data_9CAY
# 
_entry.id   9CAY 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9CAY         pdb_00009cay 10.2210/pdb9cay/pdb 
WWPDB D_1000283863 ?            ?                   
EMDB  EMD-45407    ?            ?                   
# 
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 
1 'Structure model' 1 0 2024-11-06 
2 'Structure model' 1 1 2024-11-13 
3 'Structure model' 1 2 2024-11-27 
# 
_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' 
3 3 'Structure model' 'Data collection'     
4 3 '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' citation_author 
3 2 'Structure model' em_admin        
4 3 'Structure model' citation        
5 3 '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.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
12 2 'Structure model' '_em_admin.last_update'             
13 3 'Structure model' '_citation.journal_volume'          
14 3 'Structure model' '_citation.title'                   
15 3 '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                        9CAY 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-18 
_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 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Ternary structure of Plasmodium falciparum apicoplast DNA polymerase (exo-minus)' 
_pdbx_database_related.db_id          EMD-45407 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yg60@rice.edu 
_pdbx_contact_author.name_first         Yang 
_pdbx_contact_author.name_last          Gao 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4037-0431 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lo, C.-Y.' 1 ? 
'Gao, Y.'   2 ? 
# 
_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            J.Mol.Biol. 
_citation.journal_id_ASTM           JMOBAK 
_citation.journal_id_CSD            0070 
_citation.journal_id_ISSN           1089-8638 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            436 
_citation.language                  ? 
_citation.page_first                168842 
_citation.page_last                 168842 
_citation.title                     'Cryo-EM Structures of the Plasmodium falciparum Apicoplast DNA Polymerase.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jmb.2024.168842 
_citation.pdbx_database_id_PubMed   39490679 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lo, C.Y.'     1 ? 
primary 'Ung, A.R.'    2 ? 
primary 'Koley, T.'    3 ? 
primary 'Nelson, S.W.' 4 ? 
primary 'Gao, Y.'      5 ? 
# 
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     syn 
;DNA (5'-D(P*CP*AP*GP*CP*TP*CP*TP*AP*CP*GP*GP*AP*TP*GP*CP*CP*TP*CP*AP*CP*A)-3')
;
8864.712  1 ?       ?            ? ? 
2 polymer     syn 'Plastid replication-repair enzyme'                                              74002.891 1 2.7.7.7 
'D82N, E84Q' ? ? 
3 polymer     syn 
;DNA (5'-D(*AP*TP*GP*TP*GP*AP*GP*GP*CP*AP*TP*CP*CP*GP*TP*AP*GP*(2DA))-3')
;
6198.027  1 ?       ?            ? ? 
4 non-polymer syn 'MAGNESIUM ION'                                                                  24.305    1 ?       ? ? ? 
5 non-polymer syn "2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE"                                              507.181   1 ?       ? ? ? 
# 
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 polydeoxyribonucleotide no no  
;(DG)(DC)(DA)(DG)(DT)(DC)(DA)(DG)(DC)(DT)(DC)(DT)(DA)(DC)(DG)(DG)(DA)(DT)(DG)(DC)
(DC)(DT)(DC)(DA)(DC)(DA)(DG)(DC)(DA)
;
GCAGTCAGCTCTACGGATGCCTCACAGCA E ? 
2 'polypeptide(L)'        no no  
;DEITKKYIKDNIINVDDNIIKKKDIFKLKNENNEITECAFEYFESKKKFDDDIESRFFIINDNNYNENINLIYKDIKYCG
LNIQTTGLEVFDENIRLIQIAVENYPVIIYDMFNINKKDILDGLRKVLENKNIIKIIQNGKFDAKFLLHNNFKIENIFDT
YIASKLLDKNKNMYGFKLNNIVEKYLNVILDKQQQNSVWNNSLLNNNQLFYAARDSSCLLKLYKKLKEEIKKENLHIVND
IENKCILPICDMELNGIKVDLENLQKSTNEILNELNIEKDNLKKKLKDENINVNSQQQVLKALQKNNVRDISNKLIENTS
DSNLKNFLNHEEIISLRNYRRLYKLYSAFYLKLPLHINTKTNKIHTTFNQLKTFSGRFSSEKPNLQQIPRQKNIREIFIP
NDNNIFIIADFKQIELKIAAEITNDEIMLKAYNNNIDLHTLTASIITKKNIPDINKEDRHIAKAINFGLIYGMNYVNLKN
YANTYYGLNMSLDQCLYFYNSFFEHYKGIYKWHNQVKQKRALQYSTLSNRKVIFPYFSFTKALNYPVQGTCADILKLALV
DLYDNLKDINGKIILCVHDEIIIEVNKKFQEEALKILVQSMENSASYFLKKVKCEVSVKIAENWGSKD
;
;DEITKKYIKDNIINVDDNIIKKKDIFKLKNENNEITECAFEYFESKKKFDDDIESRFFIINDNNYNENINLIYKDIKYCG
LNIQTTGLEVFDENIRLIQIAVENYPVIIYDMFNINKKDILDGLRKVLENKNIIKIIQNGKFDAKFLLHNNFKIENIFDT
YIASKLLDKNKNMYGFKLNNIVEKYLNVILDKQQQNSVWNNSLLNNNQLFYAARDSSCLLKLYKKLKEEIKKENLHIVND
IENKCILPICDMELNGIKVDLENLQKSTNEILNELNIEKDNLKKKLKDENINVNSQQQVLKALQKNNVRDISNKLIENTS
DSNLKNFLNHEEIISLRNYRRLYKLYSAFYLKLPLHINTKTNKIHTTFNQLKTFSGRFSSEKPNLQQIPRQKNIREIFIP
NDNNIFIIADFKQIELKIAAEITNDEIMLKAYNNNIDLHTLTASIITKKNIPDINKEDRHIAKAINFGLIYGMNYVNLKN
YANTYYGLNMSLDQCLYFYNSFFEHYKGIYKWHNQVKQKRALQYSTLSNRKVIFPYFSFTKALNYPVQGTCADILKLALV
DLYDNLKDINGKIILCVHDEIIIEVNKKFQEEALKILVQSMENSASYFLKKVKCEVSVKIAENWGSKD
;
A ? 
3 polydeoxyribonucleotide no yes 
;(DT)(DG)(DA)(DT)(DG)(DT)(DG)(DA)(DG)(DG)(DC)(DA)(DT)(DC)(DC)(DG)(DT)(DA)(DG)
(2DA)
;
TGATGTGAGGCATCCGTAGA F ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'MAGNESIUM ION'                     MG  
5 "2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE" DGT 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   DG  n 
1 2   DC  n 
1 3   DA  n 
1 4   DG  n 
1 5   DT  n 
1 6   DC  n 
1 7   DA  n 
1 8   DG  n 
1 9   DC  n 
1 10  DT  n 
1 11  DC  n 
1 12  DT  n 
1 13  DA  n 
1 14  DC  n 
1 15  DG  n 
1 16  DG  n 
1 17  DA  n 
1 18  DT  n 
1 19  DG  n 
1 20  DC  n 
1 21  DC  n 
1 22  DT  n 
1 23  DC  n 
1 24  DA  n 
1 25  DC  n 
1 26  DA  n 
1 27  DG  n 
1 28  DC  n 
1 29  DA  n 
2 1   ASP n 
2 2   GLU n 
2 3   ILE n 
2 4   THR n 
2 5   LYS n 
2 6   LYS n 
2 7   TYR n 
2 8   ILE n 
2 9   LYS n 
2 10  ASP n 
2 11  ASN n 
2 12  ILE n 
2 13  ILE n 
2 14  ASN n 
2 15  VAL n 
2 16  ASP n 
2 17  ASP n 
2 18  ASN n 
2 19  ILE n 
2 20  ILE n 
2 21  LYS n 
2 22  LYS n 
2 23  LYS n 
2 24  ASP n 
2 25  ILE n 
2 26  PHE n 
2 27  LYS n 
2 28  LEU n 
2 29  LYS n 
2 30  ASN n 
2 31  GLU n 
2 32  ASN n 
2 33  ASN n 
2 34  GLU n 
2 35  ILE n 
2 36  THR n 
2 37  GLU n 
2 38  CYS n 
2 39  ALA n 
2 40  PHE n 
2 41  GLU n 
2 42  TYR n 
2 43  PHE n 
2 44  GLU n 
2 45  SER n 
2 46  LYS n 
2 47  LYS n 
2 48  LYS n 
2 49  PHE n 
2 50  ASP n 
2 51  ASP n 
2 52  ASP n 
2 53  ILE n 
2 54  GLU n 
2 55  SER n 
2 56  ARG n 
2 57  PHE n 
2 58  PHE n 
2 59  ILE n 
2 60  ILE n 
2 61  ASN n 
2 62  ASP n 
2 63  ASN n 
2 64  ASN n 
2 65  TYR n 
2 66  ASN n 
2 67  GLU n 
2 68  ASN n 
2 69  ILE n 
2 70  ASN n 
2 71  LEU n 
2 72  ILE n 
2 73  TYR n 
2 74  LYS n 
2 75  ASP n 
2 76  ILE n 
2 77  LYS n 
2 78  TYR n 
2 79  CYS n 
2 80  GLY n 
2 81  LEU n 
2 82  ASN n 
2 83  ILE n 
2 84  GLN n 
2 85  THR n 
2 86  THR n 
2 87  GLY n 
2 88  LEU n 
2 89  GLU n 
2 90  VAL n 
2 91  PHE n 
2 92  ASP n 
2 93  GLU n 
2 94  ASN n 
2 95  ILE n 
2 96  ARG n 
2 97  LEU n 
2 98  ILE n 
2 99  GLN n 
2 100 ILE n 
2 101 ALA n 
2 102 VAL n 
2 103 GLU n 
2 104 ASN n 
2 105 TYR n 
2 106 PRO n 
2 107 VAL n 
2 108 ILE n 
2 109 ILE n 
2 110 TYR n 
2 111 ASP n 
2 112 MET n 
2 113 PHE n 
2 114 ASN n 
2 115 ILE n 
2 116 ASN n 
2 117 LYS n 
2 118 LYS n 
2 119 ASP n 
2 120 ILE n 
2 121 LEU n 
2 122 ASP n 
2 123 GLY n 
2 124 LEU n 
2 125 ARG n 
2 126 LYS n 
2 127 VAL n 
2 128 LEU n 
2 129 GLU n 
2 130 ASN n 
2 131 LYS n 
2 132 ASN n 
2 133 ILE n 
2 134 ILE n 
2 135 LYS n 
2 136 ILE n 
2 137 ILE n 
2 138 GLN n 
2 139 ASN n 
2 140 GLY n 
2 141 LYS n 
2 142 PHE n 
2 143 ASP n 
2 144 ALA n 
2 145 LYS n 
2 146 PHE n 
2 147 LEU n 
2 148 LEU n 
2 149 HIS n 
2 150 ASN n 
2 151 ASN n 
2 152 PHE n 
2 153 LYS n 
2 154 ILE n 
2 155 GLU n 
2 156 ASN n 
2 157 ILE n 
2 158 PHE n 
2 159 ASP n 
2 160 THR n 
2 161 TYR n 
2 162 ILE n 
2 163 ALA n 
2 164 SER n 
2 165 LYS n 
2 166 LEU n 
2 167 LEU n 
2 168 ASP n 
2 169 LYS n 
2 170 ASN n 
2 171 LYS n 
2 172 ASN n 
2 173 MET n 
2 174 TYR n 
2 175 GLY n 
2 176 PHE n 
2 177 LYS n 
2 178 LEU n 
2 179 ASN n 
2 180 ASN n 
2 181 ILE n 
2 182 VAL n 
2 183 GLU n 
2 184 LYS n 
2 185 TYR n 
2 186 LEU n 
2 187 ASN n 
2 188 VAL n 
2 189 ILE n 
2 190 LEU n 
2 191 ASP n 
2 192 LYS n 
2 193 GLN n 
2 194 GLN n 
2 195 GLN n 
2 196 ASN n 
2 197 SER n 
2 198 VAL n 
2 199 TRP n 
2 200 ASN n 
2 201 ASN n 
2 202 SER n 
2 203 LEU n 
2 204 LEU n 
2 205 ASN n 
2 206 ASN n 
2 207 ASN n 
2 208 GLN n 
2 209 LEU n 
2 210 PHE n 
2 211 TYR n 
2 212 ALA n 
2 213 ALA n 
2 214 ARG n 
2 215 ASP n 
2 216 SER n 
2 217 SER n 
2 218 CYS n 
2 219 LEU n 
2 220 LEU n 
2 221 LYS n 
2 222 LEU n 
2 223 TYR n 
2 224 LYS n 
2 225 LYS n 
2 226 LEU n 
2 227 LYS n 
2 228 GLU n 
2 229 GLU n 
2 230 ILE n 
2 231 LYS n 
2 232 LYS n 
2 233 GLU n 
2 234 ASN n 
2 235 LEU n 
2 236 HIS n 
2 237 ILE n 
2 238 VAL n 
2 239 ASN n 
2 240 ASP n 
2 241 ILE n 
2 242 GLU n 
2 243 ASN n 
2 244 LYS n 
2 245 CYS n 
2 246 ILE n 
2 247 LEU n 
2 248 PRO n 
2 249 ILE n 
2 250 CYS n 
2 251 ASP n 
2 252 MET n 
2 253 GLU n 
2 254 LEU n 
2 255 ASN n 
2 256 GLY n 
2 257 ILE n 
2 258 LYS n 
2 259 VAL n 
2 260 ASP n 
2 261 LEU n 
2 262 GLU n 
2 263 ASN n 
2 264 LEU n 
2 265 GLN n 
2 266 LYS n 
2 267 SER n 
2 268 THR n 
2 269 ASN n 
2 270 GLU n 
2 271 ILE n 
2 272 LEU n 
2 273 ASN n 
2 274 GLU n 
2 275 LEU n 
2 276 ASN n 
2 277 ILE n 
2 278 GLU n 
2 279 LYS n 
2 280 ASP n 
2 281 ASN n 
2 282 LEU n 
2 283 LYS n 
2 284 LYS n 
2 285 LYS n 
2 286 LEU n 
2 287 LYS n 
2 288 ASP n 
2 289 GLU n 
2 290 ASN n 
2 291 ILE n 
2 292 ASN n 
2 293 VAL n 
2 294 ASN n 
2 295 SER n 
2 296 GLN n 
2 297 GLN n 
2 298 GLN n 
2 299 VAL n 
2 300 LEU n 
2 301 LYS n 
2 302 ALA n 
2 303 LEU n 
2 304 GLN n 
2 305 LYS n 
2 306 ASN n 
2 307 ASN n 
2 308 VAL n 
2 309 ARG n 
2 310 ASP n 
2 311 ILE n 
2 312 SER n 
2 313 ASN n 
2 314 LYS n 
2 315 LEU n 
2 316 ILE n 
2 317 GLU n 
2 318 ASN n 
2 319 THR n 
2 320 SER n 
2 321 ASP n 
2 322 SER n 
2 323 ASN n 
2 324 LEU n 
2 325 LYS n 
2 326 ASN n 
2 327 PHE n 
2 328 LEU n 
2 329 ASN n 
2 330 HIS n 
2 331 GLU n 
2 332 GLU n 
2 333 ILE n 
2 334 ILE n 
2 335 SER n 
2 336 LEU n 
2 337 ARG n 
2 338 ASN n 
2 339 TYR n 
2 340 ARG n 
2 341 ARG n 
2 342 LEU n 
2 343 TYR n 
2 344 LYS n 
2 345 LEU n 
2 346 TYR n 
2 347 SER n 
2 348 ALA n 
2 349 PHE n 
2 350 TYR n 
2 351 LEU n 
2 352 LYS n 
2 353 LEU n 
2 354 PRO n 
2 355 LEU n 
2 356 HIS n 
2 357 ILE n 
2 358 ASN n 
2 359 THR n 
2 360 LYS n 
2 361 THR n 
2 362 ASN n 
2 363 LYS n 
2 364 ILE n 
2 365 HIS n 
2 366 THR n 
2 367 THR n 
2 368 PHE n 
2 369 ASN n 
2 370 GLN n 
2 371 LEU n 
2 372 LYS n 
2 373 THR n 
2 374 PHE n 
2 375 SER n 
2 376 GLY n 
2 377 ARG n 
2 378 PHE n 
2 379 SER n 
2 380 SER n 
2 381 GLU n 
2 382 LYS n 
2 383 PRO n 
2 384 ASN n 
2 385 LEU n 
2 386 GLN n 
2 387 GLN n 
2 388 ILE n 
2 389 PRO n 
2 390 ARG n 
2 391 GLN n 
2 392 LYS n 
2 393 ASN n 
2 394 ILE n 
2 395 ARG n 
2 396 GLU n 
2 397 ILE n 
2 398 PHE n 
2 399 ILE n 
2 400 PRO n 
2 401 ASN n 
2 402 ASP n 
2 403 ASN n 
2 404 ASN n 
2 405 ILE n 
2 406 PHE n 
2 407 ILE n 
2 408 ILE n 
2 409 ALA n 
2 410 ASP n 
2 411 PHE n 
2 412 LYS n 
2 413 GLN n 
2 414 ILE n 
2 415 GLU n 
2 416 LEU n 
2 417 LYS n 
2 418 ILE n 
2 419 ALA n 
2 420 ALA n 
2 421 GLU n 
2 422 ILE n 
2 423 THR n 
2 424 ASN n 
2 425 ASP n 
2 426 GLU n 
2 427 ILE n 
2 428 MET n 
2 429 LEU n 
2 430 LYS n 
2 431 ALA n 
2 432 TYR n 
2 433 ASN n 
2 434 ASN n 
2 435 ASN n 
2 436 ILE n 
2 437 ASP n 
2 438 LEU n 
2 439 HIS n 
2 440 THR n 
2 441 LEU n 
2 442 THR n 
2 443 ALA n 
2 444 SER n 
2 445 ILE n 
2 446 ILE n 
2 447 THR n 
2 448 LYS n 
2 449 LYS n 
2 450 ASN n 
2 451 ILE n 
2 452 PRO n 
2 453 ASP n 
2 454 ILE n 
2 455 ASN n 
2 456 LYS n 
2 457 GLU n 
2 458 ASP n 
2 459 ARG n 
2 460 HIS n 
2 461 ILE n 
2 462 ALA n 
2 463 LYS n 
2 464 ALA n 
2 465 ILE n 
2 466 ASN n 
2 467 PHE n 
2 468 GLY n 
2 469 LEU n 
2 470 ILE n 
2 471 TYR n 
2 472 GLY n 
2 473 MET n 
2 474 ASN n 
2 475 TYR n 
2 476 VAL n 
2 477 ASN n 
2 478 LEU n 
2 479 LYS n 
2 480 ASN n 
2 481 TYR n 
2 482 ALA n 
2 483 ASN n 
2 484 THR n 
2 485 TYR n 
2 486 TYR n 
2 487 GLY n 
2 488 LEU n 
2 489 ASN n 
2 490 MET n 
2 491 SER n 
2 492 LEU n 
2 493 ASP n 
2 494 GLN n 
2 495 CYS n 
2 496 LEU n 
2 497 TYR n 
2 498 PHE n 
2 499 TYR n 
2 500 ASN n 
2 501 SER n 
2 502 PHE n 
2 503 PHE n 
2 504 GLU n 
2 505 HIS n 
2 506 TYR n 
2 507 LYS n 
2 508 GLY n 
2 509 ILE n 
2 510 TYR n 
2 511 LYS n 
2 512 TRP n 
2 513 HIS n 
2 514 ASN n 
2 515 GLN n 
2 516 VAL n 
2 517 LYS n 
2 518 GLN n 
2 519 LYS n 
2 520 ARG n 
2 521 ALA n 
2 522 LEU n 
2 523 GLN n 
2 524 TYR n 
2 525 SER n 
2 526 THR n 
2 527 LEU n 
2 528 SER n 
2 529 ASN n 
2 530 ARG n 
2 531 LYS n 
2 532 VAL n 
2 533 ILE n 
2 534 PHE n 
2 535 PRO n 
2 536 TYR n 
2 537 PHE n 
2 538 SER n 
2 539 PHE n 
2 540 THR n 
2 541 LYS n 
2 542 ALA n 
2 543 LEU n 
2 544 ASN n 
2 545 TYR n 
2 546 PRO n 
2 547 VAL n 
2 548 GLN n 
2 549 GLY n 
2 550 THR n 
2 551 CYS n 
2 552 ALA n 
2 553 ASP n 
2 554 ILE n 
2 555 LEU n 
2 556 LYS n 
2 557 LEU n 
2 558 ALA n 
2 559 LEU n 
2 560 VAL n 
2 561 ASP n 
2 562 LEU n 
2 563 TYR n 
2 564 ASP n 
2 565 ASN n 
2 566 LEU n 
2 567 LYS n 
2 568 ASP n 
2 569 ILE n 
2 570 ASN n 
2 571 GLY n 
2 572 LYS n 
2 573 ILE n 
2 574 ILE n 
2 575 LEU n 
2 576 CYS n 
2 577 VAL n 
2 578 HIS n 
2 579 ASP n 
2 580 GLU n 
2 581 ILE n 
2 582 ILE n 
2 583 ILE n 
2 584 GLU n 
2 585 VAL n 
2 586 ASN n 
2 587 LYS n 
2 588 LYS n 
2 589 PHE n 
2 590 GLN n 
2 591 GLU n 
2 592 GLU n 
2 593 ALA n 
2 594 LEU n 
2 595 LYS n 
2 596 ILE n 
2 597 LEU n 
2 598 VAL n 
2 599 GLN n 
2 600 SER n 
2 601 MET n 
2 602 GLU n 
2 603 ASN n 
2 604 SER n 
2 605 ALA n 
2 606 SER n 
2 607 TYR n 
2 608 PHE n 
2 609 LEU n 
2 610 LYS n 
2 611 LYS n 
2 612 VAL n 
2 613 LYS n 
2 614 CYS n 
2 615 GLU n 
2 616 VAL n 
2 617 SER n 
2 618 VAL n 
2 619 LYS n 
2 620 ILE n 
2 621 ALA n 
2 622 GLU n 
2 623 ASN n 
2 624 TRP n 
2 625 GLY n 
2 626 SER n 
2 627 LYS n 
2 628 ASP n 
3 1   DT  n 
3 2   DG  n 
3 3   DA  n 
3 4   DT  n 
3 5   DG  n 
3 6   DT  n 
3 7   DG  n 
3 8   DA  n 
3 9   DG  n 
3 10  DG  n 
3 11  DC  n 
3 12  DA  n 
3 13  DT  n 
3 14  DC  n 
3 15  DC  n 
3 16  DG  n 
3 17  DT  n 
3 18  DA  n 
3 19  DG  n 
3 20  2DA n 
# 
loop_
_pdbx_entity_src_syn.entity_id 
_pdbx_entity_src_syn.pdbx_src_id 
_pdbx_entity_src_syn.pdbx_alt_source_flag 
_pdbx_entity_src_syn.pdbx_beg_seq_num 
_pdbx_entity_src_syn.pdbx_end_seq_num 
_pdbx_entity_src_syn.organism_scientific 
_pdbx_entity_src_syn.organism_common_name 
_pdbx_entity_src_syn.ncbi_taxonomy_id 
_pdbx_entity_src_syn.details 
1 1 sample 1 29  'Homo sapiens'                        human 9606  ? 
2 1 sample 1 628 'Plasmodium falciparum (isolate 3D7)' ?     36329 ? 
3 1 sample 1 20  'Homo sapiens'                        human 9606  ? 
# 
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 
2DA 'DNA linking'       n "2',3'-DIDEOXYADENOSINE-5'-MONOPHOSPHATE" ? 'C10 H14 N5 O5 P'   315.222 
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 
CYS 'L-peptide linking' y CYSTEINE                                  ? 'C3 H7 N O2 S'      121.158 
DA  'DNA linking'       y "2'-DEOXYADENOSINE-5'-MONOPHOSPHATE"      ? 'C10 H14 N5 O6 P'   331.222 
DC  'DNA linking'       y "2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE"       ? 'C9 H14 N3 O7 P'    307.197 
DG  'DNA linking'       y "2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE"      ? 'C10 H14 N5 O7 P'   347.221 
DGT non-polymer         . "2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE"       ? 'C10 H16 N5 O13 P3' 507.181 
DT  'DNA linking'       y "THYMIDINE-5'-MONOPHOSPHATE"              ? 'C10 H15 N2 O8 P'   322.208 
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  
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 
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   DG  1   1   ?   ?   ?   E . n 
A 1 2   DC  2   2   ?   ?   ?   E . n 
A 1 3   DA  3   3   ?   ?   ?   E . n 
A 1 4   DG  4   4   ?   ?   ?   E . n 
A 1 5   DT  5   5   ?   ?   ?   E . n 
A 1 6   DC  6   6   6   DC  DC  E . n 
A 1 7   DA  7   7   7   DA  DA  E . n 
A 1 8   DG  8   8   8   DG  DG  E . n 
A 1 9   DC  9   9   9   DC  DC  E . n 
A 1 10  DT  10  10  10  DT  DT  E . n 
A 1 11  DC  11  11  11  DC  DC  E . n 
A 1 12  DT  12  12  12  DT  DT  E . n 
A 1 13  DA  13  13  13  DA  DA  E . n 
A 1 14  DC  14  14  14  DC  DC  E . n 
A 1 15  DG  15  15  15  DG  DG  E . n 
A 1 16  DG  16  16  16  DG  DG  E . n 
A 1 17  DA  17  17  17  DA  DA  E . n 
A 1 18  DT  18  18  18  DT  DT  E . n 
A 1 19  DG  19  19  19  DG  DG  E . n 
A 1 20  DC  20  20  20  DC  DC  E . n 
A 1 21  DC  21  21  21  DC  DC  E . n 
A 1 22  DT  22  22  22  DT  DT  E . n 
A 1 23  DC  23  23  23  DC  DC  E . n 
A 1 24  DA  24  24  24  DA  DA  E . n 
A 1 25  DC  25  25  25  DC  DC  E . n 
A 1 26  DA  26  26  26  DA  DA  E . n 
A 1 27  DG  27  27  ?   ?   ?   E . n 
A 1 28  DC  28  28  ?   ?   ?   E . n 
A 1 29  DA  29  29  ?   ?   ?   E . n 
B 2 1   ASP 1   1   ?   ?   ?   A . n 
B 2 2   GLU 2   2   ?   ?   ?   A . n 
B 2 3   ILE 3   3   ?   ?   ?   A . n 
B 2 4   THR 4   4   ?   ?   ?   A . n 
B 2 5   LYS 5   5   ?   ?   ?   A . n 
B 2 6   LYS 6   6   ?   ?   ?   A . n 
B 2 7   TYR 7   7   ?   ?   ?   A . n 
B 2 8   ILE 8   8   ?   ?   ?   A . n 
B 2 9   LYS 9   9   ?   ?   ?   A . n 
B 2 10  ASP 10  10  ?   ?   ?   A . n 
B 2 11  ASN 11  11  ?   ?   ?   A . n 
B 2 12  ILE 12  12  ?   ?   ?   A . n 
B 2 13  ILE 13  13  ?   ?   ?   A . n 
B 2 14  ASN 14  14  ?   ?   ?   A . n 
B 2 15  VAL 15  15  ?   ?   ?   A . n 
B 2 16  ASP 16  16  ?   ?   ?   A . n 
B 2 17  ASP 17  17  ?   ?   ?   A . n 
B 2 18  ASN 18  18  ?   ?   ?   A . n 
B 2 19  ILE 19  19  ?   ?   ?   A . n 
B 2 20  ILE 20  20  ?   ?   ?   A . n 
B 2 21  LYS 21  21  ?   ?   ?   A . n 
B 2 22  LYS 22  22  ?   ?   ?   A . n 
B 2 23  LYS 23  23  ?   ?   ?   A . n 
B 2 24  ASP 24  24  ?   ?   ?   A . n 
B 2 25  ILE 25  25  ?   ?   ?   A . n 
B 2 26  PHE 26  26  ?   ?   ?   A . n 
B 2 27  LYS 27  27  ?   ?   ?   A . n 
B 2 28  LEU 28  28  ?   ?   ?   A . n 
B 2 29  LYS 29  29  ?   ?   ?   A . n 
B 2 30  ASN 30  30  ?   ?   ?   A . n 
B 2 31  GLU 31  31  ?   ?   ?   A . n 
B 2 32  ASN 32  32  ?   ?   ?   A . n 
B 2 33  ASN 33  33  ?   ?   ?   A . n 
B 2 34  GLU 34  34  ?   ?   ?   A . n 
B 2 35  ILE 35  35  ?   ?   ?   A . n 
B 2 36  THR 36  36  ?   ?   ?   A . n 
B 2 37  GLU 37  37  ?   ?   ?   A . n 
B 2 38  CYS 38  38  ?   ?   ?   A . n 
B 2 39  ALA 39  39  ?   ?   ?   A . n 
B 2 40  PHE 40  40  ?   ?   ?   A . n 
B 2 41  GLU 41  41  ?   ?   ?   A . n 
B 2 42  TYR 42  42  ?   ?   ?   A . n 
B 2 43  PHE 43  43  ?   ?   ?   A . n 
B 2 44  GLU 44  44  ?   ?   ?   A . n 
B 2 45  SER 45  45  ?   ?   ?   A . n 
B 2 46  LYS 46  46  ?   ?   ?   A . n 
B 2 47  LYS 47  47  ?   ?   ?   A . n 
B 2 48  LYS 48  48  ?   ?   ?   A . n 
B 2 49  PHE 49  49  ?   ?   ?   A . n 
B 2 50  ASP 50  50  ?   ?   ?   A . n 
B 2 51  ASP 51  51  ?   ?   ?   A . n 
B 2 52  ASP 52  52  ?   ?   ?   A . n 
B 2 53  ILE 53  53  ?   ?   ?   A . n 
B 2 54  GLU 54  54  ?   ?   ?   A . n 
B 2 55  SER 55  55  ?   ?   ?   A . n 
B 2 56  ARG 56  56  ?   ?   ?   A . n 
B 2 57  PHE 57  57  57  PHE PHE A . n 
B 2 58  PHE 58  58  58  PHE PHE A . n 
B 2 59  ILE 59  59  59  ILE ILE A . n 
B 2 60  ILE 60  60  60  ILE ILE A . n 
B 2 61  ASN 61  61  61  ASN ASN A . n 
B 2 62  ASP 62  62  62  ASP ASP A . n 
B 2 63  ASN 63  63  63  ASN ASN A . n 
B 2 64  ASN 64  64  64  ASN ASN A . n 
B 2 65  TYR 65  65  65  TYR TYR A . n 
B 2 66  ASN 66  66  66  ASN ASN A . n 
B 2 67  GLU 67  67  67  GLU GLU A . n 
B 2 68  ASN 68  68  68  ASN ASN A . n 
B 2 69  ILE 69  69  69  ILE ILE A . n 
B 2 70  ASN 70  70  70  ASN ASN A . n 
B 2 71  LEU 71  71  71  LEU LEU A . n 
B 2 72  ILE 72  72  72  ILE ILE A . n 
B 2 73  TYR 73  73  73  TYR TYR A . n 
B 2 74  LYS 74  74  74  LYS LYS A . n 
B 2 75  ASP 75  75  75  ASP ASP A . n 
B 2 76  ILE 76  76  76  ILE ILE A . n 
B 2 77  LYS 77  77  77  LYS LYS A . n 
B 2 78  TYR 78  78  78  TYR TYR A . n 
B 2 79  CYS 79  79  79  CYS CYS A . n 
B 2 80  GLY 80  80  80  GLY GLY A . n 
B 2 81  LEU 81  81  81  LEU LEU A . n 
B 2 82  ASN 82  82  82  ASN ASN A . n 
B 2 83  ILE 83  83  83  ILE ILE A . n 
B 2 84  GLN 84  84  84  GLN GLN A . n 
B 2 85  THR 85  85  85  THR THR A . n 
B 2 86  THR 86  86  86  THR THR A . n 
B 2 87  GLY 87  87  87  GLY GLY A . n 
B 2 88  LEU 88  88  88  LEU LEU A . n 
B 2 89  GLU 89  89  89  GLU GLU A . n 
B 2 90  VAL 90  90  90  VAL VAL A . n 
B 2 91  PHE 91  91  91  PHE PHE A . n 
B 2 92  ASP 92  92  92  ASP ASP A . n 
B 2 93  GLU 93  93  93  GLU GLU A . n 
B 2 94  ASN 94  94  94  ASN ASN A . n 
B 2 95  ILE 95  95  95  ILE ILE A . n 
B 2 96  ARG 96  96  96  ARG ARG A . n 
B 2 97  LEU 97  97  97  LEU LEU A . n 
B 2 98  ILE 98  98  98  ILE ILE A . n 
B 2 99  GLN 99  99  99  GLN GLN A . n 
B 2 100 ILE 100 100 100 ILE ILE A . n 
B 2 101 ALA 101 101 101 ALA ALA A . n 
B 2 102 VAL 102 102 102 VAL VAL A . n 
B 2 103 GLU 103 103 103 GLU GLU A . n 
B 2 104 ASN 104 104 104 ASN ASN A . n 
B 2 105 TYR 105 105 105 TYR TYR A . n 
B 2 106 PRO 106 106 106 PRO PRO A . n 
B 2 107 VAL 107 107 107 VAL VAL A . n 
B 2 108 ILE 108 108 108 ILE ILE A . n 
B 2 109 ILE 109 109 109 ILE ILE A . n 
B 2 110 TYR 110 110 110 TYR TYR A . n 
B 2 111 ASP 111 111 111 ASP ASP A . n 
B 2 112 MET 112 112 112 MET MET A . n 
B 2 113 PHE 113 113 113 PHE PHE A . n 
B 2 114 ASN 114 114 114 ASN ASN A . n 
B 2 115 ILE 115 115 115 ILE ILE A . n 
B 2 116 ASN 116 116 116 ASN ASN A . n 
B 2 117 LYS 117 117 117 LYS LYS A . n 
B 2 118 LYS 118 118 118 LYS LYS A . n 
B 2 119 ASP 119 119 119 ASP ASP A . n 
B 2 120 ILE 120 120 120 ILE ILE A . n 
B 2 121 LEU 121 121 121 LEU LEU A . n 
B 2 122 ASP 122 122 122 ASP ASP A . n 
B 2 123 GLY 123 123 123 GLY GLY A . n 
B 2 124 LEU 124 124 124 LEU LEU A . n 
B 2 125 ARG 125 125 125 ARG ARG A . n 
B 2 126 LYS 126 126 126 LYS LYS A . n 
B 2 127 VAL 127 127 127 VAL VAL A . n 
B 2 128 LEU 128 128 128 LEU LEU A . n 
B 2 129 GLU 129 129 129 GLU GLU A . n 
B 2 130 ASN 130 130 130 ASN ASN A . n 
B 2 131 LYS 131 131 131 LYS LYS A . n 
B 2 132 ASN 132 132 132 ASN ASN A . n 
B 2 133 ILE 133 133 133 ILE ILE A . n 
B 2 134 ILE 134 134 134 ILE ILE A . n 
B 2 135 LYS 135 135 135 LYS LYS A . n 
B 2 136 ILE 136 136 136 ILE ILE A . n 
B 2 137 ILE 137 137 137 ILE ILE A . n 
B 2 138 GLN 138 138 138 GLN GLN A . n 
B 2 139 ASN 139 139 139 ASN ASN A . n 
B 2 140 GLY 140 140 140 GLY GLY A . n 
B 2 141 LYS 141 141 141 LYS LYS A . n 
B 2 142 PHE 142 142 142 PHE PHE A . n 
B 2 143 ASP 143 143 143 ASP ASP A . n 
B 2 144 ALA 144 144 144 ALA ALA A . n 
B 2 145 LYS 145 145 145 LYS LYS A . n 
B 2 146 PHE 146 146 146 PHE PHE A . n 
B 2 147 LEU 147 147 147 LEU LEU A . n 
B 2 148 LEU 148 148 148 LEU LEU A . n 
B 2 149 HIS 149 149 149 HIS HIS A . n 
B 2 150 ASN 150 150 150 ASN ASN A . n 
B 2 151 ASN 151 151 151 ASN ASN A . n 
B 2 152 PHE 152 152 152 PHE PHE A . n 
B 2 153 LYS 153 153 153 LYS LYS A . n 
B 2 154 ILE 154 154 154 ILE ILE A . n 
B 2 155 GLU 155 155 155 GLU GLU A . n 
B 2 156 ASN 156 156 156 ASN ASN A . n 
B 2 157 ILE 157 157 157 ILE ILE A . n 
B 2 158 PHE 158 158 158 PHE PHE A . n 
B 2 159 ASP 159 159 159 ASP ASP A . n 
B 2 160 THR 160 160 160 THR THR A . n 
B 2 161 TYR 161 161 161 TYR TYR A . n 
B 2 162 ILE 162 162 162 ILE ILE A . n 
B 2 163 ALA 163 163 163 ALA ALA A . n 
B 2 164 SER 164 164 164 SER SER A . n 
B 2 165 LYS 165 165 165 LYS LYS A . n 
B 2 166 LEU 166 166 166 LEU LEU A . n 
B 2 167 LEU 167 167 167 LEU LEU A . n 
B 2 168 ASP 168 168 168 ASP ASP A . n 
B 2 169 LYS 169 169 ?   ?   ?   A . n 
B 2 170 ASN 170 170 ?   ?   ?   A . n 
B 2 171 LYS 171 171 ?   ?   ?   A . n 
B 2 172 ASN 172 172 ?   ?   ?   A . n 
B 2 173 MET 173 173 ?   ?   ?   A . n 
B 2 174 TYR 174 174 ?   ?   ?   A . n 
B 2 175 GLY 175 175 ?   ?   ?   A . n 
B 2 176 PHE 176 176 ?   ?   ?   A . n 
B 2 177 LYS 177 177 ?   ?   ?   A . n 
B 2 178 LEU 178 178 ?   ?   ?   A . n 
B 2 179 ASN 179 179 ?   ?   ?   A . n 
B 2 180 ASN 180 180 ?   ?   ?   A . n 
B 2 181 ILE 181 181 ?   ?   ?   A . n 
B 2 182 VAL 182 182 ?   ?   ?   A . n 
B 2 183 GLU 183 183 ?   ?   ?   A . n 
B 2 184 LYS 184 184 ?   ?   ?   A . n 
B 2 185 TYR 185 185 ?   ?   ?   A . n 
B 2 186 LEU 186 186 ?   ?   ?   A . n 
B 2 187 ASN 187 187 ?   ?   ?   A . n 
B 2 188 VAL 188 188 ?   ?   ?   A . n 
B 2 189 ILE 189 189 ?   ?   ?   A . n 
B 2 190 LEU 190 190 ?   ?   ?   A . n 
B 2 191 ASP 191 191 ?   ?   ?   A . n 
B 2 192 LYS 192 192 ?   ?   ?   A . n 
B 2 193 GLN 193 193 ?   ?   ?   A . n 
B 2 194 GLN 194 194 ?   ?   ?   A . n 
B 2 195 GLN 195 195 ?   ?   ?   A . n 
B 2 196 ASN 196 196 ?   ?   ?   A . n 
B 2 197 SER 197 197 ?   ?   ?   A . n 
B 2 198 VAL 198 198 ?   ?   ?   A . n 
B 2 199 TRP 199 199 ?   ?   ?   A . n 
B 2 200 ASN 200 200 ?   ?   ?   A . n 
B 2 201 ASN 201 201 ?   ?   ?   A . n 
B 2 202 SER 202 202 ?   ?   ?   A . n 
B 2 203 LEU 203 203 ?   ?   ?   A . n 
B 2 204 LEU 204 204 ?   ?   ?   A . n 
B 2 205 ASN 205 205 ?   ?   ?   A . n 
B 2 206 ASN 206 206 ?   ?   ?   A . n 
B 2 207 ASN 207 207 ?   ?   ?   A . n 
B 2 208 GLN 208 208 ?   ?   ?   A . n 
B 2 209 LEU 209 209 ?   ?   ?   A . n 
B 2 210 PHE 210 210 ?   ?   ?   A . n 
B 2 211 TYR 211 211 ?   ?   ?   A . n 
B 2 212 ALA 212 212 ?   ?   ?   A . n 
B 2 213 ALA 213 213 ?   ?   ?   A . n 
B 2 214 ARG 214 214 ?   ?   ?   A . n 
B 2 215 ASP 215 215 ?   ?   ?   A . n 
B 2 216 SER 216 216 ?   ?   ?   A . n 
B 2 217 SER 217 217 ?   ?   ?   A . n 
B 2 218 CYS 218 218 218 CYS CYS A . n 
B 2 219 LEU 219 219 219 LEU LEU A . n 
B 2 220 LEU 220 220 220 LEU LEU A . n 
B 2 221 LYS 221 221 221 LYS LYS A . n 
B 2 222 LEU 222 222 222 LEU LEU A . n 
B 2 223 TYR 223 223 223 TYR TYR A . n 
B 2 224 LYS 224 224 224 LYS LYS A . n 
B 2 225 LYS 225 225 225 LYS LYS A . n 
B 2 226 LEU 226 226 226 LEU LEU A . n 
B 2 227 LYS 227 227 227 LYS LYS A . n 
B 2 228 GLU 228 228 228 GLU GLU A . n 
B 2 229 GLU 229 229 229 GLU GLU A . n 
B 2 230 ILE 230 230 230 ILE ILE A . n 
B 2 231 LYS 231 231 231 LYS LYS A . n 
B 2 232 LYS 232 232 232 LYS LYS A . n 
B 2 233 GLU 233 233 233 GLU GLU A . n 
B 2 234 ASN 234 234 234 ASN ASN A . n 
B 2 235 LEU 235 235 235 LEU LEU A . n 
B 2 236 HIS 236 236 236 HIS HIS A . n 
B 2 237 ILE 237 237 237 ILE ILE A . n 
B 2 238 VAL 238 238 238 VAL VAL A . n 
B 2 239 ASN 239 239 239 ASN ASN A . n 
B 2 240 ASP 240 240 240 ASP ASP A . n 
B 2 241 ILE 241 241 241 ILE ILE A . n 
B 2 242 GLU 242 242 242 GLU GLU A . n 
B 2 243 ASN 243 243 243 ASN ASN A . n 
B 2 244 LYS 244 244 244 LYS LYS A . n 
B 2 245 CYS 245 245 245 CYS CYS A . n 
B 2 246 ILE 246 246 246 ILE ILE A . n 
B 2 247 LEU 247 247 247 LEU LEU A . n 
B 2 248 PRO 248 248 248 PRO PRO A . n 
B 2 249 ILE 249 249 249 ILE ILE A . n 
B 2 250 CYS 250 250 250 CYS CYS A . n 
B 2 251 ASP 251 251 251 ASP ASP A . n 
B 2 252 MET 252 252 252 MET MET A . n 
B 2 253 GLU 253 253 253 GLU GLU A . n 
B 2 254 LEU 254 254 254 LEU LEU A . n 
B 2 255 ASN 255 255 255 ASN ASN A . n 
B 2 256 GLY 256 256 256 GLY GLY A . n 
B 2 257 ILE 257 257 257 ILE ILE A . n 
B 2 258 LYS 258 258 258 LYS LYS A . n 
B 2 259 VAL 259 259 259 VAL VAL A . n 
B 2 260 ASP 260 260 260 ASP ASP A . n 
B 2 261 LEU 261 261 261 LEU LEU A . n 
B 2 262 GLU 262 262 262 GLU GLU A . n 
B 2 263 ASN 263 263 263 ASN ASN A . n 
B 2 264 LEU 264 264 264 LEU LEU A . n 
B 2 265 GLN 265 265 265 GLN GLN A . n 
B 2 266 LYS 266 266 266 LYS LYS A . n 
B 2 267 SER 267 267 267 SER SER A . n 
B 2 268 THR 268 268 268 THR THR A . n 
B 2 269 ASN 269 269 269 ASN ASN A . n 
B 2 270 GLU 270 270 270 GLU GLU A . n 
B 2 271 ILE 271 271 271 ILE ILE A . n 
B 2 272 LEU 272 272 272 LEU LEU A . n 
B 2 273 ASN 273 273 273 ASN ASN A . n 
B 2 274 GLU 274 274 274 GLU GLU A . n 
B 2 275 LEU 275 275 275 LEU LEU A . n 
B 2 276 ASN 276 276 276 ASN ASN A . n 
B 2 277 ILE 277 277 277 ILE ILE A . n 
B 2 278 GLU 278 278 278 GLU GLU A . n 
B 2 279 LYS 279 279 279 LYS LYS A . n 
B 2 280 ASP 280 280 280 ASP ASP A . n 
B 2 281 ASN 281 281 281 ASN ASN A . n 
B 2 282 LEU 282 282 282 LEU LEU A . n 
B 2 283 LYS 283 283 283 LYS LYS A . n 
B 2 284 LYS 284 284 284 LYS LYS A . n 
B 2 285 LYS 285 285 285 LYS LYS A . n 
B 2 286 LEU 286 286 286 LEU LEU A . n 
B 2 287 LYS 287 287 287 LYS LYS A . n 
B 2 288 ASP 288 288 288 ASP ASP A . n 
B 2 289 GLU 289 289 289 GLU GLU A . n 
B 2 290 ASN 290 290 290 ASN ASN A . n 
B 2 291 ILE 291 291 291 ILE ILE A . n 
B 2 292 ASN 292 292 292 ASN ASN A . n 
B 2 293 VAL 293 293 293 VAL VAL A . n 
B 2 294 ASN 294 294 294 ASN ASN A . n 
B 2 295 SER 295 295 295 SER SER A . n 
B 2 296 GLN 296 296 296 GLN GLN A . n 
B 2 297 GLN 297 297 297 GLN GLN A . n 
B 2 298 GLN 298 298 298 GLN GLN A . n 
B 2 299 VAL 299 299 299 VAL VAL A . n 
B 2 300 LEU 300 300 300 LEU LEU A . n 
B 2 301 LYS 301 301 301 LYS LYS A . n 
B 2 302 ALA 302 302 302 ALA ALA A . n 
B 2 303 LEU 303 303 303 LEU LEU A . n 
B 2 304 GLN 304 304 304 GLN GLN A . n 
B 2 305 LYS 305 305 305 LYS LYS A . n 
B 2 306 ASN 306 306 306 ASN ASN A . n 
B 2 307 ASN 307 307 307 ASN ASN A . n 
B 2 308 VAL 308 308 308 VAL VAL A . n 
B 2 309 ARG 309 309 309 ARG ARG A . n 
B 2 310 ASP 310 310 310 ASP ASP A . n 
B 2 311 ILE 311 311 311 ILE ILE A . n 
B 2 312 SER 312 312 312 SER SER A . n 
B 2 313 ASN 313 313 313 ASN ASN A . n 
B 2 314 LYS 314 314 314 LYS LYS A . n 
B 2 315 LEU 315 315 315 LEU LEU A . n 
B 2 316 ILE 316 316 316 ILE ILE A . n 
B 2 317 GLU 317 317 317 GLU GLU A . n 
B 2 318 ASN 318 318 318 ASN ASN A . n 
B 2 319 THR 319 319 319 THR THR A . n 
B 2 320 SER 320 320 320 SER SER A . n 
B 2 321 ASP 321 321 321 ASP ASP A . n 
B 2 322 SER 322 322 322 SER SER A . n 
B 2 323 ASN 323 323 323 ASN ASN A . n 
B 2 324 LEU 324 324 324 LEU LEU A . n 
B 2 325 LYS 325 325 325 LYS LYS A . n 
B 2 326 ASN 326 326 326 ASN ASN A . n 
B 2 327 PHE 327 327 327 PHE PHE A . n 
B 2 328 LEU 328 328 328 LEU LEU A . n 
B 2 329 ASN 329 329 329 ASN ASN A . n 
B 2 330 HIS 330 330 330 HIS HIS A . n 
B 2 331 GLU 331 331 331 GLU GLU A . n 
B 2 332 GLU 332 332 332 GLU GLU A . n 
B 2 333 ILE 333 333 333 ILE ILE A . n 
B 2 334 ILE 334 334 334 ILE ILE A . n 
B 2 335 SER 335 335 335 SER SER A . n 
B 2 336 LEU 336 336 336 LEU LEU A . n 
B 2 337 ARG 337 337 337 ARG ARG A . n 
B 2 338 ASN 338 338 338 ASN ASN A . n 
B 2 339 TYR 339 339 339 TYR TYR A . n 
B 2 340 ARG 340 340 340 ARG ARG A . n 
B 2 341 ARG 341 341 341 ARG ARG A . n 
B 2 342 LEU 342 342 342 LEU LEU A . n 
B 2 343 TYR 343 343 343 TYR TYR A . n 
B 2 344 LYS 344 344 344 LYS LYS A . n 
B 2 345 LEU 345 345 345 LEU LEU A . n 
B 2 346 TYR 346 346 346 TYR TYR A . n 
B 2 347 SER 347 347 347 SER SER A . n 
B 2 348 ALA 348 348 348 ALA ALA A . n 
B 2 349 PHE 349 349 349 PHE PHE A . n 
B 2 350 TYR 350 350 350 TYR TYR A . n 
B 2 351 LEU 351 351 351 LEU LEU A . n 
B 2 352 LYS 352 352 352 LYS LYS A . n 
B 2 353 LEU 353 353 353 LEU LEU A . n 
B 2 354 PRO 354 354 354 PRO PRO A . n 
B 2 355 LEU 355 355 355 LEU LEU A . n 
B 2 356 HIS 356 356 356 HIS HIS A . n 
B 2 357 ILE 357 357 357 ILE ILE A . n 
B 2 358 ASN 358 358 358 ASN ASN A . n 
B 2 359 THR 359 359 359 THR THR A . n 
B 2 360 LYS 360 360 360 LYS LYS A . n 
B 2 361 THR 361 361 361 THR THR A . n 
B 2 362 ASN 362 362 362 ASN ASN A . n 
B 2 363 LYS 363 363 363 LYS LYS A . n 
B 2 364 ILE 364 364 364 ILE ILE A . n 
B 2 365 HIS 365 365 365 HIS HIS A . n 
B 2 366 THR 366 366 366 THR THR A . n 
B 2 367 THR 367 367 367 THR THR A . n 
B 2 368 PHE 368 368 368 PHE PHE A . n 
B 2 369 ASN 369 369 369 ASN ASN A . n 
B 2 370 GLN 370 370 370 GLN GLN A . n 
B 2 371 LEU 371 371 371 LEU LEU A . n 
B 2 372 LYS 372 372 372 LYS LYS A . n 
B 2 373 THR 373 373 373 THR THR A . n 
B 2 374 PHE 374 374 374 PHE PHE A . n 
B 2 375 SER 375 375 375 SER SER A . n 
B 2 376 GLY 376 376 376 GLY GLY A . n 
B 2 377 ARG 377 377 377 ARG ARG A . n 
B 2 378 PHE 378 378 378 PHE PHE A . n 
B 2 379 SER 379 379 379 SER SER A . n 
B 2 380 SER 380 380 380 SER SER A . n 
B 2 381 GLU 381 381 381 GLU GLU A . n 
B 2 382 LYS 382 382 382 LYS LYS A . n 
B 2 383 PRO 383 383 383 PRO PRO A . n 
B 2 384 ASN 384 384 384 ASN ASN A . n 
B 2 385 LEU 385 385 385 LEU LEU A . n 
B 2 386 GLN 386 386 386 GLN GLN A . n 
B 2 387 GLN 387 387 387 GLN GLN A . n 
B 2 388 ILE 388 388 388 ILE ILE A . n 
B 2 389 PRO 389 389 389 PRO PRO A . n 
B 2 390 ARG 390 390 390 ARG ARG A . n 
B 2 391 GLN 391 391 391 GLN GLN A . n 
B 2 392 LYS 392 392 392 LYS LYS A . n 
B 2 393 ASN 393 393 393 ASN ASN A . n 
B 2 394 ILE 394 394 394 ILE ILE A . n 
B 2 395 ARG 395 395 395 ARG ARG A . n 
B 2 396 GLU 396 396 396 GLU GLU A . n 
B 2 397 ILE 397 397 397 ILE ILE A . n 
B 2 398 PHE 398 398 398 PHE PHE A . n 
B 2 399 ILE 399 399 399 ILE ILE A . n 
B 2 400 PRO 400 400 400 PRO PRO A . n 
B 2 401 ASN 401 401 401 ASN ASN A . n 
B 2 402 ASP 402 402 402 ASP ASP A . n 
B 2 403 ASN 403 403 403 ASN ASN A . n 
B 2 404 ASN 404 404 404 ASN ASN A . n 
B 2 405 ILE 405 405 405 ILE ILE A . n 
B 2 406 PHE 406 406 406 PHE PHE A . n 
B 2 407 ILE 407 407 407 ILE ILE A . n 
B 2 408 ILE 408 408 408 ILE ILE A . n 
B 2 409 ALA 409 409 409 ALA ALA A . n 
B 2 410 ASP 410 410 410 ASP ASP A . n 
B 2 411 PHE 411 411 411 PHE PHE A . n 
B 2 412 LYS 412 412 412 LYS LYS A . n 
B 2 413 GLN 413 413 413 GLN GLN A . n 
B 2 414 ILE 414 414 414 ILE ILE A . n 
B 2 415 GLU 415 415 415 GLU GLU A . n 
B 2 416 LEU 416 416 416 LEU LEU A . n 
B 2 417 LYS 417 417 417 LYS LYS A . n 
B 2 418 ILE 418 418 418 ILE ILE A . n 
B 2 419 ALA 419 419 419 ALA ALA A . n 
B 2 420 ALA 420 420 420 ALA ALA A . n 
B 2 421 GLU 421 421 421 GLU GLU A . n 
B 2 422 ILE 422 422 422 ILE ILE A . n 
B 2 423 THR 423 423 423 THR THR A . n 
B 2 424 ASN 424 424 424 ASN ASN A . n 
B 2 425 ASP 425 425 425 ASP ASP A . n 
B 2 426 GLU 426 426 426 GLU GLU A . n 
B 2 427 ILE 427 427 427 ILE ILE A . n 
B 2 428 MET 428 428 428 MET MET A . n 
B 2 429 LEU 429 429 429 LEU LEU A . n 
B 2 430 LYS 430 430 430 LYS LYS A . n 
B 2 431 ALA 431 431 431 ALA ALA A . n 
B 2 432 TYR 432 432 432 TYR TYR A . n 
B 2 433 ASN 433 433 433 ASN ASN A . n 
B 2 434 ASN 434 434 434 ASN ASN A . n 
B 2 435 ASN 435 435 435 ASN ASN A . n 
B 2 436 ILE 436 436 436 ILE ILE A . n 
B 2 437 ASP 437 437 437 ASP ASP A . n 
B 2 438 LEU 438 438 438 LEU LEU A . n 
B 2 439 HIS 439 439 439 HIS HIS A . n 
B 2 440 THR 440 440 440 THR THR A . n 
B 2 441 LEU 441 441 441 LEU LEU A . n 
B 2 442 THR 442 442 442 THR THR A . n 
B 2 443 ALA 443 443 443 ALA ALA A . n 
B 2 444 SER 444 444 444 SER SER A . n 
B 2 445 ILE 445 445 445 ILE ILE A . n 
B 2 446 ILE 446 446 446 ILE ILE A . n 
B 2 447 THR 447 447 447 THR THR A . n 
B 2 448 LYS 448 448 448 LYS LYS A . n 
B 2 449 LYS 449 449 449 LYS LYS A . n 
B 2 450 ASN 450 450 450 ASN ASN A . n 
B 2 451 ILE 451 451 451 ILE ILE A . n 
B 2 452 PRO 452 452 452 PRO PRO A . n 
B 2 453 ASP 453 453 453 ASP ASP A . n 
B 2 454 ILE 454 454 454 ILE ILE A . n 
B 2 455 ASN 455 455 455 ASN ASN A . n 
B 2 456 LYS 456 456 456 LYS LYS A . n 
B 2 457 GLU 457 457 457 GLU GLU A . n 
B 2 458 ASP 458 458 458 ASP ASP A . n 
B 2 459 ARG 459 459 459 ARG ARG A . n 
B 2 460 HIS 460 460 460 HIS HIS A . n 
B 2 461 ILE 461 461 461 ILE ILE A . n 
B 2 462 ALA 462 462 462 ALA ALA A . n 
B 2 463 LYS 463 463 463 LYS LYS A . n 
B 2 464 ALA 464 464 464 ALA ALA A . n 
B 2 465 ILE 465 465 465 ILE ILE A . n 
B 2 466 ASN 466 466 466 ASN ASN A . n 
B 2 467 PHE 467 467 467 PHE PHE A . n 
B 2 468 GLY 468 468 468 GLY GLY A . n 
B 2 469 LEU 469 469 469 LEU LEU A . n 
B 2 470 ILE 470 470 470 ILE ILE A . n 
B 2 471 TYR 471 471 471 TYR TYR A . n 
B 2 472 GLY 472 472 472 GLY GLY A . n 
B 2 473 MET 473 473 473 MET MET A . n 
B 2 474 ASN 474 474 474 ASN ASN A . n 
B 2 475 TYR 475 475 475 TYR TYR A . n 
B 2 476 VAL 476 476 476 VAL VAL A . n 
B 2 477 ASN 477 477 477 ASN ASN A . n 
B 2 478 LEU 478 478 478 LEU LEU A . n 
B 2 479 LYS 479 479 479 LYS LYS A . n 
B 2 480 ASN 480 480 480 ASN ASN A . n 
B 2 481 TYR 481 481 481 TYR TYR A . n 
B 2 482 ALA 482 482 482 ALA ALA A . n 
B 2 483 ASN 483 483 483 ASN ASN A . n 
B 2 484 THR 484 484 484 THR THR A . n 
B 2 485 TYR 485 485 485 TYR TYR A . n 
B 2 486 TYR 486 486 486 TYR TYR A . n 
B 2 487 GLY 487 487 487 GLY GLY A . n 
B 2 488 LEU 488 488 488 LEU LEU A . n 
B 2 489 ASN 489 489 489 ASN ASN A . n 
B 2 490 MET 490 490 490 MET MET A . n 
B 2 491 SER 491 491 491 SER SER A . n 
B 2 492 LEU 492 492 492 LEU LEU A . n 
B 2 493 ASP 493 493 493 ASP ASP A . n 
B 2 494 GLN 494 494 494 GLN GLN A . n 
B 2 495 CYS 495 495 495 CYS CYS A . n 
B 2 496 LEU 496 496 496 LEU LEU A . n 
B 2 497 TYR 497 497 497 TYR TYR A . n 
B 2 498 PHE 498 498 498 PHE PHE A . n 
B 2 499 TYR 499 499 499 TYR TYR A . n 
B 2 500 ASN 500 500 500 ASN ASN A . n 
B 2 501 SER 501 501 501 SER SER A . n 
B 2 502 PHE 502 502 502 PHE PHE A . n 
B 2 503 PHE 503 503 503 PHE PHE A . n 
B 2 504 GLU 504 504 504 GLU GLU A . n 
B 2 505 HIS 505 505 505 HIS HIS A . n 
B 2 506 TYR 506 506 506 TYR TYR A . n 
B 2 507 LYS 507 507 507 LYS LYS A . n 
B 2 508 GLY 508 508 508 GLY GLY A . n 
B 2 509 ILE 509 509 509 ILE ILE A . n 
B 2 510 TYR 510 510 510 TYR TYR A . n 
B 2 511 LYS 511 511 511 LYS LYS A . n 
B 2 512 TRP 512 512 512 TRP TRP A . n 
B 2 513 HIS 513 513 513 HIS HIS A . n 
B 2 514 ASN 514 514 514 ASN ASN A . n 
B 2 515 GLN 515 515 515 GLN GLN A . n 
B 2 516 VAL 516 516 516 VAL VAL A . n 
B 2 517 LYS 517 517 517 LYS LYS A . n 
B 2 518 GLN 518 518 518 GLN GLN A . n 
B 2 519 LYS 519 519 519 LYS LYS A . n 
B 2 520 ARG 520 520 520 ARG ARG A . n 
B 2 521 ALA 521 521 521 ALA ALA A . n 
B 2 522 LEU 522 522 522 LEU LEU A . n 
B 2 523 GLN 523 523 523 GLN GLN A . n 
B 2 524 TYR 524 524 524 TYR TYR A . n 
B 2 525 SER 525 525 525 SER SER A . n 
B 2 526 THR 526 526 526 THR THR A . n 
B 2 527 LEU 527 527 527 LEU LEU A . n 
B 2 528 SER 528 528 528 SER SER A . n 
B 2 529 ASN 529 529 529 ASN ASN A . n 
B 2 530 ARG 530 530 530 ARG ARG A . n 
B 2 531 LYS 531 531 531 LYS LYS A . n 
B 2 532 VAL 532 532 532 VAL VAL A . n 
B 2 533 ILE 533 533 533 ILE ILE A . n 
B 2 534 PHE 534 534 534 PHE PHE A . n 
B 2 535 PRO 535 535 535 PRO PRO A . n 
B 2 536 TYR 536 536 536 TYR TYR A . n 
B 2 537 PHE 537 537 537 PHE PHE A . n 
B 2 538 SER 538 538 538 SER SER A . n 
B 2 539 PHE 539 539 539 PHE PHE A . n 
B 2 540 THR 540 540 540 THR THR A . n 
B 2 541 LYS 541 541 541 LYS LYS A . n 
B 2 542 ALA 542 542 542 ALA ALA A . n 
B 2 543 LEU 543 543 543 LEU LEU A . n 
B 2 544 ASN 544 544 544 ASN ASN A . n 
B 2 545 TYR 545 545 545 TYR TYR A . n 
B 2 546 PRO 546 546 546 PRO PRO A . n 
B 2 547 VAL 547 547 547 VAL VAL A . n 
B 2 548 GLN 548 548 548 GLN GLN A . n 
B 2 549 GLY 549 549 549 GLY GLY A . n 
B 2 550 THR 550 550 550 THR THR A . n 
B 2 551 CYS 551 551 551 CYS CYS A . n 
B 2 552 ALA 552 552 552 ALA ALA A . n 
B 2 553 ASP 553 553 553 ASP ASP A . n 
B 2 554 ILE 554 554 554 ILE ILE A . n 
B 2 555 LEU 555 555 555 LEU LEU A . n 
B 2 556 LYS 556 556 556 LYS LYS A . n 
B 2 557 LEU 557 557 557 LEU LEU A . n 
B 2 558 ALA 558 558 558 ALA ALA A . n 
B 2 559 LEU 559 559 559 LEU LEU A . n 
B 2 560 VAL 560 560 560 VAL VAL A . n 
B 2 561 ASP 561 561 561 ASP ASP A . n 
B 2 562 LEU 562 562 562 LEU LEU A . n 
B 2 563 TYR 563 563 563 TYR TYR A . n 
B 2 564 ASP 564 564 564 ASP ASP A . n 
B 2 565 ASN 565 565 565 ASN ASN A . n 
B 2 566 LEU 566 566 566 LEU LEU A . n 
B 2 567 LYS 567 567 567 LYS LYS A . n 
B 2 568 ASP 568 568 568 ASP ASP A . n 
B 2 569 ILE 569 569 569 ILE ILE A . n 
B 2 570 ASN 570 570 570 ASN ASN A . n 
B 2 571 GLY 571 571 571 GLY GLY A . n 
B 2 572 LYS 572 572 572 LYS LYS A . n 
B 2 573 ILE 573 573 573 ILE ILE A . n 
B 2 574 ILE 574 574 574 ILE ILE A . n 
B 2 575 LEU 575 575 575 LEU LEU A . n 
B 2 576 CYS 576 576 576 CYS CYS A . n 
B 2 577 VAL 577 577 577 VAL VAL A . n 
B 2 578 HIS 578 578 578 HIS HIS A . n 
B 2 579 ASP 579 579 579 ASP ASP A . n 
B 2 580 GLU 580 580 580 GLU GLU A . n 
B 2 581 ILE 581 581 581 ILE ILE A . n 
B 2 582 ILE 582 582 582 ILE ILE A . n 
B 2 583 ILE 583 583 583 ILE ILE A . n 
B 2 584 GLU 584 584 584 GLU GLU A . n 
B 2 585 VAL 585 585 585 VAL VAL A . n 
B 2 586 ASN 586 586 586 ASN ASN A . n 
B 2 587 LYS 587 587 587 LYS LYS A . n 
B 2 588 LYS 588 588 588 LYS LYS A . n 
B 2 589 PHE 589 589 589 PHE PHE A . n 
B 2 590 GLN 590 590 590 GLN GLN A . n 
B 2 591 GLU 591 591 591 GLU GLU A . n 
B 2 592 GLU 592 592 592 GLU GLU A . n 
B 2 593 ALA 593 593 593 ALA ALA A . n 
B 2 594 LEU 594 594 594 LEU LEU A . n 
B 2 595 LYS 595 595 595 LYS LYS A . n 
B 2 596 ILE 596 596 596 ILE ILE A . n 
B 2 597 LEU 597 597 597 LEU LEU A . n 
B 2 598 VAL 598 598 598 VAL VAL A . n 
B 2 599 GLN 599 599 599 GLN GLN A . n 
B 2 600 SER 600 600 600 SER SER A . n 
B 2 601 MET 601 601 601 MET MET A . n 
B 2 602 GLU 602 602 602 GLU GLU A . n 
B 2 603 ASN 603 603 603 ASN ASN A . n 
B 2 604 SER 604 604 604 SER SER A . n 
B 2 605 ALA 605 605 605 ALA ALA A . n 
B 2 606 SER 606 606 606 SER SER A . n 
B 2 607 TYR 607 607 607 TYR TYR A . n 
B 2 608 PHE 608 608 608 PHE PHE A . n 
B 2 609 LEU 609 609 609 LEU LEU A . n 
B 2 610 LYS 610 610 610 LYS LYS A . n 
B 2 611 LYS 611 611 611 LYS LYS A . n 
B 2 612 VAL 612 612 612 VAL VAL A . n 
B 2 613 LYS 613 613 613 LYS LYS A . n 
B 2 614 CYS 614 614 614 CYS CYS A . n 
B 2 615 GLU 615 615 615 GLU GLU A . n 
B 2 616 VAL 616 616 616 VAL VAL A . n 
B 2 617 SER 617 617 617 SER SER A . n 
B 2 618 VAL 618 618 618 VAL VAL A . n 
B 2 619 LYS 619 619 619 LYS LYS A . n 
B 2 620 ILE 620 620 620 ILE ILE A . n 
B 2 621 ALA 621 621 621 ALA ALA A . n 
B 2 622 GLU 622 622 622 GLU GLU A . n 
B 2 623 ASN 623 623 623 ASN ASN A . n 
B 2 624 TRP 624 624 624 TRP TRP A . n 
B 2 625 GLY 625 625 625 GLY GLY A . n 
B 2 626 SER 626 626 626 SER SER A . n 
B 2 627 LYS 627 627 627 LYS LYS A . n 
B 2 628 ASP 628 628 ?   ?   ?   A . n 
C 3 1   DT  1   1   ?   ?   ?   F . n 
C 3 2   DG  2   2   ?   ?   ?   F . n 
C 3 3   DA  3   3   ?   ?   ?   F . n 
C 3 4   DT  4   4   4   DT  DT  F . n 
C 3 5   DG  5   5   5   DG  DG  F . n 
C 3 6   DT  6   6   6   DT  DT  F . n 
C 3 7   DG  7   7   7   DG  DG  F . n 
C 3 8   DA  8   8   8   DA  DA  F . n 
C 3 9   DG  9   9   9   DG  DG  F . n 
C 3 10  DG  10  10  10  DG  DG  F . n 
C 3 11  DC  11  11  11  DC  DC  F . n 
C 3 12  DA  12  12  12  DA  DA  F . n 
C 3 13  DT  13  13  13  DT  DT  F . n 
C 3 14  DC  14  14  14  DC  DC  F . n 
C 3 15  DC  15  15  15  DC  DC  F . n 
C 3 16  DG  16  16  16  DG  DG  F . n 
C 3 17  DT  17  17  17  DT  DT  F . n 
C 3 18  DA  18  18  18  DA  DA  F . n 
C 3 19  DG  19  19  19  DG  DG  F . n 
C 3 20  2DA 20  20  20  2DA 2DA F . 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 2DA ? ? 2DA ? ? 'SUBJECT OF INVESTIGATION' ? 
2 DGT ? ? DGT ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MG  ? ? MG  ? ? '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 
D 4 MG  1 701 2802 MG  MG  A . 
E 5 DGT 1 702 2801 DGT DGT A . 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CAY 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9CAY 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_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                   9CAY 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9CAY 
_struct.title                        'Ternary structure of Plasmodium falciparum apicoplast DNA polymerase (exo-minus)' 
_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        9CAY 
_struct_keywords.text            'DNA polymerase, DNA BINDING PROTEIN, DNA BINDING PROTEIN-DNA complex' 
_struct_keywords.pdbx_keywords   'DNA BINDING PROTEIN/DNA' 
# 
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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
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 PDB 9CAY         9CAY   ? 1 ? 1    
2 UNP Q8ILY1_PLAF7 Q8ILY1 ? 2 
;DEITKKYIKDNIINVDDNIIKKKDIFKLKNENNEITECAFEYFESKKKFDDDIESRFFIINDNNYNENINLIYKDIKYCG
LDIETTGLEVFDENIRLIQIAVENYPVIIYDMFNINKKDILDGLRKVLENKNIIKIIQNGKFDAKFLLHNNFKIENIFDT
YIASKLLDKNKNMYGFKLNNIVEKYLNVILDKQQQNSVWNNSLLNNNQLFYAARDSSCLLKLYKKLKEEIKKENLHIVND
IENKCILPICDMELNGIKVDLENLQKSTNEILNELNIEKDNLKKKLKDENINVNSQQQVLKALQKNNVRDISNKLIENTS
DSNLKNFLNHEEIISLRNYRRLYKLYSAFYLKLPLHINTKTNKIHTTFNQLKTFSGRFSSEKPNLQQIPRQKNIREIFIP
NDNNIFIIADFKQIELKIAAEITNDEIMLKAYNNNIDLHTLTASIITKKNIPDINKEDRHIAKAINFGLIYGMNYVNLKN
YANTYYGLNMSLDQCLYFYNSFFEHYKGIYKWHNQVKQKRALQYSTLSNRKVIFPYFSFTKALNYPVQGTCADILKLALV
DLYDNLKDINGKIILCVHDEIIIEVNKKFQEEALKILVQSMENSASYFLKKVKCEVSVKIAENWGSKD
;
1389 
3 PDB 9CAY         9CAY   ? 3 ? 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 9CAY E 1 ? 29  ? 9CAY   1    ? 29   ? 1 29  
2 2 9CAY A 1 ? 628 ? Q8ILY1 1389 ? 2016 ? 1 628 
3 3 9CAY F 1 ? 20  ? 9CAY   1    ? 20   ? 1 20  
# 
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 
2 9CAY ASN A 82 ? UNP Q8ILY1 ASP 1470 'engineered mutation' 82 1 
2 9CAY GLN A 84 ? UNP Q8ILY1 GLU 1472 'engineered mutation' 84 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
_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 
# 
_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   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 ASN B 68  ? LYS B 74  ? ASN A 68  LYS A 74  5 ? 7  
HELX_P HELX_P2  AA2 ASP B 122 ? ASN B 130 ? ASP A 122 ASN A 130 1 ? 9  
HELX_P HELX_P3  AA3 PHE B 142 ? ASN B 150 ? PHE A 142 ASN A 150 1 ? 9  
HELX_P HELX_P4  AA4 THR B 160 ? LEU B 166 ? THR A 160 LEU A 166 1 ? 7  
HELX_P HELX_P5  AA5 LEU B 219 ? LYS B 232 ? LEU A 219 LYS A 232 1 ? 14 
HELX_P HELX_P6  AA6 LEU B 235 ? GLY B 256 ? LEU A 235 GLY A 256 1 ? 22 
HELX_P HELX_P7  AA7 ASP B 260 ? LYS B 287 ? ASP A 260 LYS A 287 1 ? 28 
HELX_P HELX_P8  AA8 SER B 295 ? LYS B 305 ? SER A 295 LYS A 305 1 ? 11 
HELX_P HELX_P9  AA9 SER B 320 ? PHE B 327 ? SER A 320 PHE A 327 1 ? 8  
HELX_P HELX_P10 AB1 GLU B 332 ? ALA B 348 ? GLU A 332 ALA A 348 1 ? 17 
HELX_P HELX_P11 AB2 LEU B 353 ? ILE B 357 ? LEU A 353 ILE A 357 5 ? 5  
HELX_P HELX_P12 AB3 ASN B 384 ? ILE B 388 ? ASN A 384 ILE A 388 5 ? 5  
HELX_P HELX_P13 AB4 GLN B 391 ? GLU B 396 ? GLN A 391 GLU A 396 1 ? 6  
HELX_P HELX_P14 AB5 LYS B 417 ? ASN B 424 ? LYS A 417 ASN A 424 1 ? 8  
HELX_P HELX_P15 AB6 ASP B 425 ? ASN B 434 ? ASP A 425 ASN A 434 1 ? 10 
HELX_P HELX_P16 AB7 ASP B 437 ? ILE B 446 ? ASP A 437 ILE A 446 1 ? 10 
HELX_P HELX_P17 AB8 ASN B 455 ? GLY B 472 ? ASN A 455 GLY A 472 1 ? 18 
HELX_P HELX_P18 AB9 ASN B 474 ? TYR B 486 ? ASN A 474 TYR A 486 1 ? 13 
HELX_P HELX_P19 AC1 SER B 491 ? TYR B 506 ? SER A 491 TYR A 506 1 ? 16 
HELX_P HELX_P20 AC2 TYR B 506 ? LYS B 519 ? TYR A 506 LYS A 519 1 ? 14 
HELX_P HELX_P21 AC3 SER B 538 ? LEU B 566 ? SER A 538 LEU A 566 1 ? 29 
HELX_P HELX_P22 AC4 LYS B 567 ? ASN B 570 ? LYS A 567 ASN A 570 5 ? 4  
HELX_P HELX_P23 AC5 PHE B 589 ? TYR B 607 ? PHE A 589 TYR A 607 1 ? 19 
# 
_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 
covale1  covale both ? C DG  19  "O3'" ? ? ? 1_555 C 2DA 20 P   ? ? F DG  19  F 2DA 20  1_555 ? ? ? ? ? ? ?            1.606 ? ? 
metalc1  metalc ?    ? B ASP 410 OD1   ? ? ? 1_555 D MG  .  MG  B ? A ASP 410 A MG  701 1_555 ? ? ? ? ? ? ?            2.172 ? ? 
metalc2  metalc ?    ? B PHE 411 O     ? ? ? 1_555 D MG  .  MG  B ? A PHE 411 A MG  701 1_555 ? ? ? ? ? ? ?            2.796 ? ? 
metalc3  metalc ?    ? B ASP 579 OD2   ? ? ? 1_555 D MG  .  MG  B ? A ASP 579 A MG  701 1_555 ? ? ? ? ? ? ?            2.566 ? ? 
metalc4  metalc ?    ? D MG  .   MG    B ? ? 1_555 E DGT .  O3G ? ? A MG  701 A DGT 702 1_555 ? ? ? ? ? ? ?            2.519 ? ? 
metalc5  metalc ?    ? D MG  .   MG    B ? ? 1_555 E DGT .  O2B ? ? A MG  701 A DGT 702 1_555 ? ? ? ? ? ? ?            2.821 ? ? 
metalc6  metalc ?    ? D MG  .   MG    B ? ? 1_555 E DGT .  O2A ? ? A MG  701 A DGT 702 1_555 ? ? ? ? ? ? ?            2.743 ? ? 
hydrog1  hydrog ?    ? A DT  10  N3    ? ? ? 1_555 C 2DA 20 N1  ? ? E DT  10  F 2DA 20  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog2  hydrog ?    ? A DT  10  O4    ? ? ? 1_555 C 2DA 20 N6  ? ? E DT  10  F 2DA 20  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog3  hydrog ?    ? A DC  11  N3    ? ? ? 1_555 C DG  19 N1  ? ? E DC  11  F DG  19  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog4  hydrog ?    ? A DC  11  N4    ? ? ? 1_555 C DG  19 O6  ? ? E DC  11  F DG  19  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog5  hydrog ?    ? A DC  11  O2    ? ? ? 1_555 C DG  19 N2  ? ? E DC  11  F DG  19  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog6  hydrog ?    ? A DT  12  N3    ? ? ? 1_555 C DA  18 N1  ? ? E DT  12  F DA  18  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog7  hydrog ?    ? A DT  12  O4    ? ? ? 1_555 C DA  18 N6  ? ? E DT  12  F DA  18  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog8  hydrog ?    ? A DC  14  N3    ? ? ? 1_555 C DG  16 N1  ? ? E DC  14  F DG  16  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog9  hydrog ?    ? A DC  14  N4    ? ? ? 1_555 C DG  16 O6  ? ? E DC  14  F DG  16  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog10 hydrog ?    ? A DC  14  O2    ? ? ? 1_555 C DG  16 N2  ? ? E DC  14  F DG  16  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog11 hydrog ?    ? A DG  15  N1    ? ? ? 1_555 C DC  15 N3  ? ? E DG  15  F DC  15  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog12 hydrog ?    ? A DG  15  N2    ? ? ? 1_555 C DC  15 O2  ? ? E DG  15  F DC  15  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog13 hydrog ?    ? A DG  15  O6    ? ? ? 1_555 C DC  15 N4  ? ? E DG  15  F DC  15  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog14 hydrog ?    ? A DG  16  N1    ? ? ? 1_555 C DC  14 N3  ? ? E DG  16  F DC  14  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog15 hydrog ?    ? A DG  16  N2    ? ? ? 1_555 C DC  14 O2  ? ? E DG  16  F DC  14  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog16 hydrog ?    ? A DG  16  O6    ? ? ? 1_555 C DC  14 N4  ? ? E DG  16  F DC  14  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog17 hydrog ?    ? A DA  17  N1    ? ? ? 1_555 C DA  12 N6  ? ? E DA  17  F DA  12  1_555 ? ? ? ? ? ? TYPE_1_PAIR  ?     ? ? 
hydrog18 hydrog ?    ? A DA  17  N6    ? ? ? 1_555 C DA  12 N1  ? ? E DA  17  F DA  12  1_555 ? ? ? ? ? ? TYPE_1_PAIR  ?     ? ? 
hydrog19 hydrog ?    ? A DA  17  N1    ? ? ? 1_555 C DT  13 N3  ? ? E DA  17  F DT  13  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog20 hydrog ?    ? A DA  17  N6    ? ? ? 1_555 C DT  13 O4  ? ? E DA  17  F DT  13  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog21 hydrog ?    ? A DT  18  N3    ? ? ? 1_555 C DC  11 N3  ? ? E DT  18  F DC  11  1_555 ? ? ? ? ? ? TYPE_18_PAIR ?     ? ? 
hydrog22 hydrog ?    ? A DT  18  O4    ? ? ? 1_555 C DC  11 N4  ? ? E DT  18  F DC  11  1_555 ? ? ? ? ? ? TYPE_18_PAIR ?     ? ? 
hydrog23 hydrog ?    ? A DT  18  N3    ? ? ? 1_555 C DA  12 N1  ? ? E DT  18  F DA  12  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog24 hydrog ?    ? A DT  18  O4    ? ? ? 1_555 C DA  12 N6  ? ? E DT  18  F DA  12  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog25 hydrog ?    ? A DG  19  N1    ? ? ? 1_555 C DC  11 N3  ? ? E DG  19  F DC  11  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog26 hydrog ?    ? A DG  19  N2    ? ? ? 1_555 C DC  11 O2  ? ? E DG  19  F DC  11  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog27 hydrog ?    ? A DG  19  O6    ? ? ? 1_555 C DC  11 N4  ? ? E DG  19  F DC  11  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog28 hydrog ?    ? A DC  20  N3    ? ? ? 1_555 C DG  10 N1  ? ? E DC  20  F DG  10  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog29 hydrog ?    ? A DC  20  N4    ? ? ? 1_555 C DG  10 O6  ? ? E DC  20  F DG  10  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog30 hydrog ?    ? A DC  20  O2    ? ? ? 1_555 C DG  10 N2  ? ? E DC  20  F DG  10  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog31 hydrog ?    ? A DC  21  N3    ? ? ? 1_555 C DG  9  N1  ? ? E DC  21  F DG  9   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog32 hydrog ?    ? A DC  21  N4    ? ? ? 1_555 C DG  9  O6  ? ? E DC  21  F DG  9   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog33 hydrog ?    ? A DC  21  O2    ? ? ? 1_555 C DG  9  N2  ? ? E DC  21  F DG  9   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog34 hydrog ?    ? A DT  22  N3    ? ? ? 1_555 C DA  8  N1  ? ? E DT  22  F DA  8   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog35 hydrog ?    ? A DT  22  O4    ? ? ? 1_555 C DA  8  N6  ? ? E DT  22  F DA  8   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog36 hydrog ?    ? A DC  23  N3    ? ? ? 1_555 C DG  7  N1  ? ? E DC  23  F DG  7   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog37 hydrog ?    ? A DC  23  N4    ? ? ? 1_555 C DG  7  O6  ? ? E DC  23  F DG  7   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog38 hydrog ?    ? A DC  23  O2    ? ? ? 1_555 C DG  7  N2  ? ? E DC  23  F DG  7   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog39 hydrog ?    ? A DA  24  N1    ? ? ? 1_555 C DT  6  N3  ? ? E DA  24  F DT  6   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog40 hydrog ?    ? A DA  24  N6    ? ? ? 1_555 C DT  6  O4  ? ? E DA  24  F DT  6   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog41 hydrog ?    ? A DC  25  N3    ? ? ? 1_555 C DG  5  N1  ? ? E DC  25  F DG  5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog42 hydrog ?    ? A DC  25  N4    ? ? ? 1_555 C DG  5  O6  ? ? E DC  25  F DG  5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog43 hydrog ?    ? A DC  25  O2    ? ? ? 1_555 C DG  5  N2  ? ? E DC  25  F DG  5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog44 hydrog ?    ? A DA  26  N1    ? ? ? 1_555 C DT  4  N3  ? ? E DA  26  F DT  4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog45 hydrog ?    ? A DA  26  N6    ? ? ? 1_555 C DT  4  O4  ? ? E DA  26  F DT  4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
hydrog ? ? 
# 
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  OD1 ? B ASP 410 ? A ASP 410 ? 1_555 MG B D MG . ? A MG 701 ? 1_555 O   ? B PHE 411 ? A PHE 411 ? 1_555 60.1  ? 
2  OD1 ? B ASP 410 ? A ASP 410 ? 1_555 MG B D MG . ? A MG 701 ? 1_555 OD2 ? B ASP 579 ? A ASP 579 ? 1_555 113.8 ? 
3  O   ? B PHE 411 ? A PHE 411 ? 1_555 MG B D MG . ? A MG 701 ? 1_555 OD2 ? B ASP 579 ? A ASP 579 ? 1_555 110.7 ? 
4  OD1 ? B ASP 410 ? A ASP 410 ? 1_555 MG B D MG . ? A MG 701 ? 1_555 O3G ? E DGT .   ? A DGT 702 ? 1_555 95.7  ? 
5  O   ? B PHE 411 ? A PHE 411 ? 1_555 MG B D MG . ? A MG 701 ? 1_555 O3G ? E DGT .   ? A DGT 702 ? 1_555 73.4  ? 
6  OD2 ? B ASP 579 ? A ASP 579 ? 1_555 MG B D MG . ? A MG 701 ? 1_555 O3G ? E DGT .   ? A DGT 702 ? 1_555 148.4 ? 
7  OD1 ? B ASP 410 ? A ASP 410 ? 1_555 MG B D MG . ? A MG 701 ? 1_555 O2B ? E DGT .   ? A DGT 702 ? 1_555 140.3 ? 
8  O   ? B PHE 411 ? A PHE 411 ? 1_555 MG B D MG . ? A MG 701 ? 1_555 O2B ? E DGT .   ? A DGT 702 ? 1_555 81.5  ? 
9  OD2 ? B ASP 579 ? A ASP 579 ? 1_555 MG B D MG . ? A MG 701 ? 1_555 O2B ? E DGT .   ? A DGT 702 ? 1_555 87.5  ? 
10 O3G ? E DGT .   ? A DGT 702 ? 1_555 MG B D MG . ? A MG 701 ? 1_555 O2B ? E DGT .   ? A DGT 702 ? 1_555 61.6  ? 
11 OD1 ? B ASP 410 ? A ASP 410 ? 1_555 MG B D MG . ? A MG 701 ? 1_555 O2A ? E DGT .   ? A DGT 702 ? 1_555 124.2 ? 
12 O   ? B PHE 411 ? A PHE 411 ? 1_555 MG B D MG . ? A MG 701 ? 1_555 O2A ? E DGT .   ? A DGT 702 ? 1_555 137.8 ? 
13 OD2 ? B ASP 579 ? A ASP 579 ? 1_555 MG B D MG . ? A MG 701 ? 1_555 O2A ? E DGT .   ? A DGT 702 ? 1_555 104.5 ? 
14 O3G ? E DGT .   ? A DGT 702 ? 1_555 MG B D MG . ? A MG 701 ? 1_555 O2A ? E DGT .   ? A DGT 702 ? 1_555 64.4  ? 
15 O2B ? E DGT .   ? A DGT 702 ? 1_555 MG B D MG . ? A MG 701 ? 1_555 O2A ? E DGT .   ? A DGT 702 ? 1_555 77.3  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
AA4 ? 4 ? 
AA5 ? 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 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-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 ILE B 59  ? ILE B 60  ? ILE A 59  ILE A 60  
AA1 2 ILE B 108 ? ASP B 111 ? ILE A 108 ASP A 111 
AA1 3 ILE B 95  ? ILE B 100 ? ILE A 95  ILE A 100 
AA1 4 ASN B 82  ? THR B 85  ? ASN A 82  THR A 85  
AA2 1 LYS B 135 ? ILE B 137 ? LYS A 135 ILE A 137 
AA2 2 ILE B 157 ? ASP B 159 ? ILE A 157 ASP A 159 
AA3 1 LYS B 363 ? ILE B 364 ? LYS A 363 ILE A 364 
AA3 2 ILE B 257 ? VAL B 259 ? ILE A 257 VAL A 259 
AA3 3 PHE B 398 ? ILE B 399 ? PHE A 398 ILE A 399 
AA4 1 LYS B 572 ? VAL B 577 ? LYS A 572 VAL A 577 
AA4 2 GLU B 580 ? ASN B 586 ? GLU A 580 ASN A 586 
AA4 3 ASN B 404 ? PHE B 411 ? ASN A 404 PHE A 411 
AA4 4 VAL B 616 ? ALA B 621 ? VAL A 616 ALA A 621 
AA5 1 GLN B 523 ? TYR B 524 ? GLN A 523 TYR A 524 
AA5 2 VAL B 532 ? ILE B 533 ? VAL A 532 ILE A 533 
# 
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 ILE B 60  ? N ILE A 60  O ILE B 109 ? O ILE A 109 
AA1 2 3 O ILE B 108 ? O ILE A 108 N ILE B 100 ? N ILE A 100 
AA1 3 4 O LEU B 97  ? O LEU A 97  N GLN B 84  ? N GLN A 84  
AA2 1 2 N LYS B 135 ? N LYS A 135 O PHE B 158 ? O PHE A 158 
AA3 1 2 O ILE B 364 ? O ILE A 364 N ILE B 257 ? N ILE A 257 
AA3 2 3 N LYS B 258 ? N LYS A 258 O ILE B 399 ? O ILE A 399 
AA4 1 2 N LYS B 572 ? N LYS A 572 O GLU B 584 ? O GLU A 584 
AA4 2 3 O ILE B 581 ? O ILE A 581 N ALA B 409 ? N ALA A 409 
AA4 3 4 N ASP B 410 ? N ASP A 410 O SER B 617 ? O SER A 617 
AA5 1 2 N TYR B 524 ? N TYR A 524 O VAL B 532 ? O VAL A 532 
# 
_pdbx_entry_details.entry_id                   9CAY 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 "O4'" E DG 16 ? ? "C1'" E DG 16 ? ? N9 E DG  16 ? ? 110.25 108.30 1.95  0.30 N 
2 1 "O4'" F DG 7  ? ? "C1'" F DG 7  ? ? N9 F DG  7  ? ? 111.24 108.30 2.94  0.30 N 
3 1 "C3'" F DA 18 ? ? "O3'" F DA 18 ? ? P  F DG  19 ? ? 111.92 119.70 -7.78 1.20 Y 
4 1 "C3'" F DG 19 ? ? "O3'" F DG 19 ? ? P  F 2DA 20 ? ? 111.23 119.70 -8.47 1.20 Y 
# 
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 GLU A 67  ? ? 72.77   -4.54   
2  1 LYS A 117 ? ? 52.79   -167.92 
3  1 ASP A 119 ? ? 79.11   -7.06   
4  1 LEU A 166 ? ? -92.47  53.55   
5  1 GLU A 289 ? ? 58.22   18.16   
6  1 ASN A 290 ? ? -141.03 25.44   
7  1 LYS A 305 ? ? -87.58  47.72   
8  1 ASN A 307 ? ? 64.77   60.03   
9  1 PHE A 327 ? ? -97.19  34.43   
10 1 LEU A 328 ? ? -75.61  -168.83 
11 1 GLU A 331 ? ? -82.32  47.25   
12 1 PHE A 349 ? ? -122.09 -50.68  
13 1 LYS A 360 ? ? 59.65   5.41    
14 1 PRO A 383 ? ? -38.47  116.19  
15 1 ASN A 403 ? ? 73.78   -7.78   
16 1 LEU A 416 ? ? 73.76   -6.76   
17 1 ASN A 435 ? ? 60.95   61.28   
18 1 THR A 447 ? ? 179.33  -165.71 
19 1 ASN A 450 ? ? 69.57   153.74  
20 1 LEU A 522 ? ? 71.60   -3.35   
21 1 HIS A 578 ? ? 66.89   -26.34  
22 1 ASP A 579 ? ? -155.05 -0.16   
23 1 SER A 626 ? ? -69.02  82.69   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   LYS 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    382 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PRO 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    383 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -149.25 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9CAY 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9CAY 
_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                  3.17 
_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               101542 
_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       ? 
