data_9BYZ
# 
_entry.id   9BYZ 
# 
_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   9BYZ         pdb_00009byz 10.2210/pdb9byz/pdb 
WWPDB D_1000284419 ?            ?                   
EMDB  EMD-45049    ?            ?                   
# 
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                        9BYZ 
_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 12 model for turnover condition of Bacillus subtilis ribonucleotide reductase complex' EMD-45049 
'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 MN  ? ? MN  ? ? 'SUBJECT OF INVESTIGATION' ? 
4 MG  ? ? MG  ? ? '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                   9BYZ 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BYZ 
_struct.title                        'Class 12 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        9BYZ 
_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 9BYZ A 1  ? 700 ? P50620 1 ? 700 ? 1 700 
2 1 9BYZ B 1  ? 700 ? P50620 1 ? 700 ? 1 700 
3 2 9BYZ C 22 ? 350 ? P50621 1 ? 329 ? 1 329 
4 2 9BYZ 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 9BYZ MET C 1  ? UNP P50621 ? ? 'initiating methionine' -20 1  
3 9BYZ GLY C 2  ? UNP P50621 ? ? 'expression tag'        -19 2  
3 9BYZ SER C 3  ? UNP P50621 ? ? 'expression tag'        -18 3  
3 9BYZ SER C 4  ? UNP P50621 ? ? 'expression tag'        -17 4  
3 9BYZ HIS C 5  ? UNP P50621 ? ? 'expression tag'        -16 5  
3 9BYZ HIS C 6  ? UNP P50621 ? ? 'expression tag'        -15 6  
3 9BYZ HIS C 7  ? UNP P50621 ? ? 'expression tag'        -14 7  
3 9BYZ HIS C 8  ? UNP P50621 ? ? 'expression tag'        -13 8  
3 9BYZ HIS C 9  ? UNP P50621 ? ? 'expression tag'        -12 9  
3 9BYZ HIS C 10 ? UNP P50621 ? ? 'expression tag'        -11 10 
3 9BYZ SER C 11 ? UNP P50621 ? ? 'expression tag'        -10 11 
3 9BYZ SER C 12 ? UNP P50621 ? ? 'expression tag'        -9  12 
3 9BYZ GLY C 13 ? UNP P50621 ? ? 'expression tag'        -8  13 
3 9BYZ LEU C 14 ? UNP P50621 ? ? 'expression tag'        -7  14 
3 9BYZ VAL C 15 ? UNP P50621 ? ? 'expression tag'        -6  15 
3 9BYZ PRO C 16 ? UNP P50621 ? ? 'expression tag'        -5  16 
3 9BYZ ARG C 17 ? UNP P50621 ? ? 'expression tag'        -4  17 
3 9BYZ GLY C 18 ? UNP P50621 ? ? 'expression tag'        -3  18 
3 9BYZ SER C 19 ? UNP P50621 ? ? 'expression tag'        -2  19 
3 9BYZ HIS C 20 ? UNP P50621 ? ? 'expression tag'        -1  20 
3 9BYZ MET C 21 ? UNP P50621 ? ? 'expression tag'        0   21 
4 9BYZ MET D 1  ? UNP P50621 ? ? 'initiating methionine' -20 22 
4 9BYZ GLY D 2  ? UNP P50621 ? ? 'expression tag'        -19 23 
4 9BYZ SER D 3  ? UNP P50621 ? ? 'expression tag'        -18 24 
4 9BYZ SER D 4  ? UNP P50621 ? ? 'expression tag'        -17 25 
4 9BYZ HIS D 5  ? UNP P50621 ? ? 'expression tag'        -16 26 
4 9BYZ HIS D 6  ? UNP P50621 ? ? 'expression tag'        -15 27 
4 9BYZ HIS D 7  ? UNP P50621 ? ? 'expression tag'        -14 28 
4 9BYZ HIS D 8  ? UNP P50621 ? ? 'expression tag'        -13 29 
4 9BYZ HIS D 9  ? UNP P50621 ? ? 'expression tag'        -12 30 
4 9BYZ HIS D 10 ? UNP P50621 ? ? 'expression tag'        -11 31 
4 9BYZ SER D 11 ? UNP P50621 ? ? 'expression tag'        -10 32 
4 9BYZ SER D 12 ? UNP P50621 ? ? 'expression tag'        -9  33 
4 9BYZ GLY D 13 ? UNP P50621 ? ? 'expression tag'        -8  34 
4 9BYZ LEU D 14 ? UNP P50621 ? ? 'expression tag'        -7  35 
4 9BYZ VAL D 15 ? UNP P50621 ? ? 'expression tag'        -6  36 
4 9BYZ PRO D 16 ? UNP P50621 ? ? 'expression tag'        -5  37 
4 9BYZ ARG D 17 ? UNP P50621 ? ? 'expression tag'        -4  38 
4 9BYZ GLY D 18 ? UNP P50621 ? ? 'expression tag'        -3  39 
4 9BYZ SER D 19 ? UNP P50621 ? ? 'expression tag'        -2  40 
4 9BYZ HIS D 20 ? UNP P50621 ? ? 'expression tag'        -1  41 
4 9BYZ 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 ? ? ? ? ? ? ? 2.850 ? ? 
metalc3  metalc ? ? G TTP .   O1G ? ? ? 1_555 H MG . MG ? ? A TTP 803 A MG 804 1_555 ? ? ? ? ? ? ? 2.375 ? ? 
metalc4  metalc ? ? I TTP .   O2A ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
metalc5  metalc ? ? I TTP .   O1B ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.501 ? ? 
metalc6  metalc ? ? I TTP .   O3G ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.179 ? ? 
metalc7  metalc ? ? C ASP 87  OD1 ? ? ? 1_555 N MN . MN ? ? C ASP 66  C MN 402 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc8  metalc ? ? C GLU 118 OE2 ? ? ? 1_555 M MN . MN ? ? C GLU 97  C MN 401 1_555 ? ? ? ? ? ? ? 1.960 ? ? 
metalc9  metalc ? ? C GLU 118 OE1 ? ? ? 1_555 N MN . MN ? ? C GLU 97  C MN 402 1_555 ? ? ? ? ? ? ? 2.112 ? ? 
metalc10 metalc ? ? C HIS 122 ND1 ? ? ? 1_555 N MN . MN ? ? C HIS 101 C MN 402 1_555 ? ? ? ? ? ? ? 2.175 ? ? 
metalc11 metalc ? ? C GLU 185 OE1 ? ? ? 1_555 M MN . MN ? ? C GLU 164 C MN 401 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
metalc12 metalc ? ? C GLU 185 OE2 ? ? ? 1_555 M MN . MN ? ? C GLU 164 C MN 401 1_555 ? ? ? ? ? ? ? 1.966 ? ? 
metalc13 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 M MN . MN ? ? C GLU 198 C MN 401 1_555 ? ? ? ? ? ? ? 2.173 ? ? 
metalc14 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 N MN . MN ? ? C GLU 198 C MN 402 1_555 ? ? ? ? ? ? ? 2.711 ? ? 
metalc15 metalc ? ? C GLU 219 OE2 ? ? ? 1_555 N MN . MN ? ? C GLU 198 C MN 402 1_555 ? ? ? ? ? ? ? 2.096 ? ? 
metalc16 metalc ? ? C HIS 222 ND1 ? ? ? 1_555 M MN . MN ? ? C HIS 201 C MN 401 1_555 ? ? ? ? ? ? ? 2.408 ? ? 
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 ? ? ? ? ? ? ? 2.303 ? ? 
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 ? ? ? ? ? ? ? 2.081 ? ? 
metalc25 metalc ? ? D GLU 219 OE2 ? ? ? 1_555 P MN . MN ? ? D GLU 198 D MN 402 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
metalc26 metalc ? ? D HIS 222 ND1 ? ? ? 1_555 O MN . MN ? ? D HIS 201 D MN 401 1_555 ? ? ? ? ? ? ? 2.330 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O2A ? 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_555 138.3 ? 
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_555 137.8 ? 
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_555 104.0 ? 
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 58.7  ? 
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_555 165.7 ? 
31 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 107.0 ? 
32 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 93.8  ? 
33 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 90.2  ? 
34 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 111.3 ? 
35 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 122.1 ? 
36 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 96.5  ? 
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_555 153.3 ? 
38 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 99.6  ? 
39 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 55.6  ? 
40 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 121.7 ? 
41 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 81.3  ? 
42 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 136.8 ? 
43 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 91.4  ? 
44 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 103.0 ? 
45 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 102.6 ? 
46 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 89.6  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 355 A . ? TYR 355 A PRO 356 A ? PRO 356 A 1 0.45 
2 TYR 355 B . ? TYR 355 B PRO 356 B ? PRO 356 B 1 0.86 
# 
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                   9BYZ 
_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 ? ? -69.42  2.68    
2  1 ASP A 398 ? ? 39.34   35.67   
3  1 SER A 593 ? ? 56.70   -153.79 
4  1 ASP B 215 ? ? 74.78   -2.80   
5  1 SER B 593 ? ? 60.64   -154.21 
6  1 THR C 72  ? ? -128.06 -59.07  
7  1 ASP C 148 ? ? 58.05   15.71   
8  1 PHE C 166 ? ? -125.65 -60.80  
9  1 THR D 72  ? ? -128.15 -58.50  
10 1 PHE D 166 ? ? -144.18 -61.17  
11 1 ASP D 317 ? ? 64.30   164.41  
12 1 ASP D 318 ? ? 66.30   -1.35   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BYZ 
_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                    9BYZ 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.94 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               29000 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       '50 mM HEPES, 150 mM NaCl, 15 mM MgCl2, 5% (w/v) glycerol' 
_em_buffer.pH            7.6 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Bacillus subtilis ribonucleotide reductase complex' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       '1, 2' 
# 
_em_imaging.entry_id                        9BYZ 
_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              9BYZ 
_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                9BYZ 
_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              9BYZ 
_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           9BYZ 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              'Class 12 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                    9BYZ 
_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   ? 105.340 119.358 98.777  1.00 61.20 ?  6   VAL A N     1 
ATOM   2     C  CA    . VAL A 1 6   ? 106.426 120.065 98.112  1.00 61.32 ?  6   VAL A CA    1 
ATOM   3     C  C     . VAL A 1 6   ? 105.871 121.041 97.074  1.00 62.07 ?  6   VAL A C     1 
ATOM   4     O  O     . VAL A 1 6   ? 105.058 120.667 96.228  1.00 60.69 ?  6   VAL A O     1 
ATOM   5     C  CB    . VAL A 1 6   ? 107.428 119.069 97.479  1.00 61.34 ?  6   VAL A CB    1 
ATOM   6     C  CG1   . VAL A 1 6   ? 106.718 118.095 96.547  1.00 61.29 ?  6   VAL A CG1   1 
ATOM   7     C  CG2   . VAL A 1 6   ? 108.531 119.812 96.745  1.00 59.53 ?  6   VAL A CG2   1 
ATOM   8     N  N     . PRO A 1 7   ? 106.291 122.301 97.155  1.00 58.51 ?  7   PRO A N     1 
ATOM   9     C  CA    . PRO A 1 7   ? 105.803 123.304 96.202  1.00 54.85 ?  7   PRO A CA    1 
ATOM   10    C  C     . PRO A 1 7   ? 106.371 123.080 94.810  1.00 54.57 ?  7   PRO A C     1 
ATOM   11    O  O     . PRO A 1 7   ? 107.419 122.461 94.623  1.00 55.81 ?  7   PRO A O     1 
ATOM   12    C  CB    . PRO A 1 7   ? 106.278 124.639 96.786  1.00 53.42 ?  7   PRO A CB    1 
ATOM   13    C  CG    . PRO A 1 7   ? 107.047 124.329 98.016  1.00 53.02 ?  7   PRO A CG    1 
ATOM   14    C  CD    . PRO A 1 7   ? 107.199 122.858 98.170  1.00 55.87 ?  7   PRO A CD    1 
ATOM   15    N  N     . LYS A 1 8   ? 105.651 123.616 93.819  1.00 54.03 ?  8   LYS A N     1 
ATOM   16    C  CA    . LYS A 1 8   ? 106.004 123.375 92.422  1.00 53.45 ?  8   LYS A CA    1 
ATOM   17    C  C     . LYS A 1 8   ? 107.380 123.933 92.083  1.00 55.16 ?  8   LYS A C     1 
ATOM   18    O  O     . LYS A 1 8   ? 108.161 123.288 91.371  1.00 57.31 ?  8   LYS A O     1 
ATOM   19    C  CB    . LYS A 1 8   ? 104.939 123.981 91.506  1.00 55.50 ?  8   LYS A CB    1 
ATOM   20    C  CG    . LYS A 1 8   ? 105.283 123.922 90.027  1.00 55.15 ?  8   LYS A CG    1 
ATOM   21    C  CD    . LYS A 1 8   ? 104.355 124.808 89.211  1.00 55.42 ?  8   LYS A CD    1 
ATOM   22    C  CE    . LYS A 1 8   ? 104.785 124.863 87.754  1.00 55.63 ?  8   LYS A CE    1 
ATOM   23    N  NZ    . LYS A 1 8   ? 104.081 125.942 87.007  1.00 56.86 1  8   LYS A NZ    1 
ATOM   24    N  N     . TRP A 1 9   ? 107.696 125.135 92.575  1.00 54.44 ?  9   TRP A N     1 
ATOM   25    C  CA    . TRP A 1 9   ? 108.997 125.721 92.277  1.00 52.69 ?  9   TRP A CA    1 
ATOM   26    C  C     . TRP A 1 9   ? 110.126 124.899 92.882  1.00 51.63 ?  9   TRP A C     1 
ATOM   27    O  O     . TRP A 1 9   ? 111.206 124.798 92.290  1.00 53.76 ?  9   TRP A O     1 
ATOM   28    C  CB    . TRP A 1 9   ? 109.062 127.166 92.774  1.00 52.54 ?  9   TRP A CB    1 
ATOM   29    C  CG    . TRP A 1 9   ? 108.842 127.334 94.246  1.00 49.94 ?  9   TRP A CG    1 
ATOM   30    C  CD1   . TRP A 1 9   ? 109.785 127.257 95.227  1.00 49.74 ?  9   TRP A CD1   1 
ATOM   31    C  CD2   . TRP A 1 9   ? 107.604 127.631 94.903  1.00 51.38 ?  9   TRP A CD2   1 
ATOM   32    N  NE1   . TRP A 1 9   ? 109.212 127.476 96.456  1.00 49.45 ?  9   TRP A NE1   1 
ATOM   33    C  CE2   . TRP A 1 9   ? 107.874 127.710 96.284  1.00 51.17 ?  9   TRP A CE2   1 
ATOM   34    C  CE3   . TRP A 1 9   ? 106.295 127.833 94.460  1.00 49.58 ?  9   TRP A CE3   1 
ATOM   35    C  CZ2   . TRP A 1 9   ? 106.884 127.982 97.223  1.00 49.84 ?  9   TRP A CZ2   1 
ATOM   36    C  CZ3   . TRP A 1 9   ? 105.313 128.101 95.394  1.00 51.27 ?  9   TRP A CZ3   1 
ATOM   37    C  CH2   . TRP A 1 9   ? 105.612 128.171 96.759  1.00 51.47 ?  9   TRP A CH2   1 
ATOM   38    N  N     . ILE A 1 10  ? 109.892 124.286 94.043  1.00 54.01 ?  10  ILE A N     1 
ATOM   39    C  CA    . ILE A 1 10  ? 110.921 123.453 94.654  1.00 53.77 ?  10  ILE A CA    1 
ATOM   40    C  C     . ILE A 1 10  ? 111.139 122.184 93.837  1.00 53.66 ?  10  ILE A C     1 
ATOM   41    O  O     . ILE A 1 10  ? 112.275 121.723 93.680  1.00 56.41 ?  10  ILE A O     1 
ATOM   42    C  CB    . ILE A 1 10  ? 110.557 123.146 96.117  1.00 54.66 ?  10  ILE A CB    1 
ATOM   43    C  CG1   . ILE A 1 10  ? 110.690 124.416 96.960  1.00 54.34 ?  10  ILE A CG1   1 
ATOM   44    C  CG2   . ILE A 1 10  ? 111.450 122.050 96.675  1.00 54.60 ?  10  ILE A CG2   1 
ATOM   45    C  CD1   . ILE A 1 10  ? 110.657 124.179 98.448  1.00 55.93 ?  10  ILE A CD1   1 
ATOM   46    N  N     . GLN A 1 11  ? 110.066 121.600 93.297  1.00 57.00 ?  11  GLN A N     1 
ATOM   47    C  CA    . GLN A 1 11  ? 110.237 120.460 92.400  1.00 57.95 ?  11  GLN A CA    1 
ATOM   48    C  C     . GLN A 1 11  ? 111.004 120.857 91.145  1.00 57.73 ?  11  GLN A C     1 
ATOM   49    O  O     . GLN A 1 11  ? 111.898 120.130 90.697  1.00 59.00 ?  11  GLN A O     1 
ATOM   50    C  CB    . GLN A 1 11  ? 108.882 119.858 92.026  1.00 57.52 ?  11  GLN A CB    1 
ATOM   51    C  CG    . GLN A 1 11  ? 107.898 119.742 93.173  1.00 58.92 ?  11  GLN A CG    1 
ATOM   52    C  CD    . GLN A 1 11  ? 106.456 119.812 92.710  1.00 60.78 ?  11  GLN A CD    1 
ATOM   53    O  OE1   . GLN A 1 11  ? 106.177 119.843 91.513  1.00 58.86 ?  11  GLN A OE1   1 
ATOM   54    N  NE2   . GLN A 1 11  ? 105.531 119.837 93.663  1.00 58.93 ?  11  GLN A NE2   1 
ATOM   55    N  N     . LEU A 1 12  ? 110.672 122.014 90.566  1.00 53.91 ?  12  LEU A N     1 
ATOM   56    C  CA    . LEU A 1 12  ? 111.382 122.471 89.377  1.00 52.66 ?  12  LEU A CA    1 
ATOM   57    C  C     . LEU A 1 12  ? 112.850 122.753 89.674  1.00 54.69 ?  12  LEU A C     1 
ATOM   58    O  O     . LEU A 1 12  ? 113.705 122.584 88.798  1.00 56.24 ?  12  LEU A O     1 
ATOM   59    C  CB    . LEU A 1 12  ? 110.703 123.715 88.804  1.00 52.80 ?  12  LEU A CB    1 
ATOM   60    C  CG    . LEU A 1 12  ? 109.535 123.465 87.849  1.00 53.51 ?  12  LEU A CG    1 
ATOM   61    C  CD1   . LEU A 1 12  ? 108.770 124.752 87.584  1.00 55.35 ?  12  LEU A CD1   1 
ATOM   62    C  CD2   . LEU A 1 12  ? 110.029 122.856 86.547  1.00 52.97 ?  12  LEU A CD2   1 
ATOM   63    N  N     . ASN A 1 13  ? 113.159 123.188 90.896  1.00 53.32 ?  13  ASN A N     1 
ATOM   64    C  CA    . ASN A 1 13  ? 114.547 123.419 91.280  1.00 51.61 ?  13  ASN A CA    1 
ATOM   65    C  C     . ASN A 1 13  ? 115.294 122.110 91.506  1.00 53.33 ?  13  ASN A C     1 
ATOM   66    O  O     . ASN A 1 13  ? 116.447 121.970 91.084  1.00 57.21 ?  13  ASN A O     1 
ATOM   67    C  CB    . ASN A 1 13  ? 114.603 124.293 92.533  1.00 52.13 ?  13  ASN A CB    1 
ATOM   68    C  CG    . ASN A 1 13  ? 116.021 124.595 92.969  1.00 51.95 ?  13  ASN A CG    1 
ATOM   69    O  OD1   . ASN A 1 13  ? 116.563 123.939 93.857  1.00 52.22 ?  13  ASN A OD1   1 
ATOM   70    N  ND2   . ASN A 1 13  ? 116.630 125.596 92.344  1.00 53.37 ?  13  ASN A ND2   1 
ATOM   71    N  N     . ASN A 1 14  ? 114.659 121.143 92.172  1.00 56.37 ?  14  ASN A N     1 
ATOM   72    C  CA    . ASN A 1 14  ? 115.283 119.841 92.378  1.00 55.27 ?  14  ASN A CA    1 
ATOM   73    C  C     . ASN A 1 14  ? 115.401 119.044 91.088  1.00 55.96 ?  14  ASN A C     1 
ATOM   74    O  O     . ASN A 1 14  ? 116.176 118.083 91.036  1.00 59.84 ?  14  ASN A O     1 
ATOM   75    C  CB    . ASN A 1 14  ? 114.507 119.039 93.423  1.00 55.43 ?  14  ASN A CB    1 
ATOM   76    C  CG    . ASN A 1 14  ? 114.523 119.694 94.789  1.00 58.93 ?  14  ASN A CG    1 
ATOM   77    O  OD1   . ASN A 1 14  ? 114.552 120.917 94.906  1.00 59.21 ?  14  ASN A OD1   1 
ATOM   78    N  ND2   . ASN A 1 14  ? 114.503 118.876 95.836  1.00 59.70 ?  14  ASN A ND2   1 
ATOM   79    N  N     . GLU A 1 15  ? 114.656 119.418 90.047  1.00 57.11 ?  15  GLU A N     1 
ATOM   80    C  CA    . GLU A 1 15  ? 114.811 118.766 88.754  1.00 58.53 ?  15  GLU A CA    1 
ATOM   81    C  C     . GLU A 1 15  ? 116.138 119.097 88.080  1.00 58.60 ?  15  GLU A C     1 
ATOM   82    O  O     . GLU A 1 15  ? 116.453 118.492 87.049  1.00 61.66 ?  15  GLU A O     1 
ATOM   83    C  CB    . GLU A 1 15  ? 113.649 119.140 87.831  1.00 58.15 ?  15  GLU A CB    1 
ATOM   84    C  CG    . GLU A 1 15  ? 112.375 118.352 88.099  1.00 58.81 ?  15  GLU A CG    1 
ATOM   85    C  CD    . GLU A 1 15  ? 111.190 118.858 87.301  1.00 61.24 ?  15  GLU A CD    1 
ATOM   86    O  OE1   . GLU A 1 15  ? 111.402 119.401 86.198  1.00 60.87 ?  15  GLU A OE1   1 
ATOM   87    O  OE2   . GLU A 1 15  ? 110.044 118.712 87.777  1.00 59.03 -1 15  GLU A OE2   1 
ATOM   88    N  N     . ILE A 1 16  ? 116.909 120.043 88.622  1.00 58.15 ?  16  ILE A N     1 
ATOM   89    C  CA    . ILE A 1 16  ? 118.221 120.359 88.056  1.00 58.69 ?  16  ILE A CA    1 
ATOM   90    C  C     . ILE A 1 16  ? 119.141 119.148 88.140  1.00 57.58 ?  16  ILE A C     1 
ATOM   91    O  O     . ILE A 1 16  ? 119.816 118.789 87.168  1.00 58.61 ?  16  ILE A O     1 
ATOM   92    C  CB    . ILE A 1 16  ? 118.836 121.573 88.775  1.00 57.30 ?  16  ILE A CB    1 
ATOM   93    C  CG1   . ILE A 1 16  ? 118.119 122.862 88.380  1.00 56.73 ?  16  ILE A CG1   1 
ATOM   94    C  CG2   . ILE A 1 16  ? 120.324 121.680 88.470  1.00 57.89 ?  16  ILE A CG2   1 
ATOM   95    C  CD1   . ILE A 1 16  ? 118.259 123.951 89.410  1.00 56.64 ?  16  ILE A CD1   1 
ATOM   96    N  N     . MET A 1 17  ? 119.180 118.500 89.307  1.00 57.91 ?  17  MET A N     1 
ATOM   97    C  CA    . MET A 1 17  ? 120.087 117.374 89.501  1.00 60.77 ?  17  MET A CA    1 
ATOM   98    C  C     . MET A 1 17  ? 119.711 116.187 88.626  1.00 60.83 ?  17  MET A C     1 
ATOM   99    O  O     . MET A 1 17  ? 120.579 115.377 88.281  1.00 61.69 ?  17  MET A O     1 
ATOM   100   C  CB    . MET A 1 17  ? 120.103 116.960 90.972  1.00 60.42 ?  17  MET A CB    1 
ATOM   101   C  CG    . MET A 1 17  ? 120.503 118.069 91.928  1.00 59.88 ?  17  MET A CG    1 
ATOM   102   S  SD    . MET A 1 17  ? 121.566 119.336 91.213  1.00 62.45 ?  17  MET A SD    1 
ATOM   103   C  CE    . MET A 1 17  ? 123.130 118.466 91.158  1.00 58.33 ?  17  MET A CE    1 
ATOM   104   N  N     . ILE A 1 18  ? 118.436 116.062 88.266  1.00 63.10 ?  18  ILE A N     1 
ATOM   105   C  CA    . ILE A 1 18  ? 118.000 114.987 87.377  1.00 63.93 ?  18  ILE A CA    1 
ATOM   106   C  C     . ILE A 1 18  ? 118.651 115.227 86.018  1.00 64.49 ?  18  ILE A C     1 
ATOM   107   O  O     . ILE A 1 18  ? 118.404 116.247 85.370  1.00 66.32 ?  18  ILE A O     1 
ATOM   108   C  CB    . ILE A 1 18  ? 116.470 114.918 87.265  1.00 63.43 ?  18  ILE A CB    1 
ATOM   109   C  CG1   . ILE A 1 18  ? 115.832 114.169 88.449  1.00 64.00 ?  18  ILE A CG1   1 
ATOM   110   C  CG2   . ILE A 1 18  ? 116.057 114.239 85.967  1.00 63.67 ?  18  ILE A CG2   1 
ATOM   111   C  CD1   . ILE A 1 18  ? 116.372 114.490 89.830  1.00 63.77 ?  18  ILE A CD1   1 
ATOM   112   N  N     . GLN A 1 19  ? 119.499 114.294 85.593  1.00 67.59 ?  19  GLN A N     1 
ATOM   113   C  CA    . GLN A 1 19  ? 120.310 114.497 84.402  1.00 69.12 ?  19  GLN A CA    1 
ATOM   114   C  C     . GLN A 1 19  ? 119.577 114.005 83.161  1.00 70.12 ?  19  GLN A C     1 
ATOM   115   O  O     . GLN A 1 19  ? 119.099 112.867 83.118  1.00 70.79 ?  19  GLN A O     1 
ATOM   116   C  CB    . GLN A 1 19  ? 121.650 113.775 84.548  1.00 70.18 ?  19  GLN A CB    1 
ATOM   117   C  CG    . GLN A 1 19  ? 122.624 114.472 85.484  1.00 68.31 ?  19  GLN A CG    1 
ATOM   118   C  CD    . GLN A 1 19  ? 124.063 114.062 85.243  1.00 70.65 ?  19  GLN A CD    1 
ATOM   119   O  OE1   . GLN A 1 19  ? 124.377 113.419 84.241  1.00 71.53 ?  19  GLN A OE1   1 
ATOM   120   N  NE2   . GLN A 1 19  ? 124.946 114.432 86.162  1.00 69.08 ?  19  GLN A NE2   1 
ATOM   121   N  N     . LYS A 1 20  ? 119.489 114.868 82.155  1.00 72.27 ?  20  LYS A N     1 
ATOM   122   C  CA    . LYS A 1 20  ? 118.922 114.525 80.860  1.00 73.91 ?  20  LYS A CA    1 
ATOM   123   C  C     . LYS A 1 20  ? 120.032 114.562 79.819  1.00 76.01 ?  20  LYS A C     1 
ATOM   124   O  O     . LYS A 1 20  ? 120.725 115.577 79.685  1.00 75.81 ?  20  LYS A O     1 
ATOM   125   C  CB    . LYS A 1 20  ? 117.792 115.486 80.482  1.00 71.70 ?  20  LYS A CB    1 
ATOM   126   C  CG    . LYS A 1 20  ? 117.501 115.567 78.991  1.00 73.05 ?  20  LYS A CG    1 
ATOM   127   C  CD    . LYS A 1 20  ? 117.978 116.885 78.402  1.00 74.70 ?  20  LYS A CD    1 
ATOM   128   C  CE    . LYS A 1 20  ? 118.243 116.761 76.910  1.00 74.77 ?  20  LYS A CE    1 
ATOM   129   N  NZ    . LYS A 1 20  ? 118.206 118.084 76.227  1.00 74.65 1  20  LYS A NZ    1 
ATOM   130   N  N     . ASP A 1 21  ? 120.199 113.454 79.095  1.00 77.71 ?  21  ASP A N     1 
ATOM   131   C  CA    . ASP A 1 21  ? 121.281 113.299 78.121  1.00 78.08 ?  21  ASP A CA    1 
ATOM   132   C  C     . ASP A 1 21  ? 122.645 113.512 78.776  1.00 78.21 ?  21  ASP A C     1 
ATOM   133   O  O     . ASP A 1 21  ? 123.564 114.075 78.176  1.00 77.84 ?  21  ASP A O     1 
ATOM   134   C  CB    . ASP A 1 21  ? 121.094 114.240 76.928  1.00 78.03 ?  21  ASP A CB    1 
ATOM   135   C  CG    . ASP A 1 21  ? 121.864 113.788 75.702  1.00 79.20 ?  21  ASP A CG    1 
ATOM   136   O  OD1   . ASP A 1 21  ? 121.861 112.573 75.413  1.00 77.85 ?  21  ASP A OD1   1 
ATOM   137   O  OD2   . ASP A 1 21  ? 122.474 114.647 75.030  1.00 77.64 -1 21  ASP A OD2   1 
ATOM   138   N  N     . GLY A 1 22  ? 122.777 113.062 80.021  1.00 74.06 ?  22  GLY A N     1 
ATOM   139   C  CA    . GLY A 1 22  ? 124.027 113.203 80.738  1.00 72.25 ?  22  GLY A CA    1 
ATOM   140   C  C     . GLY A 1 22  ? 124.393 114.620 81.109  1.00 73.50 ?  22  GLY A C     1 
ATOM   141   O  O     . GLY A 1 22  ? 125.568 114.898 81.365  1.00 74.68 ?  22  GLY A O     1 
ATOM   142   N  N     . LYS A 1 23  ? 123.422 115.529 81.148  1.00 69.34 ?  23  LYS A N     1 
ATOM   143   C  CA    . LYS A 1 23  ? 123.673 116.924 81.474  1.00 67.22 ?  23  LYS A CA    1 
ATOM   144   C  C     . LYS A 1 23  ? 122.662 117.407 82.503  1.00 68.95 ?  23  LYS A C     1 
ATOM   145   O  O     . LYS A 1 23  ? 121.503 116.982 82.509  1.00 70.38 ?  23  LYS A O     1 
ATOM   146   C  CB    . LYS A 1 23  ? 123.605 117.817 80.228  1.00 68.25 ?  23  LYS A CB    1 
ATOM   147   C  CG    . LYS A 1 23  ? 124.686 117.537 79.200  1.00 68.58 ?  23  LYS A CG    1 
ATOM   148   C  CD    . LYS A 1 23  ? 124.435 118.310 77.917  1.00 68.77 ?  23  LYS A CD    1 
ATOM   149   C  CE    . LYS A 1 23  ? 125.380 117.870 76.814  1.00 71.00 ?  23  LYS A CE    1 
ATOM   150   N  NZ    . LYS A 1 23  ? 125.016 118.463 75.499  1.00 69.00 1  23  LYS A NZ    1 
ATOM   151   N  N     . PHE A 1 24  ? 123.115 118.302 83.376  1.00 62.03 ?  24  PHE A N     1 
ATOM   152   C  CA    . PHE A 1 24  ? 122.228 118.898 84.364  1.00 59.31 ?  24  PHE A CA    1 
ATOM   153   C  C     . PHE A 1 24  ? 121.240 119.838 83.686  1.00 59.62 ?  24  PHE A C     1 
ATOM   154   O  O     . PHE A 1 24  ? 121.594 120.576 82.763  1.00 59.64 ?  24  PHE A O     1 
ATOM   155   C  CB    . PHE A 1 24  ? 123.036 119.655 85.416  1.00 57.58 ?  24  PHE A CB    1 
ATOM   156   C  CG    . PHE A 1 24  ? 123.897 118.772 86.270  1.00 59.16 ?  24  PHE A CG    1 
ATOM   157   C  CD1   . PHE A 1 24  ? 123.352 118.051 87.315  1.00 60.30 ?  24  PHE A CD1   1 
ATOM   158   C  CD2   . PHE A 1 24  ? 125.257 118.666 86.026  1.00 60.20 ?  24  PHE A CD2   1 
ATOM   159   C  CE1   . PHE A 1 24  ? 124.144 117.237 88.100  1.00 61.28 ?  24  PHE A CE1   1 
ATOM   160   C  CE2   . PHE A 1 24  ? 126.054 117.855 86.810  1.00 58.77 ?  24  PHE A CE2   1 
ATOM   161   C  CZ    . PHE A 1 24  ? 125.496 117.141 87.848  1.00 59.24 ?  24  PHE A CZ    1 
ATOM   162   N  N     . GLN A 1 25  ? 119.990 119.806 84.148  1.00 59.49 ?  25  GLN A N     1 
ATOM   163   C  CA    . GLN A 1 25  ? 118.942 120.668 83.603  1.00 61.28 ?  25  GLN A CA    1 
ATOM   164   C  C     . GLN A 1 25  ? 119.015 122.022 84.304  1.00 60.68 ?  25  GLN A C     1 
ATOM   165   O  O     . GLN A 1 25  ? 118.203 122.364 85.167  1.00 62.38 ?  25  GLN A O     1 
ATOM   166   C  CB    . GLN A 1 25  ? 117.573 120.020 83.763  1.00 61.69 ?  25  GLN A CB    1 
ATOM   167   C  CG    . GLN A 1 25  ? 117.381 118.765 82.930  1.00 60.60 ?  25  GLN A CG    1 
ATOM   168   C  CD    . GLN A 1 25  ? 116.110 118.023 83.284  1.00 61.28 ?  25  GLN A CD    1 
ATOM   169   O  OE1   . GLN A 1 25  ? 115.040 118.311 82.748  1.00 60.75 ?  25  GLN A OE1   1 
ATOM   170   N  NE2   . GLN A 1 25  ? 116.221 117.060 84.190  1.00 60.63 ?  25  GLN A NE2   1 
ATOM   171   N  N     . PHE A 1 26  ? 120.027 122.803 83.920  1.00 56.32 ?  26  PHE A N     1 
ATOM   172   C  CA    . PHE A 1 26  ? 120.208 124.128 84.504  1.00 54.81 ?  26  PHE A CA    1 
ATOM   173   C  C     . PHE A 1 26  ? 119.057 125.057 84.139  1.00 56.40 ?  26  PHE A C     1 
ATOM   174   O  O     . PHE A 1 26  ? 118.580 125.824 84.984  1.00 56.54 ?  26  PHE A O     1 
ATOM   175   C  CB    . PHE A 1 26  ? 121.540 124.721 84.049  1.00 51.71 ?  26  PHE A CB    1 
ATOM   176   C  CG    . PHE A 1 26  ? 122.741 123.980 84.564  1.00 54.69 ?  26  PHE A CG    1 
ATOM   177   C  CD1   . PHE A 1 26  ? 122.885 123.724 85.916  1.00 52.92 ?  26  PHE A CD1   1 
ATOM   178   C  CD2   . PHE A 1 26  ? 123.724 123.540 83.694  1.00 52.64 ?  26  PHE A CD2   1 
ATOM   179   C  CE1   . PHE A 1 26  ? 123.988 123.043 86.392  1.00 52.85 ?  26  PHE A CE1   1 
ATOM   180   C  CE2   . PHE A 1 26  ? 124.828 122.858 84.164  1.00 50.88 ?  26  PHE A CE2   1 
ATOM   181   C  CZ    . PHE A 1 26  ? 124.961 122.610 85.514  1.00 52.70 ?  26  PHE A CZ    1 
ATOM   182   N  N     . ASP A 1 27  ? 118.596 124.996 82.886  1.00 58.64 ?  27  ASP A N     1 
ATOM   183   C  CA    . ASP A 1 27  ? 117.527 125.883 82.437  1.00 58.79 ?  27  ASP A CA    1 
ATOM   184   C  C     . ASP A 1 27  ? 116.256 125.700 83.256  1.00 59.03 ?  27  ASP A C     1 
ATOM   185   O  O     . ASP A 1 27  ? 115.477 126.649 83.411  1.00 59.44 ?  27  ASP A O     1 
ATOM   186   C  CB    . ASP A 1 27  ? 117.246 125.650 80.950  1.00 59.79 ?  27  ASP A CB    1 
ATOM   187   C  CG    . ASP A 1 27  ? 116.875 124.209 80.641  1.00 62.16 ?  27  ASP A CG    1 
ATOM   188   O  OD1   . ASP A 1 27  ? 115.796 123.756 81.077  1.00 62.25 ?  27  ASP A OD1   1 
ATOM   189   O  OD2   . ASP A 1 27  ? 117.666 123.528 79.957  1.00 62.20 -1 27  ASP A OD2   1 
ATOM   190   N  N     . LYS A 1 28  ? 116.039 124.498 83.797  1.00 56.53 ?  28  LYS A N     1 
ATOM   191   C  CA    . LYS A 1 28  ? 114.869 124.264 84.637  1.00 58.97 ?  28  LYS A CA    1 
ATOM   192   C  C     . LYS A 1 28  ? 114.825 125.231 85.810  1.00 59.60 ?  28  LYS A C     1 
ATOM   193   O  O     . LYS A 1 28  ? 113.737 125.643 86.232  1.00 59.48 ?  28  LYS A O     1 
ATOM   194   C  CB    . LYS A 1 28  ? 114.862 122.820 85.139  1.00 58.52 ?  28  LYS A CB    1 
ATOM   195   C  CG    . LYS A 1 28  ? 114.338 121.816 84.128  1.00 60.37 ?  28  LYS A CG    1 
ATOM   196   C  CD    . LYS A 1 28  ? 112.867 121.520 84.359  1.00 59.68 ?  28  LYS A CD    1 
ATOM   197   C  CE    . LYS A 1 28  ? 112.186 121.081 83.076  1.00 58.32 ?  28  LYS A CE    1 
ATOM   198   N  NZ    . LYS A 1 28  ? 112.295 122.115 82.010  1.00 59.76 1  28  LYS A NZ    1 
ATOM   199   N  N     . ASP A 1 29  ? 115.994 125.621 86.329  1.00 57.46 ?  29  ASP A N     1 
ATOM   200   C  CA    . ASP A 1 29  ? 116.036 126.604 87.408  1.00 54.95 ?  29  ASP A CA    1 
ATOM   201   C  C     . ASP A 1 29  ? 115.269 127.860 87.032  1.00 53.98 ?  29  ASP A C     1 
ATOM   202   O  O     . ASP A 1 29  ? 114.478 128.373 87.833  1.00 56.72 ?  29  ASP A O     1 
ATOM   203   C  CB    . ASP A 1 29  ? 117.484 126.950 87.752  1.00 55.38 ?  29  ASP A CB    1 
ATOM   204   C  CG    . ASP A 1 29  ? 117.655 127.362 89.201  1.00 56.18 ?  29  ASP A CG    1 
ATOM   205   O  OD1   . ASP A 1 29  ? 116.845 126.927 90.045  1.00 55.71 ?  29  ASP A OD1   1 
ATOM   206   O  OD2   . ASP A 1 29  ? 118.605 128.118 89.496  1.00 55.40 -1 29  ASP A OD2   1 
ATOM   207   N  N     . LYS A 1 30  ? 115.461 128.348 85.803  1.00 54.92 ?  30  LYS A N     1 
ATOM   208   C  CA    . LYS A 1 30  ? 114.721 129.518 85.345  1.00 56.30 ?  30  LYS A CA    1 
ATOM   209   C  C     . LYS A 1 30  ? 113.222 129.298 85.489  1.00 55.88 ?  30  LYS A C     1 
ATOM   210   O  O     . LYS A 1 30  ? 112.508 130.141 86.044  1.00 58.29 ?  30  LYS A O     1 
ATOM   211   C  CB    . LYS A 1 30  ? 115.085 129.834 83.894  1.00 57.24 ?  30  LYS A CB    1 
ATOM   212   C  CG    . LYS A 1 30  ? 116.549 130.180 83.681  1.00 59.30 ?  30  LYS A CG    1 
ATOM   213   C  CD    . LYS A 1 30  ? 116.845 130.460 82.216  1.00 59.58 ?  30  LYS A CD    1 
ATOM   214   C  CE    . LYS A 1 30  ? 118.341 130.525 81.958  1.00 58.77 ?  30  LYS A CE    1 
ATOM   215   N  NZ    . LYS A 1 30  ? 118.686 130.170 80.553  1.00 58.18 1  30  LYS A NZ    1 
ATOM   216   N  N     . GLU A 1 31  ? 112.738 128.137 85.036  1.00 57.35 ?  31  GLU A N     1 
ATOM   217   C  CA    . GLU A 1 31  ? 111.321 127.826 85.182  1.00 56.70 ?  31  GLU A CA    1 
ATOM   218   C  C     . GLU A 1 31  ? 110.901 127.899 86.642  1.00 56.29 ?  31  GLU A C     1 
ATOM   219   O  O     . GLU A 1 31  ? 109.852 128.471 86.966  1.00 58.26 ?  31  GLU A O     1 
ATOM   220   C  CB    . GLU A 1 31  ? 111.020 126.442 84.601  1.00 56.01 ?  31  GLU A CB    1 
ATOM   221   C  CG    . GLU A 1 31  ? 111.749 126.090 83.297  1.00 58.50 ?  31  GLU A CG    1 
ATOM   222   C  CD    . GLU A 1 31  ? 111.366 126.965 82.105  1.00 61.13 ?  31  GLU A CD    1 
ATOM   223   O  OE1   . GLU A 1 31  ? 111.409 128.209 82.205  1.00 60.18 ?  31  GLU A OE1   1 
ATOM   224   O  OE2   . GLU A 1 31  ? 111.017 126.392 81.052  1.00 59.93 -1 31  GLU A OE2   1 
ATOM   225   N  N     . ALA A 1 32  ? 111.735 127.365 87.538  1.00 50.08 ?  32  ALA A N     1 
ATOM   226   C  CA    . ALA A 1 32  ? 111.439 127.430 88.964  1.00 48.71 ?  32  ALA A CA    1 
ATOM   227   C  C     . ALA A 1 32  ? 111.171 128.864 89.394  1.00 52.68 ?  32  ALA A C     1 
ATOM   228   O  O     . ALA A 1 32  ? 110.178 129.143 90.079  1.00 55.36 ?  32  ALA A O     1 
ATOM   229   C  CB    . ALA A 1 32  ? 112.592 126.828 89.769  1.00 47.76 ?  32  ALA A CB    1 
ATOM   230   N  N     . VAL A 1 33  ? 112.018 129.799 88.948  1.00 50.76 ?  33  VAL A N     1 
ATOM   231   C  CA    . VAL A 1 33  ? 111.825 131.201 89.309  1.00 49.52 ?  33  VAL A CA    1 
ATOM   232   C  C     . VAL A 1 33  ? 110.429 131.646 88.910  1.00 50.65 ?  33  VAL A C     1 
ATOM   233   O  O     . VAL A 1 33  ? 109.684 132.214 89.717  1.00 52.98 ?  33  VAL A O     1 
ATOM   234   C  CB    . VAL A 1 33  ? 112.898 132.088 88.653  1.00 50.41 ?  33  VAL A CB    1 
ATOM   235   C  CG1   . VAL A 1 33  ? 113.036 133.401 89.413  1.00 48.62 ?  33  VAL A CG1   1 
ATOM   236   C  CG2   . VAL A 1 33  ? 114.216 131.365 88.575  1.00 50.88 ?  33  VAL A CG2   1 
ATOM   237   N  N     . HIS A 1 34  ? 110.038 131.341 87.670  1.00 47.66 ?  34  HIS A N     1 
ATOM   238   C  CA    . HIS A 1 34  ? 108.703 131.694 87.208  1.00 47.52 ?  34  HIS A CA    1 
ATOM   239   C  C     . HIS A 1 34  ? 107.651 131.133 88.151  1.00 50.23 ?  34  HIS A C     1 
ATOM   240   O  O     . HIS A 1 34  ? 106.774 131.864 88.629  1.00 54.05 ?  34  HIS A O     1 
ATOM   241   C  CB    . HIS A 1 34  ? 108.496 131.180 85.784  1.00 50.92 ?  34  HIS A CB    1 
ATOM   242   C  CG    . HIS A 1 34  ? 107.587 132.036 84.959  1.00 50.54 ?  34  HIS A CG    1 
ATOM   243   N  ND1   . HIS A 1 34  ? 106.294 132.327 85.334  1.00 53.04 ?  34  HIS A ND1   1 
ATOM   244   C  CD2   . HIS A 1 34  ? 107.789 132.669 83.779  1.00 51.78 ?  34  HIS A CD2   1 
ATOM   245   C  CE1   . HIS A 1 34  ? 105.736 133.098 84.418  1.00 54.94 ?  34  HIS A CE1   1 
ATOM   246   N  NE2   . HIS A 1 34  ? 106.622 133.322 83.465  1.00 54.28 ?  34  HIS A NE2   1 
ATOM   247   N  N     . SER A 1 35  ? 107.770 129.846 88.487  1.00 48.83 ?  35  SER A N     1 
ATOM   248   C  CA    . SER A 1 35  ? 106.834 129.248 89.429  1.00 49.75 ?  35  SER A CA    1 
ATOM   249   C  C     . SER A 1 35  ? 106.881 129.979 90.760  1.00 50.04 ?  35  SER A C     1 
ATOM   250   O  O     . SER A 1 35  ? 105.839 130.354 91.314  1.00 52.60 ?  35  SER A O     1 
ATOM   251   C  CB    . SER A 1 35  ? 107.151 127.763 89.611  1.00 50.64 ?  35  SER A CB    1 
ATOM   252   O  OG    . SER A 1 35  ? 106.369 127.197 90.648  1.00 52.65 ?  35  SER A OG    1 
ATOM   253   N  N     . TYR A 1 36  ? 108.092 130.254 91.256  1.00 47.40 ?  36  TYR A N     1 
ATOM   254   C  CA    . TYR A 1 36  ? 108.228 130.928 92.542  1.00 48.30 ?  36  TYR A CA    1 
ATOM   255   C  C     . TYR A 1 36  ? 107.558 132.291 92.522  1.00 46.43 ?  36  TYR A C     1 
ATOM   256   O  O     . TYR A 1 36  ? 107.164 132.804 93.574  1.00 46.71 ?  36  TYR A O     1 
ATOM   257   C  CB    . TYR A 1 36  ? 109.704 131.061 92.912  1.00 46.66 ?  36  TYR A CB    1 
ATOM   258   C  CG    . TYR A 1 36  ? 109.942 131.624 94.294  1.00 45.89 ?  36  TYR A CG    1 
ATOM   259   C  CD1   . TYR A 1 36  ? 109.445 130.984 95.421  1.00 46.40 ?  36  TYR A CD1   1 
ATOM   260   C  CD2   . TYR A 1 36  ? 110.670 132.792 94.473  1.00 45.04 ?  36  TYR A CD2   1 
ATOM   261   C  CE1   . TYR A 1 36  ? 109.662 131.493 96.687  1.00 44.74 ?  36  TYR A CE1   1 
ATOM   262   C  CE2   . TYR A 1 36  ? 110.893 133.308 95.735  1.00 44.92 ?  36  TYR A CE2   1 
ATOM   263   C  CZ    . TYR A 1 36  ? 110.387 132.655 96.837  1.00 45.50 ?  36  TYR A CZ    1 
ATOM   264   O  OH    . TYR A 1 36  ? 110.608 133.168 98.094  1.00 47.43 ?  36  TYR A OH    1 
ATOM   265   N  N     . PHE A 1 37  ? 107.404 132.884 91.340  1.00 48.48 ?  37  PHE A N     1 
ATOM   266   C  CA    . PHE A 1 37  ? 106.688 134.143 91.219  1.00 49.98 ?  37  PHE A CA    1 
ATOM   267   C  C     . PHE A 1 37  ? 105.233 133.961 90.820  1.00 52.80 ?  37  PHE A C     1 
ATOM   268   O  O     . PHE A 1 37  ? 104.398 134.794 91.179  1.00 56.29 ?  37  PHE A O     1 
ATOM   269   C  CB    . PHE A 1 37  ? 107.387 135.057 90.207  1.00 51.07 ?  37  PHE A CB    1 
ATOM   270   C  CG    . PHE A 1 37  ? 108.578 135.773 90.773  1.00 51.02 ?  37  PHE A CG    1 
ATOM   271   C  CD1   . PHE A 1 37  ? 108.430 136.989 91.416  1.00 50.72 ?  37  PHE A CD1   1 
ATOM   272   C  CD2   . PHE A 1 37  ? 109.842 135.221 90.679  1.00 50.97 ?  37  PHE A CD2   1 
ATOM   273   C  CE1   . PHE A 1 37  ? 109.522 137.645 91.944  1.00 50.45 ?  37  PHE A CE1   1 
ATOM   274   C  CE2   . PHE A 1 37  ? 110.937 135.873 91.204  1.00 50.90 ?  37  PHE A CE2   1 
ATOM   275   C  CZ    . PHE A 1 37  ? 110.777 137.085 91.840  1.00 49.87 ?  37  PHE A CZ    1 
ATOM   276   N  N     . VAL A 1 38  ? 104.907 132.886 90.100  1.00 54.56 ?  38  VAL A N     1 
ATOM   277   C  CA    . VAL A 1 38  ? 103.523 132.692 89.682  1.00 53.41 ?  38  VAL A CA    1 
ATOM   278   C  C     . VAL A 1 38  ? 102.695 132.109 90.819  1.00 53.94 ?  38  VAL A C     1 
ATOM   279   O  O     . VAL A 1 38  ? 101.512 132.438 90.972  1.00 55.77 ?  38  VAL A O     1 
ATOM   280   C  CB    . VAL A 1 38  ? 103.471 131.815 88.416  1.00 53.67 ?  38  VAL A CB    1 
ATOM   281   C  CG1   . VAL A 1 38  ? 102.171 131.028 88.341  1.00 56.03 ?  38  VAL A CG1   1 
ATOM   282   C  CG2   . VAL A 1 38  ? 103.629 132.680 87.181  1.00 52.77 ?  38  VAL A CG2   1 
ATOM   283   N  N     . ASP A 1 39  ? 103.299 131.264 91.652  1.00 52.80 ?  39  ASP A N     1 
ATOM   284   C  CA    . ASP A 1 39  ? 102.579 130.564 92.706  1.00 53.63 ?  39  ASP A CA    1 
ATOM   285   C  C     . ASP A 1 39  ? 102.678 131.244 94.065  1.00 57.33 ?  39  ASP A C     1 
ATOM   286   O  O     . ASP A 1 39  ? 101.697 131.251 94.815  1.00 58.77 ?  39  ASP A O     1 
ATOM   287   C  CB    . ASP A 1 39  ? 103.092 129.126 92.824  1.00 55.81 ?  39  ASP A CB    1 
ATOM   288   C  CG    . ASP A 1 39  ? 103.180 128.428 91.482  1.00 57.71 ?  39  ASP A CG    1 
ATOM   289   O  OD1   . ASP A 1 39  ? 102.312 128.680 90.621  1.00 56.94 ?  39  ASP A OD1   1 
ATOM   290   O  OD2   . ASP A 1 39  ? 104.119 127.627 91.288  1.00 58.02 -1 39  ASP A OD2   1 
ATOM   291   N  N     . TYR A 1 40  ? 103.831 131.818 94.410  1.00 55.98 ?  40  TYR A N     1 
ATOM   292   C  CA    . TYR A 1 40  ? 104.063 132.307 95.763  1.00 53.64 ?  40  TYR A CA    1 
ATOM   293   C  C     . TYR A 1 40  ? 104.226 133.820 95.839  1.00 58.23 ?  40  TYR A C     1 
ATOM   294   O  O     . TYR A 1 40  ? 103.487 134.479 96.575  1.00 60.63 ?  40  TYR A O     1 
ATOM   295   C  CB    . TYR A 1 40  ? 105.295 131.616 96.361  1.00 53.89 ?  40  TYR A CB    1 
ATOM   296   C  CG    . TYR A 1 40  ? 105.441 131.819 97.853  1.00 54.81 ?  40  TYR A CG    1 
ATOM   297   C  CD1   . TYR A 1 40  ? 106.139 132.906 98.360  1.00 53.49 ?  40  TYR A CD1   1 
ATOM   298   C  CD2   . TYR A 1 40  ? 104.876 130.925 98.752  1.00 55.81 ?  40  TYR A CD2   1 
ATOM   299   C  CE1   . TYR A 1 40  ? 106.272 133.097 99.721  1.00 55.23 ?  40  TYR A CE1   1 
ATOM   300   C  CE2   . TYR A 1 40  ? 105.005 131.108 100.115 1.00 57.31 ?  40  TYR A CE2   1 
ATOM   301   C  CZ    . TYR A 1 40  ? 105.703 132.195 100.593 1.00 58.22 ?  40  TYR A CZ    1 
ATOM   302   O  OH    . TYR A 1 40  ? 105.833 132.380 101.950 1.00 57.01 ?  40  TYR A OH    1 
ATOM   303   N  N     . ILE A 1 41  ? 105.180 134.393 95.103  1.00 55.03 ?  41  ILE A N     1 
ATOM   304   C  CA    . ILE A 1 41  ? 105.563 135.782 95.345  1.00 51.74 ?  41  ILE A CA    1 
ATOM   305   C  C     . ILE A 1 41  ? 104.416 136.728 95.010  1.00 50.75 ?  41  ILE A C     1 
ATOM   306   O  O     . ILE A 1 41  ? 104.065 137.606 95.806  1.00 53.01 ?  41  ILE A O     1 
ATOM   307   C  CB    . ILE A 1 41  ? 106.837 136.139 94.561  1.00 49.42 ?  41  ILE A CB    1 
ATOM   308   C  CG1   . ILE A 1 41  ? 108.044 135.399 95.140  1.00 48.58 ?  41  ILE A CG1   1 
ATOM   309   C  CG2   . ILE A 1 41  ? 107.084 137.635 94.607  1.00 48.07 ?  41  ILE A CG2   1 
ATOM   310   C  CD1   . ILE A 1 41  ? 108.218 135.587 96.628  1.00 46.20 ?  41  ILE A CD1   1 
ATOM   311   N  N     . ASN A 1 42  ? 103.804 136.557 93.836  1.00 51.13 ?  42  ASN A N     1 
ATOM   312   C  CA    . ASN A 1 42  ? 102.714 137.446 93.447  1.00 51.45 ?  42  ASN A CA    1 
ATOM   313   C  C     . ASN A 1 42  ? 101.488 137.260 94.332  1.00 55.41 ?  42  ASN A C     1 
ATOM   314   O  O     . ASN A 1 42  ? 100.773 138.230 94.609  1.00 56.50 ?  42  ASN A O     1 
ATOM   315   C  CB    . ASN A 1 42  ? 102.353 137.226 91.978  1.00 52.87 ?  42  ASN A CB    1 
ATOM   316   C  CG    . ASN A 1 42  ? 103.479 137.609 91.039  1.00 53.98 ?  42  ASN A CG    1 
ATOM   317   O  OD1   . ASN A 1 42  ? 104.440 138.266 91.439  1.00 57.56 ?  42  ASN A OD1   1 
ATOM   318   N  ND2   . ASN A 1 42  ? 103.367 137.200 89.782  1.00 54.07 ?  42  ASN A ND2   1 
ATOM   319   N  N     . GLN A 1 43  ? 101.226 136.030 94.780  1.00 57.91 ?  43  GLN A N     1 
ATOM   320   C  CA    . GLN A 1 43  ? 100.075 135.784 95.642  1.00 55.47 ?  43  GLN A CA    1 
ATOM   321   C  C     . GLN A 1 43  ? 100.235 136.463 96.998  1.00 55.81 ?  43  GLN A C     1 
ATOM   322   O  O     . GLN A 1 43  ? 99.266  137.000 97.547  1.00 56.47 ?  43  GLN A O     1 
ATOM   323   C  CB    . GLN A 1 43  ? 99.866  134.281 95.817  1.00 55.39 ?  43  GLN A CB    1 
ATOM   324   C  CG    . GLN A 1 43  ? 98.929  133.657 94.795  1.00 57.56 ?  43  GLN A CG    1 
ATOM   325   C  CD    . GLN A 1 43  ? 99.479  133.712 93.382  1.00 58.38 ?  43  GLN A CD    1 
ATOM   326   O  OE1   . GLN A 1 43  ? 100.680 133.883 93.177  1.00 57.94 ?  43  GLN A OE1   1 
ATOM   327   N  NE2   . GLN A 1 43  ? 98.598  133.566 92.399  1.00 56.72 ?  43  GLN A NE2   1 
ATOM   328   N  N     . ASN A 1 44  ? 101.446 136.451 97.552  1.00 54.90 ?  44  ASN A N     1 
ATOM   329   C  CA    . ASN A 1 44  ? 101.705 136.993 98.879  1.00 55.01 ?  44  ASN A CA    1 
ATOM   330   C  C     . ASN A 1 44  ? 102.303 138.394 98.848  1.00 54.27 ?  44  ASN A C     1 
ATOM   331   O  O     . ASN A 1 44  ? 102.805 138.863 99.874  1.00 54.47 ?  44  ASN A O     1 
ATOM   332   C  CB    . ASN A 1 44  ? 102.619 136.048 99.664  1.00 53.41 ?  44  ASN A CB    1 
ATOM   333   C  CG    . ASN A 1 44  ? 102.044 134.650 99.789  1.00 55.83 ?  44  ASN A CG    1 
ATOM   334   O  OD1   . ASN A 1 44  ? 101.612 134.237 100.864 1.00 56.75 ?  44  ASN A OD1   1 
ATOM   335   N  ND2   . ASN A 1 44  ? 102.037 133.914 98.684  1.00 56.44 ?  44  ASN A ND2   1 
ATOM   336   N  N     . THR A 1 45  ? 102.264 139.071 97.704  1.00 54.15 ?  45  THR A N     1 
ATOM   337   C  CA    . THR A 1 45  ? 102.755 140.438 97.589  1.00 55.09 ?  45  THR A CA    1 
ATOM   338   C  C     . THR A 1 45  ? 101.590 141.407 97.728  1.00 55.66 ?  45  THR A C     1 
ATOM   339   O  O     . THR A 1 45  ? 100.601 141.307 96.992  1.00 56.05 ?  45  THR A O     1 
ATOM   340   C  CB    . THR A 1 45  ? 103.469 140.658 96.252  1.00 55.01 ?  45  THR A CB    1 
ATOM   341   O  OG1   . THR A 1 45  ? 104.796 140.121 96.324  1.00 57.88 ?  45  THR A OG1   1 
ATOM   342   C  CG2   . THR A 1 45  ? 103.552 142.142 95.923  1.00 53.39 ?  45  THR A CG2   1 
ATOM   343   N  N     . VAL A 1 46  ? 101.707 142.339 98.672  1.00 55.46 ?  46  VAL A N     1 
ATOM   344   C  CA    . VAL A 1 46  ? 100.658 143.329 98.886  1.00 55.19 ?  46  VAL A CA    1 
ATOM   345   C  C     . VAL A 1 46  ? 100.702 144.345 97.753  1.00 55.73 ?  46  VAL A C     1 
ATOM   346   O  O     . VAL A 1 46  ? 101.747 144.944 97.477  1.00 58.54 ?  46  VAL A O     1 
ATOM   347   C  CB    . VAL A 1 46  ? 100.817 144.012 100.250 1.00 55.20 ?  46  VAL A CB    1 
ATOM   348   C  CG1   . VAL A 1 46  ? 99.812  145.141 100.397 1.00 54.96 ?  46  VAL A CG1   1 
ATOM   349   C  CG2   . VAL A 1 46  ? 100.650 143.005 101.368 1.00 54.62 ?  46  VAL A CG2   1 
ATOM   350   N  N     . PHE A 1 47  ? 99.567  144.545 97.093  1.00 59.11 ?  47  PHE A N     1 
ATOM   351   C  CA    . PHE A 1 47  ? 99.458  145.488 95.993  1.00 59.69 ?  47  PHE A CA    1 
ATOM   352   C  C     . PHE A 1 47  ? 98.559  146.652 96.386  1.00 61.94 ?  47  PHE A C     1 
ATOM   353   O  O     . PHE A 1 47  ? 97.595  146.491 97.139  1.00 63.68 ?  47  PHE A O     1 
ATOM   354   C  CB    . PHE A 1 47  ? 98.914  144.813 94.732  1.00 60.14 ?  47  PHE A CB    1 
ATOM   355   C  CG    . PHE A 1 47  ? 99.285  145.522 93.461  1.00 62.75 ?  47  PHE A CG    1 
ATOM   356   C  CD1   . PHE A 1 47  ? 100.551 145.384 92.920  1.00 61.43 ?  47  PHE A CD1   1 
ATOM   357   C  CD2   . PHE A 1 47  ? 98.368  146.332 92.811  1.00 62.25 ?  47  PHE A CD2   1 
ATOM   358   C  CE1   . PHE A 1 47  ? 100.897 146.038 91.752  1.00 61.54 ?  47  PHE A CE1   1 
ATOM   359   C  CE2   . PHE A 1 47  ? 98.708  146.989 91.643  1.00 61.58 ?  47  PHE A CE2   1 
ATOM   360   C  CZ    . PHE A 1 47  ? 99.973  146.841 91.114  1.00 61.77 ?  47  PHE A CZ    1 
ATOM   361   N  N     . PHE A 1 48  ? 98.889  147.827 95.863  1.00 57.51 ?  48  PHE A N     1 
ATOM   362   C  CA    . PHE A 1 48  ? 98.163  149.054 96.143  1.00 57.86 ?  48  PHE A CA    1 
ATOM   363   C  C     . PHE A 1 48  ? 97.667  149.663 94.838  1.00 58.93 ?  48  PHE A C     1 
ATOM   364   O  O     . PHE A 1 48  ? 98.200  149.389 93.759  1.00 61.11 ?  48  PHE A O     1 
ATOM   365   C  CB    . PHE A 1 48  ? 99.040  150.061 96.896  1.00 57.18 ?  48  PHE A CB    1 
ATOM   366   C  CG    . PHE A 1 48  ? 99.522  149.570 98.234  1.00 56.27 ?  48  PHE A CG    1 
ATOM   367   C  CD1   . PHE A 1 48  ? 100.652 148.777 98.332  1.00 56.87 ?  48  PHE A CD1   1 
ATOM   368   C  CD2   . PHE A 1 48  ? 98.850  149.914 99.394  1.00 58.06 ?  48  PHE A CD2   1 
ATOM   369   C  CE1   . PHE A 1 48  ? 101.100 148.332 99.561  1.00 57.84 ?  48  PHE A CE1   1 
ATOM   370   C  CE2   . PHE A 1 48  ? 99.292  149.469 100.626 1.00 58.40 ?  48  PHE A CE2   1 
ATOM   371   C  CZ    . PHE A 1 48  ? 100.418 148.677 100.708 1.00 57.22 ?  48  PHE A CZ    1 
ATOM   372   N  N     . HIS A 1 49  ? 96.627  150.492 94.951  1.00 63.64 ?  49  HIS A N     1 
ATOM   373   C  CA    . HIS A 1 49  ? 96.055  151.121 93.765  1.00 66.40 ?  49  HIS A CA    1 
ATOM   374   C  C     . HIS A 1 49  ? 97.058  152.035 93.075  1.00 67.18 ?  49  HIS A C     1 
ATOM   375   O  O     . HIS A 1 49  ? 97.047  152.155 91.845  1.00 67.16 ?  49  HIS A O     1 
ATOM   376   C  CB    . HIS A 1 49  ? 94.793  151.899 94.141  1.00 67.54 ?  49  HIS A CB    1 
ATOM   377   C  CG    . HIS A 1 49  ? 94.072  152.485 92.967  1.00 69.46 ?  49  HIS A CG    1 
ATOM   378   N  ND1   . HIS A 1 49  ? 93.675  151.729 91.886  1.00 68.49 ?  49  HIS A ND1   1 
ATOM   379   C  CD2   . HIS A 1 49  ? 93.675  153.752 92.707  1.00 67.80 ?  49  HIS A CD2   1 
ATOM   380   C  CE1   . HIS A 1 49  ? 93.065  152.506 91.008  1.00 68.74 ?  49  HIS A CE1   1 
ATOM   381   N  NE2   . HIS A 1 49  ? 93.051  153.739 91.482  1.00 69.21 ?  49  HIS A NE2   1 
ATOM   382   N  N     . ASN A 1 50  ? 97.929  152.684 93.844  1.00 64.74 ?  50  ASN A N     1 
ATOM   383   C  CA    . ASN A 1 50  ? 98.972  153.532 93.288  1.00 63.49 ?  50  ASN A CA    1 
ATOM   384   C  C     . ASN A 1 50  ? 100.125 153.600 94.279  1.00 62.85 ?  50  ASN A C     1 
ATOM   385   O  O     . ASN A 1 50  ? 100.001 153.196 95.437  1.00 61.77 ?  50  ASN A O     1 
ATOM   386   C  CB    . ASN A 1 50  ? 98.436  154.928 92.939  1.00 62.57 ?  50  ASN A CB    1 
ATOM   387   C  CG    . ASN A 1 50  ? 98.067  155.745 94.167  1.00 64.44 ?  50  ASN A CG    1 
ATOM   388   O  OD1   . ASN A 1 50  ? 97.915  155.211 95.265  1.00 64.51 ?  50  ASN A OD1   1 
ATOM   389   N  ND2   . ASN A 1 50  ? 97.922  157.050 93.981  1.00 63.77 ?  50  ASN A ND2   1 
ATOM   390   N  N     . LEU A 1 51  ? 101.262 154.113 93.802  1.00 57.68 ?  51  LEU A N     1 
ATOM   391   C  CA    . LEU A 1 51  ? 102.449 154.188 94.648  1.00 56.20 ?  51  LEU A CA    1 
ATOM   392   C  C     . LEU A 1 51  ? 102.250 155.143 95.817  1.00 57.94 ?  51  LEU A C     1 
ATOM   393   O  O     . LEU A 1 51  ? 102.877 154.970 96.868  1.00 59.15 ?  51  LEU A O     1 
ATOM   394   C  CB    . LEU A 1 51  ? 103.658 154.612 93.819  1.00 55.60 ?  51  LEU A CB    1 
ATOM   395   C  CG    . LEU A 1 51  ? 105.013 154.674 94.524  1.00 55.06 ?  51  LEU A CG    1 
ATOM   396   C  CD1   . LEU A 1 51  ? 105.447 153.291 94.981  1.00 54.14 ?  51  LEU A CD1   1 
ATOM   397   C  CD2   . LEU A 1 51  ? 106.053 155.294 93.611  1.00 54.35 ?  51  LEU A CD2   1 
ATOM   398   N  N     . LYS A 1 52  ? 101.398 156.157 95.656  1.00 57.99 ?  52  LYS A N     1 
ATOM   399   C  CA    . LYS A 1 52  ? 101.129 157.079 96.754  1.00 57.65 ?  52  LYS A CA    1 
ATOM   400   C  C     . LYS A 1 52  ? 100.512 156.345 97.938  1.00 58.88 ?  52  LYS A C     1 
ATOM   401   O  O     . LYS A 1 52  ? 100.912 156.551 99.090  1.00 59.30 ?  52  LYS A O     1 
ATOM   402   C  CB    . LYS A 1 52  ? 100.212 158.206 96.274  1.00 57.85 ?  52  LYS A CB    1 
ATOM   403   C  CG    . LYS A 1 52  ? 100.557 159.579 96.831  1.00 58.85 ?  52  LYS A CG    1 
ATOM   404   C  CD    . LYS A 1 52  ? 100.173 159.709 98.292  1.00 59.24 ?  52  LYS A CD    1 
ATOM   405   C  CE    . LYS A 1 52  ? 100.387 161.126 98.793  1.00 59.48 ?  52  LYS A CE    1 
ATOM   406   N  NZ    . LYS A 1 52  ? 100.575 161.168 100.269 1.00 59.50 1  52  LYS A NZ    1 
ATOM   407   N  N     . GLU A 1 53  ? 99.541  155.469 97.666  1.00 60.58 ?  53  GLU A N     1 
ATOM   408   C  CA    . GLU A 1 53  ? 98.925  154.688 98.733  1.00 60.45 ?  53  GLU A CA    1 
ATOM   409   C  C     . GLU A 1 53  ? 99.933  153.751 99.384  1.00 60.19 ?  53  GLU A C     1 
ATOM   410   O  O     . GLU A 1 53  ? 99.935  153.585 100.608 1.00 60.00 ?  53  GLU A O     1 
ATOM   411   C  CB    . GLU A 1 53  ? 97.737  153.897 98.184  1.00 61.07 ?  53  GLU A CB    1 
ATOM   412   C  CG    . GLU A 1 53  ? 96.914  153.186 99.245  1.00 62.36 ?  53  GLU A CG    1 
ATOM   413   C  CD    . GLU A 1 53  ? 95.913  152.216 98.649  1.00 63.76 ?  53  GLU A CD    1 
ATOM   414   O  OE1   . GLU A 1 53  ? 95.863  151.055 99.107  1.00 62.97 ?  53  GLU A OE1   1 
ATOM   415   O  OE2   . GLU A 1 53  ? 95.177  152.612 97.721  1.00 62.77 -1 53  GLU A OE2   1 
ATOM   416   N  N     . LYS A 1 54  ? 100.796 153.127 98.579  1.00 58.66 ?  54  LYS A N     1 
ATOM   417   C  CA    . LYS A 1 54  ? 101.809 152.229 99.126  1.00 54.61 ?  54  LYS A CA    1 
ATOM   418   C  C     . LYS A 1 54  ? 102.760 152.974 100.053 1.00 52.64 ?  54  LYS A C     1 
ATOM   419   O  O     . LYS A 1 54  ? 103.061 152.511 101.160 1.00 55.36 ?  54  LYS A O     1 
ATOM   420   C  CB    . LYS A 1 54  ? 102.583 151.564 97.989  1.00 54.10 ?  54  LYS A CB    1 
ATOM   421   C  CG    . LYS A 1 54  ? 103.824 150.818 98.443  1.00 57.14 ?  54  LYS A CG    1 
ATOM   422   C  CD    . LYS A 1 54  ? 104.283 149.825 97.394  1.00 55.57 ?  54  LYS A CD    1 
ATOM   423   C  CE    . LYS A 1 54  ? 105.489 149.040 97.868  1.00 55.37 ?  54  LYS A CE    1 
ATOM   424   N  NZ    . LYS A 1 54  ? 105.663 147.780 97.096  1.00 55.79 1  54  LYS A NZ    1 
ATOM   425   N  N     . LEU A 1 55  ? 103.242 154.138 99.614  1.00 53.92 ?  55  LEU A N     1 
ATOM   426   C  CA    . LEU A 1 55  ? 104.163 154.916 100.434 1.00 55.07 ?  55  LEU A CA    1 
ATOM   427   C  C     . LEU A 1 55  ? 103.483 155.418 101.700 1.00 57.40 ?  55  LEU A C     1 
ATOM   428   O  O     . LEU A 1 55  ? 104.089 155.410 102.777 1.00 58.63 ?  55  LEU A O     1 
ATOM   429   C  CB    . LEU A 1 55  ? 104.729 156.081 99.625  1.00 55.64 ?  55  LEU A CB    1 
ATOM   430   C  CG    . LEU A 1 55  ? 105.635 155.704 98.452  1.00 56.12 ?  55  LEU A CG    1 
ATOM   431   C  CD1   . LEU A 1 55  ? 105.967 156.931 97.622  1.00 56.83 ?  55  LEU A CD1   1 
ATOM   432   C  CD2   . LEU A 1 55  ? 106.903 155.019 98.937  1.00 53.50 ?  55  LEU A CD2   1 
ATOM   433   N  N     . ASP A 1 56  ? 102.223 155.853 101.594 1.00 60.10 ?  56  ASP A N     1 
ATOM   434   C  CA    . ASP A 1 56  ? 101.497 156.296 102.778 1.00 59.38 ?  56  ASP A CA    1 
ATOM   435   C  C     . ASP A 1 56  ? 101.313 155.155 103.770 1.00 57.92 ?  56  ASP A C     1 
ATOM   436   O  O     . ASP A 1 56  ? 101.493 155.340 104.978 1.00 57.64 ?  56  ASP A O     1 
ATOM   437   C  CB    . ASP A 1 56  ? 100.143 156.879 102.377 1.00 60.22 ?  56  ASP A CB    1 
ATOM   438   C  CG    . ASP A 1 56  ? 100.263 158.262 101.772 1.00 62.26 ?  56  ASP A CG    1 
ATOM   439   O  OD1   . ASP A 1 56  ? 99.259  158.757 101.218 1.00 62.19 ?  56  ASP A OD1   1 
ATOM   440   O  OD2   . ASP A 1 56  ? 101.360 158.853 101.850 1.00 61.30 -1 56  ASP A OD2   1 
ATOM   441   N  N     . TYR A 1 57  ? 100.958 153.966 103.279 1.00 52.63 ?  57  TYR A N     1 
ATOM   442   C  CA    . TYR A 1 57  ? 100.779 152.823 104.167 1.00 54.65 ?  57  TYR A CA    1 
ATOM   443   C  C     . TYR A 1 57  ? 102.089 152.427 104.832 1.00 56.13 ?  57  TYR A C     1 
ATOM   444   O  O     . TYR A 1 57  ? 102.112 152.099 106.024 1.00 57.38 ?  57  TYR A O     1 
ATOM   445   C  CB    . TYR A 1 57  ? 100.191 151.643 103.393 1.00 53.46 ?  57  TYR A CB    1 
ATOM   446   C  CG    . TYR A 1 57  ? 100.090 150.372 104.205 1.00 55.24 ?  57  TYR A CG    1 
ATOM   447   C  CD1   . TYR A 1 57  ? 99.021  150.158 105.065 1.00 54.93 ?  57  TYR A CD1   1 
ATOM   448   C  CD2   . TYR A 1 57  ? 101.064 149.385 104.110 1.00 55.44 ?  57  TYR A CD2   1 
ATOM   449   C  CE1   . TYR A 1 57  ? 98.927  148.998 105.809 1.00 55.25 ?  57  TYR A CE1   1 
ATOM   450   C  CE2   . TYR A 1 57  ? 100.977 148.225 104.851 1.00 55.86 ?  57  TYR A CE2   1 
ATOM   451   C  CZ    . TYR A 1 57  ? 99.906  148.035 105.698 1.00 55.58 ?  57  TYR A CZ    1 
ATOM   452   O  OH    . TYR A 1 57  ? 99.817  146.877 106.435 1.00 56.63 ?  57  TYR A OH    1 
ATOM   453   N  N     . LEU A 1 58  ? 103.190 152.441 104.078 1.00 51.42 ?  58  LEU A N     1 
ATOM   454   C  CA    . LEU A 1 58  ? 104.471 152.033 104.646 1.00 50.27 ?  58  LEU A CA    1 
ATOM   455   C  C     . LEU A 1 58  ? 104.986 153.056 105.652 1.00 51.95 ?  58  LEU A C     1 
ATOM   456   O  O     . LEU A 1 58  ? 105.563 152.685 106.680 1.00 52.72 ?  58  LEU A O     1 
ATOM   457   C  CB    . LEU A 1 58  ? 105.487 151.801 103.529 1.00 49.61 ?  58  LEU A CB    1 
ATOM   458   C  CG    . LEU A 1 58  ? 105.196 150.577 102.654 1.00 50.58 ?  58  LEU A CG    1 
ATOM   459   C  CD1   . LEU A 1 58  ? 106.018 150.603 101.378 1.00 51.28 ?  58  LEU A CD1   1 
ATOM   460   C  CD2   . LEU A 1 58  ? 105.442 149.291 103.425 1.00 51.20 ?  58  LEU A CD2   1 
ATOM   461   N  N     . VAL A 1 59  ? 104.785 154.347 105.380 1.00 53.73 ?  59  VAL A N     1 
ATOM   462   C  CA    . VAL A 1 59  ? 105.236 155.378 106.309 1.00 54.61 ?  59  VAL A CA    1 
ATOM   463   C  C     . VAL A 1 59  ? 104.379 155.377 107.571 1.00 57.60 ?  59  VAL A C     1 
ATOM   464   O  O     . VAL A 1 59  ? 104.896 155.441 108.692 1.00 56.54 ?  59  VAL A O     1 
ATOM   465   C  CB    . VAL A 1 59  ? 105.227 156.753 105.620 1.00 54.59 ?  59  VAL A CB    1 
ATOM   466   C  CG1   . VAL A 1 59  ? 105.234 157.864 106.653 1.00 53.14 ?  59  VAL A CG1   1 
ATOM   467   C  CG2   . VAL A 1 59  ? 106.418 156.883 104.687 1.00 54.08 ?  59  VAL A CG2   1 
ATOM   468   N  N     . GLU A 1 60  ? 103.056 155.297 107.405 1.00 60.48 ?  60  GLU A N     1 
ATOM   469   C  CA    . GLU A 1 60  ? 102.153 155.381 108.548 1.00 58.01 ?  60  GLU A CA    1 
ATOM   470   C  C     . GLU A 1 60  ? 102.307 154.180 109.472 1.00 57.85 ?  60  GLU A C     1 
ATOM   471   O  O     . GLU A 1 60  ? 102.247 154.323 110.699 1.00 58.08 ?  60  GLU A O     1 
ATOM   472   C  CB    . GLU A 1 60  ? 100.709 155.511 108.064 1.00 58.23 ?  60  GLU A CB    1 
ATOM   473   C  CG    . GLU A 1 60  ? 100.358 156.892 107.533 1.00 59.63 ?  60  GLU A CG    1 
ATOM   474   C  CD    . GLU A 1 60  ? 99.158  156.875 106.605 1.00 61.74 ?  60  GLU A CD    1 
ATOM   475   O  OE1   . GLU A 1 60  ? 98.494  155.821 106.508 1.00 59.38 ?  60  GLU A OE1   1 
ATOM   476   O  OE2   . GLU A 1 60  ? 98.882  157.914 105.969 1.00 61.31 -1 60  GLU A OE2   1 
ATOM   477   N  N     . ASN A 1 61  ? 102.505 152.990 108.908 1.00 53.71 ?  61  ASN A N     1 
ATOM   478   C  CA    . ASN A 1 61  ? 102.654 151.772 109.695 1.00 52.50 ?  61  ASN A CA    1 
ATOM   479   C  C     . ASN A 1 61  ? 104.076 151.564 110.203 1.00 54.36 ?  61  ASN A C     1 
ATOM   480   O  O     . ASN A 1 61  ? 104.427 150.437 110.576 1.00 54.46 ?  61  ASN A O     1 
ATOM   481   C  CB    . ASN A 1 61  ? 102.205 150.560 108.878 1.00 53.45 ?  61  ASN A CB    1 
ATOM   482   C  CG    . ASN A 1 61  ? 100.697 150.450 108.782 1.00 56.30 ?  61  ASN A CG    1 
ATOM   483   O  OD1   . ASN A 1 61  ? 100.002 151.447 108.593 1.00 54.48 ?  61  ASN A OD1   1 
ATOM   484   N  ND2   . ASN A 1 61  ? 100.183 149.233 108.913 1.00 55.68 ?  61  ASN A ND2   1 
ATOM   485   N  N     . GLN A 1 62  ? 104.889 152.622 110.220 1.00 53.25 ?  62  GLN A N     1 
ATOM   486   C  CA    . GLN A 1 62  ? 106.247 152.593 110.768 1.00 52.66 ?  62  GLN A CA    1 
ATOM   487   C  C     . GLN A 1 62  ? 107.140 151.586 110.047 1.00 52.40 ?  62  GLN A C     1 
ATOM   488   O  O     . GLN A 1 62  ? 108.028 150.984 110.655 1.00 53.31 ?  62  GLN A O     1 
ATOM   489   C  CB    . GLN A 1 62  ? 106.235 152.313 112.274 1.00 51.98 ?  62  GLN A CB    1 
ATOM   490   C  CG    . GLN A 1 62  ? 105.167 153.078 113.043 1.00 51.77 ?  62  GLN A CG    1 
ATOM   491   C  CD    . GLN A 1 62  ? 105.312 154.581 112.907 1.00 54.59 ?  62  GLN A CD    1 
ATOM   492   O  OE1   . GLN A 1 62  ? 106.242 155.177 113.447 1.00 54.15 ?  62  GLN A OE1   1 
ATOM   493   N  NE2   . GLN A 1 62  ? 104.389 155.200 112.182 1.00 54.94 ?  62  GLN A NE2   1 
ATOM   494   N  N     . TYR A 1 63  ? 106.912 151.390 108.749 1.00 50.12 ?  63  TYR A N     1 
ATOM   495   C  CA    . TYR A 1 63  ? 107.815 150.581 107.938 1.00 46.66 ?  63  TYR A CA    1 
ATOM   496   C  C     . TYR A 1 63  ? 108.979 151.410 107.407 1.00 48.34 ?  63  TYR A C     1 
ATOM   497   O  O     . TYR A 1 63  ? 110.132 150.975 107.465 1.00 49.61 ?  63  TYR A O     1 
ATOM   498   C  CB    . TYR A 1 63  ? 107.060 149.935 106.773 1.00 47.01 ?  63  TYR A CB    1 
ATOM   499   C  CG    . TYR A 1 63  ? 106.095 148.847 107.181 1.00 49.24 ?  63  TYR A CG    1 
ATOM   500   C  CD1   . TYR A 1 63  ? 106.543 147.702 107.823 1.00 48.39 ?  63  TYR A CD1   1 
ATOM   501   C  CD2   . TYR A 1 63  ? 104.739 148.963 106.914 1.00 50.04 ?  63  TYR A CD2   1 
ATOM   502   C  CE1   . TYR A 1 63  ? 105.664 146.705 108.192 1.00 48.45 ?  63  TYR A CE1   1 
ATOM   503   C  CE2   . TYR A 1 63  ? 103.854 147.971 107.279 1.00 50.57 ?  63  TYR A CE2   1 
ATOM   504   C  CZ    . TYR A 1 63  ? 104.321 146.846 107.920 1.00 50.75 ?  63  TYR A CZ    1 
ATOM   505   O  OH    . TYR A 1 63  ? 103.437 145.858 108.284 1.00 53.58 ?  63  TYR A OH    1 
ATOM   506   N  N     . TYR A 1 64  ? 108.688 152.599 106.890 1.00 47.25 ?  64  TYR A N     1 
ATOM   507   C  CA    . TYR A 1 64  ? 109.686 153.489 106.318 1.00 43.93 ?  64  TYR A CA    1 
ATOM   508   C  C     . TYR A 1 64  ? 109.944 154.670 107.244 1.00 46.86 ?  64  TYR A C     1 
ATOM   509   O  O     . TYR A 1 64  ? 109.261 154.869 108.251 1.00 49.91 ?  64  TYR A O     1 
ATOM   510   C  CB    . TYR A 1 64  ? 109.241 154.000 104.944 1.00 45.49 ?  64  TYR A CB    1 
ATOM   511   C  CG    . TYR A 1 64  ? 109.366 152.989 103.834 1.00 45.64 ?  64  TYR A CG    1 
ATOM   512   C  CD1   . TYR A 1 64  ? 109.975 151.760 104.050 1.00 42.74 ?  64  TYR A CD1   1 
ATOM   513   C  CD2   . TYR A 1 64  ? 108.878 153.265 102.567 1.00 47.43 ?  64  TYR A CD2   1 
ATOM   514   C  CE1   . TYR A 1 64  ? 110.090 150.835 103.035 1.00 40.32 ?  64  TYR A CE1   1 
ATOM   515   C  CE2   . TYR A 1 64  ? 108.988 152.350 101.548 1.00 46.63 ?  64  TYR A CE2   1 
ATOM   516   C  CZ    . TYR A 1 64  ? 109.593 151.136 101.786 1.00 44.90 ?  64  TYR A CZ    1 
ATOM   517   O  OH    . TYR A 1 64  ? 109.701 150.224 100.764 1.00 44.35 ?  64  TYR A OH    1 
ATOM   518   N  N     . GLU A 1 65  ? 110.952 155.457 106.881 1.00 52.27 ?  65  GLU A N     1 
ATOM   519   C  CA    . GLU A 1 65  ? 111.233 156.716 107.550 1.00 50.80 ?  65  GLU A CA    1 
ATOM   520   C  C     . GLU A 1 65  ? 110.647 157.870 106.748 1.00 53.51 ?  65  GLU A C     1 
ATOM   521   O  O     . GLU A 1 65  ? 110.678 157.864 105.514 1.00 54.80 ?  65  GLU A O     1 
ATOM   522   C  CB    . GLU A 1 65  ? 112.739 156.915 107.731 1.00 50.17 ?  65  GLU A CB    1 
ATOM   523   C  CG    . GLU A 1 65  ? 113.338 156.155 108.901 1.00 51.49 ?  65  GLU A CG    1 
ATOM   524   C  CD    . GLU A 1 65  ? 114.809 155.851 108.707 1.00 52.41 ?  65  GLU A CD    1 
ATOM   525   O  OE1   . GLU A 1 65  ? 115.460 156.546 107.899 1.00 53.30 ?  65  GLU A OE1   1 
ATOM   526   O  OE2   . GLU A 1 65  ? 115.321 154.925 109.369 1.00 52.68 -1 65  GLU A OE2   1 
ATOM   527   N  N     . GLU A 1 66  ? 110.104 158.859 107.459 1.00 54.86 ?  66  GLU A N     1 
ATOM   528   C  CA    . GLU A 1 66  ? 109.532 160.026 106.799 1.00 54.45 ?  66  GLU A CA    1 
ATOM   529   C  C     . GLU A 1 66  ? 110.602 160.973 106.276 1.00 56.09 ?  66  GLU A C     1 
ATOM   530   O  O     . GLU A 1 66  ? 110.378 161.660 105.273 1.00 56.40 ?  66  GLU A O     1 
ATOM   531   C  CB    . GLU A 1 66  ? 108.611 160.778 107.765 1.00 55.78 ?  66  GLU A CB    1 
ATOM   532   C  CG    . GLU A 1 66  ? 107.106 160.775 107.437 1.00 57.32 ?  66  GLU A CG    1 
ATOM   533   C  CD    . GLU A 1 66  ? 106.725 161.363 106.076 1.00 58.41 ?  66  GLU A CD    1 
ATOM   534   O  OE1   . GLU A 1 66  ? 107.594 161.575 105.205 1.00 58.37 ?  66  GLU A OE1   1 
ATOM   535   O  OE2   . GLU A 1 66  ? 105.519 161.621 105.878 1.00 55.35 -1 66  GLU A OE2   1 
ATOM   536   N  N     . GLU A 1 67  ? 111.761 161.025 106.936 1.00 54.76 ?  67  GLU A N     1 
ATOM   537   C  CA    . GLU A 1 67  ? 112.750 162.056 106.631 1.00 55.13 ?  67  GLU A CA    1 
ATOM   538   C  C     . GLU A 1 67  ? 113.302 161.907 105.218 1.00 55.53 ?  67  GLU A C     1 
ATOM   539   O  O     . GLU A 1 67  ? 113.375 162.884 104.464 1.00 55.42 ?  67  GLU A O     1 
ATOM   540   C  CB    . GLU A 1 67  ? 113.882 162.011 107.659 1.00 56.55 ?  67  GLU A CB    1 
ATOM   541   C  CG    . GLU A 1 67  ? 113.407 162.004 109.102 1.00 57.39 ?  67  GLU A CG    1 
ATOM   542   C  CD    . GLU A 1 67  ? 113.376 160.612 109.700 1.00 60.75 ?  67  GLU A CD    1 
ATOM   543   O  OE1   . GLU A 1 67  ? 114.453 160.098 110.069 1.00 59.46 ?  67  GLU A OE1   1 
ATOM   544   O  OE2   . GLU A 1 67  ? 112.274 160.032 109.802 1.00 57.42 -1 67  GLU A OE2   1 
ATOM   545   N  N     . PHE A 1 68  ? 113.695 160.689 104.837 1.00 48.39 ?  68  PHE A N     1 
ATOM   546   C  CA    . PHE A 1 68  ? 114.336 160.512 103.538 1.00 44.87 ?  68  PHE A CA    1 
ATOM   547   C  C     . PHE A 1 68  ? 113.334 160.611 102.395 1.00 44.22 ?  68  PHE A C     1 
ATOM   548   O  O     . PHE A 1 68  ? 113.699 161.035 101.292 1.00 47.66 ?  68  PHE A O     1 
ATOM   549   C  CB    . PHE A 1 68  ? 115.091 159.180 103.497 1.00 46.19 ?  68  PHE A CB    1 
ATOM   550   C  CG    . PHE A 1 68  ? 114.262 158.014 103.039 1.00 44.21 ?  68  PHE A CG    1 
ATOM   551   C  CD1   . PHE A 1 68  ? 113.406 157.368 103.913 1.00 44.39 ?  68  PHE A CD1   1 
ATOM   552   C  CD2   . PHE A 1 68  ? 114.364 157.544 101.740 1.00 39.83 ?  68  PHE A CD2   1 
ATOM   553   C  CE1   . PHE A 1 68  ? 112.651 156.290 103.495 1.00 42.62 ?  68  PHE A CE1   1 
ATOM   554   C  CE2   . PHE A 1 68  ? 113.613 156.468 101.316 1.00 43.07 ?  68  PHE A CE2   1 
ATOM   555   C  CZ    . PHE A 1 68  ? 112.757 155.838 102.196 1.00 45.52 ?  68  PHE A CZ    1 
ATOM   556   N  N     . LEU A 1 69  ? 112.077 160.232 102.630 1.00 46.25 ?  69  LEU A N     1 
ATOM   557   C  CA    . LEU A 1 69  ? 111.061 160.382 101.595 1.00 46.48 ?  69  LEU A CA    1 
ATOM   558   C  C     . LEU A 1 69  ? 110.588 161.823 101.464 1.00 48.21 ?  69  LEU A C     1 
ATOM   559   O  O     . LEU A 1 69  ? 110.159 162.233 100.378 1.00 45.42 ?  69  LEU A O     1 
ATOM   560   C  CB    . LEU A 1 69  ? 109.872 159.464 101.882 1.00 45.84 ?  69  LEU A CB    1 
ATOM   561   C  CG    . LEU A 1 69  ? 110.076 157.988 101.531 1.00 43.33 ?  69  LEU A CG    1 
ATOM   562   C  CD1   . LEU A 1 69  ? 108.867 157.162 101.935 1.00 43.30 ?  69  LEU A CD1   1 
ATOM   563   C  CD2   . LEU A 1 69  ? 110.377 157.820 100.051 1.00 42.58 ?  69  LEU A CD2   1 
ATOM   564   N  N     . SER A 1 70  ? 110.660 162.604 102.544 1.00 50.75 ?  70  SER A N     1 
ATOM   565   C  CA    . SER A 1 70  ? 110.208 163.990 102.499 1.00 49.04 ?  70  SER A CA    1 
ATOM   566   C  C     . SER A 1 70  ? 111.135 164.882 101.685 1.00 49.55 ?  70  SER A C     1 
ATOM   567   O  O     . SER A 1 70  ? 110.730 165.984 101.301 1.00 51.31 ?  70  SER A O     1 
ATOM   568   C  CB    . SER A 1 70  ? 110.071 164.541 103.919 1.00 50.83 ?  70  SER A CB    1 
ATOM   569   O  OG    . SER A 1 70  ? 111.342 164.795 104.491 1.00 52.71 ?  70  SER A OG    1 
ATOM   570   N  N     . LEU A 1 71  ? 112.364 164.438 101.415 1.00 44.06 ?  71  LEU A N     1 
ATOM   571   C  CA    . LEU A 1 71  ? 113.295 165.235 100.628 1.00 43.61 ?  71  LEU A CA    1 
ATOM   572   C  C     . LEU A 1 71  ? 112.922 165.296 99.153  1.00 44.26 ?  71  LEU A C     1 
ATOM   573   O  O     . LEU A 1 71  ? 113.467 166.136 98.429  1.00 44.16 ?  71  LEU A O     1 
ATOM   574   C  CB    . LEU A 1 71  ? 114.714 164.683 100.772 1.00 45.70 ?  71  LEU A CB    1 
ATOM   575   C  CG    . LEU A 1 71  ? 115.218 164.470 102.199 1.00 47.64 ?  71  LEU A CG    1 
ATOM   576   C  CD1   . LEU A 1 71  ? 116.306 163.410 102.227 1.00 47.24 ?  71  LEU A CD1   1 
ATOM   577   C  CD2   . LEU A 1 71  ? 115.722 165.778 102.783 1.00 45.83 ?  71  LEU A CD2   1 
ATOM   578   N  N     . TYR A 1 72  ? 112.017 164.438 98.695  1.00 44.00 ?  72  TYR A N     1 
ATOM   579   C  CA    . TYR A 1 72  ? 111.584 164.414 97.307  1.00 44.48 ?  72  TYR A CA    1 
ATOM   580   C  C     . TYR A 1 72  ? 110.099 164.729 97.222  1.00 46.44 ?  72  TYR A C     1 
ATOM   581   O  O     . TYR A 1 72  ? 109.326 164.413 98.131  1.00 47.83 ?  72  TYR A O     1 
ATOM   582   C  CB    . TYR A 1 72  ? 111.834 163.047 96.651  1.00 43.94 ?  72  TYR A CB    1 
ATOM   583   C  CG    . TYR A 1 72  ? 113.205 162.456 96.884  1.00 41.73 ?  72  TYR A CG    1 
ATOM   584   C  CD1   . TYR A 1 72  ? 113.499 161.779 98.060  1.00 42.19 ?  72  TYR A CD1   1 
ATOM   585   C  CD2   . TYR A 1 72  ? 114.195 162.553 95.918  1.00 40.29 ?  72  TYR A CD2   1 
ATOM   586   C  CE1   . TYR A 1 72  ? 114.746 161.233 98.274  1.00 41.19 ?  72  TYR A CE1   1 
ATOM   587   C  CE2   . TYR A 1 72  ? 115.445 162.007 96.122  1.00 40.28 ?  72  TYR A CE2   1 
ATOM   588   C  CZ    . TYR A 1 72  ? 115.714 161.348 97.302  1.00 40.85 ?  72  TYR A CZ    1 
ATOM   589   O  OH    . TYR A 1 72  ? 116.957 160.804 97.515  1.00 43.51 ?  72  TYR A OH    1 
ATOM   590   N  N     . SER A 1 73  ? 109.708 165.359 96.121  1.00 51.19 ?  73  SER A N     1 
ATOM   591   C  CA    . SER A 1 73  ? 108.298 165.412 95.779  1.00 50.58 ?  73  SER A CA    1 
ATOM   592   C  C     . SER A 1 73  ? 107.829 164.023 95.357  1.00 52.96 ?  73  SER A C     1 
ATOM   593   O  O     . SER A 1 73  ? 108.625 163.167 94.958  1.00 52.97 ?  73  SER A O     1 
ATOM   594   C  CB    . SER A 1 73  ? 108.050 166.425 94.663  1.00 50.80 ?  73  SER A CB    1 
ATOM   595   O  OG    . SER A 1 73  ? 108.421 165.896 93.402  1.00 50.85 ?  73  SER A OG    1 
ATOM   596   N  N     . PHE A 1 74  ? 106.519 163.793 95.462  1.00 55.14 ?  74  PHE A N     1 
ATOM   597   C  CA    . PHE A 1 74  ? 105.991 162.482 95.102  1.00 53.82 ?  74  PHE A CA    1 
ATOM   598   C  C     . PHE A 1 74  ? 106.226 162.166 93.631  1.00 55.08 ?  74  PHE A C     1 
ATOM   599   O  O     . PHE A 1 74  ? 106.377 160.995 93.266  1.00 56.91 ?  74  PHE A O     1 
ATOM   600   C  CB    . PHE A 1 74  ? 104.502 162.390 95.429  1.00 54.87 ?  74  PHE A CB    1 
ATOM   601   C  CG    . PHE A 1 74  ? 103.834 161.181 94.838  1.00 56.02 ?  74  PHE A CG    1 
ATOM   602   C  CD1   . PHE A 1 74  ? 104.100 159.919 95.343  1.00 54.35 ?  74  PHE A CD1   1 
ATOM   603   C  CD2   . PHE A 1 74  ? 102.954 161.300 93.776  1.00 56.03 ?  74  PHE A CD2   1 
ATOM   604   C  CE1   . PHE A 1 74  ? 103.501 158.801 94.803  1.00 56.64 ?  74  PHE A CE1   1 
ATOM   605   C  CE2   . PHE A 1 74  ? 102.348 160.184 93.232  1.00 56.94 ?  74  PHE A CE2   1 
ATOM   606   C  CZ    . PHE A 1 74  ? 102.623 158.933 93.747  1.00 57.05 ?  74  PHE A CZ    1 
ATOM   607   N  N     . GLU A 1 75  ? 106.259 163.190 92.773  1.00 54.57 ?  75  GLU A N     1 
ATOM   608   C  CA    . GLU A 1 75  ? 106.538 162.956 91.359  1.00 55.54 ?  75  GLU A CA    1 
ATOM   609   C  C     . GLU A 1 75  ? 107.941 162.390 91.163  1.00 57.99 ?  75  GLU A C     1 
ATOM   610   O  O     . GLU A 1 75  ? 108.142 161.475 90.358  1.00 58.35 ?  75  GLU A O     1 
ATOM   611   C  CB    . GLU A 1 75  ? 106.361 164.253 90.562  1.00 54.90 ?  75  GLU A CB    1 
ATOM   612   C  CG    . GLU A 1 75  ? 104.991 164.989 90.660  1.00 55.52 ?  75  GLU A CG    1 
ATOM   613   C  CD    . GLU A 1 75  ? 103.730 164.109 90.577  1.00 58.83 ?  75  GLU A CD    1 
ATOM   614   O  OE1   . GLU A 1 75  ? 103.801 162.866 90.575  1.00 59.31 ?  75  GLU A OE1   1 
ATOM   615   O  OE2   . GLU A 1 75  ? 102.624 164.692 90.519  1.00 57.49 -1 75  GLU A OE2   1 
ATOM   616   N  N     . ASP A 1 76  ? 108.920 162.913 91.903  1.00 52.85 ?  76  ASP A N     1 
ATOM   617   C  CA    . ASP A 1 76  ? 110.285 162.406 91.796  1.00 49.88 ?  76  ASP A CA    1 
ATOM   618   C  C     . ASP A 1 76  ? 110.391 160.969 92.298  1.00 49.23 ?  76  ASP A C     1 
ATOM   619   O  O     . ASP A 1 76  ? 111.080 160.144 91.689  1.00 53.95 ?  76  ASP A O     1 
ATOM   620   C  CB    . ASP A 1 76  ? 111.239 163.321 92.561  1.00 52.85 ?  76  ASP A CB    1 
ATOM   621   C  CG    . ASP A 1 76  ? 111.398 164.675 91.899  1.00 55.11 ?  76  ASP A CG    1 
ATOM   622   O  OD1   . ASP A 1 76  ? 110.700 164.935 90.897  1.00 54.60 ?  76  ASP A OD1   1 
ATOM   623   O  OD2   . ASP A 1 76  ? 112.228 165.477 92.375  1.00 53.49 -1 76  ASP A OD2   1 
ATOM   624   N  N     . ILE A 1 77  ? 109.717 160.652 93.408  1.00 44.02 ?  77  ILE A N     1 
ATOM   625   C  CA    . ILE A 1 77  ? 109.732 159.283 93.921  1.00 45.79 ?  77  ILE A CA    1 
ATOM   626   C  C     . ILE A 1 77  ? 109.076 158.334 92.928  1.00 44.53 ?  77  ILE A C     1 
ATOM   627   O  O     . ILE A 1 77  ? 109.564 157.220 92.689  1.00 47.23 ?  77  ILE A O     1 
ATOM   628   C  CB    . ILE A 1 77  ? 109.045 159.223 95.299  1.00 46.81 ?  77  ILE A CB    1 
ATOM   629   C  CG1   . ILE A 1 77  ? 109.792 160.103 96.300  1.00 46.87 ?  77  ILE A CG1   1 
ATOM   630   C  CG2   . ILE A 1 77  ? 108.979 157.791 95.802  1.00 44.75 ?  77  ILE A CG2   1 
ATOM   631   C  CD1   . ILE A 1 77  ? 109.071 160.282 97.613  1.00 45.19 ?  77  ILE A CD1   1 
ATOM   632   N  N     . LYS A 1 78  ? 107.955 158.755 92.338  1.00 48.26 ?  78  LYS A N     1 
ATOM   633   C  CA    . LYS A 1 78  ? 107.289 157.934 91.334  1.00 49.51 ?  78  LYS A CA    1 
ATOM   634   C  C     . LYS A 1 78  ? 108.176 157.734 90.113  1.00 49.50 ?  78  LYS A C     1 
ATOM   635   O  O     . LYS A 1 78  ? 108.206 156.644 89.534  1.00 51.38 ?  78  LYS A O     1 
ATOM   636   C  CB    . LYS A 1 78  ? 105.956 158.570 90.938  1.00 51.36 ?  78  LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 78  ? 105.114 157.730 89.995  1.00 50.07 ?  78  LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 78  ? 103.763 158.377 89.752  1.00 51.85 ?  78  LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 78  ? 103.063 157.753 88.561  1.00 53.23 ?  78  LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 78  ? 101.979 158.634 88.048  1.00 50.53 1  78  LYS A NZ    1 
ATOM   641   N  N     . GLU A 1 79  ? 108.905 158.776 89.704  1.00 50.11 ?  79  GLU A N     1 
ATOM   642   C  CA    . GLU A 1 79  ? 109.824 158.641 88.579  1.00 50.50 ?  79  GLU A CA    1 
ATOM   643   C  C     . GLU A 1 79  ? 110.955 157.672 88.898  1.00 48.79 ?  79  GLU A C     1 
ATOM   644   O  O     . GLU A 1 79  ? 111.370 156.888 88.038  1.00 48.81 ?  79  GLU A O     1 
ATOM   645   C  CB    . GLU A 1 79  ? 110.381 160.010 88.183  1.00 50.57 ?  79  GLU A CB    1 
ATOM   646   C  CG    . GLU A 1 79  ? 109.837 160.622 86.874  1.00 51.59 ?  79  GLU A CG    1 
ATOM   647   C  CD    . GLU A 1 79  ? 110.058 159.779 85.610  1.00 55.08 ?  79  GLU A CD    1 
ATOM   648   O  OE1   . GLU A 1 79  ? 110.047 160.377 84.513  1.00 55.04 ?  79  GLU A OE1   1 
ATOM   649   O  OE2   . GLU A 1 79  ? 110.248 158.548 85.681  1.00 54.19 -1 79  GLU A OE2   1 
ATOM   650   N  N     . VAL A 1 80  ? 111.470 157.714 90.128  1.00 44.57 ?  80  VAL A N     1 
ATOM   651   C  CA    . VAL A 1 80  ? 112.518 156.776 90.523  1.00 41.51 ?  80  VAL A CA    1 
ATOM   652   C  C     . VAL A 1 80  ? 111.992 155.343 90.509  1.00 45.35 ?  80  VAL A C     1 
ATOM   653   O  O     . VAL A 1 80  ? 112.660 154.422 90.016  1.00 46.84 ?  80  VAL A O     1 
ATOM   654   C  CB    . VAL A 1 80  ? 113.081 157.167 91.899  1.00 40.87 ?  80  VAL A CB    1 
ATOM   655   C  CG1   . VAL A 1 80  ? 113.991 156.078 92.433  1.00 41.66 ?  80  VAL A CG1   1 
ATOM   656   C  CG2   . VAL A 1 80  ? 113.831 158.483 91.801  1.00 40.91 ?  80  VAL A CG2   1 
ATOM   657   N  N     . PHE A 1 81  ? 110.786 155.131 91.041  1.00 41.17 ?  81  PHE A N     1 
ATOM   658   C  CA    . PHE A 1 81  ? 110.192 153.795 91.021  1.00 39.00 ?  81  PHE A CA    1 
ATOM   659   C  C     . PHE A 1 81  ? 109.942 153.322 89.593  1.00 43.72 ?  81  PHE A C     1 
ATOM   660   O  O     . PHE A 1 81  ? 110.140 152.143 89.275  1.00 47.44 ?  81  PHE A O     1 
ATOM   661   C  CB    . PHE A 1 81  ? 108.892 153.786 91.824  1.00 40.74 ?  81  PHE A CB    1 
ATOM   662   C  CG    . PHE A 1 81  ? 109.077 153.466 93.281  1.00 39.06 ?  81  PHE A CG    1 
ATOM   663   C  CD1   . PHE A 1 81  ? 109.452 154.451 94.179  1.00 40.39 ?  81  PHE A CD1   1 
ATOM   664   C  CD2   . PHE A 1 81  ? 108.875 152.181 93.752  1.00 38.70 ?  81  PHE A CD2   1 
ATOM   665   C  CE1   . PHE A 1 81  ? 109.621 154.161 95.518  1.00 41.25 ?  81  PHE A CE1   1 
ATOM   666   C  CE2   . PHE A 1 81  ? 109.043 151.885 95.092  1.00 39.22 ?  81  PHE A CE2   1 
ATOM   667   C  CZ    . PHE A 1 81  ? 109.416 152.877 95.975  1.00 39.43 ?  81  PHE A CZ    1 
ATOM   668   N  N     . LYS A 1 82  ? 109.496 154.227 88.720  1.00 45.50 ?  82  LYS A N     1 
ATOM   669   C  CA    . LYS A 1 82  ? 109.276 153.875 87.322  1.00 44.86 ?  82  LYS A CA    1 
ATOM   670   C  C     . LYS A 1 82  ? 110.586 153.518 86.633  1.00 44.10 ?  82  LYS A C     1 
ATOM   671   O  O     . LYS A 1 82  ? 110.628 152.600 85.810  1.00 46.58 ?  82  LYS A O     1 
ATOM   672   C  CB    . LYS A 1 82  ? 108.582 155.026 86.596  1.00 46.41 ?  82  LYS A CB    1 
ATOM   673   C  CG    . LYS A 1 82  ? 107.082 155.081 86.817  1.00 47.69 ?  82  LYS A CG    1 
ATOM   674   C  CD    . LYS A 1 82  ? 106.420 156.057 85.860  1.00 49.23 ?  82  LYS A CD    1 
ATOM   675   C  CE    . LYS A 1 82  ? 105.029 155.587 85.474  1.00 48.47 ?  82  LYS A CE    1 
ATOM   676   N  NZ    . LYS A 1 82  ? 104.936 154.101 85.457  1.00 48.61 1  82  LYS A NZ    1 
ATOM   677   N  N     . THR A 1 83  ? 111.662 154.240 86.948  1.00 41.81 ?  83  THR A N     1 
ATOM   678   C  CA    . THR A 1 83  ? 112.971 153.892 86.405  1.00 42.61 ?  83  THR A CA    1 
ATOM   679   C  C     . THR A 1 83  ? 113.409 152.515 86.883  1.00 44.80 ?  83  THR A C     1 
ATOM   680   O  O     . THR A 1 83  ? 113.994 151.739 86.117  1.00 47.02 ?  83  THR A O     1 
ATOM   681   C  CB    . THR A 1 83  ? 114.003 154.950 86.798  1.00 42.16 ?  83  THR A CB    1 
ATOM   682   O  OG1   . THR A 1 83  ? 113.542 156.244 86.389  1.00 47.88 ?  83  THR A OG1   1 
ATOM   683   C  CG2   . THR A 1 83  ? 115.339 154.668 86.131  1.00 43.17 ?  83  THR A CG2   1 
ATOM   684   N  N     . ALA A 1 84  ? 113.139 152.196 88.150  1.00 38.43 ?  84  ALA A N     1 
ATOM   685   C  CA    . ALA A 1 84  ? 113.470 150.868 88.661  1.00 35.86 ?  84  ALA A CA    1 
ATOM   686   C  C     . ALA A 1 84  ? 112.678 149.781 87.947  1.00 39.07 ?  84  ALA A C     1 
ATOM   687   O  O     . ALA A 1 84  ? 113.227 148.731 87.596  1.00 42.31 ?  84  ALA A O     1 
ATOM   688   C  CB    . ALA A 1 84  ? 113.223 150.808 90.166  1.00 36.56 ?  84  ALA A CB    1 
ATOM   689   N  N     . TYR A 1 85  ? 111.385 150.012 87.724  1.00 44.03 ?  85  TYR A N     1 
ATOM   690   C  CA    . TYR A 1 85  ? 110.534 149.004 87.105  1.00 39.83 ?  85  TYR A CA    1 
ATOM   691   C  C     . TYR A 1 85  ? 110.675 148.936 85.590  1.00 40.48 ?  85  TYR A C     1 
ATOM   692   O  O     . TYR A 1 85  ? 110.242 147.945 84.991  1.00 41.84 ?  85  TYR A O     1 
ATOM   693   C  CB    . TYR A 1 85  ? 109.069 149.259 87.469  1.00 41.64 ?  85  TYR A CB    1 
ATOM   694   C  CG    . TYR A 1 85  ? 108.664 148.704 88.814  1.00 41.09 ?  85  TYR A CG    1 
ATOM   695   C  CD1   . TYR A 1 85  ? 108.183 147.408 88.934  1.00 39.31 ?  85  TYR A CD1   1 
ATOM   696   C  CD2   . TYR A 1 85  ? 108.762 149.474 89.965  1.00 42.16 ?  85  TYR A CD2   1 
ATOM   697   C  CE1   . TYR A 1 85  ? 107.811 146.894 90.158  1.00 41.12 ?  85  TYR A CE1   1 
ATOM   698   C  CE2   . TYR A 1 85  ? 108.391 148.969 91.196  1.00 42.11 ?  85  TYR A CE2   1 
ATOM   699   C  CZ    . TYR A 1 85  ? 107.916 147.679 91.286  1.00 43.05 ?  85  TYR A CZ    1 
ATOM   700   O  OH    . TYR A 1 85  ? 107.546 147.169 92.508  1.00 43.05 ?  85  TYR A OH    1 
ATOM   701   N  N     . ALA A 1 86  ? 111.265 149.952 84.955  1.00 40.35 ?  86  ALA A N     1 
ATOM   702   C  CA    . ALA A 1 86  ? 111.426 149.934 83.508  1.00 40.94 ?  86  ALA A CA    1 
ATOM   703   C  C     . ALA A 1 86  ? 112.447 148.905 83.049  1.00 45.40 ?  86  ALA A C     1 
ATOM   704   O  O     . ALA A 1 86  ? 112.397 148.473 81.893  1.00 45.64 ?  86  ALA A O     1 
ATOM   705   C  CB    . ALA A 1 86  ? 111.828 151.321 83.006  1.00 39.65 ?  86  ALA A CB    1 
ATOM   706   N  N     . LYS A 1 87  ? 113.372 148.508 83.924  1.00 43.91 ?  87  LYS A N     1 
ATOM   707   C  CA    . LYS A 1 87  ? 114.343 147.483 83.560  1.00 41.44 ?  87  LYS A CA    1 
ATOM   708   C  C     . LYS A 1 87  ? 113.672 146.134 83.330  1.00 42.51 ?  87  LYS A C     1 
ATOM   709   O  O     . LYS A 1 87  ? 114.174 145.320 82.545  1.00 44.65 ?  87  LYS A O     1 
ATOM   710   C  CB    . LYS A 1 87  ? 115.417 147.376 84.646  1.00 41.57 ?  87  LYS A CB    1 
ATOM   711   C  CG    . LYS A 1 87  ? 116.348 146.182 84.508  1.00 43.60 ?  87  LYS A CG    1 
ATOM   712   C  CD    . LYS A 1 87  ? 117.767 146.616 84.199  1.00 40.15 ?  87  LYS A CD    1 
ATOM   713   C  CE    . LYS A 1 87  ? 118.688 145.418 84.045  1.00 40.86 ?  87  LYS A CE    1 
ATOM   714   N  NZ    . LYS A 1 87  ? 119.570 145.548 82.853  1.00 42.63 1  87  LYS A NZ    1 
ATOM   715   N  N     . LYS A 1 88  ? 112.526 145.900 83.973  1.00 43.17 ?  88  LYS A N     1 
ATOM   716   C  CA    . LYS A 1 88  ? 111.854 144.600 83.948  1.00 41.87 ?  88  LYS A CA    1 
ATOM   717   C  C     . LYS A 1 88  ? 112.803 143.504 84.425  1.00 40.24 ?  88  LYS A C     1 
ATOM   718   O  O     . LYS A 1 88  ? 112.936 142.445 83.806  1.00 43.96 ?  88  LYS A O     1 
ATOM   719   C  CB    . LYS A 1 88  ? 111.297 144.286 82.557  1.00 43.41 ?  88  LYS A CB    1 
ATOM   720   C  CG    . LYS A 1 88  ? 109.875 144.774 82.328  1.00 44.06 ?  88  LYS A CG    1 
ATOM   721   C  CD    . LYS A 1 88  ? 109.857 146.071 81.534  1.00 44.79 ?  88  LYS A CD    1 
ATOM   722   C  CE    . LYS A 1 88  ? 108.746 146.995 82.006  1.00 45.47 ?  88  LYS A CE    1 
ATOM   723   N  NZ    . LYS A 1 88  ? 108.818 148.333 81.353  1.00 43.81 1  88  LYS A NZ    1 
ATOM   724   N  N     . PHE A 1 89  ? 113.481 143.779 85.538  1.00 39.10 ?  89  PHE A N     1 
ATOM   725   C  CA    . PHE A 1 89  ? 114.471 142.853 86.067  1.00 33.63 ?  89  PHE A CA    1 
ATOM   726   C  C     . PHE A 1 89  ? 113.827 141.524 86.431  1.00 40.27 ?  89  PHE A C     1 
ATOM   727   O  O     . PHE A 1 89  ? 112.756 141.477 87.044  1.00 42.10 ?  89  PHE A O     1 
ATOM   728   C  CB    . PHE A 1 89  ? 115.159 143.454 87.294  1.00 34.46 ?  89  PHE A CB    1 
ATOM   729   C  CG    . PHE A 1 89  ? 116.097 142.508 87.985  1.00 34.23 ?  89  PHE A CG    1 
ATOM   730   C  CD1   . PHE A 1 89  ? 117.391 142.340 87.526  1.00 34.64 ?  89  PHE A CD1   1 
ATOM   731   C  CD2   . PHE A 1 89  ? 115.685 141.782 89.090  1.00 35.69 ?  89  PHE A CD2   1 
ATOM   732   C  CE1   . PHE A 1 89  ? 118.255 141.467 88.155  1.00 37.08 ?  89  PHE A CE1   1 
ATOM   733   C  CE2   . PHE A 1 89  ? 116.545 140.906 89.720  1.00 32.64 ?  89  PHE A CE2   1 
ATOM   734   C  CZ    . PHE A 1 89  ? 117.831 140.750 89.254  1.00 35.02 ?  89  PHE A CZ    1 
ATOM   735   N  N     . ARG A 1 90  ? 114.490 140.437 86.048  1.00 41.70 ?  90  ARG A N     1 
ATOM   736   C  CA    . ARG A 1 90  ? 114.050 139.090 86.372  1.00 40.07 ?  90  ARG A CA    1 
ATOM   737   C  C     . ARG A 1 90  ? 115.193 138.350 87.044  1.00 39.11 ?  90  ARG A C     1 
ATOM   738   O  O     . ARG A 1 90  ? 116.324 138.367 86.547  1.00 40.65 ?  90  ARG A O     1 
ATOM   739   C  CB    . ARG A 1 90  ? 113.593 138.336 85.117  1.00 39.99 ?  90  ARG A CB    1 
ATOM   740   C  CG    . ARG A 1 90  ? 112.520 139.048 84.316  1.00 41.43 ?  90  ARG A CG    1 
ATOM   741   C  CD    . ARG A 1 90  ? 111.187 139.045 85.046  1.00 42.63 ?  90  ARG A CD    1 
ATOM   742   N  NE    . ARG A 1 90  ? 110.233 139.963 84.437  1.00 44.13 ?  90  ARG A NE    1 
ATOM   743   C  CZ    . ARG A 1 90  ? 109.684 140.997 85.062  1.00 45.93 ?  90  ARG A CZ    1 
ATOM   744   N  NH1   . ARG A 1 90  ? 109.966 141.268 86.325  1.00 45.56 1  90  ARG A NH1   1 
ATOM   745   N  NH2   . ARG A 1 90  ? 108.832 141.775 84.403  1.00 43.70 ?  90  ARG A NH2   1 
ATOM   746   N  N     . PHE A 1 91  ? 114.902 137.716 88.171  1.00 36.18 ?  91  PHE A N     1 
ATOM   747   C  CA    . PHE A 1 91  ? 115.901 136.891 88.832  1.00 37.86 ?  91  PHE A CA    1 
ATOM   748   C  C     . PHE A 1 91  ? 116.223 135.688 87.953  1.00 43.33 ?  91  PHE A C     1 
ATOM   749   O  O     . PHE A 1 91  ? 115.311 134.956 87.555  1.00 44.55 ?  91  PHE A O     1 
ATOM   750   C  CB    . PHE A 1 91  ? 115.400 136.435 90.199  1.00 35.06 ?  91  PHE A CB    1 
ATOM   751   C  CG    . PHE A 1 91  ? 115.320 137.538 91.215  1.00 39.65 ?  91  PHE A CG    1 
ATOM   752   C  CD1   . PHE A 1 91  ? 116.442 137.923 91.930  1.00 41.67 ?  91  PHE A CD1   1 
ATOM   753   C  CD2   . PHE A 1 91  ? 114.124 138.193 91.453  1.00 38.52 ?  91  PHE A CD2   1 
ATOM   754   C  CE1   . PHE A 1 91  ? 116.371 138.937 92.865  1.00 39.51 ?  91  PHE A CE1   1 
ATOM   755   C  CE2   . PHE A 1 91  ? 114.048 139.207 92.388  1.00 38.91 ?  91  PHE A CE2   1 
ATOM   756   C  CZ    . PHE A 1 91  ? 115.173 139.580 93.093  1.00 38.48 ?  91  PHE A CZ    1 
ATOM   757   N  N     . PRO A 1 92  ? 117.498 135.450 87.626  1.00 43.39 ?  92  PRO A N     1 
ATOM   758   C  CA    . PRO A 1 92  ? 117.822 134.340 86.720  1.00 42.30 ?  92  PRO A CA    1 
ATOM   759   C  C     . PRO A 1 92  ? 117.771 132.975 87.377  1.00 43.13 ?  92  PRO A C     1 
ATOM   760   O  O     . PRO A 1 92  ? 117.653 131.970 86.664  1.00 44.76 ?  92  PRO A O     1 
ATOM   761   C  CB    . PRO A 1 92  ? 119.244 134.678 86.260  1.00 42.75 ?  92  PRO A CB    1 
ATOM   762   C  CG    . PRO A 1 92  ? 119.834 135.386 87.434  1.00 43.24 ?  92  PRO A CG    1 
ATOM   763   C  CD    . PRO A 1 92  ? 118.707 136.149 88.098  1.00 40.50 ?  92  PRO A CD    1 
ATOM   764   N  N     . SER A 1 93  ? 117.853 132.904 88.703  1.00 42.55 ?  93  SER A N     1 
ATOM   765   C  CA    . SER A 1 93  ? 117.849 131.644 89.425  1.00 41.96 ?  93  SER A CA    1 
ATOM   766   C  C     . SER A 1 93  ? 116.851 131.727 90.571  1.00 44.09 ?  93  SER A C     1 
ATOM   767   O  O     . SER A 1 93  ? 116.541 132.809 91.076  1.00 47.27 ?  93  SER A O     1 
ATOM   768   C  CB    . SER A 1 93  ? 119.244 131.298 89.961  1.00 43.27 ?  93  SER A CB    1 
ATOM   769   O  OG    . SER A 1 93  ? 119.468 131.897 91.224  1.00 45.05 ?  93  SER A OG    1 
ATOM   770   N  N     . PHE A 1 94  ? 116.338 130.560 90.967  1.00 43.75 ?  94  PHE A N     1 
ATOM   771   C  CA    . PHE A 1 94  ? 115.349 130.515 92.038  1.00 40.05 ?  94  PHE A CA    1 
ATOM   772   C  C     . PHE A 1 94  ? 115.937 131.004 93.355  1.00 42.38 ?  94  PHE A C     1 
ATOM   773   O  O     . PHE A 1 94  ? 115.263 131.700 94.122  1.00 44.10 ?  94  PHE A O     1 
ATOM   774   C  CB    . PHE A 1 94  ? 114.799 129.097 92.193  1.00 40.38 ?  94  PHE A CB    1 
ATOM   775   C  CG    . PHE A 1 94  ? 114.238 128.814 93.557  1.00 41.40 ?  94  PHE A CG    1 
ATOM   776   C  CD1   . PHE A 1 94  ? 113.036 129.374 93.955  1.00 41.31 ?  94  PHE A CD1   1 
ATOM   777   C  CD2   . PHE A 1 94  ? 114.914 127.994 94.444  1.00 44.07 ?  94  PHE A CD2   1 
ATOM   778   C  CE1   . PHE A 1 94  ? 112.522 129.123 95.210  1.00 41.35 ?  94  PHE A CE1   1 
ATOM   779   C  CE2   . PHE A 1 94  ? 114.402 127.738 95.700  1.00 45.35 ?  94  PHE A CE2   1 
ATOM   780   C  CZ    . PHE A 1 94  ? 113.204 128.302 96.083  1.00 41.55 ?  94  PHE A CZ    1 
ATOM   781   N  N     . MET A 1 95  ? 117.191 130.643 93.637  1.00 41.51 ?  95  MET A N     1 
ATOM   782   C  CA    . MET A 1 95  ? 117.787 131.000 94.918  1.00 39.30 ?  95  MET A CA    1 
ATOM   783   C  C     . MET A 1 95  ? 117.961 132.504 95.070  1.00 41.31 ?  95  MET A C     1 
ATOM   784   O  O     . MET A 1 95  ? 117.869 133.018 96.187  1.00 42.06 ?  95  MET A O     1 
ATOM   785   C  CB    . MET A 1 95  ? 119.128 130.286 95.095  1.00 40.51 ?  95  MET A CB    1 
ATOM   786   C  CG    . MET A 1 95  ? 119.758 130.426 96.482  1.00 43.89 ?  95  MET A CG    1 
ATOM   787   S  SD    . MET A 1 95  ? 118.877 129.723 97.901  1.00 54.57 ?  95  MET A SD    1 
ATOM   788   C  CE    . MET A 1 95  ? 117.858 128.451 97.158  1.00 45.92 ?  95  MET A CE    1 
ATOM   789   N  N     . SER A 1 96  ? 118.198 133.227 93.974  1.00 38.56 ?  96  SER A N     1 
ATOM   790   C  CA    . SER A 1 96  ? 118.311 134.681 94.063  1.00 34.14 ?  96  SER A CA    1 
ATOM   791   C  C     . SER A 1 96  ? 117.024 135.299 94.597  1.00 38.41 ?  96  SER A C     1 
ATOM   792   O  O     . SER A 1 96  ? 117.035 136.045 95.588  1.00 40.40 ?  96  SER A O     1 
ATOM   793   C  CB    . SER A 1 96  ? 118.651 135.256 92.689  1.00 32.01 ?  96  SER A CB    1 
ATOM   794   O  OG    . SER A 1 96  ? 119.642 134.480 92.042  1.00 36.90 ?  96  SER A OG    1 
ATOM   795   N  N     . ALA A 1 97  ? 115.897 134.974 93.962  1.00 38.59 ?  97  ALA A N     1 
ATOM   796   C  CA    . ALA A 1 97  ? 114.613 135.509 94.395  1.00 34.80 ?  97  ALA A CA    1 
ATOM   797   C  C     . ALA A 1 97  ? 114.243 135.001 95.780  1.00 35.83 ?  97  ALA A C     1 
ATOM   798   O  O     . ALA A 1 97  ? 113.697 135.752 96.596  1.00 41.87 ?  97  ALA A O     1 
ATOM   799   C  CB    . ALA A 1 97  ? 113.528 135.147 93.384  1.00 36.02 ?  97  ALA A CB    1 
ATOM   800   N  N     . PHE A 1 98  ? 114.523 133.727 96.061  1.00 37.46 ?  98  PHE A N     1 
ATOM   801   C  CA    . PHE A 1 98  ? 114.204 133.178 97.373  1.00 37.31 ?  98  PHE A CA    1 
ATOM   802   C  C     . PHE A 1 98  ? 114.974 133.900 98.471  1.00 37.48 ?  98  PHE A C     1 
ATOM   803   O  O     . PHE A 1 98  ? 114.398 134.277 99.496  1.00 46.19 ?  98  PHE A O     1 
ATOM   804   C  CB    . PHE A 1 98  ? 114.503 131.680 97.405  1.00 41.86 ?  98  PHE A CB    1 
ATOM   805   C  CG    . PHE A 1 98  ? 114.248 131.043 98.739  1.00 42.40 ?  98  PHE A CG    1 
ATOM   806   C  CD1   . PHE A 1 98  ? 112.961 130.707 99.123  1.00 42.56 ?  98  PHE A CD1   1 
ATOM   807   C  CD2   . PHE A 1 98  ? 115.292 130.787 99.613  1.00 41.56 ?  98  PHE A CD2   1 
ATOM   808   C  CE1   . PHE A 1 98  ? 112.722 130.124 100.351 1.00 43.31 ?  98  PHE A CE1   1 
ATOM   809   C  CE2   . PHE A 1 98  ? 115.057 130.205 100.842 1.00 42.84 ?  98  PHE A CE2   1 
ATOM   810   C  CZ    . PHE A 1 98  ? 113.770 129.873 101.212 1.00 44.36 ?  98  PHE A CZ    1 
ATOM   811   N  N     . LYS A 1 99  ? 116.274 134.117 98.264  1.00 38.45 ?  99  LYS A N     1 
ATOM   812   C  CA    . LYS A 1 99  ? 117.085 134.804 99.260  1.00 36.82 ?  99  LYS A CA    1 
ATOM   813   C  C     . LYS A 1 99  ? 116.638 136.247 99.434  1.00 38.12 ?  99  LYS A C     1 
ATOM   814   O  O     . LYS A 1 99  ? 116.586 136.749 100.563 1.00 43.28 ?  99  LYS A O     1 
ATOM   815   C  CB    . LYS A 1 99  ? 118.561 134.740 98.869  1.00 37.70 ?  99  LYS A CB    1 
ATOM   816   C  CG    . LYS A 1 99  ? 119.218 133.402 99.159  1.00 39.76 ?  99  LYS A CG    1 
ATOM   817   C  CD    . LYS A 1 99  ? 118.918 132.924 100.567 1.00 41.23 ?  99  LYS A CD    1 
ATOM   818   C  CE    . LYS A 1 99  ? 120.171 132.411 101.253 1.00 39.84 ?  99  LYS A CE    1 
ATOM   819   N  NZ    . LYS A 1 99  ? 119.986 132.307 102.726 1.00 43.67 1  99  LYS A NZ    1 
ATOM   820   N  N     . PHE A 1 100 ? 116.302 136.933 98.338  1.00 33.98 ?  100 PHE A N     1 
ATOM   821   C  CA    . PHE A 1 100 ? 115.843 138.310 98.486  1.00 32.03 ?  100 PHE A CA    1 
ATOM   822   C  C     . PHE A 1 100 ? 114.527 138.378 99.250  1.00 35.49 ?  100 PHE A C     1 
ATOM   823   O  O     . PHE A 1 100 ? 114.387 139.160 100.198 1.00 40.64 ?  100 PHE A O     1 
ATOM   824   C  CB    . PHE A 1 100 ? 115.689 138.996 97.132  1.00 29.77 ?  100 PHE A CB    1 
ATOM   825   C  CG    . PHE A 1 100 ? 115.052 140.349 97.237  1.00 36.38 ?  100 PHE A CG    1 
ATOM   826   C  CD1   . PHE A 1 100 ? 115.765 141.421 97.748  1.00 36.19 ?  100 PHE A CD1   1 
ATOM   827   C  CD2   . PHE A 1 100 ? 113.731 140.541 96.879  1.00 35.11 ?  100 PHE A CD2   1 
ATOM   828   C  CE1   . PHE A 1 100 ? 115.181 142.663 97.872  1.00 35.16 ?  100 PHE A CE1   1 
ATOM   829   C  CE2   . PHE A 1 100 ? 113.140 141.781 97.004  1.00 35.41 ?  100 PHE A CE2   1 
ATOM   830   C  CZ    . PHE A 1 100 ? 113.867 142.844 97.501  1.00 35.14 ?  100 PHE A CZ    1 
ATOM   831   N  N     . TYR A 1 101 ? 113.545 137.568 98.855  1.00 38.04 ?  101 TYR A N     1 
ATOM   832   C  CA    . TYR A 1 101 ? 112.220 137.654 99.451  1.00 37.60 ?  101 TYR A CA    1 
ATOM   833   C  C     . TYR A 1 101 ? 112.128 136.961 100.803 1.00 38.38 ?  101 TYR A C     1 
ATOM   834   O  O     . TYR A 1 101 ? 111.100 137.087 101.475 1.00 44.60 ?  101 TYR A O     1 
ATOM   835   C  CB    . TYR A 1 101 ? 111.177 137.082 98.490  1.00 36.13 ?  101 TYR A CB    1 
ATOM   836   C  CG    . TYR A 1 101 ? 110.871 138.009 97.336  1.00 32.59 ?  101 TYR A CG    1 
ATOM   837   C  CD1   . TYR A 1 101 ? 110.091 139.143 97.519  1.00 36.94 ?  101 TYR A CD1   1 
ATOM   838   C  CD2   . TYR A 1 101 ? 111.375 137.761 96.067  1.00 34.18 ?  101 TYR A CD2   1 
ATOM   839   C  CE1   . TYR A 1 101 ? 109.817 139.997 96.472  1.00 38.04 ?  101 TYR A CE1   1 
ATOM   840   C  CE2   . TYR A 1 101 ? 111.106 138.609 95.014  1.00 36.49 ?  101 TYR A CE2   1 
ATOM   841   C  CZ    . TYR A 1 101 ? 110.326 139.726 95.221  1.00 38.47 ?  101 TYR A CZ    1 
ATOM   842   O  OH    . TYR A 1 101 ? 110.055 140.574 94.173  1.00 41.93 ?  101 TYR A OH    1 
ATOM   843   N  N     . ASN A 1 102 ? 113.168 136.237 101.218 1.00 41.74 ?  102 ASN A N     1 
ATOM   844   C  CA    . ASN A 1 102 ? 113.218 135.665 102.553 1.00 45.03 ?  102 ASN A CA    1 
ATOM   845   C  C     . ASN A 1 102 ? 114.109 136.446 103.507 1.00 45.97 ?  102 ASN A C     1 
ATOM   846   O  O     . ASN A 1 102 ? 113.928 136.337 104.725 1.00 48.30 ?  102 ASN A O     1 
ATOM   847   C  CB    . ASN A 1 102 ? 113.709 134.213 102.489 1.00 42.99 ?  102 ASN A CB    1 
ATOM   848   C  CG    . ASN A 1 102 ? 112.576 133.209 102.538 1.00 46.78 ?  102 ASN A CG    1 
ATOM   849   O  OD1   . ASN A 1 102 ? 111.753 133.138 101.626 1.00 48.92 ?  102 ASN A OD1   1 
ATOM   850   N  ND2   . ASN A 1 102 ? 112.529 132.424 103.607 1.00 44.50 ?  102 ASN A ND2   1 
ATOM   851   N  N     . ASP A 1 103 ? 115.059 137.226 102.991 1.00 41.29 ?  103 ASP A N     1 
ATOM   852   C  CA    . ASP A 1 103 ? 116.008 137.942 103.831 1.00 41.46 ?  103 ASP A CA    1 
ATOM   853   C  C     . ASP A 1 103 ? 115.906 139.454 103.736 1.00 40.82 ?  103 ASP A C     1 
ATOM   854   O  O     . ASP A 1 103 ? 116.095 140.131 104.748 1.00 45.01 ?  103 ASP A O     1 
ATOM   855   C  CB    . ASP A 1 103 ? 117.443 137.529 103.481 1.00 44.47 ?  103 ASP A CB    1 
ATOM   856   C  CG    . ASP A 1 103 ? 117.748 136.097 103.865 1.00 48.51 ?  103 ASP A CG    1 
ATOM   857   O  OD1   . ASP A 1 103 ? 116.892 135.457 104.509 1.00 47.69 ?  103 ASP A OD1   1 
ATOM   858   O  OD2   . ASP A 1 103 ? 118.844 135.610 103.519 1.00 50.67 -1 103 ASP A OD2   1 
ATOM   859   N  N     . TYR A 1 104 ? 115.613 140.005 102.561 1.00 34.75 ?  104 TYR A N     1 
ATOM   860   C  CA    . TYR A 1 104 ? 115.706 141.442 102.347 1.00 38.48 ?  104 TYR A CA    1 
ATOM   861   C  C     . TYR A 1 104 ? 114.384 142.120 102.025 1.00 39.62 ?  104 TYR A C     1 
ATOM   862   O  O     . TYR A 1 104 ? 114.229 143.300 102.340 1.00 43.43 ?  104 TYR A O     1 
ATOM   863   C  CB    . TYR A 1 104 ? 116.706 141.746 101.220 1.00 38.18 ?  104 TYR A CB    1 
ATOM   864   C  CG    . TYR A 1 104 ? 118.093 141.216 101.498 1.00 40.21 ?  104 TYR A CG    1 
ATOM   865   C  CD1   . TYR A 1 104 ? 118.997 141.945 102.258 1.00 37.87 ?  104 TYR A CD1   1 
ATOM   866   C  CD2   . TYR A 1 104 ? 118.494 139.980 101.010 1.00 35.30 ?  104 TYR A CD2   1 
ATOM   867   C  CE1   . TYR A 1 104 ? 120.262 141.462 102.519 1.00 36.61 ?  104 TYR A CE1   1 
ATOM   868   C  CE2   . TYR A 1 104 ? 119.756 139.488 101.267 1.00 35.79 ?  104 TYR A CE2   1 
ATOM   869   C  CZ    . TYR A 1 104 ? 120.636 140.233 102.022 1.00 39.06 ?  104 TYR A CZ    1 
ATOM   870   O  OH    . TYR A 1 104 ? 121.896 139.746 102.279 1.00 40.64 ?  104 TYR A OH    1 
ATOM   871   N  N     . ALA A 1 105 ? 113.436 141.421 101.406 1.00 40.76 ?  105 ALA A N     1 
ATOM   872   C  CA    . ALA A 1 105 ? 112.159 142.039 101.080 1.00 38.14 ?  105 ALA A CA    1 
ATOM   873   C  C     . ALA A 1 105 ? 111.399 142.395 102.352 1.00 42.98 ?  105 ALA A C     1 
ATOM   874   O  O     . ALA A 1 105 ? 111.330 141.604 103.297 1.00 44.65 ?  105 ALA A O     1 
ATOM   875   C  CB    . ALA A 1 105 ? 111.320 141.108 100.208 1.00 37.75 ?  105 ALA A CB    1 
ATOM   876   N  N     . LEU A 1 106 ? 110.832 143.597 102.374 1.00 44.74 ?  106 LEU A N     1 
ATOM   877   C  CA    . LEU A 1 106 ? 110.083 144.049 103.538 1.00 40.94 ?  106 LEU A CA    1 
ATOM   878   C  C     . LEU A 1 106 ? 108.780 143.271 103.661 1.00 45.24 ?  106 LEU A C     1 
ATOM   879   O  O     . LEU A 1 106 ? 108.018 143.155 102.697 1.00 46.46 ?  106 LEU A O     1 
ATOM   880   C  CB    . LEU A 1 106 ? 109.800 145.546 103.440 1.00 44.43 ?  106 LEU A CB    1 
ATOM   881   C  CG    . LEU A 1 106 ? 109.053 146.173 104.619 1.00 43.46 ?  106 LEU A CG    1 
ATOM   882   C  CD1   . LEU A 1 106 ? 109.898 146.125 105.880 1.00 42.46 ?  106 LEU A CD1   1 
ATOM   883   C  CD2   . LEU A 1 106 ? 108.648 147.600 104.294 1.00 43.80 ?  106 LEU A CD2   1 
ATOM   884   N  N     . LYS A 1 107 ? 108.526 142.742 104.852 1.00 50.99 ?  107 LYS A N     1 
ATOM   885   C  CA    . LYS A 1 107 ? 107.324 141.978 105.138 1.00 50.88 ?  107 LYS A CA    1 
ATOM   886   C  C     . LYS A 1 107 ? 106.515 142.679 106.220 1.00 54.09 ?  107 LYS A C     1 
ATOM   887   O  O     . LYS A 1 107 ? 107.029 143.514 106.969 1.00 54.52 ?  107 LYS A O     1 
ATOM   888   C  CB    . LYS A 1 107 ? 107.663 140.548 105.579 1.00 51.63 ?  107 LYS A CB    1 
ATOM   889   C  CG    . LYS A 1 107 ? 108.809 139.914 104.810 1.00 50.31 ?  107 LYS A CG    1 
ATOM   890   C  CD    . LYS A 1 107 ? 108.302 138.918 103.783 1.00 50.99 ?  107 LYS A CD    1 
ATOM   891   C  CE    . LYS A 1 107 ? 109.019 137.583 103.908 1.00 54.46 ?  107 LYS A CE    1 
ATOM   892   N  NZ    . LYS A 1 107 ? 108.755 136.697 102.741 1.00 51.38 1  107 LYS A NZ    1 
ATOM   893   N  N     . THR A 1 108 ? 105.233 142.331 106.289 1.00 58.40 ?  108 THR A N     1 
ATOM   894   C  CA    . THR A 1 108 ? 104.357 142.883 107.308 1.00 57.21 ?  108 THR A CA    1 
ATOM   895   C  C     . THR A 1 108 ? 104.809 142.435 108.699 1.00 59.00 ?  108 THR A C     1 
ATOM   896   O  O     . THR A 1 108 ? 105.672 141.568 108.855 1.00 59.19 ?  108 THR A O     1 
ATOM   897   C  CB    . THR A 1 108 ? 102.912 142.459 107.057 1.00 57.88 ?  108 THR A CB    1 
ATOM   898   O  OG1   . THR A 1 108 ? 102.835 141.029 107.010 1.00 63.02 ?  108 THR A OG1   1 
ATOM   899   C  CG2   . THR A 1 108 ? 102.413 143.029 105.739 1.00 57.15 ?  108 THR A CG2   1 
ATOM   900   N  N     . ASN A 1 109 ? 104.210 143.047 109.723 1.00 60.83 ?  109 ASN A N     1 
ATOM   901   C  CA    . ASN A 1 109 ? 104.556 142.694 111.097 1.00 62.67 ?  109 ASN A CA    1 
ATOM   902   C  C     . ASN A 1 109 ? 104.244 141.235 111.399 1.00 64.04 ?  109 ASN A C     1 
ATOM   903   O  O     . ASN A 1 109 ? 104.907 140.618 112.240 1.00 64.25 ?  109 ASN A O     1 
ATOM   904   C  CB    . ASN A 1 109 ? 103.819 143.606 112.079 1.00 62.17 ?  109 ASN A CB    1 
ATOM   905   C  CG    . ASN A 1 109 ? 104.148 145.070 111.873 1.00 61.16 ?  109 ASN A CG    1 
ATOM   906   O  OD1   . ASN A 1 109 ? 104.337 145.523 110.746 1.00 60.42 ?  109 ASN A OD1   1 
ATOM   907   N  ND2   . ASN A 1 109 ? 104.221 145.819 112.967 1.00 61.63 ?  109 ASN A ND2   1 
ATOM   908   N  N     . ASP A 1 110 ? 103.245 140.669 110.727 1.00 65.81 ?  110 ASP A N     1 
ATOM   909   C  CA    . ASP A 1 110 ? 102.882 139.268 110.883 1.00 64.93 ?  110 ASP A CA    1 
ATOM   910   C  C     . ASP A 1 110 ? 103.703 138.337 110.000 1.00 67.09 ?  110 ASP A C     1 
ATOM   911   O  O     . ASP A 1 110 ? 103.532 137.116 110.088 1.00 67.07 ?  110 ASP A O     1 
ATOM   912   C  CB    . ASP A 1 110 ? 101.388 139.090 110.599 1.00 67.12 ?  110 ASP A CB    1 
ATOM   913   C  CG    . ASP A 1 110 ? 101.014 139.493 109.184 1.00 68.83 ?  110 ASP A CG    1 
ATOM   914   O  OD1   . ASP A 1 110 ? 101.902 139.980 108.453 1.00 68.34 ?  110 ASP A OD1   1 
ATOM   915   O  OD2   . ASP A 1 110 ? 99.838  139.332 108.805 1.00 66.30 -1 110 ASP A OD2   1 
ATOM   916   N  N     . LYS A 1 111 ? 104.585 138.883 109.158 1.00 66.76 ?  111 LYS A N     1 
ATOM   917   C  CA    . LYS A 1 111 ? 105.533 138.101 108.360 1.00 65.22 ?  111 LYS A CA    1 
ATOM   918   C  C     . LYS A 1 111 ? 104.838 137.090 107.450 1.00 67.30 ?  111 LYS A C     1 
ATOM   919   O  O     . LYS A 1 111 ? 105.353 135.994 107.220 1.00 68.62 ?  111 LYS A O     1 
ATOM   920   C  CB    . LYS A 1 111 ? 106.556 137.387 109.250 1.00 66.02 ?  111 LYS A CB    1 
ATOM   921   C  CG    . LYS A 1 111 ? 107.157 138.253 110.346 1.00 66.12 ?  111 LYS A CG    1 
ATOM   922   C  CD    . LYS A 1 111 ? 107.882 139.456 109.765 1.00 67.95 ?  111 LYS A CD    1 
ATOM   923   C  CE    . LYS A 1 111 ? 109.099 139.034 108.958 1.00 68.19 ?  111 LYS A CE    1 
ATOM   924   N  NZ    . LYS A 1 111 ? 109.853 140.208 108.436 1.00 65.71 1  111 LYS A NZ    1 
ATOM   925   N  N     . LYS A 1 112 ? 103.667 137.441 106.919 1.00 65.38 ?  112 LYS A N     1 
ATOM   926   C  CA    . LYS A 1 112 ? 102.962 136.574 105.986 1.00 66.35 ?  112 LYS A CA    1 
ATOM   927   C  C     . LYS A 1 112 ? 102.745 137.208 104.621 1.00 66.89 ?  112 LYS A C     1 
ATOM   928   O  O     . LYS A 1 112 ? 102.363 136.502 103.683 1.00 68.20 ?  112 LYS A O     1 
ATOM   929   C  CB    . LYS A 1 112 ? 101.602 136.152 106.561 1.00 67.22 ?  112 LYS A CB    1 
ATOM   930   C  CG    . LYS A 1 112 ? 100.516 137.201 106.408 1.00 67.45 ?  112 LYS A CG    1 
ATOM   931   C  CD    . LYS A 1 112 ? 99.136  136.610 106.641 1.00 67.24 ?  112 LYS A CD    1 
ATOM   932   C  CE    . LYS A 1 112 ? 99.076  135.844 107.952 1.00 69.30 ?  112 LYS A CE    1 
ATOM   933   N  NZ    . LYS A 1 112 ? 99.525  136.676 109.103 1.00 66.57 1  112 LYS A NZ    1 
ATOM   934   N  N     . LYS A 1 113 ? 102.975 138.511 104.486 1.00 59.81 ?  113 LYS A N     1 
ATOM   935   C  CA    . LYS A 1 113 ? 102.775 139.215 103.230 1.00 58.38 ?  113 LYS A CA    1 
ATOM   936   C  C     . LYS A 1 113 ? 104.046 139.963 102.862 1.00 59.83 ?  113 LYS A C     1 
ATOM   937   O  O     . LYS A 1 113 ? 104.853 140.315 103.727 1.00 60.10 ?  113 LYS A O     1 
ATOM   938   C  CB    . LYS A 1 113 ? 101.598 140.191 103.317 1.00 58.07 ?  113 LYS A CB    1 
ATOM   939   C  CG    . LYS A 1 113 ? 100.240 139.550 103.085 1.00 58.53 ?  113 LYS A CG    1 
ATOM   940   C  CD    . LYS A 1 113 ? 100.034 139.202 101.621 1.00 59.74 ?  113 LYS A CD    1 
ATOM   941   C  CE    . LYS A 1 113 ? 98.632  138.672 101.372 1.00 58.90 ?  113 LYS A CE    1 
ATOM   942   N  NZ    . LYS A 1 113 ? 98.431  138.277 99.951  1.00 60.00 1  113 LYS A NZ    1 
ATOM   943   N  N     . ILE A 1 114 ? 104.219 140.201 101.565 1.00 53.46 ?  114 ILE A N     1 
ATOM   944   C  CA    . ILE A 1 114 ? 105.402 140.859 101.027 1.00 51.44 ?  114 ILE A CA    1 
ATOM   945   C  C     . ILE A 1 114 ? 105.018 142.281 100.647 1.00 49.75 ?  114 ILE A C     1 
ATOM   946   O  O     . ILE A 1 114 ? 104.156 142.491 99.785  1.00 52.17 ?  114 ILE A O     1 
ATOM   947   C  CB    . ILE A 1 114 ? 105.976 140.098 99.824  1.00 51.20 ?  114 ILE A CB    1 
ATOM   948   C  CG1   . ILE A 1 114 ? 106.700 138.836 100.293 1.00 50.03 ?  114 ILE A CG1   1 
ATOM   949   C  CG2   . ILE A 1 114 ? 106.917 140.985 99.027  1.00 48.71 ?  114 ILE A CG2   1 
ATOM   950   C  CD1   . ILE A 1 114 ? 106.819 137.774 99.228  1.00 50.18 ?  114 ILE A CD1   1 
ATOM   951   N  N     . LEU A 1 115 ? 105.653 143.257 101.294 1.00 46.17 ?  115 LEU A N     1 
ATOM   952   C  CA    . LEU A 1 115 ? 105.392 144.660 101.004 1.00 46.36 ?  115 LEU A CA    1 
ATOM   953   C  C     . LEU A 1 115 ? 106.334 145.232 99.956  1.00 47.43 ?  115 LEU A C     1 
ATOM   954   O  O     . LEU A 1 115 ? 105.953 146.161 99.235  1.00 49.19 ?  115 LEU A O     1 
ATOM   955   C  CB    . LEU A 1 115 ? 105.497 145.491 102.284 1.00 47.39 ?  115 LEU A CB    1 
ATOM   956   C  CG    . LEU A 1 115 ? 104.442 145.217 103.355 1.00 48.80 ?  115 LEU A CG    1 
ATOM   957   C  CD1   . LEU A 1 115 ? 104.951 145.650 104.718 1.00 46.26 ?  115 LEU A CD1   1 
ATOM   958   C  CD2   . LEU A 1 115 ? 103.140 145.923 103.015 1.00 45.93 ?  115 LEU A CD2   1 
ATOM   959   N  N     . GLU A 1 116 ? 107.548 144.700 99.849  1.00 45.75 ?  116 GLU A N     1 
ATOM   960   C  CA    . GLU A 1 116 ? 108.569 145.239 98.963  1.00 42.66 ?  116 GLU A CA    1 
ATOM   961   C  C     . GLU A 1 116 ? 108.959 144.205 97.919  1.00 42.32 ?  116 GLU A C     1 
ATOM   962   O  O     . GLU A 1 116 ? 109.280 143.062 98.260  1.00 46.46 ?  116 GLU A O     1 
ATOM   963   C  CB    . GLU A 1 116 ? 109.811 145.664 99.750  1.00 43.84 ?  116 GLU A CB    1 
ATOM   964   C  CG    . GLU A 1 116 ? 109.945 147.160 99.940  1.00 44.60 ?  116 GLU A CG    1 
ATOM   965   C  CD    . GLU A 1 116 ? 111.185 147.534 100.724 1.00 43.95 ?  116 GLU A CD    1 
ATOM   966   O  OE1   . GLU A 1 116 ? 111.880 146.618 101.212 1.00 42.41 ?  116 GLU A OE1   1 
ATOM   967   O  OE2   . GLU A 1 116 ? 111.466 148.744 100.853 1.00 46.49 -1 116 GLU A OE2   1 
ATOM   968   N  N     . ARG A 1 117 ? 108.932 144.611 96.653  1.00 41.40 ?  117 ARG A N     1 
ATOM   969   C  CA    . ARG A 1 117 ? 109.553 143.839 95.592  1.00 42.35 ?  117 ARG A CA    1 
ATOM   970   C  C     . ARG A 1 117 ? 111.031 144.211 95.501  1.00 42.07 ?  117 ARG A C     1 
ATOM   971   O  O     . ARG A 1 117 ? 111.539 145.032 96.269  1.00 45.43 ?  117 ARG A O     1 
ATOM   972   C  CB    . ARG A 1 117 ? 108.835 144.080 94.267  1.00 42.96 ?  117 ARG A CB    1 
ATOM   973   C  CG    . ARG A 1 117 ? 107.362 143.706 94.277  1.00 43.74 ?  117 ARG A CG    1 
ATOM   974   C  CD    . ARG A 1 117 ? 106.870 143.361 92.882  1.00 46.22 ?  117 ARG A CD    1 
ATOM   975   N  NE    . ARG A 1 117 ? 106.964 141.934 92.604  1.00 47.84 ?  117 ARG A NE    1 
ATOM   976   C  CZ    . ARG A 1 117 ? 105.926 141.110 92.552  1.00 44.68 ?  117 ARG A CZ    1 
ATOM   977   N  NH1   . ARG A 1 117 ? 104.692 141.539 92.758  1.00 45.48 1  117 ARG A NH1   1 
ATOM   978   N  NH2   . ARG A 1 117 ? 106.131 139.824 92.283  1.00 45.28 ?  117 ARG A NH2   1 
ATOM   979   N  N     . TYR A 1 118 ? 111.740 143.595 94.555  1.00 35.82 ?  118 TYR A N     1 
ATOM   980   C  CA    . TYR A 1 118 ? 113.131 143.973 94.332  1.00 33.09 ?  118 TYR A CA    1 
ATOM   981   C  C     . TYR A 1 118 ? 113.235 145.416 93.857  1.00 35.83 ?  118 TYR A C     1 
ATOM   982   O  O     . TYR A 1 118 ? 114.089 146.177 94.329  1.00 36.46 ?  118 TYR A O     1 
ATOM   983   C  CB    . TYR A 1 118 ? 113.782 143.025 93.328  1.00 33.04 ?  118 TYR A CB    1 
ATOM   984   C  CG    . TYR A 1 118 ? 115.291 143.068 93.346  1.00 34.61 ?  118 TYR A CG    1 
ATOM   985   C  CD1   . TYR A 1 118 ? 115.991 143.015 94.542  1.00 34.13 ?  118 TYR A CD1   1 
ATOM   986   C  CD2   . TYR A 1 118 ? 116.015 143.165 92.169  1.00 32.57 ?  118 TYR A CD2   1 
ATOM   987   C  CE1   . TYR A 1 118 ? 117.369 143.053 94.564  1.00 32.21 ?  118 TYR A CE1   1 
ATOM   988   C  CE2   . TYR A 1 118 ? 117.394 143.202 92.179  1.00 28.54 ?  118 TYR A CE2   1 
ATOM   989   C  CZ    . TYR A 1 118 ? 118.065 143.146 93.379  1.00 33.42 ?  118 TYR A CZ    1 
ATOM   990   O  OH    . TYR A 1 118 ? 119.439 143.186 93.393  1.00 41.14 ?  118 TYR A OH    1 
ATOM   991   N  N     . GLU A 1 119 ? 112.359 145.812 92.931  1.00 38.05 ?  119 GLU A N     1 
ATOM   992   C  CA    . GLU A 1 119 ? 112.379 147.181 92.432  1.00 33.51 ?  119 GLU A CA    1 
ATOM   993   C  C     . GLU A 1 119 ? 112.014 148.176 93.527  1.00 34.98 ?  119 GLU A C     1 
ATOM   994   O  O     . GLU A 1 119 ? 112.589 149.265 93.593  1.00 41.26 ?  119 GLU A O     1 
ATOM   995   C  CB    . GLU A 1 119 ? 111.436 147.316 91.238  1.00 34.53 ?  119 GLU A CB    1 
ATOM   996   C  CG    . GLU A 1 119 ? 111.895 146.566 89.997  1.00 33.42 ?  119 GLU A CG    1 
ATOM   997   C  CD    . GLU A 1 119 ? 111.346 145.155 89.930  1.00 38.33 ?  119 GLU A CD    1 
ATOM   998   O  OE1   . GLU A 1 119 ? 111.093 144.557 90.997  1.00 40.04 ?  119 GLU A OE1   1 
ATOM   999   O  OE2   . GLU A 1 119 ? 111.168 144.640 88.806  1.00 39.80 -1 119 GLU A OE2   1 
ATOM   1000  N  N     . ASP A 1 120 ? 111.067 147.819 94.398  1.00 38.34 ?  120 ASP A N     1 
ATOM   1001  C  CA    . ASP A 1 120 ? 110.693 148.713 95.490  1.00 35.32 ?  120 ASP A CA    1 
ATOM   1002  C  C     . ASP A 1 120 ? 111.853 148.925 96.455  1.00 36.45 ?  120 ASP A C     1 
ATOM   1003  O  O     . ASP A 1 120 ? 112.150 150.061 96.845  1.00 37.89 ?  120 ASP A O     1 
ATOM   1004  C  CB    . ASP A 1 120 ? 109.479 148.160 96.235  1.00 39.27 ?  120 ASP A CB    1 
ATOM   1005  C  CG    . ASP A 1 120 ? 108.307 147.896 95.320  1.00 44.42 ?  120 ASP A CG    1 
ATOM   1006  O  OD1   . ASP A 1 120 ? 108.038 148.741 94.444  1.00 42.64 ?  120 ASP A OD1   1 
ATOM   1007  O  OD2   . ASP A 1 120 ? 107.653 146.844 95.478  1.00 48.92 -1 120 ASP A OD2   1 
ATOM   1008  N  N     . ARG A 1 121 ? 112.514 147.837 96.855  1.00 35.02 ?  121 ARG A N     1 
ATOM   1009  C  CA    . ARG A 1 121 ? 113.649 147.957 97.763  1.00 32.20 ?  121 ARG A CA    1 
ATOM   1010  C  C     . ARG A 1 121 ? 114.778 148.750 97.122  1.00 33.06 ?  121 ARG A C     1 
ATOM   1011  O  O     . ARG A 1 121 ? 115.398 149.600 97.772  1.00 38.75 ?  121 ARG A O     1 
ATOM   1012  C  CB    . ARG A 1 121 ? 114.135 146.569 98.181  1.00 30.88 ?  121 ARG A CB    1 
ATOM   1013  C  CG    . ARG A 1 121 ? 115.416 146.574 99.000  1.00 30.04 ?  121 ARG A CG    1 
ATOM   1014  C  CD    . ARG A 1 121 ? 115.123 146.350 100.474 1.00 29.75 ?  121 ARG A CD    1 
ATOM   1015  N  NE    . ARG A 1 121 ? 114.398 147.467 101.068 1.00 37.01 ?  121 ARG A NE    1 
ATOM   1016  C  CZ    . ARG A 1 121 ? 114.963 148.447 101.759 1.00 36.31 ?  121 ARG A CZ    1 
ATOM   1017  N  NH1   . ARG A 1 121 ? 116.266 148.474 101.984 1.00 34.61 1  121 ARG A NH1   1 
ATOM   1018  N  NH2   . ARG A 1 121 ? 114.200 149.424 102.243 1.00 33.20 ?  121 ARG A NH2   1 
ATOM   1019  N  N     . ILE A 1 122 ? 115.054 148.493 95.842  1.00 30.77 ?  122 ILE A N     1 
ATOM   1020  C  CA    . ILE A 1 122 ? 116.116 149.216 95.152  1.00 28.80 ?  122 ILE A CA    1 
ATOM   1021  C  C     . ILE A 1 122 ? 115.782 150.700 95.057  1.00 30.77 ?  122 ILE A C     1 
ATOM   1022  O  O     . ILE A 1 122 ? 116.646 151.556 95.272  1.00 34.25 ?  122 ILE A O     1 
ATOM   1023  C  CB    . ILE A 1 122 ? 116.370 148.590 93.768  1.00 30.30 ?  122 ILE A CB    1 
ATOM   1024  C  CG1   . ILE A 1 122 ? 117.216 147.325 93.918  1.00 26.40 ?  122 ILE A CG1   1 
ATOM   1025  C  CG2   . ILE A 1 122 ? 117.045 149.585 92.835  1.00 28.94 ?  122 ILE A CG2   1 
ATOM   1026  C  CD1   . ILE A 1 122 ? 117.632 146.711 92.612  1.00 28.85 ?  122 ILE A CD1   1 
ATOM   1027  N  N     . SER A 1 123 ? 114.526 151.030 94.745  1.00 31.33 ?  123 SER A N     1 
ATOM   1028  C  CA    . SER A 1 123 ? 114.119 152.430 94.670  1.00 32.29 ?  123 SER A CA    1 
ATOM   1029  C  C     . SER A 1 123 ? 114.246 153.116 96.022  1.00 30.43 ?  123 SER A C     1 
ATOM   1030  O  O     . SER A 1 123 ? 114.693 154.264 96.103  1.00 32.18 ?  123 SER A O     1 
ATOM   1031  C  CB    . SER A 1 123 ? 112.682 152.534 94.161  1.00 28.37 ?  123 SER A CB    1 
ATOM   1032  O  OG    . SER A 1 123 ? 112.457 151.651 93.081  1.00 32.84 ?  123 SER A OG    1 
ATOM   1033  N  N     . ILE A 1 124 ? 113.848 152.430 97.095  1.00 30.02 ?  124 ILE A N     1 
ATOM   1034  C  CA    . ILE A 1 124 ? 113.946 153.024 98.425  1.00 32.25 ?  124 ILE A CA    1 
ATOM   1035  C  C     . ILE A 1 124 ? 115.402 153.260 98.801  1.00 32.94 ?  124 ILE A C     1 
ATOM   1036  O  O     . ILE A 1 124 ? 115.757 154.322 99.331  1.00 38.22 ?  124 ILE A O     1 
ATOM   1037  C  CB    . ILE A 1 124 ? 113.220 152.140 99.453  1.00 36.78 ?  124 ILE A CB    1 
ATOM   1038  C  CG1   . ILE A 1 124 ? 111.707 152.277 99.283  1.00 37.74 ?  124 ILE A CG1   1 
ATOM   1039  C  CG2   . ILE A 1 124 ? 113.636 152.503 100.870 1.00 29.38 ?  124 ILE A CG2   1 
ATOM   1040  C  CD1   . ILE A 1 124 ? 111.229 153.712 99.204  1.00 32.41 ?  124 ILE A CD1   1 
ATOM   1041  N  N     . VAL A 1 125 ? 116.273 152.286 98.521  1.00 30.55 ?  125 VAL A N     1 
ATOM   1042  C  CA    . VAL A 1 125 ? 117.689 152.447 98.839  1.00 29.88 ?  125 VAL A CA    1 
ATOM   1043  C  C     . VAL A 1 125 ? 118.297 153.575 98.011  1.00 24.99 ?  125 VAL A C     1 
ATOM   1044  O  O     . VAL A 1 125 ? 119.125 154.347 98.503  1.00 32.24 ?  125 VAL A O     1 
ATOM   1045  C  CB    . VAL A 1 125 ? 118.440 151.117 98.638  1.00 30.99 ?  125 VAL A CB    1 
ATOM   1046  C  CG1   . VAL A 1 125 ? 119.923 151.301 98.882  1.00 30.65 ?  125 VAL A CG1   1 
ATOM   1047  C  CG2   . VAL A 1 125 ? 117.896 150.061 99.578  1.00 25.85 ?  125 VAL A CG2   1 
ATOM   1048  N  N     . ALA A 1 126 ? 117.891 153.692 96.744  1.00 23.57 ?  126 ALA A N     1 
ATOM   1049  C  CA    . ALA A 1 126 ? 118.389 154.771 95.897  1.00 22.17 ?  126 ALA A CA    1 
ATOM   1050  C  C     . ALA A 1 126 ? 117.938 156.135 96.404  1.00 29.36 ?  126 ALA A C     1 
ATOM   1051  O  O     . ALA A 1 126 ? 118.725 157.089 96.423  1.00 33.76 ?  126 ALA A O     1 
ATOM   1052  C  CB    . ALA A 1 126 ? 117.925 154.559 94.458  1.00 29.36 ?  126 ALA A CB    1 
ATOM   1053  N  N     . LEU A 1 127 ? 116.671 156.249 96.806  1.00 31.34 ?  127 LEU A N     1 
ATOM   1054  C  CA    . LEU A 1 127 ? 116.171 157.511 97.339  1.00 27.26 ?  127 LEU A CA    1 
ATOM   1055  C  C     . LEU A 1 127 ? 116.881 157.875 98.635  1.00 30.16 ?  127 LEU A C     1 
ATOM   1056  O  O     . LEU A 1 127 ? 117.162 159.051 98.890  1.00 36.11 ?  127 LEU A O     1 
ATOM   1057  C  CB    . LEU A 1 127 ? 114.660 157.430 97.553  1.00 32.59 ?  127 LEU A CB    1 
ATOM   1058  C  CG    . LEU A 1 127 ? 113.802 157.360 96.290  1.00 30.20 ?  127 LEU A CG    1 
ATOM   1059  C  CD1   . LEU A 1 127 ? 112.434 156.782 96.606  1.00 35.03 ?  127 LEU A CD1   1 
ATOM   1060  C  CD2   . LEU A 1 127 ? 113.671 158.730 95.647  1.00 31.61 ?  127 LEU A CD2   1 
ATOM   1061  N  N     . PHE A 1 128 ? 117.170 156.877 99.472  1.00 29.65 ?  128 PHE A N     1 
ATOM   1062  C  CA    . PHE A 1 128 ? 117.950 157.133 100.677 1.00 27.44 ?  128 PHE A CA    1 
ATOM   1063  C  C     . PHE A 1 128 ? 119.363 157.590 100.333 1.00 27.67 ?  128 PHE A C     1 
ATOM   1064  O  O     . PHE A 1 128 ? 119.898 158.505 100.970 1.00 39.06 ?  128 PHE A O     1 
ATOM   1065  C  CB    . PHE A 1 128 ? 117.986 155.880 101.550 1.00 27.29 ?  128 PHE A CB    1 
ATOM   1066  C  CG    . PHE A 1 128 ? 118.932 155.979 102.708 1.00 32.64 ?  128 PHE A CG    1 
ATOM   1067  C  CD1   . PHE A 1 128 ? 120.169 155.359 102.664 1.00 28.84 ?  128 PHE A CD1   1 
ATOM   1068  C  CD2   . PHE A 1 128 ? 118.581 156.686 103.844 1.00 32.00 ?  128 PHE A CD2   1 
ATOM   1069  C  CE1   . PHE A 1 128 ? 121.040 155.451 103.726 1.00 31.85 ?  128 PHE A CE1   1 
ATOM   1070  C  CE2   . PHE A 1 128 ? 119.449 156.778 104.912 1.00 35.22 ?  128 PHE A CE2   1 
ATOM   1071  C  CZ    . PHE A 1 128 ? 120.679 156.160 104.853 1.00 33.47 ?  128 PHE A CZ    1 
ATOM   1072  N  N     . PHE A 1 129 ? 119.982 156.959 99.333  1.00 24.44 ?  129 PHE A N     1 
ATOM   1073  C  CA    . PHE A 1 129 ? 121.340 157.318 98.938  1.00 22.14 ?  129 PHE A CA    1 
ATOM   1074  C  C     . PHE A 1 129 ? 121.413 158.747 98.417  1.00 28.86 ?  129 PHE A C     1 
ATOM   1075  O  O     . PHE A 1 129 ? 122.326 159.500 98.772  1.00 28.00 ?  129 PHE A O     1 
ATOM   1076  C  CB    . PHE A 1 129 ? 121.845 156.353 97.866  1.00 22.02 ?  129 PHE A CB    1 
ATOM   1077  C  CG    . PHE A 1 129 ? 122.322 155.037 98.398  1.00 23.96 ?  129 PHE A CG    1 
ATOM   1078  C  CD1   . PHE A 1 129 ? 122.563 154.859 99.747  1.00 24.20 ?  129 PHE A CD1   1 
ATOM   1079  C  CD2   . PHE A 1 129 ? 122.541 153.976 97.536  1.00 22.46 ?  129 PHE A CD2   1 
ATOM   1080  C  CE1   . PHE A 1 129 ? 123.006 153.644 100.225 1.00 24.48 ?  129 PHE A CE1   1 
ATOM   1081  C  CE2   . PHE A 1 129 ? 122.986 152.762 98.011  1.00 24.48 ?  129 PHE A CE2   1 
ATOM   1082  C  CZ    . PHE A 1 129 ? 123.219 152.596 99.357  1.00 26.83 ?  129 PHE A CZ    1 
ATOM   1083  N  N     . ALA A 1 130 ? 120.461 159.135 97.566  1.00 30.83 ?  130 ALA A N     1 
ATOM   1084  C  CA    . ALA A 1 130 ? 120.567 160.412 96.868  1.00 31.96 ?  130 ALA A CA    1 
ATOM   1085  C  C     . ALA A 1 130 ? 120.365 161.598 97.801  1.00 40.33 ?  130 ALA A C     1 
ATOM   1086  O  O     . ALA A 1 130 ? 120.881 162.689 97.528  1.00 42.45 ?  130 ALA A O     1 
ATOM   1087  C  CB    . ALA A 1 130 ? 119.563 160.464 95.722  1.00 32.00 ?  130 ALA A CB    1 
ATOM   1088  N  N     . ASN A 1 131 ? 119.618 161.409 98.891  1.00 40.41 ?  131 ASN A N     1 
ATOM   1089  C  CA    . ASN A 1 131 ? 119.413 162.448 99.903  1.00 38.34 ?  131 ASN A CA    1 
ATOM   1090  C  C     . ASN A 1 131 ? 118.776 163.704 99.305  1.00 41.21 ?  131 ASN A C     1 
ATOM   1091  O  O     . ASN A 1 131 ? 119.134 164.830 99.657  1.00 46.33 ?  131 ASN A O     1 
ATOM   1092  C  CB    . ASN A 1 131 ? 120.725 162.791 100.614 1.00 34.85 ?  131 ASN A CB    1 
ATOM   1093  C  CG    . ASN A 1 131 ? 120.511 163.266 102.035 1.00 43.68 ?  131 ASN A CG    1 
ATOM   1094  O  OD1   . ASN A 1 131 ? 119.534 162.897 102.686 1.00 43.08 ?  131 ASN A OD1   1 
ATOM   1095  N  ND2   . ASN A 1 131 ? 121.429 164.090 102.528 1.00 44.19 ?  131 ASN A ND2   1 
ATOM   1096  N  N     . GLY A 1 132 ? 117.826 163.512 98.393  1.00 39.55 ?  132 GLY A N     1 
ATOM   1097  C  CA    . GLY A 1 132 ? 117.049 164.605 97.841  1.00 39.30 ?  132 GLY A CA    1 
ATOM   1098  C  C     . GLY A 1 132 ? 117.268 164.885 96.371  1.00 43.26 ?  132 GLY A C     1 
ATOM   1099  O  O     . GLY A 1 132 ? 116.549 165.722 95.809  1.00 45.37 ?  132 GLY A O     1 
ATOM   1100  N  N     . ASP A 1 133 ? 118.225 164.224 95.725  1.00 43.29 ?  133 ASP A N     1 
ATOM   1101  C  CA    . ASP A 1 133 ? 118.521 164.448 94.313  1.00 41.14 ?  133 ASP A CA    1 
ATOM   1102  C  C     . ASP A 1 133 ? 117.821 163.375 93.486  1.00 42.99 ?  133 ASP A C     1 
ATOM   1103  O  O     . ASP A 1 133 ? 118.197 162.200 93.536  1.00 47.06 ?  133 ASP A O     1 
ATOM   1104  C  CB    . ASP A 1 133 ? 120.028 164.436 94.069  1.00 43.53 ?  133 ASP A CB    1 
ATOM   1105  C  CG    . ASP A 1 133 ? 120.417 165.116 92.772  1.00 46.21 ?  133 ASP A CG    1 
ATOM   1106  O  OD1   . ASP A 1 133 ? 119.516 165.417 91.961  1.00 48.02 ?  133 ASP A OD1   1 
ATOM   1107  O  OD2   . ASP A 1 133 ? 121.626 165.346 92.561  1.00 46.08 -1 133 ASP A OD2   1 
ATOM   1108  N  N     . THR A 1 134 ? 116.803 163.780 92.722  1.00 45.97 ?  134 THR A N     1 
ATOM   1109  C  CA    . THR A 1 134 ? 116.045 162.814 91.934  1.00 41.92 ?  134 THR A CA    1 
ATOM   1110  C  C     . THR A 1 134 ? 116.900 162.186 90.837  1.00 43.76 ?  134 THR A C     1 
ATOM   1111  O  O     . THR A 1 134 ? 116.795 160.982 90.577  1.00 44.74 ?  134 THR A O     1 
ATOM   1112  C  CB    . THR A 1 134 ? 114.798 163.475 91.341  1.00 45.87 ?  134 THR A CB    1 
ATOM   1113  O  OG1   . THR A 1 134 ? 114.174 162.582 90.410  1.00 48.16 ?  134 THR A OG1   1 
ATOM   1114  C  CG2   . THR A 1 134 ? 115.150 164.784 90.641  1.00 46.73 ?  134 THR A CG2   1 
ATOM   1115  N  N     . GLU A 1 135 ? 117.750 162.981 90.181  1.00 42.46 ?  135 GLU A N     1 
ATOM   1116  C  CA    . GLU A 1 135 ? 118.623 162.429 89.149  1.00 43.05 ?  135 GLU A CA    1 
ATOM   1117  C  C     . GLU A 1 135 ? 119.647 161.471 89.745  1.00 43.92 ?  135 GLU A C     1 
ATOM   1118  O  O     . GLU A 1 135 ? 119.922 160.411 89.173  1.00 43.52 ?  135 GLU A O     1 
ATOM   1119  C  CB    . GLU A 1 135 ? 119.318 163.558 88.389  1.00 43.57 ?  135 GLU A CB    1 
ATOM   1120  C  CG    . GLU A 1 135 ? 118.430 164.261 87.375  1.00 44.06 ?  135 GLU A CG    1 
ATOM   1121  C  CD    . GLU A 1 135 ? 117.327 163.366 86.843  1.00 47.86 ?  135 GLU A CD    1 
ATOM   1122  O  OE1   . GLU A 1 135 ? 117.602 162.561 85.929  1.00 47.89 ?  135 GLU A OE1   1 
ATOM   1123  O  OE2   . GLU A 1 135 ? 116.183 163.472 87.333  1.00 48.27 -1 135 GLU A OE2   1 
ATOM   1124  N  N     . LYS A 1 136 ? 120.218 161.826 90.897  1.00 35.81 ?  136 LYS A N     1 
ATOM   1125  C  CA    . LYS A 1 136 ? 121.133 160.918 91.580  1.00 32.22 ?  136 LYS A CA    1 
ATOM   1126  C  C     . LYS A 1 136 ? 120.415 159.648 92.019  1.00 33.99 ?  136 LYS A C     1 
ATOM   1127  O  O     . LYS A 1 136 ? 120.982 158.551 91.958  1.00 39.30 ?  136 LYS A O     1 
ATOM   1128  C  CB    . LYS A 1 136 ? 121.769 161.625 92.776  1.00 38.68 ?  136 LYS A CB    1 
ATOM   1129  C  CG    . LYS A 1 136 ? 122.911 160.868 93.423  1.00 37.05 ?  136 LYS A CG    1 
ATOM   1130  C  CD    . LYS A 1 136 ? 124.230 161.151 92.729  1.00 36.18 ?  136 LYS A CD    1 
ATOM   1131  C  CE    . LYS A 1 136 ? 125.402 160.703 93.585  1.00 38.80 ?  136 LYS A CE    1 
ATOM   1132  N  NZ    . LYS A 1 136 ? 126.704 161.160 93.028  1.00 39.04 1  136 LYS A NZ    1 
ATOM   1133  N  N     . ALA A 1 137 ? 119.164 159.778 92.467  1.00 33.83 ?  137 ALA A N     1 
ATOM   1134  C  CA    . ALA A 1 137 ? 118.383 158.603 92.839  1.00 30.50 ?  137 ALA A CA    1 
ATOM   1135  C  C     . ALA A 1 137 ? 118.146 157.698 91.637  1.00 31.42 ?  137 ALA A C     1 
ATOM   1136  O  O     . ALA A 1 137 ? 118.221 156.471 91.753  1.00 33.06 ?  137 ALA A O     1 
ATOM   1137  C  CB    . ALA A 1 137 ? 117.054 159.029 93.461  1.00 29.01 ?  137 ALA A CB    1 
ATOM   1138  N  N     . LYS A 1 138 ? 117.853 158.285 90.474  1.00 35.80 ?  138 LYS A N     1 
ATOM   1139  C  CA    . LYS A 1 138 ? 117.673 157.481 89.271  1.00 34.99 ?  138 LYS A CA    1 
ATOM   1140  C  C     . LYS A 1 138 ? 118.978 156.817 88.849  1.00 31.55 ?  138 LYS A C     1 
ATOM   1141  O  O     . LYS A 1 138 ? 118.975 155.681 88.362  1.00 33.93 ?  138 LYS A O     1 
ATOM   1142  C  CB    . LYS A 1 138 ? 117.114 158.342 88.139  1.00 39.13 ?  138 LYS A CB    1 
ATOM   1143  C  CG    . LYS A 1 138 ? 115.653 158.719 88.317  1.00 39.27 ?  138 LYS A CG    1 
ATOM   1144  C  CD    . LYS A 1 138 ? 115.340 160.043 87.642  1.00 37.78 ?  138 LYS A CD    1 
ATOM   1145  C  CE    . LYS A 1 138 ? 114.970 159.842 86.182  1.00 37.18 ?  138 LYS A CE    1 
ATOM   1146  N  NZ    . LYS A 1 138 ? 114.959 161.128 85.433  1.00 39.98 1  138 LYS A NZ    1 
ATOM   1147  N  N     . GLU A 1 139 ? 120.106 157.512 89.025  1.00 36.22 ?  139 GLU A N     1 
ATOM   1148  C  CA    . GLU A 1 139 ? 121.400 156.897 88.745  1.00 32.63 ?  139 GLU A CA    1 
ATOM   1149  C  C     . GLU A 1 139 ? 121.652 155.706 89.661  1.00 32.19 ?  139 GLU A C     1 
ATOM   1150  O  O     . GLU A 1 139 ? 122.128 154.657 89.213  1.00 40.53 ?  139 GLU A O     1 
ATOM   1151  C  CB    . GLU A 1 139 ? 122.520 157.926 88.893  1.00 33.71 ?  139 GLU A CB    1 
ATOM   1152  C  CG    . GLU A 1 139 ? 122.488 159.039 87.864  1.00 36.98 ?  139 GLU A CG    1 
ATOM   1153  C  CD    . GLU A 1 139 ? 123.619 160.029 88.047  1.00 45.18 ?  139 GLU A CD    1 
ATOM   1154  O  OE1   . GLU A 1 139 ? 124.753 159.589 88.333  1.00 43.35 ?  139 GLU A OE1   1 
ATOM   1155  O  OE2   . GLU A 1 139 ? 123.377 161.246 87.905  1.00 41.43 -1 139 GLU A OE2   1 
ATOM   1156  N  N     . TYR A 1 140 ? 121.333 155.846 90.950  1.00 23.52 ?  140 TYR A N     1 
ATOM   1157  C  CA    . TYR A 1 140 ? 121.482 154.729 91.877  1.00 27.69 ?  140 TYR A CA    1 
ATOM   1158  C  C     . TYR A 1 140 ? 120.553 153.579 91.511  1.00 28.10 ?  140 TYR A C     1 
ATOM   1159  O  O     . TYR A 1 140 ? 120.927 152.406 91.625  1.00 33.30 ?  140 TYR A O     1 
ATOM   1160  C  CB    . TYR A 1 140 ? 121.211 155.191 93.308  1.00 28.73 ?  140 TYR A CB    1 
ATOM   1161  C  CG    . TYR A 1 140 ? 122.352 155.934 93.954  1.00 30.16 ?  140 TYR A CG    1 
ATOM   1162  C  CD1   . TYR A 1 140 ? 123.609 155.360 94.060  1.00 28.80 ?  140 TYR A CD1   1 
ATOM   1163  C  CD2   . TYR A 1 140 ? 122.166 157.207 94.471  1.00 30.41 ?  140 TYR A CD2   1 
ATOM   1164  C  CE1   . TYR A 1 140 ? 124.652 156.037 94.655  1.00 29.52 ?  140 TYR A CE1   1 
ATOM   1165  C  CE2   . TYR A 1 140 ? 123.201 157.890 95.068  1.00 30.02 ?  140 TYR A CE2   1 
ATOM   1166  C  CZ    . TYR A 1 140 ? 124.440 157.303 95.158  1.00 25.73 ?  140 TYR A CZ    1 
ATOM   1167  O  OH    . TYR A 1 140 ? 125.468 157.988 95.754  1.00 31.30 ?  140 TYR A OH    1 
ATOM   1168  N  N     . VAL A 1 141 ? 119.328 153.898 91.091  1.00 32.97 ?  141 VAL A N     1 
ATOM   1169  C  CA    . VAL A 1 141 ? 118.380 152.865 90.687  1.00 30.44 ?  141 VAL A CA    1 
ATOM   1170  C  C     . VAL A 1 141 ? 118.901 152.111 89.471  1.00 29.32 ?  141 VAL A C     1 
ATOM   1171  O  O     . VAL A 1 141 ? 118.807 150.881 89.402  1.00 34.54 ?  141 VAL A O     1 
ATOM   1172  C  CB    . VAL A 1 141 ? 116.992 153.482 90.434  1.00 32.31 ?  141 VAL A CB    1 
ATOM   1173  C  CG1   . VAL A 1 141 ? 116.351 152.895 89.191  1.00 28.92 ?  141 VAL A CG1   1 
ATOM   1174  C  CG2   . VAL A 1 141 ? 116.095 153.253 91.632  1.00 32.26 ?  141 VAL A CG2   1 
ATOM   1175  N  N     . ASN A 1 142 ? 119.457 152.832 88.495  1.00 27.50 ?  142 ASN A N     1 
ATOM   1176  C  CA    . ASN A 1 142 ? 120.030 152.166 87.331  1.00 29.40 ?  142 ASN A CA    1 
ATOM   1177  C  C     . ASN A 1 142 ? 121.261 151.352 87.707  1.00 29.06 ?  142 ASN A C     1 
ATOM   1178  O  O     . ASN A 1 142 ? 121.525 150.312 87.095  1.00 36.97 ?  142 ASN A O     1 
ATOM   1179  C  CB    . ASN A 1 142 ? 120.379 153.193 86.257  1.00 29.77 ?  142 ASN A CB    1 
ATOM   1180  C  CG    . ASN A 1 142 ? 119.158 153.702 85.523  1.00 32.97 ?  142 ASN A CG    1 
ATOM   1181  O  OD1   . ASN A 1 142 ? 118.237 152.942 85.226  1.00 32.44 ?  142 ASN A OD1   1 
ATOM   1182  N  ND2   . ASN A 1 142 ? 119.143 154.996 85.225  1.00 33.88 ?  142 ASN A ND2   1 
ATOM   1183  N  N     . LEU A 1 143 ? 122.021 151.810 88.702  1.00 28.20 ?  143 LEU A N     1 
ATOM   1184  C  CA    . LEU A 1 143 ? 123.187 151.062 89.157  1.00 25.80 ?  143 LEU A CA    1 
ATOM   1185  C  C     . LEU A 1 143 ? 122.786 149.746 89.812  1.00 25.05 ?  143 LEU A C     1 
ATOM   1186  O  O     . LEU A 1 143 ? 123.398 148.704 89.552  1.00 28.27 ?  143 LEU A O     1 
ATOM   1187  C  CB    . LEU A 1 143 ? 123.997 151.916 90.129  1.00 23.48 ?  143 LEU A CB    1 
ATOM   1188  C  CG    . LEU A 1 143 ? 125.460 151.539 90.337  1.00 28.00 ?  143 LEU A CG    1 
ATOM   1189  C  CD1   . LEU A 1 143 ? 126.259 151.857 89.091  1.00 28.70 ?  143 LEU A CD1   1 
ATOM   1190  C  CD2   . LEU A 1 143 ? 126.018 152.274 91.540  1.00 29.39 ?  143 LEU A CD2   1 
ATOM   1191  N  N     . MET A 1 144 ? 121.767 149.776 90.668  1.00 28.78 ?  144 MET A N     1 
ATOM   1192  C  CA    . MET A 1 144 ? 121.369 148.590 91.420  1.00 23.13 ?  144 MET A CA    1 
ATOM   1193  C  C     . MET A 1 144 ? 120.453 147.655 90.643  1.00 25.40 ?  144 MET A C     1 
ATOM   1194  O  O     . MET A 1 144 ? 120.456 146.447 90.907  1.00 29.77 ?  144 MET A O     1 
ATOM   1195  C  CB    . MET A 1 144 ? 120.688 149.002 92.726  1.00 23.68 ?  144 MET A CB    1 
ATOM   1196  C  CG    . MET A 1 144 ? 121.496 149.981 93.552  1.00 26.24 ?  144 MET A CG    1 
ATOM   1197  S  SD    . MET A 1 144 ? 120.994 150.007 95.277  1.00 33.43 ?  144 MET A SD    1 
ATOM   1198  C  CE    . MET A 1 144 ? 120.250 151.631 95.353  1.00 28.66 ?  144 MET A CE    1 
ATOM   1199  N  N     . ILE A 1 145 ? 119.668 148.172 89.701  1.00 29.37 ?  145 ILE A N     1 
ATOM   1200  C  CA    . ILE A 1 145 ? 118.811 147.313 88.894  1.00 28.87 ?  145 ILE A CA    1 
ATOM   1201  C  C     . ILE A 1 145 ? 119.592 146.663 87.755  1.00 31.49 ?  145 ILE A C     1 
ATOM   1202  O  O     . ILE A 1 145 ? 119.225 145.577 87.297  1.00 35.53 ?  145 ILE A O     1 
ATOM   1203  C  CB    . ILE A 1 145 ? 117.592 148.098 88.371  1.00 27.96 ?  145 ILE A CB    1 
ATOM   1204  C  CG1   . ILE A 1 145 ? 116.402 147.159 88.163  1.00 30.70 ?  145 ILE A CG1   1 
ATOM   1205  C  CG2   . ILE A 1 145 ? 117.919 148.843 87.084  1.00 32.52 ?  145 ILE A CG2   1 
ATOM   1206  C  CD1   . ILE A 1 145 ? 115.911 146.496 89.428  1.00 28.51 ?  145 ILE A CD1   1 
ATOM   1207  N  N     . ASN A 1 146 ? 120.667 147.304 87.291  1.00 23.60 ?  146 ASN A N     1 
ATOM   1208  C  CA    . ASN A 1 146 ? 121.649 146.616 86.466  1.00 26.02 ?  146 ASN A CA    1 
ATOM   1209  C  C     . ASN A 1 146 ? 122.509 145.671 87.288  1.00 25.75 ?  146 ASN A C     1 
ATOM   1210  O  O     . ASN A 1 146 ? 123.285 144.902 86.710  1.00 30.46 ?  146 ASN A O     1 
ATOM   1211  C  CB    . ASN A 1 146 ? 122.540 147.624 85.740  1.00 25.53 ?  146 ASN A CB    1 
ATOM   1212  C  CG    . ASN A 1 146 ? 121.792 148.407 84.681  1.00 30.32 ?  146 ASN A CG    1 
ATOM   1213  O  OD1   . ASN A 1 146 ? 120.706 148.018 84.258  1.00 35.31 ?  146 ASN A OD1   1 
ATOM   1214  N  ND2   . ASN A 1 146 ? 122.375 149.517 84.245  1.00 30.38 ?  146 ASN A ND2   1 
ATOM   1215  N  N     . GLN A 1 147 ? 122.389 145.726 88.615  1.00 23.38 ?  147 GLN A N     1 
ATOM   1216  C  CA    . GLN A 1 147 ? 123.133 144.866 89.532  1.00 20.38 ?  147 GLN A CA    1 
ATOM   1217  C  C     . GLN A 1 147 ? 124.638 145.045 89.360  1.00 26.35 ?  147 GLN A C     1 
ATOM   1218  O  O     . GLN A 1 147 ? 125.415 144.104 89.523  1.00 35.68 ?  147 GLN A O     1 
ATOM   1219  C  CB    . GLN A 1 147 ? 122.727 143.400 89.370  1.00 24.70 ?  147 GLN A CB    1 
ATOM   1220  C  CG    . GLN A 1 147 ? 121.342 143.091 89.912  1.00 23.57 ?  147 GLN A CG    1 
ATOM   1221  C  CD    . GLN A 1 147 ? 121.170 141.632 90.273  1.00 26.46 ?  147 GLN A CD    1 
ATOM   1222  O  OE1   . GLN A 1 147 ? 120.533 141.299 91.272  1.00 28.11 ?  147 GLN A OE1   1 
ATOM   1223  N  NE2   . GLN A 1 147 ? 121.740 140.751 89.461  1.00 35.92 ?  147 GLN A NE2   1 
ATOM   1224  N  N     . GLU A 1 148 ? 125.050 146.267 89.021  1.00 25.21 ?  148 GLU A N     1 
ATOM   1225  C  CA    . GLU A 1 148 ? 126.471 146.583 88.960  1.00 22.94 ?  148 GLU A CA    1 
ATOM   1226  C  C     . GLU A 1 148 ? 127.053 146.785 90.351  1.00 24.69 ?  148 GLU A C     1 
ATOM   1227  O  O     . GLU A 1 148 ? 128.184 146.372 90.624  1.00 29.83 ?  148 GLU A O     1 
ATOM   1228  C  CB    . GLU A 1 148 ? 126.695 147.829 88.103  1.00 20.80 ?  148 GLU A CB    1 
ATOM   1229  C  CG    . GLU A 1 148 ? 126.211 147.692 86.672  1.00 24.20 ?  148 GLU A CG    1 
ATOM   1230  C  CD    . GLU A 1 148 ? 126.102 149.027 85.965  1.00 33.09 ?  148 GLU A CD    1 
ATOM   1231  O  OE1   . GLU A 1 148 ? 125.097 149.735 86.182  1.00 36.31 ?  148 GLU A OE1   1 
ATOM   1232  O  OE2   . GLU A 1 148 ? 127.022 149.370 85.194  1.00 36.13 -1 148 GLU A OE2   1 
ATOM   1233  N  N     . TYR A 1 149 ? 126.293 147.411 91.243  1.00 18.43 ?  149 TYR A N     1 
ATOM   1234  C  CA    . TYR A 1 149 ? 126.718 147.649 92.612  1.00 20.58 ?  149 TYR A CA    1 
ATOM   1235  C  C     . TYR A 1 149 ? 125.657 147.128 93.564  1.00 22.59 ?  149 TYR A C     1 
ATOM   1236  O  O     . TYR A 1 149 ? 124.457 147.238 93.293  1.00 30.54 ?  149 TYR A O     1 
ATOM   1237  C  CB    . TYR A 1 149 ? 126.971 149.136 92.867  1.00 22.04 ?  149 TYR A CB    1 
ATOM   1238  C  CG    . TYR A 1 149 ? 127.139 149.489 94.326  1.00 21.96 ?  149 TYR A CG    1 
ATOM   1239  C  CD1   . TYR A 1 149 ? 128.224 149.020 95.053  1.00 17.07 ?  149 TYR A CD1   1 
ATOM   1240  C  CD2   . TYR A 1 149 ? 126.210 150.290 94.976  1.00 19.77 ?  149 TYR A CD2   1 
ATOM   1241  C  CE1   . TYR A 1 149 ? 128.379 149.341 96.387  1.00 22.13 ?  149 TYR A CE1   1 
ATOM   1242  C  CE2   . TYR A 1 149 ? 126.358 150.617 96.307  1.00 17.50 ?  149 TYR A CE2   1 
ATOM   1243  C  CZ    . TYR A 1 149 ? 127.444 150.139 97.008  1.00 19.19 ?  149 TYR A CZ    1 
ATOM   1244  O  OH    . TYR A 1 149 ? 127.595 150.461 98.336  1.00 20.73 ?  149 TYR A OH    1 
ATOM   1245  N  N     . GLN A 1 150 ? 126.103 146.560 94.677  1.00 19.43 ?  150 GLN A N     1 
ATOM   1246  C  CA    . GLN A 1 150 ? 125.214 146.003 95.690  1.00 14.05 ?  150 GLN A CA    1 
ATOM   1247  C  C     . GLN A 1 150 ? 125.618 146.571 97.041  1.00 17.22 ?  150 GLN A C     1 
ATOM   1248  O  O     . GLN A 1 150 ? 126.744 146.302 97.509  1.00 18.47 ?  150 GLN A O     1 
ATOM   1249  C  CB    . GLN A 1 150 ? 125.282 144.478 95.688  1.00 19.49 ?  150 GLN A CB    1 
ATOM   1250  C  CG    . GLN A 1 150 ? 124.566 143.801 96.840  1.00 20.50 ?  150 GLN A CG    1 
ATOM   1251  C  CD    . GLN A 1 150 ? 123.109 144.201 96.941  1.00 17.04 ?  150 GLN A CD    1 
ATOM   1252  O  OE1   . GLN A 1 150 ? 122.306 143.891 96.062  1.00 22.92 ?  150 GLN A OE1   1 
ATOM   1253  N  NE2   . GLN A 1 150 ? 122.761 144.891 98.017  1.00 19.47 ?  150 GLN A NE2   1 
ATOM   1254  N  N     . PRO A 1 151 ? 124.771 147.375 97.679  1.00 24.37 ?  151 PRO A N     1 
ATOM   1255  C  CA    . PRO A 1 151 ? 125.037 147.757 99.068  1.00 10.14 ?  151 PRO A CA    1 
ATOM   1256  C  C     . PRO A 1 151 ? 125.041 146.525 99.957  1.00 13.12 ?  151 PRO A C     1 
ATOM   1257  O  O     . PRO A 1 151 ? 124.379 145.526 99.672  1.00 25.36 ?  151 PRO A O     1 
ATOM   1258  C  CB    . PRO A 1 151 ? 123.877 148.698 99.411  1.00 19.55 ?  151 PRO A CB    1 
ATOM   1259  C  CG    . PRO A 1 151 ? 123.356 149.167 98.094  1.00 19.21 ?  151 PRO A CG    1 
ATOM   1260  C  CD    . PRO A 1 151 ? 123.572 148.035 97.141  1.00 19.61 ?  151 PRO A CD    1 
ATOM   1261  N  N     . SER A 1 152 ? 125.815 146.599 101.036 1.00 23.35 ?  152 SER A N     1 
ATOM   1262  C  CA    . SER A 1 152 ? 125.946 145.470 101.940 1.00 19.59 ?  152 SER A CA    1 
ATOM   1263  C  C     . SER A 1 152 ? 124.587 145.089 102.526 1.00 22.03 ?  152 SER A C     1 
ATOM   1264  O  O     . SER A 1 152 ? 123.602 145.823 102.425 1.00 27.11 ?  152 SER A O     1 
ATOM   1265  C  CB    . SER A 1 152 ? 126.929 145.797 103.060 1.00 19.84 ?  152 SER A CB    1 
ATOM   1266  O  OG    . SER A 1 152 ? 126.440 146.850 103.869 1.00 23.90 ?  152 SER A OG    1 
ATOM   1267  N  N     . THR A 1 153 ? 124.549 143.912 103.147 1.00 26.99 ?  153 THR A N     1 
ATOM   1268  C  CA    . THR A 1 153 ? 123.324 143.448 103.790 1.00 21.18 ?  153 THR A CA    1 
ATOM   1269  C  C     . THR A 1 153 ? 122.738 144.459 104.770 1.00 30.64 ?  153 THR A C     1 
ATOM   1270  O  O     . THR A 1 153 ? 121.518 144.692 104.708 1.00 32.29 ?  153 THR A O     1 
ATOM   1271  C  CB    . THR A 1 153 ? 123.581 142.099 104.481 1.00 26.27 ?  153 THR A CB    1 
ATOM   1272  O  OG1   . THR A 1 153 ? 123.750 141.077 103.491 1.00 31.38 ?  153 THR A OG1   1 
ATOM   1273  C  CG2   . THR A 1 153 ? 122.422 141.728 105.394 1.00 25.56 ?  153 THR A CG2   1 
ATOM   1274  N  N     . PRO A 1 154 ? 123.508 145.098 105.661 1.00 28.10 ?  154 PRO A N     1 
ATOM   1275  C  CA    . PRO A 1 154 ? 122.899 146.144 106.505 1.00 20.25 ?  154 PRO A CA    1 
ATOM   1276  C  C     . PRO A 1 154 ? 122.308 147.289 105.700 1.00 20.45 ?  154 PRO A C     1 
ATOM   1277  O  O     . PRO A 1 154 ? 121.148 147.663 105.916 1.00 28.25 ?  154 PRO A O     1 
ATOM   1278  C  CB    . PRO A 1 154 ? 124.070 146.610 107.380 1.00 22.33 ?  154 PRO A CB    1 
ATOM   1279  C  CG    . PRO A 1 154 ? 125.027 145.497 107.362 1.00 18.21 ?  154 PRO A CG    1 
ATOM   1280  C  CD    . PRO A 1 154 ? 124.917 144.864 106.026 1.00 19.76 ?  154 PRO A CD    1 
ATOM   1281  N  N     . THR A 1 155 ? 123.078 147.853 104.770 1.00 21.90 ?  155 THR A N     1 
ATOM   1282  C  CA    . THR A 1 155 ? 122.585 148.977 103.980 1.00 22.24 ?  155 THR A CA    1 
ATOM   1283  C  C     . THR A 1 155 ? 121.404 148.561 103.111 1.00 24.01 ?  155 THR A C     1 
ATOM   1284  O  O     . THR A 1 155 ? 120.369 149.234 103.091 1.00 25.79 ?  155 THR A O     1 
ATOM   1285  C  CB    . THR A 1 155 ? 123.711 149.546 103.117 1.00 20.44 ?  155 THR A CB    1 
ATOM   1286  O  OG1   . THR A 1 155 ? 124.867 149.780 103.930 1.00 26.23 ?  155 THR A OG1   1 
ATOM   1287  C  CG2   . THR A 1 155 ? 123.276 150.853 102.479 1.00 15.83 ?  155 THR A CG2   1 
ATOM   1288  N  N     . PHE A 1 156 ? 121.538 147.446 102.392 1.00 26.18 ?  156 PHE A N     1 
ATOM   1289  C  CA    . PHE A 1 156 ? 120.474 147.023 101.486 1.00 22.55 ?  156 PHE A CA    1 
ATOM   1290  C  C     . PHE A 1 156 ? 119.196 146.693 102.245 1.00 29.74 ?  156 PHE A C     1 
ATOM   1291  O  O     . PHE A 1 156 ? 118.093 147.028 101.794 1.00 25.60 ?  156 PHE A O     1 
ATOM   1292  C  CB    . PHE A 1 156 ? 120.932 145.820 100.664 1.00 21.93 ?  156 PHE A CB    1 
ATOM   1293  C  CG    . PHE A 1 156 ? 120.080 145.554 99.459  1.00 27.63 ?  156 PHE A CG    1 
ATOM   1294  C  CD1   . PHE A 1 156 ? 119.876 146.539 98.509  1.00 24.70 ?  156 PHE A CD1   1 
ATOM   1295  C  CD2   . PHE A 1 156 ? 119.481 144.319 99.276  1.00 23.84 ?  156 PHE A CD2   1 
ATOM   1296  C  CE1   . PHE A 1 156 ? 119.093 146.299 97.399  1.00 24.94 ?  156 PHE A CE1   1 
ATOM   1297  C  CE2   . PHE A 1 156 ? 118.697 144.073 98.169  1.00 25.17 ?  156 PHE A CE2   1 
ATOM   1298  C  CZ    . PHE A 1 156 ? 118.502 145.064 97.230  1.00 29.02 ?  156 PHE A CZ    1 
ATOM   1299  N  N     . LEU A 1 157 ? 119.319 146.034 103.397 1.00 29.89 ?  157 LEU A N     1 
ATOM   1300  C  CA    . LEU A 1 157 ? 118.145 145.611 104.150 1.00 24.18 ?  157 LEU A CA    1 
ATOM   1301  C  C     . LEU A 1 157 ? 117.488 146.769 104.893 1.00 27.71 ?  157 LEU A C     1 
ATOM   1302  O  O     . LEU A 1 157 ? 116.256 146.845 104.953 1.00 38.07 ?  157 LEU A O     1 
ATOM   1303  C  CB    . LEU A 1 157 ? 118.535 144.502 105.127 1.00 29.60 ?  157 LEU A CB    1 
ATOM   1304  C  CG    . LEU A 1 157 ? 117.525 144.133 106.213 1.00 30.16 ?  157 LEU A CG    1 
ATOM   1305  C  CD1   . LEU A 1 157 ? 116.501 143.154 105.676 1.00 31.34 ?  157 LEU A CD1   1 
ATOM   1306  C  CD2   . LEU A 1 157 ? 118.235 143.553 107.426 1.00 25.42 ?  157 LEU A CD2   1 
ATOM   1307  N  N     . ASN A 1 158 ? 118.281 147.682 105.453 1.00 29.43 ?  158 ASN A N     1 
ATOM   1308  C  CA    . ASN A 1 158 ? 117.766 148.641 106.419 1.00 28.29 ?  158 ASN A CA    1 
ATOM   1309  C  C     . ASN A 1 158 ? 117.601 150.053 105.872 1.00 29.21 ?  158 ASN A C     1 
ATOM   1310  O  O     . ASN A 1 158 ? 116.990 150.884 106.549 1.00 35.75 ?  158 ASN A O     1 
ATOM   1311  C  CB    . ASN A 1 158 ? 118.682 148.684 107.647 1.00 28.05 ?  158 ASN A CB    1 
ATOM   1312  C  CG    . ASN A 1 158 ? 118.692 147.377 108.410 1.00 33.65 ?  158 ASN A CG    1 
ATOM   1313  O  OD1   . ASN A 1 158 ? 117.646 146.781 108.657 1.00 37.04 ?  158 ASN A OD1   1 
ATOM   1314  N  ND2   . ASN A 1 158 ? 119.881 146.921 108.781 1.00 34.74 ?  158 ASN A ND2   1 
ATOM   1315  N  N     . ALA A 1 159 ? 118.124 150.354 104.686 1.00 27.74 ?  159 ALA A N     1 
ATOM   1316  C  CA    . ALA A 1 159 ? 118.037 151.716 104.170 1.00 27.63 ?  159 ALA A CA    1 
ATOM   1317  C  C     . ALA A 1 159 ? 116.583 152.112 103.960 1.00 33.43 ?  159 ALA A C     1 
ATOM   1318  O  O     . ALA A 1 159 ? 115.837 151.427 103.254 1.00 39.61 ?  159 ALA A O     1 
ATOM   1319  C  CB    . ALA A 1 159 ? 118.815 151.846 102.862 1.00 29.21 ?  159 ALA A CB    1 
ATOM   1320  N  N     . GLY A 1 160 ? 116.185 153.221 104.577 1.00 36.32 ?  160 GLY A N     1 
ATOM   1321  C  CA    . GLY A 1 160 ? 114.838 153.727 104.446 1.00 36.92 ?  160 GLY A CA    1 
ATOM   1322  C  C     . GLY A 1 160 ? 113.807 153.082 105.344 1.00 39.04 ?  160 GLY A C     1 
ATOM   1323  O  O     . GLY A 1 160 ? 112.619 153.393 105.208 1.00 44.26 ?  160 GLY A O     1 
ATOM   1324  N  N     . ARG A 1 161 ? 114.212 152.200 106.252 1.00 41.42 ?  161 ARG A N     1 
ATOM   1325  C  CA    . ARG A 1 161 ? 113.287 151.497 107.132 1.00 41.58 ?  161 ARG A CA    1 
ATOM   1326  C  C     . ARG A 1 161 ? 113.376 152.068 108.541 1.00 43.09 ?  161 ARG A C     1 
ATOM   1327  O  O     . ARG A 1 161 ? 114.476 152.270 109.063 1.00 45.61 ?  161 ARG A O     1 
ATOM   1328  C  CB    . ARG A 1 161 ? 113.588 149.999 107.152 1.00 37.99 ?  161 ARG A CB    1 
ATOM   1329  C  CG    . ARG A 1 161 ? 113.295 149.288 105.845 1.00 40.07 ?  161 ARG A CG    1 
ATOM   1330  C  CD    . ARG A 1 161 ? 113.206 147.786 106.047 1.00 39.67 ?  161 ARG A CD    1 
ATOM   1331  N  NE    . ARG A 1 161 ? 113.216 147.065 104.780 1.00 42.62 ?  161 ARG A NE    1 
ATOM   1332  C  CZ    . ARG A 1 161 ? 113.375 145.754 104.667 1.00 43.82 ?  161 ARG A CZ    1 
ATOM   1333  N  NH1   . ARG A 1 161 ? 113.528 144.981 105.730 1.00 39.86 1  161 ARG A NH1   1 
ATOM   1334  N  NH2   . ARG A 1 161 ? 113.381 145.203 103.457 1.00 43.40 ?  161 ARG A NH2   1 
ATOM   1335  N  N     . LYS A 1 162 ? 112.217 152.329 109.151 1.00 48.38 ?  162 LYS A N     1 
ATOM   1336  C  CA    . LYS A 1 162 ? 112.202 152.862 110.510 1.00 50.04 ?  162 LYS A CA    1 
ATOM   1337  C  C     . LYS A 1 162 ? 112.605 151.797 111.524 1.00 49.96 ?  162 LYS A C     1 
ATOM   1338  O  O     . LYS A 1 162 ? 113.409 152.057 112.427 1.00 51.28 ?  162 LYS A O     1 
ATOM   1339  C  CB    . LYS A 1 162 ? 110.819 153.426 110.840 1.00 49.53 ?  162 LYS A CB    1 
ATOM   1340  C  CG    . LYS A 1 162 ? 110.777 154.240 112.124 1.00 48.91 ?  162 LYS A CG    1 
ATOM   1341  C  CD    . LYS A 1 162 ? 110.092 155.582 111.917 1.00 49.75 ?  162 LYS A CD    1 
ATOM   1342  C  CE    . LYS A 1 162 ? 108.693 155.410 111.353 1.00 52.02 ?  162 LYS A CE    1 
ATOM   1343  N  NZ    . LYS A 1 162 ? 108.312 156.534 110.455 1.00 52.03 1  162 LYS A NZ    1 
ATOM   1344  N  N     . ARG A 1 163 ? 112.056 150.592 111.392 1.00 49.65 ?  163 ARG A N     1 
ATOM   1345  C  CA    . ARG A 1 163 ? 112.413 149.472 112.263 1.00 51.16 ?  163 ARG A CA    1 
ATOM   1346  C  C     . ARG A 1 163 ? 113.647 148.810 111.665 1.00 52.31 ?  163 ARG A C     1 
ATOM   1347  O  O     . ARG A 1 163 ? 113.556 147.904 110.836 1.00 53.52 ?  163 ARG A O     1 
ATOM   1348  C  CB    . ARG A 1 163 ? 111.250 148.495 112.393 1.00 53.63 ?  163 ARG A CB    1 
ATOM   1349  C  CG    . ARG A 1 163 ? 111.109 147.853 113.767 1.00 52.96 ?  163 ARG A CG    1 
ATOM   1350  C  CD    . ARG A 1 163 ? 112.239 146.879 114.066 1.00 52.96 ?  163 ARG A CD    1 
ATOM   1351  N  NE    . ARG A 1 163 ? 112.510 145.986 112.946 1.00 53.32 ?  163 ARG A NE    1 
ATOM   1352  C  CZ    . ARG A 1 163 ? 113.698 145.461 112.678 1.00 53.85 ?  163 ARG A CZ    1 
ATOM   1353  N  NH1   . ARG A 1 163 ? 114.754 145.722 113.430 1.00 53.22 1  163 ARG A NH1   1 
ATOM   1354  N  NH2   . ARG A 1 163 ? 113.828 144.655 111.628 1.00 52.27 ?  163 ARG A NH2   1 
ATOM   1355  N  N     . ARG A 1 164 ? 114.820 149.272 112.092 1.00 50.24 ?  164 ARG A N     1 
ATOM   1356  C  CA    . ARG A 1 164 ? 116.064 148.861 111.461 1.00 50.56 ?  164 ARG A CA    1 
ATOM   1357  C  C     . ARG A 1 164 ? 117.204 148.938 112.463 1.00 49.30 ?  164 ARG A C     1 
ATOM   1358  O  O     . ARG A 1 164 ? 117.123 149.627 113.482 1.00 50.46 ?  164 ARG A O     1 
ATOM   1359  C  CB    . ARG A 1 164 ? 116.387 149.737 110.248 1.00 46.90 ?  164 ARG A CB    1 
ATOM   1360  C  CG    . ARG A 1 164 ? 116.958 151.098 110.624 1.00 43.57 ?  164 ARG A CG    1 
ATOM   1361  C  CD    . ARG A 1 164 ? 117.670 151.749 109.453 1.00 46.79 ?  164 ARG A CD    1 
ATOM   1362  N  NE    . ARG A 1 164 ? 118.118 153.104 109.753 1.00 46.54 ?  164 ARG A NE    1 
ATOM   1363  C  CZ    . ARG A 1 164 ? 119.180 153.398 110.489 1.00 49.60 ?  164 ARG A CZ    1 
ATOM   1364  N  NH1   . ARG A 1 164 ? 119.931 152.453 111.029 1.00 48.82 1  164 ARG A NH1   1 
ATOM   1365  N  NH2   . ARG A 1 164 ? 119.498 154.674 110.688 1.00 47.91 ?  164 ARG A NH2   1 
ATOM   1366  N  N     . GLY A 1 165 ? 118.274 148.207 112.155 1.00 43.35 ?  165 GLY A N     1 
ATOM   1367  C  CA    . GLY A 1 165 ? 119.545 148.380 112.822 1.00 42.46 ?  165 GLY A CA    1 
ATOM   1368  C  C     . GLY A 1 165 ? 120.399 149.407 112.107 1.00 45.44 ?  165 GLY A C     1 
ATOM   1369  O  O     . GLY A 1 165 ? 119.963 150.093 111.181 1.00 46.28 ?  165 GLY A O     1 
ATOM   1370  N  N     . GLU A 1 166 ? 121.649 149.509 112.548 1.00 39.87 ?  166 GLU A N     1 
ATOM   1371  C  CA    . GLU A 1 166 ? 122.566 150.429 111.898 1.00 37.89 ?  166 GLU A CA    1 
ATOM   1372  C  C     . GLU A 1 166 ? 122.980 149.894 110.529 1.00 38.58 ?  166 GLU A C     1 
ATOM   1373  O  O     . GLU A 1 166 ? 122.975 148.688 110.272 1.00 36.64 ?  166 GLU A O     1 
ATOM   1374  C  CB    . GLU A 1 166 ? 123.800 150.669 112.769 1.00 35.65 ?  166 GLU A CB    1 
ATOM   1375  C  CG    . GLU A 1 166 ? 123.788 151.994 113.521 1.00 38.87 ?  166 GLU A CG    1 
ATOM   1376  C  CD    . GLU A 1 166 ? 123.707 153.207 112.605 1.00 45.97 ?  166 GLU A CD    1 
ATOM   1377  O  OE1   . GLU A 1 166 ? 124.060 153.091 111.411 1.00 48.15 ?  166 GLU A OE1   1 
ATOM   1378  O  OE2   . GLU A 1 166 ? 123.287 154.282 113.081 1.00 43.24 -1 166 GLU A OE2   1 
ATOM   1379  N  N     . LEU A 1 167 ? 123.342 150.821 109.641 1.00 30.76 ?  167 LEU A N     1 
ATOM   1380  C  CA    . LEU A 1 167 ? 123.782 150.458 108.302 1.00 25.60 ?  167 LEU A CA    1 
ATOM   1381  C  C     . LEU A 1 167 ? 125.215 149.949 108.269 1.00 28.67 ?  167 LEU A C     1 
ATOM   1382  O  O     . LEU A 1 167 ? 125.653 149.442 107.232 1.00 30.69 ?  167 LEU A O     1 
ATOM   1383  C  CB    . LEU A 1 167 ? 123.641 151.654 107.362 1.00 26.21 ?  167 LEU A CB    1 
ATOM   1384  C  CG    . LEU A 1 167 ? 122.222 152.164 107.119 1.00 25.34 ?  167 LEU A CG    1 
ATOM   1385  C  CD1   . LEU A 1 167 ? 122.204 153.107 105.941 1.00 27.51 ?  167 LEU A CD1   1 
ATOM   1386  C  CD2   . LEU A 1 167 ? 121.273 151.008 106.885 1.00 27.01 ?  167 LEU A CD2   1 
ATOM   1387  N  N     . VAL A 1 168 ? 125.948 150.078 109.370 1.00 29.92 ?  168 VAL A N     1 
ATOM   1388  C  CA    . VAL A 1 168 ? 127.299 149.546 109.496 1.00 20.10 ?  168 VAL A CA    1 
ATOM   1389  C  C     . VAL A 1 168 ? 127.238 148.326 110.401 1.00 25.75 ?  168 VAL A C     1 
ATOM   1390  O  O     . VAL A 1 168 ? 126.588 148.359 111.454 1.00 33.49 ?  168 VAL A O     1 
ATOM   1391  C  CB    . VAL A 1 168 ? 128.263 150.604 110.060 1.00 24.69 ?  168 VAL A CB    1 
ATOM   1392  C  CG1   . VAL A 1 168 ? 129.677 150.050 110.132 1.00 29.31 ?  168 VAL A CG1   1 
ATOM   1393  C  CG2   . VAL A 1 168 ? 128.221 151.866 109.216 1.00 27.55 ?  168 VAL A CG2   1 
ATOM   1394  N  N     . SER A 1 169 ? 127.894 147.243 109.988 1.00 26.07 ?  169 SER A N     1 
ATOM   1395  C  CA    . SER A 1 169 ? 127.937 146.032 110.792 1.00 29.38 ?  169 SER A CA    1 
ATOM   1396  C  C     . SER A 1 169 ? 129.343 145.528 111.071 1.00 32.50 ?  169 SER A C     1 
ATOM   1397  O  O     . SER A 1 169 ? 129.489 144.476 111.703 1.00 38.92 ?  169 SER A O     1 
ATOM   1398  C  CB    . SER A 1 169 ? 127.119 144.914 110.132 1.00 30.68 ?  169 SER A CB    1 
ATOM   1399  O  OG    . SER A 1 169 ? 125.734 145.108 110.359 1.00 38.06 ?  169 SER A OG    1 
ATOM   1400  N  N     . CYS A 1 170 ? 130.377 146.229 110.622 1.00 26.32 ?  170 CYS A N     1 
ATOM   1401  C  CA    . CYS A 1 170 ? 131.749 145.902 110.982 1.00 24.16 ?  170 CYS A CA    1 
ATOM   1402  C  C     . CYS A 1 170 ? 132.277 147.000 111.897 1.00 23.58 ?  170 CYS A C     1 
ATOM   1403  O  O     . CYS A 1 170 ? 132.342 148.169 111.503 1.00 26.85 ?  170 CYS A O     1 
ATOM   1404  C  CB    . CYS A 1 170 ? 132.625 145.718 109.739 1.00 30.30 ?  170 CYS A CB    1 
ATOM   1405  S  SG    . CYS A 1 170 ? 133.038 147.200 108.789 1.00 48.74 ?  170 CYS A SG    1 
ATOM   1406  N  N     . PHE A 1 171 ? 132.612 146.624 113.127 1.00 23.10 ?  171 PHE A N     1 
ATOM   1407  C  CA    . PHE A 1 171 ? 133.110 147.554 114.129 1.00 10.69 ?  171 PHE A CA    1 
ATOM   1408  C  C     . PHE A 1 171 ? 134.377 146.986 114.739 1.00 15.01 ?  171 PHE A C     1 
ATOM   1409  O  O     . PHE A 1 171 ? 134.422 145.809 115.107 1.00 22.56 ?  171 PHE A O     1 
ATOM   1410  C  CB    . PHE A 1 171 ? 132.067 147.811 115.220 1.00 15.76 ?  171 PHE A CB    1 
ATOM   1411  C  CG    . PHE A 1 171 ? 130.783 148.384 114.704 1.00 17.29 ?  171 PHE A CG    1 
ATOM   1412  C  CD1   . PHE A 1 171 ? 130.715 149.707 114.311 1.00 19.36 ?  171 PHE A CD1   1 
ATOM   1413  C  CD2   . PHE A 1 171 ? 129.645 147.602 114.614 1.00 15.63 ?  171 PHE A CD2   1 
ATOM   1414  C  CE1   . PHE A 1 171 ? 129.539 150.239 113.832 1.00 14.98 ?  171 PHE A CE1   1 
ATOM   1415  C  CE2   . PHE A 1 171 ? 128.465 148.131 114.138 1.00 16.79 ?  171 PHE A CE2   1 
ATOM   1416  C  CZ    . PHE A 1 171 ? 128.412 149.451 113.747 1.00 16.17 ?  171 PHE A CZ    1 
ATOM   1417  N  N     . LEU A 1 172 ? 135.405 147.822 114.840 1.00 14.71 ?  172 LEU A N     1 
ATOM   1418  C  CA    . LEU A 1 172 ? 136.667 147.445 115.453 1.00 9.06  ?  172 LEU A CA    1 
ATOM   1419  C  C     . LEU A 1 172 ? 136.885 148.315 116.678 1.00 13.65 ?  172 LEU A C     1 
ATOM   1420  O  O     . LEU A 1 172 ? 136.874 149.546 116.577 1.00 16.89 ?  172 LEU A O     1 
ATOM   1421  C  CB    . LEU A 1 172 ? 137.830 147.601 114.471 1.00 14.71 ?  172 LEU A CB    1 
ATOM   1422  C  CG    . LEU A 1 172 ? 137.946 146.584 113.336 1.00 6.10  ?  172 LEU A CG    1 
ATOM   1423  C  CD1   . LEU A 1 172 ? 136.979 146.915 112.213 1.00 8.62  ?  172 LEU A CD1   1 
ATOM   1424  C  CD2   . LEU A 1 172 ? 139.369 146.545 112.821 1.00 13.30 ?  172 LEU A CD2   1 
ATOM   1425  N  N     . LEU A 1 173 ? 137.082 147.681 117.827 1.00 16.08 ?  173 LEU A N     1 
ATOM   1426  C  CA    . LEU A 1 173 ? 137.258 148.384 119.087 1.00 12.47 ?  173 LEU A CA    1 
ATOM   1427  C  C     . LEU A 1 173 ? 138.660 148.157 119.627 1.00 11.97 ?  173 LEU A C     1 
ATOM   1428  O  O     . LEU A 1 173 ? 139.183 147.039 119.583 1.00 16.59 ?  173 LEU A O     1 
ATOM   1429  C  CB    . LEU A 1 173 ? 136.232 147.928 120.126 1.00 16.96 ?  173 LEU A CB    1 
ATOM   1430  C  CG    . LEU A 1 173 ? 134.756 147.944 119.738 1.00 20.16 ?  173 LEU A CG    1 
ATOM   1431  C  CD1   . LEU A 1 173 ? 133.908 147.584 120.945 1.00 19.08 ?  173 LEU A CD1   1 
ATOM   1432  C  CD2   . LEU A 1 173 ? 134.352 149.296 119.174 1.00 16.49 ?  173 LEU A CD2   1 
ATOM   1433  N  N     . GLU A 1 174 ? 139.267 149.225 120.128 1.00 25.98 ?  174 GLU A N     1 
ATOM   1434  C  CA    . GLU A 1 174 ? 140.507 149.132 120.880 1.00 23.68 ?  174 GLU A CA    1 
ATOM   1435  C  C     . GLU A 1 174 ? 140.190 149.108 122.368 1.00 20.40 ?  174 GLU A C     1 
ATOM   1436  O  O     . GLU A 1 174 ? 139.435 149.947 122.866 1.00 29.43 ?  174 GLU A O     1 
ATOM   1437  C  CB    . GLU A 1 174 ? 141.427 150.310 120.557 1.00 26.29 ?  174 GLU A CB    1 
ATOM   1438  C  CG    . GLU A 1 174 ? 141.911 150.349 119.121 1.00 22.14 ?  174 GLU A CG    1 
ATOM   1439  C  CD    . GLU A 1 174 ? 143.315 149.803 118.969 1.00 25.00 ?  174 GLU A CD    1 
ATOM   1440  O  OE1   . GLU A 1 174 ? 143.953 149.508 120.000 1.00 28.05 ?  174 GLU A OE1   1 
ATOM   1441  O  OE2   . GLU A 1 174 ? 143.781 149.670 117.819 1.00 28.48 -1 174 GLU A OE2   1 
ATOM   1442  N  N     . VAL A 1 175 ? 140.765 148.141 123.073 1.00 19.84 ?  175 VAL A N     1 
ATOM   1443  C  CA    . VAL A 1 175 ? 140.547 147.974 124.505 1.00 20.81 ?  175 VAL A CA    1 
ATOM   1444  C  C     . VAL A 1 175 ? 141.838 148.331 125.226 1.00 18.94 ?  175 VAL A C     1 
ATOM   1445  O  O     . VAL A 1 175 ? 142.879 147.703 124.999 1.00 26.83 ?  175 VAL A O     1 
ATOM   1446  C  CB    . VAL A 1 175 ? 140.098 146.546 124.850 1.00 22.21 ?  175 VAL A CB    1 
ATOM   1447  C  CG1   . VAL A 1 175 ? 139.579 146.482 126.277 1.00 14.41 ?  175 VAL A CG1   1 
ATOM   1448  C  CG2   . VAL A 1 175 ? 139.040 146.071 123.867 1.00 19.87 ?  175 VAL A CG2   1 
ATOM   1449  N  N     . ASN A 1 176 ? 141.771 149.338 126.091 1.00 18.41 ?  176 ASN A N     1 
ATOM   1450  C  CA    . ASN A 1 176 ? 142.926 149.728 126.879 1.00 20.00 ?  176 ASN A CA    1 
ATOM   1451  C  C     . ASN A 1 176 ? 143.042 148.850 128.121 1.00 23.60 ?  176 ASN A C     1 
ATOM   1452  O  O     . ASN A 1 176 ? 142.080 148.215 128.561 1.00 24.22 ?  176 ASN A O     1 
ATOM   1453  C  CB    . ASN A 1 176 ? 142.834 151.202 127.272 1.00 18.83 ?  176 ASN A CB    1 
ATOM   1454  C  CG    . ASN A 1 176 ? 144.182 151.887 127.284 1.00 21.31 ?  176 ASN A CG    1 
ATOM   1455  O  OD1   . ASN A 1 176 ? 145.215 151.245 127.474 1.00 27.96 ?  176 ASN A OD1   1 
ATOM   1456  N  ND2   . ASN A 1 176 ? 144.181 153.197 127.077 1.00 20.44 ?  176 ASN A ND2   1 
ATOM   1457  N  N     . ASP A 1 177 ? 144.246 148.827 128.694 1.00 23.65 ?  177 ASP A N     1 
ATOM   1458  C  CA    . ASP A 1 177 ? 144.569 147.923 129.797 1.00 20.06 ?  177 ASP A CA    1 
ATOM   1459  C  C     . ASP A 1 177 ? 144.082 148.526 131.112 1.00 24.85 ?  177 ASP A C     1 
ATOM   1460  O  O     . ASP A 1 177 ? 144.850 149.048 131.924 1.00 35.39 ?  177 ASP A O     1 
ATOM   1461  C  CB    . ASP A 1 177 ? 146.065 147.642 129.829 1.00 19.80 ?  177 ASP A CB    1 
ATOM   1462  C  CG    . ASP A 1 177 ? 146.427 146.541 130.798 1.00 25.30 ?  177 ASP A CG    1 
ATOM   1463  O  OD1   . ASP A 1 177 ? 145.691 145.535 130.862 1.00 28.44 ?  177 ASP A OD1   1 
ATOM   1464  O  OD2   . ASP A 1 177 ? 147.453 146.682 131.496 1.00 31.09 -1 177 ASP A OD2   1 
ATOM   1465  N  N     . SER A 1 178 ? 142.771 148.444 131.322 1.00 20.57 ?  178 SER A N     1 
ATOM   1466  C  CA    . SER A 1 178 ? 142.169 148.894 132.569 1.00 17.37 ?  178 SER A CA    1 
ATOM   1467  C  C     . SER A 1 178 ? 140.810 148.230 132.722 1.00 17.74 ?  178 SER A C     1 
ATOM   1468  O  O     . SER A 1 178 ? 140.203 147.785 131.745 1.00 27.43 ?  178 SER A O     1 
ATOM   1469  C  CB    . SER A 1 178 ? 142.033 150.420 132.614 1.00 16.60 ?  178 SER A CB    1 
ATOM   1470  O  OG    . SER A 1 178 ? 140.775 150.837 132.119 1.00 20.62 ?  178 SER A OG    1 
ATOM   1471  N  N     . LEU A 1 179 ? 140.342 148.164 133.970 1.00 22.74 ?  179 LEU A N     1 
ATOM   1472  C  CA    . LEU A 1 179 ? 139.017 147.609 134.229 1.00 19.48 ?  179 LEU A CA    1 
ATOM   1473  C  C     . LEU A 1 179 ? 137.924 148.515 133.681 1.00 18.74 ?  179 LEU A C     1 
ATOM   1474  O  O     . LEU A 1 179 ? 136.913 148.033 133.160 1.00 22.22 ?  179 LEU A O     1 
ATOM   1475  C  CB    . LEU A 1 179 ? 138.821 147.382 135.727 1.00 26.25 ?  179 LEU A CB    1 
ATOM   1476  C  CG    . LEU A 1 179 ? 137.579 146.568 136.098 1.00 18.81 ?  179 LEU A CG    1 
ATOM   1477  C  CD1   . LEU A 1 179 ? 137.790 145.098 135.777 1.00 21.68 ?  179 LEU A CD1   1 
ATOM   1478  C  CD2   . LEU A 1 179 ? 137.222 146.759 137.561 1.00 18.45 ?  179 LEU A CD2   1 
ATOM   1479  N  N     . ASN A 1 180 ? 138.107 149.833 133.797 1.00 21.73 ?  180 ASN A N     1 
ATOM   1480  C  CA    . ASN A 1 180 ? 137.152 150.768 133.212 1.00 19.79 ?  180 ASN A CA    1 
ATOM   1481  C  C     . ASN A 1 180 ? 137.069 150.590 131.703 1.00 20.72 ?  180 ASN A C     1 
ATOM   1482  O  O     . ASN A 1 180 ? 135.974 150.562 131.130 1.00 24.18 ?  180 ASN A O     1 
ATOM   1483  C  CB    . ASN A 1 180 ? 137.545 152.204 133.556 1.00 21.19 ?  180 ASN A CB    1 
ATOM   1484  C  CG    . ASN A 1 180 ? 137.128 152.605 134.953 1.00 26.79 ?  180 ASN A CG    1 
ATOM   1485  O  OD1   . ASN A 1 180 ? 136.139 152.104 135.488 1.00 33.12 ?  180 ASN A OD1   1 
ATOM   1486  N  ND2   . ASN A 1 180 ? 137.883 153.515 135.555 1.00 26.38 ?  180 ASN A ND2   1 
ATOM   1487  N  N     . ASP A 1 181 ? 138.221 150.451 131.046 1.00 21.75 ?  181 ASP A N     1 
ATOM   1488  C  CA    . ASP A 1 181 ? 138.235 150.273 129.600 1.00 12.47 ?  181 ASP A CA    1 
ATOM   1489  C  C     . ASP A 1 181 ? 137.652 148.924 129.200 1.00 18.69 ?  181 ASP A C     1 
ATOM   1490  O  O     . ASP A 1 181 ? 136.971 148.821 128.178 1.00 26.03 ?  181 ASP A O     1 
ATOM   1491  C  CB    . ASP A 1 181 ? 139.658 150.429 129.068 1.00 20.67 ?  181 ASP A CB    1 
ATOM   1492  C  CG    . ASP A 1 181 ? 140.174 151.846 129.204 1.00 28.75 ?  181 ASP A CG    1 
ATOM   1493  O  OD1   . ASP A 1 181 ? 139.615 152.746 128.547 1.00 31.69 ?  181 ASP A OD1   1 
ATOM   1494  O  OD2   . ASP A 1 181 ? 141.140 152.060 129.966 1.00 29.88 -1 181 ASP A OD2   1 
ATOM   1495  N  N     . ILE A 1 182 ? 137.899 147.881 129.993 1.00 20.59 ?  182 ILE A N     1 
ATOM   1496  C  CA    . ILE A 1 182 ? 137.331 146.571 129.690 1.00 17.82 ?  182 ILE A CA    1 
ATOM   1497  C  C     . ILE A 1 182 ? 135.812 146.599 129.822 1.00 19.62 ?  182 ILE A C     1 
ATOM   1498  O  O     . ILE A 1 182 ? 135.088 146.068 128.969 1.00 25.76 ?  182 ILE A O     1 
ATOM   1499  C  CB    . ILE A 1 182 ? 137.967 145.498 130.591 1.00 18.58 ?  182 ILE A CB    1 
ATOM   1500  C  CG1   . ILE A 1 182 ? 139.351 145.127 130.060 1.00 20.04 ?  182 ILE A CG1   1 
ATOM   1501  C  CG2   . ILE A 1 182 ? 137.079 144.266 130.683 1.00 21.02 ?  182 ILE A CG2   1 
ATOM   1502  C  CD1   . ILE A 1 182 ? 140.192 144.373 131.044 1.00 21.69 ?  182 ILE A CD1   1 
ATOM   1503  N  N     . SER A 1 183 ? 135.303 147.219 130.888 1.00 20.91 ?  183 SER A N     1 
ATOM   1504  C  CA    . SER A 1 183 ? 133.858 147.328 131.060 1.00 19.31 ?  183 SER A CA    1 
ATOM   1505  C  C     . SER A 1 183 ? 133.233 148.171 129.956 1.00 23.27 ?  183 SER A C     1 
ATOM   1506  O  O     . SER A 1 183 ? 132.157 147.839 129.446 1.00 25.87 ?  183 SER A O     1 
ATOM   1507  C  CB    . SER A 1 183 ? 133.538 147.915 132.434 1.00 19.40 ?  183 SER A CB    1 
ATOM   1508  O  OG    . SER A 1 183 ? 134.016 149.243 132.545 1.00 29.39 ?  183 SER A OG    1 
ATOM   1509  N  N     . ARG A 1 184 ? 133.896 149.264 129.570 1.00 25.20 ?  184 ARG A N     1 
ATOM   1510  C  CA    . ARG A 1 184 ? 133.391 150.081 128.473 1.00 19.46 ?  184 ARG A CA    1 
ATOM   1511  C  C     . ARG A 1 184 ? 133.406 149.312 127.159 1.00 23.51 ?  184 ARG A C     1 
ATOM   1512  O  O     . ARG A 1 184 ? 132.496 149.462 126.341 1.00 28.66 ?  184 ARG A O     1 
ATOM   1513  C  CB    . ARG A 1 184 ? 134.206 151.367 128.355 1.00 15.25 ?  184 ARG A CB    1 
ATOM   1514  C  CG    . ARG A 1 184 ? 133.716 152.306 127.269 1.00 24.35 ?  184 ARG A CG    1 
ATOM   1515  C  CD    . ARG A 1 184 ? 132.244 152.625 127.434 1.00 24.56 ?  184 ARG A CD    1 
ATOM   1516  N  NE    . ARG A 1 184 ? 132.027 153.714 128.377 1.00 32.26 ?  184 ARG A NE    1 
ATOM   1517  C  CZ    . ARG A 1 184 ? 130.934 153.860 129.112 1.00 29.75 ?  184 ARG A CZ    1 
ATOM   1518  N  NH1   . ARG A 1 184 ? 129.934 152.997 129.042 1.00 25.23 1  184 ARG A NH1   1 
ATOM   1519  N  NH2   . ARG A 1 184 ? 130.841 154.897 129.938 1.00 26.89 ?  184 ARG A NH2   1 
ATOM   1520  N  N     . ALA A 1 185 ? 134.432 148.488 126.936 1.00 24.15 ?  185 ALA A N     1 
ATOM   1521  C  CA    . ALA A 1 185 ? 134.478 147.667 125.733 1.00 16.96 ?  185 ALA A CA    1 
ATOM   1522  C  C     . ALA A 1 185 ? 133.340 146.657 125.713 1.00 20.26 ?  185 ALA A C     1 
ATOM   1523  O  O     . ALA A 1 185 ? 132.721 146.433 124.669 1.00 23.61 ?  185 ALA A O     1 
ATOM   1524  C  CB    . ALA A 1 185 ? 135.827 146.957 125.633 1.00 16.52 ?  185 ALA A CB    1 
ATOM   1525  N  N     . ILE A 1 186 ? 133.050 146.041 126.861 1.00 23.68 ?  186 ILE A N     1 
ATOM   1526  C  CA    . ILE A 1 186 ? 131.921 145.116 126.948 1.00 20.75 ?  186 ILE A CA    1 
ATOM   1527  C  C     . ILE A 1 186 ? 130.617 145.843 126.639 1.00 20.06 ?  186 ILE A C     1 
ATOM   1528  O  O     . ILE A 1 186 ? 129.769 145.352 125.880 1.00 27.89 ?  186 ILE A O     1 
ATOM   1529  C  CB    . ILE A 1 186 ? 131.879 144.448 128.335 1.00 26.09 ?  186 ILE A CB    1 
ATOM   1530  C  CG1   . ILE A 1 186 ? 133.075 143.514 128.520 1.00 24.61 ?  186 ILE A CG1   1 
ATOM   1531  C  CG2   . ILE A 1 186 ? 130.574 143.691 128.531 1.00 24.04 ?  186 ILE A CG2   1 
ATOM   1532  C  CD1   . ILE A 1 186 ? 133.430 143.271 129.968 1.00 23.67 ?  186 ILE A CD1   1 
ATOM   1533  N  N     . ASP A 1 187 ? 130.443 147.033 127.219 1.00 21.52 ?  187 ASP A N     1 
ATOM   1534  C  CA    . ASP A 1 187 ? 129.230 147.810 126.985 1.00 19.03 ?  187 ASP A CA    1 
ATOM   1535  C  C     . ASP A 1 187 ? 129.085 148.181 125.513 1.00 23.82 ?  187 ASP A C     1 
ATOM   1536  O  O     . ASP A 1 187 ? 128.003 148.045 124.932 1.00 28.16 ?  187 ASP A O     1 
ATOM   1537  C  CB    . ASP A 1 187 ? 129.241 149.066 127.856 1.00 17.96 ?  187 ASP A CB    1 
ATOM   1538  C  CG    . ASP A 1 187 ? 128.324 150.149 127.328 1.00 28.50 ?  187 ASP A CG    1 
ATOM   1539  O  OD1   . ASP A 1 187 ? 127.118 149.877 127.146 1.00 30.94 ?  187 ASP A OD1   1 
ATOM   1540  O  OD2   . ASP A 1 187 ? 128.808 151.275 127.090 1.00 34.22 -1 187 ASP A OD2   1 
ATOM   1541  N  N     . ILE A 1 188 ? 130.170 148.653 124.896 1.00 22.45 ?  188 ILE A N     1 
ATOM   1542  C  CA    . ILE A 1 188 ? 130.116 149.068 123.498 1.00 21.59 ?  188 ILE A CA    1 
ATOM   1543  C  C     . ILE A 1 188 ? 129.869 147.869 122.593 1.00 23.18 ?  188 ILE A C     1 
ATOM   1544  O  O     . ILE A 1 188 ? 129.137 147.966 121.604 1.00 27.73 ?  188 ILE A O     1 
ATOM   1545  C  CB    . ILE A 1 188 ? 131.405 149.819 123.113 1.00 22.36 ?  188 ILE A CB    1 
ATOM   1546  C  CG1   . ILE A 1 188 ? 131.526 151.122 123.903 1.00 22.66 ?  188 ILE A CG1   1 
ATOM   1547  C  CG2   . ILE A 1 188 ? 131.421 150.136 121.634 1.00 21.91 ?  188 ILE A CG2   1 
ATOM   1548  C  CD1   . ILE A 1 188 ? 132.842 151.832 123.701 1.00 22.60 ?  188 ILE A CD1   1 
ATOM   1549  N  N     . SER A 1 189 ? 130.472 146.722 122.913 1.00 18.21 ?  189 SER A N     1 
ATOM   1550  C  CA    . SER A 1 189 ? 130.211 145.511 122.147 1.00 12.23 ?  189 SER A CA    1 
ATOM   1551  C  C     . SER A 1 189 ? 128.743 145.123 122.226 1.00 19.79 ?  189 SER A C     1 
ATOM   1552  O  O     . SER A 1 189 ? 128.135 144.752 121.217 1.00 28.18 ?  189 SER A O     1 
ATOM   1553  C  CB    . SER A 1 189 ? 131.094 144.372 122.654 1.00 20.99 ?  189 SER A CB    1 
ATOM   1554  O  OG    . SER A 1 189 ? 132.459 144.744 122.656 1.00 27.35 ?  189 SER A OG    1 
ATOM   1555  N  N     . MET A 1 190 ? 128.155 145.214 123.421 1.00 25.42 ?  190 MET A N     1 
ATOM   1556  C  CA    . MET A 1 190 ? 126.734 144.916 123.569 1.00 22.32 ?  190 MET A CA    1 
ATOM   1557  C  C     . MET A 1 190 ? 125.877 145.891 122.772 1.00 18.68 ?  190 MET A C     1 
ATOM   1558  O  O     . MET A 1 190 ? 124.911 145.488 122.115 1.00 22.42 ?  190 MET A O     1 
ATOM   1559  C  CB    . MET A 1 190 ? 126.347 144.957 125.044 1.00 25.23 ?  190 MET A CB    1 
ATOM   1560  C  CG    . MET A 1 190 ? 126.663 143.691 125.804 1.00 18.79 ?  190 MET A CG    1 
ATOM   1561  S  SD    . MET A 1 190 ? 126.716 143.995 127.574 1.00 37.97 ?  190 MET A SD    1 
ATOM   1562  C  CE    . MET A 1 190 ? 125.479 142.836 128.128 1.00 27.75 ?  190 MET A CE    1 
ATOM   1563  N  N     . GLN A 1 191 ? 126.216 147.181 122.818 1.00 21.05 ?  191 GLN A N     1 
ATOM   1564  C  CA    . GLN A 1 191 ? 125.427 148.182 122.108 1.00 22.57 ?  191 GLN A CA    1 
ATOM   1565  C  C     . GLN A 1 191 ? 125.521 148.000 120.598 1.00 24.99 ?  191 GLN A C     1 
ATOM   1566  O  O     . GLN A 1 191 ? 124.533 148.192 119.881 1.00 30.62 ?  191 GLN A O     1 
ATOM   1567  C  CB    . GLN A 1 191 ? 125.873 149.591 122.502 1.00 22.31 ?  191 GLN A CB    1 
ATOM   1568  C  CG    . GLN A 1 191 ? 125.740 149.903 123.981 1.00 21.20 ?  191 GLN A CG    1 
ATOM   1569  C  CD    . GLN A 1 191 ? 124.300 150.007 124.436 1.00 27.26 ?  191 GLN A CD    1 
ATOM   1570  O  OE1   . GLN A 1 191 ? 123.395 150.227 123.631 1.00 28.28 ?  191 GLN A OE1   1 
ATOM   1571  N  NE2   . GLN A 1 191 ? 124.080 149.855 125.736 1.00 25.51 ?  191 GLN A NE2   1 
ATOM   1572  N  N     . LEU A 1 192 ? 126.703 147.642 120.095 1.00 24.46 ?  192 LEU A N     1 
ATOM   1573  C  CA    . LEU A 1 192 ? 126.872 147.466 118.659 1.00 19.42 ?  192 LEU A CA    1 
ATOM   1574  C  C     . LEU A 1 192 ? 126.276 146.154 118.168 1.00 23.47 ?  192 LEU A C     1 
ATOM   1575  O  O     . LEU A 1 192 ? 125.783 146.092 117.036 1.00 33.19 ?  192 LEU A O     1 
ATOM   1576  C  CB    . LEU A 1 192 ? 128.352 147.550 118.288 1.00 20.09 ?  192 LEU A CB    1 
ATOM   1577  C  CG    . LEU A 1 192 ? 129.038 148.890 118.555 1.00 18.88 ?  192 LEU A CG    1 
ATOM   1578  C  CD1   . LEU A 1 192 ? 130.545 148.745 118.439 1.00 18.46 ?  192 LEU A CD1   1 
ATOM   1579  C  CD2   . LEU A 1 192 ? 128.521 149.972 117.624 1.00 16.55 ?  192 LEU A CD2   1 
ATOM   1580  N  N     . SER A 1 193 ? 126.312 145.099 118.986 1.00 19.30 ?  193 SER A N     1 
ATOM   1581  C  CA    . SER A 1 193 ? 125.599 143.876 118.637 1.00 21.10 ?  193 SER A CA    1 
ATOM   1582  C  C     . SER A 1 193 ? 124.094 144.098 118.668 1.00 30.66 ?  193 SER A C     1 
ATOM   1583  O  O     . SER A 1 193 ? 123.352 143.491 117.887 1.00 35.65 ?  193 SER A O     1 
ATOM   1584  C  CB    . SER A 1 193 ? 126.000 142.745 119.583 1.00 23.76 ?  193 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 193 ? 127.402 142.718 119.769 1.00 29.24 ?  193 SER A OG    1 
ATOM   1586  N  N     . LYS A 1 194 ? 123.628 144.961 119.573 1.00 28.35 ?  194 LYS A N     1 
ATOM   1587  C  CA    . LYS A 1 194 ? 122.222 145.351 119.582 1.00 26.81 ?  194 LYS A CA    1 
ATOM   1588  C  C     . LYS A 1 194 ? 121.838 146.036 118.276 1.00 33.98 ?  194 LYS A C     1 
ATOM   1589  O  O     . LYS A 1 194 ? 120.744 145.813 117.747 1.00 37.52 ?  194 LYS A O     1 
ATOM   1590  C  CB    . LYS A 1 194 ? 121.950 146.264 120.778 1.00 25.61 ?  194 LYS A CB    1 
ATOM   1591  C  CG    . LYS A 1 194 ? 120.608 146.966 120.747 1.00 31.84 ?  194 LYS A CG    1 
ATOM   1592  C  CD    . LYS A 1 194 ? 120.497 147.985 121.867 1.00 34.30 ?  194 LYS A CD    1 
ATOM   1593  C  CE    . LYS A 1 194 ? 119.075 148.500 122.004 1.00 30.41 ?  194 LYS A CE    1 
ATOM   1594  N  NZ    . LYS A 1 194 ? 118.962 149.541 123.061 1.00 33.10 1  194 LYS A NZ    1 
ATOM   1595  N  N     . LEU A 1 195 ? 122.730 146.871 117.742 1.00 34.63 ?  195 LEU A N     1 
ATOM   1596  C  CA    . LEU A 1 195 ? 122.508 147.511 116.452 1.00 32.10 ?  195 LEU A CA    1 
ATOM   1597  C  C     . LEU A 1 195 ? 122.615 146.536 115.286 1.00 34.27 ?  195 LEU A C     1 
ATOM   1598  O  O     . LEU A 1 195 ? 122.295 146.915 114.155 1.00 37.81 ?  195 LEU A O     1 
ATOM   1599  C  CB    . LEU A 1 195 ? 123.503 148.655 116.256 1.00 32.31 ?  195 LEU A CB    1 
ATOM   1600  C  CG    . LEU A 1 195 ? 123.347 149.854 117.191 1.00 35.80 ?  195 LEU A CG    1 
ATOM   1601  C  CD1   . LEU A 1 195 ? 124.473 150.851 116.973 1.00 35.62 ?  195 LEU A CD1   1 
ATOM   1602  C  CD2   . LEU A 1 195 ? 121.994 150.513 116.990 1.00 33.64 ?  195 LEU A CD2   1 
ATOM   1603  N  N     . GLY A 1 196 ? 123.060 145.307 115.530 1.00 34.97 ?  196 GLY A N     1 
ATOM   1604  C  CA    . GLY A 1 196 ? 123.193 144.323 114.480 1.00 33.07 ?  196 GLY A CA    1 
ATOM   1605  C  C     . GLY A 1 196 ? 124.566 144.216 113.864 1.00 37.29 ?  196 GLY A C     1 
ATOM   1606  O  O     . GLY A 1 196 ? 124.709 143.564 112.823 1.00 40.02 ?  196 GLY A O     1 
ATOM   1607  N  N     . GLY A 1 197 ? 125.580 144.825 114.468 1.00 34.21 ?  197 GLY A N     1 
ATOM   1608  C  CA    . GLY A 1 197 ? 126.908 144.825 113.896 1.00 24.52 ?  197 GLY A CA    1 
ATOM   1609  C  C     . GLY A 1 197 ? 127.830 143.779 114.494 1.00 23.86 ?  197 GLY A C     1 
ATOM   1610  O  O     . GLY A 1 197 ? 127.708 143.402 115.656 1.00 33.65 ?  197 GLY A O     1 
ATOM   1611  N  N     . GLY A 1 198 ? 128.762 143.308 113.667 1.00 17.12 ?  198 GLY A N     1 
ATOM   1612  C  CA    . GLY A 1 198 ? 129.817 142.431 114.146 1.00 16.73 ?  198 GLY A CA    1 
ATOM   1613  C  C     . GLY A 1 198 ? 130.943 143.256 114.734 1.00 17.59 ?  198 GLY A C     1 
ATOM   1614  O  O     . GLY A 1 198 ? 131.426 144.206 114.108 1.00 18.46 ?  198 GLY A O     1 
ATOM   1615  N  N     . VAL A 1 199 ? 131.366 142.896 115.940 1.00 21.76 ?  199 VAL A N     1 
ATOM   1616  C  CA    . VAL A 1 199 ? 132.300 143.696 116.722 1.00 13.39 ?  199 VAL A CA    1 
ATOM   1617  C  C     . VAL A 1 199 ? 133.610 142.939 116.854 1.00 11.65 ?  199 VAL A C     1 
ATOM   1618  O  O     . VAL A 1 199 ? 133.624 141.776 117.272 1.00 16.01 ?  199 VAL A O     1 
ATOM   1619  C  CB    . VAL A 1 199 ? 131.724 144.031 118.108 1.00 13.59 ?  199 VAL A CB    1 
ATOM   1620  C  CG1   . VAL A 1 199 ? 132.672 144.935 118.868 1.00 15.15 ?  199 VAL A CG1   1 
ATOM   1621  C  CG2   . VAL A 1 199 ? 130.361 144.670 117.966 1.00 18.65 ?  199 VAL A CG2   1 
ATOM   1622  N  N     . SER A 1 200 ? 134.707 143.600 116.505 1.00 15.20 ?  200 SER A N     1 
ATOM   1623  C  CA    . SER A 1 200 ? 136.049 143.070 116.690 1.00 3.66  ?  200 SER A CA    1 
ATOM   1624  C  C     . SER A 1 200 ? 136.766 143.911 117.734 1.00 11.73 ?  200 SER A C     1 
ATOM   1625  O  O     . SER A 1 200 ? 136.723 145.144 117.679 1.00 21.37 ?  200 SER A O     1 
ATOM   1626  C  CB    . SER A 1 200 ? 136.828 143.071 115.375 1.00 9.17  ?  200 SER A CB    1 
ATOM   1627  O  OG    . SER A 1 200 ? 138.017 142.311 115.485 1.00 16.25 ?  200 SER A OG    1 
ATOM   1628  N  N     . LEU A 1 201 ? 137.414 143.247 118.685 1.00 16.66 ?  201 LEU A N     1 
ATOM   1629  C  CA    . LEU A 1 201 ? 138.101 143.913 119.780 1.00 9.22  ?  201 LEU A CA    1 
ATOM   1630  C  C     . LEU A 1 201 ? 139.571 143.524 119.769 1.00 7.69  ?  201 LEU A C     1 
ATOM   1631  O  O     . LEU A 1 201 ? 139.903 142.341 119.646 1.00 9.39  ?  201 LEU A O     1 
ATOM   1632  C  CB    . LEU A 1 201 ? 137.470 143.554 121.128 1.00 16.07 ?  201 LEU A CB    1 
ATOM   1633  C  CG    . LEU A 1 201 ? 136.004 143.950 121.303 1.00 14.03 ?  201 LEU A CG    1 
ATOM   1634  C  CD1   . LEU A 1 201 ? 135.099 142.744 121.119 1.00 14.27 ?  201 LEU A CD1   1 
ATOM   1635  C  CD2   . LEU A 1 201 ? 135.780 144.593 122.659 1.00 15.95 ?  201 LEU A CD2   1 
ATOM   1636  N  N     . ASN A 1 202 ? 140.441 144.519 119.904 1.00 13.18 ?  202 ASN A N     1 
ATOM   1637  C  CA    . ASN A 1 202 ? 141.874 144.292 120.030 1.00 7.05  ?  202 ASN A CA    1 
ATOM   1638  C  C     . ASN A 1 202 ? 142.210 144.099 121.503 1.00 13.85 ?  202 ASN A C     1 
ATOM   1639  O  O     . ASN A 1 202 ? 141.962 144.988 122.323 1.00 25.93 ?  202 ASN A O     1 
ATOM   1640  C  CB    . ASN A 1 202 ? 142.658 145.464 119.446 1.00 8.39  ?  202 ASN A CB    1 
ATOM   1641  C  CG    . ASN A 1 202 ? 144.136 145.170 119.312 1.00 11.78 ?  202 ASN A CG    1 
ATOM   1642  O  OD1   . ASN A 1 202 ? 144.543 144.015 119.190 1.00 17.73 ?  202 ASN A OD1   1 
ATOM   1643  N  ND2   . ASN A 1 202 ? 144.951 146.216 119.331 1.00 14.87 ?  202 ASN A ND2   1 
ATOM   1644  N  N     . LEU A 1 203 ? 142.769 142.937 121.838 1.00 8.33  ?  203 LEU A N     1 
ATOM   1645  C  CA    . LEU A 1 203 ? 143.101 142.604 123.217 1.00 9.55  ?  203 LEU A CA    1 
ATOM   1646  C  C     . LEU A 1 203 ? 144.601 142.605 123.475 1.00 12.58 ?  203 LEU A C     1 
ATOM   1647  O  O     . LEU A 1 203 ? 145.036 142.152 124.538 1.00 14.59 ?  203 LEU A O     1 
ATOM   1648  C  CB    . LEU A 1 203 ? 142.504 141.246 123.589 1.00 15.42 ?  203 LEU A CB    1 
ATOM   1649  C  CG    . LEU A 1 203 ? 140.984 141.109 123.475 1.00 15.72 ?  203 LEU A CG    1 
ATOM   1650  C  CD1   . LEU A 1 203 ? 140.511 139.896 124.249 1.00 14.37 ?  203 LEU A CD1   1 
ATOM   1651  C  CD2   . LEU A 1 203 ? 140.275 142.365 123.960 1.00 12.05 ?  203 LEU A CD2   1 
ATOM   1652  N  N     . SER A 1 204 ? 145.400 143.110 122.533 1.00 17.27 ?  204 SER A N     1 
ATOM   1653  C  CA    . SER A 1 204 ? 146.850 143.082 122.689 1.00 15.28 ?  204 SER A CA    1 
ATOM   1654  C  C     . SER A 1 204 ? 147.334 144.057 123.754 1.00 17.32 ?  204 SER A C     1 
ATOM   1655  O  O     . SER A 1 204 ? 148.343 143.789 124.415 1.00 27.44 ?  204 SER A O     1 
ATOM   1656  C  CB    . SER A 1 204 ? 147.525 143.388 121.354 1.00 12.39 ?  204 SER A CB    1 
ATOM   1657  O  OG    . SER A 1 204 ? 147.049 142.526 120.336 1.00 20.84 ?  204 SER A OG    1 
ATOM   1658  N  N     . LYS A 1 205 ? 146.643 145.184 123.933 1.00 18.64 ?  205 LYS A N     1 
ATOM   1659  C  CA    . LYS A 1 205 ? 147.035 146.134 124.966 1.00 21.79 ?  205 LYS A CA    1 
ATOM   1660  C  C     . LYS A 1 205 ? 146.752 145.613 126.366 1.00 22.02 ?  205 LYS A C     1 
ATOM   1661  O  O     . LYS A 1 205 ? 147.363 146.091 127.327 1.00 28.08 ?  205 LYS A O     1 
ATOM   1662  C  CB    . LYS A 1 205 ? 146.322 147.467 124.753 1.00 22.28 ?  205 LYS A CB    1 
ATOM   1663  C  CG    . LYS A 1 205 ? 146.786 148.211 123.521 1.00 21.54 ?  205 LYS A CG    1 
ATOM   1664  C  CD    . LYS A 1 205 ? 146.081 149.541 123.381 1.00 25.34 ?  205 LYS A CD    1 
ATOM   1665  C  CE    . LYS A 1 205 ? 146.698 150.357 122.263 1.00 28.62 ?  205 LYS A CE    1 
ATOM   1666  N  NZ    . LYS A 1 205 ? 146.589 149.674 120.946 1.00 24.12 1  205 LYS A NZ    1 
ATOM   1667  N  N     . LEU A 1 206 ? 145.844 144.652 126.501 1.00 18.83 ?  206 LEU A N     1 
ATOM   1668  C  CA    . LEU A 1 206 ? 145.539 144.081 127.803 1.00 12.03 ?  206 LEU A CA    1 
ATOM   1669  C  C     . LEU A 1 206 ? 146.721 143.270 128.318 1.00 18.40 ?  206 LEU A C     1 
ATOM   1670  O  O     . LEU A 1 206 ? 147.330 142.493 127.578 1.00 24.65 ?  206 LEU A O     1 
ATOM   1671  C  CB    . LEU A 1 206 ? 144.297 143.200 127.712 1.00 16.39 ?  206 LEU A CB    1 
ATOM   1672  C  CG    . LEU A 1 206 ? 142.998 143.931 127.375 1.00 21.56 ?  206 LEU A CG    1 
ATOM   1673  C  CD1   . LEU A 1 206 ? 141.847 142.951 127.311 1.00 19.17 ?  206 LEU A CD1   1 
ATOM   1674  C  CD2   . LEU A 1 206 ? 142.722 145.024 128.391 1.00 21.52 ?  206 LEU A CD2   1 
ATOM   1675  N  N     . ARG A 1 207 ? 147.043 143.454 129.593 1.00 25.76 ?  207 ARG A N     1 
ATOM   1676  C  CA    . ARG A 1 207 ? 148.176 142.756 130.177 1.00 22.21 ?  207 ARG A CA    1 
ATOM   1677  C  C     . ARG A 1 207 ? 147.861 141.275 130.359 1.00 27.34 ?  207 ARG A C     1 
ATOM   1678  O  O     . ARG A 1 207 ? 146.709 140.877 130.547 1.00 33.02 ?  207 ARG A O     1 
ATOM   1679  C  CB    . ARG A 1 207 ? 148.572 143.397 131.507 1.00 25.46 ?  207 ARG A CB    1 
ATOM   1680  C  CG    . ARG A 1 207 ? 147.525 143.336 132.596 1.00 20.93 ?  207 ARG A CG    1 
ATOM   1681  C  CD    . ARG A 1 207 ? 147.950 144.176 133.788 1.00 21.04 ?  207 ARG A CD    1 
ATOM   1682  N  NE    . ARG A 1 207 ? 147.603 145.580 133.611 1.00 29.59 ?  207 ARG A NE    1 
ATOM   1683  C  CZ    . ARG A 1 207 ? 147.664 146.495 134.569 1.00 23.85 ?  207 ARG A CZ    1 
ATOM   1684  N  NH1   . ARG A 1 207 ? 148.076 146.190 135.788 1.00 28.40 1  207 ARG A NH1   1 
ATOM   1685  N  NH2   . ARG A 1 207 ? 147.302 147.744 134.297 1.00 19.28 ?  207 ARG A NH2   1 
ATOM   1686  N  N     . ALA A 1 208 ? 148.907 140.455 130.298 1.00 28.20 ?  208 ALA A N     1 
ATOM   1687  C  CA    . ALA A 1 208 ? 148.755 139.010 130.251 1.00 25.93 ?  208 ALA A CA    1 
ATOM   1688  C  C     . ALA A 1 208 ? 148.387 138.458 131.626 1.00 31.00 ?  208 ALA A C     1 
ATOM   1689  O  O     . ALA A 1 208 ? 148.276 139.188 132.614 1.00 33.88 ?  208 ALA A O     1 
ATOM   1690  C  CB    . ALA A 1 208 ? 150.032 138.362 129.722 1.00 27.47 ?  208 ALA A CB    1 
ATOM   1691  N  N     . LYS A 1 209 ? 148.184 137.146 131.685 1.00 30.80 ?  209 LYS A N     1 
ATOM   1692  C  CA    . LYS A 1 209 ? 147.844 136.497 132.944 1.00 25.81 ?  209 LYS A CA    1 
ATOM   1693  C  C     . LYS A 1 209 ? 149.070 136.430 133.846 1.00 33.73 ?  209 LYS A C     1 
ATOM   1694  O  O     . LYS A 1 209 ? 150.171 136.101 133.393 1.00 34.47 ?  209 LYS A O     1 
ATOM   1695  C  CB    . LYS A 1 209 ? 147.293 135.097 132.689 1.00 28.85 ?  209 LYS A CB    1 
ATOM   1696  C  CG    . LYS A 1 209 ? 146.824 134.382 133.944 1.00 32.40 ?  209 LYS A CG    1 
ATOM   1697  C  CD    . LYS A 1 209 ? 146.719 132.880 133.737 1.00 32.56 ?  209 LYS A CD    1 
ATOM   1698  C  CE    . LYS A 1 209 ? 147.847 132.349 132.867 1.00 35.58 ?  209 LYS A CE    1 
ATOM   1699  N  NZ    . LYS A 1 209 ? 147.696 130.892 132.600 1.00 35.06 1  209 LYS A NZ    1 
ATOM   1700  N  N     . GLY A 1 210 ? 148.875 136.732 135.126 1.00 37.65 ?  210 GLY A N     1 
ATOM   1701  C  CA    . GLY A 1 210 ? 149.974 136.764 136.066 1.00 32.83 ?  210 GLY A CA    1 
ATOM   1702  C  C     . GLY A 1 210 ? 150.680 138.093 136.183 1.00 35.30 ?  210 GLY A C     1 
ATOM   1703  O  O     . GLY A 1 210 ? 151.812 138.133 136.679 1.00 40.60 ?  210 GLY A O     1 
ATOM   1704  N  N     . GLU A 1 211 ? 150.058 139.179 135.740 1.00 33.92 ?  211 GLU A N     1 
ATOM   1705  C  CA    . GLU A 1 211 ? 150.630 140.510 135.846 1.00 31.71 ?  211 GLU A CA    1 
ATOM   1706  C  C     . GLU A 1 211 ? 150.099 141.218 137.087 1.00 34.75 ?  211 GLU A C     1 
ATOM   1707  O  O     . GLU A 1 211 ? 149.196 140.736 137.775 1.00 36.62 ?  211 GLU A O     1 
ATOM   1708  C  CB    . GLU A 1 211 ? 150.332 141.327 134.587 1.00 30.32 ?  211 GLU A CB    1 
ATOM   1709  C  CG    . GLU A 1 211 ? 150.995 140.775 133.343 1.00 33.60 ?  211 GLU A CG    1 
ATOM   1710  C  CD    . GLU A 1 211 ? 151.786 141.821 132.587 1.00 36.43 ?  211 GLU A CD    1 
ATOM   1711  O  OE1   . GLU A 1 211 ? 152.788 142.320 133.138 1.00 39.07 ?  211 GLU A OE1   1 
ATOM   1712  O  OE2   . GLU A 1 211 ? 151.416 142.135 131.438 1.00 30.88 -1 211 GLU A OE2   1 
ATOM   1713  N  N     . ALA A 1 212 ? 150.675 142.383 137.368 1.00 33.78 ?  212 ALA A N     1 
ATOM   1714  C  CA    . ALA A 1 212 ? 150.387 143.106 138.598 1.00 33.97 ?  212 ALA A CA    1 
ATOM   1715  C  C     . ALA A 1 212 ? 149.274 144.125 138.396 1.00 39.38 ?  212 ALA A C     1 
ATOM   1716  O  O     . ALA A 1 212 ? 149.234 144.832 137.384 1.00 41.12 ?  212 ALA A O     1 
ATOM   1717  C  CB    . ALA A 1 212 ? 151.644 143.807 139.112 1.00 35.82 ?  212 ALA A CB    1 
ATOM   1718  N  N     . ILE A 1 213 ? 148.368 144.190 139.369 1.00 32.09 ?  213 ILE A N     1 
ATOM   1719  C  CA    . ILE A 1 213 ? 147.335 145.218 139.437 1.00 34.78 ?  213 ILE A CA    1 
ATOM   1720  C  C     . ILE A 1 213 ? 147.591 146.022 140.703 1.00 36.14 ?  213 ILE A C     1 
ATOM   1721  O  O     . ILE A 1 213 ? 147.454 145.497 141.815 1.00 40.58 ?  213 ILE A O     1 
ATOM   1722  C  CB    . ILE A 1 213 ? 145.921 144.622 139.439 1.00 34.49 ?  213 ILE A CB    1 
ATOM   1723  C  CG1   . ILE A 1 213 ? 145.766 143.596 138.316 1.00 34.39 ?  213 ILE A CG1   1 
ATOM   1724  C  CG2   . ILE A 1 213 ? 144.881 145.723 139.307 1.00 29.79 ?  213 ILE A CG2   1 
ATOM   1725  C  CD1   . ILE A 1 213 ? 144.527 142.741 138.444 1.00 30.50 ?  213 ILE A CD1   1 
ATOM   1726  N  N     . LYS A 1 214 ? 147.952 147.296 140.537 1.00 41.13 ?  214 LYS A N     1 
ATOM   1727  C  CA    . LYS A 1 214 ? 148.306 148.172 141.656 1.00 40.28 ?  214 LYS A CA    1 
ATOM   1728  C  C     . LYS A 1 214 ? 149.414 147.557 142.508 1.00 46.68 ?  214 LYS A C     1 
ATOM   1729  O  O     . LYS A 1 214 ? 149.360 147.568 143.740 1.00 49.91 ?  214 LYS A O     1 
ATOM   1730  C  CB    . LYS A 1 214 ? 147.080 148.511 142.506 1.00 40.44 ?  214 LYS A CB    1 
ATOM   1731  C  CG    . LYS A 1 214 ? 146.246 149.654 141.954 1.00 40.01 ?  214 LYS A CG    1 
ATOM   1732  C  CD    . LYS A 1 214 ? 145.048 149.951 142.838 1.00 42.30 ?  214 LYS A CD    1 
ATOM   1733  C  CE    . LYS A 1 214 ? 144.374 151.250 142.426 1.00 44.11 ?  214 LYS A CE    1 
ATOM   1734  N  NZ    . LYS A 1 214 ? 143.180 151.550 143.262 1.00 42.67 1  214 LYS A NZ    1 
ATOM   1735  N  N     . ASP A 1 215 ? 150.423 147.005 141.834 1.00 47.70 ?  215 ASP A N     1 
ATOM   1736  C  CA    . ASP A 1 215 ? 151.636 146.492 142.478 1.00 49.79 ?  215 ASP A CA    1 
ATOM   1737  C  C     . ASP A 1 215 ? 151.340 145.334 143.431 1.00 48.44 ?  215 ASP A C     1 
ATOM   1738  O  O     . ASP A 1 215 ? 151.979 145.190 144.475 1.00 48.37 ?  215 ASP A O     1 
ATOM   1739  C  CB    . ASP A 1 215 ? 152.394 147.609 143.197 1.00 48.76 ?  215 ASP A CB    1 
ATOM   1740  C  CG    . ASP A 1 215 ? 152.746 148.761 142.276 1.00 52.47 ?  215 ASP A CG    1 
ATOM   1741  O  OD1   . ASP A 1 215 ? 153.131 148.500 141.117 1.00 51.00 ?  215 ASP A OD1   1 
ATOM   1742  O  OD2   . ASP A 1 215 ? 152.641 149.928 142.710 1.00 51.63 -1 215 ASP A OD2   1 
ATOM   1743  N  N     . VAL A 1 216 ? 150.367 144.499 143.074 1.00 43.69 ?  216 VAL A N     1 
ATOM   1744  C  CA    . VAL A 1 216 ? 150.168 143.203 143.711 1.00 45.86 ?  216 VAL A CA    1 
ATOM   1745  C  C     . VAL A 1 216 ? 150.357 142.137 142.637 1.00 46.94 ?  216 VAL A C     1 
ATOM   1746  O  O     . VAL A 1 216 ? 149.828 142.263 141.526 1.00 49.98 ?  216 VAL A O     1 
ATOM   1747  C  CB    . VAL A 1 216 ? 148.797 143.100 144.418 1.00 44.85 ?  216 VAL A CB    1 
ATOM   1748  C  CG1   . VAL A 1 216 ? 148.266 144.486 144.765 1.00 43.90 ?  216 VAL A CG1   1 
ATOM   1749  C  CG2   . VAL A 1 216 ? 147.773 142.308 143.612 1.00 43.37 ?  216 VAL A CG2   1 
ATOM   1750  N  N     . GLU A 1 217 ? 151.167 141.129 142.943 1.00 48.48 ?  217 GLU A N     1 
ATOM   1751  C  CA    . GLU A 1 217 ? 151.675 140.232 141.917 1.00 48.13 ?  217 GLU A CA    1 
ATOM   1752  C  C     . GLU A 1 217 ? 150.689 139.106 141.616 1.00 49.28 ?  217 GLU A C     1 
ATOM   1753  O  O     . GLU A 1 217 ? 149.855 138.732 142.444 1.00 51.39 ?  217 GLU A O     1 
ATOM   1754  C  CB    . GLU A 1 217 ? 153.023 139.645 142.337 1.00 50.28 ?  217 GLU A CB    1 
ATOM   1755  C  CG    . GLU A 1 217 ? 154.048 140.668 142.817 1.00 50.51 ?  217 GLU A CG    1 
ATOM   1756  C  CD    . GLU A 1 217 ? 153.958 141.993 142.082 1.00 52.26 ?  217 GLU A CD    1 
ATOM   1757  O  OE1   . GLU A 1 217 ? 154.519 142.096 140.971 1.00 53.56 ?  217 GLU A OE1   1 
ATOM   1758  O  OE2   . GLU A 1 217 ? 153.335 142.933 142.618 1.00 49.24 -1 217 GLU A OE2   1 
ATOM   1759  N  N     . ASN A 1 218 ? 150.810 138.562 140.400 1.00 44.02 ?  218 ASN A N     1 
ATOM   1760  C  CA    . ASN A 1 218 ? 150.025 137.409 139.949 1.00 44.04 ?  218 ASN A CA    1 
ATOM   1761  C  C     . ASN A 1 218 ? 148.527 137.655 140.103 1.00 47.82 ?  218 ASN A C     1 
ATOM   1762  O  O     . ASN A 1 218 ? 147.778 136.786 140.553 1.00 46.76 ?  218 ASN A O     1 
ATOM   1763  C  CB    . ASN A 1 218 ? 150.446 136.137 140.686 1.00 43.02 ?  218 ASN A CB    1 
ATOM   1764  C  CG    . ASN A 1 218 ? 150.468 134.920 139.782 1.00 48.15 ?  218 ASN A CG    1 
ATOM   1765  O  OD1   . ASN A 1 218 ? 151.003 134.965 138.673 1.00 50.06 ?  218 ASN A OD1   1 
ATOM   1766  N  ND2   . ASN A 1 218 ? 149.885 133.823 140.251 1.00 47.54 ?  218 ASN A ND2   1 
ATOM   1767  N  N     . ALA A 1 219 ? 148.084 138.851 139.721 1.00 38.03 ?  219 ALA A N     1 
ATOM   1768  C  CA    . ALA A 1 219 ? 146.704 139.266 139.935 1.00 33.65 ?  219 ALA A CA    1 
ATOM   1769  C  C     . ALA A 1 219 ? 145.859 139.262 138.672 1.00 35.31 ?  219 ALA A C     1 
ATOM   1770  O  O     . ALA A 1 219 ? 144.655 139.001 138.750 1.00 36.61 ?  219 ALA A O     1 
ATOM   1771  C  CB    . ALA A 1 219 ? 146.670 140.667 140.551 1.00 35.87 ?  219 ALA A CB    1 
ATOM   1772  N  N     . THR A 1 220 ? 146.452 139.545 137.517 1.00 36.45 ?  220 THR A N     1 
ATOM   1773  C  CA    . THR A 1 220 ? 145.676 139.663 136.291 1.00 30.45 ?  220 THR A CA    1 
ATOM   1774  C  C     . THR A 1 220 ? 145.205 138.295 135.813 1.00 34.14 ?  220 THR A C     1 
ATOM   1775  O  O     . THR A 1 220 ? 145.938 137.305 135.885 1.00 35.22 ?  220 THR A O     1 
ATOM   1776  C  CB    . THR A 1 220 ? 146.508 140.340 135.202 1.00 27.27 ?  220 THR A CB    1 
ATOM   1777  O  OG1   . THR A 1 220 ? 147.066 141.556 135.713 1.00 35.48 ?  220 THR A OG1   1 
ATOM   1778  C  CG2   . THR A 1 220 ? 145.645 140.661 133.995 1.00 29.46 ?  220 THR A CG2   1 
ATOM   1779  N  N     . LYS A 1 221 ? 143.966 138.246 135.323 1.00 35.92 ?  221 LYS A N     1 
ATOM   1780  C  CA    . LYS A 1 221 ? 143.424 137.033 134.728 1.00 30.05 ?  221 LYS A CA    1 
ATOM   1781  C  C     . LYS A 1 221 ? 143.841 136.853 133.276 1.00 33.95 ?  221 LYS A C     1 
ATOM   1782  O  O     . LYS A 1 221 ? 143.573 135.794 132.698 1.00 40.03 ?  221 LYS A O     1 
ATOM   1783  C  CB    . LYS A 1 221 ? 141.897 137.036 134.821 1.00 29.97 ?  221 LYS A CB    1 
ATOM   1784  C  CG    . LYS A 1 221 ? 141.364 136.847 136.226 1.00 32.25 ?  221 LYS A CG    1 
ATOM   1785  C  CD    . LYS A 1 221 ? 140.046 136.097 136.215 1.00 33.02 ?  221 LYS A CD    1 
ATOM   1786  C  CE    . LYS A 1 221 ? 139.711 135.562 137.594 1.00 33.42 ?  221 LYS A CE    1 
ATOM   1787  N  NZ    . LYS A 1 221 ? 138.564 134.614 137.557 1.00 36.29 1  221 LYS A NZ    1 
ATOM   1788  N  N     . GLY A 1 222 ? 144.484 137.849 132.680 1.00 31.76 ?  222 GLY A N     1 
ATOM   1789  C  CA    . GLY A 1 222 ? 144.885 137.765 131.296 1.00 26.99 ?  222 GLY A CA    1 
ATOM   1790  C  C     . GLY A 1 222 ? 143.767 138.159 130.351 1.00 27.61 ?  222 GLY A C     1 
ATOM   1791  O  O     . GLY A 1 222 ? 142.709 138.656 130.744 1.00 33.53 ?  222 GLY A O     1 
ATOM   1792  N  N     . VAL A 1 223 ? 144.025 137.929 129.063 1.00 25.41 ?  223 VAL A N     1 
ATOM   1793  C  CA    . VAL A 1 223 ? 143.022 138.240 128.052 1.00 24.51 ?  223 VAL A CA    1 
ATOM   1794  C  C     . VAL A 1 223 ? 141.940 137.174 127.969 1.00 18.93 ?  223 VAL A C     1 
ATOM   1795  O  O     . VAL A 1 223 ? 140.891 137.425 127.369 1.00 22.69 ?  223 VAL A O     1 
ATOM   1796  C  CB    . VAL A 1 223 ? 143.669 138.439 126.670 1.00 22.73 ?  223 VAL A CB    1 
ATOM   1797  C  CG1   . VAL A 1 223 ? 144.893 139.327 126.783 1.00 20.06 ?  223 VAL A CG1   1 
ATOM   1798  C  CG2   . VAL A 1 223 ? 144.030 137.100 126.049 1.00 20.14 ?  223 VAL A CG2   1 
ATOM   1799  N  N     . VAL A 1 224 ? 142.154 135.997 128.557 1.00 27.29 ?  224 VAL A N     1 
ATOM   1800  C  CA    . VAL A 1 224 ? 141.150 134.939 128.472 1.00 23.25 ?  224 VAL A CA    1 
ATOM   1801  C  C     . VAL A 1 224 ? 139.916 135.275 129.307 1.00 27.16 ?  224 VAL A C     1 
ATOM   1802  O  O     . VAL A 1 224 ? 138.787 134.989 128.891 1.00 29.49 ?  224 VAL A O     1 
ATOM   1803  C  CB    . VAL A 1 224 ? 141.765 133.591 128.881 1.00 30.45 ?  224 VAL A CB    1 
ATOM   1804  C  CG1   . VAL A 1 224 ? 140.717 132.492 128.852 1.00 28.30 ?  224 VAL A CG1   1 
ATOM   1805  C  CG2   . VAL A 1 224 ? 142.918 133.245 127.958 1.00 28.17 ?  224 VAL A CG2   1 
ATOM   1806  N  N     . GLY A 1 225 ? 140.094 135.882 130.481 1.00 26.05 ?  225 GLY A N     1 
ATOM   1807  C  CA    . GLY A 1 225 ? 138.940 136.330 131.246 1.00 23.64 ?  225 GLY A CA    1 
ATOM   1808  C  C     . GLY A 1 225 ? 138.160 137.415 130.529 1.00 21.95 ?  225 GLY A C     1 
ATOM   1809  O  O     . GLY A 1 225 ? 136.924 137.435 130.556 1.00 29.10 ?  225 GLY A O     1 
ATOM   1810  N  N     . VAL A 1 226 ? 138.873 138.330 129.870 1.00 22.04 ?  226 VAL A N     1 
ATOM   1811  C  CA    . VAL A 1 226 ? 138.212 139.354 129.068 1.00 21.14 ?  226 VAL A CA    1 
ATOM   1812  C  C     . VAL A 1 226 ? 137.467 138.716 127.904 1.00 19.41 ?  226 VAL A C     1 
ATOM   1813  O  O     . VAL A 1 226 ? 136.381 139.164 127.525 1.00 22.12 ?  226 VAL A O     1 
ATOM   1814  C  CB    . VAL A 1 226 ? 139.236 140.396 128.584 1.00 19.03 ?  226 VAL A CB    1 
ATOM   1815  C  CG1   . VAL A 1 226 ? 138.529 141.555 127.898 1.00 26.23 ?  226 VAL A CG1   1 
ATOM   1816  C  CG2   . VAL A 1 226 ? 140.073 140.888 129.747 1.00 16.46 ?  226 VAL A CG2   1 
ATOM   1817  N  N     . MET A 1 227 ? 138.040 137.663 127.318 1.00 21.13 ?  227 MET A N     1 
ATOM   1818  C  CA    . MET A 1 227 ? 137.354 136.951 126.245 1.00 23.66 ?  227 MET A CA    1 
ATOM   1819  C  C     . MET A 1 227 ? 136.096 136.268 126.754 1.00 23.17 ?  227 MET A C     1 
ATOM   1820  O  O     . MET A 1 227 ? 135.085 136.226 126.052 1.00 28.48 ?  227 MET A O     1 
ATOM   1821  C  CB    . MET A 1 227 ? 138.281 135.928 125.594 1.00 20.13 ?  227 MET A CB    1 
ATOM   1822  C  CG    . MET A 1 227 ? 139.444 136.525 124.840 1.00 17.73 ?  227 MET A CG    1 
ATOM   1823  S  SD    . MET A 1 227 ? 140.695 135.291 124.474 1.00 36.51 ?  227 MET A SD    1 
ATOM   1824  C  CE    . MET A 1 227 ? 139.812 134.295 123.281 1.00 24.79 ?  227 MET A CE    1 
ATOM   1825  N  N     . LYS A 1 228 ? 136.144 135.706 127.962 1.00 21.26 ?  228 LYS A N     1 
ATOM   1826  C  CA    . LYS A 1 228 ? 134.943 135.116 128.548 1.00 22.96 ?  228 LYS A CA    1 
ATOM   1827  C  C     . LYS A 1 228 ? 133.867 136.173 128.764 1.00 21.81 ?  228 LYS A C     1 
ATOM   1828  O  O     . LYS A 1 228 ? 132.686 135.945 128.463 1.00 24.62 ?  228 LYS A O     1 
ATOM   1829  C  CB    . LYS A 1 228 ? 135.283 134.427 129.869 1.00 24.81 ?  228 LYS A CB    1 
ATOM   1830  C  CG    . LYS A 1 228 ? 135.895 133.048 129.721 1.00 27.57 ?  228 LYS A CG    1 
ATOM   1831  C  CD    . LYS A 1 228 ? 136.446 132.561 131.052 1.00 30.30 ?  228 LYS A CD    1 
ATOM   1832  C  CE    . LYS A 1 228 ? 137.946 132.782 131.146 1.00 31.49 ?  228 LYS A CE    1 
ATOM   1833  N  NZ    . LYS A 1 228 ? 138.404 132.994 132.547 1.00 27.84 1  228 LYS A NZ    1 
ATOM   1834  N  N     . LEU A 1 229 ? 134.261 137.340 129.279 1.00 20.71 ?  229 LEU A N     1 
ATOM   1835  C  CA    . LEU A 1 229 ? 133.309 138.431 129.466 1.00 18.79 ?  229 LEU A CA    1 
ATOM   1836  C  C     . LEU A 1 229 ? 132.705 138.868 128.137 1.00 20.13 ?  229 LEU A C     1 
ATOM   1837  O  O     . LEU A 1 229 ? 131.490 139.073 128.028 1.00 18.55 ?  229 LEU A O     1 
ATOM   1838  C  CB    . LEU A 1 229 ? 133.995 139.611 130.151 1.00 20.16 ?  229 LEU A CB    1 
ATOM   1839  C  CG    . LEU A 1 229 ? 134.281 139.502 131.646 1.00 18.98 ?  229 LEU A CG    1 
ATOM   1840  C  CD1   . LEU A 1 229 ? 135.156 140.660 132.084 1.00 21.66 ?  229 LEU A CD1   1 
ATOM   1841  C  CD2   . LEU A 1 229 ? 132.986 139.485 132.430 1.00 18.33 ?  229 LEU A CD2   1 
ATOM   1842  N  N     . LEU A 1 230 ? 133.545 139.017 127.112 1.00 24.97 ?  230 LEU A N     1 
ATOM   1843  C  CA    . LEU A 1 230 ? 133.064 139.433 125.800 1.00 16.02 ?  230 LEU A CA    1 
ATOM   1844  C  C     . LEU A 1 230 ? 132.166 138.373 125.177 1.00 15.64 ?  230 LEU A C     1 
ATOM   1845  O  O     . LEU A 1 230 ? 131.175 138.704 124.521 1.00 30.75 ?  230 LEU A O     1 
ATOM   1846  C  CB    . LEU A 1 230 ? 134.245 139.743 124.882 1.00 23.37 ?  230 LEU A CB    1 
ATOM   1847  C  CG    . LEU A 1 230 ? 135.023 141.019 125.205 1.00 22.41 ?  230 LEU A CG    1 
ATOM   1848  C  CD1   . LEU A 1 230 ? 136.293 141.093 124.372 1.00 23.43 ?  230 LEU A CD1   1 
ATOM   1849  C  CD2   . LEU A 1 230 ? 134.154 142.247 124.984 1.00 16.74 ?  230 LEU A CD2   1 
ATOM   1850  N  N     . ASP A 1 231 ? 132.504 137.097 125.358 1.00 23.35 ?  231 ASP A N     1 
ATOM   1851  C  CA    . ASP A 1 231 ? 131.670 136.023 124.836 1.00 23.77 ?  231 ASP A CA    1 
ATOM   1852  C  C     . ASP A 1 231 ? 130.300 136.028 125.496 1.00 22.03 ?  231 ASP A C     1 
ATOM   1853  O  O     . ASP A 1 231 ? 129.280 135.851 124.822 1.00 29.84 ?  231 ASP A O     1 
ATOM   1854  C  CB    . ASP A 1 231 ? 132.368 134.677 125.038 1.00 23.08 ?  231 ASP A CB    1 
ATOM   1855  C  CG    . ASP A 1 231 ? 131.495 133.501 124.655 1.00 36.05 ?  231 ASP A CG    1 
ATOM   1856  O  OD1   . ASP A 1 231 ? 131.020 133.463 123.500 1.00 42.35 ?  231 ASP A OD1   1 
ATOM   1857  O  OD2   . ASP A 1 231 ? 131.288 132.611 125.507 1.00 33.33 -1 231 ASP A OD2   1 
ATOM   1858  N  N     . ASN A 1 232 ? 130.254 136.244 126.813 1.00 27.62 ?  232 ASN A N     1 
ATOM   1859  C  CA    . ASN A 1 232 ? 128.963 136.364 127.484 1.00 25.45 ?  232 ASN A CA    1 
ATOM   1860  C  C     . ASN A 1 232 ? 128.190 137.580 126.986 1.00 21.44 ?  232 ASN A C     1 
ATOM   1861  O  O     . ASN A 1 232 ? 126.971 137.511 126.788 1.00 28.17 ?  232 ASN A O     1 
ATOM   1862  C  CB    . ASN A 1 232 ? 129.157 136.429 128.997 1.00 26.42 ?  232 ASN A CB    1 
ATOM   1863  C  CG    . ASN A 1 232 ? 128.263 135.455 129.734 1.00 32.00 ?  232 ASN A CG    1 
ATOM   1864  O  OD1   . ASN A 1 232 ? 127.042 135.607 129.748 1.00 34.71 ?  232 ASN A OD1   1 
ATOM   1865  N  ND2   . ASN A 1 232 ? 128.862 134.437 130.334 1.00 34.25 ?  232 ASN A ND2   1 
ATOM   1866  N  N     . ALA A 1 233 ? 128.883 138.702 126.781 1.00 17.49 ?  233 ALA A N     1 
ATOM   1867  C  CA    . ALA A 1 233 ? 128.222 139.904 126.286 1.00 19.25 ?  233 ALA A CA    1 
ATOM   1868  C  C     . ALA A 1 233 ? 127.644 139.687 124.892 1.00 27.61 ?  233 ALA A C     1 
ATOM   1869  O  O     . ALA A 1 233 ? 126.544 140.161 124.586 1.00 27.48 ?  233 ALA A O     1 
ATOM   1870  C  CB    . ALA A 1 233 ? 129.201 141.077 126.287 1.00 19.50 ?  233 ALA A CB    1 
ATOM   1871  N  N     . PHE A 1 234 ? 128.378 138.980 124.030 1.00 25.88 ?  234 PHE A N     1 
ATOM   1872  C  CA    . PHE A 1 234 ? 127.903 138.732 122.675 1.00 18.99 ?  234 PHE A CA    1 
ATOM   1873  C  C     . PHE A 1 234 ? 126.787 137.698 122.650 1.00 22.17 ?  234 PHE A C     1 
ATOM   1874  O  O     . PHE A 1 234 ? 125.891 137.779 121.803 1.00 29.06 ?  234 PHE A O     1 
ATOM   1875  C  CB    . PHE A 1 234 ? 129.061 138.290 121.780 1.00 24.21 ?  234 PHE A CB    1 
ATOM   1876  C  CG    . PHE A 1 234 ? 129.959 139.415 121.354 1.00 22.59 ?  234 PHE A CG    1 
ATOM   1877  C  CD1   . PHE A 1 234 ? 129.452 140.499 120.661 1.00 21.43 ?  234 PHE A CD1   1 
ATOM   1878  C  CD2   . PHE A 1 234 ? 131.310 139.387 121.643 1.00 21.36 ?  234 PHE A CD2   1 
ATOM   1879  C  CE1   . PHE A 1 234 ? 130.276 141.535 120.271 1.00 20.43 ?  234 PHE A CE1   1 
ATOM   1880  C  CE2   . PHE A 1 234 ? 132.138 140.421 121.257 1.00 22.33 ?  234 PHE A CE2   1 
ATOM   1881  C  CZ    . PHE A 1 234 ? 131.621 141.495 120.569 1.00 22.81 ?  234 PHE A CZ    1 
ATOM   1882  N  N     . ARG A 1 235 ? 126.823 136.720 123.557 1.00 24.66 ?  235 ARG A N     1 
ATOM   1883  C  CA    . ARG A 1 235 ? 125.699 135.799 123.679 1.00 25.84 ?  235 ARG A CA    1 
ATOM   1884  C  C     . ARG A 1 235 ? 124.447 136.531 124.139 1.00 31.07 ?  235 ARG A C     1 
ATOM   1885  O  O     . ARG A 1 235 ? 123.344 136.255 123.655 1.00 39.35 ?  235 ARG A O     1 
ATOM   1886  C  CB    . ARG A 1 235 ? 126.043 134.666 124.646 1.00 26.56 ?  235 ARG A CB    1 
ATOM   1887  C  CG    . ARG A 1 235 ? 127.090 133.702 124.126 1.00 32.06 ?  235 ARG A CG    1 
ATOM   1888  C  CD    . ARG A 1 235 ? 127.094 132.408 124.919 1.00 31.55 ?  235 ARG A CD    1 
ATOM   1889  N  NE    . ARG A 1 235 ? 128.343 132.228 125.648 1.00 33.93 ?  235 ARG A NE    1 
ATOM   1890  C  CZ    . ARG A 1 235 ? 128.545 132.636 126.893 1.00 35.96 ?  235 ARG A CZ    1 
ATOM   1891  N  NH1   . ARG A 1 235 ? 127.596 133.246 127.583 1.00 35.78 1  235 ARG A NH1   1 
ATOM   1892  N  NH2   . ARG A 1 235 ? 129.731 132.428 127.460 1.00 33.53 ?  235 ARG A NH2   1 
ATOM   1893  N  N     . TYR A 1 236 ? 124.600 137.470 125.074 1.00 25.37 ?  236 TYR A N     1 
ATOM   1894  C  CA    . TYR A 1 236 ? 123.448 138.214 125.571 1.00 21.11 ?  236 TYR A CA    1 
ATOM   1895  C  C     . TYR A 1 236 ? 122.860 139.116 124.491 1.00 24.21 ?  236 TYR A C     1 
ATOM   1896  O  O     . TYR A 1 236 ? 121.640 139.153 124.295 1.00 24.55 ?  236 TYR A O     1 
ATOM   1897  C  CB    . TYR A 1 236 ? 123.845 139.035 126.797 1.00 19.94 ?  236 TYR A CB    1 
ATOM   1898  C  CG    . TYR A 1 236 ? 122.676 139.697 127.478 1.00 23.99 ?  236 TYR A CG    1 
ATOM   1899  C  CD1   . TYR A 1 236 ? 121.793 138.957 128.250 1.00 21.35 ?  236 TYR A CD1   1 
ATOM   1900  C  CD2   . TYR A 1 236 ? 122.451 141.061 127.346 1.00 24.85 ?  236 TYR A CD2   1 
ATOM   1901  C  CE1   . TYR A 1 236 ? 120.723 139.553 128.874 1.00 24.71 ?  236 TYR A CE1   1 
ATOM   1902  C  CE2   . TYR A 1 236 ? 121.381 141.667 127.969 1.00 16.98 ?  236 TYR A CE2   1 
ATOM   1903  C  CZ    . TYR A 1 236 ? 120.521 140.906 128.731 1.00 21.52 ?  236 TYR A CZ    1 
ATOM   1904  O  OH    . TYR A 1 236 ? 119.452 141.496 129.355 1.00 25.78 ?  236 TYR A OH    1 
ATOM   1905  N  N     . ALA A 1 237 ? 123.712 139.851 123.781 1.00 30.61 ?  237 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 237 ? 123.277 140.783 122.740 1.00 30.91 ?  237 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 237 ? 123.297 140.040 121.409 1.00 35.59 ?  237 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 237 ? 124.331 139.934 120.749 1.00 39.55 ?  237 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 237 ? 124.165 142.021 122.714 1.00 30.89 ?  237 ALA A CB    1 
ATOM   1910  N  N     . ASP A 1 238 ? 122.136 139.528 121.009 1.00 50.35 ?  238 ASP A N     1 
ATOM   1911  C  CA    . ASP A 1 238 ? 122.006 138.681 119.827 1.00 54.69 ?  238 ASP A CA    1 
ATOM   1912  C  C     . ASP A 1 238 ? 120.887 139.187 118.922 1.00 59.58 ?  238 ASP A C     1 
ATOM   1913  O  O     . ASP A 1 238 ? 120.031 138.427 118.463 1.00 59.96 ?  238 ASP A O     1 
ATOM   1914  C  CB    . ASP A 1 238 ? 121.767 137.230 120.235 1.00 52.63 ?  238 ASP A CB    1 
ATOM   1915  C  CG    . ASP A 1 238 ? 120.619 137.080 121.209 1.00 55.48 ?  238 ASP A CG    1 
ATOM   1916  O  OD1   . ASP A 1 238 ? 120.152 138.107 121.745 1.00 55.79 ?  238 ASP A OD1   1 
ATOM   1917  O  OD2   . ASP A 1 238 ? 120.181 135.933 121.444 1.00 56.24 -1 238 ASP A OD2   1 
ATOM   1918  N  N     . GLN A 1 239 ? 120.888 140.497 118.657 1.00 65.05 ?  239 GLN A N     1 
ATOM   1919  C  CA    . GLN A 1 239 ? 119.935 141.130 117.740 1.00 64.51 ?  239 GLN A CA    1 
ATOM   1920  C  C     . GLN A 1 239 ? 118.489 140.832 118.131 1.00 64.87 ?  239 GLN A C     1 
ATOM   1921  O  O     . GLN A 1 239 ? 117.663 140.453 117.297 1.00 64.37 ?  239 GLN A O     1 
