089 O  O     . GLN C 2 157 ? 116.030 82.639  128.421 1.00 21.75 ?  136 GLN C O     1 
ATOM   12090 C  CB    . GLN C 2 157 ? 112.954 83.534  129.038 1.00 22.50 ?  136 GLN C CB    1 
ATOM   12091 C  CG    . GLN C 2 157 ? 112.227 84.130  130.234 1.00 23.55 ?  136 GLN C CG    1 
ATOM   12092 C  CD    . GLN C 2 157 ? 110.773 83.692  130.255 1.00 26.93 ?  136 GLN C CD    1 
ATOM   12093 O  OE1   . GLN C 2 157 ? 110.428 82.658  129.687 1.00 26.36 ?  136 GLN C OE1   1 
ATOM   12094 N  NE2   . GLN C 2 157 ? 109.914 84.487  130.883 1.00 28.09 ?  136 GLN C NE2   1 
ATOM   12095 N  N     . MET C 2 158 ? 114.745 83.058  126.608 1.00 21.38 ?  137 MET C N     1 
ATOM   12096 C  CA    . MET C 2 158 ? 115.392 82.077  125.750 1.00 22.08 ?  137 MET C CA    1 
ATOM   12097 C  C     . MET C 2 158 ? 116.826 82.464  125.408 1.00 21.70 ?  137 MET C C     1 
ATOM   12098 O  O     . MET C 2 158 ? 117.732 81.628  125.430 1.00 21.83 ?  137 MET C O     1 
ATOM   12099 C  CB    . MET C 2 158 ? 114.608 81.907  124.454 1.00 22.05 ?  137 MET C CB    1 
ATOM   12100 C  CG    . MET C 2 158 ? 113.308 81.104  124.597 1.00 23.93 ?  137 MET C CG    1 
ATOM   12101 S  SD    . MET C 2 158 ? 112.371 81.167  123.057 1.00 27.75 ?  137 MET C SD    1 
ATOM   12102 C  CE    . MET C 2 158 ? 113.441 80.168  122.010 1.00 26.00 ?  137 MET C CE    1 
ATOM   12103 N  N     . ILE C 2 159 ? 117.020 83.725  125.052 1.00 20.90 ?  138 ILE C N     1 
ATOM   12104 C  CA    . ILE C 2 159 ? 118.332 84.178  124.623 1.00 20.60 ?  138 ILE C CA    1 
ATOM   12105 C  C     . ILE C 2 159 ? 119.290 84.237  125.816 1.00 20.36 ?  138 ILE C C     1 
ATOM   12106 O  O     . ILE C 2 159 ? 120.392 83.688  125.751 1.00 19.65 ?  138 ILE C O     1 
ATOM   12107 C  CB    . ILE C 2 159 ? 118.254 85.534  123.862 1.00 20.17 ?  138 ILE C CB    1 
ATOM   12108 C  CG1   . ILE C 2 159 ? 117.503 85.368  122.528 1.00 20.66 ?  138 ILE C CG1   1 
ATOM   12109 C  CG2   . ILE C 2 159 ? 119.649 86.163  123.708 1.00 20.62 ?  138 ILE C CG2   1 
ATOM   12110 C  CD1   . ILE C 2 159 ? 118.151 84.466  121.474 1.00 22.17 ?  138 ILE C CD1   1 
ATOM   12111 N  N     . VAL C 2 160 ? 118.857 84.874  126.905 1.00 19.58 ?  139 VAL C N     1 
ATOM   12112 C  CA    . VAL C 2 160 ? 119.695 85.037  128.097 1.00 19.88 ?  139 VAL C CA    1 
ATOM   12113 C  C     . VAL C 2 160 ? 119.959 83.682  128.760 1.00 19.44 ?  139 VAL C C     1 
ATOM   12114 O  O     . VAL C 2 160 ? 121.012 83.469  129.349 1.00 19.88 ?  139 VAL C O     1 
ATOM   12115 C  CB    . VAL C 2 160 ? 119.077 86.039  129.139 1.00 19.52 ?  139 VAL C CB    1 
ATOM   12116 C  CG1   . VAL C 2 160 ? 119.938 86.111  130.413 1.00 20.75 ?  139 VAL C CG1   1 
ATOM   12117 C  CG2   . VAL C 2 160 ? 118.959 87.436  128.540 1.00 20.03 ?  139 VAL C CG2   1 
ATOM   12118 N  N     . GLY C 2 161 ? 119.002 82.765  128.656 1.00 19.13 ?  140 GLY C N     1 
ATOM   12119 C  CA    . GLY C 2 161 ? 119.187 81.437  129.217 1.00 18.05 ?  140 GLY C CA    1 
ATOM   12120 C  C     . GLY C 2 161 ? 120.367 80.752  128.576 1.00 17.86 ?  140 GLY C C     1 
ATOM   12121 O  O     . GLY C 2 161 ? 121.200 80.146  129.258 1.00 17.47 ?  140 GLY C O     1 
ATOM   12122 N  N     . LEU C 2 162 ? 120.433 80.838  127.252 1.00 17.92 ?  141 LEU C N     1 
ATOM   12123 C  CA    . LEU C 2 162 ? 121.555 80.269  126.513 1.00 18.32 ?  141 LEU C CA    1 
ATOM   12124 C  C     . LEU C 2 162 ? 122.901 80.946  126.854 1.00 18.55 ?  141 LEU C C     1 
ATOM   12125 O  O     . LEU C 2 162 ? 123.910 80.260  127.014 1.00 18.49 ?  141 LEU C O     1 
ATOM   12126 C  CB    . LEU C 2 162 ? 121.269 80.317  125.007 1.00 18.50 ?  141 LEU C CB    1 
ATOM   12127 C  CG    . LEU C 2 162 ? 120.176 79.345  124.552 1.00 19.32 ?  141 LEU C CG    1 
ATOM   12128 C  CD1   . LEU C 2 162 ? 119.680 79.712  123.158 1.00 20.38 ?  141 LEU C CD1   1 
ATOM   12129 C  CD2   . LEU C 2 162 ? 120.672 77.897  124.601 1.00 19.94 ?  141 LEU C CD2   1 
ATOM   12130 N  N     . TYR C 2 163 ? 122.913 82.269  126.999 1.00 19.16 ?  142 TYR C N     1 
ATOM   12131 C  CA    . TYR C 2 163 ? 124.127 82.976  127.455 1.00 20.16 ?  142 TYR C CA    1 
ATOM   12132 C  C     . TYR C 2 163 ? 124.612 82.469  128.801 1.00 20.78 ?  142 TYR C C     1 
ATOM   12133 O  O     . TYR C 2 163 ? 125.811 82.268  129.012 1.00 20.36 ?  142 TYR C O     1 
ATOM   12134 C  CB    . TYR C 2 163 ? 123.895 84.492  127.572 1.00 20.34 ?  142 TYR C CB    1 
ATOM   12135 C  CG    . TYR C 2 163 ? 123.613 85.207  126.258 1.00 22.46 ?  142 TYR C CG    1 
ATOM   12136 C  CD1   . TYR C 2 163 ? 124.034 84.681  125.042 1.00 23.88 ?  142 TYR C CD1   1 
ATOM   12137 C  CD2   . TYR C 2 163 ? 122.932 86.419  126.244 1.00 22.41 ?  142 TYR C CD2   1 
ATOM   12138 C  CE1   . TYR C 2 163 ? 123.766 85.348  123.832 1.00 25.93 ?  142 TYR C CE1   1 
ATOM   12139 C  CE2   . TYR C 2 163 ? 122.668 87.088  125.052 1.00 22.07 ?  142 TYR C CE2   1 
ATOM   12140 C  CZ    . TYR C 2 163 ? 123.092 86.556  123.858 1.00 25.19 ?  142 TYR C CZ    1 
ATOM   12141 O  OH    . TYR C 2 163 ? 122.814 87.239  122.691 1.00 27.43 ?  142 TYR C OH    1 
ATOM   12142 N  N     . LYS C 2 164 ? 123.674 82.260  129.717 1.00 21.39 ?  143 LYS C N     1 
ATOM   12143 C  CA    . LYS C 2 164 ? 124.050 81.886  131.070 1.00 22.49 ?  143 LYS C CA    1 
ATOM   12144 C  C     . LYS C 2 164 ? 124.341 80.394  131.212 1.00 22.49 ?  143 LYS C C     1 
ATOM   12145 O  O     . LYS C 2 164 ? 124.889 79.967  132.222 1.00 22.45 ?  143 LYS C O     1 
ATOM   12146 C  CB    . LYS C 2 164 ? 123.031 82.400  132.084 1.00 23.16 ?  143 LYS C CB    1 
ATOM   12147 C  CG    . LYS C 2 164 ? 123.054 83.925  132.174 1.00 26.08 ?  143 LYS C CG    1 
ATOM   12148 C  CD    . LYS C 2 164 ? 122.499 84.431  133.473 1.00 30.38 ?  143 LYS C CD    1 
ATOM   12149 C  CE    . LYS C 2 164 ? 122.713 85.919  133.604 1.00 32.69 ?  143 LYS C CE    1 
ATOM   12150 N  NZ    . LYS C 2 164 ? 122.114 86.416  134.874 1.00 35.60 1  143 LYS C NZ    1 
ATOM   12151 N  N     . ALA C 2 165 ? 124.044 79.625  130.164 1.00 22.02 ?  144 ALA C N     1 
ATOM   12152 C  CA    . ALA C 2 165 ? 124.359 78.209  130.156 1.00 22.69 ?  144 ALA C CA    1 
ATOM   12153 C  C     . ALA C 2 165 ? 125.787 77.908  129.668 1.00 23.20 ?  144 ALA C C     1 
ATOM   12154 O  O     . ALA C 2 165 ? 126.235 76.771  129.743 1.00 23.80 ?  144 ALA C O     1 
ATOM   12155 C  CB    . ALA C 2 165 ? 123.311 77.423  129.329 1.00 21.79 ?  144 ALA C CB    1 
ATOM   12156 N  N     . ILE C 2 166 ? 126.505 78.917  129.169 1.00 23.97 ?  145 ILE C N     1 
ATOM   12157 C  CA    . ILE C 2 166 ? 127.881 78.699  128.708 1.00 24.29 ?  145 ILE C CA    1 
ATOM   12158 C  C     . ILE C 2 166 ? 128.742 78.140  129.845 1.00 25.49 ?  145 ILE C C     1 
ATOM   12159 O  O     . ILE C 2 166 ? 128.709 78.646  130.962 1.00 25.82 ?  145 ILE C O     1 
ATOM   12160 C  CB    . ILE C 2 166 ? 128.544 79.987  128.139 1.00 24.22 ?  145 ILE C CB    1 
ATOM   12161 C  CG1   . ILE C 2 166 ? 127.765 80.523  126.942 1.00 23.45 ?  145 ILE C CG1   1 
ATOM   12162 C  CG2   . ILE C 2 166 ? 129.991 79.711  127.728 1.00 23.42 ?  145 ILE C CG2   1 
ATOM   12163 C  CD1   . ILE C 2 166 ? 128.174 81.960  126.527 1.00 21.99 ?  145 ILE C CD1   1 
ATOM   12164 N  N     . GLN C 2 167 ? 129.464 77.066  129.557 1.00 26.83 ?  146 GLN C N     1 
ATOM   12165 C  CA    . GLN C 2 167 ? 130.361 76.460  130.531 1.00 28.85 ?  146 GLN C CA    1 
ATOM   12166 C  C     . GLN C 2 167 ? 131.786 76.705  130.075 1.00 29.77 ?  146 GLN C C     1 
ATOM   12167 O  O     . GLN C 2 167 ? 132.095 76.576  128.886 1.00 29.74 ?  146 GLN C O     1 
ATOM   12168 C  CB    . GLN C 2 167 ? 130.099 74.953  130.671 1.00 28.99 ?  146 GLN C CB    1 
ATOM   12169 C  CG    . GLN C 2 167 ? 128.797 74.594  131.388 1.00 30.30 ?  146 GLN C CG    1 
ATOM   12170 C  CD    . GLN C 2 167 ? 128.833 74.905  132.879 1.00 33.32 ?  146 GLN C CD    1 
ATOM   12171 O  OE1   . GLN C 2 167 ? 129.888 75.216  133.435 1.00 34.63 ?  146 GLN C OE1   1 
ATOM   12172 N  NE2   . GLN C 2 167 ? 127.681 74.801  133.536 1.00 32.32 ?  146 GLN C NE2   1 
ATOM   12173 N  N     . LYS C 2 168 ? 132.648 77.062  131.020 1.00 31.29 ?  147 LYS C N     1 
ATOM   12174 C  CA    . LYS C 2 168 ? 134.058 77.313  130.722 1.00 33.14 ?  147 LYS C CA    1 
ATOM   12175 C  C     . LYS C 2 168 ? 134.648 76.106  130.006 1.00 33.79 ?  147 LYS C C     1 
ATOM   12176 O  O     . LYS C 2 168 ? 134.318 74.959  130.324 1.00 34.06 ?  147 LYS C O     1 
ATOM   12177 C  CB    . LYS C 2 168 ? 134.827 77.623  132.005 1.00 33.44 ?  147 LYS C CB    1 
ATOM   12178 C  CG    . LYS C 2 168 ? 136.140 78.378  131.816 1.00 35.61 ?  147 LYS C CG    1 
ATOM   12179 C  CD    . LYS C 2 168 ? 136.771 78.659  133.176 1.00 38.40 ?  147 LYS C CD    1 
ATOM   12180 C  CE    . LYS C 2 168 ? 137.924 79.645  133.096 1.00 40.48 ?  147 LYS C CE    1 
ATOM   12181 N  NZ    . LYS C 2 168 ? 139.228 78.931  133.047 1.00 41.56 1  147 LYS C NZ    1 
ATOM   12182 N  N     . ASP C 2 169 ? 135.479 76.379  129.005 1.00 35.10 ?  148 ASP C N     1 
ATOM   12183 C  CA    . ASP C 2 169 ? 136.144 75.335  128.207 1.00 36.27 ?  148 ASP C CA    1 
ATOM   12184 C  C     . ASP C 2 169 ? 135.203 74.357  127.502 1.00 36.29 ?  148 ASP C C     1 
ATOM   12185 O  O     . ASP C 2 169 ? 135.629 73.290  127.057 1.00 36.95 ?  148 ASP C O     1 
ATOM   12186 C  CB    . ASP C 2 169 ? 137.143 74.556  129.069 1.00 37.15 ?  148 ASP C CB    1 
ATOM   12187 C  CG    . ASP C 2 169 ? 138.346 75.377  129.450 1.00 38.94 ?  148 ASP C CG    1 
ATOM   12188 O  OD1   . ASP C 2 169 ? 138.641 76.375  128.752 1.00 41.71 ?  148 ASP C OD1   1 
ATOM   12189 O  OD2   . ASP C 2 169 ? 138.997 75.021  130.452 1.00 41.64 -1 148 ASP C OD2   1 
ATOM   12190 N  N     . ASP C 2 170 ? 133.927 74.710  127.402 1.00 35.87 ?  149 ASP C N     1 
ATOM   12191 C  CA    . ASP C 2 170 ? 132.968 73.864  126.705 1.00 35.24 ?  149 ASP C CA    1 
ATOM   12192 C  C     . ASP C 2 170 ? 132.492 74.620  125.473 1.00 34.12 ?  149 ASP C C     1 
ATOM   12193 O  O     . ASP C 2 170 ? 131.641 75.528  125.554 1.00 33.52 ?  149 ASP C O     1 
ATOM   12194 C  CB    . ASP C 2 170 ? 131.820 73.455  127.634 1.00 36.09 ?  149 ASP C CB    1 
ATOM   12195 C  CG    . ASP C 2 170 ? 130.688 72.726  126.909 1.00 38.39 ?  149 ASP C CG    1 
ATOM   12196 O  OD1   . ASP C 2 170 ? 130.864 72.269  125.755 1.00 42.06 ?  149 ASP C OD1   1 
ATOM   12197 O  OD2   . ASP C 2 170 ? 129.605 72.600  127.512 1.00 42.21 -1 149 ASP C OD2   1 
ATOM   12198 N  N     . GLU C 2 171 ? 133.073 74.242  124.339 1.00 32.48 ?  150 GLU C N     1 
ATOM   12199 C  CA    . GLU C 2 171 ? 132.877 74.945  123.084 1.00 30.93 ?  150 GLU C CA    1 
ATOM   12200 C  C     . GLU C 2 171 ? 131.454 74.797  122.538 1.00 29.37 ?  150 GLU C C     1 
ATOM   12201 O  O     . GLU C 2 171 ? 130.969 75.680  121.831 1.00 28.99 ?  150 GLU C O     1 
ATOM   12202 C  CB    . GLU C 2 171 ? 133.935 74.521  122.046 1.00 31.30 ?  150 GLU C CB    1 
ATOM   12203 C  CG    . GLU C 2 171 ? 133.794 73.095  121.461 1.00 33.64 ?  150 GLU C CG    1 
ATOM   12204 C  CD    . GLU C 2 171 ? 135.036 72.616  120.670 1.00 36.40 ?  150 GLU C CD    1 
ATOM   12205 O  OE1   . GLU C 2 171 ? 136.012 73.385  120.526 1.00 38.62 ?  150 GLU C OE1   1 
ATOM   12206 O  OE2   . GLU C 2 171 ? 135.038 71.460  120.191 1.00 37.42 -1 150 GLU C OE2   1 
ATOM   12207 N  N     . ILE C 2 172 ? 130.793 73.685  122.862 1.00 27.68 ?  151 ILE C N     1 
ATOM   12208 C  CA    . ILE C 2 172 ? 129.428 73.450  122.385 1.00 26.26 ?  151 ILE C CA    1 
ATOM   12209 C  C     . ILE C 2 172 ? 128.437 74.414  123.042 1.00 24.85 ?  151 ILE C C     1 
ATOM   12210 O  O     . ILE C 2 172 ? 127.590 74.980  122.352 1.00 23.53 ?  151 ILE C O     1 
ATOM   12211 C  CB    . ILE C 2 172 ? 128.984 71.972  122.552 1.00 26.53 ?  151 ILE C CB    1 
ATOM   12212 C  CG1   . ILE C 2 172 ? 129.892 71.036  121.738 1.00 27.59 ?  151 ILE C CG1   1 
ATOM   12213 C  CG2   . ILE C 2 172 ? 127.498 71.784  122.191 1.00 26.51 ?  151 ILE C CG2   1 
ATOM   12214 C  CD1   . ILE C 2 172 ? 129.797 71.184  120.213 1.00 26.91 ?  151 ILE C CD1   1 
ATOM   12215 N  N     . SER C 2 173 ? 128.545 74.616  124.358 1.00 23.58 ?  152 SER C N     1 
ATOM   12216 C  CA    . SER C 2 173 ? 127.660 75.571  125.021 1.00 22.36 ?  152 SER C CA    1 
ATOM   12217 C  C     . SER C 2 173 ? 127.920 76.988  124.503 1.00 21.79 ?  152 SER C C     1 
ATOM   12218 O  O     . SER C 2 173 ? 126.992 77.798  124.393 1.00 20.91 ?  152 SER C O     1 
ATOM   12219 C  CB    . SER C 2 173 ? 127.764 75.496  126.549 1.00 22.43 ?  152 SER C CB    1 
ATOM   12220 O  OG    . SER C 2 173 ? 129.075 75.794  127.002 1.00 24.02 ?  152 SER C OG    1 
ATOM   12221 N  N     . LEU C 2 174 ? 129.184 77.275  124.188 1.00 21.65 ?  153 LEU C N     1 
ATOM   12222 C  CA    . LEU C 2 174 ? 129.567 78.570  123.632 1.00 21.86 ?  153 LEU C CA    1 
ATOM   12223 C  C     . LEU C 2 174 ? 128.961 78.772  122.241 1.00 21.98 ?  153 LEU C C     1 
ATOM   12224 O  O     . LEU C 2 174 ? 128.399 79.835  121.970 1.00 21.64 ?  153 LEU C O     1 
ATOM   12225 C  CB    . LEU C 2 174 ? 131.098 78.759  123.618 1.00 21.71 ?  153 LEU C CB    1 
ATOM   12226 C  CG    . LEU C 2 174 ? 131.678 80.069  123.050 1.00 22.04 ?  153 LEU C CG    1 
ATOM   12227 C  CD1   . LEU C 2 174 ? 131.054 81.314  123.681 1.00 21.99 ?  153 LEU C CD1   1 
ATOM   12228 C  CD2   . LEU C 2 174 ? 133.201 80.085  123.226 1.00 23.37 ?  153 LEU C CD2   1 
ATOM   12229 N  N     . PHE C 2 175 ? 129.069 77.756  121.379 1.00 22.17 ?  154 PHE C N     1 
ATOM   12230 C  CA    . PHE C 2 175 ? 128.444 77.779  120.038 1.00 22.02 ?  154 PHE C CA    1 
ATOM   12231 C  C     . PHE C 2 175 ? 126.954 78.089  120.107 1.00 21.86 ?  154 PHE C C     1 
ATOM   12232 O  O     . PHE C 2 175 ? 126.432 78.884  119.315 1.00 21.62 ?  154 PHE C O     1 
ATOM   12233 C  CB    . PHE C 2 175 ? 128.630 76.432  119.322 1.00 22.08 ?  154 PHE C CB    1 
ATOM   12234 C  CG    . PHE C 2 175 ? 127.873 76.321  118.013 1.00 21.99 ?  154 PHE C CG    1 
ATOM   12235 C  CD1   . PHE C 2 175 ? 128.409 76.846  116.833 1.00 20.87 ?  154 PHE C CD1   1 
ATOM   12236 C  CD2   . PHE C 2 175 ? 126.613 75.705  117.966 1.00 20.82 ?  154 PHE C CD2   1 
ATOM   12237 C  CE1   . PHE C 2 175 ? 127.707 76.774  115.629 1.00 20.27 ?  154 PHE C CE1   1 
ATOM   12238 C  CE2   . PHE C 2 175 ? 125.901 75.615  116.767 1.00 20.19 ?  154 PHE C CE2   1 
ATOM   12239 C  CZ    . PHE C 2 175 ? 126.452 76.147  115.587 1.00 20.93 ?  154 PHE C CZ    1 
ATOM   12240 N  N     . LYS C 2 176 ? 126.266 77.422  121.035 1.00 21.98 ?  155 LYS C N     1 
ATOM   12241 C  CA    . LYS C 2 176 ? 124.821 77.602  121.196 1.00 21.79 ?  155 LYS C CA    1 
ATOM   12242 C  C     . LYS C 2 176 ? 124.476 79.050  121.559 1.00 21.70 ?  155 LYS C C     1 
ATOM   12243 O  O     . LYS C 2 176 ? 123.531 79.629  121.004 1.00 21.10 ?  155 LYS C O     1 
ATOM   12244 C  CB    . LYS C 2 176 ? 124.268 76.612  122.230 1.00 22.00 ?  155 LYS C CB    1 
ATOM   12245 C  CG    . LYS C 2 176 ? 124.344 75.155  121.794 1.00 21.93 ?  155 LYS C CG    1 
ATOM   12246 C  CD    . LYS C 2 176 ? 123.848 74.215  122.879 1.00 23.06 ?  155 LYS C CD    1 
ATOM   12247 C  CE    . LYS C 2 176 ? 123.865 72.773  122.415 1.00 24.91 ?  155 LYS C CE    1 
ATOM   12248 N  NZ    . LYS C 2 176 ? 123.697 71.825  123.567 1.00 25.16 1  155 LYS C NZ    1 
ATOM   12249 N  N     . ALA C 2 177 ? 125.245 79.630  122.486 1.00 21.49 ?  156 ALA C N     1 
ATOM   12250 C  CA    . ALA C 2 177 ? 125.079 81.038  122.833 1.00 20.60 ?  156 ALA C CA    1 
ATOM   12251 C  C     . ALA C 2 177 ? 125.411 81.997  121.668 1.00 20.37 ?  156 ALA C C     1 
ATOM   12252 O  O     . ALA C 2 177 ? 124.752 83.015  121.507 1.00 19.61 ?  156 ALA C O     1 
ATOM   12253 C  CB    . ALA C 2 177 ? 125.892 81.397  124.073 1.00 20.88 ?  156 ALA C CB    1 
ATOM   12254 N  N     . MET C 2 178 ? 126.415 81.659  120.859 1.00 20.70 ?  157 MET C N     1 
ATOM   12255 C  CA    . MET C 2 178 ? 126.761 82.473  119.681 1.00 21.06 ?  157 MET C CA    1 
ATOM   12256 C  C     . MET C 2 178 ? 125.678 82.420  118.621 1.00 20.83 ?  157 MET C C     1 
ATOM   12257 O  O     . MET C 2 178 ? 125.465 83.401  117.902 1.00 21.28 ?  157 MET C O     1 
ATOM   12258 C  CB    . MET C 2 178 ? 128.096 82.036  119.052 1.00 20.68 ?  157 MET C CB    1 
ATOM   12259 C  CG    . MET C 2 178 ? 129.348 82.318  119.882 1.00 21.61 ?  157 MET C CG    1 
ATOM   12260 S  SD    . MET C 2 178 ? 130.795 81.530  119.138 1.00 24.32 ?  157 MET C SD    1 
ATOM   12261 C  CE    . MET C 2 178 ? 132.123 82.319  120.071 1.00 23.64 ?  157 MET C CE    1 
ATOM   12262 N  N     . VAL C 2 179 ? 125.018 81.269  118.487 1.00 20.76 ?  158 VAL C N     1 
ATOM   12263 C  CA    . VAL C 2 179 ? 123.877 81.151  117.570 1.00 20.14 ?  158 VAL C CA    1 
ATOM   12264 C  C     . VAL C 2 179 ? 122.752 82.068  118.061 1.00 20.35 ?  158 VAL C C     1 
ATOM   12265 O  O     . VAL C 2 179 ? 122.145 82.806  117.280 1.00 19.82 ?  158 VAL C O     1 
ATOM   12266 C  CB    . VAL C 2 179 ? 123.351 79.694  117.472 1.00 20.07 ?  158 VAL C CB    1 
ATOM   12267 C  CG1   . VAL C 2 179 ? 122.019 79.651  116.719 1.00 20.07 ?  158 VAL C CG1   1 
ATOM   12268 C  CG2   . VAL C 2 179 ? 124.377 78.799  116.783 1.00 20.57 ?  158 VAL C CG2   1 
ATOM   12269 N  N     . ALA C 2 180 ? 122.491 82.009  119.364 1.00 19.89 ?  159 ALA C N     1 
ATOM   12270 C  CA    . ALA C 2 180 ? 121.486 82.861  120.000 1.00 20.50 ?  159 ALA C CA    1 
ATOM   12271 C  C     . ALA C 2 180 ? 121.803 84.346  119.758 1.00 20.67 ?  159 ALA C C     1 
ATOM   12272 O  O     . ALA C 2 180 ? 120.916 85.122  119.398 1.00 21.27 ?  159 ALA C O     1 
ATOM   12273 C  CB    . ALA C 2 180 ? 121.432 82.569  121.484 1.00 20.03 ?  159 ALA C CB    1 
ATOM   12274 N  N     . SER C 2 181 ? 123.067 84.724  119.946 1.00 20.78 ?  160 SER C N     1 
ATOM   12275 C  CA    . SER C 2 181 ? 123.526 86.096  119.701 1.00 21.26 ?  160 SER C CA    1 
ATOM   12276 C  C     . SER C 2 181 ? 123.362 86.516  118.232 1.00 21.19 ?  160 SER C C     1 
ATOM   12277 O  O     . SER C 2 181 ? 122.863 87.600  117.955 1.00 20.89 ?  160 SER C O     1 
ATOM   12278 C  CB    . SER C 2 181 ? 124.980 86.279  120.162 1.00 21.42 ?  160 SER C CB    1 
ATOM   12279 O  OG    . SER C 2 181 ? 125.401 87.627  120.010 1.00 23.69 ?  160 SER C OG    1 
ATOM   12280 N  N     . VAL C 2 182 ? 123.781 85.664  117.290 1.00 20.99 ?  161 VAL C N     1 
ATOM   12281 C  CA    . VAL C 2 182 ? 123.528 85.969  115.877 1.00 21.18 ?  161 VAL C CA    1 
ATOM   12282 C  C     . VAL C 2 182 ? 122.023 86.148  115.612 1.00 21.15 ?  161 VAL C C     1 
ATOM   12283 O  O     . VAL C 2 182 ? 121.619 87.091  114.911 1.00 21.18 ?  161 VAL C O     1 
ATOM   12284 C  CB    . VAL C 2 182 ? 124.149 84.910  114.910 1.00 21.11 ?  161 VAL C CB    1 
ATOM   12285 C  CG1   . VAL C 2 182 ? 123.687 85.155  113.475 1.00 21.75 ?  161 VAL C CG1   1 
ATOM   12286 C  CG2   . VAL C 2 182 ? 125.674 84.945  114.989 1.00 20.98 ?  161 VAL C CG2   1 
ATOM   12287 N  N     . TYR C 2 183 ? 121.186 85.267  116.176 1.00 21.10 ?  162 TYR C N     1 
ATOM   12288 C  CA    . TYR C 2 183 ? 119.732 85.405  116.002 1.00 21.21 ?  162 TYR C CA    1 
ATOM   12289 C  C     . TYR C 2 183 ? 119.181 86.702  116.592 1.00 21.38 ?  162 TYR C C     1 
ATOM   12290 O  O     . TYR C 2 183 ? 118.237 87.273  116.057 1.00 20.97 ?  162 TYR C O     1 
ATOM   12291 C  CB    . TYR C 2 183 ? 118.947 84.200  116.562 1.00 21.50 ?  162 TYR C CB    1 
ATOM   12292 C  CG    . TYR C 2 183 ? 119.095 82.940  115.754 1.00 22.20 ?  162 TYR C CG    1 
ATOM   12293 C  CD1   . TYR C 2 183 ? 119.502 82.987  114.422 1.00 23.80 ?  162 TYR C CD1   1 
ATOM   12294 C  CD2   . TYR C 2 183 ? 118.808 81.690  116.315 1.00 23.71 ?  162 TYR C CD2   1 
ATOM   12295 C  CE1   . TYR C 2 183 ? 119.640 81.816  113.667 1.00 25.52 ?  162 TYR C CE1   1 
ATOM   12296 C  CE2   . TYR C 2 183 ? 118.938 80.526  115.576 1.00 24.01 ?  162 TYR C CE2   1 
ATOM   12297 C  CZ    . TYR C 2 183 ? 119.362 80.591  114.259 1.00 25.47 ?  162 TYR C CZ    1 
ATOM   12298 O  OH    . TYR C 2 183 ? 119.509 79.433  113.523 1.00 25.37 ?  162 TYR C OH    1 
ATOM   12299 N  N     . LEU C 2 184 ? 119.761 87.148  117.697 1.00 22.12 ?  163 LEU C N     1 
ATOM   12300 C  CA    . LEU C 2 184 ? 119.400 88.458  118.274 1.00 23.80 ?  163 LEU C CA    1 
ATOM   12301 C  C     . LEU C 2 184 ? 119.860 89.595  117.350 1.00 24.21 ?  163 LEU C C     1 
ATOM   12302 O  O     . LEU C 2 184 ? 119.088 90.487  117.066 1.00 24.72 ?  163 LEU C O     1 
ATOM   12303 C  CB    . LEU C 2 184 ? 119.990 88.622  119.678 1.00 23.52 ?  163 LEU C CB    1 
ATOM   12304 C  CG    . LEU C 2 184 ? 119.664 89.873  120.518 1.00 24.91 ?  163 LEU C CG    1 
ATOM   12305 C  CD1   . LEU C 2 184 ? 119.613 89.506  121.979 1.00 24.81 ?  163 LEU C CD1   1 
ATOM   12306 C  CD2   . LEU C 2 184 ? 120.649 91.029  120.294 1.00 26.39 ?  163 LEU C CD2   1 
ATOM   12307 N  N     . GLU C 2 185 ? 121.111 89.539  116.873 1.00 25.17 ?  164 GLU C N     1 
ATOM   12308 C  CA    . GLU C 2 185 ? 121.693 90.622  116.065 1.00 25.30 ?  164 GLU C CA    1 
ATOM   12309 C  C     . GLU C 2 185 ? 121.030 90.783  114.687 1.00 25.07 ?  164 GLU C C     1 
ATOM   12310 O  O     . GLU C 2 185 ? 120.760 91.906  114.229 1.00 24.49 ?  164 GLU C O     1 
ATOM   12311 C  CB    . GLU C 2 185 ? 123.208 90.396  115.847 1.00 26.17 ?  164 GLU C CB    1 
ATOM   12312 C  CG    . GLU C 2 185 ? 124.073 90.476  117.124 1.00 27.05 ?  164 GLU C CG    1 
ATOM   12313 C  CD    . GLU C 2 185 ? 124.334 91.914  117.590 1.00 29.23 ?  164 GLU C CD    1 
ATOM   12314 O  OE1   . GLU C 2 185 ? 123.845 92.887  116.948 1.00 28.79 ?  164 GLU C OE1   1 
ATOM   12315 O  OE2   . GLU C 2 185 ? 125.067 92.090  118.591 1.00 28.65 -1 164 GLU C OE2   1 
ATOM   12316 N  N     . SER C 2 186 ? 120.800 89.650  114.035 1.00 24.23 ?  165 SER C N     1 
ATOM   12317 C  CA    . SER C 2 186 ? 120.526 89.604  112.604 1.00 24.71 ?  165 SER C CA    1 
ATOM   12318 C  C     . SER C 2 186 ? 119.092 89.207  112.266 1.00 24.51 ?  165 SER C C     1 
ATOM   12319 O  O     . SER C 2 186 ? 118.694 89.280  111.106 1.00 24.87 ?  165 SER C O     1 
ATOM   12320 C  CB    . SER C 2 186 ? 121.492 88.622  111.926 1.00 25.06 ?  165 SER C CB    1 
ATOM   12321 O  OG    . SER C 2 186 ? 122.842 88.989  112.144 1.00 26.29 ?  165 SER C OG    1 
ATOM   12322 N  N     . PHE C 2 187 ? 118.334 88.777  113.272 1.00 24.71 ?  166 PHE C N     1 
ATOM   12323 C  CA    . PHE C 2 187 ? 116.944 88.362  113.085 1.00 25.69 ?  166 PHE C CA    1 
ATOM   12324 C  C     . PHE C 2 187 ? 115.980 89.110  114.018 1.00 25.87 ?  166 PHE C C     1 
ATOM   12325 O  O     . PHE C 2 187 ? 115.094 89.816  113.531 1.00 26.03 ?  166 PHE C O     1 
ATOM   12326 C  CB    . PHE C 2 187 ? 116.793 86.836  113.244 1.00 25.54 ?  166 PHE C CB    1 
ATOM   12327 C  CG    . PHE C 2 187 ? 115.358 86.360  113.331 1.00 26.64 ?  166 PHE C CG    1 
ATOM   12328 C  CD1   . PHE C 2 187 ? 114.465 86.567  112.272 1.00 25.90 ?  166 PHE C CD1   1 
ATOM   12329 C  CD2   . PHE C 2 187 ? 114.901 85.691  114.470 1.00 27.45 ?  166 PHE C CD2   1 
ATOM   12330 C  CE1   . PHE C 2 187 ? 113.130 86.128  112.352 1.00 25.64 ?  166 PHE C CE1   1 
ATOM   12331 C  CE2   . PHE C 2 187 ? 113.563 85.241  114.564 1.00 26.52 ?  166 PHE C CE2   1 
ATOM   12332 C  CZ    . PHE C 2 187 ? 112.683 85.461  113.501 1.00 27.18 ?  166 PHE C CZ    1 
ATOM   12333 N  N     . LEU C 2 188 ? 116.167 88.963  115.331 1.00 26.13 ?  167 LEU C N     1 
ATOM   12334 C  CA    . LEU C 2 188 ? 115.214 89.480  116.348 1.00 27.13 ?  167 LEU C CA    1 
ATOM   12335 C  C     . LEU C 2 188 ? 115.033 91.009  116.393 1.00 27.22 ?  167 LEU C C     1 
ATOM   12336 O  O     . LEU C 2 188 ? 113.950 91.497  116.743 1.00 28.03 ?  167 LEU C O     1 
ATOM   12337 C  CB    . LEU C 2 188 ? 115.591 88.995  117.757 1.00 26.89 ?  167 LEU C CB    1 
ATOM   12338 C  CG    . LEU C 2 188 ? 115.530 87.513  118.161 1.00 28.64 ?  167 LEU C CG    1 
ATOM   12339 C  CD1   . LEU C 2 188 ? 116.004 87.340  119.602 1.00 28.34 ?  167 LEU C CD1   1 
ATOM   12340 C  CD2   . LEU C 2 188 ? 114.141 86.921  117.995 1.00 27.90 ?  167 LEU C CD2   1 
ATOM   12341 N  N     . PHE C 2 189 ? 116.088 91.755  116.087 1.00 26.79 ?  168 PHE C N     1 
ATOM   12342 C  CA    . PHE C 2 189 ? 115.999 93.214  116.074 1.00 26.90 ?  168 PHE C CA    1 
ATOM   12343 C  C     . PHE C 2 189 ? 115.056 93.705  114.970 1.00 26.52 ?  168 PHE C C     1 
ATOM   12344 O  O     . PHE C 2 189 ? 114.552 94.835  115.030 1.00 26.02 ?  168 PHE C O     1 
ATOM   12345 C  CB    . PHE C 2 189 ? 117.382 93.858  115.850 1.00 27.03 ?  168 PHE C CB    1 
ATOM   12346 C  CG    . PHE C 2 189 ? 118.205 94.071  117.118 1.00 28.09 ?  168 PHE C CG    1 
ATOM   12347 C  CD1   . PHE C 2 189 ? 117.703 94.800  118.198 1.00 28.69 ?  168 PHE C CD1   1 
ATOM   12348 C  CD2   . PHE C 2 189 ? 119.511 93.603  117.194 1.00 29.15 ?  168 PHE C CD2   1 
ATOM   12349 C  CE1   . PHE C 2 189 ? 118.468 95.013  119.355 1.00 28.50 ?  168 PHE C CE1   1 
ATOM   12350 C  CE2   . PHE C 2 189 ? 120.293 93.808  118.346 1.00 30.19 ?  168 PHE C CE2   1 
ATOM   12351 C  CZ    . PHE C 2 189 ? 119.760 94.520  119.436 1.00 29.81 ?  168 PHE C CZ    1 
ATOM   12352 N  N     . TYR C 2 190 ? 114.833 92.873  113.952 1.00 26.18 ?  169 TYR C N     1 
ATOM   12353 C  CA    . TYR C 2 190 ? 114.253 93.386  112.716 1.00 26.24 ?  169 TYR C CA    1 
ATOM   12354 C  C     . TYR C 2 190 ? 112.739 93.645  112.724 1.00 25.94 ?  169 TYR C C     1 
ATOM   12355 O  O     . TYR C 2 190 ? 112.244 94.478  111.963 1.00 25.71 ?  169 TYR C O     1 
ATOM   12356 C  CB    . TYR C 2 190 ? 114.764 92.592  111.512 1.00 27.13 ?  169 TYR C CB    1 
ATOM   12357 C  CG    . TYR C 2 190 ? 116.184 93.014  111.196 1.00 28.07 ?  169 TYR C CG    1 
ATOM   12358 C  CD1   . TYR C 2 190 ? 117.271 92.446  111.869 1.00 29.54 ?  169 TYR C CD1   1 
ATOM   12359 C  CD2   . TYR C 2 190 ? 116.438 94.032  110.276 1.00 29.31 ?  169 TYR C CD2   1 
ATOM   12360 C  CE1   . TYR C 2 190 ? 118.581 92.857  111.602 1.00 30.44 ?  169 TYR C CE1   1 
ATOM   12361 C  CE2   . TYR C 2 190 ? 117.748 94.451  110.000 1.00 30.64 ?  169 TYR C CE2   1 
ATOM   12362 C  CZ    . TYR C 2 190 ? 118.811 93.861  110.671 1.00 30.40 ?  169 TYR C CZ    1 
ATOM   12363 O  OH    . TYR C 2 190 ? 120.098 94.274  110.411 1.00 28.85 ?  169 TYR C OH    1 
ATOM   12364 N  N     . SER C 2 191 ? 112.021 92.977  113.623 1.00 25.17 ?  170 SER C N     1 
ATOM   12365 C  CA    . SER C 2 191 ? 110.604 93.263  113.829 1.00 25.10 ?  170 SER C CA    1 
ATOM   12366 C  C     . SER C 2 191 ? 110.465 94.688  114.380 1.00 25.16 ?  170 SER C C     1 
ATOM   12367 O  O     . SER C 2 191 ? 109.460 95.361  114.130 1.00 25.30 ?  170 SER C O     1 
ATOM   12368 C  CB    . SER C 2 191 ? 109.969 92.240  114.771 1.00 24.56 ?  170 SER C CB    1 
ATOM   12369 O  OG    . SER C 2 191 ? 110.528 92.318  116.067 1.00 24.98 ?  170 SER C OG    1 
ATOM   12370 N  N     . GLY C 2 192 ? 111.494 95.120  115.118 1.00 24.32 ?  171 GLY C N     1 
ATOM   12371 C  CA    . GLY C 2 192 ? 111.609 96.472  115.648 1.00 23.97 ?  171 GLY C CA    1 
ATOM   12372 C  C     . GLY C 2 192 ? 112.117 97.484  114.635 1.00 23.85 ?  171 GLY C C     1 
ATOM   12373 O  O     . GLY C 2 192 ? 111.492 98.530  114.460 1.00 23.99 ?  171 GLY C O     1 
ATOM   12374 N  N     . PHE C 2 193 ? 113.225 97.171  113.960 1.00 23.28 ?  172 PHE C N     1 
ATOM   12375 C  CA    . PHE C 2 193 ? 113.817 98.070  112.952 1.00 23.85 ?  172 PHE C CA    1 
ATOM   12376 C  C     . PHE C 2 193 ? 112.870 98.445  111.810 1.00 23.72 ?  172 PHE C C     1 
ATOM   12377 O  O     . PHE C 2 193 ? 113.018 99.513  111.219 1.00 23.92 ?  172 PHE C O     1 
ATOM   12378 C  CB    . PHE C 2 193 ? 115.081 97.473  112.320 1.00 23.47 ?  172 PHE C CB    1 
ATOM   12379 C  CG    . PHE C 2 193 ? 116.295 97.479  113.223 1.00 24.32 ?  172 PHE C CG    1 
ATOM   12380 C  CD1   . PHE C 2 193 ? 116.410 98.387  114.276 1.00 22.28 ?  172 PHE C CD1   1 
ATOM   12381 C  CD2   . PHE C 2 193 ? 117.340 96.583  112.991 1.00 23.82 ?  172 PHE C CD2   1 
ATOM   12382 C  CE1   . PHE C 2 193 ? 117.536 98.392  115.109 1.00 23.41 ?  172 PHE C CE1   1 
ATOM   12383 C  CE2   . PHE C 2 193 ? 118.480 96.573  113.815 1.00 24.70 ?  172 PHE C CE2   1 
ATOM   12384 C  CZ    . PHE C 2 193 ? 118.579 97.486  114.877 1.00 24.87 ?  172 PHE C CZ    1 
ATOM   12385 N  N     . TYR C 2 194 ? 111.928 97.558  111.484 1.00 23.31 ?  173 TYR C N     1 
ATOM   12386 C  CA    . TYR C 2 194 ? 111.026 97.771  110.350 1.00 23.26 ?  173 TYR C CA    1 
ATOM   12387 C  C     . TYR C 2 194 ? 110.387 99.162  110.382 1.00 23.04 ?  173 TYR C C     1 
ATOM   12388 O  O     . TYR C 2 194 ? 110.361 99.867  109.369 1.00 23.47 ?  173 TYR C O     1 
ATOM   12389 C  CB    . TYR C 2 194 ? 109.920 96.703  110.288 1.00 23.13 ?  173 TYR C CB    1 
ATOM   12390 C  CG    . TYR C 2 194 ? 109.027 96.832  109.060 1.00 24.10 ?  173 TYR C CG    1 
ATOM   12391 C  CD1   . TYR C 2 194 ? 109.297 96.098  107.904 1.00 25.72 ?  173 TYR C CD1   1 
ATOM   12392 C  CD2   . TYR C 2 194 ? 107.935 97.701  109.047 1.00 27.04 ?  173 TYR C CD2   1 
ATOM   12393 C  CE1   . TYR C 2 194 ? 108.485 96.212  106.767 1.00 28.94 ?  173 TYR C CE1   1 
ATOM   12394 C  CE2   . TYR C 2 194 ? 107.120 97.831  107.907 1.00 27.84 ?  173 TYR C CE2   1 
ATOM   12395 C  CZ    . TYR C 2 194 ? 107.407 97.082  106.777 1.00 29.97 ?  173 TYR C CZ    1 
ATOM   12396 O  OH    . TYR C 2 194 ? 106.624 97.200  105.643 1.00 34.34 ?  173 TYR C OH    1 
ATOM   12397 N  N     . TYR C 2 195 ? 109.872 99.542  111.541 1.00 22.51 ?  174 TYR C N     1 
ATOM   12398 C  CA    . TYR C 2 195 ? 109.001 100.709 111.633 1.00 22.60 ?  174 TYR C CA    1 
ATOM   12399 C  C     . TYR C 2 195 ? 109.751 102.047 111.497 1.00 22.64 ?  174 TYR C C     1 
ATOM   12400 O  O     . TYR C 2 195 ? 109.312 102.900 110.717 1.00 22.39 ?  174 TYR C O     1 
ATOM   12401 C  CB    . TYR C 2 195 ? 108.139 100.634 112.893 1.00 22.32 ?  174 TYR C CB    1 
ATOM   12402 C  CG    . TYR C 2 195 ? 106.779 101.293 112.774 1.00 23.39 ?  174 TYR C CG    1 
ATOM   12403 C  CD1   . TYR C 2 195 ? 106.081 101.318 111.556 1.00 22.84 ?  174 TYR C CD1   1 
ATOM   12404 C  CD2   . TYR C 2 195 ? 106.173 101.858 113.894 1.00 22.23 ?  174 TYR C CD2   1 
ATOM   12405 C  CE1   . TYR C 2 195 ? 104.820 101.920 111.461 1.00 24.05 ?  174 TYR C CE1   1 
ATOM   12406 C  CE2   . TYR C 2 195 ? 104.910 102.448 113.814 1.00 24.11 ?  174 TYR C CE2   1 
ATOM   12407 C  CZ    . TYR C 2 195 ? 104.243 102.473 112.601 1.00 23.92 ?  174 TYR C CZ    1 
ATOM   12408 O  OH    . TYR C 2 195 ? 103.016 103.076 112.533 1.00 25.00 ?  174 TYR C OH    1 
ATOM   12409 N  N     . PRO C 2 196 ? 110.888 102.229 112.232 1.00 22.25 ?  175 PRO C N     1 
ATOM   12410 C  CA    . PRO C 2 196 ? 111.704 103.426 111.971 1.00 22.45 ?  175 PRO C CA    1 
ATOM   12411 C  C     . PRO C 2 196 ? 112.170 103.524 110.518 1.00 22.59 ?  175 PRO C C     1 
ATOM   12412 O  O     . PRO C 2 196 ? 112.201 104.630 109.966 1.00 22.19 ?  175 PRO C O     1 
ATOM   12413 C  CB    . PRO C 2 196 ? 112.914 103.264 112.904 1.00 22.25 ?  175 PRO C CB    1 
ATOM   12414 C  CG    . PRO C 2 196 ? 112.476 102.316 113.971 1.00 22.22 ?  175 PRO C CG    1 
ATOM   12415 C  CD    . PRO C 2 196 ? 111.434 101.422 113.347 1.00 22.32 ?  175 PRO C CD    1 
ATOM   12416 N  N     . LEU C 2 197 ? 112.514 102.386 109.906 1.00 21.92 ?  176 LEU C N     1 
ATOM   12417 C  CA    . LEU C 2 197 ? 112.930 102.368 108.502 1.00 22.35 ?  176 LEU C CA    1 
ATOM   12418 C  C     . LEU C 2 197 ? 111.766 102.722 107.570 1.00 22.60 ?  176 LEU C C     1 
ATOM   12419 O  O     . LEU C 2 197 ? 111.943 103.427 106.573 1.00 22.41 ?  176 LEU C O     1 
ATOM   12420 C  CB    . LEU C 2 197 ? 113.500 101.008 108.106 1.00 22.69 ?  176 LEU C CB    1 
ATOM   12421 C  CG    . LEU C 2 197 ? 114.791 100.487 108.752 1.00 23.68 ?  176 LEU C CG    1 
ATOM   12422 C  CD1   . LEU C 2 197 ? 115.116 99.091  108.196 1.00 23.70 ?  176 LEU C CD1   1 
ATOM   12423 C  CD2   . LEU C 2 197 ? 115.953 101.446 108.512 1.00 23.09 ?  176 LEU C CD2   1 
ATOM   12424 N  N     . TYR C 2 198 ? 110.580 102.224 107.911 1.00 22.64 ?  177 TYR C N     1 
ATOM   12425 C  CA    . TYR C 2 198 ? 109.370 102.467 107.137 1.00 22.92 ?  177 TYR C CA    1 
ATOM   12426 C  C     . TYR C 2 198 ? 109.063 103.976 107.113 1.00 23.68 ?  177 TYR C C     1 
ATOM   12427 O  O     . TYR C 2 198 ? 108.738 104.537 106.064 1.00 23.81 ?  177 TYR C O     1 
ATOM   12428 C  CB    . TYR C 2 198 ? 108.234 101.656 107.752 1.00 22.73 ?  177 TYR C CB    1 
ATOM   12429 C  CG    . TYR C 2 198 ? 106.871 101.795 107.130 1.00 22.91 ?  177 TYR C CG    1 
ATOM   12430 C  CD1   . TYR C 2 198 ? 106.577 101.186 105.910 1.00 23.49 ?  177 TYR C CD1   1 
ATOM   12431 C  CD2   . TYR C 2 198 ? 105.854 102.482 107.795 1.00 21.97 ?  177 TYR C CD2   1 
ATOM   12432 C  CE1   . TYR C 2 198 ? 105.306 101.286 105.343 1.00 23.57 ?  177 TYR C CE1   1 
ATOM   12433 C  CE2   . TYR C 2 198 ? 104.568 102.586 107.237 1.00 22.54 ?  177 TYR C CE2   1 
ATOM   12434 C  CZ    . TYR C 2 198 ? 104.308 101.990 106.012 1.00 22.88 ?  177 TYR C CZ    1 
ATOM   12435 O  OH    . TYR C 2 198 ? 103.049 102.070 105.448 1.00 23.17 ?  177 TYR C OH    1 
ATOM   12436 N  N     . PHE C 2 199 ? 109.212 104.636 108.256 1.00 23.50 ?  178 PHE C N     1 
ATOM   12437 C  CA    . PHE C 2 199 ? 109.038 106.088 108.310 1.00 24.60 ?  178 PHE C CA    1 
ATOM   12438 C  C     . PHE C 2 199 ? 110.152 106.883 107.615 1.00 24.72 ?  178 PHE C C     1 
ATOM   12439 O  O     . PHE C 2 199 ? 109.877 107.807 106.851 1.00 24.19 ?  178 PHE C O     1 
ATOM   12440 C  CB    . PHE C 2 199 ? 108.850 106.557 109.755 1.00 24.35 ?  178 PHE C CB    1 
ATOM   12441 C  CG    . PHE C 2 199 ? 107.487 106.264 110.305 1.00 26.36 ?  178 PHE C CG    1 
ATOM   12442 C  CD1   . PHE C 2 199 ? 106.343 106.530 109.552 1.00 28.53 ?  178 PHE C CD1   1 
ATOM   12443 C  CD2   . PHE C 2 199 ? 107.335 105.739 111.580 1.00 28.23 ?  178 PHE C CD2   1 
ATOM   12444 C  CE1   . PHE C 2 199 ? 105.070 106.253 110.060 1.00 29.37 ?  178 PHE C CE1   1 
ATOM   12445 C  CE2   . PHE C 2 199 ? 106.057 105.470 112.100 1.00 28.69 ?  178 PHE C CE2   1 
ATOM   12446 C  CZ    . PHE C 2 199 ? 104.934 105.725 111.341 1.00 28.43 ?  178 PHE C CZ    1 
ATOM   12447 N  N     . TYR C 2 200 ? 111.402 106.510 107.883 1.00 25.36 ?  179 TYR C N     1 
ATOM   12448 C  CA    . TYR C 2 200 ? 112.570 107.136 107.252 1.00 26.02 ?  179 TYR C CA    1 
ATOM   12449 C  C     . TYR C 2 200 ? 112.401 107.157 105.732 1.00 26.57 ?  179 TYR C C     1 
ATOM   12450 O  O     . TYR C 2 200 ? 112.642 108.177 105.078 1.00 26.30 ?  179 TYR C O     1 
ATOM   12451 C  CB    . TYR C 2 200 ? 113.844 106.362 107.619 1.00 26.19 ?  179 TYR C CB    1 
ATOM   12452 C  CG    . TYR C 2 200 ? 115.134 107.035 107.207 1.00 27.82 ?  179 TYR C CG    1 
ATOM   12453 C  CD1   . TYR C 2 200 ? 115.825 106.619 106.064 1.00 30.77 ?  179 TYR C CD1   1 
ATOM   12454 C  CD2   . TYR C 2 200 ? 115.672 108.080 107.961 1.00 29.20 ?  179 TYR C CD2   1 
ATOM   12455 C  CE1   . TYR C 2 200 ? 117.013 107.231 105.681 1.00 31.82 ?  179 TYR C CE1   1 
ATOM   12456 C  CE2   . TYR C 2 200 ? 116.856 108.701 107.589 1.00 30.44 ?  179 TYR C CE2   1 
ATOM   12457 C  CZ    . TYR C 2 200 ? 117.522 108.269 106.445 1.00 32.74 ?  179 TYR C CZ    1 
ATOM   12458 O  OH    . TYR C 2 200 ? 118.690 108.876 106.056 1.00 34.58 ?  179 TYR C OH    1 
ATOM   12459 N  N     . GLY C 2 201 ? 111.956 106.026 105.188 1.00 26.71 ?  180 GLY C N     1 
ATOM   12460 C  CA    . GLY C 2 201 ? 111.749 105.876 103.755 1.00 27.38 ?  180 GLY C CA    1 
ATOM   12461 C  C     . GLY C 2 201 ? 110.658 106.759 103.170 1.00 27.62 ?  180 GLY C C     1 
ATOM   12462 O  O     . GLY C 2 201 ? 110.627 106.961 101.968 1.00 28.25 ?  180 GLY C O     1 
ATOM   12463 N  N     . GLN C 2 202 ? 109.774 107.282 104.020 1.00 27.60 ?  181 GLN C N     1 
ATOM   12464 C  CA    . GLN C 2 202 ? 108.709 108.207 103.598 1.00 28.24 ?  181 GLN C CA    1 
ATOM   12465 C  C     . GLN C 2 202 ? 109.056 109.651 103.926 1.00 28.30 ?  181 GLN C C     1 
ATOM   12466 O  O     . GLN C 2 202 ? 108.217 110.539 103.757 1.00 27.98 ?  181 GLN C O     1 
ATOM   12467 C  CB    . GLN C 2 202 ? 107.393 107.900 104.318 1.00 27.90 ?  181 GLN C CB    1 
ATOM   12468 C  CG    . GLN C 2 202 ? 106.810 106.546 104.071 1.00 29.54 ?  181 GLN C CG    1 
ATOM   12469 C  CD    . GLN C 2 202 ? 105.586 106.305 104.925 1.00 31.54 ?  181 GLN C CD    1 
ATOM   12470 O  OE1   . GLN C 2 202 ? 104.534 106.916 104.714 1.00 32.11 ?  181 GLN C OE1   1 
ATOM   12471 N  NE2   . GLN C 2 202 ? 105.715 105.420 105.904 1.00 31.29 ?  181 GLN C NE2   1 
ATOM   12472 N  N     . GLY C 2 203 ? 110.266 109.871 104.439 1.00 28.14 ?  182 GLY C N     1 
ATOM   12473 C  CA    . GLY C 2 203 ? 110.716 111.194 104.842 1.00 28.38 ?  182 GLY C CA    1 
ATOM   12474 C  C     . GLY C 2 203 ? 110.124 111.645 106.161 1.00 28.71 ?  182 GLY C C     1 
ATOM   12475 O  O     . GLY C 2 203 ? 109.926 112.837 106.373 1.00 28.80 ?  182 GLY C O     1 
ATOM   12476 N  N     . LYS C 2 204 ? 109.828 110.687 107.038 1.00 28.24 ?  183 LYS C N     1 
ATOM   12477 C  CA    . LYS C 2 204 ? 109.239 110.979 108.335 1.00 28.48 ?  183 LYS C CA    1 
ATOM   12478 C  C     . LYS C 2 204 ? 110.136 110.458 109.454 1.00 27.82 ?  183 LYS C C     1 
ATOM   12479 O  O     . LYS C 2 204 ? 110.759 109.395 109.322 1.00 26.73 ?  183 LYS C O     1 
ATOM   12480 C  CB    . LYS C 2 204 ? 107.843 110.364 108.451 1.00 29.13 ?  183 LYS C CB    1 
ATOM   12481 C  CG    . LYS C 2 204 ? 106.814 110.962 107.492 1.00 30.41 ?  183 LYS C CG    1 
ATOM   12482 C  CD    . LYS C 2 204 ? 105.669 109.991 107.249 1.00 33.74 ?  183 LYS C CD    1 
ATOM   12483 C  CE    . LYS C 2 204 ? 104.594 110.620 106.348 1.00 36.26 ?  183 LYS C CE    1 
ATOM   12484 N  NZ    . LYS C 2 204 ? 103.461 109.670 106.145 1.00 39.17 1  183 LYS C NZ    1 
ATOM   12485 N  N     . LEU C 2 205 ? 110.191 111.214 110.549 1.00 27.77 ?  184 LEU C N     1 
ATOM   12486 C  CA    . LEU C 2 205 ? 111.025 110.878 111.710 1.00 27.79 ?  184 LEU C CA    1 
ATOM   12487 C  C     . LEU C 2 205 ? 112.466 110.571 111.294 1.00 27.85 ?  184 LEU C C     1 
ATOM   12488 O  O     . LEU C 2 205 ? 113.051 109.544 111.665 1.00 27.07 ?  184 LEU C O     1 
ATOM   12489 C  CB    . LEU C 2 205 ? 110.406 109.713 112.510 1.00 27.76 ?  184 LEU C CB    1 
ATOM   12490 C  CG    . LEU C 2 205 ? 108.967 109.929 112.995 1.00 28.62 ?  184 LEU C CG    1 
ATOM   12491 C  CD1   . LEU C 2 205 ? 108.421 108.676 113.652 1.00 29.18 ?  184 LEU C CD1   1 
ATOM   12492 C  CD2   . LEU C 2 205 ? 108.878 111.108 113.954 1.00 28.43 ?  184 LEU C CD2   1 
ATOM   12493 N  N     . MET C 2 206 ? 113.049 111.483 110.530 1.00 28.15 ?  185 MET C N     1 
ATOM   12494 C  CA    . MET C 2 206 ? 114.316 111.190 109.899 1.00 28.80 ?  185 MET C CA    1 
ATOM   12495 C  C     . MET C 2 206 ? 115.529 111.295 110.814 1.00 28.77 ?  185 MET C C     1 
ATOM   12496 O  O     . MET C 2 206 ? 116.546 110.657 110.548 1.00 28.79 ?  185 MET C O     1 
ATOM   12497 C  CB    . MET C 2 206 ? 114.468 112.017 108.636 1.00 29.96 ?  185 MET C CB    1 
ATOM   12498 C  CG    . MET C 2 206 ? 113.462 111.584 107.565 1.00 31.23 ?  185 MET C CG    1 
ATOM   12499 S  SD    . MET C 2 206 ? 113.971 112.163 105.969 1.00 40.10 ?  185 MET C SD    1 
ATOM   12500 C  CE    . MET C 2 206 ? 115.358 111.101 105.617 1.00 35.10 ?  185 MET C CE    1 
ATOM   12501 N  N     . GLN C 2 207 ? 115.420 112.062 111.893 1.00 28.62 ?  186 GLN C N     1 
ATOM   12502 C  CA    . GLN C 2 207 ? 116.522 112.169 112.856 1.00 29.10 ?  186 GLN C CA    1 
ATOM   12503 C  C     . GLN C 2 207 ? 116.613 110.906 113.717 1.00 28.52 ?  186 GLN C C     1 
ATOM   12504 O  O     . GLN C 2 207 ? 117.695 110.339 113.858 1.00 28.28 ?  186 GLN C O     1 
ATOM   12505 C  CB    . GLN C 2 207 ? 116.403 113.426 113.723 1.00 29.21 ?  186 GLN C CB    1 
ATOM   12506 C  CG    . GLN C 2 207 ? 116.499 114.737 112.940 1.00 31.41 ?  186 GLN C CG    1 
ATOM   12507 C  CD    . GLN C 2 207 ? 117.857 114.931 112.297 1.00 34.70 ?  186 GLN C CD    1 
ATOM   12508 O  OE1   . GLN C 2 207 ? 118.071 114.546 111.151 1.00 37.69 ?  186 GLN C OE1   1 
ATOM   12509 N  NE2   . GLN C 2 207 ? 118.794 115.503 113.045 1.00 34.75 ?  186 GLN C NE2   1 
ATOM   12510 N  N     . SER C 2 208 ? 115.475 110.479 114.277 1.00 28.38 ?  187 SER C N     1 
ATOM   12511 C  CA    . SER C 2 208 ? 115.356 109.181 114.955 1.00 28.25 ?  187 SER C CA    1 
ATOM   12512 C  C     . SER C 2 208 ? 115.797 108.068 114.013 1.00 28.00 ?  187 SER C C     1 
ATOM   12513 O  O     . SER C 2 208 ? 116.496 107.142 114.425 1.00 27.90 ?  187 SER C O     1 
ATOM   12514 C  CB    . SER C 2 208 ? 113.907 108.911 115.365 1.00 27.88 ?  187 SER C CB    1 
ATOM   12515 O  OG    . SER C 2 208 ? 113.433 109.875 116.281 1.00 30.27 ?  187 SER C OG    1 
ATOM   12516 N  N     . GLY C 2 209 ? 115.367 108.168 112.751 1.00 27.31 ?  188 GLY C N     1 
ATOM   12517 C  CA    . GLY C 2 209 ? 115.718 107.201 111.714 1.00 27.86 ?  188 GLY C CA    1 
ATOM   12518 C  C     . GLY C 2 209 ? 117.208 107.123 111.439 1.00 27.96 ?  188 GLY C C     1 
ATOM   12519 O  O     . GLY C 2 209 ? 117.737 106.041 111.157 1.00 27.84 ?  188 GLY C O     1 
ATOM   12520 N  N     . GLU C 2 210 ? 117.884 108.269 111.518 1.00 28.21 ?  189 GLU C N     1 
ATOM   12521 C  CA    . GLU C 2 210 ? 119.334 108.325 111.359 1.00 29.15 ?  189 GLU C CA    1 
ATOM   12522 C  C     . GLU C 2 210 ? 120.039 107.542 112.486 1.00 28.02 ?  189 GLU C C     1 
ATOM   12523 O  O     . GLU C 2 210 ? 120.987 106.793 112.243 1.00 27.15 ?  189 GLU C O     1 
ATOM   12524 C  CB    . GLU C 2 210 ? 119.804 109.782 111.330 1.00 30.17 ?  189 GLU C CB    1 
ATOM   12525 C  CG    . GLU C 2 210 ? 120.720 110.121 110.165 1.00 35.68 ?  189 GLU C CG    1 
ATOM   12526 C  CD    . GLU C 2 210 ? 119.962 110.327 108.850 1.00 40.25 ?  189 GLU C CD    1 
ATOM   12527 O  OE1   . GLU C 2 210 ? 119.122 111.254 108.753 1.00 42.98 ?  189 GLU C OE1   1 
ATOM   12528 O  OE2   . GLU C 2 210 ? 120.215 109.564 107.899 1.00 43.59 -1 189 GLU C OE2   1 
ATOM   12529 N  N     . ILE C 2 211 ? 119.566 107.721 113.716 1.00 27.57 ?  190 ILE C N     1 
ATOM   12530 C  CA    . ILE C 2 211 ? 120.065 106.947 114.858 1.00 27.47 ?  190 ILE C CA    1 
ATOM   12531 C  C     . ILE C 2 211 ? 119.892 105.441 114.628 1.00 26.69 ?  190 ILE C C     1 
ATOM   12532 O  O     . ILE C 2 211 ? 120.839 104.657 114.769 1.00 26.56 ?  190 ILE C O     1 
ATOM   12533 C  CB    . ILE C 2 211 ? 119.389 107.399 116.186 1.00 27.84 ?  190 ILE C CB    1 
ATOM   12534 C  CG1   . ILE C 2 211 ? 119.901 108.793 116.581 1.00 28.56 ?  190 ILE C CG1   1 
ATOM   12535 C  CG2   . ILE C 2 211 ? 119.628 106.358 117.304 1.00 27.27 ?  190 ILE C CG2   1 
ATOM   12536 C  CD1   . ILE C 2 211 ? 119.347 109.322 117.899 1.00 30.09 ?  190 ILE C CD1   1 
ATOM   12537 N  N     . ILE C 2 212 ? 118.686 105.052 114.233 1.00 26.33 ?  191 ILE C N     1 
ATOM   12538 C  CA    . ILE C 2 212 ? 118.358 103.651 113.986 1.00 25.96 ?  191 ILE C CA    1 
ATOM   12539 C  C     . ILE C 2 212 ? 119.239 103.034 112.891 1.00 25.46 ?  191 ILE C C     1 
ATOM   12540 O  O     . ILE C 2 212 ? 119.678 101.895 113.031 1.00 24.84 ?  191 ILE C O     1 
ATOM   12541 C  CB    . ILE C 2 212 ? 116.840 103.470 113.676 1.00 26.00 ?  191 ILE C CB    1 
ATOM   12542 C  CG1   . ILE C 2 212 ? 115.992 103.835 114.906 1.00 27.16 ?  191 ILE C CG1   1 
ATOM   12543 C  CG2   . ILE C 2 212 ? 116.520 102.056 113.209 1.00 26.87 ?  191 ILE C CG2   1 
ATOM   12544 C  CD1   . ILE C 2 212 ? 116.206 102.949 116.120 1.00 29.84 ?  191 ILE C CD1   1 
ATOM   12545 N  N     . ASN C 2 213 ? 119.496 103.782 111.814 1.00 25.35 ?  192 ASN C N     1 
ATOM   12546 C  CA    . ASN C 2 213 ? 120.387 103.315 110.746 1.00 25.60 ?  192 ASN C CA    1 
ATOM   12547 C  C     . ASN C 2 213 ? 121.815 103.086 111.229 1.00 25.14 ?  192 ASN C C     1 
ATOM   12548 O  O     . ASN C 2 213 ? 122.492 102.143 110.791 1.00 25.61 ?  192 ASN C O     1 
ATOM   12549 C  CB    . ASN C 2 213 ? 120.393 104.283 109.555 1.00 26.55 ?  192 ASN C CB    1 
ATOM   12550 C  CG    . ASN C 2 213 ? 119.285 103.994 108.567 1.00 28.10 ?  192 ASN C CG    1 
ATOM   12551 O  OD1   . ASN C 2 213 ? 119.240 102.923 107.953 1.00 31.67 ?  192 ASN C OD1   1 
ATOM   12552 N  ND2   . ASN C 2 213 ? 118.389 104.950 108.396 1.00 30.36 ?  192 ASN C ND2   1 
ATOM   12553 N  N     . LEU C 2 214 ? 122.273 103.943 112.133 1.00 24.54 ?  193 LEU C N     1 
ATOM   12554 C  CA    . LEU C 2 214 ? 123.593 103.759 112.741 1.00 24.40 ?  193 LEU C CA    1 
ATOM   12555 C  C     . LEU C 2 214 ? 123.628 102.501 113.611 1.00 23.55 ?  193 LEU C C     1 
ATOM   12556 O  O     . LEU C 2 214 ? 124.578 101.718 113.532 1.00 23.09 ?  193 LEU C O     1 
ATOM   12557 C  CB    . LEU C 2 214 ? 124.022 105.005 113.512 1.00 24.00 ?  193 LEU C CB    1 
ATOM   12558 C  CG    . LEU C 2 214 ? 124.403 106.226 112.647 1.00 25.69 ?  193 LEU C CG    1 
ATOM   12559 C  CD1   . LEU C 2 214 ? 124.532 107.495 113.490 1.00 26.28 ?  193 LEU C CD1   1 
ATOM   12560 C  CD2   . LEU C 2 214 ? 125.702 105.992 111.872 1.00 26.05 ?  193 LEU C CD2   1 
ATOM   12561 N  N     . ILE C 2 215 ? 122.587 102.307 114.425 1.00 23.19 ?  194 ILE C N     1 
ATOM   12562 C  CA    . ILE C 2 215 ? 122.431 101.081 115.216 1.00 22.88 ?  194 ILE C CA    1 
ATOM   12563 C  C     . ILE C 2 215 ? 122.425 99.860  114.282 1.00 23.81 ?  194 ILE C C     1 
ATOM   12564 O  O     . ILE C 2 215 ? 123.146 98.890  114.521 1.00 23.83 ?  194 ILE C O     1 
ATOM   12565 C  CB    . ILE C 2 215 ? 121.147 101.111 116.093 1.00 22.92 ?  194 ILE C CB    1 
ATOM   12566 C  CG1   . ILE C 2 215 ? 121.199 102.272 117.087 1.00 21.11 ?  194 ILE C CG1   1 
ATOM   12567 C  CG2   . ILE C 2 215 ? 120.930 99.778  116.826 1.00 21.89 ?  194 ILE C CG2   1 
ATOM   12568 C  CD1   . ILE C 2 215 ? 119.972 102.394 117.968 1.00 22.26 ?  194 ILE C CD1   1 
ATOM   12569 N  N     . LEU C 2 216 ? 121.650 99.925  113.200 1.00 24.23 ?  195 LEU C N     1 
ATOM   12570 C  CA    . LEU C 2 216 ? 121.534 98.791  112.274 1.00 25.41 ?  195 LEU C CA    1 
ATOM   12571 C  C     . LEU C 2 216 ? 122.866 98.471  111.593 1.00 25.63 ?  195 LEU C C     1 
ATOM   12572 O  O     . LEU C 2 216 ? 123.238 97.295  111.459 1.00 25.46 ?  195 LEU C O     1 
ATOM   12573 C  CB    . LEU C 2 216 ? 120.430 99.046  111.231 1.00 26.03 ?  195 LEU C CB    1 
ATOM   12574 C  CG    . LEU C 2 216 ? 120.083 97.979  110.183 1.00 28.00 ?  195 LEU C CG    1 
ATOM   12575 C  CD1   . LEU C 2 216 ? 118.680 98.241  109.661 1.00 31.45 ?  195 LEU C CD1   1 
ATOM   12576 C  CD2   . LEU C 2 216 ? 121.090 97.943  109.028 1.00 29.83 ?  195 LEU C CD2   1 
ATOM   12577 N  N     . ARG C 2 217 ? 123.577 99.514  111.175 1.00 25.98 ?  196 ARG C N     1 
ATOM   12578 C  CA    . ARG C 2 217 ? 124.911 99.370  110.600 1.00 26.73 ?  196 ARG C CA    1 
ATOM   12579 C  C     . ARG C 2 217 ? 125.852 98.612  111.569 1.00 25.95 ?  196 ARG C C     1 
ATOM   12580 O  O     . ARG C 2 217 ? 126.581 97.714  111.133 1.00 25.75 ?  196 ARG C O     1 
ATOM   12581 C  CB    . ARG C 2 217 ? 125.479 100.747 110.246 1.00 27.29 ?  196 ARG C CB    1 
ATOM   12582 C  CG    . ARG C 2 217 ? 126.750 100.738 109.386 1.00 30.12 ?  196 ARG C CG    1 