_em_buffer.pH            7.6 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               'MULTIPLE SOURCES' 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Plasmodium falciparum apicoplast DNA polymerase ternary complex' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       2,3 
# 
_em_imaging.entry_id                        9CAY 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             700 
_em_imaging.nominal_defocus_max             3000 
_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             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    GOLD 
_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              9CAY 
_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   295 
_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                9CAY 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
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 E DG  1   ? A DG  1   
2   1 Y 1 E DC  2   ? A DC  2   
3   1 Y 1 E DA  3   ? A DA  3   
4   1 Y 1 E DG  4   ? A DG  4   
5   1 Y 1 E DT  5   ? A DT  5   
6   1 Y 1 E DG  27  ? A DG  27  
7   1 Y 1 E DC  28  ? A DC  28  
8   1 Y 1 E DA  29  ? A DA  29  
9   1 Y 1 A ASP 1   ? B ASP 1   
10  1 Y 1 A GLU 2   ? B GLU 2   
11  1 Y 1 A ILE 3   ? B ILE 3   
12  1 Y 1 A THR 4   ? B THR 4   
13  1 Y 1 A LYS 5   ? B LYS 5   
14  1 Y 1 A LYS 6   ? B LYS 6   
15  1 Y 1 A TYR 7   ? B TYR 7   
16  1 Y 1 A ILE 8   ? B ILE 8   
17  1 Y 1 A LYS 9   ? B LYS 9   
18  1 Y 1 A ASP 10  ? B ASP 10  
19  1 Y 1 A ASN 11  ? B ASN 11  
20  1 Y 1 A ILE 12  ? B ILE 12  
21  1 Y 1 A ILE 13  ? B ILE 13  
22  1 Y 1 A ASN 14  ? B ASN 14  
23  1 Y 1 A VAL 15  ? B VAL 15  
24  1 Y 1 A ASP 16  ? B ASP 16  
25  1 Y 1 A ASP 17  ? B ASP 17  
26  1 Y 1 A ASN 18  ? B ASN 18  
27  1 Y 1 A ILE 19  ? B ILE 19  
28  1 Y 1 A ILE 20  ? B ILE 20  
29  1 Y 1 A LYS 21  ? B LYS 21  
30  1 Y 1 A LYS 22  ? B LYS 22  
31  1 Y 1 A LYS 23  ? B LYS 23  
32  1 Y 1 A ASP 24  ? B ASP 24  
33  1 Y 1 A ILE 25  ? B ILE 25  
34  1 Y 1 A PHE 26  ? B PHE 26  
35  1 Y 1 A LYS 27  ? B LYS 27  
36  1 Y 1 A LEU 28  ? B LEU 28  
37  1 Y 1 A LYS 29  ? B LYS 29  
38  1 Y 1 A ASN 30  ? B ASN 30  
39  1 Y 1 A GLU 31  ? B GLU 31  
40  1 Y 1 A ASN 32  ? B ASN 32  
41  1 Y 1 A ASN 33  ? B ASN 33  
42  1 Y 1 A GLU 34  ? B GLU 34  
43  1 Y 1 A ILE 35  ? B ILE 35  
44  1 Y 1 A THR 36  ? B THR 36  
45  1 Y 1 A GLU 37  ? B GLU 37  
46  1 Y 1 A CYS 38  ? B CYS 38  
47  1 Y 1 A ALA 39  ? B ALA 39  
48  1 Y 1 A PHE 40  ? B PHE 40  
49  1 Y 1 A GLU 41  ? B GLU 41  
50  1 Y 1 A TYR 42  ? B TYR 42  
51  1 Y 1 A PHE 43  ? B PHE 43  
52  1 Y 1 A GLU 44  ? B GLU 44  
53  1 Y 1 A SER 45  ? B SER 45  
54  1 Y 1 A LYS 46  ? B LYS 46  
55  1 Y 1 A LYS 47  ? B LYS 47  
56  1 Y 1 A LYS 48  ? B LYS 48  
57  1 Y 1 A PHE 49  ? B PHE 49  
58  1 Y 1 A ASP 50  ? B ASP 50  
59  1 Y 1 A ASP 51  ? B ASP 51  
60  1 Y 1 A ASP 52  ? B ASP 52  
61  1 Y 1 A ILE 53  ? B ILE 53  
62  1 Y 1 A GLU 54  ? B GLU 54  
63  1 Y 1 A SER 55  ? B SER 55  
64  1 Y 1 A ARG 56  ? B ARG 56  
65  1 Y 1 A LYS 169 ? B LYS 169 
66  1 Y 1 A ASN 170 ? B ASN 170 
67  1 Y 1 A LYS 171 ? B LYS 171 
68  1 Y 1 A ASN 172 ? B ASN 172 
69  1 Y 1 A MET 173 ? B MET 173 
70  1 Y 1 A TYR 174 ? B TYR 174 
71  1 Y 1 A GLY 175 ? B GLY 175 
72  1 Y 1 A PHE 176 ? B PHE 176 
73  1 Y 1 A LYS 177 ? B LYS 177 
74  1 Y 1 A LEU 178 ? B LEU 178 
75  1 Y 1 A ASN 179 ? B ASN 179 
76  1 Y 1 A ASN 180 ? B ASN 180 
77  1 Y 1 A ILE 181 ? B ILE 181 
78  1 Y 1 A VAL 182 ? B VAL 182 
79  1 Y 1 A GLU 183 ? B GLU 183 
80  1 Y 1 A LYS 184 ? B LYS 184 
81  1 Y 1 A TYR 185 ? B TYR 185 
82  1 Y 1 A LEU 186 ? B LEU 186 
83  1 Y 1 A ASN 187 ? B ASN 187 
84  1 Y 1 A VAL 188 ? B VAL 188 
85  1 Y 1 A ILE 189 ? B ILE 189 
86  1 Y 1 A LEU 190 ? B LEU 190 
87  1 Y 1 A ASP 191 ? B ASP 191 
88  1 Y 1 A LYS 192 ? B LYS 192 
89  1 Y 1 A GLN 193 ? B GLN 193 
90  1 Y 1 A GLN 194 ? B GLN 194 
91  1 Y 1 A GLN 195 ? B GLN 195 
92  1 Y 1 A ASN 196 ? B ASN 196 
93  1 Y 1 A SER 197 ? B SER 197 
94  1 Y 1 A VAL 198 ? B VAL 198 
95  1 Y 1 A TRP 199 ? B TRP 199 
96  1 Y 1 A ASN 200 ? B ASN 200 
97  1 Y 1 A ASN 201 ? B ASN 201 
98  1 Y 1 A SER 202 ? B SER 202 
99  1 Y 1 A LEU 203 ? B LEU 203 
100 1 Y 1 A LEU 204 ? B LEU 204 
101 1 Y 1 A ASN 205 ? B ASN 205 
102 1 Y 1 A ASN 206 ? B ASN 206 
103 1 Y 1 A ASN 207 ? B ASN 207 
104 1 Y 1 A GLN 208 ? B GLN 208 
105 1 Y 1 A LEU 209 ? B LEU 209 
106 1 Y 1 A PHE 210 ? B PHE 210 
107 1 Y 1 A TYR 211 ? B TYR 211 
108 1 Y 1 A ALA 212 ? B ALA 212 
109 1 Y 1 A ALA 213 ? B ALA 213 
110 1 Y 1 A ARG 214 ? B ARG 214 
111 1 Y 1 A ASP 215 ? B ASP 215 
112 1 Y 1 A SER 216 ? B SER 216 
113 1 Y 1 A SER 217 ? B SER 217 
114 1 Y 1 A ASP 628 ? B ASP 628 
115 1 Y 1 F DT  1   ? C DT  1   
116 1 Y 1 F DG  2   ? C DG  2   
117 1 Y 1 F DA  3   ? C DA  3   
# 
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 
2DA P      P  N N 1   
2DA OP1    O  N N 2   
2DA OP2    O  N N 3   
2DA OP3    O  N N 4   
2DA "O5'"  O  N N 5   
2DA "C5'"  C  N N 6   
2DA "C4'"  C  N S 7   
2DA "O4'"  O  N N 8   
2DA "C3'"  C  N N 9   
2DA "C2'"  C  N N 10  
2DA "C1'"  C  N R 11  
2DA N9     N  Y N 12  
2DA C8     C  Y N 13  
2DA N7     N  Y N 14  
2DA C5     C  Y N 15  
2DA C6     C  Y N 16  
2DA N6     N  N N 17  
2DA N1     N  Y N 18  
2DA C2     C  Y N 19  
2DA N3     N  Y N 20  
2DA C4     C  Y N 21  
2DA HOP2   H  N N 22  
2DA HOP3   H  N N 23  
2DA "H5'"  H  N N 24  
2DA "H5''" H  N N 25  
2DA "H4'"  H  N N 26  
2DA "H3'1" H  N N 27  
2DA "H3'2" H  N N 28  
2DA "H2'"  H  N N 29  
2DA "H2''" H  N N 30  
2DA "H1'"  H  N N 31  
2DA H8     H  N N 32  
2DA HN61   H  N N 33  
2DA HN62   H  N N 34  
2DA H2     H  N N 35  
ALA N      N  N N 36  
ALA CA     C  N S 37  
ALA C      C  N N 38  
ALA O      O  N N 39  
ALA CB     C  N N 40  
ALA OXT    O  N N 41  
ALA H      H  N N 42  
ALA H2     H  N N 43  
ALA HA     H  N N 44  
ALA HB1    H  N N 45  
ALA HB2    H  N N 46  
ALA HB3    H  N N 47  
ALA HXT    H  N N 48  
ARG N      N  N N 49  
ARG CA     C  N S 50  
ARG C      C  N N 51  
ARG O      O  N N 52  
ARG CB     C  N N 53  
ARG CG     C  N N 54  
ARG CD     C  N N 55  
ARG NE     N  N N 56  
ARG CZ     C  N N 57  
ARG NH1    N  N N 58  
ARG NH2    N  N N 59  
ARG OXT    O  N N 60  
ARG H      H  N N 61  
ARG H2     H  N N 62  
ARG HA     H  N N 63  
ARG HB2    H  N N 64  
ARG HB3    H  N N 65  
ARG HG2    H  N N 66  
ARG HG3    H  N N 67  
ARG HD2    H  N N 68  
ARG HD3    H  N N 69  
ARG HE     H  N N 70  
ARG HH11   H  N N 71  
ARG HH12   H  N N 72  
ARG HH21   H  N N 73  
ARG HH22   H  N N 74  
ARG HXT    H  N N 75  
ASN N      N  N N 76  
ASN CA     C  N S 77  
ASN C      C  N N 78  
ASN O      O  N N 79  
ASN CB     C  N N 80  
ASN CG     C  N N 81  
ASN OD1    O  N N 82  
ASN ND2    N  N N 83  
ASN OXT    O  N N 84  
ASN H      H  N N 85  
ASN H2     H  N N 86  
ASN HA     H  N N 87  
ASN HB2    H  N N 88  
ASN HB3    H  N N 89  
ASN HD21   H  N N 90  
ASN HD22   H  N N 91  
ASN HXT    H  N N 92  
ASP N      N  N N 93  
ASP CA     C  N S 94  
ASP C      C  N N 95  
ASP O      O  N N 96  
ASP CB     C  N N 97  
ASP CG     C  N N 98  
ASP OD1    O  N N 99  
ASP OD2    O  N N 100 
ASP OXT    O  N N 101 
ASP H      H  N N 102 
ASP H2     H  N N 103 
ASP HA     H  N N 104 
ASP HB2    H  N N 105 
ASP HB3    H  N N 106 
ASP HD2    H  N N 107 
ASP HXT    H  N N 108 
CYS N      N  N N 109 
CYS CA     C  N R 110 
CYS C      C  N N 111 
CYS O      O  N N 112 
CYS CB     C  N N 113 
CYS SG     S  N N 114 
CYS OXT    O  N N 115 
CYS H      H  N N 116 
CYS H2     H  N N 117 
CYS HA     H  N N 118 
CYS HB2    H  N N 119 
CYS HB3    H  N N 120 
CYS HG     H  N N 121 
CYS HXT    H  N N 122 
DA  OP3    O  N N 123 
DA  P      P  N N 124 
DA  OP1    O  N N 125 
DA  OP2    O  N N 126 
DA  "O5'"  O  N N 127 
DA  "C5'"  C  N N 128 
DA  "C4'"  C  N R 129 
DA  "O4'"  O  N N 130 
DA  "C3'"  C  N S 131 
DA  "O3'"  O  N N 132 
DA  "C2'"  C  N N 133 
DA  "C1'"  C  N R 134 
DA  N9     N  Y N 135 
DA  C8     C  Y N 136 
DA  N7     N  Y N 137 
DA  C5     C  Y N 138 
DA  C6     C  Y N 139 
DA  N6     N  N N 140 
DA  N1     N  Y N 141 
DA  C2     C  Y N 142 
DA  N3     N  Y N 143 
DA  C4     C  Y N 144 
DA  HOP3   H  N N 145 
DA  HOP2   H  N N 146 
DA  "H5'"  H  N N 147 
DA  "H5''" H  N N 148 
DA  "H4'"  H  N N 149 
DA  "H3'"  H  N N 150 
DA  "HO3'" H  N N 151 
DA  "H2'"  H  N N 152 
DA  "H2''" H  N N 153 
DA  "H1'"  H  N N 154 
DA  H8     H  N N 155 
DA  H61    H  N N 156 
DA  H62    H  N N 157 
DA  H2     H  N N 158 
DC  OP3    O  N N 159 
DC  P      P  N N 160 
DC  OP1    O  N N 161 
DC  OP2    O  N N 162 
DC  "O5'"  O  N N 163 
DC  "C5'"  C  N N 164 
DC  "C4'"  C  N R 165 
DC  "O4'"  O  N N 166 
DC  "C3'"  C  N S 167 
DC  "O3'"  O  N N 168 
DC  "C2'"  C  N N 169 
DC  "C1'"  C  N R 170 
DC  N1     N  N N 171 
DC  C2     C  N N 172 
DC  O2     O  N N 173 
DC  N3     N  N N 174 
DC  C4     C  N N 175 
DC  N4     N  N N 176 
DC  C5     C  N N 177 
DC  C6     C  N N 178 
DC  HOP3   H  N N 179 
DC  HOP2   H  N N 180 
DC  "H5'"  H  N N 181 
DC  "H5''" H  N N 182 
DC  "H4'"  H  N N 183 
DC  "H3'"  H  N N 184 
DC  "HO3'" H  N N 185 
DC  "H2'"  H  N N 186 
DC  "H2''" H  N N 187 
DC  "H1'"  H  N N 188 
DC  H41    H  N N 189 
DC  H42    H  N N 190 
DC  H5     H  N N 191 
DC  H6     H  N N 192 
DG  OP3    O  N N 193 
DG  P      P  N N 194 
DG  OP1    O  N N 195 
DG  OP2    O  N N 196 
DG  "O5'"  O  N N 197 
DG  "C5'"  C  N N 198 
DG  "C4'"  C  N R 199 
DG  "O4'"  O  N N 200 
DG  "C3'"  C  N S 201 
DG  "O3'"  O  N N 202 
DG  "C2'"  C  N N 203 
DG  "C1'"  C  N R 204 
DG  N9     N  Y N 205 
DG  C8     C  Y N 206 
DG  N7     N  Y N 207 
DG  C5     C  Y N 208 
DG  C6     C  N N 209 
DG  O6     O  N N 210 
DG  N1     N  N N 211 
DG  C2     C  N N 212 
DG  N2     N  N N 213 
DG  N3     N  N N 214 
DG  C4     C  Y N 215 
DG  HOP3   H  N N 216 
DG  HOP2   H  N N 217 
DG  "H5'"  H  N N 218 
DG  "H5''" H  N N 219 
DG  "H4'"  H  N N 220 
DG  "H3'"  H  N N 221 
DG  "HO3'" H  N N 222 
DG  "H2'"  H  N N 223 
DG  "H2''" H  N N 224 
DG  "H1'"  H  N N 225 
DG  H8     H  N N 226 
DG  H1     H  N N 227 
DG  H21    H  N N 228 
DG  H22    H  N N 229 
DGT PG     P  N N 230 
DGT O1G    O  N N 231 
DGT O2G    O  N N 232 
DGT O3G    O  N N 233 
DGT O3B    O  N N 234 
DGT PB     P  N S 235 
DGT O1B    O  N N 236 
DGT O2B    O  N N 237 
DGT O3A    O  N N 238 
DGT PA     P  N R 239 
DGT O1A    O  N N 240 
DGT O2A    O  N N 241 
DGT "O5'"  O  N N 242 
DGT "C5'"  C  N N 243 
DGT "C4'"  C  N R 244 
DGT "O4'"  O  N N 245 
DGT "C3'"  C  N S 246 
DGT "O3'"  O  N N 247 
DGT "C2'"  C  N N 248 
DGT "C1'"  C  N R 249 
DGT N9     N  Y N 250 
DGT C8     C  Y N 251 
DGT N7     N  Y N 252 
DGT C5     C  Y N 253 
DGT C6     C  N N 254 
DGT O6     O  N N 255 
DGT N1     N  N N 256 
DGT C2     C  N N 257 
DGT N2     N  N N 258 
DGT N3     N  N N 259 
DGT C4     C  Y N 260 
DGT HO1G   H  N N 261 
DGT HO2G   H  N N 262 
DGT HO1B   H  N N 263 
DGT HO1A   H  N N 264 
DGT "H5'"  H  N N 265 
DGT "H5'A" H  N N 266 
DGT "H4'"  H  N N 267 
DGT "H3'"  H  N N 268 
DGT "HO3'" H  N N 269 
DGT "H2'"  H  N N 270 
DGT "H2'A" H  N N 271 
DGT "H1'"  H  N N 272 
DGT H8     H  N N 273 
DGT HN2    H  N N 274 
DGT HN2A   H  N N 275 
DGT H16    H  N N 276 
DT  OP3    O  N N 277 
DT  P      P  N N 278 
DT  OP1    O  N N 279 
DT  OP2    O  N N 280 
DT  "O5'"  O  N N 281 
DT  "C5'"  C  N N 282 
DT  "C4'"  C  N R 283 
DT  "O4'"  O  N N 284 
DT  "C3'"  C  N S 285 
DT  "O3'"  O  N N 286 
DT  "C2'"  C  N N 287 
DT  "C1'"  C  N R 288 
DT  N1     N  N N 289 
DT  C2     C  N N 290 
DT  O2     O  N N 291 
DT  N3     N  N N 292 
DT  C4     C  N N 293 
DT  O4     O  N N 294 
DT  C5     C  N N 295 
DT  C7     C  N N 296 
DT  C6     C  N N 297 
DT  HOP3   H  N N 298 
DT  HOP2   H  N N 299 
DT  "H5'"  H  N N 300 
DT  "H5''" H  N N 301 
DT  "H4'"  H  N N 302 
DT  "H3'"  H  N N 303 
DT  "HO3'" H  N N 304 
DT  "H2'"  H  N N 305 
DT  "H2''" H  N N 306 
DT  "H1'"  H  N N 307 
DT  H3     H  N N 308 
DT  H71    H  N N 309 
DT  H72    H  N N 310 
DT  H73    H  N N 311 
DT  H6     H  N N 312 
GLN N      N  N N 313 
GLN CA     C  N S 314 
GLN C      C  N N 315 
GLN O      O  N N 316 
GLN CB     C  N N 317 
GLN CG     C  N N 318 
GLN CD     C  N N 319 
GLN OE1    O  N N 320 
GLN NE2    N  N N 321 
GLN OXT    O  N N 322 
GLN H      H  N N 323 
GLN H2     H  N N 324 
GLN HA     H  N N 325 
GLN HB2    H  N N 326 
GLN HB3    H  N N 327 
GLN HG2    H  N N 328 
GLN HG3    H  N N 329 
GLN HE21   H  N N 330 
GLN HE22   H  N N 331 
GLN HXT    H  N N 332 
GLU N      N  N N 333 
GLU CA     C  N S 334 
GLU C      C  N N 335 
GLU O      O  N N 336 
GLU CB     C  N N 337 
GLU CG     C  N N 338 
GLU CD     C  N N 339 
GLU OE1    O  N N 340 
GLU OE2    O  N N 341 
GLU OXT    O  N N 342 
GLU H      H  N N 343 
GLU H2     H  N N 344 
GLU HA     H  N N 345 
GLU HB2    H  N N 346 
GLU HB3    H  N N 347 
GLU HG2    H  N N 348 
GLU HG3    H  N N 349 
GLU HE2    H  N N 350 
GLU HXT    H  N N 351 
GLY N      N  N N 352 
GLY CA     C  N N 353 
GLY C      C  N N 354 
GLY O      O  N N 355 
GLY OXT    O  N N 356 
GLY H      H  N N 357 
GLY H2     H  N N 358 
GLY HA2    H  N N 359 
GLY HA3    H  N N 360 
GLY HXT    H  N N 361 
HIS N      N  N N 362 
HIS CA     C  N S 363 
HIS C      C  N N 364 
HIS O      O  N N 365 
HIS CB     C  N N 366 
HIS CG     C  Y N 367 
HIS ND1    N  Y N 368 
HIS CD2    C  Y N 369 
HIS CE1    C  Y N 370 
HIS NE2    N  Y N 371 
HIS OXT    O  N N 372 
HIS H      H  N N 373 
HIS H2     H  N N 374 
HIS HA     H  N N 375 
HIS HB2    H  N N 376 
HIS HB3    H  N N 377 
HIS HD1    H  N N 378 
HIS HD2    H  N N 379 
HIS HE1    H  N N 380 
HIS HE2    H  N N 381 
HIS HXT    H  N N 382 
ILE N      N  N N 383 
ILE CA     C  N S 384 
ILE C      C  N N 385 
ILE O      O  N N 386 
ILE CB     C  N S 387 
ILE CG1    C  N N 388 
ILE CG2    C  N N 389 
ILE CD1    C  N N 390 
ILE OXT    O  N N 391 
ILE H      H  N N 392 
ILE H2     H  N N 393 
ILE HA     H  N N 394 
ILE HB     H  N N 395 
ILE HG12   H  N N 396 
ILE HG13   H  N N 397 
ILE HG21   H  N N 398 
ILE HG22   H  N N 399 
ILE HG23   H  N N 400 
ILE HD11   H  N N 401 
ILE HD12   H  N N 402 
ILE HD13   H  N N 403 
ILE HXT    H  N N 404 
LEU N      N  N N 405 
LEU CA     C  N S 406 
LEU C      C  N N 407 
LEU O      O  N N 408 
LEU CB     C  N N 409 
LEU CG     C  N N 410 
LEU CD1    C  N N 411 
LEU CD2    C  N N 412 
LEU OXT    O  N N 413 
LEU H      H  N N 414 
LEU H2     H  N N 415 
LEU HA     H  N N 416 
LEU HB2    H  N N 417 
LEU HB3    H  N N 418 
LEU HG     H  N N 419 
LEU HD11   H  N N 420 
LEU HD12   H  N N 421 
LEU HD13   H  N N 422 
LEU HD21   H  N N 423 
LEU HD22   H  N N 424 
LEU HD23   H  N N 425 
LEU HXT    H  N N 426 
LYS N      N  N N 427 
LYS CA     C  N S 428 
LYS C      C  N N 429 
LYS O      O  N N 430 
LYS CB     C  N N 431 
LYS CG     C  N N 432 
LYS CD     C  N N 433 
LYS CE     C  N N 434 
LYS NZ     N  N N 435 
LYS OXT    O  N N 436 
LYS H      H  N N 437 
LYS H2     H  N N 438 
LYS HA     H  N N 439 
LYS HB2    H  N N 440 
LYS HB3    H  N N 441 
LYS HG2    H  N N 442 
LYS HG3    H  N N 443 
LYS HD2    H  N N 444 
LYS HD3    H  N N 445 
LYS HE2    H  N N 446 
LYS HE3    H  N N 447 
LYS HZ1    H  N N 448 
LYS HZ2    H  N N 449 
LYS HZ3    H  N N 450 
LYS HXT    H  N N 451 
MET N      N  N N 452 
MET CA     C  N S 453 
MET C      C  N N 454 
MET O      O  N N 455 
MET CB     C  N N 456 
MET CG     C  N N 457 
MET SD     S  N N 458 
MET CE     C  N N 459 
MET OXT    O  N N 460 
MET H      H  N N 461 
MET H2     H  N N 462 
MET HA     H  N N 463 
MET HB2    H  N N 464 
MET HB3    H  N N 465 
MET HG2    H  N N 466 
MET HG3    H  N N 467 
MET HE1    H  N N 468 
MET HE2    H  N N 469 
MET HE3    H  N N 470 
MET HXT    H  N N 471 
MG  MG     MG N N 472 
PHE N      N  N N 473 
PHE CA     C  N S 474 
PHE C      C  N N 475 
PHE O      O  N N 476 
PHE CB     C  N N 477 
PHE CG     C  Y N 478 
PHE CD1    C  Y N 479 
PHE CD2    C  Y N 480 
PHE CE1    C  Y N 481 
PHE CE2    C  Y N 482 
PHE CZ     C  Y N 483 
PHE OXT    O  N N 484 
PHE H      H  N N 485 
PHE H2     H  N N 486 
PHE HA     H  N N 487 
PHE HB2    H  N N 488 
PHE HB3    H  N N 489 
PHE HD1    H  N N 490 
PHE HD2    H  N N 491 
PHE HE1    H  N N 492 
PHE HE2    H  N N 493 
PHE HZ     H  N N 494 
PHE HXT    H  N N 495 
PRO N      N  N N 496 
PRO CA     C  N S 497 
PRO C      C  N N 498 
PRO O      O  N N 499 
PRO CB     C  N N 500 
PRO CG     C  N N 501 
PRO CD     C  N N 502 
PRO OXT    O  N N 503 
PRO H      H  N N 504 
PRO HA     H  N N 505 
PRO HB2    H  N N 506 
PRO HB3    H  N N 507 
PRO HG2    H  N N 508 
PRO HG3    H  N N 509 
PRO HD2    H  N N 510 
PRO HD3    H  N N 511 
PRO HXT    H  N N 512 
SER N      N  N N 513 
SER CA     C  N S 514 
SER C      C  N N 515 
SER O      O  N N 516 
SER CB     C  N N 517 
SER OG     O  N N 518 
SER OXT    O  N N 519 
SER H      H  N N 520 
SER H2     H  N N 521 
SER HA     H  N N 522 
SER HB2    H  N N 523 
SER HB3    H  N N 524 
SER HG     H  N N 525 
SER HXT    H  N N 526 
THR N      N  N N 527 
THR CA     C  N S 528 
THR C      C  N N 529 
THR O      O  N N 530 
THR CB     C  N R 531 
THR OG1    O  N N 532 
THR CG2    C  N N 533 
THR OXT    O  N N 534 
THR H      H  N N 535 
THR H2     H  N N 536 
THR HA     H  N N 537 
THR HB     H  N N 538 
THR HG1    H  N N 539 
THR HG21   H  N N 540 
THR HG22   H  N N 541 
THR HG23   H  N N 542 
THR HXT    H  N N 543 
TRP N      N  N N 544 
TRP CA     C  N S 545 
TRP C      C  N N 546 
TRP O      O  N N 547 
TRP CB     C  N N 548 
TRP CG     C  Y N 549 
TRP CD1    C  Y N 550 
TRP CD2    C  Y N 551 
TRP NE1    N  Y N 552 
TRP CE2    C  Y N 553 
TRP CE3    C  Y N 554 
TRP CZ2    C  Y N 555 
TRP CZ3    C  Y N 556 
TRP CH2    C  Y N 557 
TRP OXT    O  N N 558 
TRP H      H  N N 559 
TRP H2     H  N N 560 
TRP HA     H  N N 561 
TRP HB2    H  N N 562 
TRP HB3    H  N N 563 
TRP HD1    H  N N 564 
TRP HE1    H  N N 565 
TRP HE3    H  N N 566 
TRP HZ2    H  N N 567 
TRP HZ3    H  N N 568 
TRP HH2    H  N N 569 
TRP HXT    H  N N 570 
TYR N      N  N N 571 
TYR CA     C  N S 572 
TYR C      C  N N 573 
TYR O      O  N N 574 
TYR CB     C  N N 575 
TYR CG     C  Y N 576 
TYR CD1    C  Y N 577 
TYR CD2    C  Y N 578 
TYR CE1    C  Y N 579 
TYR CE2    C  Y N 580 
TYR CZ     C  Y N 581 
TYR OH     O  N N 582 
TYR OXT    O  N N 583 
TYR H      H  N N 584 
TYR H2     H  N N 585 
TYR HA     H  N N 586 
TYR HB2    H  N N 587 
TYR HB3    H  N N 588 
TYR HD1    H  N N 589 
TYR HD2    H  N N 590 
TYR HE1    H  N N 591 
TYR HE2    H  N N 592 
TYR HH     H  N N 593 
TYR HXT    H  N N 594 
VAL N      N  N N 595 
VAL CA     C  N S 596 
VAL C      C  N N 597 
VAL O      O  N N 598 
VAL CB     C  N N 599 
VAL CG1    C  N N 600 
VAL CG2    C  N N 601 
VAL OXT    O  N N 602 
VAL H      H  N N 603 
VAL H2     H  N N 604 
VAL HA     H  N N 605 
VAL HB     H  N N 606 
VAL HG11   H  N N 607 
VAL HG12   H  N N 608 
VAL HG13   H  N N 609 
VAL HG21   H  N N 610 
VAL HG22   H  N N 611 
VAL HG23   H  N N 612 
VAL HXT    H  N N 613 
# 
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 
2DA P     OP1    doub N N 1   
2DA P     OP2    sing N N 2   
2DA P     OP3    sing N N 3   
2DA P     "O5'"  sing N N 4   
2DA OP2   HOP2   sing N N 5   
2DA OP3   HOP3   sing N N 6   
2DA "O5'" "C5'"  sing N N 7   
2DA "C5'" "C4'"  sing N N 8   
2DA "C5'" "H5'"  sing N N 9   
2DA "C5'" "H5''" sing N N 10  
2DA "C4'" "O4'"  sing N N 11  
2DA "C4'" "C3'"  sing N N 12  
2DA "C4'" "H4'"  sing N N 13  
2DA "O4'" "C1'"  sing N N 14  
2DA "C3'" "C2'"  sing N N 15  
2DA "C3'" "H3'1" sing N N 16  
2DA "C3'" "H3'2" sing N N 17  
2DA "C2'" "C1'"  sing N N 18  
2DA "C2'" "H2'"  sing N N 19  
2DA "C2'" "H2''" sing N N 20  
2DA "C1'" N9     sing N N 21  
2DA "C1'" "H1'"  sing N N 22  
2DA N9    C8     sing Y N 23  
2DA N9    C4     sing Y N 24  
2DA C8    N7     doub Y N 25  
2DA C8    H8     sing N N 26  
2DA N7    C5     sing Y N 27  
2DA C5    C6     sing Y N 28  
2DA C5    C4     doub Y N 29  
2DA C6    N6     sing N N 30  
2DA C6    N1     doub Y N 31  
2DA N6    HN61   sing N N 32  
2DA N6    HN62   sing N N 33  
2DA N1    C2     sing Y N 34  
2DA C2    N3     doub Y N 35  
2DA C2    H2     sing N N 36  
2DA N3    C4     sing Y N 37  
ALA N     CA     sing N N 38  
ALA N     H      sing N N 39  
ALA N     H2     sing N N 40  
ALA CA    C      sing N N 41  
ALA CA    CB     sing N N 42  
ALA CA    HA     sing N N 43  
ALA C     O      doub N N 44  
ALA C     OXT    sing N N 45  
ALA CB    HB1    sing N N 46  
ALA CB    HB2    sing N N 47  
ALA CB    HB3    sing N N 48  
ALA OXT   HXT    sing N N 49  
ARG N     CA     sing N N 50  
ARG N     H      sing N N 51  
ARG N     H2     sing N N 52  
ARG CA    C      sing N N 53  
ARG CA    CB     sing N N 54  
ARG CA    HA     sing N N 55  
ARG C     O      doub N N 56  
ARG C     OXT    sing N N 57  
ARG CB    CG     sing N N 58  
ARG CB    HB2    sing N N 59  
ARG CB    HB3    sing N N 60  
ARG CG    CD     sing N N 61  
ARG CG    HG2    sing N N 62  
ARG CG    HG3    sing N N 63  
ARG CD    NE     sing N N 64  
ARG CD    HD2    sing N N 65  
ARG CD    HD3    sing N N 66  
ARG NE    CZ     sing N N 67  
ARG NE    HE     sing N N 68  
ARG CZ    NH1    sing N N 69  
ARG CZ    NH2    doub N N 70  
ARG NH1   HH11   sing N N 71  
ARG NH1   HH12   sing N N 72  
ARG NH2   HH21   sing N N 73  
ARG NH2   HH22   sing N N 74  
ARG OXT   HXT    sing N N 75  
ASN N     CA     sing N N 76  
ASN N     H      sing N N 77  
ASN N     H2     sing N N 78  
ASN CA    C      sing N N 79  
ASN CA    CB     sing N N 80  
ASN CA    HA     sing N N 81  
ASN C     O      doub N N 82  
ASN C     OXT    sing N N 83  
ASN CB    CG     sing N N 84  
ASN CB    HB2    sing N N 85  
ASN CB    HB3    sing N N 86  
ASN CG    OD1    doub N N 87  
ASN CG    ND2    sing N N 88  
ASN ND2   HD21   sing N N 89  
ASN ND2   HD22   sing N N 90  
ASN OXT   HXT    sing N N 91  
ASP N     CA     sing N N 92  
ASP N     H      sing N N 93  
ASP N     H2     sing N N 94  
ASP CA    C      sing N N 95  
ASP CA    CB     sing N N 96  
ASP CA    HA     sing N N 97  
ASP C     O      doub N N 98  
ASP C     OXT    sing N N 99  
ASP CB    CG     sing N N 100 
ASP CB    HB2    sing N N 101 
ASP CB    HB3    sing N N 102 
ASP CG    OD1    doub N N 103 
ASP CG    OD2    sing N N 104 
ASP OD2   HD2    sing N N 105 
ASP OXT   HXT    sing N N 106 
CYS N     CA     sing N N 107 
CYS N     H      sing N N 108 
CYS N     H2     sing N N 109 
CYS CA    C      sing N N 110 
CYS CA    CB     sing N N 111 
CYS CA    HA     sing N N 112 
CYS C     O      doub N N 113 
CYS C     OXT    sing N N 114 
CYS CB    SG     sing N N 115 
CYS CB    HB2    sing N N 116 
CYS CB    HB3    sing N N 117 
CYS SG    HG     sing N N 118 
CYS OXT   HXT    sing N N 119 
DA  OP3   P      sing N N 120 
DA  OP3   HOP3   sing N N 121 
DA  P     OP1    doub N N 122 
DA  P     OP2    sing N N 123 
DA  P     "O5'"  sing N N 124 
DA  OP2   HOP2   sing N N 125 
DA  "O5'" "C5'"  sing N N 126 
DA  "C5'" "C4'"  sing N N 127 
DA  "C5'" "H5'"  sing N N 128 
DA  "C5'" "H5''" sing N N 129 
DA  "C4'" "O4'"  sing N N 130 
DA  "C4'" "C3'"  sing N N 131 
DA  "C4'" "H4'"  sing N N 132 
DA  "O4'" "C1'"  sing N N 133 
DA  "C3'" "O3'"  sing N N 134 
DA  "C3'" "C2'"  sing N N 135 
DA  "C3'" "H3'"  sing N N 136 
DA  "O3'" "HO3'" sing N N 137 
DA  "C2'" "C1'"  sing N N 138 
DA  "C2'" "H2'"  sing N N 139 
DA  "C2'" "H2''" sing N N 140 
DA  "C1'" N9     sing N N 141 
DA  "C1'" "H1'"  sing N N 142 
DA  N9    C8     sing Y N 143 
DA  N9    C4     sing Y N 144 
DA  C8    N7     doub Y N 145 
DA  C8    H8     sing N N 146 
DA  N7    C5     sing Y N 147 
DA  C5    C6     sing Y N 148 
DA  C5    C4     doub Y N 149 
DA  C6    N6     sing N N 150 
DA  C6    N1     doub Y N 151 
DA  N6    H61    sing N N 152 
DA  N6    H62    sing N N 153 
DA  N1    C2     sing Y N 154 
DA  C2    N3     doub Y N 155 
DA  C2    H2     sing N N 156 
DA  N3    C4     sing Y N 157 
DC  OP3   P      sing N N 158 
DC  OP3   HOP3   sing N N 159 
DC  P     OP1    doub N N 160 
DC  P     OP2    sing N N 161 
DC  P     "O5'"  sing N N 162 
DC  OP2   HOP2   sing N N 163 
DC  "O5'" "C5'"  sing N N 164 
DC  "C5'" "C4'"  sing N N 165 
DC  "C5'" "H5'"  sing N N 166 
DC  "C5'" "H5''" sing N N 167 
DC  "C4'" "O4'"  sing N N 168 
DC  "C4'" "C3'"  sing N N 169 
DC  "C4'" "H4'"  sing N N 170 
DC  "O4'" "C1'"  sing N N 171 
DC  "C3'" "O3'"  sing N N 172 
DC  "C3'" "C2'"  sing N N 173 
DC  "C3'" "H3'"  sing N N 174 
DC  "O3'" "HO3'" sing N N 175 
DC  "C2'" "C1'"  sing N N 176 
DC  "C2'" "H2'"  sing N N 177 
DC  "C2'" "H2''" sing N N 178 
DC  "C1'" N1     sing N N 179 
DC  "C1'" "H1'"  sing N N 180 
DC  N1    C2     sing N N 181 
DC  N1    C6     sing N N 182 
DC  C2    O2     doub N N 183 
DC  C2    N3     sing N N 184 
DC  N3    C4     doub N N 185 
DC  C4    N4     sing N N 186 
DC  C4    C5     sing N N 187 
DC  N4    H41    sing N N 188 
DC  N4    H42    sing N N 189 
DC  C5    C6     doub N N 190 
DC  C5    H5     sing N N 191 
DC  C6    H6     sing N N 192 
DG  OP3   P      sing N N 193 
DG  OP3   HOP3   sing N N 194 
DG  P     OP1    doub N N 195 
DG  P     OP2    sing N N 196 
DG  P     "O5'"  sing N N 197 
DG  OP2   HOP2   sing N N 198 
DG  "O5'" "C5'"  sing N N 199 
DG  "C5'" "C4'"  sing N N 200 
DG  "C5'" "H5'"  sing N N 201 
DG  "C5'" "H5''" sing N N 202 
DG  "C4'" "O4'"  sing N N 203 
DG  "C4'" "C3'"  sing N N 204 
DG  "C4'" "H4'"  sing N N 205 
DG  "O4'" "C1'"  sing N N 206 
DG  "C3'" "O3'"  sing N N 207 
DG  "C3'" "C2'"  sing N N 208 
DG  "C3'" "H3'"  sing N N 209 
DG  "O3'" "HO3'" sing N N 210 
DG  "C2'" "C1'"  sing N N 211 
DG  "C2'" "H2'"  sing N N 212 
DG  "C2'" "H2''" sing N N 213 
DG  "C1'" N9     sing N N 214 
DG  "C1'" "H1'"  sing N N 215 
DG  N9    C8     sing Y N 216 
DG  N9    C4     sing Y N 217 
DG  C8    N7     doub Y N 218 
DG  C8    H8     sing N N 219 
DG  N7    C5     sing Y N 220 
DG  C5    C6     sing N N 221 
DG  C5    C4     doub Y N 222 
DG  C6    O6     doub N N 223 
DG  C6    N1     sing N N 224 
DG  N1    C2     sing N N 225 
DG  N1    H1     sing N N 226 
DG  C2    N2     sing N N 227 
DG  C2    N3     doub N N 228 
DG  N2    H21    sing N N 229 
DG  N2    H22    sing N N 230 
DG  N3    C4     sing N N 231 
DGT PG    O1G    sing N N 232 
DGT PG    O2G    sing N N 233 
DGT O1G   HO1G   sing N N 234 
DGT O2G   HO2G   sing N N 235 
DGT O3G   PG     doub N N 236 
DGT O3B   PG     sing N N 237 
DGT PB    O3B    sing N N 238 
DGT PB    O1B    sing N N 239 
DGT PB    O3A    sing N N 240 
DGT O1B   HO1B   sing N N 241 
DGT O2B   PB     doub N N 242 
DGT PA    O3A    sing N N 243 
DGT PA    O1A    sing N N 244 
DGT O1A   HO1A   sing N N 245 
DGT O2A   PA     doub N N 246 
DGT "O5'" PA     sing N N 247 
DGT "O5'" "C5'"  sing N N 248 
DGT "C5'" "H5'"  sing N N 249 
DGT "C5'" "H5'A" sing N N 250 
DGT "C4'" "C5'"  sing N N 251 
DGT "C4'" "H4'"  sing N N 252 
DGT "O4'" "C4'"  sing N N 253 
DGT "C3'" "C4'"  sing N N 254 
DGT "C3'" "O3'"  sing N N 255 
DGT "C3'" "H3'"  sing N N 256 
DGT "O3'" "HO3'" sing N N 257 
DGT "C2'" "C3'"  sing N N 258 
DGT "C2'" "C1'"  sing N N 259 
DGT "C2'" "H2'"  sing N N 260 
DGT "C2'" "H2'A" sing N N 261 
DGT "C1'" "O4'"  sing N N 262 
DGT "C1'" "H1'"  sing N N 263 
DGT N9    "C1'"  sing N N 264 
DGT N9    C4     sing Y N 265 
DGT C8    N9     sing Y N 266 
DGT C8    H8     sing N N 267 
DGT N7    C8     doub Y N 268 
DGT N7    C5     sing Y N 269 
DGT C5    C6     sing N N 270 
DGT C5    C4     doub Y N 271 
DGT C6    N1     sing N N 272 
DGT O6    C6     doub N N 273 
DGT N1    C2     sing N N 274 
DGT C2    N3     doub N N 275 
DGT C2    N2     sing N N 276 
DGT N2    HN2    sing N N 277 
DGT N2    HN2A   sing N N 278 
DGT C4    N3     sing N N 279 
DGT N1    H16    sing N N 280 
DT  OP3   P      sing N N 281 
DT  OP3   HOP3   sing N N 282 
DT  P     OP1    doub N N 283 
DT  P     OP2    sing N N 284 
DT  P     "O5'"  sing N N 285 
DT  OP2   HOP2   sing N N 286 
DT  "O5'" "C5'"  sing N N 287 
DT  "C5'" "C4'"  sing N N 288 
DT  "C5'" "H5'"  sing N N 289 
DT  "C5'" "H5''" sing N N 290 
DT  "C4'" "O4'"  sing N N 291 
DT  "C4'" "C3'"  sing N N 292 
DT  "C4'" "H4'"  sing N N 293 
DT  "O4'" "C1'"  sing N N 294 
DT  "C3'" "O3'"  sing N N 295 
DT  "C3'" "C2'"  sing N N 296 
DT  "C3'" "H3'"  sing N N 297 
DT  "O3'" "HO3'" sing N N 298 
DT  "C2'" "C1'"  sing N N 299 
DT  "C2'" "H2'"  sing N N 300 
DT  "C2'" "H2''" sing N N 301 
DT  "C1'" N1     sing N N 302 
DT  "C1'" "H1'"  sing N N 303 
DT  N1    C2     sing N N 304 
DT  N1    C6     sing N N 305 
DT  C2    O2     doub N N 306 
DT  C2    N3     sing N N 307 
DT  N3    C4     sing N N 308 
DT  N3    H3     sing N N 309 
DT  C4    O4     doub N N 310 
DT  C4    C5     sing N N 311 
DT  C5    C7     sing N N 312 
DT  C5    C6     doub N N 313 
DT  C7    H71    sing N N 314 
DT  C7    H72    sing N N 315 
DT  C7    H73    sing N N 316 
DT  C6    H6     sing N N 317 
GLN N     CA     sing N N 318 
GLN N     H      sing N N 319 
GLN N     H2     sing N N 320 
GLN CA    C      sing N N 321 
GLN CA    CB     sing N N 322 
GLN CA    HA     sing N N 323 
GLN C     O      doub N N 324 
GLN C     OXT    sing N N 325 
GLN CB    CG     sing N N 326 
GLN CB    HB2    sing N N 327 
GLN CB    HB3    sing N N 328 
GLN CG    CD     sing N N 329 
GLN CG    HG2    sing N N 330 
GLN CG    HG3    sing N N 331 
GLN CD    OE1    doub N N 332 
GLN CD    NE2    sing N N 333 
GLN NE2   HE21   sing N N 334 
GLN NE2   HE22   sing N N 335 
GLN OXT   HXT    sing N N 336 
GLU N     CA     sing N N 337 
GLU N     H      sing N N 338 
GLU N     H2     sing N N 339 
GLU CA    C      sing N N 340 
GLU CA    CB     sing N N 341 
GLU CA    HA     sing N N 342 
GLU C     O      doub N N 343 
GLU C     OXT    sing N N 344 
GLU CB    CG     sing N N 345 
GLU CB    HB2    sing N N 346 
GLU CB    HB3    sing N N 347 
GLU CG    CD     sing N N 348 
GLU CG    HG2    sing N N 349 
GLU CG    HG3    sing N N 350 
GLU CD    OE1    doub N N 351 
GLU CD    OE2    sing N N 352 
GLU OE2   HE2    sing N N 353 
GLU OXT   HXT    sing N N 354 
GLY N     CA     sing N N 355 
GLY N     H      sing N N 356 
GLY N     H2     sing N N 357 
GLY CA    C      sing N N 358 
GLY CA    HA2    sing N N 359 
GLY CA    HA3    sing N N 360 
GLY C     O      doub N N 361 
GLY C     OXT    sing N N 362 
GLY OXT   HXT    sing N N 363 
HIS N     CA     sing N N 364 
HIS N     H      sing N N 365 
HIS N     H2     sing N N 366 
HIS CA    C      sing N N 367 
HIS CA    CB     sing N N 368 
HIS CA    HA     sing N N 369 
HIS C     O      doub N N 370 
HIS C     OXT    sing N N 371 
HIS CB    CG     sing N N 372 
HIS CB    HB2    sing N N 373 
HIS CB    HB3    sing N N 374 
HIS CG    ND1    sing Y N 375 
HIS CG    CD2    doub Y N 376 
HIS ND1   CE1    doub Y N 377 
HIS ND1   HD1    sing N N 378 
HIS CD2   NE2    sing Y N 379 
HIS CD2   HD2    sing N N 380 
HIS CE1   NE2    sing Y N 381 
HIS CE1   HE1    sing N N 382 
HIS NE2   HE2    sing N N 383 
HIS OXT   HXT    sing N N 384 
ILE N     CA     sing N N 385 
ILE N     H      sing N N 386 
ILE N     H2     sing N N 387 
ILE CA    C      sing N N 388 
ILE CA    CB     sing N N 389 
ILE CA    HA     sing N N 390 
ILE C     O      doub N N 391 
ILE C     OXT    sing N N 392 
ILE CB    CG1    sing N N 393 
ILE CB    CG2    sing N N 394 
ILE CB    HB     sing N N 395 
ILE CG1   CD1    sing N N 396 
ILE CG1   HG12   sing N N 397 
ILE CG1   HG13   sing N N 398 
ILE CG2   HG21   sing N N 399 
ILE CG2   HG22   sing N N 400 
ILE CG2   HG23   sing N N 401 
ILE CD1   HD11   sing N N 402 
ILE CD1   HD12   sing N N 403 
ILE CD1   HD13   sing N N 404 
ILE OXT   HXT    sing N N 405 
LEU N     CA     sing N N 406 
LEU N     H      sing N N 407 
LEU N     H2     sing N N 408 
LEU CA    C      sing N N 409 
LEU CA    CB     sing N N 410 
LEU CA    HA     sing N N 411 
LEU C     O      doub N N 412 
LEU C     OXT    sing N N 413 
LEU CB    CG     sing N N 414 
LEU CB    HB2    sing N N 415 
LEU CB    HB3    sing N N 416 
LEU CG    CD1    sing N N 417 
LEU CG    CD2    sing N N 418 
LEU CG    HG     sing N N 419 
LEU CD1   HD11   sing N N 420 
LEU CD1   HD12   sing N N 421 
LEU CD1   HD13   sing N N 422 
LEU CD2   HD21   sing N N 423 
LEU CD2   HD22   sing N N 424 
LEU CD2   HD23   sing N N 425 
LEU OXT   HXT    sing N N 426 
LYS N     CA     sing N N 427 
LYS N     H      sing N N 428 
LYS N     H2     sing N N 429 
LYS CA    C      sing N N 430 
LYS CA    CB     sing N N 431 
LYS CA    HA     sing N N 432 
LYS C     O      doub N N 433 
LYS C     OXT    sing N N 434 
LYS CB    CG     sing N N 435 
LYS CB    HB2    sing N N 436 
LYS CB    HB3    sing N N 437 
LYS CG    CD     sing N N 438 
LYS CG    HG2    sing N N 439 
LYS CG    HG3    sing N N 440 
LYS CD    CE     sing N N 441 
LYS CD    HD2    sing N N 442 
LYS CD    HD3    sing N N 443 
LYS CE    NZ     sing N N 444 
LYS CE    HE2    sing N N 445 
LYS CE    HE3    sing N N 446 
LYS NZ    HZ1    sing N N 447 
LYS NZ    HZ2    sing N N 448 
LYS NZ    HZ3    sing N N 449 
LYS OXT   HXT    sing N N 450 
MET N     CA     sing N N 451 
MET N     H      sing N N 452 
MET N     H2     sing N N 453 
MET CA    C      sing N N 454 
MET CA    CB     sing N N 455 
MET CA    HA     sing N N 456 
MET C     O      doub N N 457 
MET C     OXT    sing N N 458 
MET CB    CG     sing N N 459 
MET CB    HB2    sing N N 460 
MET CB    HB3    sing N N 461 
MET CG    SD     sing N N 462 
MET CG    HG2    sing N N 463 
MET CG    HG3    sing N N 464 
MET SD    CE     sing N N 465 
MET CE    HE1    sing N N 466 
MET CE    HE2    sing N N 467 
MET CE    HE3    sing N N 468 
MET OXT   HXT    sing N N 469 
PHE N     CA     sing N N 470 
PHE N     H      sing N N 471 
PHE N     H2     sing N N 472 
PHE CA    C      sing N N 473 
PHE CA    CB     sing N N 474 
PHE CA    HA     sing N N 475 
PHE C     O      doub N N 476 
PHE C     OXT    sing N N 477 
PHE CB    CG     sing N N 478 
PHE CB    HB2    sing N N 479 
PHE CB    HB3    sing N N 480 
PHE CG    CD1    doub Y N 481 
PHE CG    CD2    sing Y N 482 
PHE CD1   CE1    sing Y N 483 
PHE CD1   HD1    sing N N 484 
PHE CD2   CE2    doub Y N 485 
PHE CD2   HD2    sing N N 486 
PHE CE1   CZ     doub Y N 487 
PHE CE1   HE1    sing N N 488 
PHE CE2   CZ     sing Y N 489 
PHE CE2   HE2    sing N N 490 
PHE CZ    HZ     sing N N 491 
PHE OXT   HXT    sing N N 492 
PRO N     CA     sing N N 493 
PRO N     CD     sing N N 494 
PRO N     H      sing N N 495 
PRO CA    C      sing N N 496 
PRO CA    CB     sing N N 497 
PRO CA    HA     sing N N 498 
PRO C     O      doub N N 499 
PRO C     OXT    sing N N 500 
PRO CB    CG     sing N N 501 
PRO CB    HB2    sing N N 502 
PRO CB    HB3    sing N N 503 
PRO CG    CD     sing N N 504 
PRO CG    HG2    sing N N 505 
PRO CG    HG3    sing N N 506 
PRO CD    HD2    sing N N 507 
PRO CD    HD3    sing N N 508 
PRO OXT   HXT    sing N N 509 
SER N     CA     sing N N 510 
SER N     H      sing N N 511 
SER N     H2     sing N N 512 
SER CA    C      sing N N 513 
SER CA    CB     sing N N 514 
SER CA    HA     sing N N 515 
SER C     O      doub N N 516 
SER C     OXT    sing N N 517 
SER CB    OG     sing N N 518 
SER CB    HB2    sing N N 519 
SER CB    HB3    sing N N 520 
SER OG    HG     sing N N 521 
SER OXT   HXT    sing N N 522 
THR N     CA     sing N N 523 
THR N     H      sing N N 524 
THR N     H2     sing N N 525 
THR CA    C      sing N N 526 
THR CA    CB     sing N N 527 
THR CA    HA     sing N N 528 
THR C     O      doub N N 529 
THR C     OXT    sing N N 530 
THR CB    OG1    sing N N 531 
THR CB    CG2    sing N N 532 
THR CB    HB     sing N N 533 
THR OG1   HG1    sing N N 534 
THR CG2   HG21   sing N N 535 
THR CG2   HG22   sing N N 536 
THR CG2   HG23   sing N N 537 
THR OXT   HXT    sing N N 538 
TRP N     CA     sing N N 539 
TRP N     H      sing N N 540 
TRP N     H2     sing N N 541 
TRP CA    C      sing N N 542 
TRP CA    CB     sing N N 543 
TRP CA    HA     sing N N 544 
TRP C     O      doub N N 545 
TRP C     OXT    sing N N 546 
TRP CB    CG     sing N N 547 
TRP CB    HB2    sing N N 548 
TRP CB    HB3    sing N N 549 
TRP CG    CD1    doub Y N 550 
TRP CG    CD2    sing Y N 551 
TRP CD1   NE1    sing Y N 552 
TRP CD1   HD1    sing N N 553 
TRP CD2   CE2    doub Y N 554 
TRP CD2   CE3    sing Y N 555 
TRP NE1   CE2    sing Y N 556 
TRP NE1   HE1    sing N N 557 
TRP CE2   CZ2    sing Y N 558 
TRP CE3   CZ3    doub Y N 559 
TRP CE3   HE3    sing N N 560 
TRP CZ2   CH2    doub Y N 561 
TRP CZ2   HZ2    sing N N 562 
TRP CZ3   CH2    sing Y N 563 
TRP CZ3   HZ3    sing N N 564 
TRP CH2   HH2    sing N N 565 
TRP OXT   HXT    sing N N 566 
TYR N     CA     sing N N 567 
TYR N     H      sing N N 568 
TYR N     H2     sing N N 569 
TYR CA    C      sing N N 570 
TYR CA    CB     sing N N 571 
TYR CA    HA     sing N N 572 
TYR C     O      doub N N 573 
TYR C     OXT    sing N N 574 
TYR CB    CG     sing N N 575 
TYR CB    HB2    sing N N 576 
TYR CB    HB3    sing N N 577 
TYR CG    CD1    doub Y N 578 
TYR CG    CD2    sing Y N 579 
TYR CD1   CE1    sing Y N 580 
TYR CD1   HD1    sing N N 581 
TYR CD2   CE2    doub Y N 582 
TYR CD2   HD2    sing N N 583 
TYR CE1   CZ     doub Y N 584 
TYR CE1   HE1    sing N N 585 
TYR CE2   CZ     sing Y N 586 
TYR CE2   HE2    sing N N 587 
TYR CZ    OH     sing N N 588 
TYR OH    HH     sing N N 589 
TYR OXT   HXT    sing N N 590 
VAL N     CA     sing N N 591 
VAL N     H      sing N N 592 
VAL N     H2     sing N N 593 
VAL CA    C      sing N N 594 
VAL CA    CB     sing N N 595 
VAL CA    HA     sing N N 596 
VAL C     O      doub N N 597 
VAL C     OXT    sing N N 598 
VAL CB    CG1    sing N N 599 
VAL CB    CG2    sing N N 600 
VAL CB    HB     sing N N 601 
VAL CG1   HG11   sing N N 602 
VAL CG1   HG12   sing N N 603 
VAL CG1   HG13   sing N N 604 
VAL CG2   HG21   sing N N 605 
VAL CG2   HG22   sing N N 606 
VAL CG2   HG23   sing N N 607 
VAL OXT   HXT    sing N N 608 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-06-18 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9CAY 
_em_admin.last_update        2024-11-27 
_em_admin.map_release_date   2024-11-06 
_em_admin.title              'Ternary structure of Plasmodium falciparum apicoplast DNA polymerase (exo-minus)' 
# 
_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          5833 
_em_entity_assembly_naturalsource.organism             'Plasmodium falciparum' 
_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          866768 
_em_entity_assembly_recombinant.organism             
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
_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               7 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         49 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (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                     ? 
# 
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  ? ? 1 ? ? 
MASKING                         ? 3  ? ? ? ? ? 
'CTF CORRECTION'                ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ? ? 
'MODEL FITTING'                 ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'              ? 8  ? ? ? ? ? 
OTHER                           ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? ? ? 
CLASSIFICATION                  ? 12 1 ? ? ? ? 
RECONSTRUCTION                  ? 13 1 ? ? ? ? 
'VOLUME SELECTION'              ? 14 1 1 1 ? ? 
'SERIES ALIGNMENT'              ? 15 1 1 1 ? ? 
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ? ? 
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ? ? 
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ? ? 
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 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_
_ndb_struct_conf_na.entry_id 
_ndb_struct_conf_na.feature 
9CAY 'double helix'        
9CAY 'a-form double helix' 
# 
loop_
_ndb_struct_na_base_pair.model_number 
_ndb_struct_na_base_pair.i_label_asym_id 
_ndb_struct_na_base_pair.i_label_comp_id 
_ndb_struct_na_base_pair.i_label_seq_id 
_ndb_struct_na_base_pair.i_symmetry 
_ndb_struct_na_base_pair.j_label_asym_id 
_ndb_struct_na_base_pair.j_label_comp_id 
_ndb_struct_na_base_pair.j_label_seq_id 
_ndb_struct_na_base_pair.j_symmetry 
_ndb_struct_na_base_pair.shear 
_ndb_struct_na_base_pair.stretch 
_ndb_struct_na_base_pair.stagger 
_ndb_struct_na_base_pair.buckle 
_ndb_struct_na_base_pair.propeller 
_ndb_struct_na_base_pair.opening 
_ndb_struct_na_base_pair.pair_number 
_ndb_struct_na_base_pair.pair_name 
_ndb_struct_na_base_pair.i_auth_asym_id 
_ndb_struct_na_base_pair.i_auth_seq_id 
_ndb_struct_na_base_pair.i_PDB_ins_code 
_ndb_struct_na_base_pair.j_auth_asym_id 
_ndb_struct_na_base_pair.j_auth_seq_id 
_ndb_struct_na_base_pair.j_PDB_ins_code 
_ndb_struct_na_base_pair.hbond_type_28 
_ndb_struct_na_base_pair.hbond_type_12 
1 A DT 10 1_555 C 2DA 20 1_555 0.878  -0.356 0.025  -2.030 -12.843 -5.600  1  E_DT10:2DA20_F E 10 ? F 20 ? 20 1 
1 A DC 11 1_555 C DG  19 1_555 -0.128 -0.307 -0.270 1.480  -4.221  0.958   2  E_DC11:DG19_F  E 11 ? F 19 ? 19 1 
1 A DT 12 1_555 C DA  18 1_555 0.035  -0.232 -0.164 0.087  -2.067  2.059   3  E_DT12:DA18_F  E 12 ? F 18 ? 20 1 
1 A DC 14 1_555 C DG  16 1_555 0.196  0.110  0.207  1.481  7.274   2.282   4  E_DC14:DG16_F  E 14 ? F 16 ? 19 1 
1 A DG 15 1_555 C DC  15 1_555 -0.177 -0.049 0.626  1.451  9.159   2.752   5  E_DG15:DC15_F  E 15 ? F 15 ? 19 1 
1 A DG 16 1_555 C DC  14 1_555 -0.074 -0.155 0.828  -1.252 3.623   4.406   6  E_DG16:DC14_F  E 16 ? F 14 ? 19 1 
1 A DA 17 1_555 C DT  13 1_555 0.318  -0.551 1.384  1.572  3.721   3.462   7  E_DA17:DT13_F  E 17 ? F 13 ? 20 1 
1 A DT 18 1_555 C DA  12 1_555 -0.087 -0.506 1.362  6.548  2.752   2.688   8  E_DT18:DA12_F  E 18 ? F 12 ? 20 1 
1 A DG 19 1_555 C DC  11 1_555 -0.233 -0.374 1.284  7.385  1.898   3.558   9  E_DG19:DC11_F  E 19 ? F 11 ? 19 1 
1 A DC 20 1_555 C DG  10 1_555 0.103  -0.318 0.905  -0.211 -0.695  -1.772  10 E_DC20:DG10_F  E 20 ? F 10 ? 19 1 
1 A DC 21 1_555 C DG  9  1_555 0.151  -0.147 0.293  -0.193 1.232   -4.703  11 E_DC21:DG9_F   E 21 ? F 9  ? 19 1 
1 A DT 22 1_555 C DA  8  1_555 -0.103 0.093  0.127  2.626  1.597   -16.203 12 E_DT22:DA8_F   E 22 ? F 8  ? 20 1 
1 A DC 23 1_555 C DG  7  1_555 0.344  -0.266 0.145  1.460  6.942   -8.380  13 E_DC23:DG7_F   E 23 ? F 7  ? 19 1 
1 A DA 24 1_555 C DT  6  1_555 0.233  -0.129 0.780  5.387  6.879   -15.833 14 E_DA24:DT6_F   E 24 ? F 6  ? 20 1 
1 A DC 25 1_555 C DG  5  1_555 0.383  -0.388 0.629  2.127  5.213   -4.184  15 E_DC25:DG5_F   E 25 ? F 5  ? 19 1 
1 A DA 26 1_555 C DT  4  1_555 2.972  -1.264 2.301  8.111  6.145   -3.782  16 E_DA26:DT4_F   E 26 ? F 4  ? 20 1 
# 
loop_
_ndb_struct_na_base_pair_step.model_number 
_ndb_struct_na_base_pair_step.i_label_asym_id_1 
_ndb_struct_na_base_pair_step.i_label_comp_id_1 
_ndb_struct_na_base_pair_step.i_label_seq_id_1 
_ndb_struct_na_base_pair_step.i_symmetry_1 
_ndb_struct_na_base_pair_step.j_label_asym_id_1 
_ndb_struct_na_base_pair_step.j_label_comp_id_1 
_ndb_struct_na_base_pair_step.j_label_seq_id_1 
_ndb_struct_na_base_pair_step.j_symmetry_1 
_ndb_struct_na_base_pair_step.i_label_asym_id_2 
_ndb_struct_na_base_pair_step.i_label_comp_id_2 
_ndb_struct_na_base_pair_step.i_label_seq_id_2 
_ndb_struct_na_base_pair_step.i_symmetry_2 
_ndb_struct_na_base_pair_step.j_label_asym_id_2 
_ndb_struct_na_base_pair_step.j_label_comp_id_2 
_ndb_struct_na_base_pair_step.j_label_seq_id_2 
_ndb_struct_na_base_pair_step.j_symmetry_2 
_ndb_struct_na_base_pair_step.shift 
_ndb_struct_na_base_pair_step.slide 
_ndb_struct_na_base_pair_step.rise 
_ndb_struct_na_base_pair_step.tilt 
_ndb_struct_na_base_pair_step.roll 
_ndb_struct_na_base_pair_step.twist 
_ndb_struct_na_base_pair_step.x_displacement 
_ndb_struct_na_base_pair_step.y_displacement 
_ndb_struct_na_base_pair_step.helical_rise 
_ndb_struct_na_base_pair_step.inclination 
_ndb_struct_na_base_pair_step.tip 
_ndb_struct_na_base_pair_step.helical_twist 
_ndb_struct_na_base_pair_step.step_number 
_ndb_struct_na_base_pair_step.step_name 
_ndb_struct_na_base_pair_step.i_auth_asym_id_1 
_ndb_struct_na_base_pair_step.i_auth_seq_id_1 
_ndb_struct_na_base_pair_step.i_PDB_ins_code_1 
_ndb_struct_na_base_pair_step.j_auth_asym_id_1 
_ndb_struct_na_base_pair_step.j_auth_seq_id_1 
_ndb_struct_na_base_pair_step.j_PDB_ins_code_1 
_ndb_struct_na_base_pair_step.i_auth_asym_id_2 
_ndb_struct_na_base_pair_step.i_auth_seq_id_2 
_ndb_struct_na_base_pair_step.i_PDB_ins_code_2 
_ndb_struct_na_base_pair_step.j_auth_asym_id_2 
_ndb_struct_na_base_pair_step.j_auth_seq_id_2 
_ndb_struct_na_base_pair_step.j_PDB_ins_code_2 
1 A DT 10 1_555 C 2DA 20 1_555 A DC 11 1_555 C DG 19 1_555 -0.522 -1.009 3.408 -1.011 8.475  26.610 -4.106 0.842  2.968 17.839 
2.128  27.922 1  EE_DT10DC11:DG192DA20_FF E 10 ? F 20 ? E 11 ? F 19 ? 
1 A DC 11 1_555 C DG  19 1_555 A DT 12 1_555 C DA 18 1_555 -0.109 -1.070 3.749 -0.319 6.376  24.348 -4.527 0.147  3.365 14.795 
0.740  25.158 2  EE_DC11DT12:DA18DG19_FF  E 11 ? F 19 ? E 12 ? F 18 ? 
1 A DT 12 1_555 C DA  18 1_555 A DC 14 1_555 C DG 16 1_555 0.601  -1.590 7.129 5.372  6.124  62.375 -2.120 -0.054 6.987 5.886  
-5.163 62.852 3  EE_DT12DC14:DG16DA18_FF  E 12 ? F 18 ? E 14 ? F 16 ? 
1 A DC 14 1_555 C DG  16 1_555 A DG 15 1_555 C DC 15 1_555 -0.645 -0.204 3.269 -1.606 3.333  29.681 -1.087 0.918  3.257 6.475  
3.119  29.905 4  EE_DC14DG15:DC15DG16_FF  E 14 ? F 16 ? E 15 ? F 15 ? 
1 A DG 15 1_555 C DC  15 1_555 A DG 16 1_555 C DC 14 1_555 0.962  -0.523 3.460 1.062  9.719  35.473 -2.211 -1.374 3.237 15.590 
-1.704 36.754 5  EE_DG15DG16:DC14DC15_FF  E 15 ? F 15 ? E 16 ? F 14 ? 
1 A DG 16 1_555 C DC  14 1_555 A DA 17 1_555 C DT 13 1_555 -0.590 0.101  3.140 -4.259 1.020  40.488 0.036  0.391  3.185 1.468  
6.133  40.714 6  EE_DG16DA17:DT13DC14_FF  E 16 ? F 14 ? E 17 ? F 13 ? 
1 A DA 17 1_555 C DT  13 1_555 A DT 18 1_555 C DA 12 1_555 0.222  -1.377 3.449 1.912  -0.326 33.668 -2.318 -0.054 3.468 -0.562 
-3.297 33.722 7  EE_DA17DT18:DA12DT13_FF  E 17 ? F 13 ? E 18 ? F 12 ? 
1 A DT 18 1_555 C DA  12 1_555 A DG 19 1_555 C DC 11 1_555 -0.111 1.220  3.490 3.781  0.271  42.079 1.664  0.568  3.475 0.376  
-5.253 42.242 8  EE_DT18DG19:DC11DA12_FF  E 18 ? F 12 ? E 19 ? F 11 ? 
1 A DG 19 1_555 C DC  11 1_555 A DC 20 1_555 C DG 10 1_555 -0.833 -0.868 3.372 1.342  2.940  37.557 -1.730 1.466  3.266 4.555  
-2.079 37.690 9  EE_DG19DC20:DG10DC11_FF  E 19 ? F 11 ? E 20 ? F 10 ? 
1 A DC 20 1_555 C DG  10 1_555 A DC 21 1_555 C DG 9  1_555 -0.531 -0.634 3.214 2.187  2.631  31.498 -1.632 1.363  3.110 4.829  
-4.014 31.679 10 EE_DC20DC21:DG9DG10_FF   E 20 ? F 10 ? E 21 ? F 9  ? 
1 A DC 21 1_555 C DG  9  1_555 A DT 22 1_555 C DA 8  1_555 -0.679 -0.858 3.228 3.336  6.202  24.265 -3.666 2.470  2.808 14.371 
-7.732 25.251 11 EE_DC21DT22:DA8DG9_FF    E 21 ? F 9  ? E 22 ? F 8  ? 
1 A DT 22 1_555 C DA  8  1_555 A DC 23 1_555 C DG 7  1_555 1.078  0.315  4.046 4.374  1.683  28.399 0.157  -0.930 4.173 3.401  
-8.840 28.775 12 EE_DT22DC23:DG7DA8_FF    E 22 ? F 8  ? E 23 ? F 7  ? 
1 A DC 23 1_555 C DG  7  1_555 A DA 24 1_555 C DT 6  1_555 -0.256 -0.859 3.461 0.392  6.495  22.655 -4.329 0.762  3.092 16.111 
-0.973 23.559 13 EE_DC23DA24:DT6DG7_FF    E 23 ? F 7  ? E 24 ? F 6  ? 
1 A DA 24 1_555 C DT  6  1_555 A DC 25 1_555 C DG 5  1_555 0.586  0.258  4.783 1.286  5.089  19.998 -2.564 -0.804 4.728 14.337 
-3.622 20.669 14 EE_DA24DC25:DG5DT6_FF    E 24 ? F 6  ? E 25 ? F 5  ? 
1 A DC 25 1_555 C DG  5  1_555 A DA 26 1_555 C DT 4  1_555 1.081  0.979  3.747 -2.906 0.196  39.479 1.420  -1.983 3.666 0.289  
4.294  39.582 15 EE_DC25DA26:DT4DG5_FF    E 25 ? F 5  ? E 26 ? F 4  ? 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           1R35GM142722 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9CAY 
_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 
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    P  P     . DC  A 1 6   ? 129.116 84.200  118.821 1.00 193.12 ? 6   DC  E P     1 
ATOM   2    O  OP1   . DC  A 1 6   ? 130.306 84.358  119.687 1.00 196.43 ? 6   DC  E OP1   1 
ATOM   3    O  OP2   . DC  A 1 6   ? 127.978 83.366  119.267 1.00 189.51 ? 6   DC  E OP2   1 
ATOM   4    O  "O5'" . DC  A 1 6   ? 128.547 85.645  118.436 1.00 192.86 ? 6   DC  E "O5'" 1 
ATOM   5    C  "C5'" . DC  A 1 6   ? 128.710 86.739  119.332 1.00 192.36 ? 6   DC  E "C5'" 1 
ATOM   6    C  "C4'" . DC  A 1 6   ? 127.764 86.622  120.512 1.00 189.44 ? 6   DC  E "C4'" 1 
ATOM   7    O  "O4'" . DC  A 1 6   ? 127.999 87.730  121.425 1.00 191.74 ? 6   DC  E "O4'" 1 
ATOM   8    C  "C3'" . DC  A 1 6   ? 126.285 86.693  120.153 1.00 184.79 ? 6   DC  E "C3'" 1 
ATOM   9    O  "O3'" . DC  A 1 6   ? 125.500 85.883  121.039 1.00 184.06 ? 6   DC  E "O3'" 1 
ATOM   10   C  "C2'" . DC  A 1 6   ? 125.982 88.176  120.297 1.00 174.63 ? 6   DC  E "C2'" 1 
ATOM   11   C  "C1'" . DC  A 1 6   ? 126.860 88.572  121.473 1.00 187.71 ? 6   DC  E "C1'" 1 
ATOM   12   N  N1    . DC  A 1 6   ? 127.307 89.997  121.438 1.00 191.51 ? 6   DC  E N1    1 
ATOM   13   C  C2    . DC  A 1 6   ? 126.560 90.969  122.111 1.00 192.62 ? 6   DC  E C2    1 
ATOM   14   O  O2    . DC  A 1 6   ? 125.540 90.628  122.726 1.00 190.89 ? 6   DC  E O2    1 
ATOM   15   N  N3    . DC  A 1 6   ? 126.977 92.261  122.072 1.00 194.80 ? 6   DC  E N3    1 
ATOM   16   C  C4    . DC  A 1 6   ? 128.083 92.586  121.398 1.00 195.46 ? 6   DC  E C4    1 
ATOM   17   N  N4    . DC  A 1 6   ? 128.456 93.872  121.387 1.00 193.13 ? 6   DC  E N4    1 
ATOM   18   C  C5    . DC  A 1 6   ? 128.857 91.608  120.705 1.00 195.23 ? 6   DC  E C5    1 
ATOM   19   C  C6    . DC  A 1 6   ? 128.435 90.339  120.750 1.00 192.51 ? 6   DC  E C6    1 
ATOM   20   P  P     . DA  A 1 7   ? 124.475 84.782  120.462 1.00 180.97 ? 7   DA  E P     1 
ATOM   21   O  OP1   . DA  A 1 7   ? 124.525 83.621  121.376 1.00 177.14 ? 7   DA  E OP1   1 
ATOM   22   O  OP2   . DA  A 1 7   ? 124.742 84.586  119.021 1.00 176.22 ? 7   DA  E OP2   1 
ATOM   23   O  "O5'" . DA  A 1 7   ? 123.041 85.481  120.597 1.00 163.09 ? 7   DA  E "O5'" 1 
ATOM   24   C  "C5'" . DA  A 1 7   ? 122.873 86.832  120.196 1.00 149.18 ? 7   DA  E "C5'" 1 
ATOM   25   C  "C4'" . DA  A 1 7   ? 121.498 87.066  119.597 1.00 129.93 ? 7   DA  E "C4'" 1 
ATOM   26   O  "O4'" . DA  A 1 7   ? 121.418 88.438  119.132 1.00 123.79 ? 7   DA  E "O4'" 1 
ATOM   27   C  "C3'" . DA  A 1 7   ? 121.177 86.230  118.371 1.00 118.56 ? 7   DA  E "C3'" 1 
ATOM   28   O  "O3'" . DA  A 1 7   ? 119.767 86.114  118.182 1.00 112.12 ? 7   DA  E "O3'" 1 
ATOM   29   C  "C2'" . DA  A 1 7   ? 121.839 87.038  117.270 1.00 113.57 ? 7   DA  E "C2'" 1 
ATOM   30   C  "C1'" . DA  A 1 7   ? 121.561 88.473  117.717 1.00 115.17 ? 7   DA  E "C1'" 1 
ATOM   31   N  N9    . DA  A 1 7   ? 122.618 89.423  117.369 1.00 113.37 ? 7   DA  E N9    1 
ATOM   32   C  C8    . DA  A 1 7   ? 123.725 89.184  116.605 1.00 112.09 ? 7   DA  E C8    1 
ATOM   33   N  N7    . DA  A 1 7   ? 124.499 90.231  116.448 1.00 110.00 ? 7   DA  E N7    1 
ATOM   34   C  C5    . DA  A 1 7   ? 123.851 91.231  117.152 1.00 109.69 ? 7   DA  E C5    1 
ATOM   35   C  C6    . DA  A 1 7   ? 124.157 92.589  117.375 1.00 109.79 ? 7   DA  E C6    1 
ATOM   36   N  N6    . DA  A 1 7   ? 125.247 93.190  116.891 1.00 110.13 ? 7   DA  E N6    1 
ATOM   37   N  N1    . DA  A 1 7   ? 123.298 93.306  118.124 1.00 110.36 ? 7   DA  E N1    1 
ATOM   38   C  C2    . DA  A 1 7   ? 122.209 92.705  118.612 1.00 109.78 ? 7   DA  E C2    1 
ATOM   39   N  N3    . DA  A 1 7   ? 121.816 91.441  118.470 1.00 108.33 ? 7   DA  E N3    1 
ATOM   40   C  C4    . DA  A 1 7   ? 122.687 90.751  117.722 1.00 110.77 ? 7   DA  E C4    1 
ATOM   41   P  P     . DG  A 1 8   ? 119.170 85.085  117.103 1.00 108.93 ? 8   DG  E P     1 
ATOM   42   O  OP1   . DG  A 1 8   ? 119.350 83.726  117.657 1.00 105.53 ? 8   DG  E OP1   1 
ATOM   43   O  OP2   . DG  A 1 8   ? 119.737 85.412  115.776 1.00 110.80 ? 8   DG  E OP2   1 
ATOM   44   O  "O5'" . DG  A 1 8   ? 117.600 85.410  117.083 1.00 95.82  ? 8   DG  E "O5'" 1 
ATOM   45   C  "C5'" . DG  A 1 8   ? 117.056 86.336  116.138 1.00 94.33  ? 8   DG  E "C5'" 1 
ATOM   46   C  "C4'" . DG  A 1 8   ? 116.820 87.698  116.769 1.00 89.22  ? 8   DG  E "C4'" 1 
ATOM   47   O  "O4'" . DG  A 1 8   ? 118.069 88.442  116.791 1.00 97.60  ? 8   DG  E "O4'" 1 
ATOM   48   C  "C3'" . DG  A 1 8   ? 115.823 88.577  116.020 1.00 82.22  ? 8   DG  E "C3'" 1 
ATOM   49   O  "O3'" . DG  A 1 8   ? 115.055 89.361  116.919 1.00 77.94  ? 8   DG  E "O3'" 1 
ATOM   50   C  "C2'" . DG  A 1 8   ? 116.714 89.428  115.132 1.00 81.89  ? 8   DG  E "C2'" 1 
ATOM   51   C  "C1'" . DG  A 1 8   ? 117.969 89.595  115.970 1.00 94.96  ? 8   DG  E "C1'" 1 
ATOM   52   N  N9    . DG  A 1 8   ? 119.184 89.712  115.172 1.00 97.90  ? 8   DG  E N9    1 
ATOM   53   C  C8    . DG  A 1 8   ? 119.841 88.703  114.512 1.00 95.05  ? 8   DG  E C8    1 
ATOM   54   N  N7    . DG  A 1 8   ? 120.903 89.108  113.872 1.00 94.38  ? 8   DG  E N7    1 
ATOM   55   C  C5    . DG  A 1 8   ? 120.950 90.473  114.121 1.00 101.07 ? 8   DG  E C5    1 
ATOM   56   C  C6    . DG  A 1 8   ? 121.880 91.450  113.690 1.00 99.92  ? 8   DG  E C6    1 
ATOM   57   O  O6    . DG  A 1 8   ? 122.881 91.299  112.977 1.00 97.53  ? 8   DG  E O6    1 
ATOM   58   N  N1    . DG  A 1 8   ? 121.556 92.715  114.172 1.00 98.63  ? 8   DG  E N1    1 
ATOM   59   C  C2    . DG  A 1 8   ? 120.473 93.000  114.966 1.00 96.79  ? 8   DG  E C2    1 
ATOM   60   N  N2    . DG  A 1 8   ? 120.330 94.280  115.332 1.00 93.45  ? 8   DG  E N2    1 
ATOM   61   N  N3    . DG  A 1 8   ? 119.596 92.096  115.379 1.00 99.03  ? 8   DG  E N3    1 
ATOM   62   C  C4    . DG  A 1 8   ? 119.896 90.859  114.919 1.00 101.33 ? 8   DG  E C4    1 
ATOM   63   P  P     . DC  A 1 9   ? 113.491 89.609  116.642 1.00 65.45  ? 9   DC  E P     1 
ATOM   64   O  OP1   . DC  A 1 9   ? 112.959 90.391  117.780 1.00 77.71  ? 9   DC  E OP1   1 
ATOM   65   O  OP2   . DC  A 1 9   ? 112.886 88.304  116.305 1.00 68.60  ? 9   DC  E OP2   1 
ATOM   66   O  "O5'" . DC  A 1 9   ? 113.467 90.531  115.333 1.00 59.87  ? 9   DC  E "O5'" 1 
ATOM   67   C  "C5'" . DC  A 1 9   ? 113.545 89.932  114.041 1.00 60.46  ? 9   DC  E "C5'" 1 
ATOM   68   C  "C4'" . DC  A 1 9   ? 113.138 90.900  112.942 1.00 52.93  ? 9   DC  E "C4'" 1 
ATOM   69   O  "O4'" . DC  A 1 9   ? 111.758 90.675  112.596 1.00 50.22  ? 9   DC  E "O4'" 1 
ATOM   70   C  "C3'" . DC  A 1 9   ? 113.199 92.369  113.300 1.00 48.48  ? 9   DC  E "C3'" 1 
ATOM   71   O  "O3'" . DC  A 1 9   ? 114.499 92.902  113.087 1.00 49.91  ? 9   DC  E "O3'" 1 
ATOM   72   C  "C2'" . DC  A 1 9   ? 112.165 92.995  112.370 1.00 42.58  ? 9   DC  E "C2'" 1 
ATOM   73   C  "C1'" . DC  A 1 9   ? 111.246 91.835  111.978 1.00 39.56  ? 9   DC  E "C1'" 1 
ATOM   74   N  N1    . DC  A 1 9   ? 109.825 92.027  112.406 1.00 35.23  ? 9   DC  E N1    1 
ATOM   75   C  C2    . DC  A 1 9   ? 108.899 92.549  111.501 1.00 33.85  ? 9   DC  E C2    1 
ATOM   76   O  O2    . DC  A 1 9   ? 109.273 92.841  110.362 1.00 36.48  ? 9   DC  E O2    1 
ATOM   77   N  N3    . DC  A 1 9   ? 107.616 92.723  111.900 1.00 31.47  ? 9   DC  E N3    1 
ATOM   78   C  C4    . DC  A 1 9   ? 107.253 92.397  113.139 1.00 36.57  ? 9   DC  E C4    1 
ATOM   79   N  N4    . DC  A 1 9   ? 105.977 92.586  113.490 1.00 42.42  ? 9   DC  E N4    1 
ATOM   80   C  C5    . DC  A 1 9   ? 108.183 91.863  114.079 1.00 42.16  ? 9   DC  E C5    1 
ATOM   81   C  C6    . DC  A 1 9   ? 109.445 91.697  113.673 1.00 41.80  ? 9   DC  E C6    1 
ATOM   82   P  P     . DT  A 1 10  ? 114.786 94.453  113.395 1.00 56.53  ? 10  DT  E P     1 
ATOM   83   O  OP1   . DT  A 1 10  ? 116.249 94.641  113.468 1.00 68.57  ? 10  DT  E OP1   1 
ATOM   84   O  OP2   . DT  A 1 10  ? 113.932 94.846  114.538 1.00 60.09  ? 10  DT  E OP2   1 
ATOM   85   O  "O5'" . DT  A 1 10  ? 114.260 95.208  112.089 1.00 46.94  ? 10  DT  E "O5'" 1 
ATOM   86   C  "C5'" . DT  A 1 10  ? 115.102 95.307  110.947 1.00 48.75  ? 10  DT  E "C5'" 1 
ATOM   87   C  "C4'" . DT  A 1 10  ? 114.440 96.118  109.845 1.00 45.92  ? 10  DT  E "C4'" 1 
ATOM   88   O  "O4'" . DT  A 1 10  ? 113.129 95.574  109.555 1.00 37.16  ? 10  DT  E "O4'" 1 
ATOM   89   C  "C3'" . DT  A 1 10  ? 114.174 97.567  110.187 1.00 45.04  ? 10  DT  E "C3'" 1 
ATOM   90   O  "O3'" . DT  A 1 10  ? 115.318 98.372  109.977 1.00 48.25  ? 10  DT  E "O3'" 1 
ATOM   91   C  "C2'" . DT  A 1 10  ? 113.042 97.921  109.244 1.00 39.67  ? 10  DT  E "C2'" 1 
ATOM   92   C  "C1'" . DT  A 1 10  ? 112.259 96.620  109.139 1.00 34.32  ? 10  DT  E "C1'" 1 
ATOM   93   N  N1    . DT  A 1 10  ? 111.028 96.593  109.981 1.00 31.31  ? 10  DT  E N1    1 
ATOM   94   C  C2    . DT  A 1 10  ? 109.850 97.065  109.458 1.00 28.51  ? 10  DT  E C2    1 
ATOM   95   O  O2    . DT  A 1 10  ? 109.756 97.518  108.336 1.00 30.30  ? 10  DT  E O2    1 
ATOM   96   N  N3    . DT  A 1 10  ? 108.776 96.992  110.300 1.00 30.11  ? 10  DT  E N3    1 
ATOM   97   C  C4    . DT  A 1 10  ? 108.760 96.504  111.587 1.00 35.64  ? 10  DT  E C4    1 
ATOM   98   O  O4    . DT  A 1 10  ? 107.742 96.481  112.266 1.00 36.42  ? 10  DT  E O4    1 
ATOM   99   C  C5    . DT  A 1 10  ? 110.022 96.022  112.080 1.00 36.14  ? 10  DT  E C5    1 
ATOM   100  C  C7    . DT  A 1 10  ? 110.112 95.482  113.473 1.00 34.42  ? 10  DT  E C7    1 
ATOM   101  C  C6    . DT  A 1 10  ? 111.089 96.089  111.264 1.00 36.52  ? 10  DT  E C6    1 
ATOM   102  P  P     . DC  A 1 11  ? 115.326 99.888  110.504 1.00 55.20  ? 11  DC  E P     1 
ATOM   103  O  OP1   . DC  A 1 11  ? 116.667 100.453 110.255 1.00 59.97  ? 11  DC  E OP1   1 
ATOM   104  O  OP2   . DC  A 1 11  ? 114.761 99.876  111.872 1.00 49.65  ? 11  DC  E OP2   1 
ATOM   105  O  "O5'" . DC  A 1 11  ? 114.293 100.634 109.541 1.00 50.59  ? 11  DC  E "O5'" 1 
ATOM   106  C  "C5'" . DC  A 1 11  ? 114.666 100.963 108.206 1.00 52.03  ? 11  DC  E "C5'" 1 
ATOM   107  C  "C4'" . DC  A 1 11  ? 113.658 101.912 107.583 1.00 52.66  ? 11  DC  E "C4'" 1 
ATOM   108  O  "O4'" . DC  A 1 11  ? 112.385 101.234 107.458 1.00 45.71  ? 11  DC  E "O4'" 1 
ATOM   109  C  "C3'" . DC  A 1 11  ? 113.377 103.166 108.395 1.00 52.37  ? 11  DC  E "C3'" 1 
ATOM   110  O  "O3'" . DC  A 1 11  ? 114.244 104.221 108.006 1.00 52.32  ? 11  DC  E "O3'" 1 
ATOM   111  C  "C2'" . DC  A 1 11  ? 111.919 103.475 108.084 1.00 44.78  ? 11  DC  E "C2'" 1 
ATOM   112  C  "C1'" . DC  A 1 11  ? 111.318 102.108 107.779 1.00 40.29  ? 11  DC  E "C1'" 1 
ATOM   113  N  N1    . DC  A 1 11  ? 110.553 101.513 108.912 1.00 33.14  ? 11  DC  E N1    1 
ATOM   114  C  C2    . DC  A 1 11  ? 109.176 101.698 108.985 1.00 29.98  ? 11  DC  E C2    1 
ATOM   115  O  O2    . DC  A 1 11  ? 108.619 102.364 108.113 1.00 31.53  ? 11  DC  E O2    1 
ATOM   116  N  N3    . DC  A 1 11  ? 108.493 101.140 110.013 1.00 27.12  ? 11  DC  E N3    1 
ATOM   117  C  C4    . DC  A 1 11  ? 109.138 100.426 110.932 1.00 28.43  ? 11  DC  E C4    1 
ATOM   118  N  N4    . DC  A 1 11  ? 108.429 99.896  111.932 1.00 27.42  ? 11  DC  E N4    1 
ATOM   119  C  C5    . DC  A 1 11  ? 110.544 100.223 110.870 1.00 31.94  ? 11  DC  E C5    1 
ATOM   120  C  C6    . DC  A 1 11  ? 111.204 100.782 109.854 1.00 33.85  ? 11  DC  E C6    1 
ATOM   121  P  P     . DT  A 1 12  ? 114.550 105.427 109.020 1.00 61.78  ? 12  DT  E P     1 
ATOM   122  O  OP1   . DT  A 1 12  ? 115.530 106.313 108.356 1.00 61.45  ? 12  DT  E OP1   1 
ATOM   123  O  OP2   . DT  A 1 12  ? 114.859 104.845 110.345 1.00 61.67  ? 12  DT  E OP2   1 
ATOM   124  O  "O5'" . DT  A 1 12  ? 113.152 106.193 109.128 1.00 54.12  ? 12  DT  E "O5'" 1 
ATOM   125  C  "C5'" . DT  A 1 12  ? 112.645 106.890 108.004 1.00 54.54  ? 12  DT  E "C5'" 1 
ATOM   126  C  "C4'" . DT  A 1 12  ? 111.206 107.316 108.226 1.00 51.26  ? 12  DT  E "C4'" 1 
ATOM   127  O  "O4'" . DT  A 1 12  ? 110.399 106.166 108.555 1.00 37.17  ? 12  DT  E "O4'" 1 
ATOM   128  C  "C3'" . DT  A 1 12  ? 110.986 108.268 109.381 1.00 48.99  ? 12  DT  E "C3'" 1 
ATOM   129  O  "O3'" . DT  A 1 12  ? 111.256 109.618 108.999 1.00 55.83  ? 12  DT  E "O3'" 1 
ATOM   130  C  "C2'" . DT  A 1 12  ? 109.521 108.038 109.723 1.00 42.57  ? 12  DT  E "C2'" 1 
ATOM   131  C  "C1'" . DT  A 1 12  ? 109.278 106.583 109.320 1.00 36.34  ? 12  DT  E "C1'" 1 
ATOM   132  N  N1    . DT  A 1 12  ? 109.118 105.654 110.475 1.00 38.10  ? 12  DT  E N1    1 
ATOM   133  C  C2    . DT  A 1 12  ? 107.873 105.486 111.031 1.00 35.76  ? 12  DT  E C2    1 
ATOM   134  O  O2    . DT  A 1 12  ? 106.883 106.070 110.637 1.00 34.20  ? 12  DT  E O2    1 
ATOM   135  N  N3    . DT  A 1 12  ? 107.825 104.605 112.073 1.00 31.25  ? 12  DT  E N3    1 
ATOM   136  C  C4    . DT  A 1 12  ? 108.872 103.888 112.607 1.00 29.63  ? 12  DT  E C4    1 
ATOM   137  O  O4    . DT  A 1 12  ? 108.723 103.119 113.547 1.00 28.33  ? 12  DT  E O4    1 
ATOM   138  C  C5    . DT  A 1 12  ? 110.152 104.105 111.980 1.00 33.57  ? 12  DT  E C5    1 
ATOM   139  C  C7    . DT  A 1 12  ? 111.363 103.376 112.478 1.00 32.61  ? 12  DT  E C7    1 
ATOM   140  C  C6    . DT  A 1 12  ? 110.215 104.968 110.954 1.00 38.32  ? 12  DT  E C6    1 
ATOM   141  P  P     . DA  A 1 13  ? 111.404 110.763 110.119 1.00 64.93  ? 13  DA  E P     1 
ATOM   142  O  OP1   . DA  A 1 13  ? 111.963 111.968 109.468 1.00 67.57  ? 13  DA  E OP1   1 
ATOM   143  O  OP2   . DA  A 1 13  ? 112.110 110.172 111.276 1.00 55.29  ? 13  DA  E OP2   1 
ATOM   144  O  "O5'" . DA  A 1 13  ? 109.896 111.065 110.557 1.00 58.97  ? 13  DA  E "O5'" 1 
ATOM   145  C  "C5'" . DA  A 1 13  ? 108.941 111.484 109.587 1.00 54.39  ? 13  DA  E "C5'" 1 
ATOM   146  C  "C4'" . DA  A 1 13  ? 107.565 111.646 110.212 1.00 48.77  ? 13  DA  E "C4'" 1 
ATOM   147  O  "O4'" . DA  A 1 13  ? 107.172 110.390 110.840 1.00 43.98  ? 13  DA  E "O4'" 1 
ATOM   148  C  "C3'" . DA  A 1 13  ? 107.485 112.713 111.304 1.00 54.20  ? 13  DA  E "C3'" 1 
ATOM   149  O  "O3'" . DA  A 1 13  ? 106.280 113.465 111.209 1.00 55.56  ? 13  DA  E "O3'" 1 
ATOM   150  C  "C2'" . DA  A 1 13  ? 107.558 111.909 112.589 1.00 48.86  ? 13  DA  E "C2'" 1 
ATOM   151  C  "C1'" . DA  A 1 13  ? 106.887 110.601 112.210 1.00 45.85  ? 13  DA  E "C1'" 1 
ATOM   152  N  N9    . DA  A 1 13  ? 107.374 109.465 112.988 1.00 40.12  ? 13  DA  E N9    1 
ATOM   153  C  C8    . DA  A 1 13  ? 108.640 108.953 112.990 1.00 40.29  ? 13  DA  E C8    1 
ATOM   154  N  N7    . DA  A 1 13  ? 108.798 107.937 113.798 1.00 35.22  ? 13  DA  E N7    1 
ATOM   155  C  C5    . DA  A 1 13  ? 107.556 107.781 114.379 1.00 34.72  ? 13  DA  E C5    1 
ATOM   156  C  C6    . DA  A 1 13  ? 107.070 106.875 115.332 1.00 35.28  ? 13  DA  E C6    1 
ATOM   157  N  N6    . DA  A 1 13  ? 107.824 105.919 115.884 1.00 34.84  ? 13  DA  E N6    1 
ATOM   158  N  N1    . DA  A 1 13  ? 105.778 106.989 115.699 1.00 36.30  ? 13  DA  E N1    1 
ATOM   159  C  C2    . DA  A 1 13  ? 105.034 107.951 115.142 1.00 36.72  ? 13  DA  E C2    1 
ATOM   160  N  N3    . DA  A 1 13  ? 105.383 108.859 114.236 1.00 36.97  ? 13  DA  E N3    1 
ATOM   161  C  C4    . DA  A 1 13  ? 106.667 108.719 113.894 1.00 36.35  ? 13  DA  E C4    1 
ATOM   162  P  P     . DC  A 1 14  ? 106.112 114.820 112.059 1.00 62.05  ? 14  DC  E P     1 
ATOM   163  O  OP1   . DC  A 1 14  ? 105.051 115.625 111.419 1.00 58.90  ? 14  DC  E OP1   1 
ATOM   164  O  OP2   . DC  A 1 14  ? 107.460 115.392 112.274 1.00 59.58  ? 14  DC  E OP2   1 
ATOM   165  O  "O5'" . DC  A 1 14  ? 105.549 114.320 113.464 1.00 62.05  ? 14  DC  E "O5'" 1 
ATOM   166  C  "C5'" . DC  A 1 14  ? 104.239 113.782 113.542 1.00 61.51  ? 14  DC  E "C5'" 1 
ATOM   167  C  "C4'" . DC  A 1 14  ? 103.857 113.492 114.979 1.00 65.31  ? 14  DC  E "C4'" 1 
ATOM   168  O  "O4'" . DC  A 1 14  ? 104.545 112.291 115.429 1.00 57.41  ? 14  DC  E "O4'" 1 
ATOM   169  C  "C3'" . DC  A 1 14  ? 104.226 114.594 115.981 1.00 68.06  ? 14  DC  E "C3'" 1 
ATOM   170  O  "O3'" . DC  A 1 14  ? 103.114 114.902 116.813 1.00 74.60  ? 14  DC  E "O3'" 1 
ATOM   171  C  "C2'" . DC  A 1 14  ? 105.381 113.982 116.765 1.00 61.49  ? 14  DC  E "C2'" 1 
ATOM   172  C  "C1'" . DC  A 1 14  ? 105.021 112.508 116.727 1.00 54.63  ? 14  DC  E "C1'" 1 
ATOM   173  N  N1    . DC  A 1 14  ? 106.155 111.583 117.010 1.00 48.56  ? 14  DC  E N1    1 
ATOM   174  C  C2    . DC  A 1 14  ? 105.980 110.554 117.938 1.00 47.24  ? 14  DC  E C2    1 
ATOM   175  O  O2    . DC  A 1 14  ? 104.883 110.432 118.493 1.00 52.23  ? 14  DC  E O2    1 
ATOM   176  N  N3    . DC  A 1 14  ? 107.016 109.725 118.205 1.00 44.86  ? 14  DC  E N3    1 
ATOM   177  C  C4    . DC  A 1 14  ? 108.184 109.899 117.585 1.00 42.31  ? 14  DC  E C4    1 
ATOM   178  N  N4    . DC  A 1 14  ? 109.179 109.057 117.882 1.00 42.72  ? 14  DC  E N4    1 
ATOM   179  C  C5    . DC  A 1 14  ? 108.383 110.945 116.634 1.00 43.72  ? 14  DC  E C5    1 
ATOM   180  C  C6    . DC  A 1 14  ? 107.351 111.755 116.381 1.00 46.63  ? 14  DC  E C6    1 
ATOM   181  P  P     . DG  A 1 15  ? 102.939 116.368 117.447 1.00 90.33  ? 15  DG  E P     1 
ATOM   182  O  OP1   . DG  A 1 15  ? 101.892 117.063 116.668 1.00 81.87  ? 15  DG  E OP1   1 
ATOM   183  O  OP2   . DG  A 1 15  ? 104.280 116.975 117.591 1.00 88.50  ? 15  DG  E OP2   1 
ATOM   184  O  "O5'" . DG  A 1 15  ? 102.373 116.075 118.914 1.00 86.05  ? 15  DG  E "O5'" 1 
ATOM   185  C  "C5'" . DG  A 1 15  ? 101.208 115.274 119.078 1.00 80.65  ? 15  DG  E "C5'" 1 
ATOM   186  C  "C4'" . DG  A 1 15  ? 101.246 114.516 120.396 1.00 76.88  ? 15  DG  E "C4'" 1 
ATOM   187  O  "O4'" . DG  A 1 15  ? 102.253 113.472 120.319 1.00 65.59  ? 15  DG  E "O4'" 1 
ATOM   188  C  "C3'" . DG  A 1 15  ? 101.595 115.374 121.616 1.00 78.98  ? 15  DG  E "C3'" 1 
ATOM   189  O  "O3'" . DG  A 1 15  ? 100.611 115.238 122.631 1.00 82.32  ? 15  DG  E "O3'" 1 
ATOM   190  C  "C2'" . DG  A 1 15  ? 102.961 114.861 122.062 1.00 74.79  ? 15  DG  E "C2'" 1 
ATOM   191  C  "C1'" . DG  A 1 15  ? 103.006 113.450 121.503 1.00 67.89  ? 15  DG  E "C1'" 1 
ATOM   192  N  N9    . DG  A 1 15  ? 104.355 112.999 121.198 1.00 62.88  ? 15  DG  E N9    1 
ATOM   193  C  C8    . DG  A 1 15  ? 105.200 113.509 120.246 1.00 61.38  ? 15  DG  E C8    1 
ATOM   194  N  N7    . DG  A 1 15  ? 106.357 112.915 120.209 1.00 56.86  ? 15  DG  E N7    1 
ATOM   195  C  C5    . DG  A 1 15  ? 106.276 111.956 121.205 1.00 60.22  ? 15  DG  E C5    1 
ATOM   196  C  C6    . DG  A 1 15  ? 107.226 111.008 121.633 1.00 65.27  ? 15  DG  E C6    1 
ATOM   197  O  O6    . DG  A 1 15  ? 108.371 110.820 121.202 1.00 65.32  ? 15  DG  E O6    1 
ATOM   198  N  N1    . DG  A 1 15  ? 106.740 110.228 122.671 1.00 69.02  ? 15  DG  E N1    1 
ATOM   199  C  C2    . DG  A 1 15  ? 105.489 110.346 123.228 1.00 69.71  ? 15  DG  E C2    1 
ATOM   200  N  N2    . DG  A 1 15  ? 105.203 109.501 124.225 1.00 69.27  ? 15  DG  E N2    1 
ATOM   201  N  N3    . DG  A 1 15  ? 104.587 111.231 122.837 1.00 67.11  ? 15  DG  E N3    1 
ATOM   202  C  C4    . DG  A 1 15  ? 105.048 111.998 121.824 1.00 63.22  ? 15  DG  E C4    1 
ATOM   203  P  P     . DG  A 1 16  ? 100.593 116.250 123.880 1.00 91.40  ? 16  DG  E P     1 
ATOM   204  O  OP1   . DG  A 1 16  ? 99.202  116.297 124.382 1.00 85.17  ? 16  DG  E OP1   1 
ATOM   205  O  OP2   . DG  A 1 16  ? 101.255 117.506 123.466 1.00 84.21  ? 16  DG  E OP2   1 
ATOM   206  O  "O5'" . DG  A 1 16  ? 101.531 115.536 124.961 1.00 81.75  ? 16  DG  E "O5'" 1 
ATOM   207  C  "C5'" . DG  A 1 16  ? 101.175 114.262 125.477 1.00 68.48  ? 16  DG  E "C5'" 1 
ATOM   208  C  "C4'" . DG  A 1 16  ? 102.257 113.721 126.389 1.00 70.57  ? 16  DG  E "C4'" 1 
ATOM   209  O  "O4'" . DG  A 1 16  ? 103.414 113.322 125.591 1.00 67.40  ? 16  DG  E "O4'" 1 
ATOM   210  C  "C3'" . DG  A 1 16  ? 102.786 114.723 127.423 1.00 85.74  ? 16  DG  E "C3'" 1 
ATOM   211  O  "O3'" . DG  A 1 16  ? 102.912 114.106 128.704 1.00 94.67  ? 16  DG  E "O3'" 1 
ATOM   212  C  "C2'" . DG  A 1 16  ? 104.133 115.124 126.845 1.00 87.58  ? 16  DG  E "C2'" 1 
ATOM   213  C  "C1'" . DG  A 1 16  ? 104.573 113.823 126.210 1.00 79.89  ? 16  DG  E "C1'" 1 
ATOM   214  N  N9    . DG  A 1 16  ? 105.649 113.959 125.233 1.00 79.88  ? 16  DG  E N9    1 
ATOM   215  C  C8    . DG  A 1 16  ? 105.692 114.788 124.141 1.00 77.49  ? 16  DG  E C8    1 
ATOM   216  N  N7    . DG  A 1 16  ? 106.804 114.692 123.461 1.00 76.93  ? 16  DG  E N7    1 
ATOM   217  C  C5    . DG  A 1 16  ? 107.542 113.741 124.153 1.00 81.80  ? 16  DG  E C5    1 
ATOM   218  C  C6    . DG  A 1 16  ? 108.833 113.214 123.898 1.00 87.82  ? 16  DG  E C6    1 
ATOM   219  O  O6    . DG  A 1 16  ? 109.613 113.487 122.976 1.00 93.91  ? 16  DG  E O6    1 
ATOM   220  N  N1    . DG  A 1 16  ? 109.197 112.269 124.848 1.00 88.14  ? 16  DG  E N1    1 
ATOM   221  C  C2    . DG  A 1 16  ? 108.420 111.885 125.909 1.00 89.59  ? 16  DG  E C2    1 
ATOM   222  N  N2    . DG  A 1 16  ? 108.946 110.964 126.722 1.00 97.65  ? 16  DG  E N2    1 
ATOM   223  N  N3    . DG  A 1 16  ? 107.215 112.367 126.160 1.00 85.99  ? 16  DG  E N3    1 
ATOM   224  C  C4    . DG  A 1 16  ? 106.843 113.286 125.245 1.00 81.42  ? 16  DG  E C4    1 
ATOM   225  P  P     . DA  A 1 17  ? 103.078 114.991 130.035 1.00 96.67  ? 17  DA  E P     1 
ATOM   226  O  OP1   . DA  A 1 17  ? 101.760 115.601 130.318 1.00 94.95  ? 17  DA  E OP1   1 
ATOM   227  O  OP2   . DA  A 1 17  ? 104.257 115.868 129.868 1.00 101.37 ? 17  DA  E OP2   1 
ATOM   228  O  "O5'" . DA  A 1 17  ? 103.408 113.904 131.166 1.00 92.06  ? 17  DA  E "O5'" 1 
ATOM   229  C  "C5'" . DA  A 1 17  ? 104.353 114.193 132.197 1.00 102.51 ? 17  DA  E "C5'" 1 
ATOM   230  C  "C4'" . DA  A 1 17  ? 105.505 113.206 132.167 1.00 102.98 ? 17  DA  E "C4'" 1 
ATOM   231  O  "O4'" . DA  A 1 17  ? 105.966 113.068 130.802 1.00 95.80  ? 17  DA  E "O4'" 1 
ATOM   232  C  "C3'" . DA  A 1 17  ? 106.720 113.602 133.011 1.00 106.97 ? 17  DA  E "C3'" 1 
ATOM   233  O  "O3'" . DA  A 1 17  ? 107.069 112.567 133.911 1.00 101.62 ? 17  DA  E "O3'" 1 
ATOM   234  C  "C2'" . DA  A 1 17  ? 107.830 113.875 132.003 1.00 110.54 ? 17  DA  E "C2'" 1 
ATOM   235  C  "C1'" . DA  A 1 17  ? 107.367 113.173 130.736 1.00 102.84 ? 17  DA  E "C1'" 1 
ATOM   236  N  N9    . DA  A 1 17  ? 107.713 113.901 129.525 1.00 99.63  ? 17  DA  E N9    1 
ATOM   237  C  C8    . DA  A 1 17  ? 106.922 114.772 128.836 1.00 95.44  ? 17  DA  E C8    1 
ATOM   238  N  N7    . DA  A 1 17  ? 107.502 115.292 127.782 1.00 97.01  ? 17  DA  E N7    1 
ATOM   239  C  C5    . DA  A 1 17  ? 108.763 114.725 127.788 1.00 104.35 ? 17  DA  E C5    1 
ATOM   240  C  C6    . DA  A 1 17  ? 109.870 114.866 126.932 1.00 109.04 ? 17  DA  E C6    1 
ATOM   241  N  N6    . DA  A 1 17  ? 109.868 115.662 125.859 1.00 107.28 ? 17  DA  E N6    1 
ATOM   242  N  N1    . DA  A 1 17  ? 110.980 114.149 127.223 1.00 114.99 ? 17  DA  E N1    1 
ATOM   243  C  C2    . DA  A 1 17  ? 110.970 113.364 128.305 1.00 116.99 ? 17  DA  E C2    1 
ATOM   244  N  N3    . DA  A 1 17  ? 109.989 113.149 129.175 1.00 115.24 ? 17  DA  E N3    1 
ATOM   245  C  C4    . DA  A 1 17  ? 108.907 113.867 128.858 1.00 107.30 ? 17  DA  E C4    1 
ATOM   246  P  P     . DT  A 1 18  ? 108.002 112.895 135.176 1.00 109.93 ? 18  DT  E P     1 
ATOM   247  O  OP1   . DT  A 1 18  ? 108.087 111.674 136.005 1.00 111.46 ? 18  DT  E OP1   1 
ATOM   248  O  OP2   . DT  A 1 18  ? 107.510 114.161 135.764 1.00 115.08 ? 18  DT  E OP2   1 
ATOM   249  O  "O5'" . DT  A 1 18  ? 109.438 113.178 134.534 1.00 119.75 ? 18  DT  E "O5'" 1 
ATOM   250  C  "C5'" . DT  A 1 18  ? 110.212 112.100 134.024 1.00 122.22 ? 18  DT  E "C5'" 1 
ATOM   251  C  "C4'" . DT  A 1 18  ? 111.643 112.531 133.763 1.00 138.39 ? 18  DT  E "C4'" 1 
ATOM   252  O  "O4'" . DT  A 1 18  ? 111.720 113.202 132.469 1.00 135.62 ? 18  DT  E "O4'" 1 
ATOM   253  C  "C3'" . DT  A 1 18  ? 112.216 113.521 134.782 1.00 149.16 ? 18  DT  E "C3'" 1 
ATOM   254  O  "O3'" . DT  A 1 18  ? 113.560 113.175 135.122 1.00 162.00 ? 18  DT  E "O3'" 1 
ATOM   255  C  "C2'" . DT  A 1 18  ? 112.131 114.852 134.047 1.00 150.34 ? 18  DT  E "C2'" 1 
ATOM   256  C  "C1'" . DT  A 1 18  ? 112.410 114.422 132.620 1.00 147.69 ? 18  DT  E "C1'" 1 
ATOM   257  N  N1    . DT  A 1 18  ? 111.956 115.383 131.553 1.00 143.47 ? 18  DT  E N1    1 
ATOM   258  C  C2    . DT  A 1 18  ? 112.807 115.672 130.508 1.00 148.46 ? 18  DT  E C2    1 
ATOM   259  O  O2    . DT  A 1 18  ? 113.920 115.191 130.403 1.00 154.81 ? 18  DT  E O2    1 
ATOM   260  N  N3    . DT  A 1 18  ? 112.306 116.541 129.577 1.00 144.38 ? 18  DT  E N3    1 
ATOM   261  C  C4    . DT  A 1 18  ? 111.069 117.148 129.591 1.00 137.15 ? 18  DT  E C4    1 
ATOM   262  O  O4    . DT  A 1 18  ? 110.711 117.921 128.711 1.00 138.62 ? 18  DT  E O4    1 
ATOM   263  C  C5    . DT  A 1 18  ? 110.224 116.807 130.706 1.00 129.50 ? 18  DT  E C5    1 
ATOM   264  C  C7    . DT  A 1 18  ? 108.862 117.414 130.813 1.00 122.53 ? 18  DT  E C7    1 
ATOM   265  C  C6    . DT  A 1 18  ? 110.699 115.948 131.626 1.00 133.44 ? 18  DT  E C6    1 
ATOM   266  P  P     . DG  A 1 19  ? 114.167 113.548 136.563 1.00 172.50 ? 19  DG  E P     1 
ATOM   267  O  OP1   . DG  A 1 19  ? 113.571 112.617 137.545 1.00 166.82 ? 19  DG  E OP1   1 
ATOM   268  O  OP2   . DG  A 1 19  ? 114.016 115.007 136.759 1.00 174.60 ? 19  DG  E OP2   1 
ATOM   269  O  "O5'" . DG  A 1 19  ? 115.724 113.195 136.418 1.00 183.95 ? 19  DG  E "O5'" 1 
ATOM   270  C  "C5'" . DG  A 1 19  ? 116.724 114.130 136.820 1.00 189.42 ? 19  DG  E "C5'" 1 
ATOM   271  C  "C4'" . DG  A 1 19  ? 117.782 114.278 135.744 1.00 199.21 ? 19  DG  E "C4'" 1 
ATOM   272  O  "O4'" . DG  A 1 19  ? 117.134 114.614 134.486 1.00 197.49 ? 19  DG  E "O4'" 1 
ATOM   273  C  "C3'" . DG  A 1 19  ? 118.808 115.375 135.993 1.00 208.55 ? 19  DG  E "C3'" 1 
ATOM   274  O  "O3'" . DG  A 1 19  ? 120.094 114.992 135.503 1.00 217.52 ? 19  DG  E "O3'" 1 
ATOM   275  C  "C2'" . DG  A 1 19  ? 118.241 116.568 135.247 1.00 205.27 ? 19  DG  E "C2'" 1 
ATOM   276  C  "C1'" . DG  A 1 19  ? 117.458 115.936 134.097 1.00 198.81 ? 19  DG  E "C1'" 1 
ATOM   277  N  N9    . DG  A 1 19  ? 116.224 116.652 133.773 1.00 187.29 ? 19  DG  E N9    1 
ATOM   278  C  C8    . DG  A 1 19  ? 115.079 116.723 134.524 1.00 180.17 ? 19  DG  E C8    1 
ATOM   279  N  N7    . DG  A 1 19  ? 114.138 117.448 133.974 1.00 174.37 ? 19  DG  E N7    1 
ATOM   280  C  C5    . DG  A 1 19  ? 114.701 117.887 132.784 1.00 178.81 ? 19  DG  E C5    1 
ATOM   281  C  C6    . DG  A 1 19  ? 114.166 118.712 131.759 1.00 175.74 ? 19  DG  E C6    1 
ATOM   282  O  O6    . DG  A 1 19  ? 113.042 119.236 131.690 1.00 170.53 ? 19  DG  E O6    1 
ATOM   283  N  N1    . DG  A 1 19  ? 115.084 118.905 130.728 1.00 183.42 ? 19  DG  E N1    1 
ATOM   284  C  C2    . DG  A 1 19  ? 116.355 118.374 130.696 1.00 188.90 ? 19  DG  E C2    1 