ATOM   1922  C  CB    . GLN A 1 239 ? 120.198 140.711 116.292 1.00 64.27 ?  239 GLN A CB    1 
ATOM   1923  C  CG    . GLN A 1 239 ? 121.245 141.537 115.575 1.00 63.60 ?  239 GLN A CG    1 
ATOM   1924  C  CD    . GLN A 1 239 ? 120.948 141.682 114.094 1.00 65.72 ?  239 GLN A CD    1 
ATOM   1925  O  OE1   . GLN A 1 239 ? 119.818 141.972 113.702 1.00 65.94 ?  239 GLN A OE1   1 
ATOM   1926  N  NE2   . GLN A 1 239 ? 121.962 141.473 113.262 1.00 64.99 ?  239 GLN A NE2   1 
ATOM   1927  N  N     . MET A 1 240 ? 118.183 141.010 119.417 1.00 68.51 ?  240 MET A N     1 
ATOM   1928  C  CA    . MET A 1 240 ? 116.841 140.767 119.947 1.00 68.14 ?  240 MET A CA    1 
ATOM   1929  C  C     . MET A 1 240 ? 116.386 139.336 119.670 1.00 69.94 ?  240 MET A C     1 
ATOM   1930  O  O     . MET A 1 240 ? 115.230 139.088 119.319 1.00 68.89 ?  240 MET A O     1 
ATOM   1931  C  CB    . MET A 1 240 ? 115.834 141.775 119.386 1.00 66.92 ?  240 MET A CB    1 
ATOM   1932  C  CG    . MET A 1 240 ? 116.007 143.195 119.897 1.00 68.38 ?  240 MET A CG    1 
ATOM   1933  S  SD    . MET A 1 240 ? 117.709 143.780 119.820 1.00 73.97 ?  240 MET A SD    1 
ATOM   1934  C  CE    . MET A 1 240 ? 117.443 145.550 119.781 1.00 65.29 ?  240 MET A CE    1 
ATOM   1935  N  N     . GLY A 1 241 ? 117.302 138.387 119.826 1.00 69.79 ?  241 GLY A N     1 
ATOM   1936  C  CA    . GLY A 1 241 ? 116.986 136.987 119.601 1.00 68.54 ?  241 GLY A CA    1 
ATOM   1937  C  C     . GLY A 1 241 ? 116.671 136.630 118.164 1.00 70.57 ?  241 GLY A C     1 
ATOM   1938  O  O     . GLY A 1 241 ? 115.747 135.846 117.914 1.00 71.99 ?  241 GLY A O     1 
ATOM   1939  N  N     . GLN A 1 242 ? 117.419 137.184 117.210 1.00 72.20 ?  242 GLN A N     1 
ATOM   1940  C  CA    . GLN A 1 242 ? 117.245 136.869 115.797 1.00 72.85 ?  242 GLN A CA    1 
ATOM   1941  C  C     . GLN A 1 242 ? 118.445 136.120 115.232 1.00 73.98 ?  242 GLN A C     1 
ATOM   1942  O  O     . GLN A 1 242 ? 118.287 135.044 114.650 1.00 74.28 ?  242 GLN A O     1 
ATOM   1943  C  CB    . GLN A 1 242 ? 116.986 138.154 114.999 1.00 72.37 ?  242 GLN A CB    1 
ATOM   1944  C  CG    . GLN A 1 242 ? 115.679 138.847 115.350 1.00 73.86 ?  242 GLN A CG    1 
ATOM   1945  C  CD    . GLN A 1 242 ? 115.245 139.842 114.295 1.00 75.01 ?  242 GLN A CD    1 
ATOM   1946  O  OE1   . GLN A 1 242 ? 115.814 139.897 113.204 1.00 75.76 ?  242 GLN A OE1   1 
ATOM   1947  N  NE2   . GLN A 1 242 ? 114.233 140.640 114.615 1.00 73.28 ?  242 GLN A NE2   1 
ATOM   1948  N  N     . ARG A 1 243 ? 119.649 136.664 115.393 1.00 64.01 ?  243 ARG A N     1 
ATOM   1949  C  CA    . ARG A 1 243 ? 120.875 136.013 114.959 1.00 63.58 ?  243 ARG A CA    1 
ATOM   1950  C  C     . ARG A 1 243 ? 121.796 135.824 116.155 1.00 62.97 ?  243 ARG A C     1 
ATOM   1951  O  O     . ARG A 1 243 ? 121.712 136.557 117.143 1.00 61.17 ?  243 ARG A O     1 
ATOM   1952  C  CB    . ARG A 1 243 ? 121.570 136.824 113.834 1.00 62.81 ?  243 ARG A CB    1 
ATOM   1953  C  CG    . ARG A 1 243 ? 122.066 138.239 114.196 1.00 63.98 ?  243 ARG A CG    1 
ATOM   1954  C  CD    . ARG A 1 243 ? 123.386 138.240 114.963 1.00 64.32 ?  243 ARG A CD    1 
ATOM   1955  N  NE    . ARG A 1 243 ? 123.827 139.575 115.348 1.00 65.06 ?  243 ARG A NE    1 
ATOM   1956  C  CZ    . ARG A 1 243 ? 124.777 140.259 114.727 1.00 64.23 ?  243 ARG A CZ    1 
ATOM   1957  N  NH1   . ARG A 1 243 ? 125.404 139.769 113.669 1.00 63.32 1  243 ARG A NH1   1 
ATOM   1958  N  NH2   . ARG A 1 243 ? 125.111 141.464 115.180 1.00 60.04 ?  243 ARG A NH2   1 
ATOM   1959  N  N     . GLN A 1 244 ? 122.679 134.833 116.060 1.00 64.35 ?  244 GLN A N     1 
ATOM   1960  C  CA    . GLN A 1 244 ? 123.640 134.590 117.127 1.00 62.85 ?  244 GLN A CA    1 
ATOM   1961  C  C     . GLN A 1 244 ? 124.663 135.718 117.177 1.00 62.96 ?  244 GLN A C     1 
ATOM   1962  O  O     . GLN A 1 244 ? 125.270 136.062 116.159 1.00 60.03 ?  244 GLN A O     1 
ATOM   1963  C  CB    . GLN A 1 244 ? 124.344 133.251 116.917 1.00 60.75 ?  244 GLN A CB    1 
ATOM   1964  C  CG    . GLN A 1 244 ? 123.511 132.038 117.294 1.00 62.26 ?  244 GLN A CG    1 
ATOM   1965  C  CD    . GLN A 1 244 ? 124.367 130.830 117.625 1.00 64.17 ?  244 GLN A CD    1 
ATOM   1966  O  OE1   . GLN A 1 244 ? 125.364 130.558 116.955 1.00 64.37 ?  244 GLN A OE1   1 
ATOM   1967  N  NE2   . GLN A 1 244 ? 123.981 130.099 118.664 1.00 61.33 ?  244 GLN A NE2   1 
ATOM   1968  N  N     . GLY A 1 245 ? 124.860 136.285 118.366 1.00 50.20 ?  245 GLY A N     1 
ATOM   1969  C  CA    . GLY A 1 245 ? 125.803 137.373 118.539 1.00 46.90 ?  245 GLY A CA    1 
ATOM   1970  C  C     . GLY A 1 245 ? 127.209 136.993 118.125 1.00 45.73 ?  245 GLY A C     1 
ATOM   1971  O  O     . GLY A 1 245 ? 127.784 136.038 118.653 1.00 43.83 ?  245 GLY A O     1 
ATOM   1972  N  N     . SER A 1 246 ? 127.774 137.741 117.181 1.00 40.73 ?  246 SER A N     1 
ATOM   1973  C  CA    . SER A 1 246 ? 129.059 137.416 116.578 1.00 32.62 ?  246 SER A CA    1 
ATOM   1974  C  C     . SER A 1 246 ? 130.089 138.455 116.997 1.00 31.43 ?  246 SER A C     1 
ATOM   1975  O  O     . SER A 1 246 ? 129.886 139.656 116.789 1.00 30.78 ?  246 SER A O     1 
ATOM   1976  C  CB    . SER A 1 246 ? 128.947 137.356 115.056 1.00 32.71 ?  246 SER A CB    1 
ATOM   1977  O  OG    . SER A 1 246 ? 128.099 136.297 114.647 1.00 44.32 ?  246 SER A OG    1 
ATOM   1978  N  N     . GLY A 1 247 ? 131.189 137.988 117.581 1.00 28.96 ?  247 GLY A N     1 
ATOM   1979  C  CA    . GLY A 1 247 ? 132.270 138.868 117.963 1.00 13.13 ?  247 GLY A CA    1 
ATOM   1980  C  C     . GLY A 1 247 ? 133.607 138.229 117.651 1.00 15.41 ?  247 GLY A C     1 
ATOM   1981  O  O     . GLY A 1 247 ? 133.728 137.007 117.531 1.00 23.68 ?  247 GLY A O     1 
ATOM   1982  N  N     . ALA A 1 248 ? 134.614 139.083 117.518 1.00 17.67 ?  248 ALA A N     1 
ATOM   1983  C  CA    . ALA A 1 248 ? 135.972 138.654 117.235 1.00 14.46 ?  248 ALA A CA    1 
ATOM   1984  C  C     . ALA A 1 248 ? 136.925 139.309 118.220 1.00 12.56 ?  248 ALA A C     1 
ATOM   1985  O  O     . ALA A 1 248 ? 136.723 140.450 118.640 1.00 16.39 ?  248 ALA A O     1 
ATOM   1986  C  CB    . ALA A 1 248 ? 136.389 138.997 115.798 1.00 8.12  ?  248 ALA A CB    1 
ATOM   1987  N  N     . ALA A 1 249 ? 137.966 138.571 118.588 1.00 16.30 ?  249 ALA A N     1 
ATOM   1988  C  CA    . ALA A 1 249 ? 139.024 139.072 119.452 1.00 5.45  ?  249 ALA A CA    1 
ATOM   1989  C  C     . ALA A 1 249 ? 140.357 138.868 118.752 1.00 11.13 ?  249 ALA A C     1 
ATOM   1990  O  O     . ALA A 1 249 ? 140.639 137.775 118.254 1.00 19.26 ?  249 ALA A O     1 
ATOM   1991  C  CB    . ALA A 1 249 ? 139.016 138.365 120.809 1.00 13.03 ?  249 ALA A CB    1 
ATOM   1992  N  N     . TYR A 1 250 ? 141.169 139.917 118.706 1.00 15.80 ?  250 TYR A N     1 
ATOM   1993  C  CA    . TYR A 1 250 ? 142.476 139.863 118.072 1.00 9.77  ?  250 TYR A CA    1 
ATOM   1994  C  C     . TYR A 1 250 ? 143.560 140.048 119.121 1.00 6.64  ?  250 TYR A C     1 
ATOM   1995  O  O     . TYR A 1 250 ? 143.472 140.948 119.962 1.00 17.12 ?  250 TYR A O     1 
ATOM   1996  C  CB    . TYR A 1 250 ? 142.605 140.926 116.983 1.00 10.64 ?  250 TYR A CB    1 
ATOM   1997  C  CG    . TYR A 1 250 ? 142.033 140.502 115.651 1.00 17.03 ?  250 TYR A CG    1 
ATOM   1998  C  CD1   . TYR A 1 250 ? 140.666 140.528 115.424 1.00 11.39 ?  250 TYR A CD1   1 
ATOM   1999  C  CD2   . TYR A 1 250 ? 142.861 140.070 114.624 1.00 13.62 ?  250 TYR A CD2   1 
ATOM   2000  C  CE1   . TYR A 1 250 ? 140.138 140.142 114.212 1.00 5.03  ?  250 TYR A CE1   1 
ATOM   2001  C  CE2   . TYR A 1 250 ? 142.341 139.680 113.408 1.00 9.66  ?  250 TYR A CE2   1 
ATOM   2002  C  CZ    . TYR A 1 250 ? 140.979 139.718 113.207 1.00 8.96  ?  250 TYR A CZ    1 
ATOM   2003  O  OH    . TYR A 1 250 ? 140.454 139.334 111.997 1.00 16.52 ?  250 TYR A OH    1 
ATOM   2004  N  N     . LEU A 1 251 ? 144.573 139.193 119.069 1.00 11.05 ?  251 LEU A N     1 
ATOM   2005  C  CA    . LEU A 1 251 ? 145.714 139.268 119.963 1.00 13.94 ?  251 LEU A CA    1 
ATOM   2006  C  C     . LEU A 1 251 ? 146.993 139.191 119.148 1.00 11.63 ?  251 LEU A C     1 
ATOM   2007  O  O     . LEU A 1 251 ? 147.090 138.401 118.206 1.00 16.73 ?  251 LEU A O     1 
ATOM   2008  C  CB    . LEU A 1 251 ? 145.690 138.142 120.999 1.00 17.48 ?  251 LEU A CB    1 
ATOM   2009  C  CG    . LEU A 1 251 ? 146.544 138.369 122.245 1.00 12.99 ?  251 LEU A CG    1 
ATOM   2010  C  CD1   . LEU A 1 251 ? 145.867 139.353 123.178 1.00 18.08 ?  251 LEU A CD1   1 
ATOM   2011  C  CD2   . LEU A 1 251 ? 146.819 137.057 122.952 1.00 13.39 ?  251 LEU A CD2   1 
ATOM   2012  N  N     . ASN A 1 252 ? 147.967 140.019 119.509 1.00 15.94 ?  252 ASN A N     1 
ATOM   2013  C  CA    . ASN A 1 252 ? 149.278 139.930 118.886 1.00 12.87 ?  252 ASN A CA    1 
ATOM   2014  C  C     . ASN A 1 252 ? 149.950 138.623 119.279 1.00 14.42 ?  252 ASN A C     1 
ATOM   2015  O  O     . ASN A 1 252 ? 149.805 138.145 120.407 1.00 25.53 ?  252 ASN A O     1 
ATOM   2016  C  CB    . ASN A 1 252 ? 150.143 141.120 119.293 1.00 15.10 ?  252 ASN A CB    1 
ATOM   2017  C  CG    . ASN A 1 252 ? 151.240 141.407 118.292 1.00 20.40 ?  252 ASN A CG    1 
ATOM   2018  O  OD1   . ASN A 1 252 ? 152.260 140.720 118.258 1.00 25.03 ?  252 ASN A OD1   1 
ATOM   2019  N  ND2   . ASN A 1 252 ? 151.030 142.418 117.459 1.00 17.33 ?  252 ASN A ND2   1 
ATOM   2020  N  N     . ILE A 1 253 ? 150.688 138.035 118.334 1.00 13.59 ?  253 ILE A N     1 
ATOM   2021  C  CA    . ILE A 1 253 ? 151.317 136.746 118.587 1.00 20.79 ?  253 ILE A CA    1 
ATOM   2022  C  C     . ILE A 1 253 ? 152.442 136.854 119.609 1.00 23.63 ?  253 ILE A C     1 
ATOM   2023  O  O     . ILE A 1 253 ? 152.855 135.836 120.177 1.00 25.79 ?  253 ILE A O     1 
ATOM   2024  C  CB    . ILE A 1 253 ? 151.819 136.128 117.268 1.00 19.47 ?  253 ILE A CB    1 
ATOM   2025  C  CG1   . ILE A 1 253 ? 151.923 134.608 117.399 1.00 23.14 ?  253 ILE A CG1   1 
ATOM   2026  C  CG2   . ILE A 1 253 ? 153.150 136.738 116.857 1.00 13.69 ?  253 ILE A CG2   1 
ATOM   2027  C  CD1   . ILE A 1 253 ? 151.737 133.868 116.103 1.00 21.73 ?  253 ILE A CD1   1 
ATOM   2028  N  N     . PHE A 1 254 ? 152.946 138.058 119.869 1.00 22.21 ?  254 PHE A N     1 
ATOM   2029  C  CA    . PHE A 1 254 ? 153.973 138.261 120.881 1.00 15.92 ?  254 PHE A CA    1 
ATOM   2030  C  C     . PHE A 1 254 ? 153.391 138.549 122.258 1.00 21.42 ?  254 PHE A C     1 
ATOM   2031  O  O     . PHE A 1 254 ? 154.149 138.647 123.228 1.00 29.46 ?  254 PHE A O     1 
ATOM   2032  C  CB    . PHE A 1 254 ? 154.913 139.392 120.453 1.00 22.92 ?  254 PHE A CB    1 
ATOM   2033  C  CG    . PHE A 1 254 ? 155.923 138.974 119.421 1.00 26.00 ?  254 PHE A CG    1 
ATOM   2034  C  CD1   . PHE A 1 254 ? 156.932 138.081 119.741 1.00 25.65 ?  254 PHE A CD1   1 
ATOM   2035  C  CD2   . PHE A 1 254 ? 155.850 139.455 118.126 1.00 23.77 ?  254 PHE A CD2   1 
ATOM   2036  C  CE1   . PHE A 1 254 ? 157.857 137.689 118.794 1.00 28.02 ?  254 PHE A CE1   1 
ATOM   2037  C  CE2   . PHE A 1 254 ? 156.771 139.065 117.173 1.00 26.10 ?  254 PHE A CE2   1 
ATOM   2038  C  CZ    . PHE A 1 254 ? 157.776 138.182 117.509 1.00 27.05 ?  254 PHE A CZ    1 
ATOM   2039  N  N     . HIS A 1 255 ? 152.073 138.697 122.361 1.00 26.58 ?  255 HIS A N     1 
ATOM   2040  C  CA    . HIS A 1 255 ? 151.417 138.710 123.660 1.00 17.25 ?  255 HIS A CA    1 
ATOM   2041  C  C     . HIS A 1 255 ? 151.599 137.353 124.325 1.00 19.54 ?  255 HIS A C     1 
ATOM   2042  O  O     . HIS A 1 255 ? 151.557 136.313 123.664 1.00 28.90 ?  255 HIS A O     1 
ATOM   2043  C  CB    . HIS A 1 255 ? 149.932 139.030 123.491 1.00 19.06 ?  255 HIS A CB    1 
ATOM   2044  C  CG    . HIS A 1 255 ? 149.237 139.414 124.760 1.00 23.16 ?  255 HIS A CG    1 
ATOM   2045  N  ND1   . HIS A 1 255 ? 148.959 138.512 125.763 1.00 21.46 ?  255 HIS A ND1   1 
ATOM   2046  C  CD2   . HIS A 1 255 ? 148.740 140.602 125.175 1.00 15.99 ?  255 HIS A CD2   1 
ATOM   2047  C  CE1   . HIS A 1 255 ? 148.334 139.131 126.748 1.00 16.84 ?  255 HIS A CE1   1 
ATOM   2048  N  NE2   . HIS A 1 255 ? 148.188 140.401 126.416 1.00 13.24 ?  255 HIS A NE2   1 
ATOM   2049  N  N     . ARG A 1 256 ? 151.812 137.360 125.642 1.00 21.55 ?  256 ARG A N     1 
ATOM   2050  C  CA    . ARG A 1 256 ? 152.139 136.111 126.319 1.00 21.81 ?  256 ARG A CA    1 
ATOM   2051  C  C     . ARG A 1 256 ? 150.943 135.170 126.356 1.00 27.23 ?  256 ARG A C     1 
ATOM   2052  O  O     . ARG A 1 256 ? 151.108 133.945 126.317 1.00 30.87 ?  256 ARG A O     1 
ATOM   2053  C  CB    . ARG A 1 256 ? 152.630 136.384 127.734 1.00 24.98 ?  256 ARG A CB    1 
ATOM   2054  C  CG    . ARG A 1 256 ? 153.281 135.176 128.363 1.00 29.78 ?  256 ARG A CG    1 
ATOM   2055  C  CD    . ARG A 1 256 ? 152.809 134.954 129.776 1.00 30.42 ?  256 ARG A CD    1 
ATOM   2056  N  NE    . ARG A 1 256 ? 151.360 135.042 129.903 1.00 29.67 ?  256 ARG A NE    1 
ATOM   2057  C  CZ    . ARG A 1 256 ? 150.581 134.002 130.163 1.00 31.62 ?  256 ARG A CZ    1 
ATOM   2058  N  NH1   . ARG A 1 256 ? 151.081 132.791 130.337 1.00 32.60 1  256 ARG A NH1   1 
ATOM   2059  N  NH2   . ARG A 1 256 ? 149.269 134.184 130.261 1.00 33.08 ?  256 ARG A NH2   1 
ATOM   2060  N  N     . ASP A 1 257 ? 149.735 135.718 126.427 1.00 22.54 ?  257 ASP A N     1 
ATOM   2061  C  CA    . ASP A 1 257 ? 148.507 134.926 126.463 1.00 19.25 ?  257 ASP A CA    1 
ATOM   2062  C  C     . ASP A 1 257 ? 148.209 134.228 125.158 1.00 24.96 ?  257 ASP A C     1 
ATOM   2063  O  O     . ASP A 1 257 ? 147.168 133.557 125.105 1.00 32.70 ?  257 ASP A O     1 
ATOM   2064  C  CB    . ASP A 1 257 ? 147.319 135.812 126.838 1.00 21.68 ?  257 ASP A CB    1 
ATOM   2065  C  CG    . ASP A 1 257 ? 147.283 136.157 128.309 1.00 30.64 ?  257 ASP A CG    1 
ATOM   2066  O  OD1   . ASP A 1 257 ? 147.914 135.437 129.107 1.00 28.10 ?  257 ASP A OD1   1 
ATOM   2067  O  OD2   . ASP A 1 257 ? 146.611 137.144 128.667 1.00 34.69 -1 257 ASP A OD2   1 
ATOM   2068  N  N     . ILE A 1 258 ? 149.084 134.347 124.155 1.00 26.12 ?  258 ILE A N     1 
ATOM   2069  C  CA    . ILE A 1 258 ? 148.755 133.894 122.807 1.00 25.64 ?  258 ILE A CA    1 
ATOM   2070  C  C     . ILE A 1 258 ? 148.383 132.417 122.808 1.00 23.84 ?  258 ILE A C     1 
ATOM   2071  O  O     . ILE A 1 258 ? 147.464 131.997 122.099 1.00 32.27 ?  258 ILE A O     1 
ATOM   2072  C  CB    . ILE A 1 258 ? 149.916 134.197 121.838 1.00 22.86 ?  258 ILE A CB    1 
ATOM   2073  C  CG1   . ILE A 1 258 ? 149.511 133.873 120.398 1.00 25.32 ?  258 ILE A CG1   1 
ATOM   2074  C  CG2   . ILE A 1 258 ? 151.186 133.452 122.236 1.00 19.03 ?  258 ILE A CG2   1 
ATOM   2075  C  CD1   . ILE A 1 258 ? 148.311 134.658 119.923 1.00 18.76 ?  258 ILE A CD1   1 
ATOM   2076  N  N     . ASN A 1 259 ? 149.077 131.609 123.611 1.00 23.42 ?  259 ASN A N     1 
ATOM   2077  C  CA    . ASN A 1 259 ? 148.723 130.197 123.702 1.00 23.87 ?  259 ASN A CA    1 
ATOM   2078  C  C     . ASN A 1 259 ? 147.353 130.022 124.342 1.00 27.63 ?  259 ASN A C     1 
ATOM   2079  O  O     . ASN A 1 259 ? 146.472 129.361 123.776 1.00 29.97 ?  259 ASN A O     1 
ATOM   2080  C  CB    . ASN A 1 259 ? 149.793 129.440 124.487 1.00 25.62 ?  259 ASN A CB    1 
ATOM   2081  C  CG    . ASN A 1 259 ? 151.065 129.239 123.689 1.00 30.57 ?  259 ASN A CG    1 
ATOM   2082  O  OD1   . ASN A 1 259 ? 151.084 128.498 122.706 1.00 31.68 ?  259 ASN A OD1   1 
ATOM   2083  N  ND2   . ASN A 1 259 ? 152.135 129.904 124.106 1.00 27.56 ?  259 ASN A ND2   1 
ATOM   2084  N  N     . ASP A 1 260 ? 147.136 130.651 125.501 1.00 26.94 ?  260 ASP A N     1 
ATOM   2085  C  CA    . ASP A 1 260 ? 145.845 130.543 126.173 1.00 26.40 ?  260 ASP A CA    1 
ATOM   2086  C  C     . ASP A 1 260 ? 144.735 131.095 125.290 1.00 21.16 ?  260 ASP A C     1 
ATOM   2087  O  O     . ASP A 1 260 ? 143.667 130.485 125.160 1.00 27.71 ?  260 ASP A O     1 
ATOM   2088  C  CB    . ASP A 1 260 ? 145.888 131.275 127.514 1.00 26.24 ?  260 ASP A CB    1 
ATOM   2089  C  CG    . ASP A 1 260 ? 147.154 130.991 128.295 1.00 36.42 ?  260 ASP A CG    1 
ATOM   2090  O  OD1   . ASP A 1 260 ? 147.614 131.891 129.028 1.00 35.80 ?  260 ASP A OD1   1 
ATOM   2091  O  OD2   . ASP A 1 260 ? 147.687 129.869 128.178 1.00 35.91 -1 260 ASP A OD2   1 
ATOM   2092  N  N     . PHE A 1 261 ? 144.980 132.253 124.674 1.00 26.31 ?  261 PHE A N     1 
ATOM   2093  C  CA    . PHE A 1 261 ? 144.144 132.768 123.597 1.00 23.74 ?  261 PHE A CA    1 
ATOM   2094  C  C     . PHE A 1 261 ? 143.776 131.659 122.620 1.00 20.08 ?  261 PHE A C     1 
ATOM   2095  O  O     . PHE A 1 261 ? 142.598 131.323 122.447 1.00 21.56 ?  261 PHE A O     1 
ATOM   2096  C  CB    . PHE A 1 261 ? 144.901 133.901 122.893 1.00 16.16 ?  261 PHE A CB    1 
ATOM   2097  C  CG    . PHE A 1 261 ? 144.099 134.637 121.860 1.00 22.45 ?  261 PHE A CG    1 
ATOM   2098  C  CD1   . PHE A 1 261 ? 143.174 135.594 122.234 1.00 18.74 ?  261 PHE A CD1   1 
ATOM   2099  C  CD2   . PHE A 1 261 ? 144.303 134.402 120.512 1.00 23.64 ?  261 PHE A CD2   1 
ATOM   2100  C  CE1   . PHE A 1 261 ? 142.446 136.281 121.286 1.00 13.75 ?  261 PHE A CE1   1 
ATOM   2101  C  CE2   . PHE A 1 261 ? 143.581 135.089 119.560 1.00 15.00 ?  261 PHE A CE2   1 
ATOM   2102  C  CZ    . PHE A 1 261 ? 142.652 136.030 119.948 1.00 18.00 ?  261 PHE A CZ    1 
ATOM   2103  N  N     . LEU A 1 262 ? 144.795 131.038 122.019 1.00 26.08 ?  262 LEU A N     1 
ATOM   2104  C  CA    . LEU A 1 262 ? 144.545 129.955 121.074 1.00 23.94 ?  262 LEU A CA    1 
ATOM   2105  C  C     . LEU A 1 262 ? 143.853 128.785 121.757 1.00 29.96 ?  262 LEU A C     1 
ATOM   2106  O  O     . LEU A 1 262 ? 142.990 128.128 121.161 1.00 28.96 ?  262 LEU A O     1 
ATOM   2107  C  CB    . LEU A 1 262 ? 145.859 129.510 120.436 1.00 23.93 ?  262 LEU A CB    1 
ATOM   2108  C  CG    . LEU A 1 262 ? 146.551 130.527 119.530 1.00 25.30 ?  262 LEU A CG    1 
ATOM   2109  C  CD1   . LEU A 1 262 ? 147.853 129.959 118.997 1.00 27.68 ?  262 LEU A CD1   1 
ATOM   2110  C  CD2   . LEU A 1 262 ? 145.637 130.950 118.396 1.00 23.46 ?  262 LEU A CD2   1 
ATOM   2111  N  N     . ASP A 1 263 ? 144.192 128.535 123.024 1.00 35.28 ?  263 ASP A N     1 
ATOM   2112  C  CA    . ASP A 1 263 ? 143.577 127.434 123.752 1.00 29.88 ?  263 ASP A CA    1 
ATOM   2113  C  C     . ASP A 1 263 ? 142.079 127.632 123.927 1.00 31.41 ?  263 ASP A C     1 
ATOM   2114  O  O     . ASP A 1 263 ? 141.375 126.675 124.265 1.00 39.37 ?  263 ASP A O     1 
ATOM   2115  C  CB    . ASP A 1 263 ? 144.244 127.266 125.118 1.00 33.59 ?  263 ASP A CB    1 
ATOM   2116  C  CG    . ASP A 1 263 ? 145.621 126.644 125.018 1.00 38.24 ?  263 ASP A CG    1 
ATOM   2117  O  OD1   . ASP A 1 263 ? 145.925 126.033 123.973 1.00 38.59 ?  263 ASP A OD1   1 
ATOM   2118  O  OD2   . ASP A 1 263 ? 146.399 126.764 125.988 1.00 38.50 -1 263 ASP A OD2   1 
ATOM   2119  N  N     . THR A 1 264 ? 141.575 128.849 123.708 1.00 34.25 ?  264 THR A N     1 
ATOM   2120  C  CA    . THR A 1 264 ? 140.137 129.062 123.788 1.00 32.61 ?  264 THR A CA    1 
ATOM   2121  C  C     . THR A 1 264 ? 139.388 128.392 122.645 1.00 37.29 ?  264 THR A C     1 
ATOM   2122  O  O     . THR A 1 264 ? 138.169 128.220 122.740 1.00 40.05 ?  264 THR A O     1 
ATOM   2123  C  CB    . THR A 1 264 ? 139.823 130.557 123.805 1.00 35.07 ?  264 THR A CB    1 
ATOM   2124  O  OG1   . THR A 1 264 ? 140.347 131.170 122.621 1.00 39.96 ?  264 THR A OG1   1 
ATOM   2125  C  CG2   . THR A 1 264 ? 140.440 131.213 125.030 1.00 31.28 ?  264 THR A CG2   1 
ATOM   2126  N  N     . LYS A 1 265 ? 140.080 128.009 121.571 1.00 36.99 ?  265 LYS A N     1 
ATOM   2127  C  CA    . LYS A 1 265 ? 139.434 127.383 120.426 1.00 36.97 ?  265 LYS A CA    1 
ATOM   2128  C  C     . LYS A 1 265 ? 139.676 125.884 120.335 1.00 39.83 ?  265 LYS A C     1 
ATOM   2129  O  O     . LYS A 1 265 ? 139.151 125.244 119.417 1.00 43.53 ?  265 LYS A O     1 
ATOM   2130  C  CB    . LYS A 1 265 ? 139.887 128.055 119.126 1.00 37.82 ?  265 LYS A CB    1 
ATOM   2131  C  CG    . LYS A 1 265 ? 139.154 129.344 118.816 1.00 37.62 ?  265 LYS A CG    1 
ATOM   2132  C  CD    . LYS A 1 265 ? 137.659 129.185 119.006 1.00 39.31 ?  265 LYS A CD    1 
ATOM   2133  C  CE    . LYS A 1 265 ? 136.934 130.493 118.770 1.00 36.10 ?  265 LYS A CE    1 
ATOM   2134  N  NZ    . LYS A 1 265 ? 135.507 130.412 119.181 1.00 37.78 1  265 LYS A NZ    1 
ATOM   2135  N  N     . LYS A 1 266 ? 140.449 125.307 121.248 1.00 45.49 ?  266 LYS A N     1 
ATOM   2136  C  CA    . LYS A 1 266 ? 140.651 123.866 121.236 1.00 46.34 ?  266 LYS A CA    1 
ATOM   2137  C  C     . LYS A 1 266 ? 139.399 123.147 121.721 1.00 50.98 ?  266 LYS A C     1 
ATOM   2138  O  O     . LYS A 1 266 ? 138.677 123.627 122.600 1.00 50.36 ?  266 LYS A O     1 
ATOM   2139  C  CB    . LYS A 1 266 ? 141.851 123.485 122.101 1.00 44.07 ?  266 LYS A CB    1 
ATOM   2140  C  CG    . LYS A 1 266 ? 143.189 123.677 121.408 1.00 47.04 ?  266 LYS A CG    1 
ATOM   2141  C  CD    . LYS A 1 266 ? 144.340 123.169 122.258 1.00 48.02 ?  266 LYS A CD    1 
ATOM   2142  C  CE    . LYS A 1 266 ? 145.640 123.169 121.469 1.00 48.71 ?  266 LYS A CE    1 
ATOM   2143  N  NZ    . LYS A 1 266 ? 146.827 122.955 122.342 1.00 47.04 1  266 LYS A NZ    1 
ATOM   2144  N  N     . ILE A 1 267 ? 139.137 121.983 121.124 1.00 57.94 ?  267 ILE A N     1 
ATOM   2145  C  CA    . ILE A 1 267 ? 137.975 121.191 121.518 1.00 59.55 ?  267 ILE A CA    1 
ATOM   2146  C  C     . ILE A 1 267 ? 138.155 120.647 122.929 1.00 59.12 ?  267 ILE A C     1 
ATOM   2147  O  O     . ILE A 1 267 ? 137.191 120.544 123.698 1.00 57.17 ?  267 ILE A O     1 
ATOM   2148  C  CB    . ILE A 1 267 ? 137.727 120.063 120.501 1.00 59.00 ?  267 ILE A CB    1 
ATOM   2149  C  CG1   . ILE A 1 267 ? 137.347 120.646 119.137 1.00 59.81 ?  267 ILE A CG1   1 
ATOM   2150  C  CG2   . ILE A 1 267 ? 136.643 119.124 121.006 1.00 57.14 ?  267 ILE A CG2   1 
ATOM   2151  C  CD1   . ILE A 1 267 ? 138.492 120.688 118.147 1.00 59.86 ?  267 ILE A CD1   1 
ATOM   2152  N  N     . SER A 1 268 ? 139.388 120.290 123.294 1.00 60.20 ?  268 SER A N     1 
ATOM   2153  C  CA    . SER A 1 268 ? 139.668 119.748 124.618 1.00 63.53 ?  268 SER A CA    1 
ATOM   2154  C  C     . SER A 1 268 ? 139.609 120.801 125.718 1.00 64.19 ?  268 SER A C     1 
ATOM   2155  O  O     . SER A 1 268 ? 139.695 120.440 126.897 1.00 63.68 ?  268 SER A O     1 
ATOM   2156  C  CB    . SER A 1 268 ? 141.042 119.075 124.627 1.00 63.60 ?  268 SER A CB    1 
ATOM   2157  O  OG    . SER A 1 268 ? 142.060 119.992 124.268 1.00 62.10 ?  268 SER A OG    1 
ATOM   2158  N  N     . ALA A 1 269 ? 139.474 122.078 125.368 1.00 66.10 ?  269 ALA A N     1 
ATOM   2159  C  CA    . ALA A 1 269 ? 139.435 123.133 126.370 1.00 65.74 ?  269 ALA A CA    1 
ATOM   2160  C  C     . ALA A 1 269 ? 138.217 122.981 127.274 1.00 66.79 ?  269 ALA A C     1 
ATOM   2161  O  O     . ALA A 1 269 ? 137.141 122.560 126.842 1.00 64.71 ?  269 ALA A O     1 
ATOM   2162  C  CB    . ALA A 1 269 ? 139.417 124.507 125.697 1.00 61.65 ?  269 ALA A CB    1 
ATOM   2163  N  N     . ASP A 1 270 ? 138.399 123.329 128.545 1.00 73.17 ?  270 ASP A N     1 
ATOM   2164  C  CA    . ASP A 1 270 ? 137.328 123.221 129.520 1.00 73.06 ?  270 ASP A CA    1 
ATOM   2165  C  C     . ASP A 1 270 ? 136.291 124.324 129.305 1.00 73.22 ?  270 ASP A C     1 
ATOM   2166  O  O     . ASP A 1 270 ? 136.463 125.232 128.486 1.00 73.93 ?  270 ASP A O     1 
ATOM   2167  C  CB    . ASP A 1 270 ? 137.886 123.287 130.941 1.00 73.27 ?  270 ASP A CB    1 
ATOM   2168  C  CG    . ASP A 1 270 ? 139.150 122.467 131.109 1.00 74.95 ?  270 ASP A CG    1 
ATOM   2169  O  OD1   . ASP A 1 270 ? 139.288 121.439 130.415 1.00 74.46 ?  270 ASP A OD1   1 
ATOM   2170  O  OD2   . ASP A 1 270 ? 140.003 122.851 131.937 1.00 73.37 -1 270 ASP A OD2   1 
ATOM   2171  N  N     . GLU A 1 271 ? 135.195 124.231 130.062 1.00 74.54 ?  271 GLU A N     1 
ATOM   2172  C  CA    . GLU A 1 271 ? 134.112 125.200 129.923 1.00 75.66 ?  271 GLU A CA    1 
ATOM   2173  C  C     . GLU A 1 271 ? 134.522 126.587 130.402 1.00 75.28 ?  271 GLU A C     1 
ATOM   2174  O  O     . GLU A 1 271 ? 133.982 127.589 129.922 1.00 74.37 ?  271 GLU A O     1 
ATOM   2175  C  CB    . GLU A 1 271 ? 132.878 124.718 130.686 1.00 74.59 ?  271 GLU A CB    1 
ATOM   2176  C  CG    . GLU A 1 271 ? 132.363 123.357 130.241 1.00 75.40 ?  271 GLU A CG    1 
ATOM   2177  C  CD    . GLU A 1 271 ? 132.292 123.222 128.731 1.00 76.58 ?  271 GLU A CD    1 
ATOM   2178  O  OE1   . GLU A 1 271 ? 131.706 124.111 128.077 1.00 75.75 ?  271 GLU A OE1   1 
ATOM   2179  O  OE2   . GLU A 1 271 ? 132.822 122.225 128.197 1.00 74.84 -1 271 GLU A OE2   1 
ATOM   2180  N  N     . ASP A 1 272 ? 135.465 126.668 131.336 1.00 69.39 ?  272 ASP A N     1 
ATOM   2181  C  CA    . ASP A 1 272 ? 135.960 127.947 131.827 1.00 70.33 ?  272 ASP A CA    1 
ATOM   2182  C  C     . ASP A 1 272 ? 137.089 128.508 130.973 1.00 70.67 ?  272 ASP A C     1 
ATOM   2183  O  O     . ASP A 1 272 ? 137.637 129.561 131.309 1.00 68.52 ?  272 ASP A O     1 
ATOM   2184  C  CB    . ASP A 1 272 ? 136.426 127.815 133.281 1.00 70.43 ?  272 ASP A CB    1 
ATOM   2185  C  CG    . ASP A 1 272 ? 137.641 126.919 133.428 1.00 71.48 ?  272 ASP A CG    1 
ATOM   2186  O  OD1   . ASP A 1 272 ? 137.845 126.043 132.563 1.00 70.47 ?  272 ASP A OD1   1 
ATOM   2187  O  OD2   . ASP A 1 272 ? 138.393 127.093 134.409 1.00 70.07 -1 272 ASP A OD2   1 
ATOM   2188  N  N     . VAL A 1 273 ? 137.455 127.824 129.887 1.00 65.21 ?  273 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 273 ? 138.514 128.267 128.994 1.00 64.67 ?  273 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 273 ? 137.987 128.575 127.599 1.00 62.53 ?  273 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 273 ? 138.381 129.575 126.987 1.00 65.25 ?  273 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 273 ? 139.651 127.222 128.925 1.00 66.28 ?  273 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 273 ? 140.619 127.544 127.796 1.00 63.57 ?  273 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 273 ? 140.381 127.145 130.256 1.00 64.79 ?  273 VAL A CG2   1 
ATOM   2195  N  N     . ARG A 1 274 ? 137.081 127.748 127.085 1.00 60.44 ?  274 ARG A N     1 
ATOM   2196  C  CA    . ARG A 1 274 ? 136.629 127.864 125.706 1.00 59.82 ?  274 ARG A CA    1 
ATOM   2197  C  C     . ARG A 1 274 ? 135.564 128.946 125.569 1.00 58.10 ?  274 ARG A C     1 
ATOM   2198  O  O     . ARG A 1 274 ? 134.635 129.023 126.379 1.00 58.12 ?  274 ARG A O     1 
ATOM   2199  C  CB    . ARG A 1 274 ? 136.080 126.523 125.219 1.00 59.95 ?  274 ARG A CB    1 
ATOM   2200  C  CG    . ARG A 1 274 ? 135.144 126.625 124.025 1.00 58.60 ?  274 ARG A CG    1 
ATOM   2201  C  CD    . ARG A 1 274 ? 135.147 125.346 123.203 1.00 58.80 ?  274 ARG A CD    1 
ATOM   2202  N  NE    . ARG A 1 274 ? 135.071 124.154 124.039 1.00 62.16 ?  274 ARG A NE    1 
ATOM   2203  C  CZ    . ARG A 1 274 ? 133.965 123.721 124.632 1.00 63.53 ?  274 ARG A CZ    1 
ATOM   2204  N  NH1   . ARG A 1 274 ? 132.814 124.360 124.498 1.00 62.50 1  274 ARG A NH1   1 
ATOM   2205  N  NH2   . ARG A 1 274 ? 134.016 122.619 125.374 1.00 63.03 ?  274 ARG A NH2   1 
ATOM   2206  N  N     . VAL A 1 275 ? 135.703 129.780 124.540 1.00 47.64 ?  275 VAL A N     1 
ATOM   2207  C  CA    . VAL A 1 275 ? 134.688 130.750 124.149 1.00 44.89 ?  275 VAL A CA    1 
ATOM   2208  C  C     . VAL A 1 275 ? 134.092 130.290 122.825 1.00 45.72 ?  275 VAL A C     1 
ATOM   2209  O  O     . VAL A 1 275 ? 134.826 130.001 121.873 1.00 47.61 ?  275 VAL A O     1 
ATOM   2210  C  CB    . VAL A 1 275 ? 135.270 132.172 124.042 1.00 44.54 ?  275 VAL A CB    1 
ATOM   2211  C  CG1   . VAL A 1 275 ? 135.516 132.745 125.428 1.00 42.69 ?  275 VAL A CG1   1 
ATOM   2212  C  CG2   . VAL A 1 275 ? 136.562 132.170 123.242 1.00 44.81 ?  275 VAL A CG2   1 
ATOM   2213  N  N     . LYS A 1 276 ? 132.764 130.204 122.770 1.00 46.73 ?  276 LYS A N     1 
ATOM   2214  C  CA    . LYS A 1 276 ? 132.090 129.588 121.633 1.00 47.97 ?  276 LYS A CA    1 
ATOM   2215  C  C     . LYS A 1 276 ? 131.589 130.585 120.599 1.00 47.05 ?  276 LYS A C     1 
ATOM   2216  O  O     . LYS A 1 276 ? 131.649 130.293 119.400 1.00 52.80 ?  276 LYS A O     1 
ATOM   2217  C  CB    . LYS A 1 276 ? 130.911 128.734 122.118 1.00 49.01 ?  276 LYS A CB    1 
ATOM   2218  C  CG    . LYS A 1 276 ? 129.972 129.450 123.077 1.00 52.48 ?  276 LYS A CG    1 
ATOM   2219  C  CD    . LYS A 1 276 ? 129.002 128.482 123.737 1.00 50.48 ?  276 LYS A CD    1 
ATOM   2220  C  CE    . LYS A 1 276 ? 129.721 127.250 124.268 1.00 49.46 ?  276 LYS A CE    1 
ATOM   2221  N  NZ    . LYS A 1 276 ? 130.792 127.607 125.240 1.00 48.12 1  276 LYS A NZ    1 
ATOM   2222  N  N     . THR A 1 277 ? 131.099 131.749 121.019 1.00 38.15 ?  277 THR A N     1 
ATOM   2223  C  CA    . THR A 1 277 ? 130.579 132.749 120.097 1.00 38.69 ?  277 THR A CA    1 
ATOM   2224  C  C     . THR A 1 277 ? 131.560 133.884 119.847 1.00 42.36 ?  277 THR A C     1 
ATOM   2225  O  O     . THR A 1 277 ? 131.172 134.914 119.287 1.00 41.83 ?  277 THR A O     1 
ATOM   2226  C  CB    . THR A 1 277 ? 129.253 133.309 120.615 1.00 41.43 ?  277 THR A CB    1 
ATOM   2227  O  OG1   . THR A 1 277 ? 129.503 134.229 121.686 1.00 35.00 ?  277 THR A OG1   1 
ATOM   2228  C  CG2   . THR A 1 277 ? 128.359 132.183 121.109 1.00 41.22 ?  277 THR A CG2   1 
ATOM   2229  N  N     . LEU A 1 278 ? 132.816 133.725 120.250 1.00 33.87 ?  278 LEU A N     1 
ATOM   2230  C  CA    . LEU A 1 278 ? 133.843 134.744 120.066 1.00 31.20 ?  278 LEU A CA    1 
ATOM   2231  C  C     . LEU A 1 278 ? 134.894 134.210 119.103 1.00 25.43 ?  278 LEU A C     1 
ATOM   2232  O  O     . LEU A 1 278 ? 135.691 133.340 119.467 1.00 34.43 ?  278 LEU A O     1 
ATOM   2233  C  CB    . LEU A 1 278 ? 134.474 135.130 121.401 1.00 28.77 ?  278 LEU A CB    1 
ATOM   2234  C  CG    . LEU A 1 278 ? 135.283 136.427 121.417 1.00 25.02 ?  278 LEU A CG    1 
ATOM   2235  C  CD1   . LEU A 1 278 ? 134.364 137.631 121.496 1.00 24.11 ?  278 LEU A CD1   1 
ATOM   2236  C  CD2   . LEU A 1 278 ? 136.269 136.427 122.569 1.00 31.95 ?  278 LEU A CD2   1 
ATOM   2237  N  N     . SER A 1 279 ? 134.891 134.727 117.879 1.00 26.11 ?  279 SER A N     1 
ATOM   2238  C  CA    . SER A 1 279 ? 135.957 134.423 116.939 1.00 21.19 ?  279 SER A CA    1 
ATOM   2239  C  C     . SER A 1 279 ? 137.272 135.007 117.437 1.00 20.60 ?  279 SER A C     1 
ATOM   2240  O  O     . SER A 1 279 ? 137.296 135.990 118.182 1.00 33.10 ?  279 SER A O     1 
ATOM   2241  C  CB    . SER A 1 279 ? 135.626 134.981 115.556 1.00 17.65 ?  279 SER A CB    1 
ATOM   2242  O  OG    . SER A 1 279 ? 134.549 134.276 114.966 1.00 25.68 ?  279 SER A OG    1 
ATOM   2243  N  N     . ILE A 1 280 ? 138.376 134.387 117.036 1.00 18.70 ?  280 ILE A N     1 
ATOM   2244  C  CA    . ILE A 1 280 ? 139.696 134.835 117.454 1.00 22.67 ?  280 ILE A CA    1 
ATOM   2245  C  C     . ILE A 1 280 ? 140.561 135.061 116.224 1.00 23.14 ?  280 ILE A C     1 
ATOM   2246  O  O     . ILE A 1 280 ? 140.469 134.320 115.239 1.00 26.18 ?  280 ILE A O     1 
ATOM   2247  C  CB    . ILE A 1 280 ? 140.373 133.841 118.424 1.00 17.83 ?  280 ILE A CB    1 
ATOM   2248  C  CG1   . ILE A 1 280 ? 140.609 132.487 117.757 1.00 23.84 ?  280 ILE A CG1   1 
ATOM   2249  C  CG2   . ILE A 1 280 ? 139.543 133.684 119.685 1.00 20.13 ?  280 ILE A CG2   1 
ATOM   2250  C  CD1   . ILE A 1 280 ? 141.767 131.720 118.361 1.00 18.96 ?  280 ILE A CD1   1 
ATOM   2251  N  N     . GLY A 1 281 ? 141.371 136.107 116.274 1.00 13.73 ?  281 GLY A N     1 
ATOM   2252  C  CA    . GLY A 1 281 ? 142.363 136.352 115.250 1.00 4.47  ?  281 GLY A CA    1 
ATOM   2253  C  C     . GLY A 1 281 ? 143.704 136.649 115.886 1.00 10.46 ?  281 GLY A C     1 
ATOM   2254  O  O     . GLY A 1 281 ? 143.786 137.204 116.980 1.00 18.34 ?  281 GLY A O     1 
ATOM   2255  N  N     . VAL A 1 282 ? 144.762 136.261 115.184 1.00 15.23 ?  282 VAL A N     1 
ATOM   2256  C  CA    . VAL A 1 282 ? 146.129 136.433 115.659 1.00 12.71 ?  282 VAL A CA    1 
ATOM   2257  C  C     . VAL A 1 282 ? 146.851 137.383 114.718 1.00 13.55 ?  282 VAL A C     1 
ATOM   2258  O  O     . VAL A 1 282 ? 146.807 137.211 113.494 1.00 17.64 ?  282 VAL A O     1 
ATOM   2259  C  CB    . VAL A 1 282 ? 146.865 135.086 115.764 1.00 14.51 ?  282 VAL A CB    1 
ATOM   2260  C  CG1   . VAL A 1 282 ? 148.351 135.305 115.967 1.00 19.00 ?  282 VAL A CG1   1 
ATOM   2261  C  CG2   . VAL A 1 282 ? 146.297 134.275 116.909 1.00 19.47 ?  282 VAL A CG2   1 
ATOM   2262  N  N     . VAL A 1 283 ? 147.501 138.390 115.290 1.00 12.13 ?  283 VAL A N     1 
ATOM   2263  C  CA    . VAL A 1 283 ? 148.301 139.342 114.530 1.00 11.66 ?  283 VAL A CA    1 
ATOM   2264  C  C     . VAL A 1 283 ? 149.750 138.878 114.571 1.00 16.58 ?  283 VAL A C     1 
ATOM   2265  O  O     . VAL A 1 283 ? 150.336 138.742 115.650 1.00 25.42 ?  283 VAL A O     1 
ATOM   2266  C  CB    . VAL A 1 283 ? 148.156 140.761 115.096 1.00 11.36 ?  283 VAL A CB    1 
ATOM   2267  C  CG1   . VAL A 1 283 ? 148.804 141.767 114.170 1.00 9.15  ?  283 VAL A CG1   1 
ATOM   2268  C  CG2   . VAL A 1 283 ? 146.687 141.087 115.307 1.00 14.54 ?  283 VAL A CG2   1 
ATOM   2269  N  N     . ILE A 1 284 ? 150.327 138.637 113.402 1.00 14.52 ?  284 ILE A N     1 
ATOM   2270  C  CA    . ILE A 1 284 ? 151.659 138.064 113.277 1.00 14.52 ?  284 ILE A CA    1 
ATOM   2271  C  C     . ILE A 1 284 ? 152.570 139.094 112.623 1.00 18.20 ?  284 ILE A C     1 
ATOM   2272  O  O     . ILE A 1 284 ? 152.521 139.300 111.410 1.00 20.15 ?  284 ILE A O     1 
ATOM   2273  C  CB    . ILE A 1 284 ? 151.635 136.753 112.470 1.00 16.43 ?  284 ILE A CB    1 
ATOM   2274  C  CG1   . ILE A 1 284 ? 150.697 135.741 113.131 1.00 16.93 ?  284 ILE A CG1   1 
ATOM   2275  C  CG2   . ILE A 1 284 ? 153.036 136.179 112.344 1.00 17.23 ?  284 ILE A CG2   1 
ATOM   2276  C  CD1   . ILE A 1 284 ? 150.729 134.372 112.494 1.00 19.37 ?  284 ILE A CD1   1 
ATOM   2277  N  N     . PRO A 1 285 ? 153.414 139.767 113.399 1.00 27.08 ?  285 PRO A N     1 
ATOM   2278  C  CA    . PRO A 1 285 ? 154.407 140.666 112.804 1.00 25.81 ?  285 PRO A CA    1 
ATOM   2279  C  C     . PRO A 1 285 ? 155.471 139.886 112.045 1.00 23.52 ?  285 PRO A C     1 
ATOM   2280  O  O     . PRO A 1 285 ? 155.623 138.672 112.196 1.00 25.24 ?  285 PRO A O     1 
ATOM   2281  C  CB    . PRO A 1 285 ? 155.008 141.392 114.014 1.00 19.49 ?  285 PRO A CB    1 
ATOM   2282  C  CG    . PRO A 1 285 ? 154.035 141.169 115.130 1.00 17.59 ?  285 PRO A CG    1 
ATOM   2283  C  CD    . PRO A 1 285 ? 153.423 139.834 114.868 1.00 21.54 ?  285 PRO A CD    1 
ATOM   2284  N  N     . ASP A 1 286 ? 156.212 140.614 111.205 1.00 26.51 ?  286 ASP A N     1 
ATOM   2285  C  CA    . ASP A 1 286 ? 157.280 139.985 110.433 1.00 24.40 ?  286 ASP A CA    1 
ATOM   2286  C  C     . ASP A 1 286 ? 158.355 139.397 111.335 1.00 29.80 ?  286 ASP A C     1 
ATOM   2287  O  O     . ASP A 1 286 ? 159.050 138.457 110.935 1.00 32.08 ?  286 ASP A O     1 
ATOM   2288  C  CB    . ASP A 1 286 ? 157.902 140.993 109.469 1.00 24.91 ?  286 ASP A CB    1 
ATOM   2289  C  CG    . ASP A 1 286 ? 157.333 140.888 108.071 1.00 36.92 ?  286 ASP A CG    1 
ATOM   2290  O  OD1   . ASP A 1 286 ? 156.277 140.245 107.906 1.00 36.04 ?  286 ASP A OD1   1 
ATOM   2291  O  OD2   . ASP A 1 286 ? 157.939 141.453 107.136 1.00 39.10 -1 286 ASP A OD2   1 
ATOM   2292  N  N     . LYS A 1 287 ? 158.514 139.937 112.546 1.00 30.46 ?  287 LYS A N     1 
ATOM   2293  C  CA    . LYS A 1 287 ? 159.532 139.425 113.457 1.00 28.00 ?  287 LYS A CA    1 
ATOM   2294  C  C     . LYS A 1 287 ? 159.258 137.977 113.838 1.00 29.31 ?  287 LYS A C     1 
ATOM   2295  O  O     . LYS A 1 287 ? 160.185 137.164 113.922 1.00 36.10 ?  287 LYS A O     1 
ATOM   2296  C  CB    . LYS A 1 287 ? 159.610 140.303 114.706 1.00 31.50 ?  287 LYS A CB    1 
ATOM   2297  C  CG    . LYS A 1 287 ? 160.816 140.014 115.579 1.00 27.46 ?  287 LYS A CG    1 
ATOM   2298  C  CD    . LYS A 1 287 ? 162.088 139.984 114.749 1.00 30.56 ?  287 LYS A CD    1 
ATOM   2299  C  CE    . LYS A 1 287 ? 163.322 139.898 115.625 1.00 31.46 ?  287 LYS A CE    1 
ATOM   2300  N  NZ    . LYS A 1 287 ? 164.573 139.981 114.824 1.00 34.93 1  287 LYS A NZ    1 
ATOM   2301  N  N     . PHE A 1 288 ? 157.990 137.634 114.078 1.00 24.06 ?  288 PHE A N     1 
ATOM   2302  C  CA    . PHE A 1 288 ? 157.650 136.251 114.400 1.00 24.02 ?  288 PHE A CA    1 
ATOM   2303  C  C     . PHE A 1 288 ? 157.970 135.321 113.237 1.00 24.75 ?  288 PHE A C     1 
ATOM   2304  O  O     . PHE A 1 288 ? 158.475 134.210 113.440 1.00 36.24 ?  288 PHE A O     1 
ATOM   2305  C  CB    . PHE A 1 288 ? 156.173 136.147 114.779 1.00 25.06 ?  288 PHE A CB    1 
ATOM   2306  C  CG    . PHE A 1 288 ? 155.754 134.768 115.200 1.00 26.56 ?  288 PHE A CG    1 
ATOM   2307  C  CD1   . PHE A 1 288 ? 155.957 134.336 116.500 1.00 27.58 ?  288 PHE A CD1   1 
ATOM   2308  C  CD2   . PHE A 1 288 ? 155.157 133.904 114.298 1.00 22.72 ?  288 PHE A CD2   1 
ATOM   2309  C  CE1   . PHE A 1 288 ? 155.573 133.069 116.890 1.00 26.22 ?  288 PHE A CE1   1 
ATOM   2310  C  CE2   . PHE A 1 288 ? 154.772 132.636 114.683 1.00 24.98 ?  288 PHE A CE2   1 
ATOM   2311  C  CZ    . PHE A 1 288 ? 154.979 132.218 115.981 1.00 29.33 ?  288 PHE A CZ    1 
ATOM   2312  N  N     . VAL A 1 289 ? 157.682 135.757 112.010 1.00 24.93 ?  289 VAL A N     1 
ATOM   2313  C  CA    . VAL A 1 289 ? 157.965 134.927 110.846 1.00 28.22 ?  289 VAL A CA    1 
ATOM   2314  C  C     . VAL A 1 289 ? 159.468 134.763 110.660 1.00 29.88 ?  289 VAL A C     1 
ATOM   2315  O  O     . VAL A 1 289 ? 159.944 133.688 110.281 1.00 33.12 ?  289 VAL A O     1 
ATOM   2316  C  CB    . VAL A 1 289 ? 157.296 135.518 109.592 1.00 31.83 ?  289 VAL A CB    1 
ATOM   2317  C  CG1   . VAL A 1 289 ? 157.356 134.527 108.442 1.00 25.97 ?  289 VAL A CG1   1 
ATOM   2318  C  CG2   . VAL A 1 289 ? 155.858 135.908 109.893 1.00 26.24 ?  289 VAL A CG2   1 
ATOM   2319  N  N     . GLU A 1 290 ? 160.240 135.822 110.920 1.00 33.29 ?  290 GLU A N     1 
ATOM   2320  C  CA    . GLU A 1 290 ? 161.694 135.713 110.843 1.00 32.38 ?  290 GLU A CA    1 
ATOM   2321  C  C     . GLU A 1 290 ? 162.233 134.758 111.900 1.00 35.00 ?  290 GLU A C     1 
ATOM   2322  O  O     . GLU A 1 290 ? 163.138 133.963 111.625 1.00 41.47 ?  290 GLU A O     1 
ATOM   2323  C  CB    . GLU A 1 290 ? 162.339 137.091 110.989 1.00 33.41 ?  290 GLU A CB    1 
ATOM   2324  C  CG    . GLU A 1 290 ? 162.323 137.932 109.723 1.00 38.34 ?  290 GLU A CG    1 
ATOM   2325  C  CD    . GLU A 1 290 ? 161.741 139.313 109.943 1.00 39.81 ?  290 GLU A CD    1 
ATOM   2326  O  OE1   . GLU A 1 290 ? 160.984 139.787 109.070 1.00 38.86 ?  290 GLU A OE1   1 
ATOM   2327  O  OE2   . GLU A 1 290 ? 162.039 139.927 110.990 1.00 40.07 -1 290 GLU A OE2   1 
ATOM   2328  N  N     . LEU A 1 291 ? 161.695 134.830 113.119 1.00 32.62 ?  291 LEU A N     1 
ATOM   2329  C  CA    . LEU A 1 291 ? 162.143 133.936 114.182 1.00 29.33 ?  291 LEU A CA    1 
ATOM   2330  C  C     . LEU A 1 291 ? 161.811 132.484 113.862 1.00 32.32 ?  291 LEU A C     1 
ATOM   2331  O  O     . LEU A 1 291 ? 162.635 131.590 114.090 1.00 39.75 ?  291 LEU A O     1 
ATOM   2332  C  CB    . LEU A 1 291 ? 161.518 134.349 115.514 1.00 31.03 ?  291 LEU A CB    1 
ATOM   2333  C  CG    . LEU A 1 291 ? 162.009 135.673 116.098 1.00 32.77 ?  291 LEU A CG    1 
ATOM   2334  C  CD1   . LEU A 1 291 ? 161.012 136.218 117.106 1.00 27.11 ?  291 LEU A CD1   1 
ATOM   2335  C  CD2   . LEU A 1 291 ? 163.379 135.505 116.728 1.00 32.96 ?  291 LEU A CD2   1 
ATOM   2336  N  N     . ALA A 1 292 ? 160.610 132.229 113.339 1.00 33.22 ?  292 ALA A N     1 
ATOM   2337  C  CA    . ALA A 1 292 ? 160.246 130.869 112.957 1.00 31.63 ?  292 ALA A CA    1 
ATOM   2338  C  C     . ALA A 1 292 ? 161.094 130.375 111.791 1.00 32.39 ?  292 ALA A C     1 
ATOM   2339  O  O     . ALA A 1 292 ? 161.487 129.204 111.754 1.00 37.80 ?  292 ALA A O     1 
ATOM   2340  C  CB    . ALA A 1 292 ? 158.760 130.802 112.609 1.00 30.62 ?  292 ALA A CB    1 
ATOM   2341  N  N     . ARG A 1 293 ? 161.381 131.256 110.830 1.00 34.05 ?  293 ARG A N     1 
ATOM   2342  C  CA    . ARG A 1 293 ? 162.169 130.870 109.664 1.00 33.45 ?  293 ARG A CA    1 
ATOM   2343  C  C     . ARG A 1 293 ? 163.581 130.457 110.056 1.00 39.26 ?  293 ARG A C     1 
ATOM   2344  O  O     . ARG A 1 293 ? 164.109 129.463 109.543 1.00 43.88 ?  293 ARG A O     1 
ATOM   2345  C  CB    . ARG A 1 293 ? 162.202 132.027 108.666 1.00 34.13 ?  293 ARG A CB    1 
ATOM   2346  C  CG    . ARG A 1 293 ? 163.052 131.784 107.435 1.00 34.36 ?  293 ARG A CG    1 
ATOM   2347  C  CD    . ARG A 1 293 ? 163.226 133.070 106.647 1.00 38.71 ?  293 ARG A CD    1 
ATOM   2348  N  NE    . ARG A 1 293 ? 161.972 133.806 106.543 1.00 40.23 ?  293 ARG A NE    1 
ATOM   2349  C  CZ    . ARG A 1 293 ? 161.840 135.100 106.798 1.00 39.33 ?  293 ARG A CZ    1 
ATOM   2350  N  NH1   . ARG A 1 293 ? 162.873 135.843 107.159 1.00 37.97 1  293 ARG A NH1   1 
ATOM   2351  N  NH2   . ARG A 1 293 ? 160.640 135.664 106.687 1.00 35.71 ?  293 ARG A NH2   1 
ATOM   2352  N  N     . GLU A 1 294 ? 164.206 131.203 110.961 1.00 41.45 ?  294 GLU A N     1 
ATOM   2353  C  CA    . GLU A 1 294 ? 165.555 130.892 111.417 1.00 39.06 ?  294 GLU A CA    1 
ATOM   2354  C  C     . GLU A 1 294 ? 165.577 129.880 112.553 1.00 40.16 ?  294 GLU A C     1 
ATOM   2355  O  O     . GLU A 1 294 ? 166.663 129.537 113.031 1.00 42.64 ?  294 GLU A O     1 
ATOM   2356  C  CB    . GLU A 1 294 ? 166.266 132.174 111.857 1.00 39.21 ?  294 GLU A CB    1 
ATOM   2357  C  CG    . GLU A 1 294 ? 166.719 133.058 110.707 1.00 41.33 ?  294 GLU A CG    1 
ATOM   2358  C  CD    . GLU A 1 294 ? 166.190 134.473 110.820 1.00 44.89 ?  294 GLU A CD    1 
ATOM   2359  O  OE1   . GLU A 1 294 ? 166.024 134.958 111.959 1.00 45.92 ?  294 GLU A OE1   1 
ATOM   2360  O  OE2   . GLU A 1 294 ? 165.938 135.101 109.771 1.00 46.51 -1 294 GLU A OE2   1 
ATOM   2361  N  N     . ASP A 1 295 ? 164.411 129.414 112.999 1.00 38.72 ?  295 ASP A N     1 
ATOM   2362  C  CA    . ASP A 1 295 ? 164.250 128.442 114.077 1.00 37.97 ?  295 ASP A CA    1 
ATOM   2363  C  C     . ASP A 1 295 ? 164.756 128.954 115.420 1.00 44.50 ?  295 ASP A C     1 
ATOM   2364  O  O     . ASP A 1 295 ? 164.862 128.174 116.373 1.00 44.19 ?  295 ASP A O     1 
ATOM   2365  C  CB    . ASP A 1 295 ? 164.928 127.106 113.743 1.00 40.78 ?  295 ASP A CB    1 
ATOM   2366  C  CG    . ASP A 1 295 ? 164.080 125.910 114.129 1.00 44.89 ?  295 ASP A CG    1 
ATOM   2367  O  OD1   . ASP A 1 295 ? 163.115 126.088 114.901 1.00 46.03 ?  295 ASP A OD1   1 
ATOM   2368  O  OD2   . ASP A 1 295 ? 164.382 124.791 113.663 1.00 42.65 -1 295 ASP A OD2   1 
ATOM   2369  N  N     . LYS A 1 296 ? 165.074 130.242 115.525 1.00 43.47 ?  296 LYS A N     1 
ATOM   2370  C  CA    . LYS A 1 296 ? 165.443 130.814 116.811 1.00 41.60 ?  296 LYS A CA    1 
ATOM   2371  C  C     . LYS A 1 296 ? 164.237 130.832 117.738 1.00 41.53 ?  296 LYS A C     1 
ATOM   2372  O  O     . LYS A 1 296 ? 163.117 131.134 117.318 1.00 45.89 ?  296 LYS A O     1 
ATOM   2373  C  CB    . LYS A 1 296 ? 165.987 132.232 116.638 1.00 42.27 ?  296 LYS A CB    1 
ATOM   2374  C  CG    . LYS A 1 296 ? 167.078 132.371 115.595 1.00 44.14 ?  296 LYS A CG    1 
ATOM   2375  C  CD    . LYS A 1 296 ? 167.056 133.756 114.972 1.00 42.91 ?  296 LYS A CD    1 
ATOM   2376  C  CE    . LYS A 1 296 ? 168.457 134.327 114.845 1.00 43.56 ?  296 LYS A CE    1 
ATOM   2377  N  NZ    . LYS A 1 296 ? 169.310 133.512 113.938 1.00 44.16 1  296 LYS A NZ    1 
ATOM   2378  N  N     . ALA A 1 297 ? 164.467 130.501 119.004 1.00 40.88 ?  297 ALA A N     1 
ATOM   2379  C  CA    . ALA A 1 297 ? 163.393 130.540 119.984 1.00 42.43 ?  297 ALA A CA    1 
ATOM   2380  C  C     . ALA A 1 297 ? 162.933 131.975 120.206 1.00 40.42 ?  297 ALA A C     1 
ATOM   2381  O  O     . ALA A 1 297 ? 163.747 132.891 120.349 1.00 41.09 ?  297 ALA A O     1 
ATOM   2382  C  CB    . ALA A 1 297 ? 163.852 129.922 121.302 1.00 37.53 ?  297 ALA A CB    1 
ATOM   2383  N  N     . ALA A 1 298 ? 161.618 132.166 120.234 1.00 35.05 ?  298 ALA A N     1 
ATOM   2384  C  CA    . ALA A 1 298 ? 161.033 133.488 120.359 1.00 34.96 ?  298 ALA A CA    1 
ATOM   2385  C  C     . ALA A 1 298 ? 160.642 133.752 121.809 1.00 35.60 ?  298 ALA A C     1 
ATOM   2386  O  O     . ALA A 1 298 ? 160.697 132.872 122.671 1.00 39.04 ?  298 ALA A O     1 
ATOM   2387  C  CB    . ALA A 1 298 ? 159.827 133.629 119.429 1.00 33.74 ?  298 ALA A CB    1 
ATOM   2388  N  N     . TYR A 1 299 ? 160.230 134.987 122.076 1.00 33.59 ?  299 TYR A N     1 
ATOM   2389  C  CA    . TYR A 1 299 ? 159.789 135.391 123.403 1.00 27.91 ?  299 TYR A CA    1 
ATOM   2390  C  C     . TYR A 1 299 ? 158.422 136.045 123.293 1.00 29.08 ?  299 TYR A C     1 
ATOM   2391  O  O     . TYR A 1 299 ? 158.219 136.928 122.454 1.00 30.35 ?  299 TYR A O     1 
ATOM   2392  C  CB    . TYR A 1 299 ? 160.787 136.356 124.049 1.00 29.77 ?  299 TYR A CB    1 
ATOM   2393  C  CG    . TYR A 1 299 ? 162.048 135.687 124.542 1.00 31.98 ?  299 TYR A CG    1 
ATOM   2394  C  CD1   . TYR A 1 299 ? 162.078 135.033 125.766 1.00 34.99 ?  299 TYR A CD1   1 
ATOM   2395  C  CD2   . TYR A 1 299 ? 163.207 135.703 123.779 1.00 32.52 ?  299 TYR A CD2   1 
ATOM   2396  C  CE1   . TYR A 1 299 ? 163.229 134.418 126.218 1.00 35.03 ?  299 TYR A CE1   1 
ATOM   2397  C  CE2   . TYR A 1 299 ? 164.361 135.092 124.221 1.00 33.28 ?  299 TYR A CE2   1 
ATOM   2398  C  CZ    . TYR A 1 299 ? 164.367 134.451 125.441 1.00 35.74 ?  299 TYR A CZ    1 
ATOM   2399  O  OH    . TYR A 1 299 ? 165.516 133.839 125.887 1.00 39.40 ?  299 TYR A OH    1 
ATOM   2400  N  N     . VAL A 1 300 ? 157.491 135.606 124.132 1.00 32.74 ?  300 VAL A N     1 
ATOM   2401  C  CA    . VAL A 1 300 ? 156.195 136.258 124.277 1.00 27.48 ?  300 VAL A CA    1 
ATOM   2402  C  C     . VAL A 1 300 ? 156.264 137.150 125.507 1.00 28.99 ?  300 VAL A C     1 
ATOM   2403  O  O     . VAL A 1 300 ? 156.672 136.704 126.585 1.00 35.40 ?  300 VAL A O     1 
ATOM   2404  C  CB    . VAL A 1 300 ? 155.054 135.232 124.386 1.00 25.59 ?  300 VAL A CB    1 
ATOM   2405  C  CG1   . VAL A 1 300 ? 154.696 134.694 123.009 1.00 26.29 ?  300 VAL A CG1   1 
ATOM   2406  C  CG2   . VAL A 1 300 ? 155.431 134.100 125.326 1.00 28.34 ?  300 VAL A CG2   1 
ATOM   2407  N  N     . PHE A 1 301 ? 155.883 138.410 125.347 1.00 22.22 ?  301 PHE A N     1 
ATOM   2408  C  CA    . PHE A 1 301 ? 156.143 139.423 126.356 1.00 24.64 ?  301 PHE A CA    1 
ATOM   2409  C  C     . PHE A 1 301 ? 154.902 139.749 127.174 1.00 29.79 ?  301 PHE A C     1 
ATOM   2410  O  O     . PHE A 1 301 ? 153.768 139.629 126.703 1.00 32.59 ?  301 PHE A O     1 
ATOM   2411  C  CB    . PHE A 1 301 ? 156.684 140.698 125.707 1.00 23.17 ?  301 PHE A CB    1 
ATOM   2412  C  CG    . PHE A 1 301 ? 157.868 140.461 124.819 1.00 28.71 ?  301 PHE A CG    1 
ATOM   2413  C  CD1   . PHE A 1 301 ? 159.129 140.309 125.366 1.00 27.45 ?  301 PHE A CD1   1 
ATOM   2414  C  CD2   . PHE A 1 301 ? 157.721 140.375 123.446 1.00 27.89 ?  301 PHE A CD2   1 
ATOM   2415  C  CE1   . PHE A 1 301 ? 160.224 140.083 124.563 1.00 27.89 ?  301 PHE A CE1   1 
ATOM   2416  C  CE2   . PHE A 1 301 ? 158.816 140.150 122.637 1.00 26.73 ?  301 PHE A CE2   1 
ATOM   2417  C  CZ    . PHE A 1 301 ? 160.070 140.004 123.198 1.00 29.84 ?  301 PHE A CZ    1 
ATOM   2418  N  N     . TYR A 1 302 ? 155.138 140.156 128.418 1.00 27.90 ?  302 TYR A N     1 
ATOM   2419  C  CA    . TYR A 1 302 ? 154.090 140.681 129.280 1.00 24.69 ?  302 TYR A CA    1 
ATOM   2420  C  C     . TYR A 1 302 ? 153.860 142.142 128.924 1.00 28.70 ?  302 TYR A C     1 
ATOM   2421  O  O     . TYR A 1 302 ? 154.761 142.974 129.089 1.00 30.11 ?  302 TYR A O     1 
ATOM   2422  C  CB    . TYR A 1 302 ? 154.468 140.531 130.753 1.00 25.69 ?  302 TYR A CB    1 
ATOM   2423  C  CG    . TYR A 1 302 ? 154.419 139.109 131.263 1.00 28.28 ?  302 TYR A CG    1 
ATOM   2424  C  CD1   . TYR A 1 302 ? 155.377 138.180 130.885 1.00 27.90 ?  302 TYR A CD1   1 
ATOM   2425  C  CD2   . TYR A 1 302 ? 153.413 138.698 132.123 1.00 29.97 ?  302 TYR A CD2   1 
ATOM   2426  C  CE1   . TYR A 1 302 ? 155.333 136.883 131.352 1.00 26.48 ?  302 TYR A CE1   1 
ATOM   2427  C  CE2   . TYR A 1 302 ? 153.360 137.404 132.596 1.00 30.24 ?  302 TYR A CE2   1 
ATOM   2428  C  CZ    . TYR A 1 302 ? 154.325 136.501 132.213 1.00 33.79 ?  302 TYR A CZ    1 
ATOM   2429  O  OH    . TYR A 1 302 ? 154.273 135.209 132.679 1.00 34.01 ?  302 TYR A OH    1 
ATOM   2430  N  N     . PRO A 1 303 ? 152.677 142.485 128.415 1.00 24.50 ?  303 PRO A N     1 
ATOM   2431  C  CA    . PRO A 1 303 ? 152.459 143.853 127.914 1.00 21.46 ?  303 PRO A CA    1 
ATOM   2432  C  C     . PRO A 1 303 ? 152.604 144.933 128.968 1.00 28.11 ?  303 PRO A C     1 
ATOM   2433  O  O     . PRO A 1 303 ? 153.084 146.029 128.652 1.00 32.36 ?  303 PRO A O     1 
ATOM   2434  C  CB    . PRO A 1 303 ? 151.026 143.794 127.368 1.00 24.61 ?  303 PRO A CB    1 
ATOM   2435  C  CG    . PRO A 1 303 ? 150.779 142.352 127.111 1.00 26.14 ?  303 PRO A CG    1 
ATOM   2436  C  CD    . PRO A 1 303 ? 151.513 141.619 128.179 1.00 25.81 ?  303 PRO A CD    1 
ATOM   2437  N  N     . HIS A 1 304 ? 152.203 144.666 130.213 1.00 29.80 ?  304 HIS A N     1 
ATOM   2438  C  CA    . HIS A 1 304 ? 152.236 145.712 131.227 1.00 24.97 ?  304 HIS A CA    1 
ATOM   2439  C  C     . HIS A 1 304 ? 153.662 146.068 131.620 1.00 28.58 ?  304 HIS A C     1 
ATOM   2440  O  O     . HIS A 1 304 ? 153.946 147.234 131.907 1.00 36.19 ?  304 HIS A O     1 
ATOM   2441  C  CB    . HIS A 1 304 ? 151.436 145.292 132.457 1.00 28.66 ?  304 HIS A CB    1 
ATOM   2442  C  CG    . HIS A 1 304 ? 151.236 146.394 133.449 1.00 30.65 ?  304 HIS A CG    1 
ATOM   2443  N  ND1   . HIS A 1 304 ? 151.417 146.219 134.804 1.00 33.01 ?  304 HIS A ND1   1 
ATOM   2444  C  CD2   . HIS A 1 304 ? 150.875 147.688 133.282 1.00 29.10 ?  304 HIS A CD2   1 
ATOM   2445  C  CE1   . HIS A 1 304 ? 151.171 147.357 135.430 1.00 32.39 ?  304 HIS A CE1   1 
ATOM   2446  N  NE2   . HIS A 1 304 ? 150.840 148.265 134.528 1.00 30.65 ?  304 HIS A NE2   1 
ATOM   2447  N  N     . THR A 1 305 ? 154.566 145.086 131.646 1.00 29.10 ?  305 THR A N     1 
ATOM   2448  C  CA    . THR A 1 305 ? 155.966 145.387 131.927 1.00 32.57 ?  305 THR A CA    1 
ATOM   2449  C  C     . THR A 1 305 ? 156.570 146.259 130.832 1.00 27.80 ?  305 THR A C     1 
ATOM   2450  O  O     . THR A 1 305 ? 157.321 147.199 131.117 1.00 33.42 ?  305 THR A O     1 
ATOM   2451  C  CB    . THR A 1 305 ? 156.765 144.094 132.092 1.00 31.42 ?  305 THR A CB    1 
ATOM   2452  O  OG1   . THR A 1 305 ? 156.967 143.480 130.813 1.00 31.84 ?  305 THR A OG1   1 
ATOM   2453  C  CG2   . THR A 1 305 ? 156.024 143.128 132.999 1.00 29.19 ?  305 THR A CG2   1 
ATOM   2454  N  N     . ILE A 1 306 ? 156.241 145.968 129.572 1.00 32.77 ?  306 ILE A N     1 
ATOM   2455  C  CA    . ILE A 1 306 ? 156.706 146.803 128.468 1.00 32.57 ?  306 ILE A CA    1 
ATOM   2456  C  C     . ILE A 1 306 ? 156.133 148.209 128.590 1.00 31.32 ?  306 ILE A C     1 
ATOM   2457  O  O     . ILE A 1 306 ? 156.835 149.204 128.368 1.00 32.80 ?  306 ILE A O     1 
ATOM   2458  C  CB    . ILE A 1 306 ? 156.341 146.151 127.122 1.00 28.41 ?  306 ILE A CB    1 
ATOM   2459  C  CG1   . ILE A 1 306 ? 157.321 145.022 126.799 1.00 32.43 ?  306 ILE A CG1   1 
ATOM   2460  C  CG2   . ILE A 1 306 ? 156.314 147.185 126.008 1.00 31.73 ?  306 ILE A CG2   1 
ATOM   2461  C  CD1   . ILE A 1 306 ? 157.021 144.304 125.514 1.00 31.27 ?  306 ILE A CD1   1 
ATOM   2462  N  N     . TYR A 1 307 ? 154.850 148.317 128.942 1.00 31.91 ?  307 TYR A N     1 
ATOM   2463  C  CA    . TYR A 1 307 ? 154.234 149.630 129.099 1.00 31.01 ?  307 TYR A CA    1 
ATOM   2464  C  C     . TYR A 1 307 ? 154.887 150.416 130.229 1.00 33.45 ?  307 TYR A C     1 
ATOM   2465  O  O     . TYR A 1 307 ? 155.106 151.626 130.108 1.00 36.52 ?  307 TYR A O     1 
ATOM   2466  C  CB    . TYR A 1 307 ? 152.732 149.481 129.346 1.00 28.97 ?  307 TYR A CB    1 
ATOM   2467  C  CG    . TYR A 1 307 ? 152.000 150.799 129.421 1.00 30.60 ?  307 TYR A CG    1 
ATOM   2468  C  CD1   . TYR A 1 307 ? 151.655 151.486 128.266 1.00 30.65 ?  307 TYR A CD1   1 
ATOM   2469  C  CD2   . TYR A 1 307 ? 151.660 151.358 130.644 1.00 33.18 ?  307 TYR A CD2   1 
ATOM   2470  C  CE1   . TYR A 1 307 ? 150.991 152.689 128.327 1.00 33.00 ?  307 TYR A CE1   1 
ATOM   2471  C  CE2   . TYR A 1 307 ? 150.996 152.562 130.715 1.00 33.13 ?  307 TYR A CE2   1 
ATOM   2472  C  CZ    . TYR A 1 307 ? 150.664 153.222 129.552 1.00 34.63 ?  307 TYR A CZ    1 
ATOM   2473  O  OH    . TYR A 1 307 ? 150.001 154.423 129.608 1.00 36.39 ?  307 TYR A OH    1 
ATOM   2474  N  N     . LYS A 1 308 ? 155.192 149.747 131.341 1.00 34.52 ?  308 LYS A N     1 
ATOM   2475  C  CA    . LYS A 1 308 ? 155.851 150.416 132.457 1.00 32.72 ?  308 LYS A CA    1 
ATOM   2476  C  C     . LYS A 1 308 ? 157.259 150.860 132.081 1.00 32.52 ?  308 LYS A C     1 
ATOM   2477  O  O     . LYS A 1 308 ? 157.700 151.944 132.480 1.00 38.35 ?  308 LYS A O     1 
ATOM   2478  C  CB    . LYS A 1 308 ? 155.887 149.492 133.673 1.00 33.87 ?  308 LYS A CB    1 
ATOM   2479  C  CG    . LYS A 1 308 ? 154.543 149.320 134.360 1.00 33.26 ?  308 LYS A CG    1 
ATOM   2480  C  CD    . LYS A 1 308 ? 154.680 148.538 135.656 1.00 36.34 ?  308 LYS A CD    1 
ATOM   2481  C  CE    . LYS A 1 308 ? 155.316 147.180 135.416 1.00 37.36 ?  308 LYS A CE    1 
ATOM   2482  N  NZ    . LYS A 1 308 ? 154.346 146.068 135.611 1.00 37.78 1  308 LYS A NZ    1 
ATOM   2483  N  N     . GLU A 1 309 ? 157.980 150.036 131.318 1.00 32.39 ?  309 GLU A N     1 
ATOM   2484  C  CA    . GLU A 1 309 ? 159.361 150.363 130.982 1.00 33.46 ?  309 GLU A CA    1 
ATOM   2485  C  C     . GLU A 1 309 ? 159.445 151.473 129.941 1.00 36.40 ?  309 GLU A C     1 
ATOM   2486  O  O     . GLU A 1 309 ? 160.284 152.375 130.056 1.00 37.54 ?  309 GLU A O     1 
ATOM   2487  C  CB    . GLU A 1 309 ? 160.089 149.113 130.491 1.00 31.64 ?  309 GLU A CB    1 
ATOM   2488  C  CG    . GLU A 1 309 ? 161.491 149.377 129.973 1.00 37.48 ?  309 GLU A CG    1 
ATOM   2489  C  CD    . GLU A 1 309 ? 162.451 149.804 131.064 1.00 42.65 ?  309 GLU A CD    1 
ATOM   2490  O  OE1   . GLU A 1 309 ? 162.143 149.584 132.253 1.00 41.25 ?  309 GLU A OE1   1 
ATOM   2491  O  OE2   . GLU A 1 309 ? 163.517 150.363 130.731 1.00 41.78 -1 309 GLU A OE2   1 
ATOM   2492  N  N     . TYR A 1 310 ? 158.586 151.433 128.922 1.00 37.05 ?  310 TYR A N     1 
ATOM   2493  C  CA    . TYR A 1 310 ? 158.707 152.326 127.780 1.00 36.10 ?  310 TYR A CA    1 
ATOM   2494  C  C     . TYR A 1 310 ? 157.607 153.375 127.691 1.00 33.12 ?  310 TYR A C     1 
ATOM   2495  O  O     . TYR A 1 310 ? 157.737 154.312 126.896 1.00 38.26 ?  310 TYR A O     1 
ATOM   2496  C  CB    . TYR A 1 310 ? 158.732 151.512 126.477 1.00 37.36 ?  310 TYR A CB    1 
ATOM   2497  C  CG    . TYR A 1 310 ? 159.862 150.510 126.411 1.00 33.85 ?  310 TYR A CG    1 
ATOM   2498  C  CD1   . TYR A 1 310 ? 161.120 150.884 125.960 1.00 34.94 ?  310 TYR A CD1   1 
ATOM   2499  C  CD2   . TYR A 1 310 ? 159.674 149.193 126.805 1.00 32.11 ?  310 TYR A CD2   1 
ATOM   2500  C  CE1   . TYR A 1 310 ? 162.158 149.975 125.901 1.00 36.55 ?  310 TYR A CE1   1 
ATOM   2501  C  CE2   . TYR A 1 310 ? 160.705 148.277 126.752 1.00 33.23 ?  310 TYR A CE2   1 
ATOM   2502  C  CZ    . TYR A 1 310 ? 161.944 148.674 126.297 1.00 37.01 ?  310 TYR A CZ    1 
ATOM   2503  O  OH    . TYR A 1 310 ? 162.974 147.764 126.241 1.00 41.12 ?  310 TYR A OH    1 
ATOM   2504  N  N     . GLY A 1 311 ? 156.539 153.254 128.475 1.00 27.93 ?  311 GLY A N     1 
ATOM   2505  C  CA    . GLY A 1 311 ? 155.453 154.208 128.412 1.00 31.03 ?  311 GLY A CA    1 
ATOM   2506  C  C     . GLY A 1 311 ? 154.502 154.019 127.253 1.00 36.06 ?  311 GLY A C     1 
ATOM   2507  O  O     . GLY A 1 311 ? 153.580 154.829 127.094 1.00 39.00 ?  311 GLY A O     1 
ATOM   2508  N  N     . GLN A 1 312 ? 154.697 152.985 126.439 1.00 35.59 ?  312 GLN A N     1 
ATOM   2509  C  CA    . GLN A 1 312 ? 153.829 152.687 125.313 1.00 32.40 ?  312 GLN A CA    1 
ATOM   2510  C  C     . GLN A 1 312 ? 153.468 151.209 125.340 1.00 34.00 ?  312 GLN A C     1 
ATOM   2511  O  O     . GLN A 1 312 ? 154.202 150.380 125.882 1.00 38.82 ?  312 GLN A O     1 
ATOM   2512  C  CB    . GLN A 1 312 ? 154.488 153.036 123.970 1.00 31.89 ?  312 GLN A CB    1 
ATOM   2513  C  CG    . GLN A 1 312 ? 155.596 154.072 124.059 1.00 34.46 ?  312 GLN A CG    1 
ATOM   2514  C  CD    . GLN A 1 312 ? 156.338 154.243 122.750 1.00 39.73 ?  312 GLN A CD    1 
ATOM   2515  O  OE1   . GLN A 1 312 ? 155.729 154.380 121.691 1.00 38.64 ?  312 GLN A OE1   1 
ATOM   2516  N  NE2   . GLN A 1 312 ? 157.665 154.234 122.817 1.00 38.75 ?  312 GLN A NE2   1 
ATOM   2517  N  N     . HIS A 1 313 ? 152.324 150.888 124.745 1.00 31.83 ?  313 HIS A N     1 
ATOM   2518  C  CA    . HIS A 1 313 ? 151.876 149.507 124.695 1.00 28.38 ?  313 HIS A CA    1 
ATOM   2519  C  C     . HIS A 1 313 ? 152.741 148.699 123.730 1.00 33.15 ?  313 HIS A C     1 
ATOM   2520  O  O     . HIS A 1 313 ? 153.370 149.235 122.814 1.00 35.26 ?  313 HIS A O     1 
ATOM   2521  C  CB    . HIS A 1 313 ? 150.407 149.433 124.278 1.00 28.95 ?  313 HIS A CB    1 
ATOM   2522  C  CG    . HIS A 1 313 ? 149.481 150.162 125.200 1.00 33.95 ?  313 HIS A CG    1 
ATOM   2523  N  ND1   . HIS A 1 313 ? 149.018 149.614 126.376 1.00 30.64 ?  313 HIS A ND1   1 
ATOM   2524  C  CD2   . HIS A 1 313 ? 148.928 151.395 125.116 1.00 32.84 ?  313 HIS A CD2   1 
ATOM   2525  C  CE1   . HIS A 1 313 ? 148.220 150.478 126.978 1.00 28.85 ?  313 HIS A CE1   1 
ATOM   2526  N  NE2   . HIS A 1 313 ? 148.149 151.567 126.234 1.00 30.06 ?  313 HIS A NE2   1 
ATOM   2527  N  N     . MET A 1 314 ? 152.766 147.382 123.954 1.00 34.61 ?  314 MET A N     1 
ATOM   2528  C  CA    . MET A 1 314 ? 153.589 146.503 123.130 1.00 27.28 ?  314 MET A CA    1 
ATOM   2529  C  C     . MET A 1 314 ? 153.146 146.528 121.673 1.00 31.93 ?  314 MET A C     1 
ATOM   2530  O  O     . MET A 1 314 ? 153.980 146.502 120.762 1.00 36.58 ?  314 MET A O     1 
ATOM   2531  C  CB    . MET A 1 314 ? 153.547 145.079 123.685 1.00 27.70 ?  314 MET A CB    1 
ATOM   2532  C  CG    . MET A 1 314 ? 154.456 144.101 122.962 1.00 28.99 ?  314 MET A CG    1 
ATOM   2533  S  SD    . MET A 1 314 ? 154.048 142.383 123.318 1.00 41.60 ?  314 MET A SD    1 
ATOM   2534  C  CE    . MET A 1 314 ? 152.260 142.456 123.324 1.00 30.84 ?  314 MET A CE    1 
ATOM   2535  N  N     . ASP A 1 315 ? 151.838 146.574 121.430 1.00 33.57 ?  315 ASP A N     1 
ATOM   2536  C  CA    . ASP A 1 315 ? 151.320 146.588 120.069 1.00 36.36 ?  315 ASP A CA    1 
ATOM   2537  C  C     . ASP A 1 315 ? 151.362 147.969 119.424 1.00 33.16 ?  315 ASP A C     1 
ATOM   2538  O  O     . ASP A 1 315 ? 151.028 148.089 118.241 1.00 35.57 ?  315 ASP A O     1 
ATOM   2539  C  CB    . ASP A 1 315 ? 149.887 146.045 120.047 1.00 27.80 ?  315 ASP A CB    1 
ATOM   2540  C  CG    . ASP A 1 315 ? 148.900 146.976 120.718 1.00 34.50 ?  315 ASP A CG    1 
ATOM   2541  O  OD1   . ASP A 1 315 ? 149.318 147.737 121.615 1.00 36.88 ?  315 ASP A OD1   1 
ATOM   2542  O  OD2   . ASP A 1 315 ? 147.707 146.946 120.349 1.00 31.81 -1 315 ASP A OD2   1 
ATOM   2543  N  N     . GLU A 1 316 ? 151.758 149.003 120.159 1.00 30.94 ?  316 GLU A N     1 
ATOM   2544  C  CA    . GLU A 1 316 ? 151.833 150.355 119.621 1.00 31.82 ?  316 GLU A CA    1 
ATOM   2545  C  C     . GLU A 1 316 ? 153.190 150.696 119.022 1.00 34.22 ?  316 GLU A C     1 
ATOM   2546  O  O     . GLU A 1 316 ? 153.328 151.757 118.407 1.00 36.40 ?  316 GLU A O     1 
ATOM   2547  C  CB    . GLU A 1 316 ? 151.492 151.375 120.711 1.00 34.66 ?  316 GLU A CB    1 
ATOM   2548  C  CG    . GLU A 1 316 ? 150.062 151.301 121.204 1.00 35.61 ?  316 GLU A CG    1 
ATOM   2549  C  CD    . GLU A 1 316 ? 149.162 152.300 120.511 1.00 39.42 ?  316 GLU A CD    1 
ATOM   2550  O  OE1   . GLU A 1 316 ? 149.304 152.477 119.283 1.00 36.52 ?  316 GLU A OE1   1 
ATOM   2551  O  OE2   . GLU A 1 316 ? 148.319 152.915 121.196 1.00 45.88 -1 316 GLU A OE2   1 
ATOM   2552  N  N     . MET A 1 317 ? 154.190 149.834 119.182 1.00 40.57 ?  317 MET A N     1 
ATOM   2553  C  CA    . MET A 1 317 ? 155.513 150.066 118.625 1.00 41.21 ?  317 MET A CA    1 
ATOM   2554  C  C     . MET A 1 317 ? 155.879 148.945 117.662 1.00 42.05 ?  317 MET A C     1 
ATOM   2555  O  O     . MET A 1 317 ? 155.306 147.853 117.697 1.00 38.59 ?  317 MET A O     1 
ATOM   2556  C  CB    . MET A 1 317 ? 156.579 150.178 119.722 1.00 40.57 ?  317 MET A CB    1 
ATOM   2557  C  CG    . MET A 1 317 ? 156.087 150.793 121.016 1.00 42.12 ?  317 MET A CG    1 
ATOM   2558  S  SD    . MET A 1 317 ? 157.355 150.768 122.294 1.00 51.18 ?  317 MET A SD    1 
ATOM   2559  C  CE    . MET A 1 317 ? 156.518 149.851 123.578 1.00 35.61 ?  317 MET A CE    1 
ATOM   2560  N  N     . ASP A 1 318 ? 156.855 149.229 116.803 1.00 43.69 ?  318 ASP A N     1 
ATOM   2561  C  CA    . ASP A 1 318 ? 157.294 148.281 115.784 1.00 41.03 ?  318 ASP A CA    1 
ATOM   2562  C  C     . ASP A 1 318 ? 158.104 147.178 116.450 1.00 40.87 ?  318 ASP A C     1 
ATOM   2563  O  O     . ASP A 1 318 ? 159.199 147.425 116.963 1.00 43.57 ?  318 ASP A O     1 
ATOM   2564  C  CB    . ASP A 1 318 ? 158.114 148.992 114.712 1.00 41.27 ?  318 ASP A CB    1 
ATOM   2565  C  CG    . ASP A 1 318 ? 158.719 148.030 113.710 1.00 47.77 ?  318 ASP A CG    1 
ATOM   2566  O  OD1   . ASP A 1 318 ? 158.016 147.085 113.294 1.00 46.74 ?  318 ASP A OD1   1 
ATOM   2567  O  OD2   . ASP A 1 318 ? 159.897 148.220 113.338 1.00 49.13 -1 318 ASP A OD2   1 
ATOM   2568  N  N     . MET A 1 319 ? 157.566 145.957 116.442 1.00 42.96 ?  319 MET A N     1 
ATOM   2569  C  CA    . MET A 1 319 ? 158.252 144.829 117.058 1.00 36.29 ?  319 MET A CA    1 
ATOM   2570  C  C     . MET A 1 319 ? 159.538 144.464 116.327 1.00 36.71 ?  319 MET A C     1 
ATOM   2571  O  O     . MET A 1 319 ? 160.442 143.893 116.943 1.00 41.37 ?  319 MET A O     1 
ATOM   2572  C  CB    . MET A 1 319 ? 157.309 143.623 117.122 1.00 33.84 ?  319 MET A CB    1 
ATOM   2573  C  CG    . MET A 1 319 ? 157.959 142.323 117.572 1.00 38.01 ?  319 MET A CG    1 
ATOM   2574  S  SD    . MET A 1 319 ? 157.988 142.099 119.363 1.00 45.80 ?  319 MET A SD    1 
ATOM   2575  C  CE    . MET A 1 319 ? 156.613 143.123 119.878 1.00 34.85 ?  319 MET A CE    1 
ATOM   2576  N  N     . ASN A 1 320 ? 159.659 144.809 115.044 1.00 38.02 ?  320 ASN A N     1 
ATOM   2577  C  CA    . ASN A 1 320 ? 160.876 144.481 114.309 1.00 41.12 ?  320 ASN A CA    1 
ATOM   2578  C  C     . ASN A 1 320 ? 162.093 145.168 114.917 1.00 41.90 ?  320 ASN A C     1 
ATOM   2579  O  O     . ASN A 1 320 ? 163.166 144.563 115.028 1.00 41.32 ?  320 ASN A O     1 
ATOM   2580  C  CB    . ASN A 1 320 ? 160.719 144.861 112.838 1.00 41.65 ?  320 ASN A CB    1 
ATOM   2581  C  CG    . ASN A 1 320 ? 160.074 143.761 112.021 1.00 43.37 ?  320 ASN A CG    1 
ATOM   2582  O  OD1   . ASN A 1 320 ? 158.861 143.561 112.076 1.00 38.61 ?  320 ASN A OD1   1 
ATOM   2583  N  ND2   . ASN A 1 320 ? 160.886 143.038 111.258 1.00 40.60 ?  320 ASN A ND2   1 
ATOM   2584  N  N     . GLU A 1 321 ? 161.946 146.428 115.319 1.00 42.91 ?  321 GLU A N     1 
ATOM   2585  C  CA    . GLU A 1 321 ? 163.031 147.164 115.953 1.00 44.57 ?  321 GLU A CA    1 
ATOM   2586  C  C     . GLU A 1 321 ? 162.982 147.112 117.475 1.00 42.96 ?  321 GLU A C     1 
ATOM   2587  O  O     . GLU A 1 321 ? 163.957 147.508 118.123 1.00 44.36 ?  321 GLU A O     1 
ATOM   2588  C  CB    . GLU A 1 321 ? 163.014 148.626 115.496 1.00 44.39 ?  321 GLU A CB    1 
ATOM   2589  C  CG    . GLU A 1 321 ? 161.812 149.413 115.989 1.00 47.17 ?  321 GLU A CG    1 
ATOM   2590  C  CD    . GLU A 1 321 ? 162.160 150.844 116.348 1.00 49.00 ?  321 GLU A CD    1 
ATOM   2591  O  OE1   . GLU A 1 321 ? 163.257 151.072 116.898 1.00 46.69 ?  321 GLU A OE1   1 
ATOM   2592  O  OE2   . GLU A 1 321 ? 161.334 151.742 116.079 1.00 47.46 -1 321 GLU A OE2   1 
ATOM   2593  N  N     . MET A 1 322 ? 161.883 146.636 118.058 1.00 41.35 ?  322 MET A N     1 
ATOM   2594  C  CA    . MET A 1 322 ? 161.711 146.627 119.503 1.00 35.79 ?  322 MET A CA    1 
ATOM   2595  C  C     . MET A 1 322 ? 161.941 145.261 120.137 1.00 33.07 ?  322 MET A C     1 
ATOM   2596  O  O     . MET A 1 322 ? 162.071 145.185 121.361 1.00 41.00 ?  322 MET A O     1 
ATOM   2597  C  CB    . MET A 1 322 ? 160.302 147.109 119.872 1.00 34.29 ?  322 MET A CB    1 
ATOM   2598  C  CG    . MET A 1 322 ? 160.185 148.598 120.153 1.00 39.93 ?  322 MET A CG    1 
ATOM   2599  S  SD    . MET A 1 322 ? 161.517 149.246 121.174 1.00 48.26 ?  322 MET A SD    1 
ATOM   2600  C  CE    . MET A 1 322 ? 162.311 150.351 120.011 1.00 39.75 ?  322 MET A CE    1 
ATOM   2601  N  N     . TYR A 1 323 ? 161.978 144.188 119.343 1.00 31.27 ?  323 TYR A N     1 
ATOM   2602  C  CA    . TYR A 1 323 ? 162.031 142.842 119.906 1.00 32.27 ?  323 TYR A CA    1 
ATOM   2603  C  C     . TYR A 1 323 ? 163.346 142.594 120.634 1.00 36.70 ?  323 TYR A C     1 
ATOM   2604  O  O     . TYR A 1 323 ? 163.361 142.043 121.741 1.00 38.05 ?  323 TYR A O     1 
ATOM   2605  C  CB    . TYR A 1 323 ? 161.824 141.808 118.799 1.00 30.02 ?  323 TYR A CB    1 
ATOM   2606  C  CG    . TYR A 1 323 ? 161.955 140.377 119.262 1.00 35.95 ?  323 TYR A CG    1 
ATOM   2607  C  CD1   . TYR A 1 323 ? 160.882 139.715 119.843 1.00 31.23 ?  323 TYR A CD1   1 
ATOM   2608  C  CD2   . TYR A 1 323 ? 163.150 139.686 119.119 1.00 33.51 ?  323 TYR A CD2   1 
ATOM   2609  C  CE1   . TYR A 1 323 ? 160.997 138.408 120.267 1.00 28.78 ?  323 TYR A CE1   1 
ATOM   2610  C  CE2   . TYR A 1 323 ? 163.274 138.381 119.540 1.00 26.53 ?  323 TYR A CE2   1 
ATOM   2611  C  CZ    . TYR A 1 323 ? 162.195 137.746 120.114 1.00 31.76 ?  323 TYR A CZ    1 
ATOM   2612  O  OH    . TYR A 1 323 ? 162.317 136.444 120.535 1.00 34.72 ?  323 TYR A OH    1 
ATOM   2613  N  N     . ASP A 1 324 ? 164.464 142.986 120.020 1.00 38.06 ?  324 ASP A N     1 
ATOM   2614  C  CA    . ASP A 1 324 ? 165.760 142.788 120.658 1.00 37.16 ?  324 ASP A CA    1 
ATOM   2615  C  C     . ASP A 1 324 ? 165.872 143.605 121.936 1.00 39.55 ?  324 ASP A C     1 
ATOM   2616  O  O     . ASP A 1 324 ? 166.423 143.134 122.938 1.00 45.08 ?  324 ASP A O     1 
ATOM   2617  C  CB    . ASP A 1 324 ? 166.883 143.149 119.687 1.00 40.36 ?  324 ASP A CB    1 
ATOM   2618  C  CG    . ASP A 1 324 ? 166.976 142.188 118.521 1.00 43.01 ?  324 ASP A CG    1 
ATOM   2619  O  OD1   . ASP A 1 324 ? 166.775 140.973 118.731 1.00 43.21 ?  324 ASP A OD1   1 
ATOM   2620  O  OD2   . ASP A 1 324 ? 167.249 142.646 117.392 1.00 43.38 -1 324 ASP A OD2   1 
ATOM   2621  N  N     . LYS A 1 325 ? 165.352 144.834 121.922 1.00 37.78 ?  325 LYS A N     1 
ATOM   2622  C  CA    . LYS A 1 325 ? 165.390 145.664 123.121 1.00 37.22 ?  325 LYS A CA    1 
ATOM   2623  C  C     . LYS A 1 325 ? 164.507 145.088 124.221 1.00 37.32 ?  325 LYS A C     1 
ATOM   2624  O  O     . LYS A 1 325 ? 164.862 145.153 125.402 1.00 44.63 ?  325 LYS A O     1 
ATOM   2625  C  CB    . LYS A 1 325 ? 164.976 147.094 122.780 1.00 40.71 ?  325 LYS A CB    1 
ATOM   2626  C  CG    . LYS A 1 325 ? 165.923 147.783 121.813 1.00 40.43 ?  325 LYS A CG    1 
ATOM   2627  C  CD    . LYS A 1 325 ? 165.430 149.169 121.440 1.00 40.26 ?  325 LYS A CD    1 
ATOM   2628  C  CE    . LYS A 1 325 ? 166.285 149.780 120.341 1.00 41.23 ?  325 LYS A CE    1 
ATOM   2629  N  NZ    . LYS A 1 325 ? 165.608 150.933 119.689 1.00 45.47 1  325 LYS A NZ    1 
ATOM   2630  N  N     . PHE A 1 326 ? 163.352 144.529 123.856 1.00 37.17 ?  326 PHE A N     1 
ATOM   2631  C  CA    . PHE A 1 326 ? 162.506 143.866 124.843 1.00 36.58 ?  326 PHE A CA    1 
ATOM   2632  C  C     . PHE A 1 326 ? 163.219 142.665 125.450 1.00 34.61 ?  326 PHE A C     1 
ATOM   2633  O  O     . PHE A 1 326 ? 163.193 142.463 126.669 1.00 41.38 ?  326 PHE A O     1 
ATOM   2634  C  CB    . PHE A 1 326 ? 161.188 143.426 124.203 1.00 34.54 ?  326 PHE A CB    1 
ATOM   2635  C  CG    . PHE A 1 326 ? 160.304 144.560 123.768 1.00 34.95 ?  326 PHE A CG    1 
ATOM   2636  C  CD1   . PHE A 1 326 ? 160.445 145.824 124.313 1.00 36.22 ?  326 PHE A CD1   1 
ATOM   2637  C  CD2   . PHE A 1 326 ? 159.326 144.357 122.810 1.00 34.82 ?  326 PHE A CD2   1 
ATOM   2638  C  CE1   . PHE A 1 326 ? 159.627 146.862 123.909 1.00 36.18 ?  326 PHE A CE1   1 
ATOM   2639  C  CE2   . PHE A 1 326 ? 158.505 145.390 122.405 1.00 36.20 ?  326 PHE A CE2   1 
ATOM   2640  C  CZ    . PHE A 1 326 ? 158.656 146.643 122.955 1.00 38.81 ?  326 PHE A CZ    1 
ATOM   2641  N  N     . VAL A 1 327 ? 163.862 141.855 124.608 1.00 38.25 ?  327 VAL A N     1 
ATOM   2642  C  CA    . VAL A 1 327 ? 164.537 140.654 125.092 1.00 39.48 ?  327 VAL A CA    1 
ATOM   2643  C  C     . VAL A 1 327 ? 165.707 141.023 125.998 1.00 42.72 ?  327 VAL A C     1 
ATOM   2644  O  O     . VAL A 1 327 ? 165.908 140.410 127.054 1.00 44.58 ?  327 VAL A O     1 
ATOM   2645  C  CB    . VAL A 1 327 ? 164.987 139.782 123.905 1.00 37.45 ?  327 VAL A CB    1 
ATOM   2646  C  CG1   . VAL A 1 327 ? 165.898 138.662 124.380 1.00 40.17 ?  327 VAL A CG1   1 
ATOM   2647  C  CG2   . VAL A 1 327 ? 163.779 139.214 123.181 1.00 32.45 ?  327 VAL A CG2   1 
ATOM   2648  N  N     . ASP A 1 328 ? 166.488 142.029 125.609 1.00 40.53 ?  328 ASP A N     1 
ATOM   2649  C  CA    . ASP A 1 328 ? 167.655 142.433 126.382 1.00 39.72 ?  328 ASP A CA    1 
ATOM   2650  C  C     . ASP A 1 328 ? 167.305 143.284 127.595 1.00 43.46 ?  328 ASP A C     1 
ATOM   2651  O  O     . ASP A 1 328 ? 168.196 143.576 128.400 1.00 47.01 ?  328 ASP A O     1 
ATOM   2652  C  CB    . ASP A 1 328 ? 168.635 143.198 125.489 1.00 41.20 ?  328 ASP A CB    1 
ATOM   2653  C  CG    . ASP A 1 328 ? 169.238 142.326 124.405 1.00 48.04 ?  328 ASP A CG    1 
ATOM   2654  O  OD1   . ASP A 1 328 ? 168.787 141.171 124.249 1.00 46.00 ?  328 ASP A OD1   1 
ATOM   2655  O  OD2   . ASP A 1 328 ? 170.161 142.795 123.708 1.00 47.87 -1 328 ASP A OD2   1 
ATOM   2656  N  N     . ASN A 1 329 ? 166.046 143.688 127.748 1.00 40.52 ?  329 ASN A N     1 
ATOM   2657  C  CA    . ASN A 1 329 ? 165.647 144.514 128.879 1.00 40.00 ?  329 ASN A CA    1 
ATOM   2658  C  C     . ASN A 1 329 ? 165.292 143.626 130.062 1.00 43.33 ?  329 ASN A C     1 
ATOM   2659  O  O     . ASN A 1 329 ? 164.343 142.836 129.966 1.00 43.25 ?  329 ASN A O     1 
ATOM   2660  C  CB    . ASN A 1 329 ? 164.459 145.388 128.513 1.00 36.36 ?  329 ASN A CB    1 
ATOM   2661  C  CG    . ASN A 1 329 ? 164.307 146.579 129.435 1.00 38.87 ?  329 ASN A CG    1 
ATOM   2662  O  OD1   . ASN A 1 329 ? 164.349 146.443 130.657 1.00 45.50 ?  329 ASN A OD1   1 
ATOM   2663  N  ND2   . ASN A 1 329 ? 164.134 147.758 128.852 1.00 36.20 ?  329 ASN A ND2   1 
ATOM   2664  N  N     . PRO A 1 330 ? 166.017 143.709 131.182 1.00 43.62 ?  330 PRO A N     1 
ATOM   2665  C  CA    . PRO A 1 330 ? 165.657 142.882 132.343 1.00 38.70 ?  330 PRO A CA    1 
ATOM   2666  C  C     . PRO A 1 330 ? 164.323 143.259 132.962 1.00 38.18 ?  330 PRO A C     1 
ATOM   2667  O  O     . PRO A 1 330 ? 163.672 142.401 133.569 1.00 41.07 ?  330 PRO A O     1 
ATOM   2668  C  CB    . PRO A 1 330 ? 166.820 143.120 133.316 1.00 40.51 ?  330 PRO A CB    1 
ATOM   2669  C  CG    . PRO A 1 330 ? 167.349 144.462 132.939 1.00 38.95 ?  330 PRO A CG    1 
ATOM   2670  C  CD    . PRO A 1 330 ? 167.185 144.565 131.450 1.00 40.23 ?  330 PRO A CD    1 
ATOM   2671  N  N     . ARG A 1 331 ? 163.895 144.514 132.827 1.00 37.03 ?  331 ARG A N     1 
ATOM   2672  C  CA    . ARG A 1 331 ? 162.636 144.959 133.412 1.00 38.27 ?  331 ARG A CA    1 
ATOM   2673  C  C     . ARG A 1 331 ? 161.425 144.572 132.577 1.00 39.55 ?  331 ARG A C     1 
ATOM   2674  O  O     . ARG A 1 331 ? 160.292 144.803 133.016 1.00 38.55 ?  331 ARG A O     1 
ATOM   2675  C  CB    . ARG A 1 331 ? 162.664 146.475 133.619 1.00 36.84 ?  331 ARG A CB    1 
ATOM   2676  C  CG    . ARG A 1 331 ? 163.587 146.917 134.742 1.00 38.30 ?  331 ARG A CG    1 
ATOM   2677  C  CD    . ARG A 1 331 ? 163.877 148.408 134.677 1.00 38.69 ?  331 ARG A CD    1 
ATOM   2678  N  NE    . ARG A 1 331 ? 164.418 148.807 133.384 1.00 41.16 ?  331 ARG A NE    1 
ATOM   2679  C  CZ    . ARG A 1 331 ? 165.650 148.544 132.969 1.00 40.35 ?  331 ARG A CZ    1 
ATOM   2680  N  NH1   . ARG A 1 331 ? 166.509 147.882 133.727 1.00 42.22 1  331 ARG A NH1   1 
ATOM   2681  N  NH2   . ARG A 1 331 ? 166.030 148.955 131.763 1.00 35.96 ?  331 ARG A NH2   1 
ATOM   2682  N  N     . VAL A 1 332 ? 161.630 143.997 131.397 1.00 35.93 ?  332 VAL A N     1 
ATOM   2683  C  CA    . VAL A 1 332 ? 160.550 143.469 130.574 1.00 34.17 ?  332 VAL A CA    1 
ATOM   2684  C  C     . VAL A 1 332 ? 160.473 141.969 130.823 1.00 37.50 ?  332 VAL A C     1 
ATOM   2685  O  O     . VAL A 1 332 ? 161.450 141.244 130.605 1.00 37.78 ?  332 VAL A O     1 
ATOM   2686  C  CB    . VAL A 1 332 ? 160.777 143.774 129.086 1.00 34.74 ?  332 VAL A CB    1 
ATOM   2687  C  CG1   . VAL A 1 332 ? 159.903 142.880 128.220 1.00 34.04 ?  332 VAL A CG1   1 
ATOM   2688  C  CG2   . VAL A 1 332 ? 160.501 145.239 128.796 1.00 35.22 ?  332 VAL A CG2   1 
ATOM   2689  N  N     . LYS A 1 333 ? 159.318 141.503 131.289 1.00 33.45 ?  333 LYS A N     1 
ATOM   2690  C  CA    . LYS A 1 333 ? 159.121 140.091 131.579 1.00 31.89 ?  333 LYS A CA    1 
ATOM   2691  C  C     . LYS A 1 333 ? 158.654 139.367 130.325 1.00 32.22 ?  333 LYS A C     1 
ATOM   2692  O  O     . LYS A 1 333 ? 157.793 139.859 129.591 1.00 36.70 ?  333 LYS A O     1 
ATOM   2693  C  CB    . LYS A 1 333 ? 158.107 139.910 132.709 1.00 29.77 ?  333 LYS A CB    1 
ATOM   2694  C  CG    . LYS A 1 333 ? 157.948 138.476 133.181 1.00 32.83 ?  333 LYS A CG    1 
ATOM   2695  C  CD    . LYS A 1 333 ? 157.154 138.409 134.474 1.00 33.72 ?  333 LYS A CD    1 
ATOM   2696  C  CE    . LYS A 1 333 ? 157.219 137.023 135.091 1.00 36.46 ?  333 LYS A CE    1 
ATOM   2697  N  NZ    . LYS A 1 333 ? 155.879 136.555 135.541 1.00 38.82 1  333 LYS A NZ    1 
ATOM   2698  N  N     . LYS A 1 334 ? 159.230 138.191 130.082 1.00 35.19 ?  334 LYS A N     1 
ATOM   2699  C  CA    . LYS A 1 334 ? 158.958 137.448 128.862 1.00 33.26 ?  334 LYS A CA    1 
ATOM   2700  C  C     . LYS A 1 334 ? 159.055 135.957 129.143 1.00 37.91 ?  334 LYS A C     1 
ATOM   2701  O  O     . LYS A 1 334 ? 159.668 135.526 130.124 1.00 40.87 ?  334 LYS A O     1 
ATOM   2702  C  CB    . LYS A 1 334 ? 159.930 137.838 127.743 1.00 31.87 ?  334 LYS A CB    1 
ATOM   2703  C  CG    . LYS A 1 334 ? 161.387 137.630 128.104 1.00 34.69 ?  334 LYS A CG    1 
ATOM   2704  C  CD    . LYS A 1 334 ? 162.289 138.554 127.313 1.00 33.81 ?  334 LYS A CD    1 
ATOM   2705  C  CE    . LYS A 1 334 ? 162.808 139.685 128.182 1.00 35.60 ?  334 LYS A CE    1 
ATOM   2706  N  NZ    . LYS A 1 334 ? 163.708 139.194 129.259 1.00 37.49 1  334 LYS A NZ    1 
ATOM   2707  N  N     . GLU A 1 335 ? 158.435 135.172 128.267 1.00 35.08 ?  335 GLU A N     1 
ATOM   2708  C  CA    . GLU A 1 335 ? 158.468 133.719 128.340 1.00 35.23 ?  335 GLU A CA    1 
ATOM   2709  C  C     . GLU A 1 335 ? 158.981 133.146 127.027 1.00 39.41 ?  335 GLU A C     1 
ATOM   2710  O  O     . GLU A 1 335 ? 158.630 133.626 125.945 1.00 44.34 ?  335 GLU A O     1 
ATOM   2711  C  CB    . GLU A 1 335 ? 157.085 133.142 128.660 1.00 34.11 ?  335 GLU A CB    1 
ATOM   2712  C  CG    . GLU A 1 335 ? 156.389 133.822 129.825 1.00 43.30 ?  335 GLU A CG    1 
ATOM   2713  C  CD    . GLU A 1 335 ? 156.187 132.892 131.006 1.00 43.64 ?  335 GLU A CD    1 
ATOM   2714  O  OE1   . GLU A 1 335 ? 157.165 132.234 131.420 1.00 40.96 ?  335 GLU A OE1   1 
ATOM   2715  O  OE2   . GLU A 1 335 ? 155.053 132.819 131.522 1.00 38.15 -1 335 GLU A OE2   1 
ATOM   2716  N  N     . LYS A 1 336 ? 159.819 132.119 127.139 1.00 38.66 ?  336 LYS A N     1 
ATOM   2717  C  CA    . LYS A 1 336 ? 160.400 131.452 125.982 1.00 34.38 ?  336 LYS A CA    1 
ATOM   2718  C  C     . LYS A 1 336 ? 159.354 130.589 125.286 1.00 38.68 ?  336 LYS A C     1 
ATOM   2719  O  O     . LYS A 1 336 ? 158.619 129.841 125.938 1.00 41.63 ?  336 LYS A O     1 
ATOM   2720  C  CB    . LYS A 1 336 ? 161.583 130.594 126.424 1.00 40.52 ?  336 LYS A CB    1 
ATOM   2721  C  CG    . LYS A 1 336 ? 162.760 130.560 125.468 1.00 42.05 ?  336 LYS A CG    1 
ATOM   2722  C  CD    . LYS A 1 336 ? 163.687 129.405 125.826 1.00 41.51 ?  336 LYS A CD    1 
ATOM   2723  C  CE    . LYS A 1 336 ? 164.518 128.957 124.640 1.00 40.22 ?  336 LYS A CE    1 
ATOM   2724  N  NZ    . LYS A 1 336 ? 165.147 127.627 124.868 1.00 41.73 1  336 LYS A NZ    1 
ATOM   2725  N  N     . ILE A 1 337 ? 159.287 130.694 123.956 1.00 36.69 ?  337 ILE A N     1 
ATOM   2726  C  CA    . ILE A 1 337 ? 158.407 129.867 123.141 1.00 33.68 ?  337 ILE A CA    1 
ATOM   2727  C  C     . ILE A 1 337 ? 159.163 129.437 121.892 1.00 32.64 ?  337 ILE A C     1 
ATOM   2728  O  O     . ILE A 1 337 ? 160.200 130.001 121.537 1.00 36.49 ?  337 ILE A O     1 
ATOM   2729  C  CB    . ILE A 1 337 ? 157.104 130.595 122.741 1.00 34.61 ?  337 ILE A CB    1 
ATOM   2730  C  CG1   . ILE A 1 337 ? 157.426 131.914 122.037 1.00 33.71 ?  337 ILE A CG1   1 
ATOM   2731  C  CG2   . ILE A 1 337 ? 156.213 130.820 123.954 1.00 35.33 ?  337 ILE A CG2   1 
ATOM   2732  C  CD1   . ILE A 1 337 ? 156.539 132.203 120.851 1.00 31.06 ?  337 ILE A CD1   1 
ATOM   2733  N  N     . ASN A 1 338 ? 158.626 128.419 121.221 1.00 33.74 ?  338 ASN A N     1 
ATOM   2734  C  CA    . ASN A 1 338 ? 159.156 128.001 119.934 1.00 35.16 ?  338 ASN A CA    1 
ATOM   2735  C  C     . ASN A 1 338 ? 158.247 128.535 118.841 1.00 32.98 ?  338 ASN A C     1 
ATOM   2736  O  O     . ASN A 1 338 ? 157.096 128.084 118.734 1.00 34.04 ?  338 ASN A O     1 
ATOM   2737  C  CB    . ASN A 1 338 ? 159.258 126.480 119.852 1.00 35.34 ?  338 ASN A CB    1 
ATOM   2738  C  CG    . ASN A 1 338 ? 160.002 126.013 118.616 1.00 36.98 ?  338 ASN A CG    1 
ATOM   2739  O  OD1   . ASN A 1 338 ? 159.617 125.037 117.976 1.00 37.66 ?  338 ASN A OD1   1 
ATOM   2740  N  ND2   . ASN A 1 338 ? 161.075 126.716 118.274 1.00 37.68 ?  338 ASN A ND2   1 
ATOM   2741  N  N     . PRO A 1 339 ? 158.694 129.493 118.026 1.00 35.25 ?  339 PRO A N     1 
ATOM   2742  C  CA    . PRO A 1 339 ? 157.804 130.053 116.996 1.00 31.07 ?  339 PRO A CA    1 
ATOM   2743  C  C     . PRO A 1 339 ? 157.317 129.031 115.984 1.00 32.75 ?  339 PRO A C     1 
ATOM   2744  O  O     . PRO A 1 339 ? 156.186 129.151 115.499 1.00 37.31 ?  339 PRO A O     1 
ATOM   2745  C  CB    . PRO A 1 339 ? 158.669 131.136 116.336 1.00 31.83 ?  339 PRO A CB    1 
ATOM   2746  C  CG    . PRO A 1 339 ? 160.071 130.762 116.660 1.00 34.70 ?  339 PRO A CG    1 
ATOM   2747  C  CD    . PRO A 1 339 ? 160.028 130.113 118.005 1.00 33.83 ?  339 PRO A CD    1 
ATOM   2748  N  N     . ARG A 1 340 ? 158.132 128.031 115.644 1.00 32.40 ?  340 ARG A N     1 
ATOM   2749  C  CA    . ARG A 1 340 ? 157.671 126.993 114.728 1.00 27.98 ?  340 ARG A CA    1 
ATOM   2750  C  C     . ARG A 1 340 ? 156.588 126.136 115.369 1.00 31.44 ?  340 ARG A C     1 
ATOM   2751  O  O     . ARG A 1 340 ? 155.618 125.751 114.706 1.00 37.96 ?  340 ARG A O     1 
ATOM   2752  C  CB    . ARG A 1 340 ? 158.848 126.134 114.270 1.00 30.71 ?  340 ARG A CB    1 
ATOM   2753  C  CG    . ARG A 1 340 ? 159.735 126.822 113.250 1.00 30.19 ?  340 ARG A CG    1 
ATOM   2754  C  CD    . ARG A 1 340 ? 160.614 125.836 112.508 1.00 27.86 ?  340 ARG A CD    1 
ATOM   2755  N  NE    . ARG A 1 340 ? 161.496 126.516 111.567 1.00 30.37 ?  340 ARG A NE    1 
ATOM   2756  C  CZ    . ARG A 1 340 ? 162.425 125.914 110.839 1.00 32.54 ?  340 ARG A CZ    1 
ATOM   2757  N  NH1   . ARG A 1 340 ? 162.624 124.609 110.915 1.00 32.83 1  340 ARG A NH1   1 
ATOM   2758  N  NH2   . ARG A 1 340 ? 163.173 126.640 110.012 1.00 32.68 ?  340 ARG A NH2   1 
ATOM   2759  N  N     . LYS A 1 341 ? 156.731 125.835 116.661 1.00 33.69 ?  341 LYS A N     1 
ATOM   2760  C  CA    . LYS A 1 341 ? 155.669 125.133 117.374 1.00 32.33 ?  341 LYS A CA    1 
ATOM   2761  C  C     . LYS A 1 341 ? 154.393 125.964 117.410 1.00 31.94 ?  341 LYS A C     1 
ATOM   2762  O  O     . LYS A 1 341 ? 153.290 125.425 117.278 1.00 35.86 ?  341 LYS A O     1 
ATOM   2763  C  CB    . LYS A 1 341 ? 156.123 124.784 118.791 1.00 35.30 ?  341 LYS A CB    1 
ATOM   2764  C  CG    . LYS A 1 341 ? 156.955 123.517 118.885 1.00 37.81 ?  341 LYS A CG    1 
ATOM   2765  C  CD    . LYS A 1 341 ? 156.294 122.360 118.155 1.00 36.37 ?  341 LYS A CD    1 
ATOM   2766  C  CE    . LYS A 1 341 ? 157.328 121.457 117.505 1.00 38.19 ?  341 LYS A CE    1 
ATOM   2767  N  NZ    . LYS A 1 341 ? 158.196 122.205 116.554 1.00 38.23 1  341 LYS A NZ    1 
ATOM   2768  N  N     . LEU A 1 342 ? 154.525 127.279 117.589 1.00 29.81 ?  342 LEU A N     1 
ATOM   2769  C  CA    . LEU A 1 342 ? 153.350 128.145 117.586 1.00 27.23 ?  342 LEU A CA    1 
ATOM   2770  C  C     . LEU A 1 342 ? 152.688 128.175 116.212 1.00 29.81 ?  342 LEU A C     1 
ATOM   2771  O  O     . LEU A 1 342 ? 151.456 128.181 116.112 1.00 36.01 ?  342 LEU A O     1 
ATOM   2772  C  CB    . LEU A 1 342 ? 153.741 129.553 118.035 1.00 28.01 ?  342 LEU A CB    1 
ATOM   2773  C  CG    . LEU A 1 342 ? 152.610 130.506 118.419 1.00 27.34 ?  342 LEU A CG    1 
ATOM   2774  C  CD1   . LEU A 1 342 ? 151.534 129.775 119.200 1.00 26.87 ?  342 LEU A CD1   1 
ATOM   2775  C  CD2   . LEU A 1 342 ? 153.158 131.668 119.228 1.00 28.36 ?  342 LEU A CD2   1 
ATOM   2776  N  N     . LEU A 1 343 ? 153.488 128.197 115.144 1.00 28.68 ?  343 LEU A N     1 
ATOM   2777  C  CA    . LEU A 1 343 ? 152.930 128.141 113.795 1.00 24.60 ?  343 LEU A CA    1 
ATOM   2778  C  C     . LEU A 1 343 ? 152.207 126.823 113.551 1.00 31.50 ?  343 LEU A C     1 
ATOM   2779  O  O     . LEU A 1 343 ? 151.131 126.797 112.941 1.00 36.23 ?  343 LEU A O     1 
ATOM   2780  C  CB    . LEU A 1 343 ? 154.038 128.343 112.763 1.00 28.60 ?  343 LEU A CB    1 
ATOM   2781  C  CG    . LEU A 1 343 ? 154.417 129.785 112.430 1.00 31.05 ?  343 LEU A CG    1 
ATOM   2782  C  CD1   . LEU A 1 343 ? 155.403 129.821 111.276 1.00 27.29 ?  343 LEU A CD1   1 
ATOM   2783  C  CD2   . LEU A 1 343 ? 153.179 130.604 112.104 1.00 30.62 ?  343 LEU A CD2   1 
ATOM   2784  N  N     . GLU A 1 344 ? 152.791 125.715 114.011 1.00 34.59 ?  344 GLU A N     1 
ATOM   2785  C  CA    . GLU A 1 344 ? 152.132 124.422 113.871 1.00 30.94 ?  344 GLU A CA    1 
ATOM   2786  C  C     . GLU A 1 344 ? 150.839 124.378 114.674 1.00 30.40 ?  344 GLU A C     1 
ATOM   2787  O  O     . GLU A 1 344 ? 149.850 123.782 114.236 1.00 39.33 ?  344 GLU A O     1 
ATOM   2788  C  CB    . GLU A 1 344 ? 153.075 123.299 114.301 1.00 31.41 ?  344 GLU A CB    1 
ATOM   2789  C  CG    . GLU A 1 344 ? 154.286 123.135 113.398 1.00 33.61 ?  344 GLU A CG    1 
ATOM   2790  C  CD    . GLU A 1 344 ? 155.396 122.337 114.052 1.00 40.44 ?  344 GLU A CD    1 
ATOM   2791  O  OE1   . GLU A 1 344 ? 155.124 121.660 115.066 1.00 41.47 ?  344 GLU A OE1   1 
ATOM   2792  O  OE2   . GLU A 1 344 ? 156.540 122.390 113.556 1.00 40.14 -1 344 GLU A OE2   1 
ATOM   2793  N  N     . LYS A 1 345 ? 150.829 124.999 115.854 1.00 29.13 ?  345 LYS A N     1 
ATOM   2794  C  CA    . LYS A 1 345 ? 149.602 125.085 116.641 1.00 29.09 ?  345 LYS A CA    1 
ATOM   2795  C  C     . LYS A 1 345 ? 148.540 125.903 115.919 1.00 29.83 ?  345 LYS A C     1 
ATOM   2796  O  O     . LYS A 1 345 ? 147.358 125.538 115.927 1.00 31.83 ?  345 LYS A O     1 
ATOM   2797  C  CB    . LYS A 1 345 ? 149.902 125.685 118.015 1.00 26.73 ?  345 LYS A CB    1 
ATOM   2798  C  CG    . LYS A 1 345 ? 148.691 125.769 118.928 1.00 29.26 ?  345 LYS A CG    1 
ATOM   2799  C  CD    . LYS A 1 345 ? 149.056 126.340 120.285 1.00 30.18 ?  345 LYS A CD    1 
ATOM   2800  C  CE    . LYS A 1 345 ? 147.830 126.456 121.175 1.00 32.03 ?  345 LYS A CE    1 
ATOM   2801  N  NZ    . LYS A 1 345 ? 148.151 127.065 122.493 1.00 31.82 1  345 LYS A NZ    1 
ATOM   2802  N  N     . LEU A 1 346 ? 148.939 127.012 115.292 1.00 32.88 ?  346 LEU A N     1 
ATOM   2803  C  CA    . LEU A 1 346 ? 147.997 127.802 114.505 1.00 25.13 ?  346 LEU A CA    1 
ATOM   2804  C  C     . LEU A 1 346 ? 147.418 126.982 113.360 1.00 26.69 ?  346 LEU A C     1 
ATOM   2805  O  O     . LEU A 1 346 ? 146.206 127.010 113.116 1.00 32.19 ?  346 LEU A O     1 
ATOM   2806  C  CB    . LEU A 1 346 ? 148.680 129.056 113.957 1.00 24.17 ?  346 LEU A CB    1 
ATOM   2807  C  CG    . LEU A 1 346 ? 149.203 130.110 114.932 1.00 26.88 ?  346 LEU A CG    1 
ATOM   2808  C  CD1   . LEU A 1 346 ? 150.186 131.028 114.229 1.00 27.67 ?  346 LEU A CD1   1 
ATOM   2809  C  CD2   . LEU A 1 346 ? 148.060 130.911 115.513 1.00 28.49 ?  346 LEU A CD2   1 
ATOM   2810  N  N     . ALA A 1 347 ? 148.272 126.244 112.648 1.00 25.65 ?  347 ALA A N     1 
ATOM   2811  C  CA    . ALA A 1 347 ? 147.799 125.424 111.537 1.00 26.16 ?  347 ALA A CA    1 
ATOM   2812  C  C     . ALA A 1 347 ? 146.865 124.320 112.019 1.00 29.62 ?  347 ALA A C     1 
ATOM   2813  O  O     . ALA A 1 347 ? 145.839 124.048 111.386 1.00 35.76 ?  347 ALA A O     1 
ATOM   2814  C  CB    . ALA A 1 347 ? 148.985 124.832 110.778 1.00 26.21 ?  347 ALA A CB    1 
ATOM   2815  N  N     . MET A 1 348 ? 147.201 123.677 113.140 1.00 31.30 ?  348 MET A N     1 
ATOM   2816  C  CA    . MET A 1 348 ? 146.343 122.629 113.681 1.00 34.50 ?  348 MET A CA    1 
ATOM   2817  C  C     . MET A 1 348 ? 144.991 123.187 114.103 1.00 31.34 ?  348 MET A C     1 
ATOM   2818  O  O     . MET A 1 348 ? 143.947 122.584 113.827 1.00 36.47 ?  348 MET A O     1 
ATOM   2819  C  CB    . MET A 1 348 ? 147.038 121.945 114.859 1.00 32.72 ?  348 MET A CB    1 
ATOM   2820  C  CG    . MET A 1 348 ? 146.116 121.123 115.743 1.00 37.45 ?  348 MET A CG    1 
ATOM   2821  S  SD    . MET A 1 348 ? 145.867 121.863 117.370 1.00 55.87 ?  348 MET A SD    1 
ATOM   2822  C  CE    . MET A 1 348 ? 147.540 121.852 118.008 1.00 38.89 ?  348 MET A CE    1 
ATOM   2823  N  N     . LEU A 1 349 ? 144.989 124.346 114.765 1.00 27.73 ?  349 LEU A N     1 
ATOM   2824  C  CA    . LEU A 1 349 ? 143.733 124.954 115.188 1.00 22.99 ?  349 LEU A CA    1 
ATOM   2825  C  C     . LEU A 1 349 ? 142.888 125.366 113.992 1.00 28.25 ?  349 LEU A C     1 
ATOM   2826  O  O     . LEU A 1 349 ? 141.660 125.225 114.013 1.00 30.06 ?  349 LEU A O     1 
ATOM   2827  C  CB    . LEU A 1 349 ? 144.013 126.155 116.088 1.00 26.16 ?  349 LEU A CB    1 
ATOM   2828  C  CG    . LEU A 1 349 ? 144.055 125.847 117.582 1.00 32.55 ?  349 LEU A CG    1 
ATOM   2829  C  CD1   . LEU A 1 349 ? 144.877 126.892 118.302 1.00 30.67 ?  349 LEU A CD1   1 
ATOM   2830  C  CD2   . LEU A 1 349 ? 142.651 125.776 118.157 1.00 34.59 ?  349 LEU A CD2   1 
ATOM   2831  N  N     . ARG A 1 350 ? 143.524 125.889 112.941 1.00 29.88 ?  350 ARG A N     1 
ATOM   2832  C  CA    . ARG A 1 350 ? 142.783 126.234 111.735 1.00 24.31 ?  350 ARG A CA    1 
ATOM   2833  C  C     . ARG A 1 350 ? 142.228 124.996 111.044 1.00 30.19 ?  350 ARG A C     1 
ATOM   2834  O  O     . ARG A 1 350 ? 141.141 125.048 110.460 1.00 34.35 ?  350 ARG A O     1 
ATOM   2835  C  CB    . ARG A 1 350 ? 143.673 127.029 110.781 1.00 26.02 ?  350 ARG A CB    1 
ATOM   2836  C  CG    . ARG A 1 350 ? 143.905 128.467 111.217 1.00 24.05 ?  350 ARG A CG    1 
ATOM   2837  C  CD    . ARG A 1 350 ? 145.039 129.107 110.439 1.00 23.05 ?  350 ARG A CD    1 
ATOM   2838  N  NE    . ARG A 1 350 ? 144.691 129.284 109.036 1.00 34.27 ?  350 ARG A NE    1 
ATOM   2839  C  CZ    . ARG A 1 350 ? 143.902 130.245 108.572 1.00 31.39 ?  350 ARG A CZ    1 
ATOM   2840  N  NH1   . ARG A 1 350 ? 143.370 131.153 109.375 1.00 24.59 1  350 ARG A NH1   1 
ATOM   2841  N  NH2   . ARG A 1 350 ? 143.638 130.294 107.270 1.00 28.80 ?  350 ARG A NH2   1 
ATOM   2842  N  N     . SER A 1 351 ? 142.960 123.881 111.088 1.00 33.50 ?  351 SER A N     1 
ATOM   2843  C  CA    . SER A 1 351 ? 142.430 122.635 110.547 1.00 30.16 ?  351 SER A CA    1 
ATOM   2844  C  C     . SER A 1 351 ? 141.217 122.162 111.339 1.00 31.45 ?  351 SER A C     1 
ATOM   2845  O  O     . SER A 1 351 ? 140.223 121.712 110.757 1.00 38.80 ?  351 SER A O     1 
ATOM   2846  C  CB    . SER A 1 351 ? 143.518 121.562 110.541 1.00 30.96 ?  351 SER A CB    1 
ATOM   2847  O  OG    . SER A 1 351 ? 144.466 121.802 109.516 1.00 39.77 ?  351 SER A OG    1 
ATOM   2848  N  N     . GLU A 1 352 ? 141.278 122.258 112.669 1.00 29.70 ?  352 GLU A N     1 
ATOM   2849  C  CA    . GLU A 1 352 ? 140.173 121.777 113.495 1.00 30.98 ?  352 GLU A CA    1 
ATOM   2850  C  C     . GLU A 1 352 ? 138.939 122.665 113.363 1.00 34.19 ?  352 GLU A C     1 
ATOM   2851  O  O     . GLU A 1 352 ? 137.822 122.164 113.189 1.00 39.10 ?  352 GLU A O     1 
ATOM   2852  C  CB    . GLU A 1 352 ? 140.603 121.677 114.960 1.00 33.49 ?  352 GLU A CB    1 
ATOM   2853  C  CG    . GLU A 1 352 ? 141.854 120.854 115.202 1.00 33.65 ?  352 GLU A CG    1 
ATOM   2854  C  CD    . GLU A 1 352 ? 142.359 120.967 116.627 1.00 42.38 ?  352 GLU A CD    1 
ATOM   2855  O  OE1   . GLU A 1 352 ? 143.088 120.058 117.076 1.00 41.46 ?  352 GLU A OE1   1 
ATOM   2856  O  OE2   . GLU A 1 352 ? 142.026 121.966 117.299 1.00 41.70 -1 352 GLU A OE2   1 
ATOM   2857  N  N     . SER A 1 353 ? 139.114 123.986 113.445 1.00 34.69 ?  353 SER A N     1 
ATOM   2858  C  CA    . SER A 1 353 ? 137.978 124.892 113.549 1.00 34.74 ?  353 SER A CA    1 
ATOM   2859  C  C     . SER A 1 353 ? 138.031 126.095 112.618 1.00 30.47 ?  353 SER A C     1 
ATOM   2860  O  O     . SER A 1 353 ? 137.084 126.888 112.615 1.00 31.06 ?  353 SER A O     1 
ATOM   2861  C  CB    . SER A 1 353 ? 137.835 125.394 114.994 1.00 34.34 ?  353 SER A CB    1 
ATOM   2862  O  OG    . SER A 1 353 ? 138.962 126.161 115.382 1.00 32.37 ?  353 SER A OG    1 
ATOM   2863  N  N     . GLY A 1 354 ? 139.094 126.263 111.837 1.00 27.70 ?  354 GLY A N     1 
ATOM   2864  C  CA    . GLY A 1 354 ? 139.219 127.426 110.984 1.00 27.40 ?  354 GLY A CA    1 
ATOM   2865  C  C     . GLY A 1 354 ? 139.731 128.668 111.673 1.00 21.81 ?  354 GLY A C     1 
ATOM   2866  O  O     . GLY A 1 354 ? 139.872 129.707 111.016 1.00 25.58 ?  354 GLY A O     1 
ATOM   2867  N  N     . TYR A 1 355 ? 140.017 128.598 112.967 1.00 22.77 ?  355 TYR A N     1 
ATOM   2868  C  CA    . TYR A 1 355 ? 140.519 129.699 113.764 1.00 17.75 ?  355 TYR A CA    1 
ATOM   2869  C  C     . TYR A 1 355 ? 141.990 129.479 114.102 1.00 22.19 ?  355 TYR A C     1 
ATOM   2870  O  O     . TYR A 1 355 ? 142.449 128.336 114.168 1.00 28.86 ?  355 TYR A O     1 
ATOM   2871  C  CB    . TYR A 1 355 ? 139.715 129.845 115.061 1.00 23.82 ?  355 TYR A CB    1 
ATOM   2872  C  CG    . TYR A 1 355 ? 138.308 130.354 114.854 1.00 26.78 ?  355 TYR A CG    1 
ATOM   2873  C  CD1   . TYR A 1 355 ? 138.074 131.561 114.212 1.00 20.43 ?  355 TYR A CD1   1 
ATOM   2874  C  CD2   . TYR A 1 355 ? 137.214 129.625 115.300 1.00 25.91 ?  355 TYR A CD2   1 
ATOM   2875  C  CE1   . TYR A 1 355 ? 136.791 132.028 114.020 1.00 27.50 ?  355 TYR A CE1   1 
ATOM   2876  C  CE2   . TYR A 1 355 ? 135.926 130.085 115.113 1.00 26.03 ?  355 TYR A CE2   1 
ATOM   2877  C  CZ    . TYR A 1 355 ? 135.721 131.286 114.473 1.00 30.59 ?  355 TYR A CZ    1 
ATOM   2878  O  OH    . TYR A 1 355 ? 134.439 131.750 114.284 1.00 31.21 ?  355 TYR A OH    1 
ATOM   2879  N  N     . PRO A 1 356 ? 142.759 130.548 114.329 1.00 22.84 ?  356 PRO A N     1 
ATOM   2880  C  CA    . PRO A 1 356 ? 142.384 131.967 114.310 1.00 17.73 ?  356 PRO A CA    1 
ATOM   2881  C  C     . PRO A 1 356 ? 142.498 132.609 112.937 1.00 15.52 ?  356 PRO A C     1 
ATOM   2882  O  O     . PRO A 1 356 ? 143.086 132.041 112.022 1.00 19.50 ?  356 PRO A O     1 
ATOM   2883  C  CB    . PRO A 1 356 ? 143.390 132.580 115.285 1.00 18.27 ?  356 PRO A CB    1 
ATOM   2884  C  CG    . PRO A 1 356 ? 144.633 131.780 115.032 1.00 17.73 ?  356 PRO A CG    1 
ATOM   2885  C  CD    . PRO A 1 356 ? 144.162 130.372 114.745 1.00 13.52 ?  356 PRO A CD    1 
ATOM   2886  N  N     . TYR A 1 357 ? 141.936 133.802 112.766 1.00 18.54 ?  357 TYR A N     1 
ATOM   2887  C  CA    . TYR A 1 357 ? 142.294 134.623 111.622 1.00 11.30 ?  357 TYR A CA    1 
ATOM   2888  C  C     . TYR A 1 357 ? 143.745 135.065 111.752 1.00 16.15 ?  357 TYR A C     1 
ATOM   2889  O  O     . TYR A 1 357 ? 144.248 135.307 112.853 1.00 25.34 ?  357 TYR A O     1 
ATOM   2890  C  CB    . TYR A 1 357 ? 141.384 135.848 111.517 1.00 15.07 ?  357 TYR A CB    1 
ATOM   2891  C  CG    . TYR A 1 357 ? 139.912 135.588 111.755 1.00 18.99 ?  357 TYR A CG    1 
ATOM   2892  C  CD1   . TYR A 1 357 ? 139.317 134.407 111.340 1.00 14.29 ?  357 TYR A CD1   1 
ATOM   2893  C  CD2   . TYR A 1 357 ? 139.117 136.529 112.392 1.00 18.46 ?  357 TYR A CD2   1 
ATOM   2894  C  CE1   . TYR A 1 357 ? 137.978 134.168 111.549 1.00 14.64 ?  357 TYR A CE1   1 
ATOM   2895  C  CE2   . TYR A 1 357 ? 137.774 136.299 112.610 1.00 17.60 ?  357 TYR A CE2   1 
ATOM   2896  C  CZ    . TYR A 1 357 ? 137.210 135.116 112.186 1.00 21.97 ?  357 TYR A CZ    1 
ATOM   2897  O  OH    . TYR A 1 357 ? 135.872 134.878 112.396 1.00 26.52 ?  357 TYR A OH    1 
ATOM   2898  N  N     . ILE A 1 358 ? 144.427 135.161 110.617 1.00 14.85 ?  358 ILE A N     1 
ATOM   2899  C  CA    . ILE A 1 358 ? 145.836 135.528 110.576 1.00 13.71 ?  358 ILE A CA    1 
ATOM   2900  C  C     . ILE A 1 358 ? 145.953 136.925 109.990 1.00 16.73 ?  358 ILE A C     1 
ATOM   2901  O  O     . ILE A 1 358 ? 145.482 137.178 108.874 1.00 25.12 ?  358 ILE A O     1 
ATOM   2902  C  CB    . ILE A 1 358 ? 146.662 134.520 109.760 1.00 18.73 ?  358 ILE A CB    1 
ATOM   2903  C  CG1   . ILE A 1 358 ? 146.387 133.091 110.234 1.00 21.88 ?  358 ILE A CG1   1 
ATOM   2904  C  CG2   . ILE A 1 358 ? 148.142 134.844 109.860 1.00 17.24 ?  358 ILE A CG2   1 
ATOM   2905  C  CD1   . ILE A 1 358 ? 146.852 132.814 111.643 1.00 18.48 ?  358 ILE A CD1   1 
ATOM   2906  N  N     . MET A 1 359 ? 146.575 137.830 110.739 1.00 10.67 ?  359 MET A N     1 
ATOM   2907  C  CA    . MET A 1 359 ? 146.889 139.168 110.257 1.00 8.82  ?  359 MET A CA    1 
ATOM   2908  C  C     . MET A 1 359 ? 148.402 139.306 110.188 1.00 10.43 ?  359 MET A C     1 
ATOM   2909  O  O     . MET A 1 359 ? 149.085 139.210 111.213 1.00 21.36 ?  359 MET A O     1 
ATOM   2910  C  CB    . MET A 1 359 ? 146.295 140.246 111.162 1.00 11.87 ?  359 MET A CB    1 
ATOM   2911  C  CG    . MET A 1 359 ? 145.691 141.411 110.399 1.00 12.10 ?  359 MET A CG    1 
ATOM   2912  S  SD    . MET A 1 359 ? 145.722 142.987 111.268 1.00 33.65 ?  359 MET A SD    1 
ATOM   2913  C  CE    . MET A 1 359 ? 147.466 143.372 111.235 1.00 12.22 ?  359 MET A CE    1 
ATOM   2914  N  N     . PHE A 1 360 ? 148.920 139.523 108.984 1.00 10.78 ?  360 PHE A N     1 
ATOM   2915  C  CA    . PHE A 1 360 ? 150.344 139.773 108.786 1.00 11.58 ?  360 PHE A CA    1 
ATOM   2916  C  C     . PHE A 1 360 ? 150.562 141.273 108.940 1.00 15.89 ?  360 PHE A C     1 
ATOM   2917  O  O     . PHE A 1 360 ? 150.323 142.045 108.010 1.00 25.75 ?  360 PHE A O     1 
ATOM   2918  C  CB    . PHE A 1 360 ? 150.795 139.255 107.426 1.00 9.13  ?  360 PHE A CB    1 
ATOM   2919  C  CG    . PHE A 1 360 ? 150.671 137.765 107.285 1.00 17.71 ?  360 PHE A CG    1 
ATOM   2920  C  CD1   . PHE A 1 360 ? 151.338 136.919 108.153 1.00 16.06 ?  360 PHE A CD1   1 
ATOM   2921  C  CD2   . PHE A 1 360 ? 149.879 137.210 106.294 1.00 13.68 ?  360 PHE A CD2   1 
ATOM   2922  C  CE1   . PHE A 1 360 ? 151.224 135.548 108.033 1.00 11.57 ?  360 PHE A CE1   1 
ATOM   2923  C  CE2   . PHE A 1 360 ? 149.762 135.843 106.169 1.00 17.28 ?  360 PHE A CE2   1 
ATOM   2924  C  CZ    . PHE A 1 360 ? 150.435 135.010 107.039 1.00 15.05 ?  360 PHE A CZ    1 
ATOM   2925  N  N     . GLN A 1 361 ? 151.017 141.678 110.128 1.00 11.68 ?  361 GLN A N     1 
ATOM   2926  C  CA    . GLN A 1 361 ? 151.038 143.092 110.493 1.00 11.92 ?  361 GLN A CA    1 
ATOM   2927  C  C     . GLN A 1 361 ? 151.884 143.911 109.527 1.00 15.94 ?  361 GLN A C     1 
ATOM   2928  O  O     . GLN A 1 361 ? 151.469 144.987 109.079 1.00 20.44 ?  361 GLN A O     1 
ATOM   2929  C  CB    . GLN A 1 361 ? 151.559 143.248 111.922 1.00 23.22 ?  361 GLN A CB    1 
ATOM   2930  C  CG    . GLN A 1 361 ? 151.320 144.620 112.521 1.00 17.97 ?  361 GLN A CG    1 
ATOM   2931  C  CD    . GLN A 1 361 ? 150.974 144.560 113.992 1.00 20.29 ?  361 GLN A CD    1 
ATOM   2932  O  OE1   . GLN A 1 361 ? 151.445 143.686 114.716 1.00 24.15 ?  361 GLN A OE1   1 
ATOM   2933  N  NE2   . GLN A 1 361 ? 150.150 145.497 114.442 1.00 23.91 ?  361 GLN A NE2   1 
ATOM   2934  N  N     . ASP A 1 362 ? 153.080 143.422 109.198 1.00 18.11 ?  362 ASP A N     1 
ATOM   2935  C  CA    . ASP A 1 362 ? 153.963 144.192 108.332 1.00 17.14 ?  362 ASP A CA    1 
ATOM   2936  C  C     . ASP A 1 362 ? 153.470 144.210 106.892 1.00 18.27 ?  362 ASP A C     1 
ATOM   2937  O  O     . ASP A 1 362 ? 153.673 145.204 106.189 1.00 19.69 ?  362 ASP A O     1 
ATOM   2938  C  CB    . ASP A 1 362 ? 155.385 143.647 108.412 1.00 18.97 ?  362 ASP A CB    1 
ATOM   2939  C  CG    . ASP A 1 362 ? 155.942 143.694 109.819 1.00 30.49 ?  362 ASP A CG    1 
ATOM   2940  O  OD1   . ASP A 1 362 ? 155.244 143.245 110.752 1.00 27.74 ?  362 ASP A OD1   1 
ATOM   2941  O  OD2   . ASP A 1 362 ? 157.078 144.182 109.993 1.00 34.52 -1 362 ASP A OD2   1 
ATOM   2942  N  N     . ASN A 1 363 ? 152.809 143.142 106.443 1.00 18.08 ?  363 ASN A N     1 
ATOM   2943  C  CA    . ASN A 1 363 ? 152.197 143.163 105.119 1.00 10.98 ?  363 ASN A CA    1 
ATOM   2944  C  C     . ASN A 1 363 ? 151.121 144.237 105.032 1.00 13.44 ?  363 ASN A C     1 
ATOM   2945  O  O     . ASN A 1 363 ? 150.961 144.888 103.993 1.00 21.41 ?  363 ASN A O     1 
ATOM   2946  C  CB    . ASN A 1 363 ? 151.616 141.791 104.784 1.00 11.67 ?  363 ASN A CB    1 
ATOM   2947  C  CG    . ASN A 1 363 ? 152.670 140.813 104.309 1.00 18.13 ?  363 ASN A CG    1 
ATOM   2948  O  OD1   . ASN A 1 363 ? 153.807 141.192 104.037 1.00 19.36 ?  363 ASN A OD1   1 
ATOM   2949  N  ND2   . ASN A 1 363 ? 152.294 139.545 104.206 1.00 18.77 ?  363 ASN A ND2   1 
ATOM   2950  N  N     . VAL A 1 364 ? 150.367 144.432 106.114 1.00 9.09  ?  364 VAL A N     1 
ATOM   2951  C  CA    . VAL A 1 364 ? 149.357 145.485 106.139 1.00 10.59 ?  364 VAL A CA    1 
ATOM   2952  C  C     . VAL A 1 364 ? 150.015 146.858 106.189 1.00 17.38 ?  364 VAL A C     1 
ATOM   2953  O  O     . VAL A 1 364 ? 149.618 147.783 105.471 1.00 16.12 ?  364 VAL A O     1 
ATOM   2954  C  CB    . VAL A 1 364 ? 148.401 145.283 107.329 1.00 1.48  ?  364 VAL A CB    1 
ATOM   2955  C  CG1   . VAL A 1 364 ? 147.303 146.329 107.304 1.00 4.43  ?  364 VAL A CG1   1 
ATOM   2956  C  CG2   . VAL A 1 364 ? 147.817 143.885 107.315 1.00 8.10  ?  364 VAL A CG2   1 
ATOM   2957  N  N     . ASN A 1 365 ? 151.034 147.012 107.034 1.00 21.00 ?  365 ASN A N     1 
ATOM   2958  C  CA    . ASN A 1 365 ? 151.559 148.329 107.366 1.00 11.91 ?  365 ASN A CA    1 
ATOM   2959  C  C     . ASN A 1 365 ? 152.642 148.826 106.415 1.00 15.26 ?  365 ASN A C     1 
ATOM   2960  O  O     . ASN A 1 365 ? 152.971 150.016 106.458 1.00 21.76 ?  365 ASN A O     1 
ATOM   2961  C  CB    . ASN A 1 365 ? 152.099 148.327 108.799 1.00 13.85 ?  365 ASN A CB    1 
ATOM   2962  C  CG    . ASN A 1 365 ? 150.993 148.319 109.832 1.00 15.71 ?  365 ASN A CG    1 
ATOM   2963  O  OD1   . ASN A 1 365 ? 150.112 149.177 109.821 1.00 12.41 ?  365 ASN A OD1   1 
ATOM   2964  N  ND2   . ASN A 1 365 ? 151.029 147.342 110.729 1.00 18.99 ?  365 ASN A ND2   1 
ATOM   2965  N  N     . LYS A 1 366 ? 153.200 147.968 105.562 1.00 19.00 ?  366 LYS A N     1 
ATOM   2966  C  CA    . LYS A 1 366 ? 154.158 148.434 104.571 1.00 15.84 ?  366 LYS A CA    1 
ATOM   2967  C  C     . LYS A 1 366 ? 153.486 149.132 103.399 1.00 19.99 ?  366 LYS A C     1 
ATOM   2968  O  O     . LYS A 1 366 ? 154.164 149.837 102.643 1.00 29.30 ?  366 LYS A O     1 
ATOM   2969  C  CB    . LYS A 1 366 ? 155.007 147.265 104.066 1.00 13.23 ?  366 LYS A CB    1 
ATOM   2970  C  CG    . LYS A 1 366 ? 154.359 146.442 102.970 1.00 19.82 ?  366 LYS A CG    1 
ATOM   2971  C  CD    . LYS A 1 366 ? 154.899 145.021 102.965 1.00 23.35 ?  366 LYS A CD    1 
ATOM   2972  C  CE    . LYS A 1 366 ? 154.155 144.146 101.969 1.00 26.32 ?  366 LYS A CE    1 
ATOM   2973  N  NZ    . LYS A 1 366 ? 152.697 144.444 101.938 1.00 25.54 1  366 LYS A NZ    1 
ATOM   2974  N  N     . VAL A 1 367 ? 152.177 148.953 103.237 1.00 25.26 ?  367 VAL A N     1 
ATOM   2975  C  CA    . VAL A 1 367 ? 151.389 149.666 102.243 1.00 15.02 ?  367 VAL A CA    1 
ATOM   2976  C  C     . VAL A 1 367 ? 150.297 150.510 102.874 1.00 14.05 ?  367 VAL A C     1 
ATOM   2977  O  O     . VAL A 1 367 ? 149.498 151.112 102.151 1.00 18.32 ?  367 VAL A O     1 
ATOM   2978  C  CB    . VAL A 1 367 ? 150.783 148.695 101.209 1.00 13.12 ?  367 VAL A CB    1 
ATOM   2979  C  CG1   . VAL A 1 367 ? 151.842 148.263 100.209 1.00 17.27 ?  367 VAL A CG1   1 
ATOM   2980  C  CG2   . VAL A 1 367 ? 150.194 147.488 101.911 1.00 4.98  ?  367 VAL A CG2   1 
ATOM   2981  N  N     . HIS A 1 368 ? 150.239 150.572 104.202 1.00 14.46 ?  368 HIS A N     1 
ATOM   2982  C  CA    . HIS A 1 368 ? 149.245 151.387 104.885 1.00 6.03  ?  368 HIS A CA    1 
ATOM   2983  C  C     . HIS A 1 368 ? 149.523 152.864 104.639 1.00 15.52 ?  368 HIS A C     1 
ATOM   2984  O  O     . HIS A 1 368 ? 150.644 153.339 104.836 1.00 25.03 ?  368 HIS A O     1 
ATOM   2985  C  CB    . HIS A 1 368 ? 149.260 151.084 106.381 1.00 12.53 ?  368 HIS A CB    1 
ATOM   2986  C  CG    . HIS A 1 368 ? 148.137 151.718 107.140 1.00 8.17  ?  368 HIS A CG    1 
ATOM   2987  N  ND1   . HIS A 1 368 ? 148.291 152.214 108.416 1.00 13.52 ?  368 HIS A ND1   1 
ATOM   2988  C  CD2   . HIS A 1 368 ? 146.844 151.935 106.805 1.00 10.74 ?  368 HIS A CD2   1 
ATOM   2989  C  CE1   . HIS A 1 368 ? 147.141 152.709 108.834 1.00 15.09 ?  368 HIS A CE1   1 
ATOM   2990  N  NE2   . HIS A 1 368 ? 146.246 152.552 107.876 1.00 7.25  ?  368 HIS A NE2   1 
ATOM   2991  N  N     . ALA A 1 369 ? 148.492 153.592 104.208 1.00 18.25 ?  369 ALA A N     1 
ATOM   2992  C  CA    . ALA A 1 369 ? 148.657 155.000 103.880 1.00 12.50 ?  369 ALA A CA    1 
ATOM   2993  C  C     . ALA A 1 369 ? 148.574 155.910 105.096 1.00 17.79 ?  369 ALA A C     1 
ATOM   2994  O  O     . ALA A 1 369 ? 149.003 157.065 105.015 1.00 25.01 ?  369 ALA A O     1 
ATOM   2995  C  CB    . ALA A 1 369 ? 147.605 155.423 102.855 1.00 8.96  ?  369 ALA A CB    1 
ATOM   2996  N  N     . ASN A 1 370 ? 148.049 155.423 106.216 1.00 17.23 ?  370 ASN A N     1 
ATOM   2997  C  CA    . ASN A 1 370 ? 147.807 156.244 107.394 1.00 12.34 ?  370 ASN A CA    1 
ATOM   2998  C  C     . ASN A 1 370 ? 148.574 155.720 108.601 1.00 12.14 ?  370 ASN A C     1 
ATOM   2999  O  O     . ASN A 1 370 ? 148.042 155.638 109.709 1.00 21.21 ?  370 ASN A O     1 
ATOM   3000  C  CB    . ASN A 1 370 ? 146.314 156.324 107.699 1.00 12.21 ?  370 ASN A CB    1 
ATOM   3001  C  CG    . ASN A 1 370 ? 145.516 156.878 106.539 1.00 10.47 ?  370 ASN A CG    1 
ATOM   3002  O  OD1   . ASN A 1 370 ? 145.744 158.003 106.097 1.00 26.58 ?  370 ASN A OD1   1 
ATOM   3003  N  ND2   . ASN A 1 370 ? 144.577 156.090 106.036 1.00 12.40 ?  370 ASN A ND2   1 
ATOM   3004  N  N     . ASN A 1 371 ? 149.842 155.357 108.398 1.00 14.37 ?  371 ASN A N     1 
ATOM   3005  C  CA    . ASN A 1 371 ? 150.679 154.931 109.513 1.00 11.15 ?  371 ASN A CA    1 
ATOM   3006  C  C     . ASN A 1 371 ? 150.975 156.068 110.480 1.00 16.52 ?  371 ASN A C     1 
ATOM   3007  O  O     . ASN A 1 371 ? 151.262 155.808 111.652 1.00 19.08 ?  371 ASN A O     1 
ATOM   3008  C  CB    . ASN A 1 371 ? 151.987 154.335 108.996 1.00 8.50  ?  371 ASN A CB    1 
ATOM   3009  C  CG    . ASN A 1 371 ? 151.860 152.867 108.652 1.00 16.56 ?  371 ASN A CG    1 
ATOM   3010  O  OD1   . ASN A 1 371 ? 150.988 152.171 109.169 1.00 20.95 ?  371 ASN A OD1   1 
ATOM   3011  N  ND2   . ASN A 1 371 ? 152.731 152.387 107.774 1.00 18.37 ?  371 ASN A ND2   1 
ATOM   3012  N  N     . HIS A 1 372 ? 150.921 157.318 110.012 1.00 19.53 ?  372 HIS A N     1 
ATOM   3013  C  CA    . HIS A 1 372 ? 151.127 158.453 110.906 1.00 15.92 ?  372 HIS A CA    1 
ATOM   3014  C  C     . HIS A 1 372 ? 150.036 158.525 111.966 1.00 16.49 ?  372 HIS A C     1 
ATOM   3015  O  O     . HIS A 1 372 ? 150.316 158.808 113.137 1.00 25.78 ?  372 HIS A O     1 
ATOM   3016  C  CB    . HIS A 1 372 ? 151.182 159.750 110.099 1.00 18.05 ?  372 HIS A CB    1 
ATOM   3017  C  CG    . HIS A 1 372 ? 149.885 160.106 109.442 1.00 18.35 ?  372 HIS A CG    1 
ATOM   3018  N  ND1   . HIS A 1 372 ? 149.290 159.309 108.488 1.00 23.68 ?  372 HIS A ND1   1 
ATOM   3019  C  CD2   . HIS A 1 372 ? 149.063 161.168 109.609 1.00 18.43 ?  372 HIS A CD2   1 
ATOM   3020  C  CE1   . HIS A 1 372 ? 148.159 159.866 108.095 1.00 17.06 ?  372 HIS A CE1   1 
ATOM   3021  N  NE2   . HIS A 1 372 ? 148.000 160.997 108.757 1.00 17.38 ?  372 HIS A NE2   1 
ATOM   3022  N  N     . ILE A 1 373 ? 148.783 158.286 111.573 1.00 16.32 ?  373 ILE A N     1 
ATOM   3023  C  CA    . ILE A 1 373 ? 147.697 158.233 112.546 1.00 18.68 ?  373 ILE A CA    1 
ATOM   3024  C  C     . ILE A 1 373 ? 147.910 157.071 113.504 1.00 15.16 ?  373 ILE A C     1 
ATOM   3025  O  O     . ILE A 1 373 ? 147.893 157.236 114.730 1.00 28.13 ?  373 ILE A O     1 
ATOM   3026  C  CB    . ILE A 1 373 ? 146.339 158.120 111.829 1.00 19.22 ?  373 ILE A CB    1 
ATOM   3027  C  CG1   . ILE A 1 373 ? 146.124 159.310 110.897 1.00 15.45 ?  373 ILE A CG1   1 
ATOM   3028  C  CG2   . ILE A 1 373 ? 145.207 158.009 112.838 1.00 19.60 ?  373 ILE A CG2   1 
ATOM   3029  C  CD1   . ILE A 1 373 ? 144.973 159.130 109.939 1.00 15.20 ?  373 ILE A CD1   1 
ATOM   3030  N  N     . SER A 1 374 ? 148.142 155.882 112.950 1.00 16.92 ?  374 SER A N     1 
ATOM   3031  C  CA    . SER A 1 374 ? 148.375 154.667 113.715 1.00 12.66 ?  374 SER A CA    1 
ATOM   3032  C  C     . SER A 1 374 ? 148.708 153.531 112.760 1.00 14.27 ?  374 SER A C     1 
ATOM   3033  O  O     . SER A 1 374 ? 148.309 153.562 111.592 1.00 21.20 ?  374 SER A O     1 
ATOM   3034  C  CB    . SER A 1 374 ? 147.152 154.305 114.557 1.00 19.05 ?  374 SER A CB    1 
ATOM   3035  O  OG    . SER A 1 374 ? 147.464 153.295 115.497 1.00 24.05 ?  374 SER A OG    1 
ATOM   3036  N  N     . LYS A 1 375 ? 149.436 152.530 113.235 1.00 22.39 ?  375 LYS A N     1 
ATOM   3037  C  CA    . LYS A 1 375 ? 149.599 151.315 112.457 1.00 19.34 ?  375 LYS A CA    1 
ATOM   3038  C  C     . LYS A 1 375 ? 148.404 150.399 112.676 1.00 15.28 ?  375 LYS A C     1 
ATOM   3039  O  O     . LYS A 1 375 ? 147.793 150.387 113.748 1.00 22.44 ?  375 LYS A O     1 
ATOM   3040  C  CB    . LYS A 1 375 ? 150.897 150.599 112.831 1.00 12.06 ?  375 LYS A CB    1 
ATOM   3041  C  CG    . LYS A 1 375 ? 152.137 151.247 112.240 1.00 16.85 ?  375 LYS A CG    1 
ATOM   3042  C  CD    . LYS A 1 375 ? 153.314 150.292 112.228 1.00 24.65 ?  375 LYS A CD    1 
ATOM   3043  C  CE    . LYS A 1 375 ? 154.489 150.888 111.474 1.00 24.19 ?  375 LYS A CE    1 
ATOM   3044  N  NZ    . LYS A 1 375 ? 155.596 149.910 111.303 1.00 29.43 1  375 LYS A NZ    1 
ATOM   3045  N  N     . VAL A 1 376 ? 148.057 149.642 111.639 1.00 15.10 ?  376 VAL A N     1 
ATOM   3046  C  CA    . VAL A 1 376 ? 146.937 148.712 111.726 1.00 15.74 ?  376 VAL A CA    1 
ATOM   3047  C  C     . VAL A 1 376 ? 147.337 147.582 112.670 1.00 13.96 ?  376 VAL A C     1 
ATOM   3048  O  O     . VAL A 1 376 ? 148.229 146.788 112.359 1.00 20.44 ?  376 VAL A O     1 
ATOM   3049  C  CB    . VAL A 1 376 ? 146.538 148.177 110.348 1.00 10.94 ?  376 VAL A CB    1 
ATOM   3050  C  CG1   . VAL A 1 376 ? 145.327 147.272 110.463 1.00 8.26  ?  376 VAL A CG1   1 
ATOM   3051  C  CG2   . VAL A 1 376 ? 146.264 149.328 109.395 1.00 3.91  ?  376 VAL A CG2   1 
ATOM   3052  N  N     . LYS A 1 377 ? 146.683 147.511 113.828 1.00 12.77 ?  377 LYS A N     1 
ATOM   3053  C  CA    . LYS A 1 377 ? 147.029 146.529 114.844 1.00 11.43 ?  377 LYS A CA    1 
ATOM   3054  C  C     . LYS A 1 377 ? 146.162 145.281 114.800 1.00 10.48 ?  377 LYS A C     1 
ATOM   3055  O  O     . LYS A 1 377 ? 146.576 144.246 115.327 1.00 24.90 ?  377 LYS A O     1 
ATOM   3056  C  CB    . LYS A 1 377 ? 146.927 147.145 116.242 1.00 15.92 ?  377 LYS A CB    1 
ATOM   3057  C  CG    . LYS A 1 377 ? 147.700 148.432 116.422 1.00 12.28 ?  377 LYS A CG    1 
ATOM   3058  C  CD    . LYS A 1 377 ? 147.010 149.313 117.442 1.00 21.26 ?  377 LYS A CD    1 
ATOM   3059  C  CE    . LYS A 1 377 ? 147.447 150.754 117.318 1.00 23.69 ?  377 LYS A CE    1 
ATOM   3060  N  NZ    . LYS A 1 377 ? 146.470 151.679 117.954 1.00 26.00 1  377 LYS A NZ    1 
ATOM   3061  N  N     . PHE A 1 378 ? 144.977 145.355 114.201 1.00 8.60  ?  378 PHE A N     1 
ATOM   3062  C  CA    . PHE A 1 378 ? 144.069 144.218 114.167 1.00 7.85  ?  378 PHE A CA    1 
ATOM   3063  C  C     . PHE A 1 378 ? 143.055 144.438 113.055 1.00 8.00  ?  378 PHE A C     1 
ATOM   3064  O  O     . PHE A 1 378 ? 143.005 145.500 112.431 1.00 15.64 ?  378 PHE A O     1 
ATOM   3065  C  CB    . PHE A 1 378 ? 143.385 144.005 115.524 1.00 6.52  ?  378 PHE A CB    1 
ATOM   3066  C  CG    . PHE A 1 378 ? 142.369 145.057 115.878 1.00 8.31  ?  378 PHE A CG    1 
ATOM   3067  C  CD1   . PHE A 1 378 ? 142.733 146.389 115.990 1.00 9.59  ?  378 PHE A CD1   1 
ATOM   3068  C  CD2   . PHE A 1 378 ? 141.054 144.707 116.123 1.00 5.15  ?  378 PHE A CD2   1 
ATOM   3069  C  CE1   . PHE A 1 378 ? 141.804 147.350 116.322 1.00 4.02  ?  378 PHE A CE1   1 
ATOM   3070  C  CE2   . PHE A 1 378 ? 140.120 145.665 116.455 1.00 9.56  ?  378 PHE A CE2   1 
ATOM   3071  C  CZ    . PHE A 1 378 ? 140.497 146.987 116.556 1.00 11.53 ?  378 PHE A CZ    1 
ATOM   3072  N  N     . SER A 1 379 ? 142.249 143.412 112.811 1.00 3.31  ?  379 SER A N     1 
ATOM   3073  C  CA    . SER A 1 379 ? 141.264 143.409 111.739 1.00 4.14  ?  379 SER A CA    1 
ATOM   3074  C  C     . SER A 1 379 ? 139.866 143.230 112.330 1.00 5.96  ?  379 SER A C     1 
ATOM   3075  O  O     . SER A 1 379 ? 139.675 143.252 113.548 1.00 12.37 ?  379 SER A O     1 
ATOM   3076  C  CB    . SER A 1 379 ? 141.590 142.321 110.716 1.00 5.03  ?  379 SER A CB    1 
ATOM   3077  O  OG    . SER A 1 379 ? 141.059 142.647 109.445 1.00 8.38  ?  379 SER A OG    1 
ATOM   3078  N  N     . ASN A 1 380 ? 138.886 143.057 111.451 1.00 11.92 ?  380 ASN A N     1 
ATOM   3079  C  CA    . ASN A 1 380 ? 137.493 142.954 111.846 1.00 9.17  ?  380 ASN A CA    1 
ATOM   3080  C  C     . ASN A 1 380 ? 137.096 141.489 112.013 1.00 9.46  ?  380 ASN A C     1 
ATOM   3081  O  O     . ASN A 1 380 ? 137.929 140.581 111.968 1.00 9.92  ?  380 ASN A O     1 
ATOM   3082  C  CB    . ASN A 1 380 ? 136.602 143.666 110.827 1.00 2.71  ?  380 ASN A CB    1 
ATOM   3083  C  CG    . ASN A 1 380 ? 136.540 142.944 109.501 1.00 3.90  ?  380 ASN A CG    1 
ATOM   3084  O  OD1   . ASN A 1 380 ? 137.567 142.606 108.915 1.00 12.64 ?  380 ASN A OD1   1 
ATOM   3085  N  ND2   . ASN A 1 380 ? 135.329 142.701 109.018 1.00 10.73 ?  380 ASN A ND2   1 
ATOM   3086  N  N     . LEU A 1 381 ? 135.797 141.258 112.218 1.00 17.84 ?  381 LEU A N     1 
ATOM   3087  C  CA    . LEU A 1 381 ? 135.276 139.903 112.351 1.00 6.52  ?  381 LEU A CA    1 
ATOM   3088  C  C     . LEU A 1 381 ? 135.430 139.096 111.068 1.00 6.70  ?  381 LEU A C     1 
ATOM   3089  O  O     . LEU A 1 381 ? 135.538 137.867 111.133 1.00 15.30 ?  381 LEU A O     1 
ATOM   3090  C  CB    . LEU A 1 381 ? 133.806 139.964 112.773 1.00 11.71 ?  381 LEU A CB    1 
ATOM   3091  C  CG    . LEU A 1 381 ? 132.976 138.682 112.836 1.00 20.37 ?  381 LEU A CG    1 
ATOM   3092  C  CD1   . LEU A 1 381 ? 133.492 137.743 113.910 1.00 14.47 ?  381 LEU A CD1   1 
ATOM   3093  C  CD2   . LEU A 1 381 ? 131.515 139.019 113.071 1.00 15.89 ?  381 LEU A CD2   1 
ATOM   3094  N  N     . CYS A 1 382 ? 135.453 139.753 109.911 1.00 8.83  ?  382 CYS A N     1 
ATOM   3095  C  CA    . CYS A 1 382 ? 135.647 139.083 108.634 1.00 6.39  ?  382 CYS A CA    1 
ATOM   3096  C  C     . CYS A 1 382 ? 137.076 139.194 108.122 1.00 10.63 ?  382 CYS A C     1 
ATOM   3097  O  O     . CYS A 1 382 ? 137.370 138.692 107.032 1.00 17.01 ?  382 CYS A O     1 
ATOM   3098  C  CB    . CYS A 1 382 ? 134.675 139.643 107.592 1.00 15.57 ?  382 CYS A CB    1 
ATOM   3099  S  SG    . CYS A 1 382 ? 132.935 139.568 108.080 1.00 35.34 ?  382 CYS A SG    1 
ATOM   3100  N  N     . SER A 1 383 ? 137.965 139.836 108.883 1.00 11.05 ?  383 SER A N     1 
ATOM   3101  C  CA    . SER A 1 383 ? 139.393 139.916 108.566 1.00 8.94  ?  383 SER A CA    1 
ATOM   3102  C  C     . SER A 1 383 ? 139.642 140.553 107.199 1.00 12.51 ?  383 SER A C     1 
ATOM   3103  O  O     . SER A 1 383 ? 140.441 140.058 106.403 1.00 22.80 ?  383 SER A O     1 
ATOM   3104  C  CB    . SER A 1 383 ? 140.054 138.540 108.648 1.00 12.13 ?  383 SER A CB    1 
ATOM   3105  O  OG    . SER A 1 383 ? 139.738 137.757 107.513 1.00 20.92 ?  383 SER A OG    1 
ATOM   3106  N  N     . GLU A 1 384 ? 138.954 141.659 106.919 1.00 8.02  ?  384 GLU A N     1 
ATOM   3107  C  CA    . GLU A 1 384 ? 139.233 142.436 105.720 1.00 11.46 ?  384 GLU A CA    1 
ATOM   3108  C  C     . GLU A 1 384 ? 139.330 143.934 105.971 1.00 13.32 ?  384 GLU A C     1 
ATOM   3109  O  O     . GLU A 1 384 ? 139.839 144.651 105.103 1.00 22.51 ?  384 GLU A O     1 
ATOM   3110  C  CB    . GLU A 1 384 ? 138.176 142.163 104.636 1.00 6.55  ?  384 GLU A CB    1 
ATOM   3111  C  CG    . GLU A 1 384 ? 137.142 143.255 104.413 1.00 7.25  ?  384 GLU A CG    1 
ATOM   3112  C  CD    . GLU A 1 384 ? 136.008 143.206 105.411 1.00 16.76 ?  384 GLU A CD    1 
ATOM   3113  O  OE1   . GLU A 1 384 ? 135.849 142.166 106.079 1.00 19.97 ?  384 GLU A OE1   1 
ATOM   3114  O  OE2   . GLU A 1 384 ? 135.263 144.201 105.514 1.00 21.02 -1 384 GLU A OE2   1 
ATOM   3115  N  N     . VAL A 1 385 ? 138.885 144.424 107.122 1.00 13.29 ?  385 VAL A N     1 
ATOM   3116  C  CA    . VAL A 1 385 ? 139.015 145.835 107.467 1.00 3.12  ?  385 VAL A CA    1 
ATOM   3117  C  C     . VAL A 1 385 ? 140.365 146.039 108.137 1.00 15.14 ?  385 VAL A C     1 
ATOM   3118  O  O     . VAL A 1 385 ? 140.646 145.443 109.183 1.00 19.40 ?  385 VAL A O     1 
ATOM   3119  C  CB    . VAL A 1 385 ? 137.872 146.295 108.381 1.00 3.77  ?  385 VAL A CB    1 
ATOM   3120  C  CG1   . VAL A 1 385 ? 138.011 147.767 108.678 1.00 10.14 ?  385 VAL A CG1   1 
ATOM   3121  C  CG2   . VAL A 1 385 ? 136.535 146.011 107.738 1.00 8.54  ?  385 VAL A CG2   1 
ATOM   3122  N  N     . LEU A 1 386 ? 141.205 146.879 107.537 1.00 16.86 ?  386 LEU A N     1 
ATOM   3123  C  CA    . LEU A 1 386 ? 142.551 147.148 108.036 1.00 3.54  ?  386 LEU A CA    1 
ATOM   3124  C  C     . LEU A 1 386 ? 142.760 148.658 108.045 1.00 7.34  ?  386 LEU A C     1 
ATOM   3125  O  O     . LEU A 1 386 ? 143.096 149.252 107.018 1.00 8.00  ?  386 LEU A O     1 
ATOM   3126  C  CB    . LEU A 1 386 ? 143.599 146.444 107.185 1.00 3.17  ?  386 LEU A CB    1 
ATOM   3127  C  CG    . LEU A 1 386 ? 143.490 144.922 107.213 1.00 7.86  ?  386 LEU A CG    1 
ATOM   3128  C  CD1   . LEU A 1 386 ? 144.416 144.317 106.197 1.00 9.37  ?  386 LEU A CD1   1 
ATOM   3129  C  CD2   . LEU A 1 386 ? 143.798 144.397 108.602 1.00 6.77  ?  386 LEU A CD2   1 
ATOM   3130  N  N     . GLN A 1 387 ? 142.562 149.273 109.208 1.00 14.69 ?  387 GLN A N     1 
ATOM   3131  C  CA    . GLN A 1 387 ? 142.602 150.720 109.332 1.00 4.40  ?  387 GLN A CA    1 
ATOM   3132  C  C     . GLN A 1 387 ? 143.374 151.114 110.580 1.00 6.85  ?  387 GLN A C     1 
ATOM   3133  O  O     . GLN A 1 387 ? 143.556 150.320 111.505 1.00 18.95 ?  387 GLN A O     1 
ATOM   3134  C  CB    . GLN A 1 387 ? 141.192 151.319 109.382 1.00 6.31  ?  387 GLN A CB    1 
ATOM   3135  C  CG    . GLN A 1 387 ? 140.323 150.943 108.206 1.00 8.48  ?  387 GLN A CG    1 
ATOM   3136  C  CD    . GLN A 1 387 ? 139.035 151.721 108.175 1.00 6.84  ?  387 GLN A CD    1 
ATOM   3137  O  OE1   . GLN A 1 387 ? 138.850 152.666 108.937 1.00 19.59 ?  387 GLN A OE1   1 
ATOM   3138  N  NE2   . GLN A 1 387 ? 138.138 151.337 107.281 1.00 8.43  ?  387 GLN A NE2   1 
ATOM   3139  N  N     . ALA A 1 388 ? 143.841 152.358 110.585 1.00 10.17 ?  388 ALA A N     1 
ATOM   3140  C  CA    . ALA A 1 388 ? 144.482 152.915 111.765 1.00 9.47  ?  388 ALA A CA    1 
ATOM   3141  C  C     . ALA A 1 388 ? 143.459 153.115 112.876 1.00 14.32 ?  388 ALA A C     1 
ATOM   3142  O  O     . ALA A 1 388 ? 142.345 153.589 112.640 1.00 25.46 ?  388 ALA A O     1 
ATOM   3143  C  CB    . ALA A 1 388 ? 145.155 154.244 111.427 1.00 12.02 ?  388 ALA A CB    1 
ATOM   3144  N  N     . SER A 1 389 ? 143.841 152.741 114.094 1.00 17.96 ?  389 SER A N     1 
ATOM   3145  C  CA    . SER A 1 389 ? 142.979 152.905 115.254 1.00 8.83  ?  389 SER A CA    1 
ATOM   3146  C  C     . SER A 1 389 ? 143.797 153.437 116.418 1.00 13.12 ?  389 SER A C     1 
ATOM   3147  O  O     . SER A 1 389 ? 144.952 153.048 116.606 1.00 24.46 ?  389 SER A O     1 
ATOM   3148  C  CB    . SER A 1 389 ? 142.308 151.584 115.647 1.00 16.70 ?  389 SER A CB    1 
ATOM   3149  O  OG    . SER A 1 389 ? 143.227 150.508 115.593 1.00 21.83 ?  389 SER A OG    1 
ATOM   3150  N  N     . GLN A 1 390 ? 143.190 154.328 117.197 1.00 17.64 ?  390 GLN A N     1 
ATOM   3151  C  CA    . GLN A 1 390 ? 143.800 154.870 118.402 1.00 14.92 ?  390 GLN A CA    1 
ATOM   3152  C  C     . GLN A 1 390 ? 142.970 154.442 119.601 1.00 13.36 ?  390 GLN A C     1 
ATOM   3153  O  O     . GLN A 1 390 ? 141.746 154.598 119.600 1.00 17.32 ?  390 GLN A O     1 
ATOM   3154  C  CB    . GLN A 1 390 ? 143.903 156.395 118.336 1.00 10.33 ?  390 GLN A CB    1 
ATOM   3155  C  CG    . GLN A 1 390 ? 144.967 156.899 117.377 1.00 15.85 ?  390 GLN A CG    1 
ATOM   3156  C  CD    . GLN A 1 390 ? 144.850 158.384 117.102 1.00 25.93 ?  390 GLN A CD    1 
ATOM   3157  O  OE1   . GLN A 1 390 ? 143.894 159.032 117.527 1.00 24.72 ?  390 GLN A OE1   1 
ATOM   3158  N  NE2   . GLN A 1 390 ? 145.824 158.931 116.385 1.00 21.61 ?  390 GLN A NE2   1 
ATOM   3159  N  N     . VAL A 1 391 ? 143.638 153.898 120.619 1.00 24.05 ?  391 VAL A N     1 
ATOM   3160  C  CA    . VAL A 1 391 ? 142.933 153.422 121.800 1.00 20.62 ?  391 VAL A CA    1 
ATOM   3161  C  C     . VAL A 1 391 ? 142.358 154.604 122.572 1.00 22.62 ?  391 VAL A C     1 
ATOM   3162  O  O     . VAL A 1 391 ? 142.881 155.726 122.531 1.00 24.03 ?  391 VAL A O     1 
ATOM   3163  C  CB    . VAL A 1 391 ? 143.864 152.571 122.684 1.00 19.09 ?  391 VAL A CB    1 
ATOM   3164  C  CG1   . VAL A 1 391 ? 144.770 153.453 123.530 1.00 20.19 ?  391 VAL A CG1   1 
ATOM   3165  C  CG2   . VAL A 1 391 ? 143.053 151.627 123.559 1.00 17.61 ?  391 VAL A CG2   1 
ATOM   3166  N  N     . SER A 1 392 ? 141.252 154.356 123.264 1.00 27.56 ?  392 SER A N     1 
ATOM   3167  C  CA    . SER A 1 392 ? 140.603 155.362 124.088 1.00 19.89 ?  392 SER A CA    1 
ATOM   3168  C  C     . SER A 1 392 ? 140.900 155.101 125.558 1.00 29.15 ?  392 SER A C     1 
ATOM   3169  O  O     . SER A 1 392 ? 141.036 153.955 125.992 1.00 29.80 ?  392 SER A O     1 
ATOM   3170  C  CB    . SER A 1 392 ? 139.091 155.367 123.856 1.00 20.67 ?  392 SER A CB    1 
ATOM   3171  O  OG    . SER A 1 392 ? 138.782 155.601 122.495 1.00 27.89 ?  392 SER A OG    1 
ATOM   3172  N  N     . SER A 1 393 ? 141.007 156.182 126.322 1.00 31.70 ?  393 SER A N     1 
ATOM   3173  C  CA    . SER A 1 393 ? 141.239 156.115 127.762 1.00 28.10 ?  393 SER A CA    1 
ATOM   3174  C  C     . SER A 1 393 ? 139.916 156.434 128.450 1.00 30.16 ?  393 SER A C     1 
ATOM   3175  O  O     . SER A 1 393 ? 139.604 157.593 128.729 1.00 34.98 ?  393 SER A O     1 
ATOM   3176  C  CB    . SER A 1 393 ? 142.341 157.077 128.190 1.00 30.37 ?  393 SER A CB    1 
ATOM   3177  O  OG    . SER A 1 393 ? 143.619 156.569 127.848 1.00 36.82 ?  393 SER A OG    1 
ATOM   3178  N  N     . TYR A 1 394 ? 139.133 155.393 128.715 1.00 29.20 ?  394 TYR A N     1 
ATOM   3179  C  CA    . TYR A 1 394 ? 137.873 155.544 129.432 1.00 28.90 ?  394 TYR A CA    1 
ATOM   3180  C  C     . TYR A 1 394 ? 138.170 155.566 130.925 1.00 28.85 ?  394 TYR A C     1 
ATOM   3181  O  O     . TYR A 1 394 ? 138.514 154.537 131.513 1.00 33.55 ?  394 TYR A O     1 
ATOM   3182  C  CB    . TYR A 1 394 ? 136.913 154.416 129.069 1.00 24.98 ?  394 TYR A CB    1 
ATOM   3183  C  CG    . TYR A 1 394 ? 136.405 154.488 127.648 1.00 28.24 ?  394 TYR A CG    1 
ATOM   3184  C  CD1   . TYR A 1 394 ? 135.461 155.435 127.274 1.00 29.50 ?  394 TYR A CD1   1 
ATOM   3185  C  CD2   . TYR A 1 394 ? 136.875 153.613 126.677 1.00 26.55 ?  394 TYR A CD2   1 
ATOM   3186  C  CE1   . TYR A 1 394 ? 134.994 155.504 125.978 1.00 28.34 ?  394 TYR A CE1   1 
ATOM   3187  C  CE2   . TYR A 1 394 ? 136.413 153.674 125.378 1.00 27.08 ?  394 TYR A CE2   1 
ATOM   3188  C  CZ    . TYR A 1 394 ? 135.474 154.622 125.033 1.00 36.10 ?  394 TYR A CZ    1 
ATOM   3189  O  OH    . TYR A 1 394 ? 135.013 154.687 123.739 1.00 38.36 ?  394 TYR A OH    1 
ATOM   3190  N  N     . THR A 1 395 ? 138.041 156.737 131.537 1.00 35.82 ?  395 THR A N     1 
ATOM   3191  C  CA    . THR A 1 395 ? 138.403 156.932 132.931 1.00 37.45 ?  395 THR A CA    1 
ATOM   3192  C  C     . THR A 1 395 ? 137.227 156.562 133.834 1.00 38.54 ?  395 THR A C     1 
ATOM   3193  O  O     . THR A 1 395 ? 136.240 155.965 133.398 1.00 38.57 ?  395 THR A O     1 
ATOM   3194  C  CB    . THR A 1 395 ? 138.859 158.372 133.155 1.00 36.92 ?  395 THR A CB    1 
ATOM   3195  O  OG1   . THR A 1 395 ? 137.811 159.270 132.770 1.00 38.62 ?  395 THR A OG1   1 
ATOM   3196  C  CG2   . THR A 1 395 ? 140.100 158.669 132.330 1.00 35.25 ?  395 THR A CG2   1 
ATOM   3197  N  N     . ASP A 1 396 ? 137.329 156.912 135.114 1.00 36.30 ?  396 ASP A N     1 
ATOM   3198  C  CA    . ASP A 1 396 ? 136.259 156.650 136.064 1.00 36.61 ?  396 ASP A CA    1 
ATOM   3199  C  C     . ASP A 1 396 ? 135.046 157.521 135.740 1.00 38.06 ?  396 ASP A C     1 
ATOM   3200  O  O     . ASP A 1 396 ? 135.045 158.318 134.797 1.00 42.28 ?  396 ASP A O     1 
ATOM   3201  C  CB    . ASP A 1 396 ? 136.739 156.908 137.490 1.00 38.06 ?  396 ASP A CB    1 
ATOM   3202  C  CG    . ASP A 1 396 ? 137.986 156.121 137.842 1.00 42.51 ?  396 ASP A CG    1 
ATOM   3203  O  OD1   . ASP A 1 396 ? 138.218 155.058 137.228 1.00 43.52 ?  396 ASP A OD1   1 
ATOM   3204  O  OD2   . ASP A 1 396 ? 138.733 156.565 138.737 1.00 44.02 -1 396 ASP A OD2   1 
ATOM   3205  N  N     . TYR A 1 397 ? 133.992 157.362 136.538 1.00 37.44 ?  397 TYR A N     1 
ATOM   3206  C  CA    . TYR A 1 397 ? 132.835 158.229 136.407 1.00 34.06 ?  397 TYR A CA    1 
ATOM   3207  C  C     . TYR A 1 397 ? 133.230 159.670 136.725 1.00 37.34 ?  397 TYR A C     1 
ATOM   3208  O  O     . TYR A 1 397 ? 134.326 159.944 137.213 1.00 39.74 ?  397 TYR A O     1 
ATOM   3209  C  CB    . TYR A 1 397 ? 131.705 157.756 137.321 1.00 33.65 ?  397 TYR A CB    1 
ATOM   3210  C  CG    . TYR A 1 397 ? 130.328 158.161 136.846 1.00 33.80 ?  397 TYR A CG    1 
ATOM   3211  C  CD1   . TYR A 1 397 ? 129.651 157.403 135.901 1.00 36.07 ?  397 TYR A CD1   1 
ATOM   3212  C  CD2   . TYR A 1 397 ? 129.705 159.299 137.343 1.00 34.56 ?  397 TYR A CD2   1 
ATOM   3213  C  CE1   . TYR A 1 397 ? 128.394 157.768 135.462 1.00 33.88 ?  397 TYR A CE1   1 
ATOM   3214  C  CE2   . TYR A 1 397 ? 128.450 159.671 136.910 1.00 31.84 ?  397 TYR A CE2   1 
ATOM   3215  C  CZ    . TYR A 1 397 ? 127.799 158.902 135.972 1.00 34.09 ?  397 TYR A CZ    1 
ATOM   3216  O  OH    . TYR A 1 397 ? 126.547 159.270 135.539 1.00 39.73 ?  397 TYR A OH    1 
ATOM   3217  N  N     . ASP A 1 398 ? 132.331 160.595 136.372 1.00 41.00 ?  398 ASP A N     1 
ATOM   3218  C  CA    . ASP A 1 398 ? 132.455 162.048 136.512 1.00 42.01 ?  398 ASP A CA    1 
ATOM   3219  C  C     . ASP A 1 398 ? 133.870 162.527 136.190 1.00 44.08 ?  398 ASP A C     1 
ATOM   3220  O  O     . ASP A 1 398 ? 134.372 163.488 136.781 1.00 41.83 ?  398 ASP A O     1 
ATOM   3221  C  CB    . ASP A 1 398 ? 131.959 162.526 137.898 1.00 41.67 ?  398 ASP A CB    1 
ATOM   3222  C  CG    . ASP A 1 398 ? 132.964 162.339 139.045 1.00 44.94 ?  398 ASP A CG    1 
ATOM   3223  O  OD1   . ASP A 1 398 ? 132.694 162.901 140.127 1.00 45.96 ?  398 ASP A OD1   1 
ATOM   3224  O  OD2   . ASP A 1 398 ? 134.004 161.676 138.909 1.00 42.18 -1 398 ASP A OD2   1 
ATOM   3225  N  N     . GLU A 1 399 ? 134.496 161.870 135.215 1.00 48.02 ?  399 GLU A N     1 
ATOM   3226  C  CA    . GLU A 1 399 ? 135.825 162.205 134.732 1.00 43.95 ?  399 GLU A CA    1 
ATOM   3227  C  C     . GLU A 1 399 ? 135.820 162.093 133.216 1.00 44.55 ?  399 GLU A C     1 
ATOM   3228  O  O     . GLU A 1 399 ? 135.262 161.142 132.660 1.00 42.49 ?  399 GLU A O     1 
ATOM   3229  C  CB    . GLU A 1 399 ? 136.889 161.278 135.334 1.00 39.19 ?  399 GLU A CB    1 
ATOM   3230  C  CG    . GLU A 1 399 ? 138.233 161.942 135.570 1.00 42.93 ?  399 GLU A CG    1 
ATOM   3231  C  CD    . GLU A 1 399 ? 139.356 160.938 135.750 1.00 48.39 ?  399 GLU A CD    1 
ATOM   3232  O  OE1   . GLU A 1 399 ? 139.107 159.864 136.335 1.00 47.56 ?  399 GLU A OE1   1 
ATOM   3233  O  OE2   . GLU A 1 399 ? 140.488 161.224 135.306 1.00 47.06 -1 399 GLU A OE2   1 
ATOM   3234  N  N     . GLU A 1 400 ? 136.437 163.065 132.552 1.00 44.73 ?  400 GLU A N     1 
ATOM   3235  C  CA    . GLU A 1 400 ? 136.381 163.123 131.098 1.00 40.43 ?  400 GLU A CA    1 
ATOM   3236  C  C     . GLU A 1 400 ? 137.198 161.996 130.481 1.00 43.83 ?  400 GLU A C     1 
ATOM   3237  O  O     . GLU A 1 400 ? 138.364 161.791 130.832 1.00 43.14 ?  400 GLU A O     1 
ATOM   3238  C  CB    . GLU A 1 400 ? 136.887 164.477 130.604 1.00 40.22 ?  400 GLU A CB    1 
ATOM   3239  C  CG    . GLU A 1 400 ? 136.048 165.084 129.490 1.00 45.83 ?  400 GLU A CG    1 
ATOM   3240  C  CD    . GLU A 1 400 ? 134.592 165.259 129.880 1.00 48.85 ?  400 GLU A CD    1 
ATOM   3241  O  OE1   . GLU A 1 400 ? 134.324 165.627 131.042 1.00 46.49 ?  400 GLU A OE1   1 
ATOM   3242  O  OE2   . GLU A 1 400 ? 133.714 165.028 129.022 1.00 47.21 -1 400 GLU A OE2   1 
ATOM   3243  N  N     . ASP A 1 401 ? 136.581 161.265 129.556 1.00 35.69 ?  401 ASP A N     1 
ATOM   3244  C  CA    . ASP A 1 401 ? 137.271 160.209 128.833 1.00 33.74 ?  401 ASP A CA    1 
ATOM   3245  C  C     . ASP A 1 401 ? 138.092 160.794 127.692 1.00 34.42 ?  401 ASP A C     1 
ATOM   3246  O  O     . ASP A 1 401 ? 137.758 161.841 127.130 1.00 38.08 ?  401 ASP A O     1 
ATOM   3247  C  CB    . ASP A 1 401 ? 136.274 159.192 128.279 1.00 32.53 ?  401 ASP A CB    1 
ATOM   3248  C  CG    . ASP A 1 401 ? 135.342 158.645 129.340 1.00 37.68 ?  401 ASP A CG    1 
ATOM   3249  O  OD1   . ASP A 1 401 ? 135.837 158.076 130.334 1.00 42.07 ?  401 ASP A OD1   1 
ATOM   3250  O  OD2   . ASP A 1 401 ? 134.112 158.784 129.177 1.00 38.40 -1 401 ASP A OD2   1 
ATOM   3251  N  N     . GLU A 1 402 ? 139.176 160.105 127.350 1.00 31.60 ?  402 GLU A N     1 
ATOM   3252  C  CA    . GLU A 1 402 ? 139.987 160.451 126.186 1.00 29.37 ?  402 GLU A CA    1 
ATOM   3253  C  C     . GLU A 1 402 ? 139.507 159.548 125.055 1.00 24.85 ?  402 GLU A C     1 
ATOM   3254  O  O     . GLU A 1 402 ? 139.807 158.353 125.027 1.00 30.34 ?  402 GLU A O     1 
ATOM   3255  C  CB    . GLU A 1 402 ? 141.476 160.284 126.479 1.00 31.18 ?  402 GLU A CB    1 
ATOM   3256  C  CG    . GLU A 1 402 ? 142.392 160.305 125.253 1.00 36.78 ?  402 GLU A CG    1 
ATOM   3257  C  CD    . GLU A 1 402 ? 142.656 158.929 124.665 1.00 40.42 ?  402 GLU A CD    1 
ATOM   3258  O  OE1   . GLU A 1 402 ? 143.322 158.111 125.331 1.00 35.31 ?  402 GLU A OE1   1 
ATOM   3259  O  OE2   . GLU A 1 402 ? 142.204 158.670 123.531 1.00 34.93 -1 402 GLU A OE2   1 
ATOM   3260  N  N     . ILE A 1 403 ? 138.727 160.115 124.142 1.00 27.50 ?  403 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 403 ? 138.116 159.337 123.072 1.00 26.57 ?  403 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 403 ? 139.108 159.193 121.927 1.00 28.07 ?  403 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 403 ? 139.631 160.187 121.411 1.00 28.44 ?  403 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 403 ? 136.809 159.994 122.600 1.00 24.55 ?  403 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 403 ? 135.811 160.088 123.755 1.00 24.49 ?  403 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 403 ? 136.210 159.217 121.441 1.00 20.31 ?  403 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 403 ? 135.599 158.785 124.492 1.00 26.84 ?  403 ILE A CD1   1 
ATOM   3268  N  N     . GLY A 1 404 ? 139.372 157.956 121.533 1.00 23.34 ?  404 GLY A N     1 
ATOM   3269  C  CA    . GLY A 1 404 ? 140.262 157.640 120.438 1.00 9.27  ?  404 GLY A CA    1 
ATOM   3270  C  C     . GLY A 1 404 ? 139.516 157.388 119.145 1.00 19.17 ?  404 GLY A C     1 
ATOM   3271  O  O     . GLY A 1 404 ? 138.456 157.970 118.886 1.00 31.31 ?  404 GLY A O     1 
ATOM   3272  N  N     . LEU A 1 405 ? 140.074 156.506 118.321 1.00 22.22 ?  405 LEU A N     1 
ATOM   3273  C  CA    . LEU A 1 405 ? 139.491 156.152 117.033 1.00 7.02  ?  405 LEU A CA    1 
ATOM   3274  C  C     . LEU A 1 405 ? 139.213 154.657 117.012 1.00 8.34  ?  405 LEU A C     1 
ATOM   3275  O  O     . LEU A 1 405 ? 140.134 153.849 117.165 1.00 18.34 ?  405 LEU A O     1 
ATOM   3276  C  CB    . LEU A 1 405 ? 140.423 156.540 115.883 1.00 17.23 ?  405 LEU A CB    1 
ATOM   3277  C  CG    . LEU A 1 405 ? 140.780 158.022 115.759 1.00 18.22 ?  405 LEU A CG    1 
ATOM   3278  C  CD1   . LEU A 1 405 ? 141.833 158.232 114.684 1.00 21.75 ?  405 LEU A CD1   1 
ATOM   3279  C  CD2   . LEU A 1 405 ? 139.543 158.853 115.472 1.00 15.48 ?  405 LEU A CD2   1 
ATOM   3280  N  N     . ASP A 1 406 ? 137.949 154.294 116.818 1.00 22.38 ?  406 ASP A N     1 
ATOM   3281  C  CA    . ASP A 1 406 ? 137.537 152.907 116.659 1.00 17.43 ?  406 ASP A CA    1 
ATOM   3282  C  C     . ASP A 1 406 ? 136.981 152.718 115.256 1.00 19.13 ?  406 ASP A C     1 
ATOM   3283  O  O     . ASP A 1 406 ? 136.098 153.466 114.827 1.00 31.28 ?  406 ASP A O     1 
ATOM   3284  C  CB    . ASP A 1 406 ? 136.494 152.516 117.708 1.00 18.37 ?  406 ASP A CB    1 
ATOM   3285  C  CG    . ASP A 1 406 ? 137.119 152.083 119.020 1.00 29.15 ?  406 ASP A CG    1 
ATOM   3286  O  OD1   . ASP A 1 406 ? 138.360 152.151 119.146 1.00 32.47 ?  406 ASP A OD1   1 
ATOM   3287  O  OD2   . ASP A 1 406 ? 136.367 151.678 119.929 1.00 28.37 -1 406 ASP A OD2   1 
ATOM   3288  N  N     . ILE A 1 407 ? 137.484 151.711 114.558 1.00 21.24 ?  407 ILE A N     1 
ATOM   3289  C  CA    . ILE A 1 407 ? 137.223 151.558 113.134 1.00 15.66 ?  407 ILE A CA    1 
ATOM   3290  C  C     . ILE A 1 407 ? 135.795 151.087 112.907 1.00 14.81 ?  407 ILE A C     1 
ATOM   3291  O  O     . ILE A 1 407 ? 135.294 150.192 113.598 1.00 21.70 ?  407 ILE A O     1 
ATOM   3292  C  CB    . ILE A 1 407 ? 138.233 150.579 112.511 1.00 10.60 ?  407 ILE A CB    1 
ATOM   3293  C  CG1   . ILE A 1 407 ? 139.659 151.096 112.691 1.00 6.69  ?  407 ILE A CG1   1 
ATOM   3294  C  CG2   . ILE A 1 407 ? 137.921 150.359 111.053 1.00 16.52 ?  407 ILE A CG2   1 
ATOM   3295  C  CD1   . ILE A 1 407 ? 140.667 149.998 112.887 1.00 10.78 ?  407 ILE A CD1   1 
ATOM   3296  N  N     . SER A 1 408 ? 135.132 151.702 111.929 1.00 25.69 ?  408 SER A N     1 
ATOM   3297  C  CA    . SER A 1 408 ? 133.830 151.241 111.457 1.00 21.75 ?  408 SER A CA    1 
ATOM   3298  C  C     . SER A 1 408 ? 133.703 151.671 110.004 1.00 24.54 ?  408 SER A C     1 
ATOM   3299  O  O     . SER A 1 408 ? 133.349 152.822 109.731 1.00 30.62 ?  408 SER A O     1 
ATOM   3300  C  CB    . SER A 1 408 ? 132.698 151.816 112.302 1.00 26.05 ?  408 SER A CB    1 
ATOM   3301  O  OG    . SER A 1 408 ? 132.661 153.229 112.201 1.00 29.29 ?  408 SER A OG    1 
ATOM   3302  N  N     . CYS A 1 409 ? 133.987 150.762 109.079 1.00 20.52 ?  409 CYS A N     1 
ATOM   3303  C  CA    . CYS A 1 409 ? 133.954 151.094 107.663 1.00 26.32 ?  409 CYS A CA    1 
ATOM   3304  C  C     . CYS A 1 409 ? 132.622 150.685 107.047 1.00 30.59 ?  409 CYS A C     1 
ATOM   3305  O  O     . CYS A 1 409 ? 131.853 149.903 107.610 1.00 25.65 ?  409 CYS A O     1 
ATOM   3306  C  CB    . CYS A 1 409 ? 135.113 150.435 106.911 1.00 23.24 ?  409 CYS A CB    1 
ATOM   3307  S  SG    . CYS A 1 409 ? 134.768 148.817 106.209 1.00 41.88 ?  409 CYS A SG    1 
ATOM   3308  N  N     . ASN A 1 410 ? 132.364 151.234 105.867 1.00 30.01 ?  410 ASN A N     1 
ATOM   3309  C  CA    . ASN A 1 410 ? 131.077 151.140 105.196 1.00 18.67 ?  410 ASN A CA    1 
ATOM   3310  C  C     . ASN A 1 410 ? 131.207 150.187 104.016 1.00 21.72 ?  410 ASN A C     1 
ATOM   3311  O  O     . ASN A 1 410 ? 132.008 150.431 103.109 1.00 29.59 ?  410 ASN A O     1 
ATOM   3312  C  CB    . ASN A 1 410 ? 130.637 152.525 104.733 1.00 26.98 ?  410 ASN A CB    1 
ATOM   3313  C  CG    . ASN A 1 410 ? 129.178 152.592 104.399 1.00 32.40 ?  410 ASN A CG    1 
ATOM   3314  O  OD1   . ASN A 1 410 ? 128.431 151.635 104.595 1.00 35.72 ?  410 ASN A OD1   1 
ATOM   3315  N  ND2   . ASN A 1 410 ? 128.758 153.731 103.882 1.00 34.49 ?  410 ASN A ND2   1 
ATOM   3316  N  N     . LEU A 1 411 ? 130.413 149.120 104.019 1.00 21.50 ?  411 LEU A N     1 
ATOM   3317  C  CA    . LEU A 1 411 ? 130.570 148.043 103.052 1.00 11.76 ?  411 LEU A CA    1 
ATOM   3318  C  C     . LEU A 1 411 ? 129.679 148.241 101.831 1.00 16.12 ?  411 LEU A C     1 
ATOM   3319  O  O     . LEU A 1 411 ? 128.575 148.786 101.917 1.00 26.82 ?  411 LEU A O     1 
ATOM   3320  C  CB    . LEU A 1 411 ? 130.254 146.692 103.695 1.00 19.14 ?  411 LEU A CB    1 
ATOM   3321  C  CG    . LEU A 1 411 ? 131.413 145.787 104.116 1.00 20.45 ?  411 LEU A CG    1 
ATOM   3322  C  CD1   . LEU A 1 411 ? 132.490 146.582 104.821 1.00 19.01 ?  411 LEU A CD1   1 
ATOM   3323  C  CD2   . LEU A 1 411 ? 130.910 144.658 104.999 1.00 18.70 ?  411 LEU A CD2   1 
ATOM   3324  N  N     . GLY A 1 412 ? 130.177 147.778 100.686 1.00 22.65 ?  412 GLY A N     1 
ATOM   3325  C  CA    . GLY A 1 412 ? 129.457 147.794 99.426  1.00 13.61 ?  412 GLY A CA    1 
ATOM   3326  C  C     . GLY A 1 412 ? 130.284 147.109 98.358  1.00 13.30 ?  412 GLY A C     1 
ATOM   3327  O  O     . GLY A 1 412 ? 131.499 147.320 98.302  1.00 23.34 ?  412 GLY A O     1 
ATOM   3328  N  N     . SER A 1 413 ? 129.666 146.293 97.506  1.00 14.80 ?  413 SER A N     1 
ATOM   3329  C  CA    . SER A 1 413 ? 130.408 145.420 96.605  1.00 10.91 ?  413 SER A CA    1 
ATOM   3330  C  C     . SER A 1 413 ? 130.039 145.685 95.155  1.00 17.65 ?  413 SER A C     1 
ATOM   3331  O  O     . SER A 1 413 ? 128.857 145.761 94.811  1.00 21.51 ?  413 SER A O     1 
ATOM   3332  C  CB    . SER A 1 413 ? 130.158 143.951 96.944  1.00 9.74  ?  413 SER A CB    1 
ATOM   3333  O  OG    . SER A 1 413 ? 130.667 143.639 98.226  1.00 32.49 ?  413 SER A OG    1 
ATOM   3334  N  N     . LEU A 1 414 ? 131.054 145.808 94.306  1.00 18.32 ?  414 LEU A N     1 
ATOM   3335  C  CA    . LEU A 1 414 ? 130.840 145.835 92.868  1.00 12.54 ?  414 LEU A CA    1 
ATOM   3336  C  C     . LEU A 1 414 ? 130.643 144.418 92.348  1.00 19.08 ?  414 LEU A C     1 
ATOM   3337  O  O     . LEU A 1 414 ? 131.326 143.485 92.776  1.00 24.42 ?  414 LEU A O     1 
ATOM   3338  C  CB    . LEU A 1 414 ? 132.029 146.484 92.161  1.00 17.56 ?  414 LEU A CB    1 
ATOM   3339  C  CG    . LEU A 1 414 ? 132.559 147.794 92.740  1.00 20.23 ?  414 LEU A CG    1 
ATOM   3340  C  CD1   . LEU A 1 414 ? 133.912 148.122 92.138  1.00 22.49 ?  414 LEU A CD1   1 
ATOM   3341  C  CD2   . LEU A 1 414 ? 131.574 148.921 92.493  1.00 20.11 ?  414 LEU A CD2   1 
ATOM   3342  N  N     . ASN A 1 415 ? 129.701 144.258 91.425  1.00 25.67 ?  415 ASN A N     1 
ATOM   3343  C  CA    . ASN A 1 415 ? 129.517 142.991 90.723  1.00 24.25 ?  415 ASN A CA    1 
ATOM   3344  C  C     . ASN A 1 415 ? 130.392 143.042 89.479  1.00 22.60 ?  415 ASN A C     1 
ATOM   3345  O  O     . ASN A 1 415 ? 130.057 143.710 88.499  1.00 27.33 ?  415 ASN A O     1 
ATOM   3346  C  CB    . ASN A 1 415 ? 128.048 142.765 90.386  1.00 20.70 ?  415 ASN A CB    1 
ATOM   3347  C  CG    . ASN A 1 415 ? 127.745 141.326 90.020  1.00 25.69 ?  415 ASN A CG    1 
ATOM   3348  O  OD1   . ASN A 1 415 ? 128.398 140.738 89.160  1.00 33.28 ?  415 ASN A OD1   1 
ATOM   3349  N  ND2   . ASN A 1 415 ? 126.747 140.747 90.679  1.00 29.90 ?  415 ASN A ND2   1 
ATOM   3350  N  N     . ILE A 1 416 ? 131.520 142.329 89.520  1.00 21.84 ?  416 ILE A N     1 
ATOM   3351  C  CA    . ILE A 1 416 ? 132.536 142.458 88.479  1.00 24.00 ?  416 ILE A CA    1 
ATOM   3352  C  C     . ILE A 1 416 ? 131.972 142.074 87.119  1.00 26.98 ?  416 ILE A C     1 
ATOM   3353  O  O     . ILE A 1 416 ? 132.248 142.731 86.109  1.00 29.35 ?  416 ILE A O     1 
ATOM   3354  C  CB    . ILE A 1 416 ? 133.777 141.619 88.836  1.00 20.69 ?  416 ILE A CB    1 
ATOM   3355  C  CG1   . ILE A 1 416 ? 134.430 142.153 90.110  1.00 18.38 ?  416 ILE A CG1   1 
ATOM   3356  C  CG2   . ILE A 1 416 ? 134.771 141.613 87.689  1.00 14.34 ?  416 ILE A CG2   1 
ATOM   3357  C  CD1   . ILE A 1 416 ? 135.508 141.258 90.661  1.00 19.31 ?  416 ILE A CD1   1 
ATOM   3358  N  N     . LEU A 1 417 ? 131.166 141.013 87.070  1.00 20.94 ?  417 LEU A N     1 
ATOM   3359  C  CA    . LEU A 1 417 ? 130.571 140.600 85.804  1.00 22.96 ?  417 LEU A CA    1 
ATOM   3360  C  C     . LEU A 1 417 ? 129.660 141.687 85.248  1.00 23.58 ?  417 LEU A C     1 
ATOM   3361  O  O     . LEU A 1 417 ? 129.807 142.106 84.092  1.00 34.84 ?  417 LEU A O     1 
ATOM   3362  C  CB    . LEU A 1 417 ? 129.807 139.289 85.992  1.00 25.83 ?  417 LEU A CB    1 
ATOM   3363  C  CG    . LEU A 1 417 ? 129.078 138.715 84.776  1.00 28.56 ?  417 LEU A CG    1 
ATOM   3364  C  CD1   . LEU A 1 417 ? 129.462 137.263 84.574  1.00 25.37 ?  417 LEU A CD1   1 
ATOM   3365  C  CD2   . LEU A 1 417 ? 127.575 138.849 84.938  1.00 28.76 ?  417 LEU A CD2   1 
ATOM   3366  N  N     . ASN A 1 418 ? 128.727 142.175 86.069  1.00 25.55 ?  418 ASN A N     1 
ATOM   3367  C  CA    . ASN A 1 418 ? 127.784 143.189 85.607  1.00 25.79 ?  418 ASN A CA    1 
ATOM   3368  C  C     . ASN A 1 418 ? 128.481 144.515 85.333  1.00 27.32 ?  418 ASN A C     1 
ATOM   3369  O  O     . ASN A 1 418 ? 128.125 145.223 84.384  1.00 29.87 ?  418 ASN A O     1 
ATOM   3370  C  CB    . ASN A 1 418 ? 126.664 143.365 86.632  1.00 25.54 ?  418 ASN A CB    1 
ATOM   3371  C  CG    . ASN A 1 418 ? 125.793 142.133 86.756  1.00 29.11 ?  418 ASN A CG    1 
ATOM   3372  O  OD1   . ASN A 1 418 ? 125.506 141.464 85.765  1.00 29.68 ?  418 ASN A OD1   1 
ATOM   3373  N  ND2   . ASN A 1 418 ? 125.370 141.823 87.975  1.00 29.21 ?  418 ASN A ND2   1 
ATOM   3374  N  N     . VAL A 1 419 ? 129.469 144.873 86.157  1.00 31.03 ?  419 VAL A N     1 
ATOM   3375  C  CA    . VAL A 1 419 ? 130.199 146.120 85.944  1.00 28.81 ?  419 VAL A CA    1 
ATOM   3376  C  C     . VAL A 1 419 ? 130.972 146.073 84.633  1.00 29.87 ?  419 VAL A C     1 
ATOM   3377  O  O     . VAL A 1 419 ? 130.963 147.036 83.857  1.00 32.16 ?  419 VAL A O     1 
ATOM   3378  C  CB    . VAL A 1 419 ? 131.126 146.409 87.141  1.00 26.42 ?  419 VAL A CB    1 
ATOM   3379  C  CG1   . VAL A 1 419 ? 132.156 147.455 86.777  1.00 27.47 ?  419 VAL A CG1   1 
ATOM   3380  C  CG2   . VAL A 1 419 ? 130.316 146.883 88.327  1.00 28.81 ?  419 VAL A CG2   1 
ATOM   3381  N  N     . MET A 1 420 ? 131.645 144.955 84.356  1.00 32.84 ?  420 MET A N     1 
ATOM   3382  C  CA    . MET A 1 420 ? 132.497 144.908 83.176  1.00 33.42 ?  420 MET A CA    1 
ATOM   3383  C  C     . MET A 1 420 ? 131.701 144.681 81.896  1.00 30.71 ?  420 MET A C     1 
ATOM   3384  O  O     . MET A 1 420 ? 132.113 145.155 80.832  1.00 35.76 ?  420 MET A O     1 
ATOM   3385  C  CB    . MET A 1 420 ? 133.572 143.833 83.334  1.00 31.20 ?  420 MET A CB    1 
ATOM   3386  C  CG    . MET A 1 420 ? 134.820 144.353 84.035  1.00 26.08 ?  420 MET A CG    1 
ATOM   3387  S  SD    . MET A 1 420 ? 136.148 144.900 82.946  1.00 47.11 ?  420 MET A SD    1 
ATOM   3388  C  CE    . MET A 1 420 ? 136.275 143.538 81.801  1.00 33.81 ?  420 MET A CE    1 
ATOM   3389  N  N     . GLU A 1 421 ? 130.572 143.968 81.963  1.00 32.30 ?  421 GLU A N     1 
ATOM   3390  C  CA    . GLU A 1 421 ? 129.761 143.811 80.760  1.00 37.53 ?  421 GLU A CA    1 
ATOM   3391  C  C     . GLU A 1 421 ? 129.065 145.108 80.372  1.00 37.35 ?  421 GLU A C     1 
ATOM   3392  O  O     . GLU A 1 421 ? 128.719 145.285 79.200  1.00 40.20 ?  421 GLU A O     1 
ATOM   3393  C  CB    . GLU A 1 421 ? 128.723 142.701 80.940  1.00 34.43 ?  421 GLU A CB    1 
ATOM   3394  C  CG    . GLU A 1 421 ? 127.679 142.976 82.004  1.00 39.15 ?  421 GLU A CG    1 
ATOM   3395  C  CD    . GLU A 1 421 ? 126.580 141.934 82.019  1.00 43.34 ?  421 GLU A CD    1 
ATOM   3396  O  OE1   . GLU A 1 421 ? 126.444 141.198 81.018  1.00 44.06 ?  421 GLU A OE1   1 
ATOM   3397  O  OE2   . GLU A 1 421 ? 125.850 141.848 83.028  1.00 40.29 -1 421 GLU A OE2   1 
ATOM   3398  N  N     . HIS A 1 422 ? 128.856 146.012 81.325  1.00 35.77 ?  422 HIS A N     1 
ATOM   3399  C  CA    . HIS A 1 422 ? 128.312 147.334 81.052  1.00 35.28 ?  422 HIS A CA    1 
ATOM   3400  C  C     . HIS A 1 422 ? 129.392 148.359 80.744  1.00 39.14 ?  422 HIS A C     1 
ATOM   3401  O  O     . HIS A 1 422 ? 129.061 149.504 80.418  1.00 39.84 ?  422 HIS A O     1 
ATOM   3402  C  CB    . HIS A 1 422 ? 127.476 147.818 82.242  1.00 32.46 ?  422 HIS A CB    1 
ATOM   3403  C  CG    . HIS A 1 422 ? 126.136 147.161 82.347  1.00 36.58 ?  422 HIS A CG    1 
ATOM   3404  N  ND1   . HIS A 1 422 ? 125.918 146.034 83.110  1.00 36.83 ?  422 HIS A ND1   1 
ATOM   3405  C  CD2   . HIS A 1 422 ? 124.944 147.471 81.786  1.00 36.85 ?  422 HIS A CD2   1 
ATOM   3406  C  CE1   . HIS A 1 422 ? 124.650 145.679 83.015  1.00 38.65 ?  422 HIS A CE1   1 
ATOM   3407  N  NE2   . HIS A 1 422 ? 124.037 146.534 82.217  1.00 39.61 ?  422 HIS A NE2   1 
ATOM   3408  N  N     . LYS A 1 423 ? 130.666 147.973 80.836  1.00 40.10 ?  423 LYS A N     1 
ATOM   3409  C  CA    . LYS A 1 423 ? 131.796 148.865 80.572  1.00 39.49 ?  423 LYS A CA    1 
ATOM   3410  C  C     . LYS A 1 423 ? 131.695 150.140 81.404  1.00 42.48 ?  423 LYS A C     1 
ATOM   3411  O  O     . LYS A 1 423 ? 131.908 151.254 80.919  1.00 42.19 ?  423 LYS A O     1 
ATOM   3412  C  CB    . LYS A 1 423 ? 131.900 149.185 79.080  1.00 37.95 ?  423 LYS A CB    1 
ATOM   3413  C  CG    . LYS A 1 423 ? 132.180 147.974 78.207  1.00 38.37 ?  423 LYS A CG    1 
ATOM   3414  C  CD    . LYS A 1 423 ? 132.059 148.317 76.732  1.00 40.56 ?  423 LYS A CD    1 
ATOM   3415  C  CE    . LYS A 1 423 ? 132.085 147.066 75.873  1.00 40.10 ?  423 LYS A CE    1 
ATOM   3416  N  NZ    . LYS A 1 423 ? 133.190 146.149 76.265  1.00 43.35 1  423 LYS A NZ    1 
ATOM   3417  N  N     . SER A 1 424 ? 131.367 149.967 82.682  1.00 32.26 ?  424 SER A N     1 
ATOM   3418  C  CA    . SER A 1 424 ? 131.064 151.074 83.580  1.00 29.82 ?  424 SER A CA    1 
ATOM   3419  C  C     . SER A 1 424 ? 131.818 150.930 84.894  1.00 32.67 ?  424 SER A C     1 
ATOM   3420  O  O     . SER A 1 424 ? 131.245 151.040 85.979  1.00 32.96 ?  424 SER A O     1 
ATOM   3421  C  CB    . SER A 1 424 ? 129.562 151.161 83.834  1.00 34.00 ?  424 SER A CB    1 
ATOM   3422  O  OG    . SER A 1 424 ? 129.127 150.096 84.659  1.00 31.39 ?  424 SER A OG    1 
ATOM   3423  N  N     . ILE A 1 425 ? 133.124 150.672 84.819  1.00 31.72 ?  425 ILE A N     1 
ATOM   3424  C  CA    . ILE A 1 425 ? 133.929 150.620 86.037  1.00 23.87 ?  425 ILE A CA    1 
ATOM   3425  C  C     . ILE A 1 425 ? 133.951 151.985 86.716  1.00 29.13 ?  425 ILE A C     1 
ATOM   3426  O  O     . ILE A 1 425 ? 133.710 152.098 87.924  1.00 37.02 ?  425 ILE A O     1 
ATOM   3427  C  CB    . ILE A 1 425 ? 135.353 150.125 85.727  1.00 26.96 ?  425 ILE A CB    1 
ATOM   3428  C  CG1   . ILE A 1 425 ? 135.354 148.623 85.442  1.00 31.42 ?  425 ILE A CG1   1 
ATOM   3429  C  CG2   . ILE A 1 425 ? 136.291 150.435 86.884  1.00 27.22 ?  425 ILE A CG2   1 
ATOM   3430  C  CD1   . ILE A 1 425 ? 136.703 148.092 85.009  1.00 29.41 ?  425 ILE A CD1   1 
ATOM   3431  N  N     . GLU A 1 426 ? 134.215 153.042 85.945  1.00 25.95 ?  426 GLU A N     1 
ATOM   3432  C  CA    . GLU A 1 426 ? 134.340 154.377 86.523  1.00 26.36 ?  426 GLU A CA    1 
ATOM   3433  C  C     . GLU A 1 426 ? 133.033 154.837 87.156  1.00 27.33 ?  426 GLU A C     1 
ATOM   3434  O  O     . GLU A 1 426 ? 133.006 155.257 88.320  1.00 32.66 ?  426 GLU A O     1 
ATOM   3435  C  CB    . GLU A 1 426 ? 134.790 155.366 85.449  1.00 26.18 ?  426 GLU A CB    1 
ATOM   3436  C  CG    . GLU A 1 426 ? 134.536 156.820 85.802  1.00 28.32 ?  426 GLU A CG    1 
ATOM   3437  C  CD    . GLU A 1 426 ? 135.020 157.771 84.728  1.00 36.93 ?  426 GLU A CD    1 
ATOM   3438  O  OE1   . GLU A 1 426 ? 135.449 157.291 83.657  1.00 34.16 ?  426 GLU A OE1   1 
ATOM   3439  O  OE2   . GLU A 1 426 ? 134.970 158.999 84.952  1.00 37.58 -1 426 GLU A OE2   1 
ATOM   3440  N  N     . LYS A 1 427 ? 131.937 154.773 86.397  1.00 27.52 ?  427 LYS A N     1 
ATOM   3441  C  CA    . LYS A 1 427 ? 130.659 155.267 86.897  1.00 24.47 ?  427 LYS A CA    1 
ATOM   3442  C  C     . LYS A 1 427 ? 130.191 154.465 88.103  1.00 26.33 ?  427 LYS A C     1 
ATOM   3443  O  O     . LYS A 1 427 ? 129.728 155.038 89.097  1.00 31.77 ?  427 LYS A O     1 
ATOM   3444  C  CB    . LYS A 1 427 ? 129.614 155.231 85.781  1.00 31.26 ?  427 LYS A CB    1 
ATOM   3445  C  CG    . LYS A 1 427 ? 128.173 155.285 86.263  1.00 28.72 ?  427 LYS A CG    1 
ATOM   3446  C  CD    . LYS A 1 427 ? 127.259 154.472 85.361  1.00 32.81 ?  427 LYS A CD    1 
ATOM   3447  C  CE    . LYS A 1 427 ? 127.183 153.025 85.811  1.00 32.53 ?  427 LYS A CE    1 
ATOM   3448  N  NZ    . LYS A 1 427 ? 126.177 152.248 85.032  1.00 29.00 1  427 LYS A NZ    1 
ATOM   3449  N  N     . THR A 1 428 ? 130.313 153.138 88.040  1.00 26.39 ?  428 THR A N     1 
ATOM   3450  C  CA    . THR A 1 428 ? 129.888 152.309 89.162  1.00 21.30 ?  428 THR A CA    1 
ATOM   3451  C  C     . THR A 1 428 ? 130.733 152.577 90.398  1.00 23.90 ?  428 THR A C     1 
ATOM   3452  O  O     . THR A 1 428 ? 130.195 152.692 91.504  1.00 31.41 ?  428 THR A O     1 
ATOM   3453  C  CB    . THR A 1 428 ? 129.952 150.830 88.789  1.00 25.35 ?  428 THR A CB    1 
ATOM   3454  O  OG1   . THR A 1 428 ? 129.277 150.622 87.543  1.00 29.04 ?  428 THR A OG1   1 
ATOM   3455  C  CG2   . THR A 1 428 ? 129.290 149.985 89.863  1.00 24.41 ?  428 THR A CG2   1 
ATOM   3456  N  N     . VAL A 1 429 ? 132.053 152.689 90.234  1.00 24.51 ?  429 VAL A N     1 
ATOM   3457  C  CA    . VAL A 1 429 ? 132.918 152.935 91.383  1.00 24.24 ?  429 VAL A CA    1 
ATOM   3458  C  C     . VAL A 1 429 ? 132.599 154.284 92.012  1.00 23.22 ?  429 VAL A C     1 
ATOM   3459  O  O     . VAL A 1 429 ? 132.501 154.404 93.238  1.00 26.22 ?  429 VAL A O     1 
ATOM   3460  C  CB    . VAL A 1 429 ? 134.400 152.833 90.975  1.00 21.22 ?  429 VAL A CB    1 
ATOM   3461  C  CG1   . VAL A 1 429 ? 135.284 153.494 92.016  1.00 18.94 ?  429 VAL A CG1   1 
ATOM   3462  C  CG2   . VAL A 1 429 ? 134.800 151.381 90.796  1.00 23.02 ?  429 VAL A CG2   1 
ATOM   3463  N  N     . LYS A 1 430 ? 132.415 155.318 91.187  1.00 22.34 ?  430 LYS A N     1 
ATOM   3464  C  CA    . LYS A 1 430 ? 132.144 156.645 91.733  1.00 20.97 ?  430 LYS A CA    1 
ATOM   3465  C  C     . LYS A 1 430 ? 130.782 156.706 92.413  1.00 23.22 ?  430 LYS A C     1 
ATOM   3466  O  O     . LYS A 1 430 ? 130.647 157.302 93.489  1.00 30.05 ?  430 LYS A O     1 
ATOM   3467  C  CB    . LYS A 1 430 ? 132.255 157.697 90.631  1.00 19.83 ?  430 LYS A CB    1 
ATOM   3468  C  CG    . LYS A 1 430 ? 133.657 157.824 90.063  1.00 23.31 ?  430 LYS A CG    1 
ATOM   3469  C  CD    . LYS A 1 430 ? 133.874 159.163 89.390  1.00 27.87 ?  430 LYS A CD    1 
ATOM   3470  C  CE    . LYS A 1 430 ? 135.339 159.369 89.052  1.00 28.43 ?  430 LYS A CE    1 
ATOM   3471  N  NZ    . LYS A 1 430 ? 135.592 160.720 88.484  1.00 30.72 1  430 LYS A NZ    1 
ATOM   3472  N  N     . LEU A 1 431 ? 129.759 156.089 91.817  1.00 26.98 ?  431 LEU A N     1 
ATOM   3473  C  CA    . LEU A 1 431 ? 128.440 156.094 92.442  1.00 22.52 ?  431 LEU A CA    1 
ATOM   3474  C  C     . LEU A 1 431 ? 128.435 155.283 93.732  1.00 21.71 ?  431 LEU A C     1 
ATOM   3475  O  O     . LEU A 1 431 ? 127.795 155.675 94.716  1.00 28.12 ?  431 LEU A O     1 
ATOM   3476  C  CB    . LEU A 1 431 ? 127.394 155.565 91.463  1.00 27.33 ?  431 LEU A CB    1 
ATOM   3477  C  CG    . LEU A 1 431 ? 126.682 156.611 90.604  1.00 30.18 ?  431 LEU A CG    1 
ATOM   3478  C  CD1   . LEU A 1 431 ? 125.946 155.946 89.453  1.00 26.87 ?  431 LEU A CD1   1 
ATOM   3479  C  CD2   . LEU A 1 431 ? 125.725 157.433 91.449  1.00 28.35 ?  431 LEU A CD2   1 
ATOM   3480  N  N     . ALA A 1 432 ? 129.143 154.152 93.750  1.00 20.35 ?  432 ALA A N     1 
ATOM   3481  C  CA    . ALA A 1 432 ? 129.254 153.365 94.971  1.00 19.22 ?  432 ALA A CA    1 
ATOM   3482  C  C     . ALA A 1 432 ? 129.995 154.136 96.053  1.00 24.76 ?  432 ALA A C     1 
ATOM   3483  O  O     . ALA A 1 432 ? 129.630 154.071 97.231  1.00 26.67 ?  432 ALA A O     1 
ATOM   3484  C  CB    . ALA A 1 432 ? 129.957 152.042 94.677  1.00 26.31 ?  432 ALA A CB    1 
ATOM   3485  N  N     . THR A 1 433 ? 131.042 154.870 95.671  1.00 22.76 ?  433 THR A N     1 
ATOM   3486  C  CA    . THR A 1 433 ? 131.756 155.706 96.630  1.00 17.94 ?  433 THR A CA    1 
ATOM   3487  C  C     . THR A 1 433 ? 130.847 156.787 97.197  1.00 22.72 ?  433 THR A C     1 
ATOM   3488  O  O     . THR A 1 433 ? 130.876 157.062 98.400  1.00 27.81 ?  433 THR A O     1 
ATOM   3489  C  CB    . THR A 1 433 ? 132.982 156.332 95.965  1.00 20.26 ?  433 THR A CB    1 
ATOM   3490  O  OG1   . THR A 1 433 ? 133.775 155.305 95.356  1.00 25.56 ?  433 THR A OG1   1 
ATOM   3491  C  CG2   . THR A 1 433 ? 133.826 157.077 96.987  1.00 24.42 ?  433 THR A CG2   1 
ATOM   3492  N  N     . ASP A 1 434 ? 130.033 157.411 96.343  1.00 20.19 ?  434 ASP A N     1 
ATOM   3493  C  CA    . ASP A 1 434 ? 129.100 158.428 96.822  1.00 15.86 ?  434 ASP A CA    1 
ATOM   3494  C  C     . ASP A 1 434 ? 128.073 157.835 97.781  1.00 19.40 ?  434 ASP A C     1 
ATOM   3495  O  O     . ASP A 1 434 ? 127.759 158.435 98.816  1.00 25.70 ?  434 ASP A O     1 
ATOM   3496  C  CB    . ASP A 1 434 ? 128.405 159.098 95.637  1.00 23.42 ?  434 ASP A CB    1 
ATOM   3497  C  CG    . ASP A 1 434 ? 129.357 159.908 94.786  1.00 31.37 ?  434 ASP A CG    1 
ATOM   3498  O  OD1   . ASP A 1 434 ? 130.375 160.388 95.326  1.00 29.06 ?  434 ASP A OD1   1 
ATOM   3499  O  OD2   . ASP A 1 434 ? 129.088 160.064 93.577  1.00 30.81 -1 434 ASP A OD2   1 
ATOM   3500  N  N     . SER A 1 435 ? 127.536 156.658 97.453  1.00 20.41 ?  435 SER A N     1 
ATOM   3501  C  CA    . SER A 1 435 ? 126.566 156.013 98.336  1.00 17.04 ?  435 SER A CA    1 
ATOM   3502  C  C     . SER A 1 435 ? 127.199 155.627 99.668  1.00 25.13 ?  435 SER A C     1 
ATOM   3503  O  O     . SER A 1 435 ? 126.580 155.791 100.728 1.00 34.54 ?  435 SER A O     1 
ATOM   3504  C  CB    . SER A 1 435 ? 125.970 154.785 97.651  1.00 19.28 ?  435 SER A CB    1 
ATOM   3505  O  OG    . SER A 1 435 ? 126.915 153.734 97.576  1.00 23.37 ?  435 SER A OG    1 
ATOM   3506  N  N     . LEU A 1 436 ? 128.426 155.105 99.633  1.00 18.68 ?  436 LEU A N     1 
ATOM   3507  C  CA    . LEU A 1 436 ? 129.118 154.747 100.864 1.00 13.11 ?  436 LEU A CA    1 
ATOM   3508  C  C     . LEU A 1 436 ? 129.418 155.979 101.705 1.00 15.45 ?  436 LEU A C     1 
ATOM   3509  O  O     . LEU A 1 436 ? 129.308 155.941 102.935 1.00 27.01 ?  436 LEU A O     1 
ATOM   3510  C  CB    . LEU A 1 436 ? 130.401 153.984 100.540 1.00 20.26 ?  436 LEU A CB    1 
ATOM   3511  C  CG    . LEU A 1 436 ? 130.202 152.575 99.986  1.00 17.84 ?  436 LEU A CG    1 
ATOM   3512  C  CD1   . LEU A 1 436 ? 131.526 151.967 99.558  1.00 17.53 ?  436 LEU A CD1   1 
ATOM   3513  C  CD2   . LEU A 1 436 ? 129.514 151.701 101.012 1.00 18.63 ?  436 LEU A CD2   1 
ATOM   3514  N  N     . THR A 1 437 ? 129.796 157.084 101.057 1.00 19.99 ?  437 THR A N     1 
ATOM   3515  C  CA    . THR A 1 437 ? 130.000 158.336 101.775 1.00 20.52 ?  437 THR A CA    1 
ATOM   3516  C  C     . THR A 1 437 ? 128.710 158.809 102.430 1.00 23.63 ?  437 THR A C     1 
ATOM   3517  O  O     . THR A 1 437 ? 128.718 159.257 103.581 1.00 25.90 ?  437 THR A O     1 
ATOM   3518  C  CB    . THR A 1 437 ? 130.536 159.402 100.820 1.00 18.17 ?  437 THR A CB    1 
ATOM   3519  O  OG1   . THR A 1 437 ? 131.727 158.922 100.187 1.00 17.98 ?  437 THR A OG1   1 
ATOM   3520  C  CG2   . THR A 1 437 ? 130.847 160.683 101.570 1.00 22.56 ?  437 THR A CG2   1 
ATOM   3521  N  N     . HIS A 1 438 ? 127.588 158.712 101.711 1.00 22.47 ?  438 HIS A N     1 
ATOM   3522  C  CA    . HIS A 1 438 ? 126.311 159.118 102.285 1.00 23.06 ?  438 HIS A CA    1 
ATOM   3523  C  C     . HIS A 1 438 ? 125.948 158.265 103.493 1.00 22.61 ?  438 HIS A C     1 
ATOM   3524  O  O     . HIS A 1 438 ? 125.502 158.789 104.520 1.00 26.43 ?  438 HIS A O     1 
ATOM   3525  C  CB    . HIS A 1 438 ? 125.209 159.040 101.230 1.00 26.74 ?  438 HIS A CB    1 
ATOM   3526  C  CG    . HIS A 1 438 ? 123.831 159.194 101.792 1.00 27.35 ?  438 HIS A CG    1 
ATOM   3527  N  ND1   . HIS A 1 438 ? 123.276 160.422 102.076 1.00 25.41 ?  438 HIS A ND1   1 
ATOM   3528  C  CD2   . HIS A 1 438 ? 122.900 158.273 102.133 1.00 23.58 ?  438 HIS A CD2   1 
ATOM   3529  C  CE1   . HIS A 1 438 ? 122.060 160.251 102.564 1.00 30.51 ?  438 HIS A CE1   1 
ATOM   3530  N  NE2   . HIS A 1 438 ? 121.808 158.956 102.608 1.00 29.10 ?  438 HIS A NE2   1 
ATOM   3531  N  N     . VAL A 1 439 ? 126.134 156.948 103.390 1.00 24.67 ?  439 VAL A N     1 
ATOM   3532  C  CA    . VAL A 1 439 ? 125.788 156.075 104.509 1.00 20.20 ?  439 VAL A CA    1 
ATOM   3533  C  C     . VAL A 1 439 ? 126.716 156.319 105.693 1.00 27.85 ?  439 VAL A C     1 
ATOM   3534  O  O     . VAL A 1 439 ? 126.278 156.284 106.850 1.00 36.63 ?  439 VAL A O     1 
ATOM   3535  C  CB    . VAL A 1 439 ? 125.800 154.603 104.061 1.00 20.52 ?  439 VAL A CB    1 
ATOM   3536  C  CG1   . VAL A 1 439 ? 125.784 153.670 105.262 1.00 21.99 ?  439 VAL A CG1   1 
ATOM   3537  C  CG2   . VAL A 1 439 ? 124.624 154.321 103.158 1.00 30.53 ?  439 VAL A CG2   1 
ATOM   3538  N  N     . SER A 1 440 ? 128.000 156.580 105.436 1.00 21.50 ?  440 SER A N     1 
ATOM   3539  C  CA    . SER A 1 440 ? 128.921 156.905 106.520 1.00 20.63 ?  440 SER A CA    1 
ATOM   3540  C  C     . SER A 1 440 ? 128.545 158.221 107.191 1.00 24.45 ?  440 SER A C     1 
ATOM   3541  O  O     . SER A 1 440 ? 128.652 158.352 108.416 1.00 26.57 ?  440 SER A O     1 
ATOM   3542  C  CB    . SER A 1 440 ? 130.354 156.959 105.989 1.00 25.67 ?  440 SER A CB    1 
ATOM   3543  O  OG    . SER A 1 440 ? 131.271 157.281 107.019 1.00 24.86 ?  440 SER A OG    1 
ATOM   3544  N  N     . GLU A 1 441 ? 128.108 159.207 106.404 1.00 26.21 ?  441 GLU A N     1 
ATOM   3545  C  CA    . GLU A 1 441 ? 127.724 160.495 106.972 1.00 23.41 ?  441 GLU A CA    1 
ATOM   3546  C  C     . GLU A 1 441 ? 126.418 160.404 107.748 1.00 30.31 ?  441 GLU A C     1 
ATOM   3547  O  O     . GLU A 1 441 ? 126.225 161.145 108.719 1.00 38.74 ?  441 GLU A O     1 
ATOM   3548  C  CB    . GLU A 1 441 ? 127.607 161.543 105.867 1.00 25.90 ?  441 GLU A CB    1 
ATOM   3549  C  CG    . GLU A 1 441 ? 128.935 162.014 105.306 1.00 29.16 ?  441 GLU A CG    1 
ATOM   3550  C  CD    . GLU A 1 441 ? 128.810 162.534 103.888 1.00 36.38 ?  441 GLU A CD    1 
ATOM   3551  O  OE1   . GLU A 1 441 ? 127.784 162.246 103.236 1.00 34.67 ?  441 GLU A OE1   1 
ATOM   3552  O  OE2   . GLU A 1 441 ? 129.736 163.233 103.425 1.00 36.67 -1 441 GLU A OE2   1 
ATOM   3553  N  N     . THR A 1 442 ? 125.513 159.518 107.342 1.00 30.88 ?  442 THR A N     1 
ATOM   3554  C  CA    . THR A 1 442 ? 124.229 159.369 108.015 1.00 29.96 ?  442 THR A CA    1 
ATOM   3555  C  C     . THR A 1 442 ? 124.283 158.397 109.186 1.00 30.74 ?  442 THR A C     1 
ATOM   3556  O  O     . THR A 1 442 ? 123.251 158.164 109.824 1.00 38.69 ?  442 THR A O     1 
ATOM   3557  C  CB    . THR A 1 442 ? 123.155 158.913 107.023 1.00 29.97 ?  442 THR A CB    1 
ATOM   3558  O  OG1   . THR A 1 442 ? 123.601 157.736 106.338 1.00 33.39 ?  442 THR A OG1   1 
ATOM   3559  C  CG2   . THR A 1 442 ? 122.865 160.008 106.011 1.00 29.67 ?  442 THR A CG2   1 
ATOM   3560  N  N     . THR A 1 443 ? 125.447 157.829 109.482 1.00 29.39 ?  443 THR A N     1 
ATOM   3561  C  CA    . THR A 1 443 ? 125.600 156.932 110.618 1.00 32.14 ?  443 THR A CA    1 
ATOM   3562  C  C     . THR A 1 443 ? 125.961 157.738 111.858 1.00 37.04 ?  443 THR A C     1 
ATOM   3563  O  O     . THR A 1 443 ? 126.932 158.502 111.848 1.00 39.75 ?  443 THR A O     1 
ATOM   3564  C  CB    . THR A 1 443 ? 126.673 155.879 110.340 1.00 32.36 ?  443 THR A CB    1 
ATOM   3565  O  OG1   . THR A 1 443 ? 126.240 155.024 109.274 1.00 36.65 ?  443 THR A OG1   1 
ATOM   3566  C  CG2   . THR A 1 443 ? 126.930 155.041 111.581 1.00 26.65 ?  443 THR A CG2   1 
ATOM   3567  N  N     . ASP A 1 444 ? 125.177 157.567 112.920 1.00 43.45 ?  444 ASP A N     1 
ATOM   3568  C  CA    . ASP A 1 444 ? 125.395 158.278 114.180 1.00 42.13 ?  444 ASP A CA    1 
ATOM   3569  C  C     . ASP A 1 444 ? 125.114 157.300 115.316 1.00 41.49 ?  444 ASP A C     1 
ATOM   3570  O  O     . ASP A 1 444 ? 123.953 157.010 115.620 1.00 42.15 ?  444 ASP A O     1 
ATOM   3571  C  CB    . ASP A 1 444 ? 124.511 159.515 114.277 1.00 43.52 ?  444 ASP A CB    1 
ATOM   3572  C  CG    . ASP A 1 444 ? 125.281 160.748 114.705 1.00 47.76 ?  444 ASP A CG    1 
ATOM   3573  O  OD1   . ASP A 1 444 ? 126.527 160.685 114.754 1.00 46.38 ?  444 ASP A OD1   1 
ATOM   3574  O  OD2   . ASP A 1 444 ? 124.639 161.781 114.989 1.00 47.26 -1 444 ASP A OD2   1 
ATOM   3575  N  N     . ILE A 1 445 ? 126.175 156.801 115.941 1.00 34.72 ?  445 ILE A N     1 
ATOM   3576  C  CA    . ILE A 1 445 ? 126.072 155.835 117.026 1.00 37.80 ?  445 ILE A CA    1 
ATOM   3577  C  C     . ILE A 1 445 ? 126.337 156.563 118.336 1.00 38.51 ?  445 ILE A C     1 
ATOM   3578  O  O     . ILE A 1 445 ? 127.434 157.092 118.553 1.00 39.84 ?  445 ILE A O     1 
ATOM   3579  C  CB    . ILE A 1 445 ? 127.047 154.665 116.830 1.00 36.80 ?  445 ILE A CB    1 
ATOM   3580  C  CG1   . ILE A 1 445 ? 126.685 153.894 115.560 1.00 34.86 ?  445 ILE A CG1   1 
ATOM   3581  C  CG2   . ILE A 1 445 ? 127.025 153.746 118.037 1.00 37.90 ?  445 ILE A CG2   1 
ATOM   3582  C  CD1   . ILE A 1 445 ? 127.721 152.891 115.140 1.00 34.17 ?  445 ILE A CD1   1 
ATOM   3583  N  N     . ARG A 1 446 ? 125.333 156.590 119.208 1.00 40.85 ?  446 ARG A N     1 
ATOM   3584  C  CA    . ARG A 1 446 ? 125.374 157.381 120.429 1.00 46.28 ?  446 ARG A CA    1 
ATOM   3585  C  C     . ARG A 1 446 ? 125.890 156.604 121.633 1.00 44.95 ?  446 ARG A C     1 
ATOM   3586  O  O     . ARG A 1 446 ? 125.949 157.165 122.732 1.00 41.08 ?  446 ARG A O     1 
ATOM   3587  C  CB    . ARG A 1 446 ? 123.979 157.939 120.737 1.00 44.76 ?  446 ARG A CB    1 
ATOM   3588  C  CG    . ARG A 1 446 ? 123.066 158.041 119.524 1.00 43.05 ?  446 ARG A CG    1 
ATOM   3589  C  CD    . ARG A 1 446 ? 123.519 159.132 118.560 1.00 45.48 ?  446 ARG A CD    1 
ATOM   3590  N  NE    . ARG A 1 446 ? 123.104 160.461 118.992 1.00 47.02 ?  446 ARG A NE    1 
ATOM   3591  C  CZ    . ARG A 1 446 ? 121.871 160.936 118.872 1.00 47.76 ?  446 ARG A CZ    1 
ATOM   3592  N  NH1   . ARG A 1 446 ? 120.899 160.212 118.342 1.00 43.40 1  446 ARG A NH1   1 
ATOM   3593  N  NH2   . ARG A 1 446 ? 121.609 162.170 119.292 1.00 47.17 ?  446 ARG A NH2   1 
ATOM   3594  N  N     . ASN A 1 447 ? 126.262 155.337 121.459 1.00 34.40 ?  447 ASN A N     1 
ATOM   3595  C  CA    . ASN A 1 447 ? 126.780 154.524 122.548 1.00 29.03 ?  447 ASN A CA    1 
ATOM   3596  C  C     . ASN A 1 447 ? 128.197 154.030 122.302 1.00 32.18 ?  447 ASN A C     1 
ATOM   3597  O  O     . ASN A 1 447 ? 128.754 153.338 123.160 1.00 35.53 ?  447 ASN A O     1 
ATOM   3598  C  CB    . ASN A 1 447 ? 125.855 153.328 122.803 1.00 32.55 ?  447 ASN A CB    1 
ATOM   3599  C  CG    . ASN A 1 447 ? 124.759 153.642 123.797 1.00 29.77 ?  447 ASN A CG    1 
ATOM   3600  O  OD1   . ASN A 1 447 ? 124.949 154.438 124.715 1.00 28.36 ?  447 ASN A OD1   1 
ATOM   3601  N  ND2   . ASN A 1 447 ? 123.600 153.025 123.612 1.00 32.26 ?  447 ASN A ND2   1 
ATOM   3602  N  N     . ALA A 1 448 ? 128.791 154.361 121.156 1.00 34.16 ?  448 ALA A N     1 
ATOM   3603  C  CA    . ALA A 1 448 ? 130.179 154.030 120.839 1.00 29.31 ?  448 ALA A CA    1 
ATOM   3604  C  C     . ALA A 1 448 ? 130.893 155.334 120.514 1.00 29.15 ?  448 ALA A C     1 
ATOM   3605  O  O     . ALA A 1 448 ? 130.876 155.791 119.359 1.00 29.10 ?  448 ALA A O     1 
ATOM   3606  C  CB    . ALA A 1 448 ? 130.263 153.040 119.682 1.00 24.41 ?  448 ALA A CB    1 
ATOM   3607  N  N     . PRO A 1 449 ? 131.526 155.974 121.501 1.00 28.77 ?  449 PRO A N     1 
ATOM   3608  C  CA    . PRO A 1 449 ? 132.105 157.304 121.244 1.00 22.93 ?  449 PRO A CA    1 
ATOM   3609  C  C     . PRO A 1 449 ? 133.263 157.274 120.267 1.00 27.34 ?  449 PRO A C     1 
ATOM   3610  O  O     . PRO A 1 449 ? 133.344 158.137 119.383 1.00 22.25 ?  449 PRO A O     1 
ATOM   3611  C  CB    . PRO A 1 449 ? 132.552 157.772 122.639 1.00 19.14 ?  449 PRO A CB    1 
ATOM   3612  C  CG    . PRO A 1 449 ? 131.990 156.778 123.610 1.00 25.18 ?  449 PRO A CG    1 
ATOM   3613  C  CD    . PRO A 1 449 ? 131.788 155.508 122.870 1.00 23.69 ?  449 PRO A CD    1 
ATOM   3614  N  N     . ALA A 1 450 ? 134.167 156.300 120.396 1.00 25.81 ?  450 ALA A N     1 
ATOM   3615  C  CA    . ALA A 1 450 ? 135.309 156.233 119.493 1.00 16.45 ?  450 ALA A CA    1 
ATOM   3616  C  C     . ALA A 1 450 ? 134.890 155.819 118.088 1.00 22.90 ?  450 ALA A C     1 
ATOM   3617  O  O     . ALA A 1 450 ? 135.459 156.309 117.109 1.00 26.91 ?  450 ALA A O     1 
ATOM   3618  C  CB    . ALA A 1 450 ? 136.362 155.275 120.046 1.00 19.28 ?  450 ALA A CB    1 
ATOM   3619  N  N     . VAL A 1 451 ? 133.891 154.941 117.968 1.00 28.04 ?  451 VAL A N     1 
ATOM   3620  C  CA    . VAL A 1 451 ? 133.378 154.572 116.651 1.00 18.02 ?  451 VAL A CA    1 
ATOM   3621  C  C     . VAL A 1 451 ? 132.796 155.794 115.951 1.00 21.83 ?  451 VAL A C     1 
ATOM   3622  O  O     . VAL A 1 451 ? 133.066 156.046 114.773 1.00 30.56 ?  451 VAL A O     1 
ATOM   3623  C  CB    . VAL A 1 451 ? 132.337 153.445 116.774 1.00 21.98 ?  451 VAL A CB    1 
ATOM   3624  C  CG1   . VAL A 1 451 ? 131.504 153.342 115.507 1.00 23.76 ?  451 VAL A CG1   1 
ATOM   3625  C  CG2   . VAL A 1 451 ? 133.014 152.121 117.075 1.00 22.51 ?  451 VAL A CG2   1 
ATOM   3626  N  N     . ARG A 1 452 ? 131.991 156.576 116.675 1.00 20.50 ?  452 ARG A N     1 
ATOM   3627  C  CA    . ARG A 1 452 ? 131.399 157.776 116.096 1.00 22.77 ?  452 ARG A CA    1 
ATOM   3628  C  C     . ARG A 1 452 ? 132.466 158.801 115.729 1.00 23.83 ?  452 ARG A C     1 
ATOM   3629  O  O     . ARG A 1 452 ? 132.407 159.418 114.656 1.00 33.52 ?  452 ARG A O     1 
ATOM   3630  C  CB    . ARG A 1 452 ? 130.389 158.376 117.073 1.00 21.08 ?  452 ARG A CB    1 
ATOM   3631  C  CG    . ARG A 1 452 ? 129.895 159.759 116.703 1.00 26.53 ?  452 ARG A CG    1 
ATOM   3632  C  CD    . ARG A 1 452 ? 128.835 160.233 117.680 1.00 27.26 ?  452 ARG A CD    1 
ATOM   3633  N  NE    . ARG A 1 452 ? 129.232 159.992 119.062 1.00 38.94 ?  452 ARG A NE    1 
ATOM   3634  C  CZ    . ARG A 1 452 ? 128.487 160.285 120.118 1.00 41.10 ?  452 ARG A CZ    1 
ATOM   3635  N  NH1   . ARG A 1 452 ? 127.287 160.829 119.990 1.00 34.44 1  452 ARG A NH1   1 
ATOM   3636  N  NH2   . ARG A 1 452 ? 128.956 160.024 121.336 1.00 29.62 ?  452 ARG A NH2   1 
ATOM   3637  N  N     . ARG A 1 453 ? 133.454 158.994 116.606 1.00 21.78 ?  453 ARG A N     1 
ATOM   3638  C  CA    . ARG A 1 453 ? 134.511 159.960 116.328 1.00 20.91 ?  453 ARG A CA    1 
ATOM   3639  C  C     . ARG A 1 453 ? 135.324 159.552 115.107 1.00 25.75 ?  453 ARG A C     1 
ATOM   3640  O  O     . ARG A 1 453 ? 135.644 160.390 114.257 1.00 29.91 ?  453 ARG A O     1 
ATOM   3641  C  CB    . ARG A 1 453 ? 135.415 160.117 117.552 1.00 20.33 ?  453 ARG A CB    1 
ATOM   3642  C  CG    . ARG A 1 453 ? 136.763 160.747 117.250 1.00 23.78 ?  453 ARG A CG    1 
ATOM   3643  C  CD    . ARG A 1 453 ? 137.386 161.366 118.490 1.00 21.86 ?  453 ARG A CD    1 
ATOM   3644  N  NE    . ARG A 1 453 ? 138.715 160.828 118.753 1.00 21.77 ?  453 ARG A NE    1 
ATOM   3645  C  CZ    . ARG A 1 453 ? 139.831 161.291 118.207 1.00 23.79 ?  453 ARG A CZ    1 
ATOM   3646  N  NH1   . ARG A 1 453 ? 139.817 162.304 117.357 1.00 24.12 1  453 ARG A NH1   1 
ATOM   3647  N  NH2   . ARG A 1 453 ? 140.991 160.721 118.519 1.00 25.71 ?  453 ARG A NH2   1 
ATOM   3648  N  N     . ALA A 1 454 ? 135.654 158.263 114.992 1.00 23.64 ?  454 ALA A N     1 
ATOM   3649  C  CA    . ALA A 1 454 ? 136.418 157.797 113.843 1.00 18.39 ?  454 ALA A CA    1 
ATOM   3650  C  C     . ALA A 1 454 ? 135.590 157.820 112.566 1.00 18.15 ?  454 ALA A C     1 
ATOM   3651  O  O     . ALA A 1 454 ? 136.138 158.040 111.483 1.00 23.75 ?  454 ALA A O     1 
ATOM   3652  C  CB    . ALA A 1 454 ? 136.957 156.393 114.102 1.00 20.65 ?  454 ALA A CB    1 
ATOM   3653  N  N     . ASN A 1 455 ? 134.279 157.595 112.663 1.00 20.68 ?  455 ASN A N     1 
ATOM   3654  C  CA    . ASN A 1 455 ? 133.431 157.726 111.484 1.00 21.99 ?  455 ASN A CA    1 
ATOM   3655  C  C     . ASN A 1 455 ? 133.381 159.171 111.006 1.00 25.45 ?  455 ASN A C     1 
ATOM   3656  O  O     . ASN A 1 455 ? 133.424 159.434 109.799 1.00 30.27 ?  455 ASN A O     1 
ATOM   3657  C  CB    . ASN A 1 455 ? 132.026 157.207 111.785 1.00 19.31 ?  455 ASN A CB    1 
ATOM   3658  C  CG    . ASN A 1 455 ? 131.113 157.267 110.578 1.00 27.04 ?  455 ASN A CG    1 
ATOM   3659  O  OD1   . ASN A 1 455 ? 131.410 156.690 109.532 1.00 31.25 ?  455 ASN A OD1   1 
ATOM   3660  N  ND2   . ASN A 1 455 ? 129.994 157.967 110.715 1.00 26.78 ?  455 ASN A ND2   1 
ATOM   3661  N  N     . LYS A 1 456 ? 133.289 160.121 111.941 1.00 24.12 ?  456 LYS A N     1 
ATOM   3662  C  CA    . LYS A 1 456 ? 133.274 161.529 111.558 1.00 25.23 ?  456 LYS A CA    1 
ATOM   3663  C  C     . LYS A 1 456 ? 134.620 161.973 110.997 1.00 23.97 ?  456 LYS A C     1 
ATOM   3664  O  O     . LYS A 1 456 ? 134.672 162.752 110.039 1.00 29.54 ?  456 LYS A O     1 
ATOM   3665  C  CB    . LYS A 1 456 ? 132.883 162.394 112.756 1.00 27.55 ?  456 LYS A CB    1 
ATOM   3666  C  CG    . LYS A 1 456 ? 131.442 162.879 112.731 1.00 30.26 ?  456 LYS A CG    1 
ATOM   3667  C  CD    . LYS A 1 456 ? 130.796 162.819 114.112 1.00 33.55 ?  456 LYS A CD    1 
ATOM   3668  C  CE    . LYS A 1 456 ? 131.815 163.026 115.225 1.00 33.77 ?  456 LYS A CE    1 
ATOM   3669  N  NZ    . LYS A 1 456 ? 131.213 162.866 116.577 1.00 31.84 1  456 LYS A NZ    1 
ATOM   3670  N  N     . ALA A 1 457 ? 135.719 161.492 111.581 1.00 19.17 ?  457 ALA A N     1 
ATOM   3671  C  CA    . ALA A 1 457 ? 137.044 161.981 111.214 1.00 17.96 ?  457 ALA A CA    1 
ATOM   3672  C  C     . ALA A 1 457 ? 137.595 161.265 109.985 1.00 24.71 ?  457 ALA A C     1 
ATOM   3673  O  O     . ALA A 1 457 ? 137.903 161.896 108.969 1.00 29.05 ?  457 ALA A O     1 
ATOM   3674  C  CB    . ALA A 1 457 ? 138.000 161.820 112.399 1.00 15.33 ?  457 ALA A CB    1 
ATOM   3675  N  N     . MET A 1 458 ? 137.732 159.943 110.069 1.00 23.82 ?  458 MET A N     1 
ATOM   3676  C  CA    . MET A 1 458 ? 138.365 159.167 109.010 1.00 19.43 ?  458 MET A CA    1 
ATOM   3677  C  C     . MET A 1 458 ? 137.516 159.099 107.747 1.00 23.77 ?  458 MET A C     1 
ATOM   3678  O  O     . MET A 1 458 ? 138.070 159.083 106.642 1.00 30.03 ?  458 MET A O     1 
ATOM   3679  C  CB    . MET A 1 458 ? 138.666 157.757 109.516 1.00 22.61 ?  458 MET A CB    1 
ATOM   3680  C  CG    . MET A 1 458 ? 139.557 157.722 110.746 1.00 14.51 ?  458 MET A CG    1 
ATOM   3681  S  SD    . MET A 1 458 ? 141.240 158.254 110.393 1.00 33.37 ?  458 MET A SD    1 
ATOM   3682  C  CE    . MET A 1 458 ? 142.080 156.674 110.311 1.00 22.54 ?  458 MET A CE    1 
ATOM   3683  N  N     . LYS A 1 459 ? 136.190 159.051 107.887 1.00 18.14 ?  459 LYS A N     1 
ATOM   3684  C  CA    . LYS A 1 459 ? 135.281 158.918 106.747 1.00 21.43 ?  459 LYS A CA    1 
ATOM   3685  C  C     . LYS A 1 459 ? 135.645 157.704 105.897 1.00 21.56 ?  459 LYS A C     1 
ATOM   3686  O  O     . LYS A 1 459 ? 135.598 157.740 104.666 1.00 27.81 ?  459 LYS A O     1 
ATOM   3687  C  CB    . LYS A 1 459 ? 135.263 160.189 105.896 1.00 22.37 ?  459 LYS A CB    1 
ATOM   3688  C  CG    . LYS A 1 459 ? 134.893 161.450 106.652 1.00 24.94 ?  459 LYS A CG    1 
ATOM   3689  C  CD    . LYS A 1 459 ? 135.910 162.550 106.408 1.00 25.12 ?  459 LYS A CD    1 
ATOM   3690  C  CE    . LYS A 1 459 ? 135.290 163.922 106.602 1.00 27.52 ?  459 LYS A CE    1 
ATOM   3691  N  NZ    . LYS A 1 459 ? 134.102 163.871 107.498 1.00 30.30 1  459 LYS A NZ    1 
ATOM   3692  N  N     . SER A 1 460 ? 136.017 156.618 106.566 1.00 20.55 ?  460 SER A N     1 
ATOM   3693  C  CA    . SER A 1 460 ? 136.492 155.430 105.875 1.00 11.16 ?  460 SER A CA    1 
ATOM   3694  C  C     . SER A 1 460 ? 135.323 154.595 105.374 1.00 15.54 ?  460 SER A C     1 
ATOM   3695  O  O     . SER A 1 460 ? 134.346 154.369 106.093 1.00 26.00 ?  460 SER A O     1 
ATOM   3696  C  CB    . SER A 1 460 ? 137.376 154.596 106.799 1.00 13.25 ?  460 SER A CB    1 
ATOM   3697  O  OG    . SER A 1 460 ? 136.646 153.525 107.366 1.00 13.78 ?  460 SER A OG    1 
ATOM   3698  N  N     . ILE A 1 461 ? 135.431 154.140 104.128 1.00 17.07 ?  461 ILE A N     1 
ATOM   3699  C  CA    . ILE A 1 461 ? 134.434 153.285 103.506 1.00 11.44 ?  461 ILE A CA    1 
ATOM   3700  C  C     . ILE A 1 461 ? 135.140 152.056 102.953 1.00 18.03 ?  461 ILE A C     1 
ATOM   3701  O  O     . ILE A 1 461 ? 136.344 152.065 102.696 1.00 18.23 ?  461 ILE A O     1 
ATOM   3702  C  CB    . ILE A 1 461 ? 133.660 154.010 102.385 1.00 13.11 ?  461 ILE A CB    1 
ATOM   3703  C  CG1   . ILE A 1 461 ? 134.626 154.486 101.299 1.00 8.92  ?  461 ILE A CG1   1 
ATOM   3704  C  CG2   . ILE A 1 461 ? 132.871 155.180 102.953 1.00 13.75 ?  461 ILE A CG2   1 
ATOM   3705  C  CD1   . ILE A 1 461 ? 133.947 154.990 100.054 1.00 8.18  ?  461 ILE A CD1   1 
ATOM   3706  N  N     . GLY A 1 462 ? 134.379 150.978 102.800 1.00 17.97 ?  462 GLY A N     1 
ATOM   3707  C  CA    . GLY A 1 462 ? 134.905 149.800 102.146 1.00 8.19  ?  462 GLY A CA    1 
ATOM   3708  C  C     . GLY A 1 462 ? 134.141 149.440 100.892 1.00 5.51  ?  462 GLY A C     1 
ATOM   3709  O  O     . GLY A 1 462 ? 133.006 148.963 100.967 1.00 19.62 ?  462 GLY A O     1 
ATOM   3710  N  N     . LEU A 1 463 ? 134.754 149.644 99.733  1.00 11.37 ?  463 LEU A N     1 
ATOM   3711  C  CA    . LEU A 1 463 ? 134.154 149.284 98.454  1.00 9.14  ?  463 LEU A CA    1 
ATOM   3712  C  C     . LEU A 1 463 ? 134.765 147.965 98.002  1.00 11.19 ?  463 LEU A C     1 
ATOM   3713  O  O     . LEU A 1 463 ? 135.943 147.911 97.637  1.00 20.03 ?  463 LEU A O     1 
ATOM   3714  C  CB    . LEU A 1 463 ? 134.372 150.381 97.417  1.00 18.61 ?  463 LEU A CB    1 
ATOM   3715  C  CG    . LEU A 1 463 ? 133.783 150.118 96.029  1.00 18.85 ?  463 LEU A CG    1 
ATOM   3716  C  CD1   . LEU A 1 463 ? 132.329 149.695 96.137  1.00 9.23  ?  463 LEU A CD1   1 
ATOM   3717  C  CD2   . LEU A 1 463 ? 133.923 151.345 95.146  1.00 15.50 ?  463 LEU A CD2   1 
ATOM   3718  N  N     . GLY A 1 464 ? 133.963 146.901 98.029  1.00 12.27 ?  464 GLY A N     1 
ATOM   3719  C  CA    . GLY A 1 464 ? 134.419 145.583 97.654  1.00 8.91  ?  464 GLY A CA    1 
ATOM   3720  C  C     . GLY A 1 464 ? 133.997 145.194 96.245  1.00 14.99 ?  464 GLY A C     1 
ATOM   3721  O  O     . GLY A 1 464 ? 133.380 145.955 95.504  1.00 21.90 ?  464 GLY A O     1 
ATOM   3722  N  N     . ALA A 1 465 ? 134.358 143.968 95.885  1.00 14.56 ?  465 ALA A N     1 
ATOM   3723  C  CA    . ALA A 1 465 ? 133.995 143.398 94.600  1.00 10.65 ?  465 ALA A CA    1 
ATOM   3724  C  C     . ALA A 1 465 ? 133.568 141.953 94.802  1.00 13.06 ?  465 ALA A C     1 
ATOM   3725  O  O     . ALA A 1 465 ? 133.982 141.296 95.760  1.00 22.50 ?  465 ALA A O     1 
ATOM   3726  C  CB    . ALA A 1 465 ? 135.154 143.473 93.599  1.00 16.40 ?  465 ALA A CB    1 
ATOM   3727  N  N     . MET A 1 466 ? 132.726 141.471 93.894  1.00 13.84 ?  466 MET A N     1 
ATOM   3728  C  CA    . MET A 1 466 ? 132.267 140.093 93.929  1.00 20.15 ?  466 MET A CA    1 
ATOM   3729  C  C     . MET A 1 466 ? 132.064 139.614 92.499  1.00 20.70 ?  466 MET A C     1 
ATOM   3730  O  O     . MET A 1 466 ? 132.201 140.379 91.542  1.00 27.41 ?  466 MET A O     1 
ATOM   3731  C  CB    . MET A 1 466 ? 130.978 139.951 94.743  1.00 25.63 ?  466 MET A CB    1 
ATOM   3732  C  CG    . MET A 1 466 ? 129.799 140.684 94.145  1.00 21.84 ?  466 MET A CG    1 
ATOM   3733  S  SD    . MET A 1 466 ? 128.362 140.709 95.223  1.00 34.17 ?  466 MET A SD    1 
ATOM   3734  C  CE    . MET A 1 466 ? 127.358 141.908 94.362  1.00 25.31 ?  466 MET A CE    1 
ATOM   3735  N  N     . ASN A 1 467 ? 131.736 138.328 92.370  1.00 13.45 ?  467 ASN A N     1 
ATOM   3736  C  CA    . ASN A 1 467 ? 131.534 137.676 91.076  1.00 16.31 ?  467 ASN A CA    1 
ATOM   3737  C  C     . ASN A 1 467 ? 132.807 137.671 90.238  1.00 18.38 ?  467 ASN A C     1 
ATOM   3738  O  O     . ASN A 1 467 ? 132.749 137.693 89.007  1.00 23.98 ?  467 ASN A O     1 
ATOM   3739  C  CB    . ASN A 1 467 ? 130.387 138.322 90.291  1.00 20.54 ?  467 ASN A CB    1 
ATOM   3740  C  CG    . ASN A 1 467 ? 129.560 137.307 89.531  1.00 23.54 ?  467 ASN A CG    1 
ATOM   3741  O  OD1   . ASN A 1 467 ? 129.755 136.101 89.671  1.00 31.27 ?  467 ASN A OD1   1 
ATOM   3742  N  ND2   . ASN A 1 467 ? 128.628 137.792 88.721  1.00 23.37 ?  467 ASN A ND2   1 
ATOM   3743  N  N     . LEU A 1 468 ? 133.968 137.648 90.893  1.00 18.69 ?  468 LEU A N     1 
ATOM   3744  C  CA    . LEU A 1 468 ? 135.221 137.535 90.156  1.00 13.32 ?  468 LEU A CA    1 
ATOM   3745  C  C     . LEU A 1 468 ? 135.334 136.175 89.483  1.00 20.58 ?  468 LEU A C     1 
ATOM   3746  O  O     . LEU A 1 468 ? 135.592 136.085 88.277  1.00 21.33 ?  468 LEU A O     1 
ATOM   3747  C  CB    . LEU A 1 468 ? 136.408 137.769 91.090  1.00 22.42 ?  468 LEU A CB    1 
ATOM   3748  C  CG    . LEU A 1 468 ? 137.788 137.485 90.495  1.00 19.10 ?  468 LEU A CG    1 
ATOM   3749  C  CD1   . LEU A 1 468 ? 138.141 138.510 89.431  1.00 16.67 ?  468 LEU A CD1   1 
ATOM   3750  C  CD2   . LEU A 1 468 ? 138.847 137.444 91.580  1.00 14.68 ?  468 LEU A CD2   1 
ATOM   3751  N  N     . HIS A 1 469 ? 135.120 135.103 90.247  1.00 25.22 ?  469 HIS A N     1 
ATOM   3752  C  CA    . HIS A 1 469 ? 135.187 133.767 89.671  1.00 16.21 ?  469 HIS A CA    1 
ATOM   3753  C  C     . HIS A 1 469 ? 134.053 133.538 88.685  1.00 25.21 ?  469 HIS A C     1 
ATOM   3754  O  O     . HIS A 1 469 ? 134.246 132.887 87.655  1.00 33.67 ?  469 HIS A O     1 
ATOM   3755  C  CB    . HIS A 1 469 ? 135.160 132.706 90.769  1.00 17.64 ?  469 HIS A CB    1 
ATOM   3756  C  CG    . HIS A 1 469 ? 135.528 131.338 90.286  1.00 22.56 ?  469 HIS A CG    1 
ATOM   3757  N  ND1   . HIS A 1 469 ? 135.386 130.210 91.062  1.00 27.87 ?  469 HIS A ND1   1 
ATOM   3758  C  CD2   . HIS A 1 469 ? 136.035 130.919 89.102  1.00 23.49 ?  469 HIS A CD2   1 
ATOM   3759  C  CE1   . HIS A 1 469 ? 135.788 129.154 90.378  1.00 23.94 ?  469 HIS A CE1   1 
ATOM   3760  N  NE2   . HIS A 1 469 ? 136.186 129.557 89.186  1.00 28.10 ?  469 HIS A NE2   1 
ATOM   3761  N  N     . GLY A 1 470 ? 132.862 134.056 88.984  1.00 24.88 ?  470 GLY A N     1 
ATOM   3762  C  CA    . GLY A 1 470 ? 131.772 133.957 88.029  1.00 20.72 ?  470 GLY A CA    1 
ATOM   3763  C  C     . GLY A 1 470 ? 132.104 134.632 86.713  1.00 18.09 ?  470 GLY A C     1 
ATOM   3764  O  O     . GLY A 1 470 ? 131.915 134.055 85.640  1.00 35.24 ?  470 GLY A O     1 
ATOM   3765  N  N     . TYR A 1 471 ? 132.633 135.855 86.782  1.00 17.42 ?  471 TYR A N     1 
ATOM   3766  C  CA    . TYR A 1 471 ? 132.993 136.570 85.563  1.00 21.95 ?  471 TYR A CA    1 
ATOM   3767  C  C     . TYR A 1 471 ? 134.078 135.826 84.792  1.00 25.73 ?  471 TYR A C     1 
ATOM   3768  O  O     . TYR A 1 471 ? 134.020 135.721 83.562  1.00 28.80 ?  471 TYR A O     1 
ATOM   3769  C  CB    . TYR A 1 471 ? 133.460 137.988 85.890  1.00 22.09 ?  471 TYR A CB    1 
ATOM   3770  C  CG    . TYR A 1 471 ? 134.005 138.708 84.681  1.00 19.48 ?  471 TYR A CG    1 
ATOM   3771  C  CD1   . TYR A 1 471 ? 133.146 139.289 83.756  1.00 23.38 ?  471 TYR A CD1   1 
ATOM   3772  C  CD2   . TYR A 1 471 ? 135.370 138.779 84.440  1.00 18.44 ?  471 TYR A CD2   1 
ATOM   3773  C  CE1   . TYR A 1 471 ? 133.631 139.937 82.642  1.00 25.73 ?  471 TYR A CE1   1 
ATOM   3774  C  CE2   . TYR A 1 471 ? 135.864 139.423 83.323  1.00 22.96 ?  471 TYR A CE2   1 
ATOM   3775  C  CZ    . TYR A 1 471 ? 134.989 140.000 82.429  1.00 25.21 ?  471 TYR A CZ    1 
ATOM   3776  O  OH    . TYR A 1 471 ? 135.472 140.642 81.315  1.00 31.66 ?  471 TYR A OH    1 
ATOM   3777  N  N     . LEU A 1 472 ? 135.089 135.320 85.501  1.00 27.82 ?  472 LEU A N     1 
ATOM   3778  C  CA    . LEU A 1 472 ? 136.184 134.622 84.833  1.00 24.74 ?  472 LEU A CA    1 
ATOM   3779  C  C     . LEU A 1 472 ? 135.710 133.321 84.193  1.00 27.35 ?  472 LEU A C     1 
ATOM   3780  O  O     . LEU A 1 472 ? 136.139 132.978 83.087  1.00 32.46 ?  472 LEU A O     1 
ATOM   3781  C  CB    . LEU A 1 472 ? 137.319 134.356 85.823  1.00 25.71 ?  472 LEU A CB    1 
ATOM   3782  C  CG    . LEU A 1 472 ? 138.066 135.583 86.349  1.00 24.59 ?  472 LEU A CG    1 
ATOM   3783  C  CD1   . LEU A 1 472 ? 138.924 135.216 87.549  1.00 23.05 ?  472 LEU A CD1   1 
ATOM   3784  C  CD2   . LEU A 1 472 ? 138.912 136.206 85.251  1.00 23.35 ?  472 LEU A CD2   1 
ATOM   3785  N  N     . ALA A 1 473 ? 134.834 132.582 84.876  1.00 26.73 ?  473 ALA A N     1 
ATOM   3786  C  CA    . ALA A 1 473 ? 134.357 131.312 84.344  1.00 24.56 ?  473 ALA A CA    1 
ATOM   3787  C  C     . ALA A 1 473 ? 133.424 131.518 83.156  1.00 35.21 ?  473 ALA A C     1 
ATOM   3788  O  O     . ALA A 1 473 ? 133.490 130.768 82.176  1.00 42.98 ?  473 ALA A O     1 
ATOM   3789  C  CB    . ALA A 1 473 ? 133.662 130.515 85.446  1.00 27.08 ?  473 ALA A CB    1 
ATOM   3790  N  N     . GLN A 1 474 ? 132.552 132.528 83.220  1.00 29.14 ?  474 GLN A N     1 
ATOM   3791  C  CA    . GLN A 1 474 ? 131.683 132.822 82.086  1.00 29.13 ?  474 GLN A CA    1 
ATOM   3792  C  C     . GLN A 1 474 ? 132.432 133.436 80.911  1.00 32.16 ?  474 GLN A C     1 
ATOM   3793  O  O     . GLN A 1 474 ? 131.842 133.588 79.836  1.00 36.34 ?  474 GLN A O     1 
ATOM   3794  C  CB    . GLN A 1 474 ? 130.542 133.747 82.508  1.00 28.84 ?  474 GLN A CB    1 
ATOM   3795  C  CG    . GLN A 1 474 ? 129.742 133.253 83.697  1.00 30.82 ?  474 GLN A CG    1 
ATOM   3796  C  CD    . GLN A 1 474 ? 128.322 133.773 83.696  1.00 32.74 ?  474 GLN A CD    1 
ATOM   3797  O  OE1   . GLN A 1 474 ? 127.680 133.854 82.649  1.00 37.49 ?  474 GLN A OE1   1 
ATOM   3798  N  NE2   . GLN A 1 474 ? 127.822 134.133 84.872  1.00 31.46 ?  474 GLN A NE2   1 
ATOM   3799  N  N     . ASN A 1 475 ? 133.705 133.793 81.084  1.00 33.08 ?  475 ASN A N     1 
ATOM   3800  C  CA    . ASN A 1 475 ? 134.529 134.317 80.004  1.00 35.90 ?  475 ASN A CA    1 
ATOM   3801  C  C     . ASN A 1 475 ? 135.629 133.344 79.596  1.00 35.04 ?  475 ASN A C     1 
ATOM   3802  O  O     . ASN A 1 475 ? 136.577 133.736 78.909  1.00 33.44 ?  475 ASN A O     1 
ATOM   3803  C  CB    . ASN A 1 475 ? 135.127 135.665 80.404  1.00 32.28 ?  475 ASN A CB    1 
ATOM   3804  C  CG    . ASN A 1 475 ? 134.109 136.784 80.371  1.00 31.54 ?  475 ASN A CG    1 
ATOM   3805  O  OD1   . ASN A 1 475 ? 133.921 137.438 79.345  1.00 33.91 ?  475 ASN A OD1   1 
ATOM   3806  N  ND2   . ASN A 1 475 ? 133.433 136.999 81.491  1.00 29.10 ?  475 ASN A ND2   1 
ATOM   3807  N  N     . GLY A 1 476 ? 135.515 132.083 80.002  1.00 29.82 ?  476 GLY A N     1 
ATOM   3808  C  CA    . GLY A 1 476 ? 136.498 131.077 79.628  1.00 29.15 ?  476 GLY A CA    1 
ATOM   3809  C  C     . GLY A 1 476 ? 137.881 131.323 80.189  1.00 35.07 ?  476 GLY A C     1 
ATOM   3810  O  O     . GLY A 1 476 ? 138.876 131.156 79.474  1.00 37.01 ?  476 GLY A O     1 
ATOM   3811  N  N     . ILE A 1 477 ? 137.968 131.719 81.456  1.00 31.50 ?  477 ILE A N     1 
ATOM   3812  C  CA    . ILE A 1 477 ? 139.240 131.984 82.114  1.00 26.83 ?  477 ILE A CA    1 
ATOM   3813  C  C     . ILE A 1 477 ? 139.281 131.213 83.425  1.00 31.18 ?  477 ILE A C     1 
ATOM   3814  O  O     . ILE A 1 477 ? 138.382 131.353 84.261  1.00 34.93 ?  477 ILE A O     1 
ATOM   3815  C  CB    . ILE A 1 477 ? 139.452 133.489 82.368  1.00 27.36 ?  477 ILE A CB    1 
ATOM   3816  C  CG1   . ILE A 1 477 ? 139.504 134.248 81.043  1.00 30.88 ?  477 ILE A CG1   1 
ATOM   3817  C  CG2   . ILE A 1 477 ? 140.726 133.719 83.157  1.00 28.51 ?  477 ILE A CG2   1 
ATOM   3818  C  CD1   . ILE A 1 477 ? 139.300 135.730 81.190  1.00 30.35 ?  477 ILE A CD1   1 
ATOM   3819  N  N     . ALA A 1 478 ? 140.319 130.402 83.601  1.00 31.04 ?  478 ALA A N     1 
ATOM   3820  C  CA    . ALA A 1 478 ? 140.499 129.678 84.851  1.00 27.78 ?  478 ALA A CA    1 
ATOM   3821  C  C     . ALA A 1 478 ? 140.930 130.634 85.955  1.00 30.47 ?  478 ALA A C     1 
ATOM   3822  O  O     . ALA A 1 478 ? 141.726 131.549 85.729  1.00 31.20 ?  478 ALA A O     1 
ATOM   3823  C  CB    . ALA A 1 478 ? 141.535 128.568 84.680  1.00 28.28 ?  478 ALA A CB    1 
ATOM   3824  N  N     . TYR A 1 479 ? 140.397 130.414 87.160  1.00 29.75 ?  479 TYR A N     1 
ATOM   3825  C  CA    . TYR A 1 479 ? 140.705 131.294 88.283  1.00 22.93 ?  479 TYR A CA    1 
ATOM   3826  C  C     . TYR A 1 479 ? 142.190 131.286 88.617  1.00 27.34 ?  479 TYR A C     1 
ATOM   3827  O  O     . TYR A 1 479 ? 142.733 132.307 89.051  1.00 33.22 ?  479 TYR A O     1 
ATOM   3828  C  CB    . TYR A 1 479 ? 139.878 130.882 89.501  1.00 21.32 ?  479 TYR A CB    1 
ATOM   3829  C  CG    . TYR A 1 479 ? 139.987 131.811 90.691  1.00 28.50 ?  479 TYR A CG    1 
ATOM   3830  C  CD1   . TYR A 1 479 ? 140.967 131.623 91.658  1.00 26.50 ?  479 TYR A CD1   1 
ATOM   3831  C  CD2   . TYR A 1 479 ? 139.099 132.864 90.856  1.00 22.04 ?  479 TYR A CD2   1 
ATOM   3832  C  CE1   . TYR A 1 479 ? 141.066 132.463 92.747  1.00 22.41 ?  479 TYR A CE1   1 
ATOM   3833  C  CE2   . TYR A 1 479 ? 139.190 133.709 91.944  1.00 22.90 ?  479 TYR A CE2   1 
ATOM   3834  C  CZ    . TYR A 1 479 ? 140.174 133.505 92.885  1.00 29.54 ?  479 TYR A CZ    1 
ATOM   3835  O  OH    . TYR A 1 479 ? 140.266 134.346 93.970  1.00 31.36 ?  479 TYR A OH    1 
ATOM   3836  N  N     . GLU A 1 480 ? 142.862 130.156 88.422  1.00 30.91 ?  480 GLU A N     1 
ATOM   3837  C  CA    . GLU A 1 480 ? 144.283 130.039 88.716  1.00 29.89 ?  480 GLU A CA    1 
ATOM   3838  C  C     . GLU A 1 480 ? 145.170 130.430 87.543  1.00 32.47 ?  480 GLU A C     1 
ATOM   3839  O  O     . GLU A 1 480 ? 146.397 130.416 87.683  1.00 37.66 ?  480 GLU A O     1 
ATOM   3840  C  CB    . GLU A 1 480 ? 144.615 128.609 89.144  1.00 29.48 ?  480 GLU A CB    1 
ATOM   3841  C  CG    . GLU A 1 480 ? 143.816 128.105 90.327  1.00 30.62 ?  480 GLU A CG    1 
ATOM   3842  C  CD    . GLU A 1 480 ? 143.672 126.598 90.317  1.00 37.66 ?  480 GLU A CD    1 
ATOM   3843  O  OE1   . GLU A 1 480 ? 142.805 126.089 89.577  1.00 38.85 ?  480 GLU A OE1   1 
ATOM   3844  O  OE2   . GLU A 1 480 ? 144.430 125.923 91.044  1.00 38.05 -1 480 GLU A OE2   1 
ATOM   3845  N  N     . SER A 1 481 ? 144.589 130.774 86.399  1.00 30.10 ?  481 SER A N     1 
ATOM   3846  C  CA    . SER A 1 481 ? 145.385 131.098 85.229  1.00 27.49 ?  481 SER A CA    1 
ATOM   3847  C  C     . SER A 1 481 ? 146.056 132.462 85.393  1.00 31.91 ?  481 SER A C     1 
ATOM   3848  O  O     . SER A 1 481 ? 145.545 133.334 86.099  1.00 32.24 ?  481 SER A O     1 
ATOM   3849  C  CB    . SER A 1 481 ? 144.515 131.097 83.977  1.00 29.10 ?  481 SER A CB    1 
ATOM   3850  O  OG    . SER A 1 481 ? 143.900 132.357 83.784  1.00 33.68 ?  481 SER A OG    1 
ATOM   3851  N  N     . PRO A 1 482 ? 147.214 132.663 84.757  1.00 37.78 ?  482 PRO A N     1 
ATOM   3852  C  CA    . PRO A 1 482 ? 147.825 134.003 84.767  1.00 30.91 ?  482 PRO A CA    1 
ATOM   3853  C  C     . PRO A 1 482 ? 146.947 135.062 84.127  1.00 29.86 ?  482 PRO A C     1 
ATOM   3854  O  O     . PRO A 1 482 ? 147.058 136.242 84.480  1.00 34.98 ?  482 PRO A O     1 
ATOM   3855  C  CB    . PRO A 1 482 ? 149.129 133.799 83.986  1.00 30.41 ?  482 PRO A CB    1 
ATOM   3856  C  CG    . PRO A 1 482 ? 149.405 132.336 84.072  1.00 32.89 ?  482 PRO A CG    1 
ATOM   3857  C  CD    . PRO A 1 482 ? 148.065 131.672 84.082  1.00 31.72 ?  482 PRO A CD    1 
ATOM   3858  N  N     . GLU A 1 483 ? 146.081 134.676 83.187  1.00 36.10 ?  483 GLU A N     1 
ATOM   3859  C  CA    . GLU A 1 483 ? 145.153 135.632 82.591  1.00 32.70 ?  483 GLU A CA    1 
ATOM   3860  C  C     . GLU A 1 483 ? 144.157 136.150 83.620  1.00 31.18 ?  483 GLU A C     1 
ATOM   3861  O  O     . GLU A 1 483 ? 143.793 137.332 83.599  1.00 35.55 ?  483 GLU A O     1 
ATOM   3862  C  CB    . GLU A 1 483 ? 144.421 134.989 81.413  1.00 33.67 ?  483 GLU A CB    1 
ATOM   3863  C  CG    . GLU A 1 483 ? 145.277 134.814 80.172  1.00 36.84 ?  483 GLU A CG    1 
ATOM   3864  C  CD    . GLU A 1 483 ? 146.044 133.506 80.169  1.00 39.71 ?  483 GLU A CD    1 
ATOM   3865  O  OE1   . GLU A 1 483 ? 146.116 132.853 81.232  1.00 37.12 ?  483 GLU A OE1   1 
ATOM   3866  O  OE2   . GLU A 1 483 ? 146.576 133.132 79.105  1.00 41.10 -1 483 GLU A OE2   1 
ATOM   3867  N  N     . ALA A 1 484 ? 143.697 135.279 84.519  1.00 26.19 ?  484 ALA A N     1 
ATOM   3868  C  CA    . ALA A 1 484 ? 142.795 135.720 85.578  1.00 25.77 ?  484 ALA A CA    1 
ATOM   3869  C  C     . ALA A 1 484 ? 143.470 136.733 86.491  1.00 25.99 ?  484 ALA A C     1 
ATOM   3870  O  O     . ALA A 1 484 ? 142.860 137.736 86.879  1.00 25.65 ?  484 ALA A O     1 
ATOM   3871  C  CB    . ALA A 1 484 ? 142.303 134.520 86.383  1.00 20.79 ?  484 ALA A CB    1 
ATOM   3872  N  N     . ARG A 1 485 ? 144.732 136.488 86.850  1.00 27.55 ?  485 ARG A N     1 
ATOM   3873  C  CA    . ARG A 1 485 ? 145.459 137.443 87.677  1.00 21.77 ?  485 ARG A CA    1 
ATOM   3874  C  C     . ARG A 1 485 ? 145.715 138.746 86.932  1.00 22.14 ?  485 ARG A C     1 
ATOM   3875  O  O     . ARG A 1 485 ? 145.675 139.819 87.539  1.00 30.74 ?  485 ARG A O     1 
ATOM   3876  C  CB    . ARG A 1 485 ? 146.774 136.834 88.157  1.00 24.49 ?  485 ARG A CB    1 
ATOM   3877  C  CG    . ARG A 1 485 ? 146.600 135.768 89.221  1.00 25.08 ?  485 ARG A CG    1 
ATOM   3878  C  CD    . ARG A 1 485 ? 147.933 135.367 89.819  1.00 26.67 ?  485 ARG A CD    1 
ATOM   3879  N  NE    . ARG A 1 485 ? 148.831 134.795 88.823  1.00 27.79 ?  485 ARG A NE    1 
ATOM   3880  C  CZ    . ARG A 1 485 ? 148.815 133.525 88.445  1.00 29.59 ?  485 ARG A CZ    1 
ATOM   3881  N  NH1   . ARG A 1 485 ? 147.949 132.663 88.952  1.00 27.74 1  485 ARG A NH1   1 
ATOM   3882  N  NH2   . ARG A 1 485 ? 149.691 133.109 87.535  1.00 25.12 ?  485 ARG A NH2   1 
ATOM   3883  N  N     . ASP A 1 486 ? 145.980 138.672 85.627  1.00 29.60 ?  486 ASP A N     1 
ATOM   3884  C  CA    . ASP A 1 486 ? 146.126 139.881 84.823  1.00 28.93 ?  486 ASP A CA    1 
ATOM   3885  C  C     . ASP A 1 486 ? 144.839 140.699 84.827  1.00 29.97 ?  486 ASP A C     1 
ATOM   3886  O  O     . ASP A 1 486 ? 144.863 141.928 84.993  1.00 35.68 ?  486 ASP A O     1 
ATOM   3887  C  CB    . ASP A 1 486 ? 146.525 139.501 83.399  1.00 33.99 ?  486 ASP A CB    1 
ATOM   3888  C  CG    . ASP A 1 486 ? 146.882 140.700 82.554  1.00 39.53 ?  486 ASP A CG    1 
ATOM   3889  O  OD1   . ASP A 1 486 ? 147.788 141.463 82.948  1.00 38.33 ?  486 ASP A OD1   1 
ATOM   3890  O  OD2   . ASP A 1 486 ? 146.256 140.872 81.488  1.00 40.45 -1 486 ASP A OD2   1 
ATOM   3891  N  N     . PHE A 1 487 ? 143.700 140.027 84.648  1.00 27.52 ?  487 PHE A N     1 
ATOM   3892  C  CA    . PHE A 1 487 ? 142.424 140.727 84.692  1.00 24.06 ?  487 PHE A CA    1 
ATOM   3893  C  C     . PHE A 1 487 ? 142.174 141.337 86.061  1.00 23.48 ?  487 PHE A C     1 
ATOM   3894  O  O     . PHE A 1 487 ? 141.691 142.467 86.160  1.00 28.50 ?  487 PHE A O     1 
ATOM   3895  C  CB    . PHE A 1 487 ? 141.269 139.794 84.333  1.00 23.47 ?  487 PHE A CB    1 
ATOM   3896  C  CG    . PHE A 1 487 ? 139.933 140.335 84.747  1.00 24.82 ?  487 PHE A CG    1 
ATOM   3897  C  CD1   . PHE A 1 487 ? 139.321 141.329 84.005  1.00 22.38 ?  487 PHE A CD1   1 
ATOM   3898  C  CD2   . PHE A 1 487 ? 139.306 139.879 85.895  1.00 24.88 ?  487 PHE A CD2   1 
ATOM   3899  C  CE1   . PHE A 1 487 ? 138.104 141.847 84.388  1.00 24.63 ?  487 PHE A CE1   1 
ATOM   3900  C  CE2   . PHE A 1 487 ? 138.088 140.395 86.282  1.00 25.98 ?  487 PHE A CE2   1 
ATOM   3901  C  CZ    . PHE A 1 487 ? 137.487 141.380 85.528  1.00 24.61 ?  487 PHE A CZ    1 
ATOM   3902  N  N     . ALA A 1 488 ? 142.455 140.589 87.129  1.00 20.43 ?  488 ALA A N     1 
ATOM   3903  C  CA    . ALA A 1 488 ? 142.249 141.122 88.468  1.00 16.31 ?  488 ALA A CA    1 
ATOM   3904  C  C     . ALA A 1 488 ? 143.126 142.340 88.706  1.00 23.39 ?  488 ALA A C     1 
ATOM   3905  O  O     . ALA A 1 488 ? 142.663 143.355 89.240  1.00 28.14 ?  488 ALA A O     1 
ATOM   3906  C  CB    . ALA A 1 488 ? 142.527 140.044 89.514  1.00 22.74 ?  488 ALA A CB    1 
ATOM   3907  N  N     . ASN A 1 489 ? 144.391 142.268 88.284  1.00 25.91 ?  489 ASN A N     1 
ATOM   3908  C  CA    . ASN A 1 489 ? 145.294 143.403 88.406  1.00 21.39 ?  489 ASN A CA    1 
ATOM   3909  C  C     . ASN A 1 489 ? 144.725 144.630 87.711  1.00 20.60 ?  489 ASN A C     1 
ATOM   3910  O  O     . ASN A 1 489 ? 144.596 145.697 88.322  1.00 23.98 ?  489 ASN A O     1 
ATOM   3911  C  CB    . ASN A 1 489 ? 146.659 143.039 87.819  1.00 17.63 ?  489 ASN A CB    1 
ATOM   3912  C  CG    . ASN A 1 489 ? 147.713 144.083 88.097  1.00 25.69 ?  489 ASN A CG    1 
ATOM   3913  O  OD1   . ASN A 1 489 ? 147.824 144.590 89.211  1.00 31.29 ?  489 ASN A OD1   1 
ATOM   3914  N  ND2   . ASN A 1 489 ? 148.503 144.408 87.081  1.00 28.39 ?  489 ASN A ND2   1 
ATOM   3915  N  N     . THR A 1 490 ? 144.346 144.487 86.440  1.00 22.74 ?  490 THR A N     1 
ATOM   3916  C  CA    . THR A 1 490 ? 143.853 145.641 85.694  1.00 21.31 ?  490 THR A CA    1 
ATOM   3917  C  C     . THR A 1 490 ? 142.550 146.169 86.283  1.00 22.67 ?  490 THR A C     1 
ATOM   3918  O  O     . THR A 1 490 ? 142.402 147.377 86.508  1.00 24.89 ?  490 THR A O     1 
ATOM   3919  C  CB    . THR A 1 490 ? 143.668 145.282 84.221  1.00 28.93 ?  490 THR A CB    1 
ATOM   3920  O  OG1   . THR A 1 490 ? 144.869 144.685 83.720  1.00 33.78 ?  490 THR A OG1   1 
ATOM   3921  C  CG2   . THR A 1 490 ? 143.349 146.529 83.414  1.00 22.59 ?  490 THR A CG2   1 
ATOM   3922  N  N     . PHE A 1 491 ? 141.596 145.275 86.552  1.00 19.82 ?  491 PHE A N     1 
ATOM   3923  C  CA    . PHE A 1 491 ? 140.281 145.690 87.025  1.00 17.95 ?  491 PHE A CA    1 
ATOM   3924  C  C     . PHE A 1 491 ? 140.381 146.403 88.364  1.00 22.82 ?  491 PHE A C     1 
ATOM   3925  O  O     . PHE A 1 491 ? 139.782 147.465 88.560  1.00 22.93 ?  491 PHE A O     1 
ATOM   3926  C  CB    . PHE A 1 491 ? 139.358 144.474 87.127  1.00 22.92 ?  491 PHE A CB    1 
ATOM   3927  C  CG    . PHE A 1 491 ? 138.024 144.771 87.756  1.00 19.23 ?  491 PHE A CG    1 
ATOM   3928  C  CD1   . PHE A 1 491 ? 136.968 145.219 86.986  1.00 17.23 ?  491 PHE A CD1   1 
ATOM   3929  C  CD2   . PHE A 1 491 ? 137.826 144.594 89.117  1.00 17.98 ?  491 PHE A CD2   1 
ATOM   3930  C  CE1   . PHE A 1 491 ? 135.743 145.497 87.557  1.00 15.75 ?  491 PHE A CE1   1 
ATOM   3931  C  CE2   . PHE A 1 491 ? 136.604 144.870 89.694  1.00 17.31 ?  491 PHE A CE2   1 
ATOM   3932  C  CZ    . PHE A 1 491 ? 135.561 145.322 88.911  1.00 19.56 ?  491 PHE A CZ    1 
ATOM   3933  N  N     . PHE A 1 492 ? 141.149 145.844 89.299  1.00 23.17 ?  492 PHE A N     1 
ATOM   3934  C  CA    . PHE A 1 492 ? 141.247 146.465 90.608  1.00 12.41 ?  492 PHE A CA    1 
ATOM   3935  C  C     . PHE A 1 492 ? 142.156 147.684 90.609  1.00 14.90 ?  492 PHE A C     1 
ATOM   3936  O  O     . PHE A 1 492 ? 141.969 148.566 91.450  1.00 20.08 ?  492 PHE A O     1 
ATOM   3937  C  CB    . PHE A 1 492 ? 141.702 145.432 91.636  1.00 19.66 ?  492 PHE A CB    1 