ATOM   12583 C  CD    . ARG C 2 217 ? 127.596 101.953 109.718 1.00 35.40 ?  196 ARG C CD    1 
ATOM   12584 N  NE    . ARG C 2 217 ? 127.651 102.098 111.174 1.00 39.87 ?  196 ARG C NE    1 
ATOM   12585 C  CZ    . ARG C 2 217 ? 128.100 103.156 111.837 1.00 40.55 ?  196 ARG C CZ    1 
ATOM   12586 N  NH1   . ARG C 2 217 ? 128.569 104.224 111.193 1.00 40.77 1  196 ARG C NH1   1 
ATOM   12587 N  NH2   . ARG C 2 217 ? 128.068 103.134 113.164 1.00 41.10 ?  196 ARG C NH2   1 
ATOM   12588 N  N     . ASP C 2 218 ? 125.815 98.964  112.859 1.00 24.70 ?  197 ASP C N     1 
ATOM   12589 C  CA    . ASP C 2 218 ? 126.574 98.245  113.902 1.00 24.55 ?  197 ASP C CA    1 
ATOM   12590 C  C     . ASP C 2 218 ? 126.134 96.772  114.025 1.00 24.23 ?  197 ASP C C     1 
ATOM   12591 O  O     . ASP C 2 218 ? 126.978 95.872  113.995 1.00 23.69 ?  197 ASP C O     1 
ATOM   12592 C  CB    . ASP C 2 218 ? 126.464 98.917  115.287 1.00 24.50 ?  197 ASP C CB    1 
ATOM   12593 C  CG    . ASP C 2 218 ? 127.134 100.300 115.361 1.00 25.84 ?  197 ASP C CG    1 
ATOM   12594 O  OD1   . ASP C 2 218 ? 128.058 100.606 114.575 1.00 26.91 ?  197 ASP C OD1   1 
ATOM   12595 O  OD2   . ASP C 2 218 ? 126.739 101.088 116.243 1.00 25.72 -1 197 ASP C OD2   1 
ATOM   12596 N  N     . GLU C 2 219 ? 124.825 96.524  114.136 1.00 23.92 ?  198 GLU C N     1 
ATOM   12597 C  CA    . GLU C 2 219 ? 124.357 95.147  114.367 1.00 24.20 ?  198 GLU C CA    1 
ATOM   12598 C  C     . GLU C 2 219 ? 124.717 94.232  113.211 1.00 24.02 ?  198 GLU C C     1 
ATOM   12599 O  O     . GLU C 2 219 ? 125.014 93.064  113.435 1.00 24.24 ?  198 GLU C O     1 
ATOM   12600 C  CB    . GLU C 2 219 ? 122.854 95.049  114.642 1.00 24.05 ?  198 GLU C CB    1 
ATOM   12601 C  CG    . GLU C 2 219 ? 122.241 96.133  115.509 1.00 25.03 ?  198 GLU C CG    1 
ATOM   12602 C  CD    . GLU C 2 219 ? 122.607 96.100  117.006 1.00 26.31 ?  198 GLU C CD    1 
ATOM   12603 O  OE1   . GLU C 2 219 ? 123.672 95.556  117.422 1.00 27.65 ?  198 GLU C OE1   1 
ATOM   12604 O  OE2   . GLU C 2 219 ? 121.796 96.677  117.781 1.00 26.87 -1 198 GLU C OE2   1 
ATOM   12605 N  N     . ALA C 2 220 ? 124.688 94.756  111.984 1.00 24.00 ?  199 ALA C N     1 
ATOM   12606 C  CA    . ALA C 2 220 ? 125.062 93.970  110.814 1.00 24.72 ?  199 ALA C CA    1 
ATOM   12607 C  C     . ALA C 2 220 ? 126.492 93.416  110.926 1.00 24.80 ?  199 ALA C C     1 
ATOM   12608 O  O     . ALA C 2 220 ? 126.721 92.233  110.656 1.00 25.04 ?  199 ALA C O     1 
ATOM   12609 C  CB    . ALA C 2 220 ? 124.884 94.783  109.507 1.00 24.66 ?  199 ALA C CB    1 
ATOM   12610 N  N     . ILE C 2 221 ? 127.440 94.258  111.332 1.00 24.85 ?  200 ILE C N     1 
ATOM   12611 C  CA    . ILE C 2 221 ? 128.830 93.804  111.517 1.00 25.07 ?  200 ILE C CA    1 
ATOM   12612 C  C     . ILE C 2 221 ? 128.998 92.932  112.771 1.00 23.86 ?  200 ILE C C     1 
ATOM   12613 O  O     . ILE C 2 221 ? 129.814 92.007  112.770 1.00 23.72 ?  200 ILE C O     1 
ATOM   12614 C  CB    . ILE C 2 221 ? 129.893 94.960  111.469 1.00 25.71 ?  200 ILE C CB    1 
ATOM   12615 C  CG1   . ILE C 2 221 ? 129.856 95.819  112.737 1.00 27.10 ?  200 ILE C CG1   1 
ATOM   12616 C  CG2   . ILE C 2 221 ? 129.737 95.794  110.182 1.00 27.18 ?  200 ILE C CG2   1 
ATOM   12617 C  CD1   . ILE C 2 221 ? 130.987 96.848  112.856 1.00 29.63 ?  200 ILE C CD1   1 
ATOM   12618 N  N     . HIS C 2 222 ? 128.222 93.214  113.819 1.00 22.79 ?  201 HIS C N     1 
ATOM   12619 C  CA    . HIS C 2 222 ? 128.218 92.364  115.031 1.00 22.48 ?  201 HIS C CA    1 
ATOM   12620 C  C     . HIS C 2 222 ? 127.750 90.945  114.712 1.00 22.04 ?  201 HIS C C     1 
ATOM   12621 O  O     . HIS C 2 222 ? 128.334 89.984  115.197 1.00 22.06 ?  201 HIS C O     1 
ATOM   12622 C  CB    . HIS C 2 222 ? 127.288 92.910  116.116 1.00 21.77 ?  201 HIS C CB    1 
ATOM   12623 C  CG    . HIS C 2 222 ? 127.709 94.218  116.697 1.00 21.76 ?  201 HIS C CG    1 
ATOM   12624 N  ND1   . HIS C 2 222 ? 127.044 94.798  117.754 1.00 20.70 ?  201 HIS C ND1   1 
ATOM   12625 C  CD2   . HIS C 2 222 ? 128.721 95.059  116.382 1.00 22.07 ?  201 HIS C CD2   1 
ATOM   12626 C  CE1   . HIS C 2 222 ? 127.620 95.945  118.060 1.00 22.26 ?  201 HIS C CE1   1 
ATOM   12627 N  NE2   . HIS C 2 222 ? 128.634 96.131  117.237 1.00 22.52 ?  201 HIS C NE2   1 
ATOM   12628 N  N     . GLY C 2 223 ? 126.675 90.830  113.932 1.00 22.35 ?  202 GLY C N     1 
ATOM   12629 C  CA    . GLY C 2 223 ? 126.136 89.529  113.503 1.00 22.01 ?  202 GLY C CA    1 
ATOM   12630 C  C     . GLY C 2 223 ? 127.100 88.732  112.628 1.00 22.73 ?  202 GLY C C     1 
ATOM   12631 O  O     . GLY C 2 223 ? 127.222 87.505  112.776 1.00 21.99 ?  202 GLY C O     1 
ATOM   12632 N  N     . VAL C 2 224 ? 127.794 89.422  111.720 1.00 22.45 ?  203 VAL C N     1 
ATOM   12633 C  CA    . VAL C 2 224 ? 128.804 88.767  110.887 1.00 22.54 ?  203 VAL C CA    1 
ATOM   12634 C  C     . VAL C 2 224 ? 129.959 88.245  111.745 1.00 22.28 ?  203 VAL C C     1 
ATOM   12635 O  O     . VAL C 2 224 ? 130.335 87.081  111.639 1.00 22.44 ?  203 VAL C O     1 
ATOM   12636 C  CB    . VAL C 2 224 ? 129.349 89.698  109.751 1.00 23.00 ?  203 VAL C CB    1 
ATOM   12637 C  CG1   . VAL C 2 224 ? 130.553 89.046  109.047 1.00 23.10 ?  203 VAL C CG1   1 
ATOM   12638 C  CG2   . VAL C 2 224 ? 128.239 90.020  108.713 1.00 23.14 ?  203 VAL C CG2   1 
ATOM   12639 N  N     . TYR C 2 225 ? 130.489 89.102  112.615 1.00 22.41 ?  204 TYR C N     1 
ATOM   12640 C  CA    . TYR C 2 225 ? 131.624 88.737  113.462 1.00 22.03 ?  204 TYR C CA    1 
ATOM   12641 C  C     . TYR C 2 225 ? 131.329 87.537  114.361 1.00 21.66 ?  204 TYR C C     1 
ATOM   12642 O  O     . TYR C 2 225 ? 132.077 86.549  114.350 1.00 21.72 ?  204 TYR C O     1 
ATOM   12643 C  CB    . TYR C 2 225 ? 132.115 89.929  114.297 1.00 22.22 ?  204 TYR C CB    1 
ATOM   12644 C  CG    . TYR C 2 225 ? 133.421 89.642  115.011 1.00 21.92 ?  204 TYR C CG    1 
ATOM   12645 C  CD1   . TYR C 2 225 ? 134.608 89.486  114.294 1.00 22.36 ?  204 TYR C CD1   1 
ATOM   12646 C  CD2   . TYR C 2 225 ? 133.464 89.516  116.401 1.00 21.43 ?  204 TYR C CD2   1 
ATOM   12647 C  CE1   . TYR C 2 225 ? 135.809 89.204  114.944 1.00 23.82 ?  204 TYR C CE1   1 
ATOM   12648 C  CE2   . TYR C 2 225 ? 134.662 89.242  117.068 1.00 21.49 ?  204 TYR C CE2   1 
ATOM   12649 C  CZ    . TYR C 2 225 ? 135.823 89.090  116.334 1.00 23.58 ?  204 TYR C CZ    1 
ATOM   12650 O  OH    . TYR C 2 225 ? 136.997 88.821  116.985 1.00 25.42 ?  204 TYR C OH    1 
ATOM   12651 N  N     . VAL C 2 226 ? 130.242 87.614  115.132 1.00 20.95 ?  205 VAL C N     1 
ATOM   12652 C  CA    . VAL C 2 226 ? 129.845 86.493  115.994 1.00 20.49 ?  205 VAL C CA    1 
ATOM   12653 C  C     . VAL C 2 226 ? 129.558 85.233  115.158 1.00 20.84 ?  205 VAL C C     1 
ATOM   12654 O  O     . VAL C 2 226 ? 129.938 84.119  115.543 1.00 21.10 ?  205 VAL C O     1 
ATOM   12655 C  CB    . VAL C 2 226 ? 128.672 86.861  116.944 1.00 20.57 ?  205 VAL C CB    1 
ATOM   12656 C  CG1   . VAL C 2 226 ? 128.264 85.653  117.788 1.00 20.35 ?  205 VAL C CG1   1 
ATOM   12657 C  CG2   . VAL C 2 226 ? 129.088 88.023  117.858 1.00 19.60 ?  205 VAL C CG2   1 
ATOM   12658 N  N     . GLY C 2 227 ? 128.941 85.417  113.995 1.00 21.08 ?  206 GLY C N     1 
ATOM   12659 C  CA    . GLY C 2 227 ? 128.752 84.311  113.042 1.00 21.43 ?  206 GLY C CA    1 
ATOM   12660 C  C     . GLY C 2 227 ? 130.042 83.598  112.659 1.00 21.95 ?  206 GLY C C     1 
ATOM   12661 O  O     . GLY C 2 227 ? 130.092 82.357  112.611 1.00 21.84 ?  206 GLY C O     1 
ATOM   12662 N  N     . LEU C 2 228 ? 131.094 84.372  112.391 1.00 22.09 ?  207 LEU C N     1 
ATOM   12663 C  CA    . LEU C 2 228 ? 132.394 83.783  112.053 1.00 22.96 ?  207 LEU C CA    1 
ATOM   12664 C  C     . LEU C 2 228 ? 132.996 82.987  113.221 1.00 22.60 ?  207 LEU C C     1 
ATOM   12665 O  O     . LEU C 2 228 ? 133.571 81.914  113.016 1.00 22.04 ?  207 LEU C O     1 
ATOM   12666 C  CB    . LEU C 2 228 ? 133.373 84.841  111.529 1.00 23.39 ?  207 LEU C CB    1 
ATOM   12667 C  CG    . LEU C 2 228 ? 133.046 85.512  110.182 1.00 24.35 ?  207 LEU C CG    1 
ATOM   12668 C  CD1   . LEU C 2 228 ? 133.860 86.805  110.029 1.00 25.01 ?  207 LEU C CD1   1 
ATOM   12669 C  CD2   . LEU C 2 228 ? 133.294 84.586  108.996 1.00 25.11 ?  207 LEU C CD2   1 
ATOM   12670 N  N     . LEU C 2 229 ? 132.838 83.492  114.443 1.00 22.37 ?  208 LEU C N     1 
ATOM   12671 C  CA    . LEU C 2 229 ? 133.293 82.753  115.636 1.00 22.62 ?  208 LEU C CA    1 
ATOM   12672 C  C     . LEU C 2 229 ? 132.524 81.444  115.843 1.00 22.77 ?  208 LEU C C     1 
ATOM   12673 O  O     . LEU C 2 229 ? 133.117 80.406  116.183 1.00 22.57 ?  208 LEU C O     1 
ATOM   12674 C  CB    . LEU C 2 229 ? 133.236 83.631  116.890 1.00 22.44 ?  208 LEU C CB    1 
ATOM   12675 C  CG    . LEU C 2 229 ? 134.044 84.936  116.835 1.00 23.54 ?  208 LEU C CG    1 
ATOM   12676 C  CD1   . LEU C 2 229 ? 133.821 85.760  118.101 1.00 23.37 ?  208 LEU C CD1   1 
ATOM   12677 C  CD2   . LEU C 2 229 ? 135.544 84.668  116.615 1.00 23.91 ?  208 LEU C CD2   1 
ATOM   12678 N  N     . ALA C 2 230 ? 131.209 81.493  115.626 1.00 22.42 ?  209 ALA C N     1 
ATOM   12679 C  CA    . ALA C 2 230 ? 130.369 80.299  115.700 1.00 22.02 ?  209 ALA C CA    1 
ATOM   12680 C  C     . ALA C 2 230 ? 130.800 79.247  114.673 1.00 22.58 ?  209 ALA C C     1 
ATOM   12681 O  O     . ALA C 2 230 ? 130.922 78.075  115.002 1.00 22.14 ?  209 ALA C O     1 
ATOM   12682 C  CB    . ALA C 2 230 ? 128.914 80.661  115.503 1.00 22.04 ?  209 ALA C CB    1 
ATOM   12683 N  N     . GLN C 2 231 ? 131.047 79.684  113.439 1.00 22.96 ?  210 GLN C N     1 
ATOM   12684 C  CA    . GLN C 2 231 ? 131.526 78.776  112.380 1.00 24.30 ?  210 GLN C CA    1 
ATOM   12685 C  C     . GLN C 2 231 ? 132.848 78.111  112.716 1.00 25.11 ?  210 GLN C C     1 
ATOM   12686 O  O     . GLN C 2 231 ? 133.068 76.950  112.356 1.00 24.97 ?  210 GLN C O     1 
ATOM   12687 C  CB    . GLN C 2 231 ? 131.640 79.510  111.048 1.00 24.38 ?  210 GLN C CB    1 
ATOM   12688 C  CG    . GLN C 2 231 ? 130.275 79.916  110.468 1.00 25.12 ?  210 GLN C CG    1 
ATOM   12689 C  CD    . GLN C 2 231 ? 130.406 80.641  109.146 1.00 28.08 ?  210 GLN C CD    1 
ATOM   12690 O  OE1   . GLN C 2 231 ? 131.017 80.130  108.207 1.00 27.83 ?  210 GLN C OE1   1 
ATOM   12691 N  NE2   . GLN C 2 231 ? 129.845 81.850  109.067 1.00 26.38 ?  210 GLN C NE2   1 
ATOM   12692 N  N     . GLU C 2 232 ? 133.731 78.843  113.401 1.00 25.80 ?  211 GLU C N     1 
ATOM   12693 C  CA    . GLU C 2 232 ? 134.997 78.268  113.867 1.00 27.16 ?  211 GLU C CA    1 
ATOM   12694 C  C     . GLU C 2 232 ? 134.757 77.036  114.734 1.00 26.47 ?  211 GLU C C     1 
ATOM   12695 O  O     . GLU C 2 232 ? 135.423 76.007  114.568 1.00 26.10 ?  211 GLU C O     1 
ATOM   12696 C  CB    . GLU C 2 232 ? 135.785 79.277  114.692 1.00 27.59 ?  211 GLU C CB    1 
ATOM   12697 C  CG    . GLU C 2 232 ? 136.737 80.127  113.908 1.00 32.55 ?  211 GLU C CG    1 
ATOM   12698 C  CD    . GLU C 2 232 ? 137.973 80.500  114.716 1.00 36.72 ?  211 GLU C CD    1 
ATOM   12699 O  OE1   . GLU C 2 232 ? 138.039 80.170  115.925 1.00 38.32 ?  211 GLU C OE1   1 
ATOM   12700 O  OE2   . GLU C 2 232 ? 138.884 81.120  114.133 1.00 40.62 -1 211 GLU C OE2   1 
ATOM   12701 N  N     . ILE C 2 233 ? 133.817 77.155  115.670 1.00 25.55 ?  212 ILE C N     1 
ATOM   12702 C  CA    . ILE C 2 233 ? 133.513 76.061  116.592 1.00 25.32 ?  212 ILE C CA    1 
ATOM   12703 C  C     . ILE C 2 233 ? 132.823 74.907  115.876 1.00 25.48 ?  212 ILE C C     1 
ATOM   12704 O  O     . ILE C 2 233 ? 133.219 73.749  116.028 1.00 25.82 ?  212 ILE C O     1 
ATOM   12705 C  CB    . ILE C 2 233 ? 132.674 76.536  117.799 1.00 25.39 ?  212 ILE C CB    1 
ATOM   12706 C  CG1   . ILE C 2 233 ? 133.513 77.478  118.668 1.00 24.37 ?  212 ILE C CG1   1 
ATOM   12707 C  CG2   . ILE C 2 233 ? 132.165 75.337  118.606 1.00 24.86 ?  212 ILE C CG2   1 
ATOM   12708 C  CD1   . ILE C 2 233 ? 132.688 78.316  119.631 1.00 25.10 ?  212 ILE C CD1   1 
ATOM   12709 N  N     . TYR C 2 234 ? 131.810 75.233  115.077 1.00 25.27 ?  213 TYR C N     1 
ATOM   12710 C  CA    . TYR C 2 234 ? 131.110 74.252  114.244 1.00 25.77 ?  213 TYR C CA    1 
ATOM   12711 C  C     . TYR C 2 234 ? 132.077 73.439  113.365 1.00 26.44 ?  213 TYR C C     1 
ATOM   12712 O  O     . TYR C 2 234 ? 131.936 72.220  113.233 1.00 26.29 ?  213 TYR C O     1 
ATOM   12713 C  CB    . TYR C 2 234 ? 130.072 74.981  113.376 1.00 25.67 ?  213 TYR C CB    1 
ATOM   12714 C  CG    . TYR C 2 234 ? 129.285 74.135  112.395 1.00 25.65 ?  213 TYR C CG    1 
ATOM   12715 C  CD1   . TYR C 2 234 ? 128.051 73.585  112.755 1.00 25.02 ?  213 TYR C CD1   1 
ATOM   12716 C  CD2   . TYR C 2 234 ? 129.746 73.934  111.085 1.00 26.59 ?  213 TYR C CD2   1 
ATOM   12717 C  CE1   . TYR C 2 234 ? 127.311 72.832  111.851 1.00 26.52 ?  213 TYR C CE1   1 
ATOM   12718 C  CE2   . TYR C 2 234 ? 129.015 73.174  110.171 1.00 27.00 ?  213 TYR C CE2   1 
ATOM   12719 C  CZ    . TYR C 2 234 ? 127.801 72.626  110.566 1.00 27.79 ?  213 TYR C CZ    1 
ATOM   12720 O  OH    . TYR C 2 234 ? 127.069 71.894  109.674 1.00 29.00 ?  213 TYR C OH    1 
ATOM   12721 N  N     . ASN C 2 235 ? 133.055 74.111  112.764 1.00 26.96 ?  214 ASN C N     1 
ATOM   12722 C  CA    . ASN C 2 235 ? 133.979 73.437  111.853 1.00 28.05 ?  214 ASN C CA    1 
ATOM   12723 C  C     . ASN C 2 235 ? 134.932 72.452  112.522 1.00 28.24 ?  214 ASN C C     1 
ATOM   12724 O  O     . ASN C 2 235 ? 135.541 71.632  111.842 1.00 28.63 ?  214 ASN C O     1 
ATOM   12725 C  CB    . ASN C 2 235 ? 134.734 74.443  110.972 1.00 28.38 ?  214 ASN C CB    1 
ATOM   12726 C  CG    . ASN C 2 235 ? 133.817 75.154  109.982 1.00 31.14 ?  214 ASN C CG    1 
ATOM   12727 O  OD1   . ASN C 2 235 ? 132.830 74.584  109.507 1.00 34.16 ?  214 ASN C OD1   1 
ATOM   12728 N  ND2   . ASN C 2 235 ? 134.138 76.404  109.672 1.00 32.42 ?  214 ASN C ND2   1 
ATOM   12729 N  N     . LYS C 2 236 ? 135.041 72.519  113.848 1.00 27.91 ?  215 LYS C N     1 
ATOM   12730 C  CA    . LYS C 2 236 ? 135.853 71.576  114.621 1.00 28.49 ?  215 LYS C CA    1 
ATOM   12731 C  C     . LYS C 2 236 ? 135.156 70.235  114.875 1.00 28.50 ?  215 LYS C C     1 
ATOM   12732 O  O     . LYS C 2 236 ? 135.794 69.266  115.296 1.00 28.98 ?  215 LYS C O     1 
ATOM   12733 C  CB    . LYS C 2 236 ? 136.265 72.191  115.963 1.00 28.10 ?  215 LYS C CB    1 
ATOM   12734 C  CG    . LYS C 2 236 ? 137.173 73.407  115.845 1.00 29.25 ?  215 LYS C CG    1 
ATOM   12735 C  CD    . LYS C 2 236 ? 137.557 73.950  117.211 1.00 30.19 ?  215 LYS C CD    1 
ATOM   12736 C  CE    . LYS C 2 236 ? 138.187 75.315  117.066 1.00 32.63 ?  215 LYS C CE    1 
ATOM   12737 N  NZ    . LYS C 2 236 ? 138.567 75.880  118.382 1.00 35.39 1  215 LYS C NZ    1 
ATOM   12738 N  N     . GLN C 2 237 ? 133.857 70.167  114.604 1.00 28.25 ?  216 GLN C N     1 
ATOM   12739 C  CA    . GLN C 2 237 ? 133.068 69.003  115.009 1.00 28.34 ?  216 GLN C CA    1 
ATOM   12740 C  C     . GLN C 2 237 ? 133.085 67.850  113.991 1.00 28.92 ?  216 GLN C C     1 
ATOM   12741 O  O     . GLN C 2 237 ? 133.390 68.052  112.815 1.00 28.53 ?  216 GLN C O     1 
ATOM   12742 C  CB    . GLN C 2 237 ? 131.631 69.435  115.336 1.00 27.68 ?  216 GLN C CB    1 
ATOM   12743 C  CG    . GLN C 2 237 ? 131.532 70.631  116.314 1.00 26.67 ?  216 GLN C CG    1 
ATOM   12744 C  CD    . GLN C 2 237 ? 132.354 70.458  117.587 1.00 25.32 ?  216 GLN C CD    1 
ATOM   12745 O  OE1   . GLN C 2 237 ? 132.353 69.391  118.206 1.00 25.49 ?  216 GLN C OE1   1 
ATOM   12746 N  NE2   . GLN C 2 237 ? 133.059 71.513  117.986 1.00 23.63 ?  216 GLN C NE2   1 
ATOM   12747 N  N     . THR C 2 238 ? 132.751 66.646  114.456 1.00 29.53 ?  217 THR C N     1 
ATOM   12748 C  CA    . THR C 2 238 ? 132.479 65.518  113.560 1.00 30.73 ?  217 THR C CA    1 
ATOM   12749 C  C     . THR C 2 238 ? 131.231 65.830  112.725 1.00 31.13 ?  217 THR C C     1 
ATOM   12750 O  O     . THR C 2 238 ? 130.451 66.737  113.068 1.00 30.17 ?  217 THR C O     1 
ATOM   12751 C  CB    . THR C 2 238 ? 132.195 64.218  114.333 1.00 30.79 ?  217 THR C CB    1 
ATOM   12752 O  OG1   . THR C 2 238 ? 130.946 64.344  115.026 1.00 31.16 ?  217 THR C OG1   1 
ATOM   12753 C  CG2   . THR C 2 238 ? 133.312 63.902  115.334 1.00 31.22 ?  217 THR C CG2   1 
ATOM   12754 N  N     . GLU C 2 239 ? 131.028 65.065  111.650 1.00 31.67 ?  218 GLU C N     1 
ATOM   12755 C  CA    . GLU C 2 239 ? 129.834 65.238  110.821 1.00 32.25 ?  218 GLU C CA    1 
ATOM   12756 C  C     . GLU C 2 239 ? 128.545 64.983  111.610 1.00 31.86 ?  218 GLU C C     1 
ATOM   12757 O  O     . GLU C 2 239 ? 127.549 65.692  111.436 1.00 31.09 ?  218 GLU C O     1 
ATOM   12758 C  CB    . GLU C 2 239 ? 129.909 64.368  109.554 1.00 33.29 ?  218 GLU C CB    1 
ATOM   12759 C  CG    . GLU C 2 239 ? 130.991 64.829  108.559 1.00 35.65 ?  218 GLU C CG    1 
ATOM   12760 C  CD    . GLU C 2 239 ? 130.790 66.272  108.081 1.00 39.17 ?  218 GLU C CD    1 
ATOM   12761 O  OE1   . GLU C 2 239 ? 129.642 66.636  107.718 1.00 41.08 ?  218 GLU C OE1   1 
ATOM   12762 O  OE2   . GLU C 2 239 ? 131.777 67.047  108.073 1.00 39.64 -1 218 GLU C OE2   1 
ATOM   12763 N  N     . GLU C 2 240 ? 128.590 63.993  112.502 1.00 31.72 ?  219 GLU C N     1 
ATOM   12764 C  CA    . GLU C 2 240 ? 127.464 63.656  113.362 1.00 31.76 ?  219 GLU C CA    1 
ATOM   12765 C  C     . GLU C 2 240 ? 127.115 64.815  114.307 1.00 30.21 ?  219 GLU C C     1 
ATOM   12766 O  O     . GLU C 2 240 ? 125.938 65.173  114.462 1.00 29.63 ?  219 GLU C O     1 
ATOM   12767 C  CB    . GLU C 2 240 ? 127.780 62.378  114.144 1.00 32.58 ?  219 GLU C CB    1 
ATOM   12768 C  CG    . GLU C 2 240 ? 126.603 61.785  114.902 1.00 36.93 ?  219 GLU C CG    1 
ATOM   12769 C  CD    . GLU C 2 240 ? 126.856 60.344  115.333 1.00 42.06 ?  219 GLU C CD    1 
ATOM   12770 O  OE1   . GLU C 2 240 ? 126.952 60.090  116.554 1.00 44.09 ?  219 GLU C OE1   1 
ATOM   12771 O  OE2   . GLU C 2 240 ? 126.968 59.464  114.447 1.00 44.45 -1 219 GLU C OE2   1 
ATOM   12772 N  N     . LYS C 2 241 ? 128.143 65.401  114.918 1.00 28.91 ?  220 LYS C N     1 
ATOM   12773 C  CA    . LYS C 2 241 ? 127.972 66.538  115.812 1.00 28.14 ?  220 LYS C CA    1 
ATOM   12774 C  C     . LYS C 2 241 ? 127.443 67.773  115.079 1.00 27.03 ?  220 LYS C C     1 
ATOM   12775 O  O     . LYS C 2 241 ? 126.569 68.476  115.597 1.00 26.72 ?  220 LYS C O     1 
ATOM   12776 C  CB    . LYS C 2 241 ? 129.279 66.869  116.540 1.00 27.83 ?  220 LYS C CB    1 
ATOM   12777 C  CG    . LYS C 2 241 ? 129.137 67.984  117.585 1.00 29.68 ?  220 LYS C CG    1 
ATOM   12778 C  CD    . LYS C 2 241 ? 128.968 67.436  118.995 1.00 33.58 ?  220 LYS C CD    1 
ATOM   12779 C  CE    . LYS C 2 241 ? 127.543 67.060  119.290 1.00 33.71 ?  220 LYS C CE    1 
ATOM   12780 N  NZ    . LYS C 2 241 ? 127.397 66.370  120.614 1.00 34.69 1  220 LYS C NZ    1 
ATOM   12781 N  N     . LYS C 2 242 ? 127.984 68.027  113.886 1.00 26.38 ?  221 LYS C N     1 
ATOM   12782 C  CA    . LYS C 2 242 ? 127.520 69.105  113.008 1.00 25.87 ?  221 LYS C CA    1 
ATOM   12783 C  C     . LYS C 2 242 ? 126.039 68.988  112.697 1.00 25.72 ?  221 LYS C C     1 
ATOM   12784 O  O     . LYS C 2 242 ? 125.311 69.990  112.743 1.00 24.52 ?  221 LYS C O     1 
ATOM   12785 C  CB    . LYS C 2 242 ? 128.306 69.131  111.696 1.00 25.83 ?  221 LYS C CB    1 
ATOM   12786 C  CG    . LYS C 2 242 ? 129.700 69.705  111.797 1.00 26.76 ?  221 LYS C CG    1 
ATOM   12787 C  CD    . LYS C 2 242 ? 130.322 69.800  110.408 1.00 28.40 ?  221 LYS C CD    1 
ATOM   12788 C  CE    . LYS C 2 242 ? 131.783 70.147  110.474 1.00 29.84 ?  221 LYS C CE    1 
ATOM   12789 N  NZ    . LYS C 2 242 ? 132.412 70.017  109.139 1.00 30.96 1  221 LYS C NZ    1 
ATOM   12790 N  N     . ALA C 2 243 ? 125.607 67.767  112.369 1.00 25.97 ?  222 ALA C N     1 
ATOM   12791 C  CA    . ALA C 2 243 ? 124.192 67.488  112.109 1.00 25.79 ?  222 ALA C CA    1 
ATOM   12792 C  C     . ALA C 2 243 ? 123.313 67.859  113.305 1.00 25.24 ?  222 ALA C C     1 
ATOM   12793 O  O     . ALA C 2 243 ? 122.232 68.439  113.127 1.00 25.37 ?  222 ALA C O     1 
ATOM   12794 C  CB    . ALA C 2 243 ? 123.991 66.027  111.704 1.00 26.17 ?  222 ALA C CB    1 
ATOM   12795 N  N     . GLU C 2 244 ? 123.780 67.560  114.515 1.00 25.02 ?  223 GLU C N     1 
ATOM   12796 C  CA    . GLU C 2 244 ? 123.059 67.954  115.735 1.00 25.08 ?  223 GLU C CA    1 
ATOM   12797 C  C     . GLU C 2 244 ? 123.038 69.479  115.941 1.00 24.70 ?  223 GLU C C     1 
ATOM   12798 O  O     . GLU C 2 244 ? 122.022 70.048  116.369 1.00 24.20 ?  223 GLU C O     1 
ATOM   12799 C  CB    . GLU C 2 244 ? 123.636 67.257  116.972 1.00 25.35 ?  223 GLU C CB    1 
ATOM   12800 C  CG    . GLU C 2 244 ? 122.875 67.592  118.266 1.00 26.67 ?  223 GLU C CG    1 
ATOM   12801 C  CD    . GLU C 2 244 ? 123.602 67.144  119.521 1.00 28.29 ?  223 GLU C CD    1 
ATOM   12802 O  OE1   . GLU C 2 244 ? 124.431 66.217  119.447 1.00 29.51 ?  223 GLU C OE1   1 
ATOM   12803 O  OE2   . GLU C 2 244 ? 123.343 67.728  120.589 1.00 29.09 -1 223 GLU C OE2   1 
ATOM   12804 N  N     . LEU C 2 245 ? 124.157 70.133  115.647 1.00 24.27 ?  224 LEU C N     1 
ATOM   12805 C  CA    . LEU C 2 245 ? 124.245 71.588  115.790 1.00 24.54 ?  224 LEU C CA    1 
ATOM   12806 C  C     . LEU C 2 245 ? 123.322 72.336  114.817 1.00 24.42 ?  224 LEU C C     1 
ATOM   12807 O  O     . LEU C 2 245 ? 122.726 73.352  115.184 1.00 24.10 ?  224 LEU C O     1 
ATOM   12808 C  CB    . LEU C 2 245 ? 125.705 72.065  115.682 1.00 23.86 ?  224 LEU C CB    1 
ATOM   12809 C  CG    . LEU C 2 245 ? 126.632 71.628  116.825 1.00 24.78 ?  224 LEU C CG    1 
ATOM   12810 C  CD1   . LEU C 2 245 ? 128.039 72.208  116.642 1.00 25.54 ?  224 LEU C CD1   1 
ATOM   12811 C  CD2   . LEU C 2 245 ? 126.076 72.008  118.205 1.00 25.29 ?  224 LEU C CD2   1 
ATOM   12812 N  N     . ARG C 2 246 ? 123.198 71.824  113.594 1.00 25.26 ?  225 ARG C N     1 
ATOM   12813 C  CA    . ARG C 2 246 ? 122.244 72.363  112.614 1.00 25.97 ?  225 ARG C CA    1 
ATOM   12814 C  C     . ARG C 2 246 ? 120.818 72.192  113.120 1.00 25.85 ?  225 ARG C C     1 
ATOM   12815 O  O     . ARG C 2 246 ? 120.005 73.110  113.001 1.00 25.01 ?  225 ARG C O     1 
ATOM   12816 C  CB    . ARG C 2 246 ? 122.411 71.707  111.227 1.00 26.65 ?  225 ARG C CB    1 
ATOM   12817 C  CG    . ARG C 2 246 ? 123.737 72.036  110.544 1.00 28.90 ?  225 ARG C CG    1 
ATOM   12818 C  CD    . ARG C 2 246 ? 123.744 71.715  109.029 1.00 31.26 ?  225 ARG C CD    1 
ATOM   12819 N  NE    . ARG C 2 246 ? 123.482 70.302  108.742 1.00 34.01 ?  225 ARG C NE    1 
ATOM   12820 C  CZ    . ARG C 2 246 ? 124.368 69.316  108.884 1.00 35.64 ?  225 ARG C CZ    1 
ATOM   12821 N  NH1   . ARG C 2 246 ? 125.597 69.564  109.319 1.00 36.11 1  225 ARG C NH1   1 
ATOM   12822 N  NH2   . ARG C 2 246 ? 124.018 68.069  108.590 1.00 37.05 ?  225 ARG C NH2   1 
ATOM   12823 N  N     . GLU C 2 247 ? 120.522 71.022  113.693 1.00 26.01 ?  226 GLU C N     1 
ATOM   12824 C  CA    . GLU C 2 247 ? 119.216 70.775  114.315 1.00 26.48 ?  226 GLU C CA    1 
ATOM   12825 C  C     . GLU C 2 247 ? 118.938 71.789  115.424 1.00 25.72 ?  226 GLU C C     1 
ATOM   12826 O  O     . GLU C 2 247 ? 117.847 72.376  115.479 1.00 25.16 ?  226 GLU C O     1 
ATOM   12827 C  CB    . GLU C 2 247 ? 119.119 69.359  114.889 1.00 27.18 ?  226 GLU C CB    1 
ATOM   12828 C  CG    . GLU C 2 247 ? 117.683 68.922  115.153 1.00 30.38 ?  226 GLU C CG    1 
ATOM   12829 C  CD    . GLU C 2 247 ? 117.508 68.066  116.393 1.00 35.77 ?  226 GLU C CD    1 
ATOM   12830 O  OE1   . GLU C 2 247 ? 118.443 67.338  116.790 1.00 38.02 ?  226 GLU C OE1   1 
ATOM   12831 O  OE2   . GLU C 2 247 ? 116.406 68.120  116.981 1.00 40.39 -1 226 GLU C OE2   1 
ATOM   12832 N  N     . PHE C 2 248 ? 119.925 71.993  116.299 1.00 24.71 ?  227 PHE C N     1 
ATOM   12833 C  CA    . PHE C 2 248 ? 119.800 72.985  117.366 1.00 23.71 ?  227 PHE C CA    1 
ATOM   12834 C  C     . PHE C 2 248 ? 119.482 74.362  116.780 1.00 23.14 ?  227 PHE C C     1 
ATOM   12835 O  O     . PHE C 2 248 ? 118.553 75.030  117.238 1.00 22.40 ?  227 PHE C O     1 
ATOM   12836 C  CB    . PHE C 2 248 ? 121.064 73.067  118.240 1.00 23.85 ?  227 PHE C CB    1 
ATOM   12837 C  CG    . PHE C 2 248 ? 121.103 74.297  119.111 1.00 23.64 ?  227 PHE C CG    1 
ATOM   12838 C  CD1   . PHE C 2 248 ? 120.420 74.320  120.329 1.00 23.07 ?  227 PHE C CD1   1 
ATOM   12839 C  CD2   . PHE C 2 248 ? 121.764 75.459  118.677 1.00 23.04 ?  227 PHE C CD2   1 
ATOM   12840 C  CE1   . PHE C 2 248 ? 120.425 75.461  121.131 1.00 22.73 ?  227 PHE C CE1   1 
ATOM   12841 C  CE2   . PHE C 2 248 ? 121.772 76.612  119.464 1.00 23.31 ?  227 PHE C CE2   1 
ATOM   12842 C  CZ    . PHE C 2 248 ? 121.103 76.615  120.699 1.00 21.51 ?  227 PHE C CZ    1 
ATOM   12843 N  N     . ALA C 2 249 ? 120.253 74.769  115.770 1.00 22.95 ?  228 ALA C N     1 
ATOM   12844 C  CA    . ALA C 2 249 ? 120.138 76.114  115.191 1.00 22.96 ?  228 ALA C CA    1 
ATOM   12845 C  C     . ALA C 2 249 ? 118.779 76.330  114.530 1.00 23.31 ?  228 ALA C C     1 
ATOM   12846 O  O     . ALA C 2 249 ? 118.157 77.381  114.697 1.00 22.63 ?  228 ALA C O     1 
ATOM   12847 C  CB    . ALA C 2 249 ? 121.266 76.369  114.194 1.00 22.40 ?  228 ALA C CB    1 
ATOM   12848 N  N     . ILE C 2 250 ? 118.331 75.326  113.784 1.00 23.66 ?  229 ILE C N     1 
ATOM   12849 C  CA    . ILE C 2 250 ? 117.049 75.392  113.082 1.00 25.00 ?  229 ILE C CA    1 
ATOM   12850 C  C     . ILE C 2 250 ? 115.858 75.302  114.047 1.00 24.64 ?  229 ILE C C     1 
ATOM   12851 O  O     . ILE C 2 250 ? 114.900 76.075  113.923 1.00 24.26 ?  229 ILE C O     1 
ATOM   12852 C  CB    . ILE C 2 250 ? 116.979 74.356  111.917 1.00 25.43 ?  229 ILE C CB    1 
ATOM   12853 C  CG1   . ILE C 2 250 ? 117.912 74.808  110.784 1.00 27.27 ?  229 ILE C CG1   1 
ATOM   12854 C  CG2   . ILE C 2 250 ? 115.536 74.249  111.353 1.00 27.62 ?  229 ILE C CG2   1 
ATOM   12855 C  CD1   . ILE C 2 250 ? 118.626 73.673  110.037 1.00 31.32 ?  229 ILE C CD1   1 
ATOM   12856 N  N     . ASP C 2 251 ? 115.928 74.395  115.022 1.00 24.78 ?  230 ASP C N     1 
ATOM   12857 C  CA    . ASP C 2 251 ? 114.894 74.327  116.071 1.00 25.20 ?  230 ASP C CA    1 
ATOM   12858 C  C     . ASP C 2 251 ? 114.778 75.639  116.846 1.00 24.08 ?  230 ASP C C     1 
ATOM   12859 O  O     . ASP C 2 251 ? 113.667 76.104  117.149 1.00 23.34 ?  230 ASP C O     1 
ATOM   12860 C  CB    . ASP C 2 251 ? 115.184 73.207  117.081 1.00 25.73 ?  230 ASP C CB    1 
ATOM   12861 C  CG    . ASP C 2 251 ? 114.875 71.830  116.542 1.00 28.78 ?  230 ASP C CG    1 
ATOM   12862 O  OD1   . ASP C 2 251 ? 114.333 71.712  115.418 1.00 29.99 ?  230 ASP C OD1   1 
ATOM   12863 O  OD2   . ASP C 2 251 ? 115.186 70.856  117.258 1.00 33.31 -1 230 ASP C OD2   1 
ATOM   12864 N  N     . LEU C 2 252 ? 115.924 76.226  117.181 1.00 22.98 ?  231 LEU C N     1 
ATOM   12865 C  CA    . LEU C 2 252 ? 115.929 77.489  117.920 1.00 21.63 ?  231 LEU C CA    1 
ATOM   12866 C  C     . LEU C 2 252 ? 115.345 78.607  117.064 1.00 21.66 ?  231 LEU C C     1 
ATOM   12867 O  O     . LEU C 2 252 ? 114.562 79.430  117.541 1.00 19.41 ?  231 LEU C O     1 
ATOM   12868 C  CB    . LEU C 2 252 ? 117.341 77.864  118.368 1.00 21.89 ?  231 LEU C CB    1 
ATOM   12869 C  CG    . LEU C 2 252 ? 117.519 79.217  119.082 1.00 21.33 ?  231 LEU C CG    1 
ATOM   12870 C  CD1   . LEU C 2 252 ? 116.649 79.314  120.353 1.00 20.89 ?  231 LEU C CD1   1 
ATOM   12871 C  CD2   . LEU C 2 252 ? 119.002 79.427  119.399 1.00 20.31 ?  231 LEU C CD2   1 
ATOM   12872 N  N     . LEU C 2 253 ? 115.742 78.635  115.795 1.00 22.28 ?  232 LEU C N     1 
ATOM   12873 C  CA    . LEU C 2 253 ? 115.245 79.666  114.890 1.00 23.05 ?  232 LEU C CA    1 
ATOM   12874 C  C     . LEU C 2 253 ? 113.727 79.589  114.763 1.00 23.36 ?  232 LEU C C     1 
ATOM   12875 O  O     . LEU C 2 253 ? 113.038 80.613  114.912 1.00 22.96 ?  232 LEU C O     1 
ATOM   12876 C  CB    . LEU C 2 253 ? 115.918 79.574  113.519 1.00 23.53 ?  232 LEU C CB    1 
ATOM   12877 C  CG    . LEU C 2 253 ? 115.445 80.639  112.522 1.00 25.63 ?  232 LEU C CG    1 
ATOM   12878 C  CD1   . LEU C 2 253 ? 115.816 82.049  112.982 1.00 25.88 ?  232 LEU C CD1   1 
ATOM   12879 C  CD2   . LEU C 2 253 ? 116.029 80.346  111.148 1.00 27.67 ?  232 LEU C CD2   1 
ATOM   12880 N  N     . ASN C 2 254 ? 113.211 78.382  114.509 1.00 23.55 ?  233 ASN C N     1 
ATOM   12881 C  CA    . ASN C 2 254 ? 111.756 78.164  114.424 1.00 24.61 ?  233 ASN C CA    1 
ATOM   12882 C  C     . ASN C 2 254 ? 111.000 78.558  115.696 1.00 23.57 ?  233 ASN C C     1 
ATOM   12883 O  O     . ASN C 2 254 ? 109.936 79.169  115.632 1.00 23.52 ?  233 ASN C O     1 
ATOM   12884 C  CB    . ASN C 2 254 ? 111.433 76.718  114.038 1.00 24.99 ?  233 ASN C CB    1 
ATOM   12885 C  CG    . ASN C 2 254 ? 111.467 76.493  112.532 1.00 28.92 ?  233 ASN C CG    1 
ATOM   12886 O  OD1   . ASN C 2 254 ? 110.753 77.149  111.771 1.00 33.75 ?  233 ASN C OD1   1 
ATOM   12887 N  ND2   . ASN C 2 254 ? 112.293 75.560  112.099 1.00 30.99 ?  233 ASN C ND2   1 
ATOM   12888 N  N     . GLN C 2 255 ? 111.556 78.210  116.853 1.00 23.22 ?  234 GLN C N     1 
ATOM   12889 C  CA    . GLN C 2 255 ? 110.936 78.578  118.118 1.00 22.54 ?  234 GLN C CA    1 
ATOM   12890 C  C     . GLN C 2 255 ? 110.892 80.109  118.306 1.00 22.00 ?  234 GLN C C     1 
ATOM   12891 O  O     . GLN C 2 255 ? 109.861 80.673  118.712 1.00 21.73 ?  234 GLN C O     1 
ATOM   12892 C  CB    . GLN C 2 255 ? 111.658 77.904  119.284 1.00 22.85 ?  234 GLN C CB    1 
ATOM   12893 C  CG    . GLN C 2 255 ? 110.898 77.988  120.590 1.00 23.87 ?  234 GLN C CG    1 
ATOM   12894 C  CD    . GLN C 2 255 ? 111.637 77.343  121.757 1.00 24.95 ?  234 GLN C CD    1 
ATOM   12895 O  OE1   . GLN C 2 255 ? 112.659 76.672  121.572 1.00 24.21 ?  234 GLN C OE1   1 
ATOM   12896 N  NE2   . GLN C 2 255 ? 111.133 77.569  122.971 1.00 25.97 ?  234 GLN C NE2   1 
ATOM   12897 N  N     . LEU C 2 256 ? 112.004 80.771  118.011 1.00 21.27 ?  235 LEU C N     1 
ATOM   12898 C  CA    . LEU C 2 256 ? 112.068 82.227  118.081 1.00 21.37 ?  235 LEU C CA    1 
ATOM   12899 C  C     . LEU C 2 256 ? 111.140 82.865  117.042 1.00 21.21 ?  235 LEU C C     1 
ATOM   12900 O  O     . LEU C 2 256 ? 110.473 83.861  117.318 1.00 20.75 ?  235 LEU C O     1 
ATOM   12901 C  CB    . LEU C 2 256 ? 113.510 82.703  117.856 1.00 20.93 ?  235 LEU C CB    1 
ATOM   12902 C  CG    . LEU C 2 256 ? 114.546 82.466  118.957 1.00 21.74 ?  235 LEU C CG    1 
ATOM   12903 C  CD1   . LEU C 2 256 ? 115.936 82.901  118.469 1.00 20.15 ?  235 LEU C CD1   1 
ATOM   12904 C  CD2   . LEU C 2 256 ? 114.182 83.183  120.257 1.00 20.90 ?  235 LEU C CD2   1 
ATOM   12905 N  N     . TYR C 2 257 ? 111.128 82.285  115.848 1.00 21.68 ?  236 TYR C N     1 
ATOM   12906 C  CA    . TYR C 2 257 ? 110.300 82.766  114.742 1.00 22.40 ?  236 TYR C CA    1 
ATOM   12907 C  C     . TYR C 2 257 ? 108.807 82.757  115.110 1.00 23.31 ?  236 TYR C C     1 
ATOM   12908 O  O     . TYR C 2 257 ? 108.116 83.784  114.953 1.00 22.99 ?  236 TYR C O     1 
ATOM   12909 C  CB    . TYR C 2 257 ? 110.572 81.940  113.481 1.00 22.81 ?  236 TYR C CB    1 
ATOM   12910 C  CG    . TYR C 2 257 ? 109.672 82.253  112.302 1.00 23.76 ?  236 TYR C CG    1 
ATOM   12911 C  CD1   . TYR C 2 257 ? 109.742 83.487  111.650 1.00 24.05 ?  236 TYR C CD1   1 
ATOM   12912 C  CD2   . TYR C 2 257 ? 108.742 81.319  111.849 1.00 24.04 ?  236 TYR C CD2   1 
ATOM   12913 C  CE1   . TYR C 2 257 ? 108.910 83.783  110.576 1.00 24.40 ?  236 TYR C CE1   1 
ATOM   12914 C  CE2   . TYR C 2 257 ? 107.907 81.607  110.771 1.00 26.30 ?  236 TYR C CE2   1 
ATOM   12915 C  CZ    . TYR C 2 257 ? 108.007 82.835  110.142 1.00 25.80 ?  236 TYR C CZ    1 
ATOM   12916 O  OH    . TYR C 2 257 ? 107.192 83.109  109.081 1.00 28.42 ?  236 TYR C OH    1 
ATOM   12917 N  N     . GLU C 2 258 ? 108.327 81.626  115.636 1.00 22.99 ?  237 GLU C N     1 
ATOM   12918 C  CA    . GLU C 2 258 ? 106.916 81.487  116.013 1.00 24.46 ?  237 GLU C CA    1 
ATOM   12919 C  C     . GLU C 2 258 ? 106.509 82.505  117.065 1.00 23.86 ?  237 GLU C C     1 
ATOM   12920 O  O     . GLU C 2 258 ? 105.430 83.091  116.982 1.00 24.01 ?  237 GLU C O     1 
ATOM   12921 C  CB    . GLU C 2 258 ? 106.586 80.054  116.467 1.00 25.21 ?  237 GLU C CB    1 
ATOM   12922 C  CG    . GLU C 2 258 ? 106.636 79.014  115.324 1.00 30.12 ?  237 GLU C CG    1 
ATOM   12923 C  CD    . GLU C 2 258 ? 105.553 79.234  114.263 1.00 35.29 ?  237 GLU C CD    1 
ATOM   12924 O  OE1   . GLU C 2 258 ? 104.468 79.765  114.596 1.00 37.71 ?  237 GLU C OE1   1 
ATOM   12925 O  OE2   . GLU C 2 258 ? 105.786 78.870  113.087 1.00 39.07 -1 237 GLU C OE2   1 
ATOM   12926 N  N     . ASN C 2 259 ? 107.388 82.736  118.040 1.00 23.25 ?  238 ASN C N     1 
ATOM   12927 C  CA    . ASN C 2 259 ? 107.163 83.775  119.042 1.00 23.10 ?  238 ASN C CA    1 
ATOM   12928 C  C     . ASN C 2 259 ? 107.169 85.182  118.415 1.00 22.68 ?  238 ASN C C     1 
ATOM   12929 O  O     . ASN C 2 259 ? 106.342 86.032  118.757 1.00 22.73 ?  238 ASN C O     1 
ATOM   12930 C  CB    . ASN C 2 259 ? 108.204 83.657  120.157 1.00 23.22 ?  238 ASN C CB    1 
ATOM   12931 C  CG    . ASN C 2 259 ? 108.004 84.683  121.253 1.00 24.46 ?  238 ASN C CG    1 
ATOM   12932 O  OD1   . ASN C 2 259 ? 107.043 84.611  122.025 1.00 26.28 ?  238 ASN C OD1   1 
ATOM   12933 N  ND2   . ASN C 2 259 ? 108.913 85.648  121.329 1.00 24.93 ?  238 ASN C ND2   1 
ATOM   12934 N  N     . GLU C 2 260 ? 108.086 85.417  117.478 1.00 22.64 ?  239 GLU C N     1 
ATOM   12935 C  CA    . GLU C 2 260 ? 108.201 86.726  116.835 1.00 23.18 ?  239 GLU C CA    1 
ATOM   12936 C  C     . GLU C 2 260 ? 106.962 87.059  115.985 1.00 23.40 ?  239 GLU C C     1 
ATOM   12937 O  O     . GLU C 2 260 ? 106.549 88.226  115.904 1.00 23.57 ?  239 GLU C O     1 
ATOM   12938 C  CB    . GLU C 2 260 ? 109.485 86.819  115.998 1.00 23.19 ?  239 GLU C CB    1 
ATOM   12939 C  CG    . GLU C 2 260 ? 110.036 88.257  115.845 1.00 24.33 ?  239 GLU C CG    1 
ATOM   12940 C  CD    . GLU C 2 260 ? 110.496 88.883  117.174 1.00 27.99 ?  239 GLU C CD    1 
ATOM   12941 O  OE1   . GLU C 2 260 ? 110.541 88.189  118.213 1.00 27.36 ?  239 GLU C OE1   1 
ATOM   12942 O  OE2   . GLU C 2 260 ? 110.810 90.094  117.182 1.00 28.98 -1 239 GLU C OE2   1 
ATOM   12943 N  N     . LEU C 2 261 ? 106.371 86.035  115.368 1.00 23.35 ?  240 LEU C N     1 
ATOM   12944 C  CA    . LEU C 2 261 ? 105.108 86.202  114.634 1.00 23.74 ?  240 LEU C CA    1 
ATOM   12945 C  C     . LEU C 2 261 ? 103.996 86.775  115.518 1.00 23.80 ?  240 LEU C C     1 
ATOM   12946 O  O     . LEU C 2 261 ? 103.308 87.735  115.134 1.00 23.33 ?  240 LEU C O     1 
ATOM   12947 C  CB    . LEU C 2 261 ? 104.647 84.878  114.019 1.00 24.09 ?  240 LEU C CB    1 
ATOM   12948 C  CG    . LEU C 2 261 ? 105.471 84.324  112.856 1.00 24.07 ?  240 LEU C CG    1 
ATOM   12949 C  CD1   . LEU C 2 261 ? 104.877 83.001  112.390 1.00 24.77 ?  240 LEU C CD1   1 
ATOM   12950 C  CD2   . LEU C 2 261 ? 105.546 85.336  111.695 1.00 24.38 ?  240 LEU C CD2   1 
ATOM   12951 N  N     . GLU C 2 262 ? 103.823 86.179  116.691 1.00 23.41 ?  241 GLU C N     1 
ATOM   12952 C  CA    . GLU C 2 262 ? 102.823 86.643  117.652 1.00 24.02 ?  241 GLU C CA    1 
ATOM   12953 C  C     . GLU C 2 262 ? 103.122 88.064  118.154 1.00 22.91 ?  241 GLU C C     1 
ATOM   12954 O  O     . GLU C 2 262 ? 102.215 88.877  118.277 1.00 22.94 ?  241 GLU C O     1 
ATOM   12955 C  CB    . GLU C 2 262 ? 102.739 85.668  118.827 1.00 24.92 ?  241 GLU C CB    1 
ATOM   12956 C  CG    . GLU C 2 262 ? 102.216 84.288  118.460 1.00 27.82 ?  241 GLU C CG    1 
ATOM   12957 C  CD    . GLU C 2 262 ? 102.122 83.368  119.664 1.00 33.08 ?  241 GLU C CD    1 
ATOM   12958 O  OE1   . GLU C 2 262 ? 103.152 82.781  120.068 1.00 36.94 ?  241 GLU C OE1   1 
ATOM   12959 O  OE2   . GLU C 2 262 ? 101.011 83.224  120.205 1.00 37.48 -1 241 GLU C OE2   1 
ATOM   12960 N  N     . TYR C 2 263 ? 104.394 88.342  118.447 1.00 21.84 ?  242 TYR C N     1 
ATOM   12961 C  CA    . TYR C 2 263 ? 104.860 89.675  118.826 1.00 21.66 ?  242 TYR C CA    1 
ATOM   12962 C  C     . TYR C 2 263 ? 104.567 90.688  117.726 1.00 21.28 ?  242 TYR C C     1 
ATOM   12963 O  O     . TYR C 2 263 ? 104.082 91.795  118.000 1.00 21.14 ?  242 TYR C O     1 
ATOM   12964 C  CB    . TYR C 2 263 ? 106.375 89.642  119.079 1.00 21.44 ?  242 TYR C CB    1 
ATOM   12965 C  CG    . TYR C 2 263 ? 107.013 90.956  119.509 1.00 21.89 ?  242 TYR C CG    1 
ATOM   12966 C  CD1   . TYR C 2 263 ? 106.767 91.496  120.772 1.00 22.52 ?  242 TYR C CD1   1 
ATOM   12967 C  CD2   . TYR C 2 263 ? 107.894 91.637  118.664 1.00 22.58 ?  242 TYR C CD2   1 
ATOM   12968 C  CE1   . TYR C 2 263 ? 107.370 92.687  121.177 1.00 22.67 ?  242 TYR C CE1   1 
ATOM   12969 C  CE2   . TYR C 2 263 ? 108.508 92.830  119.061 1.00 24.03 ?  242 TYR C CE2   1 
ATOM   12970 C  CZ    . TYR C 2 263 ? 108.243 93.341  120.328 1.00 23.75 ?  242 TYR C CZ    1 
ATOM   12971 O  OH    . TYR C 2 263 ? 108.833 94.520  120.738 1.00 26.82 ?  242 TYR C OH    1 
ATOM   12972 N  N     . THR C 2 264 ? 104.865 90.305  116.487 1.00 20.66 ?  243 THR C N     1 
ATOM   12973 C  CA    . THR C 2 264 ? 104.660 91.186  115.329 1.00 20.99 ?  243 THR C CA    1 
ATOM   12974 C  C     . THR C 2 264 ? 103.175 91.527  115.156 1.00 21.22 ?  243 THR C C     1 
ATOM   12975 O  O     . THR C 2 264 ? 102.818 92.702  114.978 1.00 20.95 ?  243 THR C O     1 
ATOM   12976 C  CB    . THR C 2 264 ? 105.238 90.556  114.032 1.00 20.58 ?  243 THR C CB    1 
ATOM   12977 O  OG1   . THR C 2 264 ? 106.659 90.455  114.155 1.00 20.84 ?  243 THR C OG1   1 
ATOM   12978 C  CG2   . THR C 2 264 ? 104.909 91.404  112.801 1.00 20.90 ?  243 THR C CG2   1 
ATOM   12979 N  N     . GLU C 2 265 ? 102.315 90.511  115.240 1.00 21.62 ?  244 GLU C N     1 
ATOM   12980 C  CA    . GLU C 2 265 ? 100.873 90.736  115.123 1.00 23.46 ?  244 GLU C CA    1 
ATOM   12981 C  C     . GLU C 2 265 ? 100.362 91.633  116.232 1.00 23.33 ?  244 GLU C C     1 
ATOM   12982 O  O     . GLU C 2 265 ? 99.569  92.546  115.998 1.00 22.86 ?  244 GLU C O     1 
ATOM   12983 C  CB    . GLU C 2 265 ? 100.096 89.419  115.116 1.00 24.31 ?  244 GLU C CB    1 
ATOM   12984 C  CG    . GLU C 2 265 ? 100.261 88.621  113.827 1.00 27.63 ?  244 GLU C CG    1 
ATOM   12985 C  CD    . GLU C 2 265 ? 99.469  87.317  113.839 1.00 33.27 ?  244 GLU C CD    1 
ATOM   12986 O  OE1   . GLU C 2 265 ? 98.409  87.259  114.503 1.00 35.56 ?  244 GLU C OE1   1 
ATOM   12987 O  OE2   . GLU C 2 265 ? 99.904  86.351  113.173 1.00 35.96 -1 244 GLU C OE2   1 
ATOM   12988 N  N     . ASP C 2 266 ? 100.832 91.373  117.443 1.00 23.36 ?  245 ASP C N     1 
ATOM   12989 C  CA    . ASP C 2 266 ? 100.444 92.166  118.598 1.00 24.18 ?  245 ASP C CA    1 
ATOM   12990 C  C     . ASP C 2 266 ? 100.770 93.661  118.417 1.00 23.96 ?  245 ASP C C     1 
ATOM   12991 O  O     . ASP C 2 266 ? 99.972  94.523  118.778 1.00 24.19 ?  245 ASP C O     1 
ATOM   12992 C  CB    . ASP C 2 266 ? 101.139 91.616  119.841 1.00 25.14 ?  245 ASP C CB    1 
ATOM   12993 C  CG    . ASP C 2 266 ? 100.606 92.215  121.106 1.00 27.35 ?  245 ASP C CG    1 
ATOM   12994 O  OD1   . ASP C 2 266 ? 99.381  92.130  121.333 1.00 28.45 ?  245 ASP C OD1   1 
ATOM   12995 O  OD2   . ASP C 2 266 ? 101.420 92.773  121.873 1.00 31.99 -1 245 ASP C OD2   1 
ATOM   12996 N  N     . LEU C 2 267 ? 101.929 93.960  117.844 1.00 23.34 ?  246 LEU C N     1 
ATOM   12997 C  CA    . LEU C 2 267 ? 102.349 95.352  117.654 1.00 23.53 ?  246 LEU C CA    1 
ATOM   12998 C  C     . LEU C 2 267 ? 101.800 96.017  116.401 1.00 22.94 ?  246 LEU C C     1 
ATOM   12999 O  O     . LEU C 2 267 ? 101.410 97.185  116.437 1.00 23.14 ?  246 LEU C O     1 
ATOM   13000 C  CB    . LEU C 2 267 ? 103.873 95.444  117.631 1.00 23.37 ?  246 LEU C CB    1 
ATOM   13001 C  CG    . LEU C 2 267 ? 104.609 95.235  118.956 1.00 26.17 ?  246 LEU C CG    1 
ATOM   13002 C  CD1   . LEU C 2 267 ? 106.093 95.391  118.708 1.00 27.31 ?  246 LEU C CD1   1 
ATOM   13003 C  CD2   . LEU C 2 267 ? 104.143 96.243  120.001 1.00 28.08 ?  246 LEU C CD2   1 
ATOM   13004 N  N     . TYR C 2 268 ? 101.796 95.281  115.294 1.00 22.46 ?  247 TYR C N     1 
ATOM   13005 C  CA    . TYR C 2 268 ? 101.524 95.880  113.990 1.00 22.00 ?  247 TYR C CA    1 
ATOM   13006 C  C     . TYR C 2 268 ? 100.103 95.803  113.457 1.00 22.26 ?  247 TYR C C     1 
ATOM   13007 O  O     . TYR C 2 268 ? 99.783  96.532  112.517 1.00 22.17 ?  247 TYR C O     1 
ATOM   13008 C  CB    . TYR C 2 268 ? 102.495 95.334  112.935 1.00 21.73 ?  247 TYR C CB    1 
ATOM   13009 C  CG    . TYR C 2 268 ? 103.910 95.833  113.105 1.00 21.49 ?  247 TYR C CG    1 
ATOM   13010 C  CD1   . TYR C 2 268 ? 104.883 95.033  113.711 1.00 19.45 ?  247 TYR C CD1   1 
ATOM   13011 C  CD2   . TYR C 2 268 ? 104.272 97.114  112.674 1.00 22.71 ?  247 TYR C CD2   1 
ATOM   13012 C  CE1   . TYR C 2 268 ? 106.191 95.497  113.879 1.00 20.30 ?  247 TYR C CE1   1 
ATOM   13013 C  CE2   . TYR C 2 268 ? 105.584 97.593  112.830 1.00 21.69 ?  247 TYR C CE2   1 
ATOM   13014 C  CZ    . TYR C 2 268 ? 106.533 96.772  113.420 1.00 21.40 ?  247 TYR C CZ    1 
ATOM   13015 O  OH    . TYR C 2 268 ? 107.815 97.235  113.566 1.00 22.11 ?  247 TYR C OH    1 
ATOM   13016 N  N     . ASP C 2 269 ? 99.258  94.926  114.008 1.00 22.40 ?  248 ASP C N     1 
ATOM   13017 C  CA    . ASP C 2 269 ? 97.863  94.848  113.537 1.00 22.75 ?  248 ASP C CA    1 
ATOM   13018 C  C     . ASP C 2 269 ? 97.157  96.202  113.616 1.00 22.55 ?  248 ASP C C     1 
ATOM   13019 O  O     . ASP C 2 269 ? 96.386  96.553  112.713 1.00 22.22 ?  248 ASP C O     1 
ATOM   13020 C  CB    . ASP C 2 269 ? 97.047  93.770  114.276 1.00 23.03 ?  248 ASP C CB    1 
ATOM   13021 C  CG    . ASP C 2 269 ? 97.288  92.371  113.734 1.00 25.02 ?  248 ASP C CG    1 
ATOM   13022 O  OD1   . ASP C 2 269 ? 97.920  92.217  112.667 1.00 26.85 ?  248 ASP C OD1   1 
ATOM   13023 O  OD2   . ASP C 2 269 ? 96.831  91.406  114.381 1.00 28.74 -1 248 ASP C OD2   1 
ATOM   13024 N  N     . GLN C 2 270 ? 97.430  96.965  114.678 1.00 22.21 ?  249 GLN C N     1 
ATOM   13025 C  CA    . GLN C 2 270 ? 96.783  98.285  114.854 1.00 22.39 ?  249 GLN C CA    1 
ATOM   13026 C  C     . GLN C 2 270 ? 97.236  99.355  113.850 1.00 21.65 ?  249 GLN C C     1 
ATOM   13027 O  O     . GLN C 2 270 ? 96.605  100.407 113.748 1.00 21.70 ?  249 GLN C O     1 
ATOM   13028 C  CB    . GLN C 2 270 ? 96.916  98.802  116.295 1.00 22.53 ?  249 GLN C CB    1 
ATOM   13029 C  CG    . GLN C 2 270 ? 98.362  99.046  116.795 1.00 22.73 ?  249 GLN C CG    1 
ATOM   13030 C  CD    . GLN C 2 270 ? 98.384  99.554  118.222 1.00 25.39 ?  249 GLN C CD    1 
ATOM   13031 O  OE1   . GLN C 2 270 ? 97.389  99.448  118.942 1.00 27.88 ?  249 GLN C OE1   1 
ATOM   13032 N  NE2   . GLN C 2 270 ? 99.512  100.120 118.642 1.00 24.88 ?  249 GLN C NE2   1 
ATOM   13033 N  N     . VAL C 2 271 ? 98.322  99.086  113.123 1.00 20.91 ?  250 VAL C N     1 
ATOM   13034 C  CA    . VAL C 2 271 ? 98.814  100.007 112.073 1.00 20.62 ?  250 VAL C CA    1 
ATOM   13035 C  C     . VAL C 2 271 ? 98.759  99.368  110.673 1.00 20.53 ?  250 VAL C C     1 
ATOM   13036 O  O     . VAL C 2 271 ? 99.159  99.986  109.673 1.00 20.05 ?  250 VAL C O     1 
ATOM   13037 C  CB    . VAL C 2 271 ? 100.235 100.605 112.391 1.00 20.32 ?  250 VAL C CB    1 
ATOM   13038 C  CG1   . VAL C 2 271 ? 100.191 101.481 113.638 1.00 20.35 ?  250 VAL C CG1   1 
ATOM   13039 C  CG2   . VAL C 2 271 ? 101.301 99.512  112.556 1.00 19.32 ?  250 VAL C CG2   1 
ATOM   13040 N  N     . GLY C 2 272 ? 98.250  98.136  110.617 1.00 20.29 ?  251 GLY C N     1 
ATOM   13041 C  CA    . GLY C 2 272 ? 97.954  97.458  109.351 1.00 20.51 ?  251 GLY C CA    1 
ATOM   13042 C  C     . GLY C 2 272 ? 99.142  96.856  108.618 1.00 20.99 ?  251 GLY C C     1 
ATOM   13043 O  O     . GLY C 2 272 ? 99.071  96.624  107.400 1.00 20.22 ?  251 GLY C O     1 
ATOM   13044 N  N     . LEU C 2 273 ? 100.235 96.600  109.344 1.00 20.76 ?  252 LEU C N     1 
ATOM   13045 C  CA    . LEU C 2 273 ? 101.499 96.248  108.688 1.00 21.38 ?  252 LEU C CA    1 
ATOM   13046 C  C     . LEU C 2 273 ? 102.055 94.860  108.994 1.00 21.86 ?  252 LEU C C     1 
ATOM   13047 O  O     . LEU C 2 273 ? 103.158 94.531  108.561 1.00 22.45 ?  252 LEU C O     1 
ATOM   13048 C  CB    . LEU C 2 273 ? 102.568 97.321  108.958 1.00 21.44 ?  252 LEU C CB    1 
ATOM   13049 C  CG    . LEU C 2 273 ? 102.284 98.765  108.538 1.00 22.02 ?  252 LEU C CG    1 
ATOM   13050 C  CD1   . LEU C 2 273 ? 103.441 99.659  108.971 1.00 22.86 ?  252 LEU C CD1   1 
ATOM   13051 C  CD2   . LEU C 2 273 ? 102.040 98.869  107.017 1.00 23.88 ?  252 LEU C CD2   1 
ATOM   13052 N  N     . SER C 2 274 ? 101.295 94.037  109.715 1.00 22.19 ?  253 SER C N     1 
ATOM   13053 C  CA    . SER C 2 274 ? 101.834 92.788  110.249 1.00 22.47 ?  253 SER C CA    1 
ATOM   13054 C  C     . SER C 2 274 ? 102.392 91.857  109.171 1.00 22.94 ?  253 SER C C     1 
ATOM   13055 O  O     . SER C 2 274 ? 103.481 91.315  109.322 1.00 22.07 ?  253 SER C O     1 
ATOM   13056 C  CB    . SER C 2 274 ? 100.776 92.061  111.085 1.00 22.91 ?  253 SER C CB    1 
ATOM   13057 O  OG    . SER C 2 274 ? 100.514 92.797  112.263 1.00 24.25 ?  253 SER C OG    1 
ATOM   13058 N  N     . HIS C 2 275 ? 101.656 91.709  108.072 1.00 24.59 ?  254 HIS C N     1 
ATOM   13059 C  CA    . HIS C 2 275 ? 102.075 90.823  106.979 1.00 25.66 ?  254 HIS C CA    1 
ATOM   13060 C  C     . HIS C 2 275 ? 103.386 91.292  106.328 1.00 26.01 ?  254 HIS C C     1 
ATOM   13061 O  O     . HIS C 2 275 ? 104.264 90.476  105.995 1.00 26.23 ?  254 HIS C O     1 
ATOM   13062 C  CB    . HIS C 2 275 ? 100.960 90.711  105.930 1.00 26.89 ?  254 HIS C CB    1 
ATOM   13063 C  CG    . HIS C 2 275 ? 101.264 89.746  104.827 1.00 29.10 ?  254 HIS C CG    1 
ATOM   13064 N  ND1   . HIS C 2 275 ? 101.618 88.433  105.062 1.00 32.70 ?  254 HIS C ND1   1 
ATOM   13065 C  CD2   . HIS C 2 275 ? 101.266 89.899  103.482 1.00 31.68 ?  254 HIS C CD2   1 
ATOM   13066 C  CE1   . HIS C 2 275 ? 101.827 87.822  103.909 1.00 33.55 ?  254 HIS C CE1   1 
ATOM   13067 N  NE2   . HIS C 2 275 ? 101.605 88.685  102.935 1.00 33.71 ?  254 HIS C NE2   1 
ATOM   13068 N  N     . ASP C 2 276 ? 103.507 92.603  106.152 1.00 25.93 ?  255 ASP C N     1 
ATOM   13069 C  CA    . ASP C 2 276 ? 104.712 93.212  105.598 1.00 26.65 ?  255 ASP C CA    1 
ATOM   13070 C  C     . ASP C 2 276 ? 105.936 92.987  106.488 1.00 25.61 ?  255 ASP C C     1 
ATOM   13071 O  O     . ASP C 2 276 ? 107.007 92.614  105.989 1.00 25.34 ?  255 ASP C O     1 
ATOM   13072 C  CB    . ASP C 2 276 ? 104.498 94.709  105.364 1.00 27.44 ?  255 ASP C CB    1 
ATOM   13073 C  CG    . ASP C 2 276 ? 104.499 95.069  103.895 1.00 32.09 ?  255 ASP C CG    1 
ATOM   13074 O  OD1   . ASP C 2 276 ? 105.386 94.568  103.161 1.00 36.67 ?  255 ASP C OD1   1 
ATOM   13075 O  OD2   . ASP C 2 276 ? 103.610 95.841  103.466 1.00 36.30 -1 255 ASP C OD2   1 
ATOM   13076 N  N     . VAL C 2 277 ? 105.767 93.214  107.794 1.00 24.17 ?  256 VAL C N     1 