ATOM   285  N  N2    . DG  A 1 19  ? 117.099 118.665 129.622 1.00 189.69 ? 19  DG  E N2    1 
ATOM   286  N  N3    . DG  A 1 19  ? 116.860 117.606 131.644 1.00 191.12 ? 19  DG  E N3    1 
ATOM   287  C  C4    . DG  A 1 19  ? 115.984 117.402 132.649 1.00 186.17 ? 19  DG  E C4    1 
ATOM   288  P  P     . DC  A 1 20  ? 121.394 115.872 135.856 1.00 228.85 ? 20  DC  E P     1 
ATOM   289  O  OP1   . DC  A 1 20  ? 122.568 114.974 135.781 1.00 231.46 ? 20  DC  E OP1   1 
ATOM   290  O  OP2   . DC  A 1 20  ? 121.115 116.597 137.117 1.00 226.46 ? 20  DC  E OP2   1 
ATOM   291  O  "O5'" . DC  A 1 20  ? 121.478 116.938 134.661 1.00 225.52 ? 20  DC  E "O5'" 1 
ATOM   292  C  "C5'" . DC  A 1 20  ? 121.879 116.512 133.357 1.00 227.31 ? 20  DC  E "C5'" 1 
ATOM   293  C  "C4'" . DC  A 1 20  ? 122.128 117.696 132.438 1.00 230.63 ? 20  DC  E "C4'" 1 
ATOM   294  O  "O4'" . DC  A 1 20  ? 120.857 118.213 131.959 1.00 220.46 ? 20  DC  E "O4'" 1 
ATOM   295  C  "C3'" . DC  A 1 20  ? 122.866 118.864 133.083 1.00 237.72 ? 20  DC  E "C3'" 1 
ATOM   296  O  "O3'" . DC  A 1 20  ? 123.967 119.248 132.273 1.00 247.60 ? 20  DC  E "O3'" 1 
ATOM   297  C  "C2'" . DC  A 1 20  ? 121.813 119.966 133.207 1.00 231.01 ? 20  DC  E "C2'" 1 
ATOM   298  C  "C1'" . DC  A 1 20  ? 120.782 119.610 132.144 1.00 222.62 ? 20  DC  E "C1'" 1 
ATOM   299  N  N1    . DC  A 1 20  ? 119.371 119.955 132.524 1.00 212.38 ? 20  DC  E N1    1 
ATOM   300  C  C2    . DC  A 1 20  ? 118.611 120.806 131.712 1.00 208.96 ? 20  DC  E C2    1 
ATOM   301  O  O2    . DC  A 1 20  ? 119.115 121.283 130.692 1.00 211.37 ? 20  DC  E O2    1 
ATOM   302  N  N3    . DC  A 1 20  ? 117.339 121.098 132.080 1.00 202.85 ? 20  DC  E N3    1 
ATOM   303  C  C4    . DC  A 1 20  ? 116.823 120.571 133.190 1.00 198.26 ? 20  DC  E C4    1 
ATOM   304  N  N4    . DC  A 1 20  ? 115.564 120.890 133.508 1.00 194.33 ? 20  DC  E N4    1 
ATOM   305  C  C5    . DC  A 1 20  ? 117.579 119.701 134.028 1.00 200.15 ? 20  DC  E C5    1 
ATOM   306  C  C6    . DC  A 1 20  ? 118.833 119.421 133.656 1.00 207.23 ? 20  DC  E C6    1 
ATOM   307  P  P     . DC  A 1 21  ? 125.107 120.216 132.854 1.00 257.95 ? 21  DC  E P     1 
ATOM   308  O  OP1   . DC  A 1 21  ? 126.402 119.771 132.291 1.00 260.74 ? 21  DC  E OP1   1 
ATOM   309  O  OP2   . DC  A 1 21  ? 124.941 120.262 134.325 1.00 254.96 ? 21  DC  E OP2   1 
ATOM   310  O  "O5'" . DC  A 1 21  ? 124.729 121.641 132.230 1.00 249.53 ? 21  DC  E "O5'" 1 
ATOM   311  C  "C5'" . DC  A 1 21  ? 124.635 121.797 130.806 1.00 247.05 ? 21  DC  E "C5'" 1 
ATOM   312  C  "C4'" . DC  A 1 21  ? 123.956 123.106 130.444 1.00 245.99 ? 21  DC  E "C4'" 1 
ATOM   313  O  "O4'" . DC  A 1 21  ? 122.524 122.959 130.529 1.00 237.72 ? 21  DC  E "O4'" 1 
ATOM   314  C  "C3'" . DC  A 1 21  ? 124.299 124.262 131.360 1.00 246.60 ? 21  DC  E "C3'" 1 
ATOM   315  O  "O3'" . DC  A 1 21  ? 125.392 124.981 130.825 1.00 250.66 ? 21  DC  E "O3'" 1 
ATOM   316  C  "C2'" . DC  A 1 21  ? 123.012 125.097 131.432 1.00 241.82 ? 21  DC  E "C2'" 1 
ATOM   317  C  "C1'" . DC  A 1 21  ? 121.935 124.218 130.799 1.00 235.94 ? 21  DC  E "C1'" 1 
ATOM   318  N  N1    . DC  A 1 21  ? 120.745 124.002 131.679 1.00 227.81 ? 21  DC  E N1    1 
ATOM   319  C  C2    . DC  A 1 21  ? 119.524 124.633 131.383 1.00 223.00 ? 21  DC  E C2    1 
ATOM   320  O  O2    . DC  A 1 21  ? 119.441 125.372 130.394 1.00 222.97 ? 21  DC  E O2    1 
ATOM   321  N  N3    . DC  A 1 21  ? 118.463 124.411 132.197 1.00 219.16 ? 21  DC  E N3    1 
ATOM   322  C  C4    . DC  A 1 21  ? 118.585 123.611 133.254 1.00 217.68 ? 21  DC  E C4    1 
ATOM   323  N  N4    . DC  A 1 21  ? 117.513 123.420 134.025 1.00 214.36 ? 21  DC  E N4    1 
ATOM   324  C  C5    . DC  A 1 21  ? 119.814 122.965 133.572 1.00 219.82 ? 21  DC  E C5    1 
ATOM   325  C  C6    . DC  A 1 21  ? 120.856 123.183 132.765 1.00 224.80 ? 21  DC  E C6    1 
ATOM   326  P  P     . DT  A 1 22  ? 126.215 126.010 131.736 1.00 251.58 ? 22  DT  E P     1 
ATOM   327  O  OP1   . DT  A 1 22  ? 127.567 126.148 131.150 1.00 251.78 ? 22  DT  E OP1   1 
ATOM   328  O  OP2   . DT  A 1 22  ? 126.075 125.579 133.148 1.00 251.06 ? 22  DT  E OP2   1 
ATOM   329  O  "O5'" . DT  A 1 22  ? 125.416 127.375 131.534 1.00 251.94 ? 22  DT  E "O5'" 1 
ATOM   330  C  "C5'" . DT  A 1 22  ? 124.946 127.735 130.233 1.00 251.67 ? 22  DT  E "C5'" 1 
ATOM   331  C  "C4'" . DT  A 1 22  ? 123.803 128.733 130.329 1.00 250.32 ? 22  DT  E "C4'" 1 
ATOM   332  O  "O4'" . DT  A 1 22  ? 122.549 128.073 130.619 1.00 245.11 ? 22  DT  E "O4'" 1 
ATOM   333  C  "C3'" . DT  A 1 22  ? 123.954 129.739 131.439 1.00 251.66 ? 22  DT  E "C3'" 1 
ATOM   334  O  "O3'" . DT  A 1 22  ? 124.785 130.805 131.007 1.00 254.58 ? 22  DT  E "O3'" 1 
ATOM   335  C  "C2'" . DT  A 1 22  ? 122.506 130.169 131.726 1.00 249.40 ? 22  DT  E "C2'" 1 
ATOM   336  C  "C1'" . DT  A 1 22  ? 121.645 129.039 131.135 1.00 243.62 ? 22  DT  E "C1'" 1 
ATOM   337  N  N1    . DT  A 1 22  ? 120.722 128.374 132.139 1.00 238.39 ? 22  DT  E N1    1 
ATOM   338  C  C2    . DT  A 1 22  ? 119.368 128.697 132.162 1.00 233.53 ? 22  DT  E C2    1 
ATOM   339  O  O2    . DT  A 1 22  ? 118.860 129.508 131.411 1.00 232.96 ? 22  DT  E O2    1 
ATOM   340  N  N3    . DT  A 1 22  ? 118.636 128.021 133.117 1.00 228.10 ? 22  DT  E N3    1 
ATOM   341  C  C4    . DT  A 1 22  ? 119.116 127.082 134.019 1.00 226.30 ? 22  DT  E C4    1 
ATOM   342  O  O4    . DT  A 1 22  ? 118.403 126.523 134.839 1.00 222.83 ? 22  DT  E O4    1 
ATOM   343  C  C5    . DT  A 1 22  ? 120.528 126.800 133.933 1.00 229.80 ? 22  DT  E C5    1 
ATOM   344  C  C7    . DT  A 1 22  ? 121.154 125.801 134.866 1.00 228.12 ? 22  DT  E C7    1 
ATOM   345  C  C6    . DT  A 1 22  ? 121.251 127.449 133.014 1.00 234.92 ? 22  DT  E C6    1 
ATOM   346  P  P     . DC  A 1 23  ? 125.729 131.584 132.044 1.00 257.74 ? 23  DC  E P     1 
ATOM   347  O  OP1   . DC  A 1 23  ? 126.900 132.085 131.290 1.00 257.87 ? 23  DC  E OP1   1 
ATOM   348  O  OP2   . DC  A 1 23  ? 125.953 130.719 133.225 1.00 257.15 ? 23  DC  E OP2   1 
ATOM   349  O  "O5'" . DC  A 1 23  ? 124.822 132.824 132.467 1.00 259.74 ? 23  DC  E "O5'" 1 
ATOM   350  C  "C5'" . DC  A 1 23  ? 124.097 133.525 131.462 1.00 258.47 ? 23  DC  E "C5'" 1 
ATOM   351  C  "C4'" . DC  A 1 23  ? 122.783 134.043 131.999 1.00 258.84 ? 23  DC  E "C4'" 1 
ATOM   352  O  "O4'" . DC  A 1 23  ? 121.935 132.953 132.408 1.00 255.47 ? 23  DC  E "O4'" 1 
ATOM   353  C  "C3'" . DC  A 1 23  ? 122.916 134.899 133.226 1.00 261.36 ? 23  DC  E "C3'" 1 
ATOM   354  O  "O3'" . DC  A 1 23  ? 123.206 136.216 132.833 1.00 264.30 ? 23  DC  E "O3'" 1 
ATOM   355  C  "C2'" . DC  A 1 23  ? 121.554 134.752 133.911 1.00 258.97 ? 23  DC  E "C2'" 1 
ATOM   356  C  "C1'" . DC  A 1 23  ? 121.005 133.429 133.365 1.00 255.42 ? 23  DC  E "C1'" 1 
ATOM   357  N  N1    . DC  A 1 23  ? 120.821 132.380 134.389 1.00 253.34 ? 23  DC  E N1    1 
ATOM   358  C  C2    . DC  A 1 23  ? 119.543 132.127 134.914 1.00 248.79 ? 23  DC  E C2    1 
ATOM   359  O  O2    . DC  A 1 23  ? 118.571 132.798 134.526 1.00 246.82 ? 23  DC  E O2    1 
ATOM   360  N  N3    . DC  A 1 23  ? 119.409 131.150 135.839 1.00 245.73 ? 23  DC  E N3    1 
ATOM   361  C  C4    . DC  A 1 23  ? 120.473 130.448 136.230 1.00 244.22 ? 23  DC  E C4    1 
ATOM   362  N  N4    . DC  A 1 23  ? 120.296 129.494 137.138 1.00 240.36 ? 23  DC  E N4    1 
ATOM   363  C  C5    . DC  A 1 23  ? 121.770 130.686 135.705 1.00 247.62 ? 23  DC  E C5    1 
ATOM   364  C  C6    . DC  A 1 23  ? 121.900 131.650 134.799 1.00 252.78 ? 23  DC  E C6    1 
ATOM   365  P  P     . DA  A 1 24  ? 124.056 137.190 133.779 1.00 267.41 ? 24  DA  E P     1 
ATOM   366  O  OP1   . DA  A 1 24  ? 124.682 138.196 132.894 1.00 267.72 ? 24  DA  E OP1   1 
ATOM   367  O  OP2   . DA  A 1 24  ? 124.912 136.374 134.673 1.00 266.44 ? 24  DA  E OP2   1 
ATOM   368  O  "O5'" . DA  A 1 24  ? 122.917 137.899 134.633 1.00 266.00 ? 24  DA  E "O5'" 1 
ATOM   369  C  "C5'" . DA  A 1 24  ? 121.699 138.257 133.988 1.00 264.04 ? 24  DA  E "C5'" 1 
ATOM   370  C  "C4'" . DA  A 1 24  ? 120.536 138.220 134.953 1.00 262.96 ? 24  DA  E "C4'" 1 
ATOM   371  O  "O4'" . DA  A 1 24  ? 120.140 136.861 135.246 1.00 259.44 ? 24  DA  E "O4'" 1 
ATOM   372  C  "C3'" . DA  A 1 24  ? 120.823 138.805 136.305 1.00 263.44 ? 24  DA  E "C3'" 1 
ATOM   373  O  "O3'" . DA  A 1 24  ? 120.750 140.214 136.246 1.00 266.53 ? 24  DA  E "O3'" 1 
ATOM   374  C  "C2'" . DA  A 1 24  ? 119.725 138.177 137.173 1.00 260.00 ? 24  DA  E "C2'" 1 
ATOM   375  C  "C1'" . DA  A 1 24  ? 119.357 136.879 136.428 1.00 256.68 ? 24  DA  E "C1'" 1 
ATOM   376  N  N9    . DA  A 1 24  ? 119.624 135.669 137.213 1.00 254.46 ? 24  DA  E N9    1 
ATOM   377  C  C8    . DA  A 1 24  ? 120.821 135.020 137.327 1.00 254.26 ? 24  DA  E C8    1 
ATOM   378  N  N7    . DA  A 1 24  ? 120.784 133.973 138.109 1.00 252.73 ? 24  DA  E N7    1 
ATOM   379  C  C5    . DA  A 1 24  ? 119.475 133.931 138.555 1.00 251.10 ? 24  DA  E C5    1 
ATOM   380  C  C6    . DA  A 1 24  ? 118.809 133.047 139.417 1.00 247.87 ? 24  DA  E C6    1 
ATOM   381  N  N6    . DA  A 1 24  ? 119.414 132.017 139.990 1.00 247.87 ? 24  DA  E N6    1 
ATOM   382  N  N1    . DA  A 1 24  ? 117.505 133.267 139.672 1.00 244.93 ? 24  DA  E N1    1 
ATOM   383  C  C2    . DA  A 1 24  ? 116.902 134.313 139.082 1.00 245.71 ? 24  DA  E C2    1 
ATOM   384  N  N3    . DA  A 1 24  ? 117.431 135.224 138.247 1.00 248.98 ? 24  DA  E N3    1 
ATOM   385  C  C4    . DA  A 1 24  ? 118.738 134.969 138.023 1.00 252.38 ? 24  DA  E C4    1 
ATOM   386  P  P     . DC  A 1 25  ? 122.013 141.119 136.651 1.00 269.80 ? 25  DC  E P     1 
ATOM   387  O  OP1   . DC  A 1 25  ? 122.116 142.193 135.638 1.00 269.93 ? 25  DC  E OP1   1 
ATOM   388  O  OP2   . DC  A 1 25  ? 123.189 140.256 136.902 1.00 267.64 ? 25  DC  E OP2   1 
ATOM   389  O  "O5'" . DC  A 1 25  ? 121.538 141.769 138.028 1.00 267.94 ? 25  DC  E "O5'" 1 
ATOM   390  C  "C5'" . DC  A 1 25  ? 120.357 142.549 138.039 1.00 267.38 ? 25  DC  E "C5'" 1 
ATOM   391  C  "C4'" . DC  A 1 25  ? 119.368 142.062 139.087 1.00 266.30 ? 25  DC  E "C4'" 1 
ATOM   392  O  "O4'" . DC  A 1 25  ? 119.293 140.618 139.087 1.00 264.72 ? 25  DC  E "O4'" 1 
ATOM   393  C  "C3'" . DC  A 1 25  ? 119.722 142.404 140.515 1.00 266.19 ? 25  DC  E "C3'" 1 
ATOM   394  O  "O3'" . DC  A 1 25  ? 119.374 143.754 140.817 1.00 268.50 ? 25  DC  E "O3'" 1 
ATOM   395  C  "C2'" . DC  A 1 25  ? 118.894 141.389 141.301 1.00 264.44 ? 25  DC  E "C2'" 1 
ATOM   396  C  "C1'" . DC  A 1 25  ? 118.807 140.185 140.353 1.00 263.90 ? 25  DC  E "C1'" 1 
ATOM   397  N  N1    . DC  A 1 25  ? 119.613 139.035 140.811 1.00 262.60 ? 25  DC  E N1    1 
ATOM   398  C  C2    . DC  A 1 25  ? 119.067 138.115 141.719 1.00 259.20 ? 25  DC  E C2    1 
ATOM   399  O  O2    . DC  A 1 25  ? 117.897 138.261 142.114 1.00 257.10 ? 25  DC  E O2    1 
ATOM   400  N  N3    . DC  A 1 25  ? 119.835 137.077 142.131 1.00 257.71 ? 25  DC  E N3    1 
ATOM   401  C  C4    . DC  A 1 25  ? 121.088 136.954 141.677 1.00 258.32 ? 25  DC  E C4    1 
ATOM   402  N  N4    . DC  A 1 25  ? 121.812 135.921 142.103 1.00 256.20 ? 25  DC  E N4    1 
ATOM   403  C  C5    . DC  A 1 25  ? 121.655 137.884 140.763 1.00 260.76 ? 25  DC  E C5    1 
ATOM   404  C  C6    . DC  A 1 25  ? 120.894 138.902 140.366 1.00 262.55 ? 25  DC  E C6    1 
ATOM   405  P  P     . DA  A 1 26  ? 120.500 144.904 140.818 1.00 270.49 ? 26  DA  E P     1 
ATOM   406  O  OP1   . DA  A 1 26  ? 119.989 146.026 140.001 1.00 269.40 ? 26  DA  E OP1   1 
ATOM   407  O  OP2   . DA  A 1 26  ? 121.801 144.290 140.472 1.00 269.62 ? 26  DA  E OP2   1 
ATOM   408  O  "O5'" . DA  A 1 26  ? 120.556 145.376 142.346 1.00 267.78 ? 26  DA  E "O5'" 1 
ATOM   409  C  "C5'" . DA  A 1 26  ? 119.410 145.972 142.942 1.00 267.26 ? 26  DA  E "C5'" 1 
ATOM   410  C  "C4'" . DA  A 1 26  ? 118.715 145.003 143.884 1.00 266.82 ? 26  DA  E "C4'" 1 
ATOM   411  O  "O4'" . DA  A 1 26  ? 118.819 143.649 143.356 1.00 267.53 ? 26  DA  E "O4'" 1 
ATOM   412  C  "C3'" . DA  A 1 26  ? 119.307 144.933 145.281 1.00 264.14 ? 26  DA  E "C3'" 1 
ATOM   413  O  "O3'" . DA  A 1 26  ? 118.715 145.905 146.134 1.00 262.03 ? 26  DA  E "O3'" 1 
ATOM   414  C  "C2'" . DA  A 1 26  ? 118.990 143.509 145.710 1.00 262.50 ? 26  DA  E "C2'" 1 
ATOM   415  C  "C1'" . DA  A 1 26  ? 119.107 142.732 144.402 1.00 264.31 ? 26  DA  E "C1'" 1 
ATOM   416  N  N9    . DA  A 1 26  ? 120.434 142.164 144.177 1.00 262.44 ? 26  DA  E N9    1 
ATOM   417  C  C8    . DA  A 1 26  ? 121.395 142.635 143.331 1.00 263.04 ? 26  DA  E C8    1 
ATOM   418  N  N7    . DA  A 1 26  ? 122.497 141.926 143.334 1.00 261.49 ? 26  DA  E N7    1 
ATOM   419  C  C5    . DA  A 1 26  ? 122.243 140.920 144.250 1.00 259.56 ? 26  DA  E C5    1 
ATOM   420  C  C6    . DA  A 1 26  ? 123.019 139.840 144.712 1.00 257.73 ? 26  DA  E C6    1 
ATOM   421  N  N6    . DA  A 1 26  ? 124.259 139.591 144.281 1.00 256.13 ? 26  DA  E N6    1 
ATOM   422  N  N1    . DA  A 1 26  ? 122.465 139.020 145.631 1.00 257.09 ? 26  DA  E N1    1 
ATOM   423  C  C2    . DA  A 1 26  ? 121.221 139.273 146.054 1.00 257.29 ? 26  DA  E C2    1 
ATOM   424  N  N3    . DA  A 1 26  ? 120.398 140.256 145.694 1.00 257.82 ? 26  DA  E N3    1 
ATOM   425  C  C4    . DA  A 1 26  ? 120.975 141.052 144.781 1.00 259.81 ? 26  DA  E C4    1 
ATOM   426  N  N     . PHE B 2 57  ? 122.177 139.930 81.586  1.00 100.59 ? 57  PHE A N     1 
ATOM   427  C  CA    . PHE B 2 57  ? 121.254 140.165 82.732  1.00 100.47 ? 57  PHE A CA    1 
ATOM   428  C  C     . PHE B 2 57  ? 120.046 140.971 82.271  1.00 99.81  ? 57  PHE A C     1 
ATOM   429  O  O     . PHE B 2 57  ? 119.622 141.915 82.935  1.00 97.67  ? 57  PHE A O     1 
ATOM   430  C  CB    . PHE B 2 57  ? 121.973 140.884 83.880  1.00 102.96 ? 57  PHE A CB    1 
ATOM   431  C  CG    . PHE B 2 57  ? 123.129 140.110 84.464  1.00 108.62 ? 57  PHE A CG    1 
ATOM   432  C  CD1   . PHE B 2 57  ? 124.180 139.678 83.672  1.00 108.98 ? 57  PHE A CD1   1 
ATOM   433  C  CD2   . PHE B 2 57  ? 123.171 139.835 85.820  1.00 113.90 ? 57  PHE A CD2   1 
ATOM   434  C  CE1   . PHE B 2 57  ? 125.234 138.973 84.217  1.00 114.35 ? 57  PHE A CE1   1 
ATOM   435  C  CE2   . PHE B 2 57  ? 124.222 139.131 86.366  1.00 117.08 ? 57  PHE A CE2   1 
ATOM   436  C  CZ    . PHE B 2 57  ? 125.254 138.702 85.565  1.00 117.83 ? 57  PHE A CZ    1 
ATOM   437  N  N     . PHE B 2 58  ? 119.495 140.577 81.127  1.00 100.55 ? 58  PHE A N     1 
ATOM   438  C  CA    . PHE B 2 58  ? 118.357 141.284 80.558  1.00 101.68 ? 58  PHE A CA    1 
ATOM   439  C  C     . PHE B 2 58  ? 117.133 141.132 81.452  1.00 96.59  ? 58  PHE A C     1 
ATOM   440  O  O     . PHE B 2 58  ? 116.874 140.059 82.003  1.00 95.97  ? 58  PHE A O     1 
ATOM   441  C  CB    . PHE B 2 58  ? 118.043 140.761 79.155  1.00 104.20 ? 58  PHE A CB    1 
ATOM   442  C  CG    . PHE B 2 58  ? 119.260 140.411 78.345  1.00 112.04 ? 58  PHE A CG    1 
ATOM   443  C  CD1   . PHE B 2 58  ? 120.093 141.402 77.855  1.00 116.72 ? 58  PHE A CD1   1 
ATOM   444  C  CD2   . PHE B 2 58  ? 119.572 139.090 78.078  1.00 108.73 ? 58  PHE A CD2   1 
ATOM   445  C  CE1   . PHE B 2 58  ? 121.209 141.081 77.111  1.00 118.79 ? 58  PHE A CE1   1 
ATOM   446  C  CE2   . PHE B 2 58  ? 120.687 138.765 77.336  1.00 112.19 ? 58  PHE A CE2   1 
ATOM   447  C  CZ    . PHE B 2 58  ? 121.506 139.760 76.852  1.00 118.05 ? 58  PHE A CZ    1 
ATOM   448  N  N     . ILE B 2 59  ? 116.380 142.218 81.591  1.00 99.02  ? 59  ILE A N     1 
ATOM   449  C  CA    . ILE B 2 59  ? 115.132 142.234 82.346  1.00 98.87  ? 59  ILE A CA    1 
ATOM   450  C  C     . ILE B 2 59  ? 114.012 142.495 81.351  1.00 104.89 ? 59  ILE A C     1 
ATOM   451  O  O     . ILE B 2 59  ? 114.029 143.506 80.639  1.00 111.47 ? 59  ILE A O     1 
ATOM   452  C  CB    . ILE B 2 59  ? 115.145 143.298 83.455  1.00 97.37  ? 59  ILE A CB    1 
ATOM   453  C  CG1   . ILE B 2 59  ? 116.529 143.394 84.108  1.00 95.52  ? 59  ILE A CG1   1 
ATOM   454  C  CG2   . ILE B 2 59  ? 114.081 142.985 84.498  1.00 99.25  ? 59  ILE A CG2   1 
ATOM   455  C  CD1   . ILE B 2 59  ? 116.939 142.156 84.883  1.00 93.09  ? 59  ILE A CD1   1 
ATOM   456  N  N     . ILE B 2 60  ? 113.040 141.592 81.302  1.00 103.16 ? 60  ILE A N     1 
ATOM   457  C  CA    . ILE B 2 60  ? 111.982 141.636 80.302  1.00 106.62 ? 60  ILE A CA    1 
ATOM   458  C  C     . ILE B 2 60  ? 110.784 142.350 80.908  1.00 114.44 ? 60  ILE A C     1 
ATOM   459  O  O     . ILE B 2 60  ? 110.267 141.939 81.954  1.00 112.11 ? 60  ILE A O     1 
ATOM   460  C  CB    . ILE B 2 60  ? 111.600 140.225 79.826  1.00 99.01  ? 60  ILE A CB    1 
ATOM   461  C  CG1   . ILE B 2 60  ? 112.720 139.601 78.978  1.00 102.43 ? 60  ILE A CG1   1 
ATOM   462  C  CG2   . ILE B 2 60  ? 110.294 140.267 79.037  1.00 99.52  ? 60  ILE A CG2   1 
ATOM   463  C  CD1   . ILE B 2 60  ? 113.485 140.571 78.092  1.00 105.78 ? 60  ILE A CD1   1 
ATOM   464  N  N     . ASN B 2 61  ? 110.345 143.418 80.250  1.00 119.51 ? 61  ASN A N     1 
ATOM   465  C  CA    . ASN B 2 61  ? 109.178 144.176 80.677  1.00 120.89 ? 61  ASN A CA    1 
ATOM   466  C  C     . ASN B 2 61  ? 108.607 144.891 79.458  1.00 126.71 ? 61  ASN A C     1 
ATOM   467  O  O     . ASN B 2 61  ? 109.102 144.740 78.338  1.00 127.99 ? 61  ASN A O     1 
ATOM   468  C  CB    . ASN B 2 61  ? 109.535 145.156 81.798  1.00 119.70 ? 61  ASN A CB    1 
ATOM   469  C  CG    . ASN B 2 61  ? 110.756 145.988 81.475  1.00 121.50 ? 61  ASN A CG    1 
ATOM   470  O  OD1   . ASN B 2 61  ? 110.687 146.921 80.677  1.00 125.32 ? 61  ASN A OD1   1 
ATOM   471  N  ND2   . ASN B 2 61  ? 111.883 145.654 82.089  1.00 118.35 ? 61  ASN A ND2   1 
ATOM   472  N  N     . ASP B 2 62  ? 107.555 145.678 79.687  1.00 130.58 ? 62  ASP A N     1 
ATOM   473  C  CA    . ASP B 2 62  ? 106.882 146.356 78.586  1.00 133.91 ? 62  ASP A CA    1 
ATOM   474  C  C     . ASP B 2 62  ? 107.773 147.377 77.894  1.00 134.40 ? 62  ASP A C     1 
ATOM   475  O  O     . ASP B 2 62  ? 107.533 147.696 76.725  1.00 134.06 ? 62  ASP A O     1 
ATOM   476  C  CB    . ASP B 2 62  ? 105.613 147.041 79.095  1.00 131.22 ? 62  ASP A CB    1 
ATOM   477  C  CG    . ASP B 2 62  ? 104.508 146.055 79.413  1.00 125.93 ? 62  ASP A CG    1 
ATOM   478  O  OD1   . ASP B 2 62  ? 104.400 145.034 78.701  1.00 124.45 ? 62  ASP A OD1   1 
ATOM   479  O  OD2   . ASP B 2 62  ? 103.749 146.296 80.374  1.00 124.28 ? 62  ASP A OD2   1 
ATOM   480  N  N     . ASN B 2 63  ? 108.793 147.898 78.580  1.00 134.62 ? 63  ASN A N     1 
ATOM   481  C  CA    . ASN B 2 63  ? 109.628 148.933 77.979  1.00 133.80 ? 63  ASN A CA    1 
ATOM   482  C  C     . ASN B 2 63  ? 110.479 148.370 76.847  1.00 135.21 ? 63  ASN A C     1 
ATOM   483  O  O     . ASN B 2 63  ? 110.566 148.966 75.767  1.00 135.79 ? 63  ASN A O     1 
ATOM   484  C  CB    . ASN B 2 63  ? 110.515 149.580 79.043  1.00 130.69 ? 63  ASN A CB    1 
ATOM   485  C  CG    . ASN B 2 63  ? 109.715 150.304 80.105  1.00 131.40 ? 63  ASN A CG    1 
ATOM   486  O  OD1   . ASN B 2 63  ? 108.617 150.797 79.843  1.00 131.58 ? 63  ASN A OD1   1 
ATOM   487  N  ND2   . ASN B 2 63  ? 110.262 150.375 81.312  1.00 131.44 ? 63  ASN A ND2   1 
ATOM   488  N  N     . ASN B 2 64  ? 111.110 147.220 77.072  1.00 134.96 ? 64  ASN A N     1 
ATOM   489  C  CA    . ASN B 2 64  ? 112.007 146.607 76.099  1.00 133.69 ? 64  ASN A CA    1 
ATOM   490  C  C     . ASN B 2 64  ? 111.529 145.212 75.714  1.00 131.93 ? 64  ASN A C     1 
ATOM   491  O  O     . ASN B 2 64  ? 112.313 144.266 75.618  1.00 131.12 ? 64  ASN A O     1 
ATOM   492  C  CB    . ASN B 2 64  ? 113.439 146.563 76.632  1.00 131.73 ? 64  ASN A CB    1 
ATOM   493  C  CG    . ASN B 2 64  ? 113.512 146.124 78.079  1.00 127.92 ? 64  ASN A CG    1 
ATOM   494  O  OD1   . ASN B 2 64  ? 112.845 146.690 78.945  1.00 128.63 ? 64  ASN A OD1   1 
ATOM   495  N  ND2   . ASN B 2 64  ? 114.328 145.111 78.351  1.00 121.87 ? 64  ASN A ND2   1 
ATOM   496  N  N     . TYR B 2 65  ? 110.225 145.073 75.485  1.00 132.38 ? 65  TYR A N     1 
ATOM   497  C  CA    . TYR B 2 65  ? 109.655 143.845 74.940  1.00 135.24 ? 65  TYR A CA    1 
ATOM   498  C  C     . TYR B 2 65  ? 109.669 143.938 73.419  1.00 138.04 ? 65  TYR A C     1 
ATOM   499  O  O     . TYR B 2 65  ? 108.851 144.648 72.826  1.00 141.06 ? 65  TYR A O     1 
ATOM   500  C  CB    . TYR B 2 65  ? 108.239 143.622 75.461  1.00 135.20 ? 65  TYR A CB    1 
ATOM   501  C  CG    . TYR B 2 65  ? 107.524 142.481 74.772  1.00 136.20 ? 65  TYR A CG    1 
ATOM   502  C  CD1   . TYR B 2 65  ? 108.081 141.208 74.727  1.00 136.48 ? 65  TYR A CD1   1 
ATOM   503  C  CD2   . TYR B 2 65  ? 106.293 142.678 74.161  1.00 133.77 ? 65  TYR A CD2   1 
ATOM   504  C  CE1   . TYR B 2 65  ? 107.429 140.168 74.094  1.00 135.40 ? 65  TYR A CE1   1 
ATOM   505  C  CE2   . TYR B 2 65  ? 105.637 141.642 73.529  1.00 133.20 ? 65  TYR A CE2   1 
ATOM   506  C  CZ    . TYR B 2 65  ? 106.208 140.390 73.499  1.00 134.11 ? 65  TYR A CZ    1 
ATOM   507  O  OH    . TYR B 2 65  ? 105.557 139.358 72.867  1.00 133.21 ? 65  TYR A OH    1 
ATOM   508  N  N     . ASN B 2 66  ? 110.595 143.212 72.789  1.00 135.23 ? 66  ASN A N     1 
ATOM   509  C  CA    . ASN B 2 66  ? 110.755 143.242 71.343  1.00 133.60 ? 66  ASN A CA    1 
ATOM   510  C  C     . ASN B 2 66  ? 110.270 141.975 70.655  1.00 131.69 ? 66  ASN A C     1 
ATOM   511  O  O     . ASN B 2 66  ? 110.192 141.958 69.422  1.00 133.38 ? 66  ASN A O     1 
ATOM   512  C  CB    . ASN B 2 66  ? 112.230 143.473 70.980  1.00 131.66 ? 66  ASN A CB    1 
ATOM   513  C  CG    . ASN B 2 66  ? 112.782 144.754 71.569  1.00 133.64 ? 66  ASN A CG    1 
ATOM   514  O  OD1   . ASN B 2 66  ? 113.708 144.730 72.380  1.00 133.17 ? 66  ASN A OD1   1 
ATOM   515  N  ND2   . ASN B 2 66  ? 112.212 145.883 71.168  1.00 133.51 ? 66  ASN A ND2   1 
ATOM   516  N  N     . GLU B 2 67  ? 109.974 140.915 71.411  1.00 130.31 ? 67  GLU A N     1 
ATOM   517  C  CA    . GLU B 2 67  ? 109.454 139.663 70.868  1.00 131.03 ? 67  GLU A CA    1 
ATOM   518  C  C     . GLU B 2 67  ? 110.537 138.888 70.123  1.00 128.78 ? 67  GLU A C     1 
ATOM   519  O  O     . GLU B 2 67  ? 110.300 137.761 69.676  1.00 127.12 ? 67  GLU A O     1 
ATOM   520  C  CB    . GLU B 2 67  ? 108.252 139.932 69.951  1.00 134.16 ? 67  GLU A CB    1 
ATOM   521  C  CG    . GLU B 2 67  ? 107.568 138.677 69.417  1.00 135.03 ? 67  GLU A CG    1 
ATOM   522  C  CD    . GLU B 2 67  ? 108.010 138.308 68.012  1.00 138.59 ? 67  GLU A CD    1 
ATOM   523  O  OE1   . GLU B 2 67  ? 108.759 139.091 67.389  1.00 136.41 ? 67  GLU A OE1   1 
ATOM   524  O  OE2   . GLU B 2 67  ? 107.601 137.233 67.523  1.00 142.66 ? 67  GLU A OE2   1 
ATOM   525  N  N     . ASN B 2 68  ? 111.731 139.475 69.990  1.00 129.89 ? 68  ASN A N     1 
ATOM   526  C  CA    . ASN B 2 68  ? 112.842 138.773 69.356  1.00 128.31 ? 68  ASN A CA    1 
ATOM   527  C  C     . ASN B 2 68  ? 113.500 137.780 70.304  1.00 122.72 ? 68  ASN A C     1 
ATOM   528  O  O     . ASN B 2 68  ? 114.155 136.836 69.849  1.00 117.94 ? 68  ASN A O     1 
ATOM   529  C  CB    . ASN B 2 68  ? 113.882 139.776 68.855  1.00 130.21 ? 68  ASN A CB    1 
ATOM   530  C  CG    . ASN B 2 68  ? 114.636 140.447 69.988  1.00 128.02 ? 68  ASN A CG    1 
ATOM   531  O  OD1   . ASN B 2 68  ? 114.068 140.735 71.040  1.00 128.14 ? 68  ASN A OD1   1 
ATOM   532  N  ND2   . ASN B 2 68  ? 115.925 140.695 69.778  1.00 124.45 ? 68  ASN A ND2   1 
ATOM   533  N  N     . ILE B 2 69  ? 113.349 137.982 71.615  1.00 123.17 ? 69  ILE A N     1 
ATOM   534  C  CA    . ILE B 2 69  ? 113.967 137.084 72.587  1.00 120.12 ? 69  ILE A CA    1 
ATOM   535  C  C     . ILE B 2 69  ? 113.424 135.670 72.443  1.00 116.36 ? 69  ILE A C     1 
ATOM   536  O  O     . ILE B 2 69  ? 114.132 134.694 72.719  1.00 111.03 ? 69  ILE A O     1 
ATOM   537  C  CB    . ILE B 2 69  ? 113.762 137.621 74.019  1.00 117.28 ? 69  ILE A CB    1 
ATOM   538  C  CG1   . ILE B 2 69  ? 112.301 138.020 74.246  1.00 114.92 ? 69  ILE A CG1   1 
ATOM   539  C  CG2   . ILE B 2 69  ? 114.679 138.808 74.270  1.00 116.59 ? 69  ILE A CG2   1 
ATOM   540  C  CD1   . ILE B 2 69  ? 111.931 138.158 75.703  1.00 105.78 ? 69  ILE A CD1   1 
ATOM   541  N  N     . ASN B 2 70  ? 112.169 135.529 72.010  1.00 117.16 ? 70  ASN A N     1 
ATOM   542  C  CA    . ASN B 2 70  ? 111.599 134.198 71.831  1.00 114.06 ? 70  ASN A CA    1 
ATOM   543  C  C     . ASN B 2 70  ? 112.385 133.385 70.811  1.00 113.40 ? 70  ASN A C     1 
ATOM   544  O  O     . ASN B 2 70  ? 112.395 132.151 70.875  1.00 112.15 ? 70  ASN A O     1 
ATOM   545  C  CB    . ASN B 2 70  ? 110.134 134.304 71.404  1.00 112.90 ? 70  ASN A CB    1 
ATOM   546  C  CG    . ASN B 2 70  ? 109.329 135.227 72.299  1.00 111.42 ? 70  ASN A CG    1 
ATOM   547  O  OD1   . ASN B 2 70  ? 109.887 135.974 73.102  1.00 111.71 ? 70  ASN A OD1   1 
ATOM   548  N  ND2   . ASN B 2 70  ? 108.008 135.175 72.168  1.00 110.20 ? 70  ASN A ND2   1 
ATOM   549  N  N     . LEU B 2 71  ? 113.046 134.053 69.865  1.00 117.76 ? 71  LEU A N     1 
ATOM   550  C  CA    . LEU B 2 71  ? 113.876 133.342 68.900  1.00 119.60 ? 71  LEU A CA    1 
ATOM   551  C  C     . LEU B 2 71  ? 115.037 132.623 69.571  1.00 117.45 ? 71  LEU A C     1 
ATOM   552  O  O     . LEU B 2 71  ? 115.561 131.655 69.011  1.00 117.58 ? 71  LEU A O     1 
ATOM   553  C  CB    . LEU B 2 71  ? 114.402 134.314 67.841  1.00 121.14 ? 71  LEU A CB    1 
ATOM   554  C  CG    . LEU B 2 71  ? 115.075 133.673 66.625  1.00 118.89 ? 71  LEU A CG    1 
ATOM   555  C  CD1   . LEU B 2 71  ? 114.386 134.106 65.345  1.00 117.02 ? 71  LEU A CD1   1 
ATOM   556  C  CD2   . LEU B 2 71  ? 116.555 134.033 66.583  1.00 117.88 ? 71  LEU A CD2   1 
ATOM   557  N  N     . ILE B 2 72  ? 115.453 133.077 70.756  1.00 116.34 ? 72  ILE A N     1 
ATOM   558  C  CA    . ILE B 2 72  ? 116.480 132.362 71.507  1.00 115.89 ? 72  ILE A CA    1 
ATOM   559  C  C     . ILE B 2 72  ? 115.972 130.994 71.935  1.00 119.25 ? 72  ILE A C     1 
ATOM   560  O  O     . ILE B 2 72  ? 116.739 130.025 71.995  1.00 120.32 ? 72  ILE A O     1 
ATOM   561  C  CB    . ILE B 2 72  ? 116.931 133.196 72.724  1.00 113.71 ? 72  ILE A CB    1 
ATOM   562  C  CG1   . ILE B 2 72  ? 117.629 134.485 72.280  1.00 112.09 ? 72  ILE A CG1   1 
ATOM   563  C  CG2   . ILE B 2 72  ? 117.856 132.380 73.617  1.00 114.03 ? 72  ILE A CG2   1 
ATOM   564  C  CD1   . ILE B 2 72  ? 118.961 134.275 71.572  1.00 115.30 ? 72  ILE A CD1   1 
ATOM   565  N  N     . TYR B 2 73  ? 114.678 130.892 72.244  1.00 117.97 ? 73  TYR A N     1 
ATOM   566  C  CA    . TYR B 2 73  ? 114.112 129.638 72.724  1.00 114.25 ? 73  TYR A CA    1 
ATOM   567  C  C     . TYR B 2 73  ? 114.117 128.550 71.660  1.00 119.31 ? 73  TYR A C     1 
ATOM   568  O  O     . TYR B 2 73  ? 113.978 127.370 71.999  1.00 119.67 ? 73  TYR A O     1 
ATOM   569  C  CB    . TYR B 2 73  ? 112.678 129.868 73.208  1.00 106.21 ? 73  TYR A CB    1 
ATOM   570  C  CG    . TYR B 2 73  ? 112.564 130.780 74.410  1.00 97.78  ? 73  TYR A CG    1 
ATOM   571  C  CD1   . TYR B 2 73  ? 113.623 130.944 75.293  1.00 96.15  ? 73  TYR A CD1   1 
ATOM   572  C  CD2   . TYR B 2 73  ? 111.391 131.481 74.661  1.00 95.98  ? 73  TYR A CD2   1 
ATOM   573  C  CE1   . TYR B 2 73  ? 113.517 131.777 76.382  1.00 91.72  ? 73  TYR A CE1   1 
ATOM   574  C  CE2   . TYR B 2 73  ? 111.280 132.315 75.751  1.00 94.00  ? 73  TYR A CE2   1 
ATOM   575  C  CZ    . TYR B 2 73  ? 112.345 132.458 76.607  1.00 91.86  ? 73  TYR A CZ    1 
ATOM   576  O  OH    . TYR B 2 73  ? 112.238 133.289 77.696  1.00 94.15  ? 73  TYR A OH    1 
ATOM   577  N  N     . LYS B 2 74  ? 114.271 128.910 70.388  1.00 121.14 ? 74  LYS A N     1 
ATOM   578  C  CA    . LYS B 2 74  ? 114.192 127.922 69.321  1.00 123.78 ? 74  LYS A CA    1 
ATOM   579  C  C     . LYS B 2 74  ? 115.435 127.040 69.322  1.00 124.16 ? 74  LYS A C     1 
ATOM   580  O  O     . LYS B 2 74  ? 116.565 127.537 69.365  1.00 121.57 ? 74  LYS A O     1 
ATOM   581  C  CB    . LYS B 2 74  ? 114.035 128.617 67.968  1.00 126.56 ? 74  LYS A CB    1 
ATOM   582  C  CG    . LYS B 2 74  ? 113.234 127.836 66.931  1.00 132.39 ? 74  LYS A CG    1 
ATOM   583  C  CD    . LYS B 2 74  ? 111.783 127.603 67.358  1.00 135.58 ? 74  LYS A CD    1 
ATOM   584  C  CE    . LYS B 2 74  ? 111.053 126.705 66.372  1.00 140.95 ? 74  LYS A CE    1 
ATOM   585  N  NZ    . LYS B 2 74  ? 109.644 126.471 66.778  1.00 139.18 ? 74  LYS A NZ    1 
ATOM   586  N  N     . ASP B 2 75  ? 115.221 125.725 69.275  1.00 127.82 ? 75  ASP A N     1 
ATOM   587  C  CA    . ASP B 2 75  ? 116.304 124.746 69.206  1.00 130.76 ? 75  ASP A CA    1 
ATOM   588  C  C     . ASP B 2 75  ? 117.255 124.892 70.396  1.00 128.19 ? 75  ASP A C     1 
ATOM   589  O  O     . ASP B 2 75  ? 118.438 125.212 70.251  1.00 130.37 ? 75  ASP A O     1 
ATOM   590  C  CB    . ASP B 2 75  ? 117.059 124.870 67.879  1.00 134.45 ? 75  ASP A CB    1 
ATOM   591  C  CG    . ASP B 2 75  ? 116.173 124.607 66.676  1.00 137.36 ? 75  ASP A CG    1 
ATOM   592  O  OD1   . ASP B 2 75  ? 115.433 123.601 66.687  1.00 140.89 ? 75  ASP A OD1   1 
ATOM   593  O  OD2   . ASP B 2 75  ? 116.217 125.409 65.719  1.00 138.21 ? 75  ASP A OD2   1 
ATOM   594  N  N     . ILE B 2 76  ? 116.712 124.650 71.588  1.00 123.90 ? 76  ILE A N     1 
ATOM   595  C  CA    . ILE B 2 76  ? 117.478 124.696 72.827  1.00 115.83 ? 76  ILE A CA    1 
ATOM   596  C  C     . ILE B 2 76  ? 117.200 123.430 73.626  1.00 107.03 ? 76  ILE A C     1 
ATOM   597  O  O     . ILE B 2 76  ? 116.145 122.804 73.487  1.00 104.51 ? 76  ILE A O     1 
ATOM   598  C  CB    . ILE B 2 76  ? 117.141 125.953 73.662  1.00 113.71 ? 76  ILE A CB    1 
ATOM   599  C  CG1   . ILE B 2 76  ? 118.207 126.203 74.736  1.00 109.75 ? 76  ILE A CG1   1 
ATOM   600  C  CG2   . ILE B 2 76  ? 115.768 125.813 74.300  1.00 107.43 ? 76  ILE A CG2   1 
ATOM   601  C  CD1   . ILE B 2 76  ? 119.627 126.255 74.211  1.00 110.05 ? 76  ILE A CD1   1 
ATOM   602  N  N     . LYS B 2 77  ? 118.163 123.054 74.471  1.00 106.33 ? 77  LYS A N     1 
ATOM   603  C  CA    . LYS B 2 77  ? 118.064 121.848 75.285  1.00 104.97 ? 77  LYS A CA    1 
ATOM   604  C  C     . LYS B 2 77  ? 117.972 122.162 76.774  1.00 96.96  ? 77  LYS A C     1 
ATOM   605  O  O     . LYS B 2 77  ? 117.045 121.703 77.446  1.00 89.08  ? 77  LYS A O     1 
ATOM   606  C  CB    . LYS B 2 77  ? 119.269 120.937 75.014  1.00 101.72 ? 77  LYS A CB    1 
ATOM   607  C  CG    . LYS B 2 77  ? 119.183 120.166 73.699  1.00 101.87 ? 77  LYS A CG    1 
ATOM   608  C  CD    . LYS B 2 77  ? 120.542 119.643 73.247  1.00 103.57 ? 77  LYS A CD    1 
ATOM   609  C  CE    . LYS B 2 77  ? 121.480 120.758 72.796  1.00 108.44 ? 77  LYS A CE    1 
ATOM   610  N  NZ    . LYS B 2 77  ? 121.467 120.935 71.322  1.00 109.88 ? 77  LYS A NZ    1 
ATOM   611  N  N     . TYR B 2 78  ? 118.915 122.931 77.310  1.00 96.75  ? 78  TYR A N     1 
ATOM   612  C  CA    . TYR B 2 78  ? 118.986 123.206 78.736  1.00 90.37  ? 78  TYR A CA    1 
ATOM   613  C  C     . TYR B 2 78  ? 118.463 124.604 79.039  1.00 91.23  ? 78  TYR A C     1 
ATOM   614  O  O     . TYR B 2 78  ? 118.552 125.516 78.214  1.00 97.61  ? 78  TYR A O     1 
ATOM   615  C  CB    . TYR B 2 78  ? 120.424 123.083 79.246  1.00 88.75  ? 78  TYR A CB    1 
ATOM   616  C  CG    . TYR B 2 78  ? 121.232 122.030 78.531  1.00 89.73  ? 78  TYR A CG    1 
ATOM   617  C  CD1   . TYR B 2 78  ? 120.826 120.704 78.518  1.00 93.75  ? 78  TYR A CD1   1 
ATOM   618  C  CD2   . TYR B 2 78  ? 122.405 122.362 77.871  1.00 90.87  ? 78  TYR A CD2   1 
ATOM   619  C  CE1   . TYR B 2 78  ? 121.564 119.741 77.862  1.00 96.48  ? 78  TYR A CE1   1 
ATOM   620  C  CE2   . TYR B 2 78  ? 123.149 121.405 77.214  1.00 96.06  ? 78  TYR A CE2   1 
ATOM   621  C  CZ    . TYR B 2 78  ? 122.725 120.097 77.211  1.00 98.14  ? 78  TYR A CZ    1 
ATOM   622  O  OH    . TYR B 2 78  ? 123.465 119.141 76.557  1.00 100.58 ? 78  TYR A OH    1 
ATOM   623  N  N     . CYS B 2 79  ? 117.908 124.757 80.239  1.00 87.30  ? 79  CYS A N     1 
ATOM   624  C  CA    . CYS B 2 79  ? 117.489 126.068 80.729  1.00 83.48  ? 79  CYS A CA    1 
ATOM   625  C  C     . CYS B 2 79  ? 117.400 125.992 82.247  1.00 78.12  ? 79  CYS A C     1 
ATOM   626  O  O     . CYS B 2 79  ? 116.447 125.421 82.784  1.00 77.64  ? 79  CYS A O     1 
ATOM   627  C  CB    . CYS B 2 79  ? 116.160 126.481 80.108  1.00 83.33  ? 79  CYS A CB    1 
ATOM   628  S  SG    . CYS B 2 79  ? 114.873 125.218 80.175  1.00 79.88  ? 79  CYS A SG    1 
ATOM   629  N  N     . GLY B 2 80  ? 118.378 126.583 82.929  1.00 77.52  ? 80  GLY A N     1 
ATOM   630  C  CA    . GLY B 2 80  ? 118.444 126.517 84.377  1.00 73.85  ? 80  GLY A CA    1 
ATOM   631  C  C     . GLY B 2 80  ? 117.410 127.390 85.055  1.00 74.11  ? 80  GLY A C     1 
ATOM   632  O  O     . GLY B 2 80  ? 117.749 128.389 85.695  1.00 78.55  ? 80  GLY A O     1 
ATOM   633  N  N     . LEU B 2 81  ? 116.141 127.015 84.929  1.00 66.66  ? 81  LEU A N     1 
ATOM   634  C  CA    . LEU B 2 81  ? 115.061 127.827 85.469  1.00 64.58  ? 81  LEU A CA    1 
ATOM   635  C  C     . LEU B 2 81  ? 115.095 127.821 86.992  1.00 67.53  ? 81  LEU A C     1 
ATOM   636  O  O     . LEU B 2 81  ? 115.154 126.760 87.620  1.00 69.05  ? 81  LEU A O     1 
ATOM   637  C  CB    . LEU B 2 81  ? 113.717 127.300 84.972  1.00 57.72  ? 81  LEU A CB    1 
ATOM   638  C  CG    . LEU B 2 81  ? 112.476 127.936 85.597  1.00 57.72  ? 81  LEU A CG    1 
ATOM   639  C  CD1   . LEU B 2 81  ? 111.482 128.334 84.522  1.00 61.04  ? 81  LEU A CD1   1 
ATOM   640  C  CD2   . LEU B 2 81  ? 111.836 126.994 86.597  1.00 55.11  ? 81  LEU A CD2   1 
ATOM   641  N  N     . ASN B 2 82  ? 115.062 129.013 87.584  1.00 72.30  ? 82  ASN A N     1 
ATOM   642  C  CA    . ASN B 2 82  ? 114.892 129.164 89.024  1.00 73.06  ? 82  ASN A CA    1 
ATOM   643  C  C     . ASN B 2 82  ? 114.108 130.443 89.269  1.00 71.76  ? 82  ASN A C     1 
ATOM   644  O  O     . ASN B 2 82  ? 114.456 131.495 88.727  1.00 78.76  ? 82  ASN A O     1 
ATOM   645  C  CB    . ASN B 2 82  ? 116.238 129.212 89.759  1.00 78.69  ? 82  ASN A CB    1 
ATOM   646  C  CG    . ASN B 2 82  ? 117.287 129.998 89.005  1.00 84.92  ? 82  ASN A CG    1 
ATOM   647  O  OD1   . ASN B 2 82  ? 116.998 130.612 87.982  1.00 88.38  ? 82  ASN A OD1   1 
ATOM   648  N  ND2   . ASN B 2 82  ? 118.515 129.992 89.514  1.00 83.38  ? 82  ASN A ND2   1 
ATOM   649  N  N     . ILE B 2 83  ? 113.062 130.350 90.083  1.00 66.75  ? 83  ILE A N     1 
ATOM   650  C  CA    . ILE B 2 83  ? 112.147 131.457 90.304  1.00 68.55  ? 83  ILE A CA    1 
ATOM   651  C  C     . ILE B 2 83  ? 112.416 132.069 91.675  1.00 76.02  ? 83  ILE A C     1 
ATOM   652  O  O     . ILE B 2 83  ? 113.123 131.506 92.510  1.00 77.80  ? 83  ILE A O     1 
ATOM   653  C  CB    . ILE B 2 83  ? 110.671 131.021 90.157  1.00 63.95  ? 83  ILE A CB    1 
ATOM   654  C  CG1   . ILE B 2 83  ? 110.125 130.390 91.445  1.00 69.62  ? 83  ILE A CG1   1 
ATOM   655  C  CG2   . ILE B 2 83  ? 110.524 130.048 89.003  1.00 63.47  ? 83  ILE A CG2   1 
ATOM   656  C  CD1   . ILE B 2 83  ? 108.625 130.209 91.434  1.00 70.28  ? 83  ILE A CD1   1 
ATOM   657  N  N     . GLN B 2 84  ? 111.843 133.252 91.892  1.00 79.06  ? 84  GLN A N     1 
ATOM   658  C  CA    . GLN B 2 84  ? 111.895 133.946 93.169  1.00 81.27  ? 84  GLN A CA    1 
ATOM   659  C  C     . GLN B 2 84  ? 110.502 134.454 93.507  1.00 82.19  ? 84  GLN A C     1 
ATOM   660  O  O     . GLN B 2 84  ? 109.687 134.712 92.618  1.00 80.19  ? 84  GLN A O     1 
ATOM   661  C  CB    . GLN B 2 84  ? 112.888 135.114 93.132  1.00 87.16  ? 84  GLN A CB    1 
ATOM   662  C  CG    . GLN B 2 84  ? 114.324 134.740 93.471  1.00 91.54  ? 84  GLN A CG    1 
ATOM   663  C  CD    . GLN B 2 84  ? 114.517 134.363 94.928  1.00 95.04  ? 84  GLN A CD    1 
ATOM   664  O  OE1   . GLN B 2 84  ? 113.681 133.686 95.525  1.00 90.31  ? 84  GLN A OE1   1 
ATOM   665  N  NE2   . GLN B 2 84  ? 115.625 134.808 95.510  1.00 100.34 ? 84  GLN A NE2   1 
ATOM   666  N  N     . THR B 2 85  ? 110.233 134.597 94.801  1.00 82.14  ? 85  THR A N     1 
ATOM   667  C  CA    . THR B 2 85  ? 108.901 134.956 95.263  1.00 84.85  ? 85  THR A CA    1 
ATOM   668  C  C     . THR B 2 85  ? 109.017 135.722 96.575  1.00 87.08  ? 85  THR A C     1 
ATOM   669  O  O     . THR B 2 85  ? 110.114 135.946 97.095  1.00 86.43  ? 85  THR A O     1 
ATOM   670  C  CB    . THR B 2 85  ? 108.021 133.706 95.385  1.00 81.43  ? 85  THR A CB    1 
ATOM   671  O  OG1   . THR B 2 85  ? 106.645 134.072 95.217  1.00 80.77  ? 85  THR A OG1   1 
ATOM   672  C  CG2   . THR B 2 85  ? 108.211 132.994 96.724  1.00 80.74  ? 85  THR A CG2   1 
ATOM   673  N  N     . THR B 2 86  ? 107.866 136.130 97.104  1.00 87.73  ? 86  THR A N     1 
ATOM   674  C  CA    . THR B 2 86  ? 107.798 136.973 98.289  1.00 89.09  ? 86  THR A CA    1 
ATOM   675  C  C     . THR B 2 86  ? 107.681 136.182 99.586  1.00 89.99  ? 86  THR A C     1 
ATOM   676  O  O     . THR B 2 86  ? 107.623 136.791 100.660 1.00 94.31  ? 86  THR A O     1 
ATOM   677  C  CB    . THR B 2 86  ? 106.612 137.935 98.174  1.00 89.74  ? 86  THR A CB    1 
ATOM   678  O  OG1   . THR B 2 86  ? 105.390 137.190 98.112  1.00 90.33  ? 86  THR A OG1   1 
ATOM   679  C  CG2   . THR B 2 86  ? 106.739 138.791 96.924  1.00 89.42  ? 86  THR A CG2   1 
ATOM   680  N  N     . GLY B 2 87  ? 107.652 134.854 99.523  1.00 87.32  ? 87  GLY A N     1 
ATOM   681  C  CA    . GLY B 2 87  ? 107.540 134.046 100.721 1.00 82.89  ? 87  GLY A CA    1 
ATOM   682  C  C     . GLY B 2 87  ? 107.702 132.564 100.459 1.00 83.18  ? 87  GLY A C     1 
ATOM   683  O  O     . GLY B 2 87  ? 108.559 132.161 99.667  1.00 82.73  ? 87  GLY A O     1 
ATOM   684  N  N     . LEU B 2 88  ? 106.886 131.741 101.122 1.00 84.56  ? 88  LEU A N     1 
ATOM   685  C  CA    . LEU B 2 88  ? 106.988 130.291 100.995 1.00 81.49  ? 88  LEU A CA    1 
ATOM   686  C  C     . LEU B 2 88  ? 105.642 129.658 100.662 1.00 80.30  ? 88  LEU A C     1 
ATOM   687  O  O     . LEU B 2 88  ? 105.588 128.626 99.986  1.00 79.92  ? 88  LEU A O     1 
ATOM   688  C  CB    . LEU B 2 88  ? 107.540 129.683 102.286 1.00 81.42  ? 88  LEU A CB    1 
ATOM   689  C  CG    . LEU B 2 88  ? 108.918 130.188 102.719 1.00 84.46  ? 88  LEU A CG    1 
ATOM   690  C  CD1   . LEU B 2 88  ? 109.274 129.642 104.089 1.00 88.24  ? 88  LEU A CD1   1 
ATOM   691  C  CD2   . LEU B 2 88  ? 109.982 129.808 101.700 1.00 78.23  ? 88  LEU A CD2   1 
ATOM   692  N  N     . GLU B 2 89  ? 104.554 130.262 101.132 1.00 82.01  ? 89  GLU A N     1 
ATOM   693  C  CA    . GLU B 2 89  ? 103.231 129.701 100.899 1.00 83.22  ? 89  GLU A CA    1 
ATOM   694  C  C     . GLU B 2 89  ? 102.852 129.821 99.429  1.00 86.94  ? 89  GLU A C     1 
ATOM   695  O  O     . GLU B 2 89  ? 103.226 130.780 98.749  1.00 90.36  ? 89  GLU A O     1 
ATOM   696  C  CB    . GLU B 2 89  ? 102.197 130.409 101.772 1.00 86.49  ? 89  GLU A CB    1 
ATOM   697  C  CG    . GLU B 2 89  ? 100.806 129.793 101.719 1.00 89.10  ? 89  GLU A CG    1 
ATOM   698  C  CD    . GLU B 2 89  ? 100.697 128.524 102.537 1.00 94.27  ? 89  GLU A CD    1 
ATOM   699  O  OE1   . GLU B 2 89  ? 101.579 128.285 103.388 1.00 98.23  ? 89  GLU A OE1   1 
ATOM   700  O  OE2   . GLU B 2 89  ? 99.728  127.765 102.330 1.00 96.65  ? 89  GLU A OE2   1 
ATOM   701  N  N     . VAL B 2 90  ? 102.101 128.836 98.938  1.00 86.18  ? 90  VAL A N     1 
ATOM   702  C  CA    . VAL B 2 90  ? 101.733 128.811 97.527  1.00 85.62  ? 90  VAL A CA    1 
ATOM   703  C  C     . VAL B 2 90  ? 100.374 129.456 97.271  1.00 89.10  ? 90  VAL A C     1 
ATOM   704  O  O     . VAL B 2 90  ? 100.162 130.039 96.203  1.00 90.69  ? 90  VAL A O     1 
ATOM   705  C  CB    . VAL B 2 90  ? 101.756 127.365 97.004  1.00 83.53  ? 90  VAL A CB    1 
ATOM   706  C  CG1   . VAL B 2 90  ? 100.575 126.580 97.546  1.00 83.01  ? 90  VAL A CG1   1 
ATOM   707  C  CG2   . VAL B 2 90  ? 101.771 127.351 95.480  1.00 78.74  ? 90  VAL A CG2   1 
ATOM   708  N  N     . PHE B 2 91  ? 99.449  129.370 98.222  1.00 88.34  ? 91  PHE A N     1 
ATOM   709  C  CA    . PHE B 2 91  ? 98.113  129.926 98.057  1.00 88.37  ? 91  PHE A CA    1 
ATOM   710  C  C     . PHE B 2 91  ? 97.994  131.353 98.574  1.00 89.63  ? 91  PHE A C     1 
ATOM   711  O  O     . PHE B 2 91  ? 96.892  131.911 98.554  1.00 91.31  ? 91  PHE A O     1 
ATOM   712  C  CB    . PHE B 2 91  ? 97.085  129.044 98.770  1.00 86.72  ? 91  PHE A CB    1 
ATOM   713  C  CG    . PHE B 2 91  ? 97.303  127.574 98.564  1.00 84.37  ? 91  PHE A CG    1 
ATOM   714  C  CD1   . PHE B 2 91  ? 96.902  126.960 97.393  1.00 81.62  ? 91  PHE A CD1   1 
ATOM   715  C  CD2   . PHE B 2 91  ? 97.904  126.807 99.545  1.00 84.02  ? 91  PHE A CD2   1 
ATOM   716  C  CE1   . PHE B 2 91  ? 97.100  125.611 97.203  1.00 78.28  ? 91  PHE A CE1   1 
ATOM   717  C  CE2   . PHE B 2 91  ? 98.103  125.458 99.358  1.00 78.91  ? 91  PHE A CE2   1 
ATOM   718  C  CZ    . PHE B 2 91  ? 97.701  124.859 98.187  1.00 74.15  ? 91  PHE A CZ    1 
ATOM   719  N  N     . ASP B 2 92  ? 99.091  131.953 99.037  1.00 88.52  ? 92  ASP A N     1 
ATOM   720  C  CA    . ASP B 2 92  ? 99.046  133.282 99.625  1.00 90.50  ? 92  ASP A CA    1 
ATOM   721  C  C     . ASP B 2 92  ? 100.049 134.255 99.022  1.00 94.00  ? 92  ASP A C     1 
ATOM   722  O  O     . ASP B 2 92  ? 100.069 135.422 99.429  1.00 97.48  ? 92  ASP A O     1 
ATOM   723  C  CB    . ASP B 2 92  ? 99.280  133.195 101.140 1.00 88.62  ? 92  ASP A CB    1 
ATOM   724  C  CG    . ASP B 2 92  ? 98.187  132.427 101.854 1.00 93.59  ? 92  ASP A CG    1 
ATOM   725  O  OD1   . ASP B 2 92  ? 97.060  132.367 101.319 1.00 92.81  ? 92  ASP A OD1   1 
ATOM   726  O  OD2   . ASP B 2 92  ? 98.449  131.891 102.950 1.00 100.22 ? 92  ASP A OD2   1 
ATOM   727  N  N     . GLU B 2 93  ? 100.877 133.822 98.073  1.00 92.51  ? 93  GLU A N     1 
ATOM   728  C  CA    . GLU B 2 93  ? 101.886 134.703 97.496  1.00 88.81  ? 93  GLU A CA    1 
ATOM   729  C  C     . GLU B 2 93  ? 101.903 134.597 95.976  1.00 90.57  ? 93  GLU A C     1 
ATOM   730  O  O     . GLU B 2 93  ? 101.062 133.913 95.386  1.00 90.82  ? 93  GLU A O     1 
ATOM   731  C  CB    . GLU B 2 93  ? 103.269 134.378 98.068  1.00 84.79  ? 93  GLU A CB    1 
ATOM   732  C  CG    . GLU B 2 93  ? 103.370 134.568 99.576  1.00 84.19  ? 93  GLU A CG    1 
ATOM   733  C  CD    . GLU B 2 93  ? 104.237 133.523 100.253 1.00 82.75  ? 93  GLU A CD    1 
ATOM   734  O  OE1   . GLU B 2 93  ? 104.873 132.717 99.544  1.00 85.76  ? 93  GLU A OE1   1 
ATOM   735  O  OE2   . GLU B 2 93  ? 104.281 133.507 101.499 1.00 79.98  ? 93  GLU A OE2   1 
ATOM   736  N  N     . ASN B 2 94  ? 102.856 135.275 95.338  1.00 92.18  ? 94  ASN A N     1 
ATOM   737  C  CA    . ASN B 2 94  ? 102.950 135.290 93.886  1.00 89.74  ? 94  ASN A CA    1 
ATOM   738  C  C     . ASN B 2 94  ? 104.415 135.369 93.486  1.00 87.75  ? 94  ASN A C     1 
ATOM   739  O  O     . ASN B 2 94  ? 105.280 135.728 94.289  1.00 89.70  ? 94  ASN A O     1 
ATOM   740  C  CB    . ASN B 2 94  ? 102.168 136.462 93.285  1.00 89.44  ? 94  ASN A CB    1 
ATOM   741  C  CG    . ASN B 2 94  ? 102.255 137.711 94.134  1.00 95.08  ? 94  ASN A CG    1 
ATOM   742  O  OD1   . ASN B 2 94  ? 103.077 137.796 95.045  1.00 93.57  ? 94  ASN A OD1   1 
ATOM   743  N  ND2   . ASN B 2 94  ? 101.404 138.688 93.844  1.00 97.85  ? 94  ASN A ND2   1 
ATOM   744  N  N     . ILE B 2 95  ? 104.683 135.029 92.231  1.00 81.82  ? 95  ILE A N     1 
ATOM   745  C  CA    . ILE B 2 95  ? 106.049 135.001 91.720  1.00 79.90  ? 95  ILE A CA    1 
ATOM   746  C  C     . ILE B 2 95  ? 106.499 136.420 91.406  1.00 82.16  ? 95  ILE A C     1 
ATOM   747  O  O     . ILE B 2 95  ? 105.794 137.173 90.723  1.00 85.29  ? 95  ILE A O     1 
ATOM   748  C  CB    . ILE B 2 95  ? 106.154 134.104 90.477  1.00 81.56  ? 95  ILE A CB    1 
ATOM   749  C  CG1   . ILE B 2 95  ? 105.313 132.837 90.649  1.00 79.70  ? 95  ILE A CG1   1 
ATOM   750  C  CG2   . ILE B 2 95  ? 107.605 133.744 90.209  1.00 84.01  ? 95  ILE A CG2   1 
ATOM   751  C  CD1   . ILE B 2 95  ? 104.041 132.847 89.856  1.00 73.02  ? 95  ILE A CD1   1 
ATOM   752  N  N     . ARG B 2 96  ? 107.679 136.788 91.904  1.00 85.49  ? 96  ARG A N     1 
ATOM   753  C  CA    . ARG B 2 96  ? 108.254 138.105 91.664  1.00 90.85  ? 96  ARG A CA    1 
ATOM   754  C  C     . ARG B 2 96  ? 109.219 138.100 90.486  1.00 94.12  ? 96  ARG A C     1 
ATOM   755  O  O     . ARG B 2 96  ? 109.070 138.904 89.562  1.00 97.69  ? 96  ARG A O     1 
ATOM   756  C  CB    . ARG B 2 96  ? 108.967 138.602 92.929  1.00 90.93  ? 96  ARG A CB    1 
ATOM   757  C  CG    . ARG B 2 96  ? 109.637 139.967 92.783  1.00 92.81  ? 96  ARG A CG    1 
ATOM   758  C  CD    . ARG B 2 96  ? 110.515 140.299 93.976  1.00 95.30  ? 96  ARG A CD    1 
ATOM   759  N  NE    . ARG B 2 96  ? 111.525 139.275 94.228  1.00 99.88  ? 96  ARG A NE    1 
ATOM   760  C  CZ    . ARG B 2 96  ? 112.833 139.492 94.302  1.00 103.17 ? 96  ARG A CZ    1 
ATOM   761  N  NH1   . ARG B 2 96  ? 113.350 140.700 94.147  1.00 100.18 ? 96  ARG A NH1   1 
ATOM   762  N  NH2   . ARG B 2 96  ? 113.646 138.467 94.541  1.00 103.57 ? 96  ARG A NH2   1 
ATOM   763  N  N     . LEU B 2 97  ? 110.205 137.204 90.496  1.00 92.03  ? 97  LEU A N     1 
ATOM   764  C  CA    . LEU B 2 97  ? 111.196 137.115 89.431  1.00 91.57  ? 97  LEU A CA    1 
ATOM   765  C  C     . LEU B 2 97  ? 111.333 135.671 88.979  1.00 85.57  ? 97  LEU A C     1 
ATOM   766  O  O     . LEU B 2 97  ? 111.490 134.770 89.809  1.00 86.30  ? 97  LEU A O     1 
ATOM   767  C  CB    . LEU B 2 97  ? 112.559 137.642 89.891  1.00 93.08  ? 97  LEU A CB    1 
ATOM   768  C  CG    . LEU B 2 97  ? 112.659 139.138 90.198  1.00 94.07  ? 97  LEU A CG    1 
ATOM   769  C  CD1   . LEU B 2 97  ? 114.086 139.498 90.578  1.00 97.09  ? 97  LEU A CD1   1 
ATOM   770  C  CD2   . LEU B 2 97  ? 112.194 139.981 89.018  1.00 91.34  ? 97  LEU A CD2   1 
ATOM   771  N  N     . ILE B 2 98  ? 111.281 135.457 87.666  1.00 80.15  ? 98  ILE A N     1 
ATOM   772  C  CA    . ILE B 2 98  ? 111.559 134.161 87.057  1.00 75.28  ? 98  ILE A CA    1 
ATOM   773  C  C     . ILE B 2 98  ? 112.864 134.296 86.289  1.00 76.39  ? 98  ILE A C     1 
ATOM   774  O  O     . ILE B 2 98  ? 112.970 135.122 85.374  1.00 85.27  ? 98  ILE A O     1 
ATOM   775  C  CB    . ILE B 2 98  ? 110.422 133.702 86.133  1.00 73.33  ? 98  ILE A CB    1 
ATOM   776  C  CG1   . ILE B 2 98  ? 109.178 133.368 86.960  1.00 75.87  ? 98  ILE A CG1   1 
ATOM   777  C  CG2   . ILE B 2 98  ? 110.881 132.509 85.296  1.00 68.20  ? 98  ILE A CG2   1 
ATOM   778  C  CD1   . ILE B 2 98  ? 108.012 132.835 86.147  1.00 69.40  ? 98  ILE A CD1   1 
ATOM   779  N  N     . GLN B 2 99  ? 113.852 133.485 86.649  1.00 72.42  ? 99  GLN A N     1 
ATOM   780  C  CA    . GLN B 2 99  ? 115.183 133.558 86.064  1.00 75.20  ? 99  GLN A CA    1 
ATOM   781  C  C     . GLN B 2 99  ? 115.436 132.317 85.221  1.00 73.11  ? 99  GLN A C     1 
ATOM   782  O  O     . GLN B 2 99  ? 115.311 131.192 85.713  1.00 74.18  ? 99  GLN A O     1 
ATOM   783  C  CB    . GLN B 2 99  ? 116.250 133.687 87.152  1.00 76.21  ? 99  GLN A CB    1 
ATOM   784  C  CG    . GLN B 2 99  ? 115.964 134.777 88.167  1.00 80.85  ? 99  GLN A CG    1 
ATOM   785  C  CD    . GLN B 2 99  ? 117.035 134.872 89.236  1.00 87.76  ? 99  GLN A CD    1 
ATOM   786  O  OE1   . GLN B 2 99  ? 118.213 134.635 88.972  1.00 89.82  ? 99  GLN A OE1   1 
ATOM   787  N  NE2   . GLN B 2 99  ? 116.629 135.219 90.453  1.00 88.14  ? 99  GLN A NE2   1 
ATOM   788  N  N     . ILE B 2 100 ? 115.801 132.528 83.959  1.00 74.09  ? 100 ILE A N     1 
ATOM   789  C  CA    . ILE B 2 100 ? 116.120 131.452 83.027  1.00 70.50  ? 100 ILE A CA    1 
ATOM   790  C  C     . ILE B 2 100 ? 117.549 131.654 82.549  1.00 77.79  ? 100 ILE A C     1 
ATOM   791  O  O     . ILE B 2 100 ? 117.902 132.742 82.079  1.00 87.47  ? 100 ILE A O     1 
ATOM   792  C  CB    . ILE B 2 100 ? 115.149 131.422 81.834  1.00 63.23  ? 100 ILE A CB    1 
ATOM   793  C  CG1   . ILE B 2 100 ? 113.729 131.132 82.326  1.00 57.98  ? 100 ILE A CG1   1 
ATOM   794  C  CG2   . ILE B 2 100 ? 115.627 130.396 80.807  1.00 65.40  ? 100 ILE A CG2   1 
ATOM   795  C  CD1   . ILE B 2 100 ? 112.704 130.964 81.224  1.00 55.11  ? 100 ILE A CD1   1 
ATOM   796  N  N     . ALA B 2 101 ? 118.365 130.612 82.664  1.00 76.73  ? 101 ALA A N     1 
ATOM   797  C  CA    . ALA B 2 101 ? 119.761 130.653 82.250  1.00 86.37  ? 101 ALA A CA    1 
ATOM   798  C  C     . ALA B 2 101 ? 119.938 129.800 81.003  1.00 94.97  ? 101 ALA A C     1 
ATOM   799  O  O     . ALA B 2 101 ? 119.512 128.641 80.973  1.00 95.52  ? 101 ALA A O     1 
ATOM   800  C  CB    . ALA B 2 101 ? 120.681 130.157 83.368  1.00 82.55  ? 101 ALA A CB    1 
ATOM   801  N  N     . VAL B 2 102 ? 120.569 130.372 79.980  1.00 100.55 ? 102 VAL A N     1 
ATOM   802  C  CA    . VAL B 2 102 ? 120.800 129.695 78.710  1.00 102.17 ? 102 VAL A CA    1 
ATOM   803  C  C     . VAL B 2 102 ? 122.291 129.733 78.413  1.00 109.58 ? 102 VAL A C     1 
ATOM   804  O  O     . VAL B 2 102 ? 122.951 130.754 78.634  1.00 114.40 ? 102 VAL A O     1 
ATOM   805  C  CB    . VAL B 2 102 ? 119.992 130.341 77.564  1.00 101.46 ? 102 VAL A CB    1 
ATOM   806  C  CG1   . VAL B 2 102 ? 120.646 130.059 76.216  1.00 107.34 ? 102 VAL A CG1   1 
ATOM   807  C  CG2   . VAL B 2 102 ? 118.562 129.835 77.582  1.00 92.61  ? 102 VAL A CG2   1 
ATOM   808  N  N     . GLU B 2 103 ? 122.820 128.617 77.915  1.00 109.92 ? 103 GLU A N     1 
ATOM   809  C  CA    . GLU B 2 103 ? 124.252 128.513 77.670  1.00 118.03 ? 103 GLU A CA    1 
ATOM   810  C  C     . GLU B 2 103 ? 124.706 129.574 76.676  1.00 124.28 ? 103 GLU A C     1 
ATOM   811  O  O     . GLU B 2 103 ? 123.999 129.900 75.718  1.00 123.30 ? 103 GLU A O     1 
ATOM   812  C  CB    . GLU B 2 103 ? 124.599 127.118 77.146  1.00 119.88 ? 103 GLU A CB    1 
ATOM   813  C  CG    . GLU B 2 103 ? 126.088 126.814 77.133  1.00 121.21 ? 103 GLU A CG    1 
ATOM   814  C  CD    . GLU B 2 103 ? 126.633 126.516 78.514  1.00 121.01 ? 103 GLU A CD    1 
ATOM   815  O  OE1   . GLU B 2 103 ? 126.906 127.476 79.264  1.00 122.24 ? 103 GLU A OE1   1 
ATOM   816  O  OE2   . GLU B 2 103 ? 126.790 125.323 78.849  1.00 120.45 ? 103 GLU A OE2   1 
ATOM   817  N  N     . ASN B 2 104 ? 125.898 130.121 76.919  1.00 127.85 ? 104 ASN A N     1 
ATOM   818  C  CA    . ASN B 2 104 ? 126.513 131.137 76.066  1.00 126.36 ? 104 ASN A CA    1 
ATOM   819  C  C     . ASN B 2 104 ? 125.708 132.431 76.035  1.00 123.36 ? 104 ASN A C     1 
ATOM   820  O  O     . ASN B 2 104 ? 125.868 133.241 75.117  1.00 126.50 ? 104 ASN A O     1 
ATOM   821  C  CB    . ASN B 2 104 ? 126.720 130.616 74.637  1.00 129.47 ? 104 ASN A CB    1 
ATOM   822  C  CG    . ASN B 2 104 ? 127.838 129.597 74.542  1.00 136.80 ? 104 ASN A CG    1 
ATOM   823  O  OD1   . ASN B 2 104 ? 128.888 129.749 75.165  1.00 139.42 ? 104 ASN A OD1   1 
ATOM   824  N  ND2   . ASN B 2 104 ? 127.619 128.551 73.753  1.00 139.17 ? 104 ASN A ND2   1 
ATOM   825  N  N     . TYR B 2 105 ? 124.839 132.646 77.019  1.00 120.86 ? 105 TYR A N     1 
ATOM   826  C  CA    . TYR B 2 105 ? 124.065 133.875 77.089  1.00 118.22 ? 105 TYR A CA    1 
ATOM   827  C  C     . TYR B 2 105 ? 123.839 134.226 78.551  1.00 116.69 ? 105 TYR A C     1 
ATOM   828  O  O     . TYR B 2 105 ? 123.758 133.325 79.394  1.00 117.37 ? 105 TYR A O     1 
ATOM   829  C  CB    . TYR B 2 105 ? 122.722 133.734 76.360  1.00 118.57 ? 105 TYR A CB    1 
ATOM   830  C  CG    . TYR B 2 105 ? 122.874 133.687 74.859  1.00 124.19 ? 105 TYR A CG    1 
ATOM   831  C  CD1   . TYR B 2 105 ? 123.080 134.846 74.124  1.00 126.28 ? 105 TYR A CD1   1 
ATOM   832  C  CD2   . TYR B 2 105 ? 122.827 132.479 74.177  1.00 123.46 ? 105 TYR A CD2   1 
ATOM   833  C  CE1   . TYR B 2 105 ? 123.229 134.804 72.754  1.00 128.60 ? 105 TYR A CE1   1 
ATOM   834  C  CE2   . TYR B 2 105 ? 122.973 132.429 72.808  1.00 127.81 ? 105 TYR A CE2   1 
ATOM   835  C  CZ    . TYR B 2 105 ? 123.173 133.594 72.101  1.00 132.44 ? 105 TYR A CZ    1 
ATOM   836  O  OH    . TYR B 2 105 ? 123.322 133.546 70.734  1.00 138.70 ? 105 TYR A OH    1 
ATOM   837  N  N     . PRO B 2 106 ? 123.732 135.512 78.883  1.00 115.89 ? 106 PRO A N     1 
ATOM   838  C  CA    . PRO B 2 106 ? 123.490 135.890 80.279  1.00 114.71 ? 106 PRO A CA    1 
ATOM   839  C  C     . PRO B 2 106 ? 122.105 135.473 80.749  1.00 107.80 ? 106 PRO A C     1 
ATOM   840  O  O     . PRO B 2 106 ? 121.170 135.294 79.965  1.00 104.63 ? 106 PRO A O     1 
ATOM   841  C  CB    . PRO B 2 106 ? 123.634 137.417 80.269  1.00 114.02 ? 106 PRO A CB    1 
ATOM   842  C  CG    . PRO B 2 106 ? 124.344 137.744 79.000  1.00 112.42 ? 106 PRO A CG    1 
ATOM   843  C  CD    . PRO B 2 106 ? 123.933 136.694 78.028  1.00 112.80 ? 106 PRO A CD    1 
ATOM   844  N  N     . VAL B 2 107 ? 121.987 135.326 82.070  1.00 101.98 ? 107 VAL A N     1 
ATOM   845  C  CA    . VAL B 2 107 ? 120.717 134.931 82.666  1.00 93.92  ? 107 VAL A CA    1 
ATOM   846  C  C     . VAL B 2 107 ? 119.676 136.004 82.391  1.00 90.28  ? 107 VAL A C     1 
ATOM   847  O  O     . VAL B 2 107 ? 119.923 137.201 82.583  1.00 93.92  ? 107 VAL A O     1 
ATOM   848  C  CB    . VAL B 2 107 ? 120.879 134.683 84.173  1.00 92.60  ? 107 VAL A CB    1 
ATOM   849  C  CG1   . VAL B 2 107 ? 121.541 135.876 84.860  1.00 91.77  ? 107 VAL A CG1   1 
ATOM   850  C  CG2   . VAL B 2 107 ? 119.530 134.385 84.809  1.00 90.05  ? 107 VAL A CG2   1 
ATOM   851  N  N     . ILE B 2 108 ? 118.505 135.578 81.935  1.00 84.15  ? 108 ILE A N     1 
ATOM   852  C  CA    . ILE B 2 108 ? 117.403 136.480 81.625  1.00 84.50  ? 108 ILE A CA    1 
ATOM   853  C  C     . ILE B 2 108 ? 116.377 136.404 82.744  1.00 80.22  ? 108 ILE A C     1 
ATOM   854  O  O     . ILE B 2 108 ? 116.159 135.347 83.345  1.00 81.56  ? 108 ILE A O     1 
ATOM   855  C  CB    . ILE B 2 108 ? 116.795 136.145 80.244  1.00 82.46  ? 108 ILE A CB    1 
ATOM   856  C  CG1   . ILE B 2 108 ? 115.694 135.079 80.332  1.00 77.81  ? 108 ILE A CG1   1 
ATOM   857  C  CG2   . ILE B 2 108 ? 117.884 135.683 79.293  1.00 85.98  ? 108 ILE A CG2   1 
ATOM   858  C  CD1   . ILE B 2 108 ? 114.863 134.980 79.073  1.00 81.59  ? 108 ILE A CD1   1 
ATOM   859  N  N     . ILE B 2 109 ? 115.734 137.536 83.022  1.00 82.87  ? 109 ILE A N     1 
ATOM   860  C  CA    . ILE B 2 109 ? 114.859 137.685 84.179  1.00 83.48  ? 109 ILE A CA    1 
ATOM   861  C  C     . ILE B 2 109 ? 113.525 138.262 83.731  1.00 88.88  ? 109 ILE A C     1 
ATOM   862  O  O     . ILE B 2 109 ? 113.482 139.230 82.964  1.00 96.16  ? 109 ILE A O     1 
ATOM   863  C  CB    . ILE B 2 109 ? 115.500 138.588 85.253  1.00 84.79  ? 109 ILE A CB    1 
ATOM   864  C  CG1   . ILE B 2 109 ? 116.763 137.930 85.816  1.00 82.92  ? 109 ILE A CG1   1 
ATOM   865  C  CG2   . ILE B 2 109 ? 114.500 138.891 86.359  1.00 86.92  ? 109 ILE A CG2   1 
ATOM   866  C  CD1   . ILE B 2 109 ? 118.042 138.449 85.198  1.00 89.12  ? 109 ILE A CD1   1 
ATOM   867  N  N     . TYR B 2 110 ? 112.473 137.689 84.283  1.00 88.29  ? 110 TYR A N     1 
ATOM   868  C  CA    . TYR B 2 110 ? 111.121 138.203 84.008  1.00 91.11  ? 110 TYR A CA    1 
ATOM   869  C  C     . TYR B 2 110 ? 110.516 138.643 85.330  1.00 96.35  ? 110 TYR A C     1 
ATOM   870  O  O     . TYR B 2 110 ? 110.652 137.902 86.316  1.00 95.83  ? 110 TYR A O     1 
ATOM   871  C  CB    . TYR B 2 110 ? 110.222 137.107 83.447  1.00 86.54  ? 110 TYR A CB    1 
ATOM   872  C  CG    . TYR B 2 110 ? 110.554 136.652 82.051  1.00 86.60  ? 110 TYR A CG    1 
ATOM   873  C  CD1   . TYR B 2 110 ? 111.855 136.676 81.578  1.00 82.94  ? 110 TYR A CD1   1 
ATOM   874  C  CD2   . TYR B 2 110 ? 109.561 136.189 81.206  1.00 87.49  ? 110 TYR A CD2   1 
ATOM   875  C  CE1   . TYR B 2 110 ? 112.159 136.259 80.296  1.00 85.55  ? 110 TYR A CE1   1 
ATOM   876  C  CE2   . TYR B 2 110 ? 109.848 135.769 79.920  1.00 87.53  ? 110 TYR A CE2   1 
ATOM   877  C  CZ    . TYR B 2 110 ? 111.152 135.804 79.467  1.00 88.45  ? 110 TYR A CZ    1 
ATOM   878  O  OH    . TYR B 2 110 ? 111.435 135.402 78.198  1.00 90.28  ? 110 TYR A OH    1 
ATOM   879  N  N     . ASP B 2 111 ? 109.893 139.811 85.353  1.00 105.10 ? 111 ASP A N     1 
ATOM   880  C  CA    . ASP B 2 111 ? 109.192 140.337 86.518  1.00 108.89 ? 111 ASP A CA    1 
ATOM   881  C  C     . ASP B 2 111 ? 107.705 140.424 86.201  1.00 111.58 ? 111 ASP A C     1 
ATOM   882  O  O     . ASP B 2 111 ? 107.311 141.064 85.221  1.00 115.59 ? 111 ASP A O     1 
ATOM   883  C  CB    . ASP B 2 111 ? 109.732 141.713 86.918  1.00 112.51 ? 111 ASP A CB    1 
ATOM   884  C  CG    . ASP B 2 111 ? 109.948 142.626 85.728  1.00 116.72 ? 111 ASP A CG    1 
ATOM   885  O  OD1   . ASP B 2 111 ? 109.833 142.148 84.579  1.00 115.09 ? 111 ASP A OD1   1 
ATOM   886  O  OD2   . ASP B 2 111 ? 110.234 143.823 85.940  1.00 118.06 ? 111 ASP A OD2   1 
ATOM   887  N  N     . MET B 2 112 ? 106.887 139.781 87.030  1.00 106.30 ? 112 MET A N     1 
ATOM   888  C  CA    . MET B 2 112 ? 105.455 139.677 86.785  1.00 105.66 ? 112 MET A CA    1 
ATOM   889  C  C     . MET B 2 112 ? 104.656 140.812 87.409  1.00 111.54 ? 112 MET A C     1 
ATOM   890  O  O     . MET B 2 112 ? 103.445 140.893 87.179  1.00 113.54 ? 112 MET A O     1 
ATOM   891  C  CB    . MET B 2 112 ? 104.921 138.342 87.320  1.00 97.87  ? 112 MET A CB    1 
ATOM   892  C  CG    . MET B 2 112 ? 105.724 137.118 86.905  1.00 95.63  ? 112 MET A CG    1 
ATOM   893  S  SD    . MET B 2 112 ? 105.248 136.479 85.290  1.00 90.10  ? 112 MET A SD    1 
ATOM   894  C  CE    . MET B 2 112 ? 106.844 136.408 84.485  1.00 94.52  ? 112 MET A CE    1 
ATOM   895  N  N     . PHE B 2 113 ? 105.293 141.688 88.184  1.00 112.73 ? 113 PHE A N     1 
ATOM   896  C  CA    . PHE B 2 113 ? 104.581 142.747 88.886  1.00 115.80 ? 113 PHE A CA    1 
ATOM   897  C  C     . PHE B 2 113 ? 104.438 144.021 88.065  1.00 120.47 ? 113 PHE A C     1 
ATOM   898  O  O     . PHE B 2 113 ? 103.736 144.941 88.500  1.00 119.51 ? 113 PHE A O     1 
ATOM   899  C  CB    . PHE B 2 113 ? 105.293 143.074 90.209  1.00 112.52 ? 113 PHE A CB    1 
ATOM   900  C  CG    . PHE B 2 113 ? 104.819 142.258 91.392  1.00 109.47 ? 113 PHE A CG    1 
ATOM   901  C  CD1   . PHE B 2 113 ? 103.906 141.223 91.242  1.00 106.98 ? 113 PHE A CD1   1 
ATOM   902  C  CD2   . PHE B 2 113 ? 105.296 142.533 92.663  1.00 109.54 ? 113 PHE A CD2   1 
ATOM   903  C  CE1   . PHE B 2 113 ? 103.485 140.489 92.329  1.00 106.73 ? 113 PHE A CE1   1 
ATOM   904  C  CE2   . PHE B 2 113 ? 104.875 141.799 93.752  1.00 105.86 ? 113 PHE A CE2   1 
ATOM   905  C  CZ    . PHE B 2 113 ? 103.970 140.777 93.585  1.00 105.54 ? 113 PHE A CZ    1 
ATOM   906  N  N     . ASN B 2 114 ? 105.073 144.101 86.899  1.00 122.92 ? 114 ASN A N     1 
ATOM   907  C  CA    . ASN B 2 114 ? 104.946 145.259 86.025  1.00 124.09 ? 114 ASN A CA    1 
ATOM   908  C  C     . ASN B 2 114 ? 104.353 144.933 84.663  1.00 126.74 ? 114 ASN A C     1 
ATOM   909  O  O     . ASN B 2 114 ? 103.699 145.796 84.073  1.00 129.62 ? 114 ASN A O     1 
ATOM   910  C  CB    . ASN B 2 114 ? 106.313 145.936 85.829  1.00 124.66 ? 114 ASN A CB    1 
ATOM   911  C  CG    . ASN B 2 114 ? 107.365 144.983 85.303  1.00 125.16 ? 114 ASN A CG    1 
ATOM   912  O  OD1   . ASN B 2 114 ? 107.136 143.780 85.212  1.00 122.75 ? 114 ASN A OD1   1 
ATOM   913  N  ND2   . ASN B 2 114 ? 108.530 145.519 84.951  1.00 124.50 ? 114 ASN A ND2   1 
ATOM   914  N  N     . ILE B 2 115 ? 104.554 143.722 84.150  1.00 126.06 ? 115 ILE A N     1 
ATOM   915  C  CA    . ILE B 2 115 ? 103.975 143.331 82.869  1.00 130.11 ? 115 ILE A CA    1 
ATOM   916  C  C     . ILE B 2 115 ? 102.552 142.845 83.104  1.00 135.20 ? 115 ILE A C     1 
ATOM   917  O  O     . ILE B 2 115 ? 102.307 142.003 83.976  1.00 135.00 ? 115 ILE A O     1 
ATOM   918  C  CB    . ILE B 2 115 ? 104.819 142.247 82.174  1.00 126.91 ? 115 ILE A CB    1 
ATOM   919  C  CG1   . ILE B 2 115 ? 106.314 142.387 82.488  1.00 121.88 ? 115 ILE A CG1   1 
ATOM   920  C  CG2   . ILE B 2 115 ? 104.605 142.304 80.669  1.00 129.56 ? 115 ILE A CG2   1 
ATOM   921  C  CD1   . ILE B 2 115 ? 107.140 141.200 82.048  1.00 117.99 ? 115 ILE A CD1   1 
ATOM   922  N  N     . ASN B 2 116 ? 101.613 143.373 82.328  1.00 137.34 ? 116 ASN A N     1 
ATOM   923  C  CA    . ASN B 2 116 ? 100.207 143.003 82.410  1.00 141.48 ? 116 ASN A CA    1 
ATOM   924  C  C     . ASN B 2 116 ? 99.765  142.396 81.081  1.00 144.33 ? 116 ASN A C     1 
ATOM   925  O  O     . ASN B 2 116 ? 100.568 142.196 80.169  1.00 142.72 ? 116 ASN A O     1 
ATOM   926  C  CB    . ASN B 2 116 ? 99.344  144.216 82.774  1.00 139.66 ? 116 ASN A CB    1 
ATOM   927  C  CG    . ASN B 2 116 ? 98.124  143.839 83.592  1.00 141.21 ? 116 ASN A CG    1 
ATOM   928  O  OD1   . ASN B 2 116 ? 97.931  142.674 83.942  1.00 141.48 ? 116 ASN A OD1   1 
ATOM   929  N  ND2   . ASN B 2 116 ? 97.295  144.826 83.905  1.00 142.84 ? 116 ASN A ND2   1 
ATOM   930  N  N     . LYS B 2 117 ? 98.474  142.069 81.002  1.00 146.19 ? 117 LYS A N     1 
ATOM   931  C  CA    . LYS B 2 117 ? 97.848  141.528 79.798  1.00 142.82 ? 117 LYS A CA    1 
ATOM   932  C  C     . LYS B 2 117 ? 98.613  140.315 79.280  1.00 143.06 ? 117 LYS A C     1 
ATOM   933  O  O     . LYS B 2 117 ? 99.475  139.773 79.979  1.00 145.16 ? 117 LYS A O     1 
ATOM   934  C  CB    . LYS B 2 117 ? 97.716  142.614 78.717  1.00 139.79 ? 117 LYS A CB    1 
ATOM   935  C  CG    . LYS B 2 117 ? 98.948  142.865 77.846  1.00 140.04 ? 117 LYS A CG    1 
ATOM   936  C  CD    . LYS B 2 117 ? 98.674  143.945 76.814  1.00 139.77 ? 117 LYS A CD    1 
ATOM   937  C  CE    . LYS B 2 117 ? 99.901  144.218 75.959  1.00 134.93 ? 117 LYS A CE    1 
ATOM   938  N  NZ    . LYS B 2 117 ? 100.996 144.855 76.740  1.00 132.86 ? 117 LYS A NZ    1 
ATOM   939  N  N     . LYS B 2 118 ? 98.301  139.878 78.063  1.00 140.59 ? 118 LYS A N     1 
ATOM   940  C  CA    . LYS B 2 118 ? 98.884  138.688 77.464  1.00 138.94 ? 118 LYS A CA    1 
ATOM   941  C  C     . LYS B 2 118 ? 99.778  139.082 76.289  1.00 137.60 ? 118 LYS A C     1 
ATOM   942  O  O     . LYS B 2 118 ? 100.033 140.265 76.037  1.00 137.81 ? 118 LYS A O     1 
ATOM   943  C  CB    . LYS B 2 118 ? 97.775  137.724 77.028  1.00 137.80 ? 118 LYS A CB    1 
ATOM   944  C  CG    . LYS B 2 118 ? 96.700  137.487 78.084  1.00 135.09 ? 118 LYS A CG    1 
ATOM   945  C  CD    . LYS B 2 118 ? 95.546  136.642 77.553  1.00 131.16 ? 118 LYS A CD    1 
ATOM   946  C  CE    . LYS B 2 118 ? 94.722  137.381 76.501  1.00 128.02 ? 118 LYS A CE    1 
ATOM   947  N  NZ    . LYS B 2 118 ? 94.091  138.617 77.037  1.00 128.64 ? 118 LYS A NZ    1 
ATOM   948  N  N     . ASP B 2 119 ? 100.259 138.073 75.565  1.00 134.61 ? 119 ASP A N     1 
ATOM   949  C  CA    . ASP B 2 119 ? 101.099 138.184 74.375  1.00 132.92 ? 119 ASP A CA    1 
ATOM   950  C  C     . ASP B 2 119 ? 102.558 138.462 74.721  1.00 131.44 ? 119 ASP A C     1 
ATOM   951  O  O     . ASP B 2 119 ? 103.400 138.443 73.816  1.00 132.96 ? 119 ASP A O     1 
ATOM   952  C  CB    . ASP B 2 119 ? 100.610 139.272 73.404  1.00 134.14 ? 119 ASP A CB    1 
ATOM   953  C  CG    . ASP B 2 119 ? 100.657 138.826 71.957  1.00 134.22 ? 119 ASP A CG    1 
ATOM   954  O  OD1   . ASP B 2 119 ? 101.564 138.044 71.605  1.00 134.91 ? 119 ASP A OD1   1 
ATOM   955  O  OD2   . ASP B 2 119 ? 99.789  139.259 71.171  1.00 133.05 ? 119 ASP A OD2   1 
ATOM   956  N  N     . ILE B 2 120 ? 102.890 138.712 75.984  1.00 129.60 ? 120 ILE A N     1 
ATOM   957  C  CA    . ILE B 2 120 ? 104.288 138.831 76.387  1.00 127.55 ? 120 ILE A CA    1 
ATOM   958  C  C     . ILE B 2 120 ? 104.815 137.503 76.908  1.00 126.00 ? 120 ILE A C     1 
ATOM   959  O  O     . ILE B 2 120 ? 105.944 137.114 76.602  1.00 126.32 ? 120 ILE A O     1 
ATOM   960  C  CB    . ILE B 2 120 ? 104.469 139.951 77.434  1.00 129.00 ? 120 ILE A CB    1 
ATOM   961  C  CG1   . ILE B 2 120 ? 103.578 141.159 77.124  1.00 132.13 ? 120 ILE A CG1   1 
ATOM   962  C  CG2   . ILE B 2 120 ? 105.928 140.373 77.509  1.00 127.18 ? 120 ILE A CG2   1 
ATOM   963  C  CD1   . ILE B 2 120 ? 102.222 141.129 77.796  1.00 135.39 ? 120 ILE A CD1   1 
ATOM   964  N  N     . LEU B 2 121 ? 104.007 136.800 77.700  1.00 124.87 ? 121 LEU A N     1 
ATOM   965  C  CA    . LEU B 2 121 ? 104.377 135.485 78.221  1.00 119.26 ? 121 LEU A CA    1 
ATOM   966  C  C     . LEU B 2 121 ? 103.905 134.406 77.245  1.00 115.51 ? 121 LEU A C     1 
ATOM   967  O  O     . LEU B 2 121 ? 103.023 133.593 77.527  1.00 111.71 ? 121 LEU A O     1 
ATOM   968  C  CB    . LEU B 2 121 ? 103.791 135.282 79.611  1.00 114.31 ? 121 LEU A CB    1 
ATOM   969  C  CG    . LEU B 2 121 ? 104.257 136.275 80.677  1.00 110.93 ? 121 LEU A CG    1 
ATOM   970  C  CD1   . LEU B 2 121 ? 103.486 136.064 81.972  1.00 108.45 ? 121 LEU A CD1   1 
ATOM   971  C  CD2   . LEU B 2 121 ? 105.757 136.160 80.915  1.00 100.92 ? 121 LEU A CD2   1 
ATOM   972  N  N     . ASP B 2 122 ? 104.519 134.422 76.064  1.00 116.58 ? 122 ASP A N     1 
ATOM   973  C  CA    . ASP B 2 122 ? 104.248 133.449 75.015  1.00 113.92 ? 122 ASP A CA    1 
ATOM   974  C  C     . ASP B 2 122 ? 105.413 132.498 74.800  1.00 106.83 ? 122 ASP A C     1 
ATOM   975  O  O     . ASP B 2 122 ? 105.218 131.281 74.737  1.00 103.51 ? 122 ASP A O     1 
ATOM   976  C  CB    . ASP B 2 122 ? 103.921 134.173 73.700  1.00 120.42 ? 122 ASP A CB    1 
ATOM   977  C  CG    . ASP B 2 122 ? 102.507 134.723 73.671  1.00 124.50 ? 122 ASP A CG    1 
ATOM   978  O  OD1   . ASP B 2 122 ? 101.816 134.646 74.708  1.00 125.37 ? 122 ASP A OD1   1 
ATOM   979  O  OD2   . ASP B 2 122 ? 102.087 135.230 72.610  1.00 126.79 ? 122 ASP A OD2   1 
ATOM   980  N  N     . GLY B 2 123 ? 106.630 133.029 74.679  1.00 105.85 ? 123 GLY A N     1 
ATOM   981  C  CA    . GLY B 2 123 ? 107.789 132.165 74.534  1.00 101.27 ? 123 GLY A CA    1 
ATOM   982  C  C     . GLY B 2 123 ? 108.066 131.350 75.782  1.00 100.15 ? 123 GLY A C     1 
ATOM   983  O  O     . GLY B 2 123 ? 108.398 130.164 75.699  1.00 103.43 ? 123 GLY A O     1 
ATOM   984  N  N     . LEU B 2 124 ? 107.934 131.973 76.955  1.00 97.78  ? 124 LEU A N     1 
ATOM   985  C  CA    . LEU B 2 124 ? 108.212 131.266 78.202  1.00 96.72  ? 124 LEU A CA    1 
ATOM   986  C  C     . LEU B 2 124 ? 107.227 130.122 78.414  1.00 92.84  ? 124 LEU A C     1 
ATOM   987  O  O     . LEU B 2 124 ? 107.624 129.008 78.771  1.00 89.22  ? 124 LEU A O     1 
ATOM   988  C  CB    . LEU B 2 124 ? 108.165 132.241 79.379  1.00 97.10  ? 124 LEU A CB    1 
ATOM   989  C  CG    . LEU B 2 124 ? 108.212 131.602 80.770  1.00 92.01  ? 124 LEU A CG    1 
ATOM   990  C  CD1   . LEU B 2 124 ? 109.248 132.278 81.652  1.00 87.44  ? 124 LEU A CD1   1 
ATOM   991  C  CD2   . LEU B 2 124 ? 106.842 131.648 81.425  1.00 94.20  ? 124 LEU A CD2   1 
ATOM   992  N  N     . ARG B 2 125 ? 105.935 130.379 78.204  1.00 93.73  ? 125 ARG A N     1 
ATOM   993  C  CA    . ARG B 2 125 ? 104.944 129.319 78.361  1.00 91.00  ? 125 ARG A CA    1 
ATOM   994  C  C     . ARG B 2 125 ? 105.179 128.207 77.348  1.00 92.06  ? 125 ARG A C     1 
ATOM   995  O  O     . ARG B 2 125 ? 105.054 127.021 77.675  1.00 92.67  ? 125 ARG A O     1 
ATOM   996  C  CB    . ARG B 2 125 ? 103.533 129.898 78.220  1.00 90.60  ? 125 ARG A CB    1 
ATOM   997  C  CG    . ARG B 2 125 ? 102.406 128.857 78.140  1.00 91.14  ? 125 ARG A CG    1 
ATOM   998  C  CD    . ARG B 2 125 ? 101.685 128.688 79.468  1.00 90.55  ? 125 ARG A CD    1 
ATOM   999  N  NE    . ARG B 2 125 ? 101.158 129.948 79.984  1.00 93.18  ? 125 ARG A NE    1 
ATOM   1000 C  CZ    . ARG B 2 125 ? 99.907  130.363 79.830  1.00 97.59  ? 125 ARG A CZ    1 
ATOM   1001 N  NH1   . ARG B 2 125 ? 99.016  129.649 79.160  1.00 99.68  ? 125 ARG A NH1   1 
ATOM   1002 N  NH2   . ARG B 2 125 ? 99.541  131.527 80.359  1.00 96.25  ? 125 ARG A NH2   1 
ATOM   1003 N  N     . LYS B 2 126 ? 105.516 128.570 76.108  1.00 94.64  ? 126 LYS A N     1 
ATOM   1004 C  CA    . LYS B 2 126 ? 105.762 127.561 75.084  1.00 94.64  ? 126 LYS A CA    1 
ATOM   1005 C  C     . LYS B 2 126 ? 106.955 126.689 75.452  1.00 92.97  ? 126 LYS A C     1 
ATOM   1006 O  O     . LYS B 2 126 ? 106.921 125.468 75.264  1.00 96.35  ? 126 LYS A O     1 
ATOM   1007 C  CB    . LYS B 2 126 ? 105.986 128.235 73.730  1.00 99.39  ? 126 LYS A CB    1 
ATOM   1008 C  CG    . LYS B 2 126 ? 106.275 127.266 72.593  1.00 99.35  ? 126 LYS A CG    1 
ATOM   1009 C  CD    . LYS B 2 126 ? 106.442 127.989 71.265  1.00 101.47 ? 126 LYS A CD    1 
ATOM   1010 C  CE    . LYS B 2 126 ? 107.748 128.773 71.200  1.00 101.20 ? 126 LYS A CE    1 
ATOM   1011 N  NZ    . LYS B 2 126 ? 108.943 127.892 71.298  1.00 100.02 ? 126 LYS A NZ    1 
ATOM   1012 N  N     . VAL B 2 127 ? 108.022 127.297 75.973  1.00 89.19  ? 127 VAL A N     1 
ATOM   1013 C  CA    . VAL B 2 127 ? 109.178 126.520 76.408  1.00 88.22  ? 127 VAL A CA    1 
ATOM   1014 C  C     . VAL B 2 127 ? 108.798 125.617 77.574  1.00 90.53  ? 127 VAL A C     1 
ATOM   1015 O  O     . VAL B 2 127 ? 109.159 124.435 77.609  1.00 89.82  ? 127 VAL A O     1 
ATOM   1016 C  CB    . VAL B 2 127 ? 110.345 127.454 76.775  1.00 85.18  ? 127 VAL A CB    1 
ATOM   1017 C  CG1   . VAL B 2 127 ? 111.325 126.755 77.708  1.00 83.86  ? 127 VAL A CG1   1 
ATOM   1018 C  CG2   . VAL B 2 127 ? 111.055 127.921 75.522  1.00 91.59  ? 127 VAL A CG2   1 
ATOM   1019 N  N     . LEU B 2 128 ? 108.062 126.159 78.545  1.00 89.40  ? 128 LEU A N     1 
ATOM   1020 C  CA    . LEU B 2 128 ? 107.720 125.383 79.731  1.00 84.28  ? 128 LEU A CA    1 
ATOM   1021 C  C     . LEU B 2 128 ? 106.865 124.174 79.375  1.00 82.40  ? 128 LEU A C     1 
ATOM   1022 O  O     . LEU B 2 128 ? 107.115 123.064 79.859  1.00 81.61  ? 128 LEU A O     1 
ATOM   1023 C  CB    . LEU B 2 128 ? 106.997 126.275 80.740  1.00 82.73  ? 128 LEU A CB    1 
ATOM   1024 C  CG    . LEU B 2 128 ? 107.801 126.658 81.983  1.00 78.97  ? 128 LEU A CG    1 
ATOM   1025 C  CD1   . LEU B 2 128 ? 109.021 127.481 81.611  1.00 79.74  ? 128 LEU A CD1   1 
ATOM   1026 C  CD2   . LEU B 2 128 ? 106.928 127.411 82.973  1.00 75.97  ? 128 LEU A CD2   1 
ATOM   1027 N  N     . GLU B 2 129 ? 105.857 124.365 78.522  1.00 83.58  ? 129 GLU A N     1 
ATOM   1028 C  CA    . GLU B 2 129 ? 104.967 123.268 78.161  1.00 85.28  ? 129 GLU A CA    1 
ATOM   1029 C  C     . GLU B 2 129 ? 105.623 122.256 77.232  1.00 86.60  ? 129 GLU A C     1 
ATOM   1030 O  O     . GLU B 2 129 ? 105.096 121.149 77.087  1.00 88.31  ? 129 GLU A O     1 
ATOM   1031 C  CB    . GLU B 2 129 ? 103.696 123.817 77.507  1.00 91.37  ? 129 GLU A CB    1 
ATOM   1032 C  CG    . GLU B 2 129 ? 103.898 124.353 76.095  1.00 99.72  ? 129 GLU A CG    1 
ATOM   1033 C  CD    . GLU B 2 129 ? 102.649 125.009 75.533  1.00 104.73 ? 129 GLU A CD    1 
ATOM   1034 O  OE1   . GLU B 2 129 ? 101.575 124.878 76.157  1.00 111.52 ? 129 GLU A OE1   1 
ATOM   1035 O  OE2   . GLU B 2 129 ? 102.741 125.652 74.468  1.00 101.42 ? 129 GLU A OE2   1 
ATOM   1036 N  N     . ASN B 2 130 ? 106.747 122.599 76.612  1.00 87.47  ? 130 ASN A N     1 
ATOM   1037 C  CA    . ASN B 2 130 ? 107.402 121.681 75.693  1.00 91.09  ? 130 ASN A CA    1 
ATOM   1038 C  C     . ASN B 2 130 ? 108.016 120.509 76.447  1.00 86.06  ? 130 ASN A C     1 
ATOM   1039 O  O     . ASN B 2 130 ? 108.666 120.685 77.481  1.00 83.21  ? 130 ASN A O     1 
ATOM   1040 C  CB    . ASN B 2 130 ? 108.482 122.411 74.900  1.00 91.81  ? 130 ASN A CB    1 
ATOM   1041 C  CG    . ASN B 2 130 ? 109.050 121.568 73.782  1.00 93.05  ? 130 ASN A CG    1 
ATOM   1042 O  OD1   . ASN B 2 130 ? 110.245 121.279 73.755  1.00 92.60  ? 130 ASN A OD1   1 
ATOM   1043 N  ND2   . ASN B 2 130 ? 108.194 121.169 72.848  1.00 95.17  ? 130 ASN A ND2   1 
ATOM   1044 N  N     . LYS B 2 131 ? 107.812 119.304 75.915  1.00 85.24  ? 131 LYS A N     1 
ATOM   1045 C  CA    . LYS B 2 131 ? 108.341 118.089 76.518  1.00 84.65  ? 131 LYS A CA    1 
ATOM   1046 C  C     . LYS B 2 131 ? 109.718 117.708 75.992  1.00 86.09  ? 131 LYS A C     1 
ATOM   1047 O  O     . LYS B 2 131 ? 110.329 116.776 76.523  1.00 87.27  ? 131 LYS A O     1 
ATOM   1048 C  CB    . LYS B 2 131 ? 107.376 116.923 76.280  1.00 79.42  ? 131 LYS A CB    1 
ATOM   1049 C  CG    . LYS B 2 131 ? 107.295 115.945 77.440  1.00 77.44  ? 131 LYS A CG    1 
ATOM   1050 C  CD    . LYS B 2 131 ? 106.440 114.731 77.108  1.00 80.69  ? 131 LYS A CD    1 
ATOM   1051 C  CE    . LYS B 2 131 ? 104.969 115.087 76.936  1.00 74.74  ? 131 LYS A CE    1 
ATOM   1052 N  NZ    . LYS B 2 131 ? 104.331 115.485 78.217  1.00 67.62  ? 131 LYS A NZ    1 
ATOM   1053 N  N     . ASN B 2 132 ? 110.220 118.395 74.971  1.00 86.43  ? 132 ASN A N     1 
ATOM   1054 C  CA    . ASN B 2 132 ? 111.525 118.094 74.397  1.00 89.03  ? 132 ASN A CA    1 
ATOM   1055 C  C     . ASN B 2 132 ? 112.640 118.955 74.976  1.00 85.77  ? 132 ASN A C     1 
ATOM   1056 O  O     . ASN B 2 132 ? 113.795 118.800 74.567  1.00 86.17  ? 132 ASN A O     1 
ATOM   1057 C  CB    . ASN B 2 132 ? 111.487 118.277 72.872  1.00 94.43  ? 132 ASN A CB    1 
ATOM   1058 C  CG    . ASN B 2 132 ? 110.603 117.252 72.164  1.00 95.16  ? 132 ASN A CG    1 
ATOM   1059 O  OD1   . ASN B 2 132 ? 110.205 117.467 71.019  1.00 93.23  ? 132 ASN A OD1   1 
ATOM   1060 N  ND2   . ASN B 2 132 ? 110.299 116.140 72.827  1.00 92.54  ? 132 ASN A ND2   1 
ATOM   1061 N  N     . ILE B 2 133 ? 112.328 119.854 75.905  1.00 83.74  ? 133 ILE A N     1 
ATOM   1062 C  CA    . ILE B 2 133 ? 113.308 120.738 76.525  1.00 81.72  ? 133 ILE A CA    1 
ATOM   1063 C  C     . ILE B 2 133 ? 113.307 120.477 78.022  1.00 80.86  ? 133 ILE A C     1 
ATOM   1064 O  O     . ILE B 2 133 ? 112.243 120.439 78.650  1.00 80.99  ? 133 ILE A O     1 
ATOM   1065 C  CB    . ILE B 2 133 ? 113.009 122.219 76.230  1.00 82.45  ? 133 ILE A CB    1 
ATOM   1066 C  CG1   . ILE B 2 133 ? 113.059 122.475 74.722  1.00 88.39  ? 133 ILE A CG1   1 
ATOM   1067 C  CG2   . ILE B 2 133 ? 113.995 123.104 76.983  1.00 85.21  ? 133 ILE A CG2   1 
ATOM   1068 C  CD1   . ILE B 2 133 ? 112.552 123.842 74.302  1.00 91.74  ? 133 ILE A CD1   1 
ATOM   1069 N  N     . ILE B 2 134 ? 114.494 120.292 78.585  1.00 81.61  ? 134 ILE A N     1 
ATOM   1070 C  CA    . ILE B 2 134 ? 114.634 119.967 79.998  1.00 79.06  ? 134 ILE A CA    1 
ATOM   1071 C  C     . ILE B 2 134 ? 114.653 121.246 80.825  1.00 79.31  ? 134 ILE A C     1 
ATOM   1072 O  O     . ILE B 2 134 ? 115.163 122.286 80.396  1.00 79.14  ? 134 ILE A O     1 
ATOM   1073 C  CB    . ILE B 2 134 ? 115.903 119.120 80.228  1.00 79.97  ? 134 ILE A CB    1 
ATOM   1074 C  CG1   . ILE B 2 134 ? 117.161 119.886 79.809  1.00 85.67  ? 134 ILE A CG1   1 
ATOM   1075 C  CG2   . ILE B 2 134 ? 115.824 117.816 79.454  1.00 77.97  ? 134 ILE A CG2   1 
ATOM   1076 C  CD1   . ILE B 2 134 ? 118.401 119.437 80.533  1.00 87.08  ? 134 ILE A CD1   1 