ATOM   3938  C  CG    . PHE A 1 492 ? 140.617 144.474 92.032  1.00 16.33 ?  492 PHE A CG    1 
ATOM   3939  C  CD1   . PHE A 1 492 ? 139.637 144.857 92.930  1.00 11.74 ?  492 PHE A CD1   1 
ATOM   3940  C  CD2   . PHE A 1 492 ? 140.555 143.205 91.483  1.00 16.15 ?  492 PHE A CD2   1 
ATOM   3941  C  CE1   . PHE A 1 492 ? 138.631 143.986 93.289  1.00 12.40 ?  492 PHE A CE1   1 
ATOM   3942  C  CE2   . PHE A 1 492 ? 139.548 142.329 91.838  1.00 14.11 ?  492 PHE A CE2   1 
ATOM   3943  C  CZ    . PHE A 1 492 ? 138.586 142.721 92.743  1.00 16.69 ?  492 PHE A CZ    1 
ATOM   3944  N  N     . MET A 1 493 ? 143.093 147.795 89.663  1.00 19.05 ?  493 MET A N     1 
ATOM   3945  C  CA    . MET A 1 493 ? 143.811 149.055 89.527  1.00 16.78 ?  493 MET A CA    1 
ATOM   3946  C  C     . MET A 1 493 ? 142.876 150.151 89.037  1.00 16.20 ?  493 MET A C     1 
ATOM   3947  O  O     . MET A 1 493 ? 142.945 151.285 89.518  1.00 22.30 ?  493 MET A O     1 
ATOM   3948  C  CB    . MET A 1 493 ? 145.026 148.870 88.607  1.00 17.19 ?  493 MET A CB    1 
ATOM   3949  C  CG    . MET A 1 493 ? 145.645 150.109 87.912  1.00 17.53 ?  493 MET A CG    1 
ATOM   3950  S  SD    . MET A 1 493 ? 144.675 151.192 86.836  1.00 32.83 ?  493 MET A SD    1 
ATOM   3951  C  CE    . MET A 1 493 ? 144.639 150.210 85.346  1.00 21.93 ?  493 MET A CE    1 
ATOM   3952  N  N     . MET A 1 494 ? 141.990 149.836 88.084  1.00 20.52 ?  494 MET A N     1 
ATOM   3953  C  CA    . MET A 1 494 ? 140.995 150.825 87.670  1.00 19.50 ?  494 MET A CA    1 
ATOM   3954  C  C     . MET A 1 494 ? 140.040 151.164 88.809  1.00 21.79 ?  494 MET A C     1 
ATOM   3955  O  O     . MET A 1 494 ? 139.649 152.327 88.974  1.00 24.82 ?  494 MET A O     1 
ATOM   3956  C  CB    . MET A 1 494 ? 140.208 150.341 86.451  1.00 17.94 ?  494 MET A CB    1 
ATOM   3957  C  CG    . MET A 1 494 ? 141.042 149.750 85.335  1.00 22.98 ?  494 MET A CG    1 
ATOM   3958  S  SD    . MET A 1 494 ? 140.176 149.678 83.756  1.00 39.60 ?  494 MET A SD    1 
ATOM   3959  C  CE    . MET A 1 494 ? 138.950 150.964 83.973  1.00 24.17 ?  494 MET A CE    1 
ATOM   3960  N  N     . VAL A 1 495 ? 139.645 150.163 89.596  1.00 19.25 ?  495 VAL A N     1 
ATOM   3961  C  CA    . VAL A 1 495 ? 138.768 150.417 90.737  1.00 14.86 ?  495 VAL A CA    1 
ATOM   3962  C  C     . VAL A 1 495 ? 139.447 151.354 91.726  1.00 21.00 ?  495 VAL A C     1 
ATOM   3963  O  O     . VAL A 1 495 ? 138.841 152.314 92.211  1.00 32.06 ?  495 VAL A O     1 
ATOM   3964  C  CB    . VAL A 1 495 ? 138.352 149.094 91.406  1.00 19.73 ?  495 VAL A CB    1 
ATOM   3965  C  CG1   . VAL A 1 495 ? 137.691 149.363 92.748  1.00 13.65 ?  495 VAL A CG1   1 
ATOM   3966  C  CG2   . VAL A 1 495 ? 137.412 148.317 90.505  1.00 14.21 ?  495 VAL A CG2   1 
ATOM   3967  N  N     . ASN A 1 496 ? 140.721 151.095 92.031  1.00 18.39 ?  496 ASN A N     1 
ATOM   3968  C  CA    . ASN A 1 496 ? 141.467 151.970 92.928  1.00 11.72 ?  496 ASN A CA    1 
ATOM   3969  C  C     . ASN A 1 496 ? 141.612 153.368 92.344  1.00 16.27 ?  496 ASN A C     1 
ATOM   3970  O  O     . ASN A 1 496 ? 141.475 154.365 93.061  1.00 26.76 ?  496 ASN A O     1 
ATOM   3971  C  CB    . ASN A 1 496 ? 142.841 151.366 93.220  1.00 17.45 ?  496 ASN A CB    1 
ATOM   3972  C  CG    . ASN A 1 496 ? 143.478 151.943 94.465  1.00 18.49 ?  496 ASN A CG    1 
ATOM   3973  O  OD1   . ASN A 1 496 ? 142.788 152.358 95.393  1.00 24.08 ?  496 ASN A OD1   1 
ATOM   3974  N  ND2   . ASN A 1 496 ? 144.803 151.972 94.491  1.00 18.71 ?  496 ASN A ND2   1 
ATOM   3975  N  N     . PHE A 1 497 ? 141.886 153.462 91.041  1.00 18.94 ?  497 PHE A N     1 
ATOM   3976  C  CA    . PHE A 1 497 ? 142.043 154.760 90.396  1.00 14.12 ?  497 PHE A CA    1 
ATOM   3977  C  C     . PHE A 1 497 ? 140.769 155.584 90.513  1.00 19.38 ?  497 PHE A C     1 
ATOM   3978  O  O     . PHE A 1 497 ? 140.804 156.752 90.918  1.00 24.23 ?  497 PHE A O     1 
ATOM   3979  C  CB    . PHE A 1 497 ? 142.428 154.564 88.927  1.00 17.00 ?  497 PHE A CB    1 
ATOM   3980  C  CG    . PHE A 1 497 ? 142.612 155.846 88.164  1.00 20.91 ?  497 PHE A CG    1 
ATOM   3981  C  CD1   . PHE A 1 497 ? 141.544 156.441 87.513  1.00 20.09 ?  497 PHE A CD1   1 
ATOM   3982  C  CD2   . PHE A 1 497 ? 143.856 156.446 88.081  1.00 25.45 ?  497 PHE A CD2   1 
ATOM   3983  C  CE1   . PHE A 1 497 ? 141.711 157.617 86.810  1.00 22.74 ?  497 PHE A CE1   1 
ATOM   3984  C  CE2   . PHE A 1 497 ? 144.028 157.623 87.378  1.00 23.32 ?  497 PHE A CE2   1 
ATOM   3985  C  CZ    . PHE A 1 497 ? 142.954 158.207 86.741  1.00 22.22 ?  497 PHE A CZ    1 
ATOM   3986  N  N     . TYR A 1 498 ? 139.628 154.985 90.179  1.00 25.25 ?  498 TYR A N     1 
ATOM   3987  C  CA    . TYR A 1 498 ? 138.381 155.739 90.204  1.00 18.22 ?  498 TYR A CA    1 
ATOM   3988  C  C     . TYR A 1 498 ? 137.896 155.980 91.628  1.00 23.26 ?  498 TYR A C     1 
ATOM   3989  O  O     . TYR A 1 498 ? 137.252 156.998 91.890  1.00 29.58 ?  498 TYR A O     1 
ATOM   3990  C  CB    . TYR A 1 498 ? 137.322 155.026 89.367  1.00 19.42 ?  498 TYR A CB    1 
ATOM   3991  C  CG    . TYR A 1 498 ? 137.646 155.058 87.892  1.00 22.71 ?  498 TYR A CG    1 
ATOM   3992  C  CD1   . TYR A 1 498 ? 137.863 156.265 87.241  1.00 23.96 ?  498 TYR A CD1   1 
ATOM   3993  C  CD2   . TYR A 1 498 ? 137.759 153.887 87.157  1.00 23.81 ?  498 TYR A CD2   1 
ATOM   3994  C  CE1   . TYR A 1 498 ? 138.170 156.305 85.896  1.00 19.02 ?  498 TYR A CE1   1 
ATOM   3995  C  CE2   . TYR A 1 498 ? 138.066 153.917 85.812  1.00 26.18 ?  498 TYR A CE2   1 
ATOM   3996  C  CZ    . TYR A 1 498 ? 138.270 155.128 85.187  1.00 27.69 ?  498 TYR A CZ    1 
ATOM   3997  O  OH    . TYR A 1 498 ? 138.575 155.162 83.846  1.00 33.10 ?  498 TYR A OH    1 
ATOM   3998  N  N     . SER A 1 499 ? 138.226 155.089 92.565  1.00 21.40 ?  499 SER A N     1 
ATOM   3999  C  CA    . SER A 1 499 ? 137.900 155.336 93.965  1.00 7.93  ?  499 SER A CA    1 
ATOM   4000  C  C     . SER A 1 499 ? 138.695 156.516 94.508  1.00 13.95 ?  499 SER A C     1 
ATOM   4001  O  O     . SER A 1 499 ? 138.145 157.382 95.197  1.00 20.78 ?  499 SER A O     1 
ATOM   4002  C  CB    . SER A 1 499 ? 138.163 154.076 94.789  1.00 10.95 ?  499 SER A CB    1 
ATOM   4003  O  OG    . SER A 1 499 ? 137.447 154.105 96.010  1.00 23.91 ?  499 SER A OG    1 
ATOM   4004  N  N     . ILE A 1 500 ? 139.992 156.574 94.195  1.00 13.96 ?  500 ILE A N     1 
ATOM   4005  C  CA    . ILE A 1 500 ? 140.811 157.707 94.611  1.00 17.91 ?  500 ILE A CA    1 
ATOM   4006  C  C     . ILE A 1 500 ? 140.328 158.986 93.942  1.00 18.43 ?  500 ILE A C     1 
ATOM   4007  O  O     . ILE A 1 500 ? 140.274 160.048 94.570  1.00 27.23 ?  500 ILE A O     1 
ATOM   4008  C  CB    . ILE A 1 500 ? 142.296 157.435 94.305  1.00 20.89 ?  500 ILE A CB    1 
ATOM   4009  C  CG1   . ILE A 1 500 ? 142.829 156.311 95.189  1.00 17.96 ?  500 ILE A CG1   1 
ATOM   4010  C  CG2   . ILE A 1 500 ? 143.124 158.686 94.518  1.00 14.38 ?  500 ILE A CG2   1 
ATOM   4011  C  CD1   . ILE A 1 500 ? 144.101 155.690 94.672  1.00 17.65 ?  500 ILE A CD1   1 
ATOM   4012  N  N     . GLN A 1 501 ? 139.973 158.906 92.658  1.00 21.74 ?  501 GLN A N     1 
ATOM   4013  C  CA    . GLN A 1 501 ? 139.478 160.081 91.952  1.00 21.17 ?  501 GLN A CA    1 
ATOM   4014  C  C     . GLN A 1 501 ? 138.182 160.590 92.567  1.00 23.95 ?  501 GLN A C     1 
ATOM   4015  O  O     . GLN A 1 501 ? 138.012 161.798 92.755  1.00 33.02 ?  501 GLN A O     1 
ATOM   4016  C  CB    . GLN A 1 501 ? 139.283 159.757 90.472  1.00 26.40 ?  501 GLN A CB    1 
ATOM   4017  C  CG    . GLN A 1 501 ? 139.519 160.934 89.544  1.00 26.12 ?  501 GLN A CG    1 
ATOM   4018  C  CD    . GLN A 1 501 ? 139.297 160.580 88.090  1.00 29.50 ?  501 GLN A CD    1 
ATOM   4019  O  OE1   . GLN A 1 501 ? 138.257 160.031 87.726  1.00 30.35 ?  501 GLN A OE1   1 
ATOM   4020  N  NE2   . GLN A 1 501 ? 140.275 160.890 87.249  1.00 31.13 ?  501 GLN A NE2   1 
ATOM   4021  N  N     . ARG A 1 502 ? 137.259 159.684 92.899  1.00 22.64 ?  502 ARG A N     1 
ATOM   4022  C  CA    . ARG A 1 502 ? 136.007 160.096 93.524  1.00 21.00 ?  502 ARG A CA    1 
ATOM   4023  C  C     . ARG A 1 502 ? 136.243 160.662 94.918  1.00 21.54 ?  502 ARG A C     1 
ATOM   4024  O  O     . ARG A 1 502 ? 135.596 161.637 95.311  1.00 25.89 ?  502 ARG A O     1 
ATOM   4025  C  CB    . ARG A 1 502 ? 135.034 158.920 93.580  1.00 19.91 ?  502 ARG A CB    1 
ATOM   4026  C  CG    . ARG A 1 502 ? 133.618 159.320 93.947  1.00 22.74 ?  502 ARG A CG    1 
ATOM   4027  C  CD    . ARG A 1 502 ? 133.105 160.420 93.036  1.00 23.43 ?  502 ARG A CD    1 
ATOM   4028  N  NE    . ARG A 1 502 ? 132.015 161.168 93.649  1.00 26.60 ?  502 ARG A NE    1 
ATOM   4029  C  CZ    . ARG A 1 502 ? 131.804 162.464 93.470  1.00 25.59 ?  502 ARG A CZ    1 
ATOM   4030  N  NH1   . ARG A 1 502 ? 132.583 163.191 92.688  1.00 29.04 1  502 ARG A NH1   1 
ATOM   4031  N  NH2   . ARG A 1 502 ? 130.782 163.046 94.092  1.00 26.36 ?  502 ARG A NH2   1 
ATOM   4032  N  N     . SER A 1 503 ? 137.160 160.063 95.684  1.00 19.21 ?  503 SER A N     1 
ATOM   4033  C  CA    . SER A 1 503 ? 137.473 160.593 97.007  1.00 20.41 ?  503 SER A CA    1 
ATOM   4034  C  C     . SER A 1 503 ? 138.049 161.999 96.912  1.00 23.19 ?  503 SER A C     1 
ATOM   4035  O  O     . SER A 1 503 ? 137.668 162.891 97.679  1.00 26.02 ?  503 SER A O     1 
ATOM   4036  C  CB    . SER A 1 503 ? 138.447 159.658 97.725  1.00 19.03 ?  503 SER A CB    1 
ATOM   4037  O  OG    . SER A 1 503 ? 138.446 159.887 99.122  1.00 23.30 ?  503 SER A OG    1 
ATOM   4038  N  N     . ALA A 1 504 ? 138.954 162.223 95.957  1.00 24.12 ?  504 ALA A N     1 
ATOM   4039  C  CA    . ALA A 1 504 ? 139.530 163.549 95.772  1.00 21.09 ?  504 ALA A CA    1 
ATOM   4040  C  C     . ALA A 1 504 ? 138.486 164.543 95.276  1.00 28.52 ?  504 ALA A C     1 
ATOM   4041  O  O     . ALA A 1 504 ? 138.498 165.713 95.673  1.00 37.22 ?  504 ALA A O     1 
ATOM   4042  C  CB    . ALA A 1 504 ? 140.709 163.477 94.805  1.00 24.49 ?  504 ALA A CB    1 
ATOM   4043  N  N     . GLU A 1 505 ? 137.573 164.096 94.413  1.00 26.33 ?  505 GLU A N     1 
ATOM   4044  C  CA    . GLU A 1 505 ? 136.508 164.972 93.938  1.00 26.93 ?  505 GLU A CA    1 
ATOM   4045  C  C     . GLU A 1 505 ? 135.569 165.365 95.071  1.00 29.67 ?  505 GLU A C     1 
ATOM   4046  O  O     . GLU A 1 505 ? 135.142 166.520 95.156  1.00 35.60 ?  505 GLU A O     1 
ATOM   4047  C  CB    . GLU A 1 505 ? 135.734 164.292 92.809  1.00 26.49 ?  505 GLU A CB    1 
ATOM   4048  C  CG    . GLU A 1 505 ? 136.462 164.274 91.475  1.00 27.33 ?  505 GLU A CG    1 
ATOM   4049  C  CD    . GLU A 1 505 ? 136.019 163.129 90.586  1.00 33.62 ?  505 GLU A CD    1 
ATOM   4050  O  OE1   . GLU A 1 505 ? 135.126 162.362 91.002  1.00 34.56 ?  505 GLU A OE1   1 
ATOM   4051  O  OE2   . GLU A 1 505 ? 136.565 162.995 89.471  1.00 35.30 -1 505 GLU A OE2   1 
ATOM   4052  N  N     . ILE A 1 506 ? 135.236 164.419 95.949  1.00 26.44 ?  506 ILE A N     1 
ATOM   4053  C  CA    . ILE A 1 506 ? 134.395 164.732 97.100  1.00 24.78 ?  506 ILE A CA    1 
ATOM   4054  C  C     . ILE A 1 506 ? 135.120 165.680 98.047  1.00 28.62 ?  506 ILE A C     1 
ATOM   4055  O  O     . ILE A 1 506 ? 134.517 166.608 98.598  1.00 34.21 ?  506 ILE A O     1 
ATOM   4056  C  CB    . ILE A 1 506 ? 133.956 163.437 97.810  1.00 23.01 ?  506 ILE A CB    1 
ATOM   4057  C  CG1   . ILE A 1 506 ? 133.043 162.613 96.902  1.00 26.55 ?  506 ILE A CG1   1 
ATOM   4058  C  CG2   . ILE A 1 506 ? 133.247 163.754 99.116  1.00 23.61 ?  506 ILE A CG2   1 
ATOM   4059  C  CD1   . ILE A 1 506 ? 132.848 161.188 97.365  1.00 21.55 ?  506 ILE A CD1   1 
ATOM   4060  N  N     . ALA A 1 507 ? 136.424 165.467 98.247  1.00 30.57 ?  507 ALA A N     1 
ATOM   4061  C  CA    . ALA A 1 507 ? 137.201 166.377 99.083  1.00 28.17 ?  507 ALA A CA    1 
ATOM   4062  C  C     . ALA A 1 507 ? 137.216 167.786 98.500  1.00 30.16 ?  507 ALA A C     1 
ATOM   4063  O  O     . ALA A 1 507 ? 137.100 168.772 99.236  1.00 33.75 ?  507 ALA A O     1 
ATOM   4064  C  CB    . ALA A 1 507 ? 138.625 165.851 99.248  1.00 24.00 ?  507 ALA A CB    1 
ATOM   4065  N  N     . LYS A 1 508 ? 137.366 167.898 97.180  1.00 34.66 ?  508 LYS A N     1 
ATOM   4066  C  CA    . LYS A 1 508 ? 137.352 169.205 96.532  1.00 32.34 ?  508 LYS A CA    1 
ATOM   4067  C  C     . LYS A 1 508 ? 135.980 169.863 96.634  1.00 37.17 ?  508 LYS A C     1 
ATOM   4068  O  O     . LYS A 1 508 ? 135.881 171.069 96.892  1.00 43.61 ?  508 LYS A O     1 
ATOM   4069  C  CB    . LYS A 1 508 ? 137.775 169.062 95.069  1.00 34.75 ?  508 LYS A CB    1 
ATOM   4070  C  CG    . LYS A 1 508 ? 137.549 170.301 94.224  1.00 36.97 ?  508 LYS A CG    1 
ATOM   4071  C  CD    . LYS A 1 508 ? 137.715 169.992 92.747  1.00 38.51 ?  508 LYS A CD    1 
ATOM   4072  C  CE    . LYS A 1 508 ? 137.531 171.238 91.898  1.00 37.16 ?  508 LYS A CE    1 
ATOM   4073  N  NZ    . LYS A 1 508 ? 138.367 171.200 90.667  1.00 40.86 1  508 LYS A NZ    1 
ATOM   4074  N  N     . GLU A 1 509 ? 134.911 169.090 96.430  1.00 35.71 ?  509 GLU A N     1 
ATOM   4075  C  CA    . GLU A 1 509 ? 133.563 169.647 96.478  1.00 34.30 ?  509 GLU A CA    1 
ATOM   4076  C  C     . GLU A 1 509 ? 133.214 170.128 97.881  1.00 37.22 ?  509 GLU A C     1 
ATOM   4077  O  O     . GLU A 1 509 ? 132.745 171.258 98.063  1.00 41.97 ?  509 GLU A O     1 
ATOM   4078  C  CB    . GLU A 1 509 ? 132.550 168.606 96.002  1.00 33.13 ?  509 GLU A CB    1 
ATOM   4079  C  CG    . GLU A 1 509 ? 132.574 168.354 94.504  1.00 40.38 ?  509 GLU A CG    1 
ATOM   4080  C  CD    . GLU A 1 509 ? 132.126 166.951 94.142  1.00 43.69 ?  509 GLU A CD    1 
ATOM   4081  O  OE1   . GLU A 1 509 ? 131.615 166.239 95.033  1.00 42.01 ?  509 GLU A OE1   1 
ATOM   4082  O  OE2   . GLU A 1 509 ? 132.287 166.558 92.968  1.00 40.06 -1 509 GLU A OE2   1 
ATOM   4083  N  N     . LYS A 1 510 ? 133.436 169.283 98.887  1.00 33.73 ?  510 LYS A N     1 
ATOM   4084  C  CA    . LYS A 1 510 ? 133.130 169.643 100.264 1.00 30.44 ?  510 LYS A CA    1 
ATOM   4085  C  C     . LYS A 1 510 ? 134.208 170.502 100.909 1.00 32.19 ?  510 LYS A C     1 
ATOM   4086  O  O     . LYS A 1 510 ? 133.966 171.065 101.981 1.00 38.71 ?  510 LYS A O     1 
ATOM   4087  C  CB    . LYS A 1 510 ? 132.911 168.378 101.097 1.00 29.73 ?  510 LYS A CB    1 
ATOM   4088  C  CG    . LYS A 1 510 ? 131.860 167.441 100.526 1.00 29.83 ?  510 LYS A CG    1 
ATOM   4089  C  CD    . LYS A 1 510 ? 131.599 166.268 101.452 1.00 30.57 ?  510 LYS A CD    1 
ATOM   4090  C  CE    . LYS A 1 510 ? 130.151 165.814 101.372 1.00 35.93 ?  510 LYS A CE    1 
ATOM   4091  N  NZ    . LYS A 1 510 ? 130.037 164.333 101.261 1.00 35.29 1  510 LYS A NZ    1 
ATOM   4092  N  N     . GLY A 1 511 ? 135.381 170.615 100.290 1.00 31.46 ?  511 GLY A N     1 
ATOM   4093  C  CA    . GLY A 1 511 ? 136.444 171.421 100.848 1.00 28.76 ?  511 GLY A CA    1 
ATOM   4094  C  C     . GLY A 1 511 ? 137.135 170.827 102.050 1.00 36.85 ?  511 GLY A C     1 
ATOM   4095  O  O     . GLY A 1 511 ? 137.893 171.534 102.723 1.00 40.96 ?  511 GLY A O     1 
ATOM   4096  N  N     . GLU A 1 512 ? 136.901 169.551 102.347 1.00 29.37 ?  512 GLU A N     1 
ATOM   4097  C  CA    . GLU A 1 512 ? 137.479 168.911 103.519 1.00 27.23 ?  512 GLU A CA    1 
ATOM   4098  C  C     . GLU A 1 512 ? 137.981 167.523 103.155 1.00 29.79 ?  512 GLU A C     1 
ATOM   4099  O  O     . GLU A 1 512 ? 137.391 166.827 102.326 1.00 29.31 ?  512 GLU A O     1 
ATOM   4100  C  CB    . GLU A 1 512 ? 136.462 168.813 104.664 1.00 29.38 ?  512 GLU A CB    1 
ATOM   4101  C  CG    . GLU A 1 512 ? 135.170 168.109 104.287 1.00 31.17 ?  512 GLU A CG    1 
ATOM   4102  C  CD    . GLU A 1 512 ? 134.450 167.530 105.487 1.00 33.54 ?  512 GLU A CD    1 
ATOM   4103  O  OE1   . GLU A 1 512 ? 135.130 167.169 106.470 1.00 31.95 ?  512 GLU A OE1   1 
ATOM   4104  O  OE2   . GLU A 1 512 ? 133.206 167.434 105.448 1.00 30.20 -1 512 GLU A OE2   1 
ATOM   4105  N  N     . THR A 1 513 ? 139.083 167.132 103.785 1.00 31.54 ?  513 THR A N     1 
ATOM   4106  C  CA    . THR A 1 513 ? 139.644 165.797 103.685 1.00 24.41 ?  513 THR A CA    1 
ATOM   4107  C  C     . THR A 1 513 ? 139.372 165.049 104.988 1.00 26.94 ?  513 THR A C     1 
ATOM   4108  O  O     . THR A 1 513 ? 138.698 165.560 105.890 1.00 31.85 ?  513 THR A O     1 
ATOM   4109  C  CB    . THR A 1 513 ? 141.139 165.875 103.374 1.00 26.12 ?  513 THR A CB    1 
ATOM   4110  O  OG1   . THR A 1 513 ? 141.848 166.312 104.539 1.00 35.94 ?  513 THR A OG1   1 
ATOM   4111  C  CG2   . THR A 1 513 ? 141.393 166.856 102.242 1.00 25.68 ?  513 THR A CG2   1 
ATOM   4112  N  N     . PHE A 1 514 ? 139.895 163.832 105.093 1.00 23.23 ?  514 PHE A N     1 
ATOM   4113  C  CA    . PHE A 1 514 ? 139.789 163.111 106.349 1.00 23.53 ?  514 PHE A CA    1 
ATOM   4114  C  C     . PHE A 1 514 ? 140.829 163.631 107.333 1.00 19.94 ?  514 PHE A C     1 
ATOM   4115  O  O     . PHE A 1 514 ? 141.855 164.196 106.942 1.00 28.21 ?  514 PHE A O     1 
ATOM   4116  C  CB    . PHE A 1 514 ? 139.942 161.602 106.141 1.00 16.82 ?  514 PHE A CB    1 
ATOM   4117  C  CG    . PHE A 1 514 ? 141.295 161.174 105.645 1.00 18.74 ?  514 PHE A CG    1 
ATOM   4118  C  CD1   . PHE A 1 514 ? 141.569 161.129 104.291 1.00 18.81 ?  514 PHE A CD1   1 
ATOM   4119  C  CD2   . PHE A 1 514 ? 142.281 160.779 106.534 1.00 19.05 ?  514 PHE A CD2   1 
ATOM   4120  C  CE1   . PHE A 1 514 ? 142.805 160.719 103.833 1.00 12.80 ?  514 PHE A CE1   1 
ATOM   4121  C  CE2   . PHE A 1 514 ? 143.517 160.371 106.081 1.00 16.19 ?  514 PHE A CE2   1 
ATOM   4122  C  CZ    . PHE A 1 514 ? 143.780 160.342 104.729 1.00 15.17 ?  514 PHE A CZ    1 
ATOM   4123  N  N     . ASP A 1 515 ? 140.543 163.457 108.620 1.00 22.86 ?  515 ASP A N     1 
ATOM   4124  C  CA    . ASP A 1 515 ? 141.418 163.989 109.654 1.00 26.17 ?  515 ASP A CA    1 
ATOM   4125  C  C     . ASP A 1 515 ? 142.808 163.374 109.552 1.00 27.64 ?  515 ASP A C     1 
ATOM   4126  O  O     . ASP A 1 515 ? 142.959 162.170 109.329 1.00 32.62 ?  515 ASP A O     1 
ATOM   4127  C  CB    . ASP A 1 515 ? 140.825 163.732 111.039 1.00 27.91 ?  515 ASP A CB    1 
ATOM   4128  C  CG    . ASP A 1 515 ? 139.680 164.670 111.363 1.00 30.13 ?  515 ASP A CG    1 
ATOM   4129  O  OD1   . ASP A 1 515 ? 139.093 165.241 110.421 1.00 30.97 ?  515 ASP A OD1   1 
ATOM   4130  O  OD2   . ASP A 1 515 ? 139.368 164.840 112.561 1.00 31.63 -1 515 ASP A OD2   1 
ATOM   4131  N  N     . GLN A 1 516 ? 143.825 164.223 109.711 1.00 29.29 ?  516 GLN A N     1 
ATOM   4132  C  CA    . GLN A 1 516 ? 145.228 163.828 109.595 1.00 27.02 ?  516 GLN A CA    1 
ATOM   4133  C  C     . GLN A 1 516 ? 145.550 163.276 108.210 1.00 24.74 ?  516 GLN A C     1 
ATOM   4134  O  O     . GLN A 1 516 ? 146.357 162.356 108.071 1.00 31.63 ?  516 GLN A O     1 
ATOM   4135  C  CB    . GLN A 1 516 ? 145.617 162.816 110.676 1.00 23.58 ?  516 GLN A CB    1 
ATOM   4136  C  CG    . GLN A 1 516 ? 145.403 163.301 112.098 1.00 27.32 ?  516 GLN A CG    1 
ATOM   4137  C  CD    . GLN A 1 516 ? 145.629 162.207 113.122 1.00 28.96 ?  516 GLN A CD    1 
ATOM   4138  O  OE1   . GLN A 1 516 ? 146.767 161.828 113.400 1.00 24.45 ?  516 GLN A OE1   1 
ATOM   4139  N  NE2   . GLN A 1 516 ? 144.544 161.692 113.687 1.00 30.70 ?  516 GLN A NE2   1 
ATOM   4140  N  N     . TYR A 1 517 ? 144.919 163.826 107.170 1.00 21.14 ?  517 TYR A N     1 
ATOM   4141  C  CA    . TYR A 1 517 ? 145.258 163.419 105.810 1.00 19.39 ?  517 TYR A CA    1 
ATOM   4142  C  C     . TYR A 1 517 ? 146.638 163.917 105.403 1.00 29.46 ?  517 TYR A C     1 
ATOM   4143  O  O     . TYR A 1 517 ? 147.331 163.249 104.629 1.00 36.04 ?  517 TYR A O     1 
ATOM   4144  C  CB    . TYR A 1 517 ? 144.205 163.921 104.822 1.00 18.68 ?  517 TYR A CB    1 
ATOM   4145  C  CG    . TYR A 1 517 ? 144.751 164.168 103.432 1.00 27.03 ?  517 TYR A CG    1 
ATOM   4146  C  CD1   . TYR A 1 517 ? 144.926 163.120 102.538 1.00 23.94 ?  517 TYR A CD1   1 
ATOM   4147  C  CD2   . TYR A 1 517 ? 145.095 165.449 103.016 1.00 29.69 ?  517 TYR A CD2   1 
ATOM   4148  C  CE1   . TYR A 1 517 ? 145.430 163.339 101.272 1.00 27.36 ?  517 TYR A CE1   1 
ATOM   4149  C  CE2   . TYR A 1 517 ? 145.602 165.675 101.753 1.00 25.86 ?  517 TYR A CE2   1 
ATOM   4150  C  CZ    . TYR A 1 517 ? 145.767 164.618 100.886 1.00 29.69 ?  517 TYR A CZ    1 
ATOM   4151  O  OH    . TYR A 1 517 ? 146.266 164.841 99.625  1.00 34.33 ?  517 TYR A OH    1 
ATOM   4152  N  N     . GLU A 1 518 ? 147.047 165.082 105.912 1.00 31.48 ?  518 GLU A N     1 
ATOM   4153  C  CA    . GLU A 1 518 ? 148.299 165.694 105.479 1.00 33.30 ?  518 GLU A CA    1 
ATOM   4154  C  C     . GLU A 1 518 ? 149.496 164.797 105.760 1.00 37.36 ?  518 GLU A C     1 
ATOM   4155  O  O     . GLU A 1 518 ? 150.492 164.845 105.028 1.00 39.66 ?  518 GLU A O     1 
ATOM   4156  C  CB    . GLU A 1 518 ? 148.491 167.057 106.153 1.00 32.58 ?  518 GLU A CB    1 
ATOM   4157  C  CG    . GLU A 1 518 ? 147.330 168.050 106.008 1.00 34.94 ?  518 GLU A CG    1 
ATOM   4158  C  CD    . GLU A 1 518 ? 146.079 167.644 106.768 1.00 42.69 ?  518 GLU A CD    1 
ATOM   4159  O  OE1   . GLU A 1 518 ? 144.969 168.016 106.331 1.00 41.60 ?  518 GLU A OE1   1 
ATOM   4160  O  OE2   . GLU A 1 518 ? 146.206 166.954 107.801 1.00 40.31 -1 518 GLU A OE2   1 
ATOM   4161  N  N     . GLY A 1 519 ? 149.426 163.977 106.807 1.00 26.93 ?  519 GLY A N     1 
ATOM   4162  C  CA    . GLY A 1 519 ? 150.493 163.038 107.083 1.00 23.56 ?  519 GLY A CA    1 
ATOM   4163  C  C     . GLY A 1 519 ? 150.422 161.738 106.315 1.00 23.79 ?  519 GLY A C     1 
ATOM   4164  O  O     . GLY A 1 519 ? 151.356 160.936 106.396 1.00 28.85 ?  519 GLY A O     1 
ATOM   4165  N  N     . SER A 1 520 ? 149.343 161.515 105.569 1.00 22.77 ?  520 SER A N     1 
ATOM   4166  C  CA    . SER A 1 520 ? 149.168 160.260 104.857 1.00 24.37 ?  520 SER A CA    1 
ATOM   4167  C  C     . SER A 1 520 ? 150.048 160.209 103.612 1.00 22.49 ?  520 SER A C     1 
ATOM   4168  O  O     . SER A 1 520 ? 150.538 161.227 103.117 1.00 31.54 ?  520 SER A O     1 
ATOM   4169  C  CB    . SER A 1 520 ? 147.702 160.064 104.469 1.00 19.01 ?  520 SER A CB    1 
ATOM   4170  O  OG    . SER A 1 520 ? 147.272 161.073 103.573 1.00 21.50 ?  520 SER A OG    1 
ATOM   4171  N  N     . THR A 1 521 ? 150.247 158.990 103.107 1.00 20.34 ?  521 THR A N     1 
ATOM   4172  C  CA    . THR A 1 521 ? 151.024 158.805 101.888 1.00 21.16 ?  521 THR A CA    1 
ATOM   4173  C  C     . THR A 1 521 ? 150.304 159.346 100.660 1.00 23.54 ?  521 THR A C     1 
ATOM   4174  O  O     . THR A 1 521 ? 150.950 159.580 99.633  1.00 24.52 ?  521 THR A O     1 
ATOM   4175  C  CB    . THR A 1 521 ? 151.356 157.326 101.690 1.00 22.76 ?  521 THR A CB    1 
ATOM   4176  O  OG1   . THR A 1 521 ? 150.163 156.607 101.354 1.00 23.73 ?  521 THR A OG1   1 
ATOM   4177  C  CG2   . THR A 1 521 ? 151.951 156.742 102.960 1.00 19.65 ?  521 THR A CG2   1 
ATOM   4178  N  N     . TYR A 1 522 ? 148.984 159.535 100.736 1.00 26.55 ?  522 TYR A N     1 
ATOM   4179  C  CA    . TYR A 1 522 ? 148.275 160.225 99.664  1.00 18.97 ?  522 TYR A CA    1 
ATOM   4180  C  C     . TYR A 1 522 ? 148.758 161.663 99.537  1.00 23.87 ?  522 TYR A C     1 
ATOM   4181  O  O     . TYR A 1 522 ? 149.006 162.157 98.431  1.00 25.62 ?  522 TYR A O     1 
ATOM   4182  C  CB    . TYR A 1 522 ? 146.768 160.195 99.919  1.00 17.28 ?  522 TYR A CB    1 
ATOM   4183  C  CG    . TYR A 1 522 ? 146.157 158.814 99.976  1.00 17.83 ?  522 TYR A CG    1 
ATOM   4184  C  CD1   . TYR A 1 522 ? 146.107 158.007 98.849  1.00 19.28 ?  522 TYR A CD1   1 
ATOM   4185  C  CD2   . TYR A 1 522 ? 145.611 158.327 101.155 1.00 21.38 ?  522 TYR A CD2   1 
ATOM   4186  C  CE1   . TYR A 1 522 ? 145.544 156.749 98.898  1.00 18.02 ?  522 TYR A CE1   1 
ATOM   4187  C  CE2   . TYR A 1 522 ? 145.042 157.071 101.213 1.00 18.03 ?  522 TYR A CE2   1 
ATOM   4188  C  CZ    . TYR A 1 522 ? 145.014 156.285 100.083 1.00 19.92 ?  522 TYR A CZ    1 
ATOM   4189  O  OH    . TYR A 1 522 ? 144.451 155.033 100.137 1.00 25.93 ?  522 TYR A OH    1 
ATOM   4190  N  N     . ALA A 1 523 ? 148.901 162.352 100.672 1.00 25.50 ?  523 ALA A N     1 
ATOM   4191  C  CA    . ALA A 1 523 ? 149.335 163.745 100.651 1.00 26.43 ?  523 ALA A CA    1 
ATOM   4192  C  C     . ALA A 1 523 ? 150.775 163.871 100.174 1.00 31.21 ?  523 ALA A C     1 
ATOM   4193  O  O     . ALA A 1 523 ? 151.104 164.785 99.408  1.00 32.89 ?  523 ALA A O     1 
ATOM   4194  C  CB    . ALA A 1 523 ? 149.170 164.364 102.037 1.00 25.19 ?  523 ALA A CB    1 
ATOM   4195  N  N     . THR A 1 524 ? 151.649 162.967 100.615 1.00 24.86 ?  524 THR A N     1 
ATOM   4196  C  CA    . THR A 1 524 ? 153.048 163.002 100.215 1.00 24.67 ?  524 THR A CA    1 
ATOM   4197  C  C     . THR A 1 524 ? 153.284 162.421 98.828  1.00 30.74 ?  524 THR A C     1 
ATOM   4198  O  O     . THR A 1 524 ? 154.394 162.558 98.301  1.00 36.80 ?  524 THR A O     1 
ATOM   4199  C  CB    . THR A 1 524 ? 153.907 162.250 101.235 1.00 28.88 ?  524 THR A CB    1 
ATOM   4200  O  OG1   . THR A 1 524 ? 153.724 160.839 101.070 1.00 30.78 ?  524 THR A OG1   1 
ATOM   4201  C  CG2   . THR A 1 524 ? 153.519 162.643 102.650 1.00 26.81 ?  524 THR A CG2   1 
ATOM   4202  N  N     . GLY A 1 525 ? 152.283 161.780 98.230  1.00 26.63 ?  525 GLY A N     1 
ATOM   4203  C  CA    . GLY A 1 525 ? 152.424 161.192 96.917  1.00 24.39 ?  525 GLY A CA    1 
ATOM   4204  C  C     . GLY A 1 525 ? 153.113 159.848 96.884  1.00 29.59 ?  525 GLY A C     1 
ATOM   4205  O  O     . GLY A 1 525 ? 153.293 159.291 95.794  1.00 32.79 ?  525 GLY A O     1 
ATOM   4206  N  N     . GLU A 1 526 ? 153.509 159.309 98.040  1.00 29.06 ?  526 GLU A N     1 
ATOM   4207  C  CA    . GLU A 1 526 ? 154.170 158.008 98.068  1.00 29.80 ?  526 GLU A CA    1 
ATOM   4208  C  C     . GLU A 1 526 ? 153.230 156.902 97.609  1.00 31.92 ?  526 GLU A C     1 
ATOM   4209  O  O     . GLU A 1 526 ? 153.651 155.964 96.920  1.00 37.13 ?  526 GLU A O     1 
ATOM   4210  C  CB    . GLU A 1 526 ? 154.697 157.725 99.475  1.00 30.68 ?  526 GLU A CB    1 
ATOM   4211  C  CG    . GLU A 1 526 ? 155.072 156.276 99.729  1.00 31.72 ?  526 GLU A CG    1 
ATOM   4212  C  CD    . GLU A 1 526 ? 155.172 155.952 101.207 1.00 36.24 ?  526 GLU A CD    1 
ATOM   4213  O  OE1   . GLU A 1 526 ? 155.257 156.896 102.018 1.00 35.08 ?  526 GLU A OE1   1 
ATOM   4214  O  OE2   . GLU A 1 526 ? 155.162 154.753 101.556 1.00 34.53 -1 526 GLU A OE2   1 
ATOM   4215  N  N     . TYR A 1 527 ? 151.948 157.002 97.974  1.00 31.75 ?  527 TYR A N     1 
ATOM   4216  C  CA    . TYR A 1 527 ? 150.973 155.976 97.615  1.00 22.45 ?  527 TYR A CA    1 
ATOM   4217  C  C     . TYR A 1 527 ? 150.940 155.734 96.112  1.00 24.31 ?  527 TYR A C     1 
ATOM   4218  O  O     . TYR A 1 527 ? 150.758 154.598 95.660  1.00 30.71 ?  527 TYR A O     1 
ATOM   4219  C  CB    . TYR A 1 527 ? 149.586 156.381 98.119  1.00 18.46 ?  527 TYR A CB    1 
ATOM   4220  C  CG    . TYR A 1 527 ? 148.511 155.347 97.870  1.00 25.45 ?  527 TYR A CG    1 
ATOM   4221  C  CD1   . TYR A 1 527 ? 147.799 155.326 96.677  1.00 23.33 ?  527 TYR A CD1   1 
ATOM   4222  C  CD2   . TYR A 1 527 ? 148.205 154.395 98.831  1.00 24.14 ?  527 TYR A CD2   1 
ATOM   4223  C  CE1   . TYR A 1 527 ? 146.821 154.383 96.450  1.00 20.19 ?  527 TYR A CE1   1 
ATOM   4224  C  CE2   . TYR A 1 527 ? 147.227 153.450 98.612  1.00 22.64 ?  527 TYR A CE2   1 
ATOM   4225  C  CZ    . TYR A 1 527 ? 146.537 153.449 97.420  1.00 23.29 ?  527 TYR A CZ    1 
ATOM   4226  O  OH    . TYR A 1 527 ? 145.560 152.507 97.199  1.00 29.93 ?  527 TYR A OH    1 
ATOM   4227  N  N     . PHE A 1 528 ? 151.119 156.789 95.323  1.00 26.54 ?  528 PHE A N     1 
ATOM   4228  C  CA    . PHE A 1 528 ? 151.037 156.704 93.873  1.00 27.56 ?  528 PHE A CA    1 
ATOM   4229  C  C     . PHE A 1 528 ? 152.343 156.271 93.222  1.00 31.65 ?  528 PHE A C     1 
ATOM   4230  O  O     . PHE A 1 528 ? 152.393 156.167 91.993  1.00 37.05 ?  528 PHE A O     1 
ATOM   4231  C  CB    . PHE A 1 528 ? 150.601 158.053 93.294  1.00 28.67 ?  528 PHE A CB    1 
ATOM   4232  C  CG    . PHE A 1 528 ? 149.310 158.566 93.863  1.00 31.81 ?  528 PHE A CG    1 
ATOM   4233  C  CD1   . PHE A 1 528 ? 148.101 158.229 93.279  1.00 27.01 ?  528 PHE A CD1   1 
ATOM   4234  C  CD2   . PHE A 1 528 ? 149.303 159.381 94.983  1.00 29.35 ?  528 PHE A CD2   1 
ATOM   4235  C  CE1   . PHE A 1 528 ? 146.911 158.696 93.798  1.00 27.38 ?  528 PHE A CE1   1 
ATOM   4236  C  CE2   . PHE A 1 528 ? 148.116 159.849 95.507  1.00 29.22 ?  528 PHE A CE2   1 
ATOM   4237  C  CZ    . PHE A 1 528 ? 146.919 159.506 94.914  1.00 28.09 ?  528 PHE A CZ    1 
ATOM   4238  N  N     . ASP A 1 529 ? 153.391 156.015 94.011  1.00 30.61 ?  529 ASP A N     1 
ATOM   4239  C  CA    . ASP A 1 529 ? 154.696 155.672 93.450  1.00 29.55 ?  529 ASP A CA    1 
ATOM   4240  C  C     . ASP A 1 529 ? 154.592 154.503 92.477  1.00 33.50 ?  529 ASP A C     1 
ATOM   4241  O  O     . ASP A 1 529 ? 154.869 154.643 91.279  1.00 35.83 ?  529 ASP A O     1 
ATOM   4242  C  CB    . ASP A 1 529 ? 155.676 155.351 94.580  1.00 32.37 ?  529 ASP A CB    1 
ATOM   4243  C  CG    . ASP A 1 529 ? 156.251 156.596 95.223  1.00 39.19 ?  529 ASP A CG    1 
ATOM   4244  O  OD1   . ASP A 1 529 ? 155.966 157.708 94.730  1.00 36.61 ?  529 ASP A OD1   1 
ATOM   4245  O  OD2   . ASP A 1 529 ? 156.988 156.463 96.223  1.00 39.06 -1 529 ASP A OD2   1 
ATOM   4246  N  N     . LYS A 1 530 ? 154.147 153.345 92.972  1.00 34.90 ?  530 LYS A N     1 
ATOM   4247  C  CA    . LYS A 1 530 ? 154.012 152.173 92.115  1.00 32.53 ?  530 LYS A CA    1 
ATOM   4248  C  C     . LYS A 1 530 ? 153.035 152.406 90.973  1.00 32.70 ?  530 LYS A C     1 
ATOM   4249  O  O     . LYS A 1 530 ? 153.076 151.679 89.976  1.00 34.96 ?  530 LYS A O     1 
ATOM   4250  C  CB    . LYS A 1 530 ? 153.564 150.966 92.940  1.00 31.49 ?  530 LYS A CB    1 
ATOM   4251  C  CG    . LYS A 1 530 ? 152.069 150.711 92.889  1.00 29.76 ?  530 LYS A CG    1 
ATOM   4252  C  CD    . LYS A 1 530 ? 151.641 149.693 93.921  1.00 31.93 ?  530 LYS A CD    1 
ATOM   4253  C  CE    . LYS A 1 530 ? 150.183 149.331 93.741  1.00 27.82 ?  530 LYS A CE    1 
ATOM   4254  N  NZ    . LYS A 1 530 ? 149.436 149.434 95.022  1.00 33.29 1  530 LYS A NZ    1 
ATOM   4255  N  N     . TYR A 1 531 ? 152.161 153.402 91.094  1.00 30.64 ?  531 TYR A N     1 
ATOM   4256  C  CA    . TYR A 1 531 ? 151.215 153.712 90.036  1.00 28.11 ?  531 TYR A CA    1 
ATOM   4257  C  C     . TYR A 1 531 ? 151.777 154.674 89.001  1.00 26.93 ?  531 TYR A C     1 
ATOM   4258  O  O     . TYR A 1 531 ? 151.291 154.687 87.864  1.00 32.56 ?  531 TYR A O     1 
ATOM   4259  C  CB    . TYR A 1 531 ? 149.933 154.292 90.635  1.00 27.82 ?  531 TYR A CB    1 
ATOM   4260  C  CG    . TYR A 1 531 ? 149.065 153.258 91.310  1.00 28.79 ?  531 TYR A CG    1 
ATOM   4261  C  CD1   . TYR A 1 531 ? 148.639 152.130 90.624  1.00 23.74 ?  531 TYR A CD1   1 
ATOM   4262  C  CD2   . TYR A 1 531 ? 148.671 153.409 92.633  1.00 25.66 ?  531 TYR A CD2   1 
ATOM   4263  C  CE1   . TYR A 1 531 ? 147.844 151.181 91.234  1.00 29.88 ?  531 TYR A CE1   1 
ATOM   4264  C  CE2   . TYR A 1 531 ? 147.876 152.465 93.250  1.00 25.40 ?  531 TYR A CE2   1 
ATOM   4265  C  CZ    . TYR A 1 531 ? 147.466 151.354 92.546  1.00 28.75 ?  531 TYR A CZ    1 
ATOM   4266  O  OH    . TYR A 1 531 ? 146.674 150.411 93.158  1.00 26.64 ?  531 TYR A OH    1 
ATOM   4267  N  N     . VAL A 1 532 ? 152.784 155.477 89.360  1.00 36.73 ?  532 VAL A N     1 
ATOM   4268  C  CA    . VAL A 1 532 ? 153.387 156.392 88.396  1.00 35.08 ?  532 VAL A CA    1 
ATOM   4269  C  C     . VAL A 1 532 ? 154.612 155.794 87.723  1.00 36.69 ?  532 VAL A C     1 
ATOM   4270  O  O     . VAL A 1 532 ? 155.223 156.450 86.868  1.00 41.15 ?  532 VAL A O     1 
ATOM   4271  C  CB    . VAL A 1 532 ? 153.756 157.739 89.054  1.00 35.29 ?  532 VAL A CB    1 
ATOM   4272  C  CG1   . VAL A 1 532 ? 152.524 158.385 89.667  1.00 34.97 ?  532 VAL A CG1   1 
ATOM   4273  C  CG2   . VAL A 1 532 ? 154.842 157.549 90.096  1.00 33.74 ?  532 VAL A CG2   1 
ATOM   4274  N  N     . SER A 1 533 ? 154.988 154.567 88.076  1.00 37.31 ?  533 SER A N     1 
ATOM   4275  C  CA    . SER A 1 533 ? 156.134 153.896 87.482  1.00 39.93 ?  533 SER A CA    1 
ATOM   4276  C  C     . SER A 1 533 ? 155.793 152.572 86.817  1.00 40.94 ?  533 SER A C     1 
ATOM   4277  O  O     . SER A 1 533 ? 156.444 152.209 85.835  1.00 43.31 ?  533 SER A O     1 
ATOM   4278  C  CB    . SER A 1 533 ? 157.218 153.651 88.544  1.00 41.14 ?  533 SER A CB    1 
ATOM   4279  O  OG    . SER A 1 533 ? 156.825 152.628 89.443  1.00 44.41 ?  533 SER A OG    1 
ATOM   4280  N  N     . THR A 1 534 ? 154.797 151.847 87.318  1.00 40.28 ?  534 THR A N     1 
ATOM   4281  C  CA    . THR A 1 534 ? 154.409 150.554 86.774  1.00 38.86 ?  534 THR A CA    1 
ATOM   4282  C  C     . THR A 1 534 ? 153.095 150.694 86.019  1.00 38.19 ?  534 THR A C     1 
ATOM   4283  O  O     . THR A 1 534 ? 152.121 151.235 86.555  1.00 43.56 ?  534 THR A O     1 
ATOM   4284  C  CB    . THR A 1 534 ? 154.267 149.509 87.885  1.00 39.36 ?  534 THR A CB    1 
ATOM   4285  O  OG1   . THR A 1 534 ? 155.547 149.267 88.483  1.00 42.76 ?  534 THR A OG1   1 
ATOM   4286  C  CG2   . THR A 1 534 ? 153.718 148.205 87.328  1.00 38.66 ?  534 THR A CG2   1 
ATOM   4287  N  N     . ASP A 1 535 ? 153.073 150.212 84.781  1.00 40.64 ?  535 ASP A N     1 
ATOM   4288  C  CA    . ASP A 1 535 ? 151.863 150.206 83.974  1.00 39.74 ?  535 ASP A CA    1 
ATOM   4289  C  C     . ASP A 1 535 ? 151.070 148.937 84.263  1.00 41.84 ?  535 ASP A C     1 
ATOM   4290  O  O     . ASP A 1 535 ? 151.609 147.830 84.181  1.00 42.89 ?  535 ASP A O     1 
ATOM   4291  C  CB    . ASP A 1 535 ? 152.206 150.296 82.487  1.00 38.68 ?  535 ASP A CB    1 
ATOM   4292  C  CG    . ASP A 1 535 ? 151.030 150.740 81.643  1.00 44.50 ?  535 ASP A CG    1 
ATOM   4293  O  OD1   . ASP A 1 535 ? 150.609 151.909 81.774  1.00 45.74 ?  535 ASP A OD1   1 
ATOM   4294  O  OD2   . ASP A 1 535 ? 150.529 149.921 80.846  1.00 45.92 -1 535 ASP A OD2   1 
ATOM   4295  N  N     . PHE A 1 536 ? 149.793 149.104 84.604  1.00 34.20 ?  536 PHE A N     1 
ATOM   4296  C  CA    . PHE A 1 536 ? 148.936 147.988 84.981  1.00 26.98 ?  536 PHE A CA    1 
ATOM   4297  C  C     . PHE A 1 536 ? 147.947 147.622 83.881  1.00 31.33 ?  536 PHE A C     1 
ATOM   4298  O  O     . PHE A 1 536 ? 146.912 147.006 84.159  1.00 37.66 ?  536 PHE A O     1 
ATOM   4299  C  CB    . PHE A 1 536 ? 148.202 148.305 86.283  1.00 29.06 ?  536 PHE A CB    1 
ATOM   4300  C  CG    . PHE A 1 536 ? 149.103 148.371 87.484  1.00 27.91 ?  536 PHE A CG    1 
ATOM   4301  C  CD1   . PHE A 1 536 ? 149.431 147.224 88.184  1.00 27.98 ?  536 PHE A CD1   1 
ATOM   4302  C  CD2   . PHE A 1 536 ? 149.629 149.578 87.906  1.00 27.54 ?  536 PHE A CD2   1 
ATOM   4303  C  CE1   . PHE A 1 536 ? 150.262 147.281 89.286  1.00 28.05 ?  536 PHE A CE1   1 
ATOM   4304  C  CE2   . PHE A 1 536 ? 150.462 149.640 89.007  1.00 32.24 ?  536 PHE A CE2   1 
ATOM   4305  C  CZ    . PHE A 1 536 ? 150.777 148.491 89.698  1.00 28.77 ?  536 PHE A CZ    1 
ATOM   4306  N  N     . SER A 1 537 ? 148.243 147.995 82.639  1.00 37.02 ?  537 SER A N     1 
ATOM   4307  C  CA    . SER A 1 537 ? 147.438 147.559 81.512  1.00 33.64 ?  537 SER A CA    1 
ATOM   4308  C  C     . SER A 1 537 ? 147.575 146.048 81.333  1.00 38.82 ?  537 SER A C     1 
ATOM   4309  O  O     . SER A 1 537 ? 148.603 145.465 81.688  1.00 39.19 ?  537 SER A O     1 
ATOM   4310  C  CB    . SER A 1 537 ? 147.873 148.286 80.241  1.00 37.25 ?  537 SER A CB    1 
ATOM   4311  O  OG    . SER A 1 537 ? 147.468 147.597 79.073  1.00 44.12 ?  537 SER A OG    1 
ATOM   4312  N  N     . PRO A 1 538 ? 146.543 145.387 80.806  1.00 37.27 ?  538 PRO A N     1 
ATOM   4313  C  CA    . PRO A 1 538 ? 146.609 143.929 80.652  1.00 34.32 ?  538 PRO A CA    1 
ATOM   4314  C  C     . PRO A 1 538 ? 147.769 143.502 79.765  1.00 39.19 ?  538 PRO A C     1 
ATOM   4315  O  O     . PRO A 1 538 ? 148.052 144.118 78.736  1.00 39.38 ?  538 PRO A O     1 
ATOM   4316  C  CB    . PRO A 1 538 ? 145.260 143.580 80.017  1.00 37.31 ?  538 PRO A CB    1 
ATOM   4317  C  CG    . PRO A 1 538 ? 144.362 144.701 80.397  1.00 34.46 ?  538 PRO A CG    1 
ATOM   4318  C  CD    . PRO A 1 538 ? 145.230 145.920 80.406  1.00 33.65 ?  538 PRO A CD    1 
ATOM   4319  N  N     . LYS A 1 539 ? 148.441 142.429 80.179  1.00 44.39 ?  539 LYS A N     1 
ATOM   4320  C  CA    . LYS A 1 539 ? 149.538 141.855 79.415  1.00 44.62 ?  539 LYS A CA    1 
ATOM   4321  C  C     . LYS A 1 539 ? 149.080 140.773 78.449  1.00 44.99 ?  539 LYS A C     1 
ATOM   4322  O  O     . LYS A 1 539 ? 149.888 140.300 77.643  1.00 47.43 ?  539 LYS A O     1 
ATOM   4323  C  CB    . LYS A 1 539 ? 150.595 141.277 80.361  1.00 43.77 ?  539 LYS A CB    1 
ATOM   4324  C  CG    . LYS A 1 539 ? 151.010 142.220 81.476  1.00 42.84 ?  539 LYS A CG    1 
ATOM   4325  C  CD    . LYS A 1 539 ? 152.121 143.154 81.026  1.00 45.68 ?  539 LYS A CD    1 
ATOM   4326  C  CE    . LYS A 1 539 ? 152.346 144.268 82.036  1.00 45.50 ?  539 LYS A CE    1 
ATOM   4327  N  NZ    . LYS A 1 539 ? 151.625 145.514 81.656  1.00 44.13 1  539 LYS A NZ    1 
ATOM   4328  N  N     . TYR A 1 540 ? 147.813 140.375 78.508  1.00 42.49 ?  540 TYR A N     1 
ATOM   4329  C  CA    . TYR A 1 540 ? 147.258 139.353 77.634  1.00 41.58 ?  540 TYR A CA    1 
ATOM   4330  C  C     . TYR A 1 540 ? 146.210 139.977 76.723  1.00 42.99 ?  540 TYR A C     1 
ATOM   4331  O  O     . TYR A 1 540 ? 145.454 140.859 77.143  1.00 44.81 ?  540 TYR A O     1 
ATOM   4332  C  CB    . TYR A 1 540 ? 146.641 138.211 78.447  1.00 42.66 ?  540 TYR A CB    1 
ATOM   4333  C  CG    . TYR A 1 540 ? 147.654 137.415 79.235  1.00 44.40 ?  540 TYR A CG    1 
ATOM   4334  C  CD1   . TYR A 1 540 ? 148.014 137.792 80.522  1.00 42.75 ?  540 TYR A CD1   1 
ATOM   4335  C  CD2   . TYR A 1 540 ? 148.256 136.289 78.689  1.00 45.61 ?  540 TYR A CD2   1 
ATOM   4336  C  CE1   . TYR A 1 540 ? 148.942 137.068 81.244  1.00 45.50 ?  540 TYR A CE1   1 
ATOM   4337  C  CE2   . TYR A 1 540 ? 149.185 135.560 79.405  1.00 40.60 ?  540 TYR A CE2   1 
ATOM   4338  C  CZ    . TYR A 1 540 ? 149.524 135.953 80.681  1.00 45.33 ?  540 TYR A CZ    1 
ATOM   4339  O  OH    . TYR A 1 540 ? 150.449 135.227 81.393  1.00 46.48 ?  540 TYR A OH    1 
ATOM   4340  N  N     . GLU A 1 541 ? 146.176 139.515 75.470  1.00 47.04 ?  541 GLU A N     1 
ATOM   4341  C  CA    . GLU A 1 541 ? 145.244 140.076 74.497  1.00 47.04 ?  541 GLU A CA    1 
ATOM   4342  C  C     . GLU A 1 541 ? 143.798 139.804 74.892  1.00 47.07 ?  541 GLU A C     1 
ATOM   4343  O  O     . GLU A 1 541 ? 142.916 140.638 74.657  1.00 44.24 ?  541 GLU A O     1 
ATOM   4344  C  CB    . GLU A 1 541 ? 145.534 139.512 73.107  1.00 45.13 ?  541 GLU A CB    1 
ATOM   4345  C  CG    . GLU A 1 541 ? 145.075 140.402 71.966  1.00 46.40 ?  541 GLU A CG    1 
ATOM   4346  C  CD    . GLU A 1 541 ? 145.003 139.662 70.645  1.00 52.19 ?  541 GLU A CD    1 
ATOM   4347  O  OE1   . GLU A 1 541 ? 145.000 138.413 70.663  1.00 52.67 ?  541 GLU A OE1   1 
ATOM   4348  O  OE2   . GLU A 1 541 ? 144.951 140.328 69.589  1.00 50.07 -1 541 GLU A OE2   1 
ATOM   4349  N  N     . LYS A 1 542 ? 143.533 138.637 75.484  1.00 42.45 ?  542 LYS A N     1 
ATOM   4350  C  CA    . LYS A 1 542 ? 142.172 138.302 75.887  1.00 41.73 ?  542 LYS A CA    1 
ATOM   4351  C  C     . LYS A 1 542 ? 141.653 139.271 76.944  1.00 43.05 ?  542 LYS A C     1 
ATOM   4352  O  O     . LYS A 1 542 ? 140.511 139.737 76.865  1.00 41.93 ?  542 LYS A O     1 
ATOM   4353  C  CB    . LYS A 1 542 ? 142.122 136.865 76.403  1.00 40.93 ?  542 LYS A CB    1 
ATOM   4354  C  CG    . LYS A 1 542 ? 140.728 136.362 76.728  1.00 43.00 ?  542 LYS A CG    1 
ATOM   4355  C  CD    . LYS A 1 542 ? 140.770 134.927 77.221  1.00 39.38 ?  542 LYS A CD    1 
ATOM   4356  C  CE    . LYS A 1 542 ? 139.373 134.359 77.391  1.00 41.15 ?  542 LYS A CE    1 
ATOM   4357  N  NZ    . LYS A 1 542 ? 139.404 132.911 77.733  1.00 42.60 1  542 LYS A NZ    1 
ATOM   4358  N  N     . ILE A 1 543 ? 142.488 139.602 77.930  1.00 38.22 ?  543 ILE A N     1 
ATOM   4359  C  CA    . ILE A 1 543 ? 142.064 140.528 78.975  1.00 36.34 ?  543 ILE A CA    1 
ATOM   4360  C  C     . ILE A 1 543 ? 141.881 141.930 78.402  1.00 38.94 ?  543 ILE A C     1 
ATOM   4361  O  O     . ILE A 1 543 ? 140.951 142.655 78.781  1.00 41.41 ?  543 ILE A O     1 
ATOM   4362  C  CB    . ILE A 1 543 ? 143.069 140.514 80.141  1.00 35.88 ?  543 ILE A CB    1 
ATOM   4363  C  CG1   . ILE A 1 543 ? 143.179 139.117 80.758  1.00 39.31 ?  543 ILE A CG1   1 
ATOM   4364  C  CG2   . ILE A 1 543 ? 142.649 141.501 81.210  1.00 37.77 ?  543 ILE A CG2   1 
ATOM   4365  C  CD1   . ILE A 1 543 ? 141.880 138.338 80.796  1.00 37.09 ?  543 ILE A CD1   1 
ATOM   4366  N  N     . ALA A 1 544 ? 142.759 142.331 77.480  1.00 37.81 ?  544 ALA A N     1 
ATOM   4367  C  CA    . ALA A 1 544 ? 142.614 143.632 76.837  1.00 40.47 ?  544 ALA A CA    1 
ATOM   4368  C  C     . ALA A 1 544 ? 141.311 143.718 76.051  1.00 42.32 ?  544 ALA A C     1 
ATOM   4369  O  O     . ALA A 1 544 ? 140.634 144.752 76.067  1.00 42.94 ?  544 ALA A O     1 
ATOM   4370  C  CB    . ALA A 1 544 ? 143.811 143.904 75.927  1.00 40.60 ?  544 ALA A CB    1 
ATOM   4371  N  N     . ASN A 1 545 ? 140.946 142.639 75.353  1.00 43.74 ?  545 ASN A N     1 
ATOM   4372  C  CA    . ASN A 1 545 ? 139.660 142.607 74.665  1.00 44.64 ?  545 ASN A CA    1 
ATOM   4373  C  C     . ASN A 1 545 ? 138.501 142.614 75.652  1.00 44.81 ?  545 ASN A C     1 
ATOM   4374  O  O     . ASN A 1 545 ? 137.432 143.158 75.349  1.00 47.71 ?  545 ASN A O     1 
ATOM   4375  C  CB    . ASN A 1 545 ? 139.578 141.381 73.756  1.00 44.57 ?  545 ASN A CB    1 
ATOM   4376  C  CG    . ASN A 1 545 ? 140.661 141.369 72.698  1.00 47.93 ?  545 ASN A CG    1 
ATOM   4377  O  OD1   . ASN A 1 545 ? 141.198 142.414 72.332  1.00 47.94 ?  545 ASN A OD1   1 
ATOM   4378  N  ND2   . ASN A 1 545 ? 140.990 140.182 72.201  1.00 47.29 ?  545 ASN A ND2   1 
ATOM   4379  N  N     . LEU A 1 546 ? 138.687 142.007 76.826  1.00 40.52 ?  546 LEU A N     1 
ATOM   4380  C  CA    . LEU A 1 546 ? 137.676 142.105 77.874  1.00 38.34 ?  546 LEU A CA    1 
ATOM   4381  C  C     . LEU A 1 546 ? 137.478 143.551 78.307  1.00 38.77 ?  546 LEU A C     1 
ATOM   4382  O  O     . LEU A 1 546 ? 136.345 143.990 78.540  1.00 40.95 ?  546 LEU A O     1 
ATOM   4383  C  CB    . LEU A 1 546 ? 138.069 141.240 79.070  1.00 35.29 ?  546 LEU A CB    1 
ATOM   4384  C  CG    . LEU A 1 546 ? 137.894 139.731 78.919  1.00 38.57 ?  546 LEU A CG    1 
ATOM   4385  C  CD1   . LEU A 1 546 ? 138.210 139.040 80.230  1.00 36.37 ?  546 LEU A CD1   1 
ATOM   4386  C  CD2   . LEU A 1 546 ? 136.484 139.402 78.461  1.00 34.75 ?  546 LEU A CD2   1 
ATOM   4387  N  N     . PHE A 1 547 ? 138.567 144.309 78.418  1.00 37.80 ?  547 PHE A N     1 
ATOM   4388  C  CA    . PHE A 1 547 ? 138.505 145.709 78.814  1.00 36.82 ?  547 PHE A CA    1 
ATOM   4389  C  C     . PHE A 1 547 ? 138.222 146.646 77.646  1.00 37.34 ?  547 PHE A C     1 
ATOM   4390  O  O     . PHE A 1 547 ? 138.318 147.865 77.813  1.00 38.01 ?  547 PHE A O     1 
ATOM   4391  C  CB    . PHE A 1 547 ? 139.808 146.122 79.500  1.00 35.38 ?  547 PHE A CB    1 
ATOM   4392  C  CG    . PHE A 1 547 ? 139.905 145.680 80.927  1.00 35.44 ?  547 PHE A CG    1 
ATOM   4393  C  CD1   . PHE A 1 547 ? 139.305 146.415 81.935  1.00 34.89 ?  547 PHE A CD1   1 
ATOM   4394  C  CD2   . PHE A 1 547 ? 140.594 144.530 81.263  1.00 32.16 ?  547 PHE A CD2   1 
ATOM   4395  C  CE1   . PHE A 1 547 ? 139.393 146.010 83.251  1.00 31.83 ?  547 PHE A CE1   1 
ATOM   4396  C  CE2   . PHE A 1 547 ? 140.684 144.121 82.577  1.00 34.52 ?  547 PHE A CE2   1 
ATOM   4397  C  CZ    . PHE A 1 547 ? 140.081 144.860 83.571  1.00 33.71 ?  547 PHE A CZ    1 
ATOM   4398  N  N     . GLU A 1 548 ? 137.883 146.110 76.475  1.00 43.65 ?  548 GLU A N     1 
ATOM   4399  C  CA    . GLU A 1 548 ? 137.596 146.953 75.323  1.00 46.68 ?  548 GLU A CA    1 
ATOM   4400  C  C     . GLU A 1 548 ? 136.372 147.824 75.585  1.00 47.86 ?  548 GLU A C     1 
ATOM   4401  O  O     . GLU A 1 548 ? 135.400 147.389 76.209  1.00 47.21 ?  548 GLU A O     1 
ATOM   4402  C  CB    . GLU A 1 548 ? 137.374 146.095 74.078  1.00 45.30 ?  548 GLU A CB    1 
ATOM   4403  C  CG    . GLU A 1 548 ? 138.108 146.597 72.847  1.00 46.87 ?  548 GLU A CG    1 
ATOM   4404  C  CD    . GLU A 1 548 ? 139.613 146.555 73.011  1.00 49.11 ?  548 GLU A CD    1 
ATOM   4405  O  OE1   . GLU A 1 548 ? 140.206 145.477 72.802  1.00 48.26 ?  548 GLU A OE1   1 
ATOM   4406  O  OE2   . GLU A 1 548 ? 140.204 147.602 73.352  1.00 47.53 -1 548 GLU A OE2   1 
ATOM   4407  N  N     . GLY A 1 549 ? 136.427 149.062 75.100  1.00 44.32 ?  549 GLY A N     1 
ATOM   4408  C  CA    . GLY A 1 549 ? 135.375 150.027 75.332  1.00 40.96 ?  549 GLY A CA    1 
ATOM   4409  C  C     . GLY A 1 549 ? 135.505 150.815 76.616  1.00 43.69 ?  549 GLY A C     1 
ATOM   4410  O  O     . GLY A 1 549 ? 134.653 151.671 76.885  1.00 44.76 ?  549 GLY A O     1 
ATOM   4411  N  N     . MET A 1 550 ? 136.539 150.555 77.413  1.00 43.09 ?  550 MET A N     1 
ATOM   4412  C  CA    . MET A 1 550 ? 136.758 151.236 78.681  1.00 40.92 ?  550 MET A CA    1 
ATOM   4413  C  C     . MET A 1 550 ? 138.172 151.790 78.705  1.00 41.67 ?  550 MET A C     1 
ATOM   4414  O  O     . MET A 1 550 ? 139.120 151.091 78.329  1.00 42.25 ?  550 MET A O     1 
ATOM   4415  C  CB    . MET A 1 550 ? 136.551 150.284 79.861  1.00 38.56 ?  550 MET A CB    1 
ATOM   4416  C  CG    . MET A 1 550 ? 135.294 150.543 80.662  1.00 42.56 ?  550 MET A CG    1 
ATOM   4417  S  SD    . MET A 1 550 ? 135.144 149.381 82.025  1.00 55.69 ?  550 MET A SD    1 
ATOM   4418  C  CE    . MET A 1 550 ? 135.193 147.823 81.144  1.00 41.52 ?  550 MET A CE    1 
ATOM   4419  N  N     . HIS A 1 551 ? 138.317 153.035 79.148  1.00 38.98 ?  551 HIS A N     1 
ATOM   4420  C  CA    . HIS A 1 551 ? 139.639 153.641 79.240  1.00 38.16 ?  551 HIS A CA    1 
ATOM   4421  C  C     . HIS A 1 551 ? 140.384 153.070 80.440  1.00 38.90 ?  551 HIS A C     1 
ATOM   4422  O  O     . HIS A 1 551 ? 139.906 153.153 81.576  1.00 40.01 ?  551 HIS A O     1 
ATOM   4423  C  CB    . HIS A 1 551 ? 139.523 155.159 79.353  1.00 39.46 ?  551 HIS A CB    1 
ATOM   4424  C  CG    . HIS A 1 551 ? 140.823 155.840 79.647  1.00 41.61 ?  551 HIS A CG    1 
ATOM   4425  N  ND1   . HIS A 1 551 ? 141.911 155.763 78.803  1.00 42.78 ?  551 HIS A ND1   1 
ATOM   4426  C  CD2   . HIS A 1 551 ? 141.211 156.610 80.691  1.00 42.39 ?  551 HIS A CD2   1 
ATOM   4427  C  CE1   . HIS A 1 551 ? 142.912 156.456 79.315  1.00 40.85 ?  551 HIS A CE1   1 
ATOM   4428  N  NE2   . HIS A 1 551 ? 142.514 156.979 80.460  1.00 41.74 ?  551 HIS A NE2   1 
ATOM   4429  N  N     . ILE A 1 552 ? 141.550 152.489 80.187  1.00 35.62 ?  552 ILE A N     1 
ATOM   4430  C  CA    . ILE A 1 552 ? 142.386 151.914 81.235  1.00 31.64 ?  552 ILE A CA    1 
ATOM   4431  C  C     . ILE A 1 552 ? 143.380 152.983 81.680  1.00 33.24 ?  552 ILE A C     1 
ATOM   4432  O  O     . ILE A 1 552 ? 144.169 153.459 80.848  1.00 36.10 ?  552 ILE A O     1 
ATOM   4433  C  CB    . ILE A 1 552 ? 143.113 150.657 80.745  1.00 33.70 ?  552 ILE A CB    1 
ATOM   4434  C  CG1   . ILE A 1 552 ? 142.101 149.568 80.389  1.00 32.99 ?  552 ILE A CG1   1 
ATOM   4435  C  CG2   . ILE A 1 552 ? 144.091 150.161 81.795  1.00 34.38 ?  552 ILE A CG2   1 
ATOM   4436  C  CD1   . ILE A 1 552 ? 142.710 148.375 79.698  1.00 34.55 ?  552 ILE A CD1   1 
ATOM   4437  N  N     . PRO A 1 553 ? 143.369 153.394 82.947  1.00 38.28 ?  553 PRO A N     1 
ATOM   4438  C  CA    . PRO A 1 553 ? 144.286 154.452 83.390  1.00 32.24 ?  553 PRO A CA    1 
ATOM   4439  C  C     . PRO A 1 553 ? 145.741 154.043 83.208  1.00 35.19 ?  553 PRO A C     1 
ATOM   4440  O  O     . PRO A 1 553 ? 146.154 152.949 83.598  1.00 36.48 ?  553 PRO A O     1 
ATOM   4441  C  CB    . PRO A 1 553 ? 143.930 154.631 84.871  1.00 31.02 ?  553 PRO A CB    1 
ATOM   4442  C  CG    . PRO A 1 553 ? 142.534 154.107 84.990  1.00 30.52 ?  553 PRO A CG    1 
ATOM   4443  C  CD    . PRO A 1 553 ? 142.448 152.975 84.016  1.00 32.28 ?  553 PRO A CD    1 
ATOM   4444  N  N     . THR A 1 554 ? 146.518 154.938 82.609  1.00 39.01 ?  554 THR A N     1 
ATOM   4445  C  CA    . THR A 1 554 ? 147.928 154.718 82.353  1.00 38.97 ?  554 THR A CA    1 
ATOM   4446  C  C     . THR A 1 554 ? 148.759 155.379 83.449  1.00 37.81 ?  554 THR A C     1 
ATOM   4447  O  O     . THR A 1 554 ? 148.233 155.862 84.456  1.00 39.91 ?  554 THR A O     1 
ATOM   4448  C  CB    . THR A 1 554 ? 148.299 155.247 80.966  1.00 37.93 ?  554 THR A CB    1 
ATOM   4449  O  OG1   . THR A 1 554 ? 148.198 156.675 80.955  1.00 40.49 ?  554 THR A OG1   1 
ATOM   4450  C  CG2   . THR A 1 554 ? 147.368 154.672 79.911  1.00 35.01 ?  554 THR A CG2   1 
ATOM   4451  N  N     . THR A 1 555 ? 150.080 155.400 83.258  1.00 38.74 ?  555 THR A N     1 
ATOM   4452  C  CA    . THR A 1 555 ? 150.949 156.072 84.217  1.00 36.20 ?  555 THR A CA    1 
ATOM   4453  C  C     . THR A 1 555 ? 150.751 157.581 84.193  1.00 38.34 ?  555 THR A C     1 
ATOM   4454  O  O     . THR A 1 555 ? 150.855 158.234 85.235  1.00 40.28 ?  555 THR A O     1 
ATOM   4455  C  CB    . THR A 1 555 ? 152.411 155.724 83.942  1.00 38.61 ?  555 THR A CB    1 
ATOM   4456  O  OG1   . THR A 1 555 ? 152.684 155.857 82.541  1.00 41.79 ?  555 THR A OG1   1 
ATOM   4457  C  CG2   . THR A 1 555 ? 152.709 154.297 84.380  1.00 37.28 ?  555 THR A CG2   1 
ATOM   4458  N  N     . GLU A 1 556 ? 150.472 158.154 83.018  1.00 39.91 ?  556 GLU A N     1 
ATOM   4459  C  CA    . GLU A 1 556 ? 150.185 159.583 82.943  1.00 39.82 ?  556 GLU A CA    1 
ATOM   4460  C  C     . GLU A 1 556 ? 148.881 159.921 83.657  1.00 38.55 ?  556 GLU A C     1 
ATOM   4461  O  O     . GLU A 1 556 ? 148.791 160.941 84.353  1.00 40.13 ?  556 GLU A O     1 
ATOM   4462  C  CB    . GLU A 1 556 ? 150.131 160.031 81.483  1.00 40.74 ?  556 GLU A CB    1 
ATOM   4463  C  CG    . GLU A 1 556 ? 150.118 161.538 81.298  1.00 43.25 ?  556 GLU A CG    1 
ATOM   4464  C  CD    . GLU A 1 556 ? 151.317 162.213 81.934  1.00 44.78 ?  556 GLU A CD    1 
ATOM   4465  O  OE1   . GLU A 1 556 ? 152.436 161.666 81.830  1.00 41.96 ?  556 GLU A OE1   1 
ATOM   4466  O  OE2   . GLU A 1 556 ? 151.142 163.291 82.540  1.00 44.90 -1 556 GLU A OE2   1 
ATOM   4467  N  N     . ASP A 1 557 ? 147.859 159.079 83.493  1.00 40.02 ?  557 ASP A N     1 
ATOM   4468  C  CA    . ASP A 1 557 ? 146.608 159.283 84.213  1.00 36.22 ?  557 ASP A CA    1 
ATOM   4469  C  C     . ASP A 1 557 ? 146.822 159.186 85.716  1.00 36.15 ?  557 ASP A C     1 
ATOM   4470  O  O     . ASP A 1 557 ? 146.237 159.953 86.488  1.00 37.41 ?  557 ASP A O     1 
ATOM   4471  C  CB    . ASP A 1 557 ? 145.563 158.268 83.751  1.00 35.10 ?  557 ASP A CB    1 
ATOM   4472  C  CG    . ASP A 1 557 ? 144.941 158.639 82.420  1.00 40.32 ?  557 ASP A CG    1 
ATOM   4473  O  OD1   . ASP A 1 557 ? 144.792 159.848 82.149  1.00 43.55 ?  557 ASP A OD1   1 
ATOM   4474  O  OD2   . ASP A 1 557 ? 144.604 157.720 81.645  1.00 42.22 -1 557 ASP A OD2   1 
ATOM   4475  N  N     . TRP A 1 558 ? 147.665 158.247 86.153  1.00 29.19 ?  558 TRP A N     1 
ATOM   4476  C  CA    . TRP A 1 558 ? 147.967 158.133 87.574  1.00 27.33 ?  558 TRP A CA    1 
ATOM   4477  C  C     . TRP A 1 558 ? 148.756 159.331 88.082  1.00 29.30 ?  558 TRP A C     1 
ATOM   4478  O  O     . TRP A 1 558 ? 148.557 159.758 89.223  1.00 33.21 ?  558 TRP A O     1 
ATOM   4479  C  CB    . TRP A 1 558 ? 148.724 156.836 87.845  1.00 29.55 ?  558 TRP A CB    1 
ATOM   4480  C  CG    . TRP A 1 558 ? 147.828 155.673 88.124  1.00 27.37 ?  558 TRP A CG    1 
ATOM   4481  C  CD1   . TRP A 1 558 ? 147.562 154.625 87.294  1.00 27.28 ?  558 TRP A CD1   1 
ATOM   4482  C  CD2   . TRP A 1 558 ? 147.076 155.438 89.320  1.00 28.16 ?  558 TRP A CD2   1 
ATOM   4483  N  NE1   . TRP A 1 558 ? 146.694 153.750 87.899  1.00 30.85 ?  558 TRP A NE1   1 
ATOM   4484  C  CE2   . TRP A 1 558 ? 146.382 154.225 89.145  1.00 28.47 ?  558 TRP A CE2   1 
ATOM   4485  C  CE3   . TRP A 1 558 ? 146.928 156.131 90.524  1.00 30.88 ?  558 TRP A CE3   1 
ATOM   4486  C  CZ2   . TRP A 1 558 ? 145.552 153.693 90.126  1.00 26.24 ?  558 TRP A CZ2   1 
ATOM   4487  C  CZ3   . TRP A 1 558 ? 146.102 155.601 91.498  1.00 26.03 ?  558 TRP A CZ3   1 
ATOM   4488  C  CH2   . TRP A 1 558 ? 145.425 154.395 91.293  1.00 22.82 ?  558 TRP A CH2   1 
ATOM   4489  N  N     . LYS A 1 559 ? 149.650 159.887 87.262  1.00 36.33 ?  559 LYS A N     1 
ATOM   4490  C  CA    . LYS A 1 559 ? 150.352 161.107 87.652  1.00 32.59 ?  559 LYS A CA    1 
ATOM   4491  C  C     . LYS A 1 559 ? 149.383 162.274 87.794  1.00 31.12 ?  559 LYS A C     1 
ATOM   4492  O  O     . LYS A 1 559 ? 149.489 163.074 88.733  1.00 34.31 ?  559 LYS A O     1 
ATOM   4493  C  CB    . LYS A 1 559 ? 151.436 161.439 86.626  1.00 36.36 ?  559 LYS A CB    1 
ATOM   4494  C  CG    . LYS A 1 559 ? 152.742 160.695 86.829  1.00 38.00 ?  559 LYS A CG    1 
ATOM   4495  C  CD    . LYS A 1 559 ? 153.437 160.442 85.503  1.00 39.16 ?  559 LYS A CD    1 
ATOM   4496  C  CE    . LYS A 1 559 ? 154.605 159.486 85.661  1.00 37.84 ?  559 LYS A CE    1 
ATOM   4497  N  NZ    . LYS A 1 559 ? 155.719 159.817 84.731  1.00 39.17 1  559 LYS A NZ    1 
ATOM   4498  N  N     . LYS A 1 560 ? 148.432 162.386 86.865  1.00 33.31 ?  560 LYS A N     1 
ATOM   4499  C  CA    . LYS A 1 560 ? 147.416 163.429 86.965  1.00 32.75 ?  560 LYS A CA    1 
ATOM   4500  C  C     . LYS A 1 560 ? 146.564 163.247 88.215  1.00 36.91 ?  560 LYS A C     1 
ATOM   4501  O  O     . LYS A 1 560 ? 146.231 164.222 88.895  1.00 36.57 ?  560 LYS A O     1 
ATOM   4502  C  CB    . LYS A 1 560 ? 146.539 163.433 85.714  1.00 32.44 ?  560 LYS A CB    1 
ATOM   4503  C  CG    . LYS A 1 560 ? 147.261 163.862 84.450  1.00 37.98 ?  560 LYS A CG    1 
ATOM   4504  C  CD    . LYS A 1 560 ? 146.362 163.726 83.233  1.00 38.81 ?  560 LYS A CD    1 
ATOM   4505  C  CE    . LYS A 1 560 ? 147.151 163.864 81.943  1.00 35.97 ?  560 LYS A CE    1 
ATOM   4506  N  NZ    . LYS A 1 560 ? 146.389 163.352 80.774  1.00 38.72 1  560 LYS A NZ    1 
ATOM   4507  N  N     . LEU A 1 561 ? 146.202 162.001 88.531  1.00 35.84 ?  561 LEU A N     1 
ATOM   4508  C  CA    . LEU A 1 561 ? 145.440 161.737 89.748  1.00 28.48 ?  561 LEU A CA    1 
ATOM   4509  C  C     . LEU A 1 561 ? 146.252 162.068 90.994  1.00 28.17 ?  561 LEU A C     1 
ATOM   4510  O  O     . LEU A 1 561 ? 145.708 162.580 91.977  1.00 30.26 ?  561 LEU A O     1 
ATOM   4511  C  CB    . LEU A 1 561 ? 144.982 160.279 89.778  1.00 28.29 ?  561 LEU A CB    1 
ATOM   4512  C  CG    . LEU A 1 561 ? 144.144 159.894 90.999  1.00 29.77 ?  561 LEU A CG    1 
ATOM   4513  C  CD1   . LEU A 1 561 ? 142.921 160.788 91.097  1.00 26.57 ?  561 LEU A CD1   1 
ATOM   4514  C  CD2   . LEU A 1 561 ? 143.739 158.434 90.949  1.00 24.71 ?  561 LEU A CD2   1 
ATOM   4515  N  N     . LYS A 1 562 ? 147.551 161.768 90.977  1.00 29.68 ?  562 LYS A N     1 
ATOM   4516  C  CA    . LYS A 1 562 ? 148.414 162.115 92.102  1.00 30.82 ?  562 LYS A CA    1 
ATOM   4517  C  C     . LYS A 1 562 ? 148.477 163.624 92.301  1.00 35.47 ?  562 LYS A C     1 
ATOM   4518  O  O     . LYS A 1 562 ? 148.397 164.113 93.432  1.00 35.60 ?  562 LYS A O     1 
ATOM   4519  C  CB    . LYS A 1 562 ? 149.812 161.541 91.877  1.00 28.95 ?  562 LYS A CB    1 
ATOM   4520  C  CG    . LYS A 1 562 ? 150.852 161.980 92.889  1.00 29.87 ?  562 LYS A CG    1 
ATOM   4521  C  CD    . LYS A 1 562 ? 152.240 161.546 92.452  1.00 30.17 ?  562 LYS A CD    1 
ATOM   4522  C  CE    . LYS A 1 562 ? 153.297 161.952 93.461  1.00 32.22 ?  562 LYS A CE    1 
ATOM   4523  N  NZ    . LYS A 1 562 ? 154.543 161.155 93.298  1.00 34.97 1  562 LYS A NZ    1 
ATOM   4524  N  N     . ALA A 1 563 ? 148.609 164.377 91.206  1.00 34.18 ?  563 ALA A N     1 
ATOM   4525  C  CA    . ALA A 1 563 ? 148.602 165.834 91.307  1.00 31.91 ?  563 ALA A CA    1 
ATOM   4526  C  C     . ALA A 1 563 ? 147.257 166.345 91.810  1.00 31.32 ?  563 ALA A C     1 
ATOM   4527  O  O     . ALA A 1 563 ? 147.200 167.281 92.617  1.00 37.17 ?  563 ALA A O     1 
ATOM   4528  C  CB    . ALA A 1 563 ? 148.943 166.455 89.952  1.00 33.30 ?  563 ALA A CB    1 
ATOM   4529  N  N     . PHE A 1 564 ? 146.162 165.742 91.342  1.00 33.10 ?  564 PHE A N     1 
ATOM   4530  C  CA    . PHE A 1 564 ? 144.833 166.141 91.793  1.00 30.55 ?  564 PHE A CA    1 
ATOM   4531  C  C     . PHE A 1 564 ? 144.657 165.889 93.285  1.00 31.17 ?  564 PHE A C     1 
ATOM   4532  O  O     . PHE A 1 564 ? 144.075 166.714 93.999  1.00 35.80 ?  564 PHE A O     1 
ATOM   4533  C  CB    . PHE A 1 564 ? 143.773 165.391 90.987  1.00 30.41 ?  564 PHE A CB    1 
ATOM   4534  C  CG    . PHE A 1 564 ? 142.392 165.963 91.112  1.00 30.40 ?  564 PHE A CG    1 
ATOM   4535  C  CD1   . PHE A 1 564 ? 141.984 167.008 90.303  1.00 32.82 ?  564 PHE A CD1   1 
ATOM   4536  C  CD2   . PHE A 1 564 ? 141.494 165.445 92.030  1.00 33.53 ?  564 PHE A CD2   1 
ATOM   4537  C  CE1   . PHE A 1 564 ? 140.710 167.531 90.413  1.00 38.30 ?  564 PHE A CE1   1 
ATOM   4538  C  CE2   . PHE A 1 564 ? 140.221 165.964 92.145  1.00 34.07 ?  564 PHE A CE2   1 
ATOM   4539  C  CZ    . PHE A 1 564 ? 139.828 167.008 91.336  1.00 36.68 ?  564 PHE A CZ    1 
ATOM   4540  N  N     . VAL A 1 565 ? 145.148 164.748 93.773  1.00 32.53 ?  565 VAL A N     1 
ATOM   4541  C  CA    . VAL A 1 565 ? 145.066 164.442 95.197  1.00 27.22 ?  565 VAL A CA    1 
ATOM   4542  C  C     . VAL A 1 565 ? 145.940 165.399 95.998  1.00 31.96 ?  565 VAL A C     1 
ATOM   4543  O  O     . VAL A 1 565 ? 145.560 165.842 97.089  1.00 36.49 ?  565 VAL A O     1 
ATOM   4544  C  CB    . VAL A 1 565 ? 145.450 162.972 95.445  1.00 26.89 ?  565 VAL A CB    1 
ATOM   4545  C  CG1   . VAL A 1 565 ? 145.718 162.720 96.920  1.00 28.44 ?  565 VAL A CG1   1 
ATOM   4546  C  CG2   . VAL A 1 565 ? 144.354 162.056 94.942  1.00 30.95 ?  565 VAL A CG2   1 
ATOM   4547  N  N     . ALA A 1 566 ? 147.117 165.739 95.472  1.00 35.27 ?  566 ALA A N     1 
ATOM   4548  C  CA    . ALA A 1 566 ? 147.980 166.697 96.155  1.00 33.21 ?  566 ALA A CA    1 
ATOM   4549  C  C     . ALA A 1 566 ? 147.309 168.061 96.265  1.00 36.36 ?  566 ALA A C     1 
ATOM   4550  O  O     . ALA A 1 566 ? 147.407 168.729 97.302  1.00 36.75 ?  566 ALA A O     1 
ATOM   4551  C  CB    . ALA A 1 566 ? 149.317 166.813 95.424  1.00 32.08 ?  566 ALA A CB    1 
ATOM   4552  N  N     . GLU A 1 567 ? 146.623 168.492 95.206  1.00 36.78 ?  567 GLU A N     1 
ATOM   4553  C  CA    . GLU A 1 567 ? 145.989 169.807 95.221  1.00 35.42 ?  567 GLU A CA    1 
ATOM   4554  C  C     . GLU A 1 567 ? 144.734 169.824 96.090  1.00 38.61 ?  567 GLU A C     1 
ATOM   4555  O  O     . GLU A 1 567 ? 144.501 170.787 96.829  1.00 41.33 ?  567 GLU A O     1 
ATOM   4556  C  CB    . GLU A 1 567 ? 145.659 170.248 93.797  1.00 37.27 ?  567 GLU A CB    1 
ATOM   4557  C  CG    . GLU A 1 567 ? 146.688 171.185 93.182  1.00 42.63 ?  567 GLU A CG    1 
ATOM   4558  C  CD    . GLU A 1 567 ? 148.042 170.530 92.996  1.00 45.29 ?  567 GLU A CD    1 
ATOM   4559  O  OE1   . GLU A 1 567 ? 148.939 170.763 93.833  1.00 42.73 ?  567 GLU A OE1   1 
ATOM   4560  O  OE2   . GLU A 1 567 ? 148.215 169.789 92.005  1.00 42.47 -1 567 GLU A OE2   1 
ATOM   4561  N  N     . HIS A 1 568 ? 143.916 168.771 96.021  1.00 39.00 ?  568 HIS A N     1 
ATOM   4562  C  CA    . HIS A 1 568 ? 142.593 168.788 96.629  1.00 36.41 ?  568 HIS A CA    1 
ATOM   4563  C  C     . HIS A 1 568 ? 142.445 167.872 97.836  1.00 35.41 ?  568 HIS A C     1 
ATOM   4564  O  O     . HIS A 1 568 ? 141.473 168.021 98.584  1.00 41.18 ?  568 HIS A O     1 
ATOM   4565  C  CB    . HIS A 1 568 ? 141.531 168.411 95.586  1.00 33.87 ?  568 HIS A CB    1 
ATOM   4566  C  CG    . HIS A 1 568 ? 141.338 169.445 94.522  1.00 38.50 ?  568 HIS A CG    1 
ATOM   4567  N  ND1   . HIS A 1 568 ? 141.013 170.753 94.806  1.00 36.84 ?  568 HIS A ND1   1 
ATOM   4568  C  CD2   . HIS A 1 568 ? 141.428 169.364 93.174  1.00 37.26 ?  568 HIS A CD2   1 
ATOM   4569  C  CE1   . HIS A 1 568 ? 140.909 171.434 93.679  1.00 40.24 ?  568 HIS A CE1   1 
ATOM   4570  N  NE2   . HIS A 1 568 ? 141.156 170.615 92.673  1.00 40.01 ?  568 HIS A NE2   1 
ATOM   4571  N  N     . GLY A 1 569 ? 143.365 166.941 98.052  1.00 28.17 ?  569 GLY A N     1 
ATOM   4572  C  CA    . GLY A 1 569 ? 143.229 166.015 99.153  1.00 28.04 ?  569 GLY A CA    1 
ATOM   4573  C  C     . GLY A 1 569 ? 142.345 164.831 98.809  1.00 28.41 ?  569 GLY A C     1 
ATOM   4574  O  O     . GLY A 1 569 ? 141.920 164.633 97.669  1.00 34.15 ?  569 GLY A O     1 
ATOM   4575  N  N     . MET A 1 570 ? 142.070 164.027 99.832  1.00 25.27 ?  570 MET A N     1 
ATOM   4576  C  CA    . MET A 1 570 ? 141.237 162.840 99.695  1.00 25.78 ?  570 MET A CA    1 
ATOM   4577  C  C     . MET A 1 570 ? 140.234 162.810 100.838 1.00 24.58 ?  570 MET A C     1 
ATOM   4578  O  O     . MET A 1 570 ? 140.611 162.978 102.001 1.00 27.32 ?  570 MET A O     1 
ATOM   4579  C  CB    . MET A 1 570 ? 142.089 161.567 99.686  1.00 24.02 ?  570 MET A CB    1 
ATOM   4580  C  CG    . MET A 1 570 ? 142.603 161.184 98.306  1.00 20.26 ?  570 MET A CG    1 
ATOM   4581  S  SD    . MET A 1 570 ? 142.943 159.426 98.122  1.00 39.13 ?  570 MET A SD    1 
ATOM   4582  C  CE    . MET A 1 570 ? 141.843 158.735 99.348  1.00 25.71 ?  570 MET A CE    1 
ATOM   4583  N  N     . TYR A 1 571 ? 138.961 162.596 100.504 1.00 21.91 ?  571 TYR A N     1 
ATOM   4584  C  CA    . TYR A 1 571 ? 137.907 162.653 101.509 1.00 14.14 ?  571 TYR A CA    1 
ATOM   4585  C  C     . TYR A 1 571 ? 137.896 161.430 102.417 1.00 20.21 ?  571 TYR A C     1 
ATOM   4586  O  O     . TYR A 1 571 ? 137.604 161.556 103.611 1.00 24.53 ?  571 TYR A O     1 
ATOM   4587  C  CB    . TYR A 1 571 ? 136.544 162.806 100.835 1.00 22.96 ?  571 TYR A CB    1 
ATOM   4588  C  CG    . TYR A 1 571 ? 135.420 163.107 101.799 1.00 24.15 ?  571 TYR A CG    1 
ATOM   4589  C  CD1   . TYR A 1 571 ? 135.239 164.387 102.303 1.00 23.12 ?  571 TYR A CD1   1 
ATOM   4590  C  CD2   . TYR A 1 571 ? 134.546 162.111 102.210 1.00 18.53 ?  571 TYR A CD2   1 
ATOM   4591  C  CE1   . TYR A 1 571 ? 134.216 164.667 103.185 1.00 22.43 ?  571 TYR A CE1   1 
ATOM   4592  C  CE2   . TYR A 1 571 ? 133.521 162.382 103.093 1.00 19.81 ?  571 TYR A CE2   1 
ATOM   4593  C  CZ    . TYR A 1 571 ? 133.359 163.662 103.575 1.00 25.46 ?  571 TYR A CZ    1 
ATOM   4594  O  OH    . TYR A 1 571 ? 132.339 163.939 104.455 1.00 28.14 ?  571 TYR A OH    1 
ATOM   4595  N  N     . HIS A 1 572 ? 138.206 160.253 101.885 1.00 22.73 ?  572 HIS A N     1 
ATOM   4596  C  CA    . HIS A 1 572 ? 138.137 159.011 102.642 1.00 13.70 ?  572 HIS A CA    1 
ATOM   4597  C  C     . HIS A 1 572 ? 139.537 158.557 103.027 1.00 10.41 ?  572 HIS A C     1 
ATOM   4598  O  O     . HIS A 1 572 ? 140.434 158.508 102.181 1.00 22.35 ?  572 HIS A O     1 
ATOM   4599  C  CB    . HIS A 1 572 ? 137.440 157.914 101.837 1.00 14.68 ?  572 HIS A CB    1 
ATOM   4600  C  CG    . HIS A 1 572 ? 136.141 158.341 101.228 1.00 15.57 ?  572 HIS A CG    1 
ATOM   4601  N  ND1   . HIS A 1 572 ? 136.053 158.869 99.959  1.00 16.85 ?  572 HIS A ND1   1 
ATOM   4602  C  CD2   . HIS A 1 572 ? 134.876 158.314 101.713 1.00 9.72  ?  572 HIS A CD2   1 
ATOM   4603  C  CE1   . HIS A 1 572 ? 134.792 159.152 99.688  1.00 16.23 ?  572 HIS A CE1   1 
ATOM   4604  N  NE2   . HIS A 1 572 ? 134.058 158.825 100.736 1.00 23.78 ?  572 HIS A NE2   1 
ATOM   4605  N  N     . SER A 1 573 ? 139.720 158.235 104.309 1.00 5.57  ?  573 SER A N     1 
ATOM   4606  C  CA    . SER A 1 573 ? 140.976 157.634 104.742 1.00 7.60  ?  573 SER A CA    1 
ATOM   4607  C  C     . SER A 1 573 ? 141.163 156.257 104.122 1.00 11.79 ?  573 SER A C     1 
ATOM   4608  O  O     . SER A 1 573 ? 142.282 155.882 103.751 1.00 19.77 ?  573 SER A O     1 
ATOM   4609  C  CB    . SER A 1 573 ? 141.017 157.549 106.265 1.00 15.52 ?  573 SER A CB    1 
ATOM   4610  O  OG    . SER A 1 573 ? 139.888 156.854 106.758 1.00 22.99 ?  573 SER A OG    1 
ATOM   4611  N  N     . TYR A 1 574 ? 140.082 155.491 104.009 1.00 12.39 ?  574 TYR A N     1 
ATOM   4612  C  CA    . TYR A 1 574 ? 140.101 154.178 103.384 1.00 1.15  ?  574 TYR A CA    1 
ATOM   4613  C  C     . TYR A 1 574 ? 138.896 154.063 102.466 1.00 8.90  ?  574 TYR A C     1 
ATOM   4614  O  O     . TYR A 1 574 ? 137.820 154.578 102.780 1.00 16.56 ?  574 TYR A O     1 
ATOM   4615  C  CB    . TYR A 1 574 ? 140.095 153.062 104.435 1.00 11.68 ?  574 TYR A CB    1 
ATOM   4616  C  CG    . TYR A 1 574 ? 141.199 153.208 105.456 1.00 8.23  ?  574 TYR A CG    1 
ATOM   4617  C  CD1   . TYR A 1 574 ? 141.014 153.978 106.596 1.00 10.27 ?  574 TYR A CD1   1 
ATOM   4618  C  CD2   . TYR A 1 574 ? 142.426 152.587 105.277 1.00 8.46  ?  574 TYR A CD2   1 
ATOM   4619  C  CE1   . TYR A 1 574 ? 142.016 154.126 107.526 1.00 6.62  ?  574 TYR A CE1   1 
ATOM   4620  C  CE2   . TYR A 1 574 ? 143.435 152.728 106.206 1.00 11.12 ?  574 TYR A CE2   1 
ATOM   4621  C  CZ    . TYR A 1 574 ? 143.223 153.499 107.329 1.00 5.82  ?  574 TYR A CZ    1 
ATOM   4622  O  OH    . TYR A 1 574 ? 144.222 153.642 108.260 1.00 18.04 ?  574 TYR A OH    1 
ATOM   4623  N  N     . ARG A 1 575 ? 139.080 153.393 101.334 1.00 11.09 ?  575 ARG A N     1 
ATOM   4624  C  CA    . ARG A 1 575 ? 138.050 153.326 100.306 1.00 4.65  ?  575 ARG A CA    1 
ATOM   4625  C  C     . ARG A 1 575 ? 137.636 151.911 99.944  1.00 9.69  ?  575 ARG A C     1 
ATOM   4626  O  O     . ARG A 1 575 ? 136.446 151.656 99.749  1.00 19.78 ?  575 ARG A O     1 
ATOM   4627  C  CB    . ARG A 1 575 ? 138.529 154.040 99.036  1.00 17.10 ?  575 ARG A CB    1 
ATOM   4628  C  CG    . ARG A 1 575 ? 138.810 155.518 99.210  1.00 11.51 ?  575 ARG A CG    1 
ATOM   4629  C  CD    . ARG A 1 575 ? 139.824 155.990 98.185  1.00 11.59 ?  575 ARG A CD    1 
ATOM   4630  N  NE    . ARG A 1 575 ? 141.150 155.443 98.448  1.00 16.30 ?  575 ARG A NE    1 
ATOM   4631  C  CZ    . ARG A 1 575 ? 141.696 154.439 97.774  1.00 14.92 ?  575 ARG A CZ    1 
ATOM   4632  N  NH1   . ARG A 1 575 ? 141.059 153.850 96.776  1.00 12.79 1  575 ARG A NH1   1 
ATOM   4633  N  NH2   . ARG A 1 575 ? 142.910 154.017 98.110  1.00 14.91 ?  575 ARG A NH2   1 
ATOM   4634  N  N     . LEU A 1 576 ? 138.581 150.980 99.846  1.00 19.64 ?  576 LEU A N     1 
ATOM   4635  C  CA    . LEU A 1 576 ? 138.326 149.662 99.287  1.00 12.26 ?  576 LEU A CA    1 
ATOM   4636  C  C     . LEU A 1 576 ? 138.613 148.588 100.323 1.00 3.41  ?  576 LEU A C     1 
ATOM   4637  O  O     . LEU A 1 576 ? 139.693 148.570 100.921 1.00 19.60 ?  576 LEU A O     1 
ATOM   4638  C  CB    . LEU A 1 576 ? 139.185 149.424 98.041  1.00 4.91  ?  576 LEU A CB    1 
ATOM   4639  C  CG    . LEU A 1 576 ? 139.177 150.516 96.972  1.00 8.38  ?  576 LEU A CG    1 
ATOM   4640  C  CD1   . LEU A 1 576 ? 140.218 150.217 95.909  1.00 11.87 ?  576 LEU A CD1   1 
ATOM   4641  C  CD2   . LEU A 1 576 ? 137.801 150.657 96.348  1.00 10.83 ?  576 LEU A CD2   1 
ATOM   4642  N  N     . CYS A 1 577 ? 137.645 147.699 100.532 1.00 1.85  ?  577 CYS A N     1 
ATOM   4643  C  CA    . CYS A 1 577 ? 137.857 146.479 101.299 1.00 6.52  ?  577 CYS A CA    1 
ATOM   4644  C  C     . CYS A 1 577 ? 136.904 145.428 100.753 1.00 16.04 ?  577 CYS A C     1 
ATOM   4645  O  O     . CYS A 1 577 ? 135.733 145.724 100.501 1.00 21.38 ?  577 CYS A O     1 
ATOM   4646  C  CB    . CYS A 1 577 ? 137.639 146.699 102.803 1.00 5.82  ?  577 CYS A CB    1 
ATOM   4647  S  SG    . CYS A 1 577 ? 135.926 146.650 103.384 1.00 27.63 ?  577 CYS A SG    1 
ATOM   4648  N  N     . ILE A 1 578 ? 137.408 144.217 100.551 1.00 8.13  ?  578 ILE A N     1 
ATOM   4649  C  CA    . ILE A 1 578 ? 136.645 143.148 99.919  1.00 11.51 ?  578 ILE A CA    1 
ATOM   4650  C  C     . ILE A 1 578 ? 136.100 142.254 101.027 1.00 8.57  ?  578 ILE A C     1 
ATOM   4651  O  O     . ILE A 1 578 ? 136.825 141.441 101.604 1.00 10.89 ?  578 ILE A O     1 
ATOM   4652  C  CB    . ILE A 1 578 ? 137.492 142.365 98.913  1.00 12.84 ?  578 ILE A CB    1 
ATOM   4653  C  CG1   . ILE A 1 578 ? 138.108 143.324 97.892  1.00 0.32  ?  578 ILE A CG1   1 
ATOM   4654  C  CG2   . ILE A 1 578 ? 136.646 141.322 98.208  1.00 8.42  ?  578 ILE A CG2   1 
ATOM   4655  C  CD1   . ILE A 1 578 ? 138.678 142.638 96.681  1.00 9.81  ?  578 ILE A CD1   1 
ATOM   4656  N  N     . ALA A 1 579 ? 134.815 142.408 101.318 1.00 16.56 ?  579 ALA A N     1 
ATOM   4657  C  CA    . ALA A 1 579 ? 134.078 141.652 102.317 1.00 8.89  ?  579 ALA A CA    1 
ATOM   4658  C  C     . ALA A 1 579 ? 133.635 140.308 101.752 1.00 16.81 ?  579 ALA A C     1 
ATOM   4659  O  O     . ALA A 1 579 ? 133.599 140.117 100.534 1.00 21.14 ?  579 ALA A O     1 
ATOM   4660  C  CB    . ALA A 1 579 ? 132.868 142.456 102.786 1.00 13.01 ?  579 ALA A CB    1 
ATOM   4661  N  N     . PRO A 1 580 ? 133.315 139.339 102.617 1.00 24.08 ?  580 PRO A N     1 
ATOM   4662  C  CA    . PRO A 1 580 ? 132.876 138.026 102.112 1.00 20.95 ?  580 PRO A CA    1 
ATOM   4663  C  C     . PRO A 1 580 ? 131.615 138.069 101.261 1.00 25.56 ?  580 PRO A C     1 
ATOM   4664  O  O     . PRO A 1 580 ? 131.477 137.238 100.352 1.00 31.34 ?  580 PRO A O     1 
ATOM   4665  C  CB    . PRO A 1 580 ? 132.661 137.208 103.396 1.00 17.28 ?  580 PRO A CB    1 
ATOM   4666  C  CG    . PRO A 1 580 ? 132.642 138.203 104.511 1.00 20.67 ?  580 PRO A CG    1 
ATOM   4667  C  CD    . PRO A 1 580 ? 133.520 139.320 104.074 1.00 20.22 ?  580 PRO A CD    1 
ATOM   4668  N  N     . THR A 1 581 ? 130.695 138.998 101.523 1.00 21.90 ?  581 THR A N     1 
ATOM   4669  C  CA    . THR A 1 581 ? 129.441 139.129 100.774 1.00 27.67 ?  581 THR A CA    1 
ATOM   4670  C  C     . THR A 1 581 ? 128.651 137.817 100.798 1.00 31.22 ?  581 THR A C     1 
ATOM   4671  O  O     . THR A 1 581 ? 128.450 137.151 99.783  1.00 32.14 ?  581 THR A O     1 
ATOM   4672  C  CB    . THR A 1 581 ? 129.689 139.586 99.332  1.00 27.73 ?  581 THR A CB    1 
ATOM   4673  O  OG1   . THR A 1 581 ? 130.108 138.470 98.536  1.00 23.00 ?  581 THR A OG1   1 
ATOM   4674  C  CG2   . THR A 1 581 ? 130.746 140.672 99.280  1.00 28.64 ?  581 THR A CG2   1 
ATOM   4675  N  N     . GLY A 1 582 ? 128.204 137.467 102.001 1.00 28.49 ?  582 GLY A N     1 
ATOM   4676  C  CA    . GLY A 1 582 ? 127.557 136.190 102.233 1.00 31.03 ?  582 GLY A CA    1 
ATOM   4677  C  C     . GLY A 1 582 ? 126.272 135.949 101.467 1.00 34.80 ?  582 GLY A C     1 
ATOM   4678  O  O     . GLY A 1 582 ? 126.230 135.090 100.581 1.00 33.60 ?  582 GLY A O     1 
ATOM   4679  N  N     . SER A 1 583 ? 125.215 136.695 101.789 1.00 34.42 ?  583 SER A N     1 
ATOM   4680  C  CA    . SER A 1 583 ? 123.899 136.438 101.216 1.00 38.66 ?  583 SER A CA    1 
ATOM   4681  C  C     . SER A 1 583 ? 123.537 137.367 100.068 1.00 35.70 ?  583 SER A C     1 
ATOM   4682  O  O     . SER A 1 583 ? 122.681 137.011 99.253  1.00 34.27 ?  583 SER A O     1 
ATOM   4683  C  CB    . SER A 1 583 ? 122.819 136.542 102.299 1.00 40.58 ?  583 SER A CB    1 
ATOM   4684  O  OG    . SER A 1 583 ? 122.850 135.415 103.158 1.00 41.67 ?  583 SER A OG    1 
ATOM   4685  N  N     . ILE A 1 584 ? 124.155 138.547 99.980  1.00 32.67 ?  584 ILE A N     1 
ATOM   4686  C  CA    . ILE A 1 584 ? 123.867 139.444 98.867  1.00 26.88 ?  584 ILE A CA    1 
ATOM   4687  C  C     . ILE A 1 584 ? 124.367 138.878 97.546  1.00 29.09 ?  584 ILE A C     1 
ATOM   4688  O  O     . ILE A 1 584 ? 123.879 139.276 96.483  1.00 36.37 ?  584 ILE A O     1 
ATOM   4689  C  CB    . ILE A 1 584 ? 124.468 140.840 99.117  1.00 33.33 ?  584 ILE A CB    1 
ATOM   4690  C  CG1   . ILE A 1 584 ? 125.973 140.742 99.374  1.00 34.20 ?  584 ILE A CG1   1 
ATOM   4691  C  CG2   . ILE A 1 584 ? 123.750 141.532 100.266 1.00 34.09 ?  584 ILE A CG2   1 
ATOM   4692  C  CD1   . ILE A 1 584 ? 126.573 141.982 100.001 1.00 28.91 ?  584 ILE A CD1   1 
ATOM   4693  N  N     . SER A 1 585 ? 125.334 137.959 97.582  1.00 30.54 ?  585 SER A N     1 
ATOM   4694  C  CA    . SER A 1 585 ? 125.798 137.328 96.351  1.00 27.64 ?  585 SER A CA    1 
ATOM   4695  C  C     . SER A 1 585 ? 124.715 136.459 95.727  1.00 26.77 ?  585 SER A C     1 
ATOM   4696  O  O     . SER A 1 585 ? 124.688 136.286 94.504  1.00 27.43 ?  585 SER A O     1 
ATOM   4697  C  CB    . SER A 1 585 ? 127.054 136.502 96.624  1.00 24.39 ?  585 SER A CB    1 
ATOM   4698  O  OG    . SER A 1 585 ? 126.808 135.511 97.605  1.00 31.13 ?  585 SER A OG    1 
ATOM   4699  N  N     . TYR A 1 586 ? 123.824 135.896 96.547  1.00 34.80 ?  586 TYR A N     1 
ATOM   4700  C  CA    . TYR A 1 586 ? 122.694 135.144 96.013  1.00 33.30 ?  586 TYR A CA    1 
ATOM   4701  C  C     . TYR A 1 586 ? 121.741 136.058 95.258  1.00 31.89 ?  586 TYR A C     1 
ATOM   4702  O  O     . TYR A 1 586 ? 121.372 135.777 94.113  1.00 35.40 ?  586 TYR A O     1 
ATOM   4703  C  CB    . TYR A 1 586 ? 121.955 134.432 97.146  1.00 32.22 ?  586 TYR A CB    1 
ATOM   4704  C  CG    . TYR A 1 586 ? 122.676 133.237 97.720  1.00 30.72 ?  586 TYR A CG    1 
ATOM   4705  C  CD1   . TYR A 1 586 ? 123.074 133.220 99.050  1.00 33.44 ?  586 TYR A CD1   1 
ATOM   4706  C  CD2   . TYR A 1 586 ? 122.950 132.123 96.941  1.00 34.07 ?  586 TYR A CD2   1 
ATOM   4707  C  CE1   . TYR A 1 586 ? 123.730 132.131 99.585  1.00 35.12 ?  586 TYR A CE1   1 
ATOM   4708  C  CE2   . TYR A 1 586 ? 123.606 131.028 97.468  1.00 34.78 ?  586 TYR A CE2   1 
ATOM   4709  C  CZ    . TYR A 1 586 ? 123.993 131.037 98.791  1.00 36.82 ?  586 TYR A CZ    1 
ATOM   4710  O  OH    . TYR A 1 586 ? 124.648 129.951 99.322  1.00 38.57 ?  586 TYR A OH    1 
ATOM   4711  N  N     . VAL A 1 587 ? 121.344 137.169 95.884  1.00 29.42 ?  587 VAL A N     1 
ATOM   4712  C  CA    . VAL A 1 587 ? 120.377 138.082 95.280  1.00 27.19 ?  587 VAL A CA    1 
ATOM   4713  C  C     . VAL A 1 587 ? 120.924 138.661 93.984  1.00 29.12 ?  587 VAL A C     1 
ATOM   4714  O  O     . VAL A 1 587 ? 120.185 138.857 93.011  1.00 34.89 ?  587 VAL A O     1 
ATOM   4715  C  CB    . VAL A 1 587 ? 119.997 139.189 96.280  1.00 31.21 ?  587 VAL A CB    1 
ATOM   4716  C  CG1   . VAL A 1 587 ? 118.947 140.107 95.686  1.00 31.59 ?  587 VAL A CG1   1 
ATOM   4717  C  CG2   . VAL A 1 587 ? 119.506 138.579 97.582  1.00 33.64 ?  587 VAL A CG2   1 
ATOM   4718  N  N     . GLN A 1 588 ? 122.223 138.940 93.947  1.00 31.49 ?  588 GLN A N     1 
ATOM   4719  C  CA    . GLN A 1 588 ? 122.859 139.477 92.753  1.00 26.60 ?  588 GLN A CA    1 
ATOM   4720  C  C     . GLN A 1 588 ? 123.215 138.401 91.740  1.00 28.18 ?  588 GLN A C     1 
ATOM   4721  O  O     . GLN A 1 588 ? 123.739 138.735 90.671  1.00 29.80 ?  588 GLN A O     1 
ATOM   4722  C  CB    . GLN A 1 588 ? 124.116 140.259 93.137  1.00 24.80 ?  588 GLN A CB    1 
ATOM   4723  C  CG    . GLN A 1 588 ? 123.834 141.547 93.884  1.00 23.53 ?  588 GLN A CG    1 
ATOM   4724  C  CD    . GLN A 1 588 ? 123.835 142.753 92.972  1.00 26.75 ?  588 GLN A CD    1 
ATOM   4725  O  OE1   . GLN A 1 588 ? 124.636 142.841 92.043  1.00 24.74 ?  588 GLN A OE1   1 
ATOM   4726  N  NE2   . GLN A 1 588 ? 122.936 143.694 93.233  1.00 32.10 ?  588 GLN A NE2   1 
ATOM   4727  N  N     . SER A 1 589 ? 122.934 137.135 92.044  1.00 29.68 ?  589 SER A N     1 
ATOM   4728  C  CA    . SER A 1 589 ? 123.318 136.002 91.207  1.00 26.27 ?  589 SER A CA    1 
ATOM   4729  C  C     . SER A 1 589 ? 124.806 136.078 90.868  1.00 28.13 ?  589 SER A C     1 
ATOM   4730  O  O     . SER A 1 589 ? 125.215 136.180 89.710  1.00 30.35 ?  589 SER A O     1 
ATOM   4731  C  CB    . SER A 1 589 ? 122.456 135.931 89.944  1.00 28.07 ?  589 SER A CB    1 
ATOM   4732  O  OG    . SER A 1 589 ? 122.895 136.856 88.966  1.00 34.21 ?  589 SER A OG    1 
ATOM   4733  N  N     . SER A 1 590 ? 125.616 136.036 91.921  1.00 27.77 ?  590 SER A N     1 
ATOM   4734  C  CA    . SER A 1 590 ? 127.050 136.231 91.808  1.00 22.98 ?  590 SER A CA    1 
ATOM   4735  C  C     . SER A 1 590 ? 127.766 135.270 92.742  1.00 24.82 ?  590 SER A C     1 
ATOM   4736  O  O     . SER A 1 590 ? 127.204 134.798 93.733  1.00 29.39 ?  590 SER A O     1 
ATOM   4737  C  CB    . SER A 1 590 ? 127.441 137.677 92.139  1.00 22.09 ?  590 SER A CB    1 
ATOM   4738  O  OG    . SER A 1 590 ? 127.783 137.811 93.505  1.00 29.32 ?  590 SER A OG    1 
ATOM   4739  N  N     . THR A 1 591 ? 129.018 134.973 92.408  1.00 23.96 ?  591 THR A N     1 
ATOM   4740  C  CA    . THR A 1 591 ? 129.871 134.219 93.308  1.00 24.18 ?  591 THR A CA    1 
ATOM   4741  C  C     . THR A 1 591 ? 130.340 135.116 94.448  1.00 23.05 ?  591 THR A C     1 
ATOM   4742  O  O     . THR A 1 591 ? 130.506 136.328 94.284  1.00 17.67 ?  591 THR A O     1 
ATOM   4743  C  CB    . THR A 1 591 ? 131.071 133.635 92.560  1.00 26.23 ?  591 THR A CB    1 
ATOM   4744  O  OG1   . THR A 1 591 ? 131.983 134.683 92.216  1.00 30.00 ?  591 THR A OG1   1 
ATOM   4745  C  CG2   . THR A 1 591 ? 130.609 132.940 91.291  1.00 25.88 ?  591 THR A CG2   1 
ATOM   4746  N  N     . ALA A 1 592 ? 130.546 134.509 95.613  1.00 22.30 ?  592 ALA A N     1 
ATOM   4747  C  CA    . ALA A 1 592 ? 130.811 135.284 96.817  1.00 22.38 ?  592 ALA A CA    1 
ATOM   4748  C  C     . ALA A 1 592 ? 132.208 135.887 96.781  1.00 22.73 ?  592 ALA A C     1 
ATOM   4749  O  O     . ALA A 1 592 ? 133.202 135.170 96.625  1.00 27.19 ?  592 ALA A O     1 
ATOM   4750  C  CB    . ALA A 1 592 ? 130.649 134.405 98.056  1.00 24.34 ?  592 ALA A CB    1 
ATOM   4751  N  N     . SER A 1 593 ? 132.275 137.204 96.927  1.00 24.21 ?  593 SER A N     1 
ATOM   4752  C  CA    . SER A 1 593 ? 133.523 137.960 97.058  1.00 16.30 ?  593 SER A CA    1 
ATOM   4753  C  C     . SER A 1 593 ? 134.418 137.681 95.849  1.00 15.94 ?  593 SER A C     1 
ATOM   4754  O  O     . SER A 1 593 ? 133.936 137.352 94.761  1.00 23.75 ?  593 SER A O     1 
ATOM   4755  C  CB    . SER A 1 593 ? 134.153 137.634 98.402  1.00 25.18 ?  593 SER A CB    1 
ATOM   4756  O  OG    . SER A 1 593 ? 135.197 138.536 98.712  1.00 24.78 ?  593 SER A OG    1 
ATOM   4757  N  N     . VAL A 1 594 ? 135.731 137.820 96.028  1.00 21.63 ?  594 VAL A N     1 
ATOM   4758  C  CA    . VAL A 1 594 ? 136.701 137.424 95.017  1.00 19.48 ?  594 VAL A CA    1 
ATOM   4759  C  C     . VAL A 1 594 ? 137.178 135.993 95.233  1.00 18.95 ?  594 VAL A C     1 
ATOM   4760  O  O     . VAL A 1 594 ? 138.115 135.545 94.567  1.00 18.36 ?  594 VAL A O     1 
ATOM   4761  C  CB    . VAL A 1 594 ? 137.890 138.396 94.980  1.00 21.54 ?  594 VAL A CB    1 
ATOM   4762  C  CG1   . VAL A 1 594 ? 137.435 139.768 94.506  1.00 9.11  ?  594 VAL A CG1   1 
ATOM   4763  C  CG2   . VAL A 1 594 ? 138.543 138.486 96.347  1.00 17.90 ?  594 VAL A CG2   1 
ATOM   4764  N  N     . MET A 1 595 ? 136.553 135.268 96.156  1.00 25.45 ?  595 MET A N     1 
ATOM   4765  C  CA    . MET A 1 595 ? 136.918 133.888 96.411  1.00 18.76 ?  595 MET A CA    1 
ATOM   4766  C  C     . MET A 1 595 ? 136.479 133.000 95.249  1.00 24.58 ?  595 MET A C     1 
ATOM   4767  O  O     . MET A 1 595 ? 135.496 133.295 94.565  1.00 32.18 ?  595 MET A O     1 
ATOM   4768  C  CB    . MET A 1 595 ? 136.265 133.394 97.700  1.00 22.37 ?  595 MET A CB    1 
ATOM   4769  C  CG    . MET A 1 595 ? 136.939 133.739 99.045  1.00 25.47 ?  595 MET A CG    1 
ATOM   4770  S  SD    . MET A 1 595 ? 138.738 133.646 99.255  1.00 31.61 ?  595 MET A SD    1 
ATOM   4771  C  CE    . MET A 1 595 ? 139.332 135.103 98.403  1.00 18.71 ?  595 MET A CE    1 
ATOM   4772  N  N     . PRO A 1 596 ? 137.197 131.909 95.000  1.00 27.55 ?  596 PRO A N     1 
ATOM   4773  C  CA    . PRO A 1 596 ? 136.689 130.889 94.080  1.00 22.18 ?  596 PRO A CA    1 
ATOM   4774  C  C     . PRO A 1 596 ? 135.509 130.148 94.692  1.00 27.22 ?  596 PRO A C     1 
ATOM   4775  O  O     . PRO A 1 596 ? 135.341 130.085 95.912  1.00 31.05 ?  596 PRO A O     1 
ATOM   4776  C  CB    . PRO A 1 596 ? 137.889 129.960 93.875  1.00 23.92 ?  596 PRO A CB    1 
ATOM   4777  C  CG    . PRO A 1 596 ? 138.733 130.160 95.087  1.00 28.34 ?  596 PRO A CG    1 
ATOM   4778  C  CD    . PRO A 1 596 ? 138.544 131.587 95.502  1.00 28.46 ?  596 PRO A CD    1 
ATOM   4779  N  N     . ILE A 1 597 ? 134.678 129.583 93.815  1.00 29.21 ?  597 ILE A N     1 
ATOM   4780  C  CA    . ILE A 1 597 ? 133.470 128.907 94.269  1.00 31.33 ?  597 ILE A CA    1 
ATOM   4781  C  C     . ILE A 1 597 ? 133.836 127.636 95.028  1.00 34.65 ?  597 ILE A C     1 
ATOM   4782  O  O     . ILE A 1 597 ? 134.783 126.919 94.679  1.00 36.12 ?  597 ILE A O     1 
ATOM   4783  C  CB    . ILE A 1 597 ? 132.538 128.599 93.083  1.00 32.00 ?  597 ILE A CB    1 
ATOM   4784  C  CG1   . ILE A 1 597 ? 133.189 127.599 92.124  1.00 31.16 ?  597 ILE A CG1   1 
ATOM   4785  C  CG2   . ILE A 1 597 ? 132.180 129.875 92.349  1.00 31.63 ?  597 ILE A CG2   1 
ATOM   4786  C  CD1   . ILE A 1 597 ? 132.201 126.810 91.302  1.00 31.93 ?  597 ILE A CD1   1 
ATOM   4787  N  N     . MET A 1 598 ? 133.080 127.360 96.091  1.00 39.86 ?  598 MET A N     1 
ATOM   4788  C  CA    . MET A 1 598 ? 133.302 126.143 96.861  1.00 38.55 ?  598 MET A CA    1 
ATOM   4789  C  C     . MET A 1 598 ? 132.705 124.928 96.165  1.00 38.59 ?  598 MET A C     1 
ATOM   4790  O  O     . MET A 1 598 ? 133.336 123.868 96.106  1.00 44.29 ?  598 MET A O     1 
ATOM   4791  C  CB    . MET A 1 598 ? 132.715 126.296 98.263  1.00 37.06 ?  598 MET A CB    1 
ATOM   4792  C  CG    . MET A 1 598 ? 133.641 126.980 99.250  1.00 35.00 ?  598 MET A CG    1 
ATOM   4793  S  SD    . MET A 1 598 ? 132.828 127.368 100.810 1.00 53.18 ?  598 MET A SD    1 
ATOM   4794  C  CE    . MET A 1 598 ? 131.640 128.593 100.273 1.00 39.51 ?  598 MET A CE    1 
ATOM   4795  N  N     . GLU A 1 599 ? 131.489 125.065 95.641  1.00 38.15 ?  599 GLU A N     1 
ATOM   4796  C  CA    . GLU A 1 599 ? 130.809 124.002 94.919  1.00 37.01 ?  599 GLU A CA    1 
ATOM   4797  C  C     . GLU A 1 599 ? 130.217 124.569 93.639  1.00 36.30 ?  599 GLU A C     1 
ATOM   4798  O  O     . GLU A 1 599 ? 129.837 125.740 93.581  1.00 40.49 ?  599 GLU A O     1 
ATOM   4799  C  CB    . GLU A 1 599 ? 129.695 123.364 95.765  1.00 38.85 ?  599 GLU A CB    1 
ATOM   4800  C  CG    . GLU A 1 599 ? 130.062 123.130 97.221  1.00 39.53 ?  599 GLU A CG    1 
ATOM   4801  C  CD    . GLU A 1 599 ? 128.854 123.141 98.137  1.00 43.17 ?  599 GLU A CD    1 
ATOM   4802  O  OE1   . GLU A 1 599 ? 128.374 124.242 98.478  1.00 40.97 ?  599 GLU A OE1   1 
ATOM   4803  O  OE2   . GLU A 1 599 ? 128.385 122.048 98.517  1.00 45.94 -1 599 GLU A OE2   1 
ATOM   4804  N  N     . ARG A 1 600 ? 130.148 123.731 92.603  1.00 38.66 ?  600 ARG A N     1 
ATOM   4805  C  CA    . ARG A 1 600 ? 129.501 124.158 91.367  1.00 35.38 ?  600 ARG A CA    1 
ATOM   4806  C  C     . ARG A 1 600 ? 127.996 124.289 91.562  1.00 34.16 ?  600 ARG A C     1 
ATOM   4807  O  O     . ARG A 1 600 ? 127.389 125.285 91.155  1.00 37.87 ?  600 ARG A O     1 
ATOM   4808  C  CB    . ARG A 1 600 ? 129.817 123.176 90.242  1.00 34.71 ?  600 ARG A CB    1 
ATOM   4809  C  CG    . ARG A 1 600 ? 131.183 123.377 89.630  1.00 35.12 ?  600 ARG A CG    1 
ATOM   4810  C  CD    . ARG A 1 600 ? 131.381 122.475 88.435  1.00 34.48 ?  600 ARG A CD    1 
ATOM   4811  N  NE    . ARG A 1 600 ? 132.700 122.637 87.835  1.00 34.15 ?  600 ARG A NE    1 
ATOM   4812  C  CZ    . ARG A 1 600 ? 133.790 122.009 88.250  1.00 37.48 ?  600 ARG A CZ    1 
ATOM   4813  N  NH1   . ARG A 1 600 ? 133.759 121.175 89.276  1.00 36.61 1  600 ARG A NH1   1 
ATOM   4814  N  NH2   . ARG A 1 600 ? 134.941 122.224 87.620  1.00 37.83 ?  600 ARG A NH2   1 
ATOM   4815  N  N     . ILE A 1 601 ? 127.380 123.286 92.179  1.00 39.12 ?  601 ILE A N     1 
ATOM   4816  C  CA    . ILE A 1 601 ? 125.981 123.332 92.582  1.00 41.28 ?  601 ILE A CA    1 
ATOM   4817  C  C     . ILE A 1 601 ? 125.936 123.049 94.075  1.00 40.35 ?  601 ILE A C     1 
ATOM   4818  O  O     . ILE A 1 601 ? 126.452 122.021 94.533  1.00 41.59 ?  601 ILE A O     1 
ATOM   4819  C  CB    . ILE A 1 601 ? 125.123 122.321 91.806  1.00 40.71 ?  601 ILE A CB    1 
ATOM   4820  C  CG1   . ILE A 1 601 ? 125.315 122.500 90.299  1.00 41.03 ?  601 ILE A CG1   1 
ATOM   4821  C  CG2   . ILE A 1 601 ? 123.657 122.477 92.175  1.00 37.03 ?  601 ILE A CG2   1 
ATOM   4822  C  CD1   . ILE A 1 601 ? 124.713 121.389 89.474  1.00 39.55 ?  601 ILE A CD1   1 
ATOM   4823  N  N     . GLU A 1 602 ? 125.328 123.955 94.832  1.00 45.16 ?  602 GLU A N     1 
ATOM   4824  C  CA    . GLU A 1 602 ? 125.240 123.820 96.277  1.00 47.44 ?  602 GLU A CA    1 
ATOM   4825  C  C     . GLU A 1 602 ? 123.852 123.343 96.683  1.00 48.63 ?  602 GLU A C     1 
ATOM   4826  O  O     . GLU A 1 602 ? 122.837 123.830 96.177  1.00 48.67 ?  602 GLU A O     1 
ATOM   4827  C  CB    . GLU A 1 602 ? 125.574 125.140 96.977  1.00 45.19 ?  602 GLU A CB    1 
ATOM   4828  C  CG    . GLU A 1 602 ? 124.787 126.336 96.483  1.00 47.09 ?  602 GLU A CG    1 
ATOM   4829  C  CD    . GLU A 1 602 ? 125.001 127.564 97.344  1.00 50.58 ?  602 GLU A CD    1 
ATOM   4830  O  OE1   . GLU A 1 602 ? 126.065 128.204 97.214  1.00 50.27 ?  602 GLU A OE1   1 
ATOM   4831  O  OE2   . GLU A 1 602 ? 124.104 127.891 98.150  1.00 51.85 -1 602 GLU A OE2   1 
ATOM   4832  N  N     . GLU A 1 603 ? 123.823 122.374 97.592  1.00 56.87 ?  603 GLU A N     1 
ATOM   4833  C  CA    . GLU A 1 603 ? 122.592 121.804 98.117  1.00 57.73 ?  603 GLU A CA    1 
ATOM   4834  C  C     . GLU A 1 603 ? 122.302 122.405 99.485  1.00 57.59 ?  603 GLU A C     1 
ATOM   4835  O  O     . GLU A 1 603 ? 123.151 122.358 100.380 1.00 57.50 ?  603 GLU A O     1 
ATOM   4836  C  CB    . GLU A 1 603 ? 122.705 120.283 98.221  1.00 57.17 ?  603 GLU A CB    1 
ATOM   4837  C  CG    . GLU A 1 603 ? 121.464 119.595 98.754  1.00 58.95 ?  603 GLU A CG    1 
ATOM   4838  C  CD    . GLU A 1 603 ? 121.790 118.341 99.539  1.00 60.15 ?  603 GLU A CD    1 
ATOM   4839  O  OE1   . GLU A 1 603 ? 122.119 118.458 100.738 1.00 60.48 ?  603 GLU A OE1   1 
ATOM   4840  O  OE2   . GLU A 1 603 ? 121.718 117.240 98.957  1.00 59.56 -1 603 GLU A OE2   1 
ATOM   4841  N  N     . ARG A 1 604 ? 121.106 122.967 99.644  1.00 58.62 ?  604 ARG A N     1 
ATOM   4842  C  CA    . ARG A 1 604 ? 120.708 123.585 100.898 1.00 59.06 ?  604 ARG A CA    1 
ATOM   4843  C  C     . ARG A 1 604 ? 119.387 122.994 101.367 1.00 59.92 ?  604 ARG A C     1 
ATOM   4844  O  O     . ARG A 1 604 ? 118.598 122.484 100.569 1.00 59.33 ?  604 ARG A O     1 
ATOM   4845  C  CB    . ARG A 1 604 ? 120.585 125.108 100.764 1.00 58.99 ?  604 ARG A CB    1 
ATOM   4846  C  CG    . ARG A 1 604 ? 121.857 125.788 100.292 1.00 58.38 ?  604 ARG A CG    1 
ATOM   4847  C  CD    . ARG A 1 604 ? 122.711 126.234 101.466 1.00 58.50 ?  604 ARG A CD    1 
ATOM   4848  N  NE    . ARG A 1 604 ? 123.804 125.305 101.726 1.00 58.72 ?  604 ARG A NE    1 
ATOM   4849  C  CZ    . ARG A 1 604 ? 125.015 125.404 101.194 1.00 59.29 ?  604 ARG A CZ    1 
ATOM   4850  N  NH1   . ARG A 1 604 ? 125.326 126.384 100.362 1.00 57.85 1  604 ARG A NH1   1 
ATOM   4851  N  NH2   . ARG A 1 604 ? 125.936 124.495 101.503 1.00 57.26 ?  604 ARG A NH2   1 
ATOM   4852  N  N     . THR A 1 605 ? 119.163 123.053 102.677 1.00 65.73 ?  605 THR A N     1 
ATOM   4853  C  CA    . THR A 1 605 ? 117.943 122.547 103.295 1.00 66.61 ?  605 THR A CA    1 
ATOM   4854  C  C     . THR A 1 605 ? 117.240 123.706 103.988 1.00 66.54 ?  605 THR A C     1 
ATOM   4855  O  O     . THR A 1 605 ? 117.741 124.232 104.987 1.00 65.70 ?  605 THR A O     1 
ATOM   4856  C  CB    . THR A 1 605 ? 118.251 121.425 104.286 1.00 66.19 ?  605 THR A CB    1 
ATOM   4857  O  OG1   . THR A 1 605 ? 119.003 120.397 103.630 1.00 66.36 ?  605 THR A OG1   1 
ATOM   4858  C  CG2   . THR A 1 605 ? 116.962 120.832 104.834 1.00 66.87 ?  605 THR A CG2   1 
ATOM   4859  N  N     . TYR A 1 606 ? 116.086 124.103 103.460 1.00 66.48 ?  606 TYR A N     1 
ATOM   4860  C  CA    . TYR A 1 606 ? 115.259 125.135 104.068 1.00 68.28 ?  606 TYR A CA    1 
ATOM   4861  C  C     . TYR A 1 606 ? 113.959 124.505 104.545 1.00 70.28 ?  606 TYR A C     1 
ATOM   4862  O  O     . TYR A 1 606 ? 113.252 123.862 103.759 1.00 69.13 ?  606 TYR A O     1 
ATOM   4863  C  CB    . TYR A 1 606 ? 114.978 126.275 103.086 1.00 66.57 ?  606 TYR A CB    1 
ATOM   4864  C  CG    . TYR A 1 606 ? 116.213 127.048 102.685 1.00 68.29 ?  606 TYR A CG    1 
ATOM   4865  C  CD1   . TYR A 1 606 ? 116.916 127.805 103.614 1.00 66.92 ?  606 TYR A CD1   1 
ATOM   4866  C  CD2   . TYR A 1 606 ? 116.676 127.026 101.378 1.00 67.97 ?  606 TYR A CD2   1 
ATOM   4867  C  CE1   . TYR A 1 606 ? 118.046 128.514 103.251 1.00 66.54 ?  606 TYR A CE1   1 
ATOM   4868  C  CE2   . TYR A 1 606 ? 117.804 127.731 101.006 1.00 65.78 ?  606 TYR A CE2   1 
ATOM   4869  C  CZ    . TYR A 1 606 ? 118.485 128.473 101.945 1.00 67.46 ?  606 TYR A CZ    1 
ATOM   4870  O  OH    . TYR A 1 606 ? 119.608 129.176 101.574 1.00 66.96 ?  606 TYR A OH    1 
ATOM   4871  N  N     . GLY A 1 607 ? 113.647 124.696 105.823 1.00 75.36 ?  607 GLY A N     1 
ATOM   4872  C  CA    . GLY A 1 607 ? 112.525 123.979 106.406 1.00 74.97 ?  607 GLY A CA    1 
ATOM   4873  C  C     . GLY A 1 607 ? 112.767 122.488 106.310 1.00 75.53 ?  607 GLY A C     1 
ATOM   4874  O  O     . GLY A 1 607 ? 113.807 121.974 106.737 1.00 75.04 ?  607 GLY A O     1 
ATOM   4875  N  N     . ASN A 1 608 ? 111.798 121.775 105.738 1.00 78.59 ?  608 ASN A N     1 
ATOM   4876  C  CA    . ASN A 1 608 ? 111.937 120.355 105.451 1.00 80.29 ?  608 ASN A CA    1 
ATOM   4877  C  C     . ASN A 1 608 ? 112.111 120.091 103.959 1.00 79.21 ?  608 ASN A C     1 
ATOM   4878  O  O     . ASN A 1 608 ? 111.860 118.974 103.496 1.00 78.37 ?  608 ASN A O     1 
ATOM   4879  C  CB    . ASN A 1 608 ? 110.737 119.580 105.995 1.00 79.45 ?  608 ASN A CB    1 
ATOM   4880  C  CG    . ASN A 1 608 ? 110.791 119.407 107.501 1.00 79.47 ?  608 ASN A CG    1 
ATOM   4881  O  OD1   . ASN A 1 608 ? 111.818 119.665 108.130 1.00 79.06 ?  608 ASN A OD1   1 
ATOM   4882  N  ND2   . ASN A 1 608 ? 109.684 118.968 108.087 1.00 78.01 ?  608 ASN A ND2   1 
ATOM   4883  N  N     . SER A 1 609 ? 112.537 121.099 103.201 1.00 73.08 ?  609 SER A N     1 
ATOM   4884  C  CA    . SER A 1 609 ? 112.660 121.001 101.757 1.00 72.48 ?  609 SER A CA    1 
ATOM   4885  C  C     . SER A 1 609 ? 114.110 121.190 101.334 1.00 73.03 ?  609 SER A C     1 
ATOM   4886  O  O     . SER A 1 609 ? 114.885 121.891 101.994 1.00 72.83 ?  609 SER A O     1 
ATOM   4887  C  CB    . SER A 1 609 ? 111.777 122.038 101.057 1.00 71.53 ?  609 SER A CB    1 
ATOM   4888  O  OG    . SER A 1 609 ? 112.164 123.356 101.405 1.00 70.80 ?  609 SER A OG    1 
ATOM   4889  N  N     . LYS A 1 610 ? 114.471 120.546 100.228 1.00 65.08 ?  610 LYS A N     1 
ATOM   4890  C  CA    . LYS A 1 610 ? 115.810 120.633 99.666  1.00 62.96 ?  610 LYS A CA    1 
ATOM   4891  C  C     . LYS A 1 610 ? 115.795 121.550 98.450  1.00 63.45 ?  610 LYS A C     1 
ATOM   4892  O  O     . LYS A 1 610 ? 114.821 121.577 97.692  1.00 64.05 ?  610 LYS A O     1 
ATOM   4893  C  CB    . LYS A 1 610 ? 116.328 119.249 99.273  1.00 62.17 ?  610 LYS A CB    1 
ATOM   4894  C  CG    . LYS A 1 610 ? 117.841 119.148 99.196  1.00 63.41 ?  610 LYS A CG    1 
ATOM   4895  C  CD    . LYS A 1 610 ? 118.337 117.876 99.869  1.00 64.78 ?  610 LYS A CD    1 
ATOM   4896  C  CE    . LYS A 1 610 ? 118.446 118.046 101.377 1.00 64.27 ?  610 LYS A CE    1 
ATOM   4897  N  NZ    . LYS A 1 610 ? 119.660 118.808 101.776 1.00 62.54 1  610 LYS A NZ    1 
ATOM   4898  N  N     . THR A 1 611 ? 116.878 122.301 98.270  1.00 61.72 ?  611 THR A N     1 
ATOM   4899  C  CA    . THR A 1 611 ? 116.992 123.237 97.164  1.00 58.73 ?  611 THR A CA    1 
ATOM   4900  C  C     . THR A 1 611 ? 118.406 123.180 96.604  1.00 57.57 ?  611 THR A C     1 
ATOM   4901  O  O     . THR A 1 611 ? 119.363 122.824 97.297  1.00 56.69 ?  611 THR A O     1 
ATOM   4902  C  CB    . THR A 1 611 ? 116.644 124.667 97.593  1.00 58.99 ?  611 THR A CB    1 
ATOM   4903  O  OG1   . THR A 1 611 ? 116.697 125.534 96.454  1.00 61.87 ?  611 THR A OG1   1 
ATOM   4904  C  CG2   . THR A 1 611 ? 117.620 125.153 98.642  1.00 59.35 ?  611 THR A CG2   1 
ATOM   4905  N  N     . TYR A 1 612 ? 118.521 123.549 95.331  1.00 53.41 ?  612 TYR A N     1 
ATOM   4906  C  CA    . TYR A 1 612 ? 119.750 123.385 94.565  1.00 51.64 ?  612 TYR A CA    1 
ATOM   4907  C  C     . TYR A 1 612 ? 120.080 124.705 93.891  1.00 54.03 ?  612 TYR A C     1 
ATOM   4908  O  O     . TYR A 1 612 ? 119.273 125.223 93.112  1.00 56.09 ?  612 TYR A O     1 
ATOM   4909  C  CB    . TYR A 1 612 ? 119.579 122.274 93.527  1.00 53.90 ?  612 TYR A CB    1 
ATOM   4910  C  CG    . TYR A 1 612 ? 119.517 120.891 94.132  1.00 55.12 ?  612 TYR A CG    1 
ATOM   4911  C  CD1   . TYR A 1 612 ? 120.505 120.442 94.994  1.00 54.59 ?  612 TYR A CD1   1 
ATOM   4912  C  CD2   . TYR A 1 612 ? 118.437 120.056 93.884  1.00 54.58 ?  612 TYR A CD2   1 
ATOM   4913  C  CE1   . TYR A 1 612 ? 120.441 119.183 95.555  1.00 55.95 ?  612 TYR A CE1   1 
ATOM   4914  C  CE2   . TYR A 1 612 ? 118.359 118.798 94.448  1.00 55.96 ?  612 TYR A CE2   1 
ATOM   4915  C  CZ    . TYR A 1 612 ? 119.366 118.366 95.283  1.00 57.43 ?  612 TYR A CZ    1 
ATOM   4916  O  OH    . TYR A 1 612 ? 119.299 117.114 95.849  1.00 58.99 ?  612 TYR A OH    1 
ATOM   4917  N  N     . TYR A 1 613 ? 121.256 125.252 94.188  1.00 46.07 ?  613 TYR A N     1 
ATOM   4918  C  CA    . TYR A 1 613 ? 121.715 126.495 93.568  1.00 40.41 ?  613 TYR A CA    1 
ATOM   4919  C  C     . TYR A 1 613 ? 122.964 126.239 92.742  1.00 39.86 ?  613 TYR A C     1 
ATOM   4920  O  O     . TYR A 1 613 ? 124.055 126.048 93.305  1.00 39.39 ?  613 TYR A O     1 
ATOM   4921  C  CB    . TYR A 1 613 ? 121.987 127.568 94.620  1.00 40.96 ?  613 TYR A CB    1 
ATOM   4922  C  CG    . TYR A 1 613 ? 122.459 128.879 94.032  1.00 37.21 ?  613 TYR A CG    1 
ATOM   4923  C  CD1   . TYR A 1 613 ? 121.718 129.530 93.055  1.00 37.85 ?  613 TYR A CD1   1 
ATOM   4924  C  CD2   . TYR A 1 613 ? 123.648 129.463 94.448  1.00 37.53 ?  613 TYR A CD2   1 
ATOM   4925  C  CE1   . TYR A 1 613 ? 122.142 130.728 92.515  1.00 41.31 ?  613 TYR A CE1   1 
ATOM   4926  C  CE2   . TYR A 1 613 ? 124.080 130.661 93.913  1.00 39.98 ?  613 TYR A CE2   1 
ATOM   4927  C  CZ    . TYR A 1 613 ? 123.325 131.288 92.946  1.00 44.91 ?  613 TYR A CZ    1 
ATOM   4928  O  OH    . TYR A 1 613 ? 123.751 132.480 92.409  1.00 41.53 ?  613 TYR A OH    1 
ATOM   4929  N  N     . PRO A 1 614 ? 122.857 126.185 91.418  1.00 41.29 ?  614 PRO A N     1 
ATOM   4930  C  CA    . PRO A 1 614 ? 124.065 126.192 90.590  1.00 38.89 ?  614 PRO A CA    1 
ATOM   4931  C  C     . PRO A 1 614 ? 124.725 127.558 90.628  1.00 39.14 ?  614 PRO A C     1 
ATOM   4932  O  O     . PRO A 1 614 ? 124.074 128.583 90.842  1.00 37.77 ?  614 PRO A O     1 
ATOM   4933  C  CB    . PRO A 1 614 ? 123.544 125.861 89.185  1.00 35.09 ?  614 PRO A CB    1 
ATOM   4934  C  CG    . PRO A 1 614 ? 122.134 125.381 89.379  1.00 39.46 ?  614 PRO A CG    1 
ATOM   4935  C  CD    . PRO A 1 614 ? 121.635 126.054 90.612  1.00 39.99 ?  614 PRO A CD    1 
ATOM   4936  N  N     . MET A 1 615 ? 126.038 127.566 90.424  1.00 37.84 ?  615 MET A N     1 
ATOM   4937  C  CA    . MET A 1 615 ? 126.752 128.828 90.354  1.00 35.62 ?  615 MET A CA    1 
ATOM   4938  C  C     . MET A 1 615 ? 126.283 129.627 89.140  1.00 38.19 ?  615 MET A C     1 
ATOM   4939  O  O     . MET A 1 615 ? 125.901 129.051 88.118  1.00 40.78 ?  615 MET A O     1 
ATOM   4940  C  CB    . MET A 1 615 ? 128.259 128.589 90.303  1.00 36.41 ?  615 MET A CB    1 
ATOM   4941  C  CG    . MET A 1 615 ? 128.863 128.371 91.681  1.00 37.79 ?  615 MET A CG    1 
ATOM   4942  S  SD    . MET A 1 615 ? 127.911 129.242 92.943  1.00 44.79 ?  615 MET A SD    1 
ATOM   4943  C  CE    . MET A 1 615 ? 128.399 128.376 94.428  1.00 37.65 ?  615 MET A CE    1 
ATOM   4944  N  N     . PRO A 1 616 ? 126.268 130.955 89.239  1.00 38.31 ?  616 PRO A N     1 
ATOM   4945  C  CA    . PRO A 1 616 ? 125.673 131.772 88.173  1.00 35.48 ?  616 PRO A CA    1 
ATOM   4946  C  C     . PRO A 1 616 ? 126.375 131.561 86.840  1.00 36.21 ?  616 PRO A C     1 
ATOM   4947  O  O     . PRO A 1 616 ? 127.603 131.578 86.754  1.00 38.12 ?  616 PRO A O     1 
ATOM   4948  C  CB    . PRO A 1 616 ? 125.854 133.205 88.685  1.00 36.48 ?  616 PRO A CB    1 
ATOM   4949  C  CG    . PRO A 1 616 ? 126.035 133.060 90.162  1.00 35.50 ?  616 PRO A CG    1 
ATOM   4950  C  CD    . PRO A 1 616 ? 126.756 131.776 90.359  1.00 35.95 ?  616 PRO A CD    1 
ATOM   4951  N  N     . GLY A 1 617 ? 125.577 131.368 85.793  1.00 37.13 ?  617 GLY A N     1 
ATOM   4952  C  CA    . GLY A 1 617 ? 126.119 131.133 84.471  1.00 36.09 ?  617 GLY A CA    1 
ATOM   4953  C  C     . GLY A 1 617 ? 126.716 129.763 84.257  1.00 40.13 ?  617 GLY A C     1 
ATOM   4954  O  O     . GLY A 1 617 ? 127.376 129.546 83.236  1.00 42.08 ?  617 GLY A O     1 
ATOM   4955  N  N     . LEU A 1 618 ? 126.510 128.830 85.184  1.00 41.11 ?  618 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 618 ? 127.072 127.495 85.038  1.00 37.11 ?  618 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 618 ? 126.346 126.731 83.938  1.00 39.55 ?  618 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 618 ? 125.113 126.702 83.893  1.00 44.58 ?  618 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 618 ? 126.986 126.730 86.357  1.00 37.34 ?  618 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 618 ? 127.569 125.317 86.365  1.00 38.46 ?  618 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 618 ? 129.037 125.338 85.979  1.00 38.88 ?  618 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 618 ? 127.382 124.668 87.726  1.00 39.00 ?  618 LEU A CD2   1 
ATOM   4963  N  N     . ALA A 1 619 ? 127.119 126.113 83.051  1.00 45.15 ?  619 ALA A N     1 
ATOM   4964  C  CA    . ALA A 1 619 ? 126.577 125.312 81.966  1.00 45.77 ?  619 ALA A CA    1 
ATOM   4965  C  C     . ALA A 1 619 ? 127.584 124.221 81.634  1.00 49.12 ?  619 ALA A C     1 
ATOM   4966  O  O     . ALA A 1 619 ? 128.588 124.044 82.328  1.00 51.63 ?  619 ALA A O     1 
ATOM   4967  C  CB    . ALA A 1 619 ? 126.257 126.178 80.744  1.00 44.64 ?  619 ALA A CB    1 
ATOM   4968  N  N     . SER A 1 620 ? 127.307 123.480 80.560  1.00 50.10 ?  620 SER A N     1 
ATOM   4969  C  CA    . SER A 1 620 ? 128.229 122.433 80.138  1.00 49.28 ?  620 SER A CA    1 
ATOM   4970  C  C     . SER A 1 620 ? 129.516 123.023 79.574  1.00 49.15 ?  620 SER A C     1 
ATOM   4971  O  O     . SER A 1 620 ? 130.597 122.449 79.750  1.00 51.61 ?  620 SER A O     1 
ATOM   4972  C  CB    . SER A 1 620 ? 127.554 121.527 79.108  1.00 52.72 ?  620 SER A CB    1 
ATOM   4973  O  OG    . SER A 1 620 ? 126.324 121.027 79.600  1.00 54.05 ?  620 SER A OG    1 
ATOM   4974  N  N     . ASN A 1 621 ? 129.421 124.168 78.895  1.00 47.90 ?  621 ASN A N     1 
ATOM   4975  C  CA    . ASN A 1 621 ? 130.602 124.759 78.274  1.00 50.30 ?  621 ASN A CA    1 
ATOM   4976  C  C     . ASN A 1 621 ? 131.568 125.311 79.315  1.00 50.21 ?  621 ASN A C     1 
ATOM   4977  O  O     . ASN A 1 621 ? 132.789 125.193 79.159  1.00 50.40 ?  621 ASN A O     1 
ATOM   4978  C  CB    . ASN A 1 621 ? 130.184 125.854 77.293  1.00 49.26 ?  621 ASN A CB    1 
ATOM   4979  C  CG    . ASN A 1 621 ? 128.938 126.590 77.739  1.00 51.92 ?  621 ASN A CG    1 
ATOM   4980  O  OD1   . ASN A 1 621 ? 128.904 127.177 78.820  1.00 50.98 ?  621 ASN A OD1   1 
ATOM   4981  N  ND2   . ASN A 1 621 ? 127.905 126.561 76.906  1.00 51.57 ?  621 ASN A ND2   1 
ATOM   4982  N  N     . ASN A 1 622 ? 131.046 125.917 80.382  1.00 40.26 ?  622 ASN A N     1 
ATOM   4983  C  CA    . ASN A 1 622 ? 131.877 126.517 81.418  1.00 39.73 ?  622 ASN A CA    1 
ATOM   4984  C  C     . ASN A 1 622 ? 131.898 125.691 82.701  1.00 43.21 ?  622 ASN A C     1 
ATOM   4985  O  O     . ASN A 1 622 ? 132.249 126.214 83.763  1.00 47.91 ?  622 ASN A O     1 
ATOM   4986  C  CB    . ASN A 1 622 ? 131.420 127.949 81.707  1.00 40.12 ?  622 ASN A CB    1 
ATOM   4987  C  CG    . ASN A 1 622 ? 129.947 128.037 82.063  1.00 41.94 ?  622 ASN A CG    1 
ATOM   4988  O  OD1   . ASN A 1 622 ? 129.306 127.035 82.375  1.00 47.40 ?  622 ASN A OD1   1 
ATOM   4989  N  ND2   . ASN A 1 622 ? 129.403 129.246 82.015  1.00 38.35 ?  622 ASN A ND2   1 
ATOM   4990  N  N     . TRP A 1 623 ? 131.522 124.413 82.624  1.00 40.70 ?  623 TRP A N     1 
ATOM   4991  C  CA    . TRP A 1 623 ? 131.588 123.552 83.799  1.00 40.55 ?  623 TRP A CA    1 
ATOM   4992  C  C     . TRP A 1 623 ? 133.026 123.374 84.268  1.00 41.55 ?  623 TRP A C     1 
ATOM   4993  O  O     . TRP A 1 623 ? 133.300 123.367 85.474  1.00 40.00 ?  623 TRP A O     1 
ATOM   4994  C  CB    . TRP A 1 623 ? 130.947 122.197 83.492  1.00 41.25 ?  623 TRP A CB    1 
ATOM   4995  C  CG    . TRP A 1 623 ? 131.064 121.193 84.602  1.00 40.04 ?  623 TRP A CG    1 
ATOM   4996  C  CD1   . TRP A 1 623 ? 132.115 120.358 84.847  1.00 37.86 ?  623 TRP A CD1   1 
ATOM   4997  C  CD2   . TRP A 1 623 ? 130.088 120.916 85.613  1.00 39.38 ?  623 TRP A CD2   1 
ATOM   4998  N  NE1   . TRP A 1 623 ? 131.855 119.581 85.949  1.00 37.74 ?  623 TRP A NE1   1 
ATOM   4999  C  CE2   . TRP A 1 623 ? 130.616 119.903 86.436  1.00 37.65 ?  623 TRP A CE2   1 
ATOM   5000  C  CE3   . TRP A 1 623 ? 128.819 121.427 85.901  1.00 38.03 ?  623 TRP A CE3   1 
ATOM   5001  C  CZ2   . TRP A 1 623 ? 129.922 119.393 87.531  1.00 38.90 ?  623 TRP A CZ2   1 
ATOM   5002  C  CZ3   . TRP A 1 623 ? 128.132 120.919 86.988  1.00 39.91 ?  623 TRP A CZ3   1 
ATOM   5003  C  CH2   . TRP A 1 623 ? 128.683 119.914 87.789  1.00 39.28 ?  623 TRP A CH2   1 
ATOM   5004  N  N     . PHE A 1 624 ? 133.961 123.227 83.327  1.00 43.25 ?  624 PHE A N     1 
ATOM   5005  C  CA    . PHE A 1 624 ? 135.362 123.055 83.688  1.00 43.02 ?  624 PHE A CA    1 
ATOM   5006  C  C     . PHE A 1 624 ? 135.973 124.340 84.230  1.00 41.73 ?  624 PHE A C     1 
ATOM   5007  O  O     . PHE A 1 624 ? 136.811 124.287 85.136  1.00 45.72 ?  624 PHE A O     1 
ATOM   5008  C  CB    . PHE A 1 624 ? 136.146 122.530 82.478  1.00 41.79 ?  624 PHE A CB    1 
ATOM   5009  C  CG    . PHE A 1 624 ? 137.583 122.985 82.421  1.00 45.02 ?  624 PHE A CG    1 
ATOM   5010  C  CD1   . PHE A 1 624 ? 137.930 124.187 81.819  1.00 42.97 ?  624 PHE A CD1   1 
ATOM   5011  C  CD2   . PHE A 1 624 ? 138.586 122.206 82.972  1.00 44.13 ?  624 PHE A CD2   1 
ATOM   5012  C  CE1   . PHE A 1 624 ? 139.247 124.598 81.769  1.00 43.88 ?  624 PHE A CE1   1 
ATOM   5013  C  CE2   . PHE A 1 624 ? 139.906 122.614 82.925  1.00 43.74 ?  624 PHE A CE2   1 
ATOM   5014  C  CZ    . PHE A 1 624 ? 140.235 123.811 82.323  1.00 44.28 ?  624 PHE A CZ    1 
ATOM   5015  N  N     . PHE A 1 625 ? 135.572 125.497 83.695  1.00 35.51 ?  625 PHE A N     1 
ATOM   5016  C  CA    . PHE A 1 625 ? 136.101 126.762 84.188  1.00 34.02 ?  625 PHE A CA    1 
ATOM   5017  C  C     . PHE A 1 625 ? 135.555 127.122 85.563  1.00 33.14 ?  625 PHE A C     1 
ATOM   5018  O  O     . PHE A 1 625 ? 136.174 127.922 86.270  1.00 35.40 ?  625 PHE A O     1 
ATOM   5019  C  CB    . PHE A 1 625 ? 135.799 127.886 83.196  1.00 32.94 ?  625 PHE A CB    1 
ATOM   5020  C  CG    . PHE A 1 625 ? 136.605 127.807 81.933  1.00 34.92 ?  625 PHE A CG    1 
ATOM   5021  C  CD1   . PHE A 1 625 ? 137.952 128.128 81.935  1.00 33.87 ?  625 PHE A CD1   1 
ATOM   5022  C  CD2   . PHE A 1 625 ? 136.018 127.412 80.744  1.00 34.90 ?  625 PHE A CD2   1 
ATOM   5023  C  CE1   . PHE A 1 625 ? 138.698 128.056 80.774  1.00 35.98 ?  625 PHE A CE1   1 
ATOM   5024  C  CE2   . PHE A 1 625 ? 136.757 127.339 79.580  1.00 36.21 ?  625 PHE A CE2   1 
ATOM   5025  C  CZ    . PHE A 1 625 ? 138.099 127.661 79.595  1.00 38.49 ?  625 PHE A CZ    1 
ATOM   5026  N  N     . TYR A 1 626 ? 134.418 126.549 85.958  1.00 29.63 ?  626 TYR A N     1 
ATOM   5027  C  CA    . TYR A 1 626 ? 133.898 126.763 87.302  1.00 32.34 ?  626 TYR A CA    1 
ATOM   5028  C  C     . TYR A 1 626 ? 134.523 125.771 88.271  1.00 31.25 ?  626 TYR A C     1 
ATOM   5029  O  O     . TYR A 1 626 ? 133.814 125.062 88.990  1.00 34.79 ?  626 TYR A O     1 
ATOM   5030  C  CB    . TYR A 1 626 ? 132.374 126.640 87.323  1.00 32.25 ?  626 TYR A CB    1 
ATOM   5031  C  CG    . TYR A 1 626 ? 131.665 127.968 87.217  1.00 31.54 ?  626 TYR A CG    1 
ATOM   5032  C  CD1   . TYR A 1 626 ? 131.686 128.871 88.270  1.00 34.40 ?  626 TYR A CD1   1 
ATOM   5033  C  CD2   . TYR A 1 626 ? 130.973 128.318 86.066  1.00 30.33 ?  626 TYR A CD2   1 
ATOM   5034  C  CE1   . TYR A 1 626 ? 131.043 130.086 88.180  1.00 34.43 ?  626 TYR A CE1   1 
ATOM   5035  C  CE2   . TYR A 1 626 ? 130.325 129.531 85.967  1.00 32.29 ?  626 TYR A CE2   1 
ATOM   5036  C  CZ    . TYR A 1 626 ? 130.364 130.411 87.027  1.00 33.86 ?  626 TYR A CZ    1 
ATOM   5037  O  OH    . TYR A 1 626 ? 129.723 131.622 86.936  1.00 36.02 ?  626 TYR A OH    1 
ATOM   5038  N  N     . LYS A 1 627 ? 135.852 125.721 88.295  1.00 31.15 ?  627 LYS A N     1 
ATOM   5039  C  CA    . LYS A 1 627 ? 136.558 124.795 89.169  1.00 30.24 ?  627 LYS A CA    1 
ATOM   5040  C  C     . LYS A 1 627 ? 136.256 125.104 90.629  1.00 34.65 ?  627 LYS A C     1 
ATOM   5041  O  O     . LYS A 1 627 ? 136.177 126.267 91.031  1.00 40.73 ?  627 LYS A O     1 
ATOM   5042  C  CB    . LYS A 1 627 ? 138.060 124.878 88.906  1.00 35.22 ?  627 LYS A CB    1 
ATOM   5043  C  CG    . LYS A 1 627 ? 138.891 123.830 89.617  1.00 34.08 ?  627 LYS A CG    1 
ATOM   5044  C  CD    . LYS A 1 627 ? 140.323 123.858 89.115  1.00 31.12 ?  627 LYS A CD    1 
ATOM   5045  C  CE    . LYS A 1 627 ? 141.213 122.933 89.921  1.00 36.23 ?  627 LYS A CE    1 
ATOM   5046  N  NZ    . LYS A 1 627 ? 142.647 123.109 89.569  1.00 36.73 1  627 LYS A NZ    1 
ATOM   5047  N  N     . GLU A 1 628 ? 136.069 124.053 91.421  1.00 38.83 ?  628 GLU A N     1 
ATOM   5048  C  CA    . GLU A 1 628 ? 135.797 124.241 92.837  1.00 36.13 ?  628 GLU A CA    1 
ATOM   5049  C  C     . GLU A 1 628 ? 137.052 124.707 93.565  1.00 38.43 ?  628 GLU A C     1 
ATOM   5050  O  O     . GLU A 1 628 ? 138.180 124.396 93.172  1.00 40.81 ?  628 GLU A O     1 
ATOM   5051  C  CB    . GLU A 1 628 ? 135.268 122.948 93.456  1.00 37.33 ?  628 GLU A CB    1 
ATOM   5052  C  CG    . GLU A 1 628 ? 133.824 122.647 93.088  1.00 39.57 ?  628 GLU A CG    1 
ATOM   5053  C  CD    . GLU A 1 628 ? 133.378 121.275 93.545  1.00 43.19 ?  628 GLU A CD    1 
ATOM   5054  O  OE1   . GLU A 1 628 ? 134.115 120.637 94.326  1.00 45.12 ?  628 GLU A OE1   1 
ATOM   5055  O  OE2   . GLU A 1 628 ? 132.289 120.834 93.124  1.00 39.83 -1 628 GLU A OE2   1 
ATOM   5056  N  N     . ALA A 1 629 ? 136.842 125.471 94.640  1.00 39.43 ?  629 ALA A N     1 
ATOM   5057  C  CA    . ALA A 1 629 ? 137.960 126.075 95.359  1.00 33.25 ?  629 ALA A CA    1 
ATOM   5058  C  C     . ALA A 1 629 ? 138.862 125.019 95.983  1.00 35.69 ?  629 ALA A C     1 
ATOM   5059  O  O     . ALA A 1 629 ? 140.088 125.181 96.015  1.00 42.03 ?  629 ALA A O     1 
ATOM   5060  C  CB    . ALA A 1 629 ? 137.436 127.031 96.428  1.00 30.29 ?  629 ALA A CB    1 
ATOM   5061  N  N     . TYR A 1 630 ? 138.275 123.935 96.495  1.00 40.56 ?  630 TYR A N     1 
ATOM   5062  C  CA    . TYR A 1 630 ? 139.075 122.905 97.149  1.00 36.66 ?  630 TYR A CA    1 
ATOM   5063  C  C     . TYR A 1 630 ? 139.991 122.189 96.166  1.00 41.15 ?  630 TYR A C     1 
ATOM   5064  O  O     . TYR A 1 630 ? 141.106 121.801 96.533  1.00 44.81 ?  630 TYR A O     1 
ATOM   5065  C  CB    . TYR A 1 630 ? 138.161 121.905 97.854  1.00 35.20 ?  630 TYR A CB    1 
ATOM   5066  C  CG    . TYR A 1 630 ? 137.244 122.539 98.872  1.00 36.69 ?  630 TYR A CG    1 
ATOM   5067  C  CD1   . TYR A 1 630 ? 137.706 122.873 100.138 1.00 34.53 ?  630 TYR A CD1   1 
ATOM   5068  C  CD2   . TYR A 1 630 ? 135.917 122.808 98.567  1.00 37.62 ?  630 TYR A CD2   1 
ATOM   5069  C  CE1   . TYR A 1 630 ? 136.872 123.453 101.071 1.00 37.48 ?  630 TYR A CE1   1 
ATOM   5070  C  CE2   . TYR A 1 630 ? 135.076 123.388 99.494  1.00 38.03 ?  630 TYR A CE2   1 
ATOM   5071  C  CZ    . TYR A 1 630 ? 135.559 123.709 100.744 1.00 44.44 ?  630 TYR A CZ    1 
ATOM   5072  O  OH    . TYR A 1 630 ? 134.722 124.287 101.670 1.00 44.97 ?  630 TYR A OH    1 
ATOM   5073  N  N     . ASP A 1 631 ? 139.549 122.007 94.923  1.00 38.93 ?  631 ASP A N     1 
ATOM   5074  C  CA    . ASP A 1 631 ? 140.377 121.379 93.904  1.00 38.97 ?  631 ASP A CA    1 
ATOM   5075  C  C     . ASP A 1 631 ? 141.499 122.282 93.411  1.00 41.98 ?  631 ASP A C     1 
ATOM   5076  O  O     . ASP A 1 631 ? 142.407 121.797 92.728  1.00 43.81 ?  631 ASP A O     1 
ATOM   5077  C  CB    . ASP A 1 631 ? 139.513 120.948 92.716  1.00 39.94 ?  631 ASP A CB    1 
ATOM   5078  C  CG    . ASP A 1 631 ? 138.379 120.030 93.123  1.00 45.71 ?  631 ASP A CG    1 
ATOM   5079  O  OD1   . ASP A 1 631 ? 138.563 119.239 94.072  1.00 46.44 ?  631 ASP A OD1   1 
ATOM   5080  O  OD2   . ASP A 1 631 ? 137.302 120.100 92.495  1.00 43.66 -1 631 ASP A OD2   1 
ATOM   5081  N  N     . MET A 1 632 ? 141.462 123.569 93.741  1.00 35.51 ?  632 MET A N     1 
ATOM   5082  C  CA    . MET A 1 632 ? 142.438 124.517 93.233  1.00 32.76 ?  632 MET A CA    1 
ATOM   5083  C  C     . MET A 1 632 ? 143.723 124.478 94.053  1.00 37.18 ?  632 MET A C     1 
ATOM   5084  O  O     . MET A 1 632 ? 143.742 124.068 95.216  1.00 35.27 ?  632 MET A O     1 
ATOM   5085  C  CB    . MET A 1 632 ? 141.868 125.934 93.244  1.00 31.39 ?  632 MET A CB    1 
ATOM   5086  C  CG    . MET A 1 632 ? 140.804 126.184 92.200  1.00 35.86 ?  632 MET A CG    1 
ATOM   5087  S  SD    . MET A 1 632 ? 140.258 127.898 92.185  1.00 39.76 ?  632 MET A SD    1 
ATOM   5088  C  CE    . MET A 1 632 ? 138.943 127.807 90.980  1.00 33.94 ?  632 MET A CE    1 
ATOM   5089  N  N     . ASP A 1 633 ? 144.807 124.918 93.422  1.00 33.46 ?  633 ASP A N     1 
ATOM   5090  C  CA    . ASP A 1 633 ? 146.077 125.101 94.113  1.00 31.47 ?  633 ASP A CA    1 
ATOM   5091  C  C     . ASP A 1 633 ? 146.000 126.371 94.950  1.00 31.69 ?  633 ASP A C     1 
ATOM   5092  O  O     . ASP A 1 633 ? 145.780 127.461 94.412  1.00 35.01 ?  633 ASP A O     1 
ATOM   5093  C  CB    . ASP A 1 633 ? 147.224 125.178 93.109  1.00 29.78 ?  633 ASP A CB    1 
ATOM   5094  C  CG    . ASP A 1 633 ? 148.587 125.144 93.773  1.00 36.13 ?  633 ASP A CG    1 
ATOM   5095  O  OD1   . ASP A 1 633 ? 148.652 124.937 95.003  1.00 38.03 ?  633 ASP A OD1   1 
ATOM   5096  O  OD2   . ASP A 1 633 ? 149.596 125.328 93.062  1.00 37.92 -1 633 ASP A OD2   1 
ATOM   5097  N  N     . MET A 1 634 ? 146.177 126.232 96.265  1.00 27.77 ?  634 MET A N     1 
ATOM   5098  C  CA    . MET A 1 634 ? 146.061 127.385 97.149  1.00 25.57 ?  634 MET A CA    1 
ATOM   5099  C  C     . MET A 1 634 ? 147.158 128.414 96.915  1.00 27.47 ?  634 MET A C     1 
ATOM   5100  O  O     . MET A 1 634 ? 146.966 129.585 97.251  1.00 26.26 ?  634 MET A O     1 
ATOM   5101  C  CB    . MET A 1 634 ? 146.070 126.934 98.609  1.00 27.41 ?  634 MET A CB    1 
ATOM   5102  C  CG    . MET A 1 634 ? 144.699 126.556 99.137  1.00 28.92 ?  634 MET A CG    1 
ATOM   5103  S  SD    . MET A 1 634 ? 143.505 127.894 98.953  1.00 43.53 ?  634 MET A SD    1 
ATOM   5104  C  CE    . MET A 1 634 ? 142.354 127.164 97.791  1.00 28.34 ?  634 MET A CE    1 
ATOM   5105  N  N     . PHE A 1 635 ? 148.295 128.010 96.347  1.00 26.68 ?  635 PHE A N     1 
ATOM   5106  C  CA    . PHE A 1 635 ? 149.337 128.980 96.024  1.00 23.26 ?  635 PHE A CA    1 
ATOM   5107  C  C     . PHE A 1 635 ? 148.877 129.939 94.932  1.00 21.66 ?  635 PHE A C     1 
ATOM   5108  O  O     . PHE A 1 635 ? 149.149 131.142 95.000  1.00 25.79 ?  635 PHE A O     1 
ATOM   5109  C  CB    . PHE A 1 635 ? 150.618 128.259 95.608  1.00 23.22 ?  635 PHE A CB    1 
ATOM   5110  C  CG    . PHE A 1 635 ? 151.503 127.884 96.763  1.00 24.30 ?  635 PHE A CG    1 
ATOM   5111  C  CD1   . PHE A 1 635 ? 150.972 127.311 97.904  1.00 23.65 ?  635 PHE A CD1   1 
ATOM   5112  C  CD2   . PHE A 1 635 ? 152.868 128.108 96.705  1.00 27.13 ?  635 PHE A CD2   1 
ATOM   5113  C  CE1   . PHE A 1 635 ? 151.784 126.966 98.967  1.00 22.91 ?  635 PHE A CE1   1 
ATOM   5114  C  CE2   . PHE A 1 635 ? 153.685 127.766 97.765  1.00 29.75 ?  635 PHE A CE2   1 
ATOM   5115  C  CZ    . PHE A 1 635 ? 153.141 127.194 98.896  1.00 26.44 ?  635 PHE A CZ    1 
ATOM   5116  N  N     . LYS A 1 636 ? 148.165 129.431 93.926  1.00 23.36 ?  636 LYS A N     1 
ATOM   5117  C  CA    . LYS A 1 636 ? 147.671 130.304 92.866  1.00 26.62 ?  636 LYS A CA    1 
ATOM   5118  C  C     . LYS A 1 636 ? 146.516 131.175 93.349  1.00 27.24 ?  636 LYS A C     1 
ATOM   5119  O  O     . LYS A 1 636 ? 146.377 132.322 92.905  1.00 32.63 ?  636 LYS A O     1 
ATOM   5120  C  CB    . LYS A 1 636 ? 147.262 129.465 91.657  1.00 28.33 ?  636 LYS A CB    1 
ATOM   5121  C  CG    . LYS A 1 636 ? 148.445 128.798 90.972  1.00 28.04 ?  636 LYS A CG    1 
ATOM   5122  C  CD    . LYS A 1 636 ? 148.015 127.961 89.785  1.00 33.47 ?  636 LYS A CD    1 
ATOM   5123  C  CE    . LYS A 1 636 ? 149.157 127.100 89.272  1.00 32.60 ?  636 LYS A CE    1 
ATOM   5124  N  NZ    . LYS A 1 636 ? 148.687 126.096 88.278  1.00 33.68 1  636 LYS A NZ    1 
ATOM   5125  N  N     . VAL A 1 637 ? 145.692 130.661 94.263  1.00 23.94 ?  637 VAL A N     1 
ATOM   5126  C  CA    . VAL A 1 637 ? 144.673 131.497 94.894  1.00 16.29 ?  637 VAL A CA    1 
ATOM   5127  C  C     . VAL A 1 637 ? 145.331 132.613 95.696  1.00 23.84 ?  637 VAL A C     1 
ATOM   5128  O  O     . VAL A 1 637 ? 144.877 133.763 95.677  1.00 27.23 ?  637 VAL A O     1 
ATOM   5129  C  CB    . VAL A 1 637 ? 143.742 130.639 95.769  1.00 20.35 ?  637 VAL A CB    1 
ATOM   5130  C  CG1   . VAL A 1 637 ? 142.597 131.478 96.310  1.00 21.92 ?  637 VAL A CG1   1 
ATOM   5131  C  CG2   . VAL A 1 637 ? 143.210 129.460 94.973  1.00 25.87 ?  637 VAL A CG2   1 
ATOM   5132  N  N     . VAL A 1 638 ? 146.414 132.291 96.409  1.00 25.45 ?  638 VAL A N     1 
ATOM   5133  C  CA    . VAL A 1 638 ? 147.173 133.312 97.128  1.00 21.79 ?  638 VAL A CA    1 
ATOM   5134  C  C     . VAL A 1 638 ? 147.735 134.339 96.156  1.00 17.02 ?  638 VAL A C     1 
ATOM   5135  O  O     . VAL A 1 638 ? 147.734 135.542 96.432  1.00 25.22 ?  638 VAL A O     1 
ATOM   5136  C  CB    . VAL A 1 638 ? 148.289 132.659 97.966  1.00 20.12 ?  638 VAL A CB    1 
ATOM   5137  C  CG1   . VAL A 1 638 ? 149.339 133.687 98.352  1.00 15.90 ?  638 VAL A CG1   1 
ATOM   5138  C  CG2   . VAL A 1 638 ? 147.716 132.001 99.206  1.00 18.74 ?  638 VAL A CG2   1 
ATOM   5139  N  N     . ASP A 1 639 ? 148.235 133.879 95.008  1.00 20.16 ?  639 ASP A N     1 
ATOM   5140  C  CA    . ASP A 1 639 ? 148.776 134.798 94.011  1.00 17.42 ?  639 ASP A CA    1 
ATOM   5141  C  C     . ASP A 1 639 ? 147.704 135.753 93.500  1.00 23.65 ?  639 ASP A C     1 
ATOM   5142  O  O     . ASP A 1 639 ? 147.944 136.959 93.375  1.00 34.49 ?  639 ASP A O     1 
ATOM   5143  C  CB    . ASP A 1 639 ? 149.386 134.010 92.852  1.00 22.23 ?  639 ASP A CB    1 
ATOM   5144  C  CG    . ASP A 1 639 ? 150.746 133.439 93.187  1.00 30.93 ?  639 ASP A CG    1 
ATOM   5145  O  OD1   . ASP A 1 639 ? 151.517 134.115 93.898  1.00 31.40 ?  639 ASP A OD1   1 
ATOM   5146  O  OD2   . ASP A 1 639 ? 151.045 132.312 92.741  1.00 30.53 -1 639 ASP A OD2   1 
ATOM   5147  N  N     . MET A 1 640 ? 146.511 135.230 93.208  1.00 23.94 ?  640 MET A N     1 
ATOM   5148  C  CA    . MET A 1 640 ? 145.419 136.091 92.761  1.00 17.59 ?  640 MET A CA    1 
ATOM   5149  C  C     . MET A 1 640 ? 145.006 137.078 93.848  1.00 19.97 ?  640 MET A C     1 
ATOM   5150  O  O     . MET A 1 640 ? 144.764 138.261 93.569  1.00 30.73 ?  640 MET A O     1 
ATOM   5151  C  CB    . MET A 1 640 ? 144.223 135.246 92.327  1.00 23.08 ?  640 MET A CB    1 
ATOM   5152  C  CG    . MET A 1 640 ? 142.886 135.954 92.488  1.00 26.44 ?  640 MET A CG    1 
ATOM   5153  S  SD    . MET A 1 640 ? 142.313 136.739 90.972  1.00 31.92 ?  640 MET A SD    1 
ATOM   5154  C  CE    . MET A 1 640 ? 142.209 135.330 89.880  1.00 23.12 ?  640 MET A CE    1 
ATOM   5155  N  N     . ILE A 1 641 ? 144.916 136.610 95.094  1.00 15.77 ?  641 ILE A N     1 
ATOM   5156  C  CA    . ILE A 1 641 ? 144.493 137.497 96.170  1.00 18.94 ?  641 ILE A CA    1 
ATOM   5157  C  C     . ILE A 1 641 ? 145.539 138.575 96.419  1.00 19.32 ?  641 ILE A C     1 
ATOM   5158  O  O     . ILE A 1 641 ? 145.191 139.717 96.722  1.00 24.40 ?  641 ILE A O     1 
ATOM   5159  C  CB    . ILE A 1 641 ? 144.175 136.687 97.441  1.00 20.90 ?  641 ILE A CB    1 
ATOM   5160  C  CG1   . ILE A 1 641 ? 142.983 135.766 97.185  1.00 17.33 ?  641 ILE A CG1   1 
ATOM   5161  C  CG2   . ILE A 1 641 ? 143.848 137.610 98.603  1.00 16.43 ?  641 ILE A CG2   1 
ATOM   5162  C  CD1   . ILE A 1 641 ? 141.887 136.407 96.359  1.00 20.72 ?  641 ILE A CD1   1 
ATOM   5163  N  N     . ALA A 1 642 ? 146.825 138.249 96.275  1.00 15.52 ?  642 ALA A N     1 
ATOM   5164  C  CA    . ALA A 1 642 ? 147.870 139.263 96.402  1.00 16.76 ?  642 ALA A CA    1 
ATOM   5165  C  C     . ALA A 1 642 ? 147.821 140.254 95.247  1.00 19.56 ?  642 ALA A C     1 
ATOM   5166  O  O     . ALA A 1 642 ? 148.037 141.459 95.439  1.00 30.33 ?  642 ALA A O     1 
ATOM   5167  C  CB    . ALA A 1 642 ? 149.241 138.595 96.479  1.00 17.60 ?  642 ALA A CB    1 
ATOM   5168  N  N     . THR A 1 643 ? 147.541 139.761 94.038  1.00 16.40 ?  643 THR A N     1 
ATOM   5169  C  CA    . THR A 1 643 ? 147.387 140.644 92.890  1.00 16.82 ?  643 THR A CA    1 
ATOM   5170  C  C     . THR A 1 643 ? 146.261 141.643 93.121  1.00 20.72 ?  643 THR A C     1 
ATOM   5171  O  O     . THR A 1 643 ? 146.399 142.831 92.809  1.00 23.15 ?  643 THR A O     1 
ATOM   5172  C  CB    . THR A 1 643 ? 147.126 139.815 91.633  1.00 18.01 ?  643 THR A CB    1 
ATOM   5173  O  OG1   . THR A 1 643 ? 148.298 139.058 91.307  1.00 22.20 ?  643 THR A OG1   1 
ATOM   5174  C  CG2   . THR A 1 643 ? 146.770 140.708 90.468  1.00 14.96 ?  643 THR A CG2   1 
ATOM   5175  N  N     . ILE A 1 644 ? 145.140 141.180 93.673  1.00 17.72 ?  644 ILE A N     1 
ATOM   5176  C  CA    . ILE A 1 644 ? 144.054 142.098 94.006  1.00 11.61 ?  644 ILE A CA    1 
ATOM   5177  C  C     . ILE A 1 644 ? 144.459 143.018 95.155  1.00 15.14 ?  644 ILE A C     1 
ATOM   5178  O  O     . ILE A 1 644 ? 144.174 144.221 95.134  1.00 19.99 ?  644 ILE A O     1 
ATOM   5179  C  CB    . ILE A 1 644 ? 142.771 141.314 94.334  1.00 15.27 ?  644 ILE A CB    1 
ATOM   5180  C  CG1   . ILE A 1 644 ? 142.356 140.446 93.146  1.00 18.05 ?  644 ILE A CG1   1 
ATOM   5181  C  CG2   . ILE A 1 644 ? 141.653 142.266 94.711  1.00 9.24  ?  644 ILE A CG2   1 
ATOM   5182  C  CD1   . ILE A 1 644 ? 141.324 139.399 93.494  1.00 21.85 ?  644 ILE A CD1   1 
ATOM   5183  N  N     . GLN A 1 645 ? 145.137 142.469 96.167  1.00 13.04 ?  645 GLN A N     1 
ATOM   5184  C  CA    . GLN A 1 645 ? 145.470 143.219 97.372  1.00 14.10 ?  645 GLN A CA    1 
ATOM   5185  C  C     . GLN A 1 645 ? 146.424 144.365 97.084  1.00 15.57 ?  645 GLN A C     1 
ATOM   5186  O  O     . GLN A 1 645 ? 146.419 145.370 97.806  1.00 19.84 ?  645 GLN A O     1 
ATOM   5187  C  CB    . GLN A 1 645 ? 146.076 142.278 98.413  1.00 12.50 ?  645 GLN A CB    1 
ATOM   5188  C  CG    . GLN A 1 645 ? 146.341 142.916 99.762  1.00 8.73  ?  645 GLN A CG    1 
ATOM   5189  C  CD    . GLN A 1 645 ? 145.066 143.210 100.521 1.00 11.82 ?  645 GLN A CD    1 
ATOM   5190  O  OE1   . GLN A 1 645 ? 144.542 142.352 101.229 1.00 17.05 ?  645 GLN A OE1   1 
ATOM   5191  N  NE2   . GLN A 1 645 ? 144.558 144.426 100.376 1.00 6.56  ?  645 GLN A NE2   1 
ATOM   5192  N  N     . GLN A 1 646 ? 147.244 144.240 96.044  1.00 20.80 ?  646 GLN A N     1 
ATOM   5193  C  CA    . GLN A 1 646 ? 148.135 145.343 95.710  1.00 14.50 ?  646 GLN A CA    1 
ATOM   5194  C  C     . GLN A 1 646 ? 147.378 146.592 95.271  1.00 13.51 ?  646 GLN A C     1 
ATOM   5195  O  O     . GLN A 1 646 ? 147.976 147.670 95.223  1.00 17.75 ?  646 GLN A O     1 
ATOM   5196  C  CB    . GLN A 1 646 ? 149.124 144.913 94.626  1.00 17.94 ?  646 GLN A CB    1 
ATOM   5197  C  CG    . GLN A 1 646 ? 148.603 145.028 93.213  1.00 21.82 ?  646 GLN A CG    1 
ATOM   5198  C  CD    . GLN A 1 646 ? 149.526 144.379 92.204  1.00 26.95 ?  646 GLN A CD    1 
ATOM   5199  O  OE1   . GLN A 1 646 ? 150.656 144.822 92.007  1.00 25.36 ?  646 GLN A OE1   1 
ATOM   5200  N  NE2   . GLN A 1 646 ? 149.050 143.321 91.560  1.00 22.86 ?  646 GLN A NE2   1 
ATOM   5201  N  N     . HIS A 1 647 ? 146.083 146.480 94.970  1.00 21.28 ?  647 HIS A N     1 
ATOM   5202  C  CA    . HIS A 1 647 ? 145.260 147.626 94.600  1.00 14.87 ?  647 HIS A CA    1 
ATOM   5203  C  C     . HIS A 1 647 ? 144.178 147.932 95.625  1.00 11.61 ?  647 HIS A C     1 
ATOM   5204  O  O     . HIS A 1 647 ? 143.349 148.817 95.389  1.00 19.13 ?  647 HIS A O     1 
ATOM   5205  C  CB    . HIS A 1 647 ? 144.624 147.400 93.227  1.00 10.26 ?  647 HIS A CB    1 
ATOM   5206  C  CG    . HIS A 1 647 ? 145.613 147.078 92.153  1.00 15.52 ?  647 HIS A CG    1 
ATOM   5207  N  ND1   . HIS A 1 647 ? 146.586 147.967 91.751  1.00 16.09 ?  647 HIS A ND1   1 
ATOM   5208  C  CD2   . HIS A 1 647 ? 145.786 145.965 91.404  1.00 13.32 ?  647 HIS A CD2   1 
ATOM   5209  C  CE1   . HIS A 1 647 ? 147.315 147.416 90.798  1.00 18.02 ?  647 HIS A CE1   1 
ATOM   5210  N  NE2   . HIS A 1 647 ? 146.849 146.201 90.568  1.00 19.55 ?  647 HIS A NE2   1 
ATOM   5211  N  N     . ILE A 1 648 ? 144.159 147.228 96.753  1.00 11.14 ?  648 ILE A N     1 
ATOM   5212  C  CA    . ILE A 1 648 ? 143.174 147.437 97.809  1.00 13.31 ?  648 ILE A CA    1 
ATOM   5213  C  C     . ILE A 1 648 ? 143.901 147.999 99.022  1.00 13.02 ?  648 ILE A C     1 
ATOM   5214  O  O     . ILE A 1 648 ? 144.872 147.402 99.503  1.00 23.58 ?  648 ILE A O     1 
ATOM   5215  C  CB    . ILE A 1 648 ? 142.437 146.133 98.156  1.00 11.46 ?  648 ILE A CB    1 
ATOM   5216  C  CG1   . ILE A 1 648 ? 141.810 145.514 96.904  1.00 7.66  ?  648 ILE A CG1   1 
ATOM   5217  C  CG2   . ILE A 1 648 ? 141.374 146.383 99.209  1.00 9.21  ?  648 ILE A CG2   1 
ATOM   5218  C  CD1   . ILE A 1 648 ? 140.654 146.306 96.336  1.00 9.58  ?  648 ILE A CD1   1 
ATOM   5219  N  N     . ASP A 1 649 ? 143.438 149.153 99.511  1.00 6.66  ?  649 ASP A N     1 
ATOM   5220  C  CA    . ASP A 1 649 ? 144.106 149.790 100.643 1.00 11.95 ?  649 ASP A CA    1 
ATOM   5221  C  C     . ASP A 1 649 ? 143.872 149.014 101.932 1.00 9.56  ?  649 ASP A C     1 
ATOM   5222  O  O     . ASP A 1 649 ? 144.776 148.902 102.768 1.00 28.87 ?  649 ASP A O     1 
ATOM   5223  C  CB    . ASP A 1 649 ? 143.636 151.237 100.787 1.00 21.67 ?  649 ASP A CB    1 
ATOM   5224  C  CG    . ASP A 1 649 ? 142.148 151.389 100.578 1.00 18.65 ?  649 ASP A CG    1 
ATOM   5225  O  OD1   . ASP A 1 649 ? 141.578 150.609 99.791  1.00 24.11 ?  649 ASP A OD1   1 
ATOM   5226  O  OD2   . ASP A 1 649 ? 141.548 152.290 101.197 1.00 15.97 -1 649 ASP A OD2   1 
ATOM   5227  N  N     . GLN A 1 650 ? 142.672 148.481 102.117 1.00 10.05 ?  650 GLN A N     1 
ATOM   5228  C  CA    . GLN A 1 650 ? 142.376 147.615 103.247 1.00 6.55  ?  650 GLN A CA    1 
ATOM   5229  C  C     . GLN A 1 650 ? 142.626 146.164 102.831 1.00 5.55  ?  650 GLN A C     1 
ATOM   5230  O  O     . GLN A 1 650 ? 143.249 145.901 101.800 1.00 16.73 ?  650 GLN A O     1 
ATOM   5231  C  CB    . GLN A 1 650 ? 140.948 147.864 103.740 1.00 3.48  ?  650 GLN A CB    1 
ATOM   5232  C  CG    . GLN A 1 650 ? 140.690 149.289 104.191 1.00 4.86  ?  650 GLN A CG    1 
ATOM   5233  C  CD    . GLN A 1 650 ? 139.262 149.504 104.635 1.00 10.24 ?  650 GLN A CD    1 
ATOM   5234  O  OE1   . GLN A 1 650 ? 138.855 149.036 105.697 1.00 21.25 ?  650 GLN A OE1   1 
ATOM   5235  N  NE2   . GLN A 1 650 ? 138.491 150.214 103.824 1.00 5.10  ?  650 GLN A NE2   1 
ATOM   5236  N  N     . GLY A 1 651 ? 142.159 145.207 103.630 1.00 6.66  ?  651 GLY A N     1 
ATOM   5237  C  CA    . GLY A 1 651 ? 142.390 143.809 103.350 1.00 8.64  ?  651 GLY A CA    1 
ATOM   5238  C  C     . GLY A 1 651 ? 141.282 143.170 102.535 1.00 6.35  ?  651 GLY A C     1 
ATOM   5239  O  O     . GLY A 1 651 ? 140.284 143.790 102.173 1.00 9.60  ?  651 GLY A O     1 
ATOM   5240  N  N     . ILE A 1 652 ? 141.484 141.889 102.246 1.00 18.34 ?  652 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 652 ? 140.531 141.063 101.520 1.00 8.90  ?  652 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 652 ? 140.202 139.862 102.389 1.00 7.64  ?  652 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 652 ? 141.109 139.219 102.931 1.00 19.66 ?  652 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 652 ? 141.092 140.607 100.160 1.00 6.86  ?  652 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 652 ? 141.500 141.811 99.313  1.00 0.00  ?  652 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 652 ? 140.082 139.745 99.425  1.00 10.78 ?  652 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 652 ? 142.381 141.446 98.150  1.00 4.02  ?  652 ILE A CD1   1 
ATOM   5248  N  N     . SER A 1 653 ? 138.915 139.563 102.532 1.00 15.16 ?  653 SER A N     1 
ATOM   5249  C  CA    . SER A 1 653 ? 138.501 138.363 103.253 1.00 12.99 ?  653 SER A CA    1 
ATOM   5250  C  C     . SER A 1 653 ? 138.955 137.154 102.449 1.00 13.55 ?  653 SER A C     1 
ATOM   5251  O  O     . SER A 1 653 ? 138.349 136.798 101.437 1.00 26.18 ?  653 SER A O     1 
ATOM   5252  C  CB    . SER A 1 653 ? 136.995 138.357 103.473 1.00 12.53 ?  653 SER A CB    1 
ATOM   5253  O  OG    . SER A 1 653 ? 136.678 138.691 104.811 1.00 15.77 ?  653 SER A OG    1 
ATOM   5254  N  N     . PHE A 1 654 ? 140.030 136.520 102.900 1.00 18.67 ?  654 PHE A N     1 
ATOM   5255  C  CA    . PHE A 1 654 ? 140.708 135.460 102.159 1.00 9.68  ?  654 PHE A CA    1 
ATOM   5256  C  C     . PHE A 1 654 ? 140.549 134.162 102.940 1.00 15.65 ?  654 PHE A C     1 
ATOM   5257  O  O     . PHE A 1 654 ? 141.249 133.929 103.929 1.00 24.30 ?  654 PHE A O     1 
ATOM   5258  C  CB    . PHE A 1 654 ? 142.176 135.817 101.946 1.00 9.20  ?  654 PHE A CB    1 
ATOM   5259  C  CG    . PHE A 1 654 ? 142.938 134.821 101.117 1.00 16.73 ?  654 PHE A CG    1 
ATOM   5260  C  CD1   . PHE A 1 654 ? 142.280 133.924 100.292 1.00 22.93 ?  654 PHE A CD1   1 
ATOM   5261  C  CD2   . PHE A 1 654 ? 144.319 134.788 101.163 1.00 18.70 ?  654 PHE A CD2   1 
ATOM   5262  C  CE1   . PHE A 1 654 ? 142.985 133.012 99.537  1.00 14.90 ?  654 PHE A CE1   1 
ATOM   5263  C  CE2   . PHE A 1 654 ? 145.028 133.880 100.408 1.00 20.49 ?  654 PHE A CE2   1 
ATOM   5264  C  CZ    . PHE A 1 654 ? 144.360 132.991 99.594  1.00 15.99 ?  654 PHE A CZ    1 
ATOM   5265  N  N     . THR A 1 655 ? 139.634 133.314 102.483 1.00 20.69 ?  655 THR A N     1 
ATOM   5266  C  CA    . THR A 1 655 ? 139.415 132.008 103.083 1.00 16.46 ?  655 THR A CA    1 
ATOM   5267  C  C     . THR A 1 655 ? 140.262 130.967 102.364 1.00 23.11 ?  655 THR A C     1 
ATOM   5268  O  O     . THR A 1 655 ? 140.256 130.898 101.132 1.00 28.79 ?  655 THR A O     1 
ATOM   5269  C  CB    . THR A 1 655 ? 137.935 131.627 103.015 1.00 23.48 ?  655 THR A CB    1 
ATOM   5270  O  OG1   . THR A 1 655 ? 137.189 132.423 103.945 1.00 23.66 ?  655 THR A OG1   1 
ATOM   5271  C  CG2   . THR A 1 655 ? 137.740 130.155 103.344 1.00 24.36 ?  655 THR A CG2   1 
ATOM   5272  N  N     . LEU A 1 656 ? 141.004 130.177 103.135 1.00 31.95 ?  656 LEU A N     1 
ATOM   5273  C  CA    . LEU A 1 656 ? 141.724 129.044 102.576 1.00 28.61 ?  656 LEU A CA    1 
ATOM   5274  C  C     . LEU A 1 656 ? 140.772 127.873 102.391 1.00 27.54 ?  656 LEU A C     1 
ATOM   5275  O  O     . LEU A 1 656 ? 139.905 127.623 103.231 1.00 31.16 ?  656 LEU A O     1 
ATOM   5276  C  CB    . LEU A 1 656 ? 142.881 128.634 103.487 1.00 29.59 ?  656 LEU A CB    1 
ATOM   5277  C  CG    . LEU A 1 656 ? 143.978 129.675 103.700 1.00 30.46 ?  656 LEU A CG    1 
ATOM   5278  C  CD1   . LEU A 1 656 ? 145.165 129.060 104.423 1.00 26.80 ?  656 LEU A CD1   1 
ATOM   5279  C  CD2   . LEU A 1 656 ? 144.401 130.292 102.377 1.00 27.73 ?  656 LEU A CD2   1 
ATOM   5280  N  N     . PHE A 1 657 ? 140.926 127.161 101.280 1.00 26.53 ?  657 PHE A N     1 
ATOM   5281  C  CA    . PHE A 1 657 ? 140.089 126.009 100.963 1.00 28.20 ?  657 PHE A CA    1 
ATOM   5282  C  C     . PHE A 1 657 ? 140.987 124.784 100.885 1.00 36.33 ?  657 PHE A C     1 
ATOM   5283  O  O     . PHE A 1 657 ? 141.745 124.625 99.921  1.00 37.74 ?  657 PHE A O     1 
ATOM   5284  C  CB    . PHE A 1 657 ? 139.326 126.229 99.660  1.00 29.41 ?  657 PHE A CB    1 
ATOM   5285  C  CG    . PHE A 1 657 ? 138.518 127.492 99.645  1.00 32.69 ?  657 PHE A CG    1 
ATOM   5286  C  CD1   . PHE A 1 657 ? 137.246 127.522 100.187 1.00 30.22 ?  657 PHE A CD1   1 
ATOM   5287  C  CD2   . PHE A 1 657 ? 139.030 128.651 99.087  1.00 33.87 ?  657 PHE A CD2   1 
ATOM   5288  C  CE1   . PHE A 1 657 ? 136.503 128.684 100.175 1.00 32.64 ?  657 PHE A CE1   1 
ATOM   5289  C  CE2   . PHE A 1 657 ? 138.289 129.814 99.068  1.00 29.81 ?  657 PHE A CE2   1 
ATOM   5290  C  CZ    . PHE A 1 657 ? 137.025 129.831 99.615  1.00 32.98 ?  657 PHE A CZ    1 
ATOM   5291  N  N     . LEU A 1 658 ? 140.901 123.922 101.891 1.00 40.31 ?  658 LEU A N     1 
ATOM   5292  C  CA    . LEU A 1 658 ? 141.807 122.798 102.038 1.00 42.67 ?  658 LEU A CA    1 
ATOM   5293  C  C     . LEU A 1 658 ? 141.060 121.482 101.879 1.00 45.45 ?  658 LEU A C     1 
ATOM   5294  O  O     . LEU A 1 658 ? 139.860 121.389 102.152 1.00 46.68 ?  658 LEU A O     1 
ATOM   5295  C  CB    . LEU A 1 658 ? 142.496 122.831 103.404 1.00 40.37 ?  658 LEU A CB    1 
ATOM   5296  C  CG    . LEU A 1 658 ? 142.810 124.220 103.959 1.00 39.41 ?  658 LEU A CG    1 
ATOM   5297  C  CD1   . LEU A 1 658 ? 143.092 124.136 105.447 1.00 41.38 ?  658 LEU A CD1   1 
ATOM   5298  C  CD2   . LEU A 1 658 ? 143.978 124.853 103.221 1.00 42.05 ?  658 LEU A CD2   1 
ATOM   5299  N  N     . LYS A 1 659 ? 141.780 120.473 101.407 1.00 51.27 ?  659 LYS A N     1 
ATOM   5300  C  CA    . LYS A 1 659 ? 141.291 119.106 101.406 1.00 51.78 ?  659 LYS A CA    1 
ATOM   5301  C  C     . LYS A 1 659 ? 141.637 118.437 102.731 1.00 52.89 ?  659 LYS A C     1 
ATOM   5302  O  O     . LYS A 1 659 ? 142.561 118.844 103.438 1.00 54.58 ?  659 LYS A O     1 
ATOM   5303  C  CB    . LYS A 1 659 ? 141.890 118.316 100.242 1.00 54.80 ?  659 LYS A CB    1 
ATOM   5304  C  CG    . LYS A 1 659 ? 141.652 118.943 98.878  1.00 53.58 ?  659 LYS A CG    1 
ATOM   5305  C  CD    . LYS A 1 659 ? 142.078 118.007 97.759  1.00 53.18 ?  659 LYS A CD    1 
ATOM   5306  C  CE    . LYS A 1 659 ? 141.817 118.622 96.393  1.00 53.02 ?  659 LYS A CE    1 
ATOM   5307  N  NZ    . LYS A 1 659 ? 141.880 117.610 95.303  1.00 52.86 1  659 LYS A NZ    1 
ATOM   5308  N  N     . ASP A 1 660 ? 140.870 117.397 103.068 1.00 57.82 ?  660 ASP A N     1 
ATOM   5309  C  CA    . ASP A 1 660 ? 141.145 116.648 104.287 1.00 57.29 ?  660 ASP A CA    1 
ATOM   5310  C  C     . ASP A 1 660 ? 142.473 115.905 104.221 1.00 55.49 ?  660 ASP A C     1 
ATOM   5311  O  O     . ASP A 1 660 ? 143.008 115.521 105.267 1.00 56.14 ?  660 ASP A O     1 
ATOM   5312  C  CB    . ASP A 1 660 ? 140.008 115.666 104.571 1.00 58.51 ?  660 ASP A CB    1 
ATOM   5313  C  CG    . ASP A 1 660 ? 139.440 115.051 103.306 1.00 61.52 ?  660 ASP A CG    1 
ATOM   5314  O  OD1   . ASP A 1 660 ? 140.231 114.591 102.457 1.00 59.08 ?  660 ASP A OD1   1 
ATOM   5315  O  OD2   . ASP A 1 660 ? 138.199 115.030 103.162 1.00 61.60 -1 660 ASP A OD2   1 
ATOM   5316  N  N     . THR A 1 661 ? 143.016 115.697 103.019 1.00 53.18 ?  661 THR A N     1 
ATOM   5317  C  CA    . THR A 1 661 ? 144.267 114.956 102.890 1.00 55.32 ?  661 THR A CA    1 
ATOM   5318  C  C     . THR A 1 661 ? 145.461 115.787 103.342 1.00 54.64 ?  661 THR A C     1 
ATOM   5319  O  O     . THR A 1 661 ? 146.375 115.263 103.990 1.00 55.17 ?  661 THR A O     1 
ATOM   5320  C  CB    . THR A 1 661 ? 144.457 114.493 101.446 1.00 56.55 ?  661 THR A CB    1 
ATOM   5321  O  OG1   . THR A 1 661 ? 145.038 115.553 100.676 1.00 56.41 ?  661 THR A OG1   1 
ATOM   5322  C  CG2   . THR A 1 661 ? 143.124 114.098 100.833 1.00 54.38 ?  661 THR A CG2   1 
ATOM   5323  N  N     . MET A 1 662 ? 145.478 117.077 103.012 1.00 52.78 ?  662 MET A N     1 
ATOM   5324  C  CA    . MET A 1 662 ? 146.626 117.905 103.351 1.00 52.47 ?  662 MET A CA    1 
ATOM   5325  C  C     . MET A 1 662 ? 146.718 118.116 104.858 1.00 51.28 ?  662 MET A C     1 
ATOM   5326  O  O     . MET A 1 662 ? 145.712 118.163 105.571 1.00 49.11 ?  662 MET A O     1 
ATOM   5327  C  CB    . MET A 1 662 ? 146.564 119.248 102.617 1.00 50.11 ?  662 MET A CB    1 
ATOM   5328  C  CG    . MET A 1 662 ? 146.014 120.410 103.424 1.00 51.94 ?  662 MET A CG    1 
ATOM   5329  S  SD    . MET A 1 662 ? 145.912 121.906 102.425 1.00 62.99 ?  662 MET A SD    1 
ATOM   5330  C  CE    . MET A 1 662 ? 144.963 121.315 101.029 1.00 48.13 ?  662 MET A CE    1 
ATOM   5331  N  N     . THR A 1 663 ? 147.951 118.220 105.338 1.00 45.64 ?  663 THR A N     1 
ATOM   5332  C  CA    . THR A 1 663 ? 148.261 118.256 106.756 1.00 44.52 ?  663 THR A CA    1 
ATOM   5333  C  C     . THR A 1 663 ? 148.487 119.696 107.212 1.00 44.92 ?  663 THR A C     1 
ATOM   5334  O  O     . THR A 1 663 ? 148.298 120.650 106.452 1.00 46.43 ?  663 THR A O     1 
ATOM   5335  C  CB    . THR A 1 663 ? 149.479 117.375 107.032 1.00 43.39 ?  663 THR A CB    1 
ATOM   5336  O  OG1   . THR A 1 663 ? 150.674 118.144 106.852 1.00 42.25 ?  663 THR A OG1   1 
ATOM   5337  C  CG2   . THR A 1 663 ? 149.498 116.194 106.073 1.00 44.97 ?  663 THR A CG2   1 
ATOM   5338  N  N     . THR A 1 664 ? 148.899 119.860 108.472 1.00 39.16 ?  664 THR A N     1 
ATOM   5339  C  CA    . THR A 1 664 ? 149.188 121.192 108.987 1.00 38.73 ?  664 THR A CA    1 
ATOM   5340  C  C     . THR A 1 664 ? 150.430 121.799 108.353 1.00 37.04 ?  664 THR A C     1 
ATOM   5341  O  O     . THR A 1 664 ? 150.560 123.027 108.334 1.00 40.13 ?  664 THR A O     1 
ATOM   5342  C  CB    . THR A 1 664 ? 149.352 121.159 110.508 1.00 39.50 ?  664 THR A CB    1 
ATOM   5343  O  OG1   . THR A 1 664 ? 150.607 120.557 110.846 1.00 39.06 ?  664 THR A OG1   1 
ATOM   5344  C  CG2   . THR A 1 664 ? 148.218 120.378 111.152 1.00 36.70 ?  664 THR A CG2   1 
ATOM   5345  N  N     . ARG A 1 665 ? 151.345 120.975 107.838 1.00 37.74 ?  665 ARG A N     1 
ATOM   5346  C  CA    . ARG A 1 665 ? 152.490 121.513 107.112 1.00 34.74 ?  665 ARG A CA    1 
ATOM   5347  C  C     . ARG A 1 665 ? 152.042 122.245 105.855 1.00 39.12 ?  665 ARG A C     1 
ATOM   5348  O  O     . ARG A 1 665 ? 152.568 123.313 105.531 1.00 44.89 ?  665 ARG A O     1 
ATOM   5349  C  CB    . ARG A 1 665 ? 153.469 120.396 106.758 1.00 37.03 ?  665 ARG A CB    1 
ATOM   5350  C  CG    . ARG A 1 665 ? 154.456 120.764 105.662 1.00 35.80 ?  665 ARG A CG    1 
ATOM   5351  C  CD    . ARG A 1 665 ? 155.863 120.312 106.002 1.00 37.90 ?  665 ARG A CD    1 
ATOM   5352  N  NE    . ARG A 1 665 ? 156.793 120.563 104.909 1.00 40.76 ?  665 ARG A NE    1 
ATOM   5353  C  CZ    . ARG A 1 665 ? 157.073 119.696 103.946 1.00 42.19 ?  665 ARG A CZ    1 
ATOM   5354  N  NH1   . ARG A 1 665 ? 156.505 118.502 103.908 1.00 41.36 1  665 ARG A NH1   1 
ATOM   5355  N  NH2   . ARG A 1 665 ? 157.942 120.035 102.999 1.00 41.42 ?  665 ARG A NH2   1 
ATOM   5356  N  N     . ASP A 1 666 ? 151.065 121.688 105.136 1.00 37.63 ?  666 ASP A N     1 
ATOM   5357  C  CA    . ASP A 1 666 ? 150.546 122.358 103.949 1.00 36.14 ?  666 ASP A CA    1 
ATOM   5358  C  C     . ASP A 1 666 ? 149.846 123.663 104.311 1.00 39.97 ?  666 ASP A C     1 
ATOM   5359  O  O     . ASP A 1 666 ? 149.996 124.669 103.608 1.00 44.17 ?  666 ASP A O     1 
ATOM   5360  C  CB    . ASP A 1 666 ? 149.600 121.426 103.195 1.00 42.08 ?  666 ASP A CB    1 
ATOM   5361  C  CG    . ASP A 1 666 ? 150.296 120.181 102.687 1.00 46.23 ?  666 ASP A CG    1 
ATOM   5362  O  OD1   . ASP A 1 666 ? 151.341 120.316 102.019 1.00 44.32 ?  666 ASP A OD1   1 
ATOM   5363  O  OD2   . ASP A 1 666 ? 149.801 119.066 102.960 1.00 46.85 -1 666 ASP A OD2   1 
ATOM   5364  N  N     . LEU A 1 667 ? 149.078 123.665 105.402 1.00 33.15 ?  667 LEU A N     1 
ATOM   5365  C  CA    . LEU A 1 667 ? 148.429 124.893 105.849 1.00 30.35 ?  667 LEU A CA    1 
ATOM   5366  C  C     . LEU A 1 667 ? 149.459 125.953 106.216 1.00 30.18 ?  667 LEU A C     1 
ATOM   5367  O  O     . LEU A 1 667 ? 149.316 127.126 105.849 1.00 33.76 ?  667 LEU A O     1 
ATOM   5368  C  CB    . LEU A 1 667 ? 147.522 124.596 107.044 1.00 33.25 ?  667 LEU A CB    1 
ATOM   5369  C  CG    . LEU A 1 667 ? 146.202 125.357 107.163 1.00 35.96 ?  667 LEU A CG    1 
ATOM   5370  C  CD1   . LEU A 1 667 ? 145.324 124.704 108.213 1.00 35.10 ?  667 LEU A CD1   1 
ATOM   5371  C  CD2   . LEU A 1 667 ? 146.427 126.822 107.495 1.00 33.24 ?  667 LEU A CD2   1 
ATOM   5372  N  N     . ASN A 1 668 ? 150.508 125.556 106.939 1.00 30.42 ?  668 ASN A N     1 
ATOM   5373  C  CA    . ASN A 1 668 ? 151.563 126.496 107.297 1.00 27.03 ?  668 ASN A CA    1 
ATOM   5374  C  C     . ASN A 1 668 ? 152.290 127.003 106.060 1.00 27.13 ?  668 ASN A C     1 
ATOM   5375  O  O     . ASN A 1 668 ? 152.675 128.173 105.998 1.00 33.76 ?  668 ASN A O     1 
ATOM   5376  C  CB    . ASN A 1 668 ? 152.546 125.839 108.265 1.00 28.88 ?  668 ASN A CB    1 
ATOM   5377  C  CG    . ASN A 1 668 ? 152.118 125.972 109.710 1.00 31.15 ?  668 ASN A CG    1 
ATOM   5378  O  OD1   . ASN A 1 668 ? 152.371 125.086 110.525 1.00 39.82 ?  668 ASN A OD1   1 
ATOM   5379  N  ND2   . ASN A 1 668 ? 151.465 127.080 110.035 1.00 28.99 ?  668 ASN A ND2   1 
ATOM   5380  N  N     . ARG A 1 669 ? 152.496 126.134 105.069 1.00 29.15 ?  669 ARG A N     1 
ATOM   5381  C  CA    . ARG A 1 669 ? 153.132 126.562 103.827 1.00 30.94 ?  669 ARG A CA    1 
ATOM   5382  C  C     . ARG A 1 669 ? 152.274 127.580 103.092 1.00 28.85 ?  669 ARG A C     1 
ATOM   5383  O  O     . ARG A 1 669 ? 152.795 128.560 102.549 1.00 28.98 ?  669 ARG A O     1 
ATOM   5384  C  CB    . ARG A 1 669 ? 153.414 125.356 102.934 1.00 31.95 ?  669 ARG A CB    1 
ATOM   5385  C  CG    . ARG A 1 669 ? 154.880 124.983 102.845 1.00 29.86 ?  669 ARG A CG    1 
ATOM   5386  C  CD    . ARG A 1 669 ? 155.100 123.844 101.863 1.00 35.06 ?  669 ARG A CD    1 
ATOM   5387  N  NE    . ARG A 1 669 ? 155.214 124.313 100.487 1.00 33.74 ?  669 ARG A NE    1 
ATOM   5388  C  CZ    . ARG A 1 669 ? 156.261 124.962 99.994  1.00 34.89 ?  669 ARG A CZ    1 
ATOM   5389  N  NH1   . ARG A 1 669 ? 157.319 125.235 100.738 1.00 33.74 1  669 ARG A NH1   1 
ATOM   5390  N  NH2   . ARG A 1 669 ? 156.245 125.345 98.721  1.00 37.58 ?  669 ARG A NH2   1 
ATOM   5391  N  N     . ILE A 1 670 ? 150.957 127.363 103.055 1.00 25.18 ?  670 ILE A N     1 
ATOM   5392  C  CA    . ILE A 1 670 ? 150.067 128.339 102.433 1.00 25.57 ?  670 ILE A CA    1 
ATOM   5393  C  C     . ILE A 1 670 ? 150.119 129.663 103.185 1.00 27.89 ?  670 ILE A C     1 
ATOM   5394  O  O     . ILE A 1 670 ? 150.163 130.737 102.574 1.00 32.77 ?  670 ILE A O     1 
ATOM   5395  C  CB    . ILE A 1 670 ? 148.630 127.792 102.352 1.00 28.03 ?  670 ILE A CB    1 
ATOM   5396  C  CG1   . ILE A 1 670 ? 148.587 126.510 101.519 1.00 30.18 ?  670 ILE A CG1   1 
ATOM   5397  C  CG2   . ILE A 1 670 ? 147.700 128.831 101.753 1.00 25.40 ?  670 ILE A CG2   1 
ATOM   5398  C  CD1   . ILE A 1 670 ? 147.387 125.638 101.810 1.00 26.89 ?  670 ILE A CD1   1 
ATOM   5399  N  N     . ASP A 1 671 ? 150.118 129.609 104.519 1.00 24.47 ?  671 ASP A N     1 
ATOM   5400  C  CA    . ASP A 1 671 ? 150.193 130.836 105.310 1.00 21.06 ?  671 ASP A CA    1 
ATOM   5401  C  C     . ASP A 1 671 ? 151.502 131.578 105.066 1.00 25.88 ?  671 ASP A C     1 
ATOM   5402  O  O     . ASP A 1 671 ? 151.515 132.807 104.936 1.00 27.34 ?  671 ASP A O     1 
ATOM   5403  C  CB    . ASP A 1 671 ? 150.032 130.513 106.795 1.00 22.89 ?  671 ASP A CB    1 
ATOM   5404  C  CG    . ASP A 1 671 ? 148.690 129.884 107.113 1.00 34.47 ?  671 ASP A CG    1 
ATOM   5405  O  OD1   . ASP A 1 671 ? 147.748 130.053 106.311 1.00 34.26 ?  671 ASP A OD1   1 
ATOM   5406  O  OD2   . ASP A 1 671 ? 148.579 129.220 108.165 1.00 35.03 -1 671 ASP A OD2   1 
ATOM   5407  N  N     . LEU A 1 672 ? 152.616 130.848 105.000 1.00 23.57 ?  672 LEU A N     1 
ATOM   5408  C  CA    . LEU A 1 672 ? 153.912 131.482 104.791 1.00 19.62 ?  672 LEU A CA    1 
ATOM   5409  C  C     . LEU A 1 672 ? 154.056 132.021 103.375 1.00 18.97 ?  672 LEU A C     1 
ATOM   5410  O  O     . LEU A 1 672 ? 154.720 133.041 103.171 1.00 24.16 ?  672 LEU A O     1 
ATOM   5411  C  CB    . LEU A 1 672 ? 155.035 130.494 105.102 1.00 27.26 ?  672 LEU A CB    1 
ATOM   5412  C  CG    . LEU A 1 672 ? 155.144 130.051 106.561 1.00 23.67 ?  672 LEU A CG    1 
ATOM   5413  C  CD1   . LEU A 1 672 ? 156.034 128.827 106.680 1.00 21.82 ?  672 LEU A CD1   1 
ATOM   5414  C  CD2   . LEU A 1 672 ? 155.656 131.186 107.429 1.00 20.76 ?  672 LEU A CD2   1 
ATOM   5415  N  N     . TYR A 1 673 ? 153.454 131.354 102.388 1.00 21.31 ?  673 TYR A N     1 
ATOM   5416  C  CA    . TYR A 1 673 ? 153.462 131.886 101.030 1.00 18.01 ?  673 TYR A CA    1 
ATOM   5417  C  C     . TYR A 1 673 ? 152.576 133.119 100.923 1.00 21.32 ?  673 TYR A C     1 
ATOM   5418  O  O     . TYR A 1 673 ? 152.886 134.050 100.172 1.00 23.54 ?  673 TYR A O     1 
ATOM   5419  C  CB    . TYR A 1 673 ? 153.014 130.809 100.043 1.00 16.74 ?  673 TYR A CB    1 
ATOM   5420  C  CG    . TYR A 1 673 ? 153.088 131.240 98.599  1.00 22.24 ?  673 TYR A CG    1 
ATOM   5421  C  CD1   . TYR A 1 673 ? 154.308 131.518 98.001  1.00 23.24 ?  673 TYR A CD1   1 
ATOM   5422  C  CD2   . TYR A 1 673 ? 151.939 131.370 97.833  1.00 20.22 ?  673 TYR A CD2   1 
ATOM   5423  C  CE1   . TYR A 1 673 ? 154.382 131.913 96.682  1.00 18.97 ?  673 TYR A CE1   1 
ATOM   5424  C  CE2   . TYR A 1 673 ? 152.002 131.765 96.513  1.00 22.76 ?  673 TYR A CE2   1 
ATOM   5425  C  CZ    . TYR A 1 673 ? 153.226 132.033 95.943  1.00 21.41 ?  673 TYR A CZ    1 
ATOM   5426  O  OH    . TYR A 1 673 ? 153.296 132.428 94.628  1.00 26.15 ?  673 TYR A OH    1 
ATOM   5427  N  N     . ALA A 1 674 ? 151.464 133.137 101.661 1.00 21.02 ?  674 ALA A N     1 
ATOM   5428  C  CA    . ALA A 1 674 ? 150.637 134.335 101.731 1.00 16.37 ?  674 ALA A CA    1 
ATOM   5429  C  C     . ALA A 1 674 ? 151.407 135.491 102.354 1.00 16.90 ?  674 ALA A C     1 
ATOM   5430  O  O     . ALA A 1 674 ? 151.353 136.624 101.862 1.00 25.79 ?  674 ALA A O     1 
ATOM   5431  C  CB    . ALA A 1 674 ? 149.366 134.040 102.524 1.00 18.01 ?  674 ALA A CB    1 
ATOM   5432  N  N     . HIS A 1 675 ? 152.138 135.219 103.435 1.00 15.15 ?  675 HIS A N     1 
ATOM   5433  C  CA    . HIS A 1 675 ? 152.980 136.245 104.039 1.00 15.76 ?  675 HIS A CA    1 
ATOM   5434  C  C     . HIS A 1 675 ? 154.055 136.719 103.067 1.00 20.74 ?  675 HIS A C     1 
ATOM   5435  O  O     . HIS A 1 675 ? 154.350 137.916 102.988 1.00 27.09 ?  675 HIS A O     1 
ATOM   5436  C  CB    . HIS A 1 675 ? 153.612 135.711 105.325 1.00 12.33 ?  675 HIS A CB    1 
ATOM   5437  C  CG    . HIS A 1 675 ? 154.582 136.657 105.958 1.00 21.52 ?  675 HIS A CG    1 
ATOM   5438  N  ND1   . HIS A 1 675 ? 155.946 136.529 105.814 1.00 24.93 ?  675 HIS A ND1   1 
ATOM   5439  C  CD2   . HIS A 1 675 ? 154.385 137.748 106.734 1.00 19.57 ?  675 HIS A CD2   1 
ATOM   5440  C  CE1   . HIS A 1 675 ? 156.549 137.500 106.475 1.00 25.63 ?  675 HIS A CE1   1 
ATOM   5441  N  NE2   . HIS A 1 675 ? 155.625 138.254 107.042 1.00 22.92 ?  675 HIS A NE2   1 
ATOM   5442  N  N     . HIS A 1 676 ? 154.652 135.788 102.322 1.00 19.67 ?  676 HIS A N     1 
ATOM   5443  C  CA    . HIS A 1 676 ? 155.686 136.144 101.355 1.00 20.42 ?  676 HIS A CA    1 
ATOM   5444  C  C     . HIS A 1 676 ? 155.115 136.959 100.200 1.00 24.31 ?  676 HIS A C     1 
ATOM   5445  O  O     . HIS A 1 676 ? 155.760 137.897 99.716  1.00 25.05 ?  676 HIS A O     1 
ATOM   5446  C  CB    . HIS A 1 676 ? 156.365 134.879 100.834 1.00 23.92 ?  676 HIS A CB    1 
ATOM   5447  C  CG    . HIS A 1 676 ? 157.247 135.109 99.647  1.00 25.00 ?  676 HIS A CG    1 
ATOM   5448  N  ND1   . HIS A 1 676 ? 158.440 135.795 99.727  1.00 20.88 ?  676 HIS A ND1   1 
ATOM   5449  C  CD2   . HIS A 1 676 ? 157.110 134.743 98.351  1.00 19.79 ?  676 HIS A CD2   1 
ATOM   5450  C  CE1   . HIS A 1 676 ? 158.998 135.842 98.531  1.00 25.77 ?  676 HIS A CE1   1 
ATOM   5451  N  NE2   . HIS A 1 676 ? 158.212 135.211 97.678  1.00 28.82 ?  676 HIS A NE2   1 
ATOM   5452  N  N     . ARG A 1 677 ? 153.911 136.619 99.746  1.00 21.42 ?  677 ARG A N     1 
ATOM   5453  C  CA    . ARG A 1 677 ? 153.312 137.274 98.589  1.00 20.36 ?  677 ARG A CA    1 
ATOM   5454  C  C     . ARG A 1 677 ? 152.632 138.590 98.934  1.00 24.10 ?  677 ARG A C     1 
ATOM   5455  O  O     . ARG A 1 677 ? 152.096 139.244 98.033  1.00 25.29 ?  677 ARG A O     1 
ATOM   5456  C  CB    . ARG A 1 677 ? 152.307 136.335 97.918  1.00 18.85 ?  677 ARG A CB    1 
ATOM   5457  C  CG    . ARG A 1 677 ? 152.934 135.366 96.932  1.00 20.21 ?  677 ARG A CG    1 
ATOM   5458  C  CD    . ARG A 1 677 ? 153.471 136.089 95.710  1.00 20.22 ?  677 ARG A CD    1 
ATOM   5459  N  NE    . ARG A 1 677 ? 152.452 136.252 94.680  1.00 25.02 ?  677 ARG A NE    1 
ATOM   5460  C  CZ    . ARG A 1 677 ? 151.954 137.419 94.297  1.00 27.26 ?  677 ARG A CZ    1 
ATOM   5461  N  NH1   . ARG A 1 677 ? 152.361 138.555 94.840  1.00 21.21 1  677 ARG A NH1   1 
ATOM   5462  N  NH2   . ARG A 1 677 ? 151.026 137.448 93.346  1.00 22.30 ?  677 ARG A NH2   1 
ATOM   5463  N  N     . GLY A 1 678 ? 152.639 138.994 100.200 1.00 20.70 ?  678 GLY A N     1 
ATOM   5464  C  CA    . GLY A 1 678 ? 152.033 140.248 100.594 1.00 16.08 ?  678 GLY A CA    1 
ATOM   5465  C  C     . GLY A 1 678 ? 150.584 140.162 101.002 1.00 16.22 ?  678 GLY A C     1 
ATOM   5466  O  O     . GLY A 1 678 ? 149.911 141.198 101.057 1.00 23.71 ?  678 GLY A O     1 
ATOM   5467  N  N     . ILE A 1 679 ? 150.074 138.964 101.284 1.00 15.50 ?  679 ILE A N     1 
ATOM   5468  C  CA    . ILE A 1 679 ? 148.705 138.827 101.764 1.00 11.34 ?  679 ILE A CA    1 
ATOM   5469  C  C     . ILE A 1 679 ? 148.595 139.476 103.134 1.00 15.26 ?  679 ILE A C     1 
ATOM   5470  O  O     . ILE A 1 679 ? 149.421 139.234 104.024 1.00 23.09 ?  679 ILE A O     1 
ATOM   5471  C  CB    . ILE A 1 679 ? 148.292 137.350 101.812 1.00 15.65 ?  679 ILE A CB    1 
ATOM   5472  C  CG1   . ILE A 1 679 ? 148.222 136.766 100.401 1.00 15.46 ?  679 ILE A CG1   1 
ATOM   5473  C  CG2   . ILE A 1 679 ? 146.964 137.184 102.529 1.00 15.73 ?  679 ILE A CG2   1 
ATOM   5474  C  CD1   . ILE A 1 679 ? 147.322 137.526 99.486  1.00 13.41 ?  679 ILE A CD1   1 
ATOM   5475  N  N     . LYS A 1 680 ? 147.579 140.316 103.309 1.00 13.20 ?  680 LYS A N     1 
ATOM   5476  C  CA    . LYS A 1 680 ? 147.410 141.048 104.555 1.00 8.26  ?  680 LYS A CA    1 
ATOM   5477  C  C     . LYS A 1 680 ? 146.696 140.216 105.617 1.00 8.16  ?  680 LYS A C     1 
ATOM   5478  O  O     . LYS A 1 680 ? 147.125 140.183 106.774 1.00 16.91 ?  680 LYS A O     1 
ATOM   5479  C  CB    . LYS A 1 680 ? 146.645 142.347 104.296 1.00 8.86  ?  680 LYS A CB    1 
ATOM   5480  C  CG    . LYS A 1 680 ? 147.425 143.384 103.510 1.00 0.00  ?  680 LYS A CG    1 
ATOM   5481  C  CD    . LYS A 1 680 ? 146.609 144.648 103.319 1.00 6.45  ?  680 LYS A CD    1 
ATOM   5482  C  CE    . LYS A 1 680 ? 147.210 145.547 102.260 1.00 13.22 ?  680 LYS A CE    1 
ATOM   5483  N  NZ    . LYS A 1 680 ? 146.456 146.821 102.122 1.00 10.77 1  680 LYS A NZ    1 
ATOM   5484  N  N     . THR A 1 681 ? 145.611 139.544 105.244 1.00 15.71 ?  681 THR A N     1 
ATOM   5485  C  CA    . THR A 1 681 ? 144.822 138.757 106.178 1.00 8.89  ?  681 THR A CA    1 
ATOM   5486  C  C     . THR A 1 681 ? 144.456 137.417 105.558 1.00 15.33 ?  681 THR A C     1 
ATOM   5487  O  O     . THR A 1 681 ? 144.289 137.302 104.342 1.00 22.36 ?  681 THR A O     1 
ATOM   5488  C  CB    . THR A 1 681 ? 143.533 139.483 106.593 1.00 16.05 ?  681 THR A CB    1 
ATOM   5489  O  OG1   . THR A 1 681 ? 142.847 139.951 105.426 1.00 30.21 ?  681 THR A OG1   1 
ATOM   5490  C  CG2   . THR A 1 681 ? 143.839 140.661 107.495 1.00 3.10  ?  681 THR A CG2   1 
ATOM   5491  N  N     . ILE A 1 682 ? 144.331 136.406 106.412 1.00 15.27 ?  682 ILE A N     1 
ATOM   5492  C  CA    . ILE A 1 682 ? 143.788 135.107 106.035 1.00 9.32  ?  682 ILE A CA    1 
ATOM   5493  C  C     . ILE A 1 682 ? 142.557 134.856 106.893 1.00 13.63 ?  682 ILE A C     1 
ATOM   5494  O  O     . ILE A 1 682 ? 142.638 134.893 108.126 1.00 21.07 ?  682 ILE A O     1 
ATOM   5495  C  CB    . ILE A 1 682 ? 144.820 133.980 106.208 1.00 12.93 ?  682 ILE A CB    1 
ATOM   5496  C  CG1   . ILE A 1 682 ? 146.215 134.460 105.807 1.00 17.99 ?  682 ILE A CG1   1 
ATOM   5497  C  CG2   . ILE A 1 682 ? 144.430 132.791 105.366 1.00 20.80 ?  682 ILE A CG2   1 
ATOM   5498  C  CD1   . ILE A 1 682 ? 147.254 133.363 105.799 1.00 19.45 ?  682 ILE A CD1   1 
ATOM   5499  N  N     . TYR A 1 683 ? 141.419 134.613 106.241 1.00 18.77 ?  683 TYR A N     1 
ATOM   5500  C  CA    . TYR A 1 683 ? 140.149 134.571 106.966 1.00 12.07 ?  683 TYR A CA    1 
ATOM   5501  C  C     . TYR A 1 683 ? 139.892 133.202 107.591 1.00 19.43 ?  683 TYR A C     1 
ATOM   5502  O  O     . TYR A 1 683 ? 139.854 133.063 108.815 1.00 32.31 ?  683 TYR A O     1 
ATOM   5503  C  CB    . TYR A 1 683 ? 139.005 134.965 106.025 1.00 18.00 ?  683 TYR A CB    1 
ATOM   5504  C  CG    . TYR A 1 683 ? 137.663 135.130 106.702 1.00 16.18 ?  683 TYR A CG    1 
ATOM   5505  C  CD1   . TYR A 1 683 ? 137.576 135.391 108.063 1.00 12.18 ?  683 TYR A CD1   1 
ATOM   5506  C  CD2   . TYR A 1 683 ? 136.483 135.033 105.978 1.00 9.75  ?  683 TYR A CD2   1 
ATOM   5507  C  CE1   . TYR A 1 683 ? 136.355 135.544 108.683 1.00 15.88 ?  683 TYR A CE1   1 
ATOM   5508  C  CE2   . TYR A 1 683 ? 135.257 135.187 106.592 1.00 18.37 ?  683 TYR A CE2   1 
ATOM   5509  C  CZ    . TYR A 1 683 ? 135.199 135.442 107.943 1.00 19.26 ?  683 TYR A CZ    1 
ATOM   5510  O  OH    . TYR A 1 683 ? 133.980 135.594 108.560 1.00 26.27 ?  683 TYR A OH    1 
ATOM   5511  N  N     . TYR A 1 684 ? 139.733 132.174 106.765 1.00 29.27 ?  684 TYR A N     1 
ATOM   5512  C  CA    . TYR A 1 684 ? 139.262 130.891 107.257 1.00 25.72 ?  684 TYR A CA    1 
ATOM   5513  C  C     . TYR A 1 684 ? 140.017 129.765 106.574 1.00 32.85 ?  684 TYR A C     1 
ATOM   5514  O  O     . TYR A 1 684 ? 140.550 129.928 105.473 1.00 36.53 ?  684 TYR A O     1 
ATOM   5515  C  CB    . TYR A 1 684 ? 137.755 130.719 107.023 1.00 23.92 ?  684 TYR A CB    1 
ATOM   5516  C  CG    . TYR A 1 684 ? 136.904 131.033 108.230 1.00 22.24 ?  684 TYR A CG    1 
ATOM   5517  C  CD1   . TYR A 1 684 ? 137.110 130.384 109.439 1.00 26.54 ?  684 TYR A CD1   1 
ATOM   5518  C  CD2   . TYR A 1 684 ? 135.892 131.981 108.161 1.00 29.36 ?  684 TYR A CD2   1 
ATOM   5519  C  CE1   . TYR A 1 684 ? 136.331 130.668 110.545 1.00 30.37 ?  684 TYR A CE1   1 
ATOM   5520  C  CE2   . TYR A 1 684 ? 135.109 132.274 109.261 1.00 26.07 ?  684 TYR A CE2   1 
ATOM   5521  C  CZ    . TYR A 1 684 ? 135.333 131.615 110.449 1.00 29.63 ?  684 TYR A CZ    1 
ATOM   5522  O  OH    . TYR A 1 684 ? 134.556 131.903 111.546 1.00 32.26 ?  684 TYR A OH    1 
ATOM   5523  N  N     . ALA A 1 685 ? 140.059 128.619 107.246 1.00 31.03 ?  685 ALA A N     1 
ATOM   5524  C  CA    . ALA A 1 685 ? 140.614 127.385 106.702 1.00 32.41 ?  685 ALA A CA    1 
ATOM   5525  C  C     . ALA A 1 685 ? 139.469 126.379 106.648 1.00 36.55 ?  685 ALA A C     1 
ATOM   5526  O  O     . ALA A 1 685 ? 139.266 125.598 107.581 1.00 43.59 ?  685 ALA A O     1 
ATOM   5527  C  CB    . ALA A 1 685 ? 141.779 126.880 107.543 1.00 32.11 ?  685 ALA A CB    1 
ATOM   5528  N  N     . ARG A 1 686 ? 138.714 126.408 105.552 1.00 32.51 ?  686 ARG A N     1 
ATOM   5529  C  CA    . ARG A 1 686 ? 137.587 125.507 105.367 1.00 33.05 ?  686 ARG A CA    1 
ATOM   5530  C  C     . ARG A 1 686 ? 138.088 124.196 104.775 1.00 38.70 ?  686 ARG A C     1 
ATOM   5531  O  O     . ARG A 1 686 ? 138.622 124.176 103.662 1.00 40.64 ?  686 ARG A O     1 
ATOM   5532  C  CB    . ARG A 1 686 ? 136.544 126.146 104.453 1.00 38.13 ?  686 ARG A CB    1 
ATOM   5533  C  CG    . ARG A 1 686 ? 135.827 127.335 105.064 1.00 38.73 ?  686 ARG A CG    1 
ATOM   5534  C  CD    . ARG A 1 686 ? 134.552 127.657 104.303 1.00 39.90 ?  686 ARG A CD    1 
ATOM   5535  N  NE    . ARG A 1 686 ? 133.670 126.501 104.194 1.00 42.70 ?  686 ARG A NE    1 
ATOM   5536  C  CZ    . ARG A 1 686 ? 132.353 126.552 104.331 1.00 42.66 ?  686 ARG A CZ    1 
ATOM   5537  N  NH1   . ARG A 1 686 ? 131.726 127.691 104.579 1.00 41.77 1  686 ARG A NH1   1 
ATOM   5538  N  NH2   . ARG A 1 686 ? 131.645 125.432 104.214 1.00 42.47 ?  686 ARG A NH2   1 
ATOM   5539  N  N     . THR A 1 687 ? 137.920 123.107 105.519 1.00 48.40 ?  687 THR A N     1 
ATOM   5540  C  CA    . THR A 1 687 ? 138.342 121.786 105.079 1.00 46.64 ?  687 THR A CA    1 
ATOM   5541  C  C     . THR A 1 687 ? 137.157 121.040 104.481 1.00 47.93 ?  687 THR A C     1 
ATOM   5542  O  O     . THR A 1 687 ? 136.078 120.986 105.078 1.00 50.75 ?  687 THR A O     1 
ATOM   5543  C  CB    . THR A 1 687 ? 138.937 120.987 106.242 1.00 46.66 ?  687 THR A CB    1 
ATOM   5544  O  OG1   . THR A 1 687 ? 140.238 121.499 106.562 1.00 48.39 ?  687 THR A OG1   1 
ATOM   5545  C  CG2   . THR A 1 687 ? 139.057 119.514 105.879 1.00 47.30 ?  687 THR A CG2   1 
ATOM   5546  N  N     . LYS A 1 688 ? 137.366 120.470 103.300 1.00 48.04 ?  688 LYS A N     1 
ATOM   5547  C  CA    . LYS A 1 688 ? 136.313 119.733 102.611 1.00 48.98 ?  688 LYS A CA    1 
ATOM   5548  C  C     . LYS A 1 688 ? 136.178 118.323 103.175 1.00 53.36 ?  688 LYS A C     1 
ATOM   5549  O  O     . LYS A 1 688 ? 137.153 117.733 103.639 1.00 55.18 ?  688 LYS A O     1 
ATOM   5550  C  CB    . LYS A 1 688 ? 136.594 119.674 101.109 1.00 49.54 ?  688 LYS A CB    1 
ATOM   5551  C  CG    . LYS A 1 688 ? 135.462 119.079 100.291 1.00 48.07 ?  688 LYS A CG    1 
ATOM   5552  C  CD    . LYS A 1 688 ? 135.777 119.109 98.806  1.00 47.51 ?  688 LYS A CD    1 
ATOM   5553  C  CE    . LYS A 1 688 ? 134.618 118.565 97.989  1.00 51.68 ?  688 LYS A CE    1 
ATOM   5554  N  NZ    . LYS A 1 688 ? 134.899 118.612 96.527  1.00 52.23 ?  688 LYS A NZ    1 
ATOM   5555  N  N     . VAL B 1 6   ? 155.024 118.880 163.270 1.00 57.44 ?  6   VAL B N     1 
ATOM   5556  C  CA    . VAL B 1 6   ? 153.914 119.734 163.677 1.00 58.35 ?  6   VAL B CA    1 
ATOM   5557  C  C     . VAL B 1 6   ? 154.370 120.737 164.732 1.00 60.21 ?  6   VAL B C     1 
ATOM   5558  O  O     . VAL B 1 6   ? 155.202 120.418 165.580 1.00 58.78 ?  6   VAL B O     1 
ATOM   5559  C  CB    . VAL B 1 6   ? 152.730 118.896 164.194 1.00 58.16 ?  6   VAL B CB    1 
ATOM   5560  C  CG1   . VAL B 1 6   ? 152.048 118.178 163.040 1.00 58.66 ?  6   VAL B CG1   1 
ATOM   5561  C  CG2   . VAL B 1 6   ? 153.199 117.900 165.239 1.00 58.25 ?  6   VAL B CG2   1 
ATOM   5562  N  N     . PRO B 1 7   ? 153.831 121.951 164.669 1.00 57.76 ?  7   PRO B N     1 
ATOM   5563  C  CA    . PRO B 1 7   ? 154.215 122.984 165.637 1.00 53.33 ?  7   PRO B CA    1 
ATOM   5564  C  C     . PRO B 1 7   ? 153.755 122.639 167.045 1.00 52.92 ?  7   PRO B C     1 
ATOM   5565  O  O     . PRO B 1 7   ? 152.793 121.896 167.256 1.00 55.02 ?  7   PRO B O     1 
ATOM   5566  C  CB    . PRO B 1 7   ? 153.514 124.244 165.119 1.00 52.57 ?  7   PRO B CB    1 
ATOM   5567  C  CG    . PRO B 1 7   ? 153.157 123.950 163.701 1.00 52.52 ?  7   PRO B CG    1 
ATOM   5568  C  CD    . PRO B 1 7   ? 152.945 122.474 163.617 1.00 54.44 ?  7   PRO B CD    1 
ATOM   5569  N  N     . LYS B 1 8   ? 154.474 123.198 168.022 1.00 50.58 ?  8   LYS B N     1 
ATOM   5570  C  CA    . LYS B 1 8   ? 154.160 122.933 169.423 1.00 49.37 ?  8   LYS B CA    1 
ATOM   5571  C  C     . LYS B 1 8   ? 152.773 123.446 169.790 1.00 52.20 ?  8   LYS B C     1 
ATOM   5572  O  O     . LYS B 1 8   ? 152.013 122.761 170.486 1.00 54.02 ?  8   LYS B O     1 
ATOM   5573  C  CB    . LYS B 1 8   ? 155.222 123.562 170.323 1.00 51.24 ?  8   LYS B CB    1 
ATOM   5574  C  CG    . LYS B 1 8   ? 154.800 123.702 171.776 1.00 52.38 ?  8   LYS B CG    1 
ATOM   5575  C  CD    . LYS B 1 8   ? 156.001 123.721 172.704 1.00 51.18 ?  8   LYS B CD    1 
ATOM   5576  C  CE    . LYS B 1 8   ? 155.571 123.651 174.160 1.00 51.50 ?  8   LYS B CE    1 
ATOM   5577  N  NZ    . LYS B 1 8   ? 155.518 124.999 174.789 1.00 52.01 1  8   LYS B NZ    1 
ATOM   5578  N  N     . TRP B 1 9   ? 152.424 124.653 169.334 1.00 53.51 ?  9   TRP B N     1 
ATOM   5579  C  CA    . TRP B 1 9   ? 151.099 125.186 169.628 1.00 51.21 ?  9   TRP B CA    1 
ATOM   5580  C  C     . TRP B 1 9   ? 150.008 124.357 168.966 1.00 49.73 ?  9   TRP B C     1 
ATOM   5581  O  O     . TRP B 1 9   ? 148.912 124.227 169.520 1.00 51.44 ?  9   TRP B O     1 
ATOM   5582  C  CB    . TRP B 1 9   ? 150.994 126.648 169.191 1.00 51.68 ?  9   TRP B CB    1 
ATOM   5583  C  CG    . TRP B 1 9   ? 151.325 126.894 167.752 1.00 49.36 ?  9   TRP B CG    1 
ATOM   5584  C  CD1   . TRP B 1 9   ? 150.459 126.870 166.699 1.00 48.25 ?  9   TRP B CD1   1 
ATOM   5585  C  CD2   . TRP B 1 9   ? 152.608 127.228 167.209 1.00 49.96 ?  9   TRP B CD2   1 
ATOM   5586  N  NE1   . TRP B 1 9   ? 151.123 127.157 165.533 1.00 47.82 ?  9   TRP B NE1   1 
ATOM   5587  C  CE2   . TRP B 1 9   ? 152.443 127.383 165.819 1.00 49.58 ?  9   TRP B CE2   1 
ATOM   5588  C  CE3   . TRP B 1 9   ? 153.878 127.406 167.762 1.00 47.79 ?  9   TRP B CE3   1 
ATOM   5589  C  CZ2   . TRP B 1 9   ? 153.502 127.705 164.975 1.00 48.99 ?  9   TRP B CZ2   1 
ATOM   5590  C  CZ3   . TRP B 1 9   ? 154.928 127.726 166.923 1.00 49.28 ?  9   TRP B CZ3   1 
ATOM   5591  C  CH2   . TRP B 1 9   ? 154.733 127.870 165.544 1.00 50.26 ?  9   TRP B CH2   1 
ATOM   5592  N  N     . ILE B 1 10  ? 150.289 123.784 167.795 1.00 52.27 ?  10  ILE B N     1 
ATOM   5593  C  CA    . ILE B 1 10  ? 149.320 122.910 167.145 1.00 52.32 ?  10  ILE B CA    1 
ATOM   5594  C  C     . ILE B 1 10  ? 149.066 121.670 167.994 1.00 53.45 ?  10  ILE B C     1 
ATOM   5595  O  O     . ILE B 1 10  ? 147.917 121.246 168.170 1.00 55.24 ?  10  ILE B O     1 
ATOM   5596  C  CB    . ILE B 1 10  ? 149.805 122.544 165.731 1.00 52.71 ?  10  ILE B CB    1 
ATOM   5597  C  CG1   . ILE B 1 10  ? 149.662 123.747 164.793 1.00 52.31 ?  10  ILE B CG1   1 
ATOM   5598  C  CG2   . ILE B 1 10  ? 149.046 121.338 165.196 1.00 53.05 ?  10  ILE B CG2   1 
ATOM   5599  C  CD1   . ILE B 1 10  ? 148.350 123.807 164.054 1.00 53.46 ?  10  ILE B CD1   1 
ATOM   5600  N  N     . GLN B 1 11  ? 150.130 121.075 168.539 1.00 53.92 ?  11  GLN B N     1 
ATOM   5601  C  CA    . GLN B 1 11  ? 149.963 119.924 169.422 1.00 55.14 ?  11  GLN B CA    1 
ATOM   5602  C  C     . GLN B 1 11  ? 149.198 120.301 170.683 1.00 54.84 ?  11  GLN B C     1 
ATOM   5603  O  O     . GLN B 1 11  ? 148.328 119.550 171.140 1.00 57.06 ?  11  GLN B O     1 
ATOM   5604  C  CB    . GLN B 1 11  ? 151.328 119.337 169.785 1.00 56.03 ?  11  GLN B CB    1 
ATOM   5605  C  CG    . GLN B 1 11  ? 152.183 118.960 168.591 1.00 56.59 ?  11  GLN B CG    1 
ATOM   5606  C  CD    . GLN B 1 11  ? 153.661 118.940 168.922 1.00 58.95 ?  11  GLN B CD    1 
ATOM   5607  O  OE1   . GLN B 1 11  ? 154.506 119.178 168.059 1.00 58.89 ?  11  GLN B OE1   1 
ATOM   5608  N  NE2   . GLN B 1 11  ? 153.982 118.658 170.179 1.00 55.94 ?  11  GLN B NE2   1 
ATOM   5609  N  N     . LEU B 1 12  ? 149.506 121.464 171.262 1.00 51.73 ?  12  LEU B N     1 
ATOM   5610  C  CA    . LEU B 1 12  ? 148.800 121.893 172.465 1.00 50.64 ?  12  LEU B CA    1 
ATOM   5611  C  C     . LEU B 1 12  ? 147.320 122.130 172.184 1.00 51.29 ?  12  LEU B C     1 
ATOM   5612  O  O     . LEU B 1 12  ? 146.465 121.813 173.019 1.00 53.55 ?  12  LEU B O     1 
ATOM   5613  C  CB    . LEU B 1 12  ? 149.452 123.150 173.035 1.00 52.10 ?  12  LEU B CB    1 
ATOM   5614  C  CG    . LEU B 1 12  ? 150.698 122.907 173.888 1.00 52.39 ?  12  LEU B CG    1 
ATOM   5615  C  CD1   . LEU B 1 12  ? 151.490 124.192 174.070 1.00 52.91 ?  12  LEU B CD1   1 
ATOM   5616  C  CD2   . LEU B 1 12  ? 150.315 122.313 175.232 1.00 51.76 ?  12  LEU B CD2   1 
ATOM   5617  N  N     . ASN B 1 13  ? 147.000 122.689 171.015 1.00 51.33 ?  13  ASN B N     1 
ATOM   5618  C  CA    . ASN B 1 13  ? 145.603 122.903 170.650 1.00 49.42 ?  13  ASN B CA    1 
ATOM   5619  C  C     . ASN B 1 13  ? 144.891 121.583 170.384 1.00 52.08 ?  13  ASN B C     1 
ATOM   5620  O  O     . ASN B 1 13  ? 143.712 121.430 170.719 1.00 56.58 ?  13  ASN B O     1 
ATOM   5621  C  CB    . ASN B 1 13  ? 145.518 123.820 169.430 1.00 51.33 ?  13  ASN B CB    1 
ATOM   5622  C  CG    . ASN B 1 13  ? 144.098 124.017 168.949 1.00 50.05 ?  13  ASN B CG    1 
ATOM   5623  O  OD1   . ASN B 1 13  ? 143.703 123.486 167.913 1.00 50.41 ?  13  ASN B OD1   1 
ATOM   5624  N  ND2   . ASN B 1 13  ? 143.319 124.784 169.702 1.00 51.28 ?  13  ASN B ND2   1 
ATOM   5625  N  N     . ASN B 1 14  ? 145.583 120.619 169.773 1.00 53.76 ?  14  ASN B N     1 
ATOM   5626  C  CA    . ASN B 1 14  ? 144.988 119.305 169.565 1.00 52.32 ?  14  ASN B CA    1 
ATOM   5627  C  C     . ASN B 1 14  ? 144.845 118.529 170.866 1.00 53.34 ?  14  ASN B C     1 
ATOM   5628  O  O     . ASN B 1 14  ? 144.052 117.585 170.929 1.00 56.59 ?  14  ASN B O     1 
ATOM   5629  C  CB    . ASN B 1 14  ? 145.819 118.499 168.566 1.00 52.91 ?  14  ASN B CB    1 
ATOM   5630  C  CG    . ASN B 1 14  ? 145.755 119.069 167.166 1.00 55.92 ?  14  ASN B CG    1 
ATOM   5631  O  OD1   . ASN B 1 14  ? 144.983 119.987 166.895 1.00 58.01 ?  14  ASN B OD1   1 
ATOM   5632  N  ND2   . ASN B 1 14  ? 146.567 118.527 166.267 1.00 54.69 ?  14  ASN B ND2   1 
ATOM   5633  N  N     . GLU B 1 15  ? 145.597 118.907 171.901 1.00 56.23 ?  15  GLU B N     1 
ATOM   5634  C  CA    . GLU B 1 15  ? 145.472 118.267 173.205 1.00 56.56 ?  15  GLU B CA    1 
ATOM   5635  C  C     . GLU B 1 15  ? 144.139 118.552 173.885 1.00 57.08 ?  15  GLU B C     1 
ATOM   5636  O  O     . GLU B 1 15  ? 143.838 117.914 174.900 1.00 60.06 ?  15  GLU B O     1 
ATOM   5637  C  CB    . GLU B 1 15  ? 146.619 118.708 174.117 1.00 55.53 ?  15  GLU B CB    1 
ATOM   5638  C  CG    . GLU B 1 15  ? 147.782 117.731 174.163 1.00 57.49 ?  15  GLU B CG    1 
ATOM   5639  C  CD    . GLU B 1 15  ? 149.084 118.389 174.578 1.00 61.35 ?  15  GLU B CD    1 
ATOM   5640  O  OE1   . GLU B 1 15  ? 149.215 118.751 175.766 1.00 60.81 ?  15  GLU B OE1   1 
ATOM   5641  O  OE2   . GLU B 1 15  ? 149.976 118.542 173.717 1.00 60.08 -1 15  GLU B OE2   1 
ATOM   5642  N  N     . ILE B 1 16  ? 143.346 119.493 173.367 1.00 56.73 ?  16  ILE B N     1 
ATOM   5643  C  CA    . ILE B 1 16  ? 142.039 119.776 173.957 1.00 56.54 ?  16  ILE B CA    1 
ATOM   5644  C  C     . ILE B 1 16  ? 141.137 118.551 173.863 1.00 56.57 ?  16  ILE B C     1 
ATOM   5645  O  O     . ILE B 1 16  ? 140.479 118.164 174.835 1.00 54.26 ?  16  ILE B O     1 
ATOM   5646  C  CB    . ILE B 1 16  ? 141.390 120.993 173.273 1.00 55.92 ?  16  ILE B CB    1 
ATOM   5647  C  CG1   . ILE B 1 16  ? 142.247 122.243 173.452 1.00 55.42 ?  16  ILE B CG1   1 
ATOM   5648  C  CG2   . ILE B 1 16  ? 139.990 121.230 173.821 1.00 56.40 ?  16  ILE B CG2   1 
ATOM   5649  C  CD1   . ILE B 1 16  ? 141.889 123.344 172.486 1.00 54.74 ?  16  ILE B CD1   1 
ATOM   5650  N  N     . MET B 1 17  ? 141.098 117.922 172.688 1.00 56.33 ?  17  MET B N     1 
ATOM   5651  C  CA    . MET B 1 17  ? 140.194 116.802 172.462 1.00 56.69 ?  17  MET B CA    1 
ATOM   5652  C  C     . MET B 1 17  ? 140.646 115.526 173.155 1.00 57.42 ?  17  MET B C     1 
ATOM   5653  O  O     . MET B 1 17  ? 139.825 114.625 173.356 1.00 56.86 ?  17  MET B O     1 
ATOM   5654  C  CB    . MET B 1 17  ? 140.038 116.548 170.964 1.00 57.47 ?  17  MET B CB    1 
ATOM   5655  C  CG    . MET B 1 17  ? 139.664 117.788 170.182 1.00 57.59 ?  17  MET B CG    1 
ATOM   5656  S  SD    . MET B 1 17  ? 138.082 118.481 170.699 1.00 63.33 ?  17  MET B SD    1 
ATOM   5657  C  CE    . MET B 1 17  ? 136.983 117.777 169.475 1.00 55.92 ?  17  MET B CE    1 
ATOM   5658  N  N     . ILE B 1 18  ? 141.922 115.422 173.520 1.00 59.62 ?  18  ILE B N     1 
ATOM   5659  C  CA    . ILE B 1 18  ? 142.384 114.289 174.308 1.00 58.94 ?  18  ILE B CA    1 
ATOM   5660  C  C     . ILE B 1 18  ? 141.817 114.457 175.711 1.00 60.09 ?  18  ILE B C     1 
ATOM   5661  O  O     . ILE B 1 18  ? 142.290 115.291 176.491 1.00 59.84 ?  18  ILE B O     1 
ATOM   5662  C  CB    . ILE B 1 18  ? 143.919 114.186 174.321 1.00 60.01 ?  18  ILE B CB    1 
ATOM   5663  C  CG1   . ILE B 1 18  ? 144.432 113.784 172.937 1.00 60.22 ?  18  ILE B CG1   1 
ATOM   5664  C  CG2   . ILE B 1 18  ? 144.381 113.177 175.361 1.00 59.20 ?  18  ILE B CG2   1 
ATOM   5665  C  CD1   . ILE B 1 18  ? 145.532 114.674 172.408 1.00 60.47 ?  18  ILE B CD1   1 
ATOM   5666  N  N     . GLN B 1 19  ? 140.789 113.677 176.031 1.00 62.58 ?  19  GLN B N     1 
ATOM   5667  C  CA    . GLN B 1 19  ? 140.072 113.863 177.281 1.00 62.09 ?  19  GLN B CA    1 
ATOM   5668  C  C     . GLN B 1 19  ? 140.894 113.357 178.459 1.00 64.61 ?  19  GLN B C     1 
ATOM   5669  O  O     . GLN B 1 19  ? 141.558 112.321 178.379 1.00 66.56 ?  19  GLN B O     1 
ATOM   5670  C  CB    . GLN B 1 19  ? 138.725 113.143 177.232 1.00 64.69 ?  19  GLN B CB    1 
ATOM   5671  C  CG    . GLN B 1 19  ? 138.137 113.032 175.836 1.00 64.60 ?  19  GLN B CG    1 
ATOM   5672  C  CD    . GLN B 1 19  ? 136.635 113.239 175.816 1.00 64.39 ?  19  GLN B CD    1 
ATOM   5673  O  OE1   . GLN B 1 19  ? 135.935 112.883 176.763 1.00 64.88 ?  19  GLN B OE1   1 
ATOM   5674  N  NE2   . GLN B 1 19  ? 136.132 113.817 174.732 1.00 64.21 ?  19  GLN B NE2   1 
ATOM   5675  N  N     . LYS B 1 20  ? 140.846 114.105 179.558 1.00 67.86 ?  20  LYS B N     1 
ATOM   5676  C  CA    . LYS B 1 20  ? 141.474 113.716 180.815 1.00 69.26 ?  20  LYS B CA    1 
ATOM   5677  C  C     . LYS B 1 20  ? 140.381 113.599 181.865 1.00 69.23 ?  20  LYS B C     1 
ATOM   5678  O  O     . LYS B 1 20  ? 139.665 114.572 182.128 1.00 68.81 ?  20  LYS B O     1 
ATOM   5679  C  CB    . LYS B 1 20  ? 142.538 114.730 181.238 1.00 67.79 ?  20  LYS B CB    1 
ATOM   5680  C  CG    . LYS B 1 20  ? 142.826 114.750 182.730 1.00 68.45 ?  20  LYS B CG    1 
ATOM   5681  C  CD    . LYS B 1 20  ? 144.199 115.337 183.017 1.00 69.24 ?  20  LYS B CD    1 
ATOM   5682  C  CE    . LYS B 1 20  ? 144.096 116.789 183.451 1.00 69.19 ?  20  LYS B CE    1 
ATOM   5683  N  NZ    . LYS B 1 20  ? 145.420 117.470 183.435 1.00 68.51 1  20  LYS B NZ    1 
ATOM   5684  N  N     . ASP B 1 21  ? 140.253 112.410 182.456 1.00 71.38 ?  21  ASP B N     1 
ATOM   5685  C  CA    . ASP B 1 21  ? 139.191 112.111 183.420 1.00 71.25 ?  21  ASP B CA    1 
ATOM   5686  C  C     . ASP B 1 21  ? 137.811 112.362 182.816 1.00 72.08 ?  21  ASP B C     1 
ATOM   5687  O  O     . ASP B 1 21  ? 136.893 112.836 183.489 1.00 71.47 ?  21  ASP B O     1 
ATOM   5688  C  CB    . ASP B 1 21  ? 139.375 112.907 184.713 1.00 71.76 ?  21  ASP B CB    1 
ATOM   5689  C  CG    . ASP B 1 21  ? 140.812 112.908 185.197 1.00 73.48 ?  21  ASP B CG    1 
ATOM   5690  O  OD1   . ASP B 1 21  ? 141.466 111.846 185.128 1.00 72.23 ?  21  ASP B OD1   1 
ATOM   5691  O  OD2   . ASP B 1 21  ? 141.289 113.972 185.646 1.00 72.92 -1 21  ASP B OD2   1 
ATOM   5692  N  N     . GLY B 1 22  ? 137.662 112.041 181.532 1.00 68.63 ?  22  GLY B N     1 
ATOM   5693  C  CA    . GLY B 1 22  ? 136.390 112.175 180.854 1.00 66.05 ?  22  GLY B CA    1 
ATOM   5694  C  C     . GLY B 1 22  ? 135.988 113.585 180.487 1.00 67.44 ?  22  GLY B C     1 
ATOM   5695  O  O     . GLY B 1 22  ? 134.845 113.795 180.068 1.00 67.11 ?  22  GLY B O     1 
ATOM   5696  N  N     . LYS B 1 23  ? 136.886 114.557 180.626 1.00 66.70 ?  23  LYS B N     1 
ATOM   5697  C  CA    . LYS B 1 23  ? 136.583 115.952 180.347 1.00 63.82 ?  23  LYS B CA    1 
ATOM   5698  C  C     . LYS B 1 23  ? 137.576 116.514 179.339 1.00 63.01 ?  23  LYS B C     1 
ATOM   5699  O  O     . LYS B 1 23  ? 138.747 116.123 179.312 1.00 64.84 ?  23  LYS B O     1 
ATOM   5700  C  CB    . LYS B 1 23  ? 136.617 116.797 181.627 1.00 63.78 ?  23  LYS B CB    1 
ATOM   5701  C  CG    . LYS B 1 23  ? 135.992 116.122 182.834 1.00 65.44 ?  23  LYS B CG    1 
ATOM   5702  C  CD    . LYS B 1 23  ? 134.491 115.969 182.661 1.00 65.22 ?  23  LYS B CD    1 
ATOM   5703  C  CE    . LYS B 1 23  ? 133.778 117.288 182.897 1.00 64.91 ?  23  LYS B CE    1 
ATOM   5704  N  NZ    . LYS B 1 23  ? 134.457 118.093 183.948 1.00 63.67 1  23  LYS B NZ    1 
ATOM   5705  N  N     . PHE B 1 24  ? 137.094 117.436 178.509 1.00 59.23 ?  24  PHE B N     1 
ATOM   5706  C  CA    . PHE B 1 24  ? 137.956 118.095 177.539 1.00 57.17 ?  24  PHE B CA    1 
ATOM   5707  C  C     . PHE B 1 24  ? 138.982 118.970 178.247 1.00 56.29 ?  24  PHE B C     1 
ATOM   5708  O  O     . PHE B 1 24  ? 138.699 119.571 179.287 1.00 56.56 ?  24  PHE B O     1 
ATOM   5709  C  CB    . PHE B 1 24  ? 137.126 118.942 176.575 1.00 55.54 ?  24  PHE B CB    1 
ATOM   5710  C  CG    . PHE B 1 24  ? 136.426 118.145 175.510 1.00 55.27 ?  24  PHE B CG    1 
ATOM   5711  C  CD1   . PHE B 1 24  ? 137.120 117.675 174.409 1.00 57.16 ?  24  PHE B CD1   1 
ATOM   5712  C  CD2   . PHE B 1 24  ? 135.071 117.879 175.606 1.00 55.44 ?  24  PHE B CD2   1 
ATOM   5713  C  CE1   . PHE B 1 24  ? 136.477 116.945 173.428 1.00 56.09 ?  24  PHE B CE1   1 
ATOM   5714  C  CE2   . PHE B 1 24  ? 134.424 117.150 174.627 1.00 56.44 ?  24  PHE B CE2   1 
ATOM   5715  C  CZ    . PHE B 1 24  ? 135.128 116.684 173.537 1.00 55.50 ?  24  PHE B CZ    1 
ATOM   5716  N  N     . GLN B 1 25  ? 140.185 119.039 177.675 1.00 57.29 ?  25  GLN B N     1 
ATOM   5717  C  CA    . GLN B 1 25  ? 141.264 119.854 178.234 1.00 57.15 ?  25  GLN B CA    1 
ATOM   5718  C  C     . GLN B 1 25  ? 141.218 121.233 177.581 1.00 57.88 ?  25  GLN B C     1 
ATOM   5719  O  O     . GLN B 1 25  ? 142.025 121.580 176.716 1.00 59.45 ?  25  GLN B O     1 
ATOM   5720  C  CB    . GLN B 1 25  ? 142.612 119.173 178.030 1.00 57.43 ?  25  GLN B CB    1 
ATOM   5721  C  CG    . GLN B 1 25  ? 142.697 117.779 178.624 1.00 57.27 ?  25  GLN B CG    1 
ATOM   5722  C  CD    . GLN B 1 25  ? 144.055 117.142 178.416 1.00 58.27 ?  25  GLN B CD    1 
ATOM   5723  O  OE1   . GLN B 1 25  ? 144.920 117.200 179.290 1.00 58.75 ?  25  GLN B OE1   1 
ATOM   5724  N  NE2   . GLN B 1 25  ? 144.251 116.530 177.254 1.00 58.57 ?  25  GLN B NE2   1 
ATOM   5725  N  N     . PHE B 1 26  ? 140.242 122.033 178.016 1.00 51.55 ?  26  PHE B N     1 
ATOM   5726  C  CA    . PHE B 1 26  ? 140.077 123.372 177.459 1.00 52.93 ?  26  PHE B CA    1 
ATOM   5727  C  C     . PHE B 1 26  ? 141.258 124.270 177.813 1.00 53.51 ?  26  PHE B C     1 
ATOM   5728  O  O     . PHE B 1 26  ? 141.686 125.091 176.992 1.00 52.89 ?  26  PHE B O     1 
ATOM   5729  C  CB    . PHE B 1 26  ? 138.768 123.985 177.952 1.00 50.12 ?  26  PHE B CB    1 
ATOM   5730  C  CG    . PHE B 1 26  ? 137.542 123.259 177.478 1.00 51.96 ?  26  PHE B CG    1 
ATOM   5731  C  CD1   . PHE B 1 26  ? 137.312 123.072 176.126 1.00 51.08 ?  26  PHE B CD1   1 
ATOM   5732  C  CD2   . PHE B 1 26  ? 136.620 122.764 178.384 1.00 50.64 ?  26  PHE B CD2   1 
ATOM   5733  C  CE1   . PHE B 1 26  ? 136.186 122.404 175.685 1.00 49.46 ?  26  PHE B CE1   1 
ATOM   5734  C  CE2   . PHE B 1 26  ? 135.493 122.094 177.949 1.00 49.81 ?  26  PHE B CE2   1 
ATOM   5735  C  CZ    . PHE B 1 26  ? 135.275 121.916 176.599 1.00 49.40 ?  26  PHE B CZ    1 
ATOM   5736  N  N     . ASP B 1 27  ? 141.796 124.127 179.028 1.00 57.05 ?  27  ASP B N     1 
ATOM   5737  C  CA    . ASP B 1 27  ? 142.904 124.974 179.457 1.00 54.92 ?  27  ASP B CA    1 
ATOM   5738  C  C     . ASP B 1 27  ? 144.123 124.811 178.559 1.00 55.84 ?  27  ASP B C     1 
ATOM   5739  O  O     . ASP B 1 27  ? 144.903 125.759 178.397 1.00 55.38 ?  27  ASP B O     1 
ATOM   5740  C  CB    . ASP B 1 27  ? 143.269 124.661 180.909 1.00 55.14 ?  27  ASP B CB    1 
ATOM   5741  C  CG    . ASP B 1 27  ? 143.111 123.191 181.245 1.00 59.58 ?  27  ASP B CG    1 
ATOM   5742  O  OD1   . ASP B 1 27  ? 143.518 122.344 180.423 1.00 58.90 ?  27  ASP B OD1   1 
ATOM   5743  O  OD2   . ASP B 1 27  ? 142.578 122.883 182.332 1.00 60.21 -1 27  ASP B OD2   1 
ATOM   5744  N  N     . LYS B 1 28  ? 144.296 123.629 177.960 1.00 55.09 ?  28  LYS B N     1 
ATOM   5745  C  CA    . LYS B 1 28  ? 145.397 123.423 177.023 1.00 55.69 ?  28  LYS B CA    1 
ATOM   5746  C  C     . LYS B 1 28  ? 145.374 124.469 175.917 1.00 55.91 ?  28  LYS B C     1 
ATOM   5747  O  O     . LYS B 1 28  ? 146.432 124.931 175.468 1.00 58.39 ?  28  LYS B O     1 
ATOM   5748  C  CB    . LYS B 1 28  ? 145.327 122.017 176.430 1.00 56.35 ?  28  LYS B CB    1 
ATOM   5749  C  CG    . LYS B 1 28  ? 145.831 120.919 177.352 1.00 56.47 ?  28  LYS B CG    1 
ATOM   5750  C  CD    . LYS B 1 28  ? 147.337 120.987 177.522 1.00 56.20 ?  28  LYS B CD    1 
ATOM   5751  C  CE    . LYS B 1 28  ? 147.823 119.970 178.540 1.00 56.98 ?  28  LYS B CE    1 
ATOM   5752  N  NZ    . LYS B 1 28  ? 148.635 120.602 179.616 1.00 55.47 1  28  LYS B NZ    1 
ATOM   5753  N  N     . ASP B 1 29  ? 144.174 124.872 175.488 1.00 54.35 ?  29  ASP B N     1 
ATOM   5754  C  CA    . ASP B 1 29  ? 144.044 125.915 174.476 1.00 52.22 ?  29  ASP B CA    1 
ATOM   5755  C  C     . ASP B 1 29  ? 144.845 127.149 174.861 1.00 52.26 ?  29  ASP B C     1 
ATOM   5756  O  O     . ASP B 1 29  ? 145.615 127.679 174.053 1.00 52.34 ?  29  ASP B O     1 
ATOM   5757  C  CB    . ASP B 1 29  ? 142.571 126.276 174.284 1.00 52.42 ?  29  ASP B CB    1 
ATOM   5758  C  CG    . ASP B 1 29  ? 142.287 126.858 172.914 1.00 54.90 ?  29  ASP B CG    1 
ATOM   5759  O  OD1   . ASP B 1 29  ? 143.020 126.522 171.959 1.00 55.08 ?  29  ASP B OD1   1 
ATOM   5760  O  OD2   . ASP B 1 29  ? 141.330 127.649 172.792 1.00 52.90 -1 29  ASP B OD2   1 
ATOM   5761  N  N     . LYS B 1 30  ? 144.702 127.594 176.113 1.00 52.18 ?  30  LYS B N     1 
ATOM   5762  C  CA    . LYS B 1 30  ? 145.457 128.751 176.579 1.00 53.26 ?  30  LYS B CA    1 
ATOM   5763  C  C     . LYS B 1 30  ? 146.949 128.529 176.391 1.00 51.63 ?  30  LYS B C     1 
ATOM   5764  O  O     . LYS B 1 30  ? 147.655 129.384 175.837 1.00 55.03 ?  30  LYS B O     1 
ATOM   5765  C  CB    . LYS B 1 30  ? 145.131 129.033 178.047 1.00 52.12 ?  30  LYS B CB    1 
ATOM   5766  C  CG    . LYS B 1 30  ? 145.840 130.249 178.616 1.00 51.47 ?  30  LYS B CG    1 
ATOM   5767  C  CD    . LYS B 1 30  ? 145.426 130.507 180.055 1.00 53.30 ?  30  LYS B CD    1 
ATOM   5768  C  CE    . LYS B 1 30  ? 146.150 131.714 180.628 1.00 55.90 ?  30  LYS B CE    1 
ATOM   5769  N  NZ    . LYS B 1 30  ? 145.755 131.980 182.038 1.00 55.29 1  30  LYS B NZ    1 
ATOM   5770  N  N     . GLU B 1 31  ? 147.439 127.356 176.805 1.00 53.21 ?  31  GLU B N     1 
ATOM   5771  C  CA    . GLU B 1 31  ? 148.848 127.037 176.617 1.00 52.85 ?  31  GLU B CA    1 
ATOM   5772  C  C     . GLU B 1 31  ? 149.246 127.213 175.160 1.00 52.18 ?  31  GLU B C     1 
ATOM   5773  O  O     . GLU B 1 31  ? 150.281 127.822 174.859 1.00 54.46 ?  31  GLU B O     1 
ATOM   5774  C  CB    . GLU B 1 31  ? 149.129 125.609 177.085 1.00 52.70 ?  31  GLU B CB    1 
ATOM   5775  C  CG    . GLU B 1 31  ? 148.877 125.381 178.566 1.00 54.76 ?  31  GLU B CG    1 
ATOM   5776  C  CD    . GLU B 1 31  ? 148.905 123.912 178.940 1.00 57.88 ?  31  GLU B CD    1 
ATOM   5777  O  OE1   . GLU B 1 31  ? 149.713 123.164 178.354 1.00 59.45 ?  31  GLU B OE1   1 
ATOM   5778  O  OE2   . GLU B 1 31  ? 148.118 123.506 179.820 1.00 56.50 -1 31  GLU B OE2   1 
ATOM   5779  N  N     . ALA B 1 32  ? 148.396 126.742 174.244 1.00 43.56 ?  32  ALA B N     1 
ATOM   5780  C  CA    . ALA B 1 32  ? 148.686 126.864 172.822 1.00 44.58 ?  32  ALA B CA    1 
ATOM   5781  C  C     . ALA B 1 32  ? 148.976 128.310 172.450 1.00 48.74 ?  32  ALA B C     1 
ATOM   5782  O  O     . ALA B 1 32  ? 149.996 128.605 171.812 1.00 50.09 ?  32  ALA B O     1 
ATOM   5783  C  CB    . ALA B 1 32  ? 147.521 126.316 171.998 1.00 44.78 ?  32  ALA B CB    1 
ATOM   5784  N  N     . VAL B 1 33  ? 148.119 129.237 172.896 1.00 49.04 ?  33  VAL B N     1 
ATOM   5785  C  CA    . VAL B 1 33  ? 148.329 130.644 172.564 1.00 47.36 ?  33  VAL B CA    1 
ATOM   5786  C  C     . VAL B 1 33  ? 149.708 131.083 173.030 1.00 47.53 ?  33  VAL B C     1 
ATOM   5787  O  O     . VAL B 1 33  ? 150.473 131.691 172.271 1.00 49.67 ?  33  VAL B O     1 
ATOM   5788  C  CB    . VAL B 1 33  ? 147.224 131.528 173.168 1.00 45.21 ?  33  VAL B CB    1 
ATOM   5789  C  CG1   . VAL B 1 33  ? 146.837 132.625 172.190 1.00 45.04 ?  33  VAL B CG1   1 
ATOM   5790  C  CG2   . VAL B 1 33  ? 146.015 130.705 173.530 1.00 47.96 ?  33  VAL B CG2   1 
ATOM   5791  N  N     . HIS B 1 34  ? 150.063 130.728 174.269 1.00 44.02 ?  34  HIS B N     1 
ATOM   5792  C  CA    . HIS B 1 34  ? 151.389 131.062 174.770 1.00 45.18 ?  34  HIS B CA    1 
ATOM   5793  C  C     . HIS B 1 34  ? 152.459 130.542 173.824 1.00 45.96 ?  34  HIS B C     1 
ATOM   5794  O  O     . HIS B 1 34  ? 153.318 131.303 173.361 1.00 49.13 ?  34  HIS B O     1 
ATOM   5795  C  CB    . HIS B 1 34  ? 151.580 130.494 176.176 1.00 50.39 ?  34  HIS B CB    1 
ATOM   5796  C  CG    . HIS B 1 34  ? 152.555 131.264 177.008 1.00 49.36 ?  34  HIS B CG    1 
ATOM   5797  N  ND1   . HIS B 1 34  ? 153.840 130.826 177.248 1.00 48.47 ?  34  HIS B ND1   1 
ATOM   5798  C  CD2   . HIS B 1 34  ? 152.436 132.449 177.654 1.00 49.42 ?  34  HIS B CD2   1 
ATOM   5799  C  CE1   . HIS B 1 34  ? 154.469 131.705 178.007 1.00 50.02 ?  34  HIS B CE1   1 
ATOM   5800  N  NE2   . HIS B 1 34  ? 153.640 132.700 178.267 1.00 51.44 ?  34  HIS B NE2   1 
ATOM   5801  N  N     . SER B 1 35  ? 152.377 129.257 173.469 1.00 46.26 ?  35  SER B N     1 
ATOM   5802  C  CA    . SER B 1 35  ? 153.317 128.706 172.503 1.00 47.37 ?  35  SER B CA    1 
ATOM   5803  C  C     . SER B 1 35  ? 153.273 129.502 171.210 1.00 46.78 ?  35  SER B C     1 
ATOM   5804  O  O     . SER B 1 35  ? 154.309 129.969 170.718 1.00 50.48 ?  35  SER B O     1 
ATOM   5805  C  CB    . SER B 1 35  ? 153.005 127.231 172.247 1.00 48.20 ?  35  SER B CB    1 
ATOM   5806  O  OG    . SER B 1 35  ? 153.695 126.756 171.106 1.00 48.65 ?  35  SER B OG    1 
ATOM   5807  N  N     . TYR B 1 36  ? 152.062 129.745 170.696 1.00 47.40 ?  36  TYR B N     1 
ATOM   5808  C  CA    . TYR B 1 36  ? 151.916 130.451 169.430 1.00 45.60 ?  36  TYR B CA    1 
ATOM   5809  C  C     . TYR B 1 36  ? 152.570 131.821 169.484 1.00 46.42 ?  36  TYR B C     1 
ATOM   5810  O  O     . TYR B 1 36  ? 152.973 132.357 168.446 1.00 47.08 ?  36  TYR B O     1 
ATOM   5811  C  CB    . TYR B 1 36  ? 150.435 130.580 169.070 1.00 44.83 ?  36  TYR B CB    1 
ATOM   5812  C  CG    . TYR B 1 36  ? 150.179 131.188 167.712 1.00 45.26 ?  36  TYR B CG    1 
ATOM   5813  C  CD1   . TYR B 1 36  ? 150.674 130.595 166.558 1.00 44.63 ?  36  TYR B CD1   1 
ATOM   5814  C  CD2   . TYR B 1 36  ? 149.437 132.354 167.580 1.00 42.99 ?  36  TYR B CD2   1 
ATOM   5815  C  CE1   . TYR B 1 36  ? 150.438 131.145 165.314 1.00 43.22 ?  36  TYR B CE1   1 
ATOM   5816  C  CE2   . TYR B 1 36  ? 149.196 132.912 166.342 1.00 44.18 ?  36  TYR B CE2   1 
ATOM   5817  C  CZ    . TYR B 1 36  ? 149.700 132.303 165.212 1.00 44.46 ?  36  TYR B CZ    1 
ATOM   5818  O  OH    . TYR B 1 36  ? 149.463 132.857 163.974 1.00 43.59 ?  36  TYR B OH    1 
ATOM   5819  N  N     . PHE B 1 37  ? 152.701 132.393 170.678 1.00 49.89 ?  37  PHE B N     1 
ATOM   5820  C  CA    . PHE B 1 37  ? 153.373 133.676 170.804 1.00 49.17 ?  37  PHE B CA    1 
ATOM   5821  C  C     . PHE B 1 37  ? 154.847 133.524 171.148 1.00 51.17 ?  37  PHE B C     1 
ATOM   5822  O  O     . PHE B 1 37  ? 155.671 134.309 170.669 1.00 55.25 ?  37  PHE B O     1 
ATOM   5823  C  CB    . PHE B 1 37  ? 152.667 134.539 171.850 1.00 49.72 ?  37  PHE B CB    1 
ATOM   5824  C  CG    . PHE B 1 37  ? 151.479 135.278 171.311 1.00 50.79 ?  37  PHE B CG    1 
ATOM   5825  C  CD1   . PHE B 1 37  ? 151.639 136.488 170.660 1.00 51.43 ?  37  PHE B CD1   1 
ATOM   5826  C  CD2   . PHE B 1 37  ? 150.205 134.755 171.438 1.00 50.28 ?  37  PHE B CD2   1 
ATOM   5827  C  CE1   . PHE B 1 37  ? 150.550 137.167 170.156 1.00 50.45 ?  37  PHE B CE1   1 
ATOM   5828  C  CE2   . PHE B 1 37  ? 149.112 135.430 170.936 1.00 48.78 ?  37  PHE B CE2   1 
ATOM   5829  C  CZ    . PHE B 1 37  ? 149.286 136.636 170.292 1.00 48.83 ?  37  PHE B CZ    1 
ATOM   5830  N  N     . VAL B 1 38  ? 155.211 132.522 171.954 1.00 52.14 ?  38  VAL B N     1 
ATOM   5831  C  CA    . VAL B 1 38  ? 156.610 132.407 172.367 1.00 51.44 ?  38  VAL B CA    1 
ATOM   5832  C  C     . VAL B 1 38  ? 157.458 131.659 171.355 1.00 53.54 ?  38  VAL B C     1 
ATOM   5833  O  O     . VAL B 1 38  ? 158.681 131.587 171.522 1.00 56.53 ?  38  VAL B O     1 
ATOM   5834  C  CB    . VAL B 1 38  ? 156.756 131.722 173.739 1.00 50.73 ?  38  VAL B CB    1 
ATOM   5835  C  CG1   . VAL B 1 38  ? 155.934 132.455 174.791 1.00 50.91 ?  38  VAL B CG1   1 
ATOM   5836  C  CG2   . VAL B 1 38  ? 156.366 130.258 173.655 1.00 49.68 ?  38  VAL B CG2   1 
ATOM   5837  N  N     . ASP B 1 39  ? 156.849 131.106 170.310 1.00 50.18 ?  39  ASP B N     1 
ATOM   5838  C  CA    . ASP B 1 39  ? 157.581 130.377 169.289 1.00 51.31 ?  39  ASP B CA    1 
ATOM   5839  C  C     . ASP B 1 39  ? 157.384 130.914 167.880 1.00 53.35 ?  39  ASP B C     1 
ATOM   5840  O  O     . ASP B 1 39  ? 158.277 130.746 167.048 1.00 56.10 ?  39  ASP B O     1 
ATOM   5841  C  CB    . ASP B 1 39  ? 157.190 128.890 169.310 1.00 52.76 ?  39  ASP B CB    1 
ATOM   5842  C  CG    . ASP B 1 39  ? 157.284 128.282 170.694 1.00 54.28 ?  39  ASP B CG    1 
ATOM   5843  O  OD1   . ASP B 1 39  ? 158.206 128.656 171.447 1.00 54.59 ?  39  ASP B OD1   1 
ATOM   5844  O  OD2   . ASP B 1 39  ? 156.436 127.429 171.029 1.00 53.25 -1 39  ASP B OD2   1 
ATOM   5845  N  N     . TYR B 1 40  ? 156.248 131.547 167.584 1.00 53.18 ?  40  TYR B N     1 
ATOM   5846  C  CA    . TYR B 1 40  ? 155.985 132.043 166.236 1.00 53.04 ?  40  TYR B CA    1 
ATOM   5847  C  C     . TYR B 1 40  ? 155.814 133.555 166.183 1.00 55.10 ?  40  TYR B C     1 
ATOM   5848  O  O     . TYR B 1 40  ? 156.522 134.217 165.418 1.00 55.56 ?  40  TYR B O     1 
ATOM   5849  C  CB    . TYR B 1 40  ? 154.748 131.350 165.654 1.00 52.98 ?  40  TYR B CB    1 
ATOM   5850  C  CG    . TYR B 1 40  ? 154.614 131.510 164.156 1.00 52.53 ?  40  TYR B CG    1 
ATOM   5851  C  CD1   . TYR B 1 40  ? 155.366 130.732 163.287 1.00 53.26 ?  40  TYR B CD1   1 
ATOM   5852  C  CD2   . TYR B 1 40  ? 153.739 132.442 163.613 1.00 51.96 ?  40  TYR B CD2   1 
ATOM   5853  C  CE1   . TYR B 1 40  ? 155.249 130.874 161.918 1.00 55.40 ?  40  TYR B CE1   1 
ATOM   5854  C  CE2   . TYR B 1 40  ? 153.616 132.592 162.245 1.00 52.85 ?  40  TYR B CE2   1 
ATOM   5855  C  CZ    . TYR B 1 40  ? 154.373 131.805 161.403 1.00 56.50 ?  40  TYR B CZ    1 
ATOM   5856  O  OH    . TYR B 1 40  ? 154.254 131.950 160.039 1.00 57.66 ?  40  TYR B OH    1 
ATOM   5857  N  N     . ILE B 1 41  ? 154.901 134.127 166.969 1.00 55.05 ?  41  ILE B N     1 
ATOM   5858  C  CA    . ILE B 1 41  ? 154.535 135.529 166.776 1.00 53.28 ?  41  ILE B CA    1 
ATOM   5859  C  C     . ILE B 1 41  ? 155.672 136.450 167.199 1.00 52.04 ?  41  ILE B C     1 
ATOM   5860  O  O     . ILE B 1 41  ? 156.027 137.390 166.477 1.00 54.19 ?  41  ILE B O     1 
ATOM   5861  C  CB    . ILE B 1 41  ? 153.232 135.856 167.526 1.00 50.85 ?  41  ILE B CB    1 
ATOM   5862  C  CG1   . ILE B 1 41  ? 152.082 135.001 166.994 1.00 48.55 ?  41  ILE B CG1   1 
ATOM   5863  C  CG2   . ILE B 1 41  ? 152.896 137.332 167.388 1.00 49.09 ?  41  ILE B CG2   1 
ATOM   5864  C  CD1   . ILE B 1 41  ? 151.939 135.039 165.491 1.00 49.11 ?  41  ILE B CD1   1 
ATOM   5865  N  N     . ASN B 1 42  ? 156.263 136.199 168.369 1.00 50.52 ?  42  ASN B N     1 
ATOM   5866  C  CA    . ASN B 1 42  ? 157.337 137.067 168.841 1.00 51.96 ?  42  ASN B CA    1 
ATOM   5867  C  C     . ASN B 1 42  ? 158.583 136.944 167.974 1.00 54.31 ?  42  ASN B C     1 
ATOM   5868  O  O     . ASN B 1 42  ? 159.325 137.919 167.816 1.00 54.08 ?  42  ASN B O     1 
ATOM   5869  C  CB    . ASN B 1 42  ? 157.668 136.756 170.299 1.00 53.11 ?  42  ASN B CB    1 
ATOM   5870  C  CG    . ASN B 1 42  ? 156.538 137.117 171.243 1.00 53.45 ?  42  ASN B CG    1 
ATOM   5871  O  OD1   . ASN B 1 42  ? 155.573 137.771 170.851 1.00 56.58 ?  42  ASN B OD1   1 
ATOM   5872  N  ND2   . ASN B 1 42  ? 156.654 136.690 172.495 1.00 53.35 ?  42  ASN B ND2   1 
ATOM   5873  N  N     . GLN B 1 43  ? 158.833 135.761 167.411 1.00 58.65 ?  43  GLN B N     1 
ATOM   5874  C  CA    . GLN B 1 43  ? 159.975 135.592 166.521 1.00 57.83 ?  43  GLN B CA    1 
ATOM   5875  C  C     . GLN B 1 43  ? 159.711 136.191 165.144 1.00 56.26 ?  43  GLN B C     1 
ATOM   5876  O  O     . GLN B 1 43  ? 160.623 136.746 164.523 1.00 58.13 ?  43  GLN B O     1 
ATOM   5877  C  CB    . GLN B 1 43  ? 160.333 134.111 166.401 1.00 58.46 ?  43  GLN B CB    1 
ATOM   5878  C  CG    . GLN B 1 43  ? 161.363 133.642 167.414 1.00 58.98 ?  43  GLN B CG    1 
ATOM   5879  C  CD    . GLN B 1 43  ? 160.747 133.279 168.749 1.00 60.06 ?  43  GLN B CD    1 
ATOM   5880  O  OE1   . GLN B 1 43  ? 160.314 132.146 168.958 1.00 59.73 ?  43  GLN B OE1   1 
ATOM   5881  N  NE2   . GLN B 1 43  ? 160.705 134.241 169.664 1.00 59.72 ?  43  GLN B NE2   1 
ATOM   5882  N  N     . ASN B 1 44  ? 158.478 136.091 164.654 1.00 56.45 ?  44  ASN B N     1 
ATOM   5883  C  CA    . ASN B 1 44  ? 158.127 136.600 163.336 1.00 56.94 ?  44  ASN B CA    1 
ATOM   5884  C  C     . ASN B 1 44  ? 157.730 138.070 163.350 1.00 55.64 ?  44  ASN B C     1 
ATOM   5885  O  O     . ASN B 1 44  ? 157.514 138.647 162.280 1.00 56.35 ?  44  ASN B O     1 
ATOM   5886  C  CB    . ASN B 1 44  ? 156.990 135.770 162.732 1.00 55.57 ?  44  ASN B CB    1 
ATOM   5887  C  CG    . ASN B 1 44  ? 157.496 134.611 161.898 1.00 56.91 ?  44  ASN B CG    1 
ATOM   5888  O  OD1   . ASN B 1 44  ? 158.449 133.930 162.276 1.00 58.79 ?  44  ASN B OD1   1 
ATOM   5889  N  ND2   . ASN B 1 44  ? 156.858 134.380 160.757 1.00 58.76 ?  44  ASN B ND2   1 
ATOM   5890  N  N     . THR B 1 45  ? 157.625 138.686 164.522 1.00 55.50 ?  45  THR B N     1 
ATOM   5891  C  CA    . THR B 1 45  ? 157.313 140.104 164.591 1.00 56.66 ?  45  THR B CA    1 
ATOM   5892  C  C     . THR B 1 45  ? 158.556 140.934 164.290 1.00 57.37 ?  45  THR B C     1 
ATOM   5893  O  O     . THR B 1 45  ? 159.691 140.494 164.496 1.00 60.83 ?  45  THR B O     1 
ATOM   5894  C  CB    . THR B 1 45  ? 156.742 140.473 165.965 1.00 56.50 ?  45  THR B CB    1 
ATOM   5895  O  OG1   . THR B 1 45  ? 156.252 141.818 165.936 1.00 56.05 ?  45  THR B OG1   1 
ATOM   5896  C  CG2   . THR B 1 45  ? 157.796 140.345 167.056 1.00 55.69 ?  45  THR B CG2   1 
ATOM   5897  N  N     . VAL B 1 46  ? 158.331 142.134 163.765 1.00 56.32 ?  46  VAL B N     1 
ATOM   5898  C  CA    . VAL B 1 46  ? 159.404 143.068 163.449 1.00 57.35 ?  46  VAL B CA    1 
ATOM   5899  C  C     . VAL B 1 46  ? 159.398 144.161 164.508 1.00 57.06 ?  46  VAL B C     1 
ATOM   5900  O  O     . VAL B 1 46  ? 158.431 144.924 164.622 1.00 58.31 ?  46  VAL B O     1 
ATOM   5901  C  CB    . VAL B 1 46  ? 159.239 143.660 162.040 1.00 56.58 ?  46  VAL B CB    1 
ATOM   5902  C  CG1   . VAL B 1 46  ? 160.135 144.873 161.867 1.00 55.16 ?  46  VAL B CG1   1 
ATOM   5903  C  CG2   . VAL B 1 46  ? 159.553 142.613 160.989 1.00 55.55 ?  46  VAL B CG2   1 
ATOM   5904  N  N     . PHE B 1 47  ? 160.472 144.235 165.285 1.00 58.54 ?  47  PHE B N     1 
ATOM   5905  C  CA    . PHE B 1 47  ? 160.588 145.212 166.355 1.00 60.28 ?  47  PHE B CA    1 
ATOM   5906  C  C     . PHE B 1 47  ? 161.515 146.348 165.942 1.00 60.60 ?  47  PHE B C     1 
ATOM   5907  O  O     . PHE B 1 47  ? 162.525 146.139 165.267 1.00 61.43 ?  47  PHE B O     1 
ATOM   5908  C  CB    . PHE B 1 47  ? 161.105 144.562 167.640 1.00 60.54 ?  47  PHE B CB    1 
ATOM   5909  C  CG    . PHE B 1 47  ? 160.805 145.353 168.881 1.00 60.62 ?  47  PHE B CG    1 
ATOM   5910  C  CD1   . PHE B 1 47  ? 159.500 145.670 169.218 1.00 59.97 ?  47  PHE B CD1   1 
ATOM   5911  C  CD2   . PHE B 1 47  ? 161.830 145.784 169.708 1.00 60.05 ?  47  PHE B CD2   1 
ATOM   5912  C  CE1   . PHE B 1 47  ? 159.221 146.398 170.359 1.00 60.86 ?  47  PHE B CE1   1 
ATOM   5913  C  CE2   . PHE B 1 47  ? 161.557 146.512 170.851 1.00 60.57 ?  47  PHE B CE2   1 
ATOM   5914  C  CZ    . PHE B 1 47  ? 160.252 146.821 171.176 1.00 61.43 ?  47  PHE B CZ    1 
ATOM   5915  N  N     . PHE B 1 48  ? 161.154 147.557 166.357 1.00 56.81 ?  48  PHE B N     1 
ATOM   5916  C  CA    . PHE B 1 48  ? 161.938 148.752 166.098 1.00 56.47 ?  48  PHE B CA    1 
ATOM   5917  C  C     . PHE B 1 48  ? 162.438 149.320 167.418 1.00 59.30 ?  48  PHE B C     1 
ATOM   5918  O  O     . PHE B 1 48  ? 161.998 148.916 168.498 1.00 59.94 ?  48  PHE B O     1 
ATOM   5919  C  CB    . PHE B 1 48  ? 161.120 149.808 165.341 1.00 56.72 ?  48  PHE B CB    1 
ATOM   5920  C  CG    . PHE B 1 48  ? 160.611 149.343 164.005 1.00 57.71 ?  48  PHE B CG    1 
ATOM   5921  C  CD1   . PHE B 1 48  ? 159.508 148.509 163.915 1.00 56.37 ?  48  PHE B CD1   1 
ATOM   5922  C  CD2   . PHE B 1 48  ? 161.234 149.746 162.836 1.00 57.45 ?  48  PHE B CD2   1 
ATOM   5923  C  CE1   . PHE B 1 48  ? 159.039 148.086 162.687 1.00 56.89 ?  48  PHE B CE1   1 
ATOM   5924  C  CE2   . PHE B 1 48  ? 160.770 149.324 161.606 1.00 56.57 ?  48  PHE B CE2   1 
ATOM   5925  C  CZ    . PHE B 1 48  ? 159.671 148.494 161.532 1.00 56.22 ?  48  PHE B CZ    1 
ATOM   5926  N  N     . HIS B 1 49  ? 163.378 150.264 167.321 1.00 62.05 ?  49  HIS B N     1 
ATOM   5927  C  CA    . HIS B 1 49  ? 163.936 150.868 168.527 1.00 62.83 ?  49  HIS B CA    1 
ATOM   5928  C  C     . HIS B 1 49  ? 162.863 151.604 169.321 1.00 63.07 ?  49  HIS B C     1 
ATOM   5929  O  O     . HIS B 1 49  ? 162.812 151.502 170.552 1.00 64.37 ?  49  HIS B O     1 
ATOM   5930  C  CB    . HIS B 1 49  ? 165.080 151.813 168.163 1.00 64.35 ?  49  HIS B CB    1 
ATOM   5931  C  CG    . HIS B 1 49  ? 165.779 152.396 169.351 1.00 65.21 ?  49  HIS B CG    1 
ATOM   5932  N  ND1   . HIS B 1 49  ? 166.294 151.618 170.366 1.00 63.91 ?  49  HIS B ND1   1 
ATOM   5933  C  CD2   . HIS B 1 49  ? 166.047 153.680 169.689 1.00 63.74 ?  49  HIS B CD2   1 
ATOM   5934  C  CE1   . HIS B 1 49  ? 166.850 152.398 171.277 1.00 63.98 ?  49  HIS B CE1   1 
ATOM   5935  N  NE2   . HIS B 1 49  ? 166.713 153.653 170.890 1.00 63.41 ?  49  HIS B NE2   1 
ATOM   5936  N  N     . ASN B 1 50  ? 161.998 152.346 168.635 1.00 61.05 ?  50  ASN B N     1 
ATOM   5937  C  CA    . ASN B 1 50  ? 160.853 152.983 169.267 1.00 62.50 ?  50  ASN B CA    1 
ATOM   5938  C  C     . ASN B 1 50  ? 159.731 153.083 168.242 1.00 60.99 ?  50  ASN B C     1 
ATOM   5939  O  O     . ASN B 1 50  ? 159.857 152.619 167.105 1.00 58.84 ?  50  ASN B O     1 
ATOM   5940  C  CB    . ASN B 1 50  ? 161.221 154.354 169.847 1.00 61.56 ?  50  ASN B CB    1 
ATOM   5941  C  CG    . ASN B 1 50  ? 161.910 155.249 168.840 1.00 62.99 ?  50  ASN B CG    1 
ATOM   5942  O  OD1   . ASN B 1 50  ? 162.148 154.852 167.702 1.00 62.27 ?  50  ASN B OD1   1 
ATOM   5943  N  ND2   . ASN B 1 50  ? 162.232 156.468 169.254 1.00 63.03 ?  50  ASN B ND2   1 
ATOM   5944  N  N     . LEU B 1 51  ? 158.620 153.694 168.658 1.00 55.35 ?  51  LEU B N     1 
ATOM   5945  C  CA    . LEU B 1 51  ? 157.459 153.798 167.781 1.00 54.03 ?  51  LEU B CA    1 
ATOM   5946  C  C     . LEU B 1 51  ? 157.728 154.708 166.589 1.00 56.24 ?  51  LEU B C     1 
ATOM   5947  O  O     . LEU B 1 51  ? 157.108 154.543 165.532 1.00 56.85 ?  51  LEU B O     1 
ATOM   5948  C  CB    . LEU B 1 51  ? 156.252 154.298 168.575 1.00 55.44 ?  51  LEU B CB    1 
ATOM   5949  C  CG    . LEU B 1 51  ? 154.904 154.321 167.855 1.00 53.80 ?  51  LEU B CG    1 
ATOM   5950  C  CD1   . LEU B 1 51  ? 154.484 152.916 167.454 1.00 51.80 ?  51  LEU B CD1   1 
ATOM   5951  C  CD2   . LEU B 1 51  ? 153.851 154.971 168.732 1.00 53.40 ?  51  LEU B CD2   1 
ATOM   5952  N  N     . LYS B 1 52  ? 158.639 155.673 166.739 1.00 56.71 ?  52  LYS B N     1 
ATOM   5953  C  CA    . LYS B 1 52  ? 158.926 156.598 165.645 1.00 55.26 ?  52  LYS B CA    1 