ATOM   13077 C  CA    . VAL C 2 277 ? 106.842 92.997  108.771 1.00 23.71 ?  256 VAL C CA    1 
ATOM   13078 C  C     . VAL C 2 277 ? 107.273 91.528  108.792 1.00 23.48 ?  256 VAL C C     1 
ATOM   13079 O  O     . VAL C 2 277 ? 108.466 91.229  108.859 1.00 23.08 ?  256 VAL C O     1 
ATOM   13080 C  CB    . VAL C 2 277 ? 106.441 93.439  110.206 1.00 23.27 ?  256 VAL C CB    1 
ATOM   13081 C  CG1   . VAL C 2 277 ? 107.588 93.201  111.193 1.00 24.02 ?  256 VAL C CG1   1 
ATOM   13082 C  CG2   . VAL C 2 277 ? 106.024 94.904  110.231 1.00 23.35 ?  256 VAL C CG2   1 
ATOM   13083 N  N     . LYS C 2 278 ? 106.303 90.619  108.734 1.00 23.36 ?  257 LYS C N     1 
ATOM   13084 C  CA    . LYS C 2 278 ? 106.590 89.185  108.695 1.00 24.12 ?  257 LYS C CA    1 
ATOM   13085 C  C     . LYS C 2 278 ? 107.501 88.797  107.532 1.00 24.30 ?  257 LYS C C     1 
ATOM   13086 O  O     . LYS C 2 278 ? 108.418 87.979  107.696 1.00 24.37 ?  257 LYS C O     1 
ATOM   13087 C  CB    . LYS C 2 278 ? 105.300 88.366  108.652 1.00 24.22 ?  257 LYS C CB    1 
ATOM   13088 C  CG    . LYS C 2 278 ? 104.555 88.319  109.974 1.00 24.96 ?  257 LYS C CG    1 
ATOM   13089 C  CD    . LYS C 2 278 ? 103.222 87.608  109.782 1.00 26.34 ?  257 LYS C CD    1 
ATOM   13090 C  CE    . LYS C 2 278 ? 102.425 87.572  111.057 1.00 27.16 ?  257 LYS C CE    1 
ATOM   13091 N  NZ    . LYS C 2 278 ? 101.139 86.856  110.803 1.00 29.60 1  257 LYS C NZ    1 
ATOM   13092 N  N     . LYS C 2 279 ? 107.256 89.384  106.362 1.00 24.55 ?  258 LYS C N     1 
ATOM   13093 C  CA    . LYS C 2 279 ? 108.124 89.154  105.210 1.00 24.85 ?  258 LYS C CA    1 
ATOM   13094 C  C     . LYS C 2 279 ? 109.540 89.645  105.502 1.00 24.57 ?  258 LYS C C     1 
ATOM   13095 O  O     . LYS C 2 279 ? 110.512 88.980  105.146 1.00 24.07 ?  258 LYS C O     1 
ATOM   13096 C  CB    . LYS C 2 279 ? 107.572 89.853  103.968 1.00 25.30 ?  258 LYS C CB    1 
ATOM   13097 C  CG    . LYS C 2 279 ? 106.206 89.365  103.541 1.00 26.63 ?  258 LYS C CG    1 
ATOM   13098 C  CD    . LYS C 2 279 ? 105.756 90.132  102.303 1.00 29.30 ?  258 LYS C CD    1 
ATOM   13099 C  CE    . LYS C 2 279 ? 104.478 89.566  101.762 1.00 31.79 ?  258 LYS C CE    1 
ATOM   13100 N  NZ    . LYS C 2 279 ? 103.887 90.523  100.794 1.00 33.80 1  258 LYS C NZ    1 
ATOM   13101 N  N     . PHE C 2 280 ? 109.640 90.791  106.177 1.00 24.29 ?  259 PHE C N     1 
ATOM   13102 C  CA    . PHE C 2 280 ? 110.931 91.400  106.523 1.00 24.90 ?  259 PHE C CA    1 
ATOM   13103 C  C     . PHE C 2 280 ? 111.741 90.535  107.504 1.00 24.86 ?  259 PHE C C     1 
ATOM   13104 O  O     . PHE C 2 280 ? 112.952 90.354  107.332 1.00 24.68 ?  259 PHE C O     1 
ATOM   13105 C  CB    . PHE C 2 280 ? 110.694 92.813  107.074 1.00 24.70 ?  259 PHE C CB    1 
ATOM   13106 C  CG    . PHE C 2 280 ? 111.944 93.644  107.248 1.00 25.70 ?  259 PHE C CG    1 
ATOM   13107 C  CD1   . PHE C 2 280 ? 112.780 93.923  106.166 1.00 26.86 ?  259 PHE C CD1   1 
ATOM   13108 C  CD2   . PHE C 2 280 ? 112.261 94.190  108.499 1.00 26.19 ?  259 PHE C CD2   1 
ATOM   13109 C  CE1   . PHE C 2 280 ? 113.926 94.715  106.324 1.00 26.66 ?  259 PHE C CE1   1 
ATOM   13110 C  CE2   . PHE C 2 280 ? 113.398 94.987  108.665 1.00 26.52 ?  259 PHE C CE2   1 
ATOM   13111 C  CZ    . PHE C 2 280 ? 114.237 95.245  107.573 1.00 26.23 ?  259 PHE C CZ    1 
ATOM   13112 N  N     . ILE C 2 281 ? 111.072 89.993  108.523 1.00 25.53 ?  260 ILE C N     1 
ATOM   13113 C  CA    . ILE C 2 281 ? 111.763 89.158  109.509 1.00 26.21 ?  260 ILE C CA    1 
ATOM   13114 C  C     . ILE C 2 281 ? 112.233 87.825  108.908 1.00 26.47 ?  260 ILE C C     1 
ATOM   13115 O  O     . ILE C 2 281 ? 113.289 87.323  109.282 1.00 26.52 ?  260 ILE C O     1 
ATOM   13116 C  CB    . ILE C 2 281 ? 110.970 88.978  110.849 1.00 26.27 ?  260 ILE C CB    1 
ATOM   13117 C  CG1   . ILE C 2 281 ? 109.845 87.948  110.716 1.00 27.37 ?  260 ILE C CG1   1 
ATOM   13118 C  CG2   . ILE C 2 281 ? 110.466 90.343  111.368 1.00 26.92 ?  260 ILE C CG2   1 
ATOM   13119 C  CD1   . ILE C 2 281 ? 109.082 87.679  112.014 1.00 29.51 ?  260 ILE C CD1   1 
ATOM   13120 N  N     . ARG C 2 282 ? 111.474 87.285  107.953 1.00 26.57 ?  261 ARG C N     1 
ATOM   13121 C  CA    . ARG C 2 282 ? 111.890 86.071  107.246 1.00 26.84 ?  261 ARG C CA    1 
ATOM   13122 C  C     . ARG C 2 282 ? 113.134 86.333  106.398 1.00 27.34 ?  261 ARG C C     1 
ATOM   13123 O  O     . ARG C 2 282 ? 114.069 85.538  106.400 1.00 27.54 ?  261 ARG C O     1 
ATOM   13124 C  CB    . ARG C 2 282 ? 110.756 85.497  106.392 1.00 26.98 ?  261 ARG C CB    1 
ATOM   13125 C  CG    . ARG C 2 282 ? 109.723 84.708  107.173 1.00 26.53 ?  261 ARG C CG    1 
ATOM   13126 C  CD    . ARG C 2 282 ? 108.781 83.921  106.238 1.00 27.77 ?  261 ARG C CD    1 
ATOM   13127 N  NE    . ARG C 2 282 ? 107.873 84.786  105.490 1.00 28.67 ?  261 ARG C NE    1 
ATOM   13128 C  CZ    . ARG C 2 282 ? 106.701 85.232  105.947 1.00 29.68 ?  261 ARG C CZ    1 
ATOM   13129 N  NH1   . ARG C 2 282 ? 106.273 84.899  107.164 1.00 28.31 1  261 ARG C NH1   1 
ATOM   13130 N  NH2   . ARG C 2 282 ? 105.949 86.007  105.183 1.00 29.15 ?  261 ARG C NH2   1 
ATOM   13131 N  N     . TYR C 2 283 ? 113.131 87.462  105.690 1.00 27.78 ?  262 TYR C N     1 
ATOM   13132 C  CA    . TYR C 2 283 ? 114.289 87.939  104.937 1.00 28.18 ?  262 TYR C CA    1 
ATOM   13133 C  C     . TYR C 2 283 ? 115.547 87.991  105.824 1.00 27.08 ?  262 TYR C C     1 
ATOM   13134 O  O     . TYR C 2 283 ? 116.613 87.465  105.467 1.00 26.51 ?  262 TYR C O     1 
ATOM   13135 C  CB    . TYR C 2 283 ? 113.982 89.329  104.365 1.00 29.11 ?  262 TYR C CB    1 
ATOM   13136 C  CG    . TYR C 2 283 ? 115.093 89.937  103.544 1.00 32.56 ?  262 TYR C CG    1 
ATOM   13137 C  CD1   . TYR C 2 283 ? 115.346 89.493  102.245 1.00 36.59 ?  262 TYR C CD1   1 
ATOM   13138 C  CD2   . TYR C 2 283 ? 115.883 90.971  104.057 1.00 36.34 ?  262 TYR C CD2   1 
ATOM   13139 C  CE1   . TYR C 2 283 ? 116.369 90.053  101.473 1.00 39.47 ?  262 TYR C CE1   1 
ATOM   13140 C  CE2   . TYR C 2 283 ? 116.912 91.546  103.286 1.00 39.23 ?  262 TYR C CE2   1 
ATOM   13141 C  CZ    . TYR C 2 283 ? 117.145 91.076  101.998 1.00 40.48 ?  262 TYR C CZ    1 
ATOM   13142 O  OH    . TYR C 2 283 ? 118.148 91.621  101.229 1.00 44.00 ?  262 TYR C OH    1 
ATOM   13143 N  N     . ASN C 2 284 ? 115.407 88.603  106.992 1.00 26.08 ?  263 ASN C N     1 
ATOM   13144 C  CA    . ASN C 2 284 ? 116.525 88.723  107.914 1.00 25.73 ?  263 ASN C CA    1 
ATOM   13145 C  C     . ASN C 2 284 ? 116.914 87.427  108.629 1.00 25.24 ?  263 ASN C C     1 
ATOM   13146 O  O     . ASN C 2 284 ? 118.100 87.217  108.917 1.00 25.56 ?  263 ASN C O     1 
ATOM   13147 C  CB    . ASN C 2 284 ? 116.295 89.888  108.878 1.00 25.69 ?  263 ASN C CB    1 
ATOM   13148 C  CG    . ASN C 2 284 ? 116.503 91.227  108.206 1.00 26.39 ?  263 ASN C CG    1 
ATOM   13149 O  OD1   . ASN C 2 284 ? 117.639 91.642  107.963 1.00 26.91 ?  263 ASN C OD1   1 
ATOM   13150 N  ND2   . ASN C 2 284 ? 115.410 91.908  107.891 1.00 27.56 ?  263 ASN C ND2   1 
ATOM   13151 N  N     . ALA C 2 285 ? 115.941 86.549  108.887 1.00 24.51 ?  264 ALA C N     1 
ATOM   13152 C  CA    . ALA C 2 285 ? 116.252 85.186  109.357 1.00 24.19 ?  264 ALA C CA    1 
ATOM   13153 C  C     . ALA C 2 285 ? 117.235 84.459  108.417 1.00 24.63 ?  264 ALA C C     1 
ATOM   13154 O  O     . ALA C 2 285 ? 118.174 83.810  108.875 1.00 24.01 ?  264 ALA C O     1 
ATOM   13155 C  CB    . ALA C 2 285 ? 114.989 84.362  109.528 1.00 23.63 ?  264 ALA C CB    1 
ATOM   13156 N  N     . ASN C 2 286 ? 117.011 84.576  107.109 1.00 24.66 ?  265 ASN C N     1 
ATOM   13157 C  CA    . ASN C 2 286 ? 117.929 84.017  106.117 1.00 25.24 ?  265 ASN C CA    1 
ATOM   13158 C  C     . ASN C 2 286 ? 119.342 84.587  106.187 1.00 25.09 ?  265 ASN C C     1 
ATOM   13159 O  O     . ASN C 2 286 ? 120.317 83.849  105.967 1.00 24.14 ?  265 ASN C O     1 
ATOM   13160 C  CB    . ASN C 2 286 ? 117.373 84.173  104.689 1.00 25.62 ?  265 ASN C CB    1 
ATOM   13161 C  CG    . ASN C 2 286 ? 116.237 83.204  104.399 1.00 26.46 ?  265 ASN C CG    1 
ATOM   13162 O  OD1   . ASN C 2 286 ? 115.994 82.264  105.159 1.00 27.14 ?  265 ASN C OD1   1 
ATOM   13163 N  ND2   . ASN C 2 286 ? 115.521 83.442  103.298 1.00 27.89 ?  265 ASN C ND2   1 
ATOM   13164 N  N     . LYS C 2 287 ? 119.439 85.888  106.472 1.00 24.99 ?  266 LYS C N     1 
ATOM   13165 C  CA    . LYS C 2 287 ? 120.722 86.569  106.661 1.00 25.91 ?  266 LYS C CA    1 
ATOM   13166 C  C     . LYS C 2 287 ? 121.430 86.066  107.915 1.00 25.23 ?  266 LYS C C     1 
ATOM   13167 O  O     . LYS C 2 287 ? 122.651 85.894  107.912 1.00 25.34 ?  266 LYS C O     1 
ATOM   13168 C  CB    . LYS C 2 287 ? 120.542 88.082  106.777 1.00 25.96 ?  266 LYS C CB    1 
ATOM   13169 C  CG    . LYS C 2 287 ? 120.241 88.816  105.480 1.00 29.60 ?  266 LYS C CG    1 
ATOM   13170 C  CD    . LYS C 2 287 ? 120.357 90.326  105.729 1.00 34.20 ?  266 LYS C CD    1 
ATOM   13171 C  CE    . LYS C 2 287 ? 120.171 91.135  104.469 1.00 37.67 ?  266 LYS C CE    1 
ATOM   13172 N  NZ    . LYS C 2 287 ? 120.434 92.585  104.748 1.00 39.48 1  266 LYS C NZ    1 
ATOM   13173 N  N     . ALA C 2 288 ? 120.669 85.849  108.984 1.00 24.87 ?  267 ALA C N     1 
ATOM   13174 C  CA    . ALA C 2 288 ? 121.220 85.251  110.215 1.00 24.23 ?  267 ALA C CA    1 
ATOM   13175 C  C     . ALA C 2 288 ? 121.772 83.843  109.955 1.00 24.24 ?  267 ALA C C     1 
ATOM   13176 O  O     . ALA C 2 288 ? 122.885 83.520  110.373 1.00 23.96 ?  267 ALA C O     1 
ATOM   13177 C  CB    . ALA C 2 288 ? 120.173 85.219  111.312 1.00 24.23 ?  267 ALA C CB    1 
ATOM   13178 N  N     . LEU C 2 289 ? 120.997 83.009  109.262 1.00 24.63 ?  268 LEU C N     1 
ATOM   13179 C  CA    . LEU C 2 289 ? 121.467 81.673  108.890 1.00 25.14 ?  268 LEU C CA    1 
ATOM   13180 C  C     . LEU C 2 289 ? 122.743 81.762  108.068 1.00 25.58 ?  268 LEU C C     1 
ATOM   13181 O  O     . LEU C 2 289 ? 123.693 81.028  108.314 1.00 25.42 ?  268 LEU C O     1 
ATOM   13182 C  CB    . LEU C 2 289 ? 120.393 80.877  108.132 1.00 25.28 ?  268 LEU C CB    1 
ATOM   13183 C  CG    . LEU C 2 289 ? 119.235 80.359  108.990 1.00 25.93 ?  268 LEU C CG    1 
ATOM   13184 C  CD1   . LEU C 2 289 ? 118.041 80.002  108.127 1.00 26.50 ?  268 LEU C CD1   1 
ATOM   13185 C  CD2   . LEU C 2 289 ? 119.650 79.179  109.889 1.00 25.20 ?  268 LEU C CD2   1 
ATOM   13186 N  N     . MET C 2 290 ? 122.772 82.681  107.102 1.00 26.32 ?  269 MET C N     1 
ATOM   13187 C  CA    . MET C 2 290 ? 123.964 82.845  106.276 1.00 27.41 ?  269 MET C CA    1 
ATOM   13188 C  C     . MET C 2 290 ? 125.186 83.287  107.078 1.00 26.66 ?  269 MET C C     1 
ATOM   13189 O  O     . MET C 2 290 ? 126.295 82.812  106.821 1.00 26.69 ?  269 MET C O     1 
ATOM   13190 C  CB    . MET C 2 290 ? 123.694 83.763  105.088 1.00 28.28 ?  269 MET C CB    1 
ATOM   13191 C  CG    . MET C 2 290 ? 123.223 82.973  103.868 1.00 32.91 ?  269 MET C CG    1 
ATOM   13192 S  SD    . MET C 2 290 ? 122.570 84.018  102.562 1.00 42.49 ?  269 MET C SD    1 
ATOM   13193 C  CE    . MET C 2 290 ? 120.813 83.696  102.708 1.00 38.74 ?  269 MET C CE    1 
ATOM   13194 N  N     . ASN C 2 291 ? 124.976 84.159  108.065 1.00 25.48 ?  270 ASN C N     1 
ATOM   13195 C  CA    . ASN C 2 291 ? 126.046 84.581  108.984 1.00 25.39 ?  270 ASN C CA    1 
ATOM   13196 C  C     . ASN C 2 291 ? 126.641 83.397  109.763 1.00 25.18 ?  270 ASN C C     1 
ATOM   13197 O  O     . ASN C 2 291 ? 127.812 83.428  110.170 1.00 24.73 ?  270 ASN C O     1 
ATOM   13198 C  CB    . ASN C 2 291 ? 125.539 85.658  109.951 1.00 24.83 ?  270 ASN C CB    1 
ATOM   13199 C  CG    . ASN C 2 291 ? 125.386 87.031  109.285 1.00 25.58 ?  270 ASN C CG    1 
ATOM   13200 O  OD1   . ASN C 2 291 ? 125.871 87.260  108.182 1.00 25.58 ?  270 ASN C OD1   1 
ATOM   13201 N  ND2   . ASN C 2 291 ? 124.707 87.941  109.965 1.00 24.32 ?  270 ASN C ND2   1 
ATOM   13202 N  N     . LEU C 2 292 ? 125.824 82.354  109.931 1.00 25.09 ?  271 LEU C N     1 
ATOM   13203 C  CA    . LEU C 2 292 ? 126.217 81.097  110.582 1.00 25.46 ?  271 LEU C CA    1 
ATOM   13204 C  C     . LEU C 2 292 ? 126.744 80.022  109.618 1.00 26.18 ?  271 LEU C C     1 
ATOM   13205 O  O     . LEU C 2 292 ? 127.086 78.901  110.037 1.00 26.06 ?  271 LEU C O     1 
ATOM   13206 C  CB    . LEU C 2 292 ? 125.042 80.555  111.406 1.00 25.19 ?  271 LEU C CB    1 
ATOM   13207 C  CG    . LEU C 2 292 ? 124.622 81.417  112.608 1.00 25.03 ?  271 LEU C CG    1 
ATOM   13208 C  CD1   . LEU C 2 292 ? 123.290 80.955  113.154 1.00 24.50 ?  271 LEU C CD1   1 
ATOM   13209 C  CD2   . LEU C 2 292 ? 125.705 81.382  113.699 1.00 25.64 ?  271 LEU C CD2   1 
ATOM   13210 N  N     . GLY C 2 293 ? 126.815 80.362  108.332 1.00 26.71 ?  272 GLY C N     1 
ATOM   13211 C  CA    . GLY C 2 293 ? 127.283 79.427  107.301 1.00 28.06 ?  272 GLY C CA    1 
ATOM   13212 C  C     . GLY C 2 293 ? 126.261 78.390  106.861 1.00 29.34 ?  272 GLY C C     1 
ATOM   13213 O  O     . GLY C 2 293 ? 126.628 77.333  106.326 1.00 29.73 ?  272 GLY C O     1 
ATOM   13214 N  N     . PHE C 2 294 ? 124.981 78.686  107.081 1.00 29.88 ?  273 PHE C N     1 
ATOM   13215 C  CA    . PHE C 2 294 ? 123.893 77.782  106.718 1.00 31.24 ?  273 PHE C CA    1 
ATOM   13216 C  C     . PHE C 2 294 ? 123.099 78.322  105.520 1.00 32.42 ?  273 PHE C C     1 
ATOM   13217 O  O     . PHE C 2 294 ? 123.112 79.530  105.242 1.00 32.30 ?  273 PHE C O     1 
ATOM   13218 C  CB    . PHE C 2 294 ? 122.961 77.539  107.911 1.00 30.82 ?  273 PHE C CB    1 
ATOM   13219 C  CG    . PHE C 2 294 ? 123.638 76.906  109.109 1.00 30.93 ?  273 PHE C CG    1 
ATOM   13220 C  CD1   . PHE C 2 294 ? 124.451 75.782  108.967 1.00 30.85 ?  273 PHE C CD1   1 
ATOM   13221 C  CD2   . PHE C 2 294 ? 123.449 77.430  110.380 1.00 30.30 ?  273 PHE C CD2   1 
ATOM   13222 C  CE1   . PHE C 2 294 ? 125.076 75.206  110.071 1.00 30.75 ?  273 PHE C CE1   1 
ATOM   13223 C  CE2   . PHE C 2 294 ? 124.057 76.853  111.497 1.00 30.41 ?  273 PHE C CE2   1 
ATOM   13224 C  CZ    . PHE C 2 294 ? 124.868 75.735  111.343 1.00 30.88 ?  273 PHE C CZ    1 
ATOM   13225 N  N     . ASP C 2 295 ? 122.429 77.417  104.811 1.00 33.81 ?  274 ASP C N     1 
ATOM   13226 C  CA    . ASP C 2 295 ? 121.568 77.776  103.680 1.00 35.32 ?  274 ASP C CA    1 
ATOM   13227 C  C     . ASP C 2 295 ? 120.312 78.537  104.141 1.00 35.36 ?  274 ASP C C     1 
ATOM   13228 O  O     . ASP C 2 295 ? 119.815 78.291  105.237 1.00 34.78 ?  274 ASP C O     1 
ATOM   13229 C  CB    . ASP C 2 295 ? 121.135 76.513  102.923 1.00 35.95 ?  274 ASP C CB    1 
ATOM   13230 C  CG    . ASP C 2 295 ? 122.304 75.768  102.285 1.00 37.98 ?  274 ASP C CG    1 
ATOM   13231 O  OD1   . ASP C 2 295 ? 123.333 76.396  101.953 1.00 39.83 ?  274 ASP C OD1   1 
ATOM   13232 O  OD2   . ASP C 2 295 ? 122.184 74.536  102.110 1.00 40.03 -1 274 ASP C OD2   1 
ATOM   13233 N  N     . PRO C 2 296 ? 119.792 79.453  103.302 1.00 36.33 ?  275 PRO C N     1 
ATOM   13234 C  CA    . PRO C 2 296 ? 118.515 80.131  103.618 1.00 36.92 ?  275 PRO C CA    1 
ATOM   13235 C  C     . PRO C 2 296 ? 117.361 79.143  103.854 1.00 37.68 ?  275 PRO C C     1 
ATOM   13236 O  O     . PRO C 2 296 ? 117.298 78.099  103.200 1.00 38.07 ?  275 PRO C O     1 
ATOM   13237 C  CB    . PRO C 2 296 ? 118.245 80.988  102.372 1.00 36.82 ?  275 PRO C CB    1 
ATOM   13238 C  CG    . PRO C 2 296 ? 119.208 80.479  101.308 1.00 37.42 ?  275 PRO C CG    1 
ATOM   13239 C  CD    . PRO C 2 296 ? 120.393 79.968  102.058 1.00 36.41 ?  275 PRO C CD    1 
ATOM   13240 N  N     . TYR C 2 297 ? 116.465 79.477  104.784 1.00 38.10 ?  276 TYR C N     1 
ATOM   13241 C  CA    . TYR C 2 297 ? 115.386 78.575  105.211 1.00 38.96 ?  276 TYR C CA    1 
ATOM   13242 C  C     . TYR C 2 297 ? 114.008 79.006  104.692 1.00 39.71 ?  276 TYR C C     1 
ATOM   13243 O  O     . TYR C 2 297 ? 113.120 78.169  104.498 1.00 40.18 ?  276 TYR C O     1 
ATOM   13244 C  CB    . TYR C 2 297 ? 115.368 78.502  106.742 1.00 38.94 ?  276 TYR C CB    1 
ATOM   13245 C  CG    . TYR C 2 297 ? 114.392 77.538  107.383 1.00 39.64 ?  276 TYR C CG    1 
ATOM   13246 C  CD1   . TYR C 2 297 ? 114.694 76.180  107.509 1.00 40.43 ?  276 TYR C CD1   1 
ATOM   13247 C  CD2   . TYR C 2 297 ? 113.193 77.994  107.922 1.00 41.04 ?  276 TYR C CD2   1 
ATOM   13248 C  CE1   . TYR C 2 297 ? 113.803 75.296  108.119 1.00 41.69 ?  276 TYR C CE1   1 
ATOM   13249 C  CE2   . TYR C 2 297 ? 112.292 77.121  108.532 1.00 41.60 ?  276 TYR C CE2   1 
ATOM   13250 C  CZ    . TYR C 2 297 ? 112.605 75.776  108.632 1.00 41.92 ?  276 TYR C CZ    1 
ATOM   13251 O  OH    . TYR C 2 297 ? 111.717 74.918  109.245 1.00 42.52 ?  276 TYR C OH    1 
ATOM   13252 N  N     . PHE C 2 298 ? 113.827 80.305  104.485 1.00 39.85 ?  277 PHE C N     1 
ATOM   13253 C  CA    . PHE C 2 298 ? 112.551 80.826  104.008 1.00 40.77 ?  277 PHE C CA    1 
ATOM   13254 C  C     . PHE C 2 298 ? 112.650 81.227  102.544 1.00 41.95 ?  277 PHE C C     1 
ATOM   13255 O  O     . PHE C 2 298 ? 113.715 81.636  102.084 1.00 41.91 ?  277 PHE C O     1 
ATOM   13256 C  CB    . PHE C 2 298 ? 112.111 82.025  104.856 1.00 39.94 ?  277 PHE C CB    1 
ATOM   13257 C  CG    . PHE C 2 298 ? 111.853 81.690  106.300 1.00 39.09 ?  277 PHE C CG    1 
ATOM   13258 C  CD1   . PHE C 2 298 ? 112.746 82.085  107.288 1.00 37.84 ?  277 PHE C CD1   1 
ATOM   13259 C  CD2   . PHE C 2 298 ? 110.707 80.993  106.674 1.00 38.97 ?  277 PHE C CD2   1 
ATOM   13260 C  CE1   . PHE C 2 298 ? 112.513 81.786  108.628 1.00 37.46 ?  277 PHE C CE1   1 
ATOM   13261 C  CE2   . PHE C 2 298 ? 110.462 80.687  108.007 1.00 38.20 ?  277 PHE C CE2   1 
ATOM   13262 C  CZ    . PHE C 2 298 ? 111.367 81.086  108.989 1.00 37.91 ?  277 PHE C CZ    1 
ATOM   13263 N  N     . GLU C 2 299 ? 111.546 81.108  101.806 1.00 43.74 ?  278 GLU C N     1 
ATOM   13264 C  CA    . GLU C 2 299 ? 111.540 81.517  100.398 1.00 45.61 ?  278 GLU C CA    1 
ATOM   13265 C  C     . GLU C 2 299 ? 111.566 83.042  100.280 1.00 46.04 ?  278 GLU C C     1 
ATOM   13266 O  O     . GLU C 2 299 ? 111.056 83.749  101.150 1.00 45.88 ?  278 GLU C O     1 
ATOM   13267 C  CB    . GLU C 2 299 ? 110.337 80.944  99.641  1.00 46.43 ?  278 GLU C CB    1 
ATOM   13268 C  CG    . GLU C 2 299 ? 110.622 80.684  98.152  1.00 48.82 ?  278 GLU C CG    1 
ATOM   13269 C  CD    . GLU C 2 299 ? 109.366 80.601  97.298  1.00 51.86 ?  278 GLU C CD    1 
ATOM   13270 O  OE1   . GLU C 2 299 ? 109.502 80.407  96.068  1.00 53.35 ?  278 GLU C OE1   1 
ATOM   13271 O  OE2   . GLU C 2 299 ? 108.245 80.733  97.843  1.00 53.10 -1 278 GLU C OE2   1 
ATOM   13272 N  N     . GLU C 2 300 ? 112.178 83.536  99.205  1.00 47.16 ?  279 GLU C N     1 
ATOM   13273 C  CA    . GLU C 2 300 ? 112.272 84.975  98.936  1.00 47.75 ?  279 GLU C CA    1 
ATOM   13274 C  C     . GLU C 2 300 ? 110.902 85.615  98.667  1.00 47.71 ?  279 GLU C C     1 
ATOM   13275 O  O     . GLU C 2 300 ? 110.042 85.012  98.015  1.00 47.77 ?  279 GLU C O     1 
ATOM   13276 C  CB    . GLU C 2 300 ? 113.243 85.239  97.772  1.00 48.42 ?  279 GLU C CB    1 
ATOM   13277 C  CG    . GLU C 2 300 ? 112.978 84.406  96.512  1.00 50.63 ?  279 GLU C CG    1 
ATOM   13278 C  CD    . GLU C 2 300 ? 114.210 84.257  95.619  1.00 53.06 ?  279 GLU C CD    1 
ATOM   13279 O  OE1   . GLU C 2 300 ? 114.813 85.290  95.240  1.00 54.35 ?  279 GLU C OE1   1 
ATOM   13280 O  OE2   . GLU C 2 300 ? 114.567 83.104  95.286  1.00 53.32 -1 279 GLU C OE2   1 
ATOM   13281 N  N     . GLU C 2 301 ? 110.711 86.825  99.194  1.00 47.40 ?  280 GLU C N     1 
ATOM   13282 C  CA    . GLU C 2 301 ? 109.478 87.603  99.009  1.00 47.46 ?  280 GLU C CA    1 
ATOM   13283 C  C     . GLU C 2 301 ? 109.807 89.079  98.753  1.00 47.31 ?  280 GLU C C     1 
ATOM   13284 O  O     . GLU C 2 301 ? 110.880 89.553  99.136  1.00 47.21 ?  280 GLU C O     1 
ATOM   13285 C  CB    . GLU C 2 301 ? 108.575 87.496  100.246 1.00 47.19 ?  280 GLU C CB    1 
ATOM   13286 C  CG    . GLU C 2 301 ? 108.092 86.088  100.601 1.00 47.14 ?  280 GLU C CG    1 
ATOM   13287 C  CD    . GLU C 2 301 ? 107.657 85.973  102.059 1.00 47.21 ?  280 GLU C CD    1 
ATOM   13288 O  OE1   . GLU C 2 301 ? 106.437 85.892  102.309 1.00 46.97 ?  280 GLU C OE1   1 
ATOM   13289 O  OE2   . GLU C 2 301 ? 108.535 85.975  102.956 1.00 46.13 -1 280 GLU C OE2   1 
ATOM   13290 N  N     . ASP C 2 302 ? 108.885 89.798  98.113  1.00 47.15 ?  281 ASP C N     1 
ATOM   13291 C  CA    . ASP C 2 302 ? 109.061 91.234  97.869  1.00 47.04 ?  281 ASP C CA    1 
ATOM   13292 C  C     . ASP C 2 302 ? 108.842 92.035  99.156  1.00 46.05 ?  281 ASP C C     1 
ATOM   13293 O  O     . ASP C 2 302 ? 107.753 92.002  99.739  1.00 46.10 ?  281 ASP C O     1 
ATOM   13294 C  CB    . ASP C 2 302 ? 108.109 91.738  96.769  1.00 47.66 ?  281 ASP C CB    1 
ATOM   13295 C  CG    . ASP C 2 302 ? 108.517 91.283  95.364  1.00 49.53 ?  281 ASP C CG    1 
ATOM   13296 O  OD1   . ASP C 2 302 ? 109.731 91.172  95.082  1.00 50.58 ?  281 ASP C OD1   1 
ATOM   13297 O  OD2   . ASP C 2 302 ? 107.608 91.061  94.527  1.00 51.14 -1 281 ASP C OD2   1 
ATOM   13298 N  N     . ILE C 2 303 ? 109.885 92.736  99.597  1.00 44.96 ?  282 ILE C N     1 
ATOM   13299 C  CA    . ILE C 2 303 ? 109.816 93.610  100.772 1.00 43.99 ?  282 ILE C CA    1 
ATOM   13300 C  C     . ILE C 2 303 ? 109.288 94.988  100.360 1.00 43.53 ?  282 ILE C C     1 
ATOM   13301 O  O     . ILE C 2 303 ? 109.555 95.443  99.247  1.00 43.52 ?  282 ILE C O     1 
ATOM   13302 C  CB    . ILE C 2 303 ? 111.209 93.757  101.452 1.00 43.84 ?  282 ILE C CB    1 
ATOM   13303 C  CG1   . ILE C 2 303 ? 111.811 92.381  101.799 1.00 43.91 ?  282 ILE C CG1   1 
ATOM   13304 C  CG2   . ILE C 2 303 ? 111.146 94.682  102.680 1.00 43.55 ?  282 ILE C CG2   1 
ATOM   13305 C  CD1   . ILE C 2 303 ? 110.966 91.514  102.737 1.00 42.76 ?  282 ILE C CD1   1 
ATOM   13306 N  N     . ASN C 2 304 ? 108.534 95.636  101.249 1.00 42.51 ?  283 ASN C N     1 
ATOM   13307 C  CA    . ASN C 2 304 ? 108.019 96.982  100.996 1.00 41.93 ?  283 ASN C CA    1 
ATOM   13308 C  C     . ASN C 2 304 ? 109.150 97.909  100.521 1.00 41.78 ?  283 ASN C C     1 
ATOM   13309 O  O     . ASN C 2 304 ? 110.147 98.081  101.236 1.00 41.13 ?  283 ASN C O     1 
ATOM   13310 C  CB    . ASN C 2 304 ? 107.355 97.545  102.262 1.00 41.83 ?  283 ASN C CB    1 
ATOM   13311 C  CG    . ASN C 2 304 ? 106.386 98.691  101.972 1.00 41.27 ?  283 ASN C CG    1 
ATOM   13312 O  OD1   . ASN C 2 304 ? 106.682 99.601  101.201 1.00 41.28 ?  283 ASN C OD1   1 
ATOM   13313 N  ND2   . ASN C 2 304 ? 105.223 98.647  102.605 1.00 40.67 ?  283 ASN C ND2   1 
ATOM   13314 N  N     . PRO C 2 305 ? 109.010 98.492  99.305  1.00 41.74 ?  284 PRO C N     1 
ATOM   13315 C  CA    . PRO C 2 305 ? 110.087 99.330  98.752  1.00 41.82 ?  284 PRO C CA    1 
ATOM   13316 C  C     . PRO C 2 305 ? 110.370 100.579 99.594  1.00 41.56 ?  284 PRO C C     1 
ATOM   13317 O  O     . PRO C 2 305 ? 111.470 101.131 99.523  1.00 41.46 ?  284 PRO C O     1 
ATOM   13318 C  CB    . PRO C 2 305 ? 109.573 99.707  97.349  1.00 42.14 ?  284 PRO C CB    1 
ATOM   13319 C  CG    . PRO C 2 305 ? 108.103 99.505  97.400  1.00 42.59 ?  284 PRO C CG    1 
ATOM   13320 C  CD    . PRO C 2 305 ? 107.872 98.374  98.373  1.00 42.05 ?  284 PRO C CD    1 
ATOM   13321 N  N     . ILE C 2 306 ? 109.390 101.000 100.390 1.00 41.19 ?  285 ILE C N     1 
ATOM   13322 C  CA    . ILE C 2 306 ? 109.563 102.105 101.334 1.00 41.47 ?  285 ILE C CA    1 
ATOM   13323 C  C     . ILE C 2 306 ? 110.669 101.774 102.344 1.00 41.71 ?  285 ILE C C     1 
ATOM   13324 O  O     . ILE C 2 306 ? 111.547 102.595 102.605 1.00 41.38 ?  285 ILE C O     1 
ATOM   13325 C  CB    . ILE C 2 306 ? 108.244 102.418 102.090 1.00 41.22 ?  285 ILE C CB    1 
ATOM   13326 C  CG1   . ILE C 2 306 ? 107.149 102.862 101.111 1.00 41.27 ?  285 ILE C CG1   1 
ATOM   13327 C  CG2   . ILE C 2 306 ? 108.473 103.465 103.178 1.00 40.37 ?  285 ILE C CG2   1 
ATOM   13328 C  CD1   . ILE C 2 306 ? 105.746 102.825 101.702 1.00 41.85 ?  285 ILE C CD1   1 
ATOM   13329 N  N     . VAL C 2 307 ? 110.611 100.563 102.897 1.00 42.33 ?  286 VAL C N     1 
ATOM   13330 C  CA    . VAL C 2 307 ? 111.610 100.077 103.855 1.00 43.36 ?  286 VAL C CA    1 
ATOM   13331 C  C     . VAL C 2 307 ? 113.003 99.956  103.223 1.00 44.51 ?  286 VAL C C     1 
ATOM   13332 O  O     . VAL C 2 307 ? 114.006 100.212 103.886 1.00 44.57 ?  286 VAL C O     1 
ATOM   13333 C  CB    . VAL C 2 307 ? 111.154 98.751  104.510 1.00 42.97 ?  286 VAL C CB    1 
ATOM   13334 C  CG1   . VAL C 2 307 ? 112.312 98.046  105.235 1.00 42.86 ?  286 VAL C CG1   1 
ATOM   13335 C  CG2   . VAL C 2 307 ? 110.011 99.030  105.467 1.00 41.93 ?  286 VAL C CG2   1 
ATOM   13336 N  N     . LEU C 2 308 ? 113.042 99.590  101.942 1.00 46.21 ?  287 LEU C N     1 
ATOM   13337 C  CA    . LEU C 2 308 ? 114.287 99.508  101.165 1.00 47.66 ?  287 LEU C CA    1 
ATOM   13338 C  C     . LEU C 2 308 ? 114.903 100.883 100.910 1.00 48.82 ?  287 LEU C C     1 
ATOM   13339 O  O     . LEU C 2 308 ? 116.133 101.024 100.890 1.00 49.02 ?  287 LEU C O     1 
ATOM   13340 C  CB    . LEU C 2 308 ? 114.050 98.766  99.842  1.00 47.95 ?  287 LEU C CB    1 
ATOM   13341 C  CG    . LEU C 2 308 ? 114.248 97.241  99.808  1.00 48.23 ?  287 LEU C CG    1 
ATOM   13342 C  CD1   . LEU C 2 308 ? 114.045 96.556  101.168 1.00 48.10 ?  287 LEU C CD1   1 
ATOM   13343 C  CD2   . LEU C 2 308 ? 113.374 96.595  98.736  1.00 48.81 ?  287 LEU C CD2   1 
ATOM   13344 N  N     . ASN C 2 309 ? 114.046 101.885 100.715 1.00 49.80 ?  288 ASN C N     1 
ATOM   13345 C  CA    . ASN C 2 309 ? 114.475 103.281 100.688 1.00 51.09 ?  288 ASN C CA    1 
ATOM   13346 C  C     . ASN C 2 309 ? 114.895 103.794 102.069 1.00 51.08 ?  288 ASN C C     1 
ATOM   13347 O  O     . ASN C 2 309 ? 115.684 104.733 102.170 1.00 51.41 ?  288 ASN C O     1 
ATOM   13348 C  CB    . ASN C 2 309 ? 113.396 104.179 100.078 1.00 51.37 ?  288 ASN C CB    1 
ATOM   13349 C  CG    . ASN C 2 309 ? 113.402 104.149 98.563  1.00 53.22 ?  288 ASN C CG    1 
ATOM   13350 O  OD1   . ASN C 2 309 ? 113.471 103.080 97.947  1.00 54.39 ?  288 ASN C OD1   1 
ATOM   13351 N  ND2   . ASN C 2 309 ? 113.334 105.326 97.950  1.00 54.70 ?  288 ASN C ND2   1 
ATOM   13352 N  N     . GLY C 2 310 ? 114.364 103.173 103.122 1.00 51.25 ?  289 GLY C N     1 
ATOM   13353 C  CA    . GLY C 2 310 ? 114.779 103.456 104.498 1.00 51.35 ?  289 GLY C CA    1 
ATOM   13354 C  C     . GLY C 2 310 ? 116.219 103.053 104.789 1.00 51.86 ?  289 GLY C C     1 
ATOM   13355 O  O     . GLY C 2 310 ? 116.833 103.561 105.735 1.00 51.49 ?  289 GLY C O     1 
ATOM   13356 N  N     . LEU C 2 311 ? 116.756 102.139 103.980 1.00 52.45 ?  290 LEU C N     1 
ATOM   13357 C  CA    . LEU C 2 311 ? 118.148 101.700 104.101 1.00 52.99 ?  290 LEU C CA    1 
ATOM   13358 C  C     . LEU C 2 311 ? 119.091 102.605 103.304 1.00 53.65 ?  290 LEU C C     1 
ATOM   13359 O  O     . LEU C 2 311 ? 119.097 102.597 102.067 1.00 54.22 ?  290 LEU C O     1 
ATOM   13360 C  CB    . LEU C 2 311 ? 118.299 100.244 103.647 1.00 53.08 ?  290 LEU C CB    1 
ATOM   13361 C  CG    . LEU C 2 311 ? 117.749 99.124  104.533 1.00 53.33 ?  290 LEU C CG    1 
ATOM   13362 C  CD1   . LEU C 2 311 ? 117.658 97.824  103.747 1.00 53.79 ?  290 LEU C CD1   1 
ATOM   13363 C  CD2   . LEU C 2 311 ? 118.598 98.935  105.792 1.00 53.22 ?  290 LEU C CD2   1 
ATOM   13364 N  N     . LYS C 2 330 ? 141.377 115.643 113.571 1.00 58.93 ?  309 LYS C N     1 
ATOM   13365 C  CA    . LYS C 2 330 ? 142.827 115.777 113.491 1.00 61.98 ?  309 LYS C CA    1 
ATOM   13366 C  C     . LYS C 2 330 ? 143.329 115.520 112.074 1.00 61.97 ?  309 LYS C C     1 
ATOM   13367 O  O     . LYS C 2 330 ? 142.790 114.681 111.354 1.00 59.24 ?  309 LYS C O     1 
ATOM   13368 C  CB    . LYS C 2 330 ? 143.509 114.819 114.469 1.00 60.82 ?  309 LYS C CB    1 
ATOM   13369 C  CG    . LYS C 2 330 ? 143.177 115.077 115.929 1.00 60.80 ?  309 LYS C CG    1 
ATOM   13370 C  CD    . LYS C 2 330 ? 143.881 116.323 116.442 1.00 60.28 ?  309 LYS C CD    1 
ATOM   13371 C  CE    . LYS C 2 330 ? 144.827 115.996 117.586 1.00 62.15 ?  309 LYS C CE    1 
ATOM   13372 N  NZ    . LYS C 2 330 ? 144.327 114.869 118.420 1.00 62.59 1  309 LYS C NZ    1 
ATOM   13373 N  N     . ALA C 2 331 ? 144.366 116.254 111.683 1.00 55.97 ?  310 ALA C N     1 
ATOM   13374 C  CA    . ALA C 2 331 ? 144.988 116.112 110.377 1.00 53.20 ?  310 ALA C CA    1 
ATOM   13375 C  C     . ALA C 2 331 ? 146.443 115.692 110.537 1.00 52.13 ?  310 ALA C C     1 
ATOM   13376 O  O     . ALA C 2 331 ? 147.077 115.971 111.559 1.00 53.07 ?  310 ALA C O     1 
ATOM   13377 C  CB    . ALA C 2 331 ? 144.906 117.418 109.581 1.00 51.98 ?  310 ALA C CB    1 
ATOM   13378 N  N     . THR C 2 332 ? 146.961 115.008 109.518 1.00 45.82 ?  311 THR C N     1 
ATOM   13379 C  CA    . THR C 2 332 ? 148.349 114.568 109.534 1.00 46.85 ?  311 THR C CA    1 
ATOM   13380 C  C     . THR C 2 332 ? 149.288 115.763 109.649 1.00 43.12 ?  311 THR C C     1 
ATOM   13381 O  O     . THR C 2 332 ? 149.066 116.812 109.041 1.00 48.26 ?  311 THR C O     1 
ATOM   13382 C  CB    . THR C 2 332 ? 148.661 113.757 108.275 1.00 45.72 ?  311 THR C CB    1 
ATOM   13383 O  OG1   . THR C 2 332 ? 149.955 113.154 108.393 1.00 46.36 ?  311 THR C OG1   1 
ATOM   13384 C  CG2   . THR C 2 332 ? 148.603 114.638 107.039 1.00 44.89 ?  311 THR C CG2   1 
ATOM   13385 N  N     . VAL C 2 333 ? 150.339 115.597 110.448 1.00 42.01 ?  312 VAL C N     1 
ATOM   13386 C  CA    . VAL C 2 333 ? 151.226 116.687 110.836 1.00 38.55 ?  312 VAL C CA    1 
ATOM   13387 C  C     . VAL C 2 333 ? 152.626 116.370 110.329 1.00 41.18 ?  312 VAL C C     1 
ATOM   13388 O  O     . VAL C 2 333 ? 153.184 115.310 110.639 1.00 46.85 ?  312 VAL C O     1 
ATOM   13389 C  CB    . VAL C 2 333 ? 151.229 116.898 112.357 1.00 37.39 ?  312 VAL C CB    1 
ATOM   13390 C  CG1   . VAL C 2 333 ? 152.399 117.776 112.771 1.00 40.81 ?  312 VAL C CG1   1 
ATOM   13391 C  CG2   . VAL C 2 333 ? 149.910 117.491 112.818 1.00 39.47 ?  312 VAL C CG2   1 
ATOM   13392 N  N     . GLU C 2 334 ? 153.200 117.289 109.548 1.00 34.01 ?  313 GLU C N     1 
ATOM   13393 C  CA    . GLU C 2 334 ? 154.613 117.217 109.217 1.00 34.45 ?  313 GLU C CA    1 
ATOM   13394 C  C     . GLU C 2 334 ? 155.345 118.432 109.777 1.00 37.55 ?  313 GLU C C     1 
ATOM   13395 O  O     . GLU C 2 334 ? 154.787 119.533 109.824 1.00 40.51 ?  313 GLU C O     1 
ATOM   13396 C  CB    . GLU C 2 334 ? 154.858 117.158 107.704 1.00 34.27 ?  313 GLU C CB    1 
ATOM   13397 C  CG    . GLU C 2 334 ? 154.097 116.084 106.957 1.00 38.73 ?  313 GLU C CG    1 
ATOM   13398 C  CD    . GLU C 2 334 ? 154.476 116.039 105.489 1.00 42.14 ?  313 GLU C CD    1 
ATOM   13399 O  OE1   . GLU C 2 334 ? 155.608 115.613 105.181 1.00 40.76 ?  313 GLU C OE1   1 
ATOM   13400 O  OE2   . GLU C 2 334 ? 153.652 116.443 104.643 1.00 39.96 -1 313 GLU C OE2   1 
ATOM   13401 N  N     . PRO C 2 335 ? 156.591 118.268 110.213 1.00 33.56 ?  314 PRO C N     1 
ATOM   13402 C  CA    . PRO C 2 335 ? 157.377 119.425 110.651 1.00 34.05 ?  314 PRO C CA    1 
ATOM   13403 C  C     . PRO C 2 335 ? 157.750 120.309 109.470 1.00 35.93 ?  314 PRO C C     1 
ATOM   13404 O  O     . PRO C 2 335 ? 157.789 119.881 108.315 1.00 36.72 ?  314 PRO C O     1 
ATOM   13405 C  CB    . PRO C 2 335 ? 158.618 118.800 111.299 1.00 36.78 ?  314 PRO C CB    1 
ATOM   13406 C  CG    . PRO C 2 335 ? 158.285 117.343 111.482 1.00 33.20 ?  314 PRO C CG    1 
ATOM   13407 C  CD    . PRO C 2 335 ? 157.323 117.006 110.392 1.00 33.09 ?  314 PRO C CD    1 
ATOM   13408 N  N     . LEU C 2 336 ? 158.027 121.571 109.780 1.00 31.29 ?  315 LEU C N     1 
ATOM   13409 C  CA    . LEU C 2 336 ? 158.407 122.548 108.771 1.00 25.88 ?  315 LEU C CA    1 
ATOM   13410 C  C     . LEU C 2 336 ? 159.899 122.457 108.487 1.00 28.32 ?  315 LEU C C     1 
ATOM   13411 O  O     . LEU C 2 336 ? 160.721 122.560 109.405 1.00 26.34 ?  315 LEU C O     1 
ATOM   13412 C  CB    . LEU C 2 336 ? 158.042 123.963 109.220 1.00 25.22 ?  315 LEU C CB    1 
ATOM   13413 C  CG    . LEU C 2 336 ? 156.616 124.410 108.906 1.00 26.15 ?  315 LEU C CG    1 
ATOM   13414 C  CD1   . LEU C 2 336 ? 156.373 125.816 109.424 1.00 26.32 ?  315 LEU C CD1   1 
ATOM   13415 C  CD2   . LEU C 2 336 ? 156.377 124.341 107.408 1.00 21.64 ?  315 LEU C CD2   1 
ATOM   13416 N  N     . LYS C 2 337 ? 160.243 122.264 107.220 1.00 24.69 ?  316 LYS C N     1 
ATOM   13417 C  CA    . LYS C 2 337 ? 161.630 122.266 106.787 1.00 25.14 ?  316 LYS C CA    1 
ATOM   13418 C  C     . LYS C 2 337 ? 162.093 123.694 106.520 1.00 19.78 ?  316 LYS C C     1 
ATOM   13419 O  O     . LYS C 2 337 ? 161.291 124.604 106.307 1.00 30.21 ?  316 LYS C O     1 
ATOM   13420 C  CB    . LYS C 2 337 ? 161.808 121.413 105.530 1.00 29.25 ?  316 LYS C CB    1 
ATOM   13421 C  CG    . LYS C 2 337 ? 160.937 120.169 105.489 1.00 28.02 ?  316 LYS C CG    1 
ATOM   13422 C  CD    . LYS C 2 337 ? 161.749 118.914 105.757 1.00 27.52 ?  316 LYS C CD    1 
ATOM   13423 C  CE    . LYS C 2 337 ? 160.941 117.890 106.536 1.00 32.76 ?  316 LYS C CE    1 
ATOM   13424 N  NZ    . LYS C 2 337 ? 161.797 116.796 107.072 1.00 30.53 1  316 LYS C NZ    1 
ATOM   13425 N  N     . ASP C 2 338 ? 163.414 123.880 106.538 1.00 29.74 ?  317 ASP C N     1 
ATOM   13426 C  CA    . ASP C 2 338 ? 163.978 125.190 106.242 1.00 26.29 ?  317 ASP C CA    1 
ATOM   13427 C  C     . ASP C 2 338 ? 163.734 125.611 104.799 1.00 29.71 ?  317 ASP C C     1 
ATOM   13428 O  O     . ASP C 2 338 ? 163.818 126.805 104.493 1.00 21.95 ?  317 ASP C O     1 
ATOM   13429 C  CB    . ASP C 2 338 ? 165.478 125.198 106.542 1.00 25.78 ?  317 ASP C CB    1 
ATOM   13430 C  CG    . ASP C 2 338 ? 165.811 124.511 107.850 1.00 35.15 ?  317 ASP C CG    1 
ATOM   13431 O  OD1   . ASP C 2 338 ? 165.459 123.322 108.005 1.00 32.75 ?  317 ASP C OD1   1 
ATOM   13432 O  OD2   . ASP C 2 338 ? 166.424 125.160 108.723 1.00 36.30 -1 317 ASP C OD2   1 
ATOM   13433 N  N     . ASP C 2 339 ? 163.431 124.665 103.912 1.00 26.99 ?  318 ASP C N     1 
ATOM   13434 C  CA    . ASP C 2 339 ? 163.152 124.972 102.517 1.00 24.15 ?  318 ASP C CA    1 
ATOM   13435 C  C     . ASP C 2 339 ? 161.712 125.403 102.276 1.00 20.41 ?  318 ASP C C     1 
ATOM   13436 O  O     . ASP C 2 339 ? 161.405 125.898 101.186 1.00 28.59 ?  318 ASP C O     1 
ATOM   13437 C  CB    . ASP C 2 339 ? 163.475 123.760 101.635 1.00 23.02 ?  318 ASP C CB    1 
ATOM   13438 C  CG    . ASP C 2 339 ? 164.673 122.979 102.137 1.00 32.33 ?  318 ASP C CG    1 
ATOM   13439 O  OD1   . ASP C 2 339 ? 164.481 121.863 102.665 1.00 34.56 ?  318 ASP C OD1   1 
ATOM   13440 O  OD2   . ASP C 2 339 ? 165.808 123.482 102.004 1.00 32.78 -1 318 ASP C OD2   1 
ATOM   13441 N  N     . ASP C 2 340 ? 160.828 125.230 103.256 1.00 18.60 ?  319 ASP C N     1 
ATOM   13442 C  CA    . ASP C 2 340 ? 159.447 125.679 103.142 1.00 13.68 ?  319 ASP C CA    1 
ATOM   13443 C  C     . ASP C 2 340 ? 159.289 127.164 103.433 1.00 14.05 ?  319 ASP C C     1 
ATOM   13444 O  O     . ASP C 2 340 ? 158.192 127.703 103.255 1.00 30.27 ?  319 ASP C O     1 
ATOM   13445 C  CB    . ASP C 2 340 ? 158.548 124.873 104.085 1.00 12.38 ?  319 ASP C CB    1 
ATOM   13446 C  CG    . ASP C 2 340 ? 158.807 123.384 104.005 1.00 24.62 ?  319 ASP C CG    1 
ATOM   13447 O  OD1   . ASP C 2 340 ? 158.971 122.866 102.881 1.00 25.90 ?  319 ASP C OD1   1 
ATOM   13448 O  OD2   . ASP C 2 340 ? 158.839 122.728 105.066 1.00 30.97 -1 319 ASP C OD2   1 
ATOM   13449 N  N     . PHE C 2 341 ? 160.350 127.830 103.878 1.00 14.34 ?  320 PHE C N     1 
ATOM   13450 C  CA    . PHE C 2 341 ? 160.328 129.255 104.169 1.00 3.83  ?  320 PHE C CA    1 
ATOM   13451 C  C     . PHE C 2 341 ? 160.888 130.092 103.028 1.00 6.43  ?  320 PHE C C     1 
ATOM   13452 O  O     . PHE C 2 341 ? 161.009 131.312 103.169 1.00 11.38 ?  320 PHE C O     1 
ATOM   13453 C  CB    . PHE C 2 341 ? 161.109 129.536 105.453 1.00 8.01  ?  320 PHE C CB    1 
ATOM   13454 C  CG    . PHE C 2 341 ? 160.403 129.098 106.702 1.00 9.69  ?  320 PHE C CG    1 
ATOM   13455 C  CD1   . PHE C 2 341 ? 159.546 129.958 107.365 1.00 6.44  ?  320 PHE C CD1   1 
ATOM   13456 C  CD2   . PHE C 2 341 ? 160.596 127.827 107.213 1.00 7.94  ?  320 PHE C CD2   1 
ATOM   13457 C  CE1   . PHE C 2 341 ? 158.896 129.559 108.514 1.00 10.55 ?  320 PHE C CE1   1 
ATOM   13458 C  CE2   . PHE C 2 341 ? 159.946 127.422 108.361 1.00 8.92  ?  320 PHE C CE2   1 
ATOM   13459 C  CZ    . PHE C 2 341 ? 159.094 128.290 109.013 1.00 6.02  ?  320 PHE C CZ    1 
ATOM   13460 N  N     . TYR C 2 342 ? 161.231 129.466 101.905 1.00 6.07  ?  321 TYR C N     1 
ATOM   13461 C  CA    . TYR C 2 342 ? 161.820 130.156 100.768 1.00 12.59 ?  321 TYR C CA    1 
ATOM   13462 C  C     . TYR C 2 342 ? 161.090 129.749 99.499  1.00 16.10 ?  321 TYR C C     1 
ATOM   13463 O  O     . TYR C 2 342 ? 160.722 128.583 99.329  1.00 16.79 ?  321 TYR C O     1 
ATOM   13464 C  CB    . TYR C 2 342 ? 163.315 129.840 100.641 1.00 6.93  ?  321 TYR C CB    1 
ATOM   13465 C  CG    . TYR C 2 342 ? 164.128 130.292 101.830 1.00 3.43  ?  321 TYR C CG    1 
ATOM   13466 C  CD1   . TYR C 2 342 ? 164.309 129.461 102.927 1.00 8.24  ?  321 TYR C CD1   1 
ATOM   13467 C  CD2   . TYR C 2 342 ? 164.708 131.552 101.859 1.00 11.16 ?  321 TYR C CD2   1 
ATOM   13468 C  CE1   . TYR C 2 342 ? 165.049 129.871 104.018 1.00 12.34 ?  321 TYR C CE1   1 
ATOM   13469 C  CE2   . TYR C 2 342 ? 165.449 131.970 102.946 1.00 13.11 ?  321 TYR C CE2   1 
ATOM   13470 C  CZ    . TYR C 2 342 ? 165.617 131.126 104.022 1.00 17.37 ?  321 TYR C CZ    1 
ATOM   13471 O  OH    . TYR C 2 342 ? 166.355 131.542 105.105 1.00 21.45 ?  321 TYR C OH    1 
ATOM   13472 N  N     . PHE C 2 343 ? 160.880 130.717 98.612  1.00 12.77 ?  322 PHE C N     1 
ATOM   13473 C  CA    . PHE C 2 343 ? 160.142 130.477 97.378  1.00 15.81 ?  322 PHE C CA    1 
ATOM   13474 C  C     . PHE C 2 343 ? 160.814 131.179 96.205  1.00 24.63 ?  322 PHE C C     1 
ATOM   13475 O  O     . PHE C 2 343 ? 161.623 132.087 96.389  1.00 24.06 ?  322 PHE C O     1 
ATOM   13476 C  CB    . PHE C 2 343 ? 158.681 130.938 97.500  1.00 11.49 ?  322 PHE C CB    1 
ATOM   13477 C  CG    . PHE C 2 343 ? 158.069 130.709 98.858  1.00 8.46  ?  322 PHE C CG    1 
ATOM   13478 C  CD1   . PHE C 2 343 ? 158.339 131.559 99.921  1.00 8.80  ?  322 PHE C CD1   1 
ATOM   13479 C  CD2   . PHE C 2 343 ? 157.238 129.624 99.075  1.00 13.46 ?  322 PHE C CD2   1 
ATOM   13480 C  CE1   . PHE C 2 343 ? 157.782 131.334 101.162 1.00 5.58  ?  322 PHE C CE1   1 
ATOM   13481 C  CE2   . PHE C 2 343 ? 156.681 129.397 100.315 1.00 8.14  ?  322 PHE C CE2   1 
ATOM   13482 C  CZ    . PHE C 2 343 ? 156.953 130.251 101.358 1.00 2.41  ?  322 PHE C CZ    1 
ATOM   13483 N  N     . ASP D 2 37  ? 123.130 109.021 142.217 1.00 32.44 ?  16  ASP D N     1 
ATOM   13484 C  CA    . ASP D 2 37  ? 123.406 110.459 142.167 1.00 32.83 ?  16  ASP D CA    1 
ATOM   13485 C  C     . ASP D 2 37  ? 124.524 110.845 141.200 1.00 31.65 ?  16  ASP D C     1 
ATOM   13486 O  O     . ASP D 2 37  ? 124.767 112.036 140.992 1.00 32.65 ?  16  ASP D O     1 
ATOM   13487 C  CB    . ASP D 2 37  ? 123.794 110.987 143.557 1.00 33.73 ?  16  ASP D CB    1 
ATOM   13488 C  CG    . ASP D 2 37  ? 122.664 110.896 144.571 1.00 36.81 ?  16  ASP D CG    1 
ATOM   13489 O  OD1   . ASP D 2 37  ? 122.970 110.952 145.786 1.00 39.69 ?  16  ASP D OD1   1 
ATOM   13490 O  OD2   . ASP D 2 37  ? 121.485 110.765 144.170 1.00 39.67 -1 16  ASP D OD2   1 
ATOM   13491 N  N     . PHE D 2 38  ? 125.208 109.863 140.616 1.00 29.55 ?  17  PHE D N     1 
ATOM   13492 C  CA    . PHE D 2 38  ? 126.485 110.155 139.964 1.00 27.75 ?  17  PHE D CA    1 
ATOM   13493 C  C     . PHE D 2 38  ? 126.775 109.457 138.625 1.00 26.21 ?  17  PHE D C     1 
ATOM   13494 O  O     . PHE D 2 38  ? 127.635 109.910 137.877 1.00 25.93 ?  17  PHE D O     1 
ATOM   13495 C  CB    . PHE D 2 38  ? 127.639 109.904 140.961 1.00 27.37 ?  17  PHE D CB    1 
ATOM   13496 C  CG    . PHE D 2 38  ? 127.699 108.488 141.471 1.00 27.32 ?  17  PHE D CG    1 
ATOM   13497 C  CD1   . PHE D 2 38  ? 128.353 107.500 140.740 1.00 27.01 ?  17  PHE D CD1   1 
ATOM   13498 C  CD2   . PHE D 2 38  ? 127.104 108.140 142.677 1.00 28.02 ?  17  PHE D CD2   1 
ATOM   13499 C  CE1   . PHE D 2 38  ? 128.406 106.187 141.203 1.00 27.66 ?  17  PHE D CE1   1 
ATOM   13500 C  CE2   . PHE D 2 38  ? 127.148 106.832 143.141 1.00 27.68 ?  17  PHE D CE2   1 
ATOM   13501 C  CZ    . PHE D 2 38  ? 127.803 105.852 142.400 1.00 27.47 ?  17  PHE D CZ    1 
ATOM   13502 N  N     . THR D 2 39  ? 126.072 108.370 138.324 1.00 24.88 ?  18  THR D N     1 
ATOM   13503 C  CA    . THR D 2 39  ? 126.407 107.541 137.155 1.00 23.81 ?  18  THR D CA    1 
ATOM   13504 C  C     . THR D 2 39  ? 126.249 108.257 135.801 1.00 23.56 ?  18  THR D C     1 
ATOM   13505 O  O     . THR D 2 39  ? 127.097 108.129 134.918 1.00 23.02 ?  18  THR D O     1 
ATOM   13506 C  CB    . THR D 2 39  ? 125.679 106.175 137.194 1.00 23.40 ?  18  THR D CB    1 
ATOM   13507 O  OG1   . THR D 2 39  ? 126.355 105.313 138.117 1.00 23.77 ?  18  THR D OG1   1 
ATOM   13508 C  CG2   . THR D 2 39  ? 125.679 105.500 135.832 1.00 22.31 ?  18  THR D CG2   1 
ATOM   13509 N  N     . GLN D 2 40  ? 125.180 109.025 135.635 1.00 23.78 ?  19  GLN D N     1 
ATOM   13510 C  CA    . GLN D 2 40  ? 125.008 109.756 134.377 1.00 23.88 ?  19  GLN D CA    1 
ATOM   13511 C  C     . GLN D 2 40  ? 126.088 110.822 134.174 1.00 24.09 ?  19  GLN D C     1 
ATOM   13512 O  O     . GLN D 2 40  ? 126.614 110.973 133.080 1.00 23.15 ?  19  GLN D O     1 
ATOM   13513 C  CB    . GLN D 2 40  ? 123.599 110.342 134.256 1.00 24.53 ?  19  GLN D CB    1 
ATOM   13514 C  CG    . GLN D 2 40  ? 122.543 109.259 134.103 1.00 24.06 ?  19  GLN D CG    1 
ATOM   13515 C  CD    . GLN D 2 40  ? 121.237 109.770 133.539 1.00 25.83 ?  19  GLN D CD    1 
ATOM   13516 O  OE1   . GLN D 2 40  ? 121.164 110.889 133.035 1.00 25.90 ?  19  GLN D OE1   1 
ATOM   13517 N  NE2   . GLN D 2 40  ? 120.197 108.938 133.601 1.00 23.56 ?  19  GLN D NE2   1 
ATOM   13518 N  N     . MET D 2 41  ? 126.450 111.524 135.241 1.00 24.07 ?  20  MET D N     1 
ATOM   13519 C  CA    . MET D 2 41  ? 127.568 112.465 135.180 1.00 25.53 ?  20  MET D CA    1 
ATOM   13520 C  C     . MET D 2 41  ? 128.891 111.788 134.768 1.00 24.24 ?  20  MET D C     1 
ATOM   13521 O  O     . MET D 2 41  ? 129.631 112.318 133.934 1.00 23.16 ?  20  MET D O     1 
ATOM   13522 C  CB    . MET D 2 41  ? 127.717 113.189 136.523 1.00 26.79 ?  20  MET D CB    1 
ATOM   13523 C  CG    . MET D 2 41  ? 128.867 114.175 136.592 1.00 32.62 ?  20  MET D CG    1 
ATOM   13524 S  SD    . MET D 2 41  ? 129.133 114.696 138.303 1.00 44.01 ?  20  MET D SD    1 
ATOM   13525 C  CE    . MET D 2 41  ? 130.864 115.173 138.255 1.00 41.93 ?  20  MET D CE    1 
ATOM   13526 N  N     . PHE D 2 42  ? 129.180 110.616 135.336 1.00 23.31 ?  21  PHE D N     1 
ATOM   13527 C  CA    . PHE D 2 42  ? 130.401 109.896 134.973 1.00 23.44 ?  21  PHE D CA    1 
ATOM   13528 C  C     . PHE D 2 42  ? 130.332 109.324 133.572 1.00 23.55 ?  21  PHE D C     1 
ATOM   13529 O  O     . PHE D 2 42  ? 131.341 109.268 132.878 1.00 23.74 ?  21  PHE D O     1 
ATOM   13530 C  CB    . PHE D 2 42  ? 130.743 108.809 135.994 1.00 22.97 ?  21  PHE D CB    1 
ATOM   13531 C  CG    . PHE D 2 42  ? 131.533 109.326 137.145 1.00 23.86 ?  21  PHE D CG    1 
ATOM   13532 C  CD1   . PHE D 2 42  ? 132.922 109.237 137.147 1.00 24.55 ?  21  PHE D CD1   1 
ATOM   13533 C  CD2   . PHE D 2 42  ? 130.900 109.942 138.208 1.00 24.06 ?  21  PHE D CD2   1 
ATOM   13534 C  CE1   . PHE D 2 42  ? 133.667 109.740 138.217 1.00 25.78 ?  21  PHE D CE1   1 
ATOM   13535 C  CE2   . PHE D 2 42  ? 131.636 110.449 139.283 1.00 25.25 ?  21  PHE D CE2   1 
ATOM   13536 C  CZ    . PHE D 2 42  ? 133.012 110.353 139.285 1.00 25.79 ?  21  PHE D CZ    1 
ATOM   13537 N  N     . TYR D 2 43  ? 129.132 108.921 133.158 1.00 24.08 ?  22  TYR D N     1 
ATOM   13538 C  CA    . TYR D 2 43  ? 128.907 108.495 131.787 1.00 24.74 ?  22  TYR D CA    1 
ATOM   13539 C  C     . TYR D 2 43  ? 129.371 109.595 130.830 1.00 25.72 ?  22  TYR D C     1 
ATOM   13540 O  O     . TYR D 2 43  ? 130.139 109.338 129.898 1.00 25.56 ?  22  TYR D O     1 
ATOM   13541 C  CB    . TYR D 2 43  ? 127.431 108.149 131.528 1.00 24.90 ?  22  TYR D CB    1 
ATOM   13542 C  CG    . TYR D 2 43  ? 127.165 107.870 130.056 1.00 24.38 ?  22  TYR D CG    1 
ATOM   13543 C  CD1   . TYR D 2 43  ? 127.294 106.587 129.539 1.00 23.96 ?  22  TYR D CD1   1 
ATOM   13544 C  CD2   . TYR D 2 43  ? 126.842 108.906 129.176 1.00 24.73 ?  22  TYR D CD2   1 
ATOM   13545 C  CE1   . TYR D 2 43  ? 127.086 106.332 128.182 1.00 23.42 ?  22  TYR D CE1   1 
ATOM   13546 C  CE2   . TYR D 2 43  ? 126.618 108.665 127.818 1.00 26.65 ?  22  TYR D CE2   1 
ATOM   13547 C  CZ    . TYR D 2 43  ? 126.746 107.375 127.333 1.00 25.68 ?  22  TYR D CZ    1 
ATOM   13548 O  OH    . TYR D 2 43  ? 126.529 107.133 125.996 1.00 26.57 ?  22  TYR D OH    1 
ATOM   13549 N  N     . ASN D 2 44  ? 128.890 110.812 131.072 1.00 26.77 ?  23  ASN D N     1 
ATOM   13550 C  CA    . ASN D 2 44  ? 129.219 111.963 130.239 1.00 28.57 ?  23  ASN D CA    1 
ATOM   13551 C  C     . ASN D 2 44  ? 130.712 112.224 130.173 1.00 28.70 ?  23  ASN D C     1 
ATOM   13552 O  O     . ASN D 2 44  ? 131.277 112.323 129.081 1.00 28.99 ?  23  ASN D O     1 
ATOM   13553 C  CB    . ASN D 2 44  ? 128.453 113.203 130.710 1.00 29.62 ?  23  ASN D CB    1 
ATOM   13554 C  CG    . ASN D 2 44  ? 126.960 113.099 130.427 1.00 32.44 ?  23  ASN D CG    1 
ATOM   13555 O  OD1   . ASN D 2 44  ? 126.530 112.337 129.551 1.00 34.30 ?  23  ASN D OD1   1 
ATOM   13556 N  ND2   . ASN D 2 44  ? 126.158 113.862 131.167 1.00 35.17 ?  23  ASN D ND2   1 
ATOM   13557 N  N     . GLN D 2 45  ? 131.351 112.287 131.339 1.00 28.97 ?  24  GLN D N     1 
ATOM   13558 C  CA    . GLN D 2 45  ? 132.785 112.545 131.411 1.00 29.99 ?  24  GLN D CA    1 
ATOM   13559 C  C     . GLN D 2 45  ? 133.612 111.444 130.731 1.00 29.69 ?  24  GLN D C     1 
ATOM   13560 O  O     . GLN D 2 45  ? 134.593 111.737 130.048 1.00 30.01 ?  24  GLN D O     1 
ATOM   13561 C  CB    . GLN D 2 45  ? 133.234 112.757 132.862 1.00 30.27 ?  24  GLN D CB    1 
ATOM   13562 C  CG    . GLN D 2 45  ? 134.687 113.265 132.997 1.00 32.29 ?  24  GLN D CG    1 
ATOM   13563 C  CD    . GLN D 2 45  ? 134.907 114.635 132.369 1.00 35.95 ?  24  GLN D CD    1 
ATOM   13564 O  OE1   . GLN D 2 45  ? 133.985 115.452 132.282 1.00 36.72 ?  24  GLN D OE1   1 
ATOM   13565 N  NE2   . GLN D 2 45  ? 136.134 114.893 131.928 1.00 37.05 ?  24  GLN D NE2   1 
ATOM   13566 N  N     . ASN D 2 46  ? 133.199 110.188 130.897 1.00 28.93 ?  25  ASN D N     1 
ATOM   13567 C  CA    . ASN D 2 46  ? 133.874 109.074 130.253 1.00 28.70 ?  25  ASN D CA    1 
ATOM   13568 C  C     . ASN D 2 46  ? 133.818 109.121 128.732 1.00 29.05 ?  25  ASN D C     1 
ATOM   13569 O  O     . ASN D 2 46  ? 134.857 109.027 128.072 1.00 28.51 ?  25  ASN D O     1 