ATOM   1077 N  N     . LYS B 2 135 ? 114.089 121.165 82.030  1.00 77.14  ? 135 LYS A N     1 
ATOM   1078 C  CA    . LYS B 2 135 ? 113.977 122.298 82.945  1.00 70.33  ? 135 LYS A CA    1 
ATOM   1079 C  C     . LYS B 2 135 ? 114.754 121.973 84.213  1.00 63.61  ? 135 LYS A C     1 
ATOM   1080 O  O     . LYS B 2 135 ? 114.282 121.200 85.054  1.00 62.48  ? 135 LYS A O     1 
ATOM   1081 C  CB    . LYS B 2 135 ? 112.511 122.598 83.268  1.00 67.83  ? 135 LYS A CB    1 
ATOM   1082 C  CG    . LYS B 2 135 ? 111.544 122.351 82.120  1.00 73.49  ? 135 LYS A CG    1 
ATOM   1083 C  CD    . LYS B 2 135 ? 111.752 123.358 81.001  1.00 77.55  ? 135 LYS A CD    1 
ATOM   1084 C  CE    . LYS B 2 135 ? 110.818 123.106 79.826  1.00 78.43  ? 135 LYS A CE    1 
ATOM   1085 N  NZ    . LYS B 2 135 ? 109.490 122.556 80.221  1.00 79.03  ? 135 LYS A NZ    1 
ATOM   1086 N  N     . ILE B 2 136 ? 115.931 122.573 84.362  1.00 63.72  ? 136 ILE A N     1 
ATOM   1087 C  CA    . ILE B 2 136 ? 116.781 122.320 85.521  1.00 62.45  ? 136 ILE A CA    1 
ATOM   1088 C  C     . ILE B 2 136 ? 116.303 123.231 86.645  1.00 65.33  ? 136 ILE A C     1 
ATOM   1089 O  O     . ILE B 2 136 ? 116.496 124.448 86.592  1.00 73.00  ? 136 ILE A O     1 
ATOM   1090 C  CB    . ILE B 2 136 ? 118.259 122.567 85.205  1.00 63.48  ? 136 ILE A CB    1 
ATOM   1091 C  CG1   . ILE B 2 136 ? 118.664 121.821 83.936  1.00 68.65  ? 136 ILE A CG1   1 
ATOM   1092 C  CG2   . ILE B 2 136 ? 119.129 122.126 86.370  1.00 65.02  ? 136 ILE A CG2   1 
ATOM   1093 C  CD1   . ILE B 2 136 ? 118.289 120.363 83.933  1.00 71.54  ? 136 ILE A CD1   1 
ATOM   1094 N  N     . ILE B 2 137 ? 115.690 122.647 87.669  1.00 60.48  ? 137 ILE A N     1 
ATOM   1095 C  CA    . ILE B 2 137 ? 115.121 123.402 88.778  1.00 61.06  ? 137 ILE A CA    1 
ATOM   1096 C  C     . ILE B 2 137 ? 115.832 122.978 90.052  1.00 63.29  ? 137 ILE A C     1 
ATOM   1097 O  O     . ILE B 2 137 ? 115.813 121.796 90.416  1.00 68.47  ? 137 ILE A O     1 
ATOM   1098 C  CB    . ILE B 2 137 ? 113.607 123.179 88.902  1.00 59.37  ? 137 ILE A CB    1 
ATOM   1099 C  CG1   . ILE B 2 137 ? 112.959 123.211 87.518  1.00 63.81  ? 137 ILE A CG1   1 
ATOM   1100 C  CG2   . ILE B 2 137 ? 112.991 124.239 89.802  1.00 61.73  ? 137 ILE A CG2   1 
ATOM   1101 C  CD1   . ILE B 2 137 ? 111.454 123.366 87.549  1.00 65.92  ? 137 ILE A CD1   1 
ATOM   1102 N  N     . GLN B 2 138 ? 116.451 123.939 90.733  1.00 63.45  ? 138 GLN A N     1 
ATOM   1103 C  CA    . GLN B 2 138 ? 117.064 123.662 92.024  1.00 68.40  ? 138 GLN A CA    1 
ATOM   1104 C  C     . GLN B 2 138 ? 115.967 123.483 93.064  1.00 68.61  ? 138 GLN A C     1 
ATOM   1105 O  O     . GLN B 2 138 ? 115.119 124.364 93.240  1.00 69.84  ? 138 GLN A O     1 
ATOM   1106 C  CB    . GLN B 2 138 ? 118.006 124.794 92.421  1.00 72.01  ? 138 GLN A CB    1 
ATOM   1107 C  CG    . GLN B 2 138 ? 119.165 124.345 93.293  1.00 74.07  ? 138 GLN A CG    1 
ATOM   1108 C  CD    . GLN B 2 138 ? 118.706 123.748 94.610  1.00 73.44  ? 138 GLN A CD    1 
ATOM   1109 O  OE1   . GLN B 2 138 ? 118.113 124.436 95.440  1.00 74.66  ? 138 GLN A OE1   1 
ATOM   1110 N  NE2   . GLN B 2 138 ? 118.976 122.462 94.806  1.00 70.11  ? 138 GLN A NE2   1 
ATOM   1111 N  N     . ASN B 2 139 ? 115.984 122.347 93.755  1.00 69.17  ? 139 ASN A N     1 
ATOM   1112 C  CA    . ASN B 2 139 ? 114.913 121.979 94.674  1.00 71.00  ? 139 ASN A CA    1 
ATOM   1113 C  C     . ASN B 2 139 ? 113.560 122.121 93.980  1.00 69.02  ? 139 ASN A C     1 
ATOM   1114 O  O     . ASN B 2 139 ? 112.671 122.852 94.418  1.00 67.38  ? 139 ASN A O     1 
ATOM   1115 C  CB    . ASN B 2 139 ? 114.972 122.823 95.951  1.00 71.77  ? 139 ASN A CB    1 
ATOM   1116 C  CG    . ASN B 2 139 ? 116.024 122.331 96.927  1.00 78.06  ? 139 ASN A CG    1 
ATOM   1117 O  OD1   . ASN B 2 139 ? 117.121 121.940 96.528  1.00 76.88  ? 139 ASN A OD1   1 
ATOM   1118 N  ND2   . ASN B 2 139 ? 115.692 122.340 98.213  1.00 81.82  ? 139 ASN A ND2   1 
ATOM   1119 N  N     . GLY B 2 140 ? 113.417 121.389 92.880  1.00 70.26  ? 140 GLY A N     1 
ATOM   1120 C  CA    . GLY B 2 140 ? 112.250 121.517 92.029  1.00 68.92  ? 140 GLY A CA    1 
ATOM   1121 C  C     . GLY B 2 140 ? 110.998 120.901 92.616  1.00 65.85  ? 140 GLY A C     1 
ATOM   1122 O  O     . GLY B 2 140 ? 110.283 120.154 91.942  1.00 67.28  ? 140 GLY A O     1 
ATOM   1123 N  N     . LYS B 2 141 ? 110.728 121.208 93.882  1.00 61.21  ? 141 LYS A N     1 
ATOM   1124 C  CA    . LYS B 2 141 ? 109.474 120.869 94.531  1.00 59.22  ? 141 LYS A CA    1 
ATOM   1125 C  C     . LYS B 2 141 ? 108.710 122.096 94.988  1.00 64.80  ? 141 LYS A C     1 
ATOM   1126 O  O     . LYS B 2 141 ? 107.494 122.009 95.186  1.00 64.58  ? 141 LYS A O     1 
ATOM   1127 C  CB    . LYS B 2 141 ? 109.728 119.958 95.743  1.00 61.91  ? 141 LYS A CB    1 
ATOM   1128 C  CG    . LYS B 2 141 ? 108.477 119.334 96.340  1.00 58.04  ? 141 LYS A CG    1 
ATOM   1129 C  CD    . LYS B 2 141 ? 108.801 118.618 97.642  1.00 47.79  ? 141 LYS A CD    1 
ATOM   1130 C  CE    . LYS B 2 141 ? 107.654 118.694 98.628  1.00 39.35  ? 141 LYS A CE    1 
ATOM   1131 N  NZ    . LYS B 2 141 ? 106.664 117.622 98.379  1.00 34.93  ? 141 LYS A NZ    1 
ATOM   1132 N  N     . PHE B 2 142 ? 109.387 123.231 95.155  1.00 67.81  ? 142 PHE A N     1 
ATOM   1133 C  CA    . PHE B 2 142 ? 108.774 124.506 95.497  1.00 69.28  ? 142 PHE A CA    1 
ATOM   1134 C  C     . PHE B 2 142 ? 108.549 125.380 94.269  1.00 71.29  ? 142 PHE A C     1 
ATOM   1135 O  O     . PHE B 2 142 ? 107.443 125.885 94.060  1.00 74.33  ? 142 PHE A O     1 
ATOM   1136 C  CB    . PHE B 2 142 ? 109.654 125.242 96.516  1.00 70.13  ? 142 PHE A CB    1 
ATOM   1137 C  CG    . PHE B 2 142 ? 109.240 126.661 96.766  1.00 67.64  ? 142 PHE A CG    1 
ATOM   1138 C  CD1   . PHE B 2 142 ? 108.081 126.946 97.465  1.00 67.54  ? 142 PHE A CD1   1 
ATOM   1139 C  CD2   . PHE B 2 142 ? 110.018 127.711 96.312  1.00 69.53  ? 142 PHE A CD2   1 
ATOM   1140 C  CE1   . PHE B 2 142 ? 107.704 128.249 97.698  1.00 71.72  ? 142 PHE A CE1   1 
ATOM   1141 C  CE2   . PHE B 2 142 ? 109.644 129.013 96.542  1.00 76.30  ? 142 PHE A CE2   1 
ATOM   1142 C  CZ    . PHE B 2 142 ? 108.486 129.283 97.236  1.00 79.46  ? 142 PHE A CZ    1 
ATOM   1143 N  N     . ASP B 2 143 ? 109.581 125.564 93.443  1.00 69.12  ? 143 ASP A N     1 
ATOM   1144 C  CA    . ASP B 2 143 ? 109.420 126.364 92.233  1.00 66.52  ? 143 ASP A CA    1 
ATOM   1145 C  C     . ASP B 2 143 ? 108.394 125.739 91.299  1.00 65.39  ? 143 ASP A C     1 
ATOM   1146 O  O     . ASP B 2 143 ? 107.518 126.434 90.767  1.00 67.25  ? 143 ASP A O     1 
ATOM   1147 C  CB    . ASP B 2 143 ? 110.764 126.516 91.521  1.00 68.32  ? 143 ASP A CB    1 
ATOM   1148 C  CG    . ASP B 2 143 ? 111.899 126.829 92.476  1.00 72.54  ? 143 ASP A CG    1 
ATOM   1149 O  OD1   . ASP B 2 143 ? 111.647 127.498 93.501  1.00 73.39  ? 143 ASP A OD1   1 
ATOM   1150 O  OD2   . ASP B 2 143 ? 113.042 126.408 92.203  1.00 71.42  ? 143 ASP A OD2   1 
ATOM   1151 N  N     . ALA B 2 144 ? 108.482 124.424 91.092  1.00 65.69  ? 144 ALA A N     1 
ATOM   1152 C  CA    . ALA B 2 144 ? 107.511 123.747 90.241  1.00 65.95  ? 144 ALA A CA    1 
ATOM   1153 C  C     . ALA B 2 144 ? 106.112 123.828 90.830  1.00 67.95  ? 144 ALA A C     1 
ATOM   1154 O  O     . ALA B 2 144 ? 105.129 123.921 90.087  1.00 71.03  ? 144 ALA A O     1 
ATOM   1155 C  CB    . ALA B 2 144 ? 107.920 122.290 90.037  1.00 59.14  ? 144 ALA A CB    1 
ATOM   1156 N  N     . LYS B 2 145 ? 106.002 123.793 92.158  1.00 65.13  ? 145 LYS A N     1 
ATOM   1157 C  CA    . LYS B 2 145 ? 104.702 123.957 92.798  1.00 63.25  ? 145 LYS A CA    1 
ATOM   1158 C  C     . LYS B 2 145 ? 104.090 125.305 92.445  1.00 68.84  ? 145 LYS A C     1 
ATOM   1159 O  O     . LYS B 2 145 ? 102.912 125.392 92.079  1.00 70.99  ? 145 LYS A O     1 
ATOM   1160 C  CB    . LYS B 2 145 ? 104.853 123.817 94.311  1.00 62.95  ? 145 LYS A CB    1 
ATOM   1161 C  CG    . LYS B 2 145 ? 103.662 123.202 95.010  1.00 56.52  ? 145 LYS A CG    1 
ATOM   1162 C  CD    . LYS B 2 145 ? 103.907 123.136 96.508  1.00 56.82  ? 145 LYS A CD    1 
ATOM   1163 C  CE    . LYS B 2 145 ? 102.612 122.975 97.279  1.00 61.87  ? 145 LYS A CE    1 
ATOM   1164 N  NZ    . LYS B 2 145 ? 102.846 122.997 98.746  1.00 62.13  ? 145 LYS A NZ    1 
ATOM   1165 N  N     . PHE B 2 146 ? 104.885 126.373 92.543  1.00 69.32  ? 146 PHE A N     1 
ATOM   1166 C  CA    . PHE B 2 146 ? 104.387 127.696 92.189  1.00 68.31  ? 146 PHE A CA    1 
ATOM   1167 C  C     . PHE B 2 146 ? 104.005 127.754 90.717  1.00 71.21  ? 146 PHE A C     1 
ATOM   1168 O  O     . PHE B 2 146 ? 102.957 128.303 90.359  1.00 73.95  ? 146 PHE A O     1 
ATOM   1169 C  CB    . PHE B 2 146 ? 105.446 128.756 92.499  1.00 69.04  ? 146 PHE A CB    1 
ATOM   1170 C  CG    . PHE B 2 146 ? 105.376 129.301 93.896  1.00 74.33  ? 146 PHE A CG    1 
ATOM   1171 C  CD1   . PHE B 2 146 ? 104.897 128.526 94.935  1.00 76.27  ? 146 PHE A CD1   1 
ATOM   1172 C  CD2   . PHE B 2 146 ? 105.795 130.591 94.171  1.00 76.08  ? 146 PHE A CD2   1 
ATOM   1173 C  CE1   . PHE B 2 146 ? 104.838 129.024 96.216  1.00 76.89  ? 146 PHE A CE1   1 
ATOM   1174 C  CE2   . PHE B 2 146 ? 105.733 131.092 95.450  1.00 79.14  ? 146 PHE A CE2   1 
ATOM   1175 C  CZ    . PHE B 2 146 ? 105.254 130.309 96.474  1.00 81.53  ? 146 PHE A CZ    1 
ATOM   1176 N  N     . LEU B 2 147 ? 104.842 127.184 89.849  1.00 70.56  ? 147 LEU A N     1 
ATOM   1177 C  CA    . LEU B 2 147 ? 104.564 127.232 88.418  1.00 67.72  ? 147 LEU A CA    1 
ATOM   1178 C  C     . LEU B 2 147 ? 103.254 126.528 88.094  1.00 68.26  ? 147 LEU A C     1 
ATOM   1179 O  O     . LEU B 2 147 ? 102.421 127.051 87.347  1.00 72.61  ? 147 LEU A O     1 
ATOM   1180 C  CB    . LEU B 2 147 ? 105.719 126.603 87.643  1.00 66.00  ? 147 LEU A CB    1 
ATOM   1181 C  CG    . LEU B 2 147 ? 107.008 127.424 87.640  1.00 65.45  ? 147 LEU A CG    1 
ATOM   1182 C  CD1   . LEU B 2 147 ? 108.204 126.550 87.326  1.00 61.83  ? 147 LEU A CD1   1 
ATOM   1183 C  CD2   . LEU B 2 147 ? 106.901 128.567 86.649  1.00 68.17  ? 147 LEU A CD2   1 
ATOM   1184 N  N     . LEU B 2 148 ? 103.046 125.339 88.659  1.00 69.60  ? 148 LEU A N     1 
ATOM   1185 C  CA    . LEU B 2 148 ? 101.828 124.590 88.378  1.00 72.70  ? 148 LEU A CA    1 
ATOM   1186 C  C     . LEU B 2 148 ? 100.609 125.174 89.077  1.00 72.28  ? 148 LEU A C     1 
ATOM   1187 O  O     . LEU B 2 148 ? 99.483  124.935 88.630  1.00 71.22  ? 148 LEU A O     1 
ATOM   1188 C  CB    . LEU B 2 148 ? 102.005 123.127 88.795  1.00 72.37  ? 148 LEU A CB    1 
ATOM   1189 C  CG    . LEU B 2 148 ? 100.887 122.153 88.406  1.00 64.12  ? 148 LEU A CG    1 
ATOM   1190 C  CD1   . LEU B 2 148 ? 100.521 122.286 86.937  1.00 73.81  ? 148 LEU A CD1   1 
ATOM   1191 C  CD2   . LEU B 2 148 ? 101.290 120.722 88.732  1.00 57.50  ? 148 LEU A CD2   1 
ATOM   1192 N  N     . HIS B 2 149 ? 100.803 125.935 90.157  1.00 72.86  ? 149 HIS A N     1 
ATOM   1193 C  CA    . HIS B 2 149 ? 99.662  126.456 90.903  1.00 76.79  ? 149 HIS A CA    1 
ATOM   1194 C  C     . HIS B 2 149 ? 98.806  127.369 90.035  1.00 78.15  ? 149 HIS A C     1 
ATOM   1195 O  O     . HIS B 2 149 ? 97.572  127.309 90.084  1.00 79.75  ? 149 HIS A O     1 
ATOM   1196 C  CB    . HIS B 2 149 ? 100.148 127.201 92.145  1.00 76.33  ? 149 HIS A CB    1 
ATOM   1197 C  CG    . HIS B 2 149 ? 99.064  127.948 92.857  1.00 82.36  ? 149 HIS A CG    1 
ATOM   1198 N  ND1   . HIS B 2 149 ? 99.225  129.241 93.305  1.00 87.12  ? 149 HIS A ND1   1 
ATOM   1199 C  CD2   . HIS B 2 149 ? 97.802  127.589 93.190  1.00 83.73  ? 149 HIS A CD2   1 
ATOM   1200 C  CE1   . HIS B 2 149 ? 98.110  129.645 93.886  1.00 90.47  ? 149 HIS A CE1   1 
ATOM   1201 N  NE2   . HIS B 2 149 ? 97.230  128.661 93.830  1.00 89.57  ? 149 HIS A NE2   1 
ATOM   1202 N  N     . ASN B 2 150 ? 99.440  128.220 89.239  1.00 75.69  ? 150 ASN A N     1 
ATOM   1203 C  CA    . ASN B 2 150 ? 98.732  129.150 88.374  1.00 77.04  ? 150 ASN A CA    1 
ATOM   1204 C  C     . ASN B 2 150 ? 98.517  128.492 87.010  1.00 80.87  ? 150 ASN A C     1 
ATOM   1205 O  O     . ASN B 2 150 ? 98.698  127.284 86.843  1.00 84.08  ? 150 ASN A O     1 
ATOM   1206 C  CB    . ASN B 2 150 ? 99.501  130.469 88.277  1.00 79.03  ? 150 ASN A CB    1 
ATOM   1207 C  CG    . ASN B 2 150 ? 101.002 130.269 88.225  1.00 79.80  ? 150 ASN A CG    1 
ATOM   1208 O  OD1   . ASN B 2 150 ? 101.536 129.761 87.241  1.00 81.97  ? 150 ASN A OD1   1 
ATOM   1209 N  ND2   . ASN B 2 150 ? 101.687 130.639 89.298  1.00 75.22  ? 150 ASN A ND2   1 
ATOM   1210 N  N     . ASN B 2 151 ? 98.120  129.285 86.015  1.00 82.74  ? 151 ASN A N     1 
ATOM   1211 C  CA    . ASN B 2 151 ? 97.852  128.775 84.672  1.00 87.62  ? 151 ASN A CA    1 
ATOM   1212 C  C     . ASN B 2 151 ? 99.149  128.669 83.863  1.00 87.30  ? 151 ASN A C     1 
ATOM   1213 O  O     . ASN B 2 151 ? 99.295  129.224 82.775  1.00 90.39  ? 151 ASN A O     1 
ATOM   1214 C  CB    . ASN B 2 151 ? 96.831  129.665 83.977  1.00 96.41  ? 151 ASN A CB    1 
ATOM   1215 C  CG    . ASN B 2 151 ? 95.485  129.655 84.672  1.00 99.03  ? 151 ASN A CG    1 
ATOM   1216 O  OD1   . ASN B 2 151 ? 95.043  128.623 85.177  1.00 97.76  ? 151 ASN A OD1   1 
ATOM   1217 N  ND2   . ASN B 2 151 ? 94.829  130.809 84.712  1.00 100.39 ? 151 ASN A ND2   1 
ATOM   1218 N  N     . PHE B 2 152 ? 100.104 127.938 84.430  1.00 81.40  ? 152 PHE A N     1 
ATOM   1219 C  CA    . PHE B 2 152 ? 101.361 127.612 83.770  1.00 78.70  ? 152 PHE A CA    1 
ATOM   1220 C  C     . PHE B 2 152 ? 101.536 126.100 83.761  1.00 83.39  ? 152 PHE A C     1 
ATOM   1221 O  O     . PHE B 2 152 ? 101.228 125.427 84.749  1.00 85.99  ? 152 PHE A O     1 
ATOM   1222 C  CB    . PHE B 2 152 ? 102.553 128.271 84.480  1.00 75.70  ? 152 PHE A CB    1 
ATOM   1223 C  CG    . PHE B 2 152 ? 102.902 129.640 83.961  1.00 82.49  ? 152 PHE A CG    1 
ATOM   1224 C  CD1   . PHE B 2 152 ? 103.094 129.864 82.608  1.00 89.48  ? 152 PHE A CD1   1 
ATOM   1225 C  CD2   . PHE B 2 152 ? 103.050 130.704 84.833  1.00 83.50  ? 152 PHE A CD2   1 
ATOM   1226 C  CE1   . PHE B 2 152 ? 103.419 131.122 82.140  1.00 90.09  ? 152 PHE A CE1   1 
ATOM   1227 C  CE2   . PHE B 2 152 ? 103.375 131.959 84.369  1.00 90.62  ? 152 PHE A CE2   1 
ATOM   1228 C  CZ    . PHE B 2 152 ? 103.559 132.168 83.022  1.00 91.80  ? 152 PHE A CZ    1 
ATOM   1229 N  N     . LYS B 2 153 ? 102.023 125.567 82.644  1.00 86.76  ? 153 LYS A N     1 
ATOM   1230 C  CA    . LYS B 2 153 ? 102.238 124.134 82.480  1.00 83.34  ? 153 LYS A CA    1 
ATOM   1231 C  C     . LYS B 2 153 ? 103.728 123.860 82.339  1.00 82.14  ? 153 LYS A C     1 
ATOM   1232 O  O     . LYS B 2 153 ? 104.393 124.455 81.485  1.00 86.39  ? 153 LYS A O     1 
ATOM   1233 C  CB    . LYS B 2 153 ? 101.478 123.605 81.260  1.00 85.60  ? 153 LYS A CB    1 
ATOM   1234 C  CG    . LYS B 2 153 ? 101.276 122.089 81.215  1.00 87.95  ? 153 LYS A CG    1 
ATOM   1235 C  CD    . LYS B 2 153 ? 100.628 121.524 82.477  1.00 83.00  ? 153 LYS A CD    1 
ATOM   1236 C  CE    . LYS B 2 153 ? 99.209  122.036 82.657  1.00 87.45  ? 153 LYS A CE    1 
ATOM   1237 N  NZ    . LYS B 2 153 ? 98.538  121.414 83.829  1.00 91.23  ? 153 LYS A NZ    1 
ATOM   1238 N  N     . ILE B 2 154 ? 104.243 122.955 83.167  1.00 73.83  ? 154 ILE A N     1 
ATOM   1239 C  CA    . ILE B 2 154 ? 105.668 122.657 83.240  1.00 72.29  ? 154 ILE A CA    1 
ATOM   1240 C  C     . ILE B 2 154 ? 105.848 121.156 83.059  1.00 69.37  ? 154 ILE A C     1 
ATOM   1241 O  O     . ILE B 2 154 ? 105.075 120.361 83.605  1.00 75.38  ? 154 ILE A O     1 
ATOM   1242 C  CB    . ILE B 2 154 ? 106.268 123.133 84.582  1.00 74.93  ? 154 ILE A CB    1 
ATOM   1243 C  CG1   . ILE B 2 154 ? 107.725 122.688 84.746  1.00 71.47  ? 154 ILE A CG1   1 
ATOM   1244 C  CG2   . ILE B 2 154 ? 105.440 122.619 85.748  1.00 76.29  ? 154 ILE A CG2   1 
ATOM   1245 C  CD1   . ILE B 2 154 ? 108.697 123.509 83.952  1.00 69.23  ? 154 ILE A CD1   1 
ATOM   1246 N  N     . GLU B 2 155 ? 106.862 120.769 82.287  1.00 65.51  ? 155 GLU A N     1 
ATOM   1247 C  CA    . GLU B 2 155 ? 107.146 119.359 82.059  1.00 64.07  ? 155 GLU A CA    1 
ATOM   1248 C  C     . GLU B 2 155 ? 108.647 119.165 81.902  1.00 65.75  ? 155 GLU A C     1 
ATOM   1249 O  O     . GLU B 2 155 ? 109.392 120.106 81.620  1.00 69.37  ? 155 GLU A O     1 
ATOM   1250 C  CB    . GLU B 2 155 ? 106.406 118.825 80.828  1.00 64.79  ? 155 GLU A CB    1 
ATOM   1251 C  CG    . GLU B 2 155 ? 105.027 118.256 81.135  1.00 65.22  ? 155 GLU A CG    1 
ATOM   1252 C  CD    . GLU B 2 155 ? 105.076 116.804 81.564  1.00 70.08  ? 155 GLU A CD    1 
ATOM   1253 O  OE1   . GLU B 2 155 ? 106.172 116.323 81.926  1.00 69.68  ? 155 GLU A OE1   1 
ATOM   1254 O  OE2   . GLU B 2 155 ? 104.018 116.141 81.543  1.00 71.06  ? 155 GLU A OE2   1 
ATOM   1255 N  N     . ASN B 2 156 ? 109.080 117.919 82.089  1.00 64.16  ? 156 ASN A N     1 
ATOM   1256 C  CA    . ASN B 2 156 ? 110.495 117.556 82.052  1.00 66.26  ? 156 ASN A CA    1 
ATOM   1257 C  C     . ASN B 2 156 ? 111.284 118.340 83.102  1.00 67.91  ? 156 ASN A C     1 
ATOM   1258 O  O     . ASN B 2 156 ? 112.181 119.127 82.793  1.00 67.93  ? 156 ASN A O     1 
ATOM   1259 C  CB    . ASN B 2 156 ? 111.082 117.767 80.656  1.00 68.03  ? 156 ASN A CB    1 
ATOM   1260 C  CG    . ASN B 2 156 ? 112.454 117.142 80.508  1.00 73.97  ? 156 ASN A CG    1 
ATOM   1261 O  OD1   . ASN B 2 156 ? 113.332 117.343 81.346  1.00 71.71  ? 156 ASN A OD1   1 
ATOM   1262 N  ND2   . ASN B 2 156 ? 112.646 116.377 79.441  1.00 78.84  ? 156 ASN A ND2   1 
ATOM   1263 N  N     . ILE B 2 157 ? 110.933 118.102 84.361  1.00 62.98  ? 157 ILE A N     1 
ATOM   1264 C  CA    . ILE B 2 157 ? 111.607 118.726 85.492  1.00 56.48  ? 157 ILE A CA    1 
ATOM   1265 C  C     . ILE B 2 157 ? 112.786 117.854 85.894  1.00 54.79  ? 157 ILE A C     1 
ATOM   1266 O  O     . ILE B 2 157 ? 112.632 116.647 86.112  1.00 59.71  ? 157 ILE A O     1 
ATOM   1267 C  CB    . ILE B 2 157 ? 110.642 118.921 86.674  1.00 50.96  ? 157 ILE A CB    1 
ATOM   1268 C  CG1   . ILE B 2 157 ? 109.404 119.699 86.222  1.00 57.05  ? 157 ILE A CG1   1 
ATOM   1269 C  CG2   . ILE B 2 157 ? 111.344 119.643 87.818  1.00 56.84  ? 157 ILE A CG2   1 
ATOM   1270 C  CD1   . ILE B 2 157 ? 108.401 119.948 87.321  1.00 52.42  ? 157 ILE A CD1   1 
ATOM   1271 N  N     . PHE B 2 158 ? 113.965 118.461 85.986  1.00 55.18  ? 158 PHE A N     1 
ATOM   1272 C  CA    . PHE B 2 158 ? 115.168 117.791 86.466  1.00 53.76  ? 158 PHE A CA    1 
ATOM   1273 C  C     . PHE B 2 158 ? 115.674 118.537 87.690  1.00 60.38  ? 158 PHE A C     1 
ATOM   1274 O  O     . PHE B 2 158 ? 115.986 119.729 87.607  1.00 64.58  ? 158 PHE A O     1 
ATOM   1275 C  CB    . PHE B 2 158 ? 116.248 117.745 85.386  1.00 52.20  ? 158 PHE A CB    1 
ATOM   1276 C  CG    . PHE B 2 158 ? 117.473 116.978 85.793  1.00 54.60  ? 158 PHE A CG    1 
ATOM   1277 C  CD1   . PHE B 2 158 ? 118.502 117.602 86.473  1.00 59.95  ? 158 PHE A CD1   1 
ATOM   1278 C  CD2   . PHE B 2 158 ? 117.600 115.636 85.491  1.00 60.21  ? 158 PHE A CD2   1 
ATOM   1279 C  CE1   . PHE B 2 158 ? 119.626 116.901 86.848  1.00 66.46  ? 158 PHE A CE1   1 
ATOM   1280 C  CE2   . PHE B 2 158 ? 118.725 114.934 85.864  1.00 65.26  ? 158 PHE A CE2   1 
ATOM   1281 C  CZ    . PHE B 2 158 ? 119.737 115.567 86.542  1.00 69.13  ? 158 PHE A CZ    1 
ATOM   1282 N  N     . ASP B 2 159 ? 115.761 117.836 88.816  1.00 62.29  ? 159 ASP A N     1 
ATOM   1283 C  CA    . ASP B 2 159 ? 116.205 118.416 90.077  1.00 60.63  ? 159 ASP A CA    1 
ATOM   1284 C  C     . ASP B 2 159 ? 117.616 117.948 90.396  1.00 63.60  ? 159 ASP A C     1 
ATOM   1285 O  O     . ASP B 2 159 ? 117.889 116.743 90.406  1.00 67.81  ? 159 ASP A O     1 
ATOM   1286 C  CB    . ASP B 2 159 ? 115.266 118.034 91.222  1.00 56.70  ? 159 ASP A CB    1 
ATOM   1287 C  CG    . ASP B 2 159 ? 115.500 118.870 92.459  1.00 61.96  ? 159 ASP A CG    1 
ATOM   1288 O  OD1   . ASP B 2 159 ? 116.571 119.504 92.547  1.00 63.06  ? 159 ASP A OD1   1 
ATOM   1289 O  OD2   . ASP B 2 159 ? 114.617 118.896 93.340  1.00 67.39  ? 159 ASP A OD2   1 
ATOM   1290 N  N     . THR B 2 160 ? 118.508 118.903 90.659  1.00 63.36  ? 160 THR A N     1 
ATOM   1291 C  CA    . THR B 2 160 ? 119.841 118.554 91.126  1.00 65.88  ? 160 THR A CA    1 
ATOM   1292 C  C     . THR B 2 160 ? 119.822 118.073 92.569  1.00 69.17  ? 160 THR A C     1 
ATOM   1293 O  O     . THR B 2 160 ? 120.703 117.303 92.963  1.00 74.78  ? 160 THR A O     1 
ATOM   1294 C  CB    . THR B 2 160 ? 120.783 119.752 90.987  1.00 72.65  ? 160 THR A CB    1 
ATOM   1295 O  OG1   . THR B 2 160 ? 120.294 120.847 91.770  1.00 74.53  ? 160 THR A OG1   1 
ATOM   1296 C  CG2   . THR B 2 160 ? 120.892 120.178 89.536  1.00 75.49  ? 160 THR A CG2   1 
ATOM   1297 N  N     . TYR B 2 161 ? 118.835 118.502 93.360  1.00 67.16  ? 161 TYR A N     1 
ATOM   1298 C  CA    . TYR B 2 161 ? 118.737 118.051 94.746  1.00 69.48  ? 161 TYR A CA    1 
ATOM   1299 C  C     . TYR B 2 161 ? 118.433 116.559 94.817  1.00 69.94  ? 161 TYR A C     1 
ATOM   1300 O  O     . TYR B 2 161 ? 119.068 115.820 95.581  1.00 70.08  ? 161 TYR A O     1 
ATOM   1301 C  CB    . TYR B 2 161 ? 117.666 118.861 95.479  1.00 69.63  ? 161 TYR A CB    1 
ATOM   1302 C  CG    . TYR B 2 161 ? 116.963 118.119 96.595  1.00 72.09  ? 161 TYR A CG    1 
ATOM   1303 C  CD1   . TYR B 2 161 ? 117.567 117.954 97.834  1.00 74.38  ? 161 TYR A CD1   1 
ATOM   1304 C  CD2   . TYR B 2 161 ? 115.688 117.597 96.414  1.00 71.83  ? 161 TYR A CD2   1 
ATOM   1305 C  CE1   . TYR B 2 161 ? 116.925 117.283 98.856  1.00 77.17  ? 161 TYR A CE1   1 
ATOM   1306 C  CE2   . TYR B 2 161 ? 115.040 116.925 97.432  1.00 75.52  ? 161 TYR A CE2   1 
ATOM   1307 C  CZ    . TYR B 2 161 ? 115.662 116.773 98.650  1.00 79.26  ? 161 TYR A CZ    1 
ATOM   1308 O  OH    . TYR B 2 161 ? 115.018 116.104 99.664  1.00 80.71  ? 161 TYR A OH    1 
ATOM   1309 N  N     . ILE B 2 162 ? 117.470 116.095 94.018  1.00 66.41  ? 162 ILE A N     1 
ATOM   1310 C  CA    . ILE B 2 162 ? 117.118 114.677 94.026  1.00 59.85  ? 162 ILE A CA    1 
ATOM   1311 C  C     . ILE B 2 162 ? 118.306 113.838 93.579  1.00 60.70  ? 162 ILE A C     1 
ATOM   1312 O  O     . ILE B 2 162 ? 118.612 112.800 94.177  1.00 65.81  ? 162 ILE A O     1 
ATOM   1313 C  CB    . ILE B 2 162 ? 115.884 114.429 93.139  1.00 55.41  ? 162 ILE A CB    1 
ATOM   1314 C  CG1   . ILE B 2 162 ? 114.610 114.801 93.903  1.00 54.27  ? 162 ILE A CG1   1 
ATOM   1315 C  CG2   . ILE B 2 162 ? 115.850 112.974 92.673  1.00 52.73  ? 162 ILE A CG2   1 
ATOM   1316 C  CD1   . ILE B 2 162 ? 113.325 114.465 93.181  1.00 50.19  ? 162 ILE A CD1   1 
ATOM   1317 N  N     . ALA B 2 163 ? 118.993 114.270 92.522  1.00 62.30  ? 163 ALA A N     1 
ATOM   1318 C  CA    . ALA B 2 163 ? 120.164 113.534 92.060  1.00 66.46  ? 163 ALA A CA    1 
ATOM   1319 C  C     . ALA B 2 163 ? 121.257 113.518 93.120  1.00 71.43  ? 163 ALA A C     1 
ATOM   1320 O  O     . ALA B 2 163 ? 121.915 112.493 93.329  1.00 71.35  ? 163 ALA A O     1 
ATOM   1321 C  CB    . ALA B 2 163 ? 120.686 114.144 90.761  1.00 69.19  ? 163 ALA A CB    1 
ATOM   1322 N  N     . SER B 2 164 ? 121.466 114.647 93.801  1.00 71.36  ? 164 SER A N     1 
ATOM   1323 C  CA    . SER B 2 164 ? 122.488 114.702 94.839  1.00 70.42  ? 164 SER A CA    1 
ATOM   1324 C  C     . SER B 2 164 ? 122.160 113.750 95.978  1.00 73.18  ? 164 SER A C     1 
ATOM   1325 O  O     . SER B 2 164 ? 123.051 113.083 96.518  1.00 78.00  ? 164 SER A O     1 
ATOM   1326 C  CB    . SER B 2 164 ? 122.627 116.132 95.362  1.00 66.80  ? 164 SER A CB    1 
ATOM   1327 O  OG    . SER B 2 164 ? 123.095 117.004 94.348  1.00 71.39  ? 164 SER A OG    1 
ATOM   1328 N  N     . LYS B 2 165 ? 120.885 113.672 96.358  1.00 71.54  ? 165 LYS A N     1 
ATOM   1329 C  CA    . LYS B 2 165 ? 120.489 112.775 97.436  1.00 69.66  ? 165 LYS A CA    1 
ATOM   1330 C  C     . LYS B 2 165 ? 120.676 111.309 97.069  1.00 70.18  ? 165 LYS A C     1 
ATOM   1331 O  O     . LYS B 2 165 ? 120.779 110.469 97.970  1.00 70.31  ? 165 LYS A O     1 
ATOM   1332 C  CB    . LYS B 2 165 ? 119.036 113.043 97.826  1.00 65.72  ? 165 LYS A CB    1 
ATOM   1333 C  CG    . LYS B 2 165 ? 118.761 112.912 99.312  1.00 66.96  ? 165 LYS A CG    1 
ATOM   1334 C  CD    . LYS B 2 165 ? 117.731 113.921 99.777  1.00 67.06  ? 165 LYS A CD    1 
ATOM   1335 C  CE    . LYS B 2 165 ? 117.603 113.917 101.289 1.00 62.93  ? 165 LYS A CE    1 
ATOM   1336 N  NZ    . LYS B 2 165 ? 117.250 112.570 101.810 1.00 59.17  ? 165 LYS A NZ    1 
ATOM   1337 N  N     . LEU B 2 166 ? 120.722 110.981 95.781  1.00 71.65  ? 166 LEU A N     1 
ATOM   1338 C  CA    . LEU B 2 166 ? 121.028 109.621 95.338  1.00 72.05  ? 166 LEU A CA    1 
ATOM   1339 C  C     . LEU B 2 166 ? 122.522 109.455 95.082  1.00 77.70  ? 166 LEU A C     1 
ATOM   1340 O  O     . LEU B 2 166 ? 122.947 109.035 94.008  1.00 79.65  ? 166 LEU A O     1 
ATOM   1341 C  CB    . LEU B 2 166 ? 120.225 109.283 94.089  1.00 69.06  ? 166 LEU A CB    1 
ATOM   1342 C  CG    . LEU B 2 166 ? 118.712 109.095 94.234  1.00 60.92  ? 166 LEU A CG    1 
ATOM   1343 C  CD1   . LEU B 2 166 ? 118.163 108.404 92.996  1.00 57.42  ? 166 LEU A CD1   1 
ATOM   1344 C  CD2   . LEU B 2 166 ? 118.352 108.321 95.491  1.00 59.62  ? 166 LEU A CD2   1 
ATOM   1345 N  N     . LEU B 2 167 ? 123.334 109.797 96.077  1.00 81.80  ? 167 LEU A N     1 
ATOM   1346 C  CA    . LEU B 2 167 ? 124.780 109.690 95.954  1.00 84.24  ? 167 LEU A CA    1 
ATOM   1347 C  C     . LEU B 2 167 ? 125.371 109.372 97.318  1.00 88.25  ? 167 LEU A C     1 
ATOM   1348 O  O     . LEU B 2 167 ? 124.954 109.941 98.331  1.00 86.89  ? 167 LEU A O     1 
ATOM   1349 C  CB    . LEU B 2 167 ? 125.395 110.985 95.406  1.00 83.56  ? 167 LEU A CB    1 
ATOM   1350 C  CG    . LEU B 2 167 ? 125.236 111.255 93.906  1.00 81.12  ? 167 LEU A CG    1 
ATOM   1351 C  CD1   . LEU B 2 167 ? 125.751 112.644 93.568  1.00 77.96  ? 167 LEU A CD1   1 
ATOM   1352 C  CD2   . LEU B 2 167 ? 125.959 110.205 93.072  1.00 82.68  ? 167 LEU A CD2   1 
ATOM   1353 N  N     . ASP B 2 168 ? 126.340 108.463 97.333  1.00 95.19  ? 168 ASP A N     1 
ATOM   1354 C  CA    . ASP B 2 168 ? 127.046 108.108 98.559  1.00 104.53 ? 168 ASP A CA    1 
ATOM   1355 C  C     . ASP B 2 168 ? 126.067 107.741 99.671  1.00 106.54 ? 168 ASP A C     1 
ATOM   1356 O  O     . ASP B 2 168 ? 125.127 106.977 99.456  1.00 107.40 ? 168 ASP A O     1 
ATOM   1357 C  CB    . ASP B 2 168 ? 127.945 109.262 99.010  1.00 106.78 ? 168 ASP A CB    1 
ATOM   1358 C  CG    . ASP B 2 168 ? 128.998 108.825 100.011 1.00 111.53 ? 168 ASP A CG    1 
ATOM   1359 O  OD1   . ASP B 2 168 ? 129.916 108.073 99.622  1.00 110.53 ? 168 ASP A OD1   1 
ATOM   1360 O  OD2   . ASP B 2 168 ? 128.911 109.241 101.185 1.00 112.56 ? 168 ASP A OD2   1 
ATOM   1361 N  N     . CYS B 2 218 ? 124.556 128.631 87.932  1.00 93.78  ? 218 CYS A N     1 
ATOM   1362 C  CA    . CYS B 2 218 ? 125.404 127.469 88.171  1.00 99.38  ? 218 CYS A CA    1 
ATOM   1363 C  C     . CYS B 2 218 ? 124.637 126.173 87.932  1.00 99.64  ? 218 CYS A C     1 
ATOM   1364 O  O     . CYS B 2 218 ? 125.169 125.082 88.130  1.00 97.88  ? 218 CYS A O     1 
ATOM   1365 C  CB    . CYS B 2 218 ? 125.955 127.490 89.598  1.00 102.29 ? 218 CYS A CB    1 
ATOM   1366 S  SG    . CYS B 2 218 ? 124.710 127.225 90.880  1.00 105.39 ? 218 CYS A SG    1 
ATOM   1367 N  N     . LEU B 2 219 ? 123.377 126.301 87.511  1.00 97.18  ? 219 LEU A N     1 
ATOM   1368 C  CA    . LEU B 2 219 ? 122.567 125.118 87.247  1.00 93.24  ? 219 LEU A CA    1 
ATOM   1369 C  C     . LEU B 2 219 ? 123.033 124.386 85.995  1.00 94.79  ? 219 LEU A C     1 
ATOM   1370 O  O     . LEU B 2 219 ? 122.940 123.154 85.929  1.00 98.14  ? 219 LEU A O     1 
ATOM   1371 C  CB    . LEU B 2 219 ? 121.095 125.511 87.117  1.00 84.51  ? 219 LEU A CB    1 
ATOM   1372 C  CG    . LEU B 2 219 ? 120.407 125.870 88.435  1.00 84.05  ? 219 LEU A CG    1 
ATOM   1373 C  CD1   . LEU B 2 219 ? 120.481 127.365 88.694  1.00 81.19  ? 219 LEU A CD1   1 
ATOM   1374 C  CD2   . LEU B 2 219 ? 118.963 125.404 88.433  1.00 80.43  ? 219 LEU A CD2   1 
ATOM   1375 N  N     . LEU B 2 220 ? 123.533 125.118 84.998  1.00 93.57  ? 220 LEU A N     1 
ATOM   1376 C  CA    . LEU B 2 220 ? 123.972 124.475 83.763  1.00 97.94  ? 220 LEU A CA    1 
ATOM   1377 C  C     . LEU B 2 220 ? 125.116 123.505 84.029  1.00 100.03 ? 220 LEU A C     1 
ATOM   1378 O  O     . LEU B 2 220 ? 125.110 122.372 83.536  1.00 102.46 ? 220 LEU A O     1 
ATOM   1379 C  CB    . LEU B 2 220 ? 124.390 125.533 82.742  1.00 104.14 ? 220 LEU A CB    1 
ATOM   1380 C  CG    . LEU B 2 220 ? 123.275 126.461 82.252  1.00 105.96 ? 220 LEU A CG    1 
ATOM   1381 C  CD1   . LEU B 2 220 ? 123.506 127.876 82.752  1.00 104.79 ? 220 LEU A CD1   1 
ATOM   1382 C  CD2   . LEU B 2 220 ? 123.175 126.437 80.736  1.00 110.28 ? 220 LEU A CD2   1 
ATOM   1383 N  N     . LYS B 2 221 ? 126.108 123.930 84.813  1.00 99.00  ? 221 LYS A N     1 
ATOM   1384 C  CA    . LYS B 2 221 ? 127.210 123.033 85.144  1.00 100.03 ? 221 LYS A CA    1 
ATOM   1385 C  C     . LYS B 2 221 ? 126.736 121.903 86.047  1.00 100.00 ? 221 LYS A C     1 
ATOM   1386 O  O     . LYS B 2 221 ? 127.205 120.762 85.930  1.00 101.01 ? 221 LYS A O     1 
ATOM   1387 C  CB    . LYS B 2 221 ? 128.336 123.813 85.823  1.00 99.77  ? 221 LYS A CB    1 
ATOM   1388 C  CG    . LYS B 2 221 ? 129.269 124.551 84.860  1.00 103.52 ? 221 LYS A CG    1 
ATOM   1389 C  CD    . LYS B 2 221 ? 128.767 125.946 84.466  1.00 104.30 ? 221 LYS A CD    1 
ATOM   1390 C  CE    . LYS B 2 221 ? 128.599 126.895 85.655  1.00 103.33 ? 221 LYS A CE    1 
ATOM   1391 N  NZ    . LYS B 2 221 ? 127.867 128.134 85.285  1.00 102.85 ? 221 LYS A NZ    1 
ATOM   1392 N  N     . LEU B 2 222 ? 125.807 122.207 86.956  1.00 97.76  ? 222 LEU A N     1 
ATOM   1393 C  CA    . LEU B 2 222 ? 125.336 121.210 87.910  1.00 96.59  ? 222 LEU A CA    1 
ATOM   1394 C  C     . LEU B 2 222 ? 124.600 120.076 87.209  1.00 96.67  ? 222 LEU A C     1 
ATOM   1395 O  O     . LEU B 2 222 ? 124.727 118.910 87.603  1.00 97.91  ? 222 LEU A O     1 
ATOM   1396 C  CB    . LEU B 2 222 ? 124.438 121.878 88.952  1.00 92.23  ? 222 LEU A CB    1 
ATOM   1397 C  CG    . LEU B 2 222 ? 124.421 121.271 90.356  1.00 87.50  ? 222 LEU A CG    1 
ATOM   1398 C  CD1   . LEU B 2 222 ? 125.814 121.225 90.970  1.00 91.00  ? 222 LEU A CD1   1 
ATOM   1399 C  CD2   . LEU B 2 222 ? 123.475 122.052 91.252  1.00 82.84  ? 222 LEU A CD2   1 
ATOM   1400 N  N     . TYR B 2 223 ? 123.828 120.393 86.168  1.00 94.38  ? 223 TYR A N     1 
ATOM   1401 C  CA    . TYR B 2 223 ? 123.132 119.344 85.430  1.00 91.15  ? 223 TYR A CA    1 
ATOM   1402 C  C     . TYR B 2 223 ? 124.114 118.319 84.886  1.00 95.04  ? 223 TYR A C     1 
ATOM   1403 O  O     . TYR B 2 223 ? 123.900 117.110 85.017  1.00 95.79  ? 223 TYR A O     1 
ATOM   1404 C  CB    . TYR B 2 223 ? 122.302 119.957 84.300  1.00 84.13  ? 223 TYR A CB    1 
ATOM   1405 C  CG    . TYR B 2 223 ? 121.933 118.991 83.189  1.00 82.76  ? 223 TYR A CG    1 
ATOM   1406 C  CD1   . TYR B 2 223 ? 122.837 118.683 82.178  1.00 86.95  ? 223 TYR A CD1   1 
ATOM   1407 C  CD2   . TYR B 2 223 ? 120.696 118.364 83.166  1.00 81.69  ? 223 TYR A CD2   1 
ATOM   1408 C  CE1   . TYR B 2 223 ? 122.509 117.802 81.169  1.00 90.28  ? 223 TYR A CE1   1 
ATOM   1409 C  CE2   . TYR B 2 223 ? 120.362 117.481 82.158  1.00 85.58  ? 223 TYR A CE2   1 
ATOM   1410 C  CZ    . TYR B 2 223 ? 121.270 117.203 81.163  1.00 91.67  ? 223 TYR A CZ    1 
ATOM   1411 O  OH    . TYR B 2 223 ? 120.942 116.322 80.159  1.00 93.08  ? 223 TYR A OH    1 
ATOM   1412 N  N     . LYS B 2 224 ? 125.202 118.781 84.270  1.00 95.47  ? 224 LYS A N     1 
ATOM   1413 C  CA    . LYS B 2 224 ? 126.192 117.847 83.741  1.00 97.64  ? 224 LYS A CA    1 
ATOM   1414 C  C     . LYS B 2 224 ? 126.886 117.102 84.873  1.00 100.53 ? 224 LYS A C     1 
ATOM   1415 O  O     . LYS B 2 224 ? 127.040 115.874 84.823  1.00 101.70 ? 224 LYS A O     1 
ATOM   1416 C  CB    . LYS B 2 224 ? 127.223 118.571 82.864  1.00 99.51  ? 224 LYS A CB    1 
ATOM   1417 C  CG    . LYS B 2 224 ? 126.759 119.885 82.231  1.00 100.62 ? 224 LYS A CG    1 
ATOM   1418 C  CD    . LYS B 2 224 ? 127.908 120.624 81.572  1.00 102.39 ? 224 LYS A CD    1 
ATOM   1419 C  CE    . LYS B 2 224 ? 127.460 121.986 81.063  1.00 102.57 ? 224 LYS A CE    1 
ATOM   1420 N  NZ    . LYS B 2 224 ? 126.497 121.880 79.935  1.00 100.85 ? 224 LYS A NZ    1 
ATOM   1421 N  N     . LYS B 2 225 ? 127.296 117.830 85.915  1.00 101.47 ? 225 LYS A N     1 
ATOM   1422 C  CA    . LYS B 2 225 ? 128.014 117.206 87.019  1.00 106.35 ? 225 LYS A CA    1 
ATOM   1423 C  C     . LYS B 2 225 ? 127.178 116.150 87.726  1.00 106.17 ? 225 LYS A C     1 
ATOM   1424 O  O     . LYS B 2 225 ? 127.742 115.259 88.369  1.00 108.80 ? 225 LYS A O     1 
ATOM   1425 C  CB    . LYS B 2 225 ? 128.458 118.277 88.023  1.00 106.71 ? 225 LYS A CB    1 
ATOM   1426 C  CG    . LYS B 2 225 ? 129.492 117.830 89.061  1.00 116.91 ? 225 LYS A CG    1 
ATOM   1427 C  CD    . LYS B 2 225 ? 130.798 117.335 88.446  1.00 121.59 ? 225 LYS A CD    1 
ATOM   1428 C  CE    . LYS B 2 225 ? 131.624 116.555 89.456  1.00 123.49 ? 225 LYS A CE    1 
ATOM   1429 N  NZ    . LYS B 2 225 ? 132.262 117.446 90.464  1.00 128.55 ? 225 LYS A NZ    1 
ATOM   1430 N  N     . LEU B 2 226 ? 125.852 116.233 87.634  1.00 100.38 ? 226 LEU A N     1 
ATOM   1431 C  CA    . LEU B 2 226 ? 124.991 115.219 88.233  1.00 95.97  ? 226 LEU A CA    1 
ATOM   1432 C  C     . LEU B 2 226 ? 124.645 114.104 87.255  1.00 97.59  ? 226 LEU A C     1 
ATOM   1433 O  O     . LEU B 2 226 ? 124.665 112.925 87.628  1.00 99.25  ? 226 LEU A O     1 
ATOM   1434 C  CB    . LEU B 2 226 ? 123.705 115.863 88.760  1.00 88.97  ? 226 LEU A CB    1 
ATOM   1435 C  CG    . LEU B 2 226 ? 123.691 116.262 90.240  1.00 83.30  ? 226 LEU A CG    1 
ATOM   1436 C  CD1   . LEU B 2 226 ? 124.080 115.106 91.153  1.00 82.11  ? 226 LEU A CD1   1 
ATOM   1437 C  CD2   . LEU B 2 226 ? 124.612 117.441 90.472  1.00 84.64  ? 226 LEU A CD2   1 
ATOM   1438 N  N     . LYS B 2 227 ? 124.325 114.449 86.007  1.00 97.21  ? 227 LYS A N     1 
ATOM   1439 C  CA    . LYS B 2 227 ? 123.942 113.433 85.036  1.00 96.40  ? 227 LYS A CA    1 
ATOM   1440 C  C     . LYS B 2 227 ? 125.098 112.485 84.747  1.00 98.24  ? 227 LYS A C     1 
ATOM   1441 O  O     . LYS B 2 227 ? 124.909 111.263 84.692  1.00 97.03  ? 227 LYS A O     1 
ATOM   1442 C  CB    . LYS B 2 227 ? 123.458 114.099 83.749  1.00 96.12  ? 227 LYS A CB    1 
ATOM   1443 C  CG    . LYS B 2 227 ? 122.961 113.126 82.690  1.00 95.59  ? 227 LYS A CG    1 
ATOM   1444 C  CD    . LYS B 2 227 ? 121.878 112.183 83.210  1.00 90.94  ? 227 LYS A CD    1 
ATOM   1445 C  CE    . LYS B 2 227 ? 120.718 112.928 83.852  1.00 82.86  ? 227 LYS A CE    1 
ATOM   1446 N  NZ    . LYS B 2 227 ? 120.009 113.802 82.885  1.00 80.42  ? 227 LYS A NZ    1 
ATOM   1447 N  N     . GLU B 2 228 ? 126.307 113.024 84.567  1.00 102.43 ? 228 GLU A N     1 
ATOM   1448 C  CA    . GLU B 2 228 ? 127.448 112.160 84.288  1.00 106.15 ? 228 GLU A CA    1 
ATOM   1449 C  C     . GLU B 2 228 ? 127.713 111.215 85.452  1.00 106.90 ? 228 GLU A C     1 
ATOM   1450 O  O     . GLU B 2 228 ? 128.041 110.040 85.248  1.00 107.72 ? 228 GLU A O     1 
ATOM   1451 C  CB    . GLU B 2 228 ? 128.686 113.005 83.988  1.00 112.00 ? 228 GLU A CB    1 
ATOM   1452 C  CG    . GLU B 2 228 ? 129.812 112.233 83.307  1.00 115.84 ? 228 GLU A CG    1 
ATOM   1453 C  CD    . GLU B 2 228 ? 131.031 112.039 84.193  1.00 120.35 ? 228 GLU A CD    1 
ATOM   1454 O  OE1   . GLU B 2 228 ? 131.129 112.698 85.250  1.00 119.07 ? 228 GLU A OE1   1 
ATOM   1455 O  OE2   . GLU B 2 228 ? 131.900 111.219 83.828  1.00 124.76 ? 228 GLU A OE2   1 
ATOM   1456 N  N     . GLU B 2 229 ? 127.578 111.710 86.684  1.00 106.89 ? 229 GLU A N     1 
ATOM   1457 C  CA    . GLU B 2 229 ? 127.857 110.880 87.850  1.00 108.68 ? 229 GLU A CA    1 
ATOM   1458 C  C     . GLU B 2 229 ? 126.769 109.840 88.089  1.00 104.58 ? 229 GLU A C     1 
ATOM   1459 O  O     . GLU B 2 229 ? 127.059 108.759 88.614  1.00 102.64 ? 229 GLU A O     1 
ATOM   1460 C  CB    . GLU B 2 229 ? 128.038 111.765 89.082  1.00 106.60 ? 229 GLU A CB    1 
ATOM   1461 C  CG    . GLU B 2 229 ? 129.465 112.254 89.273  1.00 112.85 ? 229 GLU A CG    1 
ATOM   1462 C  CD    . GLU B 2 229 ? 129.909 113.208 88.183  1.00 115.86 ? 229 GLU A CD    1 
ATOM   1463 O  OE1   . GLU B 2 229 ? 129.099 113.503 87.279  1.00 108.96 ? 229 GLU A OE1   1 
ATOM   1464 O  OE2   . GLU B 2 229 ? 131.071 113.665 88.230  1.00 120.98 ? 229 GLU A OE2   1 
ATOM   1465 N  N     . ILE B 2 230 ? 125.521 110.136 87.725  1.00 101.10 ? 230 ILE A N     1 
ATOM   1466 C  CA    . ILE B 2 230 ? 124.476 109.127 87.884  1.00 95.27  ? 230 ILE A CA    1 
ATOM   1467 C  C     . ILE B 2 230 ? 124.542 108.103 86.758  1.00 95.79  ? 230 ILE A C     1 
ATOM   1468 O  O     . ILE B 2 230 ? 124.123 106.953 86.934  1.00 89.89  ? 230 ILE A O     1 
ATOM   1469 C  CB    . ILE B 2 230 ? 123.078 109.770 87.981  1.00 82.46  ? 230 ILE A CB    1 
ATOM   1470 C  CG1   . ILE B 2 230 ? 122.542 110.180 86.602  1.00 87.58  ? 230 ILE A CG1   1 
ATOM   1471 C  CG2   . ILE B 2 230 ? 123.079 110.956 88.948  1.00 84.58  ? 230 ILE A CG2   1 
ATOM   1472 C  CD1   . ILE B 2 230 ? 121.053 110.377 86.576  1.00 80.99  ? 230 ILE A CD1   1 
ATOM   1473 N  N     . LYS B 2 231 ? 125.053 108.493 85.590  1.00 101.21 ? 231 LYS A N     1 
ATOM   1474 C  CA    . LYS B 2 231 ? 125.196 107.543 84.495  1.00 101.09 ? 231 LYS A CA    1 
ATOM   1475 C  C     . LYS B 2 231 ? 126.372 106.602 84.716  1.00 101.49 ? 231 LYS A C     1 
ATOM   1476 O  O     . LYS B 2 231 ? 126.323 105.445 84.285  1.00 101.26 ? 231 LYS A O     1 
ATOM   1477 C  CB    . LYS B 2 231 ? 125.361 108.290 83.169  1.00 103.38 ? 231 LYS A CB    1 
ATOM   1478 C  CG    . LYS B 2 231 ? 124.783 107.556 81.971  1.00 104.28 ? 231 LYS A CG    1 
ATOM   1479 C  CD    . LYS B 2 231 ? 123.270 107.424 82.077  1.00 101.52 ? 231 LYS A CD    1 
ATOM   1480 C  CE    . LYS B 2 231 ? 122.615 107.291 80.712  1.00 104.94 ? 231 LYS A CE    1 
ATOM   1481 N  NZ    . LYS B 2 231 ? 121.464 106.349 80.742  1.00 104.03 ? 231 LYS A NZ    1 
ATOM   1482 N  N     . LYS B 2 232 ? 127.431 107.074 85.377  1.00 101.70 ? 232 LYS A N     1 
ATOM   1483 C  CA    . LYS B 2 232 ? 128.558 106.206 85.691  1.00 103.40 ? 232 LYS A CA    1 
ATOM   1484 C  C     . LYS B 2 232 ? 128.213 105.178 86.758  1.00 102.33 ? 232 LYS A C     1 
ATOM   1485 O  O     . LYS B 2 232 ? 128.936 104.186 86.899  1.00 104.03 ? 232 LYS A O     1 
ATOM   1486 C  CB    . LYS B 2 232 ? 129.763 107.047 86.134  1.00 106.76 ? 232 LYS A CB    1 
ATOM   1487 C  CG    . LYS B 2 232 ? 129.763 107.480 87.604  1.00 106.69 ? 232 LYS A CG    1 
ATOM   1488 C  CD    . LYS B 2 232 ? 131.150 107.878 88.080  1.00 111.96 ? 232 LYS A CD    1 
ATOM   1489 C  CE    . LYS B 2 232 ? 131.813 106.759 88.862  1.00 118.92 ? 232 LYS A CE    1 
ATOM   1490 N  NZ    . LYS B 2 232 ? 133.225 107.078 89.199  1.00 124.81 ? 232 LYS A NZ    1 
ATOM   1491 N  N     . GLU B 2 233 ? 127.130 105.389 87.504  1.00 99.48  ? 233 GLU A N     1 
ATOM   1492 C  CA    . GLU B 2 233 ? 126.766 104.531 88.624  1.00 96.84  ? 233 GLU A CA    1 
ATOM   1493 C  C     . GLU B 2 233 ? 125.541 103.677 88.320  1.00 90.79  ? 233 GLU A C     1 
ATOM   1494 O  O     . GLU B 2 233 ? 125.023 103.007 89.219  1.00 89.12  ? 233 GLU A O     1 
ATOM   1495 C  CB    . GLU B 2 233 ? 126.525 105.388 89.871  1.00 97.27  ? 233 GLU A CB    1 
ATOM   1496 C  CG    . GLU B 2 233 ? 126.431 104.612 91.184  1.00 104.21 ? 233 GLU A CG    1 
ATOM   1497 C  CD    . GLU B 2 233 ? 127.741 104.583 91.953  1.00 110.93 ? 233 GLU A CD    1 
ATOM   1498 O  OE1   . GLU B 2 233 ? 128.611 105.443 91.699  1.00 112.83 ? 233 GLU A OE1   1 
ATOM   1499 O  OE2   . GLU B 2 233 ? 127.903 103.692 92.813  1.00 109.26 ? 233 GLU A OE2   1 
ATOM   1500 N  N     . ASN B 2 234 ? 125.064 103.684 87.076  1.00 90.77  ? 234 ASN A N     1 
ATOM   1501 C  CA    . ASN B 2 234 ? 123.905 102.882 86.686  1.00 88.83  ? 234 ASN A CA    1 
ATOM   1502 C  C     . ASN B 2 234 ? 122.693 103.206 87.556  1.00 81.89  ? 234 ASN A C     1 
ATOM   1503 O  O     . ASN B 2 234 ? 121.903 102.328 87.909  1.00 78.08  ? 234 ASN A O     1 
ATOM   1504 C  CB    . ASN B 2 234 ? 124.226 101.387 86.742  1.00 85.94  ? 234 ASN A CB    1 
ATOM   1505 C  CG    . ASN B 2 234 ? 123.440 100.586 85.724  1.00 81.81  ? 234 ASN A CG    1 
ATOM   1506 O  OD1   . ASN B 2 234 ? 122.238 100.787 85.557  1.00 77.63  ? 234 ASN A OD1   1 
ATOM   1507 N  ND2   . ASN B 2 234 ? 124.117 99.676  85.034  1.00 81.30  ? 234 ASN A ND2   1 
ATOM   1508 N  N     . LEU B 2 235 ? 122.545 104.482 87.902  1.00 78.41  ? 235 LEU A N     1 
ATOM   1509 C  CA    . LEU B 2 235 ? 121.391 104.970 88.644  1.00 74.14  ? 235 LEU A CA    1 
ATOM   1510 C  C     . LEU B 2 235 ? 120.414 105.720 87.750  1.00 76.51  ? 235 LEU A C     1 
ATOM   1511 O  O     . LEU B 2 235 ? 119.496 106.370 88.257  1.00 74.26  ? 235 LEU A O     1 
ATOM   1512 C  CB    . LEU B 2 235 ? 121.850 105.877 89.787  1.00 77.44  ? 235 LEU A CB    1 
ATOM   1513 C  CG    . LEU B 2 235 ? 122.372 105.166 91.034  1.00 72.71  ? 235 LEU A CG    1 
ATOM   1514 C  CD1   . LEU B 2 235 ? 123.287 106.088 91.819  1.00 76.12  ? 235 LEU A CD1   1 
ATOM   1515 C  CD2   . LEU B 2 235 ? 121.221 104.687 91.898  1.00 67.86  ? 235 LEU A CD2   1 
ATOM   1516 N  N     . HIS B 2 236 ? 120.589 105.644 86.429  1.00 78.22  ? 236 HIS A N     1 
ATOM   1517 C  CA    . HIS B 2 236 ? 119.801 106.484 85.534  1.00 75.95  ? 236 HIS A CA    1 
ATOM   1518 C  C     . HIS B 2 236 ? 118.318 106.142 85.606  1.00 72.91  ? 236 HIS A C     1 
ATOM   1519 O  O     . HIS B 2 236 ? 117.468 107.035 85.516  1.00 74.41  ? 236 HIS A O     1 
ATOM   1520 C  CB    . HIS B 2 236 ? 120.315 106.362 84.096  1.00 77.91  ? 236 HIS A CB    1 
ATOM   1521 C  CG    . HIS B 2 236 ? 120.658 104.962 83.687  1.00 82.19  ? 236 HIS A CG    1 
ATOM   1522 N  ND1   . HIS B 2 236 ? 119.701 103.996 83.466  1.00 80.96  ? 236 HIS A ND1   1 
ATOM   1523 C  CD2   . HIS B 2 236 ? 121.853 104.365 83.465  1.00 86.71  ? 236 HIS A CD2   1 
ATOM   1524 C  CE1   . HIS B 2 236 ? 120.290 102.865 83.122  1.00 82.68  ? 236 HIS A CE1   1 
ATOM   1525 N  NE2   . HIS B 2 236 ? 121.596 103.061 83.113  1.00 86.88  ? 236 HIS A NE2   1 
ATOM   1526 N  N     . ILE B 2 237 ? 117.980 104.862 85.775  1.00 71.43  ? 237 ILE A N     1 
ATOM   1527 C  CA    . ILE B 2 237 ? 116.570 104.474 85.798  1.00 69.14  ? 237 ILE A CA    1 
ATOM   1528 C  C     . ILE B 2 237 ? 115.859 105.119 86.981  1.00 62.83  ? 237 ILE A C     1 
ATOM   1529 O  O     . ILE B 2 237 ? 114.804 105.748 86.828  1.00 64.52  ? 237 ILE A O     1 
ATOM   1530 C  CB    . ILE B 2 237 ? 116.428 102.942 85.831  1.00 69.48  ? 237 ILE A CB    1 
ATOM   1531 C  CG1   . ILE B 2 237 ? 116.957 102.324 84.537  1.00 69.18  ? 237 ILE A CG1   1 
ATOM   1532 C  CG2   . ILE B 2 237 ? 114.975 102.555 86.039  1.00 64.35  ? 237 ILE A CG2   1 
ATOM   1533 C  CD1   . ILE B 2 237 ? 117.361 100.878 84.676  1.00 70.73  ? 237 ILE A CD1   1 
ATOM   1534 N  N     . VAL B 2 238 ? 116.428 104.981 88.179  1.00 56.13  ? 238 VAL A N     1 
ATOM   1535 C  CA    . VAL B 2 238 ? 115.758 105.503 89.365  1.00 53.18  ? 238 VAL A CA    1 
ATOM   1536 C  C     . VAL B 2 238 ? 115.728 107.024 89.331  1.00 57.52  ? 238 VAL A C     1 
ATOM   1537 O  O     . VAL B 2 238 ? 114.744 107.648 89.745  1.00 57.97  ? 238 VAL A O     1 
ATOM   1538 C  CB    . VAL B 2 238 ? 116.434 104.983 90.647  1.00 51.05  ? 238 VAL A CB    1 
ATOM   1539 C  CG1   . VAL B 2 238 ? 117.887 105.430 90.718  1.00 51.80  ? 238 VAL A CG1   1 
ATOM   1540 C  CG2   . VAL B 2 238 ? 115.658 105.439 91.871  1.00 51.97  ? 238 VAL A CG2   1 
ATOM   1541 N  N     . ASN B 2 239 ? 116.805 107.646 88.848  1.00 60.87  ? 239 ASN A N     1 
ATOM   1542 C  CA    . ASN B 2 239 ? 116.834 109.102 88.761  1.00 58.00  ? 239 ASN A CA    1 
ATOM   1543 C  C     . ASN B 2 239 ? 115.774 109.615 87.797  1.00 55.60  ? 239 ASN A C     1 
ATOM   1544 O  O     . ASN B 2 239 ? 115.082 110.597 88.090  1.00 54.32  ? 239 ASN A O     1 
ATOM   1545 C  CB    . ASN B 2 239 ? 118.222 109.570 88.333  1.00 57.44  ? 239 ASN A CB    1 
ATOM   1546 C  CG    . ASN B 2 239 ? 118.528 110.969 88.805  1.00 62.62  ? 239 ASN A CG    1 
ATOM   1547 O  OD1   . ASN B 2 239 ? 117.644 111.823 88.854  1.00 64.45  ? 239 ASN A OD1   1 
ATOM   1548 N  ND2   . ASN B 2 239 ? 119.779 111.210 89.176  1.00 66.24  ? 239 ASN A ND2   1 
ATOM   1549 N  N     . ASP B 2 240 ? 115.626 108.959 86.645  1.00 60.09  ? 240 ASP A N     1 
ATOM   1550 C  CA    . ASP B 2 240 ? 114.572 109.336 85.711  1.00 60.19  ? 240 ASP A CA    1 
ATOM   1551 C  C     . ASP B 2 240 ? 113.198 109.158 86.338  1.00 56.10  ? 240 ASP A C     1 
ATOM   1552 O  O     . ASP B 2 240 ? 112.321 110.020 86.191  1.00 57.06  ? 240 ASP A O     1 
ATOM   1553 C  CB    . ASP B 2 240 ? 114.685 108.504 84.436  1.00 64.53  ? 240 ASP A CB    1 
ATOM   1554 C  CG    . ASP B 2 240 ? 113.374 108.411 83.687  1.00 67.08  ? 240 ASP A CG    1 
ATOM   1555 O  OD1   . ASP B 2 240 ? 112.757 109.467 83.434  1.00 63.11  ? 240 ASP A OD1   1 
ATOM   1556 O  OD2   . ASP B 2 240 ? 112.956 107.282 83.355  1.00 69.71  ? 240 ASP A OD2   1 
ATOM   1557 N  N     . ILE B 2 241 ? 112.990 108.046 87.046  1.00 52.85  ? 241 ILE A N     1 
ATOM   1558 C  CA    . ILE B 2 241 ? 111.692 107.810 87.666  1.00 49.45  ? 241 ILE A CA    1 
ATOM   1559 C  C     . ILE B 2 241 ? 111.381 108.905 88.674  1.00 48.24  ? 241 ILE A C     1 
ATOM   1560 O  O     . ILE B 2 241 ? 110.275 109.451 88.692  1.00 53.68  ? 241 ILE A O     1 
ATOM   1561 C  CB    . ILE B 2 241 ? 111.648 106.413 88.311  1.00 49.93  ? 241 ILE A CB    1 
ATOM   1562 C  CG1   . ILE B 2 241 ? 111.752 105.335 87.230  1.00 50.07  ? 241 ILE A CG1   1 
ATOM   1563 C  CG2   . ILE B 2 241 ? 110.369 106.251 89.120  1.00 45.35  ? 241 ILE A CG2   1 
ATOM   1564 C  CD1   . ILE B 2 241 ? 112.037 103.950 87.759  1.00 49.29  ? 241 ILE A CD1   1 
ATOM   1565 N  N     . GLU B 2 242 ? 112.354 109.262 89.513  1.00 44.84  ? 242 GLU A N     1 
ATOM   1566 C  CA    . GLU B 2 242 ? 112.111 110.299 90.511  1.00 47.13  ? 242 GLU A CA    1 
ATOM   1567 C  C     . GLU B 2 242 ? 111.849 111.651 89.856  1.00 51.54  ? 242 GLU A C     1 
ATOM   1568 O  O     . GLU B 2 242 ? 110.916 112.367 90.245  1.00 51.96  ? 242 GLU A O     1 
ATOM   1569 C  CB    . GLU B 2 242 ? 113.297 110.393 91.470  1.00 48.96  ? 242 GLU A CB    1 
ATOM   1570 C  CG    . GLU B 2 242 ? 113.201 109.455 92.658  1.00 49.08  ? 242 GLU A CG    1 
ATOM   1571 C  CD    . GLU B 2 242 ? 114.186 109.800 93.757  1.00 54.37  ? 242 GLU A CD    1 
ATOM   1572 O  OE1   . GLU B 2 242 ? 113.890 110.708 94.560  1.00 53.57  ? 242 GLU A OE1   1 
ATOM   1573 O  OE2   . GLU B 2 242 ? 115.254 109.162 93.825  1.00 55.72  ? 242 GLU A OE2   1 
ATOM   1574 N  N     . ASN B 2 243 ? 112.651 112.013 88.851  1.00 50.38  ? 243 ASN A N     1 
ATOM   1575 C  CA    . ASN B 2 243 ? 112.487 113.312 88.212  1.00 43.21  ? 243 ASN A CA    1 
ATOM   1576 C  C     . ASN B 2 243 ? 111.144 113.423 87.510  1.00 44.01  ? 243 ASN A C     1 
ATOM   1577 O  O     . ASN B 2 243 ? 110.536 114.498 87.509  1.00 45.95  ? 243 ASN A O     1 
ATOM   1578 C  CB    . ASN B 2 243 ? 113.623 113.554 87.224  1.00 48.14  ? 243 ASN A CB    1 
ATOM   1579 C  CG    . ASN B 2 243 ? 114.940 113.814 87.913  1.00 52.15  ? 243 ASN A CG    1 
ATOM   1580 O  OD1   . ASN B 2 243 ? 115.007 114.579 88.872  1.00 52.56  ? 243 ASN A OD1   1 
ATOM   1581 N  ND2   . ASN B 2 243 ? 115.997 113.170 87.437  1.00 57.25  ? 243 ASN A ND2   1 
ATOM   1582 N  N     . LYS B 2 244 ? 110.664 112.335 86.908  1.00 46.80  ? 244 LYS A N     1 
ATOM   1583 C  CA    . LYS B 2 244 ? 109.327 112.348 86.329  1.00 46.78  ? 244 LYS A CA    1 
ATOM   1584 C  C     . LYS B 2 244 ? 108.241 112.242 87.390  1.00 47.08  ? 244 LYS A C     1 
ATOM   1585 O  O     . LYS B 2 244 ? 107.089 112.592 87.117  1.00 47.87  ? 244 LYS A O     1 
ATOM   1586 C  CB    . LYS B 2 244 ? 109.182 111.208 85.319  1.00 49.18  ? 244 LYS A CB    1 
ATOM   1587 C  CG    . LYS B 2 244 ? 110.003 111.402 84.057  1.00 50.72  ? 244 LYS A CG    1 
ATOM   1588 C  CD    . LYS B 2 244 ? 109.758 110.295 83.052  1.00 46.33  ? 244 LYS A CD    1 
ATOM   1589 C  CE    . LYS B 2 244 ? 108.445 110.490 82.325  1.00 46.64  ? 244 LYS A CE    1 
ATOM   1590 N  NZ    . LYS B 2 244 ? 108.282 109.531 81.204  1.00 51.58  ? 244 LYS A NZ    1 
ATOM   1591 N  N     . CYS B 2 245 ? 108.582 111.761 88.584  1.00 45.37  ? 245 CYS A N     1 
ATOM   1592 C  CA    . CYS B 2 245 ? 107.648 111.691 89.696  1.00 41.70  ? 245 CYS A CA    1 
ATOM   1593 C  C     . CYS B 2 245 ? 107.542 113.001 90.456  1.00 47.00  ? 245 CYS A C     1 
ATOM   1594 O  O     . CYS B 2 245 ? 106.637 113.146 91.284  1.00 47.62  ? 245 CYS A O     1 
ATOM   1595 C  CB    . CYS B 2 245 ? 108.069 110.585 90.669  1.00 44.48  ? 245 CYS A CB    1 
ATOM   1596 S  SG    . CYS B 2 245 ? 106.734 109.948 91.698  1.00 67.71  ? 245 CYS A SG    1 
ATOM   1597 N  N     . ILE B 2 246 ? 108.434 113.956 90.191  1.00 50.85  ? 246 ILE A N     1 
ATOM   1598 C  CA    . ILE B 2 246 ? 108.335 115.262 90.840  1.00 48.22  ? 246 ILE A CA    1 
ATOM   1599 C  C     . ILE B 2 246 ? 106.965 115.879 90.576  1.00 45.71  ? 246 ILE A C     1 
ATOM   1600 O  O     . ILE B 2 246 ? 106.318 116.412 91.484  1.00 45.70  ? 246 ILE A O     1 
ATOM   1601 C  CB    . ILE B 2 246 ? 109.472 116.184 90.363  1.00 46.26  ? 246 ILE A CB    1 
ATOM   1602 C  CG1   . ILE B 2 246 ? 110.719 115.970 91.224  1.00 47.29  ? 246 ILE A CG1   1 
ATOM   1603 C  CG2   . ILE B 2 246 ? 109.036 117.643 90.424  1.00 45.16  ? 246 ILE A CG2   1 
ATOM   1604 C  CD1   . ILE B 2 246 ? 111.916 116.787 90.789  1.00 48.81  ? 246 ILE A CD1   1 
ATOM   1605 N  N     . LEU B 2 247 ? 106.507 115.823 89.323  1.00 47.76  ? 247 LEU A N     1 
ATOM   1606 C  CA    . LEU B 2 247 ? 105.215 116.420 88.981  1.00 50.80  ? 247 LEU A CA    1 
ATOM   1607 C  C     . LEU B 2 247 ? 104.050 115.763 89.711  1.00 49.87  ? 247 LEU A C     1 
ATOM   1608 O  O     . LEU B 2 247 ? 103.186 116.492 90.229  1.00 50.59  ? 247 LEU A O     1 
ATOM   1609 C  CB    . LEU B 2 247 ? 105.013 116.372 87.463  1.00 50.75  ? 247 LEU A CB    1 
ATOM   1610 C  CG    . LEU B 2 247 ? 105.918 117.277 86.627  1.00 51.15  ? 247 LEU A CG    1 
ATOM   1611 C  CD1   . LEU B 2 247 ? 107.266 116.626 86.370  1.00 52.93  ? 247 LEU A CD1   1 
ATOM   1612 C  CD2   . LEU B 2 247 ? 105.237 117.614 85.314  1.00 60.56  ? 247 LEU A CD2   1 
ATOM   1613 N  N     . PRO B 2 248 ? 103.936 114.434 89.769  1.00 47.42  ? 248 PRO A N     1 
ATOM   1614 C  CA    . PRO B 2 248 ? 102.871 113.838 90.594  1.00 48.09  ? 248 PRO A CA    1 
ATOM   1615 C  C     . PRO B 2 248 ? 102.895 114.298 92.040  1.00 54.82  ? 248 PRO A C     1 
ATOM   1616 O  O     . PRO B 2 248 ? 101.831 114.494 92.642  1.00 62.82  ? 248 PRO A O     1 
ATOM   1617 C  CB    . PRO B 2 248 ? 103.152 112.335 90.470  1.00 46.72  ? 248 PRO A CB    1 
ATOM   1618 C  CG    . PRO B 2 248 ? 103.795 112.191 89.155  1.00 51.52  ? 248 PRO A CG    1 
ATOM   1619 C  CD    . PRO B 2 248 ? 104.571 113.439 88.891  1.00 52.26  ? 248 PRO A CD    1 
ATOM   1620 N  N     . ILE B 2 249 ? 104.081 114.476 92.623  1.00 53.26  ? 249 ILE A N     1 
ATOM   1621 C  CA    . ILE B 2 249 ? 104.165 114.963 93.998  1.00 52.94  ? 249 ILE A CA    1 
ATOM   1622 C  C     . ILE B 2 249 ? 103.551 116.353 94.101  1.00 50.72  ? 249 ILE A C     1 
ATOM   1623 O  O     . ILE B 2 249 ? 102.781 116.648 95.023  1.00 49.13  ? 249 ILE A O     1 
ATOM   1624 C  CB    . ILE B 2 249 ? 105.627 114.953 94.481  1.00 50.01  ? 249 ILE A CB    1 
ATOM   1625 C  CG1   . ILE B 2 249 ? 106.101 113.522 94.742  1.00 48.59  ? 249 ILE A CG1   1 
ATOM   1626 C  CG2   . ILE B 2 249 ? 105.784 115.801 95.735  1.00 47.63  ? 249 ILE A CG2   1 
ATOM   1627 C  CD1   . ILE B 2 249 ? 105.252 112.751 95.735  1.00 47.95  ? 249 ILE A CD1   1 
ATOM   1628 N  N     . CYS B 2 250 ? 103.889 117.228 93.153  1.00 49.53  ? 250 CYS A N     1 
ATOM   1629 C  CA    . CYS B 2 250 ? 103.326 118.572 93.159  1.00 48.83  ? 250 CYS A CA    1 
ATOM   1630 C  C     . CYS B 2 250 ? 101.817 118.533 92.972  1.00 51.68  ? 250 CYS A C     1 
ATOM   1631 O  O     . CYS B 2 250 ? 101.091 119.333 93.571  1.00 57.16  ? 250 CYS A O     1 
ATOM   1632 C  CB    . CYS B 2 250 ? 103.984 119.417 92.071  1.00 49.15  ? 250 CYS A CB    1 
ATOM   1633 S  SG    . CYS B 2 250 ? 105.735 119.739 92.360  1.00 61.30  ? 250 CYS A SG    1 
ATOM   1634 N  N     . ASP B 2 251 ? 101.324 117.616 92.139  1.00 47.91  ? 251 ASP A N     1 
ATOM   1635 C  CA    . ASP B 2 251 ? 99.881  117.489 91.966  1.00 49.44  ? 251 ASP A CA    1 
ATOM   1636 C  C     . ASP B 2 251 ? 99.212  117.063 93.267  1.00 49.64  ? 251 ASP A C     1 
ATOM   1637 O  O     . ASP B 2 251 ? 98.156  117.593 93.635  1.00 52.98  ? 251 ASP A O     1 
ATOM   1638 C  CB    . ASP B 2 251 ? 99.573  116.494 90.848  1.00 55.71  ? 251 ASP A CB    1 
ATOM   1639 C  CG    . ASP B 2 251 ? 98.090  116.323 90.620  1.00 64.04  ? 251 ASP A CG    1 
ATOM   1640 O  OD1   . ASP B 2 251 ? 97.332  117.262 90.940  1.00 61.01  ? 251 ASP A OD1   1 
ATOM   1641 O  OD2   . ASP B 2 251 ? 97.678  115.255 90.121  1.00 68.18  ? 251 ASP A OD2   1 
ATOM   1642 N  N     . MET B 2 252 ? 99.817  116.109 93.979  1.00 51.33  ? 252 MET A N     1 
ATOM   1643 C  CA    . MET B 2 252 ? 99.282  115.705 95.276  1.00 55.49  ? 252 MET A CA    1 
ATOM   1644 C  C     . MET B 2 252 ? 99.259  116.873 96.249  1.00 55.71  ? 252 MET A C     1 
ATOM   1645 O  O     . MET B 2 252 ? 98.281  117.064 96.981  1.00 56.10  ? 252 MET A O     1 
ATOM   1646 C  CB    . MET B 2 252 ? 100.107 114.556 95.862  1.00 55.57  ? 252 MET A CB    1 
ATOM   1647 C  CG    . MET B 2 252 ? 99.448  113.195 95.731  1.00 53.64  ? 252 MET A CG    1 
ATOM   1648 S  SD    . MET B 2 252 ? 100.427 111.784 96.285  1.00 57.10  ? 252 MET A SD    1 
ATOM   1649 C  CE    . MET B 2 252 ? 102.034 112.182 95.615  1.00 48.10  ? 252 MET A CE    1 
ATOM   1650 N  N     . GLU B 2 253 ? 100.330 117.662 96.276  1.00 56.57  ? 253 GLU A N     1 
ATOM   1651 C  CA    . GLU B 2 253 ? 100.388 118.776 97.214  1.00 53.00  ? 253 GLU A CA    1 
ATOM   1652 C  C     . GLU B 2 253 ? 99.361  119.847 96.862  1.00 52.49  ? 253 GLU A C     1 
ATOM   1653 O  O     . GLU B 2 253 ? 98.724  120.419 97.753  1.00 57.07  ? 253 GLU A O     1 
ATOM   1654 C  CB    . GLU B 2 253 ? 101.798 119.357 97.241  1.00 50.34  ? 253 GLU A CB    1 
ATOM   1655 C  CG    . GLU B 2 253 ? 102.825 118.390 97.787  1.00 43.94  ? 253 GLU A CG    1 
ATOM   1656 C  CD    . GLU B 2 253 ? 104.027 119.086 98.377  1.00 40.96  ? 253 GLU A CD    1 
ATOM   1657 O  OE1   . GLU B 2 253 ? 104.268 120.259 98.030  1.00 47.59  ? 253 GLU A OE1   1 
ATOM   1658 O  OE2   . GLU B 2 253 ? 104.740 118.455 99.182  1.00 37.79  ? 253 GLU A OE2   1 
ATOM   1659 N  N     . LEU B 2 254 ? 99.184  120.129 95.570  1.00 50.95  ? 254 LEU A N     1 
ATOM   1660 C  CA    . LEU B 2 254 ? 98.208  121.131 95.157  1.00 53.98  ? 254 LEU A CA    1 
ATOM   1661 C  C     . LEU B 2 254 ? 96.791  120.681 95.481  1.00 56.03  ? 254 LEU A C     1 
ATOM   1662 O  O     . LEU B 2 254 ? 96.015  121.430 96.085  1.00 61.32  ? 254 LEU A O     1 
ATOM   1663 C  CB    . LEU B 2 254 ? 98.340  121.412 93.661  1.00 54.74  ? 254 LEU A CB    1 
ATOM   1664 C  CG    . LEU B 2 254 ? 99.198  122.611 93.263  1.00 54.34  ? 254 LEU A CG    1 
ATOM   1665 C  CD1   . LEU B 2 254 ? 100.482 122.649 94.066  1.00 51.65  ? 254 LEU A CD1   1 
ATOM   1666 C  CD2   . LEU B 2 254 ? 99.498  122.587 91.776  1.00 60.67  ? 254 LEU A CD2   1 
ATOM   1667 N  N     . ASN B 2 255 ? 96.429  119.462 95.084  1.00 51.98  ? 255 ASN A N     1 
ATOM   1668 C  CA    . ASN B 2 255 ? 95.064  119.006 95.316  1.00 52.73  ? 255 ASN A CA    1 
ATOM   1669 C  C     . ASN B 2 255 ? 94.794  118.824 96.802  1.00 59.20  ? 255 ASN A C     1 
ATOM   1670 O  O     . ASN B 2 255 ? 93.790  119.320 97.327  1.00 65.25  ? 255 ASN A O     1 
ATOM   1671 C  CB    . ASN B 2 255 ? 94.810  117.707 94.556  1.00 55.64  ? 255 ASN A CB    1 
ATOM   1672 C  CG    . ASN B 2 255 ? 94.993  117.866 93.067  1.00 61.97  ? 255 ASN A CG    1 
ATOM   1673 O  OD1   . ASN B 2 255 ? 94.476  118.807 92.466  1.00 66.32  ? 255 ASN A OD1   1 
ATOM   1674 N  ND2   . ASN B 2 255 ? 95.733  116.949 92.460  1.00 60.81  ? 255 ASN A ND2   1 
ATOM   1675 N  N     . GLY B 2 256 ? 95.684  118.130 97.500  1.00 59.85  ? 256 GLY A N     1 
ATOM   1676 C  CA    . GLY B 2 256 ? 95.398  117.806 98.880  1.00 59.14  ? 256 GLY A CA    1 
ATOM   1677 C  C     . GLY B 2 256 ? 94.199  116.873 98.950  1.00 60.46  ? 256 GLY A C     1 
ATOM   1678 O  O     . GLY B 2 256 ? 93.766  116.291 97.952  1.00 65.47  ? 256 GLY A O     1 
ATOM   1679 N  N     . ILE B 2 257 ? 93.647  116.746 100.152 1.00 56.52  ? 257 ILE A N     1 
ATOM   1680 C  CA    . ILE B 2 257 ? 92.495  115.881 100.379 1.00 58.79  ? 257 ILE A CA    1 
ATOM   1681 C  C     . ILE B 2 257 ? 91.478  116.623 101.235 1.00 63.49  ? 257 ILE A C     1 
ATOM   1682 O  O     . ILE B 2 257 ? 91.838  117.307 102.198 1.00 63.26  ? 257 ILE A O     1 
ATOM   1683 C  CB    . ILE B 2 257 ? 92.914  114.546 101.027 1.00 59.78  ? 257 ILE A CB    1 
ATOM   1684 C  CG1   . ILE B 2 257 ? 91.763  113.540 100.963 1.00 58.96  ? 257 ILE A CG1   1 
ATOM   1685 C  CG2   . ILE B 2 257 ? 93.367  114.759 102.460 1.00 63.50  ? 257 ILE A CG2   1 
ATOM   1686 C  CD1   . ILE B 2 257 ? 92.197  112.113 101.206 1.00 48.19  ? 257 ILE A CD1   1 
ATOM   1687 N  N     . LYS B 2 258 ? 90.205  116.482 100.873 1.00 65.99  ? 258 LYS A N     1 
ATOM   1688 C  CA    . LYS B 2 258 ? 89.107  117.207 101.499 1.00 67.85  ? 258 LYS A CA    1 
ATOM   1689 C  C     . LYS B 2 258 ? 88.536  116.397 102.657 1.00 72.15  ? 258 LYS A C     1 
ATOM   1690 O  O     . LYS B 2 258 ? 88.439  115.169 102.581 1.00 72.40  ? 258 LYS A O     1 
ATOM   1691 C  CB    . LYS B 2 258 ? 88.027  117.496 100.457 1.00 66.69  ? 258 LYS A CB    1 
ATOM   1692 C  CG    . LYS B 2 258 ? 86.929  118.450 100.891 1.00 72.12  ? 258 LYS A CG    1 
ATOM   1693 C  CD    . LYS B 2 258 ? 85.847  118.501 99.822  1.00 75.44  ? 258 LYS A CD    1 
ATOM   1694 C  CE    . LYS B 2 258 ? 84.713  119.434 100.196 1.00 79.77  ? 258 LYS A CE    1 
ATOM   1695 N  NZ    . LYS B 2 258 ? 84.980  120.800 99.671  1.00 82.10  ? 258 LYS A NZ    1 
ATOM   1696 N  N     . VAL B 2 259 ? 88.151  117.091 103.726 1.00 73.38  ? 259 VAL A N     1 
ATOM   1697 C  CA    . VAL B 2 259 ? 87.795  116.465 104.994 1.00 68.16  ? 259 VAL A CA    1 
ATOM   1698 C  C     . VAL B 2 259 ? 86.289  116.562 105.194 1.00 73.38  ? 259 VAL A C     1 
ATOM   1699 O  O     . VAL B 2 259 ? 85.681  117.596 104.891 1.00 77.47  ? 259 VAL A O     1 
ATOM   1700 C  CB    . VAL B 2 259 ? 88.532  117.120 106.173 1.00 65.02  ? 259 VAL A CB    1 
ATOM   1701 C  CG1   . VAL B 2 259 ? 88.044  116.533 107.487 1.00 71.16  ? 259 VAL A CG1   1 
ATOM   1702 C  CG2   . VAL B 2 259 ? 90.028  116.967 106.017 1.00 57.39  ? 259 VAL A CG2   1 
ATOM   1703 N  N     . ASP B 2 260 ? 85.691  115.482 105.703 1.00 71.49  ? 260 ASP A N     1 
ATOM   1704 C  CA    . ASP B 2 260 ? 84.284  115.472 106.107 1.00 82.16  ? 260 ASP A CA    1 
ATOM   1705 C  C     . ASP B 2 260 ? 84.172  116.030 107.528 1.00 87.96  ? 260 ASP A C     1 
ATOM   1706 O  O     . ASP B 2 260 ? 84.045  115.306 108.518 1.00 90.30  ? 260 ASP A O     1 
ATOM   1707 C  CB    . ASP B 2 260 ? 83.712  114.065 106.012 1.00 80.58  ? 260 ASP A CB    1 
ATOM   1708 C  CG    . ASP B 2 260 ? 82.208  114.039 106.167 1.00 86.07  ? 260 ASP A CG    1 
ATOM   1709 O  OD1   . ASP B 2 260 ? 81.603  115.127 106.274 1.00 91.04  ? 260 ASP A OD1   1 
ATOM   1710 O  OD2   . ASP B 2 260 ? 81.629  112.932 106.189 1.00 86.02  ? 260 ASP A OD2   1 
ATOM   1711 N  N     . LEU B 2 261 ? 84.218  117.363 107.612 1.00 86.05  ? 261 LEU A N     1 
ATOM   1712 C  CA    . LEU B 2 261 ? 84.352  118.030 108.904 1.00 84.11  ? 261 LEU A CA    1 
ATOM   1713 C  C     . LEU B 2 261 ? 83.255  117.643 109.887 1.00 90.42  ? 261 LEU A C     1 
ATOM   1714 O  O     . LEU B 2 261 ? 83.522  117.504 111.086 1.00 94.46  ? 261 LEU A O     1 
ATOM   1715 C  CB    . LEU B 2 261 ? 84.348  119.549 108.713 1.00 82.81  ? 261 LEU A CB    1 
ATOM   1716 C  CG    . LEU B 2 261 ? 85.632  120.234 108.232 1.00 84.15  ? 261 LEU A CG    1 
ATOM   1717 C  CD1   . LEU B 2 261 ? 85.517  121.736 108.415 1.00 91.59  ? 261 LEU A CD1   1 
ATOM   1718 C  CD2   . LEU B 2 261 ? 86.869  119.716 108.951 1.00 80.03  ? 261 LEU A CD2   1 
ATOM   1719 N  N     . GLU B 2 262 ? 82.018  117.484 109.417 1.00 92.95  ? 262 GLU A N     1 
ATOM   1720 C  CA    . GLU B 2 262 ? 80.922  117.181 110.334 1.00 100.46 ? 262 GLU A CA    1 
ATOM   1721 C  C     . GLU B 2 262 ? 81.150  115.842 111.029 1.00 99.10  ? 262 GLU A C     1 
ATOM   1722 O  O     . GLU B 2 262 ? 81.035  115.731 112.259 1.00 98.97  ? 262 GLU A O     1 
ATOM   1723 C  CB    . GLU B 2 262 ? 79.597  117.192 109.568 1.00 104.34 ? 262 GLU A CB    1 
ATOM   1724 C  CG    . GLU B 2 262 ? 78.386  116.735 110.368 1.00 110.22 ? 262 GLU A CG    1 
ATOM   1725 C  CD    . GLU B 2 262 ? 77.876  117.799 111.320 1.00 113.01 ? 262 GLU A CD    1 
ATOM   1726 O  OE1   . GLU B 2 262 ? 78.273  118.974 111.174 1.00 106.28 ? 262 GLU A OE1   1 
ATOM   1727 O  OE2   . GLU B 2 262 ? 77.085  117.458 112.224 1.00 119.21 ? 262 GLU A OE2   1 
ATOM   1728 N  N     . ASN B 2 263 ? 81.483  114.809 110.254 1.00 95.50  ? 263 ASN A N     1 
ATOM   1729 C  CA    . ASN B 2 263 ? 81.781  113.514 110.853 1.00 98.53  ? 263 ASN A CA    1 
ATOM   1730 C  C     . ASN B 2 263 ? 82.998  113.607 111.763 1.00 95.62  ? 263 ASN A C     1 
ATOM   1731 O  O     . ASN B 2 263 ? 83.022  113.006 112.843 1.00 96.17  ? 263 ASN A O     1 
ATOM   1732 C  CB    . ASN B 2 263 ? 82.004  112.469 109.759 1.00 98.59  ? 263 ASN A CB    1 
ATOM   1733 C  CG    . ASN B 2 263 ? 80.708  111.847 109.274 1.00 103.66 ? 263 ASN A CG    1 
ATOM   1734 O  OD1   . ASN B 2 263 ? 79.767  111.667 110.046 1.00 106.62 ? 263 ASN A OD1   1 
ATOM   1735 N  ND2   . ASN B 2 263 ? 80.655  111.512 107.989 1.00 101.77 ? 263 ASN A ND2   1 
ATOM   1736 N  N     . LEU B 2 264 ? 84.015  114.364 111.346 1.00 91.53  ? 264 LEU A N     1 
ATOM   1737 C  CA    . LEU B 2 264 ? 85.225  114.486 112.152 1.00 87.97  ? 264 LEU A CA    1 
ATOM   1738 C  C     . LEU B 2 264 ? 84.917  115.077 113.522 1.00 91.06  ? 264 LEU A C     1 
ATOM   1739 O  O     . LEU B 2 264 ? 85.380  114.565 114.547 1.00 91.47  ? 264 LEU A O     1 
ATOM   1740 C  CB    . LEU B 2 264 ? 86.260  115.340 111.416 1.00 81.14  ? 264 LEU A CB    1 
ATOM   1741 C  CG    . LEU B 2 264 ? 87.469  115.785 112.241 1.00 75.38  ? 264 LEU A CG    1 
ATOM   1742 C  CD1   . LEU B 2 264 ? 88.239  114.590 112.759 1.00 75.96  ? 264 LEU A CD1   1 
ATOM   1743 C  CD2   . LEU B 2 264 ? 88.372  116.678 111.413 1.00 71.60  ? 264 LEU A CD2   1 
ATOM   1744 N  N     . GLN B 2 265 ? 84.125  116.150 113.567 1.00 91.98  ? 265 GLN A N     1 
ATOM   1745 C  CA    . GLN B 2 265 ? 83.857  116.792 114.851 1.00 93.23  ? 265 GLN A CA    1 
ATOM   1746 C  C     . GLN B 2 265 ? 82.916  115.949 115.703 1.00 95.24  ? 265 GLN A C     1 
ATOM   1747 O  O     . GLN B 2 265 ? 83.084  115.874 116.929 1.00 94.41  ? 265 GLN A O     1 
ATOM   1748 C  CB    . GLN B 2 265 ? 83.292  118.198 114.642 1.00 95.74  ? 265 GLN A CB    1 
ATOM   1749 C  CG    . GLN B 2 265 ? 81.983  118.253 113.875 1.00 99.74  ? 265 GLN A CG    1 
ATOM   1750 C  CD    . GLN B 2 265 ? 80.782  118.540 114.761 1.00 104.43 ? 265 GLN A CD    1 
ATOM   1751 O  OE1   . GLN B 2 265 ? 80.924  118.952 115.912 1.00 102.99 ? 265 GLN A OE1   1 
ATOM   1752 N  NE2   . GLN B 2 265 ? 79.587  118.317 114.224 1.00 107.66 ? 265 GLN A NE2   1 
ATOM   1753 N  N     . LYS B 2 266 ? 81.929  115.293 115.084 1.00 96.18  ? 266 LYS A N     1 
ATOM   1754 C  CA    . LYS B 2 266 ? 81.080  114.395 115.862 1.00 97.50  ? 266 LYS A CA    1 
ATOM   1755 C  C     . LYS B 2 266 ? 81.912  113.289 116.496 1.00 94.98  ? 266 LYS A C     1 
ATOM   1756 O  O     . LYS B 2 266 ? 81.767  112.986 117.689 1.00 96.12  ? 266 LYS A O     1 
ATOM   1757 C  CB    . LYS B 2 266 ? 79.983  113.791 114.985 1.00 98.79  ? 266 LYS A CB    1 
ATOM   1758 C  CG    . LYS B 2 266 ? 78.939  114.781 114.494 1.00 97.62  ? 266 LYS A CG    1 
ATOM   1759 C  CD    . LYS B 2 266 ? 78.056  114.253 113.346 1.00 99.74  ? 266 LYS A CD    1 
ATOM   1760 C  CE    . LYS B 2 266 ? 78.097  112.732 113.129 1.00 99.31  ? 266 LYS A CE    1 
ATOM   1761 N  NZ    . LYS B 2 266 ? 77.513  112.355 111.817 1.00 98.62  ? 266 LYS A NZ    1 
ATOM   1762 N  N     . SER B 2 267 ? 82.808  112.685 115.713 1.00 91.91  ? 267 SER A N     1 
ATOM   1763 C  CA    . SER B 2 267 ? 83.647  111.621 116.243 1.00 90.84  ? 267 SER A CA    1 
ATOM   1764 C  C     . SER B 2 267 ? 84.605  112.143 117.301 1.00 90.83  ? 267 SER A C     1 
ATOM   1765 O  O     . SER B 2 267 ? 84.902  111.431 118.263 1.00 93.38  ? 267 SER A O     1 
ATOM   1766 C  CB    . SER B 2 267 ? 84.417  110.947 115.107 1.00 89.85  ? 267 SER A CB    1 
ATOM   1767 O  OG    . SER B 2 267 ? 83.530  110.343 114.182 1.00 92.96  ? 267 SER A OG    1 
ATOM   1768 N  N     . THR B 2 268 ? 85.101  113.373 117.148 1.00 88.80  ? 268 THR A N     1 
ATOM   1769 C  CA    . THR B 2 268 ? 85.977  113.935 118.169 1.00 88.35  ? 268 THR A CA    1 
ATOM   1770 C  C     . THR B 2 268 ? 85.237  114.110 119.487 1.00 88.37  ? 268 THR A C     1 
ATOM   1771 O  O     . THR B 2 268 ? 85.775  113.793 120.553 1.00 86.17  ? 268 THR A O     1 
ATOM   1772 C  CB    . THR B 2 268 ? 86.558  115.268 117.697 1.00 88.54  ? 268 THR A CB    1 
ATOM   1773 O  OG1   . THR B 2 268 ? 87.067  115.126 116.365 1.00 83.16  ? 268 THR A OG1   1 
ATOM   1774 C  CG2   . THR B 2 268 ? 87.686  115.709 118.620 1.00 83.28  ? 268 THR A CG2   1 
ATOM   1775 N  N     . ASN B 2 269 ? 83.999  114.603 119.436 1.00 91.56  ? 269 ASN A N     1 
ATOM   1776 C  CA    . ASN B 2 269 ? 83.214  114.711 120.663 1.00 93.33  ? 269 ASN A CA    1 
ATOM   1777 C  C     . ASN B 2 269 ? 82.970  113.337 121.279 1.00 96.08  ? 269 ASN A C     1 
ATOM   1778 O  O     . ASN B 2 269 ? 83.085  113.161 122.502 1.00 97.64  ? 269 ASN A O     1 
ATOM   1779 C  CB    . ASN B 2 269 ? 81.889  115.418 120.379 1.00 93.86  ? 269 ASN A CB    1 
ATOM   1780 C  CG    . ASN B 2 269 ? 82.082  116.802 119.791 1.00 97.01  ? 269 ASN A CG    1 
ATOM   1781 O  OD1   . ASN B 2 269 ? 83.189  117.338 119.786 1.00 95.87  ? 269 ASN A OD1   1 
ATOM   1782 N  ND2   . ASN B 2 269 ? 80.999  117.390 119.293 1.00 100.30 ? 269 ASN A ND2   1 
ATOM   1783 N  N     . GLU B 2 270 ? 82.643  112.346 120.444 1.00 94.10  ? 270 GLU A N     1 
ATOM   1784 C  CA    . GLU B 2 270 ? 82.396  111.004 120.964 1.00 94.32  ? 270 GLU A CA    1 
ATOM   1785 C  C     . GLU B 2 270 ? 83.640  110.434 121.635 1.00 93.50  ? 270 GLU A C     1 
ATOM   1786 O  O     . GLU B 2 270 ? 83.564  109.873 122.736 1.00 95.00  ? 270 GLU A O     1 
ATOM   1787 C  CB    . GLU B 2 270 ? 81.928  110.085 119.837 1.00 94.65  ? 270 GLU A CB    1 
ATOM   1788 C  CG    . GLU B 2 270 ? 80.563  110.447 119.273 1.00 96.81  ? 270 GLU A CG    1 
ATOM   1789 C  CD    . GLU B 2 270 ? 80.226  109.664 118.018 1.00 103.09 ? 270 GLU A CD    1 
ATOM   1790 O  OE1   . GLU B 2 270 ? 81.075  108.868 117.568 1.00 105.96 ? 270 GLU A OE1   1 
ATOM   1791 O  OE2   . GLU B 2 270 ? 79.114  109.848 117.482 1.00 103.30 ? 270 GLU A OE2   1 
ATOM   1792 N  N     . ILE B 2 271 ? 84.798  110.572 120.986 1.00 89.58  ? 271 ILE A N     1 
ATOM   1793 C  CA    . ILE B 2 271 ? 86.034  110.052 121.555 1.00 85.19  ? 271 ILE A CA    1 
ATOM   1794 C  C     . ILE B 2 271 ? 86.402  110.812 122.819 1.00 89.33  ? 271 ILE A C     1 
ATOM   1795 O  O     . ILE B 2 271 ? 86.953  110.229 123.756 1.00 93.43  ? 271 ILE A O     1 
ATOM   1796 C  CB    . ILE B 2 271 ? 87.174  110.099 120.521 1.00 80.91  ? 271 ILE A CB    1 
ATOM   1797 C  CG1   . ILE B 2 271 ? 86.863  109.186 119.329 1.00 85.99  ? 271 ILE A CG1   1 
ATOM   1798 C  CG2   . ILE B 2 271 ? 88.488  109.701 121.167 1.00 73.57  ? 271 ILE A CG2   1 
ATOM   1799 C  CD1   . ILE B 2 271 ? 86.609  107.732 119.699 1.00 83.70  ? 271 ILE A CD1   1 
ATOM   1800 N  N     . LEU B 2 272 ? 86.122  112.115 122.874 1.00 90.01  ? 272 LEU A N     1 
ATOM   1801 C  CA    . LEU B 2 272 ? 86.360  112.863 124.105 1.00 88.63  ? 272 LEU A CA    1 
ATOM   1802 C  C     . LEU B 2 272 ? 85.534  112.295 125.249 1.00 91.69  ? 272 LEU A C     1 
ATOM   1803 O  O     . LEU B 2 272 ? 86.042  112.088 126.357 1.00 93.44  ? 272 LEU A O     1 
ATOM   1804 C  CB    . LEU B 2 272 ? 86.034  114.342 123.893 1.00 89.52  ? 272 LEU A CB    1 
ATOM   1805 C  CG    . LEU B 2 272 ? 86.087  115.222 125.145 1.00 92.32  ? 272 LEU A CG    1 
ATOM   1806 C  CD1   . LEU B 2 272 ? 87.464  115.178 125.787 1.00 89.61  ? 272 LEU A CD1   1 
ATOM   1807 C  CD2   . LEU B 2 272 ? 85.696  116.649 124.803 1.00 94.84  ? 272 LEU A CD2   1 
ATOM   1808 N  N     . ASN B 2 273 ? 84.251  112.030 124.996 1.00 93.00  ? 273 ASN A N     1 
ATOM   1809 C  CA    . ASN B 2 273 ? 83.408  111.469 126.048 1.00 98.03  ? 273 ASN A CA    1 
ATOM   1810 C  C     . ASN B 2 273 ? 83.912  110.095 126.482 1.00 99.68  ? 273 ASN A C     1 
ATOM   1811 O  O     . ASN B 2 273 ? 83.962  109.788 127.683 1.00 101.71 ? 273 ASN A O     1 
ATOM   1812 C  CB    . ASN B 2 273 ? 81.960  111.383 125.566 1.00 100.87 ? 273 ASN A CB    1 
ATOM   1813 C  CG    . ASN B 2 273 ? 80.965  111.428 126.707 1.00 107.34 ? 273 ASN A CG    1 
ATOM   1814 O  OD1   . ASN B 2 273 ? 81.311  111.157 127.857 1.00 106.69 ? 273 ASN A OD1   1 
ATOM   1815 N  ND2   . ASN B 2 273 ? 79.720  111.773 126.397 1.00 109.94 ? 273 ASN A ND2   1 
ATOM   1816 N  N     . GLU B 2 274 ? 84.288  109.254 125.516 1.00 96.67  ? 274 GLU A N     1 
ATOM   1817 C  CA    . GLU B 2 274 ? 84.768  107.917 125.853 1.00 94.82  ? 274 GLU A CA    1 
ATOM   1818 C  C     . GLU B 2 274 ? 86.060  107.986 126.658 1.00 90.69  ? 274 GLU A C     1 
ATOM   1819 O  O     . GLU B 2 274 ? 86.232  107.252 127.639 1.00 93.67  ? 274 GLU A O     1 
ATOM   1820 C  CB    . GLU B 2 274 ? 84.970  107.092 124.580 1.00 97.77  ? 274 GLU A CB    1 
ATOM   1821 C  CG    . GLU B 2 274 ? 83.691  106.795 123.802 1.00 104.10 ? 274 GLU A CG    1 
ATOM   1822 C  CD    . GLU B 2 274 ? 82.532  106.389 124.690 1.00 107.15 ? 274 GLU A CD    1 
ATOM   1823 O  OE1   . GLU B 2 274 ? 82.648  105.363 125.394 1.00 106.03 ? 274 GLU A OE1   1 
ATOM   1824 O  OE2   . GLU B 2 274 ? 81.504  107.098 124.687 1.00 110.60 ? 274 GLU A OE2   1 
ATOM   1825 N  N     . LEU B 2 275 ? 86.978  108.871 126.266 1.00 86.07  ? 275 LEU A N     1 
ATOM   1826 C  CA    . LEU B 2 275 ? 88.210  109.044 127.025 1.00 85.59  ? 275 LEU A CA    1 
ATOM   1827 C  C     . LEU B 2 275 ? 87.920  109.550 128.430 1.00 95.89  ? 275 LEU A C     1 
ATOM   1828 O  O     . LEU B 2 275 ? 88.575  109.135 129.389 1.00 99.41  ? 275 LEU A O     1 
ATOM   1829 C  CB    . LEU B 2 275 ? 89.148  110.009 126.300 1.00 84.76  ? 275 LEU A CB    1 
ATOM   1830 C  CG    . LEU B 2 275 ? 90.595  110.053 126.803 1.00 77.04  ? 275 LEU A CG    1 
ATOM   1831 C  CD1   . LEU B 2 275 ? 91.266  108.692 126.738 1.00 72.25  ? 275 LEU A CD1   1 
ATOM   1832 C  CD2   . LEU B 2 275 ? 91.397  111.083 126.028 1.00 71.94  ? 275 LEU A CD2   1 
ATOM   1833 N  N     . ASN B 2 276 ? 86.949  110.453 128.574 1.00 98.09  ? 276 ASN A N     1 
ATOM   1834 C  CA    . ASN B 2 276 ? 86.595  110.940 129.904 1.00 98.90  ? 276 ASN A CA    1 
ATOM   1835 C  C     . ASN B 2 276 ? 86.113  109.798 130.789 1.00 102.11 ? 276 ASN A C     1 
ATOM   1836 O  O     . ASN B 2 276 ? 86.560  109.648 131.935 1.00 104.07 ? 276 ASN A O     1 
ATOM   1837 C  CB    . ASN B 2 276 ? 85.521  112.023 129.794 1.00 97.96  ? 276 ASN A CB    1 
ATOM   1838 C  CG    . ASN B 2 276 ? 86.103  113.408 129.598 1.00 102.94 ? 276 ASN A CG    1 
ATOM   1839 O  OD1   . ASN B 2 276 ? 87.283  113.643 129.859 1.00 107.10 ? 276 ASN A OD1   1 
ATOM   1840 N  ND2   . ASN B 2 276 ? 85.274  114.338 129.137 1.00 100.89 ? 276 ASN A ND2   1 
ATOM   1841 N  N     . ILE B 2 277 ? 85.202  108.974 130.270 1.00 100.84 ? 277 ILE A N     1 
ATOM   1842 C  CA    . ILE B 2 277 ? 84.659  107.897 131.093 1.00 100.44 ? 277 ILE A CA    1 
ATOM   1843 C  C     . ILE B 2 277 ? 85.742  106.871 131.408 1.00 97.60  ? 277 ILE A C     1 
ATOM   1844 O  O     . ILE B 2 277 ? 85.795  106.323 132.517 1.00 99.72  ? 277 ILE A O     1 
ATOM   1845 C  CB    . ILE B 2 277 ? 83.425  107.258 130.420 1.00 100.76 ? 277 ILE A CB    1 
ATOM   1846 C  CG1   . ILE B 2 277 ? 83.807  106.386 129.218 1.00 98.05  ? 277 ILE A CG1   1 
ATOM   1847 C  CG2   . ILE B 2 277 ? 82.416  108.334 130.006 1.00 101.84 ? 277 ILE A CG2   1 
ATOM   1848 C  CD1   . ILE B 2 277 ? 82.726  105.406 128.825 1.00 98.90  ? 277 ILE A CD1   1 
ATOM   1849 N  N     . GLU B 2 278 ? 86.639  106.610 130.454 1.00 95.22  ? 278 GLU A N     1 
ATOM   1850 C  CA    . GLU B 2 278 ? 87.707  105.649 130.704 1.00 94.35  ? 278 GLU A CA    1 
ATOM   1851 C  C     . GLU B 2 278 ? 88.705  106.190 131.720 1.00 96.08  ? 278 GLU A C     1 
ATOM   1852 O  O     . GLU B 2 278 ? 89.214  105.438 132.557 1.00 101.94 ? 278 GLU A O     1 
ATOM   1853 C  CB    . GLU B 2 278 ? 88.412  105.292 129.393 1.00 94.54  ? 278 GLU A CB    1 
ATOM   1854 C  CG    . GLU B 2 278 ? 88.811  103.824 129.257 1.00 90.08  ? 278 GLU A CG    1 
ATOM   1855 C  CD    . GLU B 2 278 ? 87.679  102.863 129.583 1.00 94.20  ? 278 GLU A CD    1 
ATOM   1856 O  OE1   . GLU B 2 278 ? 86.658  102.873 128.864 1.00 94.91  ? 278 GLU A OE1   1 
ATOM   1857 O  OE2   . GLU B 2 278 ? 87.808  102.104 130.566 1.00 94.89  ? 278 GLU A OE2   1 
ATOM   1858 N  N     . LYS B 2 279 ? 88.999  107.490 131.663 1.00 94.39  ? 279 LYS A N     1 
ATOM   1859 C  CA    . LYS B 2 279 ? 89.850  108.098 132.677 1.00 97.03  ? 279 LYS A CA    1 
ATOM   1860 C  C     . LYS B 2 279 ? 89.218  107.979 134.054 1.00 103.16 ? 279 LYS A C     1 
ATOM   1861 O  O     . LYS B 2 279 ? 89.899  107.654 135.033 1.00 104.73 ? 279 LYS A O     1 
ATOM   1862 C  CB    . LYS B 2 279 ? 90.106  109.568 132.336 1.00 99.11  ? 279 LYS A CB    1 
ATOM   1863 C  CG    . LYS B 2 279 ? 91.132  109.792 131.240 1.00 96.50  ? 279 LYS A CG    1 
ATOM   1864 C  CD    . LYS B 2 279 ? 91.745  111.181 131.317 1.00 96.32  ? 279 LYS A CD    1 
ATOM   1865 C  CE    . LYS B 2 279 ? 92.751  111.298 132.447 1.00 98.07  ? 279 LYS A CE    1 
ATOM   1866 N  NZ    . LYS B 2 279 ? 93.459  112.605 132.427 1.00 100.59 ? 279 LYS A NZ    1 
ATOM   1867 N  N     . ASP B 2 280 ? 87.912  108.237 134.148 1.00 105.87 ? 280 ASP A N     1 