ATOM   5954  C  C     . LYS B 1 52  ? 159.489 155.863 164.436 1.00 56.32 ?  52  LYS B C     1 
ATOM   5955  O  O     . LYS B 1 52  ? 159.054 156.087 163.301 1.00 57.80 ?  52  LYS B O     1 
ATOM   5956  C  CB    . LYS B 1 52  ? 159.897 157.681 166.116 1.00 56.33 ?  52  LYS B CB    1 
ATOM   5957  C  CG    . LYS B 1 52  ? 159.376 159.099 165.946 1.00 57.26 ?  52  LYS B CG    1 
ATOM   5958  C  CD    . LYS B 1 52  ? 159.264 159.481 164.480 1.00 58.35 ?  52  LYS B CD    1 
ATOM   5959  C  CE    . LYS B 1 52  ? 158.452 160.754 164.306 1.00 58.29 ?  52  LYS B CE    1 
ATOM   5960  N  NZ    . LYS B 1 52  ? 158.202 161.062 162.870 1.00 58.58 1  52  LYS B NZ    1 
ATOM   5961  N  N     . GLU B 1 53  ? 160.461 154.974 164.663 1.00 59.10 ?  53  GLU B N     1 
ATOM   5962  C  CA    . GLU B 1 53  ? 161.042 154.220 163.557 1.00 59.32 ?  53  GLU B CA    1 
ATOM   5963  C  C     . GLU B 1 53  ? 160.011 153.305 162.913 1.00 57.39 ?  53  GLU B C     1 
ATOM   5964  O  O     . GLU B 1 53  ? 159.982 153.161 161.686 1.00 59.82 ?  53  GLU B O     1 
ATOM   5965  C  CB    . GLU B 1 53  ? 162.249 153.415 164.039 1.00 59.95 ?  53  GLU B CB    1 
ATOM   5966  C  CG    . GLU B 1 53  ? 163.246 154.221 164.848 1.00 60.72 ?  53  GLU B CG    1 
ATOM   5967  C  CD    . GLU B 1 53  ? 164.682 153.871 164.515 1.00 62.00 ?  53  GLU B CD    1 
ATOM   5968  O  OE1   . GLU B 1 53  ? 165.076 152.705 164.727 1.00 62.82 ?  53  GLU B OE1   1 
ATOM   5969  O  OE2   . GLU B 1 53  ? 165.416 154.763 164.039 1.00 61.66 -1 53  GLU B OE2   1 
ATOM   5970  N  N     . LYS B 1 54  ? 159.156 152.678 163.723 1.00 54.54 ?  54  LYS B N     1 
ATOM   5971  C  CA    . LYS B 1 54  ? 158.115 151.813 163.179 1.00 54.20 ?  54  LYS B CA    1 
ATOM   5972  C  C     . LYS B 1 54  ? 157.163 152.596 162.285 1.00 52.54 ?  54  LYS B C     1 
ATOM   5973  O  O     . LYS B 1 54  ? 156.853 152.174 161.164 1.00 52.90 ?  54  LYS B O     1 
ATOM   5974  C  CB    . LYS B 1 54  ? 157.349 151.141 164.317 1.00 53.29 ?  54  LYS B CB    1 
ATOM   5975  C  CG    . LYS B 1 54  ? 156.116 150.383 163.862 1.00 54.25 ?  54  LYS B CG    1 
ATOM   5976  C  CD    . LYS B 1 54  ? 155.714 149.336 164.878 1.00 53.22 ?  54  LYS B CD    1 
ATOM   5977  C  CE    . LYS B 1 54  ? 154.511 148.545 164.407 1.00 53.86 ?  54  LYS B CE    1 
ATOM   5978  N  NZ    . LYS B 1 54  ? 154.447 147.207 165.056 1.00 54.25 1  54  LYS B NZ    1 
ATOM   5979  N  N     . LEU B 1 55  ? 156.690 153.747 162.769 1.00 52.77 ?  55  LEU B N     1 
ATOM   5980  C  CA    . LEU B 1 55  ? 155.763 154.552 161.982 1.00 53.11 ?  55  LEU B CA    1 
ATOM   5981  C  C     . LEU B 1 55  ? 156.422 155.069 160.711 1.00 56.57 ?  55  LEU B C     1 
ATOM   5982  O  O     . LEU B 1 55  ? 155.801 155.066 159.642 1.00 60.90 ?  55  LEU B O     1 
ATOM   5983  C  CB    . LEU B 1 55  ? 155.228 155.710 162.822 1.00 55.67 ?  55  LEU B CB    1 
ATOM   5984  C  CG    . LEU B 1 55  ? 154.056 155.385 163.749 1.00 55.50 ?  55  LEU B CG    1 
ATOM   5985  C  CD1   . LEU B 1 55  ? 153.279 156.648 164.056 1.00 56.44 ?  55  LEU B CD1   1 
ATOM   5986  C  CD2   . LEU B 1 55  ? 153.147 154.329 163.137 1.00 54.78 ?  55  LEU B CD2   1 
ATOM   5987  N  N     . ASP B 1 56  ? 157.679 155.513 160.801 1.00 56.68 ?  56  ASP B N     1 
ATOM   5988  C  CA    . ASP B 1 56  ? 158.375 155.988 159.610 1.00 56.24 ?  56  ASP B CA    1 
ATOM   5989  C  C     . ASP B 1 56  ? 158.550 154.868 158.591 1.00 57.03 ?  56  ASP B C     1 
ATOM   5990  O  O     . ASP B 1 56  ? 158.318 155.068 157.394 1.00 57.75 ?  56  ASP B O     1 
ATOM   5991  C  CB    . ASP B 1 56  ? 159.728 156.582 159.996 1.00 59.58 ?  56  ASP B CB    1 
ATOM   5992  C  CG    . ASP B 1 56  ? 159.595 157.813 160.870 1.00 60.61 ?  56  ASP B CG    1 
ATOM   5993  O  OD1   . ASP B 1 56  ? 158.457 158.292 161.057 1.00 61.48 ?  56  ASP B OD1   1 
ATOM   5994  O  OD2   . ASP B 1 56  ? 160.629 158.303 161.371 1.00 59.36 -1 56  ASP B OD2   1 
ATOM   5995  N  N     . TYR B 1 57  ? 158.947 153.678 159.049 1.00 55.74 ?  57  TYR B N     1 
ATOM   5996  C  CA    . TYR B 1 57  ? 159.123 152.556 158.135 1.00 56.06 ?  57  TYR B CA    1 
ATOM   5997  C  C     . TYR B 1 57  ? 157.805 152.177 157.475 1.00 56.30 ?  57  TYR B C     1 
ATOM   5998  O  O     . TYR B 1 57  ? 157.767 151.878 156.276 1.00 60.11 ?  57  TYR B O     1 
ATOM   5999  C  CB    . TYR B 1 57  ? 159.718 151.360 158.881 1.00 55.53 ?  57  TYR B CB    1 
ATOM   6000  C  CG    . TYR B 1 57  ? 159.761 150.079 158.076 1.00 56.81 ?  57  TYR B CG    1 
ATOM   6001  C  CD1   . TYR B 1 57  ? 160.833 149.800 157.241 1.00 57.13 ?  57  TYR B CD1   1 
ATOM   6002  C  CD2   . TYR B 1 57  ? 158.735 149.145 158.160 1.00 59.01 ?  57  TYR B CD2   1 
ATOM   6003  C  CE1   . TYR B 1 57  ? 160.880 148.631 156.505 1.00 57.09 ?  57  TYR B CE1   1 
ATOM   6004  C  CE2   . TYR B 1 57  ? 158.774 147.976 157.426 1.00 59.36 ?  57  TYR B CE2   1 
ATOM   6005  C  CZ    . TYR B 1 57  ? 159.849 147.722 156.602 1.00 59.35 ?  57  TYR B CZ    1 
ATOM   6006  O  OH    . TYR B 1 57  ? 159.890 146.557 155.871 1.00 59.74 ?  57  TYR B OH    1 
ATOM   6007  N  N     . LEU B 1 58  ? 156.712 152.184 158.239 1.00 53.38 ?  58  LEU B N     1 
ATOM   6008  C  CA    . LEU B 1 58  ? 155.419 151.832 157.664 1.00 52.61 ?  58  LEU B CA    1 
ATOM   6009  C  C     . LEU B 1 58  ? 154.895 152.922 156.736 1.00 51.55 ?  58  LEU B C     1 
ATOM   6010  O  O     . LEU B 1 58  ? 154.105 152.634 155.831 1.00 53.00 ?  58  LEU B O     1 
ATOM   6011  C  CB    . LEU B 1 58  ? 154.415 151.541 158.778 1.00 52.55 ?  58  LEU B CB    1 
ATOM   6012  C  CG    . LEU B 1 58  ? 154.731 150.295 159.609 1.00 52.17 ?  58  LEU B CG    1 
ATOM   6013  C  CD1   . LEU B 1 58  ? 153.961 150.298 160.918 1.00 52.11 ?  58  LEU B CD1   1 
ATOM   6014  C  CD2   . LEU B 1 58  ? 154.439 149.032 158.817 1.00 53.03 ?  58  LEU B CD2   1 
ATOM   6015  N  N     . VAL B 1 59  ? 155.318 154.170 156.936 1.00 55.47 ?  59  VAL B N     1 
ATOM   6016  C  CA    . VAL B 1 59  ? 154.831 155.256 156.094 1.00 56.82 ?  59  VAL B CA    1 
ATOM   6017  C  C     . VAL B 1 59  ? 155.598 155.311 154.777 1.00 57.98 ?  59  VAL B C     1 
ATOM   6018  O  O     . VAL B 1 59  ? 154.997 155.367 153.697 1.00 56.51 ?  59  VAL B O     1 
ATOM   6019  C  CB    . VAL B 1 59  ? 154.906 156.594 156.852 1.00 56.13 ?  59  VAL B CB    1 
ATOM   6020  C  CG1   . VAL B 1 59  ? 154.978 157.761 155.880 1.00 55.82 ?  59  VAL B CG1   1 
ATOM   6021  C  CG2   . VAL B 1 59  ? 153.710 156.741 157.780 1.00 55.43 ?  59  VAL B CG2   1 
ATOM   6022  N  N     . GLU B 1 60  ? 156.934 155.292 154.838 1.00 59.74 ?  60  GLU B N     1 
ATOM   6023  C  CA    . GLU B 1 60  ? 157.718 155.408 153.610 1.00 59.69 ?  60  GLU B CA    1 
ATOM   6024  C  C     . GLU B 1 60  ? 157.613 154.162 152.740 1.00 59.71 ?  60  GLU B C     1 
ATOM   6025  O  O     . GLU B 1 60  ? 157.715 154.261 151.511 1.00 61.21 ?  60  GLU B O     1 
ATOM   6026  C  CB    . GLU B 1 60  ? 159.185 155.709 153.924 1.00 59.21 ?  60  GLU B CB    1 
ATOM   6027  C  CG    . GLU B 1 60  ? 159.408 156.708 155.044 1.00 60.66 ?  60  GLU B CG    1 
ATOM   6028  C  CD    . GLU B 1 60  ? 160.604 156.356 155.906 1.00 62.93 ?  60  GLU B CD    1 
ATOM   6029  O  OE1   . GLU B 1 60  ? 161.045 157.217 156.695 1.00 59.92 ?  60  GLU B OE1   1 
ATOM   6030  O  OE2   . GLU B 1 60  ? 161.104 155.216 155.796 1.00 61.95 -1 60  GLU B OE2   1 
ATOM   6031  N  N     . ASN B 1 61  ? 157.417 152.990 153.342 1.00 55.81 ?  61  ASN B N     1 
ATOM   6032  C  CA    . ASN B 1 61  ? 157.300 151.748 152.591 1.00 56.10 ?  61  ASN B CA    1 
ATOM   6033  C  C     . ASN B 1 61  ? 155.885 151.500 152.081 1.00 56.29 ?  61  ASN B C     1 
ATOM   6034  O  O     . ASN B 1 61  ? 155.561 150.367 151.707 1.00 58.43 ?  61  ASN B O     1 
ATOM   6035  C  CB    . ASN B 1 61  ? 157.770 150.568 153.441 1.00 56.83 ?  61  ASN B CB    1 
ATOM   6036  C  CG    . ASN B 1 61  ? 159.273 150.551 153.632 1.00 58.89 ?  61  ASN B CG    1 
ATOM   6037  O  OD1   . ASN B 1 61  ? 159.993 149.860 152.913 1.00 58.92 ?  61  ASN B OD1   1 
ATOM   6038  N  ND2   . ASN B 1 61  ? 159.754 151.322 154.600 1.00 58.89 ?  61  ASN B ND2   1 
ATOM   6039  N  N     . GLN B 1 62  ? 155.044 152.537 152.060 1.00 55.77 ?  62  GLN B N     1 
ATOM   6040  C  CA    . GLN B 1 62  ? 153.691 152.466 151.503 1.00 57.06 ?  62  GLN B CA    1 
ATOM   6041  C  C     . GLN B 1 62  ? 152.847 151.398 152.196 1.00 55.48 ?  62  GLN B C     1 
ATOM   6042  O  O     . GLN B 1 62  ? 152.032 150.720 151.567 1.00 56.00 ?  62  GLN B O     1 
ATOM   6043  C  CB    . GLN B 1 62  ? 153.728 152.235 149.990 1.00 54.59 ?  62  GLN B CB    1 
ATOM   6044  C  CG    . GLN B 1 62  ? 154.675 153.161 149.244 1.00 55.59 ?  62  GLN B CG    1 
ATOM   6045  C  CD    . GLN B 1 62  ? 154.512 154.614 149.647 1.00 58.59 ?  62  GLN B CD    1 
ATOM   6046  O  OE1   . GLN B 1 62  ? 153.502 155.247 149.337 1.00 58.31 ?  62  GLN B OE1   1 
ATOM   6047  N  NE2   . GLN B 1 62  ? 155.508 155.152 150.340 1.00 57.60 ?  62  GLN B NE2   1 
ATOM   6048  N  N     . TYR B 1 63  ? 153.043 151.244 153.504 1.00 52.92 ?  63  TYR B N     1 
ATOM   6049  C  CA    . TYR B 1 63  ? 152.163 150.406 154.308 1.00 52.23 ?  63  TYR B CA    1 
ATOM   6050  C  C     . TYR B 1 63  ? 151.016 151.208 154.908 1.00 52.08 ?  63  TYR B C     1 
ATOM   6051  O  O     . TYR B 1 63  ? 149.886 150.714 154.984 1.00 51.06 ?  63  TYR B O     1 
ATOM   6052  C  CB    . TYR B 1 63  ? 152.948 149.722 155.430 1.00 51.41 ?  63  TYR B CB    1 
ATOM   6053  C  CG    . TYR B 1 63  ? 153.860 148.612 154.968 1.00 53.74 ?  63  TYR B CG    1 
ATOM   6054  C  CD1   . TYR B 1 63  ? 153.346 147.468 154.376 1.00 51.61 ?  63  TYR B CD1   1 
ATOM   6055  C  CD2   . TYR B 1 63  ? 155.234 148.706 155.134 1.00 53.83 ?  63  TYR B CD2   1 
ATOM   6056  C  CE1   . TYR B 1 63  ? 154.178 146.449 153.956 1.00 54.06 ?  63  TYR B CE1   1 
ATOM   6057  C  CE2   . TYR B 1 63  ? 156.073 147.695 154.718 1.00 52.91 ?  63  TYR B CE2   1 
ATOM   6058  C  CZ    . TYR B 1 63  ? 155.542 146.569 154.129 1.00 55.02 ?  63  TYR B CZ    1 
ATOM   6059  O  OH    . TYR B 1 63  ? 156.379 145.561 153.713 1.00 55.71 ?  63  TYR B OH    1 
ATOM   6060  N  N     . TYR B 1 64  ? 151.290 152.438 155.330 1.00 49.23 ?  64  TYR B N     1 
ATOM   6061  C  CA    . TYR B 1 64  ? 150.311 153.297 155.974 1.00 46.99 ?  64  TYR B CA    1 
ATOM   6062  C  C     . TYR B 1 64  ? 150.090 154.556 155.150 1.00 48.94 ?  64  TYR B C     1 
ATOM   6063  O  O     . TYR B 1 64  ? 151.008 155.061 154.498 1.00 50.62 ?  64  TYR B O     1 
ATOM   6064  C  CB    . TYR B 1 64  ? 150.761 153.698 157.381 1.00 47.69 ?  64  TYR B CB    1 
ATOM   6065  C  CG    . TYR B 1 64  ? 150.577 152.631 158.429 1.00 47.26 ?  64  TYR B CG    1 
ATOM   6066  C  CD1   . TYR B 1 64  ? 149.960 151.425 158.124 1.00 47.65 ?  64  TYR B CD1   1 
ATOM   6067  C  CD2   . TYR B 1 64  ? 151.022 152.831 159.726 1.00 47.78 ?  64  TYR B CD2   1 
ATOM   6068  C  CE1   . TYR B 1 64  ? 149.793 150.450 159.085 1.00 45.62 ?  64  TYR B CE1   1 
ATOM   6069  C  CE2   . TYR B 1 64  ? 150.860 151.865 160.689 1.00 48.04 ?  64  TYR B CE2   1 
ATOM   6070  C  CZ    . TYR B 1 64  ? 150.247 150.676 160.366 1.00 47.45 ?  64  TYR B CZ    1 
ATOM   6071  O  OH    . TYR B 1 64  ? 150.089 149.716 161.334 1.00 49.14 ?  64  TYR B OH    1 
ATOM   6072  N  N     . GLU B 1 65  ? 148.860 155.057 155.183 1.00 51.99 ?  65  GLU B N     1 
ATOM   6073  C  CA    . GLU B 1 65  ? 148.588 156.388 154.661 1.00 51.96 ?  65  GLU B CA    1 
ATOM   6074  C  C     . GLU B 1 65  ? 149.121 157.429 155.637 1.00 54.39 ?  65  GLU B C     1 
ATOM   6075  O  O     . GLU B 1 65  ? 148.866 157.351 156.842 1.00 55.86 ?  65  GLU B O     1 
ATOM   6076  C  CB    . GLU B 1 65  ? 147.089 156.578 154.438 1.00 50.39 ?  65  GLU B CB    1 
ATOM   6077  C  CG    . GLU B 1 65  ? 146.462 155.536 153.528 1.00 51.97 ?  65  GLU B CG    1 
ATOM   6078  C  CD    . GLU B 1 65  ? 144.960 155.697 153.404 1.00 55.50 ?  65  GLU B CD    1 
ATOM   6079  O  OE1   . GLU B 1 65  ? 144.324 156.129 154.388 1.00 54.42 ?  65  GLU B OE1   1 
ATOM   6080  O  OE2   . GLU B 1 65  ? 144.415 155.392 152.322 1.00 54.21 -1 65  GLU B OE2   1 
ATOM   6081  N  N     . GLU B 1 66  ? 149.874 158.398 155.121 1.00 52.84 ?  66  GLU B N     1 
ATOM   6082  C  CA    . GLU B 1 66  ? 150.475 159.403 155.988 1.00 54.72 ?  66  GLU B CA    1 
ATOM   6083  C  C     . GLU B 1 66  ? 149.501 160.508 156.373 1.00 54.99 ?  66  GLU B C     1 
ATOM   6084  O  O     . GLU B 1 66  ? 149.772 161.246 157.328 1.00 54.13 ?  66  GLU B O     1 
ATOM   6085  C  CB    . GLU B 1 66  ? 151.708 160.009 155.314 1.00 55.88 ?  66  GLU B CB    1 
ATOM   6086  C  CG    . GLU B 1 66  ? 151.398 161.102 154.307 1.00 55.41 ?  66  GLU B CG    1 
ATOM   6087  C  CD    . GLU B 1 66  ? 152.619 161.925 153.951 1.00 56.78 ?  66  GLU B CD    1 
ATOM   6088  O  OE1   . GLU B 1 66  ? 153.719 161.342 153.850 1.00 55.65 ?  66  GLU B OE1   1 
ATOM   6089  O  OE2   . GLU B 1 66  ? 152.479 163.153 153.773 1.00 56.59 -1 66  GLU B OE2   1 
ATOM   6090  N  N     . GLU B 1 67  ? 148.375 160.629 155.670 1.00 53.83 ?  67  GLU B N     1 
ATOM   6091  C  CA    . GLU B 1 67  ? 147.450 161.728 155.931 1.00 53.55 ?  67  GLU B CA    1 
ATOM   6092  C  C     . GLU B 1 67  ? 146.789 161.588 157.297 1.00 55.20 ?  67  GLU B C     1 
ATOM   6093  O  O     . GLU B 1 67  ? 146.722 162.555 158.064 1.00 55.05 ?  67  GLU B O     1 
ATOM   6094  C  CB    . GLU B 1 67  ? 146.392 161.814 154.826 1.00 54.00 ?  67  GLU B CB    1 
ATOM   6095  C  CG    . GLU B 1 67  ? 146.924 161.853 153.391 1.00 55.13 ?  67  GLU B CG    1 
ATOM   6096  C  CD    . GLU B 1 67  ? 147.462 160.519 152.907 1.00 58.09 ?  67  GLU B CD    1 
ATOM   6097  O  OE1   . GLU B 1 67  ? 148.631 160.471 152.469 1.00 57.11 ?  67  GLU B OE1   1 
ATOM   6098  O  OE2   . GLU B 1 67  ? 146.715 159.520 152.961 1.00 56.98 -1 67  GLU B OE2   1 
ATOM   6099  N  N     . PHE B 1 68  ? 146.291 160.392 157.620 1.00 50.07 ?  68  PHE B N     1 
ATOM   6100  C  CA    . PHE B 1 68  ? 145.596 160.217 158.891 1.00 46.19 ?  68  PHE B CA    1 
ATOM   6101  C  C     . PHE B 1 68  ? 146.558 160.281 160.071 1.00 46.50 ?  68  PHE B C     1 
ATOM   6102  O  O     . PHE B 1 68  ? 146.171 160.725 161.158 1.00 50.04 ?  68  PHE B O     1 
ATOM   6103  C  CB    . PHE B 1 68  ? 144.808 158.904 158.891 1.00 47.47 ?  68  PHE B CB    1 
ATOM   6104  C  CG    . PHE B 1 68  ? 145.564 157.728 159.443 1.00 47.17 ?  68  PHE B CG    1 
ATOM   6105  C  CD1   . PHE B 1 68  ? 146.420 156.999 158.639 1.00 45.17 ?  68  PHE B CD1   1 
ATOM   6106  C  CD2   . PHE B 1 68  ? 145.392 157.334 160.759 1.00 43.14 ?  68  PHE B CD2   1 
ATOM   6107  C  CE1   . PHE B 1 68  ? 147.110 155.914 159.142 1.00 44.22 ?  68  PHE B CE1   1 
ATOM   6108  C  CE2   . PHE B 1 68  ? 146.078 156.250 161.268 1.00 42.72 ?  68  PHE B CE2   1 
ATOM   6109  C  CZ    . PHE B 1 68  ? 146.935 155.537 160.457 1.00 44.93 ?  68  PHE B CZ    1 
ATOM   6110  N  N     . LEU B 1 69  ? 147.805 159.848 159.881 1.00 49.73 ?  69  LEU B N     1 
ATOM   6111  C  CA    . LEU B 1 69  ? 148.808 159.973 160.930 1.00 47.63 ?  69  LEU B CA    1 
ATOM   6112  C  C     . LEU B 1 69  ? 149.336 161.393 161.069 1.00 48.62 ?  69  LEU B C     1 
ATOM   6113  O  O     . LEU B 1 69  ? 149.839 161.749 162.140 1.00 52.37 ?  69  LEU B O     1 
ATOM   6114  C  CB    . LEU B 1 69  ? 149.975 159.019 160.663 1.00 47.53 ?  69  LEU B CB    1 
ATOM   6115  C  CG    . LEU B 1 69  ? 149.757 157.551 161.031 1.00 47.12 ?  69  LEU B CG    1 
ATOM   6116  C  CD1   . LEU B 1 69  ? 150.899 156.690 160.514 1.00 48.48 ?  69  LEU B CD1   1 
ATOM   6117  C  CD2   . LEU B 1 69  ? 149.595 157.389 162.534 1.00 47.04 ?  69  LEU B CD2   1 
ATOM   6118  N  N     . SER B 1 70  ? 149.234 162.209 160.017 1.00 48.36 ?  70  SER B N     1 
ATOM   6119  C  CA    . SER B 1 70  ? 149.732 163.577 160.086 1.00 47.28 ?  70  SER B CA    1 
ATOM   6120  C  C     . SER B 1 70  ? 148.828 164.487 160.908 1.00 49.11 ?  70  SER B C     1 
ATOM   6121  O  O     . SER B 1 70  ? 149.256 165.582 161.288 1.00 51.02 ?  70  SER B O     1 
ATOM   6122  C  CB    . SER B 1 70  ? 149.897 164.148 158.677 1.00 49.35 ?  70  SER B CB    1 
ATOM   6123  O  OG    . SER B 1 70  ? 148.650 164.546 158.138 1.00 49.06 ?  70  SER B OG    1 
ATOM   6124  N  N     . LEU B 1 71  ? 147.595 164.066 161.189 1.00 46.46 ?  71  LEU B N     1 
ATOM   6125  C  CA    . LEU B 1 71  ? 146.689 164.868 161.999 1.00 45.72 ?  71  LEU B CA    1 
ATOM   6126  C  C     . LEU B 1 71  ? 147.046 164.853 163.478 1.00 45.67 ?  71  LEU B C     1 
ATOM   6127  O  O     . LEU B 1 71  ? 146.485 165.647 164.241 1.00 46.85 ?  71  LEU B O     1 
ATOM   6128  C  CB    . LEU B 1 71  ? 145.248 164.384 161.820 1.00 44.59 ?  71  LEU B CB    1 
ATOM   6129  C  CG    . LEU B 1 71  ? 144.704 164.367 160.393 1.00 47.01 ?  71  LEU B CG    1 
ATOM   6130  C  CD1   . LEU B 1 71  ? 143.815 163.156 160.177 1.00 49.18 ?  71  LEU B CD1   1 
ATOM   6131  C  CD2   . LEU B 1 71  ? 143.947 165.650 160.096 1.00 45.72 ?  71  LEU B CD2   1 
ATOM   6132  N  N     . TYR B 1 72  ? 147.955 163.979 163.898 1.00 43.56 ?  72  TYR B N     1 
ATOM   6133  C  CA    . TYR B 1 72  ? 148.393 163.889 165.282 1.00 44.85 ?  72  TYR B CA    1 
ATOM   6134  C  C     . TYR B 1 72  ? 149.884 164.174 165.367 1.00 46.70 ?  72  TYR B C     1 
ATOM   6135  O  O     . TYR B 1 72  ? 150.656 163.755 164.498 1.00 48.51 ?  72  TYR B O     1 
ATOM   6136  C  CB    . TYR B 1 72  ? 148.122 162.502 165.880 1.00 45.55 ?  72  TYR B CB    1 
ATOM   6137  C  CG    . TYR B 1 72  ? 146.741 161.944 165.633 1.00 42.98 ?  72  TYR B CG    1 
ATOM   6138  C  CD1   . TYR B 1 72  ? 146.434 161.299 164.441 1.00 42.35 ?  72  TYR B CD1   1 
ATOM   6139  C  CD2   . TYR B 1 72  ? 145.754 162.034 166.602 1.00 42.77 ?  72  TYR B CD2   1 
ATOM   6140  C  CE1   . TYR B 1 72  ? 145.178 160.779 164.217 1.00 40.87 ?  72  TYR B CE1   1 
ATOM   6141  C  CE2   . TYR B 1 72  ? 144.495 161.515 166.388 1.00 42.72 ?  72  TYR B CE2   1 
ATOM   6142  C  CZ    . TYR B 1 72  ? 144.213 160.890 165.193 1.00 42.62 ?  72  TYR B CZ    1 
ATOM   6143  O  OH    . TYR B 1 72  ? 142.960 160.372 164.970 1.00 45.08 ?  72  TYR B OH    1 
ATOM   6144  N  N     . SER B 1 73  ? 150.285 164.885 166.415 1.00 52.19 ?  73  SER B N     1 
ATOM   6145  C  CA    . SER B 1 73  ? 151.695 164.941 166.765 1.00 52.49 ?  73  SER B CA    1 
ATOM   6146  C  C     . SER B 1 73  ? 152.151 163.564 167.231 1.00 51.86 ?  73  SER B C     1 
ATOM   6147  O  O     . SER B 1 73  ? 151.354 162.755 167.711 1.00 54.01 ?  73  SER B O     1 
ATOM   6148  C  CB    . SER B 1 73  ? 151.940 165.982 167.856 1.00 51.38 ?  73  SER B CB    1 
ATOM   6149  O  OG    . SER B 1 73  ? 151.557 165.487 169.127 1.00 50.60 ?  73  SER B OG    1 
ATOM   6150  N  N     . PHE B 1 74  ? 153.449 163.291 167.071 1.00 54.68 ?  74  PHE B N     1 
ATOM   6151  C  CA    . PHE B 1 74  ? 153.948 161.964 167.417 1.00 53.82 ?  74  PHE B CA    1 
ATOM   6152  C  C     . PHE B 1 74  ? 153.760 161.656 168.897 1.00 54.02 ?  74  PHE B C     1 
ATOM   6153  O  O     . PHE B 1 74  ? 153.637 160.486 169.272 1.00 55.52 ?  74  PHE B O     1 
ATOM   6154  C  CB    . PHE B 1 74  ? 155.421 161.815 167.041 1.00 54.59 ?  74  PHE B CB    1 
ATOM   6155  C  CG    . PHE B 1 74  ? 156.024 160.524 167.513 1.00 55.45 ?  74  PHE B CG    1 
ATOM   6156  C  CD1   . PHE B 1 74  ? 155.650 159.323 166.936 1.00 53.33 ?  74  PHE B CD1   1 
ATOM   6157  C  CD2   . PHE B 1 74  ? 156.942 160.508 168.549 1.00 55.41 ?  74  PHE B CD2   1 
ATOM   6158  C  CE1   . PHE B 1 74  ? 156.188 158.130 167.373 1.00 55.48 ?  74  PHE B CE1   1 
ATOM   6159  C  CE2   . PHE B 1 74  ? 157.485 159.317 168.991 1.00 55.10 ?  74  PHE B CE2   1 
ATOM   6160  C  CZ    . PHE B 1 74  ? 157.108 158.127 168.403 1.00 55.55 ?  74  PHE B CZ    1 
ATOM   6161  N  N     . GLU B 1 75  ? 153.737 162.682 169.750 1.00 54.99 ?  75  GLU B N     1 
ATOM   6162  C  CA    . GLU B 1 75  ? 153.465 162.447 171.165 1.00 56.01 ?  75  GLU B CA    1 
ATOM   6163  C  C     . GLU B 1 75  ? 152.068 161.873 171.363 1.00 56.55 ?  75  GLU B C     1 
ATOM   6164  O  O     . GLU B 1 75  ? 151.871 160.960 172.172 1.00 57.06 ?  75  GLU B O     1 
ATOM   6165  C  CB    . GLU B 1 75  ? 153.633 163.745 171.956 1.00 56.12 ?  75  GLU B CB    1 
ATOM   6166  C  CG    . GLU B 1 75  ? 155.032 163.965 172.513 1.00 56.08 ?  75  GLU B CG    1 
ATOM   6167  C  CD    . GLU B 1 75  ? 156.123 163.594 171.528 1.00 59.46 ?  75  GLU B CD    1 
ATOM   6168  O  OE1   . GLU B 1 75  ? 156.303 164.326 170.532 1.00 59.31 ?  75  GLU B OE1   1 
ATOM   6169  O  OE2   . GLU B 1 75  ? 156.804 162.569 171.749 1.00 59.07 -1 75  GLU B OE2   1 
ATOM   6170  N  N     . ASP B 1 76  ? 151.086 162.389 170.621 1.00 52.52 ?  76  ASP B N     1 
ATOM   6171  C  CA    . ASP B 1 76  ? 149.723 161.879 170.727 1.00 51.01 ?  76  ASP B CA    1 
ATOM   6172  C  C     . ASP B 1 76  ? 149.624 160.442 170.226 1.00 49.96 ?  76  ASP B C     1 
ATOM   6173  O  O     . ASP B 1 76  ? 148.934 159.614 170.832 1.00 53.31 ?  76  ASP B O     1 
ATOM   6174  C  CB    . ASP B 1 76  ? 148.772 162.789 169.954 1.00 52.34 ?  76  ASP B CB    1 
ATOM   6175  C  CG    . ASP B 1 76  ? 148.575 164.128 170.633 1.00 54.36 ?  76  ASP B CG    1 
ATOM   6176  O  OD1   . ASP B 1 76  ? 149.037 164.285 171.783 1.00 53.96 ?  76  ASP B OD1   1 
ATOM   6177  O  OD2   . ASP B 1 76  ? 147.959 165.025 170.018 1.00 53.46 -1 76  ASP B OD2   1 
ATOM   6178  N  N     . ILE B 1 77  ? 150.302 160.127 169.121 1.00 47.36 ?  77  ILE B N     1 
ATOM   6179  C  CA    . ILE B 1 77  ? 150.298 158.758 168.610 1.00 47.58 ?  77  ILE B CA    1 
ATOM   6180  C  C     . ILE B 1 77  ? 150.967 157.818 169.602 1.00 48.60 ?  77  ILE B C     1 
ATOM   6181  O  O     . ILE B 1 77  ? 150.508 156.689 169.822 1.00 50.21 ?  77  ILE B O     1 
ATOM   6182  C  CB    . ILE B 1 77  ? 150.978 158.699 167.231 1.00 49.12 ?  77  ILE B CB    1 
ATOM   6183  C  CG1   . ILE B 1 77  ? 150.277 159.637 166.249 1.00 48.20 ?  77  ILE B CG1   1 
ATOM   6184  C  CG2   . ILE B 1 77  ? 150.972 157.278 166.701 1.00 46.74 ?  77  ILE B CG2   1 
ATOM   6185  C  CD1   . ILE B 1 77  ? 151.045 159.862 164.969 1.00 45.94 ?  77  ILE B CD1   1 
ATOM   6186  N  N     . LYS B 1 78  ? 152.072 158.261 170.204 1.00 50.55 ?  78  LYS B N     1 
ATOM   6187  C  CA    . LYS B 1 78  ? 152.736 157.465 171.228 1.00 50.70 ?  78  LYS B CA    1 
ATOM   6188  C  C     . LYS B 1 78  ? 151.816 157.228 172.416 1.00 49.63 ?  78  LYS B C     1 
ATOM   6189  O  O     . LYS B 1 78  ? 151.774 156.123 172.965 1.00 50.68 ?  78  LYS B O     1 
ATOM   6190  C  CB    . LYS B 1 78  ? 154.022 158.159 171.679 1.00 53.57 ?  78  LYS B CB    1 
ATOM   6191  C  CG    . LYS B 1 78  ? 155.064 157.228 172.271 1.00 52.73 ?  78  LYS B CG    1 
ATOM   6192  C  CD    . LYS B 1 78  ? 155.963 157.974 173.243 1.00 53.81 ?  78  LYS B CD    1 
ATOM   6193  C  CE    . LYS B 1 78  ? 157.254 157.220 173.501 1.00 54.50 ?  78  LYS B CE    1 
ATOM   6194  N  NZ    . LYS B 1 78  ? 158.435 157.938 172.948 1.00 52.68 1  78  LYS B NZ    1 
ATOM   6195  N  N     . GLU B 1 79  ? 151.072 158.256 172.827 1.00 51.71 ?  79  GLU B N     1 
ATOM   6196  C  CA    . GLU B 1 79  ? 150.134 158.101 173.934 1.00 51.17 ?  79  GLU B CA    1 
ATOM   6197  C  C     . GLU B 1 79  ? 149.024 157.116 173.583 1.00 49.54 ?  79  GLU B C     1 
ATOM   6198  O  O     . GLU B 1 79  ? 148.613 156.309 174.422 1.00 51.83 ?  79  GLU B O     1 
ATOM   6199  C  CB    . GLU B 1 79  ? 149.556 159.463 174.315 1.00 49.44 ?  79  GLU B CB    1 
ATOM   6200  C  CG    . GLU B 1 79  ? 150.206 160.081 175.543 1.00 52.62 ?  79  GLU B CG    1 
ATOM   6201  C  CD    . GLU B 1 79  ? 149.323 161.107 176.221 1.00 56.12 ?  79  GLU B CD    1 
ATOM   6202  O  OE1   . GLU B 1 79  ? 149.692 161.579 177.317 1.00 54.05 ?  79  GLU B OE1   1 
ATOM   6203  O  OE2   . GLU B 1 79  ? 148.267 161.455 175.654 1.00 56.75 -1 79  GLU B OE2   1 
ATOM   6204  N  N     . VAL B 1 80  ? 148.533 157.163 172.344 1.00 43.97 ?  80  VAL B N     1 
ATOM   6205  C  CA    . VAL B 1 80  ? 147.499 156.227 171.910 1.00 41.94 ?  80  VAL B CA    1 
ATOM   6206  C  C     . VAL B 1 80  ? 148.028 154.795 171.917 1.00 46.28 ?  80  VAL B C     1 
ATOM   6207  O  O     . VAL B 1 80  ? 147.356 153.869 172.392 1.00 48.04 ?  80  VAL B O     1 
ATOM   6208  C  CB    . VAL B 1 80  ? 146.972 156.635 170.522 1.00 43.34 ?  80  VAL B CB    1 
ATOM   6209  C  CG1   . VAL B 1 80  ? 146.170 155.509 169.896 1.00 44.32 ?  80  VAL B CG1   1 
ATOM   6210  C  CG2   . VAL B 1 80  ? 146.132 157.896 170.628 1.00 44.52 ?  80  VAL B CG2   1 
ATOM   6211  N  N     . PHE B 1 81  ? 149.240 154.589 171.396 1.00 46.65 ?  81  PHE B N     1 
ATOM   6212  C  CA    . PHE B 1 81  ? 149.824 153.251 171.387 1.00 43.06 ?  81  PHE B CA    1 
ATOM   6213  C  C     . PHE B 1 81  ? 150.090 152.753 172.805 1.00 45.86 ?  81  PHE B C     1 
ATOM   6214  O  O     . PHE B 1 81  ? 149.905 151.566 173.101 1.00 48.13 ?  81  PHE B O     1 
ATOM   6215  C  CB    . PHE B 1 81  ? 151.111 153.246 170.562 1.00 40.92 ?  81  PHE B CB    1 
ATOM   6216  C  CG    . PHE B 1 81  ? 150.896 152.944 169.106 1.00 40.82 ?  81  PHE B CG    1 
ATOM   6217  C  CD1   . PHE B 1 81  ? 150.492 153.939 168.232 1.00 41.95 ?  81  PHE B CD1   1 
ATOM   6218  C  CD2   . PHE B 1 81  ? 151.098 151.669 168.611 1.00 42.08 ?  81  PHE B CD2   1 
ATOM   6219  C  CE1   . PHE B 1 81  ? 150.295 153.666 166.891 1.00 43.36 ?  81  PHE B CE1   1 
ATOM   6220  C  CE2   . PHE B 1 81  ? 150.902 151.390 167.272 1.00 42.11 ?  81  PHE B CE2   1 
ATOM   6221  C  CZ    . PHE B 1 81  ? 150.500 152.391 166.412 1.00 41.06 ?  81  PHE B CZ    1 
ATOM   6222  N  N     . LYS B 1 82  ? 150.536 153.645 173.692 1.00 47.33 ?  82  LYS B N     1 
ATOM   6223  C  CA    . LYS B 1 82  ? 150.745 153.269 175.084 1.00 46.06 ?  82  LYS B CA    1 
ATOM   6224  C  C     . LYS B 1 82  ? 149.430 152.903 175.758 1.00 44.98 ?  82  LYS B C     1 
ATOM   6225  O  O     . LYS B 1 82  ? 149.381 151.976 176.570 1.00 46.57 ?  82  LYS B O     1 
ATOM   6226  C  CB    . LYS B 1 82  ? 151.438 154.404 175.838 1.00 46.55 ?  82  LYS B CB    1 
ATOM   6227  C  CG    . LYS B 1 82  ? 152.916 154.549 175.521 1.00 47.41 ?  82  LYS B CG    1 
ATOM   6228  C  CD    . LYS B 1 82  ? 153.775 153.948 176.619 1.00 47.76 ?  82  LYS B CD    1 
ATOM   6229  C  CE    . LYS B 1 82  ? 153.459 154.574 177.968 1.00 49.18 ?  82  LYS B CE    1 
ATOM   6230  N  NZ    . LYS B 1 82  ? 154.062 155.928 178.105 1.00 48.24 1  82  LYS B NZ    1 
ATOM   6231  N  N     . THR B 1 83  ? 148.354 153.623 175.435 1.00 42.72 ?  83  THR B N     1 
ATOM   6232  C  CA    . THR B 1 83  ? 147.041 153.260 175.957 1.00 41.20 ?  83  THR B CA    1 
ATOM   6233  C  C     . THR B 1 83  ? 146.619 151.886 175.457 1.00 42.79 ?  83  THR B C     1 
ATOM   6234  O  O     . THR B 1 83  ? 146.034 151.094 176.205 1.00 45.00 ?  83  THR B O     1 
ATOM   6235  C  CB    . THR B 1 83  ? 146.010 154.317 175.561 1.00 41.20 ?  83  THR B CB    1 
ATOM   6236  O  OG1   . THR B 1 83  ? 146.417 155.594 176.066 1.00 46.81 ?  83  THR B OG1   1 
ATOM   6237  C  CG2   . THR B 1 83  ? 144.643 153.972 176.130 1.00 44.21 ?  83  THR B CG2   1 
ATOM   6238  N  N     . ALA B 1 84  ? 146.908 151.586 174.189 1.00 41.52 ?  84  ALA B N     1 
ATOM   6239  C  CA    . ALA B 1 84  ? 146.579 150.270 173.648 1.00 38.00 ?  84  ALA B CA    1 
ATOM   6240  C  C     . ALA B 1 84  ? 147.359 149.165 174.349 1.00 38.28 ?  84  ALA B C     1 
ATOM   6241  O  O     . ALA B 1 84  ? 146.802 148.110 174.670 1.00 43.99 ?  84  ALA B O     1 
ATOM   6242  C  CB    . ALA B 1 84  ? 146.842 150.238 172.145 1.00 39.60 ?  84  ALA B CB    1 
ATOM   6243  N  N     . TYR B 1 85  ? 148.650 149.387 174.589 1.00 45.05 ?  85  TYR B N     1 
ATOM   6244  C  CA    . TYR B 1 85  ? 149.489 148.365 175.206 1.00 43.36 ?  85  TYR B CA    1 
ATOM   6245  C  C     . TYR B 1 85  ? 149.354 148.302 176.724 1.00 44.29 ?  85  TYR B C     1 
ATOM   6246  O  O     . TYR B 1 85  ? 149.814 147.326 177.325 1.00 46.49 ?  85  TYR B O     1 
ATOM   6247  C  CB    . TYR B 1 85  ? 150.954 148.592 174.830 1.00 40.26 ?  85  TYR B CB    1 
ATOM   6248  C  CG    . TYR B 1 85  ? 151.322 148.047 173.470 1.00 41.59 ?  85  TYR B CG    1 
ATOM   6249  C  CD1   . TYR B 1 85  ? 151.746 146.735 173.322 1.00 43.79 ?  85  TYR B CD1   1 
ATOM   6250  C  CD2   . TYR B 1 85  ? 151.237 148.841 172.334 1.00 43.92 ?  85  TYR B CD2   1 
ATOM   6251  C  CE1   . TYR B 1 85  ? 152.083 146.229 172.084 1.00 44.17 ?  85  TYR B CE1   1 
ATOM   6252  C  CE2   . TYR B 1 85  ? 151.571 148.343 171.092 1.00 43.73 ?  85  TYR B CE2   1 
ATOM   6253  C  CZ    . TYR B 1 85  ? 151.993 147.037 170.972 1.00 43.21 ?  85  TYR B CZ    1 
ATOM   6254  O  OH    . TYR B 1 85  ? 152.327 146.535 169.737 1.00 45.29 ?  85  TYR B OH    1 
ATOM   6255  N  N     . ALA B 1 86  ? 148.741 149.305 177.354 1.00 43.66 ?  86  ALA B N     1 
ATOM   6256  C  CA    . ALA B 1 86  ? 148.596 149.284 178.805 1.00 42.01 ?  86  ALA B CA    1 
ATOM   6257  C  C     . ALA B 1 86  ? 147.595 148.233 179.261 1.00 45.48 ?  86  ALA B C     1 
ATOM   6258  O  O     . ALA B 1 86  ? 147.671 147.763 180.401 1.00 47.31 ?  86  ALA B O     1 
ATOM   6259  C  CB    . ALA B 1 86  ? 148.177 150.664 179.310 1.00 42.20 ?  86  ALA B CB    1 
ATOM   6260  N  N     . LYS B 1 87  ? 146.653 147.855 178.395 1.00 44.46 ?  87  LYS B N     1 
ATOM   6261  C  CA    . LYS B 1 87  ? 145.671 146.845 178.765 1.00 45.39 ?  87  LYS B CA    1 
ATOM   6262  C  C     . LYS B 1 87  ? 146.287 145.460 178.909 1.00 44.55 ?  87  LYS B C     1 
ATOM   6263  O  O     . LYS B 1 87  ? 145.690 144.601 179.567 1.00 46.37 ?  87  LYS B O     1 
ATOM   6264  C  CB    . LYS B 1 87  ? 144.544 146.806 177.732 1.00 43.93 ?  87  LYS B CB    1 
ATOM   6265  C  CG    . LYS B 1 87  ? 143.187 146.441 178.309 1.00 43.92 ?  87  LYS B CG    1 
ATOM   6266  C  CD    . LYS B 1 87  ? 142.621 145.198 177.644 1.00 44.50 ?  87  LYS B CD    1 
ATOM   6267  C  CE    . LYS B 1 87  ? 141.492 144.600 178.469 1.00 42.38 ?  87  LYS B CE    1 
ATOM   6268  N  NZ    . LYS B 1 87  ? 140.805 143.490 177.753 1.00 40.62 1  87  LYS B NZ    1 
ATOM   6269  N  N     . LYS B 1 88  ? 147.466 145.234 178.326 1.00 44.68 ?  88  LYS B N     1 
ATOM   6270  C  CA    . LYS B 1 88  ? 148.112 143.923 178.323 1.00 44.57 ?  88  LYS B CA    1 
ATOM   6271  C  C     . LYS B 1 88  ? 147.160 142.852 177.800 1.00 42.41 ?  88  LYS B C     1 
ATOM   6272  O  O     . LYS B 1 88  ? 146.971 141.796 178.409 1.00 43.90 ?  88  LYS B O     1 
ATOM   6273  C  CB    . LYS B 1 88  ? 148.638 143.559 179.713 1.00 45.79 ?  88  LYS B CB    1 
ATOM   6274  C  CG    . LYS B 1 88  ? 150.028 144.092 180.023 1.00 46.36 ?  88  LYS B CG    1 
ATOM   6275  C  CD    . LYS B 1 88  ? 149.979 145.503 180.582 1.00 45.95 ?  88  LYS B CD    1 
ATOM   6276  C  CE    . LYS B 1 88  ? 151.253 146.267 180.258 1.00 46.97 ?  88  LYS B CE    1 
ATOM   6277  N  NZ    . LYS B 1 88  ? 151.084 147.737 180.422 1.00 47.47 1  88  LYS B NZ    1 
ATOM   6278  N  N     . PHE B 1 89  ? 146.541 143.142 176.657 1.00 42.94 ?  89  PHE B N     1 
ATOM   6279  C  CA    . PHE B 1 89  ? 145.551 142.235 176.093 1.00 39.07 ?  89  PHE B CA    1 
ATOM   6280  C  C     . PHE B 1 89  ? 146.188 140.899 175.740 1.00 43.73 ?  89  PHE B C     1 
ATOM   6281  O  O     . PHE B 1 89  ? 147.250 140.845 175.114 1.00 46.25 ?  89  PHE B O     1 
ATOM   6282  C  CB    . PHE B 1 89  ? 144.905 142.853 174.852 1.00 37.31 ?  89  PHE B CB    1 
ATOM   6283  C  CG    . PHE B 1 89  ? 143.970 141.922 174.133 1.00 38.71 ?  89  PHE B CG    1 
ATOM   6284  C  CD1   . PHE B 1 89  ? 142.650 141.806 174.528 1.00 37.31 ?  89  PHE B CD1   1 
ATOM   6285  C  CD2   . PHE B 1 89  ? 144.414 141.157 173.067 1.00 38.40 ?  89  PHE B CD2   1 
ATOM   6286  C  CE1   . PHE B 1 89  ? 141.790 140.948 173.874 1.00 37.73 ?  89  PHE B CE1   1 
ATOM   6287  C  CE2   . PHE B 1 89  ? 143.558 140.295 172.410 1.00 34.60 ?  89  PHE B CE2   1 
ATOM   6288  C  CZ    . PHE B 1 89  ? 142.245 140.193 172.813 1.00 36.67 ?  89  PHE B CZ    1 
ATOM   6289  N  N     . ARG B 1 90  ? 145.526 139.818 176.139 1.00 42.62 ?  90  ARG B N     1 
ATOM   6290  C  CA    . ARG B 1 90  ? 145.963 138.464 175.840 1.00 40.51 ?  90  ARG B CA    1 
ATOM   6291  C  C     . ARG B 1 90  ? 144.845 137.733 175.116 1.00 41.89 ?  90  ARG B C     1 
ATOM   6292  O  O     . ARG B 1 90  ? 143.683 137.800 175.532 1.00 42.84 ?  90  ARG B O     1 
ATOM   6293  C  CB    . ARG B 1 90  ? 146.348 137.714 177.118 1.00 45.34 ?  90  ARG B CB    1 
ATOM   6294  C  CG    . ARG B 1 90  ? 147.488 138.349 177.892 1.00 42.68 ?  90  ARG B CG    1 
ATOM   6295  C  CD    . ARG B 1 90  ? 148.801 138.230 177.139 1.00 45.15 ?  90  ARG B CD    1 
ATOM   6296  N  NE    . ARG B 1 90  ? 149.847 139.051 177.735 1.00 45.79 ?  90  ARG B NE    1 
ATOM   6297  C  CZ    . ARG B 1 90  ? 150.265 140.207 177.238 1.00 44.67 ?  90  ARG B CZ    1 
ATOM   6298  N  NH1   . ARG B 1 90  ? 149.752 140.707 176.126 1.00 46.68 1  90  ARG B NH1   1 
ATOM   6299  N  NH2   . ARG B 1 90  ? 151.222 140.877 177.872 1.00 44.05 ?  90  ARG B NH2   1 
ATOM   6300  N  N     . PHE B 1 91  ? 145.191 137.048 174.039 1.00 39.25 ?  91  PHE B N     1 
ATOM   6301  C  CA    . PHE B 1 91  ? 144.218 136.231 173.331 1.00 38.08 ?  91  PHE B CA    1 
ATOM   6302  C  C     . PHE B 1 91  ? 143.913 134.993 174.164 1.00 43.46 ?  91  PHE B C     1 
ATOM   6303  O  O     . PHE B 1 91  ? 144.831 134.218 174.462 1.00 45.50 ?  91  PHE B O     1 
ATOM   6304  C  CB    . PHE B 1 91  ? 144.751 135.838 171.959 1.00 38.01 ?  91  PHE B CB    1 
ATOM   6305  C  CG    . PHE B 1 91  ? 144.711 136.951 170.951 1.00 39.78 ?  91  PHE B CG    1 
ATOM   6306  C  CD1   . PHE B 1 91  ? 143.525 137.301 170.330 1.00 40.90 ?  91  PHE B CD1   1 
ATOM   6307  C  CD2   . PHE B 1 91  ? 145.862 137.649 170.627 1.00 39.02 ?  91  PHE B CD2   1 
ATOM   6308  C  CE1   . PHE B 1 91  ? 143.487 138.323 169.403 1.00 39.44 ?  91  PHE B CE1   1 
ATOM   6309  C  CE2   . PHE B 1 91  ? 145.830 138.672 169.701 1.00 39.13 ?  91  PHE B CE2   1 
ATOM   6310  C  CZ    . PHE B 1 91  ? 144.640 139.009 169.089 1.00 39.68 ?  91  PHE B CZ    1 
ATOM   6311  N  N     . PRO B 1 92  ? 142.658 134.763 174.561 1.00 42.41 ?  92  PRO B N     1 
ATOM   6312  C  CA    . PRO B 1 92  ? 142.366 133.615 175.430 1.00 42.17 ?  92  PRO B CA    1 
ATOM   6313  C  C     . PRO B 1 92  ? 142.377 132.281 174.709 1.00 42.72 ?  92  PRO B C     1 
ATOM   6314  O  O     . PRO B 1 92  ? 142.448 131.240 175.375 1.00 43.37 ?  92  PRO B O     1 
ATOM   6315  C  CB    . PRO B 1 92  ? 140.969 133.937 175.972 1.00 41.94 ?  92  PRO B CB    1 
ATOM   6316  C  CG    . PRO B 1 92  ? 140.338 134.731 174.883 1.00 41.93 ?  92  PRO B CG    1 
ATOM   6317  C  CD    . PRO B 1 92  ? 141.443 135.528 174.228 1.00 40.90 ?  92  PRO B CD    1 
ATOM   6318  N  N     . SER B 1 93  ? 142.311 132.277 173.381 1.00 42.05 ?  93  SER B N     1 
ATOM   6319  C  CA    . SER B 1 93  ? 142.310 131.053 172.599 1.00 39.78 ?  93  SER B CA    1 
ATOM   6320  C  C     . SER B 1 93  ? 143.341 131.164 171.488 1.00 40.03 ?  93  SER B C     1 
ATOM   6321  O  O     . SER B 1 93  ? 143.655 132.261 171.018 1.00 44.07 ?  93  SER B O     1 
ATOM   6322  C  CB    . SER B 1 93  ? 140.924 130.768 172.005 1.00 42.98 ?  93  SER B CB    1 
ATOM   6323  O  OG    . SER B 1 93  ? 140.739 131.461 170.784 1.00 44.75 ?  93  SER B OG    1 
ATOM   6324  N  N     . PHE B 1 94  ? 143.876 130.011 171.081 1.00 40.58 ?  94  PHE B N     1 
ATOM   6325  C  CA    . PHE B 1 94  ? 144.867 129.998 170.012 1.00 41.09 ?  94  PHE B CA    1 
ATOM   6326  C  C     . PHE B 1 94  ? 144.273 130.496 168.702 1.00 41.10 ?  94  PHE B C     1 
ATOM   6327  O  O     . PHE B 1 94  ? 144.932 131.220 167.948 1.00 43.52 ?  94  PHE B O     1 
ATOM   6328  C  CB    . PHE B 1 94  ? 145.437 128.589 169.838 1.00 42.58 ?  94  PHE B CB    1 
ATOM   6329  C  CG    . PHE B 1 94  ? 145.992 128.328 168.466 1.00 39.39 ?  94  PHE B CG    1 
ATOM   6330  C  CD1   . PHE B 1 94  ? 147.164 128.934 168.051 1.00 41.36 ?  94  PHE B CD1   1 
ATOM   6331  C  CD2   . PHE B 1 94  ? 145.336 127.480 167.589 1.00 41.92 ?  94  PHE B CD2   1 
ATOM   6332  C  CE1   . PHE B 1 94  ? 147.672 128.702 166.789 1.00 41.54 ?  94  PHE B CE1   1 
ATOM   6333  C  CE2   . PHE B 1 94  ? 145.841 127.242 166.326 1.00 44.46 ?  94  PHE B CE2   1 
ATOM   6334  C  CZ    . PHE B 1 94  ? 147.011 127.854 165.926 1.00 41.24 ?  94  PHE B CZ    1 
ATOM   6335  N  N     . MET B 1 95  ? 143.027 130.115 168.414 1.00 38.90 ?  95  MET B N     1 
ATOM   6336  C  CA    . MET B 1 95  ? 142.427 130.461 167.131 1.00 36.29 ?  95  MET B CA    1 
ATOM   6337  C  C     . MET B 1 95  ? 142.196 131.960 166.992 1.00 38.72 ?  95  MET B C     1 
ATOM   6338  O  O     . MET B 1 95  ? 142.274 132.486 165.881 1.00 44.00 ?  95  MET B O     1 
ATOM   6339  C  CB    . MET B 1 95  ? 141.118 129.696 166.938 1.00 39.90 ?  95  MET B CB    1 
ATOM   6340  C  CG    . MET B 1 95  ? 140.431 129.948 165.601 1.00 42.25 ?  95  MET B CG    1 
ATOM   6341  S  SD    . MET B 1 95  ? 141.068 129.000 164.200 1.00 51.03 ?  95  MET B SD    1 
ATOM   6342  C  CE    . MET B 1 95  ? 142.033 127.726 165.009 1.00 43.73 ?  95  MET B CE    1 
ATOM   6343  N  N     . SER B 1 96  ? 141.925 132.664 168.093 1.00 33.31 ?  96  SER B N     1 
ATOM   6344  C  CA    . SER B 1 96  ? 141.759 134.113 168.013 1.00 30.40 ?  96  SER B CA    1 
ATOM   6345  C  C     . SER B 1 96  ? 143.028 134.782 167.496 1.00 32.32 ?  96  SER B C     1 
ATOM   6346  O  O     . SER B 1 96  ? 142.997 135.544 166.518 1.00 34.21 ?  96  SER B O     1 
ATOM   6347  C  CB    . SER B 1 96  ? 141.384 134.665 169.388 1.00 33.47 ?  96  SER B CB    1 
ATOM   6348  O  OG    . SER B 1 96  ? 140.276 133.971 169.931 1.00 38.67 ?  96  SER B OG    1 
ATOM   6349  N  N     . ALA B 1 97  ? 144.161 134.486 168.135 1.00 37.86 ?  97  ALA B N     1 
ATOM   6350  C  CA    . ALA B 1 97  ? 145.432 135.057 167.710 1.00 34.01 ?  97  ALA B CA    1 
ATOM   6351  C  C     . ALA B 1 97  ? 145.811 134.580 166.317 1.00 35.07 ?  97  ALA B C     1 
ATOM   6352  O  O     . ALA B 1 97  ? 146.328 135.358 165.507 1.00 42.03 ?  97  ALA B O     1 
ATOM   6353  C  CB    . ALA B 1 97  ? 146.525 134.701 168.715 1.00 36.35 ?  97  ALA B CB    1 
ATOM   6354  N  N     . PHE B 1 98  ? 145.574 133.300 166.023 1.00 33.42 ?  98  PHE B N     1 
ATOM   6355  C  CA    . PHE B 1 98  ? 145.906 132.772 164.704 1.00 32.89 ?  98  PHE B CA    1 
ATOM   6356  C  C     . PHE B 1 98  ? 145.123 133.495 163.617 1.00 35.95 ?  98  PHE B C     1 
ATOM   6357  O  O     . PHE B 1 98  ? 145.686 133.901 162.594 1.00 43.40 ?  98  PHE B O     1 
ATOM   6358  C  CB    . PHE B 1 98  ? 145.631 131.269 164.661 1.00 37.17 ?  98  PHE B CB    1 
ATOM   6359  C  CG    . PHE B 1 98  ? 145.827 130.656 163.305 1.00 39.18 ?  98  PHE B CG    1 
ATOM   6360  C  CD1   . PHE B 1 98  ? 147.091 130.291 162.874 1.00 39.78 ?  98  PHE B CD1   1 
ATOM   6361  C  CD2   . PHE B 1 98  ? 144.750 130.446 162.461 1.00 41.11 ?  98  PHE B CD2   1 
ATOM   6362  C  CE1   . PHE B 1 98  ? 147.276 129.728 161.629 1.00 37.68 ?  98  PHE B CE1   1 
ATOM   6363  C  CE2   . PHE B 1 98  ? 144.930 129.884 161.212 1.00 43.04 ?  98  PHE B CE2   1 
ATOM   6364  C  CZ    . PHE B 1 98  ? 146.196 129.524 160.796 1.00 40.72 ?  98  PHE B CZ    1 
ATOM   6365  N  N     . LYS B 1 99  ? 143.820 133.681 163.831 1.00 39.14 ?  99  LYS B N     1 
ATOM   6366  C  CA    . LYS B 1 99  ? 142.987 134.355 162.845 1.00 37.77 ?  99  LYS B CA    1 
ATOM   6367  C  C     . LYS B 1 99  ? 143.399 135.808 162.678 1.00 35.59 ?  99  LYS B C     1 
ATOM   6368  O  O     . LYS B 1 99  ? 143.447 136.314 161.551 1.00 41.58 ?  99  LYS B O     1 
ATOM   6369  C  CB    . LYS B 1 99  ? 141.516 134.254 163.243 1.00 36.70 ?  99  LYS B CB    1 
ATOM   6370  C  CG    . LYS B 1 99  ? 140.865 132.935 162.866 1.00 39.01 ?  99  LYS B CG    1 
ATOM   6371  C  CD    . LYS B 1 99  ? 141.181 132.552 161.432 1.00 42.01 ?  99  LYS B CD    1 
ATOM   6372  C  CE    . LYS B 1 99  ? 140.042 131.769 160.806 1.00 40.21 ?  99  LYS B CE    1 
ATOM   6373  N  NZ    . LYS B 1 99  ? 139.823 132.159 159.387 1.00 42.41 1  99  LYS B NZ    1 
ATOM   6374  N  N     . PHE B 1 100 ? 143.710 136.499 163.780 1.00 32.10 ?  100 PHE B N     1 
ATOM   6375  C  CA    . PHE B 1 100 ? 144.153 137.882 163.645 1.00 35.03 ?  100 PHE B CA    1 
ATOM   6376  C  C     . PHE B 1 100 ? 145.459 137.972 162.866 1.00 35.92 ?  100 PHE B C     1 
ATOM   6377  O  O     . PHE B 1 100 ? 145.581 138.766 161.926 1.00 41.09 ?  100 PHE B O     1 
ATOM   6378  C  CB    . PHE B 1 100 ? 144.323 138.548 165.004 1.00 33.33 ?  100 PHE B CB    1 
ATOM   6379  C  CG    . PHE B 1 100 ? 144.958 139.901 164.906 1.00 35.46 ?  100 PHE B CG    1 
ATOM   6380  C  CD1   . PHE B 1 100 ? 144.263 140.963 164.354 1.00 34.60 ?  100 PHE B CD1   1 
ATOM   6381  C  CD2   . PHE B 1 100 ? 146.268 140.098 165.301 1.00 34.53 ?  100 PHE B CD2   1 
ATOM   6382  C  CE1   . PHE B 1 100 ? 144.848 142.205 164.235 1.00 34.60 ?  100 PHE B CE1   1 
ATOM   6383  C  CE2   . PHE B 1 100 ? 146.860 141.335 165.179 1.00 35.28 ?  100 PHE B CE2   1 
ATOM   6384  C  CZ    . PHE B 1 100 ? 146.148 142.392 164.646 1.00 34.72 ?  100 PHE B CZ    1 
ATOM   6385  N  N     . TYR B 1 101 ? 146.450 137.164 163.240 1.00 36.51 ?  101 TYR B N     1 
ATOM   6386  C  CA    . TYR B 1 101 ? 147.771 137.282 162.641 1.00 35.32 ?  101 TYR B CA    1 
ATOM   6387  C  C     . TYR B 1 101 ? 147.862 136.637 161.267 1.00 37.20 ?  101 TYR B C     1 
ATOM   6388  O  O     . TYR B 1 101 ? 148.878 136.814 160.586 1.00 45.47 ?  101 TYR B O     1 
ATOM   6389  C  CB    . TYR B 1 101 ? 148.824 136.689 163.579 1.00 38.28 ?  101 TYR B CB    1 
ATOM   6390  C  CG    . TYR B 1 101 ? 149.104 137.571 164.775 1.00 37.54 ?  101 TYR B CG    1 
ATOM   6391  C  CD1   . TYR B 1 101 ? 149.790 138.768 164.632 1.00 36.80 ?  101 TYR B CD1   1 
ATOM   6392  C  CD2   . TYR B 1 101 ? 148.666 137.217 166.043 1.00 36.97 ?  101 TYR B CD2   1 
ATOM   6393  C  CE1   . TYR B 1 101 ? 150.040 139.583 165.718 1.00 36.63 ?  101 TYR B CE1   1 
ATOM   6394  C  CE2   . TYR B 1 101 ? 148.911 138.025 167.135 1.00 38.05 ?  101 TYR B CE2   1 
ATOM   6395  C  CZ    . TYR B 1 101 ? 149.598 139.207 166.967 1.00 39.59 ?  101 TYR B CZ    1 
ATOM   6396  O  OH    . TYR B 1 101 ? 149.844 140.014 168.053 1.00 42.17 ?  101 TYR B OH    1 
ATOM   6397  N  N     . ASN B 1 102 ? 146.836 135.904 160.839 1.00 40.40 ?  102 ASN B N     1 
ATOM   6398  C  CA    . ASN B 1 102 ? 146.800 135.366 159.488 1.00 41.86 ?  102 ASN B CA    1 
ATOM   6399  C  C     . ASN B 1 102 ? 145.909 136.160 158.546 1.00 43.32 ?  102 ASN B C     1 
ATOM   6400  O  O     . ASN B 1 102 ? 146.178 136.193 157.342 1.00 47.54 ?  102 ASN B O     1 
ATOM   6401  C  CB    . ASN B 1 102 ? 146.329 133.909 159.513 1.00 40.01 ?  102 ASN B CB    1 
ATOM   6402  C  CG    . ASN B 1 102 ? 147.418 132.952 159.949 1.00 43.14 ?  102 ASN B CG    1 
ATOM   6403  O  OD1   . ASN B 1 102 ? 148.039 133.135 160.997 1.00 45.88 ?  102 ASN B OD1   1 
ATOM   6404  N  ND2   . ASN B 1 102 ? 147.659 131.922 159.146 1.00 43.81 ?  102 ASN B ND2   1 
ATOM   6405  N  N     . ASP B 1 103 ? 144.857 136.804 159.058 1.00 38.59 ?  103 ASP B N     1 
ATOM   6406  C  CA    . ASP B 1 103 ? 143.906 137.513 158.214 1.00 40.61 ?  103 ASP B CA    1 
ATOM   6407  C  C     . ASP B 1 103 ? 143.935 139.024 158.373 1.00 40.98 ?  103 ASP B C     1 
ATOM   6408  O  O     . ASP B 1 103 ? 143.580 139.731 157.427 1.00 46.47 ?  103 ASP B O     1 
ATOM   6409  C  CB    . ASP B 1 103 ? 142.476 137.027 158.493 1.00 42.23 ?  103 ASP B CB    1 
ATOM   6410  C  CG    . ASP B 1 103 ? 142.362 135.515 158.515 1.00 45.37 ?  103 ASP B CG    1 
ATOM   6411  O  OD1   . ASP B 1 103 ? 143.272 134.834 157.999 1.00 44.78 ?  103 ASP B OD1   1 
ATOM   6412  O  OD2   . ASP B 1 103 ? 141.354 135.008 159.049 1.00 47.06 -1 103 ASP B OD2   1 
ATOM   6413  N  N     . TYR B 1 104 ? 144.339 139.545 159.532 1.00 31.95 ?  104 TYR B N     1 
ATOM   6414  C  CA    . TYR B 1 104 ? 144.201 140.970 159.805 1.00 35.66 ?  104 TYR B CA    1 
ATOM   6415  C  C     . TYR B 1 104 ? 145.488 141.677 160.201 1.00 38.78 ?  104 TYR B C     1 
ATOM   6416  O  O     . TYR B 1 104 ? 145.580 142.892 159.989 1.00 43.88 ?  104 TYR B O     1 
ATOM   6417  C  CB    . TYR B 1 104 ? 143.150 141.207 160.900 1.00 37.44 ?  104 TYR B CB    1 
ATOM   6418  C  CG    . TYR B 1 104 ? 141.824 140.551 160.596 1.00 36.15 ?  104 TYR B CG    1 
ATOM   6419  C  CD1   . TYR B 1 104 ? 140.856 141.212 159.850 1.00 34.65 ?  104 TYR B CD1   1 
ATOM   6420  C  CD2   . TYR B 1 104 ? 141.537 139.273 161.055 1.00 33.99 ?  104 TYR B CD2   1 
ATOM   6421  C  CE1   . TYR B 1 104 ? 139.645 140.614 159.563 1.00 36.14 ?  104 TYR B CE1   1 
ATOM   6422  C  CE2   . TYR B 1 104 ? 140.327 138.668 160.775 1.00 37.33 ?  104 TYR B CE2   1 
ATOM   6423  C  CZ    . TYR B 1 104 ? 139.386 139.342 160.027 1.00 38.90 ?  104 TYR B CZ    1 
ATOM   6424  O  OH    . TYR B 1 104 ? 138.179 138.744 159.749 1.00 38.34 ?  104 TYR B OH    1 
ATOM   6425  N  N     . ALA B 1 105 ? 146.471 140.984 160.768 1.00 40.73 ?  105 ALA B N     1 
ATOM   6426  C  CA    . ALA B 1 105 ? 147.729 141.634 161.105 1.00 40.00 ?  105 ALA B CA    1 
ATOM   6427  C  C     . ALA B 1 105 ? 148.494 141.999 159.839 1.00 43.61 ?  105 ALA B C     1 
ATOM   6428  O  O     . ALA B 1 105 ? 148.561 141.217 158.887 1.00 40.70 ?  105 ALA B O     1 
ATOM   6429  C  CB    . ALA B 1 105 ? 148.581 140.731 161.990 1.00 37.04 ?  105 ALA B CB    1 
ATOM   6430  N  N     . LEU B 1 106 ? 149.069 143.198 159.832 1.00 46.91 ?  106 LEU B N     1 
ATOM   6431  C  CA    . LEU B 1 106 ? 149.818 143.657 158.672 1.00 44.23 ?  106 LEU B CA    1 
ATOM   6432  C  C     . LEU B 1 106 ? 151.151 142.927 158.582 1.00 47.83 ?  106 LEU B C     1 
ATOM   6433  O  O     . LEU B 1 106 ? 151.899 142.849 159.560 1.00 46.99 ?  106 LEU B O     1 
ATOM   6434  C  CB    . LEU B 1 106 ? 150.044 145.166 158.747 1.00 46.87 ?  106 LEU B CB    1 
ATOM   6435  C  CG    . LEU B 1 106 ? 150.889 145.785 157.634 1.00 45.27 ?  106 LEU B CG    1 
ATOM   6436  C  CD1   . LEU B 1 106 ? 150.130 145.778 156.319 1.00 45.59 ?  106 LEU B CD1   1 
ATOM   6437  C  CD2   . LEU B 1 106 ? 151.309 147.198 158.006 1.00 46.37 ?  106 LEU B CD2   1 
ATOM   6438  N  N     . LYS B 1 107 ? 151.443 142.389 157.402 1.00 53.13 ?  107 LYS B N     1 
ATOM   6439  C  CA    . LYS B 1 107 ? 152.689 141.694 157.129 1.00 52.70 ?  107 LYS B CA    1 
ATOM   6440  C  C     . LYS B 1 107 ? 153.486 142.468 156.088 1.00 55.30 ?  107 LYS B C     1 
ATOM   6441  O  O     . LYS B 1 107 ? 153.010 143.443 155.501 1.00 56.79 ?  107 LYS B O     1 
ATOM   6442  C  CB    . LYS B 1 107 ? 152.432 140.261 156.648 1.00 52.84 ?  107 LYS B CB    1 
ATOM   6443  C  CG    . LYS B 1 107 ? 151.849 139.341 157.707 1.00 51.33 ?  107 LYS B CG    1 
ATOM   6444  C  CD    . LYS B 1 107 ? 151.542 137.970 157.128 1.00 54.71 ?  107 LYS B CD    1 
ATOM   6445  C  CE    . LYS B 1 107 ? 150.994 137.032 158.188 1.00 55.56 ?  107 LYS B CE    1 
ATOM   6446  N  NZ    . LYS B 1 107 ? 150.448 135.778 157.595 1.00 52.71 1  107 LYS B NZ    1 
ATOM   6447  N  N     . THR B 1 108 ? 154.717 142.018 155.862 1.00 59.23 ?  108 THR B N     1 
ATOM   6448  C  CA    . THR B 1 108 ? 155.584 142.653 154.883 1.00 59.39 ?  108 THR B CA    1 
ATOM   6449  C  C     . THR B 1 108 ? 155.089 142.355 153.468 1.00 61.88 ?  108 THR B C     1 
ATOM   6450  O  O     . THR B 1 108 ? 154.106 141.639 153.258 1.00 61.58 ?  108 THR B O     1 
ATOM   6451  C  CB    . THR B 1 108 ? 157.026 142.185 155.068 1.00 60.99 ?  108 THR B CB    1 
ATOM   6452  O  OG1   . THR B 1 108 ? 157.044 140.772 155.309 1.00 65.24 ?  108 THR B OG1   1 
ATOM   6453  C  CG2   . THR B 1 108 ? 157.668 142.899 156.248 1.00 58.11 ?  108 THR B CG2   1 
ATOM   6454  N  N     . ASN B 1 109 ? 155.783 142.925 152.480 1.00 63.97 ?  109 ASN B N     1 
ATOM   6455  C  CA    . ASN B 1 109 ? 155.405 142.707 151.087 1.00 61.95 ?  109 ASN B CA    1 
ATOM   6456  C  C     . ASN B 1 109 ? 155.513 141.236 150.708 1.00 64.82 ?  109 ASN B C     1 
ATOM   6457  O  O     . ASN B 1 109 ? 154.649 140.702 150.003 1.00 64.81 ?  109 ASN B O     1 
ATOM   6458  C  CB    . ASN B 1 109 ? 156.274 143.563 150.166 1.00 63.18 ?  109 ASN B CB    1 
ATOM   6459  C  CG    . ASN B 1 109 ? 156.147 145.043 150.457 1.00 63.25 ?  109 ASN B CG    1 
ATOM   6460  O  OD1   . ASN B 1 109 ? 155.276 145.465 151.216 1.00 61.63 ?  109 ASN B OD1   1 
ATOM   6461  N  ND2   . ASN B 1 109 ? 157.016 145.843 149.850 1.00 64.76 ?  109 ASN B ND2   1 
ATOM   6462  N  N     . ASP B 1 110 ? 156.567 140.563 151.167 1.00 66.37 ?  110 ASP B N     1 
ATOM   6463  C  CA    . ASP B 1 110 ? 156.742 139.139 150.916 1.00 66.12 ?  110 ASP B CA    1 
ATOM   6464  C  C     . ASP B 1 110 ? 156.010 138.266 151.928 1.00 66.70 ?  110 ASP B C     1 
ATOM   6465  O  O     . ASP B 1 110 ? 156.070 137.037 151.814 1.00 67.58 ?  110 ASP B O     1 
ATOM   6466  C  CB    . ASP B 1 110 ? 158.233 138.789 150.906 1.00 66.14 ?  110 ASP B CB    1 
ATOM   6467  C  CG    . ASP B 1 110 ? 158.954 139.273 152.147 1.00 67.51 ?  110 ASP B CG    1 
ATOM   6468  O  OD1   . ASP B 1 110 ? 158.357 140.052 152.919 1.00 67.34 ?  110 ASP B OD1   1 
ATOM   6469  O  OD2   . ASP B 1 110 ? 160.123 138.882 152.344 1.00 67.65 -1 110 ASP B OD2   1 
ATOM   6470  N  N     . LYS B 1 111 ? 155.328 138.872 152.904 1.00 62.24 ?  111 LYS B N     1 
ATOM   6471  C  CA    . LYS B 1 111 ? 154.548 138.147 153.909 1.00 63.06 ?  111 LYS B CA    1 
ATOM   6472  C  C     . LYS B 1 111 ? 155.407 137.139 154.669 1.00 64.05 ?  111 LYS B C     1 
ATOM   6473  O  O     . LYS B 1 111 ? 154.975 136.021 154.959 1.00 65.21 ?  111 LYS B O     1 
ATOM   6474  C  CB    . LYS B 1 111 ? 153.333 137.459 153.280 1.00 63.14 ?  111 LYS B CB    1 
ATOM   6475  C  CG    . LYS B 1 111 ? 152.610 138.295 152.234 1.00 63.13 ?  111 LYS B CG    1 
ATOM   6476  C  CD    . LYS B 1 111 ? 151.566 139.197 152.869 1.00 64.53 ?  111 LYS B CD    1 
ATOM   6477  C  CE    . LYS B 1 111 ? 151.308 140.429 152.017 1.00 64.19 ?  111 LYS B CE    1 
ATOM   6478  N  NZ    . LYS B 1 111 ? 151.377 140.121 150.562 1.00 63.59 1  111 LYS B NZ    1 
ATOM   6479  N  N     . LYS B 1 112 ? 156.636 137.536 154.998 1.00 64.60 ?  112 LYS B N     1 
ATOM   6480  C  CA    . LYS B 1 112 ? 157.528 136.693 155.782 1.00 64.95 ?  112 LYS B CA    1 
ATOM   6481  C  C     . LYS B 1 112 ? 157.608 137.106 157.245 1.00 64.12 ?  112 LYS B C     1 
ATOM   6482  O  O     . LYS B 1 112 ? 158.065 136.309 158.071 1.00 64.02 ?  112 LYS B O     1 
ATOM   6483  C  CB    . LYS B 1 112 ? 158.940 136.705 155.186 1.00 64.38 ?  112 LYS B CB    1 
ATOM   6484  C  CG    . LYS B 1 112 ? 159.758 137.932 155.556 1.00 65.17 ?  112 LYS B CG    1 
ATOM   6485  C  CD    . LYS B 1 112 ? 161.209 137.781 155.134 1.00 66.05 ?  112 LYS B CD    1 
ATOM   6486  C  CE    . LYS B 1 112 ? 162.003 139.041 155.437 1.00 64.52 ?  112 LYS B CE    1 
ATOM   6487  N  NZ    . LYS B 1 112 ? 161.191 140.272 155.225 1.00 64.63 1  112 LYS B NZ    1 
ATOM   6488  N  N     . LYS B 1 113 ? 157.179 138.320 157.582 1.00 59.57 ?  113 LYS B N     1 
ATOM   6489  C  CA    . LYS B 1 113 ? 157.276 138.827 158.941 1.00 59.62 ?  113 LYS B CA    1 
ATOM   6490  C  C     . LYS B 1 113 ? 155.998 139.576 159.288 1.00 57.88 ?  113 LYS B C     1 
ATOM   6491  O  O     . LYS B 1 113 ? 155.217 139.955 158.412 1.00 60.09 ?  113 LYS B O     1 
ATOM   6492  C  CB    . LYS B 1 113 ? 158.495 139.743 159.115 1.00 60.10 ?  113 LYS B CB    1 
ATOM   6493  C  CG    . LYS B 1 113 ? 159.831 139.017 159.099 1.00 58.77 ?  113 LYS B CG    1 
ATOM   6494  C  CD    . LYS B 1 113 ? 159.973 138.091 160.293 1.00 60.69 ?  113 LYS B CD    1 
ATOM   6495  C  CE    . LYS B 1 113 ? 161.316 137.383 160.288 1.00 61.41 ?  113 LYS B CE    1 
ATOM   6496  N  NZ    . LYS B 1 113 ? 161.386 136.322 161.329 1.00 60.18 1  113 LYS B NZ    1 
ATOM   6497  N  N     . ILE B 1 114 ? 155.795 139.786 160.585 1.00 52.57 ?  114 ILE B N     1 
ATOM   6498  C  CA    . ILE B 1 114 ? 154.607 140.452 161.105 1.00 52.15 ?  114 ILE B CA    1 
ATOM   6499  C  C     . ILE B 1 114 ? 154.998 141.863 161.518 1.00 53.20 ?  114 ILE B C     1 
ATOM   6500  O  O     . ILE B 1 114 ? 155.863 142.048 162.384 1.00 54.37 ?  114 ILE B O     1 
ATOM   6501  C  CB    . ILE B 1 114 ? 153.997 139.681 162.287 1.00 53.28 ?  114 ILE B CB    1 
ATOM   6502  C  CG1   . ILE B 1 114 ? 153.324 138.399 161.795 1.00 49.72 ?  114 ILE B CG1   1 
ATOM   6503  C  CG2   . ILE B 1 114 ? 153.004 140.552 163.037 1.00 51.69 ?  114 ILE B CG2   1 
ATOM   6504  C  CD1   . ILE B 1 114 ? 153.024 137.414 162.897 1.00 50.40 ?  114 ILE B CD1   1 
ATOM   6505  N  N     . LEU B 1 115 ? 154.364 142.857 160.900 1.00 49.76 ?  115 LEU B N     1 
ATOM   6506  C  CA    . LEU B 1 115 ? 154.632 144.249 161.232 1.00 48.02 ?  115 LEU B CA    1 
ATOM   6507  C  C     . LEU B 1 115 ? 153.661 144.812 162.257 1.00 49.77 ?  115 LEU B C     1 
ATOM   6508  O  O     . LEU B 1 115 ? 154.016 145.745 162.985 1.00 50.66 ?  115 LEU B O     1 
ATOM   6509  C  CB    . LEU B 1 115 ? 154.589 145.114 159.969 1.00 48.78 ?  115 LEU B CB    1 
ATOM   6510  C  CG    . LEU B 1 115 ? 155.786 145.004 159.025 1.00 48.87 ?  115 LEU B CG    1 
ATOM   6511  C  CD1   . LEU B 1 115 ? 155.433 145.566 157.660 1.00 48.97 ?  115 LEU B CD1   1 
ATOM   6512  C  CD2   . LEU B 1 115 ? 156.992 145.720 159.611 1.00 49.55 ?  115 LEU B CD2   1 
ATOM   6513  N  N     . GLU B 1 116 ? 152.448 144.271 162.336 1.00 49.06 ?  116 GLU B N     1 
ATOM   6514  C  CA    . GLU B 1 116 ? 151.406 144.801 163.203 1.00 45.44 ?  116 GLU B CA    1 
ATOM   6515  C  C     . GLU B 1 116 ? 151.031 143.781 164.265 1.00 45.77 ?  116 GLU B C     1 
ATOM   6516  O  O     . GLU B 1 116 ? 150.703 142.634 163.942 1.00 48.91 ?  116 GLU B O     1 
ATOM   6517  C  CB    . GLU B 1 116 ? 150.161 145.182 162.398 1.00 44.67 ?  116 GLU B CB    1 
ATOM   6518  C  CG    . GLU B 1 116 ? 149.999 146.667 162.164 1.00 44.82 ?  116 GLU B CG    1 
ATOM   6519  C  CD    . GLU B 1 116 ? 148.712 146.998 161.438 1.00 45.82 ?  116 GLU B CD    1 
ATOM   6520  O  OE1   . GLU B 1 116 ? 147.976 146.059 161.072 1.00 44.53 ?  116 GLU B OE1   1 
ATOM   6521  O  OE2   . GLU B 1 116 ? 148.434 148.198 161.232 1.00 47.68 -1 116 GLU B OE2   1 
ATOM   6522  N  N     . ARG B 1 117 ? 151.073 144.204 165.525 1.00 40.37 ?  117 ARG B N     1 
ATOM   6523  C  CA    . ARG B 1 117 ? 150.479 143.433 166.603 1.00 41.84 ?  117 ARG B CA    1 
ATOM   6524  C  C     . ARG B 1 117 ? 148.992 143.770 166.699 1.00 42.11 ?  117 ARG B C     1 
ATOM   6525  O  O     . ARG B 1 117 ? 148.468 144.599 165.950 1.00 44.85 ?  117 ARG B O     1 
ATOM   6526  C  CB    . ARG B 1 117 ? 151.200 143.715 167.918 1.00 43.52 ?  117 ARG B CB    1 
ATOM   6527  C  CG    . ARG B 1 117 ? 152.621 143.180 167.977 1.00 43.24 ?  117 ARG B CG    1 
ATOM   6528  C  CD    . ARG B 1 117 ? 152.676 141.714 167.582 1.00 45.76 ?  117 ARG B CD    1 
ATOM   6529  N  NE    . ARG B 1 117 ? 153.659 140.971 168.361 1.00 45.69 ?  117 ARG B NE    1 
ATOM   6530  C  CZ    . ARG B 1 117 ? 153.475 140.561 169.609 1.00 45.62 ?  117 ARG B CZ    1 
ATOM   6531  N  NH1   . ARG B 1 117 ? 152.347 140.802 170.257 1.00 44.83 1  117 ARG B NH1   1 
ATOM   6532  N  NH2   . ARG B 1 117 ? 154.446 139.891 170.222 1.00 48.06 ?  117 ARG B NH2   1 
ATOM   6533  N  N     . TYR B 1 118 ? 148.292 143.111 167.624 1.00 39.73 ?  118 TYR B N     1 
ATOM   6534  C  CA    . TYR B 1 118 ? 146.890 143.451 167.847 1.00 36.21 ?  118 TYR B CA    1 
ATOM   6535  C  C     . TYR B 1 118 ? 146.755 144.877 168.360 1.00 37.83 ?  118 TYR B C     1 
ATOM   6536  O  O     . TYR B 1 118 ? 145.881 145.631 167.910 1.00 41.14 ?  118 TYR B O     1 
ATOM   6537  C  CB    . TYR B 1 118 ? 146.253 142.463 168.820 1.00 34.13 ?  118 TYR B CB    1 
ATOM   6538  C  CG    . TYR B 1 118 ? 144.747 142.560 168.884 1.00 35.58 ?  118 TYR B CG    1 
ATOM   6539  C  CD1   . TYR B 1 118 ? 143.978 142.489 167.731 1.00 34.33 ?  118 TYR B CD1   1 
ATOM   6540  C  CD2   . TYR B 1 118 ? 144.094 142.728 170.096 1.00 35.30 ?  118 TYR B CD2   1 
ATOM   6541  C  CE1   . TYR B 1 118 ? 142.602 142.578 167.784 1.00 34.36 ?  118 TYR B CE1   1 
ATOM   6542  C  CE2   . TYR B 1 118 ? 142.720 142.815 170.160 1.00 30.65 ?  118 TYR B CE2   1 
ATOM   6543  C  CZ    . TYR B 1 118 ? 141.979 142.741 169.001 1.00 36.75 ?  118 TYR B CZ    1 
ATOM   6544  O  OH    . TYR B 1 118 ? 140.607 142.832 169.061 1.00 40.55 ?  118 TYR B OH    1 
ATOM   6545  N  N     . GLU B 1 119 ? 147.627 145.271 169.288 1.00 39.86 ?  119 GLU B N     1 
ATOM   6546  C  CA    . GLU B 1 119 ? 147.597 146.633 169.804 1.00 39.18 ?  119 GLU B CA    1 
ATOM   6547  C  C     . GLU B 1 119 ? 147.958 147.643 168.722 1.00 38.98 ?  119 GLU B C     1 
ATOM   6548  O  O     . GLU B 1 119 ? 147.375 148.728 168.668 1.00 43.90 ?  119 GLU B O     1 
ATOM   6549  C  CB    . GLU B 1 119 ? 148.536 146.760 171.001 1.00 36.58 ?  119 GLU B CB    1 
ATOM   6550  C  CG    . GLU B 1 119 ? 147.993 146.152 172.281 1.00 36.87 ?  119 GLU B CG    1 
ATOM   6551  C  CD    . GLU B 1 119 ? 148.530 144.760 172.539 1.00 44.14 ?  119 GLU B CD    1 
ATOM   6552  O  OE1   . GLU B 1 119 ? 148.847 144.051 171.560 1.00 43.47 ?  119 GLU B OE1   1 
ATOM   6553  O  OE2   . GLU B 1 119 ? 148.633 144.372 173.723 1.00 45.63 -1 119 GLU B OE2   1 
ATOM   6554  N  N     . ASP B 1 120 ? 148.913 147.307 167.851 1.00 40.51 ?  120 ASP B N     1 
ATOM   6555  C  CA    . ASP B 1 120 ? 149.277 148.216 166.767 1.00 37.36 ?  120 ASP B CA    1 
ATOM   6556  C  C     . ASP B 1 120 ? 148.112 148.421 165.807 1.00 35.98 ?  120 ASP B C     1 
ATOM   6557  O  O     . ASP B 1 120 ? 147.805 149.553 165.412 1.00 39.04 ?  120 ASP B O     1 
ATOM   6558  C  CB    . ASP B 1 120 ? 150.496 147.679 166.017 1.00 41.42 ?  120 ASP B CB    1 
ATOM   6559  C  CG    . ASP B 1 120 ? 151.679 147.434 166.926 1.00 45.25 ?  120 ASP B CG    1 
ATOM   6560  O  OD1   . ASP B 1 120 ? 151.805 148.146 167.942 1.00 45.23 ?  120 ASP B OD1   1 
ATOM   6561  O  OD2   . ASP B 1 120 ? 152.484 146.530 166.624 1.00 48.28 -1 120 ASP B OD2   1 
ATOM   6562  N  N     . ARG B 1 121 ? 147.451 147.328 165.420 1.00 33.62 ?  121 ARG B N     1 
ATOM   6563  C  CA    . ARG B 1 121 ? 146.302 147.429 164.528 1.00 33.76 ?  121 ARG B CA    1 
ATOM   6564  C  C     . ARG B 1 121 ? 145.179 148.233 165.170 1.00 36.24 ?  121 ARG B C     1 
ATOM   6565  O  O     . ARG B 1 121 ? 144.567 149.090 164.519 1.00 37.10 ?  121 ARG B O     1 
ATOM   6566  C  CB    . ARG B 1 121 ? 145.819 146.029 164.148 1.00 32.18 ?  121 ARG B CB    1 
ATOM   6567  C  CG    . ARG B 1 121 ? 144.529 145.991 163.352 1.00 30.15 ?  121 ARG B CG    1 
ATOM   6568  C  CD    . ARG B 1 121 ? 144.785 146.159 161.868 1.00 30.70 ?  121 ARG B CD    1 
ATOM   6569  N  NE    . ARG B 1 121 ? 144.297 147.443 161.381 1.00 37.96 ?  121 ARG B NE    1 
ATOM   6570  C  CZ    . ARG B 1 121 ? 144.921 148.192 160.484 1.00 34.88 ?  121 ARG B CZ    1 
ATOM   6571  N  NH1   . ARG B 1 121 ? 146.067 147.813 159.943 1.00 37.95 1  121 ARG B NH1   1 
ATOM   6572  N  NH2   . ARG B 1 121 ? 144.382 149.350 160.120 1.00 31.85 ?  121 ARG B NH2   1 
ATOM   6573  N  N     . ILE B 1 122 ? 144.906 147.979 166.451 1.00 33.71 ?  122 ILE B N     1 
ATOM   6574  C  CA    . ILE B 1 122 ? 143.844 148.703 167.141 1.00 26.54 ?  122 ILE B CA    1 
ATOM   6575  C  C     . ILE B 1 122 ? 144.185 150.183 167.249 1.00 30.87 ?  122 ILE B C     1 
ATOM   6576  O  O     . ILE B 1 122 ? 143.319 151.044 167.065 1.00 37.19 ?  122 ILE B O     1 
ATOM   6577  C  CB    . ILE B 1 122 ? 143.580 148.068 168.517 1.00 33.72 ?  122 ILE B CB    1 
ATOM   6578  C  CG1   . ILE B 1 122 ? 142.715 146.819 168.351 1.00 29.67 ?  122 ILE B CG1   1 
ATOM   6579  C  CG2   . ILE B 1 122 ? 142.913 149.063 169.459 1.00 31.03 ?  122 ILE B CG2   1 
ATOM   6580  C  CD1   . ILE B 1 122 ? 142.248 146.231 169.647 1.00 29.81 ?  122 ILE B CD1   1 
ATOM   6581  N  N     . SER B 1 123 ? 145.447 150.507 167.540 1.00 35.20 ?  123 SER B N     1 
ATOM   6582  C  CA    . SER B 1 123 ? 145.858 151.905 167.624 1.00 30.91 ?  123 SER B CA    1 
ATOM   6583  C  C     . SER B 1 123 ? 145.713 152.604 166.281 1.00 30.80 ?  123 SER B C     1 
ATOM   6584  O  O     . SER B 1 123 ? 145.253 153.748 166.218 1.00 39.32 ?  123 SER B O     1 
ATOM   6585  C  CB    . SER B 1 123 ? 147.301 152.003 168.115 1.00 32.46 ?  123 SER B CB    1 
ATOM   6586  O  OG    . SER B 1 123 ? 147.506 151.211 169.267 1.00 36.41 ?  123 SER B OG    1 
ATOM   6587  N  N     . ILE B 1 124 ? 146.111 151.937 165.196 1.00 30.84 ?  124 ILE B N     1 
ATOM   6588  C  CA    . ILE B 1 124 ? 145.997 152.549 163.875 1.00 31.07 ?  124 ILE B CA    1 
ATOM   6589  C  C     . ILE B 1 124 ? 144.534 152.777 163.518 1.00 34.58 ?  124 ILE B C     1 
ATOM   6590  O  O     . ILE B 1 124 ? 144.162 153.844 163.007 1.00 36.70 ?  124 ILE B O     1 
ATOM   6591  C  CB    . ILE B 1 124 ? 146.719 151.686 162.824 1.00 37.99 ?  124 ILE B CB    1 
ATOM   6592  C  CG1   . ILE B 1 124 ? 148.233 151.797 163.011 1.00 37.08 ?  124 ILE B CG1   1 
ATOM   6593  C  CG2   . ILE B 1 124 ? 146.321 152.102 161.418 1.00 34.09 ?  124 ILE B CG2   1 
ATOM   6594  C  CD1   . ILE B 1 124 ? 148.726 153.219 163.170 1.00 34.28 ?  124 ILE B CD1   1 
ATOM   6595  N  N     . VAL B 1 125 ? 143.678 151.790 163.793 1.00 33.80 ?  125 VAL B N     1 
ATOM   6596  C  CA    . VAL B 1 125 ? 142.256 151.938 163.495 1.00 27.57 ?  125 VAL B CA    1 
ATOM   6597  C  C     . VAL B 1 125 ? 141.648 153.059 164.331 1.00 24.37 ?  125 VAL B C     1 
ATOM   6598  O  O     . VAL B 1 125 ? 140.832 153.847 163.838 1.00 35.89 ?  125 VAL B O     1 
ATOM   6599  C  CB    . VAL B 1 125 ? 141.523 150.600 163.711 1.00 31.00 ?  125 VAL B CB    1 
ATOM   6600  C  CG1   . VAL B 1 125 ? 140.028 150.784 163.576 1.00 31.11 ?  125 VAL B CG1   1 
ATOM   6601  C  CG2   . VAL B 1 125 ? 142.010 149.567 162.710 1.00 28.16 ?  125 VAL B CG2   1 
ATOM   6602  N  N     . ALA B 1 126 ? 142.041 153.158 165.604 1.00 23.02 ?  126 ALA B N     1 
ATOM   6603  C  CA    . ALA B 1 126 ? 141.524 154.213 166.469 1.00 25.33 ?  126 ALA B CA    1 
ATOM   6604  C  C     . ALA B 1 126 ? 141.977 155.591 166.006 1.00 30.57 ?  126 ALA B C     1 
ATOM   6605  O  O     . ALA B 1 126 ? 141.195 156.548 166.029 1.00 35.12 ?  126 ALA B O     1 
ATOM   6606  C  CB    . ALA B 1 126 ? 141.965 153.966 167.907 1.00 31.54 ?  126 ALA B CB    1 
ATOM   6607  N  N     . LEU B 1 127 ? 143.242 155.714 165.598 1.00 33.87 ?  127 LEU B N     1 
ATOM   6608  C  CA    . LEU B 1 127 ? 143.741 156.991 165.105 1.00 29.95 ?  127 LEU B CA    1 
ATOM   6609  C  C     . LEU B 1 127 ? 143.043 157.389 163.814 1.00 30.74 ?  127 LEU B C     1 
ATOM   6610  O  O     . LEU B 1 127 ? 142.770 158.574 163.589 1.00 36.71 ?  127 LEU B O     1 
ATOM   6611  C  CB    . LEU B 1 127 ? 145.253 156.922 164.905 1.00 33.31 ?  127 LEU B CB    1 
ATOM   6612  C  CG    . LEU B 1 127 ? 146.104 156.882 166.176 1.00 32.21 ?  127 LEU B CG    1 
ATOM   6613  C  CD1   . LEU B 1 127 ? 147.498 156.373 165.865 1.00 36.25 ?  127 LEU B CD1   1 
ATOM   6614  C  CD2   . LEU B 1 127 ? 146.163 158.250 166.831 1.00 33.87 ?  127 LEU B CD2   1 
ATOM   6615  N  N     . PHE B 1 128 ? 142.754 156.415 162.948 1.00 29.85 ?  128 PHE B N     1 
ATOM   6616  C  CA    . PHE B 1 128 ? 141.973 156.712 161.752 1.00 29.40 ?  128 PHE B CA    1 
ATOM   6617  C  C     . PHE B 1 128 ? 140.559 157.153 162.115 1.00 28.36 ?  128 PHE B C     1 
ATOM   6618  O  O     . PHE B 1 128 ? 140.017 158.087 161.512 1.00 33.31 ?  128 PHE B O     1 
ATOM   6619  C  CB    . PHE B 1 128 ? 141.934 155.492 160.830 1.00 28.61 ?  128 PHE B CB    1 
ATOM   6620  C  CG    . PHE B 1 128 ? 140.839 155.548 159.806 1.00 33.12 ?  128 PHE B CG    1 
ATOM   6621  C  CD1   . PHE B 1 128 ? 140.972 156.335 158.677 1.00 31.02 ?  128 PHE B CD1   1 
ATOM   6622  C  CD2   . PHE B 1 128 ? 139.673 154.821 159.977 1.00 32.42 ?  128 PHE B CD2   1 
ATOM   6623  C  CE1   . PHE B 1 128 ? 139.968 156.394 157.734 1.00 31.53 ?  128 PHE B CE1   1 
ATOM   6624  C  CE2   . PHE B 1 128 ? 138.665 154.879 159.040 1.00 31.93 ?  128 PHE B CE2   1 
ATOM   6625  C  CZ    . PHE B 1 128 ? 138.812 155.667 157.916 1.00 31.58 ?  128 PHE B CZ    1 
ATOM   6626  N  N     . PHE B 1 129 ? 139.946 156.486 163.094 1.00 29.04 ?  129 PHE B N     1 
ATOM   6627  C  CA    . PHE B 1 129 ? 138.583 156.823 163.496 1.00 26.13 ?  129 PHE B CA    1 
ATOM   6628  C  C     . PHE B 1 129 ? 138.499 158.229 164.073 1.00 28.48 ?  129 PHE B C     1 
ATOM   6629  O  O     . PHE B 1 129 ? 137.569 158.983 163.762 1.00 32.18 ?  129 PHE B O     1 
ATOM   6630  C  CB    . PHE B 1 129 ? 138.074 155.811 164.522 1.00 28.98 ?  129 PHE B CB    1 
ATOM   6631  C  CG    . PHE B 1 129 ? 137.601 154.520 163.928 1.00 26.86 ?  129 PHE B CG    1 
ATOM   6632  C  CD1   . PHE B 1 129 ? 137.379 154.402 162.569 1.00 25.66 ?  129 PHE B CD1   1 
ATOM   6633  C  CD2   . PHE B 1 129 ? 137.366 153.423 164.739 1.00 25.26 ?  129 PHE B CD2   1 
ATOM   6634  C  CE1   . PHE B 1 129 ? 136.939 153.212 162.029 1.00 26.72 ?  129 PHE B CE1   1 
ATOM   6635  C  CE2   . PHE B 1 129 ? 136.924 152.232 164.205 1.00 28.32 ?  129 PHE B CE2   1 
ATOM   6636  C  CZ    . PHE B 1 129 ? 136.710 152.125 162.848 1.00 30.23 ?  129 PHE B CZ    1 
ATOM   6637  N  N     . ALA B 1 130 ? 139.458 158.599 164.922 1.00 33.69 ?  130 ALA B N     1 
ATOM   6638  C  CA    . ALA B 1 130 ? 139.346 159.848 165.669 1.00 35.78 ?  130 ALA B CA    1 
ATOM   6639  C  C     . ALA B 1 130 ? 139.506 161.070 164.775 1.00 40.17 ?  130 ALA B C     1 
ATOM   6640  O  O     . ALA B 1 130 ? 138.939 162.128 165.074 1.00 46.69 ?  130 ALA B O     1 
ATOM   6641  C  CB    . ALA B 1 130 ? 140.374 159.877 166.794 1.00 33.05 ?  130 ALA B CB    1 
ATOM   6642  N  N     . ASN B 1 131 ? 140.271 160.951 163.689 1.00 41.05 ?  131 ASN B N     1 
ATOM   6643  C  CA    . ASN B 1 131 ? 140.471 162.038 162.729 1.00 41.85 ?  131 ASN B CA    1 
ATOM   6644  C  C     . ASN B 1 131 ? 141.069 163.275 163.401 1.00 41.78 ?  131 ASN B C     1 
ATOM   6645  O  O     . ASN B 1 131 ? 140.580 164.396 163.244 1.00 44.86 ?  131 ASN B O     1 
ATOM   6646  C  CB    . ASN B 1 131 ? 139.163 162.381 162.010 1.00 38.10 ?  131 ASN B CB    1 
ATOM   6647  C  CG    . ASN B 1 131 ? 139.393 162.937 160.619 1.00 45.08 ?  131 ASN B CG    1 
ATOM   6648  O  OD1   . ASN B 1 131 ? 140.379 162.609 159.960 1.00 45.24 ?  131 ASN B OD1   1 
ATOM   6649  N  ND2   . ASN B 1 131 ? 138.476 163.783 160.162 1.00 43.88 ?  131 ASN B ND2   1 
ATOM   6650  N  N     . GLY B 1 132 ? 142.141 163.061 164.162 1.00 42.24 ?  132 GLY B N     1 
ATOM   6651  C  CA    . GLY B 1 132 ? 142.881 164.146 164.773 1.00 43.72 ?  132 GLY B CA    1 
ATOM   6652  C  C     . GLY B 1 132 ? 142.587 164.409 166.233 1.00 46.62 ?  132 GLY B C     1 
ATOM   6653  O  O     . GLY B 1 132 ? 143.195 165.318 166.810 1.00 49.36 ?  132 GLY B O     1 
ATOM   6654  N  N     . ASP B 1 133 ? 141.684 163.651 166.851 1.00 42.99 ?  133 ASP B N     1 
ATOM   6655  C  CA    . ASP B 1 133 ? 141.319 163.846 168.251 1.00 43.79 ?  133 ASP B CA    1 
ATOM   6656  C  C     . ASP B 1 133 ? 142.025 162.788 169.093 1.00 46.29 ?  133 ASP B C     1 
ATOM   6657  O  O     . ASP B 1 133 ? 141.700 161.600 169.010 1.00 48.43 ?  133 ASP B O     1 
ATOM   6658  C  CB    . ASP B 1 133 ? 139.804 163.773 168.429 1.00 45.24 ?  133 ASP B CB    1 
ATOM   6659  C  CG    . ASP B 1 133 ? 139.335 164.410 169.723 1.00 48.48 ?  133 ASP B CG    1 
ATOM   6660  O  OD1   . ASP B 1 133 ? 140.163 164.585 170.641 1.00 49.94 ?  133 ASP B OD1   1 
ATOM   6661  O  OD2   . ASP B 1 133 ? 138.133 164.734 169.823 1.00 49.76 -1 133 ASP B OD2   1 
ATOM   6662  N  N     . THR B 1 134 ? 142.990 163.222 169.905 1.00 46.10 ?  134 THR B N     1 
ATOM   6663  C  CA    . THR B 1 134 ? 143.757 162.277 170.712 1.00 45.62 ?  134 THR B CA    1 
ATOM   6664  C  C     . THR B 1 134 ? 142.883 161.597 171.760 1.00 45.11 ?  134 THR B C     1 
ATOM   6665  O  O     . THR B 1 134 ? 142.993 160.385 171.974 1.00 45.77 ?  134 THR B O     1 
ATOM   6666  C  CB    . THR B 1 134 ? 144.931 162.990 171.378 1.00 47.78 ?  134 THR B CB    1 
ATOM   6667  O  OG1   . THR B 1 134 ? 145.641 163.751 170.395 1.00 49.81 ?  134 THR B OG1   1 
ATOM   6668  C  CG2   . THR B 1 134 ? 145.874 161.979 172.014 1.00 46.42 ?  134 THR B CG2   1 
ATOM   6669  N  N     . GLU B 1 135 ? 142.013 162.359 172.428 1.00 43.87 ?  135 GLU B N     1 
ATOM   6670  C  CA    . GLU B 1 135 ? 141.132 161.767 173.428 1.00 42.72 ?  135 GLU B CA    1 
ATOM   6671  C  C     . GLU B 1 135 ? 140.148 160.794 172.791 1.00 44.61 ?  135 GLU B C     1 
ATOM   6672  O  O     . GLU B 1 135 ? 139.880 159.721 173.344 1.00 45.08 ?  135 GLU B O     1 
ATOM   6673  C  CB    . GLU B 1 135 ? 140.392 162.864 174.192 1.00 45.96 ?  135 GLU B CB    1 
ATOM   6674  C  CG    . GLU B 1 135 ? 141.300 163.725 175.050 1.00 46.64 ?  135 GLU B CG    1 
ATOM   6675  C  CD    . GLU B 1 135 ? 142.241 162.900 175.907 1.00 50.56 ?  135 GLU B CD    1 
ATOM   6676  O  OE1   . GLU B 1 135 ? 141.750 162.094 176.724 1.00 49.79 ?  135 GLU B OE1   1 
ATOM   6677  O  OE2   . GLU B 1 135 ? 143.472 163.057 175.762 1.00 49.37 -1 135 GLU B OE2   1 
ATOM   6678  N  N     . LYS B 1 136 ? 139.603 161.149 171.626 1.00 40.26 ?  136 LYS B N     1 
ATOM   6679  C  CA    . LYS B 1 136 ? 138.722 160.229 170.913 1.00 37.63 ?  136 LYS B CA    1 
ATOM   6680  C  C     . LYS B 1 136 ? 139.482 158.987 170.463 1.00 37.69 ?  136 LYS B C     1 
ATOM   6681  O  O     . LYS B 1 136 ? 138.938 157.876 170.478 1.00 41.90 ?  136 LYS B O     1 
ATOM   6682  C  CB    . LYS B 1 136 ? 138.084 160.937 169.720 1.00 42.81 ?  136 LYS B CB    1 
ATOM   6683  C  CG    . LYS B 1 136 ? 136.848 160.251 169.170 1.00 41.41 ?  136 LYS B CG    1 
ATOM   6684  C  CD    . LYS B 1 136 ? 135.588 160.746 169.856 1.00 41.96 ?  136 LYS B CD    1 
ATOM   6685  C  CE    . LYS B 1 136 ? 134.353 160.428 169.032 1.00 42.73 ?  136 LYS B CE    1 
ATOM   6686  N  NZ    . LYS B 1 136 ? 133.159 161.173 169.514 1.00 43.51 1  136 LYS B NZ    1 
ATOM   6687  N  N     . ALA B 1 137 ? 140.741 159.155 170.056 1.00 36.90 ?  137 ALA B N     1 
ATOM   6688  C  CA    . ALA B 1 137 ? 141.556 158.005 169.679 1.00 33.48 ?  137 ALA B CA    1 
ATOM   6689  C  C     . ALA B 1 137 ? 141.783 157.080 170.866 1.00 36.36 ?  137 ALA B C     1 
ATOM   6690  O  O     . ALA B 1 137 ? 141.731 155.854 170.726 1.00 39.45 ?  137 ALA B O     1 
ATOM   6691  C  CB    . ALA B 1 137 ? 142.888 158.472 169.094 1.00 33.49 ?  137 ALA B CB    1 
ATOM   6692  N  N     . LYS B 1 138 ? 142.027 157.651 172.048 1.00 38.61 ?  138 LYS B N     1 
ATOM   6693  C  CA    . LYS B 1 138 ? 142.173 156.831 173.247 1.00 36.74 ?  138 LYS B CA    1 
ATOM   6694  C  C     . LYS B 1 138 ? 140.866 156.138 173.606 1.00 37.49 ?  138 LYS B C     1 
ATOM   6695  O  O     . LYS B 1 138 ? 140.872 154.991 174.068 1.00 39.01 ?  138 LYS B O     1 
ATOM   6696  C  CB    . LYS B 1 138 ? 142.664 157.684 174.415 1.00 41.46 ?  138 LYS B CB    1 
ATOM   6697  C  CG    . LYS B 1 138 ? 144.028 158.305 174.200 1.00 41.35 ?  138 LYS B CG    1 
ATOM   6698  C  CD    . LYS B 1 138 ? 144.806 158.363 175.499 1.00 38.39 ?  138 LYS B CD    1 
ATOM   6699  C  CE    . LYS B 1 138 ? 145.787 159.516 175.497 1.00 41.44 ?  138 LYS B CE    1 
ATOM   6700  N  NZ    . LYS B 1 138 ? 145.115 160.812 175.202 1.00 43.43 1  138 LYS B NZ    1 
ATOM   6701  N  N     . GLU B 1 139 ? 139.736 156.821 173.419 1.00 37.44 ?  139 GLU B N     1 
ATOM   6702  C  CA    . GLU B 1 139 ? 138.442 156.189 173.667 1.00 37.33 ?  139 GLU B CA    1 
ATOM   6703  C  C     . GLU B 1 139 ? 138.222 155.003 172.736 1.00 36.11 ?  139 GLU B C     1 
ATOM   6704  O  O     . GLU B 1 139 ? 137.765 153.940 173.168 1.00 41.74 ?  139 GLU B O     1 
ATOM   6705  C  CB    . GLU B 1 139 ? 137.318 157.212 173.509 1.00 34.82 ?  139 GLU B CB    1 
ATOM   6706  C  CG    . GLU B 1 139 ? 137.273 158.261 174.606 1.00 38.00 ?  139 GLU B CG    1 
ATOM   6707  C  CD    . GLU B 1 139 ? 136.167 159.274 174.397 1.00 45.17 ?  139 GLU B CD    1 
ATOM   6708  O  OE1   . GLU B 1 139 ? 135.126 158.907 173.812 1.00 43.55 ?  139 GLU B OE1   1 
ATOM   6709  O  OE2   . GLU B 1 139 ? 136.337 160.437 174.817 1.00 44.22 -1 139 GLU B OE2   1 
ATOM   6710  N  N     . TYR B 1 140 ? 138.555 155.164 171.453 1.00 29.54 ?  140 TYR B N     1 
ATOM   6711  C  CA    . TYR B 1 140 ? 138.439 154.055 170.510 1.00 28.47 ?  140 TYR B CA    1 
ATOM   6712  C  C     . TYR B 1 140 ? 139.392 152.923 170.871 1.00 31.07 ?  140 TYR B C     1 
ATOM   6713  O  O     . TYR B 1 140 ? 139.048 151.742 170.735 1.00 35.49 ?  140 TYR B O     1 
ATOM   6714  C  CB    . TYR B 1 140 ? 138.710 154.541 169.088 1.00 29.36 ?  140 TYR B CB    1 
ATOM   6715  C  CG    . TYR B 1 140 ? 137.583 155.326 168.465 1.00 30.90 ?  140 TYR B CG    1 
ATOM   6716  C  CD1   . TYR B 1 140 ? 136.299 154.804 168.399 1.00 31.12 ?  140 TYR B CD1   1 
ATOM   6717  C  CD2   . TYR B 1 140 ? 137.806 156.588 167.937 1.00 32.00 ?  140 TYR B CD2   1 
ATOM   6718  C  CE1   . TYR B 1 140 ? 135.270 155.521 167.824 1.00 34.65 ?  140 TYR B CE1   1 
ATOM   6719  C  CE2   . TYR B 1 140 ? 136.785 157.311 167.366 1.00 30.75 ?  140 TYR B CE2   1 
ATOM   6720  C  CZ    . TYR B 1 140 ? 135.521 156.776 167.310 1.00 28.98 ?  140 TYR B CZ    1 
ATOM   6721  O  OH    . TYR B 1 140 ? 134.509 157.503 166.737 1.00 37.84 ?  140 TYR B OH    1 
ATOM   6722  N  N     . VAL B 1 141 ? 140.602 153.267 171.316 1.00 32.75 ?  141 VAL B N     1 
ATOM   6723  C  CA    . VAL B 1 141 ? 141.570 152.254 171.730 1.00 32.90 ?  141 VAL B CA    1 
ATOM   6724  C  C     . VAL B 1 141 ? 141.030 151.454 172.906 1.00 32.97 ?  141 VAL B C     1 
ATOM   6725  O  O     . VAL B 1 141 ? 141.124 150.223 172.937 1.00 38.73 ?  141 VAL B O     1 
ATOM   6726  C  CB    . VAL B 1 141 ? 142.921 152.911 172.066 1.00 35.19 ?  141 VAL B CB    1 
ATOM   6727  C  CG1   . VAL B 1 141 ? 143.662 152.094 173.094 1.00 33.55 ?  141 VAL B CG1   1 
ATOM   6728  C  CG2   . VAL B 1 141 ? 143.760 153.040 170.817 1.00 33.99 ?  141 VAL B CG2   1 
ATOM   6729  N  N     . ASN B 1 142 ? 140.463 152.142 173.897 1.00 32.61 ?  142 ASN B N     1 
ATOM   6730  C  CA    . ASN B 1 142 ? 139.895 151.443 175.043 1.00 30.80 ?  142 ASN B CA    1 
ATOM   6731  C  C     . ASN B 1 142 ? 138.680 150.618 174.645 1.00 31.55 ?  142 ASN B C     1 
ATOM   6732  O  O     . ASN B 1 142 ? 138.435 149.556 175.227 1.00 35.97 ?  142 ASN B O     1 
ATOM   6733  C  CB    . ASN B 1 142 ? 139.529 152.442 176.138 1.00 28.16 ?  142 ASN B CB    1 
ATOM   6734  C  CG    . ASN B 1 142 ? 140.745 152.995 176.850 1.00 32.27 ?  142 ASN B CG    1 
ATOM   6735  O  OD1   . ASN B 1 142 ? 141.575 152.244 177.359 1.00 32.50 ?  142 ASN B OD1   1 
ATOM   6736  N  ND2   . ASN B 1 142 ? 140.860 154.317 176.883 1.00 34.28 ?  142 ASN B ND2   1 
ATOM   6737  N  N     . LEU B 1 143 ? 137.913 151.089 173.661 1.00 31.52 ?  143 LEU B N     1 
ATOM   6738  C  CA    . LEU B 1 143 ? 136.736 150.353 173.216 1.00 25.88 ?  143 LEU B CA    1 
ATOM   6739  C  C     . LEU B 1 143 ? 137.119 149.074 172.483 1.00 30.44 ?  143 LEU B C     1 
ATOM   6740  O  O     . LEU B 1 143 ? 136.454 148.042 172.634 1.00 32.84 ?  143 LEU B O     1 
ATOM   6741  C  CB    . LEU B 1 143 ? 135.880 151.250 172.326 1.00 25.23 ?  143 LEU B CB    1 
ATOM   6742  C  CG    . LEU B 1 143 ? 134.396 150.917 172.217 1.00 28.76 ?  143 LEU B CG    1 
ATOM   6743  C  CD1   . LEU B 1 143 ? 133.674 151.369 173.470 1.00 31.58 ?  143 LEU B CD1   1 
ATOM   6744  C  CD2   . LEU B 1 143 ? 133.811 151.588 170.993 1.00 28.42 ?  143 LEU B CD2   1 
ATOM   6745  N  N     . MET B 1 144 ? 138.179 149.122 171.677 1.00 28.96 ?  144 MET B N     1 
ATOM   6746  C  CA    . MET B 1 144 ? 138.572 147.963 170.884 1.00 21.69 ?  144 MET B CA    1 
ATOM   6747  C  C     . MET B 1 144 ? 139.493 147.005 171.628 1.00 26.49 ?  144 MET B C     1 
ATOM   6748  O  O     . MET B 1 144 ? 139.418 145.791 171.402 1.00 30.49 ?  144 MET B O     1 
ATOM   6749  C  CB    . MET B 1 144 ? 139.246 148.417 169.586 1.00 24.86 ?  144 MET B CB    1 
ATOM   6750  C  CG    . MET B 1 144 ? 138.309 149.123 168.624 1.00 25.95 ?  144 MET B CG    1 
ATOM   6751  S  SD    . MET B 1 144 ? 139.071 149.444 167.026 1.00 37.66 ?  144 MET B SD    1 
ATOM   6752  C  CE    . MET B 1 144 ? 139.666 151.112 167.276 1.00 27.90 ?  144 MET B CE    1 
ATOM   6753  N  N     . ILE B 1 145 ? 140.369 147.513 172.496 1.00 29.57 ?  145 ILE B N     1 
ATOM   6754  C  CA    . ILE B 1 145 ? 141.240 146.639 173.275 1.00 30.47 ?  145 ILE B CA    1 
ATOM   6755  C  C     . ILE B 1 145 ? 140.446 145.906 174.353 1.00 31.16 ?  145 ILE B C     1 
ATOM   6756  O  O     . ILE B 1 145 ? 140.766 144.761 174.691 1.00 35.22 ?  145 ILE B O     1 
ATOM   6757  C  CB    . ILE B 1 145 ? 142.423 147.436 173.857 1.00 29.75 ?  145 ILE B CB    1 
ATOM   6758  C  CG1   . ILE B 1 145 ? 143.665 146.549 173.965 1.00 28.07 ?  145 ILE B CG1   1 
ATOM   6759  C  CG2   . ILE B 1 145 ? 142.082 148.057 175.205 1.00 31.72 ?  145 ILE B CG2   1 
ATOM   6760  C  CD1   . ILE B 1 145 ? 144.304 146.224 172.636 1.00 28.63 ?  145 ILE B CD1   1 
ATOM   6761  N  N     . ASN B 1 146 ? 139.406 146.539 174.904 1.00 28.14 ?  146 ASN B N     1 
ATOM   6762  C  CA    . ASN B 1 146 ? 138.451 145.821 175.738 1.00 28.75 ?  146 ASN B CA    1 
ATOM   6763  C  C     . ASN B 1 146 ? 137.565 144.902 174.917 1.00 30.68 ?  146 ASN B C     1 
ATOM   6764  O  O     . ASN B 1 146 ? 136.808 144.115 175.497 1.00 37.17 ?  146 ASN B O     1 
ATOM   6765  C  CB    . ASN B 1 146 ? 137.581 146.802 176.523 1.00 28.50 ?  146 ASN B CB    1 
ATOM   6766  C  CG    . ASN B 1 146 ? 138.364 147.575 177.563 1.00 31.95 ?  146 ASN B CG    1 
ATOM   6767  O  OD1   . ASN B 1 146 ? 139.453 147.168 177.966 1.00 33.23 ?  146 ASN B OD1   1 
ATOM   6768  N  ND2   . ASN B 1 146 ? 137.813 148.699 178.003 1.00 31.99 ?  146 ASN B ND2   1 
ATOM   6769  N  N     . GLN B 1 147 ? 137.638 144.999 173.589 1.00 27.45 ?  147 GLN B N     1 
ATOM   6770  C  CA    . GLN B 1 147 ? 136.848 144.184 172.671 1.00 23.39 ?  147 GLN B CA    1 
ATOM   6771  C  C     . GLN B 1 147 ? 135.353 144.386 172.882 1.00 23.64 ?  147 GLN B C     1 
ATOM   6772  O  O     . GLN B 1 147 ? 134.561 143.464 172.693 1.00 30.53 ?  147 GLN B O     1 
ATOM   6773  C  CB    . GLN B 1 147 ? 137.219 142.703 172.787 1.00 26.93 ?  147 GLN B CB    1 
ATOM   6774  C  CG    . GLN B 1 147 ? 138.648 142.402 172.375 1.00 20.38 ?  147 GLN B CG    1 
ATOM   6775  C  CD    . GLN B 1 147 ? 138.828 140.977 171.905 1.00 27.43 ?  147 GLN B CD    1 
ATOM   6776  O  OE1   . GLN B 1 147 ? 139.520 140.719 170.920 1.00 28.19 ?  147 GLN B OE1   1 
ATOM   6777  N  NE2   . GLN B 1 147 ? 138.210 140.039 172.610 1.00 34.56 ?  147 GLN B NE2   1 
ATOM   6778  N  N     . GLU B 1 148 ? 134.962 145.593 173.293 1.00 26.03 ?  148 GLU B N     1 
ATOM   6779  C  CA    . GLU B 1 148 ? 133.547 145.937 173.354 1.00 23.10 ?  148 GLU B CA    1 
ATOM   6780  C  C     . GLU B 1 148 ? 132.966 146.165 171.966 1.00 26.63 ?  148 GLU B C     1 
ATOM   6781  O  O     . GLU B 1 148 ? 131.810 145.808 171.713 1.00 32.90 ?  148 GLU B O     1 
ATOM   6782  C  CB    . GLU B 1 148 ? 133.346 147.186 174.212 1.00 21.39 ?  148 GLU B CB    1 
ATOM   6783  C  CG    . GLU B 1 148 ? 133.780 147.024 175.655 1.00 26.46 ?  148 GLU B CG    1 
ATOM   6784  C  CD    . GLU B 1 148 ? 133.796 148.339 176.403 1.00 32.26 ?  148 GLU B CD    1 
ATOM   6785  O  OE1   . GLU B 1 148 ? 134.793 149.081 176.284 1.00 33.54 ?  148 GLU B OE1   1 
ATOM   6786  O  OE2   . GLU B 1 148 ? 132.810 148.633 177.110 1.00 37.57 -1 148 GLU B OE2   1 
ATOM   6787  N  N     . TYR B 1 149 ? 133.748 146.747 171.064 1.00 23.60 ?  149 TYR B N     1 
ATOM   6788  C  CA    . TYR B 1 149 ? 133.323 147.021 169.702 1.00 19.15 ?  149 TYR B CA    1 
ATOM   6789  C  C     . TYR B 1 149 ? 134.362 146.494 168.730 1.00 22.53 ?  149 TYR B C     1 
ATOM   6790  O  O     . TYR B 1 149 ? 135.566 146.564 168.992 1.00 28.88 ?  149 TYR B O     1 
ATOM   6791  C  CB    . TYR B 1 149 ? 133.106 148.517 169.474 1.00 21.16 ?  149 TYR B CB    1 
ATOM   6792  C  CG    . TYR B 1 149 ? 132.897 148.891 168.026 1.00 21.61 ?  149 TYR B CG    1 
ATOM   6793  C  CD1   . TYR B 1 149 ? 131.775 148.460 167.331 1.00 13.92 ?  149 TYR B CD1   1 
ATOM   6794  C  CD2   . TYR B 1 149 ? 133.821 149.679 167.355 1.00 19.53 ?  149 TYR B CD2   1 
ATOM   6795  C  CE1   . TYR B 1 149 ? 131.582 148.802 166.008 1.00 17.41 ?  149 TYR B CE1   1 
ATOM   6796  C  CE2   . TYR B 1 149 ? 133.637 150.026 166.034 1.00 20.91 ?  149 TYR B CE2   1 
ATOM   6797  C  CZ    . TYR B 1 149 ? 132.516 149.586 165.364 1.00 20.04 ?  149 TYR B CZ    1 
ATOM   6798  O  OH    . TYR B 1 149 ? 132.332 149.932 164.047 1.00 18.44 ?  149 TYR B OH    1 
ATOM   6799  N  N     . GLN B 1 150 ? 133.889 145.964 167.613 1.00 17.68 ?  150 GLN B N     1 
ATOM   6800  C  CA    . GLN B 1 150 ? 134.753 145.421 166.572 1.00 10.71 ?  150 GLN B CA    1 
ATOM   6801  C  C     . GLN B 1 150 ? 134.357 146.019 165.232 1.00 20.38 ?  150 GLN B C     1 
ATOM   6802  O  O     . GLN B 1 150 ? 133.232 145.772 164.756 1.00 23.27 ?  150 GLN B O     1 
ATOM   6803  C  CB    . GLN B 1 150 ? 134.645 143.898 166.536 1.00 17.41 ?  150 GLN B CB    1 
ATOM   6804  C  CG    . GLN B 1 150 ? 135.471 143.244 165.457 1.00 18.97 ?  150 GLN B CG    1 
ATOM   6805  C  CD    . GLN B 1 150 ? 136.938 143.607 165.542 1.00 17.16 ?  150 GLN B CD    1 
ATOM   6806  O  OE1   . GLN B 1 150 ? 137.613 143.295 166.521 1.00 30.40 ?  150 GLN B OE1   1 
ATOM   6807  N  NE2   . GLN B 1 150 ? 137.442 144.266 164.508 1.00 15.84 ?  150 GLN B NE2   1 
ATOM   6808  N  N     . PRO B 1 151 ? 135.212 146.824 164.607 1.00 26.31 ?  151 PRO B N     1 
ATOM   6809  C  CA    . PRO B 1 151 ? 134.937 147.257 163.235 1.00 16.21 ?  151 PRO B CA    1 
ATOM   6810  C  C     . PRO B 1 151 ? 134.917 146.063 162.295 1.00 16.18 ?  151 PRO B C     1 
ATOM   6811  O  O     . PRO B 1 151 ? 135.560 145.040 162.542 1.00 21.62 ?  151 PRO B O     1 
ATOM   6812  C  CB    . PRO B 1 151 ? 136.099 148.205 162.918 1.00 18.71 ?  151 PRO B CB    1 
ATOM   6813  C  CG    . PRO B 1 151 ? 136.623 148.630 164.251 1.00 18.97 ?  151 PRO B CG    1 
ATOM   6814  C  CD    . PRO B 1 151 ? 136.415 147.464 165.163 1.00 21.62 ?  151 PRO B CD    1 
ATOM   6815  N  N     . SER B 1 152 ? 134.152 146.196 161.216 1.00 21.04 ?  152 SER B N     1 
ATOM   6816  C  CA    . SER B 1 152 ? 134.019 145.113 160.254 1.00 14.61 ?  152 SER B CA    1 
ATOM   6817  C  C     . SER B 1 152 ? 135.378 144.730 159.677 1.00 22.02 ?  152 SER B C     1 
ATOM   6818  O  O     . SER B 1 152 ? 136.364 145.462 159.792 1.00 25.96 ?  152 SER B O     1 
ATOM   6819  C  CB    . SER B 1 152 ? 133.071 145.510 159.126 1.00 20.91 ?  152 SER B CB    1 
ATOM   6820  O  OG    . SER B 1 152 ? 133.629 146.542 158.331 1.00 24.93 ?  152 SER B OG    1 
ATOM   6821  N  N     . THR B 1 153 ? 135.420 143.553 159.054 1.00 28.20 ?  153 THR B N     1 
ATOM   6822  C  CA    . THR B 1 153 ? 136.649 143.075 158.426 1.00 20.89 ?  153 THR B CA    1 
ATOM   6823  C  C     . THR B 1 153 ? 137.250 144.075 157.443 1.00 27.54 ?  153 THR B C     1 
ATOM   6824  O  O     . THR B 1 153 ? 138.464 144.316 157.519 1.00 27.63 ?  153 THR B O     1 
ATOM   6825  C  CB    . THR B 1 153 ? 136.382 141.719 157.755 1.00 25.86 ?  153 THR B CB    1 
ATOM   6826  O  OG1   . THR B 1 153 ? 136.251 140.705 158.758 1.00 29.62 ?  153 THR B OG1   1 
ATOM   6827  C  CG2   . THR B 1 153 ? 137.513 141.350 156.808 1.00 25.78 ?  153 THR B CG2   1 
ATOM   6828  N  N     . PRO B 1 154 ? 136.490 144.700 156.531 1.00 25.81 ?  154 PRO B N     1 
ATOM   6829  C  CA    . PRO B 1 154 ? 137.109 145.737 155.686 1.00 19.80 ?  154 PRO B CA    1 
ATOM   6830  C  C     . PRO B 1 154 ? 137.689 146.890 156.486 1.00 20.96 ?  154 PRO B C     1 
ATOM   6831  O  O     . PRO B 1 154 ? 138.832 147.300 156.245 1.00 26.68 ?  154 PRO B O     1 
ATOM   6832  C  CB    . PRO B 1 154 ? 135.952 146.188 154.785 1.00 21.37 ?  154 PRO B CB    1 
ATOM   6833  C  CG    . PRO B 1 154 ? 135.017 145.046 154.768 1.00 24.97 ?  154 PRO B CG    1 
ATOM   6834  C  CD    . PRO B 1 154 ? 135.093 144.447 156.131 1.00 19.97 ?  154 PRO B CD    1 
ATOM   6835  N  N     . THR B 1 155 ? 136.934 147.415 157.454 1.00 22.65 ?  155 THR B N     1 
ATOM   6836  C  CA    . THR B 1 155 ? 137.411 148.553 158.232 1.00 20.13 ?  155 THR B CA    1 
ATOM   6837  C  C     . THR B 1 155 ? 138.583 148.163 159.124 1.00 24.21 ?  155 THR B C     1 
ATOM   6838  O  O     . THR B 1 155 ? 139.609 148.851 159.153 1.00 29.73 ?  155 THR B O     1 
ATOM   6839  C  CB    . THR B 1 155 ? 136.271 149.134 159.067 1.00 22.59 ?  155 THR B CB    1 
ATOM   6840  O  OG1   . THR B 1 155 ? 135.148 149.409 158.222 1.00 23.45 ?  155 THR B OG1   1 
ATOM   6841  C  CG2   . THR B 1 155 ? 136.713 150.419 159.742 1.00 17.64 ?  155 THR B CG2   1 
ATOM   6842  N  N     . PHE B 1 156 ? 138.451 147.058 159.860 1.00 23.30 ?  156 PHE B N     1 
ATOM   6843  C  CA    . PHE B 1 156 ? 139.521 146.644 160.763 1.00 20.13 ?  156 PHE B CA    1 
ATOM   6844  C  C     . PHE B 1 156 ? 140.795 146.309 159.998 1.00 29.69 ?  156 PHE B C     1 
ATOM   6845  O  O     . PHE B 1 156 ? 141.899 146.654 160.434 1.00 29.95 ?  156 PHE B O     1 
ATOM   6846  C  CB    . PHE B 1 156 ? 139.071 145.447 161.600 1.00 23.60 ?  156 PHE B CB    1 
ATOM   6847  C  CG    . PHE B 1 156 ? 139.917 145.208 162.818 1.00 28.03 ?  156 PHE B CG    1 
ATOM   6848  C  CD1   . PHE B 1 156 ? 140.057 146.190 163.784 1.00 24.88 ?  156 PHE B CD1   1 
ATOM   6849  C  CD2   . PHE B 1 156 ? 140.572 144.003 162.995 1.00 23.77 ?  156 PHE B CD2   1 
ATOM   6850  C  CE1   . PHE B 1 156 ? 140.835 145.974 164.903 1.00 26.16 ?  156 PHE B CE1   1 
ATOM   6851  C  CE2   . PHE B 1 156 ? 141.352 143.781 164.113 1.00 22.91 ?  156 PHE B CE2   1 
ATOM   6852  C  CZ    . PHE B 1 156 ? 141.482 144.767 165.068 1.00 29.01 ?  156 PHE B CZ    1 
ATOM   6853  N  N     . LEU B 1 157 ? 140.662 145.637 158.855 1.00 30.11 ?  157 LEU B N     1 
ATOM   6854  C  CA    . LEU B 1 157 ? 141.829 145.204 158.098 1.00 26.59 ?  157 LEU B CA    1 
ATOM   6855  C  C     . LEU B 1 157 ? 142.476 146.351 157.331 1.00 31.97 ?  157 LEU B C     1 
ATOM   6856  O  O     . LEU B 1 157 ? 143.705 146.400 157.211 1.00 40.37 ?  157 LEU B O     1 
ATOM   6857  C  CB    . LEU B 1 157 ? 141.430 144.079 157.139 1.00 30.79 ?  157 LEU B CB    1 
ATOM   6858  C  CG    . LEU B 1 157 ? 142.453 143.627 156.097 1.00 29.61 ?  157 LEU B CG    1 
ATOM   6859  C  CD1   . LEU B 1 157 ? 143.657 142.990 156.766 1.00 32.68 ?  157 LEU B CD1   1 
ATOM   6860  C  CD2   . LEU B 1 157 ? 141.815 142.665 155.109 1.00 30.30 ?  157 LEU B CD2   1 
ATOM   6861  N  N     . ASN B 1 158 ? 141.680 147.289 156.815 1.00 30.57 ?  158 ASN B N     1 
ATOM   6862  C  CA    . ASN B 1 158 ? 142.172 148.250 155.841 1.00 29.15 ?  158 ASN B CA    1 
ATOM   6863  C  C     . ASN B 1 158 ? 142.311 149.673 156.364 1.00 32.44 ?  158 ASN B C     1 
ATOM   6864  O  O     . ASN B 1 158 ? 142.814 150.529 155.629 1.00 39.63 ?  158 ASN B O     1 
ATOM   6865  C  CB    . ASN B 1 158 ? 141.252 148.261 154.612 1.00 29.82 ?  158 ASN B CB    1 
ATOM   6866  C  CG    . ASN B 1 158 ? 141.207 146.922 153.908 1.00 35.71 ?  158 ASN B CG    1 
ATOM   6867  O  OD1   . ASN B 1 158 ? 142.164 146.151 153.956 1.00 40.03 ?  158 ASN B OD1   1 
ATOM   6868  N  ND2   . ASN B 1 158 ? 140.090 146.637 153.250 1.00 35.98 ?  158 ASN B ND2   1 
ATOM   6869  N  N     . ALA B 1 159 ? 141.884 149.960 157.593 1.00 31.90 ?  159 ALA B N     1 
ATOM   6870  C  CA    . ALA B 1 159 ? 141.952 151.329 158.091 1.00 33.22 ?  159 ALA B CA    1 
ATOM   6871  C  C     . ALA B 1 159 ? 143.399 151.793 158.194 1.00 38.83 ?  159 ALA B C     1 
ATOM   6872  O  O     . ALA B 1 159 ? 144.243 151.115 158.786 1.00 42.87 ?  159 ALA B O     1 
ATOM   6873  C  CB    . ALA B 1 159 ? 141.269 151.439 159.453 1.00 32.12 ?  159 ALA B CB    1 
ATOM   6874  N  N     . GLY B 1 160 ? 143.683 152.954 157.611 1.00 45.42 ?  160 GLY B N     1 
ATOM   6875  C  CA    . GLY B 1 160 ? 145.005 153.536 157.697 1.00 40.42 ?  160 GLY B CA    1 
ATOM   6876  C  C     . GLY B 1 160 ? 146.066 152.878 156.846 1.00 40.71 ?  160 GLY B C     1 
ATOM   6877  O  O     . GLY B 1 160 ? 147.250 153.174 157.031 1.00 45.57 ?  160 GLY B O     1 
ATOM   6878  N  N     . ARG B 1 161 ? 145.688 151.999 155.925 1.00 43.00 ?  161 ARG B N     1 
ATOM   6879  C  CA    . ARG B 1 161 ? 146.639 151.298 155.074 1.00 44.08 ?  161 ARG B CA    1 
ATOM   6880  C  C     . ARG B 1 161 ? 146.690 151.945 153.697 1.00 46.63 ?  161 ARG B C     1 
ATOM   6881  O  O     . ARG B 1 161 ? 145.662 152.360 153.154 1.00 46.53 ?  161 ARG B O     1 
ATOM   6882  C  CB    . ARG B 1 161 ? 146.270 149.820 154.939 1.00 38.66 ?  161 ARG B CB    1 
ATOM   6883  C  CG    . ARG B 1 161 ? 146.510 149.002 156.195 1.00 39.48 ?  161 ARG B CG    1 
ATOM   6884  C  CD    . ARG B 1 161 ? 146.558 147.516 155.886 1.00 40.50 ?  161 ARG B CD    1 
ATOM   6885  N  NE    . ARG B 1 161 ? 146.556 146.706 157.099 1.00 44.00 ?  161 ARG B NE    1 
ATOM   6886  C  CZ    . ARG B 1 161 ? 146.520 145.381 157.116 1.00 44.80 ?  161 ARG B CZ    1 
ATOM   6887  N  NH1   . ARG B 1 161 ? 146.493 144.675 155.999 1.00 44.14 1  161 ARG B NH1   1 
ATOM   6888  N  NH2   . ARG B 1 161 ? 146.511 144.749 158.286 1.00 43.06 ?  161 ARG B NH2   1 
ATOM   6889  N  N     . LYS B 1 162 ? 147.900 152.042 153.138 1.00 53.05 ?  162 LYS B N     1 
ATOM   6890  C  CA    . LYS B 1 162 ? 148.050 152.602 151.799 1.00 52.29 ?  162 LYS B CA    1 
ATOM   6891  C  C     . LYS B 1 162 ? 147.544 151.634 150.735 1.00 52.62 ?  162 LYS B C     1 
ATOM   6892  O  O     . LYS B 1 162 ? 146.836 152.039 149.806 1.00 52.82 ?  162 LYS B O     1 
ATOM   6893  C  CB    . LYS B 1 162 ? 149.512 152.970 151.546 1.00 52.13 ?  162 LYS B CB    1 
ATOM   6894  C  CG    . LYS B 1 162 ? 149.824 153.326 150.103 1.00 52.46 ?  162 LYS B CG    1 
ATOM   6895  C  CD    . LYS B 1 162 ? 149.635 154.813 149.844 1.00 54.30 ?  162 LYS B CD    1 
ATOM   6896  C  CE    . LYS B 1 162 ? 150.469 155.653 150.798 1.00 54.39 ?  162 LYS B CE    1 
ATOM   6897  N  NZ    . LYS B 1 162 ? 149.812 156.954 151.104 1.00 54.64 1  162 LYS B NZ    1 
ATOM   6898  N  N     . ARG B 1 163 ? 147.886 150.351 150.860 1.00 53.33 ?  163 ARG B N     1 
ATOM   6899  C  CA    . ARG B 1 163 ? 147.453 149.320 149.925 1.00 55.14 ?  163 ARG B CA    1 
ATOM   6900  C  C     . ARG B 1 163 ? 146.052 148.803 150.232 1.00 57.86 ?  163 ARG B C     1 
ATOM   6901  O  O     . ARG B 1 163 ? 145.687 147.705 149.792 1.00 56.49 ?  163 ARG B O     1 
ATOM   6902  C  CB    . ARG B 1 163 ? 148.457 148.163 149.920 1.00 56.25 ?  163 ARG B CB    1 
ATOM   6903  C  CG    . ARG B 1 163 ? 148.540 147.404 148.602 1.00 58.12 ?  163 ARG B CG    1 
ATOM   6904  C  CD    . ARG B 1 163 ? 148.922 145.947 148.819 1.00 56.45 ?  163 ARG B CD    1 
ATOM   6905  N  NE    . ARG B 1 163 ? 148.270 145.366 149.986 1.00 59.28 ?  163 ARG B NE    1 
ATOM   6906  C  CZ    . ARG B 1 163 ? 147.023 144.916 150.005 1.00 58.45 ?  163 ARG B CZ    1 
ATOM   6907  N  NH1   . ARG B 1 163 ? 146.254 144.963 148.929 1.00 56.93 1  163 ARG B NH1   1 
ATOM   6908  N  NH2   . ARG B 1 163 ? 146.534 144.404 151.132 1.00 56.83 ?  163 ARG B NH2   1 
ATOM   6909  N  N     . ARG B 1 164 ? 145.266 149.571 150.978 1.00 55.68 ?  164 ARG B N     1 
ATOM   6910  C  CA    . ARG B 1 164 ? 143.944 149.144 151.399 1.00 50.63 ?  164 ARG B CA    1 
ATOM   6911  C  C     . ARG B 1 164 ? 142.965 149.146 150.229 1.00 50.63 ?  164 ARG B C     1 
ATOM   6912  O  O     . ARG B 1 164 ? 143.206 149.738 149.172 1.00 50.44 ?  164 ARG B O     1 
ATOM   6913  C  CB    . ARG B 1 164 ? 143.417 150.058 152.502 1.00 48.84 ?  164 ARG B CB    1 
ATOM   6914  C  CG    . ARG B 1 164 ? 142.858 151.377 151.991 1.00 45.63 ?  164 ARG B CG    1 
ATOM   6915  C  CD    . ARG B 1 164 ? 141.863 151.975 152.970 1.00 48.21 ?  164 ARG B CD    1 
ATOM   6916  N  NE    . ARG B 1 164 ? 141.231 153.179 152.444 1.00 50.38 ?  164 ARG B NE    1 
ATOM   6917  C  CZ    . ARG B 1 164 ? 140.899 154.232 153.180 1.00 53.94 ?  164 ARG B CZ    1 
ATOM   6918  N  NH1   . ARG B 1 164 ? 141.134 154.268 154.480 1.00 51.60 1  164 ARG B NH1   1 
ATOM   6919  N  NH2   . ARG B 1 164 ? 140.320 155.276 152.594 1.00 53.54 ?  164 ARG B NH2   1 
ATOM   6920  N  N     . GLY B 1 165 ? 141.848 148.462 150.433 1.00 49.03 ?  165 GLY B N     1 
ATOM   6921  C  CA    . GLY B 1 165 ? 140.696 148.550 149.558 1.00 45.13 ?  165 GLY B CA    1 
ATOM   6922  C  C     . GLY B 1 165 ? 139.702 149.571 150.064 1.00 48.10 ?  165 GLY B C     1 
ATOM   6923  O  O     . GLY B 1 165 ? 140.066 150.677 150.477 1.00 48.97 ?  165 GLY B O     1 
ATOM   6924  N  N     . GLU B 1 166 ? 138.428 149.199 150.033 1.00 43.00 ?  166 GLU B N     1 
ATOM   6925  C  CA    . GLU B 1 166 ? 137.383 150.035 150.602 1.00 39.82 ?  166 GLU B CA    1 
ATOM   6926  C  C     . GLU B 1 166 ? 136.951 149.494 151.959 1.00 37.59 ?  166 GLU B C     1 
ATOM   6927  O  O     . GLU B 1 166 ? 136.979 148.286 152.208 1.00 33.46 ?  166 GLU B O     1 
ATOM   6928  C  CB    . GLU B 1 166 ? 136.178 150.118 149.664 1.00 36.97 ?  166 GLU B CB    1 
ATOM   6929  C  CG    . GLU B 1 166 ? 136.302 151.199 148.606 1.00 41.28 ?  166 GLU B CG    1 
ATOM   6930  C  CD    . GLU B 1 166 ? 136.358 152.593 149.197 1.00 42.78 ?  166 GLU B CD    1 
ATOM   6931  O  OE1   . GLU B 1 166 ? 135.718 152.825 150.244 1.00 47.42 ?  166 GLU B OE1   1 
ATOM   6932  O  OE2   . GLU B 1 166 ? 137.044 153.458 148.615 1.00 39.22 -1 166 GLU B OE2   1 
ATOM   6933  N  N     . LEU B 1 167 ? 136.554 150.410 152.843 1.00 30.71 ?  167 LEU B N     1 
ATOM   6934  C  CA    . LEU B 1 167 ? 136.106 150.035 154.176 1.00 23.73 ?  167 LEU B CA    1 
ATOM   6935  C  C     . LEU B 1 167 ? 134.659 149.568 154.207 1.00 29.03 ?  167 LEU B C     1 
ATOM   6936  O  O     . LEU B 1 167 ? 134.221 149.034 155.232 1.00 30.76 ?  167 LEU B O     1 
ATOM   6937  C  CB    . LEU B 1 167 ? 136.278 151.210 155.141 1.00 30.06 ?  167 LEU B CB    1 
ATOM   6938  C  CG    . LEU B 1 167 ? 137.679 151.805 155.291 1.00 26.48 ?  167 LEU B CG    1 
ATOM   6939  C  CD1   . LEU B 1 167 ? 137.758 152.610 156.567 1.00 27.89 ?  167 LEU B CD1   1 
ATOM   6940  C  CD2   . LEU B 1 167 ? 138.738 150.720 155.286 1.00 26.02 ?  167 LEU B CD2   1 
ATOM   6941  N  N     . VAL B 1 168 ? 133.912 149.753 153.124 1.00 29.42 ?  168 VAL B N     1 
ATOM   6942  C  CA    . VAL B 1 168 ? 132.520 149.322 153.074 1.00 22.91 ?  168 VAL B CA    1 
ATOM   6943  C  C     . VAL B 1 168 ? 132.469 147.854 152.679 1.00 26.85 ?  168 VAL B C     1 
ATOM   6944  O  O     . VAL B 1 168 ? 133.118 147.433 151.714 1.00 28.67 ?  168 VAL B O     1 
ATOM   6945  C  CB    . VAL B 1 168 ? 131.715 150.190 152.095 1.00 27.41 ?  168 VAL B CB    1 
ATOM   6946  C  CG1   . VAL B 1 168 ? 130.237 149.859 152.194 1.00 28.93 ?  168 VAL B CG1   1 
ATOM   6947  C  CG2   . VAL B 1 168 ? 131.955 151.661 152.377 1.00 27.27 ?  168 VAL B CG2   1 
ATOM   6948  N  N     . SER B 1 169 ? 131.696 147.069 153.430 1.00 35.86 ?  169 SER B N     1 
ATOM   6949  C  CA    . SER B 1 169 ? 131.637 145.631 153.196 1.00 37.59 ?  169 SER B CA    1 
ATOM   6950  C  C     . SER B 1 169 ? 130.696 145.284 152.047 1.00 36.82 ?  169 SER B C     1 
ATOM   6951  O  O     . SER B 1 169 ? 131.064 144.533 151.139 1.00 34.09 ?  169 SER B O     1 
ATOM   6952  C  CB    . SER B 1 169 ? 131.206 144.912 154.476 1.00 31.71 ?  169 SER B CB    1 
ATOM   6953  O  OG    . SER B 1 169 ? 131.220 143.505 154.301 1.00 34.78 ?  169 SER B OG    1 
ATOM   6954  N  N     . CYS B 1 170 ? 129.478 145.819 152.072 1.00 31.77 ?  170 CYS B N     1 
ATOM   6955  C  CA    . CYS B 1 170 ? 128.427 145.410 151.153 1.00 26.64 ?  170 CYS B CA    1 
ATOM   6956  C  C     . CYS B 1 170 ? 127.931 146.595 150.338 1.00 25.35 ?  170 CYS B C     1 
ATOM   6957  O  O     . CYS B 1 170 ? 127.865 147.724 150.835 1.00 24.91 ?  170 CYS B O     1 
ATOM   6958  C  CB    . CYS B 1 170 ? 127.258 144.779 151.914 1.00 34.42 ?  170 CYS B CB    1 
ATOM   6959  S  SG    . CYS B 1 170 ? 126.666 145.767 153.304 1.00 53.61 ?  170 CYS B SG    1 
ATOM   6960  N  N     . PHE B 1 171 ? 127.583 146.325 149.081 1.00 22.77 ?  171 PHE B N     1 
ATOM   6961  C  CA    . PHE B 1 171 ? 126.995 147.310 148.186 1.00 13.83 ?  171 PHE B CA    1 
ATOM   6962  C  C     . PHE B 1 171 ? 125.755 146.716 147.538 1.00 12.90 ?  171 PHE B C     1 
ATOM   6963  O  O     . PHE B 1 171 ? 125.738 145.535 147.179 1.00 24.47 ?  171 PHE B O     1 
ATOM   6964  C  CB    . PHE B 1 171 ? 127.981 147.749 147.103 1.00 16.07 ?  171 PHE B CB    1 
ATOM   6965  C  CG    . PHE B 1 171 ? 129.304 148.201 147.637 1.00 19.04 ?  171 PHE B CG    1 
ATOM   6966  C  CD1   . PHE B 1 171 ? 129.460 149.478 148.144 1.00 15.01 ?  171 PHE B CD1   1 
ATOM   6967  C  CD2   . PHE B 1 171 ? 130.396 147.351 147.625 1.00 18.02 ?  171 PHE B CD2   1 
ATOM   6968  C  CE1   . PHE B 1 171 ? 130.675 149.894 148.636 1.00 13.11 ?  171 PHE B CE1   1 
ATOM   6969  C  CE2   . PHE B 1 171 ? 131.614 147.766 148.114 1.00 15.58 ?  171 PHE B CE2   1 
ATOM   6970  C  CZ    . PHE B 1 171 ? 131.754 149.039 148.620 1.00 15.68 ?  171 PHE B CZ    1 
ATOM   6971  N  N     . LEU B 1 172 ? 124.720 147.537 147.393 1.00 13.06 ?  172 LEU B N     1 
ATOM   6972  C  CA    . LEU B 1 172 ? 123.454 147.116 146.807 1.00 10.19 ?  172 LEU B CA    1 
ATOM   6973  C  C     . LEU B 1 172 ? 123.148 148.014 145.619 1.00 11.41 ?  172 LEU B C     1 
ATOM   6974  O  O     . LEU B 1 172 ? 123.074 149.238 145.769 1.00 17.26 ?  172 LEU B O     1 
ATOM   6975  C  CB    . LEU B 1 172 ? 122.324 147.181 147.835 1.00 13.81 ?  172 LEU B CB    1 
ATOM   6976  C  CG    . LEU B 1 172 ? 122.344 146.198 149.006 1.00 8.92  ?  172 LEU B CG    1 
ATOM   6977  C  CD1   . LEU B 1 172 ? 123.244 146.698 150.125 1.00 10.47 ?  172 LEU B CD1   1 
ATOM   6978  C  CD2   . LEU B 1 172 ? 120.936 145.994 149.512 1.00 10.66 ?  172 LEU B CD2   1 
ATOM   6979  N  N     . LEU B 1 173 ? 122.964 147.410 144.450 1.00 17.95 ?  173 LEU B N     1 
ATOM   6980  C  CA    . LEU B 1 173 ? 122.736 148.143 143.214 1.00 9.04  ?  173 LEU B CA    1 
ATOM   6981  C  C     . LEU B 1 173 ? 121.332 147.882 142.687 1.00 14.71 ?  173 LEU B C     1 
ATOM   6982  O  O     . LEU B 1 173 ? 120.849 146.747 142.711 1.00 20.11 ?  173 LEU B O     1 
ATOM   6983  C  CB    . LEU B 1 173 ? 123.757 147.758 142.143 1.00 13.46 ?  173 LEU B CB    1 
ATOM   6984  C  CG    . LEU B 1 173 ? 125.240 147.796 142.507 1.00 18.36 ?  173 LEU B CG    1 
ATOM   6985  C  CD1   . LEU B 1 173 ? 126.071 147.399 141.301 1.00 21.69 ?  173 LEU B CD1   1 
ATOM   6986  C  CD2   . LEU B 1 173 ? 125.638 149.173 143.010 1.00 20.29 ?  173 LEU B CD2   1 
ATOM   6987  N  N     . GLU B 1 174 ? 120.686 148.943 142.215 1.00 23.41 ?  174 GLU B N     1 
ATOM   6988  C  CA    . GLU B 1 174 ? 119.425 148.830 141.498 1.00 20.21 ?  174 GLU B CA    1 
ATOM   6989  C  C     . GLU B 1 174 ? 119.704 148.867 140.001 1.00 18.27 ?  174 GLU B C     1 
ATOM   6990  O  O     . GLU B 1 174 ? 120.358 149.791 139.510 1.00 27.43 ?  174 GLU B O     1 
ATOM   6991  C  CB    . GLU B 1 174 ? 118.475 149.961 141.890 1.00 23.89 ?  174 GLU B CB    1 
ATOM   6992  C  CG    . GLU B 1 174 ? 117.828 149.794 143.252 1.00 18.30 ?  174 GLU B CG    1 
ATOM   6993  C  CD    . GLU B 1 174 ? 116.323 149.660 143.166 1.00 21.69 ?  174 GLU B CD    1 
ATOM   6994  O  OE1   . GLU B 1 174 ? 115.834 149.039 142.201 1.00 28.18 ?  174 GLU B OE1   1 
ATOM   6995  O  OE2   . GLU B 1 174 ? 115.628 150.176 144.064 1.00 24.53 -1 174 GLU B OE2   1 
ATOM   6996  N  N     . VAL B 1 175 ? 119.210 147.863 139.282 1.00 16.95 ?  175 VAL B N     1 
ATOM   6997  C  CA    . VAL B 1 175 ? 119.444 147.728 137.849 1.00 18.41 ?  175 VAL B CA    1 
ATOM   6998  C  C     . VAL B 1 175 ? 118.154 148.075 137.121 1.00 17.16 ?  175 VAL B C     1 
ATOM   6999  O  O     . VAL B 1 175 ? 117.140 147.383 137.273 1.00 13.81 ?  175 VAL B O     1 
ATOM   7000  C  CB    . VAL B 1 175 ? 119.918 146.313 137.484 1.00 19.90 ?  175 VAL B CB    1 
ATOM   7001  C  CG1   . VAL B 1 175 ? 120.552 146.303 136.101 1.00 14.27 ?  175 VAL B CG1   1 
ATOM   7002  C  CG2   . VAL B 1 175 ? 120.891 145.797 138.529 1.00 14.16 ?  175 VAL B CG2   1 
ATOM   7003  N  N     . ASN B 1 176 ? 118.193 149.142 136.329 1.00 18.38 ?  176 ASN B N     1 
ATOM   7004  C  CA    . ASN B 1 176 ? 117.042 149.528 135.530 1.00 19.52 ?  176 ASN B CA    1 
ATOM   7005  C  C     . ASN B 1 176 ? 116.940 148.649 134.287 1.00 20.93 ?  176 ASN B C     1 
ATOM   7006  O  O     . ASN B 1 176 ? 117.905 148.009 133.862 1.00 19.66 ?  176 ASN B O     1 
ATOM   7007  C  CB    . ASN B 1 176 ? 117.127 151.000 135.131 1.00 18.09 ?  176 ASN B CB    1 
ATOM   7008  C  CG    . ASN B 1 176 ? 115.780 151.686 135.150 1.00 19.52 ?  176 ASN B CG    1 
ATOM   7009  O  OD1   . ASN B 1 176 ? 114.738 151.032 135.157 1.00 27.15 ?  176 ASN B OD1   1 
ATOM   7010  N  ND2   . ASN B 1 176 ? 115.792 153.013 135.156 1.00 21.83 ?  176 ASN B ND2   1 
ATOM   7011  N  N     . ASP B 1 177 ? 115.744 148.633 133.698 1.00 25.27 ?  177 ASP B N     1 
ATOM   7012  C  CA    . ASP B 1 177 ? 115.436 147.752 132.572 1.00 22.19 ?  177 ASP B CA    1 
ATOM   7013  C  C     . ASP B 1 177 ? 115.904 148.409 131.276 1.00 23.70 ?  177 ASP B C     1 
ATOM   7014  O  O     . ASP B 1 177 ? 115.128 148.989 130.511 1.00 26.99 ?  177 ASP B O     1 
ATOM   7015  C  CB    . ASP B 1 177 ? 113.947 147.436 132.540 1.00 18.71 ?  177 ASP B CB    1 
ATOM   7016  C  CG    . ASP B 1 177 ? 113.571 146.516 131.403 1.00 26.22 ?  177 ASP B CG    1 
ATOM   7017  O  OD1   . ASP B 1 177 ? 114.361 145.604 131.088 1.00 30.83 ?  177 ASP B OD1   1 
ATOM   7018  O  OD2   . ASP B 1 177 ? 112.481 146.706 130.825 1.00 29.50 -1 177 ASP B OD2   1 
ATOM   7019  N  N     . SER B 1 178 ? 117.208 148.311 131.028 1.00 19.01 ?  178 SER B N     1 
ATOM   7020  C  CA    . SER B 1 178 ? 117.794 148.817 129.797 1.00 18.37 ?  178 SER B CA    1 
ATOM   7021  C  C     . SER B 1 178 ? 119.176 148.205 129.619 1.00 16.76 ?  178 SER B C     1 
ATOM   7022  O  O     . SER B 1 178 ? 119.818 147.806 130.592 1.00 23.35 ?  178 SER B O     1 
ATOM   7023  C  CB    . SER B 1 178 ? 117.882 150.347 129.796 1.00 14.28 ?  178 SER B CB    1 
ATOM   7024  O  OG    . SER B 1 178 ? 119.122 150.790 130.313 1.00 19.63 ?  178 SER B OG    1 
ATOM   7025  N  N     . LEU B 1 179 ? 119.618 148.130 128.362 1.00 23.99 ?  179 LEU B N     1 
ATOM   7026  C  CA    . LEU B 1 179 ? 120.952 147.610 128.078 1.00 19.15 ?  179 LEU B CA    1 
ATOM   7027  C  C     . LEU B 1 179 ? 122.030 148.517 128.655 1.00 14.42 ?  179 LEU B C     1 
ATOM   7028  O  O     . LEU B 1 179 ? 123.044 148.035 129.173 1.00 18.64 ?  179 LEU B O     1 
ATOM   7029  C  CB    . LEU B 1 179 ? 121.146 147.444 126.571 1.00 20.55 ?  179 LEU B CB    1 
ATOM   7030  C  CG    . LEU B 1 179 ? 122.468 146.803 126.147 1.00 17.53 ?  179 LEU B CG    1 
ATOM   7031  C  CD1   . LEU B 1 179 ? 122.553 145.369 126.649 1.00 14.12 ?  179 LEU B CD1   1 
ATOM   7032  C  CD2   . LEU B 1 179 ? 122.638 146.862 124.640 1.00 15.45 ?  179 LEU B CD2   1 
ATOM   7033  N  N     . ASN B 1 180 ? 121.836 149.834 128.563 1.00 18.45 ?  180 ASN B N     1 
ATOM   7034  C  CA    . ASN B 1 180 ? 122.785 150.766 129.160 1.00 19.17 ?  180 ASN B CA    1 
ATOM   7035  C  C     . ASN B 1 180 ? 122.879 150.557 130.664 1.00 19.71 ?  180 ASN B C     1 
ATOM   7036  O  O     . ASN B 1 180 ? 123.980 150.520 131.228 1.00 23.44 ?  180 ASN B O     1 
ATOM   7037  C  CB    . ASN B 1 180 ? 122.376 152.205 128.847 1.00 18.93 ?  180 ASN B CB    1 
ATOM   7038  C  CG    . ASN B 1 180 ? 122.756 152.630 127.447 1.00 24.64 ?  180 ASN B CG    1 
ATOM   7039  O  OD1   . ASN B 1 180 ? 123.648 152.050 126.830 1.00 31.55 ?  180 ASN B OD1   1 
ATOM   7040  N  ND2   . ASN B 1 180 ? 122.075 153.646 126.933 1.00 25.83 ?  180 ASN B ND2   1 
ATOM   7041  N  N     . ASP B 1 181 ? 121.733 150.401 131.325 1.00 19.83 ?  181 ASP B N     1 
ATOM   7042  C  CA    . ASP B 1 181 ? 121.727 150.188 132.767 1.00 15.41 ?  181 ASP B CA    1 
ATOM   7043  C  C     . ASP B 1 181 ? 122.324 148.836 133.133 1.00 14.51 ?  181 ASP B C     1 
ATOM   7044  O  O     . ASP B 1 181 ? 123.016 148.717 134.147 1.00 25.19 ?  181 ASP B O     1 
ATOM   7045  C  CB    . ASP B 1 181 ? 120.304 150.319 133.306 1.00 21.97 ?  181 ASP B CB    1 
ATOM   7046  C  CG    . ASP B 1 181 ? 119.787 151.741 133.238 1.00 24.91 ?  181 ASP B CG    1 
ATOM   7047  O  OD1   . ASP B 1 181 ? 120.289 152.593 134.000 1.00 24.60 ?  181 ASP B OD1   1 
ATOM   7048  O  OD2   . ASP B 1 181 ? 118.878 152.009 132.425 1.00 29.14 -1 181 ASP B OD2   1 
ATOM   7049  N  N     . ILE B 1 182 ? 122.074 147.807 132.322 1.00 15.82 ?  182 ILE B N     1 
ATOM   7050  C  CA    . ILE B 1 182 ? 122.650 146.490 132.590 1.00 17.64 ?  182 ILE B CA    1 
ATOM   7051  C  C     . ILE B 1 182 ? 124.169 146.537 132.470 1.00 17.43 ?  182 ILE B C     1 
ATOM   7052  O  O     . ILE B 1 182 ? 124.895 145.999 133.316 1.00 21.16 ?  182 ILE B O     1 
ATOM   7053  C  CB    . ILE B 1 182 ? 122.039 145.439 131.645 1.00 18.63 ?  182 ILE B CB    1 
ATOM   7054  C  CG1   . ILE B 1 182 ? 120.652 145.025 132.137 1.00 15.17 ?  182 ILE B CG1   1 
ATOM   7055  C  CG2   . ILE B 1 182 ? 122.944 144.223 131.529 1.00 20.80 ?  182 ILE B CG2   1 
ATOM   7056  C  CD1   . ILE B 1 182 ? 119.851 144.263 131.116 1.00 16.89 ?  182 ILE B CD1   1 
ATOM   7057  N  N     . SER B 1 183 ? 124.673 147.179 131.414 1.00 17.86 ?  183 SER B N     1 
ATOM   7058  C  CA    . SER B 1 183 ? 126.116 147.297 131.237 1.00 18.73 ?  183 SER B CA    1 
ATOM   7059  C  C     . SER B 1 183 ? 126.743 148.125 132.351 1.00 21.57 ?  183 SER B C     1 
ATOM   7060  O  O     . SER B 1 183 ? 127.824 147.789 132.851 1.00 28.03 ?  183 SER B O     1 
ATOM   7061  C  CB    . SER B 1 183 ? 126.428 147.903 129.871 1.00 15.98 ?  183 SER B CB    1 
ATOM   7062  O  OG    . SER B 1 183 ? 125.822 149.173 129.729 1.00 30.83 ?  183 SER B OG    1 
ATOM   7063  N  N     . ARG B 1 184 ? 126.077 149.209 132.760 1.00 18.88 ?  184 ARG B N     1 
ATOM   7064  C  CA    . ARG B 1 184 ? 126.585 150.004 133.870 1.00 16.57 ?  184 ARG B CA    1 
ATOM   7065  C  C     . ARG B 1 184 ? 126.586 149.205 135.166 1.00 25.25 ?  184 ARG B C     1 
ATOM   7066  O  O     . ARG B 1 184 ? 127.501 149.340 135.982 1.00 29.17 ?  184 ARG B O     1 
ATOM   7067  C  CB    . ARG B 1 184 ? 125.762 151.280 134.030 1.00 15.37 ?  184 ARG B CB    1 
ATOM   7068  C  CG    . ARG B 1 184 ? 126.387 152.285 134.979 1.00 24.71 ?  184 ARG B CG    1 
ATOM   7069  C  CD    . ARG B 1 184 ? 127.803 152.633 134.558 1.00 24.41 ?  184 ARG B CD    1 
ATOM   7070  N  NE    . ARG B 1 184 ? 127.823 153.649 133.515 1.00 31.42 ?  184 ARG B NE    1 
ATOM   7071  C  CZ    . ARG B 1 184 ? 128.922 154.229 133.056 1.00 33.23 ?  184 ARG B CZ    1 
ATOM   7072  N  NH1   . ARG B 1 184 ? 130.119 153.900 133.512 1.00 27.36 1  184 ARG B NH1   1 
ATOM   7073  N  NH2   . ARG B 1 184 ? 128.818 155.162 132.114 1.00 28.64 ?  184 ARG B NH2   1 
ATOM   7074  N  N     . ALA B 1 185 ? 125.564 148.373 135.378 1.00 22.10 ?  185 ALA B N     1 
ATOM   7075  C  CA    . ALA B 1 185 ? 125.527 147.531 136.566 1.00 11.35 ?  185 ALA B CA    1 
ATOM   7076  C  C     . ALA B 1 185 ? 126.668 146.525 136.561 1.00 15.81 ?  185 ALA B C     1 
ATOM   7077  O  O     . ALA B 1 185 ? 127.288 146.276 137.599 1.00 20.15 ?  185 ALA B O     1 
ATOM   7078  C  CB    . ALA B 1 185 ? 124.182 146.814 136.663 1.00 15.68 ?  185 ALA B CB    1 
ATOM   7079  N  N     . ILE B 1 186 ? 126.957 145.933 135.400 1.00 24.17 ?  186 ILE B N     1 
ATOM   7080  C  CA    . ILE B 1 186 ? 128.091 145.016 135.297 1.00 21.97 ?  186 ILE B CA    1 
ATOM   7081  C  C     . ILE B 1 186 ? 129.394 145.744 135.609 1.00 20.56 ?  186 ILE B C     1 
ATOM   7082  O  O     . ILE B 1 186 ? 130.248 145.239 136.353 1.00 26.55 ?  186 ILE B O     1 
ATOM   7083  C  CB    . ILE B 1 186 ? 128.127 144.366 133.901 1.00 26.98 ?  186 ILE B CB    1 
ATOM   7084  C  CG1   . ILE B 1 186 ? 126.910 143.466 133.693 1.00 20.24 ?  186 ILE B CG1   1 
ATOM   7085  C  CG2   . ILE B 1 186 ? 129.409 143.575 133.709 1.00 22.94 ?  186 ILE B CG2   1 
ATOM   7086  C  CD1   . ILE B 1 186 ? 126.579 143.231 132.239 1.00 23.18 ?  186 ILE B CD1   1 
ATOM   7087  N  N     . ASP B 1 187 ? 129.562 146.943 135.047 1.00 22.65 ?  187 ASP B N     1 
ATOM   7088  C  CA    . ASP B 1 187 ? 130.771 147.722 135.293 1.00 21.24 ?  187 ASP B CA    1 
ATOM   7089  C  C     . ASP B 1 187 ? 130.921 148.058 136.773 1.00 23.70 ?  187 ASP B C     1 
ATOM   7090  O  O     . ASP B 1 187 ? 132.002 147.906 137.350 1.00 29.52 ?  187 ASP B O     1 
ATOM   7091  C  CB    . ASP B 1 187 ? 130.747 148.998 134.452 1.00 21.82 ?  187 ASP B CB    1 
ATOM   7092  C  CG    . ASP B 1 187 ? 131.739 150.037 134.936 1.00 30.86 ?  187 ASP B CG    1 
ATOM   7093  O  OD1   . ASP B 1 187 ? 132.935 149.706 135.073 1.00 30.90 ?  187 ASP B OD1   1 
ATOM   7094  O  OD2   . ASP B 1 187 ? 131.321 151.188 135.182 1.00 35.86 -1 187 ASP B OD2   1 
ATOM   7095  N  N     . ILE B 1 188 ? 129.836 148.512 137.404 1.00 21.60 ?  188 ILE B N     1 
ATOM   7096  C  CA    . ILE B 1 188 ? 129.889 148.897 138.811 1.00 19.74 ?  188 ILE B CA    1 
ATOM   7097  C  C     . ILE B 1 188 ? 130.128 147.677 139.692 1.00 21.48 ?  188 ILE B C     1 
ATOM   7098  O  O     . ILE B 1 188 ? 130.829 147.758 140.705 1.00 28.68 ?  188 ILE B O     1 
ATOM   7099  C  CB    . ILE B 1 188 ? 128.604 149.648 139.206 1.00 21.13 ?  188 ILE B CB    1 
ATOM   7100  C  CG1   . ILE B 1 188 ? 128.502 150.969 138.443 1.00 22.43 ?  188 ILE B CG1   1 
ATOM   7101  C  CG2   . ILE B 1 188 ? 128.578 149.928 140.693 1.00 23.49 ?  188 ILE B CG2   1 
ATOM   7102  C  CD1   . ILE B 1 188 ? 127.161 151.649 138.581 1.00 18.85 ?  188 ILE B CD1   1 
ATOM   7103  N  N     . SER B 1 189 ? 129.552 146.531 139.323 1.00 17.21 ?  189 SER B N     1 
ATOM   7104  C  CA    . SER B 1 189 ? 129.802 145.306 140.072 1.00 10.40 ?  189 SER B CA    1 
ATOM   7105  C  C     . SER B 1 189 ? 131.271 144.916 140.006 1.00 22.08 ?  189 SER B C     1 
ATOM   7106  O  O     . SER B 1 189 ? 131.868 144.552 141.025 1.00 23.66 ?  189 SER B O     1 
ATOM   7107  C  CB    . SER B 1 189 ? 128.922 144.177 139.537 1.00 18.67 ?  189 SER B CB    1 
ATOM   7108  O  OG    . SER B 1 189 ? 127.556 144.542 139.567 1.00 25.30 ?  189 SER B OG    1 
ATOM   7109  N  N     . MET B 1 190 ? 131.874 144.994 138.816 1.00 27.49 ?  190 MET B N     1 
ATOM   7110  C  CA    . MET B 1 190 ? 133.302 144.705 138.707 1.00 19.93 ?  190 MET B CA    1 
ATOM   7111  C  C     . MET B 1 190 ? 134.131 145.705 139.502 1.00 19.96 ?  190 MET B C     1 
ATOM   7112  O  O     . MET B 1 190 ? 135.110 145.329 140.154 1.00 24.18 ?  190 MET B O     1 
ATOM   7113  C  CB    . MET B 1 190 ? 133.740 144.694 137.243 1.00 20.87 ?  190 MET B CB    1 
ATOM   7114  C  CG    . MET B 1 190 ? 133.135 143.577 136.419 1.00 22.70 ?  190 MET B CG    1 
ATOM   7115  S  SD    . MET B 1 190 ? 133.886 143.446 134.786 1.00 37.29 ?  190 MET B SD    1 
ATOM   7116  C  CE    . MET B 1 190 ? 132.906 144.624 133.862 1.00 24.55 ?  190 MET B CE    1 
ATOM   7117  N  N     . GLN B 1 191 ? 133.754 146.985 139.461 1.00 19.21 ?  191 GLN B N     1 
ATOM   7118  C  CA    . GLN B 1 191 ? 134.505 148.002 140.192 1.00 23.96 ?  191 GLN B CA    1 
ATOM   7119  C  C     . GLN B 1 191 ? 134.437 147.774 141.696 1.00 23.51 ?  191 GLN B C     1 
ATOM   7120  O  O     . GLN B 1 191 ? 135.444 147.919 142.399 1.00 29.80 ?  191 GLN B O     1 
ATOM   7121  C  CB    . GLN B 1 191 ? 133.985 149.396 139.844 1.00 21.47 ?  191 GLN B CB    1 
ATOM   7122  C  CG    . GLN B 1 191 ? 134.211 149.816 138.403 1.00 20.65 ?  191 GLN B CG    1 
ATOM   7123  C  CD    . GLN B 1 191 ? 135.679 149.932 138.047 1.00 26.80 ?  191 GLN B CD    1 
ATOM   7124  O  OE1   . GLN B 1 191 ? 136.529 150.127 138.916 1.00 30.50 ?  191 GLN B OE1   1 
ATOM   7125  N  NE2   . GLN B 1 191 ? 135.984 149.817 136.761 1.00 25.97 ?  191 GLN B NE2   1 
ATOM   7126  N  N     . LEU B 1 192 ? 133.259 147.423 142.211 1.00 23.86 ?  192 LEU B N     1 
ATOM   7127  C  CA    . LEU B 1 192 ? 133.101 147.231 143.647 1.00 18.39 ?  192 LEU B CA    1 
ATOM   7128  C  C     . LEU B 1 192 ? 133.686 145.909 144.122 1.00 22.39 ?  192 LEU B C     1 
ATOM   7129  O  O     . LEU B 1 192 ? 134.155 145.824 145.262 1.00 33.29 ?  192 LEU B O     1 
ATOM   7130  C  CB    . LEU B 1 192 ? 131.626 147.330 144.031 1.00 19.17 ?  192 LEU B CB    1 
ATOM   7131  C  CG    . LEU B 1 192 ? 130.986 148.709 143.857 1.00 20.72 ?  192 LEU B CG    1 
ATOM   7132  C  CD1   . LEU B 1 192 ? 129.476 148.614 143.958 1.00 20.16 ?  192 LEU B CD1   1 
ATOM   7133  C  CD2   . LEU B 1 192 ? 131.536 149.693 144.875 1.00 21.42 ?  192 LEU B CD2   1 
ATOM   7134  N  N     . SER B 1 193 ? 133.665 144.868 143.284 1.00 19.80 ?  193 SER B N     1 
ATOM   7135  C  CA    . SER B 1 193 ? 134.369 143.640 143.629 1.00 22.09 ?  193 SER B CA    1 
ATOM   7136  C  C     . SER B 1 193 ? 135.876 143.841 143.588 1.00 27.73 ?  193 SER B C     1 
ATOM   7137  O  O     . SER B 1 193 ? 136.608 143.207 144.355 1.00 36.62 ?  193 SER B O     1 
ATOM   7138  C  CB    . SER B 1 193 ? 133.956 142.513 142.688 1.00 24.90 ?  193 SER B CB    1 
ATOM   7139  O  OG    . SER B 1 193 ? 132.585 142.215 142.844 1.00 35.01 ?  193 SER B OG    1 
ATOM   7140  N  N     . LYS B 1 194 ? 136.350 144.709 142.694 1.00 29.29 ?  194 LYS B N     1 
ATOM   7141  C  CA    . LYS B 1 194 ? 137.749 145.113 142.715 1.00 29.16 ?  194 LYS B CA    1 
ATOM   7142  C  C     . LYS B 1 194 ? 138.094 145.799 144.029 1.00 35.14 ?  194 LYS B C     1 
ATOM   7143  O  O     . LYS B 1 194 ? 139.172 145.577 144.593 1.00 39.81 ?  194 LYS B O     1 
ATOM   7144  C  CB    . LYS B 1 194 ? 138.033 146.028 141.524 1.00 26.06 ?  194 LYS B CB    1 
ATOM   7145  C  CG    . LYS B 1 194 ? 139.326 146.809 141.606 1.00 33.46 ?  194 LYS B CG    1 
ATOM   7146  C  CD    . LYS B 1 194 ? 139.363 147.885 140.535 1.00 33.37 ?  194 LYS B CD    1 
ATOM   7147  C  CE    . LYS B 1 194 ? 140.734 148.532 140.444 1.00 34.95 ?  194 LYS B CE    1 
ATOM   7148  N  NZ    . LYS B 1 194 ? 140.764 149.618 139.426 1.00 35.12 1  194 LYS B NZ    1 
ATOM   7149  N  N     . LEU B 1 195 ? 137.183 146.631 144.538 1.00 30.45 ?  195 LEU B N     1 
ATOM   7150  C  CA    . LEU B 1 195 ? 137.360 147.264 145.837 1.00 29.84 ?  195 LEU B CA    1 
ATOM   7151  C  C     . LEU B 1 195 ? 137.204 146.287 146.995 1.00 31.64 ?  195 LEU B C     1 
ATOM   7152  O  O     . LEU B 1 195 ? 137.495 146.658 148.138 1.00 35.04 ?  195 LEU B O     1 
ATOM   7153  C  CB    . LEU B 1 195 ? 136.367 148.416 145.992 1.00 31.01 ?  195 LEU B CB    1 
ATOM   7154  C  CG    . LEU B 1 195 ? 136.565 149.580 145.017 1.00 32.60 ?  195 LEU B CG    1 
ATOM   7155  C  CD1   . LEU B 1 195 ? 135.445 150.598 145.149 1.00 32.68 ?  195 LEU B CD1   1 
ATOM   7156  C  CD2   . LEU B 1 195 ? 137.921 150.235 145.234 1.00 30.72 ?  195 LEU B CD2   1 
ATOM   7157  N  N     . GLY B 1 196 ? 136.748 145.061 146.735 1.00 31.68 ?  196 GLY B N     1 
ATOM   7158  C  CA    . GLY B 1 196 ? 136.659 144.032 147.747 1.00 32.64 ?  196 GLY B CA    1 
ATOM   7159  C  C     . GLY B 1 196 ? 135.285 143.837 148.354 1.00 33.71 ?  196 GLY B C     1 
ATOM   7160  O  O     . GLY B 1 196 ? 135.112 142.913 149.159 1.00 35.13 ?  196 GLY B O     1 
ATOM   7161  N  N     . GLY B 1 197 ? 134.310 144.666 147.997 1.00 30.62 ?  197 GLY B N     1 
ATOM   7162  C  CA    . GLY B 1 197 ? 133.005 144.575 148.617 1.00 26.25 ?  197 GLY B CA    1 
ATOM   7163  C  C     . GLY B 1 197 ? 132.074 143.614 147.902 1.00 22.65 ?  197 GLY B C     1 
ATOM   7164  O  O     . GLY B 1 197 ? 132.139 143.424 146.689 1.00 27.65 ?  197 GLY B O     1 
ATOM   7165  N  N     . GLY B 1 198 ? 131.189 142.997 148.683 1.00 19.98 ?  198 GLY B N     1 
ATOM   7166  C  CA    . GLY B 1 198 ? 130.157 142.145 148.118 1.00 16.72 ?  198 GLY B CA    1 
ATOM   7167  C  C     . GLY B 1 198 ? 129.051 142.989 147.516 1.00 17.83 ?  198 GLY B C     1 
ATOM   7168  O  O     . GLY B 1 198 ? 128.559 143.932 148.146 1.00 21.91 ?  198 GLY B O     1 
ATOM   7169  N  N     . VAL B 1 199 ? 128.655 142.654 146.292 1.00 20.11 ?  199 VAL B N     1 
ATOM   7170  C  CA    . VAL B 1 199 ? 127.719 143.455 145.514 1.00 12.78 ?  199 VAL B CA    1 
ATOM   7171  C  C     . VAL B 1 199 ? 126.413 142.688 145.376 1.00 7.15  ?  199 VAL B C     1 
ATOM   7172  O  O     . VAL B 1 199 ? 126.413 141.514 144.994 1.00 15.02 ?  199 VAL B O     1 
ATOM   7173  C  CB    . VAL B 1 199 ? 128.294 143.805 144.131 1.00 13.70 ?  199 VAL B CB    1 
ATOM   7174  C  CG1   . VAL B 1 199 ? 127.369 144.755 143.397 1.00 16.53 ?  199 VAL B CG1   1 
ATOM   7175  C  CG2   . VAL B 1 199 ? 129.682 144.395 144.270 1.00 11.69 ?  199 VAL B CG2   1 
ATOM   7176  N  N     . SER B 1 200 ? 125.305 143.354 145.686 1.00 13.20 ?  200 SER B N     1 
ATOM   7177  C  CA    . SER B 1 200 ? 123.970 142.810 145.499 1.00 3.98  ?  200 SER B CA    1 
ATOM   7178  C  C     . SER B 1 200 ? 123.231 143.651 144.469 1.00 13.16 ?  200 SER B C     1 
ATOM   7179  O  O     . SER B 1 200 ? 123.283 144.883 144.509 1.00 23.38 ?  200 SER B O     1 
ATOM   7180  C  CB    . SER B 1 200 ? 123.191 142.785 146.816 1.00 10.36 ?  200 SER B CB    1 
ATOM   7181  O  OG    . SER B 1 200 ? 122.070 141.926 146.729 1.00 15.93 ?  200 SER B OG    1 
ATOM   7182  N  N     . LEU B 1 201 ? 122.551 142.984 143.543 1.00 15.98 ?  201 LEU B N     1 
ATOM   7183  C  CA    . LEU B 1 201 ? 121.852 143.651 142.453 1.00 8.21  ?  201 LEU B CA    1 
ATOM   7184  C  C     . LEU B 1 201 ? 120.394 143.223 142.437 1.00 7.83  ?  201 LEU B C     1 
ATOM   7185  O  O     . LEU B 1 201 ? 120.092 142.026 142.475 1.00 14.96 ?  201 LEU B O     1 
ATOM   7186  C  CB    . LEU B 1 201 ? 122.507 143.338 141.107 1.00 14.50 ?  201 LEU B CB    1 
ATOM   7187  C  CG    . LEU B 1 201 ? 123.988 143.698 140.994 1.00 19.27 ?  201 LEU B CG    1 
ATOM   7188  C  CD1   . LEU B 1 201 ? 124.849 142.446 141.042 1.00 16.44 ?  201 LEU B CD1   1 
ATOM   7189  C  CD2   . LEU B 1 201 ? 124.249 144.491 139.725 1.00 17.08 ?  201 LEU B CD2   1 
ATOM   7190  N  N     . ASN B 1 202 ? 119.498 144.203 142.370 1.00 13.30 ?  202 ASN B N     1 
ATOM   7191  C  CA    . ASN B 1 202 ? 118.067 143.954 142.253 1.00 4.34  ?  202 ASN B CA    1 
ATOM   7192  C  C     . ASN B 1 202 ? 117.728 143.810 140.774 1.00 19.44 ?  202 ASN B C     1 
ATOM   7193  O  O     . ASN B 1 202 ? 117.829 144.774 140.009 1.00 25.78 ?  202 ASN B O     1 
ATOM   7194  C  CB    . ASN B 1 202 ? 117.267 145.084 142.893 1.00 8.57  ?  202 ASN B CB    1 
ATOM   7195  C  CG    . ASN B 1 202 ? 115.827 144.701 143.158 1.00 9.79  ?  202 ASN B CG    1 
ATOM   7196  O  OD1   . ASN B 1 202 ? 115.495 143.522 143.263 1.00 17.92 ?  202 ASN B OD1   1 
ATOM   7197  N  ND2   . ASN B 1 202 ? 114.960 145.700 143.265 1.00 12.16 ?  202 ASN B ND2   1 
ATOM   7198  N  N     . LEU B 1 203 ? 117.327 142.606 140.372 1.00 12.94 ?  203 LEU B N     1 
ATOM   7199  C  CA    . LEU B 1 203 ? 116.987 142.320 138.987 1.00 9.62  ?  203 LEU B CA    1 
ATOM   7200  C  C     . LEU B 1 203 ? 115.486 142.326 138.739 1.00 12.21 ?  203 LEU B C     1 
ATOM   7201  O  O     . LEU B 1 203 ? 115.043 141.892 137.672 1.00 17.15 ?  203 LEU B O     1 
ATOM   7202  C  CB    . LEU B 1 203 ? 117.583 140.974 138.569 1.00 15.46 ?  203 LEU B CB    1 
ATOM   7203  C  CG    . LEU B 1 203 ? 119.089 140.804 138.779 1.00 15.40 ?  203 LEU B CG    1 
ATOM   7204  C  CD1   . LEU B 1 203 ? 119.580 139.535 138.107 1.00 14.42 ?  203 LEU B CD1   1 
ATOM   7205  C  CD2   . LEU B 1 203 ? 119.852 142.013 138.264 1.00 15.77 ?  203 LEU B CD2   1 
ATOM   7206  N  N     . SER B 1 204 ? 114.694 142.814 139.697 1.00 15.54 ?  204 SER B N     1 
ATOM   7207  C  CA    . SER B 1 204 ? 113.244 142.771 139.573 1.00 10.71 ?  204 SER B CA    1 
ATOM   7208  C  C     . SER B 1 204 ? 112.705 143.764 138.553 1.00 20.34 ?  204 SER B C     1 
ATOM   7209  O  O     . SER B 1 204 ? 111.606 143.553 138.028 1.00 23.52 ?  204 SER B O     1 
ATOM   7210  C  CB    . SER B 1 204 ? 112.595 143.034 140.932 1.00 8.35  ?  204 SER B CB    1 
ATOM   7211  O  OG    . SER B 1 204 ? 113.063 142.116 141.903 1.00 20.64 ?  204 SER B OG    1 
ATOM   7212  N  N     . LYS B 1 205 ? 113.443 144.835 138.263 1.00 22.11 ?  205 LYS B N     1 
ATOM   7213  C  CA    . LYS B 1 205 ? 113.004 145.788 137.254 1.00 16.32 ?  205 LYS B CA    1 
ATOM   7214  C  C     . LYS B 1 205 ? 113.270 145.304 135.837 1.00 15.37 ?  205 LYS B C     1 
ATOM   7215  O  O     . LYS B 1 205 ? 112.575 145.736 134.912 1.00 26.69 ?  205 LYS B O     1 
ATOM   7216  C  CB    . LYS B 1 205 ? 113.684 147.140 137.473 1.00 18.23 ?  205 LYS B CB    1 
ATOM   7217  C  CG    . LYS B 1 205 ? 113.182 147.878 138.698 1.00 15.88 ?  205 LYS B CG    1 
ATOM   7218  C  CD    . LYS B 1 205 ? 113.834 149.239 138.830 1.00 21.18 ?  205 LYS B CD    1 
ATOM   7219  C  CE    . LYS B 1 205 ? 113.125 150.083 139.872 1.00 24.74 ?  205 LYS B CE    1 
ATOM   7220  N  NZ    . LYS B 1 205 ? 113.153 149.448 141.217 1.00 17.90 1  205 LYS B NZ    1 
ATOM   7221  N  N     . LEU B 1 206 ? 114.251 144.426 135.649 1.00 19.58 ?  206 LEU B N     1 
ATOM   7222  C  CA    . LEU B 1 206 ? 114.529 143.878 134.329 1.00 19.72 ?  206 LEU B CA    1 
ATOM   7223  C  C     . LEU B 1 206 ? 113.339 143.071 133.832 1.00 20.06 ?  206 LEU B C     1 
ATOM   7224  O  O     . LEU B 1 206 ? 112.772 142.260 134.571 1.00 24.64 ?  206 LEU B O     1 
ATOM   7225  C  CB    . LEU B 1 206 ? 115.777 143.002 134.374 1.00 19.51 ?  206 LEU B CB    1 
ATOM   7226  C  CG    . LEU B 1 206 ? 117.042 143.658 134.922 1.00 18.70 ?  206 LEU B CG    1 
ATOM   7227  C  CD1   . LEU B 1 206 ? 118.151 142.633 135.041 1.00 19.93 ?  206 LEU B CD1   1 
ATOM   7228  C  CD2   . LEU B 1 206 ? 117.466 144.807 134.031 1.00 22.12 ?  206 LEU B CD2   1 
ATOM   7229  N  N     . ARG B 1 207 ? 112.962 143.293 132.577 1.00 26.04 ?  207 ARG B N     1 
ATOM   7230  C  CA    . ARG B 1 207 ? 111.823 142.582 132.019 1.00 23.84 ?  207 ARG B CA    1 
ATOM   7231  C  C     . ARG B 1 207 ? 112.156 141.109 131.814 1.00 25.07 ?  207 ARG B C     1 
ATOM   7232  O  O     . ARG B 1 207 ? 113.308 140.731 131.581 1.00 30.59 ?  207 ARG B O     1 
ATOM   7233  C  CB    . ARG B 1 207 ? 111.379 143.221 130.704 1.00 22.30 ?  207 ARG B CB    1 
ATOM   7234  C  CG    . ARG B 1 207 ? 112.440 143.309 129.628 1.00 26.52 ?  207 ARG B CG    1 
ATOM   7235  C  CD    . ARG B 1 207 ? 111.945 144.166 128.474 1.00 24.61 ?  207 ARG B CD    1 
ATOM   7236  N  NE    . ARG B 1 207 ? 112.138 145.588 128.723 1.00 25.92 ?  207 ARG B NE    1 
ATOM   7237  C  CZ    . ARG B 1 207 ? 112.227 146.510 127.775 1.00 23.22 ?  207 ARG B CZ    1 
ATOM   7238  N  NH1   . ARG B 1 207 ? 112.124 146.195 126.494 1.00 26.34 1  207 ARG B NH1   1 
ATOM   7239  N  NH2   . ARG B 1 207 ? 112.422 147.779 128.119 1.00 20.80 ?  207 ARG B NH2   1 
ATOM   7240  N  N     . ALA B 1 208 ? 111.126 140.275 131.910 1.00 29.42 ?  208 ALA B N     1 
ATOM   7241  C  CA    . ALA B 1 208 ? 111.308 138.833 131.910 1.00 21.81 ?  208 ALA B CA    1 
ATOM   7242  C  C     . ALA B 1 208 ? 111.655 138.324 130.513 1.00 28.96 ?  208 ALA B C     1 
ATOM   7243  O  O     . ALA B 1 208 ? 111.710 139.074 129.535 1.00 34.82 ?  208 ALA B O     1 
ATOM   7244  C  CB    . ALA B 1 208 ? 110.051 138.140 132.429 1.00 23.95 ?  208 ALA B CB    1 
ATOM   7245  N  N     . LYS B 1 209 ? 111.904 137.020 130.436 1.00 28.19 ?  209 LYS B N     1 
ATOM   7246  C  CA    . LYS B 1 209 ? 112.187 136.381 129.161 1.00 24.45 ?  209 LYS B CA    1 
ATOM   7247  C  C     . LYS B 1 209 ? 110.949 136.400 128.273 1.00 31.93 ?  209 LYS B C     1 
ATOM   7248  O  O     . LYS B 1 209 ? 109.825 136.203 128.741 1.00 34.54 ?  209 LYS B O     1 
ATOM   7249  C  CB    . LYS B 1 209 ? 112.657 134.944 129.380 1.00 27.07 ?  209 LYS B CB    1 
ATOM   7250  C  CG    . LYS B 1 209 ? 113.322 134.316 128.168 1.00 32.28 ?  209 LYS B CG    1 
ATOM   7251  C  CD    . LYS B 1 209 ? 114.154 133.107 128.560 1.00 29.21 ?  209 LYS B CD    1 
ATOM   7252  C  CE    . LYS B 1 209 ? 113.276 131.920 128.918 1.00 32.67 ?  209 LYS B CE    1 
ATOM   7253  N  NZ    . LYS B 1 209 ? 112.045 131.864 128.082 1.00 33.89 1  209 LYS B NZ    1 
ATOM   7254  N  N     . GLY B 1 210 ? 111.163 136.639 126.982 1.00 35.25 ?  210 GLY B N     1 
ATOM   7255  C  CA    . GLY B 1 210 ? 110.060 136.704 126.048 1.00 34.69 ?  210 GLY B CA    1 
ATOM   7256  C  C     . GLY B 1 210 ? 109.344 138.033 126.003 1.00 35.24 ?  210 GLY B C     1 
ATOM   7257  O  O     . GLY B 1 210 ? 108.166 138.081 125.635 1.00 38.95 ?  210 GLY B O     1 
ATOM   7258  N  N     . GLU B 1 211 ? 110.016 139.117 126.372 1.00 33.78 ?  211 GLU B N     1 
ATOM   7259  C  CA    . GLU B 1 211 ? 109.451 140.453 126.283 1.00 33.10 ?  211 GLU B CA    1 
ATOM   7260  C  C     . GLU B 1 211 ? 109.997 141.175 125.054 1.00 37.21 ?  211 GLU B C     1 
ATOM   7261  O  O     . GLU B 1 211 ? 110.932 140.719 124.393 1.00 40.01 ?  211 GLU B O     1 
ATOM   7262  C  CB    . GLU B 1 211 ? 109.739 141.251 127.557 1.00 31.64 ?  211 GLU B CB    1 
ATOM   7263  C  CG    . GLU B 1 211 ? 109.069 140.684 128.793 1.00 33.93 ?  211 GLU B CG    1 
ATOM   7264  C  CD    . GLU B 1 211 ? 108.166 141.686 129.482 1.00 36.00 ?  211 GLU B CD    1 
ATOM   7265  O  OE1   . GLU B 1 211 ? 107.183 142.131 128.853 1.00 39.65 ?  211 GLU B OE1   1 
ATOM   7266  O  OE2   . GLU B 1 211 ? 108.427 142.019 130.655 1.00 32.33 -1 211 GLU B OE2   1 
ATOM   7267  N  N     . ALA B 1 212 ? 109.395 142.321 124.756 1.00 38.34 ?  212 ALA B N     1 
ATOM   7268  C  CA    . ALA B 1 212 ? 109.683 143.049 123.528 1.00 35.63 ?  212 ALA B CA    1 
ATOM   7269  C  C     . ALA B 1 212 ? 110.722 144.136 123.772 1.00 41.57 ?  212 ALA B C     1 
ATOM   7270  O  O     . ALA B 1 212 ? 110.621 144.897 124.739 1.00 44.34 ?  212 ALA B O     1 
ATOM   7271  C  CB    . ALA B 1 212 ? 108.405 143.664 122.959 1.00 38.46 ?  212 ALA B CB    1 
ATOM   7272  N  N     . ILE B 1 213 ? 111.719 144.198 122.895 1.00 40.74 ?  213 ILE B N     1 
ATOM   7273  C  CA    . ILE B 1 213 ? 112.694 145.282 122.871 1.00 43.49 ?  213 ILE B CA    1 
ATOM   7274  C  C     . ILE B 1 213 ? 112.366 146.141 121.656 1.00 41.50 ?  213 ILE B C     1 
ATOM   7275  O  O     . ILE B 1 213 ? 112.831 145.867 120.548 1.00 44.98 ?  213 ILE B O     1 
ATOM   7276  C  CB    . ILE B 1 213 ? 114.131 144.758 122.820 1.00 41.22 ?  213 ILE B CB    1 
ATOM   7277  C  CG1   . ILE B 1 213 ? 114.365 143.729 123.923 1.00 41.47 ?  213 ILE B CG1   1 
ATOM   7278  C  CG2   . ILE B 1 213 ? 115.121 145.906 122.942 1.00 38.15 ?  213 ILE B CG2   1 
ATOM   7279  C  CD1   . ILE B 1 213 ? 115.483 142.762 123.623 1.00 41.34 ?  213 ILE B CD1   1 
ATOM   7280  N  N     . LYS B 1 214 ? 111.571 147.188 121.867 1.00 46.02 ?  214 LYS B N     1 
ATOM   7281  C  CA    . LYS B 1 214 ? 111.117 148.082 120.802 1.00 46.63 ?  214 LYS B CA    1 
ATOM   7282  C  C     . LYS B 1 214 ? 110.342 147.321 119.725 1.00 52.94 ?  214 LYS B C     1 
ATOM   7283  O  O     . LYS B 1 214 ? 110.767 147.198 118.574 1.00 55.44 ?  214 LYS B O     1 
ATOM   7284  C  CB    . LYS B 1 214 ? 112.286 148.860 120.192 1.00 48.06 ?  214 LYS B CB    1 
ATOM   7285  C  CG    . LYS B 1 214 ? 112.406 150.286 120.701 1.00 49.74 ?  214 LYS B CG    1 
ATOM   7286  C  CD    . LYS B 1 214 ? 113.842 150.779 120.668 1.00 49.95 ?  214 LYS B CD    1 
ATOM   7287  C  CE    . LYS B 1 214 ? 114.588 150.259 119.449 1.00 48.13 ?  214 LYS B CE    1 
ATOM   7288  N  NZ    . LYS B 1 214 ? 116.061 150.250 119.660 1.00 51.60 1  214 LYS B NZ    1 
ATOM   7289  N  N     . ASP B 1 215 ? 109.199 146.774 120.146 1.00 54.72 ?  215 ASP B N     1 
ATOM   7290  C  CA    . ASP B 1 215 ? 108.146 146.286 119.258 1.00 56.27 ?  215 ASP B CA    1 
ATOM   7291  C  C     . ASP B 1 215 ? 108.473 144.961 118.574 1.00 55.86 ?  215 ASP B C     1 
ATOM   7292  O  O     . ASP B 1 215 ? 107.633 144.425 117.843 1.00 57.90 ?  215 ASP B O     1 
ATOM   7293  C  CB    . ASP B 1 215 ? 107.808 147.344 118.202 1.00 56.75 ?  215 ASP B CB    1 
ATOM   7294  C  CG    . ASP B 1 215 ? 106.865 148.410 118.727 1.00 58.77 ?  215 ASP B CG    1 
ATOM   7295  O  OD1   . ASP B 1 215 ? 105.680 148.094 118.959 1.00 57.83 ?  215 ASP B OD1   1 
ATOM   7296  O  OD2   . ASP B 1 215 ? 107.312 149.562 118.910 1.00 57.94 -1 215 ASP B OD2   1 
ATOM   7297  N  N     . VAL B 1 216 ? 109.668 144.417 118.793 1.00 49.80 ?  216 VAL B N     1 
ATOM   7298  C  CA    . VAL B 1 216 ? 109.969 143.060 118.339 1.00 49.24 ?  216 VAL B CA    1 
ATOM   7299  C  C     . VAL B 1 216 ? 109.828 142.153 119.560 1.00 51.37 ?  216 VAL B C     1 
ATOM   7300  O  O     . VAL B 1 216 ? 110.515 142.330 120.567 1.00 54.49 ?  216 VAL B O     1 
ATOM   7301  C  CB    . VAL B 1 216 ? 111.353 142.953 117.690 1.00 49.43 ?  216 VAL B CB    1 
ATOM   7302  C  CG1   . VAL B 1 216 ? 112.219 144.141 118.056 1.00 48.26 ?  216 VAL B CG1   1 
ATOM   7303  C  CG2   . VAL B 1 216 ? 112.038 141.630 118.036 1.00 49.08 ?  216 VAL B CG2   1 
ATOM   7304  N  N     . GLU B 1 217 ? 108.906 141.196 119.482 1.00 49.49 ?  217 GLU B N     1 
ATOM   7305  C  CA    . GLU B 1 217 ? 108.493 140.445 120.657 1.00 48.12 ?  217 GLU B CA    1 
ATOM   7306  C  C     . GLU B 1 217 ? 109.360 139.201 120.845 1.00 47.97 ?  217 GLU B C     1 
ATOM   7307  O  O     . GLU B 1 217 ? 110.077 138.760 119.942 1.00 49.55 ?  217 GLU B O     1 
ATOM   7308  C  CB    . GLU B 1 217 ? 107.021 140.053 120.542 1.00 49.89 ?  217 GLU B CB    1 
ATOM   7309  C  CG    . GLU B 1 217 ? 106.112 141.198 120.126 1.00 50.43 ?  217 GLU B CG    1 
ATOM   7310  C  CD    . GLU B 1 217 ? 105.712 142.078 121.291 1.00 53.17 ?  217 GLU B CD    1 
ATOM   7311  O  OE1   . GLU B 1 217 ? 105.805 141.615 122.447 1.00 52.28 ?  217 GLU B OE1   1 
ATOM   7312  O  OE2   . GLU B 1 217 ? 105.308 143.235 121.052 1.00 49.00 -1 217 GLU B OE2   1 
ATOM   7313  N  N     . ASN B 1 218 ? 109.272 138.634 122.048 1.00 43.64 ?  218 ASN B N     1 
ATOM   7314  C  CA    . ASN B 1 218 ? 110.016 137.434 122.432 1.00 41.92 ?  218 ASN B CA    1 
ATOM   7315  C  C     . ASN B 1 218 ? 111.507 137.607 122.166 1.00 45.22 ?  218 ASN B C     1 
ATOM   7316  O  O     . ASN B 1 218 ? 112.183 136.730 121.623 1.00 46.74 ?  218 ASN B O     1 
ATOM   7317  C  CB    . ASN B 1 218 ? 109.467 136.199 121.719 1.00 43.14 ?  218 ASN B CB    1 
ATOM   7318  C  CG    . ASN B 1 218 ? 108.507 135.409 122.584 1.00 46.85 ?  218 ASN B CG    1 
ATOM   7319  O  OD1   . ASN B 1 218 ? 107.477 135.923 123.019 1.00 45.77 ?  218 ASN B OD1   1 
ATOM   7320  N  ND2   . ASN B 1 218 ? 108.845 134.151 122.845 1.00 48.32 ?  218 ASN B ND2   1 
ATOM   7321  N  N     . ALA B 1 219 ? 112.022 138.764 122.568 1.00 37.53 ?  219 ALA B N     1 
ATOM   7322  C  CA    . ALA B 1 219 ? 113.394 139.160 122.279 1.00 35.07 ?  219 ALA B CA    1 
ATOM   7323  C  C     . ALA B 1 219 ? 114.305 139.145 123.495 1.00 37.31 ?  219 ALA B C     1 
ATOM   7324  O  O     . ALA B 1 219 ? 115.500 138.880 123.357 1.00 35.41 ?  219 ALA B O     1 
ATOM   7325  C  CB    . ALA B 1 219 ? 113.409 140.561 121.659 1.00 36.43 ?  219 ALA B CB    1 
ATOM   7326  N  N     . THR B 1 220 ? 113.774 139.422 124.682 1.00 34.97 ?  220 THR B N     1 
ATOM   7327  C  CA    . THR B 1 220 ? 114.602 139.524 125.873 1.00 31.02 ?  220 THR B CA    1 
ATOM   7328  C  C     . THR B 1 220 ? 115.060 138.151 126.345 1.00 34.50 ?  220 THR B C     1 
ATOM   7329  O  O     . THR B 1 220 ? 114.344 137.154 126.221 1.00 35.03 ?  220 THR B O     1 
ATOM   7330  C  CB    . THR B 1 220 ? 113.843 140.223 127.000 1.00 32.28 ?  220 THR B CB    1 
ATOM   7331  O  OG1   . THR B 1 220 ? 112.736 139.411 127.410 1.00 38.26 ?  220 THR B OG1   1 
ATOM   7332  C  CG2   . THR B 1 220 ? 113.324 141.560 126.527 1.00 32.74 ?  220 THR B CG2   1 
ATOM   7333  N  N     . LYS B 1 221 ? 116.274 138.113 126.890 1.00 32.78 ?  221 LYS B N     1 
ATOM   7334  C  CA    . LYS B 1 221 ? 116.801 136.915 127.525 1.00 29.71 ?  221 LYS B CA    1 
ATOM   7335  C  C     . LYS B 1 221 ? 116.340 136.762 128.966 1.00 31.82 ?  221 LYS B C     1 
ATOM   7336  O  O     . LYS B 1 221 ? 116.618 135.728 129.583 1.00 34.84 ?  221 LYS B O     1 
ATOM   7337  C  CB    . LYS B 1 221 ? 118.332 136.922 127.482 1.00 29.40 ?  221 LYS B CB    1 
ATOM   7338  C  CG    . LYS B 1 221 ? 118.907 136.679 126.104 1.00 30.09 ?  221 LYS B CG    1 
ATOM   7339  C  CD    . LYS B 1 221 ? 120.087 135.727 126.168 1.00 32.86 ?  221 LYS B CD    1 
ATOM   7340  C  CE    . LYS B 1 221 ? 120.533 135.322 124.778 1.00 35.04 ?  221 LYS B CE    1 
ATOM   7341  N  NZ    . LYS B 1 221 ? 119.485 135.611 123.761 1.00 32.52 1  221 LYS B NZ    1 
ATOM   7342  N  N     . GLY B 1 222 ? 115.647 137.755 129.509 1.00 31.02 ?  222 GLY B N     1 
ATOM   7343  C  CA    . GLY B 1 222 ? 115.198 137.696 130.878 1.00 27.64 ?  222 GLY B CA    1 
ATOM   7344  C  C     . GLY B 1 222 ? 116.308 138.013 131.861 1.00 28.06 ?  222 GLY B C     1 
ATOM   7345  O  O     . GLY B 1 222 ? 117.394 138.482 131.507 1.00 31.31 ?  222 GLY B O     1 
ATOM   7346  N  N     . VAL B 1 223 ? 116.014 137.748 133.135 1.00 27.28 ?  223 VAL B N     1 
ATOM   7347  C  CA    . VAL B 1 223 ? 116.992 138.007 134.183 1.00 25.17 ?  223 VAL B CA    1 
ATOM   7348  C  C     . VAL B 1 223 ? 118.099 136.965 134.193 1.00 20.16 ?  223 VAL B C     1 
ATOM   7349  O  O     . VAL B 1 223 ? 119.135 137.184 134.823 1.00 26.46 ?  223 VAL B O     1 
ATOM   7350  C  CB    . VAL B 1 223 ? 116.310 138.084 135.562 1.00 21.99 ?  223 VAL B CB    1 
ATOM   7351  C  CG1   . VAL B 1 223 ? 115.060 138.944 135.489 1.00 22.24 ?  223 VAL B CG1   1 
ATOM   7352  C  CG2   . VAL B 1 223 ? 115.982 136.691 136.079 1.00 22.98 ?  223 VAL B CG2   1 
ATOM   7353  N  N     . VAL B 1 224 ? 117.912 135.833 133.514 1.00 24.17 ?  224 VAL B N     1 
ATOM   7354  C  CA    . VAL B 1 224 ? 118.939 134.795 133.507 1.00 22.49 ?  224 VAL B CA    1 
ATOM   7355  C  C     . VAL B 1 224 ? 120.155 135.217 132.685 1.00 26.27 ?  224 VAL B C     1 
ATOM   7356  O  O     . VAL B 1 224 ? 121.295 134.920 133.060 1.00 30.84 ?  224 VAL B O     1 
ATOM   7357  C  CB    . VAL B 1 224 ? 118.345 133.468 133.006 1.00 27.68 ?  224 VAL B CB    1 
ATOM   7358  C  CG1   . VAL B 1 224 ? 119.433 132.423 132.824 1.00 27.23 ?  224 VAL B CG1   1 
ATOM   7359  C  CG2   . VAL B 1 224 ? 117.294 132.971 133.981 1.00 26.03 ?  224 VAL B CG2   1 
ATOM   7360  N  N     . GLY B 1 225 ? 119.950 135.907 131.561 1.00 22.82 ?  225 GLY B N     1 
ATOM   7361  C  CA    . GLY B 1 225 ? 121.085 136.407 130.799 1.00 18.39 ?  225 GLY B CA    1 
ATOM   7362  C  C     . GLY B 1 225 ? 121.889 137.439 131.567 1.00 21.88 ?  225 GLY B C     1 
ATOM   7363  O  O     . GLY B 1 225 ? 123.124 137.402 131.578 1.00 34.08 ?  225 GLY B O     1 
ATOM   7364  N  N     . VAL B 1 226 ? 121.198 138.373 132.225 1.00 19.13 ?  226 VAL B N     1 
ATOM   7365  C  CA    . VAL B 1 226 ? 121.878 139.341 133.077 1.00 19.93 ?  226 VAL B CA    1 
ATOM   7366  C  C     . VAL B 1 226 ? 122.568 138.636 134.231 1.00 19.06 ?  226 VAL B C     1 
ATOM   7367  O  O     . VAL B 1 226 ? 123.643 139.054 134.673 1.00 23.03 ?  226 VAL B O     1 
ATOM   7368  C  CB    . VAL B 1 226 ? 120.882 140.404 133.579 1.00 17.08 ?  226 VAL B CB    1 
ATOM   7369  C  CG1   . VAL B 1 226 ? 121.625 141.593 134.168 1.00 22.26 ?  226 VAL B CG1   1 
ATOM   7370  C  CG2   . VAL B 1 226 ? 119.970 140.840 132.452 1.00 16.72 ?  226 VAL B CG2   1 
ATOM   7371  N  N     . MET B 1 227 ? 121.963 137.562 134.741 1.00 22.71 ?  227 MET B N     1 
ATOM   7372  C  CA    . MET B 1 227 ? 122.588 136.775 135.796 1.00 21.23 ?  227 MET B CA    1 
ATOM   7373  C  C     . MET B 1 227 ? 123.893 136.156 135.322 1.00 21.57 ?  227 MET B C     1 
ATOM   7374  O  O     . MET B 1 227 ? 124.886 136.151 136.052 1.00 27.55 ?  227 MET B O     1 
ATOM   7375  C  CB    . MET B 1 227 ? 121.627 135.688 136.267 1.00 20.01 ?  227 MET B CB    1 
ATOM   7376  C  CG    . MET B 1 227 ? 120.698 136.113 137.375 1.00 16.03 ?  227 MET B CG    1 
ATOM   7377  S  SD    . MET B 1 227 ? 119.735 134.718 137.967 1.00 40.04 ?  227 MET B SD    1 
ATOM   7378  C  CE    . MET B 1 227 ? 120.553 134.429 139.525 1.00 24.27 ?  227 MET B CE    1 
ATOM   7379  N  N     . LYS B 1 228 ? 123.904 135.615 134.104 1.00 22.19 ?  228 LYS B N     1 
ATOM   7380  C  CA    . LYS B 1 228 ? 125.133 135.046 133.555 1.00 22.43 ?  228 LYS B CA    1 
ATOM   7381  C  C     . LYS B 1 228 ? 126.194 136.122 133.356 1.00 22.93 ?  228 LYS B C     1 
ATOM   7382  O  O     . LYS B 1 228 ? 127.378 135.904 133.649 1.00 23.93 ?  228 LYS B O     1 
ATOM   7383  C  CB    . LYS B 1 228 ? 124.838 134.335 132.236 1.00 24.69 ?  228 LYS B CB    1 
ATOM   7384  C  CG    . LYS B 1 228 ? 124.608 132.844 132.374 1.00 29.35 ?  228 LYS B CG    1 
ATOM   7385  C  CD    . LYS B 1 228 ? 123.205 132.474 131.931 1.00 29.88 ?  228 LYS B CD    1 
ATOM   7386  C  CE    . LYS B 1 228 ? 122.968 132.866 130.483 1.00 33.12 ?  228 LYS B CE    1 
ATOM   7387  N  NZ    . LYS B 1 228 ? 121.764 132.200 129.914 1.00 34.24 1  228 LYS B NZ    1 
ATOM   7388  N  N     . LEU B 1 229 ? 125.783 137.291 132.859 1.00 22.47 ?  229 LEU B N     1 
ATOM   7389  C  CA    . LEU B 1 229 ? 126.724 138.395 132.691 1.00 20.86 ?  229 LEU B CA    1 
ATOM   7390  C  C     . LEU B 1 229 ? 127.327 138.806 134.028 1.00 19.28 ?  229 LEU B C     1 
ATOM   7391  O  O     . LEU B 1 229 ? 128.541 139.004 134.142 1.00 25.07 ?  229 LEU B O     1 
ATOM   7392  C  CB    . LEU B 1 229 ? 126.026 139.588 132.039 1.00 23.23 ?  229 LEU B CB    1 
ATOM   7393  C  CG    . LEU B 1 229 ? 125.480 139.421 130.627 1.00 19.52 ?  229 LEU B CG    1 
ATOM   7394  C  CD1   . LEU B 1 229 ? 124.326 140.382 130.423 1.00 20.88 ?  229 LEU B CD1   1 
ATOM   7395  C  CD2   . LEU B 1 229 ? 126.574 139.662 129.606 1.00 17.63 ?  229 LEU B CD2   1 
ATOM   7396  N  N     . LEU B 1 230 ? 126.486 138.935 135.056 1.00 21.75 ?  230 LEU B N     1 
ATOM   7397  C  CA    . LEU B 1 230 ? 126.968 139.316 136.378 1.00 17.81 ?  230 LEU B CA    1 
ATOM   7398  C  C     . LEU B 1 230 ? 127.856 138.234 136.974 1.00 17.83 ?  230 LEU B C     1 
ATOM   7399  O  O     . LEU B 1 230 ? 128.841 138.539 137.651 1.00 28.53 ?  230 LEU B O     1 
ATOM   7400  C  CB    . LEU B 1 230 ? 125.788 139.611 137.301 1.00 19.03 ?  230 LEU B CB    1 
ATOM   7401  C  CG    . LEU B 1 230 ? 124.999 140.886 137.005 1.00 23.50 ?  230 LEU B CG    1 
ATOM   7402  C  CD1   . LEU B 1 230 ? 123.695 140.896 137.783 1.00 24.96 ?  230 LEU B CD1   1 
ATOM   7403  C  CD2   . LEU B 1 230 ? 125.831 142.115 137.328 1.00 20.05 ?  230 LEU B CD2   1 
ATOM   7404  N  N     . ASP B 1 231 ? 127.518 136.965 136.743 1.00 21.74 ?  231 ASP B N     1 
ATOM   7405  C  CA    . ASP B 1 231 ? 128.345 135.873 137.237 1.00 24.81 ?  231 ASP B CA    1 
ATOM   7406  C  C     . ASP B 1 231 ? 129.734 135.915 136.617 1.00 26.22 ?  231 ASP B C     1 
ATOM   7407  O  O     . ASP B 1 231 ? 130.741 135.757 137.318 1.00 32.42 ?  231 ASP B O     1 
ATOM   7408  C  CB    . ASP B 1 231 ? 127.664 134.536 136.946 1.00 26.44 ?  231 ASP B CB    1 
ATOM   7409  C  CG    . ASP B 1 231 ? 128.477 133.353 137.419 1.00 35.82 ?  231 ASP B CG    1 
ATOM   7410  O  OD1   . ASP B 1 231 ? 128.913 133.362 138.587 1.00 38.60 ?  231 ASP B OD1   1 
ATOM   7411  O  OD2   . ASP B 1 231 ? 128.682 132.413 136.623 1.00 35.57 -1 231 ASP B OD2   1 
ATOM   7412  N  N     . ASN B 1 232 ? 129.810 136.148 135.305 1.00 29.25 ?  232 ASN B N     1 
ATOM   7413  C  CA    . ASN B 1 232 ? 131.115 136.273 134.663 1.00 26.54 ?  232 ASN B CA    1 
ATOM   7414  C  C     . ASN B 1 232 ? 131.856 137.515 135.142 1.00 23.51 ?  232 ASN B C     1 
ATOM   7415  O  O     . ASN B 1 232 ? 133.083 137.491 135.294 1.00 31.02 ?  232 ASN B O     1 
ATOM   7416  C  CB    . ASN B 1 232 ? 130.960 136.286 133.145 1.00 29.57 ?  232 ASN B CB    1 
ATOM   7417  C  CG    . ASN B 1 232 ? 131.891 135.309 132.462 1.00 31.72 ?  232 ASN B CG    1 
ATOM   7418  O  OD1   . ASN B 1 232 ? 131.446 134.381 131.788 1.00 31.09 ?  232 ASN B OD1   1 
ATOM   7419  N  ND2   . ASN B 1 232 ? 133.191 135.521 132.616 1.00 30.58 ?  232 ASN B ND2   1 
ATOM   7420  N  N     . ALA B 1 233 ? 131.132 138.612 135.379 1.00 22.25 ?  233 ALA B N     1 
ATOM   7421  C  CA    . ALA B 1 233 ? 131.766 139.826 135.880 1.00 19.36 ?  233 ALA B CA    1 
ATOM   7422  C  C     . ALA B 1 233 ? 132.364 139.610 137.264 1.00 30.42 ?  233 ALA B C     1 
ATOM   7423  O  O     . ALA B 1 233 ? 133.477 140.067 137.547 1.00 37.00 ?  233 ALA B O     1 
ATOM   7424  C  CB    . ALA B 1 233 ? 130.754 140.969 135.903 1.00 21.32 ?  233 ALA B CB    1 
ATOM   7425  N  N     . PHE B 1 234 ? 131.636 138.918 138.141 1.00 26.24 ?  234 PHE B N     1 
ATOM   7426  C  CA    . PHE B 1 234 ? 132.144 138.640 139.480 1.00 18.46 ?  234 PHE B CA    1 
ATOM   7427  C  C     . PHE B 1 234 ? 133.272 137.620 139.448 1.00 23.57 ?  234 PHE B C     1 
ATOM   7428  O  O     . PHE B 1 234 ? 134.187 137.686 140.278 1.00 30.29 ?  234 PHE B O     1 
ATOM   7429  C  CB    . PHE B 1 234 ? 131.009 138.161 140.385 1.00 25.09 ?  234 PHE B CB    1 
ATOM   7430  C  CG    . PHE B 1 234 ? 130.100 139.264 140.847 1.00 21.29 ?  234 PHE B CG    1 
ATOM   7431  C  CD1   . PHE B 1 234 ? 130.590 140.308 141.605 1.00 22.20 ?  234 PHE B CD1   1 
ATOM   7432  C  CD2   . PHE B 1 234 ? 128.757 139.258 140.519 1.00 20.87 ?  234 PHE B CD2   1 
ATOM   7433  C  CE1   . PHE B 1 234 ? 129.760 141.325 142.026 1.00 20.21 ?  234 PHE B CE1   1 
ATOM   7434  C  CE2   . PHE B 1 234 ? 127.923 140.275 140.936 1.00 20.94 ?  234 PHE B CE2   1 
ATOM   7435  C  CZ    . PHE B 1 234 ? 128.426 141.307 141.692 1.00 20.90 ?  234 PHE B CZ    1 
ATOM   7436  N  N     . ARG B 1 235 ? 133.224 136.667 138.513 1.00 29.56 ?  235 ARG B N     1 
ATOM   7437  C  CA    . ARG B 1 235 ? 134.345 135.752 138.338 1.00 26.83 ?  235 ARG B CA    1 
ATOM   7438  C  C     . ARG B 1 235 ? 135.598 136.498 137.902 1.00 28.32 ?  235 ARG B C     1 
ATOM   7439  O  O     . ARG B 1 235 ? 136.699 136.213 138.384 1.00 36.66 ?  235 ARG B O     1 
ATOM   7440  C  CB    . ARG B 1 235 ? 133.988 134.670 137.319 1.00 24.84 ?  235 ARG B CB    1 
ATOM   7441  C  CG    . ARG B 1 235 ? 133.616 133.339 137.935 1.00 32.99 ?  235 ARG B CG    1 
ATOM   7442  C  CD    . ARG B 1 235 ? 133.352 132.288 136.871 1.00 30.46 ?  235 ARG B CD    1 
ATOM   7443  N  NE    . ARG B 1 235 ? 131.964 132.291 136.427 1.00 34.53 ?  235 ARG B NE    1 
ATOM   7444  C  CZ    . ARG B 1 235 ? 131.585 132.452 135.166 1.00 36.67 ?  235 ARG B CZ    1 
ATOM   7445  N  NH1   . ARG B 1 235 ? 132.466 132.633 134.197 1.00 35.53 1  235 ARG B NH1   1 
ATOM   7446  N  NH2   . ARG B 1 235 ? 130.288 132.429 134.871 1.00 32.65 ?  235 ARG B NH2   1 
ATOM   7447  N  N     . TYR B 1 236 ? 135.447 137.459 136.989 1.00 24.71 ?  236 TYR B N     1 
ATOM   7448  C  CA    . TYR B 1 236 ? 136.602 138.203 136.500 1.00 25.51 ?  236 TYR B CA    1 
ATOM   7449  C  C     . TYR B 1 236 ? 137.170 139.110 137.585 1.00 27.63 ?  236 TYR B C     1 
ATOM   7450  O  O     . TYR B 1 236 ? 138.386 139.143 137.809 1.00 28.35 ?  236 TYR B O     1 
ATOM   7451  C  CB    . TYR B 1 236 ? 136.213 139.016 135.268 1.00 22.47 ?  236 TYR B CB    1 
ATOM   7452  C  CG    . TYR B 1 236 ? 137.370 139.747 134.636 1.00 23.31 ?  236 TYR B CG    1 
ATOM   7453  C  CD1   . TYR B 1 236 ? 138.324 139.059 133.902 1.00 21.64 ?  236 TYR B CD1   1 
ATOM   7454  C  CD2   . TYR B 1 236 ? 137.511 141.121 134.773 1.00 24.88 ?  236 TYR B CD2   1 
ATOM   7455  C  CE1   . TYR B 1 236 ? 139.384 139.714 133.321 1.00 24.32 ?  236 TYR B CE1   1 
ATOM   7456  C  CE2   . TYR B 1 236 ? 138.571 141.786 134.192 1.00 17.73 ?  236 TYR B CE2   1 
ATOM   7457  C  CZ    . TYR B 1 236 ? 139.503 141.076 133.468 1.00 20.63 ?  236 TYR B CZ    1 
ATOM   7458  O  OH    . TYR B 1 236 ? 140.563 141.723 132.885 1.00 30.59 ?  236 TYR B OH    1 
ATOM   7459  N  N     . ALA B 1 237 ? 136.305 139.859 138.267 1.00 29.98 ?  237 ALA B N     1 
ATOM   7460  C  CA    . ALA B 1 237 ? 136.722 140.750 139.349 1.00 29.43 ?  237 ALA B CA    1 
ATOM   7461  C  C     . ALA B 1 237 ? 136.657 139.964 140.651 1.00 36.88 ?  237 ALA B C     1 
ATOM   7462  O  O     . ALA B 1 237 ? 135.641 139.950 141.347 1.00 39.03 ?  237 ALA B O     1 
ATOM   7463  C  CB    . ALA B 1 237 ? 135.846 141.995 139.391 1.00 30.69 ?  237 ALA B CB    1 
ATOM   7464  N  N     . ASP B 1 238 ? 137.763 139.302 140.986 1.00 50.17 ?  238 ASP B N     1 
ATOM   7465  C  CA    . ASP B 1 238 ? 137.808 138.435 142.157 1.00 53.56 ?  238 ASP B CA    1 
ATOM   7466  C  C     . ASP B 1 238 ? 138.881 138.883 143.142 1.00 57.82 ?  238 ASP B C     1 
ATOM   7467  O  O     . ASP B 1 238 ? 139.680 138.063 143.608 1.00 57.80 ?  238 ASP B O     1 
ATOM   7468  C  CB    . ASP B 1 238 ? 138.042 136.980 141.736 1.00 52.95 ?  238 ASP B CB    1 
ATOM   7469  C  CG    . ASP B 1 238 ? 139.294 136.807 140.899 1.00 57.45 ?  238 ASP B CG    1 
ATOM   7470  O  OD1   . ASP B 1 238 ? 139.764 137.805 140.313 1.00 57.54 ?  238 ASP B OD1   1 
ATOM   7471  O  OD2   . ASP B 1 238 ? 139.812 135.673 140.833 1.00 56.42 -1 238 ASP B OD2   1 
ATOM   7472  N  N     . GLN B 1 239 ? 138.914 140.181 143.449 1.00 63.48 ?  239 GLN B N     1 
ATOM   7473  C  CA    . GLN B 1 239 ? 139.857 140.747 144.417 1.00 64.82 ?  239 GLN B CA    1 
ATOM   7474  C  C     . GLN B 1 239 ? 141.297 140.378 144.071 1.00 67.35 ?  239 GLN B C     1 
ATOM   7475  O  O     . GLN B 1 239 ? 142.080 139.953 144.924 1.00 66.69 ?  239 GLN B O     1 
ATOM   7476  C  CB    . GLN B 1 239 ? 139.514 140.308 145.842 1.00 64.62 ?  239 GLN B CB    1 
ATOM   7477  C  CG    . GLN B 1 239 ? 138.480 141.173 146.535 1.00 63.82 ?  239 GLN B CG    1 
ATOM   7478  C  CD    . GLN B 1 239 ? 138.762 141.330 148.017 1.00 66.05 ?  239 GLN B CD    1 
ATOM   7479  O  OE1   . GLN B 1 239 ? 137.873 141.169 148.853 1.00 65.31 ?  239 GLN B OE1   1 
ATOM   7480  N  NE2   . GLN B 1 239 ? 140.008 141.648 148.351 1.00 65.72 ?  239 GLN B NE2   1 
ATOM   7481  N  N     . MET B 1 240 ? 141.641 140.545 142.792 1.00 69.45 ?  240 MET B N     1 
ATOM   7482  C  CA    . MET B 1 240 ? 142.973 140.224 142.280 1.00 68.65 ?  240 MET B CA    1 
ATOM   7483  C  C     . MET B 1 240 ? 143.345 138.766 142.538 1.00 69.19 ?  240 MET B C     1 
ATOM   7484  O  O     . MET B 1 240 ? 144.512 138.442 142.770 1.00 69.12 ?  240 MET B O     1 
ATOM   7485  C  CB    . MET B 1 240 ? 144.035 141.161 142.866 1.00 68.32 ?  240 MET B CB    1 
ATOM   7486  C  CG    . MET B 1 240 ? 143.882 142.620 142.456 1.00 68.69 ?  240 MET B CG    1 
ATOM   7487  S  SD    . MET B 1 240 ? 142.199 143.247 142.605 1.00 73.09 ?  240 MET B SD    1 
ATOM   7488  C  CE    . MET B 1 240 ? 142.437 144.962 142.153 1.00 67.85 ?  240 MET B CE    1 
ATOM   7489  N  N     . GLY B 1 241 ? 142.355 137.877 142.501 1.00 67.80 ?  241 GLY B N     1 
ATOM   7490  C  CA    . GLY B 1 241 ? 142.597 136.458 142.664 1.00 68.08 ?  241 GLY B CA    1 
ATOM   7491  C  C     . GLY B 1 241 ? 142.790 135.986 144.087 1.00 70.85 ?  241 GLY B C     1 
ATOM   7492  O  O     . GLY B 1 241 ? 143.127 134.814 144.289 1.00 70.98 ?  241 GLY B O     1 
ATOM   7493  N  N     . GLN B 1 242 ? 142.588 136.853 145.080 1.00 75.83 ?  242 GLN B N     1 
ATOM   7494  C  CA    . GLN B 1 242 ? 142.758 136.458 146.474 1.00 75.30 ?  242 GLN B CA    1 
ATOM   7495  C  C     . GLN B 1 242 ? 141.484 135.850 147.052 1.00 76.57 ?  242 GLN B C     1 
ATOM   7496  O  O     . GLN B 1 242 ? 141.501 134.717 147.543 1.00 76.27 ?  242 GLN B O     1 
ATOM   7497  C  CB    . GLN B 1 242 ? 143.197 137.663 147.311 1.00 74.11 ?  242 GLN B CB    1 
ATOM   7498  C  CG    . GLN B 1 242 ? 144.616 138.128 147.026 1.00 76.09 ?  242 GLN B CG    1 
ATOM   7499  C  CD    . GLN B 1 242 ? 145.182 138.990 148.136 1.00 77.11 ?  242 GLN B CD    1 
ATOM   7500  O  OE1   . GLN B 1 242 ? 144.599 139.097 149.216 1.00 76.41 ?  242 GLN B OE1   1 
ATOM   7501  N  NE2   . GLN B 1 242 ? 146.327 139.612 147.876 1.00 75.63 ?  242 GLN B NE2   1 
ATOM   7502  N  N     . ARG B 1 243 ? 140.378 136.587 147.001 1.00 64.77 ?  243 ARG B N     1 
ATOM   7503  C  CA    . ARG B 1 243 ? 139.082 136.108 147.460 1.00 64.67 ?  243 ARG B CA    1 
ATOM   7504  C  C     . ARG B 1 243 ? 138.144 136.026 146.265 1.00 63.62 ?  243 ARG B C     1 
ATOM   7505  O  O     . ARG B 1 243 ? 138.061 136.972 145.476 1.00 62.13 ?  243 ARG B O     1 
ATOM   7506  C  CB    . ARG B 1 243 ? 138.501 137.030 148.539 1.00 63.04 ?  243 ARG B CB    1 
ATOM   7507  C  CG    . ARG B 1 243 ? 136.978 137.086 148.571 1.00 63.91 ?  243 ARG B CG    1 
ATOM   7508  C  CD    . ARG B 1 243 ? 136.454 138.398 148.002 1.00 63.15 ?  243 ARG B CD    1 
ATOM   7509  N  NE    . ARG B 1 243 ? 135.085 138.673 148.424 1.00 65.04 ?  243 ARG B NE    1 
ATOM   7510  C  CZ    . ARG B 1 243 ? 134.340 139.661 147.949 1.00 62.89 ?  243 ARG B CZ    1 
ATOM   7511  N  NH1   . ARG B 1 243 ? 134.799 140.493 147.027 1.00 59.40 1  243 ARG B NH1   1 
ATOM   7512  N  NH2   . ARG B 1 243 ? 133.102 139.818 148.409 1.00 60.40 ?  243 ARG B NH2   1 
ATOM   7513  N  N     . GLN B 1 244 ? 137.448 134.898 146.134 1.00 61.88 ?  244 GLN B N     1 
ATOM   7514  C  CA    . GLN B 1 244 ? 136.534 134.710 145.015 1.00 62.67 ?  244 GLN B CA    1 
ATOM   7515  C  C     . GLN B 1 244 ? 135.482 135.811 144.997 1.00 61.97 ?  244 GLN B C     1 
ATOM   7516  O  O     . GLN B 1 244 ? 134.899 136.147 146.032 1.00 61.07 ?  244 GLN B O     1 
ATOM   7517  C  CB    . GLN B 1 244 ? 135.860 133.340 145.109 1.00 59.38 ?  244 GLN B CB    1 
ATOM   7518  C  CG    . GLN B 1 244 ? 136.791 132.167 144.853 1.00 59.03 ?  244 GLN B CG    1 
ATOM   7519  C  CD    . GLN B 1 244 ? 136.044 130.908 144.459 1.00 60.67 ?  244 GLN B CD    1 
ATOM   7520  O  OE1   . GLN B 1 244 ? 135.002 130.586 145.029 1.00 61.69 ?  244 GLN B OE1   1 
ATOM   7521  N  NE2   . GLN B 1 244 ? 136.575 130.187 143.478 1.00 59.63 ?  244 GLN B NE2   1 
ATOM   7522  N  N     . GLY B 1 245 ? 135.252 136.381 143.816 1.00 50.30 ?  245 GLY B N     1 
ATOM   7523  C  CA    . GLY B 1 245 ? 134.253 137.419 143.665 1.00 47.08 ?  245 GLY B CA    1 
ATOM   7524  C  C     . GLY B 1 245 ? 132.866 136.927 144.018 1.00 46.51 ?  245 GLY B C     1 
ATOM   7525  O  O     . GLY B 1 245 ? 132.372 135.964 143.425 1.00 46.35 ?  245 GLY B O     1 
ATOM   7526  N  N     . SER B 1 246 ? 132.229 137.579 144.985 1.00 41.79 ?  246 SER B N     1 
ATOM   7527  C  CA    . SER B 1 246 ? 130.932 137.159 145.498 1.00 37.18 ?  246 SER B CA    1 
ATOM   7528  C  C     . SER B 1 246 ? 129.886 138.194 145.112 1.00 35.91 ?  246 SER B C     1 
ATOM   7529  O  O     . SER B 1 246 ? 130.030 139.380 145.430 1.00 30.02 ?  246 SER B O     1 
ATOM   7530  C  CB    . SER B 1 246 ? 130.976 136.978 147.015 1.00 37.49 ?  246 SER B CB    1 
ATOM   7531  O  OG    . SER B 1 246 ? 131.775 135.865 147.372 1.00 43.74 ?  246 SER B OG    1 
ATOM   7532  N  N     . GLY B 1 247 ? 128.835 137.740 144.432 1.00 25.68 ?  247 GLY B N     1 
ATOM   7533  C  CA    . GLY B 1 247 ? 127.737 138.604 144.075 1.00 8.74  ?  247 GLY B CA    1 
ATOM   7534  C  C     . GLY B 1 247 ? 126.417 137.984 144.487 1.00 13.22 ?  247 GLY B C     1 
ATOM   7535  O  O     . GLY B 1 247 ? 126.307 136.780 144.712 1.00 20.58 ?  247 GLY B O     1 
ATOM   7536  N  N     . ALA B 1 248 ? 125.411 138.842 144.595 1.00 14.03 ?  248 ALA B N     1 
ATOM   7537  C  CA    . ALA B 1 248 ? 124.059 138.423 144.921 1.00 14.28 ?  248 ALA B CA    1 
ATOM   7538  C  C     . ALA B 1 248 ? 123.096 139.027 143.915 1.00 10.37 ?  248 ALA B C     1 
ATOM   7539  O  O     . ALA B 1 248 ? 123.238 140.188 143.527 1.00 17.81 ?  248 ALA B O     1 
ATOM   7540  C  CB    . ALA B 1 248 ? 123.666 138.836 146.342 1.00 9.00  ?  248 ALA B CB    1 
ATOM   7541  N  N     . ALA B 1 249 ? 122.129 138.228 143.481 1.00 12.61 ?  249 ALA B N     1 
ATOM   7542  C  CA    . ALA B 1 249 ? 121.039 138.693 142.638 1.00 12.36 ?  249 ALA B CA    1 
ATOM   7543  C  C     . ALA B 1 249 ? 119.737 138.510 143.399 1.00 8.88  ?  249 ALA B C     1 
ATOM   7544  O  O     . ALA B 1 249 ? 119.492 137.441 143.966 1.00 16.83 ?  249 ALA B O     1 
ATOM   7545  C  CB    . ALA B 1 249 ? 120.994 137.934 141.310 1.00 14.14 ?  249 ALA B CB    1 
ATOM   7546  N  N     . TYR B 1 250 ? 118.916 139.552 143.428 1.00 8.30  ?  250 TYR B N     1 
ATOM   7547  C  CA    . TYR B 1 250 ? 117.629 139.507 144.102 1.00 8.18  ?  250 TYR B CA    1 
ATOM   7548  C  C     . TYR B 1 250 ? 116.526 139.690 143.074 1.00 7.77  ?  250 TYR B C     1 
ATOM   7549  O  O     . TYR B 1 250 ? 116.602 140.585 142.225 1.00 13.56 ?  250 TYR B O     1 
ATOM   7550  C  CB    . TYR B 1 250 ? 117.534 140.579 145.186 1.00 7.54  ?  250 TYR B CB    1 
ATOM   7551  C  CG    . TYR B 1 250 ? 118.114 140.149 146.511 1.00 15.50 ?  250 TYR B CG    1 
ATOM   7552  C  CD1   . TYR B 1 250 ? 119.487 140.091 146.701 1.00 3.04  ?  250 TYR B CD1   1 
ATOM   7553  C  CD2   . TYR B 1 250 ? 117.291 139.799 147.572 1.00 12.49 ?  250 TYR B CD2   1 
ATOM   7554  C  CE1   . TYR B 1 250 ? 120.024 139.700 147.906 1.00 0.74  ?  250 TYR B CE1   1 
ATOM   7555  C  CE2   . TYR B 1 250 ? 117.821 139.404 148.784 1.00 7.28  ?  250 TYR B CE2   1 
ATOM   7556  C  CZ    . TYR B 1 250 ? 119.189 139.358 148.945 1.00 8.49  ?  250 TYR B CZ    1 
ATOM   7557  O  OH    . TYR B 1 250 ? 119.724 138.966 150.149 1.00 12.85 ?  250 TYR B OH    1 
ATOM   7558  N  N     . LEU B 1 251 ? 115.511 138.839 143.147 1.00 12.99 ?  251 LEU B N     1 
ATOM   7559  C  CA    . LEU B 1 251 ? 114.367 138.910 142.254 1.00 14.29 ?  251 LEU B CA    1 
ATOM   7560  C  C     . LEU B 1 251 ? 113.088 138.808 143.066 1.00 12.54 ?  251 LEU B C     1 
ATOM   7561  O  O     . LEU B 1 251 ? 112.999 138.007 144.001 1.00 15.58 ?  251 LEU B O     1 
ATOM   7562  C  CB    . LEU B 1 251 ? 114.409 137.797 141.204 1.00 15.25 ?  251 LEU B CB    1 
ATOM   7563  C  CG    . LEU B 1 251 ? 113.525 138.030 139.979 1.00 11.75 ?  251 LEU B CG    1 
ATOM   7564  C  CD1   . LEU B 1 251 ? 114.071 139.177 139.154 1.00 12.25 ?  251 LEU B CD1   1 
ATOM   7565  C  CD2   . LEU B 1 251 ? 113.418 136.770 139.145 1.00 7.68  ?  251 LEU B CD2   1 
ATOM   7566  N  N     . ASN B 1 252 ? 112.104 139.625 142.710 1.00 11.64 ?  252 ASN B N     1 
ATOM   7567  C  CA    . ASN B 1 252 ? 110.795 139.519 143.334 1.00 10.65 ?  252 ASN B CA    1 
ATOM   7568  C  C     . ASN B 1 252 ? 110.136 138.206 142.938 1.00 15.17 ?  252 ASN B C     1 
ATOM   7569  O  O     . ASN B 1 252 ? 110.285 137.733 141.808 1.00 23.08 ?  252 ASN B O     1 
ATOM   7570  C  CB    . ASN B 1 252 ? 109.913 140.700 142.934 1.00 12.48 ?  252 ASN B CB    1 
ATOM   7571  C  CG    . ASN B 1 252 ? 108.855 141.010 143.971 1.00 20.70 ?  252 ASN B CG    1 
ATOM   7572  O  OD1   . ASN B 1 252 ? 107.888 140.266 144.130 1.00 30.12 ?  252 ASN B OD1   1 
ATOM   7573  N  ND2   . ASN B 1 252 ? 109.038 142.109 144.691 1.00 20.44 ?  252 ASN B ND2   1 
ATOM   7574  N  N     . ILE B 1 253 ? 109.405 137.609 143.882 1.00 13.68 ?  253 ILE B N     1 
ATOM   7575  C  CA    . ILE B 1 253 ? 108.765 136.327 143.624 1.00 17.48 ?  253 ILE B CA    1 
ATOM   7576  C  C     . ILE B 1 253 ? 107.637 136.448 142.608 1.00 20.96 ?  253 ILE B C     1 
ATOM   7577  O  O     . ILE B 1 253 ? 107.197 135.435 142.052 1.00 23.60 ?  253 ILE B O     1 
ATOM   7578  C  CB    . ILE B 1 253 ? 108.260 135.709 144.943 1.00 16.66 ?  253 ILE B CB    1 
ATOM   7579  C  CG1   . ILE B 1 253 ? 108.142 134.190 144.810 1.00 16.22 ?  253 ILE B CG1   1 
ATOM   7580  C  CG2   . ILE B 1 253 ? 106.936 136.328 145.358 1.00 13.72 ?  253 ILE B CG2   1 
ATOM   7581  C  CD1   . ILE B 1 253 ? 108.354 133.448 146.101 1.00 16.69 ?  253 ILE B CD1   1 
ATOM   7582  N  N     . PHE B 1 254 ? 107.159 137.660 142.341 1.00 19.04 ?  254 PHE B N     1 
ATOM   7583  C  CA    . PHE B 1 254 ? 106.121 137.883 141.346 1.00 16.79 ?  254 PHE B CA    1 
ATOM   7584  C  C     . PHE B 1 254 ? 106.686 138.151 139.957 1.00 18.10 ?  254 PHE B C     1 
ATOM   7585  O  O     . PHE B 1 254 ? 105.913 138.340 139.014 1.00 25.04 ?  254 PHE B O     1 
ATOM   7586  C  CB    . PHE B 1 254 ? 105.218 139.039 141.780 1.00 23.09 ?  254 PHE B CB    1 
ATOM   7587  C  CG    . PHE B 1 254 ? 104.213 138.654 142.825 1.00 22.28 ?  254 PHE B CG    1 
ATOM   7588  C  CD1   . PHE B 1 254 ? 103.167 137.804 142.516 1.00 22.04 ?  254 PHE B CD1   1 
ATOM   7589  C  CD2   . PHE B 1 254 ? 104.325 139.126 144.120 1.00 26.07 ?  254 PHE B CD2   1 
ATOM   7590  C  CE1   . PHE B 1 254 ? 102.244 137.441 143.477 1.00 24.80 ?  254 PHE B CE1   1 
ATOM   7591  C  CE2   . PHE B 1 254 ? 103.406 138.766 145.086 1.00 27.48 ?  254 PHE B CE2   1 
ATOM   7592  C  CZ    . PHE B 1 254 ? 102.363 137.924 144.762 1.00 21.77 ?  254 PHE B CZ    1 
ATOM   7593  N  N     . HIS B 1 255 ? 108.007 138.183 139.818 1.00 25.56 ?  255 HIS B N     1 
ATOM   7594  C  CA    . HIS B 1 255 ? 108.629 138.247 138.504 1.00 14.87 ?  255 HIS B CA    1 
ATOM   7595  C  C     . HIS B 1 255 ? 108.371 136.953 137.745 1.00 18.41 ?  255 HIS B C     1 
ATOM   7596  O  O     . HIS B 1 255 ? 108.364 135.866 138.328 1.00 27.28 ?  255 HIS B O     1 
ATOM   7597  C  CB    . HIS B 1 255 ? 110.131 138.485 138.651 1.00 17.20 ?  255 HIS B CB    1 
ATOM   7598  C  CG    . HIS B 1 255 ? 110.776 139.087 137.444 1.00 19.61 ?  255 HIS B CG    1 
ATOM   7599  N  ND1   . HIS B 1 255 ? 110.980 138.380 136.278 1.00 17.88 ?  255 HIS B ND1   1 
ATOM   7600  C  CD2   . HIS B 1 255 ? 111.283 140.323 137.227 1.00 14.91 ?  255 HIS B CD2   1 
ATOM   7601  C  CE1   . HIS B 1 255 ? 111.574 139.159 135.393 1.00 16.46 ?  255 HIS B CE1   1 
ATOM   7602  N  NE2   . HIS B 1 255 ? 111.771 140.342 135.944 1.00 11.54 ?  255 HIS B NE2   1 
ATOM   7603  N  N     . ARG B 1 256 ? 108.151 137.071 136.433 1.00 21.76 ?  256 ARG B N     1 
ATOM   7604  C  CA    . ARG B 1 256 ? 107.865 135.885 135.632 1.00 22.18 ?  256 ARG B CA    1 
ATOM   7605  C  C     . ARG B 1 256 ? 109.055 134.934 135.592 1.00 23.41 ?  256 ARG B C     1 
ATOM   7606  O  O     . ARG B 1 256 ? 108.874 133.714 135.515 1.00 25.13 ?  256 ARG B O     1 
ATOM   7607  C  CB    . ARG B 1 256 ? 107.461 136.290 134.214 1.00 22.61 ?  256 ARG B CB    1 
ATOM   7608  C  CG    . ARG B 1 256 ? 107.194 135.113 133.292 1.00 23.62 ?  256 ARG B CG    1 
ATOM   7609  C  CD    . ARG B 1 256 ? 108.046 135.181 132.038 1.00 25.89 ?  256 ARG B CD    1 
ATOM   7610  N  NE    . ARG B 1 256 ? 109.307 134.464 132.179 1.00 27.83 ?  256 ARG B NE    1 
ATOM   7611  C  CZ    . ARG B 1 256 ? 109.427 133.144 132.151 1.00 29.95 ?  256 ARG B CZ    1 
ATOM   7612  N  NH1   . ARG B 1 256 ? 108.376 132.356 131.991 1.00 28.67 1  256 ARG B NH1   1 
ATOM   7613  N  NH2   . ARG B 1 256 ? 110.633 132.600 132.289 1.00 27.86 ?  256 ARG B NH2   1 
ATOM   7614  N  N     . ASP B 1 257 ? 110.270 135.467 135.662 1.00 14.82 ?  257 ASP B N     1 
ATOM   7615  C  CA    . ASP B 1 257 ? 111.482 134.663 135.593 1.00 19.17 ?  257 ASP B CA    1 
ATOM   7616  C  C     . ASP B 1 257 ? 111.820 133.976 136.909 1.00 18.74 ?  257 ASP B C     1 
ATOM   7617  O  O     . ASP B 1 257 ? 112.876 133.339 136.994 1.00 24.95 ?  257 ASP B O     1 
ATOM   7618  C  CB    . ASP B 1 257 ? 112.663 135.533 135.161 1.00 23.39 ?  257 ASP B CB    1 
ATOM   7619  C  CG    . ASP B 1 257 ? 112.645 135.843 133.683 1.00 26.85 ?  257 ASP B CG    1 
ATOM   7620  O  OD1   . ASP B 1 257 ? 111.895 135.175 132.940 1.00 27.01 ?  257 ASP B OD1   1 
ATOM   7621  O  OD2   . ASP B 1 257 ? 113.384 136.754 133.264 1.00 31.26 -1 257 ASP B OD2   1 
ATOM   7622  N  N     . ILE B 1 258 ? 110.943 134.067 137.914 1.00 19.61 ?  258 ILE B N     1 
ATOM   7623  C  CA    . ILE B 1 258 ? 111.290 133.611 139.258 1.00 21.87 ?  258 ILE B CA    1 
ATOM   7624  C  C     . ILE B 1 258 ? 111.669 132.136 139.247 1.00 23.00 ?  258 ILE B C     1 
ATOM   7625  O  O     . ILE B 1 258 ? 112.580 131.711 139.966 1.00 32.37 ?  258 ILE B O     1 
ATOM   7626  C  CB    . ILE B 1 258 ? 110.141 133.902 140.243 1.00 23.55 ?  258 ILE B CB    1 
ATOM   7627  C  CG1   . ILE B 1 258 ? 110.564 133.569 141.675 1.00 21.31 ?  258 ILE B CG1   1 
ATOM   7628  C  CG2   . ILE B 1 258 ? 108.878 133.139 139.865 1.00 20.68 ?  258 ILE B CG2   1 
ATOM   7629  C  CD1   . ILE B 1 258 ? 111.737 134.382 142.168 1.00 19.07 ?  258 ILE B CD1   1 
ATOM   7630  N  N     . ASN B 1 259 ? 110.992 131.333 138.425 1.00 26.15 ?  259 ASN B N     1 
ATOM   7631  C  CA    . ASN B 1 259 ? 111.364 129.928 138.311 1.00 24.53 ?  259 ASN B CA    1 
ATOM   7632  C  C     . ASN B 1 259 ? 112.740 129.782 137.676 1.00 23.29 ?  259 ASN B C     1 
ATOM   7633  O  O     . ASN B 1 259 ? 113.621 129.113 138.228 1.00 26.89 ?  259 ASN B O     1 
ATOM   7634  C  CB    . ASN B 1 259 ? 110.307 129.171 137.508 1.00 24.70 ?  259 ASN B CB    1 
ATOM   7635  C  CG    . ASN B 1 259 ? 109.132 128.739 138.359 1.00 24.50 ?  259 ASN B CG    1 
ATOM   7636  O  OD1   . ASN B 1 259 ? 109.258 127.857 139.207 1.00 26.50 ?  259 ASN B OD1   1 
ATOM   7637  N  ND2   . ASN B 1 259 ? 107.981 129.362 138.138 1.00 30.54 ?  259 ASN B ND2   1 
ATOM   7638  N  N     . ASP B 1 260 ? 112.957 130.441 136.533 1.00 27.76 ?  260 ASP B N     1 
ATOM   7639  C  CA    . ASP B 1 260 ? 114.250 130.359 135.863 1.00 24.59 ?  260 ASP B CA    1 
ATOM   7640  C  C     . ASP B 1 260 ? 115.358 130.870 136.774 1.00 19.53 ?  260 ASP B C     1 
ATOM   7641  O  O     . ASP B 1 260 ? 116.423 130.251 136.885 1.00 27.97 ?  260 ASP B O     1 
ATOM   7642  C  CB    . ASP B 1 260 ? 114.215 131.151 134.557 1.00 23.49 ?  260 ASP B CB    1 
ATOM   7643  C  CG    . ASP B 1 260 ? 113.242 130.573 133.550 1.00 32.69 ?  260 ASP B CG    1 
ATOM   7644  O  OD1   . ASP B 1 260 ? 113.037 129.340 133.558 1.00 33.48 ?  260 ASP B OD1   1 
ATOM   7645  O  OD2   . ASP B 1 260 ? 112.684 131.351 132.749 1.00 33.86 -1 260 ASP B OD2   1 
ATOM   7646  N  N     . PHE B 1 261 ? 115.113 132.005 137.431 1.00 26.81 ?  261 PHE B N     1 
ATOM   7647  C  CA    . PHE B 1 261 ? 115.957 132.493 138.512 1.00 22.12 ?  261 PHE B CA    1 
ATOM   7648  C  C     . PHE B 1 261 ? 116.341 131.361 139.459 1.00 16.07 ?  261 PHE B C     1 
ATOM   7649  O  O     . PHE B 1 261 ? 117.526 131.048 139.633 1.00 21.75 ?  261 PHE B O     1 
ATOM   7650  C  CB    . PHE B 1 261 ? 115.204 133.607 139.251 1.00 10.28 ?  261 PHE B CB    1 
ATOM   7651  C  CG    . PHE B 1 261 ? 116.018 134.330 140.284 1.00 22.77 ?  261 PHE B CG    1 
ATOM   7652  C  CD1   . PHE B 1 261 ? 116.932 135.299 139.913 1.00 20.56 ?  261 PHE B CD1   1 
ATOM   7653  C  CD2   . PHE B 1 261 ? 115.837 134.069 141.632 1.00 23.60 ?  261 PHE B CD2   1 
ATOM   7654  C  CE1   . PHE B 1 261 ? 117.669 135.976 140.863 1.00 15.18 ?  261 PHE B CE1   1 
ATOM   7655  C  CE2   . PHE B 1 261 ? 116.570 134.743 142.585 1.00 15.89 ?  261 PHE B CE2   1 
ATOM   7656  C  CZ    . PHE B 1 261 ? 117.488 135.697 142.199 1.00 15.76 ?  261 PHE B CZ    1 
ATOM   7657  N  N     . LEU B 1 262 ? 115.334 130.701 140.035 1.00 23.93 ?  262 LEU B N     1 
ATOM   7658  C  CA    . LEU B 1 262 ? 115.604 129.602 140.955 1.00 23.77 ?  262 LEU B CA    1 
ATOM   7659  C  C     . LEU B 1 262 ? 116.330 128.466 140.249 1.00 28.49 ?  262 LEU B C     1 
ATOM   7660  O  O     . LEU B 1 262 ? 117.202 127.814 140.836 1.00 30.74 ?  262 LEU B O     1 
ATOM   7661  C  CB    . LEU B 1 262 ? 114.303 129.105 141.577 1.00 27.44 ?  262 LEU B CB    1 
ATOM   7662  C  CG    . LEU B 1 262 ? 113.566 130.111 142.460 1.00 24.56 ?  262 LEU B CG    1 
ATOM   7663  C  CD1   . LEU B 1 262 ? 112.238 129.540 142.921 1.00 26.12 ?  262 LEU B CD1   1 
ATOM   7664  C  CD2   . LEU B 1 262 ? 114.426 130.520 143.642 1.00 23.89 ?  262 LEU B CD2   1 
ATOM   7665  N  N     . ASP B 1 263 ? 116.007 128.236 138.975 1.00 34.07 ?  263 ASP B N     1 
ATOM   7666  C  CA    . ASP B 1 263 ? 116.660 127.172 138.230 1.00 25.65 ?  263 ASP B CA    1 
ATOM   7667  C  C     . ASP B 1 263 ? 118.149 127.425 138.046 1.00 29.95 ?  263 ASP B C     1 
ATOM   7668  O  O     . ASP B 1 263 ? 118.873 126.497 137.671 1.00 38.33 ?  263 ASP B O     1 
ATOM   7669  C  CB    . ASP B 1 263 ? 115.988 126.994 136.868 1.00 30.81 ?  263 ASP B CB    1 
ATOM   7670  C  CG    . ASP B 1 263 ? 114.603 126.387 136.979 1.00 37.05 ?  263 ASP B CG    1 
ATOM   7671  O  OD1   . ASP B 1 263 ? 114.306 125.768 138.022 1.00 36.66 ?  263 ASP B OD1   1 
ATOM   7672  O  OD2   . ASP B 1 263 ? 113.813 126.530 136.023 1.00 35.56 -1 263 ASP B OD2   1 
ATOM   7673  N  N     . THR B 1 264 ? 118.621 128.649 138.296 1.00 33.51 ?  264 THR B N     1 
ATOM   7674  C  CA    . THR B 1 264 ? 120.056 128.896 138.257 1.00 32.04 ?  264 THR B CA    1 
ATOM   7675  C  C     . THR B 1 264 ? 120.795 128.171 139.374 1.00 36.16 ?  264 THR B C     1 
ATOM   7676  O  O     . THR B 1 264 ? 121.999 127.926 139.243 1.00 36.90 ?  264 THR B O     1 
ATOM   7677  C  CB    . THR B 1 264 ? 120.340 130.396 138.335 1.00 33.04 ?  264 THR B CB    1 
ATOM   7678  O  OG1   . THR B 1 264 ? 119.799 130.925 139.552 1.00 36.48 ?  264 THR B OG1   1 
ATOM   7679  C  CG2   . THR B 1 264 ? 119.716 131.117 137.151 1.00 30.51 ?  264 THR B CG2   1 
ATOM   7680  N  N     . LYS B 1 265 ? 120.109 127.818 140.462 1.00 32.38 ?  265 LYS B N     1 
ATOM   7681  C  CA    . LYS B 1 265 ? 120.743 127.165 141.599 1.00 34.15 ?  265 LYS B CA    1 
ATOM   7682  C  C     . LYS B 1 265 ? 120.430 125.678 141.699 1.00 36.53 ?  265 LYS B C     1 
ATOM   7683  O  O     . LYS B 1 265 ? 120.931 125.018 142.614 1.00 39.20 ?  265 LYS B O     1 
ATOM   7684  C  CB    . LYS B 1 265 ? 120.342 127.863 142.901 1.00 33.86 ?  265 LYS B CB    1 
ATOM   7685  C  CG    . LYS B 1 265 ? 121.082 129.163 143.151 1.00 32.96 ?  265 LYS B CG    1 
ATOM   7686  C  CD    . LYS B 1 265 ? 122.581 128.971 143.038 1.00 35.96 ?  265 LYS B CD    1 
ATOM   7687  C  CE    . LYS B 1 265 ? 123.309 130.297 143.108 1.00 34.47 ?  265 LYS B CE    1 
ATOM   7688  N  NZ    . LYS B 1 265 ? 124.745 130.161 142.745 1.00 37.38 1  265 LYS B NZ    1 
ATOM   7689  N  N     . LYS B 1 266 ? 119.618 125.137 140.796 1.00 45.03 ?  266 LYS B N     1 
ATOM   7690  C  CA    . LYS B 1 266 ? 119.365 123.703 140.801 1.00 44.08 ?  266 LYS B CA    1 
ATOM   7691  C  C     . LYS B 1 266 ? 120.634 122.945 140.437 1.00 48.90 ?  266 LYS B C     1 
ATOM   7692  O  O     . LYS B 1 266 ? 121.387 123.352 139.548 1.00 50.53 ?  266 LYS B O     1 
ATOM   7693  C  CB    . LYS B 1 266 ? 118.241 123.354 139.827 1.00 44.10 ?  266 LYS B CB    1 
ATOM   7694  C  CG    . LYS B 1 266 ? 116.847 123.539 140.405 1.00 46.71 ?  266 LYS B CG    1 
ATOM   7695  C  CD    . LYS B 1 266 ? 115.779 123.016 139.461 1.00 48.45 ?  266 LYS B CD    1 
ATOM   7696  C  CE    . LYS B 1 266 ? 114.467 122.783 140.195 1.00 47.44 ?  266 LYS B CE    1 
ATOM   7697  N  NZ    . LYS B 1 266 ? 113.350 122.477 139.260 1.00 49.34 1  266 LYS B NZ    1 
ATOM   7698  N  N     . ILE B 1 267 ? 120.875 121.835 141.139 1.00 56.82 ?  267 ILE B N     1 
ATOM   7699  C  CA    . ILE B 1 267 ? 122.095 121.069 140.915 1.00 59.40 ?  267 ILE B CA    1 
ATOM   7700  C  C     . ILE B 1 267 ? 122.079 120.339 139.577 1.00 59.98 ?  267 ILE B C     1 
ATOM   7701  O  O     . ILE B 1 267 ? 123.128 119.881 139.112 1.00 58.71 ?  267 ILE B O     1 
ATOM   7702  C  CB    . ILE B 1 267 ? 122.344 120.105 142.096 1.00 60.41 ?  267 ILE B CB    1 
ATOM   7703  C  CG1   . ILE B 1 267 ? 121.045 119.466 142.617 1.00 59.80 ?  267 ILE B CG1   1 
ATOM   7704  C  CG2   . ILE B 1 267 ? 123.061 120.830 143.227 1.00 58.18 ?  267 ILE B CG2   1 
ATOM   7705  C  CD1   . ILE B 1 267 ? 120.281 118.595 141.636 1.00 57.74 ?  267 ILE B CD1   1 
ATOM   7706  N  N     . SER B 1 268 ? 120.914 120.222 138.942 1.00 62.10 ?  268 SER B N     1 
ATOM   7707  C  CA    . SER B 1 268 ? 120.783 119.584 137.640 1.00 64.31 ?  268 SER B CA    1 
ATOM   7708  C  C     . SER B 1 268 ? 120.719 120.592 136.499 1.00 65.31 ?  268 SER B C     1 
ATOM   7709  O  O     . SER B 1 268 ? 120.462 120.204 135.356 1.00 66.20 ?  268 SER B O     1 
ATOM   7710  C  CB    . SER B 1 268 ? 119.542 118.691 137.616 1.00 67.03 ?  268 SER B CB    1 
ATOM   7711  O  OG    . SER B 1 268 ? 118.385 119.419 137.993 1.00 64.20 ?  268 SER B OG    1 
ATOM   7712  N  N     . ALA B 1 269 ? 120.942 121.872 136.786 1.00 66.97 ?  269 ALA B N     1 
ATOM   7713  C  CA    . ALA B 1 269 ? 120.825 122.906 135.768 1.00 67.58 ?  269 ALA B CA    1 
ATOM   7714  C  C     . ALA B 1 269 ? 121.917 122.768 134.714 1.00 67.63 ?  269 ALA B C     1 
ATOM   7715  O  O     . ALA B 1 269 ? 123.051 122.378 135.003 1.00 65.97 ?  269 ALA B O     1 
ATOM   7716  C  CB    . ALA B 1 269 ? 120.892 124.292 136.409 1.00 65.51 ?  269 ALA B CB    1 
ATOM   7717  N  N     . ASP B 1 270 ? 121.560 123.096 133.475 1.00 73.26 ?  270 ASP B N     1 
ATOM   7718  C  CA    . ASP B 1 270 ? 122.515 123.071 132.381 1.00 73.45 ?  270 ASP B CA    1 
ATOM   7719  C  C     . ASP B 1 270 ? 123.510 124.222 132.517 1.00 73.74 ?  270 ASP B C     1 
ATOM   7720  O  O     . ASP B 1 270 ? 123.272 125.206 133.223 1.00 74.05 ?  270 ASP B O     1 
ATOM   7721  C  CB    . ASP B 1 270 ? 121.791 123.153 131.037 1.00 73.73 ?  270 ASP B CB    1 
ATOM   7722  C  CG    . ASP B 1 270 ? 122.588 122.536 129.905 1.00 75.07 ?  270 ASP B CG    1 
ATOM   7723  O  OD1   . ASP B 1 270 ? 123.711 123.013 129.636 1.00 75.22 ?  270 ASP B OD1   1 
ATOM   7724  O  OD2   . ASP B 1 270 ? 122.093 121.572 129.284 1.00 74.14 -1 270 ASP B OD2   1 
ATOM   7725  N  N     . GLU B 1 271 ? 124.643 124.086 131.823 1.00 73.75 ?  271 GLU B N     1 
ATOM   7726  C  CA    . GLU B 1 271 ? 125.701 125.085 131.931 1.00 73.72 ?  271 GLU B CA    1 
ATOM   7727  C  C     . GLU B 1 271 ? 125.267 126.441 131.386 1.00 72.95 ?  271 GLU B C     1 
ATOM   7728  O  O     . GLU B 1 271 ? 125.750 127.476 131.856 1.00 72.44 ?  271 GLU B O     1 
ATOM   7729  C  CB    . GLU B 1 271 ? 126.957 124.600 131.207 1.00 72.64 ?  271 GLU B CB    1 
ATOM   7730  C  CG    . GLU B 1 271 ? 127.761 123.575 131.989 1.00 73.86 ?  271 GLU B CG    1 
ATOM   7731  C  CD    . GLU B 1 271 ? 128.305 124.131 133.291 1.00 74.42 ?  271 GLU B CD    1 
ATOM   7732  O  OE1   . GLU B 1 271 ? 128.691 125.318 133.318 1.00 73.57 ?  271 GLU B OE1   1 
ATOM   7733  O  OE2   . GLU B 1 271 ? 128.344 123.380 134.288 1.00 73.53 -1 271 GLU B OE2   1 
ATOM   7734  N  N     . ASP B 1 272 ? 124.365 126.460 130.403 1.00 69.22 ?  272 ASP B N     1 
ATOM   7735  C  CA    . ASP B 1 272 ? 123.887 127.725 129.858 1.00 70.00 ?  272 ASP B CA    1 
ATOM   7736  C  C     . ASP B 1 272 ? 122.931 128.449 130.799 1.00 69.56 ?  272 ASP B C     1 
ATOM   7737  O  O     . ASP B 1 272 ? 122.617 129.618 130.554 1.00 68.28 ?  272 ASP B O     1 
ATOM   7738  C  CB    . ASP B 1 272 ? 123.211 127.493 128.505 1.00 69.68 ?  272 ASP B CB    1 
ATOM   7739  C  CG    . ASP B 1 272 ? 121.857 126.822 128.633 1.00 72.04 ?  272 ASP B CG    1 
ATOM   7740  O  OD1   . ASP B 1 272 ? 121.663 126.037 129.585 1.00 71.80 ?  272 ASP B OD1   1 
ATOM   7741  O  OD2   . ASP B 1 272 ? 120.984 127.078 127.777 1.00 69.21 -1 272 ASP B OD2   1 
ATOM   7742  N  N     . VAL B 1 273 ? 122.458 127.785 131.855 1.00 62.08 ?  273 VAL B N     1 
ATOM   7743  C  CA    . VAL B 1 273 ? 121.566 128.386 132.834 1.00 62.78 ?  273 VAL B CA    1 
ATOM   7744  C  C     . VAL B 1 273 ? 122.211 128.471 134.211 1.00 61.16 ?  273 VAL B C     1 
ATOM   7745  O  O     . VAL B 1 273 ? 122.012 129.453 134.935 1.00 60.96 ?  273 VAL B O     1 
ATOM   7746  C  CB    . VAL B 1 273 ? 120.228 127.617 132.907 1.00 63.68 ?  273 VAL B CB    1 
ATOM   7747  C  CG1   . VAL B 1 273 ? 119.339 128.175 134.010 1.00 61.00 ?  273 VAL B CG1   1 
ATOM   7748  C  CG2   . VAL B 1 273 ? 119.514 127.669 131.566 1.00 62.41 ?  273 VAL B CG2   1 
ATOM   7749  N  N     . ARG B 1 274 ? 122.995 127.461 134.586 1.00 61.27 ?  274 ARG B N     1 
ATOM   7750  C  CA    . ARG B 1 274 ? 123.577 127.405 135.920 1.00 60.75 ?  274 ARG B CA    1 
ATOM   7751  C  C     . ARG B 1 274 ? 124.489 128.600 136.176 1.00 59.70 ?  274 ARG B C     1 
ATOM   7752  O  O     . ARG B 1 274 ? 125.299 128.982 135.326 1.00 62.45 ?  274 ARG B O     1 
ATOM   7753  C  CB    . ARG B 1 274 ? 124.359 126.101 136.099 1.00 62.89 ?  274 ARG B CB    1 
ATOM   7754  C  CG    . ARG B 1 274 ? 125.587 126.221 136.990 1.00 58.68 ?  274 ARG B CG    1 
ATOM   7755  C  CD    . ARG B 1 274 ? 125.792 124.976 137.835 1.00 61.77 ?  274 ARG B CD    1 
ATOM   7756  N  NE    . ARG B 1 274 ? 126.087 123.805 137.019 1.00 65.06 ?  274 ARG B NE    1 
ATOM   7757  C  CZ    . ARG B 1 274 ? 125.371 122.689 137.023 1.00 66.11 ?  274 ARG B CZ    1 
ATOM   7758  N  NH1   . ARG B 1 274 ? 124.309 122.551 137.799 1.00 63.75 1  274 ARG B NH1   1 
ATOM   7759  N  NH2   . ARG B 1 274 ? 125.731 121.684 136.229 1.00 63.75 ?  274 ARG B NH2   1 
ATOM   7760  N  N     . VAL B 1 275 ? 124.342 129.192 137.357 1.00 47.00 ?  275 VAL B N     1 
ATOM   7761  C  CA    . VAL B 1 275 ? 125.192 130.277 137.830 1.00 44.89 ?  275 VAL B CA    1 
ATOM   7762  C  C     . VAL B 1 275 ? 125.747 129.864 139.186 1.00 48.71 ?  275 VAL B C     1 
ATOM   7763  O  O     . VAL B 1 275 ? 124.985 129.459 140.072 1.00 51.14 ?  275 VAL B O     1 
ATOM   7764  C  CB    . VAL B 1 275 ? 124.414 131.601 137.929 1.00 45.84 ?  275 VAL B CB    1 
ATOM   7765  C  CG1   . VAL B 1 275 ? 125.181 132.593 138.757 1.00 45.29 ?  275 VAL B CG1   1 
ATOM   7766  C  CG2   . VAL B 1 275 ? 124.133 132.160 136.544 1.00 43.95 ?  275 VAL B CG2   1 
ATOM   7767  N  N     . LYS B 1 276 ? 127.069 129.964 139.352 1.00 46.32 ?  276 LYS B N     1 
ATOM   7768  C  CA    . LYS B 1 276 ? 127.731 129.353 140.496 1.00 47.39 ?  276 LYS B CA    1 
ATOM   7769  C  C     . LYS B 1 276 ? 128.425 130.325 141.443 1.00 45.61 ?  276 LYS B C     1 
ATOM   7770  O  O     . LYS B 1 276 ? 128.623 129.968 142.610 1.00 51.16 ?  276 LYS B O     1 
ATOM   7771  C  CB    . LYS B 1 276 ? 128.752 128.305 140.021 1.00 48.20 ?  276 LYS B CB    1 
ATOM   7772  C  CG    . LYS B 1 276 ? 130.087 128.870 139.578 1.00 47.46 ?  276 LYS B CG    1 
ATOM   7773  C  CD    . LYS B 1 276 ? 130.809 127.913 138.648 1.00 50.60 ?  276 LYS B CD    1 
ATOM   7774  C  CE    . LYS B 1 276 ? 130.029 127.720 137.358 1.00 49.82 ?  276 LYS B CE    1 
ATOM   7775  N  NZ    . LYS B 1 276 ? 129.559 129.020 136.807 1.00 48.35 1  276 LYS B NZ    1 
ATOM   7776  N  N     . THR B 1 277 ? 128.802 131.522 140.997 1.00 37.24 ?  277 THR B N     1 
ATOM   7777  C  CA    . THR B 1 277 ? 129.436 132.498 141.876 1.00 36.87 ?  277 THR B CA    1 
ATOM   7778  C  C     . THR B 1 277 ? 128.517 133.646 142.264 1.00 38.11 ?  277 THR B C     1 
ATOM   7779  O  O     . THR B 1 277 ? 128.979 134.607 142.889 1.00 42.20 ?  277 THR B O     1 
ATOM   7780  C  CB    . THR B 1 277 ? 130.708 133.069 141.233 1.00 39.89 ?  277 THR B CB    1 
ATOM   7781  O  OG1   . THR B 1 277 ? 130.375 134.215 140.439 1.00 37.56 ?  277 THR B OG1   1 
ATOM   7782  C  CG2   . THR B 1 277 ? 131.385 132.031 140.366 1.00 40.45 ?  277 THR B CG2   1 
ATOM   7783  N  N     . LEU B 1 278 ? 127.238 133.578 141.917 1.00 29.21 ?  278 LEU B N     1 
ATOM   7784  C  CA    . LEU B 1 278 ? 126.282 134.643 142.200 1.00 29.10 ?  278 LEU B CA    1 
ATOM   7785  C  C     . LEU B 1 278 ? 125.182 134.082 143.092 1.00 23.31 ?  278 LEU B C     1 
ATOM   7786  O  O     . LEU B 1 278 ? 124.378 133.256 142.649 1.00 29.21 ?  278 LEU B O     1 
ATOM   7787  C  CB    . LEU B 1 278 ? 125.711 135.213 140.905 1.00 26.18 ?  278 LEU B CB    1 
ATOM   7788  C  CG    . LEU B 1 278 ? 124.790 136.428 140.956 1.00 26.72 ?  278 LEU B CG    1 
ATOM   7789  C  CD1   . LEU B 1 278 ? 125.597 137.703 141.050 1.00 23.26 ?  278 LEU B CD1   1 
ATOM   7790  C  CD2   . LEU B 1 278 ? 123.900 136.447 139.726 1.00 23.82 ?  278 LEU B CD2   1 
ATOM   7791  N  N     . SER B 1 279 ? 125.151 134.530 144.343 1.00 23.24 ?  279 SER B N     1 
ATOM   7792  C  CA    . SER B 1 279 ? 124.085 134.138 145.253 1.00 18.49 ?  279 SER B CA    1 
ATOM   7793  C  C     . SER B 1 279 ? 122.754 134.695 144.769 1.00 19.07 ?  279 SER B C     1 
ATOM   7794  O  O     . SER B 1 279 ? 122.694 135.716 144.081 1.00 29.86 ?  279 SER B O     1 
ATOM   7795  C  CB    . SER B 1 279 ? 124.380 134.636 146.665 1.00 17.19 ?  279 SER B CB    1 
ATOM   7796  O  OG    . SER B 1 279 ? 125.604 134.110 147.146 1.00 23.76 ?  279 SER B OG    1 
ATOM   7797  N  N     . ILE B 1 280 ? 121.673 134.008 145.122 1.00 20.84 ?  280 ILE B N     1 
ATOM   7798  C  CA    . ILE B 1 280 ? 120.341 134.394 144.681 1.00 19.36 ?  280 ILE B CA    1 
ATOM   7799  C  C     . ILE B 1 280 ? 119.478 134.672 145.902 1.00 20.82 ?  280 ILE B C     1 
ATOM   7800  O  O     . ILE B 1 280 ? 119.588 133.989 146.926 1.00 24.93 ?  280 ILE B O     1 
ATOM   7801  C  CB    . ILE B 1 280 ? 119.697 133.326 143.771 1.00 16.70 ?  280 ILE B CB    1 
ATOM   7802  C  CG1   . ILE B 1 280 ? 119.330 132.065 144.550 1.00 22.49 ?  280 ILE B CG1   1 
ATOM   7803  C  CG2   . ILE B 1 280 ? 120.647 132.943 142.663 1.00 25.14 ?  280 ILE B CG2   1 
ATOM   7804  C  CD1   . ILE B 1 280 ? 118.276 131.227 143.857 1.00 21.68 ?  280 ILE B CD1   1 
ATOM   7805  N  N     . GLY B 1 281 ? 118.652 135.704 145.801 1.00 11.91 ?  281 GLY B N     1 
ATOM   7806  C  CA    . GLY B 1 281 ? 117.686 136.010 146.834 1.00 6.43  ?  281 GLY B CA    1 
ATOM   7807  C  C     . GLY B 1 281 ? 116.328 136.266 146.220 1.00 8.98  ?  281 GLY B C     1 
ATOM   7808  O  O     . GLY B 1 281 ? 116.211 136.769 145.105 1.00 18.68 ?  281 GLY B O     1 
ATOM   7809  N  N     . VAL B 1 282 ? 115.292 135.903 146.970 1.00 8.40  ?  282 VAL B N     1 
ATOM   7810  C  CA    . VAL B 1 282 ? 113.912 136.039 146.524 1.00 14.89 ?  282 VAL B CA    1 
ATOM   7811  C  C     . VAL B 1 282 ? 113.189 136.971 147.484 1.00 11.81 ?  282 VAL B C     1 
ATOM   7812  O  O     . VAL B 1 282 ? 113.244 136.780 148.704 1.00 18.21 ?  282 VAL B O     1 
ATOM   7813  C  CB    . VAL B 1 282 ? 113.206 134.673 146.438 1.00 13.09 ?  282 VAL B CB    1 
ATOM   7814  C  CG1   . VAL B 1 282 ? 111.707 134.856 146.323 1.00 15.57 ?  282 VAL B CG1   1 
ATOM   7815  C  CG2   . VAL B 1 282 ? 113.730 133.891 145.251 1.00 19.32 ?  282 VAL B CG2   1 
ATOM   7816  N  N     . VAL B 1 283 ? 112.524 137.980 146.932 1.00 7.35  ?  283 VAL B N     1 
ATOM   7817  C  CA    . VAL B 1 283 ? 111.764 138.948 147.710 1.00 10.05 ?  283 VAL B CA    1 
ATOM   7818  C  C     . VAL B 1 283 ? 110.296 138.556 147.642 1.00 12.37 ?  283 VAL B C     1 
ATOM   7819  O  O     . VAL B 1 283 ? 109.695 138.553 146.561 1.00 22.54 ?  283 VAL B O     1 
ATOM   7820  C  CB    . VAL B 1 283 ? 111.987 140.376 147.193 1.00 6.35  ?  283 VAL B CB    1 
ATOM   7821  C  CG1   . VAL B 1 283 ? 111.283 141.378 148.087 1.00 9.67  ?  283 VAL B CG1   1 
ATOM   7822  C  CG2   . VAL B 1 283 ? 113.474 140.672 147.115 1.00 8.67  ?  283 VAL B CG2   1 
ATOM   7823  N  N     . ILE B 1 284 ? 109.720 138.224 148.791 1.00 17.09 ?  284 ILE B N     1 
ATOM   7824  C  CA    . ILE B 1 284 ? 108.369 137.682 148.879 1.00 17.92 ?  284 ILE B CA    1 
ATOM   7825  C  C     . ILE B 1 284 ? 107.484 138.722 149.561 1.00 17.41 ?  284 ILE B C     1 
ATOM   7826  O  O     . ILE B 1 284 ? 107.613 138.946 150.775 1.00 19.60 ?  284 ILE B O     1 
ATOM   7827  C  CB    . ILE B 1 284 ? 108.345 136.350 149.640 1.00 12.85 ?  284 ILE B CB    1 
ATOM   7828  C  CG1   . ILE B 1 284 ? 109.402 135.397 149.080 1.00 13.68 ?  284 ILE B CG1   1 
ATOM   7829  C  CG2   . ILE B 1 284 ? 106.962 135.725 149.570 1.00 17.19 ?  284 ILE B CG2   1 
ATOM   7830  C  CD1   . ILE B 1 284 ? 109.350 134.011 149.673 1.00 15.71 ?  284 ILE B CD1   1 
ATOM   7831  N  N     . PRO B 1 285 ? 106.582 139.378 148.839 1.00 22.30 ?  285 PRO B N     1 
ATOM   7832  C  CA    . PRO B 1 285 ? 105.579 140.218 149.499 1.00 25.67 ?  285 PRO B CA    1 
ATOM   7833  C  C     . PRO B 1 285 ? 104.570 139.371 150.259 1.00 25.21 ?  285 PRO B C     1 
ATOM   7834  O  O     . PRO B 1 285 ? 104.473 138.155 150.081 1.00 24.82 ?  285 PRO B O     1 
ATOM   7835  C  CB    . PRO B 1 285 ? 104.912 140.964 148.337 1.00 23.16 ?  285 PRO B CB    1 
ATOM   7836  C  CG    . PRO B 1 285 ? 105.865 140.837 147.192 1.00 19.61 ?  285 PRO B CG    1 
ATOM   7837  C  CD    . PRO B 1 285 ? 106.541 139.517 147.375 1.00 16.49 ?  285 PRO B CD    1 
ATOM   7838  N  N     . ASP B 1 286 ? 103.814 140.040 151.133 1.00 29.11 ?  286 ASP B N     1 
ATOM   7839  C  CA    . ASP B 1 286 ? 102.768 139.355 151.884 1.00 23.66 ?  286 ASP B CA    1 
ATOM   7840  C  C     . ASP B 1 286 ? 101.684 138.792 150.978 1.00 30.67 ?  286 ASP B C     1 
ATOM   7841  O  O     . ASP B 1 286 ? 100.993 137.845 151.371 1.00 32.81 ?  286 ASP B O     1 
ATOM   7842  C  CB    . ASP B 1 286 ? 102.148 140.304 152.910 1.00 26.22 ?  286 ASP B CB    1 
ATOM   7843  C  CG    . ASP B 1 286 ? 102.666 140.067 154.312 1.00 37.25 ?  286 ASP B CG    1 
ATOM   7844  O  OD1   . ASP B 1 286 ? 103.874 139.786 154.461 1.00 38.58 ?  286 ASP B OD1   1 
ATOM   7845  O  OD2   . ASP B 1 286 ? 101.868 140.166 155.267 1.00 39.34 -1 286 ASP B OD2   1 
ATOM   7846  N  N     . LYS B 1 287 ? 101.517 139.356 149.778 1.00 33.03 ?  287 LYS B N     1 
ATOM   7847  C  CA    . LYS B 1 287 ? 100.515 138.847 148.849 1.00 25.93 ?  287 LYS B CA    1 
ATOM   7848  C  C     . LYS B 1 287 ? 100.811 137.409 148.445 1.00 26.93 ?  287 LYS B C     1 
ATOM   7849  O  O     . LYS B 1 287 ? 99.894  136.586 148.347 1.00 33.99 ?  287 LYS B O     1 
ATOM   7850  C  CB    . LYS B 1 287 ? 100.441 139.744 147.615 1.00 27.63 ?  287 LYS B CB    1 
ATOM   7851  C  CG    . LYS B 1 287 ? 99.255  139.452 146.714 1.00 27.80 ?  287 LYS B CG    1 
ATOM   7852  C  CD    . LYS B 1 287 ? 97.956  139.479 147.500 1.00 32.66 ?  287 LYS B CD    1 
ATOM   7853  C  CE    . LYS B 1 287 ? 96.753  139.320 146.590 1.00 31.91 ?  287 LYS B CE    1 
ATOM   7854  N  NZ    . LYS B 1 287 ? 95.476  139.499 147.333 1.00 33.82 1  287 LYS B NZ    1 
ATOM   7855  N  N     . PHE B 1 288 ? 102.082 137.089 148.197 1.00 26.58 ?  288 PHE B N     1 
ATOM   7856  C  CA    . PHE B 1 288 ? 102.434 135.725 147.811 1.00 23.20 ?  288 PHE B CA    1 
ATOM   7857  C  C     . PHE B 1 288 ? 102.141 134.739 148.934 1.00 22.50 ?  288 PHE B C     1 
ATOM   7858  O  O     . PHE B 1 288 ? 101.622 133.643 148.690 1.00 30.53 ?  288 PHE B O     1 
ATOM   7859  C  CB    . PHE B 1 288 ? 103.906 135.652 147.409 1.00 27.79 ?  288 PHE B CB    1 
ATOM   7860  C  CG    . PHE B 1 288 ? 104.320 134.308 146.886 1.00 26.67 ?  288 PHE B CG    1 
ATOM   7861  C  CD1   . PHE B 1 288 ? 104.104 133.971 145.562 1.00 23.90 ?  288 PHE B CD1   1 
ATOM   7862  C  CD2   . PHE B 1 288 ? 104.917 133.377 147.720 1.00 23.29 ?  288 PHE B CD2   1 
ATOM   7863  C  CE1   . PHE B 1 288 ? 104.478 132.734 145.077 1.00 28.59 ?  288 PHE B CE1   1 
ATOM   7864  C  CE2   . PHE B 1 288 ? 105.293 132.139 147.241 1.00 24.98 ?  288 PHE B CE2   1 
ATOM   7865  C  CZ    . PHE B 1 288 ? 105.076 131.818 145.919 1.00 26.34 ?  288 PHE B CZ    1 
ATOM   7866  N  N     . VAL B 1 289 ? 102.475 135.107 150.171 1.00 25.75 ?  289 VAL B N     1 
ATOM   7867  C  CA    . VAL B 1 289 ? 102.200 134.234 151.307 1.00 26.07 ?  289 VAL B CA    1 
ATOM   7868  C  C     . VAL B 1 289 ? 100.699 134.067 151.497 1.00 26.59 ?  289 VAL B C     1 
ATOM   7869  O  O     . VAL B 1 289 ? 100.220 132.981 151.838 1.00 29.88 ?  289 VAL B O     1 
ATOM   7870  C  CB    . VAL B 1 289 ? 102.877 134.780 152.576 1.00 31.81 ?  289 VAL B CB    1 
ATOM   7871  C  CG1   . VAL B 1 289 ? 102.743 133.789 153.719 1.00 23.07 ?  289 VAL B CG1   1 
ATOM   7872  C  CG2   . VAL B 1 289 ? 104.339 135.095 152.302 1.00 25.12 ?  289 VAL B CG2   1 
ATOM   7873  N  N     . GLU B 1 290 ? 99.933  135.139 151.282 1.00 34.76 ?  290 GLU B N     1 
ATOM   7874  C  CA    . GLU B 1 290 ? 98.480  135.045 151.380 1.00 30.92 ?  290 GLU B CA    1 
ATOM   7875  C  C     . GLU B 1 290 ? 97.912  134.114 150.314 1.00 34.54 ?  290 GLU B C     1 
ATOM   7876  O  O     . GLU B 1 290 ? 97.029  133.297 150.598 1.00 39.59 ?  290 GLU B O     1 
ATOM   7877  C  CB    . GLU B 1 290 ? 97.864  136.439 151.270 1.00 28.23 ?  290 GLU B CB    1 
ATOM   7878  C  CG    . GLU B 1 290 ? 96.480  136.474 150.646 1.00 37.04 ?  290 GLU B CG    1 
ATOM   7879  C  CD    . GLU B 1 290 ? 95.876  137.864 150.653 1.00 41.41 ?  290 GLU B CD    1 
ATOM   7880  O  OE1   . GLU B 1 290 ? 95.903  138.518 151.716 1.00 42.37 ?  290 GLU B OE1   1 
ATOM   7881  O  OE2   . GLU B 1 290 ? 95.376  138.302 149.596 1.00 38.39 -1 290 GLU B OE2   1 
ATOM   7882  N  N     . LEU B 1 291 ? 98.412  134.222 149.080 1.00 27.28 ?  291 LEU B N     1 
ATOM   7883  C  CA    . LEU B 1 291 ? 97.943  133.348 148.007 1.00 25.18 ?  291 LEU B CA    1 
ATOM   7884  C  C     . LEU B 1 291 ? 98.298  131.892 148.280 1.00 32.91 ?  291 LEU B C     1 
ATOM   7885  O  O     . LEU B 1 291 ? 97.482  130.995 148.043 1.00 37.34 ?  291 LEU B O     1 
ATOM   7886  C  CB    . LEU B 1 291 ? 98.528  133.798 146.668 1.00 29.43 ?  291 LEU B CB    1 
ATOM   7887  C  CG    . LEU B 1 291 ? 98.067  135.153 146.129 1.00 29.44 ?  291 LEU B CG    1 
ATOM   7888  C  CD1   . LEU B 1 291 ? 99.072  135.697 145.131 1.00 26.20 ?  291 LEU B CD1   1 
ATOM   7889  C  CD2   . LEU B 1 291 ? 96.690  135.042 145.502 1.00 32.36 ?  291 LEU B CD2   1 
ATOM   7890  N  N     . ALA B 1 292 ? 99.517  131.638 148.763 1.00 32.40 ?  292 ALA B N     1 
ATOM   7891  C  CA    . ALA B 1 292 ? 99.911  130.272 149.091 1.00 27.35 ?  292 ALA B CA    1 
ATOM   7892  C  C     . ALA B 1 292 ? 99.082  129.719 150.245 1.00 29.21 ?  292 ALA B C     1 
ATOM   7893  O  O     . ALA B 1 292 ? 98.713  128.540 150.242 1.00 36.30 ?  292 ALA B O     1 
ATOM   7894  C  CB    . ALA B 1 292 ? 101.401 130.221 149.426 1.00 27.19 ?  292 ALA B CB    1 
ATOM   7895  N  N     . ARG B 1 293 ? 98.787  130.557 151.240 1.00 28.11 ?  293 ARG B N     1 
ATOM   7896  C  CA    . ARG B 1 293 ? 97.988  130.118 152.379 1.00 28.07 ?  293 ARG B CA    1 
ATOM   7897  C  C     . ARG B 1 293 ? 96.584  129.716 151.950 1.00 35.25 ?  293 ARG B C     1 
ATOM   7898  O  O     . ARG B 1 293 ? 96.051  128.702 152.413 1.00 39.63 ?  293 ARG B O     1 
ATOM   7899  C  CB    . ARG B 1 293 ? 97.939  131.229 153.427 1.00 29.39 ?  293 ARG B CB    1 
ATOM   7900  C  CG    . ARG B 1 293 ? 96.856  131.072 154.478 1.00 31.61 ?  293 ARG B CG    1 
ATOM   7901  C  CD    . ARG B 1 293 ? 96.680  132.364 155.253 1.00 32.58 ?  293 ARG B CD    1 
ATOM   7902  N  NE    . ARG B 1 293 ? 97.964  132.924 155.657 1.00 38.76 ?  293 ARG B NE    1 
ATOM   7903  C  CZ    . ARG B 1 293 ? 98.351  134.167 155.408 1.00 37.05 ?  293 ARG B CZ    1 
ATOM   7904  N  NH1   . ARG B 1 293 ? 97.569  135.018 154.764 1.00 36.91 1  293 ARG B NH1   1 
ATOM   7905  N  NH2   . ARG B 1 293 ? 99.554  134.565 155.810 1.00 29.92 ?  293 ARG B NH2   1 
ATOM   7906  N  N     . GLU B 1 294 ? 95.973  130.494 151.059 1.00 44.02 ?  294 GLU B N     1 
ATOM   7907  C  CA    . GLU B 1 294 ? 94.631  130.210 150.572 1.00 41.02 ?  294 GLU B CA    1 
ATOM   7908  C  C     . GLU B 1 294 ? 94.614  129.197 149.435 1.00 42.10 ?  294 GLU B C     1 
ATOM   7909  O  O     . GLU B 1 294 ? 93.528  128.843 148.964 1.00 46.91 ?  294 GLU B O     1 
ATOM   7910  C  CB    . GLU B 1 294 ? 93.958  131.508 150.120 1.00 37.63 ?  294 GLU B CB    1 
ATOM   7911  C  CG    . GLU B 1 294 ? 93.849  132.556 151.215 1.00 42.57 ?  294 GLU B CG    1 
ATOM   7912  C  CD    . GLU B 1 294 ? 93.387  133.902 150.693 1.00 48.77 ?  294 GLU B CD    1 
ATOM   7913  O  OE1   . GLU B 1 294 ? 93.209  134.036 149.465 1.00 48.12 ?  294 GLU B OE1   1 
ATOM   7914  O  OE2   . GLU B 1 294 ? 93.203  134.827 151.512 1.00 45.21 -1 294 GLU B OE2   1 
ATOM   7915  N  N     . ASP B 1 295 ? 95.782  128.739 148.984 1.00 39.29 ?  295 ASP B N     1 
ATOM   7916  C  CA    . ASP B 1 295 ? 95.921  127.759 147.908 1.00 41.69 ?  295 ASP B CA    1 
ATOM   7917  C  C     . ASP B 1 295 ? 95.345  128.258 146.587 1.00 45.58 ?  295 ASP B C     1 
ATOM   7918  O  O     . ASP B 1 295 ? 95.091  127.462 145.676 1.00 46.25 ?  295 ASP B O     1 
ATOM   7919  C  CB    . ASP B 1 295 ? 95.285  126.416 148.286 1.00 45.70 ?  295 ASP B CB    1 
ATOM   7920  C  CG    . ASP B 1 295 ? 96.101  125.231 147.808 1.00 50.22 ?  295 ASP B CG    1 
ATOM   7921  O  OD1   . ASP B 1 295 ? 96.033  124.164 148.451 1.00 47.79 ?  295 ASP B OD1   1 
ATOM   7922  O  OD2   . ASP B 1 295 ? 96.810  125.368 146.790 1.00 47.83 -1 295 ASP B OD2   1 
ATOM   7923  N  N     . LYS B 1 296 ? 95.133  129.566 146.462 1.00 45.81 ?  296 LYS B N     1 
ATOM   7924  C  CA    . LYS B 1 296 ? 94.666  130.145 145.213 1.00 44.99 ?  296 LYS B CA    1 
ATOM   7925  C  C     . LYS B 1 296 ? 95.835  130.296 144.251 1.00 46.34 ?  296 LYS B C     1 
ATOM   7926  O  O     . LYS B 1 296 ? 96.905  130.777 144.636 1.00 48.28 ?  296 LYS B O     1 
ATOM   7927  C  CB    . LYS B 1 296 ? 94.007  131.500 145.468 1.00 45.13 ?  296 LYS B CB    1 
ATOM   7928  C  CG    . LYS B 1 296 ? 92.764  131.431 146.340 1.00 46.13 ?  296 LYS B CG    1 
ATOM   7929  C  CD    . LYS B 1 296 ? 92.194  132.814 146.604 1.00 46.16 ?  296 LYS B CD    1 
ATOM   7930  C  CE    . LYS B 1 296 ? 90.897  132.734 147.394 1.00 47.56 ?  296 LYS B CE    1 
ATOM   7931  N  NZ    . LYS B 1 296 ? 90.469  134.070 147.895 1.00 45.77 1  296 LYS B NZ    1 
ATOM   7932  N  N     . ALA B 1 297 ? 95.635  129.880 143.002 1.00 44.65 ?  297 ALA B N     1 
ATOM   7933  C  CA    . ALA B 1 297 ? 96.695  129.967 142.006 1.00 43.38 ?  297 ALA B CA    1 
ATOM   7934  C  C     . ALA B 1 297 ? 97.112  131.417 141.802 1.00 42.38 ?  297 ALA B C     1 
ATOM   7935  O  O     . ALA B 1 297 ? 96.270  132.301 141.620 1.00 44.72 ?  297 ALA B O     1 
ATOM   7936  C  CB    . ALA B 1 297 ? 96.232  129.356 140.686 1.00 42.71 ?  297 ALA B CB    1 
ATOM   7937  N  N     . ALA B 1 298 ? 98.418  131.658 141.834 1.00 34.57 ?  298 ALA B N     1 
ATOM   7938  C  CA    . ALA B 1 298 ? 98.948  133.006 141.733 1.00 33.18 ?  298 ALA B CA    1 
ATOM   7939  C  C     . ALA B 1 298 ? 99.368  133.306 140.300 1.00 35.87 ?  298 ALA B C     1 
ATOM   7940  O  O     . ALA B 1 298 ? 99.348  132.444 139.420 1.00 40.21 ?  298 ALA B O     1 
ATOM   7941  C  CB    . ALA B 1 298 ? 100.128 133.188 142.687 1.00 34.50 ?  298 ALA B CB    1 
ATOM   7942  N  N     . TYR B 1 299 ? 99.763  134.554 140.069 1.00 36.18 ?  299 TYR B N     1 
ATOM   7943  C  CA    . TYR B 1 299 ? 100.206 134.993 138.754 1.00 25.69 ?  299 TYR B CA    1 
ATOM   7944  C  C     . TYR B 1 299 ? 101.531 135.724 138.887 1.00 27.90 ?  299 TYR B C     1 
ATOM   7945  O  O     . TYR B 1 299 ? 101.646 136.672 139.670 1.00 34.61 ?  299 TYR B O     1 
ATOM   7946  C  CB    . TYR B 1 299 ? 99.165  135.903 138.097 1.00 30.33 ?  299 TYR B CB    1 
ATOM   7947  C  CG    . TYR B 1 299 ? 97.993  135.160 137.497 1.00 31.78 ?  299 TYR B CG    1 
ATOM   7948  C  CD1   . TYR B 1 299 ? 98.116  134.489 136.288 1.00 33.34 ?  299 TYR B CD1   1 
ATOM   7949  C  CD2   . TYR B 1 299 ? 96.760  135.139 138.135 1.00 32.79 ?  299 TYR B CD2   1 
ATOM   7950  C  CE1   . TYR B 1 299 ? 97.048  133.813 135.735 1.00 33.86 ?  299 TYR B CE1   1 
ATOM   7951  C  CE2   . TYR B 1 299 ? 95.684  134.466 137.590 1.00 33.08 ?  299 TYR B CE2   1 
ATOM   7952  C  CZ    . TYR B 1 299 ? 95.834  133.803 136.389 1.00 35.07 ?  299 TYR B CZ    1 
ATOM   7953  O  OH    . TYR B 1 299 ? 94.766  133.132 135.841 1.00 37.22 ?  299 TYR B OH    1 
ATOM   7954  N  N     . VAL B 1 300 ? 102.524 135.282 138.132 1.00 29.64 ?  300 VAL B N     1 
ATOM   7955  C  CA    . VAL B 1 300 ? 103.771 136.021 137.988 1.00 22.32 ?  300 VAL B CA    1 
ATOM   7956  C  C     . VAL B 1 300 ? 103.616 136.952 136.797 1.00 25.64 ?  300 VAL B C     1 
ATOM   7957  O  O     . VAL B 1 300 ? 102.863 136.666 135.865 1.00 30.12 ?  300 VAL B O     1 
ATOM   7958  C  CB    . VAL B 1 300 ? 104.981 135.077 137.827 1.00 24.45 ?  300 VAL B CB    1 
ATOM   7959  C  CG1   . VAL B 1 300 ? 105.328 134.434 139.157 1.00 23.16 ?  300 VAL B CG1   1 
ATOM   7960  C  CG2   . VAL B 1 300 ? 104.694 134.020 136.774 1.00 26.14 ?  300 VAL B CG2   1 
ATOM   7961  N  N     . PHE B 1 301 ? 104.319 138.077 136.819 1.00 25.84 ?  301 PHE B N     1 
ATOM   7962  C  CA    . PHE B 1 301 ? 104.039 139.151 135.885 1.00 20.81 ?  301 PHE B CA    1 
ATOM   7963  C  C     . PHE B 1 301 ? 105.260 139.493 135.044 1.00 28.11 ?  301 PHE B C     1 
ATOM   7964  O  O     . PHE B 1 301 ? 106.407 139.279 135.445 1.00 29.52 ?  301 PHE B O     1 
ATOM   7965  C  CB    . PHE B 1 301 ? 103.551 140.401 136.623 1.00 24.66 ?  301 PHE B CB    1 
ATOM   7966  C  CG    . PHE B 1 301 ? 102.317 140.171 137.440 1.00 27.51 ?  301 PHE B CG    1 
ATOM   7967  C  CD1   . PHE B 1 301 ? 101.089 140.005 136.826 1.00 26.92 ?  301 PHE B CD1   1 
ATOM   7968  C  CD2   . PHE B 1 301 ? 102.385 140.114 138.820 1.00 25.39 ?  301 PHE B CD2   1 
ATOM   7969  C  CE1   . PHE B 1 301 ? 99.952  139.785 137.572 1.00 27.62 ?  301 PHE B CE1   1 
ATOM   7970  C  CE2   . PHE B 1 301 ? 101.251 139.898 139.571 1.00 28.97 ?  301 PHE B CE2   1 