ATOM   13570 C  CB    . ASN D 2 46  ? 133.339 107.728 130.763 1.00 28.36 ?  25  ASN D CB    1 
ATOM   13571 C  CG    . ASN D 2 46  ? 134.064 107.253 132.004 1.00 28.45 ?  25  ASN D CG    1 
ATOM   13572 O  OD1   . ASN D 2 46  ? 134.991 106.451 131.910 1.00 28.03 ?  25  ASN D OD1   1 
ATOM   13573 N  ND2   . ASN D 2 46  ? 133.669 107.765 133.168 1.00 26.53 ?  25  ASN D ND2   1 
ATOM   13574 N  N     . VAL D 2 47  ? 132.618 109.294 128.179 1.00 29.66 ?  26  VAL D N     1 
ATOM   13575 C  CA    . VAL D 2 47  ? 132.449 109.238 126.726 1.00 31.15 ?  26  VAL D CA    1 
ATOM   13576 C  C     . VAL D 2 47  ? 133.052 110.461 126.041 1.00 32.39 ?  26  VAL D C     1 
ATOM   13577 O  O     . VAL D 2 47  ? 133.523 110.370 124.909 1.00 32.80 ?  26  VAL D O     1 
ATOM   13578 C  CB    . VAL D 2 47  ? 130.972 108.990 126.270 1.00 31.08 ?  26  VAL D CB    1 
ATOM   13579 C  CG1   . VAL D 2 47  ? 130.418 107.719 126.902 1.00 31.09 ?  26  VAL D CG1   1 
ATOM   13580 C  CG2   . VAL D 2 47  ? 130.070 110.197 126.563 1.00 30.81 ?  26  VAL D CG2   1 
ATOM   13581 N  N     . LYS D 2 48  ? 133.071 111.597 126.728 1.00 33.28 ?  27  LYS D N     1 
ATOM   13582 C  CA    . LYS D 2 48  ? 133.680 112.774 126.128 1.00 34.87 ?  27  LYS D CA    1 
ATOM   13583 C  C     . LYS D 2 48  ? 135.222 112.748 126.156 1.00 34.91 ?  27  LYS D C     1 
ATOM   13584 O  O     . LYS D 2 48  ? 135.868 113.545 125.481 1.00 34.92 ?  27  LYS D O     1 
ATOM   13585 C  CB    . LYS D 2 48  ? 133.085 114.070 126.699 1.00 35.45 ?  27  LYS D CB    1 
ATOM   13586 C  CG    . LYS D 2 48  ? 133.704 114.589 127.976 1.00 37.41 ?  27  LYS D CG    1 
ATOM   13587 C  CD    . LYS D 2 48  ? 133.288 116.052 128.197 1.00 40.91 ?  27  LYS D CD    1 
ATOM   13588 C  CE    . LYS D 2 48  ? 134.188 116.732 129.233 1.00 42.46 ?  27  LYS D CE    1 
ATOM   13589 N  NZ    . LYS D 2 48  ? 133.920 118.195 129.365 1.00 45.13 1  27  LYS D NZ    1 
ATOM   13590 N  N     . GLN D 2 49  ? 135.791 111.814 126.922 1.00 34.66 ?  28  GLN D N     1 
ATOM   13591 C  CA    . GLN D 2 49  ? 137.235 111.604 126.987 1.00 34.64 ?  28  GLN D CA    1 
ATOM   13592 C  C     . GLN D 2 49  ? 137.696 110.533 126.000 1.00 34.20 ?  28  GLN D C     1 
ATOM   13593 O  O     . GLN D 2 49  ? 138.859 110.127 126.036 1.00 34.53 ?  28  GLN D O     1 
ATOM   13594 C  CB    . GLN D 2 49  ? 137.666 111.195 128.410 1.00 34.89 ?  28  GLN D CB    1 
ATOM   13595 C  CG    . GLN D 2 49  ? 137.959 112.359 129.355 1.00 36.47 ?  28  GLN D CG    1 
ATOM   13596 C  CD    . GLN D 2 49  ? 138.191 111.924 130.805 1.00 38.37 ?  28  GLN D CD    1 
ATOM   13597 O  OE1   . GLN D 2 49  ? 137.872 112.665 131.735 1.00 40.68 ?  28  GLN D OE1   1 
ATOM   13598 N  NE2   . GLN D 2 49  ? 138.743 110.726 131.001 1.00 38.57 ?  28  GLN D NE2   1 
ATOM   13599 N  N     . PHE D 2 50  ? 136.800 110.069 125.128 1.00 33.42 ?  29  PHE D N     1 
ATOM   13600 C  CA    . PHE D 2 50  ? 137.140 108.984 124.208 1.00 32.57 ?  29  PHE D CA    1 
ATOM   13601 C  C     . PHE D 2 50  ? 138.272 109.413 123.274 1.00 32.60 ?  29  PHE D C     1 
ATOM   13602 O  O     . PHE D 2 50  ? 138.298 110.548 122.790 1.00 32.39 ?  29  PHE D O     1 
ATOM   13603 C  CB    . PHE D 2 50  ? 135.916 108.502 123.412 1.00 32.77 ?  29  PHE D CB    1 
ATOM   13604 C  CG    . PHE D 2 50  ? 136.212 107.354 122.467 1.00 32.24 ?  29  PHE D CG    1 
ATOM   13605 C  CD1   . PHE D 2 50  ? 136.389 106.061 122.950 1.00 31.50 ?  29  PHE D CD1   1 
ATOM   13606 C  CD2   . PHE D 2 50  ? 136.315 107.572 121.099 1.00 33.60 ?  29  PHE D CD2   1 
ATOM   13607 C  CE1   . PHE D 2 50  ? 136.663 105.007 122.092 1.00 33.02 ?  29  PHE D CE1   1 
ATOM   13608 C  CE2   . PHE D 2 50  ? 136.594 106.521 120.222 1.00 33.78 ?  29  PHE D CE2   1 
ATOM   13609 C  CZ    . PHE D 2 50  ? 136.760 105.237 120.717 1.00 33.13 ?  29  PHE D CZ    1 
ATOM   13610 N  N     . TRP D 2 51  ? 139.204 108.499 123.040 1.00 31.95 ?  30  TRP D N     1 
ATOM   13611 C  CA    . TRP D 2 51  ? 140.358 108.753 122.178 1.00 32.03 ?  30  TRP D CA    1 
ATOM   13612 C  C     . TRP D 2 51  ? 140.851 107.436 121.595 1.00 33.03 ?  30  TRP D C     1 
ATOM   13613 O  O     . TRP D 2 51  ? 140.439 106.359 122.033 1.00 32.54 ?  30  TRP D O     1 
ATOM   13614 C  CB    . TRP D 2 51  ? 141.478 109.475 122.944 1.00 31.19 ?  30  TRP D CB    1 
ATOM   13615 C  CG    . TRP D 2 51  ? 142.026 108.692 124.121 1.00 28.11 ?  30  TRP D CG    1 
ATOM   13616 C  CD1   . TRP D 2 51  ? 141.460 108.570 125.352 1.00 26.51 ?  30  TRP D CD1   1 
ATOM   13617 C  CD2   . TRP D 2 51  ? 143.240 107.925 124.158 1.00 25.93 ?  30  TRP D CD2   1 
ATOM   13618 N  NE1   . TRP D 2 51  ? 142.248 107.778 126.162 1.00 24.52 ?  30  TRP D NE1   1 
ATOM   13619 C  CE2   . TRP D 2 51  ? 143.343 107.367 125.454 1.00 24.42 ?  30  TRP D CE2   1 
ATOM   13620 C  CE3   . TRP D 2 51  ? 144.254 107.659 123.226 1.00 25.37 ?  30  TRP D CE3   1 
ATOM   13621 C  CZ2   . TRP D 2 51  ? 144.423 106.563 125.844 1.00 24.00 ?  30  TRP D CZ2   1 
ATOM   13622 C  CZ3   . TRP D 2 51  ? 145.324 106.852 123.612 1.00 24.99 ?  30  TRP D CZ3   1 
ATOM   13623 C  CH2   . TRP D 2 51  ? 145.398 106.314 124.910 1.00 23.72 ?  30  TRP D CH2   1 
ATOM   13624 N  N     . LEU D 2 52  ? 141.720 107.535 120.593 1.00 34.81 ?  31  LEU D N     1 
ATOM   13625 C  CA    . LEU D 2 52  ? 142.272 106.376 119.909 1.00 36.58 ?  31  LEU D CA    1 
ATOM   13626 C  C     . LEU D 2 52  ? 143.785 106.523 119.769 1.00 37.80 ?  31  LEU D C     1 
ATOM   13627 O  O     . LEU D 2 52  ? 144.280 107.637 119.621 1.00 37.92 ?  31  LEU D O     1 
ATOM   13628 C  CB    . LEU D 2 52  ? 141.616 106.201 118.530 1.00 36.95 ?  31  LEU D CB    1 
ATOM   13629 C  CG    . LEU D 2 52  ? 140.243 105.526 118.440 1.00 38.15 ?  31  LEU D CG    1 
ATOM   13630 C  CD1   . LEU D 2 52  ? 139.940 105.141 116.997 1.00 39.50 ?  31  LEU D CD1   1 
ATOM   13631 C  CD2   . LEU D 2 52  ? 140.155 104.289 119.327 1.00 37.94 ?  31  LEU D CD2   1 
ATOM   13632 N  N     . PRO D 2 53  ? 144.527 105.399 119.809 1.00 39.26 ?  32  PRO D N     1 
ATOM   13633 C  CA    . PRO D 2 53  ? 145.998 105.416 119.704 1.00 40.41 ?  32  PRO D CA    1 
ATOM   13634 C  C     . PRO D 2 53  ? 146.518 106.146 118.458 1.00 41.91 ?  32  PRO D C     1 
ATOM   13635 O  O     . PRO D 2 53  ? 147.457 106.944 118.553 1.00 42.52 ?  32  PRO D O     1 
ATOM   13636 C  CB    . PRO D 2 53  ? 146.361 103.929 119.618 1.00 40.42 ?  32  PRO D CB    1 
ATOM   13637 C  CG    . PRO D 2 53  ? 145.205 103.213 120.191 1.00 40.01 ?  32  PRO D CG    1 
ATOM   13638 C  CD    . PRO D 2 53  ? 143.997 104.026 119.883 1.00 39.30 ?  32  PRO D CD    1 
ATOM   13639 N  N     . GLU D 2 54  ? 145.894 105.884 117.313 1.00 43.27 ?  33  GLU D N     1 
ATOM   13640 C  CA    . GLU D 2 54  ? 146.284 106.459 116.015 1.00 45.17 ?  33  GLU D CA    1 
ATOM   13641 C  C     . GLU D 2 54  ? 146.390 107.993 115.981 1.00 45.57 ?  33  GLU D C     1 
ATOM   13642 O  O     . GLU D 2 54  ? 147.066 108.551 115.111 1.00 46.08 ?  33  GLU D O     1 
ATOM   13643 C  CB    . GLU D 2 54  ? 145.312 105.988 114.923 1.00 45.55 ?  33  GLU D CB    1 
ATOM   13644 C  CG    . GLU D 2 54  ? 145.598 104.593 114.364 1.00 48.19 ?  33  GLU D CG    1 
ATOM   13645 C  CD    . GLU D 2 54  ? 145.459 103.480 115.394 1.00 50.61 ?  33  GLU D CD    1 
ATOM   13646 O  OE1   . GLU D 2 54  ? 144.438 103.454 116.121 1.00 51.10 ?  33  GLU D OE1   1 
ATOM   13647 O  OE2   . GLU D 2 54  ? 146.381 102.633 115.475 1.00 52.64 -1 33  GLU D OE2   1 
ATOM   13648 N  N     . GLU D 2 55  ? 145.723 108.661 116.921 1.00 45.74 ?  34  GLU D N     1 
ATOM   13649 C  CA    . GLU D 2 55  ? 145.687 110.128 116.970 1.00 46.28 ?  34  GLU D CA    1 
ATOM   13650 C  C     . GLU D 2 55  ? 147.052 110.759 117.274 1.00 46.49 ?  34  GLU D C     1 
ATOM   13651 O  O     . GLU D 2 55  ? 147.339 111.875 116.831 1.00 46.73 ?  34  GLU D O     1 
ATOM   13652 C  CB    . GLU D 2 55  ? 144.644 110.615 117.981 1.00 46.17 ?  34  GLU D CB    1 
ATOM   13653 C  CG    . GLU D 2 55  ? 143.197 110.239 117.648 1.00 47.10 ?  34  GLU D CG    1 
ATOM   13654 C  CD    . GLU D 2 55  ? 142.202 110.802 118.661 1.00 48.43 ?  34  GLU D CD    1 
ATOM   13655 O  OE1   . GLU D 2 55  ? 142.093 112.044 118.769 1.00 49.62 ?  34  GLU D OE1   1 
ATOM   13656 O  OE2   . GLU D 2 55  ? 141.528 110.006 119.347 1.00 47.11 -1 34  GLU D OE2   1 
ATOM   13657 N  N     . ILE D 2 56  ? 147.882 110.046 118.034 1.00 46.23 ?  35  ILE D N     1 
ATOM   13658 C  CA    . ILE D 2 56  ? 149.224 110.517 118.368 1.00 46.25 ?  35  ILE D CA    1 
ATOM   13659 C  C     . ILE D 2 56  ? 150.250 109.785 117.505 1.00 46.30 ?  35  ILE D C     1 
ATOM   13660 O  O     . ILE D 2 56  ? 150.345 108.554 117.552 1.00 46.36 ?  35  ILE D O     1 
ATOM   13661 C  CB    . ILE D 2 56  ? 149.562 110.301 119.885 1.00 45.84 ?  35  ILE D CB    1 
ATOM   13662 C  CG1   . ILE D 2 56  ? 148.376 110.657 120.806 1.00 46.15 ?  35  ILE D CG1   1 
ATOM   13663 C  CG2   . ILE D 2 56  ? 150.859 111.039 120.279 1.00 45.72 ?  35  ILE D CG2   1 
ATOM   13664 C  CD1   . ILE D 2 56  ? 147.926 112.114 120.780 1.00 47.27 ?  35  ILE D CD1   1 
ATOM   13665 N  N     . ALA D 2 57  ? 151.007 110.537 116.712 1.00 46.51 ?  36  ALA D N     1 
ATOM   13666 C  CA    . ALA D 2 57  ? 152.111 109.969 115.934 1.00 46.56 ?  36  ALA D CA    1 
ATOM   13667 C  C     . ALA D 2 57  ? 153.303 109.714 116.862 1.00 46.08 ?  36  ALA D C     1 
ATOM   13668 O  O     . ALA D 2 57  ? 153.748 110.625 117.558 1.00 45.70 ?  36  ALA D O     1 
ATOM   13669 C  CB    . ALA D 2 57  ? 152.505 110.905 114.794 1.00 47.10 ?  36  ALA D CB    1 
ATOM   13670 N  N     . LEU D 2 58  ? 153.818 108.486 116.857 1.00 45.66 ?  37  LEU D N     1 
ATOM   13671 C  CA    . LEU D 2 58  ? 154.858 108.086 117.817 1.00 45.27 ?  37  LEU D CA    1 
ATOM   13672 C  C     . LEU D 2 58  ? 156.305 108.187 117.339 1.00 45.25 ?  37  LEU D C     1 
ATOM   13673 O  O     . LEU D 2 58  ? 157.226 108.256 118.159 1.00 44.82 ?  37  LEU D O     1 
ATOM   13674 C  CB    . LEU D 2 58  ? 154.591 106.673 118.335 1.00 45.05 ?  37  LEU D CB    1 
ATOM   13675 C  CG    . LEU D 2 58  ? 153.510 106.580 119.409 1.00 45.41 ?  37  LEU D CG    1 
ATOM   13676 C  CD1   . LEU D 2 58  ? 153.289 105.129 119.792 1.00 45.40 ?  37  LEU D CD1   1 
ATOM   13677 C  CD2   . LEU D 2 58  ? 153.885 107.413 120.633 1.00 44.70 ?  37  LEU D CD2   1 
ATOM   13678 N  N     . ASN D 2 59  ? 156.506 108.210 116.024 1.00 45.33 ?  38  ASN D N     1 
ATOM   13679 C  CA    . ASN D 2 59  ? 157.850 108.070 115.456 1.00 45.22 ?  38  ASN D CA    1 
ATOM   13680 C  C     . ASN D 2 59  ? 158.873 109.126 115.899 1.00 44.39 ?  38  ASN D C     1 
ATOM   13681 O  O     . ASN D 2 59  ? 160.064 108.820 116.025 1.00 44.33 ?  38  ASN D O     1 
ATOM   13682 C  CB    . ASN D 2 59  ? 157.780 107.988 113.934 1.00 46.22 ?  38  ASN D CB    1 
ATOM   13683 C  CG    . ASN D 2 59  ? 158.826 107.052 113.354 1.00 47.90 ?  38  ASN D CG    1 
ATOM   13684 O  OD1   . ASN D 2 59  ? 159.697 107.472 112.593 1.00 49.28 ?  38  ASN D OD1   1 
ATOM   13685 N  ND2   . ASN D 2 59  ? 158.743 105.770 113.713 1.00 49.18 ?  38  ASN D ND2   1 
ATOM   13686 N  N     . GLY D 2 60  ? 158.403 110.348 116.156 1.00 43.45 ?  39  GLY D N     1 
ATOM   13687 C  CA    . GLY D 2 60  ? 159.260 111.451 116.602 1.00 42.42 ?  39  GLY D CA    1 
ATOM   13688 C  C     . GLY D 2 60  ? 159.896 111.290 117.981 1.00 41.55 ?  39  GLY D C     1 
ATOM   13689 O  O     . GLY D 2 60  ? 160.742 112.096 118.380 1.00 41.29 ?  39  GLY D O     1 
ATOM   13690 N  N     . ASP D 2 61  ? 159.488 110.257 118.716 1.00 40.35 ?  40  ASP D N     1 
ATOM   13691 C  CA    . ASP D 2 61  ? 160.114 109.937 120.005 1.00 39.53 ?  40  ASP D CA    1 
ATOM   13692 C  C     . ASP D 2 61  ? 161.520 109.371 119.862 1.00 39.38 ?  40  ASP D C     1 
ATOM   13693 O  O     . ASP D 2 61  ? 162.325 109.457 120.787 1.00 38.90 ?  40  ASP D O     1 
ATOM   13694 C  CB    . ASP D 2 61  ? 159.257 108.950 120.783 1.00 38.93 ?  40  ASP D CB    1 
ATOM   13695 C  CG    . ASP D 2 61  ? 158.182 109.626 121.586 1.00 38.21 ?  40  ASP D CG    1 
ATOM   13696 O  OD1   . ASP D 2 61  ? 158.099 110.875 121.568 1.00 38.79 ?  40  ASP D OD1   1 
ATOM   13697 O  OD2   . ASP D 2 61  ? 157.421 108.903 122.247 1.00 38.02 -1 40  ASP D OD2   1 
ATOM   13698 N  N     . LEU D 2 62  ? 161.805 108.793 118.700 1.00 39.82 ?  41  LEU D N     1 
ATOM   13699 C  CA    . LEU D 2 62  ? 163.107 108.194 118.428 1.00 40.22 ?  41  LEU D CA    1 
ATOM   13700 C  C     . LEU D 2 62  ? 164.226 109.235 118.453 1.00 40.40 ?  41  LEU D C     1 
ATOM   13701 O  O     . LEU D 2 62  ? 165.394 108.890 118.636 1.00 40.91 ?  41  LEU D O     1 
ATOM   13702 C  CB    . LEU D 2 62  ? 163.074 107.446 117.093 1.00 40.52 ?  41  LEU D CB    1 
ATOM   13703 C  CG    . LEU D 2 62  ? 162.155 106.220 117.029 1.00 41.03 ?  41  LEU D CG    1 
ATOM   13704 C  CD1   . LEU D 2 62  ? 162.142 105.632 115.625 1.00 42.53 ?  41  LEU D CD1   1 
ATOM   13705 C  CD2   . LEU D 2 62  ? 162.555 105.161 118.065 1.00 41.89 ?  41  LEU D CD2   1 
ATOM   13706 N  N     . LEU D 2 63  ? 163.847 110.507 118.293 1.00 40.20 ?  42  LEU D N     1 
ATOM   13707 C  CA    . LEU D 2 63  ? 164.772 111.639 118.310 1.00 39.85 ?  42  LEU D CA    1 
ATOM   13708 C  C     . LEU D 2 63  ? 165.243 112.022 119.726 1.00 38.90 ?  42  LEU D C     1 
ATOM   13709 O  O     . LEU D 2 63  ? 166.225 112.757 119.885 1.00 39.48 ?  42  LEU D O     1 
ATOM   13710 C  CB    . LEU D 2 63  ? 164.120 112.841 117.609 1.00 40.50 ?  42  LEU D CB    1 
ATOM   13711 C  CG    . LEU D 2 63  ? 164.938 113.863 116.803 1.00 41.98 ?  42  LEU D CG    1 
ATOM   13712 C  CD1   . LEU D 2 63  ? 165.770 113.209 115.705 1.00 43.07 ?  42  LEU D CD1   1 
ATOM   13713 C  CD2   . LEU D 2 63  ? 164.002 114.885 116.183 1.00 43.17 ?  42  LEU D CD2   1 
ATOM   13714 N  N     . THR D 2 64  ? 164.547 111.545 120.755 1.00 37.28 ?  43  THR D N     1 
ATOM   13715 C  CA    . THR D 2 64  ? 165.028 111.729 122.133 1.00 35.53 ?  43  THR D CA    1 
ATOM   13716 C  C     . THR D 2 64  ? 165.415 110.407 122.785 1.00 34.57 ?  43  THR D C     1 
ATOM   13717 O  O     . THR D 2 64  ? 166.291 110.371 123.654 1.00 34.23 ?  43  THR D O     1 
ATOM   13718 C  CB    . THR D 2 64  ? 164.038 112.501 123.034 1.00 35.18 ?  43  THR D CB    1 
ATOM   13719 O  OG1   . THR D 2 64  ? 162.721 111.956 122.909 1.00 34.59 ?  43  THR D OG1   1 
ATOM   13720 C  CG2   . THR D 2 64  ? 164.013 113.957 122.661 1.00 35.48 ?  43  THR D CG2   1 
ATOM   13721 N  N     . TRP D 2 65  ? 164.763 109.329 122.350 1.00 33.62 ?  44  TRP D N     1 
ATOM   13722 C  CA    . TRP D 2 65  ? 165.036 107.971 122.846 1.00 32.87 ?  44  TRP D CA    1 
ATOM   13723 C  C     . TRP D 2 65  ? 166.505 107.574 122.646 1.00 33.46 ?  44  TRP D C     1 
ATOM   13724 O  O     . TRP D 2 65  ? 167.132 107.016 123.548 1.00 32.58 ?  44  TRP D O     1 
ATOM   13725 C  CB    . TRP D 2 65  ? 164.107 106.965 122.149 1.00 32.09 ?  44  TRP D CB    1 
ATOM   13726 C  CG    . TRP D 2 65  ? 164.334 105.527 122.524 1.00 30.42 ?  44  TRP D CG    1 
ATOM   13727 C  CD1   . TRP D 2 65  ? 164.926 104.565 121.752 1.00 29.35 ?  44  TRP D CD1   1 
ATOM   13728 C  CD2   . TRP D 2 65  ? 163.969 104.885 123.756 1.00 28.04 ?  44  TRP D CD2   1 
ATOM   13729 N  NE1   . TRP D 2 65  ? 164.951 103.366 122.425 1.00 28.44 ?  44  TRP D NE1   1 
ATOM   13730 C  CE2   . TRP D 2 65  ? 164.375 103.535 123.657 1.00 28.14 ?  44  TRP D CE2   1 
ATOM   13731 C  CE3   . TRP D 2 65  ? 163.348 105.320 124.934 1.00 27.11 ?  44  TRP D CE3   1 
ATOM   13732 C  CZ2   . TRP D 2 65  ? 164.172 102.609 124.690 1.00 27.21 ?  44  TRP D CZ2   1 
ATOM   13733 C  CZ3   . TRP D 2 65  ? 163.138 104.395 125.961 1.00 27.45 ?  44  TRP D CZ3   1 
ATOM   13734 C  CH2   . TRP D 2 65  ? 163.546 103.054 125.825 1.00 27.25 ?  44  TRP D CH2   1 
ATOM   13735 N  N     . LYS D 2 66  ? 167.032 107.877 121.461 1.00 34.52 ?  45  LYS D N     1 
ATOM   13736 C  CA    . LYS D 2 66  ? 168.420 107.590 121.109 1.00 36.41 ?  45  LYS D CA    1 
ATOM   13737 C  C     . LYS D 2 66  ? 169.444 108.280 122.008 1.00 36.26 ?  45  LYS D C     1 
ATOM   13738 O  O     . LYS D 2 66  ? 170.590 107.838 122.085 1.00 36.52 ?  45  LYS D O     1 
ATOM   13739 C  CB    . LYS D 2 66  ? 168.688 107.948 119.641 1.00 36.98 ?  45  LYS D CB    1 
ATOM   13740 C  CG    . LYS D 2 66  ? 168.713 106.743 118.703 1.00 40.03 ?  45  LYS D CG    1 
ATOM   13741 C  CD    . LYS D 2 66  ? 167.325 106.122 118.503 1.00 43.70 ?  45  LYS D CD    1 
ATOM   13742 C  CE    . LYS D 2 66  ? 167.374 104.953 117.515 1.00 45.57 ?  45  LYS D CE    1 
ATOM   13743 N  NZ    . LYS D 2 66  ? 167.820 105.365 116.151 1.00 46.59 1  45  LYS D NZ    1 
ATOM   13744 N  N     . TYR D 2 67  ? 169.026 109.342 122.692 1.00 36.26 ?  46  TYR D N     1 
ATOM   13745 C  CA    . TYR D 2 67  ? 169.939 110.088 123.564 1.00 36.90 ?  46  TYR D CA    1 
ATOM   13746 C  C     . TYR D 2 67  ? 169.900 109.684 125.040 1.00 36.28 ?  46  TYR D C     1 
ATOM   13747 O  O     . TYR D 2 67  ? 170.647 110.235 125.843 1.00 36.44 ?  46  TYR D O     1 
ATOM   13748 C  CB    . TYR D 2 67  ? 169.742 111.601 123.412 1.00 37.15 ?  46  TYR D CB    1 
ATOM   13749 C  CG    . TYR D 2 67  ? 169.919 112.095 121.996 1.00 39.40 ?  46  TYR D CG    1 
ATOM   13750 C  CD1   . TYR D 2 67  ? 170.972 111.634 121.201 1.00 41.26 ?  46  TYR D CD1   1 
ATOM   13751 C  CD2   . TYR D 2 67  ? 169.052 113.040 121.457 1.00 41.06 ?  46  TYR D CD2   1 
ATOM   13752 C  CE1   . TYR D 2 67  ? 171.139 112.084 119.892 1.00 43.03 ?  46  TYR D CE1   1 
ATOM   13753 C  CE2   . TYR D 2 67  ? 169.215 113.505 120.150 1.00 43.05 ?  46  TYR D CE2   1 
ATOM   13754 C  CZ    . TYR D 2 67  ? 170.258 113.025 119.374 1.00 43.80 ?  46  TYR D CZ    1 
ATOM   13755 O  OH    . TYR D 2 67  ? 170.414 113.483 118.078 1.00 45.18 ?  46  TYR D OH    1 
ATOM   13756 N  N     . LEU D 2 68  ? 169.034 108.739 125.399 1.00 35.71 ?  47  LEU D N     1 
ATOM   13757 C  CA    . LEU D 2 68  ? 168.993 108.246 126.777 1.00 34.92 ?  47  LEU D CA    1 
ATOM   13758 C  C     . LEU D 2 68  ? 170.075 107.186 127.008 1.00 34.32 ?  47  LEU D C     1 
ATOM   13759 O  O     . LEU D 2 68  ? 170.422 106.432 126.095 1.00 34.50 ?  47  LEU D O     1 
ATOM   13760 C  CB    . LEU D 2 68  ? 167.609 107.681 127.131 1.00 35.00 ?  47  LEU D CB    1 
ATOM   13761 C  CG    . LEU D 2 68  ? 166.354 108.535 126.879 1.00 35.82 ?  47  LEU D CG    1 
ATOM   13762 C  CD1   . LEU D 2 68  ? 165.110 107.771 127.309 1.00 35.95 ?  47  LEU D CD1   1 
ATOM   13763 C  CD2   . LEU D 2 68  ? 166.410 109.896 127.572 1.00 35.97 ?  47  LEU D CD2   1 
ATOM   13764 N  N     . GLY D 2 69  ? 170.600 107.138 128.230 1.00 33.50 ?  48  GLY D N     1 
ATOM   13765 C  CA    . GLY D 2 69  ? 171.515 106.079 128.649 1.00 32.41 ?  48  GLY D CA    1 
ATOM   13766 C  C     . GLY D 2 69  ? 170.840 104.717 128.725 1.00 32.15 ?  48  GLY D C     1 
ATOM   13767 O  O     . GLY D 2 69  ? 169.607 104.615 128.690 1.00 30.98 ?  48  GLY D O     1 
ATOM   13768 N  N     . LYS D 2 70  ? 171.654 103.670 128.839 1.00 32.14 ?  49  LYS D N     1 
ATOM   13769 C  CA    . LYS D 2 70  ? 171.152 102.303 128.933 1.00 32.25 ?  49  LYS D CA    1 
ATOM   13770 C  C     . LYS D 2 70  ? 170.245 102.093 130.144 1.00 31.24 ?  49  LYS D C     1 
ATOM   13771 O  O     . LYS D 2 70  ? 169.209 101.445 130.017 1.00 31.34 ?  49  LYS D O     1 
ATOM   13772 C  CB    . LYS D 2 70  ? 172.304 101.296 128.956 1.00 33.07 ?  49  LYS D CB    1 
ATOM   13773 C  CG    . LYS D 2 70  ? 173.156 101.305 127.697 1.00 35.74 ?  49  LYS D CG    1 
ATOM   13774 C  CD    . LYS D 2 70  ? 174.432 100.497 127.916 1.00 39.67 ?  49  LYS D CD    1 
ATOM   13775 C  CE    . LYS D 2 70  ? 175.445 100.751 126.810 1.00 40.96 ?  49  LYS D CE    1 
ATOM   13776 N  NZ    . LYS D 2 70  ? 176.768 100.201 127.197 1.00 42.55 1  49  LYS D NZ    1 
ATOM   13777 N  N     . ASN D 2 71  ? 170.625 102.647 131.300 1.00 29.92 ?  50  ASN D N     1 
ATOM   13778 C  CA    . ASN D 2 71  ? 169.815 102.523 132.518 1.00 29.37 ?  50  ASN D CA    1 
ATOM   13779 C  C     . ASN D 2 71  ? 168.457 103.203 132.370 1.00 28.35 ?  50  ASN D C     1 
ATOM   13780 O  O     . ASN D 2 71  ? 167.443 102.666 132.831 1.00 27.64 ?  50  ASN D O     1 
ATOM   13781 C  CB    . ASN D 2 71  ? 170.538 103.063 133.766 1.00 29.38 ?  50  ASN D CB    1 
ATOM   13782 C  CG    . ASN D 2 71  ? 171.623 102.120 134.284 1.00 31.22 ?  50  ASN D CG    1 
ATOM   13783 O  OD1   . ASN D 2 71  ? 171.530 100.898 134.149 1.00 33.03 ?  50  ASN D OD1   1 
ATOM   13784 N  ND2   . ASN D 2 71  ? 172.656 102.692 134.893 1.00 31.97 ?  50  ASN D ND2   1 
ATOM   13785 N  N     . GLU D 2 72  ? 168.445 104.369 131.719 1.00 27.72 ?  51  GLU D N     1 
ATOM   13786 C  CA    . GLU D 2 72  ? 167.191 105.095 131.462 1.00 27.70 ?  51  GLU D CA    1 
ATOM   13787 C  C     . GLU D 2 72  ? 166.268 104.310 130.526 1.00 27.62 ?  51  GLU D C     1 
ATOM   13788 O  O     . GLU D 2 72  ? 165.057 104.231 130.753 1.00 27.56 ?  51  GLU D O     1 
ATOM   13789 C  CB    . GLU D 2 72  ? 167.459 106.484 130.872 1.00 27.55 ?  51  GLU D CB    1 
ATOM   13790 C  CG    . GLU D 2 72  ? 168.306 107.411 131.753 1.00 28.77 ?  51  GLU D CG    1 
ATOM   13791 C  CD    . GLU D 2 72  ? 168.419 108.801 131.155 1.00 31.18 ?  51  GLU D CD    1 
ATOM   13792 O  OE1   . GLU D 2 72  ? 169.130 108.960 130.140 1.00 33.17 ?  51  GLU D OE1   1 
ATOM   13793 O  OE2   . GLU D 2 72  ? 167.788 109.732 131.694 1.00 31.66 -1 51  GLU D OE2   1 
ATOM   13794 N  N     . GLN D 2 73  ? 166.850 103.733 129.478 1.00 27.32 ?  52  GLN D N     1 
ATOM   13795 C  CA    . GLN D 2 73  ? 166.090 102.949 128.510 1.00 27.33 ?  52  GLN D CA    1 
ATOM   13796 C  C     . GLN D 2 73  ? 165.563 101.669 129.164 1.00 26.85 ?  52  GLN D C     1 
ATOM   13797 O  O     . GLN D 2 73  ? 164.409 101.286 128.949 1.00 26.24 ?  52  GLN D O     1 
ATOM   13798 C  CB    . GLN D 2 73  ? 166.941 102.628 127.287 1.00 27.65 ?  52  GLN D CB    1 
ATOM   13799 C  CG    . GLN D 2 73  ? 167.194 103.821 126.345 1.00 29.66 ?  52  GLN D CG    1 
ATOM   13800 C  CD    . GLN D 2 73  ? 167.881 103.419 125.041 1.00 32.60 ?  52  GLN D CD    1 
ATOM   13801 O  OE1   . GLN D 2 73  ? 168.509 102.366 124.955 1.00 34.76 ?  52  GLN D OE1   1 
ATOM   13802 N  NE2   . GLN D 2 73  ? 167.777 104.268 124.029 1.00 33.42 ?  52  GLN D NE2   1 
ATOM   13803 N  N     . ASP D 2 74  ? 166.405 101.045 129.985 1.00 26.26 ?  53  ASP D N     1 
ATOM   13804 C  CA    . ASP D 2 74  ? 166.055 99.832  130.733 1.00 26.50 ?  53  ASP D CA    1 
ATOM   13805 C  C     . ASP D 2 74  ? 164.916 100.091 131.709 1.00 25.81 ?  53  ASP D C     1 
ATOM   13806 O  O     . ASP D 2 74  ? 163.952 99.331  131.751 1.00 26.12 ?  53  ASP D O     1 
ATOM   13807 C  CB    . ASP D 2 74  ? 167.285 99.317  131.493 1.00 26.84 ?  53  ASP D CB    1 
ATOM   13808 C  CG    . ASP D 2 74  ? 167.053 97.972  132.180 1.00 29.50 ?  53  ASP D CG    1 
ATOM   13809 O  OD1   . ASP D 2 74  ? 166.814 96.960  131.487 1.00 32.08 ?  53  ASP D OD1   1 
ATOM   13810 O  OD2   . ASP D 2 74  ? 167.159 97.918  133.422 1.00 33.52 -1 53  ASP D OD2   1 
ATOM   13811 N  N     . THR D 2 75  ? 165.023 101.163 132.492 1.00 25.10 ?  54  THR D N     1 
ATOM   13812 C  CA    . THR D 2 75  ? 163.973 101.499 133.457 1.00 24.11 ?  54  THR D CA    1 
ATOM   13813 C  C     . THR D 2 75  ? 162.651 101.774 132.735 1.00 23.82 ?  54  THR D C     1 
ATOM   13814 O  O     . THR D 2 75  ? 161.608 101.243 133.118 1.00 23.81 ?  54  THR D O     1 
ATOM   13815 C  CB    . THR D 2 75  ? 164.377 102.684 134.356 1.00 23.80 ?  54  THR D CB    1 
ATOM   13816 O  OG1   . THR D 2 75  ? 165.525 102.311 135.131 1.00 24.62 ?  54  THR D OG1   1 
ATOM   13817 C  CG2   . THR D 2 75  ? 163.230 103.069 135.308 1.00 23.25 ?  54  THR D CG2   1 
ATOM   13818 N  N     . TYR D 2 76  ? 162.703 102.610 131.707 1.00 24.06 ?  55  TYR D N     1 
ATOM   13819 C  CA    . TYR D 2 76  ? 161.522 102.918 130.906 1.00 24.76 ?  55  TYR D CA    1 
ATOM   13820 C  C     . TYR D 2 76  ? 160.827 101.662 130.363 1.00 24.85 ?  55  TYR D C     1 
ATOM   13821 O  O     . TYR D 2 76  ? 159.609 101.517 130.504 1.00 24.83 ?  55  TYR D O     1 
ATOM   13822 C  CB    . TYR D 2 76  ? 161.875 103.859 129.754 1.00 24.78 ?  55  TYR D CB    1 
ATOM   13823 C  CG    . TYR D 2 76  ? 160.673 104.599 129.203 1.00 26.19 ?  55  TYR D CG    1 
ATOM   13824 C  CD1   . TYR D 2 76  ? 160.312 105.843 129.722 1.00 27.81 ?  55  TYR D CD1   1 
ATOM   13825 C  CD2   . TYR D 2 76  ? 159.889 104.057 128.181 1.00 28.03 ?  55  TYR D CD2   1 
ATOM   13826 C  CE1   . TYR D 2 76  ? 159.214 106.539 129.233 1.00 29.32 ?  55  TYR D CE1   1 
ATOM   13827 C  CE2   . TYR D 2 76  ? 158.775 104.748 127.681 1.00 29.01 ?  55  TYR D CE2   1 
ATOM   13828 C  CZ    . TYR D 2 76  ? 158.450 105.988 128.218 1.00 30.76 ?  55  TYR D CZ    1 
ATOM   13829 O  OH    . TYR D 2 76  ? 157.371 106.701 127.750 1.00 34.50 ?  55  TYR D OH    1 
ATOM   13830 N  N     . MET D 2 77  ? 161.599 100.768 129.747 1.00 25.76 ?  56  MET D N     1 
ATOM   13831 C  CA    . MET D 2 77  ? 161.062 99.507  129.226 1.00 26.81 ?  56  MET D CA    1 
ATOM   13832 C  C     . MET D 2 77  ? 160.371 98.687  130.320 1.00 26.23 ?  56  MET D C     1 
ATOM   13833 O  O     . MET D 2 77  ? 159.262 98.186  130.126 1.00 25.00 ?  56  MET D O     1 
ATOM   13834 C  CB    . MET D 2 77  ? 162.164 98.674  128.574 1.00 28.11 ?  56  MET D CB    1 
ATOM   13835 C  CG    . MET D 2 77  ? 162.720 99.239  127.262 1.00 32.52 ?  56  MET D CG    1 
ATOM   13836 S  SD    . MET D 2 77  ? 161.598 99.088  125.863 1.00 42.68 ?  56  MET D SD    1 
ATOM   13837 C  CE    . MET D 2 77  ? 160.590 100.564 126.010 1.00 38.97 ?  56  MET D CE    1 
ATOM   13838 N  N     . LYS D 2 78  ? 161.045 98.553  131.463 1.00 26.01 ?  57  LYS D N     1 
ATOM   13839 C  CA    . LYS D 2 78  ? 160.531 97.756  132.580 1.00 26.07 ?  57  LYS D CA    1 
ATOM   13840 C  C     . LYS D 2 78  ? 159.261 98.354  133.183 1.00 25.69 ?  57  LYS D C     1 
ATOM   13841 O  O     . LYS D 2 78  ? 158.324 97.625  133.531 1.00 25.58 ?  57  LYS D O     1 
ATOM   13842 C  CB    . LYS D 2 78  ? 161.603 97.568  133.663 1.00 26.08 ?  57  LYS D CB    1 
ATOM   13843 C  CG    . LYS D 2 78  ? 162.761 96.655  133.234 1.00 27.64 ?  57  LYS D CG    1 
ATOM   13844 C  CD    . LYS D 2 78  ? 163.876 96.642  134.273 1.00 29.47 ?  57  LYS D CD    1 
ATOM   13845 C  CE    . LYS D 2 78  ? 164.909 95.578  133.936 1.00 31.69 ?  57  LYS D CE    1 
ATOM   13846 N  NZ    . LYS D 2 78  ? 166.003 95.518  134.941 1.00 33.36 1  57  LYS D NZ    1 
ATOM   13847 N  N     . VAL D 2 79  ? 159.239 99.679  133.307 1.00 25.32 ?  58  VAL D N     1 
ATOM   13848 C  CA    . VAL D 2 79  ? 158.075 100.401 133.834 1.00 25.47 ?  58  VAL D CA    1 
ATOM   13849 C  C     . VAL D 2 79  ? 156.898 100.214 132.882 1.00 25.09 ?  58  VAL D C     1 
ATOM   13850 O  O     . VAL D 2 79  ? 155.785 99.886  133.300 1.00 24.46 ?  58  VAL D O     1 
ATOM   13851 C  CB    . VAL D 2 79  ? 158.410 101.908 134.014 1.00 25.83 ?  58  VAL D CB    1 
ATOM   13852 C  CG1   . VAL D 2 79  ? 157.173 102.771 133.910 1.00 27.35 ?  58  VAL D CG1   1 
ATOM   13853 C  CG2   . VAL D 2 79  ? 159.151 102.127 135.332 1.00 26.42 ?  58  VAL D CG2   1 
ATOM   13854 N  N     . LEU D 2 80  ? 157.178 100.379 131.591 1.00 25.27 ?  59  LEU D N     1 
ATOM   13855 C  CA    . LEU D 2 80  ? 156.163 100.277 130.566 1.00 25.55 ?  59  LEU D CA    1 
ATOM   13856 C  C     . LEU D 2 80  ? 155.533 98.886  130.577 1.00 24.94 ?  59  LEU D C     1 
ATOM   13857 O  O     . LEU D 2 80  ? 154.312 98.761  130.497 1.00 24.82 ?  59  LEU D O     1 
ATOM   13858 C  CB    . LEU D 2 80  ? 156.770 100.576 129.194 1.00 25.80 ?  59  LEU D CB    1 
ATOM   13859 C  CG    . LEU D 2 80  ? 156.231 101.692 128.292 1.00 28.76 ?  59  LEU D CG    1 
ATOM   13860 C  CD1   . LEU D 2 80  ? 156.441 101.273 126.836 1.00 30.25 ?  59  LEU D CD1   1 
ATOM   13861 C  CD2   . LEU D 2 80  ? 154.774 102.050 128.533 1.00 27.79 ?  59  LEU D CD2   1 
ATOM   13862 N  N     . ALA D 2 81  ? 156.370 97.852  130.681 1.00 24.86 ?  60  ALA D N     1 
ATOM   13863 C  CA    . ALA D 2 81  ? 155.894 96.462  130.713 1.00 24.60 ?  60  ALA D CA    1 
ATOM   13864 C  C     . ALA D 2 81  ? 155.066 96.204  131.968 1.00 23.80 ?  60  ALA D C     1 
ATOM   13865 O  O     . ALA D 2 81  ? 154.064 95.499  131.925 1.00 24.07 ?  60  ALA D O     1 
ATOM   13866 C  CB    . ALA D 2 81  ? 157.070 95.489  130.639 1.00 24.48 ?  60  ALA D CB    1 
ATOM   13867 N  N     . GLY D 2 82  ? 155.488 96.789  133.082 1.00 23.54 ?  61  GLY D N     1 
ATOM   13868 C  CA    . GLY D 2 82  ? 154.738 96.711  134.331 1.00 22.53 ?  61  GLY D CA    1 
ATOM   13869 C  C     . GLY D 2 82  ? 153.336 97.263  134.173 1.00 22.23 ?  61  GLY D C     1 
ATOM   13870 O  O     . GLY D 2 82  ? 152.360 96.615  134.548 1.00 21.27 ?  61  GLY D O     1 
ATOM   13871 N  N     . LEU D 2 83  ? 153.234 98.466  133.610 1.00 22.36 ?  62  LEU D N     1 
ATOM   13872 C  CA    . LEU D 2 83  ? 151.928 99.091  133.370 1.00 22.42 ?  62  LEU D CA    1 
ATOM   13873 C  C     . LEU D 2 83  ? 151.079 98.253  132.425 1.00 22.91 ?  62  LEU D C     1 
ATOM   13874 O  O     . LEU D 2 83  ? 149.881 98.055  132.666 1.00 22.99 ?  62  LEU D O     1 
ATOM   13875 C  CB    . LEU D 2 83  ? 152.085 100.508 132.802 1.00 22.19 ?  62  LEU D CB    1 
ATOM   13876 C  CG    . LEU D 2 83  ? 152.732 101.555 133.723 1.00 22.17 ?  62  LEU D CG    1 
ATOM   13877 C  CD1   . LEU D 2 83  ? 153.131 102.791 132.907 1.00 21.55 ?  62  LEU D CD1   1 
ATOM   13878 C  CD2   . LEU D 2 83  ? 151.768 101.926 134.838 1.00 22.42 ?  62  LEU D CD2   1 
ATOM   13879 N  N     . THR D 2 84  ? 151.706 97.746  131.368 1.00 23.39 ?  63  THR D N     1 
ATOM   13880 C  CA    . THR D 2 84  ? 150.999 96.952  130.366 1.00 24.42 ?  63  THR D CA    1 
ATOM   13881 C  C     . THR D 2 84  ? 150.379 95.702  130.994 1.00 24.55 ?  63  THR D C     1 
ATOM   13882 O  O     . THR D 2 84  ? 149.193 95.422  130.803 1.00 23.68 ?  63  THR D O     1 
ATOM   13883 C  CB    . THR D 2 84  ? 151.928 96.542  129.195 1.00 24.70 ?  63  THR D CB    1 
ATOM   13884 O  OG1   . THR D 2 84  ? 152.456 97.719  128.570 1.00 25.57 ?  63  THR D OG1   1 
ATOM   13885 C  CG2   . THR D 2 84  ? 151.152 95.750  128.156 1.00 25.36 ?  63  THR D CG2   1 
ATOM   13886 N  N     . LEU D 2 85  ? 151.200 94.971  131.741 1.00 25.38 ?  64  LEU D N     1 
ATOM   13887 C  CA    . LEU D 2 85  ? 150.768 93.739  132.389 1.00 26.44 ?  64  LEU D CA    1 
ATOM   13888 C  C     . LEU D 2 85  ? 149.635 93.976  133.391 1.00 25.96 ?  64  LEU D C     1 
ATOM   13889 O  O     . LEU D 2 85  ? 148.627 93.255  133.355 1.00 25.83 ?  64  LEU D O     1 
ATOM   13890 C  CB    . LEU D 2 85  ? 151.963 92.990  133.000 1.00 26.65 ?  64  LEU D CB    1 
ATOM   13891 C  CG    . LEU D 2 85  ? 152.811 92.264  131.937 1.00 29.62 ?  64  LEU D CG    1 
ATOM   13892 C  CD1   . LEU D 2 85  ? 154.231 92.017  132.412 1.00 31.57 ?  64  LEU D CD1   1 
ATOM   13893 C  CD2   . LEU D 2 85  ? 152.167 90.938  131.491 1.00 30.96 ?  64  LEU D CD2   1 
ATOM   13894 N  N     . LEU D 2 86  ? 149.763 94.999  134.239 1.00 25.63 ?  65  LEU D N     1 
ATOM   13895 C  CA    . LEU D 2 86  ? 148.687 95.320  135.179 1.00 25.59 ?  65  LEU D CA    1 
ATOM   13896 C  C     . LEU D 2 86  ? 147.394 95.762  134.494 1.00 25.60 ?  65  LEU D C     1 
ATOM   13897 O  O     . LEU D 2 86  ? 146.296 95.420  134.943 1.00 25.47 ?  65  LEU D O     1 
ATOM   13898 C  CB    . LEU D 2 86  ? 149.124 96.361  136.228 1.00 25.76 ?  65  LEU D CB    1 
ATOM   13899 C  CG    . LEU D 2 86  ? 150.159 95.890  137.258 1.00 26.71 ?  65  LEU D CG    1 
ATOM   13900 C  CD1   . LEU D 2 86  ? 150.758 97.062  138.030 1.00 28.01 ?  65  LEU D CD1   1 
ATOM   13901 C  CD2   . LEU D 2 86  ? 149.564 94.888  138.220 1.00 28.01 ?  65  LEU D CD2   1 
ATOM   13902 N  N     . ASP D 2 87  ? 147.517 96.528  133.417 1.00 25.49 ?  66  ASP D N     1 
ATOM   13903 C  CA    . ASP D 2 87  ? 146.341 97.047  132.739 1.00 25.83 ?  66  ASP D CA    1 
ATOM   13904 C  C     . ASP D 2 87  ? 145.560 95.947  132.007 1.00 26.20 ?  66  ASP D C     1 
ATOM   13905 O  O     . ASP D 2 87  ? 144.342 96.022  131.886 1.00 25.99 ?  66  ASP D O     1 
ATOM   13906 C  CB    . ASP D 2 87  ? 146.722 98.175  131.789 1.00 25.50 ?  66  ASP D CB    1 
ATOM   13907 C  CG    . ASP D 2 87  ? 145.634 99.203  131.664 1.00 25.76 ?  66  ASP D CG    1 
ATOM   13908 O  OD1   . ASP D 2 87  ? 144.857 99.362  132.636 1.00 26.91 ?  66  ASP D OD1   1 
ATOM   13909 O  OD2   . ASP D 2 87  ? 145.547 99.856  130.606 1.00 23.11 -1 66  ASP D OD2   1 
ATOM   13910 N  N     . THR D 2 88  ? 146.273 94.923  131.547 1.00 27.12 ?  67  THR D N     1 
ATOM   13911 C  CA    . THR D 2 88  ? 145.662 93.756  130.926 1.00 28.40 ?  67  THR D CA    1 
ATOM   13912 C  C     . THR D 2 88  ? 144.788 92.998  131.911 1.00 28.28 ?  67  THR D C     1 
ATOM   13913 O  O     . THR D 2 88  ? 143.691 92.566  131.560 1.00 28.10 ?  67  THR D O     1 
ATOM   13914 C  CB    . THR D 2 88  ? 146.725 92.811  130.331 1.00 29.04 ?  67  THR D CB    1 
ATOM   13915 O  OG1   . THR D 2 88  ? 147.484 93.525  129.353 1.00 31.00 ?  67  THR D OG1   1 
ATOM   13916 C  CG2   . THR D 2 88  ? 146.064 91.612  129.654 1.00 30.16 ?  67  THR D CG2   1 
ATOM   13917 N  N     . GLU D 2 89  ? 145.264 92.839  133.144 1.00 28.28 ?  68  GLU D N     1 
ATOM   13918 C  CA    . GLU D 2 89  ? 144.447 92.216  134.180 1.00 29.16 ?  68  GLU D CA    1 
ATOM   13919 C  C     . GLU D 2 89  ? 143.167 93.023  134.389 1.00 28.65 ?  68  GLU D C     1 
ATOM   13920 O  O     . GLU D 2 89  ? 142.093 92.454  134.530 1.00 28.44 ?  68  GLU D O     1 
ATOM   13921 C  CB    . GLU D 2 89  ? 145.210 92.083  135.506 1.00 29.32 ?  68  GLU D CB    1 
ATOM   13922 C  CG    . GLU D 2 89  ? 146.482 91.228  135.429 1.00 31.95 ?  68  GLU D CG    1 
ATOM   13923 C  CD    . GLU D 2 89  ? 146.224 89.763  135.090 1.00 35.19 ?  68  GLU D CD    1 
ATOM   13924 O  OE1   . GLU D 2 89  ? 145.072 89.286  135.203 1.00 35.47 ?  68  GLU D OE1   1 
ATOM   13925 O  OE2   . GLU D 2 89  ? 147.195 89.081  134.701 1.00 38.06 -1 68  GLU D OE2   1 
ATOM   13926 N  N     . GLN D 2 90  ? 143.287 94.347  134.389 1.00 28.45 ?  69  GLN D N     1 
ATOM   13927 C  CA    . GLN D 2 90  ? 142.125 95.210  134.605 1.00 28.47 ?  69  GLN D CA    1 
ATOM   13928 C  C     . GLN D 2 90  ? 141.108 95.101  133.460 1.00 28.97 ?  69  GLN D C     1 
ATOM   13929 O  O     . GLN D 2 90  ? 139.901 95.097  133.700 1.00 28.84 ?  69  GLN D O     1 
ATOM   13930 C  CB    . GLN D 2 90  ? 142.560 96.661  134.838 1.00 28.21 ?  69  GLN D CB    1 
ATOM   13931 C  CG    . GLN D 2 90  ? 141.494 97.549  135.477 1.00 27.75 ?  69  GLN D CG    1 
ATOM   13932 C  CD    . GLN D 2 90  ? 141.230 97.242  136.947 1.00 28.91 ?  69  GLN D CD    1 
ATOM   13933 O  OE1   . GLN D 2 90  ? 141.515 96.142  137.441 1.00 27.62 ?  69  GLN D OE1   1 
ATOM   13934 N  NE2   . GLN D 2 90  ? 140.656 98.218  137.653 1.00 28.23 ?  69  GLN D NE2   1 
ATOM   13935 N  N     . GLY D 2 91  ? 141.600 94.985  132.226 1.00 29.62 ?  70  GLY D N     1 
ATOM   13936 C  CA    . GLY D 2 91  ? 140.736 94.816  131.057 1.00 30.43 ?  70  GLY D CA    1 
ATOM   13937 C  C     . GLY D 2 91  ? 140.079 93.446  130.935 1.00 31.11 ?  70  GLY D C     1 
ATOM   13938 O  O     . GLY D 2 91  ? 138.906 93.334  130.566 1.00 30.77 ?  70  GLY D O     1 
ATOM   13939 N  N     . ASN D 2 92  ? 140.833 92.398  131.232 1.00 31.69 ?  71  ASN D N     1 
ATOM   13940 C  CA    . ASN D 2 92  ? 140.299 91.047  131.110 1.00 32.72 ?  71  ASN D CA    1 
ATOM   13941 C  C     . ASN D 2 92  ? 139.469 90.570  132.293 1.00 32.60 ?  71  ASN D C     1 
ATOM   13942 O  O     . ASN D 2 92  ? 138.560 89.756  132.112 1.00 33.12 ?  71  ASN D O     1 
ATOM   13943 C  CB    . ASN D 2 92  ? 141.416 90.055  130.812 1.00 33.68 ?  71  ASN D CB    1 
ATOM   13944 C  CG    . ASN D 2 92  ? 141.948 90.196  129.401 1.00 35.15 ?  71  ASN D CG    1 
ATOM   13945 O  OD1   . ASN D 2 92  ? 143.099 89.868  129.139 1.00 40.21 ?  71  ASN D OD1   1 
ATOM   13946 N  ND2   . ASN D 2 92  ? 141.115 90.698  128.487 1.00 36.91 ?  71  ASN D ND2   1 
ATOM   13947 N  N     . THR D 2 93  ? 139.766 91.090  133.484 1.00 31.76 ?  72  THR D N     1 
ATOM   13948 C  CA    . THR D 2 93  ? 139.130 90.616  134.707 1.00 31.47 ?  72  THR D CA    1 
ATOM   13949 C  C     . THR D 2 93  ? 138.521 91.727  135.560 1.00 30.62 ?  72  THR D C     1 
ATOM   13950 O  O     . THR D 2 93  ? 137.322 91.708  135.827 1.00 30.71 ?  72  THR D O     1 
ATOM   13951 C  CB    . THR D 2 93  ? 140.112 89.805  135.549 1.00 31.60 ?  72  THR D CB    1 
ATOM   13952 O  OG1   . THR D 2 93  ? 140.637 88.737  134.750 1.00 33.14 ?  72  THR D OG1   1 
ATOM   13953 C  CG2   . THR D 2 93  ? 139.422 89.230  136.776 1.00 31.89 ?  72  THR D CG2   1 
ATOM   13954 N  N     . GLY D 2 94  ? 139.346 92.686  135.974 1.00 29.61 ?  73  GLY D N     1 
ATOM   13955 C  CA    . GLY D 2 94  ? 138.932 93.723  136.921 1.00 28.47 ?  73  GLY D CA    1 
ATOM   13956 C  C     . GLY D 2 94  ? 137.660 94.469  136.572 1.00 27.90 ?  73  GLY D C     1 
ATOM   13957 O  O     . GLY D 2 94  ? 136.716 94.525  137.372 1.00 28.27 ?  73  GLY D O     1 
ATOM   13958 N  N     . MET D 2 95  ? 137.624 95.073  135.392 1.00 26.67 ?  74  MET D N     1 
ATOM   13959 C  CA    . MET D 2 95  ? 136.424 95.819  135.021 1.00 26.00 ?  74  MET D CA    1 
ATOM   13960 C  C     . MET D 2 95  ? 135.267 94.895  134.663 1.00 25.25 ?  74  MET D C     1 
ATOM   13961 O  O     . MET D 2 95  ? 134.147 95.151  135.086 1.00 24.97 ?  74  MET D O     1 
ATOM   13962 C  CB    . MET D 2 95  ? 136.682 96.842  133.907 1.00 26.00 ?  74  MET D CB    1 
ATOM   13963 C  CG    . MET D 2 95  ? 137.328 98.119  134.388 1.00 26.40 ?  74  MET D CG    1 
ATOM   13964 S  SD    . MET D 2 95  ? 136.338 99.039  135.594 1.00 28.10 ?  74  MET D SD    1 
ATOM   13965 C  CE    . MET D 2 95  ? 137.519 100.312 136.019 1.00 28.95 ?  74  MET D CE    1 
ATOM   13966 N  N     . PRO D 2 96  ? 135.523 93.830  133.879 1.00 24.98 ?  75  PRO D N     1 
ATOM   13967 C  CA    . PRO D 2 96  ? 134.359 92.989  133.548 1.00 24.59 ?  75  PRO D CA    1 
ATOM   13968 C  C     . PRO D 2 96  ? 133.741 92.272  134.745 1.00 23.90 ?  75  PRO D C     1 
ATOM   13969 O  O     . PRO D 2 96  ? 132.535 92.056  134.749 1.00 23.45 ?  75  PRO D O     1 
ATOM   13970 C  CB    . PRO D 2 96  ? 134.923 91.962  132.556 1.00 24.80 ?  75  PRO D CB    1 
ATOM   13971 C  CG    . PRO D 2 96  ? 136.122 92.650  131.943 1.00 25.75 ?  75  PRO D CG    1 
ATOM   13972 C  CD    . PRO D 2 96  ? 136.702 93.488  133.053 1.00 25.07 ?  75  PRO D CD    1 
ATOM   13973 N  N     . ILE D 2 97  ? 134.550 91.897  135.740 1.00 23.36 ?  76  ILE D N     1 
ATOM   13974 C  CA    . ILE D 2 97  ? 134.014 91.182  136.894 1.00 23.48 ?  76  ILE D CA    1 
ATOM   13975 C  C     . ILE D 2 97  ? 133.164 92.105  137.752 1.00 23.30 ?  76  ILE D C     1 
ATOM   13976 O  O     . ILE D 2 97  ? 132.138 91.685  138.281 1.00 23.45 ?  76  ILE D O     1 
ATOM   13977 C  CB    . ILE D 2 97  ? 135.114 90.467  137.729 1.00 23.96 ?  76  ILE D CB    1 
ATOM   13978 C  CG1   . ILE D 2 97  ? 134.529 89.279  138.485 1.00 24.71 ?  76  ILE D CG1   1 
ATOM   13979 C  CG2   . ILE D 2 97  ? 135.845 91.436  138.689 1.00 24.02 ?  76  ILE D CG2   1 
ATOM   13980 C  CD1   . ILE D 2 97  ? 135.538 88.113  138.628 1.00 29.17 ?  76  ILE D CD1   1 
ATOM   13981 N  N     . VAL D 2 98  ? 133.584 93.363  137.877 1.00 22.71 ?  77  VAL D N     1 
ATOM   13982 C  CA    . VAL D 2 98  ? 132.808 94.356  138.638 1.00 22.78 ?  77  VAL D CA    1 
ATOM   13983 C  C     . VAL D 2 98  ? 131.503 94.683  137.908 1.00 22.89 ?  77  VAL D C     1 
ATOM   13984 O  O     . VAL D 2 98  ? 130.441 94.758  138.525 1.00 23.72 ?  77  VAL D O     1 
ATOM   13985 C  CB    . VAL D 2 98  ? 133.649 95.625  138.950 1.00 22.49 ?  77  VAL D CB    1 
ATOM   13986 C  CG1   . VAL D 2 98  ? 132.781 96.752  139.539 1.00 21.91 ?  77  VAL D CG1   1 
ATOM   13987 C  CG2   . VAL D 2 98  ? 134.763 95.272  139.922 1.00 23.02 ?  77  VAL D CG2   1 
ATOM   13988 N  N     . ALA D 2 99  ? 131.578 94.841  136.587 1.00 23.19 ?  78  ALA D N     1 
ATOM   13989 C  CA    . ALA D 2 99  ? 130.374 95.080  135.778 1.00 23.05 ?  78  ALA D CA    1 
ATOM   13990 C  C     . ALA D 2 99  ? 129.368 93.937  135.938 1.00 23.52 ?  78  ALA D C     1 
ATOM   13991 O  O     . ALA D 2 99  ? 128.153 94.156  135.987 1.00 23.68 ?  78  ALA D O     1 
ATOM   13992 C  CB    . ALA D 2 99  ? 130.749 95.274  134.318 1.00 22.81 ?  78  ALA D CB    1 
ATOM   13993 N  N     . GLU D 2 100 ? 129.876 92.712  136.029 1.00 23.68 ?  79  GLU D N     1 
ATOM   13994 C  CA    . GLU D 2 100 ? 129.021 91.542  136.212 1.00 24.14 ?  79  GLU D CA    1 
ATOM   13995 C  C     . GLU D 2 100 ? 128.231 91.542  137.531 1.00 23.66 ?  79  GLU D C     1 
ATOM   13996 O  O     . GLU D 2 100 ? 127.046 91.196  137.553 1.00 22.94 ?  79  GLU D O     1 
ATOM   13997 C  CB    . GLU D 2 100 ? 129.862 90.270  136.100 1.00 24.47 ?  79  GLU D CB    1 
ATOM   13998 C  CG    . GLU D 2 100 ? 129.046 88.994  136.038 1.00 27.90 ?  79  GLU D CG    1 
ATOM   13999 C  CD    . GLU D 2 100 ? 129.907 87.746  136.107 1.00 32.30 ?  79  GLU D CD    1 
ATOM   14000 O  OE1   . GLU D 2 100 ? 131.095 87.806  135.714 1.00 32.88 ?  79  GLU D OE1   1 
ATOM   14001 O  OE2   . GLU D 2 100 ? 129.390 86.705  136.562 1.00 34.74 -1 79  GLU D OE2   1 
ATOM   14002 N  N     . HIS D 2 101 ? 128.886 91.918  138.629 1.00 23.62 ?  80  HIS D N     1 
ATOM   14003 C  CA    . HIS D 2 101 ? 128.255 91.851  139.960 1.00 23.99 ?  80  HIS D CA    1 
ATOM   14004 C  C     . HIS D 2 101 ? 127.504 93.107  140.422 1.00 24.35 ?  80  HIS D C     1 
ATOM   14005 O  O     . HIS D 2 101 ? 126.691 93.033  141.344 1.00 24.21 ?  80  HIS D O     1 
ATOM   14006 C  CB    . HIS D 2 101 ? 129.278 91.405  141.014 1.00 24.13 ?  80  HIS D CB    1 
ATOM   14007 C  CG    . HIS D 2 101 ? 129.768 90.002  140.811 1.00 24.76 ?  80  HIS D CG    1 
ATOM   14008 N  ND1   . HIS D 2 101 ? 129.195 88.915  141.438 1.00 25.68 ?  80  HIS D ND1   1 
ATOM   14009 C  CD2   . HIS D 2 101 ? 130.758 89.507  140.032 1.00 25.75 ?  80  HIS D CD2   1 
ATOM   14010 C  CE1   . HIS D 2 101 ? 129.816 87.811  141.057 1.00 26.21 ?  80  HIS D CE1   1 
ATOM   14011 N  NE2   . HIS D 2 101 ? 130.769 88.143  140.205 1.00 25.35 ?  80  HIS D NE2   1 
ATOM   14012 N  N     . VAL D 2 102 ? 127.779 94.254  139.803 1.00 24.50 ?  81  VAL D N     1 
ATOM   14013 C  CA    . VAL D 2 102 ? 127.075 95.492  140.134 1.00 25.50 ?  81  VAL D CA    1 
ATOM   14014 C  C     . VAL D 2 102 ? 125.664 95.480  139.524 1.00 26.14 ?  81  VAL D C     1 
ATOM   14015 O  O     . VAL D 2 102 ? 125.502 95.125  138.359 1.00 26.96 ?  81  VAL D O     1 
ATOM   14016 C  CB    . VAL D 2 102 ? 127.867 96.740  139.644 1.00 25.30 ?  81  VAL D CB    1 
ATOM   14017 C  CG1   . VAL D 2 102 ? 127.026 97.991  139.733 1.00 27.08 ?  81  VAL D CG1   1 
ATOM   14018 C  CG2   . VAL D 2 102 ? 129.131 96.920  140.469 1.00 25.41 ?  81  VAL D CG2   1 
ATOM   14019 N  N     . ASP D 2 103 ? 124.661 95.848  140.316 1.00 26.45 ?  82  ASP D N     1 
ATOM   14020 C  CA    . ASP D 2 103 ? 123.289 95.981  139.822 1.00 27.15 ?  82  ASP D CA    1 
ATOM   14021 C  C     . ASP D 2 103 ? 123.036 97.395  139.318 1.00 26.39 ?  82  ASP D C     1 
ATOM   14022 O  O     . ASP D 2 103 ? 123.506 98.374  139.913 1.00 26.40 ?  82  ASP D O     1 
ATOM   14023 C  CB    . ASP D 2 103 ? 122.268 95.642  140.913 1.00 27.72 ?  82  ASP D CB    1 
ATOM   14024 C  CG    . ASP D 2 103 ? 122.362 94.198  141.394 1.00 31.46 ?  82  ASP D CG    1 
ATOM   14025 O  OD1   . ASP D 2 103 ? 122.715 93.289  140.594 1.00 34.26 ?  82  ASP D OD1   1 
ATOM   14026 O  OD2   . ASP D 2 103 ? 122.070 93.966  142.589 1.00 35.52 -1 82  ASP D OD2   1 
ATOM   14027 N  N     . GLY D 2 104 ? 122.276 97.495  138.232 1.00 25.52 ?  83  GLY D N     1 
ATOM   14028 C  CA    . GLY D 2 104 ? 121.913 98.790  137.659 1.00 24.31 ?  83  GLY D CA    1 
ATOM   14029 C  C     . GLY D 2 104 ? 122.354 98.840  136.201 1.00 23.27 ?  83  GLY D C     1 
ATOM   14030 O  O     . GLY D 2 104 ? 123.526 98.632  135.892 1.00 22.38 ?  83  GLY D O     1 
ATOM   14031 N  N     . HIS D 2 105 ? 121.409 99.098  135.302 1.00 22.46 ?  84  HIS D N     1 
ATOM   14032 C  CA    . HIS D 2 105 ? 121.720 99.157  133.872 1.00 22.17 ?  84  HIS D CA    1 
ATOM   14033 C  C     . HIS D 2 105 ? 122.710 100.253 133.514 1.00 21.13 ?  84  HIS D C     1 
ATOM   14034 O  O     . HIS D 2 105 ? 123.583 100.046 132.674 1.00 20.91 ?  84  HIS D O     1 
ATOM   14035 C  CB    . HIS D 2 105 ? 120.436 99.311  133.044 1.00 22.07 ?  84  HIS D CB    1 
ATOM   14036 C  CG    . HIS D 2 105 ? 119.470 98.189  133.249 1.00 23.85 ?  84  HIS D CG    1 
ATOM   14037 N  ND1   . HIS D 2 105 ? 119.840 96.866  133.129 1.00 24.86 ?  84  HIS D ND1   1 
ATOM   14038 C  CD2   . HIS D 2 105 ? 118.164 98.186  133.603 1.00 25.19 ?  84  HIS D CD2   1 
ATOM   14039 C  CE1   . HIS D 2 105 ? 118.795 96.097  133.378 1.00 24.94 ?  84  HIS D CE1   1 
ATOM   14040 N  NE2   . HIS D 2 105 ? 117.769 96.873  133.674 1.00 26.41 ?  84  HIS D NE2   1 
ATOM   14041 N  N     . GLN D 2 106 ? 122.574 101.411 134.143 1.00 20.66 ?  85  GLN D N     1 
ATOM   14042 C  CA    . GLN D 2 106 ? 123.404 102.553 133.770 1.00 20.70 ?  85  GLN D CA    1 
ATOM   14043 C  C     . GLN D 2 106 ? 124.832 102.353 134.274 1.00 20.46 ?  85  GLN D C     1 
ATOM   14044 O  O     . GLN D 2 106 ? 125.788 102.683 133.573 1.00 20.72 ?  85  GLN D O     1 
ATOM   14045 C  CB    . GLN D 2 106 ? 122.770 103.879 134.222 1.00 20.60 ?  85  GLN D CB    1 
ATOM   14046 C  CG    . GLN D 2 106 ? 121.386 104.138 133.566 1.00 20.74 ?  85  GLN D CG    1 
ATOM   14047 C  CD    . GLN D 2 106 ? 120.631 105.345 134.137 1.00 22.11 ?  85  GLN D CD    1 
ATOM   14048 O  OE1   . GLN D 2 106 ? 121.232 106.303 134.612 1.00 22.88 ?  85  GLN D OE1   1 
ATOM   14049 N  NE2   . GLN D 2 106 ? 119.303 105.299 134.074 1.00 21.64 ?  85  GLN D NE2   1 
ATOM   14050 N  N     . ARG D 2 107 ? 124.968 101.763 135.464 1.00 20.17 ?  86  ARG D N     1 
ATOM   14051 C  CA    . ARG D 2 107 ? 126.284 101.438 136.019 1.00 20.29 ?  86  ARG D CA    1 
ATOM   14052 C  C     . ARG D 2 107 ? 126.985 100.393 135.166 1.00 20.07 ?  86  ARG D C     1 
ATOM   14053 O  O     . ARG D 2 107 ? 128.176 100.506 134.908 1.00 19.53 ?  86  ARG D O     1 
ATOM   14054 C  CB    . ARG D 2 107 ? 126.163 100.914 137.447 1.00 20.88 ?  86  ARG D CB    1 
ATOM   14055 C  CG    . ARG D 2 107 ? 125.505 101.886 138.372 1.00 22.56 ?  86  ARG D CG    1 
ATOM   14056 C  CD    . ARG D 2 107 ? 125.112 101.213 139.662 1.00 27.21 ?  86  ARG D CD    1 
ATOM   14057 N  NE    . ARG D 2 107 ? 124.977 102.263 140.654 1.00 31.70 ?  86  ARG D NE    1 
ATOM   14058 C  CZ    . ARG D 2 107 ? 125.029 102.088 141.958 1.00 32.23 ?  86  ARG D CZ    1 
ATOM   14059 N  NH1   . ARG D 2 107 ? 125.204 100.873 142.475 1.00 34.27 1  86  ARG D NH1   1 
ATOM   14060 N  NH2   . ARG D 2 107 ? 124.909 103.149 142.736 1.00 33.79 ?  86  ARG D NH2   1 
ATOM   14061 N  N     . LYS D 2 108 ? 126.244 99.367  134.744 1.00 19.61 ?  87  LYS D N     1 
ATOM   14062 C  CA    . LYS D 2 108 ? 126.818 98.346  133.870 1.00 19.92 ?  87  LYS D CA    1 
ATOM   14063 C  C     . LYS D 2 108 ? 127.321 98.945  132.553 1.00 20.08 ?  87  LYS D C     1 