ATOM   1868 C  CA    . ASP B 2 280 ? 87.234  108.100 135.433 1.00 109.74 ? 280 ASP A CA    1 
ATOM   1869 C  C     . ASP B 2 280 ? 87.323  106.670 135.947 1.00 107.26 ? 280 ASP A C     1 
ATOM   1870 O  O     . ASP B 2 280 ? 87.625  106.441 137.126 1.00 106.08 ? 280 ASP A O     1 
ATOM   1871 C  CB    . ASP B 2 280 ? 85.774  108.535 135.305 1.00 113.66 ? 280 ASP A CB    1 
ATOM   1872 C  CG    . ASP B 2 280 ? 85.064  108.594 136.643 1.00 123.75 ? 280 ASP A CG    1 
ATOM   1873 O  OD1   . ASP B 2 280 ? 85.500  109.375 137.514 1.00 127.61 ? 280 ASP A OD1   1 
ATOM   1874 O  OD2   . ASP B 2 280 ? 84.069  107.860 136.825 1.00 126.59 ? 280 ASP A OD2   1 
ATOM   1875 N  N     . ASN B 2 281 ? 87.078  105.692 135.072 1.00 105.91 ? 281 ASN A N     1 
ATOM   1876 C  CA    . ASN B 2 281 ? 87.144  104.296 135.491 1.00 106.79 ? 281 ASN A CA    1 
ATOM   1877 C  C     . ASN B 2 281 ? 88.548  103.921 135.951 1.00 104.42 ? 281 ASN A C     1 
ATOM   1878 O  O     . ASN B 2 281 ? 88.715  103.252 136.977 1.00 105.62 ? 281 ASN A O     1 
ATOM   1879 C  CB    . ASN B 2 281 ? 86.694  103.385 134.348 1.00 108.12 ? 281 ASN A CB    1 
ATOM   1880 C  CG    . ASN B 2 281 ? 86.832  101.915 134.688 1.00 108.98 ? 281 ASN A CG    1 
ATOM   1881 O  OD1   . ASN B 2 281 ? 87.896  101.323 134.513 1.00 104.62 ? 281 ASN A OD1   1 
ATOM   1882 N  ND2   . ASN B 2 281 ? 85.751  101.315 135.174 1.00 110.52 ? 281 ASN A ND2   1 
ATOM   1883 N  N     . LEU B 2 282 ? 89.572  104.345 135.206 1.00 103.43 ? 282 LEU A N     1 
ATOM   1884 C  CA    . LEU B 2 282 ? 90.946  104.014 135.572 1.00 99.44  ? 282 LEU A CA    1 
ATOM   1885 C  C     . LEU B 2 282 ? 91.334  104.656 136.896 1.00 103.89 ? 282 LEU A C     1 
ATOM   1886 O  O     . LEU B 2 282 ? 91.984  104.020 137.734 1.00 106.65 ? 282 LEU A O     1 
ATOM   1887 C  CB    . LEU B 2 282 ? 91.903  104.457 134.464 1.00 97.32  ? 282 LEU A CB    1 
ATOM   1888 C  CG    . LEU B 2 282 ? 93.241  103.720 134.355 1.00 85.95  ? 282 LEU A CG    1 
ATOM   1889 C  CD1   . LEU B 2 282 ? 93.958  104.122 133.078 1.00 85.41  ? 282 LEU A CD1   1 
ATOM   1890 C  CD2   . LEU B 2 282 ? 94.127  103.991 135.560 1.00 88.18  ? 282 LEU A CD2   1 
ATOM   1891 N  N     . LYS B 2 283 ? 90.952  105.918 137.100 1.00 105.48 ? 283 LYS A N     1 
ATOM   1892 C  CA    . LYS B 2 283 ? 91.268  106.586 138.357 1.00 108.87 ? 283 LYS A CA    1 
ATOM   1893 C  C     . LYS B 2 283 ? 90.573  105.903 139.526 1.00 111.24 ? 283 LYS A C     1 
ATOM   1894 O  O     . LYS B 2 283 ? 91.177  105.704 140.586 1.00 111.82 ? 283 LYS A O     1 
ATOM   1895 C  CB    . LYS B 2 283 ? 90.865  108.062 138.278 1.00 109.12 ? 283 LYS A CB    1 
ATOM   1896 C  CG    . LYS B 2 283 ? 91.676  108.951 137.313 1.00 108.06 ? 283 LYS A CG    1 
ATOM   1897 C  CD    . LYS B 2 283 ? 93.193  108.737 137.338 1.00 108.78 ? 283 LYS A CD    1 
ATOM   1898 C  CE    . LYS B 2 283 ? 93.881  109.890 138.040 1.00 107.44 ? 283 LYS A CE    1 
ATOM   1899 N  NZ    . LYS B 2 283 ? 95.308  109.608 138.329 1.00 104.98 ? 283 LYS A NZ    1 
ATOM   1900 N  N     . LYS B 2 284 ? 89.303  105.528 139.351 1.00 111.39 ? 284 LYS A N     1 
ATOM   1901 C  CA    . LYS B 2 284 ? 88.599  104.816 140.412 1.00 111.23 ? 284 LYS A CA    1 
ATOM   1902 C  C     . LYS B 2 284 ? 89.270  103.482 140.710 1.00 108.65 ? 284 LYS A C     1 
ATOM   1903 O  O     . LYS B 2 284 ? 89.433  103.106 141.877 1.00 105.63 ? 284 LYS A O     1 
ATOM   1904 C  CB    . LYS B 2 284 ? 87.135  104.605 140.020 1.00 111.66 ? 284 LYS A CB    1 
ATOM   1905 C  CG    . LYS B 2 284 ? 86.346  103.739 140.999 1.00 112.75 ? 284 LYS A CG    1 
ATOM   1906 C  CD    . LYS B 2 284 ? 86.152  102.313 140.489 1.00 111.74 ? 284 LYS A CD    1 
ATOM   1907 C  CE    . LYS B 2 284 ? 85.185  102.255 139.318 1.00 110.01 ? 284 LYS A CE    1 
ATOM   1908 N  NZ    . LYS B 2 284 ? 84.926  100.859 138.877 1.00 103.14 ? 284 LYS A NZ    1 
ATOM   1909 N  N     . LYS B 2 285 ? 89.667  102.752 139.667 1.00 110.46 ? 285 LYS A N     1 
ATOM   1910 C  CA    . LYS B 2 285 ? 90.277  101.443 139.871 1.00 110.58 ? 285 LYS A CA    1 
ATOM   1911 C  C     . LYS B 2 285 ? 91.622  101.553 140.577 1.00 111.46 ? 285 LYS A C     1 
ATOM   1912 O  O     . LYS B 2 285 ? 91.928  100.755 141.470 1.00 114.86 ? 285 LYS A O     1 
ATOM   1913 C  CB    . LYS B 2 285 ? 90.443  100.732 138.528 1.00 108.77 ? 285 LYS A CB    1 
ATOM   1914 C  CG    . LYS B 2 285 ? 89.287  99.822  138.147 1.00 109.51 ? 285 LYS A CG    1 
ATOM   1915 C  CD    . LYS B 2 285 ? 89.167  98.641  139.099 1.00 108.92 ? 285 LYS A CD    1 
ATOM   1916 C  CE    . LYS B 2 285 ? 88.558  97.422  138.417 1.00 112.19 ? 285 LYS A CE    1 
ATOM   1917 N  NZ    . LYS B 2 285 ? 87.582  97.782  137.353 1.00 114.03 ? 285 LYS A NZ    1 
ATOM   1918 N  N     . LEU B 2 286 ? 92.443  102.531 140.190 1.00 109.86 ? 286 LEU A N     1 
ATOM   1919 C  CA    . LEU B 2 286 ? 93.781  102.636 140.759 1.00 109.42 ? 286 LEU A CA    1 
ATOM   1920 C  C     . LEU B 2 286 ? 93.767  103.123 142.200 1.00 110.81 ? 286 LEU A C     1 
ATOM   1921 O  O     . LEU B 2 286 ? 94.759  102.937 142.912 1.00 109.79 ? 286 LEU A O     1 
ATOM   1922 C  CB    . LEU B 2 286 ? 94.645  103.570 139.909 1.00 107.95 ? 286 LEU A CB    1 
ATOM   1923 C  CG    . LEU B 2 286 ? 95.714  102.916 139.029 1.00 105.13 ? 286 LEU A CG    1 
ATOM   1924 C  CD1   . LEU B 2 286 ? 96.550  103.983 138.343 1.00 104.38 ? 286 LEU A CD1   1 
ATOM   1925 C  CD2   . LEU B 2 286 ? 96.610  101.979 139.833 1.00 95.79  ? 286 LEU A CD2   1 
ATOM   1926 N  N     . LYS B 2 287 ? 92.675  103.743 142.644 1.00 111.82 ? 287 LYS A N     1 
ATOM   1927 C  CA    . LYS B 2 287 ? 92.542  104.213 144.021 1.00 114.02 ? 287 LYS A CA    1 
ATOM   1928 C  C     . LYS B 2 287 ? 93.624  105.227 144.382 1.00 116.78 ? 287 LYS A C     1 
ATOM   1929 O  O     . LYS B 2 287 ? 94.041  105.317 145.539 1.00 116.25 ? 287 LYS A O     1 
ATOM   1930 C  CB    . LYS B 2 287 ? 92.569  103.042 145.007 1.00 112.14 ? 287 LYS A CB    1 
ATOM   1931 C  CG    . LYS B 2 287 ? 91.491  101.996 144.770 1.00 110.11 ? 287 LYS A CG    1 
ATOM   1932 C  CD    . LYS B 2 287 ? 91.620  100.840 145.749 1.00 107.03 ? 287 LYS A CD    1 
ATOM   1933 C  CE    . LYS B 2 287 ? 90.535  99.797  145.533 1.00 104.58 ? 287 LYS A CE    1 
ATOM   1934 N  NZ    . LYS B 2 287 ? 90.685  99.086  144.233 1.00 106.46 ? 287 LYS A NZ    1 
ATOM   1935 N  N     . ASP B 2 288 ? 94.089  105.998 143.399 1.00 117.93 ? 288 ASP A N     1 
ATOM   1936 C  CA    . ASP B 2 288 ? 95.097  107.027 143.620 1.00 119.20 ? 288 ASP A CA    1 
ATOM   1937 C  C     . ASP B 2 288 ? 94.536  108.426 143.394 1.00 119.24 ? 288 ASP A C     1 
ATOM   1938 O  O     . ASP B 2 288 ? 94.622  109.279 144.283 1.00 119.86 ? 288 ASP A O     1 
ATOM   1939 C  CB    . ASP B 2 288 ? 96.305  106.783 142.704 1.00 119.46 ? 288 ASP A CB    1 
ATOM   1940 C  CG    . ASP B 2 288 ? 97.511  107.613 143.099 1.00 118.65 ? 288 ASP A CG    1 
ATOM   1941 O  OD1   . ASP B 2 288 ? 97.396  108.856 143.127 1.00 116.15 ? 288 ASP A OD1   1 
ATOM   1942 O  OD2   . ASP B 2 288 ? 98.576  107.022 143.376 1.00 120.66 ? 288 ASP A OD2   1 
ATOM   1943 N  N     . GLU B 2 289 ? 93.964  108.683 142.220 1.00 117.45 ? 289 GLU A N     1 
ATOM   1944 C  CA    . GLU B 2 289 ? 93.332  109.960 141.897 1.00 116.98 ? 289 GLU A CA    1 
ATOM   1945 C  C     . GLU B 2 289 ? 94.298  111.135 142.026 1.00 115.05 ? 289 GLU A C     1 
ATOM   1946 O  O     . GLU B 2 289 ? 93.867  112.290 142.115 1.00 110.71 ? 289 GLU A O     1 
ATOM   1947 C  CB    . GLU B 2 289 ? 92.091  110.195 142.768 1.00 117.47 ? 289 GLU A CB    1 
ATOM   1948 C  CG    . GLU B 2 289 ? 90.792  109.723 142.125 1.00 115.29 ? 289 GLU A CG    1 
ATOM   1949 C  CD    . GLU B 2 289 ? 90.515  108.249 142.366 1.00 117.44 ? 289 GLU A CD    1 
ATOM   1950 O  OE1   . GLU B 2 289 ? 91.336  107.587 143.035 1.00 118.60 ? 289 GLU A OE1   1 
ATOM   1951 O  OE2   . GLU B 2 289 ? 89.479  107.752 141.879 1.00 115.84 ? 289 GLU A OE2   1 
ATOM   1952 N  N     . ASN B 2 290 ? 95.607  110.865 142.033 1.00 114.29 ? 290 ASN A N     1 
ATOM   1953 C  CA    . ASN B 2 290 ? 96.598  111.930 142.136 1.00 112.71 ? 290 ASN A CA    1 
ATOM   1954 C  C     . ASN B 2 290 ? 97.815  111.673 141.250 1.00 109.31 ? 290 ASN A C     1 
ATOM   1955 O  O     . ASN B 2 290 ? 98.903  112.181 141.549 1.00 109.54 ? 290 ASN A O     1 
ATOM   1956 C  CB    . ASN B 2 290 ? 97.052  112.106 143.590 1.00 114.44 ? 290 ASN A CB    1 
ATOM   1957 C  CG    . ASN B 2 290 ? 97.407  113.542 143.917 1.00 114.52 ? 290 ASN A CG    1 
ATOM   1958 O  OD1   . ASN B 2 290 ? 98.567  113.862 144.177 1.00 114.98 ? 290 ASN A OD1   1 
ATOM   1959 N  ND2   . ASN B 2 290 ? 96.407  114.417 143.904 1.00 113.65 ? 290 ASN A ND2   1 
ATOM   1960 N  N     . ILE B 2 291 ? 97.664  110.905 140.174 1.00 108.71 ? 291 ILE A N     1 
ATOM   1961 C  CA    . ILE B 2 291 ? 98.775  110.513 139.316 1.00 105.47 ? 291 ILE A CA    1 
ATOM   1962 C  C     . ILE B 2 291 ? 98.350  110.710 137.869 1.00 102.43 ? 291 ILE A C     1 
ATOM   1963 O  O     . ILE B 2 291 ? 97.258  110.284 137.476 1.00 102.04 ? 291 ILE A O     1 
ATOM   1964 C  CB    . ILE B 2 291 ? 99.192  109.050 139.568 1.00 103.64 ? 291 ILE A CB    1 
ATOM   1965 C  CG1   . ILE B 2 291 ? 100.272 108.607 138.579 1.00 91.29  ? 291 ILE A CG1   1 
ATOM   1966 C  CG2   . ILE B 2 291 ? 97.985  108.119 139.446 1.00 103.82 ? 291 ILE A CG2   1 
ATOM   1967 C  CD1   . ILE B 2 291 ? 100.604 107.142 138.684 1.00 87.85  ? 291 ILE A CD1   1 
ATOM   1968 N  N     . ASN B 2 292 ? 99.213  111.338 137.075 1.00 101.63 ? 292 ASN A N     1 
ATOM   1969 C  CA    . ASN B 2 292 ? 98.915  111.564 135.666 1.00 99.25  ? 292 ASN A CA    1 
ATOM   1970 C  C     . ASN B 2 292 ? 99.055  110.248 134.912 1.00 95.54  ? 292 ASN A C     1 
ATOM   1971 O  O     . ASN B 2 292 ? 100.160 109.707 134.794 1.00 96.92  ? 292 ASN A O     1 
ATOM   1972 C  CB    . ASN B 2 292 ? 99.845  112.621 135.071 1.00 100.33 ? 292 ASN A CB    1 
ATOM   1973 C  CG    . ASN B 2 292 ? 101.298 112.414 135.463 1.00 102.57 ? 292 ASN A CG    1 
ATOM   1974 O  OD1   . ASN B 2 292 ? 101.604 111.620 136.354 1.00 104.84 ? 292 ASN A OD1   1 
ATOM   1975 N  ND2   . ASN B 2 292 ? 102.200 113.127 134.797 1.00 94.81  ? 292 ASN A ND2   1 
ATOM   1976 N  N     . VAL B 2 293 ? 97.937  109.740 134.390 1.00 89.30  ? 293 VAL A N     1 
ATOM   1977 C  CA    . VAL B 2 293 ? 97.946  108.452 133.704 1.00 86.61  ? 293 VAL A CA    1 
ATOM   1978 C  C     . VAL B 2 293 ? 98.783  108.464 132.435 1.00 84.14  ? 293 VAL A C     1 
ATOM   1979 O  O     . VAL B 2 293 ? 99.017  107.400 131.853 1.00 85.47  ? 293 VAL A O     1 
ATOM   1980 C  CB    . VAL B 2 293 ? 96.511  107.994 133.367 1.00 85.60  ? 293 VAL A CB    1 
ATOM   1981 C  CG1   . VAL B 2 293 ? 95.879  107.322 134.571 1.00 89.89  ? 293 VAL A CG1   1 
ATOM   1982 C  CG2   . VAL B 2 293 ? 95.661  109.159 132.894 1.00 83.84  ? 293 VAL A CG2   1 
ATOM   1983 N  N     . ASN B 2 294 ? 99.245  109.630 131.992 1.00 85.96  ? 294 ASN A N     1 
ATOM   1984 C  CA    . ASN B 2 294 ? 100.119 109.732 130.830 1.00 86.32  ? 294 ASN A CA    1 
ATOM   1985 C  C     . ASN B 2 294 ? 101.597 109.630 131.188 1.00 89.59  ? 294 ASN A C     1 
ATOM   1986 O  O     . ASN B 2 294 ? 102.446 109.788 130.304 1.00 87.55  ? 294 ASN A O     1 
ATOM   1987 C  CB    . ASN B 2 294 ? 99.867  111.049 130.090 1.00 85.44  ? 294 ASN A CB    1 
ATOM   1988 C  CG    . ASN B 2 294 ? 98.395  111.350 129.921 1.00 83.37  ? 294 ASN A CG    1 
ATOM   1989 O  OD1   . ASN B 2 294 ? 97.578  110.441 129.796 1.00 80.73  ? 294 ASN A OD1   1 
ATOM   1990 N  ND2   . ASN B 2 294 ? 98.048  112.632 129.912 1.00 82.62  ? 294 ASN A ND2   1 
ATOM   1991 N  N     . SER B 2 295 ? 101.924 109.383 132.452 1.00 90.07  ? 295 SER A N     1 
ATOM   1992 C  CA    . SER B 2 295 ? 103.309 109.250 132.899 1.00 91.24  ? 295 SER A CA    1 
ATOM   1993 C  C     . SER B 2 295 ? 103.575 107.770 133.147 1.00 89.96  ? 295 SER A C     1 
ATOM   1994 O  O     . SER B 2 295 ? 103.164 107.221 134.172 1.00 91.25  ? 295 SER A O     1 
ATOM   1995 C  CB    . SER B 2 295 ? 103.553 110.080 134.154 1.00 93.95  ? 295 SER A CB    1 
ATOM   1996 O  OG    . SER B 2 295 ? 104.922 110.060 134.518 1.00 96.52  ? 295 SER A OG    1 
ATOM   1997 N  N     . GLN B 2 296 ? 104.275 107.126 132.210 1.00 92.75  ? 296 GLN A N     1 
ATOM   1998 C  CA    . GLN B 2 296 ? 104.503 105.689 132.326 1.00 93.19  ? 296 GLN A CA    1 
ATOM   1999 C  C     . GLN B 2 296 ? 105.315 105.362 133.574 1.00 95.01  ? 296 GLN A C     1 
ATOM   2000 O  O     . GLN B 2 296 ? 105.015 104.395 134.288 1.00 94.45  ? 296 GLN A O     1 
ATOM   2001 C  CB    . GLN B 2 296 ? 105.201 105.163 131.072 1.00 91.94  ? 296 GLN A CB    1 
ATOM   2002 C  CG    . GLN B 2 296 ? 106.596 105.716 130.839 1.00 95.33  ? 296 GLN A CG    1 
ATOM   2003 C  CD    . GLN B 2 296 ? 107.686 104.806 131.380 1.00 92.53  ? 296 GLN A CD    1 
ATOM   2004 O  OE1   . GLN B 2 296 ? 107.406 103.747 131.941 1.00 89.54  ? 296 GLN A OE1   1 
ATOM   2005 N  NE2   . GLN B 2 296 ? 108.938 105.205 131.190 1.00 91.78  ? 296 GLN A NE2   1 
ATOM   2006 N  N     . GLN B 2 297 ? 106.329 106.181 133.870 1.00 95.28  ? 297 GLN A N     1 
ATOM   2007 C  CA    . GLN B 2 297 ? 107.223 105.910 134.992 1.00 95.53  ? 297 GLN A CA    1 
ATOM   2008 C  C     . GLN B 2 297 ? 106.483 105.822 136.317 1.00 92.85  ? 297 GLN A C     1 
ATOM   2009 O  O     . GLN B 2 297 ? 106.970 105.163 137.242 1.00 92.99  ? 297 GLN A O     1 
ATOM   2010 C  CB    . GLN B 2 297 ? 108.305 106.990 135.091 1.00 94.45  ? 297 GLN A CB    1 
ATOM   2011 C  CG    . GLN B 2 297 ? 108.994 107.322 133.777 1.00 92.91  ? 297 GLN A CG    1 
ATOM   2012 C  CD    . GLN B 2 297 ? 108.296 108.417 132.993 1.00 94.90  ? 297 GLN A CD    1 
ATOM   2013 O  OE1   . GLN B 2 297 ? 107.333 109.018 133.467 1.00 96.29  ? 297 GLN A OE1   1 
ATOM   2014 N  NE2   . GLN B 2 297 ? 108.774 108.675 131.782 1.00 97.36  ? 297 GLN A NE2   1 
ATOM   2015 N  N     . GLN B 2 298 ? 105.326 106.467 136.436 1.00 89.43  ? 298 GLN A N     1 
ATOM   2016 C  CA    . GLN B 2 298 ? 104.555 106.424 137.669 1.00 89.51  ? 298 GLN A CA    1 
ATOM   2017 C  C     . GLN B 2 298 ? 103.399 105.439 137.618 1.00 90.13  ? 298 GLN A C     1 
ATOM   2018 O  O     . GLN B 2 298 ? 103.086 104.818 138.640 1.00 97.10  ? 298 GLN A O     1 
ATOM   2019 C  CB    . GLN B 2 298 ? 104.016 107.819 138.005 1.00 89.32  ? 298 GLN A CB    1 
ATOM   2020 C  CG    . GLN B 2 298 ? 105.080 108.907 138.023 1.00 91.84  ? 298 GLN A CG    1 
ATOM   2021 C  CD    . GLN B 2 298 ? 104.488 110.297 138.090 1.00 94.40  ? 298 GLN A CD    1 
ATOM   2022 O  OE1   . GLN B 2 298 ? 103.281 110.460 138.268 1.00 90.77  ? 298 GLN A OE1   1 
ATOM   2023 N  NE2   . GLN B 2 298 ? 105.335 111.309 137.952 1.00 98.03  ? 298 GLN A NE2   1 
ATOM   2024 N  N     . VAL B 2 299 ? 102.753 105.270 136.463 1.00 85.92  ? 299 VAL A N     1 
ATOM   2025 C  CA    . VAL B 2 299 ? 101.659 104.309 136.403 1.00 84.80  ? 299 VAL A CA    1 
ATOM   2026 C  C     . VAL B 2 299 ? 102.200 102.895 136.530 1.00 86.50  ? 299 VAL A C     1 
ATOM   2027 O  O     . VAL B 2 299 ? 101.513 102.010 137.051 1.00 86.64  ? 299 VAL A O     1 
ATOM   2028 C  CB    . VAL B 2 299 ? 100.825 104.471 135.118 1.00 86.34  ? 299 VAL A CB    1 
ATOM   2029 C  CG1   . VAL B 2 299 ? 101.702 104.380 133.897 1.00 89.46  ? 299 VAL A CG1   1 
ATOM   2030 C  CG2   . VAL B 2 299 ? 99.707  103.429 135.068 1.00 77.24  ? 299 VAL A CG2   1 
ATOM   2031 N  N     . LEU B 2 300 ? 103.424 102.643 136.056 1.00 88.58  ? 300 LEU A N     1 
ATOM   2032 C  CA    . LEU B 2 300 ? 104.010 101.322 136.264 1.00 89.57  ? 300 LEU A CA    1 
ATOM   2033 C  C     . LEU B 2 300 ? 104.205 101.041 137.750 1.00 93.81  ? 300 LEU A C     1 
ATOM   2034 O  O     . LEU B 2 300 ? 103.951 99.924  138.216 1.00 95.52  ? 300 LEU A O     1 
ATOM   2035 C  CB    . LEU B 2 300 ? 105.333 101.193 135.507 1.00 87.95  ? 300 LEU A CB    1 
ATOM   2036 C  CG    . LEU B 2 300 ? 106.594 101.830 136.096 1.00 90.58  ? 300 LEU A CG    1 
ATOM   2037 C  CD1   . LEU B 2 300 ? 107.375 100.825 136.922 1.00 90.02  ? 300 LEU A CD1   1 
ATOM   2038 C  CD2   . LEU B 2 300 ? 107.468 102.375 134.983 1.00 90.35  ? 300 LEU A CD2   1 
ATOM   2039 N  N     . LYS B 2 301 ? 104.655 102.043 138.510 1.00 92.52  ? 301 LYS A N     1 
ATOM   2040 C  CA    . LYS B 2 301 ? 104.759 101.883 139.957 1.00 88.49  ? 301 LYS A CA    1 
ATOM   2041 C  C     . LYS B 2 301 ? 103.388 101.677 140.584 1.00 87.30  ? 301 LYS A C     1 
ATOM   2042 O  O     . LYS B 2 301 ? 103.230 100.849 141.487 1.00 91.57  ? 301 LYS A O     1 
ATOM   2043 C  CB    . LYS B 2 301 ? 105.447 103.103 140.573 1.00 87.72  ? 301 LYS A CB    1 
ATOM   2044 C  CG    . LYS B 2 301 ? 106.868 103.364 140.086 1.00 91.07  ? 301 LYS A CG    1 
ATOM   2045 C  CD    . LYS B 2 301 ? 107.785 102.165 140.297 1.00 93.48  ? 301 LYS A CD    1 
ATOM   2046 C  CE    . LYS B 2 301 ? 108.014 101.900 141.776 1.00 100.98 ? 301 LYS A CE    1 
ATOM   2047 N  NZ    . LYS B 2 301 ? 109.126 100.944 142.015 1.00 106.13 ? 301 LYS A NZ    1 
ATOM   2048 N  N     . ALA B 2 302 ? 102.385 102.420 140.117 1.00 84.90  ? 302 ALA A N     1 
ATOM   2049 C  CA    . ALA B 2 302 ? 101.038 102.243 140.647 1.00 86.96  ? 302 ALA A CA    1 
ATOM   2050 C  C     . ALA B 2 302 ? 100.547 100.822 140.408 1.00 89.85  ? 302 ALA A C     1 
ATOM   2051 O  O     . ALA B 2 302 ? 99.890  100.227 141.269 1.00 91.97  ? 302 ALA A O     1 
ATOM   2052 C  CB    . ALA B 2 302 ? 100.084 103.253 140.012 1.00 89.88  ? 302 ALA A CB    1 
ATOM   2053 N  N     . LEU B 2 303 ? 100.852 100.266 139.235 1.00 91.28  ? 303 LEU A N     1 
ATOM   2054 C  CA    . LEU B 2 303 ? 100.506 98.878  138.956 1.00 93.65  ? 303 LEU A CA    1 
ATOM   2055 C  C     . LEU B 2 303 ? 101.259 97.933  139.879 1.00 95.34  ? 303 LEU A C     1 
ATOM   2056 O  O     . LEU B 2 303 ? 100.692 96.954  140.377 1.00 99.35  ? 303 LEU A O     1 
ATOM   2057 C  CB    . LEU B 2 303 ? 100.808 98.550  137.494 1.00 91.28  ? 303 LEU A CB    1 
ATOM   2058 C  CG    . LEU B 2 303 ? 99.706  98.854  136.478 1.00 85.20  ? 303 LEU A CG    1 
ATOM   2059 C  CD1   . LEU B 2 303 ? 100.239 98.680  135.071 1.00 83.47  ? 303 LEU A CD1   1 
ATOM   2060 C  CD2   . LEU B 2 303 ? 98.488  97.968  136.695 1.00 82.34  ? 303 LEU A CD2   1 
ATOM   2061 N  N     . GLN B 2 304 ? 102.543 98.209  140.117 1.00 94.45  ? 304 GLN A N     1 
ATOM   2062 C  CA    . GLN B 2 304 ? 103.332 97.349  140.991 1.00 96.19  ? 304 GLN A CA    1 
ATOM   2063 C  C     . GLN B 2 304 ? 102.763 97.334  142.403 1.00 97.79  ? 304 GLN A C     1 
ATOM   2064 O  O     . GLN B 2 304 ? 102.663 96.272  143.029 1.00 98.09  ? 304 GLN A O     1 
ATOM   2065 C  CB    . GLN B 2 304 ? 104.791 97.810  141.004 1.00 94.14  ? 304 GLN A CB    1 
ATOM   2066 C  CG    . GLN B 2 304 ? 105.567 97.446  139.747 1.00 88.22  ? 304 GLN A CG    1 
ATOM   2067 C  CD    . GLN B 2 304 ? 106.991 97.964  139.770 1.00 91.29  ? 304 GLN A CD    1 
ATOM   2068 O  OE1   . GLN B 2 304 ? 107.317 98.882  140.521 1.00 94.12  ? 304 GLN A OE1   1 
ATOM   2069 N  NE2   . GLN B 2 304 ? 107.848 97.378  138.944 1.00 91.83  ? 304 GLN A NE2   1 
ATOM   2070 N  N     . LYS B 2 305 ? 102.379 98.496  142.919 1.00 95.80  ? 305 LYS A N     1 
ATOM   2071 C  CA    . LYS B 2 305 ? 101.773 98.573  144.247 1.00 96.83  ? 305 LYS A CA    1 
ATOM   2072 C  C     . LYS B 2 305 ? 100.262 98.373  144.172 1.00 98.97  ? 305 LYS A C     1 
ATOM   2073 O  O     . LYS B 2 305 ? 99.479  99.126  144.749 1.00 100.50 ? 305 LYS A O     1 
ATOM   2074 C  CB    . LYS B 2 305 ? 102.117 99.909  144.896 1.00 95.60  ? 305 LYS A CB    1 
ATOM   2075 C  CG    . LYS B 2 305 ? 103.587 100.304 144.797 1.00 95.99  ? 305 LYS A CG    1 
ATOM   2076 C  CD    . LYS B 2 305 ? 104.499 99.304  145.488 1.00 99.88  ? 305 LYS A CD    1 
ATOM   2077 C  CE    . LYS B 2 305 ? 105.950 99.527  145.104 1.00 100.00 ? 305 LYS A CE    1 
ATOM   2078 N  NZ    . LYS B 2 305 ? 106.231 99.084  143.710 1.00 94.97  ? 305 LYS A NZ    1 
ATOM   2079 N  N     . ASN B 2 306 ? 99.850  97.336  143.444 1.00 98.97  ? 306 ASN A N     1 
ATOM   2080 C  CA    . ASN B 2 306 ? 98.459  96.913  143.423 1.00 102.85 ? 306 ASN A CA    1 
ATOM   2081 C  C     . ASN B 2 306 ? 98.334  95.395  143.370 1.00 106.43 ? 306 ASN A C     1 
ATOM   2082 O  O     . ASN B 2 306 ? 97.211  94.881  143.336 1.00 107.69 ? 306 ASN A O     1 
ATOM   2083 C  CB    . ASN B 2 306 ? 97.725  97.563  142.227 1.00 105.72 ? 306 ASN A CB    1 
ATOM   2084 C  CG    . ASN B 2 306 ? 96.374  96.928  141.942 1.00 110.74 ? 306 ASN A CG    1 
ATOM   2085 O  OD1   . ASN B 2 306 ? 96.262  96.021  141.118 1.00 109.99 ? 306 ASN A OD1   1 
ATOM   2086 N  ND2   . ASN B 2 306 ? 95.340  97.403  142.627 1.00 109.35 ? 306 ASN A ND2   1 
ATOM   2087 N  N     . ASN B 2 307 ? 99.446  94.661  143.418 1.00 106.44 ? 307 ASN A N     1 
ATOM   2088 C  CA    . ASN B 2 307 ? 99.450  93.207  143.287 1.00 110.36 ? 307 ASN A CA    1 
ATOM   2089 C  C     . ASN B 2 307 ? 98.977  92.784  141.895 1.00 110.95 ? 307 ASN A C     1 
ATOM   2090 O  O     . ASN B 2 307 ? 97.982  92.074  141.730 1.00 111.91 ? 307 ASN A O     1 
ATOM   2091 C  CB    . ASN B 2 307 ? 98.594  92.558  144.381 1.00 112.37 ? 307 ASN A CB    1 
ATOM   2092 C  CG    . ASN B 2 307 ? 98.882  91.080  144.542 1.00 114.44 ? 307 ASN A CG    1 
ATOM   2093 O  OD1   . ASN B 2 307 ? 98.183  90.234  143.982 1.00 113.84 ? 307 ASN A OD1   1 
ATOM   2094 N  ND2   . ASN B 2 307 ? 99.919  90.759  145.308 1.00 115.00 ? 307 ASN A ND2   1 
ATOM   2095 N  N     . VAL B 2 308 ? 99.716  93.241  140.886 1.00 109.91 ? 308 VAL A N     1 
ATOM   2096 C  CA    . VAL B 2 308 ? 99.521  92.825  139.500 1.00 107.81 ? 308 VAL A CA    1 
ATOM   2097 C  C     . VAL B 2 308 ? 100.799 92.139  139.043 1.00 103.76 ? 308 VAL A C     1 
ATOM   2098 O  O     . VAL B 2 308 ? 101.873 92.755  139.039 1.00 103.33 ? 308 VAL A O     1 
ATOM   2099 C  CB    . VAL B 2 308 ? 99.181  94.008  138.580 1.00 104.62 ? 308 VAL A CB    1 
ATOM   2100 C  CG1   . VAL B 2 308 ? 99.140  93.551  137.128 1.00 98.78  ? 308 VAL A CG1   1 
ATOM   2101 C  CG2   . VAL B 2 308 ? 97.860  94.631  138.985 1.00 105.44 ? 308 VAL A CG2   1 
ATOM   2102 N  N     . ARG B 2 309 ? 100.684 90.872  138.652 1.00 100.32 ? 309 ARG A N     1 
ATOM   2103 C  CA    . ARG B 2 309 ? 101.839 90.097  138.226 1.00 101.55 ? 309 ARG A CA    1 
ATOM   2104 C  C     . ARG B 2 309 ? 101.366 88.978  137.313 1.00 102.45 ? 309 ARG A C     1 
ATOM   2105 O  O     . ARG B 2 309 ? 100.181 88.638  137.277 1.00 103.44 ? 309 ARG A O     1 
ATOM   2106 C  CB    . ARG B 2 309 ? 102.607 89.533  139.428 1.00 104.98 ? 309 ARG A CB    1 
ATOM   2107 C  CG    . ARG B 2 309 ? 102.059 88.215  139.959 1.00 110.40 ? 309 ARG A CG    1 
ATOM   2108 C  CD    . ARG B 2 309 ? 102.385 88.023  141.427 1.00 112.74 ? 309 ARG A CD    1 
ATOM   2109 N  NE    . ARG B 2 309 ? 103.811 88.183  141.696 1.00 110.99 ? 309 ARG A NE    1 
ATOM   2110 C  CZ    . ARG B 2 309 ? 104.334 89.027  142.577 1.00 112.04 ? 309 ARG A CZ    1 
ATOM   2111 N  NH1   . ARG B 2 309 ? 103.576 89.824  143.313 1.00 112.26 ? 309 ARG A NH1   1 
ATOM   2112 N  NH2   . ARG B 2 309 ? 105.654 89.069  142.729 1.00 108.89 ? 309 ARG A NH2   1 
ATOM   2113 N  N     . ASP B 2 310 ? 102.313 88.410  136.575 1.00 101.90 ? 310 ASP A N     1 
ATOM   2114 C  CA    . ASP B 2 310 ? 102.004 87.322  135.663 1.00 101.00 ? 310 ASP A CA    1 
ATOM   2115 C  C     . ASP B 2 310 ? 101.650 86.059  136.441 1.00 107.32 ? 310 ASP A C     1 
ATOM   2116 O  O     . ASP B 2 310 ? 101.989 85.902  137.618 1.00 108.77 ? 310 ASP A O     1 
ATOM   2117 C  CB    . ASP B 2 310 ? 103.191 87.047  134.739 1.00 98.52  ? 310 ASP A CB    1 
ATOM   2118 C  CG    . ASP B 2 310 ? 102.821 86.171  133.559 1.00 101.85 ? 310 ASP A CG    1 
ATOM   2119 O  OD1   . ASP B 2 310 ? 101.639 86.182  133.155 1.00 100.89 ? 310 ASP A OD1   1 
ATOM   2120 O  OD2   . ASP B 2 310 ? 103.713 85.473  133.037 1.00 105.75 ? 310 ASP A OD2   1 
ATOM   2121 N  N     . ILE B 2 311 ? 100.950 85.146  135.763 1.00 109.48 ? 311 ILE A N     1 
ATOM   2122 C  CA    . ILE B 2 311 ? 100.611 83.866  136.372 1.00 111.64 ? 311 ILE A CA    1 
ATOM   2123 C  C     . ILE B 2 311 ? 101.861 83.068  136.706 1.00 109.48 ? 311 ILE A C     1 
ATOM   2124 O  O     . ILE B 2 311 ? 101.807 82.149  137.530 1.00 109.01 ? 311 ILE A O     1 
ATOM   2125 C  CB    . ILE B 2 311 ? 99.675  83.063  135.445 1.00 110.71 ? 311 ILE A CB    1 
ATOM   2126 C  CG1   . ILE B 2 311 ? 100.389 82.698  134.141 1.00 108.05 ? 311 ILE A CG1   1 
ATOM   2127 C  CG2   . ILE B 2 311 ? 98.416  83.862  135.149 1.00 111.83 ? 311 ILE A CG2   1 
ATOM   2128 C  CD1   . ILE B 2 311 ? 99.484  82.053  133.118 1.00 106.28 ? 311 ILE A CD1   1 
ATOM   2129 N  N     . SER B 2 312 ? 102.995 83.398  136.084 1.00 109.78 ? 312 SER A N     1 
ATOM   2130 C  CA    . SER B 2 312 ? 104.271 82.754  136.367 1.00 108.59 ? 312 SER A CA    1 
ATOM   2131 C  C     . SER B 2 312 ? 105.057 83.475  137.453 1.00 108.39 ? 312 SER A C     1 
ATOM   2132 O  O     . SER B 2 312 ? 106.294 83.396  137.476 1.00 107.42 ? 312 SER A O     1 
ATOM   2133 C  CB    . SER B 2 312 ? 105.101 82.655  135.087 1.00 107.95 ? 312 SER A CB    1 
ATOM   2134 O  OG    . SER B 2 312 ? 104.334 82.114  134.024 1.00 106.46 ? 312 SER A OG    1 
ATOM   2135 N  N     . ASN B 2 313 ? 104.371 84.180  138.354 1.00 109.75 ? 313 ASN A N     1 
ATOM   2136 C  CA    . ASN B 2 313 ? 105.019 84.884  139.459 1.00 112.06 ? 313 ASN A CA    1 
ATOM   2137 C  C     . ASN B 2 313 ? 106.048 85.889  138.948 1.00 112.80 ? 313 ASN A C     1 
ATOM   2138 O  O     . ASN B 2 313 ? 107.152 86.002  139.484 1.00 114.64 ? 313 ASN A O     1 
ATOM   2139 C  CB    . ASN B 2 313 ? 105.663 83.897  140.436 1.00 113.63 ? 313 ASN A CB    1 
ATOM   2140 C  CG    . ASN B 2 313 ? 104.657 82.937  141.047 1.00 112.67 ? 313 ASN A CG    1 
ATOM   2141 O  OD1   . ASN B 2 313 ? 104.919 81.740  141.163 1.00 107.03 ? 313 ASN A OD1   1 
ATOM   2142 N  ND2   . ASN B 2 313 ? 103.499 83.458  141.441 1.00 114.86 ? 313 ASN A ND2   1 
ATOM   2143 N  N     . LYS B 2 314 ? 105.684 86.628  137.902 1.00 110.63 ? 314 LYS A N     1 
ATOM   2144 C  CA    . LYS B 2 314 ? 106.522 87.685  137.347 1.00 106.40 ? 314 LYS A CA    1 
ATOM   2145 C  C     . LYS B 2 314 ? 105.797 89.013  137.497 1.00 103.12 ? 314 LYS A C     1 
ATOM   2146 O  O     . LYS B 2 314 ? 104.660 89.159  137.035 1.00 103.18 ? 314 LYS A O     1 
ATOM   2147 C  CB    . LYS B 2 314 ? 106.856 87.414  135.877 1.00 103.76 ? 314 LYS A CB    1 
ATOM   2148 C  CG    . LYS B 2 314 ? 107.940 86.369  135.676 1.00 108.94 ? 314 LYS A CG    1 
ATOM   2149 C  CD    . LYS B 2 314 ? 109.318 86.917  136.014 1.00 110.56 ? 314 LYS A CD    1 
ATOM   2150 C  CE    . LYS B 2 314 ? 109.863 86.295  137.287 1.00 109.90 ? 314 LYS A CE    1 
ATOM   2151 N  NZ    . LYS B 2 314 ? 111.245 86.750  137.591 1.00 109.89 ? 314 LYS A NZ    1 
ATOM   2152 N  N     . LEU B 2 315 ? 106.453 89.974  138.140 1.00 100.33 ? 315 LEU A N     1 
ATOM   2153 C  CA    . LEU B 2 315 ? 105.872 91.289  138.345 1.00 94.54  ? 315 LEU A CA    1 
ATOM   2154 C  C     . LEU B 2 315 ? 105.965 92.124  137.070 1.00 96.00  ? 315 LEU A C     1 
ATOM   2155 O  O     . LEU B 2 315 ? 106.776 91.863  136.179 1.00 97.14  ? 315 LEU A O     1 
ATOM   2156 C  CB    . LEU B 2 315 ? 106.580 92.009  139.493 1.00 90.98  ? 315 LEU A CB    1 
ATOM   2157 C  CG    . LEU B 2 315 ? 105.772 92.997  140.339 1.00 92.25  ? 315 LEU A CG    1 
ATOM   2158 C  CD1   . LEU B 2 315 ? 104.487 92.380  140.873 1.00 98.68  ? 315 LEU A CD1   1 
ATOM   2159 C  CD2   . LEU B 2 315 ? 106.624 93.513  141.485 1.00 88.95  ? 315 LEU A CD2   1 
ATOM   2160 N  N     . ILE B 2 316 ? 105.111 93.145  136.995 1.00 93.63  ? 316 ILE A N     1 
ATOM   2161 C  CA    . ILE B 2 316 ? 105.108 94.038  135.842 1.00 86.90  ? 316 ILE A CA    1 
ATOM   2162 C  C     . ILE B 2 316 ? 106.404 94.834  135.813 1.00 86.17  ? 316 ILE A C     1 
ATOM   2163 O  O     . ILE B 2 316 ? 106.812 95.430  136.819 1.00 89.23  ? 316 ILE A O     1 
ATOM   2164 C  CB    . ILE B 2 316 ? 103.880 94.961  135.880 1.00 87.39  ? 316 ILE A CB    1 
ATOM   2165 C  CG1   . ILE B 2 316 ? 103.760 95.771  134.584 1.00 85.47  ? 316 ILE A CG1   1 
ATOM   2166 C  CG2   . ILE B 2 316 ? 103.937 95.888  137.083 1.00 92.28  ? 316 ILE A CG2   1 
ATOM   2167 C  CD1   . ILE B 2 316 ? 103.746 94.949  133.312 1.00 83.71  ? 316 ILE A CD1   1 
ATOM   2168 N  N     . GLU B 2 317 ? 107.063 94.839  134.657 1.00 82.88  ? 317 GLU A N     1 
ATOM   2169 C  CA    . GLU B 2 317 ? 108.301 95.583  134.457 1.00 86.62  ? 317 GLU A CA    1 
ATOM   2170 C  C     . GLU B 2 317 ? 108.156 96.666  133.402 1.00 88.23  ? 317 GLU A C     1 
ATOM   2171 O  O     . GLU B 2 317 ? 108.493 97.827  133.662 1.00 89.83  ? 317 GLU A O     1 
ATOM   2172 C  CB    . GLU B 2 317 ? 109.436 94.621  134.068 1.00 88.55  ? 317 GLU A CB    1 
ATOM   2173 C  CG    . GLU B 2 317 ? 110.826 95.148  134.380 1.00 92.43  ? 317 GLU A CG    1 
ATOM   2174 C  CD    . GLU B 2 317 ? 111.855 94.040  134.508 1.00 96.43  ? 317 GLU A CD    1 
ATOM   2175 O  OE1   . GLU B 2 317 ? 111.570 93.029  135.186 1.00 100.08 ? 317 GLU A OE1   1 
ATOM   2176 O  OE2   . GLU B 2 317 ? 112.953 94.181  133.930 1.00 96.32  ? 317 GLU A OE2   1 
ATOM   2177 N  N     . ASN B 2 318 ? 107.660 96.320  132.218 1.00 87.55  ? 318 ASN A N     1 
ATOM   2178 C  CA    . ASN B 2 318 ? 107.435 97.266  131.136 1.00 81.42  ? 318 ASN A CA    1 
ATOM   2179 C  C     . ASN B 2 318 ? 105.960 97.257  130.766 1.00 77.54  ? 318 ASN A C     1 
ATOM   2180 O  O     . ASN B 2 318 ? 105.307 96.210  130.806 1.00 77.22  ? 318 ASN A O     1 
ATOM   2181 C  CB    . ASN B 2 318 ? 108.284 96.921  129.908 1.00 82.66  ? 318 ASN A CB    1 
ATOM   2182 C  CG    . ASN B 2 318 ? 109.752 97.243  130.103 1.00 84.31  ? 318 ASN A CG    1 
ATOM   2183 O  OD1   . ASN B 2 318 ? 110.122 97.983  131.015 1.00 79.91  ? 318 ASN A OD1   1 
ATOM   2184 N  ND2   . ASN B 2 318 ? 110.600 96.687  129.243 1.00 86.77  ? 318 ASN A ND2   1 
ATOM   2185 N  N     . THR B 2 319 ? 105.438 98.426  130.410 1.00 75.36  ? 319 THR A N     1 
ATOM   2186 C  CA    . THR B 2 319 ? 104.032 98.579  130.070 1.00 76.57  ? 319 THR A CA    1 
ATOM   2187 C  C     . THR B 2 319 ? 103.770 98.473  128.572 1.00 76.47  ? 319 THR A C     1 
ATOM   2188 O  O     . THR B 2 319 ? 102.647 98.740  128.134 1.00 72.81  ? 319 THR A O     1 
ATOM   2189 C  CB    . THR B 2 319 ? 103.510 99.919  130.590 1.00 74.22  ? 319 THR A CB    1 
ATOM   2190 O  OG1   . THR B 2 319 ? 104.406 100.969 130.202 1.00 78.67  ? 319 THR A OG1   1 
ATOM   2191 C  CG2   . THR B 2 319 ? 103.385 99.886  132.104 1.00 70.58  ? 319 THR A CG2   1 
ATOM   2192 N  N     . SER B 2 320 ? 104.772 98.093  127.781 1.00 76.02  ? 320 SER A N     1 
ATOM   2193 C  CA    . SER B 2 320 ? 104.565 97.924  126.350 1.00 73.06  ? 320 SER A CA    1 
ATOM   2194 C  C     . SER B 2 320 ? 103.448 96.922  126.102 1.00 73.09  ? 320 SER A C     1 
ATOM   2195 O  O     . SER B 2 320 ? 103.340 95.908  126.795 1.00 78.73  ? 320 SER A O     1 
ATOM   2196 C  CB    . SER B 2 320 ? 105.854 97.450  125.678 1.00 74.63  ? 320 SER A CB    1 
ATOM   2197 O  OG    . SER B 2 320 ? 106.959 98.245  126.069 1.00 73.73  ? 320 SER A OG    1 
ATOM   2198 N  N     . ASP B 2 321 ? 102.611 97.210  125.101 1.00 68.18  ? 321 ASP A N     1 
ATOM   2199 C  CA    . ASP B 2 321 ? 101.438 96.376  124.863 1.00 68.04  ? 321 ASP A CA    1 
ATOM   2200 C  C     . ASP B 2 321 ? 101.817 94.918  124.647 1.00 75.26  ? 321 ASP A C     1 
ATOM   2201 O  O     . ASP B 2 321 ? 101.086 94.018  125.077 1.00 79.96  ? 321 ASP A O     1 
ATOM   2202 C  CB    . ASP B 2 321 ? 100.652 96.901  123.661 1.00 65.55  ? 321 ASP A CB    1 
ATOM   2203 C  CG    . ASP B 2 321 ? 99.191  96.499  123.699 1.00 68.26  ? 321 ASP A CG    1 
ATOM   2204 O  OD1   . ASP B 2 321 ? 98.793  95.783  124.641 1.00 72.32  ? 321 ASP A OD1   1 
ATOM   2205 O  OD2   . ASP B 2 321 ? 98.438  96.895  122.785 1.00 70.19  ? 321 ASP A OD2   1 
ATOM   2206 N  N     . SER B 2 322 ? 102.955 94.661  124.001 1.00 72.76  ? 322 SER A N     1 
ATOM   2207 C  CA    . SER B 2 322 ? 103.415 93.285  123.844 1.00 73.08  ? 322 SER A CA    1 
ATOM   2208 C  C     . SER B 2 322 ? 103.633 92.629  125.203 1.00 75.19  ? 322 SER A C     1 
ATOM   2209 O  O     . SER B 2 322 ? 103.139 91.526  125.462 1.00 74.23  ? 322 SER A O     1 
ATOM   2210 C  CB    . SER B 2 322 ? 104.703 93.258  123.023 1.00 73.39  ? 322 SER A CB    1 
ATOM   2211 O  OG    . SER B 2 322 ? 105.769 93.876  123.726 1.00 73.05  ? 322 SER A OG    1 
ATOM   2212 N  N     . ASN B 2 323 ? 104.371 93.302  126.087 1.00 76.46  ? 323 ASN A N     1 
ATOM   2213 C  CA    . ASN B 2 323 ? 104.557 92.795  127.441 1.00 72.33  ? 323 ASN A CA    1 
ATOM   2214 C  C     . ASN B 2 323 ? 103.305 92.980  128.282 1.00 70.19  ? 323 ASN A C     1 
ATOM   2215 O  O     . ASN B 2 323 ? 103.086 92.231  129.239 1.00 73.52  ? 323 ASN A O     1 
ATOM   2216 C  CB    . ASN B 2 323 ? 105.739 93.498  128.105 1.00 71.49  ? 323 ASN A CB    1 
ATOM   2217 C  CG    . ASN B 2 323 ? 106.337 92.688  129.233 1.00 76.65  ? 323 ASN A CG    1 
ATOM   2218 O  OD1   . ASN B 2 323 ? 105.649 92.343  130.193 1.00 83.41  ? 323 ASN A OD1   1 
ATOM   2219 N  ND2   . ASN B 2 323 ? 107.624 92.380  129.127 1.00 74.25  ? 323 ASN A ND2   1 
ATOM   2220 N  N     . LEU B 2 324 ? 102.477 93.967  127.945 1.00 73.69  ? 324 LEU A N     1 
ATOM   2221 C  CA    . LEU B 2 324 ? 101.288 94.240  128.742 1.00 76.02  ? 324 LEU A CA    1 
ATOM   2222 C  C     . LEU B 2 324 ? 100.224 93.168  128.552 1.00 75.85  ? 324 LEU A C     1 
ATOM   2223 O  O     . LEU B 2 324 ? 99.409  92.942  129.452 1.00 83.17  ? 324 LEU A O     1 
ATOM   2224 C  CB    . LEU B 2 324 ? 100.734 95.618  128.379 1.00 77.59  ? 324 LEU A CB    1 
ATOM   2225 C  CG    . LEU B 2 324 ? 99.833  96.321  129.392 1.00 75.60  ? 324 LEU A CG    1 
ATOM   2226 C  CD1   . LEU B 2 324 ? 100.487 96.420  130.762 1.00 76.24  ? 324 LEU A CD1   1 
ATOM   2227 C  CD2   . LEU B 2 324 ? 99.468  97.703  128.881 1.00 69.38  ? 324 LEU A CD2   1 
ATOM   2228 N  N     . LYS B 2 325 ? 100.208 92.503  127.396 1.00 71.68  ? 325 LYS A N     1 
ATOM   2229 C  CA    . LYS B 2 325 ? 99.230  91.443  127.175 1.00 76.53  ? 325 LYS A CA    1 
ATOM   2230 C  C     . LYS B 2 325 ? 99.599  90.187  127.953 1.00 80.00  ? 325 LYS A C     1 
ATOM   2231 O  O     . LYS B 2 325 ? 98.718  89.473  128.447 1.00 79.53  ? 325 LYS A O     1 
ATOM   2232 C  CB    . LYS B 2 325 ? 99.114  91.149  125.677 1.00 80.65  ? 325 LYS A CB    1 
ATOM   2233 C  CG    . LYS B 2 325 ? 98.319  89.896  125.315 1.00 87.88  ? 325 LYS A CG    1 
ATOM   2234 C  CD    . LYS B 2 325 ? 96.826  90.168  125.330 1.00 91.16  ? 325 LYS A CD    1 
ATOM   2235 C  CE    . LYS B 2 325 ? 96.035  89.002  124.758 1.00 92.09  ? 325 LYS A CE    1 
ATOM   2236 N  NZ    . LYS B 2 325 ? 96.080  88.976  123.271 1.00 87.99  ? 325 LYS A NZ    1 
ATOM   2237 N  N     . ASN B 2 326 ? 100.898 89.899  128.069 1.00 79.82  ? 326 ASN A N     1 
ATOM   2238 C  CA    . ASN B 2 326 ? 101.339 88.721  128.808 1.00 79.07  ? 326 ASN A CA    1 
ATOM   2239 C  C     . ASN B 2 326 ? 100.776 88.714  130.222 1.00 81.31  ? 326 ASN A C     1 
ATOM   2240 O  O     . ASN B 2 326 ? 100.430 87.656  130.760 1.00 86.73  ? 326 ASN A O     1 
ATOM   2241 C  CB    . ASN B 2 326 ? 102.868 88.671  128.855 1.00 78.39  ? 326 ASN A CB    1 
ATOM   2242 C  CG    . ASN B 2 326 ? 103.474 88.051  127.613 1.00 79.32  ? 326 ASN A CG    1 
ATOM   2243 O  OD1   . ASN B 2 326 ? 102.868 87.189  126.977 1.00 82.96  ? 326 ASN A OD1   1 
ATOM   2244 N  ND2   . ASN B 2 326 ? 104.684 88.479  127.265 1.00 78.39  ? 326 ASN A ND2   1 
ATOM   2245 N  N     . PHE B 2 327 ? 100.671 89.889  130.835 1.00 78.20  ? 327 PHE A N     1 
ATOM   2246 C  CA    . PHE B 2 327 ? 100.337 90.014  132.251 1.00 77.76  ? 327 PHE A CA    1 
ATOM   2247 C  C     . PHE B 2 327 ? 98.856  90.286  132.455 1.00 78.71  ? 327 PHE A C     1 
ATOM   2248 O  O     . PHE B 2 327 ? 98.457  91.007  133.372 1.00 78.99  ? 327 PHE A O     1 
ATOM   2249 C  CB    . PHE B 2 327 ? 101.195 91.106  132.884 1.00 76.38  ? 327 PHE A CB    1 
ATOM   2250 C  CG    . PHE B 2 327 ? 102.669 90.773  132.935 1.00 82.50  ? 327 PHE A CG    1 
ATOM   2251 C  CD1   . PHE B 2 327 ? 103.180 89.671  132.266 1.00 87.03  ? 327 PHE A CD1   1 
ATOM   2252 C  CD2   . PHE B 2 327 ? 103.545 91.567  133.649 1.00 85.40  ? 327 PHE A CD2   1 
ATOM   2253 C  CE1   . PHE B 2 327 ? 104.525 89.375  132.309 1.00 90.34  ? 327 PHE A CE1   1 
ATOM   2254 C  CE2   . PHE B 2 327 ? 104.891 91.268  133.693 1.00 89.49  ? 327 PHE A CE2   1 
ATOM   2255 C  CZ    . PHE B 2 327 ? 105.378 90.173  133.024 1.00 92.20  ? 327 PHE A CZ    1 
ATOM   2256 N  N     . LEU B 2 328 ? 98.024  89.709  131.593 1.00 81.47  ? 328 LEU A N     1 
ATOM   2257 C  CA    . LEU B 2 328 ? 96.578  89.862  131.663 1.00 85.13  ? 328 LEU A CA    1 
ATOM   2258 C  C     . LEU B 2 328 ? 96.081  88.984  132.817 1.00 93.43  ? 328 LEU A C     1 
ATOM   2259 O  O     . LEU B 2 328 ? 96.873  88.487  133.623 1.00 96.63  ? 328 LEU A O     1 
ATOM   2260 C  CB    . LEU B 2 328 ? 95.977  89.513  130.299 1.00 83.63  ? 328 LEU A CB    1 
ATOM   2261 C  CG    . LEU B 2 328 ? 94.476  89.392  130.009 1.00 87.75  ? 328 LEU A CG    1 
ATOM   2262 C  CD1   . LEU B 2 328 ? 93.656  90.516  130.639 1.00 88.66  ? 328 LEU A CD1   1 
ATOM   2263 C  CD2   . LEU B 2 328 ? 94.244  89.347  128.504 1.00 88.58  ? 328 LEU A CD2   1 
ATOM   2264 N  N     . ASN B 2 329 ? 94.767  88.787  132.927 1.00 95.02  ? 329 ASN A N     1 
ATOM   2265 C  CA    . ASN B 2 329 ? 94.112  88.085  134.030 1.00 96.17  ? 329 ASN A CA    1 
ATOM   2266 C  C     . ASN B 2 329 ? 94.039  88.932  135.292 1.00 97.83  ? 329 ASN A C     1 
ATOM   2267 O  O     . ASN B 2 329 ? 93.588  88.443  136.335 1.00 97.17  ? 329 ASN A O     1 
ATOM   2268 C  CB    . ASN B 2 329 ? 94.795  86.751  134.357 1.00 93.87  ? 329 ASN A CB    1 
ATOM   2269 C  CG    . ASN B 2 329 ? 95.129  85.948  133.117 1.00 95.24  ? 329 ASN A CG    1 
ATOM   2270 O  OD1   . ASN B 2 329 ? 94.254  85.642  132.308 1.00 94.87  ? 329 ASN A OD1   1 
ATOM   2271 N  ND2   . ASN B 2 329 ? 96.400  85.601  132.961 1.00 95.78  ? 329 ASN A ND2   1 
ATOM   2272 N  N     . HIS B 2 330 ? 94.474  90.186  135.228 1.00 99.86  ? 330 HIS A N     1 
ATOM   2273 C  CA    . HIS B 2 330 ? 94.294  91.152  136.303 1.00 102.97 ? 330 HIS A CA    1 
ATOM   2274 C  C     . HIS B 2 330 ? 93.347  92.237  135.815 1.00 101.29 ? 330 HIS A C     1 
ATOM   2275 O  O     . HIS B 2 330 ? 93.502  92.739  134.697 1.00 99.34  ? 330 HIS A O     1 
ATOM   2276 C  CB    . HIS B 2 330 ? 95.632  91.762  136.727 1.00 101.57 ? 330 HIS A CB    1 
ATOM   2277 C  CG    . HIS B 2 330 ? 96.304  91.029  137.845 1.00 105.60 ? 330 HIS A CG    1 
ATOM   2278 N  ND1   . HIS B 2 330 ? 97.159  89.969  137.634 1.00 103.54 ? 330 HIS A ND1   1 
ATOM   2279 C  CD2   . HIS B 2 330 ? 96.246  91.205  139.186 1.00 109.16 ? 330 HIS A CD2   1 
ATOM   2280 C  CE1   . HIS B 2 330 ? 97.597  89.522  138.797 1.00 105.14 ? 330 HIS A CE1   1 
ATOM   2281 N  NE2   . HIS B 2 330 ? 97.061  90.256  139.755 1.00 109.04 ? 330 HIS A NE2   1 
ATOM   2282 N  N     . GLU B 2 331 ? 92.372  92.604  136.646 1.00 101.98 ? 331 GLU A N     1 
ATOM   2283 C  CA    . GLU B 2 331 ? 91.373  93.573  136.213 1.00 101.96 ? 331 GLU A CA    1 
ATOM   2284 C  C     . GLU B 2 331 ? 91.902  94.994  136.370 1.00 97.74  ? 331 GLU A C     1 
ATOM   2285 O  O     . GLU B 2 331 ? 91.210  95.871  136.897 1.00 99.97  ? 331 GLU A O     1 
ATOM   2286 C  CB    . GLU B 2 331 ? 90.079  93.388  137.010 1.00 105.05 ? 331 GLU A CB    1 
ATOM   2287 C  CG    . GLU B 2 331 ? 89.177  92.282  136.480 1.00 105.10 ? 331 GLU A CG    1 
ATOM   2288 C  CD    . GLU B 2 331 ? 88.411  92.695  135.239 1.00 110.80 ? 331 GLU A CD    1 
ATOM   2289 O  OE1   . GLU B 2 331 ? 88.087  93.893  135.104 1.00 113.40 ? 331 GLU A OE1   1 
ATOM   2290 O  OE2   . GLU B 2 331 ? 88.129  91.818  134.395 1.00 114.20 ? 331 GLU A OE2   1 
ATOM   2291 N  N     . GLU B 2 332 ? 93.130  95.227  135.906 1.00 93.56  ? 332 GLU A N     1 
ATOM   2292 C  CA    . GLU B 2 332 ? 93.678  96.573  135.771 1.00 90.21  ? 332 GLU A CA    1 
ATOM   2293 C  C     . GLU B 2 332 ? 94.405  96.796  134.457 1.00 85.67  ? 332 GLU A C     1 
ATOM   2294 O  O     . GLU B 2 332 ? 94.499  97.946  134.017 1.00 82.69  ? 332 GLU A O     1 
ATOM   2295 C  CB    . GLU B 2 332 ? 94.643  96.878  136.924 1.00 92.78  ? 332 GLU A CB    1 
ATOM   2296 C  CG    . GLU B 2 332 ? 94.976  98.352  137.081 1.00 96.35  ? 332 GLU A CG    1 
ATOM   2297 C  CD    . GLU B 2 332 ? 93.978  99.075  137.958 1.00 101.81 ? 332 GLU A CD    1 
ATOM   2298 O  OE1   . GLU B 2 332 ? 92.804  98.654  137.982 1.00 101.18 ? 332 GLU A OE1   1 
ATOM   2299 O  OE2   . GLU B 2 332 ? 94.364  100.063 138.618 1.00 99.59  ? 332 GLU A OE2   1 
ATOM   2300 N  N     . ILE B 2 333 ? 94.913  95.748  133.808 1.00 88.18  ? 333 ILE A N     1 
ATOM   2301 C  CA    . ILE B 2 333 ? 95.624  95.922  132.547 1.00 84.38  ? 333 ILE A CA    1 
ATOM   2302 C  C     . ILE B 2 333 ? 94.652  96.253  131.425 1.00 84.82  ? 333 ILE A C     1 
ATOM   2303 O  O     . ILE B 2 333 ? 94.978  97.016  130.508 1.00 85.08  ? 333 ILE A O     1 
ATOM   2304 C  CB    . ILE B 2 333 ? 96.447  94.664  132.223 1.00 83.22  ? 333 ILE A CB    1 
ATOM   2305 C  CG1   . ILE B 2 333 ? 97.545  94.440  133.271 1.00 84.94  ? 333 ILE A CG1   1 
ATOM   2306 C  CG2   . ILE B 2 333 ? 97.042  94.787  130.839 1.00 76.26  ? 333 ILE A CG2   1 
ATOM   2307 C  CD1   . ILE B 2 333 ? 98.337  95.679  133.631 1.00 75.04  ? 333 ILE A CD1   1 
ATOM   2308 N  N     . ILE B 2 334 ? 93.452  95.672  131.463 1.00 86.08  ? 334 ILE A N     1 
ATOM   2309 C  CA    . ILE B 2 334 ? 92.453  95.985  130.447 1.00 84.43  ? 334 ILE A CA    1 
ATOM   2310 C  C     . ILE B 2 334 ? 92.167  97.479  130.441 1.00 81.89  ? 334 ILE A C     1 
ATOM   2311 O  O     . ILE B 2 334 ? 92.098  98.112  129.379 1.00 82.63  ? 334 ILE A O     1 
ATOM   2312 C  CB    . ILE B 2 334 ? 91.171  95.165  130.686 1.00 83.71  ? 334 ILE A CB    1 
ATOM   2313 C  CG1   . ILE B 2 334 ? 91.470  93.666  130.588 1.00 86.29  ? 334 ILE A CG1   1 
ATOM   2314 C  CG2   . ILE B 2 334 ? 90.090  95.573  129.695 1.00 83.77  ? 334 ILE A CG2   1 
ATOM   2315 C  CD1   . ILE B 2 334 ? 91.435  92.955  131.916 1.00 87.68  ? 334 ILE A CD1   1 
ATOM   2316 N  N     . SER B 2 335 ? 92.008  98.068  131.628 1.00 79.73  ? 335 SER A N     1 
ATOM   2317 C  CA    . SER B 2 335 ? 91.735  99.497  131.708 1.00 78.93  ? 335 SER A CA    1 
ATOM   2318 C  C     . SER B 2 335 ? 92.888  100.309 131.136 1.00 74.99  ? 335 SER A C     1 
ATOM   2319 O  O     . SER B 2 335 ? 92.668  101.267 130.389 1.00 76.32  ? 335 SER A O     1 
ATOM   2320 C  CB    . SER B 2 335 ? 91.464  99.896  133.158 1.00 84.94  ? 335 SER A CB    1 
ATOM   2321 O  OG    . SER B 2 335 ? 92.237  99.115  134.052 1.00 90.73  ? 335 SER A OG    1 
ATOM   2322 N  N     . LEU B 2 336 ? 94.127  99.941  131.470 1.00 70.92  ? 336 LEU A N     1 
ATOM   2323 C  CA    . LEU B 2 336 ? 95.273  100.687 130.961 1.00 68.99  ? 336 LEU A CA    1 
ATOM   2324 C  C     . LEU B 2 336 ? 95.344  100.611 129.441 1.00 75.33  ? 336 LEU A C     1 
ATOM   2325 O  O     . LEU B 2 336 ? 95.545  101.626 128.766 1.00 78.70  ? 336 LEU A O     1 
ATOM   2326 C  CB    . LEU B 2 336 ? 96.566  100.162 131.587 1.00 60.46  ? 336 LEU A CB    1 
ATOM   2327 C  CG    . LEU B 2 336 ? 97.870  100.731 131.014 1.00 56.28  ? 336 LEU A CG    1 
ATOM   2328 C  CD1   . LEU B 2 336 ? 97.927  102.248 131.109 1.00 61.87  ? 336 LEU A CD1   1 
ATOM   2329 C  CD2   . LEU B 2 336 ? 99.068  100.124 131.716 1.00 59.27  ? 336 LEU A CD2   1 
ATOM   2330 N  N     . ARG B 2 337 ? 95.170  99.413  128.881 1.00 74.82  ? 337 ARG A N     1 
ATOM   2331 C  CA    . ARG B 2 337 ? 95.235  99.263  127.430 1.00 70.94  ? 337 ARG A CA    1 
ATOM   2332 C  C     . ARG B 2 337 ? 94.137  100.067 126.748 1.00 68.22  ? 337 ARG A C     1 
ATOM   2333 O  O     . ARG B 2 337 ? 94.393  100.797 125.781 1.00 68.07  ? 337 ARG A O     1 
ATOM   2334 C  CB    . ARG B 2 337 ? 95.129  97.784  127.054 1.00 77.39  ? 337 ARG A CB    1 
ATOM   2335 C  CG    . ARG B 2 337 ? 96.306  96.938  127.514 1.00 82.08  ? 337 ARG A CG    1 
ATOM   2336 C  CD    . ARG B 2 337 ? 96.047  95.460  127.293 1.00 83.97  ? 337 ARG A CD    1 
ATOM   2337 N  NE    . ARG B 2 337 ? 95.705  95.163  125.905 1.00 92.46  ? 337 ARG A NE    1 
ATOM   2338 C  CZ    . ARG B 2 337 ? 94.621  94.508  125.507 1.00 97.79  ? 337 ARG A CZ    1 
ATOM   2339 N  NH1   . ARG B 2 337 ? 93.722  94.058  126.368 1.00 97.16  ? 337 ARG A NH1   1 
ATOM   2340 N  NH2   . ARG B 2 337 ? 94.434  94.296  124.207 1.00 97.01  ? 337 ARG A NH2   1 
ATOM   2341 N  N     . ASN B 2 338 ? 92.900  99.948  127.239 1.00 68.69  ? 338 ASN A N     1 
ATOM   2342 C  CA    . ASN B 2 338 ? 91.793  100.665 126.616 1.00 68.82  ? 338 ASN A CA    1 
ATOM   2343 C  C     . ASN B 2 338 ? 91.994  102.169 126.707 1.00 71.55  ? 338 ASN A C     1 
ATOM   2344 O  O     . ASN B 2 338 ? 91.798  102.892 125.719 1.00 75.26  ? 338 ASN A O     1 
ATOM   2345 C  CB    . ASN B 2 338 ? 90.474  100.260 127.271 1.00 72.46  ? 338 ASN A CB    1 
ATOM   2346 C  CG    . ASN B 2 338 ? 89.283  100.497 126.368 1.00 76.30  ? 338 ASN A CG    1 
ATOM   2347 O  OD1   . ASN B 2 338 ? 89.354  101.285 125.427 1.00 77.94  ? 338 ASN A OD1   1 
ATOM   2348 N  ND2   . ASN B 2 338 ? 88.183  99.808  126.643 1.00 80.94  ? 338 ASN A ND2   1 
ATOM   2349 N  N     . TYR B 2 339 ? 92.292  102.668 127.899 1.00 73.32  ? 339 TYR A N     1 
ATOM   2350 C  CA    . TYR B 2 339 ? 92.547  104.127 127.943 1.00 72.11  ? 339 TYR A CA    1 
ATOM   2351 C  C     . TYR B 2 339 ? 93.665  104.472 126.956 1.00 69.43  ? 339 TYR A C     1 
ATOM   2352 O  O     . TYR B 2 339 ? 93.409  105.312 126.086 1.00 71.33  ? 339 TYR A O     1 
ATOM   2353 C  CB    . TYR B 2 339 ? 92.827  104.617 129.362 1.00 68.90  ? 339 TYR A CB    1 
ATOM   2354 C  CG    . TYR B 2 339 ? 93.516  105.953 129.422 1.00 69.97  ? 339 TYR A CG    1 
ATOM   2355 C  CD1   . TYR B 2 339 ? 92.781  107.122 129.391 1.00 76.33  ? 339 TYR A CD1   1 
ATOM   2356 C  CD2   . TYR B 2 339 ? 94.895  106.052 129.501 1.00 69.93  ? 339 TYR A CD2   1 
ATOM   2357 C  CE1   . TYR B 2 339 ? 93.397  108.358 129.435 1.00 76.60  ? 339 TYR A CE1   1 
ATOM   2358 C  CE2   . TYR B 2 339 ? 95.528  107.281 129.551 1.00 71.13  ? 339 TYR A CE2   1 
ATOM   2359 C  CZ    . TYR B 2 339 ? 94.772  108.437 129.519 1.00 75.28  ? 339 TYR A CZ    1 
ATOM   2360 O  OH    . TYR B 2 339 ? 95.354  109.664 129.567 1.00 77.64  ? 339 TYR A OH    1 
ATOM   2361 N  N     . ARG B 2 340 ? 94.824  103.821 127.021 1.00 64.81  ? 340 ARG A N     1 
ATOM   2362 C  CA    . ARG B 2 340 ? 95.926  104.258 126.173 1.00 65.91  ? 340 ARG A CA    1 
ATOM   2363 C  C     . ARG B 2 340 ? 95.513  104.289 124.708 1.00 67.84  ? 340 ARG A C     1 
ATOM   2364 O  O     . ARG B 2 340 ? 95.855  105.231 123.981 1.00 66.48  ? 340 ARG A O     1 
ATOM   2365 C  CB    . ARG B 2 340 ? 97.139  103.350 126.376 1.00 61.92  ? 340 ARG A CB    1 
ATOM   2366 C  CG    . ARG B 2 340 ? 98.461  104.083 126.253 1.00 63.32  ? 340 ARG A CG    1 
ATOM   2367 C  CD    . ARG B 2 340 ? 99.639  103.205 126.619 1.00 62.61  ? 340 ARG A CD    1 
ATOM   2368 N  NE    . ARG B 2 340 ? 99.868  103.173 128.059 1.00 63.94  ? 340 ARG A NE    1 
ATOM   2369 C  CZ    . ARG B 2 340 ? 100.952 102.672 128.635 1.00 67.45  ? 340 ARG A CZ    1 
ATOM   2370 N  NH1   . ARG B 2 340 ? 101.942 102.164 127.922 1.00 69.30  ? 340 ARG A NH1   1 
ATOM   2371 N  NH2   . ARG B 2 340 ? 101.047 102.689 129.962 1.00 70.52  ? 340 ARG A NH2   1 
ATOM   2372 N  N     . ARG B 2 341 ? 94.770  103.277 124.257 1.00 68.95  ? 341 ARG A N     1 
ATOM   2373 C  CA    . ARG B 2 341 ? 94.304  103.273 122.874 1.00 65.61  ? 341 ARG A CA    1 
ATOM   2374 C  C     . ARG B 2 341 ? 93.409  104.474 122.603 1.00 65.31  ? 341 ARG A C     1 
ATOM   2375 O  O     . ARG B 2 341 ? 93.591  105.189 121.608 1.00 66.95  ? 341 ARG A O     1 
ATOM   2376 C  CB    . ARG B 2 341 ? 93.563  101.968 122.575 1.00 66.10  ? 341 ARG A CB    1 
ATOM   2377 C  CG    . ARG B 2 341 ? 93.094  101.835 121.134 1.00 63.04  ? 341 ARG A CG    1 
ATOM   2378 C  CD    . ARG B 2 341 ? 92.105  100.700 120.975 1.00 65.95  ? 341 ARG A CD    1 
ATOM   2379 N  NE    . ARG B 2 341 ? 90.893  100.910 121.758 1.00 71.38  ? 341 ARG A NE    1 
ATOM   2380 C  CZ    . ARG B 2 341 ? 89.874  101.671 121.379 1.00 73.85  ? 341 ARG A CZ    1 
ATOM   2381 N  NH1   . ARG B 2 341 ? 89.891  102.330 120.231 1.00 68.53  ? 341 ARG A NH1   1 
ATOM   2382 N  NH2   . ARG B 2 341 ? 88.810  101.771 122.170 1.00 77.23  ? 341 ARG A NH2   1 
ATOM   2383 N  N     . LEU B 2 342 ? 92.439  104.720 123.487 1.00 66.91  ? 342 LEU A N     1 
ATOM   2384 C  CA    . LEU B 2 342 ? 91.537  105.846 123.280 1.00 66.02  ? 342 LEU A CA    1 
ATOM   2385 C  C     . LEU B 2 342 ? 92.291  107.167 123.326 1.00 66.57  ? 342 LEU A C     1 
ATOM   2386 O  O     . LEU B 2 342 ? 92.021  108.073 122.530 1.00 70.07  ? 342 LEU A O     1 
ATOM   2387 C  CB    . LEU B 2 342 ? 90.423  105.830 124.326 1.00 68.46  ? 342 LEU A CB    1 
ATOM   2388 C  CG    . LEU B 2 342 ? 89.133  105.093 123.962 1.00 72.91  ? 342 LEU A CG    1 
ATOM   2389 C  CD1   . LEU B 2 342 ? 88.125  105.223 125.089 1.00 79.90  ? 342 LEU A CD1   1 
ATOM   2390 C  CD2   . LEU B 2 342 ? 88.529  105.607 122.662 1.00 70.09  ? 342 LEU A CD2   1 
ATOM   2391 N  N     . TYR B 2 343 ? 93.243  107.294 124.249 1.00 64.93  ? 343 TYR A N     1 
ATOM   2392 C  CA    . TYR B 2 343 ? 93.986  108.539 124.378 1.00 64.73  ? 343 TYR A CA    1 
ATOM   2393 C  C     . TYR B 2 343 ? 94.832  108.807 123.145 1.00 66.57  ? 343 TYR A C     1 
ATOM   2394 O  O     . TYR B 2 343 ? 94.938  109.955 122.702 1.00 70.99  ? 343 TYR A O     1 
ATOM   2395 C  CB    . TYR B 2 343 ? 94.864  108.509 125.625 1.00 63.81  ? 343 TYR A CB    1 
ATOM   2396 C  CG    . TYR B 2 343 ? 95.677  109.769 125.807 1.00 62.15  ? 343 TYR A CG    1 
ATOM   2397 C  CD1   . TYR B 2 343 ? 95.075  110.960 126.189 1.00 65.27  ? 343 TYR A CD1   1 
ATOM   2398 C  CD2   . TYR B 2 343 ? 97.048  109.769 125.589 1.00 60.71  ? 343 TYR A CD2   1 
ATOM   2399 C  CE1   . TYR B 2 343 ? 95.817  112.111 126.350 1.00 72.10  ? 343 TYR A CE1   1 
ATOM   2400 C  CE2   . TYR B 2 343 ? 97.796  110.915 125.749 1.00 64.10  ? 343 TYR A CE2   1 
ATOM   2401 C  CZ    . TYR B 2 343 ? 97.177  112.082 126.131 1.00 72.02  ? 343 TYR A CZ    1 
ATOM   2402 O  OH    . TYR B 2 343 ? 97.926  113.224 126.289 1.00 72.04  ? 343 TYR A OH    1 
ATOM   2403 N  N     . LYS B 2 344 ? 95.463  107.776 122.584 1.00 63.67  ? 344 LYS A N     1 
ATOM   2404 C  CA    . LYS B 2 344 ? 96.184  107.998 121.337 1.00 61.02  ? 344 LYS A CA    1 
ATOM   2405 C  C     . LYS B 2 344 ? 95.222  108.391 120.225 1.00 58.55  ? 344 LYS A C     1 
ATOM   2406 O  O     . LYS B 2 344 ? 95.409  109.428 119.580 1.00 60.49  ? 344 LYS A O     1 
ATOM   2407 C  CB    . LYS B 2 344 ? 96.983  106.758 120.944 1.00 61.60  ? 344 LYS A CB    1 
ATOM   2408 C  CG    . LYS B 2 344 ? 97.583  106.844 119.545 1.00 52.25  ? 344 LYS A CG    1 
ATOM   2409 C  CD    . LYS B 2 344 ? 98.965  106.230 119.496 1.00 50.05  ? 344 LYS A CD    1 
ATOM   2410 C  CE    . LYS B 2 344 ? 100.039 107.258 119.764 1.00 41.30  ? 344 LYS A CE    1 
ATOM   2411 N  NZ    . LYS B 2 344 ? 100.310 108.086 118.568 1.00 39.62  ? 344 LYS A NZ    1 
ATOM   2412 N  N     . LEU B 2 345 ? 94.143  107.623 120.043 1.00 59.74  ? 345 LEU A N     1 
ATOM   2413 C  CA    . LEU B 2 345 ? 93.191  107.936 118.980 1.00 58.40  ? 345 LEU A CA    1 
ATOM   2414 C  C     . LEU B 2 345 ? 92.664  109.356 119.102 1.00 62.10  ? 345 LEU A C     1 
ATOM   2415 O  O     . LEU B 2 345 ? 92.342  109.988 118.090 1.00 70.13  ? 345 LEU A O     1 
ATOM   2416 C  CB    . LEU B 2 345 ? 92.024  106.949 119.010 1.00 57.21  ? 345 LEU A CB    1 
ATOM   2417 C  CG    . LEU B 2 345 ? 91.398  106.585 117.664 1.00 53.76  ? 345 LEU A CG    1 
ATOM   2418 C  CD1   . LEU B 2 345 ? 92.392  105.868 116.773 1.00 55.97  ? 345 LEU A CD1   1 
ATOM   2419 C  CD2   . LEU B 2 345 ? 90.152  105.740 117.874 1.00 59.77  ? 345 LEU A CD2   1 
ATOM   2420 N  N     . TYR B 2 346 ? 92.566  109.873 120.325 1.00 58.23  ? 346 TYR A N     1 
ATOM   2421 C  CA    . TYR B 2 346 ? 92.083  111.234 120.526 1.00 61.71  ? 346 TYR A CA    1 
ATOM   2422 C  C     . TYR B 2 346 ? 93.191  112.252 120.280 1.00 63.64  ? 346 TYR A C     1 
ATOM   2423 O  O     . TYR B 2 346 ? 93.160  112.999 119.296 1.00 66.30  ? 346 TYR A O     1 
ATOM   2424 C  CB    . TYR B 2 346 ? 91.532  111.371 121.947 1.00 66.43  ? 346 TYR A CB    1 
ATOM   2425 C  CG    . TYR B 2 346 ? 90.889  112.704 122.243 1.00 75.04  ? 346 TYR A CG    1 
ATOM   2426 C  CD1   . TYR B 2 346 ? 89.660  113.038 121.695 1.00 79.29  ? 346 TYR A CD1   1 
ATOM   2427 C  CD2   . TYR B 2 346 ? 91.500  113.620 123.087 1.00 74.73  ? 346 TYR A CD2   1 
ATOM   2428 C  CE1   . TYR B 2 346 ? 89.066  114.251 121.966 1.00 82.29  ? 346 TYR A CE1   1 
ATOM   2429 C  CE2   . TYR B 2 346 ? 90.911  114.834 123.365 1.00 74.73  ? 346 TYR A CE2   1 
ATOM   2430 C  CZ    . TYR B 2 346 ? 89.694  115.146 122.802 1.00 82.19  ? 346 TYR A CZ    1 
ATOM   2431 O  OH    . TYR B 2 346 ? 89.104  116.360 123.077 1.00 92.73  ? 346 TYR A OH    1 
ATOM   2432 N  N     . SER B 2 347 ? 94.207  112.254 121.144 1.00 59.66  ? 347 SER A N     1 
ATOM   2433 C  CA    . SER B 2 347 ? 95.206  113.315 121.120 1.00 60.37  ? 347 SER A CA    1 
ATOM   2434 C  C     . SER B 2 347 ? 96.046  113.281 119.850 1.00 61.67  ? 347 SER A C     1 
ATOM   2435 O  O     . SER B 2 347 ? 96.273  114.324 119.227 1.00 64.22  ? 347 SER A O     1 
ATOM   2436 C  CB    . SER B 2 347 ? 96.112  113.205 122.346 1.00 61.15  ? 347 SER A CB    1 
ATOM   2437 O  OG    . SER B 2 347 ? 97.276  113.995 122.183 1.00 67.90  ? 347 SER A OG    1 
ATOM   2438 N  N     . ALA B 2 348 ? 96.523  112.102 119.447 1.00 61.88  ? 348 ALA A N     1 
ATOM   2439 C  CA    . ALA B 2 348 ? 97.541  112.038 118.406 1.00 65.15  ? 348 ALA A CA    1 
ATOM   2440 C  C     . ALA B 2 348 ? 97.031  112.629 117.099 1.00 59.60  ? 348 ALA A C     1 
ATOM   2441 O  O     . ALA B 2 348 ? 97.758  113.348 116.404 1.00 60.93  ? 348 ALA A O     1 
ATOM   2442 C  CB    . ALA B 2 348 ? 97.985  110.589 118.205 1.00 69.04  ? 348 ALA A CB    1 
ATOM   2443 N  N     . PHE B 2 349 ? 95.784  112.328 116.741 1.00 55.39  ? 349 PHE A N     1 
ATOM   2444 C  CA    . PHE B 2 349 ? 95.227  112.745 115.461 1.00 57.15  ? 349 PHE A CA    1 
ATOM   2445 C  C     . PHE B 2 349 ? 93.971  113.591 115.592 1.00 63.72  ? 349 PHE A C     1 
ATOM   2446 O  O     . PHE B 2 349 ? 93.899  114.671 114.993 1.00 67.31  ? 349 PHE A O     1 
ATOM   2447 C  CB    . PHE B 2 349 ? 94.950  111.506 114.590 1.00 51.71  ? 349 PHE A CB    1 
ATOM   2448 C  CG    . PHE B 2 349 ? 96.089  111.165 113.686 1.00 53.79  ? 349 PHE A CG    1 
ATOM   2449 C  CD1   . PHE B 2 349 ? 97.141  110.398 114.149 1.00 54.52  ? 349 PHE A CD1   1 
ATOM   2450 C  CD2   . PHE B 2 349 ? 96.129  111.636 112.387 1.00 53.00  ? 349 PHE A CD2   1 
ATOM   2451 C  CE1   . PHE B 2 349 ? 98.203  110.099 113.338 1.00 51.93  ? 349 PHE A CE1   1 
ATOM   2452 C  CE2   . PHE B 2 349 ? 97.194  111.339 111.569 1.00 53.02  ? 349 PHE A CE2   1 
ATOM   2453 C  CZ    . PHE B 2 349 ? 98.232  110.567 112.045 1.00 52.35  ? 349 PHE A CZ    1 
ATOM   2454 N  N     . TYR B 2 350 ? 92.976  113.144 116.364 1.00 60.03  ? 350 TYR A N     1 
ATOM   2455 C  CA    . TYR B 2 350 ? 91.667  113.786 116.299 1.00 59.61  ? 350 TYR A CA    1 
ATOM   2456 C  C     . TYR B 2 350 ? 91.753  115.261 116.672 1.00 59.21  ? 350 TYR A C     1 
ATOM   2457 O  O     . TYR B 2 350 ? 91.149  116.112 116.009 1.00 64.35  ? 350 TYR A O     1 
ATOM   2458 C  CB    . TYR B 2 350 ? 90.679  113.064 117.210 1.00 62.46  ? 350 TYR A CB    1 
ATOM   2459 C  CG    . TYR B 2 350 ? 89.816  112.056 116.494 1.00 64.67  ? 350 TYR A CG    1 
ATOM   2460 C  CD1   . TYR B 2 350 ? 90.372  111.103 115.652 1.00 58.55  ? 350 TYR A CD1   1 
ATOM   2461 C  CD2   . TYR B 2 350 ? 88.444  112.062 116.658 1.00 68.50  ? 350 TYR A CD2   1 
ATOM   2462 C  CE1   . TYR B 2 350 ? 89.576  110.178 114.999 1.00 63.57  ? 350 TYR A CE1   1 
ATOM   2463 C  CE2   . TYR B 2 350 ? 87.640  111.149 116.015 1.00 70.16  ? 350 TYR A CE2   1 
ATOM   2464 C  CZ    . TYR B 2 350 ? 88.208  110.205 115.186 1.00 70.02  ? 350 TYR A CZ    1 
ATOM   2465 O  OH    . TYR B 2 350 ? 87.408  109.292 114.539 1.00 71.47  ? 350 TYR A OH    1 
ATOM   2466 N  N     . LEU B 2 351 ? 92.498  115.584 117.729 1.00 60.21  ? 351 LEU A N     1 
ATOM   2467 C  CA    . LEU B 2 351 ? 92.625  116.980 118.135 1.00 62.80  ? 351 LEU A CA    1 
ATOM   2468 C  C     . LEU B 2 351 ? 93.458  117.775 117.139 1.00 66.47  ? 351 LEU A C     1 
ATOM   2469 O  O     . LEU B 2 351 ? 93.180  118.954 116.892 1.00 70.21  ? 351 LEU A O     1 
ATOM   2470 C  CB    . LEU B 2 351 ? 93.250  117.071 119.528 1.00 64.14  ? 351 LEU A CB    1 
ATOM   2471 C  CG    . LEU B 2 351 ? 92.347  116.813 120.736 1.00 68.28  ? 351 LEU A CG    1 
ATOM   2472 C  CD1   . LEU B 2 351 ? 93.136  117.004 122.020 1.00 69.46  ? 351 LEU A CD1   1 
ATOM   2473 C  CD2   . LEU B 2 351 ? 91.134  117.723 120.717 1.00 71.50  ? 351 LEU A CD2   1 
ATOM   2474 N  N     . LYS B 2 352 ? 94.480  117.153 116.558 1.00 64.93  ? 352 LYS A N     1 
ATOM   2475 C  CA    . LYS B 2 352 ? 95.455  117.860 115.739 1.00 68.33  ? 352 LYS A CA    1 
ATOM   2476 C  C     . LYS B 2 352 ? 95.102  117.870 114.258 1.00 69.57  ? 352 LYS A C     1 
ATOM   2477 O  O     . LYS B 2 352 ? 95.888  118.384 113.454 1.00 71.50  ? 352 LYS A O     1 
ATOM   2478 C  CB    . LYS B 2 352 ? 96.848  117.243 115.930 1.00 63.53  ? 352 LYS A CB    1 
ATOM   2479 C  CG    . LYS B 2 352 ? 97.597  117.754 117.154 1.00 63.04  ? 352 LYS A CG    1 
ATOM   2480 C  CD    . LYS B 2 352 ? 97.002  117.227 118.455 1.00 62.47  ? 352 LYS A CD    1 
ATOM   2481 C  CE    . LYS B 2 352 ? 97.280  118.161 119.620 1.00 67.97  ? 352 LYS A CE    1 
ATOM   2482 N  NZ    . LYS B 2 352 ? 96.511  117.783 120.836 1.00 67.98  ? 352 LYS A NZ    1 
ATOM   2483 N  N     . LEU B 2 353 ? 93.954  117.324 113.874 1.00 66.06  ? 353 LEU A N     1 
ATOM   2484 C  CA    . LEU B 2 353 ? 93.588  117.273 112.466 1.00 65.55  ? 353 LEU A CA    1 
ATOM   2485 C  C     . LEU B 2 353 ? 92.997  118.607 112.016 1.00 71.09  ? 353 LEU A C     1 
ATOM   2486 O  O     . LEU B 2 353 ? 93.423  119.149 110.988 1.00 71.66  ? 353 LEU A O     1 
ATOM   2487 C  CB    . LEU B 2 353 ? 92.606  116.129 112.211 1.00 57.25  ? 353 LEU A CB    1 
ATOM   2488 C  CG    . LEU B 2 353 ? 92.412  115.725 110.751 1.00 57.43  ? 353 LEU A CG    1 
ATOM   2489 C  CD1   . LEU B 2 353 ? 93.726  115.234 110.158 1.00 58.38  ? 353 LEU A CD1   1 
ATOM   2490 C  CD2   . LEU B 2 353 ? 91.345  114.655 110.636 1.00 54.82  ? 353 LEU A CD2   1 
ATOM   2491 N  N     . PRO B 2 354 ? 92.030  119.179 112.744 1.00 71.01  ? 354 PRO A N     1 
ATOM   2492 C  CA    . PRO B 2 354 ? 91.455  120.459 112.300 1.00 68.81  ? 354 PRO A CA    1 
ATOM   2493 C  C     . PRO B 2 354 ? 92.450  121.602 112.303 1.00 70.57  ? 354 PRO A C     1 
ATOM   2494 O  O     . PRO B 2 354 ? 92.238  122.582 111.580 1.00 73.52  ? 354 PRO A O     1 
ATOM   2495 C  CB    . PRO B 2 354 ? 90.318  120.708 113.304 1.00 68.92  ? 354 PRO A CB    1 
ATOM   2496 C  CG    . PRO B 2 354 ? 90.094  119.390 113.982 1.00 71.65  ? 354 PRO A CG    1 
ATOM   2497 C  CD    . PRO B 2 354 ? 91.437  118.749 114.020 1.00 70.62  ? 354 PRO A CD    1 
ATOM   2498 N  N     . LEU B 2 355 ? 93.526  121.513 113.087 1.00 71.84  ? 355 LEU A N     1 
ATOM   2499 C  CA    . LEU B 2 355 ? 94.517  122.582 113.129 1.00 73.00  ? 355 LEU A CA    1 
ATOM   2500 C  C     . LEU B 2 355 ? 95.417  122.604 111.903 1.00 70.73  ? 355 LEU A C     1 
ATOM   2501 O  O     . LEU B 2 355 ? 96.120  123.598 111.693 1.00 69.71  ? 355 LEU A O     1 
ATOM   2502 C  CB    . LEU B 2 355 ? 95.377  122.450 114.387 1.00 72.48  ? 355 LEU A CB    1 
ATOM   2503 C  CG    . LEU B 2 355 ? 94.831  123.094 115.666 1.00 72.12  ? 355 LEU A CG    1 
ATOM   2504 C  CD1   . LEU B 2 355 ? 95.221  124.564 115.720 1.00 69.22  ? 355 LEU A CD1   1 
ATOM   2505 C  CD2   . LEU B 2 355 ? 93.320  122.940 115.775 1.00 71.66  ? 355 LEU A CD2   1 
ATOM   2506 N  N     . HIS B 2 356 ? 95.417  121.546 111.095 1.00 69.57  ? 356 HIS A N     1 
ATOM   2507 C  CA    . HIS B 2 356 ? 96.269  121.457 109.918 1.00 69.05  ? 356 HIS A CA    1 
ATOM   2508 C  C     . HIS B 2 356 ? 95.518  121.751 108.625 1.00 70.41  ? 356 HIS A C     1 
ATOM   2509 O  O     . HIS B 2 356 ? 96.095  121.613 107.542 1.00 65.21  ? 356 HIS A O     1 
ATOM   2510 C  CB    . HIS B 2 356 ? 96.906  120.070 109.840 1.00 64.15  ? 356 HIS A CB    1 
ATOM   2511 C  CG    . HIS B 2 356 ? 98.114  119.911 110.708 1.00 63.21  ? 356 HIS A CG    1 
ATOM   2512 N  ND1   . HIS B 2 356 ? 99.255  120.665 110.543 1.00 59.81  ? 356 HIS A ND1   1 
ATOM   2513 C  CD2   . HIS B 2 356 ? 98.359  119.084 111.752 1.00 62.02  ? 356 HIS A CD2   1 
ATOM   2514 C  CE1   . HIS B 2 356 ? 100.151 120.311 111.447 1.00 60.12  ? 356 HIS A CE1   1 
ATOM   2515 N  NE2   . HIS B 2 356 ? 99.633  119.353 112.193 1.00 61.78  ? 356 HIS A NE2   1 
ATOM   2516 N  N     . ILE B 2 357 ? 94.257  122.159 108.711 1.00 73.91  ? 357 ILE A N     1 
ATOM   2517 C  CA    . ILE B 2 357 ? 93.435  122.413 107.532 1.00 73.08  ? 357 ILE A CA    1 
ATOM   2518 C  C     . ILE B 2 357 ? 93.631  123.862 107.103 1.00 74.09  ? 357 ILE A C     1 
ATOM   2519 O  O     . ILE B 2 357 ? 93.400  124.789 107.888 1.00 74.22  ? 357 ILE A O     1 
ATOM   2520 C  CB    . ILE B 2 357 ? 91.954  122.119 107.815 1.00 71.42  ? 357 ILE A CB    1 
ATOM   2521 C  CG1   . ILE B 2 357 ? 91.757  120.617 108.047 1.00 66.37  ? 357 ILE A CG1   1 
ATOM   2522 C  CG2   . ILE B 2 357 ? 91.090  122.647 106.670 1.00 72.91  ? 357 ILE A CG2   1 
ATOM   2523 C  CD1   . ILE B 2 357 ? 90.310  120.183 108.173 1.00 66.27  ? 357 ILE A CD1   1 
ATOM   2524 N  N     . ASN B 2 358 ? 94.052  124.059 105.857 1.00 75.73  ? 358 ASN A N     1 
ATOM   2525 C  CA    . ASN B 2 358 ? 94.201  125.404 105.320 1.00 80.38  ? 358 ASN A CA    1 
ATOM   2526 C  C     . ASN B 2 358 ? 92.841  126.075 105.186 1.00 83.45  ? 358 ASN A C     1 
ATOM   2527 O  O     . ASN B 2 358 ? 91.848  125.438 104.825 1.00 83.65  ? 358 ASN A O     1 
ATOM   2528 C  CB    . ASN B 2 358 ? 94.896  125.363 103.959 1.00 78.39  ? 358 ASN A CB    1 
ATOM   2529 C  CG    . ASN B 2 358 ? 96.370  125.703 104.045 1.00 76.88  ? 358 ASN A CG    1 
ATOM   2530 O  OD1   . ASN B 2 358 ? 96.968  125.666 105.119 1.00 79.80  ? 358 ASN A OD1   1 
ATOM   2531 N  ND2   . ASN B 2 358 ? 96.965  126.041 102.907 1.00 73.14  ? 358 ASN A ND2   1 
ATOM   2532 N  N     . THR B 2 359 ? 92.802  127.371 105.478 1.00 85.89  ? 359 THR A N     1 
ATOM   2533 C  CA    . THR B 2 359 ? 91.556  128.115 105.400 1.00 87.93  ? 359 THR A CA    1 
ATOM   2534 C  C     . THR B 2 359 ? 91.142  128.310 103.941 1.00 90.63  ? 359 THR A C     1 
ATOM   2535 O  O     . THR B 2 359 ? 91.900  128.035 103.010 1.00 89.69  ? 359 THR A O     1 
ATOM   2536 C  CB    . THR B 2 359 ? 91.690  129.467 106.099 1.00 91.20  ? 359 THR A CB    1 
ATOM   2537 O  OG1   . THR B 2 359 ? 90.433  130.156 106.054 1.00 92.52  ? 359 THR A OG1   1 
ATOM   2538 C  CG2   . THR B 2 359 ? 92.758  130.326 105.431 1.00 95.35  ? 359 THR A CG2   1 
ATOM   2539 N  N     . LYS B 2 360 ? 89.879  128.708 103.766 1.00 95.59  ? 360 LYS A N     1 
ATOM   2540 C  CA    . LYS B 2 360 ? 89.248  129.083 102.497 1.00 97.13  ? 360 LYS A CA    1 
ATOM   2541 C  C     . LYS B 2 360 ? 89.275  127.938 101.486 1.00 95.74  ? 360 LYS A C     1 
ATOM   2542 O  O     . LYS B 2 360 ? 88.882  128.123 100.330 1.00 94.62  ? 360 LYS A O     1 
ATOM   2543 C  CB    . LYS B 2 360 ? 89.884  130.343 101.878 1.00 98.83  ? 360 LYS A CB    1 
ATOM   2544 C  CG    . LYS B 2 360 ? 91.234  130.193 101.183 1.00 98.88  ? 360 LYS A CG    1 
ATOM   2545 C  CD    . LYS B 2 360 ? 92.083  131.444 101.339 1.00 106.23 ? 360 LYS A CD    1 
ATOM   2546 C  CE    . LYS B 2 360 ? 93.417  131.306 100.615 1.00 104.22 ? 360 LYS A CE    1 
ATOM   2547 N  NZ    . LYS B 2 360 ? 94.102  130.015 100.897 1.00 98.97  ? 360 LYS A NZ    1 
ATOM   2548 N  N     . THR B 2 361 ? 89.743  126.758 101.902 1.00 94.72  ? 361 THR A N     1 
ATOM   2549 C  CA    . THR B 2 361 ? 89.728  125.572 101.057 1.00 89.56  ? 361 THR A CA    1 
ATOM   2550 C  C     . THR B 2 361 ? 89.356  124.301 101.805 1.00 85.42  ? 361 THR A C     1 
ATOM   2551 O  O     . THR B 2 361 ? 89.125  123.276 101.154 1.00 81.08  ? 361 THR A O     1 
ATOM   2552 C  CB    . THR B 2 361 ? 91.096  125.359 100.390 1.00 88.06  ? 361 THR A CB    1 
ATOM   2553 O  OG1   . THR B 2 361 ? 92.104  125.201 101.395 1.00 86.89  ? 361 THR A OG1   1 
ATOM   2554 C  CG2   . THR B 2 361 ? 91.447  126.537 99.498  1.00 91.07  ? 361 THR A CG2   1 
ATOM   2555 N  N     . ASN B 2 362 ? 89.310  124.331 103.138 1.00 85.79  ? 362 ASN A N     1 
ATOM   2556 C  CA    . ASN B 2 362 ? 88.897  123.195 103.956 1.00 81.28  ? 362 ASN A CA    1 
ATOM   2557 C  C     . ASN B 2 362 ? 89.484  121.881 103.451 1.00 77.81  ? 362 ASN A C     1 
ATOM   2558 O  O     . ASN B 2 362 ? 88.832  120.834 103.518 1.00 75.86  ? 362 ASN A O     1 
ATOM   2559 C  CB    . ASN B 2 362 ? 87.364  123.126 104.027 1.00 84.02  ? 362 ASN A CB    1 
ATOM   2560 C  CG    . ASN B 2 362 ? 86.738  122.510 102.788 1.00 85.67  ? 362 ASN A CG    1 
ATOM   2561 O  OD1   . ASN B 2 362 ? 86.727  123.117 101.717 1.00 86.95  ? 362 ASN A OD1   1 
ATOM   2562 N  ND2   . ASN B 2 362 ? 86.210  121.300 102.929 1.00 81.55  ? 362 ASN A ND2   1 
ATOM   2563 N  N     . LYS B 2 363 ? 90.723  121.921 102.967 1.00 74.55  ? 363 LYS A N     1 
ATOM   2564 C  CA    . LYS B 2 363 ? 91.426  120.739 102.489 1.00 70.15  ? 363 LYS A CA    1 
ATOM   2565 C  C     . LYS B 2 363 ? 92.783  120.624 103.168 1.00 64.09  ? 363 LYS A C     1 
ATOM   2566 O  O     . LYS B 2 363 ? 93.516  121.610 103.283 1.00 59.94  ? 363 LYS A O     1 
ATOM   2567 C  CB    . LYS B 2 363 ? 91.612  120.780 100.966 1.00 69.81  ? 363 LYS A CB    1 
ATOM   2568 C  CG    . LYS B 2 363 ? 90.512  120.079 100.192 1.00 68.82  ? 363 LYS A CG    1 
ATOM   2569 C  CD    . LYS B 2 363 ? 90.679  120.255 98.696  1.00 68.54  ? 363 LYS A CD    1 
ATOM   2570 C  CE    . LYS B 2 363 ? 90.120  121.580 98.225  1.00 77.12  ? 363 LYS A CE    1 
ATOM   2571 N  NZ    . LYS B 2 363 ? 89.903  121.594 96.761  1.00 77.47  ? 363 LYS A NZ    1 
ATOM   2572 N  N     . ILE B 2 364 ? 93.119  119.412 103.600 1.00 65.77  ? 364 ILE A N     1 
ATOM   2573 C  CA    . ILE B 2 364 ? 94.421  119.145 104.201 1.00 60.37  ? 364 ILE A CA    1 
ATOM   2574 C  C     . ILE B 2 364 ? 95.459  119.121 103.089 1.00 56.99  ? 364 ILE A C     1 
ATOM   2575 O  O     . ILE B 2 364 ? 95.396  118.282 102.185 1.00 61.92  ? 364 ILE A O     1 
ATOM   2576 C  CB    . ILE B 2 364 ? 94.423  117.819 104.976 1.00 56.83  ? 364 ILE A CB    1 
ATOM   2577 C  CG1   . ILE B 2 364 ? 93.268  117.755 105.975 1.00 54.69  ? 364 ILE A CG1   1 
ATOM   2578 C  CG2   . ILE B 2 364 ? 95.746  117.631 105.710 1.00 49.62  ? 364 ILE A CG2   1 
ATOM   2579 C  CD1   . ILE B 2 364 ? 92.998  116.361 106.481 1.00 49.62  ? 364 ILE A CD1   1 
ATOM   2580 N  N     . HIS B 2 365 ? 96.416  120.037 103.153 1.00 51.52  ? 365 HIS A N     1 
ATOM   2581 C  CA    . HIS B 2 365 ? 97.517  120.095 102.197 1.00 50.33  ? 365 HIS A CA    1 
ATOM   2582 C  C     . HIS B 2 365 ? 98.772  119.647 102.938 1.00 44.10  ? 365 HIS A C     1 
ATOM   2583 O  O     . HIS B 2 365 ? 99.475  120.452 103.548 1.00 48.30  ? 365 HIS A O     1 
ATOM   2584 C  CB    . HIS B 2 365 ? 97.663  121.492 101.612 1.00 52.19  ? 365 HIS A CB    1 
ATOM   2585 C  CG    . HIS B 2 365 ? 96.472  121.937 100.822 1.00 57.50  ? 365 HIS A CG    1 
ATOM   2586 N  ND1   . HIS B 2 365 ? 95.643  121.053 100.165 1.00 57.16  ? 365 HIS A ND1   1 
ATOM   2587 C  CD2   . HIS B 2 365 ? 95.971  123.171 100.579 1.00 64.81  ? 365 HIS A CD2   1 
ATOM   2588 C  CE1   . HIS B 2 365 ? 94.682  121.722 99.554  1.00 61.46  ? 365 HIS A CE1   1 
ATOM   2589 N  NE2   . HIS B 2 365 ? 94.858  123.010 99.788  1.00 67.75  ? 365 HIS A NE2   1 
ATOM   2590 N  N     . THR B 2 366 ? 99.050  118.349 102.875 1.00 37.06  ? 366 THR A N     1 
ATOM   2591 C  CA    . THR B 2 366 ? 100.185 117.789 103.588 1.00 34.44  ? 366 THR A CA    1 
ATOM   2592 C  C     . THR B 2 366 ? 101.481 118.178 102.887 1.00 30.91  ? 366 THR A C     1 
ATOM   2593 O  O     . THR B 2 366 ? 101.497 118.952 101.927 1.00 38.70  ? 366 THR A O     1 
ATOM   2594 C  CB    . THR B 2 366 ? 100.083 116.267 103.686 1.00 44.16  ? 366 THR A CB    1 
ATOM   2595 O  OG1   . THR B 2 366 ? 100.690 115.672 102.534 1.00 41.17  ? 366 THR A OG1   1 
ATOM   2596 C  CG2   . THR B 2 366 ? 98.636  115.809 103.797 1.00 54.50  ? 366 THR A CG2   1 
ATOM   2597 N  N     . THR B 2 367 ? 102.585 117.630 103.379 1.00 29.98  ? 367 THR A N     1 
ATOM   2598 C  CA    . THR B 2 367 ? 103.895 117.797 102.768 1.00 30.97  ? 367 THR A CA    1 
ATOM   2599 C  C     . THR B 2 367 ? 104.455 116.414 102.485 1.00 34.27  ? 367 THR A C     1 
ATOM   2600 O  O     . THR B 2 367 ? 104.568 115.591 103.398 1.00 39.03  ? 367 THR A O     1 
ATOM   2601 C  CB    . THR B 2 367 ? 104.833 118.590 103.679 1.00 33.21  ? 367 THR A CB    1 
ATOM   2602 O  OG1   . THR B 2 367 ? 104.418 119.961 103.717 1.00 33.29  ? 367 THR A OG1   1 
ATOM   2603 C  CG2   . THR B 2 367 ? 106.266 118.507 103.179 1.00 37.97  ? 367 THR A CG2   1 
ATOM   2604 N  N     . PHE B 2 368 ? 104.797 116.158 101.228 1.00 36.62  ? 368 PHE A N     1 
ATOM   2605 C  CA    . PHE B 2 368 ? 105.305 114.862 100.801 1.00 39.91  ? 368 PHE A CA    1 
ATOM   2606 C  C     . PHE B 2 368 ? 106.803 114.959 100.559 1.00 46.03  ? 368 PHE A C     1 
ATOM   2607 O  O     . PHE B 2 368 ? 107.268 115.870 99.867  1.00 52.10  ? 368 PHE A O     1 
ATOM   2608 C  CB    . PHE B 2 368 ? 104.597 114.389 99.532  1.00 39.62  ? 368 PHE A CB    1 
ATOM   2609 C  CG    . PHE B 2 368 ? 103.448 113.468 99.793  1.00 38.33  ? 368 PHE A CG    1 
ATOM   2610 C  CD1   . PHE B 2 368 ? 103.668 112.165 100.193 1.00 44.63  ? 368 PHE A CD1   1 
ATOM   2611 C  CD2   . PHE B 2 368 ? 102.148 113.903 99.636  1.00 40.05  ? 368 PHE A CD2   1 
ATOM   2612 C  CE1   . PHE B 2 368 ? 102.613 111.316 100.434 1.00 46.82  ? 368 PHE A CE1   1 
ATOM   2613 C  CE2   . PHE B 2 368 ? 101.090 113.057 99.874  1.00 40.09  ? 368 PHE A CE2   1 
ATOM   2614 C  CZ    . PHE B 2 368 ? 101.324 111.763 100.274 1.00 42.70  ? 368 PHE A CZ    1 
ATOM   2615 N  N     . ASN B 2 369 ? 107.551 114.025 101.132 1.00 43.08  ? 369 ASN A N     1 
ATOM   2616 C  CA    . ASN B 2 369 ? 108.992 113.956 100.957 1.00 45.12  ? 369 ASN A CA    1 
ATOM   2617 C  C     . ASN B 2 369 ? 109.341 112.721 100.142 1.00 48.86  ? 369 ASN A C     1 
ATOM   2618 O  O     . ASN B 2 369 ? 108.684 111.683 100.258 1.00 53.28  ? 369 ASN A O     1 
ATOM   2619 C  CB    . ASN B 2 369 ? 109.708 113.924 102.305 1.00 46.62  ? 369 ASN A CB    1 
ATOM   2620 C  CG    . ASN B 2 369 ? 109.066 114.842 103.320 1.00 46.22  ? 369 ASN A CG    1 
ATOM   2621 O  OD1   . ASN B 2 369 ? 108.852 114.462 104.468 1.00 54.36  ? 369 ASN A OD1   1 
ATOM   2622 N  ND2   . ASN B 2 369 ? 108.750 116.059 102.900 1.00 37.70  ? 369 ASN A ND2   1 
ATOM   2623 N  N     . GLN B 2 370 ? 110.368 112.846 99.305  1.00 45.76  ? 370 GLN A N     1 
ATOM   2624 C  CA    . GLN B 2 370 ? 110.721 111.805 98.351  1.00 44.71  ? 370 GLN A CA    1 
ATOM   2625 C  C     . GLN B 2 370 ? 111.936 110.991 98.761  1.00 49.19  ? 370 GLN A C     1 
ATOM   2626 O  O     . GLN B 2 370 ? 112.061 109.837 98.340  1.00 52.68  ? 370 GLN A O     1 
ATOM   2627 C  CB    . GLN B 2 370 ? 110.982 112.426 96.975  1.00 44.91  ? 370 GLN A CB    1 
ATOM   2628 C  CG    . GLN B 2 370 ? 109.782 112.381 96.049  1.00 47.00  ? 370 GLN A CG    1 
ATOM   2629 C  CD    . GLN B 2 370 ? 110.000 113.184 94.789  1.00 44.74  ? 370 GLN A CD    1 
ATOM   2630 O  OE1   . GLN B 2 370 ? 110.744 112.774 93.900  1.00 47.68  ? 370 GLN A OE1   1 
ATOM   2631 N  NE2   . GLN B 2 370 ? 109.360 114.343 94.709  1.00 40.87  ? 370 GLN A NE2   1 
ATOM   2632 N  N     . LEU B 2 371 ? 112.838 111.559 99.564  1.00 49.89  ? 371 LEU A N     1 
ATOM   2633 C  CA    . LEU B 2 371 ? 114.073 110.864 99.907  1.00 56.18  ? 371 LEU A CA    1 
ATOM   2634 C  C     . LEU B 2 371 ? 114.445 111.021 101.379 1.00 59.43  ? 371 LEU A C     1 
ATOM   2635 O  O     . LEU B 2 371 ? 115.621 110.866 101.729 1.00 61.13  ? 371 LEU A O     1 
ATOM   2636 C  CB    . LEU B 2 371 ? 115.219 111.364 99.031  1.00 54.91  ? 371 LEU A CB    1 
ATOM   2637 C  CG    . LEU B 2 371 ? 114.973 111.269 97.522  1.00 52.60  ? 371 LEU A CG    1 
ATOM   2638 C  CD1   . LEU B 2 371 ? 114.508 112.609 96.995  1.00 56.20  ? 371 LEU A CD1   1 
ATOM   2639 C  CD2   . LEU B 2 371 ? 116.214 110.811 96.760  1.00 51.54  ? 371 LEU A CD2   1 
ATOM   2640 N  N     . LYS B 2 372 ? 113.484 111.325 102.248 1.00 59.27  ? 372 LYS A N     1 
ATOM   2641 C  CA    . LYS B 2 372 ? 113.747 111.420 103.677 1.00 60.61  ? 372 LYS A CA    1 
ATOM   2642 C  C     . LYS B 2 372 ? 113.640 110.075 104.382 1.00 57.74  ? 372 LYS A C     1 
ATOM   2643 O  O     . LYS B 2 372 ? 113.909 110.000 105.585 1.00 57.67  ? 372 LYS A O     1 
ATOM   2644 C  CB    . LYS B 2 372 ? 112.785 112.416 104.333 1.00 61.81  ? 372 LYS A CB    1 
ATOM   2645 C  CG    . LYS B 2 372 ? 112.917 113.837 103.811 1.00 58.70  ? 372 LYS A CG    1 
ATOM   2646 C  CD    . LYS B 2 372 ? 113.859 114.662 104.671 1.00 61.04  ? 372 LYS A CD    1 
ATOM   2647 C  CE    . LYS B 2 372 ? 113.814 116.130 104.286 1.00 70.12  ? 372 LYS A CE    1 
ATOM   2648 N  NZ    . LYS B 2 372 ? 114.084 116.336 102.837 1.00 70.80  ? 372 LYS A NZ    1 
ATOM   2649 N  N     . THR B 2 373 ? 113.260 109.020 103.668 1.00 56.21  ? 373 THR A N     1 
ATOM   2650 C  CA    . THR B 2 373 ? 113.183 107.675 104.217 1.00 54.77  ? 373 THR A CA    1 
ATOM   2651 C  C     . THR B 2 373 ? 114.348 106.851 103.691 1.00 55.78  ? 373 THR A C     1 
ATOM   2652 O  O     . THR B 2 373 ? 114.758 107.000 102.536 1.00 56.33  ? 373 THR A O     1 
ATOM   2653 C  CB    . THR B 2 373 ? 111.858 107.003 103.854 1.00 52.36  ? 373 THR A CB    1 
ATOM   2654 O  OG1   . THR B 2 373 ? 110.781 107.921 104.081 1.00 52.35  ? 373 THR A OG1   1 
ATOM   2655 C  CG2   . THR B 2 373 ? 111.636 105.748 104.693 1.00 50.44  ? 373 THR A CG2   1 
ATOM   2656 N  N     . PHE B 2 374 ? 114.876 105.979 104.550 1.00 57.46  ? 374 PHE A N     1 
ATOM   2657 C  CA    . PHE B 2 374 ? 116.107 105.267 104.228 1.00 63.78  ? 374 PHE A CA    1 
ATOM   2658 C  C     . PHE B 2 374 ? 115.926 104.376 103.003 1.00 65.14  ? 374 PHE A C     1 
ATOM   2659 O  O     . PHE B 2 374 ? 116.797 104.328 102.127 1.00 63.86  ? 374 PHE A O     1 