ATOM   7971  C  CZ    . PHE B 1 301 ? 100.033 139.735 138.946 1.00 28.06 ?  301 PHE B CZ    1 
ATOM   7972  N  N     . TYR B 1 302 ? 104.982 140.031 133.857 1.00 25.95 ?  302 TYR B N     1 
ATOM   7973  C  CA    . TYR B 1 302 ? 106.018 140.557 132.982 1.00 26.54 ?  302 TYR B CA    1 
ATOM   7974  C  C     . TYR B 1 302 ? 106.248 142.015 133.353 1.00 29.50 ?  302 TYR B C     1 
ATOM   7975  O  O     . TYR B 1 302 ? 105.328 142.831 133.201 1.00 30.63 ?  302 TYR B O     1 
ATOM   7976  C  CB    . TYR B 1 302 ? 105.603 140.434 131.523 1.00 25.74 ?  302 TYR B CB    1 
ATOM   7977  C  CG    . TYR B 1 302 ? 105.621 139.019 130.994 1.00 27.02 ?  302 TYR B CG    1 
ATOM   7978  C  CD1   . TYR B 1 302 ? 104.633 138.111 131.349 1.00 25.03 ?  302 TYR B CD1   1 
ATOM   7979  C  CD2   . TYR B 1 302 ? 106.625 138.591 130.139 1.00 27.54 ?  302 TYR B CD2   1 
ATOM   7980  C  CE1   . TYR B 1 302 ? 104.645 136.820 130.868 1.00 25.70 ?  302 TYR B CE1   1 
ATOM   7981  C  CE2   . TYR B 1 302 ? 106.646 137.301 129.651 1.00 26.81 ?  302 TYR B CE2   1 
ATOM   7982  C  CZ    . TYR B 1 302 ? 105.653 136.420 130.019 1.00 30.33 ?  302 TYR B CZ    1 
ATOM   7983  O  OH    . TYR B 1 302 ? 105.672 135.132 129.536 1.00 33.17 ?  302 TYR B OH    1 
ATOM   7984  N  N     . PRO B 1 303 ? 107.428 142.384 133.856 1.00 28.05 ?  303 PRO B N     1 
ATOM   7985  C  CA    . PRO B 1 303 ? 107.622 143.760 134.338 1.00 25.48 ?  303 PRO B CA    1 
ATOM   7986  C  C     . PRO B 1 303 ? 107.433 144.826 133.274 1.00 29.88 ?  303 PRO B C     1 
ATOM   7987  O  O     . PRO B 1 303 ? 106.948 145.919 133.590 1.00 30.10 ?  303 PRO B O     1 
ATOM   7988  C  CB    . PRO B 1 303 ? 109.066 143.746 134.860 1.00 23.10 ?  303 PRO B CB    1 
ATOM   7989  C  CG    . PRO B 1 303 ? 109.358 142.319 135.135 1.00 25.78 ?  303 PRO B CG    1 
ATOM   7990  C  CD    . PRO B 1 303 ? 108.603 141.536 134.111 1.00 22.71 ?  303 PRO B CD    1 
ATOM   7991  N  N     . HIS B 1 304 ? 107.802 144.547 132.021 1.00 29.63 ?  304 HIS B N     1 
ATOM   7992  C  CA    . HIS B 1 304 ? 107.756 145.591 131.003 1.00 29.90 ?  304 HIS B CA    1 
ATOM   7993  C  C     . HIS B 1 304 ? 106.323 145.952 130.639 1.00 31.79 ?  304 HIS B C     1 
ATOM   7994  O  O     . HIS B 1 304 ? 106.023 147.121 130.377 1.00 37.64 ?  304 HIS B O     1 
ATOM   7995  C  CB    . HIS B 1 304 ? 108.528 145.161 129.759 1.00 27.70 ?  304 HIS B CB    1 
ATOM   7996  C  CG    . HIS B 1 304 ? 108.667 146.245 128.738 1.00 28.80 ?  304 HIS B CG    1 
ATOM   7997  N  ND1   . HIS B 1 304 ? 108.956 147.549 129.075 1.00 27.07 ?  304 HIS B ND1   1 
ATOM   7998  C  CD2   . HIS B 1 304 ? 108.550 146.222 127.390 1.00 35.59 ?  304 HIS B CD2   1 
ATOM   7999  C  CE1   . HIS B 1 304 ? 109.015 148.282 127.979 1.00 30.15 ?  304 HIS B CE1   1 
ATOM   8000  N  NE2   . HIS B 1 304 ? 108.773 147.501 126.942 1.00 35.61 ?  304 HIS B NE2   1 
ATOM   8001  N  N     . THR B 1 305 ? 105.425 144.966 130.605 1.00 28.56 ?  305 THR B N     1 
ATOM   8002  C  CA    . THR B 1 305 ? 104.020 145.263 130.339 1.00 32.68 ?  305 THR B CA    1 
ATOM   8003  C  C     . THR B 1 305 ? 103.427 146.131 131.440 1.00 29.26 ?  305 THR B C     1 
ATOM   8004  O  O     . THR B 1 305 ? 102.682 147.080 131.164 1.00 34.96 ?  305 THR B O     1 
ATOM   8005  C  CB    . THR B 1 305 ? 103.229 143.964 130.193 1.00 30.45 ?  305 THR B CB    1 
ATOM   8006  O  OG1   . THR B 1 305 ? 103.240 143.253 131.437 1.00 28.12 ?  305 THR B OG1   1 
ATOM   8007  C  CG2   . THR B 1 305 ? 103.841 143.090 129.114 1.00 31.29 ?  305 THR B CG2   1 
ATOM   8008  N  N     . ILE B 1 306 ? 103.758 145.826 132.696 1.00 29.89 ?  306 ILE B N     1 
ATOM   8009  C  CA    . ILE B 1 306 ? 103.281 146.632 133.815 1.00 30.13 ?  306 ILE B CA    1 
ATOM   8010  C  C     . ILE B 1 306 ? 103.843 148.044 133.732 1.00 29.22 ?  306 ILE B C     1 
ATOM   8011  O  O     . ILE B 1 306 ? 103.132 149.026 133.981 1.00 34.03 ?  306 ILE B O     1 
ATOM   8012  C  CB    . ILE B 1 306 ? 103.642 145.952 135.148 1.00 26.76 ?  306 ILE B CB    1 
ATOM   8013  C  CG1   . ILE B 1 306 ? 102.790 144.701 135.350 1.00 26.49 ?  306 ILE B CG1   1 
ATOM   8014  C  CG2   . ILE B 1 306 ? 103.466 146.909 136.306 1.00 29.75 ?  306 ILE B CG2   1 
ATOM   8015  C  CD1   . ILE B 1 306 ? 103.126 143.941 136.599 1.00 28.94 ?  306 ILE B CD1   1 
ATOM   8016  N  N     . TYR B 1 307 ? 105.124 148.171 133.384 1.00 30.63 ?  307 TYR B N     1 
ATOM   8017  C  CA    . TYR B 1 307 ? 105.726 149.494 133.257 1.00 27.67 ?  307 TYR B CA    1 
ATOM   8018  C  C     . TYR B 1 307 ? 105.080 150.287 132.128 1.00 31.63 ?  307 TYR B C     1 
ATOM   8019  O  O     . TYR B 1 307 ? 104.856 151.495 132.259 1.00 35.31 ?  307 TYR B O     1 
ATOM   8020  C  CB    . TYR B 1 307 ? 107.236 149.364 133.045 1.00 24.46 ?  307 TYR B CB    1 
ATOM   8021  C  CG    . TYR B 1 307 ? 107.967 150.683 132.918 1.00 31.21 ?  307 TYR B CG    1 
ATOM   8022  C  CD1   . TYR B 1 307 ? 108.023 151.362 131.706 1.00 31.54 ?  307 TYR B CD1   1 
ATOM   8023  C  CD2   . TYR B 1 307 ? 108.588 151.258 134.019 1.00 26.86 ?  307 TYR B CD2   1 
ATOM   8024  C  CE1   . TYR B 1 307 ? 108.682 152.567 131.595 1.00 31.01 ?  307 TYR B CE1   1 
ATOM   8025  C  CE2   . TYR B 1 307 ? 109.248 152.462 133.916 1.00 29.82 ?  307 TYR B CE2   1 
ATOM   8026  C  CZ    . TYR B 1 307 ? 109.294 153.113 132.702 1.00 34.47 ?  307 TYR B CZ    1 
ATOM   8027  O  OH    . TYR B 1 307 ? 109.953 154.315 132.594 1.00 36.60 ?  307 TYR B OH    1 
ATOM   8028  N  N     . LYS B 1 308 ? 104.786 149.627 131.006 1.00 34.42 ?  308 LYS B N     1 
ATOM   8029  C  CA    . LYS B 1 308 ? 104.117 150.301 129.900 1.00 31.88 ?  308 LYS B CA    1 
ATOM   8030  C  C     . LYS B 1 308 ? 102.723 150.763 130.297 1.00 31.61 ?  308 LYS B C     1 
ATOM   8031  O  O     . LYS B 1 308 ? 102.312 151.881 129.964 1.00 36.40 ?  308 LYS B O     1 
ATOM   8032  C  CB    . LYS B 1 308 ? 104.044 149.369 128.690 1.00 32.36 ?  308 LYS B CB    1 
ATOM   8033  C  CG    . LYS B 1 308 ? 105.310 149.334 127.849 1.00 33.85 ?  308 LYS B CG    1 
ATOM   8034  C  CD    . LYS B 1 308 ? 105.499 147.988 127.154 1.00 35.89 ?  308 LYS B CD    1 
ATOM   8035  C  CE    . LYS B 1 308 ? 104.220 147.163 127.128 1.00 36.98 ?  308 LYS B CE    1 
ATOM   8036  N  NZ    . LYS B 1 308 ? 104.196 146.207 125.988 1.00 35.60 1  308 LYS B NZ    1 
ATOM   8037  N  N     . GLU B 1 309 ? 101.979 149.917 131.014 1.00 29.97 ?  309 GLU B N     1 
ATOM   8038  C  CA    . GLU B 1 309 ? 100.599 150.254 131.345 1.00 34.83 ?  309 GLU B CA    1 
ATOM   8039  C  C     . GLU B 1 309 ? 100.518 151.336 132.416 1.00 35.03 ?  309 GLU B C     1 
ATOM   8040  O  O     . GLU B 1 309 ? 99.707  152.262 132.307 1.00 37.16 ?  309 GLU B O     1 
ATOM   8041  C  CB    . GLU B 1 309 ? 99.850  149.002 131.795 1.00 32.85 ?  309 GLU B CB    1 
ATOM   8042  C  CG    . GLU B 1 309 ? 98.508  149.290 132.442 1.00 35.09 ?  309 GLU B CG    1 
ATOM   8043  C  CD    . GLU B 1 309 ? 97.488  149.850 131.469 1.00 40.22 ?  309 GLU B CD    1 
ATOM   8044  O  OE1   . GLU B 1 309 ? 97.680  149.700 130.244 1.00 40.62 ?  309 GLU B OE1   1 
ATOM   8045  O  OE2   . GLU B 1 309 ? 96.492  150.444 131.932 1.00 39.65 -1 309 GLU B OE2   1 
ATOM   8046  N  N     . TYR B 1 310 ? 101.348 151.243 133.455 1.00 33.44 ?  310 TYR B N     1 
ATOM   8047  C  CA    . TYR B 1 310 ? 101.223 152.114 134.614 1.00 33.04 ?  310 TYR B CA    1 
ATOM   8048  C  C     . TYR B 1 310 ? 102.298 153.187 134.703 1.00 31.90 ?  310 TYR B C     1 
ATOM   8049  O  O     . TYR B 1 310 ? 102.127 154.143 135.467 1.00 31.87 ?  310 TYR B O     1 
ATOM   8050  C  CB    . TYR B 1 310 ? 101.240 151.279 135.903 1.00 31.08 ?  310 TYR B CB    1 
ATOM   8051  C  CG    . TYR B 1 310 ? 100.123 150.263 135.982 1.00 32.59 ?  310 TYR B CG    1 
ATOM   8052  C  CD1   . TYR B 1 310 ? 98.870  150.616 136.465 1.00 31.36 ?  310 TYR B CD1   1 
ATOM   8053  C  CD2   . TYR B 1 310 ? 100.320 148.953 135.568 1.00 32.26 ?  310 TYR B CD2   1 
ATOM   8054  C  CE1   . TYR B 1 310 ? 97.847  149.692 136.538 1.00 33.04 ?  310 TYR B CE1   1 
ATOM   8055  C  CE2   . TYR B 1 310 ? 99.301  148.022 135.635 1.00 32.17 ?  310 TYR B CE2   1 
ATOM   8056  C  CZ    . TYR B 1 310 ? 98.068  148.397 136.122 1.00 33.62 ?  310 TYR B CZ    1 
ATOM   8057  O  OH    . TYR B 1 310 ? 97.052  147.474 136.192 1.00 34.39 ?  310 TYR B OH    1 
ATOM   8058  N  N     . GLY B 1 311 ? 103.387 153.065 133.950 1.00 29.63 ?  311 GLY B N     1 
ATOM   8059  C  CA    . GLY B 1 311 ? 104.473 154.015 134.037 1.00 29.67 ?  311 GLY B CA    1 
ATOM   8060  C  C     . GLY B 1 311 ? 105.438 153.778 135.176 1.00 34.53 ?  311 GLY B C     1 
ATOM   8061  O  O     . GLY B 1 311 ? 106.403 154.539 135.315 1.00 36.90 ?  311 GLY B O     1 
ATOM   8062  N  N     . GLN B 1 312 ? 105.211 152.753 135.993 1.00 31.52 ?  312 GLN B N     1 
ATOM   8063  C  CA    . GLN B 1 312 ? 106.084 152.424 137.107 1.00 29.78 ?  312 GLN B CA    1 
ATOM   8064  C  C     . GLN B 1 312 ? 106.451 150.949 137.042 1.00 32.31 ?  312 GLN B C     1 
ATOM   8065  O  O     . GLN B 1 312 ? 105.735 150.134 136.455 1.00 39.23 ?  312 GLN B O     1 
ATOM   8066  C  CB    . GLN B 1 312 ? 105.428 152.738 138.459 1.00 32.47 ?  312 GLN B CB    1 
ATOM   8067  C  CG    . GLN B 1 312 ? 104.370 153.826 138.408 1.00 31.94 ?  312 GLN B CG    1 
ATOM   8068  C  CD    . GLN B 1 312 ? 103.462 153.812 139.620 1.00 35.90 ?  312 GLN B CD    1 
ATOM   8069  O  OE1   . GLN B 1 312 ? 103.881 154.148 140.728 1.00 38.51 ?  312 GLN B OE1   1 
ATOM   8070  N  NE2   . GLN B 1 312 ? 102.210 153.420 139.417 1.00 33.65 ?  312 GLN B NE2   1 
ATOM   8071  N  N     . HIS B 1 313 ? 107.582 150.615 137.656 1.00 29.23 ?  313 HIS B N     1 
ATOM   8072  C  CA    . HIS B 1 313 ? 108.035 149.236 137.689 1.00 29.45 ?  313 HIS B CA    1 
ATOM   8073  C  C     . HIS B 1 313 ? 107.167 148.407 138.632 1.00 32.07 ?  313 HIS B C     1 
ATOM   8074  O  O     . HIS B 1 313 ? 106.513 148.928 139.540 1.00 32.39 ?  313 HIS B O     1 
ATOM   8075  C  CB    . HIS B 1 313 ? 109.501 149.168 138.115 1.00 26.13 ?  313 HIS B CB    1 
ATOM   8076  C  CG    . HIS B 1 313 ? 110.423 149.933 137.219 1.00 27.87 ?  313 HIS B CG    1 
ATOM   8077  N  ND1   . HIS B 1 313 ? 110.900 149.421 136.031 1.00 30.95 ?  313 HIS B ND1   1 
ATOM   8078  C  CD2   . HIS B 1 313 ? 110.954 151.173 137.332 1.00 29.49 ?  313 HIS B CD2   1 
ATOM   8079  C  CE1   . HIS B 1 313 ? 111.685 150.312 135.453 1.00 28.56 ?  313 HIS B CE1   1 
ATOM   8080  N  NE2   . HIS B 1 313 ? 111.735 151.384 136.223 1.00 30.09 ?  313 HIS B NE2   1 
ATOM   8081  N  N     . MET B 1 314 ? 107.164 147.093 138.398 1.00 35.31 ?  314 MET B N     1 
ATOM   8082  C  CA    . MET B 1 314 ? 106.337 146.198 139.204 1.00 30.43 ?  314 MET B CA    1 
ATOM   8083  C  C     . MET B 1 314 ? 106.766 146.215 140.666 1.00 37.07 ?  314 MET B C     1 
ATOM   8084  O  O     . MET B 1 314 ? 105.920 146.204 141.568 1.00 39.69 ?  314 MET B O     1 
ATOM   8085  C  CB    . MET B 1 314 ? 106.397 144.778 138.645 1.00 28.98 ?  314 MET B CB    1 
ATOM   8086  C  CG    . MET B 1 314 ? 105.464 143.810 139.352 1.00 29.54 ?  314 MET B CG    1 
ATOM   8087  S  SD    . MET B 1 314 ? 106.005 142.092 139.310 1.00 45.32 ?  314 MET B SD    1 
ATOM   8088  C  CE    . MET B 1 314 ? 107.111 142.112 137.907 1.00 30.08 ?  314 MET B CE    1 
ATOM   8089  N  N     . ASP B 1 315 ? 108.072 146.241 140.922 1.00 30.29 ?  315 ASP B N     1 
ATOM   8090  C  CA    . ASP B 1 315 ? 108.578 146.291 142.287 1.00 34.42 ?  315 ASP B CA    1 
ATOM   8091  C  C     . ASP B 1 315 ? 108.597 147.701 142.859 1.00 30.20 ?  315 ASP B C     1 
ATOM   8092  O  O     . ASP B 1 315 ? 108.984 147.877 144.019 1.00 36.93 ?  315 ASP B O     1 
ATOM   8093  C  CB    . ASP B 1 315 ? 109.983 145.686 142.351 1.00 33.18 ?  315 ASP B CB    1 
ATOM   8094  C  CG    . ASP B 1 315 ? 110.995 146.478 141.551 1.00 32.79 ?  315 ASP B CG    1 
ATOM   8095  O  OD1   . ASP B 1 315 ? 110.590 147.141 140.574 1.00 36.65 ?  315 ASP B OD1   1 
ATOM   8096  O  OD2   . ASP B 1 315 ? 112.191 146.439 141.900 1.00 29.78 -1 315 ASP B OD2   1 
ATOM   8097  N  N     . GLU B 1 316 ? 108.192 148.704 142.079 1.00 28.38 ?  316 GLU B N     1 
ATOM   8098  C  CA    . GLU B 1 316 ? 108.139 150.078 142.556 1.00 29.96 ?  316 GLU B CA    1 
ATOM   8099  C  C     . GLU B 1 316 ? 106.858 150.398 143.314 1.00 35.54 ?  316 GLU B C     1 
ATOM   8100  O  O     . GLU B 1 316 ? 106.777 151.464 143.934 1.00 39.07 ?  316 GLU B O     1 
ATOM   8101  C  CB    . GLU B 1 316 ? 108.283 151.048 141.380 1.00 36.44 ?  316 GLU B CB    1 
ATOM   8102  C  CG    . GLU B 1 316 ? 109.704 151.517 141.113 1.00 34.69 ?  316 GLU B CG    1 
ATOM   8103  C  CD    . GLU B 1 316 ? 110.505 151.728 142.380 1.00 36.36 ?  316 GLU B CD    1 
ATOM   8104  O  OE1   . GLU B 1 316 ? 110.073 152.526 143.239 1.00 38.09 ?  316 GLU B OE1   1 
ATOM   8105  O  OE2   . GLU B 1 316 ? 111.573 151.097 142.516 1.00 41.39 -1 316 GLU B OE2   1 
ATOM   8106  N  N     . MET B 1 317 ? 105.863 149.517 143.280 1.00 38.06 ?  317 MET B N     1 
ATOM   8107  C  CA    . MET B 1 317 ? 104.586 149.756 143.935 1.00 38.40 ?  317 MET B CA    1 
ATOM   8108  C  C     . MET B 1 317 ? 104.184 148.537 144.754 1.00 37.91 ?  317 MET B C     1 
ATOM   8109  O  O     . MET B 1 317 ? 104.789 147.467 144.667 1.00 37.39 ?  317 MET B O     1 
ATOM   8110  C  CB    . MET B 1 317 ? 103.490 150.111 142.921 1.00 40.05 ?  317 MET B CB    1 
ATOM   8111  C  CG    . MET B 1 317 ? 103.615 149.408 141.584 1.00 34.68 ?  317 MET B CG    1 
ATOM   8112  S  SD    . MET B 1 317 ? 102.946 150.428 140.256 1.00 48.10 ?  317 MET B SD    1 
ATOM   8113  C  CE    . MET B 1 317 ? 103.261 149.389 138.837 1.00 33.99 ?  317 MET B CE    1 
ATOM   8114  N  N     . ASP B 1 318 ? 103.136 148.720 145.556 1.00 40.30 ?  318 ASP B N     1 
ATOM   8115  C  CA    . ASP B 1 318 ? 102.694 147.713 146.515 1.00 38.45 ?  318 ASP B CA    1 
ATOM   8116  C  C     . ASP B 1 318 ? 101.916 146.625 145.788 1.00 38.44 ?  318 ASP B C     1 
ATOM   8117  O  O     . ASP B 1 318 ? 100.872 146.893 145.185 1.00 41.14 ?  318 ASP B O     1 
ATOM   8118  C  CB    . ASP B 1 318 ? 101.844 148.364 147.602 1.00 37.95 ?  318 ASP B CB    1 
ATOM   8119  C  CG    . ASP B 1 318 ? 101.369 147.373 148.644 1.00 46.03 ?  318 ASP B CG    1 
ATOM   8120  O  OD1   . ASP B 1 318 ? 102.203 146.895 149.442 1.00 42.17 ?  318 ASP B OD1   1 
ATOM   8121  O  OD2   . ASP B 1 318 ? 100.157 147.076 148.667 1.00 44.77 -1 318 ASP B OD2   1 
ATOM   8122  N  N     . MET B 1 319 ? 102.425 145.391 145.841 1.00 39.69 ?  319 MET B N     1 
ATOM   8123  C  CA    . MET B 1 319 ? 101.716 144.272 145.232 1.00 35.15 ?  319 MET B CA    1 
ATOM   8124  C  C     . MET B 1 319 ? 100.455 143.911 146.005 1.00 36.04 ?  319 MET B C     1 
ATOM   8125  O  O     . MET B 1 319 ? 99.492  143.419 145.412 1.00 38.25 ?  319 MET B O     1 
ATOM   8126  C  CB    . MET B 1 319 ? 102.636 143.055 145.126 1.00 36.87 ?  319 MET B CB    1 
ATOM   8127  C  CG    . MET B 1 319 ? 102.111 141.957 144.208 1.00 37.09 ?  319 MET B CG    1 
ATOM   8128  S  SD    . MET B 1 319 ? 102.482 142.180 142.455 1.00 44.18 ?  319 MET B SD    1 
ATOM   8129  C  CE    . MET B 1 319 ? 103.810 143.378 142.515 1.00 38.47 ?  319 MET B CE    1 
ATOM   8130  N  N     . ASN B 1 320 ? 100.435 144.158 147.317 1.00 38.47 ?  320 ASN B N     1 
ATOM   8131  C  CA    . ASN B 1 320 ? 99.268  143.803 148.118 1.00 38.98 ?  320 ASN B CA    1 
ATOM   8132  C  C     . ASN B 1 320 ? 98.026  144.564 147.675 1.00 40.89 ?  320 ASN B C     1 
ATOM   8133  O  O     . ASN B 1 320 ? 96.903  144.088 147.874 1.00 41.47 ?  320 ASN B O     1 
ATOM   8134  C  CB    . ASN B 1 320 ? 99.550  144.061 149.597 1.00 37.46 ?  320 ASN B CB    1 
ATOM   8135  C  CG    . ASN B 1 320 ? 100.656 143.181 150.139 1.00 42.30 ?  320 ASN B CG    1 
ATOM   8136  O  OD1   . ASN B 1 320 ? 101.774 143.180 149.623 1.00 37.80 ?  320 ASN B OD1   1 
ATOM   8137  N  ND2   . ASN B 1 320 ? 100.348 142.424 151.183 1.00 41.25 ?  320 ASN B ND2   1 
ATOM   8138  N  N     . GLU B 1 321 ? 98.204  145.740 147.076 1.00 42.19 ?  321 GLU B N     1 
ATOM   8139  C  CA    . GLU B 1 321 ? 97.088  146.543 146.599 1.00 40.34 ?  321 GLU B CA    1 
ATOM   8140  C  C     . GLU B 1 321 ? 96.966  146.576 145.083 1.00 40.01 ?  321 GLU B C     1 
ATOM   8141  O  O     . GLU B 1 321 ? 95.920  146.997 144.575 1.00 46.31 ?  321 GLU B O     1 
ATOM   8142  C  CB    . GLU B 1 321 ? 97.209  147.981 147.127 1.00 42.72 ?  321 GLU B CB    1 
ATOM   8143  C  CG    . GLU B 1 321 ? 97.965  148.920 146.201 1.00 39.85 ?  321 GLU B CG    1 
ATOM   8144  C  CD    . GLU B 1 321 ? 98.663  150.038 146.946 1.00 45.15 ?  321 GLU B CD    1 
ATOM   8145  O  OE1   . GLU B 1 321 ? 98.654  150.018 148.194 1.00 45.47 ?  321 GLU B OE1   1 
ATOM   8146  O  OE2   . GLU B 1 321 ? 99.229  150.934 146.284 1.00 45.61 -1 321 GLU B OE2   1 
ATOM   8147  N  N     . MET B 1 322 ? 97.989  146.144 144.347 1.00 34.71 ?  322 MET B N     1 
ATOM   8148  C  CA    . MET B 1 322 ? 97.984  146.238 142.895 1.00 32.82 ?  322 MET B CA    1 
ATOM   8149  C  C     . MET B 1 322 ? 97.973  144.879 142.207 1.00 33.10 ?  322 MET B C     1 
ATOM   8150  O  O     . MET B 1 322 ? 97.933  144.830 140.975 1.00 39.54 ?  322 MET B O     1 
ATOM   8151  C  CB    . MET B 1 322 ? 99.195  147.045 142.414 1.00 33.39 ?  322 MET B CB    1 
ATOM   8152  C  CG    . MET B 1 322 ? 99.073  148.550 142.627 1.00 35.60 ?  322 MET B CG    1 
ATOM   8153  S  SD    . MET B 1 322 ? 98.166  149.466 141.365 1.00 45.22 ?  322 MET B SD    1 
ATOM   8154  C  CE    . MET B 1 322 ? 98.339  148.397 139.945 1.00 36.56 ?  322 MET B CE    1 
ATOM   8155  N  N     . TYR B 1 323 ? 98.018  143.778 142.964 1.00 32.48 ?  323 TYR B N     1 
ATOM   8156  C  CA    . TYR B 1 323 ? 98.038  142.452 142.353 1.00 28.69 ?  323 TYR B CA    1 
ATOM   8157  C  C     . TYR B 1 323 ? 96.743  142.164 141.605 1.00 29.49 ?  323 TYR B C     1 
ATOM   8158  O  O     . TYR B 1 323 ? 96.768  141.630 140.489 1.00 33.38 ?  323 TYR B O     1 
ATOM   8159  C  CB    . TYR B 1 323 ? 98.288  141.389 143.424 1.00 32.87 ?  323 TYR B CB    1 
ATOM   8160  C  CG    . TYR B 1 323 ? 98.212  139.968 142.912 1.00 30.91 ?  323 TYR B CG    1 
ATOM   8161  C  CD1   . TYR B 1 323 ? 99.317  139.356 142.342 1.00 27.40 ?  323 TYR B CD1   1 
ATOM   8162  C  CD2   . TYR B 1 323 ? 97.034  139.237 143.005 1.00 30.40 ?  323 TYR B CD2   1 
ATOM   8163  C  CE1   . TYR B 1 323 ? 99.250  138.060 141.872 1.00 29.80 ?  323 TYR B CE1   1 
ATOM   8164  C  CE2   . TYR B 1 323 ? 96.958  137.943 142.539 1.00 25.97 ?  323 TYR B CE2   1 
ATOM   8165  C  CZ    . TYR B 1 323 ? 98.069  137.359 141.975 1.00 31.28 ?  323 TYR B CZ    1 
ATOM   8166  O  OH    . TYR B 1 323 ? 97.999  136.070 141.508 1.00 30.96 ?  323 TYR B OH    1 
ATOM   8167  N  N     . ASP B 1 324 ? 95.602  142.501 142.208 1.00 36.10 ?  324 ASP B N     1 
ATOM   8168  C  CA    . ASP B 1 324 ? 94.324  142.276 141.543 1.00 34.38 ?  324 ASP B CA    1 
ATOM   8169  C  C     . ASP B 1 324 ? 94.193  143.141 140.295 1.00 38.34 ?  324 ASP B C     1 
ATOM   8170  O  O     . ASP B 1 324 ? 93.642  142.699 139.281 1.00 41.12 ?  324 ASP B O     1 
ATOM   8171  C  CB    . ASP B 1 324 ? 93.176  142.544 142.514 1.00 38.72 ?  324 ASP B CB    1 
ATOM   8172  C  CG    . ASP B 1 324 ? 92.925  141.376 143.448 1.00 40.69 ?  324 ASP B CG    1 
ATOM   8173  O  OD1   . ASP B 1 324 ? 93.265  140.235 143.077 1.00 40.70 ?  324 ASP B OD1   1 
ATOM   8174  O  OD2   . ASP B 1 324 ? 92.390  141.601 144.554 1.00 42.71 -1 324 ASP B OD2   1 
ATOM   8175  N  N     . LYS B 1 325 ? 94.691  144.379 140.353 1.00 33.53 ?  325 LYS B N     1 
ATOM   8176  C  CA    . LYS B 1 325 ? 94.675  145.237 139.174 1.00 31.34 ?  325 LYS B CA    1 
ATOM   8177  C  C     . LYS B 1 325 ? 95.570  144.681 138.071 1.00 32.90 ?  325 LYS B C     1 
ATOM   8178  O  O     . LYS B 1 325 ? 95.214  144.740 136.890 1.00 40.84 ?  325 LYS B O     1 
ATOM   8179  C  CB    . LYS B 1 325 ? 95.097  146.654 139.554 1.00 36.26 ?  325 LYS B CB    1 
ATOM   8180  C  CG    . LYS B 1 325 ? 94.133  147.337 140.507 1.00 34.78 ?  325 LYS B CG    1 
ATOM   8181  C  CD    . LYS B 1 325 ? 94.748  148.578 141.121 1.00 34.18 ?  325 LYS B CD    1 
ATOM   8182  C  CE    . LYS B 1 325 ? 93.678  149.542 141.600 1.00 36.84 ?  325 LYS B CE    1 
ATOM   8183  N  NZ    . LYS B 1 325 ? 92.360  148.869 141.761 1.00 36.00 1  325 LYS B NZ    1 
ATOM   8184  N  N     . PHE B 1 326 ? 96.734  144.141 138.439 1.00 35.11 ?  326 PHE B N     1 
ATOM   8185  C  CA    . PHE B 1 326 ? 97.589  143.474 137.460 1.00 33.24 ?  326 PHE B CA    1 
ATOM   8186  C  C     . PHE B 1 326 ? 96.878  142.288 136.822 1.00 29.94 ?  326 PHE B C     1 
ATOM   8187  O  O     . PHE B 1 326 ? 96.956  142.088 135.604 1.00 36.57 ?  326 PHE B O     1 
ATOM   8188  C  CB    . PHE B 1 326 ? 98.886  143.006 138.121 1.00 30.23 ?  326 PHE B CB    1 
ATOM   8189  C  CG    . PHE B 1 326 ? 99.810  144.116 138.524 1.00 30.01 ?  326 PHE B CG    1 
ATOM   8190  C  CD1   . PHE B 1 326 ? 99.698  145.375 137.965 1.00 33.25 ?  326 PHE B CD1   1 
ATOM   8191  C  CD2   . PHE B 1 326 ? 100.797 143.894 139.470 1.00 33.29 ?  326 PHE B CD2   1 
ATOM   8192  C  CE1   . PHE B 1 326 ? 100.558 146.389 138.337 1.00 30.86 ?  326 PHE B CE1   1 
ATOM   8193  C  CE2   . PHE B 1 326 ? 101.655 144.905 139.848 1.00 33.97 ?  326 PHE B CE2   1 
ATOM   8194  C  CZ    . PHE B 1 326 ? 101.534 146.155 139.283 1.00 35.34 ?  326 PHE B CZ    1 
ATOM   8195  N  N     . VAL B 1 327 ? 96.189  141.483 137.632 1.00 31.40 ?  327 VAL B N     1 
ATOM   8196  C  CA    . VAL B 1 327 ? 95.552  140.275 137.116 1.00 34.99 ?  327 VAL B CA    1 
ATOM   8197  C  C     . VAL B 1 327 ? 94.381  140.627 136.204 1.00 36.86 ?  327 VAL B C     1 
ATOM   8198  O  O     . VAL B 1 327 ? 94.207  140.028 135.136 1.00 41.34 ?  327 VAL B O     1 
ATOM   8199  C  CB    . VAL B 1 327 ? 95.117  139.364 138.278 1.00 32.98 ?  327 VAL B CB    1 
ATOM   8200  C  CG1   . VAL B 1 327 ? 94.190  138.267 137.782 1.00 35.22 ?  327 VAL B CG1   1 
ATOM   8201  C  CG2   . VAL B 1 327 ? 96.335  138.766 138.962 1.00 29.82 ?  327 VAL B CG2   1 
ATOM   8202  N  N     . ASP B 1 328 ? 93.571  141.608 136.598 1.00 36.62 ?  328 ASP B N     1 
ATOM   8203  C  CA    . ASP B 1 328 ? 92.394  141.983 135.824 1.00 36.77 ?  328 ASP B CA    1 
ATOM   8204  C  C     . ASP B 1 328 ? 92.718  142.869 134.629 1.00 40.53 ?  328 ASP B C     1 
ATOM   8205  O  O     . ASP B 1 328 ? 91.821  143.148 133.827 1.00 43.97 ?  328 ASP B O     1 
ATOM   8206  C  CB    . ASP B 1 328 ? 91.381  142.693 136.726 1.00 38.73 ?  328 ASP B CB    1 
ATOM   8207  C  CG    . ASP B 1 328 ? 90.934  141.830 137.889 1.00 45.21 ?  328 ASP B CG    1 
ATOM   8208  O  OD1   . ASP B 1 328 ? 90.344  142.378 138.844 1.00 46.00 ?  328 ASP B OD1   1 
ATOM   8209  O  OD2   . ASP B 1 328 ? 91.174  140.605 137.848 1.00 44.15 -1 328 ASP B OD2   1 
ATOM   8210  N  N     . ASN B 1 329 ? 93.964  143.314 134.490 1.00 36.19 ?  329 ASN B N     1 
ATOM   8211  C  CA    . ASN B 1 329 ? 94.343  144.196 133.394 1.00 35.52 ?  329 ASN B CA    1 
ATOM   8212  C  C     . ASN B 1 329 ? 94.735  143.356 132.186 1.00 39.38 ?  329 ASN B C     1 
ATOM   8213  O  O     . ASN B 1 329 ? 95.724  142.613 132.259 1.00 39.32 ?  329 ASN B O     1 
ATOM   8214  C  CB    . ASN B 1 329 ? 95.501  145.089 133.812 1.00 35.64 ?  329 ASN B CB    1 
ATOM   8215  C  CG    . ASN B 1 329 ? 95.669  146.305 132.919 1.00 39.66 ?  329 ASN B CG    1 
ATOM   8216  O  OD1   . ASN B 1 329 ? 96.271  147.295 133.326 1.00 37.91 ?  329 ASN B OD1   1 
ATOM   8217  N  ND2   . ASN B 1 329 ? 95.141  146.241 131.706 1.00 42.21 ?  329 ASN B ND2   1 
ATOM   8218  N  N     . PRO B 1 330 ? 94.002  143.431 131.070 1.00 43.55 ?  330 PRO B N     1 
ATOM   8219  C  CA    . PRO B 1 330 ? 94.400  142.649 129.889 1.00 40.99 ?  330 PRO B CA    1 
ATOM   8220  C  C     . PRO B 1 330 ? 95.695  143.125 129.257 1.00 37.31 ?  330 PRO B C     1 
ATOM   8221  O  O     . PRO B 1 330 ? 96.369  142.332 128.587 1.00 39.57 ?  330 PRO B O     1 
ATOM   8222  C  CB    . PRO B 1 330 ? 93.208  142.821 128.939 1.00 41.98 ?  330 PRO B CB    1 
ATOM   8223  C  CG    . PRO B 1 330 ? 92.589  144.114 129.349 1.00 37.44 ?  330 PRO B CG    1 
ATOM   8224  C  CD    . PRO B 1 330 ? 92.768  144.200 130.837 1.00 40.19 ?  330 PRO B CD    1 
ATOM   8225  N  N     . ARG B 1 331 ? 96.069  144.391 129.445 1.00 38.79 ?  331 ARG B N     1 
ATOM   8226  C  CA    . ARG B 1 331 ? 97.307  144.911 128.879 1.00 42.17 ?  331 ARG B CA    1 
ATOM   8227  C  C     . ARG B 1 331 ? 98.538  144.502 129.675 1.00 40.20 ?  331 ARG B C     1 
ATOM   8228  O  O     . ARG B 1 331 ? 99.659  144.788 129.243 1.00 38.14 ?  331 ARG B O     1 
ATOM   8229  C  CB    . ARG B 1 331 ? 97.238  146.436 128.772 1.00 39.65 ?  331 ARG B CB    1 
ATOM   8230  C  CG    . ARG B 1 331 ? 96.280  146.930 127.702 1.00 38.38 ?  331 ARG B CG    1 
ATOM   8231  C  CD    . ARG B 1 331 ? 95.890  148.385 127.919 1.00 40.13 ?  331 ARG B CD    1 
ATOM   8232  N  NE    . ARG B 1 331 ? 95.182  148.593 129.178 1.00 42.43 ?  331 ARG B NE    1 
ATOM   8233  C  CZ    . ARG B 1 331 ? 93.944  148.183 129.424 1.00 42.33 ?  331 ARG B CZ    1 
ATOM   8234  N  NH1   . ARG B 1 331 ? 93.237  147.531 128.516 1.00 41.73 1  331 ARG B NH1   1 
ATOM   8235  N  NH2   . ARG B 1 331 ? 93.401  148.440 130.610 1.00 40.55 ?  331 ARG B NH2   1 
ATOM   8236  N  N     . VAL B 1 332 ? 98.356  143.849 130.819 1.00 38.10 ?  332 VAL B N     1 
ATOM   8237  C  CA    . VAL B 1 332 ? 99.454  143.304 131.606 1.00 33.72 ?  332 VAL B CA    1 
ATOM   8238  C  C     . VAL B 1 332 ? 99.569  141.820 131.292 1.00 34.64 ?  332 VAL B C     1 
ATOM   8239  O  O     . VAL B 1 332 ? 98.571  141.091 131.339 1.00 37.29 ?  332 VAL B O     1 
ATOM   8240  C  CB    . VAL B 1 332 ? 99.229  143.536 133.111 1.00 33.18 ?  332 VAL B CB    1 
ATOM   8241  C  CG1   . VAL B 1 332 ? 100.163 142.663 133.933 1.00 33.55 ?  332 VAL B CG1   1 
ATOM   8242  C  CG2   . VAL B 1 332 ? 99.422  145.006 133.453 1.00 33.28 ?  332 VAL B CG2   1 
ATOM   8243  N  N     . LYS B 1 333 ? 100.774 141.376 130.953 1.00 31.25 ?  333 LYS B N     1 
ATOM   8244  C  CA    . LYS B 1 333 ? 101.020 139.975 130.648 1.00 31.37 ?  333 LYS B CA    1 
ATOM   8245  C  C     . LYS B 1 333 ? 101.428 139.233 131.914 1.00 33.26 ?  333 LYS B C     1 
ATOM   8246  O  O     . LYS B 1 333 ? 102.226 139.733 132.711 1.00 34.81 ?  333 LYS B O     1 
ATOM   8247  C  CB    . LYS B 1 333 ? 102.106 139.837 129.581 1.00 26.23 ?  333 LYS B CB    1 
ATOM   8248  C  CG    . LYS B 1 333 ? 102.099 138.506 128.851 1.00 32.17 ?  333 LYS B CG    1 
ATOM   8249  C  CD    . LYS B 1 333 ? 103.263 138.405 127.881 1.00 34.40 ?  333 LYS B CD    1 
ATOM   8250  C  CE    . LYS B 1 333 ? 103.362 137.013 127.279 1.00 35.85 ?  333 LYS B CE    1 
ATOM   8251  N  NZ    . LYS B 1 333 ? 104.501 136.902 126.327 1.00 37.67 1  333 LYS B NZ    1 
ATOM   8252  N  N     . LYS B 1 334 ? 100.875 138.035 132.095 1.00 32.05 ?  334 LYS B N     1 
ATOM   8253  C  CA    . LYS B 1 334 ? 101.134 137.263 133.300 1.00 29.36 ?  334 LYS B CA    1 
ATOM   8254  C  C     . LYS B 1 334 ? 101.062 135.777 132.985 1.00 33.55 ?  334 LYS B C     1 
ATOM   8255  O  O     . LYS B 1 334 ? 100.485 135.358 131.978 1.00 35.10 ?  334 LYS B O     1 
ATOM   8256  C  CB    . LYS B 1 334 ? 100.143 137.612 134.417 1.00 31.14 ?  334 LYS B CB    1 
ATOM   8257  C  CG    . LYS B 1 334 ? 98.725  137.141 134.158 1.00 35.88 ?  334 LYS B CG    1 
ATOM   8258  C  CD    . LYS B 1 334 ? 97.706  138.157 134.635 1.00 32.50 ?  334 LYS B CD    1 
ATOM   8259  C  CE    . LYS B 1 334 ? 97.523  139.262 133.616 1.00 33.97 ?  334 LYS B CE    1 
ATOM   8260  N  NZ    . LYS B 1 334 ? 96.168  139.871 133.685 1.00 34.33 1  334 LYS B NZ    1 
ATOM   8261  N  N     . GLU B 1 335 ? 101.663 134.985 133.869 1.00 33.86 ?  335 GLU B N     1 
ATOM   8262  C  CA    . GLU B 1 335 ? 101.668 133.533 133.778 1.00 33.23 ?  335 GLU B CA    1 
ATOM   8263  C  C     . GLU B 1 335 ? 101.133 132.943 135.073 1.00 34.05 ?  335 GLU B C     1 
ATOM   8264  O  O     . GLU B 1 335 ? 101.416 133.452 136.162 1.00 40.53 ?  335 GLU B O     1 
ATOM   8265  C  CB    . GLU B 1 335 ? 103.077 132.991 133.505 1.00 29.97 ?  335 GLU B CB    1 
ATOM   8266  C  CG    . GLU B 1 335 ? 103.864 133.785 132.482 1.00 37.48 ?  335 GLU B CG    1 
ATOM   8267  C  CD    . GLU B 1 335 ? 104.660 132.900 131.544 1.00 41.55 ?  335 GLU B CD    1 
ATOM   8268  O  OE1   . GLU B 1 335 ? 105.613 132.241 132.012 1.00 36.02 ?  335 GLU B OE1   1 
ATOM   8269  O  OE2   . GLU B 1 335 ? 104.331 132.863 130.340 1.00 36.24 -1 335 GLU B OE2   1 
ATOM   8270  N  N     . LYS B 1 336 ? 100.365 131.866 134.950 1.00 33.34 ?  336 LYS B N     1 
ATOM   8271  C  CA    . LYS B 1 336 ? 99.806  131.196 136.115 1.00 29.33 ?  336 LYS B CA    1 
ATOM   8272  C  C     . LYS B 1 336 ? 100.858 130.324 136.786 1.00 35.73 ?  336 LYS B C     1 
ATOM   8273  O  O     . LYS B 1 336 ? 101.606 129.602 136.123 1.00 37.25 ?  336 LYS B O     1 
ATOM   8274  C  CB    . LYS B 1 336 ? 98.603  130.342 135.713 1.00 37.44 ?  336 LYS B CB    1 
ATOM   8275  C  CG    . LYS B 1 336 ? 97.566  130.174 136.810 1.00 41.25 ?  336 LYS B CG    1 
ATOM   8276  C  CD    . LYS B 1 336 ? 96.410  129.305 136.345 1.00 38.03 ?  336 LYS B CD    1 
ATOM   8277  C  CE    . LYS B 1 336 ? 95.076  130.001 136.550 1.00 39.22 ?  336 LYS B CE    1 
ATOM   8278  N  NZ    . LYS B 1 336 ? 95.010  130.698 137.863 1.00 39.13 1  336 LYS B NZ    1 
ATOM   8279  N  N     . ILE B 1 337 ? 100.914 130.400 138.118 1.00 36.47 ?  337 ILE B N     1 
ATOM   8280  C  CA    . ILE B 1 337 ? 101.807 129.580 138.923 1.00 34.68 ?  337 ILE B CA    1 
ATOM   8281  C  C     . ILE B 1 337 ? 101.039 129.079 140.136 1.00 35.24 ?  337 ILE B C     1 
ATOM   8282  O  O     . ILE B 1 337 ? 99.986  129.609 140.498 1.00 39.38 ?  337 ILE B O     1 
ATOM   8283  C  CB    . ILE B 1 337 ? 103.071 130.342 139.382 1.00 33.50 ?  337 ILE B CB    1 
ATOM   8284  C  CG1   . ILE B 1 337 ? 102.680 131.604 140.155 1.00 33.10 ?  337 ILE B CG1   1 
ATOM   8285  C  CG2   . ILE B 1 337 ? 103.961 130.683 138.198 1.00 35.27 ?  337 ILE B CG2   1 
ATOM   8286  C  CD1   . ILE B 1 337 ? 103.589 131.910 141.321 1.00 31.75 ?  337 ILE B CD1   1 
ATOM   8287  N  N     . ASN B 1 338 ? 101.578 128.039 140.765 1.00 35.06 ?  338 ASN B N     1 
ATOM   8288  C  CA    . ASN B 1 338 ? 101.049 127.566 142.033 1.00 34.44 ?  338 ASN B CA    1 
ATOM   8289  C  C     . ASN B 1 338 ? 101.922 128.117 143.147 1.00 34.15 ?  338 ASN B C     1 
ATOM   8290  O  O     . ASN B 1 338 ? 103.082 127.698 143.274 1.00 37.77 ?  338 ASN B O     1 
ATOM   8291  C  CB    . ASN B 1 338 ? 101.023 126.040 142.077 1.00 32.16 ?  338 ASN B CB    1 
ATOM   8292  C  CG    . ASN B 1 338 ? 100.109 125.502 143.162 1.00 35.79 ?  338 ASN B CG    1 
ATOM   8293  O  OD1   . ASN B 1 338 ? 100.048 124.295 143.395 1.00 38.49 ?  338 ASN B OD1   1 
ATOM   8294  N  ND2   . ASN B 1 338 ? 99.388  126.396 143.826 1.00 37.38 ?  338 ASN B ND2   1 
ATOM   8295  N  N     . PRO B 1 339 ? 101.432 129.058 143.960 1.00 33.80 ?  339 PRO B N     1 
ATOM   8296  C  CA    . PRO B 1 339 ? 102.285 129.627 145.016 1.00 28.56 ?  339 PRO B CA    1 
ATOM   8297  C  C     . PRO B 1 339 ? 102.778 128.599 146.018 1.00 32.53 ?  339 PRO B C     1 
ATOM   8298  O  O     . PRO B 1 339 ? 103.903 128.728 146.516 1.00 35.56 ?  339 PRO B O     1 
ATOM   8299  C  CB    . PRO B 1 339 ? 101.376 130.673 145.676 1.00 29.85 ?  339 PRO B CB    1 
ATOM   8300  C  CG    . PRO B 1 339 ? 99.989  130.273 145.304 1.00 33.77 ?  339 PRO B CG    1 
ATOM   8301  C  CD    . PRO B 1 339 ? 100.090 129.659 143.946 1.00 33.82 ?  339 PRO B CD    1 
ATOM   8302  N  N     . ARG B 1 340 ? 101.977 127.577 146.329 1.00 31.45 ?  340 ARG B N     1 
ATOM   8303  C  CA    . ARG B 1 340 ? 102.447 126.526 147.224 1.00 28.07 ?  340 ARG B CA    1 
ATOM   8304  C  C     . ARG B 1 340 ? 103.545 125.697 146.570 1.00 31.70 ?  340 ARG B C     1 
ATOM   8305  O  O     . ARG B 1 340 ? 104.515 125.311 147.231 1.00 34.63 ?  340 ARG B O     1 
ATOM   8306  C  CB    . ARG B 1 340 ? 101.281 125.640 147.656 1.00 31.53 ?  340 ARG B CB    1 
ATOM   8307  C  CG    . ARG B 1 340 ? 100.387 126.290 148.692 1.00 29.55 ?  340 ARG B CG    1 
ATOM   8308  C  CD    . ARG B 1 340 ? 99.623  125.268 149.511 1.00 28.13 ?  340 ARG B CD    1 
ATOM   8309  N  NE    . ARG B 1 340 ? 98.678  125.916 150.413 1.00 31.78 ?  340 ARG B NE    1 
ATOM   8310  C  CZ    . ARG B 1 340 ? 97.858  125.274 151.232 1.00 34.23 ?  340 ARG B CZ    1 
ATOM   8311  N  NH1   . ARG B 1 340 ? 97.842  123.953 151.297 1.00 34.73 1  340 ARG B NH1   1 
ATOM   8312  N  NH2   . ARG B 1 340 ? 97.034  125.974 152.005 1.00 34.57 ?  340 ARG B NH2   1 
ATOM   8313  N  N     . LYS B 1 341 ? 103.414 125.418 145.271 1.00 30.60 ?  341 LYS B N     1 
ATOM   8314  C  CA    . LYS B 1 341 ? 104.485 124.728 144.562 1.00 27.34 ?  341 LYS B CA    1 
ATOM   8315  C  C     . LYS B 1 341 ? 105.748 125.575 144.506 1.00 30.08 ?  341 LYS B C     1 
ATOM   8316  O  O     . LYS B 1 341 ? 106.856 125.041 144.609 1.00 29.73 ?  341 LYS B O     1 
ATOM   8317  C  CB    . LYS B 1 341 ? 104.036 124.351 143.149 1.00 35.91 ?  341 LYS B CB    1 
ATOM   8318  C  CG    . LYS B 1 341 ? 103.071 123.172 143.070 1.00 37.10 ?  341 LYS B CG    1 
ATOM   8319  C  CD    . LYS B 1 341 ? 103.095 122.314 144.325 1.00 34.20 ?  341 LYS B CD    1 
ATOM   8320  C  CE    . LYS B 1 341 ? 102.687 120.881 144.021 1.00 36.14 ?  341 LYS B CE    1 
ATOM   8321  N  NZ    . LYS B 1 341 ? 101.333 120.805 143.405 1.00 33.97 1  341 LYS B NZ    1 
ATOM   8322  N  N     . LEU B 1 342 ? 105.604 126.892 144.349 1.00 29.26 ?  342 LEU B N     1 
ATOM   8323  C  CA    . LEU B 1 342 ? 106.771 127.768 144.368 1.00 26.52 ?  342 LEU B CA    1 
ATOM   8324  C  C     . LEU B 1 342 ? 107.427 127.782 145.744 1.00 30.91 ?  342 LEU B C     1 
ATOM   8325  O  O     . LEU B 1 342 ? 108.658 127.792 145.850 1.00 37.75 ?  342 LEU B O     1 
ATOM   8326  C  CB    . LEU B 1 342 ? 106.375 129.179 143.941 1.00 30.07 ?  342 LEU B CB    1 
ATOM   8327  C  CG    . LEU B 1 342 ? 107.518 130.115 143.541 1.00 27.23 ?  342 LEU B CG    1 
ATOM   8328  C  CD1   . LEU B 1 342 ? 108.537 129.382 142.685 1.00 25.62 ?  342 LEU B CD1   1 
ATOM   8329  C  CD2   . LEU B 1 342 ? 106.977 131.332 142.810 1.00 26.81 ?  342 LEU B CD2   1 
ATOM   8330  N  N     . LEU B 1 343 ? 106.623 127.782 146.811 1.00 29.53 ?  343 LEU B N     1 
ATOM   8331  C  CA    . LEU B 1 343 ? 107.176 127.698 148.159 1.00 26.59 ?  343 LEU B CA    1 
ATOM   8332  C  C     . LEU B 1 343 ? 107.916 126.384 148.373 1.00 28.70 ?  343 LEU B C     1 
ATOM   8333  O  O     . LEU B 1 343 ? 108.994 126.357 148.979 1.00 33.74 ?  343 LEU B O     1 
ATOM   8334  C  CB    . LEU B 1 343 ? 106.062 127.854 149.192 1.00 30.61 ?  343 LEU B CB    1 
ATOM   8335  C  CG    . LEU B 1 343 ? 105.840 129.254 149.760 1.00 30.70 ?  343 LEU B CG    1 
ATOM   8336  C  CD1   . LEU B 1 343 ? 104.814 129.210 150.879 1.00 27.27 ?  343 LEU B CD1   1 
ATOM   8337  C  CD2   . LEU B 1 343 ? 107.151 129.846 150.247 1.00 30.33 ?  343 LEU B CD2   1 
ATOM   8338  N  N     . GLU B 1 344 ? 107.343 125.278 147.893 1.00 30.95 ?  344 GLU B N     1 
ATOM   8339  C  CA    . GLU B 1 344 ? 108.013 123.988 148.011 1.00 28.52 ?  344 GLU B CA    1 
ATOM   8340  C  C     . GLU B 1 344 ? 109.304 123.962 147.204 1.00 29.40 ?  344 GLU B C     1 
ATOM   8341  O  O     . GLU B 1 344 ? 110.294 123.358 147.628 1.00 34.84 ?  344 GLU B O     1 
ATOM   8342  C  CB    . GLU B 1 344 ? 107.075 122.865 147.572 1.00 30.80 ?  344 GLU B CB    1 
ATOM   8343  C  CG    . GLU B 1 344 ? 105.890 122.656 148.499 1.00 33.67 ?  344 GLU B CG    1 
ATOM   8344  C  CD    . GLU B 1 344 ? 104.781 121.853 147.854 1.00 38.15 ?  344 GLU B CD    1 
ATOM   8345  O  OE1   . GLU B 1 344 ? 105.003 121.317 146.749 1.00 39.86 ?  344 GLU B OE1   1 
ATOM   8346  O  OE2   . GLU B 1 344 ? 103.687 121.761 148.449 1.00 37.98 -1 344 GLU B OE2   1 
ATOM   8347  N  N     . LYS B 1 345 ? 109.311 124.609 146.037 1.00 29.24 ?  345 LYS B N     1 
ATOM   8348  C  CA    . LYS B 1 345 ? 110.540 124.724 145.258 1.00 27.16 ?  345 LYS B CA    1 
ATOM   8349  C  C     . LYS B 1 345 ? 111.590 125.533 146.007 1.00 30.72 ?  345 LYS B C     1 
ATOM   8350  O  O     . LYS B 1 345 ? 112.777 125.191 145.989 1.00 32.03 ?  345 LYS B O     1 
ATOM   8351  C  CB    . LYS B 1 345 ? 110.245 125.355 143.898 1.00 26.14 ?  345 LYS B CB    1 
ATOM   8352  C  CG    . LYS B 1 345 ? 111.461 125.475 142.999 1.00 29.85 ?  345 LYS B CG    1 
ATOM   8353  C  CD    . LYS B 1 345 ? 111.093 126.030 141.635 1.00 30.37 ?  345 LYS B CD    1 
ATOM   8354  C  CE    . LYS B 1 345 ? 112.311 126.103 140.730 1.00 30.62 ?  345 LYS B CE    1 
ATOM   8355  N  NZ    . LYS B 1 345 ? 111.985 126.672 139.396 1.00 31.25 1  345 LYS B NZ    1 
ATOM   8356  N  N     . LEU B 1 346 ? 111.171 126.615 146.669 1.00 29.75 ?  346 LEU B N     1 
ATOM   8357  C  CA    . LEU B 1 346 ? 112.096 127.393 147.487 1.00 23.48 ?  346 LEU B CA    1 
ATOM   8358  C  C     . LEU B 1 346 ? 112.689 126.538 148.599 1.00 27.62 ?  346 LEU B C     1 
ATOM   8359  O  O     . LEU B 1 346 ? 113.900 126.569 148.846 1.00 30.54 ?  346 LEU B O     1 
ATOM   8360  C  CB    . LEU B 1 346 ? 111.384 128.608 148.084 1.00 24.10 ?  346 LEU B CB    1 
ATOM   8361  C  CG    . LEU B 1 346 ? 110.852 129.705 147.161 1.00 26.77 ?  346 LEU B CG    1 
ATOM   8362  C  CD1   . LEU B 1 346 ? 110.075 130.731 147.965 1.00 28.15 ?  346 LEU B CD1   1 
ATOM   8363  C  CD2   . LEU B 1 346 ? 111.983 130.369 146.412 1.00 26.32 ?  346 LEU B CD2   1 
ATOM   8364  N  N     . ALA B 1 347 ? 111.843 125.763 149.280 1.00 26.89 ?  347 ALA B N     1 
ATOM   8365  C  CA    . ALA B 1 347 ? 112.322 124.914 150.367 1.00 20.29 ?  347 ALA B CA    1 
ATOM   8366  C  C     . ALA B 1 347 ? 113.276 123.841 149.856 1.00 29.91 ?  347 ALA B C     1 
ATOM   8367  O  O     . ALA B 1 347 ? 114.307 123.571 150.483 1.00 35.16 ?  347 ALA B O     1 
ATOM   8368  C  CB    . ALA B 1 347 ? 111.140 124.279 151.096 1.00 22.69 ?  347 ALA B CB    1 
ATOM   8369  N  N     . MET B 1 348 ? 112.952 123.222 148.719 1.00 31.69 ?  348 MET B N     1 
ATOM   8370  C  CA    . MET B 1 348 ? 113.834 122.212 148.142 1.00 29.01 ?  348 MET B CA    1 
ATOM   8371  C  C     . MET B 1 348 ? 115.172 122.814 147.736 1.00 31.20 ?  348 MET B C     1 
ATOM   8372  O  O     . MET B 1 348 ? 116.228 122.222 147.983 1.00 35.64 ?  348 MET B O     1 
ATOM   8373  C  CB    . MET B 1 348 ? 113.153 121.553 146.943 1.00 31.96 ?  348 MET B CB    1 
ATOM   8374  C  CG    . MET B 1 348 ? 114.092 120.768 146.040 1.00 38.36 ?  348 MET B CG    1 
ATOM   8375  S  SD    . MET B 1 348 ? 114.321 121.552 144.432 1.00 53.07 ?  348 MET B SD    1 
ATOM   8376  C  CE    . MET B 1 348 ? 112.641 121.557 143.815 1.00 37.32 ?  348 MET B CE    1 
ATOM   8377  N  N     . LEU B 1 349 ? 115.148 123.996 147.117 1.00 28.67 ?  349 LEU B N     1 
ATOM   8378  C  CA    . LEU B 1 349 ? 116.387 124.654 146.721 1.00 25.58 ?  349 LEU B CA    1 
ATOM   8379  C  C     . LEU B 1 349 ? 117.235 125.007 147.934 1.00 25.72 ?  349 LEU B C     1 
ATOM   8380  O  O     . LEU B 1 349 ? 118.462 124.858 147.906 1.00 30.40 ?  349 LEU B O     1 
ATOM   8381  C  CB    . LEU B 1 349 ? 116.075 125.908 145.906 1.00 30.48 ?  349 LEU B CB    1 
ATOM   8382  C  CG    . LEU B 1 349 ? 116.429 125.889 144.421 1.00 31.43 ?  349 LEU B CG    1 
ATOM   8383  C  CD1   . LEU B 1 349 ? 115.349 125.184 143.618 1.00 31.89 ?  349 LEU B CD1   1 
ATOM   8384  C  CD2   . LEU B 1 349 ? 116.636 127.307 143.926 1.00 28.13 ?  349 LEU B CD2   1 
ATOM   8385  N  N     . ARG B 1 350 ? 116.603 125.493 149.004 1.00 25.07 ?  350 ARG B N     1 
ATOM   8386  C  CA    . ARG B 1 350 ? 117.353 125.825 150.210 1.00 25.84 ?  350 ARG B CA    1 
ATOM   8387  C  C     . ARG B 1 350 ? 117.911 124.580 150.884 1.00 28.68 ?  350 ARG B C     1 
ATOM   8388  O  O     . ARG B 1 350 ? 119.003 124.627 151.461 1.00 33.54 ?  350 ARG B O     1 
ATOM   8389  C  CB    . ARG B 1 350 ? 116.472 126.616 151.175 1.00 22.89 ?  350 ARG B CB    1 
ATOM   8390  C  CG    . ARG B 1 350 ? 116.100 128.001 150.672 1.00 23.30 ?  350 ARG B CG    1 
ATOM   8391  C  CD    . ARG B 1 350 ? 115.041 128.646 151.546 1.00 23.06 ?  350 ARG B CD    1 
ATOM   8392  N  NE    . ARG B 1 350 ? 115.462 128.723 152.939 1.00 34.99 ?  350 ARG B NE    1 
ATOM   8393  C  CZ    . ARG B 1 350 ? 116.331 129.605 153.413 1.00 31.12 ?  350 ARG B CZ    1 
ATOM   8394  N  NH1   . ARG B 1 350 ? 116.889 130.516 152.633 1.00 26.96 1  350 ARG B NH1   1 
ATOM   8395  N  NH2   . ARG B 1 350 ? 116.649 129.572 154.703 1.00 27.93 ?  350 ARG B NH2   1 
ATOM   8396  N  N     . SER B 1 351 ? 117.181 123.466 150.836 1.00 28.79 ?  351 SER B N     1 
ATOM   8397  C  CA    . SER B 1 351 ? 117.718 122.214 151.357 1.00 29.95 ?  351 SER B CA    1 
ATOM   8398  C  C     . SER B 1 351 ? 118.920 121.748 150.545 1.00 33.63 ?  351 SER B C     1 
ATOM   8399  O  O     . SER B 1 351 ? 119.919 121.290 151.111 1.00 40.76 ?  351 SER B O     1 
ATOM   8400  C  CB    . SER B 1 351 ? 116.631 121.141 151.372 1.00 31.21 ?  351 SER B CB    1 
ATOM   8401  O  OG    . SER B 1 351 ? 115.498 121.572 152.104 1.00 36.59 ?  351 SER B OG    1 
ATOM   8402  N  N     . GLU B 1 352 ? 118.843 121.860 149.218 1.00 31.55 ?  352 GLU B N     1 
ATOM   8403  C  CA    . GLU B 1 352 ? 119.921 121.357 148.372 1.00 30.05 ?  352 GLU B CA    1 
ATOM   8404  C  C     . GLU B 1 352 ? 121.164 122.238 148.446 1.00 35.96 ?  352 GLU B C     1 
ATOM   8405  O  O     . GLU B 1 352 ? 122.283 121.725 148.569 1.00 39.68 ?  352 GLU B O     1 
ATOM   8406  C  CB    . GLU B 1 352 ? 119.441 121.231 146.925 1.00 34.33 ?  352 GLU B CB    1 
ATOM   8407  C  CG    . GLU B 1 352 ? 118.298 120.251 146.730 1.00 36.76 ?  352 GLU B CG    1 
ATOM   8408  C  CD    . GLU B 1 352 ? 117.748 120.272 145.319 1.00 41.55 ?  352 GLU B CD    1 
ATOM   8409  O  OE1   . GLU B 1 352 ? 117.817 121.335 144.668 1.00 38.58 ?  352 GLU B OE1   1 
ATOM   8410  O  OE2   . GLU B 1 352 ? 117.245 119.225 144.860 1.00 41.64 -1 352 GLU B OE2   1 
ATOM   8411  N  N     . SER B 1 353 ? 120.997 123.561 148.374 1.00 34.01 ?  353 SER B N     1 
ATOM   8412  C  CA    . SER B 1 353 ? 122.134 124.461 148.239 1.00 35.75 ?  353 SER B CA    1 
ATOM   8413  C  C     . SER B 1 353 ? 122.123 125.651 149.190 1.00 31.83 ?  353 SER B C     1 
ATOM   8414  O  O     . SER B 1 353 ? 123.080 126.432 149.178 1.00 34.71 ?  353 SER B O     1 
ATOM   8415  C  CB    . SER B 1 353 ? 122.227 124.983 146.797 1.00 35.48 ?  353 SER B CB    1 
ATOM   8416  O  OG    . SER B 1 353 ? 121.114 125.799 146.479 1.00 36.62 ?  353 SER B OG    1 
ATOM   8417  N  N     . GLY B 1 354 ? 121.084 125.818 150.005 1.00 22.19 ?  354 GLY B N     1 
ATOM   8418  C  CA    . GLY B 1 354 ? 121.005 126.959 150.892 1.00 23.41 ?  354 GLY B CA    1 
ATOM   8419  C  C     . GLY B 1 354 ? 120.481 128.229 150.261 1.00 21.72 ?  354 GLY B C     1 
ATOM   8420  O  O     . GLY B 1 354 ? 120.374 129.247 150.956 1.00 28.76 ?  354 GLY B O     1 
ATOM   8421  N  N     . TYR B 1 355 ? 120.150 128.203 148.979 1.00 25.60 ?  355 TYR B N     1 
ATOM   8422  C  CA    . TYR B 1 355 ? 119.608 129.329 148.243 1.00 17.85 ?  355 TYR B CA    1 
ATOM   8423  C  C     . TYR B 1 355 ? 118.151 129.068 147.889 1.00 20.21 ?  355 TYR B C     1 
ATOM   8424  O  O     . TYR B 1 355 ? 117.726 127.913 147.796 1.00 28.32 ?  355 TYR B O     1 
ATOM   8425  C  CB    . TYR B 1 355 ? 120.420 129.568 146.963 1.00 22.73 ?  355 TYR B CB    1 
ATOM   8426  C  CG    . TYR B 1 355 ? 121.818 130.076 147.216 1.00 25.91 ?  355 TYR B CG    1 
ATOM   8427  C  CD1   . TYR B 1 355 ? 122.036 131.206 147.990 1.00 23.53 ?  355 TYR B CD1   1 
ATOM   8428  C  CD2   . TYR B 1 355 ? 122.922 129.423 146.683 1.00 26.75 ?  355 TYR B CD2   1 
ATOM   8429  C  CE1   . TYR B 1 355 ? 123.310 131.673 148.225 1.00 26.24 ?  355 TYR B CE1   1 
ATOM   8430  C  CE2   . TYR B 1 355 ? 124.201 129.883 146.914 1.00 28.07 ?  355 TYR B CE2   1 
ATOM   8431  C  CZ    . TYR B 1 355 ? 124.389 131.010 147.686 1.00 29.17 ?  355 TYR B CZ    1 
ATOM   8432  O  OH    . TYR B 1 355 ? 125.662 131.474 147.920 1.00 30.83 ?  355 TYR B OH    1 
ATOM   8433  N  N     . PRO B 1 356 ? 117.346 130.116 147.674 1.00 21.44 ?  356 PRO B N     1 
ATOM   8434  C  CA    . PRO B 1 356 ? 117.655 131.550 147.709 1.00 17.78 ?  356 PRO B CA    1 
ATOM   8435  C  C     . PRO B 1 356 ? 117.614 132.174 149.095 1.00 17.32 ?  356 PRO B C     1 
ATOM   8436  O  O     . PRO B 1 356 ? 117.104 131.591 150.046 1.00 20.04 ?  356 PRO B O     1 
ATOM   8437  C  CB    . PRO B 1 356 ? 116.555 132.142 146.826 1.00 16.77 ?  356 PRO B CB    1 
ATOM   8438  C  CG    . PRO B 1 356 ? 115.376 131.275 147.131 1.00 19.79 ?  356 PRO B CG    1 
ATOM   8439  C  CD    . PRO B 1 356 ? 115.943 129.883 147.289 1.00 17.79 ?  356 PRO B CD    1 
ATOM   8440  N  N     . TYR B 1 357 ? 118.163 133.378 149.223 1.00 23.57 ?  357 TYR B N     1 
ATOM   8441  C  CA    . TYR B 1 357 ? 117.832 134.220 150.360 1.00 11.38 ?  357 TYR B CA    1 
ATOM   8442  C  C     . TYR B 1 357 ? 116.361 134.600 150.283 1.00 17.94 ?  357 TYR B C     1 
ATOM   8443  O  O     . TYR B 1 357 ? 115.822 134.836 149.199 1.00 26.55 ?  357 TYR B O     1 
ATOM   8444  C  CB    . TYR B 1 357 ? 118.697 135.481 150.373 1.00 16.41 ?  357 TYR B CB    1 
ATOM   8445  C  CG    . TYR B 1 357 ? 120.182 135.236 150.233 1.00 21.16 ?  357 TYR B CG    1 
ATOM   8446  C  CD1   . TYR B 1 357 ? 120.769 134.094 150.753 1.00 15.33 ?  357 TYR B CD1   1 
ATOM   8447  C  CD2   . TYR B 1 357 ? 120.998 136.150 149.581 1.00 20.38 ?  357 TYR B CD2   1 
ATOM   8448  C  CE1   . TYR B 1 357 ? 122.121 133.866 150.633 1.00 20.34 ?  357 TYR B CE1   1 
ATOM   8449  C  CE2   . TYR B 1 357 ? 122.354 135.931 149.453 1.00 15.32 ?  357 TYR B CE2   1 
ATOM   8450  C  CZ    . TYR B 1 357 ? 122.911 134.786 149.982 1.00 21.33 ?  357 TYR B CZ    1 
ATOM   8451  O  OH    . TYR B 1 357 ? 124.261 134.559 149.861 1.00 31.57 ?  357 TYR B OH    1 
ATOM   8452  N  N     . ILE B 1 358 ? 115.704 134.650 151.434 1.00 15.26 ?  358 ILE B N     1 
ATOM   8453  C  CA    . ILE B 1 358 ? 114.288 134.983 151.509 1.00 14.09 ?  358 ILE B CA    1 
ATOM   8454  C  C     . ILE B 1 358 ? 114.164 136.350 152.160 1.00 15.26 ?  358 ILE B C     1 
ATOM   8455  O  O     . ILE B 1 358 ? 114.634 136.554 153.284 1.00 24.51 ?  358 ILE B O     1 
ATOM   8456  C  CB    . ILE B 1 358 ? 113.494 133.925 152.289 1.00 23.12 ?  358 ILE B CB    1 
ATOM   8457  C  CG1   . ILE B 1 358 ? 113.571 132.570 151.584 1.00 15.21 ?  358 ILE B CG1   1 
ATOM   8458  C  CG2   . ILE B 1 358 ? 112.048 134.360 152.445 1.00 16.12 ?  358 ILE B CG2   1 
ATOM   8459  C  CD1   . ILE B 1 358 ? 113.028 132.585 150.174 1.00 19.53 ?  358 ILE B CD1   1 
ATOM   8460  N  N     . MET B 1 359 ? 113.538 137.286 151.452 1.00 17.72 ?  359 MET B N     1 
ATOM   8461  C  CA    . MET B 1 359 ? 113.269 138.624 151.968 1.00 7.28  ?  359 MET B CA    1 
ATOM   8462  C  C     . MET B 1 359 ? 111.762 138.822 152.002 1.00 9.30  ?  359 MET B C     1 
ATOM   8463  O  O     . MET B 1 359 ? 111.116 138.894 150.951 1.00 20.49 ?  359 MET B O     1 
ATOM   8464  C  CB    . MET B 1 359 ? 113.942 139.695 151.114 1.00 8.65  ?  359 MET B CB    1 
ATOM   8465  C  CG    . MET B 1 359 ? 113.847 141.091 151.704 1.00 9.10  ?  359 MET B CG    1 
ATOM   8466  S  SD    . MET B 1 359 ? 113.787 142.383 150.454 1.00 32.53 ?  359 MET B SD    1 
ATOM   8467  C  CE    . MET B 1 359 ? 112.798 143.614 151.290 1.00 9.56  ?  359 MET B CE    1 
ATOM   8468  N  N     . PHE B 1 360 ? 111.202 138.904 153.204 1.00 10.36 ?  360 PHE B N     1 
ATOM   8469  C  CA    . PHE B 1 360 ? 109.775 139.162 153.371 1.00 10.65 ?  360 PHE B CA    1 
ATOM   8470  C  C     . PHE B 1 360 ? 109.563 140.664 153.253 1.00 16.04 ?  360 PHE B C     1 
ATOM   8471  O  O     . PHE B 1 360 ? 109.750 141.409 154.217 1.00 19.76 ?  360 PHE B O     1 
ATOM   8472  C  CB    . PHE B 1 360 ? 109.287 138.615 154.705 1.00 12.02 ?  360 PHE B CB    1 
ATOM   8473  C  CG    . PHE B 1 360 ? 109.380 137.121 154.809 1.00 15.34 ?  360 PHE B CG    1 
ATOM   8474  C  CD1   . PHE B 1 360 ? 108.659 136.307 153.951 1.00 15.19 ?  360 PHE B CD1   1 
ATOM   8475  C  CD2   . PHE B 1 360 ? 110.204 136.529 155.751 1.00 14.96 ?  360 PHE B CD2   1 
ATOM   8476  C  CE1   . PHE B 1 360 ? 108.751 134.932 154.040 1.00 13.79 ?  360 PHE B CE1   1 
ATOM   8477  C  CE2   . PHE B 1 360 ? 110.298 135.155 155.844 1.00 14.37 ?  360 PHE B CE2   1 
ATOM   8478  C  CZ    . PHE B 1 360 ? 109.570 134.356 154.988 1.00 17.05 ?  360 PHE B CZ    1 
ATOM   8479  N  N     . GLN B 1 361 ? 109.163 141.106 152.056 1.00 16.85 ?  361 GLN B N     1 
ATOM   8480  C  CA    . GLN B 1 361 ? 109.143 142.532 151.740 1.00 9.93  ?  361 GLN B CA    1 
ATOM   8481  C  C     . GLN B 1 361 ? 108.217 143.306 152.668 1.00 13.61 ?  361 GLN B C     1 
ATOM   8482  O  O     . GLN B 1 361 ? 108.564 144.397 153.136 1.00 15.15 ?  361 GLN B O     1 
ATOM   8483  C  CB    . GLN B 1 361 ? 108.722 142.728 150.284 1.00 15.59 ?  361 GLN B CB    1 
ATOM   8484  C  CG    . GLN B 1 361 ? 108.764 144.164 149.804 1.00 15.46 ?  361 GLN B CG    1 
ATOM   8485  C  CD    . GLN B 1 361 ? 108.904 144.265 148.302 1.00 17.89 ?  361 GLN B CD    1 
ATOM   8486  O  OE1   . GLN B 1 361 ? 108.326 143.473 147.560 1.00 27.70 ?  361 GLN B OE1   1 
ATOM   8487  N  NE2   . GLN B 1 361 ? 109.677 145.241 147.843 1.00 18.34 ?  361 GLN B NE2   1 
ATOM   8488  N  N     . ASP B 1 362 ? 107.029 142.763 152.942 1.00 20.04 ?  362 ASP B N     1 
ATOM   8489  C  CA    . ASP B 1 362 ? 106.086 143.471 153.798 1.00 15.90 ?  362 ASP B CA    1 
ATOM   8490  C  C     . ASP B 1 362 ? 106.570 143.532 155.240 1.00 16.17 ?  362 ASP B C     1 
ATOM   8491  O  O     . ASP B 1 362 ? 106.338 144.534 155.923 1.00 23.66 ?  362 ASP B O     1 
ATOM   8492  C  CB    . ASP B 1 362 ? 104.710 142.816 153.720 1.00 22.13 ?  362 ASP B CB    1 
ATOM   8493  C  CG    . ASP B 1 362 ? 103.941 143.230 152.483 1.00 29.34 ?  362 ASP B CG    1 
ATOM   8494  O  OD1   . ASP B 1 362 ? 104.262 142.728 151.386 1.00 29.39 ?  362 ASP B OD1   1 
ATOM   8495  O  OD2   . ASP B 1 362 ? 103.016 144.059 152.607 1.00 30.44 -1 362 ASP B OD2   1 
ATOM   8496  N  N     . ASN B 1 363 ? 107.247 142.486 155.715 1.00 21.55 ?  363 ASN B N     1 
ATOM   8497  C  CA    . ASN B 1 363 ? 107.843 142.539 157.045 1.00 10.88 ?  363 ASN B CA    1 
ATOM   8498  C  C     . ASN B 1 363 ? 108.905 143.625 157.133 1.00 14.86 ?  363 ASN B C     1 
ATOM   8499  O  O     . ASN B 1 363 ? 109.057 144.265 158.180 1.00 25.42 ?  363 ASN B O     1 
ATOM   8500  C  CB    . ASN B 1 363 ? 108.446 141.182 157.408 1.00 12.50 ?  363 ASN B CB    1 
ATOM   8501  C  CG    . ASN B 1 363 ? 107.394 140.156 157.769 1.00 16.62 ?  363 ASN B CG    1 
ATOM   8502  O  OD1   . ASN B 1 363 ? 106.273 140.503 158.133 1.00 21.40 ?  363 ASN B OD1   1 
ATOM   8503  N  ND2   . ASN B 1 363 ? 107.751 138.883 157.667 1.00 15.52 ?  363 ASN B ND2   1 
ATOM   8504  N  N     . VAL B 1 364 ? 109.653 143.842 156.050 1.00 14.12 ?  364 VAL B N     1 
ATOM   8505  C  CA    . VAL B 1 364 ? 110.654 144.901 156.033 1.00 9.03  ?  364 VAL B CA    1 
ATOM   8506  C  C     . VAL B 1 364 ? 109.988 146.271 156.007 1.00 16.84 ?  364 VAL B C     1 
ATOM   8507  O  O     . VAL B 1 364 ? 110.408 147.193 156.717 1.00 18.99 ?  364 VAL B O     1 
ATOM   8508  C  CB    . VAL B 1 364 ? 111.603 144.717 154.835 1.00 2.44  ?  364 VAL B CB    1 
ATOM   8509  C  CG1   . VAL B 1 364 ? 112.691 145.771 154.858 1.00 6.38  ?  364 VAL B CG1   1 
ATOM   8510  C  CG2   . VAL B 1 364 ? 112.205 143.327 154.847 1.00 9.06  ?  364 VAL B CG2   1 
ATOM   8511  N  N     . ASN B 1 365 ? 108.944 146.431 155.197 1.00 18.91 ?  365 ASN B N     1 
ATOM   8512  C  CA    . ASN B 1 365 ? 108.390 147.750 154.926 1.00 7.74  ?  365 ASN B CA    1 
ATOM   8513  C  C     . ASN B 1 365 ? 107.287 148.170 155.888 1.00 15.37 ?  365 ASN B C     1 
ATOM   8514  O  O     . ASN B 1 365 ? 106.889 149.339 155.864 1.00 22.95 ?  365 ASN B O     1 
ATOM   8515  C  CB    . ASN B 1 365 ? 107.860 147.813 153.491 1.00 11.88 ?  365 ASN B CB    1 
ATOM   8516  C  CG    . ASN B 1 365 ? 108.970 147.848 152.465 1.00 13.44 ?  365 ASN B CG    1 
ATOM   8517  O  OD1   . ASN B 1 365 ? 109.888 148.661 152.556 1.00 15.79 ?  365 ASN B OD1   1 
ATOM   8518  N  ND2   . ASN B 1 365 ? 108.895 146.964 151.481 1.00 19.25 ?  365 ASN B ND2   1 
ATOM   8519  N  N     . LYS B 1 366 ? 106.781 147.267 156.729 1.00 15.39 ?  366 LYS B N     1 
ATOM   8520  C  CA    . LYS B 1 366 ? 105.797 147.673 157.723 1.00 17.04 ?  366 LYS B CA    1 
ATOM   8521  C  C     . LYS B 1 366 ? 106.428 148.434 158.879 1.00 19.24 ?  366 LYS B C     1 
ATOM   8522  O  O     . LYS B 1 366 ? 105.724 149.173 159.576 1.00 26.94 ?  366 LYS B O     1 
ATOM   8523  C  CB    . LYS B 1 366 ? 105.041 146.452 158.255 1.00 18.92 ?  366 LYS B CB    1 
ATOM   8524  C  CG    . LYS B 1 366 ? 105.916 145.425 158.955 1.00 22.26 ?  366 LYS B CG    1 
ATOM   8525  C  CD    . LYS B 1 366 ? 105.100 144.533 159.882 1.00 24.45 ?  366 LYS B CD    1 
ATOM   8526  C  CE    . LYS B 1 366 ? 103.753 144.166 159.275 1.00 24.01 ?  366 LYS B CE    1 
ATOM   8527  N  NZ    . LYS B 1 366 ? 103.880 143.156 158.189 1.00 24.16 1  366 LYS B NZ    1 
ATOM   8528  N  N     . VAL B 1 367 ? 107.731 148.271 159.093 1.00 24.11 ?  367 VAL B N     1 
ATOM   8529  C  CA    . VAL B 1 367 ? 108.471 149.017 160.100 1.00 14.42 ?  367 VAL B CA    1 
ATOM   8530  C  C     . VAL B 1 367 ? 109.586 149.852 159.495 1.00 16.80 ?  367 VAL B C     1 
ATOM   8531  O  O     . VAL B 1 367 ? 110.349 150.477 160.238 1.00 22.49 ?  367 VAL B O     1 
ATOM   8532  C  CB    . VAL B 1 367 ? 109.034 148.084 161.191 1.00 12.46 ?  367 VAL B CB    1 
ATOM   8533  C  CG1   . VAL B 1 367 ? 107.900 147.404 161.938 1.00 19.88 ?  367 VAL B CG1   1 
ATOM   8534  C  CG2   . VAL B 1 367 ? 109.959 147.054 160.574 1.00 9.76  ?  367 VAL B CG2   1 
ATOM   8535  N  N     . HIS B 1 368 ? 109.706 149.876 158.170 1.00 20.92 ?  368 HIS B N     1 
ATOM   8536  C  CA    . HIS B 1 368 ? 110.720 150.686 157.510 1.00 5.32  ?  368 HIS B CA    1 
ATOM   8537  C  C     . HIS B 1 368 ? 110.450 152.164 157.754 1.00 15.48 ?  368 HIS B C     1 
ATOM   8538  O  O     . HIS B 1 368 ? 109.335 152.649 157.534 1.00 25.96 ?  368 HIS B O     1 
ATOM   8539  C  CB    . HIS B 1 368 ? 110.732 150.382 156.014 1.00 13.01 ?  368 HIS B CB    1 
ATOM   8540  C  CG    . HIS B 1 368 ? 111.805 151.096 155.256 1.00 10.56 ?  368 HIS B CG    1 
ATOM   8541  N  ND1   . HIS B 1 368 ? 111.635 151.527 153.959 1.00 14.86 ?  368 HIS B ND1   1 
ATOM   8542  C  CD2   . HIS B 1 368 ? 113.063 151.450 155.609 1.00 7.35  ?  368 HIS B CD2   1 
ATOM   8543  C  CE1   . HIS B 1 368 ? 112.742 152.117 153.545 1.00 14.41 ?  368 HIS B CE1   1 
ATOM   8544  N  NE2   . HIS B 1 368 ? 113.624 152.083 154.528 1.00 10.81 ?  368 HIS B NE2   1 
ATOM   8545  N  N     . ALA B 1 369 ? 111.475 152.882 158.210 1.00 20.22 ?  369 ALA B N     1 
ATOM   8546  C  CA    . ALA B 1 369 ? 111.319 154.279 158.585 1.00 10.07 ?  369 ALA B CA    1 
ATOM   8547  C  C     . ALA B 1 369 ? 111.437 155.239 157.411 1.00 17.57 ?  369 ALA B C     1 
ATOM   8548  O  O     . ALA B 1 369 ? 111.103 156.417 157.566 1.00 26.04 ?  369 ALA B O     1 
ATOM   8549  C  CB    . ALA B 1 369 ? 112.352 154.648 159.651 1.00 10.84 ?  369 ALA B CB    1 
ATOM   8550  N  N     . ASN B 1 370 ? 111.893 154.775 156.252 1.00 16.15 ?  370 ASN B N     1 
ATOM   8551  C  CA    . ASN B 1 370 ? 112.151 155.638 155.106 1.00 14.72 ?  370 ASN B CA    1 
ATOM   8552  C  C     . ASN B 1 370 ? 111.383 155.171 153.876 1.00 12.00 ?  370 ASN B C     1 
ATOM   8553  O  O     . ASN B 1 370 ? 111.907 155.161 152.761 1.00 18.38 ?  370 ASN B O     1 
ATOM   8554  C  CB    . ASN B 1 370 ? 113.646 155.713 154.813 1.00 11.27 ?  370 ASN B CB    1 
ATOM   8555  C  CG    . ASN B 1 370 ? 114.440 156.256 155.982 1.00 11.90 ?  370 ASN B CG    1 
ATOM   8556  O  OD1   . ASN B 1 370 ? 114.214 157.378 156.432 1.00 26.54 ?  370 ASN B OD1   1 
ATOM   8557  N  ND2   . ASN B 1 370 ? 115.373 155.459 156.485 1.00 16.28 ?  370 ASN B ND2   1 
ATOM   8558  N  N     . ASN B 1 371 ? 110.124 154.772 154.069 1.00 20.31 ?  371 ASN B N     1 
ATOM   8559  C  CA    . ASN B 1 371 ? 109.287 154.379 152.943 1.00 10.79 ?  371 ASN B CA    1 
ATOM   8560  C  C     . ASN B 1 371 ? 109.000 155.539 152.002 1.00 16.41 ?  371 ASN B C     1 
ATOM   8561  O  O     . ASN B 1 371 ? 108.722 155.310 150.822 1.00 19.64 ?  371 ASN B O     1 
ATOM   8562  C  CB    . ASN B 1 371 ? 107.971 153.784 153.446 1.00 6.58  ?  371 ASN B CB    1 
ATOM   8563  C  CG    . ASN B 1 371 ? 108.081 152.308 153.758 1.00 16.28 ?  371 ASN B CG    1 
ATOM   8564  O  OD1   . ASN B 1 371 ? 108.945 151.613 153.225 1.00 20.36 ?  371 ASN B OD1   1 
ATOM   8565  N  ND2   . ASN B 1 371 ? 107.203 151.820 154.624 1.00 19.92 ?  371 ASN B ND2   1 
ATOM   8566  N  N     . HIS B 1 372 ? 109.054 156.776 152.502 1.00 21.65 ?  372 HIS B N     1 
ATOM   8567  C  CA    . HIS B 1 372 ? 108.837 157.938 151.646 1.00 17.77 ?  372 HIS B CA    1 
ATOM   8568  C  C     . HIS B 1 372 ? 109.912 158.040 150.571 1.00 20.25 ?  372 HIS B C     1 
ATOM   8569  O  O     . HIS B 1 372 ? 109.612 158.343 149.410 1.00 26.17 ?  372 HIS B O     1 
ATOM   8570  C  CB    . HIS B 1 372 ? 108.800 159.208 152.494 1.00 19.55 ?  372 HIS B CB    1 
ATOM   8571  C  CG    . HIS B 1 372 ? 110.102 159.523 153.161 1.00 19.08 ?  372 HIS B CG    1 
ATOM   8572  N  ND1   . HIS B 1 372 ? 110.694 158.678 154.074 1.00 22.10 ?  372 HIS B ND1   1 
ATOM   8573  C  CD2   . HIS B 1 372 ? 110.932 160.586 153.039 1.00 20.71 ?  372 HIS B CD2   1 
ATOM   8574  C  CE1   . HIS B 1 372 ? 111.831 159.207 154.487 1.00 17.13 ?  372 HIS B CE1   1 
ATOM   8575  N  NE2   . HIS B 1 372 ? 111.996 160.367 153.877 1.00 24.73 ?  372 HIS B NE2   1 
ATOM   8576  N  N     . ILE B 1 373 ? 111.173 157.802 150.941 1.00 16.01 ?  373 ILE B N     1 
ATOM   8577  C  CA    . ILE B 1 373 ? 112.249 157.800 149.955 1.00 18.41 ?  373 ILE B CA    1 
ATOM   8578  C  C     . ILE B 1 373 ? 112.037 156.671 148.958 1.00 18.51 ?  373 ILE B C     1 
ATOM   8579  O  O     . ILE B 1 373 ? 112.040 156.882 147.738 1.00 28.73 ?  373 ILE B O     1 
ATOM   8580  C  CB    . ILE B 1 373 ? 113.614 157.677 150.655 1.00 20.64 ?  373 ILE B CB    1 
ATOM   8581  C  CG1   . ILE B 1 373 ? 113.842 158.863 151.589 1.00 18.92 ?  373 ILE B CG1   1 
ATOM   8582  C  CG2   . ILE B 1 373 ? 114.734 157.572 149.631 1.00 19.25 ?  373 ILE B CG2   1 
ATOM   8583  C  CD1   . ILE B 1 373 ? 114.998 158.682 152.536 1.00 14.77 ?  373 ILE B CD1   1 
ATOM   8584  N  N     . SER B 1 374 ? 111.827 155.460 149.470 1.00 17.14 ?  374 SER B N     1 
ATOM   8585  C  CA    . SER B 1 374 ? 111.594 154.273 148.661 1.00 6.86  ?  374 SER B CA    1 
ATOM   8586  C  C     . SER B 1 374 ? 111.288 153.098 149.576 1.00 13.56 ?  374 SER B C     1 
ATOM   8587  O  O     . SER B 1 374 ? 111.709 153.087 150.737 1.00 16.95 ?  374 SER B O     1 
ATOM   8588  C  CB    . SER B 1 374 ? 112.807 153.960 147.784 1.00 18.97 ?  374 SER B CB    1 
ATOM   8589  O  OG    . SER B 1 374 ? 112.449 153.130 146.697 1.00 32.64 ?  374 SER B OG    1 
ATOM   8590  N  N     . LYS B 1 375 ? 110.554 152.113 149.077 1.00 24.02 ?  375 LYS B N     1 
ATOM   8591  C  CA    . LYS B 1 375 ? 110.399 150.868 149.805 1.00 14.13 ?  375 LYS B CA    1 
ATOM   8592  C  C     . LYS B 1 375 ? 111.636 150.002 149.611 1.00 15.05 ?  375 LYS B C     1 
ATOM   8593  O  O     . LYS B 1 375 ? 112.331 150.096 148.597 1.00 23.95 ?  375 LYS B O     1 
ATOM   8594  C  CB    . LYS B 1 375 ? 109.154 150.114 149.339 1.00 11.94 ?  375 LYS B CB    1 
ATOM   8595  C  CG    . LYS B 1 375 ? 107.859 150.877 149.529 1.00 17.96 ?  375 LYS B CG    1 
ATOM   8596  C  CD    . LYS B 1 375 ? 107.022 150.269 150.638 1.00 17.81 ?  375 LYS B CD    1 
ATOM   8597  C  CE    . LYS B 1 375 ? 105.699 150.997 150.788 1.00 16.98 ?  375 LYS B CE    1 
ATOM   8598  N  NZ    . LYS B 1 375 ? 105.843 152.459 150.552 1.00 23.96 1  375 LYS B NZ    1 
ATOM   8599  N  N     . VAL B 1 376 ? 111.916 149.160 150.599 1.00 9.75  ?  376 VAL B N     1 
ATOM   8600  C  CA    . VAL B 1 376 ? 113.030 148.227 150.493 1.00 13.73 ?  376 VAL B CA    1 
ATOM   8601  C  C     . VAL B 1 376 ? 112.610 147.089 149.573 1.00 16.12 ?  376 VAL B C     1 
ATOM   8602  O  O     . VAL B 1 376 ? 111.682 146.335 149.886 1.00 23.12 ?  376 VAL B O     1 
ATOM   8603  C  CB    . VAL B 1 376 ? 113.452 147.703 151.871 1.00 11.90 ?  376 VAL B CB    1 
ATOM   8604  C  CG1   . VAL B 1 376 ? 114.651 146.783 151.736 1.00 10.55 ?  376 VAL B CG1   1 
ATOM   8605  C  CG2   . VAL B 1 376 ? 113.767 148.858 152.803 1.00 6.92  ?  376 VAL B CG2   1 
ATOM   8606  N  N     . LYS B 1 377 ? 113.286 146.966 148.432 1.00 14.55 ?  377 LYS B N     1 
ATOM   8607  C  CA    . LYS B 1 377 ? 112.912 145.980 147.430 1.00 9.58  ?  377 LYS B CA    1 
ATOM   8608  C  C     . LYS B 1 377 ? 113.838 144.777 147.384 1.00 9.63  ?  377 LYS B C     1 
ATOM   8609  O  O     . LYS B 1 377 ? 113.486 143.775 146.758 1.00 24.47 ?  377 LYS B O     1 
ATOM   8610  C  CB    . LYS B 1 377 ? 112.870 146.618 146.037 1.00 13.22 ?  377 LYS B CB    1 
ATOM   8611  C  CG    . LYS B 1 377 ? 112.126 147.930 145.976 1.00 9.80  ?  377 LYS B CG    1 
ATOM   8612  C  CD    . LYS B 1 377 ? 112.785 148.857 144.980 1.00 18.20 ?  377 LYS B CD    1 
ATOM   8613  C  CE    . LYS B 1 377 ? 112.619 150.302 145.384 1.00 20.76 ?  377 LYS B CE    1 
ATOM   8614  N  NZ    . LYS B 1 377 ? 113.532 151.188 144.613 1.00 19.82 1  377 LYS B NZ    1 
ATOM   8615  N  N     . PHE B 1 378 ? 115.007 144.850 148.012 1.00 11.14 ?  378 PHE B N     1 
ATOM   8616  C  CA    . PHE B 1 378 ? 115.949 143.740 148.013 1.00 8.11  ?  378 PHE B CA    1 
ATOM   8617  C  C     . PHE B 1 378 ? 116.930 143.941 149.161 1.00 7.41  ?  378 PHE B C     1 
ATOM   8618  O  O     . PHE B 1 378 ? 116.925 144.975 149.835 1.00 16.36 ?  378 PHE B O     1 
ATOM   8619  C  CB    . PHE B 1 378 ? 116.656 143.609 146.660 1.00 4.29  ?  378 PHE B CB    1 
ATOM   8620  C  CG    . PHE B 1 378 ? 117.672 144.681 146.385 1.00 4.17  ?  378 PHE B CG    1 
ATOM   8621  C  CD1   . PHE B 1 378 ? 117.300 146.011 146.317 1.00 10.59 ?  378 PHE B CD1   1 
ATOM   8622  C  CD2   . PHE B 1 378 ? 118.998 144.351 146.172 1.00 3.19  ?  378 PHE B CD2   1 
ATOM   8623  C  CE1   . PHE B 1 378 ? 118.230 146.992 146.058 1.00 7.65  ?  378 PHE B CE1   1 
ATOM   8624  C  CE2   . PHE B 1 378 ? 119.931 145.329 145.910 1.00 10.18 ?  378 PHE B CE2   1 
ATOM   8625  C  CZ    . PHE B 1 378 ? 119.546 146.652 145.852 1.00 11.71 ?  378 PHE B CZ    1 
ATOM   8626  N  N     . SER B 1 379 ? 117.770 142.938 149.383 1.00 2.13  ?  379 SER B N     1 
ATOM   8627  C  CA    . SER B 1 379 ? 118.747 142.942 150.462 1.00 0.54  ?  379 SER B CA    1 
ATOM   8628  C  C     . SER B 1 379 ? 120.149 142.783 149.878 1.00 4.59  ?  379 SER B C     1 
ATOM   8629  O  O     . SER B 1 379 ? 120.343 142.782 148.660 1.00 7.64  ?  379 SER B O     1 
ATOM   8630  C  CB    . SER B 1 379 ? 118.429 141.844 151.478 1.00 10.27 ?  379 SER B CB    1 
ATOM   8631  O  OG    . SER B 1 379 ? 118.860 142.218 152.774 1.00 10.56 ?  379 SER B OG    1 
ATOM   8632  N  N     . ASN B 1 380 ? 121.133 142.659 150.761 1.00 11.08 ?  380 ASN B N     1 
ATOM   8633  C  CA    . ASN B 1 380 ? 122.528 142.573 150.371 1.00 7.33  ?  380 ASN B CA    1 
ATOM   8634  C  C     . ASN B 1 380 ? 122.946 141.110 150.238 1.00 13.50 ?  380 ASN B C     1 
ATOM   8635  O  O     . ASN B 1 380 ? 122.121 140.194 150.284 1.00 16.85 ?  380 ASN B O     1 
ATOM   8636  C  CB    . ASN B 1 380 ? 123.402 143.329 151.372 1.00 8.68  ?  380 ASN B CB    1 
ATOM   8637  C  CG    . ASN B 1 380 ? 123.440 142.667 152.731 1.00 6.85  ?  380 ASN B CG    1 
ATOM   8638  O  OD1   . ASN B 1 380 ? 122.407 142.279 153.274 1.00 19.12 ?  380 ASN B OD1   1 
ATOM   8639  N  ND2   . ASN B 1 380 ? 124.635 142.536 153.289 1.00 13.32 ?  380 ASN B ND2   1 
ATOM   8640  N  N     . LEU B 1 381 ? 124.249 140.886 150.058 1.00 18.23 ?  381 LEU B N     1 
ATOM   8641  C  CA    . LEU B 1 381 ? 124.771 139.536 149.897 1.00 11.49 ?  381 LEU B CA    1 
ATOM   8642  C  C     . LEU B 1 381 ? 124.613 138.700 151.161 1.00 7.62  ?  381 LEU B C     1 
ATOM   8643  O  O     . LEU B 1 381 ? 124.532 137.470 151.071 1.00 18.28 ?  381 LEU B O     1 
ATOM   8644  C  CB    . LEU B 1 381 ? 126.243 139.604 149.479 1.00 17.87 ?  381 LEU B CB    1 
ATOM   8645  C  CG    . LEU B 1 381 ? 127.054 138.313 149.349 1.00 19.37 ?  381 LEU B CG    1 
ATOM   8646  C  CD1   . LEU B 1 381 ? 126.577 137.483 148.171 1.00 15.88 ?  381 LEU B CD1   1 
ATOM   8647  C  CD2   . LEU B 1 381 ? 128.530 138.635 149.218 1.00 17.74 ?  381 LEU B CD2   1 
ATOM   8648  N  N     . CYS B 1 382 ? 124.552 139.332 152.330 1.00 11.63 ?  382 CYS B N     1 
ATOM   8649  C  CA    . CYS B 1 382 ? 124.324 138.631 153.584 1.00 5.10  ?  382 CYS B CA    1 
ATOM   8650  C  C     . CYS B 1 382 ? 122.892 138.772 154.081 1.00 8.11  ?  382 CYS B C     1 
ATOM   8651  O  O     . CYS B 1 382 ? 122.581 138.289 155.175 1.00 17.87 ?  382 CYS B O     1 
ATOM   8652  C  CB    . CYS B 1 382 ? 125.301 139.126 154.652 1.00 16.37 ?  382 CYS B CB    1 
ATOM   8653  S  SG    . CYS B 1 382 ? 127.031 139.146 154.128 1.00 31.70 ?  382 CYS B SG    1 
ATOM   8654  N  N     . SER B 1 383 ? 122.020 139.418 153.306 1.00 10.35 ?  383 SER B N     1 
ATOM   8655  C  CA    . SER B 1 383 ? 120.588 139.520 153.600 1.00 9.66  ?  383 SER B CA    1 
ATOM   8656  C  C     . SER B 1 383 ? 120.327 140.121 154.979 1.00 12.91 ?  383 SER B C     1 
ATOM   8657  O  O     . SER B 1 383 ? 119.484 139.644 155.740 1.00 23.55 ?  383 SER B O     1 
ATOM   8658  C  CB    . SER B 1 383 ? 119.897 138.162 153.464 1.00 13.23 ?  383 SER B CB    1 
ATOM   8659  O  OG    . SER B 1 383 ? 120.426 137.221 154.376 1.00 18.79 ?  383 SER B OG    1 
ATOM   8660  N  N     . GLU B 1 384 ? 121.064 141.181 155.312 1.00 7.46  ?  384 GLU B N     1 
ATOM   8661  C  CA    . GLU B 1 384 ? 120.799 141.936 156.527 1.00 8.37  ?  384 GLU B CA    1 
ATOM   8662  C  C     . GLU B 1 384 ? 120.676 143.433 156.294 1.00 13.49 ?  384 GLU B C     1 
ATOM   8663  O  O     . GLU B 1 384 ? 120.195 144.140 157.188 1.00 23.85 ?  384 GLU B O     1 
ATOM   8664  C  CB    . GLU B 1 384 ? 121.886 141.669 157.583 1.00 6.60  ?  384 GLU B CB    1 
ATOM   8665  C  CG    . GLU B 1 384 ? 122.925 142.765 157.761 1.00 10.32 ?  384 GLU B CG    1 
ATOM   8666  C  CD    . GLU B 1 384 ? 124.016 142.715 156.717 1.00 19.47 ?  384 GLU B CD    1 
ATOM   8667  O  OE1   . GLU B 1 384 ? 124.123 141.687 156.021 1.00 13.01 ?  384 GLU B OE1   1 
ATOM   8668  O  OE2   . GLU B 1 384 ? 124.777 143.697 156.605 1.00 26.60 -1 384 GLU B OE2   1 
ATOM   8669  N  N     . VAL B 1 385 ? 121.070 143.937 155.132 1.00 10.47 ?  385 VAL B N     1 
ATOM   8670  C  CA    . VAL B 1 385 ? 120.924 145.348 154.803 1.00 6.73  ?  385 VAL B CA    1 
ATOM   8671  C  C     . VAL B 1 385 ? 119.580 145.543 154.116 1.00 15.55 ?  385 VAL B C     1 
ATOM   8672  O  O     . VAL B 1 385 ? 119.318 144.944 153.068 1.00 24.31 ?  385 VAL B O     1 
ATOM   8673  C  CB    . VAL B 1 385 ? 122.073 145.833 153.911 1.00 6.60  ?  385 VAL B CB    1 
ATOM   8674  C  CG1   . VAL B 1 385 ? 121.809 147.243 153.447 1.00 6.70  ?  385 VAL B CG1   1 
ATOM   8675  C  CG2   . VAL B 1 385 ? 123.380 145.761 154.661 1.00 11.92 ?  385 VAL B CG2   1 
ATOM   8676  N  N     . LEU B 1 386 ? 118.727 146.377 154.708 1.00 12.50 ?  386 LEU B N     1 
ATOM   8677  C  CA    . LEU B 1 386 ? 117.376 146.626 154.207 1.00 2.08  ?  386 LEU B CA    1 
ATOM   8678  C  C     . LEU B 1 386 ? 117.139 148.132 154.231 1.00 5.19  ?  386 LEU B C     1 
ATOM   8679  O  O     . LEU B 1 386 ? 116.710 148.688 155.245 1.00 11.17 ?  386 LEU B O     1 
ATOM   8680  C  CB    . LEU B 1 386 ? 116.346 145.872 155.032 1.00 5.06  ?  386 LEU B CB    1 
ATOM   8681  C  CG    . LEU B 1 386 ? 116.463 144.353 154.923 1.00 5.85  ?  386 LEU B CG    1 
ATOM   8682  C  CD1   . LEU B 1 386 ? 115.654 143.689 156.004 1.00 10.23 ?  386 LEU B CD1   1 
ATOM   8683  C  CD2   . LEU B 1 386 ? 116.019 143.877 153.550 1.00 8.67  ?  386 LEU B CD2   1 
ATOM   8684  N  N     . GLN B 1 387 ? 117.418 148.786 153.107 1.00 11.72 ?  387 GLN B N     1 
ATOM   8685  C  CA    . GLN B 1 387 ? 117.373 150.236 153.023 1.00 9.78  ?  387 GLN B CA    1 
ATOM   8686  C  C     . GLN B 1 387 ? 116.644 150.659 151.756 1.00 11.25 ?  387 GLN B C     1 
ATOM   8687  O  O     . GLN B 1 387 ? 116.503 149.887 150.805 1.00 19.86 ?  387 GLN B O     1 
ATOM   8688  C  CB    . GLN B 1 387 ? 118.781 150.842 153.044 1.00 4.43  ?  387 GLN B CB    1 
ATOM   8689  C  CG    . GLN B 1 387 ? 119.621 150.405 154.226 1.00 6.44  ?  387 GLN B CG    1 
ATOM   8690  C  CD    . GLN B 1 387 ? 120.973 151.069 154.244 1.00 10.27 ?  387 GLN B CD    1 
ATOM   8691  O  OE1   . GLN B 1 387 ? 121.196 152.058 153.549 1.00 21.83 ?  387 GLN B OE1   1 
ATOM   8692  N  NE2   . GLN B 1 387 ? 121.888 150.532 155.038 1.00 10.90 ?  387 GLN B NE2   1 
ATOM   8693  N  N     . ALA B 1 388 ? 116.166 151.899 151.765 1.00 13.59 ?  388 ALA B N     1 
ATOM   8694  C  CA    . ALA B 1 388 ? 115.529 152.469 150.589 1.00 10.79 ?  388 ALA B CA    1 
ATOM   8695  C  C     . ALA B 1 388 ? 116.548 152.672 149.477 1.00 17.73 ?  388 ALA B C     1 
ATOM   8696  O  O     . ALA B 1 388 ? 117.671 153.123 149.714 1.00 23.67 ?  388 ALA B O     1 
ATOM   8697  C  CB    . ALA B 1 388 ? 114.863 153.799 150.937 1.00 9.43  ?  388 ALA B CB    1 
ATOM   8698  N  N     . SER B 1 389 ? 116.152 152.332 148.254 1.00 21.15 ?  389 SER B N     1 
ATOM   8699  C  CA    . SER B 1 389 ? 116.999 152.519 147.088 1.00 8.55  ?  389 SER B CA    1 
ATOM   8700  C  C     . SER B 1 389 ? 116.166 153.066 145.942 1.00 16.13 ?  389 SER B C     1 
ATOM   8701  O  O     . SER B 1 389 ? 115.027 152.640 145.733 1.00 23.96 ?  389 SER B O     1 
ATOM   8702  C  CB    . SER B 1 389 ? 117.675 151.211 146.662 1.00 14.47 ?  389 SER B CB    1 
ATOM   8703  O  OG    . SER B 1 389 ? 116.727 150.169 146.514 1.00 24.83 ?  389 SER B OG    1 
ATOM   8704  N  N     . GLN B 1 390 ? 116.739 154.011 145.206 1.00 17.90 ?  390 GLN B N     1 
ATOM   8705  C  CA    . GLN B 1 390 ? 116.128 154.562 144.007 1.00 11.04 ?  390 GLN B CA    1 
ATOM   8706  C  C     . GLN B 1 390 ? 116.965 154.154 142.806 1.00 12.59 ?  390 GLN B C     1 
ATOM   8707  O  O     . GLN B 1 390 ? 118.188 154.329 142.808 1.00 26.82 ?  390 GLN B O     1 
ATOM   8708  C  CB    . GLN B 1 390 ? 116.016 156.085 144.098 1.00 16.03 ?  390 GLN B CB    1 
ATOM   8709  C  CG    . GLN B 1 390 ? 115.021 156.563 145.145 1.00 18.30 ?  390 GLN B CG    1 
ATOM   8710  C  CD    . GLN B 1 390 ? 115.076 158.060 145.369 1.00 22.91 ?  390 GLN B CD    1 
ATOM   8711  O  OE1   . GLN B 1 390 ? 115.953 158.746 144.846 1.00 25.83 ?  390 GLN B OE1   1 
ATOM   8712  N  NE2   . GLN B 1 390 ? 114.134 158.576 146.151 1.00 18.30 ?  390 GLN B NE2   1 
ATOM   8713  N  N     . VAL B 1 391 ? 116.309 153.596 141.788 1.00 22.98 ?  391 VAL B N     1 
ATOM   8714  C  CA    . VAL B 1 391 ? 117.029 153.113 140.618 1.00 20.87 ?  391 VAL B CA    1 
ATOM   8715  C  C     . VAL B 1 391 ? 117.609 154.292 139.846 1.00 23.00 ?  391 VAL B C     1 
ATOM   8716  O  O     . VAL B 1 391 ? 117.062 155.403 139.847 1.00 21.34 ?  391 VAL B O     1 
ATOM   8717  C  CB    . VAL B 1 391 ? 116.112 152.249 139.732 1.00 15.39 ?  391 VAL B CB    1 
ATOM   8718  C  CG1   . VAL B 1 391 ? 115.178 153.115 138.902 1.00 20.83 ?  391 VAL B CG1   1 
ATOM   8719  C  CG2   . VAL B 1 391 ? 116.937 151.332 138.842 1.00 17.46 ?  391 VAL B CG2   1 
ATOM   8720  N  N     . SER B 1 392 ? 118.743 154.054 139.196 1.00 28.78 ?  392 SER B N     1 
ATOM   8721  C  CA    . SER B 1 392 ? 119.413 155.067 138.397 1.00 21.82 ?  392 SER B CA    1 
ATOM   8722  C  C     . SER B 1 392 ? 119.070 154.884 136.924 1.00 28.18 ?  392 SER B C     1 
ATOM   8723  O  O     . SER B 1 392 ? 118.874 153.764 136.447 1.00 31.29 ?  392 SER B O     1 
ATOM   8724  C  CB    . SER B 1 392 ? 120.930 155.002 138.587 1.00 20.84 ?  392 SER B CB    1 
ATOM   8725  O  OG    . SER B 1 392 ? 121.284 155.188 139.945 1.00 30.03 ?  392 SER B OG    1 
ATOM   8726  N  N     . SER B 1 393 ? 118.996 156.001 136.211 1.00 25.65 ?  393 SER B N     1 
ATOM   8727  C  CA    . SER B 1 393 ? 118.739 156.006 134.774 1.00 23.85 ?  393 SER B CA    1 
ATOM   8728  C  C     . SER B 1 393 ? 120.062 156.313 134.078 1.00 25.99 ?  393 SER B C     1 
ATOM   8729  O  O     . SER B 1 393 ? 120.393 157.471 133.821 1.00 31.14 ?  393 SER B O     1 
ATOM   8730  C  CB    . SER B 1 393 ? 117.661 157.021 134.407 1.00 28.94 ?  393 SER B CB    1 
ATOM   8731  O  OG    . SER B 1 393 ? 116.522 156.877 135.238 1.00 31.30 ?  393 SER B OG    1 
ATOM   8732  N  N     . TYR B 1 394 ? 120.822 155.262 133.784 1.00 28.75 ?  394 TYR B N     1 
ATOM   8733  C  CA    . TYR B 1 394 ? 122.067 155.402 133.037 1.00 26.75 ?  394 TYR B CA    1 
ATOM   8734  C  C     . TYR B 1 394 ? 121.723 155.489 131.557 1.00 26.39 ?  394 TYR B C     1 
ATOM   8735  O  O     . TYR B 1 394 ? 121.277 154.506 130.955 1.00 29.18 ?  394 TYR B O     1 
ATOM   8736  C  CB    . TYR B 1 394 ? 123.001 154.233 133.326 1.00 24.95 ?  394 TYR B CB    1 
ATOM   8737  C  CG    . TYR B 1 394 ? 123.426 154.141 134.775 1.00 23.85 ?  394 TYR B CG    1 
ATOM   8738  C  CD1   . TYR B 1 394 ? 124.238 155.111 135.343 1.00 23.65 ?  394 TYR B CD1   1 
ATOM   8739  C  CD2   . TYR B 1 394 ? 123.009 153.085 135.574 1.00 25.91 ?  394 TYR B CD2   1 
ATOM   8740  C  CE1   . TYR B 1 394 ? 124.628 155.031 136.666 1.00 28.58 ?  394 TYR B CE1   1 
ATOM   8741  C  CE2   . TYR B 1 394 ? 123.392 152.996 136.897 1.00 26.75 ?  394 TYR B CE2   1 
ATOM   8742  C  CZ    . TYR B 1 394 ? 124.201 153.972 137.437 1.00 30.68 ?  394 TYR B CZ    1 
ATOM   8743  O  OH    . TYR B 1 394 ? 124.586 153.888 138.756 1.00 34.71 ?  394 TYR B OH    1 
ATOM   8744  N  N     . THR B 1 395 ? 121.917 156.663 130.972 1.00 31.26 ?  395 THR B N     1 
ATOM   8745  C  CA    . THR B 1 395 ? 121.501 156.939 129.610 1.00 30.91 ?  395 THR B CA    1 
ATOM   8746  C  C     . THR B 1 395 ? 122.643 156.645 128.640 1.00 32.44 ?  395 THR B C     1 
ATOM   8747  O  O     . THR B 1 395 ? 123.680 156.085 129.011 1.00 32.19 ?  395 THR B O     1 
ATOM   8748  C  CB    . THR B 1 395 ? 121.018 158.385 129.502 1.00 30.55 ?  395 THR B CB    1 
ATOM   8749  O  OG1   . THR B 1 395 ? 122.060 159.271 129.927 1.00 32.79 ?  395 THR B OG1   1 
ATOM   8750  C  CG2   . THR B 1 395 ? 119.794 158.600 130.376 1.00 30.29 ?  395 THR B CG2   1 
ATOM   8751  N  N     . ASP B 1 396 ? 122.453 157.023 127.380 1.00 33.29 ?  396 ASP B N     1 
ATOM   8752  C  CA    . ASP B 1 396 ? 123.472 156.812 126.366 1.00 31.68 ?  396 ASP B CA    1 
ATOM   8753  C  C     . ASP B 1 396 ? 124.685 157.695 126.634 1.00 34.49 ?  396 ASP B C     1 
ATOM   8754  O  O     . ASP B 1 396 ? 124.646 158.630 127.438 1.00 40.59 ?  396 ASP B O     1 
ATOM   8755  C  CB    . ASP B 1 396 ? 122.916 157.107 124.973 1.00 33.18 ?  396 ASP B CB    1 
ATOM   8756  C  CG    . ASP B 1 396 ? 121.809 156.156 124.570 1.00 36.09 ?  396 ASP B CG    1 
ATOM   8757  O  OD1   . ASP B 1 396 ? 121.744 155.042 125.129 1.00 39.61 ?  396 ASP B OD1   1 
ATOM   8758  O  OD2   . ASP B 1 396 ? 121.004 156.522 123.689 1.00 36.46 -1 396 ASP B OD2   1 
ATOM   8759  N  N     . TYR B 1 397 ? 125.781 157.379 125.950 1.00 32.92 ?  397 TYR B N     1 
ATOM   8760  C  CA    . TYR B 1 397 ? 126.964 158.222 126.018 1.00 32.88 ?  397 TYR B CA    1 
ATOM   8761  C  C     . TYR B 1 397 ? 126.648 159.606 125.464 1.00 38.23 ?  397 TYR B C     1 
ATOM   8762  O  O     . TYR B 1 397 ? 125.820 159.762 124.561 1.00 43.77 ?  397 TYR B O     1 
ATOM   8763  C  CB    . TYR B 1 397 ? 128.121 157.589 125.245 1.00 31.40 ?  397 TYR B CB    1 
ATOM   8764  C  CG    . TYR B 1 397 ? 129.484 158.044 125.707 1.00 31.29 ?  397 TYR B CG    1 
ATOM   8765  C  CD1   . TYR B 1 397 ? 130.050 159.213 125.217 1.00 34.49 ?  397 TYR B CD1   1 
ATOM   8766  C  CD2   . TYR B 1 397 ? 130.205 157.307 126.636 1.00 32.36 ?  397 TYR B CD2   1 
ATOM   8767  C  CE1   . TYR B 1 397 ? 131.295 159.633 125.637 1.00 33.49 ?  397 TYR B CE1   1 
ATOM   8768  C  CE2   . TYR B 1 397 ? 131.452 157.719 127.061 1.00 29.46 ?  397 TYR B CE2   1 
ATOM   8769  C  CZ    . TYR B 1 397 ? 131.992 158.883 126.559 1.00 31.74 ?  397 TYR B CZ    1 
ATOM   8770  O  OH    . TYR B 1 397 ? 133.233 159.299 126.979 1.00 35.13 ?  397 TYR B OH    1 
ATOM   8771  N  N     . ASP B 1 398 ? 127.302 160.618 126.035 1.00 35.77 ?  398 ASP B N     1 
ATOM   8772  C  CA    . ASP B 1 398 ? 127.076 162.035 125.759 1.00 40.56 ?  398 ASP B CA    1 
ATOM   8773  C  C     . ASP B 1 398 ? 125.720 162.515 126.255 1.00 41.34 ?  398 ASP B C     1 
ATOM   8774  O  O     . ASP B 1 398 ? 125.296 163.625 125.908 1.00 39.21 ?  398 ASP B O     1 
ATOM   8775  C  CB    . ASP B 1 398 ? 127.224 162.369 124.269 1.00 39.07 ?  398 ASP B CB    1 
ATOM   8776  C  CG    . ASP B 1 398 ? 128.531 163.069 123.955 1.00 44.22 ?  398 ASP B CG    1 
ATOM   8777  O  OD1   . ASP B 1 398 ? 128.637 163.672 122.866 1.00 42.46 ?  398 ASP B OD1   1 
ATOM   8778  O  OD2   . ASP B 1 398 ? 129.453 163.015 124.796 1.00 45.23 -1 398 ASP B OD2   1 
ATOM   8779  N  N     . GLU B 1 399 ? 125.024 161.713 127.056 1.00 44.70 ?  399 GLU B N     1 
ATOM   8780  C  CA    . GLU B 1 399 ? 123.768 162.099 127.679 1.00 41.11 ?  399 GLU B CA    1 
ATOM   8781  C  C     . GLU B 1 399 ? 123.922 162.023 129.190 1.00 44.21 ?  399 GLU B C     1 
ATOM   8782  O  O     . GLU B 1 399 ? 124.579 161.117 129.713 1.00 39.66 ?  399 GLU B O     1 
ATOM   8783  C  CB    . GLU B 1 399 ? 122.616 161.197 127.222 1.00 37.86 ?  399 GLU B CB    1 
ATOM   8784  C  CG    . GLU B 1 399 ? 122.307 161.287 125.738 1.00 43.97 ?  399 GLU B CG    1 
ATOM   8785  C  CD    . GLU B 1 399 ? 121.678 162.612 125.353 1.00 47.43 ?  399 GLU B CD    1 
ATOM   8786  O  OE1   . GLU B 1 399 ? 120.808 163.100 126.104 1.00 47.85 ?  399 GLU B OE1   1 
ATOM   8787  O  OE2   . GLU B 1 399 ? 122.054 163.166 124.298 1.00 46.53 -1 399 GLU B OE2   1 
ATOM   8788  N  N     . GLU B 1 400 ? 123.320 162.982 129.891 1.00 45.70 ?  400 GLU B N     1 
ATOM   8789  C  CA    . GLU B 1 400 ? 123.410 163.010 131.343 1.00 39.54 ?  400 GLU B CA    1 
ATOM   8790  C  C     . GLU B 1 400 ? 122.629 161.849 131.944 1.00 40.22 ?  400 GLU B C     1 
ATOM   8791  O  O     . GLU B 1 400 ? 121.503 161.559 131.526 1.00 39.36 ?  400 GLU B O     1 
ATOM   8792  C  CB    . GLU B 1 400 ? 122.884 164.338 131.883 1.00 40.02 ?  400 GLU B CB    1 
ATOM   8793  C  CG    . GLU B 1 400 ? 123.906 165.461 131.862 1.00 44.35 ?  400 GLU B CG    1 
ATOM   8794  C  CD    . GLU B 1 400 ? 125.215 165.069 132.516 1.00 47.31 ?  400 GLU B CD    1 
ATOM   8795  O  OE1   . GLU B 1 400 ? 125.205 164.740 133.720 1.00 46.59 ?  400 GLU B OE1   1 
ATOM   8796  O  OE2   . GLU B 1 400 ? 126.255 165.088 131.826 1.00 45.60 -1 400 GLU B OE2   1 
ATOM   8797  N  N     . ASP B 1 401 ? 123.229 161.184 132.927 1.00 35.64 ?  401 ASP B N     1 
ATOM   8798  C  CA    . ASP B 1 401 ? 122.584 160.078 133.619 1.00 31.88 ?  401 ASP B CA    1 
ATOM   8799  C  C     . ASP B 1 401 ? 121.833 160.588 134.840 1.00 32.92 ?  401 ASP B C     1 
ATOM   8800  O  O     . ASP B 1 401 ? 122.298 161.492 135.539 1.00 38.51 ?  401 ASP B O     1 
ATOM   8801  C  CB    . ASP B 1 401 ? 123.614 159.031 134.044 1.00 31.73 ?  401 ASP B CB    1 
ATOM   8802  C  CG    . ASP B 1 401 ? 124.429 158.506 132.881 1.00 36.42 ?  401 ASP B CG    1 
ATOM   8803  O  OD1   . ASP B 1 401 ? 123.973 158.632 131.725 1.00 38.79 ?  401 ASP B OD1   1 
ATOM   8804  O  OD2   . ASP B 1 401 ? 125.527 157.966 133.122 1.00 38.06 -1 401 ASP B OD2   1 
ATOM   8805  N  N     . GLU B 1 402 ? 120.665 160.002 135.092 1.00 29.52 ?  402 GLU B N     1 
ATOM   8806  C  CA    . GLU B 1 402 ? 119.892 160.295 136.298 1.00 27.64 ?  402 GLU B CA    1 
ATOM   8807  C  C     . GLU B 1 402 ? 120.373 159.347 137.387 1.00 29.15 ?  402 GLU B C     1 
ATOM   8808  O  O     . GLU B 1 402 ? 120.039 158.161 137.388 1.00 30.97 ?  402 GLU B O     1 
ATOM   8809  C  CB    . GLU B 1 402 ? 118.399 160.149 136.037 1.00 29.73 ?  402 GLU B CB    1 
ATOM   8810  C  CG    . GLU B 1 402 ? 117.812 161.234 135.149 1.00 33.82 ?  402 GLU B CG    1 
ATOM   8811  C  CD    . GLU B 1 402 ? 118.315 162.619 135.508 1.00 39.10 ?  402 GLU B CD    1 
ATOM   8812  O  OE1   . GLU B 1 402 ? 117.928 163.136 136.576 1.00 35.36 ?  402 GLU B OE1   1 
ATOM   8813  O  OE2   . GLU B 1 402 ? 119.100 163.190 134.722 1.00 36.60 -1 402 GLU B OE2   1 
ATOM   8814  N  N     . ILE B 1 403 ? 121.160 159.872 138.318 1.00 29.66 ?  403 ILE B N     1 
ATOM   8815  C  CA    . ILE B 1 403 ? 121.794 159.065 139.354 1.00 24.05 ?  403 ILE B CA    1 
ATOM   8816  C  C     . ILE B 1 403 ? 120.811 158.880 140.503 1.00 25.63 ?  403 ILE B C     1 
ATOM   8817  O  O     . ILE B 1 403 ? 120.318 159.857 141.075 1.00 30.61 ?  403 ILE B O     1 
ATOM   8818  C  CB    . ILE B 1 403 ? 123.098 159.712 139.840 1.00 21.38 ?  403 ILE B CB    1 
ATOM   8819  C  CG1   . ILE B 1 403 ? 124.133 159.731 138.714 1.00 23.71 ?  403 ILE B CG1   1 
ATOM   8820  C  CG2   . ILE B 1 403 ? 123.639 158.976 141.050 1.00 20.95 ?  403 ILE B CG2   1 
ATOM   8821  C  CD1   . ILE B 1 403 ? 124.345 158.389 138.055 1.00 27.98 ?  403 ILE B CD1   1 
ATOM   8822  N  N     . GLY B 1 404 ? 120.530 157.629 140.839 1.00 22.24 ?  404 GLY B N     1 
ATOM   8823  C  CA    . GLY B 1 404 ? 119.647 157.290 141.935 1.00 10.85 ?  404 GLY B CA    1 
ATOM   8824  C  C     . GLY B 1 404 ? 120.398 157.034 143.222 1.00 19.17 ?  404 GLY B C     1 
ATOM   8825  O  O     . GLY B 1 404 ? 121.459 157.611 143.478 1.00 26.62 ?  404 GLY B O     1 
ATOM   8826  N  N     . LEU B 1 405 ? 119.841 156.152 144.045 1.00 23.93 ?  405 LEU B N     1 
ATOM   8827  C  CA    . LEU B 1 405 ? 120.424 155.795 145.331 1.00 10.66 ?  405 LEU B CA    1 
ATOM   8828  C  C     . LEU B 1 405 ? 120.693 154.298 145.353 1.00 13.07 ?  405 LEU B C     1 
ATOM   8829  O  O     . LEU B 1 405 ? 119.758 153.496 145.258 1.00 14.56 ?  405 LEU B O     1 
ATOM   8830  C  CB    . LEU B 1 405 ? 119.498 156.191 146.483 1.00 17.18 ?  405 LEU B CB    1 
ATOM   8831  C  CG    . LEU B 1 405 ? 119.151 157.676 146.604 1.00 17.59 ?  405 LEU B CG    1 
ATOM   8832  C  CD1   . LEU B 1 405 ? 117.963 157.869 147.527 1.00 20.83 ?  405 LEU B CD1   1 
ATOM   8833  C  CD2   . LEU B 1 405 ? 120.346 158.476 147.092 1.00 16.71 ?  405 LEU B CD2   1 
ATOM   8834  N  N     . ASP B 1 406 ? 121.962 153.925 145.480 1.00 24.08 ?  406 ASP B N     1 
ATOM   8835  C  CA    . ASP B 1 406 ? 122.367 152.532 145.613 1.00 17.26 ?  406 ASP B CA    1 
ATOM   8836  C  C     . ASP B 1 406 ? 122.881 152.300 147.025 1.00 18.11 ?  406 ASP B C     1 
ATOM   8837  O  O     . ASP B 1 406 ? 123.797 152.992 147.480 1.00 27.75 ?  406 ASP B O     1 
ATOM   8838  C  CB    . ASP B 1 406 ? 123.441 152.165 144.588 1.00 17.89 ?  406 ASP B CB    1 
ATOM   8839  C  CG    . ASP B 1 406 ? 122.855 151.742 143.255 1.00 29.59 ?  406 ASP B CG    1 
ATOM   8840  O  OD1   . ASP B 1 406 ? 121.635 151.483 143.194 1.00 31.46 ?  406 ASP B OD1   1 
ATOM   8841  O  OD2   . ASP B 1 406 ? 123.616 151.664 142.269 1.00 31.03 -1 406 ASP B OD2   1 
ATOM   8842  N  N     . ILE B 1 407 ? 122.303 151.311 147.705 1.00 18.55 ?  407 ILE B N     1 
ATOM   8843  C  CA    . ILE B 1 407 ? 122.535 151.140 149.132 1.00 14.68 ?  407 ILE B CA    1 
ATOM   8844  C  C     . ILE B 1 407 ? 123.987 150.764 149.404 1.00 15.53 ?  407 ILE B C     1 
ATOM   8845  O  O     . ILE B 1 407 ? 124.618 150.009 148.651 1.00 21.25 ?  407 ILE B O     1 
ATOM   8846  C  CB    . ILE B 1 407 ? 121.572 150.082 149.701 1.00 15.58 ?  407 ILE B CB    1 
ATOM   8847  C  CG1   . ILE B 1 407 ? 120.122 150.452 149.393 1.00 3.84  ?  407 ILE B CG1   1 
ATOM   8848  C  CG2   . ILE B 1 407 ? 121.771 149.926 151.185 1.00 13.32 ?  407 ILE B CG2   1 
ATOM   8849  C  CD1   . ILE B 1 407 ? 119.224 149.254 149.241 1.00 11.74 ?  407 ILE B CD1   1 
ATOM   8850  N  N     . SER B 1 408 ? 124.522 151.305 150.496 1.00 26.34 ?  408 SER B N     1 
ATOM   8851  C  CA    . SER B 1 408 ? 125.854 150.969 150.983 1.00 23.56 ?  408 SER B CA    1 
ATOM   8852  C  C     . SER B 1 408 ? 125.949 151.429 152.428 1.00 27.78 ?  408 SER B C     1 
ATOM   8853  O  O     . SER B 1 408 ? 125.675 152.596 152.723 1.00 38.28 ?  408 SER B O     1 
ATOM   8854  C  CB    . SER B 1 408 ? 126.941 151.635 150.132 1.00 29.16 ?  408 SER B CB    1 
ATOM   8855  O  OG    . SER B 1 408 ? 128.074 151.959 150.914 1.00 27.58 ?  408 SER B OG    1 
ATOM   8856  N  N     . CYS B 1 409 ? 126.322 150.520 153.324 1.00 23.83 ?  409 CYS B N     1 
ATOM   8857  C  CA    . CYS B 1 409 ? 126.468 150.852 154.733 1.00 30.39 ?  409 CYS B CA    1 
ATOM   8858  C  C     . CYS B 1 409 ? 127.744 150.230 155.281 1.00 28.90 ?  409 CYS B C     1 
ATOM   8859  O  O     . CYS B 1 409 ? 128.254 149.235 154.759 1.00 26.96 ?  409 CYS B O     1 
ATOM   8860  C  CB    . CYS B 1 409 ? 125.257 150.391 155.560 1.00 25.10 ?  409 CYS B CB    1 
ATOM   8861  S  SG    . CYS B 1 409 ? 125.199 148.623 155.913 1.00 45.46 ?  409 CYS B SG    1 
ATOM   8862  N  N     . ASN B 1 410 ? 128.254 150.840 156.346 1.00 22.93 ?  410 ASN B N     1 
ATOM   8863  C  CA    . ASN B 1 410 ? 129.470 150.394 157.010 1.00 20.91 ?  410 ASN B CA    1 
ATOM   8864  C  C     . ASN B 1 410 ? 129.099 149.524 158.200 1.00 25.91 ?  410 ASN B C     1 
ATOM   8865  O  O     . ASN B 1 410 ? 128.206 149.877 158.977 1.00 28.35 ?  410 ASN B O     1 
ATOM   8866  C  CB    . ASN B 1 410 ? 130.308 151.587 157.464 1.00 24.20 ?  410 ASN B CB    1 
ATOM   8867  C  CG    . ASN B 1 410 ? 130.092 152.803 156.596 1.00 32.33 ?  410 ASN B CG    1 
ATOM   8868  O  OD1   . ASN B 1 410 ? 129.508 153.791 157.033 1.00 34.43 ?  410 ASN B OD1   1 
ATOM   8869  N  ND2   . ASN B 1 410 ? 130.561 152.737 155.356 1.00 34.92 ?  410 ASN B ND2   1 
ATOM   8870  N  N     . LEU B 1 411 ? 129.781 148.396 158.339 1.00 19.65 ?  411 LEU B N     1 
ATOM   8871  C  CA    . LEU B 1 411 ? 129.456 147.412 159.359 1.00 10.94 ?  411 LEU B CA    1 
ATOM   8872  C  C     . LEU B 1 411 ? 130.346 147.585 160.583 1.00 11.69 ?  411 LEU B C     1 
ATOM   8873  O  O     . LEU B 1 411 ? 131.515 147.964 160.481 1.00 22.88 ?  411 LEU B O     1 
ATOM   8874  C  CB    . LEU B 1 411 ? 129.603 145.992 158.810 1.00 19.20 ?  411 LEU B CB    1 
ATOM   8875  C  CG    . LEU B 1 411 ? 128.436 145.358 158.051 1.00 17.67 ?  411 LEU B CG    1 
ATOM   8876  C  CD1   . LEU B 1 411 ? 128.158 146.076 156.743 1.00 18.06 ?  411 LEU B CD1   1 
ATOM   8877  C  CD2   . LEU B 1 411 ? 128.735 143.893 157.797 1.00 23.52 ?  411 LEU B CD2   1 
ATOM   8878  N  N     . GLY B 1 412 ? 129.769 147.308 161.745 1.00 17.26 ?  412 GLY B N     1 
ATOM   8879  C  CA    . GLY B 1 412 ? 130.491 147.293 163.000 1.00 11.56 ?  412 GLY B CA    1 
ATOM   8880  C  C     . GLY B 1 412 ? 129.680 146.551 164.037 1.00 10.58 ?  412 GLY B C     1 
ATOM   8881  O  O     . GLY B 1 412 ? 128.469 146.759 164.130 1.00 27.55 ?  412 GLY B O     1 
ATOM   8882  N  N     . SER B 1 413 ? 130.312 145.680 164.815 1.00 11.05 ?  413 SER B N     1 
ATOM   8883  C  CA    . SER B 1 413 ? 129.588 144.796 165.716 1.00 11.98 ?  413 SER B CA    1 
ATOM   8884  C  C     . SER B 1 413 ? 129.945 145.078 167.167 1.00 19.09 ?  413 SER B C     1 
ATOM   8885  O  O     . SER B 1 413 ? 131.119 145.231 167.513 1.00 20.96 ?  413 SER B O     1 
ATOM   8886  C  CB    . SER B 1 413 ? 129.882 143.331 165.392 1.00 13.26 ?  413 SER B CB    1 
ATOM   8887  O  OG    . SER B 1 413 ? 129.363 142.984 164.122 1.00 31.25 ?  413 SER B OG    1 
ATOM   8888  N  N     . LEU B 1 414 ? 128.927 145.131 168.015 1.00 20.36 ?  414 LEU B N     1 
ATOM   8889  C  CA    . LEU B 1 414 ? 129.131 145.166 169.452 1.00 13.08 ?  414 LEU B CA    1 
ATOM   8890  C  C     . LEU B 1 414 ? 129.341 143.751 169.966 1.00 21.50 ?  414 LEU B C     1 
ATOM   8891  O  O     . LEU B 1 414 ? 128.617 142.828 169.588 1.00 25.61 ?  414 LEU B O     1 
ATOM   8892  C  CB    . LEU B 1 414 ? 127.933 145.800 170.160 1.00 22.88 ?  414 LEU B CB    1 
ATOM   8893  C  CG    . LEU B 1 414 ? 127.415 147.132 169.626 1.00 21.75 ?  414 LEU B CG    1 
ATOM   8894  C  CD1   . LEU B 1 414 ? 126.149 147.519 170.360 1.00 22.36 ?  414 LEU B CD1   1 
ATOM   8895  C  CD2   . LEU B 1 414 ? 128.471 148.212 169.774 1.00 24.62 ?  414 LEU B CD2   1 
ATOM   8896  N  N     . ASN B 1 415 ? 130.342 143.583 170.822 1.00 29.80 ?  415 ASN B N     1 
ATOM   8897  C  CA    . ASN B 1 415 ? 130.536 142.317 171.518 1.00 27.12 ?  415 ASN B CA    1 
ATOM   8898  C  C     . ASN B 1 415 ? 129.664 142.338 172.764 1.00 25.14 ?  415 ASN B C     1 
ATOM   8899  O  O     . ASN B 1 415 ? 129.975 143.032 173.737 1.00 29.23 ?  415 ASN B O     1 
ATOM   8900  C  CB    . ASN B 1 415 ? 132.008 142.114 171.861 1.00 22.71 ?  415 ASN B CB    1 
ATOM   8901  C  CG    . ASN B 1 415 ? 132.329 140.685 172.248 1.00 28.99 ?  415 ASN B CG    1 
ATOM   8902  O  OD1   . ASN B 1 415 ? 131.591 140.048 172.997 1.00 34.87 ?  415 ASN B OD1   1 
ATOM   8903  N  ND2   . ASN B 1 415 ? 133.441 140.173 171.737 1.00 29.53 ?  415 ASN B ND2   1 
ATOM   8904  N  N     . ILE B 1 416 ? 128.569 141.575 172.734 1.00 20.40 ?  416 ILE B N     1 
ATOM   8905  C  CA    . ILE B 1 416 ? 127.556 141.672 173.782 1.00 23.03 ?  416 ILE B CA    1 
ATOM   8906  C  C     . ILE B 1 416 ? 128.142 141.299 175.137 1.00 30.00 ?  416 ILE B C     1 
ATOM   8907  O  O     . ILE B 1 416 ? 127.875 141.962 176.147 1.00 30.28 ?  416 ILE B O     1 
ATOM   8908  C  CB    . ILE B 1 416 ? 126.340 140.798 173.422 1.00 22.35 ?  416 ILE B CB    1 
ATOM   8909  C  CG1   . ILE B 1 416 ? 125.606 141.396 172.220 1.00 22.82 ?  416 ILE B CG1   1 
ATOM   8910  C  CG2   . ILE B 1 416 ? 125.399 140.673 174.604 1.00 17.29 ?  416 ILE B CG2   1 
ATOM   8911  C  CD1   . ILE B 1 416 ? 124.481 140.539 171.692 1.00 21.61 ?  416 ILE B CD1   1 
ATOM   8912  N  N     . LEU B 1 417 ? 128.959 140.245 175.181 1.00 24.98 ?  417 LEU B N     1 
ATOM   8913  C  CA    . LEU B 1 417 ? 129.558 139.827 176.445 1.00 27.55 ?  417 LEU B CA    1 
ATOM   8914  C  C     . LEU B 1 417 ? 130.456 140.914 177.018 1.00 28.75 ?  417 LEU B C     1 
ATOM   8915  O  O     . LEU B 1 417 ? 130.365 141.250 178.205 1.00 34.00 ?  417 LEU B O     1 
ATOM   8916  C  CB    . LEU B 1 417 ? 130.344 138.531 176.247 1.00 28.61 ?  417 LEU B CB    1 
ATOM   8917  C  CG    . LEU B 1 417 ? 130.960 137.931 177.511 1.00 29.91 ?  417 LEU B CG    1 
ATOM   8918  C  CD1   . LEU B 1 417 ? 130.407 136.544 177.760 1.00 27.31 ?  417 LEU B CD1   1 
ATOM   8919  C  CD2   . LEU B 1 417 ? 132.474 137.893 177.399 1.00 32.64 ?  417 LEU B CD2   1 
ATOM   8920  N  N     . ASN B 1 418 ? 131.325 141.488 176.184 1.00 34.08 ?  418 ASN B N     1 
ATOM   8921  C  CA    . ASN B 1 418 ? 132.239 142.515 176.668 1.00 29.41 ?  418 ASN B CA    1 
ATOM   8922  C  C     . ASN B 1 418 ? 131.517 143.825 176.955 1.00 29.20 ?  418 ASN B C     1 
ATOM   8923  O  O     . ASN B 1 418 ? 131.883 144.539 177.895 1.00 35.03 ?  418 ASN B O     1 
ATOM   8924  C  CB    . ASN B 1 418 ? 133.363 142.733 175.658 1.00 27.06 ?  418 ASN B CB    1 
ATOM   8925  C  CG    . ASN B 1 418 ? 134.290 141.539 175.559 1.00 28.65 ?  418 ASN B CG    1 
ATOM   8926  O  OD1   . ASN B 1 418 ? 134.616 140.910 176.564 1.00 36.71 ?  418 ASN B OD1   1 
ATOM   8927  N  ND2   . ASN B 1 418 ? 134.716 141.218 174.344 1.00 30.28 ?  418 ASN B ND2   1 
ATOM   8928  N  N     . VAL B 1 419 ? 130.500 144.159 176.159 1.00 31.16 ?  419 VAL B N     1 
ATOM   8929  C  CA    . VAL B 1 419 ? 129.742 145.384 176.395 1.00 31.46 ?  419 VAL B CA    1 
ATOM   8930  C  C     . VAL B 1 419 ? 128.991 145.304 177.719 1.00 29.36 ?  419 VAL B C     1 
ATOM   8931  O  O     . VAL B 1 419 ? 128.997 146.253 178.512 1.00 36.08 ?  419 VAL B O     1 
ATOM   8932  C  CB    . VAL B 1 419 ? 128.790 145.659 175.216 1.00 26.47 ?  419 VAL B CB    1 
ATOM   8933  C  CG1   . VAL B 1 419 ? 127.711 146.636 175.620 1.00 28.15 ?  419 VAL B CG1   1 
ATOM   8934  C  CG2   . VAL B 1 419 ? 129.565 146.200 174.032 1.00 25.84 ?  419 VAL B CG2   1 
ATOM   8935  N  N     . MET B 1 420 ? 128.340 144.169 177.987 1.00 31.99 ?  420 MET B N     1 
ATOM   8936  C  CA    . MET B 1 420 ? 127.578 144.041 179.222 1.00 34.66 ?  420 MET B CA    1 
ATOM   8937  C  C     . MET B 1 420 ? 128.472 143.812 180.434 1.00 33.26 ?  420 MET B C     1 
ATOM   8938  O  O     . MET B 1 420 ? 128.113 144.220 181.544 1.00 35.93 ?  420 MET B O     1 
ATOM   8939  C  CB    . MET B 1 420 ? 126.552 142.913 179.102 1.00 32.45 ?  420 MET B CB    1 
ATOM   8940  C  CG    . MET B 1 420 ? 125.495 143.165 178.043 1.00 30.51 ?  420 MET B CG    1 
ATOM   8941  S  SD    . MET B 1 420 ? 123.961 143.808 178.735 1.00 43.53 ?  420 MET B SD    1 
ATOM   8942  C  CE    . MET B 1 420 ? 123.779 142.795 180.197 1.00 31.04 ?  420 MET B CE    1 
ATOM   8943  N  N     . GLU B 1 421 ? 129.624 143.164 180.251 1.00 37.77 ?  421 GLU B N     1 
ATOM   8944  C  CA    . GLU B 1 421 ? 130.566 143.014 181.355 1.00 34.78 ?  421 GLU B CA    1 
ATOM   8945  C  C     . GLU B 1 421 ? 131.095 144.367 181.808 1.00 38.51 ?  421 GLU B C     1 
ATOM   8946  O  O     . GLU B 1 421 ? 131.249 144.615 183.010 1.00 41.72 ?  421 GLU B O     1 
ATOM   8947  C  CB    . GLU B 1 421 ? 131.713 142.093 180.941 1.00 34.46 ?  421 GLU B CB    1 
ATOM   8948  C  CG    . GLU B 1 421 ? 132.957 142.211 181.805 1.00 42.35 ?  421 GLU B CG    1 
ATOM   8949  C  CD    . GLU B 1 421 ? 134.232 142.231 180.986 1.00 44.83 ?  421 GLU B CD    1 
ATOM   8950  O  OE1   . GLU B 1 421 ? 134.143 142.127 179.744 1.00 43.17 ?  421 GLU B OE1   1 
ATOM   8951  O  OE2   . GLU B 1 421 ? 135.322 142.350 181.584 1.00 41.27 -1 421 GLU B OE2   1 
ATOM   8952  N  N     . HIS B 1 422 ? 131.366 145.262 180.860 1.00 34.24 ?  422 HIS B N     1 
ATOM   8953  C  CA    . HIS B 1 422 ? 131.822 146.609 181.175 1.00 35.44 ?  422 HIS B CA    1 
ATOM   8954  C  C     . HIS B 1 422 ? 130.680 147.555 181.519 1.00 38.64 ?  422 HIS B C     1 
ATOM   8955  O  O     . HIS B 1 422 ? 130.946 148.705 181.882 1.00 41.12 ?  422 HIS B O     1 
ATOM   8956  C  CB    . HIS B 1 422 ? 132.627 147.175 180.002 1.00 32.69 ?  422 HIS B CB    1 
ATOM   8957  C  CG    . HIS B 1 422 ? 133.938 146.487 179.781 1.00 35.81 ?  422 HIS B CG    1 
ATOM   8958  N  ND1   . HIS B 1 422 ? 134.067 145.375 178.978 1.00 36.57 ?  422 HIS B ND1   1 
ATOM   8959  C  CD2   . HIS B 1 422 ? 135.175 146.752 180.260 1.00 37.01 ?  422 HIS B CD2   1 
ATOM   8960  C  CE1   . HIS B 1 422 ? 135.329 144.985 178.971 1.00 39.80 ?  422 HIS B CE1   1 
ATOM   8961  N  NE2   . HIS B 1 422 ? 136.022 145.803 179.741 1.00 39.81 ?  422 HIS B NE2   1 
ATOM   8962  N  N     . LYS B 1 423 ? 129.429 147.099 181.417 1.00 40.97 ?  423 LYS B N     1 
ATOM   8963  C  CA    . LYS B 1 423 ? 128.255 147.920 181.720 1.00 42.37 ?  423 LYS B CA    1 
ATOM   8964  C  C     . LYS B 1 423 ? 128.278 149.224 180.928 1.00 43.69 ?  423 LYS B C     1 
ATOM   8965  O  O     . LYS B 1 423 ? 128.009 150.305 181.456 1.00 46.33 ?  423 LYS B O     1 
ATOM   8966  C  CB    . LYS B 1 423 ? 128.153 148.197 183.221 1.00 40.41 ?  423 LYS B CB    1 
ATOM   8967  C  CG    . LYS B 1 423 ? 127.642 147.023 184.038 1.00 42.43 ?  423 LYS B CG    1 
ATOM   8968  C  CD    . LYS B 1 423 ? 127.750 147.303 185.527 1.00 43.32 ?  423 LYS B CD    1 
ATOM   8969  C  CE    . LYS B 1 423 ? 128.917 146.549 186.147 1.00 45.85 ?  423 LYS B CE    1 
ATOM   8970  N  NZ    . LYS B 1 423 ? 128.469 145.592 187.196 1.00 43.92 1  423 LYS B NZ    1 
ATOM   8971  N  N     . SER B 1 424 ? 128.601 149.119 179.642 1.00 31.73 ?  424 SER B N     1 
ATOM   8972  C  CA    . SER B 1 424 ? 128.857 150.279 178.798 1.00 33.97 ?  424 SER B CA    1 
ATOM   8973  C  C     . SER B 1 424 ? 128.114 150.164 177.476 1.00 34.09 ?  424 SER B C     1 
ATOM   8974  O  O     . SER B 1 424 ? 128.683 150.353 176.400 1.00 32.55 ?  424 SER B O     1 
ATOM   8975  C  CB    . SER B 1 424 ? 130.352 150.441 178.552 1.00 35.65 ?  424 SER B CB    1 
ATOM   8976  O  OG    . SER B 1 424 ? 130.835 149.413 177.706 1.00 32.02 ?  424 SER B OG    1 
ATOM   8977  N  N     . ILE B 1 425 ? 126.820 149.842 177.535 1.00 33.46 ?  425 ILE B N     1 
ATOM   8978  C  CA    . ILE B 1 425 ? 126.015 149.817 176.316 1.00 26.93 ?  425 ILE B CA    1 
ATOM   8979  C  C     . ILE B 1 425 ? 125.991 151.197 175.673 1.00 32.03 ?  425 ILE B C     1 
ATOM   8980  O  O     . ILE B 1 425 ? 126.230 151.347 174.470 1.00 35.69 ?  425 ILE B O     1 
ATOM   8981  C  CB    . ILE B 1 425 ? 124.592 149.313 176.614 1.00 32.10 ?  425 ILE B CB    1 
ATOM   8982  C  CG1   . ILE B 1 425 ? 124.584 147.799 176.823 1.00 32.37 ?  425 ILE B CG1   1 
ATOM   8983  C  CG2   . ILE B 1 425 ? 123.646 149.682 175.482 1.00 27.48 ?  425 ILE B CG2   1 
ATOM   8984  C  CD1   . ILE B 1 425 ? 123.244 147.258 177.262 1.00 33.35 ?  425 ILE B CD1   1 
ATOM   8985  N  N     . GLU B 1 426 ? 125.729 152.230 176.478 1.00 27.69 ?  426 GLU B N     1 
ATOM   8986  C  CA    . GLU B 1 426 ? 125.597 153.580 175.938 1.00 23.51 ?  426 GLU B CA    1 
ATOM   8987  C  C     . GLU B 1 426 ? 126.899 154.059 175.310 1.00 26.23 ?  426 GLU B C     1 
ATOM   8988  O  O     . GLU B 1 426 ? 126.918 154.498 174.154 1.00 34.59 ?  426 GLU B O     1 
ATOM   8989  C  CB    . GLU B 1 426 ? 125.152 154.538 177.042 1.00 26.59 ?  426 GLU B CB    1 
ATOM   8990  C  CG    . GLU B 1 426 ? 125.357 156.003 176.705 1.00 29.01 ?  426 GLU B CG    1 
ATOM   8991  C  CD    . GLU B 1 426 ? 124.883 156.927 177.808 1.00 33.93 ?  426 GLU B CD    1 
ATOM   8992  O  OE1   . GLU B 1 426 ? 124.531 156.427 178.896 1.00 33.66 ?  426 GLU B OE1   1 
ATOM   8993  O  OE2   . GLU B 1 426 ? 124.863 158.156 177.586 1.00 36.80 -1 426 GLU B OE2   1 
ATOM   8994  N  N     . LYS B 1 427 ? 128.001 153.983 176.059 1.00 33.18 ?  427 LYS B N     1 
ATOM   8995  C  CA    . LYS B 1 427 ? 129.271 154.501 175.561 1.00 27.99 ?  427 LYS B CA    1 
ATOM   8996  C  C     . LYS B 1 427 ? 129.737 153.733 174.333 1.00 28.32 ?  427 LYS B C     1 
ATOM   8997  O  O     . LYS B 1 427 ? 130.185 154.334 173.348 1.00 32.78 ?  427 LYS B O     1 
ATOM   8998  C  CB    . LYS B 1 427 ? 130.326 154.450 176.665 1.00 28.87 ?  427 LYS B CB    1 
ATOM   8999  C  CG    . LYS B 1 427 ? 131.745 154.701 176.183 1.00 32.24 ?  427 LYS B CG    1 
ATOM   9000  C  CD    . LYS B 1 427 ? 132.760 154.455 177.286 1.00 33.02 ?  427 LYS B CD    1 
ATOM   9001  C  CE    . LYS B 1 427 ? 132.762 153.003 177.731 1.00 31.84 ?  427 LYS B CE    1 
ATOM   9002  N  NZ    . LYS B 1 427 ? 132.684 152.062 176.580 1.00 33.99 1  427 LYS B NZ    1 
ATOM   9003  N  N     . THR B 1 428 ? 129.630 152.403 174.367 1.00 30.09 ?  428 THR B N     1 
ATOM   9004  C  CA    . THR B 1 428 ? 130.050 151.600 173.225 1.00 24.75 ?  428 THR B CA    1 
ATOM   9005  C  C     . THR B 1 428 ? 129.199 151.898 172.000 1.00 24.98 ?  428 THR B C     1 
ATOM   9006  O  O     . THR B 1 428 ? 129.728 152.028 170.891 1.00 32.34 ?  428 THR B O     1 
ATOM   9007  C  CB    . THR B 1 428 ? 129.986 150.112 173.565 1.00 24.64 ?  428 THR B CB    1 
ATOM   9008  O  OG1   . THR B 1 428 ? 130.628 149.881 174.825 1.00 26.31 ?  428 THR B OG1   1 
ATOM   9009  C  CG2   . THR B 1 428 ? 130.681 149.298 172.491 1.00 25.22 ?  428 THR B CG2   1 
ATOM   9010  N  N     . VAL B 1 429 ? 127.881 152.014 172.178 1.00 23.05 ?  429 VAL B N     1 
ATOM   9011  C  CA    . VAL B 1 429 ? 127.006 152.289 171.043 1.00 22.40 ?  429 VAL B CA    1 
ATOM   9012  C  C     . VAL B 1 429 ? 127.326 153.649 170.438 1.00 27.00 ?  429 VAL B C     1 
ATOM   9013  O  O     . VAL B 1 429 ? 127.422 153.789 169.213 1.00 28.05 ?  429 VAL B O     1 
ATOM   9014  C  CB    . VAL B 1 429 ? 125.527 152.187 171.463 1.00 25.19 ?  429 VAL B CB    1 
ATOM   9015  C  CG1   . VAL B 1 429 ? 124.642 152.863 170.436 1.00 22.74 ?  429 VAL B CG1   1 
ATOM   9016  C  CG2   . VAL B 1 429 ? 125.121 150.735 171.614 1.00 26.03 ?  429 VAL B CG2   1 
ATOM   9017  N  N     . LYS B 1 430 ? 127.504 154.671 171.280 1.00 25.79 ?  430 LYS B N     1 
ATOM   9018  C  CA    . LYS B 1 430 ? 127.787 156.005 170.753 1.00 20.82 ?  430 LYS B CA    1 
ATOM   9019  C  C     . LYS B 1 430 ? 129.139 156.056 170.049 1.00 23.73 ?  430 LYS B C     1 
ATOM   9020  O  O     . LYS B 1 430 ? 129.259 156.651 168.970 1.00 30.67 ?  430 LYS B O     1 
ATOM   9021  C  CB    . LYS B 1 430 ? 127.720 157.043 171.874 1.00 23.66 ?  430 LYS B CB    1 
ATOM   9022  C  CG    . LYS B 1 430 ? 126.402 157.047 172.630 1.00 25.85 ?  430 LYS B CG    1 
ATOM   9023  C  CD    . LYS B 1 430 ? 125.704 158.389 172.560 1.00 27.12 ?  430 LYS B CD    1 
ATOM   9024  C  CE    . LYS B 1 430 ? 124.565 158.457 173.561 1.00 29.17 ?  430 LYS B CE    1 
ATOM   9025  N  NZ    . LYS B 1 430 ? 124.079 159.849 173.761 1.00 32.65 1  430 LYS B NZ    1 
ATOM   9026  N  N     . LEU B 1 431 ? 130.166 155.433 170.633 1.00 25.57 ?  431 LEU B N     1 
ATOM   9027  C  CA    . LEU B 1 431 ? 131.479 155.437 169.996 1.00 21.63 ?  431 LEU B CA    1 
ATOM   9028  C  C     . LEU B 1 431 ? 131.469 154.649 168.692 1.00 24.56 ?  431 LEU B C     1 
ATOM   9029  O  O     . LEU B 1 431 ? 132.108 155.051 167.712 1.00 28.94 ?  431 LEU B O     1 
ATOM   9030  C  CB    . LEU B 1 431 ? 132.527 154.882 170.956 1.00 26.72 ?  431 LEU B CB    1 
ATOM   9031  C  CG    . LEU B 1 431 ? 133.239 155.902 171.844 1.00 29.74 ?  431 LEU B CG    1 
ATOM   9032  C  CD1   . LEU B 1 431 ? 134.112 155.197 172.865 1.00 27.85 ?  431 LEU B CD1   1 
ATOM   9033  C  CD2   . LEU B 1 431 ? 134.060 156.863 171.001 1.00 28.68 ?  431 LEU B CD2   1 
ATOM   9034  N  N     . ALA B 1 432 ? 130.753 153.522 168.658 1.00 26.78 ?  432 ALA B N     1 
ATOM   9035  C  CA    . ALA B 1 432 ? 130.637 152.753 167.425 1.00 15.82 ?  432 ALA B CA    1 
ATOM   9036  C  C     . ALA B 1 432 ? 129.888 153.535 166.357 1.00 25.44 ?  432 ALA B C     1 
ATOM   9037  O  O     . ALA B 1 432 ? 130.246 153.483 165.175 1.00 27.92 ?  432 ALA B O     1 
ATOM   9038  C  CB    . ALA B 1 432 ? 129.939 151.424 167.705 1.00 17.76 ?  432 ALA B CB    1 
ATOM   9039  N  N     . THR B 1 433 ? 128.839 154.260 166.752 1.00 25.72 ?  433 THR B N     1 
ATOM   9040  C  CA    . THR B 1 433 ? 128.123 155.103 165.804 1.00 19.97 ?  433 THR B CA    1 
ATOM   9041  C  C     . THR B 1 433 ? 129.032 156.189 165.247 1.00 23.21 ?  433 THR B C     1 
ATOM   9042  O  O     . THR B 1 433 ? 129.001 156.479 164.047 1.00 32.64 ?  433 THR B O     1 
ATOM   9043  C  CB    . THR B 1 433 ? 126.895 155.720 166.475 1.00 22.90 ?  433 THR B CB    1 
ATOM   9044  O  OG1   . THR B 1 433 ? 126.060 154.679 166.995 1.00 31.80 ?  433 THR B OG1   1 
ATOM   9045  C  CG2   . THR B 1 433 ? 126.098 156.550 165.481 1.00 22.05 ?  433 THR B CG2   1 
ATOM   9046  N  N     . ASP B 1 434 ? 129.858 156.793 166.104 1.00 23.10 ?  434 ASP B N     1 
ATOM   9047  C  CA    . ASP B 1 434 ? 130.804 157.801 165.632 1.00 23.64 ?  434 ASP B CA    1 
ATOM   9048  C  C     . ASP B 1 434 ? 131.820 157.203 164.665 1.00 20.53 ?  434 ASP B C     1 
ATOM   9049  O  O     . ASP B 1 434 ? 132.147 157.813 163.640 1.00 25.07 ?  434 ASP B O     1 
ATOM   9050  C  CB    . ASP B 1 434 ? 131.511 158.452 166.819 1.00 26.42 ?  434 ASP B CB    1 
ATOM   9051  C  CG    . ASP B 1 434 ? 130.573 159.273 167.674 1.00 32.91 ?  434 ASP B CG    1 
ATOM   9052  O  OD1   . ASP B 1 434 ? 129.645 159.889 167.110 1.00 34.35 ?  434 ASP B OD1   1 
ATOM   9053  O  OD2   . ASP B 1 434 ? 130.762 159.304 168.907 1.00 33.39 -1 434 ASP B OD2   1 
ATOM   9054  N  N     . SER B 1 435 ? 132.334 156.012 164.978 1.00 23.60 ?  435 SER B N     1 
ATOM   9055  C  CA    . SER B 1 435 ? 133.302 155.368 164.094 1.00 18.43 ?  435 SER B CA    1 
ATOM   9056  C  C     . SER B 1 435 ? 132.680 155.020 162.745 1.00 22.69 ?  435 SER B C     1 
ATOM   9057  O  O     . SER B 1 435 ? 133.310 155.207 161.697 1.00 32.06 ?  435 SER B O     1 
ATOM   9058  C  CB    . SER B 1 435 ? 133.869 154.117 164.762 1.00 22.49 ?  435 SER B CB    1 
ATOM   9059  O  OG    . SER B 1 435 ? 132.914 153.071 164.781 1.00 23.75 ?  435 SER B OG    1 
ATOM   9060  N  N     . LEU B 1 436 ? 131.445 154.518 162.750 1.00 21.95 ?  436 LEU B N     1 
ATOM   9061  C  CA    . LEU B 1 436 ? 130.774 154.191 161.495 1.00 13.09 ?  436 LEU B CA    1 
ATOM   9062  C  C     . LEU B 1 436 ? 130.453 155.450 160.699 1.00 18.56 ?  436 LEU B C     1 
ATOM   9063  O  O     . LEU B 1 436 ? 130.527 155.446 159.465 1.00 23.01 ?  436 LEU B O     1 
ATOM   9064  C  CB    . LEU B 1 436 ? 129.507 153.385 161.776 1.00 22.43 ?  436 LEU B CB    1 
ATOM   9065  C  CG    . LEU B 1 436 ? 129.726 151.996 162.380 1.00 21.08 ?  436 LEU B CG    1 
ATOM   9066  C  CD1   . LEU B 1 436 ? 128.435 151.452 162.967 1.00 18.38 ?  436 LEU B CD1   1 
ATOM   9067  C  CD2   . LEU B 1 436 ? 130.291 151.045 161.344 1.00 18.57 ?  436 LEU B CD2   1 
ATOM   9068  N  N     . THR B 1 437 ? 130.099 156.536 161.389 1.00 21.16 ?  437 THR B N     1 
ATOM   9069  C  CA    . THR B 1 437 ? 129.893 157.810 160.712 1.00 20.15 ?  437 THR B CA    1 
ATOM   9070  C  C     . THR B 1 437 ? 131.180 158.293 160.058 1.00 22.83 ?  437 THR B C     1 
ATOM   9071  O  O     . THR B 1 437 ? 131.162 158.795 158.929 1.00 29.74 ?  437 THR B O     1 
ATOM   9072  C  CB    . THR B 1 437 ? 129.374 158.850 161.704 1.00 20.41 ?  437 THR B CB    1 
ATOM   9073  O  OG1   . THR B 1 437 ? 128.218 158.336 162.374 1.00 23.40 ?  437 THR B OG1   1 
ATOM   9074  C  CG2   . THR B 1 437 ? 129.010 160.136 160.989 1.00 20.77 ?  437 THR B CG2   1 
ATOM   9075  N  N     . HIS B 1 438 ? 132.308 158.148 160.754 1.00 21.30 ?  438 HIS B N     1 
ATOM   9076  C  CA    . HIS B 1 438 ? 133.592 158.514 160.165 1.00 21.63 ?  438 HIS B CA    1 
ATOM   9077  C  C     . HIS B 1 438 ? 133.903 157.655 158.946 1.00 23.01 ?  438 HIS B C     1 
ATOM   9078  O  O     . HIS B 1 438 ? 134.374 158.165 157.921 1.00 32.46 ?  438 HIS B O     1 
ATOM   9079  C  CB    . HIS B 1 438 ? 134.702 158.386 161.208 1.00 26.49 ?  438 HIS B CB    1 
ATOM   9080  C  CG    . HIS B 1 438 ? 136.072 158.642 160.662 1.00 27.67 ?  438 HIS B CG    1 
ATOM   9081  N  ND1   . HIS B 1 438 ? 136.569 159.913 160.470 1.00 25.54 ?  438 HIS B ND1   1 
ATOM   9082  C  CD2   . HIS B 1 438 ? 137.044 157.792 160.259 1.00 28.00 ?  438 HIS B CD2   1 
ATOM   9083  C  CE1   . HIS B 1 438 ? 137.794 159.834 159.979 1.00 30.66 ?  438 HIS B CE1   1 
ATOM   9084  N  NE2   . HIS B 1 438 ? 138.105 158.558 159.840 1.00 31.16 ?  438 HIS B NE2   1 
ATOM   9085  N  N     . VAL B 1 439 ? 133.644 156.349 159.036 1.00 21.40 ?  439 VAL B N     1 
ATOM   9086  C  CA    . VAL B 1 439 ? 133.907 155.458 157.907 1.00 19.11 ?  439 VAL B CA    1 
ATOM   9087  C  C     . VAL B 1 439 ? 133.054 155.852 156.709 1.00 28.84 ?  439 VAL B C     1 
ATOM   9088  O  O     . VAL B 1 439 ? 133.523 155.847 155.565 1.00 32.53 ?  439 VAL B O     1 
ATOM   9089  C  CB    . VAL B 1 439 ? 133.672 153.991 158.314 1.00 23.77 ?  439 VAL B CB    1 
ATOM   9090  C  CG1   . VAL B 1 439 ? 133.712 153.085 157.092 1.00 20.70 ?  439 VAL B CG1   1 
ATOM   9091  C  CG2   . VAL B 1 439 ? 134.710 153.555 159.323 1.00 21.77 ?  439 VAL B CG2   1 
ATOM   9092  N  N     . SER B 1 440 ? 131.787 156.199 156.951 1.00 24.41 ?  440 SER B N     1 
ATOM   9093  C  CA    . SER B 1 440 ? 130.929 156.669 155.869 1.00 20.03 ?  440 SER B CA    1 
ATOM   9094  C  C     . SER B 1 440 ? 131.449 157.976 155.279 1.00 25.90 ?  440 SER B C     1 
ATOM   9095  O  O     . SER B 1 440 ? 131.456 158.155 154.057 1.00 31.54 ?  440 SER B O     1 
ATOM   9096  C  CB    . SER B 1 440 ? 129.497 156.841 156.371 1.00 22.41 ?  440 SER B CB    1 
ATOM   9097  O  OG    . SER B 1 440 ? 128.604 157.087 155.299 1.00 31.27 ?  440 SER B OG    1 
ATOM   9098  N  N     . GLU B 1 441 ? 131.886 158.901 156.136 1.00 26.70 ?  441 GLU B N     1 
ATOM   9099  C  CA    . GLU B 1 441 ? 132.319 160.213 155.664 1.00 24.82 ?  441 GLU B CA    1 
ATOM   9100  C  C     . GLU B 1 441 ? 133.583 160.120 154.818 1.00 32.63 ?  441 GLU B C     1 
ATOM   9101  O  O     . GLU B 1 441 ? 133.708 160.817 153.805 1.00 40.05 ?  441 GLU B O     1 
ATOM   9102  C  CB    . GLU B 1 441 ? 132.535 161.151 156.850 1.00 27.11 ?  441 GLU B CB    1 
ATOM   9103  C  CG    . GLU B 1 441 ? 131.257 161.793 157.362 1.00 27.69 ?  441 GLU B CG    1 
ATOM   9104  C  CD    . GLU B 1 441 ? 131.329 162.150 158.833 1.00 35.39 ?  441 GLU B CD    1 
ATOM   9105  O  OE1   . GLU B 1 441 ? 132.357 161.846 159.474 1.00 37.20 ?  441 GLU B OE1   1 
ATOM   9106  O  OE2   . GLU B 1 441 ? 130.353 162.733 159.349 1.00 36.45 -1 441 GLU B OE2   1 
ATOM   9107  N  N     . THR B 1 442 ? 134.531 159.271 155.210 1.00 31.61 ?  442 THR B N     1 
ATOM   9108  C  CA    . THR B 1 442 ? 135.771 159.129 154.457 1.00 30.94 ?  442 THR B CA    1 
ATOM   9109  C  C     . THR B 1 442 ? 135.659 158.151 153.294 1.00 29.64 ?  442 THR B C     1 
ATOM   9110  O  O     . THR B 1 442 ? 136.656 157.918 152.604 1.00 34.42 ?  442 THR B O     1 
ATOM   9111  C  CB    . THR B 1 442 ? 136.921 158.698 155.376 1.00 29.54 ?  442 THR B CB    1 
ATOM   9112  O  OG1   . THR B 1 442 ? 136.850 157.287 155.616 1.00 31.14 ?  442 THR B OG1   1 
ATOM   9113  C  CG2   . THR B 1 442 ? 136.879 159.458 156.687 1.00 31.60 ?  442 THR B CG2   1 
ATOM   9114  N  N     . THR B 1 443 ? 134.484 157.575 153.061 1.00 30.24 ?  443 THR B N     1 
ATOM   9115  C  CA    . THR B 1 443 ? 134.270 156.701 151.917 1.00 34.71 ?  443 THR B CA    1 
ATOM   9116  C  C     . THR B 1 443 ? 133.863 157.530 150.707 1.00 35.60 ?  443 THR B C     1 
ATOM   9117  O  O     . THR B 1 443 ? 132.890 158.288 150.763 1.00 36.53 ?  443 THR B O     1 
ATOM   9118  C  CB    . THR B 1 443 ? 133.198 155.654 152.222 1.00 33.90 ?  443 THR B CB    1 
ATOM   9119  O  OG1   . THR B 1 443 ? 133.693 154.728 153.197 1.00 39.26 ?  443 THR B OG1   1 
ATOM   9120  C  CG2   . THR B 1 443 ? 132.822 154.899 150.957 1.00 27.95 ?  443 THR B CG2   1 
ATOM   9121  N  N     . ASP B 1 444 ? 134.612 157.384 149.616 1.00 39.02 ?  444 ASP B N     1 
ATOM   9122  C  CA    . ASP B 1 444 ? 134.320 158.077 148.364 1.00 38.94 ?  444 ASP B CA    1 
ATOM   9123  C  C     . ASP B 1 444 ? 134.667 157.136 147.219 1.00 39.94 ?  444 ASP B C     1 
ATOM   9124  O  O     . ASP B 1 444 ? 135.848 156.903 146.942 1.00 40.16 ?  444 ASP B O     1 
ATOM   9125  C  CB    . ASP B 1 444 ? 135.102 159.387 148.257 1.00 41.00 ?  444 ASP B CB    1 
ATOM   9126  C  CG    . ASP B 1 444 ? 134.382 160.428 147.423 1.00 46.45 ?  444 ASP B CG    1 
ATOM   9127  O  OD1   . ASP B 1 444 ? 133.248 160.803 147.786 1.00 44.63 ?  444 ASP B OD1   1 
ATOM   9128  O  OD2   . ASP B 1 444 ? 134.953 160.875 146.405 1.00 43.46 -1 444 ASP B OD2   1 
ATOM   9129  N  N     . ILE B 1 445 ? 133.646 156.600 146.559 1.00 37.64 ?  445 ILE B N     1 
ATOM   9130  C  CA    . ILE B 1 445 ? 133.822 155.641 145.475 1.00 36.46 ?  445 ILE B CA    1 
ATOM   9131  C  C     . ILE B 1 445 ? 133.609 156.371 144.158 1.00 37.15 ?  445 ILE B C     1 
ATOM   9132  O  O     . ILE B 1 445 ? 132.529 156.916 143.906 1.00 42.66 ?  445 ILE B O     1 
ATOM   9133  C  CB    . ILE B 1 445 ? 132.858 154.454 145.619 1.00 32.65 ?  445 ILE B CB    1 
ATOM   9134  C  CG1   . ILE B 1 445 ? 133.300 153.563 146.779 1.00 33.55 ?  445 ILE B CG1   1 
ATOM   9135  C  CG2   . ILE B 1 445 ? 132.808 153.651 144.331 1.00 35.35 ?  445 ILE B CG2   1 
ATOM   9136  C  CD1   . ILE B 1 445 ? 132.213 152.670 147.301 1.00 35.02 ?  445 ILE B CD1   1 
ATOM   9137  N  N     . ARG B 1 446 ? 134.638 156.378 143.315 1.00 36.82 ?  446 ARG B N     1 
ATOM   9138  C  CA    . ARG B 1 446 ? 134.656 157.198 142.113 1.00 39.43 ?  446 ARG B CA    1 
ATOM   9139  C  C     . ARG B 1 446 ? 134.119 156.481 140.881 1.00 40.16 ?  446 ARG B C     1 
ATOM   9140  O  O     . ARG B 1 446 ? 134.068 157.088 139.806 1.00 37.10 ?  446 ARG B O     1 
ATOM   9141  C  CB    . ARG B 1 446 ? 136.081 157.691 141.839 1.00 37.35 ?  446 ARG B CB    1 
ATOM   9142  C  CG    . ARG B 1 446 ? 136.941 157.801 143.088 1.00 37.48 ?  446 ARG B CG    1 
ATOM   9143  C  CD    . ARG B 1 446 ? 136.632 159.065 143.876 1.00 39.79 ?  446 ARG B CD    1 
ATOM   9144  N  NE    . ARG B 1 446 ? 136.486 160.232 143.017 1.00 40.67 ?  446 ARG B NE    1 
ATOM   9145  C  CZ    . ARG B 1 446 ? 136.605 161.486 143.434 1.00 40.52 ?  446 ARG B CZ    1 
ATOM   9146  N  NH1   . ARG B 1 446 ? 136.871 161.771 144.698 1.00 37.72 1  446 ARG B NH1   1 
ATOM   9147  N  NH2   . ARG B 1 446 ? 136.451 162.478 142.561 1.00 39.59 ?  446 ARG B NH2   1 
ATOM   9148  N  N     . ASN B 1 447 ? 133.713 155.217 141.002 1.00 33.35 ?  447 ASN B N     1 
ATOM   9149  C  CA    . ASN B 1 447 ? 133.192 154.466 139.871 1.00 25.93 ?  447 ASN B CA    1 
ATOM   9150  C  C     . ASN B 1 447 ? 131.773 153.962 140.085 1.00 30.51 ?  447 ASN B C     1 
ATOM   9151  O  O     . ASN B 1 447 ? 131.207 153.347 139.173 1.00 37.20 ?  447 ASN B O     1 
ATOM   9152  C  CB    . ASN B 1 447 ? 134.111 153.281 139.547 1.00 31.43 ?  447 ASN B CB    1 
ATOM   9153  C  CG    . ASN B 1 447 ? 135.167 153.633 138.522 1.00 30.80 ?  447 ASN B CG    1 
ATOM   9154  O  OD1   . ASN B 1 447 ? 134.851 153.969 137.383 1.00 34.38 ?  447 ASN B OD1   1 
ATOM   9155  N  ND2   . ASN B 1 447 ? 136.430 153.562 138.923 1.00 29.87 ?  447 ASN B ND2   1 
ATOM   9156  N  N     . ALA B 1 448 ? 131.183 154.200 141.255 1.00 31.55 ?  448 ALA B N     1 
ATOM   9157  C  CA    . ALA B 1 448 ? 129.785 153.879 141.533 1.00 26.92 ?  448 ALA B CA    1 
ATOM   9158  C  C     . ALA B 1 448 ? 129.089 155.179 141.910 1.00 27.73 ?  448 ALA B C     1 
ATOM   9159  O  O     . ALA B 1 448 ? 129.151 155.614 143.070 1.00 29.36 ?  448 ALA B O     1 
ATOM   9160  C  CB    . ALA B 1 448 ? 129.662 152.835 142.639 1.00 26.31 ?  448 ALA B CB    1 
ATOM   9161  N  N     . PRO B 1 449 ? 128.424 155.840 140.959 1.00 27.20 ?  449 PRO B N     1 
ATOM   9162  C  CA    . PRO B 1 449 ? 127.847 157.158 141.269 1.00 24.21 ?  449 PRO B CA    1 
ATOM   9163  C  C     . PRO B 1 449 ? 126.656 157.082 142.201 1.00 24.86 ?  449 PRO B C     1 
ATOM   9164  O  O     . PRO B 1 449 ? 126.529 157.916 143.107 1.00 21.81 ?  449 PRO B O     1 
ATOM   9165  C  CB    . PRO B 1 449 ? 127.450 157.706 139.888 1.00 21.18 ?  449 PRO B CB    1 
ATOM   9166  C  CG    . PRO B 1 449 ? 127.965 156.715 138.882 1.00 25.67 ?  449 PRO B CG    1 
ATOM   9167  C  CD    . PRO B 1 449 ? 128.136 155.419 139.581 1.00 25.18 ?  449 PRO B CD    1 
ATOM   9168  N  N     . ALA B 1 450 ? 125.769 156.106 142.000 1.00 28.94 ?  450 ALA B N     1 
ATOM   9169  C  CA    . ALA B 1 450 ? 124.617 155.964 142.882 1.00 19.52 ?  450 ALA B CA    1 
ATOM   9170  C  C     . ALA B 1 450 ? 125.049 155.576 144.289 1.00 23.03 ?  450 ALA B C     1 
ATOM   9171  O  O     . ALA B 1 450 ? 124.475 156.055 145.272 1.00 24.84 ?  450 ALA B O     1 
ATOM   9172  C  CB    . ALA B 1 450 ? 123.641 154.941 142.308 1.00 19.72 ?  450 ALA B CB    1 
ATOM   9173  N  N     . VAL B 1 451 ? 126.065 154.718 144.407 1.00 26.08 ?  451 VAL B N     1 
ATOM   9174  C  CA    . VAL B 1 451 ? 126.589 154.360 145.722 1.00 19.47 ?  451 VAL B CA    1 
ATOM   9175  C  C     . VAL B 1 451 ? 127.168 155.586 146.415 1.00 19.53 ?  451 VAL B C     1 
ATOM   9176  O  O     . VAL B 1 451 ? 126.937 155.807 147.609 1.00 26.05 ?  451 VAL B O     1 
ATOM   9177  C  CB    . VAL B 1 451 ? 127.634 153.235 145.598 1.00 22.52 ?  451 VAL B CB    1 
ATOM   9178  C  CG1   . VAL B 1 451 ? 128.343 153.014 146.924 1.00 25.41 ?  451 VAL B CG1   1 
ATOM   9179  C  CG2   . VAL B 1 451 ? 126.979 151.950 145.128 1.00 19.90 ?  451 VAL B CG2   1 
ATOM   9180  N  N     . ARG B 1 452 ? 127.926 156.403 145.682 1.00 21.20 ?  452 ARG B N     1 
ATOM   9181  C  CA    . ARG B 1 452 ? 128.506 157.608 146.268 1.00 23.42 ?  452 ARG B CA    1 
ATOM   9182  C  C     . ARG B 1 452 ? 127.420 158.577 146.720 1.00 24.60 ?  452 ARG B C     1 
ATOM   9183  O  O     . ARG B 1 452 ? 127.478 159.124 147.830 1.00 30.17 ?  452 ARG B O     1 
ATOM   9184  C  CB    . ARG B 1 452 ? 129.439 158.280 145.259 1.00 20.90 ?  452 ARG B CB    1 
ATOM   9185  C  CG    . ARG B 1 452 ? 129.950 159.638 145.702 1.00 24.84 ?  452 ARG B CG    1 
ATOM   9186  C  CD    . ARG B 1 452 ? 131.364 159.886 145.214 1.00 27.79 ?  452 ARG B CD    1 
ATOM   9187  N  NE    . ARG B 1 452 ? 131.385 160.754 144.043 1.00 33.94 ?  452 ARG B NE    1 
ATOM   9188  C  CZ    . ARG B 1 452 ? 132.390 160.826 143.182 1.00 38.90 ?  452 ARG B CZ    1 
ATOM   9189  N  NH1   . ARG B 1 452 ? 133.480 160.093 143.330 1.00 31.79 1  452 ARG B NH1   1 
ATOM   9190  N  NH2   . ARG B 1 452 ? 132.299 161.656 142.147 1.00 34.38 ?  452 ARG B NH2   1 
ATOM   9191  N  N     . ARG B 1 453 ? 126.414 158.797 145.871 1.00 22.40 ?  453 ARG B N     1 
ATOM   9192  C  CA    . ARG B 1 453 ? 125.339 159.721 146.219 1.00 20.83 ?  453 ARG B CA    1 
ATOM   9193  C  C     . ARG B 1 453 ? 124.546 159.218 147.419 1.00 23.25 ?  453 ARG B C     1 
ATOM   9194  O  O     . ARG B 1 453 ? 124.188 160.000 148.306 1.00 25.88 ?  453 ARG B O     1 
ATOM   9195  C  CB    . ARG B 1 453 ? 124.424 159.935 145.012 1.00 20.64 ?  453 ARG B CB    1 
ATOM   9196  C  CG    . ARG B 1 453 ? 123.071 160.534 145.350 1.00 20.05 ?  453 ARG B CG    1 
ATOM   9197  C  CD    . ARG B 1 453 ? 122.401 161.114 144.119 1.00 20.46 ?  453 ARG B CD    1 
ATOM   9198  N  NE    . ARG B 1 453 ? 121.050 160.598 143.941 1.00 22.82 ?  453 ARG B NE    1 
ATOM   9199  C  CZ    . ARG B 1 453 ? 119.971 161.110 144.516 1.00 26.10 ?  453 ARG B CZ    1 
ATOM   9200  N  NH1   . ARG B 1 453 ? 120.046 162.161 145.316 1.00 28.13 1  453 ARG B NH1   1 
ATOM   9201  N  NH2   . ARG B 1 453 ? 118.786 160.554 144.283 1.00 25.07 ?  453 ARG B NH2   1 
ATOM   9202  N  N     . ALA B 1 454 ? 124.269 157.912 147.469 1.00 23.91 ?  454 ALA B N     1 
ATOM   9203  C  CA    . ALA B 1 454 ? 123.535 157.355 148.599 1.00 17.46 ?  454 ALA B CA    1 
ATOM   9204  C  C     . ALA B 1 454 ? 124.356 157.412 149.880 1.00 21.92 ?  454 ALA B C     1 
ATOM   9205  O  O     . ALA B 1 454 ? 123.808 157.646 150.959 1.00 24.78 ?  454 ALA B O     1 
ATOM   9206  C  CB    . ALA B 1 454 ? 123.112 155.921 148.293 1.00 19.55 ?  454 ALA B CB    1 
ATOM   9207  N  N     . ASN B 1 455 ? 125.668 157.190 149.790 1.00 23.90 ?  455 ASN B N     1 
ATOM   9208  C  CA    . ASN B 1 455 ? 126.514 157.328 150.968 1.00 20.72 ?  455 ASN B CA    1 
ATOM   9209  C  C     . ASN B 1 455 ? 126.512 158.764 151.472 1.00 26.36 ?  455 ASN B C     1 
ATOM   9210  O  O     . ASN B 1 455 ? 126.464 159.007 152.684 1.00 30.59 ?  455 ASN B O     1 
ATOM   9211  C  CB    . ASN B 1 455 ? 127.937 156.871 150.652 1.00 20.52 ?  455 ASN B CB    1 
ATOM   9212  C  CG    . ASN B 1 455 ? 128.818 156.821 151.881 1.00 24.75 ?  455 ASN B CG    1 
ATOM   9213  O  OD1   . ASN B 1 455 ? 128.690 155.924 152.713 1.00 30.97 ?  455 ASN B OD1   1 
ATOM   9214  N  ND2   . ASN B 1 455 ? 129.716 157.789 152.005 1.00 27.07 ?  455 ASN B ND2   1 
ATOM   9215  N  N     . LYS B 1 456 ? 126.562 159.732 150.554 1.00 27.25 ?  456 LYS B N     1 
ATOM   9216  C  CA    . LYS B 1 456 ? 126.580 161.133 150.958 1.00 25.06 ?  456 LYS B CA    1 
ATOM   9217  C  C     . LYS B 1 456 ? 125.237 161.587 151.518 1.00 23.96 ?  456 LYS B C     1 
ATOM   9218  O  O     . LYS B 1 456 ? 125.199 162.433 152.417 1.00 32.65 ?  456 LYS B O     1 
ATOM   9219  C  CB    . LYS B 1 456 ? 126.982 162.013 149.775 1.00 26.81 ?  456 LYS B CB    1 
ATOM   9220  C  CG    . LYS B 1 456 ? 128.115 162.979 150.073 1.00 30.51 ?  456 LYS B CG    1 
ATOM   9221  C  CD    . LYS B 1 456 ? 128.651 163.612 148.799 1.00 33.74 ?  456 LYS B CD    1 
ATOM   9222  C  CE    . LYS B 1 456 ? 129.145 162.557 147.822 1.00 33.23 ?  456 LYS B CE    1 
ATOM   9223  N  NZ    . LYS B 1 456 ? 130.408 161.916 148.282 1.00 28.20 1  456 LYS B NZ    1 
ATOM   9224  N  N     . ALA B 1 457 ? 124.131 161.046 151.007 1.00 24.59 ?  457 ALA B N     1 
ATOM   9225  C  CA    . ALA B 1 457 ? 122.801 161.522 151.379 1.00 18.66 ?  457 ALA B CA    1 
ATOM   9226  C  C     . ALA B 1 457 ? 122.207 160.730 152.541 1.00 26.26 ?  457 ALA B C     1 
ATOM   9227  O  O     . ALA B 1 457 ? 121.839 161.305 153.570 1.00 32.54 ?  457 ALA B O     1 
ATOM   9228  C  CB    . ALA B 1 457 ? 121.874 161.461 150.161 1.00 18.26 ?  457 ALA B CB    1 
ATOM   9229  N  N     . MET B 1 458 ? 122.092 159.411 152.378 1.00 24.94 ?  458 MET B N     1 
ATOM   9230  C  CA    . MET B 1 458 ? 121.504 158.566 153.411 1.00 16.55 ?  458 MET B CA    1 
ATOM   9231  C  C     . MET B 1 458 ? 122.336 158.579 154.687 1.00 21.35 ?  458 MET B C     1 
ATOM   9232  O  O     . MET B 1 458 ? 121.783 158.582 155.793 1.00 30.53 ?  458 MET B O     1 
ATOM   9233  C  CB    . MET B 1 458 ? 121.359 157.136 152.889 1.00 22.58 ?  458 MET B CB    1 
ATOM   9234  C  CG    . MET B 1 458 ? 120.708 157.029 151.521 1.00 21.89 ?  458 MET B CG    1 
ATOM   9235  S  SD    . MET B 1 458 ? 119.160 157.937 151.419 1.00 29.65 ?  458 MET B SD    1 
ATOM   9236  C  CE    . MET B 1 458 ? 118.133 156.935 152.487 1.00 23.61 ?  458 MET B CE    1 
ATOM   9237  N  N     . LYS B 1 459 ? 123.664 158.566 154.553 1.00 19.92 ?  459 LYS B N     1 
ATOM   9238  C  CA    . LYS B 1 459 ? 124.577 158.467 155.695 1.00 17.97 ?  459 LYS B CA    1 
ATOM   9239  C  C     . LYS B 1 459 ? 124.288 157.213 156.516 1.00 20.01 ?  459 LYS B C     1 
ATOM   9240  O  O     . LYS B 1 459 ? 124.425 157.203 157.740 1.00 26.61 ?  459 LYS B O     1 
ATOM   9241  C  CB    . LYS B 1 459 ? 124.512 159.717 156.576 1.00 20.12 ?  459 LYS B CB    1 
ATOM   9242  C  CG    . LYS B 1 459 ? 125.053 160.974 155.924 1.00 24.69 ?  459 LYS B CG    1 
ATOM   9243  C  CD    . LYS B 1 459 ? 124.279 162.198 156.379 1.00 25.09 ?  459 LYS B CD    1 
ATOM   9244  C  CE    . LYS B 1 459 ? 124.441 163.346 155.402 1.00 25.13 ?  459 LYS B CE    1 
ATOM   9245  N  NZ    . LYS B 1 459 ? 125.871 163.719 155.220 1.00 27.84 1  459 LYS B NZ    1 
ATOM   9246  N  N     . SER B 1 460 ? 123.886 156.147 155.833 1.00 24.04 ?  460 SER B N     1 
ATOM   9247  C  CA    . SER B 1 460 ? 123.480 154.922 156.503 1.00 13.89 ?  460 SER B CA    1 
ATOM   9248  C  C     . SER B 1 460 ? 124.687 154.163 157.032 1.00 13.09 ?  460 SER B C     1 
ATOM   9249  O  O     . SER B 1 460 ? 125.714 154.045 156.359 1.00 26.30 ?  460 SER B O     1 
ATOM   9250  C  CB    . SER B 1 460 ? 122.685 154.034 155.548 1.00 15.88 ?  460 SER B CB    1 
ATOM   9251  O  OG    . SER B 1 460 ? 122.889 152.667 155.852 1.00 26.50 ?  460 SER B OG    1 
ATOM   9252  N  N     . ILE B 1 461 ? 124.553 153.642 158.252 1.00 10.69 ?  461 ILE B N     1 
ATOM   9253  C  CA    . ILE B 1 461 ? 125.578 152.823 158.878 1.00 19.56 ?  461 ILE B CA    1 
ATOM   9254  C  C     . ILE B 1 461 ? 124.920 151.550 159.390 1.00 16.81 ?  461 ILE B C     1 
ATOM   9255  O  O     . ILE B 1 461 ? 123.704 151.479 159.570 1.00 20.02 ?  461 ILE B O     1 
ATOM   9256  C  CB    . ILE B 1 461 ? 126.297 153.557 160.031 1.00 14.38 ?  461 ILE B CB    1 
ATOM   9257  C  CG1   . ILE B 1 461 ? 125.308 153.890 161.148 1.00 10.83 ?  461 ILE B CG1   1 
ATOM   9258  C  CG2   . ILE B 1 461 ? 126.982 154.816 159.521 1.00 17.22 ?  461 ILE B CG2   1 
ATOM   9259  C  CD1   . ILE B 1 461 ? 125.956 154.439 162.396 1.00 14.55 ?  461 ILE B CD1   1 
ATOM   9260  N  N     . GLY B 1 462 ? 125.743 150.529 159.603 1.00 15.87 ?  462 GLY B N     1 
ATOM   9261  C  CA    . GLY B 1 462 ? 125.252 149.300 160.190 1.00 6.58  ?  462 GLY B CA    1 
ATOM   9262  C  C     . GLY B 1 462 ? 125.990 148.927 161.457 1.00 11.82 ?  462 GLY B C     1 
ATOM   9263  O  O     . GLY B 1 462 ? 127.166 148.557 161.410 1.00 26.95 ?  462 GLY B O     1 
ATOM   9264  N  N     . LEU B 1 463 ? 125.310 149.013 162.595 1.00 12.36 ?  463 LEU B N     1 
ATOM   9265  C  CA    . LEU B 1 463 ? 125.889 148.652 163.883 1.00 11.25 ?  463 LEU B CA    1 
ATOM   9266  C  C     . LEU B 1 463 ? 125.294 147.316 164.309 1.00 13.98 ?  463 LEU B C     1 
ATOM   9267  O  O     . LEU B 1 463 ? 124.130 147.246 164.711 1.00 25.51 ?  463 LEU B O     1 
ATOM   9268  C  CB    . LEU B 1 463 ? 125.627 149.737 164.925 1.00 19.67 ?  463 LEU B CB    1 
ATOM   9269  C  CG    . LEU B 1 463 ? 126.120 149.452 166.346 1.00 18.45 ?  463 LEU B CG    1 
ATOM   9270  C  CD1   . LEU B 1 463 ? 127.573 149.016 166.329 1.00 6.51  ?  463 LEU B CD1   1 
ATOM   9271  C  CD2   . LEU B 1 463 ? 125.932 150.671 167.233 1.00 14.56 ?  463 LEU B CD2   1 
ATOM   9272  N  N     . GLY B 1 464 ? 126.097 146.256 164.216 1.00 14.85 ?  464 GLY B N     1 
ATOM   9273  C  CA    . GLY B 1 464 ? 125.659 144.922 164.552 1.00 13.86 ?  464 GLY B CA    1 
ATOM   9274  C  C     . GLY B 1 464 ? 126.013 144.532 165.975 1.00 13.07 ?  464 GLY B C     1 
ATOM   9275  O  O     . GLY B 1 464 ? 126.407 145.353 166.806 1.00 15.05 ?  464 GLY B O     1 
ATOM   9276  N  N     . ALA B 1 465 ? 125.863 143.239 166.250 1.00 15.16 ?  465 ALA B N     1 
ATOM   9277  C  CA    . ALA B 1 465 ? 126.179 142.690 167.558 1.00 12.37 ?  465 ALA B CA    1 
ATOM   9278  C  C     . ALA B 1 465 ? 126.669 141.262 167.386 1.00 14.17 ?  465 ALA B C     1 
ATOM   9279  O  O     . ALA B 1 465 ? 126.202 140.541 166.500 1.00 28.53 ?  465 ALA B O     1 
ATOM   9280  C  CB    . ALA B 1 465 ? 124.965 142.728 168.494 1.00 19.00 ?  465 ALA B CB    1 
ATOM   9281  N  N     . MET B 1 466 ? 127.617 140.867 168.230 1.00 20.66 ?  466 MET B N     1 
ATOM   9282  C  CA    . MET B 1 466 ? 128.153 139.516 168.249 1.00 20.75 ?  466 MET B CA    1 
ATOM   9283  C  C     . MET B 1 466 ? 128.144 139.000 169.680 1.00 20.58 ?  466 MET B C     1 
ATOM   9284  O  O     . MET B 1 466 ? 127.930 139.753 170.634 1.00 26.81 ?  466 MET B O     1 
ATOM   9285  C  CB    . MET B 1 466 ? 129.575 139.463 167.671 1.00 27.19 ?  466 MET B CB    1 
ATOM   9286  C  CG    . MET B 1 466 ? 130.527 140.486 168.270 1.00 22.89 ?  466 MET B CG    1 
ATOM   9287  S  SD    . MET B 1 466 ? 132.197 140.402 167.595 1.00 38.02 ?  466 MET B SD    1 
ATOM   9288  C  CE    . MET B 1 466 ? 131.864 140.340 165.838 1.00 29.36 ?  466 MET B CE    1 
ATOM   9289  N  N     . ASN B 1 467 ? 128.365 137.691 169.816 1.00 19.96 ?  467 ASN B N     1 
ATOM   9290  C  CA    . ASN B 1 467 ? 128.502 137.032 171.116 1.00 19.55 ?  467 ASN B CA    1 
ATOM   9291  C  C     . ASN B 1 467 ? 127.208 137.088 171.927 1.00 20.51 ?  467 ASN B C     1 
ATOM   9292  O  O     . ASN B 1 467 ? 127.237 137.222 173.150 1.00 27.46 ?  467 ASN B O     1 
ATOM   9293  C  CB    . ASN B 1 467 ? 129.661 137.619 171.924 1.00 21.54 ?  467 ASN B CB    1 
ATOM   9294  C  CG    . ASN B 1 467 ? 130.459 136.559 172.651 1.00 24.57 ?  467 ASN B CG    1 
ATOM   9295  O  OD1   . ASN B 1 467 ? 130.268 135.364 172.433 1.00 28.94 ?  467 ASN B OD1   1 
ATOM   9296  N  ND2   . ASN B 1 467 ? 131.363 136.991 173.518 1.00 28.00 ?  467 ASN B ND2   1 
ATOM   9297  N  N     . LEU B 1 468 ? 126.064 136.995 171.247 1.00 19.53 ?  468 LEU B N     1 
ATOM   9298  C  CA    . LEU B 1 468 ? 124.806 136.838 171.970 1.00 18.12 ?  468 LEU B CA    1 
ATOM   9299  C  C     . LEU B 1 468 ? 124.734 135.469 172.631 1.00 22.01 ?  468 LEU B C     1 
ATOM   9300  O  O     . LEU B 1 468 ? 124.468 135.358 173.835 1.00 25.58 ?  468 LEU B O     1 
ATOM   9301  C  CB    . LEU B 1 468 ? 123.623 137.038 171.026 1.00 24.55 ?  468 LEU B CB    1 
ATOM   9302  C  CG    . LEU B 1 468 ? 122.260 136.686 171.625 1.00 20.38 ?  468 LEU B CG    1 
ATOM   9303  C  CD1   . LEU B 1 468 ? 121.918 137.626 172.768 1.00 17.94 ?  468 LEU B CD1   1 
ATOM   9304  C  CD2   . LEU B 1 468 ? 121.170 136.702 170.568 1.00 15.41 ?  468 LEU B CD2   1 
ATOM   9305  N  N     . HIS B 1 469 ? 124.999 134.413 171.861 1.00 25.31 ?  469 HIS B N     1 
ATOM   9306  C  CA    . HIS B 1 469 ? 124.962 133.066 172.417 1.00 16.96 ?  469 HIS B CA    1 
ATOM   9307  C  C     . HIS B 1 469 ? 126.091 132.854 173.415 1.00 26.08 ?  469 HIS B C     1 
ATOM   9308  O  O     . HIS B 1 469 ? 125.913 132.154 174.415 1.00 38.87 ?  469 HIS B O     1 
ATOM   9309  C  CB    . HIS B 1 469 ? 125.034 132.026 171.301 1.00 20.40 ?  469 HIS B CB    1 
ATOM   9310  C  CG    . HIS B 1 469 ? 124.611 130.655 171.732 1.00 24.73 ?  469 HIS B CG    1 
ATOM   9311  N  ND1   . HIS B 1 469 ? 124.754 129.545 170.931 1.00 28.72 ?  469 HIS B ND1   1 
ATOM   9312  C  CD2   . HIS B 1 469 ? 124.050 130.218 172.885 1.00 25.30 ?  469 HIS B CD2   1 
ATOM   9313  C  CE1   . HIS B 1 469 ? 124.298 128.482 171.569 1.00 22.84 ?  469 HIS B CE1   1 
ATOM   9314  N  NE2   . HIS B 1 469 ? 123.867 128.863 172.756 1.00 25.44 ?  469 HIS B NE2   1 
ATOM   9315  N  N     . GLY B 1 470 ? 127.259 133.443 173.157 1.00 21.78 ?  470 GLY B N     1 
ATOM   9316  C  CA    . GLY B 1 470 ? 128.344 133.347 174.119 1.00 18.71 ?  470 GLY B CA    1 
ATOM   9317  C  C     . GLY B 1 470 ? 127.986 133.970 175.453 1.00 19.99 ?  470 GLY B C     1 
ATOM   9318  O  O     . GLY B 1 470 ? 128.223 133.383 176.512 1.00 34.01 ?  470 GLY B O     1 
ATOM   9319  N  N     . TYR B 1 471 ? 127.396 135.166 175.418 1.00 22.88 ?  471 TYR B N     1 
ATOM   9320  C  CA    . TYR B 1 471 ? 126.980 135.818 176.654 1.00 25.52 ?  471 TYR B CA    1 
ATOM   9321  C  C     . TYR B 1 471 ? 125.899 135.015 177.364 1.00 27.96 ?  471 TYR B C     1 
ATOM   9322  O  O     . TYR B 1 471 ? 125.933 134.863 178.591 1.00 32.88 ?  471 TYR B O     1 
ATOM   9323  C  CB    . TYR B 1 471 ? 126.484 137.235 176.369 1.00 24.23 ?  471 TYR B CB    1 
ATOM   9324  C  CG    . TYR B 1 471 ? 126.103 137.997 177.617 1.00 26.56 ?  471 TYR B CG    1 
ATOM   9325  C  CD1   . TYR B 1 471 ? 127.076 138.452 178.498 1.00 28.31 ?  471 TYR B CD1   1 
ATOM   9326  C  CD2   . TYR B 1 471 ? 124.773 138.240 177.930 1.00 18.57 ?  471 TYR B CD2   1 
ATOM   9327  C  CE1   . TYR B 1 471 ? 126.736 139.144 179.641 1.00 28.21 ?  471 TYR B CE1   1 
ATOM   9328  C  CE2   . TYR B 1 471 ? 124.425 138.927 179.075 1.00 21.27 ?  471 TYR B CE2   1 
ATOM   9329  C  CZ    . TYR B 1 471 ? 125.410 139.377 179.925 1.00 27.48 ?  471 TYR B CZ    1 
ATOM   9330  O  OH    . TYR B 1 471 ? 125.071 140.060 181.069 1.00 32.99 ?  471 TYR B OH    1 
ATOM   9331  N  N     . LEU B 1 472 ? 124.926 134.495 176.610 1.00 26.27 ?  472 LEU B N     1 
ATOM   9332  C  CA    . LEU B 1 472 ? 123.838 133.747 177.232 1.00 23.87 ?  472 LEU B CA    1 
ATOM   9333  C  C     . LEU B 1 472 ? 124.333 132.444 177.850 1.00 25.52 ?  472 LEU B C     1 
ATOM   9334  O  O     . LEU B 1 472 ? 123.916 132.079 178.955 1.00 31.23 ?  472 LEU B O     1 
ATOM   9335  C  CB    . LEU B 1 472 ? 122.736 133.471 176.209 1.00 28.13 ?  472 LEU B CB    1 
ATOM   9336  C  CG    . LEU B 1 472 ? 121.995 134.687 175.653 1.00 27.42 ?  472 LEU B CG    1 
ATOM   9337  C  CD1   . LEU B 1 472 ? 121.139 134.292 174.460 1.00 24.49 ?  472 LEU B CD1   1 
ATOM   9338  C  CD2   . LEU B 1 472 ? 121.151 135.346 176.731 1.00 19.86 ?  472 LEU B CD2   1 
ATOM   9339  N  N     . ALA B 1 473 ? 125.219 131.727 177.154 1.00 25.93 ?  473 ALA B N     1 
ATOM   9340  C  CA    . ALA B 1 473 ? 125.713 130.455 177.665 1.00 26.31 ?  473 ALA B CA    1 
ATOM   9341  C  C     . ALA B 1 473 ? 126.669 130.657 178.832 1.00 33.22 ?  473 ALA B C     1 
ATOM   9342  O  O     . ALA B 1 473 ? 126.673 129.866 179.782 1.00 38.99 ?  473 ALA B O     1 
ATOM   9343  C  CB    . ALA B 1 473 ? 126.390 129.670 176.543 1.00 26.76 ?  473 ALA B CB    1 
ATOM   9344  N  N     . GLN B 1 474 ? 127.490 131.707 178.782 1.00 27.75 ?  474 GLN B N     1 
ATOM   9345  C  CA    . GLN B 1 474 ? 128.403 131.994 179.879 1.00 28.56 ?  474 GLN B CA    1 
ATOM   9346  C  C     . GLN B 1 474 ? 127.697 132.571 181.097 1.00 29.18 ?  474 GLN B C     1 
ATOM   9347  O  O     . GLN B 1 474 ? 128.320 132.680 182.159 1.00 36.85 ?  474 GLN B O     1 
ATOM   9348  C  CB    . GLN B 1 474 ? 129.500 132.953 179.410 1.00 28.71 ?  474 GLN B CB    1 
ATOM   9349  C  CG    . GLN B 1 474 ? 130.546 132.292 178.529 1.00 28.77 ?  474 GLN B CG    1 
ATOM   9350  C  CD    . GLN B 1 474 ? 131.528 133.283 177.947 1.00 33.70 ?  474 GLN B CD    1 
ATOM   9351  O  OE1   . GLN B 1 474 ? 132.338 133.868 178.666 1.00 36.08 ?  474 GLN B OE1   1 
ATOM   9352  N  NE2   . GLN B 1 474 ? 131.465 133.479 176.635 1.00 33.97 ?  474 GLN B NE2   1 
ATOM   9353  N  N     . ASN B 1 475 ? 126.425 132.945 180.970 1.00 31.43 ?  475 ASN B N     1 
ATOM   9354  C  CA    . ASN B 1 475 ? 125.629 133.431 182.087 1.00 31.52 ?  475 ASN B CA    1 
ATOM   9355  C  C     . ASN B 1 475 ? 124.538 132.449 182.491 1.00 31.77 ?  475 ASN B C     1 
ATOM   9356  O  O     . ASN B 1 475 ? 123.637 132.816 183.250 1.00 34.96 ?  475 ASN B O     1 
ATOM   9357  C  CB    . ASN B 1 475 ? 125.016 134.790 181.743 1.00 30.74 ?  475 ASN B CB    1 
ATOM   9358  C  CG    . ASN B 1 475 ? 126.039 135.905 181.756 1.00 30.26 ?  475 ASN B CG    1 
ATOM   9359  O  OD1   . ASN B 1 475 ? 126.234 136.574 182.770 1.00 38.24 ?  475 ASN B OD1   1 
ATOM   9360  N  ND2   . ASN B 1 475 ? 126.709 136.102 180.629 1.00 28.97 ?  475 ASN B ND2   1 
ATOM   9361  N  N     . GLY B 1 476 ? 124.599 131.214 182.003 1.00 31.06 ?  476 GLY B N     1 
ATOM   9362  C  CA    . GLY B 1 476 ? 123.619 130.204 182.359 1.00 30.18 ?  476 GLY B CA    1 
ATOM   9363  C  C     . GLY B 1 476 ? 122.217 130.474 181.859 1.00 35.17 ?  476 GLY B C     1 
ATOM   9364  O  O     . GLY B 1 476 ? 121.248 130.248 182.594 1.00 37.39 ?  476 GLY B O     1 
ATOM   9365  N  N     . ILE B 1 477 ? 122.082 130.957 180.627 1.00 32.15 ?  477 ILE B N     1 
ATOM   9366  C  CA    . ILE B 1 477 ? 120.785 131.209 180.012 1.00 27.50 ?  477 ILE B CA    1 
ATOM   9367  C  C     . ILE B 1 477 ? 120.719 130.425 178.710 1.00 31.33 ?  477 ILE B C     1 
ATOM   9368  O  O     . ILE B 1 477 ? 121.586 130.583 177.840 1.00 36.33 ?  477 ILE B O     1 
ATOM   9369  C  CB    . ILE B 1 477 ? 120.548 132.706 179.761 1.00 26.02 ?  477 ILE B CB    1 
ATOM   9370  C  CG1   . ILE B 1 477 ? 120.682 133.496 181.062 1.00 29.49 ?  477 ILE B CG1   1 
ATOM   9371  C  CG2   . ILE B 1 477 ? 119.179 132.929 179.147 1.00 30.20 ?  477 ILE B CG2   1 
ATOM   9372  C  CD1   . ILE B 1 477 ? 120.954 134.962 180.850 1.00 32.35 ?  477 ILE B CD1   1 
ATOM   9373  N  N     . ALA B 1 478 ? 119.700 129.580 178.579 1.00 33.41 ?  478 ALA B N     1 
ATOM   9374  C  CA    . ALA B 1 478 ? 119.501 128.836 177.343 1.00 27.28 ?  478 ALA B CA    1 
ATOM   9375  C  C     . ALA B 1 478 ? 119.080 129.784 176.229 1.00 32.74 ?  478 ALA B C     1 
ATOM   9376  O  O     . ALA B 1 478 ? 118.226 130.651 176.429 1.00 34.41 ?  478 ALA B O     1 
ATOM   9377  C  CB    . ALA B 1 478 ? 118.450 127.746 177.544 1.00 27.73 ?  478 ALA B CB    1 
ATOM   9378  N  N     . TYR B 1 479 ? 119.683 129.614 175.049 1.00 30.56 ?  479 TYR B N     1 
ATOM   9379  C  CA    . TYR B 1 479 ? 119.402 130.508 173.929 1.00 23.51 ?  479 TYR B CA    1 
ATOM   9380  C  C     . TYR B 1 479 ? 117.932 130.470 173.532 1.00 26.65 ?  479 TYR B C     1 
ATOM   9381  O  O     . TYR B 1 479 ? 117.382 131.487 173.096 1.00 32.90 ?  479 TYR B O     1 
ATOM   9382  C  CB    . TYR B 1 479 ? 120.294 130.141 172.742 1.00 18.58 ?  479 TYR B CB    1 
ATOM   9383  C  CG    . TYR B 1 479 ? 120.168 131.039 171.529 1.00 26.64 ?  479 TYR B CG    1 
ATOM   9384  C  CD1   . TYR B 1 479 ? 119.211 130.794 170.552 1.00 24.92 ?  479 TYR B CD1   1 
ATOM   9385  C  CD2   . TYR B 1 479 ? 121.021 132.120 171.353 1.00 25.29 ?  479 TYR B CD2   1 
ATOM   9386  C  CE1   . TYR B 1 479 ? 119.098 131.610 169.442 1.00 22.84 ?  479 TYR B CE1   1 
ATOM   9387  C  CE2   . TYR B 1 479 ? 120.918 132.939 170.246 1.00 22.12 ?  479 TYR B CE2   1 
ATOM   9388  C  CZ    . TYR B 1 479 ? 119.956 132.680 169.294 1.00 28.95 ?  479 TYR B CZ    1 
ATOM   9389  O  OH    . TYR B 1 479 ? 119.851 133.495 168.191 1.00 29.93 ?  479 TYR B OH    1 
ATOM   9390  N  N     . GLU B 1 480 ? 117.281 129.318 173.673 1.00 28.98 ?  480 GLU B N     1 
ATOM   9391  C  CA    . GLU B 1 480 ? 115.869 129.192 173.338 1.00 28.27 ?  480 GLU B CA    1 
ATOM   9392  C  C     . GLU B 1 480 ? 114.946 129.603 174.476 1.00 27.46 ?  480 GLU B C     1 
ATOM   9393  O  O     . GLU B 1 480 ? 113.728 129.665 174.271 1.00 33.76 ?  480 GLU B O     1 
ATOM   9394  C  CB    . GLU B 1 480 ? 115.545 127.752 172.933 1.00 30.32 ?  480 GLU B CB    1 
ATOM   9395  C  CG    . GLU B 1 480 ? 116.269 127.260 171.696 1.00 28.24 ?  480 GLU B CG    1 
ATOM   9396  C  CD    . GLU B 1 480 ? 116.098 125.769 171.493 1.00 36.35 ?  480 GLU B CD    1 
ATOM   9397  O  OE1   . GLU B 1 480 ? 114.980 125.341 171.138 1.00 36.92 ?  480 GLU B OE1   1 
ATOM   9398  O  OE2   . GLU B 1 480 ? 117.077 125.022 171.698 1.00 36.74 -1 480 GLU B OE2   1 
ATOM   9399  N  N     . SER B 1 481 ? 115.485 129.883 175.657 1.00 26.14 ?  481 SER B N     1 
ATOM   9400  C  CA    . SER B 1 481 ? 114.649 130.189 176.804 1.00 26.98 ?  481 SER B CA    1 
ATOM   9401  C  C     . SER B 1 481 ? 113.990 131.558 176.645 1.00 28.79 ?  481 SER B C     1 
ATOM   9402  O  O     . SER B 1 481 ? 114.512 132.431 175.945 1.00 29.80 ?  481 SER B O     1 
ATOM   9403  C  CB    . SER B 1 481 ? 115.476 130.160 178.086 1.00 28.32 ?  481 SER B CB    1 
ATOM   9404  O  OG    . SER B 1 481 ? 116.058 131.424 178.344 1.00 32.20 ?  481 SER B OG    1 
ATOM   9405  N  N     . PRO B 1 482 ? 112.829 131.764 177.271 1.00 36.02 ?  482 PRO B N     1 
ATOM   9406  C  CA    . PRO B 1 482 ? 112.236 133.110 177.279 1.00 32.05 ?  482 PRO B CA    1 
ATOM   9407  C  C     . PRO B 1 482 ? 113.114 134.147 177.955 1.00 31.69 ?  482 PRO B C     1 
ATOM   9408  O  O     . PRO B 1 482 ? 113.019 135.334 177.622 1.00 31.35 ?  482 PRO B O     1 
ATOM   9409  C  CB    . PRO B 1 482 ? 110.915 132.906 178.034 1.00 30.81 ?  482 PRO B CB    1 
ATOM   9410  C  CG    . PRO B 1 482 ? 110.618 131.453 177.901 1.00 31.49 ?  482 PRO B CG    1 
ATOM   9411  C  CD    . PRO B 1 482 ? 111.947 130.766 177.899 1.00 33.90 ?  482 PRO B CD    1 
ATOM   9412  N  N     . GLU B 1 483 ? 113.957 133.737 178.906 1.00 34.74 ?  483 GLU B N     1 
ATOM   9413  C  CA    . GLU B 1 483 ? 114.872 134.678 179.544 1.00 33.51 ?  483 GLU B CA    1 
ATOM   9414  C  C     . GLU B 1 483 ? 115.875 135.235 178.542 1.00 33.18 ?  483 GLU B C     1 
ATOM   9415  O  O     . GLU B 1 483 ? 116.222 136.421 178.594 1.00 38.65 ?  483 GLU B O     1 
ATOM   9416  C  CB    . GLU B 1 483 ? 115.595 134.001 180.706 1.00 36.12 ?  483 GLU B CB    1 
ATOM   9417  C  CG    . GLU B 1 483 ? 114.737 133.808 181.941 1.00 37.22 ?  483 GLU B CG    1 
ATOM   9418  C  CD    . GLU B 1 483 ? 114.106 132.432 182.000 1.00 41.25 ?  483 GLU B CD    1 
ATOM   9419  O  OE1   . GLU B 1 483 ? 113.706 131.913 180.937 1.00 39.62 ?  483 GLU B OE1   1 
ATOM   9420  O  OE2   . GLU B 1 483 ? 114.009 131.869 183.111 1.00 40.92 -1 483 GLU B OE2   1 
ATOM   9421  N  N     . ALA B 1 484 ? 116.360 134.390 177.631 1.00 26.92 ?  484 ALA B N     1 
ATOM   9422  C  CA    . ALA B 1 484 ? 117.274 134.860 176.597 1.00 25.36 ?  484 ALA B CA    1 
ATOM   9423  C  C     . ALA B 1 484 ? 116.598 135.870 175.679 1.00 27.63 ?  484 ALA B C     1 
ATOM   9424  O  O     . ALA B 1 484 ? 117.203 136.881 175.303 1.00 27.44 ?  484 ALA B O     1 
ATOM   9425  C  CB    . ALA B 1 484 ? 117.805 133.674 175.796 1.00 24.44 ?  484 ALA B CB    1 
ATOM   9426  N  N     . ARG B 1 485 ? 115.344 135.612 175.300 1.00 29.59 ?  485 ARG B N     1 
ATOM   9427  C  CA    . ARG B 1 485 ? 114.619 136.566 174.469 1.00 22.93 ?  485 ARG B CA    1 
ATOM   9428  C  C     . ARG B 1 485 ? 114.347 137.865 175.217 1.00 23.94 ?  485 ARG B C     1 
ATOM   9429  O  O     . ARG B 1 485 ? 114.386 138.942 174.617 1.00 33.77 ?  485 ARG B O     1 
ATOM   9430  C  CB    . ARG B 1 485 ? 113.313 135.950 173.974 1.00 28.90 ?  485 ARG B CB    1 
ATOM   9431  C  CG    . ARG B 1 485 ? 113.509 134.816 172.984 1.00 27.03 ?  485 ARG B CG    1 
ATOM   9432  C  CD    . ARG B 1 485 ? 112.195 134.404 172.351 1.00 27.04 ?  485 ARG B CD    1 
ATOM   9433  N  NE    . ARG B 1 485 ? 111.206 134.005 173.345 1.00 27.22 ?  485 ARG B NE    1 
ATOM   9434  C  CZ    . ARG B 1 485 ? 111.073 132.773 173.817 1.00 27.87 ?  485 ARG B CZ    1 
ATOM   9435  N  NH1   . ARG B 1 485 ? 111.862 131.790 173.415 1.00 25.07 1  485 ARG B NH1   1 
ATOM   9436  N  NH2   . ARG B 1 485 ? 110.124 132.522 174.713 1.00 30.16 ?  485 ARG B NH2   1 
ATOM   9437  N  N     . ASP B 1 486 ? 114.078 137.782 176.522 1.00 30.99 ?  486 ASP B N     1 
ATOM   9438  C  CA    . ASP B 1 486 ? 113.924 138.988 177.330 1.00 27.43 ?  486 ASP B CA    1 
ATOM   9439  C  C     . ASP B 1 486 ? 115.215 139.797 177.363 1.00 26.61 ?  486 ASP B C     1 
ATOM   9440  O  O     . ASP B 1 486 ? 115.194 141.030 177.229 1.00 33.37 ?  486 ASP B O     1 
ATOM   9441  C  CB    . ASP B 1 486 ? 113.490 138.602 178.743 1.00 32.56 ?  486 ASP B CB    1 
ATOM   9442  C  CG    . ASP B 1 486 ? 113.163 139.801 179.603 1.00 40.37 ?  486 ASP B CG    1 
ATOM   9443  O  OD1   . ASP B 1 486 ? 112.367 140.654 179.163 1.00 37.86 ?  486 ASP B OD1   1 
ATOM   9444  O  OD2   . ASP B 1 486 ? 113.703 139.880 180.725 1.00 37.16 -1 486 ASP B OD2   1 
ATOM   9445  N  N     . PHE B 1 487 ? 116.350 139.117 177.535 1.00 25.12 ?  487 PHE B N     1 
ATOM   9446  C  CA    . PHE B 1 487 ? 117.632 139.811 177.510 1.00 24.05 ?  487 PHE B CA    1 
ATOM   9447  C  C     . PHE B 1 487 ? 117.872 140.466 176.159 1.00 23.70 ?  487 PHE B C     1 
ATOM   9448  O  O     . PHE B 1 487 ? 118.347 141.602 176.088 1.00 29.55 ?  487 PHE B O     1 
ATOM   9449  C  CB    . PHE B 1 487 ? 118.780 138.857 177.827 1.00 25.33 ?  487 PHE B CB    1 
ATOM   9450  C  CG    . PHE B 1 487 ? 120.116 139.394 177.409 1.00 27.57 ?  487 PHE B CG    1 
ATOM   9451  C  CD1   . PHE B 1 487 ? 120.741 140.372 178.159 1.00 22.50 ?  487 PHE B CD1   1 
ATOM   9452  C  CD2   . PHE B 1 487 ? 120.725 138.957 176.244 1.00 29.01 ?  487 PHE B CD2   1 
ATOM   9453  C  CE1   . PHE B 1 487 ? 121.955 140.890 177.772 1.00 24.30 ?  487 PHE B CE1   1 
ATOM   9454  C  CE2   . PHE B 1 487 ? 121.941 139.474 175.852 1.00 25.24 ?  487 PHE B CE2   1 
ATOM   9455  C  CZ    . PHE B 1 487 ? 122.556 140.442 176.618 1.00 27.43 ?  487 PHE B CZ    1 
ATOM   9456  N  N     . ALA B 1 488 ? 117.586 139.746 175.074 1.00 24.45 ?  488 ALA B N     1 
ATOM   9457  C  CA    . ALA B 1 488 ? 117.782 140.314 173.745 1.00 19.89 ?  488 ALA B CA    1 
ATOM   9458  C  C     . ALA B 1 488 ? 116.894 141.532 173.542 1.00 26.39 ?  488 ALA B C     1 
ATOM   9459  O  O     . ALA B 1 488 ? 117.344 142.559 173.024 1.00 31.88 ?  488 ALA B O     1 
ATOM   9460  C  CB    . ALA B 1 488 ? 117.507 139.261 172.674 1.00 20.17 ?  488 ALA B CB    1 
ATOM   9461  N  N     . ASN B 1 489 ? 115.634 141.442 173.971 1.00 25.22 ?  489 ASN B N     1 
ATOM   9462  C  CA    . ASN B 1 489 ? 114.719 142.571 173.873 1.00 24.36 ?  489 ASN B CA    1 
ATOM   9463  C  C     . ASN B 1 489 ? 115.281 143.791 174.585 1.00 23.95 ?  489 ASN B C     1 
ATOM   9464  O  O     . ASN B 1 489 ? 115.390 144.873 173.997 1.00 24.39 ?  489 ASN B O     1 
ATOM   9465  C  CB    . ASN B 1 489 ? 113.361 142.183 174.459 1.00 21.91 ?  489 ASN B CB    1 
ATOM   9466  C  CG    . ASN B 1 489 ? 112.290 143.210 174.181 1.00 27.14 ?  489 ASN B CG    1 
ATOM   9467  O  OD1   . ASN B 1 489 ? 112.161 143.702 173.062 1.00 33.77 ?  489 ASN B OD1   1 
ATOM   9468  N  ND2   . ASN B 1 489 ? 111.507 143.537 175.201 1.00 30.58 ?  489 ASN B ND2   1 
ATOM   9469  N  N     . THR B 1 490 ? 115.675 143.627 175.850 1.00 27.27 ?  490 THR B N     1 
ATOM   9470  C  CA    . THR B 1 490 ? 116.166 144.769 176.616 1.00 22.97 ?  490 THR B CA    1 
ATOM   9471  C  C     . THR B 1 490 ? 117.467 145.313 176.035 1.00 24.75 ?  490 THR B C     1 
ATOM   9472  O  O     . THR B 1 490 ? 117.616 146.528 175.849 1.00 25.78 ?  490 THR B O     1 
ATOM   9473  C  CB    . THR B 1 490 ? 116.356 144.380 178.081 1.00 28.98 ?  490 THR B CB    1 
ATOM   9474  O  OG1   . THR B 1 490 ? 115.133 143.839 178.595 1.00 32.64 ?  490 THR B OG1   1 
ATOM   9475  C  CG2   . THR B 1 490 ? 116.756 145.595 178.899 1.00 26.06 ?  490 THR B CG2   1 
ATOM   9476  N  N     . PHE B 1 491 ? 118.418 144.426 175.733 1.00 24.63 ?  491 PHE B N     1 
ATOM   9477  C  CA    . PHE B 1 491 ? 119.726 144.860 175.257 1.00 19.07 ?  491 PHE B CA    1 
ATOM   9478  C  C     . PHE B 1 491 ? 119.616 145.592 173.928 1.00 19.39 ?  491 PHE B C     1 
ATOM   9479  O  O     . PHE B 1 491 ? 120.240 146.642 173.738 1.00 28.67 ?  491 PHE B O     1 
ATOM   9480  C  CB    . PHE B 1 491 ? 120.659 143.655 175.129 1.00 25.23 ?  491 PHE B CB    1 
ATOM   9481  C  CG    . PHE B 1 491 ? 121.980 143.973 174.484 1.00 23.98 ?  491 PHE B CG    1 
ATOM   9482  C  CD1   . PHE B 1 491 ? 123.036 144.443 175.243 1.00 19.94 ?  491 PHE B CD1   1 
ATOM   9483  C  CD2   . PHE B 1 491 ? 122.168 143.796 173.123 1.00 19.44 ?  491 PHE B CD2   1 
ATOM   9484  C  CE1   . PHE B 1 491 ? 124.251 144.737 174.659 1.00 16.87 ?  491 PHE B CE1   1 
ATOM   9485  C  CE2   . PHE B 1 491 ? 123.377 144.092 172.534 1.00 17.20 ?  491 PHE B CE2   1 
ATOM   9486  C  CZ    . PHE B 1 491 ? 124.421 144.563 173.304 1.00 23.78 ?  491 PHE B CZ    1 
ATOM   9487  N  N     . PHE B 1 492 ? 118.828 145.063 172.995 1.00 17.42 ?  492 PHE B N     1 
ATOM   9488  C  CA    . PHE B 1 492 ? 118.726 145.702 171.696 1.00 12.24 ?  492 PHE B CA    1 
ATOM   9489  C  C     . PHE B 1 492 ? 117.812 146.917 171.713 1.00 13.03 ?  492 PHE B C     1 
ATOM   9490  O  O     . PHE B 1 492 ? 118.002 147.819 170.894 1.00 24.31 ?  492 PHE B O     1 
ATOM   9491  C  CB    . PHE B 1 492 ? 118.280 144.679 170.654 1.00 17.91 ?  492 PHE B CB    1 
ATOM   9492  C  CG    . PHE B 1 492 ? 119.369 143.718 170.272 1.00 20.42 ?  492 PHE B CG    1 
ATOM   9493  C  CD1   . PHE B 1 492 ? 120.399 144.115 169.439 1.00 14.94 ?  492 PHE B CD1   1 
ATOM   9494  C  CD2   . PHE B 1 492 ? 119.385 142.431 170.778 1.00 19.18 ?  492 PHE B CD2   1 
ATOM   9495  C  CE1   . PHE B 1 492 ? 121.410 143.240 169.100 1.00 10.03 ?  492 PHE B CE1   1 
ATOM   9496  C  CE2   . PHE B 1 492 ? 120.393 141.551 170.444 1.00 15.06 ?  492 PHE B CE2   1 
ATOM   9497  C  CZ    . PHE B 1 492 ? 121.406 141.956 169.602 1.00 15.00 ?  492 PHE B CZ    1 
ATOM   9498  N  N     . MET B 1 493 ? 116.864 147.000 172.652 1.00 16.96 ?  493 MET B N     1 
ATOM   9499  C  CA    . MET B 1 493 ? 116.169 148.266 172.854 1.00 17.53 ?  493 MET B CA    1 
ATOM   9500  C  C     . MET B 1 493 ? 117.133 149.332 173.360 1.00 17.63 ?  493 MET B C     1 
ATOM   9501  O  O     . MET B 1 493 ? 117.073 150.483 172.921 1.00 26.01 ?  493 MET B O     1 
ATOM   9502  C  CB    . MET B 1 493 ? 114.992 148.074 173.815 1.00 17.60 ?  493 MET B CB    1 
ATOM   9503  C  CG    . MET B 1 493 ? 114.362 149.357 174.364 1.00 20.72 ?  493 MET B CG    1 
ATOM   9504  S  SD    . MET B 1 493 ? 115.207 150.100 175.776 1.00 30.63 ?  493 MET B SD    1 
ATOM   9505  C  CE    . MET B 1 493 ? 115.191 148.730 176.924 1.00 24.03 ?  493 MET B CE    1 
ATOM   9506  N  N     . MET B 1 494 ? 118.030 148.965 174.280 1.00 21.86 ?  494 MET B N     1 
ATOM   9507  C  CA    . MET B 1 494 ? 119.059 149.901 174.730 1.00 16.39 ?  494 MET B CA    1 
ATOM   9508  C  C     . MET B 1 494 ? 119.967 150.322 173.581 1.00 19.03 ?  494 MET B C     1 
ATOM   9509  O  O     . MET B 1 494 ? 120.307 151.506 173.445 1.00 22.87 ?  494 MET B O     1 
ATOM   9510  C  CB    . MET B 1 494 ? 119.889 149.273 175.850 1.00 20.19 ?  494 MET B CB    1 
ATOM   9511  C  CG    . MET B 1 494 ? 119.125 148.965 177.123 1.00 20.19 ?  494 MET B CG    1 
ATOM   9512  S  SD    . MET B 1 494 ? 120.230 148.815 178.539 1.00 37.53 ?  494 MET B SD    1 
ATOM   9513  C  CE    . MET B 1 494 ? 120.649 150.527 178.834 1.00 30.33 ?  494 MET B CE    1 
ATOM   9514  N  N     . VAL B 1 495 ? 120.377 149.361 172.752 1.00 19.01 ?  495 VAL B N     1 
ATOM   9515  C  CA    . VAL B 1 495 ? 121.238 149.668 171.615 1.00 17.66 ?  495 VAL B CA    1 
ATOM   9516  C  C     . VAL B 1 495 ? 120.535 150.616 170.653 1.00 17.55 ?  495 VAL B C     1 
ATOM   9517  O  O     . VAL B 1 495 ? 121.127 151.591 170.183 1.00 28.72 ?  495 VAL B O     1 
ATOM   9518  C  CB    . VAL B 1 495 ? 121.681 148.371 170.912 1.00 15.28 ?  495 VAL B CB    1 
ATOM   9519  C  CG1   . VAL B 1 495 ? 122.341 148.684 169.580 1.00 10.14 ?  495 VAL B CG1   1 
ATOM   9520  C  CG2   . VAL B 1 495 ? 122.627 147.586 171.799 1.00 19.24 ?  495 VAL B CG2   1 
ATOM   9521  N  N     . ASN B 1 496 ? 119.262 150.348 170.350 1.00 19.18 ?  496 ASN B N     1 
ATOM   9522  C  CA    . ASN B 1 496 ? 118.505 151.229 169.468 1.00 12.13 ?  496 ASN B CA    1 
ATOM   9523  C  C     . ASN B 1 496 ? 118.344 152.615 170.073 1.00 19.26 ?  496 ASN B C     1 
ATOM   9524  O  O     . ASN B 1 496 ? 118.479 153.626 169.374 1.00 30.91 ?  496 ASN B O     1 
ATOM   9525  C  CB    . ASN B 1 496 ? 117.139 150.617 169.163 1.00 16.23 ?  496 ASN B CB    1 
ATOM   9526  C  CG    . ASN B 1 496 ? 116.480 151.238 167.952 1.00 16.08 ?  496 ASN B CG    1 
ATOM   9527  O  OD1   . ASN B 1 496 ? 117.155 151.701 167.033 1.00 24.74 ?  496 ASN B OD1   1 
ATOM   9528  N  ND2   . ASN B 1 496 ? 115.154 151.256 167.943 1.00 15.35 ?  496 ASN B ND2   1 
ATOM   9529  N  N     . PHE B 1 497 ? 118.055 152.684 171.374 1.00 20.27 ?  497 PHE B N     1 
ATOM   9530  C  CA    . PHE B 1 497 ? 117.886 153.971 172.039 1.00 15.60 ?  497 PHE B CA    1 
ATOM   9531  C  C     . PHE B 1 497 ? 119.154 154.803 171.940 1.00 19.24 ?  497 PHE B C     1 
ATOM   9532  O  O     . PHE B 1 497 ? 119.115 155.977 171.557 1.00 26.32 ?  497 PHE B O     1 
ATOM   9533  C  CB    . PHE B 1 497 ? 117.500 153.747 173.503 1.00 17.84 ?  497 PHE B CB    1 
ATOM   9534  C  CG    . PHE B 1 497 ? 117.352 155.013 174.299 1.00 20.97 ?  497 PHE B CG    1 
ATOM   9535  C  CD1   . PHE B 1 497 ? 118.437 155.563 174.963 1.00 21.66 ?  497 PHE B CD1   1 
ATOM   9536  C  CD2   . PHE B 1 497 ? 116.126 155.645 174.394 1.00 21.23 ?  497 PHE B CD2   1 
ATOM   9537  C  CE1   . PHE B 1 497 ? 118.300 156.725 175.695 1.00 22.63 ?  497 PHE B CE1   1 
ATOM   9538  C  CE2   . PHE B 1 497 ? 115.984 156.807 175.126 1.00 20.87 ?  497 PHE B CE2   1 
ATOM   9539  C  CZ    . PHE B 1 497 ? 117.073 157.345 175.777 1.00 23.33 ?  497 PHE B CZ    1 
ATOM   9540  N  N     . TYR B 1 498 ? 120.298 154.203 172.267 1.00 26.89 ?  498 TYR B N     1 
ATOM   9541  C  CA    . TYR B 1 498 ? 121.535 154.970 172.266 1.00 18.43 ?  498 TYR B CA    1 
ATOM   9542  C  C     . TYR B 1 498 ? 122.035 155.245 170.854 1.00 18.27 ?  498 TYR B C     1 
ATOM   9543  O  O     . TYR B 1 498 ? 122.673 156.276 170.625 1.00 26.71 ?  498 TYR B O     1 
ATOM   9544  C  CB    . TYR B 1 498 ? 122.590 154.255 173.108 1.00 18.97 ?  498 TYR B CB    1 
ATOM   9545  C  CG    . TYR B 1 498 ? 122.272 154.327 174.583 1.00 22.61 ?  498 TYR B CG    1 
ATOM   9546  C  CD1   . TYR B 1 498 ? 122.116 155.554 175.214 1.00 23.34 ?  498 TYR B CD1   1 
ATOM   9547  C  CD2   . TYR B 1 498 ? 122.102 153.175 175.338 1.00 26.29 ?  498 TYR B CD2   1 
ATOM   9548  C  CE1   . TYR B 1 498 ? 121.812 155.632 176.557 1.00 24.09 ?  498 TYR B CE1   1 
ATOM   9549  C  CE2   . TYR B 1 498 ? 121.799 153.244 176.683 1.00 25.24 ?  498 TYR B CE2   1 
ATOM   9550  C  CZ    . TYR B 1 498 ? 121.655 154.475 177.287 1.00 29.24 ?  498 TYR B CZ    1 
ATOM   9551  O  OH    . TYR B 1 498 ? 121.356 154.552 178.627 1.00 35.73 ?  498 TYR B OH    1 
ATOM   9552  N  N     . SER B 1 499 ? 121.722 154.376 169.890 1.00 19.26 ?  499 SER B N     1 
ATOM   9553  C  CA    . SER B 1 499 ? 122.057 154.667 168.502 1.00 13.36 ?  499 SER B CA    1 
ATOM   9554  C  C     . SER B 1 499 ? 121.242 155.842 167.974 1.00 18.33 ?  499 SER B C     1 
ATOM   9555  O  O     . SER B 1 499 ? 121.781 156.719 167.293 1.00 20.27 ?  499 SER B O     1 
ATOM   9556  C  CB    . SER B 1 499 ? 121.838 153.426 167.638 1.00 14.93 ?  499 SER B CB    1 
ATOM   9557  O  OG    . SER B 1 499 ? 122.514 153.541 166.400 1.00 19.27 ?  499 SER B OG    1 
ATOM   9558  N  N     . ILE B 1 500 ? 119.944 155.879 168.289 1.00 18.14 ?  500 ILE B N     1 
ATOM   9559  C  CA    . ILE B 1 500 ? 119.114 157.013 167.894 1.00 20.90 ?  500 ILE B CA    1 
ATOM   9560  C  C     . ILE B 1 500 ? 119.592 158.283 168.582 1.00 19.50 ?  500 ILE B C     1 
ATOM   9561  O  O     . ILE B 1 500 ? 119.637 159.358 167.973 1.00 26.97 ?  500 ILE B O     1 
ATOM   9562  C  CB    . ILE B 1 500 ? 117.633 156.727 168.203 1.00 23.62 ?  500 ILE B CB    1 
ATOM   9563  C  CG1   . ILE B 1 500 ? 117.105 155.604 167.314 1.00 18.38 ?  500 ILE B CG1   1 
ATOM   9564  C  CG2   . ILE B 1 500 ? 116.789 157.974 168.016 1.00 18.21 ?  500 ILE B CG2   1 
ATOM   9565  C  CD1   . ILE B 1 500 ? 115.798 155.038 167.785 1.00 22.35 ?  500 ILE B CD1   1 
ATOM   9566  N  N     . GLN B 1 501 ? 119.955 158.180 169.863 1.00 20.82 ?  501 GLN B N     1 
ATOM   9567  C  CA    . GLN B 1 501 ? 120.453 159.345 170.584 1.00 22.83 ?  501 GLN B CA    1 
ATOM   9568  C  C     . GLN B 1 501 ? 121.740 159.871 169.962 1.00 24.83 ?  501 GLN B C     1 
ATOM   9569  O  O     . GLN B 1 501 ? 121.893 161.082 169.776 1.00 30.68 ?  501 GLN B O     1 
ATOM   9570  C  CB    . GLN B 1 501 ? 120.669 158.995 172.055 1.00 27.35 ?  501 GLN B CB    1 
ATOM   9571  C  CG    . GLN B 1 501 ? 120.592 160.189 172.989 1.00 24.19 ?  501 GLN B CG    1 
ATOM   9572  C  CD    . GLN B 1 501 ? 120.533 159.782 174.445 1.00 28.90 ?  501 GLN B CD    1 
ATOM   9573  O  OE1   . GLN B 1 501 ? 121.338 158.978 174.911 1.00 34.53 ?  501 GLN B OE1   1 
ATOM   9574  N  NE2   . GLN B 1 501 ? 119.572 160.336 175.174 1.00 31.97 ?  501 GLN B NE2   1 
ATOM   9575  N  N     . ARG B 1 502 ? 122.672 158.977 169.625 1.00 23.90 ?  502 ARG B N     1 
ATOM   9576  C  CA    . ARG B 1 502 ? 123.913 159.411 168.994 1.00 20.10 ?  502 ARG B CA    1 
ATOM   9577  C  C     . ARG B 1 502 ? 123.662 159.996 167.610 1.00 22.90 ?  502 ARG B C     1 
ATOM   9578  O  O     . ARG B 1 502 ? 124.300 160.979 167.227 1.00 30.30 ?  502 ARG B O     1 
ATOM   9579  C  CB    . ARG B 1 502 ? 124.902 158.250 168.910 1.00 23.30 ?  502 ARG B CB    1 
ATOM   9580  C  CG    . ARG B 1 502 ? 126.316 158.692 168.577 1.00 26.41 ?  502 ARG B CG    1 
ATOM   9581  C  CD    . ARG B 1 502 ? 126.749 159.845 169.465 1.00 26.01 ?  502 ARG B CD    1 
ATOM   9582  N  NE    . ARG B 1 502 ? 127.974 160.473 168.986 1.00 24.91 ?  502 ARG B NE    1 
ATOM   9583  C  CZ    . ARG B 1 502 ? 128.230 161.771 169.068 1.00 23.93 ?  502 ARG B CZ    1 
ATOM   9584  N  NH1   . ARG B 1 502 ? 127.370 162.613 169.616 1.00 30.63 1  502 ARG B NH1   1 
ATOM   9585  N  NH2   . ARG B 1 502 ? 129.379 162.236 168.587 1.00 28.82 ?  502 ARG B NH2   1 
ATOM   9586  N  N     . SER B 1 503 ? 122.747 159.401 166.841 1.00 23.38 ?  503 SER B N     1 
ATOM   9587  C  CA    . SER B 1 503 ? 122.431 159.941 165.524 1.00 22.11 ?  503 SER B CA    1 
ATOM   9588  C  C     . SER B 1 503 ? 121.851 161.345 165.635 1.00 23.05 ?  503 SER B C     1 
ATOM   9589  O  O     . SER B 1 503 ? 122.232 162.248 164.881 1.00 28.92 ?  503 SER B O     1 
ATOM   9590  C  CB    . SER B 1 503 ? 121.461 159.009 164.799 1.00 18.74 ?  503 SER B CB    1 
ATOM   9591  O  OG    . SER B 1 503 ? 121.558 159.154 163.395 1.00 24.69 ?  503 SER B OG    1 
ATOM   9592  N  N     . ALA B 1 504 ? 120.943 161.552 166.591 1.00 23.24 ?  504 ALA B N     1 
ATOM   9593  C  CA    . ALA B 1 504 ? 120.369 162.877 166.795 1.00 25.89 ?  504 ALA B CA    1 
ATOM   9594  C  C     . ALA B 1 504 ? 121.415 163.866 167.295 1.00 27.48 ?  504 ALA B C     1 
ATOM   9595  O  O     . ALA B 1 504 ? 121.402 165.038 166.906 1.00 34.08 ?  504 ALA B O     1 
ATOM   9596  C  CB    . ALA B 1 504 ? 119.194 162.791 167.768 1.00 26.38 ?  504 ALA B CB    1 
ATOM   9597  N  N     . GLU B 1 505 ? 122.333 163.413 168.153 1.00 25.13 ?  505 GLU B N     1 
ATOM   9598  C  CA    . GLU B 1 505 ? 123.392 164.293 168.639 1.00 25.65 ?  505 GLU B CA    1 
ATOM   9599  C  C     . GLU B 1 505 ? 124.339 164.694 167.516 1.00 26.97 ?  505 GLU B C     1 
ATOM   9600  O  O     . GLU B 1 505 ? 124.786 165.845 167.457 1.00 31.65 ?  505 GLU B O     1 
ATOM   9601  C  CB    . GLU B 1 505 ? 124.158 163.613 169.772 1.00 26.13 ?  505 GLU B CB    1 
ATOM   9602  C  CG    . GLU B 1 505 ? 123.406 163.572 171.090 1.00 27.47 ?  505 GLU B CG    1 
ATOM   9603  C  CD    . GLU B 1 505 ? 123.933 162.505 172.025 1.00 32.39 ?  505 GLU B CD    1 
ATOM   9604  O  OE1   . GLU B 1 505 ? 124.933 161.847 171.671 1.00 31.08 ?  505 GLU B OE1   1 
ATOM   9605  O  OE2   . GLU B 1 505 ? 123.350 162.324 173.114 1.00 34.66 -1 505 GLU B OE2   1 
ATOM   9606  N  N     . ILE B 1 506 ? 124.666 163.759 166.624 1.00 26.20 ?  506 ILE B N     1 
ATOM   9607  C  CA    . ILE B 1 506 ? 125.495 164.086 165.468 1.00 26.19 ?  506 ILE B CA    1 
ATOM   9608  C  C     . ILE B 1 506 ? 124.767 165.059 164.550 1.00 26.67 ?  506 ILE B C     1 
ATOM   9609  O  O     . ILE B 1 506 ? 125.366 166.004 164.024 1.00 33.16 ?  506 ILE B O     1 
ATOM   9610  C  CB    . ILE B 1 506 ? 125.913 162.804 164.725 1.00 25.49 ?  506 ILE B CB    1 
ATOM   9611  C  CG1   . ILE B 1 506 ? 126.798 161.934 165.617 1.00 28.34 ?  506 ILE B CG1   1 
ATOM   9612  C  CG2   . ILE B 1 506 ? 126.644 163.140 163.440 1.00 24.77 ?  506 ILE B CG2   1 
ATOM   9613  C  CD1   . ILE B 1 506 ? 127.012 160.537 165.085 1.00 21.69 ?  506 ILE B CD1   1 
ATOM   9614  N  N     . ALA B 1 507 ? 123.465 164.848 164.342 1.00 26.64 ?  507 ALA B N     1 
ATOM   9615  C  CA    . ALA B 1 507 ? 122.687 165.778 163.531 1.00 28.48 ?  507 ALA B CA    1 
ATOM   9616  C  C     . ALA B 1 507 ? 122.673 167.171 164.149 1.00 32.25 ?  507 ALA B C     1 
ATOM   9617  O  O     . ALA B 1 507 ? 122.746 168.178 163.436 1.00 36.65 ?  507 ALA B O     1 
ATOM   9618  C  CB    . ALA B 1 507 ? 121.262 165.254 163.355 1.00 24.25 ?  507 ALA B CB    1 
ATOM   9619  N  N     . LYS B 1 508 ? 122.572 167.245 165.477 1.00 32.69 ?  508 LYS B N     1 
ATOM   9620  C  CA    . LYS B 1 508 ? 122.596 168.533 166.162 1.00 30.69 ?  508 LYS B CA    1 
ATOM   9621  C  C     . LYS B 1 508 ? 123.961 169.203 166.047 1.00 36.95 ?  508 LYS B C     1 
ATOM   9622  O  O     . LYS B 1 508 ? 124.047 170.409 165.790 1.00 43.58 ?  508 LYS B O     1 
ATOM   9623  C  CB    . LYS B 1 508 ? 122.215 168.340 167.630 1.00 34.62 ?  508 LYS B CB    1 
ATOM   9624  C  CG    . LYS B 1 508 ? 122.328 169.590 168.483 1.00 35.60 ?  508 LYS B CG    1 
ATOM   9625  C  CD    . LYS B 1 508 ? 122.207 169.248 169.959 1.00 34.74 ?  508 LYS B CD    1 
ATOM   9626  C  CE    . LYS B 1 508 ? 122.015 170.493 170.806 1.00 36.44 ?  508 LYS B CE    1 
ATOM   9627  N  NZ    . LYS B 1 508 ? 121.221 170.209 172.033 1.00 38.05 1  508 LYS B NZ    1 
ATOM   9628  N  N     . GLU B 1 509 ? 125.037 168.435 166.234 1.00 34.40 ?  509 GLU B N     1 
ATOM   9629  C  CA    . GLU B 1 509 ? 126.376 169.015 166.226 1.00 35.15 ?  509 GLU B CA    1 
ATOM   9630  C  C     . GLU B 1 509 ? 126.816 169.409 164.823 1.00 36.28 ?  509 GLU B C     1 
ATOM   9631  O  O     . GLU B 1 509 ? 127.643 170.314 164.666 1.00 39.64 ?  509 GLU B O     1 
ATOM   9632  C  CB    . GLU B 1 509 ? 127.371 168.036 166.854 1.00 35.08 ?  509 GLU B CB    1 
ATOM   9633  C  CG    . GLU B 1 509 ? 128.169 167.210 165.859 1.00 32.91 ?  509 GLU B CG    1 
ATOM   9634  C  CD    . GLU B 1 509 ? 128.761 165.960 166.482 1.00 41.57 ?  509 GLU B CD    1 
ATOM   9635  O  OE1   . GLU B 1 509 ? 128.701 165.825 167.722 1.00 40.77 ?  509 GLU B OE1   1 
ATOM   9636  O  OE2   . GLU B 1 509 ? 129.285 165.111 165.730 1.00 40.46 -1 509 GLU B OE2   1 
ATOM   9637  N  N     . LYS B 1 510 ? 126.283 168.750 163.795 1.00 32.33 ?  510 LYS B N     1 
ATOM   9638  C  CA    . LYS B 1 510 ? 126.607 169.082 162.416 1.00 31.26 ?  510 LYS B CA    1 
ATOM   9639  C  C     . LYS B 1 510 ? 125.543 169.936 161.741 1.00 35.37 ?  510 LYS B C     1 
ATOM   9640  O  O     . LYS B 1 510 ? 125.780 170.428 160.633 1.00 39.87 ?  510 LYS B O     1 
ATOM   9641  C  CB    . LYS B 1 510 ? 126.825 167.802 161.599 1.00 30.84 ?  510 LYS B CB    1 
ATOM   9642  C  CG    . LYS B 1 510 ? 127.882 166.881 162.176 1.00 32.21 ?  510 LYS B CG    1 
ATOM   9643  C  CD    . LYS B 1 510 ? 128.333 165.847 161.162 1.00 31.73 ?  510 LYS B CD    1 
ATOM   9644  C  CE    . LYS B 1 510 ? 129.477 165.009 161.707 1.00 33.69 ?  510 LYS B CE    1 
ATOM   9645  N  NZ    . LYS B 1 510 ? 130.451 164.642 160.645 1.00 32.53 1  510 LYS B NZ    1 
ATOM   9646  N  N     . GLY B 1 511 ? 124.389 170.124 162.377 1.00 32.71 ?  511 GLY B N     1 
ATOM   9647  C  CA    . GLY B 1 511 ? 123.328 170.918 161.793 1.00 32.43 ?  511 GLY B CA    1 
ATOM   9648  C  C     . GLY B 1 511 ? 122.689 170.326 160.560 1.00 36.03 ?  511 GLY B C     1 
ATOM   9649  O  O     . GLY B 1 511 ? 121.957 171.032 159.861 1.00 39.42 ?  511 GLY B O     1 
ATOM   9650  N  N     . GLU B 1 512 ? 122.940 169.052 160.268 1.00 33.04 ?  512 GLU B N     1 
ATOM   9651  C  CA    . GLU B 1 512 ? 122.410 168.404 159.078 1.00 29.38 ?  512 GLU B CA    1 
ATOM   9652  C  C     . GLU B 1 512 ? 121.879 167.024 159.427 1.00 31.47 ?  512 GLU B C     1 
ATOM   9653  O  O     . GLU B 1 512 ? 122.445 166.322 160.271 1.00 32.91 ?  512 GLU B O     1 
ATOM   9654  C  CB    . GLU B 1 512 ? 123.480 168.288 157.983 1.00 31.29 ?  512 GLU B CB    1 
ATOM   9655  C  CG    . GLU B 1 512 ? 124.771 167.632 158.439 1.00 31.45 ?  512 GLU B CG    1 
ATOM   9656  C  CD    . GLU B 1 512 ? 125.540 167.002 157.294 1.00 36.04 ?  512 GLU B CD    1 
ATOM   9657  O  OE1   . GLU B 1 512 ? 124.897 166.520 156.340 1.00 32.30 ?  512 GLU B OE1   1 
ATOM   9658  O  OE2   . GLU B 1 512 ? 126.788 166.988 157.349 1.00 36.73 -1 512 GLU B OE2   1 
ATOM   9659  N  N     . THR B 1 513 ? 120.785 166.646 158.778 1.00 31.96 ?  513 THR B N     1 
ATOM   9660  C  CA    . THR B 1 513 ? 120.206 165.316 158.868 1.00 26.26 ?  513 THR B CA    1 
ATOM   9661  C  C     . THR B 1 513 ? 120.465 164.572 157.563 1.00 27.02 ?  513 THR B C     1 
ATOM   9662  O  O     . THR B 1 513 ? 121.073 165.102 156.630 1.00 34.08 ?  513 THR B O     1 
ATOM   9663  C  CB    . THR B 1 513 ? 118.708 165.400 159.171 1.00 27.27 ?  513 THR B CB    1 
ATOM   9664  O  OG1   . THR B 1 513 ? 118.037 166.048 158.084 1.00 29.20 ?  513 THR B OG1   1 
ATOM   9665  C  CG2   . THR B 1 513 ? 118.469 166.191 160.444 1.00 24.46 ?  513 THR B CG2   1 
ATOM   9666  N  N     . PHE B 1 514 ? 120.001 163.328 157.496 1.00 21.67 ?  514 PHE B N     1 
ATOM   9667  C  CA    . PHE B 1 514 ? 120.104 162.613 156.236 1.00 22.78 ?  514 PHE B CA    1 
ATOM   9668  C  C     . PHE B 1 514 ? 119.047 163.123 155.262 1.00 22.05 ?  514 PHE B C     1 
ATOM   9669  O  O     . PHE B 1 514 ? 118.034 163.706 155.655 1.00 26.25 ?  514 PHE B O     1 
ATOM   9670  C  CB    . PHE B 1 514 ? 119.977 161.100 156.442 1.00 19.13 ?  514 PHE B CB    1 
ATOM   9671  C  CG    . PHE B 1 514 ? 118.635 160.650 156.952 1.00 19.25 ?  514 PHE B CG    1 
ATOM   9672  C  CD1   . PHE B 1 514 ? 118.381 160.585 158.309 1.00 17.52 ?  514 PHE B CD1   1 
ATOM   9673  C  CD2   . PHE B 1 514 ? 117.640 160.259 156.071 1.00 19.76 ?  514 PHE B CD2   1 
ATOM   9674  C  CE1   . PHE B 1 514 ? 117.157 160.156 158.778 1.00 20.16 ?  514 PHE B CE1   1 
ATOM   9675  C  CE2   . PHE B 1 514 ? 116.414 159.831 156.534 1.00 14.93 ?  514 PHE B CE2   1 
ATOM   9676  C  CZ    . PHE B 1 514 ? 116.172 159.780 157.890 1.00 21.93 ?  514 PHE B CZ    1 
ATOM   9677  N  N     . ASP B 1 515 ? 119.306 162.910 153.975 1.00 25.10 ?  515 ASP B N     1 
ATOM   9678  C  CA    . ASP B 1 515 ? 118.430 163.447 152.944 1.00 26.53 ?  515 ASP B CA    1 
ATOM   9679  C  C     . ASP B 1 515 ? 117.030 162.860 153.062 1.00 31.04 ?  515 ASP B C     1 
ATOM   9680  O  O     . ASP B 1 515 ? 116.858 161.660 153.293 1.00 40.44 ?  515 ASP B O     1 
ATOM   9681  C  CB    . ASP B 1 515 ? 119.006 163.163 151.558 1.00 29.27 ?  515 ASP B CB    1 
ATOM   9682  C  CG    . ASP B 1 515 ? 119.955 164.247 151.091 1.00 33.63 ?  515 ASP B CG    1 
ATOM   9683  O  OD1   . ASP B 1 515 ? 120.417 165.040 151.938 1.00 32.53 ?  515 ASP B OD1   1 
ATOM   9684  O  OD2   . ASP B 1 515 ? 120.240 164.307 149.878 1.00 38.46 -1 515 ASP B OD2   1 
ATOM   9685  N  N     . GLN B 1 516 ? 116.028 163.727 152.908 1.00 28.92 ?  516 GLN B N     1 
ATOM   9686  C  CA    . GLN B 1 516 ? 114.617 163.352 153.003 1.00 26.49 ?  516 GLN B CA    1 
ATOM   9687  C  C     . GLN B 1 516 ? 114.268 162.794 154.380 1.00 27.05 ?  516 GLN B C     1 
ATOM   9688  O  O     . GLN B 1 516 ? 113.405 161.924 154.505 1.00 32.99 ?  516 GLN B O     1 
ATOM   9689  C  CB    . GLN B 1 516 ? 114.230 162.352 151.911 1.00 26.22 ?  516 GLN B CB    1 
ATOM   9690  C  CG    . GLN B 1 516 ? 114.469 162.838 150.496 1.00 29.62 ?  516 GLN B CG    1 
ATOM   9691  C  CD    . GLN B 1 516 ? 114.304 161.733 149.473 1.00 32.34 ?  516 GLN B CD    1 
ATOM   9692  O  OE1   . GLN B 1 516 ? 113.188 161.311 149.173 1.00 29.80 ?  516 GLN B OE1   1 
ATOM   9693  N  NE2   . GLN B 1 516 ? 115.419 161.254 148.933 1.00 32.48 ?  516 GLN B NE2   1 
ATOM   9694  N  N     . TYR B 1 517 ? 114.933 163.285 155.427 1.00 24.80 ?  517 TYR B N     1 
ATOM   9695  C  CA    . TYR B 1 517 ? 114.588 162.849 156.776 1.00 22.80 ?  517 TYR B CA    1 
ATOM   9696  C  C     . TYR B 1 517 ? 113.205 163.336 157.186 1.00 29.59 ?  517 TYR B C     1 
ATOM   9697  O  O     . TYR B 1 517 ? 112.529 162.680 157.988 1.00 35.82 ?  517 TYR B O     1 
ATOM   9698  C  CB    . TYR B 1 517 ? 115.639 163.333 157.778 1.00 18.52 ?  517 TYR B CB    1 
ATOM   9699  C  CG    . TYR B 1 517 ? 115.086 163.574 159.165 1.00 28.00 ?  517 TYR B CG    1 
ATOM   9700  C  CD1   . TYR B 1 517 ? 114.917 162.524 160.059 1.00 23.79 ?  517 TYR B CD1   1 
ATOM   9701  C  CD2   . TYR B 1 517 ? 114.725 164.851 159.579 1.00 29.52 ?  517 TYR B CD2   1 
ATOM   9702  C  CE1   . TYR B 1 517 ? 114.406 162.739 161.323 1.00 27.50 ?  517 TYR B CE1   1 
ATOM   9703  C  CE2   . TYR B 1 517 ? 114.212 165.073 160.838 1.00 24.93 ?  517 TYR B CE2   1 
ATOM   9704  C  CZ    . TYR B 1 517 ? 114.054 164.014 161.706 1.00 27.75 ?  517 TYR B CZ    1 
ATOM   9705  O  OH    . TYR B 1 517 ? 113.546 164.235 162.965 1.00 36.93 ?  517 TYR B OH    1 
ATOM   9706  N  N     . GLU B 1 518 ? 112.763 164.474 156.644 1.00 28.16 ?  518 GLU B N     1 
ATOM   9707  C  CA    . GLU B 1 518 ? 111.522 165.093 157.098 1.00 30.08 ?  518 GLU B CA    1 
ATOM   9708  C  C     . GLU B 1 518 ? 110.311 164.206 156.837 1.00 34.42 ?  518 GLU B C     1 
ATOM   9709  O  O     . GLU B 1 518 ? 109.339 164.249 157.600 1.00 35.10 ?  518 GLU B O     1 
ATOM   9710  C  CB    . GLU B 1 518 ? 111.336 166.453 156.425 1.00 29.58 ?  518 GLU B CB    1 
ATOM   9711  C  CG    . GLU B 1 518 ? 112.418 167.475 156.753 1.00 34.09 ?  518 GLU B CG    1 
ATOM   9712  C  CD    . GLU B 1 518 ? 113.698 167.253 155.966 1.00 41.01 ?  518 GLU B CD    1 
ATOM   9713  O  OE1   . GLU B 1 518 ? 113.615 166.770 154.817 1.00 38.63 ?  518 GLU B OE1   1 
ATOM   9714  O  OE2   . GLU B 1 518 ? 114.786 167.560 156.497 1.00 38.53 -1 518 GLU B OE2   1 
ATOM   9715  N  N     . GLY B 1 519 ? 110.342 163.407 155.776 1.00 23.98 ?  519 GLY B N     1 
ATOM   9716  C  CA    . GLY B 1 519 ? 109.270 162.480 155.491 1.00 20.26 ?  519 GLY B CA    1 
ATOM   9717  C  C     . GLY B 1 519 ? 109.361 161.153 156.202 1.00 19.74 ?  519 GLY B C     1 
ATOM   9718  O  O     . GLY B 1 519 ? 108.446 160.332 156.083 1.00 28.28 ?  519 GLY B O     1 
ATOM   9719  N  N     . SER B 1 520 ? 110.438 160.914 156.944 1.00 21.17 ?  520 SER B N     1 
ATOM   9720  C  CA    . SER B 1 520 ? 110.639 159.641 157.616 1.00 22.77 ?  520 SER B CA    1 
ATOM   9721  C  C     . SER B 1 520 ? 109.778 159.547 158.872 1.00 22.36 ?  520 SER B C     1 
ATOM   9722  O  O     . SER B 1 520 ? 109.256 160.542 159.382 1.00 24.18 ?  520 SER B O     1 
ATOM   9723  C  CB    . SER B 1 520 ? 112.112 159.451 157.977 1.00 18.69 ?  520 SER B CB    1 
ATOM   9724  O  OG    . SER B 1 520 ? 112.544 160.441 158.892 1.00 23.96 ?  520 SER B OG    1 
ATOM   9725  N  N     . THR B 1 521 ? 109.629 158.315 159.366 1.00 21.97 ?  521 THR B N     1 
ATOM   9726  C  CA    . THR B 1 521 ? 108.890 158.096 160.602 1.00 18.95 ?  521 THR B CA    1 
ATOM   9727  C  C     . THR B 1 521 ? 109.643 158.615 161.819 1.00 25.21 ?  521 THR B C     1 
ATOM   9728  O  O     . THR B 1 521 ? 109.035 158.788 162.880 1.00 26.86 ?  521 THR B O     1 
ATOM   9729  C  CB    . THR B 1 521 ? 108.576 156.610 160.775 1.00 24.09 ?  521 THR B CB    1 
ATOM   9730  O  OG1   . THR B 1 521 ? 109.772 155.902 161.121 1.00 29.44 ?  521 THR B OG1   1 
ATOM   9731  C  CG2   . THR B 1 521 ? 108.013 156.036 159.489 1.00 15.63 ?  521 THR B CG2   1 
ATOM   9732  N  N     . TYR B 1 522 ? 110.950 158.856 161.695 1.00 25.01 ?  522 TYR B N     1 
ATOM   9733  C  CA    . TYR B 1 522 ? 111.684 159.515 162.770 1.00 20.83 ?  522 TYR B CA    1 
ATOM   9734  C  C     . TYR B 1 522 ? 111.210 160.950 162.953 1.00 25.33 ?  522 TYR B C     1 
ATOM   9735  O  O     . TYR B 1 522 ? 111.052 161.421 164.085 1.00 24.25 ?  522 TYR B O     1 
ATOM   9736  C  CB    . TYR B 1 522 ? 113.184 159.488 162.481 1.00 18.01 ?  522 TYR B CB    1 
ATOM   9737  C  CG    . TYR B 1 522 ? 113.798 158.109 162.459 1.00 24.21 ?  522 TYR B CG    1 
ATOM   9738  C  CD1   . TYR B 1 522 ? 113.850 157.329 163.607 1.00 24.70 ?  522 TYR B CD1   1 
ATOM   9739  C  CD2   . TYR B 1 522 ? 114.342 157.592 161.292 1.00 22.12 ?  522 TYR B CD2   1 
ATOM   9740  C  CE1   . TYR B 1 522 ? 114.417 156.072 163.588 1.00 24.61 ?  522 TYR B CE1   1 
ATOM   9741  C  CE2   . TYR B 1 522 ? 114.911 156.336 161.265 1.00 20.99 ?  522 TYR B CE2   1 
ATOM   9742  C  CZ    . TYR B 1 522 ? 114.945 155.580 162.415 1.00 22.49 ?  522 TYR B CZ    1 
ATOM   9743  O  OH    . TYR B 1 522 ? 115.510 154.328 162.391 1.00 28.05 ?  522 TYR B OH    1 
ATOM   9744  N  N     . ALA B 1 523 ? 110.978 161.661 161.847 1.00 27.79 ?  523 ALA B N     1 
ATOM   9745  C  CA    . ALA B 1 523 ? 110.557 163.056 161.929 1.00 30.41 ?  523 ALA B CA    1 
ATOM   9746  C  C     . ALA B 1 523 ? 109.122 163.177 162.423 1.00 29.48 ?  523 ALA B C     1 
ATOM   9747  O  O     . ALA B 1 523 ? 108.803 164.080 163.205 1.00 28.29 ?  523 ALA B O     1 
ATOM   9748  C  CB    . ALA B 1 523 ? 110.716 163.731 160.569 1.00 27.66 ?  523 ALA B CB    1 
ATOM   9749  N  N     . THR B 1 524 ? 108.243 162.280 161.977 1.00 26.48 ?  524 THR B N     1 
ATOM   9750  C  CA    . THR B 1 524 ? 106.842 162.327 162.368 1.00 27.99 ?  524 THR B CA    1 
ATOM   9751  C  C     . THR B 1 524 ? 106.588 161.747 163.753 1.00 33.26 ?  524 THR B C     1 
ATOM   9752  O  O     . THR B 1 524 ? 105.484 161.919 164.283 1.00 38.05 ?  524 THR B O     1 
ATOM   9753  C  CB    . THR B 1 524 ? 105.981 161.583 161.342 1.00 28.49 ?  524 THR B CB    1 
ATOM   9754  O  OG1   . THR B 1 524 ? 106.257 160.180 161.411 1.00 32.57 ?  524 THR B OG1   1 
ATOM   9755  C  CG2   . THR B 1 524 ? 106.278 162.085 159.937 1.00 27.48 ?  524 THR B CG2   1 
ATOM   9756  N  N     . GLY B 1 525 ? 107.569 161.073 164.348 1.00 25.50 ?  525 GLY B N     1 
ATOM   9757  C  CA    . GLY B 1 525 ? 107.405 160.474 165.654 1.00 23.63 ?  525 GLY B CA    1 
ATOM   9758  C  C     . GLY B 1 525 ? 106.736 159.119 165.660 1.00 26.91 ?  525 GLY B C     1 
ATOM   9759  O  O     . GLY B 1 525 ? 106.576 158.532 166.737 1.00 31.03 ?  525 GLY B O     1 
ATOM   9760  N  N     . GLU B 1 526 ? 106.339 158.603 164.495 1.00 31.40 ?  526 GLU B N     1 
ATOM   9761  C  CA    . GLU B 1 526 ? 105.692 157.296 164.442 1.00 30.90 ?  526 GLU B CA    1 
ATOM   9762  C  C     . GLU B 1 526 ? 106.649 156.189 164.866 1.00 31.91 ?  526 GLU B C     1 
ATOM   9763  O  O     . GLU B 1 526 ? 106.245 155.230 165.535 1.00 36.63 ?  526 GLU B O     1 
ATOM   9764  C  CB    . GLU B 1 526 ? 105.154 157.043 163.033 1.00 29.22 ?  526 GLU B CB    1 
ATOM   9765  C  CG    . GLU B 1 526 ? 104.754 155.604 162.756 1.00 33.58 ?  526 GLU B CG    1 
ATOM   9766  C  CD    . GLU B 1 526 ? 104.614 155.316 161.275 1.00 39.33 ?  526 GLU B CD    1 
ATOM   9767  O  OE1   . GLU B 1 526 ? 104.079 156.179 160.548 1.00 39.85 ?  526 GLU B OE1   1 
ATOM   9768  O  OE2   . GLU B 1 526 ? 105.041 154.227 160.837 1.00 35.42 -1 526 GLU B OE2   1 
ATOM   9769  N  N     . TYR B 1 527 ? 107.929 156.315 164.497 1.00 33.11 ?  527 TYR B N     1 
ATOM   9770  C  CA    . TYR B 1 527 ? 108.911 155.279 164.802 1.00 22.71 ?  527 TYR B CA    1 
ATOM   9771  C  C     . TYR B 1 527 ? 108.974 154.984 166.295 1.00 25.58 ?  527 TYR B C     1 
ATOM   9772  O  O     . TYR B 1 527 ? 109.196 153.839 166.702 1.00 30.15 ?  527 TYR B O     1 
ATOM   9773  C  CB    . TYR B 1 527 ? 110.289 155.703 164.291 1.00 18.10 ?  527 TYR B CB    1 
ATOM   9774  C  CG    . TYR B 1 527 ? 111.379 154.691 164.560 1.00 26.66 ?  527 TYR B CG    1 
ATOM   9775  C  CD1   . TYR B 1 527 ? 111.643 153.676 163.652 1.00 26.45 ?  527 TYR B CD1   1 
ATOM   9776  C  CD2   . TYR B 1 527 ? 112.137 154.744 165.722 1.00 24.18 ?  527 TYR B CD2   1 
ATOM   9777  C  CE1   . TYR B 1 527 ? 112.632 152.748 163.889 1.00 23.64 ?  527 TYR B CE1   1 
ATOM   9778  C  CE2   . TYR B 1 527 ? 113.126 153.817 165.969 1.00 19.65 ?  527 TYR B CE2   1 
ATOM   9779  C  CZ    . TYR B 1 527 ? 113.370 152.823 165.049 1.00 20.98 ?  527 TYR B CZ    1 
ATOM   9780  O  OH    . TYR B 1 527 ? 114.358 151.897 165.289 1.00 30.81 ?  527 TYR B OH    1 
ATOM   9781  N  N     . PHE B 1 528 ? 108.783 156.004 167.124 1.00 29.04 ?  528 PHE B N     1 
ATOM   9782  C  CA    . PHE B 1 528 ? 108.895 155.867 168.568 1.00 26.61 ?  528 PHE B CA    1 
ATOM   9783  C  C     . PHE B 1 528 ? 107.613 155.378 169.224 1.00 33.94 ?  528 PHE B C     1 
ATOM   9784  O  O     . PHE B 1 528 ? 107.579 155.255 170.452 1.00 38.82 ?  528 PHE B O     1 
ATOM   9785  C  CB    . PHE B 1 528 ? 109.309 157.204 169.190 1.00 27.80 ?  528 PHE B CB    1 
ATOM   9786  C  CG    . PHE B 1 528 ? 110.569 157.778 168.611 1.00 29.99 ?  528 PHE B CG    1 
ATOM   9787  C  CD1   . PHE B 1 528 ? 111.803 157.451 169.145 1.00 26.60 ?  528 PHE B CD1   1 
ATOM   9788  C  CD2   . PHE B 1 528 ? 110.519 158.647 167.535 1.00 25.41 ?  528 PHE B CD2   1 
ATOM   9789  C  CE1   . PHE B 1 528 ? 112.964 157.979 168.616 1.00 28.91 ?  528 PHE B CE1   1 
ATOM   9790  C  CE2   . PHE B 1 528 ? 111.676 159.176 167.001 1.00 27.68 ?  528 PHE B CE2   1 
ATOM   9791  C  CZ    . PHE B 1 528 ? 112.900 158.841 167.542 1.00 27.60 ?  528 PHE B CZ    1 
ATOM   9792  N  N     . ASP B 1 529 ? 106.567 155.096 168.440 1.00 31.57 ?  529 ASP B N     1 
ATOM   9793  C  CA    . ASP B 1 529 ? 105.272 154.724 169.006 1.00 31.29 ?  529 ASP B CA    1 
ATOM   9794  C  C     . ASP B 1 529 ? 105.402 153.567 169.991 1.00 32.79 ?  529 ASP B C     1 
ATOM   9795  O  O     . ASP B 1 529 ? 105.125 153.715 171.188 1.00 37.04 ?  529 ASP B O     1 
ATOM   9796  C  CB    . ASP B 1 529 ? 104.301 154.365 167.880 1.00 31.85 ?  529 ASP B CB    1 
ATOM   9797  C  CG    . ASP B 1 529 ? 103.694 155.589 167.225 1.00 33.93 ?  529 ASP B CG    1 
ATOM   9798  O  OD1   . ASP B 1 529 ? 103.921 156.708 167.730 1.00 36.54 ?  529 ASP B OD1   1 
ATOM   9799  O  OD2   . ASP B 1 529 ? 102.992 155.429 166.204 1.00 36.46 -1 529 ASP B OD2   1 
ATOM   9800  N  N     . LYS B 1 530 ? 105.863 152.411 169.508 1.00 34.54 ?  530 LYS B N     1 
ATOM   9801  C  CA    . LYS B 1 530 ? 106.010 151.250 170.377 1.00 34.43 ?  530 LYS B CA    1 
ATOM   9802  C  C     . LYS B 1 530 ? 106.998 151.501 171.507 1.00 36.06 ?  530 LYS B C     1 
ATOM   9803  O  O     . LYS B 1 530 ? 106.971 150.781 172.510 1.00 36.80 ?  530 LYS B O     1 
ATOM   9804  C  CB    . LYS B 1 530 ? 106.452 150.032 169.565 1.00 33.22 ?  530 LYS B CB    1 
ATOM   9805  C  CG    . LYS B 1 530 ? 107.956 149.819 169.537 1.00 31.06 ?  530 LYS B CG    1 
ATOM   9806  C  CD    . LYS B 1 530 ? 108.362 148.866 168.433 1.00 32.94 ?  530 LYS B CD    1 
ATOM   9807  C  CE    . LYS B 1 530 ? 109.848 148.584 168.486 1.00 31.12 ?  530 LYS B CE    1 
ATOM   9808  N  NZ    . LYS B 1 530 ? 110.488 148.758 167.153 1.00 37.43 1  530 LYS B NZ    1 
ATOM   9809  N  N     . TYR B 1 531 ? 107.864 152.501 171.369 1.00 35.29 ?  531 TYR B N     1 
ATOM   9810  C  CA    . TYR B 1 531 ? 108.819 152.820 172.417 1.00 28.42 ?  531 TYR B CA    1 
ATOM   9811  C  C     . TYR B 1 531 ? 108.270 153.796 173.445 1.00 29.68 ?  531 TYR B C     1 
ATOM   9812  O  O     . TYR B 1 531 ? 108.827 153.891 174.545 1.00 33.16 ?  531 TYR B O     1 
ATOM   9813  C  CB    . TYR B 1 531 ? 110.099 153.388 171.803 1.00 27.04 ?  531 TYR B CB    1 
ATOM   9814  C  CG    . TYR B 1 531 ? 110.963 152.346 171.133 1.00 28.11 ?  531 TYR B CG    1 
ATOM   9815  C  CD1   . TYR B 1 531 ? 111.417 151.239 171.835 1.00 25.95 ?  531 TYR B CD1   1 
ATOM   9816  C  CD2   . TYR B 1 531 ? 111.323 152.470 169.798 1.00 27.49 ?  531 TYR B CD2   1 
ATOM   9817  C  CE1   . TYR B 1 531 ? 112.207 150.286 171.228 1.00 28.69 ?  531 TYR B CE1   1 
ATOM   9818  C  CE2   . TYR B 1 531 ? 112.113 151.520 169.183 1.00 23.66 ?  531 TYR B CE2   1 
ATOM   9819  C  CZ    . TYR B 1 531 ? 112.551 150.431 169.903 1.00 28.29 ?  531 TYR B CZ    1 
ATOM   9820  O  OH    . TYR B 1 531 ? 113.338 149.482 169.295 1.00 32.32 ?  531 TYR B OH    1 
ATOM   9821  N  N     . VAL B 1 532 ? 107.193 154.519 173.124 1.00 33.72 ?  532 VAL B N     1 
ATOM   9822  C  CA    . VAL B 1 532 ? 106.594 155.450 174.073 1.00 31.71 ?  532 VAL B CA    1 
ATOM   9823  C  C     . VAL B 1 532 ? 105.331 154.893 174.709 1.00 34.87 ?  532 VAL B C     1 
ATOM   9824  O  O     . VAL B 1 532 ? 104.654 155.613 175.455 1.00 40.13 ?  532 VAL B O     1 
ATOM   9825  C  CB    . VAL B 1 532 ? 106.303 156.814 173.412 1.00 34.38 ?  532 VAL B CB    1 
ATOM   9826  C  CG1   . VAL B 1 532 ? 107.586 157.432 172.881 1.00 32.64 ?  532 VAL B CG1   1 
ATOM   9827  C  CG2   . VAL B 1 532 ? 105.272 156.669 172.306 1.00 34.61 ?  532 VAL B CG2   1 
ATOM   9828  N  N     . SER B 1 533 ? 104.994 153.633 174.439 1.00 40.20 ?  533 SER B N     1 
ATOM   9829  C  CA    . SER B 1 533 ? 103.789 153.029 174.990 1.00 39.75 ?  533 SER B CA    1 
ATOM   9830  C  C     . SER B 1 533 ? 104.099 151.685 175.637 1.00 40.09 ?  533 SER B C     1 
ATOM   9831  O  O     . SER B 1 533 ? 103.383 151.245 176.542 1.00 44.55 ?  533 SER B O     1 
ATOM   9832  C  CB    . SER B 1 533 ? 102.732 152.862 173.898 1.00 41.09 ?  533 SER B CB    1 
ATOM   9833  O  OG    . SER B 1 533 ? 103.097 151.837 172.991 1.00 42.45 ?  533 SER B OG    1 
ATOM   9834  N  N     . THR B 1 534 ? 105.160 151.028 175.180 1.00 39.24 ?  534 THR B N     1 
ATOM   9835  C  CA    . THR B 1 534 ? 105.555 149.721 175.683 1.00 38.89 ?  534 THR B CA    1 
ATOM   9836  C  C     . THR B 1 534 ? 106.883 149.827 176.418 1.00 37.46 ?  534 THR B C     1 
ATOM   9837  O  O     . THR B 1 534 ? 107.813 150.492 175.950 1.00 43.15 ?  534 THR B O     1 
ATOM   9838  C  CB    . THR B 1 534 ? 105.670 148.701 174.546 1.00 39.21 ?  534 THR B CB    1 
ATOM   9839  O  OG1   . THR B 1 534 ? 104.492 148.754 173.733 1.00 40.92 ?  534 THR B OG1   1 
ATOM   9840  C  CG2   . THR B 1 534 ? 105.836 147.294 175.100 1.00 40.55 ?  534 THR B CG2   1 
ATOM   9841  N  N     . ASP B 1 535 ? 106.965 149.169 177.570 1.00 42.63 ?  535 ASP B N     1 
ATOM   9842  C  CA    . ASP B 1 535 ? 108.184 149.138 178.364 1.00 41.49 ?  535 ASP B CA    1 
ATOM   9843  C  C     . ASP B 1 535 ? 108.985 147.890 178.021 1.00 41.07 ?  535 ASP B C     1 
ATOM   9844  O  O     . ASP B 1 535 ? 108.449 146.777 178.035 1.00 42.97 ?  535 ASP B O     1 
ATOM   9845  C  CB    . ASP B 1 535 ? 107.852 149.169 179.857 1.00 38.42 ?  535 ASP B CB    1 
ATOM   9846  C  CG    . ASP B 1 535 ? 109.072 148.970 180.729 1.00 44.29 ?  535 ASP B CG    1 
ATOM   9847  O  OD1   . ASP B 1 535 ? 109.776 149.963 181.007 1.00 47.58 ?  535 ASP B OD1   1 
ATOM   9848  O  OD2   . ASP B 1 535 ? 109.321 147.818 181.140 1.00 46.27 -1 535 ASP B OD2   1 
ATOM   9849  N  N     . PHE B 1 536 ? 110.268 148.077 177.713 1.00 32.24 ?  536 PHE B N     1 
ATOM   9850  C  CA    . PHE B 1 536 ? 111.141 146.984 177.310 1.00 32.66 ?  536 PHE B CA    1 
ATOM   9851  C  C     . PHE B 1 536 ? 112.158 146.630 178.389 1.00 33.90 ?  536 PHE B C     1 
ATOM   9852  O  O     . PHE B 1 536 ? 113.200 146.040 178.086 1.00 35.05 ?  536 PHE B O     1 
ATOM   9853  C  CB    . PHE B 1 536 ? 111.845 147.326 175.997 1.00 29.99 ?  536 PHE B CB    1 
ATOM   9854  C  CG    . PHE B 1 536 ? 110.909 147.465 174.832 1.00 27.01 ?  536 PHE B CG    1 
ATOM   9855  C  CD1   . PHE B 1 536 ? 110.582 146.368 174.054 1.00 28.60 ?  536 PHE B CD1   1 
ATOM   9856  C  CD2   . PHE B 1 536 ? 110.347 148.691 174.518 1.00 30.83 ?  536 PHE B CD2   1 
ATOM   9857  C  CE1   . PHE B 1 536 ? 109.719 146.490 172.984 1.00 30.63 ?  536 PHE B CE1   1 
ATOM   9858  C  CE2   . PHE B 1 536 ? 109.482 148.820 173.450 1.00 35.58 ?  536 PHE B CE2   1 
ATOM   9859  C  CZ    . PHE B 1 536 ? 109.168 147.718 172.681 1.00 32.38 ?  536 PHE B CZ    1 
ATOM   9860  N  N     . SER B 1 537 ? 111.876 146.981 179.640 1.00 35.74 ?  537 SER B N     1 
ATOM   9861  C  CA    . SER B 1 537 ? 112.714 146.545 180.742 1.00 33.49 ?  537 SER B CA    1 
ATOM   9862  C  C     . SER B 1 537 ? 112.571 145.036 180.932 1.00 37.92 ?  537 SER B C     1 
ATOM   9863  O  O     . SER B 1 537 ? 111.540 144.455 180.583 1.00 39.77 ?  537 SER B O     1 
ATOM   9864  C  CB    . SER B 1 537 ? 112.331 147.275 182.026 1.00 35.62 ?  537 SER B CB    1 
ATOM   9865  O  OG    . SER B 1 537 ? 112.390 148.680 181.849 1.00 41.80 ?  537 SER B OG    1 
ATOM   9866  N  N     . PRO B 1 538 ? 113.599 144.374 181.464 1.00 35.53 ?  538 PRO B N     1 
ATOM   9867  C  CA    . PRO B 1 538 ? 113.535 142.915 181.607 1.00 34.54 ?  538 PRO B CA    1 
ATOM   9868  C  C     . PRO B 1 538 ? 112.379 142.479 182.494 1.00 38.77 ?  538 PRO B C     1 
ATOM   9869  O  O     . PRO B 1 538 ? 112.109 143.076 183.538 1.00 41.83 ?  538 PRO B O     1 
ATOM   9870  C  CB    . PRO B 1 538 ? 114.890 142.561 182.232 1.00 36.06 ?  538 PRO B CB    1 
ATOM   9871  C  CG    . PRO B 1 538 ? 115.774 143.715 181.912 1.00 37.65 ?  538 PRO B CG    1 
ATOM   9872  C  CD    . PRO B 1 538 ? 114.886 144.914 181.929 1.00 35.67 ?  538 PRO B CD    1 
ATOM   9873  N  N     . LYS B 1 539 ? 111.697 141.418 182.065 1.00 41.02 ?  539 LYS B N     1 
ATOM   9874  C  CA    . LYS B 1 539 ? 110.599 140.838 182.824 1.00 41.05 ?  539 LYS B CA    1 
ATOM   9875  C  C     . LYS B 1 539 ? 111.055 139.763 183.799 1.00 44.29 ?  539 LYS B C     1 
ATOM   9876  O  O     . LYS B 1 539 ? 110.253 139.321 184.628 1.00 47.25 ?  539 LYS B O     1 
ATOM   9877  C  CB    . LYS B 1 539 ? 109.552 140.249 181.873 1.00 42.03 ?  539 LYS B CB    1 
ATOM   9878  C  CG    . LYS B 1 539 ? 109.344 141.058 180.606 1.00 42.44 ?  539 LYS B CG    1 
ATOM   9879  C  CD    . LYS B 1 539 ? 108.136 141.972 180.728 1.00 42.09 ?  539 LYS B CD    1 
ATOM   9880  C  CE    . LYS B 1 539 ? 107.913 142.764 179.451 1.00 44.54 ?  539 LYS B CE    1 
ATOM   9881  N  NZ    . LYS B 1 539 ? 109.176 143.379 178.954 1.00 45.96 1  539 LYS B NZ    1 
ATOM   9882  N  N     . TYR B 1 540 ? 112.311 139.335 183.720 1.00 42.27 ?  540 TYR B N     1 
ATOM   9883  C  CA    . TYR B 1 540 ? 112.857 138.313 184.598 1.00 39.72 ?  540 TYR B CA    1 
ATOM   9884  C  C     . TYR B 1 540 ? 113.895 138.933 185.523 1.00 46.19 ?  540 TYR B C     1 
ATOM   9885  O  O     . TYR B 1 540 ? 114.639 139.833 185.122 1.00 47.07 ?  540 TYR B O     1 
ATOM   9886  C  CB    . TYR B 1 540 ? 113.481 137.172 183.790 1.00 41.89 ?  540 TYR B CB    1 
ATOM   9887  C  CG    . TYR B 1 540 ? 112.476 136.382 182.984 1.00 45.05 ?  540 TYR B CG    1 
ATOM   9888  C  CD1   . TYR B 1 540 ? 112.128 136.772 181.697 1.00 42.64 ?  540 TYR B CD1   1 
ATOM   9889  C  CD2   . TYR B 1 540 ? 111.869 135.251 183.513 1.00 45.24 ?  540 TYR B CD2   1 
ATOM   9890  C  CE1   . TYR B 1 540 ? 111.206 136.054 180.958 1.00 42.42 ?  540 TYR B CE1   1 
ATOM   9891  C  CE2   . TYR B 1 540 ? 110.947 134.528 182.782 1.00 42.26 ?  540 TYR B CE2   1 
ATOM   9892  C  CZ    . TYR B 1 540 ? 110.620 134.933 181.506 1.00 43.92 ?  540 TYR B CZ    1 
ATOM   9893  O  OH    . TYR B 1 540 ? 109.702 134.214 180.777 1.00 46.28 ?  540 TYR B OH    1 
ATOM   9894  N  N     . GLU B 1 541 ? 113.932 138.450 186.767 1.00 49.66 ?  541 GLU B N     1 
ATOM   9895  C  CA    . GLU B 1 541 ? 114.853 139.008 187.751 1.00 45.98 ?  541 GLU B CA    1 
ATOM   9896  C  C     . GLU B 1 541 ? 116.304 138.762 187.358 1.00 46.37 ?  541 GLU B C     1 
ATOM   9897  O  O     . GLU B 1 541 ? 117.170 139.613 187.593 1.00 45.04 ?  541 GLU B O     1 
ATOM   9898  C  CB    . GLU B 1 541 ? 114.565 138.422 189.133 1.00 46.69 ?  541 GLU B CB    1 
ATOM   9899  C  CG    . GLU B 1 541 ? 115.241 139.169 190.270 1.00 48.66 ?  541 GLU B CG    1 
ATOM   9900  C  CD    . GLU B 1 541 ? 115.063 140.671 190.167 1.00 50.84 ?  541 GLU B CD    1 
ATOM   9901  O  OE1   . GLU B 1 541 ? 113.904 141.131 190.112 1.00 50.80 ?  541 GLU B OE1   1 
ATOM   9902  O  OE2   . GLU B 1 541 ? 116.082 141.392 190.138 1.00 52.89 -1 541 GLU B OE2   1 
ATOM   9903  N  N     . LYS B 1 542 ? 116.593 137.598 186.772 1.00 42.48 ?  542 LYS B N     1 
ATOM   9904  C  CA    . LYS B 1 542 ? 117.962 137.293 186.365 1.00 39.80 ?  542 LYS B CA    1 
ATOM   9905  C  C     . LYS B 1 542 ? 118.455 138.271 185.306 1.00 42.82 ?  542 LYS B C     1 
ATOM   9906  O  O     . LYS B 1 542 ? 119.591 138.754 185.375 1.00 44.21 ?  542 LYS B O     1 
ATOM   9907  C  CB    . LYS B 1 542 ? 118.045 135.855 185.853 1.00 38.45 ?  542 LYS B CB    1 
ATOM   9908  C  CG    . LYS B 1 542 ? 119.446 135.406 185.476 1.00 43.63 ?  542 LYS B CG    1 
ATOM   9909  C  CD    . LYS B 1 542 ? 119.464 133.942 185.077 1.00 42.93 ?  542 LYS B CD    1 
ATOM   9910  C  CE    . LYS B 1 542 ? 120.883 133.450 184.851 1.00 43.45 ?  542 LYS B CE    1 
ATOM   9911  N  NZ    . LYS B 1 542 ? 120.941 131.974 184.668 1.00 41.95 1  542 LYS B NZ    1 
ATOM   9912  N  N     . ILE B 1 543 ? 117.610 138.587 184.325 1.00 39.40 ?  543 ILE B N     1 
ATOM   9913  C  CA    . ILE B 1 543 ? 118.000 139.534 183.285 1.00 37.20 ?  543 ILE B CA    1 
ATOM   9914  C  C     . ILE B 1 543 ? 118.166 140.933 183.865 1.00 36.34 ?  543 ILE B C     1 
ATOM   9915  O  O     . ILE B 1 543 ? 119.089 141.669 183.496 1.00 39.33 ?  543 ILE B O     1 
ATOM   9916  C  CB    . ILE B 1 543 ? 116.977 139.509 182.136 1.00 36.93 ?  543 ILE B CB    1 
ATOM   9917  C  CG1   . ILE B 1 543 ? 116.737 138.072 181.666 1.00 36.34 ?  543 ILE B CG1   1 
ATOM   9918  C  CG2   . ILE B 1 543 ? 117.454 140.372 180.989 1.00 35.21 ?  543 ILE B CG2   1 
ATOM   9919  C  CD1   . ILE B 1 543 ? 118.001 137.331 181.283 1.00 34.56 ?  543 ILE B CD1   1 
ATOM   9920  N  N     . ALA B 1 544 ? 117.273 141.326 184.778 1.00 37.78 ?  544 ALA B N     1 
ATOM   9921  C  CA    . ALA B 1 544 ? 117.401 142.629 185.422 1.00 40.15 ?  544 ALA B CA    1 
ATOM   9922  C  C     . ALA B 1 544 ? 118.705 142.731 186.202 1.00 39.96 ?  544 ALA B C     1 
ATOM   9923  O  O     . ALA B 1 544 ? 119.370 143.774 186.180 1.00 42.67 ?  544 ALA B O     1 
ATOM   9924  C  CB    . ALA B 1 544 ? 116.204 142.881 186.340 1.00 41.98 ?  544 ALA B CB    1 
ATOM   9925  N  N     . ASN B 1 545 ? 119.087 141.659 186.899 1.00 43.77 ?  545 ASN B N     1 
ATOM   9926  C  CA    . ASN B 1 545 ? 120.378 141.634 187.576 1.00 47.64 ?  545 ASN B CA    1 
ATOM   9927  C  C     . ASN B 1 545 ? 121.523 141.717 186.575 1.00 45.05 ?  545 ASN B C     1 
ATOM   9928  O  O     . ASN B 1 545 ? 122.540 142.370 186.834 1.00 46.84 ?  545 ASN B O     1 
ATOM   9929  C  CB    . ASN B 1 545 ? 120.500 140.372 188.430 1.00 44.49 ?  545 ASN B CB    1 
ATOM   9930  C  CG    . ASN B 1 545 ? 119.520 140.354 189.582 1.00 47.52 ?  545 ASN B CG    1 
ATOM   9931  O  OD1   . ASN B 1 545 ? 119.042 141.401 190.022 1.00 49.39 ?  545 ASN B OD1   1 
ATOM   9932  N  ND2   . ASN B 1 545 ? 119.211 139.163 190.080 1.00 44.45 ?  545 ASN B ND2   1 
ATOM   9933  N  N     . LEU B 1 546 ? 121.380 141.045 185.430 1.00 38.60 ?  546 LEU B N     1 
ATOM   9934  C  CA    . LEU B 1 546 ? 122.375 141.160 184.370 1.00 39.55 ?  546 LEU B CA    1 
ATOM   9935  C  C     . LEU B 1 546 ? 122.530 142.600 183.903 1.00 39.47 ?  546 LEU B C     1 
ATOM   9936  O  O     . LEU B 1 546 ? 123.636 143.025 183.553 1.00 39.00 ?  546 LEU B O     1 
ATOM   9937  C  CB    . LEU B 1 546 ? 121.994 140.261 183.194 1.00 36.75 ?  546 LEU B CB    1 
ATOM   9938  C  CG    . LEU B 1 546 ? 122.399 138.791 183.287 1.00 39.09 ?  546 LEU B CG    1 
ATOM   9939  C  CD1   . LEU B 1 546 ? 122.361 138.152 181.912 1.00 37.33 ?  546 LEU B CD1   1 
ATOM   9940  C  CD2   . LEU B 1 546 ? 123.779 138.649 183.909 1.00 38.77 ?  546 LEU B CD2   1 
ATOM   9941  N  N     . PHE B 1 547 ? 121.440 143.364 183.896 1.00 40.07 ?  547 PHE B N     1 
ATOM   9942  C  CA    . PHE B 1 547 ? 121.464 144.757 183.472 1.00 37.64 ?  547 PHE B CA    1 
ATOM   9943  C  C     . PHE B 1 547 ? 121.701 145.730 184.620 1.00 39.81 ?  547 PHE B C     1 
ATOM   9944  O  O     . PHE B 1 547 ? 121.513 146.937 184.437 1.00 43.53 ?  547 PHE B O     1 
ATOM   9945  C  CB    . PHE B 1 547 ? 120.157 145.113 182.760 1.00 35.49 ?  547 PHE B CB    1 
ATOM   9946  C  CG    . PHE B 1 547 ? 120.095 144.647 181.337 1.00 36.65 ?  547 PHE B CG    1 
ATOM   9947  C  CD1   . PHE B 1 547 ? 120.746 145.348 180.338 1.00 35.91 ?  547 PHE B CD1   1 
ATOM   9948  C  CD2   . PHE B 1 547 ? 119.386 143.509 180.997 1.00 35.72 ?  547 PHE B CD2   1 
ATOM   9949  C  CE1   . PHE B 1 547 ? 120.690 144.923 179.027 1.00 34.64 ?  547 PHE B CE1   1 
ATOM   9950  C  CE2   . PHE B 1 547 ? 119.328 143.081 179.688 1.00 36.03 ?  547 PHE B CE2   1 
ATOM   9951  C  CZ    . PHE B 1 547 ? 119.982 143.787 178.703 1.00 35.01 ?  547 PHE B CZ    1 
ATOM   9952  N  N     . GLU B 1 548 ? 122.103 145.241 185.790 1.00 47.04 ?  548 GLU B N     1 
ATOM   9953  C  CA    . GLU B 1 548 ? 122.359 146.126 186.918 1.00 47.44 ?  548 GLU B CA    1 
ATOM   9954  C  C     . GLU B 1 548 ? 123.576 147.004 186.654 1.00 47.26 ?  548 GLU B C     1 
ATOM   9955  O  O     . GLU B 1 548 ? 124.512 146.616 185.950 1.00 50.56 ?  548 GLU B O     1 
ATOM   9956  C  CB    . GLU B 1 548 ? 122.564 145.323 188.202 1.00 46.82 ?  548 GLU B CB    1 
ATOM   9957  C  CG    . GLU B 1 548 ? 121.274 144.871 188.867 1.00 48.12 ?  548 GLU B CG    1 
ATOM   9958  C  CD    . GLU B 1 548 ? 120.374 146.029 189.265 1.00 50.79 ?  548 GLU B CD    1 
ATOM   9959  O  OE1   . GLU B 1 548 ? 120.890 147.142 189.498 1.00 48.80 ?  548 GLU B OE1   1 
ATOM   9960  O  OE2   . GLU B 1 548 ? 119.146 145.822 189.345 1.00 50.91 -1 548 GLU B OE2   1 
ATOM   9961  N  N     . GLY B 1 549 ? 123.553 148.203 187.231 1.00 45.31 ?  549 GLY B N     1 
ATOM   9962  C  CA    . GLY B 1 549 ? 124.585 149.185 186.990 1.00 44.97 ?  549 GLY B CA    1 
ATOM   9963  C  C     . GLY B 1 549 ? 124.430 149.960 185.703 1.00 46.10 ?  549 GLY B C     1 
ATOM   9964  O  O     . GLY B 1 549 ? 125.311 150.764 185.373 1.00 47.53 ?  549 GLY B O     1 
ATOM   9965  N  N     . MET B 1 550 ? 123.342 149.745 184.967 1.00 45.44 ?  550 MET B N     1 
ATOM   9966  C  CA    . MET B 1 550 ? 123.098 150.409 183.696 1.00 44.20 ?  550 MET B CA    1 
ATOM   9967  C  C     . MET B 1 550 ? 121.668 150.925 183.679 1.00 44.33 ?  550 MET B C     1 
ATOM   9968  O  O     . MET B 1 550 ? 120.745 150.210 184.081 1.00 46.15 ?  550 MET B O     1 
ATOM   9969  C  CB    . MET B 1 550 ? 123.335 149.451 182.526 1.00 43.15 ?  550 MET B CB    1 
ATOM   9970  C  CG    . MET B 1 550 ? 124.582 149.757 181.724 1.00 48.10 ?  550 MET B CG    1 
ATOM   9971  S  SD    . MET B 1 550 ? 124.636 148.843 180.176 1.00 54.89 ?  550 MET B SD    1 
ATOM   9972  C  CE    . MET B 1 550 ? 124.613 147.155 180.771 1.00 44.40 ?  550 MET B CE    1 
ATOM   9973  N  N     . HIS B 1 551 ? 121.487 152.159 183.217 1.00 40.63 ?  551 HIS B N     1 
ATOM   9974  C  CA    . HIS B 1 551 ? 120.169 152.785 183.196 1.00 40.60 ?  551 HIS B CA    1 
ATOM   9975  C  C     . HIS B 1 551 ? 119.394 152.296 181.978 1.00 40.33 ?  551 HIS B C     1 
ATOM   9976  O  O     . HIS B 1 551 ? 119.642 152.744 180.855 1.00 41.37 ?  551 HIS B O     1 
ATOM   9977  C  CB    . HIS B 1 551 ? 120.294 154.304 183.182 1.00 39.84 ?  551 HIS B CB    1 
ATOM   9978  C  CG    . HIS B 1 551 ? 119.011 155.006 182.862 1.00 41.55 ?  551 HIS B CG    1 
ATOM   9979  N  ND1   . HIS B 1 551 ? 117.939 155.025 183.726 1.00 44.88 ?  551 HIS B ND1   1 
ATOM   9980  C  CD2   . HIS B 1 551 ? 118.626 155.705 181.768 1.00 41.27 ?  551 HIS B CD2   1 
ATOM   9981  C  CE1   . HIS B 1 551 ? 116.949 155.709 183.180 1.00 43.33 ?  551 HIS B CE1   1 
ATOM   9982  N  NE2   . HIS B 1 551 ? 117.340 156.132 181.992 1.00 40.71 ?  551 HIS B NE2   1 
ATOM   9983  N  N     . ILE B 1 552 ? 118.446 151.392 182.201 1.00 35.98 ?  552 ILE B N     1 
ATOM   9984  C  CA    . ILE B 1 552 ? 117.595 150.876 181.133 1.00 32.38 ?  552 ILE B CA    1 
ATOM   9985  C  C     . ILE B 1 552 ? 116.585 151.953 180.758 1.00 33.83 ?  552 ILE B C     1 
ATOM   9986  O  O     . ILE B 1 552 ? 115.825 152.413 181.621 1.00 38.54 ?  552 ILE B O     1 
ATOM   9987  C  CB    . ILE B 1 552 ? 116.893 149.578 181.560 1.00 35.25 ?  552 ILE B CB    1 