ATOM   14064 O  O     . LYS D 2 108 ? 128.331 98.490  132.005 1.00 20.38 ?  87  LYS D O     1 
ATOM   14065 C  CB    . LYS D 2 108 ? 125.834 97.203  133.605 1.00 19.54 ?  87  LYS D CB    1 
ATOM   14066 C  CG    . LYS D 2 108 ? 125.508 96.365  134.826 1.00 20.55 ?  87  LYS D CG    1 
ATOM   14067 C  CD    . LYS D 2 108 ? 124.544 95.228  134.481 1.00 21.09 ?  87  LYS D CD    1 
ATOM   14068 C  CE    . LYS D 2 108 ? 124.238 94.348  135.688 1.00 22.98 ?  87  LYS D CE    1 
ATOM   14069 N  NZ    . LYS D 2 108 ? 125.431 93.494  136.054 1.00 22.30 1  87  LYS D NZ    1 
ATOM   14070 N  N     . ALA D 2 109 ? 126.616 99.955  132.044 1.00 19.72 ?  88  ALA D N     1 
ATOM   14071 C  CA    . ALA D 2 109 ? 127.014 100.599 130.798 1.00 19.83 ?  88  ALA D CA    1 
ATOM   14072 C  C     . ALA D 2 109 ? 128.312 101.388 130.968 1.00 19.84 ?  88  ALA D C     1 
ATOM   14073 O  O     . ALA D 2 109 ? 129.224 101.283 130.140 1.00 19.96 ?  88  ALA D O     1 
ATOM   14074 C  CB    . ALA D 2 109 ? 125.884 101.490 130.255 1.00 19.65 ?  88  ALA D CB    1 
ATOM   14075 N  N     . VAL D 2 110 ? 128.406 102.156 132.051 1.00 19.33 ?  89  VAL D N     1 
ATOM   14076 C  CA    . VAL D 2 110 ? 129.624 102.927 132.342 1.00 19.22 ?  89  VAL D CA    1 
ATOM   14077 C  C     . VAL D 2 110 ? 130.802 101.954 132.532 1.00 19.45 ?  89  VAL D C     1 
ATOM   14078 O  O     . VAL D 2 110 ? 131.848 102.086 131.883 1.00 18.97 ?  89  VAL D O     1 
ATOM   14079 C  CB    . VAL D 2 110 ? 129.410 103.884 133.550 1.00 19.01 ?  89  VAL D CB    1 
ATOM   14080 C  CG1   . VAL D 2 110 ? 130.737 104.564 133.996 1.00 19.90 ?  89  VAL D CG1   1 
ATOM   14081 C  CG2   . VAL D 2 110 ? 128.397 104.943 133.180 1.00 19.69 ?  89  VAL D CG2   1 
ATOM   14082 N  N     . LEU D 2 111 ? 130.596 100.933 133.367 1.00 19.27 ?  90  LEU D N     1 
ATOM   14083 C  CA    . LEU D 2 111 ? 131.627 99.914  133.573 1.00 19.96 ?  90  LEU D CA    1 
ATOM   14084 C  C     . LEU D 2 111 ? 132.062 99.213  132.279 1.00 20.30 ?  90  LEU D C     1 
ATOM   14085 O  O     . LEU D 2 111 ? 133.257 98.989  132.071 1.00 19.88 ?  90  LEU D O     1 
ATOM   14086 C  CB    . LEU D 2 111 ? 131.214 98.913  134.661 1.00 19.87 ?  90  LEU D CB    1 
ATOM   14087 C  CG    . LEU D 2 111 ? 131.135 99.538  136.056 1.00 20.24 ?  90  LEU D CG    1 
ATOM   14088 C  CD1   . LEU D 2 111 ? 130.395 98.650  137.069 1.00 21.85 ?  90  LEU D CD1   1 
ATOM   14089 C  CD2   . LEU D 2 111 ? 132.535 99.926  136.569 1.00 20.29 ?  90  LEU D CD2   1 
ATOM   14090 N  N     . ASN D 2 112 ? 131.102 98.893  131.407 1.00 20.92 ?  91  ASN D N     1 
ATOM   14091 C  CA    . ASN D 2 112 ? 131.423 98.362  130.061 1.00 20.70 ?  91  ASN D CA    1 
ATOM   14092 C  C     . ASN D 2 112 ? 132.283 99.304  129.238 1.00 20.57 ?  91  ASN D C     1 
ATOM   14093 O  O     . ASN D 2 112 ? 133.164 98.864  128.482 1.00 20.45 ?  91  ASN D O     1 
ATOM   14094 C  CB    . ASN D 2 112 ? 130.155 98.105  129.246 1.00 21.16 ?  91  ASN D CB    1 
ATOM   14095 C  CG    . ASN D 2 112 ? 129.679 96.668  129.321 1.00 21.98 ?  91  ASN D CG    1 
ATOM   14096 O  OD1   . ASN D 2 112 ? 130.228 95.842  130.057 1.00 25.37 ?  91  ASN D OD1   1 
ATOM   14097 N  ND2   . ASN D 2 112 ? 128.634 96.369  128.572 1.00 21.12 ?  91  ASN D ND2   1 
ATOM   14098 N  N     . PHE D 2 113 ? 131.966 100.594 129.317 1.00 19.70 ?  92  PHE D N     1 
ATOM   14099 C  CA    . PHE D 2 113 ? 132.741 101.591 128.610 1.00 20.02 ?  92  PHE D CA    1 
ATOM   14100 C  C     . PHE D 2 113 ? 134.190 101.621 129.122 1.00 19.97 ?  92  PHE D C     1 
ATOM   14101 O  O     . PHE D 2 113 ? 135.137 101.657 128.329 1.00 19.22 ?  92  PHE D O     1 
ATOM   14102 C  CB    . PHE D 2 113 ? 132.098 102.986 128.685 1.00 20.09 ?  92  PHE D CB    1 
ATOM   14103 C  CG    . PHE D 2 113 ? 132.785 103.985 127.821 1.00 20.54 ?  92  PHE D CG    1 
ATOM   14104 C  CD1   . PHE D 2 113 ? 132.395 104.159 126.492 1.00 20.14 ?  92  PHE D CD1   1 
ATOM   14105 C  CD2   . PHE D 2 113 ? 133.871 104.712 128.313 1.00 20.77 ?  92  PHE D CD2   1 
ATOM   14106 C  CE1   . PHE D 2 113 ? 133.062 105.067 125.673 1.00 20.54 ?  92  PHE D CE1   1 
ATOM   14107 C  CE2   . PHE D 2 113 ? 134.547 105.617 127.497 1.00 21.23 ?  92  PHE D CE2   1 
ATOM   14108 C  CZ    . PHE D 2 113 ? 134.137 105.788 126.169 1.00 20.92 ?  92  PHE D CZ    1 
ATOM   14109 N  N     . MET D 2 114 ? 134.349 101.592 130.442 1.00 19.67 ?  93  MET D N     1 
ATOM   14110 C  CA    . MET D 2 114 ? 135.677 101.548 131.041 1.00 20.55 ?  93  MET D CA    1 
ATOM   14111 C  C     . MET D 2 114 ? 136.453 100.291 130.642 1.00 20.82 ?  93  MET D C     1 
ATOM   14112 O  O     . MET D 2 114 ? 137.632 100.396 130.332 1.00 20.43 ?  93  MET D O     1 
ATOM   14113 C  CB    . MET D 2 114 ? 135.596 101.674 132.558 1.00 20.24 ?  93  MET D CB    1 
ATOM   14114 C  CG    . MET D 2 114 ? 134.894 102.952 132.969 1.00 22.05 ?  93  MET D CG    1 
ATOM   14115 S  SD    . MET D 2 114 ? 134.580 103.093 134.713 1.00 25.85 ?  93  MET D SD    1 
ATOM   14116 C  CE    . MET D 2 114 ? 134.455 104.884 134.847 1.00 27.57 ?  93  MET D CE    1 
ATOM   14117 N  N     . ALA D 2 115 ? 135.790 99.125  130.648 1.00 21.19 ?  94  ALA D N     1 
ATOM   14118 C  CA    . ALA D 2 115 ? 136.426 97.869  130.203 1.00 21.53 ?  94  ALA D CA    1 
ATOM   14119 C  C     . ALA D 2 115 ? 136.872 97.974  128.746 1.00 21.75 ?  94  ALA D C     1 
ATOM   14120 O  O     . ALA D 2 115 ? 137.982 97.560  128.408 1.00 22.18 ?  94  ALA D O     1 
ATOM   14121 C  CB    . ALA D 2 115 ? 135.495 96.668  130.402 1.00 21.32 ?  94  ALA D CB    1 
ATOM   14122 N  N     . MET D 2 116 ? 136.020 98.554  127.897 1.00 21.47 ?  95  MET D N     1 
ATOM   14123 C  CA    . MET D 2 116 ? 136.367 98.806  126.501 1.00 21.83 ?  95  MET D CA    1 
ATOM   14124 C  C     . MET D 2 116 ? 137.660 99.635  126.373 1.00 22.15 ?  95  MET D C     1 
ATOM   14125 O  O     . MET D 2 116 ? 138.540 99.290  125.588 1.00 22.09 ?  95  MET D O     1 
ATOM   14126 C  CB    . MET D 2 116 ? 135.201 99.490  125.769 1.00 21.72 ?  95  MET D CB    1 
ATOM   14127 C  CG    . MET D 2 116 ? 135.493 99.896  124.315 1.00 22.57 ?  95  MET D CG    1 
ATOM   14128 S  SD    . MET D 2 116 ? 136.453 101.422 124.137 1.00 22.75 ?  95  MET D SD    1 
ATOM   14129 C  CE    . MET D 2 116 ? 135.301 102.650 124.750 1.00 22.96 ?  95  MET D CE    1 
ATOM   14130 N  N     . MET D 2 117 ? 137.764 100.718 127.146 1.00 22.04 ?  96  MET D N     1 
ATOM   14131 C  CA    . MET D 2 117 ? 138.954 101.585 127.109 1.00 22.45 ?  96  MET D CA    1 
ATOM   14132 C  C     . MET D 2 117 ? 140.233 100.812 127.474 1.00 22.39 ?  96  MET D C     1 
ATOM   14133 O  O     . MET D 2 117 ? 141.279 101.005 126.853 1.00 21.88 ?  96  MET D O     1 
ATOM   14134 C  CB    . MET D 2 117 ? 138.776 102.819 128.017 1.00 22.00 ?  96  MET D CB    1 
ATOM   14135 C  CG    . MET D 2 117 ? 137.767 103.860 127.465 1.00 23.25 ?  96  MET D CG    1 
ATOM   14136 S  SD    . MET D 2 117 ? 138.200 104.502 125.830 1.00 24.28 ?  96  MET D SD    1 
ATOM   14137 C  CE    . MET D 2 117 ? 139.589 105.562 126.215 1.00 24.59 ?  96  MET D CE    1 
ATOM   14138 N  N     . GLU D 2 118 ? 140.137 99.923  128.463 1.00 22.66 ?  97  GLU D N     1 
ATOM   14139 C  CA    . GLU D 2 118 ? 141.281 99.089  128.852 1.00 23.52 ?  97  GLU D CA    1 
ATOM   14140 C  C     . GLU D 2 118 ? 141.748 98.211  127.704 1.00 24.25 ?  97  GLU D C     1 
ATOM   14141 O  O     . GLU D 2 118 ? 142.937 98.204  127.377 1.00 25.05 ?  97  GLU D O     1 
ATOM   14142 C  CB    . GLU D 2 118 ? 140.975 98.202  130.082 1.00 23.11 ?  97  GLU D CB    1 
ATOM   14143 C  CG    . GLU D 2 118 ? 140.244 98.881  131.247 1.00 23.08 ?  97  GLU D CG    1 
ATOM   14144 C  CD    . GLU D 2 118 ? 141.072 99.913  131.995 1.00 24.08 ?  97  GLU D CD    1 
ATOM   14145 O  OE1   . GLU D 2 118 ? 142.105 100.355 131.469 1.00 26.39 ?  97  GLU D OE1   1 
ATOM   14146 O  OE2   . GLU D 2 118 ? 140.671 100.309 133.109 1.00 27.52 -1 97  GLU D OE2   1 
ATOM   14147 N  N     . ASN D 2 119 ? 140.808 97.497  127.089 1.00 25.47 ?  98  ASN D N     1 
ATOM   14148 C  CA    . ASN D 2 119 ? 141.108 96.449  126.093 1.00 26.32 ?  98  ASN D CA    1 
ATOM   14149 C  C     . ASN D 2 119 ? 141.327 96.950  124.668 1.00 26.22 ?  98  ASN D C     1 
ATOM   14150 O  O     . ASN D 2 119 ? 142.186 96.422  123.932 1.00 26.54 ?  98  ASN D O     1 
ATOM   14151 C  CB    . ASN D 2 119 ? 139.996 95.384  126.086 1.00 26.72 ?  98  ASN D CB    1 
ATOM   14152 C  CG    . ASN D 2 119 ? 139.928 94.604  127.399 1.00 29.12 ?  98  ASN D CG    1 
ATOM   14153 O  OD1   . ASN D 2 119 ? 140.929 94.044  127.859 1.00 32.07 ?  98  ASN D OD1   1 
ATOM   14154 N  ND2   . ASN D 2 119 ? 138.754 94.594  128.021 1.00 29.12 ?  98  ASN D ND2   1 
ATOM   14155 N  N     . ALA D 2 120 ? 140.536 97.944  124.279 1.00 25.46 ?  99  ALA D N     1 
ATOM   14156 C  CA    . ALA D 2 120 ? 140.540 98.446  122.906 1.00 25.77 ?  99  ALA D CA    1 
ATOM   14157 C  C     . ALA D 2 120 ? 141.453 99.652  122.704 1.00 25.51 ?  99  ALA D C     1 
ATOM   14158 O  O     . ALA D 2 120 ? 141.947 99.871  121.596 1.00 26.64 ?  99  ALA D O     1 
ATOM   14159 C  CB    . ALA D 2 120 ? 139.111 98.780  122.448 1.00 25.75 ?  99  ALA D CB    1 
ATOM   14160 N  N     . VAL D 2 121 ? 141.669 100.434 123.757 1.00 24.40 ?  100 VAL D N     1 
ATOM   14161 C  CA    . VAL D 2 121 ? 142.401 101.687 123.609 1.00 24.15 ?  100 VAL D CA    1 
ATOM   14162 C  C     . VAL D 2 121 ? 143.748 101.647 124.334 1.00 23.94 ?  100 VAL D C     1 
ATOM   14163 O  O     . VAL D 2 121 ? 144.801 101.796 123.706 1.00 23.75 ?  100 VAL D O     1 
ATOM   14164 C  CB    . VAL D 2 121 ? 141.544 102.912 124.052 1.00 23.68 ?  100 VAL D CB    1 
ATOM   14165 C  CG1   . VAL D 2 121 ? 142.317 104.215 123.850 1.00 23.76 ?  100 VAL D CG1   1 
ATOM   14166 C  CG2   . VAL D 2 121 ? 140.235 102.953 123.258 1.00 23.99 ?  100 VAL D CG2   1 
ATOM   14167 N  N     . HIS D 2 122 ? 143.709 101.440 125.649 1.00 23.68 ?  101 HIS D N     1 
ATOM   14168 C  CA    . HIS D 2 122 ? 144.928 101.402 126.458 1.00 24.02 ?  101 HIS D CA    1 
ATOM   14169 C  C     . HIS D 2 122 ? 145.890 100.306 126.030 1.00 24.39 ?  101 HIS D C     1 
ATOM   14170 O  O     . HIS D 2 122 ? 147.081 100.567 125.875 1.00 24.71 ?  101 HIS D O     1 
ATOM   14171 C  CB    . HIS D 2 122 ? 144.619 101.280 127.956 1.00 23.20 ?  101 HIS D CB    1 
ATOM   14172 C  CG    . HIS D 2 122 ? 143.880 102.454 128.520 1.00 22.82 ?  101 HIS D CG    1 
ATOM   14173 N  ND1   . HIS D 2 122 ? 143.458 102.503 129.830 1.00 20.48 ?  101 HIS D ND1   1 
ATOM   14174 C  CD2   . HIS D 2 122 ? 143.465 103.609 127.946 1.00 21.03 ?  101 HIS D CD2   1 
ATOM   14175 C  CE1   . HIS D 2 122 ? 142.829 103.644 130.044 1.00 19.88 ?  101 HIS D CE1   1 
ATOM   14176 N  NE2   . HIS D 2 122 ? 142.821 104.335 128.918 1.00 21.62 ?  101 HIS D NE2   1 
ATOM   14177 N  N     . ALA D 2 123 ? 145.383 99.090  125.830 1.00 25.30 ?  102 ALA D N     1 
ATOM   14178 C  CA    . ALA D 2 123 ? 146.257 97.956  125.492 1.00 25.77 ?  102 ALA D CA    1 
ATOM   14179 C  C     . ALA D 2 123 ? 146.961 98.146  124.145 1.00 26.37 ?  102 ALA D C     1 
ATOM   14180 O  O     . ALA D 2 123 ? 148.143 97.813  123.996 1.00 25.87 ?  102 ALA D O     1 
ATOM   14181 C  CB    . ALA D 2 123 ? 145.477 96.635  125.519 1.00 26.43 ?  102 ALA D CB    1 
ATOM   14182 N  N     . LYS D 2 124 ? 146.227 98.685  123.170 1.00 26.51 ?  103 LYS D N     1 
ATOM   14183 C  CA    . LYS D 2 124 ? 146.785 98.974  121.857 1.00 27.22 ?  103 LYS D CA    1 
ATOM   14184 C  C     . LYS D 2 124 ? 147.819 100.106 121.947 1.00 26.63 ?  103 LYS D C     1 
ATOM   14185 O  O     . LYS D 2 124 ? 148.831 100.076 121.246 1.00 26.07 ?  103 LYS D O     1 
ATOM   14186 C  CB    . LYS D 2 124 ? 145.666 99.321  120.854 1.00 27.51 ?  103 LYS D CB    1 
ATOM   14187 C  CG    . LYS D 2 124 ? 146.139 99.734  119.444 1.00 30.58 ?  103 LYS D CG    1 
ATOM   14188 C  CD    . LYS D 2 124 ? 146.786 98.581  118.691 1.00 35.72 ?  103 LYS D CD    1 
ATOM   14189 C  CE    . LYS D 2 124 ? 147.284 99.001  117.305 1.00 37.33 ?  103 LYS D CE    1 
ATOM   14190 N  NZ    . LYS D 2 124 ? 146.142 99.365  116.426 1.00 40.73 1  103 LYS D NZ    1 
ATOM   14191 N  N     . SER D 2 125 ? 147.561 101.078 122.825 1.00 26.02 ?  104 SER D N     1 
ATOM   14192 C  CA    . SER D 2 125 ? 148.449 102.227 123.023 1.00 26.16 ?  104 SER D CA    1 
ATOM   14193 C  C     . SER D 2 125 ? 149.803 101.819 123.604 1.00 26.18 ?  104 SER D C     1 
ATOM   14194 O  O     . SER D 2 125 ? 150.846 102.302 123.148 1.00 26.06 ?  104 SER D O     1 
ATOM   14195 C  CB    . SER D 2 125 ? 147.795 103.283 123.917 1.00 26.10 ?  104 SER D CB    1 
ATOM   14196 O  OG    . SER D 2 125 ? 146.663 103.837 123.272 1.00 26.58 ?  104 SER D OG    1 
ATOM   14197 N  N     . TYR D 2 126 ? 149.778 100.937 124.600 1.00 25.68 ?  105 TYR D N     1 
ATOM   14198 C  CA    . TYR D 2 126 ? 151.008 100.412 125.206 1.00 26.12 ?  105 TYR D CA    1 
ATOM   14199 C  C     . TYR D 2 126 ? 151.813 99.604  124.183 1.00 26.38 ?  105 TYR D C     1 
ATOM   14200 O  O     . TYR D 2 126 ? 153.033 99.750  124.082 1.00 26.83 ?  105 TYR D O     1 
ATOM   14201 C  CB    . TYR D 2 126 ? 150.700 99.537  126.436 1.00 25.35 ?  105 TYR D CB    1 
ATOM   14202 C  CG    . TYR D 2 126 ? 150.374 100.300 127.706 1.00 25.46 ?  105 TYR D CG    1 
ATOM   14203 C  CD1   . TYR D 2 126 ? 151.259 101.252 128.215 1.00 25.41 ?  105 TYR D CD1   1 
ATOM   14204 C  CD2   . TYR D 2 126 ? 149.194 100.048 128.422 1.00 24.77 ?  105 TYR D CD2   1 
ATOM   14205 C  CE1   . TYR D 2 126 ? 150.973 101.957 129.382 1.00 25.89 ?  105 TYR D CE1   1 
ATOM   14206 C  CE2   . TYR D 2 126 ? 148.897 100.754 129.599 1.00 23.11 ?  105 TYR D CE2   1 
ATOM   14207 C  CZ    . TYR D 2 126 ? 149.799 101.693 130.077 1.00 25.38 ?  105 TYR D CZ    1 
ATOM   14208 O  OH    . TYR D 2 126 ? 149.542 102.403 131.230 1.00 23.31 ?  105 TYR D OH    1 
ATOM   14209 N  N     . SER D 2 127 ? 151.119 98.772  123.414 1.00 27.16 ?  106 SER D N     1 
ATOM   14210 C  CA    . SER D 2 127 ? 151.752 97.976  122.358 1.00 27.83 ?  106 SER D CA    1 
ATOM   14211 C  C     . SER D 2 127 ? 152.438 98.878  121.321 1.00 28.21 ?  106 SER D C     1 
ATOM   14212 O  O     . SER D 2 127 ? 153.600 98.641  120.964 1.00 28.30 ?  106 SER D O     1 
ATOM   14213 C  CB    . SER D 2 127 ? 150.724 97.045  121.695 1.00 28.37 ?  106 SER D CB    1 
ATOM   14214 O  OG    . SER D 2 127 ? 151.290 96.341  120.591 1.00 29.33 ?  106 SER D OG    1 
ATOM   14215 N  N     . ASN D 2 128 ? 151.719 99.906  120.859 1.00 28.27 ?  107 ASN D N     1 
ATOM   14216 C  CA    . ASN D 2 128 ? 152.251 100.918 119.933 1.00 28.79 ?  107 ASN D CA    1 
ATOM   14217 C  C     . ASN D 2 128 ? 153.518 101.607 120.432 1.00 28.53 ?  107 ASN D C     1 
ATOM   14218 O  O     . ASN D 2 128 ? 154.472 101.776 119.665 1.00 28.03 ?  107 ASN D O     1 
ATOM   14219 C  CB    . ASN D 2 128 ? 151.196 101.987 119.595 1.00 29.05 ?  107 ASN D CB    1 
ATOM   14220 C  CG    . ASN D 2 128 ? 150.062 101.449 118.718 1.00 30.48 ?  107 ASN D CG    1 
ATOM   14221 O  OD1   . ASN D 2 128 ? 150.138 100.342 118.191 1.00 32.19 ?  107 ASN D OD1   1 
ATOM   14222 N  ND2   . ASN D 2 128 ? 148.998 102.233 118.580 1.00 31.59 ?  107 ASN D ND2   1 
ATOM   14223 N  N     . ILE D 2 129 ? 153.518 102.027 121.699 1.00 28.21 ?  108 ILE D N     1 
ATOM   14224 C  CA    . ILE D 2 129 ? 154.717 102.631 122.295 1.00 28.76 ?  108 ILE D CA    1 
ATOM   14225 C  C     . ILE D 2 129 ? 155.905 101.654 122.245 1.00 29.83 ?  108 ILE D C     1 
ATOM   14226 O  O     . ILE D 2 129 ? 157.006 102.021 121.814 1.00 29.99 ?  108 ILE D O     1 
ATOM   14227 C  CB    . ILE D 2 129 ? 154.476 103.147 123.749 1.00 28.28 ?  108 ILE D CB    1 
ATOM   14228 C  CG1   . ILE D 2 129 ? 153.432 104.273 123.765 1.00 27.94 ?  108 ILE D CG1   1 
ATOM   14229 C  CG2   . ILE D 2 129 ? 155.788 103.650 124.368 1.00 27.52 ?  108 ILE D CG2   1 
ATOM   14230 C  CD1   . ILE D 2 129 ? 152.868 104.584 125.146 1.00 27.98 ?  108 ILE D CD1   1 
ATOM   14231 N  N     . PHE D 2 130 ? 155.679 100.417 122.679 1.00 30.86 ?  109 PHE D N     1 
ATOM   14232 C  CA    . PHE D 2 130 ? 156.718 99.391  122.648 1.00 32.76 ?  109 PHE D CA    1 
ATOM   14233 C  C     . PHE D 2 130 ? 157.297 99.157  121.249 1.00 34.37 ?  109 PHE D C     1 
ATOM   14234 O  O     . PHE D 2 130 ? 158.511 99.212  121.066 1.00 34.61 ?  109 PHE D O     1 
ATOM   14235 C  CB    . PHE D 2 130 ? 156.201 98.073  123.218 1.00 32.81 ?  109 PHE D CB    1 
ATOM   14236 C  CG    . PHE D 2 130 ? 156.526 97.868  124.670 1.00 33.84 ?  109 PHE D CG    1 
ATOM   14237 C  CD1   . PHE D 2 130 ? 157.843 97.670  125.079 1.00 34.61 ?  109 PHE D CD1   1 
ATOM   14238 C  CD2   . PHE D 2 130 ? 155.515 97.840  125.621 1.00 35.74 ?  109 PHE D CD2   1 
ATOM   14239 C  CE1   . PHE D 2 130 ? 158.153 97.467  126.424 1.00 36.99 ?  109 PHE D CE1   1 
ATOM   14240 C  CE2   . PHE D 2 130 ? 155.809 97.637  126.976 1.00 36.96 ?  109 PHE D CE2   1 
ATOM   14241 C  CZ    . PHE D 2 130 ? 157.131 97.450  127.378 1.00 36.91 ?  109 PHE D CZ    1 
ATOM   14242 N  N     . MET D 2 131 ? 156.418 98.914  120.276 1.00 35.90 ?  110 MET D N     1 
ATOM   14243 C  CA    . MET D 2 131 ? 156.817 98.630  118.896 1.00 37.94 ?  110 MET D CA    1 
ATOM   14244 C  C     . MET D 2 131 ? 157.602 99.775  118.271 1.00 38.05 ?  110 MET D C     1 
ATOM   14245 O  O     . MET D 2 131 ? 158.427 99.548  117.394 1.00 38.20 ?  110 MET D O     1 
ATOM   14246 C  CB    . MET D 2 131 ? 155.598 98.292  118.021 1.00 38.63 ?  110 MET D CB    1 
ATOM   14247 C  CG    . MET D 2 131 ? 154.910 96.961  118.365 1.00 42.34 ?  110 MET D CG    1 
ATOM   14248 S  SD    . MET D 2 131 ? 153.472 96.559  117.319 1.00 50.15 ?  110 MET D SD    1 
ATOM   14249 C  CE    . MET D 2 131 ? 152.250 97.773  117.833 1.00 48.14 ?  110 MET D CE    1 
ATOM   14250 N  N     . THR D 2 132 ? 157.340 101.000 118.726 1.00 38.12 ?  111 THR D N     1 
ATOM   14251 C  CA    . THR D 2 132 ? 158.062 102.173 118.233 1.00 38.79 ?  111 THR D CA    1 
ATOM   14252 C  C     . THR D 2 132 ? 159.499 102.246 118.779 1.00 38.81 ?  111 THR D C     1 
ATOM   14253 O  O     . THR D 2 132 ? 160.431 102.556 118.029 1.00 39.26 ?  111 THR D O     1 
ATOM   14254 C  CB    . THR D 2 132 ? 157.296 103.474 118.550 1.00 38.78 ?  111 THR D CB    1 
ATOM   14255 O  OG1   . THR D 2 132 ? 155.982 103.402 117.985 1.00 39.32 ?  111 THR D OG1   1 
ATOM   14256 C  CG2   . THR D 2 132 ? 158.008 104.688 117.961 1.00 39.75 ?  111 THR D CG2   1 
ATOM   14257 N  N     . LEU D 2 133 ? 159.666 101.946 120.068 1.00 38.34 ?  112 LEU D N     1 
ATOM   14258 C  CA    . LEU D 2 133 ? 160.935 102.146 120.773 1.00 38.36 ?  112 LEU D CA    1 
ATOM   14259 C  C     . LEU D 2 133 ? 161.885 100.947 120.761 1.00 38.94 ?  112 LEU D C     1 
ATOM   14260 O  O     . LEU D 2 133 ? 163.102 101.123 120.787 1.00 39.14 ?  112 LEU D O     1 
ATOM   14261 C  CB    . LEU D 2 133 ? 160.681 102.568 122.230 1.00 37.62 ?  112 LEU D CB    1 
ATOM   14262 C  CG    . LEU D 2 133 ? 159.801 103.793 122.493 1.00 36.50 ?  112 LEU D CG    1 
ATOM   14263 C  CD1   . LEU D 2 133 ? 159.467 103.900 123.984 1.00 35.80 ?  112 LEU D CD1   1 
ATOM   14264 C  CD2   . LEU D 2 133 ? 160.434 105.076 121.983 1.00 35.32 ?  112 LEU D CD2   1 
ATOM   14265 N  N     . ALA D 2 134 ? 161.347 99.734  120.735 1.00 39.41 ?  113 ALA D N     1 
ATOM   14266 C  CA    . ALA D 2 134 ? 162.209 98.547  120.790 1.00 40.33 ?  113 ALA D CA    1 
ATOM   14267 C  C     . ALA D 2 134 ? 161.958 97.583  119.635 1.00 41.05 ?  113 ALA D C     1 
ATOM   14268 O  O     . ALA D 2 134 ? 160.842 97.512  119.134 1.00 40.81 ?  113 ALA D O     1 
ATOM   14269 C  CB    . ALA D 2 134 ? 162.039 97.839  122.121 1.00 40.15 ?  113 ALA D CB    1 
ATOM   14270 N  N     . PRO D 2 135 ? 163.001 96.844  119.200 1.00 42.21 ?  114 PRO D N     1 
ATOM   14271 C  CA    . PRO D 2 135 ? 162.758 95.774  118.225 1.00 43.27 ?  114 PRO D CA    1 
ATOM   14272 C  C     . PRO D 2 135 ? 162.041 94.582  118.878 1.00 43.89 ?  114 PRO D C     1 
ATOM   14273 O  O     . PRO D 2 135 ? 162.078 94.436  120.102 1.00 43.31 ?  114 PRO D O     1 
ATOM   14274 C  CB    . PRO D 2 135 ? 164.165 95.377  117.773 1.00 43.69 ?  114 PRO D CB    1 
ATOM   14275 C  CG    . PRO D 2 135 ? 165.039 95.734  118.915 1.00 43.01 ?  114 PRO D CG    1 
ATOM   14276 C  CD    . PRO D 2 135 ? 164.430 96.952  119.553 1.00 42.16 ?  114 PRO D CD    1 
ATOM   14277 N  N     . THR D 2 136 ? 161.412 93.743  118.055 1.00 45.26 ?  115 THR D N     1 
ATOM   14278 C  CA    . THR D 2 136 ? 160.576 92.629  118.530 1.00 46.11 ?  115 THR D CA    1 
ATOM   14279 C  C     . THR D 2 136 ? 161.259 91.763  119.593 1.00 46.35 ?  115 THR D C     1 
ATOM   14280 O  O     . THR D 2 136 ? 160.650 91.451  120.622 1.00 46.25 ?  115 THR D O     1 
ATOM   14281 C  CB    . THR D 2 136 ? 160.063 91.750  117.356 1.00 46.59 ?  115 THR D CB    1 
ATOM   14282 O  OG1   . THR D 2 136 ? 159.412 92.582  116.391 1.00 47.80 ?  115 THR D OG1   1 
ATOM   14283 C  CG2   . THR D 2 136 ? 159.056 90.706  117.836 1.00 46.94 ?  115 THR D CG2   1 
ATOM   14284 N  N     . GLU D 2 137 ? 162.520 91.401  119.357 1.00 46.92 ?  116 GLU D N     1 
ATOM   14285 C  CA    . GLU D 2 137 ? 163.261 90.547  120.284 1.00 47.37 ?  116 GLU D CA    1 
ATOM   14286 C  C     . GLU D 2 137 ? 163.454 91.184  121.663 1.00 46.64 ?  116 GLU D C     1 
ATOM   14287 O  O     . GLU D 2 137 ? 163.372 90.490  122.678 1.00 46.89 ?  116 GLU D O     1 
ATOM   14288 C  CB    . GLU D 2 137 ? 164.610 90.114  119.688 1.00 48.04 ?  116 GLU D CB    1 
ATOM   14289 C  CG    . GLU D 2 137 ? 165.402 89.109  120.546 1.00 49.86 ?  116 GLU D CG    1 
ATOM   14290 C  CD    . GLU D 2 137 ? 164.791 87.700  120.588 1.00 52.40 ?  116 GLU D CD    1 
ATOM   14291 O  OE1   . GLU D 2 137 ? 163.593 87.556  120.920 1.00 52.97 ?  116 GLU D OE1   1 
ATOM   14292 O  OE2   . GLU D 2 137 ? 165.527 86.724  120.312 1.00 54.12 -1 116 GLU D OE2   1 
ATOM   14293 N  N     . THR D 2 138 ? 163.704 92.492  121.689 1.00 46.09 ?  117 THR D N     1 
ATOM   14294 C  CA    . THR D 2 138 ? 163.853 93.244  122.944 1.00 45.30 ?  117 THR D CA    1 
ATOM   14295 C  C     . THR D 2 138 ? 162.540 93.307  123.736 1.00 44.63 ?  117 THR D C     1 
ATOM   14296 O  O     . THR D 2 138 ? 162.543 93.182  124.964 1.00 44.51 ?  117 THR D O     1 
ATOM   14297 C  CB    . THR D 2 138 ? 164.385 94.675  122.688 1.00 45.20 ?  117 THR D CB    1 
ATOM   14298 O  OG1   . THR D 2 138 ? 165.626 94.602  121.978 1.00 45.69 ?  117 THR D OG1   1 
ATOM   14299 C  CG2   . THR D 2 138 ? 164.610 95.431  123.996 1.00 44.67 ?  117 THR D CG2   1 
ATOM   14300 N  N     . ILE D 2 139 ? 161.424 93.493  123.030 1.00 44.24 ?  118 ILE D N     1 
ATOM   14301 C  CA    . ILE D 2 139 ? 160.103 93.511  123.662 1.00 43.65 ?  118 ILE D CA    1 
ATOM   14302 C  C     . ILE D 2 139 ? 159.811 92.167  124.346 1.00 43.87 ?  118 ILE D C     1 
ATOM   14303 O  O     . ILE D 2 139 ? 159.424 92.131  125.518 1.00 43.36 ?  118 ILE D O     1 
ATOM   14304 C  CB    . ILE D 2 139 ? 158.992 93.899  122.652 1.00 43.68 ?  118 ILE D CB    1 
ATOM   14305 C  CG1   . ILE D 2 139 ? 159.167 95.361  122.212 1.00 43.30 ?  118 ILE D CG1   1 
ATOM   14306 C  CG2   . ILE D 2 139 ? 157.591 93.676  123.251 1.00 43.11 ?  118 ILE D CG2   1 
ATOM   14307 C  CD1   . ILE D 2 139 ? 158.408 95.750  120.950 1.00 43.41 ?  118 ILE D CD1   1 
ATOM   14308 N  N     . ASN D 2 140 ? 160.028 91.072  123.619 1.00 44.52 ?  119 ASN D N     1 
ATOM   14309 C  CA    . ASN D 2 140 ? 159.823 89.723  124.157 1.00 45.00 ?  119 ASN D CA    1 
ATOM   14310 C  C     . ASN D 2 140 ? 160.659 89.441  125.423 1.00 44.99 ?  119 ASN D C     1 
ATOM   14311 O  O     . ASN D 2 140 ? 160.163 88.831  126.378 1.00 44.61 ?  119 ASN D O     1 
ATOM   14312 C  CB    . ASN D 2 140 ? 160.076 88.658  123.075 1.00 45.74 ?  119 ASN D CB    1 
ATOM   14313 C  CG    . ASN D 2 140 ? 159.127 88.784  121.877 1.00 46.40 ?  119 ASN D CG    1 
ATOM   14314 O  OD1   . ASN D 2 140 ? 158.099 89.467  121.937 1.00 46.85 ?  119 ASN D OD1   1 
ATOM   14315 N  ND2   . ASN D 2 140 ? 159.473 88.110  120.782 1.00 48.16 ?  119 ASN D ND2   1 
ATOM   14316 N  N     . GLU D 2 141 ? 161.909 89.910  125.434 1.00 45.09 ?  120 GLU D N     1 
ATOM   14317 C  CA    . GLU D 2 141 ? 162.803 89.718  126.581 1.00 45.27 ?  120 GLU D CA    1 
ATOM   14318 C  C     . GLU D 2 141 ? 162.400 90.534  127.818 1.00 44.75 ?  120 GLU D C     1 
ATOM   14319 O  O     . GLU D 2 141 ? 162.444 90.026  128.944 1.00 44.37 ?  120 GLU D O     1 
ATOM   14320 C  CB    . GLU D 2 141 ? 164.253 90.018  126.200 1.00 45.75 ?  120 GLU D CB    1 
ATOM   14321 C  CG    . GLU D 2 141 ? 164.864 89.006  125.230 1.00 48.17 ?  120 GLU D CG    1 
ATOM   14322 C  CD    . GLU D 2 141 ? 166.319 89.287  124.914 1.00 50.15 ?  120 GLU D CD    1 
ATOM   14323 O  OE1   . GLU D 2 141 ? 167.117 89.481  125.855 1.00 50.90 ?  120 GLU D OE1   1 
ATOM   14324 O  OE2   . GLU D 2 141 ? 166.669 89.308  123.715 1.00 52.25 -1 120 GLU D OE2   1 
ATOM   14325 N  N     . VAL D 2 142 ? 162.027 91.795  127.603 1.00 44.31 ?  121 VAL D N     1 
ATOM   14326 C  CA    . VAL D 2 142 ? 161.555 92.663  128.683 1.00 43.91 ?  121 VAL D CA    1 
ATOM   14327 C  C     . VAL D 2 142 ? 160.304 92.072  129.342 1.00 43.71 ?  121 VAL D C     1 
ATOM   14328 O  O     . VAL D 2 142 ? 160.192 92.055  130.566 1.00 43.44 ?  121 VAL D O     1 
ATOM   14329 C  CB    . VAL D 2 142 ? 161.280 94.111  128.191 1.00 43.65 ?  121 VAL D CB    1 
ATOM   14330 C  CG1   . VAL D 2 142 ? 160.665 94.959  129.303 1.00 43.40 ?  121 VAL D CG1   1 
ATOM   14331 C  CG2   . VAL D 2 142 ? 162.570 94.759  127.699 1.00 43.96 ?  121 VAL D CG2   1 
ATOM   14332 N  N     . PHE D 2 143 ? 159.377 91.577  128.525 1.00 44.03 ?  122 PHE D N     1 
ATOM   14333 C  CA    . PHE D 2 143 ? 158.163 90.964  129.052 1.00 44.42 ?  122 PHE D CA    1 
ATOM   14334 C  C     . PHE D 2 143 ? 158.429 89.649  129.776 1.00 45.38 ?  122 PHE D C     1 
ATOM   14335 O  O     . PHE D 2 143 ? 157.781 89.359  130.778 1.00 45.50 ?  122 PHE D O     1 
ATOM   14336 C  CB    . PHE D 2 143 ? 157.087 90.820  127.975 1.00 44.27 ?  122 PHE D CB    1 
ATOM   14337 C  CG    . PHE D 2 143 ? 156.233 92.044  127.833 1.00 43.28 ?  122 PHE D CG    1 
ATOM   14338 C  CD1   . PHE D 2 143 ? 155.166 92.266  128.702 1.00 42.17 ?  122 PHE D CD1   1 
ATOM   14339 C  CD2   . PHE D 2 143 ? 156.515 92.994  126.861 1.00 42.76 ?  122 PHE D CD2   1 
ATOM   14340 C  CE1   . PHE D 2 143 ? 154.380 93.406  128.593 1.00 42.16 ?  122 PHE D CE1   1 
ATOM   14341 C  CE2   . PHE D 2 143 ? 155.736 94.140  126.742 1.00 42.77 ?  122 PHE D CE2   1 
ATOM   14342 C  CZ    . PHE D 2 143 ? 154.664 94.348  127.610 1.00 42.28 ?  122 PHE D CZ    1 
ATOM   14343 N  N     . GLU D 2 144 ? 159.393 88.875  129.284 1.00 46.18 ?  123 GLU D N     1 
ATOM   14344 C  CA    . GLU D 2 144 ? 159.863 87.685  129.992 1.00 47.19 ?  123 GLU D CA    1 
ATOM   14345 C  C     . GLU D 2 144 ? 160.417 88.045  131.379 1.00 46.99 ?  123 GLU D C     1 
ATOM   14346 O  O     . GLU D 2 144 ? 160.093 87.373  132.363 1.00 46.94 ?  123 GLU D O     1 
ATOM   14347 C  CB    . GLU D 2 144 ? 160.920 86.947  129.159 1.00 47.80 ?  123 GLU D CB    1 
ATOM   14348 C  CG    . GLU D 2 144 ? 161.386 85.602  129.727 1.00 49.54 ?  123 GLU D CG    1 
ATOM   14349 C  CD    . GLU D 2 144 ? 162.522 84.973  128.915 1.00 52.37 ?  123 GLU D CD    1 
ATOM   14350 O  OE1   . GLU D 2 144 ? 163.490 85.686  128.561 1.00 52.92 ?  123 GLU D OE1   1 
ATOM   14351 O  OE2   . GLU D 2 144 ? 162.451 83.757  128.635 1.00 53.55 -1 123 GLU D OE2   1 
ATOM   14352 N  N     . TRP D 2 145 ? 161.239 89.099  131.444 1.00 47.02 ?  124 TRP D N     1 
ATOM   14353 C  CA    . TRP D 2 145 ? 161.848 89.572  132.701 1.00 46.93 ?  124 TRP D CA    1 
ATOM   14354 C  C     . TRP D 2 145 ? 160.795 90.072  133.678 1.00 46.55 ?  124 TRP D C     1 
ATOM   14355 O  O     . TRP D 2 145 ? 160.764 89.650  134.831 1.00 46.42 ?  124 TRP D O     1 
ATOM   14356 C  CB    . TRP D 2 145 ? 162.867 90.693  132.437 1.00 47.07 ?  124 TRP D CB    1 
ATOM   14357 C  CG    . TRP D 2 145 ? 163.703 91.112  133.650 1.00 47.82 ?  124 TRP D CG    1 
ATOM   14358 C  CD1   . TRP D 2 145 ? 164.936 90.628  134.002 1.00 48.78 ?  124 TRP D CD1   1 
ATOM   14359 C  CD2   . TRP D 2 145 ? 163.371 92.108  134.640 1.00 47.80 ?  124 TRP D CD2   1 
ATOM   14360 N  NE1   . TRP D 2 145 ? 165.387 91.250  135.145 1.00 49.06 ?  124 TRP D NE1   1 
ATOM   14361 C  CE2   . TRP D 2 145 ? 164.448 92.159  135.559 1.00 48.24 ?  124 TRP D CE2   1 
ATOM   14362 C  CE3   . TRP D 2 145 ? 162.271 92.952  134.842 1.00 47.65 ?  124 TRP D CE3   1 
ATOM   14363 C  CZ2   . TRP D 2 145 ? 164.453 93.024  136.667 1.00 47.74 ?  124 TRP D CZ2   1 
ATOM   14364 C  CZ3   . TRP D 2 145 ? 162.276 93.813  135.943 1.00 46.92 ?  124 TRP D CZ3   1 
ATOM   14365 C  CH2   . TRP D 2 145 ? 163.365 93.839  136.840 1.00 47.88 ?  124 TRP D CH2   1 
ATOM   14366 N  N     . VAL D 2 146 ? 159.934 90.973  133.213 1.00 46.09 ?  125 VAL D N     1 
ATOM   14367 C  CA    . VAL D 2 146 ? 158.924 91.579  134.072 1.00 45.36 ?  125 VAL D CA    1 
ATOM   14368 C  C     . VAL D 2 146 ? 157.888 90.531  134.508 1.00 45.28 ?  125 VAL D C     1 
ATOM   14369 O  O     . VAL D 2 146 ? 157.374 90.589  135.631 1.00 45.29 ?  125 VAL D O     1 
ATOM   14370 C  CB    . VAL D 2 146 ? 158.323 92.864  133.415 1.00 45.33 ?  125 VAL D CB    1 
ATOM   14371 C  CG1   . VAL D 2 146 ? 157.174 93.417  134.219 1.00 44.97 ?  125 VAL D CG1   1 
ATOM   14372 C  CG2   . VAL D 2 146 ? 159.404 93.940  133.286 1.00 44.52 ?  125 VAL D CG2   1 
ATOM   14373 N  N     . LYS D 2 147 ? 157.629 89.550  133.644 1.00 44.98 ?  126 LYS D N     1 
ATOM   14374 C  CA    . LYS D 2 147 ? 156.739 88.430  133.978 1.00 44.65 ?  126 LYS D CA    1 
ATOM   14375 C  C     . LYS D 2 147 ? 157.276 87.560  135.127 1.00 44.06 ?  126 LYS D C     1 
ATOM   14376 O  O     . LYS D 2 147 ? 156.501 86.965  135.877 1.00 44.65 ?  126 LYS D O     1 
ATOM   14377 C  CB    . LYS D 2 147 ? 156.472 87.550  132.754 1.00 45.31 ?  126 LYS D CB    1 
ATOM   14378 C  CG    . LYS D 2 147 ? 155.008 87.172  132.583 1.00 46.54 ?  126 LYS D CG    1 
ATOM   14379 C  CD    . LYS D 2 147 ? 154.817 85.708  132.185 1.00 49.06 ?  126 LYS D CD    1 
ATOM   14380 C  CE    . LYS D 2 147 ? 154.740 84.800  133.420 1.00 50.46 ?  126 LYS D CE    1 
ATOM   14381 N  NZ    . LYS D 2 147 ? 153.965 83.548  133.170 1.00 51.33 1  126 LYS D NZ    1 
ATOM   14382 N  N     . GLN D 2 148 ? 158.599 87.490  135.256 1.00 42.58 ?  127 GLN D N     1 
ATOM   14383 C  CA    . GLN D 2 148 ? 159.242 86.713  136.314 1.00 41.39 ?  127 GLN D CA    1 
ATOM   14384 C  C     . GLN D 2 148 ? 159.564 87.557  137.554 1.00 39.56 ?  127 GLN D C     1 
ATOM   14385 O  O     . GLN D 2 148 ? 159.837 87.010  138.622 1.00 39.77 ?  127 GLN D O     1 
ATOM   14386 C  CB    . GLN D 2 148 ? 160.498 86.015  135.756 1.00 42.11 ?  127 GLN D CB    1 
ATOM   14387 C  CG    . GLN D 2 148 ? 161.677 85.871  136.714 1.00 44.08 ?  127 GLN D CG    1 
ATOM   14388 C  CD    . GLN D 2 148 ? 162.742 86.955  136.538 1.00 46.12 ?  127 GLN D CD    1 
ATOM   14389 O  OE1   . GLN D 2 148 ? 162.432 88.140  136.354 1.00 46.47 ?  127 GLN D OE1   1 
ATOM   14390 N  NE2   . GLN D 2 148 ? 164.010 86.549  136.610 1.00 45.69 ?  127 GLN D NE2   1 
ATOM   14391 N  N     . ASN D 2 149 ? 159.519 88.884  137.406 1.00 36.99 ?  128 ASN D N     1 
ATOM   14392 C  CA    . ASN D 2 149 ? 159.866 89.809  138.485 1.00 34.54 ?  128 ASN D CA    1 
ATOM   14393 C  C     . ASN D 2 149 ? 159.003 89.659  139.741 1.00 33.13 ?  128 ASN D C     1 
ATOM   14394 O  O     . ASN D 2 149 ? 157.778 89.727  139.679 1.00 32.62 ?  128 ASN D O     1 
ATOM   14395 C  CB    . ASN D 2 149 ? 159.817 91.256  137.993 1.00 34.24 ?  128 ASN D CB    1 
ATOM   14396 C  CG    . ASN D 2 149 ? 160.284 92.237  139.050 1.00 33.83 ?  128 ASN D CG    1 
ATOM   14397 O  OD1   . ASN D 2 149 ? 159.473 92.873  139.726 1.00 32.21 ?  128 ASN D OD1   1 
ATOM   14398 N  ND2   . ASN D 2 149 ? 161.600 92.339  139.221 1.00 33.26 ?  128 ASN D ND2   1 
ATOM   14399 N  N     . LYS D 2 150 ? 159.666 89.489  140.882 1.00 31.49 ?  129 LYS D N     1 
ATOM   14400 C  CA    . LYS D 2 150 ? 159.007 89.204  142.154 1.00 30.68 ?  129 LYS D CA    1 
ATOM   14401 C  C     . LYS D 2 150 ? 158.026 90.304  142.628 1.00 28.95 ?  129 LYS D C     1 
ATOM   14402 O  O     . LYS D 2 150 ? 156.936 89.998  143.126 1.00 27.90 ?  129 LYS D O     1 
ATOM   14403 C  CB    . LYS D 2 150 ? 160.087 88.910  143.206 1.00 31.17 ?  129 LYS D CB    1 
ATOM   14404 C  CG    . LYS D 2 150 ? 159.668 88.933  144.662 1.00 33.66 ?  129 LYS D CG    1 
ATOM   14405 C  CD    . LYS D 2 150 ? 160.891 88.645  145.547 1.00 38.08 ?  129 LYS D CD    1 
ATOM   14406 C  CE    . LYS D 2 150 ? 160.743 89.242  146.952 1.00 40.20 ?  129 LYS D CE    1 
ATOM   14407 N  NZ    . LYS D 2 150 ? 160.143 88.282  147.918 1.00 42.60 1  129 LYS D NZ    1 
ATOM   14408 N  N     . TYR D 2 151 ? 158.413 91.569  142.476 1.00 27.36 ?  130 TYR D N     1 
ATOM   14409 C  CA    . TYR D 2 151 ? 157.603 92.685  142.999 1.00 26.56 ?  130 TYR D CA    1 
ATOM   14410 C  C     . TYR D 2 151 ? 156.409 92.998  142.112 1.00 25.66 ?  130 TYR D C     1 
ATOM   14411 O  O     . TYR D 2 151 ? 155.331 93.313  142.626 1.00 25.61 ?  130 TYR D O     1 
ATOM   14412 C  CB    . TYR D 2 151 ? 158.465 93.936  143.265 1.00 26.32 ?  130 TYR D CB    1 
ATOM   14413 C  CG    . TYR D 2 151 ? 159.752 93.591  143.988 1.00 27.20 ?  130 TYR D CG    1 
ATOM   14414 C  CD1   . TYR D 2 151 ? 159.729 93.183  145.322 1.00 27.31 ?  130 TYR D CD1   1 
ATOM   14415 C  CD2   . TYR D 2 151 ? 160.979 93.618  143.327 1.00 27.22 ?  130 TYR D CD2   1 
ATOM   14416 C  CE1   . TYR D 2 151 ? 160.901 92.832  145.988 1.00 29.65 ?  130 TYR D CE1   1 
ATOM   14417 C  CE2   . TYR D 2 151 ? 162.166 93.267  143.989 1.00 28.75 ?  130 TYR D CE2   1 
ATOM   14418 C  CZ    . TYR D 2 151 ? 162.105 92.882  145.331 1.00 29.17 ?  130 TYR D CZ    1 
ATOM   14419 O  OH    . TYR D 2 151 ? 163.243 92.529  146.021 1.00 30.61 ?  130 TYR D OH    1 
ATOM   14420 N  N     . LEU D 2 152 ? 156.600 92.908  140.794 1.00 24.87 ?  131 LEU D N     1 
ATOM   14421 C  CA    . LEU D 2 152 ? 155.488 93.047  139.860 1.00 24.37 ?  131 LEU D CA    1 
ATOM   14422 C  C     . LEU D 2 152 ? 154.476 91.913  140.066 1.00 24.18 ?  131 LEU D C     1 
ATOM   14423 O  O     . LEU D 2 152 ? 153.284 92.172  140.226 1.00 23.16 ?  131 LEU D O     1 
ATOM   14424 C  CB    . LEU D 2 152 ? 155.942 93.102  138.398 1.00 24.45 ?  131 LEU D CB    1 
ATOM   14425 C  CG    . LEU D 2 152 ? 154.661 93.297  137.567 1.00 26.33 ?  131 LEU D CG    1 
ATOM   14426 C  CD1   . LEU D 2 152 ? 154.140 94.736  137.691 1.00 25.00 ?  131 LEU D CD1   1 
ATOM   14427 C  CD2   . LEU D 2 152 ? 154.788 92.871  136.133 1.00 29.15 ?  131 LEU D CD2   1 
ATOM   14428 N  N     . GLN D 2 153 ? 154.960 90.669  140.095 1.00 24.07 ?  132 GLN D N     1 
ATOM   14429 C  CA    . GLN D 2 153 ? 154.077 89.512  140.354 1.00 24.99 ?  132 GLN D CA    1 
ATOM   14430 C  C     . GLN D 2 153 ? 153.331 89.596  141.683 1.00 24.24 ?  132 GLN D C     1 
ATOM   14431 O  O     . GLN D 2 153 ? 152.119 89.322  141.746 1.00 23.75 ?  132 GLN D O     1 
ATOM   14432 C  CB    . GLN D 2 153 ? 154.833 88.178  140.232 1.00 25.84 ?  132 GLN D CB    1 
ATOM   14433 C  CG    . GLN D 2 153 ? 155.221 87.817  138.773 1.00 28.48 ?  132 GLN D CG    1 
ATOM   14434 C  CD    . GLN D 2 153 ? 154.016 87.660  137.832 1.00 30.95 ?  132 GLN D CD    1 
ATOM   14435 O  OE1   . GLN D 2 153 ? 152.965 87.173  138.232 1.00 31.78 ?  132 GLN D OE1   1 
ATOM   14436 N  NE2   . GLN D 2 153 ? 154.181 88.065  136.572 1.00 32.81 ?  132 GLN D NE2   1 
ATOM   14437 N  N     . LYS D 2 154 ? 154.028 89.983  142.748 1.00 24.00 ?  133 LYS D N     1 
ATOM   14438 C  CA    . LYS D 2 154 ? 153.357 90.059  144.046 1.00 24.43 ?  133 LYS D CA    1 
ATOM   14439 C  C     . LYS D 2 154 ? 152.100 90.939  143.973 1.00 23.40 ?  133 LYS D C     1 
ATOM   14440 O  O     . LYS D 2 154 ? 151.009 90.501  144.345 1.00 22.68 ?  133 LYS D O     1 
ATOM   14441 C  CB    . LYS D 2 154 ? 154.278 90.560  145.164 1.00 24.64 ?  133 LYS D CB    1 
ATOM   14442 C  CG    . LYS D 2 154 ? 153.540 90.587  146.515 1.00 28.01 ?  133 LYS D CG    1 
ATOM   14443 C  CD    . LYS D 2 154 ? 154.423 90.901  147.699 1.00 32.56 ?  133 LYS D CD    1 
ATOM   14444 C  CE    . LYS D 2 154 ? 155.370 89.765  147.998 1.00 34.45 ?  133 LYS D CE    1 
ATOM   14445 N  NZ    . LYS D 2 154 ? 156.242 90.101  149.167 1.00 36.11 1  133 LYS D NZ    1 
ATOM   14446 N  N     . LYS D 2 155 ? 152.253 92.172  143.491 1.00 23.07 ?  134 LYS D N     1 
ATOM   14447 C  CA    . LYS D 2 155 ? 151.099 93.063  143.394 1.00 22.70 ?  134 LYS D CA    1 
ATOM   14448 C  C     . LYS D 2 155 ? 150.074 92.586  142.366 1.00 21.96 ?  134 LYS D C     1 
ATOM   14449 O  O     . LYS D 2 155 ? 148.881 92.621  142.645 1.00 22.25 ?  134 LYS D O     1 
ATOM   14450 C  CB    . LYS D 2 155 ? 151.504 94.533  143.179 1.00 22.70 ?  134 LYS D CB    1 
ATOM   14451 C  CG    . LYS D 2 155 ? 152.202 94.861  141.874 1.00 23.62 ?  134 LYS D CG    1 
ATOM   14452 C  CD    . LYS D 2 155 ? 152.454 96.366  141.806 1.00 25.32 ?  134 LYS D CD    1 
ATOM   14453 C  CE    . LYS D 2 155 ? 153.763 96.658  141.080 1.00 27.09 ?  134 LYS D CE    1 
ATOM   14454 N  NZ    . LYS D 2 155 ? 153.973 98.130  140.949 1.00 26.65 1  134 LYS D NZ    1 
ATOM   14455 N  N     . ALA D 2 156 ? 150.517 92.113  141.200 1.00 21.76 ?  135 ALA D N     1 
ATOM   14456 C  CA    . ALA D 2 156 ? 149.556 91.649  140.182 1.00 21.83 ?  135 ALA D CA    1 
ATOM   14457 C  C     . ALA D 2 156 ? 148.670 90.519  140.732 1.00 22.30 ?  135 ALA D C     1 
ATOM   14458 O  O     . ALA D 2 156 ? 147.445 90.552  140.584 1.00 21.92 ?  135 ALA D O     1 
ATOM   14459 C  CB    . ALA D 2 156 ? 150.274 91.200  138.897 1.00 22.30 ?  135 ALA D CB    1 
ATOM   14460 N  N     . GLN D 2 157 ? 149.288 89.537  141.391 1.00 22.15 ?  136 GLN D N     1 
ATOM   14461 C  CA    . GLN D 2 157 ? 148.533 88.395  141.918 1.00 22.38 ?  136 GLN D CA    1 
ATOM   14462 C  C     . GLN D 2 157 ? 147.671 88.733  143.141 1.00 21.59 ?  136 GLN D C     1 
ATOM   14463 O  O     . GLN D 2 157 ? 146.613 88.135  143.335 1.00 21.44 ?  136 GLN D O     1 
ATOM   14464 C  CB    . GLN D 2 157 ? 149.449 87.192  142.208 1.00 22.94 ?  136 GLN D CB    1 
ATOM   14465 C  CG    . GLN D 2 157 ? 150.247 86.677  141.000 1.00 25.31 ?  136 GLN D CG    1 
ATOM   14466 C  CD    . GLN D 2 157 ? 149.416 86.535  139.721 1.00 28.02 ?  136 GLN D CD    1 
ATOM   14467 O  OE1   . GLN D 2 157 ? 148.255 86.114  139.750 1.00 27.14 ?  136 GLN D OE1   1 
ATOM   14468 N  NE2   . GLN D 2 157 ? 150.024 86.882  138.589 1.00 29.47 ?  136 GLN D NE2   1 
ATOM   14469 N  N     . MET D 2 158 ? 148.116 89.675  143.966 1.00 21.52 ?  137 MET D N     1 
ATOM   14470 C  CA    . MET D 2 158 ? 147.292 90.145  145.093 1.00 22.20 ?  137 MET D CA    1 
ATOM   14471 C  C     . MET D 2 158 ? 145.962 90.741  144.618 1.00 21.84 ?  137 MET D C     1 
ATOM   14472 O  O     . MET D 2 158 ? 144.904 90.447  145.180 1.00 21.91 ?  137 MET D O     1 
ATOM   14473 C  CB    . MET D 2 158 ? 148.042 91.170  145.944 1.00 22.52 ?  137 MET D CB    1 
ATOM   14474 C  CG    . MET D 2 158 ? 149.087 90.551  146.883 1.00 25.81 ?  137 MET D CG    1 
ATOM   14475 S  SD    . MET D 2 158 ? 149.977 91.776  147.880 1.00 31.19 ?  137 MET D SD    1 
ATOM   14476 C  CE    . MET D 2 158 ? 148.606 92.403  148.814 1.00 23.91 ?  137 MET D CE    1 
ATOM   14477 N  N     . ILE D 2 159 ? 146.033 91.573  143.581 1.00 21.41 ?  138 ILE D N     1 
ATOM   14478 C  CA    . ILE D 2 159 ? 144.855 92.228  143.020 1.00 21.51 ?  138 ILE D CA    1 
ATOM   14479 C  C     . ILE D 2 159 ? 143.923 91.192  142.371 1.00 21.77 ?  138 ILE D C     1 
ATOM   14480 O  O     . ILE D 2 159 ? 142.714 91.174  142.648 1.00 21.44 ?  138 ILE D O     1 
ATOM   14481 C  CB    . ILE D 2 159 ? 145.280 93.372  142.019 1.00 21.49 ?  138 ILE D CB    1 
ATOM   14482 C  CG1   . ILE D 2 159 ? 146.078 94.472  142.736 1.00 21.16 ?  138 ILE D CG1   1 
ATOM   14483 C  CG2   . ILE D 2 159 ? 144.076 93.966  141.278 1.00 22.34 ?  138 ILE D CG2   1 
ATOM   14484 C  CD1   . ILE D 2 159 ? 145.309 95.221  143.845 1.00 23.85 ?  138 ILE D CD1   1 
ATOM   14485 N  N     . VAL D 2 160 ? 144.502 90.332  141.524 1.00 21.96 ?  139 VAL D N     1 
ATOM   14486 C  CA    . VAL D 2 160 ? 143.768 89.285  140.797 1.00 22.59 ?  139 VAL D CA    1 
ATOM   14487 C  C     . VAL D 2 160 ? 143.101 88.307  141.774 1.00 22.36 ?  139 VAL D C     1 
ATOM   14488 O  O     . VAL D 2 160 ? 141.978 87.852  141.533 1.00 21.64 ?  139 VAL D O     1 
ATOM   14489 C  CB    . VAL D 2 160 ? 144.701 88.532  139.789 1.00 23.08 ?  139 VAL D CB    1 
ATOM   14490 C  CG1   . VAL D 2 160 ? 144.087 87.207  139.299 1.00 24.33 ?  139 VAL D CG1   1 
ATOM   14491 C  CG2   . VAL D 2 160 ? 145.039 89.433  138.590 1.00 22.87 ?  139 VAL D CG2   1 
ATOM   14492 N  N     . GLY D 2 161 ? 143.795 87.998  142.873 1.00 22.21 ?  140 GLY D N     1 
ATOM   14493 C  CA    . GLY D 2 161 ? 143.246 87.139  143.919 1.00 22.50 ?  140 GLY D CA    1 
ATOM   14494 C  C     . GLY D 2 161 ? 141.928 87.668  144.476 1.00 22.88 ?  140 GLY D C     1 
ATOM   14495 O  O     . GLY D 2 161 ? 140.973 86.902  144.665 1.00 23.54 ?  140 GLY D O     1 
ATOM   14496 N  N     . LEU D 2 162 ? 141.864 88.976  144.725 1.00 22.25 ?  141 LEU D N     1 
ATOM   14497 C  CA    . LEU D 2 162 ? 140.631 89.591  145.225 1.00 22.48 ?  141 LEU D CA    1 
ATOM   14498 C  C     . LEU D 2 162 ? 139.501 89.605  144.192 1.00 22.27 ?  141 LEU D C     1 
ATOM   14499 O  O     . LEU D 2 162 ? 138.336 89.446  144.559 1.00 22.31 ?  141 LEU D O     1 
ATOM   14500 C  CB    . LEU D 2 162 ? 140.887 90.990  145.821 1.00 22.07 ?  141 LEU D CB    1 
ATOM   14501 C  CG    . LEU D 2 162 ? 141.579 90.966  147.202 1.00 22.81 ?  141 LEU D CG    1 
ATOM   14502 C  CD1   . LEU D 2 162 ? 142.268 92.291  147.525 1.00 21.65 ?  141 LEU D CD1   1 
ATOM   14503 C  CD2   . LEU D 2 162 ? 140.640 90.528  148.331 1.00 23.35 ?  141 LEU D CD2   1 
ATOM   14504 N  N     . TYR D 2 163 ? 139.834 89.794  142.913 1.00 22.63 ?  142 TYR D N     1 
ATOM   14505 C  CA    . TYR D 2 163 ? 138.826 89.684  141.839 1.00 23.30 ?  142 TYR D CA    1 
ATOM   14506 C  C     . TYR D 2 163 ? 138.266 88.272  141.728 1.00 23.40 ?  142 TYR D C     1 
ATOM   14507 O  O     . TYR D 2 163 ? 137.076 88.094  141.513 1.00 23.75 ?  142 TYR D O     1 
ATOM   14508 C  CB    . TYR D 2 163 ? 139.402 90.043  140.476 1.00 23.22 ?  142 TYR D CB    1 
ATOM   14509 C  CG    . TYR D 2 163 ? 139.916 91.448  140.323 1.00 24.01 ?  142 TYR D CG    1 
ATOM   14510 C  CD1   . TYR D 2 163 ? 139.469 92.473  141.147 1.00 24.47 ?  142 TYR D CD1   1 
ATOM   14511 C  CD2   . TYR D 2 163 ? 140.851 91.748  139.336 1.00 24.62 ?  142 TYR D CD2   1 
ATOM   14512 C  CE1   . TYR D 2 163 ? 139.942 93.761  141.000 1.00 26.33 ?  142 TYR D CE1   1 
ATOM   14513 C  CE2   . TYR D 2 163 ? 141.323 93.040  139.171 1.00 26.07 ?  142 TYR D CE2   1 
ATOM   14514 C  CZ    . TYR D 2 163 ? 140.856 94.042  140.011 1.00 26.65 ?  142 TYR D CZ    1 
ATOM   14515 O  OH    . TYR D 2 163 ? 141.320 95.330  139.874 1.00 31.13 ?  142 TYR D OH    1 
ATOM   14516 N  N     . LYS D 2 164 ? 139.127 87.272  141.866 1.00 23.70 ?  143 LYS D N     1 
ATOM   14517 C  CA    . LYS D 2 164 ? 138.694 85.868  141.799 1.00 24.47 ?  143 LYS D CA    1 
ATOM   14518 C  C     . LYS D 2 164 ? 137.850 85.425  143.005 1.00 24.55 ?  143 LYS D C     1 
ATOM   14519 O  O     . LYS D 2 164 ? 137.155 84.409  142.944 1.00 24.49 ?  143 LYS D O     1 
ATOM   14520 C  CB    . LYS D 2 164 ? 139.913 84.954  141.649 1.00 24.98 ?  143 LYS D CB    1 
ATOM   14521 C  CG    . LYS D 2 164 ? 140.544 84.951  140.249 1.00 27.10 ?  143 LYS D CG    1 
ATOM   14522 C  CD    . LYS D 2 164 ? 141.662 83.920  140.190 1.00 30.75 ?  143 LYS D CD    1 
ATOM   14523 C  CE    . LYS D 2 164 ? 142.271 83.786  138.796 1.00 32.81 ?  143 LYS D CE    1 
ATOM   14524 N  NZ    . LYS D 2 164 ? 143.453 82.834  138.781 1.00 33.68 1  143 LYS D NZ    1 
ATOM   14525 N  N     . ALA D 2 165 ? 137.922 86.179  144.099 1.00 24.18 ?  144 ALA D N     1 
ATOM   14526 C  CA    . ALA D 2 165 ? 137.218 85.821  145.334 1.00 25.04 ?  144 ALA D CA    1 
ATOM   14527 C  C     . ALA D 2 165 ? 135.810 86.419  145.463 1.00 25.00 ?  144 ALA D C     1 
ATOM   14528 O  O     . ALA D 2 165 ? 135.114 86.152  146.454 1.00 25.50 ?  144 ALA D O     1 
ATOM   14529 C  CB    . ALA D 2 165 ? 138.068 86.185  146.563 1.00 25.02 ?  144 ALA D CB    1 
ATOM   14530 N  N     . ILE D 2 166 ? 135.387 87.222  144.483 1.00 24.60 ?  145 ILE D N     1 
ATOM   14531 C  CA    . ILE D 2 166 ? 134.031 87.772  144.490 1.00 24.40 ?  145 ILE D CA    1 
ATOM   14532 C  C     . ILE D 2 166 ? 133.018 86.622  144.387 1.00 25.75 ?  145 ILE D C     1 
ATOM   14533 O  O     . ILE D 2 166 ? 133.167 85.722  143.553 1.00 25.84 ?  145 ILE D O     1 
ATOM   14534 C  CB    . ILE D 2 166 ? 133.771 88.777  143.332 1.00 24.15 ?  145 ILE D CB    1 
ATOM   14535 C  CG1   . ILE D 2 166 ? 134.861 89.846  143.275 1.00 23.15 ?  145 ILE D CG1   1 
ATOM   14536 C  CG2   . ILE D 2 166 ? 132.397 89.428  143.492 1.00 22.72 ?  145 ILE D CG2   1 
ATOM   14537 C  CD1   . ILE D 2 166 ? 134.800 90.717  142.037 1.00 21.70 ?  145 ILE D CD1   1 
ATOM   14538 N  N     . GLN D 2 167 ? 132.019 86.644  145.259 1.00 26.52 ?  146 GLN D N     1 
ATOM   14539 C  CA    . GLN D 2 167 ? 130.958 85.647  145.230 1.00 28.77 ?  146 GLN D CA    1 
ATOM   14540 C  C     . GLN D 2 167 ? 129.634 86.284  144.830 1.00 29.20 ?  146 GLN D C     1 
ATOM   14541 O  O     . GLN D 2 167 ? 129.325 87.412  145.243 1.00 28.89 ?  146 GLN D O     1 
ATOM   14542 C  CB    . GLN D 2 167 ? 130.826 84.974  146.594 1.00 29.04 ?  146 GLN D CB    1 
ATOM   14543 C  CG    . GLN D 2 167 ? 132.047 84.163  146.983 1.00 31.87 ?  146 GLN D CG    1 
ATOM   14544 C  CD    . GLN D 2 167 ? 132.438 84.384  148.419 1.00 35.35 ?  146 GLN D CD    1 
ATOM   14545 O  OE1   . GLN D 2 167 ? 131.725 83.977  149.340 1.00 36.91 ?  146 GLN D OE1   1 
ATOM   14546 N  NE2   . GLN D 2 167 ? 133.582 85.034  148.626 1.00 36.19 ?  146 GLN D NE2   1 
ATOM   14547 N  N     . LYS D 2 168 ? 128.856 85.559  144.029 1.00 30.29 ?  147 LYS D N     1 
ATOM   14548 C  CA    . LYS D 2 168 ? 127.532 86.024  143.621 1.00 31.24 ?  147 LYS D CA    1 
ATOM   14549 C  C     . LYS D 2 168 ? 126.697 86.453  144.827 1.00 31.73 ?  147 LYS D C     1 
ATOM   14550 O  O     . LYS D 2 168 ? 126.687 85.766  145.848 1.00 31.46 ?  147 LYS D O     1 
ATOM   14551 C  CB    . LYS D 2 168 ? 126.807 84.944  142.822 1.00 31.92 ?  147 LYS D CB    1 
ATOM   14552 C  CG    . LYS D 2 168 ? 125.453 85.390  142.289 1.00 33.23 ?  147 LYS D CG    1 
ATOM   14553 C  CD    . LYS D 2 168 ? 124.877 84.382  141.307 1.00 36.06 ?  147 LYS D CD    1 
ATOM   14554 C  CE    . LYS D 2 168 ? 123.498 84.799  140.839 1.00 35.46 ?  147 LYS D CE    1 
ATOM   14555 N  NZ    . LYS D 2 168 ? 123.545 85.979  139.935 1.00 38.24 1  147 LYS D NZ    1 
ATOM   14556 N  N     . ASP D 2 169 ? 126.023 87.599  144.703 1.00 32.28 ?  148 ASP D N     1 
ATOM   14557 C  CA    . ASP D 2 169 ? 125.167 88.156  145.765 1.00 33.45 ?  148 ASP D CA    1 