ATOM   2660 C  CB    . PHE B 2 374 ? 116.545 104.448 105.447 1.00 66.06  ? 374 PHE A CB    1 
ATOM   2661 C  CG    . PHE B 2 374 ? 117.869 103.746 105.287 1.00 70.96  ? 374 PHE A CG    1 
ATOM   2662 C  CD1   . PHE B 2 374 ? 118.744 104.075 104.267 1.00 69.81  ? 374 PHE A CD1   1 
ATOM   2663 C  CD2   . PHE B 2 374 ? 118.238 102.754 106.179 1.00 71.71  ? 374 PHE A CD2   1 
ATOM   2664 C  CE1   . PHE B 2 374 ? 119.951 103.424 104.140 1.00 70.35  ? 374 PHE A CE1   1 
ATOM   2665 C  CE2   . PHE B 2 374 ? 119.443 102.103 106.053 1.00 74.97  ? 374 PHE A CE2   1 
ATOM   2666 C  CZ    . PHE B 2 374 ? 120.299 102.437 105.034 1.00 74.61  ? 374 PHE A CZ    1 
ATOM   2667 N  N     . SER B 2 375 ? 114.797 103.671 102.919 1.00 63.60  ? 375 SER A N     1 
ATOM   2668 C  CA    . SER B 2 375 ? 114.563 102.712 101.847 1.00 55.99  ? 375 SER A CA    1 
ATOM   2669 C  C     . SER B 2 375 ? 114.009 103.344 100.578 1.00 53.49  ? 375 SER A C     1 
ATOM   2670 O  O     . SER B 2 375 ? 113.877 102.641 99.571  1.00 52.52  ? 375 SER A O     1 
ATOM   2671 C  CB    . SER B 2 375 ? 113.599 101.626 102.324 1.00 50.84  ? 375 SER A CB    1 
ATOM   2672 O  OG    . SER B 2 375 ? 112.368 102.186 102.746 1.00 46.31  ? 375 SER A OG    1 
ATOM   2673 N  N     . GLY B 2 376 ? 113.690 104.633 100.591 1.00 52.46  ? 376 GLY A N     1 
ATOM   2674 C  CA    . GLY B 2 376 ? 113.116 105.291 99.437  1.00 50.39  ? 376 GLY A CA    1 
ATOM   2675 C  C     . GLY B 2 376 ? 111.610 105.422 99.446  1.00 52.95  ? 376 GLY A C     1 
ATOM   2676 O  O     . GLY B 2 376 ? 111.036 105.812 98.425  1.00 61.79  ? 376 GLY A O     1 
ATOM   2677 N  N     . ARG B 2 377 ? 110.954 105.112 100.557 1.00 50.38  ? 377 ARG A N     1 
ATOM   2678 C  CA    . ARG B 2 377 ? 109.508 105.251 100.668 1.00 46.60  ? 377 ARG A CA    1 
ATOM   2679 C  C     . ARG B 2 377 ? 109.164 106.725 100.892 1.00 49.50  ? 377 ARG A C     1 
ATOM   2680 O  O     . ARG B 2 377 ? 110.019 107.611 100.820 1.00 48.88  ? 377 ARG A O     1 
ATOM   2681 C  CB    . ARG B 2 377 ? 108.996 104.342 101.779 1.00 45.45  ? 377 ARG A CB    1 
ATOM   2682 C  CG    . ARG B 2 377 ? 109.227 102.871 101.497 1.00 48.18  ? 377 ARG A CG    1 
ATOM   2683 C  CD    . ARG B 2 377 ? 109.292 102.042 102.762 1.00 49.15  ? 377 ARG A CD    1 
ATOM   2684 N  NE    . ARG B 2 377 ? 108.041 102.005 103.511 1.00 51.61  ? 377 ARG A NE    1 
ATOM   2685 C  CZ    . ARG B 2 377 ? 107.378 100.901 103.837 1.00 48.34  ? 377 ARG A CZ    1 
ATOM   2686 N  NH1   . ARG B 2 377 ? 107.730 99.713  103.374 1.00 39.25  ? 377 ARG A NH1   1 
ATOM   2687 N  NH2   . ARG B 2 377 ? 106.333 100.990 104.650 1.00 46.72  ? 377 ARG A NH2   1 
ATOM   2688 N  N     . PHE B 2 378 ? 107.895 107.000 101.174 1.00 48.68  ? 378 PHE A N     1 
ATOM   2689 C  CA    . PHE B 2 378 ? 107.385 108.361 101.279 1.00 49.38  ? 378 PHE A CA    1 
ATOM   2690 C  C     . PHE B 2 378 ? 107.180 108.726 102.743 1.00 52.25  ? 378 PHE A C     1 
ATOM   2691 O  O     . PHE B 2 378 ? 106.574 107.960 103.501 1.00 50.93  ? 378 PHE A O     1 
ATOM   2692 C  CB    . PHE B 2 378 ? 106.060 108.506 100.516 1.00 46.60  ? 378 PHE A CB    1 
ATOM   2693 C  CG    . PHE B 2 378 ? 106.208 108.933 99.070  1.00 48.86  ? 378 PHE A CG    1 
ATOM   2694 C  CD1   . PHE B 2 378 ? 107.376 109.511 98.587  1.00 46.93  ? 378 PHE A CD1   1 
ATOM   2695 C  CD2   . PHE B 2 378 ? 105.160 108.739 98.188  1.00 49.87  ? 378 PHE A CD2   1 
ATOM   2696 C  CE1   . PHE B 2 378 ? 107.483 109.887 97.267  1.00 47.35  ? 378 PHE A CE1   1 
ATOM   2697 C  CE2   . PHE B 2 378 ? 105.268 109.113 96.867  1.00 47.36  ? 378 PHE A CE2   1 
ATOM   2698 C  CZ    . PHE B 2 378 ? 106.430 109.685 96.407  1.00 46.08  ? 378 PHE A CZ    1 
ATOM   2699 N  N     . SER B 2 379 ? 107.683 109.896 103.131 1.00 49.62  ? 379 SER A N     1 
ATOM   2700 C  CA    . SER B 2 379 ? 107.501 110.446 104.468 1.00 42.87  ? 379 SER A CA    1 
ATOM   2701 C  C     . SER B 2 379 ? 106.656 111.706 104.374 1.00 42.66  ? 379 SER A C     1 
ATOM   2702 O  O     . SER B 2 379 ? 106.968 112.607 103.590 1.00 47.18  ? 379 SER A O     1 
ATOM   2703 C  CB    . SER B 2 379 ? 108.848 110.766 105.118 1.00 44.68  ? 379 SER A CB    1 
ATOM   2704 O  OG    . SER B 2 379 ? 109.786 109.731 104.888 1.00 49.31  ? 379 SER A OG    1 
ATOM   2705 N  N     . SER B 2 380 ? 105.598 111.769 105.173 1.00 41.61  ? 380 SER A N     1 
ATOM   2706 C  CA    . SER B 2 380 ? 104.693 112.917 105.212 1.00 43.93  ? 380 SER A CA    1 
ATOM   2707 C  C     . SER B 2 380 ? 104.891 113.619 106.556 1.00 47.49  ? 380 SER A C     1 
ATOM   2708 O  O     . SER B 2 380 ? 104.239 113.290 107.548 1.00 50.46  ? 380 SER A O     1 
ATOM   2709 C  CB    . SER B 2 380 ? 103.246 112.474 105.006 1.00 38.99  ? 380 SER A CB    1 
ATOM   2710 O  OG    . SER B 2 380 ? 102.342 113.513 105.334 1.00 42.85  ? 380 SER A OG    1 
ATOM   2711 N  N     . GLU B 2 381 ? 105.784 114.611 106.572 1.00 43.84  ? 381 GLU A N     1 
ATOM   2712 C  CA    . GLU B 2 381 ? 106.205 115.266 107.807 1.00 43.13  ? 381 GLU A CA    1 
ATOM   2713 C  C     . GLU B 2 381 ? 105.172 116.235 108.360 1.00 42.08  ? 381 GLU A C     1 
ATOM   2714 O  O     . GLU B 2 381 ? 105.390 116.788 109.442 1.00 49.42  ? 381 GLU A O     1 
ATOM   2715 C  CB    . GLU B 2 381 ? 107.529 116.005 107.587 1.00 49.19  ? 381 GLU A CB    1 
ATOM   2716 C  CG    . GLU B 2 381 ? 108.755 115.108 107.677 1.00 52.96  ? 381 GLU A CG    1 
ATOM   2717 C  CD    . GLU B 2 381 ? 109.989 115.841 108.169 1.00 64.90  ? 381 GLU A CD    1 
ATOM   2718 O  OE1   . GLU B 2 381 ? 109.977 117.090 108.202 1.00 70.78  ? 381 GLU A OE1   1 
ATOM   2719 O  OE2   . GLU B 2 381 ? 110.977 115.164 108.524 1.00 67.81  ? 381 GLU A OE2   1 
ATOM   2720 N  N     . LYS B 2 382 ? 104.081 116.476 107.647 1.00 38.59  ? 382 LYS A N     1 
ATOM   2721 C  CA    . LYS B 2 382 ? 102.945 117.214 108.183 1.00 38.80  ? 382 LYS A CA    1 
ATOM   2722 C  C     . LYS B 2 382 ? 101.747 116.276 108.091 1.00 40.14  ? 382 LYS A C     1 
ATOM   2723 O  O     . LYS B 2 382 ? 101.917 115.152 107.604 1.00 44.07  ? 382 LYS A O     1 
ATOM   2724 C  CB    . LYS B 2 382 ? 102.761 118.532 107.430 1.00 39.34  ? 382 LYS A CB    1 
ATOM   2725 C  CG    . LYS B 2 382 ? 102.542 119.764 108.319 1.00 41.02  ? 382 LYS A CG    1 
ATOM   2726 C  CD    . LYS B 2 382 ? 103.595 119.924 109.425 1.00 42.38  ? 382 LYS A CD    1 
ATOM   2727 C  CE    . LYS B 2 382 ? 104.989 120.121 108.859 1.00 41.75  ? 382 LYS A CE    1 
ATOM   2728 N  NZ    . LYS B 2 382 ? 106.016 120.234 109.929 1.00 39.56  ? 382 LYS A NZ    1 
ATOM   2729 N  N     . PRO B 2 383 ? 100.518 116.682 108.516 1.00 39.39  ? 383 PRO A N     1 
ATOM   2730 C  CA    . PRO B 2 383 ? 99.581  115.686 109.062 1.00 44.46  ? 383 PRO A CA    1 
ATOM   2731 C  C     . PRO B 2 383 ? 99.629  114.367 108.319 1.00 53.98  ? 383 PRO A C     1 
ATOM   2732 O  O     . PRO B 2 383 ? 99.303  114.287 107.131 1.00 58.16  ? 383 PRO A O     1 
ATOM   2733 C  CB    . PRO B 2 383 ? 98.213  116.366 108.912 1.00 42.00  ? 383 PRO A CB    1 
ATOM   2734 C  CG    . PRO B 2 383 ? 98.415  117.368 107.858 1.00 41.38  ? 383 PRO A CG    1 
ATOM   2735 C  CD    . PRO B 2 383 ? 99.785  117.894 108.115 1.00 40.95  ? 383 PRO A CD    1 
ATOM   2736 N  N     . ASN B 2 384 ? 100.038 113.322 109.028 1.00 51.17  ? 384 ASN A N     1 
ATOM   2737 C  CA    . ASN B 2 384 ? 100.410 112.062 108.398 1.00 46.31  ? 384 ASN A CA    1 
ATOM   2738 C  C     . ASN B 2 384 ? 99.137  111.358 107.961 1.00 47.97  ? 384 ASN A C     1 
ATOM   2739 O  O     . ASN B 2 384 ? 98.542  110.573 108.700 1.00 50.46  ? 384 ASN A O     1 
ATOM   2740 C  CB    . ASN B 2 384 ? 101.229 111.207 109.356 1.00 49.39  ? 384 ASN A CB    1 
ATOM   2741 C  CG    . ASN B 2 384 ? 102.608 110.884 108.817 1.00 50.14  ? 384 ASN A CG    1 
ATOM   2742 O  OD1   . ASN B 2 384 ? 102.787 110.697 107.616 1.00 51.11  ? 384 ASN A OD1   1 
ATOM   2743 N  ND2   . ASN B 2 384 ? 103.589 110.809 109.707 1.00 46.15  ? 384 ASN A ND2   1 
ATOM   2744 N  N     . LEU B 2 385 ? 98.707  111.652 106.735 1.00 47.57  ? 385 LEU A N     1 
ATOM   2745 C  CA    . LEU B 2 385 ? 97.619  110.895 106.136 1.00 49.70  ? 385 LEU A CA    1 
ATOM   2746 C  C     . LEU B 2 385 ? 97.994  109.438 105.920 1.00 51.19  ? 385 LEU A C     1 
ATOM   2747 O  O     . LEU B 2 385 ? 97.103  108.609 105.704 1.00 52.08  ? 385 LEU A O     1 
ATOM   2748 C  CB    . LEU B 2 385 ? 97.213  111.530 104.807 1.00 51.41  ? 385 LEU A CB    1 
ATOM   2749 C  CG    . LEU B 2 385 ? 95.919  112.347 104.824 1.00 53.97  ? 385 LEU A CG    1 
ATOM   2750 C  CD1   . LEU B 2 385 ? 94.731  111.433 105.034 1.00 55.28  ? 385 LEU A CD1   1 
ATOM   2751 C  CD2   . LEU B 2 385 ? 95.953  113.431 105.896 1.00 52.14  ? 385 LEU A CD2   1 
ATOM   2752 N  N     . GLN B 2 386 ? 99.288  109.114 105.971 1.00 49.43  ? 386 GLN A N     1 
ATOM   2753 C  CA    . GLN B 2 386 ? 99.715  107.722 105.917 1.00 47.01  ? 386 GLN A CA    1 
ATOM   2754 C  C     . GLN B 2 386 ? 99.372  106.983 107.205 1.00 46.92  ? 386 GLN A C     1 
ATOM   2755 O  O     . GLN B 2 386 ? 99.111  105.775 107.175 1.00 50.25  ? 386 GLN A O     1 
ATOM   2756 C  CB    . GLN B 2 386 ? 101.219 107.658 105.652 1.00 47.70  ? 386 GLN A CB    1 
ATOM   2757 C  CG    . GLN B 2 386 ? 101.640 108.364 104.370 1.00 49.39  ? 386 GLN A CG    1 
ATOM   2758 C  CD    . GLN B 2 386 ? 103.093 108.119 103.998 1.00 48.92  ? 386 GLN A CD    1 
ATOM   2759 O  OE1   . GLN B 2 386 ? 103.456 108.161 102.822 1.00 51.23  ? 386 GLN A OE1   1 
ATOM   2760 N  NE2   . GLN B 2 386 ? 103.935 107.878 104.999 1.00 45.12  ? 386 GLN A NE2   1 
ATOM   2761 N  N     . GLN B 2 387 ? 99.352  107.689 108.336 1.00 41.42  ? 387 GLN A N     1 
ATOM   2762 C  CA    . GLN B 2 387 ? 99.217  107.073 109.649 1.00 41.83  ? 387 GLN A CA    1 
ATOM   2763 C  C     . GLN B 2 387 ? 97.775  106.966 110.122 1.00 44.65  ? 387 GLN A C     1 
ATOM   2764 O  O     . GLN B 2 387 ? 97.546  106.552 111.262 1.00 44.90  ? 387 GLN A O     1 
ATOM   2765 C  CB    . GLN B 2 387 ? 100.011 107.866 110.687 1.00 42.84  ? 387 GLN A CB    1 
ATOM   2766 C  CG    . GLN B 2 387 ? 101.503 107.602 110.680 1.00 42.81  ? 387 GLN A CG    1 
ATOM   2767 C  CD    . GLN B 2 387 ? 102.234 108.305 111.817 1.00 45.33  ? 387 GLN A CD    1 
ATOM   2768 O  OE1   . GLN B 2 387 ? 103.374 107.965 112.130 1.00 45.95  ? 387 GLN A OE1   1 
ATOM   2769 N  NE2   . GLN B 2 387 ? 101.586 109.291 112.435 1.00 43.31  ? 387 GLN A NE2   1 
ATOM   2770 N  N     . ILE B 2 388 ? 96.802  107.330 109.292 1.00 45.22  ? 388 ILE A N     1 
ATOM   2771 C  CA    . ILE B 2 388 ? 95.414  107.288 109.765 1.00 47.95  ? 388 ILE A CA    1 
ATOM   2772 C  C     . ILE B 2 388 ? 95.078  105.863 110.185 1.00 49.82  ? 388 ILE A C     1 
ATOM   2773 O  O     . ILE B 2 388 ? 95.523  104.903 109.523 1.00 51.75  ? 388 ILE A O     1 
ATOM   2774 C  CB    . ILE B 2 388 ? 94.448  107.787 108.678 1.00 49.10  ? 388 ILE A CB    1 
ATOM   2775 C  CG1   . ILE B 2 388 ? 94.866  109.172 108.170 1.00 50.79  ? 388 ILE A CG1   1 
ATOM   2776 C  CG2   . ILE B 2 388 ? 93.031  107.832 109.220 1.00 51.08  ? 388 ILE A CG2   1 
ATOM   2777 C  CD1   . ILE B 2 388 ? 94.908  110.241 109.249 1.00 56.62  ? 388 ILE A CD1   1 
ATOM   2778 N  N     . PRO B 2 389 ? 94.322  105.651 111.265 1.00 49.45  ? 389 PRO A N     1 
ATOM   2779 C  CA    . PRO B 2 389 ? 94.091  104.280 111.733 1.00 52.81  ? 389 PRO A CA    1 
ATOM   2780 C  C     . PRO B 2 389 ? 93.467  103.413 110.651 1.00 52.73  ? 389 PRO A C     1 
ATOM   2781 O  O     . PRO B 2 389 ? 92.634  103.861 109.863 1.00 57.47  ? 389 PRO A O     1 
ATOM   2782 C  CB    . PRO B 2 389 ? 93.136  104.468 112.915 1.00 55.70  ? 389 PRO A CB    1 
ATOM   2783 C  CG    . PRO B 2 389 ? 93.436  105.827 113.420 1.00 54.55  ? 389 PRO A CG    1 
ATOM   2784 C  CD    . PRO B 2 389 ? 93.799  106.647 112.217 1.00 47.53  ? 389 PRO A CD    1 
ATOM   2785 N  N     . ARG B 2 390 ? 93.824  102.157 110.623 1.00 49.52  ? 390 ARG A N     1 
ATOM   2786 C  CA    . ARG B 2 390 ? 93.334  101.374 109.492 1.00 50.04  ? 390 ARG A CA    1 
ATOM   2787 C  C     . ARG B 2 390 ? 91.835  101.397 109.523 1.00 53.07  ? 390 ARG A C     1 
ATOM   2788 O  O     . ARG B 2 390 ? 91.231  101.530 108.471 1.00 55.80  ? 390 ARG A O     1 
ATOM   2789 C  CB    . ARG B 2 390 ? 93.800  99.936  109.638 1.00 58.40  ? 390 ARG A CB    1 
ATOM   2790 C  CG    . ARG B 2 390 ? 95.304  99.775  109.810 1.00 58.93  ? 390 ARG A CG    1 
ATOM   2791 C  CD    . ARG B 2 390 ? 95.768  98.350  109.549 1.00 64.84  ? 390 ARG A CD    1 
ATOM   2792 N  NE    . ARG B 2 390 ? 96.797  97.883  110.470 1.00 68.98  ? 390 ARG A NE    1 
ATOM   2793 C  CZ    . ARG B 2 390 ? 98.037  98.356  110.514 1.00 66.41  ? 390 ARG A CZ    1 
ATOM   2794 N  NH1   . ARG B 2 390 ? 98.399  99.316  109.688 1.00 57.80  ? 390 ARG A NH1   1 
ATOM   2795 N  NH2   . ARG B 2 390 ? 98.911  97.880  111.382 1.00 62.14  ? 390 ARG A NH2   1 
ATOM   2796 N  N     . GLN B 2 391 ? 91.261  101.287 110.700 1.00 54.15  ? 391 GLN A N     1 
ATOM   2797 C  CA    . GLN B 2 391 ? 89.815  101.114 110.742 1.00 61.39  ? 391 GLN A CA    1 
ATOM   2798 C  C     . GLN B 2 391 ? 89.143  102.115 109.810 1.00 64.75  ? 391 GLN A C     1 
ATOM   2799 O  O     . GLN B 2 391 ? 89.519  103.289 109.755 1.00 61.47  ? 391 GLN A O     1 
ATOM   2800 C  CB    . GLN B 2 391 ? 89.273  101.286 112.165 1.00 63.51  ? 391 GLN A CB    1 
ATOM   2801 C  CG    . GLN B 2 391 ? 89.881  102.429 112.962 1.00 63.49  ? 391 GLN A CG    1 
ATOM   2802 C  CD    . GLN B 2 391 ? 91.109  102.021 113.751 1.00 64.72  ? 391 GLN A CD    1 
ATOM   2803 O  OE1   . GLN B 2 391 ? 92.017  101.384 113.219 1.00 64.04  ? 391 GLN A OE1   1 
ATOM   2804 N  NE2   . GLN B 2 391 ? 91.140  102.383 115.028 1.00 60.06  ? 391 GLN A NE2   1 
ATOM   2805 N  N     . LYS B 2 392 ? 88.139  101.639 109.070 1.00 68.89  ? 392 LYS A N     1 
ATOM   2806 C  CA    . LYS B 2 392 ? 87.461  102.485 108.095 1.00 65.75  ? 392 LYS A CA    1 
ATOM   2807 C  C     . LYS B 2 392 ? 86.696  103.626 108.748 1.00 64.93  ? 392 LYS A C     1 
ATOM   2808 O  O     . LYS B 2 392 ? 86.499  104.664 108.108 1.00 67.11  ? 392 LYS A O     1 
ATOM   2809 C  CB    . LYS B 2 392 ? 86.503  101.654 107.238 1.00 65.93  ? 392 LYS A CB    1 
ATOM   2810 C  CG    . LYS B 2 392 ? 85.419  100.926 108.027 1.00 71.77  ? 392 LYS A CG    1 
ATOM   2811 C  CD    . LYS B 2 392 ? 84.397  100.264 107.108 1.00 79.25  ? 392 LYS A CD    1 
ATOM   2812 C  CE    . LYS B 2 392 ? 83.496  101.277 106.404 1.00 80.36  ? 392 LYS A CE    1 
ATOM   2813 N  NZ    . LYS B 2 392 ? 82.462  101.848 107.309 1.00 81.02  ? 392 LYS A NZ    1 
ATOM   2814 N  N     . ASN B 2 393 ? 86.268  103.469 110.003 1.00 64.91  ? 393 ASN A N     1 
ATOM   2815 C  CA    . ASN B 2 393 ? 85.466  104.503 110.644 1.00 65.58  ? 393 ASN A CA    1 
ATOM   2816 C  C     . ASN B 2 393 ? 86.240  105.796 110.864 1.00 64.72  ? 393 ASN A C     1 
ATOM   2817 O  O     . ASN B 2 393 ? 85.619  106.823 111.156 1.00 67.53  ? 393 ASN A O     1 
ATOM   2818 C  CB    . ASN B 2 393 ? 84.897  103.981 111.969 1.00 68.79  ? 393 ASN A CB    1 
ATOM   2819 C  CG    . ASN B 2 393 ? 85.892  104.061 113.111 1.00 71.92  ? 393 ASN A CG    1 
ATOM   2820 O  OD1   . ASN B 2 393 ? 87.098  104.124 112.893 1.00 70.67  ? 393 ASN A OD1   1 
ATOM   2821 N  ND2   . ASN B 2 393 ? 85.387  104.054 114.342 1.00 73.83  ? 393 ASN A ND2   1 
ATOM   2822 N  N     . ILE B 2 394 ? 87.563  105.777 110.727 1.00 62.06  ? 394 ILE A N     1 
ATOM   2823 C  CA    . ILE B 2 394 ? 88.353  107.006 110.768 1.00 61.64  ? 394 ILE A CA    1 
ATOM   2824 C  C     . ILE B 2 394 ? 88.596  107.555 109.371 1.00 66.73  ? 394 ILE A C     1 
ATOM   2825 O  O     . ILE B 2 394 ? 88.410  108.747 109.121 1.00 71.16  ? 394 ILE A O     1 
ATOM   2826 C  CB    . ILE B 2 394 ? 89.686  106.772 111.508 1.00 56.28  ? 394 ILE A CB    1 
ATOM   2827 C  CG1   . ILE B 2 394 ? 89.472  105.950 112.779 1.00 61.00  ? 394 ILE A CG1   1 
ATOM   2828 C  CG2   . ILE B 2 394 ? 90.352  108.104 111.828 1.00 53.31  ? 394 ILE A CG2   1 
ATOM   2829 C  CD1   . ILE B 2 394 ? 88.507  106.583 113.763 1.00 65.62  ? 394 ILE A CD1   1 
ATOM   2830 N  N     . ARG B 2 395 ? 89.033  106.708 108.440 1.00 63.80  ? 395 ARG A N     1 
ATOM   2831 C  CA    . ARG B 2 395 ? 89.318  107.171 107.087 1.00 59.30  ? 395 ARG A CA    1 
ATOM   2832 C  C     . ARG B 2 395 ? 88.065  107.533 106.298 1.00 63.16  ? 395 ARG A C     1 
ATOM   2833 O  O     . ARG B 2 395 ? 88.189  108.095 105.205 1.00 62.91  ? 395 ARG A O     1 
ATOM   2834 C  CB    . ARG B 2 395 ? 90.132  106.113 106.346 1.00 53.17  ? 395 ARG A CB    1 
ATOM   2835 C  CG    . ARG B 2 395 ? 91.551  106.000 106.870 1.00 49.47  ? 395 ARG A CG    1 
ATOM   2836 C  CD    . ARG B 2 395 ? 92.344  104.923 106.156 1.00 50.91  ? 395 ARG A CD    1 
ATOM   2837 N  NE    . ARG B 2 395 ? 93.670  104.759 106.738 1.00 49.81  ? 395 ARG A NE    1 
ATOM   2838 C  CZ    . ARG B 2 395 ? 94.584  103.904 106.298 1.00 49.30  ? 395 ARG A CZ    1 
ATOM   2839 N  NH1   . ARG B 2 395 ? 94.330  103.071 105.305 1.00 48.51  ? 395 ARG A NH1   1 
ATOM   2840 N  NH2   . ARG B 2 395 ? 95.780  103.879 106.875 1.00 49.00  ? 395 ARG A NH2   1 
ATOM   2841 N  N     . GLU B 2 396 ? 86.872  107.241 106.819 1.00 67.62  ? 396 GLU A N     1 
ATOM   2842 C  CA    . GLU B 2 396 ? 85.643  107.686 106.171 1.00 67.27  ? 396 GLU A CA    1 
ATOM   2843 C  C     . GLU B 2 396 ? 85.472  109.199 106.204 1.00 67.86  ? 396 GLU A C     1 
ATOM   2844 O  O     . GLU B 2 396 ? 84.555  109.712 105.554 1.00 74.37  ? 396 GLU A O     1 
ATOM   2845 C  CB    . GLU B 2 396 ? 84.434  107.011 106.824 1.00 68.98  ? 396 GLU A CB    1 
ATOM   2846 C  CG    . GLU B 2 396 ? 84.105  105.655 106.225 1.00 77.13  ? 396 GLU A CG    1 
ATOM   2847 C  CD    . GLU B 2 396 ? 82.944  104.974 106.924 1.00 81.22  ? 396 GLU A CD    1 
ATOM   2848 O  OE1   . GLU B 2 396 ? 82.777  105.180 108.144 1.00 77.87  ? 396 GLU A OE1   1 
ATOM   2849 O  OE2   . GLU B 2 396 ? 82.197  104.232 106.252 1.00 82.90  ? 396 GLU A OE2   1 
ATOM   2850 N  N     . ILE B 2 397 ? 86.322  109.923 106.941 1.00 65.16  ? 397 ILE A N     1 
ATOM   2851 C  CA    . ILE B 2 397 ? 86.219  111.380 107.020 1.00 68.40  ? 397 ILE A CA    1 
ATOM   2852 C  C     . ILE B 2 397 ? 86.920  112.095 105.876 1.00 68.22  ? 397 ILE A C     1 
ATOM   2853 O  O     . ILE B 2 397 ? 86.859  113.329 105.807 1.00 69.17  ? 397 ILE A O     1 
ATOM   2854 C  CB    . ILE B 2 397 ? 86.768  111.876 108.375 1.00 69.45  ? 397 ILE A CB    1 
ATOM   2855 C  CG1   . ILE B 2 397 ? 88.302  111.857 108.394 1.00 65.04  ? 397 ILE A CG1   1 
ATOM   2856 C  CG2   . ILE B 2 397 ? 86.188  111.038 109.512 1.00 70.40  ? 397 ILE A CG2   1 
ATOM   2857 C  CD1   . ILE B 2 397 ? 88.903  112.250 109.729 1.00 60.19  ? 397 ILE A CD1   1 
ATOM   2858 N  N     . PHE B 2 398 ? 87.574  111.370 104.973 1.00 66.57  ? 398 PHE A N     1 
ATOM   2859 C  CA    . PHE B 2 398 ? 88.257  111.964 103.830 1.00 68.00  ? 398 PHE A CA    1 
ATOM   2860 C  C     . PHE B 2 398 ? 87.439  111.687 102.576 1.00 68.84  ? 398 PHE A C     1 
ATOM   2861 O  O     . PHE B 2 398 ? 87.041  110.544 102.332 1.00 73.03  ? 398 PHE A O     1 
ATOM   2862 C  CB    . PHE B 2 398 ? 89.677  111.408 103.694 1.00 57.93  ? 398 PHE A CB    1 
ATOM   2863 C  CG    . PHE B 2 398 ? 90.462  111.442 104.972 1.00 55.30  ? 398 PHE A CG    1 
ATOM   2864 C  CD1   . PHE B 2 398 ? 90.384  110.401 105.876 1.00 57.35  ? 398 PHE A CD1   1 
ATOM   2865 C  CD2   . PHE B 2 398 ? 91.263  112.523 105.277 1.00 56.98  ? 398 PHE A CD2   1 
ATOM   2866 C  CE1   . PHE B 2 398 ? 91.100  110.436 107.050 1.00 59.73  ? 398 PHE A CE1   1 
ATOM   2867 C  CE2   . PHE B 2 398 ? 91.975  112.560 106.452 1.00 57.40  ? 398 PHE A CE2   1 
ATOM   2868 C  CZ    . PHE B 2 398 ? 91.894  111.516 107.337 1.00 58.57  ? 398 PHE A CZ    1 
ATOM   2869 N  N     . ILE B 2 399 ? 87.188  112.730 101.789 1.00 69.10  ? 399 ILE A N     1 
ATOM   2870 C  CA    . ILE B 2 399 ? 86.136  112.691 100.773 1.00 76.44  ? 399 ILE A CA    1 
ATOM   2871 C  C     . ILE B 2 399 ? 86.621  113.369 99.498  1.00 79.45  ? 399 ILE A C     1 
ATOM   2872 O  O     . ILE B 2 399 ? 87.575  114.151 99.509  1.00 80.17  ? 399 ILE A O     1 
ATOM   2873 C  CB    . ILE B 2 399 ? 84.846  113.376 101.261 1.00 78.32  ? 399 ILE A CB    1 
ATOM   2874 C  CG1   . ILE B 2 399 ? 85.189  114.628 102.078 1.00 75.44  ? 399 ILE A CG1   1 
ATOM   2875 C  CG2   . ILE B 2 399 ? 84.008  112.387 102.063 1.00 76.46  ? 399 ILE A CG2   1 
ATOM   2876 C  CD1   . ILE B 2 399 ? 83.990  115.326 102.686 1.00 80.31  ? 399 ILE A CD1   1 
ATOM   2877 N  N     . PRO B 2 400 ? 85.967  113.066 98.375  1.00 78.23  ? 400 PRO A N     1 
ATOM   2878 C  CA    . PRO B 2 400 ? 86.245  113.803 97.138  1.00 81.11  ? 400 PRO A CA    1 
ATOM   2879 C  C     . PRO B 2 400 ? 85.569  115.164 97.115  1.00 84.70  ? 400 PRO A C     1 
ATOM   2880 O  O     . PRO B 2 400 ? 84.637  115.447 97.871  1.00 85.57  ? 400 PRO A O     1 
ATOM   2881 C  CB    . PRO B 2 400 ? 85.663  112.894 96.050  1.00 83.17  ? 400 PRO A CB    1 
ATOM   2882 C  CG    . PRO B 2 400 ? 84.534  112.205 96.732  1.00 81.37  ? 400 PRO A CG    1 
ATOM   2883 C  CD    . PRO B 2 400 ? 85.010  111.972 98.146  1.00 75.82  ? 400 PRO A CD    1 
ATOM   2884 N  N     . ASN B 2 401 ? 86.060  116.013 96.216  1.00 84.50  ? 401 ASN A N     1 
ATOM   2885 C  CA    . ASN B 2 401 ? 85.322  117.212 95.850  1.00 87.84  ? 401 ASN A CA    1 
ATOM   2886 C  C     . ASN B 2 401 ? 83.991  116.815 95.223  1.00 94.21  ? 401 ASN A C     1 
ATOM   2887 O  O     . ASN B 2 401 ? 83.863  115.755 94.606  1.00 95.22  ? 401 ASN A O     1 
ATOM   2888 C  CB    . ASN B 2 401 ? 86.138  118.066 94.879  1.00 82.50  ? 401 ASN A CB    1 
ATOM   2889 C  CG    . ASN B 2 401 ? 87.548  118.324 95.371  1.00 78.99  ? 401 ASN A CG    1 
ATOM   2890 O  OD1   . ASN B 2 401 ? 87.774  119.190 96.216  1.00 79.58  ? 401 ASN A OD1   1 
ATOM   2891 N  ND2   . ASN B 2 401 ? 88.506  117.577 94.839  1.00 74.89  ? 401 ASN A ND2   1 
ATOM   2892 N  N     . ASP B 2 402 ? 82.991  117.678 95.382  1.00 100.48 ? 402 ASP A N     1 
ATOM   2893 C  CA    . ASP B 2 402 ? 81.636  117.313 94.992  1.00 104.03 ? 402 ASP A CA    1 
ATOM   2894 C  C     . ASP B 2 402 ? 81.576  116.914 93.520  1.00 102.03 ? 402 ASP A C     1 
ATOM   2895 O  O     . ASP B 2 402 ? 82.292  117.455 92.672  1.00 99.53  ? 402 ASP A O     1 
ATOM   2896 C  CB    . ASP B 2 402 ? 80.667  118.468 95.257  1.00 112.01 ? 402 ASP A CB    1 
ATOM   2897 C  CG    . ASP B 2 402 ? 81.259  119.817 94.917  1.00 115.23 ? 402 ASP A CG    1 
ATOM   2898 O  OD1   . ASP B 2 402 ? 82.188  120.250 95.632  1.00 113.27 ? 402 ASP A OD1   1 
ATOM   2899 O  OD2   . ASP B 2 402 ? 80.800  120.437 93.938  1.00 115.79 ? 402 ASP A OD2   1 
ATOM   2900 N  N     . ASN B 2 403 ? 80.721  115.928 93.237  1.00 101.65 ? 403 ASN A N     1 
ATOM   2901 C  CA    . ASN B 2 403 ? 80.447  115.431 91.890  1.00 101.35 ? 403 ASN A CA    1 
ATOM   2902 C  C     . ASN B 2 403 ? 81.588  114.588 91.327  1.00 101.46 ? 403 ASN A C     1 
ATOM   2903 O  O     . ASN B 2 403 ? 81.434  113.962 90.273  1.00 102.89 ? 403 ASN A O     1 
ATOM   2904 C  CB    . ASN B 2 403 ? 80.146  116.603 90.948  1.00 102.70 ? 403 ASN A CB    1 
ATOM   2905 C  CG    . ASN B 2 403 ? 79.741  116.149 89.559  1.00 107.37 ? 403 ASN A CG    1 
ATOM   2906 O  OD1   . ASN B 2 403 ? 78.685  115.544 89.371  1.00 112.87 ? 403 ASN A OD1   1 
ATOM   2907 N  ND2   . ASN B 2 403 ? 80.580  116.452 88.573  1.00 105.60 ? 403 ASN A ND2   1 
ATOM   2908 N  N     . ASN B 2 404 ? 82.722  114.536 92.022  1.00 98.22  ? 404 ASN A N     1 
ATOM   2909 C  CA    . ASN B 2 404 ? 83.831  113.696 91.596  1.00 91.92  ? 404 ASN A CA    1 
ATOM   2910 C  C     . ASN B 2 404 ? 83.862  112.400 92.405  1.00 90.20  ? 404 ASN A C     1 
ATOM   2911 O  O     . ASN B 2 404 ? 83.069  112.186 93.326  1.00 89.77  ? 404 ASN A O     1 
ATOM   2912 C  CB    . ASN B 2 404 ? 85.145  114.464 91.703  1.00 85.37  ? 404 ASN A CB    1 
ATOM   2913 C  CG    . ASN B 2 404 ? 85.138  115.733 90.879  1.00 85.97  ? 404 ASN A CG    1 
ATOM   2914 O  OD1   . ASN B 2 404 ? 84.449  115.816 89.864  1.00 89.19  ? 404 ASN A OD1   1 
ATOM   2915 N  ND2   . ASN B 2 404 ? 85.909  116.724 91.302  1.00 84.89  ? 404 ASN A ND2   1 
ATOM   2916 N  N     . ILE B 2 405 ? 84.794  111.514 92.045  1.00 88.70  ? 405 ILE A N     1 
ATOM   2917 C  CA    . ILE B 2 405 ? 84.920  110.201 92.665  1.00 86.41  ? 405 ILE A CA    1 
ATOM   2918 C  C     . ILE B 2 405 ? 86.389  109.792 92.664  1.00 82.48  ? 405 ILE A C     1 
ATOM   2919 O  O     . ILE B 2 405 ? 87.196  110.289 91.876  1.00 81.70  ? 405 ILE A O     1 
ATOM   2920 C  CB    . ILE B 2 405 ? 84.052  109.143 91.939  1.00 87.58  ? 405 ILE A CB    1 
ATOM   2921 C  CG1   . ILE B 2 405 ? 83.842  107.903 92.814  1.00 81.64  ? 405 ILE A CG1   1 
ATOM   2922 C  CG2   . ILE B 2 405 ? 84.675  108.755 90.606  1.00 88.24  ? 405 ILE A CG2   1 
ATOM   2923 C  CD1   . ILE B 2 405 ? 82.606  107.092 92.427  1.00 83.47  ? 405 ILE A CD1   1 
ATOM   2924 N  N     . PHE B 2 406 ? 86.729  108.874 93.567  1.00 79.04  ? 406 PHE A N     1 
ATOM   2925 C  CA    . PHE B 2 406 ? 88.085  108.346 93.684  1.00 76.65  ? 406 PHE A CA    1 
ATOM   2926 C  C     . PHE B 2 406 ? 88.220  106.963 93.062  1.00 78.52  ? 406 PHE A C     1 
ATOM   2927 O  O     . PHE B 2 406 ? 87.281  106.163 93.078  1.00 81.37  ? 406 PHE A O     1 
ATOM   2928 C  CB    . PHE B 2 406 ? 88.534  108.251 95.146  1.00 80.56  ? 406 PHE A CB    1 
ATOM   2929 C  CG    . PHE B 2 406 ? 88.614  109.564 95.867  1.00 86.82  ? 406 PHE A CG    1 
ATOM   2930 C  CD1   . PHE B 2 406 ? 88.822  110.747 95.184  1.00 85.39  ? 406 PHE A CD1   1 
ATOM   2931 C  CD2   . PHE B 2 406 ? 88.518  109.603 97.246  1.00 79.66  ? 406 PHE A CD2   1 
ATOM   2932 C  CE1   . PHE B 2 406 ? 88.917  111.939 95.866  1.00 78.66  ? 406 PHE A CE1   1 
ATOM   2933 C  CE2   . PHE B 2 406 ? 88.609  110.789 97.924  1.00 74.85  ? 406 PHE A CE2   1 
ATOM   2934 C  CZ    . PHE B 2 406 ? 88.811  111.955 97.237  1.00 71.87  ? 406 PHE A CZ    1 
ATOM   2935 N  N     . ILE B 2 407 ? 89.410  106.694 92.522  1.00 79.82  ? 407 ILE A N     1 
ATOM   2936 C  CA    . ILE B 2 407 ? 89.869  105.346 92.208  1.00 79.38  ? 407 ILE A CA    1 
ATOM   2937 C  C     . ILE B 2 407 ? 90.951  105.007 93.221  1.00 78.59  ? 407 ILE A C     1 
ATOM   2938 O  O     . ILE B 2 407 ? 91.848  105.824 93.464  1.00 74.82  ? 407 ILE A O     1 
ATOM   2939 C  CB    . ILE B 2 407 ? 90.433  105.255 90.779  1.00 74.61  ? 407 ILE A CB    1 
ATOM   2940 C  CG1   . ILE B 2 407 ? 89.439  105.788 89.741  1.00 83.05  ? 407 ILE A CG1   1 
ATOM   2941 C  CG2   . ILE B 2 407 ? 90.801  103.811 90.457  1.00 69.32  ? 407 ILE A CG2   1 
ATOM   2942 C  CD1   . ILE B 2 407 ? 88.014  105.300 89.899  1.00 89.36  ? 407 ILE A CD1   1 
ATOM   2943 N  N     . ILE B 2 408 ? 90.880  103.819 93.818  1.00 77.78  ? 408 ILE A N     1 
ATOM   2944 C  CA    . ILE B 2 408 ? 91.902  103.361 94.755  1.00 71.96  ? 408 ILE A CA    1 
ATOM   2945 C  C     . ILE B 2 408 ? 92.462  102.034 94.267  1.00 69.73  ? 408 ILE A C     1 
ATOM   2946 O  O     . ILE B 2 408 ? 91.714  101.161 93.814  1.00 69.82  ? 408 ILE A O     1 
ATOM   2947 C  CB    . ILE B 2 408 ? 91.372  103.220 96.198  1.00 68.98  ? 408 ILE A CB    1 
ATOM   2948 C  CG1   . ILE B 2 408 ? 90.473  104.400 96.569  1.00 68.17  ? 408 ILE A CG1   1 
ATOM   2949 C  CG2   . ILE B 2 408 ? 92.536  103.117 97.181  1.00 63.05  ? 408 ILE A CG2   1 
ATOM   2950 C  CD1   . ILE B 2 408 ? 89.819  104.254 97.919  1.00 69.64  ? 408 ILE A CD1   1 
ATOM   2951 N  N     . ALA B 2 409 ? 93.782  101.886 94.367  1.00 65.48  ? 409 ALA A N     1 
ATOM   2952 C  CA    . ALA B 2 409 ? 94.464  100.664 93.966  1.00 64.85  ? 409 ALA A CA    1 
ATOM   2953 C  C     . ALA B 2 409 ? 95.475  100.278 95.031  1.00 64.36  ? 409 ALA A C     1 
ATOM   2954 O  O     . ALA B 2 409 ? 96.245  101.125 95.493  1.00 62.31  ? 409 ALA A O     1 
ATOM   2955 C  CB    . ALA B 2 409 ? 95.171  100.832 92.621  1.00 68.96  ? 409 ALA A CB    1 
ATOM   2956 N  N     . ASP B 2 410 ? 95.479  98.998  95.397  1.00 65.43  ? 410 ASP A N     1 
ATOM   2957 C  CA    . ASP B 2 410 ? 96.367  98.460  96.417  1.00 58.70  ? 410 ASP A CA    1 
ATOM   2958 C  C     . ASP B 2 410 ? 97.028  97.207  95.863  1.00 61.01  ? 410 ASP A C     1 
ATOM   2959 O  O     . ASP B 2 410 ? 96.345  96.334  95.318  1.00 63.43  ? 410 ASP A O     1 
ATOM   2960 C  CB    . ASP B 2 410 ? 95.594  98.140  97.704  1.00 57.49  ? 410 ASP A CB    1 
ATOM   2961 C  CG    . ASP B 2 410 ? 96.492  97.646  98.824  1.00 57.61  ? 410 ASP A CG    1 
ATOM   2962 O  OD1   . ASP B 2 410 ? 97.401  96.832  98.558  1.00 57.51  ? 410 ASP A OD1   1 
ATOM   2963 O  OD2   . ASP B 2 410 ? 96.285  98.071  99.980  1.00 57.07  ? 410 ASP A OD2   1 
ATOM   2964 N  N     . PHE B 2 411 ? 98.350  97.122  95.997  1.00 58.33  ? 411 PHE A N     1 
ATOM   2965 C  CA    . PHE B 2 411 ? 99.072  95.949  95.526  1.00 55.02  ? 411 PHE A CA    1 
ATOM   2966 C  C     . PHE B 2 411 ? 98.652  94.713  96.310  1.00 55.10  ? 411 PHE A C     1 
ATOM   2967 O  O     . PHE B 2 411 ? 98.466  94.761  97.529  1.00 55.64  ? 411 PHE A O     1 
ATOM   2968 C  CB    . PHE B 2 411 ? 100.581 96.158  95.663  1.00 50.96  ? 411 PHE A CB    1 
ATOM   2969 C  CG    . PHE B 2 411 ? 101.249 96.658  94.412  1.00 55.17  ? 411 PHE A CG    1 
ATOM   2970 C  CD1   . PHE B 2 411 ? 101.076 96.007  93.205  1.00 57.28  ? 411 PHE A CD1   1 
ATOM   2971 C  CD2   . PHE B 2 411 ? 102.068 97.772  94.450  1.00 58.99  ? 411 PHE A CD2   1 
ATOM   2972 C  CE1   . PHE B 2 411 ? 101.694 96.467  92.062  1.00 54.77  ? 411 PHE A CE1   1 
ATOM   2973 C  CE2   . PHE B 2 411 ? 102.688 98.232  93.309  1.00 57.18  ? 411 PHE A CE2   1 
ATOM   2974 C  CZ    . PHE B 2 411 ? 102.502 97.578  92.116  1.00 53.63  ? 411 PHE A CZ    1 
ATOM   2975 N  N     . LYS B 2 412 ? 98.503  93.598  95.600  1.00 55.11  ? 412 LYS A N     1 
ATOM   2976 C  CA    . LYS B 2 412 ? 98.131  92.322  96.210  1.00 51.37  ? 412 LYS A CA    1 
ATOM   2977 C  C     . LYS B 2 412 ? 99.405  91.570  96.561  1.00 46.14  ? 412 LYS A C     1 
ATOM   2978 O  O     . LYS B 2 412 ? 100.041 90.962  95.696  1.00 42.02  ? 412 LYS A O     1 
ATOM   2979 C  CB    . LYS B 2 412 ? 97.241  91.516  95.273  1.00 58.84  ? 412 LYS A CB    1 
ATOM   2980 C  CG    . LYS B 2 412 ? 95.773  91.539  95.664  1.00 65.45  ? 412 LYS A CG    1 
ATOM   2981 C  CD    . LYS B 2 412 ? 94.986  90.457  94.950  1.00 68.80  ? 412 LYS A CD    1 
ATOM   2982 C  CE    . LYS B 2 412 ? 94.356  91.004  93.685  1.00 72.46  ? 412 LYS A CE    1 
ATOM   2983 N  NZ    . LYS B 2 412 ? 93.515  90.008  92.976  1.00 75.89  ? 412 LYS A NZ    1 
ATOM   2984 N  N     . GLN B 2 413 ? 99.781  91.619  97.836  1.00 49.52  ? 413 GLN A N     1 
ATOM   2985 C  CA    . GLN B 2 413 ? 100.927 90.881  98.355  1.00 46.40  ? 413 GLN A CA    1 
ATOM   2986 C  C     . GLN B 2 413 ? 102.184 91.201  97.547  1.00 45.34  ? 413 GLN A C     1 
ATOM   2987 O  O     . GLN B 2 413 ? 102.869 90.323  97.025  1.00 43.14  ? 413 GLN A O     1 
ATOM   2988 C  CB    . GLN B 2 413 ? 100.630 89.383  98.356  1.00 43.65  ? 413 GLN A CB    1 
ATOM   2989 C  CG    . GLN B 2 413 ? 101.699 88.523  98.979  1.00 41.07  ? 413 GLN A CG    1 
ATOM   2990 C  CD    . GLN B 2 413 ? 101.307 87.067  98.986  1.00 50.71  ? 413 GLN A CD    1 
ATOM   2991 O  OE1   . GLN B 2 413 ? 100.123 86.730  98.967  1.00 56.32  ? 413 GLN A OE1   1 
ATOM   2992 N  NE2   . GLN B 2 413 ? 102.300 86.193  98.982  1.00 55.94  ? 413 GLN A NE2   1 
ATOM   2993 N  N     . ILE B 2 414 ? 102.480 92.498  97.456  1.00 47.89  ? 414 ILE A N     1 
ATOM   2994 C  CA    . ILE B 2 414 ? 103.629 92.935  96.671  1.00 48.16  ? 414 ILE A CA    1 
ATOM   2995 C  C     . ILE B 2 414 ? 104.908 92.320  97.217  1.00 45.10  ? 414 ILE A C     1 
ATOM   2996 O  O     . ILE B 2 414 ? 105.783 91.897  96.454  1.00 45.77  ? 414 ILE A O     1 
ATOM   2997 C  CB    . ILE B 2 414 ? 103.706 94.474  96.628  1.00 49.24  ? 414 ILE A CB    1 
ATOM   2998 C  CG1   . ILE B 2 414 ? 105.066 94.936  96.097  1.00 46.59  ? 414 ILE A CG1   1 
ATOM   2999 C  CG2   . ILE B 2 414 ? 103.455 95.071  98.006  1.00 53.26  ? 414 ILE A CG2   1 
ATOM   3000 C  CD1   . ILE B 2 414 ? 105.297 94.588  94.650  1.00 42.05  ? 414 ILE A CD1   1 
ATOM   3001 N  N     . GLU B 2 415 ? 105.053 92.280  98.535  1.00 41.53  ? 415 GLU A N     1 
ATOM   3002 C  CA    . GLU B 2 415 ? 106.229 91.653  99.109  1.00 42.25  ? 415 GLU A CA    1 
ATOM   3003 C  C     . GLU B 2 415 ? 106.016 90.144  99.209  1.00 46.58  ? 415 GLU A C     1 
ATOM   3004 O  O     . GLU B 2 415 ? 104.890 89.642  99.159  1.00 47.02  ? 415 GLU A O     1 
ATOM   3005 C  CB    . GLU B 2 415 ? 106.546 92.271  100.469 1.00 43.69  ? 415 GLU A CB    1 
ATOM   3006 C  CG    . GLU B 2 415 ? 106.783 93.773  100.382 1.00 50.21  ? 415 GLU A CG    1 
ATOM   3007 C  CD    . GLU B 2 415 ? 107.850 94.269  101.336 1.00 52.92  ? 415 GLU A CD    1 
ATOM   3008 O  OE1   . GLU B 2 415 ? 108.998 94.476  100.892 1.00 51.11  ? 415 GLU A OE1   1 
ATOM   3009 O  OE2   . GLU B 2 415 ? 107.543 94.451  102.530 1.00 52.33  ? 415 GLU A OE2   1 
ATOM   3010 N  N     . LEU B 2 416 ? 107.130 89.423  99.326  1.00 45.17  ? 416 LEU A N     1 
ATOM   3011 C  CA    . LEU B 2 416 ? 107.185 87.975  99.137  1.00 37.90  ? 416 LEU A CA    1 
ATOM   3012 C  C     . LEU B 2 416 ? 107.073 87.612  97.659  1.00 43.10  ? 416 LEU A C     1 
ATOM   3013 O  O     . LEU B 2 416 ? 107.233 86.443  97.294  1.00 49.81  ? 416 LEU A O     1 
ATOM   3014 C  CB    . LEU B 2 416 ? 106.092 87.253  99.932  1.00 39.28  ? 416 LEU A CB    1 
ATOM   3015 C  CG    . LEU B 2 416 ? 105.896 87.624  101.403 1.00 46.79  ? 416 LEU A CG    1 
ATOM   3016 C  CD1   . LEU B 2 416 ? 104.909 86.663  102.031 1.00 48.91  ? 416 LEU A CD1   1 
ATOM   3017 C  CD2   . LEU B 2 416 ? 107.209 87.598  102.167 1.00 48.31  ? 416 LEU A CD2   1 
ATOM   3018 N  N     . LYS B 2 417 ? 106.809 88.597  96.800  1.00 41.39  ? 417 LYS A N     1 
ATOM   3019 C  CA    . LYS B 2 417 ? 106.948 88.411  95.362  1.00 39.64  ? 417 LYS A CA    1 
ATOM   3020 C  C     . LYS B 2 417 ? 108.273 88.965  94.868  1.00 41.80  ? 417 LYS A C     1 
ATOM   3021 O  O     . LYS B 2 417 ? 108.950 88.326  94.057  1.00 49.49  ? 417 LYS A O     1 
ATOM   3022 C  CB    . LYS B 2 417 ? 105.791 89.076  94.619  1.00 35.64  ? 417 LYS A CB    1 
ATOM   3023 C  CG    . LYS B 2 417 ? 104.474 88.355  94.776  1.00 34.90  ? 417 LYS A CG    1 
ATOM   3024 C  CD    . LYS B 2 417 ? 103.371 89.056  94.007  1.00 34.98  ? 417 LYS A CD    1 
ATOM   3025 C  CE    . LYS B 2 417 ? 102.038 88.368  94.218  1.00 38.29  ? 417 LYS A CE    1 
ATOM   3026 N  NZ    . LYS B 2 417 ? 100.904 89.174  93.706  1.00 41.58  ? 417 LYS A NZ    1 
ATOM   3027 N  N     . ILE B 2 418 ? 108.655 90.147  95.346  1.00 34.20  ? 418 ILE A N     1 
ATOM   3028 C  CA    . ILE B 2 418 ? 110.016 90.617  95.132  1.00 34.02  ? 418 ILE A CA    1 
ATOM   3029 C  C     . ILE B 2 418 ? 111.001 89.664  95.786  1.00 39.90  ? 418 ILE A C     1 
ATOM   3030 O  O     . ILE B 2 418 ? 112.066 89.368  95.233  1.00 43.49  ? 418 ILE A O     1 
ATOM   3031 C  CB    . ILE B 2 418 ? 110.179 92.051  95.665  1.00 36.34  ? 418 ILE A CB    1 
ATOM   3032 C  CG1   . ILE B 2 418 ? 109.204 93.001  94.966  1.00 41.12  ? 418 ILE A CG1   1 
ATOM   3033 C  CG2   . ILE B 2 418 ? 111.611 92.512  95.485  1.00 37.57  ? 418 ILE A CG2   1 
ATOM   3034 C  CD1   . ILE B 2 418 ? 108.871 94.222  95.776  1.00 39.60  ? 418 ILE A CD1   1 
ATOM   3035 N  N     . ALA B 2 419 ? 110.665 89.171  96.978  1.00 42.92  ? 419 ALA A N     1 
ATOM   3036 C  CA    . ALA B 2 419 ? 111.509 88.178  97.633  1.00 48.01  ? 419 ALA A CA    1 
ATOM   3037 C  C     . ALA B 2 419 ? 111.591 86.903  96.806  1.00 54.01  ? 419 ALA A C     1 
ATOM   3038 O  O     . ALA B 2 419 ? 112.664 86.308  96.664  1.00 56.51  ? 419 ALA A O     1 
ATOM   3039 C  CB    . ALA B 2 419 ? 110.975 87.879  99.031  1.00 43.63  ? 419 ALA A CB    1 
ATOM   3040 N  N     . ALA B 2 420 ? 110.458 86.460  96.256  1.00 54.13  ? 420 ALA A N     1 
ATOM   3041 C  CA    . ALA B 2 420 ? 110.464 85.255  95.436  1.00 50.32  ? 420 ALA A CA    1 
ATOM   3042 C  C     . ALA B 2 420 ? 111.394 85.408  94.238  1.00 53.91  ? 420 ALA A C     1 
ATOM   3043 O  O     . ALA B 2 420 ? 112.182 84.504  93.936  1.00 58.94  ? 420 ALA A O     1 
ATOM   3044 C  CB    . ALA B 2 420 ? 109.042 84.937  94.977  1.00 49.09  ? 420 ALA A CB    1 
ATOM   3045 N  N     . GLU B 2 421 ? 111.328 86.549  93.549  1.00 52.11  ? 421 GLU A N     1 
ATOM   3046 C  CA    . GLU B 2 421 ? 112.164 86.746  92.370  1.00 55.62  ? 421 GLU A CA    1 
ATOM   3047 C  C     . GLU B 2 421 ? 113.628 86.934  92.745  1.00 57.08  ? 421 GLU A C     1 
ATOM   3048 O  O     . GLU B 2 421 ? 114.521 86.480  92.022  1.00 60.79  ? 421 GLU A O     1 
ATOM   3049 C  CB    . GLU B 2 421 ? 111.663 87.941  91.564  1.00 52.69  ? 421 GLU A CB    1 
ATOM   3050 C  CG    . GLU B 2 421 ? 110.218 87.814  91.106  1.00 51.26  ? 421 GLU A CG    1 
ATOM   3051 C  CD    . GLU B 2 421 ? 110.009 88.287  89.678  1.00 60.32  ? 421 GLU A CD    1 
ATOM   3052 O  OE1   . GLU B 2 421 ? 111.000 88.640  89.005  1.00 67.00  ? 421 GLU A OE1   1 
ATOM   3053 O  OE2   . GLU B 2 421 ? 108.850 88.293  89.217  1.00 61.93  ? 421 GLU A OE2   1 
ATOM   3054 N  N     . ILE B 2 422 ? 113.898 87.611  93.861  1.00 52.52  ? 422 ILE A N     1 
ATOM   3055 C  CA    . ILE B 2 422 ? 115.278 87.777  94.303  1.00 52.89  ? 422 ILE A CA    1 
ATOM   3056 C  C     . ILE B 2 422 ? 115.879 86.428  94.677  1.00 60.03  ? 422 ILE A C     1 
ATOM   3057 O  O     . ILE B 2 422 ? 117.061 86.166  94.424  1.00 63.49  ? 422 ILE A O     1 
ATOM   3058 C  CB    . ILE B 2 422 ? 115.345 88.769  95.479  1.00 49.93  ? 422 ILE A CB    1 
ATOM   3059 C  CG1   . ILE B 2 422 ? 115.090 90.196  94.990  1.00 45.45  ? 422 ILE A CG1   1 
ATOM   3060 C  CG2   . ILE B 2 422 ? 116.695 88.678  96.179  1.00 57.94  ? 422 ILE A CG2   1 
ATOM   3061 C  CD1   . ILE B 2 422 ? 116.263 90.825  94.260  1.00 47.11  ? 422 ILE A CD1   1 
ATOM   3062 N  N     . THR B 2 423 ? 115.078 85.558  95.293  1.00 61.27  ? 423 THR A N     1 
ATOM   3063 C  CA    . THR B 2 423 ? 115.551 84.264  95.762  1.00 64.01  ? 423 THR A CA    1 
ATOM   3064 C  C     . THR B 2 423 ? 115.543 83.202  94.674  1.00 67.86  ? 423 THR A C     1 
ATOM   3065 O  O     . THR B 2 423 ? 116.222 82.180  94.821  1.00 71.60  ? 423 THR A O     1 
ATOM   3066 C  CB    . THR B 2 423 ? 114.679 83.784  96.923  1.00 66.63  ? 423 THR A CB    1 
ATOM   3067 O  OG1   . THR B 2 423 ? 113.297 83.994  96.606  1.00 64.43  ? 423 THR A OG1   1 
ATOM   3068 C  CG2   . THR B 2 423 ? 115.010 84.558  98.183  1.00 68.01  ? 423 THR A CG2   1 
ATOM   3069 N  N     . ASN B 2 424 ? 114.804 83.418  93.587  1.00 67.93  ? 424 ASN A N     1 
ATOM   3070 C  CA    . ASN B 2 424 ? 114.625 82.397  92.560  1.00 69.30  ? 424 ASN A CA    1 
ATOM   3071 C  C     . ASN B 2 424 ? 114.043 81.126  93.172  1.00 73.47  ? 424 ASN A C     1 
ATOM   3072 O  O     . ASN B 2 424 ? 114.354 80.007  92.759  1.00 78.39  ? 424 ASN A O     1 
ATOM   3073 C  CB    . ASN B 2 424 ? 115.944 82.101  91.844  1.00 70.66  ? 424 ASN A CB    1 
ATOM   3074 C  CG    . ASN B 2 424 ? 116.774 83.347  91.609  1.00 69.58  ? 424 ASN A CG    1 
ATOM   3075 O  OD1   . ASN B 2 424 ? 117.436 83.847  92.519  1.00 66.11  ? 424 ASN A OD1   1 
ATOM   3076 N  ND2   . ASN B 2 424 ? 116.742 83.858  90.383  1.00 73.51  ? 424 ASN A ND2   1 
ATOM   3077 N  N     . ASP B 2 425 ? 113.181 81.305  94.168  1.00 71.02  ? 425 ASP A N     1 
ATOM   3078 C  CA    . ASP B 2 425 ? 112.567 80.180  94.865  1.00 70.86  ? 425 ASP A CA    1 
ATOM   3079 C  C     . ASP B 2 425 ? 111.509 79.549  93.970  1.00 74.38  ? 425 ASP A C     1 
ATOM   3080 O  O     . ASP B 2 425 ? 110.478 80.165  93.683  1.00 75.31  ? 425 ASP A O     1 
ATOM   3081 C  CB    . ASP B 2 425 ? 111.964 80.651  96.183  1.00 64.46  ? 425 ASP A CB    1 
ATOM   3082 C  CG    . ASP B 2 425 ? 111.559 79.502  97.079  1.00 68.18  ? 425 ASP A CG    1 
ATOM   3083 O  OD1   . ASP B 2 425 ? 110.560 78.825  96.762  1.00 72.29  ? 425 ASP A OD1   1 
ATOM   3084 O  OD2   . ASP B 2 425 ? 112.240 79.276  98.100  1.00 70.95  ? 425 ASP A OD2   1 
ATOM   3085 N  N     . GLU B 2 426 ? 111.760 78.313  93.534  1.00 73.26  ? 426 GLU A N     1 
ATOM   3086 C  CA    . GLU B 2 426 ? 110.870 77.672  92.571  1.00 77.42  ? 426 GLU A CA    1 
ATOM   3087 C  C     . GLU B 2 426 ? 109.492 77.416  93.168  1.00 72.10  ? 426 GLU A C     1 
ATOM   3088 O  O     . GLU B 2 426 ? 108.472 77.630  92.503  1.00 69.17  ? 426 GLU A O     1 
ATOM   3089 C  CB    . GLU B 2 426 ? 111.483 76.362  92.069  1.00 87.72  ? 426 GLU A CB    1 
ATOM   3090 C  CG    . GLU B 2 426 ? 112.959 76.447  91.696  1.00 94.61  ? 426 GLU A CG    1 
ATOM   3091 C  CD    . GLU B 2 426 ? 113.183 77.071  90.333  1.00 102.12 ? 426 GLU A CD    1 
ATOM   3092 O  OE1   . GLU B 2 426 ? 112.208 77.194  89.562  1.00 100.63 ? 426 GLU A OE1   1 
ATOM   3093 O  OE2   . GLU B 2 426 ? 114.334 77.450  90.036  1.00 105.14 ? 426 GLU A OE2   1 
ATOM   3094 N  N     . ILE B 2 427 ? 109.441 76.954  94.417  1.00 66.96  ? 427 ILE A N     1 
ATOM   3095 C  CA    . ILE B 2 427 ? 108.159 76.617  95.026  1.00 65.88  ? 427 ILE A CA    1 
ATOM   3096 C  C     . ILE B 2 427 ? 107.326 77.873  95.249  1.00 69.26  ? 427 ILE A C     1 
ATOM   3097 O  O     . ILE B 2 427 ? 106.103 77.861  95.069  1.00 69.20  ? 427 ILE A O     1 
ATOM   3098 C  CB    . ILE B 2 427 ? 108.379 75.840  96.335  1.00 62.46  ? 427 ILE A CB    1 
ATOM   3099 C  CG1   . ILE B 2 427 ? 109.297 74.642  96.085  1.00 71.99  ? 427 ILE A CG1   1 
ATOM   3100 C  CG2   . ILE B 2 427 ? 107.052 75.367  96.899  1.00 57.53  ? 427 ILE A CG2   1 
ATOM   3101 C  CD1   . ILE B 2 427 ? 110.707 74.838  96.578  1.00 73.51  ? 427 ILE A CD1   1 
ATOM   3102 N  N     . MET B 2 428 ? 107.968 78.973  95.646  1.00 70.24  ? 428 MET A N     1 
ATOM   3103 C  CA    . MET B 2 428 ? 107.242 80.228  95.813  1.00 58.79  ? 428 MET A CA    1 
ATOM   3104 C  C     . MET B 2 428 ? 106.566 80.639  94.514  1.00 65.21  ? 428 MET A C     1 
ATOM   3105 O  O     . MET B 2 428 ? 105.356 80.894  94.480  1.00 66.94  ? 428 MET A O     1 
ATOM   3106 C  CB    . MET B 2 428 ? 108.198 81.325  96.279  1.00 57.27  ? 428 MET A CB    1 
ATOM   3107 C  CG    . MET B 2 428 ? 108.226 81.567  97.776  1.00 61.87  ? 428 MET A CG    1 
ATOM   3108 S  SD    . MET B 2 428 ? 106.701 82.321  98.377  1.00 67.39  ? 428 MET A SD    1 
ATOM   3109 C  CE    . MET B 2 428 ? 107.277 83.093  99.888  1.00 49.18  ? 428 MET A CE    1 
ATOM   3110 N  N     . LEU B 2 429 ? 107.334 80.691  93.424  1.00 66.70  ? 429 LEU A N     1 
ATOM   3111 C  CA    . LEU B 2 429 ? 106.780 81.129  92.147  1.00 63.53  ? 429 LEU A CA    1 
ATOM   3112 C  C     . LEU B 2 429 ? 105.722 80.159  91.644  1.00 66.06  ? 429 LEU A C     1 
ATOM   3113 O  O     . LEU B 2 429 ? 104.721 80.577  91.052  1.00 68.49  ? 429 LEU A O     1 
ATOM   3114 C  CB    . LEU B 2 429 ? 107.900 81.296  91.119  1.00 61.75  ? 429 LEU A CB    1 
ATOM   3115 C  CG    . LEU B 2 429 ? 109.083 82.156  91.572  1.00 59.03  ? 429 LEU A CG    1 
ATOM   3116 C  CD1   . LEU B 2 429 ? 110.319 81.890  90.734  1.00 60.28  ? 429 LEU A CD1   1 
ATOM   3117 C  CD2   . LEU B 2 429 ? 108.707 83.622  91.515  1.00 61.36  ? 429 LEU A CD2   1 
ATOM   3118 N  N     . LYS B 2 430 ? 105.922 78.859  91.870  1.00 62.48  ? 430 LYS A N     1 
ATOM   3119 C  CA    . LYS B 2 430 ? 104.904 77.888  91.489  1.00 62.93  ? 430 LYS A CA    1 
ATOM   3120 C  C     . LYS B 2 430 ? 103.606 78.131  92.247  1.00 65.00  ? 430 LYS A C     1 
ATOM   3121 O  O     . LYS B 2 430 ? 102.517 78.076  91.664  1.00 66.48  ? 430 LYS A O     1 
ATOM   3122 C  CB    . LYS B 2 430 ? 105.415 76.470  91.743  1.00 64.88  ? 430 LYS A CB    1 
ATOM   3123 C  CG    . LYS B 2 430 ? 104.729 75.404  90.905  1.00 65.36  ? 430 LYS A CG    1 
ATOM   3124 C  CD    . LYS B 2 430 ? 105.242 74.007  91.234  1.00 64.12  ? 430 LYS A CD    1 
ATOM   3125 C  CE    . LYS B 2 430 ? 104.878 73.573  92.650  1.00 62.46  ? 430 LYS A CE    1 
ATOM   3126 N  NZ    . LYS B 2 430 ? 103.477 73.906  93.021  1.00 66.12  ? 430 LYS A NZ    1 
ATOM   3127 N  N     . ALA B 2 431 ? 103.702 78.403  93.550  1.00 65.66  ? 431 ALA A N     1 
ATOM   3128 C  CA    . ALA B 2 431 ? 102.509 78.705  94.334  1.00 66.80  ? 431 ALA A CA    1 
ATOM   3129 C  C     . ALA B 2 431 ? 101.855 79.999  93.869  1.00 66.83  ? 431 ALA A C     1 
ATOM   3130 O  O     . ALA B 2 431 ? 100.624 80.096  93.815  1.00 66.83  ? 431 ALA A O     1 
ATOM   3131 C  CB    . ALA B 2 431 ? 102.864 78.791  95.817  1.00 61.44  ? 431 ALA A CB    1 
ATOM   3132 N  N     . TYR B 2 432 ? 102.663 81.006  93.536  1.00 66.19  ? 432 TYR A N     1 
ATOM   3133 C  CA    . TYR B 2 432 ? 102.108 82.271  93.070  1.00 63.04  ? 432 TYR A CA    1 
ATOM   3134 C  C     . TYR B 2 432 ? 101.338 82.076  91.773  1.00 65.11  ? 432 TYR A C     1 
ATOM   3135 O  O     . TYR B 2 432 ? 100.279 82.681  91.573  1.00 65.72  ? 432 TYR A O     1 
ATOM   3136 C  CB    . TYR B 2 432 ? 103.232 83.294  92.884  1.00 55.23  ? 432 TYR A CB    1 
ATOM   3137 C  CG    . TYR B 2 432 ? 103.668 83.978  94.162  1.00 51.64  ? 432 TYR A CG    1 
ATOM   3138 C  CD1   . TYR B 2 432 ? 102.778 84.189  95.206  1.00 51.88  ? 432 TYR A CD1   1 
ATOM   3139 C  CD2   . TYR B 2 432 ? 104.984 84.390  94.335  1.00 49.59  ? 432 TYR A CD2   1 
ATOM   3140 C  CE1   . TYR B 2 432 ? 103.173 84.797  96.363  1.00 47.29  ? 432 TYR A CE1   1 
ATOM   3141 C  CE2   . TYR B 2 432 ? 105.388 85.001  95.500  1.00 45.79  ? 432 TYR A CE2   1 
ATOM   3142 C  CZ    . TYR B 2 432 ? 104.476 85.199  96.511  1.00 46.17  ? 432 TYR A CZ    1 
ATOM   3143 O  OH    . TYR B 2 432 ? 104.861 85.808  97.679  1.00 53.22  ? 432 TYR A OH    1 
ATOM   3144 N  N     . ASN B 2 433 ? 101.851 81.227  90.881  1.00 67.30  ? 433 ASN A N     1 
ATOM   3145 C  CA    . ASN B 2 433 ? 101.127 80.913  89.658  1.00 71.36  ? 433 ASN A CA    1 
ATOM   3146 C  C     . ASN B 2 433 ? 99.803  80.219  89.943  1.00 73.83  ? 433 ASN A C     1 
ATOM   3147 O  O     . ASN B 2 433 ? 98.917  80.226  89.083  1.00 77.91  ? 433 ASN A O     1 
ATOM   3148 C  CB    . ASN B 2 433 ? 101.990 80.036  88.750  1.00 71.88  ? 433 ASN A CB    1 
ATOM   3149 C  CG    . ASN B 2 433 ? 103.257 80.734  88.301  1.00 68.72  ? 433 ASN A CG    1 
ATOM   3150 O  OD1   . ASN B 2 433 ? 103.292 81.957  88.171  1.00 63.82  ? 433 ASN A OD1   1 
ATOM   3151 N  ND2   . ASN B 2 433 ? 104.306 79.958  88.054  1.00 66.35  ? 433 ASN A ND2   1 
ATOM   3152 N  N     . ASN B 2 434 ? 99.646  79.630  91.127  1.00 70.15  ? 434 ASN A N     1 
ATOM   3153 C  CA    . ASN B 2 434 ? 98.406  78.970  91.511  1.00 71.14  ? 434 ASN A CA    1 
ATOM   3154 C  C     . ASN B 2 434 ? 97.451  79.890  92.261  1.00 69.50  ? 434 ASN A C     1 
ATOM   3155 O  O     . ASN B 2 434 ? 96.343  79.461  92.600  1.00 70.71  ? 434 ASN A O     1 
ATOM   3156 C  CB    . ASN B 2 434 ? 98.714  77.741  92.374  1.00 70.18  ? 434 ASN A CB    1 
ATOM   3157 C  CG    . ASN B 2 434 ? 99.152  76.547  91.551  1.00 67.12  ? 434 ASN A CG    1 
ATOM   3158 O  OD1   . ASN B 2 434 ? 100.138 76.613  90.817  1.00 67.63  ? 434 ASN A OD1   1 
ATOM   3159 N  ND2   . ASN B 2 434 ? 98.414  75.449  91.661  1.00 65.06  ? 434 ASN A ND2   1 
ATOM   3160 N  N     . ASN B 2 435 ? 97.846  81.134  92.528  1.00 68.86  ? 435 ASN A N     1 
ATOM   3161 C  CA    . ASN B 2 435 ? 96.980  82.122  93.170  1.00 71.03  ? 435 ASN A CA    1 
ATOM   3162 C  C     . ASN B 2 435 ? 96.550  81.658  94.564  1.00 72.64  ? 435 ASN A C     1 
ATOM   3163 O  O     . ASN B 2 435 ? 95.366  81.474  94.854  1.00 77.93  ? 435 ASN A O     1 
ATOM   3164 C  CB    . ASN B 2 435 ? 95.759  82.422  92.294  1.00 69.80  ? 435 ASN A CB    1 
ATOM   3165 C  CG    . ASN B 2 435 ? 96.135  83.055  90.973  1.00 70.69  ? 435 ASN A CG    1 
ATOM   3166 O  OD1   . ASN B 2 435 ? 96.581  82.373  90.050  1.00 69.94  ? 435 ASN A OD1   1 
ATOM   3167 N  ND2   . ASN B 2 435 ? 95.958  84.368  90.873  1.00 66.08  ? 435 ASN A ND2   1 
ATOM   3168 N  N     . ILE B 2 436 ? 97.543  81.470  95.430  1.00 69.91  ? 436 ILE A N     1 
ATOM   3169 C  CA    . ILE B 2 436 ? 97.319  81.143  96.834  1.00 66.84  ? 436 ILE A CA    1 
ATOM   3170 C  C     . ILE B 2 436 ? 98.131  82.110  97.684  1.00 66.78  ? 436 ILE A C     1 
ATOM   3171 O  O     . ILE B 2 436 ? 99.322  82.319  97.428  1.00 69.53  ? 436 ILE A O     1 
ATOM   3172 C  CB    . ILE B 2 436 ? 97.699  79.685  97.154  1.00 68.99  ? 436 ILE A CB    1 
ATOM   3173 C  CG1   . ILE B 2 436 ? 99.042  79.328  96.510  1.00 70.60  ? 436 ILE A CG1   1 
ATOM   3174 C  CG2   . ILE B 2 436 ? 96.600  78.747  96.676  1.00 70.19  ? 436 ILE A CG2   1 
ATOM   3175 C  CD1   . ILE B 2 436 ? 99.626  78.009  96.985  1.00 68.07  ? 436 ILE A CD1   1 
ATOM   3176 N  N     . ASP B 2 437 ? 97.489  82.695  98.692  1.00 65.17  ? 437 ASP A N     1 
ATOM   3177 C  CA    . ASP B 2 437 ? 98.145  83.692  99.528  1.00 58.01  ? 437 ASP A CA    1 
ATOM   3178 C  C     . ASP B 2 437 ? 99.159  83.035  100.454 1.00 56.90  ? 437 ASP A C     1 
ATOM   3179 O  O     . ASP B 2 437 ? 98.846  82.060  101.143 1.00 62.74  ? 437 ASP A O     1 
ATOM   3180 C  CB    . ASP B 2 437 ? 97.106  84.451  100.354 1.00 59.18  ? 437 ASP A CB    1 
ATOM   3181 C  CG    . ASP B 2 437 ? 96.708  85.773  99.729  1.00 70.61  ? 437 ASP A CG    1 
ATOM   3182 O  OD1   . ASP B 2 437 ? 97.393  86.230  98.790  1.00 68.62  ? 437 ASP A OD1   1 
ATOM   3183 O  OD2   . ASP B 2 437 ? 95.702  86.357  100.182 1.00 76.92  ? 437 ASP A OD2   1 
ATOM   3184 N  N     . LEU B 2 438 ? 100.380 83.573  100.472 1.00 53.98  ? 438 LEU A N     1 
ATOM   3185 C  CA    . LEU B 2 438 ? 101.363 83.114  101.448 1.00 56.47  ? 438 LEU A CA    1 
ATOM   3186 C  C     . LEU B 2 438 ? 100.941 83.491  102.860 1.00 56.03  ? 438 LEU A C     1 
ATOM   3187 O  O     . LEU B 2 438 ? 101.114 82.706  103.798 1.00 57.96  ? 438 LEU A O     1 
ATOM   3188 C  CB    . LEU B 2 438 ? 102.736 83.708  101.139 1.00 53.88  ? 438 LEU A CB    1 
ATOM   3189 C  CG    . LEU B 2 438 ? 103.628 82.924  100.179 1.00 52.11  ? 438 LEU A CG    1 
ATOM   3190 C  CD1   . LEU B 2 438 ? 104.399 81.870  100.945 1.00 55.16  ? 438 LEU A CD1   1 
ATOM   3191 C  CD2   . LEU B 2 438 ? 102.817 82.289  99.059  1.00 52.94  ? 438 LEU A CD2   1 
ATOM   3192 N  N     . HIS B 2 439 ? 100.397 84.697  103.032 1.00 52.43  ? 439 HIS A N     1 
ATOM   3193 C  CA    . HIS B 2 439 ? 99.959  85.126  104.354 1.00 49.73  ? 439 HIS A CA    1 
ATOM   3194 C  C     . HIS B 2 439 ? 98.843  84.232  104.870 1.00 54.57  ? 439 HIS A C     1 
ATOM   3195 O  O     . HIS B 2 439 ? 98.834  83.853  106.046 1.00 60.74  ? 439 HIS A O     1 
ATOM   3196 C  CB    . HIS B 2 439 ? 99.506  86.584  104.307 1.00 51.73  ? 439 HIS A CB    1 
ATOM   3197 C  CG    . HIS B 2 439 ? 100.564 87.531  103.830 1.00 47.17  ? 439 HIS A CG    1 
ATOM   3198 N  ND1   . HIS B 2 439 ? 101.904 87.343  104.085 1.00 46.88  ? 439 HIS A ND1   1 
ATOM   3199 C  CD2   . HIS B 2 439 ? 100.476 88.672  103.106 1.00 41.87  ? 439 HIS A CD2   1 
ATOM   3200 C  CE1   . HIS B 2 439 ? 102.597 88.329  103.545 1.00 40.28  ? 439 HIS A CE1   1 
ATOM   3201 N  NE2   . HIS B 2 439 ? 101.754 89.148  102.944 1.00 40.61  ? 439 HIS A NE2   1 
ATOM   3202 N  N     . THR B 2 440 ? 97.899  83.870  104.003 1.00 54.89  ? 440 THR A N     1 
ATOM   3203 C  CA    . THR B 2 440 ? 96.821  82.984  104.425 1.00 61.67  ? 440 THR A CA    1 
ATOM   3204 C  C     . THR B 2 440 ? 97.354  81.600  104.774 1.00 61.24  ? 440 THR A C     1 
ATOM   3205 O  O     . THR B 2 440 ? 96.848  80.947  105.694 1.00 64.91  ? 440 THR A O     1 
ATOM   3206 C  CB    . THR B 2 440 ? 95.763  82.891  103.329 1.00 65.35  ? 440 THR A CB    1 
ATOM   3207 O  OG1   . THR B 2 440 ? 95.382  84.210  102.919 1.00 58.51  ? 440 THR A OG1   1 
ATOM   3208 C  CG2   . THR B 2 440 ? 94.535  82.158  103.838 1.00 72.60  ? 440 THR A CG2   1 
ATOM   3209 N  N     . LEU B 2 441 ? 98.369  81.132  104.046 1.00 58.60  ? 441 LEU A N     1 
ATOM   3210 C  CA    . LEU B 2 441 ? 98.960  79.831  104.347 1.00 59.96  ? 441 LEU A CA    1 
ATOM   3211 C  C     . LEU B 2 441 ? 99.663  79.851  105.700 1.00 61.98  ? 441 LEU A C     1 
ATOM   3212 O  O     . LEU B 2 441 ? 99.426  78.982  106.547 1.00 62.92  ? 441 LEU A O     1 
ATOM   3213 C  CB    . LEU B 2 441 ? 99.935  79.436  103.233 1.00 55.80  ? 441 LEU A CB    1 
ATOM   3214 C  CG    . LEU B 2 441 ? 100.845 78.223  103.460 1.00 55.62  ? 441 LEU A CG    1 
ATOM   3215 C  CD1   . LEU B 2 441 ? 100.133 76.941  103.069 1.00 58.71  ? 441 LEU A CD1   1 
ATOM   3216 C  CD2   . LEU B 2 441 ? 102.137 78.385  102.680 1.00 53.51  ? 441 LEU A CD2   1 
ATOM   3217 N  N     . THR B 2 442 ? 100.528 80.841  105.923 1.00 56.71  ? 442 THR A N     1 
ATOM   3218 C  CA    . THR B 2 442 ? 101.206 80.961  107.209 1.00 55.86  ? 442 THR A CA    1 
ATOM   3219 C  C     . THR B 2 442 ? 100.231 81.257  108.337 1.00 55.28  ? 442 THR A C     1 
ATOM   3220 O  O     . THR B 2 442 ? 100.573 81.054  109.506 1.00 57.45  ? 442 THR A O     1 
ATOM   3221 C  CB    . THR B 2 442 ? 102.279 82.048  107.139 1.00 54.68  ? 442 THR A CB    1 
ATOM   3222 O  OG1   . THR B 2 442 ? 103.005 81.921  105.911 1.00 55.99  ? 442 THR A OG1   1 
ATOM   3223 C  CG2   . THR B 2 442 ? 103.243 81.934  108.308 1.00 50.05  ? 442 THR A CG2   1 
ATOM   3224 N  N     . ALA B 2 443 ? 99.031  81.739  108.017 1.00 52.97  ? 443 ALA A N     1 
ATOM   3225 C  CA    . ALA B 2 443 ? 97.970  81.804  109.013 1.00 53.65  ? 443 ALA A CA    1 
ATOM   3226 C  C     . ALA B 2 443 ? 97.431  80.412  109.315 1.00 62.03  ? 443 ALA A C     1 
ATOM   3227 O  O     . ALA B 2 443 ? 97.507  79.933  110.452 1.00 66.34  ? 443 ALA A O     1 
ATOM   3228 C  CB    . ALA B 2 443 ? 96.846  82.718  108.523 1.00 54.97  ? 443 ALA A CB    1 
ATOM   3229 N  N     . SER B 2 444 ? 96.900  79.736  108.294 1.00 65.85  ? 444 SER A N     1 
ATOM   3230 C  CA    . SER B 2 444 ? 96.218  78.465  108.506 1.00 68.61  ? 444 SER A CA    1 
ATOM   3231 C  C     . SER B 2 444 ? 97.127  77.400  109.104 1.00 64.18  ? 444 SER A C     1 
ATOM   3232 O  O     . SER B 2 444 ? 96.634  76.504  109.796 1.00 65.22  ? 444 SER A O     1 
ATOM   3233 C  CB    . SER B 2 444 ? 95.635  77.962  107.184 1.00 74.57  ? 444 SER A CB    1 
ATOM   3234 O  OG    . SER B 2 444 ? 95.048  76.682  107.340 1.00 76.85  ? 444 SER A OG    1 
ATOM   3235 N  N     . ILE B 2 445 ? 98.438  77.477  108.868 1.00 61.93  ? 445 ILE A N     1 
ATOM   3236 C  CA    . ILE B 2 445 ? 99.341  76.472  109.425 1.00 63.82  ? 445 ILE A CA    1 
ATOM   3237 C  C     . ILE B 2 445 ? 99.308  76.517  110.948 1.00 64.36  ? 445 ILE A C     1 
ATOM   3238 O  O     . ILE B 2 445 ? 99.244  75.475  111.612 1.00 65.68  ? 445 ILE A O     1 
ATOM   3239 C  CB    . ILE B 2 445 ? 100.770 76.667  108.884 1.00 61.43  ? 445 ILE A CB    1 
ATOM   3240 C  CG1   . ILE B 2 445 ? 101.702 75.589  109.443 1.00 62.91  ? 445 ILE A CG1   1 
ATOM   3241 C  CG2   . ILE B 2 445 ? 101.310 78.034  109.255 1.00 61.40  ? 445 ILE A CG2   1 
ATOM   3242 C  CD1   . ILE B 2 445 ? 102.887 75.283  108.548 1.00 61.15  ? 445 ILE A CD1   1 
ATOM   3243 N  N     . ILE B 2 446 ? 99.348  77.719  111.528 1.00 61.23  ? 446 ILE A N     1 
ATOM   3244 C  CA    . ILE B 2 446 ? 99.195  77.878  112.972 1.00 57.96  ? 446 ILE A CA    1 
ATOM   3245 C  C     . ILE B 2 446 ? 98.111  78.906  113.279 1.00 60.46  ? 446 ILE A C     1 
ATOM   3246 O  O     . ILE B 2 446 ? 98.396  80.088  113.491 1.00 54.51  ? 446 ILE A O     1 
ATOM   3247 C  CB    . ILE B 2 446 ? 100.541 78.269  113.614 1.00 54.32  ? 446 ILE A CB    1 
ATOM   3248 C  CG1   . ILE B 2 446 ? 101.126 79.525  112.953 1.00 46.71  ? 446 ILE A CG1   1 
ATOM   3249 C  CG2   . ILE B 2 446 ? 101.521 77.116  113.520 1.00 60.78  ? 446 ILE A CG2   1 
ATOM   3250 C  CD1   . ILE B 2 446 ? 102.392 80.016  113.605 1.00 48.48  ? 446 ILE A CD1   1 
ATOM   3251 N  N     . THR B 2 447 ? 96.864  78.449  113.347 1.00 67.61  ? 447 THR A N     1 
ATOM   3252 C  CA    . THR B 2 447 ? 95.727  79.277  113.742 1.00 74.88  ? 447 THR A CA    1 
ATOM   3253 C  C     . THR B 2 447 ? 94.474  78.408  113.683 1.00 86.13  ? 447 THR A C     1 
ATOM   3254 O  O     . THR B 2 447 ? 94.557  77.178  113.608 1.00 84.92  ? 447 THR A O     1 
ATOM   3255 C  CB    . THR B 2 447 ? 95.588  80.517  112.852 1.00 75.96  ? 447 THR A CB    1 
ATOM   3256 O  OG1   . THR B 2 447 ? 94.767  81.487  113.512 1.00 79.44  ? 447 THR A OG1   1 
ATOM   3257 C  CG2   . THR B 2 447 ? 94.948  80.155  111.524 1.00 80.11  ? 447 THR A CG2   1 
ATOM   3258 N  N     . LYS B 2 448 ? 93.309  79.052  113.722 1.00 92.48  ? 448 LYS A N     1 
ATOM   3259 C  CA    . LYS B 2 448 ? 92.049  78.365  113.458 1.00 96.47  ? 448 LYS A CA    1 
ATOM   3260 C  C     . LYS B 2 448 ? 92.146  77.598  112.145 1.00 95.71  ? 448 LYS A C     1 
ATOM   3261 O  O     . LYS B 2 448 ? 92.662  78.109  111.147 1.00 93.01  ? 448 LYS A O     1 
ATOM   3262 C  CB    . LYS B 2 448 ? 90.875  79.358  113.408 1.00 96.77  ? 448 LYS A CB    1 
ATOM   3263 C  CG    . LYS B 2 448 ? 90.962  80.560  114.361 1.00 93.33  ? 448 LYS A CG    1 
ATOM   3264 C  CD    . LYS B 2 448 ? 90.593  80.164  115.784 1.00 97.76  ? 448 LYS A CD    1 
ATOM   3265 C  CE    . LYS B 2 448 ? 90.522  81.369  116.713 1.00 98.07  ? 448 LYS A CE    1 
ATOM   3266 N  NZ    . LYS B 2 448 ? 89.770  82.512  116.134 1.00 93.57  ? 448 LYS A NZ    1 
ATOM   3267 N  N     . LYS B 2 449 ? 91.656  76.362  112.157 1.00 96.79  ? 449 LYS A N     1 
ATOM   3268 C  CA    . LYS B 2 449 ? 91.901  75.446  111.056 1.00 100.06 ? 449 LYS A CA    1 
ATOM   3269 C  C     . LYS B 2 449 ? 91.253  75.946  109.764 1.00 103.90 ? 449 LYS A C     1 
ATOM   3270 O  O     . LYS B 2 449 ? 90.456  76.886  109.748 1.00 105.34 ? 449 LYS A O     1 
ATOM   3271 C  CB    . LYS B 2 449 ? 91.382  74.050  111.403 1.00 99.33  ? 449 LYS A CB    1 
ATOM   3272 C  CG    . LYS B 2 449 ? 92.132  73.363  112.538 1.00 97.83  ? 449 LYS A CG    1 
ATOM   3273 C  CD    . LYS B 2 449 ? 93.621  73.219  112.244 1.00 94.44  ? 449 LYS A CD    1 
ATOM   3274 C  CE    . LYS B 2 449 ? 94.460  73.934  113.286 1.00 88.79  ? 449 LYS A CE    1 
ATOM   3275 N  NZ    . LYS B 2 449 ? 95.897  73.991  112.909 1.00 83.67  ? 449 LYS A NZ    1 
ATOM   3276 N  N     . ASN B 2 450 ? 91.628  75.289  108.663 1.00 104.13 ? 450 ASN A N     1 
ATOM   3277 C  CA    . ASN B 2 450 ? 91.108  75.580  107.331 1.00 102.95 ? 450 ASN A CA    1 
ATOM   3278 C  C     . ASN B 2 450 ? 91.603  76.928  106.818 1.00 95.83  ? 450 ASN A C     1 
ATOM   3279 O  O     . ASN B 2 450 ? 91.925  77.824  107.605 1.00 92.61  ? 450 ASN A O     1 
ATOM   3280 C  CB    . ASN B 2 450 ? 89.578  75.543  107.329 1.00 105.16 ? 450 ASN A CB    1 
ATOM   3281 C  CG    . ASN B 2 450 ? 89.022  74.362  108.096 1.00 105.56 ? 450 ASN A CG    1 
ATOM   3282 O  OD1   . ASN B 2 450 ? 88.226  74.525  109.020 1.00 107.89 ? 450 ASN A OD1   1 
ATOM   3283 N  ND2   . ASN B 2 450 ? 89.439  73.161  107.714 1.00 101.46 ? 450 ASN A ND2   1 
ATOM   3284 N  N     . ILE B 2 451 ? 91.668  77.071  105.498 1.00 93.21  ? 451 ILE A N     1 
ATOM   3285 C  CA    . ILE B 2 451 ? 92.169  78.283  104.853 1.00 92.93  ? 451 ILE A CA    1 
ATOM   3286 C  C     . ILE B 2 451 ? 91.092  79.364  104.817 1.00 96.38  ? 451 ILE A C     1 
ATOM   3287 O  O     . ILE B 2 451 ? 91.368  80.509  105.203 1.00 97.93  ? 451 ILE A O     1 
ATOM   3288 C  CB    . ILE B 2 451 ? 92.680  77.977  103.435 1.00 85.69  ? 451 ILE A CB    1 
ATOM   3289 C  CG1   . ILE B 2 451 ? 94.110  77.428  103.480 1.00 81.61  ? 451 ILE A CG1   1 
ATOM   3290 C  CG2   . ILE B 2 451 ? 92.639  79.225  102.562 1.00 81.13  ? 451 ILE A CG2   1 
ATOM   3291 C  CD1   . ILE B 2 451 ? 95.174  78.460  103.803 1.00 65.84  ? 451 ILE A CD1   1 
ATOM   3292 N  N     . PRO B 2 452 ? 89.867  79.074  104.363 1.00 96.85  ? 452 PRO A N     1 
ATOM   3293 C  CA    . PRO B 2 452 ? 88.897  80.162  104.152 1.00 97.48  ? 452 PRO A CA    1 
ATOM   3294 C  C     . PRO B 2 452 ? 88.432  80.850  105.427 1.00 98.32  ? 452 PRO A C     1 
ATOM   3295 O  O     . PRO B 2 452 ? 87.739  81.872  105.330 1.00 95.77  ? 452 PRO A O     1 
ATOM   3296 C  CB    . PRO B 2 452 ? 87.731  79.458  103.445 1.00 99.53  ? 452 PRO A CB    1 
ATOM   3297 C  CG    . PRO B 2 452 ? 87.843  78.043  103.866 1.00 98.58  ? 452 PRO A CG    1 
ATOM   3298 C  CD    . PRO B 2 452 ? 89.313  77.775  103.938 1.00 94.30  ? 452 PRO A CD    1 
ATOM   3299 N  N     . ASP B 2 453 ? 88.784  80.341  106.610 1.00 100.37 ? 453 ASP A N     1 
ATOM   3300 C  CA    . ASP B 2 453 ? 88.348  80.931  107.871 1.00 100.57 ? 453 ASP A CA    1 
ATOM   3301 C  C     . ASP B 2 453 ? 89.314  81.988  108.396 1.00 97.16  ? 453 ASP A C     1 
ATOM   3302 O  O     . ASP B 2 453 ? 89.355  82.237  109.609 1.00 97.01  ? 453 ASP A O     1 
ATOM   3303 C  CB    . ASP B 2 453 ? 88.137  79.836  108.918 1.00 102.82 ? 453 ASP A CB    1 
ATOM   3304 C  CG    . ASP B 2 453 ? 87.184  78.754  108.448 1.00 103.94 ? 453 ASP A CG    1 
ATOM   3305 O  OD1   . ASP B 2 453 ? 86.122  79.102  107.891 1.00 104.67 ? 453 ASP A OD1   1 
ATOM   3306 O  OD2   . ASP B 2 453 ? 87.485  77.559  108.649 1.00 103.46 ? 453 ASP A OD2   1 
ATOM   3307 N  N     . ILE B 2 454 ? 90.086  82.621  107.518 1.00 95.09  ? 454 ILE A N     1 
ATOM   3308 C  CA    . ILE B 2 454 ? 91.011  83.686  107.893 1.00 92.12  ? 454 ILE A CA    1 
ATOM   3309 C  C     . ILE B 2 454 ? 90.322  85.027  107.691 1.00 90.36  ? 454 ILE A C     1 
ATOM   3310 O  O     . ILE B 2 454 ? 89.800  85.311  106.605 1.00 89.63  ? 454 ILE A O     1 
ATOM   3311 C  CB    . ILE B 2 454 ? 92.312  83.608  107.075 1.00 89.09  ? 454 ILE A CB    1 
ATOM   3312 C  CG1   . ILE B 2 454 ? 93.030  82.277  107.322 1.00 84.70  ? 454 ILE A CG1   1 
ATOM   3313 C  CG2   . ILE B 2 454 ? 93.215  84.786  107.397 1.00 83.83  ? 454 ILE A CG2   1 
ATOM   3314 C  CD1   . ILE B 2 454 ? 93.224  81.939  108.787 1.00 74.89  ? 454 ILE A CD1   1 
ATOM   3315 N  N     . ASN B 2 455 ? 90.316  85.851  108.737 1.00 88.01  ? 455 ASN A N     1 
ATOM   3316 C  CA    . ASN B 2 455 ? 89.755  87.189  108.686 1.00 88.39  ? 455 ASN A CA    1 
ATOM   3317 C  C     . ASN B 2 455 ? 90.884  88.214  108.567 1.00 83.41  ? 455 ASN A C     1 
ATOM   3318 O  O     . ASN B 2 455 ? 92.058  87.865  108.404 1.00 79.79  ? 455 ASN A O     1 
ATOM   3319 C  CB    . ASN B 2 455 ? 88.876  87.436  109.915 1.00 86.77  ? 455 ASN A CB    1 
ATOM   3320 C  CG    . ASN B 2 455 ? 89.645  87.326  111.218 1.00 84.87  ? 455 ASN A CG    1 
ATOM   3321 O  OD1   . ASN B 2 455 ? 90.874  87.327  111.229 1.00 81.63  ? 455 ASN A OD1   1 
ATOM   3322 N  ND2   . ASN B 2 455 ? 88.920  87.226  112.327 1.00 89.44  ? 455 ASN A ND2   1 
ATOM   3323 N  N     . LYS B 2 456 ? 90.526  89.498  108.642 1.00 83.92  ? 456 LYS A N     1 
ATOM   3324 C  CA    . LYS B 2 456 ? 91.516  90.553  108.447 1.00 82.31  ? 456 LYS A CA    1 
ATOM   3325 C  C     . LYS B 2 456 ? 92.571  90.544  109.547 1.00 79.51  ? 456 LYS A C     1 
ATOM   3326 O  O     . LYS B 2 456 ? 93.765  90.685  109.266 1.00 74.63  ? 456 LYS A O     1 
ATOM   3327 C  CB    . LYS B 2 456 ? 90.827  91.918  108.379 1.00 82.62  ? 456 LYS A CB    1 
ATOM   3328 C  CG    . LYS B 2 456 ? 89.791  92.092  107.257 1.00 84.39  ? 456 LYS A CG    1 
ATOM   3329 C  CD    . LYS B 2 456 ? 90.213  91.502  105.908 1.00 89.18  ? 456 LYS A CD    1 
ATOM   3330 C  CE    . LYS B 2 456 ? 91.082  92.468  105.121 1.00 94.35  ? 456 LYS A CE    1 
ATOM   3331 N  NZ    . LYS B 2 456 ? 91.579  91.868  103.852 1.00 90.71  ? 456 LYS A NZ    1 
ATOM   3332 N  N     . GLU B 2 457 ? 92.155  90.393  110.806 1.00 80.84  ? 457 GLU A N     1 
ATOM   3333 C  CA    . GLU B 2 457 ? 93.127  90.362  111.895 1.00 77.88  ? 457 GLU A CA    1 
ATOM   3334 C  C     . GLU B 2 457 ? 94.035  89.141  111.790 1.00 76.22  ? 457 GLU A C     1 
ATOM   3335 O  O     . GLU B 2 457 ? 95.246  89.235  112.032 1.00 72.02  ? 457 GLU A O     1 
ATOM   3336 C  CB    . GLU B 2 457 ? 92.404  90.379  113.240 1.00 78.53  ? 457 GLU A CB    1 
ATOM   3337 C  CG    . GLU B 2 457 ? 91.644  91.665  113.521 1.00 78.05  ? 457 GLU A CG    1 
ATOM   3338 C  CD    . GLU B 2 457 ? 90.268  91.682  112.882 1.00 78.52  ? 457 GLU A CD    1 
ATOM   3339 O  OE1   . GLU B 2 457 ? 89.954  90.744  112.120 1.00 79.71  ? 457 GLU A OE1   1 
ATOM   3340 O  OE2   . GLU B 2 457 ? 89.500  92.632  113.141 1.00 74.12  ? 457 GLU A OE2   1 
ATOM   3341 N  N     . ASP B 2 458 ? 93.463  87.984  111.448 1.00 79.11  ? 458 ASP A N     1 
ATOM   3342 C  CA    . ASP B 2 458 ? 94.273  86.788  111.246 1.00 76.12  ? 458 ASP A CA    1 
ATOM   3343 C  C     . ASP B 2 458 ? 95.270  86.997  110.118 1.00 69.89  ? 458 ASP A C     1 
ATOM   3344 O  O     . ASP B 2 458 ? 96.449  86.642  110.237 1.00 65.52  ? 458 ASP A O     1 
ATOM   3345 C  CB    . ASP B 2 458 ? 93.368  85.597  110.933 1.00 80.17  ? 458 ASP A CB    1 
ATOM   3346 C  CG    . ASP B 2 458 ? 92.899  84.877  112.173 1.00 84.08  ? 458 ASP A CG    1 
ATOM   3347 O  OD1   . ASP B 2 458 ? 93.679  84.801  113.137 1.00 82.66  ? 458 ASP A OD1   1 
ATOM   3348 O  OD2   . ASP B 2 458 ? 91.749  84.388  112.181 1.00 90.05  ? 458 ASP A OD2   1 
ATOM   3349 N  N     . ARG B 2 459 ? 94.812  87.581  109.012 1.00 70.91  ? 459 ARG A N     1 
ATOM   3350 C  CA    . ARG B 2 459 ? 95.715  87.853  107.903 1.00 68.32  ? 459 ARG A CA    1 
ATOM   3351 C  C     . ARG B 2 459 ? 96.808  88.827  108.318 1.00 64.25  ? 459 ARG A C     1 
ATOM   3352 O  O     . ARG B 2 459 ? 97.956  88.694  107.891 1.00 61.60  ? 459 ARG A O     1 
ATOM   3353 C  CB    . ARG B 2 459 ? 94.921  88.384  106.710 1.00 71.71  ? 459 ARG A CB    1 
ATOM   3354 C  CG    . ARG B 2 459 ? 95.537  88.047  105.362 1.00 63.29  ? 459 ARG A CG    1 
ATOM   3355 C  CD    . ARG B 2 459 ? 94.959  88.921  104.266 1.00 62.33  ? 459 ARG A CD    1 
ATOM   3356 N  NE    . ARG B 2 459 ? 95.596  88.671  102.979 1.00 62.46  ? 459 ARG A NE    1 
ATOM   3357 C  CZ    . ARG B 2 459 ? 96.803  89.107  102.647 1.00 54.33  ? 459 ARG A CZ    1 
ATOM   3358 N  NH1   . ARG B 2 459 ? 97.521  89.850  103.473 1.00 46.61  ? 459 ARG A NH1   1 
ATOM   3359 N  NH2   . ARG B 2 459 ? 97.299  88.797  101.454 1.00 52.60  ? 459 ARG A NH2   1 
ATOM   3360 N  N     . HIS B 2 460 ? 96.480  89.793  109.176 1.00 61.79  ? 460 HIS A N     1 
ATOM   3361 C  CA    . HIS B 2 460 ? 97.470  90.782  109.593 1.00 57.96  ? 460 HIS A CA    1 
ATOM   3362 C  C     . HIS B 2 460 ? 98.541  90.152  110.478 1.00 58.42  ? 460 HIS A C     1 
ATOM   3363 O  O     . HIS B 2 460 ? 99.741  90.398  110.294 1.00 57.66  ? 460 HIS A O     1 
ATOM   3364 C  CB    . HIS B 2 460 ? 96.778  91.927  110.329 1.00 62.43  ? 460 HIS A CB    1 
ATOM   3365 C  CG    . HIS B 2 460 ? 97.632  93.146  110.497 1.00 65.06  ? 460 HIS A CG    1 
ATOM   3366 N  ND1   . HIS B 2 460 ? 99.008  93.091  110.578 1.00 64.45  ? 460 HIS A ND1   1 
ATOM   3367 C  CD2   . HIS B 2 460 ? 97.301  94.452  110.625 1.00 62.69  ? 460 HIS A CD2   1 
ATOM   3368 C  CE1   . HIS B 2 460 ? 99.487  94.313  110.728 1.00 62.89  ? 460 HIS A CE1   1 
ATOM   3369 N  NE2   . HIS B 2 460 ? 98.472  95.157  110.763 1.00 59.67  ? 460 HIS A NE2   1 
ATOM   3370 N  N     . ILE B 2 461 ? 98.131  89.349  111.462 1.00 58.38  ? 461 ILE A N     1 
ATOM   3371 C  CA    . ILE B 2 461 ? 99.124  88.722  112.332 1.00 56.05  ? 461 ILE A CA    1 
ATOM   3372 C  C     . ILE B 2 461 ? 99.966  87.730  111.537 1.00 57.08  ? 461 ILE A C     1 
ATOM   3373 O  O     . ILE B 2 461 ? 101.177 87.601  111.758 1.00 58.71  ? 461 ILE A O     1 
ATOM   3374 C  CB    . ILE B 2 461 ? 98.456  88.062  113.554 1.00 54.72  ? 461 ILE A CB    1 
ATOM   3375 C  CG1   . ILE B 2 461 ? 97.409  87.036  113.130 1.00 60.83  ? 461 ILE A CG1   1 
ATOM   3376 C  CG2   . ILE B 2 461 ? 97.815  89.113  114.435 1.00 50.39  ? 461 ILE A CG2   1 
ATOM   3377 C  CD1   . ILE B 2 461 ? 97.808  85.603  113.405 1.00 51.27  ? 461 ILE A CD1   1 
ATOM   3378 N  N     . ALA B 2 462 ? 99.350  87.030  110.580 1.00 54.10  ? 462 ALA A N     1 
ATOM   3379 C  CA    . ALA B 2 462 ? 100.131 86.150  109.719 1.00 51.56  ? 462 ALA A CA    1 
ATOM   3380 C  C     . ALA B 2 462 ? 101.089 86.940  108.839 1.00 46.49  ? 462 ALA A C     1 
ATOM   3381 O  O     . ALA B 2 462 ? 102.196 86.475  108.557 1.00 47.98  ? 462 ALA A O     1 
ATOM   3382 C  CB    . ALA B 2 462 ? 99.199  85.300  108.863 1.00 59.32  ? 462 ALA A CB    1 
ATOM   3383 N  N     . LYS B 2 463 ? 100.677 88.123  108.391 1.00 45.82  ? 463 LYS A N     1 
ATOM   3384 C  CA    . LYS B 2 463 ? 101.575 89.011  107.666 1.00 48.45  ? 463 LYS A CA    1 
ATOM   3385 C  C     . LYS B 2 463 ? 102.783 89.367  108.518 1.00 46.42  ? 463 LYS A C     1 
ATOM   3386 O  O     . LYS B 2 463 ? 103.931 89.332  108.048 1.00 46.07  ? 463 LYS A O     1 
ATOM   3387 C  CB    . LYS B 2 463 ? 100.800 90.267  107.265 1.00 45.42  ? 463 LYS A CB    1 
ATOM   3388 C  CG    . LYS B 2 463 ? 101.451 91.122  106.209 1.00 36.82  ? 463 LYS A CG    1 
ATOM   3389 C  CD    . LYS B 2 463 ? 100.739 92.457  106.033 1.00 35.78  ? 463 LYS A CD    1 
ATOM   3390 C  CE    . LYS B 2 463 ? 99.266  92.290  105.687 1.00 38.63  ? 463 LYS A CE    1 
ATOM   3391 N  NZ    . LYS B 2 463 ? 98.548  93.584  105.616 1.00 39.54  ? 463 LYS A NZ    1 
ATOM   3392 N  N     . ALA B 2 464 ? 102.537 89.690  109.785 1.00 46.65  ? 464 ALA A N     1 
ATOM   3393 C  CA    . ALA B 2 464 ? 103.632 89.988  110.696 1.00 43.47  ? 464 ALA A CA    1 
ATOM   3394 C  C     . ALA B 2 464 ? 104.567 88.796  110.829 1.00 45.72  ? 464 ALA A C     1 
ATOM   3395 O  O     . ALA B 2 464 ? 105.790 88.950  110.777 1.00 45.47  ? 464 ALA A O     1 
ATOM   3396 C  CB    . ALA B 2 464 ? 103.081 90.388  112.061 1.00 45.58  ? 464 ALA A CB    1 
ATOM   3397 N  N     . ILE B 2 465 ? 104.008 87.594  110.985 1.00 48.34  ? 465 ILE A N     1 
ATOM   3398 C  CA    . ILE B 2 465 ? 104.842 86.404  111.157 1.00 47.35  ? 465 ILE A CA    1 
ATOM   3399 C  C     . ILE B 2 465 ? 105.678 86.148  109.910 1.00 45.29  ? 465 ILE A C     1 
ATOM   3400 O  O     . ILE B 2 465 ? 106.878 85.841  109.993 1.00 44.52  ? 465 ILE A O     1 
ATOM   3401 C  CB    . ILE B 2 465 ? 103.968 85.184  111.499 1.00 46.61  ? 465 ILE A CB    1 
ATOM   3402 C  CG1   . ILE B 2 465 ? 103.386 85.318  112.905 1.00 47.88  ? 465 ILE A CG1   1 
ATOM   3403 C  CG2   . ILE B 2 465 ? 104.777 83.906  111.390 1.00 47.30  ? 465 ILE A CG2   1 
ATOM   3404 C  CD1   . ILE B 2 465 ? 102.218 84.397  113.170 1.00 44.56  ? 465 ILE A CD1   1 
ATOM   3405 N  N     . ASN B 2 466 ? 105.050 86.238  108.736 1.00 46.22  ? 466 ASN A N     1 
ATOM   3406 C  CA    . ASN B 2 466 ? 105.757 85.966  107.492 1.00 44.65  ? 466 ASN A CA    1 
ATOM   3407 C  C     . ASN B 2 466 ? 106.908 86.936  107.300 1.00 45.72  ? 466 ASN A C     1 
ATOM   3408 O  O     . ASN B 2 466 ? 108.030 86.524  106.999 1.00 47.99  ? 466 ASN A O     1 
ATOM   3409 C  CB    . ASN B 2 466 ? 104.796 86.033  106.304 1.00 42.84  ? 466 ASN A CB    1 
ATOM   3410 C  CG    . ASN B 2 466 ? 104.229 84.681  105.934 1.00 44.19  ? 466 ASN A CG    1 
ATOM   3411 O  OD1   . ASN B 2 466 ? 104.835 83.646  106.201 1.00 46.91  ? 466 ASN A OD1   1 
ATOM   3412 N  ND2   . ASN B 2 466 ? 103.065 84.684  105.303 1.00 43.31  ? 466 ASN A ND2   1 
ATOM   3413 N  N     . PHE B 2 467 ? 106.655 88.234  107.465 1.00 47.96  ? 467 PHE A N     1 
ATOM   3414 C  CA    . PHE B 2 467 ? 107.748 89.184  107.296 1.00 46.34  ? 467 PHE A CA    1 
ATOM   3415 C  C     . PHE B 2 467 ? 108.805 89.022  108.383 1.00 46.15  ? 467 PHE A C     1 
ATOM   3416 O  O     . PHE B 2 467 ? 110.003 89.115  108.092 1.00 45.05  ? 467 PHE A O     1 
ATOM   3417 C  CB    . PHE B 2 467 ? 107.195 90.608  107.236 1.00 40.08  ? 467 PHE A CB    1 
ATOM   3418 C  CG    . PHE B 2 467 ? 106.359 90.867  106.008 1.00 40.69  ? 467 PHE A CG    1 
ATOM   3419 C  CD1   . PHE B 2 467 ? 106.820 90.481  104.761 1.00 46.70  ? 467 PHE A CD1   1 
ATOM   3420 C  CD2   . PHE B 2 467 ? 105.123 91.478  106.091 1.00 38.04  ? 467 PHE A CD2   1 
ATOM   3421 C  CE1   . PHE B 2 467 ? 106.075 90.697  103.629 1.00 45.44  ? 467 PHE A CE1   1 
ATOM   3422 C  CE2   . PHE B 2 467 ? 104.376 91.698  104.950 1.00 44.49  ? 467 PHE A CE2   1 
ATOM   3423 C  CZ    . PHE B 2 467 ? 104.854 91.305  103.723 1.00 49.06  ? 467 PHE A CZ    1 
ATOM   3424 N  N     . GLY B 2 468 ? 108.402 88.740  109.618 1.00 45.94  ? 468 GLY A N     1 
ATOM   3425 C  CA    . GLY B 2 468 ? 109.359 88.425  110.655 1.00 46.93  ? 468 GLY A CA    1 
ATOM   3426 C  C     . GLY B 2 468 ? 110.339 87.356  110.225 1.00 50.97  ? 468 GLY A C     1 
ATOM   3427 O  O     . GLY B 2 468 ? 111.540 87.616  110.104 1.00 51.03  ? 468 GLY A O     1 
ATOM   3428 N  N     . LEU B 2 469 ? 109.833 86.145  109.976 1.00 54.53  ? 469 LEU A N     1 
ATOM   3429 C  CA    . LEU B 2 469 ? 110.726 85.018  109.719 1.00 56.21  ? 469 LEU A CA    1 
ATOM   3430 C  C     . LEU B 2 469 ? 111.342 85.045  108.325 1.00 55.61  ? 469 LEU A C     1 
ATOM   3431 O  O     . LEU B 2 469 ? 112.371 84.397  108.114 1.00 59.00  ? 469 LEU A O     1 
ATOM   3432 C  CB    . LEU B 2 469 ? 110.001 83.691  109.957 1.00 55.64  ? 469 LEU A CB    1 
ATOM   3433 C  CG    . LEU B 2 469 ? 108.846 83.287  109.048 1.00 57.16  ? 469 LEU A CG    1 
ATOM   3434 C  CD1   . LEU B 2 469 ? 109.340 82.387  107.952 1.00 59.98  ? 469 LEU A CD1   1 
ATOM   3435 C  CD2   . LEU B 2 469 ? 107.777 82.575  109.861 1.00 52.50  ? 469 LEU A CD2   1 
ATOM   3436 N  N     . ILE B 2 470 ? 110.753 85.771  107.373 1.00 52.48  ? 470 ILE A N     1 
ATOM   3437 C  CA    . ILE B 2 470 ? 111.431 86.019  106.104 1.00 52.76  ? 470 ILE A CA    1 
ATOM   3438 C  C     . ILE B 2 470 ? 112.642 86.917  106.321 1.00 59.79  ? 470 ILE A C     1 
ATOM   3439 O  O     . ILE B 2 470 ? 113.702 86.712  105.718 1.00 64.96  ? 470 ILE A O     1 
ATOM   3440 C  CB    . ILE B 2 470 ? 110.447 86.630  105.086 1.00 50.45  ? 470 ILE A CB    1 
ATOM   3441 C  CG1   . ILE B 2 470 ? 109.366 85.618  104.697 1.00 54.34  ? 470 ILE A CG1   1 
ATOM   3442 C  CG2   . ILE B 2 470 ? 111.188 87.114  103.849 1.00 50.16  ? 470 ILE A CG2   1 
ATOM   3443 C  CD1   . ILE B 2 470 ? 109.805 84.601  103.666 1.00 62.50  ? 470 ILE A CD1   1 
ATOM   3444 N  N     . TYR B 2 471 ? 112.502 87.933  107.176 1.00 54.93  ? 471 TYR A N     1 
ATOM   3445 C  CA    . TYR B 2 471 ? 113.593 88.851  107.474 1.00 53.09  ? 471 TYR A CA    1 
ATOM   3446 C  C     . TYR B 2 471 ? 114.432 88.442  108.681 1.00 58.33  ? 471 TYR A C     1 
ATOM   3447 O  O     . TYR B 2 471 ? 115.480 89.056  108.913 1.00 64.27  ? 471 TYR A O     1 
ATOM   3448 C  CB    . TYR B 2 471 ? 113.046 90.270  107.674 1.00 51.10  ? 471 TYR A CB    1 
ATOM   3449 C  CG    . TYR B 2 471 ? 112.265 90.805  106.486 1.00 53.09  ? 471 TYR A CG    1 
ATOM   3450 C  CD1   . TYR B 2 471 ? 112.838 90.846  105.220 1.00 52.66  ? 471 TYR A CD1   1 