ATOM   9988  C  CG1   . ILE B 1 552 ? 117.926 148.532 181.981 1.00 34.38 ?  552 ILE B CG1   1 
ATOM   9989  C  CG2   . ILE B 1 552 ? 116.022 149.048 180.436 1.00 35.00 ?  552 ILE B CG2   1 
ATOM   9990  C  CD1   . ILE B 1 552 ? 117.350 147.415 182.813 1.00 33.66 ?  552 ILE B CD1   1 
ATOM   9991  N  N     . PRO B 1 553 ? 116.548 152.392 179.499 1.00 37.53 ?  553 PRO B N     1 
ATOM   9992  C  CA    . PRO B 1 553 ? 115.606 153.450 179.116 1.00 34.70 ?  553 PRO B CA    1 
ATOM   9993  C  C     . PRO B 1 553 ? 114.162 153.008 179.303 1.00 35.12 ?  553 PRO B C     1 
ATOM   9994  O  O     . PRO B 1 553 ? 113.788 151.879 178.977 1.00 37.86 ?  553 PRO B O     1 
ATOM   9995  C  CB    . PRO B 1 553 ? 115.931 153.698 177.639 1.00 32.01 ?  553 PRO B CB    1 
ATOM   9996  C  CG    . PRO B 1 553 ? 117.316 153.171 177.455 1.00 30.36 ?  553 PRO B CG    1 
ATOM   9997  C  CD    . PRO B 1 553 ? 117.431 152.009 178.387 1.00 32.54 ?  553 PRO B CD    1 
ATOM   9998  N  N     . THR B 1 554 ? 113.352 153.915 179.831 1.00 39.81 ?  554 THR B N     1 
ATOM   9999  C  CA    . THR B 1 554 ? 111.934 153.682 180.035 1.00 38.48 ?  554 THR B CA    1 
ATOM   10000 C  C     . THR B 1 554 ? 111.141 154.430 178.967 1.00 36.43 ?  554 THR B C     1 
ATOM   10001 O  O     . THR B 1 554 ? 111.703 154.995 178.024 1.00 36.73 ?  554 THR B O     1 
ATOM   10002 C  CB    . THR B 1 554 ? 111.528 154.104 181.448 1.00 38.13 ?  554 THR B CB    1 
ATOM   10003 O  OG1   . THR B 1 554 ? 111.754 155.509 181.613 1.00 37.11 ?  554 THR B OG1   1 
ATOM   10004 C  CG2   . THR B 1 554 ? 112.341 153.341 182.485 1.00 36.24 ?  554 THR B CG2   1 
ATOM   10005 N  N     . THR B 1 555 ? 109.813 154.433 179.107 1.00 39.09 ?  555 THR B N     1 
ATOM   10006 C  CA    . THR B 1 555 ? 108.983 155.170 178.160 1.00 36.65 ?  555 THR B CA    1 
ATOM   10007 C  C     . THR B 1 555 ? 109.224 156.671 178.252 1.00 39.53 ?  555 THR B C     1 
ATOM   10008 O  O     . THR B 1 555 ? 109.082 157.380 177.250 1.00 40.35 ?  555 THR B O     1 
ATOM   10009 C  CB    . THR B 1 555 ? 107.505 154.857 178.393 1.00 38.95 ?  555 THR B CB    1 
ATOM   10010 O  OG1   . THR B 1 555 ? 107.164 155.136 179.757 1.00 44.10 ?  555 THR B OG1   1 
ATOM   10011 C  CG2   . THR B 1 555 ? 107.217 153.395 178.090 1.00 39.39 ?  555 THR B CG2   1 
ATOM   10012 N  N     . GLU B 1 556 ? 109.591 157.173 179.434 1.00 37.71 ?  556 GLU B N     1 
ATOM   10013 C  CA    . GLU B 1 556 ? 109.884 158.597 179.574 1.00 37.73 ?  556 GLU B CA    1 
ATOM   10014 C  C     . GLU B 1 556 ? 111.179 158.968 178.859 1.00 40.49 ?  556 GLU B C     1 
ATOM   10015 O  O     . GLU B 1 556 ? 111.249 160.007 178.189 1.00 41.86 ?  556 GLU B O     1 
ATOM   10016 C  CB    . GLU B 1 556 ? 109.960 158.973 181.052 1.00 39.97 ?  556 GLU B CB    1 
ATOM   10017 C  CG    . GLU B 1 556 ? 108.615 158.990 181.758 1.00 41.23 ?  556 GLU B CG    1 
ATOM   10018 C  CD    . GLU B 1 556 ? 107.517 159.595 180.907 1.00 44.19 ?  556 GLU B CD    1 
ATOM   10019 O  OE1   . GLU B 1 556 ? 107.559 160.819 180.660 1.00 42.40 ?  556 GLU B OE1   1 
ATOM   10020 O  OE2   . GLU B 1 556 ? 106.609 158.848 180.485 1.00 44.24 -1 556 GLU B OE2   1 
ATOM   10021 N  N     . ASP B 1 557 ? 112.215 158.138 178.994 1.00 40.06 ?  557 ASP B N     1 
ATOM   10022 C  CA    . ASP B 1 557 ? 113.454 158.380 178.263 1.00 34.63 ?  557 ASP B CA    1 
ATOM   10023 C  C     . ASP B 1 557 ? 113.221 158.312 176.761 1.00 36.07 ?  557 ASP B C     1 
ATOM   10024 O  O     . ASP B 1 557 ? 113.793 159.099 175.998 1.00 38.98 ?  557 ASP B O     1 
ATOM   10025 C  CB    . ASP B 1 557 ? 114.524 157.373 178.686 1.00 32.74 ?  557 ASP B CB    1 
ATOM   10026 C  CG    . ASP B 1 557 ? 114.521 157.113 180.178 1.00 41.14 ?  557 ASP B CG    1 
ATOM   10027 O  OD1   . ASP B 1 557 ? 113.472 156.686 180.705 1.00 44.16 ?  557 ASP B OD1   1 
ATOM   10028 O  OD2   . ASP B 1 557 ? 115.567 157.333 180.823 1.00 42.26 -1 557 ASP B OD2   1 
ATOM   10029 N  N     . TRP B 1 558 ? 112.378 157.378 176.317 1.00 32.21 ?  558 TRP B N     1 
ATOM   10030 C  CA    . TRP B 1 558 ? 112.062 157.285 174.898 1.00 26.34 ?  558 TRP B CA    1 
ATOM   10031 C  C     . TRP B 1 558 ? 111.261 158.491 174.421 1.00 31.81 ?  558 TRP B C     1 
ATOM   10032 O  O     . TRP B 1 558 ? 111.445 158.951 173.292 1.00 38.07 ?  558 TRP B O     1 
ATOM   10033 C  CB    . TRP B 1 558 ? 111.309 155.988 174.616 1.00 27.19 ?  558 TRP B CB    1 
ATOM   10034 C  CG    . TRP B 1 558 ? 112.209 154.848 174.267 1.00 27.01 ?  558 TRP B CG    1 
ATOM   10035 C  CD1   . TRP B 1 558 ? 112.505 153.768 175.044 1.00 26.33 ?  558 TRP B CD1   1 
ATOM   10036 C  CD2   . TRP B 1 558 ? 112.927 154.669 173.041 1.00 27.89 ?  558 TRP B CD2   1 
ATOM   10037 N  NE1   . TRP B 1 558 ? 113.364 152.929 174.380 1.00 30.65 ?  558 TRP B NE1   1 
ATOM   10038 C  CE2   . TRP B 1 558 ? 113.638 153.458 173.147 1.00 28.06 ?  558 TRP B CE2   1 
ATOM   10039 C  CE3   . TRP B 1 558 ? 113.035 155.413 171.863 1.00 31.92 ?  558 TRP B CE3   1 
ATOM   10040 C  CZ2   . TRP B 1 558 ? 114.445 152.976 172.120 1.00 25.09 ?  558 TRP B CZ2   1 
ATOM   10041 C  CZ3   . TRP B 1 558 ? 113.838 154.934 170.847 1.00 26.96 ?  558 TRP B CZ3   1 
ATOM   10042 C  CH2   . TRP B 1 558 ? 114.532 153.727 170.981 1.00 21.83 ?  558 TRP B CH2   1 
ATOM   10043 N  N     . LYS B 1 559 ? 110.368 159.018 175.263 1.00 36.75 ?  559 LYS B N     1 
ATOM   10044 C  CA    . LYS B 1 559 ? 109.649 160.238 174.906 1.00 31.12 ?  559 LYS B CA    1 
ATOM   10045 C  C     . LYS B 1 559 ? 110.599 161.424 174.790 1.00 34.26 ?  559 LYS B C     1 
ATOM   10046 O  O     . LYS B 1 559 ? 110.479 162.242 173.869 1.00 34.78 ?  559 LYS B O     1 
ATOM   10047 C  CB    . LYS B 1 559 ? 108.559 160.525 175.937 1.00 35.39 ?  559 LYS B CB    1 
ATOM   10048 C  CG    . LYS B 1 559 ? 107.299 159.696 175.762 1.00 37.52 ?  559 LYS B CG    1 
ATOM   10049 C  CD    . LYS B 1 559 ? 106.419 159.766 176.998 1.00 36.46 ?  559 LYS B CD    1 
ATOM   10050 C  CE    . LYS B 1 559 ? 105.460 158.589 177.063 1.00 37.55 ?  559 LYS B CE    1 
ATOM   10051 N  NZ    . LYS B 1 559 ? 104.995 158.330 178.453 1.00 36.41 1  559 LYS B NZ    1 
ATOM   10052 N  N     . LYS B 1 560 ? 111.552 161.531 175.719 1.00 31.68 ?  560 LYS B N     1 
ATOM   10053 C  CA    . LYS B 1 560 ? 112.550 162.592 175.638 1.00 30.42 ?  560 LYS B CA    1 
ATOM   10054 C  C     . LYS B 1 560 ? 113.398 162.449 174.381 1.00 34.62 ?  560 LYS B C     1 
ATOM   10055 O  O     . LYS B 1 560 ? 113.715 163.444 173.720 1.00 36.67 ?  560 LYS B O     1 
ATOM   10056 C  CB    . LYS B 1 560 ? 113.429 162.583 176.887 1.00 30.64 ?  560 LYS B CB    1 
ATOM   10057 C  CG    . LYS B 1 560 ? 112.752 163.141 178.126 1.00 35.01 ?  560 LYS B CG    1 
ATOM   10058 C  CD    . LYS B 1 560 ? 113.712 163.181 179.304 1.00 37.36 ?  560 LYS B CD    1 
ATOM   10059 C  CE    . LYS B 1 560 ? 112.965 163.253 180.625 1.00 35.42 ?  560 LYS B CE    1 
ATOM   10060 N  NZ    . LYS B 1 560 ? 112.322 161.955 180.972 1.00 37.29 1  560 LYS B NZ    1 
ATOM   10061 N  N     . LEU B 1 561 ? 113.774 161.217 174.035 1.00 31.74 ?  561 LEU B N     1 
ATOM   10062 C  CA    . LEU B 1 561 ? 114.541 160.987 172.815 1.00 27.68 ?  561 LEU B CA    1 
ATOM   10063 C  C     . LEU B 1 561 ? 113.722 161.323 171.574 1.00 31.16 ?  561 LEU B C     1 
ATOM   10064 O  O     . LEU B 1 561 ? 114.258 161.853 170.596 1.00 33.36 ?  561 LEU B O     1 
ATOM   10065 C  CB    . LEU B 1 561 ? 115.024 159.538 172.762 1.00 29.77 ?  561 LEU B CB    1 
ATOM   10066 C  CG    . LEU B 1 561 ? 115.832 159.159 171.521 1.00 28.99 ?  561 LEU B CG    1 
ATOM   10067 C  CD1   . LEU B 1 561 ? 117.006 160.107 171.345 1.00 25.20 ?  561 LEU B CD1   1 
ATOM   10068 C  CD2   . LEU B 1 561 ? 116.310 157.724 171.607 1.00 26.50 ?  561 LEU B CD2   1 
ATOM   10069 N  N     . LYS B 1 562 ? 112.425 161.011 171.592 1.00 31.63 ?  562 LYS B N     1 
ATOM   10070 C  CA    . LYS B 1 562 ? 111.557 161.365 170.475 1.00 29.39 ?  562 LYS B CA    1 
ATOM   10071 C  C     . LYS B 1 562 ? 111.472 162.875 170.304 1.00 31.00 ?  562 LYS B C     1 
ATOM   10072 O  O     . LYS B 1 562 ? 111.532 163.387 169.180 1.00 35.93 ?  562 LYS B O     1 
ATOM   10073 C  CB    . LYS B 1 562 ? 110.168 160.763 170.691 1.00 27.01 ?  562 LYS B CB    1 
ATOM   10074 C  CG    . LYS B 1 562 ? 109.103 161.262 169.732 1.00 29.64 ?  562 LYS B CG    1 
ATOM   10075 C  CD    . LYS B 1 562 ? 107.740 160.700 170.101 1.00 30.78 ?  562 LYS B CD    1 
ATOM   10076 C  CE    . LYS B 1 562 ? 106.653 161.222 169.177 1.00 32.17 ?  562 LYS B CE    1 
ATOM   10077 N  NZ    . LYS B 1 562 ? 105.419 160.392 169.253 1.00 32.25 1  562 LYS B NZ    1 
ATOM   10078 N  N     . ALA B 1 563 ? 111.338 163.607 171.412 1.00 31.70 ?  563 ALA B N     1 
ATOM   10079 C  CA    . ALA B 1 563 ? 111.330 165.066 171.336 1.00 32.22 ?  563 ALA B CA    1 
ATOM   10080 C  C     . ALA B 1 563 ? 112.666 165.598 170.831 1.00 32.55 ?  563 ALA B C     1 
ATOM   10081 O  O     . ALA B 1 563 ? 112.708 166.539 170.028 1.00 36.45 ?  563 ALA B O     1 
ATOM   10082 C  CB    . ALA B 1 563 ? 110.996 165.661 172.704 1.00 32.53 ?  563 ALA B CB    1 
ATOM   10083 N  N     . PHE B 1 564 ? 113.770 165.004 171.290 1.00 32.33 ?  564 PHE B N     1 
ATOM   10084 C  CA    . PHE B 1 564 ? 115.094 165.425 170.844 1.00 27.46 ?  564 PHE B CA    1 
ATOM   10085 C  C     . PHE B 1 564 ? 115.269 165.197 169.346 1.00 30.75 ?  564 PHE B C     1 
ATOM   10086 O  O     . PHE B 1 564 ? 115.836 166.041 168.644 1.00 33.53 ?  564 PHE B O     1 
ATOM   10087 C  CB    . PHE B 1 564 ? 116.162 164.672 171.636 1.00 28.79 ?  564 PHE B CB    1 
ATOM   10088 C  CG    . PHE B 1 564 ? 117.544 165.234 171.487 1.00 32.18 ?  564 PHE B CG    1 
ATOM   10089 C  CD1   . PHE B 1 564 ? 117.954 166.313 172.251 1.00 31.86 ?  564 PHE B CD1   1 
ATOM   10090 C  CD2   . PHE B 1 564 ? 118.440 164.676 170.591 1.00 33.00 ?  564 PHE B CD2   1 
ATOM   10091 C  CE1   . PHE B 1 564 ? 119.228 166.827 172.118 1.00 34.64 ?  564 PHE B CE1   1 
ATOM   10092 C  CE2   . PHE B 1 564 ? 119.714 165.187 170.454 1.00 32.71 ?  564 PHE B CE2   1 
ATOM   10093 C  CZ    . PHE B 1 564 ? 120.110 166.263 171.218 1.00 34.29 ?  564 PHE B CZ    1 
ATOM   10094 N  N     . VAL B 1 565 ? 114.790 164.059 168.844 1.00 31.07 ?  565 VAL B N     1 
ATOM   10095 C  CA    . VAL B 1 565 ? 114.864 163.775 167.414 1.00 27.20 ?  565 VAL B CA    1 
ATOM   10096 C  C     . VAL B 1 565 ? 113.988 164.744 166.631 1.00 32.84 ?  565 VAL B C     1 
ATOM   10097 O  O     . VAL B 1 565 ? 114.388 165.246 165.575 1.00 34.16 ?  565 VAL B O     1 
ATOM   10098 C  CB    . VAL B 1 565 ? 114.477 162.311 167.141 1.00 27.17 ?  565 VAL B CB    1 
ATOM   10099 C  CG1   . VAL B 1 565 ? 114.293 162.075 165.652 1.00 27.37 ?  565 VAL B CG1   1 
ATOM   10100 C  CG2   . VAL B 1 565 ? 115.537 161.377 167.693 1.00 29.85 ?  565 VAL B CG2   1 
ATOM   10101 N  N     . ALA B 1 566 ? 112.784 165.024 167.131 1.00 34.96 ?  566 ALA B N     1 
ATOM   10102 C  CA    . ALA B 1 566 ? 111.911 165.978 166.455 1.00 34.18 ?  566 ALA B CA    1 
ATOM   10103 C  C     . ALA B 1 566 ? 112.556 167.356 166.383 1.00 36.19 ?  566 ALA B C     1 
ATOM   10104 O  O     . ALA B 1 566 ? 112.405 168.071 165.386 1.00 38.31 ?  566 ALA B O     1 
ATOM   10105 C  CB    . ALA B 1 566 ? 110.561 166.051 167.167 1.00 33.11 ?  566 ALA B CB    1 
ATOM   10106 N  N     . GLU B 1 567 ? 113.280 167.746 167.434 1.00 36.81 ?  567 GLU B N     1 
ATOM   10107 C  CA    . GLU B 1 567 ? 113.919 169.058 167.440 1.00 35.87 ?  567 GLU B CA    1 
ATOM   10108 C  C     . GLU B 1 567 ? 115.145 169.092 166.531 1.00 38.64 ?  567 GLU B C     1 
ATOM   10109 O  O     . GLU B 1 567 ? 115.345 170.063 165.790 1.00 44.38 ?  567 GLU B O     1 
ATOM   10110 C  CB    . GLU B 1 567 ? 114.296 169.446 168.870 1.00 34.73 ?  567 GLU B CB    1 
ATOM   10111 C  CG    . GLU B 1 567 ? 115.526 170.329 168.976 1.00 37.84 ?  567 GLU B CG    1 
ATOM   10112 C  CD    . GLU B 1 567 ? 115.441 171.311 170.127 1.00 42.89 ?  567 GLU B CD    1 
ATOM   10113 O  OE1   . GLU B 1 567 ? 116.382 172.112 170.297 1.00 42.59 ?  567 GLU B OE1   1 
ATOM   10114 O  OE2   . GLU B 1 567 ? 114.430 171.282 170.859 1.00 42.45 -1 567 GLU B OE2   1 
ATOM   10115 N  N     . HIS B 1 568 ? 115.972 168.044 166.561 1.00 34.94 ?  568 HIS B N     1 
ATOM   10116 C  CA    . HIS B 1 568 ? 117.265 168.071 165.890 1.00 31.70 ?  568 HIS B CA    1 
ATOM   10117 C  C     . HIS B 1 568 ? 117.368 167.162 164.674 1.00 32.49 ?  568 HIS B C     1 
ATOM   10118 O  O     . HIS B 1 568 ? 118.245 167.387 163.834 1.00 37.18 ?  568 HIS B O     1 
ATOM   10119 C  CB    . HIS B 1 568 ? 118.381 167.692 166.874 1.00 31.46 ?  568 HIS B CB    1 
ATOM   10120 C  CG    . HIS B 1 568 ? 118.575 168.684 167.976 1.00 35.80 ?  568 HIS B CG    1 
ATOM   10121 N  ND1   . HIS B 1 568 ? 118.455 168.351 169.307 1.00 36.83 ?  568 HIS B ND1   1 
ATOM   10122 C  CD2   . HIS B 1 568 ? 118.880 170.003 167.944 1.00 34.09 ?  568 HIS B CD2   1 
ATOM   10123 C  CE1   . HIS B 1 568 ? 118.679 169.421 170.048 1.00 32.59 ?  568 HIS B CE1   1 
ATOM   10124 N  NE2   . HIS B 1 568 ? 118.938 170.437 169.246 1.00 39.37 ?  568 HIS B NE2   1 
ATOM   10125 N  N     . GLY B 1 569 ? 116.514 166.155 164.553 1.00 28.65 ?  569 GLY B N     1 
ATOM   10126 C  CA    . GLY B 1 569 ? 116.618 165.227 163.448 1.00 27.61 ?  569 GLY B CA    1 
ATOM   10127 C  C     . GLY B 1 569 ? 117.598 164.104 163.726 1.00 29.72 ?  569 GLY B C     1 
ATOM   10128 O  O     . GLY B 1 569 ? 118.155 163.969 164.817 1.00 33.19 ?  569 GLY B O     1 
ATOM   10129 N  N     . MET B 1 570 ? 117.803 163.276 162.703 1.00 26.84 ?  570 MET B N     1 
ATOM   10130 C  CA    . MET B 1 570 ? 118.730 162.156 162.777 1.00 24.33 ?  570 MET B CA    1 
ATOM   10131 C  C     . MET B 1 570 ? 119.747 162.259 161.654 1.00 26.64 ?  570 MET B C     1 
ATOM   10132 O  O     . MET B 1 570 ? 119.392 162.550 160.508 1.00 30.44 ?  570 MET B O     1 
ATOM   10133 C  CB    . MET B 1 570 ? 118.002 160.812 162.692 1.00 25.96 ?  570 MET B CB    1 
ATOM   10134 C  CG    . MET B 1 570 ? 117.053 160.540 163.841 1.00 23.78 ?  570 MET B CG    1 
ATOM   10135 S  SD    . MET B 1 570 ? 117.412 158.972 164.645 1.00 38.72 ?  570 MET B SD    1 
ATOM   10136 C  CE    . MET B 1 570 ? 117.450 157.873 163.236 1.00 28.81 ?  570 MET B CE    1 
ATOM   10137 N  N     . TYR B 1 571 ? 121.013 162.016 161.988 1.00 19.73 ?  571 TYR B N     1 
ATOM   10138 C  CA    . TYR B 1 571 ? 122.070 162.079 160.987 1.00 11.33 ?  571 TYR B CA    1 
ATOM   10139 C  C     . TYR B 1 571 ? 122.073 160.865 160.068 1.00 18.37 ?  571 TYR B C     1 
ATOM   10140 O  O     . TYR B 1 571 ? 122.459 160.981 158.901 1.00 22.60 ?  571 TYR B O     1 
ATOM   10141 C  CB    . TYR B 1 571 ? 123.432 162.213 161.665 1.00 19.31 ?  571 TYR B CB    1 
ATOM   10142 C  CG    . TYR B 1 571 ? 124.541 162.599 160.717 1.00 20.16 ?  571 TYR B CG    1 
ATOM   10143 C  CD1   . TYR B 1 571 ? 124.621 163.885 160.203 1.00 23.18 ?  571 TYR B CD1   1 
ATOM   10144 C  CD2   . TYR B 1 571 ? 125.504 161.677 160.330 1.00 18.13 ?  571 TYR B CD2   1 
ATOM   10145 C  CE1   . TYR B 1 571 ? 125.631 164.243 159.334 1.00 23.37 ?  571 TYR B CE1   1 
ATOM   10146 C  CE2   . TYR B 1 571 ? 126.516 162.027 159.460 1.00 22.50 ?  571 TYR B CE2   1 
ATOM   10147 C  CZ    . TYR B 1 571 ? 126.575 163.312 158.966 1.00 27.73 ?  571 TYR B CZ    1 
ATOM   10148 O  OH    . TYR B 1 571 ? 127.584 163.665 158.100 1.00 26.73 ?  571 TYR B OH    1 
ATOM   10149 N  N     . HIS B 1 572 ? 121.654 159.706 160.566 1.00 20.02 ?  572 HIS B N     1 
ATOM   10150 C  CA    . HIS B 1 572 ? 121.735 158.457 159.823 1.00 13.85 ?  572 HIS B CA    1 
ATOM   10151 C  C     . HIS B 1 572 ? 120.338 157.971 159.470 1.00 22.03 ?  572 HIS B C     1 
ATOM   10152 O  O     . HIS B 1 572 ? 119.470 157.876 160.344 1.00 26.66 ?  572 HIS B O     1 
ATOM   10153 C  CB    . HIS B 1 572 ? 122.471 157.385 160.630 1.00 13.30 ?  572 HIS B CB    1 
ATOM   10154 C  CG    . HIS B 1 572 ? 123.758 157.858 161.229 1.00 14.70 ?  572 HIS B CG    1 
ATOM   10155 N  ND1   . HIS B 1 572 ? 123.842 158.363 162.508 1.00 18.30 ?  572 HIS B ND1   1 
ATOM   10156 C  CD2   . HIS B 1 572 ? 125.014 157.902 160.724 1.00 16.96 ?  572 HIS B CD2   1 
ATOM   10157 C  CE1   . HIS B 1 572 ? 125.094 158.698 162.766 1.00 19.14 ?  572 HIS B CE1   1 
ATOM   10158 N  NE2   . HIS B 1 572 ? 125.824 158.428 161.700 1.00 26.58 ?  572 HIS B NE2   1 
ATOM   10159 N  N     . SER B 1 573 ? 120.126 157.668 158.188 1.00 13.21 ?  573 SER B N     1 
ATOM   10160 C  CA    . SER B 1 573 ? 118.871 157.054 157.772 1.00 7.91  ?  573 SER B CA    1 
ATOM   10161 C  C     . SER B 1 573 ? 118.725 155.657 158.361 1.00 14.44 ?  573 SER B C     1 
ATOM   10162 O  O     . SER B 1 573 ? 117.624 155.252 158.752 1.00 21.39 ?  573 SER B O     1 
ATOM   10163 C  CB    . SER B 1 573 ? 118.791 157.006 156.248 1.00 14.15 ?  573 SER B CB    1 
ATOM   10164 O  OG    . SER B 1 573 ? 119.991 156.497 155.697 1.00 22.11 ?  573 SER B OG    1 
ATOM   10165 N  N     . TYR B 1 574 ? 119.822 154.908 158.425 1.00 14.03 ?  574 TYR B N     1 
ATOM   10166 C  CA    . TYR B 1 574 ? 119.833 153.565 158.980 1.00 7.35  ?  574 TYR B CA    1 
ATOM   10167 C  C     . TYR B 1 574 ? 121.046 153.430 159.884 1.00 8.48  ?  574 TYR B C     1 
ATOM   10168 O  O     . TYR B 1 574 ? 122.127 153.928 159.560 1.00 18.38 ?  574 TYR B O     1 
ATOM   10169 C  CB    . TYR B 1 574 ? 119.862 152.504 157.874 1.00 10.15 ?  574 TYR B CB    1 
ATOM   10170 C  CG    . TYR B 1 574 ? 118.749 152.661 156.866 1.00 7.41  ?  574 TYR B CG    1 
ATOM   10171 C  CD1   . TYR B 1 574 ? 118.896 153.495 155.766 1.00 9.48  ?  574 TYR B CD1   1 
ATOM   10172 C  CD2   . TYR B 1 574 ? 117.547 151.983 157.017 1.00 7.15  ?  574 TYR B CD2   1 
ATOM   10173 C  CE1   . TYR B 1 574 ? 117.880 153.651 154.848 1.00 9.78  ?  574 TYR B CE1   1 
ATOM   10174 C  CE2   . TYR B 1 574 ? 116.527 152.131 156.101 1.00 9.31  ?  574 TYR B CE2   1 
ATOM   10175 C  CZ    . TYR B 1 574 ? 116.700 152.966 155.020 1.00 4.50  ?  574 TYR B CZ    1 
ATOM   10176 O  OH    . TYR B 1 574 ? 115.688 153.116 154.102 1.00 17.16 ?  574 TYR B OH    1 
ATOM   10177 N  N     . ARG B 1 575 ? 120.861 152.766 161.019 1.00 10.32 ?  575 ARG B N     1 
ATOM   10178 C  CA    . ARG B 1 575 ? 121.897 152.699 162.041 1.00 4.99  ?  575 ARG B CA    1 
ATOM   10179 C  C     . ARG B 1 575 ? 122.303 151.284 162.414 1.00 12.76 ?  575 ARG B C     1 
ATOM   10180 O  O     . ARG B 1 575 ? 123.494 151.019 162.586 1.00 18.56 ?  575 ARG B O     1 
ATOM   10181 C  CB    . ARG B 1 575 ? 121.429 153.433 163.303 1.00 13.95 ?  575 ARG B CB    1 
ATOM   10182 C  CG    . ARG B 1 575 ? 121.117 154.901 163.090 1.00 6.32  ?  575 ARG B CG    1 
ATOM   10183 C  CD    . ARG B 1 575 ? 120.121 155.396 164.121 1.00 13.67 ?  575 ARG B CD    1 
ATOM   10184 N  NE    . ARG B 1 575 ? 118.803 154.801 163.936 1.00 18.22 ?  575 ARG B NE    1 
ATOM   10185 C  CZ    . ARG B 1 575 ? 118.318 153.807 164.667 1.00 13.40 ?  575 ARG B CZ    1 
ATOM   10186 N  NH1   . ARG B 1 575 ? 119.023 153.261 165.644 1.00 12.95 1  575 ARG B NH1   1 
ATOM   10187 N  NH2   . ARG B 1 575 ? 117.096 153.349 164.413 1.00 11.24 ?  575 ARG B NH2   1 
ATOM   10188 N  N     . LEU B 1 576 ? 121.352 150.365 162.543 1.00 20.40 ?  576 LEU B N     1 
ATOM   10189 C  CA    . LEU B 1 576 ? 121.615 149.036 163.074 1.00 10.53 ?  576 LEU B CA    1 
ATOM   10190 C  C     . LEU B 1 576 ? 121.345 147.984 162.010 1.00 5.36  ?  576 LEU B C     1 
ATOM   10191 O  O     . LEU B 1 576 ? 120.249 147.933 161.445 1.00 15.05 ?  576 LEU B O     1 
ATOM   10192 C  CB    . LEU B 1 576 ? 120.754 148.761 164.310 1.00 6.04  ?  576 LEU B CB    1 
ATOM   10193 C  CG    . LEU B 1 576 ? 120.795 149.803 165.426 1.00 7.13  ?  576 LEU B CG    1 
ATOM   10194 C  CD1   . LEU B 1 576 ? 119.784 149.461 166.506 1.00 13.51 ?  576 LEU B CD1   1 
ATOM   10195 C  CD2   . LEU B 1 576 ? 122.188 149.908 166.011 1.00 10.43 ?  576 LEU B CD2   1 
ATOM   10196 N  N     . CYS B 1 577 ? 122.347 147.151 161.741 1.00 14.04 ?  577 CYS B N     1 
ATOM   10197 C  CA    . CYS B 1 577 ? 122.181 145.965 160.913 1.00 8.07  ?  577 CYS B CA    1 
ATOM   10198 C  C     . CYS B 1 577 ? 123.129 144.902 161.444 1.00 14.92 ?  577 CYS B C     1 
ATOM   10199 O  O     . CYS B 1 577 ? 124.301 145.187 161.701 1.00 21.80 ?  577 CYS B O     1 
ATOM   10200 C  CB    . CYS B 1 577 ? 122.445 146.264 159.429 1.00 5.93  ?  577 CYS B CB    1 
ATOM   10201 S  SG    . CYS B 1 577 ? 124.152 146.107 158.849 1.00 35.18 ?  577 CYS B SG    1 
ATOM   10202 N  N     . ILE B 1 578 ? 122.614 143.692 161.636 1.00 16.01 ?  578 ILE B N     1 
ATOM   10203 C  CA    . ILE B 1 578 ? 123.360 142.615 162.275 1.00 12.46 ?  578 ILE B CA    1 
ATOM   10204 C  C     . ILE B 1 578 ? 123.906 141.715 161.172 1.00 9.65  ?  578 ILE B C     1 
ATOM   10205 O  O     . ILE B 1 578 ? 123.198 140.859 160.635 1.00 18.17 ?  578 ILE B O     1 
ATOM   10206 C  CB    . ILE B 1 578 ? 122.495 141.844 163.275 1.00 9.77  ?  578 ILE B CB    1 
ATOM   10207 C  CG1   . ILE B 1 578 ? 121.965 142.796 164.348 1.00 8.00  ?  578 ILE B CG1   1 
ATOM   10208 C  CG2   . ILE B 1 578 ? 123.292 140.732 163.922 1.00 9.50  ?  578 ILE B CG2   1 
ATOM   10209 C  CD1   . ILE B 1 578 ? 121.262 142.103 165.481 1.00 8.95  ?  578 ILE B CD1   1 
ATOM   10210 N  N     . ALA B 1 579 ? 125.176 141.917 160.835 1.00 17.09 ?  579 ALA B N     1 
ATOM   10211 C  CA    . ALA B 1 579 ? 125.874 141.134 159.832 1.00 7.33  ?  579 ALA B CA    1 
ATOM   10212 C  C     . ALA B 1 579 ? 126.264 139.767 160.388 1.00 21.03 ?  579 ALA B C     1 
ATOM   10213 O  O     . ALA B 1 579 ? 126.255 139.556 161.601 1.00 28.62 ?  579 ALA B O     1 
ATOM   10214 C  CB    . ALA B 1 579 ? 127.111 141.889 159.360 1.00 11.73 ?  579 ALA B CB    1 
ATOM   10215 N  N     . PRO B 1 580 ? 126.584 138.806 159.514 1.00 25.04 ?  580 PRO B N     1 
ATOM   10216 C  CA    . PRO B 1 580 ? 127.021 137.489 160.008 1.00 22.61 ?  580 PRO B CA    1 
ATOM   10217 C  C     . PRO B 1 580 ? 128.284 137.528 160.855 1.00 25.92 ?  580 PRO B C     1 
ATOM   10218 O  O     . PRO B 1 580 ? 128.419 136.704 161.769 1.00 32.85 ?  580 PRO B O     1 
ATOM   10219 C  CB    . PRO B 1 580 ? 127.228 136.677 158.721 1.00 22.52 ?  580 PRO B CB    1 
ATOM   10220 C  CG    . PRO B 1 580 ? 127.240 137.673 157.609 1.00 21.75 ?  580 PRO B CG    1 
ATOM   10221 C  CD    . PRO B 1 580 ? 126.385 138.803 158.056 1.00 19.76 ?  580 PRO B CD    1 
ATOM   10222 N  N     . THR B 1 581 ? 129.207 138.454 160.585 1.00 21.55 ?  581 THR B N     1 
ATOM   10223 C  CA    . THR B 1 581 ? 130.474 138.576 161.317 1.00 29.18 ?  581 THR B CA    1 
ATOM   10224 C  C     . THR B 1 581 ? 131.216 137.235 161.360 1.00 28.51 ?  581 THR B C     1 
ATOM   10225 O  O     . THR B 1 581 ? 131.421 136.629 162.410 1.00 27.81 ?  581 THR B O     1 
ATOM   10226 C  CB    . THR B 1 581 ? 130.260 139.118 162.736 1.00 28.11 ?  581 THR B CB    1 
ATOM   10227 O  OG1   . THR B 1 581 ? 130.008 138.032 163.637 1.00 27.66 ?  581 THR B OG1   1 
ATOM   10228 C  CG2   . THR B 1 581 ? 129.109 140.109 162.785 1.00 30.44 ?  581 THR B CG2   1 
ATOM   10229 N  N     . GLY B 1 582 ? 131.619 136.793 160.171 1.00 31.48 ?  582 GLY B N     1 
ATOM   10230 C  CA    . GLY B 1 582 ? 132.184 135.469 160.010 1.00 33.44 ?  582 GLY B CA    1 
ATOM   10231 C  C     . GLY B 1 582 ? 133.521 135.234 160.681 1.00 37.00 ?  582 GLY B C     1 
ATOM   10232 O  O     . GLY B 1 582 ? 133.607 134.459 161.639 1.00 38.24 ?  582 GLY B O     1 
ATOM   10233 N  N     . SER B 1 583 ? 134.576 135.895 160.200 1.00 31.25 ?  583 SER B N     1 
ATOM   10234 C  CA    . SER B 1 583 ? 135.926 135.598 160.660 1.00 33.74 ?  583 SER B CA    1 
ATOM   10235 C  C     . SER B 1 583 ? 136.434 136.552 161.730 1.00 35.09 ?  583 SER B C     1 
ATOM   10236 O  O     . SER B 1 583 ? 137.327 136.174 162.496 1.00 37.38 ?  583 SER B O     1 
ATOM   10237 C  CB    . SER B 1 583 ? 136.903 135.610 159.478 1.00 37.87 ?  583 SER B CB    1 
ATOM   10238 O  OG    . SER B 1 583 ? 136.917 134.354 158.822 1.00 41.00 ?  583 SER B OG    1 
ATOM   10239 N  N     . ILE B 1 584 ? 135.895 137.770 161.807 1.00 33.94 ?  584 ILE B N     1 
ATOM   10240 C  CA    . ILE B 1 584 ? 136.328 138.700 162.840 1.00 27.57 ?  584 ILE B CA    1 
ATOM   10241 C  C     . ILE B 1 584 ? 135.783 138.313 164.209 1.00 26.21 ?  584 ILE B C     1 
ATOM   10242 O  O     . ILE B 1 584 ? 136.250 138.834 165.228 1.00 29.85 ?  584 ILE B O     1 
ATOM   10243 C  CB    . ILE B 1 584 ? 135.926 140.138 162.465 1.00 31.69 ?  584 ILE B CB    1 
ATOM   10244 C  CG1   . ILE B 1 584 ? 136.875 141.143 163.119 1.00 28.37 ?  584 ILE B CG1   1 
ATOM   10245 C  CG2   . ILE B 1 584 ? 134.485 140.417 162.864 1.00 29.13 ?  584 ILE B CG2   1 
ATOM   10246 C  CD1   . ILE B 1 584 ? 138.328 140.922 162.810 1.00 31.61 ?  584 ILE B CD1   1 
ATOM   10247 N  N     . SER B 1 585 ? 134.804 137.407 164.261 1.00 31.58 ?  585 SER B N     1 
ATOM   10248 C  CA    . SER B 1 585 ? 134.323 136.920 165.548 1.00 30.22 ?  585 SER B CA    1 
ATOM   10249 C  C     . SER B 1 585 ? 135.362 136.043 166.232 1.00 28.05 ?  585 SER B C     1 
ATOM   10250 O  O     . SER B 1 585 ? 135.349 135.912 167.461 1.00 26.72 ?  585 SER B O     1 
ATOM   10251 C  CB    . SER B 1 585 ? 133.013 136.153 165.367 1.00 25.61 ?  585 SER B CB    1 
ATOM   10252 O  OG    . SER B 1 585 ? 133.195 135.023 164.533 1.00 30.23 ?  585 SER B OG    1 
ATOM   10253 N  N     . TYR B 1 586 ? 136.258 135.431 165.455 1.00 31.10 ?  586 TYR B N     1 
ATOM   10254 C  CA    . TYR B 1 586 ? 137.341 134.646 166.035 1.00 32.10 ?  586 TYR B CA    1 
ATOM   10255 C  C     . TYR B 1 586 ? 138.271 135.526 166.859 1.00 31.26 ?  586 TYR B C     1 
ATOM   10256 O  O     . TYR B 1 586 ? 138.635 135.179 167.989 1.00 34.53 ?  586 TYR B O     1 
ATOM   10257 C  CB    . TYR B 1 586 ? 138.122 133.944 164.926 1.00 28.08 ?  586 TYR B CB    1 
ATOM   10258 C  CG    . TYR B 1 586 ? 137.432 132.732 164.351 1.00 31.07 ?  586 TYR B CG    1 
ATOM   10259 C  CD1   . TYR B 1 586 ? 137.139 131.633 165.144 1.00 31.09 ?  586 TYR B CD1   1 
ATOM   10260 C  CD2   . TYR B 1 586 ? 137.071 132.690 163.012 1.00 31.81 ?  586 TYR B CD2   1 
ATOM   10261 C  CE1   . TYR B 1 586 ? 136.507 130.526 164.619 1.00 33.96 ?  586 TYR B CE1   1 
ATOM   10262 C  CE2   . TYR B 1 586 ? 136.439 131.588 162.478 1.00 30.57 ?  586 TYR B CE2   1 
ATOM   10263 C  CZ    . TYR B 1 586 ? 136.160 130.509 163.285 1.00 34.73 ?  586 TYR B CZ    1 
ATOM   10264 O  OH    . TYR B 1 586 ? 135.530 129.408 162.754 1.00 37.76 ?  586 TYR B OH    1 
ATOM   10265 N  N     . VAL B 1 587 ? 138.657 136.679 166.308 1.00 28.11 ?  587 VAL B N     1 
ATOM   10266 C  CA    . VAL B 1 587 ? 139.612 137.558 166.978 1.00 24.65 ?  587 VAL B CA    1 
ATOM   10267 C  C     . VAL B 1 587 ? 139.029 138.093 168.278 1.00 29.14 ?  587 VAL B C     1 
ATOM   10268 O  O     . VAL B 1 587 ? 139.741 138.246 169.279 1.00 35.72 ?  587 VAL B O     1 
ATOM   10269 C  CB    . VAL B 1 587 ? 140.031 138.701 166.035 1.00 30.15 ?  587 VAL B CB    1 
ATOM   10270 C  CG1   . VAL B 1 587 ? 141.166 139.504 166.645 1.00 30.11 ?  587 VAL B CG1   1 
ATOM   10271 C  CG2   . VAL B 1 587 ? 140.427 138.150 164.675 1.00 28.67 ?  587 VAL B CG2   1 
ATOM   10272 N  N     . GLN B 1 588 ? 137.731 138.378 168.289 1.00 31.14 ?  588 GLN B N     1 
ATOM   10273 C  CA    . GLN B 1 588 ? 137.073 138.928 169.465 1.00 24.26 ?  588 GLN B CA    1 
ATOM   10274 C  C     . GLN B 1 588 ? 136.709 137.867 170.493 1.00 25.55 ?  588 GLN B C     1 
ATOM   10275 O  O     . GLN B 1 588 ? 136.175 138.218 171.550 1.00 32.76 ?  588 GLN B O     1 
ATOM   10276 C  CB    . GLN B 1 588 ? 135.814 139.693 169.053 1.00 25.03 ?  588 GLN B CB    1 
ATOM   10277 C  CG    . GLN B 1 588 ? 136.091 141.033 168.399 1.00 28.82 ?  588 GLN B CG    1 
ATOM   10278 C  CD    . GLN B 1 588 ? 135.992 142.183 169.379 1.00 24.32 ?  588 GLN B CD    1 
ATOM   10279 O  OE1   . GLN B 1 588 ? 135.037 142.278 170.147 1.00 29.94 ?  588 GLN B OE1   1 
ATOM   10280 N  NE2   . GLN B 1 588 ? 136.982 143.067 169.357 1.00 26.90 ?  588 GLN B NE2   1 
ATOM   10281 N  N     . SER B 1 589 ? 136.992 136.595 170.213 1.00 30.06 ?  589 SER B N     1 
ATOM   10282 C  CA    . SER B 1 589 ? 136.599 135.480 171.071 1.00 27.12 ?  589 SER B CA    1 
ATOM   10283 C  C     . SER B 1 589 ? 135.099 135.535 171.349 1.00 26.93 ?  589 SER B C     1 
ATOM   10284 O  O     . SER B 1 589 ? 134.642 135.592 172.491 1.00 28.72 ?  589 SER B O     1 
ATOM   10285 C  CB    . SER B 1 589 ? 137.409 135.470 172.369 1.00 32.57 ?  589 SER B CB    1 
ATOM   10286 O  OG    . SER B 1 589 ? 138.783 135.255 172.106 1.00 36.64 ?  589 SER B OG    1 
ATOM   10287 N  N     . SER B 1 590 ? 134.335 135.529 170.261 1.00 25.89 ?  590 SER B N     1 
ATOM   10288 C  CA    . SER B 1 590 ? 132.897 135.726 170.320 1.00 22.92 ?  590 SER B CA    1 
ATOM   10289 C  C     . SER B 1 590 ? 132.211 134.762 169.367 1.00 25.94 ?  590 SER B C     1 
ATOM   10290 O  O     . SER B 1 590 ? 132.781 134.352 168.353 1.00 29.51 ?  590 SER B O     1 
ATOM   10291 C  CB    . SER B 1 590 ? 132.523 137.169 169.964 1.00 21.98 ?  590 SER B CB    1 
ATOM   10292 O  OG    . SER B 1 590 ? 132.267 137.302 168.578 1.00 31.28 ?  590 SER B OG    1 
ATOM   10293 N  N     . THR B 1 591 ? 130.978 134.397 169.708 1.00 25.52 ?  591 THR B N     1 
ATOM   10294 C  CA    . THR B 1 591 ? 130.156 133.621 168.795 1.00 21.76 ?  591 THR B CA    1 
ATOM   10295 C  C     . THR B 1 591 ? 129.684 134.499 167.642 1.00 24.15 ?  591 THR B C     1 
ATOM   10296 O  O     . THR B 1 591 ? 129.468 135.704 167.797 1.00 22.75 ?  591 THR B O     1 
ATOM   10297 C  CB    . THR B 1 591 ? 128.959 133.017 169.524 1.00 22.02 ?  591 THR B CB    1 
ATOM   10298 O  OG1   . THR B 1 591 ? 128.009 134.046 169.825 1.00 29.69 ?  591 THR B OG1   1 
ATOM   10299 C  CG2   . THR B 1 591 ? 129.409 132.357 170.815 1.00 20.22 ?  591 THR B CG2   1 
ATOM   10300 N  N     . ALA B 1 592 ? 129.529 133.882 166.475 1.00 22.71 ?  592 ALA B N     1 
ATOM   10301 C  CA    . ALA B 1 592 ? 129.237 134.626 165.257 1.00 20.11 ?  592 ALA B CA    1 
ATOM   10302 C  C     . ALA B 1 592 ? 127.854 135.262 165.337 1.00 19.32 ?  592 ALA B C     1 
ATOM   10303 O  O     . ALA B 1 592 ? 126.841 134.558 165.388 1.00 27.49 ?  592 ALA B O     1 
ATOM   10304 C  CB    . ALA B 1 592 ? 129.332 133.705 164.044 1.00 24.99 ?  592 ALA B CB    1 
ATOM   10305 N  N     . SER B 1 593 ? 127.822 136.591 165.354 1.00 25.09 ?  593 SER B N     1 
ATOM   10306 C  CA    . SER B 1 593 ? 126.588 137.380 165.238 1.00 14.55 ?  593 SER B CA    1 
ATOM   10307 C  C     . SER B 1 593 ? 125.660 137.031 166.404 1.00 16.18 ?  593 SER B C     1 
ATOM   10308 O  O     . SER B 1 593 ? 126.116 136.608 167.475 1.00 27.98 ?  593 SER B O     1 
ATOM   10309 C  CB    . SER B 1 593 ? 125.986 137.162 163.862 1.00 27.06 ?  593 SER B CB    1 
ATOM   10310 O  OG    . SER B 1 593 ? 124.933 138.072 163.610 1.00 23.36 ?  593 SER B OG    1 
ATOM   10311 N  N     . VAL B 1 594 ? 124.354 137.210 166.208 1.00 19.65 ?  594 VAL B N     1 
ATOM   10312 C  CA    . VAL B 1 594 ? 123.354 136.798 167.182 1.00 19.52 ?  594 VAL B CA    1 
ATOM   10313 C  C     . VAL B 1 594 ? 122.861 135.380 166.914 1.00 18.59 ?  594 VAL B C     1 
ATOM   10314 O  O     . VAL B 1 594 ? 121.931 134.913 167.578 1.00 18.18 ?  594 VAL B O     1 
ATOM   10315 C  CB    . VAL B 1 594 ? 122.178 137.788 167.222 1.00 17.07 ?  594 VAL B CB    1 
ATOM   10316 C  CG1   . VAL B 1 594 ? 122.658 139.161 167.663 1.00 12.24 ?  594 VAL B CG1   1 
ATOM   10317 C  CG2   . VAL B 1 594 ? 121.504 137.867 165.864 1.00 19.04 ?  594 VAL B CG2   1 
ATOM   10318 N  N     . MET B 1 595 ? 123.463 134.687 165.952 1.00 23.61 ?  595 MET B N     1 
ATOM   10319 C  CA    . MET B 1 595 ? 123.090 133.315 165.667 1.00 19.01 ?  595 MET B CA    1 
ATOM   10320 C  C     . MET B 1 595 ? 123.597 132.387 166.768 1.00 26.69 ?  595 MET B C     1 
ATOM   10321 O  O     . MET B 1 595 ? 124.620 132.662 167.403 1.00 29.65 ?  595 MET B O     1 
ATOM   10322 C  CB    . MET B 1 595 ? 123.666 132.871 164.324 1.00 18.08 ?  595 MET B CB    1 
ATOM   10323 C  CG    . MET B 1 595 ? 122.847 133.261 163.102 1.00 24.07 ?  595 MET B CG    1 
ATOM   10324 S  SD    . MET B 1 595 ? 121.081 133.416 163.415 1.00 29.78 ?  595 MET B SD    1 
ATOM   10325 C  CE    . MET B 1 595 ? 120.912 135.196 163.420 1.00 22.55 ?  595 MET B CE    1 
ATOM   10326 N  N     . PRO B 1 596 ? 122.900 131.283 167.019 1.00 29.56 ?  596 PRO B N     1 
ATOM   10327 C  CA    . PRO B 1 596 ? 123.438 130.264 167.922 1.00 19.09 ?  596 PRO B CA    1 
ATOM   10328 C  C     . PRO B 1 596 ? 124.606 129.527 167.282 1.00 25.93 ?  596 PRO B C     1 
ATOM   10329 O  O     . PRO B 1 596 ? 124.743 129.458 166.059 1.00 30.62 ?  596 PRO B O     1 
ATOM   10330 C  CB    . PRO B 1 596 ? 122.248 129.331 168.158 1.00 20.74 ?  596 PRO B CB    1 
ATOM   10331 C  CG    . PRO B 1 596 ? 121.392 129.503 166.955 1.00 23.25 ?  596 PRO B CG    1 
ATOM   10332 C  CD    . PRO B 1 596 ? 121.570 130.922 166.497 1.00 25.77 ?  596 PRO B CD    1 
ATOM   10333 N  N     . ILE B 1 597 ? 125.462 128.974 168.143 1.00 28.44 ?  597 ILE B N     1 
ATOM   10334 C  CA    . ILE B 1 597 ? 126.687 128.335 167.679 1.00 31.03 ?  597 ILE B CA    1 
ATOM   10335 C  C     . ILE B 1 597 ? 126.354 127.097 166.857 1.00 34.42 ?  597 ILE B C     1 
ATOM   10336 O  O     . ILE B 1 597 ? 125.428 126.339 167.179 1.00 37.08 ?  597 ILE B O     1 
ATOM   10337 C  CB    . ILE B 1 597 ? 127.597 127.985 168.868 1.00 32.17 ?  597 ILE B CB    1 
ATOM   10338 C  CG1   . ILE B 1 597 ? 126.908 126.985 169.798 1.00 30.45 ?  597 ILE B CG1   1 
ATOM   10339 C  CG2   . ILE B 1 597 ? 127.980 129.240 169.627 1.00 29.22 ?  597 ILE B CG2   1 
ATOM   10340 C  CD1   . ILE B 1 597 ? 127.858 126.053 170.504 1.00 29.18 ?  597 ILE B CD1   1 
ATOM   10341 N  N     . MET B 1 598 ? 127.103 126.898 165.772 1.00 40.22 ?  598 MET B N     1 
ATOM   10342 C  CA    . MET B 1 598 ? 126.922 125.698 164.962 1.00 38.65 ?  598 MET B CA    1 
ATOM   10343 C  C     . MET B 1 598 ? 127.428 124.461 165.692 1.00 36.48 ?  598 MET B C     1 
ATOM   10344 O  O     . MET B 1 598 ? 126.777 123.410 165.671 1.00 42.09 ?  598 MET B O     1 
ATOM   10345 C  CB    . MET B 1 598 ? 127.637 125.859 163.621 1.00 38.14 ?  598 MET B CB    1 
ATOM   10346 C  CG    . MET B 1 598 ? 126.838 126.623 162.583 1.00 35.63 ?  598 MET B CG    1 
ATOM   10347 S  SD    . MET B 1 598 ? 127.873 127.374 161.314 1.00 53.34 ?  598 MET B SD    1 
ATOM   10348 C  CE    . MET B 1 598 ? 129.023 128.307 162.321 1.00 40.76 ?  598 MET B CE    1 
ATOM   10349 N  N     . GLU B 1 599 ? 128.583 124.567 166.344 1.00 37.86 ?  599 GLU B N     1 
ATOM   10350 C  CA    . GLU B 1 599 ? 129.168 123.453 167.071 1.00 37.80 ?  599 GLU B CA    1 
ATOM   10351 C  C     . GLU B 1 599 ? 129.908 123.991 168.284 1.00 34.97 ?  599 GLU B C     1 
ATOM   10352 O  O     . GLU B 1 599 ? 130.377 125.132 168.285 1.00 40.23 ?  599 GLU B O     1 
ATOM   10353 C  CB    . GLU B 1 599 ? 130.119 122.642 166.184 1.00 39.85 ?  599 GLU B CB    1 
ATOM   10354 C  CG    . GLU B 1 599 ? 131.117 123.493 165.422 1.00 37.81 ?  599 GLU B CG    1 
ATOM   10355 C  CD    . GLU B 1 599 ? 131.384 122.972 164.025 1.00 43.29 ?  599 GLU B CD    1 
ATOM   10356 O  OE1   . GLU B 1 599 ? 131.250 121.749 163.810 1.00 44.64 ?  599 GLU B OE1   1 
ATOM   10357 O  OE2   . GLU B 1 599 ? 131.730 123.785 163.143 1.00 43.83 -1 599 GLU B OE2   1 
ATOM   10358 N  N     . ARG B 1 600 ? 130.005 123.158 169.321 1.00 36.52 ?  600 ARG B N     1 
ATOM   10359 C  CA    . ARG B 1 600 ? 130.713 123.566 170.530 1.00 32.88 ?  600 ARG B CA    1 
ATOM   10360 C  C     . ARG B 1 600 ? 132.208 123.690 170.274 1.00 33.71 ?  600 ARG B C     1 
ATOM   10361 O  O     . ARG B 1 600 ? 132.832 124.692 170.642 1.00 39.87 ?  600 ARG B O     1 
ATOM   10362 C  CB    . ARG B 1 600 ? 130.435 122.572 171.655 1.00 35.62 ?  600 ARG B CB    1 
ATOM   10363 C  CG    . ARG B 1 600 ? 129.056 122.712 172.260 1.00 33.67 ?  600 ARG B CG    1 
ATOM   10364 C  CD    . ARG B 1 600 ? 128.927 121.891 173.521 1.00 31.09 ?  600 ARG B CD    1 
ATOM   10365 N  NE    . ARG B 1 600 ? 127.569 121.908 174.048 1.00 32.40 ?  600 ARG B NE    1 
ATOM   10366 C  CZ    . ARG B 1 600 ? 126.579 121.153 173.592 1.00 34.59 ?  600 ARG B CZ    1 
ATOM   10367 N  NH1   . ARG B 1 600 ? 126.758 120.315 172.585 1.00 33.92 1  600 ARG B NH1   1 
ATOM   10368 N  NH2   . ARG B 1 600 ? 125.381 121.243 174.161 1.00 35.08 ?  600 ARG B NH2   1 
ATOM   10369 N  N     . ILE B 1 601 ? 132.801 122.680 169.647 1.00 38.78 ?  601 ILE B N     1 
ATOM   10370 C  CA    . ILE B 1 601 ? 134.199 122.704 169.235 1.00 37.26 ?  601 ILE B CA    1 
ATOM   10371 C  C     . ILE B 1 601 ? 134.235 122.453 167.737 1.00 37.70 ?  601 ILE B C     1 
ATOM   10372 O  O     . ILE B 1 601 ? 133.729 121.428 167.262 1.00 42.98 ?  601 ILE B O     1 
ATOM   10373 C  CB    . ILE B 1 601 ? 135.041 121.662 169.987 1.00 39.69 ?  601 ILE B CB    1 
ATOM   10374 C  CG1   . ILE B 1 601 ? 134.750 121.716 171.487 1.00 40.45 ?  601 ILE B CG1   1 
ATOM   10375 C  CG2   . ILE B 1 601 ? 136.521 121.884 169.724 1.00 37.99 ?  601 ILE B CG2   1 
ATOM   10376 C  CD1   . ILE B 1 601 ? 135.374 120.585 172.272 1.00 39.25 ?  601 ILE B CD1   1 
ATOM   10377 N  N     . GLU B 1 602 ? 134.830 123.379 166.993 1.00 45.48 ?  602 GLU B N     1 
ATOM   10378 C  CA    . GLU B 1 602 ? 134.902 123.275 165.543 1.00 46.01 ?  602 GLU B CA    1 
ATOM   10379 C  C     . GLU B 1 602 ? 136.299 122.848 165.116 1.00 47.78 ?  602 GLU B C     1 
ATOM   10380 O  O     . GLU B 1 602 ? 137.299 123.423 165.553 1.00 47.96 ?  602 GLU B O     1 
ATOM   10381 C  CB    . GLU B 1 602 ? 134.537 124.602 164.877 1.00 44.80 ?  602 GLU B CB    1 
ATOM   10382 C  CG    . GLU B 1 602 ? 135.096 125.824 165.572 1.00 47.22 ?  602 GLU B CG    1 
ATOM   10383 C  CD    . GLU B 1 602 ? 135.112 127.041 164.674 1.00 50.05 ?  602 GLU B CD    1 
ATOM   10384 O  OE1   . GLU B 1 602 ? 134.026 127.591 164.394 1.00 48.81 ?  602 GLU B OE1   1 
ATOM   10385 O  OE2   . GLU B 1 602 ? 136.211 127.445 164.243 1.00 49.61 -1 602 GLU B OE2   1 
ATOM   10386 N  N     . GLU B 1 603 ? 136.361 121.835 164.256 1.00 53.84 ?  603 GLU B N     1 
ATOM   10387 C  CA    . GLU B 1 603 ? 137.620 121.318 163.732 1.00 54.70 ?  603 GLU B CA    1 
ATOM   10388 C  C     . GLU B 1 603 ? 137.843 121.913 162.348 1.00 53.81 ?  603 GLU B C     1 
ATOM   10389 O  O     . GLU B 1 603 ? 137.091 121.625 161.410 1.00 54.77 ?  603 GLU B O     1 
ATOM   10390 C  CB    . GLU B 1 603 ? 137.604 119.792 163.684 1.00 54.03 ?  603 GLU B CB    1 
ATOM   10391 C  CG    . GLU B 1 603 ? 138.872 119.173 163.122 1.00 56.11 ?  603 GLU B CG    1 
ATOM   10392 C  CD    . GLU B 1 603 ? 138.684 117.723 162.720 1.00 58.17 ?  603 GLU B CD    1 
ATOM   10393 O  OE1   . GLU B 1 603 ? 138.631 116.858 163.620 1.00 57.94 ?  603 GLU B OE1   1 
ATOM   10394 O  OE2   . GLU B 1 603 ? 138.587 117.448 161.506 1.00 56.54 -1 603 GLU B OE2   1 
ATOM   10395 N  N     . ARG B 1 604 ? 138.876 122.743 162.222 1.00 55.14 ?  604 ARG B N     1 
ATOM   10396 C  CA    . ARG B 1 604 ? 139.203 123.417 160.976 1.00 55.62 ?  604 ARG B CA    1 
ATOM   10397 C  C     . ARG B 1 604 ? 140.597 123.004 160.526 1.00 56.99 ?  604 ARG B C     1 
ATOM   10398 O  O     . ARG B 1 604 ? 141.528 122.945 161.333 1.00 58.94 ?  604 ARG B O     1 
ATOM   10399 C  CB    . ARG B 1 604 ? 139.136 124.939 161.138 1.00 57.20 ?  604 ARG B CB    1 
ATOM   10400 C  CG    . ARG B 1 604 ? 137.727 125.512 161.151 1.00 57.77 ?  604 ARG B CG    1 
ATOM   10401 C  CD    . ARG B 1 604 ? 136.838 124.844 160.116 1.00 56.81 ?  604 ARG B CD    1 
ATOM   10402 N  NE    . ARG B 1 604 ? 135.807 124.018 160.734 1.00 59.20 ?  604 ARG B NE    1 
ATOM   10403 C  CZ    . ARG B 1 604 ? 134.655 124.480 161.198 1.00 59.01 ?  604 ARG B CZ    1 
ATOM   10404 N  NH1   . ARG B 1 604 ? 134.351 125.766 161.138 1.00 56.40 1  604 ARG B NH1   1 
ATOM   10405 N  NH2   . ARG B 1 604 ? 133.785 123.629 161.735 1.00 56.67 ?  604 ARG B NH2   1 
ATOM   10406 N  N     . THR B 1 605 ? 140.741 122.727 159.235 1.00 63.74 ?  605 THR B N     1 
ATOM   10407 C  CA    . THR B 1 605 ? 142.010 122.290 158.670 1.00 64.57 ?  605 THR B CA    1 
ATOM   10408 C  C     . THR B 1 605 ? 142.726 123.489 158.057 1.00 64.75 ?  605 THR B C     1 
ATOM   10409 O  O     . THR B 1 605 ? 142.197 124.133 157.144 1.00 64.19 ?  605 THR B O     1 
ATOM   10410 C  CB    . THR B 1 605 ? 141.797 121.200 157.620 1.00 64.44 ?  605 THR B CB    1 
ATOM   10411 O  OG1   . THR B 1 605 ? 141.164 120.067 158.227 1.00 64.01 ?  605 THR B OG1   1 
ATOM   10412 C  CG2   . THR B 1 605 ? 143.128 120.772 157.024 1.00 64.39 ?  605 THR B CG2   1 
ATOM   10413 N  N     . TYR B 1 606 ? 143.920 123.782 158.563 1.00 64.82 ?  606 TYR B N     1 
ATOM   10414 C  CA    . TYR B 1 606 ? 144.769 124.840 158.030 1.00 66.48 ?  606 TYR B CA    1 
ATOM   10415 C  C     . TYR B 1 606 ? 146.092 124.227 157.598 1.00 67.41 ?  606 TYR B C     1 
ATOM   10416 O  O     . TYR B 1 606 ? 146.746 123.533 158.386 1.00 65.23 ?  606 TYR B O     1 
ATOM   10417 C  CB    . TYR B 1 606 ? 144.996 125.944 159.066 1.00 64.43 ?  606 TYR B CB    1 
ATOM   10418 C  CG    . TYR B 1 606 ? 143.721 126.611 159.530 1.00 65.10 ?  606 TYR B CG    1 
ATOM   10419 C  CD1   . TYR B 1 606 ? 143.024 127.475 158.695 1.00 64.08 ?  606 TYR B CD1   1 
ATOM   10420 C  CD2   . TYR B 1 606 ? 143.212 126.376 160.800 1.00 63.67 ?  606 TYR B CD2   1 
ATOM   10421 C  CE1   . TYR B 1 606 ? 141.859 128.086 159.112 1.00 64.22 ?  606 TYR B CE1   1 
ATOM   10422 C  CE2   . TYR B 1 606 ? 142.046 126.982 161.226 1.00 62.41 ?  606 TYR B CE2   1 
ATOM   10423 C  CZ    . TYR B 1 606 ? 141.374 127.836 160.378 1.00 65.40 ?  606 TYR B CZ    1 
ATOM   10424 O  OH    . TYR B 1 606 ? 140.212 128.443 160.798 1.00 66.17 ?  606 TYR B OH    1 
ATOM   10425 N  N     . GLY B 1 607 ? 146.481 124.485 156.353 1.00 74.58 ?  607 GLY B N     1 
ATOM   10426 C  CA    . GLY B 1 607 ? 147.657 123.829 155.807 1.00 74.32 ?  607 GLY B CA    1 
ATOM   10427 C  C     . GLY B 1 607 ? 147.474 122.325 155.827 1.00 75.00 ?  607 GLY B C     1 
ATOM   10428 O  O     . GLY B 1 607 ? 146.444 121.794 155.399 1.00 73.95 ?  607 GLY B O     1 
ATOM   10429 N  N     . ASN B 1 608 ? 148.484 121.622 156.333 1.00 78.45 ?  608 ASN B N     1 
ATOM   10430 C  CA    . ASN B 1 608 ? 148.404 120.185 156.546 1.00 78.79 ?  608 ASN B CA    1 
ATOM   10431 C  C     . ASN B 1 608 ? 148.036 119.832 157.980 1.00 78.89 ?  608 ASN B C     1 
ATOM   10432 O  O     . ASN B 1 608 ? 147.999 118.648 158.328 1.00 79.13 ?  608 ASN B O     1 
ATOM   10433 C  CB    . ASN B 1 608 ? 149.727 119.519 156.164 1.00 78.58 ?  608 ASN B CB    1 
ATOM   10434 C  CG    . ASN B 1 608 ? 149.930 119.447 154.663 1.00 79.08 ?  608 ASN B CG    1 
ATOM   10435 O  OD1   . ASN B 1 608 ? 148.987 119.615 153.890 1.00 78.71 ?  608 ASN B OD1   1 
ATOM   10436 N  ND2   . ASN B 1 608 ? 151.164 119.192 154.243 1.00 78.97 ?  608 ASN B ND2   1 
ATOM   10437 N  N     . SER B 1 609 ? 147.760 120.828 158.816 1.00 72.52 ?  609 SER B N     1 
ATOM   10438 C  CA    . SER B 1 609 ? 147.432 120.616 160.216 1.00 71.89 ?  609 SER B CA    1 
ATOM   10439 C  C     . SER B 1 609 ? 145.943 120.834 160.451 1.00 70.62 ?  609 SER B C     1 
ATOM   10440 O  O     . SER B 1 609 ? 145.244 121.447 159.641 1.00 71.68 ?  609 SER B O     1 
ATOM   10441 C  CB    . SER B 1 609 ? 148.245 121.550 161.117 1.00 69.93 ?  609 SER B CB    1 
ATOM   10442 O  OG    . SER B 1 609 ? 147.863 122.901 160.923 1.00 69.72 ?  609 SER B OG    1 
ATOM   10443 N  N     . LYS B 1 610 ? 145.464 120.312 161.575 1.00 61.32 ?  610 LYS B N     1 
ATOM   10444 C  CA    . LYS B 1 610 ? 144.084 120.488 161.998 1.00 61.43 ?  610 LYS B CA    1 
ATOM   10445 C  C     . LYS B 1 610 ? 144.059 121.133 163.376 1.00 61.84 ?  610 LYS B C     1 
ATOM   10446 O  O     . LYS B 1 610 ? 144.890 120.820 164.235 1.00 59.72 ?  610 LYS B O     1 
ATOM   10447 C  CB    . LYS B 1 610 ? 143.331 119.151 162.009 1.00 62.88 ?  610 LYS B CB    1 
ATOM   10448 C  CG    . LYS B 1 610 ? 143.813 118.152 163.047 1.00 61.41 ?  610 LYS B CG    1 
ATOM   10449 C  CD    . LYS B 1 610 ? 142.855 116.977 163.186 1.00 61.32 ?  610 LYS B CD    1 
ATOM   10450 C  CE    . LYS B 1 610 ? 142.101 116.701 161.892 1.00 61.36 ?  610 LYS B CE    1 
ATOM   10451 N  NZ    . LYS B 1 610 ? 141.114 115.598 162.046 1.00 60.10 1  610 LYS B NZ    1 
ATOM   10452 N  N     . THR B 1 611 ? 143.122 122.056 163.572 1.00 60.71 ?  611 THR B N     1 
ATOM   10453 C  CA    . THR B 1 611 ? 142.992 122.796 164.816 1.00 57.67 ?  611 THR B CA    1 
ATOM   10454 C  C     . THR B 1 611 ? 141.561 122.693 165.315 1.00 54.85 ?  611 THR B C     1 
ATOM   10455 O  O     . THR B 1 611 ? 140.621 122.551 164.528 1.00 57.03 ?  611 THR B O     1 
ATOM   10456 C  CB    . THR B 1 611 ? 143.366 124.274 164.639 1.00 58.17 ?  611 THR B CB    1 
ATOM   10457 O  OG1   . THR B 1 611 ? 142.518 124.863 163.647 1.00 58.82 ?  611 THR B OG1   1 
ATOM   10458 C  CG2   . THR B 1 611 ? 144.813 124.413 164.204 1.00 55.74 ?  611 THR B CG2   1 
ATOM   10459 N  N     . TYR B 1 612 ? 141.400 122.754 166.633 1.00 49.86 ?  612 TYR B N     1 
ATOM   10460 C  CA    . TYR B 1 612 ? 140.087 122.719 167.260 1.00 50.17 ?  612 TYR B CA    1 
ATOM   10461 C  C     . TYR B 1 612 ? 139.862 124.022 168.008 1.00 50.25 ?  612 TYR B C     1 
ATOM   10462 O  O     . TYR B 1 612 ? 140.651 124.384 168.888 1.00 51.80 ?  612 TYR B O     1 
ATOM   10463 C  CB    . TYR B 1 612 ? 139.938 121.522 168.202 1.00 52.03 ?  612 TYR B CB    1 
ATOM   10464 C  CG    . TYR B 1 612 ? 140.280 120.185 167.577 1.00 54.51 ?  612 TYR B CG    1 
ATOM   10465 C  CD1   . TYR B 1 612 ? 141.599 119.809 167.355 1.00 53.62 ?  612 TYR B CD1   1 
ATOM   10466 C  CD2   . TYR B 1 612 ? 139.275 119.315 167.178 1.00 54.03 ?  612 TYR B CD2   1 
ATOM   10467 C  CE1   . TYR B 1 612 ? 141.905 118.592 166.780 1.00 55.62 ?  612 TYR B CE1   1 
ATOM   10468 C  CE2   . TYR B 1 612 ? 139.572 118.097 166.603 1.00 54.22 ?  612 TYR B CE2   1 
ATOM   10469 C  CZ    . TYR B 1 612 ? 140.888 117.741 166.405 1.00 55.61 ?  612 TYR B CZ    1 
ATOM   10470 O  OH    . TYR B 1 612 ? 141.183 116.527 165.830 1.00 55.81 ?  612 TYR B OH    1 
ATOM   10471 N  N     . TYR B 1 613 ? 138.789 124.721 167.656 1.00 42.10 ?  613 TYR B N     1 
ATOM   10472 C  CA    . TYR B 1 613 ? 138.394 125.951 168.327 1.00 38.05 ?  613 TYR B CA    1 
ATOM   10473 C  C     . TYR B 1 613 ? 137.170 125.684 169.186 1.00 38.01 ?  613 TYR B C     1 
ATOM   10474 O  O     . TYR B 1 613 ? 136.082 125.435 168.641 1.00 36.70 ?  613 TYR B O     1 
ATOM   10475 C  CB    . TYR B 1 613 ? 138.101 127.055 167.310 1.00 38.76 ?  613 TYR B CB    1 
ATOM   10476 C  CG    . TYR B 1 613 ? 137.599 128.340 167.928 1.00 35.14 ?  613 TYR B CG    1 
ATOM   10477 C  CD1   . TYR B 1 613 ? 138.368 129.037 168.849 1.00 36.58 ?  613 TYR B CD1   1 
ATOM   10478 C  CD2   . TYR B 1 613 ? 136.358 128.859 167.588 1.00 36.96 ?  613 TYR B CD2   1 
ATOM   10479 C  CE1   . TYR B 1 613 ? 137.917 130.212 169.414 1.00 38.78 ?  613 TYR B CE1   1 
ATOM   10480 C  CE2   . TYR B 1 613 ? 135.897 130.034 168.147 1.00 39.76 ?  613 TYR B CE2   1 
ATOM   10481 C  CZ    . TYR B 1 613 ? 136.681 130.706 169.060 1.00 41.14 ?  613 TYR B CZ    1 
ATOM   10482 O  OH    . TYR B 1 613 ? 136.230 131.877 169.621 1.00 40.64 ?  613 TYR B OH    1 
ATOM   10483 N  N     . PRO B 1 614 ? 137.300 125.662 170.509 1.00 35.86 ?  614 PRO B N     1 
ATOM   10484 C  CA    . PRO B 1 614 ? 136.110 125.624 171.361 1.00 34.87 ?  614 PRO B CA    1 
ATOM   10485 C  C     . PRO B 1 614 ? 135.399 126.966 171.350 1.00 38.36 ?  614 PRO B C     1 
ATOM   10486 O  O     . PRO B 1 614 ? 136.007 128.015 171.125 1.00 39.87 ?  614 PRO B O     1 
ATOM   10487 C  CB    . PRO B 1 614 ? 136.672 125.303 172.753 1.00 33.93 ?  614 PRO B CB    1 
ATOM   10488 C  CG    . PRO B 1 614 ? 138.095 124.871 172.526 1.00 36.88 ?  614 PRO B CG    1 
ATOM   10489 C  CD    . PRO B 1 614 ? 138.542 125.575 171.291 1.00 35.12 ?  614 PRO B CD    1 
ATOM   10490 N  N     . MET B 1 615 ? 134.095 126.921 171.592 1.00 32.85 ?  615 MET B N     1 
ATOM   10491 C  CA    . MET B 1 615 ? 133.330 128.153 171.685 1.00 29.77 ?  615 MET B CA    1 
ATOM   10492 C  C     . MET B 1 615 ? 133.820 128.977 172.873 1.00 36.44 ?  615 MET B C     1 
ATOM   10493 O  O     . MET B 1 615 ? 134.243 128.411 173.888 1.00 40.66 ?  615 MET B O     1 
ATOM   10494 C  CB    . MET B 1 615 ? 131.838 127.850 171.817 1.00 30.91 ?  615 MET B CB    1 
ATOM   10495 C  CG    . MET B 1 615 ? 131.140 127.512 170.503 1.00 35.52 ?  615 MET B CG    1 
ATOM   10496 S  SD    . MET B 1 615 ? 131.786 128.374 169.050 1.00 41.17 ?  615 MET B SD    1 
ATOM   10497 C  CE    . MET B 1 615 ? 132.912 127.162 168.360 1.00 34.86 ?  615 MET B CE    1 
ATOM   10498 N  N     . PRO B 1 616 ? 133.795 130.306 172.777 1.00 37.15 ?  616 PRO B N     1 
ATOM   10499 C  CA    . PRO B 1 616 ? 134.368 131.144 173.844 1.00 33.00 ?  616 PRO B CA    1 
ATOM   10500 C  C     . PRO B 1 616 ? 133.672 130.915 175.175 1.00 35.01 ?  616 PRO B C     1 
ATOM   10501 O  O     . PRO B 1 616 ? 132.458 131.083 175.300 1.00 37.07 ?  616 PRO B O     1 
ATOM   10502 C  CB    . PRO B 1 616 ? 134.147 132.568 173.325 1.00 34.26 ?  616 PRO B CB    1 
ATOM   10503 C  CG    . PRO B 1 616 ? 133.969 132.417 171.851 1.00 33.99 ?  616 PRO B CG    1 
ATOM   10504 C  CD    . PRO B 1 616 ? 133.286 131.110 171.655 1.00 33.29 ?  616 PRO B CD    1 
ATOM   10505 N  N     . GLY B 1 617 ? 134.457 130.538 176.180 1.00 35.39 ?  617 GLY B N     1 
ATOM   10506 C  CA    . GLY B 1 617 ? 133.920 130.263 177.494 1.00 33.60 ?  617 GLY B CA    1 
ATOM   10507 C  C     . GLY B 1 617 ? 133.345 128.878 177.675 1.00 38.16 ?  617 GLY B C     1 
ATOM   10508 O  O     . GLY B 1 617 ? 132.744 128.611 178.722 1.00 41.04 ?  617 GLY B O     1 
ATOM   10509 N  N     . LEU B 1 618 ? 133.500 127.994 176.692 1.00 38.93 ?  618 LEU B N     1 
ATOM   10510 C  CA    . LEU B 1 618 ? 132.997 126.635 176.827 1.00 33.74 ?  618 LEU B CA    1 
ATOM   10511 C  C     . LEU B 1 618 ? 133.742 125.902 177.936 1.00 36.51 ?  618 LEU B C     1 
ATOM   10512 O  O     . LEU B 1 618 ? 134.968 125.981 178.042 1.00 38.95 ?  618 LEU B O     1 
ATOM   10513 C  CB    . LEU B 1 618 ? 133.140 125.882 175.504 1.00 30.87 ?  618 LEU B CB    1 
ATOM   10514 C  CG    . LEU B 1 618 ? 132.636 124.437 175.468 1.00 35.47 ?  618 LEU B CG    1 
ATOM   10515 C  CD1   . LEU B 1 618 ? 131.138 124.379 175.721 1.00 36.01 ?  618 LEU B CD1   1 
ATOM   10516 C  CD2   . LEU B 1 618 ? 132.984 123.784 174.142 1.00 35.81 ?  618 LEU B CD2   1 
ATOM   10517 N  N     . ALA B 1 619 ? 132.991 125.187 178.763 1.00 42.84 ?  619 ALA B N     1 
ATOM   10518 C  CA    . ALA B 1 619 ? 133.550 124.460 179.895 1.00 42.21 ?  619 ALA B CA    1 
ATOM   10519 C  C     . ALA B 1 619 ? 132.560 123.371 180.293 1.00 43.92 ?  619 ALA B C     1 
ATOM   10520 O  O     . ALA B 1 619 ? 131.558 123.141 179.608 1.00 49.67 ?  619 ALA B O     1 
ATOM   10521 C  CB    . ALA B 1 619 ? 133.864 125.410 181.055 1.00 41.95 ?  619 ALA B CB    1 
ATOM   10522 N  N     . SER B 1 620 ? 132.845 122.694 181.406 1.00 47.85 ?  620 SER B N     1 
ATOM   10523 C  CA    . SER B 1 620 ? 131.963 121.628 181.868 1.00 49.40 ?  620 SER B CA    1 
ATOM   10524 C  C     . SER B 1 620 ? 130.645 122.182 182.394 1.00 49.40 ?  620 SER B C     1 
ATOM   10525 O  O     . SER B 1 620 ? 129.580 121.605 182.148 1.00 51.23 ?  620 SER B O     1 
ATOM   10526 C  CB    . SER B 1 620 ? 132.663 120.801 182.945 1.00 50.49 ?  620 SER B CB    1 
ATOM   10527 O  OG    . SER B 1 620 ? 134.051 120.692 182.683 1.00 53.13 ?  620 SER B OG    1 
ATOM   10528 N  N     . ASN B 1 621 ? 130.692 123.302 183.119 1.00 47.53 ?  621 ASN B N     1 
ATOM   10529 C  CA    . ASN B 1 621 ? 129.487 123.835 183.741 1.00 49.06 ?  621 ASN B CA    1 
ATOM   10530 C  C     . ASN B 1 621 ? 128.542 124.482 182.737 1.00 50.49 ?  621 ASN B C     1 
ATOM   10531 O  O     . ASN B 1 621 ? 127.339 124.558 183.002 1.00 51.11 ?  621 ASN B O     1 
ATOM   10532 C  CB    . ASN B 1 621 ? 129.858 124.848 184.826 1.00 48.58 ?  621 ASN B CB    1 
ATOM   10533 C  CG    . ASN B 1 621 ? 130.779 125.936 184.318 1.00 51.79 ?  621 ASN B CG    1 
ATOM   10534 O  OD1   . ASN B 1 621 ? 131.574 125.716 183.404 1.00 54.59 ?  621 ASN B OD1   1 
ATOM   10535 N  ND2   . ASN B 1 621 ? 130.678 127.120 184.908 1.00 50.11 ?  621 ASN B ND2   1 
ATOM   10536 N  N     . ASN B 1 622 ? 129.051 124.944 181.595 1.00 42.43 ?  622 ASN B N     1 
ATOM   10537 C  CA    . ASN B 1 622 ? 128.224 125.580 180.576 1.00 42.64 ?  622 ASN B CA    1 
ATOM   10538 C  C     . ASN B 1 622 ? 128.257 124.806 179.261 1.00 45.50 ?  622 ASN B C     1 
ATOM   10539 O  O     . ASN B 1 622 ? 128.058 125.382 178.190 1.00 48.48 ?  622 ASN B O     1 
ATOM   10540 C  CB    . ASN B 1 622 ? 128.646 127.034 180.361 1.00 42.25 ?  622 ASN B CB    1 
ATOM   10541 C  CG    . ASN B 1 622 ? 130.101 127.174 179.943 1.00 43.85 ?  622 ASN B CG    1 
ATOM   10542 O  OD1   . ASN B 1 622 ? 130.776 126.190 179.646 1.00 45.91 ?  622 ASN B OD1   1 
ATOM   10543 N  ND2   . ASN B 1 622 ? 130.589 128.407 179.920 1.00 41.49 ?  622 ASN B ND2   1 
ATOM   10544 N  N     . TRP B 1 623 ? 128.520 123.499 179.331 1.00 40.13 ?  623 TRP B N     1 
ATOM   10545 C  CA    . TRP B 1 623 ? 128.545 122.689 178.116 1.00 38.16 ?  623 TRP B CA    1 
ATOM   10546 C  C     . TRP B 1 623 ? 127.166 122.612 177.474 1.00 39.87 ?  623 TRP B C     1 
ATOM   10547 O  O     . TRP B 1 623 ? 127.032 122.768 176.254 1.00 42.48 ?  623 TRP B O     1 
ATOM   10548 C  CB    . TRP B 1 623 ? 129.072 121.289 178.428 1.00 42.24 ?  623 TRP B CB    1 
ATOM   10549 C  CG    . TRP B 1 623 ? 128.997 120.340 177.268 1.00 40.48 ?  623 TRP B CG    1 
ATOM   10550 C  CD1   . TRP B 1 623 ? 127.938 119.553 176.920 1.00 39.05 ?  623 TRP B CD1   1 
ATOM   10551 C  CD2   . TRP B 1 623 ? 130.023 120.080 176.303 1.00 39.60 ?  623 TRP B CD2   1 
ATOM   10552 N  NE1   . TRP B 1 623 ? 128.241 118.820 175.800 1.00 40.20 ?  623 TRP B NE1   1 
ATOM   10553 C  CE2   . TRP B 1 623 ? 129.515 119.123 175.402 1.00 39.80 ?  623 TRP B CE2   1 
ATOM   10554 C  CE3   . TRP B 1 623 ? 131.321 120.562 176.114 1.00 40.04 ?  623 TRP B CE3   1 
ATOM   10555 C  CZ2   . TRP B 1 623 ? 130.259 118.643 174.327 1.00 39.15 ?  623 TRP B CZ2   1 
ATOM   10556 C  CZ3   . TRP B 1 623 ? 132.059 120.081 175.047 1.00 39.84 ?  623 TRP B CZ3   1 
ATOM   10557 C  CH2   . TRP B 1 623 ? 131.525 119.132 174.168 1.00 39.02 ?  623 TRP B CH2   1 
ATOM   10558 N  N     . PHE B 1 624 ? 126.127 122.374 178.275 1.00 44.42 ?  624 PHE B N     1 
ATOM   10559 C  CA    . PHE B 1 624 ? 124.781 122.236 177.739 1.00 44.06 ?  624 PHE B CA    1 
ATOM   10560 C  C     . PHE B 1 624 ? 124.091 123.570 177.499 1.00 41.51 ?  624 PHE B C     1 
ATOM   10561 O  O     . PHE B 1 624 ? 123.080 123.605 176.789 1.00 46.26 ?  624 PHE B O     1 
ATOM   10562 C  CB    . PHE B 1 624 ? 123.933 121.367 178.668 1.00 42.66 ?  624 PHE B CB    1 
ATOM   10563 C  CG    . PHE B 1 624 ? 124.345 119.924 178.681 1.00 44.84 ?  624 PHE B CG    1 
ATOM   10564 C  CD1   . PHE B 1 624 ? 123.932 119.067 177.674 1.00 42.91 ?  624 PHE B CD1   1 
ATOM   10565 C  CD2   . PHE B 1 624 ? 125.152 119.426 179.689 1.00 45.60 ?  624 PHE B CD2   1 
ATOM   10566 C  CE1   . PHE B 1 624 ? 124.312 117.739 177.678 1.00 42.49 ?  624 PHE B CE1   1 
ATOM   10567 C  CE2   . PHE B 1 624 ? 125.535 118.100 179.697 1.00 45.60 ?  624 PHE B CE2   1 
ATOM   10568 C  CZ    . PHE B 1 624 ? 125.114 117.255 178.690 1.00 45.64 ?  624 PHE B CZ    1 
ATOM   10569 N  N     . PHE B 1 625 ? 124.601 124.664 178.067 1.00 37.19 ?  625 PHE B N     1 
ATOM   10570 C  CA    . PHE B 1 625 ? 124.113 125.982 177.684 1.00 32.73 ?  625 PHE B CA    1 
ATOM   10571 C  C     . PHE B 1 625 ? 124.634 126.397 176.318 1.00 30.95 ?  625 PHE B C     1 
ATOM   10572 O  O     . PHE B 1 625 ? 124.007 127.228 175.652 1.00 33.43 ?  625 PHE B O     1 
ATOM   10573 C  CB    . PHE B 1 625 ? 124.499 127.019 178.738 1.00 29.88 ?  625 PHE B CB    1 
ATOM   10574 C  CG    . PHE B 1 625 ? 123.651 126.966 179.974 1.00 32.89 ?  625 PHE B CG    1 
ATOM   10575 C  CD1   . PHE B 1 625 ? 122.301 127.269 179.916 1.00 33.41 ?  625 PHE B CD1   1 
ATOM   10576 C  CD2   . PHE B 1 625 ? 124.200 126.611 181.195 1.00 33.39 ?  625 PHE B CD2   1 
ATOM   10577 C  CE1   . PHE B 1 625 ? 121.516 127.220 181.050 1.00 33.55 ?  625 PHE B CE1   1 
ATOM   10578 C  CE2   . PHE B 1 625 ? 123.419 126.561 182.332 1.00 35.07 ?  625 PHE B CE2   1 
ATOM   10579 C  CZ    . PHE B 1 625 ? 122.076 126.866 182.259 1.00 35.94 ?  625 PHE B CZ    1 
ATOM   10580 N  N     . TYR B 1 626 ? 125.759 125.835 175.887 1.00 29.75 ?  626 TYR B N     1 
ATOM   10581 C  CA    . TYR B 1 626 ? 126.268 126.033 174.531 1.00 29.27 ?  626 TYR B CA    1 
ATOM   10582 C  C     . TYR B 1 626 ? 125.641 125.036 173.564 1.00 32.33 ?  626 TYR B C     1 
ATOM   10583 O  O     . TYR B 1 626 ? 126.326 124.324 172.834 1.00 35.80 ?  626 TYR B O     1 
ATOM   10584 C  CB    . TYR B 1 626 ? 127.787 125.925 174.523 1.00 31.54 ?  626 TYR B CB    1 
ATOM   10585 C  CG    . TYR B 1 626 ? 128.487 127.259 174.576 1.00 29.75 ?  626 TYR B CG    1 
ATOM   10586 C  CD1   . TYR B 1 626 ? 128.423 128.138 173.505 1.00 33.90 ?  626 TYR B CD1   1 
ATOM   10587 C  CD2   . TYR B 1 626 ? 129.212 127.640 175.697 1.00 28.57 ?  626 TYR B CD2   1 
ATOM   10588 C  CE1   . TYR B 1 626 ? 129.060 129.360 173.547 1.00 30.73 ?  626 TYR B CE1   1 
ATOM   10589 C  CE2   . TYR B 1 626 ? 129.853 128.860 175.748 1.00 31.89 ?  626 TYR B CE2   1 
ATOM   10590 C  CZ    . TYR B 1 626 ? 129.773 129.715 174.669 1.00 33.56 ?  626 TYR B CZ    1 
ATOM   10591 O  OH    . TYR B 1 626 ? 130.408 130.933 174.711 1.00 36.80 ?  626 TYR B OH    1 
ATOM   10592 N  N     . LYS B 1 627 ? 124.311 124.985 173.568 1.00 33.36 ?  627 LYS B N     1 
ATOM   10593 C  CA    . LYS B 1 627 ? 123.589 124.059 172.710 1.00 31.32 ?  627 LYS B CA    1 
ATOM   10594 C  C     . LYS B 1 627 ? 123.848 124.380 171.243 1.00 31.42 ?  627 LYS B C     1 
ATOM   10595 O  O     . LYS B 1 627 ? 123.829 125.543 170.832 1.00 34.42 ?  627 LYS B O     1 
ATOM   10596 C  CB    . LYS B 1 627 ? 122.093 124.129 173.014 1.00 32.93 ?  627 LYS B CB    1 
ATOM   10597 C  CG    . LYS B 1 627 ? 121.246 123.103 172.290 1.00 33.39 ?  627 LYS B CG    1 
ATOM   10598 C  CD    . LYS B 1 627 ? 119.809 123.161 172.777 1.00 30.93 ?  627 LYS B CD    1 
ATOM   10599 C  CE    . LYS B 1 627 ? 118.924 122.190 172.020 1.00 36.51 ?  627 LYS B CE    1 
ATOM   10600 N  NZ    . LYS B 1 627 ? 117.497 122.324 172.426 1.00 36.73 1  627 LYS B NZ    1 
ATOM   10601 N  N     . GLU B 1 628 ? 124.100 123.339 170.456 1.00 33.49 ?  628 GLU B N     1 
ATOM   10602 C  CA    . GLU B 1 628 ? 124.361 123.532 169.039 1.00 33.47 ?  628 GLU B CA    1 
ATOM   10603 C  C     . GLU B 1 628 ? 123.091 123.968 168.318 1.00 35.41 ?  628 GLU B C     1 
ATOM   10604 O  O     . GLU B 1 628 ? 121.977 123.580 168.679 1.00 39.24 ?  628 GLU B O     1 
ATOM   10605 C  CB    . GLU B 1 628 ? 124.916 122.252 168.417 1.00 35.21 ?  628 GLU B CB    1 
ATOM   10606 C  CG    . GLU B 1 628 ? 126.338 121.938 168.849 1.00 33.53 ?  628 GLU B CG    1 
ATOM   10607 C  CD    . GLU B 1 628 ? 126.910 120.725 168.147 1.00 41.02 ?  628 GLU B CD    1 
ATOM   10608 O  OE1   . GLU B 1 628 ? 126.296 120.262 167.162 1.00 41.66 ?  628 GLU B OE1   1 
ATOM   10609 O  OE2   . GLU B 1 628 ? 127.975 120.237 168.576 1.00 38.10 -1 628 GLU B OE2   1 
ATOM   10610 N  N     . ALA B 1 629 ? 123.275 124.794 167.285 1.00 33.48 ?  629 ALA B N     1 
ATOM   10611 C  CA    . ALA B 1 629 ? 122.139 125.383 166.585 1.00 28.50 ?  629 ALA B CA    1 
ATOM   10612 C  C     . ALA B 1 629 ? 121.279 124.321 165.913 1.00 33.82 ?  629 ALA B C     1 
ATOM   10613 O  O     . ALA B 1 629 ? 120.048 124.427 165.899 1.00 41.85 ?  629 ALA B O     1 
ATOM   10614 C  CB    . ALA B 1 629 ? 122.631 126.401 165.559 1.00 29.76 ?  629 ALA B CB    1 
ATOM   10615 N  N     . TYR B 1 630 ? 121.909 123.292 165.341 1.00 39.39 ?  630 TYR B N     1 
ATOM   10616 C  CA    . TYR B 1 630 ? 121.151 122.253 164.652 1.00 37.06 ?  630 TYR B CA    1 
ATOM   10617 C  C     . TYR B 1 630 ? 120.256 121.478 165.609 1.00 39.49 ?  630 TYR B C     1 
ATOM   10618 O  O     . TYR B 1 630 ? 119.183 121.012 165.209 1.00 42.63 ?  630 TYR B O     1 
ATOM   10619 C  CB    . TYR B 1 630 ? 122.104 121.305 163.925 1.00 34.90 ?  630 TYR B CB    1 
ATOM   10620 C  CG    . TYR B 1 630 ? 122.996 121.998 162.924 1.00 37.14 ?  630 TYR B CG    1 
ATOM   10621 C  CD1   . TYR B 1 630 ? 122.517 122.356 161.671 1.00 33.86 ?  630 TYR B CD1   1 
ATOM   10622 C  CD2   . TYR B 1 630 ? 124.315 122.297 163.230 1.00 37.66 ?  630 TYR B CD2   1 
ATOM   10623 C  CE1   . TYR B 1 630 ? 123.327 122.991 160.752 1.00 37.39 ?  630 TYR B CE1   1 
ATOM   10624 C  CE2   . TYR B 1 630 ? 125.134 122.931 162.317 1.00 36.27 ?  630 TYR B CE2   1 
ATOM   10625 C  CZ    . TYR B 1 630 ? 124.634 123.276 161.080 1.00 39.87 ?  630 TYR B CZ    1 
ATOM   10626 O  OH    . TYR B 1 630 ? 125.444 123.908 160.166 1.00 43.03 ?  630 TYR B OH    1 
ATOM   10627 N  N     . ASP B 1 631 ? 120.669 121.335 166.867 1.00 36.75 ?  631 ASP B N     1 
ATOM   10628 C  CA    . ASP B 1 631 ? 119.854 120.654 167.864 1.00 32.70 ?  631 ASP B CA    1 
ATOM   10629 C  C     . ASP B 1 631 ? 118.731 121.526 168.408 1.00 37.19 ?  631 ASP B C     1 
ATOM   10630 O  O     . ASP B 1 631 ? 117.882 121.023 169.152 1.00 39.80 ?  631 ASP B O     1 
ATOM   10631 C  CB    . ASP B 1 631 ? 120.733 120.176 169.022 1.00 34.41 ?  631 ASP B CB    1 
ATOM   10632 C  CG    . ASP B 1 631 ? 121.834 119.238 168.569 1.00 41.11 ?  631 ASP B CG    1 
ATOM   10633 O  OD1   . ASP B 1 631 ? 121.562 118.360 167.725 1.00 43.19 ?  631 ASP B OD1   1 
ATOM   10634 O  OD2   . ASP B 1 631 ? 122.975 119.380 169.058 1.00 42.19 -1 631 ASP B OD2   1 
ATOM   10635 N  N     . MET B 1 632 ? 118.702 122.807 168.054 1.00 36.47 ?  632 MET B N     1 
ATOM   10636 C  CA    . MET B 1 632 ? 117.733 123.744 168.598 1.00 32.57 ?  632 MET B CA    1 
ATOM   10637 C  C     . MET B 1 632 ? 116.455 123.750 167.773 1.00 34.91 ?  632 MET B C     1 
ATOM   10638 O  O     . MET B 1 632 ? 116.453 123.417 166.584 1.00 34.50 ?  632 MET B O     1 
ATOM   10639 C  CB    . MET B 1 632 ? 118.314 125.156 168.637 1.00 31.54 ?  632 MET B CB    1 
ATOM   10640 C  CG    . MET B 1 632 ? 119.456 125.331 169.612 1.00 36.57 ?  632 MET B CG    1 
ATOM   10641 S  SD    . MET B 1 632 ? 120.083 127.015 169.626 1.00 39.71 ?  632 MET B SD    1 
ATOM   10642 C  CE    . MET B 1 632 ? 120.916 127.037 171.206 1.00 30.53 ?  632 MET B CE    1 
ATOM   10643 N  N     . ASP B 1 633 ? 115.360 124.137 168.421 1.00 33.36 ?  633 ASP B N     1 
ATOM   10644 C  CA    . ASP B 1 633 ? 114.105 124.362 167.718 1.00 26.12 ?  633 ASP B CA    1 
ATOM   10645 C  C     . ASP B 1 633 ? 114.211 125.643 166.903 1.00 31.27 ?  633 ASP B C     1 
ATOM   10646 O  O     . ASP B 1 633 ? 114.440 126.722 167.459 1.00 37.33 ?  633 ASP B O     1 
ATOM   10647 C  CB    . ASP B 1 633 ? 112.951 124.450 168.713 1.00 28.86 ?  633 ASP B CB    1 
ATOM   10648 C  CG    . ASP B 1 633 ? 111.595 124.443 168.038 1.00 36.59 ?  633 ASP B CG    1 
ATOM   10649 O  OD1   . ASP B 1 633 ? 111.537 124.219 166.811 1.00 39.85 ?  633 ASP B OD1   1 
ATOM   10650 O  OD2   . ASP B 1 633 ? 110.583 124.663 168.735 1.00 35.97 -1 633 ASP B OD2   1 
ATOM   10651 N  N     . MET B 1 634 ? 114.051 125.528 165.584 1.00 28.97 ?  634 MET B N     1 
ATOM   10652 C  CA    . MET B 1 634 ? 114.151 126.701 164.725 1.00 19.79 ?  634 MET B CA    1 
ATOM   10653 C  C     . MET B 1 634 ? 113.046 127.712 164.995 1.00 23.83 ?  634 MET B C     1 
ATOM   10654 O  O     . MET B 1 634 ? 113.219 128.893 164.684 1.00 30.66 ?  634 MET B O     1 
ATOM   10655 C  CB    . MET B 1 634 ? 114.128 126.287 163.254 1.00 24.77 ?  634 MET B CB    1 
ATOM   10656 C  CG    . MET B 1 634 ? 115.503 126.152 162.612 1.00 26.45 ?  634 MET B CG    1 
ATOM   10657 S  SD    . MET B 1 634 ? 116.679 127.417 163.135 1.00 40.68 ?  634 MET B SD    1 
ATOM   10658 C  CE    . MET B 1 634 ? 117.735 126.474 164.232 1.00 27.98 ?  634 MET B CE    1 
ATOM   10659 N  N     . PHE B 1 635 ? 111.920 127.280 165.566 1.00 22.81 ?  635 PHE B N     1 
ATOM   10660 C  CA    . PHE B 1 635 ? 110.852 128.221 165.892 1.00 23.82 ?  635 PHE B CA    1 
ATOM   10661 C  C     . PHE B 1 635 ? 111.272 129.165 167.013 1.00 20.23 ?  635 PHE B C     1 
ATOM   10662 O  O     . PHE B 1 635 ? 110.979 130.365 166.966 1.00 23.00 ?  635 PHE B O     1 
ATOM   10663 C  CB    . PHE B 1 635 ? 109.584 127.459 166.274 1.00 22.81 ?  635 PHE B CB    1 
ATOM   10664 C  CG    . PHE B 1 635 ? 108.692 127.146 165.106 1.00 23.55 ?  635 PHE B CG    1 
ATOM   10665 C  CD1   . PHE B 1 635 ? 109.229 126.700 163.910 1.00 25.61 ?  635 PHE B CD1   1 
ATOM   10666 C  CD2   . PHE B 1 635 ? 107.321 127.298 165.204 1.00 24.32 ?  635 PHE B CD2   1 
ATOM   10667 C  CE1   . PHE B 1 635 ? 108.415 126.411 162.833 1.00 22.74 ?  635 PHE B CE1   1 
ATOM   10668 C  CE2   . PHE B 1 635 ? 106.502 127.011 164.130 1.00 25.49 ?  635 PHE B CE2   1 
ATOM   10669 C  CZ    . PHE B 1 635 ? 107.050 126.567 162.943 1.00 23.57 ?  635 PHE B CZ    1 
ATOM   10670 N  N     . LYS B 1 636 ? 111.976 128.649 168.020 1.00 26.75 ?  636 LYS B N     1 
ATOM   10671 C  CA    . LYS B 1 636 ? 112.453 129.504 169.099 1.00 29.79 ?  636 LYS B CA    1 
ATOM   10672 C  C     . LYS B 1 636 ? 113.604 130.397 168.649 1.00 26.40 ?  636 LYS B C     1 
ATOM   10673 O  O     . LYS B 1 636 ? 113.732 131.529 169.131 1.00 29.33 ?  636 LYS B O     1 
ATOM   10674 C  CB    . LYS B 1 636 ? 112.865 128.647 170.296 1.00 27.22 ?  636 LYS B CB    1 
ATOM   10675 C  CG    . LYS B 1 636 ? 111.713 127.844 170.879 1.00 27.67 ?  636 LYS B CG    1 
ATOM   10676 C  CD    . LYS B 1 636 ? 112.098 127.171 172.183 1.00 33.78 ?  636 LYS B CD    1 
ATOM   10677 C  CE    . LYS B 1 636 ? 110.982 126.275 172.690 1.00 33.82 ?  636 LYS B CE    1 
ATOM   10678 N  NZ    . LYS B 1 636 ? 111.406 125.478 173.873 1.00 35.15 1  636 LYS B NZ    1 
ATOM   10679 N  N     . VAL B 1 637 ? 114.431 129.921 167.718 1.00 22.60 ?  637 VAL B N     1 
ATOM   10680 C  CA    . VAL B 1 637 ? 115.436 130.792 167.119 1.00 19.51 ?  637 VAL B CA    1 
ATOM   10681 C  C     . VAL B 1 637 ? 114.764 131.904 166.322 1.00 25.77 ?  637 VAL B C     1 
ATOM   10682 O  O     . VAL B 1 637 ? 115.215 133.055 166.337 1.00 26.46 ?  637 VAL B O     1 
ATOM   10683 C  CB    . VAL B 1 637 ? 116.406 129.972 166.250 1.00 19.65 ?  637 VAL B CB    1 
ATOM   10684 C  CG1   . VAL B 1 637 ? 117.556 130.842 165.772 1.00 20.23 ?  637 VAL B CG1   1 
ATOM   10685 C  CG2   . VAL B 1 637 ? 116.932 128.778 167.029 1.00 24.93 ?  637 VAL B CG2   1 
ATOM   10686 N  N     . VAL B 1 638 ? 113.674 131.583 165.622 1.00 20.68 ?  638 VAL B N     1 
ATOM   10687 C  CA    . VAL B 1 638 ? 112.900 132.606 164.923 1.00 20.02 ?  638 VAL B CA    1 
ATOM   10688 C  C     . VAL B 1 638 ? 112.331 133.610 165.916 1.00 20.80 ?  638 VAL B C     1 
ATOM   10689 O  O     . VAL B 1 638 ? 112.309 134.818 165.658 1.00 28.07 ?  638 VAL B O     1 
ATOM   10690 C  CB    . VAL B 1 638 ? 111.785 131.954 164.080 1.00 22.27 ?  638 VAL B CB    1 
ATOM   10691 C  CG1   . VAL B 1 638 ? 110.732 132.979 163.700 1.00 16.86 ?  638 VAL B CG1   1 
ATOM   10692 C  CG2   . VAL B 1 638 ? 112.361 131.303 162.837 1.00 18.92 ?  638 VAL B CG2   1 
ATOM   10693 N  N     . ASP B 1 639 ? 111.849 133.123 167.061 1.00 21.40 ?  639 ASP B N     1 
ATOM   10694 C  CA    . ASP B 1 639 ? 111.342 134.019 168.096 1.00 16.39 ?  639 ASP B CA    1 
ATOM   10695 C  C     . ASP B 1 639 ? 112.431 134.964 168.590 1.00 22.64 ?  639 ASP B C     1 
ATOM   10696 O  O     . ASP B 1 639 ? 112.195 136.168 168.746 1.00 31.87 ?  639 ASP B O     1 
ATOM   10697 C  CB    . ASP B 1 639 ? 110.775 133.207 169.259 1.00 20.16 ?  639 ASP B CB    1 
ATOM   10698 C  CG    . ASP B 1 639 ? 109.404 132.645 168.964 1.00 30.99 ?  639 ASP B CG    1 
ATOM   10699 O  OD1   . ASP B 1 639 ? 108.613 133.333 168.285 1.00 30.17 ?  639 ASP B OD1   1 
ATOM   10700 O  OD2   . ASP B 1 639 ? 109.113 131.517 169.412 1.00 33.70 -1 639 ASP B OD2   1 
ATOM   10701 N  N     . MET B 1 640 ? 113.631 134.434 168.835 1.00 20.10 ?  640 MET B N     1 
ATOM   10702 C  CA    . MET B 1 640 ? 114.753 135.280 169.238 1.00 16.85 ?  640 MET B CA    1 
ATOM   10703 C  C     . MET B 1 640 ? 115.077 136.320 168.174 1.00 18.80 ?  640 MET B C     1 
ATOM   10704 O  O     . MET B 1 640 ? 115.295 137.499 168.482 1.00 24.56 ?  640 MET B O     1 
ATOM   10705 C  CB    . MET B 1 640 ? 115.985 134.425 169.524 1.00 18.97 ?  640 MET B CB    1 
ATOM   10706 C  CG    . MET B 1 640 ? 117.196 135.250 169.923 1.00 23.29 ?  640 MET B CG    1 
ATOM   10707 S  SD    . MET B 1 640 ? 117.169 135.820 171.626 1.00 26.94 ?  640 MET B SD    1 
ATOM   10708 C  CE    . MET B 1 640 ? 118.072 134.496 172.408 1.00 20.08 ?  640 MET B CE    1 
ATOM   10709 N  N     . ILE B 1 641 ? 115.130 135.896 166.912 1.00 22.96 ?  641 ILE B N     1 
ATOM   10710 C  CA    . ILE B 1 641 ? 115.521 136.813 165.850 1.00 18.61 ?  641 ILE B CA    1 
ATOM   10711 C  C     . ILE B 1 641 ? 114.464 137.890 165.659 1.00 17.77 ?  641 ILE B C     1 
ATOM   10712 O  O     . ILE B 1 641 ? 114.789 139.046 165.392 1.00 25.68 ?  641 ILE B O     1 
ATOM   10713 C  CB    . ILE B 1 641 ? 115.812 136.046 164.546 1.00 23.86 ?  641 ILE B CB    1 
ATOM   10714 C  CG1   . ILE B 1 641 ? 116.964 135.064 164.758 1.00 22.05 ?  641 ILE B CG1   1 
ATOM   10715 C  CG2   . ILE B 1 641 ? 116.184 137.007 163.433 1.00 13.33 ?  641 ILE B CG2   1 
ATOM   10716 C  CD1   . ILE B 1 641 ? 118.107 135.628 165.571 1.00 20.77 ?  641 ILE B CD1   1 
ATOM   10717 N  N     . ALA B 1 642 ? 113.185 137.538 165.814 1.00 9.77  ?  642 ALA B N     1 
ATOM   10718 C  CA    . ALA B 1 642 ? 112.124 138.540 165.737 1.00 17.35 ?  642 ALA B CA    1 
ATOM   10719 C  C     . ALA B 1 642 ? 112.190 139.511 166.910 1.00 19.47 ?  642 ALA B C     1 
ATOM   10720 O  O     . ALA B 1 642 ? 111.971 140.720 166.741 1.00 29.13 ?  642 ALA B O     1 
ATOM   10721 C  CB    . ALA B 1 642 ? 110.760 137.854 165.684 1.00 23.44 ?  642 ALA B CB    1 
ATOM   10722 N  N     . THR B 1 643 ? 112.493 138.999 168.106 1.00 13.83 ?  643 THR B N     1 
ATOM   10723 C  CA    . THR B 1 643 ? 112.646 139.865 169.269 1.00 15.50 ?  643 THR B CA    1 
ATOM   10724 C  C     . THR B 1 643 ? 113.773 140.867 169.061 1.00 18.38 ?  643 THR B C     1 
ATOM   10725 O  O     . THR B 1 643 ? 113.638 142.046 169.406 1.00 22.78 ?  643 THR B O     1 
ATOM   10726 C  CB    . THR B 1 643 ? 112.902 139.020 170.517 1.00 18.85 ?  643 THR B CB    1 
ATOM   10727 O  OG1   . THR B 1 643 ? 111.815 138.108 170.711 1.00 23.42 ?  643 THR B OG1   1 
ATOM   10728 C  CG2   . THR B 1 643 ? 113.037 139.902 171.741 1.00 17.01 ?  643 THR B CG2   1 
ATOM   10729 N  N     . ILE B 1 644 ? 114.895 140.416 168.503 1.00 16.84 ?  644 ILE B N     1 
ATOM   10730 C  CA    . ILE B 1 644 ? 115.982 141.338 168.193 1.00 12.86 ?  644 ILE B CA    1 
ATOM   10731 C  C     . ILE B 1 644 ? 115.582 142.281 167.063 1.00 16.93 ?  644 ILE B C     1 
ATOM   10732 O  O     . ILE B 1 644 ? 115.894 143.477 167.092 1.00 23.05 ?  644 ILE B O     1 
ATOM   10733 C  CB    . ILE B 1 644 ? 117.265 140.559 167.853 1.00 14.99 ?  644 ILE B CB    1 
ATOM   10734 C  CG1   . ILE B 1 644 ? 117.657 139.643 169.012 1.00 15.83 ?  644 ILE B CG1   1 
ATOM   10735 C  CG2   . ILE B 1 644 ? 118.392 141.515 167.527 1.00 10.19 ?  644 ILE B CG2   1 
ATOM   10736 C  CD1   . ILE B 1 644 ? 118.705 138.623 168.645 1.00 18.65 ?  644 ILE B CD1   1 
ATOM   10737 N  N     . GLN B 1 645 ? 114.873 141.759 166.060 1.00 7.72  ?  645 GLN B N     1 
ATOM   10738 C  CA    . GLN B 1 645 ? 114.550 142.514 164.858 1.00 14.27 ?  645 GLN B CA    1 
ATOM   10739 C  C     . GLN B 1 645 ? 113.607 143.668 165.152 1.00 20.95 ?  645 GLN B C     1 
ATOM   10740 O  O     . GLN B 1 645 ? 113.644 144.690 164.457 1.00 28.01 ?  645 GLN B O     1 
ATOM   10741 C  CB    . GLN B 1 645 ? 113.932 141.577 163.820 1.00 12.79 ?  645 GLN B CB    1 
ATOM   10742 C  CG    . GLN B 1 645 ? 113.601 142.227 162.495 1.00 10.57 ?  645 GLN B CG    1 
ATOM   10743 C  CD    . GLN B 1 645 ? 114.812 142.338 161.600 1.00 15.11 ?  645 GLN B CD    1 
ATOM   10744 O  OE1   . GLN B 1 645 ? 115.511 143.346 161.612 1.00 8.69  ?  645 GLN B OE1   1 
ATOM   10745 N  NE2   . GLN B 1 645 ? 115.068 141.298 160.816 1.00 17.69 ?  645 GLN B NE2   1 
ATOM   10746 N  N     . GLN B 1 646 ? 112.756 143.524 166.167 1.00 18.85 ?  646 GLN B N     1 
ATOM   10747 C  CA    . GLN B 1 646 ? 111.854 144.616 166.513 1.00 16.53 ?  646 GLN B CA    1 
ATOM   10748 C  C     . GLN B 1 646 ? 112.606 145.878 166.927 1.00 13.75 ?  646 GLN B C     1 
ATOM   10749 O  O     . GLN B 1 646 ? 112.030 146.969 166.881 1.00 21.39 ?  646 GLN B O     1 
ATOM   10750 C  CB    . GLN B 1 646 ? 110.895 144.173 167.618 1.00 19.98 ?  646 GLN B CB    1 
ATOM   10751 C  CG    . GLN B 1 646 ? 111.454 144.281 169.017 1.00 21.39 ?  646 GLN B CG    1 
ATOM   10752 C  CD    . GLN B 1 646 ? 110.501 143.741 170.062 1.00 27.82 ?  646 GLN B CD    1 
ATOM   10753 O  OE1   . GLN B 1 646 ? 110.794 142.754 170.734 1.00 25.23 ?  646 GLN B OE1   1 
ATOM   10754 N  NE2   . GLN B 1 646 ? 109.349 144.387 170.201 1.00 27.04 ?  646 GLN B NE2   1 
ATOM   10755 N  N     . HIS B 1 647 ? 113.879 145.761 167.305 1.00 22.19 ?  647 HIS B N     1 
ATOM   10756 C  CA    . HIS B 1 647 ? 114.695 146.909 167.679 1.00 19.27 ?  647 HIS B CA    1 
ATOM   10757 C  C     . HIS B 1 647 ? 115.767 147.248 166.652 1.00 16.97 ?  647 HIS B C     1 
ATOM   10758 O  O     . HIS B 1 647 ? 116.535 148.189 166.869 1.00 22.98 ?  647 HIS B O     1 
ATOM   10759 C  CB    . HIS B 1 647 ? 115.356 146.667 169.040 1.00 13.76 ?  647 HIS B CB    1 
ATOM   10760 C  CG    . HIS B 1 647 ? 114.391 146.300 170.122 1.00 17.51 ?  647 HIS B CG    1 
ATOM   10761 N  ND1   . HIS B 1 647 ? 113.427 147.170 170.583 1.00 13.19 ?  647 HIS B ND1   1 
ATOM   10762 C  CD2   . HIS B 1 647 ? 114.242 145.159 170.834 1.00 16.95 ?  647 HIS B CD2   1 
ATOM   10763 C  CE1   . HIS B 1 647 ? 112.725 146.580 171.533 1.00 19.01 ?  647 HIS B CE1   1 
ATOM   10764 N  NE2   . HIS B 1 647 ? 113.198 145.360 171.705 1.00 21.98 ?  647 HIS B NE2   1 
ATOM   10765 N  N     . ILE B 1 648 ? 115.841 146.515 165.544 1.00 12.68 ?  648 ILE B N     1 
ATOM   10766 C  CA    . ILE B 1 648 ? 116.831 146.745 164.499 1.00 11.44 ?  648 ILE B CA    1 
ATOM   10767 C  C     . ILE B 1 648 ? 116.112 147.320 163.286 1.00 16.81 ?  648 ILE B C     1 
ATOM   10768 O  O     . ILE B 1 648 ? 115.150 146.722 162.788 1.00 27.46 ?  648 ILE B O     1 
ATOM   10769 C  CB    . ILE B 1 648 ? 117.580 145.451 164.139 1.00 13.28 ?  648 ILE B CB    1 
ATOM   10770 C  CG1   . ILE B 1 648 ? 118.230 144.843 165.384 1.00 16.65 ?  648 ILE B CG1   1 
ATOM   10771 C  CG2   . ILE B 1 648 ? 118.628 145.714 163.076 1.00 5.40  ?  648 ILE B CG2   1 
ATOM   10772 C  CD1   . ILE B 1 648 ? 119.281 145.722 166.017 1.00 8.73  ?  648 ILE B CD1   1 
ATOM   10773 N  N     . ASP B 1 649 ? 116.572 148.482 162.817 1.00 12.87 ?  649 ASP B N     1 
ATOM   10774 C  CA    . ASP B 1 649 ? 115.902 149.146 161.701 1.00 7.33  ?  649 ASP B CA    1 
ATOM   10775 C  C     . ASP B 1 649 ? 116.167 148.435 160.379 1.00 10.36 ?  649 ASP B C     1 
ATOM   10776 O  O     . ASP B 1 649 ? 115.276 148.353 159.529 1.00 29.65 ?  649 ASP B O     1 
ATOM   10777 C  CB    . ASP B 1 649 ? 116.332 150.611 161.622 1.00 16.59 ?  649 ASP B CB    1 
ATOM   10778 C  CG    . ASP B 1 649 ? 117.817 150.795 161.833 1.00 16.75 ?  649 ASP B CG    1 
ATOM   10779 O  OD1   . ASP B 1 649 ? 118.350 150.223 162.803 1.00 20.57 ?  649 ASP B OD1   1 
ATOM   10780 O  OD2   . ASP B 1 649 ? 118.448 151.515 161.037 1.00 15.48 -1 649 ASP B OD2   1 
ATOM   10781 N  N     . GLN B 1 650 ? 117.378 147.928 160.185 1.00 12.34 ?  650 GLN B N     1 
ATOM   10782 C  CA    . GLN B 1 650 ? 117.684 147.087 159.037 1.00 3.46  ?  650 GLN B CA    1 
ATOM   10783 C  C     . GLN B 1 650 ? 117.440 145.630 159.429 1.00 7.97  ?  650 GLN B C     1 
ATOM   10784 O  O     . GLN B 1 650 ? 116.813 145.352 160.453 1.00 18.13 ?  650 GLN B O     1 
ATOM   10785 C  CB    . GLN B 1 650 ? 119.110 147.351 158.553 1.00 7.16  ?  650 GLN B CB    1 
ATOM   10786 C  CG    . GLN B 1 650 ? 119.370 148.787 158.155 1.00 8.51  ?  650 GLN B CG    1 
ATOM   10787 C  CD    . GLN B 1 650 ? 120.779 148.997 157.650 1.00 13.48 ?  650 GLN B CD    1 
ATOM   10788 O  OE1   . GLN B 1 650 ? 121.120 148.588 156.543 1.00 18.42 ?  650 GLN B OE1   1 
ATOM   10789 N  NE2   . GLN B 1 650 ? 121.607 149.641 158.463 1.00 6.77  ?  650 GLN B NE2   1 
ATOM   10790 N  N     . GLY B 1 651 ? 117.912 144.686 158.620 1.00 7.27  ?  651 GLY B N     1 
ATOM   10791 C  CA    . GLY B 1 651 ? 117.667 143.284 158.873 1.00 8.37  ?  651 GLY B CA    1 
ATOM   10792 C  C     . GLY B 1 651 ? 118.768 142.615 159.673 1.00 7.98  ?  651 GLY B C     1 
ATOM   10793 O  O     . GLY B 1 651 ? 119.743 143.229 160.104 1.00 12.97 ?  651 GLY B O     1 
ATOM   10794 N  N     . ILE B 1 652 ? 118.584 141.314 159.876 1.00 12.55 ?  652 ILE B N     1 
ATOM   10795 C  CA    . ILE B 1 652 ? 119.529 140.460 160.581 1.00 11.63 ?  652 ILE B CA    1 
ATOM   10796 C  C     . ILE B 1 652 ? 119.820 139.263 159.692 1.00 14.25 ?  652 ILE B C     1 
ATOM   10797 O  O     . ILE B 1 652 ? 118.892 138.648 159.155 1.00 25.45 ?  652 ILE B O     1 
ATOM   10798 C  CB    . ILE B 1 652 ? 118.979 139.996 161.942 1.00 6.36  ?  652 ILE B CB    1 
ATOM   10799 C  CG1   . ILE B 1 652 ? 118.546 141.191 162.790 1.00 6.35  ?  652 ILE B CG1   1 
ATOM   10800 C  CG2   . ILE B 1 652 ? 120.006 139.153 162.677 1.00 10.09 ?  652 ILE B CG2   1 
ATOM   10801 C  CD1   . ILE B 1 652 ? 117.736 140.805 164.001 1.00 9.76  ?  652 ILE B CD1   1 
ATOM   10802 N  N     . SER B 1 653 ? 121.096 138.931 159.535 1.00 5.70  ?  653 SER B N     1 
ATOM   10803 C  CA    . SER B 1 653 ? 121.474 137.767 158.739 1.00 12.44 ?  653 SER B CA    1 
ATOM   10804 C  C     . SER B 1 653 ? 121.076 136.517 159.510 1.00 19.34 ?  653 SER B C     1 
ATOM   10805 O  O     . SER B 1 653 ? 121.812 136.039 160.375 1.00 23.48 ?  653 SER B O     1 
ATOM   10806 C  CB    . SER B 1 653 ? 122.966 137.782 158.436 1.00 12.43 ?  653 SER B CB    1 
ATOM   10807 O  OG    . SER B 1 653 ? 123.239 138.571 157.292 1.00 21.12 ?  653 SER B OG    1 
ATOM   10808 N  N     . PHE B 1 654 ? 119.899 135.988 159.196 1.00 19.33 ?  654 PHE B N     1 
ATOM   10809 C  CA    . PHE B 1 654 ? 119.301 134.880 159.932 1.00 12.91 ?  654 PHE B CA    1 
ATOM   10810 C  C     . PHE B 1 654 ? 119.541 133.596 159.145 1.00 16.26 ?  654 PHE B C     1 
ATOM   10811 O  O     . PHE B 1 654 ? 118.877 133.335 158.139 1.00 25.36 ?  654 PHE B O     1 
ATOM   10812 C  CB    . PHE B 1 654 ? 117.815 135.137 160.158 1.00 13.27 ?  654 PHE B CB    1 
ATOM   10813 C  CG    . PHE B 1 654 ? 117.129 134.087 160.980 1.00 16.91 ?  654 PHE B CG    1 
ATOM   10814 C  CD1   . PHE B 1 654 ? 117.849 133.245 161.809 1.00 18.96 ?  654 PHE B CD1   1 
ATOM   10815 C  CD2   . PHE B 1 654 ? 115.756 133.946 160.922 1.00 17.86 ?  654 PHE B CD2   1 
ATOM   10816 C  CE1   . PHE B 1 654 ? 117.212 132.282 162.559 1.00 19.71 ?  654 PHE B CE1   1 
ATOM   10817 C  CE2   . PHE B 1 654 ? 115.115 132.987 161.672 1.00 17.55 ?  654 PHE B CE2   1 
ATOM   10818 C  CZ    . PHE B 1 654 ? 115.843 132.154 162.492 1.00 16.60 ?  654 PHE B CZ    1 
ATOM   10819 N  N     . THR B 1 655 ? 120.488 132.792 159.615 1.00 21.60 ?  655 THR B N     1 
ATOM   10820 C  CA    . THR B 1 655 ? 120.767 131.493 159.025 1.00 22.15 ?  655 THR B CA    1 
ATOM   10821 C  C     . THR B 1 655 ? 119.911 130.434 159.708 1.00 22.47 ?  655 THR B C     1 
ATOM   10822 O  O     . THR B 1 655 ? 119.866 130.364 160.939 1.00 27.99 ?  655 THR B O     1 
ATOM   10823 C  CB    . THR B 1 655 ? 122.250 131.146 159.161 1.00 24.56 ?  655 THR B CB    1 
ATOM   10824 O  OG1   . THR B 1 655 ? 123.030 132.055 158.376 1.00 31.42 ?  655 THR B OG1   1 
ATOM   10825 C  CG2   . THR B 1 655 ? 122.516 129.724 158.692 1.00 24.12 ?  655 THR B CG2   1 
ATOM   10826 N  N     . LEU B 1 656 ? 119.225 129.626 158.908 1.00 28.74 ?  656 LEU B N     1 
ATOM   10827 C  CA    . LEU B 1 656 ? 118.462 128.499 159.423 1.00 31.33 ?  656 LEU B CA    1 
ATOM   10828 C  C     . LEU B 1 656 ? 119.381 127.293 159.550 1.00 24.98 ?  656 LEU B C     1 
ATOM   10829 O  O     . LEU B 1 656 ? 120.172 127.013 158.645 1.00 30.77 ?  656 LEU B O     1 
ATOM   10830 C  CB    . LEU B 1 656 ? 117.278 128.176 158.513 1.00 28.54 ?  656 LEU B CB    1 
ATOM   10831 C  CG    . LEU B 1 656 ? 116.191 129.248 158.444 1.00 29.96 ?  656 LEU B CG    1 
ATOM   10832 C  CD1   . LEU B 1 656 ? 115.024 128.775 157.596 1.00 27.74 ?  656 LEU B CD1   1 
ATOM   10833 C  CD2   . LEU B 1 656 ? 115.725 129.638 159.838 1.00 26.15 ?  656 LEU B CD2   1 
ATOM   10834 N  N     . PHE B 1 657 ? 119.294 126.603 160.680 1.00 25.49 ?  657 PHE B N     1 
ATOM   10835 C  CA    . PHE B 1 657 ? 120.133 125.446 160.970 1.00 29.93 ?  657 PHE B CA    1 
ATOM   10836 C  C     . PHE B 1 657 ? 119.231 124.222 161.025 1.00 34.81 ?  657 PHE B C     1 
ATOM   10837 O  O     . PHE B 1 657 ? 118.450 124.061 161.969 1.00 38.68 ?  657 PHE B O     1 
ATOM   10838 C  CB    . PHE B 1 657 ? 120.896 125.648 162.275 1.00 28.95 ?  657 PHE B CB    1 
ATOM   10839 C  CG    . PHE B 1 657 ? 121.730 126.895 162.293 1.00 33.74 ?  657 PHE B CG    1 
ATOM   10840 C  CD1   . PHE B 1 657 ? 123.001 126.902 161.747 1.00 32.30 ?  657 PHE B CD1   1 
ATOM   10841 C  CD2   . PHE B 1 657 ? 121.238 128.065 162.848 1.00 33.75 ?  657 PHE B CD2   1 
ATOM   10842 C  CE1   . PHE B 1 657 ? 123.766 128.052 161.757 1.00 32.19 ?  657 PHE B CE1   1 
ATOM   10843 C  CE2   . PHE B 1 657 ? 122.000 129.215 162.865 1.00 31.68 ?  657 PHE B CE2   1 
ATOM   10844 C  CZ    . PHE B 1 657 ? 123.266 129.209 162.318 1.00 31.73 ?  657 PHE B CZ    1 
ATOM   10845 N  N     . LEU B 1 658 ? 119.340 123.363 160.018 1.00 35.52 ?  658 LEU B N     1 
ATOM   10846 C  CA    . LEU B 1 658 ? 118.393 122.284 159.804 1.00 38.84 ?  658 LEU B CA    1 
ATOM   10847 C  C     . LEU B 1 658 ? 119.080 120.936 159.974 1.00 42.86 ?  658 LEU B C     1 
ATOM   10848 O  O     . LEU B 1 658 ? 120.290 120.806 159.767 1.00 42.45 ?  658 LEU B O     1 
ATOM   10849 C  CB    . LEU B 1 658 ? 117.782 122.375 158.405 1.00 38.92 ?  658 LEU B CB    1 
ATOM   10850 C  CG    . LEU B 1 658 ? 117.233 123.745 158.000 1.00 36.73 ?  658 LEU B CG    1 
ATOM   10851 C  CD1   . LEU B 1 658 ? 117.310 123.902 156.492 1.00 36.74 ?  658 LEU B CD1   1 
ATOM   10852 C  CD2   . LEU B 1 658 ? 115.822 123.985 158.501 1.00 34.53 ?  658 LEU B CD2   1 
ATOM   10853 N  N     . LYS B 1 659 ? 118.299 119.939 160.371 1.00 46.82 ?  659 LYS B N     1 
ATOM   10854 C  CA    . LYS B 1 659 ? 118.765 118.563 160.409 1.00 45.01 ?  659 LYS B CA    1 
ATOM   10855 C  C     . LYS B 1 659 ? 118.437 117.866 159.096 1.00 47.48 ?  659 LYS B C     1 
ATOM   10856 O  O     . LYS B 1 659 ? 117.507 118.248 158.381 1.00 49.57 ?  659 LYS B O     1 
ATOM   10857 C  CB    . LYS B 1 659 ? 118.137 117.804 161.576 1.00 45.65 ?  659 LYS B CB    1 
ATOM   10858 C  CG    . LYS B 1 659 ? 118.528 118.329 162.946 1.00 46.86 ?  659 LYS B CG    1 
ATOM   10859 C  CD    . LYS B 1 659 ? 118.015 117.417 164.048 1.00 49.12 ?  659 LYS B CD    1 
ATOM   10860 C  CE    . LYS B 1 659 ? 118.450 117.906 165.419 1.00 46.79 ?  659 LYS B CE    1 
ATOM   10861 N  NZ    . LYS B 1 659 ? 118.247 116.873 166.473 1.00 49.98 1  659 LYS B NZ    1 
ATOM   10862 N  N     . ASP B 1 660 ? 119.223 116.834 158.778 1.00 53.65 ?  660 ASP B N     1 
ATOM   10863 C  CA    . ASP B 1 660 ? 118.994 116.073 157.555 1.00 52.62 ?  660 ASP B CA    1 
ATOM   10864 C  C     . ASP B 1 660 ? 117.678 115.308 157.586 1.00 51.96 ?  660 ASP B C     1 
ATOM   10865 O  O     . ASP B 1 660 ? 117.108 115.035 156.524 1.00 51.23 ?  660 ASP B O     1 
ATOM   10866 C  CB    . ASP B 1 660 ? 120.153 115.102 157.321 1.00 53.34 ?  660 ASP B CB    1 
ATOM   10867 C  CG    . ASP B 1 660 ? 121.109 115.583 156.247 1.00 55.56 ?  660 ASP B CG    1 
ATOM   10868 O  OD1   . ASP B 1 660 ? 120.670 116.334 155.352 1.00 54.48 ?  660 ASP B OD1   1 
ATOM   10869 O  OD2   . ASP B 1 660 ? 122.300 115.211 156.299 1.00 53.90 -1 660 ASP B OD2   1 
ATOM   10870 N  N     . THR B 1 661 ? 117.182 114.960 158.775 1.00 52.85 ?  661 THR B N     1 
ATOM   10871 C  CA    . THR B 1 661 ? 115.968 114.156 158.870 1.00 52.27 ?  661 THR B CA    1 
ATOM   10872 C  C     . THR B 1 661 ? 114.737 114.943 158.436 1.00 52.80 ?  661 THR B C     1 
ATOM   10873 O  O     . THR B 1 661 ? 113.815 114.381 157.835 1.00 55.96 ?  661 THR B O     1 
ATOM   10874 C  CB    . THR B 1 661 ? 115.791 113.639 160.297 1.00 53.12 ?  661 THR B CB    1 
ATOM   10875 O  OG1   . THR B 1 661 ? 115.836 114.739 161.215 1.00 54.39 ?  661 THR B OG1   1 
ATOM   10876 C  CG2   . THR B 1 661 ? 116.892 112.650 160.645 1.00 52.13 ?  661 THR B CG2   1 
ATOM   10877 N  N     . MET B 1 662 ? 114.701 116.238 158.734 1.00 51.33 ?  662 MET B N     1 
ATOM   10878 C  CA    . MET B 1 662 ? 113.515 117.035 158.452 1.00 52.61 ?  662 MET B CA    1 
ATOM   10879 C  C     . MET B 1 662 ? 113.345 117.256 156.952 1.00 51.05 ?  662 MET B C     1 
ATOM   10880 O  O     . MET B 1 662 ? 114.306 117.222 156.179 1.00 52.14 ?  662 MET B O     1 
ATOM   10881 C  CB    . MET B 1 662 ? 113.589 118.372 159.189 1.00 51.42 ?  662 MET B CB    1 
ATOM   10882 C  CG    . MET B 1 662 ? 114.390 119.446 158.486 1.00 49.54 ?  662 MET B CG    1 
ATOM   10883 S  SD    . MET B 1 662 ? 114.415 120.968 159.446 1.00 59.95 ?  662 MET B SD    1 
ATOM   10884 C  CE    . MET B 1 662 ? 114.403 120.324 161.117 1.00 49.08 ?  662 MET B CE    1 
ATOM   10885 N  N     . THR B 1 663 ? 112.099 117.479 156.547 1.00 43.99 ?  663 THR B N     1 
ATOM   10886 C  CA    . THR B 1 663 ? 111.717 117.549 155.147 1.00 44.61 ?  663 THR B CA    1 
ATOM   10887 C  C     . THR B 1 663 ? 111.630 119.003 154.689 1.00 44.35 ?  663 THR B C     1 
ATOM   10888 O  O     . THR B 1 663 ? 111.828 119.942 155.461 1.00 47.40 ?  663 THR B O     1 
ATOM   10889 C  CB    . THR B 1 663 ? 110.385 116.830 154.927 1.00 44.65 ?  663 THR B CB    1 
ATOM   10890 O  OG1   . THR B 1 663 ? 109.360 117.482 155.686 1.00 46.81 ?  663 THR B OG1   1 
ATOM   10891 C  CG2   . THR B 1 663 ? 110.485 115.383 155.374 1.00 45.09 ?  663 THR B CG2   1 
ATOM   10892 N  N     . THR B 1 664 ? 111.329 119.185 153.399 1.00 36.56 ?  664 THR B N     1 
ATOM   10893 C  CA    . THR B 1 664 ? 111.117 120.531 152.876 1.00 37.93 ?  664 THR B CA    1 
ATOM   10894 C  C     . THR B 1 664 ? 109.873 121.170 153.477 1.00 36.91 ?  664 THR B C     1 
ATOM   10895 O  O     . THR B 1 664 ? 109.765 122.400 153.517 1.00 39.76 ?  664 THR B O     1 
ATOM   10896 C  CB    . THR B 1 664 ? 111.005 120.502 151.350 1.00 37.84 ?  664 THR B CB    1 
ATOM   10897 O  OG1   . THR B 1 664 ? 109.810 119.809 150.970 1.00 38.33 ?  664 THR B OG1   1 
ATOM   10898 C  CG2   . THR B 1 664 ? 112.210 119.804 150.740 1.00 37.08 ?  664 THR B CG2   1 
ATOM   10899 N  N     . ARG B 1 665 ? 108.923 120.355 153.939 1.00 39.50 ?  665 ARG B N     1 
ATOM   10900 C  CA    . ARG B 1 665 ? 107.748 120.891 154.617 1.00 37.27 ?  665 ARG B CA    1 
ATOM   10901 C  C     . ARG B 1 665 ? 108.129 121.560 155.930 1.00 40.60 ?  665 ARG B C     1 
ATOM   10902 O  O     . ARG B 1 665 ? 107.565 122.598 156.289 1.00 42.67 ?  665 ARG B O     1 
ATOM   10903 C  CB    . ARG B 1 665 ? 106.731 119.774 154.846 1.00 39.03 ?  665 ARG B CB    1 
ATOM   10904 C  CG    . ARG B 1 665 ? 105.405 120.211 155.447 1.00 36.25 ?  665 ARG B CG    1 
ATOM   10905 C  CD    . ARG B 1 665 ? 105.220 119.612 156.830 1.00 39.06 ?  665 ARG B CD    1 
ATOM   10906 N  NE    . ARG B 1 665 ? 103.817 119.344 157.125 1.00 42.59 ?  665 ARG B NE    1 
ATOM   10907 C  CZ    . ARG B 1 665 ? 103.199 119.711 158.239 1.00 42.49 ?  665 ARG B CZ    1 
ATOM   10908 N  NH1   . ARG B 1 665 ? 103.834 120.360 159.200 1.00 43.20 1  665 ARG B NH1   1 
ATOM   10909 N  NH2   . ARG B 1 665 ? 101.912 119.418 158.394 1.00 41.16 ?  665 ARG B NH2   1 
ATOM   10910 N  N     . ASP B 1 666 ? 109.089 120.986 156.659 1.00 40.52 ?  666 ASP B N     1 
ATOM   10911 C  CA    . ASP B 1 666 ? 109.575 121.627 157.877 1.00 36.31 ?  666 ASP B CA    1 
ATOM   10912 C  C     . ASP B 1 666 ? 110.262 122.952 157.567 1.00 40.69 ?  666 ASP B C     1 
ATOM   10913 O  O     . ASP B 1 666 ? 110.085 123.935 158.296 1.00 43.81 ?  666 ASP B O     1 
ATOM   10914 C  CB    . ASP B 1 666 ? 110.526 120.688 158.618 1.00 39.39 ?  666 ASP B CB    1 
ATOM   10915 C  CG    . ASP B 1 666 ? 109.830 119.444 159.133 1.00 46.56 ?  666 ASP B CG    1 
ATOM   10916 O  OD1   . ASP B 1 666 ? 108.771 119.581 159.782 1.00 46.49 ?  666 ASP B OD1   1 
ATOM   10917 O  OD2   . ASP B 1 666 ? 110.338 118.331 158.888 1.00 46.36 -1 666 ASP B OD2   1 
ATOM   10918 N  N     . LEU B 1 667 ? 111.049 122.996 156.491 1.00 34.44 ?  667 LEU B N     1 
ATOM   10919 C  CA    . LEU B 1 667 ? 111.686 124.246 156.086 1.00 29.98 ?  667 LEU B CA    1 
ATOM   10920 C  C     . LEU B 1 667 ? 110.648 125.295 155.707 1.00 28.63 ?  667 LEU B C     1 
ATOM   10921 O  O     . LEU B 1 667 ? 110.780 126.471 156.069 1.00 35.33 ?  667 LEU B O     1 
ATOM   10922 C  CB    . LEU B 1 667 ? 112.642 123.985 154.922 1.00 33.52 ?  667 LEU B CB    1 
ATOM   10923 C  CG    . LEU B 1 667 ? 113.576 125.119 154.504 1.00 32.74 ?  667 LEU B CG    1 
ATOM   10924 C  CD1   . LEU B 1 667 ? 114.166 125.800 155.723 1.00 34.04 ?  667 LEU B CD1   1 
ATOM   10925 C  CD2   . LEU B 1 667 ? 114.675 124.587 153.604 1.00 31.27 ?  667 LEU B CD2   1 
ATOM   10926 N  N     . ASN B 1 668 ? 109.604 124.886 154.983 1.00 29.56 ?  668 ASN B N     1 
ATOM   10927 C  CA    . ASN B 1 668 ? 108.536 125.815 154.631 1.00 24.89 ?  668 ASN B CA    1 
ATOM   10928 C  C     . ASN B 1 668 ? 107.799 126.304 155.871 1.00 26.58 ?  668 ASN B C     1 
ATOM   10929 O  O     . ASN B 1 668 ? 107.431 127.479 155.955 1.00 28.91 ?  668 ASN B O     1 
ATOM   10930 C  CB    . ASN B 1 668 ? 107.564 125.155 153.654 1.00 28.31 ?  668 ASN B CB    1 
ATOM   10931 C  CG    . ASN B 1 668 ? 107.960 125.366 152.209 1.00 32.47 ?  668 ASN B CG    1 
ATOM   10932 O  OD1   . ASN B 1 668 ? 108.593 126.364 151.866 1.00 33.33 ?  668 ASN B OD1   1 
ATOM   10933 N  ND2   . ASN B 1 668 ? 107.589 124.423 151.352 1.00 33.17 ?  668 ASN B ND2   1 
ATOM   10934 N  N     . ARG B 1 669 ? 107.570 125.416 156.842 1.00 30.84 ?  669 ARG B N     1 
ATOM   10935 C  CA    . ARG B 1 669 ? 106.929 125.827 158.086 1.00 33.19 ?  669 ARG B CA    1 
ATOM   10936 C  C     . ARG B 1 669 ? 107.785 126.831 158.841 1.00 27.48 ?  669 ARG B C     1 
ATOM   10937 O  O     . ARG B 1 669 ? 107.266 127.802 159.400 1.00 28.14 ?  669 ARG B O     1 
ATOM   10938 C  CB    . ARG B 1 669 ? 106.646 124.608 158.963 1.00 31.40 ?  669 ARG B CB    1 
ATOM   10939 C  CG    . ARG B 1 669 ? 105.179 124.254 159.077 1.00 30.10 ?  669 ARG B CG    1 
ATOM   10940 C  CD    . ARG B 1 669 ? 104.948 123.236 160.183 1.00 32.17 ?  669 ARG B CD    1 
ATOM   10941 N  NE    . ARG B 1 669 ? 104.883 123.850 161.505 1.00 31.03 ?  669 ARG B NE    1 
ATOM   10942 C  CZ    . ARG B 1 669 ? 103.872 124.587 161.947 1.00 34.14 ?  669 ARG B CZ    1 
ATOM   10943 N  NH1   . ARG B 1 669 ? 102.809 124.824 161.196 1.00 33.10 1  669 ARG B NH1   1 
ATOM   10944 N  NH2   . ARG B 1 669 ? 103.927 125.094 163.175 1.00 34.56 ?  669 ARG B NH2   1 
ATOM   10945 N  N     . ILE B 1 670 ? 109.100 126.611 158.877 1.00 24.89 ?  670 ILE B N     1 
ATOM   10946 C  CA    . ILE B 1 670 ? 109.993 127.563 159.533 1.00 28.67 ?  670 ILE B CA    1 
ATOM   10947 C  C     . ILE B 1 670 ? 109.951 128.908 158.820 1.00 27.42 ?  670 ILE B C     1 
ATOM   10948 O  O     . ILE B 1 670 ? 109.900 129.964 159.460 1.00 27.35 ?  670 ILE B O     1 
ATOM   10949 C  CB    . ILE B 1 670 ? 111.425 126.999 159.604 1.00 28.82 ?  670 ILE B CB    1 
ATOM   10950 C  CG1   . ILE B 1 670 ? 111.472 125.777 160.524 1.00 28.87 ?  670 ILE B CG1   1 
ATOM   10951 C  CG2   . ILE B 1 670 ? 112.392 128.059 160.097 1.00 26.47 ?  670 ILE B CG2   1 
ATOM   10952 C  CD1   . ILE B 1 670 ? 112.645 124.861 160.258 1.00 28.03 ?  670 ILE B CD1   1 
ATOM   10953 N  N     . ASP B 1 671 ? 109.964 128.891 157.485 1.00 27.88 ?  671 ASP B N     1 
ATOM   10954 C  CA    . ASP B 1 671 ? 109.899 130.136 156.723 1.00 21.61 ?  671 ASP B CA    1 
ATOM   10955 C  C     . ASP B 1 671 ? 108.592 130.879 156.984 1.00 22.57 ?  671 ASP B C     1 
ATOM   10956 O  O     . ASP B 1 671 ? 108.586 132.104 157.155 1.00 26.72 ?  671 ASP B O     1 
ATOM   10957 C  CB    . ASP B 1 671 ? 110.053 129.843 155.230 1.00 22.56 ?  671 ASP B CB    1 
ATOM   10958 C  CG    . ASP B 1 671 ? 111.454 129.400 154.863 1.00 32.56 ?  671 ASP B CG    1 
ATOM   10959 O  OD1   . ASP B 1 671 ? 112.401 129.735 155.603 1.00 35.53 ?  671 ASP B OD1   1 
ATOM   10960 O  OD2   . ASP B 1 671 ? 111.609 128.713 153.831 1.00 33.40 -1 671 ASP B OD2   1 
ATOM   10961 N  N     . LEU B 1 672 ? 107.475 130.152 157.019 1.00 22.25 ?  672 LEU B N     1 
ATOM   10962 C  CA    . LEU B 1 672 ? 106.183 130.787 157.244 1.00 20.71 ?  672 LEU B CA    1 
ATOM   10963 C  C     . LEU B 1 672 ? 106.045 131.300 158.670 1.00 21.52 ?  672 LEU B C     1 
ATOM   10964 O  O     . LEU B 1 672 ? 105.398 132.327 158.895 1.00 26.69 ?  672 LEU B O     1 
ATOM   10965 C  CB    . LEU B 1 672 ? 105.054 129.813 156.914 1.00 24.45 ?  672 LEU B CB    1 
ATOM   10966 C  CG    . LEU B 1 672 ? 104.967 129.397 155.445 1.00 23.66 ?  672 LEU B CG    1 
ATOM   10967 C  CD1   . LEU B 1 672 ? 104.148 128.126 155.294 1.00 22.52 ?  672 LEU B CD1   1 
ATOM   10968 C  CD2   . LEU B 1 672 ? 104.399 130.524 154.598 1.00 20.82 ?  672 LEU B CD2   1 
ATOM   10969 N  N     . TYR B 1 673 ? 106.634 130.603 159.643 1.00 21.13 ?  673 TYR B N     1 
ATOM   10970 C  CA    . TYR B 1 673 ? 106.637 131.110 161.010 1.00 18.26 ?  673 TYR B CA    1 
ATOM   10971 C  C     . TYR B 1 673 ? 107.506 132.354 161.128 1.00 19.58 ?  673 TYR B C     1 
ATOM   10972 O  O     . TYR B 1 673 ? 107.171 133.283 161.870 1.00 27.13 ?  673 TYR B O     1 
ATOM   10973 C  CB    . TYR B 1 673 ? 107.118 130.026 161.973 1.00 18.99 ?  673 TYR B CB    1 
ATOM   10974 C  CG    . TYR B 1 673 ? 107.053 130.436 163.425 1.00 23.24 ?  673 TYR B CG    1 
ATOM   10975 C  CD1   . TYR B 1 673 ? 105.839 130.728 164.029 1.00 22.65 ?  673 TYR B CD1   1 
ATOM   10976 C  CD2   . TYR B 1 673 ? 108.206 130.534 164.191 1.00 16.57 ?  673 TYR B CD2   1 
ATOM   10977 C  CE1   . TYR B 1 673 ? 105.773 131.103 165.353 1.00 18.82 ?  673 TYR B CE1   1 
ATOM   10978 C  CE2   . TYR B 1 673 ? 108.150 130.910 165.517 1.00 19.29 ?  673 TYR B CE2   1 
ATOM   10979 C  CZ    . TYR B 1 673 ? 106.932 131.192 166.092 1.00 20.46 ?  673 TYR B CZ    1 
ATOM   10980 O  OH    . TYR B 1 673 ? 106.871 131.567 167.415 1.00 28.40 ?  673 TYR B OH    1 
ATOM   10981 N  N     . ALA B 1 674 ? 108.632 132.381 160.414 1.00 18.23 ?  674 ALA B N     1 
ATOM   10982 C  CA    . ALA B 1 674 ? 109.464 133.577 160.380 1.00 14.78 ?  674 ALA B CA    1 
ATOM   10983 C  C     . ALA B 1 674 ? 108.698 134.753 159.790 1.00 19.33 ?  674 ALA B C     1 
ATOM   10984 O  O     . ALA B 1 674 ? 108.736 135.867 160.324 1.00 23.74 ?  674 ALA B O     1 
ATOM   10985 C  CB    . ALA B 1 674 ? 110.737 133.302 159.579 1.00 13.81 ?  674 ALA B CB    1 
ATOM   10986 N  N     . HIS B 1 675 ? 107.983 134.515 158.690 1.00 18.20 ?  675 HIS B N     1 
ATOM   10987 C  CA    . HIS B 1 675 ? 107.160 135.568 158.103 1.00 19.37 ?  675 HIS B CA    1 
ATOM   10988 C  C     . HIS B 1 675 ? 106.069 136.016 159.069 1.00 18.72 ?  675 HIS B C     1 
ATOM   10989 O  O     . HIS B 1 675 ? 105.776 137.213 159.176 1.00 26.02 ?  675 HIS B O     1 
ATOM   10990 C  CB    . HIS B 1 675 ? 106.548 135.082 156.791 1.00 19.31 ?  675 HIS B CB    1 
ATOM   10991 C  CG    . HIS B 1 675 ? 105.501 135.997 156.240 1.00 17.26 ?  675 HIS B CG    1 
ATOM   10992 N  ND1   . HIS B 1 675 ? 104.153 135.797 156.446 1.00 24.61 ?  675 HIS B ND1   1 
ATOM   10993 C  CD2   . HIS B 1 675 ? 105.605 137.123 155.496 1.00 13.15 ?  675 HIS B CD2   1 
ATOM   10994 C  CE1   . HIS B 1 675 ? 103.472 136.757 155.849 1.00 22.93 ?  675 HIS B CE1   1 
ATOM   10995 N  NE2   . HIS B 1 675 ? 104.329 137.575 155.266 1.00 27.16 ?  675 HIS B NE2   1 
ATOM   10996 N  N     . HIS B 1 676 ? 105.456 135.067 159.777 1.00 18.21 ?  676 HIS B N     1 
ATOM   10997 C  CA    . HIS B 1 676 ? 104.410 135.398 160.739 1.00 18.52 ?  676 HIS B CA    1 
ATOM   10998 C  C     . HIS B 1 676 ? 104.961 136.209 161.904 1.00 23.94 ?  676 HIS B C     1 
ATOM   10999 O  O     . HIS B 1 676 ? 104.301 137.131 162.396 1.00 25.31 ?  676 HIS B O     1 
ATOM   11000 C  CB    . HIS B 1 676 ? 103.746 134.116 161.241 1.00 19.23 ?  676 HIS B CB    1 
ATOM   11001 C  CG    . HIS B 1 676 ? 102.909 134.306 162.466 1.00 20.47 ?  676 HIS B CG    1 
ATOM   11002 N  ND1   . HIS B 1 676 ? 101.705 134.977 162.450 1.00 25.04 ?  676 HIS B ND1   1 
ATOM   11003 C  CD2   . HIS B 1 676 ? 103.102 133.913 163.747 1.00 21.47 ?  676 HIS B CD2   1 
ATOM   11004 C  CE1   . HIS B 1 676 ? 101.193 134.988 163.667 1.00 26.61 ?  676 HIS B CE1   1 
ATOM   11005 N  NE2   . HIS B 1 676 ? 102.022 134.349 164.473 1.00 26.42 ?  676 HIS B NE2   1 
ATOM   11006 N  N     . ARG B 1 677 ? 106.169 135.884 162.359 1.00 22.89 ?  677 ARG B N     1 
ATOM   11007 C  CA    . ARG B 1 677 ? 106.759 136.539 163.518 1.00 19.61 ?  677 ARG B CA    1 
ATOM   11008 C  C     . ARG B 1 677 ? 107.415 137.871 163.185 1.00 21.29 ?  677 ARG B C     1 
ATOM   11009 O  O     . ARG B 1 677 ? 107.932 138.530 164.093 1.00 29.33 ?  677 ARG B O     1 
ATOM   11010 C  CB    . ARG B 1 677 ? 107.784 135.614 164.178 1.00 19.71 ?  677 ARG B CB    1 
ATOM   11011 C  CG    . ARG B 1 677 ? 107.167 134.451 164.926 1.00 23.45 ?  677 ARG B CG    1 
ATOM   11012 C  CD    . ARG B 1 677 ? 106.573 134.899 166.249 1.00 21.42 ?  677 ARG B CD    1 
ATOM   11013 N  NE    . ARG B 1 677 ? 107.598 135.342 167.186 1.00 28.85 ?  677 ARG B NE    1 
ATOM   11014 C  CZ    . ARG B 1 677 ? 107.765 136.597 167.579 1.00 35.20 ?  677 ARG B CZ    1 
ATOM   11015 N  NH1   . ARG B 1 677 ? 106.984 137.570 167.136 1.00 30.86 1  677 ARG B NH1   1 
ATOM   11016 N  NH2   . ARG B 1 677 ? 108.741 136.885 168.435 1.00 26.43 ?  677 ARG B NH2   1 
ATOM   11017 N  N     . GLY B 1 678 ? 107.410 138.282 161.922 1.00 20.57 ?  678 GLY B N     1 
ATOM   11018 C  CA    . GLY B 1 678 ? 107.994 139.546 161.538 1.00 13.88 ?  678 GLY B CA    1 
ATOM   11019 C  C     . GLY B 1 678 ? 109.434 139.485 161.090 1.00 12.96 ?  678 GLY B C     1 
ATOM   11020 O  O     . GLY B 1 678 ? 110.079 140.536 161.000 1.00 18.02 ?  678 GLY B O     1 
ATOM   11021 N  N     . ILE B 1 679 ? 109.965 138.291 160.816 1.00 15.56 ?  679 ILE B N     1 
ATOM   11022 C  CA    . ILE B 1 679 ? 111.336 138.183 160.337 1.00 15.82 ?  679 ILE B CA    1 
ATOM   11023 C  C     . ILE B 1 679 ? 111.444 138.858 158.981 1.00 13.14 ?  679 ILE B C     1 
ATOM   11024 O  O     . ILE B 1 679 ? 110.636 138.610 158.077 1.00 26.35 ?  679 ILE B O     1 
ATOM   11025 C  CB    . ILE B 1 679 ? 111.769 136.711 160.266 1.00 16.76 ?  679 ILE B CB    1 
ATOM   11026 C  CG1   . ILE B 1 679 ? 111.797 136.096 161.665 1.00 11.88 ?  679 ILE B CG1   1 
ATOM   11027 C  CG2   . ILE B 1 679 ? 113.123 136.582 159.591 1.00 14.34 ?  679 ILE B CG2   1 
ATOM   11028 C  CD1   . ILE B 1 679 ? 112.735 136.780 162.603 1.00 13.38 ?  679 ILE B CD1   1 
ATOM   11029 N  N     . LYS B 1 680 ? 112.441 139.728 158.835 1.00 9.64  ?  680 LYS B N     1 
ATOM   11030 C  CA    . LYS B 1 680 ? 112.583 140.481 157.597 1.00 9.10  ?  680 LYS B CA    1 
ATOM   11031 C  C     . LYS B 1 680 ? 113.263 139.652 156.515 1.00 6.32  ?  680 LYS B C     1 
ATOM   11032 O  O     . LYS B 1 680 ? 112.779 139.583 155.381 1.00 19.51 ?  680 LYS B O     1 
ATOM   11033 C  CB    . LYS B 1 680 ? 113.361 141.768 157.861 1.00 6.44  ?  680 LYS B CB    1 
ATOM   11034 C  CG    . LYS B 1 680 ? 112.597 142.798 158.667 1.00 0.00  ?  680 LYS B CG    1 
ATOM   11035 C  CD    . LYS B 1 680 ? 113.410 144.063 158.853 1.00 8.90  ?  680 LYS B CD    1 
ATOM   11036 C  CE    . LYS B 1 680 ? 112.808 144.949 159.921 1.00 9.68  ?  680 LYS B CE    1 
ATOM   11037 N  NZ    . LYS B 1 680 ? 113.593 146.195 160.118 1.00 17.63 1  680 LYS B NZ    1 
ATOM   11038 N  N     . THR B 1 681 ? 114.382 139.014 156.846 1.00 14.09 ?  681 THR B N     1 
ATOM   11039 C  CA    . THR B 1 681 ? 115.148 138.247 155.876 1.00 7.46  ?  681 THR B CA    1 
ATOM   11040 C  C     . THR B 1 681 ? 115.612 136.941 156.499 1.00 12.18 ?  681 THR B C     1 
ATOM   11041 O  O     . THR B 1 681 ? 115.800 136.844 157.714 1.00 19.65 ?  681 THR B O     1 
ATOM   11042 C  CB    . THR B 1 681 ? 116.369 139.027 155.363 1.00 12.38 ?  681 THR B CB    1 
ATOM   11043 O  OG1   . THR B 1 681 ? 117.104 139.557 156.474 1.00 23.17 ?  681 THR B OG1   1 
ATOM   11044 C  CG2   . THR B 1 681 ? 115.942 140.168 154.458 1.00 8.64  ?  681 THR B CG2   1 
ATOM   11045 N  N     . ILE B 1 682 ? 115.798 135.936 155.648 1.00 12.38 ?  682 ILE B N     1 
ATOM   11046 C  CA    . ILE B 1 682 ? 116.375 134.655 156.032 1.00 9.09  ?  682 ILE B CA    1 
ATOM   11047 C  C     . ILE B 1 682 ? 117.625 134.440 155.190 1.00 15.98 ?  682 ILE B C     1 
ATOM   11048 O  O     . ILE B 1 682 ? 117.568 134.521 153.958 1.00 19.54 ?  682 ILE B O     1 
ATOM   11049 C  CB    . ILE B 1 682 ? 115.378 133.499 155.844 1.00 11.04 ?  682 ILE B CB    1 
ATOM   11050 C  CG1   . ILE B 1 682 ? 114.035 133.849 156.485 1.00 17.16 ?  682 ILE B CG1   1 
ATOM   11051 C  CG2   . ILE B 1 682 ? 115.931 132.231 156.447 1.00 19.66 ?  682 ILE B CG2   1 
ATOM   11052 C  CD1   . ILE B 1 682 ? 112.981 132.787 156.314 1.00 18.91 ?  682 ILE B CD1   1 
ATOM   11053 N  N     . TYR B 1 683 ? 118.752 134.181 155.854 1.00 13.01 ?  683 TYR B N     1 
ATOM   11054 C  CA    . TYR B 1 683 ? 120.033 134.149 155.148 1.00 12.37 ?  683 TYR B CA    1 
ATOM   11055 C  C     . TYR B 1 683 ? 120.290 132.797 154.488 1.00 20.43 ?  683 TYR B C     1 
ATOM   11056 O  O     . TYR B 1 683 ? 120.327 132.689 153.260 1.00 33.65 ?  683 TYR B O     1 
ATOM   11057 C  CB    . TYR B 1 683 ? 121.164 134.502 156.119 1.00 19.94 ?  683 TYR B CB    1 
ATOM   11058 C  CG    . TYR B 1 683 ? 122.518 134.676 155.469 1.00 16.76 ?  683 TYR B CG    1 
ATOM   11059 C  CD1   . TYR B 1 683 ? 122.632 134.975 154.117 1.00 10.05 ?  683 TYR B CD1   1 
ATOM   11060 C  CD2   . TYR B 1 683 ? 123.684 134.553 156.212 1.00 14.57 ?  683 TYR B CD2   1 
ATOM   11061 C  CE1   . TYR B 1 683 ? 123.864 135.137 153.524 1.00 17.35 ?  683 TYR B CE1   1 
ATOM   11062 C  CE2   . TYR B 1 683 ? 124.922 134.715 155.626 1.00 20.79 ?  683 TYR B CE2   1 
ATOM   11063 C  CZ    . TYR B 1 683 ? 125.007 135.008 154.283 1.00 21.07 ?  683 TYR B CZ    1 
ATOM   11064 O  OH    . TYR B 1 683 ? 126.239 135.171 153.696 1.00 18.47 ?  683 TYR B OH    1 
ATOM   11065 N  N     . TYR B 1 684 ? 120.446 131.749 155.287 1.00 28.72 ?  684 TYR B N     1 
ATOM   11066 C  CA    . TYR B 1 684 ? 120.909 130.476 154.762 1.00 22.47 ?  684 TYR B CA    1 
ATOM   11067 C  C     . TYR B 1 684 ? 120.120 129.338 155.384 1.00 33.54 ?  684 TYR B C     1 
ATOM   11068 O  O     . TYR B 1 684 ? 119.602 129.453 156.497 1.00 33.94 ?  684 TYR B O     1 
ATOM   11069 C  CB    . TYR B 1 684 ? 122.405 130.263 155.028 1.00 23.90 ?  684 TYR B CB    1 
ATOM   11070 C  CG    . TYR B 1 684 ? 123.298 130.617 153.863 1.00 25.15 ?  684 TYR B CG    1 
ATOM   11071 C  CD1   . TYR B 1 684 ? 123.094 130.059 152.609 1.00 28.20 ?  684 TYR B CD1   1 
ATOM   11072 C  CD2   . TYR B 1 684 ? 124.353 131.507 154.020 1.00 27.14 ?  684 TYR B CD2   1 
ATOM   11073 C  CE1   . TYR B 1 684 ? 123.911 130.381 151.543 1.00 30.33 ?  684 TYR B CE1   1 
ATOM   11074 C  CE2   . TYR B 1 684 ? 125.174 131.835 152.961 1.00 27.12 ?  684 TYR B CE2   1 
ATOM   11075 C  CZ    . TYR B 1 684 ? 124.950 131.270 151.725 1.00 30.90 ?  684 TYR B CZ    1 
ATOM   11076 O  OH    . TYR B 1 684 ? 125.769 131.596 150.669 1.00 33.34 ?  684 TYR B OH    1 
ATOM   11077 N  N     . ALA B 1 685 ? 120.038 128.241 154.646 1.00 32.23 ?  685 ALA B N     1 
ATOM   11078 C  CA    . ALA B 1 685 ? 119.496 126.983 155.140 1.00 31.89 ?  685 ALA B CA    1 
ATOM   11079 C  C     . ALA B 1 685 ? 120.655 125.990 155.159 1.00 34.11 ?  685 ALA B C     1 
ATOM   11080 O  O     . ALA B 1 685 ? 120.867 125.242 154.204 1.00 41.93 ?  685 ALA B O     1 
ATOM   11081 C  CB    . ALA B 1 685 ? 118.343 126.501 154.272 1.00 30.04 ?  685 ALA B CB    1 
ATOM   11082 N  N     . ARG B 1 686 ? 121.412 125.999 156.252 1.00 31.14 ?  686 ARG B N     1 
ATOM   11083 C  CA    . ARG B 1 686 ? 122.542 125.094 156.412 1.00 35.59 ?  686 ARG B CA    1 
ATOM   11084 C  C     . ARG B 1 686 ? 122.054 123.798 157.044 1.00 40.36 ?  686 ARG B C     1 
ATOM   11085 O  O     . ARG B 1 686 ? 121.502 123.810 158.148 1.00 39.37 ?  686 ARG B O     1 
ATOM   11086 C  CB    . ARG B 1 686 ? 123.622 125.738 157.277 1.00 35.54 ?  686 ARG B CB    1 
ATOM   11087 C  CG    . ARG B 1 686 ? 124.297 126.938 156.642 1.00 39.12 ?  686 ARG B CG    1 
ATOM   11088 C  CD    . ARG B 1 686 ? 125.441 127.442 157.506 1.00 40.12 ?  686 ARG B CD    1 
ATOM   11089 N  NE    . ARG B 1 686 ? 126.058 126.370 158.276 1.00 42.56 ?  686 ARG B NE    1 
ATOM   11090 C  CZ    . ARG B 1 686 ? 127.272 125.888 158.048 1.00 41.73 ?  686 ARG B CZ    1 
ATOM   11091 N  NH1   . ARG B 1 686 ? 128.032 126.362 157.075 1.00 40.57 1  686 ARG B NH1   1 
ATOM   11092 N  NH2   . ARG B 1 686 ? 127.736 124.906 158.816 1.00 38.17 ?  686 ARG B NH2   1 
ATOM   11093 N  N     . THR B 1 687 ? 122.263 122.683 156.351 1.00 42.20 ?  687 THR B N     1 
ATOM   11094 C  CA    . THR B 1 687 ? 121.821 121.379 156.816 1.00 45.25 ?  687 THR B CA    1 
ATOM   11095 C  C     . THR B 1 687 ? 123.004 120.608 157.384 1.00 45.70 ?  687 THR B C     1 
ATOM   11096 O  O     . THR B 1 687 ? 124.080 120.566 156.779 1.00 45.26 ?  687 THR B O     1 
ATOM   11097 C  CB    . THR B 1 687 ? 121.170 120.581 155.684 1.00 43.73 ?  687 THR B CB    1 
ATOM   11098 O  OG1   . THR B 1 687 ? 120.282 121.431 154.949 1.00 43.79 ?  687 THR B OG1   1 
ATOM   11099 C  CG2   . THR B 1 687 ? 120.382 119.412 156.250 1.00 42.22 ?  687 THR B CG2   1 
ATOM   11100 N  N     . LYS B 1 688 ? 122.798 120.004 158.548 1.00 40.87 ?  688 LYS B N     1 
ATOM   11101 C  CA    . LYS B 1 688 ? 123.858 119.268 159.227 1.00 43.33 ?  688 LYS B CA    1 
ATOM   11102 C  C     . LYS B 1 688 ? 124.157 117.953 158.515 1.00 48.17 ?  688 LYS B C     1 
ATOM   11103 O  O     . LYS B 1 688 ? 123.355 117.020 158.552 1.00 48.97 ?  688 LYS B O     1 
ATOM   11104 C  CB    . LYS B 1 688 ? 123.478 119.008 160.685 1.00 42.70 ?  688 LYS B CB    1 
ATOM   11105 C  CG    . LYS B 1 688 ? 124.559 118.318 161.496 1.00 41.41 ?  688 LYS B CG    1 
ATOM   11106 C  CD    . LYS B 1 688 ? 124.177 118.238 162.963 1.00 44.48 ?  688 LYS B CD    1 
ATOM   11107 C  CE    . LYS B 1 688 ? 125.330 117.718 163.805 1.00 46.73 ?  688 LYS B CE    1 
ATOM   11108 N  NZ    . LYS B 1 688 ? 124.980 117.669 165.251 1.00 44.27 ?  688 LYS B NZ    1 
ATOM   11109 N  N     . ASP C 2 37  ? 144.976 79.643  108.233 1.00 45.99 ?  16  ASP C N     1 
ATOM   11110 C  CA    . ASP C 2 37  ? 144.497 80.171  106.953 1.00 45.47 ?  16  ASP C CA    1 
ATOM   11111 C  C     . ASP C 2 37  ? 143.169 80.926  107.035 1.00 44.13 ?  16  ASP C C     1 
ATOM   11112 O  O     . ASP C 2 37  ? 142.720 81.495  106.038 1.00 44.46 ?  16  ASP C O     1 
ATOM   11113 C  CB    . ASP C 2 37  ? 144.366 79.032  105.939 1.00 45.90 ?  16  ASP C CB    1 
ATOM   11114 C  CG    . ASP C 2 37  ? 145.605 78.174  105.873 1.00 47.25 ?  16  ASP C CG    1 
ATOM   11115 O  OD1   . ASP C 2 37  ? 146.722 78.729  105.948 1.00 47.99 ?  16  ASP C OD1   1 
ATOM   11116 O  OD2   . ASP C 2 37  ? 145.459 76.941  105.748 1.00 49.50 -1 16  ASP C OD2   1 
ATOM   11117 N  N     . PHE C 2 38  ? 142.545 80.935  108.210 1.00 42.17 ?  17  PHE C N     1 
ATOM   11118 C  CA    . PHE C 2 38  ? 141.168 81.430  108.321 1.00 40.67 ?  17  PHE C CA    1 
ATOM   11119 C  C     . PHE C 2 38  ? 140.856 82.398  109.469 1.00 39.46 ?  17  PHE C C     1 
ATOM   11120 O  O     . PHE C 2 38  ? 139.897 83.167  109.376 1.00 39.17 ?  17  PHE C O     1 
ATOM   11121 C  CB    . PHE C 2 38  ? 140.182 80.249  108.344 1.00 40.24 ?  17  PHE C CB    1 
ATOM   11122 C  CG    . PHE C 2 38  ? 140.470 79.224  109.417 1.00 39.58 ?  17  PHE C CG    1 
ATOM   11123 C  CD1   . PHE C 2 38  ? 139.958 79.380  110.706 1.00 38.78 ?  17  PHE C CD1   1 
ATOM   11124 C  CD2   . PHE C 2 38  ? 141.240 78.095  109.135 1.00 39.43 ?  17  PHE C CD2   1 
ATOM   11125 C  CE1   . PHE C 2 38  ? 140.211 78.433  111.699 1.00 38.07 ?  17  PHE C CE1   1 
ATOM   11126 C  CE2   . PHE C 2 38  ? 141.500 77.140  110.123 1.00 39.10 ?  17  PHE C CE2   1 
ATOM   11127 C  CZ    . PHE C 2 38  ? 140.985 77.312  111.408 1.00 38.63 ?  17  PHE C CZ    1 
ATOM   11128 N  N     . THR C 2 39  ? 141.645 82.358  110.545 1.00 38.22 ?  18  THR C N     1 
ATOM   11129 C  CA    . THR C 2 39  ? 141.329 83.146  111.749 1.00 37.09 ?  18  THR C CA    1 
ATOM   11130 C  C     . THR C 2 39  ? 141.191 84.652  111.463 1.00 36.84 ?  18  THR C C     1 
ATOM   11131 O  O     . THR C 2 39  ? 140.229 85.287  111.925 1.00 36.13 ?  18  THR C O     1 
ATOM   11132 C  CB    . THR C 2 39  ? 142.292 82.853  112.936 1.00 36.59 ?  18  THR C CB    1 
ATOM   11133 O  OG1   . THR C 2 39  ? 141.974 81.573  113.489 1.00 36.50 ?  18  THR C OG1   1 
ATOM   11134 C  CG2   . THR C 2 39  ? 142.132 83.881  114.038 1.00 36.06 ?  18  THR C CG2   1 
ATOM   11135 N  N     . GLN C 2 40  ? 142.131 85.205  110.692 1.00 37.01 ?  19  GLN C N     1 
ATOM   11136 C  CA    . GLN C 2 40  ? 142.110 86.639  110.366 1.00 37.33 ?  19  GLN C CA    1 
ATOM   11137 C  C     . GLN C 2 40  ? 140.832 87.076  109.670 1.00 36.63 ?  19  GLN C C     1 
ATOM   11138 O  O     . GLN C 2 40  ? 140.272 88.121  110.000 1.00 36.10 ?  19  GLN C O     1 
ATOM   11139 C  CB    . GLN C 2 40  ? 143.325 87.058  109.538 1.00 38.24 ?  19  GLN C CB    1 
ATOM   11140 C  CG    . GLN C 2 40  ? 144.548 87.325  110.386 1.00 41.33 ?  19  GLN C CG    1 
ATOM   11141 C  CD    . GLN C 2 40  ? 145.405 88.459  109.858 1.00 45.15 ?  19  GLN C CD    1 
ATOM   11142 O  OE1   . GLN C 2 40  ? 145.513 88.668  108.643 1.00 47.33 ?  19  GLN C OE1   1 
ATOM   11143 N  NE2   . GLN C 2 40  ? 146.026 89.202  110.773 1.00 46.51 ?  19  GLN C NE2   1 
ATOM   11144 N  N     . MET C 2 41  ? 140.366 86.269  108.722 1.00 36.23 ?  20  MET C N     1 
ATOM   11145 C  CA    . MET C 2 41  ? 139.126 86.584  108.026 1.00 36.40 ?  20  MET C CA    1 
ATOM   11146 C  C     . MET C 2 41  ? 137.896 86.425  108.939 1.00 34.93 ?  20  MET C C     1 
ATOM   11147 O  O     . MET C 2 41  ? 136.945 87.196  108.828 1.00 34.20 ?  20  MET C O     1 
ATOM   11148 C  CB    . MET C 2 41  ? 139.015 85.841  106.676 1.00 37.35 ?  20  MET C CB    1 
ATOM   11149 C  CG    . MET C 2 41  ? 138.420 84.446  106.685 1.00 40.49 ?  20  MET C CG    1 
ATOM   11150 S  SD    . MET C 2 41  ? 138.175 83.845  104.983 1.00 48.68 ?  20  MET C SD    1 
ATOM   11151 C  CE    . MET C 2 41  ? 139.784 83.128  104.621 1.00 47.17 ?  20  MET C CE    1 
ATOM   11152 N  N     . PHE C 2 42  ? 137.939 85.467  109.869 1.00 33.75 ?  21  PHE C N     1 
ATOM   11153 C  CA    . PHE C 2 42  ? 136.883 85.359  110.887 1.00 32.62 ?  21  PHE C CA    1 
ATOM   11154 C  C     . PHE C 2 42  ? 136.922 86.514  111.881 1.00 32.59 ?  21  PHE C C     1 
ATOM   11155 O  O     . PHE C 2 42  ? 135.874 87.028  112.284 1.00 32.23 ?  21  PHE C O     1 
ATOM   11156 C  CB    . PHE C 2 42  ? 136.924 84.010  111.604 1.00 32.12 ?  21  PHE C CB    1 
ATOM   11157 C  CG    . PHE C 2 42  ? 136.251 82.906  110.841 1.00 31.04 ?  21  PHE C CG    1 
ATOM   11158 C  CD1   . PHE C 2 42  ? 134.916 82.587  111.086 1.00 30.75 ?  21  PHE C CD1   1 
ATOM   11159 C  CD2   . PHE C 2 42  ? 136.945 82.190  109.873 1.00 30.99 ?  21  PHE C CD2   1 
ATOM   11160 C  CE1   . PHE C 2 42  ? 134.283 81.562  110.374 1.00 30.30 ?  21  PHE C CE1   1 
ATOM   11161 C  CE2   . PHE C 2 42  ? 136.321 81.161  109.149 1.00 30.74 ?  21  PHE C CE2   1 
ATOM   11162 C  CZ    . PHE C 2 42  ? 134.989 80.848  109.402 1.00 30.48 ?  21  PHE C CZ    1 
ATOM   11163 N  N     . TYR C 2 43  ? 138.130 86.925  112.264 1.00 32.33 ?  22  TYR C N     1 
ATOM   11164 C  CA    . TYR C 2 43  ? 138.297 88.099  113.117 1.00 32.50 ?  22  TYR C CA    1 
ATOM   11165 C  C     . TYR C 2 43  ? 137.633 89.318  112.479 1.00 33.01 ?  22  TYR C C     1 
ATOM   11166 O  O     . TYR C 2 43  ? 136.832 90.001  113.122 1.00 32.50 ?  22  TYR C O     1 
ATOM   11167 C  CB    . TYR C 2 43  ? 139.780 88.380  113.428 1.00 32.53 ?  22  TYR C CB    1 
ATOM   11168 C  CG    . TYR C 2 43  ? 139.981 89.726  114.101 1.00 33.27 ?  22  TYR C CG    1 
ATOM   11169 C  CD1   . TYR C 2 43  ? 139.768 89.883  115.473 1.00 32.34 ?  22  TYR C CD1   1 
ATOM   11170 C  CD2   . TYR C 2 43  ? 140.342 90.851  113.356 1.00 33.71 ?  22  TYR C CD2   1 
ATOM   11171 C  CE1   . TYR C 2 43  ? 139.930 91.123  116.091 1.00 33.58 ?  22  TYR C CE1   1 
ATOM   11172 C  CE2   . TYR C 2 43  ? 140.502 92.100  113.959 1.00 35.12 ?  22  TYR C CE2   1 
ATOM   11173 C  CZ    . TYR C 2 43  ? 140.298 92.227  115.328 1.00 35.30 ?  22  TYR C CZ    1 
ATOM   11174 O  OH    . TYR C 2 43  ? 140.458 93.459  115.923 1.00 36.54 ?  22  TYR C OH    1 
ATOM   11175 N  N     . ASN C 2 44  ? 137.961 89.571  111.210 1.00 33.80 ?  23  ASN C N     1 
ATOM   11176 C  CA    . ASN C 2 44  ? 137.421 90.713  110.484 1.00 34.80 ?  23  ASN C CA    1 
ATOM   11177 C  C     . ASN C 2 44  ? 135.904 90.628  110.327 1.00 34.40 ?  23  ASN C C     1 
ATOM   11178 O  O     . ASN C 2 44  ? 135.207 91.621  110.507 1.00 33.99 ?  23  ASN C O     1 
ATOM   11179 C  CB    . ASN C 2 44  ? 138.104 90.875  109.116 1.00 35.46 ?  23  ASN C CB    1 
ATOM   11180 C  CG    . ASN C 2 44  ? 139.607 91.172  109.227 1.00 38.28 ?  23  ASN C CG    1 
ATOM   11181 O  OD1   . ASN C 2 44  ? 140.096 91.680  110.247 1.00 41.01 ?  23  ASN C OD1   1 
ATOM   11182 N  ND2   . ASN C 2 44  ? 140.344 90.859  108.162 1.00 39.13 ?  23  ASN C ND2   1 
ATOM   11183 N  N     . GLN C 2 45  ? 135.400 89.434  110.009 1.00 34.49 ?  24  GLN C N     1 
ATOM   11184 C  CA    . GLN C 2 45  ? 133.964 89.224  109.859 1.00 34.81 ?  24  GLN C CA    1 
ATOM   11185 C  C     . GLN C 2 45  ? 133.220 89.428  111.184 1.00 34.68 ?  24  GLN C C     1 
ATOM   11186 O  O     . GLN C 2 45  ? 132.184 90.097  111.222 1.00 34.59 ?  24  GLN C O     1 
ATOM   11187 C  CB    . GLN C 2 45  ? 133.675 87.841  109.265 1.00 34.83 ?  24  GLN C CB    1 
ATOM   11188 C  CG    . GLN C 2 45  ? 132.256 87.666  108.719 1.00 36.14 ?  24  GLN C CG    1 
ATOM   11189 C  CD    . GLN C 2 45  ? 131.917 88.626  107.575 1.00 38.04 ?  24  GLN C CD    1 
ATOM   11190 O  OE1   . GLN C 2 45  ? 132.791 89.055  106.816 1.00 38.57 ?  24  GLN C OE1   1 
ATOM   11191 N  NE2   . GLN C 2 45  ? 130.634 88.970  107.456 1.00 38.67 ?  24  GLN C NE2   1 
ATOM   11192 N  N     . ASN C 2 46  ? 133.753 88.873  112.269 1.00 34.71 ?  25  ASN C N     1 
ATOM   11193 C  CA    . ASN C 2 46  ? 133.122 89.029  113.580 1.00 34.99 ?  25  ASN C CA    1 
ATOM   11194 C  C     . ASN C 2 46  ? 133.041 90.487  114.028 1.00 35.69 ?  25  ASN C C     1 
ATOM   11195 O  O     . ASN C 2 46  ? 131.977 90.959  114.442 1.00 35.41 ?  25  ASN C O     1 
ATOM   11196 C  CB    . ASN C 2 46  ? 133.806 88.157  114.640 1.00 34.64 ?  25  ASN C CB    1 
ATOM   11197 C  CG    . ASN C 2 46  ? 133.327 86.722  114.602 1.00 34.71 ?  25  ASN C CG    1 
ATOM   11198 O  OD1   . ASN C 2 46  ? 132.396 86.359  115.316 1.00 35.68 ?  25  ASN C OD1   1 
ATOM   11199 N  ND2   . ASN C 2 46  ? 133.936 85.902  113.740 1.00 34.71 ?  25  ASN C ND2   1 
ATOM   11200 N  N     . VAL C 2 47  ? 134.151 91.212  113.920 1.00 36.69 ?  26  VAL C N     1 
ATOM   11201 C  CA    . VAL C 2 47  ? 134.165 92.606  114.366 1.00 38.00 ?  26  VAL C CA    1 
ATOM   11202 C  C     . VAL C 2 47  ? 133.329 93.529  113.470 1.00 38.90 ?  26  VAL C C     1 
ATOM   11203 O  O     . VAL C 2 47  ? 132.767 94.508  113.953 1.00 39.46 ?  26  VAL C O     1 
ATOM   11204 C  CB    . VAL C 2 47  ? 135.595 93.166  114.589 1.00 38.16 ?  26  VAL C CB    1 
ATOM   11205 C  CG1   . VAL C 2 47  ? 136.334 92.322  115.610 1.00 37.75 ?  26  VAL C CG1   1 
ATOM   11206 C  CG2   . VAL C 2 47  ? 136.374 93.258  113.278 1.00 38.81 ?  26  VAL C CG2   1 
ATOM   11207 N  N     . LYS C 2 48  ? 133.219 93.200  112.183 1.00 39.67 ?  27  LYS C N     1 
ATOM   11208 C  CA    . LYS C 2 48  ? 132.398 93.998  111.268 1.00 40.50 ?  27  LYS C CA    1 
ATOM   11209 C  C     . LYS C 2 48  ? 130.902 93.704  111.439 1.00 40.02 ?  27  LYS C C     1 
ATOM   11210 O  O     . LYS C 2 48  ? 130.052 94.459  110.964 1.00 40.55 ?  27  LYS C O     1 
ATOM   11211 C  CB    . LYS C 2 48  ? 132.840 93.811  109.804 1.00 41.23 ?  27  LYS C CB    1 
ATOM   11212 C  CG    . LYS C 2 48  ? 132.252 92.587  109.103 1.00 42.50 ?  27  LYS C CG    1 
ATOM   11213 C  CD    . LYS C 2 48  ? 132.675 92.491  107.630 1.00 44.92 ?  27  LYS C CD    1 
ATOM   11214 C  CE    . LYS C 2 48  ? 131.847 93.406  106.730 1.00 46.66 ?  27  LYS C CE    1 
ATOM   11215 N  NZ    . LYS C 2 48  ? 130.393 93.069  106.769 1.00 47.26 1  27  LYS C NZ    1 
ATOM   11216 N  N     . GLN C 2 49  ? 130.585 92.601  112.108 1.00 39.10 ?  28  GLN C N     1 
ATOM   11217 C  CA    . GLN C 2 49  ? 129.204 92.256  112.371 1.00 38.22 ?  28  GLN C CA    1 
ATOM   11218 C  C     . GLN C 2 49  ? 128.725 92.815  113.710 1.00 37.23 ?  28  GLN C C     1 
ATOM   11219 O  O     . GLN C 2 49  ? 127.565 92.618  114.066 1.00 37.40 ?  28  GLN C O     1 
ATOM   11220 C  CB    . GLN C 2 49  ? 128.986 90.735  112.292 1.00 38.69 ?  28  GLN C CB    1 
ATOM   11221 C  CG    . GLN C 2 49  ? 129.001 90.174  110.862 1.00 39.57 ?  28  GLN C CG    1 
ATOM   11222 C  CD    . GLN C 2 49  ? 128.593 88.706  110.770 1.00 41.20 ?  28  GLN C CD    1 
ATOM   11223 O  OE1   . GLN C 2 49  ? 128.638 88.116  109.690 1.00 42.94 ?  28  GLN C OE1   1 
ATOM   11224 N  NE2   . GLN C 2 49  ? 128.193 88.113  111.898 1.00 41.23 ?  28  GLN C NE2   1 
ATOM   11225 N  N     . PHE C 2 50  ? 129.599 93.523  114.434 1.00 35.83 ?  29  PHE C N     1 
ATOM   11226 C  CA    . PHE C 2 50  ? 129.250 94.027  115.770 1.00 34.51 ?  29  PHE C CA    1 
ATOM   11227 C  C     . PHE C 2 50  ? 127.969 94.866  115.782 1.00 33.81 ?  29  PHE C C     1 
ATOM   11228 O  O     . PHE C 2 50  ? 127.784 95.735  114.930 1.00 33.66 ?  29  PHE C O     1 
ATOM   11229 C  CB    . PHE C 2 50  ? 130.397 94.809  116.417 1.00 34.59 ?  29  PHE C CB    1 
ATOM   11230 C  CG    . PHE C 2 50  ? 130.076 95.312  117.813 1.00 34.59 ?  29  PHE C CG    1 
ATOM   11231 C  CD1   . PHE C 2 50  ? 130.004 94.427  118.894 1.00 34.34 ?  29  PHE C CD1   1 
ATOM   11232 C  CD2   . PHE C 2 50  ? 129.824 96.665  118.041 1.00 35.49 ?  29  PHE C CD2   1 
ATOM   11233 C  CE1   . PHE C 2 50  ? 129.700 94.884  120.185 1.00 33.88 ?  29  PHE C CE1   1 
ATOM   11234 C  CE2   . PHE C 2 50  ? 129.514 97.138  119.330 1.00 34.12 ?  29  PHE C CE2   1 
ATOM   11235 C  CZ    . PHE C 2 50  ? 129.453 96.248  120.401 1.00 33.87 ?  29  PHE C CZ    1 
ATOM   11236 N  N     . TRP C 2 51  ? 127.102 94.593  116.760 1.00 32.24 ?  30  TRP C N     1 
ATOM   11237 C  CA    . TRP C 2 51  ? 125.823 95.286  116.899 1.00 31.28 ?  30  TRP C CA    1 
ATOM   11238 C  C     . TRP C 2 51  ? 125.343 95.302  118.352 1.00 31.12 ?  30  TRP C C     1 
ATOM   11239 O  O     . TRP C 2 51  ? 125.854 94.547  119.187 1.00 30.71 ?  30  TRP C O     1 
ATOM   11240 C  CB    . TRP C 2 51  ? 124.764 94.649  115.988 1.00 30.85 ?  30  TRP C CB    1 
ATOM   11241 C  CG    . TRP C 2 51  ? 124.456 93.208  116.313 1.00 29.31 ?  30  TRP C CG    1 
ATOM   11242 C  CD1   . TRP C 2 51  ? 125.163 92.105  115.916 1.00 29.07 ?  30  TRP C CD1   1 
ATOM   11243 C  CD2   . TRP C 2 51  ? 123.377 92.722  117.117 1.00 28.33 ?  30  TRP C CD2   1 
ATOM   11244 N  NE1   . TRP C 2 51  ? 124.584 90.964  116.416 1.00 28.01 ?  30  TRP C NE1   1 
ATOM   11245 C  CE2   . TRP C 2 51  ? 123.486 91.312  117.157 1.00 27.67 ?  30  TRP C CE2   1 
ATOM   11246 C  CE3   . TRP C 2 51  ? 122.329 93.340  117.814 1.00 27.27 ?  30  TRP C CE3   1 
ATOM   11247 C  CZ2   . TRP C 2 51  ? 122.588 90.513  117.862 1.00 26.54 ?  30  TRP C CZ2   1 
ATOM   11248 C  CZ3   . TRP C 2 51  ? 121.430 92.543  118.508 1.00 27.07 ?  30  TRP C CZ3   1 
ATOM   11249 C  CH2   . TRP C 2 51  ? 121.570 91.143  118.533 1.00 26.52 ?  30  TRP C CH2   1 
ATOM   11250 N  N     . LEU C 2 52  ? 124.366 96.168  118.640 1.00 30.65 ?  31  LEU C N     1 
ATOM   11251 C  CA    . LEU C 2 52  ? 123.691 96.224  119.939 1.00 30.38 ?  31  LEU C CA    1 
ATOM   11252 C  C     . LEU C 2 52  ? 122.179 96.254  119.728 1.00 30.51 ?  31  LEU C C     1 
ATOM   11253 O  O     . LEU C 2 52  ? 121.712 96.901  118.789 1.00 30.77 ?  31  LEU C O     1 
ATOM   11254 C  CB    . LEU C 2 52  ? 124.131 97.465  120.732 1.00 30.45 ?  31  LEU C CB    1 
ATOM   11255 C  CG    . LEU C 2 52  ? 125.605 97.504  121.147 1.00 30.29 ?  31  LEU C CG    1 
ATOM   11256 C  CD1   . LEU C 2 52  ? 126.073 98.923  121.498 1.00 30.69 ?  31  LEU C CD1   1 
ATOM   11257 C  CD2   . LEU C 2 52  ? 125.883 96.517  122.292 1.00 29.91 ?  31  LEU C CD2   1 
ATOM   11258 N  N     . PRO C 2 53  ? 121.406 95.567  120.600 1.00 30.73 ?  32  PRO C N     1 
ATOM   11259 C  CA    . PRO C 2 53  ? 119.944 95.522  120.432 1.00 31.17 ?  32  PRO C CA    1 
ATOM   11260 C  C     . PRO C 2 53  ? 119.288 96.901  120.412 1.00 32.18 ?  32  PRO C C     1 
ATOM   11261 O  O     . PRO C 2 53  ? 118.264 97.083  119.733 1.00 32.66 ?  32  PRO C O     1 
ATOM   11262 C  CB    . PRO C 2 53  ? 119.465 94.728  121.653 1.00 30.99 ?  32  PRO C CB    1 
ATOM   11263 C  CG    . PRO C 2 53  ? 120.627 94.732  122.617 1.00 30.50 ?  32  PRO C CG    1 
ATOM   11264 C  CD    . PRO C 2 53  ? 121.845 94.764  121.758 1.00 30.46 ?  32  PRO C CD    1 
ATOM   11265 N  N     . GLU C 2 54  ? 119.882 97.859  121.128 1.00 32.62 ?  33  GLU C N     1 
ATOM   11266 C  CA    . GLU C 2 54  ? 119.366 99.237  121.189 1.00 33.44 ?  33  GLU C CA    1 
ATOM   11267 C  C     . GLU C 2 54  ? 119.351 99.950  119.832 1.00 33.59 ?  33  GLU C C     1 
ATOM   11268 O  O     . GLU C 2 54  ? 118.685 100.972 119.683 1.00 34.05 ?  33  GLU C O     1 
ATOM   11269 C  CB    . GLU C 2 54  ? 120.141 100.084 122.214 1.00 33.72 ?  33  GLU C CB    1 
ATOM   11270 C  CG    . GLU C 2 54  ? 119.863 99.737  123.690 1.00 34.53 ?  33  GLU C CG    1 
ATOM   11271 C  CD    . GLU C 2 54  ? 120.533 98.438  124.139 1.00 35.09 ?  33  GLU C CD    1 
ATOM   11272 O  OE1   . GLU C 2 54  ? 121.534 98.017  123.505 1.00 34.38 ?  33  GLU C OE1   1 
ATOM   11273 O  OE2   . GLU C 2 54  ? 120.055 97.837  125.128 1.00 35.53 -1 33  GLU C OE2   1 
ATOM   11274 N  N     . GLU C 2 55  ? 120.083 99.413  118.853 1.00 33.82 ?  34  GLU C N     1 
ATOM   11275 C  CA    . GLU C 2 55  ? 120.070 99.942  117.486 1.00 34.19 ?  34  GLU C CA    1 
ATOM   11276 C  C     . GLU C 2 55  ? 118.708 99.728  116.810 1.00 33.83 ?  34  GLU C C     1 
ATOM   11277 O  O     . GLU C 2 55  ? 118.376 100.416 115.846 1.00 33.93 ?  34  GLU C O     1 
ATOM   11278 C  CB    . GLU C 2 55  ? 121.167 99.293  116.623 1.00 34.52 ?  34  GLU C CB    1 
ATOM   11279 C  CG    . GLU C 2 55  ? 122.605 99.536  117.072 1.00 36.50 ?  34  GLU C CG    1 
ATOM   11280 C  CD    . GLU C 2 55  ? 123.622 99.099  116.022 1.00 40.03 ?  34  GLU C CD    1 
ATOM   11281 O  OE1   . GLU C 2 55  ? 123.921 99.892  115.101 1.00 42.43 ?  34  GLU C OE1   1 
ATOM   11282 O  OE2   . GLU C 2 55  ? 124.133 97.967  116.117 1.00 39.35 -1 34  GLU C OE2   1 
ATOM   11283 N  N     . ILE C 2 56  ? 117.951 98.751  117.309 1.00 33.31 ?  35  ILE C N     1 
ATOM   11284 C  CA    . ILE C 2 56  ? 116.647 98.367  116.764 1.00 33.14 ?  35  ILE C CA    1 
ATOM   11285 C  C     . ILE C 2 56  ? 115.547 98.828  117.727 1.00 32.58 ?  35  ILE C C     1 
ATOM   11286 O  O     . ILE C 2 56  ? 115.500 98.379  118.867 1.00 32.12 ?  35  ILE C O     1 
ATOM   11287 C  CB    . ILE C 2 56  ? 116.545 96.813  116.586 1.00 33.03 ?  35  ILE C CB    1 
ATOM   11288 C  CG1   . ILE C 2 56  ? 117.744 96.241  115.798 1.00 34.76 ?  35  ILE C CG1   1 
ATOM   11289 C  CG2   . ILE C 2 56  ? 115.204 96.401  115.965 1.00 33.61 ?  35  ILE C CG2   1 
ATOM   11290 C  CD1   . ILE C 2 56  ? 117.823 96.642  114.322 1.00 36.75 ?  35  ILE C CD1   1 
ATOM   11291 N  N     . ALA C 2 57  ? 114.678 99.729  117.275 1.00 32.36 ?  36  ALA C N     1 
ATOM   11292 C  CA    . ALA C 2 57  ? 113.537 100.164 118.086 1.00 32.17 ?  36  ALA C CA    1 
ATOM   11293 C  C     . ALA C 2 57  ? 112.434 99.101  118.049 1.00 31.76 ?  36  ALA C C     1 
ATOM   11294 O  O     . ALA C 2 57  ? 112.068 98.616  116.977 1.00 31.95 ?  36  ALA C O     1 
ATOM   11295 C  CB    . ALA C 2 57  ? 113.012 101.502 117.589 1.00 33.01 ?  36  ALA C CB    1 
ATOM   11296 N  N     . LEU C 2 58  ? 111.905 98.743  119.215 1.00 30.68 ?  37  LEU C N     1 
ATOM   11297 C  CA    . LEU C 2 58  ? 111.033 97.574  119.317 1.00 30.14 ?  37  LEU C CA    1 
ATOM   11298 C  C     . LEU C 2 58  ? 109.548 97.887  119.466 1.00 30.21 ?  37  LEU C C     1 
ATOM   11299 O  O     . LEU C 2 58  ? 108.707 96.987  119.336 1.00 29.91 ?  37  LEU C O     1 
ATOM   11300 C  CB    . LEU C 2 58  ? 111.504 96.655  120.450 1.00 29.46 ?  37  LEU C CB    1 
ATOM   11301 C  CG    . LEU C 2 58  ? 112.856 95.963  120.224 1.00 29.08 ?  37  LEU C CG    1 
ATOM   11302 C  CD1   . LEU C 2 58  ? 113.303 95.229  121.475 1.00 29.23 ?  37  LEU C CD1   1 
ATOM   11303 C  CD2   . LEU C 2 58  ? 112.801 95.004  119.036 1.00 28.84 ?  37  LEU C CD2   1 
ATOM   11304 N  N     . ASN C 2 59  ? 109.229 99.154  119.712 1.00 30.50 ?  38  ASN C N     1 
ATOM   11305 C  CA    . ASN C 2 59  ? 107.839 99.569  119.926 1.00 31.23 ?  38  ASN C CA    1 
ATOM   11306 C  C     . ASN C 2 59  ? 106.918 99.321  118.720 1.00 31.03 ?  38  ASN C C     1 
ATOM   11307 O  O     . ASN C 2 59  ? 105.703 99.246  118.874 1.00 30.82 ?  38  ASN C O     1 
ATOM   11308 C  CB    . ASN C 2 59  ? 107.761 101.025 120.425 1.00 31.98 ?  38  ASN C CB    1 
ATOM   11309 C  CG    . ASN C 2 59  ? 108.403 102.018 119.471 1.00 33.59 ?  38  ASN C CG    1 
ATOM   11310 O  OD1   . ASN C 2 59  ? 109.578 101.884 119.106 1.00 36.48 ?  38  ASN C OD1   1 
ATOM   11311 N  ND2   . ASN C 2 59  ? 107.640 103.032 119.070 1.00 34.77 ?  38  ASN C ND2   1 
ATOM   11312 N  N     . GLY C 2 60  ? 107.511 99.161  117.540 1.00 30.88 ?  39  GLY C N     1 
ATOM   11313 C  CA    . GLY C 2 60  ? 106.775 98.786  116.326 1.00 31.37 ?  39  GLY C CA    1 
ATOM   11314 C  C     . GLY C 2 60  ? 106.139 97.401  116.343 1.00 31.05 ?  39  GLY C C     1 
ATOM   11315 O  O     . GLY C 2 60  ? 105.148 97.182  115.660 1.00 31.21 ?  39  GLY C O     1 
ATOM   11316 N  N     . ASP C 2 61  ? 106.697 96.471  117.124 1.00 30.63 ?  40  ASP C N     1 
ATOM   11317 C  CA    . ASP C 2 61  ? 106.095 95.137  117.314 1.00 30.65 ?  40  ASP C CA    1 
ATOM   11318 C  C     . ASP C 2 61  ? 104.904 95.097  118.277 1.00 31.00 ?  40  ASP C C     1 
ATOM   11319 O  O     . ASP C 2 61  ? 104.245 94.061  118.384 1.00 30.91 ?  40  ASP C O     1 
ATOM   11320 C  CB    . ASP C 2 61  ? 107.133 94.130  117.823 1.00 30.00 ?  40  ASP C CB    1 
ATOM   11321 C  CG    . ASP C 2 61  ? 108.210 93.824  116.810 1.00 30.88 ?  40  ASP C CG    1 
ATOM   11322 O  OD1   . ASP C 2 61  ? 108.193 94.397  115.695 1.00 30.42 ?  40  ASP C OD1   1 
ATOM   11323 O  OD2   . ASP C 2 61  ? 109.089 93.001  117.146 1.00 31.17 -1 40  ASP C OD2   1 
ATOM   11324 N  N     . LEU C 2 62  ? 104.642 96.196  118.983 1.00 31.54 ?  41  LEU C N     1 
ATOM   11325 C  CA    . LEU C 2 62  ? 103.633 96.209  120.055 1.00 32.47 ?  41  LEU C CA    1 
ATOM   11326 C  C     . LEU C 2 62  ? 102.254 95.721  119.622 1.00 33.21 ?  41  LEU C C     1 
ATOM   11327 O  O     . LEU C 2 62  ? 101.597 94.974  120.354 1.00 32.84 ?  41  LEU C O     1 
ATOM   11328 C  CB    . LEU C 2 62  ? 103.513 97.595  120.692 1.00 33.14 ?  41  LEU C CB    1 
ATOM   11329 C  CG    . LEU C 2 62  ? 104.500 97.948  121.804 1.00 34.44 ?  41  LEU C CG    1 
ATOM   11330 C  CD1   . LEU C 2 62  ? 104.439 99.441  122.097 1.00 35.04 ?  41  LEU C CD1   1 
ATOM   11331 C  CD2   . LEU C 2 62  ? 104.213 97.127  123.067 1.00 35.52 ?  41  LEU C CD2   1 
ATOM   11332 N  N     . LEU C 2 63  ? 101.826 96.141  118.433 1.00 33.75 ?  42  LEU C N     1 
ATOM   11333 C  CA    . LEU C 2 63  ? 100.512 95.760  117.933 1.00 34.79 ?  42  LEU C CA    1 
ATOM   11334 C  C     . LEU C 2 63  ? 100.409 94.329  117.408 1.00 34.66 ?  42  LEU C C     1 
ATOM   11335 O  O     . LEU C 2 63  ? 99.457  93.634  117.755 1.00 34.67 ?  42  LEU C O     1 
ATOM   11336 C  CB    . LEU C 2 63  ? 99.986  96.767  116.907 1.00 35.27 ?  42  LEU C CB    1 
ATOM   11337 C  CG    . LEU C 2 63  ? 99.335  98.004  117.538 1.00 36.82 ?  42  LEU C CG    1 
ATOM   11338 C  CD1   . LEU C 2 63  ? 98.884  98.962  116.442 1.00 37.93 ?  42  LEU C CD1   1 
ATOM   11339 C  CD2   . LEU C 2 63  ? 98.151  97.636  118.433 1.00 37.85 ?  42  LEU C CD2   1 
ATOM   11340 N  N     . THR C 2 64  ? 101.363 93.883  116.586 1.00 34.70 ?  43  THR C N     1 
ATOM   11341 C  CA    . THR C 2 64  ? 101.328 92.487  116.119 1.00 35.10 ?  43  THR C CA    1 
ATOM   11342 C  C     . THR C 2 64  ? 101.475 91.489  117.279 1.00 34.78 ?  43  THR C C     1 
ATOM   11343 O  O     . THR C 2 64  ? 100.989 90.367  117.190 1.00 35.04 ?  43  THR C O     1 
ATOM   11344 C  CB    . THR C 2 64  ? 102.323 92.168  114.959 1.00 35.30 ?  43  THR C CB    1 
ATOM   11345 O  OG1   . THR C 2 64  ? 103.666 92.511  115.333 1.00 36.01 ?  43  THR C OG1   1 
ATOM   11346 C  CG2   . THR C 2 64  ? 101.932 92.912  113.682 1.00 35.96 ?  43  THR C CG2   1 
ATOM   11347 N  N     . TRP C 2 65  ? 102.114 91.914  118.372 1.00 34.63 ?  44  TRP C N     1 
ATOM   11348 C  CA    . TRP C 2 65  ? 102.223 91.091  119.583 1.00 34.37 ?  44  TRP C CA    1 
ATOM   11349 C  C     . TRP C 2 65  ? 100.885 91.000  120.315 1.00 35.13 ?  44  TRP C C     1 
ATOM   11350 O  O     . TRP C 2 65  ? 100.422 89.907  120.666 1.00 34.98 ?  44  TRP C O     1 
ATOM   11351 C  CB    . TRP C 2 65  ? 103.290 91.655  120.520 1.00 33.95 ?  44  TRP C CB    1 
ATOM   11352 C  CG    . TRP C 2 65  ? 103.321 91.005  121.866 1.00 33.26 ?  44  TRP C CG    1 
ATOM   11353 C  CD1   . TRP C 2 65  ? 102.830 91.513  123.037 1.00 32.51 ?  44  TRP C CD1   1 
ATOM   11354 C  CD2   . TRP C 2 65  ? 103.878 89.723  122.186 1.00 30.93 ?  44  TRP C CD2   1 
ATOM   11355 N  NE1   . TRP C 2 65  ? 103.053 90.627  124.069 1.00 31.66 ?  44  TRP C NE1   1 
ATOM   11356 C  CE2   . TRP C 2 65  ? 103.693 89.520  123.574 1.00 30.39 ?  44  TRP C CE2   1 
ATOM   11357 C  CE3   . TRP C 2 65  ? 104.520 88.728  121.435 1.00 30.36 ?  44  TRP C CE3   1 
ATOM   11358 C  CZ2   . TRP C 2 65  ? 104.117 88.359  124.225 1.00 29.16 ?  44  TRP C CZ2   1 
ATOM   11359 C  CZ3   . TRP C 2 65  ? 104.948 87.569  122.085 1.00 28.84 ?  44  TRP C CZ3   1 
ATOM   11360 C  CH2   . TRP C 2 65  ? 104.749 87.400  123.466 1.00 29.34 ?  44  TRP C CH2   1 
ATOM   11361 N  N     . LYS C 2 66  ? 100.284 92.164  120.552 1.00 35.69 ?  45  LYS C N     1 
ATOM   11362 C  CA    . LYS C 2 66  ? 98.967  92.269  121.163 1.00 36.38 ?  45  LYS C CA    1 
ATOM   11363 C  C     . LYS C 2 66  ? 97.936  91.365  120.477 1.00 36.24 ?  45  LYS C C     1 
ATOM   11364 O  O     . LYS C 2 66  ? 97.056  90.831  121.142 1.00 36.78 ?  45  LYS C O     1 
ATOM   11365 C  CB    . LYS C 2 66  ? 98.507  93.727  121.106 1.00 37.14 ?  45  LYS C CB    1 
ATOM   11366 C  CG    . LYS C 2 66  ? 97.162  94.016  121.749 1.00 38.91 ?  45  LYS C CG    1 
ATOM   11367 C  CD    . LYS C 2 66  ? 96.702  95.434  121.408 1.00 41.12 ?  45  LYS C CD    1 
ATOM   11368 C  CE    . LYS C 2 66  ? 95.554  95.870  122.303 1.00 43.00 ?  45  LYS C CE    1 
ATOM   11369 N  NZ    . LYS C 2 66  ? 95.858  95.618  123.745 1.00 44.38 1  45  LYS C NZ    1 
ATOM   11370 N  N     . TYR C 2 67  ? 98.089  91.176  119.163 1.00 36.03 ?  46  TYR C N     1 
ATOM   11371 C  CA    . TYR C 2 67  ? 97.126  90.461  118.309 1.00 36.03 ?  46  TYR C CA    1 
ATOM   11372 C  C     . TYR C 2 67  ? 97.277  88.934  118.287 1.00 35.25 ?  46  TYR C C     1 
ATOM   11373 O  O     . TYR C 2 67  ? 96.406  88.227  117.771 1.00 35.32 ?  46  TYR C O     1 
ATOM   11374 C  CB    . TYR C 2 67  ? 97.210  90.973  116.860 1.00 36.60 ?  46  TYR C CB    1 
ATOM   11375 C  CG    . TYR C 2 67  ? 96.864  92.443  116.659 1.00 37.85 ?  46  TYR C CG    1 
ATOM   11376 C  CD1   . TYR C 2 67  ? 96.214  93.174  117.653 1.00 38.97 ?  46  TYR C CD1   1 
ATOM   11377 C  CD2   . TYR C 2 67  ? 97.176  93.095  115.457 1.00 40.06 ?  46  TYR C CD2   1 
ATOM   11378 C  CE1   . TYR C 2 67  ? 95.902  94.521  117.477 1.00 40.36 ?  46  TYR C CE1   1 
ATOM   11379 C  CE2   . TYR C 2 67  ? 96.861  94.450  115.266 1.00 40.53 ?  46  TYR C CE2   1 
ATOM   11380 C  CZ    . TYR C 2 67  ? 96.220  95.153  116.286 1.00 41.43 ?  46  TYR C CZ    1 
ATOM   11381 O  OH    . TYR C 2 67  ? 95.887  96.487  116.129 1.00 41.48 ?  46  TYR C OH    1 
ATOM   11382 N  N     . LEU C 2 68  ? 98.387  88.431  118.819 1.00 33.80 ?  47  LEU C N     1 
ATOM   11383 C  CA    . LEU C 2 68  ? 98.615  86.991  118.871 1.00 32.77 ?  47  LEU C CA    1 
ATOM   11384 C  C     . LEU C 2 68  ? 97.749  86.358  119.952 1.00 31.84 ?  47  LEU C C     1 
ATOM   11385 O  O     . LEU C 2 68  ? 97.450  86.991  120.962 1.00 31.90 ?  47  LEU C O     1 
ATOM   11386 C  CB    . LEU C 2 68  ? 100.087 86.682  119.156 1.00 32.39 ?  47  LEU C CB    1 
ATOM   11387 C  CG    . LEU C 2 68  ? 101.189 87.068  118.167 1.00 32.68 ?  47  LEU C CG    1 
ATOM   11388 C  CD1   . LEU C 2 68  ? 102.541 86.645  118.731 1.00 33.03 ?  47  LEU C CD1   1 
ATOM   11389 C  CD2   . LEU C 2 68  ? 100.971 86.460  116.778 1.00 32.78 ?  47  LEU C CD2   1 
ATOM   11390 N  N     . GLY C 2 69  ? 97.365  85.104  119.746 1.00 30.99 ?  48  GLY C N     1 
ATOM   11391 C  CA    . GLY C 2 69  ? 96.661  84.344  120.778 1.00 30.58 ?  48  GLY C CA    1 
ATOM   11392 C  C     . GLY C 2 69  ? 97.522  84.101  122.011 1.00 29.87 ?  48  GLY C C     1 
ATOM   11393 O  O     . GLY C 2 69  ? 98.746  84.213  121.955 1.00 28.79 ?  48  GLY C O     1 
ATOM   11394 N  N     . LYS C 2 70  ? 96.881  83.780  123.130 1.00 29.89 ?  49  LYS C N     1 
ATOM   11395 C  CA    . LYS C 2 70  ? 97.605  83.499  124.368 1.00 29.49 ?  49  LYS C CA    1 
ATOM   11396 C  C     . LYS C 2 70  ? 98.594  82.328  124.209 1.00 28.74 ?  49  LYS C C     1 
ATOM   11397 O  O     . LYS C 2 70  ? 99.713  82.385  124.735 1.00 27.27 ?  49  LYS C O     1 
ATOM   11398 C  CB    . LYS C 2 70  ? 96.634  83.275  125.532 1.00 30.67 ?  49  LYS C CB    1 
ATOM   11399 C  CG    . LYS C 2 70  ? 96.074  84.597  126.114 1.00 33.73 ?  49  LYS C CG    1 
ATOM   11400 C  CD    . LYS C 2 70  ? 94.816  84.393  126.976 1.00 38.93 ?  49  LYS C CD    1 
ATOM   11401 C  CE    . LYS C 2 70  ? 95.125  83.880  128.389 1.00 41.04 ?  49  LYS C CE    1 
ATOM   11402 N  NZ    . LYS C 2 70  ? 95.746  84.910  129.274 1.00 42.21 1  49  LYS C NZ    1 
ATOM   11403 N  N     . ASN C 2 71  ? 98.176  81.294  123.472 1.00 27.54 ?  50  ASN C N     1 
ATOM   11404 C  CA    . ASN C 2 71  ? 99.041  80.157  123.151 1.00 27.00 ?  50  ASN C CA    1 
ATOM   11405 C  C     . ASN C 2 71  ? 100.299 80.572  122.387 1.00 26.19 ?  50  ASN C C     1 
ATOM   11406 O  O     . ASN C 2 71  ? 101.412 80.085  122.676 1.00 25.38 ?  50  ASN C O     1 
ATOM   11407 C  CB    . ASN C 2 71  ? 98.271  79.076  122.359 1.00 27.08 ?  50  ASN C CB    1 
ATOM   11408 C  CG    . ASN C 2 71  ? 97.701  79.586  121.014 1.00 28.69 ?  50  ASN C CG    1 
ATOM   11409 O  OD1   . ASN C 2 71  ? 97.128  80.688  120.919 1.00 30.45 ?  50  ASN C OD1   1 
ATOM   11410 N  ND2   . ASN C 2 71  ? 97.835  78.755  119.968 1.00 29.42 ?  50  ASN C ND2   1 
ATOM   11411 N  N     . GLU C 2 72  ? 100.115 81.467  121.418 1.00 24.91 ?  51  GLU C N     1 
ATOM   11412 C  CA    . GLU C 2 72  ? 101.213 81.937  120.583 1.00 24.97 ?  51  GLU C CA    1 
ATOM   11413 C  C     . GLU C 2 72  ? 102.217 82.767  121.391 1.00 24.45 ?  51  GLU C C     1 
ATOM   11414 O  O     . GLU C 2 72  ? 103.437 82.579  121.265 1.00 23.90 ?  51  GLU C O     1 
ATOM   11415 C  CB    . GLU C 2 72  ? 100.675 82.741  119.398 1.00 25.27 ?  51  GLU C CB    1 
ATOM   11416 C  CG    . GLU C 2 72  ? 99.853  81.916  118.409 1.00 26.16 ?  51  GLU C CG    1 
ATOM   11417 C  CD    . GLU C 2 72  ? 99.298  82.772  117.279 1.00 28.70 ?  51  GLU C CD    1 
ATOM   11418 O  OE1   . GLU C 2 72  ? 98.311  83.499  117.513 1.00 28.70 ?  51  GLU C OE1   1 
ATOM   11419 O  OE2   . GLU C 2 72  ? 99.846  82.717  116.155 1.00 28.92 -1 51  GLU C OE2   1 
ATOM   11420 N  N     . GLN C 2 73  ? 101.696 83.659  122.231 1.00 23.75 ?  52  GLN C N     1 
ATOM   11421 C  CA    . GLN C 2 73  ? 102.539 84.492  123.086 1.00 23.94 ?  52  GLN C CA    1 
ATOM   11422 C  C     . GLN C 2 73  ? 103.320 83.639  124.087 1.00 23.36 ?  52  GLN C C     1 
ATOM   11423 O  O     . GLN C 2 73  ? 104.483 83.915  124.358 1.00 22.95 ?  52  GLN C O     1 
ATOM   11424 C  CB    . GLN C 2 73  ? 101.700 85.532  123.844 1.00 24.28 ?  52  GLN C CB    1 
ATOM   11425 C  CG    . GLN C 2 73  ? 101.163 86.696  122.988 1.00 25.22 ?  52  GLN C CG    1 
ATOM   11426 C  CD    . GLN C 2 73  ? 100.416 87.753  123.812 1.00 29.02 ?  52  GLN C CD    1 
ATOM   11427 O  OE1   . GLN C 2 73  ? 100.278 87.627  125.027 1.00 32.08 ?  52  GLN C OE1   1 
ATOM   11428 N  NE2   . GLN C 2 73  ? 99.937  88.796  123.145 1.00 29.13 ?  52  GLN C NE2   1 
ATOM   11429 N  N     . ASP C 2 74  ? 102.657 82.627  124.649 1.00 23.02 ?  53  ASP C N     1 
ATOM   11430 C  CA    . ASP C 2 74  ? 103.278 81.725  125.610 1.00 23.44 ?  53  ASP C CA    1 
ATOM   11431 C  C     . ASP C 2 74  ? 104.459 80.983  124.971 1.00 23.00 ?  53  ASP C C     1 
ATOM   11432 O  O     . ASP C 2 74  ? 105.548 80.951  125.536 1.00 22.96 ?  53  ASP C O     1 
ATOM   11433 C  CB    . ASP C 2 74  ? 102.253 80.716  126.146 1.00 23.31 ?  53  ASP C CB    1 
ATOM   11434 C  CG    . ASP C 2 74  ? 102.803 79.868  127.275 1.00 25.80 ?  53  ASP C CG    1 
ATOM   11435 O  OD1   . ASP C 2 74  ? 103.190 80.432  128.330 1.00 27.95 ?  53  ASP C OD1   1 
ATOM   11436 O  OD2   . ASP C 2 74  ? 102.840 78.633  127.109 1.00 26.30 -1 53  ASP C OD2   1 
ATOM   11437 N  N     . THR C 2 75  ? 104.224 80.384  123.805 1.00 22.20 ?  54  THR C N     1 
ATOM   11438 C  CA    . THR C 2 75  ? 105.264 79.663  123.084 1.00 21.84 ?  54  THR C CA    1 
ATOM   11439 C  C     . THR C 2 75  ? 106.412 80.602  122.726 1.00 22.09 ?  54  THR C C     1 
ATOM   11440 O  O     . THR C 2 75  ? 107.574 80.257  122.912 1.00 21.88 ?  54  THR C O     1 
ATOM   11441 C  CB    . THR C 2 75  ? 104.708 78.948  121.822 1.00 21.74 ?  54  THR C CB    1 
ATOM   11442 O  OG1   . THR C 2 75  ? 103.802 77.925  122.237 1.00 22.09 ?  54  THR C OG1   1 
ATOM   11443 C  CG2   . THR C 2 75  ? 105.835 78.283  121.019 1.00 19.76 ?  54  THR C CG2   1 
ATOM   11444 N  N     . TYR C 2 76  ? 106.079 81.789  122.229 1.00 22.38 ?  55  TYR C N     1 
ATOM   11445 C  CA    . TYR C 2 76  ? 107.095 82.776  121.872 1.00 22.85 ?  55  TYR C CA    1 
ATOM   11446 C  C     . TYR C 2 76  ? 108.001 83.160  123.056 1.00 22.56 ?  55  TYR C C     1 
ATOM   11447 O  O     . TYR C 2 76  ? 109.220 83.177  122.907 1.00 21.97 ?  55  TYR C O     1 
ATOM   11448 C  CB    . TYR C 2 76  ? 106.442 84.016  121.278 1.00 23.57 ?  55  TYR C CB    1 
ATOM   11449 C  CG    . TYR C 2 76  ? 107.380 84.930  120.517 1.00 25.59 ?  55  TYR C CG    1 
ATOM   11450 C  CD1   . TYR C 2 76  ? 107.569 84.779  119.139 1.00 27.49 ?  55  TYR C CD1   1 
ATOM   11451 C  CD2   . TYR C 2 76  ? 108.049 85.968  121.166 1.00 27.70 ?  55  TYR C CD2   1 
ATOM   11452 C  CE1   . TYR C 2 76  ? 108.415 85.639  118.429 1.00 30.28 ?  55  TYR C CE1   1 
ATOM   11453 C  CE2   . TYR C 2 76  ? 108.903 86.831  120.467 1.00 30.38 ?  55  TYR C CE2   1 
ATOM   11454 C  CZ    . TYR C 2 76  ? 109.081 86.658  119.100 1.00 31.39 ?  55  TYR C CZ    1 
ATOM   11455 O  OH    . TYR C 2 76  ? 109.913 87.518  118.408 1.00 32.67 ?  55  TYR C OH    1 
ATOM   11456 N  N     . MET C 2 77  ? 107.405 83.470  124.209 1.00 23.14 ?  56  MET C N     1 
ATOM   11457 C  CA    . MET C 2 77  ? 108.169 83.841  125.416 1.00 23.90 ?  56  MET C CA    1 
ATOM   11458 C  C     . MET C 2 77  ? 109.105 82.715  125.833 1.00 23.24 ?  56  MET C C     1 
ATOM   11459 O  O     . MET C 2 77  ? 110.265 82.942  126.198 1.00 22.47 ?  56  MET C O     1 
ATOM   11460 C  CB    . MET C 2 77  ? 107.235 84.139  126.594 1.00 24.38 ?  56  MET C CB    1 
ATOM   11461 C  CG    . MET C 2 77  ? 106.324 85.348  126.440 1.00 28.52 ?  56  MET C CG    1 
ATOM   11462 S  SD    . MET C 2 77  ? 107.188 86.900  126.644 1.00 34.32 ?  56  MET C SD    1 
ATOM   11463 C  CE    . MET C 2 77  ? 107.668 86.828  128.373 1.00 33.84 ?  56  MET C CE    1 
ATOM   11464 N  N     . LYS C 2 78  ? 108.579 81.493  125.786 1.00 23.25 ?  57  LYS C N     1 
ATOM   11465 C  CA    . LYS C 2 78  ? 109.298 80.334  126.298 1.00 22.98 ?  57  LYS C CA    1 
ATOM   11466 C  C     . LYS C 2 78  ? 110.462 79.995  125.378 1.00 22.77 ?  57  LYS C C     1 
ATOM   11467 O  O     . LYS C 2 78  ? 111.564 79.719  125.842 1.00 22.56 ?  57  LYS C O     1 
ATOM   11468 C  CB    . LYS C 2 78  ? 108.339 79.155  126.500 1.00 22.99 ?  57  LYS C CB    1 
ATOM   11469 C  CG    . LYS C 2 78  ? 107.468 79.313  127.749 1.00 24.86 ?  57  LYS C CG    1 
ATOM   11470 C  CD    . LYS C 2 78  ? 106.382 78.241  127.846 1.00 27.37 ?  57  LYS C CD    1 
ATOM   11471 C  CE    . LYS C 2 78  ? 105.695 78.279  129.217 1.00 28.99 ?  57  LYS C CE    1 
ATOM   11472 N  NZ    . LYS C 2 78  ? 104.514 77.366  129.218 1.00 29.82 1  57  LYS C NZ    1 
ATOM   11473 N  N     . VAL C 2 79  ? 110.196 80.048  124.074 1.00 22.70 ?  58  VAL C N     1 
ATOM   11474 C  CA    . VAL C 2 79  ? 111.195 79.862  123.025 1.00 23.48 ?  58  VAL C CA    1 
ATOM   11475 C  C     . VAL C 2 79  ? 112.403 80.810  123.219 1.00 23.04 ?  58  VAL C C     1 
ATOM   11476 O  O     . VAL C 2 79  ? 113.566 80.360  123.249 1.00 22.83 ?  58  VAL C O     1 
ATOM   11477 C  CB    . VAL C 2 79  ? 110.489 80.009  121.640 1.00 24.24 ?  58  VAL C CB    1 
ATOM   11478 C  CG1   . VAL C 2 79  ? 111.356 80.686  120.594 1.00 25.71 ?  58  VAL C CG1   1 
ATOM   11479 C  CG2   . VAL C 2 79  ? 109.940 78.642  121.174 1.00 25.04 ?  58  VAL C CG2   1 
ATOM   11480 N  N     . LEU C 2 80  ? 112.128 82.098  123.402 1.00 22.84 ?  59  LEU C N     1 
ATOM   11481 C  CA    . LEU C 2 80  ? 113.195 83.082  123.597 1.00 23.35 ?  59  LEU C CA    1 
ATOM   11482 C  C     . LEU C 2 80  ? 113.912 82.880  124.937 1.00 22.75 ?  59  LEU C C     1 
ATOM   11483 O  O     . LEU C 2 80  ? 115.115 83.110  125.030 1.00 22.75 ?  59  LEU C O     1 
ATOM   11484 C  CB    . LEU C 2 80  ? 112.676 84.522  123.483 1.00 23.91 ?  59  LEU C CB    1 
ATOM   11485 C  CG    . LEU C 2 80  ? 112.154 85.114  122.158 1.00 26.63 ?  59  LEU C CG    1 
ATOM   11486 C  CD1   . LEU C 2 80  ? 112.136 86.632  122.238 1.00 26.99 ?  59  LEU C CD1   1 
ATOM   11487 C  CD2   . LEU C 2 80  ? 112.961 84.676  120.947 1.00 27.23 ?  59  LEU C CD2   1 
ATOM   11488 N  N     . ALA C 2 81  ? 113.178 82.425  125.955 1.00 22.28 ?  60  ALA C N     1 
ATOM   11489 C  CA    . ALA C 2 81  ? 113.766 82.124  127.264 1.00 22.21 ?  60  ALA C CA    1 
ATOM   11490 C  C     . ALA C 2 81  ? 114.754 80.956  127.178 1.00 22.07 ?  60  ALA C C     1 
ATOM   11491 O  O     . ALA C 2 81  ? 115.823 81.017  127.777 1.00 21.97 ?  60  ALA C O     1 
ATOM   11492 C  CB    . ALA C 2 81  ? 112.667 81.862  128.316 1.00 22.38 ?  60  ALA C CB    1 
ATOM   11493 N  N     . GLY C 2 82  ? 114.403 79.927  126.397 1.00 21.67 ?  61  GLY C N     1 
ATOM   11494 C  CA    . GLY C 2 82  ? 115.281 78.793  126.120 1.00 21.74 ?  61  GLY C CA    1 
ATOM   11495 C  C     . GLY C 2 82  ? 116.548 79.219  125.397 1.00 21.79 ?  61  GLY C C     1 
ATOM   11496 O  O     . GLY C 2 82  ? 117.646 78.720  125.683 1.00 21.93 ?  61  GLY C O     1 
ATOM   11497 N  N     . LEU C 2 83  ? 116.391 80.163  124.471 1.00 21.54 ?  62  LEU C N     1 
ATOM   11498 C  CA    . LEU C 2 83  ? 117.524 80.759  123.764 1.00 21.12 ?  62  LEU C CA    1 
ATOM   11499 C  C     . LEU C 2 83  ? 118.405 81.554  124.718 1.00 20.89 ?  62  LEU C C     1 
ATOM   11500 O  O     . LEU C 2 83  ? 119.631 81.461  124.642 1.00 20.84 ?  62  LEU C O     1 
ATOM   11501 C  CB    . LEU C 2 83  ? 117.058 81.665  122.619 1.00 21.23 ?  62  LEU C CB    1 
ATOM   11502 C  CG    . LEU C 2 83  ? 116.328 81.044  121.420 1.00 21.98 ?  62  LEU C CG    1 
ATOM   11503 C  CD1   . LEU C 2 83  ? 115.803 82.124  120.472 1.00 24.12 ?  62  LEU C CD1   1 
ATOM   11504 C  CD2   . LEU C 2 83  ? 117.209 80.071  120.659 1.00 22.03 ?  62  LEU C CD2   1 
ATOM   11505 N  N     . THR C 2 84  ? 117.775 82.331  125.601 1.00 19.93 ?  63  THR C N     1 
ATOM   11506 C  CA    . THR C 2 84  ? 118.502 83.136  126.580 1.00 19.71 ?  63  THR C CA    1 
ATOM   11507 C  C     . THR C 2 84  ? 119.387 82.258  127.450 1.00 19.63 ?  63  THR C C     1 
ATOM   11508 O  O     . THR C 2 84  ? 120.534 82.618  127.732 1.00 19.62 ?  63  THR C O     1 
ATOM   11509 C  CB    . THR C 2 84  ? 117.542 83.952  127.480 1.00 20.22 ?  63  THR C CB    1 
ATOM   11510 O  OG1   . THR C 2 84  ? 116.613 84.683  126.661 1.00 19.37 ?  63  THR C OG1   1 
ATOM   11511 C  CG2   . THR C 2 84  ? 118.318 84.901  128.360 1.00 19.45 ?  63  THR C CG2   1 
ATOM   11512 N  N     . LEU C 2 85  ? 118.853 81.117  127.877 1.00 19.66 ?  64  LEU C N     1 
ATOM   11513 C  CA    . LEU C 2 85  ? 119.599 80.184  128.718 1.00 20.51 ?  64  LEU C CA    1 
ATOM   11514 C  C     . LEU C 2 85  ? 120.842 79.663  127.989 1.00 20.84 ?  64  LEU C C     1 
ATOM   11515 O  O     . LEU C 2 85  ? 121.948 79.709  128.531 1.00 21.30 ?  64  LEU C O     1 
ATOM   11516 C  CB    . LEU C 2 85  ? 118.711 79.027  129.206 1.00 20.03 ?  64  LEU C CB    1 
ATOM   11517 C  CG    . LEU C 2 85  ? 119.453 77.983  130.074 1.00 21.43 ?  64  LEU C CG    1 
ATOM   11518 C  CD1   . LEU C 2 85  ? 119.934 78.576  131.419 1.00 21.61 ?  64  LEU C CD1   1 
ATOM   11519 C  CD2   . LEU C 2 85  ? 118.618 76.729  130.322 1.00 20.99 ?  64  LEU C CD2   1 
ATOM   11520 N  N     . LEU C 2 86  ? 120.651 79.190  126.763 1.00 21.37 ?  65  LEU C N     1 
ATOM   11521 C  CA    . LEU C 2 86  ? 121.753 78.711  125.926 1.00 21.92 ?  65  LEU C CA    1 
ATOM   11522 C  C     . LEU C 2 86  ? 122.865 79.759  125.746 1.00 21.76 ?  65  LEU C C     1 
ATOM   11523 O  O     . LEU C 2 86  ? 124.042 79.443  125.923 1.00 21.72 ?  65  LEU C O     1 
ATOM   11524 C  CB    . LEU C 2 86  ? 121.237 78.246  124.556 1.00 22.42 ?  65  LEU C CB    1 
ATOM   11525 C  CG    . LEU C 2 86  ? 120.361 76.982  124.425 1.00 24.26 ?  65  LEU C CG    1 
ATOM   11526 C  CD1   . LEU C 2 86  ? 119.881 76.836  122.982 1.00 24.67 ?  65  LEU C CD1   1 
ATOM   11527 C  CD2   . LEU C 2 86  ? 121.109 75.734  124.858 1.00 25.60 ?  65  LEU C CD2   1 
ATOM   11528 N  N     . ASP C 2 87  ? 122.492 80.991  125.396 1.00 21.75 ?  66  ASP C N     1 
ATOM   11529 C  CA    . ASP C 2 87  ? 123.466 82.090  125.247 1.00 21.99 ?  66  ASP C CA    1 
ATOM   11530 C  C     . ASP C 2 87  ? 124.146 82.503  126.557 1.00 21.76 ?  66  ASP C C     1 
ATOM   11531 O  O     . ASP C 2 87  ? 125.319 82.902  126.560 1.00 21.65 ?  66  ASP C O     1 
ATOM   11532 C  CB    . ASP C 2 87  ? 122.808 83.327  124.631 1.00 22.23 ?  66  ASP C CB    1 
ATOM   11533 C  CG    . ASP C 2 87  ? 122.966 83.384  123.137 1.00 24.59 ?  66  ASP C CG    1 
ATOM   11534 O  OD1   . ASP C 2 87  ? 124.075 83.091  122.632 1.00 27.46 ?  66  ASP C OD1   1 
ATOM   11535 O  OD2   . ASP C 2 87  ? 121.975 83.736  122.465 1.00 27.98 -1 66  ASP C OD2   1 
ATOM   11536 N  N     . THR C 2 88  ? 123.396 82.442  127.655 1.00 21.50 ?  67  THR C N     1 
ATOM   11537 C  CA    . THR C 2 88  ? 123.957 82.687  128.979 1.00 21.80 ?  67  THR C CA    1 
ATOM   11538 C  C     . THR C 2 88  ? 125.142 81.740  129.249 1.00 22.04 ?  67  THR C C     1 
ATOM   11539 O  O     . THR C 2 88  ? 126.221 82.185  129.665 1.00 22.21 ?  67  THR C O     1 
ATOM   11540 C  CB    . THR C 2 88  ? 122.879 82.558  130.070 1.00 22.15 ?  67  THR C CB    1 
ATOM   11541 O  OG1   . THR C 2 88  ? 121.846 83.514  129.819 1.00 22.23 ?  67  THR C OG1   1 
ATOM   11542 C  CG2   . THR C 2 88  ? 123.454 82.810  131.467 1.00 21.19 ?  67  THR C CG2   1 
ATOM   11543 N  N     . GLU C 2 89  ? 124.946 80.453  128.979 1.00 21.55 ?  68  GLU C N     1 
ATOM   11544 C  CA    . GLU C 2 89  ? 125.980 79.463  129.251 1.00 21.81 ?  68  GLU C CA    1 
ATOM   11545 C  C     . GLU C 2 89  ? 127.090 79.475  128.188 1.00 21.35 ?  68  GLU C C     1 
ATOM   11546 O  O     . GLU C 2 89  ? 128.258 79.263  128.506 1.00 21.34 ?  68  GLU C O     1 
ATOM   11547 C  CB    . GLU C 2 89  ? 125.365 78.075  129.456 1.00 22.25 ?  68  GLU C CB    1 
ATOM   11548 C  CG    . GLU C 2 89  ? 124.755 77.889  130.876 1.00 24.02 ?  68  GLU C CG    1 
ATOM   11549 C  CD    . GLU C 2 89  ? 125.742 78.233  131.993 1.00 25.78 ?  68  GLU C CD    1 
ATOM   11550 O  OE1   . GLU C 2 89  ? 126.912 77.798  131.927 1.00 26.69 ?  68  GLU C OE1   1 
ATOM   11551 O  OE2   . GLU C 2 89  ? 125.350 78.942  132.949 1.00 28.98 -1 68  GLU C OE2   1 
ATOM   11552 N  N     . GLN C 2 90  ? 126.730 79.775  126.942 1.00 20.82 ?  69  GLN C N     1 
ATOM   11553 C  CA    . GLN C 2 90  ? 127.716 79.902  125.875 1.00 21.28 ?  69  GLN C CA    1 
ATOM   11554 C  C     . GLN C 2 90  ? 128.654 81.085  126.136 1.00 21.24 ?  69  GLN C C     1 
ATOM   11555 O  O     . GLN C 2 90  ? 129.855 80.999  125.866 1.00 20.99 ?  69  GLN C O     1 
ATOM   11556 C  CB    . GLN C 2 90  ? 127.033 80.023  124.501 1.00 21.86 ?  69  GLN C CB    1 
ATOM   11557 C  CG    . GLN C 2 90  ? 127.987 79.806  123.304 1.00 24.29 ?  69  GLN C CG    1 
ATOM   11558 C  CD    . GLN C 2 90  ? 128.464 78.355  123.172 1.00 27.14 ?  69  GLN C CD    1 
ATOM   11559 O  OE1   . GLN C 2 90  ? 128.429 77.587  124.137 1.00 27.13 ?  69  GLN C OE1   1 
ATOM   11560 N  NE2   . GLN C 2 90  ? 128.927 77.986  121.975 1.00 27.69 ?  69  GLN C NE2   1 
ATOM   11561 N  N     . GLY C 2 91  ? 128.103 82.167  126.694 1.00 20.62 ?  70  GLY C N     1 
ATOM   11562 C  CA    . GLY C 2 91  ? 128.881 83.367  127.016 1.00 22.00 ?  70  GLY C CA    1 
ATOM   11563 C  C     . GLY C 2 91  ? 129.655 83.260  128.315 1.00 22.45 ?  70  GLY C C     1 
ATOM   11564 O  O     . GLY C 2 91  ? 130.821 83.644  128.361 1.00 23.53 ?  70  GLY C O     1 
ATOM   11565 N  N     . ASN C 2 92  ? 129.011 82.740  129.362 1.00 22.79 ?  71  ASN C N     1 
ATOM   11566 C  CA    . ASN C 2 92  ? 129.634 82.607  130.688 1.00 23.85 ?  71  ASN C CA    1 
ATOM   11567 C  C     . ASN C 2 92  ? 130.704 81.522  130.729 1.00 24.33 ?  71  ASN C C     1 
ATOM   11568 O  O     . ASN C 2 92  ? 131.708 81.661  131.436 1.00 24.17 ?  71  ASN C O     1 
ATOM   11569 C  CB    . ASN C 2 92  ? 128.592 82.259  131.759 1.00 23.74 ?  71  ASN C CB    1 
ATOM   11570 C  CG    . ASN C 2 92  ? 127.630 83.396  132.060 1.00 24.38 ?  71  ASN C CG    1 
ATOM   11571 O  OD1   . ASN C 2 92  ? 127.683 84.475  131.457 1.00 25.16 ?  71  ASN C OD1   1 
ATOM   11572 N  ND2   . ASN C 2 92  ? 126.732 83.149  133.000 1.00 24.07 ?  71  ASN C ND2   1 
ATOM   11573 N  N     . THR C 2 93  ? 130.485 80.447  129.968 1.00 23.97 ?  72  THR C N     1 
ATOM   11574 C  CA    . THR C 2 93  ? 131.233 79.200  130.183 1.00 24.97 ?  72  THR C CA    1 
ATOM   11575 C  C     . THR C 2 93  ? 131.877 78.673  128.910 1.00 24.52 ?  72  THR C C     1 
ATOM   11576 O  O     . THR C 2 93  ? 133.091 78.526  128.852 1.00 25.39 ?  72  THR C O     1 
ATOM   11577 C  CB    . THR C 2 93  ? 130.330 78.096  130.796 1.00 24.54 ?  72  THR C CB    1 
ATOM   11578 O  OG1   . THR C 2 93  ? 129.704 78.589  131.988 1.00 26.43 ?  72  THR C OG1   1 
ATOM   11579 C  CG2   . THR C 2 93  ? 131.137 76.856  131.144 1.00 26.83 ?  72  THR C CG2   1 
ATOM   11580 N  N     . GLY C 2 94  ? 131.057 78.403  127.904 1.00 24.37 ?  73  GLY C N     1 
ATOM   11581 C  CA    . GLY C 2 94  ? 131.485 77.702  126.684 1.00 24.24 ?  73  GLY C CA    1 
ATOM   11582 C  C     . GLY C 2 94  ? 132.585 78.400  125.913 1.00 24.94 ?  73  GLY C C     1 
ATOM   11583 O  O     . GLY C 2 94  ? 133.675 77.848  125.732 1.00 25.86 ?  73  GLY C O     1 
ATOM   11584 N  N     . MET C 2 95  ? 132.306 79.615  125.454 1.00 24.07 ?  74  MET C N     1 
ATOM   11585 C  CA    . MET C 2 95  ? 133.300 80.356  124.688 1.00 24.35 ?  74  MET C CA    1 
ATOM   11586 C  C     . MET C 2 95  ? 134.574 80.729  125.470 1.00 23.52 ?  74  MET C C     1 
ATOM   11587 O  O     . MET C 2 95  ? 135.659 80.552  124.927 1.00 23.40 ?  74  MET C O     1 
ATOM   11588 C  CB    . MET C 2 95  ? 132.679 81.560  123.980 1.00 24.38 ?  74  MET C CB    1 
ATOM   11589 C  CG    . MET C 2 95  ? 131.757 81.188  122.818 1.00 27.47 ?  74  MET C CG    1 
ATOM   11590 S  SD    . MET C 2 95  ? 132.672 80.321  121.515 1.00 32.54 ?  74  MET C SD    1 
ATOM   11591 C  CE    . MET C 2 95  ? 133.626 81.640  120.853 1.00 34.32 ?  74  MET C CE    1 
ATOM   11592 N  N     . PRO C 2 96  ? 134.452 81.235  126.731 1.00 23.36 ?  75  PRO C N     1 
ATOM   11593 C  CA    . PRO C 2 96  ? 135.662 81.517  127.533 1.00 23.27 ?  75  PRO C CA    1 
ATOM   11594 C  C     . PRO C 2 96  ? 136.538 80.297  127.799 1.00 23.77 ?  75  PRO C C     1 
ATOM   11595 O  O     . PRO C 2 96  ? 137.762 80.404  127.730 1.00 23.46 ?  75  PRO C O     1 
ATOM   11596 C  CB    . PRO C 2 96  ? 135.098 82.027  128.870 1.00 23.55 ?  75  PRO C CB    1 
ATOM   11597 C  CG    . PRO C 2 96  ? 133.768 82.601  128.522 1.00 23.85 ?  75  PRO C CG    1 
ATOM   11598 C  CD    . PRO C 2 96  ? 133.232 81.693  127.427 1.00 22.76 ?  75  PRO C CD    1 
ATOM   11599 N  N     . ILE C 2 97  ? 135.926 79.155  128.120 1.00 23.81 ?  76  ILE C N     1 
ATOM   11600 C  CA    . ILE C 2 97  ? 136.693 77.935  128.384 1.00 24.52 ?  76  ILE C CA    1 
ATOM   11601 C  C     . ILE C 2 97  ? 137.420 77.393  127.134 1.00 23.92 ?  76  ILE C C     1 
ATOM   11602 O  O     . ILE C 2 97  ? 138.588 76.989  127.209 1.00 23.99 ?  76  ILE C O     1 
ATOM   11603 C  CB    . ILE C 2 97  ? 135.837 76.847  129.094 1.00 24.49 ?  76  ILE C CB    1 
ATOM   11604 C  CG1   . ILE C 2 97  ? 136.733 75.865  129.845 1.00 27.08 ?  76  ILE C CG1   1 
ATOM   11605 C  CG2   . ILE C 2 97  ? 134.916 76.096  128.109 1.00 26.06 ?  76  ILE C CG2   1 
ATOM   11606 C  CD1   . ILE C 2 97  ? 136.021 75.180  131.001 1.00 31.37 ?  76  ILE C CD1   1 
ATOM   11607 N  N     . VAL C 2 98  ? 136.745 77.414  125.989 1.00 23.97 ?  77  VAL C N     1 
ATOM   11608 C  CA    . VAL C 2 98  ? 137.394 77.050  124.721 1.00 24.01 ?  77  VAL C CA    1 
ATOM   11609 C  C     . VAL C 2 98  ? 138.531 78.045  124.408 1.00 25.23 ?  77  VAL C C     1 
ATOM   11610 O  O     . VAL C 2 98  ? 139.634 77.636  124.030 1.00 25.77 ?  77  VAL C O     1 
ATOM   11611 C  CB    . VAL C 2 98  ? 136.369 76.952  123.562 1.00 23.98 ?  77  VAL C CB    1 
ATOM   11612 C  CG1   . VAL C 2 98  ? 137.072 76.852  122.210 1.00 23.17 ?  77  VAL C CG1   1 
ATOM   11613 C  CG2   . VAL C 2 98  ? 135.451 75.743  123.780 1.00 22.55 ?  77  VAL C CG2   1 
ATOM   11614 N  N     . ALA C 2 99  ? 138.281 79.338  124.622 1.00 25.42 ?  78  ALA C N     1 
ATOM   11615 C  CA    . ALA C 2 99  ? 139.331 80.356  124.435 1.00 26.72 ?  78  ALA C CA    1 
ATOM   11616 C  C     . ALA C 2 99  ? 140.571 80.041  125.277 1.00 27.46 ?  78  ALA C C     1 
ATOM   11617 O  O     . ALA C 2 99  ? 141.697 80.158  124.795 1.00 28.07 ?  78  ALA C O     1 
ATOM   11618 C  CB    . ALA C 2 99  ? 138.810 81.743  124.757 1.00 26.52 ?  78  ALA C CB    1 
ATOM   11619 N  N     . GLU C 2 100 ? 140.352 79.604  126.516 1.00 28.33 ?  79  GLU C N     1 
ATOM   11620 C  CA    . GLU C 2 100 ? 141.449 79.294  127.437 1.00 29.60 ?  79  GLU C CA    1 
ATOM   11621 C  C     . GLU C 2 100 ? 142.362 78.184  126.908 1.00 29.64 ?  79  GLU C C     1 
ATOM   11622 O  O     . GLU C 2 100 ? 143.585 78.232  127.086 1.00 29.72 ?  79  GLU C O     1 
ATOM   11623 C  CB    . GLU C 2 100 ? 140.903 78.927  128.818 1.00 29.70 ?  79  GLU C CB    1 
ATOM   11624 C  CG    . GLU C 2 100 ? 141.984 78.664  129.866 1.00 33.58 ?  79  GLU C CG    1 
ATOM   11625 C  CD    . GLU C 2 100 ? 141.440 78.178  131.194 1.00 37.83 ?  79  GLU C CD    1 
ATOM   11626 O  OE1   . GLU C 2 100 ? 140.202 78.183  131.402 1.00 40.64 ?  79  GLU C OE1   1 
ATOM   11627 O  OE2   . GLU C 2 100 ? 142.265 77.777  132.044 1.00 41.40 -1 79  GLU C OE2   1 
ATOM   11628 N  N     . HIS C 2 101 ? 141.769 77.197  126.239 1.00 29.43 ?  80  HIS C N     1 
ATOM   11629 C  CA    . HIS C 2 101 ? 142.508 76.006  125.842 1.00 29.74 ?  80  HIS C CA    1 
ATOM   11630 C  C     . HIS C 2 101 ? 143.059 76.030  124.415 1.00 30.18 ?  80  HIS C C     1 
ATOM   11631 O  O     . HIS C 2 101 ? 143.933 75.240  124.079 1.00 30.30 ?  80  HIS C O     1 
ATOM   11632 C  CB    . HIS C 2 101 ? 141.678 74.744  126.132 1.00 29.21 ?  80  HIS C CB    1 
ATOM   11633 C  CG    . HIS C 2 101 ? 141.527 74.465  127.596 1.00 29.60 ?  80  HIS C CG    1 
ATOM   11634 N  ND1   . HIS C 2 101 ? 140.471 74.945  128.343 1.00 30.06 ?  80  HIS C ND1   1 
ATOM   11635 C  CD2   . HIS C 2 101 ? 142.323 73.793  128.460 1.00 29.49 ?  80  HIS C CD2   1 
ATOM   11636 C  CE1   . HIS C 2 101 ? 140.617 74.568  129.602 1.00 29.56 ?  80  HIS C CE1   1 
ATOM   11637 N  NE2   . HIS C 2 101 ? 141.731 73.867  129.699 1.00 30.20 ?  80  HIS C NE2   1 
ATOM   11638 N  N     . VAL C 2 102 ? 142.557 76.945  123.590 1.00 30.70 ?  81  VAL C N     1 
ATOM   11639 C  CA    . VAL C 2 102 ? 143.019 77.091  122.212 1.00 31.47 ?  81  VAL C CA    1 
ATOM   11640 C  C     . VAL C 2 102 ? 144.253 77.991  122.180 1.00 32.45 ?  81  VAL C C     1 
ATOM   11641 O  O     . VAL C 2 102 ? 144.246 79.075  122.777 1.00 32.50 ?  81  VAL C O     1 
ATOM   11642 C  CB    . VAL C 2 102 ? 141.914 77.667  121.288 1.00 31.18 ?  81  VAL C CB    1 
ATOM   11643 C  CG1   . VAL C 2 102 ? 142.471 78.010  119.905 1.00 31.20 ?  81  VAL C CG1   1 
ATOM   11644 C  CG2   . VAL C 2 102 ? 140.770 76.674  121.148 1.00 31.28 ?  81  VAL C CG2   1 
ATOM   11645 N  N     . ASP C 2 103 ? 145.293 77.541  121.476 1.00 33.38 ?  82  ASP C N     1 
ATOM   11646 C  CA    . ASP C 2 103 ? 146.558 78.275  121.378 1.00 34.82 ?  82  ASP C CA    1 
ATOM   11647 C  C     . ASP C 2 103 ? 146.567 79.313  120.262 1.00 34.74 ?  82  ASP C C     1 
ATOM   11648 O  O     . ASP C 2 103 ? 146.026 79.078  119.175 1.00 35.00 ?  82  ASP C O     1 
ATOM   11649 C  CB    . ASP C 2 103 ? 147.735 77.306  121.190 1.00 35.82 ?  82  ASP C CB    1 
ATOM   11650 C  CG    . ASP C 2 103 ? 148.080 76.540  122.464 1.00 38.29 ?  82  ASP C CG    1 
ATOM   11651 O  OD1   . ASP C 2 103 ? 147.908 77.092  123.579 1.00 41.49 ?  82  ASP C OD1   1 
ATOM   11652 O  OD2   . ASP C 2 103 ? 148.528 75.383  122.352 1.00 41.10 -1 82  ASP C OD2   1 
ATOM   11653 N  N     . GLY C 2 104 ? 147.191 80.457  120.543 1.00 34.89 ?  83  GLY C N     1 
ATOM   11654 C  CA    . GLY C 2 104 ? 147.364 81.528  119.555 1.00 35.11 ?  83  GLY C CA    1 
ATOM   11655 C  C     . GLY C 2 104 ? 146.538 82.760  119.871 1.00 34.96 ?  83  GLY C C     1 
ATOM   11656 O  O     . GLY C 2 104 ? 145.313 82.674  119.988 1.00 34.57 ?  83  GLY C O     1 
ATOM   11657 N  N     . HIS C 2 105 ? 147.210 83.907  119.993 1.00 35.02 ?  84  HIS C N     1 
ATOM   11658 C  CA    . HIS C 2 105 ? 146.563 85.161  120.407 1.00 34.83 ?  84  HIS C CA    1 
ATOM   11659 C  C     . HIS C 2 105 ? 145.423 85.606  119.500 1.00 33.77 ?  84  HIS C C     1 
ATOM   11660 O  O     . HIS C 2 105 ? 144.429 86.157  119.977 1.00 33.25 ?  84  HIS C O     1 
ATOM   11661 C  CB    . HIS C 2 105 ? 147.585 86.291  120.577 1.00 36.09 ?  84  HIS C CB    1 
ATOM   11662 C  CG    . HIS C 2 105 ? 148.403 86.174  121.826 1.00 39.17 ?  84  HIS C CG    1 
ATOM   11663 N  ND1   . HIS C 2 105 ? 149.719 86.585  121.897 1.00 43.00 ?  84  HIS C ND1   1 
ATOM   11664 C  CD2   . HIS C 2 105 ? 148.100 85.672  123.048 1.00 41.84 ?  84  HIS C CD2   1 
ATOM   11665 C  CE1   . HIS C 2 105 ? 150.186 86.349  123.113 1.00 43.47 ?  84  HIS C CE1   1 
ATOM   11666 N  NE2   . HIS C 2 105 ? 149.223 85.796  123.830 1.00 43.10 ?  84  HIS C NE2   1 
ATOM   11667 N  N     . GLN C 2 106 ? 145.554 85.354  118.203 1.00 32.84 ?  85  GLN C N     1 
ATOM   11668 C  CA    . GLN C 2 106 ? 144.493 85.719  117.268 1.00 32.29 ?  85  GLN C CA    1 
ATOM   11669 C  C     . GLN C 2 106 ? 143.274 84.797  117.384 1.00 30.88 ?  85  GLN C C     1 
ATOM   11670 O  O     . GLN C 2 106 ? 142.132 85.268  117.331 1.00 30.44 ?  85  GLN C O     1 
ATOM   11671 C  CB    . GLN C 2 106 ? 145.012 85.747  115.838 1.00 32.85 ?  85  GLN C CB    1 
ATOM   11672 C  CG    . GLN C 2 106 ? 146.049 86.834  115.588 1.00 35.55 ?  85  GLN C CG    1 
ATOM   11673 C  CD    . GLN C 2 106 ? 146.618 86.764  114.195 1.00 38.12 ?  85  GLN C CD    1 
ATOM   11674 O  OE1   . GLN C 2 106 ? 145.906 86.466  113.237 1.00 39.96 ?  85  GLN C OE1   1 
ATOM   11675 N  NE2   . GLN C 2 106 ? 147.915 87.041  114.070 1.00 40.39 ?  85  GLN C NE2   1 
ATOM   11676 N  N     . ARG C 2 107 ? 143.516 83.496  117.537 1.00 29.75 ?  86  ARG C N     1 
ATOM   11677 C  CA    . ARG C 2 107 ? 142.424 82.541  117.760 1.00 28.87 ?  86  ARG C CA    1 
ATOM   11678 C  C     . ARG C 2 107 ? 141.700 82.889  119.054 1.00 28.16 ?  86  ARG C C     1 
ATOM   11679 O  O     . ARG C 2 107 ? 140.472 82.867  119.102 1.00 27.55 ?  86  ARG C O     1 
ATOM   11680 C  CB    . ARG C 2 107 ? 142.939 81.104  117.815 1.00 28.48 ?  86  ARG C CB    1 
ATOM   11681 C  CG    . ARG C 2 107 ? 143.373 80.569  116.461 1.00 29.86 ?  86  ARG C CG    1 
ATOM   11682 C  CD    . ARG C 2 107 ? 143.916 79.152  116.549 1.00 30.23 ?  86  ARG C CD    1 
ATOM   11683 N  NE    . ARG C 2 107 ? 143.881 78.549  115.222 1.00 33.04 ?  86  ARG C NE    1 
ATOM   11684 C  CZ    . ARG C 2 107 ? 143.933 77.251  114.978 1.00 31.54 ?  86  ARG C CZ    1 
ATOM   11685 N  NH1   . ARG C 2 107 ? 144.047 76.383  115.973 1.00 31.85 1  86  ARG C NH1   1 
ATOM   11686 N  NH2   . ARG C 2 107 ? 143.878 76.829  113.725 1.00 34.74 ?  86  ARG C NH2   1 
ATOM   11687 N  N     . LYS C 2 108 ? 142.466 83.224  120.091 1.00 27.65 ?  87  LYS C N     1 
ATOM   11688 C  CA    . LYS C 2 108 ? 141.879 83.634  121.371 1.00 27.96 ?  87  LYS C CA    1 
ATOM   11689 C  C     . LYS C 2 108 ? 141.073 84.921  121.264 1.00 27.75 ?  87  LYS C C     1 
ATOM   11690 O  O     . LYS C 2 108 ? 140.037 85.051  121.916 1.00 28.29 ?  87  LYS C O     1 
ATOM   11691 C  CB    . LYS C 2 108 ? 142.940 83.778  122.461 1.00 27.80 ?  87  LYS C CB    1 
ATOM   11692 C  CG    . LYS C 2 108 ? 143.550 82.462  122.897 1.00 29.04 ?  87  LYS C CG    1 
ATOM   11693 C  CD    . LYS C 2 108 ? 144.569 82.703  124.001 1.00 31.15 ?  87  LYS C CD    1 
ATOM   11694 C  CE    . LYS C 2 108 ? 145.356 81.444  124.314 1.00 32.05 ?  87  LYS C CE    1 
ATOM   11695 N  NZ    . LYS C 2 108 ? 144.552 80.509  125.140 1.00 30.88 1  87  LYS C NZ    1 
ATOM   11696 N  N     . ALA C 2 109 ? 141.541 85.865  120.447 1.00 27.69 ?  88  ALA C N     1 
ATOM   11697 C  CA    . ALA C 2 109 ? 140.815 87.125  120.237 1.00 27.46 ?  88  ALA C CA    1 
ATOM   11698 C  C     . ALA C 2 109 ? 139.450 86.915  119.574 1.00 26.87 ?  88  ALA C C     1 
ATOM   11699 O  O     . ALA C 2 109 ? 138.476 87.577  119.932 1.00 26.47 ?  88  ALA C O     1 
ATOM   11700 C  CB    . ALA C 2 109 ? 141.649 88.093  119.424 1.00 27.98 ?  88  ALA C CB    1 
ATOM   11701 N  N     . VAL C 2 110 ? 139.392 86.009  118.600 1.00 25.98 ?  89  VAL C N     1 
ATOM   11702 C  CA    . VAL C 2 110 ? 138.135 85.661  117.934 1.00 25.46 ?  89  VAL C CA    1 
ATOM   11703 C  C     . VAL C 2 110 ? 137.179 85.005  118.936 1.00 24.57 ?  89  VAL C C     1 
ATOM   11704 O  O     . VAL C 2 110 ? 136.022 85.416  119.065 1.00 23.62 ?  89  VAL C O     1 
ATOM   11705 C  CB    . VAL C 2 110 ? 138.374 84.738  116.714 1.00 25.80 ?  89  VAL C CB    1 
ATOM   11706 C  CG1   . VAL C 2 110 ? 137.055 84.177  116.165 1.00 25.44 ?  89  VAL C CG1   1 
ATOM   11707 C  CG2   . VAL C 2 110 ? 139.134 85.490  115.622 1.00 26.23 ?  89  VAL C CG2   1 
ATOM   11708 N  N     . LEU C 2 111 ? 137.681 84.012  119.668 1.00 24.33 ?  90  LEU C N     1 
ATOM   11709 C  CA    . LEU C 2 111 ? 136.854 83.308  120.649 1.00 23.93 ?  90  LEU C CA    1 
ATOM   11710 C  C     . LEU C 2 111 ? 136.372 84.211  121.784 1.00 23.77 ?  90  LEU C C     1 
ATOM   11711 O  O     . LEU C 2 111 ? 135.232 84.078  122.232 1.00 23.04 ?  90  LEU C O     1 
ATOM   11712 C  CB    . LEU C 2 111 ? 137.564 82.065  121.191 1.00 23.73 ?  90  LEU C CB    1 
ATOM   11713 C  CG    . LEU C 2 111 ? 137.849 80.982  120.147 1.00 24.50 ?  90  LEU C CG    1 
ATOM   11714 C  CD1   . LEU C 2 111 ? 138.936 80.033  120.628 1.00 24.02 ?  90  LEU C CD1   1 
ATOM   11715 C  CD2   . LEU C 2 111 ? 136.580 80.214  119.769 1.00 25.38 ?  90  LEU C CD2   1 
ATOM   11716 N  N     . ASN C 2 112 ? 137.239 85.114  122.253 1.00 24.24 ?  91  ASN C N     1 
ATOM   11717 C  CA    . ASN C 2 112 ? 136.838 86.128  123.241 1.00 24.95 ?  91  ASN C CA    1 
ATOM   11718 C  C     . ASN C 2 112 ? 135.752 87.070  122.732 1.00 24.25 ?  91  ASN C C     1 
ATOM   11719 O  O     . ASN C 2 112 ? 134.838 87.424  123.476 1.00 23.99 ?  91  ASN C O     1 
ATOM   11720 C  CB    . ASN C 2 112 ? 138.037 86.960  123.706 1.00 25.81 ?  91  ASN C CB    1 
ATOM   11721 C  CG    . ASN C 2 112 ? 138.778 86.314  124.845 1.00 29.96 ?  91  ASN C CG    1 
ATOM   11722 O  OD1   . ASN C 2 112 ? 138.477 86.570  126.012 1.00 35.44 ?  91  ASN C OD1   1 
ATOM   11723 N  ND2   . ASN C 2 112 ? 139.753 85.464  124.522 1.00 32.37 ?  91  ASN C ND2   1 
ATOM   11724 N  N     . PHE C 2 113 ? 135.878 87.501  121.477 1.00 23.60 ?  92  PHE C N     1 
ATOM   11725 C  CA    . PHE C 2 113 ? 134.861 88.342  120.855 1.00 23.32 ?  92  PHE C CA    1 
ATOM   11726 C  C     . PHE C 2 113 ? 133.514 87.611  120.761 1.00 22.63 ?  92  PHE C C     1 
ATOM   11727 O  O     . PHE C 2 113 ? 132.472 88.186  121.082 1.00 21.94 ?  92  PHE C O     1 
ATOM   11728 C  CB    . PHE C 2 113 ? 135.285 88.788  119.448 1.00 23.27 ?  92  PHE C CB    1 
ATOM   11729 C  CG    . PHE C 2 113 ? 134.393 89.851  118.867 1.00 24.66 ?  92  PHE C CG    1 
ATOM   11730 C  CD1   . PHE C 2 113 ? 134.664 91.208  119.095 1.00 25.72 ?  92  PHE C CD1   1 
ATOM   11731 C  CD2   . PHE C 2 113 ? 133.272 89.505  118.117 1.00 25.36 ?  92  PHE C CD2   1 
ATOM   11732 C  CE1   . PHE C 2 113 ? 133.830 92.198  118.575 1.00 25.92 ?  92  PHE C CE1   1 
ATOM   11733 C  CE2   . PHE C 2 113 ? 132.427 90.491  117.591 1.00 25.82 ?  92  PHE C CE2   1 
ATOM   11734 C  CZ    . PHE C 2 113 ? 132.705 91.839  117.825 1.00 25.80 ?  92  PHE C CZ    1 
ATOM   11735 N  N     . MET C 2 114 ? 133.549 86.359  120.298 1.00 22.03 ?  93  MET C N     1 
ATOM   11736 C  CA    . MET C 2 114 ? 132.344 85.521  120.227 1.00 22.14 ?  93  MET C CA    1 
ATOM   11737 C  C     . MET C 2 114 ? 131.682 85.340  121.604 1.00 21.64 ?  93  MET C C     1 
ATOM   11738 O  O     . MET C 2 114 ? 130.456 85.438  121.719 1.00 21.59 ?  93  MET C O     1 
ATOM   11739 C  CB    . MET C 2 114 ? 132.667 84.167  119.605 1.00 22.46 ?  93  MET C CB    1 
ATOM   11740 C  CG    . MET C 2 114 ? 133.027 84.241  118.129 1.00 23.80 ?  93  MET C CG    1 
ATOM   11741 S  SD    . MET C 2 114 ? 133.586 82.651  117.480 1.00 28.07 ?  93  MET C SD    1 
ATOM   11742 C  CE    . MET C 2 114 ? 133.571 83.030  115.708 1.00 26.42 ?  93  MET C CE    1 
ATOM   11743 N  N     . ALA C 2 115 ? 132.495 85.113  122.641 1.00 20.98 ?  94  ALA C N     1 
ATOM   11744 C  CA    . ALA C 2 115 ? 132.006 85.033  124.030 1.00 20.58 ?  94  ALA C CA    1 
ATOM   11745 C  C     . ALA C 2 115 ? 131.273 86.296  124.479 1.00 21.01 ?  94  ALA C C     1 
ATOM   11746 O  O     . ALA C 2 115 ? 130.215 86.228  125.131 1.00 21.06 ?  94  ALA C O     1 
ATOM   11747 C  CB    . ALA C 2 115 ? 133.177 84.723  124.993 1.00 20.83 ?  94  ALA C CB    1 
ATOM   11748 N  N     . MET C 2 116 ? 131.855 87.452  124.163 1.00 20.36 ?  95  MET C N     1 
ATOM   11749 C  CA    . MET C 2 116 ? 131.240 88.726  124.489 1.00 20.83 ?  95  MET C CA    1 
ATOM   11750 C  C     . MET C 2 116 ? 129.871 88.853  123.801 1.00 20.55 ?  95  MET C C     1 
ATOM   11751 O  O     . MET C 2 116 ? 128.888 89.245  124.428 1.00 20.70 ?  95  MET C O     1 
ATOM   11752 C  CB    . MET C 2 116 ? 132.180 89.874  124.099 1.00 20.64 ?  95  MET C CB    1 
ATOM   11753 C  CG    . MET C 2 116 ? 131.603 91.280  124.274 1.00 21.42 ?  95  MET C CG    1 
ATOM   11754 S  SD    . MET C 2 116 ? 130.520 91.750  122.910 1.00 22.51 ?  95  MET C SD    1 
ATOM   11755 C  CE    . MET C 2 116 ? 131.640 91.665  121.512 1.00 20.66 ?  95  MET C CE    1 
ATOM   11756 N  N     . MET C 2 117 ? 129.813 88.497  122.522 1.00 20.50 ?  96  MET C N     1 
ATOM   11757 C  CA    . MET C 2 117 ? 128.563 88.554  121.777 1.00 21.22 ?  96  MET C CA    1 
ATOM   11758 C  C     . MET C 2 117 ? 127.477 87.711  122.445 1.00 21.11 ?  96  MET C C     1 
ATOM   11759 O  O     . MET C 2 117 ? 126.339 88.168  122.577 1.00 20.71 ?  96  MET C O     1 
ATOM   11760 C  CB    . MET C 2 117 ? 128.765 88.137  120.314 1.00 21.35 ?  96  MET C CB    1 
ATOM   11761 C  CG    . MET C 2 117 ? 129.527 89.174  119.430 1.00 22.54 ?  96  MET C CG    1 
ATOM   11762 S  SD    . MET C 2 117 ? 128.841 90.846  119.405 1.00 24.89 ?  96  MET C SD    1 
ATOM   11763 C  CE    . MET C 2 117 ? 127.407 90.620  118.354 1.00 24.95 ?  96  MET C CE    1 
ATOM   11764 N  N     . GLU C 2 118 ? 127.841 86.505  122.881 1.00 21.18 ?  97  GLU C N     1 
ATOM   11765 C  CA    . GLU C 2 118 ? 126.897 85.585  123.527 1.00 21.99 ?  97  GLU C CA    1 
ATOM   11766 C  C     . GLU C 2 118 ? 126.178 86.218  124.719 1.00 22.10 ?  97  GLU C C     1 
ATOM   11767 O  O     . GLU C 2 118 ? 124.946 86.245  124.760 1.00 22.22 ?  97  GLU C O     1 
ATOM   11768 C  CB    . GLU C 2 118 ? 127.575 84.278  123.969 1.00 22.01 ?  97  GLU C CB    1 
ATOM   11769 C  CG    . GLU C 2 118 ? 128.367 83.504  122.908 1.00 24.38 ?  97  GLU C CG    1 
ATOM   11770 C  CD    . GLU C 2 118 ? 127.553 83.040  121.694 1.00 26.32 ?  97  GLU C CD    1 
ATOM   11771 O  OE1   . GLU C 2 118 ? 126.592 83.711  121.291 1.00 29.86 ?  97  GLU C OE1   1 
ATOM   11772 O  OE2   . GLU C 2 118 ? 127.914 82.010  121.100 1.00 29.19 -1 97  GLU C OE2   1 
ATOM   11773 N  N     . ASN C 2 119 ? 126.936 86.724  125.690 1.00 22.26 ?  98  ASN C N     1 
ATOM   11774 C  CA    . ASN C 2 119 ? 126.305 87.213  126.916 1.00 21.91 ?  98  ASN C CA    1 
ATOM   11775 C  C     . ASN C 2 119 ? 126.075 88.728  127.023 1.00 22.41 ?  98  ASN C C     1 
ATOM   11776 O  O     . ASN C 2 119 ? 125.139 89.162  127.691 1.00 23.07 ?  98  ASN C O     1 
ATOM   11777 C  CB    . ASN C 2 119 ? 126.918 86.589  128.189 1.00 21.93 ?  98  ASN C CB    1 
ATOM   11778 C  CG    . ASN C 2 119 ? 128.376 86.940  128.392 1.00 21.31 ?  98  ASN C CG    1 
ATOM   11779 O  OD1   . ASN C 2 119 ? 128.991 87.632  127.578 1.00 21.88 ?  98  ASN C OD1   1 
ATOM   11780 N  ND2   . ASN C 2 119 ? 128.939 86.469  129.503 1.00 21.73 ?  98  ASN C ND2   1 
ATOM   11781 N  N     . ALA C 2 120 ? 126.928 89.522  126.381 1.00 22.75 ?  99  ALA C N     1 
ATOM   11782 C  CA    . ALA C 2 120 ? 126.783 90.977  126.400 1.00 23.12 ?  99  ALA C CA    1 
ATOM   11783 C  C     . ALA C 2 120 ? 125.853 91.492  125.319 1.00 23.60 ?  99  ALA C C     1 
ATOM   11784 O  O     . ALA C 2 120 ? 125.292 92.583  125.467 1.00 24.14 ?  99  ALA C O     1 
ATOM   11785 C  CB    . ALA C 2 120 ? 128.153 91.683  126.319 1.00 23.28 ?  99  ALA C CB    1 
ATOM   11786 N  N     . VAL C 2 121 ? 125.677 90.721  124.240 1.00 23.23 ?  100 VAL C N     1 
ATOM   11787 C  CA    . VAL C 2 121 ? 124.792 91.158  123.145 1.00 23.74 ?  100 VAL C CA    1 
ATOM   11788 C  C     . VAL C 2 121 ? 123.561 90.270  122.957 1.00 23.62 ?  100 VAL C C     1 
ATOM   11789 O  O     . VAL C 2 121 ? 122.439 90.760  123.047 1.00 24.51 ?  100 VAL C O     1 
ATOM   11790 C  CB    . VAL C 2 121 ? 125.545 91.328  121.808 1.00 23.19 ?  100 VAL C CB    1 
ATOM   11791 C  CG1   . VAL C 2 121 ? 124.578 91.734  120.681 1.00 24.10 ?  100 VAL C CG1   1 
ATOM   11792 C  CG2   . VAL C 2 121 ? 126.665 92.371  121.959 1.00 23.48 ?  100 VAL C CG2   1 
ATOM   11793 N  N     . HIS C 2 122 ? 123.775 88.980  122.707 1.00 23.45 ?  101 HIS C N     1 
ATOM   11794 C  CA    . HIS C 2 122 ? 122.675 88.062  122.403 1.00 23.81 ?  101 HIS C CA    1 
ATOM   11795 C  C     . HIS C 2 122 ? 121.737 87.839  123.571 1.00 24.33 ?  101 HIS C C     1 
ATOM   11796 O  O     . HIS C 2 122 ? 120.532 88.072  123.441 1.00 24.80 ?  101 HIS C O     1 
ATOM   11797 C  CB    . HIS C 2 122 ? 123.182 86.709  121.913 1.00 23.30 ?  101 HIS C CB    1 
ATOM   11798 C  CG    . HIS C 2 122 ? 123.960 86.776  120.638 1.00 22.96 ?  101 HIS C CG    1 
ATOM   11799 N  ND1   . HIS C 2 122 ? 124.607 85.679  120.107 1.00 22.78 ?  101 HIS C ND1   1 
ATOM   11800 C  CD2   . HIS C 2 122 ? 124.225 87.812  119.808 1.00 23.25 ?  101 HIS C CD2   1 
ATOM   11801 C  CE1   . HIS C 2 122 ? 125.223 86.036  118.995 1.00 22.57 ?  101 HIS C CE1   1 
ATOM   11802 N  NE2   . HIS C 2 122 ? 125.007 87.323  118.791 1.00 21.75 ?  101 HIS C NE2   1 
ATOM   11803 N  N     . ALA C 2 123 ? 122.279 87.357  124.693 1.00 24.40 ?  102 ALA C N     1 
ATOM   11804 C  CA    . ALA C 2 123 ? 121.456 87.061  125.867 1.00 24.00 ?  102 ALA C CA    1 
ATOM   11805 C  C     . ALA C 2 123 ? 120.691 88.309  126.314 1.00 24.05 ?  102 ALA C C     1 
ATOM   11806 O  O     . ALA C 2 123 ? 119.520 88.220  126.677 1.00 23.89 ?  102 ALA C O     1 
ATOM   11807 C  CB    . ALA C 2 123 ? 122.303 86.494  127.005 1.00 23.73 ?  102 ALA C CB    1 
ATOM   11808 N  N     . LYS C 2 124 ? 121.350 89.466  126.264 1.00 24.36 ?  103 LYS C N     1 
ATOM   11809 C  CA    . LYS C 2 124 ? 120.728 90.734  126.663 1.00 24.31 ?  103 LYS C CA    1 
ATOM   11810 C  C     . LYS C 2 124 ? 119.598 91.198  125.736 1.00 23.84 ?  103 LYS C C     1 
ATOM   11811 O  O     . LYS C 2 124 ? 118.582 91.720  126.214 1.00 24.21 ?  103 LYS C O     1 
ATOM   11812 C  CB    . LYS C 2 124 ? 121.769 91.841  126.855 1.00 24.93 ?  103 LYS C CB    1 
ATOM   11813 C  CG    . LYS C 2 124 ? 121.183 93.113  127.486 1.00 26.37 ?  103 LYS C CG    1 
ATOM   11814 C  CD    . LYS C 2 124 ? 122.257 94.129  127.836 1.00 29.42 ?  103 LYS C CD    1 
ATOM   11815 C  CE    . LYS C 2 124 ? 121.628 95.447  128.299 1.00 31.51 ?  103 LYS C CE    1 
ATOM   11816 N  NZ    . LYS C 2 124 ? 120.860 96.121  127.210 1.00 32.37 1  103 LYS C NZ    1 
ATOM   11817 N  N     . SER C 2 125 ? 119.765 90.999  124.427 1.00 23.52 ?  104 SER C N     1 
ATOM   11818 C  CA    . SER C 2 125 ? 118.741 91.353  123.438 0.50 23.23 ?  104 SER C CA    1 
ATOM   11819 C  C     . SER C 2 125 ? 117.386 90.723  123.760 1.00 22.91 ?  104 SER C C     1 
ATOM   11820 O  O     . SER C 2 125 ? 116.344 91.322  123.526 1.00 22.33 ?  104 SER C O     1 
ATOM   11821 C  CB    . SER C 2 125 ? 119.173 90.928  122.029 0.50 23.25 ?  104 SER C CB    1 
ATOM   11822 O  OG    . SER C 2 125 ? 120.381 91.555  121.645 0.50 24.57 ?  104 SER C OG    1 
ATOM   11823 N  N     . TYR C 2 126 ? 117.398 89.499  124.283 1.00 22.72 ?  105 TYR C N     1 
ATOM   11824 C  CA    . TYR C 2 126 ? 116.138 88.836  124.618 1.00 23.34 ?  105 TYR C CA    1 
ATOM   11825 C  C     . TYR C 2 126 ? 115.397 89.571  125.710 1.00 23.32 ?  105 TYR C C     1 
ATOM   11826 O  O     . TYR C 2 126 ? 114.177 89.626  125.677 1.00 23.17 ?  105 TYR C O     1 
ATOM   11827 C  CB    . TYR C 2 126 ? 116.325 87.371  125.020 1.00 23.45 ?  105 TYR C CB    1 
ATOM   11828 C  CG    . TYR C 2 126 ? 117.024 86.528  123.979 1.00 25.16 ?  105 TYR C CG    1 
ATOM   11829 C  CD1   . TYR C 2 126 ? 116.473 86.341  122.714 1.00 26.75 ?  105 TYR C CD1   1 
ATOM   11830 C  CD2   . TYR C 2 126 ? 118.242 85.916  124.269 1.00 26.36 ?  105 TYR C CD2   1 
ATOM   11831 C  CE1   . TYR C 2 126 ? 117.135 85.570  121.751 1.00 28.22 ?  105 TYR C CE1   1 
ATOM   11832 C  CE2   . TYR C 2 126 ? 118.907 85.152  123.322 1.00 27.17 ?  105 TYR C CE2   1 
ATOM   11833 C  CZ    . TYR C 2 126 ? 118.343 84.971  122.073 1.00 29.26 ?  105 TYR C CZ    1 
ATOM   11834 O  OH    . TYR C 2 126 ? 119.001 84.197  121.137 1.00 30.76 ?  105 TYR C OH    1 
ATOM   11835 N  N     . SER C 2 127 ? 116.141 90.129  126.669 1.00 23.61 ?  106 SER C N     1 
ATOM   11836 C  CA    . SER C 2 127 ? 115.544 90.940  127.724 1.00 24.40 ?  106 SER C CA    1 
ATOM   11837 C  C     . SER C 2 127 ? 114.968 92.235  127.168 1.00 24.55 ?  106 SER C C     1 
ATOM   11838 O  O     . SER C 2 127 ? 113.966 92.716  127.676 1.00 24.74 ?  106 SER C O     1 
ATOM   11839 C  CB    . SER C 2 127 ? 116.536 91.236  128.848 1.00 24.54 ?  106 SER C CB    1 
ATOM   11840 O  OG    . SER C 2 127 ? 116.696 90.104  129.695 1.00 24.69 ?  106 SER C OG    1 
ATOM   11841 N  N     . ASN C 2 128 ? 115.604 92.797  126.141 1.00 25.28 ?  107 ASN C N     1 
ATOM   11842 C  CA    . ASN C 2 128 ? 115.062 93.983  125.468 1.00 25.88 ?  107 ASN C CA    1 
ATOM   11843 C  C     . ASN C 2 128 ? 113.713 93.648  124.845 1.00 25.48 ?  107 ASN C C     1 
ATOM   11844 O  O     . ASN C 2 128 ? 112.755 94.409  124.967 1.00 25.23 ?  107 ASN C O     1 
ATOM   11845 C  CB    . ASN C 2 128 ? 116.019 94.516  124.395 1.00 26.40 ?  107 ASN C CB    1 
ATOM   11846 C  CG    . ASN C 2 128 ? 117.195 95.292  124.974 1.00 27.90 ?  107 ASN C CG    1 
ATOM   11847 O  OD1   . ASN C 2 128 ? 117.665 95.011  126.078 1.00 30.62 ?  107 ASN C OD1   1 
ATOM   11848 N  ND2   . ASN C 2 128 ? 117.686 96.265  124.214 1.00 27.91 ?  107 ASN C ND2   1 
ATOM   11849 N  N     . ILE C 2 129 ? 113.645 92.497  124.185 1.00 25.44 ?  108 ILE C N     1 
ATOM   11850 C  CA    . ILE C 2 129 ? 112.382 92.032  123.611 1.00 25.48 ?  108 ILE C CA    1 
ATOM   11851 C  C     . ILE C 2 129 ? 111.337 91.805  124.716 1.00 25.93 ?  108 ILE C C     1 
ATOM   11852 O  O     . ILE C 2 129 ? 110.227 92.340  124.628 1.00 25.54 ?  108 ILE C O     1 
ATOM   11853 C  CB    . ILE C 2 129 ? 112.566 90.796  122.693 1.00 25.21 ?  108 ILE C CB    1 
ATOM   11854 C  CG1   . ILE C 2 129 ? 113.475 91.161  121.506 1.00 25.96 ?  108 ILE C CG1   1 
ATOM   11855 C  CG2   . ILE C 2 129 ? 111.200 90.268  122.206 1.00 24.43 ?  108 ILE C CG2   1 
ATOM   11856 C  CD1   . ILE C 2 129 ? 113.969 89.979  120.674 1.00 26.11 ?  108 ILE C CD1   1 
ATOM   11857 N  N     . PHE C 2 130 ? 111.695 91.042  125.754 1.00 26.04 ?  109 PHE C N     1 
ATOM   11858 C  CA    . PHE C 2 130 ? 110.778 90.780  126.879 1.00 26.66 ?  109 PHE C CA    1 
ATOM   11859 C  C     . PHE C 2 130 ? 110.254 92.068  127.520 1.00 27.38 ?  109 PHE C C     1 
ATOM   11860 O  O     . PHE C 2 130 ? 109.050 92.192  127.798 1.00 27.22 ?  109 PHE C O     1 
ATOM   11861 C  CB    . PHE C 2 130 ? 111.456 89.932  127.978 1.00 26.98 ?  109 PHE C CB    1 
ATOM   11862 C  CG    . PHE C 2 130 ? 111.704 88.492  127.601 1.00 27.46 ?  109 PHE C CG    1 
ATOM   11863 C  CD1   . PHE C 2 130 ? 110.886 87.828  126.695 1.00 28.57 ?  109 PHE C CD1   1 
ATOM   11864 C  CD2   . PHE C 2 130 ? 112.762 87.791  128.182 1.00 28.51 ?  109 PHE C CD2   1 
ATOM   11865 C  CE1   . PHE C 2 130 ? 111.125 86.497  126.357 1.00 29.17 ?  109 PHE C CE1   1 
ATOM   11866 C  CE2   . PHE C 2 130 ? 113.008 86.450  127.856 1.00 29.27 ?  109 PHE C CE2   1 
ATOM   11867 C  CZ    . PHE C 2 130 ? 112.188 85.799  126.947 1.00 28.83 ?  109 PHE C CZ    1 
ATOM   11868 N  N     . MET C 2 131 ? 111.151 93.026  127.755 1.00 27.52 ?  110 MET C N     1 
ATOM   11869 C  CA    . MET C 2 131 ? 110.783 94.260  128.458 1.00 29.07 ?  110 MET C CA    1 
ATOM   11870 C  C     . MET C 2 131 ? 109.843 95.148  127.660 1.00 29.58 ?  110 MET C C     1 
ATOM   11871 O  O     . MET C 2 131 ? 109.077 95.920  128.236 1.00 30.07 ?  110 MET C O     1 
ATOM   11872 C  CB    . MET C 2 131 ? 112.015 95.052  128.888 1.00 28.96 ?  110 MET C CB    1 
ATOM   11873 C  CG    . MET C 2 131 ? 112.658 94.513  130.149 1.00 31.09 ?  110 MET C CG    1 
ATOM   11874 S  SD    . MET C 2 131 ? 114.149 95.404  130.649 1.00 35.43 ?  110 MET C SD    1 
ATOM   11875 C  CE    . MET C 2 131 ? 115.284 95.024  129.318 1.00 33.13 ?  110 MET C CE    1 
ATOM   11876 N  N     . THR C 2 132 ? 109.907 95.025  126.340 1.00 30.25 ?  111 THR C N     1 
ATOM   11877 C  CA    . THR C 2 132 ? 109.007 95.739  125.439 1.00 30.97 ?  111 THR C CA    1 
ATOM   11878 C  C     . THR C 2 132 ? 107.613 95.104  125.412 1.00 31.36 ?  111 THR C C     1 
ATOM   11879 O  O     . THR C 2 132 ? 106.600 95.786  125.617 1.00 31.60 ?  111 THR C O     1 
ATOM   11880 C  CB    . THR C 2 132 ? 109.609 95.792  124.006 1.00 30.88 ?  111 THR C CB    1 
ATOM   11881 O  OG1   . THR C 2 132 ? 110.844 96.516  124.044 1.00 29.86 ?  111 THR C OG1   1 
ATOM   11882 C  CG2   . THR C 2 132 ? 108.660 96.479  123.012 1.00 31.44 ?  111 THR C CG2   1 
ATOM   11883 N  N     . LEU C 2 133 ? 107.571 93.797  125.171 1.00 31.34 ?  112 LEU C N     1 
ATOM   11884 C  CA    . LEU C 2 133 ? 106.313 93.097  124.905 1.00 31.68 ?  112 LEU C CA    1 
ATOM   11885 C  C     . LEU C 2 133 ? 105.523 92.634  126.132 1.00 31.96 ?  112 LEU C C     1 
ATOM   11886 O  O     . LEU C 2 133 ? 104.295 92.572  126.092 1.00 31.69 ?  112 LEU C O     1 
ATOM   11887 C  CB    . LEU C 2 133 ? 106.568 91.901  123.993 1.00 31.35 ?  112 LEU C CB    1 
ATOM   11888 C  CG    . LEU C 2 133 ? 107.320 92.161  122.683 1.00 32.14 ?  112 LEU C CG    1 
ATOM   11889 C  CD1   . LEU C 2 133 ? 107.532 90.850  121.964 1.00 32.15 ?  112 LEU C CD1   1 
ATOM   11890 C  CD2   . LEU C 2 133 ? 106.573 93.159  121.801 1.00 32.39 ?  112 LEU C CD2   1 
ATOM   11891 N  N     . ALA C 2 134 ? 106.223 92.309  127.214 1.00 32.12 ?  113 ALA C N     1 
ATOM   11892 C  CA    . ALA C 2 134 ? 105.599 91.616  128.333 1.00 32.53 ?  113 ALA C CA    1 
ATOM   11893 C  C     . ALA C 2 134 ? 105.659 92.390  129.643 1.00 33.15 ?  113 ALA C C     1 
ATOM   11894 O  O     . ALA C 2 134 ? 106.623 93.110  129.893 1.00 32.47 ?  113 ALA C O     1 
ATOM   11895 C  CB    . ALA C 2 134 ? 106.223 90.225  128.506 1.00 32.20 ?  113 ALA C CB    1 
ATOM   11896 N  N     . PRO C 2 135 ? 104.626 92.226  130.494 1.00 34.27 ?  114 PRO C N     1 
ATOM   11897 C  CA    . PRO C 2 135 ? 104.665 92.793  131.836 1.00 35.35 ?  114 PRO C CA    1 
ATOM   11898 C  C     . PRO C 2 135 ? 105.628 92.007  132.719 1.00 36.17 ?  114 PRO C C     1 
ATOM   11899 O  O     . PRO C 2 135 ? 105.897 90.833  132.451 1.00 35.92 ?  114 PRO C O     1 
ATOM   11900 C  CB    . PRO C 2 135 ? 103.219 92.657  132.328 1.00 35.48 ?  114 PRO C CB    1 
ATOM   11901 C  CG    . PRO C 2 135 ? 102.630 91.559  131.530 1.00 34.94 ?  114 PRO C CG    1 
ATOM   11902 C  CD    . PRO C 2 135 ? 103.376 91.486  130.231 1.00 34.50 ?  114 PRO C CD    1 
ATOM   11903 N  N     . THR C 2 136 ? 106.146 92.661  133.754 1.00 37.30 ?  115 THR C N     1 
ATOM   11904 C  CA    . THR C 2 136 ? 107.169 92.086  134.634 1.00 38.49 ?  115 THR C CA    1 
ATOM   11905 C  C     . THR C 2 136 ? 106.845 90.687  135.179 1.00 38.48 ?  115 THR C C     1 
ATOM   11906 O  O     . THR C 2 136 ? 107.743 89.845  135.283 1.00 38.74 ?  115 THR C O     1 
ATOM   11907 C  CB    . THR C 2 136 ? 107.476 93.039  135.808 1.00 38.95 ?  115 THR C CB    1 
ATOM   11908 O  OG1   . THR C 2 136 ? 107.772 94.337  135.285 1.00 40.08 ?  115 THR C OG1   1 
ATOM   11909 C  CG2   . THR C 2 136 ? 108.666 92.546  136.632 1.00 39.82 ?  115 THR C CG2   1 
ATOM   11910 N  N     . GLU C 2 137 ? 105.576 90.448  135.516 1.00 38.89 ?  116 GLU C N     1 
ATOM   11911 C  CA    . GLU C 2 137 ? 105.151 89.171  136.106 1.00 38.65 ?  116 GLU C CA    1 
ATOM   11912 C  C     . GLU C 2 137 ? 105.289 88.015  135.121 1.00 37.38 ?  116 GLU C C     1 
ATOM   11913 O  O     . GLU C 2 137 ? 105.673 86.911  135.502 1.00 37.22 ?  116 GLU C O     1 
ATOM   11914 C  CB    . GLU C 2 137 ? 103.720 89.237  136.682 1.00 39.52 ?  116 GLU C CB    1 
ATOM   11915 C  CG    . GLU C 2 137 ? 102.568 89.341  135.654 1.00 41.90 ?  116 GLU C CG    1 
ATOM   11916 C  CD    . GLU C 2 137 ? 101.708 90.608  135.803 1.00 46.43 ?  116 GLU C CD    1 
ATOM   11917 O  OE1   . GLU C 2 137 ? 102.102 91.542  136.541 1.00 47.84 ?  116 GLU C OE1   1 
ATOM   11918 O  OE2   . GLU C 2 137 ? 100.624 90.665  135.171 1.00 47.52 -1 116 GLU C OE2   1 
ATOM   11919 N  N     . THR C 2 138 ? 104.984 88.288  133.855 1.00 36.05 ?  117 THR C N     1 
ATOM   11920 C  CA    . THR C 2 138 ? 105.122 87.303  132.794 1.00 34.88 ?  117 THR C CA    1 
ATOM   11921 C  C     . THR C 2 138 ? 106.600 87.028  132.534 1.00 33.58 ?  117 THR C C     1 
ATOM   11922 O  O     . THR C 2 138 ? 106.983 85.883  132.280 1.00 33.61 ?  117 THR C O     1 
ATOM   11923 C  CB    . THR C 2 138 ? 104.426 87.768  131.508 1.00 34.85 ?  117 THR C CB    1 
ATOM   11924 O  OG1   . THR C 2 138 ? 103.081 88.148  131.818 1.00 35.98 ?  117 THR C OG1   1 
ATOM   11925 C  CG2   . THR C 2 138 ? 104.404 86.656  130.468 1.00 34.92 ?  117 THR C CG2   1 
ATOM   11926 N  N     . ILE C 2 139 ? 107.417 88.077  132.604 1.00 32.29 ?  118 ILE C N     1 
ATOM   11927 C  CA    . ILE C 2 139 ? 108.868 87.935  132.486 1.00 31.19 ?  118 ILE C CA    1 
ATOM   11928 C  C     . ILE C 2 139 ? 109.426 87.087  133.644 1.00 30.85 ?  118 ILE C C     1 
ATOM   11929 O  O     . ILE C 2 139 ? 110.174 86.138  133.408 1.00 29.77 ?  118 ILE C O     1 
ATOM   11930 C  CB    . ILE C 2 139 ? 109.602 89.306  132.383 1.00 31.25 ?  118 ILE C CB    1 
ATOM   11931 C  CG1   . ILE C 2 139 ? 109.097 90.118  131.177 1.00 30.12 ?  118 ILE C CG1   1 
ATOM   11932 C  CG2   . ILE C 2 139 ? 111.123 89.111  132.287 1.00 30.21 ?  118 ILE C CG2   1 
ATOM   11933 C  CD1   . ILE C 2 139 ? 109.672 91.545  131.102 1.00 29.41 ?  118 ILE C CD1   1 
ATOM   11934 N  N     . ASN C 2 140 ? 109.043 87.422  134.881 1.00 31.17 ?  119 ASN C N     1 
ATOM   11935 C  CA    . ASN C 2 140 ? 109.456 86.650  136.065 1.00 31.76 ?  119 ASN C CA    1 
ATOM   11936 C  C     . ASN C 2 140 ? 109.072 85.171  135.952 1.00 31.25 ?  119 ASN C C     1 
ATOM   11937 O  O     . ASN C 2 140 ? 109.889 84.292  136.229 1.00 31.47 ?  119 ASN C O     1 
ATOM   11938 C  CB    . ASN C 2 140 ? 108.858 87.227  137.358 1.00 32.65 ?  119 ASN C CB    1 
ATOM   11939 C  CG    . ASN C 2 140 ? 109.478 88.558  137.770 1.00 35.14 ?  119 ASN C CG    1 
ATOM   11940 O  OD1   . ASN C 2 140 ? 110.631 88.864  137.449 1.00 36.75 ?  119 ASN C OD1   1 
ATOM   11941 N  ND2   . ASN C 2 140 ? 108.706 89.350  138.519 1.00 38.05 ?  119 ASN C ND2   1 
ATOM   11942 N  N     . GLU C 2 141 ? 107.833 84.918  135.534 1.00 30.96 ?  120 GLU C N     1 
ATOM   11943 C  CA    . GLU C 2 141 ? 107.306 83.564  135.366 1.00 30.36 ?  120 GLU C CA    1 
ATOM   11944 C  C     . GLU C 2 141 ? 108.085 82.753  134.328 1.00 28.60 ?  120 GLU C C     1 
ATOM   11945 O  O     . GLU C 2 141 ? 108.370 81.580  134.555 1.00 27.94 ?  120 GLU C O     1 
ATOM   11946 C  CB    . GLU C 2 141 ? 105.823 83.603  134.986 1.00 30.86 ?  120 GLU C CB    1 
ATOM   11947 C  CG    . GLU C 2 141 ? 104.877 83.903  136.144 1.00 34.89 ?  120 GLU C CG    1 
ATOM   11948 C  CD    . GLU C 2 141 ? 103.443 84.127  135.684 1.00 39.82 ?  120 GLU C CD    1 
ATOM   11949 O  OE1   . GLU C 2 141 ? 103.116 83.789  134.520 1.00 41.95 ?  120 GLU C OE1   1 
ATOM   11950 O  OE2   . GLU C 2 141 ? 102.637 84.638  136.489 1.00 41.94 -1 120 GLU C OE2   1 
ATOM   11951 N  N     . VAL C 2 142 ? 108.427 83.363  133.196 1.00 27.29 ?  121 VAL C N     1 
ATOM   11952 C  CA    . VAL C 2 142 ? 109.157 82.606  132.157 1.00 25.89 ?  121 VAL C CA    1 
ATOM   11953 C  C     . VAL C 2 142 ? 110.584 82.246  132.585 1.00 25.11 ?  121 VAL C C     1 
ATOM   11954 O  O     . VAL C 2 142 ? 111.092 81.182  132.232 1.00 24.23 ?  121 VAL C O     1 
ATOM   11955 C  CB    . VAL C 2 142 ? 109.095 83.267  130.736 1.00 25.99 ?  121 VAL C CB    1 
ATOM   11956 C  CG1   . VAL C 2 142 ? 110.180 84.328  130.534 1.00 25.21 ?  121 VAL C CG1   1 
ATOM   11957 C  CG2   . VAL C 2 142 ? 109.211 82.203  129.655 1.00 25.78 ?  121 VAL C CG2   1 
ATOM   11958 N  N     . PHE C 2 143 ? 111.230 83.114  133.358 1.00 24.69 ?  122 PHE C N     1 
ATOM   11959 C  CA    . PHE C 2 143 ? 112.564 82.784  133.881 1.00 24.77 ?  122 PHE C CA    1 
ATOM   11960 C  C     . PHE C 2 143 ? 112.495 81.699  134.971 1.00 24.99 ?  122 PHE C C     1 
ATOM   11961 O  O     . PHE C 2 143 ? 113.388 80.859  135.083 1.00 24.73 ?  122 PHE C O     1 
ATOM   11962 C  CB    . PHE C 2 143 ? 113.323 84.037  134.334 1.00 24.83 ?  122 PHE C CB    1 
ATOM   11963 C  CG    . PHE C 2 143 ? 113.916 84.821  133.183 1.00 25.12 ?  122 PHE C CG    1 
ATOM   11964 C  CD1   . PHE C 2 143 ? 115.031 84.343  132.497 1.00 26.58 ?  122 PHE C CD1   1 
ATOM   11965 C  CD2   . PHE C 2 143 ? 113.350 86.019  132.773 1.00 24.49 ?  122 PHE C CD2   1 
ATOM   11966 C  CE1   . PHE C 2 143 ? 115.572 85.059  131.421 1.00 26.96 ?  122 PHE C CE1   1 
ATOM   11967 C  CE2   . PHE C 2 143 ? 113.879 86.737  131.711 1.00 25.79 ?  122 PHE C CE2   1 
ATOM   11968 C  CZ    . PHE C 2 143 ? 114.992 86.258  131.027 1.00 26.45 ?  122 PHE C CZ    1 
ATOM   11969 N  N     . GLU C 2 144 ? 111.419 81.707  135.754 1.00 25.22 ?  123 GLU C N     1 
ATOM   11970 C  CA    . GLU C 2 144 ? 111.155 80.605  136.684 1.00 25.72 ?  123 GLU C CA    1 
ATOM   11971 C  C     . GLU C 2 144 ? 110.901 79.305  135.923 1.00 25.08 ?  123 GLU C C     1 
ATOM   11972 O  O     . GLU C 2 144 ? 111.378 78.240  136.321 1.00 24.67 ?  123 GLU C O     1 
ATOM   11973 C  CB    . GLU C 2 144 ? 109.991 80.937  137.614 1.00 26.23 ?  123 GLU C CB    1 
ATOM   11974 C  CG    . GLU C 2 144 ? 110.352 81.990  138.648 1.00 29.96 ?  123 GLU C CG    1 
ATOM   11975 C  CD    . GLU C 2 144 ? 111.601 81.621  139.432 1.00 33.82 ?  123 GLU C CD    1 
ATOM   11976 O  OE1   . GLU C 2 144 ? 111.557 80.618  140.176 1.00 36.54 ?  123 GLU C OE1   1 
ATOM   11977 O  OE2   . GLU C 2 144 ? 112.629 82.318  139.291 1.00 35.84 -1 123 GLU C OE2   1 
ATOM   11978 N  N     . TRP C 2 145 ? 110.175 79.408  134.813 1.00 24.21 ?  124 TRP C N     1 
ATOM   11979 C  CA    . TRP C 2 145 ? 109.898 78.260  133.951 1.00 23.99 ?  124 TRP C CA    1 
ATOM   11980 C  C     . TRP C 2 145 ? 111.160 77.621  133.354 1.00 23.95 ?  124 TRP C C     1 
ATOM   11981 O  O     . TRP C 2 145 ? 111.232 76.382  133.248 1.00 23.31 ?  124 TRP C O     1 
ATOM   11982 C  CB    . TRP C 2 145 ? 108.903 78.640  132.842 1.00 24.13 ?  124 TRP C CB    1 
ATOM   11983 C  CG    . TRP C 2 145 ? 108.795 77.603  131.747 1.00 24.37 ?  124 TRP C CG    1 
ATOM   11984 C  CD1   . TRP C 2 145 ? 107.948 76.521  131.708 1.00 24.76 ?  124 TRP C CD1   1 
ATOM   11985 C  CD2   . TRP C 2 145 ? 109.560 77.561  130.536 1.00 23.31 ?  124 TRP C CD2   1 
ATOM   11986 N  NE1   . TRP C 2 145 ? 108.153 75.806  130.542 1.00 24.97 ?  124 TRP C NE1   1 
ATOM   11987 C  CE2   . TRP C 2 145 ? 109.131 76.423  129.807 1.00 24.20 ?  124 TRP C CE2   1 
ATOM   11988 C  CE3   . TRP C 2 145 ? 110.573 78.366  129.998 1.00 23.76 ?  124 TRP C CE3   1 
ATOM   11989 C  CZ2   . TRP C 2 145 ? 109.682 76.077  128.565 1.00 23.41 ?  124 TRP C CZ2   1 
ATOM   11990 C  CZ3   . TRP C 2 145 ? 111.123 78.020  128.765 1.00 23.29 ?  124 TRP C CZ3   1 
ATOM   11991 C  CH2   . TRP C 2 145 ? 110.668 76.886  128.061 1.00 22.93 ?  124 TRP C CH2   1 
ATOM   11992 N  N     . VAL C 2 146 ? 112.150 78.427  132.954 1.00 23.35 ?  125 VAL C N     1 
ATOM   11993 C  CA    . VAL C 2 146 ? 113.409 77.804  132.469 1.00 23.53 ?  125 VAL C CA    1 
ATOM   11994 C  C     . VAL C 2 146 ? 114.091 76.952  133.547 1.00 23.73 ?  125 VAL C C     1 
ATOM   11995 O  O     . VAL C 2 146 ? 114.565 75.866  133.248 1.00 23.03 ?  125 VAL C O     1 
ATOM   11996 C  CB    . VAL C 2 146 ? 114.411 78.751  131.656 1.00 23.63 ?  125 VAL C CB    1 
ATOM   11997 C  CG1   . VAL C 2 146 ? 113.873 80.132  131.398 1.00 24.40 ?  125 VAL C CG1   1 
ATOM   11998 C  CG2   . VAL C 2 146 ? 115.846 78.772  132.217 1.00 22.97 ?  125 VAL C CG2   1 
ATOM   11999 N  N     . LYS C 2 147 ? 114.080 77.425  134.796 1.00 24.06 ?  126 LYS C N     1 
ATOM   12000 C  CA    . LYS C 2 147 ? 114.731 76.704  135.903 1.00 25.41 ?  126 LYS C CA    1 
ATOM   12001 C  C     . LYS C 2 147 ? 114.140 75.315  136.159 1.00 25.82 ?  126 LYS C C     1 
ATOM   12002 O  O     . LYS C 2 147 ? 114.863 74.403  136.566 1.00 26.08 ?  126 LYS C O     1 
ATOM   12003 C  CB    . LYS C 2 147 ? 114.661 77.514  137.200 1.00 25.49 ?  126 LYS C CB    1 
ATOM   12004 C  CG    . LYS C 2 147 ? 115.486 78.784  137.214 1.00 27.52 ?  126 LYS C CG    1 