ATOM   14558 C  C     . ASP D 2 169 ? 125.850 88.390  147.112 1.00 33.30 ?  148 ASP D C     1 
ATOM   14559 O  O     . ASP D 2 169 ? 125.187 88.410  148.151 1.00 34.32 ?  148 ASP D O     1 
ATOM   14560 C  CB    . ASP D 2 169 ? 123.929 87.273  145.993 1.00 34.63 ?  148 ASP D CB    1 
ATOM   14561 C  CG    . ASP D 2 169 ? 122.911 87.378  144.878 1.00 36.09 ?  148 ASP D CG    1 
ATOM   14562 O  OD1   . ASP D 2 169 ? 123.003 88.293  144.032 1.00 37.80 ?  148 ASP D OD1   1 
ATOM   14563 O  OD2   . ASP D 2 169 ? 121.999 86.526  144.861 1.00 40.47 -1 148 ASP D OD2   1 
ATOM   14564 N  N     . ASP D 2 170 ? 127.165 88.542  147.114 1.00 32.58 ?  149 ASP D N     1 
ATOM   14565 C  CA    . ASP D 2 170 ? 127.865 88.889  148.349 1.00 32.01 ?  149 ASP D CA    1 
ATOM   14566 C  C     . ASP D 2 170 ? 128.559 90.233  148.160 1.00 30.59 ?  149 ASP D C     1 
ATOM   14567 O  O     . ASP D 2 170 ? 129.598 90.323  147.506 1.00 29.11 ?  149 ASP D O     1 
ATOM   14568 C  CB    . ASP D 2 170 ? 128.847 87.789  148.762 1.00 32.93 ?  149 ASP D CB    1 
ATOM   14569 C  CG    . ASP D 2 170 ? 129.770 88.212  149.897 1.00 35.05 ?  149 ASP D CG    1 
ATOM   14570 O  OD1   . ASP D 2 170 ? 129.392 89.054  150.741 1.00 39.25 ?  149 ASP D OD1   1 
ATOM   14571 O  OD2   . ASP D 2 170 ? 130.887 87.681  149.958 1.00 39.22 -1 149 ASP D OD2   1 
ATOM   14572 N  N     . GLU D 2 171 ? 127.954 91.269  148.735 1.00 29.34 ?  150 GLU D N     1 
ATOM   14573 C  CA    . GLU D 2 171 ? 128.431 92.639  148.568 1.00 28.51 ?  150 GLU D CA    1 
ATOM   14574 C  C     . GLU D 2 171 ? 129.740 92.926  149.317 1.00 27.27 ?  150 GLU D C     1 
ATOM   14575 O  O     . GLU D 2 171 ? 130.462 93.841  148.954 1.00 26.62 ?  150 GLU D O     1 
ATOM   14576 C  CB    . GLU D 2 171 ? 127.335 93.643  148.952 1.00 29.09 ?  150 GLU D CB    1 
ATOM   14577 C  CG    . GLU D 2 171 ? 126.993 93.704  150.439 1.00 30.68 ?  150 GLU D CG    1 
ATOM   14578 C  CD    . GLU D 2 171 ? 125.783 94.581  150.722 1.00 33.92 ?  150 GLU D CD    1 
ATOM   14579 O  OE1   . GLU D 2 171 ? 125.236 95.175  149.760 1.00 36.31 ?  150 GLU D OE1   1 
ATOM   14580 O  OE2   . GLU D 2 171 ? 125.374 94.688  151.898 1.00 34.02 -1 150 GLU D OE2   1 
ATOM   14581 N  N     . ILE D 2 172 ? 130.051 92.132  150.340 1.00 26.19 ?  151 ILE D N     1 
ATOM   14582 C  CA    . ILE D 2 172 ? 131.309 92.286  151.071 1.00 25.49 ?  151 ILE D CA    1 
ATOM   14583 C  C     . ILE D 2 172 ? 132.498 91.917  150.180 1.00 24.61 ?  151 ILE D C     1 
ATOM   14584 O  O     . ILE D 2 172 ? 133.475 92.671  150.090 1.00 24.09 ?  151 ILE D O     1 
ATOM   14585 C  CB    . ILE D 2 172 ? 131.318 91.477  152.399 1.00 25.98 ?  151 ILE D CB    1 
ATOM   14586 C  CG1   . ILE D 2 172 ? 130.244 91.994  153.358 1.00 26.86 ?  151 ILE D CG1   1 
ATOM   14587 C  CG2   . ILE D 2 172 ? 132.711 91.486  153.084 1.00 26.50 ?  151 ILE D CG2   1 
ATOM   14588 C  CD1   . ILE D 2 172 ? 130.412 93.451  153.764 1.00 27.81 ?  151 ILE D CD1   1 
ATOM   14589 N  N     . SER D 2 173 ? 132.397 90.773  149.509 1.00 23.71 ?  152 SER D N     1 
ATOM   14590 C  CA    . SER D 2 173 ? 133.446 90.323  148.595 1.00 23.38 ?  152 SER D CA    1 
ATOM   14591 C  C     . SER D 2 173 ? 133.562 91.262  147.381 1.00 22.41 ?  152 SER D C     1 
ATOM   14592 O  O     . SER D 2 173 ? 134.657 91.492  146.860 1.00 21.43 ?  152 SER D O     1 
ATOM   14593 C  CB    . SER D 2 173 ? 133.216 88.869  148.164 1.00 23.90 ?  152 SER D CB    1 
ATOM   14594 O  OG    . SER D 2 173 ? 132.099 88.709  147.291 1.00 23.74 ?  152 SER D OG    1 
ATOM   14595 N  N     . LEU D 2 174 ? 132.433 91.816  146.950 1.00 21.63 ?  153 LEU D N     1 
ATOM   14596 C  CA    . LEU D 2 174 ? 132.449 92.794  145.859 1.00 20.75 ?  153 LEU D CA    1 
ATOM   14597 C  C     . LEU D 2 174 ? 133.190 94.055  146.302 1.00 20.96 ?  153 LEU D C     1 
ATOM   14598 O  O     . LEU D 2 174 ? 134.016 94.585  145.560 1.00 20.41 ?  153 LEU D O     1 
ATOM   14599 C  CB    . LEU D 2 174 ? 131.021 93.136  145.389 1.00 20.62 ?  153 LEU D CB    1 
ATOM   14600 C  CG    . LEU D 2 174 ? 130.895 94.188  144.267 1.00 19.55 ?  153 LEU D CG    1 
ATOM   14601 C  CD1   . LEU D 2 174 ? 131.760 93.807  143.059 1.00 20.44 ?  153 LEU D CD1   1 
ATOM   14602 C  CD2   . LEU D 2 174 ? 129.423 94.356  143.865 1.00 20.99 ?  153 LEU D CD2   1 
ATOM   14603 N  N     . PHE D 2 175 ? 132.894 94.526  147.513 1.00 21.07 ?  154 PHE D N     1 
ATOM   14604 C  CA    . PHE D 2 175 ? 133.551 95.715  148.052 1.00 21.32 ?  154 PHE D CA    1 
ATOM   14605 C  C     . PHE D 2 175 ? 135.073 95.536  148.111 1.00 21.08 ?  154 PHE D C     1 
ATOM   14606 O  O     . PHE D 2 175 ? 135.828 96.429  147.722 1.00 20.85 ?  154 PHE D O     1 
ATOM   14607 C  CB    . PHE D 2 175 ? 133.005 96.045  149.445 1.00 21.20 ?  154 PHE D CB    1 
ATOM   14608 C  CG    . PHE D 2 175 ? 133.805 97.079  150.181 1.00 22.46 ?  154 PHE D CG    1 
ATOM   14609 C  CD1   . PHE D 2 175 ? 133.486 98.431  150.067 1.00 21.21 ?  154 PHE D CD1   1 
ATOM   14610 C  CD2   . PHE D 2 175 ? 134.876 96.707  150.999 1.00 22.53 ?  154 PHE D CD2   1 
ATOM   14611 C  CE1   . PHE D 2 175 ? 134.209 99.390  150.748 1.00 22.11 ?  154 PHE D CE1   1 
ATOM   14612 C  CE2   . PHE D 2 175 ? 135.621 97.668  151.676 1.00 23.26 ?  154 PHE D CE2   1 
ATOM   14613 C  CZ    . PHE D 2 175 ? 135.286 99.013  151.557 1.00 22.08 ?  154 PHE D CZ    1 
ATOM   14614 N  N     . LYS D 2 176 ? 135.513 94.386  148.611 1.00 21.14 ?  155 LYS D N     1 
ATOM   14615 C  CA    . LYS D 2 176 ? 136.944 94.080  148.702 1.00 20.93 ?  155 LYS D CA    1 
ATOM   14616 C  C     . LYS D 2 176 ? 137.633 94.131  147.341 1.00 20.61 ?  155 LYS D C     1 
ATOM   14617 O  O     . LYS D 2 176 ? 138.737 94.670  147.210 1.00 20.62 ?  155 LYS D O     1 
ATOM   14618 C  CB    . LYS D 2 176 ? 137.141 92.720  149.354 1.00 21.27 ?  155 LYS D CB    1 
ATOM   14619 C  CG    . LYS D 2 176 ? 136.858 92.758  150.831 1.00 22.04 ?  155 LYS D CG    1 
ATOM   14620 C  CD    . LYS D 2 176 ? 136.948 91.388  151.482 1.00 25.24 ?  155 LYS D CD    1 
ATOM   14621 C  CE    . LYS D 2 176 ? 136.715 91.529  152.964 1.00 25.83 ?  155 LYS D CE    1 
ATOM   14622 N  NZ    . LYS D 2 176 ? 136.803 90.230  153.693 1.00 26.64 1  155 LYS D NZ    1 
ATOM   14623 N  N     . ALA D 2 177 ? 136.963 93.592  146.328 1.00 20.02 ?  156 ALA D N     1 
ATOM   14624 C  CA    . ALA D 2 177 ? 137.458 93.667  144.955 1.00 19.86 ?  156 ALA D CA    1 
ATOM   14625 C  C     . ALA D 2 177 ? 137.488 95.109  144.428 1.00 19.61 ?  156 ALA D C     1 
ATOM   14626 O  O     . ALA D 2 177 ? 138.378 95.484  143.663 1.00 19.69 ?  156 ALA D O     1 
ATOM   14627 C  CB    . ALA D 2 177 ? 136.611 92.808  144.075 1.00 19.99 ?  156 ALA D CB    1 
ATOM   14628 N  N     . MET D 2 178 ? 136.505 95.913  144.830 1.00 19.75 ?  157 MET D N     1 
ATOM   14629 C  CA    . MET D 2 178 ? 136.442 97.322  144.390 1.00 18.89 ?  157 MET D CA    1 
ATOM   14630 C  C     . MET D 2 178 ? 137.589 98.114  144.998 1.00 18.62 ?  157 MET D C     1 
ATOM   14631 O  O     . MET D 2 178 ? 138.190 98.964  144.330 1.00 18.10 ?  157 MET D O     1 
ATOM   14632 C  CB    . MET D 2 178 ? 135.104 97.952  144.766 1.00 18.82 ?  157 MET D CB    1 
ATOM   14633 C  CG    . MET D 2 178 ? 133.954 97.488  143.887 1.00 20.20 ?  157 MET D CG    1 
ATOM   14634 S  SD    . MET D 2 178 ? 132.400 98.159  144.495 1.00 23.78 ?  157 MET D SD    1 
ATOM   14635 C  CE    . MET D 2 178 ? 131.310 97.674  143.160 1.00 22.62 ?  157 MET D CE    1 
ATOM   14636 N  N     . VAL D 2 179 ? 137.899 97.809  146.260 1.00 18.34 ?  158 VAL D N     1 
ATOM   14637 C  CA    . VAL D 2 179 ? 139.044 98.396  146.938 1.00 18.75 ?  158 VAL D CA    1 
ATOM   14638 C  C     . VAL D 2 179 ? 140.329 98.064  146.191 1.00 18.86 ?  158 VAL D C     1 
ATOM   14639 O  O     . VAL D 2 179 ? 141.157 98.960  145.951 1.00 18.79 ?  158 VAL D O     1 
ATOM   14640 C  CB    . VAL D 2 179 ? 139.162 97.941  148.417 1.00 19.02 ?  158 VAL D CB    1 
ATOM   14641 C  CG1   . VAL D 2 179 ? 140.500 98.406  149.009 1.00 19.10 ?  158 VAL D CG1   1 
ATOM   14642 C  CG2   . VAL D 2 179 ? 137.981 98.469  149.246 1.00 18.94 ?  158 VAL D CG2   1 
ATOM   14643 N  N     . ALA D 2 180 ? 140.493 96.782  145.841 1.00 18.96 ?  159 ALA D N     1 
ATOM   14644 C  CA    . ALA D 2 180 ? 141.627 96.336  145.028 1.00 19.05 ?  159 ALA D CA    1 
ATOM   14645 C  C     . ALA D 2 180 ? 141.687 97.097  143.701 1.00 18.67 ?  159 ALA D C     1 
ATOM   14646 O  O     . ALA D 2 180 ? 142.758 97.570  143.299 1.00 17.72 ?  159 ALA D O     1 
ATOM   14647 C  CB    . ALA D 2 180 ? 141.562 94.818  144.781 1.00 19.43 ?  159 ALA D CB    1 
ATOM   14648 N  N     . SER D 2 181 ? 140.531 97.240  143.047 1.00 18.49 ?  160 SER D N     1 
ATOM   14649 C  CA    . SER D 2 181 ? 140.461 97.963  141.776 1.00 18.51 ?  160 SER D CA    1 
ATOM   14650 C  C     . SER D 2 181 ? 140.858 99.433  141.915 1.00 18.23 ?  160 SER D C     1 
ATOM   14651 O  O     . SER D 2 181 ? 141.641 99.942  141.126 1.00 18.18 ?  160 SER D O     1 
ATOM   14652 C  CB    . SER D 2 181 ? 139.064 97.861  141.155 1.00 18.51 ?  160 SER D CB    1 
ATOM   14653 O  OG    . SER D 2 181 ? 139.088 98.422  139.857 1.00 19.42 ?  160 SER D OG    1 
ATOM   14654 N  N     . VAL D 2 182 ? 140.318 100.106 142.929 1.00 18.43 ?  161 VAL D N     1 
ATOM   14655 C  CA    . VAL D 2 182 ? 140.697 101.498 143.196 1.00 18.09 ?  161 VAL D CA    1 
ATOM   14656 C  C     . VAL D 2 182 ? 142.196 101.618 143.491 1.00 18.41 ?  161 VAL D C     1 
ATOM   14657 O  O     . VAL D 2 182 ? 142.858 102.530 142.991 1.00 18.52 ?  161 VAL D O     1 
ATOM   14658 C  CB    . VAL D 2 182 ? 139.856 102.116 144.320 1.00 17.71 ?  161 VAL D CB    1 
ATOM   14659 C  CG1   . VAL D 2 182 ? 140.412 103.502 144.727 1.00 16.02 ?  161 VAL D CG1   1 
ATOM   14660 C  CG2   . VAL D 2 182 ? 138.398 102.242 143.855 1.00 17.78 ?  161 VAL D CG2   1 
ATOM   14661 N  N     . TYR D 2 183 ? 142.736 100.673 144.262 1.00 19.06 ?  162 TYR D N     1 
ATOM   14662 C  CA    . TYR D 2 183 ? 144.167 100.690 144.545 1.00 19.73 ?  162 TYR D CA    1 
ATOM   14663 C  C     . TYR D 2 183 ? 144.990 100.536 143.274 1.00 19.90 ?  162 TYR D C     1 
ATOM   14664 O  O     . TYR D 2 183 ? 146.038 101.149 143.153 1.00 20.73 ?  162 TYR D O     1 
ATOM   14665 C  CB    . TYR D 2 183 ? 144.580 99.647  145.600 1.00 19.84 ?  162 TYR D CB    1 
ATOM   14666 C  CG    . TYR D 2 183 ? 144.163 99.990  147.015 1.00 20.24 ?  162 TYR D CG    1 
ATOM   14667 C  CD1   . TYR D 2 183 ? 143.703 101.263 147.343 1.00 21.51 ?  162 TYR D CD1   1 
ATOM   14668 C  CD2   . TYR D 2 183 ? 144.249 99.039  148.040 1.00 20.45 ?  162 TYR D CD2   1 
ATOM   14669 C  CE1   . TYR D 2 183 ? 143.324 101.580 148.654 1.00 21.68 ?  162 TYR D CE1   1 
ATOM   14670 C  CE2   . TYR D 2 183 ? 143.893 99.353  149.358 1.00 19.97 ?  162 TYR D CE2   1 
ATOM   14671 C  CZ    . TYR D 2 183 ? 143.427 100.623 149.653 1.00 21.83 ?  162 TYR D CZ    1 
ATOM   14672 O  OH    . TYR D 2 183 ? 143.063 100.944 150.946 1.00 21.96 ?  162 TYR D OH    1 
ATOM   14673 N  N     . LEU D 2 184 ? 144.518 99.743  142.321 1.00 20.22 ?  163 LEU D N     1 
ATOM   14674 C  CA    . LEU D 2 184 ? 145.244 99.604  141.062 1.00 20.89 ?  163 LEU D CA    1 
ATOM   14675 C  C     . LEU D 2 184 ? 145.146 100.902 140.247 1.00 20.72 ?  163 LEU D C     1 
ATOM   14676 O  O     . LEU D 2 184 ? 146.166 101.476 139.874 1.00 21.07 ?  163 LEU D O     1 
ATOM   14677 C  CB    . LEU D 2 184 ? 144.779 98.365  140.272 1.00 21.16 ?  163 LEU D CB    1 
ATOM   14678 C  CG    . LEU D 2 184 ? 145.402 98.076  138.890 1.00 22.77 ?  163 LEU D CG    1 
ATOM   14679 C  CD1   . LEU D 2 184 ? 146.946 98.070  138.918 1.00 22.44 ?  163 LEU D CD1   1 
ATOM   14680 C  CD2   . LEU D 2 184 ? 144.883 96.769  138.314 1.00 24.75 ?  163 LEU D CD2   1 
ATOM   14681 N  N     . GLU D 2 185 ? 143.923 101.374 140.018 1.00 20.65 ?  164 GLU D N     1 
ATOM   14682 C  CA    . GLU D 2 185 ? 143.666 102.573 139.206 1.00 20.69 ?  164 GLU D CA    1 
ATOM   14683 C  C     . GLU D 2 185 ? 144.301 103.854 139.748 1.00 20.64 ?  164 GLU D C     1 
ATOM   14684 O  O     . GLU D 2 185 ? 144.803 104.685 138.977 1.00 20.25 ?  164 GLU D O     1 
ATOM   14685 C  CB    . GLU D 2 185 ? 142.155 102.809 139.067 1.00 21.03 ?  164 GLU D CB    1 
ATOM   14686 C  CG    . GLU D 2 185 ? 141.376 101.654 138.431 1.00 22.19 ?  164 GLU D CG    1 
ATOM   14687 C  CD    . GLU D 2 185 ? 141.402 101.656 136.905 1.00 24.19 ?  164 GLU D CD    1 
ATOM   14688 O  OE1   . GLU D 2 185 ? 142.094 102.483 136.285 1.00 27.97 ?  164 GLU D OE1   1 
ATOM   14689 O  OE2   . GLU D 2 185 ? 140.703 100.836 136.309 1.00 25.47 -1 164 GLU D OE2   1 
ATOM   14690 N  N     . SER D 2 186 ? 144.247 104.025 141.065 1.00 20.42 ?  165 SER D N     1 
ATOM   14691 C  CA    . SER D 2 186 ? 144.585 105.303 141.689 1.00 20.70 ?  165 SER D CA    1 
ATOM   14692 C  C     . SER D 2 186 ? 145.900 105.292 142.467 1.00 20.88 ?  165 SER D C     1 
ATOM   14693 O  O     . SER D 2 186 ? 146.286 106.311 143.040 1.00 21.21 ?  165 SER D O     1 
ATOM   14694 C  CB    . SER D 2 186 ? 143.447 105.769 142.615 1.00 21.25 ?  165 SER D CB    1 
ATOM   14695 O  OG    . SER D 2 186 ? 142.191 105.773 141.951 1.00 20.97 ?  165 SER D OG    1 
ATOM   14696 N  N     . PHE D 2 187 ? 146.600 104.157 142.489 1.00 20.94 ?  166 PHE D N     1 
ATOM   14697 C  CA    . PHE D 2 187 ? 147.763 104.039 143.356 1.00 21.19 ?  166 PHE D CA    1 
ATOM   14698 C  C     . PHE D 2 187 ? 148.880 103.207 142.726 1.00 21.22 ?  166 PHE D C     1 
ATOM   14699 O  O     . PHE D 2 187 ? 149.962 103.747 142.470 1.00 21.10 ?  166 PHE D O     1 
ATOM   14700 C  CB    . PHE D 2 187 ? 147.324 103.565 144.770 1.00 21.63 ?  166 PHE D CB    1 
ATOM   14701 C  CG    . PHE D 2 187 ? 148.414 102.950 145.607 1.00 24.05 ?  166 PHE D CG    1 
ATOM   14702 C  CD1   . PHE D 2 187 ? 149.567 103.664 145.933 1.00 25.52 ?  166 PHE D CD1   1 
ATOM   14703 C  CD2   . PHE D 2 187 ? 148.262 101.663 146.117 1.00 27.03 ?  166 PHE D CD2   1 
ATOM   14704 C  CE1   . PHE D 2 187 ? 150.554 103.095 146.726 1.00 26.73 ?  166 PHE D CE1   1 
ATOM   14705 C  CE2   . PHE D 2 187 ? 149.263 101.082 146.910 1.00 27.36 ?  166 PHE D CE2   1 
ATOM   14706 C  CZ    . PHE D 2 187 ? 150.403 101.800 147.207 1.00 27.87 ?  166 PHE D CZ    1 
ATOM   14707 N  N     . LEU D 2 188 ? 148.610 101.939 142.427 1.00 20.78 ?  167 LEU D N     1 
ATOM   14708 C  CA    . LEU D 2 188 ? 149.654 101.020 141.930 1.00 21.78 ?  167 LEU D CA    1 
ATOM   14709 C  C     . LEU D 2 188 ? 150.266 101.402 140.576 1.00 21.91 ?  167 LEU D C     1 
ATOM   14710 O  O     . LEU D 2 188 ? 151.444 101.138 140.340 1.00 22.87 ?  167 LEU D O     1 
ATOM   14711 C  CB    . LEU D 2 188 ? 149.136 99.584  141.867 1.00 22.32 ?  167 LEU D CB    1 
ATOM   14712 C  CG    . LEU D 2 188 ? 148.792 98.831  143.152 1.00 23.33 ?  167 LEU D CG    1 
ATOM   14713 C  CD1   . LEU D 2 188 ? 148.283 97.448  142.784 1.00 22.43 ?  167 LEU D CD1   1 
ATOM   14714 C  CD2   . LEU D 2 188 ? 149.980 98.731  144.118 1.00 25.71 ?  167 LEU D CD2   1 
ATOM   14715 N  N     . PHE D 2 189 ? 149.468 101.999 139.688 1.00 21.56 ?  168 PHE D N     1 
ATOM   14716 C  CA    . PHE D 2 189 ? 149.966 102.473 138.394 1.00 21.86 ?  168 PHE D CA    1 
ATOM   14717 C  C     . PHE D 2 189 ? 151.017 103.594 138.533 1.00 21.87 ?  168 PHE D C     1 
ATOM   14718 O  O     . PHE D 2 189 ? 151.831 103.809 137.631 1.00 21.79 ?  168 PHE D O     1 
ATOM   14719 C  CB    . PHE D 2 189 ? 148.817 103.016 137.523 1.00 21.79 ?  168 PHE D CB    1 
ATOM   14720 C  CG    . PHE D 2 189 ? 147.997 101.954 136.827 1.00 21.88 ?  168 PHE D CG    1 
ATOM   14721 C  CD1   . PHE D 2 189 ? 148.593 100.812 136.287 1.00 21.44 ?  168 PHE D CD1   1 
ATOM   14722 C  CD2   . PHE D 2 189 ? 146.620 102.124 136.683 1.00 22.82 ?  168 PHE D CD2   1 
ATOM   14723 C  CE1   . PHE D 2 189 ? 147.822 99.839  135.638 1.00 22.35 ?  168 PHE D CE1   1 
ATOM   14724 C  CE2   . PHE D 2 189 ? 145.837 101.167 136.037 1.00 22.08 ?  168 PHE D CE2   1 
ATOM   14725 C  CZ    . PHE D 2 189 ? 146.436 100.014 135.522 1.00 22.60 ?  168 PHE D CZ    1 
ATOM   14726 N  N     . TYR D 2 190 ? 150.986 104.322 139.645 1.00 21.91 ?  169 TYR D N     1 
ATOM   14727 C  CA    . TYR D 2 190 ? 151.734 105.585 139.720 1.00 22.52 ?  169 TYR D CA    1 
ATOM   14728 C  C     . TYR D 2 190 ? 153.244 105.460 139.931 1.00 22.75 ?  169 TYR D C     1 
ATOM   14729 O  O     . TYR D 2 190 ? 153.979 106.348 139.521 1.00 21.93 ?  169 TYR D O     1 
ATOM   14730 C  CB    . TYR D 2 190 ? 151.078 106.573 140.689 1.00 22.67 ?  169 TYR D CB    1 
ATOM   14731 C  CG    . TYR D 2 190 ? 149.842 107.190 140.067 1.00 24.77 ?  169 TYR D CG    1 
ATOM   14732 C  CD1   . TYR D 2 190 ? 148.651 106.464 139.960 1.00 25.65 ?  169 TYR D CD1   1 
ATOM   14733 C  CD2   . TYR D 2 190 ? 149.877 108.479 139.542 1.00 25.94 ?  169 TYR D CD2   1 
ATOM   14734 C  CE1   . TYR D 2 190 ? 147.520 107.023 139.355 1.00 26.62 ?  169 TYR D CE1   1 
ATOM   14735 C  CE2   . TYR D 2 190 ? 148.752 109.051 138.953 1.00 26.91 ?  169 TYR D CE2   1 
ATOM   14736 C  CZ    . TYR D 2 190 ? 147.582 108.321 138.860 1.00 27.39 ?  169 TYR D CZ    1 
ATOM   14737 O  OH    . TYR D 2 190 ? 146.479 108.904 138.265 1.00 27.50 ?  169 TYR D OH    1 
ATOM   14738 N  N     . SER D 2 191 ? 153.704 104.356 140.529 1.00 22.74 ?  170 SER D N     1 
ATOM   14739 C  CA    . SER D 2 191 ? 155.144 104.073 140.559 1.00 23.43 ?  170 SER D CA    1 
ATOM   14740 C  C     . SER D 2 191 ? 155.656 103.926 139.126 1.00 23.08 ?  170 SER D C     1 
ATOM   14741 O  O     . SER D 2 191 ? 156.802 104.223 138.837 1.00 23.67 ?  170 SER D O     1 
ATOM   14742 C  CB    . SER D 2 191 ? 155.469 102.815 141.380 1.00 23.39 ?  170 SER D CB    1 
ATOM   14743 O  OG    . SER D 2 191 ? 154.855 101.659 140.828 1.00 24.10 ?  170 SER D OG    1 
ATOM   14744 N  N     . GLY D 2 192 ? 154.775 103.500 138.230 1.00 22.82 ?  171 GLY D N     1 
ATOM   14745 C  CA    . GLY D 2 192 ? 155.091 103.367 136.813 1.00 22.08 ?  171 GLY D CA    1 
ATOM   14746 C  C     . GLY D 2 192 ? 154.928 104.659 136.029 1.00 22.12 ?  171 GLY D C     1 
ATOM   14747 O  O     . GLY D 2 192 ? 155.837 105.057 135.298 1.00 22.86 ?  171 GLY D O     1 
ATOM   14748 N  N     . PHE D 2 193 ? 153.780 105.317 136.180 1.00 21.48 ?  172 PHE D N     1 
ATOM   14749 C  CA    . PHE D 2 193 ? 153.506 106.591 135.489 1.00 21.06 ?  172 PHE D CA    1 
ATOM   14750 C  C     . PHE D 2 193 ? 154.584 107.643 135.754 1.00 21.13 ?  172 PHE D C     1 
ATOM   14751 O  O     . PHE D 2 193 ? 154.823 108.506 134.909 1.00 21.18 ?  172 PHE D O     1 
ATOM   14752 C  CB    . PHE D 2 193 ? 152.157 107.169 135.912 1.00 21.33 ?  172 PHE D CB    1 
ATOM   14753 C  CG    . PHE D 2 193 ? 150.956 106.424 135.377 1.00 20.93 ?  172 PHE D CG    1 
ATOM   14754 C  CD1   . PHE D 2 193 ? 151.000 105.751 134.157 1.00 20.88 ?  172 PHE D CD1   1 
ATOM   14755 C  CD2   . PHE D 2 193 ? 149.761 106.447 136.083 1.00 19.83 ?  172 PHE D CD2   1 
ATOM   14756 C  CE1   . PHE D 2 193 ? 149.868 105.083 133.672 1.00 22.31 ?  172 PHE D CE1   1 
ATOM   14757 C  CE2   . PHE D 2 193 ? 148.622 105.793 135.599 1.00 20.67 ?  172 PHE D CE2   1 
ATOM   14758 C  CZ    . PHE D 2 193 ? 148.678 105.111 134.393 1.00 21.00 ?  172 PHE D CZ    1 
ATOM   14759 N  N     . TYR D 2 194 ? 155.235 107.558 136.915 1.00 20.48 ?  173 TYR D N     1 
ATOM   14760 C  CA    . TYR D 2 194 ? 156.245 108.537 137.310 1.00 20.76 ?  173 TYR D CA    1 
ATOM   14761 C  C     . TYR D 2 194 ? 157.253 108.810 136.187 1.00 20.53 ?  173 TYR D C     1 
ATOM   14762 O  O     . TYR D 2 194 ? 157.521 109.960 135.829 1.00 19.89 ?  173 TYR D O     1 
ATOM   14763 C  CB    . TYR D 2 194 ? 156.984 108.095 138.598 1.00 20.94 ?  173 TYR D CB    1 
ATOM   14764 C  CG    . TYR D 2 194 ? 157.874 109.187 139.163 1.00 21.56 ?  173 TYR D CG    1 
ATOM   14765 C  CD1   . TYR D 2 194 ? 157.444 109.984 140.227 1.00 22.23 ?  173 TYR D CD1   1 
ATOM   14766 C  CD2   . TYR D 2 194 ? 159.138 109.442 138.617 1.00 22.00 ?  173 TYR D CD2   1 
ATOM   14767 C  CE1   . TYR D 2 194 ? 158.249 111.004 140.733 1.00 21.58 ?  173 TYR D CE1   1 
ATOM   14768 C  CE2   . TYR D 2 194 ? 159.944 110.447 139.118 1.00 20.52 ?  173 TYR D CE2   1 
ATOM   14769 C  CZ    . TYR D 2 194 ? 159.496 111.225 140.172 1.00 21.66 ?  173 TYR D CZ    1 
ATOM   14770 O  OH    . TYR D 2 194 ? 160.289 112.240 140.651 1.00 21.37 ?  173 TYR D OH    1 
ATOM   14771 N  N     . TYR D 2 195 ? 157.787 107.745 135.613 1.00 20.77 ?  174 TYR D N     1 
ATOM   14772 C  CA    . TYR D 2 195 ? 158.903 107.895 134.695 1.00 21.12 ?  174 TYR D CA    1 
ATOM   14773 C  C     . TYR D 2 195 ? 158.517 108.585 133.374 1.00 21.49 ?  174 TYR D C     1 
ATOM   14774 O  O     . TYR D 2 195 ? 159.171 109.560 132.994 1.00 21.60 ?  174 TYR D O     1 
ATOM   14775 C  CB    . TYR D 2 195 ? 159.619 106.555 134.503 1.00 21.23 ?  174 TYR D CB    1 
ATOM   14776 C  CG    . TYR D 2 195 ? 161.098 106.659 134.205 1.00 21.77 ?  174 TYR D CG    1 
ATOM   14777 C  CD1   . TYR D 2 195 ? 161.901 107.620 134.828 1.00 23.28 ?  174 TYR D CD1   1 
ATOM   14778 C  CD2   . TYR D 2 195 ? 161.702 105.775 133.313 1.00 22.87 ?  174 TYR D CD2   1 
ATOM   14779 C  CE1   . TYR D 2 195 ? 163.273 107.701 134.547 1.00 23.81 ?  174 TYR D CE1   1 
ATOM   14780 C  CE2   . TYR D 2 195 ? 163.066 105.844 133.038 1.00 24.09 ?  174 TYR D CE2   1 
ATOM   14781 C  CZ    . TYR D 2 195 ? 163.840 106.808 133.650 1.00 23.51 ?  174 TYR D CZ    1 
ATOM   14782 O  OH    . TYR D 2 195 ? 165.190 106.878 133.365 1.00 25.36 ?  174 TYR D OH    1 
ATOM   14783 N  N     . PRO D 2 196 ? 157.457 108.100 132.677 1.00 21.86 ?  175 PRO D N     1 
ATOM   14784 C  CA    . PRO D 2 196 ? 156.993 108.817 131.479 1.00 22.03 ?  175 PRO D CA    1 
ATOM   14785 C  C     . PRO D 2 196 ? 156.635 110.276 131.759 1.00 22.18 ?  175 PRO D C     1 
ATOM   14786 O  O     . PRO D 2 196 ? 156.924 111.137 130.924 1.00 23.00 ?  175 PRO D O     1 
ATOM   14787 C  CB    . PRO D 2 196 ? 155.733 108.050 131.055 1.00 21.50 ?  175 PRO D CB    1 
ATOM   14788 C  CG    . PRO D 2 196 ? 155.857 106.735 131.647 1.00 22.47 ?  175 PRO D CG    1 
ATOM   14789 C  CD    . PRO D 2 196 ? 156.797 106.789 132.815 1.00 20.91 ?  175 PRO D CD    1 
ATOM   14790 N  N     . LEU D 2 197 ? 156.028 110.553 132.915 1.00 21.70 ?  176 LEU D N     1 
ATOM   14791 C  CA    . LEU D 2 197 ? 155.719 111.936 133.306 1.00 22.40 ?  176 LEU D CA    1 
ATOM   14792 C  C     . LEU D 2 197 ? 156.978 112.770 133.555 1.00 22.58 ?  176 LEU D C     1 
ATOM   14793 O  O     . LEU D 2 197 ? 157.018 113.962 133.223 1.00 22.15 ?  176 LEU D O     1 
ATOM   14794 C  CB    . LEU D 2 197 ? 154.845 111.972 134.553 1.00 22.15 ?  176 LEU D CB    1 
ATOM   14795 C  CG    . LEU D 2 197 ? 153.380 111.525 134.458 1.00 23.08 ?  176 LEU D CG    1 
ATOM   14796 C  CD1   . LEU D 2 197 ? 152.854 111.312 135.867 1.00 21.62 ?  176 LEU D CD1   1 
ATOM   14797 C  CD2   . LEU D 2 197 ? 152.530 112.560 133.693 1.00 21.94 ?  176 LEU D CD2   1 
ATOM   14798 N  N     . TYR D 2 198 ? 157.988 112.128 134.148 1.00 22.76 ?  177 TYR D N     1 
ATOM   14799 C  CA    . TYR D 2 198 ? 159.300 112.733 134.383 1.00 23.23 ?  177 TYR D CA    1 
ATOM   14800 C  C     . TYR D 2 198 ? 159.965 113.138 133.067 1.00 23.91 ?  177 TYR D C     1 
ATOM   14801 O  O     . TYR D 2 198 ? 160.463 114.266 132.940 1.00 24.20 ?  177 TYR D O     1 
ATOM   14802 C  CB    . TYR D 2 198 ? 160.188 111.773 135.193 1.00 23.19 ?  177 TYR D CB    1 
ATOM   14803 C  CG    . TYR D 2 198 ? 161.569 112.289 135.548 1.00 23.52 ?  177 TYR D CG    1 
ATOM   14804 C  CD1   . TYR D 2 198 ? 161.732 113.351 136.426 1.00 24.85 ?  177 TYR D CD1   1 
ATOM   14805 C  CD2   . TYR D 2 198 ? 162.719 111.677 135.032 1.00 25.30 ?  177 TYR D CD2   1 
ATOM   14806 C  CE1   . TYR D 2 198 ? 163.004 113.817 136.772 1.00 26.05 ?  177 TYR D CE1   1 
ATOM   14807 C  CE2   . TYR D 2 198 ? 164.002 112.135 135.376 1.00 26.38 ?  177 TYR D CE2   1 
ATOM   14808 C  CZ    . TYR D 2 198 ? 164.127 113.202 136.245 1.00 26.68 ?  177 TYR D CZ    1 
ATOM   14809 O  OH    . TYR D 2 198 ? 165.374 113.669 136.601 1.00 30.01 ?  177 TYR D OH    1 
ATOM   14810 N  N     . PHE D 2 199 ? 159.967 112.239 132.082 1.00 24.84 ?  178 PHE D N     1 
ATOM   14811 C  CA    . PHE D 2 199 ? 160.469 112.601 130.752 1.00 25.81 ?  178 PHE D CA    1 
ATOM   14812 C  C     . PHE D 2 199 ? 159.626 113.670 130.067 1.00 26.23 ?  178 PHE D C     1 
ATOM   14813 O  O     . PHE D 2 199 ? 160.165 114.625 129.507 1.00 26.58 ?  178 PHE D O     1 
ATOM   14814 C  CB    . PHE D 2 199 ? 160.604 111.378 129.856 1.00 26.08 ?  178 PHE D CB    1 
ATOM   14815 C  CG    . PHE D 2 199 ? 161.793 110.525 130.183 1.00 28.71 ?  178 PHE D CG    1 
ATOM   14816 C  CD1   . PHE D 2 199 ? 163.039 111.099 130.399 1.00 32.03 ?  178 PHE D CD1   1 
ATOM   14817 C  CD2   . PHE D 2 199 ? 161.673 109.149 130.283 1.00 31.77 ?  178 PHE D CD2   1 
ATOM   14818 C  CE1   . PHE D 2 199 ? 164.156 110.312 130.719 1.00 32.29 ?  178 PHE D CE1   1 
ATOM   14819 C  CE2   . PHE D 2 199 ? 162.784 108.357 130.592 1.00 32.72 ?  178 PHE D CE2   1 
ATOM   14820 C  CZ    . PHE D 2 199 ? 164.024 108.946 130.808 1.00 31.91 ?  178 PHE D CZ    1 
ATOM   14821 N  N     . TYR D 2 200 ? 158.309 113.490 130.124 1.00 26.46 ?  179 TYR D N     1 
ATOM   14822 C  CA    . TYR D 2 200 ? 157.327 114.400 129.514 1.00 27.43 ?  179 TYR D CA    1 
ATOM   14823 C  C     . TYR D 2 200 ? 157.500 115.821 130.040 1.00 27.68 ?  179 TYR D C     1 
ATOM   14824 O  O     . TYR D 2 200 ? 157.407 116.784 129.280 1.00 28.71 ?  179 TYR D O     1 
ATOM   14825 C  CB    . TYR D 2 200 ? 155.930 113.887 129.847 1.00 27.27 ?  179 TYR D CB    1 
ATOM   14826 C  CG    . TYR D 2 200 ? 154.778 114.408 129.024 1.00 28.90 ?  179 TYR D CG    1 
ATOM   14827 C  CD1   . TYR D 2 200 ? 154.836 114.445 127.637 1.00 29.00 ?  179 TYR D CD1   1 
ATOM   14828 C  CD2   . TYR D 2 200 ? 153.591 114.801 129.649 1.00 30.14 ?  179 TYR D CD2   1 
ATOM   14829 C  CE1   . TYR D 2 200 ? 153.754 114.898 126.886 1.00 31.26 ?  179 TYR D CE1   1 
ATOM   14830 C  CE2   . TYR D 2 200 ? 152.504 115.244 128.913 1.00 31.86 ?  179 TYR D CE2   1 
ATOM   14831 C  CZ    . TYR D 2 200 ? 152.592 115.296 127.532 1.00 32.51 ?  179 TYR D CZ    1 
ATOM   14832 O  OH    . TYR D 2 200 ? 151.515 115.738 126.803 1.00 33.77 ?  179 TYR D OH    1 
ATOM   14833 N  N     . GLY D 2 201 ? 157.758 115.944 131.341 1.00 27.68 ?  180 GLY D N     1 
ATOM   14834 C  CA    . GLY D 2 201 ? 158.007 117.239 131.965 1.00 28.02 ?  180 GLY D CA    1 
ATOM   14835 C  C     . GLY D 2 201 ? 159.334 117.892 131.591 1.00 28.60 ?  180 GLY D C     1 
ATOM   14836 O  O     . GLY D 2 201 ? 159.524 119.074 131.850 1.00 28.44 ?  180 GLY D O     1 
ATOM   14837 N  N     . GLN D 2 202 ? 160.247 117.113 131.003 1.00 29.34 ?  181 GLN D N     1 
ATOM   14838 C  CA    . GLN D 2 202 ? 161.573 117.580 130.561 1.00 30.39 ?  181 GLN D CA    1 
ATOM   14839 C  C     . GLN D 2 202 ? 161.665 117.815 129.053 1.00 30.55 ?  181 GLN D C     1 
ATOM   14840 O  O     . GLN D 2 202 ? 162.720 118.222 128.555 1.00 31.23 ?  181 GLN D O     1 
ATOM   14841 C  CB    . GLN D 2 202 ? 162.636 116.519 130.852 1.00 30.31 ?  181 GLN D CB    1 
ATOM   14842 C  CG    . GLN D 2 202 ? 162.971 116.236 132.267 1.00 32.40 ?  181 GLN D CG    1 
ATOM   14843 C  CD    . GLN D 2 202 ? 164.031 115.157 132.349 1.00 33.85 ?  181 GLN D CD    1 
ATOM   14844 O  OE1   . GLN D 2 202 ? 163.746 114.011 132.690 1.00 33.94 ?  181 GLN D OE1   1 
ATOM   14845 N  NE2   . GLN D 2 202 ? 165.254 115.508 131.990 1.00 34.92 ?  181 GLN D NE2   1 
ATOM   14846 N  N     . GLY D 2 203 ? 160.606 117.496 128.317 1.00 30.57 ?  182 GLY D N     1 
ATOM   14847 C  CA    . GLY D 2 203 ? 160.627 117.621 126.858 1.00 30.83 ?  182 GLY D CA    1 
ATOM   14848 C  C     . GLY D 2 203 ? 161.129 116.382 126.133 1.00 30.80 ?  182 GLY D C     1 
ATOM   14849 O  O     . GLY D 2 203 ? 161.385 116.426 124.926 1.00 30.86 ?  182 GLY D O     1 
ATOM   14850 N  N     . LYS D 2 204 ? 161.264 115.274 126.863 1.00 30.14 ?  183 LYS D N     1 
ATOM   14851 C  CA    . LYS D 2 204 ? 161.705 114.005 126.278 1.00 30.35 ?  183 LYS D CA    1 
ATOM   14852 C  C     . LYS D 2 204 ? 160.544 113.029 126.096 1.00 29.52 ?  183 LYS D C     1 
ATOM   14853 O  O     . LYS D 2 204 ? 159.614 113.017 126.899 1.00 28.60 ?  183 LYS D O     1 
ATOM   14854 C  CB    . LYS D 2 204 ? 162.795 113.371 127.140 1.00 30.76 ?  183 LYS D CB    1 
ATOM   14855 C  CG    . LYS D 2 204 ? 164.094 114.183 127.179 1.00 32.95 ?  183 LYS D CG    1 
ATOM   14856 C  CD    . LYS D 2 204 ? 165.003 113.651 128.261 1.00 36.37 ?  183 LYS D CD    1 
ATOM   14857 C  CE    . LYS D 2 204 ? 166.308 114.422 128.342 1.00 38.47 ?  183 LYS D CE    1 
ATOM   14858 N  NZ    . LYS D 2 204 ? 167.024 114.000 129.583 1.00 40.21 1  183 LYS D NZ    1 
ATOM   14859 N  N     . LEU D 2 205 ? 160.615 112.211 125.043 1.00 29.47 ?  184 LEU D N     1 
ATOM   14860 C  CA    . LEU D 2 205 ? 159.574 111.222 124.722 1.00 29.06 ?  184 LEU D CA    1 
ATOM   14861 C  C     . LEU D 2 205 ? 158.156 111.810 124.883 1.00 28.96 ?  184 LEU D C     1 
ATOM   14862 O  O     . LEU D 2 205 ? 157.308 111.274 125.606 1.00 27.68 ?  184 LEU D O     1 
ATOM   14863 C  CB    . LEU D 2 205 ? 159.750 109.944 125.557 1.00 28.63 ?  184 LEU D CB    1 
ATOM   14864 C  CG    . LEU D 2 205 ? 161.098 109.210 125.475 1.00 29.00 ?  184 LEU D CG    1 
ATOM   14865 C  CD1   . LEU D 2 205 ? 161.110 108.015 126.430 1.00 28.90 ?  184 LEU D CD1   1 
ATOM   14866 C  CD2   . LEU D 2 205 ? 161.399 108.751 124.054 1.00 28.67 ?  184 LEU D CD2   1 
ATOM   14867 N  N     . MET D 2 206 ? 157.936 112.920 124.185 1.00 29.02 ?  185 MET D N     1 
ATOM   14868 C  CA    . MET D 2 206 ? 156.707 113.695 124.256 1.00 29.72 ?  185 MET D CA    1 
ATOM   14869 C  C     . MET D 2 206 ? 155.469 113.021 123.671 1.00 29.54 ?  185 MET D C     1 
ATOM   14870 O  O     . MET D 2 206 ? 154.366 113.246 124.161 1.00 29.47 ?  185 MET D O     1 
ATOM   14871 C  CB    . MET D 2 206 ? 156.916 115.059 123.586 1.00 30.69 ?  185 MET D CB    1 
ATOM   14872 C  CG    . MET D 2 206 ? 158.037 115.866 124.223 1.00 32.03 ?  185 MET D CG    1 
ATOM   14873 S  SD    . MET D 2 206 ? 157.727 116.153 125.975 1.00 36.63 ?  185 MET D SD    1 
ATOM   14874 C  CE    . MET D 2 206 ? 156.690 117.602 125.889 1.00 33.80 ?  185 MET D CE    1 
ATOM   14875 N  N     . GLN D 2 207 ? 155.648 112.226 122.617 1.00 29.56 ?  186 GLN D N     1 
ATOM   14876 C  CA    . GLN D 2 207 ? 154.523 111.551 121.960 1.00 29.17 ?  186 GLN D CA    1 
ATOM   14877 C  C     . GLN D 2 207 ? 153.991 110.420 122.835 1.00 28.26 ?  186 GLN D C     1 
ATOM   14878 O  O     . GLN D 2 207 ? 152.785 110.316 123.045 1.00 27.98 ?  186 GLN D O     1 
ATOM   14879 C  CB    . GLN D 2 207 ? 154.918 111.019 120.573 1.00 29.80 ?  186 GLN D CB    1 
ATOM   14880 C  CG    . GLN D 2 207 ? 155.519 112.066 119.636 1.00 31.75 ?  186 GLN D CG    1 
ATOM   14881 C  CD    . GLN D 2 207 ? 154.650 113.302 119.526 1.00 34.93 ?  186 GLN D CD    1 
ATOM   14882 O  OE1   . GLN D 2 207 ? 153.570 113.274 118.922 1.00 36.91 ?  186 GLN D OE1   1 
ATOM   14883 N  NE2   . GLN D 2 207 ? 155.111 114.396 120.121 1.00 36.09 ?  186 GLN D NE2   1 
ATOM   14884 N  N     . SER D 2 208 ? 154.887 109.579 123.345 0.50 27.75 ?  187 SER D N     1 
ATOM   14885 C  CA    . SER D 2 208 ? 154.484 108.498 124.237 0.50 27.12 ?  187 SER D CA    1 
ATOM   14886 C  C     . SER D 2 208 ? 154.025 109.052 125.584 0.50 26.72 ?  187 SER D C     1 
ATOM   14887 O  O     . SER D 2 208 ? 153.141 108.475 126.216 0.50 26.30 ?  187 SER D O     1 
ATOM   14888 C  CB    . SER D 2 208 ? 155.610 107.481 124.425 0.50 26.88 ?  187 SER D CB    1 
ATOM   14889 O  OG    . SER D 2 208 ? 156.806 108.127 124.805 0.50 26.59 ?  187 SER D OG    1 
ATOM   14890 N  N     . GLY D 2 209 ? 154.624 110.165 126.008 1.00 26.64 ?  188 GLY D N     1 
ATOM   14891 C  CA    . GLY D 2 209 ? 154.208 110.862 127.242 1.00 26.43 ?  188 GLY D CA    1 
ATOM   14892 C  C     . GLY D 2 209 ? 152.800 111.434 127.144 1.00 26.66 ?  188 GLY D C     1 
ATOM   14893 O  O     . GLY D 2 209 ? 152.049 111.440 128.120 1.00 26.57 ?  188 GLY D O     1 
ATOM   14894 N  N     . GLU D 2 210 ? 152.438 111.925 125.962 1.00 27.42 ?  189 GLU D N     1 
ATOM   14895 C  CA    . GLU D 2 210 ? 151.077 112.397 125.716 1.00 27.73 ?  189 GLU D CA    1 
ATOM   14896 C  C     . GLU D 2 210 ? 150.091 111.224 125.818 1.00 27.04 ?  189 GLU D C     1 
ATOM   14897 O  O     . GLU D 2 210 ? 149.053 111.330 126.472 1.00 26.57 ?  189 GLU D O     1 
ATOM   14898 C  CB    . GLU D 2 210 ? 150.969 113.103 124.352 1.00 28.28 ?  189 GLU D CB    1 
ATOM   14899 C  CG    . GLU D 2 210 ? 149.582 113.707 124.083 1.00 30.71 ?  189 GLU D CG    1 
ATOM   14900 C  CD    . GLU D 2 210 ? 149.523 114.631 122.868 1.00 35.43 ?  189 GLU D CD    1 
ATOM   14901 O  OE1   . GLU D 2 210 ? 150.511 114.715 122.097 1.00 36.89 ?  189 GLU D OE1   1 
ATOM   14902 O  OE2   . GLU D 2 210 ? 148.472 115.289 122.694 1.00 37.04 -1 189 GLU D OE2   1 
ATOM   14903 N  N     . ILE D 2 211 ? 150.431 110.107 125.182 1.00 26.80 ?  190 ILE D N     1 
ATOM   14904 C  CA    . ILE D 2 211 ? 149.631 108.891 125.294 1.00 26.92 ?  190 ILE D CA    1 
ATOM   14905 C  C     . ILE D 2 211 ? 149.470 108.470 126.748 1.00 26.45 ?  190 ILE D C     1 
ATOM   14906 O  O     . ILE D 2 211 ? 148.355 108.188 127.183 1.00 26.65 ?  190 ILE D O     1 
ATOM   14907 C  CB    . ILE D 2 211 ? 150.204 107.734 124.435 1.00 27.00 ?  190 ILE D CB    1 
ATOM   14908 C  CG1   . ILE D 2 211 ? 149.998 108.048 122.948 1.00 28.77 ?  190 ILE D CG1   1 
ATOM   14909 C  CG2   . ILE D 2 211 ? 149.528 106.400 124.795 1.00 26.82 ?  190 ILE D CG2   1 
ATOM   14910 C  CD1   . ILE D 2 211 ? 150.653 107.065 121.987 1.00 30.88 ?  190 ILE D CD1   1 
ATOM   14911 N  N     . ILE D 2 212 ? 150.568 108.455 127.508 1.00 26.49 ?  191 ILE D N     1 
ATOM   14912 C  CA    . ILE D 2 212 ? 150.513 108.019 128.904 1.00 25.73 ?  191 ILE D CA    1 
ATOM   14913 C  C     . ILE D 2 212 ? 149.619 108.947 129.729 1.00 25.48 ?  191 ILE D C     1 
ATOM   14914 O  O     . ILE D 2 212 ? 148.855 108.489 130.584 1.00 24.95 ?  191 ILE D O     1 
ATOM   14915 C  CB    . ILE D 2 212 ? 151.929 107.887 129.543 1.00 26.44 ?  191 ILE D CB    1 
ATOM   14916 C  CG1   . ILE D 2 212 ? 152.730 106.768 128.864 1.00 26.71 ?  191 ILE D CG1   1 
ATOM   14917 C  CG2   . ILE D 2 212 ? 151.834 107.652 131.066 1.00 26.01 ?  191 ILE D CG2   1 
ATOM   14918 C  CD1   . ILE D 2 212 ? 152.153 105.370 128.986 1.00 30.50 ?  191 ILE D CD1   1 
ATOM   14919 N  N     . ASN D 2 213 ? 149.700 110.244 129.447 1.00 24.79 ?  192 ASN D N     1 
ATOM   14920 C  CA    . ASN D 2 213 ? 148.871 111.223 130.135 1.00 24.80 ?  192 ASN D CA    1 
ATOM   14921 C  C     . ASN D 2 213 ? 147.364 111.006 129.881 1.00 24.44 ?  192 ASN D C     1 
ATOM   14922 O  O     . ASN D 2 213 ? 146.536 111.233 130.771 1.00 23.25 ?  192 ASN D O     1 
ATOM   14923 C  CB    . ASN D 2 213 ? 149.300 112.640 129.750 1.00 25.68 ?  192 ASN D CB    1 
ATOM   14924 C  CG    . ASN D 2 213 ? 149.226 113.610 130.914 1.00 27.89 ?  192 ASN D CG    1 
ATOM   14925 O  OD1   . ASN D 2 213 ? 149.401 113.234 132.070 1.00 31.05 ?  192 ASN D OD1   1 
ATOM   14926 N  ND2   . ASN D 2 213 ? 148.970 114.875 130.607 1.00 31.70 ?  192 ASN D ND2   1 
ATOM   14927 N  N     . LEU D 2 214 ? 147.020 110.554 128.675 1.00 23.60 ?  193 LEU D N     1 
ATOM   14928 C  CA    . LEU D 2 214 ? 145.623 110.271 128.340 1.00 23.84 ?  193 LEU D CA    1 
ATOM   14929 C  C     . LEU D 2 214 ? 145.155 109.019 129.059 1.00 23.48 ?  193 LEU D C     1 
ATOM   14930 O  O     . LEU D 2 214 ? 144.035 108.977 129.577 1.00 24.12 ?  193 LEU D O     1 
ATOM   14931 C  CB    . LEU D 2 214 ? 145.449 110.111 126.830 1.00 23.71 ?  193 LEU D CB    1 
ATOM   14932 C  CG    . LEU D 2 214 ? 145.524 111.410 126.015 1.00 25.29 ?  193 LEU D CG    1 
ATOM   14933 C  CD1   . LEU D 2 214 ? 145.487 111.104 124.517 1.00 25.41 ?  193 LEU D CD1   1 
ATOM   14934 C  CD2   . LEU D 2 214 ? 144.407 112.371 126.387 1.00 25.80 ?  193 LEU D CD2   1 
ATOM   14935 N  N     . ILE D 2 215 ? 146.024 108.009 129.096 1.00 22.89 ?  194 ILE D N     1 
ATOM   14936 C  CA    . ILE D 2 215 ? 145.747 106.771 129.810 1.00 22.25 ?  194 ILE D CA    1 
ATOM   14937 C  C     . ILE D 2 215 ? 145.536 107.084 131.288 1.00 22.55 ?  194 ILE D C     1 
ATOM   14938 O  O     . ILE D 2 215 ? 144.533 106.672 131.888 1.00 22.53 ?  194 ILE D O     1 
ATOM   14939 C  CB    . ILE D 2 215 ? 146.892 105.750 129.654 1.00 22.37 ?  194 ILE D CB    1 
ATOM   14940 C  CG1   . ILE D 2 215 ? 146.987 105.274 128.198 1.00 21.89 ?  194 ILE D CG1   1 
ATOM   14941 C  CG2   . ILE D 2 215 ? 146.704 104.572 130.631 1.00 20.25 ?  194 ILE D CG2   1 
ATOM   14942 C  CD1   . ILE D 2 215 ? 148.109 104.262 127.934 1.00 20.48 ?  194 ILE D CD1   1 
ATOM   14943 N  N     . LEU D 2 216 ? 146.474 107.829 131.865 1.00 22.35 ?  195 LEU D N     1 
ATOM   14944 C  CA    . LEU D 2 216 ? 146.427 108.164 133.285 1.00 22.51 ?  195 LEU D CA    1 
ATOM   14945 C  C     . LEU D 2 216 ? 145.131 108.909 133.617 1.00 22.30 ?  195 LEU D C     1 
ATOM   14946 O  O     . LEU D 2 216 ? 144.508 108.639 134.651 1.00 21.62 ?  195 LEU D O     1 
ATOM   14947 C  CB    . LEU D 2 216 ? 147.658 109.007 133.656 1.00 23.06 ?  195 LEU D CB    1 
ATOM   14948 C  CG    . LEU D 2 216 ? 147.872 109.636 135.041 1.00 23.98 ?  195 LEU D CG    1 
ATOM   14949 C  CD1   . LEU D 2 216 ? 149.320 110.037 135.155 1.00 24.44 ?  195 LEU D CD1   1 
ATOM   14950 C  CD2   . LEU D 2 216 ? 146.976 110.865 135.271 1.00 25.00 ?  195 LEU D CD2   1 
ATOM   14951 N  N     . ARG D 2 217 ? 144.740 109.843 132.743 1.00 21.64 ?  196 ARG D N     1 
ATOM   14952 C  CA    . ARG D 2 217 ? 143.492 110.596 132.917 1.00 22.49 ?  196 ARG D CA    1 
ATOM   14953 C  C     . ARG D 2 217 ? 142.258 109.661 132.937 1.00 21.56 ?  196 ARG D C     1 
ATOM   14954 O  O     . ARG D 2 217 ? 141.343 109.875 133.720 1.00 21.32 ?  196 ARG D O     1 
ATOM   14955 C  CB    . ARG D 2 217 ? 143.341 111.714 131.867 1.00 23.07 ?  196 ARG D CB    1 
ATOM   14956 C  CG    . ARG D 2 217 ? 142.136 112.648 132.111 1.00 25.64 ?  196 ARG D CG    1 
ATOM   14957 C  CD    . ARG D 2 217 ? 141.873 113.614 130.940 1.00 32.11 ?  196 ARG D CD    1 
ATOM   14958 N  NE    . ARG D 2 217 ? 141.617 112.907 129.678 1.00 35.06 ?  196 ARG D NE    1 
ATOM   14959 C  CZ    . ARG D 2 217 ? 141.154 113.476 128.570 1.00 37.65 ?  196 ARG D CZ    1 
ATOM   14960 N  NH1   . ARG D 2 217 ? 140.861 114.772 128.551 1.00 40.20 1  196 ARG D NH1   1 
ATOM   14961 N  NH2   . ARG D 2 217 ? 140.969 112.744 127.474 1.00 38.20 ?  196 ARG D NH2   1 
ATOM   14962 N  N     . ASP D 2 218 ? 142.243 108.633 132.086 1.00 21.34 ?  197 ASP D N     1 
ATOM   14963 C  CA    . ASP D 2 218 ? 141.206 107.592 132.153 1.00 21.09 ?  197 ASP D CA    1 
ATOM   14964 C  C     . ASP D 2 218 ? 141.260 106.809 133.480 1.00 20.65 ?  197 ASP D C     1 
ATOM   14965 O  O     . ASP D 2 218 ? 140.224 106.605 134.118 1.00 20.16 ?  197 ASP D O     1 
ATOM   14966 C  CB    . ASP D 2 218 ? 141.312 106.614 130.973 1.00 21.58 ?  197 ASP D CB    1 
ATOM   14967 C  CG    . ASP D 2 218 ? 140.992 107.261 129.625 1.00 22.60 ?  197 ASP D CG    1 
ATOM   14968 O  OD1   . ASP D 2 218 ? 140.282 108.292 129.581 1.00 24.72 ?  197 ASP D OD1   1 
ATOM   14969 O  OD2   . ASP D 2 218 ? 141.473 106.728 128.598 1.00 22.64 -1 197 ASP D OD2   1 
ATOM   14970 N  N     . GLU D 2 219 ? 142.447 106.368 133.900 1.00 20.59 ?  198 GLU D N     1 
ATOM   14971 C  CA    . GLU D 2 219 ? 142.546 105.576 135.146 1.00 20.66 ?  198 GLU D CA    1 
ATOM   14972 C  C     . GLU D 2 219 ? 142.089 106.378 136.367 1.00 20.45 ?  198 GLU D C     1 
ATOM   14973 O  O     . GLU D 2 219 ? 141.472 105.824 137.282 1.00 20.59 ?  198 GLU D O     1 
ATOM   14974 C  CB    . GLU D 2 219 ? 143.958 105.011 135.377 1.00 20.55 ?  198 GLU D CB    1 
ATOM   14975 C  CG    . GLU D 2 219 ? 144.682 104.428 134.123 1.00 21.99 ?  198 GLU D CG    1 
ATOM   14976 C  CD    . GLU D 2 219 ? 143.976 103.247 133.445 1.00 24.00 ?  198 GLU D CD    1 
ATOM   14977 O  OE1   . GLU D 2 219 ? 142.743 103.078 133.562 1.00 25.06 ?  198 GLU D OE1   1 
ATOM   14978 O  OE2   . GLU D 2 219 ? 144.664 102.483 132.748 1.00 24.49 -1 198 GLU D OE2   1 
ATOM   14979 N  N     . ALA D 2 220 ? 142.377 107.677 136.368 1.00 20.47 ?  199 ALA D N     1 
ATOM   14980 C  CA    . ALA D 2 220 ? 141.919 108.576 137.449 1.00 21.10 ?  199 ALA D CA    1 
ATOM   14981 C  C     . ALA D 2 220 ? 140.402 108.553 137.609 1.00 21.34 ?  199 ALA D C     1 
ATOM   14982 O  O     . ALA D 2 220 ? 139.904 108.292 138.703 1.00 21.19 ?  199 ALA D O     1 
ATOM   14983 C  CB    . ALA D 2 220 ? 142.428 110.004 137.239 1.00 21.09 ?  199 ALA D CB    1 
ATOM   14984 N  N     . ILE D 2 221 ? 139.672 108.795 136.518 1.00 21.31 ?  200 ILE D N     1 
ATOM   14985 C  CA    . ILE D 2 221 ? 138.214 108.709 136.562 1.00 21.80 ?  200 ILE D CA    1 
ATOM   14986 C  C     . ILE D 2 221 ? 137.689 107.288 136.857 1.00 20.90 ?  200 ILE D C     1 
ATOM   14987 O  O     . ILE D 2 221 ? 136.695 107.137 137.566 1.00 20.54 ?  200 ILE D O     1 
ATOM   14988 C  CB    . ILE D 2 221 ? 137.526 109.361 135.328 1.00 22.75 ?  200 ILE D CB    1 
ATOM   14989 C  CG1   . ILE D 2 221 ? 136.052 109.608 135.634 1.00 24.63 ?  200 ILE D CG1   1 
ATOM   14990 C  CG2   . ILE D 2 221 ? 137.651 108.487 134.082 1.00 23.38 ?  200 ILE D CG2   1 
ATOM   14991 C  CD1   . ILE D 2 221 ? 135.419 110.661 134.773 1.00 26.91 ?  200 ILE D CD1   1 
ATOM   14992 N  N     . HIS D 2 222 ? 138.370 106.251 136.355 1.00 20.31 ?  201 HIS D N     1 
ATOM   14993 C  CA    . HIS D 2 222 ? 137.992 104.877 136.695 1.00 20.25 ?  201 HIS D CA    1 
ATOM   14994 C  C     . HIS D 2 222 ? 138.061 104.666 138.206 1.00 20.51 ?  201 HIS D C     1 
ATOM   14995 O  O     . HIS D 2 222 ? 137.109 104.168 138.819 1.00 20.99 ?  201 HIS D O     1 
ATOM   14996 C  CB    . HIS D 2 222 ? 138.872 103.839 135.987 1.00 19.79 ?  201 HIS D CB    1 
ATOM   14997 C  CG    . HIS D 2 222 ? 138.793 103.869 134.492 1.00 19.25 ?  201 HIS D CG    1 
ATOM   14998 N  ND1   . HIS D 2 222 ? 139.632 103.116 133.699 1.00 18.35 ?  201 HIS D ND1   1 
ATOM   14999 C  CD2   . HIS D 2 222 ? 137.992 104.562 133.643 1.00 17.64 ?  201 HIS D CD2   1 
ATOM   15000 C  CE1   . HIS D 2 222 ? 139.346 103.330 132.426 1.00 18.28 ?  201 HIS D CE1   1 
ATOM   15001 N  NE2   . HIS D 2 222 ? 138.361 104.210 132.364 1.00 20.01 ?  201 HIS D NE2   1 
ATOM   15002 N  N     . GLY D 2 223 ? 139.184 105.070 138.804 1.00 20.33 ?  202 GLY D N     1 
ATOM   15003 C  CA    . GLY D 2 223 ? 139.378 104.975 140.257 1.00 19.94 ?  202 GLY D CA    1 
ATOM   15004 C  C     . GLY D 2 223 ? 138.327 105.727 141.066 1.00 19.80 ?  202 GLY D C     1 
ATOM   15005 O  O     . GLY D 2 223 ? 137.799 105.193 142.040 1.00 19.96 ?  202 GLY D O     1 
ATOM   15006 N  N     . VAL D 2 224 ? 137.998 106.952 140.651 1.00 19.49 ?  203 VAL D N     1 
ATOM   15007 C  CA    . VAL D 2 224 ? 136.966 107.744 141.340 1.00 18.88 ?  203 VAL D CA    1 
ATOM   15008 C  C     . VAL D 2 224 ? 135.588 107.073 141.267 1.00 18.55 ?  203 VAL D C     1 
ATOM   15009 O  O     . VAL D 2 224 ? 134.866 106.987 142.274 1.00 17.65 ?  203 VAL D O     1 
ATOM   15010 C  CB    . VAL D 2 224 ? 136.890 109.221 140.803 1.00 19.22 ?  203 VAL D CB    1 
ATOM   15011 C  CG1   . VAL D 2 224 ? 135.781 110.013 141.524 1.00 18.51 ?  203 VAL D CG1   1 
ATOM   15012 C  CG2   . VAL D 2 224 ? 138.247 109.936 140.973 1.00 19.69 ?  203 VAL D CG2   1 
ATOM   15013 N  N     . TYR D 2 225 ? 135.240 106.576 140.082 1.00 18.17 ?  204 TYR D N     1 
ATOM   15014 C  CA    . TYR D 2 225 ? 133.941 105.939 139.854 1.00 18.76 ?  204 TYR D CA    1 
ATOM   15015 C  C     . TYR D 2 225 ? 133.785 104.643 140.668 1.00 18.93 ?  204 TYR D C     1 
ATOM   15016 O  O     . TYR D 2 225 ? 132.805 104.470 141.406 1.00 18.77 ?  204 TYR D O     1 
ATOM   15017 C  CB    . TYR D 2 225 ? 133.708 105.668 138.353 1.00 18.96 ?  204 TYR D CB    1 
ATOM   15018 C  CG    . TYR D 2 225 ? 132.307 105.131 138.084 1.00 20.06 ?  204 TYR D CG    1 
ATOM   15019 C  CD1   . TYR D 2 225 ? 131.182 105.938 138.300 1.00 21.79 ?  204 TYR D CD1   1 
ATOM   15020 C  CD2   . TYR D 2 225 ? 132.105 103.818 137.650 1.00 19.51 ?  204 TYR D CD2   1 
ATOM   15021 C  CE1   . TYR D 2 225 ? 129.891 105.451 138.085 1.00 20.38 ?  204 TYR D CE1   1 
ATOM   15022 C  CE2   . TYR D 2 225 ? 130.803 103.319 137.425 1.00 19.38 ?  204 TYR D CE2   1 
ATOM   15023 C  CZ    . TYR D 2 225 ? 129.709 104.149 137.652 1.00 20.84 ?  204 TYR D CZ    1 
ATOM   15024 O  OH    . TYR D 2 225 ? 128.424 103.692 137.457 1.00 20.77 ?  204 TYR D OH    1 
ATOM   15025 N  N     . VAL D 2 226 ? 134.753 103.737 140.541 1.00 18.76 ?  205 VAL D N     1 
ATOM   15026 C  CA    . VAL D 2 226 ? 134.711 102.493 141.305 1.00 18.85 ?  205 VAL D CA    1 
ATOM   15027 C  C     . VAL D 2 226 ? 134.713 102.799 142.802 1.00 19.19 ?  205 VAL D C     1 
ATOM   15028 O  O     . VAL D 2 226 ? 134.036 102.114 143.571 1.00 19.87 ?  205 VAL D O     1 
ATOM   15029 C  CB    . VAL D 2 226 ? 135.851 101.543 140.917 1.00 19.28 ?  205 VAL D CB    1 
ATOM   15030 C  CG1   . VAL D 2 226 ? 135.823 100.257 141.787 1.00 18.22 ?  205 VAL D CG1   1 
ATOM   15031 C  CG2   . VAL D 2 226 ? 135.731 101.200 139.423 1.00 18.40 ?  205 VAL D CG2   1 
ATOM   15032 N  N     . GLY D 2 227 ? 135.446 103.842 143.197 1.00 18.53 ?  206 GLY D N     1 
ATOM   15033 C  CA    . GLY D 2 227 ? 135.437 104.322 144.591 1.00 18.74 ?  206 GLY D CA    1 
ATOM   15034 C  C     . GLY D 2 227 ? 134.059 104.688 145.115 1.00 19.17 ?  206 GLY D C     1 
ATOM   15035 O  O     . GLY D 2 227 ? 133.717 104.386 146.267 1.00 18.66 ?  206 GLY D O     1 
ATOM   15036 N  N     . LEU D 2 228 ? 133.268 105.357 144.279 1.00 19.00 ?  207 LEU D N     1 
ATOM   15037 C  CA    . LEU D 2 228 ? 131.903 105.725 144.662 1.00 19.73 ?  207 LEU D CA    1 
ATOM   15038 C  C     . LEU D 2 228 ? 131.016 104.482 144.805 1.00 19.76 ?  207 LEU D C     1 
ATOM   15039 O  O     . LEU D 2 228 ? 130.214 104.398 145.736 1.00 20.07 ?  207 LEU D O     1 
ATOM   15040 C  CB    . LEU D 2 228 ? 131.312 106.734 143.674 1.00 19.36 ?  207 LEU D CB    1 
ATOM   15041 C  CG    . LEU D 2 228 ? 131.941 108.136 143.709 1.00 20.50 ?  207 LEU D CG    1 
ATOM   15042 C  CD1   . LEU D 2 228 ? 131.474 108.961 142.524 1.00 19.87 ?  207 LEU D CD1   1 
ATOM   15043 C  CD2   . LEU D 2 228 ? 131.627 108.871 145.044 1.00 22.38 ?  207 LEU D CD2   1 
ATOM   15044 N  N     . LEU D 2 229 ? 131.191 103.505 143.916 1.00 19.27 ?  208 LEU D N     1 
ATOM   15045 C  CA    . LEU D 2 229 ? 130.472 102.222 144.034 1.00 19.47 ?  208 LEU D CA    1 
ATOM   15046 C  C     . LEU D 2 229 ? 130.838 101.450 145.307 1.00 19.67 ?  208 LEU D C     1 
ATOM   15047 O  O     . LEU D 2 229 ? 129.978 100.799 145.915 1.00 19.82 ?  208 LEU D O     1 
ATOM   15048 C  CB    . LEU D 2 229 ? 130.708 101.334 142.794 1.00 19.51 ?  208 LEU D CB    1 
ATOM   15049 C  CG    . LEU D 2 229 ? 130.270 101.837 141.408 1.00 19.48 ?  208 LEU D CG    1 
ATOM   15050 C  CD1   . LEU D 2 229 ? 130.745 100.863 140.314 1.00 20.14 ?  208 LEU D CD1   1 
ATOM   15051 C  CD2   . LEU D 2 229 ? 128.748 102.083 141.306 1.00 19.95 ?  208 LEU D CD2   1 