ATOM   3451 C  CD2   . TYR B 2 471 ? 110.965 91.277  106.626 1.00 51.10  ? 471 TYR A CD2   1 
ATOM   3452 C  CE1   . TYR B 2 471 ? 112.142 91.335  104.138 1.00 46.18  ? 471 TYR A CE1   1 
ATOM   3453 C  CE2   . TYR B 2 471 ? 110.264 91.763  105.540 1.00 45.32  ? 471 TYR A CE2   1 
ATOM   3454 C  CZ    . TYR B 2 471 ? 110.859 91.790  104.304 1.00 41.21  ? 471 TYR A CZ    1 
ATOM   3455 O  OH    . TYR B 2 471 ? 110.168 92.274  103.223 1.00 41.26  ? 471 TYR A OH    1 
ATOM   3456 N  N     . GLY B 2 472 ? 114.016 87.437  109.454 1.00 54.33  ? 472 GLY A N     1 
ATOM   3457 C  CA    . GLY B 2 472 ? 114.919 86.872  110.444 1.00 59.26  ? 472 GLY A CA    1 
ATOM   3458 C  C     . GLY B 2 472 ? 114.370 86.558  111.824 1.00 62.28  ? 472 GLY A C     1 
ATOM   3459 O  O     . GLY B 2 472 ? 115.137 86.168  112.710 1.00 66.24  ? 472 GLY A O     1 
ATOM   3460 N  N     . MET B 2 473 ? 113.068 86.722  112.037 1.00 58.60  ? 473 MET A N     1 
ATOM   3461 C  CA    . MET B 2 473 ? 112.485 86.429  113.342 1.00 56.85  ? 473 MET A CA    1 
ATOM   3462 C  C     . MET B 2 473 ? 112.714 84.969  113.716 1.00 68.27  ? 473 MET A C     1 
ATOM   3463 O  O     . MET B 2 473 ? 112.435 84.063  112.925 1.00 71.49  ? 473 MET A O     1 
ATOM   3464 C  CB    . MET B 2 473 ? 110.989 86.741  113.325 1.00 53.09  ? 473 MET A CB    1 
ATOM   3465 C  CG    . MET B 2 473 ? 110.290 86.502  114.650 1.00 60.79  ? 473 MET A CG    1 
ATOM   3466 S  SD    . MET B 2 473 ? 108.795 87.493  114.827 1.00 47.89  ? 473 MET A SD    1 
ATOM   3467 C  CE    . MET B 2 473 ? 107.589 86.409  114.066 1.00 52.75  ? 473 MET A CE    1 
ATOM   3468 N  N     . ASN B 2 474 ? 113.210 84.739  114.931 1.00 70.73  ? 474 ASN A N     1 
ATOM   3469 C  CA    . ASN B 2 474 ? 113.536 83.395  115.389 1.00 72.17  ? 474 ASN A CA    1 
ATOM   3470 C  C     . ASN B 2 474 ? 112.307 82.714  115.988 1.00 70.20  ? 474 ASN A C     1 
ATOM   3471 O  O     . ASN B 2 474 ? 111.241 83.313  116.141 1.00 68.55  ? 474 ASN A O     1 
ATOM   3472 C  CB    . ASN B 2 474 ? 114.677 83.424  116.410 1.00 73.09  ? 474 ASN A CB    1 
ATOM   3473 C  CG    . ASN B 2 474 ? 114.258 84.016  117.746 1.00 73.44  ? 474 ASN A CG    1 
ATOM   3474 O  OD1   . ASN B 2 474 ? 113.254 83.613  118.332 1.00 74.27  ? 474 ASN A OD1   1 
ATOM   3475 N  ND2   . ASN B 2 474 ? 115.038 84.969  118.241 1.00 78.00  ? 474 ASN A ND2   1 
ATOM   3476 N  N     . TYR B 2 475 ? 112.475 81.435  116.339 1.00 68.02  ? 475 TYR A N     1 
ATOM   3477 C  CA    . TYR B 2 475 ? 111.337 80.620  116.749 1.00 70.83  ? 475 TYR A CA    1 
ATOM   3478 C  C     . TYR B 2 475 ? 110.867 80.911  118.169 1.00 73.00  ? 475 TYR A C     1 
ATOM   3479 O  O     . TYR B 2 475 ? 109.687 80.701  118.460 1.00 73.59  ? 475 TYR A O     1 
ATOM   3480 C  CB    . TYR B 2 475 ? 111.664 79.131  116.603 1.00 72.49  ? 475 TYR A CB    1 
ATOM   3481 C  CG    . TYR B 2 475 ? 112.729 78.606  117.540 1.00 78.40  ? 475 TYR A CG    1 
ATOM   3482 C  CD1   . TYR B 2 475 ? 114.079 78.749  117.244 1.00 84.44  ? 475 TYR A CD1   1 
ATOM   3483 C  CD2   . TYR B 2 475 ? 112.385 77.938  118.710 1.00 80.95  ? 475 TYR A CD2   1 
ATOM   3484 C  CE1   . TYR B 2 475 ? 115.051 78.262  118.095 1.00 92.48  ? 475 TYR A CE1   1 
ATOM   3485 C  CE2   . TYR B 2 475 ? 113.353 77.449  119.562 1.00 87.46  ? 475 TYR A CE2   1 
ATOM   3486 C  CZ    . TYR B 2 475 ? 114.682 77.612  119.250 1.00 92.69  ? 475 TYR A CZ    1 
ATOM   3487 O  OH    . TYR B 2 475 ? 115.643 77.123  120.101 1.00 92.12  ? 475 TYR A OH    1 
ATOM   3488 N  N     . VAL B 2 476 ? 111.736 81.398  119.056 1.00 74.03  ? 476 VAL A N     1 
ATOM   3489 C  CA    . VAL B 2 476 ? 111.271 81.710  120.407 1.00 72.96  ? 476 VAL A CA    1 
ATOM   3490 C  C     . VAL B 2 476 ? 110.570 83.061  120.429 1.00 73.27  ? 476 VAL A C     1 
ATOM   3491 O  O     . VAL B 2 476 ? 109.517 83.220  121.057 1.00 73.22  ? 476 VAL A O     1 
ATOM   3492 C  CB    . VAL B 2 476 ? 112.431 81.656  121.419 1.00 71.07  ? 476 VAL A CB    1 
ATOM   3493 C  CG1   . VAL B 2 476 ? 113.556 82.598  121.034 1.00 67.93  ? 476 VAL A CG1   1 
ATOM   3494 C  CG2   . VAL B 2 476 ? 111.925 81.972  122.822 1.00 70.94  ? 476 VAL A CG2   1 
ATOM   3495 N  N     . ASN B 2 477 ? 111.134 84.055  119.742 1.00 74.06  ? 477 ASN A N     1 
ATOM   3496 C  CA    . ASN B 2 477 ? 110.424 85.316  119.570 1.00 70.63  ? 477 ASN A CA    1 
ATOM   3497 C  C     . ASN B 2 477 ? 109.134 85.104  118.792 1.00 68.37  ? 477 ASN A C     1 
ATOM   3498 O  O     . ASN B 2 477 ? 108.120 85.758  119.061 1.00 64.21  ? 477 ASN A O     1 
ATOM   3499 C  CB    . ASN B 2 477 ? 111.318 86.325  118.853 1.00 68.96  ? 477 ASN A CB    1 
ATOM   3500 C  CG    . ASN B 2 477 ? 112.405 86.878  119.746 1.00 70.14  ? 477 ASN A CG    1 
ATOM   3501 O  OD1   . ASN B 2 477 ? 113.502 86.327  119.823 1.00 76.35  ? 477 ASN A OD1   1 
ATOM   3502 N  ND2   . ASN B 2 477 ? 112.114 87.987  120.414 1.00 64.59  ? 477 ASN A ND2   1 
ATOM   3503 N  N     . LEU B 2 478 ? 109.154 84.196  117.815 1.00 69.14  ? 478 LEU A N     1 
ATOM   3504 C  CA    . LEU B 2 478 ? 107.935 83.876  117.084 1.00 69.38  ? 478 LEU A CA    1 
ATOM   3505 C  C     . LEU B 2 478 ? 106.911 83.215  117.999 1.00 70.12  ? 478 LEU A C     1 
ATOM   3506 O  O     . LEU B 2 478 ? 105.710 83.486  117.891 1.00 67.15  ? 478 LEU A O     1 
ATOM   3507 C  CB    . LEU B 2 478 ? 108.268 82.983  115.885 1.00 64.28  ? 478 LEU A CB    1 
ATOM   3508 C  CG    . LEU B 2 478 ? 107.139 82.548  114.941 1.00 61.97  ? 478 LEU A CG    1 
ATOM   3509 C  CD1   . LEU B 2 478 ? 107.720 82.288  113.564 1.00 63.14  ? 478 LEU A CD1   1 
ATOM   3510 C  CD2   . LEU B 2 478 ? 106.404 81.313  115.416 1.00 65.27  ? 478 LEU A CD2   1 
ATOM   3511 N  N     . LYS B 2 479 ? 107.365 82.338  118.899 1.00 71.39  ? 479 LYS A N     1 
ATOM   3512 C  CA    . LYS B 2 479 ? 106.465 81.761  119.893 1.00 74.34  ? 479 LYS A CA    1 
ATOM   3513 C  C     . LYS B 2 479 ? 105.836 82.849  120.747 1.00 75.94  ? 479 LYS A C     1 
ATOM   3514 O  O     . LYS B 2 479 ? 104.627 82.839  120.995 1.00 75.11  ? 479 LYS A O     1 
ATOM   3515 C  CB    . LYS B 2 479 ? 107.223 80.775  120.781 1.00 76.89  ? 479 LYS A CB    1 
ATOM   3516 C  CG    . LYS B 2 479 ? 106.462 80.396  122.056 1.00 79.30  ? 479 LYS A CG    1 
ATOM   3517 C  CD    . LYS B 2 479 ? 107.169 79.297  122.822 1.00 84.53  ? 479 LYS A CD    1 
ATOM   3518 C  CE    . LYS B 2 479 ? 106.789 79.323  124.293 1.00 88.01  ? 479 LYS A CE    1 
ATOM   3519 N  NZ    . LYS B 2 479 ? 105.328 79.129  124.488 1.00 92.64  ? 479 LYS A NZ    1 
ATOM   3520 N  N     . ASN B 2 480 ? 106.652 83.786  121.229 1.00 76.30  ? 480 ASN A N     1 
ATOM   3521 C  CA    . ASN B 2 480 ? 106.122 84.868  122.051 1.00 77.24  ? 480 ASN A CA    1 
ATOM   3522 C  C     . ASN B 2 480 ? 105.090 85.678  121.277 1.00 76.93  ? 480 ASN A C     1 
ATOM   3523 O  O     . ASN B 2 480 ? 104.018 86.002  121.799 1.00 77.43  ? 480 ASN A O     1 
ATOM   3524 C  CB    . ASN B 2 480 ? 107.258 85.770  122.529 1.00 81.39  ? 480 ASN A CB    1 
ATOM   3525 C  CG    . ASN B 2 480 ? 108.212 85.062  123.466 1.00 82.53  ? 480 ASN A CG    1 
ATOM   3526 O  OD1   . ASN B 2 480 ? 109.428 85.218  123.360 1.00 83.12  ? 480 ASN A OD1   1 
ATOM   3527 N  ND2   . ASN B 2 480 ? 107.667 84.292  124.403 1.00 84.44  ? 480 ASN A ND2   1 
ATOM   3528 N  N     . TYR B 2 481 ? 105.404 86.016  120.025 1.00 72.82  ? 481 TYR A N     1 
ATOM   3529 C  CA    . TYR B 2 481 ? 104.485 86.806  119.212 1.00 69.46  ? 481 TYR A CA    1 
ATOM   3530 C  C     . TYR B 2 481 ? 103.168 86.071  119.002 1.00 69.50  ? 481 TYR A C     1 
ATOM   3531 O  O     . TYR B 2 481 ? 102.086 86.643  119.179 1.00 69.33  ? 481 TYR A O     1 
ATOM   3532 C  CB    . TYR B 2 481 ? 105.130 87.130  117.863 1.00 68.15  ? 481 TYR A CB    1 
ATOM   3533 C  CG    . TYR B 2 481 ? 104.365 88.145  117.030 1.00 71.29  ? 481 TYR A CG    1 
ATOM   3534 C  CD1   . TYR B 2 481 ? 103.169 87.805  116.408 1.00 67.37  ? 481 TYR A CD1   1 
ATOM   3535 C  CD2   . TYR B 2 481 ? 104.845 89.436  116.857 1.00 70.29  ? 481 TYR A CD2   1 
ATOM   3536 C  CE1   . TYR B 2 481 ? 102.470 88.722  115.654 1.00 61.71  ? 481 TYR A CE1   1 
ATOM   3537 C  CE2   . TYR B 2 481 ? 104.150 90.354  116.103 1.00 67.88  ? 481 TYR A CE2   1 
ATOM   3538 C  CZ    . TYR B 2 481 ? 102.965 89.992  115.504 1.00 67.16  ? 481 TYR A CZ    1 
ATOM   3539 O  OH    . TYR B 2 481 ? 102.272 90.911  114.754 1.00 75.55  ? 481 TYR A OH    1 
ATOM   3540 N  N     . ALA B 2 482 ? 103.243 84.796  118.614 1.00 67.44  ? 482 ALA A N     1 
ATOM   3541 C  CA    . ALA B 2 482 ? 102.034 84.026  118.353 1.00 70.03  ? 482 ALA A CA    1 
ATOM   3542 C  C     . ALA B 2 482 ? 101.216 83.842  119.622 1.00 76.36  ? 482 ALA A C     1 
ATOM   3543 O  O     . ALA B 2 482 ? 99.982  83.908  119.586 1.00 80.37  ? 482 ALA A O     1 
ATOM   3544 C  CB    . ALA B 2 482 ? 102.404 82.674  117.745 1.00 68.98  ? 482 ALA A CB    1 
ATOM   3545 N  N     . ASN B 2 483 ? 101.883 83.627  120.757 1.00 73.95  ? 483 ASN A N     1 
ATOM   3546 C  CA    . ASN B 2 483 ? 101.159 83.421  122.005 1.00 74.49  ? 483 ASN A CA    1 
ATOM   3547 C  C     . ASN B 2 483 ? 100.488 84.708  122.456 1.00 78.47  ? 483 ASN A C     1 
ATOM   3548 O  O     . ASN B 2 483 ? 99.337  84.693  122.908 1.00 82.42  ? 483 ASN A O     1 
ATOM   3549 C  CB    . ASN B 2 483 ? 102.118 82.916  123.084 1.00 79.63  ? 483 ASN A CB    1 
ATOM   3550 C  CG    . ASN B 2 483 ? 102.634 81.505  122.815 1.00 80.09  ? 483 ASN A CG    1 
ATOM   3551 O  OD1   . ASN B 2 483 ? 103.475 81.000  123.558 1.00 84.51  ? 483 ASN A OD1   1 
ATOM   3552 N  ND2   . ASN B 2 483 ? 102.155 80.875  121.746 1.00 76.66  ? 483 ASN A ND2   1 
ATOM   3553 N  N     . THR B 2 484 ? 101.186 85.837  122.326 1.00 76.41  ? 484 THR A N     1 
ATOM   3554 C  CA    . THR B 2 484 ? 100.620 87.112  122.744 1.00 76.37  ? 484 THR A CA    1 
ATOM   3555 C  C     . THR B 2 484 ? 99.445  87.500  121.862 1.00 78.37  ? 484 THR A C     1 
ATOM   3556 O  O     . THR B 2 484 ? 98.357  87.815  122.359 1.00 79.50  ? 484 THR A O     1 
ATOM   3557 C  CB    . THR B 2 484 ? 101.700 88.194  122.706 1.00 75.89  ? 484 THR A CB    1 
ATOM   3558 O  OG1   . THR B 2 484 ? 102.963 87.627  123.075 1.00 73.21  ? 484 THR A OG1   1 
ATOM   3559 C  CG2   . THR B 2 484 ? 101.348 89.336  123.643 1.00 79.99  ? 484 THR A CG2   1 
ATOM   3560 N  N     . TYR B 2 485 ? 99.641  87.471  120.545 1.00 77.17  ? 485 TYR A N     1 
ATOM   3561 C  CA    . TYR B 2 485 ? 98.617  87.923  119.615 1.00 75.04  ? 485 TYR A CA    1 
ATOM   3562 C  C     . TYR B 2 485 ? 97.609  86.841  119.258 1.00 71.93  ? 485 TYR A C     1 
ATOM   3563 O  O     . TYR B 2 485 ? 96.622  87.144  118.579 1.00 72.10  ? 485 TYR A O     1 
ATOM   3564 C  CB    . TYR B 2 485 ? 99.285  88.479  118.356 1.00 72.98  ? 485 TYR A CB    1 
ATOM   3565 C  CG    . TYR B 2 485 ? 100.055 89.752  118.633 1.00 73.55  ? 485 TYR A CG    1 
ATOM   3566 C  CD1   . TYR B 2 485 ? 99.387  90.939  118.906 1.00 74.67  ? 485 TYR A CD1   1 
ATOM   3567 C  CD2   . TYR B 2 485 ? 101.445 89.770  118.641 1.00 72.89  ? 485 TYR A CD2   1 
ATOM   3568 C  CE1   . TYR B 2 485 ? 100.076 92.102  119.169 1.00 79.06  ? 485 TYR A CE1   1 
ATOM   3569 C  CE2   . TYR B 2 485 ? 102.141 90.935  118.905 1.00 72.16  ? 485 TYR A CE2   1 
ATOM   3570 C  CZ    . TYR B 2 485 ? 101.450 92.096  119.168 1.00 78.26  ? 485 TYR A CZ    1 
ATOM   3571 O  OH    . TYR B 2 485 ? 102.128 93.263  119.432 1.00 86.51  ? 485 TYR A OH    1 
ATOM   3572 N  N     . TYR B 2 486 ? 97.817  85.602  119.694 1.00 75.23  ? 486 TYR A N     1 
ATOM   3573 C  CA    . TYR B 2 486 ? 96.838  84.554  119.461 1.00 83.50  ? 486 TYR A CA    1 
ATOM   3574 C  C     . TYR B 2 486 ? 96.799  83.616  120.660 1.00 89.28  ? 486 TYR A C     1 
ATOM   3575 O  O     . TYR B 2 486 ? 97.803  83.414  121.346 1.00 87.12  ? 486 TYR A O     1 
ATOM   3576 C  CB    . TYR B 2 486 ? 97.154  83.784  118.179 1.00 83.02  ? 486 TYR A CB    1 
ATOM   3577 C  CG    . TYR B 2 486 ? 95.948  83.619  117.290 1.00 88.48  ? 486 TYR A CG    1 
ATOM   3578 C  CD1   . TYR B 2 486 ? 95.423  84.708  116.608 1.00 89.38  ? 486 TYR A CD1   1 
ATOM   3579 C  CD2   . TYR B 2 486 ? 95.331  82.388  117.127 1.00 92.60  ? 486 TYR A CD2   1 
ATOM   3580 C  CE1   . TYR B 2 486 ? 94.321  84.580  115.800 1.00 89.44  ? 486 TYR A CE1   1 
ATOM   3581 C  CE2   . TYR B 2 486 ? 94.225  82.252  116.312 1.00 95.50  ? 486 TYR A CE2   1 
ATOM   3582 C  CZ    . TYR B 2 486 ? 93.726  83.351  115.649 1.00 95.04  ? 486 TYR A CZ    1 
ATOM   3583 O  OH    . TYR B 2 486 ? 92.624  83.230  114.834 1.00 96.63  ? 486 TYR A OH    1 
ATOM   3584 N  N     . GLY B 2 487 ? 95.621  83.044  120.900 1.00 92.03  ? 487 GLY A N     1 
ATOM   3585 C  CA    . GLY B 2 487 ? 95.382  82.212  122.066 1.00 93.99  ? 487 GLY A CA    1 
ATOM   3586 C  C     . GLY B 2 487 ? 95.834  80.773  121.913 1.00 96.01  ? 487 GLY A C     1 
ATOM   3587 O  O     . GLY B 2 487 ? 95.178  79.857  122.417 1.00 100.17 ? 487 GLY A O     1 
ATOM   3588 N  N     . LEU B 2 488 ? 96.953  80.554  121.219 1.00 93.79  ? 488 LEU A N     1 
ATOM   3589 C  CA    . LEU B 2 488 ? 97.379  79.188  120.928 1.00 96.62  ? 488 LEU A CA    1 
ATOM   3590 C  C     . LEU B 2 488 ? 97.797  78.438  122.187 1.00 96.82  ? 488 LEU A C     1 
ATOM   3591 O  O     . LEU B 2 488 ? 97.414  77.278  122.379 1.00 97.04  ? 488 LEU A O     1 
ATOM   3592 C  CB    . LEU B 2 488 ? 98.537  79.195  119.931 1.00 93.39  ? 488 LEU A CB    1 
ATOM   3593 C  CG    . LEU B 2 488 ? 98.267  79.779  118.545 1.00 86.14  ? 488 LEU A CG    1 
ATOM   3594 C  CD1   . LEU B 2 488 ? 99.534  79.722  117.708 1.00 78.57  ? 488 LEU A CD1   1 
ATOM   3595 C  CD2   . LEU B 2 488 ? 97.122  79.043  117.854 1.00 85.11  ? 488 LEU A CD2   1 
ATOM   3596 N  N     . ASN B 2 489 ? 98.579  79.077  123.056 1.00 94.12  ? 489 ASN A N     1 
ATOM   3597 C  CA    . ASN B 2 489 ? 99.291  78.370  124.121 1.00 94.97  ? 489 ASN A CA    1 
ATOM   3598 C  C     . ASN B 2 489 ? 100.238 77.326  123.531 1.00 95.49  ? 489 ASN A C     1 
ATOM   3599 O  O     . ASN B 2 489 ? 100.414 76.233  124.072 1.00 97.95  ? 489 ASN A O     1 
ATOM   3600 C  CB    . ASN B 2 489 ? 98.311  77.721  125.100 1.00 97.01  ? 489 ASN A CB    1 
ATOM   3601 C  CG    . ASN B 2 489 ? 98.975  77.315  126.402 1.00 103.46 ? 489 ASN A CG    1 
ATOM   3602 O  OD1   . ASN B 2 489 ? 100.081 77.758  126.709 1.00 105.61 ? 489 ASN A OD1   1 
ATOM   3603 N  ND2   . ASN B 2 489 ? 98.305  76.464  127.172 1.00 105.90 ? 489 ASN A ND2   1 
ATOM   3604 N  N     . MET B 2 490 ? 100.855 77.674  122.405 1.00 93.69  ? 490 MET A N     1 
ATOM   3605 C  CA    . MET B 2 490 ? 101.732 76.748  121.699 1.00 91.34  ? 490 MET A CA    1 
ATOM   3606 C  C     . MET B 2 490 ? 103.047 76.567  122.452 1.00 87.25  ? 490 MET A C     1 
ATOM   3607 O  O     . MET B 2 490 ? 103.603 77.528  122.992 1.00 85.16  ? 490 MET A O     1 
ATOM   3608 C  CB    . MET B 2 490 ? 101.997 77.265  120.285 1.00 96.89  ? 490 MET A CB    1 
ATOM   3609 C  CG    . MET B 2 490 ? 103.008 76.446  119.499 1.00 100.46 ? 490 MET A CG    1 
ATOM   3610 S  SD    . MET B 2 490 ? 103.170 77.018  117.798 1.00 88.62  ? 490 MET A SD    1 
ATOM   3611 C  CE    . MET B 2 490 ? 103.770 78.684  118.073 1.00 79.11  ? 490 MET A CE    1 
ATOM   3612 N  N     . SER B 2 491 ? 103.542 75.332  122.488 1.00 88.88  ? 491 SER A N     1 
ATOM   3613 C  CA    . SER B 2 491 ? 104.794 75.022  123.161 1.00 89.20  ? 491 SER A CA    1 
ATOM   3614 C  C     . SER B 2 491 ? 105.990 75.332  122.263 1.00 88.04  ? 491 SER A C     1 
ATOM   3615 O  O     . SER B 2 491 ? 105.865 75.503  121.047 1.00 89.37  ? 491 SER A O     1 
ATOM   3616 C  CB    . SER B 2 491 ? 104.830 73.554  123.587 1.00 92.14  ? 491 SER A CB    1 
ATOM   3617 O  OG    . SER B 2 491 ? 104.676 72.692  122.473 1.00 93.82  ? 491 SER A OG    1 
ATOM   3618 N  N     . LEU B 2 492 ? 107.168 75.403  122.890 1.00 87.03  ? 492 LEU A N     1 
ATOM   3619 C  CA    . LEU B 2 492 ? 108.381 75.773  122.167 1.00 84.30  ? 492 LEU A CA    1 
ATOM   3620 C  C     . LEU B 2 492 ? 108.766 74.728  121.127 1.00 87.69  ? 492 LEU A C     1 
ATOM   3621 O  O     . LEU B 2 492 ? 109.207 75.077  120.027 1.00 89.99  ? 492 LEU A O     1 
ATOM   3622 C  CB    . LEU B 2 492 ? 109.532 75.986  123.151 1.00 82.83  ? 492 LEU A CB    1 
ATOM   3623 C  CG    . LEU B 2 492 ? 110.821 76.539  122.538 1.00 78.25  ? 492 LEU A CG    1 
ATOM   3624 C  CD1   . LEU B 2 492 ? 110.632 77.975  122.085 1.00 77.76  ? 492 LEU A CD1   1 
ATOM   3625 C  CD2   . LEU B 2 492 ? 111.963 76.444  123.527 1.00 80.79  ? 492 LEU A CD2   1 
ATOM   3626 N  N     . ASP B 2 493 ? 108.636 73.441  121.460 1.00 85.87  ? 493 ASP A N     1 
ATOM   3627 C  CA    . ASP B 2 493 ? 109.064 72.399  120.528 1.00 84.95  ? 493 ASP A CA    1 
ATOM   3628 C  C     . ASP B 2 493 ? 108.215 72.407  119.262 1.00 85.46  ? 493 ASP A C     1 
ATOM   3629 O  O     . ASP B 2 493 ? 108.744 72.279  118.150 1.00 83.86  ? 493 ASP A O     1 
ATOM   3630 C  CB    . ASP B 2 493 ? 109.002 71.031  121.207 1.00 86.93  ? 493 ASP A CB    1 
ATOM   3631 C  CG    . ASP B 2 493 ? 107.651 70.756  121.835 1.00 91.73  ? 493 ASP A CG    1 
ATOM   3632 O  OD1   . ASP B 2 493 ? 106.791 71.661  121.811 1.00 91.05  ? 493 ASP A OD1   1 
ATOM   3633 O  OD2   . ASP B 2 493 ? 107.454 69.642  122.359 1.00 96.11  ? 493 ASP A OD2   1 
ATOM   3634 N  N     . GLN B 2 494 ? 106.899 72.562  119.412 1.00 87.17  ? 494 GLN A N     1 
ATOM   3635 C  CA    . GLN B 2 494 ? 106.031 72.662  118.245 1.00 88.38  ? 494 GLN A CA    1 
ATOM   3636 C  C     . GLN B 2 494 ? 106.414 73.860  117.389 1.00 82.62  ? 494 GLN A C     1 
ATOM   3637 O  O     . GLN B 2 494 ? 106.438 73.774  116.154 1.00 75.32  ? 494 GLN A O     1 
ATOM   3638 C  CB    . GLN B 2 494 ? 104.573 72.767  118.695 1.00 89.45  ? 494 GLN A CB    1 
ATOM   3639 C  CG    . GLN B 2 494 ? 104.007 71.487  119.288 1.00 94.88  ? 494 GLN A CG    1 
ATOM   3640 C  CD    . GLN B 2 494 ? 102.536 71.303  118.978 1.00 102.02 ? 494 GLN A CD    1 
ATOM   3641 O  OE1   . GLN B 2 494 ? 101.728 72.209  119.186 1.00 97.97  ? 494 GLN A OE1   1 
ATOM   3642 N  NE2   . GLN B 2 494 ? 102.175 70.120  118.494 1.00 106.90 ? 494 GLN A NE2   1 
ATOM   3643 N  N     . CYS B 2 495 ? 106.714 74.990  118.028 1.00 81.76  ? 495 CYS A N     1 
ATOM   3644 C  CA    . CYS B 2 495 ? 107.105 76.175  117.278 1.00 73.19  ? 495 CYS A CA    1 
ATOM   3645 C  C     . CYS B 2 495 ? 108.403 75.942  116.520 1.00 73.71  ? 495 CYS A C     1 
ATOM   3646 O  O     . CYS B 2 495 ? 108.538 76.360  115.366 1.00 76.91  ? 495 CYS A O     1 
ATOM   3647 C  CB    . CYS B 2 495 ? 107.242 77.369  118.219 1.00 71.70  ? 495 CYS A CB    1 
ATOM   3648 S  SG    . CYS B 2 495 ? 107.449 78.936  117.361 1.00 67.17  ? 495 CYS A SG    1 
ATOM   3649 N  N     . LEU B 2 496 ? 109.379 75.294  117.158 1.00 74.50  ? 496 LEU A N     1 
ATOM   3650 C  CA    . LEU B 2 496 ? 110.633 75.000  116.473 1.00 72.85  ? 496 LEU A CA    1 
ATOM   3651 C  C     . LEU B 2 496 ? 110.392 74.096  115.273 1.00 72.86  ? 496 LEU A C     1 
ATOM   3652 O  O     . LEU B 2 496 ? 110.973 74.301  114.198 1.00 70.93  ? 496 LEU A O     1 
ATOM   3653 C  CB    . LEU B 2 496 ? 111.622 74.348  117.441 1.00 75.94  ? 496 LEU A CB    1 
ATOM   3654 C  CG    . LEU B 2 496 ? 113.048 74.079  116.939 1.00 79.80  ? 496 LEU A CG    1 
ATOM   3655 C  CD1   . LEU B 2 496 ? 113.513 75.104  115.911 1.00 73.26  ? 496 LEU A CD1   1 
ATOM   3656 C  CD2   . LEU B 2 496 ? 114.021 74.022  118.107 1.00 84.37  ? 496 LEU A CD2   1 
ATOM   3657 N  N     . TYR B 2 497 ? 109.540 73.083  115.440 1.00 76.29  ? 497 TYR A N     1 
ATOM   3658 C  CA    . TYR B 2 497 ? 109.243 72.191  114.326 1.00 76.57  ? 497 TYR A CA    1 
ATOM   3659 C  C     . TYR B 2 497 ? 108.588 72.952  113.181 1.00 74.20  ? 497 TYR A C     1 
ATOM   3660 O  O     . TYR B 2 497 ? 108.921 72.734  112.013 1.00 71.83  ? 497 TYR A O     1 
ATOM   3661 C  CB    . TYR B 2 497 ? 108.342 71.047  114.788 1.00 75.44  ? 497 TYR A CB    1 
ATOM   3662 C  CG    . TYR B 2 497 ? 107.534 70.427  113.670 1.00 75.23  ? 497 TYR A CG    1 
ATOM   3663 C  CD1   . TYR B 2 497 ? 108.150 69.665  112.686 1.00 73.32  ? 497 TYR A CD1   1 
ATOM   3664 C  CD2   . TYR B 2 497 ? 106.159 70.607  113.591 1.00 76.49  ? 497 TYR A CD2   1 
ATOM   3665 C  CE1   . TYR B 2 497 ? 107.422 69.098  111.662 1.00 75.94  ? 497 TYR A CE1   1 
ATOM   3666 C  CE2   . TYR B 2 497 ? 105.423 70.042  112.567 1.00 75.41  ? 497 TYR A CE2   1 
ATOM   3667 C  CZ    . TYR B 2 497 ? 106.060 69.290  111.605 1.00 77.06  ? 497 TYR A CZ    1 
ATOM   3668 O  OH    . TYR B 2 497 ? 105.332 68.726  110.584 1.00 77.67  ? 497 TYR A OH    1 
ATOM   3669 N  N     . PHE B 2 498 ? 107.649 73.845  113.498 1.00 73.06  ? 498 PHE A N     1 
ATOM   3670 C  CA    . PHE B 2 498 ? 106.991 74.641  112.463 1.00 68.42  ? 498 PHE A CA    1 
ATOM   3671 C  C     . PHE B 2 498 ? 107.988 75.546  111.745 1.00 65.68  ? 498 PHE A C     1 
ATOM   3672 O  O     . PHE B 2 498 ? 107.946 75.693  110.517 1.00 65.56  ? 498 PHE A O     1 
ATOM   3673 C  CB    . PHE B 2 498 ? 105.869 75.470  113.088 1.00 67.86  ? 498 PHE A CB    1 
ATOM   3674 C  CG    . PHE B 2 498 ? 105.528 76.714  112.318 1.00 63.38  ? 498 PHE A CG    1 
ATOM   3675 C  CD1   . PHE B 2 498 ? 104.786 76.648  111.153 1.00 61.50  ? 498 PHE A CD1   1 
ATOM   3676 C  CD2   . PHE B 2 498 ? 105.956 77.952  112.760 1.00 62.11  ? 498 PHE A CD2   1 
ATOM   3677 C  CE1   . PHE B 2 498 ? 104.474 77.791  110.453 1.00 60.13  ? 498 PHE A CE1   1 
ATOM   3678 C  CE2   . PHE B 2 498 ? 105.648 79.093  112.062 1.00 60.78  ? 498 PHE A CE2   1 
ATOM   3679 C  CZ    . PHE B 2 498 ? 104.907 79.013  110.908 1.00 61.22  ? 498 PHE A CZ    1 
ATOM   3680 N  N     . TYR B 2 499 ? 108.871 76.190  112.508 1.00 65.26  ? 499 TYR A N     1 
ATOM   3681 C  CA    . TYR B 2 499 ? 109.896 77.050  111.926 1.00 60.67  ? 499 TYR A CA    1 
ATOM   3682 C  C     . TYR B 2 499 ? 110.773 76.268  110.958 1.00 66.93  ? 499 TYR A C     1 
ATOM   3683 O  O     . TYR B 2 499 ? 111.026 76.708  109.828 1.00 71.05  ? 499 TYR A O     1 
ATOM   3684 C  CB    . TYR B 2 499 ? 110.732 77.660  113.052 1.00 62.40  ? 499 TYR A CB    1 
ATOM   3685 C  CG    . TYR B 2 499 ? 111.928 78.477  112.617 1.00 63.31  ? 499 TYR A CG    1 
ATOM   3686 C  CD1   . TYR B 2 499 ? 113.165 77.880  112.418 1.00 67.66  ? 499 TYR A CD1   1 
ATOM   3687 C  CD2   . TYR B 2 499 ? 111.834 79.851  112.448 1.00 64.26  ? 499 TYR A CD2   1 
ATOM   3688 C  CE1   . TYR B 2 499 ? 114.259 78.622  112.039 1.00 65.19  ? 499 TYR A CE1   1 
ATOM   3689 C  CE2   . TYR B 2 499 ? 112.926 80.596  112.070 1.00 66.53  ? 499 TYR A CE2   1 
ATOM   3690 C  CZ    . TYR B 2 499 ? 114.134 79.978  111.867 1.00 68.21  ? 499 TYR A CZ    1 
ATOM   3691 O  OH    . TYR B 2 499 ? 115.227 80.721  111.491 1.00 73.14  ? 499 TYR A OH    1 
ATOM   3692 N  N     . ASN B 2 500 ? 111.241 75.094  111.385 1.00 66.14  ? 500 ASN A N     1 
ATOM   3693 C  CA    . ASN B 2 500 ? 112.071 74.270  110.514 1.00 64.53  ? 500 ASN A CA    1 
ATOM   3694 C  C     . ASN B 2 500 ? 111.292 73.813  109.288 1.00 65.23  ? 500 ASN A C     1 
ATOM   3695 O  O     . ASN B 2 500 ? 111.834 73.769  108.178 1.00 65.67  ? 500 ASN A O     1 
ATOM   3696 C  CB    . ASN B 2 500 ? 112.604 73.068  111.292 1.00 66.45  ? 500 ASN A CB    1 
ATOM   3697 C  CG    . ASN B 2 500 ? 113.661 73.455  112.304 1.00 70.47  ? 500 ASN A CG    1 
ATOM   3698 O  OD1   . ASN B 2 500 ? 113.499 73.227  113.502 1.00 74.73  ? 500 ASN A OD1   1 
ATOM   3699 N  ND2   . ASN B 2 500 ? 114.753 74.041  111.827 1.00 72.10  ? 500 ASN A ND2   1 
ATOM   3700 N  N     . SER B 2 501 ? 110.018 73.464  109.472 1.00 65.34  ? 501 SER A N     1 
ATOM   3701 C  CA    . SER B 2 501 ? 109.193 73.027  108.353 1.00 65.81  ? 501 SER A CA    1 
ATOM   3702 C  C     . SER B 2 501 ? 109.070 74.122  107.305 1.00 67.15  ? 501 SER A C     1 
ATOM   3703 O  O     . SER B 2 501 ? 109.205 73.867  106.104 1.00 69.28  ? 501 SER A O     1 
ATOM   3704 C  CB    . SER B 2 501 ? 107.813 72.615  108.862 1.00 65.33  ? 501 SER A CB    1 
ATOM   3705 O  OG    . SER B 2 501 ? 106.861 72.623  107.813 1.00 62.47  ? 501 SER A OG    1 
ATOM   3706 N  N     . PHE B 2 502 ? 108.805 75.353  107.741 1.00 66.08  ? 502 PHE A N     1 
ATOM   3707 C  CA    . PHE B 2 502 ? 108.718 76.456  106.790 1.00 59.33  ? 502 PHE A CA    1 
ATOM   3708 C  C     . PHE B 2 502 ? 110.055 76.680  106.101 1.00 59.76  ? 502 PHE A C     1 
ATOM   3709 O  O     . PHE B 2 502 ? 110.117 76.835  104.877 1.00 61.11  ? 502 PHE A O     1 
ATOM   3710 C  CB    . PHE B 2 502 ? 108.257 77.734  107.493 1.00 56.93  ? 502 PHE A CB    1 
ATOM   3711 C  CG    . PHE B 2 502 ? 108.094 78.914  106.568 1.00 54.33  ? 502 PHE A CG    1 
ATOM   3712 C  CD1   . PHE B 2 502 ? 109.196 79.619  106.105 1.00 53.85  ? 502 PHE A CD1   1 
ATOM   3713 C  CD2   . PHE B 2 502 ? 106.837 79.313  106.157 1.00 56.24  ? 502 PHE A CD2   1 
ATOM   3714 C  CE1   . PHE B 2 502 ? 109.042 80.693  105.253 1.00 52.83  ? 502 PHE A CE1   1 
ATOM   3715 C  CE2   . PHE B 2 502 ? 106.683 80.388  105.309 1.00 54.56  ? 502 PHE A CE2   1 
ATOM   3716 C  CZ    . PHE B 2 502 ? 107.785 81.078  104.859 1.00 52.09  ? 502 PHE A CZ    1 
ATOM   3717 N  N     . PHE B 2 503 ? 111.143 76.696  106.872 1.00 61.87  ? 503 PHE A N     1 
ATOM   3718 C  CA    . PHE B 2 503 ? 112.441 77.000  106.284 1.00 64.32  ? 503 PHE A CA    1 
ATOM   3719 C  C     . PHE B 2 503 ? 112.942 75.905  105.352 1.00 69.21  ? 503 PHE A C     1 
ATOM   3720 O  O     . PHE B 2 503 ? 113.794 76.185  104.502 1.00 69.69  ? 503 PHE A O     1 
ATOM   3721 C  CB    . PHE B 2 503 ? 113.462 77.270  107.385 1.00 69.04  ? 503 PHE A CB    1 
ATOM   3722 C  CG    . PHE B 2 503 ? 113.741 78.728  107.587 1.00 71.36  ? 503 PHE A CG    1 
ATOM   3723 C  CD1   . PHE B 2 503 ? 112.718 79.601  107.905 1.00 69.35  ? 503 PHE A CD1   1 
ATOM   3724 C  CD2   . PHE B 2 503 ? 115.021 79.231  107.443 1.00 75.83  ? 503 PHE A CD2   1 
ATOM   3725 C  CE1   . PHE B 2 503 ? 112.967 80.941  108.082 1.00 68.92  ? 503 PHE A CE1   1 
ATOM   3726 C  CE2   . PHE B 2 503 ? 115.272 80.571  107.620 1.00 74.63  ? 503 PHE A CE2   1 
ATOM   3727 C  CZ    . PHE B 2 503 ? 114.244 81.427  107.940 1.00 70.91  ? 503 PHE A CZ    1 
ATOM   3728 N  N     . GLU B 2 504 ? 112.447 74.673  105.485 1.00 68.22  ? 504 GLU A N     1 
ATOM   3729 C  CA    . GLU B 2 504 ? 112.824 73.621  104.546 1.00 65.97  ? 504 GLU A CA    1 
ATOM   3730 C  C     . GLU B 2 504 ? 111.862 73.528  103.371 1.00 64.15  ? 504 GLU A C     1 
ATOM   3731 O  O     . GLU B 2 504 ? 112.268 73.122  102.277 1.00 63.65  ? 504 GLU A O     1 
ATOM   3732 C  CB    . GLU B 2 504 ? 112.914 72.265  105.264 1.00 67.51  ? 504 GLU A CB    1 
ATOM   3733 C  CG    . GLU B 2 504 ? 111.622 71.749  105.907 1.00 66.69  ? 504 GLU A CG    1 
ATOM   3734 C  CD    . GLU B 2 504 ? 110.620 71.181  104.912 1.00 68.87  ? 504 GLU A CD    1 
ATOM   3735 O  OE1   . GLU B 2 504 ? 110.973 71.001  103.727 1.00 71.13  ? 504 GLU A OE1   1 
ATOM   3736 O  OE2   . GLU B 2 504 ? 109.471 70.916  105.320 1.00 67.63  ? 504 GLU A OE2   1 
ATOM   3737 N  N     . HIS B 2 505 ? 110.596 73.896  103.575 1.00 63.85  ? 505 HIS A N     1 
ATOM   3738 C  CA    . HIS B 2 505 ? 109.623 73.857  102.489 1.00 62.76  ? 505 HIS A CA    1 
ATOM   3739 C  C     . HIS B 2 505 ? 110.015 74.810  101.368 1.00 66.39  ? 505 HIS A C     1 
ATOM   3740 O  O     . HIS B 2 505 ? 109.931 74.460  100.185 1.00 65.48  ? 505 HIS A O     1 
ATOM   3741 C  CB    . HIS B 2 505 ? 108.237 74.199  103.035 1.00 62.81  ? 505 HIS A CB    1 
ATOM   3742 C  CG    . HIS B 2 505 ? 107.145 74.139  102.013 1.00 60.62  ? 505 HIS A CG    1 
ATOM   3743 N  ND1   . HIS B 2 505 ? 105.993 74.887  102.118 1.00 56.11  ? 505 HIS A ND1   1 
ATOM   3744 C  CD2   . HIS B 2 505 ? 107.025 73.423  100.869 1.00 63.11  ? 505 HIS A CD2   1 
ATOM   3745 C  CE1   . HIS B 2 505 ? 105.210 74.636  101.085 1.00 57.51  ? 505 HIS A CE1   1 
ATOM   3746 N  NE2   . HIS B 2 505 ? 105.813 73.752  100.311 1.00 61.57  ? 505 HIS A NE2   1 
ATOM   3747 N  N     . TYR B 2 506 ? 110.452 76.019  101.720 1.00 66.98  ? 506 TYR A N     1 
ATOM   3748 C  CA    . TYR B 2 506 ? 110.917 77.002  100.745 1.00 61.61  ? 506 TYR A CA    1 
ATOM   3749 C  C     . TYR B 2 506 ? 112.443 76.978  100.755 1.00 63.32  ? 506 TYR A C     1 
ATOM   3750 O  O     . TYR B 2 506 ? 113.105 77.771  101.423 1.00 65.32  ? 506 TYR A O     1 
ATOM   3751 C  CB    . TYR B 2 506 ? 110.362 78.384  101.071 1.00 54.49  ? 506 TYR A CB    1 
ATOM   3752 C  CG    . TYR B 2 506 ? 108.855 78.485  100.974 1.00 51.03  ? 506 TYR A CG    1 
ATOM   3753 C  CD1   . TYR B 2 506 ? 108.200 78.272  99.771  1.00 52.50  ? 506 TYR A CD1   1 
ATOM   3754 C  CD2   . TYR B 2 506 ? 108.086 78.806  102.085 1.00 53.92  ? 506 TYR A CD2   1 
ATOM   3755 C  CE1   . TYR B 2 506 ? 106.830 78.367  99.682  1.00 53.63  ? 506 TYR A CE1   1 
ATOM   3756 C  CE2   . TYR B 2 506 ? 106.718 78.903  101.998 1.00 52.53  ? 506 TYR A CE2   1 
ATOM   3757 C  CZ    . TYR B 2 506 ? 106.095 78.683  100.797 1.00 49.50  ? 506 TYR A CZ    1 
ATOM   3758 O  OH    . TYR B 2 506 ? 104.728 78.781  100.712 1.00 47.78  ? 506 TYR A OH    1 
ATOM   3759 N  N     . LYS B 2 507 ? 113.004 76.044  99.983  1.00 64.42  ? 507 LYS A N     1 
ATOM   3760 C  CA    . LYS B 2 507 ? 114.449 75.844  99.996  1.00 68.79  ? 507 LYS A CA    1 
ATOM   3761 C  C     . LYS B 2 507 ? 115.185 77.099  99.547  1.00 68.63  ? 507 LYS A C     1 
ATOM   3762 O  O     . LYS B 2 507 ? 116.248 77.433  100.086 1.00 70.20  ? 507 LYS A O     1 
ATOM   3763 C  CB    . LYS B 2 507 ? 114.818 74.659  99.105  1.00 71.36  ? 507 LYS A CB    1 
ATOM   3764 C  CG    . LYS B 2 507 ? 116.315 74.491  98.890  1.00 74.44  ? 507 LYS A CG    1 
ATOM   3765 C  CD    . LYS B 2 507 ? 116.745 73.031  98.927  1.00 73.26  ? 507 LYS A CD    1 
ATOM   3766 C  CE    . LYS B 2 507 ? 116.592 72.420  100.315 1.00 71.19  ? 507 LYS A CE    1 
ATOM   3767 N  NZ    . LYS B 2 507 ? 117.303 73.210  101.356 1.00 78.39  ? 507 LYS A NZ    1 
ATOM   3768 N  N     . GLY B 2 508 ? 114.640 77.804  98.556  1.00 66.80  ? 508 GLY A N     1 
ATOM   3769 C  CA    . GLY B 2 508 ? 115.278 79.027  98.099  1.00 68.54  ? 508 GLY A CA    1 
ATOM   3770 C  C     . GLY B 2 508 ? 115.402 80.057  99.203  1.00 71.96  ? 508 GLY A C     1 
ATOM   3771 O  O     . GLY B 2 508 ? 116.421 80.741  99.317  1.00 75.23  ? 508 GLY A O     1 
ATOM   3772 N  N     . ILE B 2 509 ? 114.366 80.179  100.032 1.00 69.90  ? 509 ILE A N     1 
ATOM   3773 C  CA    . ILE B 2 509 ? 114.408 81.128  101.140 1.00 67.14  ? 509 ILE A CA    1 
ATOM   3774 C  C     . ILE B 2 509 ? 115.557 80.783  102.081 1.00 73.52  ? 509 ILE A C     1 
ATOM   3775 O  O     . ILE B 2 509 ? 116.320 81.658  102.510 1.00 73.53  ? 509 ILE A O     1 
ATOM   3776 C  CB    . ILE B 2 509 ? 113.060 81.140  101.881 1.00 64.61  ? 509 ILE A CB    1 
ATOM   3777 C  CG1   . ILE B 2 509 ? 111.925 81.562  100.943 1.00 60.31  ? 509 ILE A CG1   1 
ATOM   3778 C  CG2   . ILE B 2 509 ? 113.128 82.073  103.074 1.00 70.66  ? 509 ILE A CG2   1 
ATOM   3779 C  CD1   . ILE B 2 509 ? 111.954 83.023  100.546 1.00 58.22  ? 509 ILE A CD1   1 
ATOM   3780 N  N     . TYR B 2 510 ? 115.693 79.498  102.417 1.00 77.53  ? 510 TYR A N     1 
ATOM   3781 C  CA    . TYR B 2 510 ? 116.757 79.070  103.321 1.00 79.06  ? 510 TYR A CA    1 
ATOM   3782 C  C     . TYR B 2 510 ? 118.128 79.330  102.714 1.00 81.46  ? 510 TYR A C     1 
ATOM   3783 O  O     . TYR B 2 510 ? 119.041 79.809  103.398 1.00 80.59  ? 510 TYR A O     1 
ATOM   3784 C  CB    . TYR B 2 510 ? 116.592 77.584  103.645 1.00 79.98  ? 510 TYR A CB    1 
ATOM   3785 C  CG    . TYR B 2 510 ? 117.420 77.093  104.815 1.00 85.78  ? 510 TYR A CG    1 
ATOM   3786 C  CD1   . TYR B 2 510 ? 118.803 76.992  104.732 1.00 89.54  ? 510 TYR A CD1   1 
ATOM   3787 C  CD2   . TYR B 2 510 ? 116.811 76.711  106.000 1.00 91.29  ? 510 TYR A CD2   1 
ATOM   3788 C  CE1   . TYR B 2 510 ? 119.551 76.540  105.804 1.00 97.00  ? 510 TYR A CE1   1 
ATOM   3789 C  CE2   . TYR B 2 510 ? 117.552 76.258  107.073 1.00 100.97 ? 510 TYR A CE2   1 
ATOM   3790 C  CZ    . TYR B 2 510 ? 118.921 76.176  106.969 1.00 103.44 ? 510 TYR A CZ    1 
ATOM   3791 O  OH    . TYR B 2 510 ? 119.667 75.725  108.033 1.00 104.71 ? 510 TYR A OH    1 
ATOM   3792 N  N     . LYS B 2 511 ? 118.291 79.014  101.429 1.00 81.41  ? 511 LYS A N     1 
ATOM   3793 C  CA    . LYS B 2 511 ? 119.576 79.220  100.772 1.00 81.46  ? 511 LYS A CA    1 
ATOM   3794 C  C     . LYS B 2 511 ? 119.935 80.700  100.738 1.00 80.74  ? 511 LYS A C     1 
ATOM   3795 O  O     . LYS B 2 511 ? 121.094 81.073  100.966 1.00 82.83  ? 511 LYS A O     1 
ATOM   3796 C  CB    . LYS B 2 511 ? 119.521 78.631  99.361  1.00 80.85  ? 511 LYS A CB    1 
ATOM   3797 C  CG    . LYS B 2 511 ? 120.768 78.865  98.522  1.00 84.54  ? 511 LYS A CG    1 
ATOM   3798 C  CD    . LYS B 2 511 ? 120.661 78.313  97.096  1.00 83.83  ? 511 LYS A CD    1 
ATOM   3799 C  CE    . LYS B 2 511 ? 120.119 76.891  97.022  1.00 80.56  ? 511 LYS A CE    1 
ATOM   3800 N  NZ    . LYS B 2 511 ? 119.814 76.486  95.627  1.00 75.35  ? 511 LYS A NZ    1 
ATOM   3801 N  N     . TRP B 2 512 ? 118.950 81.554  100.452 1.00 79.22  ? 512 TRP A N     1 
ATOM   3802 C  CA    . TRP B 2 512 ? 119.167 82.997  100.484 1.00 78.43  ? 512 TRP A CA    1 
ATOM   3803 C  C     . TRP B 2 512 ? 119.596 83.456  101.871 1.00 77.70  ? 512 TRP A C     1 
ATOM   3804 O  O     . TRP B 2 512 ? 120.543 84.242  102.014 1.00 77.45  ? 512 TRP A O     1 
ATOM   3805 C  CB    . TRP B 2 512 ? 117.892 83.715  100.047 1.00 74.40  ? 512 TRP A CB    1 
ATOM   3806 C  CG    . TRP B 2 512 ? 117.945 85.209  100.181 1.00 73.74  ? 512 TRP A CG    1 
ATOM   3807 C  CD1   . TRP B 2 512 ? 118.987 86.036  99.862  1.00 73.63  ? 512 TRP A CD1   1 
ATOM   3808 C  CD2   . TRP B 2 512 ? 116.894 86.057  100.662 1.00 69.96  ? 512 TRP A CD2   1 
ATOM   3809 N  NE1   . TRP B 2 512 ? 118.649 87.340  100.121 1.00 70.00  ? 512 TRP A NE1   1 
ATOM   3810 C  CE2   . TRP B 2 512 ? 117.370 87.380  100.612 1.00 66.49  ? 512 TRP A CE2   1 
ATOM   3811 C  CE3   . TRP B 2 512 ? 115.599 85.824  101.132 1.00 65.26  ? 512 TRP A CE3   1 
ATOM   3812 C  CZ2   . TRP B 2 512 ? 116.601 88.464  101.013 1.00 58.82  ? 512 TRP A CZ2   1 
ATOM   3813 C  CZ3   . TRP B 2 512 ? 114.834 86.905  101.531 1.00 57.66  ? 512 TRP A CZ3   1 
ATOM   3814 C  CH2   . TRP B 2 512 ? 115.340 88.209  101.469 1.00 55.03  ? 512 TRP A CH2   1 
ATOM   3815 N  N     . HIS B 2 513 ? 118.890 82.994  102.908 1.00 76.89  ? 513 HIS A N     1 
ATOM   3816 C  CA    . HIS B 2 513 ? 119.299 83.315  104.270 1.00 78.39  ? 513 HIS A CA    1 
ATOM   3817 C  C     . HIS B 2 513 ? 120.747 82.915  104.505 1.00 81.37  ? 513 HIS A C     1 
ATOM   3818 O  O     . HIS B 2 513 ? 121.526 83.674  105.096 1.00 82.53  ? 513 HIS A O     1 
ATOM   3819 C  CB    . HIS B 2 513 ? 118.392 82.616  105.282 1.00 76.38  ? 513 HIS A CB    1 
ATOM   3820 C  CG    . HIS B 2 513 ? 117.040 83.241  105.426 1.00 69.82  ? 513 HIS A CG    1 
ATOM   3821 N  ND1   . HIS B 2 513 ? 116.164 83.384  104.372 1.00 65.51  ? 513 HIS A ND1   1 
ATOM   3822 C  CD2   . HIS B 2 513 ? 116.414 83.761  106.507 1.00 67.07  ? 513 HIS A CD2   1 
ATOM   3823 C  CE1   . HIS B 2 513 ? 115.056 83.963  104.799 1.00 58.71  ? 513 HIS A CE1   1 
ATOM   3824 N  NE2   . HIS B 2 513 ? 115.182 84.201  106.091 1.00 57.93  ? 513 HIS A NE2   1 
ATOM   3825 N  N     . ASN B 2 514 ? 121.132 81.731  104.027 1.00 81.02  ? 514 ASN A N     1 
ATOM   3826 C  CA    . ASN B 2 514 ? 122.501 81.269  104.222 1.00 84.47  ? 514 ASN A CA    1 
ATOM   3827 C  C     . ASN B 2 514 ? 123.498 82.224  103.577 1.00 87.09  ? 514 ASN A C     1 
ATOM   3828 O  O     . ASN B 2 514 ? 124.423 82.712  104.240 1.00 84.13  ? 514 ASN A O     1 
ATOM   3829 C  CB    . ASN B 2 514 ? 122.667 79.866  103.640 1.00 85.04  ? 514 ASN A CB    1 
ATOM   3830 C  CG    . ASN B 2 514 ? 121.951 78.811  104.448 1.00 87.60  ? 514 ASN A CG    1 
ATOM   3831 O  OD1   . ASN B 2 514 ? 121.386 79.095  105.503 1.00 89.78  ? 514 ASN A OD1   1 
ATOM   3832 N  ND2   . ASN B 2 514 ? 121.984 77.576  103.962 1.00 85.48  ? 514 ASN A ND2   1 
ATOM   3833 N  N     . GLN B 2 515 ? 123.311 82.526  102.288 1.00 88.58  ? 515 GLN A N     1 
ATOM   3834 C  CA    . GLN B 2 515 ? 124.310 83.346  101.604 1.00 87.38  ? 515 GLN A CA    1 
ATOM   3835 C  C     . GLN B 2 515 ? 124.392 84.728  102.231 1.00 87.30  ? 515 GLN A C     1 
ATOM   3836 O  O     . GLN B 2 515 ? 125.489 85.272  102.404 1.00 89.78  ? 515 GLN A O     1 
ATOM   3837 C  CB    . GLN B 2 515 ? 124.043 83.493  100.100 1.00 85.68  ? 515 GLN A CB    1 
ATOM   3838 C  CG    . GLN B 2 515 ? 122.619 83.383  99.606  1.00 84.40  ? 515 GLN A CG    1 
ATOM   3839 C  CD    . GLN B 2 515 ? 122.564 83.114  98.117  1.00 90.11  ? 515 GLN A CD    1 
ATOM   3840 O  OE1   . GLN B 2 515 ? 122.719 84.025  97.305  1.00 92.48  ? 515 GLN A OE1   1 
ATOM   3841 N  NE2   . GLN B 2 515 ? 122.373 81.854  97.751  1.00 87.26  ? 515 GLN A NE2   1 
ATOM   3842 N  N     . VAL B 2 516 ? 123.246 85.318  102.578 1.00 83.90  ? 516 VAL A N     1 
ATOM   3843 C  CA    . VAL B 2 516 ? 123.295 86.649  103.170 1.00 79.52  ? 516 VAL A CA    1 
ATOM   3844 C  C     . VAL B 2 516 ? 123.986 86.596  104.523 1.00 80.70  ? 516 VAL A C     1 
ATOM   3845 O  O     . VAL B 2 516 ? 124.692 87.538  104.902 1.00 79.29  ? 516 VAL A O     1 
ATOM   3846 C  CB    . VAL B 2 516 ? 121.886 87.260  103.277 1.00 78.02  ? 516 VAL A CB    1 
ATOM   3847 C  CG1   . VAL B 2 516 ? 121.015 86.454  104.214 1.00 74.03  ? 516 VAL A CG1   1 
ATOM   3848 C  CG2   . VAL B 2 516 ? 121.975 88.713  103.726 1.00 76.64  ? 516 VAL A CG2   1 
ATOM   3849 N  N     . LYS B 2 517 ? 123.805 85.505  105.273 1.00 84.55  ? 517 LYS A N     1 
ATOM   3850 C  CA    . LYS B 2 517 ? 124.494 85.381  106.552 1.00 87.94  ? 517 LYS A CA    1 
ATOM   3851 C  C     . LYS B 2 517 ? 126.003 85.291  106.365 1.00 90.92  ? 517 LYS A C     1 
ATOM   3852 O  O     . LYS B 2 517 ? 126.763 85.946  107.088 1.00 89.35  ? 517 LYS A O     1 
ATOM   3853 C  CB    . LYS B 2 517 ? 123.977 84.159  107.310 1.00 84.83  ? 517 LYS A CB    1 
ATOM   3854 C  CG    . LYS B 2 517 ? 123.322 84.496  108.638 1.00 81.28  ? 517 LYS A CG    1 
ATOM   3855 C  CD    . LYS B 2 517 ? 122.983 83.240  109.426 1.00 87.30  ? 517 LYS A CD    1 
ATOM   3856 C  CE    . LYS B 2 517 ? 122.174 83.579  110.666 1.00 85.53  ? 517 LYS A CE    1 
ATOM   3857 N  NZ    . LYS B 2 517 ? 121.502 82.383  111.239 1.00 86.52  ? 517 LYS A NZ    1 
ATOM   3858 N  N     . GLN B 2 518 ? 126.462 84.490  105.400 1.00 90.62  ? 518 GLN A N     1 
ATOM   3859 C  CA    . GLN B 2 518 ? 127.903 84.331  105.219 1.00 90.28  ? 518 GLN A CA    1 
ATOM   3860 C  C     . GLN B 2 518 ? 128.546 85.622  104.726 1.00 89.98  ? 518 GLN A C     1 
ATOM   3861 O  O     . GLN B 2 518 ? 129.565 86.066  105.269 1.00 91.55  ? 518 GLN A O     1 
ATOM   3862 C  CB    . GLN B 2 518 ? 128.204 83.186  104.248 1.00 88.01  ? 518 GLN A CB    1 
ATOM   3863 C  CG    . GLN B 2 518 ? 127.457 81.883  104.519 1.00 87.50  ? 518 GLN A CG    1 
ATOM   3864 C  CD    . GLN B 2 518 ? 127.512 81.437  105.971 1.00 94.18  ? 518 GLN A CD    1 
ATOM   3865 O  OE1   . GLN B 2 518 ? 128.273 81.973  106.775 1.00 98.12  ? 518 GLN A OE1   1 
ATOM   3866 N  NE2   . GLN B 2 518 ? 126.699 80.444  106.312 1.00 93.96  ? 518 GLN A NE2   1 
ATOM   3867 N  N     . LYS B 2 519 ? 127.966 86.242  103.702 1.00 88.42  ? 519 LYS A N     1 
ATOM   3868 C  CA    . LYS B 2 519 ? 128.574 87.426  103.112 1.00 90.10  ? 519 LYS A CA    1 
ATOM   3869 C  C     . LYS B 2 519 ? 128.422 88.633  104.031 1.00 90.39  ? 519 LYS A C     1 
ATOM   3870 O  O     . LYS B 2 519 ? 127.400 88.802  104.702 1.00 89.99  ? 519 LYS A O     1 
ATOM   3871 C  CB    . LYS B 2 519 ? 127.951 87.723  101.748 1.00 92.28  ? 519 LYS A CB    1 
ATOM   3872 C  CG    . LYS B 2 519 ? 128.635 87.011  100.594 1.00 95.60  ? 519 LYS A CG    1 
ATOM   3873 C  CD    . LYS B 2 519 ? 127.864 87.180  99.297  1.00 94.08  ? 519 LYS A CD    1 
ATOM   3874 C  CE    . LYS B 2 519 ? 126.892 86.033  99.071  1.00 94.29  ? 519 LYS A CE    1 
ATOM   3875 N  NZ    . LYS B 2 519 ? 127.584 84.737  98.837  1.00 91.20  ? 519 LYS A NZ    1 
ATOM   3876 N  N     . ARG B 2 520 ? 129.454 89.475  104.054 1.00 90.19  ? 520 ARG A N     1 
ATOM   3877 C  CA    . ARG B 2 520 ? 129.484 90.704  104.842 1.00 90.68  ? 520 ARG A CA    1 
ATOM   3878 C  C     . ARG B 2 520 ? 129.954 91.869  103.980 1.00 92.76  ? 520 ARG A C     1 
ATOM   3879 O  O     . ARG B 2 520 ? 130.789 92.683  104.382 1.00 94.03  ? 520 ARG A O     1 
ATOM   3880 C  CB    . ARG B 2 520 ? 130.388 90.558  106.064 1.00 89.29  ? 520 ARG A CB    1 
ATOM   3881 C  CG    . ARG B 2 520 ? 130.213 89.261  106.841 1.00 90.65  ? 520 ARG A CG    1 
ATOM   3882 C  CD    . ARG B 2 520 ? 128.899 89.238  107.603 1.00 90.18  ? 520 ARG A CD    1 
ATOM   3883 N  NE    . ARG B 2 520 ? 129.045 88.624  108.917 1.00 88.92  ? 520 ARG A NE    1 
ATOM   3884 C  CZ    . ARG B 2 520 ? 129.457 89.265  110.004 1.00 89.71  ? 520 ARG A CZ    1 
ATOM   3885 N  NH1   . ARG B 2 520 ? 129.790 90.545  109.971 1.00 90.48  ? 520 ARG A NH1   1 
ATOM   3886 N  NH2   . ARG B 2 520 ? 129.541 88.602  111.154 1.00 86.34  ? 520 ARG A NH2   1 
ATOM   3887 N  N     . ALA B 2 521 ? 129.410 91.963  102.765 1.00 92.16  ? 521 ALA A N     1 
ATOM   3888 C  CA    . ALA B 2 521 ? 129.857 92.994  101.833 1.00 93.25  ? 521 ALA A CA    1 
ATOM   3889 C  C     . ALA B 2 521 ? 129.489 94.393  102.311 1.00 92.35  ? 521 ALA A C     1 
ATOM   3890 O  O     . ALA B 2 521 ? 130.203 95.355  102.008 1.00 90.56  ? 521 ALA A O     1 
ATOM   3891 C  CB    . ALA B 2 521 ? 129.263 92.742  100.448 1.00 89.78  ? 521 ALA A CB    1 
ATOM   3892 N  N     . LEU B 2 522 ? 128.385 94.528  103.044 1.00 90.73  ? 522 LEU A N     1 
ATOM   3893 C  CA    . LEU B 2 522 ? 127.865 95.786  103.571 1.00 88.01  ? 522 LEU A CA    1 
ATOM   3894 C  C     . LEU B 2 522 ? 127.276 96.683  102.489 1.00 86.68  ? 522 LEU A C     1 
ATOM   3895 O  O     . LEU B 2 522 ? 126.738 97.747  102.818 1.00 83.46  ? 522 LEU A O     1 
ATOM   3896 C  CB    . LEU B 2 522 ? 128.933 96.583  104.335 1.00 87.77  ? 522 LEU A CB    1 
ATOM   3897 C  CG    . LEU B 2 522 ? 129.621 95.856  105.490 1.00 89.06  ? 522 LEU A CG    1 
ATOM   3898 C  CD1   . LEU B 2 522 ? 130.760 96.698  106.036 1.00 93.65  ? 522 LEU A CD1   1 
ATOM   3899 C  CD2   . LEU B 2 522 ? 128.625 95.529  106.590 1.00 88.28  ? 522 LEU A CD2   1 
ATOM   3900 N  N     . GLN B 2 523 ? 127.347 96.294  101.219 1.00 86.24  ? 523 GLN A N     1 
ATOM   3901 C  CA    . GLN B 2 523 ? 126.750 97.047  100.123 1.00 81.30  ? 523 GLN A CA    1 
ATOM   3902 C  C     . GLN B 2 523 ? 125.538 96.283  99.609  1.00 73.91  ? 523 GLN A C     1 
ATOM   3903 O  O     . GLN B 2 523 ? 125.646 95.099  99.275  1.00 76.31  ? 523 GLN A O     1 
ATOM   3904 C  CB    . GLN B 2 523 ? 127.754 97.266  98.988  1.00 83.43  ? 523 GLN A CB    1 
ATOM   3905 C  CG    . GLN B 2 523 ? 129.198 97.460  99.435  1.00 87.92  ? 523 GLN A CG    1 
ATOM   3906 C  CD    . GLN B 2 523 ? 129.378 98.644  100.365 1.00 90.13  ? 523 GLN A CD    1 
ATOM   3907 O  OE1   . GLN B 2 523 ? 129.197 99.791  99.965  1.00 84.41  ? 523 GLN A OE1   1 
ATOM   3908 N  NE2   . GLN B 2 523 ? 129.748 98.370  101.609 1.00 91.00  ? 523 GLN A NE2   1 
ATOM   3909 N  N     . TYR B 2 524 ? 124.394 96.958  99.540  1.00 66.74  ? 524 TYR A N     1 
ATOM   3910 C  CA    . TYR B 2 524 ? 123.141 96.323  99.160  1.00 62.67  ? 524 TYR A CA    1 
ATOM   3911 C  C     . TYR B 2 524 ? 122.434 97.169  98.112  1.00 61.07  ? 524 TYR A C     1 
ATOM   3912 O  O     . TYR B 2 524 ? 122.769 98.335  97.887  1.00 61.50  ? 524 TYR A O     1 
ATOM   3913 C  CB    . TYR B 2 524 ? 122.239 96.111  100.381 1.00 62.13  ? 524 TYR A CB    1 
ATOM   3914 C  CG    . TYR B 2 524 ? 122.718 95.006  101.291 1.00 67.04  ? 524 TYR A CG    1 
ATOM   3915 C  CD1   . TYR B 2 524 ? 123.737 95.228  102.209 1.00 68.52  ? 524 TYR A CD1   1 
ATOM   3916 C  CD2   . TYR B 2 524 ? 122.157 93.737  101.231 1.00 68.11  ? 524 TYR A CD2   1 
ATOM   3917 C  CE1   . TYR B 2 524 ? 124.179 94.221  103.040 1.00 67.76  ? 524 TYR A CE1   1 
ATOM   3918 C  CE2   . TYR B 2 524 ? 122.596 92.727  102.057 1.00 66.40  ? 524 TYR A CE2   1 
ATOM   3919 C  CZ    . TYR B 2 524 ? 123.608 92.972  102.958 1.00 65.27  ? 524 TYR A CZ    1 
ATOM   3920 O  OH    . TYR B 2 524 ? 124.042 91.964  103.785 1.00 66.50  ? 524 TYR A OH    1 
ATOM   3921 N  N     . SER B 2 525 ? 121.446 96.562  97.460  1.00 60.68  ? 525 SER A N     1 
ATOM   3922 C  CA    . SER B 2 525 ? 120.740 97.215  96.366  1.00 61.20  ? 525 SER A CA    1 
ATOM   3923 C  C     . SER B 2 525 ? 119.381 96.555  96.193  1.00 55.22  ? 525 SER A C     1 
ATOM   3924 O  O     . SER B 2 525 ? 119.118 95.474  96.724  1.00 53.62  ? 525 SER A O     1 
ATOM   3925 C  CB    . SER B 2 525 ? 121.540 97.133  95.066  1.00 61.79  ? 525 SER A CB    1 
ATOM   3926 O  OG    . SER B 2 525 ? 121.769 95.784  94.694  1.00 55.29  ? 525 SER A OG    1 
ATOM   3927 N  N     . THR B 2 526 ? 118.520 97.226  95.434  1.00 49.14  ? 526 THR A N     1 
ATOM   3928 C  CA    . THR B 2 526 ? 117.225 96.700  95.040  1.00 40.85  ? 526 THR A CA    1 
ATOM   3929 C  C     . THR B 2 526 ? 117.228 96.471  93.531  1.00 46.89  ? 526 THR A C     1 
ATOM   3930 O  O     . THR B 2 526 ? 118.256 96.621  92.859  1.00 52.17  ? 526 THR A O     1 
ATOM   3931 C  CB    . THR B 2 526 ? 116.085 97.636  95.461  1.00 36.76  ? 526 THR A CB    1 
ATOM   3932 O  OG1   . THR B 2 526 ? 115.858 98.610  94.438  1.00 43.05  ? 526 THR A OG1   1 
ATOM   3933 C  CG2   . THR B 2 526 ? 116.369 98.343  96.783  1.00 44.01  ? 526 THR A CG2   1 
ATOM   3934 N  N     . LEU B 2 527 ? 116.067 96.105  92.989  1.00 44.93  ? 527 LEU A N     1 
ATOM   3935 C  CA    . LEU B 2 527 ? 115.987 95.730  91.583  1.00 44.72  ? 527 LEU A CA    1 
ATOM   3936 C  C     . LEU B 2 527 ? 116.207 96.900  90.634  1.00 46.04  ? 527 LEU A C     1 
ATOM   3937 O  O     . LEU B 2 527 ? 116.343 96.670  89.428  1.00 45.18  ? 527 LEU A O     1 
ATOM   3938 C  CB    . LEU B 2 527 ? 114.635 95.076  91.290  1.00 40.71  ? 527 LEU A CB    1 
ATOM   3939 C  CG    . LEU B 2 527 ? 114.447 93.646  91.814  1.00 38.59  ? 527 LEU A CG    1 
ATOM   3940 C  CD1   . LEU B 2 527 ? 113.152 93.056  91.292  1.00 39.07  ? 527 LEU A CD1   1 
ATOM   3941 C  CD2   . LEU B 2 527 ? 115.621 92.754  91.435  1.00 38.83  ? 527 LEU A CD2   1 
ATOM   3942 N  N     . SER B 2 528 ? 116.239 98.136  91.129  1.00 43.59  ? 528 SER A N     1 
ATOM   3943 C  CA    . SER B 2 528 ? 116.531 99.300  90.302  1.00 39.91  ? 528 SER A CA    1 
ATOM   3944 C  C     . SER B 2 528 ? 117.880 99.921  90.655  1.00 45.67  ? 528 SER A C     1 
ATOM   3945 O  O     . SER B 2 528 ? 118.100 101.112 90.426  1.00 50.92  ? 528 SER A O     1 
ATOM   3946 C  CB    . SER B 2 528 ? 115.424 100.342 90.426  1.00 35.89  ? 528 SER A CB    1 
ATOM   3947 O  OG    . SER B 2 528 ? 115.657 101.187 91.536  1.00 40.60  ? 528 SER A OG    1 
ATOM   3948 N  N     . ASN B 2 529 ? 118.788 99.125  91.218  1.00 47.70  ? 529 ASN A N     1 
ATOM   3949 C  CA    . ASN B 2 529 ? 120.160 99.558  91.482  1.00 53.05  ? 529 ASN A CA    1 
ATOM   3950 C  C     . ASN B 2 529 ? 120.218 100.748 92.434  1.00 57.89  ? 529 ASN A C     1 
ATOM   3951 O  O     . ASN B 2 529 ? 121.097 101.605 92.318  1.00 63.84  ? 529 ASN A O     1 
ATOM   3952 C  CB    . ASN B 2 529 ? 120.888 99.892  90.179  1.00 57.33  ? 529 ASN A CB    1 
ATOM   3953 C  CG    . ASN B 2 529 ? 120.652 98.857  89.101  1.00 59.72  ? 529 ASN A CG    1 
ATOM   3954 O  OD1   . ASN B 2 529 ? 120.261 97.727  89.389  1.00 58.48  ? 529 ASN A OD1   1 
ATOM   3955 N  ND2   . ASN B 2 529 ? 120.892 99.235  87.850  1.00 61.90  ? 529 ASN A ND2   1 
ATOM   3956 N  N     . ARG B 2 530 ? 119.291 100.813 93.387  1.00 54.57  ? 530 ARG A N     1 
ATOM   3957 C  CA    . ARG B 2 530 ? 119.316 101.848 94.420  1.00 52.17  ? 530 ARG A CA    1 
ATOM   3958 C  C     . ARG B 2 530 ? 120.315 101.423 95.490  1.00 57.61  ? 530 ARG A C     1 
ATOM   3959 O  O     . ARG B 2 530 ? 119.959 100.831 96.510  1.00 59.38  ? 530 ARG A O     1 
ATOM   3960 C  CB    . ARG B 2 530 ? 117.925 102.069 94.997  1.00 43.11  ? 530 ARG A CB    1 
ATOM   3961 C  CG    . ARG B 2 530 ? 117.847 103.249 95.944  1.00 44.14  ? 530 ARG A CG    1 
ATOM   3962 C  CD    . ARG B 2 530 ? 116.611 103.190 96.818  1.00 49.99  ? 530 ARG A CD    1 
ATOM   3963 N  NE    . ARG B 2 530 ? 115.383 103.359 96.049  1.00 47.07  ? 530 ARG A NE    1 
ATOM   3964 C  CZ    . ARG B 2 530 ? 114.749 104.514 95.893  1.00 51.83  ? 530 ARG A CZ    1 
ATOM   3965 N  NH1   . ARG B 2 530 ? 115.219 105.639 96.408  1.00 53.27  ? 530 ARG A NH1   1 
ATOM   3966 N  NH2   . ARG B 2 530 ? 113.615 104.544 95.199  1.00 44.77  ? 530 ARG A NH2   1 
ATOM   3967 N  N     . LYS B 2 531 ? 121.585 101.748 95.259  1.00 61.77  ? 531 LYS A N     1 
ATOM   3968 C  CA    . LYS B 2 531 ? 122.660 101.248 96.104  1.00 63.64  ? 531 LYS A CA    1 
ATOM   3969 C  C     . LYS B 2 531 ? 122.647 101.925 97.471  1.00 65.46  ? 531 LYS A C     1 
ATOM   3970 O  O     . LYS B 2 531 ? 122.290 103.098 97.608  1.00 61.93  ? 531 LYS A O     1 
ATOM   3971 C  CB    . LYS B 2 531 ? 124.019 101.477 95.437  1.00 64.36  ? 531 LYS A CB    1 
ATOM   3972 C  CG    . LYS B 2 531 ? 124.068 101.156 93.949  1.00 59.84  ? 531 LYS A CG    1 
ATOM   3973 C  CD    . LYS B 2 531 ? 123.786 99.683  93.670  1.00 61.57  ? 531 LYS A CD    1 
ATOM   3974 C  CE    . LYS B 2 531 ? 125.062 98.862  93.542  1.00 70.69  ? 531 LYS A CE    1 
ATOM   3975 N  NZ    . LYS B 2 531 ? 124.910 97.764  92.551  1.00 72.17  ? 531 LYS A NZ    1 
ATOM   3976 N  N     . VAL B 2 532 ? 123.054 101.167 98.488  1.00 63.42  ? 532 VAL A N     1 
ATOM   3977 C  CA    . VAL B 2 532 ? 123.140 101.654 99.862  1.00 60.20  ? 532 VAL A CA    1 
ATOM   3978 C  C     . VAL B 2 532 ? 124.392 101.076 100.505 1.00 68.87  ? 532 VAL A C     1 
ATOM   3979 O  O     . VAL B 2 532 ? 124.726 99.906  100.294 1.00 76.57  ? 532 VAL A O     1 
ATOM   3980 C  CB    . VAL B 2 532 ? 121.896 101.269 100.686 1.00 57.04  ? 532 VAL A CB    1 
ATOM   3981 C  CG1   . VAL B 2 532 ? 121.553 99.807  100.475 1.00 63.72  ? 532 VAL A CG1   1 
ATOM   3982 C  CG2   . VAL B 2 532 ? 122.130 101.548 102.158 1.00 55.98  ? 532 VAL A CG2   1 
ATOM   3983 N  N     . ILE B 2 533 ? 125.081 101.895 101.294 1.00 69.28  ? 533 ILE A N     1 
ATOM   3984 C  CA    . ILE B 2 533 ? 126.249 101.467 102.057 1.00 77.02  ? 533 ILE A CA    1 
ATOM   3985 C  C     . ILE B 2 533 ? 125.839 101.416 103.522 1.00 76.64  ? 533 ILE A C     1 
ATOM   3986 O  O     . ILE B 2 533 ? 125.668 102.459 104.165 1.00 77.40  ? 533 ILE A O     1 
ATOM   3987 C  CB    . ILE B 2 533 ? 127.449 102.401 101.848 1.00 83.54  ? 533 ILE A CB    1 
ATOM   3988 C  CG1   . ILE B 2 533 ? 127.689 102.637 100.354 1.00 81.89  ? 533 ILE A CG1   1 
ATOM   3989 C  CG2   . ILE B 2 533 ? 128.693 101.818 102.511 1.00 83.80  ? 533 ILE A CG2   1 
ATOM   3990 C  CD1   . ILE B 2 533 ? 128.807 103.614 100.055 1.00 84.72  ? 533 ILE A CD1   1 
ATOM   3991 N  N     . PHE B 2 534 ? 125.681 100.207 104.055 1.00 78.89  ? 534 PHE A N     1 
ATOM   3992 C  CA    . PHE B 2 534 ? 125.296 100.054 105.448 1.00 78.92  ? 534 PHE A CA    1 
ATOM   3993 C  C     . PHE B 2 534 ? 126.461 100.432 106.364 1.00 81.66  ? 534 PHE A C     1 
ATOM   3994 O  O     . PHE B 2 534 ? 127.627 100.306 105.981 1.00 86.07  ? 534 PHE A O     1 
ATOM   3995 C  CB    . PHE B 2 534 ? 124.867 98.614  105.731 1.00 78.51  ? 534 PHE A CB    1 
ATOM   3996 C  CG    . PHE B 2 534 ? 123.388 98.366  105.579 1.00 71.15  ? 534 PHE A CG    1 
ATOM   3997 C  CD1   . PHE B 2 534 ? 122.456 99.280  106.034 1.00 68.41  ? 534 PHE A CD1   1 
ATOM   3998 C  CD2   . PHE B 2 534 ? 122.934 97.207  104.976 1.00 65.93  ? 534 PHE A CD2   1 
ATOM   3999 C  CE1   . PHE B 2 534 ? 121.108 99.043  105.890 1.00 67.28  ? 534 PHE A CE1   1 
ATOM   4000 C  CE2   . PHE B 2 534 ? 121.588 96.968  104.831 1.00 61.58  ? 534 PHE A CE2   1 
ATOM   4001 C  CZ    . PHE B 2 534 ? 120.675 97.885  105.288 1.00 61.86  ? 534 PHE A CZ    1 
ATOM   4002 N  N     . PRO B 2 535 ? 126.175 100.902 107.584 1.00 79.87  ? 535 PRO A N     1 
ATOM   4003 C  CA    . PRO B 2 535 ? 127.267 101.206 108.520 1.00 82.00  ? 535 PRO A CA    1 
ATOM   4004 C  C     . PRO B 2 535 ? 127.836 99.947  109.155 1.00 83.65  ? 535 PRO A C     1 
ATOM   4005 O  O     . PRO B 2 535 ? 129.051 99.827  109.340 1.00 83.09  ? 535 PRO A O     1 
ATOM   4006 C  CB    . PRO B 2 535 ? 126.607 102.118 109.562 1.00 78.48  ? 535 PRO A CB    1 
ATOM   4007 C  CG    . PRO B 2 535 ? 125.126 101.906 109.423 1.00 75.80  ? 535 PRO A CG    1 
ATOM   4008 C  CD    . PRO B 2 535 ? 124.845 101.115 108.181 1.00 75.30  ? 535 PRO A CD    1 
ATOM   4009 N  N     . TYR B 2 536 ? 126.959 99.000  109.487 1.00 82.91  ? 536 TYR A N     1 
ATOM   4010 C  CA    . TYR B 2 536 ? 127.368 97.704  110.005 1.00 79.78  ? 536 TYR A CA    1 
ATOM   4011 C  C     . TYR B 2 536 ? 126.464 96.635  109.410 1.00 78.75  ? 536 TYR A C     1 
ATOM   4012 O  O     . TYR B 2 536 ? 125.354 96.919  108.954 1.00 81.97  ? 536 TYR A O     1 
ATOM   4013 C  CB    . TYR B 2 536 ? 127.322 97.658  111.542 1.00 80.08  ? 536 TYR A CB    1 
ATOM   4014 C  CG    . TYR B 2 536 ? 126.031 98.149  112.172 1.00 81.65  ? 536 TYR A CG    1 
ATOM   4015 C  CD1   . TYR B 2 536 ? 124.799 97.602  111.823 1.00 79.93  ? 536 TYR A CD1   1 
ATOM   4016 C  CD2   . TYR B 2 536 ? 126.046 99.158  113.129 1.00 81.58  ? 536 TYR A CD2   1 
ATOM   4017 C  CE1   . TYR B 2 536 ? 123.625 98.047  112.405 1.00 78.81  ? 536 TYR A CE1   1 
ATOM   4018 C  CE2   . TYR B 2 536 ? 124.878 99.609  113.713 1.00 82.55  ? 536 TYR A CE2   1 
ATOM   4019 C  CZ    . TYR B 2 536 ? 123.671 99.052  113.347 1.00 83.71  ? 536 TYR A CZ    1 
ATOM   4020 O  OH    . TYR B 2 536 ? 122.511 99.503  113.932 1.00 82.49  ? 536 TYR A OH    1 
ATOM   4021 N  N     . PHE B 2 537 ? 126.946 95.395  109.423 1.00 77.23  ? 537 PHE A N     1 
ATOM   4022 C  CA    . PHE B 2 537 ? 126.176 94.276  108.892 1.00 76.76  ? 537 PHE A CA    1 
ATOM   4023 C  C     . PHE B 2 537 ? 125.062 93.929  109.870 1.00 77.04  ? 537 PHE A C     1 
ATOM   4024 O  O     . PHE B 2 537 ? 125.313 93.340  110.926 1.00 80.60  ? 537 PHE A O     1 
ATOM   4025 C  CB    . PHE B 2 537 ? 127.068 93.062  108.650 1.00 79.18  ? 537 PHE A CB    1 
ATOM   4026 C  CG    . PHE B 2 537 ? 126.317 91.856  108.156 1.00 80.90  ? 537 PHE A CG    1 
ATOM   4027 C  CD1   . PHE B 2 537 ? 126.036 91.699  106.809 1.00 83.18  ? 537 PHE A CD1   1 
ATOM   4028 C  CD2   . PHE B 2 537 ? 125.870 90.890  109.040 1.00 79.21  ? 537 PHE A CD2   1 
ATOM   4029 C  CE1   . PHE B 2 537 ? 125.340 90.598  106.357 1.00 82.45  ? 537 PHE A CE1   1 
ATOM   4030 C  CE2   . PHE B 2 537 ? 125.172 89.790  108.591 1.00 78.20  ? 537 PHE A CE2   1 
ATOM   4031 C  CZ    . PHE B 2 537 ? 124.907 89.644  107.249 1.00 79.67  ? 537 PHE A CZ    1 
ATOM   4032 N  N     . SER B 2 538 ? 123.832 94.291  109.522 1.00 73.08  ? 538 SER A N     1 
ATOM   4033 C  CA    . SER B 2 538 ? 122.649 93.878  110.263 1.00 74.57  ? 538 SER A CA    1 
ATOM   4034 C  C     . SER B 2 538 ? 121.872 92.883  109.412 1.00 72.47  ? 538 SER A C     1 
ATOM   4035 O  O     . SER B 2 538 ? 121.458 93.205  108.293 1.00 68.14  ? 538 SER A O     1 
ATOM   4036 C  CB    . SER B 2 538 ? 121.777 95.074  110.632 1.00 74.66  ? 538 SER A CB    1 
ATOM   4037 O  OG    . SER B 2 538 ? 120.459 94.656  110.947 1.00 72.71  ? 538 SER A OG    1 
ATOM   4038 N  N     . PHE B 2 539 ? 121.680 91.680  109.949 1.00 76.40  ? 539 PHE A N     1 
ATOM   4039 C  CA    . PHE B 2 539 ? 121.097 90.591  109.174 1.00 71.55  ? 539 PHE A CA    1 
ATOM   4040 C  C     . PHE B 2 539 ? 119.704 90.963  108.677 1.00 67.76  ? 539 PHE A C     1 
ATOM   4041 O  O     . PHE B 2 539 ? 119.435 90.963  107.469 1.00 68.95  ? 539 PHE A O     1 
ATOM   4042 C  CB    . PHE B 2 539 ? 121.061 89.332  110.046 1.00 74.75  ? 539 PHE A CB    1 
ATOM   4043 C  CG    . PHE B 2 539 ? 120.321 88.173  109.439 1.00 78.84  ? 539 PHE A CG    1 
ATOM   4044 C  CD1   . PHE B 2 539 ? 120.874 87.451  108.397 1.00 82.30  ? 539 PHE A CD1   1 
ATOM   4045 C  CD2   . PHE B 2 539 ? 119.086 87.784  109.930 1.00 80.45  ? 539 PHE A CD2   1 
ATOM   4046 C  CE1   . PHE B 2 539 ? 120.205 86.375  107.850 1.00 79.35  ? 539 PHE A CE1   1 
ATOM   4047 C  CE2   . PHE B 2 539 ? 118.414 86.712  109.383 1.00 75.31  ? 539 PHE A CE2   1 
ATOM   4048 C  CZ    . PHE B 2 539 ? 118.974 86.007  108.342 1.00 75.40  ? 539 PHE A CZ    1 
ATOM   4049 N  N     . THR B 2 540 ? 118.810 91.326  109.600 1.00 65.19  ? 540 THR A N     1 
ATOM   4050 C  CA    . THR B 2 540 ? 117.430 91.588  109.209 1.00 61.64  ? 540 THR A CA    1 
ATOM   4051 C  C     . THR B 2 540 ? 117.325 92.869  108.391 1.00 62.92  ? 540 THR A C     1 
ATOM   4052 O  O     . THR B 2 540 ? 116.545 92.935  107.436 1.00 64.20  ? 540 THR A O     1 
ATOM   4053 C  CB    . THR B 2 540 ? 116.540 91.650  110.448 1.00 59.11  ? 540 THR A CB    1 
ATOM   4054 O  OG1   . THR B 2 540 ? 116.642 90.412  111.159 1.00 62.31  ? 540 THR A OG1   1 
ATOM   4055 C  CG2   . THR B 2 540 ? 115.080 91.845  110.064 1.00 55.33  ? 540 THR A CG2   1 
ATOM   4056 N  N     . LYS B 2 541 ? 118.110 93.894  108.731 1.00 61.74  ? 541 LYS A N     1 
ATOM   4057 C  CA    . LYS B 2 541 ? 118.119 95.098  107.904 1.00 65.96  ? 541 LYS A CA    1 
ATOM   4058 C  C     . LYS B 2 541 ? 118.580 94.773  106.491 1.00 67.12  ? 541 LYS A C     1 
ATOM   4059 O  O     . LYS B 2 541 ? 118.022 95.282  105.508 1.00 64.20  ? 541 LYS A O     1 
ATOM   4060 C  CB    . LYS B 2 541 ? 119.024 96.166  108.525 1.00 67.37  ? 541 LYS A CB    1 
ATOM   4061 C  CG    . LYS B 2 541 ? 118.383 97.000  109.626 1.00 64.59  ? 541 LYS A CG    1 
ATOM   4062 C  CD    . LYS B 2 541 ? 119.416 97.643  110.546 1.00 65.60  ? 541 LYS A CD    1 
ATOM   4063 C  CE    . LYS B 2 541 ? 119.916 98.971  110.020 1.00 68.72  ? 541 LYS A CE    1 
ATOM   4064 N  NZ    . LYS B 2 541 ? 121.024 99.488  110.856 1.00 75.20  ? 541 LYS A NZ    1 
ATOM   4065 N  N     . ALA B 2 542 ? 119.605 93.927  106.371 1.00 67.96  ? 542 ALA A N     1 
ATOM   4066 C  CA    . ALA B 2 542 ? 120.103 93.540  105.058 1.00 61.04  ? 542 ALA A CA    1 
ATOM   4067 C  C     . ALA B 2 542 ? 119.036 92.813  104.257 1.00 55.74  ? 542 ALA A C     1 
ATOM   4068 O  O     . ALA B 2 542 ? 118.850 93.087  103.066 1.00 55.10  ? 542 ALA A O     1 
ATOM   4069 C  CB    . ALA B 2 542 ? 121.341 92.662  105.214 1.00 65.87  ? 542 ALA A CB    1 
ATOM   4070 N  N     . LEU B 2 543 ? 118.325 91.879  104.887 1.00 57.78  ? 543 LEU A N     1 
ATOM   4071 C  CA    . LEU B 2 543 ? 117.266 91.184  104.164 1.00 58.27  ? 543 LEU A CA    1 
ATOM   4072 C  C     . LEU B 2 543 ? 116.110 92.111  103.820 1.00 55.21  ? 543 LEU A C     1 
ATOM   4073 O  O     . LEU B 2 543 ? 115.430 91.900  102.810 1.00 54.69  ? 543 LEU A O     1 
ATOM   4074 C  CB    . LEU B 2 543 ? 116.749 89.997  104.972 1.00 56.36  ? 543 LEU A CB    1 
ATOM   4075 C  CG    . LEU B 2 543 ? 117.577 88.716  104.898 1.00 63.67  ? 543 LEU A CG    1 
ATOM   4076 C  CD1   . LEU B 2 543 ? 118.703 88.742  105.891 1.00 71.71  ? 543 LEU A CD1   1 
ATOM   4077 C  CD2   . LEU B 2 543 ? 116.683 87.512  105.134 1.00 65.29  ? 543 LEU A CD2   1 
ATOM   4078 N  N     . ASN B 2 544 ? 115.860 93.129  104.642 1.00 51.66  ? 544 ASN A N     1 
ATOM   4079 C  CA    . ASN B 2 544 ? 114.666 93.940  104.446 1.00 50.54  ? 544 ASN A CA    1 
ATOM   4080 C  C     . ASN B 2 544 ? 114.871 95.071  103.444 1.00 57.74  ? 544 ASN A C     1 
ATOM   4081 O  O     . ASN B 2 544 ? 113.905 95.487  102.794 1.00 55.30  ? 544 ASN A O     1 
ATOM   4082 C  CB    . ASN B 2 544 ? 114.201 94.520  105.778 1.00 48.25  ? 544 ASN A CB    1 
ATOM   4083 C  CG    . ASN B 2 544 ? 113.013 95.431  105.615 1.00 47.98  ? 544 ASN A CG    1 
ATOM   4084 O  OD1   . ASN B 2 544 ? 113.158 96.651  105.555 1.00 54.33  ? 544 ASN A OD1   1 
ATOM   4085 N  ND2   . ASN B 2 544 ? 111.827 94.844  105.518 1.00 42.10  ? 544 ASN A ND2   1 
ATOM   4086 N  N     . TYR B 2 545 ? 116.090 95.592  103.305 1.00 58.27  ? 545 TYR A N     1 
ATOM   4087 C  CA    . TYR B 2 545 ? 116.292 96.712  102.385 1.00 51.32  ? 545 TYR A CA    1 
ATOM   4088 C  C     . TYR B 2 545 ? 115.858 96.402  100.960 1.00 47.57  ? 545 TYR A C     1 
ATOM   4089 O  O     . TYR B 2 545 ? 115.090 97.196  100.388 1.00 46.92  ? 545 TYR A O     1 
ATOM   4090 C  CB    . TYR B 2 545 ? 117.757 97.162  102.415 1.00 52.55  ? 545 TYR A CB    1 
ATOM   4091 C  CG    . TYR B 2 545 ? 118.012 98.447  101.649 1.00 52.36  ? 545 TYR A CG    1 
ATOM   4092 C  CD1   . TYR B 2 545 ? 118.176 98.430  100.270 1.00 50.01  ? 545 TYR A CD1   1 
ATOM   4093 C  CD2   . TYR B 2 545 ? 118.088 99.672  102.299 1.00 59.23  ? 545 TYR A CD2   1 
ATOM   4094 C  CE1   . TYR B 2 545 ? 118.406 99.593  99.566  1.00 54.20  ? 545 TYR A CE1   1 
ATOM   4095 C  CE2   . TYR B 2 545 ? 118.318 100.840 101.597 1.00 54.90  ? 545 TYR A CE2   1 
ATOM   4096 C  CZ    . TYR B 2 545 ? 118.476 100.794 100.235 1.00 51.74  ? 545 TYR A CZ    1 
ATOM   4097 O  OH    . TYR B 2 545 ? 118.707 101.954 99.540  1.00 49.07  ? 545 TYR A OH    1 
ATOM   4098 N  N     . PRO B 2 546 ? 116.290 95.303  100.330 1.00 46.66  ? 546 PRO A N     1 
ATOM   4099 C  CA    . PRO B 2 546 ? 115.997 95.131  98.897  1.00 47.65  ? 546 PRO A CA    1 
ATOM   4100 C  C     . PRO B 2 546 ? 114.515 95.083  98.576  1.00 45.28  ? 546 PRO A C     1 
ATOM   4101 O  O     . PRO B 2 546 ? 114.070 95.733  97.620  1.00 51.08  ? 546 PRO A O     1 
ATOM   4102 C  CB    . PRO B 2 546 ? 116.692 93.800  98.559  1.00 45.46  ? 546 PRO A CB    1 
ATOM   4103 C  CG    . PRO B 2 546 ? 117.764 93.673  99.585  1.00 46.44  ? 546 PRO A CG    1 
ATOM   4104 C  CD    . PRO B 2 546 ? 117.119 94.201  100.834 1.00 46.70  ? 546 PRO A CD    1 
ATOM   4105 N  N     . VAL B 2 547 ? 113.730 94.348  99.361  1.00 39.22  ? 547 VAL A N     1 
ATOM   4106 C  CA    . VAL B 2 547 ? 112.331 94.141  99.006  1.00 39.24  ? 547 VAL A CA    1 
ATOM   4107 C  C     . VAL B 2 547 ? 111.563 95.453  99.106  1.00 41.21  ? 547 VAL A C     1 
ATOM   4108 O  O     . VAL B 2 547 ? 110.830 95.834  98.185  1.00 44.26  ? 547 VAL A O     1 
ATOM   4109 C  CB    . VAL B 2 547 ? 111.705 93.046  99.890  1.00 40.94  ? 547 VAL A CB    1 
ATOM   4110 C  CG1   . VAL B 2 547 ? 110.376 92.585  99.311  1.00 38.92  ? 547 VAL A CG1   1 
ATOM   4111 C  CG2   . VAL B 2 547 ? 112.651 91.867  100.033 1.00 40.74  ? 547 VAL A CG2   1 
ATOM   4112 N  N     . GLN B 2 548 ? 111.728 96.172  100.218 1.00 38.99  ? 548 GLN A N     1 
ATOM   4113 C  CA    . GLN B 2 548 ? 111.003 97.428  100.381 1.00 42.66  ? 548 GLN A CA    1 
ATOM   4114 C  C     . GLN B 2 548 ? 111.503 98.500  99.420  1.00 47.32  ? 548 GLN A C     1 
ATOM   4115 O  O     . GLN B 2 548 ? 110.706 99.314  98.937  1.00 47.39  ? 548 GLN A O     1 
ATOM   4116 C  CB    . GLN B 2 548 ? 111.100 97.911  101.826 1.00 43.41  ? 548 GLN A CB    1 
ATOM   4117 C  CG    . GLN B 2 548 ? 110.175 97.158  102.764 1.00 48.69  ? 548 GLN A CG    1 
ATOM   4118 C  CD    . GLN B 2 548 ? 110.057 97.812  104.127 1.00 50.74  ? 548 GLN A CD    1 
ATOM   4119 O  OE1   . GLN B 2 548 ? 110.435 98.970  104.305 1.00 44.34  ? 548 GLN A OE1   1 
ATOM   4120 N  NE2   . GLN B 2 548 ? 109.522 97.074  105.096 1.00 44.89  ? 548 GLN A NE2   1 
ATOM   4121 N  N     . GLY B 2 549 ? 112.801 98.518  99.117  1.00 47.06  ? 549 GLY A N     1 
ATOM   4122 C  CA    . GLY B 2 549 ? 113.291 99.457  98.122  1.00 39.20  ? 549 GLY A CA    1 
ATOM   4123 C  C     . GLY B 2 549 ? 112.686 99.210  96.754  1.00 36.97  ? 549 GLY A C     1 
ATOM   4124 O  O     . GLY B 2 549 ? 112.275 100.150 96.065  1.00 39.03  ? 549 GLY A O     1 
ATOM   4125 N  N     . THR B 2 550 ? 112.607 97.943  96.345  1.00 33.91  ? 550 THR A N     1 
ATOM   4126 C  CA    . THR B 2 550 ? 111.966 97.625  95.074  1.00 33.82  ? 550 THR A CA    1 
ATOM   4127 C  C     . THR B 2 550 ? 110.487 97.987  95.094  1.00 38.80  ? 550 THR A C     1 
ATOM   4128 O  O     . THR B 2 550 ? 109.942 98.451  94.086  1.00 45.77  ? 550 THR A O     1 
ATOM   4129 C  CB    . THR B 2 550 ? 112.143 96.145  94.749  1.00 36.59  ? 550 THR A CB    1 
ATOM   4130 O  OG1   . THR B 2 550 ? 113.532 95.856  94.546  1.00 38.22  ? 550 THR A OG1   1 
ATOM   4131 C  CG2   . THR B 2 550 ? 111.353 95.773  93.503  1.00 37.57  ? 550 THR A CG2   1 
ATOM   4132 N  N     . CYS B 2 551 ? 109.812 97.761  96.223  1.00 37.26  ? 551 CYS A N     1 
ATOM   4133 C  CA    . CYS B 2 551 ? 108.406 98.144  96.313  1.00 36.52  ? 551 CYS A CA    1 
ATOM   4134 C  C     . CYS B 2 551 ? 108.239 99.646  96.124  1.00 39.24  ? 551 CYS A C     1 
ATOM   4135 O  O     . CYS B 2 551 ? 107.348 100.098 95.393  1.00 44.83  ? 551 CYS A O     1 
ATOM   4136 C  CB    . CYS B 2 551 ? 107.828 97.705  97.657  1.00 41.07  ? 551 CYS A CB    1 
ATOM   4137 S  SG    . CYS B 2 551 ? 106.071 98.067  97.851  1.00 53.78  ? 551 CYS A SG    1 
ATOM   4138 N  N     . ALA B 2 552 ? 109.103 100.437 96.764  1.00 38.92  ? 552 ALA A N     1 
ATOM   4139 C  CA    . ALA B 2 552 ? 109.031 101.887 96.613  1.00 40.96  ? 552 ALA A CA    1 
ATOM   4140 C  C     . ALA B 2 552 ? 109.302 102.310 95.174  1.00 40.17  ? 552 ALA A C     1 
ATOM   4141 O  O     . ALA B 2 552 ? 108.644 103.218 94.651  1.00 40.42  ? 552 ALA A O     1 
ATOM   4142 C  CB    . ALA B 2 552 ? 110.021 102.559 97.561  1.00 42.26  ? 552 ALA A CB    1 
ATOM   4143 N  N     . ASP B 2 553 ? 110.284 101.681 94.525  1.00 39.48  ? 553 ASP A N     1 
ATOM   4144 C  CA    . ASP B 2 553 ? 110.588 102.029 93.138  1.00 34.62  ? 553 ASP A CA    1 
ATOM   4145 C  C     . ASP B 2 553 ? 109.421 101.699 92.218  1.00 32.52  ? 553 ASP A C     1 
ATOM   4146 O  O     . ASP B 2 553 ? 109.086 102.482 91.317  1.00 39.11  ? 553 ASP A O     1 
ATOM   4147 C  CB    . ASP B 2 553 ? 111.850 101.302 92.684  1.00 37.44  ? 553 ASP A CB    1 
ATOM   4148 C  CG    . ASP B 2 553 ? 113.053 101.651 93.532  1.00 45.28  ? 553 ASP A CG    1 
ATOM   4149 O  OD1   . ASP B 2 553 ? 112.874 102.332 94.564  1.00 41.00  ? 553 ASP A OD1   1 
ATOM   4150 O  OD2   . ASP B 2 553 ? 114.175 101.248 93.170  1.00 48.98  ? 553 ASP A OD2   1 
ATOM   4151 N  N     . ILE B 2 554 ? 108.791 100.544 92.428  1.00 32.91  ? 554 ILE A N     1 
ATOM   4152 C  CA    . ILE B 2 554 ? 107.605 100.194 91.654  1.00 34.98  ? 554 ILE A CA    1 
ATOM   4153 C  C     . ILE B 2 554 ? 106.521 101.240 91.859  1.00 36.64  ? 554 ILE A C     1 
ATOM   4154 O  O     . ILE B 2 554 ? 105.860 101.667 90.905  1.00 42.37  ? 554 ILE A O     1 
ATOM   4155 C  CB    . ILE B 2 554 ? 107.111 98.788  92.041  1.00 35.79  ? 554 ILE A CB    1 
ATOM   4156 C  CG1   . ILE B 2 554 ? 108.106 97.724  91.568  1.00 39.22  ? 554 ILE A CG1   1 
ATOM   4157 C  CG2   . ILE B 2 554 ? 105.723 98.533  91.471  1.00 39.56  ? 554 ILE A CG2   1 
ATOM   4158 C  CD1   . ILE B 2 554 ? 107.955 96.396  92.273  1.00 39.93  ? 554 ILE A CD1   1 
ATOM   4159 N  N     . LEU B 2 555 ? 106.322 101.671 93.105  1.00 36.42  ? 555 LEU A N     1 
ATOM   4160 C  CA    . LEU B 2 555 ? 105.304 102.680 93.378  1.00 36.76  ? 555 LEU A CA    1 
ATOM   4161 C  C     . LEU B 2 555 ? 105.611 103.988 92.655  1.00 41.07  ? 555 LEU A C     1 
ATOM   4162 O  O     . LEU B 2 555 ? 104.716 104.613 92.073  1.00 47.93  ? 555 LEU A O     1 
ATOM   4163 C  CB    . LEU B 2 555 ? 105.202 102.907 94.884  1.00 37.70  ? 555 LEU A CB    1 
ATOM   4164 C  CG    . LEU B 2 555 ? 104.069 103.798 95.382  1.00 35.96  ? 555 LEU A CG    1 
ATOM   4165 C  CD1   . LEU B 2 555 ? 102.728 103.142 95.114  1.00 41.64  ? 555 LEU A CD1   1 
ATOM   4166 C  CD2   . LEU B 2 555 ? 104.270 104.074 96.864  1.00 42.91  ? 555 LEU A CD2   1 
ATOM   4167 N  N     . LYS B 2 556 ? 106.874 104.418 92.680  1.00 43.49  ? 556 LYS A N     1 
ATOM   4168 C  CA    . LYS B 2 556 ? 107.239 105.670 92.024  1.00 41.96  ? 556 LYS A CA    1 
ATOM   4169 C  C     . LYS B 2 556 ? 107.011 105.595 90.520  1.00 42.15  ? 556 LYS A C     1 
ATOM   4170 O  O     . LYS B 2 556 ? 106.481 106.537 89.916  1.00 44.36  ? 556 LYS A O     1 
ATOM   4171 C  CB    . LYS B 2 556 ? 108.698 106.016 92.314  1.00 37.78  ? 556 LYS A CB    1 
ATOM   4172 C  CG    . LYS B 2 556 ? 108.962 106.469 93.738  1.00 37.95  ? 556 LYS A CG    1 
ATOM   4173 C  CD    . LYS B 2 556 ? 110.405 106.904 93.904  1.00 41.84  ? 556 LYS A CD    1 
ATOM   4174 C  CE    . LYS B 2 556 ? 110.716 107.239 95.349  1.00 38.52  ? 556 LYS A CE    1 
ATOM   4175 N  NZ    . LYS B 2 556 ? 109.828 108.304 95.880  1.00 37.16  ? 556 LYS A NZ    1 
ATOM   4176 N  N     . LEU B 2 557 ? 107.409 104.488 89.893  1.00 37.16  ? 557 LEU A N     1 
ATOM   4177 C  CA    . LEU B 2 557 ? 107.195 104.361 88.455  1.00 37.02  ? 557 LEU A CA    1 
ATOM   4178 C  C     . LEU B 2 557 ? 105.708 104.297 88.127  1.00 39.37  ? 557 LEU A C     1 
ATOM   4179 O  O     . LEU B 2 557 ? 105.261 104.852 87.112  1.00 46.36  ? 557 LEU A O     1 
ATOM   4180 C  CB    . LEU B 2 557 ? 107.927 103.132 87.919  1.00 39.87  ? 557 LEU A CB    1 
ATOM   4181 C  CG    . LEU B 2 557 ? 107.893 102.955 86.400  1.00 45.40  ? 557 LEU A CG    1 
ATOM   4182 C  CD1   . LEU B 2 557 ? 108.900 103.869 85.730  1.00 45.34  ? 557 LEU A CD1   1 
ATOM   4183 C  CD2   . LEU B 2 557 ? 108.171 101.512 86.029  1.00 49.52  ? 557 LEU A CD2   1 
ATOM   4184 N  N     . ALA B 2 558 ? 104.924 103.631 88.976  1.00 38.16  ? 558 ALA A N     1 
ATOM   4185 C  CA    . ALA B 2 558 ? 103.482 103.611 88.774  1.00 41.25  ? 558 ALA A CA    1 
ATOM   4186 C  C     . ALA B 2 558 ? 102.913 105.020 88.818  1.00 41.16  ? 558 ALA A C     1 
ATOM   4187 O  O     . ALA B 2 558 ? 102.066 105.379 87.996  1.00 43.03  ? 558 ALA A O     1 
ATOM   4188 C  CB    . ALA B 2 558 ? 102.813 102.730 89.828  1.00 47.29  ? 558 ALA A CB    1 
ATOM   4189 N  N     . LEU B 2 559 ? 103.372 105.837 89.767  1.00 43.56  ? 559 LEU A N     1 
ATOM   4190 C  CA    . LEU B 2 559 ? 102.901 107.218 89.836  1.00 43.08  ? 559 LEU A CA    1 
ATOM   4191 C  C     . LEU B 2 559 ? 103.301 107.999 88.592  1.00 45.23  ? 559 LEU A C     1 
ATOM   4192 O  O     . LEU B 2 559 ? 102.507 108.786 88.056  1.00 46.79  ? 559 LEU A O     1 
ATOM   4193 C  CB    . LEU B 2 559 ? 103.454 107.904 91.085  1.00 40.82  ? 559 LEU A CB    1 
ATOM   4194 C  CG    . LEU B 2 559 ? 102.674 107.751 92.391  1.00 43.03  ? 559 LEU A CG    1 
ATOM   4195 C  CD1   . LEU B 2 559 ? 103.269 108.668 93.442  1.00 46.54  ? 559 LEU A CD1   1 
ATOM   4196 C  CD2   . LEU B 2 559 ? 101.191 108.034 92.204  1.00 46.05  ? 559 LEU A CD2   1 
ATOM   4197 N  N     . VAL B 2 560 ? 104.538 107.811 88.128  1.00 47.56  ? 560 VAL A N     1 
ATOM   4198 C  CA    . VAL B 2 560 ? 105.001 108.533 86.946  1.00 44.59  ? 560 VAL A CA    1 
ATOM   4199 C  C     . VAL B 2 560 ? 104.096 108.230 85.761  1.00 45.05  ? 560 VAL A C     1 
ATOM   4200 O  O     . VAL B 2 560 ? 103.591 109.140 85.089  1.00 46.61  ? 560 VAL A O     1 
ATOM   4201 C  CB    . VAL B 2 560 ? 106.464 108.170 86.636  1.00 44.66  ? 560 VAL A CB    1 
ATOM   4202 C  CG1   . VAL B 2 560 ? 106.820 108.561 85.214  1.00 47.20  ? 560 VAL A CG1   1 
ATOM   4203 C  CG2   . VAL B 2 560 ? 107.392 108.829 87.625  1.00 43.11  ? 560 VAL A CG2   1 
ATOM   4204 N  N     . ASP B 2 561 ? 103.862 106.943 85.498  1.00 46.73  ? 561 ASP A N     1 
ATOM   4205 C  CA    . ASP B 2 561 ? 103.013 106.575 84.369  1.00 49.35  ? 561 ASP A CA    1 
ATOM   4206 C  C     . ASP B 2 561 ? 101.576 107.029 84.590  1.00 52.81  ? 561 ASP A C     1 
ATOM   4207 O  O     . ASP B 2 561 ? 100.900 107.454 83.645  1.00 60.47  ? 561 ASP A O     1 
ATOM   4208 C  CB    . ASP B 2 561 ? 103.073 105.067 84.132  1.00 56.26  ? 561 ASP A CB    1 
ATOM   4209 C  CG    . ASP B 2 561 ? 104.369 104.628 83.472  1.00 59.24  ? 561 ASP A CG    1 
ATOM   4210 O  OD1   . ASP B 2 561 ? 105.104 105.500 82.960  1.00 58.82  ? 561 ASP A OD1   1 
ATOM   4211 O  OD2   . ASP B 2 561 ? 104.647 103.411 83.454  1.00 56.54  ? 561 ASP A OD2   1 
ATOM   4212 N  N     . LEU B 2 562 ? 101.095 106.964 85.832  1.00 52.23  ? 562 LEU A N     1 
ATOM   4213 C  CA    . LEU B 2 562 ? 99.741  107.407 86.133  1.00 51.88  ? 562 LEU A CA    1 
ATOM   4214 C  C     . LEU B 2 562 ? 99.546  108.862 85.737  1.00 52.30  ? 562 LEU A C     1 
ATOM   4215 O  O     . LEU B 2 562 ? 98.590  109.206 85.034  1.00 56.08  ? 562 LEU A O     1 
ATOM   4216 C  CB    . LEU B 2 562 ? 99.461  107.215 87.625  1.00 51.99  ? 562 LEU A CB    1 
ATOM   4217 C  CG    . LEU B 2 562 ? 98.019  107.355 88.121  1.00 52.78  ? 562 LEU A CG    1 
ATOM   4218 C  CD1   . LEU B 2 562 ? 97.028  106.687 87.186  1.00 62.31  ? 562 LEU A CD1   1 
ATOM   4219 C  CD2   . LEU B 2 562 ? 97.890  106.807 89.531  1.00 53.38  ? 562 LEU A CD2   1 
ATOM   4220 N  N     . TYR B 2 563 ? 100.452 109.735 86.175  1.00 52.32  ? 563 TYR A N     1 
ATOM   4221 C  CA    . TYR B 2 563 ? 100.317 111.143 85.822  1.00 55.34  ? 563 TYR A CA    1 
ATOM   4222 C  C     . TYR B 2 563 ? 100.510 111.360 84.327  1.00 56.42  ? 563 TYR A C     1 
ATOM   4223 O  O     . TYR B 2 563 ? 99.783  112.148 83.713  1.00 56.59  ? 563 TYR A O     1 
ATOM   4224 C  CB    . TYR B 2 563 ? 101.304 111.991 86.617  1.00 54.84  ? 563 TYR A CB    1 
ATOM   4225 C  CG    . TYR B 2 563 ? 101.172 113.475 86.351  1.00 57.69  ? 563 TYR A CG    1 
ATOM   4226 C  CD1   . TYR B 2 563 ? 99.976  114.140 86.585  1.00 61.83  ? 563 TYR A CD1   1 
ATOM   4227 C  CD2   . TYR B 2 563 ? 102.246 114.213 85.871  1.00 57.06  ? 563 TYR A CD2   1 
ATOM   4228 C  CE1   . TYR B 2 563 ? 99.853  115.492 86.339  1.00 61.68  ? 563 TYR A CE1   1 
ATOM   4229 C  CE2   . TYR B 2 563 ? 102.130 115.564 85.627  1.00 57.83  ? 563 TYR A CE2   1 
ATOM   4230 C  CZ    . TYR B 2 563 ? 100.933 116.199 85.863  1.00 59.81  ? 563 TYR A CZ    1 
ATOM   4231 O  OH    . TYR B 2 563 ? 100.814 117.547 85.617  1.00 63.42  ? 563 TYR A OH    1 
ATOM   4232 N  N     . ASP B 2 564 ? 101.476 110.670 83.718  1.00 58.33  ? 564 ASP A N     1 
ATOM   4233 C  CA    . ASP B 2 564 ? 101.704 110.856 82.291  1.00 58.35  ? 564 ASP A CA    1 
ATOM   4234 C  C     . ASP B 2 564 ? 100.559 110.335 81.435  1.00 57.82  ? 564 ASP A C     1 
ATOM   4235 O  O     . ASP B 2 564 ? 100.503 110.670 80.248  1.00 61.05  ? 564 ASP A O     1 
ATOM   4236 C  CB    . ASP B 2 564 ? 103.001 110.166 81.867  1.00 59.05  ? 564 ASP A CB    1 
ATOM   4237 C  CG    . ASP B 2 564 ? 104.226 111.017 82.126  1.00 57.94  ? 564 ASP A CG    1 
ATOM   4238 O  OD1   . ASP B 2 564 ? 104.074 112.145 82.638  1.00 60.50  ? 564 ASP A OD1   1 
ATOM   4239 O  OD2   . ASP B 2 564 ? 105.344 110.562 81.807  1.00 55.35  ? 564 ASP A OD2   1 
ATOM   4240 N  N     . ASN B 2 565 ? 99.650  109.535 81.997  1.00 59.18  ? 565 ASN A N     1 
ATOM   4241 C  CA    . ASN B 2 565 ? 98.621  108.879 81.203  1.00 63.67  ? 565 ASN A CA    1 
ATOM   4242 C  C     . ASN B 2 565 ? 97.209  109.383 81.487  1.00 65.05  ? 565 ASN A C     1 