ATOM   12005 C  CD    . LYS C 2 147 ? 115.248 79.523  138.526 1.00 30.43 ?  126 LYS C CD    1 
ATOM   12006 C  CE    . LYS C 2 147 ? 115.757 80.947  138.468 1.00 33.10 ?  126 LYS C CE    1 
ATOM   12007 N  NZ    . LYS C 2 147 ? 115.399 81.671  139.720 1.00 34.86 1  126 LYS C NZ    1 
ATOM   12008 N  N     . GLN C 2 148 ? 112.838 75.163  135.922 1.00 26.45 ?  127 GLN C N     1 
ATOM   12009 C  CA    . GLN C 2 148 ? 112.128 73.923  136.247 1.00 26.85 ?  127 GLN C CA    1 
ATOM   12010 C  C     . GLN C 2 148 ? 111.804 73.039  135.041 1.00 26.01 ?  127 GLN C C     1 
ATOM   12011 O  O     . GLN C 2 148 ? 111.307 71.924  135.214 1.00 26.12 ?  127 GLN C O     1 
ATOM   12012 C  CB    . GLN C 2 148 ? 110.853 74.212  137.062 1.00 28.08 ?  127 GLN C CB    1 
ATOM   12013 C  CG    . GLN C 2 148 ? 109.792 75.050  136.343 1.00 30.69 ?  127 GLN C CG    1 
ATOM   12014 C  CD    . GLN C 2 148 ? 109.016 74.267  135.286 1.00 34.64 ?  127 GLN C CD    1 
ATOM   12015 O  OE1   . GLN C 2 148 ? 109.108 74.557  134.081 1.00 33.80 ?  127 GLN C OE1   1 
ATOM   12016 N  NE2   . GLN C 2 148 ? 108.254 73.259  135.731 1.00 36.24 ?  127 GLN C NE2   1 
ATOM   12017 N  N     . ASN C 2 149 ? 112.072 73.532  133.829 1.00 24.97 ?  128 ASN C N     1 
ATOM   12018 C  CA    . ASN C 2 149 ? 111.806 72.765  132.616 1.00 24.03 ?  128 ASN C CA    1 
ATOM   12019 C  C     . ASN C 2 149 ? 112.850 71.676  132.428 1.00 24.13 ?  128 ASN C C     1 
ATOM   12020 O  O     . ASN C 2 149 ? 114.038 71.988  132.302 1.00 22.93 ?  128 ASN C O     1 
ATOM   12021 C  CB    . ASN C 2 149 ? 111.817 73.673  131.397 1.00 23.97 ?  128 ASN C CB    1 
ATOM   12022 C  CG    . ASN C 2 149 ? 111.410 72.947  130.138 1.00 23.94 ?  128 ASN C CG    1 
ATOM   12023 O  OD1   . ASN C 2 149 ? 112.246 72.376  129.439 1.00 24.85 ?  128 ASN C OD1   1 
ATOM   12024 N  ND2   . ASN C 2 149 ? 110.112 72.919  129.866 1.00 24.76 ?  128 ASN C ND2   1 
ATOM   12025 N  N     . LYS C 2 150 ? 112.412 70.415  132.379 1.00 24.32 ?  129 LYS C N     1 
ATOM   12026 C  CA    . LYS C 2 150 ? 113.353 69.278  132.405 1.00 24.77 ?  129 LYS C CA    1 
ATOM   12027 C  C     . LYS C 2 150 ? 114.214 69.108  131.151 1.00 24.54 ?  129 LYS C C     1 
ATOM   12028 O  O     . LYS C 2 150 ? 115.355 68.653  131.243 1.00 24.17 ?  129 LYS C O     1 
ATOM   12029 C  CB    . LYS C 2 150 ? 112.649 67.967  132.778 1.00 25.27 ?  129 LYS C CB    1 
ATOM   12030 C  CG    . LYS C 2 150 ? 111.575 67.499  131.818 1.00 28.72 ?  129 LYS C CG    1 
ATOM   12031 C  CD    . LYS C 2 150 ? 111.215 66.042  132.115 1.00 33.40 ?  129 LYS C CD    1 
ATOM   12032 C  CE    . LYS C 2 150 ? 109.840 65.693  131.578 1.00 36.77 ?  129 LYS C CE    1 
ATOM   12033 N  NZ    . LYS C 2 150 ? 109.422 64.342  132.066 1.00 39.66 1  129 LYS C NZ    1 
ATOM   12034 N  N     . TYR C 2 151 ? 113.665 69.467  129.985 1.00 23.92 ?  130 TYR C N     1 
ATOM   12035 C  CA    . TYR C 2 151 ? 114.405 69.369  128.720 1.00 24.12 ?  130 TYR C CA    1 
ATOM   12036 C  C     . TYR C 2 151 ? 115.486 70.432  128.600 1.00 23.54 ?  130 TYR C C     1 
ATOM   12037 O  O     . TYR C 2 151 ? 116.589 70.164  128.102 1.00 23.32 ?  130 TYR C O     1 
ATOM   12038 C  CB    . TYR C 2 151 ? 113.436 69.425  127.524 1.00 24.53 ?  130 TYR C CB    1 
ATOM   12039 C  CG    . TYR C 2 151 ? 112.214 68.558  127.736 1.00 25.83 ?  130 TYR C CG    1 
ATOM   12040 C  CD1   . TYR C 2 151 ? 112.334 67.172  127.847 1.00 26.57 ?  130 TYR C CD1   1 
ATOM   12041 C  CD2   . TYR C 2 151 ? 110.943 69.128  127.871 1.00 27.87 ?  130 TYR C CD2   1 
ATOM   12042 C  CE1   . TYR C 2 151 ? 111.222 66.366  128.063 1.00 29.65 ?  130 TYR C CE1   1 
ATOM   12043 C  CE2   . TYR C 2 151 ? 109.816 68.326  128.092 1.00 29.91 ?  130 TYR C CE2   1 
ATOM   12044 C  CZ    . TYR C 2 151 ? 109.968 66.949  128.188 1.00 31.19 ?  130 TYR C CZ    1 
ATOM   12045 O  OH    . TYR C 2 151 ? 108.869 66.143  128.405 1.00 34.44 ?  130 TYR C OH    1 
ATOM   12046 N  N     . LEU C 2 152 ? 115.163 71.638  129.056 1.00 23.38 ?  131 LEU C N     1 
ATOM   12047 C  CA    . LEU C 2 152 ? 116.104 72.743  129.046 1.00 23.43 ?  131 LEU C CA    1 
ATOM   12048 C  C     . LEU C 2 152 ? 117.218 72.490  130.067 1.00 23.37 ?  131 LEU C C     1 
ATOM   12049 O  O     . LEU C 2 152 ? 118.394 72.726  129.774 1.00 23.05 ?  131 LEU C O     1 
ATOM   12050 C  CB    . LEU C 2 152 ? 115.354 74.040  129.346 1.00 23.73 ?  131 LEU C CB    1 
ATOM   12051 C  CG    . LEU C 2 152 ? 115.535 75.347  128.584 1.00 24.71 ?  131 LEU C CG    1 
ATOM   12052 C  CD1   . LEU C 2 152 ? 116.179 75.215  127.193 1.00 21.63 ?  131 LEU C CD1   1 
ATOM   12053 C  CD2   . LEU C 2 152 ? 114.193 76.035  128.485 1.00 26.87 ?  131 LEU C CD2   1 
ATOM   12054 N  N     . GLN C 2 153 ? 116.857 72.011  131.261 1.00 22.80 ?  132 GLN C N     1 
ATOM   12055 C  CA    . GLN C 2 153 ? 117.882 71.605  132.237 1.00 22.70 ?  132 GLN C CA    1 
ATOM   12056 C  C     . GLN C 2 153 ? 118.768 70.460  131.740 1.00 22.54 ?  132 GLN C C     1 
ATOM   12057 O  O     . GLN C 2 153 ? 119.997 70.513  131.903 1.00 21.73 ?  132 GLN C O     1 
ATOM   12058 C  CB    . GLN C 2 153 ? 117.281 71.297  133.611 1.00 23.07 ?  132 GLN C CB    1 
ATOM   12059 C  CG    . GLN C 2 153 ? 116.641 72.520  134.266 1.00 21.83 ?  132 GLN C CG    1 
ATOM   12060 C  CD    . GLN C 2 153 ? 117.613 73.688  134.454 1.00 22.34 ?  132 GLN C CD    1 
ATOM   12061 O  OE1   . GLN C 2 153 ? 118.730 73.514  134.946 1.00 24.07 ?  132 GLN C OE1   1 
ATOM   12062 N  NE2   . GLN C 2 153 ? 117.179 74.883  134.076 1.00 22.26 ?  132 GLN C NE2   1 
ATOM   12063 N  N     . LYS C 2 154 ? 118.160 69.439  131.129 1.00 22.53 ?  133 LYS C N     1 
ATOM   12064 C  CA    . LYS C 2 154 ? 118.946 68.337  130.574 1.00 22.84 ?  133 LYS C CA    1 
ATOM   12065 C  C     . LYS C 2 154 ? 119.943 68.815  129.516 1.00 22.42 ?  133 LYS C C     1 
ATOM   12066 O  O     . LYS C 2 154 ? 121.100 68.412  129.551 1.00 21.90 ?  133 LYS C O     1 
ATOM   12067 C  CB    . LYS C 2 154 ? 118.067 67.185  130.034 1.00 22.96 ?  133 LYS C CB    1 
ATOM   12068 C  CG    . LYS C 2 154 ? 118.874 65.973  129.474 1.00 23.45 ?  133 LYS C CG    1 
ATOM   12069 C  CD    . LYS C 2 154 ? 119.706 65.239  130.549 1.00 26.74 ?  133 LYS C CD    1 
ATOM   12070 C  CE    . LYS C 2 154 ? 120.446 64.030  129.961 1.00 27.93 ?  133 LYS C CE    1 
ATOM   12071 N  NZ    . LYS C 2 154 ? 121.417 63.414  130.904 1.00 27.86 1  133 LYS C NZ    1 
ATOM   12072 N  N     . LYS C 2 155 ? 119.515 69.683  128.594 1.00 22.77 ?  134 LYS C N     1 
ATOM   12073 C  CA    . LYS C 2 155 ? 120.420 70.092  127.515 1.00 22.87 ?  134 LYS C CA    1 
ATOM   12074 C  C     . LYS C 2 155 ? 121.565 70.956  128.035 1.00 22.30 ?  134 LYS C C     1 
ATOM   12075 O  O     . LYS C 2 155 ? 122.720 70.764  127.619 1.00 21.89 ?  134 LYS C O     1 
ATOM   12076 C  CB    . LYS C 2 155 ? 119.686 70.709  126.301 1.00 23.33 ?  134 LYS C CB    1 
ATOM   12077 C  CG    . LYS C 2 155 ? 119.185 72.124  126.440 1.00 24.25 ?  134 LYS C CG    1 
ATOM   12078 C  CD    . LYS C 2 155 ? 118.493 72.598  125.151 1.00 26.87 ?  134 LYS C CD    1 
ATOM   12079 C  CE    . LYS C 2 155 ? 117.028 72.175  125.119 1.00 28.26 ?  134 LYS C CE    1 
ATOM   12080 N  NZ    . LYS C 2 155 ? 116.300 72.903  124.036 1.00 28.97 1  134 LYS C NZ    1 
ATOM   12081 N  N     . ALA C 2 156 ? 121.254 71.856  128.967 1.00 21.96 ?  135 ALA C N     1 
ATOM   12082 C  CA    . ALA C 2 156 ? 122.286 72.623  129.692 1.00 22.43 ?  135 ALA C CA    1 
ATOM   12083 C  C     . ALA C 2 156 ? 123.248 71.728  130.475 1.00 22.02 ?  135 ALA C C     1 
ATOM   12084 O  O     . ALA C 2 156 ? 124.455 71.951  130.447 1.00 22.60 ?  135 ALA C O     1 
ATOM   12085 C  CB    . ALA C 2 156 ? 121.650 73.660  130.642 1.00 22.05 ?  135 ALA C CB    1 
ATOM   12086 N  N     . GLN C 2 157 ? 122.715 70.734  131.187 1.00 21.97 ?  136 GLN C N     1 
ATOM   12087 C  CA    . GLN C 2 157 ? 123.554 69.795  131.943 1.00 22.10 ?  136 GLN C CA    1 
ATOM   12088 C  C     . GLN C 2 157 ? 124.558 69.110  131.039 1.00 21.87 ?  136 GLN C C     1 
ATOM   12089 O  O     . GLN C 2 157 ? 125.729 68.985  131.396 1.00 21.75 ?  136 GLN C O     1 
ATOM   12090 C  CB    . GLN C 2 157 ? 122.716 68.707  132.614 1.00 22.50 ?  136 GLN C CB    1 
ATOM   12091 C  CG    . GLN C 2 157 ? 122.038 69.123  133.911 1.00 23.55 ?  136 GLN C CG    1 
ATOM   12092 C  CD    . GLN C 2 157 ? 120.908 68.170  134.259 1.00 26.93 ?  136 GLN C CD    1 
ATOM   12093 O  OE1   . GLN C 2 157 ? 120.909 67.021  133.822 1.00 26.36 ?  136 GLN C OE1   1 
ATOM   12094 N  NE2   . GLN C 2 157 ? 119.930 68.647  135.021 1.00 28.09 ?  136 GLN C NE2   1 
ATOM   12095 N  N     . MET C 2 158 ? 124.082 68.656  129.881 1.00 21.38 ?  137 MET C N     1 
ATOM   12096 C  CA    . MET C 2 158 ? 124.902 67.899  128.948 1.00 22.08 ?  137 MET C CA    1 
ATOM   12097 C  C     . MET C 2 158 ? 125.977 68.758  128.292 1.00 21.70 ?  137 MET C C     1 
ATOM   12098 O  O     . MET C 2 158 ? 127.129 68.341  128.156 1.00 21.83 ?  137 MET C O     1 
ATOM   12099 C  CB    . MET C 2 158 ? 124.033 67.284  127.856 1.00 22.05 ?  137 MET C CB    1 
ATOM   12100 C  CG    . MET C 2 158 ? 123.210 66.071  128.306 1.00 23.93 ?  137 MET C CG    1 
ATOM   12101 S  SD    . MET C 2 158 ? 122.067 65.582  126.999 1.00 27.75 ?  137 MET C SD    1 
ATOM   12102 C  CE    . MET C 2 158 ? 123.240 64.946  125.792 1.00 26.00 ?  137 MET C CE    1 
ATOM   12103 N  N     . ILE C 2 159 ? 125.585 69.944  127.850 1.00 20.90 ?  138 ILE C N     1 
ATOM   12104 C  CA    . ILE C 2 159 ? 126.509 70.806  127.133 1.00 20.60 ?  138 ILE C CA    1 
ATOM   12105 C  C     . ILE C 2 159 ? 127.560 71.373  128.092 1.00 20.36 ?  138 ILE C C     1 
ATOM   12106 O  O     . ILE C 2 159 ? 128.759 71.282  127.817 1.00 19.65 ?  138 ILE C O     1 
ATOM   12107 C  CB    . ILE C 2 159 ? 125.762 71.926  126.350 1.00 20.17 ?  138 ILE C CB    1 
ATOM   12108 C  CG1   . ILE C 2 159 ? 124.915 71.323  125.214 1.00 20.66 ?  138 ILE C CG1   1 
ATOM   12109 C  CG2   . ILE C 2 159 ? 126.739 73.015  125.875 1.00 20.62 ?  138 ILE C CG2   1 
ATOM   12110 C  CD1   . ILE C 2 159 ? 125.669 70.615  124.085 1.00 22.17 ?  138 ILE C CD1   1 
ATOM   12111 N  N     . VAL C 2 160 ? 127.111 71.925  129.219 1.00 19.58 ?  139 VAL C N     1 
ATOM   12112 C  CA    . VAL C 2 160 ? 128.012 72.540  130.199 1.00 19.88 ?  139 VAL C CA    1 
ATOM   12113 C  C     . VAL C 2 160 ? 128.909 71.481  130.847 1.00 19.44 ?  139 VAL C C     1 
ATOM   12114 O  O     . VAL C 2 160 ? 130.047 71.760  131.207 1.00 19.88 ?  139 VAL C O     1 
ATOM   12115 C  CB    . VAL C 2 160 ? 127.244 73.351  131.304 1.00 19.52 ?  139 VAL C CB    1 
ATOM   12116 C  CG1   . VAL C 2 160 ? 128.217 73.902  132.362 1.00 20.75 ?  139 VAL C CG1   1 
ATOM   12117 C  CG2   . VAL C 2 160 ? 126.474 74.512  130.686 1.00 20.03 ?  139 VAL C CG2   1 
ATOM   12118 N  N     . GLY C 2 161 ? 128.394 70.263  130.988 1.00 19.13 ?  140 GLY C N     1 
ATOM   12119 C  CA    . GLY C 2 161 ? 129.191 69.186  131.553 1.00 18.05 ?  140 GLY C CA    1 
ATOM   12120 C  C     . GLY C 2 161 ? 130.410 68.930  130.705 1.00 17.86 ?  140 GLY C C     1 
ATOM   12121 O  O     . GLY C 2 161 ? 131.524 68.776  131.219 1.00 17.47 ?  140 GLY C O     1 
ATOM   12122 N  N     . LEU C 2 162 ? 130.200 68.871  129.395 1.00 17.92 ?  141 LEU C N     1 
ATOM   12123 C  CA    . LEU C 2 162 ? 131.304 68.687  128.459 1.00 18.32 ?  141 LEU C CA    1 
ATOM   12124 C  C     . LEU C 2 162 ? 132.306 69.863  128.477 1.00 18.55 ?  141 LEU C C     1 
ATOM   12125 O  O     . LEU C 2 162 ? 133.515 69.639  128.447 1.00 18.49 ?  141 LEU C O     1 
ATOM   12126 C  CB    . LEU C 2 162 ? 130.758 68.437  127.048 1.00 18.50 ?  141 LEU C CB    1 
ATOM   12127 C  CG    . LEU C 2 162 ? 130.081 67.073  126.877 1.00 19.32 ?  141 LEU C CG    1 
ATOM   12128 C  CD1   . LEU C 2 162 ? 129.239 67.049  125.606 1.00 20.38 ?  141 LEU C CD1   1 
ATOM   12129 C  CD2   . LEU C 2 162 ? 131.113 65.942  126.880 1.00 19.94 ?  141 LEU C CD2   1 
ATOM   12130 N  N     . TYR C 2 163 ? 131.815 71.097  128.559 1.00 19.16 ?  142 TYR C N     1 
ATOM   12131 C  CA    . TYR C 2 163 ? 132.707 72.264  128.717 1.00 20.16 ?  142 TYR C CA    1 
ATOM   12132 C  C     . TYR C 2 163 ? 133.585 72.150  129.949 1.00 20.78 ?  142 TYR C C     1 
ATOM   12133 O  O     . TYR C 2 163 ? 134.782 72.449  129.909 1.00 20.36 ?  142 TYR C O     1 
ATOM   12134 C  CB    . TYR C 2 163 ? 131.915 73.579  128.816 1.00 20.34 ?  142 TYR C CB    1 
ATOM   12135 C  CG    . TYR C 2 163 ? 131.141 73.965  127.564 1.00 22.46 ?  142 TYR C CG    1 
ATOM   12136 C  CD1   . TYR C 2 163 ? 131.512 73.494  126.309 1.00 23.88 ?  142 TYR C CD1   1 
ATOM   12137 C  CD2   . TYR C 2 163 ? 130.043 74.814  127.643 1.00 22.41 ?  142 TYR C CD2   1 
ATOM   12138 C  CE1   . TYR C 2 163 ? 130.790 73.854  125.156 1.00 25.93 ?  142 TYR C CE1   1 
ATOM   12139 C  CE2   . TYR C 2 163 ? 129.326 75.179  126.507 1.00 22.07 ?  142 TYR C CE2   1 
ATOM   12140 C  CZ    . TYR C 2 163 ? 129.707 74.707  125.273 1.00 25.19 ?  142 TYR C CZ    1 
ATOM   12141 O  OH    . TYR C 2 163 ? 128.976 75.084  124.165 1.00 27.43 ?  142 TYR C OH    1 
ATOM   12142 N  N     . LYS C 2 164 ? 132.988 71.713  131.052 1.00 21.39 ?  143 LYS C N     1 
ATOM   12143 C  CA    . LYS C 2 164 ? 133.717 71.680  132.309 1.00 22.49 ?  143 LYS C CA    1 
ATOM   12144 C  C     . LYS C 2 164 ? 134.599 70.442  132.448 1.00 22.49 ?  143 LYS C C     1 
ATOM   12145 O  O     . LYS C 2 164 ? 135.443 70.383  133.336 1.00 22.45 ?  143 LYS C O     1 
ATOM   12146 C  CB    . LYS C 2 164 ? 132.777 71.887  133.494 1.00 23.16 ?  143 LYS C CB    1 
ATOM   12147 C  CG    . LYS C 2 164 ? 132.206 73.304  133.511 1.00 26.08 ?  143 LYS C CG    1 
ATOM   12148 C  CD    . LYS C 2 164 ? 131.737 73.715  134.876 1.00 30.38 ?  143 LYS C CD    1 
ATOM   12149 C  CE    . LYS C 2 164 ? 131.360 75.177  134.896 1.00 32.69 ?  143 LYS C CE    1 
ATOM   12150 N  NZ    . LYS C 2 164 ? 130.850 75.559  136.241 1.00 35.60 1  143 LYS C NZ    1 
ATOM   12151 N  N     . ALA C 2 165 ? 134.452 69.495  131.521 1.00 22.02 ?  144 ALA C N     1 
ATOM   12152 C  CA    . ALA C 2 165 ? 135.297 68.316  131.506 1.00 22.69 ?  144 ALA C CA    1 
ATOM   12153 C  C     . ALA C 2 165 ? 136.614 68.526  130.739 1.00 23.20 ?  144 ALA C C     1 
ATOM   12154 O  O     . ALA C 2 165 ? 137.484 67.665  130.766 1.00 23.80 ?  144 ALA C O     1 
ATOM   12155 C  CB    . ALA C 2 165 ? 134.520 67.095  130.956 1.00 21.79 ?  144 ALA C CB    1 
ATOM   12156 N  N     . ILE C 2 166 ? 136.770 69.663  130.056 1.00 23.97 ?  145 ILE C N     1 
ATOM   12157 C  CA    . ILE C 2 166 ? 138.013 69.931  129.323 1.00 24.29 ?  145 ILE C CA    1 
ATOM   12158 C  C     . ILE C 2 166 ? 139.212 69.887  130.274 1.00 25.49 ?  145 ILE C C     1 
ATOM   12159 O  O     . ILE C 2 166 ? 139.180 70.475  131.350 1.00 25.82 ?  145 ILE C O     1 
ATOM   12160 C  CB    . ILE C 2 166 ? 137.993 71.294  128.572 1.00 24.22 ?  145 ILE C CB    1 
ATOM   12161 C  CG1   . ILE C 2 166 ? 136.865 71.341  127.546 1.00 23.45 ?  145 ILE C CG1   1 
ATOM   12162 C  CG2   . ILE C 2 166 ? 139.332 71.543  127.876 1.00 23.42 ?  145 ILE C CG2   1 
ATOM   12163 C  CD1   . ILE C 2 166 ? 136.587 72.763  126.994 1.00 21.99 ?  145 ILE C CD1   1 
ATOM   12164 N  N     . GLN C 2 167 ? 140.239 69.144  129.885 1.00 26.83 ?  146 GLN C N     1 
ATOM   12165 C  CA    . GLN C 2 167 ? 141.461 69.050  130.671 1.00 28.85 ?  146 GLN C CA    1 
ATOM   12166 C  C     . GLN C 2 167 ? 142.564 69.762  129.913 1.00 29.77 ?  146 GLN C C     1 
ATOM   12167 O  O     . GLN C 2 167 ? 142.680 69.616  128.691 1.00 29.74 ?  146 GLN C O     1 
ATOM   12168 C  CB    . GLN C 2 167 ? 141.851 67.587  130.927 1.00 28.99 ?  146 GLN C CB    1 
ATOM   12169 C  CG    . GLN C 2 167 ? 140.951 66.849  131.919 1.00 30.30 ?  146 GLN C CG    1 
ATOM   12170 C  CD    . GLN C 2 167 ? 141.125 67.331  133.354 1.00 33.32 ?  146 GLN C CD    1 
ATOM   12171 O  OE1   . GLN C 2 167 ? 142.050 68.087  133.659 1.00 34.63 ?  146 GLN C OE1   1 
ATOM   12172 N  NE2   . GLN C 2 167 ? 140.248 66.877  134.245 1.00 32.32 ?  146 GLN C NE2   1 
ATOM   12173 N  N     . LYS C 2 168 ? 143.366 70.534  130.636 1.00 31.29 ?  147 LYS C N     1 
ATOM   12174 C  CA    . LYS C 2 168 ? 144.481 71.266  130.036 1.00 33.14 ?  147 LYS C CA    1 
ATOM   12175 C  C     . LYS C 2 168 ? 145.364 70.297  129.262 1.00 33.79 ?  147 LYS C C     1 
ATOM   12176 O  O     . LYS C 2 168 ? 145.582 69.159  129.691 1.00 34.06 ?  147 LYS C O     1 
ATOM   12177 C  CB    . LYS C 2 168 ? 145.278 72.000  131.111 1.00 33.44 ?  147 LYS C CB    1 
ATOM   12178 C  CG    . LYS C 2 168 ? 146.125 73.170  130.616 1.00 35.61 ?  147 LYS C CG    1 
ATOM   12179 C  CD    . LYS C 2 168 ? 146.824 73.835  131.797 1.00 38.40 ?  147 LYS C CD    1 
ATOM   12180 C  CE    . LYS C 2 168 ? 147.454 75.169  131.432 1.00 40.48 ?  147 LYS C CE    1 
ATOM   12181 N  NZ    . LYS C 2 168 ? 148.902 75.006  131.138 1.00 41.56 1  147 LYS C NZ    1 
ATOM   12182 N  N     . ASP C 2 169 ? 145.825 70.741  128.097 1.00 35.10 ?  148 ASP C N     1 
ATOM   12183 C  CA    . ASP C 2 169 ? 146.696 69.940  127.220 1.00 36.27 ?  148 ASP C CA    1 
ATOM   12184 C  C     . ASP C 2 169 ? 146.114 68.598  126.773 1.00 36.29 ?  148 ASP C C     1 
ATOM   12185 O  O     . ASP C 2 169 ? 146.843 67.728  126.294 1.00 36.95 ?  148 ASP C O     1 
ATOM   12186 C  CB    . ASP C 2 169 ? 148.060 69.713  127.882 1.00 37.15 ?  148 ASP C CB    1 
ATOM   12187 C  CG    . ASP C 2 169 ? 148.882 70.971  127.964 1.00 38.94 ?  148 ASP C CG    1 
ATOM   12188 O  OD1   . ASP C 2 169 ? 148.626 71.913  127.177 1.00 41.71 ?  148 ASP C OD1   1 
ATOM   12189 O  OD2   . ASP C 2 169 ? 149.789 71.016  128.819 1.00 41.64 -1 148 ASP C OD2   1 
ATOM   12190 N  N     . ASP C 2 170 ? 144.807 68.423  126.932 1.00 35.87 ?  149 ASP C N     1 
ATOM   12191 C  CA    . ASP C 2 170 ? 144.158 67.196  126.492 1.00 35.24 ?  149 ASP C CA    1 
ATOM   12192 C  C     . ASP C 2 170 ? 143.208 67.556  125.358 1.00 34.12 ?  149 ASP C C     1 
ATOM   12193 O  O     . ASP C 2 170 ? 142.095 68.073  125.579 1.00 33.52 ?  149 ASP C O     1 
ATOM   12194 C  CB    . ASP C 2 170 ? 143.454 66.497  127.660 1.00 36.09 ?  149 ASP C CB    1 
ATOM   12195 C  CG    . ASP C 2 170 ? 142.596 65.309  127.224 1.00 38.39 ?  149 ASP C CG    1 
ATOM   12196 O  OD1   . ASP C 2 170 ? 142.730 64.816  126.079 1.00 42.06 ?  149 ASP C OD1   1 
ATOM   12197 O  OD2   . ASP C 2 170 ? 141.780 64.854  128.048 1.00 42.21 -1 149 ASP C OD2   1 
ATOM   12198 N  N     . GLU C 2 171 ? 143.679 67.292  124.143 1.00 32.48 ?  150 GLU C N     1 
ATOM   12199 C  CA    . GLU C 2 171 ? 142.998 67.708  122.930 1.00 30.93 ?  150 GLU C CA    1 
ATOM   12200 C  C     . GLU C 2 171 ? 141.679 66.961  122.706 1.00 29.37 ?  150 GLU C C     1 
ATOM   12201 O  O     . GLU C 2 171 ? 140.765 67.499  122.081 1.00 28.99 ?  150 GLU C O     1 
ATOM   12202 C  CB    . GLU C 2 171 ? 143.933 67.594  121.710 1.00 31.30 ?  150 GLU C CB    1 
ATOM   12203 C  CG    . GLU C 2 171 ? 144.271 66.163  121.229 1.00 33.64 ?  150 GLU C CG    1 
ATOM   12204 C  CD    . GLU C 2 171 ? 145.438 66.101  120.214 1.00 36.40 ?  150 GLU C CD    1 
ATOM   12205 O  OE1   . GLU C 2 171 ? 145.983 67.160  119.833 1.00 38.62 ?  150 GLU C OE1   1 
ATOM   12206 O  OE2   . GLU C 2 171 ? 145.814 64.983  119.794 1.00 37.42 -1 150 GLU C OE2   1 
ATOM   12207 N  N     . ILE C 2 172 ? 141.586 65.731  123.210 1.00 27.68 ?  151 ILE C N     1 
ATOM   12208 C  CA    . ILE C 2 172 ? 140.366 64.936  123.044 1.00 26.26 ?  151 ILE C CA    1 
ATOM   12209 C  C     . ILE C 2 172 ? 139.208 65.522  123.856 1.00 24.85 ?  151 ILE C C     1 
ATOM   12210 O  O     . ILE C 2 172 ? 138.098 65.632  123.338 1.00 23.53 ?  151 ILE C O     1 
ATOM   12211 C  CB    . ILE C 2 172 ? 140.585 63.433  123.364 1.00 26.53 ?  151 ILE C CB    1 
ATOM   12212 C  CG1   . ILE C 2 172 ? 141.630 62.822  122.416 1.00 27.59 ?  151 ILE C CG1   1 
ATOM   12213 C  CG2   . ILE C 2 172 ? 139.259 62.649  123.336 1.00 26.51 ?  151 ILE C CG2   1 
ATOM   12214 C  CD1   . ILE C 2 172 ? 141.214 62.734  120.942 1.00 26.91 ?  151 ILE C CD1   1 
ATOM   12215 N  N     . SER C 2 173 ? 139.460 65.909  125.109 1.00 23.58 ?  152 SER C N     1 
ATOM   12216 C  CA    . SER C 2 173 ? 138.401 66.529  125.903 1.00 22.36 ?  152 SER C CA    1 
ATOM   12217 C  C     . SER C 2 173 ? 137.979 67.862  125.282 1.00 21.79 ?  152 SER C C     1 
ATOM   12218 O  O     . SER C 2 173 ? 136.801 68.237  125.338 1.00 20.91 ?  152 SER C O     1 
ATOM   12219 C  CB    . SER C 2 173 ? 138.798 66.687  127.376 1.00 22.43 ?  152 SER C CB    1 
ATOM   12220 O  OG    . SER C 2 173 ? 139.939 67.516  127.527 1.00 24.02 ?  152 SER C OG    1 
ATOM   12221 N  N     . LEU C 2 174 ? 138.945 68.568  124.694 1.00 21.65 ?  153 LEU C N     1 
ATOM   12222 C  CA    . LEU C 2 174 ? 138.674 69.833  124.015 1.00 21.86 ?  153 LEU C CA    1 
ATOM   12223 C  C     . LEU C 2 174 ? 137.800 69.616  122.778 1.00 21.98 ?  153 LEU C C     1 
ATOM   12224 O  O     . LEU C 2 174 ? 136.822 70.343  122.588 1.00 21.64 ?  153 LEU C O     1 
ATOM   12225 C  CB    . LEU C 2 174 ? 139.973 70.588  123.668 1.00 21.71 ?  153 LEU C CB    1 
ATOM   12226 C  CG    . LEU C 2 174 ? 139.871 71.941  122.935 1.00 22.04 ?  153 LEU C CG    1 
ATOM   12227 C  CD1   . LEU C 2 174 ? 138.927 72.920  123.631 1.00 21.99 ?  153 LEU C CD1   1 
ATOM   12228 C  CD2   . LEU C 2 174 ? 141.266 72.557  122.782 1.00 23.37 ?  153 LEU C CD2   1 
ATOM   12229 N  N     . PHE C 2 175 ? 138.148 68.620  121.956 1.00 22.17 ?  154 PHE C N     1 
ATOM   12230 C  CA    . PHE C 2 175 ? 137.337 68.239  120.778 1.00 22.02 ?  154 PHE C CA    1 
ATOM   12231 C  C     . PHE C 2 175 ? 135.885 67.963  121.150 1.00 21.86 ?  154 PHE C C     1 
ATOM   12232 O  O     . PHE C 2 175 ? 134.958 68.394  120.454 1.00 21.62 ?  154 PHE C O     1 
ATOM   12233 C  CB    . PHE C 2 175 ? 137.913 66.987  120.098 1.00 22.08 ?  154 PHE C CB    1 
ATOM   12234 C  CG    . PHE C 2 175 ? 137.042 66.436  118.985 1.00 21.99 ?  154 PHE C CG    1 
ATOM   12235 C  CD1   . PHE C 2 175 ? 137.105 66.976  117.697 1.00 20.87 ?  154 PHE C CD1   1 
ATOM   12236 C  CD2   . PHE C 2 175 ? 136.146 65.385  119.233 1.00 20.82 ?  154 PHE C CD2   1 
ATOM   12237 C  CE1   . PHE C 2 175 ? 136.286 66.495  116.674 1.00 20.27 ?  154 PHE C CE1   1 
ATOM   12238 C  CE2   . PHE C 2 175 ? 135.327 64.883  118.218 1.00 20.19 ?  154 PHE C CE2   1 
ATOM   12239 C  CZ    . PHE C 2 175 ? 135.400 65.436  116.927 1.00 20.93 ?  154 PHE C CZ    1 
ATOM   12240 N  N     . LYS C 2 176 ? 135.698 67.202  122.230 1.00 21.98 ?  155 LYS C N     1 
ATOM   12241 C  CA    . LYS C 2 176 ? 134.355 66.836  122.687 1.00 21.79 ?  155 LYS C CA    1 
ATOM   12242 C  C     . LYS C 2 176 ? 133.532 68.075  123.054 1.00 21.70 ?  155 LYS C C     1 
ATOM   12243 O  O     . LYS C 2 176 ? 132.352 68.178  122.688 1.00 21.10 ?  155 LYS C O     1 
ATOM   12244 C  CB    . LYS C 2 176 ? 134.437 65.845  123.856 1.00 22.00 ?  155 LYS C CB    1 
ATOM   12245 C  CG    . LYS C 2 176 ? 135.007 64.485  123.476 1.00 21.93 ?  155 LYS C CG    1 
ATOM   12246 C  CD    . LYS C 2 176 ? 135.130 63.569  124.681 1.00 23.06 ?  155 LYS C CD    1 
ATOM   12247 C  CE    . LYS C 2 176 ? 135.637 62.197  124.285 1.00 24.91 ?  155 LYS C CE    1 
ATOM   12248 N  NZ    . LYS C 2 176 ? 136.070 61.406  125.485 1.00 25.16 1  155 LYS C NZ    1 
ATOM   12249 N  N     . ALA C 2 177 ? 134.159 69.015  123.770 1.00 21.49 ?  156 ALA C N     1 
ATOM   12250 C  CA    . ALA C 2 177 ? 133.510 70.284  124.085 1.00 20.60 ?  156 ALA C CA    1 
ATOM   12251 C  C     . ALA C 2 177 ? 133.219 71.145  122.836 1.00 20.37 ?  156 ALA C C     1 
ATOM   12252 O  O     . ALA C 2 177 ? 132.191 71.807  122.776 1.00 19.61 ?  156 ALA C O     1 
ATOM   12253 C  CB    . ALA C 2 177 ? 134.320 71.075  125.107 1.00 20.88 ?  156 ALA C CB    1 
ATOM   12254 N  N     . MET C 2 178 ? 134.112 71.120  121.847 1.00 20.70 ?  157 MET C N     1 
ATOM   12255 C  CA    . MET C 2 178 ? 133.888 71.853  120.589 1.00 21.06 ?  157 MET C CA    1 
ATOM   12256 C  C     . MET C 2 178 ? 132.746 71.260  119.787 1.00 20.83 ?  157 MET C C     1 
ATOM   12257 O  O     . MET C 2 178 ? 132.035 71.991  119.089 1.00 21.28 ?  157 MET C O     1 
ATOM   12258 C  CB    . MET C 2 178 ? 135.152 71.885  119.710 1.00 20.68 ?  157 MET C CB    1 
ATOM   12259 C  CG    . MET C 2 178 ? 136.313 72.722  120.242 1.00 21.61 ?  157 MET C CG    1 
ATOM   12260 S  SD    . MET C 2 178 ? 137.796 72.461  119.241 1.00 24.32 ?  157 MET C SD    1 
ATOM   12261 C  CE    . MET C 2 178 ? 138.843 73.805  119.837 1.00 23.64 ?  157 MET C CE    1 
ATOM   12262 N  N     . VAL C 2 179 ? 132.586 69.938  119.845 1.00 20.76 ?  158 VAL C N     1 
ATOM   12263 C  CA    . VAL C 2 179 ? 131.444 69.282  119.197 1.00 20.14 ?  158 VAL C CA    1 
ATOM   12264 C  C     . VAL C 2 179 ? 130.154 69.754  119.877 1.00 20.35 ?  158 VAL C C     1 
ATOM   12265 O  O     . VAL C 2 179 ? 129.175 70.103  119.213 1.00 19.82 ?  158 VAL C O     1 
ATOM   12266 C  CB    . VAL C 2 179 ? 131.534 67.735  119.276 1.00 20.07 ?  158 VAL C CB    1 
ATOM   12267 C  CG1   . VAL C 2 179 ? 130.218 67.095  118.825 1.00 20.07 ?  158 VAL C CG1   1 
ATOM   12268 C  CG2   . VAL C 2 179 ? 132.690 67.222  118.423 1.00 20.57 ?  158 VAL C CG2   1 
ATOM   12269 N  N     . ALA C 2 180 ? 130.175 69.760  121.207 1.00 19.89 ?  159 ALA C N     1 
ATOM   12270 C  CA    . ALA C 2 180 ? 129.046 70.235  122.006 1.00 20.50 ?  159 ALA C CA    1 
ATOM   12271 C  C     . ALA C 2 180 ? 128.695 71.687  121.639 1.00 20.67 ?  159 ALA C C     1 
ATOM   12272 O  O     . ALA C 2 180 ? 127.524 72.015  121.443 1.00 21.27 ?  159 ALA C O     1 
ATOM   12273 C  CB    . ALA C 2 180 ? 129.379 70.129  123.478 1.00 20.03 ?  159 ALA C CB    1 
ATOM   12274 N  N     . SER C 2 181 ? 129.715 72.539  121.538 1.00 20.78 ?  160 SER C N     1 
ATOM   12275 C  CA    . SER C 2 181 ? 129.537 73.941  121.142 1.00 21.26 ?  160 SER C CA    1 
ATOM   12276 C  C     . SER C 2 181 ? 128.961 74.082  119.726 1.00 21.19 ?  160 SER C C     1 
ATOM   12277 O  O     . SER C 2 181 ? 128.030 74.851  119.515 1.00 20.89 ?  160 SER C O     1 
ATOM   12278 C  CB    . SER C 2 181 ? 130.855 74.720  121.276 1.00 21.42 ?  160 SER C CB    1 
ATOM   12279 O  OG    . SER C 2 181 ? 130.669 76.097  120.981 1.00 23.69 ?  160 SER C OG    1 
ATOM   12280 N  N     . VAL C 2 182 ? 129.509 73.346  118.753 1.00 20.99 ?  161 VAL C N     1 
ATOM   12281 C  CA    . VAL C 2 182 ? 128.907 73.355  117.415 1.00 21.18 ?  161 VAL C CA    1 
ATOM   12282 C  C     . VAL C 2 182 ? 127.435 72.913  117.468 1.00 21.15 ?  161 VAL C C     1 
ATOM   12283 O  O     . VAL C 2 182 ? 126.571 73.536  116.830 1.00 21.18 ?  161 VAL C O     1 
ATOM   12284 C  CB    . VAL C 2 182 ? 129.715 72.503  116.383 1.00 21.11 ?  161 VAL C CB    1 
ATOM   12285 C  CG1   . VAL C 2 182 ? 128.946 72.375  115.070 1.00 21.75 ?  161 VAL C CG1   1 
ATOM   12286 C  CG2   . VAL C 2 182 ? 131.087 73.126  116.135 1.00 20.98 ?  161 VAL C CG2   1 
ATOM   12287 N  N     . TYR C 2 183 ? 127.133 71.855  118.234 1.00 21.10 ?  162 TYR C N     1 
ATOM   12288 C  CA    . TYR C 2 183 ? 125.739 71.405  118.368 1.00 21.21 ?  162 TYR C CA    1 
ATOM   12289 C  C     . TYR C 2 183 ? 124.832 72.457  119.006 1.00 21.38 ?  162 TYR C C     1 
ATOM   12290 O  O     . TYR C 2 183 ? 123.660 72.554  118.660 1.00 20.97 ?  162 TYR C O     1 
ATOM   12291 C  CB    . TYR C 2 183 ? 125.614 70.072  119.133 1.00 21.50 ?  162 TYR C CB    1 
ATOM   12292 C  CG    . TYR C 2 183 ? 126.105 68.874  118.365 1.00 22.20 ?  162 TYR C CG    1 
ATOM   12293 C  CD1   . TYR C 2 183 ? 126.214 68.908  116.976 1.00 23.80 ?  162 TYR C CD1   1 
ATOM   12294 C  CD2   . TYR C 2 183 ? 126.445 67.688  119.027 1.00 23.71 ?  162 TYR C CD2   1 
ATOM   12295 C  CE1   . TYR C 2 183 ? 126.671 67.795  116.260 1.00 25.52 ?  162 TYR C CE1   1 
ATOM   12296 C  CE2   . TYR C 2 183 ? 126.894 66.580  118.327 1.00 24.01 ?  162 TYR C CE2   1 
ATOM   12297 C  CZ    . TYR C 2 183 ? 127.014 66.640  116.949 1.00 25.47 ?  162 TYR C CZ    1 
ATOM   12298 O  OH    . TYR C 2 183 ? 127.476 65.545  116.248 1.00 25.37 ?  162 TYR C OH    1 
ATOM   12299 N  N     . LEU C 2 184 ? 125.373 73.222  119.942 1.00 22.12 ?  163 LEU C N     1 
ATOM   12300 C  CA    . LEU C 2 184 ? 124.630 74.355  120.526 1.00 23.80 ?  163 LEU C CA    1 
ATOM   12301 C  C     . LEU C 2 184 ? 124.426 75.459  119.479 1.00 24.21 ?  163 LEU C C     1 
ATOM   12302 O  O     . LEU C 2 184 ? 123.325 75.946  119.328 1.00 24.72 ?  163 LEU C O     1 
ATOM   12303 C  CB    . LEU C 2 184 ? 125.346 74.903  121.765 1.00 23.52 ?  163 LEU C CB    1 
ATOM   12304 C  CG    . LEU C 2 184 ? 124.704 76.028  122.602 1.00 24.91 ?  163 LEU C CG    1 
ATOM   12305 C  CD1   . LEU C 2 184 ? 125.066 75.852  124.054 1.00 24.81 ?  163 LEU C CD1   1 
ATOM   12306 C  CD2   . LEU C 2 184 ? 125.089 77.435  122.124 1.00 26.39 ?  163 LEU C CD2   1 
ATOM   12307 N  N     . GLU C 2 185 ? 125.488 75.826  118.749 1.00 25.17 ?  164 GLU C N     1 
ATOM   12308 C  CA    . GLU C 2 185 ? 125.436 76.941  117.791 1.00 25.30 ?  164 GLU C CA    1 
ATOM   12309 C  C     . GLU C 2 185 ? 124.529 76.666  116.580 1.00 25.07 ?  164 GLU C C     1 
ATOM   12310 O  O     . GLU C 2 185 ? 123.756 77.536  116.143 1.00 24.49 ?  164 GLU C O     1 
ATOM   12311 C  CB    . GLU C 2 185 ? 126.849 77.285  117.266 1.00 26.17 ?  164 GLU C CB    1 
ATOM   12312 C  CG    . GLU C 2 185 ? 127.824 77.846  118.325 1.00 27.05 ?  164 GLU C CG    1 
ATOM   12313 C  CD    . GLU C 2 185 ? 127.569 79.320  118.664 1.00 29.23 ?  164 GLU C CD    1 
ATOM   12314 O  OE1   . GLU C 2 185 ? 126.626 79.945  118.100 1.00 28.79 ?  164 GLU C OE1   1 
ATOM   12315 O  OE2   . GLU C 2 185 ? 128.337 79.883  119.478 1.00 28.65 -1 164 GLU C OE2   1 
ATOM   12316 N  N     . SER C 2 186 ? 124.657 75.461  116.040 1.00 24.23 ?  165 SER C N     1 
ATOM   12317 C  CA    . SER C 2 186 ? 124.173 75.138  114.704 1.00 24.71 ?  165 SER C CA    1 
ATOM   12318 C  C     . SER C 2 186 ? 122.981 74.186  114.696 1.00 24.51 ?  165 SER C C     1 
ATOM   12319 O  O     . SER C 2 186 ? 122.387 73.958  113.645 1.00 24.87 ?  165 SER C O     1 
ATOM   12320 C  CB    . SER C 2 186 ? 125.312 74.524  113.878 1.00 25.06 ?  165 SER C CB    1 
ATOM   12321 O  OG    . SER C 2 186 ? 126.419 75.402  113.788 1.00 26.29 ?  165 SER C OG    1 
ATOM   12322 N  N     . PHE C 2 187 ? 122.650 73.626  115.857 1.00 24.71 ?  166 PHE C N     1 
ATOM   12323 C  CA    . PHE C 2 187 ? 121.532 72.693  115.987 1.00 25.69 ?  166 PHE C CA    1 
ATOM   12324 C  C     . PHE C 2 187 ? 120.533 73.125  117.071 1.00 25.87 ?  166 PHE C C     1 
ATOM   12325 O  O     . PHE C 2 187 ? 119.368 73.374  116.754 1.00 26.03 ?  166 PHE C O     1 
ATOM   12326 C  CB    . PHE C 2 187 ? 122.033 71.257  116.239 1.00 25.54 ?  166 PHE C CB    1 
ATOM   12327 C  CG    . PHE C 2 187 ? 120.947 70.284  116.650 1.00 26.64 ?  166 PHE C CG    1 
ATOM   12328 C  CD1   . PHE C 2 187 ? 119.872 70.003  115.796 1.00 25.90 ?  166 PHE C CD1   1 
ATOM   12329 C  CD2   . PHE C 2 187 ? 121.006 69.637  117.887 1.00 27.45 ?  166 PHE C CD2   1 
ATOM   12330 C  CE1   . PHE C 2 187 ? 118.860 69.101  116.177 1.00 25.64 ?  166 PHE C CE1   1 
ATOM   12331 C  CE2   . PHE C 2 187 ? 119.998 68.725  118.282 1.00 26.52 ?  166 PHE C CE2   1 
ATOM   12332 C  CZ    . PHE C 2 187 ? 118.929 68.460  117.422 1.00 27.18 ?  166 PHE C CZ    1 
ATOM   12333 N  N     . LEU C 2 188 ? 120.994 73.223  118.320 1.00 26.13 ?  167 LEU C N     1 
ATOM   12334 C  CA    . LEU C 2 188 ? 120.113 73.459  119.493 1.00 27.13 ?  167 LEU C CA    1 
ATOM   12335 C  C     . LEU C 2 188 ? 119.348 74.795  119.510 1.00 27.22 ?  167 LEU C C     1 
ATOM   12336 O  O     . LEU C 2 188 ? 118.242 74.872  120.062 1.00 28.03 ?  167 LEU C O     1 
ATOM   12337 C  CB    . LEU C 2 188 ? 120.897 73.330  120.809 1.00 26.89 ?  167 LEU C CB    1 
ATOM   12338 C  CG    . LEU C 2 188 ? 121.505 72.000  121.279 1.00 28.64 ?  167 LEU C CG    1 
ATOM   12339 C  CD1   . LEU C 2 188 ? 122.258 72.199  122.593 1.00 28.34 ?  167 LEU C CD1   1 
ATOM   12340 C  CD2   . LEU C 2 188 ? 120.462 70.907  121.438 1.00 27.90 ?  167 LEU C CD2   1 
ATOM   12341 N  N     . PHE C 2 189 ? 119.946 75.843  118.956 1.00 26.79 ?  168 PHE C N     1 
ATOM   12342 C  CA    . PHE C 2 189 ? 119.282 77.145  118.900 1.00 26.90 ?  168 PHE C CA    1 
ATOM   12343 C  C     . PHE C 2 189 ? 118.041 77.100  118.002 1.00 26.52 ?  168 PHE C C     1 
ATOM   12344 O  O     . PHE C 2 189 ? 117.148 77.950  118.120 1.00 26.02 ?  168 PHE C O     1 
ATOM   12345 C  CB    . PHE C 2 189 ? 120.229 78.235  118.360 1.00 27.03 ?  168 PHE C CB    1 
ATOM   12346 C  CG    . PHE C 2 189 ? 121.111 78.900  119.415 1.00 28.09 ?  168 PHE C CG    1 
ATOM   12347 C  CD1   . PHE C 2 189 ? 120.562 79.509  120.545 1.00 28.69 ?  168 PHE C CD1   1 
ATOM   12348 C  CD2   . PHE C 2 189 ? 122.487 78.978  119.231 1.00 29.15 ?  168 PHE C CD2   1 
ATOM   12349 C  CE1   . PHE C 2 189 ? 121.372 80.138  121.502 1.00 28.50 ?  168 PHE C CE1   1 
ATOM   12350 C  CE2   . PHE C 2 189 ? 123.314 79.607  120.180 1.00 30.19 ?  168 PHE C CE2   1 
ATOM   12351 C  CZ    . PHE C 2 189 ? 122.745 80.189  121.327 1.00 29.81 ?  168 PHE C CZ    1 
ATOM   12352 N  N     . TYR C 2 190 ? 117.990 76.127  117.092 1.00 26.18 ?  169 TYR C N     1 
ATOM   12353 C  CA    . TYR C 2 190 ? 117.043 76.224  115.986 1.00 26.24 ?  169 TYR C CA    1 
ATOM   12354 C  C     . TYR C 2 190 ? 115.579 75.884  116.305 1.00 25.94 ?  169 TYR C C     1 
ATOM   12355 O  O     . TYR C 2 190 ? 114.666 76.366  115.632 1.00 25.71 ?  169 TYR C O     1 
ATOM   12356 C  CB    . TYR C 2 190 ? 117.604 75.544  114.736 1.00 27.13 ?  169 TYR C CB    1 
ATOM   12357 C  CG    . TYR C 2 190 ? 118.657 76.433  114.108 1.00 28.07 ?  169 TYR C CG    1 
ATOM   12358 C  CD1   . TYR C 2 190 ? 119.982 76.410  114.558 1.00 29.54 ?  169 TYR C CD1   1 
ATOM   12359 C  CD2   . TYR C 2 190 ? 118.315 77.350  113.113 1.00 29.31 ?  169 TYR C CD2   1 
ATOM   12360 C  CE1   . TYR C 2 190 ? 120.948 77.253  114.001 1.00 30.44 ?  169 TYR C CE1   1 
ATOM   12361 C  CE2   . TYR C 2 190 ? 119.278 78.199  112.546 1.00 30.64 ?  169 TYR C CE2   1 
ATOM   12362 C  CZ    . TYR C 2 190 ? 120.589 78.147  113.001 1.00 30.40 ?  169 TYR C CZ    1 
ATOM   12363 O  OH    . TYR C 2 190 ? 121.536 78.985  112.455 1.00 28.85 ?  169 TYR C OH    1 
ATOM   12364 N  N     . SER C 2 191 ? 115.361 75.109  117.364 1.00 25.17 ?  170 SER C N     1 
ATOM   12365 C  CA    . SER C 2 191 ? 114.008 74.856  117.854 1.00 25.10 ?  170 SER C CA    1 
ATOM   12366 C  C     . SER C 2 191 ? 113.414 76.176  118.361 1.00 25.16 ?  170 SER C C     1 
ATOM   12367 O  O     . SER C 2 191 ? 112.197 76.378  118.302 1.00 25.30 ?  170 SER C O     1 
ATOM   12368 C  CB    . SER C 2 191 ? 114.013 73.792  118.951 1.00 24.56 ?  170 SER C CB    1 
ATOM   12369 O  OG    . SER C 2 191 ? 114.716 74.236  120.095 1.00 24.98 ?  170 SER C OG    1 
ATOM   12370 N  N     . GLY C 2 192 ? 114.299 77.055  118.844 1.00 24.32 ?  171 GLY C N     1 
ATOM   12371 C  CA    . GLY C 2 192 ? 113.958 78.403  119.280 1.00 23.97 ?  171 GLY C CA    1 
ATOM   12372 C  C     . GLY C 2 192 ? 113.831 79.399  118.140 1.00 23.85 ?  171 GLY C C     1 
ATOM   12373 O  O     . GLY C 2 192 ? 112.821 80.098  118.057 1.00 23.99 ?  171 GLY C O     1 
ATOM   12374 N  N     . PHE C 2 193 ? 114.832 79.452  117.259 1.00 23.28 ?  172 PHE C N     1 
ATOM   12375 C  CA    . PHE C 2 193 ? 114.826 80.378  116.110 1.00 23.85 ?  172 PHE C CA    1 
ATOM   12376 C  C     . PHE C 2 193 ? 113.621 80.220  115.182 1.00 23.72 ?  172 PHE C C     1 
ATOM   12377 O  O     . PHE C 2 193 ? 113.223 81.182  114.528 1.00 23.92 ?  172 PHE C O     1 
ATOM   12378 C  CB    . PHE C 2 193 ? 116.089 80.235  115.250 1.00 23.47 ?  172 PHE C CB    1 
ATOM   12379 C  CG    . PHE C 2 193 ? 117.339 80.815  115.873 1.00 24.32 ?  172 PHE C CG    1 
ATOM   12380 C  CD1   . PHE C 2 193 ? 117.269 81.820  116.839 1.00 22.28 ?  172 PHE C CD1   1 
ATOM   12381 C  CD2   . PHE C 2 193 ? 118.595 80.364  115.463 1.00 23.82 ?  172 PHE C CD2   1 
ATOM   12382 C  CE1   . PHE C 2 193 ? 118.429 82.356  117.412 1.00 23.41 ?  172 PHE C CE1   1 
ATOM   12383 C  CE2   . PHE C 2 193 ? 119.772 80.891  116.026 1.00 24.70 ?  172 PHE C CE2   1 
ATOM   12384 C  CZ    . PHE C 2 193 ? 119.686 81.896  117.003 1.00 24.87 ?  172 PHE C CZ    1 
ATOM   12385 N  N     . TYR C 2 194 ? 113.069 79.008  115.101 1.00 23.31 ?  173 TYR C N     1 
ATOM   12386 C  CA    . TYR C 2 194 ? 111.970 78.720  114.176 1.00 23.26 ?  173 TYR C CA    1 
ATOM   12387 C  C     . TYR C 2 194 ? 110.846 79.754  114.285 1.00 23.04 ?  173 TYR C C     1 
ATOM   12388 O  O     . TYR C 2 194 ? 110.361 80.266  113.272 1.00 23.47 ?  173 TYR C O     1 
ATOM   12389 C  CB    . TYR C 2 194 ? 111.389 77.312  114.396 1.00 23.13 ?  173 TYR C CB    1 
ATOM   12390 C  CG    . TYR C 2 194 ? 110.316 76.938  113.382 1.00 24.10 ?  173 TYR C CG    1 
ATOM   12391 C  CD1   . TYR C 2 194 ? 110.645 76.226  112.227 1.00 25.72 ?  173 TYR C CD1   1 
ATOM   12392 C  CD2   . TYR C 2 194 ? 108.985 77.316  113.564 1.00 27.04 ?  173 TYR C CD2   1 
ATOM   12393 C  CE1   . TYR C 2 194 ? 109.666 75.881  111.285 1.00 28.94 ?  173 TYR C CE1   1 
ATOM   12394 C  CE2   . TYR C 2 194 ? 107.996 76.984  112.620 1.00 27.84 ?  173 TYR C CE2   1 
ATOM   12395 C  CZ    . TYR C 2 194 ? 108.351 76.268  111.487 1.00 29.97 ?  173 TYR C CZ    1 
ATOM   12396 O  OH    . TYR C 2 194 ? 107.397 75.939  110.541 1.00 34.34 ?  173 TYR C OH    1 
ATOM   12397 N  N     . TYR C 2 195 ? 110.438 80.048  115.510 1.00 22.51 ?  174 TYR C N     1 
ATOM   12398 C  CA    . TYR C 2 195 ? 109.207 80.796  115.735 1.00 22.60 ?  174 TYR C CA    1 
ATOM   12399 C  C     . TYR C 2 195 ? 109.323 82.292  115.386 1.00 22.64 ?  174 TYR C C     1 
ATOM   12400 O  O     . TYR C 2 195 ? 108.450 82.810  114.682 1.00 22.39 ?  174 TYR C O     1 
ATOM   12401 C  CB    . TYR C 2 195 ? 108.686 80.553  117.152 1.00 22.32 ?  174 TYR C CB    1 
ATOM   12402 C  CG    . TYR C 2 195 ? 107.179 80.624  117.297 1.00 23.39 ?  174 TYR C CG    1 
ATOM   12403 C  CD1   . TYR C 2 195 ? 106.323 80.231  116.255 1.00 22.84 ?  174 TYR C CD1   1 
ATOM   12404 C  CD2   . TYR C 2 195 ? 106.608 81.048  118.495 1.00 22.23 ?  174 TYR C CD2   1 
ATOM   12405 C  CE1   . TYR C 2 195 ? 104.932 80.290  116.405 1.00 24.05 ?  174 TYR C CE1   1 
ATOM   12406 C  CE2   . TYR C 2 195 ? 105.222 81.097  118.660 1.00 24.11 ?  174 TYR C CE2   1 
ATOM   12407 C  CZ    . TYR C 2 195 ? 104.396 80.716  117.616 1.00 23.92 ?  174 TYR C CZ    1 
ATOM   12408 O  OH    . TYR C 2 195 ? 103.040 80.793  117.786 1.00 25.00 ?  174 TYR C OH    1 
ATOM   12409 N  N     . PRO C 2 196 ? 110.405 82.983  115.854 1.00 22.25 ?  175 PRO C N     1 
ATOM   12410 C  CA    . PRO C 2 196 ? 110.616 84.359  115.375 1.00 22.45 ?  175 PRO C CA    1 
ATOM   12411 C  C     . PRO C 2 196 ? 110.736 84.447  113.854 1.00 22.59 ?  175 PRO C C     1 
ATOM   12412 O  O     . PRO C 2 196 ? 110.225 85.405  113.261 1.00 22.19 ?  175 PRO C O     1 
ATOM   12413 C  CB    . PRO C 2 196 ? 111.935 84.786  116.036 1.00 22.25 ?  175 PRO C CB    1 
ATOM   12414 C  CG    . PRO C 2 196 ? 112.110 83.882  117.211 1.00 22.22 ?  175 PRO C CG    1 
ATOM   12415 C  CD    . PRO C 2 196 ? 111.417 82.588  116.861 1.00 22.32 ?  175 PRO C CD    1 
ATOM   12416 N  N     . LEU C 2 197 ? 111.390 83.461  113.232 1.00 21.92 ?  176 LEU C N     1 
ATOM   12417 C  CA    . LEU C 2 197 ? 111.521 83.431  111.773 1.00 22.35 ?  176 LEU C CA    1 
ATOM   12418 C  C     . LEU C 2 197 ? 110.166 83.197  111.096 1.00 22.60 ?  176 LEU C C     1 
ATOM   12419 O  O     . LEU C 2 197 ? 109.866 83.787  110.055 1.00 22.41 ?  176 LEU C O     1 
ATOM   12420 C  CB    . LEU C 2 197 ? 112.505 82.353  111.322 1.00 22.69 ?  176 LEU C CB    1 
ATOM   12421 C  CG    . LEU C 2 197 ? 113.989 82.448  111.701 1.00 23.68 ?  176 LEU C CG    1 
ATOM   12422 C  CD1   . LEU C 2 197 ? 114.738 81.225  111.148 1.00 23.70 ?  176 LEU C CD1   1 
ATOM   12423 C  CD2   . LEU C 2 197 ? 114.609 83.740  111.179 1.00 23.09 ?  176 LEU C CD2   1 
ATOM   12424 N  N     . TYR C 2 198 ? 109.358 82.330  111.702 1.00 22.64 ?  177 TYR C N     1 
ATOM   12425 C  CA    . TYR C 2 198 ? 108.035 81.995  111.193 1.00 22.92 ?  177 TYR C CA    1 
ATOM   12426 C  C     . TYR C 2 198 ? 107.153 83.258  111.171 1.00 23.68 ?  177 TYR C C     1 
ATOM   12427 O  O     . TYR C 2 198 ? 106.450 83.519  110.192 1.00 23.81 ?  177 TYR C O     1 
ATOM   12428 C  CB    . TYR C 2 198 ? 107.446 80.894  112.069 1.00 22.73 ?  177 TYR C CB    1 
ATOM   12429 C  CG    . TYR C 2 198 ? 106.053 80.426  111.746 1.00 22.91 ?  177 TYR C CG    1 
ATOM   12430 C  CD1   . TYR C 2 198 ? 105.813 79.606  110.643 1.00 23.49 ?  177 TYR C CD1   1 
ATOM   12431 C  CD2   . TYR C 2 198 ? 104.984 80.749  112.582 1.00 21.97 ?  177 TYR C CD2   1 
ATOM   12432 C  CE1   . TYR C 2 198 ? 104.529 79.143  110.355 1.00 23.57 ?  177 TYR C CE1   1 
ATOM   12433 C  CE2   . TYR C 2 198 ? 103.686 80.285  112.306 1.00 22.54 ?  177 TYR C CE2   1 
ATOM   12434 C  CZ    . TYR C 2 198 ? 103.471 79.489  111.191 1.00 22.88 ?  177 TYR C CZ    1 
ATOM   12435 O  OH    . TYR C 2 198 ? 102.205 79.013  110.904 1.00 23.17 ?  177 TYR C OH    1 
ATOM   12436 N  N     . PHE C 2 199 ? 107.228 84.060  112.227 1.00 23.50 ?  178 PHE C N     1 
ATOM   12437 C  CA    . PHE C 2 199 ? 106.503 85.330  112.255 1.00 24.60 ?  178 PHE C CA    1 
ATOM   12438 C  C     . PHE C 2 199 ? 107.064 86.398  111.306 1.00 24.72 ?  178 PHE C C     1 
ATOM   12439 O  O     . PHE C 2 199 ? 106.312 87.046  110.580 1.00 24.19 ?  178 PHE C O     1 
ATOM   12440 C  CB    . PHE C 2 199 ? 106.405 85.866  113.686 1.00 24.35 ?  178 PHE C CB    1 
ATOM   12441 C  CG    . PHE C 2 199 ? 105.394 85.145  114.525 1.00 26.36 ?  178 PHE C CG    1 
ATOM   12442 C  CD1   . PHE C 2 199 ? 104.124 84.860  114.022 1.00 28.53 ?  178 PHE C CD1   1 
ATOM   12443 C  CD2   . PHE C 2 199 ? 105.694 84.763  115.825 1.00 28.23 ?  178 PHE C CD2   1 
ATOM   12444 C  CE1   . PHE C 2 199 ? 103.179 84.183  114.801 1.00 29.37 ?  178 PHE C CE1   1 
ATOM   12445 C  CE2   . PHE C 2 199 ? 104.744 84.093  116.615 1.00 28.69 ?  178 PHE C CE2   1 
ATOM   12446 C  CZ    . PHE C 2 199 ? 103.497 83.805  116.102 1.00 28.43 ?  178 PHE C CZ    1 
ATOM   12447 N  N     . TYR C 2 200 ? 108.384 86.566  111.318 1.00 25.36 ?  179 TYR C N     1 
ATOM   12448 C  CA    . TYR C 2 200 ? 109.074 87.508  110.427 1.00 26.02 ?  179 TYR C CA    1 
ATOM   12449 C  C     . TYR C 2 200 ? 108.641 87.276  108.979 1.00 26.57 ?  179 TYR C C     1 
ATOM   12450 O  O     . TYR C 2 200 ? 108.335 88.222  108.246 1.00 26.30 ?  179 TYR C O     1 
ATOM   12451 C  CB    . TYR C 2 200 ? 110.593 87.330  110.548 1.00 26.19 ?  179 TYR C CB    1 
ATOM   12452 C  CG    . TYR C 2 200 ? 111.412 88.388  109.842 1.00 27.82 ?  179 TYR C CG    1 
ATOM   12453 C  CD1   . TYR C 2 200 ? 111.996 88.130  108.598 1.00 30.77 ?  179 TYR C CD1   1 
ATOM   12454 C  CD2   . TYR C 2 200 ? 111.614 89.644  110.420 1.00 29.20 ?  179 TYR C CD2   1 
ATOM   12455 C  CE1   . TYR C 2 200 ? 112.751 89.096  107.945 1.00 31.82 ?  179 TYR C CE1   1 
ATOM   12456 C  CE2   . TYR C 2 200 ? 112.365 90.618  109.779 1.00 30.44 ?  179 TYR C CE2   1 
ATOM   12457 C  CZ    . TYR C 2 200 ? 112.932 90.336  108.539 1.00 32.74 ?  179 TYR C CZ    1 
ATOM   12458 O  OH    . TYR C 2 200 ? 113.672 91.290  107.885 1.00 34.58 ?  179 TYR C OH    1 
ATOM   12459 N  N     . GLY C 2 201 ? 108.595 86.003  108.590 1.00 26.71 ?  180 GLY C N     1 
ATOM   12460 C  CA    . GLY C 2 201 ? 108.212 85.611  107.241 1.00 27.38 ?  180 GLY C CA    1 
ATOM   12461 C  C     . GLY C 2 201 ? 106.775 85.932  106.865 1.00 27.62 ?  180 GLY C C     1 
ATOM   12462 O  O     . GLY C 2 201 ? 106.452 85.957  105.689 1.00 28.25 ?  180 GLY C O     1 
ATOM   12463 N  N     . GLN C 2 202 ? 105.923 86.178  107.860 1.00 27.60 ?  181 GLN C N     1 
ATOM   12464 C  CA    . GLN C 2 202 ? 104.520 86.568  107.635 1.00 28.24 ?  181 GLN C CA    1 
ATOM   12465 C  C     . GLN C 2 202 ? 104.316 88.063  107.821 1.00 28.30 ?  181 GLN C C     1 
ATOM   12466 O  O     . GLN C 2 202 ? 103.177 88.536  107.796 1.00 27.98 ?  181 GLN C O     1 
ATOM   12467 C  CB    . GLN C 2 202 ? 103.588 85.873  108.631 1.00 27.90 ?  181 GLN C CB    1 
ATOM   12468 C  CG    . GLN C 2 202 ? 103.558 84.379  108.571 1.00 29.54 ?  181 GLN C CG    1 
ATOM   12469 C  CD    . GLN C 2 202 ? 102.706 83.796  109.676 1.00 31.54 ?  181 GLN C CD    1 
ATOM   12470 O  OE1   . GLN C 2 202 ? 101.479 83.929  109.667 1.00 32.11 ?  181 GLN C OE1   1 
ATOM   12471 N  NE2   . GLN C 2 202 ? 103.350 83.155  110.642 1.00 31.29 ?  181 GLN C NE2   1 
ATOM   12472 N  N     . GLY C 2 203 ? 105.409 88.789  108.055 1.00 28.14 ?  182 GLY C N     1 
ATOM   12473 C  CA    . GLY C 2 203 ? 105.358 90.222  108.297 1.00 28.38 ?  182 GLY C CA    1 
ATOM   12474 C  C     . GLY C 2 203 ? 104.881 90.572  109.691 1.00 28.71 ?  182 GLY C C     1 
ATOM   12475 O  O     . GLY C 2 203 ? 104.266 91.615  109.890 1.00 28.80 ?  182 GLY C O     1 
ATOM   12476 N  N     . LYS C 2 204 ? 105.154 89.689  110.651 1.00 28.24 ?  183 LYS C N     1 
ATOM   12477 C  CA    . LYS C 2 204 ? 104.739 89.891  112.030 1.00 28.48 ?  183 LYS C CA    1 
ATOM   12478 C  C     . LYS C 2 204 ? 105.953 89.894  112.954 1.00 27.82 ?  183 LYS C C     1 
ATOM   12479 O  O     . LYS C 2 204 ? 106.913 89.141  112.737 1.00 26.73 ?  183 LYS C O     1 
ATOM   12480 C  CB    . LYS C 2 204 ? 103.749 88.810  112.466 1.00 29.13 ?  183 LYS C CB    1 
ATOM   12481 C  CG    . LYS C 2 204 ? 102.413 88.847  111.723 1.00 30.41 ?  183 LYS C CG    1 
ATOM   12482 C  CD    . LYS C 2 204 ? 101.727 87.491  111.771 1.00 33.74 ?  183 LYS C CD    1 
ATOM   12483 C  CE    . LYS C 2 204 ? 100.348 87.546  111.093 1.00 36.26 ?  183 LYS C CE    1 
ATOM   12484 N  NZ    . LYS C 2 204 ? 99.671  86.219  111.175 1.00 39.17 1  183 LYS C NZ    1 
ATOM   12485 N  N     . LEU C 2 205 ? 105.897 90.742  113.979 1.00 27.77 ?  184 LEU C N     1 
ATOM   12486 C  CA    . LEU C 2 205 ? 106.988 90.895  114.949 1.00 27.79 ?  184 LEU C CA    1 
ATOM   12487 C  C     . LEU C 2 205 ? 108.333 91.112  114.250 1.00 27.85 ?  184 LEU C C     1 
ATOM   12488 O  O     . LEU C 2 205 ? 109.335 90.440  114.531 1.00 27.07 ?  184 LEU C O     1 
ATOM   12489 C  CB    . LEU C 2 205 ? 107.039 89.690  115.911 1.00 27.76 ?  184 LEU C CB    1 
ATOM   12490 C  CG    . LEU C 2 205 ? 105.744 89.398  116.682 1.00 28.62 ?  184 LEU C CG    1 
ATOM   12491 C  CD1   . LEU C 2 205 ? 105.870 88.123  117.492 1.00 29.18 ?  184 LEU C CD1   1 
ATOM   12492 C  CD2   . LEU C 2 205 ? 105.366 90.561  117.586 1.00 28.43 ?  184 LEU C CD2   1 
ATOM   12493 N  N     . MET C 2 206 ? 108.357 92.076  113.342 1.00 28.15 ?  185 MET C N     1 
ATOM   12494 C  CA    . MET C 2 206 ? 109.501 92.213  112.468 1.00 28.80 ?  185 MET C CA    1 
ATOM   12495 C  C     . MET C 2 206 ? 110.714 92.884  113.099 1.00 28.77 ?  185 MET C C     1 
ATOM   12496 O  O     . MET C 2 206 ? 111.836 92.656  112.651 1.00 28.79 ?  185 MET C O     1 
ATOM   12497 C  CB    . MET C 2 206 ? 109.082 92.874  111.168 1.00 29.96 ?  185 MET C CB    1 
ATOM   12498 C  CG    . MET C 2 206 ? 108.159 91.962  110.355 1.00 31.23 ?  185 MET C CG    1 
ATOM   12499 S  SD    . MET C 2 206 ? 108.101 92.490  108.664 1.00 40.10 ?  185 MET C SD    1 
ATOM   12500 C  CE    . MET C 2 206 ? 109.709 92.003  108.071 1.00 35.10 ?  185 MET C CE    1 
ATOM   12501 N  N     . GLN C 2 207 ? 110.503 93.678  114.144 1.00 28.62 ?  186 GLN C N     1 
ATOM   12502 C  CA    . GLN C 2 207 ? 111.623 94.315  114.844 1.00 29.10 ?  186 GLN C CA    1 
ATOM   12503 C  C     . GLN C 2 207 ? 112.363 93.299  115.720 1.00 28.52 ?  186 GLN C C     1 
ATOM   12504 O  O     . GLN C 2 207 ? 113.587 93.209  115.651 1.00 28.28 ?  186 GLN C O     1 
ATOM   12505 C  CB    . GLN C 2 207 ? 111.170 95.528  115.663 1.00 29.21 ?  186 GLN C CB    1 
ATOM   12506 C  CG    . GLN C 2 207 ? 110.595 96.669  114.823 1.00 31.41 ?  186 GLN C CG    1 
ATOM   12507 C  CD    . GLN C 2 207 ? 111.624 97.286  113.898 1.00 34.70 ?  186 GLN C CD    1 
ATOM   12508 O  OE1   . GLN C 2 207 ? 111.765 96.874  112.750 1.00 37.69 ?  186 GLN C OE1   1 
ATOM   12509 N  NE2   . GLN C 2 207 ? 112.373 98.260  114.404 1.00 34.75 ?  186 GLN C NE2   1 
ATOM   12510 N  N     . SER C 2 208 ? 111.609 92.542  116.526 1.00 28.38 ?  187 SER C N     1 
ATOM   12511 C  CA    . SER C 2 208 ? 112.140 91.391  117.268 1.00 28.25 ?  187 SER C CA    1 
ATOM   12512 C  C     . SER C 2 208 ? 112.813 90.423  116.301 1.00 28.00 ?  187 SER C C     1 
ATOM   12513 O  O     . SER C 2 208 ? 113.884 89.892  116.595 1.00 27.90 ?  187 SER C O     1 
ATOM   12514 C  CB    . SER C 2 208 ? 111.018 90.641  117.988 1.00 27.88 ?  187 SER C CB    1 
ATOM   12515 O  OG    . SER C 2 208 ? 110.371 91.456  118.942 1.00 30.27 ?  187 SER C OG    1 
ATOM   12516 N  N     . GLY C 2 209 ? 112.160 90.196  115.157 1.00 27.31 ?  188 GLY C N     1 
ATOM   12517 C  CA    . GLY C 2 209 ? 112.676 89.316  114.111 1.00 27.86 ?  188 GLY C CA    1 
ATOM   12518 C  C     . GLY C 2 209 ? 113.999 89.780  113.530 1.00 27.96 ?  188 GLY C C     1 
ATOM   12519 O  O     . GLY C 2 209 ? 114.856 88.956  113.187 1.00 27.84 ?  188 GLY C O     1 
ATOM   12520 N  N     . GLU C 2 210 ? 114.164 91.098  113.414 1.00 28.21 ?  189 GLU C N     1 
ATOM   12521 C  CA    . GLU C 2 210 ? 115.418 91.682  112.949 1.00 29.15 ?  189 GLU C CA    1 
ATOM   12522 C  C     . GLU C 2 210 ? 116.565 91.372  113.931 1.00 28.02 ?  189 GLU C C     1 
ATOM   12523 O  O     . GLU C 2 210 ? 117.674 91.017  113.525 1.00 27.15 ?  189 GLU C O     1 
ATOM   12524 C  CB    . GLU C 2 210 ? 115.255 93.193  112.758 1.00 30.17 ?  189 GLU C CB    1 
ATOM   12525 C  CG    . GLU C 2 210 ? 115.736 93.710  111.412 1.00 35.68 ?  189 GLU C CG    1 
ATOM   12526 C  CD    . GLU C 2 210 ? 114.736 93.448  110.281 1.00 40.25 ?  189 GLU C CD    1 
ATOM   12527 O  OE1   . GLU C 2 210 ? 113.594 93.965  110.325 1.00 42.98 ?  189 GLU C OE1   1 
ATOM   12528 O  OE2   . GLU C 2 210 ? 115.099 92.728  109.330 1.00 43.59 -1 189 GLU C OE2   1 
ATOM   12529 N  N     . ILE C 2 211 ? 116.288 91.507  115.226 1.00 27.57 ?  190 ILE C N     1 
ATOM   12530 C  CA    . ILE C 2 211 ? 117.250 91.128  116.267 1.00 27.47 ?  190 ILE C CA    1 
ATOM   12531 C  C     . ILE C 2 211 ? 117.653 89.655  116.143 1.00 26.69 ?  190 ILE C C     1 
ATOM   12532 O  O     . ILE C 2 211 ? 118.843 89.314  116.113 1.00 26.56 ?  190 ILE C O     1 
ATOM   12533 C  CB    . ILE C 2 211 ? 116.698 91.447  117.688 1.00 27.84 ?  190 ILE C CB    1 
ATOM   12534 C  CG1   . ILE C 2 211 ? 116.674 92.969  117.905 1.00 28.56 ?  190 ILE C CG1   1 
ATOM   12535 C  CG2   . ILE C 2 211 ? 117.528 90.722  118.773 1.00 27.27 ?  190 ILE C CG2   1 
ATOM   12536 C  CD1   . ILE C 2 211 ? 116.200 93.404  119.288 1.00 30.09 ?  190 ILE C CD1   1 
ATOM   12537 N  N     . ILE C 2 212 ? 116.653 88.789  116.031 1.00 26.33 ?  191 ILE C N     1 
ATOM   12538 C  CA    . ILE C 2 212 ? 116.872 87.351  115.918 1.00 25.96 ?  191 ILE C CA    1 
ATOM   12539 C  C     . ILE C 2 212 ? 117.715 86.986  114.688 1.00 25.46 ?  191 ILE C C     1 
ATOM   12540 O  O     . ILE C 2 212 ? 118.589 86.128  114.780 1.00 24.84 ?  191 ILE C O     1 
ATOM   12541 C  CB    . ILE C 2 212 ? 115.523 86.567  115.946 1.00 26.00 ?  191 ILE C CB    1 
ATOM   12542 C  CG1   . ILE C 2 212 ? 114.835 86.729  117.311 1.00 27.16 ?  191 ILE C CG1   1 
ATOM   12543 C  CG2   . ILE C 2 212 ? 115.715 85.093  115.618 1.00 26.87 ?  191 ILE C CG2   1 
ATOM   12544 C  CD1   . ILE C 2 212 ? 115.597 86.148  118.488 1.00 29.84 ?  191 ILE C CD1   1 
ATOM   12545 N  N     . ASN C 2 213 ? 117.456 87.638  113.551 1.00 25.35 ?  192 ASN C N     1 
ATOM   12546 C  CA    . ASN C 2 213 ? 118.252 87.419  112.338 1.00 25.60 ?  192 ASN C CA    1 
ATOM   12547 C  C     . ASN C 2 213 ? 119.714 87.813  112.516 1.00 25.14 ?  192 ASN C C     1 
ATOM   12548 O  O     . ASN C 2 213 ? 120.621 87.154  111.985 1.00 25.61 ?  192 ASN C O     1 
ATOM   12549 C  CB    . ASN C 2 213 ? 117.659 88.162  111.133 1.00 26.55 ?  192 ASN C CB    1 
ATOM   12550 C  CG    . ASN C 2 213 ? 116.601 87.352  110.417 1.00 28.10 ?  192 ASN C CG    1 
ATOM   12551 O  OD1   . ASN C 2 213 ? 116.878 86.278  109.872 1.00 31.67 ?  192 ASN C OD1   1 
ATOM   12552 N  ND2   . ASN C 2 213 ? 115.384 87.865  110.400 1.00 30.36 ?  192 ASN C ND2   1 
ATOM   12553 N  N     . LEU C 2 214 ? 119.946 88.884  113.265 1.00 24.54 ?  193 LEU C N     1 
ATOM   12554 C  CA    . LEU C 2 214 ? 121.316 89.294  113.585 1.00 24.40 ?  193 LEU C CA    1 
ATOM   12555 C  C     . LEU C 2 214 ? 122.004 88.262  114.480 1.00 23.55 ?  193 LEU C C     1 
ATOM   12556 O  O     . LEU C 2 214 ? 123.157 87.896  114.235 1.00 23.09 ?  193 LEU C O     1 
ATOM   12557 C  CB    . LEU C 2 214 ? 121.343 90.693  114.195 1.00 24.00 ?  193 LEU C CB    1 
ATOM   12558 C  CG    . LEU C 2 214 ? 121.045 91.851  113.217 1.00 25.69 ?  193 LEU C CG    1 
ATOM   12559 C  CD1   . LEU C 2 214 ? 120.805 93.167  113.959 1.00 26.28 ?  193 LEU C CD1   1 
ATOM   12560 C  CD2   . LEU C 2 214 ? 122.168 92.037  112.194 1.00 26.05 ?  193 LEU C CD2   1 
ATOM   12561 N  N     . ILE C 2 215 ? 121.291 87.786  115.504 1.00 23.19 ?  194 ILE C N     1 
ATOM   12562 C  CA    . ILE C 2 215 ? 121.779 86.701  116.362 1.00 22.88 ?  194 ILE C CA    1 
ATOM   12563 C  C     . ILE C 2 215 ? 122.094 85.465  115.504 1.00 23.81 ?  194 ILE C C     1 
ATOM   12564 O  O     . ILE C 2 215 ? 123.172 84.881  115.625 1.00 23.83 ?  194 ILE C O     1 
ATOM   12565 C  CB    . ILE C 2 215 ? 120.769 86.346  117.490 1.00 22.92 ?  194 ILE C CB    1 
ATOM   12566 C  CG1   . ILE C 2 215 ? 120.530 87.552  118.400 1.00 21.11 ?  194 ILE C CG1   1 
ATOM   12567 C  CG2   . ILE C 2 215 ? 121.237 85.132  118.308 1.00 21.89 ?  194 ILE C CG2   1 
ATOM   12568 C  CD1   . ILE C 2 215 ? 119.536 87.304  119.516 1.00 22.26 ?  194 ILE C CD1   1 
ATOM   12569 N  N     . LEU C 2 216 ? 121.178 85.096  114.609 1.00 24.23 ?  195 LEU C N     1 
ATOM   12570 C  CA    . LEU C 2 216 ? 121.360 83.899  113.778 1.00 25.41 ?  195 LEU C CA    1 
ATOM   12571 C  C     . LEU C 2 216 ? 122.565 84.030  112.844 1.00 25.63 ?  195 LEU C C     1 
ATOM   12572 O  O     . LEU C 2 216 ? 123.344 83.079  112.683 1.00 25.46 ?  195 LEU C O     1 
ATOM   12573 C  CB    . LEU C 2 216 ? 120.079 83.583  112.984 1.00 26.03 ?  195 LEU C CB    1 
ATOM   12574 C  CG    . LEU C 2 216 ? 120.004 82.345  112.079 1.00 28.00 ?  195 LEU C CG    1 
ATOM   12575 C  CD1   . LEU C 2 216 ? 118.545 81.985  111.857 1.00 31.45 ?  195 LEU C CD1   1 
ATOM   12576 C  CD2   . LEU C 2 216 ? 120.719 82.554  110.739 1.00 29.83 ?  195 LEU C CD2   1 
ATOM   12577 N  N     . ARG C 2 217 ? 122.714 85.206  112.240 1.00 25.98 ?  196 ARG C N     1 
ATOM   12578 C  CA    . ARG C 2 217 ? 123.868 85.512  111.401 1.00 26.73 ?  196 ARG C CA    1 
ATOM   12579 C  C     . ARG C 2 217 ? 125.190 85.295  112.180 1.00 25.95 ?  196 ARG C C     1 
ATOM   12580 O  O     . ARG C 2 217 ? 126.126 84.698  111.637 1.00 25.75 ?  196 ARG C O     1 
ATOM   12581 C  CB    . ARG C 2 217 ? 123.767 86.946  110.876 1.00 27.29 ?  196 ARG C CB    1 
ATOM   12582 C  CG    . ARG C 2 217 ? 124.761 87.318  109.767 1.00 30.12 ?  196 ARG C CG    1 
ATOM   12583 C  CD    . ARG C 2 217 ? 125.097 88.795  109.860 1.00 35.40 ?  196 ARG C CD    1 
ATOM   12584 N  NE    . ARG C 2 217 ? 125.349 89.127  111.263 1.00 39.87 ?  196 ARG C NE    1 
ATOM   12585 C  CZ    . ARG C 2 217 ? 125.449 90.349  111.770 1.00 40.55 ?  196 ARG C CZ    1 
ATOM   12586 N  NH1   . ARG C 2 217 ? 125.331 91.428  110.997 1.00 40.77 1  196 ARG C NH1   1 
ATOM   12587 N  NH2   . ARG C 2 217 ? 125.666 90.480  113.073 1.00 41.10 ?  196 ARG C NH2   1 
ATOM   12588 N  N     . ASP C 2 218 ? 125.246 85.763  113.432 1.00 24.70 ?  197 ASP C N     1 
ATOM   12589 C  CA    . ASP C 2 218 ? 126.403 85.522  114.319 1.00 24.55 ?  197 ASP C CA    1 
ATOM   12590 C  C     . ASP C 2 218 ? 126.616 84.020  114.595 1.00 24.23 ?  197 ASP C C     1 
ATOM   12591 O  O     . ASP C 2 218 ? 127.728 83.513  114.424 1.00 23.69 ?  197 ASP C O     1 
ATOM   12592 C  CB    . ASP C 2 218 ? 126.283 86.265  115.666 1.00 24.50 ?  197 ASP C CB    1 
ATOM   12593 C  CG    . ASP C 2 218 ? 126.348 87.798  115.537 1.00 25.84 ?  197 ASP C CG    1 
ATOM   12594 O  OD1   . ASP C 2 218 ? 126.917 88.334  114.561 1.00 26.91 ?  197 ASP C OD1   1 
ATOM   12595 O  OD2   . ASP C 2 218 ? 125.836 88.477  116.449 1.00 25.72 -1 197 ASP C OD2   1 
ATOM   12596 N  N     . GLU C 2 219 ? 125.557 83.307  114.992 1.00 23.92 ?  198 GLU C N     1 
ATOM   12597 C  CA    . GLU C 2 219 ? 125.726 81.895  115.375 1.00 24.20 ?  198 GLU C CA    1 
ATOM   12598 C  C     . GLU C 2 219 ? 126.208 81.051  114.209 1.00 24.02 ?  198 GLU C C     1 
ATOM   12599 O  O     . GLU C 2 219 ? 126.981 80.123  114.414 1.00 24.24 ?  198 GLU C O     1 
ATOM   12600 C  CB    . GLU C 2 219 ? 124.462 81.265  115.968 1.00 24.05 ?  198 GLU C CB    1 
ATOM   12601 C  CG    . GLU C 2 219 ? 123.633 82.131  116.899 1.00 25.03 ?  198 GLU C CG    1 
ATOM   12602 C  CD    . GLU C 2 219 ? 124.243 82.424  118.283 1.00 26.31 ?  198 GLU C CD    1 
ATOM   12603 O  OE1   . GLU C 2 219 ? 125.492 82.383  118.487 1.00 27.65 ?  198 GLU C OE1   1 
ATOM   12604 O  OE2   . GLU C 2 219 ? 123.422 82.739  119.188 1.00 26.87 -1 198 GLU C OE2   1 
ATOM   12605 N  N     . ALA C 2 220 ? 125.754 81.370  112.995 1.00 24.00 ?  199 ALA C N     1 
ATOM   12606 C  CA    . ALA C 2 220 ? 126.195 80.649  111.807 1.00 24.72 ?  199 ALA C CA    1 
ATOM   12607 C  C     . ALA C 2 220 ? 127.722 80.700  111.636 1.00 24.80 ?  199 ALA C C     1 
ATOM   12608 O  O     . ALA C 2 220 ? 128.351 79.671  111.374 1.00 25.04 ?  199 ALA C O     1 
ATOM   12609 C  CB    . ALA C 2 220 ? 125.476 81.165  110.534 1.00 24.66 ?  199 ALA C CB    1 
ATOM   12610 N  N     . ILE C 2 221 ? 128.311 81.884  111.795 1.00 24.85 ?  200 ILE C N     1 
ATOM   12611 C  CA    . ILE C 2 221 ? 129.776 82.020  111.700 1.00 25.07 ?  200 ILE C CA    1 
ATOM   12612 C  C     . ILE C 2 221 ? 130.498 81.440  112.925 1.00 23.86 ?  200 ILE C C     1 
ATOM   12613 O  O     . ILE C 2 221 ? 131.601 80.903  112.789 1.00 23.72 ?  200 ILE C O     1 
ATOM   12614 C  CB    . ILE C 2 221 ? 130.263 83.479  111.378 1.00 25.71 ?  200 ILE C CB    1 
ATOM   12615 C  CG1   . ILE C 2 221 ? 130.114 84.408  112.586 1.00 27.10 ?  200 ILE C CG1   1 
ATOM   12616 C  CG2   . ILE C 2 221 ? 129.561 84.025  110.119 1.00 27.18 ?  200 ILE C CG2   1 
ATOM   12617 C  CD1   . ILE C 2 221 ? 130.742 85.797  112.419 1.00 29.63 ?  200 ILE C CD1   1 
ATOM   12618 N  N     . HIS C 2 222 ? 129.875 81.531  114.100 1.00 22.79 ?  201 HIS C N     1 
ATOM   12619 C  CA    . HIS C 2 222 ? 130.426 80.899  115.320 1.00 22.48 ?  201 HIS C CA    1 
ATOM   12620 C  C     . HIS C 2 222 ? 130.514 79.382  115.169 1.00 22.04 ?  201 HIS C C     1 
ATOM   12621 O  O     . HIS C 2 222 ? 131.510 78.783  115.559 1.00 22.06 ?  201 HIS C O     1 
ATOM   12622 C  CB    . HIS C 2 222 ? 129.566 81.178  116.555 1.00 21.77 ?  201 HIS C CB    1 
ATOM   12623 C  CG    . HIS C 2 222 ? 129.527 82.608  116.977 1.00 21.76 ?  201 HIS C CG    1 
ATOM   12624 N  ND1   . HIS C 2 222 ? 128.887 83.016  118.126 1.00 20.70 ?  201 HIS C ND1   1 
ATOM   12625 C  CD2   . HIS C 2 222 ? 130.046 83.726  116.419 1.00 22.07 ?  201 HIS C CD2   1 
ATOM   12626 C  CE1   . HIS C 2 222 ? 129.002 84.324  118.253 1.00 22.26 ?  201 HIS C CE1   1 
ATOM   12627 N  NE2   . HIS C 2 222 ? 129.694 84.780  117.227 1.00 22.52 ?  201 HIS C NE2   1 
ATOM   12628 N  N     . GLY C 2 223 ? 129.453 78.770  114.641 1.00 22.35 ?  202 GLY C N     1 
ATOM   12629 C  CA    . GLY C 2 223 ? 129.410 77.320  114.392 1.00 22.01 ?  202 GLY C CA    1 
ATOM   12630 C  C     . GLY C 2 223 ? 130.439 76.850  113.367 1.00 22.73 ?  202 GLY C C     1 
ATOM   12631 O  O     . GLY C 2 223 ? 131.065 75.790  113.537 1.00 21.99 ?  202 GLY C O     1 
ATOM   12632 N  N     . VAL C 2 224 ? 130.626 77.635  112.304 1.00 22.45 ?  203 VAL C N     1 
ATOM   12633 C  CA    . VAL C 2 224 ? 131.647 77.318  111.303 1.00 22.54 ?  203 VAL C CA    1 
ATOM   12634 C  C     . VAL C 2 224 ? 133.047 77.386  111.917 1.00 22.28 ?  203 VAL C C     1 
ATOM   12635 O  O     . VAL C 2 224 ? 133.831 76.450  111.783 1.00 22.44 ?  203 VAL C O     1 
ATOM   12636 C  CB    . VAL C 2 224 ? 131.564 78.239  110.039 1.00 23.00 ?  203 VAL C CB    1 
ATOM   12637 C  CG1   . VAL C 2 224 ? 132.781 78.015  109.123 1.00 23.10 ?  203 VAL C CG1   1 
ATOM   12638 C  CG2   . VAL C 2 224 ? 130.252 77.984  109.248 1.00 23.14 ?  203 VAL C CG2   1 
ATOM   12639 N  N     . TYR C 2 225 ? 133.338 78.480  112.618 1.00 22.41 ?  204 TYR C N     1 
ATOM   12640 C  CA    . TYR C 2 225 ? 134.656 78.682  113.219 1.00 22.03 ?  204 TYR C CA    1 
ATOM   12641 C  C     . TYR C 2 225 ? 135.030 77.582  114.210 1.00 21.66 ?  204 TYR C C     1 
ATOM   12642 O  O     . TYR C 2 225 ? 136.094 76.960  114.082 1.00 21.72 ?  204 TYR C O     1 
ATOM   12643 C  CB    . TYR C 2 225 ? 134.772 80.065  113.879 1.00 22.22 ?  204 TYR C CB    1 
ATOM   12644 C  CG    . TYR C 2 225 ? 136.189 80.388  114.311 1.00 21.92 ?  204 TYR C CG    1 
ATOM   12645 C  CD1   . TYR C 2 225 ? 137.190 80.610  113.365 1.00 22.36 ?  204 TYR C CD1   1 
ATOM   12646 C  CD2   . TYR C 2 225 ? 136.525 80.459  115.663 1.00 21.43 ?  204 TYR C CD2   1 
ATOM   12647 C  CE1   . TYR C 2 225 ? 138.499 80.890  113.757 1.00 23.82 ?  204 TYR C CE1   1 
ATOM   12648 C  CE2   . TYR C 2 225 ? 137.832 80.748  116.072 1.00 21.49 ?  204 TYR C CE2   1 
ATOM   12649 C  CZ    . TYR C 2 225 ? 138.805 80.961  115.115 1.00 23.58 ?  204 TYR C CZ    1 
ATOM   12650 O  OH    . TYR C 2 225 ? 140.085 81.243  115.512 1.00 25.42 ?  204 TYR C OH    1 
ATOM   12651 N  N     . VAL C 2 226 ? 134.159 77.332  115.191 1.00 20.95 ?  205 VAL C N     1 
ATOM   12652 C  CA    . VAL C 2 226 ? 134.402 76.259  116.164 1.00 20.49 ?  205 VAL C CA    1 
ATOM   12653 C  C     . VAL C 2 226 ? 134.497 74.893  115.462 1.00 20.84 ?  205 VAL C C     1 
ATOM   12654 O  O     . VAL C 2 226 ? 135.351 74.064  115.805 1.00 21.10 ?  205 VAL C O     1 
ATOM   12655 C  CB    . VAL C 2 226 ? 133.370 76.266  117.325 1.00 20.57 ?  205 VAL C CB    1 
ATOM   12656 C  CG1   . VAL C 2 226 ? 133.635 75.107  118.287 1.00 20.35 ?  205 VAL C CG1   1 
ATOM   12657 C  CG2   . VAL C 2 226 ? 133.445 77.602  118.079 1.00 19.60 ?  205 VAL C CG2   1 
ATOM   12658 N  N     . GLY C 2 227 ? 133.661 74.683  114.450 1.00 21.08 ?  206 GLY C N     1 
ATOM   12659 C  CA    . GLY C 2 227 ? 133.761 73.481  113.607 1.00 21.43 ?  206 GLY C CA    1 
ATOM   12660 C  C     . GLY C 2 227 ? 135.138 73.273  112.989 1.00 21.95 ?  206 GLY C C     1 
ATOM   12661 O  O     . GLY C 2 227 ? 135.668 72.149  112.984 1.00 21.84 ?  206 GLY C O     1 
ATOM   12662 N  N     . LEU C 2 228 ? 135.728 74.350  112.471 1.00 22.09 ?  207 LEU C N     1 
ATOM   12663 C  CA    . LEU C 2 228 ? 137.071 74.265  111.889 1.00 22.96 ?  207 LEU C CA    1 
ATOM   12664 C  C     . LEU C 2 228 ? 138.138 73.909  112.936 1.00 22.60 ?  207 LEU C C     1 
ATOM   12665 O  O     . LEU C 2 228 ? 139.047 73.120  112.659 1.00 22.04 ?  207 LEU C O     1 
ATOM   12666 C  CB    . LEU C 2 228 ? 137.437 75.544  111.125 1.00 23.39 ?  207 LEU C CB    1 
ATOM   12667 C  CG    . LEU C 2 228 ? 136.635 75.868  109.851 1.00 24.35 ?  207 LEU C CG    1 
ATOM   12668 C  CD1   . LEU C 2 228 ? 136.824 77.344  109.474 1.00 25.01 ?  207 LEU C CD1   1 
ATOM   12669 C  CD2   . LEU C 2 228 ? 137.015 74.969  108.680 1.00 25.11 ?  207 LEU C CD2   1 
ATOM   12670 N  N     . LEU C 2 229 ? 138.013 74.461  114.140 1.00 22.37 ?  208 LEU C N     1 
ATOM   12671 C  CA    . LEU C 2 229 ? 138.931 74.105  115.240 1.00 22.62 ?  208 LEU C CA    1 
ATOM   12672 C  C     . LEU C 2 229 ? 138.797 72.637  115.661 1.00 22.77 ?  208 LEU C C     1 
ATOM   12673 O  O     . LEU C 2 229 ? 139.805 71.954  115.911 1.00 22.57 ?  208 LEU C O     1 
ATOM   12674 C  CB    . LEU C 2 229 ? 138.753 75.041  116.439 1.00 22.44 ?  208 LEU C CB    1 
ATOM   12675 C  CG    . LEU C 2 229 ? 138.950 76.538  116.159 1.00 23.54 ?  208 LEU C CG    1 
ATOM   12676 C  CD1   . LEU C 2 229 ? 138.647 77.363  117.407 1.00 23.37 ?  208 LEU C CD1   1 
ATOM   12677 C  CD2   . LEU C 2 229 ? 140.367 76.837  115.636 1.00 23.91 ?  208 LEU C CD2   1 
ATOM   12678 N  N     . ALA C 2 230 ? 137.556 72.154  115.726 1.00 22.42 ?  209 ALA C N     1 
ATOM   12679 C  CA    . ALA C 2 230 ? 137.289 70.749  116.028 1.00 22.02 ?  209 ALA C CA    1 
ATOM   12680 C  C     . ALA C 2 230 ? 137.913 69.823  114.978 1.00 22.58 ?  209 ALA C C     1 
ATOM   12681 O  O     . ALA C 2 230 ? 138.549 68.836  115.323 1.00 22.14 ?  209 ALA C O     1 
ATOM   12682 C  CB    . ALA C 2 230 ? 135.801 70.501  116.129 1.00 22.04 ?  209 ALA C CB    1 
ATOM   12683 N  N     . GLN C 2 231 ? 137.741 70.166  113.703 1.00 22.96 ?  210 GLN C N     1 
ATOM   12684 C  CA    . GLN C 2 231 ? 138.344 69.387  112.606 1.00 24.30 ?  210 GLN C CA    1 
ATOM   12685 C  C     . GLN C 2 231 ? 139.859 69.323  112.681 1.00 25.11 ?  210 GLN C C     1 
ATOM   12686 O  O     . GLN C 2 231 ? 140.455 68.299  112.332 1.00 24.97 ?  210 GLN C O     1 
ATOM   12687 C  CB    . GLN C 2 231 ? 137.916 69.939  111.250 1.00 24.38 ?  210 GLN C CB    1 
ATOM   12688 C  CG    . GLN C 2 231 ? 136.423 69.720  110.957 1.00 25.12 ?  210 GLN C CG    1 
ATOM   12689 C  CD    . GLN C 2 231 ? 136.016 70.271  109.607 1.00 28.08 ?  210 GLN C CD    1 
ATOM   12690 O  OE1   . GLN C 2 231 ? 136.602 69.920  108.582 1.00 27.83 ?  210 GLN C OE1   1 
ATOM   12691 N  NE2   . GLN C 2 231 ? 135.015 71.154  109.598 1.00 26.38 ?  210 GLN C NE2   1 
ATOM   12692 N  N     . GLU C 2 232 ? 140.483 70.414  113.131 1.00 25.80 ?  211 GLU C N     1 
ATOM   12693 C  CA    . GLU C 2 232 ? 141.935 70.428  113.340 1.00 27.16 ?  211 GLU C CA    1 
ATOM   12694 C  C     . GLU C 2 232 ? 142.365 69.314  114.290 1.00 26.47 ?  211 GLU C C     1 
ATOM   12695 O  O     . GLU C 2 232 ? 143.344 68.605  114.030 1.00 26.10 ?  211 GLU C O     1 
ATOM   12696 C  CB    . GLU C 2 232 ? 142.389 71.754  113.936 1.00 27.59 ?  211 GLU C CB    1 
ATOM   12697 C  CG    . GLU C 2 232 ? 142.767 72.800  112.932 1.00 32.55 ?  211 GLU C CG    1 
ATOM   12698 C  CD    . GLU C 2 232 ? 143.874 73.713  113.443 1.00 36.72 ?  211 GLU C CD    1 
ATOM   12699 O  OE1   . GLU C 2 232 ? 144.280 73.584  114.623 1.00 38.32 ?  211 GLU C OE1   1 
ATOM   12700 O  OE2   . GLU C 2 232 ? 144.343 74.557  112.654 1.00 40.62 -1 211 GLU C OE2   1 
ATOM   12701 N  N     . ILE C 2 233 ? 141.639 69.180  115.399 1.00 25.55 ?  212 ILE C N     1 
ATOM   12702 C  CA    . ILE C 2 233 ? 141.966 68.175  116.410 1.00 25.32 ?  212 ILE C CA    1 
ATOM   12703 C  C     . ILE C 2 233 ? 141.677 66.766  115.907 1.00 25.48 ?  212 ILE C C     1 
ATOM   12704 O  O     . ILE C 2 233 ? 142.522 65.875  116.020 1.00 25.82 ?  212 ILE C O     1 
ATOM   12705 C  CB    . ILE C 2 233 ? 141.238 68.439  117.746 1.00 25.39 ?  212 ILE C CB    1 
ATOM   12706 C  CG1   . ILE C 2 233 ? 141.772 69.728  118.376 1.00 24.37 ?  212 ILE C CG1   1 
ATOM   12707 C  CG2   . ILE C 2 233 ? 141.402 67.245  118.693 1.00 24.86 ?  212 ILE C CG2   1 
ATOM   12708 C  CD1   . ILE C 2 233 ? 140.868 70.299  119.457 1.00 25.10 ?  212 ILE C CD1   1 
ATOM   12709 N  N     . TYR C 2 234 ? 140.494 66.580  115.328 1.00 25.27 ?  213 TYR C N     1 
ATOM   12710 C  CA    . TYR C 2 234 ? 140.106 65.313  114.705 1.00 25.77 ?  213 TYR C CA    1 
ATOM   12711 C  C     . TYR C 2 234 ? 141.143 64.828  113.676 1.00 26.44 ?  213 TYR C C     1 
ATOM   12712 O  O     . TYR C 2 234 ? 141.478 63.642  113.629 1.00 26.29 ?  213 TYR C O     1 
ATOM   12713 C  CB    . TYR C 2 234 ? 138.726 65.477  114.047 1.00 25.67 ?  213 TYR C CB    1 
ATOM   12714 C  CG    . TYR C 2 234 ? 138.180 64.282  113.294 1.00 25.65 ?  213 TYR C CG    1 
ATOM   12715 C  CD1   . TYR C 2 234 ? 137.354 63.352  113.930 1.00 25.02 ?  213 TYR C CD1   1 
ATOM   12716 C  CD2   . TYR C 2 234 ? 138.441 64.112  111.925 1.00 26.59 ?  213 TYR C CD2   1 
ATOM   12717 C  CE1   . TYR C 2 234 ? 136.827 62.267  113.237 1.00 26.52 ?  213 TYR C CE1   1 
ATOM   12718 C  CE2   . TYR C 2 234 ? 137.923 63.025  111.220 1.00 27.00 ?  213 TYR C CE2   1 
ATOM   12719 C  CZ    . TYR C 2 234 ? 137.120 62.108  111.887 1.00 27.79 ?  213 TYR C CZ    1 
ATOM   12720 O  OH    . TYR C 2 234 ? 136.594 61.049  111.203 1.00 29.00 ?  213 TYR C OH    1 
ATOM   12721 N  N     . ASN C 2 235 ? 141.648 65.744  112.853 1.00 26.96 ?  214 ASN C N     1 
ATOM   12722 C  CA    . ASN C 2 235 ? 142.585 65.366  111.796 1.00 28.05 ?  214 ASN C CA    1 
ATOM   12723 C  C     . ASN C 2 235 ? 143.954 64.910  112.288 1.00 28.24 ?  214 ASN C C     1 
ATOM   12724 O  O     . ASN C 2 235 ? 144.708 64.307  111.529 1.00 28.63 ?  214 ASN C O     1 
ATOM   12725 C  CB    . ASN C 2 235 ? 142.706 66.468  110.732 1.00 28.38 ?  214 ASN C CB    1 
ATOM   12726 C  CG    . ASN C 2 235 ? 141.421 66.647  109.931 1.00 31.14 ?  214 ASN C CG    1 
ATOM   12727 O  OD1   . ASN C 2 235 ? 140.675 65.690  109.701 1.00 34.16 ?  214 ASN C OD1   1 
ATOM   12728 N  ND2   . ASN C 2 235 ? 141.156 67.877  109.507 1.00 32.42 ?  214 ASN C ND2   1 
ATOM   12729 N  N     . LYS C 2 236 ? 144.262 65.175  113.557 1.00 27.91 ?  215 LYS C N     1 
ATOM   12730 C  CA    . LYS C 2 236 ? 145.507 64.716  114.178 1.00 28.49 ?  215 LYS C CA    1 
ATOM   12731 C  C     . LYS C 2 236 ? 145.459 63.253  114.631 1.00 28.50 ?  215 LYS C C     1 
ATOM   12732 O  O     . LYS C 2 236 ? 146.494 62.661  114.947 1.00 28.98 ?  215 LYS C O     1 
ATOM   12733 C  CB    . LYS C 2 236 ? 145.871 65.602  115.375 1.00 28.10 ?  215 LYS C CB    1 
ATOM   12734 C  CG    . LYS C 2 236 ? 146.183 67.047  115.015 1.00 29.25 ?  215 LYS C CG    1 
ATOM   12735 C  CD    . LYS C 2 236 ? 146.556 67.859  116.244 1.00 30.19 ?  215 LYS C CD    1 
ATOM   12736 C  CE    . LYS C 2 236 ? 146.553 69.332  115.911 1.00 32.63 ?  215 LYS C CE    1 
ATOM   12737 N  NZ    . LYS C 2 236 ? 146.904 70.157  117.091 1.00 35.39 1  215 LYS C NZ    1 
ATOM   12738 N  N     . GLN C 2 237 ? 144.270 62.662  114.646 1.00 28.25 ?  216 GLN C N     1 
ATOM   12739 C  CA    . GLN C 2 237 ? 144.096 61.344  115.258 1.00 28.34 ?  216 GLN C CA    1 
ATOM   12740 C  C     . GLN C 2 237 ? 144.389 60.169  114.310 1.00 28.92 ?  216 GLN C C     1 
ATOM   12741 O  O     . GLN C 2 237 ? 144.372 60.326  113.088 1.00 28.53 ?  216 GLN C O     1 
ATOM   12742 C  CB    . GLN C 2 237 ? 142.690 61.232  115.865 1.00 27.68 ?  216 GLN C CB    1 
ATOM   12743 C  CG    . GLN C 2 237 ? 142.298 62.410  116.790 1.00 26.67 ?  216 GLN C CG    1 
ATOM   12744 C  CD    . GLN C 2 237 ? 143.334 62.721  117.865 1.00 25.32 ?  216 GLN C CD    1 
ATOM   12745 O  OE1   . GLN C 2 237 ? 143.869 61.820  118.515 1.00 25.49 ?  216 GLN C OE1   1 
ATOM   12746 N  NE2   . GLN C 2 237 ? 143.619 64.006  118.060 1.00 23.63 ?  216 GLN C NE2   1 
ATOM   12747 N  N     . THR C 2 238 ? 144.652 58.996  114.886 1.00 29.53 ?  217 THR C N     1 
ATOM   12748 C  CA    . THR C 2 238 ? 144.696 57.749  114.117 1.00 30.73 ?  217 THR C CA    1 
ATOM   12749 C  C     . THR C 2 238 ? 143.300 57.456  113.553 1.00 31.13 ?  217 THR C C     1 
ATOM   12750 O  O     . THR C 2 238 ? 142.298 58.032  114.016 1.00 30.17 ?  217 THR C O     1 
ATOM   12751 C  CB    . THR C 2 238 ? 145.097 56.544  114.987 1.00 30.79 ?  217 THR C CB    1 
ATOM   12752 O  OG1   . THR C 2 238 ? 144.046 56.268  115.923 1.00 31.16 ?  217 THR C OG1   1 
ATOM   12753 C  CG2   . THR C 2 238 ? 146.406 56.804  115.740 1.00 31.22 ?  217 THR C CG2   1 
ATOM   12754 N  N     . GLU C 2 239 ? 143.230 56.545  112.580 1.00 31.67 ?  218 GLU C N     1 
ATOM   12755 C  CA    . GLU C 2 239 ? 141.939 56.146  112.017 1.00 32.25 ?  218 GLU C CA    1 
ATOM   12756 C  C     . GLU C 2 239 ? 141.022 55.518  113.072 1.00 31.86 ?  218 GLU C C     1 
ATOM   12757 O  O     . GLU C 2 239 ? 139.813 55.766  113.084 1.00 31.09 ?  218 GLU C O     1 
ATOM   12758 C  CB    . GLU C 2 239 ? 142.127 55.222  110.801 1.00 33.29 ?  218 GLU C CB    1 
ATOM   12759 C  CG    . GLU C 2 239 ? 142.739 55.935  109.580 1.00 35.65 ?  218 GLU C CG    1 
ATOM   12760 C  CD    . GLU C 2 239 ? 141.897 57.121  109.095 1.00 39.17 ?  218 GLU C CD    1 
ATOM   12761 O  OE1   . GLU C 2 239 ? 140.655 56.973  108.970 1.00 41.08 ?  218 GLU C OE1   1 
ATOM   12762 O  OE2   . GLU C 2 239 ? 142.475 58.208  108.845 1.00 39.64 -1 218 GLU C OE2   1 
ATOM   12763 N  N     . GLU C 2 240 ? 141.617 54.738  113.975 1.00 31.72 ?  219 GLU C N     1 
ATOM   12764 C  CA    . GLU C 2 240 ? 140.891 54.105  115.069 1.00 31.76 ?  219 GLU C CA    1 
ATOM   12765 C  C     . GLU C 2 240 ? 140.284 55.150  116.016 1.00 30.21 ?  219 GLU C C     1 
ATOM   12766 O  O     . GLU C 2 240 ? 139.110 55.048  116.403 1.00 29.63 ?  219 GLU C O     1 
ATOM   12767 C  CB    . GLU C 2 240 ? 141.824 53.151  115.819 1.00 32.58 ?  219 GLU C CB    1 
ATOM   12768 C  CG    . GLU C 2 240 ? 141.138 52.251  116.834 1.00 36.93 ?  219 GLU C CG    1 
ATOM   12769 C  CD    . GLU C 2 240 ? 142.017 51.081  117.262 1.00 42.06 ?  219 GLU C CD    1 
ATOM   12770 O  OE1   . GLU C 2 240 ? 142.423 51.035  118.445 1.00 44.09 ?  219 GLU C OE1   1 
ATOM   12771 O  OE2   . GLU C 2 240 ? 142.309 50.208  116.411 1.00 44.45 -1 219 GLU C OE2   1 
ATOM   12772 N  N     . LYS C 2 241 ? 141.085 56.154  116.369 1.00 28.91 ?  220 LYS C N     1 
ATOM   12773 C  CA    . LYS C 2 241 ? 140.637 57.241  117.230 1.00 28.14 ?  220 LYS C CA    1 
ATOM   12774 C  C     . LYS C 2 241 ? 139.538 58.080  116.575 1.00 27.03 ?  220 LYS C C     1 
ATOM   12775 O  O     . LYS C 2 241 ? 138.564 58.454  117.236 1.00 26.72 ?  220 LYS C O     1 
ATOM   12776 C  CB    . LYS C 2 241 ? 141.811 58.131  117.649 1.00 27.83 ?  220 LYS C CB    1 
ATOM   12777 C  CG    . LYS C 2 241 ? 141.426 59.227  118.652 1.00 29.68 ?  220 LYS C CG    1 
ATOM   12778 C  CD    . LYS C 2 241 ? 141.744 58.834  120.087 1.00 33.58 ?  220 LYS C CD    1 
ATOM   12779 C  CE    . LYS C 2 241 ? 140.664 57.982  120.694 1.00 33.71 ?  220 LYS C CE    1 
ATOM   12780 N  NZ    . LYS C 2 241 ? 141.045 57.457  122.047 1.00 34.69 1  220 LYS C NZ    1 
ATOM   12781 N  N     . LYS C 2 242 ? 139.710 58.372  115.285 1.00 26.38 ?  221 LYS C N     1 
ATOM   12782 C  CA    . LYS C 2 242 ? 138.707 59.075  114.480 1.00 25.87 ?  221 LYS C CA    1 
ATOM   12783 C  C     . LYS C 2 242 ? 137.366 58.365  114.496 1.00 25.72 ?  221 LYS C C     1 
ATOM   12784 O  O     . LYS C 2 242 ? 136.320 59.011  114.653 1.00 24.52 ?  221 LYS C O     1 
ATOM   12785 C  CB    . LYS C 2 242 ? 139.169 59.237  113.031 1.00 25.83 ?  221 LYS C CB    1 
ATOM   12786 C  CG    . LYS C 2 242 ? 140.213 60.308  112.809 1.00 26.76 ?  221 LYS C CG    1 
ATOM   12787 C  CD    . LYS C 2 242 ? 140.487 60.462  111.317 1.00 28.40 ?  221 LYS C CD    1 
ATOM   12788 C  CE    . LYS C 2 242 ? 141.674 61.345  111.056 1.00 29.84 ?  221 LYS C CE    1 
ATOM   12789 N  NZ    . LYS C 2 242 ? 142.053 61.301  109.624 1.00 30.96 1  221 LYS C NZ    1 
ATOM   12790 N  N     . ALA C 2 243 ? 137.405 57.041  114.320 1.00 25.97 ?  222 ALA C N     1 
ATOM   12791 C  CA    . ALA C 2 243 ? 136.197 56.214  114.378 1.00 25.79 ?  222 ALA C CA    1 
ATOM   12792 C  C     . ALA C 2 243 ? 135.472 56.366  115.717 1.00 25.24 ?  222 ALA C C     1 
ATOM   12793 O  O     . ALA C 2 243 ? 134.237 56.463  115.749 1.00 25.37 ?  222 ALA C O     1 
ATOM   12794 C  CB    . ALA C 2 243 ? 136.526 54.749  114.088 1.00 26.17 ?  222 ALA C CB    1 
ATOM   12795 N  N     . GLU C 2 244 ? 136.227 56.418  116.812 1.00 25.02 ?  223 GLU C N     1 
ATOM   12796 C  CA    . GLU C 2 244 ? 135.639 56.654  118.140 1.00 25.08 ?  223 GLU C CA    1 
ATOM   12797 C  C     . GLU C 2 244 ? 135.049 58.069  118.281 1.00 24.70 ?  223 GLU C C     1 
ATOM   12798 O  O     . GLU C 2 244 ? 133.986 58.255  118.890 1.00 24.20 ?  223 GLU C O     1 
ATOM   12799 C  CB    . GLU C 2 244 ? 136.657 56.388  119.254 1.00 25.35 ?  223 GLU C CB    1 
ATOM   12800 C  CG    . GLU C 2 244 ? 136.070 56.563  120.665 1.00 26.67 ?  223 GLU C CG    1 
ATOM   12801 C  CD    . GLU C 2 244 ? 137.127 56.585  121.754 1.00 28.29 ?  223 GLU C CD    1 
ATOM   12802 O  OE1   . GLU C 2 244 ? 138.229 56.042  121.545 1.00 29.51 ?  223 GLU C OE1   1 
ATOM   12803 O  OE2   . GLU C 2 244 ? 136.852 57.152  122.827 1.00 29.09 -1 223 GLU C OE2   1 
ATOM   12804 N  N     . LEU C 2 245 ? 135.744 59.059  117.728 1.00 24.27 ?  224 LEU C N     1 
ATOM   12805 C  CA    . LEU C 2 245 ? 135.268 60.442  117.787 1.00 24.54 ?  224 LEU C CA    1 
ATOM   12806 C  C     . LEU C 2 245 ? 133.965 60.657  117.002 1.00 24.42 ?  224 LEU C C     1 
ATOM   12807 O  O     . LEU C 2 245 ? 133.090 61.405  117.444 1.00 24.10 ?  224 LEU C O     1 
ATOM   12808 C  CB    . LEU C 2 245 ? 136.372 61.424  117.350 1.00 23.86 ?  224 LEU C CB    1 
ATOM   12809 C  CG    . LEU C 2 245 ? 137.584 61.517  118.288 1.00 24.78 ?  224 LEU C CG    1 
ATOM   12810 C  CD1   . LEU C 2 245 ? 138.586 62.563  117.785 1.00 25.54 ?  224 LEU C CD1   1 
ATOM   12811 C  CD2   . LEU C 2 245 ? 137.179 61.822  119.737 1.00 25.29 ?  224 LEU C CD2   1 
ATOM   12812 N  N     . ARG C 2 246 ? 133.840 59.989  115.856 1.00 25.26 ?  225 ARG C N     1 
ATOM   12813 C  CA    . ARG C 2 246 ? 132.592 59.999  115.079 1.00 25.97 ?  225 ARG C CA    1 
ATOM   12814 C  C     . ARG C 2 246 ? 131.468 59.360  115.883 1.00 25.85 ?  225 ARG C C     1 
ATOM   12815 O  O     . ARG C 2 246 ? 130.349 59.877  115.901 1.00 25.01 ?  225 ARG C O     1 
ATOM   12816 C  CB    . ARG C 2 246 ? 132.756 59.291  113.717 1.00 26.65 ?  225 ARG C CB    1 
ATOM   12817 C  CG    . ARG C 2 246 ? 133.695 60.014  112.754 1.00 28.90 ?  225 ARG C CG    1 
ATOM   12818 C  CD    . ARG C 2 246 ? 133.559 59.537  111.288 1.00 31.26 ?  225 ARG C CD    1 
ATOM   12819 N  NE    . ARG C 2 246 ? 133.835 58.108  111.123 1.00 34.01 ?  225 ARG C NE    1 
ATOM   12820 C  CZ    . ARG C 2 246 ? 135.050 57.559  111.115 1.00 35.64 ?  225 ARG C CZ    1 
ATOM   12821 N  NH1   . ARG C 2 246 ? 136.135 58.308  111.268 1.00 36.11 1  225 ARG C NH1   1 
ATOM   12822 N  NH2   . ARG C 2 246 ? 135.180 56.247  110.955 1.00 37.05 ?  225 ARG C NH2   1 
ATOM   12823 N  N     . GLU C 2 247 ? 131.770 58.246  116.556 1.00 26.01 ?  226 GLU C N     1 
ATOM   12824 C  CA    . GLU C 2 247 ? 130.804 57.598  117.450 1.00 26.48 ?  226 GLU C CA    1 
ATOM   12825 C  C     . GLU C 2 247 ? 130.348 58.557  118.549 1.00 25.72 ?  226 GLU C C     1 
ATOM   12826 O  O     . GLU C 2 247 ? 129.143 58.685  118.810 1.00 25.16 ?  226 GLU C O     1 
ATOM   12827 C  CB    . GLU C 2 247 ? 131.384 56.335  118.092 1.00 27.18 ?  226 GLU C CB    1 
ATOM   12828 C  CG    . GLU C 2 247 ? 130.314 55.419  118.673 1.00 30.38 ?  226 GLU C CG    1 
ATOM   12829 C  CD    . GLU C 2 247 ? 130.719 54.720  119.957 1.00 35.77 ?  226 GLU C CD    1 
ATOM   12830 O  OE1   . GLU C 2 247 ? 131.920 54.458  120.176 1.00 38.02 ?  226 GLU C OE1   1 
ATOM   12831 O  OE2   . GLU C 2 247 ? 129.811 54.421  120.763 1.00 40.39 -1 226 GLU C OE2   1 
ATOM   12832 N  N     . PHE C 2 248 ? 131.311 59.228  119.185 1.00 24.71 ?  227 PHE C N     1 
ATOM   12833 C  CA    . PHE C 2 248 ? 130.994 60.220  120.211 1.00 23.71 ?  227 PHE C CA    1 
ATOM   12834 C  C     . PHE C 2 248 ? 130.054 61.289  119.649 1.00 23.14 ?  227 PHE C C     1 
ATOM   12835 O  O     . PHE C 2 248 ? 129.034 61.602  120.264 1.00 22.40 ?  227 PHE C O     1 
ATOM   12836 C  CB    . PHE C 2 248 ? 132.255 60.885  120.792 1.00 23.85 ?  227 PHE C CB    1 
ATOM   12837 C  CG    . PHE C 2 248 ? 131.955 62.134  121.582 1.00 23.64 ?  227 PHE C CG    1 
ATOM   12838 C  CD1   . PHE C 2 248 ? 131.549 62.044  122.915 1.00 23.07 ?  227 PHE C CD1   1 
ATOM   12839 C  CD2   . PHE C 2 248 ? 132.009 63.397  120.968 1.00 23.04 ?  227 PHE C CD2   1 
ATOM   12840 C  CE1   . PHE C 2 248 ? 131.242 63.190  123.649 1.00 22.73 ?  227 PHE C CE1   1 
ATOM   12841 C  CE2   . PHE C 2 248 ? 131.697 64.553  121.686 1.00 23.31 ?  227 PHE C CE2   1 
ATOM   12842 C  CZ    . PHE C 2 248 ? 131.314 64.453  123.034 1.00 21.51 ?  227 PHE C CZ    1 
ATOM   12843 N  N     . ALA C 2 249 ? 130.406 61.831  118.481 1.00 22.95 ?  228 ALA C N     1 
ATOM   12844 C  CA    . ALA C 2 249 ? 129.662 62.949  117.883 1.00 22.96 ?  228 ALA C CA    1 
ATOM   12845 C  C     . ALA C 2 249 ? 128.236 62.547  117.518 1.00 23.31 ?  228 ALA C C     1 
ATOM   12846 O  O     . ALA C 2 249 ? 127.287 63.293  117.768 1.00 22.63 ?  228 ALA C O     1 
ATOM   12847 C  CB    . ALA C 2 249 ? 130.397 63.490  116.659 1.00 22.40 ?  228 ALA C CB    1 
ATOM   12848 N  N     . ILE C 2 250 ? 128.100 61.365  116.927 1.00 23.66 ?  229 ILE C N     1 
ATOM   12849 C  CA    . ILE C 2 250 ? 126.794 60.850  116.511 1.00 25.00 ?  229 ILE C CA    1 
ATOM   12850 C  C     . ILE C 2 250 ? 125.932 60.432  117.711 1.00 24.64 ?  229 ILE C C     1 
ATOM   12851 O  O     . ILE C 2 250 ? 124.740 60.759  117.760 1.00 24.26 ?  229 ILE C O     1 
ATOM   12852 C  CB    . ILE C 2 250 ? 126.937 59.731  115.433 1.00 25.43 ?  229 ILE C CB    1 
ATOM   12853 C  CG1   . ILE C 2 250 ? 127.393 60.362  114.110 1.00 27.27 ?  229 ILE C CG1   1 
ATOM   12854 C  CG2   . ILE C 2 250 ? 125.580 59.013  115.194 1.00 27.62 ?  229 ILE C CG2   1 
ATOM   12855 C  CD1   . ILE C 2 250 ? 128.355 59.502  113.277 1.00 31.32 ?  229 ILE C CD1   1 
ATOM   12856 N  N     . ASP C 2 251 ? 126.530 59.748  118.686 1.00 24.78 ?  230 ASP C N     1 
ATOM   12857 C  CA    . ASP C 2 251 ? 125.814 59.419  119.933 1.00 25.20 ?  230 ASP C CA    1 
ATOM   12858 C  C     . ASP C 2 251 ? 125.325 60.672  120.659 1.00 24.08 ?  230 ASP C C     1 
ATOM   12859 O  O     . ASP C 2 251 ? 124.196 60.711  121.171 1.00 23.34 ?  230 ASP C O     1 
ATOM   12860 C  CB    . ASP C 2 251 ? 126.701 58.628  120.905 1.00 25.73 ?  230 ASP C CB    1 
ATOM   12861 C  CG    . ASP C 2 251 ? 126.876 57.182  120.502 1.00 28.78 ?  230 ASP C CG    1 
ATOM   12862 O  OD1   . ASP C 2 251 ? 126.235 56.729  119.526 1.00 29.99 ?  230 ASP C OD1   1 
ATOM   12863 O  OD2   . ASP C 2 251 ? 127.673 56.496  121.177 1.00 33.31 -1 230 ASP C OD2   1 
ATOM   12864 N  N     . LEU C 2 252 ? 126.183 61.688  120.717 1.00 22.98 ?  231 LEU C N     1 
ATOM   12865 C  CA    . LEU C 2 252 ? 125.816 62.938  121.384 1.00 21.63 ?  231 LEU C CA    1 
ATOM   12866 C  C     . LEU C 2 252 ? 124.692 63.635  120.625 1.00 21.66 ?  231 LEU C C     1 
ATOM   12867 O  O     . LEU C 2 252 ? 123.744 64.148  121.222 1.00 19.41 ?  231 LEU C O     1 
ATOM   12868 C  CB    . LEU C 2 252 ? 127.017 63.876  121.505 1.00 21.89 ?  231 LEU C CB    1 
ATOM   12869 C  CG    . LEU C 2 252 ? 126.765 65.270  122.107 1.00 21.33 ?  231 LEU C CG    1 
ATOM   12870 C  CD1   . LEU C 2 252 ? 126.171 65.184  123.529 1.00 20.89 ?  231 LEU C CD1   1 
ATOM   12871 C  CD2   . LEU C 2 252 ? 128.072 66.068  122.092 1.00 20.31 ?  231 LEU C CD2   1 
ATOM   12872 N  N     . LEU C 2 253 ? 124.811 63.656  119.300 1.00 22.28 ?  232 LEU C N     1 
ATOM   12873 C  CA    . LEU C 2 253 ? 123.791 64.299  118.479 1.00 23.05 ?  232 LEU C CA    1 
ATOM   12874 C  C     . LEU C 2 253 ? 122.434 63.634  118.681 1.00 23.36 ?  232 LEU C C     1 
ATOM   12875 O  O     . LEU C 2 253 ? 121.433 64.327  118.929 1.00 22.96 ?  232 LEU C O     1 
ATOM   12876 C  CB    . LEU C 2 253 ? 124.189 64.304  117.002 1.00 23.53 ?  232 LEU C CB    1 
ATOM   12877 C  CG    . LEU C 2 253 ? 123.161 64.977  116.084 1.00 25.63 ?  232 LEU C CG    1 
ATOM   12878 C  CD1   . LEU C 2 253 ? 123.014 66.466  116.394 1.00 25.88 ?  232 LEU C CD1   1 
ATOM   12879 C  CD2   . LEU C 2 253 ? 123.557 64.762  114.631 1.00 27.67 ?  232 LEU C CD2   1 
ATOM   12880 N  N     . ASN C 2 254 ? 122.406 62.300  118.594 1.00 23.55 ?  233 ASN C N     1 
ATOM   12881 C  CA    . ASN C 2 254 ? 121.168 61.535  118.830 1.00 24.61 ?  233 ASN C CA    1 
ATOM   12882 C  C     . ASN C 2 254 ? 120.559 61.764  120.215 1.00 23.57 ?  233 ASN C C     1 
ATOM   12883 O  O     . ASN C 2 254 ? 119.346 61.910  120.353 1.00 23.52 ?  233 ASN C O     1 
ATOM   12884 C  CB    . ASN C 2 254 ? 121.385 60.040  118.582 1.00 24.99 ?  233 ASN C CB    1 
ATOM   12885 C  CG    . ASN C 2 254 ? 121.236 59.661  117.114 1.00 28.92 ?  233 ASN C CG    1 
ATOM   12886 O  OD1   . ASN C 2 254 ? 120.197 59.897  116.495 1.00 33.75 ?  233 ASN C OD1   1 
ATOM   12887 N  ND2   . ASN C 2 254 ? 122.274 59.068  116.556 1.00 30.99 ?  233 ASN C ND2   1 
ATOM   12888 N  N     . GLN C 2 255 ? 121.404 61.799  121.242 1.00 23.22 ?  234 GLN C N     1 
ATOM   12889 C  CA    . GLN C 2 255 ? 120.925 62.055  122.593 1.00 22.54 ?  234 GLN C CA    1 
ATOM   12890 C  C     . GLN C 2 255 ? 120.309 63.464  122.721 1.00 22.00 ?  234 GLN C C     1 
ATOM   12891 O  O     . GLN C 2 255 ? 119.230 63.638  123.312 1.00 21.73 ?  234 GLN C O     1 
ATOM   12892 C  CB    . GLN C 2 255 ? 122.052 61.857  123.605 1.00 22.85 ?  234 GLN C CB    1 
ATOM   12893 C  CG    . GLN C 2 255 ? 121.567 61.804  125.039 1.00 23.87 ?  234 GLN C CG    1 
ATOM   12894 C  CD    . GLN C 2 255 ? 122.698 61.638  126.048 1.00 24.95 ?  234 GLN C CD    1 
ATOM   12895 O  OE1   . GLN C 2 255 ? 123.851 61.390  125.679 1.00 24.21 ?  234 GLN C OE1   1 
ATOM   12896 N  NE2   . GLN C 2 255 ? 122.372 61.803  127.331 1.00 25.97 ?  234 GLN C NE2   1 
ATOM   12897 N  N     . LEU C 2 256 ? 120.994 64.459  122.168 1.00 21.27 ?  235 LEU C N     1 
ATOM   12898 C  CA    . LEU C 2 256 ? 120.482 65.826  122.161 1.00 21.37 ?  235 LEU C CA    1 
ATOM   12899 C  C     . LEU C 2 256 ? 119.208 65.929  121.317 1.00 21.21 ?  235 LEU C C     1 
ATOM   12900 O  O     . LEU C 2 256 ? 118.261 66.621  121.686 1.00 20.75 ?  235 LEU C O     1 
ATOM   12901 C  CB    . LEU C 2 256 ? 121.550 66.784  121.615 1.00 20.93 ?  235 LEU C CB    1 
ATOM   12902 C  CG    . LEU C 2 256 ? 122.774 67.098  122.480 1.00 21.74 ?  235 LEU C CG    1 
ATOM   12903 C  CD1   . LEU C 2 256 ? 123.763 67.967  121.689 1.00 20.15 ?  235 LEU C CD1   1 
ATOM   12904 C  CD2   . LEU C 2 256 ? 122.392 67.776  123.795 1.00 20.90 ?  235 LEU C CD2   1 
ATOM   12905 N  N     . TYR C 2 257 ? 119.215 65.245  120.178 1.00 21.68 ?  236 TYR C N     1 
ATOM   12906 C  CA    . TYR C 2 257 ? 118.081 65.235  119.254 1.00 22.40 ?  236 TYR C CA    1 
ATOM   12907 C  C     . TYR C 2 257 ? 116.807 64.702  119.931 1.00 23.31 ?  236 TYR C C     1 
ATOM   12908 O  O     . TYR C 2 257 ? 115.749 65.360  119.882 1.00 22.99 ?  236 TYR C O     1 
ATOM   12909 C  CB    . TYR C 2 257 ? 118.430 64.427  118.001 1.00 22.81 ?  236 TYR C CB    1 
ATOM   12910 C  CG    . TYR C 2 257 ? 117.285 64.225  117.027 1.00 23.76 ?  236 TYR C CG    1 
ATOM   12911 C  CD1   . TYR C 2 257 ? 116.740 65.303  116.324 1.00 24.05 ?  236 TYR C CD1   1 
ATOM   12912 C  CD2   . TYR C 2 257 ? 116.739 62.960  116.823 1.00 24.04 ?  236 TYR C CD2   1 
ATOM   12913 C  CE1   . TYR C 2 257 ? 115.681 65.125  115.440 1.00 24.40 ?  236 TYR C CE1   1 
ATOM   12914 C  CE2   . TYR C 2 257 ? 115.681 62.772  115.936 1.00 26.30 ?  236 TYR C CE2   1 
ATOM   12915 C  CZ    . TYR C 2 257 ? 115.169 63.858  115.249 1.00 25.80 ?  236 TYR C CZ    1 
ATOM   12916 O  OH    . TYR C 2 257 ? 114.138 63.668  114.374 1.00 28.42 ?  236 TYR C OH    1 
ATOM   12917 N  N     . GLU C 2 258 ? 116.920 63.547  120.595 1.00 22.99 ?  237 GLU C N     1 
ATOM   12918 C  CA    . GLU C 2 258 ? 115.773 62.928  121.269 1.00 24.46 ?  237 GLU C CA    1 
ATOM   12919 C  C     . GLU C 2 258 ? 115.189 63.835  122.340 1.00 23.86 ?  237 GLU C C     1 
ATOM   12920 O  O     . GLU C 2 258 ? 113.971 63.950  122.463 1.00 24.01 ?  237 GLU C O     1 
ATOM   12921 C  CB    . GLU C 2 258 ? 116.129 61.545  121.843 1.00 25.21 ?  237 GLU C CB    1 
ATOM   12922 C  CG    . GLU C 2 258 ? 116.384 60.471  120.760 1.00 30.12 ?  237 GLU C CG    1 
ATOM   12923 C  CD    . GLU C 2 258 ? 115.133 60.130  119.946 1.00 35.29 ?  237 GLU C CD    1 
ATOM   12924 O  OE1   . GLU C 2 258 ? 114.005 60.242  120.479 1.00 37.71 ?  237 GLU C OE1   1 
ATOM   12925 O  OE2   . GLU C 2 258 ? 115.278 59.740  118.764 1.00 39.07 -1 237 GLU C OE2   1 
ATOM   12926 N  N     . ASN C 2 259 ? 116.062 64.502  123.094 1.00 23.25 ?  238 ASN C N     1 
ATOM   12927 C  CA    . ASN C 2 259 ? 115.625 65.491  124.076 1.00 23.10 ?  238 ASN C CA    1 
ATOM   12928 C  C     . ASN C 2 259 ? 114.958 66.706  123.403 1.00 22.68 ?  238 ASN C C     1 
ATOM   12929 O  O     . ASN C 2 259 ? 113.936 67.210  123.877 1.00 22.73 ?  238 ASN C O     1 
ATOM   12930 C  CB    . ASN C 2 259 ? 116.808 65.917  124.948 1.00 23.22 ?  238 ASN C CB    1 
ATOM   12931 C  CG    . ASN C 2 259 ? 116.414 66.915  126.017 1.00 24.46 ?  238 ASN C CG    1 
ATOM   12932 O  OD1   . ASN C 2 259 ? 115.716 66.577  126.978 1.00 26.28 ?  238 ASN C OD1   1 
ATOM   12933 N  ND2   . ASN C 2 259 ? 116.861 68.156  125.857 1.00 24.93 ?  238 ASN C ND2   1 
ATOM   12934 N  N     . GLU C 2 260 ? 115.522 67.155  122.284 1.00 22.64 ?  239 GLU C N     1 
ATOM   12935 C  CA    . GLU C 2 260 ? 114.988 68.320  121.576 1.00 23.18 ?  239 GLU C CA    1 
ATOM   12936 C  C     . GLU C 2 260 ? 113.590 68.048  120.996 1.00 23.40 ?  239 GLU C C     1 
ATOM   12937 O  O     . GLU C 2 260 ? 112.738 68.949  120.955 1.00 23.57 ?  239 GLU C O     1 
ATOM   12938 C  CB    . GLU C 2 260 ? 115.957 68.791  120.482 1.00 23.19 ?  239 GLU C CB    1 
ATOM   12939 C  CG    . GLU C 2 260 ? 115.852 70.300  120.155 1.00 24.33 ?  239 GLU C CG    1 
ATOM   12940 C  CD    . GLU C 2 260 ? 116.254 71.213  121.327 1.00 27.99 ?  239 GLU C CD    1 
ATOM   12941 O  OE1   . GLU C 2 260 ? 116.757 70.722  122.362 1.00 27.36 ?  239 GLU C OE1   1 
ATOM   12942 O  OE2   . GLU C 2 260 ? 116.056 72.443  121.217 1.00 28.98 -1 239 GLU C OE2   1 
ATOM   12943 N  N     . LEU C 2 261 ? 113.356 66.808  120.563 1.00 23.35 ?  240 LEU C N     1 
ATOM   12944 C  CA    . LEU C 2 261 ? 112.021 66.389  120.107 1.00 23.74 ?  240 LEU C CA    1 
ATOM   12945 C  C     . LEU C 2 261 ? 110.951 66.599  121.182 1.00 23.80 ?  240 LEU C C     1 
ATOM   12946 O  O     . LEU C 2 261 ? 109.881 67.168  120.913 1.00 23.33 ?  240 LEU C O     1 
ATOM   12947 C  CB    . LEU C 2 261 ? 112.025 64.925  119.661 1.00 24.09 ?  240 LEU C CB    1 
ATOM   12948 C  CG    . LEU C 2 261 ? 112.779 64.588  118.374 1.00 24.07 ?  240 LEU C CG    1 
ATOM   12949 C  CD1   . LEU C 2 261 ? 112.689 63.093  118.101 1.00 24.77 ?  240 LEU C CD1   1 
ATOM   12950 C  CD2   . LEU C 2 261 ? 112.236 65.402  117.182 1.00 24.38 ?  240 LEU C CD2   1 
ATOM   12951 N  N     . GLU C 2 262 ? 111.242 66.130  122.390 1.00 23.41 ?  241 GLU C N     1 
ATOM   12952 C  CA    . GLU C 2 262 ? 110.329 66.292  123.520 1.00 24.02 ?  241 GLU C CA    1 
ATOM   12953 C  C     . GLU C 2 262 ? 110.121 67.770  123.886 1.00 22.91 ?  241 GLU C C     1 
ATOM   12954 O  O     . GLU C 2 262 ? 109.003 68.184  124.165 1.00 22.94 ?  241 GLU C O     1 
ATOM   12955 C  CB    . GLU C 2 262 ? 110.852 65.511  124.727 1.00 24.92 ?  241 GLU C CB    1 
ATOM   12956 C  CG    . GLU C 2 262 ? 110.866 64.002  124.538 1.00 27.82 ?  241 GLU C CG    1 
ATOM   12957 C  CD    . GLU C 2 262 ? 111.363 63.271  125.772 1.00 33.08 ?  241 GLU C CD    1 
ATOM   12958 O  OE1   . GLU C 2 262 ? 112.596 63.176  125.972 1.00 36.94 ?  241 GLU C OE1   1 
ATOM   12959 O  OE2   . GLU C 2 262 ? 110.518 62.782  126.543 1.00 37.48 -1 241 GLU C OE2   1 
ATOM   12960 N  N     . TYR C 2 263 ? 111.207 68.546  123.891 1.00 21.84 ?  242 TYR C N     1 
ATOM   12961 C  CA    . TYR C 2 263 ? 111.163 69.991  124.105 1.00 21.66 ?  242 TYR C CA    1 
ATOM   12962 C  C     . TYR C 2 263 ? 110.299 70.672  123.051 1.00 21.28 ?  242 TYR C C     1 
ATOM   12963 O  O     . TYR C 2 263 ? 109.471 71.535  123.374 1.00 21.14 ?  242 TYR C O     1 
ATOM   12964 C  CB    . TYR C 2 263 ? 112.585 70.570  124.032 1.00 21.44 ?  242 TYR C CB    1 
ATOM   12965 C  CG    . TYR C 2 263 ? 112.712 72.070  124.260 1.00 21.89 ?  242 TYR C CG    1 
ATOM   12966 C  CD1   . TYR C 2 263 ? 112.501 72.626  125.523 1.00 22.52 ?  242 TYR C CD1   1 
ATOM   12967 C  CD2   . TYR C 2 263 ? 113.082 72.926  123.219 1.00 22.58 ?  242 TYR C CD2   1 
ATOM   12968 C  CE1   . TYR C 2 263 ? 112.640 73.997  125.739 1.00 22.67 ?  242 TYR C CE1   1 
ATOM   12969 C  CE2   . TYR C 2 263 ? 113.229 74.302  123.425 1.00 24.03 ?  242 TYR C CE2   1 
ATOM   12970 C  CZ    . TYR C 2 263 ? 113.014 74.825  124.696 1.00 23.75 ?  242 TYR C CZ    1 
ATOM   12971 O  OH    . TYR C 2 263 ? 113.148 76.181  124.922 1.00 26.82 ?  242 TYR C OH    1 
ATOM   12972 N  N     . THR C 2 264 ? 110.499 70.283  121.794 1.00 20.66 ?  243 THR C N     1 
ATOM   12973 C  CA    . THR C 2 264 ? 109.756 70.870  120.669 1.00 20.99 ?  243 THR C CA    1 
ATOM   12974 C  C     . THR C 2 264 ? 108.254 70.595  120.802 1.00 21.22 ?  243 THR C C     1 
ATOM   12975 O  O     . THR C 2 264 ? 107.433 71.513  120.654 1.00 20.95 ?  243 THR C O     1 
ATOM   12976 C  CB    . THR C 2 264 ? 110.296 70.353  119.307 1.00 20.58 ?  243 THR C CB    1 
ATOM   12977 O  OG1   . THR C 2 264 ? 111.637 70.818  119.130 1.00 20.84 ?  243 THR C OG1   1 
ATOM   12978 C  CG2   . THR C 2 264 ? 109.442 70.854  118.140 1.00 20.90 ?  243 THR C CG2   1 
ATOM   12979 N  N     . GLU C 2 265 ? 107.900 69.346  121.110 1.00 21.62 ?  244 GLU C N     1 
ATOM   12980 C  CA    . GLU C 2 265 ? 106.493 68.987  121.293 1.00 23.46 ?  244 GLU C CA    1 
ATOM   12981 C  C     . GLU C 2 265 ? 105.873 69.751  122.446 1.00 23.33 ?  244 GLU C C     1 
ATOM   12982 O  O     . GLU C 2 265 ? 104.754 70.256  122.348 1.00 22.86 ?  244 GLU C O     1 
ATOM   12983 C  CB    . GLU C 2 265 ? 106.317 67.483  121.507 1.00 24.31 ?  244 GLU C CB    1 
ATOM   12984 C  CG    . GLU C 2 265 ? 106.553 66.657  120.247 1.00 27.63 ?  244 GLU C CG    1 
ATOM   12985 C  CD    . GLU C 2 265 ? 106.362 65.162  120.483 1.00 33.27 ?  244 GLU C CD    1 
ATOM   12986 O  OE1   . GLU C 2 265 ? 105.551 64.786  121.359 1.00 35.56 ?  244 GLU C OE1   1 
ATOM   12987 O  OE2   . GLU C 2 265 ? 107.020 64.360  119.781 1.00 35.96 -1 244 GLU C OE2   1 
ATOM   12988 N  N     . ASP C 2 266 ? 106.616 69.840  123.540 1.00 23.36 ?  245 ASP C N     1 
ATOM   12989 C  CA    . ASP C 2 266 ? 106.157 70.561  124.716 1.00 24.18 ?  245 ASP C CA    1 
ATOM   12990 C  C     . ASP C 2 266 ? 105.823 72.032  124.407 1.00 23.96 ?  245 ASP C C     1 
ATOM   12991 O  O     . ASP C 2 266 ? 104.826 72.562  124.892 1.00 24.19 ?  245 ASP C O     1 
ATOM   12992 C  CB    . ASP C 2 266 ? 107.224 70.475  125.805 1.00 25.14 ?  245 ASP C CB    1 
ATOM   12993 C  CG    . ASP C 2 266 ? 106.732 70.975  127.128 1.00 27.35 ?  245 ASP C CG    1 
ATOM   12994 O  OD1   . ASP C 2 266 ? 105.703 70.458  127.613 1.00 28.45 ?  245 ASP C OD1   1 
ATOM   12995 O  OD2   . ASP C 2 266 ? 107.378 71.892  127.679 1.00 31.99 -1 245 ASP C OD2   1 
ATOM   12996 N  N     . LEU C 2 267 ? 106.644 72.678  123.587 1.00 23.34 ?  246 LEU C N     1 
ATOM   12997 C  CA    . LEU C 2 267 ? 106.433 74.091  123.254 1.00 23.53 ?  246 LEU C CA    1 
ATOM   12998 C  C     . LEU C 2 267 ? 105.450 74.336  122.119 1.00 22.94 ?  246 LEU C C     1 
ATOM   12999 O  O     . LEU C 2 267 ? 104.640 75.262  122.188 1.00 23.14 ?  246 LEU C O     1 
ATOM   13000 C  CB    . LEU C 2 267 ? 107.763 74.753  122.904 1.00 23.37 ?  246 LEU C CB    1 
ATOM   13001 C  CG    . LEU C 2 267 ? 108.745 75.005  124.049 1.00 26.17 ?  246 LEU C CG    1 
ATOM   13002 C  CD1   . LEU C 2 267 ? 109.973 75.684  123.485 1.00 27.31 ?  246 LEU C CD1   1 
ATOM   13003 C  CD2   . LEU C 2 267 ? 108.111 75.879  125.126 1.00 28.08 ?  246 LEU C CD2   1 
ATOM   13004 N  N     . TYR C 2 268 ? 105.542 73.524  121.070 1.00 22.46 ?  247 TYR C N     1 
ATOM   13005 C  CA    . TYR C 2 268 ? 104.825 73.809  119.830 1.00 22.00 ?  247 TYR C CA    1 
ATOM   13006 C  C     . TYR C 2 268 ? 103.483 73.131  119.615 1.00 22.26 ?  247 TYR C C     1 
ATOM   13007 O  O     . TYR C 2 268 ? 102.736 73.562  118.735 1.00 22.17 ?  247 TYR C O     1 
ATOM   13008 C  CB    . TYR C 2 268 ? 105.729 73.550  118.617 1.00 21.73 ?  247 TYR C CB    1 
ATOM   13009 C  CG    . TYR C 2 268 ? 106.832 74.568  118.461 1.00 21.49 ?  247 TYR C CG    1 
ATOM   13010 C  CD1   . TYR C 2 268 ? 108.135 74.281  118.880 1.00 19.45 ?  247 TYR C CD1   1 
ATOM   13011 C  CD2   . TYR C 2 268 ? 106.571 75.827  117.909 1.00 22.71 ?  247 TYR C CD2   1 
ATOM   13012 C  CE1   . TYR C 2 268 ? 109.157 75.226  118.746 1.00 20.30 ?  247 TYR C CE1   1 
ATOM   13013 C  CE2   . TYR C 2 268 ? 107.588 76.785  117.763 1.00 21.69 ?  247 TYR C CE2   1 
ATOM   13014 C  CZ    . TYR C 2 268 ? 108.874 76.467  118.171 1.00 21.40 ?  247 TYR C CZ    1 
ATOM   13015 O  OH    . TYR C 2 268 ? 109.869 77.399  118.022 1.00 22.11 ?  247 TYR C OH    1 
ATOM   13016 N  N     . ASP C 2 269 ? 103.170 72.073  120.370 1.00 22.40 ?  248 ASP C N     1 
ATOM   13017 C  CA    . ASP C 2 269 ? 101.863 71.412  120.210 1.00 22.75 ?  248 ASP C CA    1 
ATOM   13018 C  C     . ASP C 2 269 ? 100.702 72.393  120.379 1.00 22.55 ?  248 ASP C C     1 
ATOM   13019 O  O     . ASP C 2 269 ? 99.707  72.309  119.648 1.00 22.22 ?  248 ASP C O     1 
ATOM   13020 C  CB    . ASP C 2 269 ? 101.690 70.203  121.150 1.00 23.03 ?  248 ASP C CB    1 
ATOM   13021 C  CG    . ASP C 2 269 ? 102.368 68.947  120.629 1.00 25.02 ?  248 ASP C CG    1 
ATOM   13022 O  OD1   . ASP C 2 269 ? 102.807 68.916  119.460 1.00 26.85 ?  248 ASP C OD1   1 
ATOM   13023 O  OD2   . ASP C 2 269 ? 102.456 67.968  121.399 1.00 28.74 -1 248 ASP C OD2   1 
ATOM   13024 N  N     . GLN C 2 270 ? 100.833 73.326  121.326 1.00 22.21 ?  249 GLN C N     1 
ATOM   13025 C  CA    . GLN C 2 270 ? 99.756  74.310  121.579 1.00 22.39 ?  249 GLN C CA    1 
ATOM   13026 C  C     . GLN C 2 270 ? 99.558  75.340  120.458 1.00 21.65 ?  249 GLN C C     1 
ATOM   13027 O  O     . GLN C 2 270 ? 98.553  76.051  120.448 1.00 21.70 ?  249 GLN C O     1 
ATOM   13028 C  CB    . GLN C 2 270 ? 99.927  75.012  122.936 1.00 22.53 ?  249 GLN C CB    1 
ATOM   13029 C  CG    . GLN C 2 270 ? 101.221 75.849  123.107 1.00 22.73 ?  249 GLN C CG    1 
ATOM   13030 C  CD    . GLN C 2 270 ? 101.292 76.498  124.474 1.00 25.39 ?  249 GLN C CD    1 
ATOM   13031 O  OE1   . GLN C 2 270 ? 100.568 76.109  125.392 1.00 27.88 ?  249 GLN C OE1   1 
ATOM   13032 N  NE2   . GLN C 2 270 ? 102.157 77.498  124.620 1.00 24.88 ?  249 GLN C NE2   1 
ATOM   13033 N  N     . VAL C 2 271 ? 100.512 75.419  119.529 1.00 20.91 ?  250 VAL C N     1 
ATOM   13034 C  CA    . VAL C 2 271 ? 100.400 76.321  118.360 1.00 20.62 ?  250 VAL C CA    1 
ATOM   13035 C  C     . VAL C 2 271 ? 100.356 75.543  117.032 1.00 20.53 ?  250 VAL C C     1 
ATOM   13036 O  O     . VAL C 2 271 ? 100.291 76.139  115.945 1.00 20.05 ?  250 VAL C O     1 
ATOM   13037 C  CB    . VAL C 2 271 ? 101.498 77.450  118.342 1.00 20.32 ?  250 VAL C CB    1 
ATOM   13038 C  CG1   . VAL C 2 271 ? 101.331 78.389  119.532 1.00 20.35 ?  250 VAL C CG1   1 
ATOM   13039 C  CG2   . VAL C 2 271 ? 102.922 76.876  118.324 1.00 19.32 ?  250 VAL C CG2   1 
ATOM   13040 N  N     . GLY C 2 272 ? 100.379 74.212  117.138 1.00 20.29 ?  251 GLY C N     1 
ATOM   13041 C  CA    . GLY C 2 272 ? 100.157 73.324  115.994 1.00 20.51 ?  251 GLY C CA    1 
ATOM   13042 C  C     . GLY C 2 272 ? 101.335 73.135  115.051 1.00 20.99 ?  251 GLY C C     1 
ATOM   13043 O  O     . GLY C 2 272 ? 101.146 72.745  113.887 1.00 20.22 ?  251 GLY C O     1 
ATOM   13044 N  N     . LEU C 2 273 ? 102.549 73.407  115.538 1.00 20.76 ?  252 LEU C N     1 
ATOM   13045 C  CA    . LEU C 2 273 ? 103.709 73.486  114.644 1.00 21.38 ?  252 LEU C CA    1 
ATOM   13046 C  C     . LEU C 2 273 ? 104.817 72.464  114.884 1.00 21.86 ?  252 LEU C C     1 
ATOM   13047 O  O     . LEU C 2 273 ? 105.863 72.530  114.240 1.00 22.45 ?  252 LEU C O     1 
ATOM   13048 C  CB    . LEU C 2 273 ? 104.291 74.910  114.635 1.00 21.44 ?  252 LEU C CB    1 
ATOM   13049 C  CG    . LEU C 2 273 ? 103.385 76.073  114.224 1.00 22.02 ?  252 LEU C CG    1 
ATOM   13050 C  CD1   . LEU C 2 273 ? 104.148 77.386  114.363 1.00 22.86 ?  252 LEU C CD1   1 
ATOM   13051 C  CD2   . LEU C 2 273 ? 102.853 75.888  112.787 1.00 23.88 ?  252 LEU C CD2   1 
ATOM   13052 N  N     . SER C 2 274 ? 104.591 71.508  115.784 1.00 22.19 ?  253 SER C N     1 
ATOM   13053 C  CA    . SER C 2 274 ? 105.668 70.635  116.243 1.00 22.47 ?  253 SER C CA    1 
ATOM   13054 C  C     . SER C 2 274 ? 106.349 69.863  115.111 1.00 22.94 ?  253 SER C C     1 
ATOM   13055 O  O     . SER C 2 274 ? 107.572 69.801  115.051 1.00 22.07 ?  253 SER C O     1 
ATOM   13056 C  CB    . SER C 2 274 ? 105.156 69.669  117.315 1.00 22.91 ?  253 SER C CB    1 
ATOM   13057 O  OG    . SER C 2 274 ? 104.837 70.387  118.489 1.00 24.25 ?  253 SER C OG    1 
ATOM   13058 N  N     . HIS C 2 275 ? 105.550 69.311  114.201 1.00 24.59 ?  254 HIS C N     1 
ATOM   13059 C  CA    . HIS C 2 275 ? 106.084 68.525  113.083 1.00 25.66 ?  254 HIS C CA    1 
ATOM   13060 C  C     . HIS C 2 275 ? 106.961 69.375  112.149 1.00 26.01 ?  254 HIS C C     1 
ATOM   13061 O  O     . HIS C 2 275 ? 108.016 68.922  111.672 1.00 26.23 ?  254 HIS C O     1 
ATOM   13062 C  CB    . HIS C 2 275 ? 104.939 67.868  112.301 1.00 26.89 ?  254 HIS C CB    1 
ATOM   13063 C  CG    . HIS C 2 275 ? 105.400 66.965  111.200 1.00 29.10 ?  254 HIS C CG    1 
ATOM   13064 N  ND1   . HIS C 2 275 ? 106.283 65.925  111.410 1.00 32.70 ?  254 HIS C ND1   1 
ATOM   13065 C  CD2   . HIS C 2 275 ? 105.100 66.941  109.881 1.00 31.68 ?  254 HIS C CD2   1 
ATOM   13066 C  CE1   . HIS C 2 275 ? 106.509 65.304  110.266 1.00 33.55 ?  254 HIS C CE1   1 
ATOM   13067 N  NE2   . HIS C 2 275 ? 105.792 65.890  109.326 1.00 33.71 ?  254 HIS C NE2   1 
ATOM   13068 N  N     . ASP C 2 276 ? 106.516 70.601  111.896 1.00 25.93 ?  255 ASP C N     1 
ATOM   13069 C  CA    . ASP C 2 276 ? 107.258 71.551  111.073 1.00 26.65 ?  255 ASP C CA    1 
ATOM   13070 C  C     . ASP C 2 276 ? 108.608 71.920  111.691 1.00 25.61 ?  255 ASP C C     1 
ATOM   13071 O  O     . ASP C 2 276 ? 109.631 71.926  110.992 1.00 25.34 ?  255 ASP C O     1 
ATOM   13072 C  CB    . ASP C 2 276 ? 106.427 72.811  110.827 1.00 27.44 ?  255 ASP C CB    1 
ATOM   13073 C  CG    . ASP C 2 276 ? 106.022 72.961  109.377 1.00 32.09 ?  255 ASP C CG    1 
ATOM   13074 O  OD1   . ASP C 2 276 ? 106.889 72.750  108.494 1.00 36.67 ?  255 ASP C OD1   1 
ATOM   13075 O  OD2   . ASP C 2 276 ? 104.838 73.277  109.115 1.00 36.30 -1 255 ASP C OD2   1 
ATOM   13076 N  N     . VAL C 2 277 ? 108.599 72.224  112.993 1.00 24.17 ?  256 VAL C N     1 
ATOM   13077 C  CA    . VAL C 2 277 ? 109.827 72.556  113.727 1.00 23.71 ?  256 VAL C CA    1 
ATOM   13078 C  C     . VAL C 2 277 ? 110.803 71.377  113.718 1.00 23.48 ?  256 VAL C C     1 
ATOM   13079 O  O     . VAL C 2 277 ? 112.007 71.567  113.543 1.00 23.08 ?  256 VAL C O     1 
ATOM   13080 C  CB    . VAL C 2 277 ? 109.546 72.984  115.195 1.00 23.27 ?  256 VAL C CB    1 
ATOM   13081 C  CG1   . VAL C 2 277 ? 110.849 73.325  115.925 1.00 24.02 ?  256 VAL C CG1   1 
ATOM   13082 C  CG2   . VAL C 2 277 ? 108.592 74.170  115.246 1.00 23.35 ?  256 VAL C CG2   1 
ATOM   13083 N  N     . LYS C 2 278 ? 110.283 70.167  113.906 1.00 23.36 ?  257 LYS C N     1 
ATOM   13084 C  CA    . LYS C 2 278 ? 111.105 68.958  113.868 1.00 24.12 ?  257 LYS C CA    1 
ATOM   13085 C  C     . LYS C 2 278 ? 111.872 68.807  112.555 1.00 24.30 ?  257 LYS C C     1 
ATOM   13086 O  O     . LYS C 2 278 ? 113.052 68.428  112.555 1.00 24.37 ?  257 LYS C O     1 
ATOM   13087 C  CB    . LYS C 2 278 ? 110.264 67.710  114.134 1.00 24.22 ?  257 LYS C CB    1 
ATOM   13088 C  CG    . LYS C 2 278 ? 109.848 67.545  115.586 1.00 24.96 ?  257 LYS C CG    1 
ATOM   13089 C  CD    . LYS C 2 278 ? 108.898 66.361  115.712 1.00 26.34 ?  257 LYS C CD    1 
ATOM   13090 C  CE    . LYS C 2 278 ? 108.424 66.181  117.128 1.00 27.16 ?  257 LYS C CE    1 
ATOM   13091 N  NZ    . LYS C 2 278 ? 107.507 65.003  117.184 1.00 29.60 1  257 LYS C NZ    1 
ATOM   13092 N  N     . LYS C 2 279 ? 111.209 69.108  111.440 1.00 24.55 ?  258 LYS C N     1 
ATOM   13093 C  CA    . LYS C 2 279 ? 111.875 69.086  110.141 1.00 24.85 ?  258 LYS C CA    1 
ATOM   13094 C  C     . LYS C 2 279 ? 113.006 70.112  110.104 1.00 24.57 ?  258 LYS C C     1 
ATOM   13095 O  O     . LYS C 2 279 ? 114.082 69.831  109.578 1.00 24.07 ?  258 LYS C O     1 
ATOM   13096 C  CB    . LYS C 2 279 ? 110.878 69.364  109.016 1.00 25.30 ?  258 LYS C CB    1 
ATOM   13097 C  CG    . LYS C 2 279 ? 109.768 68.344  108.910 1.00 26.63 ?  258 LYS C CG    1 
ATOM   13098 C  CD    . LYS C 2 279 ? 108.836 68.722  107.765 1.00 29.30 ?  258 LYS C CD    1 
ATOM   13099 C  CE    . LYS C 2 279 ? 107.815 67.649  107.533 1.00 31.79 ?  258 LYS C CE    1 
ATOM   13100 N  NZ    . LYS C 2 279 ? 106.730 68.182  106.672 1.00 33.80 1  258 LYS C NZ    1 
ATOM   13101 N  N     . PHE C 2 280 ? 112.759 71.283  110.693 1.00 24.29 ?  259 PHE C N     1 
ATOM   13102 C  CA    . PHE C 2 280 ? 113.740 72.377  110.731 1.00 24.90 ?  259 PHE C CA    1 
ATOM   13103 C  C     . PHE C 2 280 ? 114.989 72.013  111.553 1.00 24.86 ?  259 PHE C C     1 
ATOM   13104 O  O     . PHE C 2 280 ? 116.119 72.289  111.136 1.00 24.68 ?  259 PHE C O     1 
ATOM   13105 C  CB    . PHE C 2 280 ? 113.062 73.649  111.259 1.00 24.70 ?  259 PHE C CB    1 
ATOM   13106 C  CG    . PHE C 2 280 ? 113.887 74.908  111.128 1.00 25.70 ?  259 PHE C CG    1 
ATOM   13107 C  CD1   . PHE C 2 280 ? 114.334 75.349  109.882 1.00 26.86 ?  259 PHE C CD1   1 
ATOM   13108 C  CD2   . PHE C 2 280 ? 114.178 75.682  112.259 1.00 26.19 ?  259 PHE C CD2   1 
ATOM   13109 C  CE1   . PHE C 2 280 ? 115.078 76.531  109.760 1.00 26.66 ?  259 PHE C CE1   1 
ATOM   13110 C  CE2   . PHE C 2 280 ? 114.913 76.867  112.146 1.00 26.52 ?  259 PHE C CE2   1 
ATOM   13111 C  CZ    . PHE C 2 280 ? 115.369 77.289  110.890 1.00 26.23 ?  259 PHE C CZ    1 
ATOM   13112 N  N     . ILE C 2 281 ? 114.785 71.387  112.713 1.00 25.53 ?  260 ILE C N     1 
ATOM   13113 C  CA    . ILE C 2 281 ? 115.915 71.007  113.563 1.00 26.21 ?  260 ILE C CA    1 
ATOM   13114 C  C     . ILE C 2 281 ? 116.762 69.891  112.934 1.00 26.47 ?  260 ILE C C     1 
ATOM   13115 O  O     . ILE C 2 281 ? 117.978 69.880  113.096 1.00 26.52 ?  260 ILE C O     1 
ATOM   13116 C  CB    . ILE C 2 281 ? 115.513 70.703  115.048 1.00 26.27 ?  260 ILE C CB    1 
ATOM   13117 C  CG1   . ILE C 2 281 ? 114.888 69.315  115.201 1.00 27.37 ?  260 ILE C CG1   1 
ATOM   13118 C  CG2   . ILE C 2 281 ? 114.608 71.825  115.604 1.00 26.92 ?  260 ILE C CG2   1 
ATOM   13119 C  CD1   . ILE C 2 281 ? 114.540 68.936  116.642 1.00 29.51 ?  260 ILE C CD1   1 
ATOM   13120 N  N     . ARG C 2 282 ? 116.124 68.989  112.186 1.00 26.57 ?  261 ARG C N     1 
ATOM   13121 C  CA    . ARG C 2 282 ? 116.856 67.948  111.458 1.00 26.84 ?  261 ARG C CA    1 
ATOM   13122 C  C     . ARG C 2 282 ? 117.718 68.559  110.355 1.00 27.34 ?  261 ARG C C     1 
ATOM   13123 O  O     . ARG C 2 282 ? 118.877 68.187  110.192 1.00 27.54 ?  261 ARG C O     1 
ATOM   13124 C  CB    . ARG C 2 282 ? 115.912 66.886  110.890 1.00 26.98 ?  261 ARG C CB    1 
ATOM   13125 C  CG    . ARG C 2 282 ? 115.436 65.864  111.905 1.00 26.53 ?  261 ARG C CG    1 
ATOM   13126 C  CD    . ARG C 2 282 ? 114.736 64.669  111.227 1.00 27.77 ?  261 ARG C CD    1 
ATOM   13127 N  NE    . ARG C 2 282 ? 113.441 65.023  110.653 1.00 28.67 ?  261 ARG C NE    1 
ATOM   13128 C  CZ    . ARG C 2 282 ? 112.290 65.041  111.329 1.00 29.68 ?  261 ARG C CZ    1 
ATOM   13129 N  NH1   . ARG C 2 282 ? 112.255 64.722  112.622 1.00 28.31 1  261 ARG C NH1   1 
ATOM   13130 N  NH2   . ARG C 2 282 ? 111.168 65.371  110.710 1.00 29.15 ?  261 ARG C NH2   1 
ATOM   13131 N  N     . TYR C 2 283 ? 117.140 69.505  109.617 1.00 27.78 ?  262 TYR C N     1 
ATOM   13132 C  CA    . TYR C 2 283 ? 117.857 70.292  108.616 1.00 28.18 ?  262 TYR C CA    1 
ATOM   13133 C  C     . TYR C 2 283 ? 119.126 70.928  109.212 1.00 27.08 ?  262 TYR C C     1 
ATOM   13134 O  O     . TYR C 2 283 ? 120.231 70.809  108.659 1.00 26.51 ?  262 TYR C O     1 
ATOM   13135 C  CB    . TYR C 2 283 ? 116.925 71.378  108.063 1.00 29.11 ?  262 TYR C CB    1 
ATOM   13136 C  CG    . TYR C 2 283 ? 117.535 72.258  107.000 1.00 32.56 ?  262 TYR C CG    1 
ATOM   13137 C  CD1   . TYR C 2 283 ? 117.708 71.788  105.697 1.00 36.59 ?  262 TYR C CD1   1 
ATOM   13138 C  CD2   . TYR C 2 283 ? 117.925 73.569  107.289 1.00 36.34 ?  262 TYR C CD2   1 
ATOM   13139 C  CE1   . TYR C 2 283 ? 118.267 72.597  104.702 1.00 39.47 ?  262 TYR C CE1   1 
ATOM   13140 C  CE2   . TYR C 2 283 ? 118.484 74.394  106.294 1.00 39.23 ?  262 TYR C CE2   1 
ATOM   13141 C  CZ    . TYR C 2 283 ? 118.651 73.894  105.006 1.00 40.48 ?  262 TYR C CZ    1 
ATOM   13142 O  OH    . TYR C 2 283 ? 119.199 74.681  104.019 1.00 44.00 ?  262 TYR C OH    1 
ATOM   13143 N  N     . ASN C 2 284 ? 118.965 71.579  110.356 1.00 26.08 ?  263 ASN C N     1 
ATOM   13144 C  CA    . ASN C 2 284 ? 120.088 72.229  111.013 1.00 25.73 ?  263 ASN C CA    1 
ATOM   13145 C  C     . ASN C 2 284 ? 121.082 71.278  111.683 1.00 25.24 ?  263 ASN C C     1 
ATOM   13146 O  O     . ASN C 2 284 ? 122.284 71.573  111.722 1.00 25.56 ?  263 ASN C O     1 
ATOM   13147 C  CB    . ASN C 2 284 ? 119.588 73.327  111.954 1.00 25.69 ?  263 ASN C CB    1 
ATOM   13148 C  CG    . ASN C 2 284 ? 119.122 74.550  111.197 1.00 26.39 ?  263 ASN C CG    1 
ATOM   13149 O  OD1   . ASN C 2 284 ? 119.935 75.334  110.700 1.00 26.91 ?  263 ASN C OD1   1 
ATOM   13150 N  ND2   . ASN C 2 284 ? 117.812 74.718  111.093 1.00 27.56 ?  263 ASN C ND2   1 
ATOM   13151 N  N     . ALA C 2 285 ? 120.603 70.134  112.179 1.00 24.51 ?  264 ALA C N     1 
ATOM   13152 C  CA    . ALA C 2 285 ? 121.510 69.061  112.630 1.00 24.19 ?  264 ALA C CA    1 
ATOM   13153 C  C     . ALA C 2 285 ? 122.516 68.654  111.534 1.00 24.63 ?  264 ALA C C     1 
ATOM   13154 O  O     . ALA C 2 285 ? 123.701 68.474  111.809 1.00 24.01 ?  264 ALA C O     1 
ATOM   13155 C  CB    . ALA C 2 285 ? 120.733 67.846  113.100 1.00 23.63 ?  264 ALA C CB    1 
ATOM   13156 N  N     . ASN C 2 286 ? 122.034 68.516  110.300 1.00 24.66 ?  265 ASN C N     1 
ATOM   13157 C  CA    . ASN C 2 286 ? 122.905 68.232  109.159 1.00 25.24 ?  265 ASN C CA    1 
ATOM   13158 C  C     . ASN C 2 286 ? 123.962 69.302  108.904 1.00 25.09 ?  265 ASN C C     1 
ATOM   13159 O  O     . ASN C 2 286 ? 125.093 68.971  108.513 1.00 24.14 ?  265 ASN C O     1 
ATOM   13160 C  CB    . ASN C 2 286 ? 122.088 67.987  107.878 1.00 25.62 ?  265 ASN C CB    1 
ATOM   13161 C  CG    . ASN C 2 286 ? 121.400 66.631  107.877 1.00 26.46 ?  265 ASN C CG    1 
ATOM   13162 O  OD1   . ASN C 2 286 ? 121.692 65.770  108.711 1.00 27.14 ?  265 ASN C OD1   1 
ATOM   13163 N  ND2   . ASN C 2 286 ? 120.465 66.441  106.944 1.00 27.89 ?  265 ASN C ND2   1 
ATOM   13164 N  N     . LYS C 2 287 ? 123.581 70.566  109.106 1.00 24.99 ?  266 LYS C N     1 
ATOM   13165 C  CA    . LYS C 2 287 ? 124.498 71.702  108.989 1.00 25.91 ?  266 LYS C CA    1 
ATOM   13166 C  C     . LYS C 2 287 ? 125.559 71.666  110.084 1.00 25.23 ?  266 LYS C C     1 
ATOM   13167 O  O     . LYS C 2 287 ? 126.726 71.973  109.829 1.00 25.34 ?  266 LYS C O     1 
ATOM   13168 C  CB    . LYS C 2 287 ? 123.754 73.035  109.076 1.00 25.96 ?  266 LYS C CB    1 
ATOM   13169 C  CG    . LYS C 2 287 ? 122.959 73.432  107.843 1.00 29.60 ?  266 LYS C CG    1 
ATOM   13170 C  CD    . LYS C 2 287 ? 122.506 74.890  107.997 1.00 34.20 ?  266 LYS C CD    1 
ATOM   13171 C  CE    . LYS C 2 287 ? 121.791 75.406  106.773 1.00 37.67 ?  266 LYS C CE    1 
ATOM   13172 N  NZ    . LYS C 2 287 ? 121.499 76.869  106.928 1.00 39.48 1  266 LYS C NZ    1 
ATOM   13173 N  N     . ALA C 2 288 ? 125.152 71.307  111.298 1.00 24.87 ?  267 ALA C N     1 
ATOM   13174 C  CA    . ALA C 2 288 ? 126.106 71.122  112.408 1.00 24.23 ?  267 ALA C CA    1 
ATOM   13175 C  C     . ALA C 2 288 ? 127.117 70.010  112.097 1.00 24.24 ?  267 ALA C C     1 
ATOM   13176 O  O     . ALA C 2 288 ? 128.322 70.190  112.282 1.00 23.96 ?  267 ALA C O     1 
ATOM   13177 C  CB    . ALA C 2 288 ? 125.372 70.828  113.703 1.00 24.23 ?  267 ALA C CB    1 
ATOM   13178 N  N     . LEU C 2 289 ? 126.628 68.865  111.620 1.00 24.63 ?  268 LEU C N     1 
ATOM   13179 C  CA    . LEU C 2 289 ? 127.518 67.775  111.214 1.00 25.14 ?  268 LEU C CA    1 
ATOM   13180 C  C     . LEU C 2 289 ? 128.483 68.242  110.136 1.00 25.58 ?  268 LEU C C     1 
ATOM   13181 O  O     . LEU C 2 289 ? 129.674 67.962  110.206 1.00 25.42 ?  268 LEU C O     1 
ATOM   13182 C  CB    . LEU C 2 289 ? 126.733 66.543  110.736 1.00 25.28 ?  268 LEU C CB    1 
ATOM   13183 C  CG    . LEU C 2 289 ? 126.051 65.731  111.842 1.00 25.93 ?  268 LEU C CG    1 
ATOM   13184 C  CD1   . LEU C 2 289 ? 124.965 64.843  111.268 1.00 26.50 ?  268 LEU C CD1   1 
ATOM   13185 C  CD2   . LEU C 2 289 ? 127.055 64.920  112.682 1.00 25.20 ?  268 LEU C CD2   1 
ATOM   13186 N  N     . MET C 2 290 ? 127.970 68.976  109.148 1.00 26.32 ?  269 MET C N     1 
ATOM   13187 C  CA    . MET C 2 290 ? 128.830 69.480  108.082 1.00 27.41 ?  269 MET C CA    1 
ATOM   13188 C  C     . MET C 2 290 ? 129.897 70.449  108.587 1.00 26.66 ?  269 MET C C     1 
ATOM   13189 O  O     . MET C 2 290 ? 131.037 70.406  108.120 1.00 26.69 ?  269 MET C O     1 
ATOM   13190 C  CB    . MET C 2 290 ? 128.009 70.072  106.941 1.00 28.28 ?  269 MET C CB    1 
ATOM   13191 C  CG    . MET C 2 290 ? 127.682 69.019  105.883 1.00 32.91 ?  269 MET C CG    1 
ATOM   13192 S  SD    . MET C 2 290 ? 126.445 69.567  104.702 1.00 42.49 ?  269 MET C SD    1 
ATOM   13193 C  CE    . MET C 2 290 ? 125.019 68.619  105.232 1.00 38.74 ?  269 MET C CE    1 
ATOM   13194 N  N     . ASN C 2 291 ? 129.536 71.290  109.557 1.00 25.48 ?  270 ASN C N     1 
ATOM   13195 C  CA    . ASN C 2 291 ? 130.494 72.197  110.209 1.00 25.39 ?  270 ASN C CA    1 
ATOM   13196 C  C     . ASN C 2 291 ? 131.641 71.435  110.893 1.00 25.18 ?  270 ASN C C     1 
ATOM   13197 O  O     . ASN C 2 291 ? 132.755 71.960  111.040 1.00 24.73 ?  270 ASN C O     1 
ATOM   13198 C  CB    . ASN C 2 291 ? 129.781 73.110  111.216 1.00 24.83 ?  270 ASN C CB    1 
ATOM   13199 C  CG    . ASN C 2 291 ? 128.978 74.227  110.540 1.00 25.58 ?  270 ASN C CG    1 
ATOM   13200 O  OD1   . ASN C 2 291 ? 129.126 74.487  109.350 1.00 25.58 ?  270 ASN C OD1   1 
ATOM   13201 N  ND2   . ASN C 2 291 ? 128.126 74.886  111.309 1.00 24.32 ?  270 ASN C ND2   1 
ATOM   13202 N  N     . LEU C 2 292 ? 131.351 70.189  111.275 1.00 25.09 ?  271 LEU C N     1 
ATOM   13203 C  CA    . LEU C 2 292 ? 132.322 69.267  111.881 1.00 25.46 ?  271 LEU C CA    1 
ATOM   13204 C  C     . LEU C 2 292 ? 133.053 68.364  110.873 1.00 26.18 ?  271 LEU C C     1 
ATOM   13205 O  O     . LEU C 2 292 ? 133.882 67.519  111.256 1.00 26.06 ?  271 LEU C O     1 
ATOM   13206 C  CB    . LEU C 2 292 ? 131.628 68.423  112.958 1.00 25.19 ?  271 LEU C CB    1 
ATOM   13207 C  CG    . LEU C 2 292 ? 131.122 69.201  114.184 1.00 25.03 ?  271 LEU C CG    1 
ATOM   13208 C  CD1   . LEU C 2 292 ? 130.205 68.336  115.020 1.00 24.50 ?  271 LEU C CD1   1 
ATOM   13209 C  CD2   . LEU C 2 292 ? 132.305 69.716  115.020 1.00 25.64 ?  271 LEU C CD2   1 
ATOM   13210 N  N     . GLY C 2 293 ? 132.751 68.545  109.588 1.00 26.71 ?  272 GLY C N     1 
ATOM   13211 C  CA    . GLY C 2 293 ? 133.361 67.741  108.521 1.00 28.06 ?  272 GLY C CA    1 
ATOM   13212 C  C     . GLY C 2 293 ? 132.776 66.347  108.353 1.00 29.34 ?  272 GLY C C     1 
ATOM   13213 O  O     . GLY C 2 293 ? 133.432 65.452  107.798 1.00 29.73 ?  272 GLY C O     1 
ATOM   13214 N  N     . PHE C 2 294 ? 131.546 66.157  108.828 1.00 29.88 ?  273 PHE C N     1 
ATOM   13215 C  CA    . PHE C 2 294 ? 130.863 64.869  108.742 1.00 31.24 ?  273 PHE C CA    1 
ATOM   13216 C  C     . PHE C 2 294 ? 129.720 64.913  107.719 1.00 32.42 ?  273 PHE C C     1 
ATOM   13217 O  O     . PHE C 2 294 ? 129.200 65.990  107.394 1.00 32.30 ?  273 PHE C O     1 
ATOM   13218 C  CB    . PHE C 2 294 ? 130.334 64.437  110.116 1.00 30.82 ?  273 PHE C CB    1 
ATOM   13219 C  CG    . PHE C 2 294 ? 131.409 64.263  111.168 1.00 30.93 ?  273 PHE C CG    1 
ATOM   13220 C  CD1   . PHE C 2 294 ? 132.563 63.525  110.904 1.00 30.85 ?  273 PHE C CD1   1 
ATOM   13221 C  CD2   . PHE C 2 294 ? 131.258 64.826  112.427 1.00 30.30 ?  273 PHE C CD2   1 
ATOM   13222 C  CE1   . PHE C 2 294 ? 133.552 63.372  111.874 1.00 30.75 ?  273 PHE C CE1   1 
ATOM   13223 C  CE2   . PHE C 2 294 ? 132.234 64.667  113.412 1.00 30.41 ?  273 PHE C CE2   1 
ATOM   13224 C  CZ    . PHE C 2 294 ? 133.382 63.934  113.137 1.00 30.88 ?  273 PHE C CZ    1 
ATOM   13225 N  N     . ASP C 2 295 ? 129.350 63.741  107.208 1.00 33.81 ?  274 ASP C N     1 
ATOM   13226 C  CA    . ASP C 2 295 ? 128.231 63.603  106.271 1.00 35.32 ?  274 ASP C CA    1 
ATOM   13227 C  C     . ASP C 2 295 ? 126.880 63.877  106.956 1.00 35.36 ?  274 ASP C C     1 
ATOM   13228 O  O     . ASP C 2 295 ? 126.727 63.597  108.143 1.00 34.78 ?  274 ASP C O     1 
ATOM   13229 C  CB    . ASP C 2 295 ? 128.209 62.187  105.678 1.00 35.95 ?  274 ASP C CB    1 
ATOM   13230 C  CG    . ASP C 2 295 ? 129.444 61.873  104.838 1.00 37.98 ?  274 ASP C CG    1 
ATOM   13231 O  OD1   . ASP C 2 295 ? 130.060 62.800  104.269 1.00 39.83 ?  274 ASP C OD1   1 
ATOM   13232 O  OD2   . ASP C 2 295 ? 129.796 60.677  104.746 1.00 40.03 -1 274 ASP C OD2   1 
ATOM   13233 N  N     . PRO C 2 296 ? 125.897 64.416  106.209 1.00 36.33 ?  275 PRO C N     1 
ATOM   13234 C  CA    . PRO C 2 296 ? 124.535 64.588  106.760 1.00 36.92 ?  275 PRO C CA    1 
ATOM   13235 C  C     . PRO C 2 296 ? 123.932 63.272  107.278 1.00 37.68 ?  275 PRO C C     1 
ATOM   13236 O  O     . PRO C 2 296 ? 124.175 62.211  106.697 1.00 38.07 ?  275 PRO C O     1 
ATOM   13237 C  CB    . PRO C 2 296 ? 123.728 65.118  105.564 1.00 36.82 ?  275 PRO C CB    1 
ATOM   13238 C  CG    . PRO C 2 296 ? 124.607 64.888  104.343 1.00 37.42 ?  275 PRO C CG    1 
ATOM   13239 C  CD    . PRO C 2 296 ? 126.011 64.964  104.845 1.00 36.41 ?  275 PRO C CD    1 
ATOM   13240 N  N     . TYR C 2 297 ? 123.160 63.350  108.362 1.00 38.10 ?  276 TYR C N     1 
ATOM   13241 C  CA    . TYR C 2 297 ? 122.624 62.164  109.047 1.00 38.96 ?  276 TYR C CA    1 
ATOM   13242 C  C     . TYR C 2 297 ? 121.121 61.970  108.815 1.00 39.71 ?  276 TYR C C     1 
ATOM   13243 O  O     . TYR C 2 297 ? 120.620 60.841  108.849 1.00 40.18 ?  276 TYR C O     1 
ATOM   13244 C  CB    . TYR C 2 297 ? 122.911 62.279  110.548 1.00 38.94 ?  276 TYR C CB    1 
ATOM   13245 C  CG    . TYR C 2 297 ? 122.531 61.102  111.422 1.00 39.64 ?  276 TYR C CG    1 
ATOM   13246 C  CD1   . TYR C 2 297 ? 123.367 59.989  111.538 1.00 40.43 ?  276 TYR C CD1   1 
ATOM   13247 C  CD2   . TYR C 2 297 ? 121.367 61.129  112.183 1.00 41.04 ?  276 TYR C CD2   1 
ATOM   13248 C  CE1   . TYR C 2 297 ? 123.026 58.913  112.361 1.00 41.69 ?  276 TYR C CE1   1 
ATOM   13249 C  CE2   . TYR C 2 297 ? 121.014 60.060  113.008 1.00 41.60 ?  276 TYR C CE2   1 
ATOM   13250 C  CZ    . TYR C 2 297 ? 121.850 58.959  113.096 1.00 41.92 ?  276 TYR C CZ    1 
ATOM   13251 O  OH    . TYR C 2 297 ? 121.502 57.910  113.919 1.00 42.52 ?  276 TYR C OH    1 
ATOM   13252 N  N     . PHE C 2 298 ? 120.403 63.066  108.595 1.00 39.85 ?  277 PHE C N     1 
ATOM   13253 C  CA    . PHE C 2 298 ? 118.962 62.998  108.379 1.00 40.77 ?  277 PHE C CA    1 
ATOM   13254 C  C     . PHE C 2 298 ? 118.630 63.223  106.912 1.00 41.95 ?  277 PHE C C     1 
ATOM   13255 O  O     . PHE C 2 298 ? 119.342 63.947  106.219 1.00 41.91 ?  277 PHE C O     1 
ATOM   13256 C  CB    . PHE C 2 298 ? 118.240 64.032  109.250 1.00 39.94 ?  277 PHE C CB    1 
ATOM   13257 C  CG    . PHE C 2 298 ? 118.399 63.805  110.728 1.00 39.09 ?  277 PHE C CG    1 
ATOM   13258 C  CD1   . PHE C 2 298 ? 119.222 64.629  111.486 1.00 37.84 ?  277 PHE C CD1   1 
ATOM   13259 C  CD2   . PHE C 2 298 ? 117.713 62.774  111.367 1.00 38.97 ?  277 PHE C CD2   1 
ATOM   13260 C  CE1   . PHE C 2 298 ? 119.371 64.430  112.856 1.00 37.46 ?  277 PHE C CE1   1 
ATOM   13261 C  CE2   . PHE C 2 298 ? 117.853 62.565  112.734 1.00 38.20 ?  277 PHE C CE2   1 
ATOM   13262 C  CZ    . PHE C 2 298 ? 118.683 63.396  113.482 1.00 37.91 ?  277 PHE C CZ    1 
ATOM   13263 N  N     . GLU C 2 299 ? 117.552 62.602  106.431 1.00 43.74 ?  278 GLU C N     1 
ATOM   13264 C  CA    . GLU C 2 299 ? 117.133 62.802  105.040 1.00 45.61 ?  278 GLU C CA    1 
ATOM   13265 C  C     . GLU C 2 299 ? 116.528 64.194  104.856 1.00 46.04 ?  278 GLU C C     1 
ATOM   13266 O  O     . GLU C 2 299 ? 115.942 64.755  105.783 1.00 45.88 ?  278 GLU C O     1 
ATOM   13267 C  CB    . GLU C 2 299 ? 116.144 61.725  104.582 1.00 46.43 ?  278 GLU C CB    1 
ATOM   13268 C  CG    . GLU C 2 299 ? 116.238 61.412  103.079 1.00 48.82 ?  278 GLU C CG    1 
ATOM   13269 C  CD    . GLU C 2 299 ? 114.988 60.752  102.515 1.00 51.86 ?  278 GLU C CD    1 
ATOM   13270 O  OE1   . GLU C 2 299 ? 114.968 60.475  101.295 1.00 53.35 ?  278 GLU C OE1   1 
ATOM   13271 O  OE2   . GLU C 2 299 ? 114.024 60.512  103.280 1.00 53.10 -1 278 GLU C OE2   1 
ATOM   13272 N  N     . GLU C 2 300 ? 116.689 64.748  103.655 1.00 47.16 ?  279 GLU C N     1 
ATOM   13273 C  CA    . GLU C 2 300 ? 116.152 66.069  103.312 1.00 47.75 ?  279 GLU C CA    1 
ATOM   13274 C  C     . GLU C 2 300 ? 114.616 66.100  103.313 1.00 47.71 ?  279 GLU C C     1 
ATOM   13275 O  O     . GLU C 2 300 ? 113.967 65.140  102.884 1.00 47.77 ?  279 GLU C O     1 
ATOM   13276 C  CB    . GLU C 2 300 ? 116.712 66.538  101.957 1.00 48.42 ?  279 GLU C CB    1 
ATOM   13277 C  CG    . GLU C 2 300 ? 116.581 65.520  100.819 1.00 50.63 ?  279 GLU C CG    1 
ATOM   13278 C  CD    . GLU C 2 300 ? 117.589 65.744  99.692  1.00 53.06 ?  279 GLU C CD    1 
ATOM   13279 O  OE1   . GLU C 2 300 ? 117.652 66.874  99.150  1.00 54.35 ?  279 GLU C OE1   1 
ATOM   13280 O  OE2   . GLU C 2 300 ? 118.310 64.782  99.340  1.00 53.32 -1 279 GLU C OE2   1 
ATOM   13281 N  N     . GLU C 2 301 ? 114.056 67.200  103.817 1.00 47.40 ?  280 GLU C N     1 
ATOM   13282 C  CA    . GLU C 2 301 ? 112.605 67.420  103.865 1.00 47.46 ?  280 GLU C CA    1 
ATOM   13283 C  C     . GLU C 2 301 ? 112.266 68.866  103.483 1.00 47.31 ?  280 GLU C C     1 
ATOM   13284 O  O     . GLU C 2 301 ? 113.111 69.757  103.608 1.00 47.21 ?  280 GLU C O     1 
ATOM   13285 C  CB    . GLU C 2 301 ? 112.055 67.129  105.269 1.00 47.19 ?  280 GLU C CB    1 
ATOM   13286 C  CG    . GLU C 2 301 ? 112.245 65.699  105.778 1.00 47.14 ?  280 GLU C CG    1 
ATOM   13287 C  CD    . GLU C 2 301 ? 112.160 65.607  107.299 1.00 47.21 ?  280 GLU C CD    1 
ATOM   13288 O  OE1   . GLU C 2 301 ? 111.140 65.098  107.806 1.00 46.97 ?  280 GLU C OE1   1 
ATOM   13289 O  OE2   . GLU C 2 301 ? 113.109 66.054  107.988 1.00 46.13 -1 280 GLU C OE2   1 
ATOM   13290 N  N     . ASP C 2 302 ? 111.036 69.095  103.024 1.00 47.15 ?  281 ASP C N     1 
ATOM   13291 C  CA    . ASP C 2 302 ? 110.579 70.447  102.687 1.00 47.04 ?  281 ASP C CA    1 
ATOM   13292 C  C     . ASP C 2 302 ? 110.292 71.256  103.957 1.00 46.05 ?  281 ASP C C     1 
ATOM   13293 O  O     . ASP C 2 302 ? 109.430 70.882  104.758 1.00 46.10 ?  281 ASP C O     1 
ATOM   13294 C  CB    . ASP C 2 302 ? 109.325 70.411  101.794 1.00 47.66 ?  281 ASP C CB    1 
ATOM   13295 C  CG    . ASP C 2 302 ? 109.622 69.978  100.356 1.00 49.53 ?  281 ASP C CG    1 
ATOM   13296 O  OD1   . ASP C 2 302 ? 110.708 70.304  99.827  1.00 50.58 ?  281 ASP C OD1   1 
ATOM   13297 O  OD2   . ASP C 2 302 ? 108.743 69.325  99.741  1.00 51.14 -1 281 ASP C OD2   1 
ATOM   13298 N  N     . ILE C 2 303 ? 111.030 72.350  104.135 1.00 44.96 ?  282 ILE C N     1 
ATOM   13299 C  CA    . ILE C 2 303 ? 110.829 73.269  105.260 1.00 43.99 ?  282 ILE C CA    1 
ATOM   13300 C  C     . ILE C 2 303 ? 109.732 74.279  104.912 1.00 43.53 ?  282 ILE C C     1 
ATOM   13301 O  O     . ILE C 2 303 ? 109.592 74.662  103.749 1.00 43.52 ?  282 ILE C O     1 
ATOM   13302 C  CB    . ILE C 2 303 ? 112.146 74.019  105.622 1.00 43.84 ?  282 ILE C CB    1 
ATOM   13303 C  CG1   . ILE C 2 303 ? 113.296 73.031  105.891 1.00 43.91 ?  282 ILE C CG1   1 
ATOM   13304 C  CG2   . ILE C 2 303 ? 111.940 74.993  106.795 1.00 43.55 ?  282 ILE C CG2   1 
ATOM   13305 C  CD1   . ILE C 2 303 ? 113.050 72.029  107.023 1.00 42.76 ?  282 ILE C CD1   1 
ATOM   13306 N  N     . ASN C 2 304 ? 108.954 74.695  105.912 1.00 42.51 ?  283 ASN C N     1 
ATOM   13307 C  CA    . ASN C 2 304 ? 107.909 75.701  105.718 1.00 41.93 ?  283 ASN C CA    1 
ATOM   13308 C  C     . ASN C 2 304 ? 108.472 76.922  104.975 1.00 41.78 ?  283 ASN C C     1 
ATOM   13309 O  O     . ASN C 2 304 ? 109.428 77.548  105.453 1.00 41.13 ?  283 ASN C O     1 
ATOM   13310 C  CB    . ASN C 2 304 ? 107.313 76.118  107.071 1.00 41.83 ?  283 ASN C CB    1 
ATOM   13311 C  CG    . ASN C 2 304 ? 105.933 76.763  106.946 1.00 41.27 ?  283 ASN C CG    1 
ATOM   13312 O  OD1   . ASN C 2 304 ? 105.698 77.615  106.092 1.00 41.28 ?  283 ASN C OD1   1 
ATOM   13313 N  ND2   . ASN C 2 304 ? 105.017 76.357  107.813 1.00 40.67 ?  283 ASN C ND2   1 
ATOM   13314 N  N     . PRO C 2 305 ? 107.896 77.255  103.793 1.00 41.74 ?  284 PRO C N     1 
ATOM   13315 C  CA    . PRO C 2 305 ? 108.432 78.364  102.988 1.00 41.82 ?  284 PRO C CA    1 
ATOM   13316 C  C     . PRO C 2 305 ? 108.340 79.720  103.697 1.00 41.56 ?  284 PRO C C     1 
ATOM   13317 O  O     . PRO C 2 305 ? 109.097 80.637  103.370 1.00 41.46 ?  284 PRO C O     1 
ATOM   13318 C  CB    . PRO C 2 305 ? 107.569 78.342  101.712 1.00 42.14 ?  284 PRO C CB    1 
ATOM   13319 C  CG    . PRO C 2 305 ? 106.336 77.602  102.082 1.00 42.59 ?  284 PRO C CG    1 
ATOM   13320 C  CD    . PRO C 2 305 ? 106.753 76.598  103.129 1.00 42.05 ?  284 PRO C CD    1 
ATOM   13321 N  N     . ILE C 2 306 ? 107.433 79.831  104.664 1.00 41.19 ?  285 ILE C N     1 
ATOM   13322 C  CA    . ILE C 2 306 ? 107.316 81.024  105.502 1.00 41.47 ?  285 ILE C CA    1 
ATOM   13323 C  C     . ILE C 2 306 ? 108.624 81.267  106.267 1.00 41.71 ?  285 ILE C C     1 
ATOM   13324 O  O     . ILE C 2 306 ? 109.133 82.387  106.301 1.00 41.38 ?  285 ILE C O     1 
ATOM   13325 C  CB    . ILE C 2 306 ? 106.140 80.901  106.508 1.00 41.22 ?  285 ILE C CB    1 
ATOM   13326 C  CG1   . ILE C 2 306 ? 104.803 80.770  105.766 1.00 41.27 ?  285 ILE C CG1   1 
ATOM   13327 C  CG2   . ILE C 2 306 ? 106.123 82.081  107.477 1.00 40.37 ?  285 ILE C CG2   1 
ATOM   13328 C  CD1   . ILE C 2 306 ? 103.662 80.274  106.643 1.00 41.85 ?  285 ILE C CD1   1 
ATOM   13329 N  N     . VAL C 2 307 ? 109.153 80.204  106.871 1.00 42.33 ?  286 VAL C N     1 
ATOM   13330 C  CA    . VAL C 2 307 ? 110.416 80.257  107.614 1.00 43.36 ?  286 VAL C CA    1 
ATOM   13331 C  C     . VAL C 2 307 ? 111.605 80.600  106.706 1.00 44.51 ?  286 VAL C C     1 
ATOM   13332 O  O     . VAL C 2 307 ? 112.524 81.299  107.129 1.00 44.57 ?  286 VAL C O     1 
ATOM   13333 C  CB    . VAL C 2 307 ? 110.651 78.949  108.407 1.00 42.97 ?  286 VAL C CB    1 
ATOM   13334 C  CG1   . VAL C 2 307 ? 112.104 78.834  108.898 1.00 42.86 ?  286 VAL C CG1   1 
ATOM   13335 C  CG2   . VAL C 2 307 ? 109.682 78.886  109.572 1.00 41.93 ?  286 VAL C CG2   1 
ATOM   13336 N  N     . LEU C 2 308 ? 111.557 80.123  105.463 1.00 46.21 ?  287 LEU C N     1 
ATOM   13337 C  CA    . LEU C 2 308 ? 112.571 80.427  104.443 1.00 47.66 ?  287 LEU C CA    1 
ATOM   13338 C  C     . LEU C 2 308 ? 112.532 81.890  104.005 1.00 48.82 ?  287 LEU C C     1 
ATOM   13339 O  O     . LEU C 2 308 ? 113.579 82.486  103.718 1.00 49.02 ?  287 LEU C O     1 
ATOM   13340 C  CB    . LEU C 2 308 ? 112.417 79.494  103.233 1.00 47.95 ?  287 LEU C CB    1 
ATOM   13341 C  CG    . LEU C 2 308 ? 113.197 78.168  103.223 1.00 48.23 ?  287 LEU C CG    1 
ATOM   13342 C  CD1   . LEU C 2 308 ? 113.530 77.630  104.622 1.00 48.10 ?  287 LEU C CD1   1 
ATOM   13343 C  CD2   . LEU C 2 308 ? 112.477 77.111  102.389 1.00 48.81 ?  287 LEU C CD2   1 
ATOM   13344 N  N     . ASN C 2 309 ? 111.326 82.457  103.954 1.00 49.80 ?  288 ASN C N     1 
ATOM   13345 C  CA    . ASN C 2 309 ? 111.151 83.897  103.778 1.00 51.09 ?  288 ASN C CA    1 
ATOM   13346 C  C     . ASN C 2 309 ? 111.571 84.697  105.015 1.00 51.08 ?  288 ASN C C     1 
ATOM   13347 O  O     . ASN C 2 309 ? 111.925 85.870  104.906 1.00 51.41 ?  288 ASN C O     1 
ATOM   13348 C  CB    . ASN C 2 309 ? 109.713 84.233  103.374 1.00 51.37 ?  288 ASN C CB    1 
ATOM   13349 C  CG    . ASN C 2 309 ? 109.461 84.021  101.894 1.00 53.22 ?  288 ASN C CG    1 
ATOM   13350 O  OD1   . ASN C 2 309 ? 109.838 82.992  101.324 1.00 54.39 ?  288 ASN C OD1   1 
ATOM   13351 N  ND2   . ASN C 2 309 ? 108.821 84.998  101.261 1.00 54.70 ?  288 ASN C ND2   1 
ATOM   13352 N  N     . GLY C 2 310 ? 111.529 84.054  106.182 1.00 51.25 ?  289 GLY C N     1 
ATOM   13353 C  CA    . GLY C 2 310 ? 112.035 84.641  107.425 1.00 51.35 ?  289 GLY C CA    1 
ATOM   13354 C  C     . GLY C 2 310 ? 113.543 84.857  107.420 1.00 51.86 ?  289 GLY C C     1 
ATOM   13355 O  O     . GLY C 2 310 ? 114.062 85.672  108.191 1.00 51.49 ?  289 GLY C O     1 
ATOM   13356 N  N     . LEU C 2 311 ? 114.246 84.125  106.555 1.00 52.45 ?  290 LEU C N     1 
ATOM   13357 C  CA    . LEU C 2 311 ? 115.695 84.268  106.396 1.00 52.99 ?  290 LEU C CA    1 
ATOM   13358 C  C     . LEU C 2 311 ? 116.040 85.359  105.379 1.00 53.65 ?  290 LEU C C     1 
ATOM   13359 O  O     . LEU C 2 311 ? 115.828 85.202  104.170 1.00 54.22 ?  290 LEU C O     1 
ATOM   13360 C  CB    . LEU C 2 311 ? 116.330 82.937  105.982 1.00 53.08 ?  290 LEU C CB    1 
ATOM   13361 C  CG    . LEU C 2 311 ? 116.440 81.809  107.012 1.00 53.33 ?  290 LEU C CG    1 
ATOM   13362 C  CD1   . LEU C 2 311 ? 116.736 80.487  106.319 1.00 53.79 ?  290 LEU C CD1   1 
ATOM   13363 C  CD2   . LEU C 2 311 ? 117.504 82.115  108.068 1.00 53.22 ?  290 LEU C CD2   1 
ATOM   13364 N  N     . LYS C 2 330 ? 140.685 116.309 114.431 1.00 58.93 ?  309 LYS C N     1 
ATOM   13365 C  CA    . LYS C 2 330 ? 142.137 116.410 114.345 1.00 61.98 ?  309 LYS C CA    1 
ATOM   13366 C  C     . LYS C 2 330 ? 142.631 116.113 112.934 1.00 61.97 ?  309 LYS C C     1 
ATOM   13367 O  O     . LYS C 2 330 ? 142.072 115.270 112.232 1.00 59.24 ?  309 LYS C O     1 
ATOM   13368 C  CB    . LYS C 2 330 ? 142.800 115.457 115.343 1.00 60.82 ?  309 LYS C CB    1 
ATOM   13369 C  CG    . LYS C 2 330 ? 142.477 115.753 116.798 1.00 60.80 ?  309 LYS C CG    1 
ATOM   13370 C  CD    . LYS C 2 330 ? 143.209 116.994 117.283 1.00 60.28 ?  309 LYS C CD    1 
ATOM   13371 C  CE    . LYS C 2 330 ? 144.150 116.670 118.433 1.00 62.15 ?  309 LYS C CE    1 
ATOM   13372 N  NZ    . LYS C 2 330 ? 143.627 115.572 119.291 1.00 62.59 1  309 LYS C NZ    1 
ATOM   13373 N  N     . ALA C 2 331 ? 143.683 116.815 112.525 1.00 55.97 ?  310 ALA C N     1 
ATOM   13374 C  CA    . ALA C 2 331 ? 144.299 116.633 111.222 1.00 53.20 ?  310 ALA C CA    1 
ATOM   13375 C  C     . ALA C 2 331 ? 145.745 116.185 111.389 1.00 52.13 ?  310 ALA C C     1 
ATOM   13376 O  O     . ALA C 2 331 ? 146.387 116.471 112.404 1.00 53.07 ?  310 ALA C O     1 
ATOM   13377 C  CB    . ALA C 2 331 ? 144.244 117.923 110.399 1.00 51.98 ?  310 ALA C CB    1 
ATOM   13378 N  N     . THR C 2 332 ? 146.246 115.468 110.384 1.00 45.82 ?  311 THR C N     1 
ATOM   13379 C  CA    . THR C 2 332 ? 147.624 114.999 110.407 1.00 46.85 ?  311 THR C CA    1 
ATOM   13380 C  C     . THR C 2 332 ? 148.590 116.175 110.496 1.00 43.12 ?  311 THR C C     1 
ATOM   13381 O  O     . THR C 2 332 ? 148.388 117.216 109.866 1.00 48.26 ?  311 THR C O     1 
ATOM   13382 C  CB    . THR C 2 332 ? 147.916 114.156 109.164 1.00 45.72 ?  311 THR C CB    1 
ATOM   13383 O  OG1   . THR C 2 332 ? 149.198 113.527 109.293 1.00 46.36 ?  311 THR C OG1   1 
ATOM   13384 C  CG2   . THR C 2 332 ? 147.875 115.011 107.910 1.00 44.89 ?  311 THR C CG2   1 
ATOM   13385 N  N     . VAL C 2 333 ? 149.638 116.003 111.296 1.00 42.01 ?  312 VAL C N     1 
ATOM   13386 C  CA    . VAL C 2 333 ? 150.549 117.082 111.660 1.00 38.55 ?  312 VAL C CA    1 
ATOM   13387 C  C     . VAL C 2 333 ? 151.941 116.724 111.158 1.00 41.18 ?  312 VAL C C     1 
ATOM   13388 O  O     . VAL C 2 333 ? 152.476 115.659 111.489 1.00 46.85 ?  312 VAL C O     1 
ATOM   13389 C  CB    . VAL C 2 333 ? 150.560 117.324 113.176 1.00 37.39 ?  312 VAL C CB    1 
ATOM   13390 C  CG1   . VAL C 2 333 ? 151.749 118.186 113.570 1.00 40.81 ?  312 VAL C CG1   1 
ATOM   13391 C  CG2   . VAL C 2 333 ? 149.254 117.956 113.627 1.00 39.47 ?  312 VAL C CG2   1 
ATOM   13392 N  N     . GLU C 2 334 ? 152.533 117.614 110.357 1.00 34.01 ?  313 GLU C N     1 
ATOM   13393 C  CA    . GLU C 2 334 ? 153.943 117.505 110.025 1.00 34.45 ?  313 GLU C CA    1 
ATOM   13394 C  C     . GLU C 2 334 ? 154.703 118.714 110.559 1.00 37.55 ?  313 GLU C C     1 
ATOM   13395 O  O     . GLU C 2 334 ? 154.168 119.828 110.583 1.00 40.51 ?  313 GLU C O     1 
ATOM   13396 C  CB    . GLU C 2 334 ? 154.185 117.409 108.514 1.00 34.27 ?  313 GLU C CB    1 
ATOM   13397 C  CG    . GLU C 2 334 ? 155.627 117.221 108.092 1.00 38.73 ?  313 GLU C CG    1 
ATOM   13398 C  CD    . GLU C 2 334 ? 155.763 117.088 106.585 1.00 42.14 ?  313 GLU C CD    1 
ATOM   13399 O  OE1   . GLU C 2 334 ? 154.732 117.183 105.887 1.00 40.76 ?  313 GLU C OE1   1 
ATOM   13400 O  OE2   . GLU C 2 334 ? 156.892 116.874 106.101 1.00 39.96 -1 313 GLU C OE2   1 
ATOM   13401 N  N     . PRO C 2 335 ? 155.945 118.533 110.996 1.00 33.56 ?  314 PRO C N     1 
ATOM   13402 C  CA    . PRO C 2 335 ? 156.757 119.682 111.409 1.00 34.05 ?  314 PRO C CA    1 
ATOM   13403 C  C     . PRO C 2 335 ? 157.147 120.532 110.209 1.00 35.93 ?  314 PRO C C     1 
ATOM   13404 O  O     . PRO C 2 335 ? 157.174 120.080 109.063 1.00 36.72 ?  314 PRO C O     1 
ATOM   13405 C  CB    . PRO C 2 335 ? 157.986 119.044 112.068 1.00 36.78 ?  314 PRO C CB    1 
ATOM   13406 C  CG    . PRO C 2 335 ? 157.621 117.598 112.282 1.00 33.20 ?  314 PRO C CG    1 
ATOM   13407 C  CD    . PRO C 2 335 ? 156.651 117.260 111.201 1.00 33.09 ?  314 PRO C CD    1 
ATOM   13408 N  N     . LEU C 2 336 ? 157.452 121.794 110.492 1.00 31.29 ?  315 LEU C N     1 
ATOM   13409 C  CA    . LEU C 2 336 ? 157.851 122.742 109.462 1.00 25.88 ?  315 LEU C CA    1 
ATOM   13410 C  C     . LEU C 2 336 ? 159.340 122.613 109.178 1.00 28.32 ?  315 LEU C C     1 
ATOM   13411 O  O     . LEU C 2 336 ? 160.166 122.717 110.092 1.00 26.34 ?  315 LEU C O     1 
ATOM   13412 C  CB    . LEU C 2 336 ? 157.517 124.173 109.882 1.00 25.22 ?  315 LEU C CB    1 
ATOM   13413 C  CG    . LEU C 2 336 ? 156.101 124.645 109.560 1.00 26.15 ?  315 LEU C CG    1 
ATOM   13414 C  CD1   . LEU C 2 336 ? 155.889 126.066 110.050 1.00 26.32 ?  315 LEU C CD1   1 
ATOM   13415 C  CD2   . LEU C 2 336 ? 155.858 124.549 108.065 1.00 21.64 ?  315 LEU C CD2   1 
ATOM   13416 N  N     . LYS C 2 337 ? 159.678 122.386 107.914 1.00 24.69 ?  316 LYS C N     1 
ATOM   13417 C  CA    . LYS C 2 337 ? 161.063 122.349 107.480 1.00 25.14 ?  316 LYS C CA    1 
ATOM   13418 C  C     . LYS C 2 337 ? 161.557 123.760 107.182 1.00 19.78 ?  316 LYS C C     1 
ATOM   13419 O  O     . LYS C 2 337 ? 160.774 124.683 106.951 1.00 30.21 ?  316 LYS C O     1 
ATOM   13420 C  CB    . LYS C 2 337 ? 161.220 121.466 106.241 1.00 29.25 ?  316 LYS C CB    1 
ATOM   13421 C  CG    . LYS C 2 337 ? 160.961 119.990 106.487 1.00 28.02 ?  316 LYS C CG    1 
ATOM   13422 C  CD    . LYS C 2 337 ? 161.111 119.180 105.211 1.00 27.52 ?  316 LYS C CD    1 
ATOM   13423 C  CE    . LYS C 2 337 ? 160.875 117.701 105.465 1.00 32.76 ?  316 LYS C CE    1 
ATOM   13424 N  NZ    . LYS C 2 337 ? 160.995 116.895 104.218 1.00 30.53 1  316 LYS C NZ    1 
ATOM   13425 N  N     . ASP C 2 338 ? 162.881 123.918 107.194 1.00 29.74 ?  317 ASP C N     1 
ATOM   13426 C  CA    . ASP C 2 338 ? 163.473 125.209 106.870 1.00 26.29 ?  317 ASP C CA    1 
ATOM   13427 C  C     . ASP C 2 338 ? 163.235 125.605 105.420 1.00 29.71 ?  317 ASP C C     1 
ATOM   13428 O  O     . ASP C 2 338 ? 163.345 126.790 105.088 1.00 21.95 ?  317 ASP C O     1 
ATOM   13429 C  CB    . ASP C 2 338 ? 164.973 125.191 107.168 1.00 25.78 ?  317 ASP C CB    1 
ATOM   13430 C  CG    . ASP C 2 338 ? 165.294 124.524 108.489 1.00 35.15 ?  317 ASP C CG    1 
ATOM   13431 O  OD1   . ASP C 2 338 ? 164.917 123.347 108.669 1.00 32.75 ?  317 ASP C OD1   1 
ATOM   13432 O  OD2   . ASP C 2 338 ? 165.923 125.178 109.348 1.00 36.30 -1 317 ASP C OD2   1 
ATOM   13433 N  N     . ASP C 2 339 ? 162.910 124.648 104.553 1.00 26.99 ?  318 ASP C N     1 
ATOM   13434 C  CA    . ASP C 2 339 ? 162.635 124.931 103.152 1.00 24.15 ?  318 ASP C CA    1 
ATOM   13435 C  C     . ASP C 2 339 ? 161.205 125.388 102.904 1.00 20.41 ?  318 ASP C C     1 
ATOM   13436 O  O     . ASP C 2 339 ? 160.906 125.867 101.805 1.00 28.59 ?  318 ASP C O     1 
ATOM   13437 C  CB    . ASP C 2 339 ? 162.930 123.695 102.295 1.00 23.02 ?  318 ASP C CB    1 
ATOM   13438 C  CG    . ASP C 2 339 ? 164.112 122.898 102.812 1.00 32.33 ?  318 ASP C CG    1 
ATOM   13439 O  OD1   . ASP C 2 339 ? 163.897 121.798 103.363 1.00 34.56 ?  318 ASP C OD1   1 
ATOM   13440 O  OD2   . ASP C 2 339 ? 165.258 123.374 102.667 1.00 32.78 -1 318 ASP C OD2   1 
ATOM   13441 N  N     . ASP C 2 340 ? 160.319 125.255 103.888 1.00 18.60 ?  319 ASP C N     1 
ATOM   13442 C  CA    . ASP C 2 340 ? 158.948 125.731 103.768 1.00 13.68 ?  319 ASP C CA    1 
ATOM   13443 C  C     . ASP C 2 340 ? 158.822 127.225 104.027 1.00 14.05 ?  319 ASP C C     1 
ATOM   13444 O  O     . ASP C 2 340 ? 157.737 127.784 103.840 1.00 30.27 ?  319 ASP C O     1 
ATOM   13445 C  CB    . ASP C 2 340 ? 158.034 124.964 104.729 1.00 12.38 ?  319 ASP C CB    1 
ATOM   13446 C  CG    . ASP C 2 340 ? 158.259 123.469 104.679 1.00 24.62 ?  319 ASP C CG    1 
ATOM   13447 O  OD1   . ASP C 2 340 ? 158.410 122.925 103.566 1.00 25.90 ?  319 ASP C OD1   1 
ATOM   13448 O  OD2   . ASP C 2 340 ? 158.279 122.835 105.754 1.00 30.97 -1 319 ASP C OD2   1 
ATOM   13449 N  N     . PHE C 2 341 ? 159.898 127.877 104.457 1.00 14.34 ?  320 PHE C N     1 
ATOM   13450 C  CA    . PHE C 2 341 ? 159.908 129.308 104.719 1.00 3.83  ?  320 PHE C CA    1 
ATOM   13451 C  C     . PHE C 2 341 ? 160.483 130.108 103.559 1.00 6.43  ?  320 PHE C C     1 
ATOM   13452 O  O     . PHE C 2 341 ? 160.631 131.328 103.674 1.00 11.38 ?  320 PHE C O     1 
ATOM   13453 C  CB    . PHE C 2 341 ? 160.697 129.599 105.995 1.00 8.01  ?  320 PHE C CB    1 
ATOM   13454 C  CG    . PHE C 2 341 ? 159.984 129.202 107.254 1.00 9.69  ?  320 PHE C CG    1 
ATOM   13455 C  CD1   . PHE C 2 341 ? 159.147 130.094 107.900 1.00 6.44  ?  320 PHE C CD1   1 
ATOM   13456 C  CD2   . PHE C 2 341 ? 160.150 127.938 107.791 1.00 7.94  ?  320 PHE C CD2   1 
ATOM   13457 C  CE1   . PHE C 2 341 ? 158.491 129.733 109.058 1.00 10.55 ?  320 PHE C CE1   1 
ATOM   13458 C  CE2   . PHE C 2 341 ? 159.494 127.571 108.949 1.00 8.92  ?  320 PHE C CE2   1 
ATOM   13459 C  CZ    . PHE C 2 341 ? 158.662 128.471 109.583 1.00 6.02  ?  320 PHE C CZ    1 
ATOM   13460 N  N     . TYR C 2 342 ? 160.811 129.452 102.449 1.00 6.07  ?  321 TYR C N     1 
ATOM   13461 C  CA    . TYR C 2 342 ? 161.412 130.105 101.297 1.00 12.59 ?  321 TYR C CA    1 
ATOM   13462 C  C     . TYR C 2 342 ? 160.672 129.688 100.037 1.00 16.10 ?  321 TYR C C     1 
ATOM   13463 O  O     . TYR C 2 342 ? 160.278 128.527 99.893  1.00 16.79 ?  321 TYR C O     1 
ATOM   13464 C  CB    . TYR C 2 342 ? 162.899 129.755 101.174 1.00 6.93  ?  321 TYR C CB    1 
ATOM   13465 C  CG    . TYR C 2 342 ? 163.725 130.214 102.352 1.00 3.43  ?  321 TYR C CG    1 
ATOM   13466 C  CD1   . TYR C 2 342 ? 163.890 129.402 103.466 1.00 8.24  ?  321 TYR C CD1   1 
ATOM   13467 C  CD2   . TYR C 2 342 ? 164.331 131.461 102.354 1.00 11.16 ?  321 TYR C CD2   1 
ATOM   13468 C  CE1   . TYR C 2 342 ? 164.641 129.818 104.547 1.00 12.34 ?  321 TYR C CE1   1 
ATOM   13469 C  CE2   . TYR C 2 342 ? 165.084 131.886 103.431 1.00 13.11 ?  321 TYR C CE2   1 
ATOM   13470 C  CZ    . TYR C 2 342 ? 165.236 131.061 104.525 1.00 17.37 ?  321 TYR C CZ    1 
ATOM   13471 O  OH    . TYR C 2 342 ? 165.985 131.483 105.597 1.00 21.45 ?  321 TYR C OH    1 
ATOM   13472 N  N     . PHE C 2 343 ? 160.480 130.641 99.131  1.00 12.77 ?  322 PHE C N     1 
ATOM   13473 C  CA    . PHE C 2 343 ? 159.736 130.391 97.904  1.00 15.81 ?  322 PHE C CA    1 
ATOM   13474 C  C     . PHE C 2 343 ? 160.420 131.055 96.715  1.00 24.63 ?  322 PHE C C     1 
ATOM   13475 O  O     . PHE C 2 343 ? 161.249 131.948 96.879  1.00 24.06 ?  322 PHE C O     1 
ATOM   13476 C  CB    . PHE C 2 343 ? 158.285 130.887 98.018  1.00 11.49 ?  322 PHE C CB    1 
ATOM   13477 C  CG    . PHE C 2 343 ? 157.670 130.700 99.382  1.00 8.46  ?  322 PHE C CG    1 
ATOM   13478 C  CD1   . PHE C 2 343 ? 157.960 131.566 100.426 1.00 8.80  ?  322 PHE C CD1   1 
ATOM   13479 C  CD2   . PHE C 2 343 ? 156.817 129.637 99.622  1.00 13.46 ?  322 PHE C CD2   1 
ATOM   13480 C  CE1   . PHE C 2 343 ? 157.402 131.379 101.672 1.00 5.58  ?  322 PHE C CE1   1 
ATOM   13481 C  CE2   . PHE C 2 343 ? 156.257 129.448 100.867 1.00 8.14  ?  322 PHE C CE2   1 
ATOM   13482 C  CZ    . PHE C 2 343 ? 156.550 130.318 101.892 1.00 2.41  ?  322 PHE C CZ    1 
ATOM   13483 N  N     . ASP D 2 37  ? 124.067 97.559  142.237 1.00 32.44 ?  16  ASP D N     1 
ATOM   13484 C  CA    . ASP D 2 37  ? 123.733 98.976  142.068 1.00 32.83 ?  16  ASP D CA    1 
ATOM   13485 C  C     . ASP D 2 37  ? 124.412 99.637  140.870 1.00 31.65 ?  16  ASP D C     1 
ATOM   13486 O  O     . ASP D 2 37  ? 124.119 100.796 140.565 1.00 32.65 ?  16  ASP D O     1 
ATOM   13487 C  CB    . ASP D 2 37  ? 124.120 99.778  143.320 1.00 33.73 ?  16  ASP D CB    1 
ATOM   13488 C  CG    . ASP D 2 37  ? 123.320 99.388  144.554 1.00 36.81 ?  16  ASP D CG    1 
ATOM   13489 O  OD1   . ASP D 2 37  ? 123.791 99.705  145.673 1.00 39.69 ?  16  ASP D OD1   1 
ATOM   13490 O  OD2   . ASP D 2 37  ? 122.240 98.768  144.418 1.00 39.67 -1 16  ASP D OD2   1 
ATOM   13491 N  N     . PHE D 2 38  ? 125.315 98.926  140.196 1.00 29.55 ?  17  PHE D N     1 
ATOM   13492 C  CA    . PHE D 2 38  ? 126.230 99.601  139.275 1.00 27.75 ?  17  PHE D CA    1 
ATOM   13493 C  C     . PHE D 2 38  ? 126.530 98.908  137.936 1.00 26.21 ?  17  PHE D C     1 
ATOM   13494 O  O     . PHE D 2 38  ? 126.990 99.559  137.004 1.00 25.93 ?  17  PHE D O     1 
ATOM   13495 C  CB    . PHE D 2 38  ? 127.547 99.933  140.014 1.00 27.37 ?  17  PHE D CB    1 
ATOM   13496 C  CG    . PHE D 2 38  ? 128.256 98.722  140.559 1.00 27.32 ?  17  PHE D CG    1 
ATOM   13497 C  CD1   . PHE D 2 38  ? 129.107 97.977  139.749 1.00 27.01 ?  17  PHE D CD1   1 
ATOM   13498 C  CD2   . PHE D 2 38  ? 128.074 98.324  141.877 1.00 28.02 ?  17  PHE D CD2   1 
ATOM   13499 C  CE1   . PHE D 2 38  ? 129.761 96.851  140.245 1.00 27.66 ?  17  PHE D CE1   1 
ATOM   13500 C  CE2   . PHE D 2 38  ? 128.719 97.199  142.376 1.00 27.68 ?  17  PHE D CE2   1 
ATOM   13501 C  CZ    . PHE D 2 38  ? 129.566 96.460  141.556 1.00 27.47 ?  17  PHE D CZ    1 
ATOM   13502 N  N     . THR D 2 39  ? 126.277 97.606  137.838 1.00 24.88 ?  18  THR D N     1 
ATOM   13503 C  CA    . THR D 2 39  ? 126.700 96.831  136.660 1.00 23.81 ?  18  THR D CA    1 
ATOM   13504 C  C     . THR D 2 39  ? 126.031 97.261  135.342 1.00 23.56 ?  18  THR D C     1 
ATOM   13505 O  O     . THR D 2 39  ? 126.688 97.358  134.305 1.00 23.02 ?  18  THR D O     1 
ATOM   13506 C  CB    . THR D 2 39  ? 126.596 95.307  136.911 1.00 23.40 ?  18  THR D CB    1 
ATOM   13507 O  OG1   . THR D 2 39  ? 127.713 94.888  137.705 1.00 23.77 ?  18  THR D OG1   1 
ATOM   13508 C  CG2   . THR D 2 39  ? 126.622 94.521  135.610 1.00 22.31 ?  18  THR D CG2   1 
ATOM   13509 N  N     . GLN D 2 40  ? 124.734 97.536  135.375 1.00 23.78 ?  19  GLN D N     1 
ATOM   13510 C  CA    . GLN D 2 40  ? 124.062 97.985  134.152 1.00 23.88 ?  19  GLN D CA    1 
ATOM   13511 C  C     . GLN D 2 40  ? 124.574 99.349  133.680 1.00 24.09 ?  19  GLN D C     1 
ATOM   13512 O  O     . GLN D 2 40  ? 124.791 99.554  132.493 1.00 23.15 ?  19  GLN D O     1 
ATOM   13513 C  CB    . GLN D 2 40  ? 122.541 97.970  134.309 1.00 24.53 ?  19  GLN D CB    1 
ATOM   13514 C  CG    . GLN D 2 40  ? 121.994 96.556  134.430 1.00 24.06 ?  19  GLN D CG    1 
ATOM   13515 C  CD    . GLN D 2 40  ? 120.515 96.457  134.136 1.00 25.83 ?  19  GLN D CD    1 
ATOM   13516 O  OE1   . GLN D 2 40  ? 119.914 97.392  133.612 1.00 25.90 ?  19  GLN D OE1   1 
ATOM   13517 N  NE2   . GLN D 2 40  ? 119.923 95.305  134.452 1.00 23.56 ?  19  GLN D NE2   1 
ATOM   13518 N  N     . MET D 2 41  ? 124.810 100.261 134.614 1.00 24.07 ?  20  MET D N     1 
ATOM   13519 C  CA    . MET D 2 41  ? 125.430 101.543 134.277 1.00 25.53 ?  20  MET D CA    1 
ATOM   13520 C  C     . MET D 2 41  ? 126.816 101.376 133.622 1.00 24.24 ?  20  MET D C     1 
ATOM   13521 O  O     . MET D 2 41  ? 127.121 102.042 132.628 1.00 23.16 ?  20  MET D O     1 
ATOM   13522 C  CB    . MET D 2 41  ? 125.515 102.428 135.526 1.00 26.79 ?  20  MET D CB    1 
ATOM   13523 C  CG    . MET D 2 41  ? 126.169 103.778 135.307 1.00 32.62 ?  20  MET D CG    1 
ATOM   13524 S  SD    . MET D 2 41  ? 126.507 104.567 136.899 1.00 44.01 ?  20  MET D SD    1 
ATOM   13525 C  CE    . MET D 2 41  ? 127.864 105.659 136.464 1.00 41.93 ?  20  MET D CE    1 
ATOM   13526 N  N     . PHE D 2 42  ? 127.645 100.482 134.165 1.00 23.31 ?  21  PHE D N     1 
ATOM   13527 C  CA    . PHE D 2 42  ? 128.965 100.245 133.582 1.00 23.44 ?  21  PHE D CA    1 
ATOM   13528 C  C     . PHE D 2 42  ? 128.880 99.522  132.252 1.00 23.55 ?  21  PHE D C     1 
ATOM   13529 O  O     . PHE D 2 42  ? 129.687 99.770  131.363 1.00 23.74 ?  21  PHE D O     1 
ATOM   13530 C  CB    . PHE D 2 42  ? 129.888 99.505  134.552 1.00 22.97 ?  21  PHE D CB    1 
ATOM   13531 C  CG    . PHE D 2 42  ? 130.598 100.421 135.486 1.00 23.86 ?  21  PHE D CG    1 
ATOM   13532 C  CD1   . PHE D 2 42  ? 131.884 100.870 135.196 1.00 24.55 ?  21  PHE D CD1   1 
ATOM   13533 C  CD2   . PHE D 2 42  ? 129.973 100.874 136.632 1.00 24.06 ?  21  PHE D CD2   1 
ATOM   13534 C  CE1   . PHE D 2 42  ? 132.544 101.746 136.061 1.00 25.78 ?  21  PHE D CE1   1 
ATOM   13535 C  CE2   . PHE D 2 42  ? 130.626 101.752 137.503 1.00 25.25 ?  21  PHE D CE2   1 
ATOM   13536 C  CZ    . PHE D 2 42  ? 131.902 102.189 137.217 1.00 25.79 ?  21  PHE D CZ    1 
ATOM   13537 N  N     . TYR D 2 43  ? 127.888 98.644  132.121 1.00 24.08 ?  22  TYR D N     1 
ATOM   13538 C  CA    . TYR D 2 43  ? 127.611 97.999  130.848 1.00 24.74 ?  22  TYR D CA    1 
ATOM   13539 C  C     . TYR D 2 43  ? 127.419 99.067  129.769 1.00 25.72 ?  22  TYR D C     1 
ATOM   13540 O  O     . TYR D 2 43  ? 128.046 99.010  128.706 1.00 25.56 ?  22  TYR D O     1 
ATOM   13541 C  CB    . TYR D 2 43  ? 126.374 97.088  130.924 1.00 24.90 ?  22  TYR D CB    1 
ATOM   13542 C  CG    . TYR D 2 43  ? 125.983 96.549  129.555 1.00 24.38 ?  22  TYR D CG    1 
ATOM   13543 C  CD1   . TYR D 2 43  ? 126.518 95.360  129.078 1.00 23.96 ?  22  TYR D CD1   1 
ATOM   13544 C  CD2   . TYR D 2 43  ? 125.122 97.268  128.721 1.00 24.73 ?  22  TYR D CD2   1 
ATOM   13545 C  CE1   . TYR D 2 43  ? 126.190 94.880  127.808 1.00 23.42 ?  22  TYR D CE1   1 
ATOM   13546 C  CE2   . TYR D 2 43  ? 124.774 96.795  127.453 1.00 26.65 ?  22  TYR D CE2   1 
ATOM   13547 C  CZ    . TYR D 2 43  ? 125.317 95.602  127.007 1.00 25.68 ?  22  TYR D CZ    1 
ATOM   13548 O  OH    . TYR D 2 43  ? 124.980 95.133  125.758 1.00 26.57 ?  22  TYR D OH    1 
ATOM   13549 N  N     . ASN D 2 44  ? 126.544 100.028 130.055 1.00 26.77 ?  23  ASN D N     1 
ATOM   13550 C  CA    . ASN D 2 44  ? 126.233 101.106 129.123 1.00 28.57 ?  23  ASN D CA    1 
ATOM   13551 C  C     . ASN D 2 44  ? 127.460 101.906 128.731 1.00 28.70 ?  23  ASN D C     1 
ATOM   13552 O  O     . ASN D 2 44  ? 127.733 102.078 127.541 1.00 28.99 ?  23  ASN D O     1 
ATOM   13553 C  CB    . ASN D 2 44  ? 125.133 102.007 129.694 1.00 29.62 ?  23  ASN D CB    1 
ATOM   13554 C  CG    . ASN D 2 44  ? 123.781 101.308 129.739 1.00 32.44 ?  23  ASN D CG    1 
ATOM   13555 O  OD1   . ASN D 2 44  ? 123.542 100.338 129.008 1.00 34.30 ?  23  ASN D OD1   1 
ATOM   13556 N  ND2   . ASN D 2 44  ? 122.888 101.792 130.600 1.00 35.17 ?  23  ASN D ND2   1 
ATOM   13557 N  N     . GLN D 2 45  ? 128.218 102.351 129.731 1.00 28.97 ?  24  GLN D N     1 
ATOM   13558 C  CA    . GLN D 2 45  ? 129.417 103.143 129.485 1.00 29.99 ?  24  GLN D CA    1 
ATOM   13559 C  C     . GLN D 2 45  ? 130.479 102.366 128.692 1.00 29.69 ?  24  GLN D C     1 
ATOM   13560 O  O     . GLN D 2 45  ? 131.123 102.925 127.805 1.00 30.01 ?  24  GLN D O     1 
ATOM   13561 C  CB    . GLN D 2 45  ? 129.996 103.687 130.797 1.00 30.27 ?  24  GLN D CB    1 
ATOM   13562 C  CG    . GLN D 2 45  ? 131.125 104.723 130.599 1.00 32.29 ?  24  GLN D CG    1 
ATOM   13563 C  CD    . GLN D 2 45  ? 130.665 105.985 129.881 1.00 35.95 ?  24  GLN D CD    1 
ATOM   13564 O  OE1   . GLN D 2 45  ? 129.495 106.372 129.957 1.00 36.72 ?  24  GLN D OE1   1 
ATOM   13565 N  NE2   . GLN D 2 45  ? 131.587 106.636 129.179 1.00 37.05 ?  24  GLN D NE2   1 
ATOM   13566 N  N     . ASN D 2 46  ? 130.638 101.079 128.996 1.00 28.93 ?  25  ASN D N     1 
ATOM   13567 C  CA    . ASN D 2 46  ? 131.574 100.236 128.271 1.00 28.70 ?  25  ASN D CA    1 
ATOM   13568 C  C     . ASN D 2 46  ? 131.233 100.072 126.795 1.00 29.05 ?  25  ASN D C     1 
ATOM   13569 O  O     . ASN D 2 46  ? 132.088 100.300 125.934 1.00 28.51 ?  25  ASN D O     1 
ATOM   13570 C  CB    . ASN D 2 46  ? 131.720 98.862  128.939 1.00 28.36 ?  25  ASN D CB    1 
ATOM   13571 C  CG    . ASN D 2 46  ? 132.783 98.855  130.016 1.00 28.45 ?  25  ASN D CG    1 
ATOM   13572 O  OD1   . ASN D 2 46  ? 133.920 98.463  129.762 1.00 28.03 ?  25  ASN D OD1   1 
ATOM   13573 N  ND2   . ASN D 2 46  ? 132.432 99.317  131.215 1.00 26.53 ?  25  ASN D ND2   1 
ATOM   13574 N  N     . VAL D 2 47  ? 129.986 99.703  126.503 1.00 29.66 ?  26  VAL D N     1 
ATOM   13575 C  CA    . VAL D 2 47  ? 129.597 99.410  125.124 1.00 31.15 ?  26  VAL D CA    1 
ATOM   13576 C  C     . VAL D 2 47  ? 129.530 100.676 124.275 1.00 32.39 ?  26  VAL D C     1 
ATOM   13577 O  O     . VAL D 2 47  ? 129.787 100.633 123.073 1.00 32.80 ?  26  VAL D O     1 
ATOM   13578 C  CB    . VAL D 2 47  ? 128.286 98.563  125.003 1.00 31.08 ?  26  VAL D CB    1 
ATOM   13579 C  CG1   . VAL D 2 47  ? 128.407 97.265  125.791 1.00 31.09 ?  26  VAL D CG1   1 
ATOM   13580 C  CG2   . VAL D 2 47  ? 127.045 99.361  125.429 1.00 30.81 ?  26  VAL D CG2   1 
ATOM   13581 N  N     . LYS D 2 48  ? 129.217 101.809 124.893 1.00 33.28 ?  27  LYS D N     1 
ATOM   13582 C  CA    . LYS D 2 48  ? 129.188 103.045 124.128 1.00 34.87 ?  27  LYS D CA    1 
ATOM   13583 C  C     . LYS D 2 48  ? 130.591 103.613 123.829 1.00 34.91 ?  27  LYS D C     1 
ATOM   13584 O  O     . LYS D 2 48  ? 130.733 104.507 122.999 1.00 34.92 ?  27  LYS D O     1 
ATOM   13585 C  CB    . LYS D 2 48  ? 128.239 104.076 124.757 1.00 35.45 ?  27  LYS D CB    1 
ATOM   13586 C  CG    . LYS D 2 48  ? 128.816 104.944 125.850 1.00 37.41 ?  27  LYS D CG    1 
ATOM   13587 C  CD    . LYS D 2 48  ? 127.898 106.153 126.093 1.00 40.91 ?  27  LYS D CD    1 
ATOM   13588 C  CE    . LYS D 2 48  ? 128.622 107.247 126.883 1.00 42.46 ?  27  LYS D CE    1 
ATOM   13589 N  NZ    . LYS D 2 48  ? 127.822 108.501 127.007 1.00 45.13 1  27  LYS D NZ    1 
ATOM   13590 N  N     . GLN D 2 49  ? 131.612 103.069 124.495 1.00 34.66 ?  28  GLN D N     1 
ATOM   13591 C  CA    . GLN D 2 49  ? 133.006 103.435 124.261 1.00 34.64 ?  28  GLN D CA    1 
ATOM   13592 C  C     . GLN D 2 49  ? 133.671 102.509 123.244 1.00 34.20 ?  28  GLN D C     1 
ATOM   13593 O  O     . GLN D 2 49  ? 134.885 102.585 123.049 1.00 34.53 ?  28  GLN D O     1 
ATOM   13594 C  CB    . GLN D 2 49  ? 133.811 103.400 125.575 1.00 34.89 ?  28  GLN D CB    1 
ATOM   13595 C  CG    . GLN D 2 49  ? 133.779 104.693 126.386 1.00 36.47 ?  28  GLN D CG    1 
ATOM   13596 C  CD    . GLN D 2 49  ? 134.420 104.562 127.770 1.00 38.37 ?  28  GLN D CD    1 
ATOM   13597 O  OE1   . GLN D 2 49  ? 134.004 105.234 128.715 1.00 40.68 ?  28  GLN D OE1   1 
ATOM   13598 N  NE2   . GLN D 2 49  ? 135.429 103.699 127.896 1.00 38.57 ?  28  GLN D NE2   1 
ATOM   13599 N  N     . PHE D 2 50  ? 132.895 101.634 122.603 1.00 33.42 ?  29  PHE D N     1 
ATOM   13600 C  CA    . PHE D 2 50  ? 133.468 100.657 121.679 1.00 32.57 ?  29  PHE D CA    1 
ATOM   13601 C  C     . PHE D 2 50  ? 134.148 101.367 120.508 1.00 32.60 ?  29  PHE D C     1 
ATOM   13602 O  O     . PHE D 2 50  ? 133.633 102.358 119.981 1.00 32.39 ?  29  PHE D O     1 
ATOM   13603 C  CB    . PHE D 2 50  ? 132.417 99.651  121.182 1.00 32.77 ?  29  PHE D CB    1 
ATOM   13604 C  CG    . PHE D 2 50  ? 132.972 98.596  120.246 1.00 32.24 ?  29  PHE D CG    1 
ATOM   13605 C  CD1   . PHE D 2 50  ? 133.733 97.538  120.734 1.00 31.50 ?  29  PHE D CD1   1 
ATOM   13606 C  CD2   . PHE D 2 50  ? 132.733 98.666  118.878 1.00 33.60 ?  29  PHE D CD2   1 
ATOM   13607 C  CE1   . PHE D 2 50  ? 134.246 96.572  119.882 1.00 33.02 ?  29  PHE D CE1   1 
ATOM   13608 C  CE2   . PHE D 2 50  ? 133.246 97.702  118.008 1.00 33.78 ?  29  PHE D CE2   1 
ATOM   13609 C  CZ    . PHE D 2 50  ? 133.997 96.650  118.510 1.00 33.13 ?  29  PHE D CZ    1 
ATOM   13610 N  N     . TRP D 2 51  ? 135.310 100.857 120.121 1.00 31.95 ?  30  TRP D N     1 
ATOM   13611 C  CA    . TRP D 2 51  ? 136.093 101.424 119.023 1.00 32.03 ?  30  TRP D CA    1 
ATOM   13612 C  C     . TRP D 2 51  ? 136.957 100.333 118.404 1.00 33.03 ?  30  TRP D C     1 
ATOM   13613 O  O     . TRP D 2 51  ? 137.094 99.244  118.965 1.00 32.54 ?  30  TRP D O     1 
ATOM   13614 C  CB    . TRP D 2 51  ? 136.950 102.607 119.502 1.00 31.19 ?  30  TRP D CB    1 
ATOM   13615 C  CG    . TRP D 2 51  ? 137.964 102.243 120.567 1.00 28.11 ?  30  TRP D CG    1 
ATOM   13616 C  CD1   . TRP D 2 51  ? 137.724 102.066 121.894 1.00 26.51 ?  30  TRP D CD1   1 
ATOM   13617 C  CD2   . TRP D 2 51  ? 139.369 102.008 120.378 1.00 25.93 ?  30  TRP D CD2   1 
ATOM   13618 N  NE1   . TRP D 2 51  ? 138.893 101.741 122.552 1.00 24.52 ?  30  TRP D NE1   1 
ATOM   13619 C  CE2   . TRP D 2 51  ? 139.915 101.696 121.645 1.00 24.42 ?  30  TRP D CE2   1 
ATOM   13620 C  CE3   . TRP D 2 51  ? 140.221 102.037 119.264 1.00 25.37 ?  30  TRP D CE3   1 
ATOM   13621 C  CZ2   . TRP D 2 51  ? 141.277 101.419 121.830 1.00 24.00 ?  30  TRP D CZ2   1 
ATOM   13622 C  CZ3   . TRP D 2 51  ? 141.574 101.753 119.448 1.00 24.99 ?  30  TRP D CZ3   1 
ATOM   13623 C  CH2   . TRP D 2 51  ? 142.087 101.447 120.721 1.00 23.72 ?  30  TRP D CH2   1 
ATOM   13624 N  N     . LEU D 2 52  ? 137.520 100.632 117.238 1.00 34.81 ?  31  LEU D N     1 
ATOM   13625 C  CA    . LEU D 2 52  ? 138.357 99.697  116.501 1.00 36.58 ?  31  LEU D CA    1 
ATOM   13626 C  C     . LEU D 2 52  ? 139.634 100.392 116.037 1.00 37.80 ?  31  LEU D C     1 
ATOM   13627 O  O     . LEU D 2 52  ? 139.609 101.583 115.740 1.00 37.92 ?  31  LEU D O     1 
ATOM   13628 C  CB    . LEU D 2 52  ? 137.589 99.118  115.302 1.00 36.95 ?  31  LEU D CB    1 
ATOM   13629 C  CG    . LEU D 2 52  ? 136.608 97.964  115.535 1.00 38.15 ?  31  LEU D CG    1 
ATOM   13630 C  CD1   . LEU D 2 52  ? 136.231 97.319  114.206 1.00 39.50 ?  31  LEU D CD1   1 
ATOM   13631 C  CD2   . LEU D 2 52  ? 137.180 96.906  116.472 1.00 37.94 ?  31  LEU D CD2   1 
ATOM   13632 N  N     . PRO D 2 53  ? 140.757 99.650  115.966 1.00 39.26 ?  32  PRO D N     1 
ATOM   13633 C  CA    . PRO D 2 53  ? 142.054 100.215 115.550 1.00 40.41 ?  32  PRO D CA    1 
ATOM   13634 C  C     . PRO D 2 53  ? 142.009 100.929 114.192 1.00 41.91 ?  32  PRO D C     1 
ATOM   13635 O  O     . PRO D 2 53  ? 142.552 102.030 114.051 1.00 42.52 ?  32  PRO D O     1 
ATOM   13636 C  CB    . PRO D 2 53  ? 142.958 98.980  115.451 1.00 40.42 ?  32  PRO D CB    1 
ATOM   13637 C  CG    . PRO D 2 53  ? 142.306 97.953  116.287 1.00 40.01 ?  32  PRO D CG    1 
ATOM   13638 C  CD    . PRO D 2 53  ? 140.840 98.199  116.209 1.00 39.30 ?  32  PRO D CD    1 
ATOM   13639 N  N     . GLU D 2 54  ? 141.348 100.309 113.218 1.00 43.27 ?  33  GLU D N     1 
ATOM   13640 C  CA    . GLU D 2 54  ? 141.237 100.826 111.844 1.00 45.17 ?  33  GLU D CA    1 
ATOM   13641 C  C     . GLU D 2 54  ? 140.715 102.267 111.723 1.00 45.57 ?  33  GLU D C     1 
ATOM   13642 O  O     . GLU D 2 54  ? 140.946 102.930 110.707 1.00 46.08 ?  33  GLU D O     1 
ATOM   13643 C  CB    . GLU D 2 54  ? 140.355 99.890  111.004 1.00 45.55 ?  33  GLU D CB    1 
ATOM   13644 C  CG    . GLU D 2 54  ? 141.069 98.651  110.456 1.00 48.19 ?  33  GLU D CG    1 
ATOM   13645 C  CD    . GLU D 2 54  ? 141.572 97.706  111.539 1.00 50.61 ?  33  GLU D CD    1 
ATOM   13646 O  OE1   . GLU D 2 54  ? 140.793 97.382  112.467 1.00 51.10 ?  33  GLU D OE1   1 
ATOM   13647 O  OE2   . GLU D 2 54  ? 142.753 97.291  111.458 1.00 52.64 -1 33  GLU D OE2   1 
ATOM   13648 N  N     . GLU D 2 55  ? 140.017 102.740 112.754 1.00 45.74 ?  34  GLU D N     1 
ATOM   13649 C  CA    . GLU D 2 55  ? 139.408 104.077 112.747 1.00 46.28 ?  34  GLU D CA    1 
ATOM   13650 C  C     . GLU D 2 55  ? 140.439 105.213 112.727 1.00 46.49 ?  34  GLU D C     1 
ATOM   13651 O  O     . GLU D 2 55  ? 140.173 106.290 112.186 1.00 46.73 ?  34  GLU D O     1 
ATOM   13652 C  CB    . GLU D 2 55  ? 138.457 104.249 113.936 1.00 46.17 ?  34  GLU D CB    1 
ATOM   13653 C  CG    . GLU D 2 55  ? 137.246 103.312 113.934 1.00 47.10 ?  34  GLU D CG    1 
ATOM   13654 C  CD    . GLU D 2 55  ? 136.307 103.573 115.110 1.00 48.43 ?  34  GLU D CD    1 
ATOM   13655 O  OE1   . GLU D 2 55  ? 135.733 104.682 115.186 1.00 49.62 ?  34  GLU D OE1   1 
ATOM   13656 O  OE2   . GLU D 2 55  ? 136.140 102.670 115.957 1.00 47.11 -1 34  GLU D OE2   1 
ATOM   13657 N  N     . ILE D 2 56  ? 141.606 104.969 113.322 1.00 46.23 ?  35  ILE D N     1 
ATOM   13658 C  CA    . ILE D 2 56  ? 142.685 105.954 113.344 1.00 46.25 ?  35  ILE D CA    1 
ATOM   13659 C  C     . ILE D 2 56  ? 143.746 105.569 112.314 1.00 46.30 ?  35  ILE D C     1 
ATOM   13660 O  O     . ILE D 2 56  ? 144.330 104.483 112.392 1.00 46.36 ?  35  ILE D O     1 
ATOM   13661 C  CB    . ILE D 2 56  ? 143.346 106.072 114.762 1.00 45.84 ?  35  ILE D CB    1 
ATOM   13662 C  CG1   . ILE D 2 56  ? 142.302 106.059 115.898 1.00 46.15 ?  35  ILE D CG1   1 
ATOM   13663 C  CG2   . ILE D 2 56  ? 144.289 107.291 114.839 1.00 45.72 ?  35  ILE D CG2   1 
ATOM   13664 C  CD1   . ILE D 2 56  ? 141.312 107.218 115.907 1.00 47.27 ?  35  ILE D CD1   1 
ATOM   13665 N  N     . ALA D 2 57  ? 143.986 106.449 111.347 1.00 46.51 ?  36  ALA D N     1 
ATOM   13666 C  CA    . ALA D 2 57  ? 145.066 106.255 110.377 1.00 46.56 ?  36  ALA D CA    1 
ATOM   13667 C  C     . ALA D 2 57  ? 146.405 106.589 111.040 1.00 46.08 ?  36  ALA D C     1 
ATOM   13668 O  O     . ALA D 2 57  ? 146.567 107.680 111.587 1.00 45.70 ?  36  ALA D O     1 
ATOM   13669 C  CB    . ALA D 2 57  ? 144.843 107.123 109.141 1.00 47.10 ?  36  ALA D CB    1 
ATOM   13670 N  N     . LEU D 2 58  ? 147.357 105.660 110.978 1.00 45.66 ?  37  LEU D N     1 
ATOM   13671 C  CA    . LEU D 2 58  ? 148.624 105.808 111.711 1.00 45.27 ?  37  LEU D CA    1 
ATOM   13672 C  C     . LEU D 2 58  ? 149.800 106.394 110.933 1.00 45.25 ?  37  LEU D C     1 
ATOM   13673 O  O     . LEU D 2 58  ? 150.748 106.909 111.534 1.00 44.82 ?  37  LEU D O     1 
ATOM   13674 C  CB    . LEU D 2 58  ? 149.039 104.476 112.333 1.00 45.05 ?  37  LEU D CB    1 
ATOM   13675 C  CG    . LEU D 2 58  ? 148.296 104.110 113.616 1.00 45.41 ?  37  LEU D CG    1 
ATOM   13676 C  CD1   . LEU D 2 58  ? 148.743 102.743 114.098 1.00 45.40 ?  37  LEU D CD1   1 
ATOM   13677 C  CD2   . LEU D 2 58  ? 148.519 105.167 114.696 1.00 44.70 ?  37  LEU D CD2   1 
ATOM   13678 N  N     . ASN D 2 59  ? 149.736 106.331 109.605 1.00 45.33 ?  38  ASN D N     1 
ATOM   13679 C  CA    . ASN D 2 59  ? 150.900 106.646 108.771 1.00 45.22 ?  38  ASN D CA    1 
ATOM   13680 C  C     . ASN D 2 59  ? 151.479 108.058 108.941 1.00 44.39 ?  38  ASN D C     1 
ATOM   13681 O  O     . ASN D 2 59  ? 152.695 108.247 108.823 1.00 44.33 ?  38  ASN D O     1 
ATOM   13682 C  CB    . ASN D 2 59  ? 150.598 106.356 107.303 1.00 46.22 ?  38  ASN D CB    1 
ATOM   13683 C  CG    . ASN D 2 59  ? 151.808 105.827 106.554 1.00 47.90 ?  38  ASN D CG    1 
ATOM   13684 O  OD1   . ASN D 2 59  ? 152.288 106.450 105.609 1.00 49.28 ?  38  ASN D OD1   1 
ATOM   13685 N  ND2   . ASN D 2 59  ? 152.308 104.664 106.977 1.00 49.18 ?  38  ASN D ND2   1 
ATOM   13686 N  N     . GLY D 2 60  ? 150.614 109.029 109.240 1.00 43.45 ?  39  GLY D N     1 
ATOM   13687 C  CA    . GLY D 2 60  ? 151.026 110.421 109.446 1.00 42.42 ?  39  GLY D CA    1 
ATOM   13688 C  C     . GLY D 2 60  ? 151.909 110.686 110.664 1.00 41.55 ?  39  GLY D C     1 
ATOM   13689 O  O     . GLY D 2 60  ? 152.419 111.797 110.840 1.00 41.29 ?  39  GLY D O     1 
ATOM   13690 N  N     . ASP D 2 61  ? 152.085 109.675 111.513 1.00 40.35 ?  40  ASP D N     1 
ATOM   13691 C  CA    . ASP D 2 61  ? 153.005 109.778 112.651 1.00 39.53 ?  40  ASP D CA    1 
ATOM   13692 C  C     . ASP D 2 61  ? 154.471 109.778 112.237 1.00 39.38 ?  40  ASP D C     1 
ATOM   13693 O  O     . ASP D 2 61  ? 155.325 110.278 112.965 1.00 38.90 ?  40  ASP D O     1 
ATOM   13694 C  CB    . ASP D 2 61  ? 152.766 108.643 113.635 1.00 38.93 ?  40  ASP D CB    1 
ATOM   13695 C  CG    . ASP D 2 61  ? 151.673 108.951 114.618 1.00 38.21 ?  40  ASP D CG    1 
ATOM   13696 O  OD1   . ASP D 2 61  ? 151.098 110.061 114.565 1.00 38.79 ?  40  ASP D OD1   1 
ATOM   13697 O  OD2   . ASP D 2 61  ? 151.395 108.079 115.457 1.00 38.02 -1 40  ASP D OD2   1 
ATOM   13698 N  N     . LEU D 2 62  ? 154.750 109.215 111.067 1.00 39.82 ?  41  LEU D N     1 
ATOM   13699 C  CA    . LEU D 2 62  ? 156.110 109.130 110.550 1.00 40.22 ?  41  LEU D CA    1 
ATOM   13700 C  C     . LEU D 2 62  ? 156.707 110.513 110.292 1.00 40.40 ?  41  LEU D C     1 
ATOM   13701 O  O     . LEU D 2 62  ? 157.928 110.665 110.237 1.00 40.91 ?  41  LEU D O     1 
ATOM   13702 C  CB    . LEU D 2 62  ? 156.141 108.267 109.285 1.00 40.52 ?  41  LEU D CB    1 
ATOM   13703 C  CG    . LEU D 2 62  ? 155.791 106.786 109.470 1.00 41.03 ?  41  LEU D CG    1 
ATOM   13704 C  CD1   . LEU D 2 62  ? 155.763 106.069 108.127 1.00 42.53 ?  41  LEU D CD1   1 
ATOM   13705 C  CD2   . LEU D 2 62  ? 156.758 106.096 110.441 1.00 41.89 ?  41  LEU D CD2   1 
ATOM   13706 N  N     . LEU D 2 63  ? 155.831 111.514 110.162 1.00 40.20 ?  42  LEU D N     1 
ATOM   13707 C  CA    . LEU D 2 63  ? 156.214 112.906 109.934 1.00 39.85 ?  42  LEU D CA    1 
ATOM   13708 C  C     . LEU D 2 63  ? 156.738 113.611 111.200 1.00 38.90 ?  42  LEU D C     1 
ATOM   13709 O  O     . LEU D 2 63  ? 157.358 114.678 111.115 1.00 39.48 ?  42  LEU D O     1 
ATOM   13710 C  CB    . LEU D 2 63  ? 155.023 113.673 109.337 1.00 40.50 ?  42  LEU D CB    1 
ATOM   13711 C  CG    . LEU D 2 63  ? 154.451 113.345 107.949 1.00 41.98 ?  42  LEU D CG    1 
ATOM   13712 C  CD1   . LEU D 2 63  ? 153.186 114.138 107.637 1.00 43.07 ?  42  LEU D CD1   1 
ATOM   13713 C  CD2   . LEU D 2 63  ? 155.499 113.634 106.888 1.00 43.17 ?  42  LEU D CD2   1 
ATOM   13714 N  N     . THR D 2 64  ? 156.486 113.035 112.373 1.00 37.28 ?  43  THR D N     1 
ATOM   13715 C  CA    . THR D 2 64  ? 157.092 113.556 113.608 1.00 35.53 ?  43  THR D CA    1 
ATOM   13716 C  C     . THR D 2 64  ? 158.083 112.573 114.219 1.00 34.57 ?  43  THR D C     1 
ATOM   13717 O  O     . THR D 2 64  ? 159.040 112.981 114.882 1.00 34.23 ?  43  THR D O     1 
ATOM   13718 C  CB    . THR D 2 64  ? 156.055 113.996 114.666 1.00 35.18 ?  43  THR D CB    1 
ATOM   13719 O  OG1   . THR D 2 64  ? 155.064 112.979 114.847 1.00 34.59 ?  43  THR D OG1   1 
ATOM   13720 C  CG2   . THR D 2 64  ? 155.385 115.275 114.245 1.00 35.48 ?  43  THR D CG2   1 
ATOM   13721 N  N     . TRP D 2 65  ? 157.849 111.283 113.978 1.00 33.62 ?  44  TRP D N     1 
ATOM   13722 C  CA    . TRP D 2 65  ? 158.724 110.204 114.462 1.00 32.87 ?  44  TRP D CA    1 
ATOM   13723 C  C     . TRP D 2 65  ? 160.168 110.376 113.971 1.00 33.46 ?  44  TRP D C     1 
ATOM   13724 O  O     . TRP D 2 65  ? 161.116 110.214 114.742 1.00 32.58 ?  44  TRP D O     1 
ATOM   13725 C  CB    . TRP D 2 65  ? 158.165 108.842 114.021 1.00 32.09 ?  44  TRP D CB    1 
ATOM   13726 C  CG    . TRP D 2 65  ? 159.009 107.657 114.400 1.00 30.42 ?  44  TRP D CG    1 
ATOM   13727 C  CD1   . TRP D 2 65  ? 159.787 106.907 113.562 1.00 29.35 ?  44  TRP D CD1   1 
ATOM   13728 C  CD2   . TRP D 2 65  ? 159.157 107.081 115.707 1.00 28.04 ?  44  TRP D CD2   1 
ATOM   13729 N  NE1   . TRP D 2 65  ? 160.407 105.901 114.264 1.00 28.44 ?  44  TRP D NE1   1 
ATOM   13730 C  CE2   . TRP D 2 65  ? 160.042 105.987 115.582 1.00 28.14 ?  44  TRP D CE2   1 
ATOM   13731 C  CE3   . TRP D 2 65  ? 158.635 107.387 116.971 1.00 27.11 ?  44  TRP D CE3   1 
ATOM   13732 C  CZ2   . TRP D 2 65  ? 160.413 105.188 116.673 1.00 27.21 ?  44  TRP D CZ2   1 
ATOM   13733 C  CZ3   . TRP D 2 65  ? 158.998 106.586 118.058 1.00 27.45 ?  44  TRP D CZ3   1 
ATOM   13734 C  CH2   . TRP D 2 65  ? 159.875 105.496 117.895 1.00 27.25 ?  44  TRP D CH2   1 
ATOM   13735 N  N     . LYS D 2 66  ? 160.310 110.709 112.689 1.00 34.52 ?  45  LYS D N     1 
ATOM   13736 C  CA    . LYS D 2 66  ? 161.610 110.932 112.063 1.00 36.41 ?  45  LYS D CA    1 
ATOM   13737 C  C     . LYS D 2 66  ? 162.417 112.066 112.694 1.00 36.26 ?  45  LYS D C     1 
ATOM   13738 O  O     . LYS D 2 66  ? 163.638 112.108 112.544 1.00 36.52 ?  45  LYS D O     1 
ATOM   13739 C  CB    . LYS D 2 66  ? 161.446 111.182 110.558 1.00 36.98 ?  45  LYS D CB    1 
ATOM   13740 C  CG    . LYS D 2 66  ? 161.781 109.973 109.688 1.00 40.03 ?  45  LYS D CG    1 
ATOM   13741 C  CD    . LYS D 2 66  ? 160.745 108.850 109.814 1.00 43.70 ?  45  LYS D CD    1 
ATOM   13742 C  CE    . LYS D 2 66  ? 161.078 107.676 108.889 1.00 45.57 ?  45  LYS D CE    1 
ATOM   13743 N  NZ    . LYS D 2 66  ? 161.071 108.056 107.445 1.00 46.59 1  45  LYS D NZ    1 
ATOM   13744 N  N     . TYR D 2 67  ? 161.740 112.963 113.405 1.00 36.26 ?  46  TYR D N     1 
ATOM   13745 C  CA    . TYR D 2 67  ? 162.419 114.102 114.031 1.00 36.90 ?  46  TYR D CA    1 
ATOM   13746 C  C     . TYR D 2 67  ? 162.809 113.899 115.497 1.00 36.28 ?  46  TYR D C     1 
ATOM   13747 O  O     . TYR D 2 67  ? 163.404 114.787 116.099 1.00 36.44 ?  46  TYR D O     1 
ATOM   13748 C  CB    . TYR D 2 67  ? 161.612 115.394 113.860 1.00 37.15 ?  46  TYR D CB    1 
ATOM   13749 C  CG    . TYR D 2 67  ? 161.321 115.740 112.419 1.00 39.40 ?  46  TYR D CG    1 
ATOM   13750 C  CD1   . TYR D 2 67  ? 162.310 115.622 111.439 1.00 41.26 ?  46  TYR D CD1   1 
ATOM   13751 C  CD2   . TYR D 2 67  ? 160.069 116.210 112.037 1.00 41.06 ?  46  TYR D CD2   1 
ATOM   13752 C  CE1   . TYR D 2 67  ? 162.048 115.938 110.106 1.00 43.03 ?  46  TYR D CE1   1 
ATOM   13753 C  CE2   . TYR D 2 67  ? 159.796 116.537 110.707 1.00 43.05 ?  46  TYR D CE2   1 
ATOM   13754 C  CZ    . TYR D 2 67  ? 160.787 116.400 109.748 1.00 43.80 ?  46  TYR D CZ    1 
ATOM   13755 O  OH    . TYR D 2 67  ? 160.513 116.720 108.430 1.00 45.18 ?  46  TYR D OH    1 
ATOM   13756 N  N     . LEU D 2 68  ? 162.471 112.746 116.072 1.00 35.71 ?  47  LEU D N     1 
ATOM   13757 C  CA    . LEU D 2 68  ? 162.876 112.448 117.447 1.00 34.92 ?  47  LEU D CA    1 
ATOM   13758 C  C     . LEU D 2 68  ? 164.313 111.918 117.486 1.00 34.32 ?  47  LEU D C     1 
ATOM   13759 O  O     . LEU D 2 68  ? 164.763 111.248 116.554 1.00 34.50 ?  47  LEU D O     1 
ATOM   13760 C  CB    . LEU D 2 68  ? 161.919 111.446 118.111 1.00 35.00 ?  47  LEU D CB    1 
ATOM   13761 C  CG    . LEU D 2 68  ? 160.405 111.718 118.095 1.00 35.82 ?  47  LEU D CG    1 
ATOM   13762 C  CD1   . LEU D 2 68  ? 159.667 110.597 118.812 1.00 35.95 ?  47  LEU D CD1   1 
ATOM   13763 C  CD2   . LEU D 2 68  ? 160.037 113.072 118.702 1.00 35.97 ?  47  LEU D CD2   1 
ATOM   13764 N  N     . GLY D 2 69  ? 165.023 112.224 118.571 1.00 33.50 ?  48  GLY D N     1 
ATOM   13765 C  CA    . GLY D 2 69  ? 166.343 111.655 118.829 1.00 32.41 ?  48  GLY D CA    1 
ATOM   13766 C  C     . GLY D 2 69  ? 166.292 110.159 119.105 1.00 32.15 ?  48  GLY D C     1 
ATOM   13767 O  O     . GLY D 2 69  ? 165.217 109.591 119.337 1.00 30.98 ?  48  GLY D O     1 
ATOM   13768 N  N     . LYS D 2 70  ? 167.462 109.524 119.087 1.00 32.14 ?  49  LYS D N     1 
ATOM   13769 C  CA    . LYS D 2 70  ? 167.572 108.091 119.344 1.00 32.25 ?  49  LYS D CA    1 
ATOM   13770 C  C     . LYS D 2 70  ? 167.055 107.702 120.728 1.00 31.24 ?  49  LYS D C     1 
ATOM   13771 O  O     . LYS D 2 70  ? 166.359 106.697 120.851 1.00 31.34 ?  49  LYS D O     1 
ATOM   13772 C  CB    . LYS D 2 70  ? 169.014 107.611 119.165 1.00 33.07 ?  49  LYS D CB    1 
ATOM   13773 C  CG    . LYS D 2 70  ? 169.552 107.790 117.753 1.00 35.74 ?  49  LYS D CG    1 
ATOM   13774 C  CD    . LYS D 2 70  ? 171.061 107.564 117.730 1.00 39.67 ?  49  LYS D CD    1 
ATOM   13775 C  CE    . LYS D 2 70  ? 171.674 108.047 116.425 1.00 40.96 ?  49  LYS D CE    1 
ATOM   13776 N  NZ    . LYS D 2 70  ? 173.152 108.095 116.545 1.00 42.55 1  49  LYS D NZ    1 
ATOM   13777 N  N     . ASN D 2 71  ? 167.383 108.496 121.753 1.00 29.92 ?  50  ASN D N     1 
ATOM   13778 C  CA    . ASN D 2 71  ? 166.921 108.223 123.119 1.00 29.37 ?  50  ASN D CA    1 
ATOM   13779 C  C     . ASN D 2 71  ? 165.403 108.311 123.234 1.00 28.35 ?  50  ASN D C     1 
ATOM   13780 O  O     . ASN D 2 71  ? 164.786 107.488 123.922 1.00 27.64 ?  50  ASN D O     1 
ATOM   13781 C  CB    . ASN D 2 71  ? 167.580 109.148 124.160 1.00 29.38 ?  50  ASN D CB    1 
ATOM   13782 C  CG    . ASN D 2 71  ? 169.024 108.761 124.475 1.00 31.22 ?  50  ASN D CG    1 
ATOM   13783 O  OD1   . ASN D 2 71  ? 169.404 107.590 124.415 1.00 33.03 ?  50  ASN D OD1   1 
ATOM   13784 N  ND2   . ASN D 2 71  ? 169.834 109.754 124.826 1.00 31.97 ?  50  ASN D ND2   1 
ATOM   13785 N  N     . GLU D 2 72  ? 164.810 109.294 122.552 1.00 27.72 ?  51  GLU D N     1 
ATOM   13786 C  CA    . GLU D 2 72  ? 163.348 109.449 122.537 1.00 27.70 ?  51  GLU D CA    1 
ATOM   13787 C  C     . GLU D 2 72  ? 162.663 108.263 121.852 1.00 27.62 ?  51  GLU D C     1 
ATOM   13788 O  O     . GLU D 2 72  ? 161.645 107.756 122.335 1.00 27.56 ?  51  GLU D O     1 
ATOM   13789 C  CB    . GLU D 2 72  ? 162.930 110.751 121.845 1.00 27.55 ?  51  GLU D CB    1 
ATOM   13790 C  CG    . GLU D 2 72  ? 163.480 112.032 122.485 1.00 28.77 ?  51  GLU D CG    1 
ATOM   13791 C  CD    . GLU D 2 72  ? 162.920 113.276 121.819 1.00 31.18 ?  51  GLU D CD    1 
ATOM   13792 O  OE1   . GLU D 2 72  ? 163.315 113.567 120.670 1.00 33.17 ?  51  GLU D OE1   1 
ATOM   13793 O  OE2   . GLU D 2 72  ? 162.078 113.954 122.440 1.00 31.66 -1 51  GLU D OE2   1 
ATOM   13794 N  N     . GLN D 2 73  ? 163.229 107.828 120.730 1.00 27.32 ?  52  GLN D N     1 
ATOM   13795 C  CA    . GLN D 2 73  ? 162.686 106.700 119.980 1.00 27.33 ?  52  GLN D CA    1 
ATOM   13796 C  C     . GLN D 2 73  ? 162.838 105.407 120.784 1.00 26.85 ?  52  GLN D C     1 
ATOM   13797 O  O     . GLN D 2 73  ? 161.914 104.589 120.836 1.00 26.24 ?  52  GLN D O     1 
ATOM   13798 C  CB    . GLN D 2 73  ? 163.360 106.581 118.619 1.00 27.65 ?  52  GLN D CB    1 
ATOM   13799 C  CG    . GLN D 2 73  ? 162.944 107.655 117.595 1.00 29.66 ?  52  GLN D CG    1 
ATOM   13800 C  CD    . GLN D 2 73  ? 163.490 107.388 116.192 1.00 32.60 ?  52  GLN D CD    1 
ATOM   13801 O  OE1   . GLN D 2 73  ? 164.458 106.653 116.020 1.00 34.76 ?  52  GLN D OE1   1 
ATOM   13802 N  NE2   . GLN D 2 73  ? 162.877 108.002 115.191 1.00 33.42 ?  52  GLN D NE2   1 
ATOM   13803 N  N     . ASP D 2 74  ? 163.990 105.258 121.434 1.00 26.26 ?  53  ASP D N     1 
ATOM   13804 C  CA    . ASP D 2 74  ? 164.293 104.104 122.289 1.00 26.50 ?  53  ASP D CA    1 
ATOM   13805 C  C     . ASP D 2 74  ? 163.340 104.027 123.473 1.00 25.81 ?  53  ASP D C     1 
ATOM   13806 O  O     . ASP D 2 74  ? 162.782 102.969 123.752 1.00 26.12 ?  53  ASP D O     1 
ATOM   13807 C  CB    . ASP D 2 74  ? 165.741 104.196 122.792 1.00 26.84 ?  53  ASP D CB    1 
ATOM   13808 C  CG    . ASP D 2 74  ? 166.191 102.959 123.569 1.00 29.50 ?  53  ASP D CG    1 
ATOM   13809 O  OD1   . ASP D 2 74  ? 166.255 101.856 122.986 1.00 32.08 ?  53  ASP D OD1   1 
ATOM   13810 O  OD2   . ASP D 2 74  ? 166.529 103.102 124.761 1.00 33.52 -1 53  ASP D OD2   1 
ATOM   13811 N  N     . THR D 2 75  ? 163.149 105.146 124.170 1.00 25.10 ?  54  THR D N     1 
ATOM   13812 C  CA    . THR D 2 75  ? 162.242 105.172 125.321 1.00 24.11 ?  54  THR D CA    1 
ATOM   13813 C  C     . THR D 2 75  ? 160.814 104.831 124.886 1.00 23.82 ?  54  THR D C     1 
ATOM   13814 O  O     . THR D 2 75  ? 160.156 103.994 125.504 1.00 23.81 ?  54  THR D O     1 
ATOM   13815 C  CB    . THR D 2 75  ? 162.294 106.522 126.063 1.00 23.80 ?  54  THR D CB    1 
ATOM   13816 O  OG1   . THR D 2 75  ? 163.613 106.714 126.591 1.00 24.62 ?  54  THR D OG1   1 
ATOM   13817 C  CG2   . THR D 2 75  ? 161.279 106.555 127.219 1.00 23.25 ?  54  THR D CG2   1 
ATOM   13818 N  N     . TYR D 2 76  ? 160.344 105.490 123.836 1.00 24.06 ?  55  TYR D N     1 
ATOM   13819 C  CA    . TYR D 2 76  ? 159.016 105.224 123.291 1.00 24.76 ?  55  TYR D CA    1 
ATOM   13820 C  C     . TYR D 2 76  ? 158.794 103.741 122.963 1.00 24.85 ?  55  TYR D C     1 
ATOM   13821 O  O     . TYR D 2 76  ? 157.781 103.161 123.364 1.00 24.83 ?  55  TYR D O     1 
ATOM   13822 C  CB    . TYR D 2 76  ? 158.753 106.079 122.051 1.00 24.78 ?  55  TYR D CB    1 
ATOM   13823 C  CG    . TYR D 2 76  ? 157.278 106.231 121.738 1.00 26.19 ?  55  TYR D CG    1 
ATOM   13824 C  CD1   . TYR D 2 76  ? 156.550 107.297 122.269 1.00 27.81 ?  55  TYR D CD1   1 
ATOM   13825 C  CD2   . TYR D 2 76  ? 156.606 105.309 120.930 1.00 28.03 ?  55  TYR D CD2   1 
ATOM   13826 C  CE1   . TYR D 2 76  ? 155.198 107.455 121.995 1.00 29.32 ?  55  TYR D CE1   1 
ATOM   13827 C  CE2   . TYR D 2 76  ? 155.240 105.456 120.649 1.00 29.01 ?  55  TYR D CE2   1 
ATOM   13828 C  CZ    . TYR D 2 76  ? 154.549 106.535 121.190 1.00 30.76 ?  55  TYR D CZ    1 
ATOM   13829 O  OH    . TYR D 2 76  ? 153.210 106.718 120.933 1.00 34.50 ?  55  TYR D OH    1 
ATOM   13830 N  N     . MET D 2 77  ? 159.735 103.141 122.234 1.00 25.76 ?  56  MET D N     1 
ATOM   13831 C  CA    . MET D 2 77  ? 159.662 101.716 121.893 1.00 26.81 ?  56  MET D CA    1 
ATOM   13832 C  C     . MET D 2 77  ? 159.562 100.836 123.143 1.00 26.23 ?  56  MET D C     1 
ATOM   13833 O  O     . MET D 2 77  ? 158.729 99.930  123.211 1.00 25.00 ?  56  MET D O     1 
ATOM   13834 C  CB    . MET D 2 77  ? 160.868 101.294 121.058 1.00 28.11 ?  56  MET D CB    1 
ATOM   13835 C  CG    . MET D 2 77  ? 160.909 101.863 119.635 1.00 32.52 ?  56  MET D CG    1 
ATOM   13836 S  SD    . MET D 2 77  ? 159.709 101.124 118.514 1.00 42.68 ?  56  MET D SD    1 
ATOM   13837 C  CE    . MET D 2 77  ? 158.241 102.110 118.810 1.00 38.97 ?  56  MET D CE    1 
ATOM   13838 N  N     . LYS D 2 78  ? 160.426 101.111 124.121 1.00 26.01 ?  57  LYS D N     1 
ATOM   13839 C  CA    . LYS D 2 78  ? 160.481 100.322 125.355 1.00 26.07 ?  57  LYS D CA    1 
ATOM   13840 C  C     . LYS D 2 78  ? 159.208 100.460 126.189 1.00 25.69 ?  57  LYS D C     1 
ATOM   13841 O  O     . LYS D 2 78  ? 158.718 99.477  126.758 1.00 25.58 ?  57  LYS D O     1 
ATOM   13842 C  CB    . LYS D 2 78  ? 161.713 100.692 126.192 1.00 26.08 ?  57  LYS D CB    1 
ATOM   13843 C  CG    . LYS D 2 78  ? 163.042 100.245 125.566 1.00 27.64 ?  57  LYS D CG    1 
ATOM   13844 C  CD    . LYS D 2 78  ? 164.236 100.786 126.344 1.00 29.47 ?  57  LYS D CD    1 
ATOM   13845 C  CE    . LYS D 2 78  ? 165.529 100.163 125.840 1.00 31.69 ?  57  LYS D CE    1 
ATOM   13846 N  NZ    . LYS D 2 78  ? 166.717 100.650 126.591 1.00 33.36 1  57  LYS D NZ    1 
ATOM   13847 N  N     . VAL D 2 79  ? 158.682 101.681 126.257 1.00 25.32 ?  58  VAL D N     1 
ATOM   13848 C  CA    . VAL D 2 79  ? 157.441 101.962 126.989 1.00 25.47 ?  58  VAL D CA    1 
ATOM   13849 C  C     . VAL D 2 79  ? 156.287 101.225 126.318 1.00 25.09 ?  58  VAL D C     1 
ATOM   13850 O  O     . VAL D 2 79  ? 155.490 100.551 126.977 1.00 24.46 ?  58  VAL D O     1 
ATOM   13851 C  CB    . VAL D 2 79  ? 157.174 103.493 127.029 1.00 25.83 ?  58  VAL D CB    1 
ATOM   13852 C  CG1   . VAL D 2 79  ? 155.698 103.799 127.154 1.00 27.35 ?  58  VAL D CG1   1 
ATOM   13853 C  CG2   . VAL D 2 79  ? 157.989 104.138 128.150 1.00 26.42 ?  58  VAL D CG2   1 
ATOM   13854 N  N     . LEU D 2 80  ? 156.242 101.324 124.991 1.00 25.27 ?  59  LEU D N     1 
ATOM   13855 C  CA    . LEU D 2 80  ? 155.187 100.718 124.210 1.00 25.55 ?  59  LEU D CA    1 
ATOM   13856 C  C     . LEU D 2 80  ? 155.176 99.204  124.414 1.00 24.94 ?  59  LEU D C     1 
ATOM   13857 O  O     . LEU D 2 80  ? 154.114 98.614  124.601 1.00 24.82 ?  59  LEU D O     1 
ATOM   13858 C  CB    . LEU D 2 80  ? 155.369 101.055 122.729 1.00 25.80 ?  59  LEU D CB    1 
ATOM   13859 C  CG    . LEU D 2 80  ? 154.278 101.761 121.916 1.00 28.76 ?  59  LEU D CG    1 
ATOM   13860 C  CD1   . LEU D 2 80  ? 154.373 101.279 120.468 1.00 30.25 ?  59  LEU D CD1   1 
ATOM   13861 C  CD2   . LEU D 2 80  ? 152.867 101.563 122.446 1.00 27.79 ?  59  LEU D CD2   1 
ATOM   13862 N  N     . ALA D 2 81  ? 156.360 98.590  124.382 1.00 24.86 ?  60  ALA D N     1 
ATOM   13863 C  CA    . ALA D 2 81  ? 156.492 97.138  124.573 1.00 24.60 ?  60  ALA D CA    1 
ATOM   13864 C  C     . ALA D 2 81  ? 156.073 96.740  125.985 1.00 23.80 ?  60  ALA D C     1 
ATOM   13865 O  O     . ALA D 2 81  ? 155.446 95.707  126.186 1.00 24.07 ?  60  ALA D O     1 
ATOM   13866 C  CB    . ALA D 2 81  ? 157.924 96.686  124.291 1.00 24.48 ?  60  ALA D CB    1 
ATOM   13867 N  N     . GLY D 2 82  ? 156.419 97.574  126.958 1.00 23.54 ?  61  GLY D N     1 
ATOM   13868 C  CA    . GLY D 2 82  ? 155.998 97.369  128.340 1.00 22.53 ?  61  GLY D CA    1 
ATOM   13869 C  C     . GLY D 2 82  ? 154.489 97.322  128.460 1.00 22.23 ?  61  GLY D C     1 
ATOM   13870 O  O     . GLY D 2 82  ? 153.936 96.401  129.061 1.00 21.27 ?  61  GLY D O     1 
ATOM   13871 N  N     . LEU D 2 83  ? 153.817 98.316  127.881 1.00 22.36 ?  62  LEU D N     1 
ATOM   13872 C  CA    . LEU D 2 83  ? 152.350 98.361  127.898 1.00 22.42 ?  62  LEU D CA    1 
ATOM   13873 C  C     . LEU D 2 83  ? 151.752 97.153  127.191 1.00 22.91 ?  62  LEU D C     1 
ATOM   13874 O  O     . LEU D 2 83  ? 150.796 96.544  127.690 1.00 22.99 ?  62  LEU D O     1 
ATOM   13875 C  CB    . LEU D 2 83  ? 151.826 99.649  127.251 1.00 22.19 ?  62  LEU D CB    1 
ATOM   13876 C  CG    . LEU D 2 83  ? 152.154 100.968 127.968 1.00 22.17 ?  62  LEU D CG    1 
ATOM   13877 C  CD1   . LEU D 2 83  ? 151.875 102.152 127.033 1.00 21.55 ?  62  LEU D CD1   1 
ATOM   13878 C  CD2   . LEU D 2 83  ? 151.339 101.077 129.245 1.00 22.42 ?  62  LEU D CD2   1 
ATOM   13879 N  N     . THR D 2 84  ? 152.329 96.797  126.048 1.00 23.39 ?  63  THR D N     1 
ATOM   13880 C  CA    . THR D 2 84  ? 151.831 95.677  125.254 1.00 24.42 ?  63  THR D CA    1 
ATOM   13881 C  C     . THR D 2 84  ? 151.883 94.373  126.052 1.00 24.55 ?  63  THR D C     1 
ATOM   13882 O  O     . THR D 2 84  ? 150.894 93.640  126.129 1.00 23.68 ?  63  THR D O     1 
ATOM   13883 C  CB    . THR D 2 84  ? 152.621 95.512  123.930 1.00 24.70 ?  63  THR D CB    1 
ATOM   13884 O  OG1   . THR D 2 84  ? 152.515 96.715  123.158 1.00 25.57 ?  63  THR D OG1   1 
ATOM   13885 C  CG2   . THR D 2 84  ? 152.052 94.363  123.115 1.00 25.36 ?  63  THR D CG2   1 
ATOM   13886 N  N     . LEU D 2 85  ? 153.046 94.108  126.638 1.00 25.38 ?  64  LEU D N     1 
ATOM   13887 C  CA    . LEU D 2 85  ? 153.265 92.894  127.414 1.00 26.44 ?  64  LEU D CA    1 
ATOM   13888 C  C     . LEU D 2 85  ? 152.330 92.801  128.623 1.00 25.96 ?  64  LEU D C     1 
ATOM   13889 O  O     . LEU D 2 85  ? 151.704 91.753  128.833 1.00 25.83 ?  64  LEU D O     1 
ATOM   13890 C  CB    . LEU D 2 85  ? 154.747 92.739  127.789 1.00 26.65 ?  64  LEU D CB    1 
ATOM   13891 C  CG    . LEU D 2 85  ? 155.610 92.267  126.601 1.00 29.62 ?  64  LEU D CG    1 
ATOM   13892 C  CD1   . LEU D 2 85  ? 157.070 92.640  126.773 1.00 31.57 ?  64  LEU D CD1   1 
ATOM   13893 C  CD2   . LEU D 2 85  ? 155.479 90.751  126.359 1.00 30.96 ?  64  LEU D CD2   1 
ATOM   13894 N  N     . LEU D 2 86  ? 152.189 93.892  129.380 1.00 25.63 ?  65  LEU D N     1 
ATOM   13895 C  CA    . LEU D 2 86  ? 151.260 93.892  130.513 1.00 25.59 ?  65  LEU D CA    1 
ATOM   13896 C  C     . LEU D 2 86  ? 149.800 93.719  130.101 1.00 25.60 ?  65  LEU D C     1 
ATOM   13897 O  O     . LEU D 2 86  ? 149.028 93.042  130.787 1.00 25.47 ?  65  LEU D O     1 
ATOM   13898 C  CB    . LEU D 2 86  ? 151.426 95.141  131.400 1.00 25.76 ?  65  LEU D CB    1 
ATOM   13899 C  CG    . LEU D 2 86  ? 152.729 95.231  132.206 1.00 26.71 ?  65  LEU D CG    1 
ATOM   13900 C  CD1   . LEU D 2 86  ? 152.939 96.627  132.782 1.00 28.01 ?  65  LEU D CD1   1 
ATOM   13901 C  CD2   . LEU D 2 86  ? 152.765 94.204  133.314 1.00 28.01 ?  65  LEU D CD2   1 
ATOM   13902 N  N     . ASP D 2 87  ? 149.412 94.335  128.990 1.00 25.49 ?  66  ASP D N     1 
ATOM   13903 C  CA    . ASP D 2 87  ? 148.026 94.279  128.557 1.00 25.83 ?  66  ASP D CA    1 
ATOM   13904 C  C     . ASP D 2 87  ? 147.631 92.884  128.055 1.00 26.20 ?  66  ASP D C     1 
ATOM   13905 O  O     . ASP D 2 87  ? 146.484 92.473  128.193 1.00 25.99 ?  66  ASP D O     1 
ATOM   13906 C  CB    . ASP D 2 87  ? 147.750 95.340  127.500 1.00 25.50 ?  66  ASP D CB    1 
ATOM   13907 C  CG    . ASP D 2 87  ? 146.340 95.852  127.566 1.00 25.76 ?  66  ASP D CG    1 
ATOM   13908 O  OD1   . ASP D 2 87  ? 145.750 95.821  128.674 1.00 26.91 ?  66  ASP D OD1   1 
ATOM   13909 O  OD2   . ASP D 2 87  ? 145.812 96.288  126.524 1.00 23.11 -1 66  ASP D OD2   1 
ATOM   13910 N  N     . THR D 2 88  ? 148.599 92.160  127.497 1.00 27.12 ?  67  THR D N     1 
ATOM   13911 C  CA    . THR D 2 88  ? 148.404 90.782  127.070 1.00 28.40 ?  67  THR D CA    1 
ATOM   13912 C  C     . THR D 2 88  ? 148.095 89.875  128.250 1.00 28.28 ?  67  THR D C     1 
ATOM   13913 O  O     . THR D 2 88  ? 147.218 89.018  128.159 1.00 28.10 ?  67  THR D O     1 
ATOM   13914 C  CB    . THR D 2 88  ? 149.630 90.248  126.304 1.00 29.04 ?  67  THR D CB    1 
ATOM   13915 O  OG1   . THR D 2 88  ? 149.853 91.072  125.157 1.00 31.00 ?  67  THR D OG1   1 
ATOM   13916 C  CG2   . THR D 2 88  ? 149.392 88.815  125.834 1.00 30.16 ?  67  THR D CG2   1 
ATOM   13917 N  N     . GLU D 2 89  ? 148.807 90.062  129.360 1.00 28.28 ?  68  GLU D N     1 
ATOM   13918 C  CA    . GLU D 2 89  ? 148.505 89.307  130.571 1.00 29.16 ?  68  GLU D CA    1 
ATOM   13919 C  C     . GLU D 2 89  ? 147.069 89.584  131.013 1.00 28.65 ?  68  GLU D C     1 
ATOM   13920 O  O     . GLU D 2 89  ? 146.356 88.670  131.403 1.00 28.44 ?  68  GLU D O     1 
ATOM   13921 C  CB    . GLU D 2 89  ? 149.481 89.640  131.708 1.00 29.32 ?  68  GLU D CB    1 
ATOM   13922 C  CG    . GLU D 2 89  ? 150.953 89.332  131.400 1.00 31.95 ?  68  GLU D CG    1 
ATOM   13923 C  CD    . GLU D 2 89  ? 151.244 87.850  131.186 1.00 35.19 ?  68  GLU D CD    1 
ATOM   13924 O  OE1   . GLU D 2 89  ? 150.418 86.987  131.561 1.00 35.47 ?  68  GLU D OE1   1 
ATOM   13925 O  OE2   . GLU D 2 89  ? 152.320 87.547  130.628 1.00 38.06 -1 68  GLU D OE2   1 
ATOM   13926 N  N     . GLN D 2 90  ? 146.649 90.843  130.931 1.00 28.45 ?  69  GLN D N     1 
ATOM   13927 C  CA    . GLN D 2 90  ? 145.299 91.217  131.352 1.00 28.47 ?  69  GLN D CA    1 
ATOM   13928 C  C     . GLN D 2 90  ? 144.223 90.588  130.456 1.00 28.97 ?  69  GLN D C     1 
ATOM   13929 O  O     . GLN D 2 90  ? 143.182 90.153  130.947 1.00 28.84 ?  69  GLN D O     1 
ATOM   13930 C  CB    . GLN D 2 90  ? 145.153 92.740  131.426 1.00 28.21 ?  69  GLN D CB    1 
ATOM   13931 C  CG    . GLN D 2 90  ? 143.955 93.226  132.239 1.00 27.75 ?  69  GLN D CG    1 
ATOM   13932 C  CD    . GLN D 2 90  ? 144.102 93.025  133.743 1.00 28.91 ?  69  GLN D CD    1 
ATOM   13933 O  OE1   . GLN D 2 90  ? 144.886 92.186  134.211 1.00 27.62 ?  69  GLN D OE1   1 
ATOM   13934 N  NE2   . GLN D 2 90  ? 143.323 93.786  134.512 1.00 28.23 ?  69  GLN D NE2   1 
ATOM   13935 N  N     . GLY D 2 91  ? 144.492 90.518  129.152 1.00 29.62 ?  70  GLY D N     1 
ATOM   13936 C  CA    . GLY D 2 91  ? 143.572 89.890  128.201 1.00 30.43 ?  70  GLY D CA    1 
ATOM   13937 C  C     . GLY D 2 91  ? 143.506 88.369  128.279 1.00 31.11 ?  70  GLY D C     1 
ATOM   13938 O  O     . GLY D 2 91  ? 142.429 87.774  128.173 1.00 30.77 ?  70  GLY D O     1 
ATOM   13939 N  N     . ASN D 2 92  ? 144.655 87.733  128.453 1.00 31.69 ?  71  ASN D N     1 
ATOM   13940 C  CA    . ASN D 2 92  ? 144.691 86.277  128.505 1.00 32.72 ?  71  ASN D CA    1 
ATOM   13941 C  C     . ASN D 2 92  ? 144.346 85.668  129.857 1.00 32.60 ?  71  ASN D C     1 
ATOM   13942 O  O     . ASN D 2 92  ? 143.821 84.553  129.908 1.00 33.12 ?  71  ASN D O     1 
ATOM   13943 C  CB    . ASN D 2 92  ? 146.038 85.757  128.019 1.00 33.68 ?  71  ASN D CB    1 
ATOM   13944 C  CG    . ASN D 2 92  ? 146.209 85.917  126.522 1.00 35.15 ?  71  ASN D CG    1 
ATOM   13945 O  OD1   . ASN D 2 92  ? 147.328 86.022  126.036 1.00 40.21 ?  71  ASN D OD1   1 
ATOM   13946 N  ND2   . ASN D 2 92  ? 145.096 85.946  125.786 1.00 36.91 ?  71  ASN D ND2   1 
ATOM   13947 N  N     . THR D 2 93  ? 144.619 86.405  130.934 1.00 31.76 ?  72  THR D N     1 
ATOM   13948 C  CA    . THR D 2 93  ? 144.453 85.878  132.284 1.00 31.47 ?  72  THR D CA    1 
ATOM   13949 C  C     . THR D 2 93  ? 143.615 86.768  133.198 1.00 30.62 ?  72  THR D C     1 
ATOM   13950 O  O     . THR D 2 93  ? 142.592 86.327  133.715 1.00 30.71 ?  72  THR D O     1 
ATOM   13951 C  CB    . THR D 2 93  ? 145.810 85.613  132.931 1.00 31.60 ?  72  THR D CB    1 
ATOM   13952 O  OG1   . THR D 2 93  ? 146.566 84.737  132.084 1.00 33.14 ?  72  THR D OG1   1 
ATOM   13953 C  CG2   . THR D 2 93  ? 145.639 84.973  134.299 1.00 31.89 ?  72  THR D CG2   1 
ATOM   13954 N  N     . GLY D 2 94  ? 144.050 88.012  133.387 1.00 29.61 ?  73  GLY D N     1 
ATOM   13955 C  CA    . GLY D 2 94  ? 143.433 88.921  134.355 1.00 28.47 ?  73  GLY D CA    1 
ATOM   13956 C  C     . GLY D 2 94  ? 141.929 89.076  134.253 1.00 27.90 ?  73  GLY D C     1 
ATOM   13957 O  O     . GLY D 2 94  ? 141.200 88.866  135.233 1.00 28.27 ?  73  GLY D O     1 
ATOM   13958 N  N     . MET D 2 95  ? 141.445 89.471  133.084 1.00 26.67 ?  74  MET D N     1 
ATOM   13959 C  CA    . MET D 2 95  ? 140.002 89.651  132.945 1.00 26.00 ?  74  MET D CA    1 
ATOM   13960 C  C     . MET D 2 95  ? 139.265 88.318  132.880 1.00 25.25 ?  74  MET D C     1 
ATOM   13961 O  O     . MET D 2 95  ? 138.232 88.178  133.521 1.00 24.97 ?  74  MET D O     1 
ATOM   13962 C  CB    . MET D 2 95  ? 139.627 90.550  131.759 1.00 26.00 ?  74  MET D CB    1 
ATOM   13963 C  CG    . MET D 2 95  ? 139.786 92.025  132.037 1.00 26.40 ?  74  MET D CG    1 
ATOM   13964 S  SD    . MET D 2 95  ? 138.744 92.638  133.385 1.00 28.10 ?  74  MET D SD    1 
ATOM   13965 C  CE    . MET D 2 95  ? 139.375 94.308  133.496 1.00 28.95 ?  74  MET D CE    1 
ATOM   13966 N  N     . PRO D 2 96  ? 139.781 87.344  132.106 1.00 24.98 ?  75  PRO D N     1 
ATOM   13967 C  CA    . PRO D 2 96  ? 139.009 86.089  132.065 1.00 24.59 ?  75  PRO D CA    1 
ATOM   13968 C  C     . PRO D 2 96  ? 138.953 85.344  133.396 1.00 23.90 ?  75  PRO D C     1 
ATOM   13969 O  O     . PRO D 2 96  ? 137.954 84.686  133.666 1.00 23.45 ?  75  PRO D O     1 
ATOM   13970 C  CB    . PRO D 2 96  ? 139.749 85.242  131.021 1.00 24.80 ?  75  PRO D CB    1 
ATOM   13971 C  CG    . PRO D 2 96  ? 140.443 86.254  130.138 1.00 25.75 ?  75  PRO D CG    1 
ATOM   13972 C  CD    . PRO D 2 96  ? 140.829 87.380  131.063 1.00 25.07 ?  75  PRO D CD    1 
ATOM   13973 N  N     . ILE D 2 97  ? 140.008 85.431  134.211 1.00 23.36 ?  76  ILE D N     1 
ATOM   13974 C  CA    . ILE D 2 97  ? 140.016 84.713  135.482 1.00 23.48 ?  76  ILE D CA    1 
ATOM   13975 C  C     . ILE D 2 97  ? 139.037 85.340  136.461 1.00 23.30 ?  76  ILE D C     1 
ATOM   13976 O  O     . ILE D 2 97  ? 138.376 84.629  137.214 1.00 23.45 ?  76  ILE D O     1 
ATOM   13977 C  CB    . ILE D 2 97  ? 141.440 84.580  136.094 1.00 23.96 ?  76  ILE D CB    1 
ATOM   13978 C  CG1   . ILE D 2 97  ? 141.522 83.362  137.006 1.00 24.71 ?  76  ILE D CG1   1 
ATOM   13979 C  CG2   . ILE D 2 97  ? 141.883 85.865  136.835 1.00 24.02 ?  76  ILE D CG2   1 
ATOM   13980 C  CD1   . ILE D 2 97  ? 142.920 82.696  136.981 1.00 29.17 ?  76  ILE D CD1   1 
ATOM   13981 N  N     . VAL D 2 98  ? 138.936 86.669  136.440 1.00 22.71 ?  77  VAL D N     1 
ATOM   13982 C  CA    . VAL D 2 98  ? 137.978 87.375  137.306 1.00 22.78 ?  77  VAL D CA    1 
ATOM   13983 C  C     . VAL D 2 98  ? 136.544 87.088  136.857 1.00 22.89 ?  77  VAL D C     1 
ATOM   13984 O  O     . VAL D 2 98  ? 135.668 86.826  137.683 1.00 23.72 ?  77  VAL D O     1 
ATOM   13985 C  CB    . VAL D 2 98  ? 138.285 88.897  137.379 1.00 22.49 ?  77  VAL D CB    1 
ATOM   13986 C  CG1   . VAL D 2 98  ? 137.159 89.671  138.090 1.00 21.91 ?  77  VAL D CG1   1 
ATOM   13987 C  CG2   . VAL D 2 98  ? 139.601 89.119  138.105 1.00 23.02 ?  77  VAL D CG2   1 
ATOM   13988 N  N     . ALA D 2 99  ? 136.312 87.099  135.545 1.00 23.19 ?  78  ALA D N     1 
ATOM   13989 C  CA    . ALA D 2 99  ? 134.989 86.759  135.001 1.00 23.05 ?  78  ALA D CA    1 
ATOM   13990 C  C     . ALA D 2 99  ? 134.568 85.348  135.419 1.00 23.52 ?  78  ALA D C     1 
ATOM   13991 O  O     . ALA D 2 99  ? 133.397 85.091  135.716 1.00 23.68 ?  78  ALA D O     1 
ATOM   13992 C  CB    . ALA D 2 99  ? 134.988 86.901  133.488 1.00 22.81 ?  78  ALA D CB    1 
ATOM   13993 N  N     . GLU D 2 100 ? 135.530 84.430  135.452 1.00 23.68 ?  79  GLU D N     1 
ATOM   13994 C  CA    . GLU D 2 100 ? 135.260 83.055  135.863 1.00 24.14 ?  79  GLU D CA    1 
ATOM   13995 C  C     . GLU D 2 100 ? 134.784 82.915  137.318 1.00 23.66 ?  79  GLU D C     1 
ATOM   13996 O  O     . GLU D 2 100 ? 133.860 82.149  137.606 1.00 22.94 ?  79  GLU D O     1 
ATOM   13997 C  CB    . GLU D 2 100 ? 136.503 82.197  135.628 1.00 24.47 ?  79  GLU D CB    1 
ATOM   13998 C  CG    . GLU D 2 100 ? 136.266 80.708  135.795 1.00 27.90 ?  79  GLU D CG    1 
ATOM   13999 C  CD    . GLU D 2 100 ? 137.551 79.902  135.732 1.00 32.30 ?  79  GLU D CD    1 
ATOM   14000 O  OE1   . GLU D 2 100 ? 138.525 80.362  135.094 1.00 32.88 ?  79  GLU D OE1   1 
ATOM   14001 O  OE2   . GLU D 2 100 ? 137.582 78.807  136.330 1.00 34.74 -1 79  GLU D OE2   1 
ATOM   14002 N  N     . HIS D 2 101 ? 135.419 83.644  138.234 1.00 23.62 ?  80  HIS D N     1 
ATOM   14003 C  CA    . HIS D 2 101 ? 135.116 83.505  139.671 1.00 23.99 ?  80  HIS D CA    1 
ATOM   14004 C  C     . HIS D 2 101 ? 134.023 84.427  140.228 1.00 24.35 ?  80  HIS D C     1 
ATOM   14005 O  O     . HIS D 2 101 ? 133.486 84.162  141.304 1.00 24.21 ?  80  HIS D O     1 
ATOM   14006 C  CB    . HIS D 2 101 ? 136.403 83.618  140.501 1.00 24.13 ?  80  HIS D CB    1 
ATOM   14007 C  CG    . HIS D 2 101 ? 137.366 82.493  140.258 1.00 24.76 ?  80  HIS D CG    1 
ATOM   14008 N  ND1   . HIS D 2 101 ? 137.396 81.356  141.039 1.00 25.68 ?  80  HIS D ND1   1 
ATOM   14009 C  CD2   . HIS D 2 101 ? 138.315 82.322  139.309 1.00 25.75 ?  80  HIS D CD2   1 
ATOM   14010 C  CE1   . HIS D 2 101 ? 138.327 80.535  140.581 1.00 26.21 ?  80  HIS D CE1   1 
ATOM   14011 N  NE2   . HIS D 2 101 ? 138.900 81.098  139.532 1.00 25.35 ?  80  HIS D NE2   1 
ATOM   14012 N  N     . VAL D 2 102 ? 133.703 85.507  139.517 1.00 24.50 ?  81  VAL D N     1 
ATOM   14013 C  CA    . VAL D 2 102 ? 132.635 86.413  139.937 1.00 25.50 ?  81  VAL D CA    1 
ATOM   14014 C  C     . VAL D 2 102 ? 131.262 85.788  139.642 1.00 26.14 ?  81  VAL D C     1 
ATOM   14015 O  O     . VAL D 2 102 ? 131.049 85.258  138.555 1.00 26.96 ?  81  VAL D O     1 
ATOM   14016 C  CB    . VAL D 2 102 ? 132.763 87.798  139.237 1.00 25.30 ?  81  VAL D CB    1 
ATOM   14017 C  CG1   . VAL D 2 102 ? 131.523 88.634  139.451 1.00 27.08 ?  81  VAL D CG1   1 
ATOM   14018 C  CG2   . VAL D 2 102 ? 133.975 88.546  139.767 1.00 25.41 ?  81  VAL D CG2   1 
ATOM   14019 N  N     . ASP D 2 103 ? 130.354 85.840  140.613 1.00 26.45 ?  82  ASP D N     1 
ATOM   14020 C  CA    . ASP D 2 103 ? 128.978 85.379  140.417 1.00 27.15 ?  82  ASP D CA    1 
ATOM   14021 C  C     . ASP D 2 103 ? 128.098 86.515  139.919 1.00 26.39 ?  82  ASP D C     1 