ATOM   15052 N  N     . ALA D 2 230 ? 132.109 101.510 145.707 1.00 19.43 ?  209 ALA D N     1 
ATOM   15053 C  CA    . ALA D 2 230 ? 132.558 100.896 146.964 1.00 20.29 ?  209 ALA D CA    1 
ATOM   15054 C  C     . ALA D 2 230 ? 131.970 101.596 148.190 1.00 21.17 ?  209 ALA D C     1 
ATOM   15055 O  O     . ALA D 2 230 ? 131.529 100.937 149.126 1.00 21.73 ?  209 ALA D O     1 
ATOM   15056 C  CB    . ALA D 2 230 ? 134.083 100.875 147.037 1.00 19.99 ?  209 ALA D CB    1 
ATOM   15057 N  N     . GLN D 2 231 ? 131.958 102.929 148.182 1.00 22.26 ?  210 GLN D N     1 
ATOM   15058 C  CA    . GLN D 2 231 ? 131.362 103.710 149.282 1.00 23.33 ?  210 GLN D CA    1 
ATOM   15059 C  C     . GLN D 2 231 ? 129.869 103.411 149.456 1.00 23.85 ?  210 GLN D C     1 
ATOM   15060 O  O     . GLN D 2 231 ? 129.372 103.365 150.578 1.00 24.91 ?  210 GLN D O     1 
ATOM   15061 C  CB    . GLN D 2 231 ? 131.555 105.214 149.066 1.00 23.49 ?  210 GLN D CB    1 
ATOM   15062 C  CG    . GLN D 2 231 ? 133.006 105.704 149.123 1.00 23.05 ?  210 GLN D CG    1 
ATOM   15063 C  CD    . GLN D 2 231 ? 133.109 107.207 148.870 1.00 24.65 ?  210 GLN D CD    1 
ATOM   15064 O  OE1   . GLN D 2 231 ? 132.411 107.994 149.510 1.00 25.85 ?  210 GLN D OE1   1 
ATOM   15065 N  NE2   . GLN D 2 231 ? 133.965 107.608 147.929 1.00 22.30 ?  210 GLN D NE2   1 
ATOM   15066 N  N     . GLU D 2 232 ? 129.159 103.228 148.346 1.00 24.36 ?  211 GLU D N     1 
ATOM   15067 C  CA    . GLU D 2 232 ? 127.759 102.812 148.387 1.00 24.83 ?  211 GLU D CA    1 
ATOM   15068 C  C     . GLU D 2 232 ? 127.569 101.514 149.179 1.00 24.34 ?  211 GLU D C     1 
ATOM   15069 O  O     . GLU D 2 232 ? 126.666 101.426 150.012 1.00 24.20 ?  211 GLU D O     1 
ATOM   15070 C  CB    . GLU D 2 232 ? 127.206 102.646 146.976 1.00 25.15 ?  211 GLU D CB    1 
ATOM   15071 C  CG    . GLU D 2 232 ? 125.711 102.477 146.920 1.00 28.55 ?  211 GLU D CG    1 
ATOM   15072 C  CD    . GLU D 2 232 ? 125.227 102.343 145.502 1.00 33.83 ?  211 GLU D CD    1 
ATOM   15073 O  OE1   . GLU D 2 232 ? 124.882 103.383 144.904 1.00 35.09 ?  211 GLU D OE1   1 
ATOM   15074 O  OE2   . GLU D 2 232 ? 125.235 101.210 144.972 1.00 35.51 -1 211 GLU D OE2   1 
ATOM   15075 N  N     . ILE D 2 233 ? 128.418 100.518 148.927 1.00 23.39 ?  212 ILE D N     1 
ATOM   15076 C  CA    . ILE D 2 233 ? 128.369 99.259  149.690 1.00 23.42 ?  212 ILE D CA    1 
ATOM   15077 C  C     . ILE D 2 233 ? 128.750 99.490  151.153 1.00 23.74 ?  212 ILE D C     1 
ATOM   15078 O  O     . ILE D 2 233 ? 128.044 99.058  152.063 1.00 24.61 ?  212 ILE D O     1 
ATOM   15079 C  CB    . ILE D 2 233 ? 129.250 98.148  149.056 1.00 22.81 ?  212 ILE D CB    1 
ATOM   15080 C  CG1   . ILE D 2 233 ? 128.691 97.738  147.686 1.00 22.94 ?  212 ILE D CG1   1 
ATOM   15081 C  CG2   . ILE D 2 233 ? 129.327 96.919  149.972 1.00 22.45 ?  212 ILE D CG2   1 
ATOM   15082 C  CD1   . ILE D 2 233 ? 129.672 96.909  146.829 1.00 22.21 ?  212 ILE D CD1   1 
ATOM   15083 N  N     . TYR D 2 234 ? 129.859 100.191 151.372 1.00 24.19 ?  213 TYR D N     1 
ATOM   15084 C  CA    . TYR D 2 234 ? 130.351 100.505 152.706 1.00 24.59 ?  213 TYR D CA    1 
ATOM   15085 C  C     . TYR D 2 234 ? 129.267 101.160 153.570 1.00 25.15 ?  213 TYR D C     1 
ATOM   15086 O  O     . TYR D 2 234 ? 129.116 100.810 154.744 1.00 24.94 ?  213 TYR D O     1 
ATOM   15087 C  CB    . TYR D 2 234 ? 131.568 101.428 152.603 1.00 24.41 ?  213 TYR D CB    1 
ATOM   15088 C  CG    . TYR D 2 234 ? 132.173 101.848 153.927 1.00 25.93 ?  213 TYR D CG    1 
ATOM   15089 C  CD1   . TYR D 2 234 ? 133.110 101.045 154.569 1.00 24.70 ?  213 TYR D CD1   1 
ATOM   15090 C  CD2   . TYR D 2 234 ? 131.810 103.059 154.532 1.00 26.11 ?  213 TYR D CD2   1 
ATOM   15091 C  CE1   . TYR D 2 234 ? 133.674 101.429 155.782 1.00 27.90 ?  213 TYR D CE1   1 
ATOM   15092 C  CE2   . TYR D 2 234 ? 132.374 103.451 155.739 1.00 27.70 ?  213 TYR D CE2   1 
ATOM   15093 C  CZ    . TYR D 2 234 ? 133.304 102.635 156.356 1.00 27.89 ?  213 TYR D CZ    1 
ATOM   15094 O  OH    . TYR D 2 234 ? 133.863 103.016 157.554 1.00 32.34 ?  213 TYR D OH    1 
ATOM   15095 N  N     . ASN D 2 235 ? 128.531 102.104 152.982 1.00 25.43 ?  214 ASN D N     1 
ATOM   15096 C  CA    . ASN D 2 235 ? 127.497 102.863 153.705 1.00 26.77 ?  214 ASN D CA    1 
ATOM   15097 C  C     . ASN D 2 235 ? 126.250 102.050 154.050 1.00 27.06 ?  214 ASN D C     1 
ATOM   15098 O  O     . ASN D 2 235 ? 125.417 102.487 154.838 1.00 27.42 ?  214 ASN D O     1 
ATOM   15099 C  CB    . ASN D 2 235 ? 127.074 104.108 152.921 1.00 26.80 ?  214 ASN D CB    1 
ATOM   15100 C  CG    . ASN D 2 235 ? 128.195 105.097 152.745 1.00 28.19 ?  214 ASN D CG    1 
ATOM   15101 O  OD1   . ASN D 2 235 ? 129.050 105.255 153.613 1.00 29.35 ?  214 ASN D OD1   1 
ATOM   15102 N  ND2   . ASN D 2 235 ? 128.192 105.781 151.612 1.00 30.84 ?  214 ASN D ND2   1 
ATOM   15103 N  N     . LYS D 2 236 ? 126.126 100.873 153.454 1.00 26.87 ?  215 LYS D N     1 
ATOM   15104 C  CA    . LYS D 2 236 ? 125.008 99.987  153.751 1.00 27.86 ?  215 LYS D CA    1 
ATOM   15105 C  C     . LYS D 2 236 ? 125.320 99.064  154.938 1.00 28.07 ?  215 LYS D C     1 
ATOM   15106 O  O     . LYS D 2 236 ? 124.470 98.283  155.361 1.00 28.22 ?  215 LYS D O     1 
ATOM   15107 C  CB    . LYS D 2 236 ? 124.634 99.165  152.517 1.00 27.52 ?  215 LYS D CB    1 
ATOM   15108 C  CG    . LYS D 2 236 ? 124.113 99.984  151.362 1.00 29.60 ?  215 LYS D CG    1 
ATOM   15109 C  CD    . LYS D 2 236 ? 123.209 99.167  150.453 1.00 34.24 ?  215 LYS D CD    1 
ATOM   15110 C  CE    . LYS D 2 236 ? 123.909 98.657  149.208 1.00 36.75 ?  215 LYS D CE    1 
ATOM   15111 N  NZ    . LYS D 2 236 ? 124.969 97.680  149.536 1.00 40.41 1  215 LYS D NZ    1 
ATOM   15112 N  N     . GLN D 2 237 ? 126.533 99.168  155.474 1.00 28.33 ?  216 GLN D N     1 
ATOM   15113 C  CA    . GLN D 2 237 ? 126.995 98.248  156.516 1.00 29.60 ?  216 GLN D CA    1 
ATOM   15114 C  C     . GLN D 2 237 ? 126.795 98.802  157.922 1.00 30.69 ?  216 GLN D C     1 
ATOM   15115 O  O     . GLN D 2 237 ? 126.677 100.018 158.109 1.00 30.85 ?  216 GLN D O     1 
ATOM   15116 C  CB    . GLN D 2 237 ? 128.481 97.883  156.315 1.00 29.08 ?  216 GLN D CB    1 
ATOM   15117 C  CG    . GLN D 2 237 ? 128.854 97.360  154.925 1.00 27.78 ?  216 GLN D CG    1 
ATOM   15118 C  CD    . GLN D 2 237 ? 127.943 96.246  154.434 1.00 28.38 ?  216 GLN D CD    1 
ATOM   15119 O  OE1   . GLN D 2 237 ? 127.709 95.264  155.136 1.00 29.30 ?  216 GLN D OE1   1 
ATOM   15120 N  NE2   . GLN D 2 237 ? 127.433 96.392  153.215 1.00 26.88 ?  216 GLN D NE2   1 
ATOM   15121 N  N     . THR D 2 238 ? 126.775 97.901  158.903 1.00 32.02 ?  217 THR D N     1 
ATOM   15122 C  CA    . THR D 2 238 ? 126.761 98.284  160.319 1.00 33.47 ?  217 THR D CA    1 
ATOM   15123 C  C     . THR D 2 238 ? 128.068 98.978  160.715 1.00 34.29 ?  217 THR D C     1 
ATOM   15124 O  O     . THR D 2 238 ? 129.048 98.982  159.952 1.00 33.78 ?  217 THR D O     1 
ATOM   15125 C  CB    . THR D 2 238 ? 126.547 97.049  161.238 1.00 34.00 ?  217 THR D CB    1 
ATOM   15126 O  OG1   . THR D 2 238 ? 127.674 96.166  161.134 1.00 34.33 ?  217 THR D OG1   1 
ATOM   15127 C  CG2   . THR D 2 238 ? 125.266 96.290  160.854 1.00 33.53 ?  217 THR D CG2   1 
ATOM   15128 N  N     . GLU D 2 239 ? 128.095 99.553  161.913 1.00 35.45 ?  218 GLU D N     1 
ATOM   15129 C  CA    . GLU D 2 239 ? 129.297 100.224 162.396 1.00 36.37 ?  218 GLU D CA    1 
ATOM   15130 C  C     . GLU D 2 239 ? 130.456 99.257  162.626 1.00 36.29 ?  218 GLU D C     1 
ATOM   15131 O  O     . GLU D 2 239 ? 131.605 99.579  162.306 1.00 36.18 ?  218 GLU D O     1 
ATOM   15132 C  CB    . GLU D 2 239 ? 129.006 101.057 163.647 1.00 37.27 ?  218 GLU D CB    1 
ATOM   15133 C  CG    . GLU D 2 239 ? 128.138 102.298 163.369 1.00 39.45 ?  218 GLU D CG    1 
ATOM   15134 C  CD    . GLU D 2 239 ? 128.729 103.225 162.308 1.00 41.22 ?  218 GLU D CD    1 
ATOM   15135 O  OE1   . GLU D 2 239 ? 129.940 103.528 162.371 1.00 42.62 ?  218 GLU D OE1   1 
ATOM   15136 O  OE2   . GLU D 2 239 ? 127.978 103.651 161.404 1.00 41.24 -1 218 GLU D OE2   1 
ATOM   15137 N  N     . GLU D 2 240 ? 130.156 98.073  163.156 1.00 36.66 ?  219 GLU D N     1 
ATOM   15138 C  CA    . GLU D 2 240 ? 131.184 97.053  163.375 1.00 37.01 ?  219 GLU D CA    1 
ATOM   15139 C  C     . GLU D 2 240 ? 131.737 96.538  162.046 1.00 35.85 ?  219 GLU D C     1 
ATOM   15140 O  O     . GLU D 2 240 ? 132.949 96.351  161.910 1.00 35.62 ?  219 GLU D O     1 
ATOM   15141 C  CB    . GLU D 2 240 ? 130.655 95.886  164.222 1.00 37.98 ?  219 GLU D CB    1 
ATOM   15142 C  CG    . GLU D 2 240 ? 131.737 94.848  164.561 1.00 40.87 ?  219 GLU D CG    1 
ATOM   15143 C  CD    . GLU D 2 240 ? 131.240 93.667  165.391 1.00 44.58 ?  219 GLU D CD    1 
ATOM   15144 O  OE1   . GLU D 2 240 ? 132.076 93.069  166.112 1.00 45.86 ?  219 GLU D OE1   1 
ATOM   15145 O  OE2   . GLU D 2 240 ? 130.032 93.331  165.326 1.00 45.75 -1 219 GLU D OE2   1 
ATOM   15146 N  N     . LYS D 2 241 ? 130.843 96.312  161.084 1.00 34.54 ?  220 LYS D N     1 
ATOM   15147 C  CA    . LYS D 2 241 ? 131.231 95.849  159.750 1.00 33.65 ?  220 LYS D CA    1 
ATOM   15148 C  C     . LYS D 2 241 ? 132.053 96.915  159.015 1.00 32.67 ?  220 LYS D C     1 
ATOM   15149 O  O     . LYS D 2 241 ? 133.009 96.579  158.322 1.00 32.05 ?  220 LYS D O     1 
ATOM   15150 C  CB    . LYS D 2 241 ? 130.003 95.435  158.932 1.00 33.30 ?  220 LYS D CB    1 
ATOM   15151 C  CG    . LYS D 2 241 ? 130.302 94.783  157.569 1.00 34.50 ?  220 LYS D CG    1 
ATOM   15152 C  CD    . LYS D 2 241 ? 131.117 93.489  157.688 1.00 36.30 ?  220 LYS D CD    1 
ATOM   15153 C  CE    . LYS D 2 241 ? 130.294 92.353  158.286 1.00 38.44 ?  220 LYS D CE    1 
ATOM   15154 N  NZ    . LYS D 2 241 ? 131.170 91.319  158.899 1.00 39.28 1  220 LYS D NZ    1 
ATOM   15155 N  N     . LYS D 2 242 ? 131.677 98.188  159.177 1.00 31.90 ?  221 LYS D N     1 
ATOM   15156 C  CA    . LYS D 2 242 ? 132.441 99.304  158.619 1.00 31.28 ?  221 LYS D CA    1 
ATOM   15157 C  C     . LYS D 2 242 ? 133.874 99.322  159.148 1.00 31.32 ?  221 LYS D C     1 
ATOM   15158 O  O     . LYS D 2 242 ? 134.813 99.407  158.366 1.00 30.72 ?  221 LYS D O     1 
ATOM   15159 C  CB    . LYS D 2 242 ? 131.763 100.651 158.909 1.00 31.38 ?  221 LYS D CB    1 
ATOM   15160 C  CG    . LYS D 2 242 ? 130.632 101.016 157.954 1.00 30.64 ?  221 LYS D CG    1 
ATOM   15161 C  CD    . LYS D 2 242 ? 130.039 102.374 158.327 1.00 32.51 ?  221 LYS D CD    1 
ATOM   15162 C  CE    . LYS D 2 242 ? 128.934 102.768 157.372 1.00 32.66 ?  221 LYS D CE    1 
ATOM   15163 N  NZ    . LYS D 2 242 ? 128.205 103.955 157.870 1.00 35.31 1  221 LYS D NZ    1 
ATOM   15164 N  N     . ALA D 2 243 ? 134.030 99.249  160.473 1.00 31.62 ?  222 ALA D N     1 
ATOM   15165 C  CA    . ALA D 2 243 ? 135.353 99.214  161.107 1.00 31.66 ?  222 ALA D CA    1 
ATOM   15166 C  C     . ALA D 2 243 ? 136.209 98.054  160.582 1.00 31.52 ?  222 ALA D C     1 
ATOM   15167 O  O     . ALA D 2 243 ? 137.426 98.187  160.420 1.00 31.41 ?  222 ALA D O     1 
ATOM   15168 C  CB    . ALA D 2 243 ? 135.215 99.144  162.632 1.00 31.89 ?  222 ALA D CB    1 
ATOM   15169 N  N     . GLU D 2 244 ? 135.549 96.934  160.301 1.00 31.35 ?  223 GLU D N     1 
ATOM   15170 C  CA    . GLU D 2 244 ? 136.178 95.735  159.774 1.00 31.54 ?  223 GLU D CA    1 
ATOM   15171 C  C     . GLU D 2 244 ? 136.628 95.922  158.307 1.00 30.63 ?  223 GLU D C     1 
ATOM   15172 O  O     . GLU D 2 244 ? 137.711 95.470  157.907 1.00 29.47 ?  223 GLU D O     1 
ATOM   15173 C  CB    . GLU D 2 244 ? 135.175 94.599  159.897 1.00 32.45 ?  223 GLU D CB    1 
ATOM   15174 C  CG    . GLU D 2 244 ? 135.696 93.209  159.703 1.00 35.31 ?  223 GLU D CG    1 
ATOM   15175 C  CD    . GLU D 2 244 ? 134.685 92.180  160.167 1.00 38.36 ?  223 GLU D CD    1 
ATOM   15176 O  OE1   . GLU D 2 244 ? 134.439 92.093  161.388 1.00 41.93 ?  223 GLU D OE1   1 
ATOM   15177 O  OE2   . GLU D 2 244 ? 134.123 91.464  159.314 1.00 39.37 -1 223 GLU D OE2   1 
ATOM   15178 N  N     . LEU D 2 245 ? 135.792 96.594  157.522 1.00 29.62 ?  224 LEU D N     1 
ATOM   15179 C  CA    . LEU D 2 245 ? 136.130 96.943  156.144 1.00 29.44 ?  224 LEU D CA    1 
ATOM   15180 C  C     . LEU D 2 245 ? 137.242 97.990  156.062 1.00 28.99 ?  224 LEU D C     1 
ATOM   15181 O  O     . LEU D 2 245 ? 138.065 97.936  155.153 1.00 28.63 ?  224 LEU D O     1 
ATOM   15182 C  CB    . LEU D 2 245 ? 134.884 97.411  155.385 1.00 29.06 ?  224 LEU D CB    1 
ATOM   15183 C  CG    . LEU D 2 245 ? 133.810 96.352  155.114 1.00 29.27 ?  224 LEU D CG    1 
ATOM   15184 C  CD1   . LEU D 2 245 ? 132.674 96.975  154.308 1.00 30.76 ?  224 LEU D CD1   1 
ATOM   15185 C  CD2   . LEU D 2 245 ? 134.373 95.141  154.376 1.00 28.11 ?  224 LEU D CD2   1 
ATOM   15186 N  N     . ARG D 2 246 ? 137.261 98.933  157.006 1.00 29.31 ?  225 ARG D N     1 
ATOM   15187 C  CA    . ARG D 2 246 ? 138.352 99.909  157.100 1.00 29.86 ?  225 ARG D CA    1 
ATOM   15188 C  C     . ARG D 2 246 ? 139.676 99.221  157.402 1.00 29.23 ?  225 ARG D C     1 
ATOM   15189 O  O     . ARG D 2 246 ? 140.691 99.537  156.797 1.00 28.95 ?  225 ARG D O     1 
ATOM   15190 C  CB    . ARG D 2 246 ? 138.092 100.963 158.183 1.00 30.56 ?  225 ARG D CB    1 
ATOM   15191 C  CG    . ARG D 2 246 ? 137.093 102.030 157.799 1.00 33.71 ?  225 ARG D CG    1 
ATOM   15192 C  CD    . ARG D 2 246 ? 137.260 103.316 158.632 1.00 37.42 ?  225 ARG D CD    1 
ATOM   15193 N  NE    . ARG D 2 246 ? 137.189 103.090 160.080 1.00 39.17 ?  225 ARG D NE    1 
ATOM   15194 C  CZ    . ARG D 2 246 ? 136.067 102.912 160.780 1.00 40.68 ?  225 ARG D CZ    1 
ATOM   15195 N  NH1   . ARG D 2 246 ? 134.878 102.914 160.183 1.00 40.28 1  225 ARG D NH1   1 
ATOM   15196 N  NH2   . ARG D 2 246 ? 136.138 102.718 162.093 1.00 41.65 ?  225 ARG D NH2   1 
ATOM   15197 N  N     . GLU D 2 247 ? 139.657 98.295  158.353 1.00 28.89 ?  226 GLU D N     1 
ATOM   15198 C  CA    . GLU D 2 247 ? 140.849 97.524  158.692 1.00 29.27 ?  226 GLU D CA    1 
ATOM   15199 C  C     . GLU D 2 247 ? 141.341 96.729  157.484 1.00 27.84 ?  226 GLU D C     1 
ATOM   15200 O  O     . GLU D 2 247 ? 142.547 96.700  157.223 1.00 27.37 ?  226 GLU D O     1 
ATOM   15201 C  CB    . GLU D 2 247 ? 140.598 96.604  159.900 1.00 30.21 ?  226 GLU D CB    1 
ATOM   15202 C  CG    . GLU D 2 247 ? 141.768 95.665  160.253 1.00 34.46 ?  226 GLU D CG    1 
ATOM   15203 C  CD    . GLU D 2 247 ? 143.058 96.412  160.582 1.00 40.77 ?  226 GLU D CD    1 
ATOM   15204 O  OE1   . GLU D 2 247 ? 143.068 97.172  161.579 1.00 44.03 ?  226 GLU D OE1   1 
ATOM   15205 O  OE2   . GLU D 2 247 ? 144.063 96.245  159.845 1.00 42.98 -1 226 GLU D OE2   1 
ATOM   15206 N  N     . PHE D 2 248 ? 140.415 96.108  156.748 1.00 26.73 ?  227 PHE D N     1 
ATOM   15207 C  CA    . PHE D 2 248 ? 140.754 95.408  155.502 1.00 26.15 ?  227 PHE D CA    1 
ATOM   15208 C  C     . PHE D 2 248 ? 141.480 96.329  154.518 1.00 25.33 ?  227 PHE D C     1 
ATOM   15209 O  O     . PHE D 2 248 ? 142.522 95.960  153.983 1.00 24.70 ?  227 PHE D O     1 
ATOM   15210 C  CB    . PHE D 2 248 ? 139.526 94.796  154.799 1.00 26.02 ?  227 PHE D CB    1 
ATOM   15211 C  CG    . PHE D 2 248 ? 139.792 94.409  153.344 1.00 25.61 ?  227 PHE D CG    1 
ATOM   15212 C  CD1   . PHE D 2 248 ? 140.340 93.169  153.028 1.00 26.51 ?  227 PHE D CD1   1 
ATOM   15213 C  CD2   . PHE D 2 248 ? 139.528 95.305  152.305 1.00 26.21 ?  227 PHE D CD2   1 
ATOM   15214 C  CE1   . PHE D 2 248 ? 140.611 92.815  151.706 1.00 26.16 ?  227 PHE D CE1   1 
ATOM   15215 C  CE2   . PHE D 2 248 ? 139.798 94.965  150.972 1.00 26.07 ?  227 PHE D CE2   1 
ATOM   15216 C  CZ    . PHE D 2 248 ? 140.344 93.712  150.677 1.00 25.82 ?  227 PHE D CZ    1 
ATOM   15217 N  N     . ALA D 2 249 ? 140.908 97.511  154.279 1.00 24.83 ?  228 ALA D N     1 
ATOM   15218 C  CA    . ALA D 2 249 ? 141.441 98.469  153.302 1.00 24.08 ?  228 ALA D CA    1 
ATOM   15219 C  C     . ALA D 2 249 ? 142.842 98.965  153.689 1.00 23.93 ?  228 ALA D C     1 
ATOM   15220 O  O     . ALA D 2 249 ? 143.733 99.053  152.841 1.00 22.51 ?  228 ALA D O     1 
ATOM   15221 C  CB    . ALA D 2 249 ? 140.482 99.656  153.154 1.00 24.18 ?  228 ALA D CB    1 
ATOM   15222 N  N     . ILE D 2 250 ? 143.024 99.291  154.969 1.00 24.20 ?  229 ILE D N     1 
ATOM   15223 C  CA    . ILE D 2 250 ? 144.311 99.780  155.464 1.00 24.86 ?  229 ILE D CA    1 
ATOM   15224 C  C     . ILE D 2 250 ? 145.366 98.668  155.439 1.00 24.68 ?  229 ILE D C     1 
ATOM   15225 O  O     . ILE D 2 250 ? 146.503 98.902  155.049 1.00 24.30 ?  229 ILE D O     1 
ATOM   15226 C  CB    . ILE D 2 250 ? 144.190 100.428 156.888 1.00 25.44 ?  229 ILE D CB    1 
ATOM   15227 C  CG1   . ILE D 2 250 ? 143.200 101.609 156.896 1.00 26.49 ?  229 ILE D CG1   1 
ATOM   15228 C  CG2   . ILE D 2 250 ? 145.557 100.867 157.430 1.00 27.13 ?  229 ILE D CG2   1 
ATOM   15229 C  CD1   . ILE D 2 250 ? 143.460 102.700 155.855 1.00 28.58 ?  229 ILE D CD1   1 
ATOM   15230 N  N     . ASP D 2 251 ? 144.979 97.460  155.851 1.00 24.90 ?  230 ASP D N     1 
ATOM   15231 C  CA    . ASP D 2 251 ? 145.869 96.305  155.822 1.00 25.04 ?  230 ASP D CA    1 
ATOM   15232 C  C     . ASP D 2 251 ? 146.330 96.002  154.385 1.00 24.25 ?  230 ASP D C     1 
ATOM   15233 O  O     . ASP D 2 251 ? 147.520 95.795  154.138 1.00 23.60 ?  230 ASP D O     1 
ATOM   15234 C  CB    . ASP D 2 251 ? 145.167 95.091  156.440 1.00 26.23 ?  230 ASP D CB    1 
ATOM   15235 C  CG    . ASP D 2 251 ? 145.978 93.819  156.330 1.00 28.91 ?  230 ASP D CG    1 
ATOM   15236 O  OD1   . ASP D 2 251 ? 147.035 93.709  156.986 1.00 32.03 ?  230 ASP D OD1   1 
ATOM   15237 O  OD2   . ASP D 2 251 ? 145.538 92.909  155.599 1.00 33.16 -1 230 ASP D OD2   1 
ATOM   15238 N  N     . LEU D 2 252 ? 145.382 95.972  153.451 1.00 23.43 ?  231 LEU D N     1 
ATOM   15239 C  CA    . LEU D 2 252 ? 145.703 95.780  152.040 1.00 22.79 ?  231 LEU D CA    1 
ATOM   15240 C  C     . LEU D 2 252 ? 146.636 96.883  151.530 1.00 22.71 ?  231 LEU D C     1 
ATOM   15241 O  O     . LEU D 2 252 ? 147.625 96.600  150.843 1.00 21.58 ?  231 LEU D O     1 
ATOM   15242 C  CB    . LEU D 2 252 ? 144.432 95.734  151.185 1.00 22.48 ?  231 LEU D CB    1 
ATOM   15243 C  CG    . LEU D 2 252 ? 144.653 95.530  149.674 1.00 21.05 ?  231 LEU D CG    1 
ATOM   15244 C  CD1   . LEU D 2 252 ? 145.430 94.229  149.376 1.00 22.94 ?  231 LEU D CD1   1 
ATOM   15245 C  CD2   . LEU D 2 252 ? 143.328 95.525  148.925 1.00 19.31 ?  231 LEU D CD2   1 
ATOM   15246 N  N     . LEU D 2 253 ? 146.315 98.133  151.865 1.00 22.90 ?  232 LEU D N     1 
ATOM   15247 C  CA    . LEU D 2 253 ? 147.154 99.265  151.443 1.00 23.78 ?  232 LEU D CA    1 
ATOM   15248 C  C     . LEU D 2 253 ? 148.594 99.096  151.939 1.00 23.75 ?  232 LEU D C     1 
ATOM   15249 O  O     . LEU D 2 253 ? 149.543 99.297  151.180 1.00 23.26 ?  232 LEU D O     1 
ATOM   15250 C  CB    . LEU D 2 253 ? 146.592 100.596 151.947 1.00 24.03 ?  232 LEU D CB    1 
ATOM   15251 C  CG    . LEU D 2 253 ? 147.529 101.801 151.750 1.00 26.46 ?  232 LEU D CG    1 
ATOM   15252 C  CD1   . LEU D 2 253 ? 147.594 102.177 150.289 1.00 26.52 ?  232 LEU D CD1   1 
ATOM   15253 C  CD2   . LEU D 2 253 ? 147.091 103.006 152.587 1.00 27.50 ?  232 LEU D CD2   1 
ATOM   15254 N  N     . ASN D 2 254 ? 148.738 98.753  153.220 1.00 24.63 ?  233 ASN D N     1 
ATOM   15255 C  CA    . ASN D 2 254 ? 150.050 98.493  153.819 1.00 25.49 ?  233 ASN D CA    1 
ATOM   15256 C  C     . ASN D 2 254 ? 150.860 97.412  153.087 1.00 24.94 ?  233 ASN D C     1 
ATOM   15257 O  O     . ASN D 2 254 ? 152.055 97.599  152.847 1.00 24.64 ?  233 ASN D O     1 
ATOM   15258 C  CB    . ASN D 2 254 ? 149.912 98.116  155.291 1.00 26.98 ?  233 ASN D CB    1 
ATOM   15259 C  CG    . ASN D 2 254 ? 149.863 99.325  156.198 1.00 29.94 ?  233 ASN D CG    1 
ATOM   15260 O  OD1   . ASN D 2 254 ? 150.592 100.306 155.998 1.00 34.55 ?  233 ASN D OD1   1 
ATOM   15261 N  ND2   . ASN D 2 254 ? 149.013 99.261  157.214 1.00 33.81 ?  233 ASN D ND2   1 
ATOM   15262 N  N     . GLN D 2 255 ? 150.215 96.294  152.753 1.00 24.08 ?  234 GLN D N     1 
ATOM   15263 C  CA    . GLN D 2 255 ? 150.896 95.206  152.045 1.00 24.35 ?  234 GLN D CA    1 
ATOM   15264 C  C     . GLN D 2 255 ? 151.381 95.689  150.690 1.00 23.26 ?  234 GLN D C     1 
ATOM   15265 O  O     . GLN D 2 255 ? 152.541 95.462  150.333 1.00 23.12 ?  234 GLN D O     1 
ATOM   15266 C  CB    . GLN D 2 255 ? 149.986 93.990  151.833 1.00 24.84 ?  234 GLN D CB    1 
ATOM   15267 C  CG    . GLN D 2 255 ? 149.678 93.170  153.066 1.00 27.45 ?  234 GLN D CG    1 
ATOM   15268 C  CD    . GLN D 2 255 ? 150.924 92.673  153.779 1.00 32.02 ?  234 GLN D CD    1 
ATOM   15269 O  OE1   . GLN D 2 255 ? 151.154 93.018  154.936 1.00 35.80 ?  234 GLN D OE1   1 
ATOM   15270 N  NE2   . GLN D 2 255 ? 151.730 91.858  153.096 1.00 32.12 ?  234 GLN D NE2   1 
ATOM   15271 N  N     . LEU D 2 256 ? 150.491 96.355  149.951 1.00 21.77 ?  235 LEU D N     1 
ATOM   15272 C  CA    . LEU D 2 256 ? 150.821 96.863  148.618 1.00 21.68 ?  235 LEU D CA    1 
ATOM   15273 C  C     . LEU D 2 256 ? 151.894 97.944  148.695 1.00 21.49 ?  235 LEU D C     1 
ATOM   15274 O  O     . LEU D 2 256 ? 152.806 97.971  147.875 1.00 20.89 ?  235 LEU D O     1 
ATOM   15275 C  CB    . LEU D 2 256 ? 149.576 97.414  147.894 1.00 20.49 ?  235 LEU D CB    1 
ATOM   15276 C  CG    . LEU D 2 256 ? 148.508 96.390  147.482 1.00 21.52 ?  235 LEU D CG    1 
ATOM   15277 C  CD1   . LEU D 2 256 ? 147.226 97.073  146.978 1.00 20.71 ?  235 LEU D CD1   1 
ATOM   15278 C  CD2   . LEU D 2 256 ? 149.031 95.424  146.428 1.00 20.74 ?  235 LEU D CD2   1 
ATOM   15279 N  N     . TYR D 2 257 ? 151.780 98.824  149.688 1.00 21.42 ?  236 TYR D N     1 
ATOM   15280 C  CA    . TYR D 2 257 ? 152.748 99.908  149.848 1.00 22.02 ?  236 TYR D CA    1 
ATOM   15281 C  C     . TYR D 2 257 ? 154.161 99.395  150.126 1.00 22.61 ?  236 TYR D C     1 
ATOM   15282 O  O     . TYR D 2 257 ? 155.129 99.888  149.546 1.00 22.19 ?  236 TYR D O     1 
ATOM   15283 C  CB    . TYR D 2 257 ? 152.304 100.889 150.928 1.00 22.06 ?  236 TYR D CB    1 
ATOM   15284 C  CG    . TYR D 2 257 ? 153.334 101.946 151.258 1.00 23.44 ?  236 TYR D CG    1 
ATOM   15285 C  CD1   . TYR D 2 257 ? 153.687 102.926 150.323 1.00 24.01 ?  236 TYR D CD1   1 
ATOM   15286 C  CD2   . TYR D 2 257 ? 153.947 101.970 152.508 1.00 25.22 ?  236 TYR D CD2   1 
ATOM   15287 C  CE1   . TYR D 2 257 ? 154.633 103.902 150.631 1.00 25.14 ?  236 TYR D CE1   1 
ATOM   15288 C  CE2   . TYR D 2 257 ? 154.901 102.934 152.823 1.00 26.71 ?  236 TYR D CE2   1 
ATOM   15289 C  CZ    . TYR D 2 257 ? 155.233 103.895 151.885 1.00 25.35 ?  236 TYR D CZ    1 
ATOM   15290 O  OH    . TYR D 2 257 ? 156.164 104.846 152.212 1.00 26.77 ?  236 TYR D OH    1 
ATOM   15291 N  N     . GLU D 2 258 ? 154.282 98.399  151.001 1.00 23.09 ?  237 GLU D N     1 
ATOM   15292 C  CA    . GLU D 2 258 ? 155.608 97.870  151.328 1.00 23.98 ?  237 GLU D CA    1 
ATOM   15293 C  C     . GLU D 2 258 ? 156.256 97.191  150.121 1.00 23.13 ?  237 GLU D C     1 
ATOM   15294 O  O     . GLU D 2 258 ? 157.456 97.331  149.902 1.00 23.02 ?  237 GLU D O     1 
ATOM   15295 C  CB    . GLU D 2 258 ? 155.561 96.946  152.554 1.00 25.20 ?  237 GLU D CB    1 
ATOM   15296 C  CG    . GLU D 2 258 ? 155.187 97.673  153.857 1.00 28.82 ?  237 GLU D CG    1 
ATOM   15297 C  CD    . GLU D 2 258 ? 156.274 98.619  154.386 1.00 34.48 ?  237 GLU D CD    1 
ATOM   15298 O  OE1   . GLU D 2 258 ? 157.486 98.378  154.142 1.00 37.75 ?  237 GLU D OE1   1 
ATOM   15299 O  OE2   . GLU D 2 258 ? 155.916 99.610  155.068 1.00 37.16 -1 237 GLU D OE2   1 
ATOM   15300 N  N     . ASN D 2 259 ? 155.454 96.491  149.328 1.00 22.12 ?  238 ASN D N     1 
ATOM   15301 C  CA    . ASN D 2 259 ? 155.923 95.932  148.060 1.00 22.35 ?  238 ASN D CA    1 
ATOM   15302 C  C     . ASN D 2 259 ? 156.271 97.012  147.000 1.00 22.11 ?  238 ASN D C     1 
ATOM   15303 O  O     . ASN D 2 259 ? 157.229 96.845  146.241 1.00 22.24 ?  238 ASN D O     1 
ATOM   15304 C  CB    . ASN D 2 259 ? 154.904 94.926  147.510 1.00 21.69 ?  238 ASN D CB    1 
ATOM   15305 C  CG    . ASN D 2 259 ? 155.365 94.278  146.216 1.00 23.38 ?  238 ASN D CG    1 
ATOM   15306 O  OD1   . ASN D 2 259 ? 156.274 93.434  146.213 1.00 23.95 ?  238 ASN D OD1   1 
ATOM   15307 N  ND2   . ASN D 2 259 ? 154.752 94.676  145.110 1.00 21.14 ?  238 ASN D ND2   1 
ATOM   15308 N  N     . GLU D 2 260 ? 155.500 98.104  146.958 1.00 21.95 ?  239 GLU D N     1 
ATOM   15309 C  CA    . GLU D 2 260 ? 155.796 99.247  146.070 1.00 22.50 ?  239 GLU D CA    1 
ATOM   15310 C  C     . GLU D 2 260 ? 157.156 99.876  146.368 1.00 22.03 ?  239 GLU D C     1 
ATOM   15311 O  O     . GLU D 2 260 ? 157.853 100.313 145.457 1.00 22.03 ?  239 GLU D O     1 
ATOM   15312 C  CB    . GLU D 2 260 ? 154.736 100.358 146.181 1.00 22.90 ?  239 GLU D CB    1 
ATOM   15313 C  CG    . GLU D 2 260 ? 153.466 100.174 145.336 1.00 25.84 ?  239 GLU D CG    1 
ATOM   15314 C  CD    . GLU D 2 260 ? 153.737 99.801  143.882 1.00 28.59 ?  239 GLU D CD    1 
ATOM   15315 O  OE1   . GLU D 2 260 ? 154.006 98.612  143.615 1.00 28.18 ?  239 GLU D OE1   1 
ATOM   15316 O  OE2   . GLU D 2 260 ? 153.642 100.688 143.001 1.00 30.32 -1 239 GLU D OE2   1 
ATOM   15317 N  N     . LEU D 2 261 ? 157.510 99.954  147.647 1.00 21.50 ?  240 LEU D N     1 
ATOM   15318 C  CA    . LEU D 2 261 ? 158.802 100.511 148.033 1.00 22.03 ?  240 LEU D CA    1 
ATOM   15319 C  C     . LEU D 2 261 ? 159.923 99.655  147.470 1.00 21.52 ?  240 LEU D C     1 
ATOM   15320 O  O     . LEU D 2 261 ? 160.894 100.186 146.930 1.00 21.44 ?  240 LEU D O     1 
ATOM   15321 C  CB    . LEU D 2 261 ? 158.937 100.634 149.548 1.00 21.57 ?  240 LEU D CB    1 
ATOM   15322 C  CG    . LEU D 2 261 ? 157.946 101.537 150.285 1.00 23.22 ?  240 LEU D CG    1 
ATOM   15323 C  CD1   . LEU D 2 261 ? 158.241 101.484 151.773 1.00 23.06 ?  240 LEU D CD1   1 
ATOM   15324 C  CD2   . LEU D 2 261 ? 158.014 102.974 149.769 1.00 23.52 ?  240 LEU D CD2   1 
ATOM   15325 N  N     . GLU D 2 262 ? 159.771 98.335  147.580 1.00 21.69 ?  241 GLU D N     1 
ATOM   15326 C  CA    . GLU D 2 262 ? 160.757 97.397  147.018 1.00 22.31 ?  241 GLU D CA    1 
ATOM   15327 C  C     . GLU D 2 262 ? 160.781 97.447  145.489 1.00 21.69 ?  241 GLU D C     1 
ATOM   15328 O  O     . GLU D 2 262 ? 161.851 97.447  144.875 1.00 21.75 ?  241 GLU D O     1 
ATOM   15329 C  CB    . GLU D 2 262 ? 160.481 95.963  147.480 1.00 22.46 ?  241 GLU D CB    1 
ATOM   15330 C  CG    . GLU D 2 262 ? 160.556 95.723  148.990 1.00 25.63 ?  241 GLU D CG    1 
ATOM   15331 C  CD    . GLU D 2 262 ? 160.363 94.250  149.324 1.00 29.83 ?  241 GLU D CD    1 
ATOM   15332 O  OE1   . GLU D 2 262 ? 159.205 93.782  149.334 1.00 33.22 ?  241 GLU D OE1   1 
ATOM   15333 O  OE2   . GLU D 2 262 ? 161.366 93.550  149.546 1.00 33.36 -1 241 GLU D OE2   1 
ATOM   15334 N  N     . TYR D 2 263 ? 159.597 97.466  144.879 1.00 21.42 ?  242 TYR D N     1 
ATOM   15335 C  CA    . TYR D 2 263 ? 159.454 97.599  143.424 1.00 21.04 ?  242 TYR D CA    1 
ATOM   15336 C  C     . TYR D 2 263 ? 160.173 98.865  142.939 1.00 21.15 ?  242 TYR D C     1 
ATOM   15337 O  O     . TYR D 2 263 ? 160.860 98.853  141.916 1.00 20.32 ?  242 TYR D O     1 
ATOM   15338 C  CB    . TYR D 2 263 ? 157.961 97.668  143.062 1.00 20.95 ?  242 TYR D CB    1 
ATOM   15339 C  CG    . TYR D 2 263 ? 157.649 97.907  141.597 1.00 21.86 ?  242 TYR D CG    1 
ATOM   15340 C  CD1   . TYR D 2 263 ? 157.689 96.860  140.676 1.00 23.53 ?  242 TYR D CD1   1 
ATOM   15341 C  CD2   . TYR D 2 263 ? 157.313 99.182  141.130 1.00 21.20 ?  242 TYR D CD2   1 
ATOM   15342 C  CE1   . TYR D 2 263 ? 157.403 97.072  139.336 1.00 23.34 ?  242 TYR D CE1   1 
ATOM   15343 C  CE2   . TYR D 2 263 ? 157.024 99.403  139.787 1.00 23.11 ?  242 TYR D CE2   1 
ATOM   15344 C  CZ    . TYR D 2 263 ? 157.077 98.343  138.897 1.00 23.27 ?  242 TYR D CZ    1 
ATOM   15345 O  OH    . TYR D 2 263 ? 156.791 98.556  137.565 1.00 27.07 ?  242 TYR D OH    1 
ATOM   15346 N  N     . THR D 2 264 ? 159.984 99.950  143.686 1.00 21.12 ?  243 THR D N     1 
ATOM   15347 C  CA    . THR D 2 264 ? 160.536 101.260 143.354 1.00 21.98 ?  243 THR D CA    1 
ATOM   15348 C  C     . THR D 2 264 ? 162.063 101.246 143.381 1.00 22.32 ?  243 THR D C     1 
ATOM   15349 O  O     . THR D 2 264 ? 162.698 101.657 142.412 1.00 21.78 ?  243 THR D O     1 
ATOM   15350 C  CB    . THR D 2 264 ? 159.964 102.353 144.285 1.00 21.68 ?  243 THR D CB    1 
ATOM   15351 O  OG1   . THR D 2 264 ? 158.562 102.485 144.034 1.00 23.29 ?  243 THR D OG1   1 
ATOM   15352 C  CG2   . THR D 2 264 ? 160.653 103.715 144.075 1.00 23.16 ?  243 THR D CG2   1 
ATOM   15353 N  N     . GLU D 2 265 ? 162.646 100.752 144.472 1.00 22.48 ?  244 GLU D N     1 
ATOM   15354 C  CA    . GLU D 2 265 ? 164.106 100.676 144.564 1.00 23.73 ?  244 GLU D CA    1 
ATOM   15355 C  C     . GLU D 2 265 ? 164.688 99.797  143.468 1.00 23.85 ?  244 GLU D C     1 
ATOM   15356 O  O     . GLU D 2 265 ? 165.705 100.144 142.881 1.00 24.40 ?  244 GLU D O     1 
ATOM   15357 C  CB    . GLU D 2 265 ? 164.544 100.177 145.932 1.00 23.19 ?  244 GLU D CB    1 
ATOM   15358 C  CG    . GLU D 2 265 ? 164.363 101.225 146.998 1.00 25.08 ?  244 GLU D CG    1 
ATOM   15359 C  CD    . GLU D 2 265 ? 164.626 100.703 148.395 1.00 27.30 ?  244 GLU D CD    1 
ATOM   15360 O  OE1   . GLU D 2 265 ? 165.150 99.581  148.538 1.00 27.77 ?  244 GLU D OE1   1 
ATOM   15361 O  OE2   . GLU D 2 265 ? 164.306 101.429 149.353 1.00 28.63 -1 244 GLU D OE2   1 
ATOM   15362 N  N     . ASP D 2 266 ? 164.011 98.684  143.180 1.00 24.13 ?  245 ASP D N     1 
ATOM   15363 C  CA    . ASP D 2 266 ? 164.440 97.729  142.154 1.00 25.22 ?  245 ASP D CA    1 
ATOM   15364 C  C     . ASP D 2 266 ? 164.570 98.374  140.756 1.00 24.84 ?  245 ASP D C     1 
ATOM   15365 O  O     . ASP D 2 266 ? 165.481 98.034  139.994 1.00 25.64 ?  245 ASP D O     1 
ATOM   15366 C  CB    . ASP D 2 266 ? 163.463 96.543  142.126 1.00 25.79 ?  245 ASP D CB    1 
ATOM   15367 C  CG    . ASP D 2 266 ? 163.901 95.427  141.186 1.00 27.71 ?  245 ASP D CG    1 
ATOM   15368 O  OD1   . ASP D 2 266 ? 165.024 94.925  141.343 1.00 31.57 ?  245 ASP D OD1   1 
ATOM   15369 O  OD2   . ASP D 2 266 ? 163.111 95.033  140.302 1.00 30.29 -1 245 ASP D OD2   1 
ATOM   15370 N  N     . LEU D 2 267 ? 163.678 99.308  140.438 1.00 24.07 ?  246 LEU D N     1 
ATOM   15371 C  CA    . LEU D 2 267 ? 163.649 99.948  139.120 1.00 23.98 ?  246 LEU D CA    1 
ATOM   15372 C  C     . LEU D 2 267 ? 164.374 101.293 139.047 1.00 22.83 ?  246 LEU D C     1 
ATOM   15373 O  O     . LEU D 2 267 ? 165.027 101.590 138.039 1.00 23.00 ?  246 LEU D O     1 
ATOM   15374 C  CB    . LEU D 2 267 ? 162.199 100.145 138.644 1.00 23.82 ?  246 LEU D CB    1 
ATOM   15375 C  CG    . LEU D 2 267 ? 161.415 98.877  138.280 1.00 26.05 ?  246 LEU D CG    1 
ATOM   15376 C  CD1   . LEU D 2 267 ? 160.127 99.230  137.590 1.00 26.74 ?  246 LEU D CD1   1 
ATOM   15377 C  CD2   . LEU D 2 267 ? 162.229 97.947  137.400 1.00 28.00 ?  246 LEU D CD2   1 
ATOM   15378 N  N     . TYR D 2 268 ? 164.249 102.093 140.106 1.00 21.68 ?  247 TYR D N     1 
ATOM   15379 C  CA    . TYR D 2 268 ? 164.664 103.499 140.066 1.00 20.95 ?  247 TYR D CA    1 
ATOM   15380 C  C     . TYR D 2 268 ? 166.005 103.848 140.725 1.00 21.43 ?  247 TYR D C     1 
ATOM   15381 O  O     . TYR D 2 268 ? 166.535 104.928 140.468 1.00 20.73 ?  247 TYR D O     1 
ATOM   15382 C  CB    . TYR D 2 268 ? 163.571 104.404 140.644 1.00 20.27 ?  247 TYR D CB    1 
ATOM   15383 C  CG    . TYR D 2 268 ? 162.333 104.534 139.777 1.00 19.54 ?  247 TYR D CG    1 
ATOM   15384 C  CD1   . TYR D 2 268 ? 161.176 103.820 140.073 1.00 18.52 ?  247 TYR D CD1   1 
ATOM   15385 C  CD2   . TYR D 2 268 ? 162.326 105.373 138.653 1.00 20.62 ?  247 TYR D CD2   1 
ATOM   15386 C  CE1   . TYR D 2 268 ? 160.010 103.946 139.273 1.00 18.33 ?  247 TYR D CE1   1 
ATOM   15387 C  CE2   . TYR D 2 268 ? 161.172 105.506 137.847 1.00 20.79 ?  247 TYR D CE2   1 
ATOM   15388 C  CZ    . TYR D 2 268 ? 160.025 104.796 138.173 1.00 20.23 ?  247 TYR D CZ    1 
ATOM   15389 O  OH    . TYR D 2 268 ? 158.905 104.934 137.377 1.00 20.50 ?  247 TYR D OH    1 
ATOM   15390 N  N     . ASP D 2 269 ? 166.547 102.971 141.577 1.00 21.65 ?  248 ASP D N     1 
ATOM   15391 C  CA    . ASP D 2 269 ? 167.885 103.232 142.122 1.00 22.30 ?  248 ASP D CA    1 
ATOM   15392 C  C     . ASP D 2 269 ? 168.948 103.442 141.018 1.00 22.54 ?  248 ASP D C     1 
ATOM   15393 O  O     . ASP D 2 269 ? 169.825 104.299 141.161 1.00 22.49 ?  248 ASP D O     1 
ATOM   15394 C  CB    . ASP D 2 269 ? 168.329 102.137 143.094 1.00 22.83 ?  248 ASP D CB    1 
ATOM   15395 C  CG    . ASP D 2 269 ? 167.746 102.318 144.492 1.00 23.55 ?  248 ASP D CG    1 
ATOM   15396 O  OD1   . ASP D 2 269 ? 167.123 103.366 144.759 1.00 24.95 ?  248 ASP D OD1   1 
ATOM   15397 O  OD2   . ASP D 2 269 ? 167.910 101.403 145.330 1.00 24.47 -1 248 ASP D OD2   1 
ATOM   15398 N  N     . GLN D 2 270 ? 168.862 102.675 139.929 1.00 22.79 ?  249 GLN D N     1 
ATOM   15399 C  CA    . GLN D 2 270 ? 169.844 102.769 138.841 1.00 23.41 ?  249 GLN D CA    1 
ATOM   15400 C  C     . GLN D 2 270 ? 169.802 104.101 138.086 1.00 22.83 ?  249 GLN D C     1 
ATOM   15401 O  O     . GLN D 2 270 ? 170.739 104.426 137.359 1.00 23.75 ?  249 GLN D O     1 
ATOM   15402 C  CB    . GLN D 2 270 ? 169.719 101.597 137.862 1.00 24.02 ?  249 GLN D CB    1 
ATOM   15403 C  CG    . GLN D 2 270 ? 168.448 101.609 136.995 1.00 25.40 ?  249 GLN D CG    1 
ATOM   15404 C  CD    . GLN D 2 270 ? 168.217 100.290 136.278 1.00 29.23 ?  249 GLN D CD    1 
ATOM   15405 O  OE1   . GLN D 2 270 ? 168.581 99.226  136.782 1.00 31.31 ?  249 GLN D OE1   1 
ATOM   15406 N  NE2   . GLN D 2 270 ? 167.596 100.350 135.102 1.00 30.04 ?  249 GLN D NE2   1 
ATOM   15407 N  N     . VAL D 2 271 ? 168.714 104.854 138.242 1.00 21.93 ?  250 VAL D N     1 
ATOM   15408 C  CA    . VAL D 2 271 ? 168.615 106.194 137.654 1.00 21.29 ?  250 VAL D CA    1 
ATOM   15409 C  C     . VAL D 2 271 ? 168.465 107.292 138.724 1.00 21.16 ?  250 VAL D C     1 
ATOM   15410 O  O     . VAL D 2 271 ? 168.153 108.443 138.403 1.00 21.54 ?  250 VAL D O     1 
ATOM   15411 C  CB    . VAL D 2 271 ? 167.479 106.266 136.582 1.00 21.62 ?  250 VAL D CB    1 
ATOM   15412 C  CG1   . VAL D 2 271 ? 167.803 105.355 135.400 1.00 21.36 ?  250 VAL D CG1   1 
ATOM   15413 C  CG2   . VAL D 2 271 ? 166.111 105.908 137.190 1.00 21.17 ?  250 VAL D CG2   1 
ATOM   15414 N  N     . GLY D 2 272 ? 168.665 106.921 139.994 1.00 20.92 ?  251 GLY D N     1 
ATOM   15415 C  CA    . GLY D 2 272 ? 168.742 107.875 141.118 1.00 20.61 ?  251 GLY D CA    1 
ATOM   15416 C  C     . GLY D 2 272 ? 167.467 108.609 141.529 1.00 20.77 ?  251 GLY D C     1 
ATOM   15417 O  O     . GLY D 2 272 ? 167.532 109.704 142.108 1.00 20.28 ?  251 GLY D O     1 
ATOM   15418 N  N     . LEU D 2 273 ? 166.311 108.008 141.260 1.00 19.85 ?  252 LEU D N     1 
ATOM   15419 C  CA    . LEU D 2 273 ? 165.045 108.720 141.442 1.00 20.09 ?  252 LEU D CA    1 
ATOM   15420 C  C     . LEU D 2 273 ? 164.145 108.226 142.578 1.00 19.88 ?  252 LEU D C     1 
ATOM   15421 O  O     . LEU D 2 273 ? 163.115 108.838 142.841 1.00 20.04 ?  252 LEU D O     1 
ATOM   15422 C  CB    . LEU D 2 273 ? 164.246 108.684 140.129 1.00 19.97 ?  252 LEU D CB    1 
ATOM   15423 C  CG    . LEU D 2 273 ? 164.909 109.292 138.902 1.00 20.26 ?  252 LEU D CG    1 
ATOM   15424 C  CD1   . LEU D 2 273 ? 163.914 109.248 137.764 1.00 18.98 ?  252 LEU D CD1   1 
ATOM   15425 C  CD2   . LEU D 2 273 ? 165.393 110.747 139.159 1.00 21.03 ?  252 LEU D CD2   1 
ATOM   15426 N  N     . SER D 2 274 ? 164.543 107.141 143.244 0.50 19.54 ?  253 SER D N     1 
ATOM   15427 C  CA    . SER D 2 274 ? 163.655 106.412 144.163 0.50 19.34 ?  253 SER D CA    1 
ATOM   15428 C  C     . SER D 2 274 ? 163.027 107.261 145.275 0.50 20.05 ?  253 SER D C     1 
ATOM   15429 O  O     . SER D 2 274 ? 161.844 107.102 145.576 0.50 20.31 ?  253 SER D O     1 
ATOM   15430 C  CB    . SER D 2 274 ? 164.361 105.186 144.757 0.50 18.97 ?  253 SER D CB    1 
ATOM   15431 O  OG    . SER D 2 274 ? 164.848 104.329 143.741 0.50 15.35 ?  253 SER D OG    1 
ATOM   15432 N  N     . HIS D 2 275 ? 163.815 108.146 145.884 1.00 20.77 ?  254 HIS D N     1 
ATOM   15433 C  CA    . HIS D 2 275 ? 163.306 109.053 146.932 1.00 21.18 ?  254 HIS D CA    1 
ATOM   15434 C  C     . HIS D 2 275 ? 162.065 109.837 146.469 1.00 21.50 ?  254 HIS D C     1 
ATOM   15435 O  O     . HIS D 2 275 ? 161.036 109.861 147.164 1.00 19.88 ?  254 HIS D O     1 
ATOM   15436 C  CB    . HIS D 2 275 ? 164.395 110.020 147.424 1.00 21.60 ?  254 HIS D CB    1 
ATOM   15437 C  CG    . HIS D 2 275 ? 163.890 111.044 148.396 1.00 22.43 ?  254 HIS D CG    1 
ATOM   15438 N  ND1   . HIS D 2 275 ? 163.849 110.827 149.758 1.00 22.77 ?  254 HIS D ND1   1 
ATOM   15439 C  CD2   . HIS D 2 275 ? 163.389 112.289 148.196 1.00 22.50 ?  254 HIS D CD2   1 
ATOM   15440 C  CE1   . HIS D 2 275 ? 163.348 111.896 150.355 1.00 24.05 ?  254 HIS D CE1   1 
ATOM   15441 N  NE2   . HIS D 2 275 ? 163.055 112.794 149.428 1.00 23.22 ?  254 HIS D NE2   1 
ATOM   15442 N  N     . ASP D 2 276 ? 162.167 110.457 145.292 1.00 22.34 ?  255 ASP D N     1 
ATOM   15443 C  CA    . ASP D 2 276 ? 161.066 111.245 144.745 1.00 23.19 ?  255 ASP D CA    1 
ATOM   15444 C  C     . ASP D 2 276 ? 159.895 110.382 144.298 1.00 22.17 ?  255 ASP D C     1 
ATOM   15445 O  O     . ASP D 2 276 ? 158.752 110.801 144.419 1.00 21.87 ?  255 ASP D O     1 
ATOM   15446 C  CB    . ASP D 2 276 ? 161.530 112.128 143.575 1.00 24.33 ?  255 ASP D CB    1 
ATOM   15447 C  CG    . ASP D 2 276 ? 162.068 113.488 144.025 1.00 27.58 ?  255 ASP D CG    1 
ATOM   15448 O  OD1   . ASP D 2 276 ? 161.699 113.971 145.119 1.00 31.10 ?  255 ASP D OD1   1 
ATOM   15449 O  OD2   . ASP D 2 276 ? 162.874 114.076 143.268 1.00 29.88 -1 255 ASP D OD2   1 
ATOM   15450 N  N     . VAL D 2 277 ? 160.179 109.201 143.751 1.00 21.21 ?  256 VAL D N     1 
ATOM   15451 C  CA    . VAL D 2 277 ? 159.112 108.273 143.363 1.00 20.51 ?  256 VAL D CA    1 
ATOM   15452 C  C     . VAL D 2 277 ? 158.289 107.836 144.581 1.00 20.32 ?  256 VAL D C     1 
ATOM   15453 O  O     . VAL D 2 277 ? 157.066 107.754 144.503 1.00 19.81 ?  256 VAL D O     1 
ATOM   15454 C  CB    . VAL D 2 277 ? 159.650 107.029 142.599 1.00 20.30 ?  256 VAL D CB    1 
ATOM   15455 C  CG1   . VAL D 2 277 ? 158.519 106.064 142.285 1.00 21.16 ?  256 VAL D CG1   1 
ATOM   15456 C  CG2   . VAL D 2 277 ? 160.337 107.454 141.314 1.00 19.06 ?  256 VAL D CG2   1 
ATOM   15457 N  N     . LYS D 2 278 ? 158.970 107.581 145.698 1.00 19.84 ?  257 LYS D N     1 
ATOM   15458 C  CA    . LYS D 2 278 ? 158.303 107.209 146.946 1.00 20.27 ?  257 LYS D CA    1 
ATOM   15459 C  C     . LYS D 2 278 ? 157.319 108.282 147.430 1.00 20.16 ?  257 LYS D C     1 
ATOM   15460 O  O     . LYS D 2 278 ? 156.222 107.945 147.866 1.00 19.88 ?  257 LYS D O     1 
ATOM   15461 C  CB    . LYS D 2 278 ? 159.317 106.848 148.034 1.00 20.20 ?  257 LYS D CB    1 
ATOM   15462 C  CG    . LYS D 2 278 ? 159.988 105.498 147.804 1.00 21.60 ?  257 LYS D CG    1 
ATOM   15463 C  CD    . LYS D 2 278 ? 161.176 105.288 148.735 1.00 21.53 ?  257 LYS D CD    1 
ATOM   15464 C  CE    . LYS D 2 278 ? 161.906 104.022 148.358 1.00 24.52 ?  257 LYS D CE    1 
ATOM   15465 N  NZ    . LYS D 2 278 ? 163.058 103.776 149.287 1.00 26.32 1  257 LYS D NZ    1 
ATOM   15466 N  N     . LYS D 2 279 ? 157.703 109.560 147.327 1.00 19.67 ?  258 LYS D N     1 
ATOM   15467 C  CA    . LYS D 2 279 ? 156.785 110.660 147.658 1.00 20.10 ?  258 LYS D CA    1 
ATOM   15468 C  C     . LYS D 2 279 ? 155.531 110.620 146.776 1.00 19.12 ?  258 LYS D C     1 
ATOM   15469 O  O     . LYS D 2 279 ? 154.422 110.842 147.266 1.00 18.59 ?  258 LYS D O     1 
ATOM   15470 C  CB    . LYS D 2 279 ? 157.469 112.036 147.544 1.00 20.54 ?  258 LYS D CB    1 
ATOM   15471 C  CG    . LYS D 2 279 ? 158.660 112.242 148.478 1.00 22.84 ?  258 LYS D CG    1 
ATOM   15472 C  CD    . LYS D 2 279 ? 158.940 113.738 148.754 1.00 24.16 ?  258 LYS D CD    1 
ATOM   15473 C  CE    . LYS D 2 279 ? 159.407 114.489 147.511 1.00 25.61 ?  258 LYS D CE    1 
ATOM   15474 N  NZ    . LYS D 2 279 ? 159.685 115.952 147.792 1.00 24.70 1  258 LYS D NZ    1 
ATOM   15475 N  N     . PHE D 2 280 ? 155.724 110.313 145.490 1.00 19.04 ?  259 PHE D N     1 
ATOM   15476 C  CA    . PHE D 2 280 ? 154.634 110.233 144.499 1.00 19.31 ?  259 PHE D CA    1 
ATOM   15477 C  C     . PHE D 2 280 ? 153.678 109.063 144.754 1.00 19.25 ?  259 PHE D C     1 
ATOM   15478 O  O     . PHE D 2 280 ? 152.459 109.191 144.583 1.00 19.71 ?  259 PHE D O     1 
ATOM   15479 C  CB    . PHE D 2 280 ? 155.222 110.121 143.092 1.00 19.04 ?  259 PHE D CB    1 
ATOM   15480 C  CG    . PHE D 2 280 ? 154.244 110.421 141.972 1.00 20.15 ?  259 PHE D CG    1 
ATOM   15481 C  CD1   . PHE D 2 280 ? 153.561 111.627 141.923 1.00 21.63 ?  259 PHE D CD1   1 
ATOM   15482 C  CD2   . PHE D 2 280 ? 154.059 109.501 140.938 1.00 19.95 ?  259 PHE D CD2   1 
ATOM   15483 C  CE1   . PHE D 2 280 ? 152.683 111.915 140.855 1.00 22.56 ?  259 PHE D CE1   1 
ATOM   15484 C  CE2   . PHE D 2 280 ? 153.197 109.769 139.876 1.00 20.29 ?  259 PHE D CE2   1 
ATOM   15485 C  CZ    . PHE D 2 280 ? 152.503 110.980 139.835 1.00 21.30 ?  259 PHE D CZ    1 
ATOM   15486 N  N     . ILE D 2 281 ? 154.229 107.919 145.148 1.00 19.36 ?  260 ILE D N     1 
ATOM   15487 C  CA    . ILE D 2 281 ? 153.419 106.777 145.583 1.00 19.45 ?  260 ILE D CA    1 
ATOM   15488 C  C     . ILE D 2 281 ? 152.500 107.126 146.773 1.00 19.61 ?  260 ILE D C     1 
ATOM   15489 O  O     . ILE D 2 281 ? 151.308 106.815 146.739 1.00 19.72 ?  260 ILE D O     1 
ATOM   15490 C  CB    . ILE D 2 281 ? 154.334 105.568 145.911 1.00 19.49 ?  260 ILE D CB    1 
ATOM   15491 C  CG1   . ILE D 2 281 ? 155.020 105.081 144.631 1.00 20.10 ?  260 ILE D CG1   1 
ATOM   15492 C  CG2   . ILE D 2 281 ? 153.577 104.433 146.635 1.00 20.53 ?  260 ILE D CG2   1 
ATOM   15493 C  CD1   . ILE D 2 281 ? 156.183 104.126 144.919 1.00 21.17 ?  260 ILE D CD1   1 
ATOM   15494 N  N     . ARG D 2 282 ? 153.048 107.774 147.804 1.00 19.75 ?  261 ARG D N     1 
ATOM   15495 C  CA    . ARG D 2 282 ? 152.271 108.107 149.013 1.00 20.34 ?  261 ARG D CA    1 
ATOM   15496 C  C     . ARG D 2 282 ? 151.169 109.118 148.720 1.00 21.18 ?  261 ARG D C     1 
ATOM   15497 O  O     . ARG D 2 282 ? 150.044 109.005 149.228 1.00 21.68 ?  261 ARG D O     1 
ATOM   15498 C  CB    . ARG D 2 282 ? 153.181 108.611 150.141 1.00 20.20 ?  261 ARG D CB    1 
ATOM   15499 C  CG    . ARG D 2 282 ? 154.052 107.532 150.758 1.00 20.57 ?  261 ARG D CG    1 
ATOM   15500 C  CD    . ARG D 2 282 ? 154.807 108.057 151.981 1.00 23.15 ?  261 ARG D CD    1 
ATOM   15501 N  NE    . ARG D 2 282 ? 155.918 108.951 151.646 1.00 23.46 ?  261 ARG D NE    1 
ATOM   15502 C  CZ    . ARG D 2 282 ? 157.163 108.551 151.395 1.00 22.84 ?  261 ARG D CZ    1 
ATOM   15503 N  NH1   . ARG D 2 282 ? 157.474 107.261 151.402 1.00 23.37 1  261 ARG D NH1   1 
ATOM   15504 N  NH2   . ARG D 2 282 ? 158.102 109.448 151.125 1.00 22.27 ?  261 ARG D NH2   1 
ATOM   15505 N  N     . TYR D 2 283 ? 151.511 110.116 147.913 1.00 21.46 ?  262 TYR D N     1 
ATOM   15506 C  CA    . TYR D 2 283 ? 150.558 111.131 147.468 1.00 22.97 ?  262 TYR D CA    1 
ATOM   15507 C  C     . TYR D 2 283 ? 149.380 110.470 146.717 1.00 22.12 ?  262 TYR D C     1 
ATOM   15508 O  O     . TYR D 2 283 ? 148.217 110.811 146.944 1.00 22.00 ?  262 TYR D O     1 
ATOM   15509 C  CB    . TYR D 2 283 ? 151.306 112.158 146.611 1.00 23.37 ?  262 TYR D CB    1 
ATOM   15510 C  CG    . TYR D 2 283 ? 150.461 113.090 145.775 1.00 27.31 ?  262 TYR D CG    1 
ATOM   15511 C  CD1   . TYR D 2 283 ? 149.975 114.286 146.305 1.00 30.79 ?  262 TYR D CD1   1 
ATOM   15512 C  CD2   . TYR D 2 283 ? 150.186 112.797 144.440 1.00 30.31 ?  262 TYR D CD2   1 
ATOM   15513 C  CE1   . TYR D 2 283 ? 149.196 115.158 145.527 1.00 33.18 ?  262 TYR D CE1   1 
ATOM   15514 C  CE2   . TYR D 2 283 ? 149.421 113.661 143.651 1.00 33.20 ?  262 TYR D CE2   1 
ATOM   15515 C  CZ    . TYR D 2 283 ? 148.936 114.842 144.202 1.00 34.74 ?  262 TYR D CZ    1 
ATOM   15516 O  OH    . TYR D 2 283 ? 148.187 115.697 143.418 1.00 37.63 ?  262 TYR D OH    1 
ATOM   15517 N  N     . ASN D 2 284 ? 149.678 109.491 145.867 1.00 21.63 ?  263 ASN D N     1 
ATOM   15518 C  CA    . ASN D 2 284 ? 148.626 108.800 145.126 1.00 21.41 ?  263 ASN D CA    1 
ATOM   15519 C  C     . ASN D 2 284 ? 147.862 107.770 145.963 1.00 20.86 ?  263 ASN D C     1 
ATOM   15520 O  O     . ASN D 2 284 ? 146.678 107.552 145.732 1.00 20.92 ?  263 ASN D O     1 
ATOM   15521 C  CB    . ASN D 2 284 ? 149.161 108.214 143.817 1.00 21.15 ?  263 ASN D CB    1 
ATOM   15522 C  CG    . ASN D 2 284 ? 149.393 109.288 142.763 1.00 22.59 ?  263 ASN D CG    1 
ATOM   15523 O  OD1   . ASN D 2 284 ? 148.441 109.843 142.208 1.00 22.35 ?  263 ASN D OD1   1 
ATOM   15524 N  ND2   . ASN D 2 284 ? 150.658 109.598 142.494 1.00 22.93 ?  263 ASN D ND2   1 
ATOM   15525 N  N     . ALA D 2 285 ? 148.536 107.152 146.932 1.00 20.92 ?  264 ALA D N     1 
ATOM   15526 C  CA    . ALA D 2 285 ? 147.859 106.318 147.941 1.00 20.77 ?  264 ALA D CA    1 
ATOM   15527 C  C     . ALA D 2 285 ? 146.774 107.102 148.688 1.00 21.13 ?  264 ALA D C     1 
ATOM   15528 O  O     . ALA D 2 285 ? 145.665 106.594 148.897 1.00 19.92 ?  264 ALA D O     1 
ATOM   15529 C  CB    . ALA D 2 285 ? 148.873 105.719 148.927 1.00 20.68 ?  264 ALA D CB    1 
ATOM   15530 N  N     . ASN D 2 286 ? 147.100 108.338 149.079 1.00 21.38 ?  265 ASN D N     1 
ATOM   15531 C  CA    . ASN D 2 286 ? 146.140 109.237 149.727 1.00 21.94 ?  265 ASN D CA    1 
ATOM   15532 C  C     . ASN D 2 286 ? 144.935 109.557 148.825 1.00 22.13 ?  265 ASN D C     1 
ATOM   15533 O  O     . ASN D 2 286 ? 143.808 109.621 149.300 1.00 21.95 ?  265 ASN D O     1 
ATOM   15534 C  CB    . ASN D 2 286 ? 146.817 110.538 150.162 1.00 22.22 ?  265 ASN D CB    1 
ATOM   15535 C  CG    . ASN D 2 286 ? 147.613 110.404 151.457 1.00 22.80 ?  265 ASN D CG    1 
ATOM   15536 O  OD1   . ASN D 2 286 ? 147.500 109.419 152.195 1.00 22.57 ?  265 ASN D OD1   1 
ATOM   15537 N  ND2   . ASN D 2 286 ? 148.434 111.411 151.730 1.00 23.91 ?  265 ASN D ND2   1 
ATOM   15538 N  N     . LYS D 2 287 ? 145.175 109.748 147.530 1.00 22.51 ?  266 LYS D N     1 
ATOM   15539 C  CA    . LYS D 2 287 ? 144.074 109.977 146.583 1.00 22.91 ?  266 LYS D CA    1 
ATOM   15540 C  C     . LYS D 2 287 ? 143.158 108.750 146.489 1.00 22.33 ?  266 LYS D C     1 
ATOM   15541 O  O     . LYS D 2 287 ? 141.942 108.890 146.470 1.00 22.24 ?  266 LYS D O     1 
ATOM   15542 C  CB    . LYS D 2 287 ? 144.600 110.364 145.194 1.00 23.65 ?  266 LYS D CB    1 
ATOM   15543 C  CG    . LYS D 2 287 ? 145.128 111.797 145.112 1.00 26.50 ?  266 LYS D CG    1 
ATOM   15544 C  CD    . LYS D 2 287 ? 145.623 112.114 143.688 1.00 31.30 ?  266 LYS D CD    1 
ATOM   15545 C  CE    . LYS D 2 287 ? 145.668 113.615 143.467 1.00 35.08 ?  266 LYS D CE    1 
ATOM   15546 N  NZ    . LYS D 2 287 ? 146.105 114.008 142.094 1.00 37.66 1  266 LYS D NZ    1 
ATOM   15547 N  N     . ALA D 2 288 ? 143.757 107.558 146.447 1.00 21.41 ?  267 ALA D N     1 
ATOM   15548 C  CA    . ALA D 2 288 ? 143.025 106.292 146.407 1.00 21.53 ?  267 ALA D CA    1 
ATOM   15549 C  C     . ALA D 2 288 ? 142.139 106.109 147.651 1.00 21.77 ?  267 ALA D C     1 
ATOM   15550 O  O     . ALA D 2 288 ? 140.963 105.718 147.552 1.00 21.59 ?  267 ALA D O     1 
ATOM   15551 C  CB    . ALA D 2 288 ? 144.000 105.116 146.250 1.00 21.33 ?  267 ALA D CB    1 
ATOM   15552 N  N     . LEU D 2 289 ? 142.696 106.416 148.815 1.00 21.71 ?  268 LEU D N     1 
ATOM   15553 C  CA    . LEU D 2 289 ? 141.921 106.387 150.050 1.00 22.36 ?  268 LEU D CA    1 
ATOM   15554 C  C     . LEU D 2 289 ? 140.771 107.382 149.999 1.00 23.01 ?  268 LEU D C     1 
ATOM   15555 O  O     . LEU D 2 289 ? 139.636 107.044 150.346 1.00 23.14 ?  268 LEU D O     1 
ATOM   15556 C  CB    . LEU D 2 289 ? 142.819 106.627 151.270 1.00 22.61 ?  268 LEU D CB    1 
ATOM   15557 C  CG    . LEU D 2 289 ? 143.793 105.480 151.613 1.00 21.22 ?  268 LEU D CG    1 
ATOM   15558 C  CD1   . LEU D 2 289 ? 144.837 105.937 152.620 1.00 20.77 ?  268 LEU D CD1   1 
ATOM   15559 C  CD2   . LEU D 2 289 ? 143.052 104.226 152.131 1.00 21.40 ?  268 LEU D CD2   1 
ATOM   15560 N  N     . MET D 2 290 ? 141.041 108.602 149.544 1.00 23.87 ?  269 MET D N     1 
ATOM   15561 C  CA    . MET D 2 290 ? 139.964 109.582 149.441 1.00 25.26 ?  269 MET D CA    1 
ATOM   15562 C  C     . MET D 2 290 ? 138.864 109.129 148.466 1.00 24.37 ?  269 MET D C     1 
ATOM   15563 O  O     . MET D 2 290 ? 137.687 109.331 148.748 1.00 23.97 ?  269 MET D O     1 
ATOM   15564 C  CB    . MET D 2 290 ? 140.507 110.980 149.160 1.00 25.94 ?  269 MET D CB    1 
ATOM   15565 C  CG    . MET D 2 290 ? 141.052 111.631 150.446 1.00 31.08 ?  269 MET D CG    1 
ATOM   15566 S  SD    . MET D 2 290 ? 141.749 113.282 150.214 1.00 41.28 ?  269 MET D SD    1 
ATOM   15567 C  CE    . MET D 2 290 ? 140.391 114.131 149.366 1.00 38.56 ?  269 MET D CE    1 
ATOM   15568 N  N     . ASN D 2 291 ? 139.242 108.474 147.363 1.00 23.66 ?  270 ASN D N     1 
ATOM   15569 C  CA    . ASN D 2 291 ? 138.253 107.848 146.454 1.00 23.17 ?  270 ASN D CA    1 
ATOM   15570 C  C     . ASN D 2 291 ? 137.322 106.840 147.133 1.00 23.22 ?  270 ASN D C     1 
ATOM   15571 O  O     . ASN D 2 291 ? 136.177 106.667 146.717 1.00 22.68 ?  270 ASN D O     1 
ATOM   15572 C  CB    . ASN D 2 291 ? 138.934 107.173 145.253 1.00 22.41 ?  270 ASN D CB    1 
ATOM   15573 C  CG    . ASN D 2 291 ? 139.546 108.168 144.294 1.00 21.93 ?  270 ASN D CG    1 
ATOM   15574 O  OD1   . ASN D 2 291 ? 139.269 109.370 144.364 1.00 20.94 ?  270 ASN D OD1   1 
ATOM   15575 N  ND2   . ASN D 2 291 ? 140.385 107.675 143.387 1.00 19.20 ?  270 ASN D ND2   1 
ATOM   15576 N  N     . LEU D 2 292 ? 137.833 106.182 148.173 1.00 23.53 ?  271 LEU D N     1 
ATOM   15577 C  CA    . LEU D 2 292 ? 137.069 105.201 148.948 1.00 24.21 ?  271 LEU D CA    1 
ATOM   15578 C  C     . LEU D 2 292 ? 136.398 105.831 150.173 1.00 25.14 ?  271 LEU D C     1 
ATOM   15579 O  O     . LEU D 2 292 ? 135.865 105.122 151.041 1.00 25.14 ?  271 LEU D O     1 
ATOM   15580 C  CB    . LEU D 2 292 ? 137.976 104.023 149.364 1.00 23.71 ?  271 LEU D CB    1 
ATOM   15581 C  CG    . LEU D 2 292 ? 138.564 103.150 148.246 1.00 23.37 ?  271 LEU D CG    1 
ATOM   15582 C  CD1   . LEU D 2 292 ? 139.730 102.306 148.767 1.00 23.28 ?  271 LEU D CD1   1 
ATOM   15583 C  CD2   . LEU D 2 292 ? 137.490 102.256 147.595 1.00 23.06 ?  271 LEU D CD2   1 
ATOM   15584 N  N     . GLY D 2 293 ? 136.419 107.164 150.232 1.00 25.82 ?  272 GLY D N     1 
ATOM   15585 C  CA    . GLY D 2 293 ? 135.813 107.909 151.329 1.00 27.13 ?  272 GLY D CA    1 
ATOM   15586 C  C     . GLY D 2 293 ? 136.556 107.806 152.645 1.00 27.99 ?  272 GLY D C     1 
ATOM   15587 O  O     . GLY D 2 293 ? 135.984 108.081 153.696 1.00 27.97 ?  272 GLY D O     1 
ATOM   15588 N  N     . PHE D 2 294 ? 137.830 107.407 152.590 1.00 28.02 ?  273 PHE D N     1 
ATOM   15589 C  CA    . PHE D 2 294 ? 138.667 107.276 153.790 1.00 28.75 ?  273 PHE D CA    1 
ATOM   15590 C  C     . PHE D 2 294 ? 139.633 108.455 153.960 1.00 29.00 ?  273 PHE D C     1 
ATOM   15591 O  O     . PHE D 2 294 ? 139.928 109.166 153.001 1.00 28.74 ?  273 PHE D O     1 
ATOM   15592 C  CB    . PHE D 2 294 ? 139.468 105.964 153.745 1.00 28.32 ?  273 PHE D CB    1 
ATOM   15593 C  CG    . PHE D 2 294 ? 138.616 104.725 153.794 1.00 28.66 ?  273 PHE D CG    1 
ATOM   15594 C  CD1   . PHE D 2 294 ? 137.521 104.645 154.654 1.00 30.23 ?  273 PHE D CD1   1 
ATOM   15595 C  CD2   . PHE D 2 294 ? 138.919 103.634 152.991 1.00 26.94 ?  273 PHE D CD2   1 
ATOM   15596 C  CE1   . PHE D 2 294 ? 136.729 103.492 154.699 1.00 31.04 ?  273 PHE D CE1   1 
ATOM   15597 C  CE2   . PHE D 2 294 ? 138.146 102.482 153.029 1.00 27.39 ?  273 PHE D CE2   1 
ATOM   15598 C  CZ    . PHE D 2 294 ? 137.052 102.401 153.881 1.00 29.80 ?  273 PHE D CZ    1 
ATOM   15599 N  N     . ASP D 2 295 ? 140.117 108.653 155.185 1.00 29.60 ?  274 ASP D N     1 
ATOM   15600 C  CA    . ASP D 2 295 ? 141.095 109.699 155.477 1.00 30.40 ?  274 ASP D CA    1 
ATOM   15601 C  C     . ASP D 2 295 ? 142.472 109.376 154.866 1.00 29.58 ?  274 ASP D C     1 
ATOM   15602 O  O     . ASP D 2 295 ? 142.815 108.206 154.692 1.00 28.68 ?  274 ASP D O     1 
ATOM   15603 C  CB    . ASP D 2 295 ? 141.239 109.899 156.992 1.00 31.44 ?  274 ASP D CB    1 
ATOM   15604 C  CG    . ASP D 2 295 ? 139.970 110.432 157.647 1.00 34.27 ?  274 ASP D CG    1 
ATOM   15605 O  OD1   . ASP D 2 295 ? 139.182 111.144 156.980 1.00 36.43 ?  274 ASP D OD1   1 
ATOM   15606 O  OD2   . ASP D 2 295 ? 139.770 110.134 158.844 1.00 38.03 -1 274 ASP D OD2   1 
ATOM   15607 N  N     . PRO D 2 296 ? 143.267 110.416 154.550 1.00 29.59 ?  275 PRO D N     1 
ATOM   15608 C  CA    . PRO D 2 296 ? 144.620 110.145 154.056 1.00 29.09 ?  275 PRO D CA    1 
ATOM   15609 C  C     . PRO D 2 296 ? 145.448 109.411 155.111 1.00 29.26 ?  275 PRO D C     1 
ATOM   15610 O  O     . PRO D 2 296 ? 145.282 109.646 156.308 1.00 29.36 ?  275 PRO D O     1 
ATOM   15611 C  CB    . PRO D 2 296 ? 145.199 111.543 153.797 1.00 29.49 ?  275 PRO D CB    1 
ATOM   15612 C  CG    . PRO D 2 296 ? 144.331 112.491 154.578 1.00 30.28 ?  275 PRO D CG    1 
ATOM   15613 C  CD    . PRO D 2 296 ? 142.973 111.861 154.619 1.00 29.63 ?  275 PRO D CD    1 
ATOM   15614 N  N     . TYR D 2 297 ? 146.314 108.514 154.665 1.00 28.97 ?  276 TYR D N     1 
ATOM   15615 C  CA    . TYR D 2 297 ? 147.129 107.714 155.571 1.00 29.63 ?  276 TYR D CA    1 
ATOM   15616 C  C     . TYR D 2 297 ? 148.498 108.368 155.820 1.00 29.55 ?  276 TYR D C     1 
ATOM   15617 O  O     . TYR D 2 297 ? 149.062 108.274 156.918 1.00 30.12 ?  276 TYR D O     1 
ATOM   15618 C  CB    . TYR D 2 297 ? 147.317 106.324 154.962 1.00 29.49 ?  276 TYR D CB    1 
ATOM   15619 C  CG    . TYR D 2 297 ? 147.861 105.278 155.898 1.00 31.19 ?  276 TYR D CG    1 
ATOM   15620 C  CD1   . TYR D 2 297 ? 147.144 104.895 157.036 1.00 31.93 ?  276 TYR D CD1   1 
ATOM   15621 C  CD2   . TYR D 2 297 ? 149.079 104.648 155.637 1.00 31.98 ?  276 TYR D CD2   1 
ATOM   15622 C  CE1   . TYR D 2 297 ? 147.633 103.924 157.901 1.00 33.86 ?  276 TYR D CE1   1 
ATOM   15623 C  CE2   . TYR D 2 297 ? 149.577 103.667 156.496 1.00 33.88 ?  276 TYR D CE2   1 
ATOM   15624 C  CZ    . TYR D 2 297 ? 148.841 103.312 157.621 1.00 34.42 ?  276 TYR D CZ    1 
ATOM   15625 O  OH    . TYR D 2 297 ? 149.315 102.356 158.482 1.00 37.63 ?  276 TYR D OH    1 
ATOM   15626 N  N     . PHE D 2 298 ? 149.014 109.022 154.786 1.00 29.10 ?  277 PHE D N     1 
ATOM   15627 C  CA    . PHE D 2 298 ? 150.360 109.586 154.783 1.00 28.97 ?  277 PHE D CA    1 
ATOM   15628 C  C     . PHE D 2 298 ? 150.313 111.112 154.922 1.00 29.77 ?  277 PHE D C     1 
ATOM   15629 O  O     . PHE D 2 298 ? 149.371 111.757 154.455 1.00 29.07 ?  277 PHE D O     1 
ATOM   15630 C  CB    . PHE D 2 298 ? 151.081 109.214 153.482 1.00 27.99 ?  277 PHE D CB    1 
ATOM   15631 C  CG    . PHE D 2 298 ? 151.251 107.728 153.275 1.00 27.61 ?  277 PHE D CG    1 
ATOM   15632 C  CD1   . PHE D 2 298 ? 150.503 107.054 152.319 1.00 25.91 ?  277 PHE D CD1   1 
ATOM   15633 C  CD2   . PHE D 2 298 ? 152.180 107.008 154.028 1.00 27.32 ?  277 PHE D CD2   1 
ATOM   15634 C  CE1   . PHE D 2 298 ? 150.666 105.694 152.123 1.00 26.65 ?  277 PHE D CE1   1 
ATOM   15635 C  CE2   . PHE D 2 298 ? 152.355 105.648 153.842 1.00 25.38 ?  277 PHE D CE2   1 
ATOM   15636 C  CZ    . PHE D 2 298 ? 151.596 104.983 152.898 1.00 26.20 ?  277 PHE D CZ    1 
ATOM   15637 N  N     . GLU D 2 299 ? 151.332 111.674 155.572 1.00 31.10 ?  278 GLU D N     1 
ATOM   15638 C  CA    . GLU D 2 299 ? 151.491 113.128 155.667 1.00 32.86 ?  278 GLU D CA    1 
ATOM   15639 C  C     . GLU D 2 299 ? 151.651 113.727 154.263 1.00 33.04 ?  278 GLU D C     1 
ATOM   15640 O  O     . GLU D 2 299 ? 152.163 113.070 153.353 1.00 32.23 ?  278 GLU D O     1 
ATOM   15641 C  CB    . GLU D 2 299 ? 152.695 113.489 156.554 1.00 33.45 ?  278 GLU D CB    1 
ATOM   15642 C  CG    . GLU D 2 299 ? 154.037 112.973 156.011 1.00 36.27 ?  278 GLU D CG    1 
ATOM   15643 C  CD    . GLU D 2 299 ? 155.257 113.433 156.795 1.00 40.47 ?  278 GLU D CD    1 
ATOM   15644 O  OE1   . GLU D 2 299 ? 155.211 113.466 158.047 1.00 41.72 ?  278 GLU D OE1   1 
ATOM   15645 O  OE2   . GLU D 2 299 ? 156.279 113.734 156.141 1.00 42.65 -1 278 GLU D OE2   1 
ATOM   15646 N  N     . GLU D 2 300 ? 151.203 114.971 154.106 1.00 34.09 ?  279 GLU D N     1 
ATOM   15647 C  CA    . GLU D 2 300 ? 151.304 115.693 152.845 1.00 35.06 ?  279 GLU D CA    1 
ATOM   15648 C  C     . GLU D 2 300 ? 152.769 115.979 152.513 1.00 34.97 ?  279 GLU D C     1 
ATOM   15649 O  O     . GLU D 2 300 ? 153.544 116.391 153.379 1.00 34.96 ?  279 GLU D O     1 
ATOM   15650 C  CB    . GLU D 2 300 ? 150.493 116.999 152.916 1.00 35.81 ?  279 GLU D CB    1 
ATOM   15651 C  CG    . GLU D 2 300 ? 150.375 117.741 151.583 1.00 38.58 ?  279 GLU D CG    1 
ATOM   15652 C  CD    . GLU D 2 300 ? 149.147 118.646 151.505 1.00 43.09 ?  279 GLU D CD    1 
ATOM   15653 O  OE1   . GLU D 2 300 ? 148.337 118.466 150.568 1.00 44.69 ?  279 GLU D OE1   1 
ATOM   15654 O  OE2   . GLU D 2 300 ? 148.986 119.527 152.381 1.00 44.94 -1 279 GLU D OE2   1 
ATOM   15655 N  N     . GLU D 2 301 ? 153.138 115.729 151.261 1.00 34.73 ?  280 GLU D N     1 
ATOM   15656 C  CA    . GLU D 2 301 ? 154.487 115.981 150.771 1.00 35.16 ?  280 GLU D CA    1 
ATOM   15657 C  C     . GLU D 2 301 ? 154.401 116.718 149.445 1.00 35.23 ?  280 GLU D C     1 
ATOM   15658 O  O     . GLU D 2 301 ? 153.418 116.577 148.711 1.00 34.92 ?  280 GLU D O     1 
ATOM   15659 C  CB    . GLU D 2 301 ? 155.242 114.660 150.570 1.00 35.10 ?  280 GLU D CB    1 
ATOM   15660 C  CG    . GLU D 2 301 ? 155.833 114.056 151.842 1.00 36.62 ?  280 GLU D CG    1 
ATOM   15661 C  CD    . GLU D 2 301 ? 156.332 112.625 151.644 1.00 37.59 ?  280 GLU D CD    1 
ATOM   15662 O  OE1   . GLU D 2 301 ? 155.535 111.757 151.230 1.00 38.10 ?  280 GLU D OE1   1 
ATOM   15663 O  OE2   . GLU D 2 301 ? 157.516 112.359 151.929 1.00 38.93 -1 280 GLU D OE2   1 
ATOM   15664 N  N     . ASP D 2 302 ? 155.425 117.503 149.135 1.00 35.60 ?  281 ASP D N     1 
ATOM   15665 C  CA    . ASP D 2 302 ? 155.492 118.157 147.834 1.00 35.96 ?  281 ASP D CA    1 
ATOM   15666 C  C     . ASP D 2 302 ? 155.992 117.146 146.810 1.00 35.01 ?  281 ASP D C     1 
ATOM   15667 O  O     . ASP D 2 302 ? 156.699 116.203 147.164 1.00 35.52 ?  281 ASP D O     1 
ATOM   15668 C  CB    . ASP D 2 302 ? 156.369 119.421 147.885 1.00 36.82 ?  281 ASP D CB    1 
ATOM   15669 C  CG    . ASP D 2 302 ? 157.843 119.130 148.222 1.00 39.01 ?  281 ASP D CG    1 
ATOM   15670 O  OD1   . ASP D 2 302 ? 158.169 118.063 148.801 1.00 40.83 ?  281 ASP D OD1   1 
ATOM   15671 O  OD2   . ASP D 2 302 ? 158.682 120.002 147.918 1.00 41.13 -1 281 ASP D OD2   1 
ATOM   15672 N  N     . ILE D 2 303 ? 155.598 117.311 145.555 1.00 33.94 ?  282 ILE D N     1 
ATOM   15673 C  CA    . ILE D 2 303 ? 156.013 116.383 144.505 1.00 33.00 ?  282 ILE D CA    1 
ATOM   15674 C  C     . ILE D 2 303 ? 157.076 116.994 143.581 1.00 31.59 ?  282 ILE D C     1 
ATOM   15675 O  O     . ILE D 2 303 ? 157.129 118.213 143.407 1.00 31.14 ?  282 ILE D O     1 
ATOM   15676 C  CB    . ILE D 2 303 ? 154.783 115.818 143.724 1.00 33.44 ?  282 ILE D CB    1 
ATOM   15677 C  CG1   . ILE D 2 303 ? 155.130 115.486 142.268 1.00 34.29 ?  282 ILE D CG1   1 
ATOM   15678 C  CG2   . ILE D 2 303 ? 153.606 116.776 143.809 1.00 35.47 ?  282 ILE D CG2   1 
ATOM   15679 C  CD1   . ILE D 2 303 ? 153.934 115.125 141.411 1.00 36.30 ?  282 ILE D CD1   1 
ATOM   15680 N  N     . ASN D 2 304 ? 157.930 116.139 143.018 1.00 29.53 ?  283 ASN D N     1 
ATOM   15681 C  CA    . ASN D 2 304 ? 158.934 116.569 142.049 1.00 28.49 ?  283 ASN D CA    1 
ATOM   15682 C  C     . ASN D 2 304 ? 158.330 117.514 140.988 1.00 27.87 ?  283 ASN D C     1 
ATOM   15683 O  O     . ASN D 2 304 ? 157.352 117.159 140.332 1.00 27.02 ?  283 ASN D O     1 
ATOM   15684 C  CB    . ASN D 2 304 ? 159.570 115.349 141.380 1.00 28.20 ?  283 ASN D CB    1 
ATOM   15685 C  CG    . ASN D 2 304 ? 160.681 115.725 140.436 1.00 28.17 ?  283 ASN D CG    1 
ATOM   15686 O  OD1   . ASN D 2 304 ? 160.436 116.036 139.274 1.00 29.01 ?  283 ASN D OD1   1 
ATOM   15687 N  ND2   . ASN D 2 304 ? 161.911 115.700 140.924 1.00 27.24 ?  283 ASN D ND2   1 
ATOM   15688 N  N     . PRO D 2 305 ? 158.903 118.725 140.832 1.00 28.00 ?  284 PRO D N     1 
ATOM   15689 C  CA    . PRO D 2 305 ? 158.314 119.726 139.928 1.00 27.58 ?  284 PRO D CA    1 
ATOM   15690 C  C     . PRO D 2 305 ? 158.349 119.347 138.446 1.00 27.01 ?  284 PRO D C     1 
ATOM   15691 O  O     . PRO D 2 305 ? 157.525 119.829 137.676 1.00 26.66 ?  284 PRO D O     1 
ATOM   15692 C  CB    . PRO D 2 305 ? 159.162 120.981 140.177 1.00 28.21 ?  284 PRO D CB    1 
ATOM   15693 C  CG    . PRO D 2 305 ? 160.409 120.505 140.783 1.00 28.80 ?  284 PRO D CG    1 
ATOM   15694 C  CD    . PRO D 2 305 ? 160.032 119.287 141.597 1.00 28.11 ?  284 PRO D CD    1 
ATOM   15695 N  N     . ILE D 2 306 ? 159.287 118.489 138.054 1.00 26.52 ?  285 ILE D N     1 
ATOM   15696 C  CA    . ILE D 2 306 ? 159.356 118.028 136.673 1.00 26.50 ?  285 ILE D CA    1 
ATOM   15697 C  C     . ILE D 2 306 ? 158.167 117.106 136.368 1.00 26.43 ?  285 ILE D C     1 
ATOM   15698 O  O     . ILE D 2 306 ? 157.468 117.275 135.358 1.00 26.00 ?  285 ILE D O     1 
ATOM   15699 C  CB    . ILE D 2 306 ? 160.716 117.357 136.356 1.00 26.88 ?  285 ILE D CB    1 
ATOM   15700 C  CG1   . ILE D 2 306 ? 161.858 118.367 136.572 1.00 26.98 ?  285 ILE D CG1   1 
ATOM   15701 C  CG2   . ILE D 2 306 ? 160.706 116.803 134.931 1.00 24.94 ?  285 ILE D CG2   1 
ATOM   15702 C  CD1   . ILE D 2 306 ? 163.245 117.792 136.480 1.00 26.65 ?  285 ILE D CD1   1 
ATOM   15703 N  N     . VAL D 2 307 ? 157.926 116.158 137.266 1.00 26.36 ?  286 VAL D N     1 
ATOM   15704 C  CA    . VAL D 2 307 ? 156.737 115.317 137.195 1.00 26.71 ?  286 VAL D CA    1 
ATOM   15705 C  C     . VAL D 2 307 ? 155.451 116.147 137.265 1.00 27.68 ?  286 VAL D C     1 
ATOM   15706 O  O     . VAL D 2 307 ? 154.521 115.889 136.501 1.00 27.92 ?  286 VAL D O     1 
ATOM   15707 C  CB    . VAL D 2 307 ? 156.771 114.186 138.259 1.00 26.37 ?  286 VAL D CB    1 
ATOM   15708 C  CG1   . VAL D 2 307 ? 155.420 113.459 138.354 1.00 25.48 ?  286 VAL D CG1   1 
ATOM   15709 C  CG2   . VAL D 2 307 ? 157.845 113.211 137.897 1.00 25.55 ?  286 VAL D CG2   1 
ATOM   15710 N  N     . LEU D 2 308 ? 155.406 117.160 138.136 1.00 28.80 ?  287 LEU D N     1 
ATOM   15711 C  CA    . LEU D 2 308 ? 154.252 118.074 138.163 1.00 30.07 ?  287 LEU D CA    1 
ATOM   15712 C  C     . LEU D 2 308 ? 154.020 118.769 136.818 1.00 30.38 ?  287 LEU D C     1 
ATOM   15713 O  O     . LEU D 2 308 ? 152.879 118.903 136.363 1.00 30.71 ?  287 LEU D O     1 
ATOM   15714 C  CB    . LEU D 2 308 ? 154.383 119.115 139.278 1.00 30.86 ?  287 LEU D CB    1 
ATOM   15715 C  CG    . LEU D 2 308 ? 153.914 118.668 140.667 1.00 32.62 ?  287 LEU D CG    1 
ATOM   15716 C  CD1   . LEU D 2 308 ? 154.281 119.697 141.714 1.00 33.97 ?  287 LEU D CD1   1 
ATOM   15717 C  CD2   . LEU D 2 308 ? 152.401 118.384 140.689 1.00 34.73 ?  287 LEU D CD2   1 
ATOM   15718 N  N     . ASN D 2 309 ? 155.100 119.202 136.177 1.00 30.81 ?  288 ASN D N     1 
ATOM   15719 C  CA    . ASN D 2 309 ? 154.994 119.834 134.866 1.00 31.25 ?  288 ASN D CA    1 
ATOM   15720 C  C     . ASN D 2 309 ? 154.468 118.860 133.811 1.00 31.83 ?  288 ASN D C     1 
ATOM   15721 O  O     . ASN D 2 309 ? 153.737 119.258 132.899 1.00 31.73 ?  288 ASN D O     1 
ATOM   15722 C  CB    . ASN D 2 309 ? 156.325 120.456 134.431 1.00 31.21 ?  288 ASN D CB    1 
ATOM   15723 C  CG    . ASN D 2 309 ? 156.187 121.288 133.166 1.00 31.41 ?  288 ASN D CG    1 
ATOM   15724 O  OD1   . ASN D 2 309 ? 155.240 122.070 133.026 1.00 31.88 ?  288 ASN D OD1   1 
ATOM   15725 N  ND2   . ASN D 2 309 ? 157.122 121.119 132.237 1.00 29.12 ?  288 ASN D ND2   1 
ATOM   15726 N  N     . GLY D 2 310 ? 154.837 117.586 133.949 1.00 32.04 ?  289 GLY D N     1 
ATOM   15727 C  CA    . GLY D 2 310 ? 154.292 116.523 133.113 1.00 33.04 ?  289 GLY D CA    1 
ATOM   15728 C  C     . GLY D 2 310 ? 152.802 116.327 133.363 1.00 33.85 ?  289 GLY D C     1 
ATOM   15729 O  O     . GLY D 2 310 ? 152.017 116.256 132.417 1.00 34.05 ?  289 GLY D O     1 
ATOM   15730 N  N     . LEU D 2 311 ? 152.417 116.246 134.636 1.00 34.33 ?  290 LEU D N     1 
ATOM   15731 C  CA    . LEU D 2 311 ? 151.023 116.037 135.035 1.00 35.77 ?  290 LEU D CA    1 
ATOM   15732 C  C     . LEU D 2 311 ? 150.091 117.158 134.586 1.00 37.01 ?  290 LEU D C     1 
ATOM   15733 O  O     . LEU D 2 311 ? 148.966 116.902 134.156 1.00 37.18 ?  290 LEU D O     1 
ATOM   15734 C  CB    . LEU D 2 311 ? 150.913 115.892 136.558 1.00 35.50 ?  290 LEU D CB    1 
ATOM   15735 C  CG    . LEU D 2 311 ? 151.009 114.531 137.242 1.00 35.45 ?  290 LEU D CG    1 
ATOM   15736 C  CD1   . LEU D 2 311 ? 151.054 114.735 138.765 1.00 35.28 ?  290 LEU D CD1   1 
ATOM   15737 C  CD2   . LEU D 2 311 ? 149.850 113.606 136.861 1.00 34.16 ?  290 LEU D CD2   1 
ATOM   15738 N  N     . LYS D 2 330 ? 120.152 114.603 147.810 1.00 42.55 ?  309 LYS D N     1 
ATOM   15739 C  CA    . LYS D 2 330 ? 118.757 114.360 147.464 1.00 44.90 ?  309 LYS D CA    1 
ATOM   15740 C  C     . LYS D 2 330 ? 117.945 113.905 148.671 1.00 43.76 ?  309 LYS D C     1 
ATOM   15741 O  O     . LYS D 2 330 ? 117.858 112.712 148.959 1.00 44.28 ?  309 LYS D O     1 
ATOM   15742 C  CB    . LYS D 2 330 ? 118.658 113.315 146.348 1.00 40.63 ?  309 LYS D CB    1 
ATOM   15743 C  CG    . LYS D 2 330 ? 117.288 113.240 145.689 1.00 43.98 ?  309 LYS D CG    1 
ATOM   15744 C  CD    . LYS D 2 330 ? 116.917 114.548 145.010 1.00 43.19 ?  309 LYS D CD    1 
ATOM   15745 C  CE    . LYS D 2 330 ? 116.923 114.404 143.497 1.00 45.38 ?  309 LYS D CE    1 
ATOM   15746 N  NZ    . LYS D 2 330 ? 116.858 115.723 142.812 1.00 43.90 1  309 LYS D NZ    1 
ATOM   15747 N  N     . ALA D 2 331 ? 117.354 114.865 149.377 1.00 41.98 ?  310 ALA D N     1 
ATOM   15748 C  CA    . ALA D 2 331 ? 116.463 114.545 150.478 1.00 42.36 ?  310 ALA D CA    1 
ATOM   15749 C  C     . ALA D 2 331 ? 115.146 113.988 149.947 1.00 42.70 ?  310 ALA D C     1 
ATOM   15750 O  O     . ALA D 2 331 ? 114.760 114.222 148.798 1.00 44.14 ?  310 ALA D O     1 
ATOM   15751 C  CB    . ALA D 2 331 ? 116.204 115.777 151.344 1.00 39.32 ?  310 ALA D CB    1 
ATOM   15752 N  N     . THR D 2 332 ? 114.457 113.238 150.801 1.00 33.29 ?  311 THR D N     1 
ATOM   15753 C  CA    . THR D 2 332 ? 113.210 112.580 150.417 1.00 32.46 ?  311 THR D CA    1 
ATOM   15754 C  C     . THR D 2 332 ? 112.157 113.643 150.138 1.00 32.78 ?  311 THR D C     1 
ATOM   15755 O  O     . THR D 2 332 ? 111.837 114.463 151.001 1.00 35.85 ?  311 THR D O     1 
ATOM   15756 C  CB    . THR D 2 332 ? 112.751 111.623 151.512 1.00 36.71 ?  311 THR D CB    1 
ATOM   15757 O  OG1   . THR D 2 332 ? 113.479 110.394 151.409 1.00 39.19 ?  311 THR D OG1   1 
ATOM   15758 C  CG2   . THR D 2 332 ? 111.264 111.326 151.371 1.00 34.82 ?  311 THR D CG2   1 
ATOM   15759 N  N     . VAL D 2 333 ? 111.623 113.644 148.919 1.00 30.31 ?  312 VAL D N     1 
ATOM   15760 C  CA    . VAL D 2 333 ? 110.583 114.592 148.538 1.00 24.24 ?  312 VAL D CA    1 
ATOM   15761 C  C     . VAL D 2 333 ? 109.255 114.128 149.117 1.00 30.13 ?  312 VAL D C     1 
ATOM   15762 O  O     . VAL D 2 333 ? 108.750 113.058 148.759 1.00 35.56 ?  312 VAL D O     1 
ATOM   15763 C  CB    . VAL D 2 333 ? 110.498 114.748 147.010 1.00 29.05 ?  312 VAL D CB    1 
ATOM   15764 C  CG1   . VAL D 2 333 ? 109.510 115.844 146.645 1.00 31.60 ?  312 VAL D CG1   1 
ATOM   15765 C  CG2   . VAL D 2 333 ? 111.872 115.043 146.430 1.00 29.59 ?  312 VAL D CG2   1 
ATOM   15766 N  N     . GLU D 2 334 ? 108.684 114.925 150.014 1.00 28.79 ?  313 GLU D N     1 
ATOM   15767 C  CA    . GLU D 2 334 ? 107.405 114.610 150.636 1.00 29.66 ?  313 GLU D CA    1 
ATOM   15768 C  C     . GLU D 2 334 ? 106.448 115.769 150.395 1.00 31.26 ?  313 GLU D C     1 
ATOM   15769 O  O     . GLU D 2 334 ? 106.761 116.912 150.767 1.00 34.83 ?  313 GLU D O     1 
ATOM   15770 C  CB    . GLU D 2 334 ? 107.574 114.348 152.134 1.00 29.26 ?  313 GLU D CB    1 
ATOM   15771 C  CG    . GLU D 2 334 ? 106.276 114.334 152.918 1.00 33.58 ?  313 GLU D CG    1 
ATOM   15772 C  CD    . GLU D 2 334 ? 106.474 113.896 154.357 1.00 35.28 ?  313 GLU D CD    1 
ATOM   15773 O  OE1   . GLU D 2 334 ? 107.554 114.171 154.919 1.00 33.47 ?  313 GLU D OE1   1 
ATOM   15774 O  OE2   . GLU D 2 334 ? 105.550 113.276 154.924 1.00 31.19 -1 313 GLU D OE2   1 
ATOM   15775 N  N     . PRO D 2 335 ? 105.292 115.536 149.774 1.00 31.21 ?  314 PRO D N     1 
ATOM   15776 C  CA    . PRO D 2 335 ? 104.399 116.648 149.430 1.00 33.35 ?  314 PRO D CA    1 
ATOM   15777 C  C     . PRO D 2 335 ? 103.858 117.347 150.669 1.00 33.18 ?  314 PRO D C     1 
ATOM   15778 O  O     . PRO D 2 335 ? 103.692 116.739 151.729 1.00 33.38 ?  314 PRO D O     1 
ATOM   15779 C  CB    . PRO D 2 335 ? 103.278 115.966 148.637 1.00 30.11 ?  314 PRO D CB    1 
ATOM   15780 C  CG    . PRO D 2 335 ? 103.337 114.530 149.055 1.00 31.03 ?  314 PRO D CG    1 
ATOM   15781 C  CD    . PRO D 2 335 ? 104.787 114.249 149.273 1.00 33.22 ?  314 PRO D CD    1 
ATOM   15782 N  N     . LEU D 2 336 ? 103.589 118.642 150.527 1.00 30.38 ?  315 LEU D N     1 
ATOM   15783 C  CA    . LEU D 2 336 ? 102.944 119.397 151.588 1.00 26.61 ?  315 LEU D CA    1 
ATOM   15784 C  C     . LEU D 2 336 ? 101.502 118.935 151.749 1.00 27.64 ?  315 LEU D C     1 
ATOM   15785 O  O     . LEU D 2 336 ? 100.733 118.879 150.786 1.00 34.77 ?  315 LEU D O     1 
ATOM   15786 C  CB    . LEU D 2 336 ? 102.994 120.895 151.286 1.00 22.39 ?  315 LEU D CB    1 
ATOM   15787 C  CG    . LEU D 2 336 ? 104.284 121.614 151.684 1.00 25.97 ?  315 LEU D CG    1 
ATOM   15788 C  CD1   . LEU D 2 336 ? 104.257 123.062 151.225 1.00 19.59 ?  315 LEU D CD1   1 
ATOM   15789 C  CD2   . LEU D 2 336 ? 104.516 121.528 153.185 1.00 27.01 ?  315 LEU D CD2   1 
ATOM   15790 N  N     . LYS D 2 337 ? 101.138 118.605 152.988 1.00 28.30 ?  316 LYS D N     1 
ATOM   15791 C  CA    . LYS D 2 337 ? 99.864  117.957 153.281 1.00 36.46 ?  316 LYS D CA    1 
ATOM   15792 C  C     . LYS D 2 337 ? 98.798  118.928 153.766 1.00 36.32 ?  316 LYS D C     1 
ATOM   15793 O  O     . LYS D 2 337 ? 97.759  118.481 154.266 1.00 40.02 ?  316 LYS D O     1 
ATOM   15794 C  CB    . LYS D 2 337 ? 100.060 116.855 154.326 1.00 33.57 ?  316 LYS D CB    1 
ATOM   15795 C  CG    . LYS D 2 337 ? 101.271 115.976 154.086 1.00 36.47 ?  316 LYS D CG    1 
ATOM   15796 C  CD    . LYS D 2 337 ? 100.923 114.509 154.260 1.00 38.79 ?  316 LYS D CD    1 
ATOM   15797 C  CE    . LYS D 2 337 ? 102.175 113.656 154.327 1.00 37.56 ?  316 LYS D CE    1 
ATOM   15798 N  NZ    . LYS D 2 337 ? 103.022 113.841 153.119 1.00 36.72 1  316 LYS D NZ    1 
ATOM   15799 N  N     . ASP D 2 338 ? 99.036  120.238 153.652 1.00 24.38 ?  317 ASP D N     1 
ATOM   15800 C  CA    . ASP D 2 338 ? 98.184  121.270 154.240 1.00 29.04 ?  317 ASP D CA    1 
ATOM   15801 C  C     . ASP D 2 338 ? 98.216  121.158 155.762 1.00 28.87 ?  317 ASP D C     1 
ATOM   15802 O  O     . ASP D 2 338 ? 98.693  120.156 156.305 1.00 33.66 ?  317 ASP D O     1 
ATOM   15803 C  CB    . ASP D 2 338 ? 96.750  121.187 153.705 1.00 31.69 ?  317 ASP D CB    1 
ATOM   15804 C  CG    . ASP D 2 338 ? 95.933  122.421 154.029 1.00 32.42 ?  317 ASP D CG    1 
ATOM   15805 O  OD1   . ASP D 2 338 ? 96.538  123.478 154.303 1.00 34.34 ?  317 ASP D OD1   1 
ATOM   15806 O  OD2   . ASP D 2 338 ? 94.688  122.336 154.007 1.00 28.35 -1 317 ASP D OD2   1 
ATOM   15807 N  N     . ASP D 2 339 ? 97.759  122.204 156.453 1.00 22.82 ?  318 ASP D N     1 
ATOM   15808 C  CA    . ASP D 2 339 ? 97.881  122.332 157.904 1.00 24.73 ?  318 ASP D CA    1 
ATOM   15809 C  C     . ASP D 2 339 ? 99.347  122.474 158.298 1.00 24.49 ?  318 ASP D C     1 
ATOM   15810 O  O     . ASP D 2 339 ? 99.671  122.617 159.481 1.00 31.22 ?  318 ASP D O     1 
ATOM   15811 C  CB    . ASP D 2 339 ? 97.227  121.152 158.632 1.00 23.30 ?  318 ASP D CB    1 
ATOM   15812 C  CG    . ASP D 2 339 ? 95.864  120.804 158.067 1.00 31.35 ?  318 ASP D CG    1 
ATOM   15813 O  OD1   . ASP D 2 339 ? 94.953  121.656 158.143 1.00 29.84 ?  318 ASP D OD1   1 
ATOM   15814 O  OD2   . ASP D 2 339 ? 95.703  119.681 157.545 1.00 30.37 -1 318 ASP D OD2   1 
ATOM   15815 N  N     . ASP D 2 340 ? 100.239 122.431 157.309 1.00 24.54 ?  319 ASP D N     1 
ATOM   15816 C  CA    . ASP D 2 340 ? 101.621 122.856 157.459 1.00 16.40 ?  319 ASP D CA    1 
ATOM   15817 C  C     . ASP D 2 340 ? 101.765 124.355 157.264 1.00 13.50 ?  319 ASP D C     1 
ATOM   15818 O  O     . ASP D 2 340 ? 102.844 124.906 157.500 1.00 33.12 ?  319 ASP D O     1 
ATOM   15819 C  CB    . ASP D 2 340 ? 102.513 122.113 156.462 1.00 15.31 ?  319 ASP D CB    1 
ATOM   15820 C  CG    . ASP D 2 340 ? 102.632 120.636 156.773 1.00 20.12 ?  319 ASP D CG    1 
ATOM   15821 O  OD1   . ASP D 2 340 ? 102.557 120.267 157.964 1.00 32.00 ?  319 ASP D OD1   1 
ATOM   15822 O  OD2   . ASP D 2 340 ? 102.801 119.842 155.825 1.00 22.25 -1 319 ASP D OD2   1 
ATOM   15823 N  N     . PHE D 2 341 ? 100.691 125.020 156.833 1.00 10.33 ?  320 PHE D N     1 
ATOM   15824 C  CA    . PHE D 2 341 ? 100.655 126.464 156.667 1.00 15.27 ?  320 PHE D CA    1 
ATOM   15825 C  C     . PHE D 2 341 ? 100.027 127.150 157.871 1.00 19.34 ?  320 PHE D C     1 
ATOM   15826 O  O     . PHE D 2 341 ? 99.907  128.380 157.879 1.00 16.81 ?  320 PHE D O     1 
ATOM   15827 C  CB    . PHE D 2 341 ? 99.874  126.833 155.401 1.00 19.36 ?  320 PHE D CB    1 
ATOM   15828 C  CG    . PHE D 2 341 ? 100.510 126.350 154.131 1.00 13.21 ?  320 PHE D CG    1 
ATOM   15829 C  CD1   . PHE D 2 341 ? 101.409 127.146 153.442 1.00 12.45 ?  320 PHE D CD1   1 
ATOM   15830 C  CD2   . PHE D 2 341 ? 100.210 125.097 153.627 1.00 11.41 ?  320 PHE D CD2   1 
ATOM   15831 C  CE1   . PHE D 2 341 ? 101.990 126.701 152.272 1.00 11.53 ?  320 PHE D CE1   1 
ATOM   15832 C  CE2   . PHE D 2 341 ? 100.791 124.648 152.459 1.00 15.13 ?  320 PHE D CE2   1 
ATOM   15833 C  CZ    . PHE D 2 341 ? 101.683 125.451 151.782 1.00 8.25  ?  320 PHE D CZ    1 
ATOM   15834 N  N     . TYR D 2 342 ? 99.620  126.387 158.882 1.00 12.30 ?  321 TYR D N     1 
ATOM   15835 C  CA    . TYR D 2 342 ? 98.930  126.914 160.048 1.00 16.33 ?  321 TYR D CA    1 
ATOM   15836 C  C     . TYR D 2 342 ? 99.678  126.487 161.300 1.00 22.82 ?  321 TYR D C     1 
ATOM   15837 O  O     . TYR D 2 342 ? 100.197 125.369 161.372 1.00 19.28 ?  321 TYR D O     1 
ATOM   15838 C  CB    . TYR D 2 342 ? 97.481  126.420 160.100 1.00 12.46 ?  321 TYR D CB    1 
ATOM   15839 C  CG    . TYR D 2 342 ? 96.667  126.815 158.891 1.00 15.87 ?  321 TYR D CG    1 
ATOM   15840 C  CD1   . TYR D 2 342 ? 96.057  128.059 158.814 1.00 18.56 ?  321 TYR D CD1   1 
ATOM   15841 C  CD2   . TYR D 2 342 ? 96.514  125.944 157.820 1.00 15.63 ?  321 TYR D CD2   1 
ATOM   15842 C  CE1   . TYR D 2 342 ? 95.316  128.425 157.708 1.00 14.14 ?  321 TYR D CE1   1 
ATOM   15843 C  CE2   . TYR D 2 342 ? 95.774  126.301 156.709 1.00 15.01 ?  321 TYR D CE2   1 
ATOM   15844 C  CZ    . TYR D 2 342 ? 95.177  127.541 156.659 1.00 17.53 ?  321 TYR D CZ    1 
ATOM   15845 O  OH    . TYR D 2 342 ? 94.438  127.900 155.555 1.00 21.36 ?  321 TYR D OH    1 
ATOM   15846 N  N     . PHE D 2 343 ? 99.736  127.383 162.278 1.00 12.45 ?  322 PHE D N     1 
ATOM   15847 C  CA    . PHE D 2 343 ? 100.520 127.144 163.482 1.00 16.01 ?  322 PHE D CA    1 
ATOM   15848 C  C     . PHE D 2 343 ? 99.777  127.620 164.725 1.00 27.60 ?  322 PHE D C     1 
ATOM   15849 O  O     . PHE D 2 343 ? 98.928  128.509 164.654 1.00 22.19 ?  322 PHE D O     1 
ATOM   15850 C  CB    . PHE D 2 343 ? 101.879 127.842 163.373 1.00 18.28 ?  322 PHE D CB    1 
ATOM   15851 C  CG    . PHE D 2 343 ? 102.581 127.596 162.067 1.00 19.26 ?  322 PHE D CG    1 
ATOM   15852 C  CD1   . PHE D 2 343 ? 103.382 126.482 161.893 1.00 20.02 ?  322 PHE D CD1   1 
ATOM   15853 C  CD2   . PHE D 2 343 ? 102.424 128.473 161.007 1.00 13.80 ?  322 PHE D CD2   1 
ATOM   15854 C  CE1   . PHE D 2 343 ? 104.020 126.252 160.690 1.00 12.20 ?  322 PHE D CE1   1 
ATOM   15855 C  CE2   . PHE D 2 343 ? 103.057 128.247 159.804 1.00 9.90  ?  322 PHE D CE2   1 
ATOM   15856 C  CZ    . PHE D 2 343 ? 103.856 127.136 159.645 1.00 11.36 ?  322 PHE D CZ    1 
HETATM 15857 P  PG    . ATP E 3 .   ? 103.915 140.443 82.923  1.00 68.91 ?  801 ATP A PG    1 
HETATM 15858 O  O1G   . ATP E 3 .   ? 102.653 140.821 82.223  1.00 61.99 ?  801 ATP A O1G   1 
HETATM 15859 O  O2G   . ATP E 3 .   ? 105.052 141.454 82.733  1.00 61.48 -1 801 ATP A O2G   1 
HETATM 15860 O  O3G   . ATP E 3 .   ? 103.731 140.172 84.420  1.00 57.91 ?  801 ATP A O3G   1 
HETATM 15861 P  PB    . ATP E 3 .   ? 105.660 138.552 81.384  1.00 68.42 ?  801 ATP A PB    1 
HETATM 15862 O  O1B   . ATP E 3 .   ? 105.454 138.967 79.981  1.00 59.48 -1 801 ATP A O1B   1 
HETATM 15863 O  O2B   . ATP E 3 .   ? 106.985 138.985 82.013  1.00 59.06 ?  801 ATP A O2B   1 
HETATM 15864 O  O3B   . ATP E 3 .   ? 104.495 139.072 82.335  1.00 62.04 ?  801 ATP A O3B   1 
HETATM 15865 P  PA    . ATP E 3 .   ? 105.786 135.916 82.724  1.00 63.87 ?  801 ATP A PA    1 
HETATM 15866 O  O1A   . ATP E 3 .   ? 106.992 135.101 82.474  1.00 60.02 -1 801 ATP A O1A   1 
HETATM 15867 O  O2A   . ATP E 3 .   ? 104.492 135.117 82.880  1.00 58.33 ?  801 ATP A O2A   1 
HETATM 15868 O  O3A   . ATP E 3 .   ? 105.546 136.974 81.560  1.00 62.45 ?  801 ATP A O3A   1 
HETATM 15869 O  "O5'" . ATP E 3 .   ? 105.963 136.825 84.001  1.00 59.78 ?  801 ATP A "O5'" 1 
HETATM 15870 C  "C5'" . ATP E 3 .   ? 104.911 136.957 84.980  1.00 58.13 ?  801 ATP A "C5'" 1 
HETATM 15871 C  "C4'" . ATP E 3 .   ? 105.419 137.785 86.132  1.00 59.51 ?  801 ATP A "C4'" 1 
HETATM 15872 O  "O4'" . ATP E 3 .   ? 105.997 136.916 87.132  1.00 62.13 ?  801 ATP A "O4'" 1 
HETATM 15873 C  "C3'" . ATP E 3 .   ? 106.515 138.787 85.780  1.00 57.82 ?  801 ATP A "C3'" 1 
HETATM 15874 O  "O3'" . ATP E 3 .   ? 105.960 140.038 85.394  1.00 58.51 ?  801 ATP A "O3'" 1 
HETATM 15875 C  "C2'" . ATP E 3 .   ? 107.290 138.899 87.094  1.00 58.31 ?  801 ATP A "C2'" 1 
HETATM 15876 O  "O2'" . ATP E 3 .   ? 106.658 139.791 88.004  1.00 58.66 ?  801 ATP A "O2'" 1 
HETATM 15877 C  "C1'" . ATP E 3 .   ? 107.216 137.459 87.609  1.00 58.50 ?  801 ATP A "C1'" 1 
HETATM 15878 N  N9    . ATP E 3 .   ? 108.309 136.608 87.153  1.00 58.48 ?  801 ATP A N9    1 
HETATM 15879 C  C8    . ATP E 3 .   ? 108.220 135.508 86.340  1.00 58.26 ?  801 ATP A C8    1 
HETATM 15880 N  N7    . ATP E 3 .   ? 109.370 134.931 86.092  1.00 56.05 ?  801 ATP A N7    1 
HETATM 15881 C  C5    . ATP E 3 .   ? 110.283 135.704 86.792  1.00 58.55 ?  801 ATP A C5    1 
HETATM 15882 C  C6    . ATP E 3 .   ? 111.681 135.623 86.943  1.00 56.46 ?  801 ATP A C6    1 
HETATM 15883 N  N6    . ATP E 3 .   ? 112.438 134.682 86.371  1.00 55.74 ?  801 ATP A N6    1 
HETATM 15884 N  N1    . ATP E 3 .   ? 112.284 136.554 87.714  1.00 57.23 ?  801 ATP A N1    1 
HETATM 15885 C  C2    . ATP E 3 .   ? 111.536 137.501 88.285  1.00 55.67 ?  801 ATP A C2    1 
HETATM 15886 N  N3    . ATP E 3 .   ? 110.215 137.677 88.216  1.00 57.17 ?  801 ATP A N3    1 
HETATM 15887 C  C4    . ATP E 3 .   ? 109.643 136.742 87.451  1.00 59.07 ?  801 ATP A C4    1 
HETATM 15888 P  PB    . GDP F 4 .   ? 100.566 153.541 86.723  1.00 70.96 ?  802 GDP A PB    1 
HETATM 15889 O  O1B   . GDP F 4 .   ? 101.766 152.952 86.023  1.00 59.03 ?  802 GDP A O1B   1 
HETATM 15890 O  O2B   . GDP F 4 .   ? 99.950  154.607 85.850  1.00 60.98 -1 802 GDP A O2B   1 
HETATM 15891 O  O3B   . GDP F 4 .   ? 99.550  152.455 86.988  1.00 60.51 ?  802 GDP A O3B   1 
HETATM 15892 O  O3A   . GDP F 4 .   ? 101.049 154.207 88.105  1.00 58.04 ?  802 GDP A O3A   1 
HETATM 15893 P  PA    . GDP F 4 .   ? 101.597 153.309 89.322  1.00 62.53 ?  802 GDP A PA    1 
HETATM 15894 O  O1A   . GDP F 4 .   ? 101.196 153.907 90.648  1.00 60.36 -1 802 GDP A O1A   1 
HETATM 15895 O  O2A   . GDP F 4 .   ? 101.109 151.884 89.221  1.00 57.51 ?  802 GDP A O2A   1 
HETATM 15896 O  "O5'" . GDP F 4 .   ? 103.195 153.381 89.134  1.00 58.41 ?  802 GDP A "O5'" 1 
HETATM 15897 C  "C5'" . GDP F 4 .   ? 104.045 153.211 90.262  1.00 58.74 ?  802 GDP A "C5'" 1 
HETATM 15898 C  "C4'" . GDP F 4 .   ? 105.191 152.269 89.928  1.00 56.36 ?  802 GDP A "C4'" 1 
HETATM 15899 O  "O4'" . GDP F 4 .   ? 105.561 151.584 91.127  1.00 56.52 ?  802 GDP A "O4'" 1 
HETATM 15900 C  "C3'" . GDP F 4 .   ? 104.767 151.231 88.905  1.00 58.64 ?  802 GDP A "C3'" 1 
HETATM 15901 O  "O3'" . GDP F 4 .   ? 105.615 151.307 87.755  1.00 59.90 ?  802 GDP A "O3'" 1 
HETATM 15902 C  "C2'" . GDP F 4 .   ? 104.929 149.882 89.573  1.00 57.17 ?  802 GDP A "C2'" 1 
HETATM 15903 O  "O2'" . GDP F 4 .   ? 105.776 149.041 88.787  1.00 58.14 ?  802 GDP A "O2'" 1 
HETATM 15904 C  "C1'" . GDP F 4 .   ? 105.579 150.170 90.917  1.00 54.02 ?  802 GDP A "C1'" 1 
HETATM 15905 N  N9    . GDP F 4 .   ? 104.906 149.467 92.042  1.00 54.87 ?  802 GDP A N9    1 
HETATM 15906 C  C8    . GDP F 4 .   ? 105.554 148.903 93.076  1.00 56.62 ?  802 GDP A C8    1 
HETATM 15907 N  N7    . GDP F 4 .   ? 104.692 148.338 93.957  1.00 56.41 ?  802 GDP A N7    1 
HETATM 15908 C  C5    . GDP F 4 .   ? 103.449 148.551 93.492  1.00 56.75 ?  802 GDP A C5    1 
HETATM 15909 C  C6    . GDP F 4 .   ? 102.078 148.220 93.944  1.00 57.45 ?  802 GDP A C6    1 
HETATM 15910 O  O6    . GDP F 4 .   ? 101.887 147.587 95.004  1.00 57.90 ?  802 GDP A O6    1 
HETATM 15911 N  N1    . GDP F 4 .   ? 101.053 148.616 93.182  1.00 57.76 ?  802 GDP A N1    1 
HETATM 15912 C  C2    . GDP F 4 .   ? 101.232 149.298 92.037  1.00 56.48 ?  802 GDP A C2    1 
HETATM 15913 N  N2    . GDP F 4 .   ? 100.142 149.663 91.323  1.00 57.02 ?  802 GDP A N2    1 
HETATM 15914 N  N3    . GDP F 4 .   ? 102.460 149.636 91.565  1.00 58.50 ?  802 GDP A N3    1 
HETATM 15915 C  C4    . GDP F 4 .   ? 103.590 149.298 92.233  1.00 57.68 ?  802 GDP A C4    1 
HETATM 15916 P  PA    . TTP G 5 .   ? 143.329 147.567 135.851 1.00 19.24 ?  803 TTP A PA    1 
HETATM 15917 O  O1A   . TTP G 5 .   ? 141.901 147.329 136.270 1.00 19.64 -1 803 TTP A O1A   1 
HETATM 15918 O  O2A   . TTP G 5 .   ? 143.489 148.914 135.193 1.00 31.54 ?  803 TTP A O2A   1 
HETATM 15919 O  O3A   . TTP G 5 .   ? 144.342 147.420 137.090 1.00 30.64 ?  803 TTP A O3A   1 
HETATM 15920 P  PB    . TTP G 5 .   ? 144.524 148.580 138.186 1.00 31.57 ?  803 TTP A PB    1 
HETATM 15921 O  O1B   . TTP G 5 .   ? 144.286 149.952 137.607 1.00 27.79 -1 803 TTP A O1B   1 
HETATM 15922 O  O2B   . TTP G 5 .   ? 143.612 148.337 139.361 1.00 31.36 ?  803 TTP A O2B   1 
HETATM 15923 O  O3B   . TTP G 5 .   ? 146.060 148.387 138.617 1.00 27.98 ?  803 TTP A O3B   1 
HETATM 15924 P  PG    . TTP G 5 .   ? 147.247 148.561 137.544 1.00 26.76 ?  803 TTP A PG    1 
HETATM 15925 O  O1G   . TTP G 5 .   ? 146.859 149.575 136.496 1.00 32.07 ?  803 TTP A O1G   1 
HETATM 15926 O  O2G   . TTP G 5 .   ? 148.505 149.009 138.243 1.00 34.92 -1 803 TTP A O2G   1 
HETATM 15927 O  O3G   . TTP G 5 .   ? 147.505 147.231 136.884 1.00 18.37 ?  803 TTP A O3G   1 
HETATM 15928 O  "O5'" . TTP G 5 .   ? 143.844 146.400 134.878 1.00 23.88 ?  803 TTP A "O5'" 1 
HETATM 15929 C  "C5'" . TTP G 5 .   ? 144.400 145.221 135.446 1.00 21.43 ?  803 TTP A "C5'" 1 
HETATM 15930 C  "C4'" . TTP G 5 .   ? 144.431 144.124 134.399 1.00 24.35 ?  803 TTP A "C4'" 1 
HETATM 15931 O  "O4'" . TTP G 5 .   ? 144.282 142.873 135.068 1.00 31.28 ?  803 TTP A "O4'" 1 
HETATM 15932 C  "C3'" . TTP G 5 .   ? 143.275 144.282 133.430 1.00 26.08 ?  803 TTP A "C3'" 1 
HETATM 15933 O  "O3'" . TTP G 5 .   ? 143.761 144.408 132.092 1.00 24.00 ?  803 TTP A "O3'" 1 
HETATM 15934 C  "C2'" . TTP G 5 .   ? 142.448 143.022 133.554 1.00 25.88 ?  803 TTP A "C2'" 1 
HETATM 15935 C  "C1'" . TTP G 5 .   ? 143.161 142.142 134.568 1.00 25.26 ?  803 TTP A "C1'" 1 
HETATM 15936 N  N1    . TTP G 5 .   ? 142.261 141.835 135.678 1.00 25.70 ?  803 TTP A N1    1 
HETATM 15937 C  C2    . TTP G 5 .   ? 141.955 140.492 135.985 1.00 25.54 ?  803 TTP A C2    1 
HETATM 15938 O  O2    . TTP G 5 .   ? 142.459 139.577 135.300 1.00 22.46 ?  803 TTP A O2    1 
HETATM 15939 N  N3    . TTP G 5 .   ? 141.136 140.179 136.995 1.00 24.38 ?  803 TTP A N3    1 
HETATM 15940 C  C4    . TTP G 5 .   ? 140.583 141.137 137.744 1.00 29.17 ?  803 TTP A C4    1 
HETATM 15941 O  O4    . TTP G 5 .   ? 139.819 140.844 138.687 1.00 37.02 ?  803 TTP A O4    1 
HETATM 15942 C  C5    . TTP G 5 .   ? 140.888 142.555 137.443 1.00 28.26 ?  803 TTP A C5    1 
HETATM 15943 C  C5M   . TTP G 5 .   ? 140.287 143.663 138.264 1.00 26.39 ?  803 TTP A C5M   1 
HETATM 15944 C  C6    . TTP G 5 .   ? 141.741 142.840 136.389 1.00 27.03 ?  803 TTP A C6    1 
HETATM 15945 MG MG    . MG  H 6 .   ? 145.174 150.086 134.903 1.00 18.30 ?  804 MG  A MG    1 
HETATM 15946 P  PA    . TTP I 5 .   ? 116.819 147.135 125.990 1.00 24.11 ?  801 TTP B PA    1 
HETATM 15947 O  O1A   . TTP I 5 .   ? 118.261 147.556 126.118 1.00 30.19 -1 801 TTP B O1A   1 
HETATM 15948 O  O2A   . TTP I 5 .   ? 115.925 148.006 126.835 1.00 22.18 ?  801 TTP B O2A   1 
HETATM 15949 O  O3A   . TTP I 5 .   ? 116.365 147.117 124.449 1.00 32.55 ?  801 TTP B O3A   1 
HETATM 15950 P  PB    . TTP I 5 .   ? 115.522 148.324 123.804 1.00 29.61 ?  801 TTP B PB    1 
HETATM 15951 O  O1B   . TTP I 5 .   ? 115.489 149.548 124.683 1.00 32.07 -1 801 TTP B O1B   1 
HETATM 15952 O  O2B   . TTP I 5 .   ? 116.085 148.668 122.449 1.00 29.33 ?  801 TTP B O2B   1 
HETATM 15953 O  O3B   . TTP I 5 .   ? 114.068 147.646 123.676 1.00 19.28 ?  801 TTP B O3B   1 
HETATM 15954 P  PG    . TTP I 5 .   ? 112.803 148.237 124.476 1.00 31.34 ?  801 TTP B PG    1 
HETATM 15955 O  O1G   . TTP I 5 .   ? 112.376 149.547 123.861 1.00 34.07 ?  801 TTP B O1G   1 
HETATM 15956 O  O2G   . TTP I 5 .   ? 111.662 147.253 124.404 1.00 23.32 -1 801 TTP B O2G   1 
HETATM 15957 O  O3G   . TTP I 5 .   ? 113.178 148.457 125.920 1.00 34.53 ?  801 TTP B O3G   1 
HETATM 15958 O  "O5'" . TTP I 5 .   ? 116.626 145.595 126.403 1.00 24.93 ?  801 TTP B "O5'" 1 
HETATM 15959 C  "C5'" . TTP I 5 .   ? 115.672 145.273 127.409 1.00 24.44 ?  801 TTP B "C5'" 1 
HETATM 15960 C  "C4'" . TTP I 5 .   ? 115.744 143.793 127.745 1.00 24.00 ?  801 TTP B "C4'" 1 
HETATM 15961 O  "O4'" . TTP I 5 .   ? 115.963 143.026 126.563 1.00 28.53 ?  801 TTP B "O4'" 1 
HETATM 15962 C  "C3'" . TTP I 5 .   ? 116.904 143.486 128.672 1.00 27.23 ?  801 TTP B "C3'" 1 
HETATM 15963 O  "O3'" . TTP I 5 .   ? 116.456 143.378 130.025 1.00 27.74 ?  801 TTP B "O3'" 1 
HETATM 15964 C  "C2'" . TTP I 5 .   ? 117.449 142.157 128.191 1.00 27.40 ?  801 TTP B "C2'" 1 
HETATM 15965 C  "C1'" . TTP I 5 .   ? 116.749 141.874 126.870 1.00 29.90 ?  801 TTP B "C1'" 1 
HETATM 15966 N  N1    . TTP I 5 .   ? 117.746 141.631 125.828 1.00 28.87 ?  801 TTP B N1    1 
HETATM 15967 C  C2    . TTP I 5 .   ? 118.182 140.310 125.589 1.00 27.67 ?  801 TTP B C2    1 
HETATM 15968 O  O2    . TTP I 5 .   ? 117.700 139.378 126.265 1.00 29.22 ?  801 TTP B O2    1 
HETATM 15969 N  N3    . TTP I 5 .   ? 119.094 140.033 124.648 1.00 25.56 ?  801 TTP B N3    1 
HETATM 15970 C  C4    . TTP I 5 .   ? 119.622 141.010 123.911 1.00 29.58 ?  801 TTP B C4    1 
HETATM 15971 O  O4    . TTP I 5 .   ? 120.473 140.751 123.035 1.00 38.14 ?  801 TTP B O4    1 
HETATM 15972 C  C5    . TTP I 5 .   ? 119.186 142.408 124.146 1.00 24.40 ?  801 TTP B C5    1 
HETATM 15973 C  C5M   . TTP I 5 .   ? 119.760 143.538 123.334 1.00 26.91 ?  801 TTP B C5M   1 
HETATM 15974 C  C6    . TTP I 5 .   ? 118.240 142.657 125.128 1.00 27.32 ?  801 TTP B C6    1 
HETATM 15975 MG MG    . MG  J 6 .   ? 114.663 149.590 127.043 1.00 37.62 ?  802 MG  B MG    1 
HETATM 15976 P  PG    . ATP K 3 .   ? 154.188 138.214 179.869 1.00 70.08 ?  803 ATP B PG    1 
HETATM 15977 O  O1G   . ATP K 3 .   ? 154.108 138.812 178.505 1.00 62.41 ?  803 ATP B O1G   1 
HETATM 15978 O  O2G   . ATP K 3 .   ? 154.121 139.251 180.996 1.00 61.28 -1 803 ATP B O2G   1 
HETATM 15979 O  O3G   . ATP K 3 .   ? 153.142 137.125 180.128 1.00 60.15 ?  803 ATP B O3G   1 
HETATM 15980 P  PB    . ATP K 3 .   ? 156.187 136.022 180.319 1.00 67.84 ?  803 ATP B PB    1 
HETATM 15981 O  O1B   . ATP K 3 .   ? 157.476 135.829 179.624 1.00 59.55 -1 803 ATP B O1B   1 
HETATM 15982 O  O2B   . ATP K 3 .   ? 156.202 135.780 181.829 1.00 61.48 ?  803 ATP B O2B   1 
HETATM 15983 O  O3B   . ATP K 3 .   ? 155.596 137.482 180.082 1.00 62.14 ?  803 ATP B O3B   1 
HETATM 15984 P  PA    . ATP K 3 .   ? 154.685 134.494 178.278 1.00 67.77 ?  803 ATP B PA    1 
HETATM 15985 O  O1A   . ATP K 3 .   ? 153.253 134.672 177.962 1.00 60.17 -1 803 ATP B O1A   1 
HETATM 15986 O  O2A   . ATP K 3 .   ? 155.178 133.048 178.264 1.00 60.55 ?  803 ATP B O2A   1 
HETATM 15987 O  O3A   . ATP K 3 .   ? 155.046 135.098 179.704 1.00 61.79 ?  803 ATP B O3A   1 
HETATM 15988 O  "O5'" . ATP K 3 .   ? 155.593 135.337 177.299 1.00 60.51 ?  803 ATP B "O5'" 1 
HETATM 15989 C  "C5'" . ATP K 3 .   ? 155.725 134.980 175.907 1.00 57.17 ?  803 ATP B "C5'" 1 
HETATM 15990 C  "C4'" . ATP K 3 .   ? 155.195 136.110 175.059 1.00 59.72 ?  803 ATP B "C4'" 1 
HETATM 15991 O  "O4'" . ATP K 3 .   ? 154.527 135.567 173.899 1.00 60.83 ?  803 ATP B "O4'" 1 
HETATM 15992 C  "C3'" . ATP K 3 .   ? 154.170 137.009 175.742 1.00 58.64 ?  803 ATP B "C3'" 1 
HETATM 15993 O  "O3'" . ATP K 3 .   ? 154.805 138.098 176.402 1.00 58.59 ?  803 ATP B "O3'" 1 
HETATM 15994 C  "C2'" . ATP K 3 .   ? 153.312 137.484 174.568 1.00 58.56 ?  803 ATP B "C2'" 1 
HETATM 15995 O  "O2'" . ATP K 3 .   ? 153.910 138.578 173.884 1.00 59.99 ?  803 ATP B "O2'" 1 
HETATM 15996 C  "C1'" . ATP K 3 .   ? 153.298 136.237 173.682 1.00 57.94 ?  803 ATP B "C1'" 1 
HETATM 15997 N  N9    . ATP K 3 .   ? 152.211 135.309 173.976 1.00 59.22 ?  803 ATP B N9    1 
HETATM 15998 C  C8    . ATP K 3 .   ? 152.300 134.101 174.617 1.00 57.41 ?  803 ATP B C8    1 
HETATM 15999 N  N7    . ATP K 3 .   ? 151.156 133.476 174.743 1.00 58.19 ?  803 ATP B N7    1 
HETATM 16000 C  C5    . ATP K 3 .   ? 150.246 134.333 174.144 1.00 58.18 ?  803 ATP B C5    1 
HETATM 16001 C  C6    . ATP K 3 .   ? 148.854 134.255 173.944 1.00 55.35 ?  803 ATP B C6    1 
HETATM 16002 N  N6    . ATP K 3 .   ? 148.101 133.228 174.346 1.00 55.86 ?  803 ATP B N6    1 
HETATM 16003 N  N1    . ATP K 3 .   ? 148.252 135.284 173.308 1.00 57.37 ?  803 ATP B N1    1 
HETATM 16004 C  C2    . ATP K 3 .   ? 148.997 136.316 172.905 1.00 55.85 ?  803 ATP B C2    1 
HETATM 16005 N  N3    . ATP K 3 .   ? 150.312 136.499 173.034 1.00 57.67 ?  803 ATP B N3    1 
HETATM 16006 C  C4    . ATP K 3 .   ? 150.882 135.468 173.666 1.00 59.74 ?  803 ATP B C4    1 
HETATM 16007 P  PB    . GDP L 4 .   ? 159.856 152.939 174.629 1.00 69.13 ?  804 GDP B PB    1 
HETATM 16008 O  O1B   . GDP L 4 .   ? 160.686 151.679 174.615 1.00 61.24 ?  804 GDP B O1B   1 
HETATM 16009 O  O2B   . GDP L 4 .   ? 159.879 153.539 176.014 1.00 59.98 -1 804 GDP B O2B   1 
HETATM 16010 O  O3B   . GDP L 4 .   ? 160.420 153.927 173.637 1.00 59.87 ?  804 GDP B O3B   1 
HETATM 16011 O  O3A   . GDP L 4 .   ? 158.336 152.586 174.242 1.00 58.19 ?  804 GDP B O3A   1 
HETATM 16012 P  PA    . GDP L 4 .   ? 157.921 152.103 172.764 1.00 64.69 ?  804 GDP B PA    1 
HETATM 16013 O  O1A   . GDP L 4 .   ? 158.010 153.228 171.762 1.00 59.39 -1 804 GDP B O1A   1 
HETATM 16014 O  O2A   . GDP L 4 .   ? 158.771 150.936 172.322 1.00 58.30 ?  804 GDP B O2A   1 
HETATM 16015 O  "O5'" . GDP L 4 .   ? 156.394 151.652 172.989 1.00 61.40 ?  804 GDP B "O5'" 1 
HETATM 16016 C  "C5'" . GDP L 4 .   ? 155.388 151.925 172.018 1.00 57.46 ?  804 GDP B "C5'" 1 
HETATM 16017 C  "C4'" . GDP L 4 .   ? 154.256 150.927 172.204 1.00 55.92 ?  804 GDP B "C4'" 1 
HETATM 16018 O  "O4'" . GDP L 4 .   ? 154.007 150.307 170.943 1.00 58.58 ?  804 GDP B "O4'" 1 
HETATM 16019 C  "C3'" . GDP L 4 .   ? 154.657 149.843 173.191 1.00 59.02 ?  804 GDP B "C3'" 1 
HETATM 16020 O  "O3'" . GDP L 4 .   ? 153.641 149.674 174.185 1.00 58.82 ?  804 GDP B "O3'" 1 
HETATM 16021 C  "C2'" . GDP L 4 .   ? 154.800 148.574 172.381 1.00 56.94 ?  804 GDP B "C2'" 1 
HETATM 16022 O  "O2'" . GDP L 4 .   ? 154.135 147.489 173.032 1.00 59.26 ?  804 GDP B "O2'" 1 
HETATM 16023 C  "C1'" . GDP L 4 .   ? 154.139 148.888 171.048 1.00 55.87 ?  804 GDP B "C1'" 1 
HETATM 16024 N  N9    . GDP L 4 .   ? 154.893 148.354 169.883 1.00 56.16 ?  804 GDP B N9    1 
HETATM 16025 C  C8    . GDP L 4 .   ? 154.317 147.853 168.776 1.00 57.86 ?  804 GDP B C8    1 
HETATM 16026 N  N7    . GDP L 4 .   ? 155.245 147.449 167.877 1.00 59.36 ?  804 GDP B N7    1 
HETATM 16027 C  C5    . GDP L 4 .   ? 156.454 147.706 168.403 1.00 59.05 ?  804 GDP B C5    1 
HETATM 16028 C  C6    . GDP L 4 .   ? 157.860 147.527 167.972 1.00 58.07 ?  804 GDP B C6    1 
HETATM 16029 O  O6    . GDP L 4 .   ? 158.131 147.023 166.861 1.00 59.08 ?  804 GDP B O6    1 
HETATM 16030 N  N1    . GDP L 4 .   ? 158.829 147.921 168.806 1.00 57.10 ?  804 GDP B N1    1 
HETATM 16031 C  C2    . GDP L 4 .   ? 158.563 148.466 170.006 1.00 57.92 ?  804 GDP B C2    1 
HETATM 16032 N  N2    . GDP L 4 .   ? 159.598 148.840 170.797 1.00 58.60 ?  804 GDP B N2    1 
HETATM 16033 N  N3    . GDP L 4 .   ? 157.301 148.660 170.463 1.00 60.62 ?  804 GDP B N3    1 
HETATM 16034 C  C4    . GDP L 4 .   ? 156.222 148.307 169.725 1.00 59.26 ?  804 GDP B C4    1 
HETATM 16035 MN MN    . MN  M 7 .   ? 124.859 94.037  118.425 0.85 25.05 ?  401 MN  C MN    1 
HETATM 16036 MN MN    . MN  N 7 .   ? 122.819 96.941  119.590 0.85 26.37 ?  402 MN  C MN    1 
HETATM 16037 MN MN    . MN  O 7 .   ? 141.374 101.670 134.253 1.00 22.51 ?  401 MN  D MN    1 
HETATM 16038 MN MN    . MN  P 7 .   ? 143.952 101.091 131.370 1.00 24.72 ?  402 MN  D MN    1 
# 