ATOM   14022 O  O     . ASP D 2 103 ? 128.236 87.665  140.358 1.00 26.40 ?  82  ASP D O     1 
ATOM   14023 C  CB    . ASP D 2 103 ? 128.390 84.812  141.714 1.00 27.72 ?  82  ASP D CB    1 
ATOM   14024 C  CG    . ASP D 2 103 ? 129.136 83.585  142.224 1.00 31.46 ?  82  ASP D CG    1 
ATOM   14025 O  OD1   . ASP D 2 103 ? 129.673 82.788  141.407 1.00 34.26 ?  82  ASP D OD1   1 
ATOM   14026 O  OD2   . ASP D 2 103 ? 129.179 83.408  143.463 1.00 35.52 -1 82  ASP D OD2   1 
ATOM   14027 N  N     . GLY D 2 104 ? 127.180 86.184  139.016 1.00 25.52 ?  83  GLY D N     1 
ATOM   14028 C  CA    . GLY D 2 104 ? 126.235 87.161  138.479 1.00 24.31 ?  83  GLY D CA    1 
ATOM   14029 C  C     . GLY D 2 104 ? 126.352 87.196  136.960 1.00 23.27 ?  83  GLY D C     1 
ATOM   14030 O  O     . GLY D 2 104 ? 127.434 87.415  136.417 1.00 22.38 ?  83  GLY D O     1 
ATOM   14031 N  N     . HIS D 2 105 ? 125.238 86.961  136.272 1.00 22.46 ?  84  HIS D N     1 
ATOM   14032 C  CA    . HIS D 2 105 ? 125.239 86.958  134.807 1.00 22.17 ?  84  HIS D CA    1 
ATOM   14033 C  C     . HIS D 2 105 ? 125.628 88.296  134.201 1.00 21.13 ?  84  HIS D C     1 
ATOM   14034 O  O     . HIS D 2 105 ? 126.347 88.336  133.204 1.00 20.91 ?  84  HIS D O     1 
ATOM   14035 C  CB    . HIS D 2 105 ? 123.875 86.508  134.265 1.00 22.07 ?  84  HIS D CB    1 
ATOM   14036 C  CG    . HIS D 2 105 ? 123.489 85.137  134.719 1.00 23.85 ?  84  HIS D CG    1 
ATOM   14037 N  ND1   . HIS D 2 105 ? 124.327 84.051  134.579 1.00 24.86 ?  84  HIS D ND1   1 
ATOM   14038 C  CD2   . HIS D 2 105 ? 122.379 84.679  135.341 1.00 25.19 ?  84  HIS D CD2   1 
ATOM   14039 C  CE1   . HIS D 2 105 ? 123.739 82.979  135.077 1.00 24.94 ?  84  HIS D CE1   1 
ATOM   14040 N  NE2   . HIS D 2 105 ? 122.559 83.335  135.551 1.00 26.41 ?  84  HIS D NE2   1 
ATOM   14041 N  N     . GLN D 2 106 ? 125.157 89.383  134.794 1.00 20.66 ?  85  GLN D N     1 
ATOM   14042 C  CA    . GLN D 2 106 ? 125.382 90.700  134.206 1.00 20.70 ?  85  GLN D CA    1 
ATOM   14043 C  C     . GLN D 2 106 ? 126.837 91.123  134.403 1.00 20.46 ?  85  GLN D C     1 
ATOM   14044 O  O     . GLN D 2 106 ? 127.440 91.704  133.501 1.00 20.72 ?  85  GLN D O     1 
ATOM   14045 C  CB    . GLN D 2 106 ? 124.364 91.728  134.726 1.00 20.60 ?  85  GLN D CB    1 
ATOM   14046 C  CG    . GLN D 2 106 ? 122.899 91.357  134.368 1.00 20.74 ?  85  GLN D CG    1 
ATOM   14047 C  CD    . GLN D 2 106 ? 121.840 92.245  135.035 1.00 22.11 ?  85  GLN D CD    1 
ATOM   14048 O  OE1   . GLN D 2 106 ? 122.084 93.410  135.330 1.00 22.88 ?  85  GLN D OE1   1 
ATOM   14049 N  NE2   . GLN D 2 106 ? 120.653 91.688  135.258 1.00 21.64 ?  85  GLN D NE2   1 
ATOM   14050 N  N     . ARG D 2 107 ? 127.407 90.781  135.561 1.00 20.17 ?  86  ARG D N     1 
ATOM   14051 C  CA    . ARG D 2 107 ? 128.819 91.053  135.836 1.00 20.29 ?  86  ARG D CA    1 
ATOM   14052 C  C     . ARG D 2 107 ? 129.714 90.259  134.899 1.00 20.07 ?  86  ARG D C     1 
ATOM   14053 O  O     . ARG D 2 107 ? 130.694 90.785  134.389 1.00 19.53 ?  86  ARG D O     1 
ATOM   14054 C  CB    . ARG D 2 107 ? 129.174 90.703  137.279 1.00 20.88 ?  86  ARG D CB    1 
ATOM   14055 C  CG    . ARG D 2 107 ? 128.360 91.455  138.280 1.00 22.56 ?  86  ARG D CG    1 
ATOM   14056 C  CD    . ARG D 2 107 ? 128.505 90.848  139.652 1.00 27.21 ?  86  ARG D CD    1 
ATOM   14057 N  NE    . ARG D 2 107 ? 128.142 91.880  140.604 1.00 31.70 ?  86  ARG D NE    1 
ATOM   14058 C  CZ    . ARG D 2 107 ? 128.492 91.900  141.874 1.00 32.23 ?  86  ARG D CZ    1 
ATOM   14059 N  NH1   . ARG D 2 107 ? 129.226 90.917  142.393 1.00 34.27 1  86  ARG D NH1   1 
ATOM   14060 N  NH2   . ARG D 2 107 ? 128.100 92.921  142.613 1.00 33.79 ?  86  ARG D NH2   1 
ATOM   14061 N  N     . LYS D 2 108 ? 129.380 88.984  134.688 1.00 19.61 ?  87  LYS D N     1 
ATOM   14062 C  CA    . LYS D 2 108 ? 130.148 88.160  133.756 1.00 19.92 ?  87  LYS D CA    1 
ATOM   14063 C  C     . LYS D 2 108 ? 130.126 88.739  132.338 1.00 20.08 ?  87  LYS D C     1 
ATOM   14064 O  O     . LYS D 2 108 ? 131.118 88.640  131.607 1.00 20.38 ?  87  LYS D O     1 
ATOM   14065 C  CB    . LYS D 2 108 ? 129.671 86.705  133.754 1.00 19.54 ?  87  LYS D CB    1 
ATOM   14066 C  CG    . LYS D 2 108 ? 129.930 85.963  135.052 1.00 20.55 ?  87  LYS D CG    1 
ATOM   14067 C  CD    . LYS D 2 108 ? 129.454 84.511  134.968 1.00 21.09 ?  87  LYS D CD    1 
ATOM   14068 C  CE    . LYS D 2 108 ? 129.744 83.737  136.249 1.00 22.98 ?  87  LYS D CE    1 
ATOM   14069 N  NZ    . LYS D 2 108 ? 131.224 83.453  136.388 1.00 22.30 1  87  LYS D NZ    1 
ATOM   14070 N  N     . ALA D 2 109 ? 128.999 89.333  131.948 1.00 19.72 ?  88  ALA D N     1 
ATOM   14071 C  CA    . ALA D 2 109 ? 128.877 89.921  130.620 1.00 19.83 ?  88  ALA D CA    1 
ATOM   14072 C  C     . ALA D 2 109 ? 129.761 91.161  130.476 1.00 19.84 ?  88  ALA D C     1 
ATOM   14073 O  O     . ALA D 2 109 ? 130.475 91.311  129.479 1.00 19.96 ?  88  ALA D O     1 
ATOM   14074 C  CB    . ALA D 2 109 ? 127.409 90.240  130.292 1.00 19.65 ?  88  ALA D CB    1 
ATOM   14075 N  N     . VAL D 2 110 ? 129.734 92.033  131.482 1.00 19.33 ?  89  VAL D N     1 
ATOM   14076 C  CA    . VAL D 2 110 ? 130.574 93.240  131.474 1.00 19.22 ?  89  VAL D CA    1 
ATOM   14077 C  C     . VAL D 2 110 ? 132.055 92.821  131.450 1.00 19.45 ?  89  VAL D C     1 
ATOM   14078 O  O     . VAL D 2 110 ? 132.827 93.262  130.588 1.00 18.97 ?  89  VAL D O     1 
ATOM   14079 C  CB    . VAL D 2 110 ? 130.215 94.183  132.658 1.00 19.01 ?  89  VAL D CB    1 
ATOM   14080 C  CG1   . VAL D 2 110 ? 131.218 95.367  132.782 1.00 19.90 ?  89  VAL D CG1   1 
ATOM   14081 C  CG2   . VAL D 2 110 ? 128.816 94.722  132.467 1.00 19.69 ?  89  VAL D CG2   1 
ATOM   14082 N  N     . LEU D 2 111 ? 132.426 91.910  132.352 1.00 19.27 ?  90  LEU D N     1 
ATOM   14083 C  CA    . LEU D 2 111 ? 133.796 91.395  132.377 1.00 19.96 ?  90  LEU D CA    1 
ATOM   14084 C  C     . LEU D 2 111 ? 134.235 90.759  131.052 1.00 20.30 ?  90  LEU D C     1 
ATOM   14085 O  O     . LEU D 2 111 ? 135.363 90.985  130.604 1.00 19.88 ?  90  LEU D O     1 
ATOM   14086 C  CB    . LEU D 2 111 ? 134.018 90.454  133.570 1.00 19.87 ?  90  LEU D CB    1 
ATOM   14087 C  CG    . LEU D 2 111 ? 133.947 91.168  134.921 1.00 20.24 ?  90  LEU D CG    1 
ATOM   14088 C  CD1   . LEU D 2 111 ? 133.816 90.196  136.105 1.00 21.85 ?  90  LEU D CD1   1 
ATOM   14089 C  CD2   . LEU D 2 111 ? 135.143 92.121  135.109 1.00 20.29 ?  90  LEU D CD2   1 
ATOM   14090 N  N     . ASN D 2 112 ? 133.344 89.993  130.417 1.00 20.92 ?  91  ASN D N     1 
ATOM   14091 C  CA    . ASN D 2 112 ? 133.604 89.463  129.058 1.00 20.70 ?  91  ASN D CA    1 
ATOM   14092 C  C     . ASN D 2 112 ? 133.855 90.554  128.032 1.00 20.57 ?  91  ASN D C     1 
ATOM   14093 O  O     . ASN D 2 112 ? 134.688 90.394  127.125 1.00 20.45 ?  91  ASN D O     1 
ATOM   14094 C  CB    . ASN D 2 112 ? 132.419 88.645  128.543 1.00 21.16 ?  91  ASN D CB    1 
ATOM   14095 C  CG    . ASN D 2 112 ? 132.578 87.156  128.778 1.00 21.98 ?  91  ASN D CG    1 
ATOM   14096 O  OD1   . ASN D 2 112 ? 133.532 86.699  129.415 1.00 25.37 ?  91  ASN D OD1   1 
ATOM   14097 N  ND2   . ASN D 2 112 ? 131.623 86.390  128.281 1.00 21.12 ?  91  ASN D ND2   1 
ATOM   14098 N  N     . PHE D 2 113 ? 133.070 91.625  128.122 1.00 19.70 ?  92  PHE D N     1 
ATOM   14099 C  CA    . PHE D 2 113 ? 133.244 92.747  127.225 1.00 20.02 ?  92  PHE D CA    1 
ATOM   14100 C  C     . PHE D 2 113 ? 134.626 93.389  127.415 1.00 19.97 ?  92  PHE D C     1 
ATOM   14101 O  O     . PHE D 2 113 ? 135.322 93.686  126.438 1.00 19.22 ?  92  PHE D O     1 
ATOM   14102 C  CB    . PHE D 2 113 ? 132.122 93.789  127.375 1.00 20.09 ?  92  PHE D CB    1 
ATOM   14103 C  CG    . PHE D 2 113 ? 132.188 94.860  126.343 1.00 20.54 ?  92  PHE D CG    1 
ATOM   14104 C  CD1   . PHE D 2 113 ? 131.531 94.707  125.121 1.00 20.14 ?  92  PHE D CD1   1 
ATOM   14105 C  CD2   . PHE D 2 113 ? 132.963 96.000  126.562 1.00 20.77 ?  92  PHE D CD2   1 
ATOM   14106 C  CE1   . PHE D 2 113 ? 131.622 95.692  124.141 1.00 20.54 ?  92  PHE D CE1   1 
ATOM   14107 C  CE2   . PHE D 2 113 ? 133.065 96.987  125.583 1.00 21.23 ?  92  PHE D CE2   1 
ATOM   14108 C  CZ    . PHE D 2 113 ? 132.391 96.825  124.366 1.00 20.92 ?  92  PHE D CZ    1 
ATOM   14109 N  N     . MET D 2 114 ? 135.017 93.586  128.671 1.00 19.67 ?  93  MET D N     1 
ATOM   14110 C  CA    . MET D 2 114 ? 136.336 94.126  128.976 1.00 20.55 ?  93  MET D CA    1 
ATOM   14111 C  C     . MET D 2 114 ? 137.463 93.221  128.474 1.00 20.82 ?  93  MET D C     1 
ATOM   14112 O  O     . MET D 2 114 ? 138.427 93.729  127.916 1.00 20.43 ?  93  MET D O     1 
ATOM   14113 C  CB    . MET D 2 114 ? 136.484 94.397  130.468 1.00 20.24 ?  93  MET D CB    1 
ATOM   14114 C  CG    . MET D 2 114 ? 135.416 95.350  130.964 1.00 22.05 ?  93  MET D CG    1 
ATOM   14115 S  SD    . MET D 2 114 ? 135.389 95.574  132.728 1.00 25.85 ?  93  MET D SD    1 
ATOM   14116 C  CE    . MET D 2 114 ? 134.587 97.183  132.809 1.00 27.57 ?  93  MET D CE    1 
ATOM   14117 N  N     . ALA D 2 115 ? 137.333 91.901  128.670 1.00 21.19 ?  94  ALA D N     1 
ATOM   14118 C  CA    . ALA D 2 115 ? 138.326 90.938  128.154 1.00 21.53 ?  94  ALA D CA    1 
ATOM   14119 C  C     . ALA D 2 115 ? 138.426 91.025  126.632 1.00 21.75 ?  94  ALA D C     1 
ATOM   14120 O  O     . ALA D 2 115 ? 139.528 91.028  126.084 1.00 22.18 ?  94  ALA D O     1 
ATOM   14121 C  CB    . ALA D 2 115 ? 138.003 89.507  128.597 1.00 21.32 ?  94  ALA D CB    1 
ATOM   14122 N  N     . MET D 2 116 ? 137.277 91.127  125.960 1.00 21.47 ?  95  MET D N     1 
ATOM   14123 C  CA    . MET D 2 116 ? 137.239 91.319  124.513 1.00 21.83 ?  95  MET D CA    1 
ATOM   14124 C  C     . MET D 2 116 ? 138.049 92.556  124.078 1.00 22.15 ?  95  MET D C     1 
ATOM   14125 O  O     . MET D 2 116 ? 138.838 92.480  123.139 1.00 22.09 ?  95  MET D O     1 
ATOM   14126 C  CB    . MET D 2 116 ? 135.786 91.411  124.017 1.00 21.72 ?  95  MET D CB    1 
ATOM   14127 C  CG    . MET D 2 116 ? 135.628 91.716  122.518 1.00 22.57 ?  95  MET D CG    1 
ATOM   14128 S  SD    . MET D 2 116 ? 135.852 93.458  122.075 1.00 22.75 ?  95  MET D SD    1 
ATOM   14129 C  CE    . MET D 2 116 ? 134.435 94.220  122.867 1.00 22.96 ?  95  MET D CE    1 
ATOM   14130 N  N     . MET D 2 117 ? 137.848 93.683  124.764 1.00 22.04 ?  96  MET D N     1 
ATOM   14131 C  CA    . MET D 2 117 ? 138.567 94.927  124.438 1.00 22.45 ?  96  MET D CA    1 
ATOM   14132 C  C     . MET D 2 117 ? 140.091 94.751  124.556 1.00 22.39 ?  96  MET D C     1 
ATOM   14133 O  O     . MET D 2 117 ? 140.844 95.251  123.718 1.00 21.88 ?  96  MET D O     1 
ATOM   14134 C  CB    . MET D 2 117 ? 138.077 96.101  125.310 1.00 22.00 ?  96  MET D CB    1 
ATOM   14135 C  CG    . MET D 2 117 ? 136.656 96.602  124.942 1.00 23.25 ?  96  MET D CG    1 
ATOM   14136 S  SD    . MET D 2 117 ? 136.498 97.154  123.227 1.00 24.28 ?  96  MET D SD    1 
ATOM   14137 C  CE    . MET D 2 117 ? 137.394 98.703  123.262 1.00 24.59 ?  96  MET D CE    1 
ATOM   14138 N  N     . GLU D 2 118 ? 140.536 94.022  125.579 1.00 22.66 ?  97  GLU D N     1 
ATOM   14139 C  CA    . GLU D 2 118 ? 141.966 93.741  125.751 1.00 23.52 ?  97  GLU D CA    1 
ATOM   14140 C  C     . GLU D 2 118 ? 142.532 92.974  124.568 1.00 24.25 ?  97  GLU D C     1 
ATOM   14141 O  O     . GLU D 2 118 ? 143.545 93.381  123.997 1.00 25.05 ?  97  GLU D O     1 
ATOM   14142 C  CB    . GLU D 2 118 ? 142.265 92.964  127.054 1.00 23.11 ?  97  GLU D CB    1 
ATOM   14143 C  CG    . GLU D 2 118 ? 141.544 93.450  128.319 1.00 23.08 ?  97  GLU D CG    1 
ATOM   14144 C  CD    . GLU D 2 118 ? 142.011 94.804  128.829 1.00 24.08 ?  97  GLU D CD    1 
ATOM   14145 O  OE1   . GLU D 2 118 ? 142.671 95.537  128.077 1.00 26.39 ?  97  GLU D OE1   1 
ATOM   14146 O  OE2   . GLU D 2 118 ? 141.692 95.150  129.985 1.00 27.52 -1 97  GLU D OE2   1 
ATOM   14147 N  N     . ASN D 2 119 ? 141.860 91.886  124.198 1.00 25.47 ?  98  ASN D N     1 
ATOM   14148 C  CA    . ASN D 2 119 ? 142.370 90.918  123.206 1.00 26.32 ?  98  ASN D CA    1 
ATOM   14149 C  C     . ASN D 2 119 ? 142.114 91.286  121.748 1.00 26.22 ?  98  ASN D C     1 
ATOM   14150 O  O     . ASN D 2 119 ? 142.965 91.039  120.869 1.00 26.54 ?  98  ASN D O     1 
ATOM   14151 C  CB    . ASN D 2 119 ? 141.794 89.517  123.481 1.00 26.72 ?  98  ASN D CB    1 
ATOM   14152 C  CG    . ASN D 2 119 ? 142.277 88.939  124.811 1.00 29.12 ?  98  ASN D CG    1 
ATOM   14153 O  OD1   . ASN D 2 119 ? 143.483 88.864  125.070 1.00 32.07 ?  98  ASN D OD1   1 
ATOM   14154 N  ND2   . ASN D 2 119 ? 141.336 88.558  125.667 1.00 29.12 ?  98  ASN D ND2   1 
ATOM   14155 N  N     . ALA D 2 120 ? 140.936 91.847  121.494 1.00 25.46 ?  99  ALA D N     1 
ATOM   14156 C  CA    . ALA D 2 120 ? 140.495 92.140  120.132 1.00 25.77 ?  99  ALA D CA    1 
ATOM   14157 C  C     . ALA D 2 120 ? 140.799 93.568  119.689 1.00 25.51 ?  99  ALA D C     1 
ATOM   14158 O  O     . ALA D 2 120 ? 140.958 93.822  118.493 1.00 26.64 ?  99  ALA D O     1 
ATOM   14159 C  CB    . ALA D 2 120 ? 138.994 91.844  119.974 1.00 25.75 ?  99  ALA D CB    1 
ATOM   14160 N  N     . VAL D 2 121 ? 140.869 94.496  120.638 1.00 24.40 ?  100 VAL D N     1 
ATOM   14161 C  CA    . VAL D 2 121 ? 141.002 95.905  120.285 1.00 24.15 ?  100 VAL D CA    1 
ATOM   14162 C  C     . VAL D 2 121 ? 142.360 96.471  120.708 1.00 23.94 ?  100 VAL D C     1 
ATOM   14163 O  O     . VAL D 2 121 ? 143.135 96.932  119.865 1.00 23.75 ?  100 VAL D O     1 
ATOM   14164 C  CB    . VAL D 2 121 ? 139.822 96.755  120.847 1.00 23.68 ?  100 VAL D CB    1 
ATOM   14165 C  CG1   . VAL D 2 121 ? 139.962 98.219  120.431 1.00 23.76 ?  100 VAL D CG1   1 
ATOM   14166 C  CG2   . VAL D 2 121 ? 138.486 96.196  120.349 1.00 23.99 ?  100 VAL D CG2   1 
ATOM   14167 N  N     . HIS D 2 122 ? 142.641 96.428  122.009 1.00 23.68 ?  101 HIS D N     1 
ATOM   14168 C  CA    . HIS D 2 122 ? 143.898 96.958  122.541 1.00 24.02 ?  101 HIS D CA    1 
ATOM   14169 C  C     . HIS D 2 122 ? 145.124 96.269  121.965 1.00 24.39 ?  101 HIS D C     1 
ATOM   14170 O  O     . HIS D 2 122 ? 146.063 96.943  121.550 1.00 24.71 ?  101 HIS D O     1 
ATOM   14171 C  CB    . HIS D 2 122 ? 143.936 96.913  124.074 1.00 23.20 ?  101 HIS D CB    1 
ATOM   14172 C  CG    . HIS D 2 122 ? 142.904 97.775  124.732 1.00 22.82 ?  101 HIS D CG    1 
ATOM   14173 N  ND1   . HIS D 2 122 ? 142.739 97.820  126.098 1.00 20.48 ?  101 HIS D ND1   1 
ATOM   14174 C  CD2   . HIS D 2 122 ? 141.968 98.605  124.211 1.00 21.03 ?  101 HIS D CD2   1 
ATOM   14175 C  CE1   . HIS D 2 122 ? 141.756 98.652  126.393 1.00 19.88 ?  101 HIS D CE1   1 
ATOM   14176 N  NE2   . HIS D 2 122 ? 141.272 99.144  125.266 1.00 21.62 ?  101 HIS D NE2   1 
ATOM   14177 N  N     . ALA D 2 123 ? 145.117 94.936  121.929 1.00 25.30 ?  102 ALA D N     1 
ATOM   14178 C  CA    . ALA D 2 123 ? 146.294 94.189  121.462 1.00 25.77 ?  102 ALA D CA    1 
ATOM   14179 C  C     . ALA D 2 123 ? 146.611 94.467  119.988 1.00 26.37 ?  102 ALA D C     1 
ATOM   14180 O  O     . ALA D 2 123 ? 147.781 94.595  119.606 1.00 25.87 ?  102 ALA D O     1 
ATOM   14181 C  CB    . ALA D 2 123 ? 146.124 92.685  121.710 1.00 26.43 ?  102 ALA D CB    1 
ATOM   14182 N  N     . LYS D 2 124 ? 145.562 94.560  119.170 1.00 26.51 ?  103 LYS D N     1 
ATOM   14183 C  CA    . LYS D 2 124 ? 145.714 94.877  117.757 1.00 27.22 ?  103 LYS D CA    1 
ATOM   14184 C  C     . LYS D 2 124 ? 146.210 96.319  117.577 1.00 26.63 ?  103 LYS D C     1 
ATOM   14185 O  O     . LYS D 2 124 ? 147.007 96.592  116.679 1.00 26.07 ?  103 LYS D O     1 
ATOM   14186 C  CB    . LYS D 2 124 ? 144.390 94.645  117.002 1.00 27.51 ?  103 LYS D CB    1 
ATOM   14187 C  CG    . LYS D 2 124 ? 144.399 95.031  115.507 1.00 30.58 ?  103 LYS D CG    1 
ATOM   14188 C  CD    . LYS D 2 124 ? 145.306 94.129  114.683 1.00 35.72 ?  103 LYS D CD    1 
ATOM   14189 C  CE    . LYS D 2 124 ? 145.340 94.533  113.207 1.00 37.33 ?  103 LYS D CE    1 
ATOM   14190 N  NZ    . LYS D 2 124 ? 144.010 94.323  112.576 1.00 40.73 1  103 LYS D NZ    1 
ATOM   14191 N  N     . SER D 2 125 ? 145.747 97.220  118.449 1.00 26.02 ?  104 SER D N     1 
ATOM   14192 C  CA    . SER D 2 125 ? 146.123 98.635  118.404 1.00 26.16 ?  104 SER D CA    1 
ATOM   14193 C  C     . SER D 2 125 ? 147.608 98.849  118.700 1.00 26.18 ?  104 SER D C     1 
ATOM   14194 O  O     . SER D 2 125 ? 148.272 99.634  118.014 1.00 26.06 ?  104 SER D O     1 
ATOM   14195 C  CB    . SER D 2 125 ? 145.274 99.463  119.371 1.00 26.10 ?  104 SER D CB    1 
ATOM   14196 O  OG    . SER D 2 125 ? 143.919 99.460  118.958 1.00 26.58 ?  104 SER D OG    1 
ATOM   14197 N  N     . TYR D 2 126 ? 148.114 98.154  119.716 1.00 25.68 ?  105 TYR D N     1 
ATOM   14198 C  CA    . TYR D 2 126 ? 149.538 98.217  120.069 1.00 26.12 ?  105 TYR D CA    1 
ATOM   14199 C  C     . TYR D 2 126 ? 150.401 97.658  118.932 1.00 26.38 ?  105 TYR D C     1 
ATOM   14200 O  O     . TYR D 2 126 ? 151.423 98.244  118.568 1.00 26.83 ?  105 TYR D O     1 
ATOM   14201 C  CB    . TYR D 2 126 ? 149.829 97.449  121.372 1.00 25.35 ?  105 TYR D CB    1 
ATOM   14202 C  CG    . TYR D 2 126 ? 149.459 98.180  122.648 1.00 25.46 ?  105 TYR D CG    1 
ATOM   14203 C  CD1   . TYR D 2 126 ? 149.967 99.451  122.916 1.00 25.41 ?  105 TYR D CD1   1 
ATOM   14204 C  CD2   . TYR D 2 126 ? 148.626 97.586  123.609 1.00 24.77 ?  105 TYR D CD2   1 
ATOM   14205 C  CE1   . TYR D 2 126 ? 149.637 100.132 124.087 1.00 25.89 ?  105 TYR D CE1   1 
ATOM   14206 C  CE2   . TYR D 2 126 ? 148.288 98.264  124.791 1.00 23.11 ?  105 TYR D CE2   1 
ATOM   14207 C  CZ    . TYR D 2 126 ? 148.811 99.528  125.026 1.00 25.38 ?  105 TYR D CZ    1 
ATOM   14208 O  OH    . TYR D 2 126 ? 148.502 100.222 126.176 1.00 23.31 ?  105 TYR D OH    1 
ATOM   14209 N  N     . SER D 2 127 ? 149.971 96.537  118.365 1.00 27.16 ?  106 SER D N     1 
ATOM   14210 C  CA    . SER D 2 127 ? 150.670 95.919  117.232 1.00 27.83 ?  106 SER D CA    1 
ATOM   14211 C  C     . SER D 2 127 ? 150.743 96.879  116.036 1.00 28.21 ?  106 SER D C     1 
ATOM   14212 O  O     . SER D 2 127 ? 151.818 97.062  115.451 1.00 28.30 ?  106 SER D O     1 
ATOM   14213 C  CB    . SER D 2 127 ? 149.997 94.592  116.844 1.00 28.37 ?  106 SER D CB    1 
ATOM   14214 O  OG    . SER D 2 127 ? 150.590 94.028  115.675 1.00 29.33 ?  106 SER D OG    1 
ATOM   14215 N  N     . ASN D 2 128 ? 149.603 97.490  115.695 1.00 28.27 ?  107 ASN D N     1 
ATOM   14216 C  CA    . ASN D 2 128 ? 149.513 98.507  114.635 1.00 28.79 ?  107 ASN D CA    1 
ATOM   14217 C  C     . ASN D 2 128 ? 150.467 99.682  114.823 1.00 28.53 ?  107 ASN D C     1 
ATOM   14218 O  O     . ASN D 2 128 ? 151.122 100.107 113.865 1.00 28.03 ?  107 ASN D O     1 
ATOM   14219 C  CB    . ASN D 2 128 ? 148.078 99.043  114.484 1.00 29.05 ?  107 ASN D CB    1 
ATOM   14220 C  CG    . ASN D 2 128 ? 147.115 98.009  113.892 1.00 30.48 ?  107 ASN D CG    1 
ATOM   14221 O  OD1   . ASN D 2 128 ? 147.531 96.959  113.407 1.00 32.19 ?  107 ASN D OD1   1 
ATOM   14222 N  ND2   . ASN D 2 128 ? 145.821 98.304  113.949 1.00 31.59 ?  107 ASN D ND2   1 
ATOM   14223 N  N     . ILE D 2 129 ? 150.526 100.223 116.042 1.00 28.21 ?  108 ILE D N     1 
ATOM   14224 C  CA    . ILE D 2 129 ? 151.471 101.307 116.343 1.00 28.76 ?  108 ILE D CA    1 
ATOM   14225 C  C     . ILE D 2 129 ? 152.920 100.859 116.084 1.00 29.83 ?  108 ILE D C     1 
ATOM   14226 O  O     . ILE D 2 129 ? 153.687 101.563 115.413 1.00 29.99 ?  108 ILE D O     1 
ATOM   14227 C  CB    . ILE D 2 129 ? 151.308 101.867 117.793 1.00 28.28 ?  108 ILE D CB    1 
ATOM   14228 C  CG1   . ILE D 2 129 ? 149.922 102.502 117.982 1.00 27.94 ?  108 ILE D CG1   1 
ATOM   14229 C  CG2   . ILE D 2 129 ? 152.399 102.904 118.097 1.00 27.52 ?  108 ILE D CG2   1 
ATOM   14230 C  CD1   . ILE D 2 129 ? 149.538 102.741 119.438 1.00 27.98 ?  108 ILE D CD1   1 
ATOM   14231 N  N     . PHE D 2 130 ? 153.287 99.693  116.608 1.00 30.86 ?  109 PHE D N     1 
ATOM   14232 C  CA    . PHE D 2 130 ? 154.625 99.145  116.400 1.00 32.76 ?  109 PHE D CA    1 
ATOM   14233 C  C     . PHE D 2 130 ? 154.989 98.980  114.921 1.00 34.37 ?  109 PHE D C     1 
ATOM   14234 O  O     . PHE D 2 130 ? 156.027 99.470  114.482 1.00 34.61 ?  109 PHE D O     1 
ATOM   14235 C  CB    . PHE D 2 130 ? 154.787 97.810  117.122 1.00 32.81 ?  109 PHE D CB    1 
ATOM   14236 C  CG    . PHE D 2 130 ? 155.421 97.926  118.479 1.00 33.84 ?  109 PHE D CG    1 
ATOM   14237 C  CD1   . PHE D 2 130 ? 156.757 98.297  118.608 1.00 34.61 ?  109 PHE D CD1   1 
ATOM   14238 C  CD2   . PHE D 2 130 ? 154.692 97.631  119.624 1.00 35.74 ?  109 PHE D CD2   1 
ATOM   14239 C  CE1   . PHE D 2 130 ? 157.357 98.394  119.863 1.00 36.99 ?  109 PHE D CE1   1 
ATOM   14240 C  CE2   . PHE D 2 130 ? 155.280 97.724  120.892 1.00 36.96 ?  109 PHE D CE2   1 
ATOM   14241 C  CZ    . PHE D 2 130 ? 156.615 98.106  121.012 1.00 36.91 ?  109 PHE D CZ    1 
ATOM   14242 N  N     . MET D 2 131 ? 154.121 98.303  114.168 1.00 35.90 ?  110 MET D N     1 
ATOM   14243 C  CA    . MET D 2 131 ? 154.347 98.025  112.749 1.00 37.94 ?  110 MET D CA    1 
ATOM   14244 C  C     . MET D 2 131 ? 154.485 99.297  111.923 1.00 38.05 ?  110 MET D C     1 
ATOM   14245 O  O     . MET D 2 131 ? 155.162 99.296  110.901 1.00 38.20 ?  110 MET D O     1 
ATOM   14246 C  CB    . MET D 2 131 ? 153.229 97.143  112.168 1.00 38.63 ?  110 MET D CB    1 
ATOM   14247 C  CG    . MET D 2 131 ? 153.202 95.703  112.707 1.00 42.34 ?  110 MET D CG    1 
ATOM   14248 S  SD    . MET D 2 131 ? 151.882 94.658  112.009 1.00 50.15 ?  110 MET D SD    1 
ATOM   14249 C  CE    . MET D 2 131 ? 150.390 95.367  112.718 1.00 48.14 ?  110 MET D CE    1 
ATOM   14250 N  N     . THR D 2 132 ? 153.843 100.375 112.371 1.00 38.12 ?  111 THR D N     1 
ATOM   14251 C  CA    . THR D 2 132 ? 153.936 101.665 111.687 1.00 38.79 ?  111 THR D CA    1 
ATOM   14252 C  C     . THR D 2 132 ? 155.298 102.347 111.911 1.00 38.81 ?  111 THR D C     1 
ATOM   14253 O  O     . THR D 2 132 ? 155.879 102.895 110.968 1.00 39.26 ?  111 THR D O     1 
ATOM   14254 C  CB    . THR D 2 132 ? 152.786 102.604 112.104 1.00 38.78 ?  111 THR D CB    1 
ATOM   14255 O  OG1   . THR D 2 132 ? 151.532 101.967 111.835 1.00 39.32 ?  111 THR D OG1   1 
ATOM   14256 C  CG2   . THR D 2 132 ? 152.838 103.915 111.326 1.00 39.75 ?  111 THR D CG2   1 
ATOM   14257 N  N     . LEU D 2 133 ? 155.797 102.294 113.147 1.00 38.34 ?  112 LEU D N     1 
ATOM   14258 C  CA    . LEU D 2 133 ? 156.986 103.048 113.557 1.00 38.36 ?  112 LEU D CA    1 
ATOM   14259 C  C     . LEU D 2 133 ? 158.316 102.310 113.393 1.00 38.94 ?  112 LEU D C     1 
ATOM   14260 O  O     . LEU D 2 133 ? 159.346 102.939 113.153 1.00 39.14 ?  112 LEU D O     1 
ATOM   14261 C  CB    . LEU D 2 133 ? 156.849 103.516 115.016 1.00 37.62 ?  112 LEU D CB    1 
ATOM   14262 C  CG    . LEU D 2 133 ? 155.617 104.335 115.407 1.00 36.50 ?  112 LEU D CG    1 
ATOM   14263 C  CD1   . LEU D 2 133 ? 155.539 104.489 116.930 1.00 35.80 ?  112 LEU D CD1   1 
ATOM   14264 C  CD2   . LEU D 2 133 ? 155.584 105.690 114.721 1.00 35.32 ?  112 LEU D CD2   1 
ATOM   14265 N  N     . ALA D 2 134 ? 158.311 100.991 113.534 1.00 39.41 ?  113 ALA D N     1 
ATOM   14266 C  CA    . ALA D 2 134 ? 159.569 100.239 113.455 1.00 40.33 ?  113 ALA D CA    1 
ATOM   14267 C  C     . ALA D 2 134 ? 159.522 99.118  112.422 1.00 41.05 ?  113 ALA D C     1 
ATOM   14268 O  O     . ALA D 2 134 ? 158.456 98.566  112.172 1.00 40.81 ?  113 ALA D O     1 
ATOM   14269 C  CB    . ALA D 2 134 ? 159.936 99.689  114.821 1.00 40.15 ?  113 ALA D CB    1 
ATOM   14270 N  N     . PRO D 2 135 ? 160.677 98.785  111.807 1.00 42.21 ?  114 PRO D N     1 
ATOM   14271 C  CA    . PRO D 2 135 ? 160.710 97.592  110.952 1.00 43.27 ?  114 PRO D CA    1 
ATOM   14272 C  C     . PRO D 2 135 ? 160.657 96.307  111.792 1.00 43.89 ?  114 PRO D C     1 
ATOM   14273 O  O     . PRO D 2 135 ? 160.967 96.338  112.986 1.00 43.31 ?  114 PRO D O     1 
ATOM   14274 C  CB    . PRO D 2 135 ? 162.054 97.710  110.228 1.00 43.69 ?  114 PRO D CB    1 
ATOM   14275 C  CG    . PRO D 2 135 ? 162.902 98.510  111.142 1.00 43.01 ?  114 PRO D CG    1 
ATOM   14276 C  CD    . PRO D 2 135 ? 161.983 99.472  111.843 1.00 42.16 ?  114 PRO D CD    1 
ATOM   14277 N  N     . THR D 2 136 ? 160.278 95.198  111.158 1.00 45.26 ?  115 THR D N     1 
ATOM   14278 C  CA    . THR D 2 136 ? 160.055 93.916  111.847 1.00 46.11 ?  115 THR D CA    1 
ATOM   14279 C  C     . THR D 2 136 ? 161.204 93.514  112.776 1.00 46.35 ?  115 THR D C     1 
ATOM   14280 O  O     . THR D 2 136 ? 160.965 93.122  113.923 1.00 46.25 ?  115 THR D O     1 
ATOM   14281 C  CB    . THR D 2 136 ? 159.735 92.771  110.846 1.00 46.59 ?  115 THR D CB    1 
ATOM   14282 O  OG1   . THR D 2 136 ? 158.644 93.166  110.008 1.00 47.80 ?  115 THR D OG1   1 
ATOM   14283 C  CG2   . THR D 2 136 ? 159.331 91.489  111.574 1.00 46.94 ?  115 THR D CG2   1 
ATOM   14284 N  N     . GLU D 2 137 ? 162.441 93.634  112.293 1.00 46.92 ?  116 GLU D N     1 
ATOM   14285 C  CA    . GLU D 2 137 ? 163.614 93.248  113.077 1.00 47.37 ?  116 GLU D CA    1 
ATOM   14286 C  C     . GLU D 2 137 ? 163.780 94.075  114.354 1.00 46.64 ?  116 GLU D C     1 
ATOM   14287 O  O     . GLU D 2 137 ? 164.164 93.533  115.392 1.00 46.89 ?  116 GLU D O     1 
ATOM   14288 C  CB    . GLU D 2 137 ? 164.893 93.293  112.227 1.00 48.04 ?  116 GLU D CB    1 
ATOM   14289 C  CG    . GLU D 2 137 ? 166.159 92.780  112.938 1.00 49.86 ?  116 GLU D CG    1 
ATOM   14290 C  CD    . GLU D 2 137 ? 166.179 91.261  113.169 1.00 52.40 ?  116 GLU D CD    1 
ATOM   14291 O  OE1   . GLU D 2 137 ? 165.218 90.713  113.753 1.00 52.97 ?  116 GLU D OE1   1 
ATOM   14292 O  OE2   . GLU D 2 137 ? 167.181 90.614  112.784 1.00 54.12 -1 116 GLU D OE2   1 
ATOM   14293 N  N     . THR D 2 138 ? 163.488 95.372  114.271 1.00 46.09 ?  117 THR D N     1 
ATOM   14294 C  CA    . THR D 2 138 ? 163.546 96.272  115.433 1.00 45.30 ?  117 THR D CA    1 
ATOM   14295 C  C     . THR D 2 138 ? 162.481 95.926  116.482 1.00 44.63 ?  117 THR D C     1 
ATOM   14296 O  O     . THR D 2 138 ? 162.753 95.964  117.686 1.00 44.51 ?  117 THR D O     1 
ATOM   14297 C  CB    . THR D 2 138 ? 163.409 97.754  115.009 1.00 45.20 ?  117 THR D CB    1 
ATOM   14298 O  OG1   . THR D 2 138 ? 164.428 98.073  114.056 1.00 45.69 ?  117 THR D OG1   1 
ATOM   14299 C  CG2   . THR D 2 138 ? 163.543 98.694  116.207 1.00 44.67 ?  117 THR D CG2   1 
ATOM   14300 N  N     . ILE D 2 139 ? 161.278 95.584  116.023 1.00 44.24 ?  118 ILE D N     1 
ATOM   14301 C  CA    . ILE D 2 139 ? 160.194 95.174  116.920 1.00 43.65 ?  118 ILE D CA    1 
ATOM   14302 C  C     . ILE D 2 139 ? 160.589 93.916  117.707 1.00 43.87 ?  118 ILE D C     1 
ATOM   14303 O  O     . ILE D 2 139 ? 160.465 93.879  118.934 1.00 43.36 ?  118 ILE D O     1 
ATOM   14304 C  CB    . ILE D 2 139 ? 158.860 94.981  116.153 1.00 43.68 ?  118 ILE D CB    1 
ATOM   14305 C  CG1   . ILE D 2 139 ? 158.356 96.333  115.625 1.00 43.30 ?  118 ILE D CG1   1 
ATOM   14306 C  CG2   . ILE D 2 139 ? 157.796 94.316  117.046 1.00 43.11 ?  118 ILE D CG2   1 
ATOM   14307 C  CD1   . ILE D 2 139 ? 157.293 96.245  114.538 1.00 43.41 ?  118 ILE D CD1   1 
ATOM   14308 N  N     . ASN D 2 140 ? 161.091 92.906  116.997 1.00 44.52 ?  119 ASN D N     1 
ATOM   14309 C  CA    . ASN D 2 140 ? 161.541 91.657  117.623 1.00 45.00 ?  119 ASN D CA    1 
ATOM   14310 C  C     . ASN D 2 140 ? 162.632 91.874  118.693 1.00 44.99 ?  119 ASN D C     1 
ATOM   14311 O  O     . ASN D 2 140 ? 162.599 91.243  119.757 1.00 44.61 ?  119 ASN D O     1 
ATOM   14312 C  CB    . ASN D 2 140 ? 162.000 90.646  116.558 1.00 45.74 ?  119 ASN D CB    1 
ATOM   14313 C  CG    . ASN D 2 140 ? 160.882 90.252  115.585 1.00 46.40 ?  119 ASN D CG    1 
ATOM   14314 O  OD1   . ASN D 2 140 ? 159.695 90.492  115.834 1.00 46.85 ?  119 ASN D OD1   1 
ATOM   14315 N  ND2   . ASN D 2 140 ? 161.266 89.632  114.471 1.00 48.16 ?  119 ASN D ND2   1 
ATOM   14316 N  N     . GLU D 2 141 ? 163.571 92.782  118.419 1.00 45.09 ?  120 GLU D N     1 
ATOM   14317 C  CA    . GLU D 2 141 ? 164.656 93.088  119.356 1.00 45.27 ?  120 GLU D CA    1 
ATOM   14318 C  C     . GLU D 2 141 ? 164.190 93.833  120.615 1.00 44.75 ?  120 GLU D C     1 
ATOM   14319 O  O     . GLU D 2 141 ? 164.633 93.523  121.726 1.00 44.37 ?  120 GLU D O     1 
ATOM   14320 C  CB    . GLU D 2 141 ? 165.774 93.869  118.664 1.00 45.75 ?  120 GLU D CB    1 
ATOM   14321 C  CG    . GLU D 2 141 ? 166.553 93.056  117.629 1.00 48.17 ?  120 GLU D CG    1 
ATOM   14322 C  CD    . GLU D 2 141 ? 167.694 93.830  116.999 1.00 50.15 ?  120 GLU D CD    1 
ATOM   14323 O  OE1   . GLU D 2 141 ? 168.502 94.427  117.741 1.00 50.90 ?  120 GLU D OE1   1 
ATOM   14324 O  OE2   . GLU D 2 141 ? 167.786 93.835  115.754 1.00 52.25 -1 120 GLU D OE2   1 
ATOM   14325 N  N     . VAL D 2 142 ? 163.313 94.820  120.431 1.00 44.31 ?  121 VAL D N     1 
ATOM   14326 C  CA    . VAL D 2 142 ? 162.735 95.568  121.549 1.00 43.91 ?  121 VAL D CA    1 
ATOM   14327 C  C     . VAL D 2 142 ? 161.963 94.630  122.483 1.00 43.71 ?  121 VAL D C     1 
ATOM   14328 O  O     . VAL D 2 142 ? 162.088 94.722  123.703 1.00 43.44 ?  121 VAL D O     1 
ATOM   14329 C  CB    . VAL D 2 142 ? 161.823 96.729  121.065 1.00 43.65 ?  121 VAL D CB    1 
ATOM   14330 C  CG1   . VAL D 2 142 ? 161.131 97.408  122.246 1.00 43.40 ?  121 VAL D CG1   1 
ATOM   14331 C  CG2   . VAL D 2 142 ? 162.637 97.755  120.283 1.00 43.96 ?  121 VAL D CG2   1 
ATOM   14332 N  N     . PHE D 2 143 ? 161.181 93.723  121.904 1.00 44.03 ?  122 PHE D N     1 
ATOM   14333 C  CA    . PHE D 2 143 ? 160.428 92.763  122.702 1.00 44.42 ?  122 PHE D CA    1 
ATOM   14334 C  C     . PHE D 2 143 ? 161.320 91.748  123.408 1.00 45.38 ?  122 PHE D C     1 
ATOM   14335 O  O     . PHE D 2 143 ? 161.032 91.359  124.536 1.00 45.50 ?  122 PHE D O     1 
ATOM   14336 C  CB    . PHE D 2 143 ? 159.324 92.088  121.885 1.00 44.27 ?  122 PHE D CB    1 
ATOM   14337 C  CG    . PHE D 2 143 ? 158.043 92.866  121.877 1.00 43.28 ?  122 PHE D CG    1 
ATOM   14338 C  CD1   . PHE D 2 143 ? 157.150 92.769  122.942 1.00 42.17 ?  122 PHE D CD1   1 
ATOM   14339 C  CD2   . PHE D 2 143 ? 157.744 93.725  120.827 1.00 42.76 ?  122 PHE D CD2   1 
ATOM   14340 C  CE1   . PHE D 2 143 ? 155.969 93.501  122.954 1.00 42.16 ?  122 PHE D CE1   1 
ATOM   14341 C  CE2   . PHE D 2 143 ? 156.566 94.463  120.829 1.00 42.77 ?  122 PHE D CE2   1 
ATOM   14342 C  CZ    . PHE D 2 143 ? 155.674 94.351  121.895 1.00 42.28 ?  122 PHE D CZ    1 
ATOM   14343 N  N     . GLU D 2 144 ? 162.408 91.347  122.755 1.00 46.18 ?  123 GLU D N     1 
ATOM   14344 C  CA    . GLU D 2 144 ? 163.431 90.523  123.397 1.00 47.19 ?  123 GLU D CA    1 
ATOM   14345 C  C     . GLU D 2 144 ? 164.034 91.234  124.618 1.00 46.99 ?  123 GLU D C     1 
ATOM   14346 O  O     . GLU D 2 144 ? 164.186 90.616  125.676 1.00 46.94 ?  123 GLU D O     1 
ATOM   14347 C  CB    . GLU D 2 144 ? 164.527 90.147  122.390 1.00 47.80 ?  123 GLU D CB    1 
ATOM   14348 C  CG    . GLU D 2 144 ? 165.584 89.163  122.903 1.00 49.54 ?  123 GLU D CG    1 
ATOM   14349 C  CD    . GLU D 2 144 ? 166.712 88.920  121.895 1.00 52.37 ?  123 GLU D CD    1 
ATOM   14350 O  OE1   . GLU D 2 144 ? 167.235 89.899  121.314 1.00 52.92 ?  123 GLU D OE1   1 
ATOM   14351 O  OE2   . GLU D 2 144 ? 167.083 87.744  121.688 1.00 53.55 -1 123 GLU D OE2   1 
ATOM   14352 N  N     . TRP D 2 145 ? 164.365 92.522  124.463 1.00 47.02 ?  124 TRP D N     1 
ATOM   14353 C  CA    . TRP D 2 145 ? 164.949 93.342  125.539 1.00 46.93 ?  124 TRP D CA    1 
ATOM   14354 C  C     . TRP D 2 145 ? 163.977 93.517  126.697 1.00 46.55 ?  124 TRP D C     1 
ATOM   14355 O  O     . TRP D 2 145 ? 164.323 93.261  127.846 1.00 46.42 ?  124 TRP D O     1 
ATOM   14356 C  CB    . TRP D 2 145 ? 165.371 94.724  125.018 1.00 47.07 ?  124 TRP D CB    1 
ATOM   14357 C  CG    . TRP D 2 145 ? 166.173 95.576  126.006 1.00 47.82 ?  124 TRP D CG    1 
ATOM   14358 C  CD1   . TRP D 2 145 ? 167.538 95.647  126.108 1.00 48.78 ?  124 TRP D CD1   1 
ATOM   14359 C  CD2   . TRP D 2 145 ? 165.655 96.484  127.001 1.00 47.80 ?  124 TRP D CD2   1 
ATOM   14360 N  NE1   . TRP D 2 145 ? 167.900 96.529  127.103 1.00 49.06 ?  124 TRP D NE1   1 
ATOM   14361 C  CE2   . TRP D 2 145 ? 166.767 97.054  127.668 1.00 48.24 ?  124 TRP D CE2   1 
ATOM   14362 C  CE3   . TRP D 2 145 ? 164.365 96.863  127.397 1.00 47.65 ?  124 TRP D CE3   1 
ATOM   14363 C  CZ2   . TRP D 2 145 ? 166.625 97.985  128.711 1.00 47.74 ?  124 TRP D CZ2   1 
ATOM   14364 C  CZ3   . TRP D 2 145 ? 164.222 97.788  128.434 1.00 46.92 ?  124 TRP D CZ3   1 
ATOM   14365 C  CH2   . TRP D 2 145 ? 165.352 98.338  129.077 1.00 47.88 ?  124 TRP D CH2   1 
ATOM   14366 N  N     . VAL D 2 146 ? 162.760 93.958  126.387 1.00 46.09 ?  125 VAL D N     1 
ATOM   14367 C  CA    . VAL D 2 146 ? 161.763 94.233  127.414 1.00 45.36 ?  125 VAL D CA    1 
ATOM   14368 C  C     . VAL D 2 146 ? 161.327 92.931  128.105 1.00 45.28 ?  125 VAL D C     1 
ATOM   14369 O  O     . VAL D 2 146 ? 161.041 92.926  129.308 1.00 45.29 ?  125 VAL D O     1 
ATOM   14370 C  CB    . VAL D 2 146 ? 160.593 95.100  126.847 1.00 45.33 ?  125 VAL D CB    1 
ATOM   14371 C  CG1   . VAL D 2 146 ? 159.483 95.267  127.852 1.00 44.97 ?  125 VAL D CG1   1 
ATOM   14372 C  CG2   . VAL D 2 146 ? 161.114 96.482  126.446 1.00 44.52 ?  125 VAL D CG2   1 
ATOM   14373 N  N     . LYS D 2 147 ? 161.330 91.828  127.358 1.00 44.98 ?  126 LYS D N     1 
ATOM   14374 C  CA    . LYS D 2 147 ? 161.036 90.503  127.922 1.00 44.65 ?  126 LYS D CA    1 
ATOM   14375 C  C     . LYS D 2 147 ? 162.071 90.052  128.965 1.00 44.06 ?  126 LYS D C     1 
ATOM   14376 O  O     . LYS D 2 147 ? 161.745 89.304  129.888 1.00 44.65 ?  126 LYS D O     1 
ATOM   14377 C  CB    . LYS D 2 147 ? 160.928 89.444  126.820 1.00 45.31 ?  126 LYS D CB    1 
ATOM   14378 C  CG    . LYS D 2 147 ? 159.731 88.519  126.980 1.00 46.54 ?  126 LYS D CG    1 
ATOM   14379 C  CD    . LYS D 2 147 ? 160.071 87.055  126.694 1.00 49.06 ?  126 LYS D CD    1 
ATOM   14380 C  CE    . LYS D 2 147 ? 160.584 86.347  127.955 1.00 50.46 ?  126 LYS D CE    1 
ATOM   14381 N  NZ    . LYS D 2 147 ? 160.341 84.872  127.929 1.00 51.33 1  126 LYS D NZ    1 
ATOM   14382 N  N     . GLN D 2 148 ? 163.311 90.508  128.813 1.00 42.58 ?  127 GLN D N     1 
ATOM   14383 C  CA    . GLN D 2 148 ? 164.389 90.172  129.743 1.00 41.39 ?  127 GLN D CA    1 
ATOM   14384 C  C     . GLN D 2 148 ? 164.564 91.221  130.849 1.00 39.56 ?  127 GLN D C     1 
ATOM   14385 O  O     . GLN D 2 148 ? 165.218 90.954  131.856 1.00 39.77 ?  127 GLN D O     1 
ATOM   14386 C  CB    . GLN D 2 148 ? 165.697 89.943  128.960 1.00 42.11 ?  127 GLN D CB    1 
ATOM   14387 C  CG    . GLN D 2 148 ? 166.986 90.378  129.651 1.00 44.08 ?  127 GLN D CG    1 
ATOM   14388 C  CD    . GLN D 2 148 ? 167.481 91.756  129.207 1.00 46.12 ?  127 GLN D CD    1 
ATOM   14389 O  OE1   . GLN D 2 148 ? 166.697 92.701  129.043 1.00 46.47 ?  127 GLN D OE1   1 
ATOM   14390 N  NE2   . GLN D 2 148 ? 168.796 91.877  129.024 1.00 45.69 ?  127 GLN D NE2   1 
ATOM   14391 N  N     . ASN D 2 149 ? 163.968 92.400  130.657 1.00 36.99 ?  128 ASN D N     1 
ATOM   14392 C  CA    . ASN D 2 149 ? 164.104 93.513  131.598 1.00 34.54 ?  128 ASN D CA    1 
ATOM   14393 C  C     . ASN D 2 149 ? 163.613 93.200  133.014 1.00 33.13 ?  128 ASN D C     1 
ATOM   14394 O  O     . ASN D 2 149 ? 162.472 92.788  133.211 1.00 32.62 ?  128 ASN D O     1 
ATOM   14395 C  CB    . ASN D 2 149 ? 163.396 94.760  131.066 1.00 34.24 ?  128 ASN D CB    1 
ATOM   14396 C  CG    . ASN D 2 149 ? 163.614 95.966  131.958 1.00 33.83 ?  128 ASN D CG    1 
ATOM   14397 O  OD1   . ASN D 2 149 ? 162.751 96.322  132.763 1.00 32.21 ?  128 ASN D OD1   1 
ATOM   14398 N  ND2   . ASN D 2 149 ? 164.787 96.583  131.840 1.00 33.26 ?  128 ASN D ND2   1 
ATOM   14399 N  N     . LYS D 2 150 ? 164.480 93.438  133.994 1.00 31.49 ?  129 LYS D N     1 
ATOM   14400 C  CA    . LYS D 2 150 ? 164.228 93.082  135.388 1.00 30.68 ?  129 LYS D CA    1 
ATOM   14401 C  C     . LYS D 2 150 ? 162.991 93.773  136.012 1.00 28.95 ?  129 LYS D C     1 
ATOM   14402 O  O     . LYS D 2 150 ? 162.222 93.138  136.743 1.00 27.90 ?  129 LYS D O     1 
ATOM   14403 C  CB    . LYS D 2 150 ? 165.504 93.353  136.198 1.00 31.17 ?  129 LYS D CB    1 
ATOM   14404 C  CG    . LYS D 2 150 ? 165.379 93.393  137.707 1.00 33.66 ?  129 LYS D CG    1 
ATOM   14405 C  CD    . LYS D 2 150 ? 166.751 93.705  138.324 1.00 38.08 ?  129 LYS D CD    1 
ATOM   14406 C  CE    . LYS D 2 150 ? 166.631 94.368  139.701 1.00 40.20 ?  129 LYS D CE    1 
ATOM   14407 N  NZ    . LYS D 2 150 ? 166.647 93.379  140.812 1.00 42.60 1  129 LYS D NZ    1 
ATOM   14408 N  N     . TYR D 2 151 ? 162.808 95.062  135.728 1.00 27.36 ?  130 TYR D N     1 
ATOM   14409 C  CA    . TYR D 2 151 ? 161.729 95.839  136.364 1.00 26.56 ?  130 TYR D CA    1 
ATOM   14410 C  C     . TYR D 2 151 ? 160.371 95.562  135.738 1.00 25.66 ?  130 TYR D C     1 
ATOM   14411 O  O     . TYR D 2 151 ? 159.367 95.502  136.455 1.00 25.61 ?  130 TYR D O     1 
ATOM   14412 C  CB    . TYR D 2 151 ? 162.052 97.347  136.387 1.00 26.32 ?  130 TYR D CB    1 
ATOM   14413 C  CG    . TYR D 2 151 ? 163.477 97.611  136.834 1.00 27.20 ?  130 TYR D CG    1 
ATOM   14414 C  CD1   . TYR D 2 151 ? 163.858 97.392  138.158 1.00 27.31 ?  130 TYR D CD1   1 
ATOM   14415 C  CD2   . TYR D 2 151 ? 164.452 98.023  135.927 1.00 27.22 ?  130 TYR D CD2   1 
ATOM   14416 C  CE1   . TYR D 2 151 ? 165.171 97.599  138.574 1.00 29.65 ?  130 TYR D CE1   1 
ATOM   14417 C  CE2   . TYR D 2 151 ? 165.778 98.234  136.335 1.00 28.75 ?  130 TYR D CE2   1 
ATOM   14418 C  CZ    . TYR D 2 151 ? 166.117 98.024  137.675 1.00 29.17 ?  130 TYR D CZ    1 
ATOM   14419 O  OH    . TYR D 2 151 ? 167.404 98.220  138.121 1.00 30.61 ?  130 TYR D OH    1 
ATOM   14420 N  N     . LEU D 2 152 ? 160.344 95.390  134.415 1.00 24.87 ?  131 LEU D N     1 
ATOM   14421 C  CA    . LEU D 2 152 ? 159.121 94.978  133.733 1.00 24.37 ?  131 LEU D CA    1 
ATOM   14422 C  C     . LEU D 2 152 ? 158.700 93.578  134.198 1.00 24.18 ?  131 LEU D C     1 
ATOM   14423 O  O     . LEU D 2 152 ? 157.552 93.380  134.596 1.00 23.16 ?  131 LEU D O     1 
ATOM   14424 C  CB    . LEU D 2 152 ? 159.246 95.022  132.207 1.00 24.45 ?  131 LEU D CB    1 
ATOM   14425 C  CG    . LEU D 2 152 ? 157.867 94.610  131.660 1.00 26.33 ?  131 LEU D CG    1 
ATOM   14426 C  CD1   . LEU D 2 152 ? 156.848 95.745  131.831 1.00 25.00 ?  131 LEU D CD1   1 
ATOM   14427 C  CD2   . LEU D 2 152 ? 157.895 94.092  130.251 1.00 29.15 ?  131 LEU D CD2   1 
ATOM   14428 N  N     . GLN D 2 153 ? 159.636 92.628  134.176 1.00 24.07 ?  132 GLN D N     1 
ATOM   14429 C  CA    . GLN D 2 153 ? 159.349 91.263  134.666 1.00 24.99 ?  132 GLN D CA    1 
ATOM   14430 C  C     . GLN D 2 153 ? 158.881 91.218  136.118 1.00 24.24 ?  132 GLN D C     1 
ATOM   14431 O  O     . GLN D 2 153 ? 157.911 90.512  136.449 1.00 23.75 ?  132 GLN D O     1 
ATOM   14432 C  CB    . GLN D 2 153 ? 160.538 90.314  134.442 1.00 25.84 ?  132 GLN D CB    1 
ATOM   14433 C  CG    . GLN D 2 153 ? 160.771 89.951  132.951 1.00 28.48 ?  132 GLN D CG    1 
ATOM   14434 C  CD    . GLN D 2 153 ? 159.581 89.232  132.295 1.00 30.95 ?  132 GLN D CD    1 
ATOM   14435 O  OE1   . GLN D 2 153 ? 158.902 88.434  132.929 1.00 31.78 ?  132 GLN D OE1   1 
ATOM   14436 N  NE2   . GLN D 2 153 ? 159.343 89.512  131.012 1.00 32.81 ?  132 GLN D NE2   1 
ATOM   14437 N  N     . LYS D 2 154 ? 159.544 91.968  136.993 1.00 24.00 ?  133 LYS D N     1 
ATOM   14438 C  CA    . LYS D 2 154 ? 159.142 91.942  138.399 1.00 24.43 ?  133 LYS D CA    1 
ATOM   14439 C  C     . LYS D 2 154 ? 157.648 92.260  138.558 1.00 23.40 ?  133 LYS D C     1 
ATOM   14440 O  O     . LYS D 2 154 ? 156.907 91.488  139.172 1.00 22.68 ?  133 LYS D O     1 
ATOM   14441 C  CB    . LYS D 2 154 ? 159.970 92.889  139.274 1.00 24.64 ?  133 LYS D CB    1 
ATOM   14442 C  CG    . LYS D 2 154 ? 159.537 92.799  140.748 1.00 28.01 ?  133 LYS D CG    1 
ATOM   14443 C  CD    . LYS D 2 154 ? 160.418 93.569  141.704 1.00 32.56 ?  133 LYS D CD    1 
ATOM   14444 C  CE    . LYS D 2 154 ? 161.776 92.926  141.842 1.00 34.45 ?  133 LYS D CE    1 
ATOM   14445 N  NZ    . LYS D 2 154 ? 162.635 93.711  142.784 1.00 36.11 1  133 LYS D NZ    1 
ATOM   14446 N  N     . LYS D 2 155 ? 157.208 93.388  138.003 1.00 23.07 ?  134 LYS D N     1 
ATOM   14447 C  CA    . LYS D 2 155 ? 155.797 93.753  138.116 1.00 22.70 ?  134 LYS D CA    1 
ATOM   14448 C  C     . LYS D 2 155 ? 154.882 92.799  137.350 1.00 21.96 ?  134 LYS D C     1 
ATOM   14449 O  O     . LYS D 2 155 ? 153.844 92.409  137.875 1.00 22.25 ?  134 LYS D O     1 
ATOM   14450 C  CB    . LYS D 2 155 ? 155.537 95.227  137.757 1.00 22.70 ?  134 LYS D CB    1 
ATOM   14451 C  CG    . LYS D 2 155 ? 155.802 95.634  136.321 1.00 23.62 ?  134 LYS D CG    1 
ATOM   14452 C  CD    . LYS D 2 155 ? 155.416 97.100  136.138 1.00 25.32 ?  134 LYS D CD    1 
ATOM   14453 C  CE    . LYS D 2 155 ? 156.348 97.779  135.138 1.00 27.09 ?  134 LYS D CE    1 
ATOM   14454 N  NZ    . LYS D 2 155 ? 155.926 99.191  134.903 1.00 26.65 1  134 LYS D NZ    1 
ATOM   14455 N  N     . ALA D 2 156 ? 155.261 92.391  136.138 1.00 21.76 ?  135 ALA D N     1 
ATOM   14456 C  CA    . ALA D 2 156 ? 154.399 91.475  135.368 1.00 21.83 ?  135 ALA D CA    1 
ATOM   14457 C  C     . ALA D 2 156 ? 154.151 90.168  136.142 1.00 22.30 ?  135 ALA D C     1 
ATOM   14458 O  O     . ALA D 2 156 ? 153.009 89.713  136.256 1.00 21.92 ?  135 ALA D O     1 
ATOM   14459 C  CB    . ALA D 2 156 ? 154.994 91.179  133.980 1.00 22.30 ?  135 ALA D CB    1 
ATOM   14460 N  N     . GLN D 2 157 ? 155.216 89.585  136.694 1.00 22.15 ?  136 GLN D N     1 
ATOM   14461 C  CA    . GLN D 2 157 ? 155.086 88.316  137.418 1.00 22.38 ?  136 GLN D CA    1 
ATOM   14462 C  C     . GLN D 2 157 ? 154.394 88.447  138.781 1.00 21.59 ?  136 GLN D C     1 
ATOM   14463 O  O     . GLN D 2 157 ? 153.715 87.519  139.221 1.00 21.44 ?  136 GLN D O     1 
ATOM   14464 C  CB    . GLN D 2 157 ? 156.441 87.599  137.558 1.00 22.94 ?  136 GLN D CB    1 
ATOM   14465 C  CG    . GLN D 2 157 ? 157.148 87.283  136.230 1.00 25.31 ?  136 GLN D CG    1 
ATOM   14466 C  CD    . GLN D 2 157 ? 156.229 86.678  135.165 1.00 28.02 ?  136 GLN D CD    1 
ATOM   14467 O  OE1   . GLN D 2 157 ? 155.357 85.853  135.457 1.00 27.14 ?  136 GLN D OE1   1 
ATOM   14468 N  NE2   . GLN D 2 157 ? 156.435 87.089  133.915 1.00 29.47 ?  136 GLN D NE2   1 
ATOM   14469 N  N     . MET D 2 158 ? 154.566 89.581  139.452 1.00 21.52 ?  137 MET D N     1 
ATOM   14470 C  CA    . MET D 2 158 ? 153.839 89.835  140.707 1.00 22.20 ?  137 MET D CA    1 
ATOM   14471 C  C     . MET D 2 158 ? 152.320 89.816  140.501 1.00 21.84 ?  137 MET D C     1 
ATOM   14472 O  O     . MET D 2 158 ? 151.586 89.212  141.287 1.00 21.91 ?  137 MET D O     1 
ATOM   14473 C  CB    . MET D 2 158 ? 154.257 91.165  141.335 1.00 22.52 ?  137 MET D CB    1 
ATOM   14474 C  CG    . MET D 2 158 ? 155.612 91.112  142.056 1.00 25.81 ?  137 MET D CG    1 
ATOM   14475 S  SD    . MET D 2 158 ? 156.103 92.697  142.788 1.00 31.19 ?  137 MET D SD    1 
ATOM   14476 C  CE    . MET D 2 158 ? 154.786 92.863  143.965 1.00 23.91 ?  137 MET D CE    1 
ATOM   14477 N  N     . ILE D 2 159 ? 151.867 90.478  139.439 1.00 21.41 ?  138 ILE D N     1 
ATOM   14478 C  CA    . ILE D 2 159 ? 150.446 90.560  139.113 1.00 21.51 ?  138 ILE D CA    1 
ATOM   14479 C  C     . ILE D 2 159 ? 149.905 89.176  138.721 1.00 21.77 ?  138 ILE D C     1 
ATOM   14480 O  O     . ILE D 2 159 ? 148.874 88.731  139.250 1.00 21.44 ?  138 ILE D O     1 
ATOM   14481 C  CB    . ILE D 2 159 ? 150.194 91.647  137.997 1.00 21.49 ?  138 ILE D CB    1 
ATOM   14482 C  CG1   . ILE D 2 159 ? 150.602 93.047  138.481 1.00 21.16 ?  138 ILE D CG1   1 
ATOM   14483 C  CG2   . ILE D 2 159 ? 148.742 91.641  137.505 1.00 22.34 ?  138 ILE D CG2   1 
ATOM   14484 C  CD1   . ILE D 2 159 ? 149.809 93.576  139.695 1.00 23.85 ?  138 ILE D CD1   1 
ATOM   14485 N  N     . VAL D 2 160 ? 150.617 88.504  137.809 1.00 21.96 ?  139 VAL D N     1 
ATOM   14486 C  CA    . VAL D 2 160 ? 150.244 87.176  137.299 1.00 22.59 ?  139 VAL D CA    1 
ATOM   14487 C  C     . VAL D 2 160 ? 150.208 86.145  138.436 1.00 22.36 ?  139 VAL D C     1 
ATOM   14488 O  O     . VAL D 2 160 ? 149.336 85.271  138.459 1.00 21.64 ?  139 VAL D O     1 
ATOM   14489 C  CB    . VAL D 2 160 ? 151.203 86.718  136.149 1.00 23.08 ?  139 VAL D CB    1 
ATOM   14490 C  CG1   . VAL D 2 160 ? 151.092 85.210  135.857 1.00 24.33 ?  139 VAL D CG1   1 
ATOM   14491 C  CG2   . VAL D 2 160 ? 150.935 87.525  134.868 1.00 22.87 ?  139 VAL D CG2   1 
ATOM   14492 N  N     . GLY D 2 161 ? 151.152 86.262  139.375 1.00 22.21 ?  140 GLY D N     1 
ATOM   14493 C  CA    . GLY D 2 161 ? 151.187 85.394  140.549 1.00 22.50 ?  140 GLY D CA    1 
ATOM   14494 C  C     . GLY D 2 161 ? 149.890 85.444  141.350 1.00 22.88 ?  140 GLY D C     1 
ATOM   14495 O  O     . GLY D 2 161 ? 149.370 84.401  141.771 1.00 23.54 ?  140 GLY D O     1 
ATOM   14496 N  N     . LEU D 2 162 ? 149.356 86.649  141.551 1.00 22.25 ?  141 LEU D N     1 
ATOM   14497 C  CA    . LEU D 2 162 ? 148.091 86.803  142.276 1.00 22.48 ?  141 LEU D CA    1 
ATOM   14498 C  C     . LEU D 2 162 ? 146.885 86.259  141.507 1.00 22.27 ?  141 LEU D C     1 
ATOM   14499 O  O     . LEU D 2 162 ? 145.965 85.714  142.120 1.00 22.31 ?  141 LEU D O     1 
ATOM   14500 C  CB    . LEU D 2 162 ? 147.871 88.256  142.744 1.00 22.07 ?  141 LEU D CB    1 
ATOM   14501 C  CG    . LEU D 2 162 ? 148.749 88.668  143.946 1.00 22.81 ?  141 LEU D CG    1 
ATOM   14502 C  CD1   . LEU D 2 162 ? 148.898 90.184  144.058 1.00 21.65 ?  141 LEU D CD1   1 
ATOM   14503 C  CD2   . LEU D 2 162 ? 148.280 88.046  145.266 1.00 23.35 ?  141 LEU D CD2   1 
ATOM   14504 N  N     . TYR D 2 163 ? 146.880 86.401  140.179 1.00 22.63 ?  142 TYR D N     1 
ATOM   14505 C  CA    . TYR D 2 163 ? 145.826 85.784  139.350 1.00 23.30 ?  142 TYR D CA    1 
ATOM   14506 C  C     . TYR D 2 163 ? 145.864 84.263  139.421 1.00 23.40 ?  142 TYR D C     1 
ATOM   14507 O  O     . TYR D 2 163 ? 144.827 83.620  139.471 1.00 23.75 ?  142 TYR D O     1 
ATOM   14508 C  CB    . TYR D 2 163 ? 145.957 86.165  137.882 1.00 23.22 ?  142 TYR D CB    1 
ATOM   14509 C  CG    . TYR D 2 163 ? 145.832 87.630  137.563 1.00 24.01 ?  142 TYR D CG    1 
ATOM   14510 C  CD1   . TYR D 2 163 ? 145.169 88.500  138.419 1.00 24.47 ?  142 TYR D CD1   1 
ATOM   14511 C  CD2   . TYR D 2 163 ? 146.377 88.140  136.389 1.00 24.62 ?  142 TYR D CD2   1 
ATOM   14512 C  CE1   . TYR D 2 163 ? 145.054 89.842  138.121 1.00 26.33 ?  142 TYR D CE1   1 
ATOM   14513 C  CE2   . TYR D 2 163 ? 146.258 89.484  136.072 1.00 26.07 ?  142 TYR D CE2   1 
ATOM   14514 C  CZ    . TYR D 2 163 ? 145.588 90.327  136.949 1.00 26.65 ?  142 TYR D CZ    1 
ATOM   14515 O  OH    . TYR D 2 163 ? 145.468 91.667  136.662 1.00 31.13 ?  142 TYR D OH    1 
ATOM   14516 N  N     . LYS D 2 164 ? 147.062 83.693  139.414 1.00 23.70 ?  143 LYS D N     1 
ATOM   14517 C  CA    . LYS D 2 164 ? 147.221 82.233  139.501 1.00 24.47 ?  143 LYS D CA    1 
ATOM   14518 C  C     . LYS D 2 164 ? 146.853 81.653  140.877 1.00 24.55 ?  143 LYS D C     1 
ATOM   14519 O  O     . LYS D 2 164 ? 146.622 80.449  141.007 1.00 24.49 ?  143 LYS D O     1 
ATOM   14520 C  CB    . LYS D 2 164 ? 148.654 81.841  139.134 1.00 24.98 ?  143 LYS D CB    1 
ATOM   14521 C  CG    . LYS D 2 164 ? 148.974 81.908  137.633 1.00 27.10 ?  143 LYS D CG    1 
ATOM   14522 C  CD    . LYS D 2 164 ? 150.379 81.383  137.382 1.00 30.75 ?  143 LYS D CD    1 
ATOM   14523 C  CE    . LYS D 2 164 ? 150.731 81.321  135.896 1.00 32.81 ?  143 LYS D CE    1 
ATOM   14524 N  NZ    . LYS D 2 164 ? 152.172 80.898  135.672 1.00 33.68 1  143 LYS D NZ    1 
ATOM   14525 N  N     . ALA D 2 165 ? 146.812 82.505  141.897 1.00 24.18 ?  144 ALA D N     1 
ATOM   14526 C  CA    . ALA D 2 165 ? 146.543 82.061  143.267 1.00 25.04 ?  144 ALA D CA    1 
ATOM   14527 C  C     . ALA D 2 165 ? 145.061 82.087  143.667 1.00 25.00 ?  144 ALA D C     1 
ATOM   14528 O  O     . ALA D 2 165 ? 144.718 81.699  144.794 1.00 25.50 ?  144 ALA D O     1 
ATOM   14529 C  CB    . ALA D 2 165 ? 147.382 82.870  144.271 1.00 25.02 ?  144 ALA D CB    1 
ATOM   14530 N  N     . ILE D 2 166 ? 144.186 82.541  142.767 1.00 24.60 ?  145 ILE D N     1 
ATOM   14531 C  CA    . ILE D 2 166 ? 142.748 82.528  143.038 1.00 24.40 ?  145 ILE D CA    1 
ATOM   14532 C  C     . ILE D 2 166 ? 142.276 81.076  143.202 1.00 25.75 ?  145 ILE D C     1 
ATOM   14533 O  O     . ILE D 2 166 ? 142.620 80.206  142.394 1.00 25.84 ?  145 ILE D O     1 
ATOM   14534 C  CB    . ILE D 2 166 ? 141.906 83.208  141.921 1.00 24.15 ?  145 ILE D CB    1 
ATOM   14535 C  CG1   . ILE D 2 166 ? 142.450 84.596  141.587 1.00 23.15 ?  145 ILE D CG1   1 
ATOM   14536 C  CG2   . ILE D 2 166 ? 140.439 83.300  142.341 1.00 22.72 ?  145 ILE D CG2   1 
ATOM   14537 C  CD1   . ILE D 2 166 ? 141.828 85.219  140.355 1.00 21.70 ?  145 ILE D CD1   1 
ATOM   14538 N  N     . GLN D 2 167 ? 141.524 80.822  144.264 1.00 26.52 ?  146 GLN D N     1 
ATOM   14539 C  CA    . GLN D 2 167 ? 140.962 79.500  144.504 1.00 28.77 ?  146 GLN D CA    1 
ATOM   14540 C  C     . GLN D 2 167 ? 139.445 79.530  144.368 1.00 29.20 ?  146 GLN D C     1 
ATOM   14541 O  O     . GLN D 2 167 ? 138.791 80.496  144.789 1.00 28.89 ?  146 GLN D O     1 
ATOM   14542 C  CB    . GLN D 2 167 ? 141.354 79.001  145.892 1.00 29.04 ?  146 GLN D CB    1 
ATOM   14543 C  CG    . GLN D 2 167 ? 142.846 78.771  146.047 1.00 31.87 ?  146 GLN D CG    1 
ATOM   14544 C  CD    . GLN D 2 167 ? 143.366 79.300  147.356 1.00 35.35 ?  146 GLN D CD    1 
ATOM   14545 O  OE1   . GLN D 2 167 ? 143.051 78.768  148.424 1.00 36.91 ?  146 GLN D OE1   1 
ATOM   14546 N  NE2   . GLN D 2 167 ? 144.173 80.357  147.288 1.00 36.19 ?  146 GLN D NE2   1 
ATOM   14547 N  N     . LYS D 2 168 ? 138.892 78.471  143.782 1.00 30.29 ?  147 LYS D N     1 
ATOM   14548 C  CA    . LYS D 2 168 ? 137.442 78.341  143.645 1.00 31.24 ?  147 LYS D CA    1 
ATOM   14549 C  C     . LYS D 2 168 ? 136.736 78.564  144.982 1.00 31.73 ?  147 LYS D C     1 
ATOM   14550 O  O     . LYS D 2 168 ? 137.183 78.056  146.010 1.00 31.46 ?  147 LYS D O     1 
ATOM   14551 C  CB    . LYS D 2 168 ? 137.077 76.977  143.065 1.00 31.92 ?  147 LYS D CB    1 
ATOM   14552 C  CG    . LYS D 2 168 ? 135.587 76.803  142.814 1.00 33.23 ?  147 LYS D CG    1 
ATOM   14553 C  CD    . LYS D 2 168 ? 135.295 75.540  142.021 1.00 36.06 ?  147 LYS D CD    1 
ATOM   14554 C  CE    . LYS D 2 168 ? 133.805 75.339  141.839 1.00 35.46 ?  147 LYS D CE    1 
ATOM   14555 N  NZ    . LYS D 2 168 ? 133.215 76.326  140.897 1.00 38.24 1  147 LYS D NZ    1 
ATOM   14556 N  N     . ASP D 2 169 ? 135.650 79.342  144.956 1.00 32.28 ?  148 ASP D N     1 
ATOM   14557 C  CA    . ASP D 2 169 ? 134.848 79.656  146.151 1.00 33.45 ?  148 ASP D CA    1 
ATOM   14558 C  C     . ASP D 2 169 ? 135.610 80.296  147.310 1.00 33.30 ?  148 ASP D C     1 
ATOM   14559 O  O     . ASP D 2 169 ? 135.191 80.189  148.465 1.00 34.32 ?  148 ASP D O     1 
ATOM   14560 C  CB    . ASP D 2 169 ? 134.126 78.403  146.674 1.00 34.63 ?  148 ASP D CB    1 
ATOM   14561 C  CG    . ASP D 2 169 ? 132.970 77.974  145.798 1.00 36.09 ?  148 ASP D CG    1 
ATOM   14562 O  OD1   . ASP D 2 169 ? 132.537 78.743  144.914 1.00 37.80 ?  148 ASP D OD1   1 
ATOM   14563 O  OD2   . ASP D 2 169 ? 132.487 76.843  146.011 1.00 40.47 -1 148 ASP D OD2   1 
ATOM   14564 N  N     . ASP D 2 170 ? 136.733 80.938  147.027 1.00 32.58 ?  149 ASP D N     1 
ATOM   14565 C  CA    . ASP D 2 170 ? 137.444 81.674  148.069 1.00 32.01 ?  149 ASP D CA    1 
ATOM   14566 C  C     . ASP D 2 170 ? 137.499 83.147  147.680 1.00 30.59 ?  149 ASP D C     1 
ATOM   14567 O  O     . ASP D 2 170 ? 138.282 83.546  146.817 1.00 29.11 ?  149 ASP D O     1 
ATOM   14568 C  CB    . ASP D 2 170 ? 138.839 81.092  148.310 1.00 32.93 ?  149 ASP D CB    1 
ATOM   14569 C  CG    . ASP D 2 170 ? 139.704 81.970  149.204 1.00 35.05 ?  149 ASP D CG    1 
ATOM   14570 O  OD1   . ASP D 2 170 ? 139.180 82.701  150.073 1.00 39.25 ?  149 ASP D OD1   1 
ATOM   14571 O  OD2   . ASP D 2 170 ? 140.932 81.917  149.049 1.00 39.22 -1 149 ASP D OD2   1 
ATOM   14572 N  N     . GLU D 2 171 ? 136.645 83.936  148.326 1.00 29.34 ?  150 GLU D N     1 
ATOM   14573 C  CA    . GLU D 2 171 ? 136.498 85.352  148.004 1.00 28.51 ?  150 GLU D CA    1 
ATOM   14574 C  C     . GLU D 2 171 ? 137.695 86.207  148.444 1.00 27.27 ?  150 GLU D C     1 
ATOM   14575 O  O     . GLU D 2 171 ? 137.915 87.276  147.897 1.00 26.62 ?  150 GLU D O     1 
ATOM   14576 C  CB    . GLU D 2 171 ? 135.181 85.901  148.569 1.00 29.09 ?  150 GLU D CB    1 
ATOM   14577 C  CG    . GLU D 2 171 ? 135.114 86.010  150.091 1.00 30.68 ?  150 GLU D CG    1 
ATOM   14578 C  CD    . GLU D 2 171 ? 133.727 86.386  150.586 1.00 33.92 ?  150 GLU D CD    1 
ATOM   14579 O  OE1   . GLU D 2 171 ? 132.826 86.604  149.739 1.00 36.31 ?  150 GLU D OE1   1 
ATOM   14580 O  OE2   . GLU D 2 171 ? 133.526 86.472  151.818 1.00 34.02 -1 150 GLU D OE2   1 
ATOM   14581 N  N     . ILE D 2 172 ? 138.474 85.723  149.411 1.00 26.19 ?  151 ILE D N     1 
ATOM   14582 C  CA    . ILE D 2 172 ? 139.675 86.435  149.850 1.00 25.49 ?  151 ILE D CA    1 
ATOM   14583 C  C     . ILE D 2 172 ? 140.733 86.440  148.743 1.00 24.61 ?  151 ILE D C     1 
ATOM   14584 O  O     . ILE D 2 172 ? 141.295 87.493  148.416 1.00 24.09 ?  151 ILE D O     1 
ATOM   14585 C  CB    . ILE D 2 172 ? 140.242 85.860  151.179 1.00 25.98 ?  151 ILE D CB    1 
ATOM   14586 C  CG1   . ILE D 2 172 ? 139.242 86.041  152.321 1.00 26.86 ?  151 ILE D CG1   1 
ATOM   14587 C  CG2   . ILE D 2 172 ? 141.614 86.484  151.551 1.00 26.50 ?  151 ILE D CG2   1 
ATOM   14588 C  CD1   . ILE D 2 172 ? 138.885 87.490  152.620 1.00 27.81 ?  151 ILE D CD1   1 
ATOM   14589 N  N     . SER D 2 173 ? 140.977 85.272  148.158 1.00 23.71 ?  152 SER D N     1 
ATOM   14590 C  CA    . SER D 2 173 ? 141.937 85.147  147.062 1.00 23.38 ?  152 SER D CA    1 
ATOM   14591 C  C     . SER D 2 173 ? 141.451 85.902  145.812 1.00 22.41 ?  152 SER D C     1 
ATOM   14592 O  O     . SER D 2 173 ? 142.251 86.467  145.061 1.00 21.43 ?  152 SER D O     1 
ATOM   14593 C  CB    . SER D 2 173 ? 142.233 83.674  146.752 1.00 23.90 ?  152 SER D CB    1 
ATOM   14594 O  OG    . SER D 2 173 ? 141.136 82.994  146.144 1.00 23.74 ?  152 SER D OG    1 
ATOM   14595 N  N     . LEU D 2 174 ? 140.137 85.926  145.608 1.00 21.63 ?  153 LEU D N     1 
ATOM   14596 C  CA    . LEU D 2 174 ? 139.567 86.694  144.498 1.00 20.75 ?  153 LEU D CA    1 
ATOM   14597 C  C     . LEU D 2 174 ? 139.810 88.186  144.720 1.00 20.96 ?  153 LEU D C     1 
ATOM   14598 O  O     . LEU D 2 174 ? 140.210 88.897  143.798 1.00 20.41 ?  153 LEU D O     1 
ATOM   14599 C  CB    . LEU D 2 174 ? 138.062 86.405  144.329 1.00 20.62 ?  153 LEU D CB    1 
ATOM   14600 C  CG    . LEU D 2 174 ? 137.329 87.183  143.215 1.00 19.55 ?  153 LEU D CG    1 
ATOM   14601 C  CD1   . LEU D 2 174 ? 138.044 87.016  141.869 1.00 20.44 ?  153 LEU D CD1   1 
ATOM   14602 C  CD2   . LEU D 2 174 ? 135.866 86.726  143.129 1.00 20.99 ?  153 LEU D CD2   1 
ATOM   14603 N  N     . PHE D 2 175 ? 139.573 88.654  145.944 1.00 21.07 ?  154 PHE D N     1 
ATOM   14604 C  CA    . PHE D 2 175 ? 139.787 90.060  146.281 1.00 21.32 ?  154 PHE D CA    1 
ATOM   14605 C  C     . PHE D 2 175 ? 141.237 90.485  146.023 1.00 21.08 ?  154 PHE D C     1 
ATOM   14606 O  O     . PHE D 2 175 ? 141.491 91.543  145.445 1.00 20.85 ?  154 PHE D O     1 
ATOM   14607 C  CB    . PHE D 2 175 ? 139.412 90.326  147.743 1.00 21.20 ?  154 PHE D CB    1 
ATOM   14608 C  CG    . PHE D 2 175 ? 139.851 91.668  148.248 1.00 22.46 ?  154 PHE D CG    1 
ATOM   14609 C  CD1   . PHE D 2 175 ? 139.005 92.772  148.146 1.00 21.21 ?  154 PHE D CD1   1 
ATOM   14610 C  CD2   . PHE D 2 175 ? 141.109 91.837  148.834 1.00 22.53 ?  154 PHE D CD2   1 
ATOM   14611 C  CE1   . PHE D 2 175 ? 139.395 94.009  148.618 1.00 22.11 ?  154 PHE D CE1   1 
ATOM   14612 C  CE2   . PHE D 2 175 ? 141.518 93.085  149.296 1.00 23.26 ?  154 PHE D CE2   1 
ATOM   14613 C  CZ    . PHE D 2 175 ? 140.658 94.174  149.194 1.00 22.08 ?  154 PHE D CZ    1 
ATOM   14614 N  N     . LYS D 2 176 ? 142.180 89.660  146.466 1.00 21.14 ?  155 LYS D N     1 
ATOM   14615 C  CA    . LYS D 2 176 ? 143.606 89.936  146.264 1.00 20.93 ?  155 LYS D CA    1 
ATOM   14616 C  C     . LYS D 2 176 ? 143.963 90.079  144.786 1.00 20.61 ?  155 LYS D C     1 
ATOM   14617 O  O     . LYS D 2 176 ? 144.718 90.978  144.401 1.00 20.62 ?  155 LYS D O     1 
ATOM   14618 C  CB    . LYS D 2 176 ? 144.442 88.846  146.916 1.00 21.27 ?  155 LYS D CB    1 
ATOM   14619 C  CG    . LYS D 2 176 ? 144.436 88.955  148.416 1.00 22.04 ?  155 LYS D CG    1 
ATOM   14620 C  CD    . LYS D 2 176 ? 145.179 87.814  149.090 1.00 25.24 ?  155 LYS D CD    1 
ATOM   14621 C  CE    . LYS D 2 176 ? 145.178 88.036  150.581 1.00 25.83 ?  155 LYS D CE    1 
ATOM   14622 N  NZ    . LYS D 2 176 ? 145.905 86.969  151.329 1.00 26.64 1  155 LYS D NZ    1 
ATOM   14623 N  N     . ALA D 2 177 ? 143.394 89.205  143.962 1.00 20.02 ?  156 ALA D N     1 
ATOM   14624 C  CA    . ALA D 2 177 ? 143.564 89.294  142.514 1.00 19.86 ?  156 ALA D CA    1 
ATOM   14625 C  C     . ALA D 2 177 ? 142.922 90.562  141.932 1.00 19.61 ?  156 ALA D C     1 
ATOM   14626 O  O     . ALA D 2 177 ? 143.437 91.151  140.980 1.00 19.69 ?  156 ALA D O     1 
ATOM   14627 C  CB    . ALA D 2 177 ? 142.987 88.076  141.871 1.00 19.99 ?  156 ALA D CB    1 
ATOM   14628 N  N     . MET D 2 178 ? 141.790 90.973  142.499 1.00 19.75 ?  157 MET D N     1 
ATOM   14629 C  CA    . MET D 2 178 ? 141.093 92.185  142.023 1.00 18.89 ?  157 MET D CA    1 
ATOM   14630 C  C     . MET D 2 178 ? 141.917 93.424  142.340 1.00 18.62 ?  157 MET D C     1 
ATOM   14631 O  O     . MET D 2 178 ? 142.000 94.349  141.524 1.00 18.10 ?  157 MET D O     1 
ATOM   14632 C  CB    . MET D 2 178 ? 139.705 92.299  142.648 1.00 18.82 ?  157 MET D CB    1 
ATOM   14633 C  CG    . MET D 2 178 ? 138.698 91.327  142.054 1.00 20.20 ?  157 MET D CG    1 
ATOM   14634 S  SD    . MET D 2 178 ? 137.141 91.424  142.949 1.00 23.78 ?  157 MET D SD    1 
ATOM   14635 C  CE    . MET D 2 178 ? 136.115 90.399  141.898 1.00 22.62 ?  157 MET D CE    1 
ATOM   14636 N  N     . VAL D 2 179 ? 142.543 93.417  143.518 1.00 18.34 ?  158 VAL D N     1 
ATOM   14637 C  CA    . VAL D 2 179 ? 143.460 94.476  143.912 1.00 18.75 ?  158 VAL D CA    1 
ATOM   14638 C  C     . VAL D 2 179 ? 144.615 94.570  142.923 1.00 18.86 ?  158 VAL D C     1 
ATOM   14639 O  O     . VAL D 2 179 ? 144.960 95.677  142.475 1.00 18.79 ?  158 VAL D O     1 
ATOM   14640 C  CB    . VAL D 2 179 ? 144.012 94.285  145.350 1.00 19.02 ?  158 VAL D CB    1 
ATOM   14641 C  CG1   . VAL D 2 179 ? 145.136 95.295  145.624 1.00 19.10 ?  158 VAL D CG1   1 
ATOM   14642 C  CG2   . VAL D 2 179 ? 142.887 94.420  146.388 1.00 18.94 ?  158 VAL D CG2   1 
ATOM   14643 N  N     . ALA D 2 180 ? 145.211 93.415  142.601 1.00 18.96 ?  159 ALA D N     1 
ATOM   14644 C  CA    . ALA D 2 180 ? 146.264 93.339  141.586 1.00 19.05 ?  159 ALA D CA    1 
ATOM   14645 C  C     . ALA D 2 180 ? 145.778 93.896  140.246 1.00 18.67 ?  159 ALA D C     1 
ATOM   14646 O  O     . ALA D 2 180 ? 146.481 94.689  139.606 1.00 17.72 ?  159 ALA D O     1 
ATOM   14647 C  CB    . ALA D 2 180 ? 146.766 91.893  141.423 1.00 19.43 ?  159 ALA D CB    1 
ATOM   14648 N  N     . SER D 2 181 ? 144.563 93.506  139.847 1.00 18.49 ?  160 SER D N     1 
ATOM   14649 C  CA    . SER D 2 181 ? 143.985 93.985  138.590 1.00 18.51 ?  160 SER D CA    1 
ATOM   14650 C  C     . SER D 2 181 ? 143.782 95.500  138.579 1.00 18.23 ?  160 SER D C     1 
ATOM   14651 O  O     . SER D 2 181 ? 144.142 96.169  137.620 1.00 18.18 ?  160 SER D O     1 
ATOM   14652 C  CB    . SER D 2 181 ? 142.659 93.282  138.285 1.00 18.51 ?  160 SER D CB    1 
ATOM   14653 O  OG    . SER D 2 181 ? 142.225 93.647  136.989 1.00 19.42 ?  160 SER D OG    1 
ATOM   14654 N  N     . VAL D 2 182 ? 143.209 96.036  139.655 1.00 18.43 ?  161 VAL D N     1 
ATOM   14655 C  CA    . VAL D 2 182 ? 143.042 97.488  139.776 1.00 18.09 ?  161 VAL D CA    1 
ATOM   14656 C  C     . VAL D 2 182 ? 144.396 98.206  139.740 1.00 18.41 ?  161 VAL D C     1 
ATOM   14657 O  O     . VAL D 2 182 ? 144.539 99.233  139.073 1.00 18.52 ?  161 VAL D O     1 
ATOM   14658 C  CB    . VAL D 2 182 ? 142.240 97.872  141.026 1.00 17.71 ?  161 VAL D CB    1 
ATOM   14659 C  CG1   . VAL D 2 182 ? 142.261 99.403  141.247 1.00 16.02 ?  161 VAL D CG1   1 
ATOM   14660 C  CG2   . VAL D 2 182 ? 140.795 97.374  140.877 1.00 17.78 ?  161 VAL D CG2   1 
ATOM   14661 N  N     . TYR D 2 183 ? 145.396 97.641  140.419 1.00 19.06 ?  162 TYR D N     1 
ATOM   14662 C  CA    . TYR D 2 183 ? 146.728 98.238  140.390 1.00 19.73 ?  162 TYR D CA    1 
ATOM   14663 C  C     . TYR D 2 183 ? 147.302 98.254  138.980 1.00 19.90 ?  162 TYR D C     1 
ATOM   14664 O  O     . TYR D 2 183 ? 147.979 99.201  138.614 1.00 20.73 ?  162 TYR D O     1 
ATOM   14665 C  CB    . TYR D 2 183 ? 147.703 97.569  141.376 1.00 19.84 ?  162 TYR D CB    1 
ATOM   14666 C  CG    . TYR D 2 183 ? 147.444 97.898  142.832 1.00 20.24 ?  162 TYR D CG    1 
ATOM   14667 C  CD1   . TYR D 2 183 ? 146.581 98.929  143.196 1.00 21.51 ?  162 TYR D CD1   1 
ATOM   14668 C  CD2   . TYR D 2 183 ? 148.083 97.185  143.854 1.00 20.45 ?  162 TYR D CD2   1 
ATOM   14669 C  CE1   . TYR D 2 183 ? 146.348 99.236  144.542 1.00 21.68 ?  162 TYR D CE1   1 
ATOM   14670 C  CE2   . TYR D 2 183 ? 147.873 97.499  145.203 1.00 19.97 ?  162 TYR D CE2   1 
ATOM   14671 C  CZ    . TYR D 2 183 ? 147.001 98.521  145.536 1.00 21.83 ?  162 TYR D CZ    1 
ATOM   14672 O  OH    . TYR D 2 183 ? 146.776 98.835  146.863 1.00 21.96 ?  162 TYR D OH    1 
ATOM   14673 N  N     . LEU D 2 184 ? 147.023 97.230  138.184 1.00 20.22 ?  163 LEU D N     1 
ATOM   14674 C  CA    . LEU D 2 184 ? 147.507 97.226  136.807 1.00 20.89 ?  163 LEU D CA    1 
ATOM   14675 C  C     . LEU D 2 184 ? 146.756 98.278  135.977 1.00 20.72 ?  163 LEU D C     1 
ATOM   14676 O  O     . LEU D 2 184 ? 147.378 99.146  135.372 1.00 21.07 ?  163 LEU D O     1 
ATOM   14677 C  CB    . LEU D 2 184 ? 147.441 95.816  136.186 1.00 21.16 ?  163 LEU D CB    1 
ATOM   14678 C  CG    . LEU D 2 184 ? 147.870 95.619  134.718 1.00 22.77 ?  163 LEU D CG    1 
ATOM   14679 C  CD1   . LEU D 2 184 ? 149.267 96.206  134.417 1.00 22.44 ?  163 LEU D CD1   1 
ATOM   14680 C  CD2   . LEU D 2 184 ? 147.821 94.152  134.321 1.00 24.75 ?  163 LEU D CD2   1 
ATOM   14681 N  N     . GLU D 2 185 ? 145.426 98.215  135.994 1.00 20.65 ?  164 GLU D N     1 
ATOM   14682 C  CA    . GLU D 2 185 ? 144.573 99.116  135.205 1.00 20.69 ?  164 GLU D CA    1 
ATOM   14683 C  C     . GLU D 2 185 ? 144.730 100.598 135.545 1.00 20.64 ?  164 GLU D C     1 
ATOM   14684 O  O     . GLU D 2 185 ? 144.713 101.456 134.650 1.00 20.25 ?  164 GLU D O     1 
ATOM   14685 C  CB    . GLU D 2 185 ? 143.095 98.739  135.380 1.00 21.03 ?  164 GLU D CB    1 
ATOM   14686 C  CG    . GLU D 2 185 ? 142.740 97.305  134.974 1.00 22.19 ?  164 GLU D CG    1 
ATOM   14687 C  CD    . GLU D 2 185 ? 142.490 97.129  133.478 1.00 24.19 ?  164 GLU D CD    1 
ATOM   14688 O  OE1   . GLU D 2 185 ? 142.673 98.074  132.690 1.00 27.97 ?  164 GLU D OE1   1 
ATOM   14689 O  OE2   . GLU D 2 185 ? 142.082 96.037  133.079 1.00 25.47 -1 164 GLU D OE2   1 
ATOM   14690 N  N     . SER D 2 186 ? 144.848 100.895 136.834 1.00 20.42 ?  165 SER D N     1 
ATOM   14691 C  CA    . SER D 2 186 ? 144.754 102.273 137.318 1.00 20.70 ?  165 SER D CA    1 
ATOM   14692 C  C     . SER D 2 186 ? 146.081 102.860 137.798 1.00 20.88 ?  165 SER D C     1 
ATOM   14693 O  O     . SER D 2 186 ? 146.125 104.011 138.232 1.00 21.21 ?  165 SER D O     1 
ATOM   14694 C  CB    . SER D 2 186 ? 143.711 102.379 138.444 1.00 21.25 ?  165 SER D CB    1 
ATOM   14695 O  OG    . SER D 2 186 ? 142.461 101.822 138.062 1.00 20.97 ?  165 SER D OG    1 
ATOM   14696 N  N     . PHE D 2 187 ? 147.167 102.090 137.718 1.00 20.94 ?  166 PHE D N     1 
ATOM   14697 C  CA    . PHE D 2 187 ? 148.416 102.532 138.323 1.00 21.19 ?  166 PHE D CA    1 
ATOM   14698 C  C     . PHE D 2 187 ? 149.639 102.118 137.505 1.00 21.22 ?  166 PHE D C     1 
ATOM   14699 O  O     . PHE D 2 187 ? 150.351 102.994 137.002 1.00 21.10 ?  166 PHE D O     1 
ATOM   14700 C  CB    . PHE D 2 187 ? 148.461 102.104 139.816 1.00 21.63 ?  166 PHE D CB    1 
ATOM   14701 C  CG    . PHE D 2 187 ? 149.837 102.059 140.428 1.00 24.05 ?  166 PHE D CG    1 
ATOM   14702 C  CD1   . PHE D 2 187 ? 150.648 103.193 140.470 1.00 25.52 ?  166 PHE D CD1   1 
ATOM   14703 C  CD2   . PHE D 2 187 ? 150.304 100.885 141.012 1.00 27.03 ?  166 PHE D CD2   1 
ATOM   14704 C  CE1   . PHE D 2 187 ? 151.905 103.145 141.060 1.00 26.73 ?  166 PHE D CE1   1 
ATOM   14705 C  CE2   . PHE D 2 187 ? 151.578 100.831 141.598 1.00 27.36 ?  166 PHE D CE2   1 
ATOM   14706 C  CZ    . PHE D 2 187 ? 152.371 101.961 141.616 1.00 27.87 ?  166 PHE D CZ    1 
ATOM   14707 N  N     . LEU D 2 188 ? 149.848 100.817 137.325 1.00 20.78 ?  167 LEU D N     1 
ATOM   14708 C  CA    . LEU D 2 188 ? 151.064 100.312 136.656 1.00 21.78 ?  167 LEU D CA    1 
ATOM   14709 C  C     . LEU D 2 188 ? 151.221 100.729 135.188 1.00 21.91 ?  167 LEU D C     1 
ATOM   14710 O  O     . LEU D 2 188 ? 152.344 100.907 134.719 1.00 22.87 ?  167 LEU D O     1 
ATOM   14711 C  CB    . LEU D 2 188 ? 151.160 98.790  136.767 1.00 22.32 ?  167 LEU D CB    1 
ATOM   14712 C  CG    . LEU D 2 188 ? 151.380 98.127  138.126 1.00 23.33 ?  167 LEU D CG    1 
ATOM   14713 C  CD1   . LEU D 2 188 ? 151.408 96.621  137.933 1.00 22.43 ?  167 LEU D CD1   1 
ATOM   14714 C  CD2   . LEU D 2 188 ? 152.661 98.608  138.820 1.00 25.71 ?  167 LEU D CD2   1 
ATOM   14715 N  N     . PHE D 2 189 ? 150.107 100.862 134.466 1.00 21.56 ?  168 PHE D N     1 
ATOM   14716 C  CA    . PHE D 2 189 ? 150.134 101.328 133.076 1.00 21.86 ?  168 PHE D CA    1 
ATOM   14717 C  C     . PHE D 2 189 ? 150.659 102.773 132.941 1.00 21.87 ?  168 PHE D C     1 
ATOM   14718 O  O     . PHE D 2 189 ? 151.144 103.169 131.879 1.00 21.79 ?  168 PHE D O     1 
ATOM   14719 C  CB    . PHE D 2 189 ? 148.729 101.280 132.448 1.00 21.79 ?  168 PHE D CB    1 
ATOM   14720 C  CG    . PHE D 2 189 ? 148.291 99.909  131.987 1.00 21.88 ?  168 PHE D CG    1 
ATOM   14721 C  CD1   . PHE D 2 189 ? 149.185 99.023  131.382 1.00 21.44 ?  168 PHE D CD1   1 
ATOM   14722 C  CD2   . PHE D 2 189 ? 146.958 99.521  132.133 1.00 22.82 ?  168 PHE D CD2   1 
ATOM   14723 C  CE1   . PHE D 2 189 ? 148.763 97.758  130.954 1.00 22.35 ?  168 PHE D CE1   1 
ATOM   14724 C  CE2   . PHE D 2 189 ? 146.520 98.266  131.709 1.00 22.08 ?  168 PHE D CE2   1 
ATOM   14725 C  CZ    . PHE D 2 189 ? 147.427 97.375  131.128 1.00 22.60 ?  168 PHE D CZ    1 
ATOM   14726 N  N     . TYR D 2 190 ? 150.539 103.564 134.003 1.00 21.91 ?  169 TYR D N     1 
ATOM   14727 C  CA    . TYR D 2 190 ? 150.722 105.016 133.863 1.00 22.52 ?  169 TYR D CA    1 
ATOM   14728 C  C     . TYR D 2 190 ? 152.168 105.503 133.754 1.00 22.75 ?  169 TYR D C     1 
ATOM   14729 O  O     . TYR D 2 190 ? 152.402 106.547 133.160 1.00 21.93 ?  169 TYR D O     1 
ATOM   14730 C  CB    . TYR D 2 190 ? 149.911 105.790 134.907 1.00 22.67 ?  169 TYR D CB    1 
ATOM   14731 C  CG    . TYR D 2 190 ? 148.442 105.807 134.536 1.00 24.77 ?  169 TYR D CG    1 
ATOM   14732 C  CD1   . TYR D 2 190 ? 147.641 104.675 134.716 1.00 25.65 ?  169 TYR D CD1   1 
ATOM   14733 C  CD2   . TYR D 2 190 ? 147.867 106.937 133.962 1.00 25.94 ?  169 TYR D CD2   1 
ATOM   14734 C  CE1   . TYR D 2 190 ? 146.292 104.681 134.342 1.00 26.62 ?  169 TYR D CE1   1 
ATOM   14735 C  CE2   . TYR D 2 190 ? 146.521 106.959 133.602 1.00 26.91 ?  169 TYR D CE2   1 
ATOM   14736 C  CZ    . TYR D 2 190 ? 145.743 105.833 133.790 1.00 27.39 ?  169 TYR D CZ    1 
ATOM   14737 O  OH    . TYR D 2 190 ? 144.412 105.873 133.419 1.00 27.50 ?  169 TYR D OH    1 
ATOM   14738 N  N     . SER D 2 191 ? 153.128 104.741 134.287 1.00 22.74 ?  170 SER D N     1 
ATOM   14739 C  CA    . SER D 2 191 ? 154.542 105.035 134.022 1.00 23.43 ?  170 SER D CA    1 
ATOM   14740 C  C     . SER D 2 191 ? 154.805 104.919 132.520 1.00 23.08 ?  170 SER D C     1 
ATOM   14741 O  O     . SER D 2 191 ? 155.666 105.594 131.982 1.00 23.67 ?  170 SER D O     1 
ATOM   14742 C  CB    . SER D 2 191 ? 155.482 104.107 134.807 1.00 23.39 ?  170 SER D CB    1 
ATOM   14743 O  OG    . SER D 2 191 ? 155.292 102.746 134.448 1.00 24.10 ?  170 SER D OG    1 
ATOM   14744 N  N     . GLY D 2 192 ? 154.023 104.083 131.850 1.00 22.82 ?  171 GLY D N     1 
ATOM   14745 C  CA    . GLY D 2 192 ? 154.107 103.908 130.406 1.00 22.08 ?  171 GLY D CA    1 
ATOM   14746 C  C     . GLY D 2 192 ? 153.306 104.933 129.620 1.00 22.12 ?  171 GLY D C     1 
ATOM   14747 O  O     . GLY D 2 192 ? 153.834 105.554 128.697 1.00 22.86 ?  171 GLY D O     1 
ATOM   14748 N  N     . PHE D 2 193 ? 152.037 105.117 129.984 1.00 21.48 ?  172 PHE D N     1 
ATOM   14749 C  CA    . PHE D 2 193 ? 151.160 106.094 129.314 1.00 21.06 ?  172 PHE D CA    1 
ATOM   14750 C  C     . PHE D 2 193 ? 151.757 107.501 129.298 1.00 21.13 ?  172 PHE D C     1 
ATOM   14751 O  O     . PHE D 2 193 ? 151.478 108.280 128.386 1.00 21.18 ?  172 PHE D O     1 
ATOM   14752 C  CB    . PHE D 2 193 ? 149.791 106.161 129.989 1.00 21.33 ?  172 PHE D CB    1 
ATOM   14753 C  CG    . PHE D 2 193 ? 148.912 104.955 129.753 1.00 20.93 ?  172 PHE D CG    1 
ATOM   14754 C  CD1   . PHE D 2 193 ? 149.002 104.205 128.581 1.00 20.88 ?  172 PHE D CD1   1 
ATOM   14755 C  CD2   . PHE D 2 193 ? 147.954 104.606 130.696 1.00 19.83 ?  172 PHE D CD2   1 
ATOM   14756 C  CE1   . PHE D 2 193 ? 148.163 103.102 128.377 1.00 22.31 ?  172 PHE D CE1   1 
ATOM   14757 C  CE2   . PHE D 2 193 ? 147.103 103.513 130.493 1.00 20.67 ?  172 PHE D CE2   1 
ATOM   14758 C  CZ    . PHE D 2 193 ? 147.210 102.762 129.332 1.00 21.00 ?  172 PHE D CZ    1 
ATOM   14759 N  N     . TYR D 2 194 ? 152.584 107.815 130.298 1.00 20.48 ?  173 TYR D N     1 
ATOM   14760 C  CA    . TYR D 2 194 ? 153.173 109.146 130.427 1.00 20.76 ?  173 TYR D CA    1 
ATOM   14761 C  C     . TYR D 2 194 ? 153.771 109.642 129.105 1.00 20.53 ?  173 TYR D C     1 
ATOM   14762 O  O     . TYR D 2 194 ? 153.489 110.754 128.649 1.00 19.89 ?  173 TYR D O     1 
ATOM   14763 C  CB    . TYR D 2 194 ? 154.244 109.180 131.545 1.00 20.94 ?  173 TYR D CB    1 
ATOM   14764 C  CG    . TYR D 2 194 ? 154.710 110.590 131.862 1.00 21.56 ?  173 TYR D CG    1 
ATOM   14765 C  CD1   . TYR D 2 194 ? 154.196 111.287 132.958 1.00 22.23 ?  173 TYR D CD1   1 
ATOM   14766 C  CD2   . TYR D 2 194 ? 155.648 111.239 131.050 1.00 22.00 ?  173 TYR D CD2   1 
ATOM   14767 C  CE1   . TYR D 2 194 ? 154.604 112.590 133.237 1.00 21.58 ?  173 TYR D CE1   1 
ATOM   14768 C  CE2   . TYR D 2 194 ? 156.063 112.529 131.325 1.00 20.52 ?  173 TYR D CE2   1 
ATOM   14769 C  CZ    . TYR D 2 194 ? 155.538 113.200 132.416 1.00 21.66 ?  173 TYR D CZ    1 
ATOM   14770 O  OH    . TYR D 2 194 ? 155.932 114.491 132.672 1.00 21.37 ?  173 TYR D OH    1 
ATOM   14771 N  N     . TYR D 2 195 ? 154.573 108.799 128.475 1.00 20.77 ?  174 TYR D N     1 
ATOM   14772 C  CA    . TYR D 2 195 ? 155.353 109.250 127.336 1.00 21.12 ?  174 TYR D CA    1 
ATOM   14773 C  C     . TYR D 2 195 ? 154.495 109.572 126.099 1.00 21.49 ?  174 TYR D C     1 
ATOM   14774 O  O     . TYR D 2 195 ? 154.627 110.669 125.548 1.00 21.60 ?  174 TYR D O     1 
ATOM   14775 C  CB    . TYR D 2 195 ? 156.497 108.272 127.053 1.00 21.23 ?  174 TYR D CB    1 
ATOM   14776 C  CG    . TYR D 2 195 ? 157.733 108.895 126.443 1.00 21.77 ?  174 TYR D CG    1 
ATOM   14777 C  CD1   . TYR D 2 195 ? 158.184 110.158 126.840 1.00 23.28 ?  174 TYR D CD1   1 
ATOM   14778 C  CD2   . TYR D 2 195 ? 158.469 108.205 125.482 1.00 22.87 ?  174 TYR D CD2   1 
ATOM   14779 C  CE1   . TYR D 2 195 ? 159.336 110.721 126.271 1.00 23.81 ?  174 TYR D CE1   1 
ATOM   14780 C  CE2   . TYR D 2 195 ? 159.619 108.756 124.920 1.00 24.09 ?  174 TYR D CE2   1 
ATOM   14781 C  CZ    . TYR D 2 195 ? 160.041 110.009 125.313 1.00 23.51 ?  174 TYR D CZ    1 
ATOM   14782 O  OH    . TYR D 2 195 ? 161.177 110.553 124.744 1.00 25.36 ?  174 TYR D OH    1 
ATOM   14783 N  N     . PRO D 2 196 ? 153.610 108.638 125.664 1.00 21.86 ?  175 PRO D N     1 
ATOM   14784 C  CA    . PRO D 2 196 ? 152.693 108.971 124.563 1.00 22.03 ?  175 PRO D CA    1 
ATOM   14785 C  C     . PRO D 2 196 ? 151.840 110.205 124.851 1.00 22.18 ?  175 PRO D C     1 
ATOM   14786 O  O     . PRO D 2 196 ? 151.608 111.002 123.938 1.00 23.00 ?  175 PRO D O     1 
ATOM   14787 C  CB    . PRO D 2 196 ? 151.790 107.735 124.450 1.00 21.50 ?  175 PRO D CB    1 
ATOM   14788 C  CG    . PRO D 2 196 ? 152.531 106.651 125.057 1.00 22.47 ?  175 PRO D CG    1 
ATOM   14789 C  CD    . PRO D 2 196 ? 153.564 107.203 125.995 1.00 20.91 ?  175 PRO D CD    1 
ATOM   14790 N  N     . LEU D 2 197 ? 151.389 110.370 126.096 1.00 21.70 ?  176 LEU D N     1 
ATOM   14791 C  CA    . LEU D 2 197 ? 150.630 111.567 126.485 1.00 22.40 ?  176 LEU D CA    1 
ATOM   14792 C  C     . LEU D 2 197 ? 151.475 112.842 126.426 1.00 22.58 ?  176 LEU D C     1 
ATOM   14793 O  O     . LEU D 2 197 ? 150.977 113.908 126.042 1.00 22.15 ?  176 LEU D O     1 
ATOM   14794 C  CB    . LEU D 2 197 ? 150.052 111.419 127.887 1.00 22.15 ?  176 LEU D CB    1 
ATOM   14795 C  CG    . LEU D 2 197 ? 148.896 110.440 128.124 1.00 23.08 ?  176 LEU D CG    1 
ATOM   14796 C  CD1   . LEU D 2 197 ? 148.759 110.217 129.621 1.00 21.62 ?  176 LEU D CD1   1 
ATOM   14797 C  CD2   . LEU D 2 197 ? 147.581 110.970 127.515 1.00 21.94 ?  176 LEU D CD2   1 
ATOM   14798 N  N     . TYR D 2 198 ? 152.745 112.712 126.817 1.00 22.76 ?  177 TYR D N     1 
ATOM   14799 C  CA    . TYR D 2 198 ? 153.727 113.795 126.742 1.00 23.23 ?  177 TYR D CA    1 
ATOM   14800 C  C     . TYR D 2 198 ? 153.928 114.258 125.299 1.00 23.91 ?  177 TYR D C     1 
ATOM   14801 O  O     . TYR D 2 198 ? 153.904 115.467 125.021 1.00 24.20 ?  177 TYR D O     1 
ATOM   14802 C  CB    . TYR D 2 198 ? 155.053 113.355 127.385 1.00 23.19 ?  177 TYR D CB    1 
ATOM   14803 C  CG    . TYR D 2 198 ? 156.153 114.398 127.415 1.00 23.52 ?  177 TYR D CG    1 
ATOM   14804 C  CD1   . TYR D 2 198 ? 156.034 115.540 128.194 1.00 24.85 ?  177 TYR D CD1   1 
ATOM   14805 C  CD2   . TYR D 2 198 ? 157.339 114.212 126.693 1.00 25.30 ?  177 TYR D CD2   1 
ATOM   14806 C  CE1   . TYR D 2 198 ? 157.053 116.495 128.241 1.00 26.05 ?  177 TYR D CE1   1 
ATOM   14807 C  CE2   . TYR D 2 198 ? 158.373 115.163 126.737 1.00 26.38 ?  177 TYR D CE2   1 
ATOM   14808 C  CZ    . TYR D 2 198 ? 158.215 116.296 127.513 1.00 26.68 ?  177 TYR D CZ    1 
ATOM   14809 O  OH    . TYR D 2 198 ? 159.213 117.242 127.576 1.00 30.01 ?  177 TYR D OH    1 
ATOM   14810 N  N     . PHE D 2 199 ? 154.113 113.315 124.375 1.00 24.84 ?  178 PHE D N     1 
ATOM   14811 C  CA    . PHE D 2 199 ? 154.182 113.675 122.955 1.00 25.81 ?  178 PHE D CA    1 
ATOM   14812 C  C     . PHE D 2 199 ? 152.875 114.248 122.420 1.00 26.23 ?  178 PHE D C     1 
ATOM   14813 O  O     . PHE D 2 199 ? 152.879 115.260 121.718 1.00 26.58 ?  178 PHE D O     1 
ATOM   14814 C  CB    . PHE D 2 199 ? 154.631 112.495 122.103 1.00 26.08 ?  178 PHE D CB    1 
ATOM   14815 C  CG    . PHE D 2 199 ? 156.099 112.207 122.206 1.00 28.71 ?  178 PHE D CG    1 
ATOM   14816 C  CD1   . PHE D 2 199 ? 157.030 113.236 122.127 1.00 32.03 ?  178 PHE D CD1   1 
ATOM   14817 C  CD2   . PHE D 2 199 ? 156.557 110.913 122.387 1.00 31.77 ?  178 PHE D CD2   1 
ATOM   14818 C  CE1   . PHE D 2 199 ? 158.406 112.980 122.235 1.00 32.29 ?  178 PHE D CE1   1 
ATOM   14819 C  CE2   . PHE D 2 199 ? 157.928 110.649 122.486 1.00 32.72 ?  178 PHE D CE2   1 
ATOM   14820 C  CZ    . PHE D 2 199 ? 158.847 111.690 122.408 1.00 31.91 ?  178 PHE D CZ    1 
ATOM   14821 N  N     . TYR D 2 200 ? 151.773 113.588 122.763 1.00 26.46 ?  179 TYR D N     1 
ATOM   14822 C  CA    . TYR D 2 200 ? 150.418 113.972 122.337 1.00 27.43 ?  179 TYR D CA    1 
ATOM   14823 C  C     . TYR D 2 200 ? 150.101 115.404 122.754 1.00 27.68 ?  179 TYR D C     1 
ATOM   14824 O  O     . TYR D 2 200 ? 149.498 116.158 121.991 1.00 28.71 ?  179 TYR D O     1 
ATOM   14825 C  CB    . TYR D 2 200 ? 149.425 113.010 122.981 1.00 27.27 ?  179 TYR D CB    1 
ATOM   14826 C  CG    . TYR D 2 200 ? 148.034 112.947 122.400 1.00 28.90 ?  179 TYR D CG    1 
ATOM   14827 C  CD1   . TYR D 2 200 ? 147.823 112.832 121.033 1.00 29.00 ?  179 TYR D CD1   1 
ATOM   14828 C  CD2   . TYR D 2 200 ? 146.921 112.931 123.246 1.00 30.14 ?  179 TYR D CD2   1 
ATOM   14829 C  CE1   . TYR D 2 200 ? 146.535 112.743 120.510 1.00 31.26 ?  179 TYR D CE1   1 
ATOM   14830 C  CE2   . TYR D 2 200 ? 145.636 112.831 122.741 1.00 31.86 ?  179 TYR D CE2   1 
ATOM   14831 C  CZ    . TYR D 2 200 ? 145.447 112.743 121.371 1.00 32.51 ?  179 TYR D CZ    1 
ATOM   14832 O  OH    . TYR D 2 200 ? 144.172 112.648 120.869 1.00 33.77 ?  179 TYR D OH    1 
ATOM   14833 N  N     . GLY D 2 201 ? 150.516 115.775 123.964 1.00 27.68 ?  180 GLY D N     1 
ATOM   14834 C  CA    . GLY D 2 201 ? 150.336 117.134 124.466 1.00 28.02 ?  180 GLY D CA    1 
ATOM   14835 C  C     . GLY D 2 201 ? 151.203 118.193 123.791 1.00 28.60 ?  180 GLY D C     1 
ATOM   14836 O  O     . GLY D 2 201 ? 150.949 119.379 123.952 1.00 28.44 ?  180 GLY D O     1 
ATOM   14837 N  N     . GLN D 2 202 ? 152.229 117.755 123.055 1.00 29.34 ?  181 GLN D N     1 
ATOM   14838 C  CA    . GLN D 2 202 ? 153.157 118.634 122.322 1.00 30.39 ?  181 GLN D CA    1 
ATOM   14839 C  C     . GLN D 2 202 ? 152.876 118.699 120.820 1.00 30.55 ?  181 GLN D C     1 
ATOM   14840 O  O     . GLN D 2 202 ? 153.575 119.413 120.093 1.00 31.23 ?  181 GLN D O     1 
ATOM   14841 C  CB    . GLN D 2 202 ? 154.588 118.103 122.425 1.00 30.31 ?  181 GLN D CB    1 
ATOM   14842 C  CG    . GLN D 2 202 ? 155.255 118.146 123.747 1.00 32.40 ?  181 GLN D CG    1 
ATOM   14843 C  CD    . GLN D 2 202 ? 156.653 117.571 123.648 1.00 33.85 ?  181 GLN D CD    1 
ATOM   14844 O  OE1   . GLN D 2 202 ? 156.914 116.455 124.090 1.00 33.94 ?  181 GLN D OE1   1 
ATOM   14845 N  NE2   . GLN D 2 202 ? 157.549 118.315 123.022 1.00 34.92 ?  181 GLN D NE2   1 
ATOM   14846 N  N     . GLY D 2 203 ? 151.920 117.912 120.341 1.00 30.57 ?  182 GLY D N     1 
ATOM   14847 C  CA    . GLY D 2 203 ? 151.629 117.856 118.907 1.00 30.83 ?  182 GLY D CA    1 
ATOM   14848 C  C     . GLY D 2 203 ? 152.445 116.823 118.144 1.00 30.80 ?  182 GLY D C     1 
ATOM   14849 O  O     . GLY D 2 203 ? 152.441 116.813 116.910 1.00 30.86 ?  182 GLY D O     1 
ATOM   14850 N  N     . LYS D 2 204 ? 153.137 115.949 118.876 1.00 30.14 ?  183 LYS D N     1 
ATOM   14851 C  CA    . LYS D 2 204 ? 153.935 114.882 118.265 1.00 30.35 ?  183 LYS D CA    1 
ATOM   14852 C  C     . LYS D 2 204 ? 153.247 113.524 118.375 1.00 29.52 ?  183 LYS D C     1 
ATOM   14853 O  O     . LYS D 2 204 ? 152.559 113.256 119.357 1.00 28.60 ?  183 LYS D O     1 
ATOM   14854 C  CB    . LYS D 2 204 ? 155.323 114.823 118.901 1.00 30.76 ?  183 LYS D CB    1 
ATOM   14855 C  CG    . LYS D 2 204 ? 156.175 116.067 118.629 1.00 32.95 ?  183 LYS D CG    1 
ATOM   14856 C  CD    . LYS D 2 204 ? 157.397 116.060 119.514 1.00 36.37 ?  183 LYS D CD    1 
ATOM   14857 C  CE    . LYS D 2 204 ? 158.279 117.274 119.283 1.00 38.47 ?  183 LYS D CE    1 
ATOM   14858 N  NZ    . LYS D 2 204 ? 159.313 117.313 120.361 1.00 40.21 1  183 LYS D NZ    1 
ATOM   14859 N  N     . LEU D 2 205 ? 153.449 112.672 117.366 1.00 29.47 ?  184 LEU D N     1 
ATOM   14860 C  CA    . LEU D 2 205 ? 152.849 111.329 117.317 1.00 29.06 ?  184 LEU D CA    1 
ATOM   14861 C  C     . LEU D 2 205 ? 151.369 111.347 117.750 1.00 28.96 ?  184 LEU D C     1 
ATOM   14862 O  O     . LEU D 2 205 ? 150.948 110.621 118.659 1.00 27.68 ?  184 LEU D O     1 
ATOM   14863 C  CB    . LEU D 2 205 ? 153.667 110.328 118.148 1.00 28.63 ?  184 LEU D CB    1 
ATOM   14864 C  CG    . LEU D 2 205 ? 155.157 110.160 117.813 1.00 29.00 ?  184 LEU D CG    1 
ATOM   14865 C  CD1   . LEU D 2 205 ? 155.815 109.186 118.794 1.00 28.90 ?  184 LEU D CD1   1 
ATOM   14866 C  CD2   . LEU D 2 205 ? 155.357 109.680 116.381 1.00 28.67 ?  184 LEU D CD2   1 
ATOM   14867 N  N     . MET D 2 206 ? 150.603 112.194 117.068 1.00 29.02 ?  185 MET D N     1 
ATOM   14868 C  CA    . MET D 2 206 ? 149.201 112.444 117.366 1.00 29.72 ?  185 MET D CA    1 
ATOM   14869 C  C     . MET D 2 206 ? 148.252 111.283 117.086 1.00 29.54 ?  185 MET D C     1 
ATOM   14870 O  O     . MET D 2 206 ? 147.257 111.128 117.790 1.00 29.47 ?  185 MET D O     1 
ATOM   14871 C  CB    . MET D 2 206 ? 148.727 113.691 116.610 1.00 30.69 ?  185 MET D CB    1 
ATOM   14872 C  CG    . MET D 2 206 ? 149.527 114.936 116.960 1.00 32.03 ?  185 MET D CG    1 
ATOM   14873 S  SD    . MET D 2 206 ? 149.447 115.296 118.723 1.00 36.63 ?  185 MET D SD    1 
ATOM   14874 C  CE    . MET D 2 206 ? 147.921 116.217 118.799 1.00 33.80 ?  185 MET D CE    1 
ATOM   14875 N  N     . GLN D 2 207 ? 148.541 110.492 116.054 1.00 29.56 ?  186 GLN D N     1 
ATOM   14876 C  CA    . GLN D 2 207 ? 147.682 109.364 115.680 1.00 29.17 ?  186 GLN D CA    1 
ATOM   14877 C  C     . GLN D 2 207 ? 147.809 108.233 116.695 1.00 28.26 ?  186 GLN D C     1 
ATOM   14878 O  O     . GLN D 2 207 ? 146.804 107.703 117.161 1.00 27.98 ?  186 GLN D O     1 
ATOM   14879 C  CB    . GLN D 2 207 ? 148.001 108.857 114.265 1.00 29.80 ?  186 GLN D CB    1 
ATOM   14880 C  CG    . GLN D 2 207 ? 147.958 109.930 113.178 1.00 31.75 ?  186 GLN D CG    1 
ATOM   14881 C  CD    . GLN D 2 207 ? 146.663 110.718 113.203 1.00 34.93 ?  186 GLN D CD    1 
ATOM   14882 O  OE1   . GLN D 2 207 ? 145.594 110.206 112.844 1.00 36.91 ?  186 GLN D OE1   1 
ATOM   14883 N  NE2   . GLN D 2 207 ? 146.748 111.970 113.639 1.00 36.09 ?  186 GLN D NE2   1 
ATOM   14884 N  N     . SER D 2 208 ? 149.043 107.866 117.038 0.50 27.75 ?  187 SER D N     1 
ATOM   14885 C  CA    . SER D 2 208 ? 149.269 106.832 118.041 0.50 27.12 ?  187 SER D CA    1 
ATOM   14886 C  C     . SER D 2 208 ? 148.876 107.329 119.429 0.50 26.72 ?  187 SER D C     1 
ATOM   14887 O  O     . SER D 2 208 ? 148.424 106.542 120.259 0.50 26.30 ?  187 SER D O     1 
ATOM   14888 C  CB    . SER D 2 208 ? 150.722 106.353 118.028 0.50 26.88 ?  187 SER D CB    1 
ATOM   14889 O  OG    . SER D 2 208 ? 151.608 107.447 118.118 0.50 26.59 ?  187 SER D OG    1 
ATOM   14890 N  N     . GLY D 2 209 ? 149.047 108.630 119.669 1.00 26.64 ?  188 GLY D N     1 
ATOM   14891 C  CA    . GLY D 2 209 ? 148.616 109.261 120.933 1.00 26.43 ?  188 GLY D CA    1 
ATOM   14892 C  C     . GLY D 2 209 ? 147.104 109.237 121.112 1.00 26.66 ?  188 GLY D C     1 
ATOM   14893 O  O     . GLY D 2 209 ? 146.601 109.076 122.224 1.00 26.57 ?  188 GLY D O     1 
ATOM   14894 N  N     . GLU D 2 210 ? 146.371 109.403 120.014 1.00 27.42 ?  189 GLU D N     1 
ATOM   14895 C  CA    . GLU D 2 210 ? 144.915 109.286 120.043 1.00 27.73 ?  189 GLU D CA    1 
ATOM   14896 C  C     . GLU D 2 210 ? 144.514 107.848 120.403 1.00 27.04 ?  189 GLU D C     1 
ATOM   14897 O  O     . GLU D 2 210 ? 143.654 107.630 121.257 1.00 26.57 ?  189 GLU D O     1 
ATOM   14898 C  CB    . GLU D 2 210 ? 144.293 109.724 118.705 1.00 28.28 ?  189 GLU D CB    1 
ATOM   14899 C  CG    . GLU D 2 210 ? 142.757 109.716 118.712 1.00 30.71 ?  189 GLU D CG    1 
ATOM   14900 C  CD    . GLU D 2 210 ? 142.118 110.391 117.499 1.00 35.43 ?  189 GLU D CD    1 
ATOM   14901 O  OE1   . GLU D 2 210 ? 142.836 110.750 116.532 1.00 36.89 ?  189 GLU D OE1   1 
ATOM   14902 O  OE2   . GLU D 2 210 ? 140.879 110.570 117.524 1.00 37.04 -1 189 GLU D OE2   1 
ATOM   14903 N  N     . ILE D 2 211 ? 145.151 106.876 119.757 1.00 26.80 ?  190 ILE D N     1 
ATOM   14904 C  CA    . ILE D 2 211 ? 144.936 105.470 120.087 1.00 26.92 ?  190 ILE D CA    1 
ATOM   14905 C  C     . ILE D 2 211 ? 145.219 105.202 121.559 1.00 26.45 ?  190 ILE D C     1 
ATOM   14906 O  O     . ILE D 2 211 ? 144.406 104.572 122.233 1.00 26.65 ?  190 ILE D O     1 
ATOM   14907 C  CB    . ILE D 2 211 ? 145.759 104.523 119.176 1.00 27.00 ?  190 ILE D CB    1 
ATOM   14908 C  CG1   . ILE D 2 211 ? 145.184 104.550 117.755 1.00 28.77 ?  190 ILE D CG1   1 
ATOM   14909 C  CG2   . ILE D 2 211 ? 145.747 103.088 119.728 1.00 26.82 ?  190 ILE D CG2   1 
ATOM   14910 C  CD1   . ILE D 2 211 ? 145.993 103.781 116.719 1.00 30.88 ?  190 ILE D CD1   1 
ATOM   14911 N  N     . ILE D 2 212 ? 146.349 105.700 122.068 1.00 26.49 ?  191 ILE D N     1 
ATOM   14912 C  CA    . ILE D 2 212 ? 146.722 105.452 123.461 1.00 25.73 ?  191 ILE D CA    1 
ATOM   14913 C  C     . ILE D 2 212 ? 145.695 106.062 124.417 1.00 25.48 ?  191 ILE D C     1 
ATOM   14914 O  O     . ILE D 2 212 ? 145.343 105.456 125.433 1.00 24.95 ?  191 ILE D O     1 
ATOM   14915 C  CB    . ILE D 2 212 ? 148.162 105.949 123.789 1.00 26.44 ?  191 ILE D CB    1 
ATOM   14916 C  CG1   . ILE D 2 212 ? 149.208 105.147 123.004 1.00 26.71 ?  191 ILE D CG1   1 
ATOM   14917 C  CG2   . ILE D 2 212 ? 148.443 105.885 125.307 1.00 26.01 ?  191 ILE D CG2   1 
ATOM   14918 C  CD1   . ILE D 2 212 ? 149.267 103.660 123.305 1.00 30.50 ?  191 ILE D CD1   1 
ATOM   14919 N  N     . ASN D 2 213 ? 145.201 107.246 124.070 1.00 24.79 ?  192 ASN D N     1 
ATOM   14920 C  CA    . ASN D 2 213 ? 144.187 107.912 124.876 1.00 24.80 ?  192 ASN D CA    1 
ATOM   14921 C  C     . ASN D 2 213 ? 142.873 107.107 124.958 1.00 24.44 ?  192 ASN D C     1 
ATOM   14922 O  O     . ASN D 2 213 ? 142.197 107.109 125.993 1.00 23.25 ?  192 ASN D O     1 
ATOM   14923 C  CB    . ASN D 2 213 ? 143.940 109.327 124.349 1.00 25.68 ?  192 ASN D CB    1 
ATOM   14924 C  CG    . ASN D 2 213 ? 143.694 110.330 125.460 1.00 27.89 ?  192 ASN D CG    1 
ATOM   14925 O  OD1   . ASN D 2 213 ? 144.208 110.194 126.567 1.00 31.05 ?  192 ASN D OD1   1 
ATOM   14926 N  ND2   . ASN D 2 213 ? 142.906 111.353 125.161 1.00 31.70 ?  192 ASN D ND2   1 
ATOM   14927 N  N     . LEU D 2 214 ? 142.528 106.413 123.873 1.00 23.60 ?  193 LEU D N     1 
ATOM   14928 C  CA    . LEU D 2 214 ? 141.324 105.580 123.855 1.00 23.84 ?  193 LEU D CA    1 
ATOM   14929 C  C     . LEU D 2 214 ? 141.531 104.343 124.709 1.00 23.48 ?  193 LEU D C     1 
ATOM   14930 O  O     . LEU D 2 214 ? 140.633 103.941 125.454 1.00 24.12 ?  193 LEU D O     1 
ATOM   14931 C  CB    . LEU D 2 214 ? 140.962 105.182 122.424 1.00 23.71 ?  193 LEU D CB    1 
ATOM   14932 C  CG    . LEU D 2 214 ? 140.367 106.300 121.558 1.00 25.29 ?  193 LEU D CG    1 
ATOM   14933 C  CD1   . LEU D 2 214 ? 140.187 105.822 120.116 1.00 25.41 ?  193 LEU D CD1   1 
ATOM   14934 C  CD2   . LEU D 2 214 ? 139.045 106.800 122.117 1.00 25.80 ?  193 LEU D CD2   1 
ATOM   14935 N  N     . ILE D 2 215 ? 142.722 103.753 124.603 1.00 22.89 ?  194 ILE D N     1 
ATOM   14936 C  CA    . ILE D 2 215 ? 143.094 102.601 125.412 1.00 22.25 ?  194 ILE D CA    1 
ATOM   14937 C  C     . ILE D 2 215 ? 143.042 102.989 126.886 1.00 22.55 ?  194 ILE D C     1 
ATOM   14938 O  O     . ILE D 2 215 ? 142.412 102.303 127.703 1.00 22.53 ?  194 ILE D O     1 
ATOM   14939 C  CB    . ILE D 2 215 ? 144.503 102.084 125.059 1.00 22.37 ?  194 ILE D CB    1 
ATOM   14940 C  CG1   . ILE D 2 215 ? 144.518 101.505 123.638 1.00 21.89 ?  194 ILE D CG1   1 
ATOM   14941 C  CG2   . ILE D 2 215 ? 144.978 101.053 126.103 1.00 20.25 ?  194 ILE D CG2   1 
ATOM   14942 C  CD1   . ILE D 2 215 ? 145.883 100.973 123.184 1.00 20.48 ?  194 ILE D CD1   1 
ATOM   14943 N  N     . LEU D 2 216 ? 143.693 104.101 127.218 1.00 22.35 ?  195 LEU D N     1 
ATOM   14944 C  CA    . LEU D 2 216 ? 143.771 104.564 128.600 1.00 22.51 ?  195 LEU D CA    1 
ATOM   14945 C  C     . LEU D 2 216 ? 142.367 104.793 129.168 1.00 22.30 ?  195 LEU D C     1 
ATOM   14946 O  O     . LEU D 2 216 ? 142.099 104.435 130.322 1.00 21.62 ?  195 LEU D O     1 
ATOM   14947 C  CB    . LEU D 2 216 ? 144.608 105.851 128.666 1.00 23.06 ?  195 LEU D CB    1 
ATOM   14948 C  CG    . LEU D 2 216 ? 144.798 106.680 129.945 1.00 23.98 ?  195 LEU D CG    1 
ATOM   14949 C  CD1   . LEU D 2 216 ? 145.960 107.613 129.731 1.00 24.44 ?  195 LEU D CD1   1 
ATOM   14950 C  CD2   . LEU D 2 216 ? 143.543 107.491 130.308 1.00 25.00 ?  195 LEU D CD2   1 
ATOM   14951 N  N     . ARG D 2 217 ? 141.487 105.392 128.358 1.00 21.64 ?  196 ARG D N     1 
ATOM   14952 C  CA    . ARG D 2 217 ? 140.096 105.627 128.762 1.00 22.49 ?  196 ARG D CA    1 
ATOM   14953 C  C     . ARG D 2 217 ? 139.362 104.302 129.083 1.00 21.56 ?  196 ARG D C     1 
ATOM   14954 O  O     . ARG D 2 217 ? 138.593 104.245 130.034 1.00 21.32 ?  196 ARG D O     1 
ATOM   14955 C  CB    . ARG D 2 217 ? 139.326 106.465 127.721 1.00 23.07 ?  196 ARG D CB    1 
ATOM   14956 C  CG    . ARG D 2 217 ? 137.913 106.891 128.176 1.00 25.64 ?  196 ARG D CG    1 
ATOM   14957 C  CD    . ARG D 2 217 ? 137.083 107.532 127.049 1.00 32.11 ?  196 ARG D CD    1 
ATOM   14958 N  NE    . ARG D 2 217 ? 136.910 106.631 125.901 1.00 35.06 ?  196 ARG D NE    1 
ATOM   14959 C  CZ    . ARG D 2 217 ? 136.069 106.840 124.893 1.00 37.65 ?  196 ARG D CZ    1 
ATOM   14960 N  NH1   . ARG D 2 217 ? 135.285 107.913 124.882 1.00 40.20 1  196 ARG D NH1   1 
ATOM   14961 N  NH2   . ARG D 2 217 ? 135.998 105.964 123.894 1.00 38.20 ?  196 ARG D NH2   1 
ATOM   14962 N  N     . ASP D 2 218 ? 139.606 103.250 128.299 1.00 21.34 ?  197 ASP D N     1 
ATOM   14963 C  CA    . ASP D 2 218 ? 139.099 101.909 128.629 1.00 21.09 ?  197 ASP D CA    1 
ATOM   14964 C  C     . ASP D 2 218 ? 139.697 101.375 129.947 1.00 20.65 ?  197 ASP D C     1 
ATOM   14965 O  O     . ASP D 2 218 ? 138.961 100.871 130.798 1.00 20.16 ?  197 ASP D O     1 
ATOM   14966 C  CB    . ASP D 2 218 ? 139.374 100.909 127.496 1.00 21.58 ?  197 ASP D CB    1 
ATOM   14967 C  CG    . ASP D 2 218 ? 138.588 101.214 126.221 1.00 22.60 ?  197 ASP D CG    1 
ATOM   14968 O  OD1   . ASP D 2 218 ? 137.530 101.882 126.286 1.00 24.72 ?  197 ASP D OD1   1 
ATOM   14969 O  OD2   . ASP D 2 218 ? 139.049 100.783 125.139 1.00 22.64 -1 197 ASP D OD2   1 
ATOM   14970 N  N     . GLU D 2 219 ? 141.016 101.476 130.123 1.00 20.59 ?  198 GLU D N     1 
ATOM   14971 C  CA    . GLU D 2 219 ? 141.644 100.941 131.352 1.00 20.66 ?  198 GLU D CA    1 
ATOM   14972 C  C     . GLU D 2 219 ? 141.131 101.651 132.607 1.00 20.45 ?  198 GLU D C     1 
ATOM   14973 O  O     . GLU D 2 219 ? 140.959 101.021 133.655 1.00 20.59 ?  198 GLU D O     1 
ATOM   14974 C  CB    . GLU D 2 219 ? 143.179 100.990 131.301 1.00 20.55 ?  198 GLU D CB    1 
ATOM   14975 C  CG    . GLU D 2 219 ? 143.839 100.578 129.948 1.00 21.99 ?  198 GLU D CG    1 
ATOM   14976 C  CD    . GLU D 2 219 ? 143.554 99.144  129.486 1.00 24.00 ?  198 GLU D CD    1 
ATOM   14977 O  OE1   . GLU D 2 219 ? 142.533 98.533  129.869 1.00 25.06 ?  198 GLU D OE1   1 
ATOM   14978 O  OE2   . GLU D 2 219 ? 144.353 98.620  128.692 1.00 24.49 -1 198 GLU D OE2   1 
ATOM   14979 N  N     . ALA D 2 220 ? 140.872 102.951 132.492 1.00 20.47 ?  199 ALA D N     1 
ATOM   14980 C  CA    . ALA D 2 220 ? 140.295 103.733 133.606 1.00 21.10 ?  199 ALA D CA    1 
ATOM   14981 C  C     . ALA D 2 220 ? 138.968 103.153 134.086 1.00 21.34 ?  199 ALA D C     1 
ATOM   14982 O  O     . ALA D 2 220 ? 138.819 102.858 135.271 1.00 21.19 ?  199 ALA D O     1 
ATOM   14983 C  CB    . ALA D 2 220 ? 140.146 105.210 133.232 1.00 21.09 ?  199 ALA D CB    1 
ATOM   14984 N  N     . ILE D 2 221 ? 138.020 102.963 133.166 1.00 21.31 ?  200 ILE D N     1 
ATOM   14985 C  CA    . ILE D 2 221 ? 136.750 102.333 133.522 1.00 21.80 ?  200 ILE D CA    1 
ATOM   14986 C  C     . ILE D 2 221 ? 136.897 100.866 133.982 1.00 20.90 ?  200 ILE D C     1 
ATOM   14987 O  O     . ILE D 2 221 ? 136.189 100.437 134.892 1.00 20.54 ?  200 ILE D O     1 
ATOM   14988 C  CB    . ILE D 2 221 ? 135.651 102.516 132.437 1.00 22.75 ?  200 ILE D CB    1 
ATOM   14989 C  CG1   . ILE D 2 221 ? 134.282 102.218 133.037 1.00 24.63 ?  200 ILE D CG1   1 
ATOM   14990 C  CG2   . ILE D 2 221 ? 135.889 101.610 131.230 1.00 23.38 ?  200 ILE D CG2   1 
ATOM   14991 C  CD1   . ILE D 2 221 ? 133.139 102.835 132.287 1.00 26.91 ?  200 ILE D CD1   1 
ATOM   14992 N  N     . HIS D 2 222 ? 137.833 100.115 133.391 1.00 20.31 ?  201 HIS D N     1 
ATOM   14993 C  CA    . HIS D 2 222 ? 138.102 98.753  133.861 1.00 20.25 ?  201 HIS D CA    1 
ATOM   14994 C  C     . HIS D 2 222 ? 138.518 98.772  135.331 1.00 20.51 ?  201 HIS D C     1 
ATOM   14995 O  O     . HIS D 2 222 ? 137.969 98.028  136.152 1.00 20.99 ?  201 HIS D O     1 
ATOM   14996 C  CB    . HIS D 2 222 ? 139.180 98.052  133.028 1.00 19.79 ?  201 HIS D CB    1 
ATOM   14997 C  CG    . HIS D 2 222 ? 138.830 97.865  131.583 1.00 19.25 ?  201 HIS D CG    1 
ATOM   14998 N  ND1   . HIS D 2 222 ? 139.744 97.398  130.663 1.00 18.35 ?  201 HIS D ND1   1 
ATOM   14999 C  CD2   . HIS D 2 222 ? 137.682 98.090  130.895 1.00 17.64 ?  201 HIS D CD2   1 
ATOM   15000 C  CE1   . HIS D 2 222 ? 139.174 97.328  129.472 1.00 18.28 ?  201 HIS D CE1   1 
ATOM   15001 N  NE2   . HIS D 2 222 ? 137.926 97.751  129.584 1.00 20.01 ?  201 HIS D NE2   1 
ATOM   15002 N  N     . GLY D 2 223 ? 139.474 99.644  135.660 1.00 20.33 ?  202 GLY D N     1 
ATOM   15003 C  CA    . GLY D 2 223 ? 139.946 99.810  137.041 1.00 19.94 ?  202 GLY D CA    1 
ATOM   15004 C  C     . GLY D 2 223 ? 138.845 100.197 138.021 1.00 19.80 ?  202 GLY D C     1 
ATOM   15005 O  O     . GLY D 2 223 ? 138.756 99.626  139.107 1.00 19.96 ?  202 GLY D O     1 
ATOM   15006 N  N     . VAL D 2 224 ? 137.987 101.143 137.635 1.00 19.49 ?  203 VAL D N     1 
ATOM   15007 C  CA    . VAL D 2 224 ? 136.865 101.559 138.493 1.00 18.88 ?  203 VAL D CA    1 
ATOM   15008 C  C     . VAL D 2 224 ? 135.880 100.410 138.743 1.00 18.55 ?  203 VAL D C     1 
ATOM   15009 O  O     . VAL D 2 224 ? 135.445 100.179 139.883 1.00 17.65 ?  203 VAL D O     1 
ATOM   15010 C  CB    . VAL D 2 224 ? 136.113 102.817 137.922 1.00 19.22 ?  203 VAL D CB    1 
ATOM   15011 C  CG1   . VAL D 2 224 ? 134.928 103.209 138.828 1.00 18.51 ?  203 VAL D CG1   1 
ATOM   15012 C  CG2   . VAL D 2 224 ? 137.079 104.011 137.770 1.00 19.69 ?  203 VAL D CG2   1 
ATOM   15013 N  N     . TYR D 2 225 ? 135.553 99.676  137.681 1.00 18.17 ?  204 TYR D N     1 
ATOM   15014 C  CA    . TYR D 2 225 ? 134.598 98.569  137.761 1.00 18.76 ?  204 TYR D CA    1 
ATOM   15015 C  C     . TYR D 2 225 ? 135.120 97.422  138.644 1.00 18.93 ?  204 TYR D C     1 
ATOM   15016 O  O     . TYR D 2 225 ? 134.439 96.981  139.580 1.00 18.77 ?  204 TYR D O     1 
ATOM   15017 C  CB    . TYR D 2 225 ? 134.229 98.048  136.358 1.00 18.96 ?  204 TYR D CB    1 
ATOM   15018 C  CG    . TYR D 2 225 ? 133.134 96.988  136.416 1.00 20.06 ?  204 TYR D CG    1 
ATOM   15019 C  CD1   . TYR D 2 225 ? 131.839 97.325  136.831 1.00 21.79 ?  204 TYR D CD1   1 
ATOM   15020 C  CD2   . TYR D 2 225 ? 133.399 95.655  136.091 1.00 19.51 ?  204 TYR D CD2   1 
ATOM   15021 C  CE1   . TYR D 2 225 ? 130.834 96.359  136.917 1.00 20.38 ?  204 TYR D CE1   1 
ATOM   15022 C  CE2   . TYR D 2 225 ? 132.386 94.673  136.169 1.00 19.38 ?  204 TYR D CE2   1 
ATOM   15023 C  CZ    . TYR D 2 225 ? 131.111 95.044  136.587 1.00 20.84 ?  204 TYR D CZ    1 
ATOM   15024 O  OH    . TYR D 2 225 ? 130.102 94.112  136.690 1.00 20.77 ?  204 TYR D OH    1 
ATOM   15025 N  N     . VAL D 2 226 ? 136.329 96.946  138.354 1.00 18.76 ?  205 VAL D N     1 
ATOM   15026 C  CA    . VAL D 2 226 ? 136.924 95.884  139.160 1.00 18.85 ?  205 VAL D CA    1 
ATOM   15027 C  C     . VAL D 2 226 ? 137.070 96.349  140.608 1.00 19.19 ?  205 VAL D C     1 
ATOM   15028 O  O     . VAL D 2 226 ? 136.872 95.558  141.532 1.00 19.87 ?  205 VAL D O     1 
ATOM   15029 C  CB    . VAL D 2 226 ? 138.258 95.400  138.580 1.00 19.28 ?  205 VAL D CB    1 
ATOM   15030 C  CG1   . VAL D 2 226 ? 138.901 94.319  139.490 1.00 18.22 ?  205 VAL D CG1   1 
ATOM   15031 C  CG2   . VAL D 2 226 ? 138.020 94.857  137.161 1.00 18.40 ?  205 VAL D CG2   1 
ATOM   15032 N  N     . GLY D 2 227 ? 137.384 97.633  140.794 1.00 18.53 ?  206 GLY D N     1 
ATOM   15033 C  CA    . GLY D 2 227 ? 137.435 98.241  142.137 1.00 18.74 ?  206 GLY D CA    1 
ATOM   15034 C  C     . GLY D 2 227 ? 136.142 98.114  142.926 1.00 19.17 ?  206 GLY D C     1 
ATOM   15035 O  O     . GLY D 2 227 ? 136.161 97.848  144.136 1.00 18.66 ?  206 GLY D O     1 
ATOM   15036 N  N     . LEU D 2 228 ? 135.015 98.323  142.249 1.00 19.00 ?  207 LEU D N     1 
ATOM   15037 C  CA    . LEU D 2 228 ? 133.709 98.187  142.898 1.00 19.73 ?  207 LEU D CA    1 
ATOM   15038 C  C     . LEU D 2 228 ? 133.432 96.726  143.279 1.00 19.76 ?  207 LEU D C     1 
ATOM   15039 O  O     . LEU D 2 228 ? 132.910 96.458  144.361 1.00 20.07 ?  207 LEU D O     1 
ATOM   15040 C  CB    . LEU D 2 228 ? 132.599 98.764  142.016 1.00 19.36 ?  207 LEU D CB    1 
ATOM   15041 C  CG    . LEU D 2 228 ? 132.612 100.293 141.857 1.00 20.50 ?  207 LEU D CG    1 
ATOM   15042 C  CD1   . LEU D 2 228 ? 131.651 100.725 140.765 1.00 19.87 ?  207 LEU D CD1   1 
ATOM   15043 C  CD2   . LEU D 2 228 ? 132.275 101.010 143.196 1.00 22.38 ?  207 LEU D CD2   1 
ATOM   15044 N  N     . LEU D 2 229 ? 133.820 95.789  142.415 1.00 19.27 ?  208 LEU D N     1 
ATOM   15045 C  CA    . LEU D 2 229 ? 133.706 94.354  142.737 1.00 19.47 ?  208 LEU D CA    1 
ATOM   15046 C  C     . LEU D 2 229 ? 134.570 93.942  143.935 1.00 19.67 ?  208 LEU D C     1 
ATOM   15047 O  O     . LEU D 2 229 ? 134.164 93.093  144.739 1.00 19.82 ?  208 LEU D O     1 
ATOM   15048 C  CB    . LEU D 2 229 ? 134.050 93.478  141.514 1.00 19.51 ?  208 LEU D CB    1 
ATOM   15049 C  CG    . LEU D 2 229 ? 133.208 93.601  140.233 1.00 19.48 ?  208 LEU D CG    1 
ATOM   15050 C  CD1   . LEU D 2 229 ? 133.828 92.756  139.105 1.00 20.14 ?  208 LEU D CD1   1 
ATOM   15051 C  CD2   . LEU D 2 229 ? 131.723 93.234  140.446 1.00 19.95 ?  208 LEU D CD2   1 
ATOM   15052 N  N     . ALA D 2 230 ? 135.760 94.532  144.053 1.00 19.43 ?  209 ALA D N     1 
ATOM   15053 C  CA    . ALA D 2 230 ? 136.633 94.295  145.210 1.00 20.29 ?  209 ALA D CA    1 
ATOM   15054 C  C     . ALA D 2 230 ? 136.044 94.862  146.503 1.00 21.17 ?  209 ALA D C     1 
ATOM   15055 O  O     . ALA D 2 230 ? 136.078 94.205  147.538 1.00 21.73 ?  209 ALA D O     1 
ATOM   15056 C  CB    . ALA D 2 230 ? 138.027 94.866  144.958 1.00 19.99 ?  209 ALA D CB    1 
ATOM   15057 N  N     . GLN D 2 231 ? 135.501 96.078  146.441 1.00 22.26 ?  210 GLN D N     1 
ATOM   15058 C  CA    . GLN D 2 231 ? 134.850 96.701  147.608 1.00 23.33 ?  210 GLN D CA    1 
ATOM   15059 C  C     . GLN D 2 231 ? 133.658 95.879  148.108 1.00 23.85 ?  210 GLN D C     1 
ATOM   15060 O  O     . GLN D 2 231 ? 133.429 95.785  149.311 1.00 24.91 ?  210 GLN D O     1 
ATOM   15061 C  CB    . GLN D 2 231 ? 134.386 98.126  147.292 1.00 23.49 ?  210 GLN D CB    1 
ATOM   15062 C  CG    . GLN D 2 231 ? 135.506 99.136  147.019 1.00 23.05 ?  210 GLN D CG    1 
ATOM   15063 C  CD    . GLN D 2 231 ? 134.954 100.521 146.687 1.00 24.65 ?  210 GLN D CD    1 
ATOM   15064 O  OE1   . GLN D 2 231 ? 134.127 101.055 147.426 1.00 25.85 ?  210 GLN D OE1   1 
ATOM   15065 N  NE2   . GLN D 2 231 ? 135.397 101.099 145.569 1.00 22.30 ?  210 GLN D NE2   1 
ATOM   15066 N  N     . GLU D 2 232 ? 132.894 95.305  147.184 1.00 24.36 ?  211 GLU D N     1 
ATOM   15067 C  CA    . GLU D 2 232 ? 131.807 94.394  147.538 1.00 24.83 ?  211 GLU D CA    1 
ATOM   15068 C  C     . GLU D 2 232 ? 132.295 93.230  148.407 1.00 24.34 ?  211 GLU D C     1 
ATOM   15069 O  O     . GLU D 2 232 ? 131.666 92.907  149.416 1.00 24.20 ?  211 GLU D O     1 
ATOM   15070 C  CB    . GLU D 2 232 ? 131.124 93.858  146.285 1.00 25.15 ?  211 GLU D CB    1 
ATOM   15071 C  CG    . GLU D 2 232 ? 129.836 93.126  146.556 1.00 28.55 ?  211 GLU D CG    1 
ATOM   15072 C  CD    . GLU D 2 232 ? 129.201 92.644  145.280 1.00 33.83 ?  211 GLU D CD    1 
ATOM   15073 O  OE1   . GLU D 2 232 ? 128.369 93.392  144.726 1.00 35.09 ?  211 GLU D OE1   1 
ATOM   15074 O  OE2   . GLU D 2 232 ? 129.565 91.544  144.810 1.00 35.51 -1 211 GLU D OE2   1 
ATOM   15075 N  N     . ILE D 2 233 ? 133.410 92.610  148.023 1.00 23.39 ?  212 ILE D N     1 
ATOM   15076 C  CA    . ILE D 2 233 ? 134.005 91.532  148.832 1.00 23.42 ?  212 ILE D CA    1 
ATOM   15077 C  C     . ILE D 2 233 ? 134.517 92.069  150.169 1.00 23.74 ?  212 ILE D C     1 
ATOM   15078 O  O     . ILE D 2 233 ? 134.216 91.515  151.225 1.00 24.61 ?  212 ILE D O     1 
ATOM   15079 C  CB    . ILE D 2 233 ? 135.127 90.772  148.073 1.00 22.81 ?  212 ILE D CB    1 
ATOM   15080 C  CG1   . ILE D 2 233 ? 134.543 90.014  146.871 1.00 22.94 ?  212 ILE D CG1   1 
ATOM   15081 C  CG2   . ILE D 2 233 ? 135.850 89.788  149.002 1.00 22.45 ?  212 ILE D CG2   1 
ATOM   15082 C  CD1   . ILE D 2 233 ? 135.603 89.524  145.861 1.00 22.21 ?  212 ILE D CD1   1 
ATOM   15083 N  N     . TYR D 2 234 ? 135.274 93.161  150.117 1.00 24.19 ?  213 TYR D N     1 
ATOM   15084 C  CA    . TYR D 2 234 ? 135.829 93.800  151.302 1.00 24.59 ?  213 TYR D CA    1 
ATOM   15085 C  C     . TYR D 2 234 ? 134.748 94.092  152.348 1.00 25.15 ?  213 TYR D C     1 
ATOM   15086 O  O     . TYR D 2 234 ? 134.961 93.858  153.541 1.00 24.94 ?  213 TYR D O     1 
ATOM   15087 C  CB    . TYR D 2 234 ? 136.538 95.097  150.904 1.00 24.41 ?  213 TYR D CB    1 
ATOM   15088 C  CG    . TYR D 2 234 ? 137.151 95.875  152.050 1.00 25.93 ?  213 TYR D CG    1 
ATOM   15089 C  CD1   . TYR D 2 234 ? 138.429 95.576  152.510 1.00 24.70 ?  213 TYR D CD1   1 
ATOM   15090 C  CD2   . TYR D 2 234 ? 136.451 96.921  152.666 1.00 26.11 ?  213 TYR D CD2   1 
ATOM   15091 C  CE1   . TYR D 2 234 ? 139.000 96.292  153.559 1.00 27.90 ?  213 TYR D CE1   1 
ATOM   15092 C  CE2   . TYR D 2 234 ? 137.017 97.643  153.708 1.00 27.70 ?  213 TYR D CE2   1 
ATOM   15093 C  CZ    . TYR D 2 234 ? 138.290 97.326  154.147 1.00 27.89 ?  213 TYR D CZ    1 
ATOM   15094 O  OH    . TYR D 2 234 ? 138.854 98.035  155.181 1.00 32.34 ?  213 TYR D OH    1 
ATOM   15095 N  N     . ASN D 2 235 ? 133.605 94.605  151.891 1.00 25.43 ?  214 ASN D N     1 
ATOM   15096 C  CA    . ASN D 2 235 ? 132.501 94.995  152.784 1.00 26.77 ?  214 ASN D CA    1 
ATOM   15097 C  C     . ASN D 2 235 ? 131.765 93.816  153.420 1.00 27.06 ?  214 ASN D C     1 
ATOM   15098 O  O     . ASN D 2 235 ? 130.982 93.996  154.347 1.00 27.42 ?  214 ASN D O     1 
ATOM   15099 C  CB    . ASN D 2 235 ? 131.484 95.877  152.056 1.00 26.80 ?  214 ASN D CB    1 
ATOM   15100 C  CG    . ASN D 2 235 ? 132.067 97.189  151.603 1.00 28.19 ?  214 ASN D CG    1 
ATOM   15101 O  OD1   . ASN D 2 235 ? 132.928 97.767  152.263 1.00 29.35 ?  214 ASN D OD1   1 
ATOM   15102 N  ND2   . ASN D 2 235 ? 131.589 97.675  150.469 1.00 30.84 ?  214 ASN D ND2   1 
ATOM   15103 N  N     . LYS D 2 236 ? 132.015 92.617  152.914 1.00 26.87 ?  215 LYS D N     1 
ATOM   15104 C  CA    . LYS D 2 236 ? 131.416 91.415  153.480 1.00 27.86 ?  215 LYS D CA    1 
ATOM   15105 C  C     . LYS D 2 236 ? 132.276 90.835  154.611 1.00 28.07 ?  215 LYS D C     1 
ATOM   15106 O  O     . LYS D 2 236 ? 131.899 89.846  155.238 1.00 28.22 ?  215 LYS D O     1 
ATOM   15107 C  CB    . LYS D 2 236 ? 131.187 90.368  152.389 1.00 27.52 ?  215 LYS D CB    1 
ATOM   15108 C  CG    . LYS D 2 236 ? 130.185 90.778  151.337 1.00 29.60 ?  215 LYS D CG    1 
ATOM   15109 C  CD    . LYS D 2 236 ? 129.535 89.573  150.677 1.00 34.24 ?  215 LYS D CD    1 
ATOM   15110 C  CE    . LYS D 2 236 ? 130.146 89.220  149.335 1.00 36.75 ?  215 LYS D CE    1 
ATOM   15111 N  NZ    . LYS D 2 236 ? 131.548 88.769  149.471 1.00 40.41 1  215 LYS D NZ    1 
ATOM   15112 N  N     . GLN D 2 237 ? 133.422 91.458  154.872 1.00 28.33 ?  216 GLN D N     1 
ATOM   15113 C  CA    . GLN D 2 237 ? 134.390 90.919  155.830 1.00 29.60 ?  216 GLN D CA    1 
ATOM   15114 C  C     . GLN D 2 237 ? 134.241 91.524  157.221 1.00 30.69 ?  216 GLN D C     1 
ATOM   15115 O  O     . GLN D 2 237 ? 133.683 92.615  157.378 1.00 30.85 ?  216 GLN D O     1 
ATOM   15116 C  CB    . GLN D 2 237 ? 135.837 91.128  155.334 1.00 29.08 ?  216 GLN D CB    1 
ATOM   15117 C  CG    . GLN D 2 237 ? 136.133 90.620  153.919 1.00 27.78 ?  216 GLN D CG    1 
ATOM   15118 C  CD    . GLN D 2 237 ? 135.669 89.191  153.681 1.00 28.38 ?  216 GLN D CD    1 
ATOM   15119 O  OE1   . GLN D 2 237 ? 135.976 88.289  154.457 1.00 29.30 ?  216 GLN D OE1   1 
ATOM   15120 N  NE2   . GLN D 2 237 ? 134.934 88.981  152.593 1.00 26.88 ?  216 GLN D NE2   1 
ATOM   15121 N  N     . THR D 2 238 ? 134.757 90.811  158.222 1.00 32.02 ?  217 THR D N     1 
ATOM   15122 C  CA    . THR D 2 238 ? 134.845 91.330  159.591 1.00 33.47 ?  217 THR D CA    1 
ATOM   15123 C  C     . THR D 2 238 ? 135.815 92.514  159.670 1.00 34.29 ?  217 THR D C     1 
ATOM   15124 O  O     . THR D 2 238 ? 136.559 92.798  158.717 1.00 33.78 ?  217 THR D O     1 
ATOM   15125 C  CB    . THR D 2 238 ? 135.309 90.230  160.586 1.00 34.00 ?  217 THR D CB    1 
ATOM   15126 O  OG1   . THR D 2 238 ? 136.656 89.839  160.282 1.00 34.33 ?  217 THR D OG1   1 
ATOM   15127 C  CG2   . THR D 2 238 ? 134.390 88.999  160.515 1.00 33.53 ?  217 THR D CG2   1 
ATOM   15128 N  N     . GLU D 2 239 ? 135.823 93.198  160.810 1.00 35.45 ?  218 GLU D N     1 
ATOM   15129 C  CA    . GLU D 2 239 ? 136.724 94.331  160.997 1.00 36.37 ?  218 GLU D CA    1 
ATOM   15130 C  C     . GLU D 2 239 ? 138.194 93.915  161.016 1.00 36.29 ?  218 GLU D C     1 
ATOM   15131 O  O     . GLU D 2 239 ? 139.041 94.609  160.446 1.00 36.18 ?  218 GLU D O     1 
ATOM   15132 C  CB    . GLU D 2 239 ? 136.354 95.137  162.245 1.00 37.27 ?  218 GLU D CB    1 
ATOM   15133 C  CG    . GLU D 2 239 ? 135.028 95.908  162.105 1.00 39.45 ?  218 GLU D CG    1 
ATOM   15134 C  CD    . GLU D 2 239 ? 135.002 96.852  160.905 1.00 41.22 ?  218 GLU D CD    1 
ATOM   15135 O  OE1   . GLU D 2 239 ? 135.981 97.600  160.696 1.00 42.62 ?  218 GLU D OE1   1 
ATOM   15136 O  OE2   . GLU D 2 239 ? 133.994 96.846  160.164 1.00 41.24 -1 218 GLU D OE2   1 
ATOM   15137 N  N     . GLU D 2 240 ? 138.490 92.781  161.648 1.00 36.66 ?  219 GLU D N     1 
ATOM   15138 C  CA    . GLU D 2 240 ? 139.860 92.266  161.686 1.00 37.01 ?  219 GLU D CA    1 
ATOM   15139 C  C     . GLU D 2 240 ? 140.326 91.842  160.293 1.00 35.85 ?  219 GLU D C     1 
ATOM   15140 O  O     . GLU D 2 240 ? 141.466 92.116  159.911 1.00 35.62 ?  219 GLU D O     1 
ATOM   15141 C  CB    . GLU D 2 240 ? 140.001 91.099  162.675 1.00 37.98 ?  219 GLU D CB    1 
ATOM   15142 C  CG    . GLU D 2 240 ? 141.448 90.602  162.819 1.00 40.87 ?  219 GLU D CG    1 
ATOM   15143 C  CD    . GLU D 2 240 ? 141.620 89.432  163.786 1.00 44.58 ?  219 GLU D CD    1 
ATOM   15144 O  OE1   . GLU D 2 240 ? 142.739 89.292  164.337 1.00 45.86 ?  219 GLU D OE1   1 
ATOM   15145 O  OE2   . GLU D 2 240 ? 140.655 88.656  163.994 1.00 45.75 -1 219 GLU D OE2   1 
ATOM   15146 N  N     . LYS D 2 241 ? 139.439 91.175  159.553 1.00 34.54 ?  220 LYS D N     1 
ATOM   15147 C  CA    . LYS D 2 241 ? 139.735 90.735  158.188 1.00 33.65 ?  220 LYS D CA    1 
ATOM   15148 C  C     . LYS D 2 241 ? 139.918 91.936  157.251 1.00 32.67 ?  220 LYS D C     1 
ATOM   15149 O  O     . LYS D 2 241 ? 140.789 91.907  156.385 1.00 32.05 ?  220 LYS D O     1 
ATOM   15150 C  CB    . LYS D 2 241 ? 138.649 89.787  157.668 1.00 33.30 ?  220 LYS D CB    1 
ATOM   15151 C  CG    . LYS D 2 241 ? 138.935 89.136  156.301 1.00 34.50 ?  220 LYS D CG    1 
ATOM   15152 C  CD    . LYS D 2 241 ? 140.205 88.276  156.299 1.00 36.30 ?  220 LYS D CD    1 
ATOM   15153 C  CE    . LYS D 2 241 ? 140.024 86.995  157.106 1.00 38.44 ?  220 LYS D CE    1 
ATOM   15154 N  NZ    . LYS D 2 241 ? 141.333 86.457  157.563 1.00 39.28 1  220 LYS D NZ    1 
ATOM   15155 N  N     . LYS D 2 242 ? 139.102 92.978  157.435 1.00 31.90 ?  221 LYS D N     1 
ATOM   15156 C  CA    . LYS D 2 242 ? 139.244 94.223  156.680 1.00 31.28 ?  221 LYS D CA    1 
ATOM   15157 C  C     . LYS D 2 242 ? 140.621 94.852  156.891 1.00 31.32 ?  221 LYS D C     1 
ATOM   15158 O  O     . LYS D 2 242 ? 141.292 95.191  155.925 1.00 30.72 ?  221 LYS D O     1 
ATOM   15159 C  CB    . LYS D 2 242 ? 138.150 95.235  157.051 1.00 31.38 ?  221 LYS D CB    1 
ATOM   15160 C  CG    . LYS D 2 242 ? 136.816 95.019  156.343 1.00 30.64 ?  221 LYS D CG    1 
ATOM   15161 C  CD    . LYS D 2 242 ? 135.808 96.083  156.776 1.00 32.51 ?  221 LYS D CD    1 
ATOM   15162 C  CE    . LYS D 2 242 ? 134.487 95.906  156.062 1.00 32.66 ?  221 LYS D CE    1 
ATOM   15163 N  NZ    . LYS D 2 242 ? 133.446 96.777  156.653 1.00 35.31 1  221 LYS D NZ    1 
ATOM   15164 N  N     . ALA D 2 243 ? 141.027 95.007  158.155 1.00 31.62 ?  222 ALA D N     1 
ATOM   15165 C  CA    . ALA D 2 243 ? 142.344 95.557  158.494 1.00 31.66 ?  222 ALA D CA    1 
ATOM   15166 C  C     . ALA D 2 243 ? 143.483 94.757  157.849 1.00 31.52 ?  222 ALA D C     1 
ATOM   15167 O  O     . ALA D 2 243 ? 144.495 95.323  157.426 1.00 31.41 ?  222 ALA D O     1 
ATOM   15168 C  CB    . ALA D 2 243 ? 142.520 95.628  160.015 1.00 31.89 ?  222 ALA D CB    1 
ATOM   15169 N  N     . GLU D 2 244 ? 143.285 93.445  157.762 1.00 31.35 ?  223 GLU D N     1 
ATOM   15170 C  CA    . GLU D 2 244 ? 144.235 92.521  157.165 1.00 31.54 ?  223 GLU D CA    1 
ATOM   15171 C  C     . GLU D 2 244 ? 144.304 92.684  155.629 1.00 30.63 ?  223 GLU D C     1 
ATOM   15172 O  O     . GLU D 2 244 ? 145.386 92.633  155.028 1.00 29.47 ?  223 GLU D O     1 
ATOM   15173 C  CB    . GLU D 2 244 ? 143.807 91.113  157.547 1.00 32.45 ?  223 GLU D CB    1 
ATOM   15174 C  CG    . GLU D 2 244 ? 144.796 90.014  157.305 1.00 35.31 ?  223 GLU D CG    1 
ATOM   15175 C  CD    . GLU D 2 244 ? 144.378 88.743  158.016 1.00 38.36 ?  223 GLU D CD    1 
ATOM   15176 O  OE1   . GLU D 2 244 ? 144.410 88.719  159.264 1.00 41.93 ?  223 GLU D OE1   1 
ATOM   15177 O  OE2   . GLU D 2 244 ? 144.006 87.768  157.334 1.00 39.37 -1 223 GLU D OE2   1 
ATOM   15178 N  N     . LEU D 2 245 ? 143.143 92.885  155.012 1.00 29.62 ?  224 LEU D N     1 
ATOM   15179 C  CA    . LEU D 2 245 ? 143.062 93.163  153.581 1.00 29.44 ?  224 LEU D CA    1 
ATOM   15180 C  C     . LEU D 2 245 ? 143.630 94.537  153.220 1.00 28.99 ?  224 LEU D C     1 
ATOM   15181 O  O     . LEU D 2 245 ? 144.230 94.690  152.160 1.00 28.63 ?  224 LEU D O     1 
ATOM   15182 C  CB    . LEU D 2 245 ? 141.619 93.023  153.084 1.00 29.06 ?  224 LEU D CB    1 
ATOM   15183 C  CG    . LEU D 2 245 ? 141.027 91.610  153.093 1.00 29.27 ?  224 LEU D CG    1 
ATOM   15184 C  CD1   . LEU D 2 245 ? 139.613 91.649  152.521 1.00 30.76 ?  224 LEU D CD1   1 
ATOM   15185 C  CD2   . LEU D 2 245 ? 141.884 90.625  152.304 1.00 28.11 ?  224 LEU D CD2   1 
ATOM   15186 N  N     . ARG D 2 246 ? 143.440 95.524  154.097 1.00 29.31 ?  225 ARG D N     1 
ATOM   15187 C  CA    . ARG D 2 246 ? 144.049 96.846  153.916 1.00 29.86 ?  225 ARG D CA    1 
ATOM   15188 C  C     . ARG D 2 246 ? 145.569 96.758  153.958 1.00 29.23 ?  225 ARG D C     1 
ATOM   15189 O  O     . ARG D 2 246 ? 146.247 97.360  153.138 1.00 28.95 ?  225 ARG D O     1 
ATOM   15190 C  CB    . ARG D 2 246 ? 143.589 97.846  154.983 1.00 30.56 ?  225 ARG D CB    1 
ATOM   15191 C  CG    . ARG D 2 246 ? 142.196 98.395  154.776 1.00 33.71 ?  225 ARG D CG    1 
ATOM   15192 C  CD    . ARG D 2 246 ? 141.983 99.739  155.499 1.00 37.42 ?  225 ARG D CD    1 
ATOM   15193 N  NE    . ARG D 2 246 ? 142.268 99.682  156.938 1.00 39.17 ?  225 ARG D NE    1 
ATOM   15194 C  CZ    . ARG D 2 246 ? 141.455 99.177  157.866 1.00 40.68 ?  225 ARG D CZ    1 
ATOM   15195 N  NH1   . ARG D 2 246 ? 140.278 98.652  157.537 1.00 40.28 1  225 ARG D NH1   1 
ATOM   15196 N  NH2   . ARG D 2 246 ? 141.830 99.188  159.142 1.00 41.65 ?  225 ARG D NH2   1 
ATOM   15197 N  N     . GLU D 2 247 ? 146.090 96.019  154.930 1.00 28.89 ?  226 GLU D N     1 
ATOM   15198 C  CA    . GLU D 2 247 ? 147.531 95.809  155.040 1.00 29.27 ?  226 GLU D CA    1 
ATOM   15199 C  C     . GLU D 2 247 ? 148.074 95.120  153.789 1.00 27.84 ?  226 GLU D C     1 
ATOM   15200 O  O     . GLU D 2 247 ? 149.124 95.521  153.280 1.00 27.37 ?  226 GLU D O     1 
ATOM   15201 C  CB    . GLU D 2 247 ? 147.887 95.019  156.311 1.00 30.21 ?  226 GLU D CB    1 
ATOM   15202 C  CG    . GLU D 2 247 ? 149.377 94.648  156.448 1.00 34.46 ?  226 GLU D CG    1 
ATOM   15203 C  CD    . GLU D 2 247 ? 150.298 95.865  156.462 1.00 40.77 ?  226 GLU D CD    1 
ATOM   15204 O  OE1   . GLU D 2 247 ? 150.183 96.688  157.401 1.00 44.03 ?  226 GLU D OE1   1 
ATOM   15205 O  OE2   . GLU D 2 247 ? 151.138 96.005  155.537 1.00 42.98 -1 226 GLU D OE2   1 
ATOM   15206 N  N     . PHE D 2 248 ? 147.358 94.107  153.295 1.00 26.73 ?  227 PHE D N     1 
ATOM   15207 C  CA    . PHE D 2 248 ? 147.718 93.442  152.036 1.00 26.15 ?  227 PHE D CA    1 
ATOM   15208 C  C     . PHE D 2 248 ? 147.829 94.443  150.882 1.00 25.33 ?  227 PHE D C     1 
ATOM   15209 O  O     . PHE D 2 248 ? 148.818 94.436  150.154 1.00 24.70 ?  227 PHE D O     1 
ATOM   15210 C  CB    . PHE D 2 248 ? 146.733 92.327  151.636 1.00 26.02 ?  227 PHE D CB    1 
ATOM   15211 C  CG    . PHE D 2 248 ? 146.867 91.894  150.176 1.00 25.61 ?  227 PHE D CG    1 
ATOM   15212 C  CD1   . PHE D 2 248 ? 147.797 90.929  149.804 1.00 26.51 ?  227 PHE D CD1   1 
ATOM   15213 C  CD2   . PHE D 2 248 ? 146.086 92.488  149.180 1.00 26.21 ?  227 PHE D CD2   1 
ATOM   15214 C  CE1   . PHE D 2 248 ? 147.946 90.545  148.471 1.00 26.16 ?  227 PHE D CE1   1 
ATOM   15215 C  CE2   . PHE D 2 248 ? 146.227 92.115  147.836 1.00 26.07 ?  227 PHE D CE2   1 
ATOM   15216 C  CZ    . PHE D 2 248 ? 147.165 91.139  147.484 1.00 25.82 ?  227 PHE D CZ    1 
ATOM   15217 N  N     . ALA D 2 249 ? 146.801 95.277  150.720 1.00 24.83 ?  228 ALA D N     1 
ATOM   15218 C  CA    . ALA D 2 249 ? 146.724 96.239  149.612 1.00 24.08 ?  228 ALA D CA    1 
ATOM   15219 C  C     . ALA D 2 249 ? 147.856 97.275  149.671 1.00 23.93 ?  228 ALA D C     1 
ATOM   15220 O  O     . ALA D 2 249 ? 148.471 97.591  148.650 1.00 22.51 ?  228 ALA D O     1 
ATOM   15221 C  CB    . ALA D 2 249 ? 145.362 96.942  149.621 1.00 24.18 ?  228 ALA D CB    1 
ATOM   15222 N  N     . ILE D 2 250 ? 148.118 97.800  150.868 1.00 24.20 ?  229 ILE D N     1 
ATOM   15223 C  CA    . ILE D 2 250 ? 149.170 98.800  151.057 1.00 24.86 ?  229 ILE D CA    1 
ATOM   15224 C  C     . ILE D 2 250 ? 150.557 98.180  150.855 1.00 24.68 ?  229 ILE D C     1 
ATOM   15225 O  O     . ILE D 2 250 ? 151.418 98.781  150.223 1.00 24.30 ?  229 ILE D O     1 
ATOM   15226 C  CB    . ILE D 2 250 ? 149.057 99.522  152.446 1.00 25.44 ?  229 ILE D CB    1 
ATOM   15227 C  CG1   . ILE D 2 250 ? 147.697 100.227 152.614 1.00 26.49 ?  229 ILE D CG1   1 
ATOM   15228 C  CG2   . ILE D 2 250 ? 150.209 100.512 152.665 1.00 27.13 ?  229 ILE D CG2   1 
ATOM   15229 C  CD1   . ILE D 2 250 ? 147.310 101.198 151.496 1.00 28.58 ?  229 ILE D CD1   1 
ATOM   15230 N  N     . ASP D 2 251 ? 150.764 96.976  151.391 1.00 24.90 ?  230 ASP D N     1 
ATOM   15231 C  CA    . ASP D 2 251 ? 152.020 96.255  151.223 1.00 25.04 ?  230 ASP D CA    1 
ATOM   15232 C  C     . ASP D 2 251 ? 152.299 95.976  149.734 1.00 24.25 ?  230 ASP D C     1 
ATOM   15233 O  O     . ASP D 2 251 ? 153.408 96.210  149.250 1.00 23.60 ?  230 ASP D O     1 
ATOM   15234 C  CB    . ASP D 2 251 ? 151.982 94.951  152.027 1.00 26.23 ?  230 ASP D CB    1 
ATOM   15235 C  CG    . ASP D 2 251 ? 153.200 94.081  151.801 1.00 28.91 ?  230 ASP D CG    1 
ATOM   15236 O  OD1   . ASP D 2 251 ? 154.312 94.464  152.221 1.00 32.03 ?  230 ASP D OD1   1 
ATOM   15237 O  OD2   . ASP D 2 251 ? 153.036 92.990  151.220 1.00 33.16 -1 230 ASP D OD2   1 
ATOM   15238 N  N     . LEU D 2 252 ? 151.291 95.472  149.026 1.00 23.43 ?  231 LEU D N     1 
ATOM   15239 C  CA    . LEU D 2 252 ? 151.404 95.246  147.588 1.00 22.79 ?  231 LEU D CA    1 
ATOM   15240 C  C     . LEU D 2 252 ? 151.713 96.549  146.845 1.00 22.71 ?  231 LEU D C     1 
ATOM   15241 O  O     . LEU D 2 252 ? 152.593 96.583  145.976 1.00 21.58 ?  231 LEU D O     1 
ATOM   15242 C  CB    . LEU D 2 252 ? 150.127 94.613  147.026 1.00 22.48 ?  231 LEU D CB    1 
ATOM   15243 C  CG    . LEU D 2 252 ? 150.137 94.325  145.512 1.00 21.05 ?  231 LEU D CG    1 
ATOM   15244 C  CD1   . LEU D 2 252 ? 151.301 93.393  145.111 1.00 22.94 ?  231 LEU D CD1   1 
ATOM   15245 C  CD2   . LEU D 2 252 ? 148.813 93.723  145.063 1.00 19.31 ?  231 LEU D CD2   1 
ATOM   15246 N  N     . LEU D 2 253 ? 150.986 97.613  147.187 1.00 22.90 ?  232 LEU D N     1 
ATOM   15247 C  CA    . LEU D 2 253 ? 151.214 98.918  146.549 1.00 23.78 ?  232 LEU D CA    1 
ATOM   15248 C  C     . LEU D 2 253 ? 152.666 99.375  146.735 1.00 23.75 ?  232 LEU D C     1 
ATOM   15249 O  O     . LEU D 2 253 ? 153.304 99.827  145.783 1.00 23.26 ?  232 LEU D O     1 
ATOM   15250 C  CB    . LEU D 2 253 ? 150.268 99.986  147.104 1.00 24.03 ?  232 LEU D CB    1 
ATOM   15251 C  CG    . LEU D 2 253 ? 150.596 101.423 146.662 1.00 26.46 ?  232 LEU D CG    1 
ATOM   15252 C  CD1   . LEU D 2 253 ? 150.243 101.613 145.205 1.00 26.52 ?  232 LEU D CD1   1 
ATOM   15253 C  CD2   . LEU D 2 253 ? 149.871 102.463 147.521 1.00 27.50 ?  232 LEU D CD2   1 
ATOM   15254 N  N     . ASN D 2 254 ? 153.161 99.273  147.969 1.00 24.63 ?  233 ASN D N     1 
ATOM   15255 C  CA    . ASN D 2 254 ? 154.552 99.608  148.285 1.00 25.49 ?  233 ASN D CA    1 
ATOM   15256 C  C     . ASN D 2 254 ? 155.580 98.837  147.445 1.00 24.94 ?  233 ASN D C     1 
ATOM   15257 O  O     . ASN D 2 254 ? 156.538 99.435  146.949 1.00 24.64 ?  233 ASN D O     1 
ATOM   15258 C  CB    . ASN D 2 254 ? 154.841 99.391  149.768 1.00 26.98 ?  233 ASN D CB    1 
ATOM   15259 C  CG    . ASN D 2 254 ? 154.477 100.591 150.613 1.00 29.94 ?  233 ASN D CG    1 
ATOM   15260 O  OD1   . ASN D 2 254 ? 154.706 101.743 150.221 1.00 34.55 ?  233 ASN D OD1   1 
ATOM   15261 N  ND2   . ASN D 2 254 ? 153.919 100.333 151.788 1.00 33.81 ?  233 ASN D ND2   1 
ATOM   15262 N  N     . GLN D 2 255 ? 155.386 97.525  147.303 1.00 24.08 ?  234 GLN D N     1 
ATOM   15263 C  CA    . GLN D 2 255 ? 156.306 96.702  146.513 1.00 24.35 ?  234 GLN D CA    1 
ATOM   15264 C  C     . GLN D 2 255 ? 156.307 97.163  145.067 1.00 23.26 ?  234 GLN D C     1 
ATOM   15265 O  O     . GLN D 2 255 ? 157.378 97.353  144.481 1.00 23.12 ?  234 GLN D O     1 
ATOM   15266 C  CB    . GLN D 2 255 ? 155.934 95.214  146.551 1.00 24.84 ?  234 GLN D CB    1 
ATOM   15267 C  CG    . GLN D 2 255 ? 156.204 94.497  147.855 1.00 27.45 ?  234 GLN D CG    1 
ATOM   15268 C  CD    . GLN D 2 255 ? 157.650 94.604  148.308 1.00 32.02 ?  234 GLN D CD    1 
ATOM   15269 O  OE1   . GLN D 2 255 ? 157.926 95.150  149.373 1.00 35.80 ?  234 GLN D OE1   1 
ATOM   15270 N  NE2   . GLN D 2 255 ? 158.578 94.081  147.504 1.00 32.12 ?  234 GLN D NE2   1 
ATOM   15271 N  N     . LEU D 2 256 ? 155.110 97.342  144.507 1.00 21.77 ?  235 LEU D N     1 
ATOM   15272 C  CA    . LEU D 2 256 ? 154.965 97.770  143.113 1.00 21.68 ?  235 LEU D CA    1 
ATOM   15273 C  C     . LEU D 2 256 ? 155.514 99.179  142.914 1.00 21.49 ?  235 LEU D C     1 
ATOM   15274 O  O     . LEU D 2 256 ? 156.177 99.451  141.919 1.00 20.89 ?  235 LEU D O     1 
ATOM   15275 C  CB    . LEU D 2 256 ? 153.497 97.711  142.648 1.00 20.49 ?  235 LEU D CB    1 
ATOM   15276 C  CG    . LEU D 2 256 ? 152.871 96.315  142.517 1.00 21.52 ?  235 LEU D CG    1 
ATOM   15277 C  CD1   . LEU D 2 256 ? 151.355 96.390  142.267 1.00 20.71 ?  235 LEU D CD1   1 
ATOM   15278 C  CD2   . LEU D 2 256 ? 153.538 95.499  141.417 1.00 20.74 ?  235 LEU D CD2   1 
ATOM   15279 N  N     . TYR D 2 257 ? 155.238 100.064 143.871 1.00 21.42 ?  236 TYR D N     1 
ATOM   15280 C  CA    . TYR D 2 257 ? 155.706 101.446 143.775 1.00 22.02 ?  236 TYR D CA    1 
ATOM   15281 C  C     . TYR D 2 257 ? 157.231 101.549 143.768 1.00 22.61 ?  236 TYR D C     1 
ATOM   15282 O  O     . TYR D 2 257 ? 157.802 102.299 142.975 1.00 22.19 ?  236 TYR D O     1 
ATOM   15283 C  CB    . TYR D 2 257 ? 155.108 102.308 144.882 1.00 22.06 ?  236 TYR D CB    1 
ATOM   15284 C  CG    . TYR D 2 257 ? 155.672 103.709 144.942 1.00 23.44 ?  236 TYR D CG    1 
ATOM   15285 C  CD1   . TYR D 2 257 ? 155.432 104.627 143.912 1.00 24.01 ?  236 TYR D CD1   1 
ATOM   15286 C  CD2   . TYR D 2 257 ? 156.438 104.120 146.030 1.00 25.22 ?  236 TYR D CD2   1 
ATOM   15287 C  CE1   . TYR D 2 257 ? 155.949 105.920 143.970 1.00 25.14 ?  236 TYR D CE1   1 
ATOM   15288 C  CE2   . TYR D 2 257 ? 156.967 105.406 146.094 1.00 26.71 ?  236 TYR D CE2   1 
ATOM   15289 C  CZ    . TYR D 2 257 ? 156.716 106.297 145.067 1.00 25.35 ?  236 TYR D CZ    1 
ATOM   15290 O  OH    . TYR D 2 257 ? 157.233 107.564 145.148 1.00 26.77 ?  236 TYR D OH    1 
ATOM   15291 N  N     . GLU D 2 258 ? 157.893 100.790 144.639 1.00 23.09 ?  237 GLU D N     1 
ATOM   15292 C  CA    . GLU D 2 258 ? 159.354 100.851 144.699 1.00 23.98 ?  237 GLU D CA    1 
ATOM   15293 C  C     . GLU D 2 258 ? 159.993 100.329 143.411 1.00 23.13 ?  237 GLU D C     1 
ATOM   15294 O  O     . GLU D 2 258 ? 160.977 100.888 142.937 1.00 23.02 ?  237 GLU D O     1 
ATOM   15295 C  CB    . GLU D 2 258 ? 159.900 100.137 145.944 1.00 25.20 ?  237 GLU D CB    1 
ATOM   15296 C  CG    . GLU D 2 258 ? 159.506 100.821 147.265 1.00 28.82 ?  237 GLU D CG    1 
ATOM   15297 C  CD    . GLU D 2 258 ? 160.202 102.167 147.511 1.00 34.48 ?  237 GLU D CD    1 
ATOM   15298 O  OE1   . GLU D 2 258 ? 161.344 102.379 147.026 1.00 37.75 ?  237 GLU D OE1   1 
ATOM   15299 O  OE2   . GLU D 2 258 ? 159.606 103.023 148.211 1.00 37.16 -1 237 GLU D OE2   1 
ATOM   15300 N  N     . ASN D 2 259 ? 159.409 99.284  142.838 1.00 22.12 ?  238 ASN D N     1 
ATOM   15301 C  CA    . ASN D 2 259 ? 159.827 98.795  141.523 1.00 22.35 ?  238 ASN D CA    1 
ATOM   15302 C  C     . ASN D 2 259 ? 159.520 99.786  140.369 1.00 22.11 ?  238 ASN D C     1 
ATOM   15303 O  O     . ASN D 2 259 ? 160.313 99.906  139.432 1.00 22.24 ?  238 ASN D O     1 
ATOM   15304 C  CB    . ASN D 2 259 ? 159.213 97.417  141.246 1.00 21.69 ?  238 ASN D CB    1 
ATOM   15305 C  CG    . ASN D 2 259 ? 159.655 96.840  139.913 1.00 23.38 ?  238 ASN D CG    1 
ATOM   15306 O  OD1   . ASN D 2 259 ? 160.808 96.413  139.752 1.00 23.95 ?  238 ASN D OD1   1 
ATOM   15307 N  ND2   . ASN D 2 259 ? 158.747 96.835  138.946 1.00 21.14 ?  238 ASN D ND2   1 
ATOM   15308 N  N     . GLU D 2 260 ? 158.384 100.488 140.446 1.00 21.95 ?  239 GLU D N     1 
ATOM   15309 C  CA    . GLU D 2 260 ? 158.036 101.539 139.467 1.00 22.50 ?  239 GLU D CA    1 
ATOM   15310 C  C     . GLU D 2 260 ? 159.062 102.671 139.443 1.00 22.03 ?  239 GLU D C     1 
ATOM   15311 O  O     . GLU D 2 260 ? 159.353 103.225 138.387 1.00 22.03 ?  239 GLU D O     1 
ATOM   15312 C  CB    . GLU D 2 260 ? 156.660 102.167 139.754 1.00 22.90 ?  239 GLU D CB    1 
ATOM   15313 C  CG    . GLU D 2 260 ? 155.439 101.409 139.207 1.00 25.84 ?  239 GLU D CG    1 
ATOM   15314 C  CD    . GLU D 2 260 ? 155.572 100.993 137.746 1.00 28.59 ?  239 GLU D CD    1 
ATOM   15315 O  OE1   . GLU D 2 260 ? 156.241 99.973  137.479 1.00 28.18 ?  239 GLU D OE1   1 
ATOM   15316 O  OE2   . GLU D 2 260 ? 154.976 101.661 136.869 1.00 30.32 -1 239 GLU D OE2   1 
ATOM   15317 N  N     . LEU D 2 261 ? 159.578 103.034 140.612 1.00 21.50 ?  240 LEU D N     1 
ATOM   15318 C  CA    . LEU D 2 261 ? 160.587 104.085 140.691 1.00 22.03 ?  240 LEU D CA    1 
ATOM   15319 C  C     . LEU D 2 261 ? 161.836 103.659 139.940 1.00 21.52 ?  240 LEU D C     1 
ATOM   15320 O  O     . LEU D 2 261 ? 162.401 104.449 139.183 1.00 21.44 ?  240 LEU D O     1 
ATOM   15321 C  CB    . LEU D 2 261 ? 160.930 104.436 142.137 1.00 21.57 ?  240 LEU D CB    1 
ATOM   15322 C  CG    . LEU D 2 261 ? 159.811 104.975 143.028 1.00 23.22 ?  240 LEU D CG    1 
ATOM   15323 C  CD1   . LEU D 2 261 ? 160.363 105.222 144.420 1.00 23.06 ?  240 LEU D CD1   1 
ATOM   15324 C  CD2   . LEU D 2 261 ? 159.206 106.254 142.449 1.00 23.52 ?  240 LEU D CD2   1 
ATOM   15325 N  N     . GLU D 2 262 ? 162.245 102.405 140.135 1.00 21.69 ?  241 GLU D N     1 
ATOM   15326 C  CA    . GLU D 2 262 ? 163.406 101.853 139.417 1.00 22.31 ?  241 GLU D CA    1 
ATOM   15327 C  C     . GLU D 2 262 ? 163.135 101.720 137.917 1.00 21.69 ?  241 GLU D C     1 
ATOM   15328 O  O     . GLU D 2 262 ? 163.987 102.053 137.090 1.00 21.75 ?  241 GLU D O     1 
ATOM   15329 C  CB    . GLU D 2 262 ? 163.811 100.490 139.987 1.00 22.46 ?  241 GLU D CB    1 
ATOM   15330 C  CG    . GLU D 2 262 ? 164.244 100.485 141.455 1.00 25.63 ?  241 GLU D CG    1 
ATOM   15331 C  CD    . GLU D 2 262 ? 164.717 99.103  141.885 1.00 29.83 ?  241 GLU D CD    1 
ATOM   15332 O  OE1   . GLU D 2 262 ? 163.864 98.233  142.161 1.00 33.22 ?  241 GLU D OE1   1 
ATOM   15333 O  OE2   . GLU D 2 262 ? 165.938 98.872  141.919 1.00 33.36 -1 241 GLU D OE2   1 
ATOM   15334 N  N     . TYR D 2 263 ? 161.953 101.211 137.572 1.00 21.42 ?  242 TYR D N     1 
ATOM   15335 C  CA    . TYR D 2 263 ? 161.511 101.100 136.177 1.00 21.04 ?  242 TYR D CA    1 
ATOM   15336 C  C     . TYR D 2 263 ? 161.567 102.474 135.496 1.00 21.15 ?  242 TYR D C     1 
ATOM   15337 O  O     . TYR D 2 263 ? 162.007 102.600 134.353 1.00 20.32 ?  242 TYR D O     1 
ATOM   15338 C  CB    . TYR D 2 263 ? 160.076 100.549 136.138 1.00 20.95 ?  242 TYR D CB    1 
ATOM   15339 C  CG    . TYR D 2 263 ? 159.438 100.469 134.763 1.00 21.86 ?  242 TYR D CG    1 
ATOM   15340 C  CD1   . TYR D 2 263 ? 159.728 99.412  133.901 1.00 23.53 ?  242 TYR D CD1   1 
ATOM   15341 C  CD2   . TYR D 2 263 ? 158.544 101.451 134.325 1.00 21.20 ?  242 TYR D CD2   1 
ATOM   15342 C  CE1   . TYR D 2 263 ? 159.145 99.332  132.644 1.00 23.34 ?  242 TYR D CE1   1 
ATOM   15343 C  CE2   . TYR D 2 263 ? 157.957 101.378 133.066 1.00 23.11 ?  242 TYR D CE2   1 
ATOM   15344 C  CZ    . TYR D 2 263 ? 158.268 100.318 132.231 1.00 23.27 ?  242 TYR D CZ    1 
ATOM   15345 O  OH    . TYR D 2 263 ? 157.688 100.241 130.983 1.00 27.07 ?  242 TYR D OH    1 
ATOM   15346 N  N     . THR D 2 264 ? 161.098 103.488 136.221 1.00 21.12 ?  243 THR D N     1 
ATOM   15347 C  CA    . THR D 2 264 ? 161.013 104.858 135.724 1.00 21.98 ?  243 THR D CA    1 
ATOM   15348 C  C     . THR D 2 264 ? 162.397 105.431 135.425 1.00 22.32 ?  243 THR D C     1 
ATOM   15349 O  O     . THR D 2 264 ? 162.631 105.931 134.327 1.00 21.78 ?  243 THR D O     1 
ATOM   15350 C  CB    . THR D 2 264 ? 160.229 105.755 136.707 1.00 21.68 ?  243 THR D CB    1 
ATOM   15351 O  OG1   . THR D 2 264 ? 158.870 105.311 136.755 1.00 23.29 ?  243 THR D OG1   1 
ATOM   15352 C  CG2   . THR D 2 264 ? 160.268 107.240 136.298 1.00 23.16 ?  243 THR D CG2   1 
ATOM   15353 N  N     . GLU D 2 265 ? 163.313 105.334 136.388 1.00 22.48 ?  244 GLU D N     1 
ATOM   15354 C  CA    . GLU D 2 265 ? 164.673 105.834 136.170 1.00 23.73 ?  244 GLU D CA    1 
ATOM   15355 C  C     . GLU D 2 265 ? 165.351 105.115 135.014 1.00 23.85 ?  244 GLU D C     1 
ATOM   15356 O  O     . GLU D 2 265 ? 166.023 105.749 134.210 1.00 24.40 ?  244 GLU D O     1 
ATOM   15357 C  CB    . GLU D 2 265 ? 165.511 105.712 137.434 1.00 23.19 ?  244 GLU D CB    1 
ATOM   15358 C  CG    . GLU D 2 265 ? 165.120 106.733 138.468 1.00 25.08 ?  244 GLU D CG    1 
ATOM   15359 C  CD    . GLU D 2 265 ? 165.815 106.527 139.798 1.00 27.30 ?  244 GLU D CD    1 
ATOM   15360 O  OE1   . GLU D 2 265 ? 166.758 105.717 139.874 1.00 27.77 ?  244 GLU D OE1   1 
ATOM   15361 O  OE2   . GLU D 2 265 ? 165.408 107.188 140.771 1.00 28.63 -1 244 GLU D OE2   1 
ATOM   15362 N  N     . ASP D 2 266 ? 165.135 103.803 134.923 1.00 24.13 ?  245 ASP D N     1 
ATOM   15363 C  CA    . ASP D 2 266 ? 165.718 102.965 133.871 1.00 25.22 ?  245 ASP D CA    1 
ATOM   15364 C  C     . ASP D 2 266 ? 165.328 103.433 132.452 1.00 24.84 ?  245 ASP D C     1 
ATOM   15365 O  O     . ASP D 2 266 ? 166.147 103.376 131.529 1.00 25.64 ?  245 ASP D O     1 
ATOM   15366 C  CB    . ASP D 2 266 ? 165.307 101.502 134.102 1.00 25.79 ?  245 ASP D CB    1 
ATOM   15367 C  CG    . ASP D 2 266 ? 165.977 100.532 133.139 1.00 27.71 ?  245 ASP D CG    1 
ATOM   15368 O  OD1   . ASP D 2 266 ? 167.216 100.519 133.075 1.00 31.57 ?  245 ASP D OD1   1 
ATOM   15369 O  OD2   . ASP D 2 266 ? 165.266 99.760  132.461 1.00 30.29 -1 245 ASP D OD2   1 
ATOM   15370 N  N     . LEU D 2 267 ? 164.097 103.911 132.291 1.00 24.07 ?  246 LEU D N     1 
ATOM   15371 C  CA    . LEU D 2 267 ? 163.580 104.323 130.984 1.00 23.98 ?  246 LEU D CA    1 
ATOM   15372 C  C     . LEU D 2 267 ? 163.683 105.823 130.701 1.00 22.83 ?  246 LEU D C     1 
ATOM   15373 O  O     . LEU D 2 267 ? 163.973 106.220 129.566 1.00 23.00 ?  246 LEU D O     1 
ATOM   15374 C  CB    . LEU D 2 267 ? 162.112 103.892 130.819 1.00 23.82 ?  246 LEU D CB    1 
ATOM   15375 C  CG    . LEU D 2 267 ? 161.848 102.387 130.684 1.00 26.05 ?  246 LEU D CG    1 
ATOM   15376 C  CD1   . LEU D 2 267 ? 160.424 102.134 130.269 1.00 26.74 ?  246 LEU D CD1   1 
ATOM   15377 C  CD2   . LEU D 2 267 ? 162.793 101.737 129.692 1.00 28.00 ?  246 LEU D CD2   1 
ATOM   15378 N  N     . TYR D 2 268 ? 163.441 106.639 131.728 1.00 21.68 ?  247 TYR D N     1 
ATOM   15379 C  CA    . TYR D 2 268 ? 163.247 108.080 131.541 1.00 20.95 ?  247 TYR D CA    1 
ATOM   15380 C  C     . TYR D 2 268 ? 164.432 108.993 131.884 1.00 21.43 ?  247 TYR D C     1 
ATOM   15381 O  O     . TYR D 2 268 ? 164.432 110.153 131.475 1.00 20.73 ?  247 TYR D O     1 
ATOM   15382 C  CB    . TYR D 2 268 ? 162.007 108.563 132.300 1.00 20.27 ?  247 TYR D CB    1 
ATOM   15383 C  CG    . TYR D 2 268 ? 160.686 108.103 131.710 1.00 19.54 ?  247 TYR D CG    1 
ATOM   15384 C  CD1   . TYR D 2 268 ? 159.982 107.045 132.275 1.00 18.52 ?  247 TYR D CD1   1 
ATOM   15385 C  CD2   . TYR D 2 268 ? 160.145 108.732 130.579 1.00 20.62 ?  247 TYR D CD2   1 
ATOM   15386 C  CE1   . TYR D 2 268 ? 158.740 106.616 131.738 1.00 18.33 ?  247 TYR D CE1   1 
ATOM   15387 C  CE2   . TYR D 2 268 ? 158.909 108.314 130.031 1.00 20.79 ?  247 TYR D CE2   1 
ATOM   15388 C  CZ    . TYR D 2 268 ? 158.218 107.266 130.624 1.00 20.23 ?  247 TYR D CZ    1 
ATOM   15389 O  OH    . TYR D 2 268 ? 157.014 106.867 130.080 1.00 20.50 ?  247 TYR D OH    1 
ATOM   15390 N  N     . ASP D 2 269 ? 165.421 108.501 132.638 1.00 21.65 ?  248 ASP D N     1 
ATOM   15391 C  CA    . ASP D 2 269 ? 166.618 109.316 132.874 1.00 22.30 ?  248 ASP D CA    1 
ATOM   15392 C  C     . ASP D 2 269 ? 167.294 109.779 131.562 1.00 22.54 ?  248 ASP D C     1 
ATOM   15393 O  O     . ASP D 2 269 ? 167.766 110.916 131.479 1.00 22.49 ?  248 ASP D O     1 
ATOM   15394 C  CB    . ASP D 2 269 ? 167.627 108.603 133.776 1.00 22.83 ?  248 ASP D CB    1 
ATOM   15395 C  CG    . ASP D 2 269 ? 167.280 108.718 135.256 1.00 23.55 ?  248 ASP D CG    1 
ATOM   15396 O  OD1   . ASP D 2 269 ? 166.350 109.473 135.605 1.00 24.95 ?  248 ASP D OD1   1 
ATOM   15397 O  OD2   . ASP D 2 269 ? 167.943 108.045 136.079 1.00 24.47 -1 248 ASP D OD2   1 
ATOM   15398 N  N     . GLN D 2 270 ? 167.327 108.910 130.550 1.00 22.79 ?  249 GLN D N     1 
ATOM   15399 C  CA    . GLN D 2 270 ? 167.979 109.237 129.275 1.00 23.41 ?  249 GLN D CA    1 
ATOM   15400 C  C     . GLN D 2 270 ? 167.276 110.348 128.490 1.00 22.83 ?  249 GLN D C     1 
ATOM   15401 O  O     . GLN D 2 270 ? 167.859 110.914 127.568 1.00 23.75 ?  249 GLN D O     1 
ATOM   15402 C  CB    . GLN D 2 270 ? 168.159 107.995 128.395 1.00 24.02 ?  249 GLN D CB    1 
ATOM   15403 C  CG    . GLN D 2 270 ? 166.855 107.415 127.819 1.00 25.40 ?  249 GLN D CG    1 
ATOM   15404 C  CD    . GLN D 2 270 ? 167.045 106.030 127.224 1.00 29.23 ?  249 GLN D CD    1 
ATOM   15405 O  OE1   . GLN D 2 270 ? 167.887 105.256 127.684 1.00 31.31 ?  249 GLN D OE1   1 
ATOM   15406 N  NE2   . GLN D 2 270 ? 166.253 105.703 126.205 1.00 30.04 ?  249 GLN D NE2   1 
ATOM   15407 N  N     . VAL D 2 271 ? 166.025 110.643 128.842 1.00 21.93 ?  250 VAL D N     1 
ATOM   15408 C  CA    . VAL D 2 271 ? 165.296 111.760 128.232 1.00 21.29 ?  250 VAL D CA    1 
ATOM   15409 C  C     . VAL D 2 271 ? 164.914 112.840 129.262 1.00 21.16 ?  250 VAL D C     1 
ATOM   15410 O  O     . VAL D 2 271 ? 164.118 113.736 128.966 1.00 21.54 ?  250 VAL D O     1 
ATOM   15411 C  CB    . VAL D 2 271 ? 164.055 111.261 127.424 1.00 21.62 ?  250 VAL D CB    1 
ATOM   15412 C  CG1   . VAL D 2 271 ? 164.498 110.405 126.240 1.00 21.36 ?  250 VAL D CG1   1 
ATOM   15413 C  CG2   . VAL D 2 271 ? 163.075 110.485 128.324 1.00 21.17 ?  250 VAL D CG2   1 
ATOM   15414 N  N     . GLY D 2 272 ? 165.469 112.732 130.475 1.00 20.92 ?  251 GLY D N     1 
ATOM   15415 C  CA    . GLY D 2 272 ? 165.359 113.774 131.516 1.00 20.61 ?  251 GLY D CA    1 
ATOM   15416 C  C     . GLY D 2 272 ? 163.994 114.011 132.157 1.00 20.77 ?  251 GLY D C     1 
ATOM   15417 O  O     . GLY D 2 272 ? 163.719 115.110 132.661 1.00 20.28 ?  251 GLY D O     1 
ATOM   15418 N  N     . LEU D 2 273 ? 163.145 112.986 132.165 1.00 19.85 ?  252 LEU D N     1 
ATOM   15419 C  CA    . LEU D 2 273 ? 161.755 113.178 132.582 1.00 20.09 ?  252 LEU D CA    1 
ATOM   15420 C  C     . LEU D 2 273 ? 161.345 112.521 133.903 1.00 19.88 ?  252 LEU D C     1 
ATOM   15421 O  O     . LEU D 2 273 ? 160.222 112.722 134.353 1.00 20.04 ?  252 LEU D O     1 
ATOM   15422 C  CB    . LEU D 2 273 ? 160.816 112.679 131.472 1.00 19.97 ?  252 LEU D CB    1 
ATOM   15423 C  CG    . LEU D 2 273 ? 160.950 113.338 130.107 1.00 20.26 ?  252 LEU D CG    1 
ATOM   15424 C  CD1   . LEU D 2 273 ? 159.869 112.778 129.209 1.00 18.98 ?  252 LEU D CD1   1 
ATOM   15425 C  CD2   . LEU D 2 273 ? 160.852 114.887 130.193 1.00 21.03 ?  252 LEU D CD2   1 
ATOM   15426 N  N     . SER D 2 274 ? 162.255 111.761 134.514 0.50 19.54 ?  253 SER D N     1 
ATOM   15427 C  CA    . SER D 2 274 ? 161.910 110.868 135.632 0.50 19.34 ?  253 SER D CA    1 
ATOM   15428 C  C     . SER D 2 274 ? 161.205 111.542 136.814 0.50 20.05 ?  253 SER D C     1 
ATOM   15429 O  O     . SER D 2 274 ? 160.258 110.982 137.366 0.50 20.31 ?  253 SER D O     1 
ATOM   15430 C  CB    . SER D 2 274 ? 163.140 110.086 136.113 0.50 18.97 ?  253 SER D CB    1 
ATOM   15431 O  OG    . SER D 2 274 ? 163.738 109.362 135.054 0.50 15.35 ?  253 SER D OG    1 
ATOM   15432 N  N     . HIS D 2 275 ? 161.671 112.728 137.204 1.00 20.77 ?  254 HIS D N     1 
ATOM   15433 C  CA    . HIS D 2 275 ? 161.038 113.494 138.297 1.00 21.18 ?  254 HIS D CA    1 
ATOM   15434 C  C     . HIS D 2 275 ? 159.526 113.682 138.075 1.00 21.50 ?  254 HIS D C     1 
ATOM   15435 O  O     . HIS D 2 275 ? 158.715 113.397 138.972 1.00 19.88 ?  254 HIS D O     1 
ATOM   15436 C  CB    . HIS D 2 275 ? 161.721 114.856 138.505 1.00 21.60 ?  254 HIS D CB    1 
ATOM   15437 C  CG    . HIS D 2 275 ? 161.032 115.721 139.517 1.00 22.43 ?  254 HIS D CG    1 
ATOM   15438 N  ND1   . HIS D 2 275 ? 161.324 115.673 140.866 1.00 22.77 ?  254 HIS D ND1   1 
ATOM   15439 C  CD2   . HIS D 2 275 ? 160.049 116.645 139.377 1.00 22.50 ?  254 HIS D CD2   1 
ATOM   15440 C  CE1   . HIS D 2 275 ? 160.554 116.536 141.509 1.00 24.05 ?  254 HIS D CE1   1 
ATOM   15441 N  NE2   . HIS D 2 275 ? 159.767 117.133 140.629 1.00 23.22 ?  254 HIS D NE2   1 
ATOM   15442 N  N     . ASP D 2 276 ? 159.161 114.144 136.878 1.00 22.34 ?  255 ASP D N     1 
ATOM   15443 C  CA    . ASP D 2 276 ? 157.759 114.379 136.545 1.00 23.19 ?  255 ASP D CA    1 
ATOM   15444 C  C     . ASP D 2 276 ? 156.969 113.087 136.395 1.00 22.17 ?  255 ASP D C     1 
ATOM   15445 O  O     . ASP D 2 276 ? 155.796 113.049 136.737 1.00 21.87 ?  255 ASP D O     1 
ATOM   15446 C  CB    . ASP D 2 276 ? 157.616 115.221 135.267 1.00 24.33 ?  255 ASP D CB    1 
ATOM   15447 C  CG    . ASP D 2 276 ? 157.637 116.728 135.535 1.00 27.58 ?  255 ASP D CG    1 
ATOM   15448 O  OD1   . ASP D 2 276 ? 157.308 117.164 136.660 1.00 31.10 ?  255 ASP D OD1   1 
ATOM   15449 O  OD2   . ASP D 2 276 ? 157.993 117.481 134.599 1.00 29.88 -1 255 ASP D OD2   1 
ATOM   15450 N  N     . VAL D 2 277 ? 157.598 112.046 135.850 1.00 21.21 ?  256 VAL D N     1 
ATOM   15451 C  CA    . VAL D 2 277 ? 156.939 110.741 135.738 1.00 20.51 ?  256 VAL D CA    1 
ATOM   15452 C  C     . VAL D 2 277 ? 156.590 110.176 137.120 1.00 20.32 ?  256 VAL D C     1 
ATOM   15453 O  O     . VAL D 2 277 ? 155.509 109.625 137.308 1.00 19.81 ?  256 VAL D O     1 
ATOM   15454 C  CB    . VAL D 2 277 ? 157.781 109.713 134.930 1.00 20.30 ?  256 VAL D CB    1 
ATOM   15455 C  CG1   . VAL D 2 277 ? 157.093 108.359 134.905 1.00 21.16 ?  256 VAL D CG1   1 
ATOM   15456 C  CG2   . VAL D 2 277 ? 158.001 110.206 133.511 1.00 19.06 ?  256 VAL D CG2   1 
ATOM   15457 N  N     . LYS D 2 278 ? 157.504 110.340 138.077 1.00 19.84 ?  257 LYS D N     1 
ATOM   15458 C  CA    . LYS D 2 278 ? 157.274 109.898 139.452 1.00 20.27 ?  257 LYS D CA    1 
ATOM   15459 C  C     . LYS D 2 278 ? 156.048 110.565 140.089 1.00 20.16 ?  257 LYS D C     1 
ATOM   15460 O  O     . LYS D 2 278 ? 155.273 109.891 140.762 1.00 19.88 ?  257 LYS D O     1 
ATOM   15461 C  CB    . LYS D 2 278 ? 158.525 110.087 140.314 1.00 20.20 ?  257 LYS D CB    1 
ATOM   15462 C  CG    . LYS D 2 278 ? 159.626 109.078 140.004 1.00 21.60 ?  257 LYS D CG    1 
ATOM   15463 C  CD    . LYS D 2 278 ? 160.944 109.453 140.670 1.00 21.53 ?  257 LYS D CD    1 
ATOM   15464 C  CE    . LYS D 2 278 ? 162.038 108.525 140.200 1.00 24.52 ?  257 LYS D CE    1 
ATOM   15465 N  NZ    . LYS D 2 278 ? 163.338 108.854 140.872 1.00 26.32 1  257 LYS D NZ    1 
ATOM   15466 N  N     . LYS D 2 279 ? 155.866 111.869 139.852 1.00 19.67 ?  258 LYS D N     1 
ATOM   15467 C  CA    . LYS D 2 279 ? 154.661 112.567 140.324 1.00 20.10 ?  258 LYS D CA    1 
ATOM   15468 C  C     . LYS D 2 279 ? 153.391 111.944 139.732 1.00 19.12 ?  258 LYS D C     1 
ATOM   15469 O  O     . LYS D 2 279 ? 152.392 111.785 140.436 1.00 18.59 ?  258 LYS D O     1 
ATOM   15470 C  CB    . LYS D 2 279 ? 154.708 114.075 140.009 1.00 20.54 ?  258 LYS D CB    1 
ATOM   15471 C  CG    . LYS D 2 279 ? 155.864 114.833 140.659 1.00 22.84 ?  258 LYS D CG    1 
ATOM   15472 C  CD    . LYS D 2 279 ? 155.569 116.345 140.805 1.00 24.16 ?  258 LYS D CD    1 
ATOM   15473 C  CE    . LYS D 2 279 ? 155.468 117.058 139.461 1.00 25.61 ?  258 LYS D CE    1 
ATOM   15474 N  NZ    . LYS D 2 279 ? 155.185 118.539 139.614 1.00 24.70 1  258 LYS D NZ    1 
ATOM   15475 N  N     . PHE D 2 280 ? 153.457 111.579 138.448 1.00 19.04 ?  259 PHE D N     1 
ATOM   15476 C  CA    . PHE D 2 280 ? 152.332 110.968 137.715 1.00 19.31 ?  259 PHE D CA    1 
ATOM   15477 C  C     . PHE D 2 280 ? 151.984 109.562 138.218 1.00 19.25 ?  259 PHE D C     1 
ATOM   15478 O  O     . PHE D 2 280 ? 150.806 109.194 138.303 1.00 19.71 ?  259 PHE D O     1 
ATOM   15479 C  CB    . PHE D 2 280 ? 152.655 110.917 136.222 1.00 19.04 ?  259 PHE D CB    1 
ATOM   15480 C  CG    . PHE D 2 280 ? 151.455 110.681 135.324 1.00 20.15 ?  259 PHE D CG    1 
ATOM   15481 C  CD1   . PHE D 2 280 ? 150.351 111.519 135.370 1.00 21.63 ?  259 PHE D CD1   1 
ATOM   15482 C  CD2   . PHE D 2 280 ? 151.470 109.640 134.392 1.00 19.95 ?  259 PHE D CD2   1 
ATOM   15483 C  CE1   . PHE D 2 280 ? 149.255 111.316 134.502 1.00 22.56 ?  259 PHE D CE1   1 
ATOM   15484 C  CE2   . PHE D 2 280 ? 150.398 109.427 133.528 1.00 20.29 ?  259 PHE D CE2   1 
ATOM   15485 C  CZ    . PHE D 2 280 ? 149.284 110.266 133.584 1.00 21.30 ?  259 PHE D CZ    1 
ATOM   15486 N  N     . ILE D 2 281 ? 153.006 108.773 138.533 1.00 19.36 ?  260 ILE D N     1 
ATOM   15487 C  CA    . ILE D 2 281 ? 152.810 107.471 139.178 1.00 19.45 ?  260 ILE D CA    1 
ATOM   15488 C  C     . ILE D 2 281 ? 152.057 107.587 140.521 1.00 19.61 ?  260 ILE D C     1 
ATOM   15489 O  O     . ILE D 2 281 ? 151.102 106.843 140.754 1.00 19.72 ?  260 ILE D O     1 
ATOM   15490 C  CB    . ILE D 2 281 ? 154.173 106.753 139.355 1.00 19.49 ?  260 ILE D CB    1 
ATOM   15491 C  CG1   . ILE D 2 281 ? 154.756 106.411 137.980 1.00 20.10 ?  260 ILE D CG1   1 
ATOM   15492 C  CG2   . ILE D 2 281 ? 154.074 105.513 140.271 1.00 20.53 ?  260 ILE D CG2   1 
ATOM   15493 C  CD1   . ILE D 2 281 ? 156.235 106.016 138.055 1.00 21.17 ?  260 ILE D CD1   1 
ATOM   15494 N  N     . ARG D 2 282 ? 152.476 108.516 141.383 1.00 19.75 ?  261 ARG D N     1 
ATOM   15495 C  CA    . ARG D 2 282 ? 151.860 108.673 142.715 1.00 20.34 ?  261 ARG D CA    1 
ATOM   15496 C  C     . ARG D 2 282 ? 150.413 109.143 142.620 1.00 21.18 ?  261 ARG D C     1 
ATOM   15497 O  O     . ARG D 2 282 ? 149.536 108.673 143.360 1.00 21.68 ?  261 ARG D O     1 
ATOM   15498 C  CB    . ARG D 2 282 ? 152.679 109.621 143.601 1.00 20.20 ?  261 ARG D CB    1 
ATOM   15499 C  CG    . ARG D 2 282 ? 154.003 109.040 144.063 1.00 20.57 ?  261 ARG D CG    1 
ATOM   15500 C  CD    . ARG D 2 282 ? 154.691 109.959 145.075 1.00 23.15 ?  261 ARG D CD    1 
ATOM   15501 N  NE    . ARG D 2 282 ? 155.274 111.161 144.473 1.00 23.46 ?  261 ARG D NE    1 
ATOM   15502 C  CZ    . ARG D 2 282 ? 156.510 111.239 143.981 1.00 22.84 ?  261 ARG D CZ    1 
ATOM   15503 N  NH1   . ARG D 2 282 ? 157.304 110.177 143.976 1.00 23.37 1  261 ARG D NH1   1 
ATOM   15504 N  NH2   . ARG D 2 282 ? 156.947 112.386 143.480 1.00 22.27 ?  261 ARG D NH2   1 
ATOM   15505 N  N     . TYR D 2 283 ? 150.179 110.088 141.717 1.00 21.46 ?  262 TYR D N     1 
ATOM   15506 C  CA    . TYR D 2 283 ? 148.838 110.600 141.442 1.00 22.97 ?  262 TYR D CA    1 
ATOM   15507 C  C     . TYR D 2 283 ? 147.907 109.453 140.988 1.00 22.12 ?  262 TYR D C     1 
ATOM   15508 O  O     . TYR D 2 283 ? 146.765 109.350 141.442 1.00 22.00 ?  262 TYR D O     1 
ATOM   15509 C  CB    . TYR D 2 283 ? 148.948 111.722 140.403 1.00 23.37 ?  262 TYR D CB    1 
ATOM   15510 C  CG    . TYR D 2 283 ? 147.667 112.151 139.727 1.00 27.31 ?  262 TYR D CG    1 
ATOM   15511 C  CD1   . TYR D 2 283 ? 146.848 113.126 140.297 1.00 30.79 ?  262 TYR D CD1   1 
ATOM   15512 C  CD2   . TYR D 2 283 ? 147.298 111.613 138.495 1.00 30.31 ?  262 TYR D CD2   1 
ATOM   15513 C  CE1   . TYR D 2 283 ? 145.661 113.531 139.666 1.00 33.18 ?  262 TYR D CE1   1 
ATOM   15514 C  CE2   . TYR D 2 283 ? 146.125 112.016 137.850 1.00 33.20 ?  262 TYR D CE2   1 
ATOM   15515 C  CZ    . TYR D 2 283 ? 145.316 112.980 138.441 1.00 34.74 ?  262 TYR D CZ    1 
ATOM   15516 O  OH    . TYR D 2 283 ? 144.161 113.382 137.799 1.00 37.63 ?  262 TYR D OH    1 
ATOM   15517 N  N     . ASN D 2 284 ? 148.414 108.565 140.136 1.00 21.63 ?  263 ASN D N     1 
ATOM   15518 C  CA    . ASN D 2 284 ? 147.611 107.440 139.665 1.00 21.41 ?  263 ASN D CA    1 
ATOM   15519 C  C     . ASN D 2 284 ? 147.483 106.308 140.688 1.00 20.86 ?  263 ASN D C     1 
ATOM   15520 O  O     . ASN D 2 284 ? 146.464 105.628 140.724 1.00 20.92 ?  263 ASN D O     1 
ATOM   15521 C  CB    . ASN D 2 284 ? 148.091 106.946 138.299 1.00 21.15 ?  263 ASN D CB    1 
ATOM   15522 C  CG    . ASN D 2 284 ? 147.683 107.889 137.175 1.00 22.59 ?  263 ASN D CG    1 
ATOM   15523 O  OD1   . ASN D 2 284 ? 146.507 107.966 136.812 1.00 22.35 ?  263 ASN D OD1   1 
ATOM   15524 N  ND2   . ASN D 2 284 ? 148.650 108.623 136.630 1.00 22.93 ?  263 ASN D ND2   1 
ATOM   15525 N  N     . ALA D 2 285 ? 148.509 106.118 141.518 1.00 20.92 ?  264 ALA D N     1 
ATOM   15526 C  CA    . ALA D 2 285 ? 148.412 105.219 142.681 1.00 20.77 ?  264 ALA D CA    1 
ATOM   15527 C  C     . ALA D 2 285 ? 147.257 105.615 143.608 1.00 21.13 ?  264 ALA D C     1 
ATOM   15528 O  O     . ALA D 2 285 ? 146.499 104.753 144.069 1.00 19.92 ?  264 ALA D O     1 
ATOM   15529 C  CB    . ALA D 2 285 ? 149.739 105.178 143.454 1.00 20.68 ?  264 ALA D CB    1 
ATOM   15530 N  N     . ASN D 2 286 ? 147.127 106.920 143.869 1.00 21.38 ?  265 ASN D N     1 
ATOM   15531 C  CA    . ASN D 2 286 ? 146.022 107.457 144.667 1.00 21.94 ?  265 ASN D CA    1 
ATOM   15532 C  C     . ASN D 2 286 ? 144.649 107.180 144.029 1.00 22.13 ?  265 ASN D C     1 
ATOM   15533 O  O     . ASN D 2 286 ? 143.694 106.867 144.730 1.00 21.95 ?  265 ASN D O     1 
ATOM   15534 C  CB    . ASN D 2 286 ? 146.189 108.961 144.893 1.00 22.22 ?  265 ASN D CB    1 
ATOM   15535 C  CG    . ASN D 2 286 ? 147.191 109.301 145.993 1.00 22.80 ?  265 ASN D CG    1 
ATOM   15536 O  OD1   . ASN D 2 286 ? 147.614 108.446 146.779 1.00 22.57 ?  265 ASN D OD1   1 
ATOM   15537 N  ND2   . ASN D 2 286 ? 147.577 110.571 146.043 1.00 23.91 ?  265 ASN D ND2   1 
ATOM   15538 N  N     . LYS D 2 287 ? 144.557 107.288 142.705 1.00 22.51 ?  266 LYS D N     1 
ATOM   15539 C  CA    . LYS D 2 287 ? 143.307 106.961 142.006 1.00 22.91 ?  266 LYS D CA    1 
ATOM   15540 C  C     . LYS D 2 287 ? 142.955 105.475 142.161 1.00 22.33 ?  266 LYS D C     1 
ATOM   15541 O  O     . LYS D 2 287 ? 141.801 105.138 142.395 1.00 22.24 ?  266 LYS D O     1 
ATOM   15542 C  CB    . LYS D 2 287 ? 143.377 107.345 140.521 1.00 23.65 ?  266 LYS D CB    1 
ATOM   15543 C  CG    . LYS D 2 287 ? 143.267 108.849 140.268 1.00 26.50 ?  266 LYS D CG    1 
ATOM   15544 C  CD    . LYS D 2 287 ? 143.331 109.154 138.760 1.00 31.30 ?  266 LYS D CD    1 
ATOM   15545 C  CE    . LYS D 2 287 ? 142.734 110.519 138.471 1.00 35.08 ?  266 LYS D CE    1 
ATOM   15546 N  NZ    . LYS D 2 287 ? 142.725 110.878 137.021 1.00 37.66 1  266 LYS D NZ    1 
ATOM   15547 N  N     . ALA D 2 288 ? 143.961 104.607 142.043 1.00 21.41 ?  267 ALA D N     1 
ATOM   15548 C  CA    . ALA D 2 288 ? 143.800 103.163 142.212 1.00 21.53 ?  267 ALA D CA    1 
ATOM   15549 C  C     . ALA D 2 288 ? 143.298 102.810 143.623 1.00 21.77 ?  267 ALA D C     1 
ATOM   15550 O  O     . ALA D 2 288 ? 142.378 101.991 143.793 1.00 21.59 ?  267 ALA D O     1 
ATOM   15551 C  CB    . ALA D 2 288 ? 145.118 102.438 141.902 1.00 21.33 ?  267 ALA D CB    1 
ATOM   15552 N  N     . LEU D 2 289 ? 143.885 103.446 144.629 1.00 21.71 ?  268 LEU D N     1 
ATOM   15553 C  CA    . LEU D 2 289 ? 143.420 103.276 146.000 1.00 22.36 ?  268 LEU D CA    1 
ATOM   15554 C  C     . LEU D 2 289 ? 141.979 103.743 146.153 1.00 23.01 ?  268 LEU D C     1 
ATOM   15555 O  O     . LEU D 2 289 ? 141.155 103.043 146.747 1.00 23.14 ?  268 LEU D O     1 
ATOM   15556 C  CB    . LEU D 2 289 ? 144.349 103.989 146.989 1.00 22.61 ?  268 LEU D CB    1 
ATOM   15557 C  CG    . LEU D 2 289 ? 145.744 103.351 147.166 1.00 21.22 ?  268 LEU D CG    1 
ATOM   15558 C  CD1   . LEU D 2 289 ? 146.681 104.292 147.908 1.00 20.77 ?  268 LEU D CD1   1 
ATOM   15559 C  CD2   . LEU D 2 289 ? 145.670 101.984 147.882 1.00 21.40 ?  268 LEU D CD2   1 
ATOM   15560 N  N     . MET D 2 290 ? 141.655 104.907 145.599 1.00 23.87 ?  269 MET D N     1 
ATOM   15561 C  CA    . MET D 2 290 ? 140.277 105.383 145.686 1.00 25.26 ?  269 MET D CA    1 
ATOM   15562 C  C     . MET D 2 290 ? 139.294 104.427 144.987 1.00 24.37 ?  269 MET D C     1 
ATOM   15563 O  O     . MET D 2 290 ? 138.205 104.198 145.504 1.00 23.97 ?  269 MET D O     1 
ATOM   15564 C  CB    . MET D 2 290 ? 140.158 106.835 145.237 1.00 25.94 ?  269 MET D CB    1 
ATOM   15565 C  CG    . MET D 2 290 ? 140.619 107.798 146.349 1.00 31.08 ?  269 MET D CG    1 
ATOM   15566 S  SD    . MET D 2 290 ? 140.546 109.548 145.904 1.00 41.28 ?  269 MET D SD    1 
ATOM   15567 C  CE    . MET D 2 290 ? 138.835 109.704 145.330 1.00 38.56 ?  269 MET D CE    1 
ATOM   15568 N  N     . ASN D 2 291 ? 139.698 103.836 143.858 1.00 23.66 ?  270 ASN D N     1 
ATOM   15569 C  CA    . ASN D 2 291 ? 138.896 102.774 143.207 1.00 23.17 ?  270 ASN D CA    1 
ATOM   15570 C  C     . ASN D 2 291 ? 138.581 101.578 144.111 1.00 23.22 ?  270 ASN D C     1 
ATOM   15571 O  O     . ASN D 2 291 ? 137.545 100.933 143.955 1.00 22.68 ?  270 ASN D O     1 
ATOM   15572 C  CB    . ASN D 2 291 ? 139.563 102.267 141.919 1.00 22.41 ?  270 ASN D CB    1 
ATOM   15573 C  CG    . ASN D 2 291 ? 139.545 103.295 140.810 1.00 21.93 ?  270 ASN D CG    1 
ATOM   15574 O  OD1   . ASN D 2 291 ? 138.830 104.299 140.887 1.00 20.94 ?  270 ASN D OD1   1 
ATOM   15575 N  ND2   . ASN D 2 291 ? 140.334 103.052 139.767 1.00 19.20 ?  270 ASN D ND2   1 
ATOM   15576 N  N     . LEU D 2 292 ? 139.488 101.298 145.045 1.00 23.53 ?  271 LEU D N     1 
ATOM   15577 C  CA    . LEU D 2 292 ? 139.330 100.204 146.006 1.00 24.21 ?  271 LEU D CA    1 
ATOM   15578 C  C     . LEU D 2 292 ? 138.695 100.675 147.318 1.00 25.14 ?  271 LEU D C     1 
ATOM   15579 O  O     . LEU D 2 292 ? 138.652 99.929  148.309 1.00 25.14 ?  271 LEU D O     1 
ATOM   15580 C  CB    . LEU D 2 292 ? 140.690 99.521  146.270 1.00 23.71 ?  271 LEU D CB    1 
ATOM   15581 C  CG    . LEU D 2 292 ? 141.367 98.809  145.090 1.00 23.37 ?  271 LEU D CG    1 
ATOM   15582 C  CD1   . LEU D 2 292 ? 142.846 98.544  145.386 1.00 23.28 ?  271 LEU D CD1   1 
ATOM   15583 C  CD2   . LEU D 2 292 ? 140.641 97.500  144.720 1.00 23.06 ?  271 LEU D CD2   1 
ATOM   15584 N  N     . GLY D 2 293 ? 138.193 101.912 147.314 1.00 25.82 ?  272 GLY D N     1 
ATOM   15585 C  CA    . GLY D 2 293 ? 137.547 102.498 148.482 1.00 27.13 ?  272 GLY D CA    1 
ATOM   15586 C  C     . GLY D 2 293 ? 138.491 102.848 149.614 1.00 27.99 ?  272 GLY D C     1 
ATOM   15587 O  O     . GLY D 2 293 ? 138.055 103.012 150.750 1.00 27.97 ?  272 GLY D O     1 
ATOM   15588 N  N     . PHE D 2 294 ? 139.786 102.962 149.306 1.00 28.02 ?  273 PHE D N     1 
ATOM   15589 C  CA    . PHE D 2 294 ? 140.806 103.309 150.305 1.00 28.75 ?  273 PHE D CA    1 
ATOM   15590 C  C     . PHE D 2 294 ? 141.235 104.779 150.216 1.00 29.00 ?  273 PHE D C     1 
ATOM   15591 O  O     . PHE D 2 294 ? 141.046 105.424 149.187 1.00 28.74 ?  273 PHE D O     1 
ATOM   15592 C  CB    . PHE D 2 294 ? 142.041 102.407 150.147 1.00 28.32 ?  273 PHE D CB    1 
ATOM   15593 C  CG    . PHE D 2 294 ? 141.777 100.953 150.428 1.00 28.66 ?  273 PHE D CG    1 
ATOM   15594 C  CD1   . PHE D 2 294 ? 140.978 100.567 151.503 1.00 30.23 ?  273 PHE D CD1   1 
ATOM   15595 C  CD2   . PHE D 2 294 ? 142.341 99.970  149.625 1.00 26.94 ?  273 PHE D CD2   1 
ATOM   15596 C  CE1   . PHE D 2 294 ? 140.733 99.214  151.765 1.00 31.04 ?  273 PHE D CE1   1 
ATOM   15597 C  CE2   . PHE D 2 294 ? 142.112 98.624  149.876 1.00 27.39 ?  273 PHE D CE2   1 
ATOM   15598 C  CZ    . PHE D 2 294 ? 141.312 98.238  150.944 1.00 29.80 ?  273 PHE D CZ    1 
ATOM   15599 N  N     . ASP D 2 295 ? 141.811 105.295 151.300 1.00 29.60 ?  274 ASP D N     1 
ATOM   15600 C  CA    . ASP D 2 295 ? 142.326 106.662 151.334 1.00 30.40 ?  274 ASP D CA    1 
ATOM   15601 C  C     . ASP D 2 295 ? 143.584 106.816 150.457 1.00 29.58 ?  274 ASP D C     1 
ATOM   15602 O  O     . ASP D 2 295 ? 144.328 105.854 150.265 1.00 28.68 ?  274 ASP D O     1 
ATOM   15603 C  CB    . ASP D 2 295 ? 142.646 107.086 152.773 1.00 31.44 ?  274 ASP D CB    1 
ATOM   15604 C  CG    . ASP D 2 295 ? 141.409 107.171 153.660 1.00 34.27 ?  274 ASP D CG    1 
ATOM   15605 O  OD1   . ASP D 2 295 ? 140.297 107.441 153.145 1.00 36.43 ?  274 ASP D OD1   1 
ATOM   15606 O  OD2   . ASP D 2 295 ? 141.561 106.969 154.884 1.00 38.03 -1 274 ASP D OD2   1 
ATOM   15607 N  N     . PRO D 2 296 ? 143.828 108.034 149.936 1.00 29.59 ?  275 PRO D N     1 
ATOM   15608 C  CA    . PRO D 2 296 ? 145.065 108.241 149.178 1.00 29.09 ?  275 PRO D CA    1 
ATOM   15609 C  C     . PRO D 2 296 ? 146.291 108.014 150.063 1.00 29.26 ?  275 PRO D C     1 
ATOM   15610 O  O     . PRO D 2 296 ? 146.261 108.313 151.257 1.00 29.36 ?  275 PRO D O     1 
ATOM   15611 C  CB    . PRO D 2 296 ? 144.983 109.710 148.742 1.00 29.49 ?  275 PRO D CB    1 
ATOM   15612 C  CG    . PRO D 2 296 ? 143.963 110.344 149.650 1.00 30.28 ?  275 PRO D CG    1 
ATOM   15613 C  CD    . PRO D 2 296 ? 143.001 109.254 150.005 1.00 29.63 ?  275 PRO D CD    1 
ATOM   15614 N  N     . TYR D 2 297 ? 147.348 107.468 149.481 1.00 28.97 ?  276 TYR D N     1 
ATOM   15615 C  CA    . TYR D 2 297 ? 148.562 107.157 150.226 1.00 29.63 ?  276 TYR D CA    1 
ATOM   15616 C  C     . TYR D 2 297 ? 149.577 108.309 150.151 1.00 29.55 ?  276 TYR D C     1 
ATOM   15617 O  O     . TYR D 2 297 ? 150.318 108.573 151.107 1.00 30.12 ?  276 TYR D O     1 
ATOM   15618 C  CB    . TYR D 2 297 ? 149.176 105.881 149.651 1.00 29.49 ?  276 TYR D CB    1 
ATOM   15619 C  CG    . TYR D 2 297 ? 150.250 105.245 150.493 1.00 31.19 ?  276 TYR D CG    1 
ATOM   15620 C  CD1   . TYR D 2 297 ? 149.961 104.760 151.773 1.00 31.93 ?  276 TYR D CD1   1 
ATOM   15621 C  CD2   . TYR D 2 297 ? 151.550 105.100 150.006 1.00 31.98 ?  276 TYR D CD2   1 
ATOM   15622 C  CE1   . TYR D 2 297 ? 150.942 104.163 152.554 1.00 33.86 ?  276 TYR D CE1   1 
ATOM   15623 C  CE2   . TYR D 2 297 ? 152.542 104.497 150.781 1.00 33.88 ?  276 TYR D CE2   1 
ATOM   15624 C  CZ    . TYR D 2 297 ? 152.222 104.029 152.050 1.00 34.42 ?  276 TYR D CZ    1 
ATOM   15625 O  OH    . TYR D 2 297 ? 153.184 103.440 152.831 1.00 37.63 ?  276 TYR D OH    1 
ATOM   15626 N  N     . PHE D 2 298 ? 149.596 108.978 149.004 1.00 29.10 ?  277 PHE D N     1 
ATOM   15627 C  CA    . PHE D 2 298 ? 150.581 110.008 148.691 1.00 28.97 ?  277 PHE D CA    1 
ATOM   15628 C  C     . PHE D 2 298 ? 149.956 111.406 148.772 1.00 29.77 ?  277 PHE D C     1 
ATOM   15629 O  O     . PHE D 2 298 ? 148.768 111.579 148.489 1.00 29.07 ?  277 PHE D O     1 
ATOM   15630 C  CB    . PHE D 2 298 ? 151.146 109.782 147.284 1.00 27.99 ?  277 PHE D CB    1 
ATOM   15631 C  CG    . PHE D 2 298 ? 151.855 108.460 147.108 1.00 27.61 ?  277 PHE D CG    1 
ATOM   15632 C  CD1   . PHE D 2 298 ? 151.279 107.440 146.363 1.00 25.91 ?  277 PHE D CD1   1 
ATOM   15633 C  CD2   . PHE D 2 298 ? 153.112 108.247 147.676 1.00 27.32 ?  277 PHE D CD2   1 
ATOM   15634 C  CE1   . PHE D 2 298 ? 151.933 106.232 146.194 1.00 26.65 ?  277 PHE D CE1   1 
ATOM   15635 C  CE2   . PHE D 2 298 ? 153.778 107.046 147.515 1.00 25.38 ?  277 PHE D CE2   1 
ATOM   15636 C  CZ    . PHE D 2 298 ? 153.191 106.031 146.783 1.00 26.20 ?  277 PHE D CZ    1 
ATOM   15637 N  N     . GLU D 2 299 ? 150.765 112.389 149.166 1.00 31.10 ?  278 GLU D N     1 
ATOM   15638 C  CA    . GLU D 2 299 ? 150.345 113.793 149.163 1.00 32.86 ?  278 GLU D CA    1 
ATOM   15639 C  C     . GLU D 2 299 ? 150.000 114.231 147.734 1.00 33.04 ?  278 GLU D C     1 
ATOM   15640 O  O     . GLU D 2 299 ? 150.559 113.712 146.764 1.00 32.23 ?  278 GLU D O     1 
ATOM   15641 C  CB    . GLU D 2 299 ? 151.443 114.692 149.758 1.00 33.45 ?  278 GLU D CB    1 
ATOM   15642 C  CG    . GLU D 2 299 ? 152.758 114.665 148.964 1.00 36.27 ?  278 GLU D CG    1 
ATOM   15643 C  CD    . GLU D 2 299 ? 153.813 115.648 149.451 1.00 40.47 ?  278 GLU D CD    1 
ATOM   15644 O  OE1   . GLU D 2 299 ? 153.982 115.815 150.681 1.00 41.72 ?  278 GLU D OE1   1 
ATOM   15645 O  OE2   . GLU D 2 299 ? 154.496 116.233 148.583 1.00 42.65 -1 278 GLU D OE2   1 
ATOM   15646 N  N     . GLU D 2 300 ? 149.073 115.180 147.623 1.00 34.09 ?  279 GLU D N     1 
ATOM   15647 C  CA    . GLU D 2 300 ? 148.651 115.725 146.340 1.00 35.06 ?  279 GLU D CA    1 
ATOM   15648 C  C     . GLU D 2 300 ? 149.796 116.506 145.692 1.00 34.97 ?  279 GLU D C     1 
ATOM   15649 O  O     . GLU D 2 300 ? 150.483 117.285 146.355 1.00 34.96 ?  279 GLU D O     1 
ATOM   15650 C  CB    . GLU D 2 300 ? 147.413 116.621 146.526 1.00 35.81 ?  279 GLU D CB    1 
ATOM   15651 C  CG    . GLU D 2 300 ? 146.773 117.092 145.218 1.00 38.58 ?  279 GLU D CG    1 
ATOM   15652 C  CD    . GLU D 2 300 ? 145.294 117.443 145.365 1.00 43.09 ?  279 GLU D CD    1 
ATOM   15653 O  OE1   . GLU D 2 300 ? 144.470 116.854 144.629 1.00 44.69 ?  279 GLU D OE1   1 
ATOM   15654 O  OE2   . GLU D 2 300 ? 144.955 118.296 146.217 1.00 44.94 -1 279 GLU D OE2   1 
ATOM   15655 N  N     . GLU D 2 301 ? 150.003 116.263 144.402 1.00 34.73 ?  280 GLU D N     1 
ATOM   15656 C  CA    . GLU D 2 301 ? 151.029 116.948 143.626 1.00 35.16 ?  280 GLU D CA    1 
ATOM   15657 C  C     . GLU D 2 301 ? 150.421 117.428 142.319 1.00 35.23 ?  280 GLU D C     1 
ATOM   15658 O  O     . GLU D 2 301 ? 149.462 116.833 141.816 1.00 34.92 ?  280 GLU D O     1 
ATOM   15659 C  CB    . GLU D 2 301 ? 152.199 116.001 143.325 1.00 35.10 ?  280 GLU D CB    1 
ATOM   15660 C  CG    . GLU D 2 301 ? 153.198 115.830 144.467 1.00 36.62 ?  280 GLU D CG    1 
ATOM   15661 C  CD    . GLU D 2 301 ? 154.182 114.685 144.229 1.00 37.59 ?  280 GLU D CD    1 
ATOM   15662 O  OE1   . GLU D 2 301 ? 153.737 113.535 144.030 1.00 38.10 ?  280 GLU D OE1   1 
ATOM   15663 O  OE2   . GLU D 2 301 ? 155.404 114.928 144.266 1.00 38.93 -1 280 GLU D OE2   1 
ATOM   15664 N  N     . ASP D 2 302 ? 150.974 118.500 141.765 1.00 35.60 ?  281 ASP D N     1 
ATOM   15665 C  CA    . ASP D 2 302 ? 150.541 118.964 140.453 1.00 35.96 ?  281 ASP D CA    1 
ATOM   15666 C  C     . ASP D 2 302 ? 151.212 118.103 139.390 1.00 35.01 ?  281 ASP D C     1 
ATOM   15667 O  O     . ASP D 2 302 ? 152.287 117.553 139.625 1.00 35.52 ?  281 ASP D O     1 
ATOM   15668 C  CB    . ASP D 2 302 ? 150.836 120.463 140.263 1.00 36.82 ?  281 ASP D CB    1 
ATOM   15669 C  CG    . ASP D 2 302 ? 152.338 120.800 140.290 1.00 39.01 ?  281 ASP D CG    1 
ATOM   15670 O  OD1   . ASP D 2 302 ? 153.160 120.019 140.832 1.00 40.83 ?  281 ASP D OD1   1 
ATOM   15671 O  OD2   . ASP D 2 302 ? 152.691 121.882 139.778 1.00 41.13 -1 281 ASP D OD2   1 
ATOM   15672 N  N     . ILE D 2 303 ? 150.567 117.950 138.241 1.00 33.94 ?  282 ILE D N     1 
ATOM   15673 C  CA    . ILE D 2 303 ? 151.122 117.130 137.167 1.00 33.00 ?  282 ILE D CA    1 
ATOM   15674 C  C     . ILE D 2 303 ? 151.670 117.981 136.014 1.00 31.59 ?  282 ILE D C     1 
ATOM   15675 O  O     . ILE D 2 303 ? 151.202 119.097 135.781 1.00 31.14 ?  282 ILE D O     1 
ATOM   15676 C  CB    . ILE D 2 303 ? 150.102 116.047 136.691 1.00 33.44 ?  282 ILE D CB    1 
ATOM   15677 C  CG1   . ILE D 2 303 ? 150.286 115.695 135.210 1.00 34.29 ?  282 ILE D CG1   1 
ATOM   15678 C  CG2   . ILE D 2 303 ? 148.676 116.486 136.983 1.00 35.47 ?  282 ILE D CG2   1 
ATOM   15679 C  CD1   . ILE D 2 303 ? 149.201 114.803 134.642 1.00 36.30 ?  282 ILE D CD1   1 
ATOM   15680 N  N     . ASN D 2 304 ? 152.679 117.455 135.319 1.00 29.53 ?  283 ASN D N     1 
ATOM   15681 C  CA    . ASN D 2 304 ? 153.238 118.112 134.141 1.00 28.49 ?  283 ASN D CA    1 
ATOM   15682 C  C     . ASN D 2 304 ? 152.128 118.617 133.194 1.00 27.87 ?  283 ASN D C     1 
ATOM   15683 O  O     . ASN D 2 304 ? 151.272 117.838 132.776 1.00 27.02 ?  283 ASN D O     1 
ATOM   15684 C  CB    . ASN D 2 304 ? 154.177 117.155 133.404 1.00 28.20 ?  283 ASN D CB    1 
ATOM   15685 C  CG    . ASN D 2 304 ? 154.857 117.808 132.230 1.00 28.17 ?  283 ASN D CG    1 
ATOM   15686 O  OD1   . ASN D 2 304 ? 154.305 117.856 131.136 1.00 29.01 ?  283 ASN D OD1   1 
ATOM   15687 N  ND2   . ASN D 2 304 ? 156.061 118.314 132.447 1.00 27.24 ?  283 ASN D ND2   1 
ATOM   15688 N  N     . PRO D 2 305 ? 152.133 119.926 132.868 1.00 28.00 ?  284 PRO D N     1 
ATOM   15689 C  CA    . PRO D 2 305 ? 151.043 120.508 132.068 1.00 27.58 ?  284 PRO D CA    1 
ATOM   15690 C  C     . PRO D 2 305 ? 150.961 119.991 130.630 1.00 27.01 ?  284 PRO D C     1 
ATOM   15691 O  O     . PRO D 2 305 ? 149.890 120.024 130.033 1.00 26.66 ?  284 PRO D O     1 
ATOM   15692 C  CB    . PRO D 2 305 ? 151.351 122.011 132.078 1.00 28.21 ?  284 PRO D CB    1 
ATOM   15693 C  CG    . PRO D 2 305 ? 152.770 122.125 132.425 1.00 28.80 ?  284 PRO D CG    1 
ATOM   15694 C  CD    . PRO D 2 305 ? 153.061 120.965 133.351 1.00 28.11 ?  284 PRO D CD    1 
ATOM   15695 N  N     . ILE D 2 306 ? 152.076 119.515 130.085 1.00 26.52 ?  285 ILE D N     1 
ATOM   15696 C  CA    . ILE D 2 306 ? 152.076 118.949 128.741 1.00 26.50 ?  285 ILE D CA    1 
ATOM   15697 C  C     . ILE D 2 306 ? 151.319 117.614 128.735 1.00 26.43 ?  285 ILE D C     1 
ATOM   15698 O  O     . ILE D 2 306 ? 150.442 117.378 127.891 1.00 26.00 ?  285 ILE D O     1 
ATOM   15699 C  CB    . ILE D 2 306 ? 153.510 118.814 128.171 1.00 26.88 ?  285 ILE D CB    1 
ATOM   15700 C  CG1   . ILE D 2 306 ? 154.173 120.202 128.096 1.00 26.98 ?  285 ILE D CG1   1 
ATOM   15701 C  CG2   . ILE D 2 306 ? 153.467 118.128 126.806 1.00 24.94 ?  285 ILE D CG2   1 
ATOM   15702 C  CD1   . ILE D 2 306 ? 155.634 120.193 127.737 1.00 26.65 ?  285 ILE D CD1   1 
ATOM   15703 N  N     . VAL D 2 307 ? 151.640 116.763 129.704 1.00 26.36 ?  286 VAL D N     1 
ATOM   15704 C  CA    . VAL D 2 307 ? 150.894 115.531 129.923 1.00 26.71 ?  286 VAL D CA    1 
ATOM   15705 C  C     . VAL D 2 307 ? 149.418 115.810 130.229 1.00 27.68 ?  286 VAL D C     1 
ATOM   15706 O  O     . VAL D 2 307 ? 148.548 115.124 129.692 1.00 27.92 ?  286 VAL D O     1 
ATOM   15707 C  CB    . VAL D 2 307 ? 151.565 114.638 131.001 1.00 26.37 ?  286 VAL D CB    1 
ATOM   15708 C  CG1   . VAL D 2 307 ? 150.656 113.468 131.413 1.00 25.48 ?  286 VAL D CG1   1 
ATOM   15709 C  CG2   . VAL D 2 307 ? 152.855 114.110 130.461 1.00 25.55 ?  286 VAL D CG2   1 
ATOM   15710 N  N     . LEU D 2 308 ? 149.130 116.827 131.045 1.00 28.80 ?  287 LEU D N     1 
ATOM   15711 C  CA    . LEU D 2 308 ? 147.732 117.227 131.279 1.00 30.07 ?  287 LEU D CA    1 
ATOM   15712 C  C     . LEU D 2 308 ? 147.006 117.611 129.985 1.00 30.38 ?  287 LEU D C     1 
ATOM   15713 O  O     . LEU D 2 308 ? 145.845 117.242 129.778 1.00 30.71 ?  287 LEU D O     1 
ATOM   15714 C  CB    . LEU D 2 308 ? 147.634 118.368 132.296 1.00 30.86 ?  287 LEU D CB    1 
ATOM   15715 C  CG    . LEU D 2 308 ? 147.639 117.950 133.770 1.00 32.62 ?  287 LEU D CG    1 
ATOM   15716 C  CD1   . LEU D 2 308 ? 147.746 119.162 134.670 1.00 33.97 ?  287 LEU D CD1   1 
ATOM   15717 C  CD2   . LEU D 2 308 ? 146.394 117.116 134.125 1.00 34.73 ?  287 LEU D CD2   1 
ATOM   15718 N  N     . ASN D 2 309 ? 147.691 118.341 129.112 1.00 30.81 ?  288 ASN D N     1 
ATOM   15719 C  CA    . ASN D 2 309 ? 147.109 118.718 127.828 1.00 31.25 ?  288 ASN D CA    1 
ATOM   15720 C  C     . ASN D 2 309 ? 146.835 117.495 126.951 1.00 31.83 ?  288 ASN D C     1 
ATOM   15721 O  O     . ASN D 2 309 ? 145.856 117.469 126.199 1.00 31.73 ?  288 ASN D O     1 
ATOM   15722 C  CB    . ASN D 2 309 ? 147.981 119.742 127.094 1.00 31.21 ?  288 ASN D CB    1 
ATOM   15723 C  CG    . ASN D 2 309 ? 147.299 120.296 125.853 1.00 31.41 ?  288 ASN D CG    1 
ATOM   15724 O  OD1   . ASN D 2 309 ? 146.111 120.635 125.885 1.00 31.88 ?  288 ASN D OD1   1 
ATOM   15725 N  ND2   . ASN D 2 309 ? 148.041 120.384 124.754 1.00 29.12 ?  288 ASN D ND2   1 
ATOM   15726 N  N     . GLY D 2 310 ? 147.700 116.486 127.061 1.00 32.04 ?  289 GLY D N     1 
ATOM   15727 C  CA    . GLY D 2 310 ? 147.484 115.201 126.407 1.00 33.04 ?  289 GLY D CA    1 
ATOM   15728 C  C     . GLY D 2 310 ? 146.266 114.484 126.976 1.00 33.85 ?  289 GLY D C     1 
ATOM   15729 O  O     . GLY D 2 310 ? 145.420 114.003 126.222 1.00 34.05 ?  289 GLY D O     1 
ATOM   15730 N  N     . LEU D 2 311 ? 146.180 114.419 128.304 1.00 34.33 ?  290 LEU D N     1 
ATOM   15731 C  CA    . LEU D 2 311 ? 145.080 113.745 128.998 1.00 35.77 ?  290 LEU D CA    1 
ATOM   15732 C  C     . LEU D 2 311 ? 143.715 114.362 128.711 1.00 37.01 ?  290 LEU D C     1 
ATOM   15733 O  O     . LEU D 2 311 ? 142.728 113.645 128.540 1.00 37.18 ?  290 LEU D O     1 
ATOM   15734 C  CB    . LEU D 2 311 ? 145.311 113.757 130.515 1.00 35.50 ?  290 LEU D CB    1 
ATOM   15735 C  CG    . LEU D 2 311 ? 146.061 112.631 131.220 1.00 35.45 ?  290 LEU D CG    1 
ATOM   15736 C  CD1   . LEU D 2 311 ? 146.294 113.022 132.688 1.00 35.28 ?  290 LEU D CD1   1 
ATOM   15737 C  CD2   . LEU D 2 311 ? 145.320 111.295 131.133 1.00 34.16 ?  290 LEU D CD2   1 
ATOM   15738 N  N     . LYS D 2 330 ? 119.508 116.444 148.715 1.00 42.55 ?  309 LYS D N     1 
ATOM   15739 C  CA    . LYS D 2 330 ? 118.108 116.223 148.376 1.00 44.90 ?  309 LYS D CA    1 
ATOM   15740 C  C     . LYS D 2 330 ? 117.288 115.811 149.593 1.00 43.76 ?  309 LYS D C     1 
ATOM   15741 O  O     . LYS D 2 330 ? 117.176 114.627 149.907 1.00 44.28 ?  309 LYS D O     1 
ATOM   15742 C  CB    . LYS D 2 330 ? 117.983 115.158 147.283 1.00 40.63 ?  309 LYS D CB    1 
ATOM   15743 C  CG    . LYS D 2 330 ? 116.612 115.099 146.627 1.00 43.98 ?  309 LYS D CG    1 
ATOM   15744 C  CD    . LYS D 2 330 ? 116.268 116.400 145.921 1.00 43.19 ?  309 LYS D CD    1 
ATOM   15745 C  CE    . LYS D 2 330 ? 116.268 116.224 144.412 1.00 45.38 ?  309 LYS D CE    1 
ATOM   15746 N  NZ    . LYS D 2 330 ? 116.230 117.530 143.699 1.00 43.90 1  309 LYS D NZ    1 
ATOM   15747 N  N     . ALA D 2 331 ? 116.719 116.798 150.280 1.00 41.98 ?  310 ALA D N     1 
ATOM   15748 C  CA    . ALA D 2 331 ? 115.824 116.521 151.389 1.00 42.36 ?  310 ALA D CA    1 
ATOM   15749 C  C     . ALA D 2 331 ? 114.494 115.981 150.871 1.00 42.70 ?  310 ALA D C     1 
ATOM   15750 O  O     . ALA D 2 331 ? 114.111 116.199 149.719 1.00 44.14 ?  310 ALA D O     1 
ATOM   15751 C  CB    . ALA D 2 331 ? 115.593 117.776 152.230 1.00 39.32 ?  310 ALA D CB    1 
ATOM   15752 N  N     . THR D 2 332 ? 113.790 115.265 151.742 1.00 33.29 ?  311 THR D N     1 
ATOM   15753 C  CA    . THR D 2 332 ? 112.529 114.626 151.374 1.00 32.46 ?  311 THR D CA    1 
ATOM   15754 C  C     . THR D 2 332 ? 111.499 115.706 151.074 1.00 32.78 ?  311 THR D C     1 
ATOM   15755 O  O     . THR D 2 332 ? 111.198 116.550 151.920 1.00 35.85 ?  311 THR D O     1 
ATOM   15756 C  CB    . THR D 2 332 ? 112.051 113.703 152.489 1.00 36.71 ?  311 THR D CB    1 
ATOM   15757 O  OG1   . THR D 2 332 ? 112.752 112.456 152.411 1.00 39.19 ?  311 THR D OG1   1 
ATOM   15758 C  CG2   . THR D 2 332 ? 110.558 113.434 152.357 1.00 34.82 ?  311 THR D CG2   1 
ATOM   15759 N  N     . VAL D 2 333 ? 110.962 115.693 149.856 1.00 30.31 ?  312 VAL D N     1 
ATOM   15760 C  CA    . VAL D 2 333 ? 109.943 116.655 149.457 1.00 24.24 ?  312 VAL D CA    1 
ATOM   15761 C  C     . VAL D 2 333 ? 108.606 116.231 150.048 1.00 30.13 ?  312 VAL D C     1 
ATOM   15762 O  O     . VAL D 2 333 ? 108.077 115.166 149.713 1.00 35.56 ?  312 VAL D O     1 
ATOM   15763 C  CB    . VAL D 2 333 ? 109.858 116.781 147.926 1.00 29.05 ?  312 VAL D CB    1 
ATOM   15764 C  CG1   . VAL D 2 333 ? 108.894 117.890 147.540 1.00 31.60 ?  312 VAL D CG1   1 
ATOM   15765 C  CG2   . VAL D 2 333 ? 111.237 117.033 147.338 1.00 29.59 ?  312 VAL D CG2   1 
ATOM   15766 N  N     . GLU D 2 334 ? 108.054 117.059 150.929 1.00 28.79 ?  313 GLU D N     1 
ATOM   15767 C  CA    . GLU D 2 334 ? 106.770 116.786 151.559 1.00 29.66 ?  313 GLU D CA    1 
ATOM   15768 C  C     . GLU D 2 334 ? 105.837 117.959 151.295 1.00 31.26 ?  313 GLU D C     1 
ATOM   15769 O  O     . GLU D 2 334 ? 106.176 119.103 151.643 1.00 34.83 ?  313 GLU D O     1 
ATOM   15770 C  CB    . GLU D 2 334 ? 106.936 116.551 153.062 1.00 29.26 ?  313 GLU D CB    1 
ATOM   15771 C  CG    . GLU D 2 334 ? 105.640 116.581 153.848 1.00 33.58 ?  313 GLU D CG    1 
ATOM   15772 C  CD    . GLU D 2 334 ? 105.830 116.169 155.295 1.00 35.28 ?  313 GLU D CD    1 
ATOM   15773 O  OE1   . GLU D 2 334 ? 106.917 116.432 155.850 1.00 33.47 ?  313 GLU D OE1   1 
ATOM   15774 O  OE2   . GLU D 2 334 ? 104.894 115.581 155.877 1.00 31.19 -1 313 GLU D OE2   1 
ATOM   15775 N  N     . PRO D 2 335 ? 104.675 117.739 150.681 1.00 31.21 ?  314 PRO D N     1 
ATOM   15776 C  CA    . PRO D 2 335 ? 103.806 118.862 150.315 1.00 33.35 ?  314 PRO D CA    1 
ATOM   15777 C  C     . PRO D 2 335 ? 103.283 119.598 151.540 1.00 33.18 ?  314 PRO D C     1 
ATOM   15778 O  O     . PRO D 2 335 ? 103.106 119.016 152.612 1.00 33.38 ?  314 PRO D O     1 
ATOM   15779 C  CB    . PRO D 2 335 ? 102.669 118.189 149.538 1.00 30.11 ?  314 PRO D CB    1 
ATOM   15780 C  CG    . PRO D 2 335 ? 102.698 116.760 149.985 1.00 31.03 ?  314 PRO D CG    1 
ATOM   15781 C  CD    . PRO D 2 335 ? 104.142 116.452 150.207 1.00 33.22 ?  314 PRO D CD    1 
ATOM   15782 N  N     . LEU D 2 336 ? 103.041 120.895 151.371 1.00 30.38 ?  315 LEU D N     1 
ATOM   15783 C  CA    . LEU D 2 336 ? 102.415 121.687 152.418 1.00 26.61 ?  315 LEU D CA    1 
ATOM   15784 C  C     . LEU D 2 336 ? 100.963 121.260 152.590 1.00 27.64 ?  315 LEU D C     1 
ATOM   15785 O  O     . LEU D 2 336 ? 100.192 121.200 151.629 1.00 34.77 ?  315 LEU D O     1 
ATOM   15786 C  CB    . LEU D 2 336 ? 102.497 123.176 152.084 1.00 22.39 ?  315 LEU D CB    1 
ATOM   15787 C  CG    . LEU D 2 336 ? 103.803 123.876 152.465 1.00 25.97 ?  315 LEU D CG    1 
ATOM   15788 C  CD1   . LEU D 2 336 ? 103.806 125.314 151.976 1.00 19.59 ?  315 LEU D CD1   1 
ATOM   15789 C  CD2   . LEU D 2 336 ? 104.036 123.816 153.967 1.00 27.01 ?  315 LEU D CD2   1 
ATOM   15790 N  N     . LYS D 2 337 ? 100.595 120.963 153.836 1.00 28.30 ?  316 LYS D N     1 
ATOM   15791 C  CA    . LYS D 2 337 ? 99.308  120.349 154.145 1.00 36.46 ?  316 LYS D CA    1 
ATOM   15792 C  C     . LYS D 2 337 ? 98.264  121.353 154.611 1.00 36.32 ?  316 LYS D C     1 
ATOM   15793 O  O     . LYS D 2 337 ? 97.216  120.939 155.121 1.00 40.02 ?  316 LYS D O     1 
ATOM   15794 C  CB    . LYS D 2 337 ? 99.482  119.266 155.212 1.00 33.57 ?  316 LYS D CB    1 
ATOM   15795 C  CG    . LYS D 2 337 ? 100.673 118.355 154.989 1.00 36.47 ?  316 LYS D CG    1 
ATOM   15796 C  CD    . LYS D 2 337 ? 100.294 116.900 155.194 1.00 38.79 ?  316 LYS D CD    1 
ATOM   15797 C  CE    . LYS D 2 337 ? 101.527 116.022 155.277 1.00 37.56 ?  316 LYS D CE    1 
ATOM   15798 N  NZ    . LYS D 2 337 ? 102.376 116.164 154.064 1.00 36.72 1  316 LYS D NZ    1 
ATOM   15799 N  N     . ASP D 2 338 ? 98.530  122.655 154.469 1.00 24.38 ?  317 ASP D N     1 
ATOM   15800 C  CA    . ASP D 2 338 ? 97.701  123.717 155.037 1.00 29.04 ?  317 ASP D CA    1 
ATOM   15801 C  C     . ASP D 2 338 ? 97.734  123.636 156.560 1.00 28.87 ?  317 ASP D C     1 
ATOM   15802 O  O     . ASP D 2 338 ? 98.190  122.636 157.123 1.00 33.66 ?  317 ASP D O     1 
ATOM   15803 C  CB    . ASP D 2 338 ? 96.265  123.654 154.505 1.00 31.69 ?  317 ASP D CB    1 
ATOM   15804 C  CG    . ASP D 2 338 ? 95.476  124.912 154.804 1.00 32.42 ?  317 ASP D CG    1 
ATOM   15805 O  OD1   . ASP D 2 338 ? 96.104  125.961 155.056 1.00 34.34 ?  317 ASP D OD1   1 
ATOM   15806 O  OD2   . ASP D 2 338 ? 94.229  124.853 154.786 1.00 28.35 -1 317 ASP D OD2   1 
ATOM   15807 N  N     . ASP D 2 339 ? 97.301  124.706 157.230 1.00 22.82 ?  318 ASP D N     1 
ATOM   15808 C  CA    . ASP D 2 339 ? 97.429  124.862 158.678 1.00 24.73 ?  318 ASP D CA    1 
ATOM   15809 C  C     . ASP D 2 339 ? 98.899  124.980 159.066 1.00 24.49 ?  318 ASP D C     1 
ATOM   15810 O  O     . ASP D 2 339 ? 99.228  125.140 160.246 1.00 31.22 ?  318 ASP D O     1 
ATOM   15811 C  CB    . ASP D 2 339 ? 96.751  123.711 159.431 1.00 23.30 ?  318 ASP D CB    1 
ATOM   15812 C  CG    . ASP D 2 339 ? 95.380  123.381 158.876 1.00 31.35 ?  318 ASP D CG    1 
ATOM   15813 O  OD1   . ASP D 2 339 ? 94.487  124.254 158.935 1.00 29.84 ?  318 ASP D OD1   1 
ATOM   15814 O  OD2   . ASP D 2 339 ? 95.193  122.251 158.377 1.00 30.37 -1 318 ASP D OD2   1 
ATOM   15815 N  N     . ASP D 2 340 ? 99.787  124.897 158.077 1.00 24.54 ?  319 ASP D N     1 
ATOM   15816 C  CA    . ASP D 2 340 ? 101.178 125.295 158.216 1.00 16.40 ?  319 ASP D CA    1 
ATOM   15817 C  C     . ASP D 2 340 ? 101.354 126.786 157.989 1.00 13.50 ?  319 ASP D C     1 
ATOM   15818 O  O     . ASP D 2 340 ? 102.446 127.318 158.212 1.00 33.12 ?  319 ASP D O     1 
ATOM   15819 C  CB    . ASP D 2 340 ? 102.052 124.513 157.234 1.00 15.31 ?  319 ASP D CB    1 
ATOM   15820 C  CG    . ASP D 2 340 ? 102.140 123.039 157.575 1.00 20.12 ?  319 ASP D CG    1 
ATOM   15821 O  OD1   . ASP D 2 340 ? 102.059 122.698 158.774 1.00 32.00 ?  319 ASP D OD1   1 
ATOM   15822 O  OD2   . ASP D 2 340 ? 102.289 122.222 156.644 1.00 22.25 -1 319 ASP D OD2   1 
ATOM   15823 N  N     . PHE D 2 341 ? 100.294 127.465 157.547 1.00 10.33 ?  320 PHE D N     1 
ATOM   15824 C  CA    . PHE D 2 341 ? 100.289 128.906 157.350 1.00 15.27 ?  320 PHE D CA    1 
ATOM   15825 C  C     . PHE D 2 341 ? 99.678  129.630 158.541 1.00 19.34 ?  320 PHE D C     1 
ATOM   15826 O  O     . PHE D 2 341 ? 99.585  130.863 158.523 1.00 16.81 ?  320 PHE D O     1 
ATOM   15827 C  CB    . PHE D 2 341 ? 99.514  129.265 156.078 1.00 19.36 ?  320 PHE D CB    1 
ATOM   15828 C  CG    . PHE D 2 341 ? 100.137 128.743 154.818 1.00 13.21 ?  320 PHE D CG    1 
ATOM   15829 C  CD1   . PHE D 2 341 ? 101.051 129.504 154.111 1.00 12.45 ?  320 PHE D CD1   1 
ATOM   15830 C  CD2   . PHE D 2 341 ? 99.808  127.486 154.340 1.00 11.41 ?  320 PHE D CD2   1 
ATOM   15831 C  CE1   . PHE D 2 341 ? 101.621 129.022 152.949 1.00 11.53 ?  320 PHE D CE1   1 
ATOM   15832 C  CE2   . PHE D 2 341 ? 100.378 127.000 153.182 1.00 15.13 ?  320 PHE D CE2   1 
ATOM   15833 C  CZ    . PHE D 2 341 ? 101.285 127.769 152.486 1.00 8.25  ?  320 PHE D CZ    1 
ATOM   15834 N  N     . TYR D 2 342 ? 99.257  128.898 159.568 1.00 12.30 ?  321 TYR D N     1 
ATOM   15835 C  CA    . TYR D 2 342 ? 98.581  129.463 160.723 1.00 16.33 ?  321 TYR D CA    1 
ATOM   15836 C  C     . TYR D 2 342 ? 99.321  129.047 161.983 1.00 22.82 ?  321 TYR D C     1 
ATOM   15837 O  O     . TYR D 2 342 ? 99.817  127.920 162.078 1.00 19.28 ?  321 TYR D O     1 
ATOM   15838 C  CB    . TYR D 2 342 ? 97.121  129.002 160.789 1.00 12.46 ?  321 TYR D CB    1 
ATOM   15839 C  CG    . TYR D 2 342 ? 96.313  129.390 159.572 1.00 15.87 ?  321 TYR D CG    1 
ATOM   15840 C  CD1   . TYR D 2 342 ? 95.731  130.645 159.471 1.00 18.56 ?  321 TYR D CD1   1 
ATOM   15841 C  CD2   . TYR D 2 342 ? 96.140  128.500 158.520 1.00 15.63 ?  321 TYR D CD2   1 
ATOM   15842 C  CE1   . TYR D 2 342 ? 94.995  131.003 158.358 1.00 14.14 ?  321 TYR D CE1   1 
ATOM   15843 C  CE2   . TYR D 2 342 ? 95.406  128.849 157.403 1.00 15.01 ?  321 TYR D CE2   1 
ATOM   15844 C  CZ    . TYR D 2 342 ? 94.836  130.101 157.328 1.00 17.53 ?  321 TYR D CZ    1 
ATOM   15845 O  OH    . TYR D 2 342 ? 94.103  130.453 156.218 1.00 21.36 ?  321 TYR D OH    1 
ATOM   15846 N  N     . PHE D 2 343 ? 99.401  129.962 162.943 1.00 12.45 ?  322 PHE D N     1 
ATOM   15847 C  CA    . PHE D 2 343 ? 100.182 129.731 164.150 1.00 16.01 ?  322 PHE D CA    1 
ATOM   15848 C  C     . PHE D 2 343 ? 99.451  130.249 165.384 1.00 27.60 ?  322 PHE D C     1 
ATOM   15849 O  O     . PHE D 2 343 ? 98.622  131.154 165.295 1.00 22.19 ?  322 PHE D O     1 
ATOM   15850 C  CB    . PHE D 2 343 ? 101.555 130.396 164.025 1.00 18.28 ?  322 PHE D CB    1 
ATOM   15851 C  CG    . PHE D 2 343 ? 102.249 130.108 162.723 1.00 19.26 ?  322 PHE D CG    1 
ATOM   15852 C  CD1   . PHE D 2 343 ? 103.026 128.974 162.571 1.00 20.02 ?  322 PHE D CD1   1 
ATOM   15853 C  CD2   . PHE D 2 343 ? 102.109 130.967 161.645 1.00 13.80 ?  322 PHE D CD2   1 
ATOM   15854 C  CE1   . PHE D 2 343 ? 103.656 128.705 161.372 1.00 12.20 ?  322 PHE D CE1   1 
ATOM   15855 C  CE2   . PHE D 2 343 ? 102.735 130.702 160.446 1.00 9.90  ?  322 PHE D CE2   1 
ATOM   15856 C  CZ    . PHE D 2 343 ? 103.509 129.570 160.309 1.00 11.36 ?  322 PHE D CZ    1 
HETATM 15857 P  PG    . ATP E 3 .   ? 103.709 141.268 83.326  1.00 68.91 ?  801 ATP A PG    1 
HETATM 15858 O  O1G   . ATP E 3 .   ? 102.454 141.660 82.620  1.00 61.99 ?  801 ATP A O1G   1 
HETATM 15859 O  O2G   . ATP E 3 .   ? 104.867 142.251 83.113  1.00 61.48 -1 801 ATP A O2G   1 
HETATM 15860 O  O3G   . ATP E 3 .   ? 103.522 141.033 84.828  1.00 57.91 ?  801 ATP A O3G   1 
HETATM 15861 P  PB    . ATP E 3 .   ? 105.410 139.309 81.824  1.00 68.42 ?  801 ATP A PB    1 
HETATM 15862 O  O1B   . ATP E 3 .   ? 105.210 139.699 80.413  1.00 59.48 -1 801 ATP A O1B   1 
HETATM 15863 O  O2B   . ATP E 3 .   ? 106.745 139.726 82.442  1.00 59.06 ?  801 ATP A O2B   1 
HETATM 15864 O  O3B   . ATP E 3 .   ? 104.258 139.873 82.766  1.00 62.04 ?  801 ATP A O3B   1 
HETATM 15865 P  PA    . ATP E 3 .   ? 105.481 136.699 83.219  1.00 63.87 ?  801 ATP A PA    1 
HETATM 15866 O  O1A   . ATP E 3 .   ? 106.669 135.853 82.984  1.00 60.02 -1 801 ATP A O1A   1 
HETATM 15867 O  O2A   . ATP E 3 .   ? 104.171 135.932 83.393  1.00 58.33 ?  801 ATP A O2A   1 
HETATM 15868 O  O3A   . ATP E 3 .   ? 105.262 137.738 82.033  1.00 62.45 ?  801 ATP A O3A   1 
HETATM 15869 O  "O5'" . ATP E 3 .   ? 105.681 137.630 84.477  1.00 59.78 ?  801 ATP A "O5'" 1 
HETATM 15870 C  "C5'" . ATP E 3 .   ? 104.633 137.806 85.453  1.00 58.13 ?  801 ATP A "C5'" 1 
HETATM 15871 C  "C4'" . ATP E 3 .   ? 105.161 138.647 86.588  1.00 59.51 ?  801 ATP A "C4'" 1 
HETATM 15872 O  "O4'" . ATP E 3 .   ? 105.723 137.787 87.605  1.00 62.13 ?  801 ATP A "O4'" 1 
HETATM 15873 C  "C3'" . ATP E 3 .   ? 106.278 139.616 86.213  1.00 57.82 ?  801 ATP A "C3'" 1 
HETATM 15874 O  "O3'" . ATP E 3 .   ? 105.750 140.871 85.801  1.00 58.51 ?  801 ATP A "O3'" 1 
HETATM 15875 C  "C2'" . ATP E 3 .   ? 107.057 139.739 87.523  1.00 58.31 ?  801 ATP A "C2'" 1 
HETATM 15876 O  "O2'" . ATP E 3 .   ? 106.447 140.663 88.415  1.00 58.66 ?  801 ATP A "O2'" 1 
HETATM 15877 C  "C1'" . ATP E 3 .   ? 106.954 138.313 88.068  1.00 58.50 ?  801 ATP A "C1'" 1 
HETATM 15878 N  N9    . ATP E 3 .   ? 108.027 137.428 87.628  1.00 58.48 ?  801 ATP A N9    1 
HETATM 15879 C  C8    . ATP E 3 .   ? 107.913 136.314 86.838  1.00 58.26 ?  801 ATP A C8    1 
HETATM 15880 N  N7    . ATP E 3 .   ? 109.049 135.707 86.601  1.00 56.05 ?  801 ATP A N7    1 
HETATM 15881 C  C5    . ATP E 3 .   ? 109.981 136.475 87.284  1.00 58.55 ?  801 ATP A C5    1 
HETATM 15882 C  C6    . ATP E 3 .   ? 111.376 136.366 87.434  1.00 56.46 ?  801 ATP A C6    1 
HETATM 15883 N  N6    . ATP E 3 .   ? 112.112 135.398 86.881  1.00 55.74 ?  801 ATP A N6    1 
HETATM 15884 N  N1    . ATP E 3 .   ? 112.001 137.300 88.184  1.00 57.23 ?  801 ATP A N1    1 
HETATM 15885 C  C2    . ATP E 3 .   ? 111.275 138.275 88.736  1.00 55.67 ?  801 ATP A C2    1 
HETATM 15886 N  N3    . ATP E 3 .   ? 109.958 138.478 88.666  1.00 57.17 ?  801 ATP A N3    1 
HETATM 15887 C  C4    . ATP E 3 .   ? 109.365 137.540 87.922  1.00 59.07 ?  801 ATP A C4    1 
HETATM 15888 P  PB    . GDP F 4 .   ? 100.651 154.513 86.856  1.00 70.96 ?  802 GDP A PB    1 
HETATM 15889 O  O1B   . GDP F 4 .   ? 101.837 153.884 86.167  1.00 59.03 ?  802 GDP A O1B   1 
HETATM 15890 O  O2B   . GDP F 4 .   ? 100.057 155.573 85.961  1.00 60.98 -1 802 GDP A O2B   1 
HETATM 15891 O  O3B   . GDP F 4 .   ? 99.612  153.455 87.145  1.00 60.51 ?  802 GDP A O3B   1 
HETATM 15892 O  O3A   . GDP F 4 .   ? 101.151 155.197 88.223  1.00 58.04 ?  802 GDP A O3A   1 
HETATM 15893 P  PA    . GDP F 4 .   ? 101.682 154.313 89.458  1.00 62.53 ?  802 GDP A PA    1 
HETATM 15894 O  O1A   . GDP F 4 .   ? 101.296 154.947 90.772  1.00 60.36 -1 802 GDP A O1A   1 
HETATM 15895 O  O2A   . GDP F 4 .   ? 101.163 152.897 89.387  1.00 57.51 ?  802 GDP A O2A   1 
HETATM 15896 O  "O5'" . GDP F 4 .   ? 103.281 154.346 89.266  1.00 58.41 ?  802 GDP A "O5'" 1 
HETATM 15897 C  "C5'" . GDP F 4 .   ? 104.129 154.181 90.396  1.00 58.74 ?  802 GDP A "C5'" 1 
HETATM 15898 C  "C4'" . GDP F 4 .   ? 105.253 153.208 90.081  1.00 56.36 ?  802 GDP A "C4'" 1 
HETATM 15899 O  "O4'" . GDP F 4 .   ? 105.611 152.540 91.292  1.00 56.52 ?  802 GDP A "O4'" 1 
HETATM 15900 C  "C3'" . GDP F 4 .   ? 104.806 152.158 89.079  1.00 58.64 ?  802 GDP A "C3'" 1 
HETATM 15901 O  "O3'" . GDP F 4 .   ? 105.653 152.192 87.927  1.00 59.90 ?  802 GDP A "O3'" 1 
HETATM 15902 C  "C2'" . GDP F 4 .   ? 104.939 150.820 89.775  1.00 57.17 ?  802 GDP A "C2'" 1 
HETATM 15903 O  "O2'" . GDP F 4 .   ? 105.767 149.945 89.006  1.00 58.14 ?  802 GDP A "O2'" 1 
HETATM 15904 C  "C1'" . GDP F 4 .   ? 105.598 151.122 91.112  1.00 54.02 ?  802 GDP A "C1'" 1 
HETATM 15905 N  N9    . GDP F 4 .   ? 104.912 150.457 92.253  1.00 54.87 ?  802 GDP A N9    1 
HETATM 15906 C  C8    . GDP F 4 .   ? 105.549 149.901 93.298  1.00 56.62 ?  802 GDP A C8    1 
HETATM 15907 N  N7    . GDP F 4 .   ? 104.678 149.374 94.191  1.00 56.41 ?  802 GDP A N7    1 
HETATM 15908 C  C5    . GDP F 4 .   ? 103.439 149.604 93.723  1.00 56.75 ?  802 GDP A C5    1 
HETATM 15909 C  C6    . GDP F 4 .   ? 102.061 149.312 94.184  1.00 57.45 ?  802 GDP A C6    1 
HETATM 15910 O  O6    . GDP F 4 .   ? 101.859 148.705 95.257  1.00 57.90 ?  802 GDP A O6    1 
HETATM 15911 N  N1    . GDP F 4 .   ? 101.044 149.714 93.416  1.00 57.76 ?  802 GDP A N1    1 
HETATM 15912 C  C2    . GDP F 4 .   ? 101.236 150.368 92.257  1.00 56.48 ?  802 GDP A C2    1 
HETATM 15913 N  N2    . GDP F 4 .   ? 100.152 150.742 91.536  1.00 57.02 ?  802 GDP A N2    1 
HETATM 15914 N  N3    . GDP F 4 .   ? 102.469 150.670 91.775  1.00 58.50 ?  802 GDP A N3    1 
HETATM 15915 C  C4    . GDP F 4 .   ? 103.594 150.321 92.449  1.00 57.68 ?  802 GDP A C4    1 
HETATM 15916 P  PA    . TTP G 5 .   ? 143.369 148.641 136.035 1.00 19.24 ?  803 TTP A PA    1 
HETATM 15917 O  O1A   . TTP G 5 .   ? 141.937 148.443 136.462 1.00 19.64 -1 803 TTP A O1A   1 
HETATM 15918 O  O2A   . TTP G 5 .   ? 143.557 149.970 135.349 1.00 31.54 ?  803 TTP A O2A   1 
HETATM 15919 O  O3A   . TTP G 5 .   ? 144.381 148.499 137.275 1.00 30.64 ?  803 TTP A O3A   1 
HETATM 15920 P  PB    . TTP G 5 .   ? 144.590 149.676 138.347 1.00 31.57 ?  803 TTP A PB    1 
HETATM 15921 O  O1B   . TTP G 5 .   ? 144.381 151.041 137.740 1.00 27.79 -1 803 TTP A O1B   1 
HETATM 15922 O  O2B   . TTP G 5 .   ? 143.676 149.478 139.528 1.00 31.36 ?  803 TTP A O2B   1 
HETATM 15923 O  O3B   . TTP G 5 .   ? 146.123 149.459 138.779 1.00 27.98 ?  803 TTP A O3B   1 
HETATM 15924 P  PG    . TTP G 5 .   ? 147.311 149.585 137.701 1.00 26.76 ?  803 TTP A PG    1 
HETATM 15925 O  O1G   . TTP G 5 .   ? 146.943 150.585 136.633 1.00 32.07 ?  803 TTP A O1G   1 
HETATM 15926 O  O2G   . TTP G 5 .   ? 148.580 150.021 138.389 1.00 34.92 -1 803 TTP A O2G   1 
HETATM 15927 O  O3G   . TTP G 5 .   ? 147.539 148.236 137.069 1.00 18.37 ?  803 TTP A O3G   1 
HETATM 15928 O  "O5'" . TTP G 5 .   ? 143.857 147.443 135.086 1.00 23.88 ?  803 TTP A "O5'" 1 
HETATM 15929 C  "C5'" . TTP G 5 .   ? 144.389 146.265 135.678 1.00 21.43 ?  803 TTP A "C5'" 1 
HETATM 15930 C  "C4'" . TTP G 5 .   ? 144.393 145.145 134.654 1.00 24.35 ?  803 TTP A "C4'" 1 
HETATM 15931 O  "O4'" . TTP G 5 .   ? 144.219 143.912 135.349 1.00 31.28 ?  803 TTP A "O4'" 1 
HETATM 15932 C  "C3'" . TTP G 5 .   ? 143.239 145.308 133.684 1.00 26.08 ?  803 TTP A "C3'" 1 
HETATM 15933 O  "O3'" . TTP G 5 .   ? 143.726 145.396 132.343 1.00 24.00 ?  803 TTP A "O3'" 1 
HETATM 15934 C  "C2'" . TTP G 5 .   ? 142.385 144.069 133.835 1.00 25.88 ?  803 TTP A "C2'" 1 
HETATM 15935 C  "C1'" . TTP G 5 .   ? 143.082 143.196 134.866 1.00 25.26 ?  803 TTP A "C1'" 1 
HETATM 15936 N  N1    . TTP G 5 .   ? 142.177 142.932 135.984 1.00 25.70 ?  803 TTP A N1    1 
HETATM 15937 C  C2    . TTP G 5 .   ? 141.843 141.602 136.319 1.00 25.54 ?  803 TTP A C2    1 
HETATM 15938 O  O2    . TTP G 5 .   ? 142.326 140.662 135.653 1.00 22.46 ?  803 TTP A O2    1 
HETATM 15939 N  N3    . TTP G 5 .   ? 141.019 141.328 137.337 1.00 24.38 ?  803 TTP A N3    1 
HETATM 15940 C  C4    . TTP G 5 .   ? 140.488 142.313 138.066 1.00 29.17 ?  803 TTP A C4    1 
HETATM 15941 O  O4    . TTP G 5 .   ? 139.720 142.056 139.017 1.00 37.02 ?  803 TTP A O4    1 
HETATM 15942 C  C5    . TTP G 5 .   ? 140.824 143.718 137.735 1.00 28.26 ?  803 TTP A C5    1 
HETATM 15943 C  C5M   . TTP G 5 .   ? 140.248 144.855 138.534 1.00 26.39 ?  803 TTP A C5M   1 
HETATM 15944 C  C6    . TTP G 5 .   ? 141.680 143.962 136.675 1.00 27.03 ?  803 TTP A C6    1 
HETATM 15945 MG MG    . MG  H 6 .   ? 145.266 151.099 135.032 1.00 18.30 ?  804 MG  A MG    1 
HETATM 15946 P  PA    . TTP I 5 .   ? 116.837 148.577 126.224 1.00 24.11 ?  801 TTP B PA    1 
HETATM 15947 O  O1A   . TTP I 5 .   ? 118.288 148.969 126.342 1.00 30.19 -1 801 TTP B O1A   1 
HETATM 15948 O  O2A   . TTP I 5 .   ? 115.963 149.485 127.052 1.00 22.18 ?  801 TTP B O2A   1 
HETATM 15949 O  O3A   . TTP I 5 .   ? 116.380 148.537 124.685 1.00 32.55 ?  801 TTP B O3A   1 
HETATM 15950 P  PB    . TTP I 5 .   ? 115.562 149.748 124.016 1.00 29.61 ?  801 TTP B PB    1 
HETATM 15951 O  O1B   . TTP I 5 .   ? 115.557 150.991 124.869 1.00 32.07 -1 801 TTP B O1B   1 
HETATM 15952 O  O2B   . TTP I 5 .   ? 116.129 150.052 122.653 1.00 29.33 ?  801 TTP B O2B   1 
HETATM 15953 O  O3B   . TTP I 5 .   ? 114.093 149.099 123.904 1.00 19.28 ?  801 TTP B O3B   1 
HETATM 15954 P  PG    . TTP I 5 .   ? 112.843 149.734 124.693 1.00 31.34 ?  801 TTP B PG    1 
HETATM 15955 O  O1G   . TTP I 5 .   ? 112.443 151.040 124.052 1.00 34.07 ?  801 TTP B O1G   1 
HETATM 15956 O  O2G   . TTP I 5 .   ? 111.681 148.773 124.643 1.00 23.32 -1 801 TTP B O2G   1 
HETATM 15957 O  O3G   . TTP I 5 .   ? 113.226 149.976 126.132 1.00 34.53 ?  801 TTP B O3G   1 
HETATM 15958 O  "O5'" . TTP I 5 .   ? 116.612 147.050 126.670 1.00 24.93 ?  801 TTP B "O5'" 1 
HETATM 15959 C  "C5'" . TTP I 5 .   ? 115.653 146.771 127.683 1.00 24.44 ?  801 TTP B "C5'" 1 
HETATM 15960 C  "C4'" . TTP I 5 .   ? 115.694 145.296 128.051 1.00 24.00 ?  801 TTP B "C4'" 1 
HETATM 15961 O  "O4'" . TTP I 5 .   ? 115.893 144.501 126.884 1.00 28.53 ?  801 TTP B "O4'" 1 
HETATM 15962 C  "C3'" . TTP I 5 .   ? 116.849 144.984 128.982 1.00 27.23 ?  801 TTP B "C3'" 1 
HETATM 15963 O  "O3'" . TTP I 5 .   ? 116.401 144.914 130.338 1.00 27.74 ?  801 TTP B "O3'" 1 
HETATM 15964 C  "C2'" . TTP I 5 .   ? 117.364 143.633 128.528 1.00 27.40 ?  801 TTP B "C2'" 1 
HETATM 15965 C  "C1'" . TTP I 5 .   ? 116.656 143.338 127.215 1.00 29.90 ?  801 TTP B "C1'" 1 
HETATM 15966 N  N1    . TTP I 5 .   ? 117.645 143.052 126.177 1.00 28.87 ?  801 TTP B N1    1 
HETATM 15967 C  C2    . TTP I 5 .   ? 118.051 141.718 125.964 1.00 27.67 ?  801 TTP B C2    1 
HETATM 15968 O  O2    . TTP I 5 .   ? 117.550 140.810 126.660 1.00 29.22 ?  801 TTP B O2    1 
HETATM 15969 N  N3    . TTP I 5 .   ? 118.955 141.401 125.028 1.00 25.56 ?  801 TTP B N3    1 
HETATM 15970 C  C4    . TTP I 5 .   ? 119.503 142.351 124.269 1.00 29.58 ?  801 TTP B C4    1 
HETATM 15971 O  O4    . TTP I 5 .   ? 120.347 142.055 123.398 1.00 38.14 ?  801 TTP B O4    1 
HETATM 15972 C  C5    . TTP I 5 .   ? 119.098 143.763 124.476 1.00 24.40 ?  801 TTP B C5    1 
HETATM 15973 C  C5M   . TTP I 5 .   ? 119.694 144.863 123.640 1.00 26.91 ?  801 TTP B C5M   1 
HETATM 15974 C  C6    . TTP I 5 .   ? 118.159 144.052 125.454 1.00 27.32 ?  801 TTP B C6    1 
HETATM 15975 MG MG    . MG  J 6 .   ? 114.737 151.100 127.229 1.00 37.62 ?  802 MG  B MG    1 
HETATM 15976 P  PG    . ATP K 3 .   ? 154.108 139.976 180.223 1.00 70.08 ?  803 ATP B PG    1 
HETATM 15977 O  O1G   . ATP K 3 .   ? 154.038 140.547 178.848 1.00 62.41 ?  803 ATP B O1G   1 
HETATM 15978 O  O2G   . ATP K 3 .   ? 154.065 141.038 181.328 1.00 61.28 -1 803 ATP B O2G   1 
HETATM 15979 O  O3G   . ATP K 3 .   ? 153.039 138.916 180.506 1.00 60.15 ?  803 ATP B O3G   1 
HETATM 15980 P  PB    . ATP K 3 .   ? 156.060 137.751 180.716 1.00 67.84 ?  803 ATP B PB    1 
HETATM 15981 O  O1B   . ATP K 3 .   ? 157.343 137.516 180.024 1.00 59.55 -1 803 ATP B O1B   1 
HETATM 15982 O  O2B   . ATP K 3 .   ? 156.072 137.541 182.231 1.00 61.48 ?  803 ATP B O2B   1 
HETATM 15983 O  O3B   . ATP K 3 .   ? 155.500 139.218 180.449 1.00 62.14 ?  803 ATP B O3B   1 
HETATM 15984 P  PA    . ATP K 3 .   ? 154.521 136.213 178.709 1.00 67.77 ?  803 ATP B PA    1 
HETATM 15985 O  O1A   . ATP K 3 .   ? 153.093 136.416 178.392 1.00 60.17 -1 803 ATP B O1A   1 
HETATM 15986 O  O2A   . ATP K 3 .   ? 154.983 134.757 178.725 1.00 60.55 ?  803 ATP B O2A   1 
HETATM 15987 O  O3A   . ATP K 3 .   ? 154.898 136.840 180.123 1.00 61.79 ?  803 ATP B O3A   1 
HETATM 15988 O  "O5'" . ATP K 3 .   ? 155.445 137.016 177.712 1.00 60.51 ?  803 ATP B "O5'" 1 
HETATM 15989 C  "C5'" . ATP K 3 .   ? 155.567 136.628 176.327 1.00 57.17 ?  803 ATP B "C5'" 1 
HETATM 15990 C  "C4'" . ATP K 3 .   ? 155.060 137.750 175.457 1.00 59.72 ?  803 ATP B "C4'" 1 
HETATM 15991 O  "O4'" . ATP K 3 .   ? 154.378 137.198 174.309 1.00 60.83 ?  803 ATP B "O4'" 1 
HETATM 15992 C  "C3'" . ATP K 3 .   ? 154.056 138.686 176.123 1.00 58.64 ?  803 ATP B "C3'" 1 
HETATM 15993 O  "O3'" . ATP K 3 .   ? 154.715 139.774 176.759 1.00 58.59 ?  803 ATP B "O3'" 1 
HETATM 15994 C  "C2'" . ATP K 3 .   ? 153.206 139.154 174.940 1.00 58.56 ?  803 ATP B "C2'" 1 
HETATM 15995 O  "O2'" . ATP K 3 .   ? 153.826 140.221 174.232 1.00 59.99 ?  803 ATP B "O2'" 1 
HETATM 15996 C  "C1'" . ATP K 3 .   ? 153.163 137.890 174.080 1.00 57.94 ?  803 ATP B "C1'" 1 
HETATM 15997 N  N9    . ATP K 3 .   ? 152.057 136.992 174.395 1.00 59.22 ?  803 ATP B N9    1 
HETATM 15998 C  C8    . ATP K 3 .   ? 152.122 135.796 175.061 1.00 57.41 ?  803 ATP B C8    1 
HETATM 15999 N  N7    . ATP K 3 .   ? 150.964 135.199 175.202 1.00 58.19 ?  803 ATP B N7    1 
HETATM 16000 C  C5    . ATP K 3 .   ? 150.072 136.063 174.586 1.00 58.18 ?  803 ATP B C5    1 
HETATM 16001 C  C6    . ATP K 3 .   ? 148.679 136.011 174.390 1.00 55.35 ?  803 ATP B C6    1 
HETATM 16002 N  N6    . ATP K 3 .   ? 147.904 135.008 174.815 1.00 55.86 ?  803 ATP B N6    1 
HETATM 16003 N  N1    . ATP K 3 .   ? 148.097 137.038 173.734 1.00 57.37 ?  803 ATP B N1    1 
HETATM 16004 C  C2    . ATP K 3 .   ? 148.864 138.046 173.308 1.00 55.85 ?  803 ATP B C2    1 
HETATM 16005 N  N3    . ATP K 3 .   ? 150.183 138.203 173.432 1.00 57.67 ?  803 ATP B N3    1 
HETATM 16006 C  C4    . ATP K 3 .   ? 150.732 137.173 174.084 1.00 59.74 ?  803 ATP B C4    1 
HETATM 16007 P  PB    . GDP L 4 .   ? 160.083 154.462 174.668 1.00 69.13 ?  804 GDP B PB    1 
HETATM 16008 O  O1B   . GDP L 4 .   ? 160.886 153.184 174.679 1.00 61.24 ?  804 GDP B O1B   1 
HETATM 16009 O  O2B   . GDP L 4 .   ? 160.122 155.090 176.041 1.00 59.98 -1 804 GDP B O2B   1 
HETATM 16010 O  O3B   . GDP L 4 .   ? 160.666 155.417 173.655 1.00 59.87 ?  804 GDP B O3B   1 
HETATM 16011 O  O3A   . GDP L 4 .   ? 158.554 154.134 174.291 1.00 58.19 ?  804 GDP B O3A   1 
HETATM 16012 P  PA    . GDP L 4 .   ? 158.126 153.629 172.824 1.00 64.69 ?  804 GDP B PA    1 
HETATM 16013 O  O1A   . GDP L 4 .   ? 158.238 154.731 171.798 1.00 59.39 -1 804 GDP B O1A   1 
HETATM 16014 O  O2A   . GDP L 4 .   ? 158.950 152.435 172.406 1.00 58.30 ?  804 GDP B O2A   1 
HETATM 16015 O  "O5'" . GDP L 4 .   ? 156.591 153.216 173.061 1.00 61.40 ?  804 GDP B "O5'" 1 
HETATM 16016 C  "C5'" . GDP L 4 .   ? 155.589 153.490 172.086 1.00 57.46 ?  804 GDP B "C5'" 1 
HETATM 16017 C  "C4'" . GDP L 4 .   ? 154.436 152.522 172.294 1.00 55.92 ?  804 GDP B "C4'" 1 
HETATM 16018 O  "O4'" . GDP L 4 .   ? 154.171 151.881 171.047 1.00 58.58 ?  804 GDP B "O4'" 1 
HETATM 16019 C  "C3'" . GDP L 4 .   ? 154.815 151.451 173.303 1.00 59.02 ?  804 GDP B "C3'" 1 
HETATM 16020 O  "O3'" . GDP L 4 .   ? 153.798 151.324 174.301 1.00 58.82 ?  804 GDP B "O3'" 1 
HETATM 16021 C  "C2'" . GDP L 4 .   ? 154.929 150.162 172.519 1.00 56.94 ?  804 GDP B "C2'" 1 
HETATM 16022 O  "O2'" . GDP L 4 .   ? 154.243 149.105 173.194 1.00 59.26 ?  804 GDP B "O2'" 1 
HETATM 16023 C  "C1'" . GDP L 4 .   ? 154.273 150.462 171.181 1.00 55.87 ?  804 GDP B "C1'" 1 
HETATM 16024 N  N9    . GDP L 4 .   ? 155.013 149.887 170.027 1.00 56.16 ?  804 GDP B N9    1 
HETATM 16025 C  C8    . GDP L 4 .   ? 154.424 149.376 168.931 1.00 57.86 ?  804 GDP B C8    1 
HETATM 16026 N  N7    . GDP L 4 .   ? 155.341 148.933 168.040 1.00 59.36 ?  804 GDP B N7    1 
HETATM 16027 C  C5    . GDP L 4 .   ? 156.557 149.175 168.558 1.00 59.05 ?  804 GDP B C5    1 
HETATM 16028 C  C6    . GDP L 4 .   ? 157.958 148.957 168.129 1.00 58.07 ?  804 GDP B C6    1 
HETATM 16029 O  O6    . GDP L 4 .   ? 158.215 148.424 167.029 1.00 59.08 ?  804 GDP B O6    1 
HETATM 16030 N  N1    . GDP L 4 .   ? 158.937 149.348 168.953 1.00 57.10 ?  804 GDP B N1    1 
HETATM 16031 C  C2    . GDP L 4 .   ? 158.684 149.923 170.142 1.00 57.92 ?  804 GDP B C2    1 
HETATM 16032 N  N2    . GDP L 4 .   ? 159.729 150.290 170.923 1.00 58.60 ?  804 GDP B N2    1 
HETATM 16033 N  N3    . GDP L 4 .   ? 157.428 150.153 170.596 1.00 60.62 ?  804 GDP B N3    1 
HETATM 16034 C  C4    . GDP L 4 .   ? 156.340 149.809 169.867 1.00 59.26 ?  804 GDP B C4    1 
HETATM 16035 MN MN    . MN  M 7 .   ? 127.345 81.568  119.277 0.85 25.05 ?  401 MN  C MN    1 
HETATM 16036 MN MN    . MN  N 7 .   ? 124.560 83.594  120.726 0.85 26.37 ?  402 MN  C MN    1 
HETATM 16037 MN MN    . MN  O 7 .   ? 141.986 96.806  130.894 1.00 22.51 ?  401 MN  D MN    1 
HETATM 16038 MN MN    . MN  P 7 .   ? 144.021 96.904  127.556 1.00 24.72 ?  402 MN  D MN    1 
# 