ATOM   4243 O  O     . ASN B 2 565 ? 96.345  109.257 80.616  1.00 68.18  ? 565 ASN A O     1 
ATOM   4244 C  CB    . ASN B 2 565 ? 98.700  107.359 81.426  1.00 64.87  ? 565 ASN A CB    1 
ATOM   4245 C  CG    . ASN B 2 565 ? 97.432  106.630 81.042  1.00 66.50  ? 565 ASN A CG    1 
ATOM   4246 O  OD1   . ASN B 2 565 ? 96.790  106.948 80.043  1.00 66.64  ? 565 ASN A OD1   1 
ATOM   4247 N  ND2   . ASN B 2 565 ? 97.097  105.604 81.809  1.00 67.23  ? 565 ASN A ND2   1 
ATOM   4248 N  N     . LEU B 2 566 ? 96.956  109.975 82.656  1.00 63.24  ? 566 LEU A N     1 
ATOM   4249 C  CA    . LEU B 2 566 ? 95.633  110.520 82.956  1.00 66.69  ? 566 LEU A CA    1 
ATOM   4250 C  C     . LEU B 2 566 ? 95.359  111.856 82.277  1.00 71.71  ? 566 LEU A C     1 
ATOM   4251 O  O     . LEU B 2 566 ? 94.245  112.375 82.405  1.00 74.38  ? 566 LEU A O     1 
ATOM   4252 C  CB    . LEU B 2 566 ? 95.443  110.713 84.462  1.00 67.51  ? 566 LEU A CB    1 
ATOM   4253 C  CG    . LEU B 2 566 ? 95.653  109.542 85.416  1.00 64.22  ? 566 LEU A CG    1 
ATOM   4254 C  CD1   . LEU B 2 566 ? 96.184  110.061 86.734  1.00 61.97  ? 566 LEU A CD1   1 
ATOM   4255 C  CD2   . LEU B 2 566 ? 94.351  108.792 85.630  1.00 65.09  ? 566 LEU A CD2   1 
ATOM   4256 N  N     . LYS B 2 567 ? 96.329  112.422 81.557  1.00 73.26  ? 567 LYS A N     1 
ATOM   4257 C  CA    . LYS B 2 567 ? 96.160  113.764 81.011  1.00 73.93  ? 567 LYS A CA    1 
ATOM   4258 C  C     . LYS B 2 567 ? 94.939  113.876 80.110  1.00 76.99  ? 567 LYS A C     1 
ATOM   4259 O  O     . LYS B 2 567 ? 94.412  114.979 79.934  1.00 80.76  ? 567 LYS A O     1 
ATOM   4260 C  CB    . LYS B 2 567 ? 97.405  114.172 80.225  1.00 68.07  ? 567 LYS A CB    1 
ATOM   4261 C  CG    . LYS B 2 567 ? 98.677  114.227 81.054  1.00 66.20  ? 567 LYS A CG    1 
ATOM   4262 C  CD    . LYS B 2 567 ? 99.870  114.604 80.196  1.00 60.53  ? 567 LYS A CD    1 
ATOM   4263 C  CE    . LYS B 2 567 ? 101.133 114.732 81.027  1.00 60.32  ? 567 LYS A CE    1 
ATOM   4264 N  NZ    . LYS B 2 567 ? 101.032 115.818 82.038  1.00 60.03  ? 567 LYS A NZ    1 
ATOM   4265 N  N     . ASP B 2 568 ? 94.477  112.767 79.537  1.00 77.05  ? 568 ASP A N     1 
ATOM   4266 C  CA    . ASP B 2 568 ? 93.390  112.805 78.568  1.00 83.26  ? 568 ASP A CA    1 
ATOM   4267 C  C     . ASP B 2 568 ? 92.010  112.918 79.207  1.00 85.32  ? 568 ASP A C     1 
ATOM   4268 O  O     . ASP B 2 568 ? 91.043  113.198 78.490  1.00 92.75  ? 568 ASP A O     1 
ATOM   4269 C  CB    . ASP B 2 568 ? 93.446  111.556 77.686  1.00 83.78  ? 568 ASP A CB    1 
ATOM   4270 C  CG    . ASP B 2 568 ? 94.754  111.439 76.927  1.00 83.04  ? 568 ASP A CG    1 
ATOM   4271 O  OD1   . ASP B 2 568 ? 95.808  111.269 77.574  1.00 79.59  ? 568 ASP A OD1   1 
ATOM   4272 O  OD2   . ASP B 2 568 ? 94.727  111.518 75.682  1.00 85.48  ? 568 ASP A OD2   1 
ATOM   4273 N  N     . ILE B 2 569 ? 91.887  112.707 80.517  1.00 77.74  ? 569 ILE A N     1 
ATOM   4274 C  CA    . ILE B 2 569 ? 90.589  112.779 81.184  1.00 76.47  ? 569 ILE A CA    1 
ATOM   4275 C  C     . ILE B 2 569 ? 90.667  113.673 82.415  1.00 82.25  ? 569 ILE A C     1 
ATOM   4276 O  O     . ILE B 2 569 ? 89.819  113.585 83.310  1.00 86.75  ? 569 ILE A O     1 
ATOM   4277 C  CB    . ILE B 2 569 ? 90.085  111.374 81.561  1.00 73.92  ? 569 ILE A CB    1 
ATOM   4278 C  CG1   . ILE B 2 569 ? 91.074  110.680 82.501  1.00 73.92  ? 569 ILE A CG1   1 
ATOM   4279 C  CG2   . ILE B 2 569 ? 89.861  110.547 80.308  1.00 77.20  ? 569 ILE A CG2   1 
ATOM   4280 C  CD1   . ILE B 2 569 ? 90.546  109.396 83.093  1.00 80.23  ? 569 ILE A CD1   1 
ATOM   4281 N  N     . ASN B 2 570 ? 91.680  114.537 82.472  1.00 83.63  ? 570 ASN A N     1 
ATOM   4282 C  CA    . ASN B 2 570 ? 91.845  115.482 83.576  1.00 83.79  ? 570 ASN A CA    1 
ATOM   4283 C  C     . ASN B 2 570 ? 91.924  114.740 84.913  1.00 83.68  ? 570 ASN A C     1 
ATOM   4284 O  O     . ASN B 2 570 ? 91.091  114.911 85.805  1.00 79.82  ? 570 ASN A O     1 
ATOM   4285 C  CB    . ASN B 2 570 ? 90.707  116.509 83.579  1.00 87.24  ? 570 ASN A CB    1 
ATOM   4286 C  CG    . ASN B 2 570 ? 90.863  117.556 84.670  1.00 91.17  ? 570 ASN A CG    1 
ATOM   4287 O  OD1   . ASN B 2 570 ? 91.792  117.497 85.474  1.00 88.52  ? 570 ASN A OD1   1 
ATOM   4288 N  ND2   . ASN B 2 570 ? 89.950  118.520 84.703  1.00 93.99  ? 570 ASN A ND2   1 
ATOM   4289 N  N     . GLY B 2 571 ? 92.954  113.904 85.036  1.00 84.71  ? 571 GLY A N     1 
ATOM   4290 C  CA    . GLY B 2 571 ? 93.129  113.082 86.223  1.00 79.64  ? 571 GLY A CA    1 
ATOM   4291 C  C     . GLY B 2 571 ? 94.058  113.735 87.233  1.00 78.05  ? 571 GLY A C     1 
ATOM   4292 O  O     . GLY B 2 571 ? 95.070  114.335 86.875  1.00 75.15  ? 571 GLY A O     1 
ATOM   4293 N  N     . LYS B 2 572 ? 93.696  113.599 88.507  1.00 76.17  ? 572 LYS A N     1 
ATOM   4294 C  CA    . LYS B 2 572 ? 94.439  114.194 89.607  1.00 69.71  ? 572 LYS A CA    1 
ATOM   4295 C  C     . LYS B 2 572 ? 94.670  113.148 90.685  1.00 63.31  ? 572 LYS A C     1 
ATOM   4296 O  O     . LYS B 2 572 ? 93.757  112.396 91.040  1.00 61.63  ? 572 LYS A O     1 
ATOM   4297 C  CB    . LYS B 2 572 ? 93.691  115.397 90.190  1.00 69.16  ? 572 LYS A CB    1 
ATOM   4298 C  CG    . LYS B 2 572 ? 93.926  116.700 89.439  1.00 68.27  ? 572 LYS A CG    1 
ATOM   4299 C  CD    . LYS B 2 572 ? 92.820  117.704 89.737  1.00 71.79  ? 572 LYS A CD    1 
ATOM   4300 C  CE    . LYS B 2 572 ? 93.197  119.108 89.296  1.00 75.58  ? 572 LYS A CE    1 
ATOM   4301 N  NZ    . LYS B 2 572 ? 92.733  120.134 90.266  1.00 73.87  ? 572 LYS A NZ    1 
ATOM   4302 N  N     . ILE B 2 573 ? 95.892  113.109 91.200  1.00 61.86  ? 573 ILE A N     1 
ATOM   4303 C  CA    . ILE B 2 573 ? 96.304  112.152 92.219  1.00 60.04  ? 573 ILE A CA    1 
ATOM   4304 C  C     . ILE B 2 573 ? 96.387  112.864 93.563  1.00 59.44  ? 573 ILE A C     1 
ATOM   4305 O  O     . ILE B 2 573 ? 96.863  114.002 93.645  1.00 62.35  ? 573 ILE A O     1 
ATOM   4306 C  CB    . ILE B 2 573 ? 97.640  111.490 91.823  1.00 59.33  ? 573 ILE A CB    1 
ATOM   4307 C  CG1   . ILE B 2 573 ? 98.815  112.443 92.019  1.00 57.96  ? 573 ILE A CG1   1 
ATOM   4308 C  CG2   . ILE B 2 573 ? 97.613  111.073 90.365  1.00 59.03  ? 573 ILE A CG2   1 
ATOM   4309 C  CD1   . ILE B 2 573 ? 100.147 111.790 91.857  1.00 55.93  ? 573 ILE A CD1   1 
ATOM   4310 N  N     . ILE B 2 574 ? 95.919  112.199 94.622  1.00 56.94  ? 574 ILE A N     1 
ATOM   4311 C  CA    . ILE B 2 574 ? 95.680  112.884 95.889  1.00 53.65  ? 574 ILE A CA    1 
ATOM   4312 C  C     . ILE B 2 574 ? 96.423  112.251 97.061  1.00 58.98  ? 574 ILE A C     1 
ATOM   4313 O  O     . ILE B 2 574 ? 96.697  112.929 98.057  1.00 62.18  ? 574 ILE A O     1 
ATOM   4314 C  CB    . ILE B 2 574 ? 94.169  112.948 96.182  1.00 57.52  ? 574 ILE A CB    1 
ATOM   4315 C  CG1   . ILE B 2 574 ? 93.641  111.597 96.674  1.00 59.77  ? 574 ILE A CG1   1 
ATOM   4316 C  CG2   . ILE B 2 574 ? 93.407  113.393 94.938  1.00 61.77  ? 574 ILE A CG2   1 
ATOM   4317 C  CD1   . ILE B 2 574 ? 92.151  111.597 96.954  1.00 62.09  ? 574 ILE A CD1   1 
ATOM   4318 N  N     . LEU B 2 575 ? 96.757  110.965 96.973  1.00 62.08  ? 575 LEU A N     1 
ATOM   4319 C  CA    . LEU B 2 575 ? 97.406  110.320 98.109  1.00 58.21  ? 575 LEU A CA    1 
ATOM   4320 C  C     . LEU B 2 575 ? 98.125  109.056 97.660  1.00 54.97  ? 575 LEU A C     1 
ATOM   4321 O  O     . LEU B 2 575 ? 97.713  108.393 96.705  1.00 50.89  ? 575 LEU A O     1 
ATOM   4322 C  CB    . LEU B 2 575 ? 96.389  109.991 99.212  1.00 54.47  ? 575 LEU A CB    1 
ATOM   4323 C  CG    . LEU B 2 575 ? 96.866  109.846 100.663 1.00 54.74  ? 575 LEU A CG    1 
ATOM   4324 C  CD1   . LEU B 2 575 ? 98.065  110.719 100.980 1.00 50.46  ? 575 LEU A CD1   1 
ATOM   4325 C  CD2   . LEU B 2 575 ? 95.727  110.148 101.623 1.00 57.32  ? 575 LEU A CD2   1 
ATOM   4326 N  N     . CYS B 2 576 ? 99.205  108.734 98.375  1.00 56.83  ? 576 CYS A N     1 
ATOM   4327 C  CA    . CYS B 2 576 ? 100.055 107.590 98.051  1.00 54.26  ? 576 CYS A CA    1 
ATOM   4328 C  C     . CYS B 2 576 ? 100.740 107.127 99.330  1.00 54.92  ? 576 CYS A C     1 
ATOM   4329 O  O     . CYS B 2 576 ? 101.618 107.829 99.837  1.00 54.59  ? 576 CYS A O     1 
ATOM   4330 C  CB    . CYS B 2 576 ? 101.081 107.972 96.989  1.00 48.21  ? 576 CYS A CB    1 
ATOM   4331 S  SG    . CYS B 2 576 ? 102.563 106.961 97.005  1.00 58.85  ? 576 CYS A SG    1 
ATOM   4332 N  N     . VAL B 2 577 ? 100.363 105.957 99.848  1.00 52.70  ? 577 VAL A N     1 
ATOM   4333 C  CA    . VAL B 2 577 ? 100.856 105.480 101.146 1.00 47.99  ? 577 VAL A CA    1 
ATOM   4334 C  C     . VAL B 2 577 ? 101.612 104.171 100.922 1.00 50.58  ? 577 VAL A C     1 
ATOM   4335 O  O     . VAL B 2 577 ? 101.089 103.070 101.112 1.00 51.19  ? 577 VAL A O     1 
ATOM   4336 C  CB    . VAL B 2 577 ? 99.727  105.316 102.167 1.00 45.17  ? 577 VAL A CB    1 
ATOM   4337 C  CG1   . VAL B 2 577 ? 98.619  104.412 101.634 1.00 45.11  ? 577 VAL A CG1   1 
ATOM   4338 C  CG2   . VAL B 2 577 ? 100.276 104.795 103.488 1.00 50.58  ? 577 VAL A CG2   1 
ATOM   4339 N  N     . HIS B 2 578 ? 102.876 104.301 100.520 1.00 49.27  ? 578 HIS A N     1 
ATOM   4340 C  CA    . HIS B 2 578 ? 103.909 103.265 100.526 1.00 45.00  ? 578 HIS A CA    1 
ATOM   4341 C  C     . HIS B 2 578 ? 103.685 102.104 99.565  1.00 46.12  ? 578 HIS A C     1 
ATOM   4342 O  O     . HIS B 2 578 ? 104.654 101.473 99.132  1.00 42.57  ? 578 HIS A O     1 
ATOM   4343 C  CB    . HIS B 2 578 ? 104.048 102.666 101.926 1.00 43.73  ? 578 HIS A CB    1 
ATOM   4344 C  CG    . HIS B 2 578 ? 104.452 103.650 102.976 1.00 45.27  ? 578 HIS A CG    1 
ATOM   4345 N  ND1   . HIS B 2 578 ? 105.705 104.221 103.016 1.00 47.07  ? 578 HIS A ND1   1 
ATOM   4346 C  CD2   . HIS B 2 578 ? 103.776 104.152 104.036 1.00 48.08  ? 578 HIS A CD2   1 
ATOM   4347 C  CE1   . HIS B 2 578 ? 105.782 105.038 104.050 1.00 50.37  ? 578 HIS A CE1   1 
ATOM   4348 N  NE2   . HIS B 2 578 ? 104.624 105.015 104.686 1.00 52.51  ? 578 HIS A NE2   1 
ATOM   4349 N  N     . ASP B 2 579 ? 102.443 101.806 99.214  1.00 46.28  ? 579 ASP A N     1 
ATOM   4350 C  CA    . ASP B 2 579 ? 102.185 100.969 98.049  1.00 45.39  ? 579 ASP A CA    1 
ATOM   4351 C  C     . ASP B 2 579 ? 100.815 101.196 97.428  1.00 48.78  ? 579 ASP A C     1 
ATOM   4352 O  O     . ASP B 2 579 ? 100.498 100.528 96.441  1.00 49.82  ? 579 ASP A O     1 
ATOM   4353 C  CB    . ASP B 2 579 ? 102.371 99.480  98.410  1.00 47.61  ? 579 ASP A CB    1 
ATOM   4354 C  CG    . ASP B 2 579 ? 101.193 98.900  99.174  1.00 54.55  ? 579 ASP A CG    1 
ATOM   4355 O  OD1   . ASP B 2 579 ? 100.270 99.653  99.535  1.00 57.23  ? 579 ASP A OD1   1 
ATOM   4356 O  OD2   . ASP B 2 579 ? 101.189 97.677  99.413  1.00 52.58  ? 579 ASP A OD2   1 
ATOM   4357 N  N     . GLU B 2 580 ? 99.993  102.092 97.966  1.00 48.80  ? 580 GLU A N     1 
ATOM   4358 C  CA    . GLU B 2 580 ? 98.628  102.295 97.509  1.00 53.55  ? 580 GLU A CA    1 
ATOM   4359 C  C     . GLU B 2 580 ? 98.526  103.653 96.839  1.00 57.29  ? 580 GLU A C     1 
ATOM   4360 O  O     . GLU B 2 580 ? 99.094  104.634 97.325  1.00 58.84  ? 580 GLU A O     1 
ATOM   4361 C  CB    . GLU B 2 580 ? 97.629  102.220 98.669  1.00 50.88  ? 580 GLU A CB    1 
ATOM   4362 C  CG    . GLU B 2 580 ? 97.817  101.029 99.587  1.00 56.95  ? 580 GLU A CG    1 
ATOM   4363 C  CD    . GLU B 2 580 ? 96.697  100.888 100.594 1.00 61.41  ? 580 GLU A CD    1 
ATOM   4364 O  OE1   . GLU B 2 580 ? 95.570  101.345 100.308 1.00 59.22  ? 580 GLU A OE1   1 
ATOM   4365 O  OE2   . GLU B 2 580 ? 96.939  100.304 101.672 1.00 62.67  ? 580 GLU A OE2   1 
ATOM   4366 N  N     . ILE B 2 581 ? 97.804  103.708 95.726  1.00 59.77  ? 581 ILE A N     1 
ATOM   4367 C  CA    . ILE B 2 581 ? 97.570  104.950 95.005  1.00 59.35  ? 581 ILE A CA    1 
ATOM   4368 C  C     . ILE B 2 581 ? 96.072  105.191 94.942  1.00 67.18  ? 581 ILE A C     1 
ATOM   4369 O  O     . ILE B 2 581 ? 95.292  104.265 94.695  1.00 70.77  ? 581 ILE A O     1 
ATOM   4370 C  CB    . ILE B 2 581 ? 98.171  104.924 93.587  1.00 59.31  ? 581 ILE A CB    1 
ATOM   4371 C  CG1   . ILE B 2 581 ? 99.642  104.518 93.639  1.00 52.45  ? 581 ILE A CG1   1 
ATOM   4372 C  CG2   . ILE B 2 581 ? 98.013  106.285 92.937  1.00 63.15  ? 581 ILE A CG2   1 
ATOM   4373 C  CD1   . ILE B 2 581 ? 100.484 105.390 94.540  1.00 46.08  ? 581 ILE A CD1   1 
ATOM   4374 N  N     . ILE B 2 582 ? 95.676  106.437 95.179  1.00 64.33  ? 582 ILE A N     1 
ATOM   4375 C  CA    . ILE B 2 582 ? 94.287  106.857 95.069  1.00 68.90  ? 582 ILE A CA    1 
ATOM   4376 C  C     . ILE B 2 582 ? 94.265  108.161 94.290  1.00 67.59  ? 582 ILE A C     1 
ATOM   4377 O  O     . ILE B 2 582 ? 95.142  109.013 94.466  1.00 69.45  ? 582 ILE A O     1 
ATOM   4378 C  CB    . ILE B 2 582 ? 93.622  107.019 96.452  1.00 70.29  ? 582 ILE A CB    1 
ATOM   4379 C  CG1   . ILE B 2 582 ? 92.316  107.811 96.349  1.00 72.62  ? 582 ILE A CG1   1 
ATOM   4380 C  CG2   . ILE B 2 582 ? 94.575  107.705 97.406  1.00 65.11  ? 582 ILE A CG2   1 
ATOM   4381 C  CD1   . ILE B 2 582 ? 91.587  107.911 97.667  1.00 70.95  ? 582 ILE A CD1   1 
ATOM   4382 N  N     . ILE B 2 583 ? 93.269  108.313 93.419  1.00 65.96  ? 583 ILE A N     1 
ATOM   4383 C  CA    . ILE B 2 583 ? 93.253  109.399 92.451  1.00 68.41  ? 583 ILE A CA    1 
ATOM   4384 C  C     . ILE B 2 583 ? 91.824  109.905 92.320  1.00 71.39  ? 583 ILE A C     1 
ATOM   4385 O  O     . ILE B 2 583 ? 90.865  109.217 92.674  1.00 71.59  ? 583 ILE A O     1 
ATOM   4386 C  CB    . ILE B 2 583 ? 93.788  108.933 91.083  1.00 73.60  ? 583 ILE A CB    1 
ATOM   4387 C  CG1   . ILE B 2 583 ? 93.150  107.603 90.700  1.00 73.93  ? 583 ILE A CG1   1 
ATOM   4388 C  CG2   . ILE B 2 583 ? 95.284  108.707 91.159  1.00 65.99  ? 583 ILE A CG2   1 
ATOM   4389 C  CD1   . ILE B 2 583 ? 93.076  107.369 89.204  1.00 72.46  ? 583 ILE A CD1   1 
ATOM   4390 N  N     . GLU B 2 584 ? 91.686  111.125 91.808  1.00 69.34  ? 584 GLU A N     1 
ATOM   4391 C  CA    . GLU B 2 584 ? 90.383  111.710 91.523  1.00 73.34  ? 584 GLU A CA    1 
ATOM   4392 C  C     . GLU B 2 584 ? 90.190  111.825 90.018  1.00 74.94  ? 584 GLU A C     1 
ATOM   4393 O  O     . GLU B 2 584 ? 91.106  112.225 89.291  1.00 72.91  ? 584 GLU A O     1 
ATOM   4394 C  CB    . GLU B 2 584 ? 90.225  113.094 92.159  1.00 75.04  ? 584 GLU A CB    1 
ATOM   4395 C  CG    . GLU B 2 584 ? 88.813  113.664 92.033  1.00 78.74  ? 584 GLU A CG    1 
ATOM   4396 C  CD    . GLU B 2 584 ? 88.798  115.179 91.959  1.00 79.04  ? 584 GLU A CD    1 
ATOM   4397 O  OE1   . GLU B 2 584 ? 89.478  115.738 91.073  1.00 73.39  ? 584 GLU A OE1   1 
ATOM   4398 O  OE2   . GLU B 2 584 ? 88.108  115.812 92.784  1.00 87.42  ? 584 GLU A OE2   1 
ATOM   4399 N  N     . VAL B 2 585 ? 88.997  111.460 89.557  1.00 76.87  ? 585 VAL A N     1 
ATOM   4400 C  CA    . VAL B 2 585 ? 88.581  111.668 88.178  1.00 79.00  ? 585 VAL A CA    1 
ATOM   4401 C  C     . VAL B 2 585 ? 87.090  111.965 88.175  1.00 85.62  ? 585 VAL A C     1 
ATOM   4402 O  O     . VAL B 2 585 ? 86.334  111.448 89.004  1.00 86.96  ? 585 VAL A O     1 
ATOM   4403 C  CB    . VAL B 2 585 ? 88.897  110.450 87.287  1.00 82.41  ? 585 VAL A CB    1 
ATOM   4404 C  CG1   . VAL B 2 585 ? 88.337  110.649 85.884  1.00 89.13  ? 585 VAL A CG1   1 
ATOM   4405 C  CG2   . VAL B 2 585 ? 90.393  110.215 87.239  1.00 78.59  ? 585 VAL A CG2   1 
ATOM   4406 N  N     . ASN B 2 586 ? 86.664  112.801 87.232  1.00 87.12  ? 586 ASN A N     1 
ATOM   4407 C  CA    . ASN B 2 586 ? 85.244  113.091 87.107  1.00 89.87  ? 586 ASN A CA    1 
ATOM   4408 C  C     . ASN B 2 586 ? 84.476  111.796 86.876  1.00 92.49  ? 586 ASN A C     1 
ATOM   4409 O  O     . ASN B 2 586 ? 84.908  110.923 86.119  1.00 92.24  ? 586 ASN A O     1 
ATOM   4410 C  CB    . ASN B 2 586 ? 84.991  114.080 85.967  1.00 92.72  ? 586 ASN A CB    1 
ATOM   4411 C  CG    . ASN B 2 586 ? 85.906  115.289 86.029  1.00 91.03  ? 586 ASN A CG    1 
ATOM   4412 O  OD1   . ASN B 2 586 ? 86.653  115.565 85.090  1.00 91.21  ? 586 ASN A OD1   1 
ATOM   4413 N  ND2   . ASN B 2 586 ? 85.839  116.025 87.132  1.00 86.90  ? 586 ASN A ND2   1 
ATOM   4414 N  N     . LYS B 2 587 ? 83.321  111.682 87.532  1.00 93.41  ? 587 LYS A N     1 
ATOM   4415 C  CA    . LYS B 2 587 ? 82.594  110.419 87.555  1.00 94.67  ? 587 LYS A CA    1 
ATOM   4416 C  C     . LYS B 2 587 ? 82.240  109.937 86.156  1.00 97.07  ? 587 LYS A C     1 
ATOM   4417 O  O     . LYS B 2 587 ? 81.987  108.742 85.971  1.00 93.93  ? 587 LYS A O     1 
ATOM   4418 C  CB    . LYS B 2 587 ? 81.329  110.574 88.404  1.00 95.19  ? 587 LYS A CB    1 
ATOM   4419 C  CG    . LYS B 2 587 ? 80.744  109.266 88.910  1.00 100.26 ? 587 LYS A CG    1 
ATOM   4420 C  CD    . LYS B 2 587 ? 79.486  109.513 89.729  1.00 100.59 ? 587 LYS A CD    1 
ATOM   4421 C  CE    . LYS B 2 587 ? 79.030  108.249 90.437  1.00 99.15  ? 587 LYS A CE    1 
ATOM   4422 N  NZ    . LYS B 2 587 ? 78.834  107.119 89.496  1.00 95.84  ? 587 LYS A NZ    1 
ATOM   4423 N  N     . LYS B 2 588 ? 82.220  110.837 85.170  1.00 99.98  ? 588 LYS A N     1 
ATOM   4424 C  CA    . LYS B 2 588 ? 81.905  110.441 83.801  1.00 97.77  ? 588 LYS A CA    1 
ATOM   4425 C  C     . LYS B 2 588 ? 82.884  109.400 83.268  1.00 97.82  ? 588 LYS A C     1 
ATOM   4426 O  O     . LYS B 2 588 ? 82.518  108.589 82.411  1.00 98.80  ? 588 LYS A O     1 
ATOM   4427 C  CB    . LYS B 2 588 ? 81.900  111.677 82.896  1.00 95.94  ? 588 LYS A CB    1 
ATOM   4428 C  CG    . LYS B 2 588 ? 80.776  112.656 83.205  1.00 98.17  ? 588 LYS A CG    1 
ATOM   4429 C  CD    . LYS B 2 588 ? 80.788  113.876 82.288  1.00 101.21 ? 588 LYS A CD    1 
ATOM   4430 C  CE    . LYS B 2 588 ? 80.539  113.518 80.831  1.00 100.95 ? 588 LYS A CE    1 
ATOM   4431 N  NZ    . LYS B 2 588 ? 80.467  114.717 79.953  1.00 105.86 ? 588 LYS A NZ    1 
ATOM   4432 N  N     . PHE B 2 589 ? 84.125  109.402 83.763  1.00 94.87  ? 589 PHE A N     1 
ATOM   4433 C  CA    . PHE B 2 589 ? 85.191  108.555 83.235  1.00 93.53  ? 589 PHE A CA    1 
ATOM   4434 C  C     . PHE B 2 589 ? 85.717  107.567 84.275  1.00 94.71  ? 589 PHE A C     1 
ATOM   4435 O  O     . PHE B 2 589 ? 86.870  107.135 84.185  1.00 94.59  ? 589 PHE A O     1 
ATOM   4436 C  CB    . PHE B 2 589 ? 86.336  109.422 82.701  1.00 89.48  ? 589 PHE A CB    1 
ATOM   4437 C  CG    . PHE B 2 589 ? 85.905  110.793 82.247  1.00 92.86  ? 589 PHE A CG    1 
ATOM   4438 C  CD1   . PHE B 2 589 ? 85.099  110.949 81.132  1.00 98.52  ? 589 PHE A CD1   1 
ATOM   4439 C  CD2   . PHE B 2 589 ? 86.325  111.927 82.922  1.00 89.00  ? 589 PHE A CD2   1 
ATOM   4440 C  CE1   . PHE B 2 589 ? 84.708  112.207 80.712  1.00 98.59  ? 589 PHE A CE1   1 
ATOM   4441 C  CE2   . PHE B 2 589 ? 85.937  113.185 82.502  1.00 89.11  ? 589 PHE A CE2   1 
ATOM   4442 C  CZ    . PHE B 2 589 ? 85.129  113.323 81.396  1.00 93.23  ? 589 PHE A CZ    1 
ATOM   4443 N  N     . GLN B 2 590 ? 84.894  107.203 85.263  1.00 97.24  ? 590 GLN A N     1 
ATOM   4444 C  CA    . GLN B 2 590 ? 85.365  106.394 86.386  1.00 95.48  ? 590 GLN A CA    1 
ATOM   4445 C  C     . GLN B 2 590 ? 85.908  105.031 85.946  1.00 92.44  ? 590 GLN A C     1 
ATOM   4446 O  O     . GLN B 2 590 ? 86.988  104.613 86.387  1.00 88.37  ? 590 GLN A O     1 
ATOM   4447 C  CB    . GLN B 2 590 ? 84.224  106.246 87.401  1.00 94.55  ? 590 GLN A CB    1 
ATOM   4448 C  CG    . GLN B 2 590 ? 83.094  105.313 86.973  1.00 97.70  ? 590 GLN A CG    1 
ATOM   4449 C  CD    . GLN B 2 590 ? 82.054  105.125 88.056  1.00 101.49 ? 590 GLN A CD    1 
ATOM   4450 O  OE1   . GLN B 2 590 ? 81.536  106.095 88.611  1.00 99.89  ? 590 GLN A OE1   1 
ATOM   4451 N  NE2   . GLN B 2 590 ? 81.726  103.873 88.351  1.00 103.55 ? 590 GLN A NE2   1 
ATOM   4452 N  N     . GLU B 2 591 ? 85.185  104.330 85.067  1.00 93.63  ? 591 GLU A N     1 
ATOM   4453 C  CA    . GLU B 2 591 ? 85.625  103.003 84.636  1.00 95.07  ? 591 GLU A CA    1 
ATOM   4454 C  C     . GLU B 2 591 ? 86.945  103.094 83.883  1.00 89.48  ? 591 GLU A C     1 
ATOM   4455 O  O     . GLU B 2 591 ? 87.860  102.272 84.079  1.00 85.18  ? 591 GLU A O     1 
ATOM   4456 C  CB    . GLU B 2 591 ? 84.552  102.375 83.743  1.00 97.49  ? 591 GLU A CB    1 
ATOM   4457 C  CG    . GLU B 2 591 ? 83.182  102.232 84.388  1.00 104.84 ? 591 GLU A CG    1 
ATOM   4458 C  CD    . GLU B 2 591 ? 83.197  101.380 85.637  1.00 108.28 ? 591 GLU A CD    1 
ATOM   4459 O  OE1   . GLU B 2 591 ? 83.854  100.318 85.628  1.00 110.75 ? 591 GLU A OE1   1 
ATOM   4460 O  OE2   . GLU B 2 591 ? 82.551  101.772 86.631  1.00 103.98 ? 591 GLU A OE2   1 
ATOM   4461 N  N     . GLU B 2 592 ? 87.062  104.105 83.025  1.00 88.35  ? 592 GLU A N     1 
ATOM   4462 C  CA    . GLU B 2 592 ? 88.298  104.308 82.291  1.00 84.65  ? 592 GLU A CA    1 
ATOM   4463 C  C     . GLU B 2 592 ? 89.443  104.571 83.255  1.00 82.04  ? 592 GLU A C     1 
ATOM   4464 O  O     . GLU B 2 592 ? 90.547  104.062 83.065  1.00 78.01  ? 592 GLU A O     1 
ATOM   4465 C  CB    . GLU B 2 592 ? 88.141  105.465 81.302  1.00 84.24  ? 592 GLU A CB    1 
ATOM   4466 C  CG    . GLU B 2 592 ? 89.376  105.741 80.457  1.00 84.15  ? 592 GLU A CG    1 
ATOM   4467 C  CD    . GLU B 2 592 ? 90.005  104.476 79.898  1.00 92.47  ? 592 GLU A CD    1 
ATOM   4468 O  OE1   . GLU B 2 592 ? 89.400  103.851 79.001  1.00 93.91  ? 592 GLU A OE1   1 
ATOM   4469 O  OE2   . GLU B 2 592 ? 91.105  104.106 80.355  1.00 93.41  ? 592 GLU A OE2   1 
ATOM   4470 N  N     . ALA B 2 593 ? 89.194  105.361 84.304  1.00 83.32  ? 593 ALA A N     1 
ATOM   4471 C  CA    . ALA B 2 593 ? 90.228  105.624 85.301  1.00 77.45  ? 593 ALA A CA    1 
ATOM   4472 C  C     . ALA B 2 593 ? 90.653  104.351 86.024  1.00 81.17  ? 593 ALA A C     1 
ATOM   4473 O  O     . ALA B 2 593 ? 91.839  104.181 86.335  1.00 80.83  ? 593 ALA A O     1 
ATOM   4474 C  CB    . ALA B 2 593 ? 89.732  106.666 86.305  1.00 73.25  ? 593 ALA A CB    1 
ATOM   4475 N  N     . LEU B 2 594 ? 89.710  103.447 86.299  1.00 85.32  ? 594 LEU A N     1 
ATOM   4476 C  CA    . LEU B 2 594 ? 90.079  102.161 86.889  1.00 82.96  ? 594 LEU A CA    1 
ATOM   4477 C  C     . LEU B 2 594 ? 91.047  101.410 85.981  1.00 78.04  ? 594 LEU A C     1 
ATOM   4478 O  O     . LEU B 2 594 ? 92.114  100.945 86.419  1.00 74.55  ? 594 LEU A O     1 
ATOM   4479 C  CB    . LEU B 2 594 ? 88.816  101.334 87.150  1.00 81.14  ? 594 LEU A CB    1 
ATOM   4480 C  CG    . LEU B 2 594 ? 88.948  99.929  87.750  1.00 76.51  ? 594 LEU A CG    1 
ATOM   4481 C  CD1   . LEU B 2 594 ? 87.747  99.625  88.625  1.00 78.28  ? 594 LEU A CD1   1 
ATOM   4482 C  CD2   . LEU B 2 594 ? 89.076  98.864  86.673  1.00 77.01  ? 594 LEU A CD2   1 
ATOM   4483 N  N     . LYS B 2 595 ? 90.695  101.297 84.700  1.00 78.24  ? 595 LYS A N     1 
ATOM   4484 C  CA    . LYS B 2 595 ? 91.585  100.606 83.767  1.00 77.98  ? 595 LYS A CA    1 
ATOM   4485 C  C     . LYS B 2 595 ? 92.925  101.330 83.657  1.00 74.28  ? 595 LYS A C     1 
ATOM   4486 O  O     . LYS B 2 595 ? 93.982  100.695 83.527  1.00 72.33  ? 595 LYS A O     1 
ATOM   4487 C  CB    . LYS B 2 595 ? 90.920  100.486 82.397  1.00 78.29  ? 595 LYS A CB    1 
ATOM   4488 C  CG    . LYS B 2 595 ? 91.446  99.327  81.559  1.00 77.24  ? 595 LYS A CG    1 
ATOM   4489 C  CD    . LYS B 2 595 ? 90.376  98.691  80.684  1.00 79.03  ? 595 LYS A CD    1 
ATOM   4490 C  CE    . LYS B 2 595 ? 89.603  99.723  79.881  1.00 80.27  ? 595 LYS A CE    1 
ATOM   4491 N  NZ    . LYS B 2 595 ? 90.504  100.496 78.986  1.00 82.15  ? 595 LYS A NZ    1 
ATOM   4492 N  N     . ILE B 2 596 ? 92.890  102.664 83.680  1.00 72.70  ? 596 ILE A N     1 
ATOM   4493 C  CA    . ILE B 2 596 ? 94.104  103.478 83.659  1.00 71.30  ? 596 ILE A CA    1 
ATOM   4494 C  C     . ILE B 2 596 ? 95.031  103.082 84.797  1.00 71.71  ? 596 ILE A C     1 
ATOM   4495 O  O     . ILE B 2 596 ? 96.229  102.872 84.599  1.00 73.74  ? 596 ILE A O     1 
ATOM   4496 C  CB    . ILE B 2 596 ? 93.748  104.975 83.733  1.00 69.35  ? 596 ILE A CB    1 
ATOM   4497 C  CG1   . ILE B 2 596 ? 93.059  105.446 82.447  1.00 70.30  ? 596 ILE A CG1   1 
ATOM   4498 C  CG2   . ILE B 2 596 ? 94.978  105.803 84.051  1.00 66.92  ? 596 ILE A CG2   1 
ATOM   4499 C  CD1   . ILE B 2 596 ? 93.952  105.515 81.243  1.00 68.23  ? 596 ILE A CD1   1 
ATOM   4500 N  N     . LEU B 2 597 ? 94.496  103.012 86.015  1.00 69.18  ? 597 LEU A N     1 
ATOM   4501 C  CA    . LEU B 2 597 ? 95.351  102.699 87.156  1.00 67.46  ? 597 LEU A CA    1 
ATOM   4502 C  C     . LEU B 2 597 ? 95.898  101.280 87.066  1.00 68.48  ? 597 LEU A C     1 
ATOM   4503 O  O     . LEU B 2 597 ? 97.064  101.033 87.421  1.00 68.11  ? 597 LEU A O     1 
ATOM   4504 C  CB    . LEU B 2 597 ? 94.578  102.912 88.460  1.00 69.97  ? 597 LEU A CB    1 
ATOM   4505 C  CG    . LEU B 2 597 ? 95.362  102.850 89.775  1.00 69.33  ? 597 LEU A CG    1 
ATOM   4506 C  CD1   . LEU B 2 597 ? 96.684  103.577 89.661  1.00 66.96  ? 597 LEU A CD1   1 
ATOM   4507 C  CD2   . LEU B 2 597 ? 94.536  103.466 90.886  1.00 69.63  ? 597 LEU A CD2   1 
ATOM   4508 N  N     . VAL B 2 598 ? 95.093  100.337 86.566  1.00 67.19  ? 598 VAL A N     1 
ATOM   4509 C  CA    . VAL B 2 598 ? 95.610  98.982  86.381  1.00 64.32  ? 598 VAL A CA    1 
ATOM   4510 C  C     . VAL B 2 598 ? 96.802  98.999  85.431  1.00 66.33  ? 598 VAL A C     1 
ATOM   4511 O  O     . VAL B 2 598 ? 97.870  98.454  85.736  1.00 64.51  ? 598 VAL A O     1 
ATOM   4512 C  CB    . VAL B 2 598 ? 94.504  98.037  85.879  1.00 66.83  ? 598 VAL A CB    1 
ATOM   4513 C  CG1   . VAL B 2 598 ? 95.109  96.828  85.183  1.00 63.54  ? 598 VAL A CG1   1 
ATOM   4514 C  CG2   . VAL B 2 598 ? 93.643  97.586  87.034  1.00 66.67  ? 598 VAL A CG2   1 
ATOM   4515 N  N     . GLN B 2 599 ? 96.645  99.633  84.266  1.00 68.25  ? 599 GLN A N     1 
ATOM   4516 C  CA    . GLN B 2 599 ? 97.770  99.709  83.338  1.00 65.26  ? 599 GLN A CA    1 
ATOM   4517 C  C     . GLN B 2 599 ? 98.932  100.497 83.919  1.00 67.34  ? 599 GLN A C     1 
ATOM   4518 O  O     . GLN B 2 599 ? 100.084 100.254 83.545  1.00 67.26  ? 599 GLN A O     1 
ATOM   4519 C  CB    . GLN B 2 599 ? 97.351  100.346 82.013  1.00 64.43  ? 599 GLN A CB    1 
ATOM   4520 C  CG    . GLN B 2 599 ? 96.664  99.396  81.055  1.00 72.02  ? 599 GLN A CG    1 
ATOM   4521 C  CD    . GLN B 2 599 ? 95.461  100.023 80.386  1.00 76.83  ? 599 GLN A CD    1 
ATOM   4522 O  OE1   . GLN B 2 599 ? 94.350  99.964  80.905  1.00 77.94  ? 599 GLN A OE1   1 
ATOM   4523 N  NE2   . GLN B 2 599 ? 95.678  100.629 79.222  1.00 75.47  ? 599 GLN A NE2   1 
ATOM   4524 N  N     . SER B 2 600 ? 98.654  101.429 84.829  1.00 67.57  ? 600 SER A N     1 
ATOM   4525 C  CA    . SER B 2 600 ? 99.712  102.232 85.421  1.00 62.01  ? 600 SER A CA    1 
ATOM   4526 C  C     . SER B 2 600 ? 100.566 101.407 86.366  1.00 62.77  ? 600 SER A C     1 
ATOM   4527 O  O     . SER B 2 600 ? 101.765 101.672 86.503  1.00 64.15  ? 600 SER A O     1 
ATOM   4528 C  CB    . SER B 2 600 ? 99.106  103.420 86.168  1.00 61.36  ? 600 SER A CB    1 
ATOM   4529 O  OG    . SER B 2 600 ? 98.300  104.206 85.308  1.00 61.59  ? 600 SER A OG    1 
ATOM   4530 N  N     . MET B 2 601 ? 99.978  100.403 87.012  1.00 62.30  ? 601 MET A N     1 
ATOM   4531 C  CA    . MET B 2 601 ? 100.719 99.601  87.981  1.00 59.48  ? 601 MET A CA    1 
ATOM   4532 C  C     . MET B 2 601 ? 101.281 98.308  87.406  1.00 61.13  ? 601 MET A C     1 
ATOM   4533 O  O     . MET B 2 601 ? 102.470 98.029  87.591  1.00 59.38  ? 601 MET A O     1 
ATOM   4534 C  CB    . MET B 2 601 ? 99.839  99.290  89.198  1.00 66.05  ? 601 MET A CB    1 
ATOM   4535 C  CG    . MET B 2 601 ? 99.338  100.534 89.913  1.00 72.65  ? 601 MET A CG    1 
ATOM   4536 S  SD    . MET B 2 601 ? 97.995  100.192 91.058  1.00 88.86  ? 601 MET A SD    1 
ATOM   4537 C  CE    . MET B 2 601 ? 98.738  100.677 92.614  1.00 60.70  ? 601 MET A CE    1 
ATOM   4538 N  N     . GLU B 2 602 ? 100.477 97.500  86.709  1.00 64.27  ? 602 GLU A N     1 
ATOM   4539 C  CA    . GLU B 2 602 ? 100.997 96.223  86.217  1.00 66.52  ? 602 GLU A CA    1 
ATOM   4540 C  C     . GLU B 2 602 ? 102.198 96.430  85.301  1.00 68.38  ? 602 GLU A C     1 
ATOM   4541 O  O     . GLU B 2 602 ? 103.232 95.770  85.460  1.00 69.49  ? 602 GLU A O     1 
ATOM   4542 C  CB    . GLU B 2 602 ? 99.907  95.424  85.500  1.00 67.26  ? 602 GLU A CB    1 
ATOM   4543 C  CG    . GLU B 2 602 ? 98.561  95.441  86.181  1.00 66.63  ? 602 GLU A CG    1 
ATOM   4544 C  CD    . GLU B 2 602 ? 98.674  95.241  87.673  1.00 69.00  ? 602 GLU A CD    1 
ATOM   4545 O  OE1   . GLU B 2 602 ? 98.735  94.074  88.114  1.00 72.21  ? 602 GLU A OE1   1 
ATOM   4546 O  OE2   . GLU B 2 602 ? 98.712  96.249  88.409  1.00 70.54  ? 602 GLU A OE2   1 
ATOM   4547 N  N     . ASN B 2 603 ? 102.086 97.345  84.336  1.00 64.24  ? 603 ASN A N     1 
ATOM   4548 C  CA    . ASN B 2 603 ? 103.212 97.609  83.444  1.00 62.46  ? 603 ASN A CA    1 
ATOM   4549 C  C     . ASN B 2 603 ? 104.443 98.026  84.237  1.00 60.38  ? 603 ASN A C     1 
ATOM   4550 O  O     . ASN B 2 603 ? 105.564 97.596  83.944  1.00 57.89  ? 603 ASN A O     1 
ATOM   4551 C  CB    . ASN B 2 603 ? 102.842 98.684  82.420  1.00 66.88  ? 603 ASN A CB    1 
ATOM   4552 C  CG    . ASN B 2 603 ? 101.561 98.368  81.679  1.00 74.41  ? 603 ASN A CG    1 
ATOM   4553 O  OD1   . ASN B 2 603 ? 101.122 97.219  81.636  1.00 77.20  ? 603 ASN A OD1   1 
ATOM   4554 N  ND2   . ASN B 2 603 ? 100.963 99.386  81.072  1.00 74.49  ? 603 ASN A ND2   1 
ATOM   4555 N  N     . SER B 2 604 ? 104.249 98.870  85.250  1.00 59.17  ? 604 SER A N     1 
ATOM   4556 C  CA    . SER B 2 604 ? 105.360 99.250  86.114  1.00 59.08  ? 604 SER A CA    1 
ATOM   4557 C  C     . SER B 2 604 ? 105.964 98.026  86.790  1.00 60.92  ? 604 SER A C     1 
ATOM   4558 O  O     . SER B 2 604 ? 107.189 97.889  86.875  1.00 64.14  ? 604 SER A O     1 
ATOM   4559 C  CB    . SER B 2 604 ? 104.886 100.264 87.152  1.00 53.52  ? 604 SER A CB    1 
ATOM   4560 O  OG    . SER B 2 604 ? 104.106 101.275 86.543  1.00 55.75  ? 604 SER A OG    1 
ATOM   4561 N  N     . ALA B 2 605 ? 105.114 97.124  87.286  1.00 58.86  ? 605 ALA A N     1 
ATOM   4562 C  CA    . ALA B 2 605 ? 105.622 95.890  87.873  1.00 55.90  ? 605 ALA A CA    1 
ATOM   4563 C  C     . ALA B 2 605 ? 106.394 95.071  86.846  1.00 59.62  ? 605 ALA A C     1 
ATOM   4564 O  O     . ALA B 2 605 ? 107.466 94.533  87.147  1.00 56.97  ? 605 ALA A O     1 
ATOM   4565 C  CB    . ALA B 2 605 ? 104.470 95.074  88.454  1.00 56.69  ? 605 ALA A CB    1 
ATOM   4566 N  N     . SER B 2 606 ? 105.870 94.974  85.622  1.00 61.51  ? 606 SER A N     1 
ATOM   4567 C  CA    . SER B 2 606 ? 106.541 94.200  84.585  1.00 60.97  ? 606 SER A CA    1 
ATOM   4568 C  C     . SER B 2 606 ? 107.932 94.733  84.287  1.00 62.04  ? 606 SER A C     1 
ATOM   4569 O  O     . SER B 2 606 ? 108.793 93.972  83.835  1.00 63.61  ? 606 SER A O     1 
ATOM   4570 C  CB    . SER B 2 606 ? 105.706 94.203  83.304  1.00 63.64  ? 606 SER A CB    1 
ATOM   4571 O  OG    . SER B 2 606 ? 104.478 93.524  83.492  1.00 62.20  ? 606 SER A OG    1 
ATOM   4572 N  N     . TYR B 2 607 ? 108.172 96.021  84.529  1.00 59.02  ? 607 TYR A N     1 
ATOM   4573 C  CA    . TYR B 2 607 ? 109.495 96.582  84.295  1.00 57.38  ? 607 TYR A CA    1 
ATOM   4574 C  C     . TYR B 2 607 ? 110.522 96.070  85.294  1.00 57.02  ? 607 TYR A C     1 
ATOM   4575 O  O     . TYR B 2 607 ? 111.725 96.184  85.038  1.00 56.65  ? 607 TYR A O     1 
ATOM   4576 C  CB    . TYR B 2 607 ? 109.439 98.108  84.356  1.00 54.85  ? 607 TYR A CB    1 
ATOM   4577 C  CG    . TYR B 2 607 ? 110.725 98.772  83.930  1.00 55.30  ? 607 TYR A CG    1 
ATOM   4578 C  CD1   . TYR B 2 607 ? 111.132 98.756  82.606  1.00 62.53  ? 607 TYR A CD1   1 
ATOM   4579 C  CD2   . TYR B 2 607 ? 111.541 99.402  84.857  1.00 55.37  ? 607 TYR A CD2   1 
ATOM   4580 C  CE1   . TYR B 2 607 ? 112.307 99.356  82.217  1.00 65.21  ? 607 TYR A CE1   1 
ATOM   4581 C  CE2   . TYR B 2 607 ? 112.717 100.002 84.475  1.00 58.85  ? 607 TYR A CE2   1 
ATOM   4582 C  CZ    . TYR B 2 607 ? 113.097 99.975  83.155  1.00 63.52  ? 607 TYR A CZ    1 
ATOM   4583 O  OH    . TYR B 2 607 ? 114.272 100.575 82.771  1.00 64.67  ? 607 TYR A OH    1 
ATOM   4584 N  N     . PHE B 2 608 ? 110.080 95.510  86.417  1.00 53.96  ? 608 PHE A N     1 
ATOM   4585 C  CA    . PHE B 2 608 ? 110.976 95.045  87.467  1.00 53.60  ? 608 PHE A CA    1 
ATOM   4586 C  C     . PHE B 2 608 ? 110.857 93.551  87.719  1.00 56.95  ? 608 PHE A C     1 
ATOM   4587 O  O     . PHE B 2 608 ? 111.876 92.854  87.777  1.00 58.98  ? 608 PHE A O     1 
ATOM   4588 C  CB    . PHE B 2 608 ? 110.697 95.823  88.764  1.00 53.38  ? 608 PHE A CB    1 
ATOM   4589 C  CG    . PHE B 2 608 ? 110.994 97.290  88.665  1.00 49.14  ? 608 PHE A CG    1 
ATOM   4590 C  CD1   . PHE B 2 608 ? 112.299 97.746  88.652  1.00 49.70  ? 608 PHE A CD1   1 
ATOM   4591 C  CD2   . PHE B 2 608 ? 109.970 98.213  88.583  1.00 44.90  ? 608 PHE A CD2   1 
ATOM   4592 C  CE1   . PHE B 2 608 ? 112.573 99.090  88.560  1.00 48.71  ? 608 PHE A CE1   1 
ATOM   4593 C  CE2   . PHE B 2 608 ? 110.241 99.556  88.491  1.00 44.69  ? 608 PHE A CE2   1 
ATOM   4594 C  CZ    . PHE B 2 608 ? 111.544 99.995  88.479  1.00 45.65  ? 608 PHE A CZ    1 
ATOM   4595 N  N     . LEU B 2 609 ? 109.641 93.035  87.863  1.00 57.39  ? 609 LEU A N     1 
ATOM   4596 C  CA    . LEU B 2 609 ? 109.415 91.628  88.165  1.00 54.88  ? 609 LEU A CA    1 
ATOM   4597 C  C     . LEU B 2 609 ? 109.033 90.901  86.882  1.00 55.69  ? 609 LEU A C     1 
ATOM   4598 O  O     . LEU B 2 609 ? 107.980 91.174  86.298  1.00 59.71  ? 609 LEU A O     1 
ATOM   4599 C  CB    . LEU B 2 609 ? 108.321 91.474  89.220  1.00 54.78  ? 609 LEU A CB    1 
ATOM   4600 C  CG    . LEU B 2 609 ? 108.473 92.360  90.460  1.00 49.80  ? 609 LEU A CG    1 
ATOM   4601 C  CD1   . LEU B 2 609 ? 107.378 92.049  91.454  1.00 46.16  ? 609 LEU A CD1   1 
ATOM   4602 C  CD2   . LEU B 2 609 ? 109.840 92.192  91.099  1.00 45.66  ? 609 LEU A CD2   1 
ATOM   4603 N  N     . LYS B 2 610 ? 109.885 89.971  86.453  1.00 56.13  ? 610 LYS A N     1 
ATOM   4604 C  CA    . LYS B 2 610 ? 109.705 89.281  85.181  1.00 57.87  ? 610 LYS A CA    1 
ATOM   4605 C  C     . LYS B 2 610 ? 109.038 87.920  85.312  1.00 59.52  ? 610 LYS A C     1 
ATOM   4606 O  O     . LYS B 2 610 ? 108.351 87.491  84.380  1.00 63.63  ? 610 LYS A O     1 
ATOM   4607 C  CB    . LYS B 2 610 ? 111.059 89.094  84.485  1.00 57.65  ? 610 LYS A CB    1 
ATOM   4608 C  CG    . LYS B 2 610 ? 111.889 90.362  84.356  1.00 63.47  ? 610 LYS A CG    1 
ATOM   4609 C  CD    . LYS B 2 610 ? 111.366 91.254  83.236  1.00 65.74  ? 610 LYS A CD    1 
ATOM   4610 C  CE    . LYS B 2 610 ? 112.181 92.530  83.117  1.00 64.07  ? 610 LYS A CE    1 
ATOM   4611 N  NZ    . LYS B 2 610 ? 111.661 93.417  82.045  1.00 66.72  ? 610 LYS A NZ    1 
ATOM   4612 N  N     . LYS B 2 611 ? 109.216 87.230  86.437  1.00 57.86  ? 611 LYS A N     1 
ATOM   4613 C  CA    . LYS B 2 611 ? 108.733 85.861  86.572  1.00 56.92  ? 611 LYS A CA    1 
ATOM   4614 C  C     . LYS B 2 611 ? 107.291 85.790  87.063  1.00 59.50  ? 611 LYS A C     1 
ATOM   4615 O  O     . LYS B 2 611 ? 106.466 85.100  86.458  1.00 61.50  ? 611 LYS A O     1 
ATOM   4616 C  CB    . LYS B 2 611 ? 109.642 85.072  87.519  1.00 52.59  ? 611 LYS A CB    1 
ATOM   4617 C  CG    . LYS B 2 611 ? 109.183 83.642  87.773  1.00 58.45  ? 611 LYS A CG    1 
ATOM   4618 C  CD    . LYS B 2 611 ? 108.946 82.868  86.483  1.00 61.07  ? 611 LYS A CD    1 
ATOM   4619 C  CE    . LYS B 2 611 ? 108.423 81.468  86.766  1.00 63.10  ? 611 LYS A CE    1 
ATOM   4620 N  NZ    . LYS B 2 611 ? 107.492 80.999  85.707  1.00 66.42  ? 611 LYS A NZ    1 
ATOM   4621 N  N     . VAL B 2 612 ? 106.972 86.484  88.151  1.00 59.24  ? 612 VAL A N     1 
ATOM   4622 C  CA    . VAL B 2 612 ? 105.648 86.417  88.762  1.00 59.52  ? 612 VAL A CA    1 
ATOM   4623 C  C     . VAL B 2 612 ? 104.831 87.609  88.289  1.00 62.45  ? 612 VAL A C     1 
ATOM   4624 O  O     . VAL B 2 612 ? 105.317 88.746  88.287  1.00 63.87  ? 612 VAL A O     1 
ATOM   4625 C  CB    . VAL B 2 612 ? 105.734 86.382  90.299  1.00 59.41  ? 612 VAL A CB    1 
ATOM   4626 C  CG1   . VAL B 2 612 ? 106.689 87.439  90.822  1.00 53.70  ? 612 VAL A CG1   1 
ATOM   4627 C  CG2   . VAL B 2 612 ? 104.349 86.557  90.909  1.00 59.03  ? 612 VAL A CG2   1 
ATOM   4628 N  N     . LYS B 2 613 ? 103.593 87.347  87.878  1.00 61.84  ? 613 LYS A N     1 
ATOM   4629 C  CA    . LYS B 2 613 ? 102.695 88.395  87.406  1.00 64.32  ? 613 LYS A CA    1 
ATOM   4630 C  C     . LYS B 2 613 ? 102.050 89.074  88.606  1.00 66.06  ? 613 LYS A C     1 
ATOM   4631 O  O     . LYS B 2 613 ? 101.245 88.462  89.317  1.00 64.08  ? 613 LYS A O     1 
ATOM   4632 C  CB    . LYS B 2 613 ? 101.639 87.806  86.475  1.00 67.32  ? 613 LYS A CB    1 
ATOM   4633 C  CG    . LYS B 2 613 ? 100.748 88.843  85.811  1.00 71.28  ? 613 LYS A CG    1 
ATOM   4634 C  CD    . LYS B 2 613 ? 99.398  88.941  86.509  1.00 72.63  ? 613 LYS A CD    1 
ATOM   4635 C  CE    . LYS B 2 613 ? 98.452  89.864  85.758  1.00 76.56  ? 613 LYS A CE    1 
ATOM   4636 N  NZ    . LYS B 2 613 ? 97.093  89.883  86.362  1.00 74.36  ? 613 LYS A NZ    1 
ATOM   4637 N  N     . CYS B 2 614 ? 102.397 90.338  88.833  1.00 70.41  ? 614 CYS A N     1 
ATOM   4638 C  CA    . CYS B 2 614 ? 101.799 91.091  89.925  1.00 65.81  ? 614 CYS A CA    1 
ATOM   4639 C  C     . CYS B 2 614 ? 100.322 91.346  89.658  1.00 66.06  ? 614 CYS A C     1 
ATOM   4640 O  O     . CYS B 2 614 ? 99.872  91.410  88.512  1.00 69.26  ? 614 CYS A O     1 
ATOM   4641 C  CB    . CYS B 2 614 ? 102.518 92.425  90.122  1.00 55.60  ? 614 CYS A CB    1 
ATOM   4642 S  SG    . CYS B 2 614 ? 103.908 92.361  91.264  1.00 47.00  ? 614 CYS A SG    1 
ATOM   4643 N  N     . GLU B 2 615 ? 99.568  91.495  90.739  1.00 62.82  ? 615 GLU A N     1 
ATOM   4644 C  CA    . GLU B 2 615 ? 98.157  91.827  90.680  1.00 63.71  ? 615 GLU A CA    1 
ATOM   4645 C  C     . GLU B 2 615 ? 97.906  93.059  91.536  1.00 63.40  ? 615 GLU A C     1 
ATOM   4646 O  O     . GLU B 2 615 ? 98.693  93.395  92.424  1.00 63.29  ? 615 GLU A O     1 
ATOM   4647 C  CB    . GLU B 2 615 ? 97.289  90.660  91.163  1.00 63.13  ? 615 GLU A CB    1 
ATOM   4648 C  CG    . GLU B 2 615 ? 96.690  89.821  90.051  1.00 65.21  ? 615 GLU A CG    1 
ATOM   4649 C  CD    . GLU B 2 615 ? 97.640  88.755  89.554  1.00 67.91  ? 615 GLU A CD    1 
ATOM   4650 O  OE1   . GLU B 2 615 ? 98.742  88.623  90.126  1.00 69.36  ? 615 GLU A OE1   1 
ATOM   4651 O  OE2   . GLU B 2 615 ? 97.285  88.046  88.590  1.00 68.58  ? 615 GLU A OE2   1 
ATOM   4652 N  N     . VAL B 2 616 ? 96.806  93.745  91.248  1.00 62.38  ? 616 VAL A N     1 
ATOM   4653 C  CA    . VAL B 2 616 ? 96.425  94.950  91.973  1.00 62.09  ? 616 VAL A CA    1 
ATOM   4654 C  C     . VAL B 2 616 ? 94.927  94.903  92.223  1.00 69.04  ? 616 VAL A C     1 
ATOM   4655 O  O     . VAL B 2 616 ? 94.154  94.569  91.320  1.00 73.82  ? 616 VAL A O     1 
ATOM   4656 C  CB    . VAL B 2 616 ? 96.810  96.226  91.200  1.00 63.63  ? 616 VAL A CB    1 
ATOM   4657 C  CG1   . VAL B 2 616 ? 95.870  97.369  91.545  1.00 64.88  ? 616 VAL A CG1   1 
ATOM   4658 C  CG2   . VAL B 2 616 ? 98.257  96.602  91.492  1.00 61.18  ? 616 VAL A CG2   1 
ATOM   4659 N  N     . SER B 2 617 ? 94.519  95.228  93.447  1.00 68.54  ? 617 SER A N     1 
ATOM   4660 C  CA    . SER B 2 617 ? 93.106  95.351  93.774  1.00 72.33  ? 617 SER A CA    1 
ATOM   4661 C  C     . SER B 2 617 ? 92.654  96.778  93.491  1.00 71.77  ? 617 SER A C     1 
ATOM   4662 O  O     . SER B 2 617 ? 93.182  97.728  94.076  1.00 69.54  ? 617 SER A O     1 
ATOM   4663 C  CB    . SER B 2 617 ? 92.861  94.988  95.236  1.00 68.33  ? 617 SER A CB    1 
ATOM   4664 O  OG    . SER B 2 617 ? 93.552  95.876  96.098  1.00 68.24  ? 617 SER A OG    1 
ATOM   4665 N  N     . VAL B 2 618 ? 91.687  96.929  92.590  1.00 70.89  ? 618 VAL A N     1 
ATOM   4666 C  CA    . VAL B 2 618 ? 91.139  98.228  92.220  1.00 71.51  ? 618 VAL A CA    1 
ATOM   4667 C  C     . VAL B 2 618 ? 89.728  98.343  92.773  1.00 75.54  ? 618 VAL A C     1 
ATOM   4668 O  O     . VAL B 2 618 ? 88.980  97.360  92.802  1.00 76.14  ? 618 VAL A O     1 
ATOM   4669 C  CB    . VAL B 2 618 ? 91.138  98.433  90.694  1.00 77.42  ? 618 VAL A CB    1 
ATOM   4670 C  CG1   . VAL B 2 618 ? 92.534  98.727  90.196  1.00 76.61  ? 618 VAL A CG1   1 
ATOM   4671 C  CG2   . VAL B 2 618 ? 90.555  97.215  89.993  1.00 74.72  ? 618 VAL A CG2   1 
ATOM   4672 N  N     . LYS B 2 619 ? 89.364  99.549  93.207  1.00 77.06  ? 619 LYS A N     1 
ATOM   4673 C  CA    . LYS B 2 619 ? 88.036  99.806  93.742  1.00 79.85  ? 619 LYS A CA    1 
ATOM   4674 C  C     . LYS B 2 619 ? 87.565  101.200 93.359  1.00 79.93  ? 619 LYS A C     1 
ATOM   4675 O  O     . LYS B 2 619 ? 88.361  102.107 93.104  1.00 73.83  ? 619 LYS A O     1 
ATOM   4676 C  CB    . LYS B 2 619 ? 88.005  99.639  95.270  1.00 77.24  ? 619 LYS A CB    1 
ATOM   4677 C  CG    . LYS B 2 619 ? 86.622  99.353  95.853  1.00 75.61  ? 619 LYS A CG    1 
ATOM   4678 C  CD    . LYS B 2 619 ? 85.982  98.083  95.302  1.00 76.02  ? 619 LYS A CD    1 
ATOM   4679 C  CE    . LYS B 2 619 ? 86.858  96.860  95.466  1.00 79.87  ? 619 LYS A CE    1 
ATOM   4680 N  NZ    . LYS B 2 619 ? 86.177  95.649  94.941  1.00 87.67  ? 619 LYS A NZ    1 
ATOM   4681 N  N     . ILE B 2 620 ? 86.244  101.349 93.316  1.00 80.29  ? 620 ILE A N     1 
ATOM   4682 C  CA    . ILE B 2 620 ? 85.592  102.640 93.155  1.00 79.50  ? 620 ILE A CA    1 
ATOM   4683 C  C     . ILE B 2 620 ? 85.156  103.083 94.542  1.00 78.84  ? 620 ILE A C     1 
ATOM   4684 O  O     . ILE B 2 620 ? 84.430  102.355 95.231  1.00 77.38  ? 620 ILE A O     1 
ATOM   4685 C  CB    . ILE B 2 620 ? 84.390  102.545 92.199  1.00 83.19  ? 620 ILE A CB    1 
ATOM   4686 C  CG1   . ILE B 2 620 ? 84.809  102.066 90.800  1.00 83.60  ? 620 ILE A CG1   1 
ATOM   4687 C  CG2   . ILE B 2 620 ? 83.698  103.899 92.079  1.00 86.32  ? 620 ILE A CG2   1 
ATOM   4688 C  CD1   . ILE B 2 620 ? 86.235  102.375 90.405  1.00 78.14  ? 620 ILE A CD1   1 
ATOM   4689 N  N     . ALA B 2 621 ? 85.589  104.269 94.956  1.00 78.74  ? 621 ALA A N     1 
ATOM   4690 C  CA    . ALA B 2 621 ? 85.502  104.670 96.353  1.00 72.43  ? 621 ALA A CA    1 
ATOM   4691 C  C     . ALA B 2 621 ? 84.846  106.031 96.489  1.00 74.15  ? 621 ALA A C     1 
ATOM   4692 O  O     . ALA B 2 621 ? 85.235  106.986 95.808  1.00 78.27  ? 621 ALA A O     1 
ATOM   4693 C  CB    . ALA B 2 621 ? 86.891  104.711 96.988  1.00 68.32  ? 621 ALA A CB    1 
ATOM   4694 N  N     . GLU B 2 622 ? 83.859  106.116 97.380  1.00 73.72  ? 622 GLU A N     1 
ATOM   4695 C  CA    . GLU B 2 622 ? 83.337  107.400 97.819  1.00 77.90  ? 622 GLU A CA    1 
ATOM   4696 C  C     . GLU B 2 622 ? 84.171  108.012 98.933  1.00 76.43  ? 622 GLU A C     1 
ATOM   4697 O  O     . GLU B 2 622 ? 83.999  109.198 99.237  1.00 78.00  ? 622 GLU A O     1 
ATOM   4698 C  CB    . GLU B 2 622 ? 81.887  107.251 98.298  1.00 82.16  ? 622 GLU A CB    1 
ATOM   4699 C  CG    . GLU B 2 622 ? 81.196  108.566 98.632  1.00 85.70  ? 622 GLU A CG    1 
ATOM   4700 C  CD    . GLU B 2 622 ? 81.134  109.514 97.453  1.00 87.36  ? 622 GLU A CD    1 
ATOM   4701 O  OE1   . GLU B 2 622 ? 81.212  109.039 96.300  1.00 87.56  ? 622 GLU A OE1   1 
ATOM   4702 O  OE2   . GLU B 2 622 ? 81.011  110.736 97.679  1.00 84.06  ? 622 GLU A OE2   1 
ATOM   4703 N  N     . ASN B 2 623 ? 85.066  107.237 99.544  1.00 73.24  ? 623 ASN A N     1 
ATOM   4704 C  CA    . ASN B 2 623 ? 85.902  107.733 100.625 1.00 69.13  ? 623 ASN A CA    1 
ATOM   4705 C  C     . ASN B 2 623 ? 87.295  107.131 100.525 1.00 65.96  ? 623 ASN A C     1 
ATOM   4706 O  O     . ASN B 2 623 ? 87.565  106.235 99.721  1.00 73.74  ? 623 ASN A O     1 
ATOM   4707 C  CB    . ASN B 2 623 ? 85.307  107.406 102.002 1.00 66.64  ? 623 ASN A CB    1 
ATOM   4708 C  CG    . ASN B 2 623 ? 83.909  107.946 102.176 1.00 73.10  ? 623 ASN A CG    1 
ATOM   4709 O  OD1   . ASN B 2 623 ? 83.674  109.147 102.051 1.00 74.08  ? 623 ASN A OD1   1 
ATOM   4710 N  ND2   . ASN B 2 623 ? 82.971  107.064 102.496 1.00 73.95  ? 623 ASN A ND2   1 
ATOM   4711 N  N     . TRP B 2 624 ? 88.181  107.654 101.369 1.00 58.06  ? 624 TRP A N     1 
ATOM   4712 C  CA    . TRP B 2 624 ? 89.481  107.037 101.592 1.00 51.41  ? 624 TRP A CA    1 
ATOM   4713 C  C     . TRP B 2 624 ? 89.344  105.780 102.441 1.00 55.61  ? 624 TRP A C     1 
ATOM   4714 O  O     . TRP B 2 624 ? 90.226  104.914 102.418 1.00 53.95  ? 624 TRP A O     1 
ATOM   4715 C  CB    . TRP B 2 624 ? 90.395  108.069 102.260 1.00 57.68  ? 624 TRP A CB    1 
ATOM   4716 C  CG    . TRP B 2 624 ? 91.708  107.597 102.785 1.00 53.56  ? 624 TRP A CG    1 
ATOM   4717 C  CD1   . TRP B 2 624 ? 92.316  108.013 103.935 1.00 57.49  ? 624 TRP A CD1   1 
ATOM   4718 C  CD2   . TRP B 2 624 ? 92.603  106.667 102.176 1.00 43.97  ? 624 TRP A CD2   1 
ATOM   4719 N  NE1   . TRP B 2 624 ? 93.523  107.388 104.087 1.00 50.12  ? 624 TRP A NE1   1 
ATOM   4720 C  CE2   . TRP B 2 624 ? 93.724  106.556 103.020 1.00 43.38  ? 624 TRP A CE2   1 
ATOM   4721 C  CE3   . TRP B 2 624 ? 92.565  105.913 101.004 1.00 47.79  ? 624 TRP A CE3   1 
ATOM   4722 C  CZ2   . TRP B 2 624 ? 94.791  105.723 102.734 1.00 42.25  ? 624 TRP A CZ2   1 
ATOM   4723 C  CZ3   . TRP B 2 624 ? 93.626  105.083 100.722 1.00 56.85  ? 624 TRP A CZ3   1 
ATOM   4724 C  CH2   . TRP B 2 624 ? 94.728  104.994 101.585 1.00 48.52  ? 624 TRP A CH2   1 
ATOM   4725 N  N     . GLY B 2 625 ? 88.244  105.666 103.190 1.00 61.86  ? 625 GLY A N     1 
ATOM   4726 C  CA    . GLY B 2 625 ? 88.067  104.521 104.070 1.00 63.64  ? 625 GLY A CA    1 
ATOM   4727 C  C     . GLY B 2 625 ? 87.534  103.299 103.345 1.00 65.64  ? 625 GLY A C     1 
ATOM   4728 O  O     . GLY B 2 625 ? 88.078  102.200 103.476 1.00 67.52  ? 625 GLY A O     1 
ATOM   4729 N  N     . SER B 2 626 ? 86.473  103.475 102.557 1.00 65.93  ? 626 SER A N     1 
ATOM   4730 C  CA    . SER B 2 626 ? 85.895  102.366 101.803 1.00 62.60  ? 626 SER A CA    1 
ATOM   4731 C  C     . SER B 2 626 ? 86.911  101.996 100.727 1.00 60.47  ? 626 SER A C     1 
ATOM   4732 O  O     . SER B 2 626 ? 86.835  102.412 99.569  1.00 62.68  ? 626 SER A O     1 
ATOM   4733 C  CB    . SER B 2 626 ? 84.542  102.744 101.212 1.00 66.35  ? 626 SER A CB    1 
ATOM   4734 O  OG    . SER B 2 626 ? 84.636  103.904 100.403 1.00 72.52  ? 626 SER A OG    1 
ATOM   4735 N  N     . LYS B 2 627 ? 87.885  101.194 101.142 1.00 59.90  ? 627 LYS A N     1 
ATOM   4736 C  CA    . LYS B 2 627 ? 89.082  100.915 100.364 1.00 57.86  ? 627 LYS A CA    1 
ATOM   4737 C  C     . LYS B 2 627 ? 88.735  100.472 98.948  1.00 63.30  ? 627 LYS A C     1 
ATOM   4738 O  O     . LYS B 2 627 ? 89.274  99.489  98.445  1.00 74.49  ? 627 LYS A O     1 
ATOM   4739 C  CB    . LYS B 2 627 ? 89.904  99.840  101.071 1.00 54.94  ? 627 LYS A CB    1 
ATOM   4740 C  CG    . LYS B 2 627 ? 91.346  99.743  100.627 1.00 50.93  ? 627 LYS A CG    1 
ATOM   4741 C  CD    . LYS B 2 627 ? 92.016  98.552  101.286 1.00 55.88  ? 627 LYS A CD    1 
ATOM   4742 C  CE    . LYS B 2 627 ? 93.516  98.570  101.078 1.00 54.22  ? 627 LYS A CE    1 
ATOM   4743 N  NZ    . LYS B 2 627 ? 94.135  99.726  101.785 1.00 51.10  ? 627 LYS A NZ    1 
ATOM   4744 P  P     . DT  C 3 4   ? 121.748 135.478 152.700 1.00 262.56 ? 4   DT  F P     1 
ATOM   4745 O  OP1   . DT  C 3 4   ? 122.588 134.981 153.812 1.00 259.39 ? 4   DT  F OP1   1 
ATOM   4746 O  OP2   . DT  C 3 4   ? 121.746 136.919 152.367 1.00 261.36 ? 4   DT  F OP2   1 
ATOM   4747 O  "O5'" . DT  C 3 4   ? 122.123 134.673 151.370 1.00 260.35 ? 4   DT  F "O5'" 1 
ATOM   4748 C  "C5'" . DT  C 3 4   ? 121.950 133.261 151.313 1.00 258.16 ? 4   DT  F "C5'" 1 
ATOM   4749 C  "C4'" . DT  C 3 4   ? 120.535 132.905 150.905 1.00 258.00 ? 4   DT  F "C4'" 1 
ATOM   4750 O  "O4'" . DT  C 3 4   ? 120.063 133.877 149.934 1.00 258.43 ? 4   DT  F "O4'" 1 
ATOM   4751 C  "C3'" . DT  C 3 4   ? 120.385 131.546 150.237 1.00 256.29 ? 4   DT  F "C3'" 1 
ATOM   4752 O  "O3'" . DT  C 3 4   ? 119.121 130.969 150.538 1.00 255.69 ? 4   DT  F "O3'" 1 
ATOM   4753 C  "C2'" . DT  C 3 4   ? 120.542 131.878 148.759 1.00 256.16 ? 4   DT  F "C2'" 1 
ATOM   4754 C  "C1'" . DT  C 3 4   ? 119.915 133.273 148.662 1.00 257.07 ? 4   DT  F "C1'" 1 
ATOM   4755 N  N1    . DT  C 3 4   ? 120.531 134.185 147.624 1.00 257.02 ? 4   DT  F N1    1 
ATOM   4756 C  C2    . DT  C 3 4   ? 119.733 135.121 147.003 1.00 256.04 ? 4   DT  F C2    1 
ATOM   4757 O  O2    . DT  C 3 4   ? 118.546 135.246 147.238 1.00 255.09 ? 4   DT  F O2    1 
ATOM   4758 N  N3    . DT  C 3 4   ? 120.376 135.904 146.082 1.00 256.12 ? 4   DT  F N3    1 
ATOM   4759 C  C4    . DT  C 3 4   ? 121.711 135.853 145.731 1.00 256.03 ? 4   DT  F C4    1 
ATOM   4760 O  O4    . DT  C 3 4   ? 122.197 136.601 144.891 1.00 256.63 ? 4   DT  F O4    1 
ATOM   4761 C  C5    . DT  C 3 4   ? 122.493 134.858 146.422 1.00 255.33 ? 4   DT  F C5    1 
ATOM   4762 C  C7    . DT  C 3 4   ? 123.952 134.707 146.124 1.00 253.07 ? 4   DT  F C7    1 
ATOM   4763 C  C6    . DT  C 3 4   ? 121.877 134.084 147.325 1.00 256.47 ? 4   DT  F C6    1 
ATOM   4764 P  P     . DG  C 3 5   ? 118.790 129.461 150.095 1.00 252.99 ? 5   DG  F P     1 
ATOM   4765 O  OP1   . DG  C 3 5   ? 118.350 128.716 151.295 1.00 257.45 ? 5   DG  F OP1   1 
ATOM   4766 O  OP2   . DG  C 3 5   ? 119.906 128.966 149.257 1.00 252.83 ? 5   DG  F OP2   1 
ATOM   4767 O  "O5'" . DG  C 3 5   ? 117.518 129.626 149.157 1.00 252.02 ? 5   DG  F "O5'" 1 
ATOM   4768 C  "C5'" . DG  C 3 5   ? 116.357 130.249 149.662 1.00 252.70 ? 5   DG  F "C5'" 1 
ATOM   4769 C  "C4'" . DG  C 3 5   ? 115.478 130.722 148.527 1.00 253.12 ? 5   DG  F "C4'" 1 
ATOM   4770 O  "O4'" . DG  C 3 5   ? 115.979 131.985 148.024 1.00 254.12 ? 5   DG  F "O4'" 1 
ATOM   4771 C  "C3'" . DG  C 3 5   ? 115.456 129.797 147.323 1.00 253.43 ? 5   DG  F "C3'" 1 
ATOM   4772 O  "O3'" . DG  C 3 5   ? 114.460 128.789 147.468 1.00 254.17 ? 5   DG  F "O3'" 1 
ATOM   4773 C  "C2'" . DG  C 3 5   ? 115.165 130.743 146.169 1.00 252.26 ? 5   DG  F "C2'" 1 
ATOM   4774 C  "C1'" . DG  C 3 5   ? 115.780 132.065 146.622 1.00 253.34 ? 5   DG  F "C1'" 1 
ATOM   4775 N  N9    . DG  C 3 5   ? 117.055 132.343 145.981 1.00 254.24 ? 5   DG  F N9    1 
ATOM   4776 C  C8    . DG  C 3 5   ? 118.224 131.645 146.144 1.00 254.52 ? 5   DG  F C8    1 
ATOM   4777 N  N7    . DG  C 3 5   ? 119.209 132.111 145.433 1.00 254.31 ? 5   DG  F N7    1 
ATOM   4778 C  C5    . DG  C 3 5   ? 118.655 133.181 144.745 1.00 254.45 ? 5   DG  F C5    1 
ATOM   4779 C  C6    . DG  C 3 5   ? 119.252 134.068 143.828 1.00 254.15 ? 5   DG  F C6    1 
ATOM   4780 O  O6    . DG  C 3 5   ? 120.424 134.065 143.429 1.00 254.09 ? 5   DG  F O6    1 
ATOM   4781 N  N1    . DG  C 3 5   ? 118.341 135.017 143.358 1.00 253.01 ? 5   DG  F N1    1 
ATOM   4782 C  C2    . DG  C 3 5   ? 117.016 135.098 143.741 1.00 251.76 ? 5   DG  F C2    1 
ATOM   4783 N  N2    . DG  C 3 5   ? 116.291 136.090 143.194 1.00 248.80 ? 5   DG  F N2    1 
ATOM   4784 N  N3    . DG  C 3 5   ? 116.449 134.267 144.611 1.00 253.14 ? 5   DG  F N3    1 
ATOM   4785 C  C4    . DG  C 3 5   ? 117.327 133.339 145.069 1.00 254.18 ? 5   DG  F C4    1 
ATOM   4786 P  P     . DT  C 3 6   ? 114.557 127.429 146.616 1.00 254.40 ? 6   DT  F P     1 
ATOM   4787 O  OP1   . DT  C 3 6   ? 114.174 126.305 147.503 1.00 251.87 ? 6   DT  F OP1   1 
ATOM   4788 O  OP2   . DT  C 3 6   ? 115.878 127.412 145.951 1.00 252.26 ? 6   DT  F OP2   1 
ATOM   4789 O  "O5'" . DT  C 3 6   ? 113.469 127.625 145.460 1.00 252.63 ? 6   DT  F "O5'" 1 
ATOM   4790 C  "C5'" . DT  C 3 6   ? 112.207 128.200 145.761 1.00 251.43 ? 6   DT  F "C5'" 1 
ATOM   4791 C  "C4'" . DT  C 3 6   ? 111.814 129.249 144.727 1.00 249.02 ? 6   DT  F "C4'" 1 
ATOM   4792 O  "O4'" . DT  C 3 6   ? 112.989 129.988 144.276 1.00 248.33 ? 6   DT  F "O4'" 1 
ATOM   4793 C  "C3'" . DT  C 3 6   ? 111.158 128.688 143.470 1.00 246.68 ? 6   DT  F "C3'" 1 
ATOM   4794 O  "O3'" . DT  C 3 6   ? 109.961 129.385 143.218 1.00 247.49 ? 6   DT  F "O3'" 1 
ATOM   4795 C  "C2'" . DT  C 3 6   ? 112.213 128.887 142.372 1.00 244.44 ? 6   DT  F "C2'" 1 
ATOM   4796 C  "C1'" . DT  C 3 6   ? 112.985 130.096 142.863 1.00 245.24 ? 6   DT  F "C1'" 1 
ATOM   4797 N  N1    . DT  C 3 6   ? 114.404 130.149 142.391 1.00 244.92 ? 6   DT  F N1    1 
ATOM   4798 C  C2    . DT  C 3 6   ? 114.785 131.041 141.397 1.00 243.15 ? 6   DT  F C2    1 
ATOM   4799 O  O2    . DT  C 3 6   ? 114.012 131.804 140.848 1.00 240.58 ? 6   DT  F O2    1 
ATOM   4800 N  N3    . DT  C 3 6   ? 116.120 130.987 141.066 1.00 243.98 ? 6   DT  F N3    1 
ATOM   4801 C  C4    . DT  C 3 6   ? 117.080 130.151 141.628 1.00 245.44 ? 6   DT  F C4    1 
ATOM   4802 O  O4    . DT  C 3 6   ? 118.249 130.159 141.280 1.00 245.89 ? 6   DT  F O4    1 
ATOM   4803 C  C5    . DT  C 3 6   ? 116.603 129.261 142.657 1.00 245.61 ? 6   DT  F C5    1 
ATOM   4804 C  C7    . DT  C 3 6   ? 117.546 128.311 143.335 1.00 244.83 ? 6   DT  F C7    1 
ATOM   4805 C  C6    . DT  C 3 6   ? 115.312 129.303 142.981 1.00 246.13 ? 6   DT  F C6    1 
ATOM   4806 P  P     . DG  C 3 7   ? 108.821 128.741 142.296 1.00 247.87 ? 7   DG  F P     1 
ATOM   4807 O  OP1   . DG  C 3 7   ? 107.613 128.572 143.136 1.00 248.30 ? 7   DG  F OP1   1 
ATOM   4808 O  OP2   . DG  C 3 7   ? 109.412 127.566 141.614 1.00 243.71 ? 7   DG  F OP2   1 
ATOM   4809 O  "O5'" . DG  C 3 7   ? 108.540 129.891 141.221 1.00 243.47 ? 7   DG  F "O5'" 1 
ATOM   4810 C  "C5'" . DG  C 3 7   ? 109.579 130.818 140.880 1.00 241.59 ? 7   DG  F "C5'" 1 
ATOM   4811 C  "C4'" . DG  C 3 7   ? 110.041 130.610 139.454 1.00 239.16 ? 7   DG  F "C4'" 1 
ATOM   4812 O  "O4'" . DG  C 3 7   ? 111.493 130.733 139.366 1.00 238.25 ? 7   DG  F "O4'" 1 
ATOM   4813 C  "C3'" . DG  C 3 7   ? 109.705 129.229 138.866 1.00 237.49 ? 7   DG  F "C3'" 1 
ATOM   4814 O  "O3'" . DG  C 3 7   ? 108.983 129.363 137.681 1.00 235.55 ? 7   DG  F "O3'" 1 
ATOM   4815 C  "C2'" . DG  C 3 7   ? 111.061 128.604 138.622 1.00 235.76 ? 7   DG  F "C2'" 1 
ATOM   4816 C  "C1'" . DG  C 3 7   ? 111.923 129.824 138.389 1.00 235.47 ? 7   DG  F "C1'" 1 
ATOM   4817 N  N9    . DG  C 3 7   ? 113.337 129.537 138.525 1.00 234.85 ? 7   DG  F N9    1 
ATOM   4818 C  C8    . DG  C 3 7   ? 113.887 128.650 139.407 1.00 236.80 ? 7   DG  F C8    1 
ATOM   4819 N  N7    . DG  C 3 7   ? 115.167 128.540 139.303 1.00 237.73 ? 7   DG  F N7    1 
ATOM   4820 C  C5    . DG  C 3 7   ? 115.498 129.390 138.268 1.00 236.67 ? 7   DG  F C5    1 
ATOM   4821 C  C6    . DG  C 3 7   ? 116.753 129.662 137.728 1.00 237.19 ? 7   DG  F C6    1 
ATOM   4822 O  O6    . DG  C 3 7   ? 117.831 129.182 138.086 1.00 237.80 ? 7   DG  F O6    1 
ATOM   4823 N  N1    . DG  C 3 7   ? 116.685 130.579 136.688 1.00 235.91 ? 7   DG  F N1    1 
ATOM   4824 C  C2    . DG  C 3 7   ? 115.527 131.165 136.225 1.00 231.84 ? 7   DG  F C2    1 
ATOM   4825 N  N2    . DG  C 3 7   ? 115.672 132.036 135.210 1.00 227.98 ? 7   DG  F N2    1 
ATOM   4826 N  N3    . DG  C 3 7   ? 114.316 130.914 136.735 1.00 230.77 ? 7   DG  F N3    1 
ATOM   4827 C  C4    . DG  C 3 7   ? 114.385 130.011 137.756 1.00 233.84 ? 7   DG  F C4    1 
ATOM   4828 P  P     . DA  C 3 8   ? 107.429 128.978 137.620 1.00 234.87 ? 8   DA  F P     1 
ATOM   4829 O  OP1   . DA  C 3 8   ? 106.714 129.696 138.700 1.00 236.93 ? 8   DA  F OP1   1 
ATOM   4830 O  OP2   . DA  C 3 8   ? 107.333 127.504 137.524 1.00 233.96 ? 8   DA  F OP2   1 
ATOM   4831 O  "O5'" . DA  C 3 8   ? 106.985 129.607 136.228 1.00 232.39 ? 8   DA  F "O5'" 1 
ATOM   4832 C  "C5'" . DA  C 3 8   ? 107.596 130.817 135.786 1.00 231.62 ? 8   DA  F "C5'" 1 
ATOM   4833 C  "C4'" . DA  C 3 8   ? 108.477 130.582 134.569 1.00 230.26 ? 8   DA  F "C4'" 1 
ATOM   4834 O  "O4'" . DA  C 3 8   ? 109.822 130.220 134.957 1.00 228.35 ? 8   DA  F "O4'" 1 
ATOM   4835 C  "C3'" . DA  C 3 8   ? 108.008 129.458 133.660 1.00 230.57 ? 8   DA  F "C3'" 1 
ATOM   4836 O  "O3'" . DA  C 3 8   ? 107.258 130.014 132.588 1.00 233.78 ? 8   DA  F "O3'" 1 
ATOM   4837 C  "C2'" . DA  C 3 8   ? 109.312 128.749 133.216 1.00 227.49 ? 8   DA  F "C2'" 1 
ATOM   4838 C  "C1'" . DA  C 3 8   ? 110.429 129.588 133.851 1.00 225.56 ? 8   DA  F "C1'" 1 
ATOM   4839 N  N9    . DA  C 3 8   ? 111.590 128.814 134.325 1.00 222.61 ? 8   DA  F N9    1 
ATOM   4840 C  C8    . DA  C 3 8   ? 111.597 127.937 135.367 1.00 224.10 ? 8   DA  F C8    1 
ATOM   4841 N  N7    . DA  C 3 8   ? 112.762 127.389 135.600 1.00 223.64 ? 8   DA  F N7    1 
ATOM   4842 C  C5    . DA  C 3 8   ? 113.593 127.941 134.645 1.00 222.38 ? 8   DA  F C5    1 
ATOM   4843 C  C6    . DA  C 3 8   ? 114.961 127.752 134.375 1.00 221.31 ? 8   DA  F C6    1 
ATOM   4844 N  N6    . DA  C 3 8   ? 115.726 126.922 135.077 1.00 221.00 ? 8   DA  F N6    1 
ATOM   4845 N  N1    . DA  C 3 8   ? 115.507 128.443 133.356 1.00 219.54 ? 8   DA  F N1    1 
ATOM   4846 C  C2    . DA  C 3 8   ? 114.725 129.278 132.653 1.00 219.38 ? 8   DA  F C2    1 
ATOM   4847 N  N3    . DA  C 3 8   ? 113.414 129.541 132.814 1.00 219.50 ? 8   DA  F N3    1 
ATOM   4848 C  C4    . DA  C 3 8   ? 112.902 128.830 133.844 1.00 220.89 ? 8   DA  F C4    1 
ATOM   4849 P  P     . DG  C 3 9   ? 106.600 129.079 131.466 1.00 235.00 ? 9   DG  F P     1 
ATOM   4850 O  OP1   . DG  C 3 9   ? 105.550 129.865 130.780 1.00 234.74 ? 9   DG  F OP1   1 
ATOM   4851 O  OP2   . DG  C 3 9   ? 106.250 127.783 132.091 1.00 232.83 ? 9   DG  F OP2   1 
ATOM   4852 O  "O5'" . DG  C 3 9   ? 107.809 128.853 130.458 1.00 231.21 ? 9   DG  F "O5'" 1 
ATOM   4853 C  "C5'" . DG  C 3 9   ? 108.680 129.937 130.138 1.00 229.83 ? 9   DG  F "C5'" 1 
ATOM   4854 C  "C4'" . DG  C 3 9   ? 109.922 129.423 129.448 1.00 227.14 ? 9   DG  F "C4'" 1 
ATOM   4855 O  "O4'" . DG  C 3 9   ? 110.862 128.924 130.422 1.00 224.34 ? 9   DG  F "O4'" 1 
ATOM   4856 C  "C3'" . DG  C 3 9   ? 109.665 128.257 128.499 1.00 226.83 ? 9   DG  F "C3'" 1 
ATOM   4857 O  "O3'" . DG  C 3 9   ? 109.617 128.717 127.158 1.00 230.00 ? 9   DG  F "O3'" 1 
ATOM   4858 C  "C2'" . DG  C 3 9   ? 110.824 127.282 128.759 1.00 220.89 ? 9   DG  F "C2'" 1 
ATOM   4859 C  "C1'" . DG  C 3 9   ? 111.701 128.000 129.782 1.00 219.31 ? 9   DG  F "C1'" 1 
ATOM   4860 N  N9    . DG  C 3 9   ? 112.278 127.114 130.787 1.00 216.05 ? 9   DG  F N9    1 
ATOM   4861 C  C8    . DG  C 3 9   ? 111.634 126.586 131.879 1.00 217.17 ? 9   DG  F C8    1 
ATOM   4862 N  N7    . DG  C 3 9   ? 112.391 125.829 132.612 1.00 214.86 ? 9   DG  F N7    1 
ATOM   4863 C  C5    . DG  C 3 9   ? 113.618 125.850 131.971 1.00 212.49 ? 9   DG  F C5    1 
ATOM   4864 C  C6    . DG  C 3 9   ? 114.817 125.206 132.316 1.00 210.71 ? 9   DG  F C6    1 
ATOM   4865 O  O6    . DG  C 3 9   ? 115.025 124.471 133.284 1.00 209.34 ? 9   DG  F O6    1 
ATOM   4866 N  N1    . DG  C 3 9   ? 115.834 125.479 131.408 1.00 211.82 ? 9   DG  F N1    1 
ATOM   4867 C  C2    . DG  C 3 9   ? 115.706 126.282 130.298 1.00 211.95 ? 9   DG  F C2    1 
ATOM   4868 N  N2    . DG  C 3 9   ? 116.807 126.429 129.540 1.00 212.79 ? 9   DG  F N2    1 
ATOM   4869 N  N3    . DG  C 3 9   ? 114.573 126.900 129.959 1.00 210.88 ? 9   DG  F N3    1 
ATOM   4870 C  C4    . DG  C 3 9   ? 113.573 126.636 130.843 1.00 212.93 ? 9   DG  F C4    1 
ATOM   4871 P  P     . DG  C 3 10  ? 109.008 127.785 126.001 1.00 236.12 ? 10  DG  F P     1 
ATOM   4872 O  OP1   . DG  C 3 10  ? 108.481 128.679 124.945 1.00 234.63 ? 10  DG  F OP1   1 
ATOM   4873 O  OP2   . DG  C 3 10  ? 108.100 126.802 126.634 1.00 234.97 ? 10  DG  F OP2   1 
ATOM   4874 O  "O5'" . DG  C 3 10  ? 110.299 127.023 125.445 1.00 225.35 ? 10  DG  F "O5'" 1 
ATOM   4875 C  "C5'" . DG  C 3 10  ? 111.483 127.769 125.205 1.00 219.22 ? 10  DG  F "C5'" 1 
ATOM   4876 C  "C4'" . DG  C 3 10  ? 112.719 126.890 125.242 1.00 211.83 ? 10  DG  F "C4'" 1 
ATOM   4877 O  "O4'" . DG  C 3 10  ? 112.957 126.428 126.594 1.00 209.26 ? 10  DG  F "O4'" 1 
ATOM   4878 C  "C3'" . DG  C 3 10  ? 112.640 125.629 124.376 1.00 207.25 ? 10  DG  F "C3'" 1 
ATOM   4879 O  "O3'" . DG  C 3 10  ? 113.510 125.732 123.229 1.00 203.76 ? 10  DG  F "O3'" 1 
ATOM   4880 C  "C2'" . DG  C 3 10  ? 113.031 124.483 125.317 1.00 199.83 ? 10  DG  F "C2'" 1 
ATOM   4881 C  "C1'" . DG  C 3 10  ? 113.610 125.188 126.532 1.00 200.15 ? 10  DG  F "C1'" 1 
ATOM   4882 N  N9    . DG  C 3 10  ? 113.391 124.460 127.777 1.00 197.66 ? 10  DG  F N9    1 
ATOM   4883 C  C8    . DG  C 3 10  ? 112.236 124.418 128.518 1.00 200.26 ? 10  DG  F C8    1 
ATOM   4884 N  N7    . DG  C 3 10  ? 112.325 123.671 129.578 1.00 198.09 ? 10  DG  F N7    1 
ATOM   4885 C  C5    . DG  C 3 10  ? 113.619 123.178 129.536 1.00 196.14 ? 10  DG  F C5    1 
ATOM   4886 C  C6    . DG  C 3 10  ? 114.283 122.311 130.425 1.00 194.97 ? 10  DG  F C6    1 
ATOM   4887 O  O6    . DG  C 3 10  ? 113.845 121.794 131.458 1.00 193.95 ? 10  DG  F O6    1 
ATOM   4888 N  N1    . DG  C 3 10  ? 115.588 122.057 130.019 1.00 195.32 ? 10  DG  F N1    1 
ATOM   4889 C  C2    . DG  C 3 10  ? 116.179 122.576 128.891 1.00 195.09 ? 10  DG  F C2    1 
ATOM   4890 N  N2    . DG  C 3 10  ? 117.453 122.215 128.671 1.00 197.66 ? 10  DG  F N2    1 
ATOM   4891 N  N3    . DG  C 3 10  ? 115.565 123.394 128.044 1.00 193.46 ? 10  DG  F N3    1 
ATOM   4892 C  C4    . DG  C 3 10  ? 114.290 123.650 128.431 1.00 194.90 ? 10  DG  F C4    1 
ATOM   4893 P  P     . DC  C 3 11  ? 115.111 125.836 123.387 1.00 197.29 ? 11  DC  F P     1 
ATOM   4894 O  OP1   . DC  C 3 11  ? 115.469 126.624 124.584 1.00 196.18 ? 11  DC  F OP1   1 
ATOM   4895 O  OP2   . DC  C 3 11  ? 115.639 126.244 122.067 1.00 194.01 ? 11  DC  F OP2   1 
ATOM   4896 O  "O5'" . DC  C 3 11  ? 115.574 124.340 123.678 1.00 191.86 ? 11  DC  F "O5'" 1 
ATOM   4897 C  "C5'" . DC  C 3 11  ? 116.808 124.098 124.344 1.00 188.39 ? 11  DC  F "C5'" 1 
ATOM   4898 C  "C4'" . DC  C 3 11  ? 117.104 122.615 124.397 1.00 182.59 ? 11  DC  F "C4'" 1 
ATOM   4899 O  "O4'" . DC  C 3 11  ? 116.513 122.043 125.601 1.00 183.22 ? 11  DC  F "O4'" 1 
ATOM   4900 C  "C3'" . DC  C 3 11  ? 116.517 121.804 123.242 1.00 175.83 ? 11  DC  F "C3'" 1 
ATOM   4901 O  "O3'" . DC  C 3 11  ? 117.368 120.723 122.904 1.00 171.66 ? 11  DC  F "O3'" 1 
ATOM   4902 C  "C2'" . DC  C 3 11  ? 115.210 121.325 123.835 1.00 174.40 ? 11  DC  F "C2'" 1 
ATOM   4903 C  "C1'" . DC  C 3 11  ? 115.698 120.956 125.218 1.00 176.34 ? 11  DC  F "C1'" 1 
ATOM   4904 N  N1    . DC  C 3 11  ? 114.646 120.739 126.238 1.00 176.85 ? 11  DC  F N1    1 
ATOM   4905 C  C2    . DC  C 3 11  ? 114.880 119.815 127.254 1.00 173.96 ? 11  DC  F C2    1 
ATOM   4906 O  O2    . DC  C 3 11  ? 115.959 119.216 127.288 1.00 172.89 ? 11  DC  F O2    1 
ATOM   4907 N  N3    . DC  C 3 11  ? 113.937 119.619 128.197 1.00 173.93 ? 11  DC  F N3    1 
ATOM   4908 C  C4    . DC  C 3 11  ? 112.785 120.286 128.130 1.00 174.79 ? 11  DC  F C4    1 
ATOM   4909 N  N4    . DC  C 3 11  ? 111.884 120.052 129.085 1.00 170.56 ? 11  DC  F N4    1 
ATOM   4910 C  C5    . DC  C 3 11  ? 112.520 121.234 127.095 1.00 177.57 ? 11  DC  F C5    1 
ATOM   4911 C  C6    . DC  C 3 11  ? 113.471 121.424 126.178 1.00 178.62 ? 11  DC  F C6    1 
ATOM   4912 P  P     . DA  C 3 12  ? 117.880 120.535 121.397 1.00 171.95 ? 12  DA  F P     1 
ATOM   4913 O  OP1   . DA  C 3 12  ? 118.417 121.845 120.968 1.00 175.40 ? 12  DA  F OP1   1 
ATOM   4914 O  OP2   . DA  C 3 12  ? 116.773 119.918 120.628 1.00 167.25 ? 12  DA  F OP2   1 
ATOM   4915 O  "O5'" . DA  C 3 12  ? 119.087 119.486 121.531 1.00 165.56 ? 12  DA  F "O5'" 1 
ATOM   4916 C  "C5'" . DA  C 3 12  ? 118.853 118.083 121.375 1.00 163.18 ? 12  DA  F "C5'" 1 
ATOM   4917 C  "C4'" . DA  C 3 12  ? 119.227 117.312 122.635 1.00 162.14 ? 12  DA  F "C4'" 1 
ATOM   4918 O  "O4'" . DA  C 3 12  ? 118.314 117.676 123.713 1.00 162.87 ? 12  DA  F "O4'" 1 
ATOM   4919 C  "C3'" . DA  C 3 12  ? 119.106 115.797 122.521 1.00 159.43 ? 12  DA  F "C3'" 1 
ATOM   4920 O  "O3'" . DA  C 3 12  ? 119.988 115.136 123.433 1.00 161.21 ? 12  DA  F "O3'" 1 
ATOM   4921 C  "C2'" . DA  C 3 12  ? 117.654 115.588 122.882 1.00 155.04 ? 12  DA  F "C2'" 1 
ATOM   4922 C  "C1'" . DA  C 3 12  ? 117.508 116.553 124.046 1.00 156.53 ? 12  DA  F "C1'" 1 
ATOM   4923 N  N9    . DA  C 3 12  ? 116.142 117.001 124.291 1.00 153.91 ? 12  DA  F N9    1 
ATOM   4924 C  C8    . DA  C 3 12  ? 115.448 117.955 123.604 1.00 155.01 ? 12  DA  F C8    1 
ATOM   4925 N  N7    . DA  C 3 12  ? 114.231 118.155 124.060 1.00 154.61 ? 12  DA  F N7    1 
ATOM   4926 C  C5    . DA  C 3 12  ? 114.124 117.270 125.120 1.00 149.07 ? 12  DA  F C5    1 
ATOM   4927 C  C6    . DA  C 3 12  ? 113.078 116.986 126.023 1.00 144.57 ? 12  DA  F C6    1 
ATOM   4928 N  N6    . DA  C 3 12  ? 111.892 117.606 125.997 1.00 144.16 ? 12  DA  F N6    1 
ATOM   4929 N  N1    . DA  C 3 12  ? 113.307 116.050 126.971 1.00 139.09 ? 12  DA  F N1    1 
ATOM   4930 C  C2    . DA  C 3 12  ? 114.494 115.433 126.987 1.00 139.99 ? 12  DA  F C2    1 
ATOM   4931 N  N3    . DA  C 3 12  ? 115.547 115.617 126.197 1.00 144.94 ? 12  DA  F N3    1 
ATOM   4932 C  C4    . DA  C 3 12  ? 115.294 116.554 125.276 1.00 148.96 ? 12  DA  F C4    1 
ATOM   4933 P  P     . DT  C 3 13  ? 120.269 113.560 123.288 1.00 167.03 ? 13  DT  F P     1 
ATOM   4934 O  OP1   . DT  C 3 13  ? 121.715 113.390 123.020 1.00 171.58 ? 13  DT  F OP1   1 
ATOM   4935 O  OP2   . DT  C 3 13  ? 119.277 113.042 122.322 1.00 159.97 ? 13  DT  F OP2   1 
ATOM   4936 O  "O5'" . DT  C 3 13  ? 119.920 112.949 124.732 1.00 156.86 ? 13  DT  F "O5'" 1 
ATOM   4937 C  "C5'" . DT  C 3 13  ? 118.622 113.133 125.294 1.00 148.17 ? 13  DT  F "C5'" 1 
ATOM   4938 C  "C4'" . DT  C 3 13  ? 118.142 111.883 126.014 1.00 141.38 ? 13  DT  F "C4'" 1 
ATOM   4939 O  "O4'" . DT  C 3 13  ? 116.761 112.073 126.423 1.00 134.26 ? 13  DT  F "O4'" 1 
ATOM   4940 C  "C3'" . DT  C 3 13  ? 118.117 110.613 125.182 1.00 138.64 ? 13  DT  F "C3'" 1 
ATOM   4941 O  "O3'" . DT  C 3 13  ? 118.193 109.470 126.027 1.00 135.86 ? 13  DT  F "O3'" 1 
ATOM   4942 C  "C2'" . DT  C 3 13  ? 116.774 110.727 124.481 1.00 131.35 ? 13  DT  F "C2'" 1 
ATOM   4943 C  "C1'" . DT  C 3 13  ? 115.898 111.308 125.589 1.00 127.47 ? 13  DT  F "C1'" 1 
ATOM   4944 N  N1    . DT  C 3 13  ? 114.774 112.196 125.130 1.00 123.64 ? 13  DT  F N1    1 
ATOM   4945 C  C2    . DT  C 3 13  ? 113.586 112.162 125.818 1.00 119.94 ? 13  DT  F C2    1 
ATOM   4946 O  O2    . DT  C 3 13  ? 113.390 111.433 126.772 1.00 117.54 ? 13  DT  F O2    1 
ATOM   4947 N  N3    . DT  C 3 13  ? 112.625 113.013 125.350 1.00 119.50 ? 13  DT  F N3    1 
ATOM   4948 C  C4    . DT  C 3 13  ? 112.730 113.880 124.286 1.00 123.49 ? 13  DT  F C4    1 
ATOM   4949 O  O4    . DT  C 3 13  ? 111.807 114.605 123.939 1.00 120.50 ? 13  DT  F O4    1 
ATOM   4950 C  C5    . DT  C 3 13  ? 113.998 113.875 123.609 1.00 128.67 ? 13  DT  F C5    1 
ATOM   4951 C  C7    . DT  C 3 13  ? 114.215 114.780 122.440 1.00 131.82 ? 13  DT  F C7    1 
ATOM   4952 C  C6    . DT  C 3 13  ? 114.954 113.048 124.058 1.00 127.81 ? 13  DT  F C6    1 
ATOM   4953 P  P     . DC  C 3 14  ? 118.527 108.020 125.424 1.00 133.14 ? 14  DC  F P     1 
ATOM   4954 O  OP1   . DC  C 3 14  ? 119.898 107.668 125.857 1.00 137.09 ? 14  DC  F OP1   1 
ATOM   4955 O  OP2   . DC  C 3 14  ? 118.187 108.041 123.983 1.00 129.40 ? 14  DC  F OP2   1 
ATOM   4956 O  "O5'" . DC  C 3 14  ? 117.486 107.052 126.163 1.00 122.76 ? 14  DC  F "O5'" 1 
ATOM   4957 C  "C5'" . DC  C 3 14  ? 116.233 106.761 125.556 1.00 117.65 ? 14  DC  F "C5'" 1 
ATOM   4958 C  "C4'" . DC  C 3 14  ? 115.140 106.594 126.597 1.00 112.08 ? 14  DC  F "C4'" 1 
ATOM   4959 O  "O4'" . DC  C 3 14  ? 114.351 107.814 126.652 1.00 109.81 ? 14  DC  F "O4'" 1 
ATOM   4960 C  "C3'" . DC  C 3 14  ? 114.139 105.481 126.306 1.00 108.18 ? 14  DC  F "C3'" 1 
ATOM   4961 O  "O3'" . DC  C 3 14  ? 113.594 104.935 127.511 1.00 106.49 ? 14  DC  F "O3'" 1 
ATOM   4962 C  "C2'" . DC  C 3 14  ? 113.086 106.192 125.483 1.00 103.46 ? 14  DC  F "C2'" 1 
ATOM   4963 C  "C1'" . DC  C 3 14  ? 113.068 107.593 126.087 1.00 103.98 ? 14  DC  F "C1'" 1 
ATOM   4964 N  N1    . DC  C 3 14  ? 112.782 108.675 125.086 1.00 106.66 ? 14  DC  F N1    1 
ATOM   4965 C  C2    . DC  C 3 14  ? 111.559 109.353 125.127 1.00 103.62 ? 14  DC  F C2    1 
ATOM   4966 O  O2    . DC  C 3 14  ? 110.736 109.058 125.995 1.00 100.73 ? 14  DC  F O2    1 
ATOM   4967 N  N3    . DC  C 3 14  ? 111.313 110.325 124.216 1.00 102.22 ? 14  DC  F N3    1 
ATOM   4968 C  C4    . DC  C 3 14  ? 112.224 110.618 123.291 1.00 106.96 ? 14  DC  F C4    1 
ATOM   4969 N  N4    . DC  C 3 14  ? 111.932 111.584 122.411 1.00 106.70 ? 14  DC  F N4    1 
ATOM   4970 C  C5    . DC  C 3 14  ? 113.475 109.937 123.228 1.00 111.73 ? 14  DC  F C5    1 
ATOM   4971 C  C6    . DC  C 3 14  ? 113.708 108.981 124.135 1.00 111.61 ? 14  DC  F C6    1 
ATOM   4972 P  P     . DC  C 3 15  ? 112.804 103.532 127.483 1.00 102.46 ? 15  DC  F P     1 
ATOM   4973 O  OP1   . DC  C 3 15  ? 112.726 103.041 128.876 1.00 100.88 ? 15  DC  F OP1   1 
ATOM   4974 O  OP2   . DC  C 3 15  ? 113.428 102.695 126.435 1.00 102.44 ? 15  DC  F OP2   1 
ATOM   4975 O  "O5'" . DC  C 3 15  ? 111.324 103.914 126.998 1.00 96.57  ? 15  DC  F "O5'" 1 
ATOM   4976 C  "C5'" . DC  C 3 15  ? 110.578 104.890 127.713 1.00 91.61  ? 15  DC  F "C5'" 1 
ATOM   4977 C  "C4'" . DC  C 3 15  ? 109.116 104.488 127.873 1.00 85.51  ? 15  DC  F "C4'" 1 
ATOM   4978 O  "O4'" . DC  C 3 15  ? 108.277 105.457 127.205 1.00 83.85  ? 15  DC  F "O4'" 1 
ATOM   4979 C  "C3'" . DC  C 3 15  ? 108.714 103.157 127.267 1.00 79.66  ? 15  DC  F "C3'" 1 
ATOM   4980 O  "O3'" . DC  C 3 15  ? 107.583 102.627 127.965 1.00 76.57  ? 15  DC  F "O3'" 1 
ATOM   4981 C  "C2'" . DC  C 3 15  ? 108.401 103.528 125.818 1.00 77.87  ? 15  DC  F "C2'" 1 
ATOM   4982 C  "C1'" . DC  C 3 15  ? 107.925 104.986 125.916 1.00 80.43  ? 15  DC  F "C1'" 1 
ATOM   4983 N  N1    . DC  C 3 15  ? 108.530 105.916 124.901 1.00 82.55  ? 15  DC  F N1    1 
ATOM   4984 C  C2    . DC  C 3 15  ? 107.734 106.885 124.285 1.00 78.28  ? 15  DC  F C2    1 
ATOM   4985 O  O2    . DC  C 3 15  ? 106.538 106.960 124.572 1.00 75.81  ? 15  DC  F O2    1 
ATOM   4986 N  N3    . DC  C 3 15  ? 108.298 107.723 123.383 1.00 77.06  ? 15  DC  F N3    1 
ATOM   4987 C  C4    . DC  C 3 15  ? 109.592 107.622 123.096 1.00 81.52  ? 15  DC  F C4    1 
ATOM   4988 N  N4    . DC  C 3 15  ? 110.101 108.470 122.197 1.00 81.03  ? 15  DC  F N4    1 
ATOM   4989 C  C5    . DC  C 3 15  ? 110.423 106.647 123.714 1.00 86.34  ? 15  DC  F C5    1 
ATOM   4990 C  C6    . DC  C 3 15  ? 109.857 105.828 124.605 1.00 85.66  ? 15  DC  F C6    1 
ATOM   4991 P  P     . DG  C 3 16  ? 106.813 101.326 127.426 1.00 81.35  ? 16  DG  F P     1 
ATOM   4992 O  OP1   . DG  C 3 16  ? 106.040 100.752 128.550 1.00 75.69  ? 16  DG  F OP1   1 
ATOM   4993 O  OP2   . DG  C 3 16  ? 107.794 100.493 126.698 1.00 88.41  ? 16  DG  F OP2   1 
ATOM   4994 O  "O5'" . DG  C 3 16  ? 105.779 101.918 126.365 1.00 77.92  ? 16  DG  F "O5'" 1 
ATOM   4995 C  "C5'" . DG  C 3 16  ? 104.814 102.878 126.771 1.00 72.42  ? 16  DG  F "C5'" 1 
ATOM   4996 C  "C4'" . DG  C 3 16  ? 103.950 103.294 125.597 1.00 66.87  ? 16  DG  F "C4'" 1 
ATOM   4997 O  "O4'" . DG  C 3 16  ? 104.661 104.289 124.800 1.00 67.76  ? 16  DG  F "O4'" 1 
ATOM   4998 C  "C3'" . DG  C 3 16  ? 103.598 102.149 124.647 1.00 61.31  ? 16  DG  F "C3'" 1 
ATOM   4999 O  "O3'" . DG  C 3 16  ? 102.210 102.114 124.376 1.00 53.54  ? 16  DG  F "O3'" 1 
ATOM   5000 C  "C2'" . DG  C 3 16  ? 104.425 102.439 123.402 1.00 61.55  ? 16  DG  F "C2'" 1 
ATOM   5001 C  "C1'" . DG  C 3 16  ? 104.579 103.949 123.436 1.00 64.05  ? 16  DG  F "C1'" 1 
ATOM   5002 N  N9    . DG  C 3 16  ? 105.770 104.437 122.738 1.00 63.55  ? 16  DG  F N9    1 
ATOM   5003 C  C8    . DG  C 3 16  ? 107.052 103.956 122.851 1.00 66.81  ? 16  DG  F C8    1 
ATOM   5004 N  N7    . DG  C 3 16  ? 107.912 104.584 122.096 1.00 68.22  ? 16  DG  F N7    1 
ATOM   5005 C  C5    . DG  C 3 16  ? 107.153 105.539 121.434 1.00 64.75  ? 16  DG  F C5    1 
ATOM   5006 C  C6    . DG  C 3 16  ? 107.540 106.517 120.485 1.00 58.65  ? 16  DG  F C6    1 
ATOM   5007 O  O6    . DG  C 3 16  ? 108.670 106.740 120.024 1.00 56.02  ? 16  DG  F O6    1 
ATOM   5008 N  N1    . DG  C 3 16  ? 106.459 107.283 120.066 1.00 55.05  ? 16  DG  F N1    1 
ATOM   5009 C  C2    . DG  C 3 16  ? 105.167 107.128 120.509 1.00 55.60  ? 16  DG  F C2    1 
ATOM   5010 N  N2    . DG  C 3 16  ? 104.260 107.961 119.992 1.00 50.06  ? 16  DG  F N2    1 
ATOM   5011 N  N3    . DG  C 3 16  ? 104.791 106.218 121.398 1.00 59.65  ? 16  DG  F N3    1 
ATOM   5012 C  C4    . DG  C 3 16  ? 105.831 105.462 121.817 1.00 62.89  ? 16  DG  F C4    1 
ATOM   5013 P  P     . DT  C 3 17  ? 101.524 100.730 123.941 1.00 63.17  ? 17  DT  F P     1 
ATOM   5014 O  OP1   . DT  C 3 17  ? 100.481 100.400 124.935 1.00 67.87  ? 17  DT  F OP1   1 
ATOM   5015 O  OP2   . DT  C 3 17  ? 102.611 99.769  123.655 1.00 72.59  ? 17  DT  F OP2   1 
ATOM   5016 O  "O5'" . DT  C 3 17  ? 100.825 101.074 122.552 1.00 62.50  ? 17  DT  F "O5'" 1 
ATOM   5017 C  "C5'" . DT  C 3 17  ? 99.931  102.162 122.465 1.00 59.28  ? 17  DT  F "C5'" 1 
ATOM   5018 C  "C4'" . DT  C 3 17  ? 100.045 102.839 121.113 1.00 55.42  ? 17  DT  F "C4'" 1 
ATOM   5019 O  "O4'" . DT  C 3 17  ? 101.409 103.265 120.904 1.00 53.06  ? 17  DT  F "O4'" 1 
ATOM   5020 C  "C3'" . DT  C 3 17  ? 99.708  101.946 119.916 1.00 49.68  ? 17  DT  F "C3'" 1 
ATOM   5021 O  "O3'" . DT  C 3 17  ? 98.431  102.281 119.389 1.00 44.47  ? 17  DT  F "O3'" 1 
ATOM   5022 C  "C2'" . DT  C 3 17  ? 100.843 102.196 118.911 1.00 44.14  ? 17  DT  F "C2'" 1 
ATOM   5023 C  "C1'" . DT  C 3 17  ? 101.633 103.345 119.526 1.00 47.53  ? 17  DT  F "C1'" 1 
ATOM   5024 N  N1    . DT  C 3 17  ? 103.100 103.286 119.263 1.00 47.10  ? 17  DT  F N1    1 
ATOM   5025 C  C2    . DT  C 3 17  ? 103.643 104.136 118.335 1.00 48.29  ? 17  DT  F C2    1 
ATOM   5026 O  O2    . DT  C 3 17  ? 102.985 104.938 117.706 1.00 49.40  ? 17  DT  F O2    1 
ATOM   5027 N  N3    . DT  C 3 17  ? 104.991 104.008 118.156 1.00 48.59  ? 17  DT  F N3    1 
ATOM   5028 C  C4    . DT  C 3 17  ? 105.836 103.137 118.806 1.00 50.85  ? 17  DT  F C4    1 
ATOM   5029 O  O4    . DT  C 3 17  ? 107.039 103.099 118.578 1.00 53.17  ? 17  DT  F O4    1 
ATOM   5030 C  C5    . DT  C 3 17  ? 105.206 102.273 119.772 1.00 50.28  ? 17  DT  F C5    1 
ATOM   5031 C  C7    . DT  C 3 17  ? 106.030 101.281 120.538 1.00 54.91  ? 17  DT  F C7    1 
ATOM   5032 C  C6    . DT  C 3 17  ? 103.881 102.386 119.952 1.00 50.34  ? 17  DT  F C6    1 
ATOM   5033 P  P     . DA  C 3 18  ? 97.776  101.500 118.157 1.00 63.85  ? 18  DA  F P     1 
ATOM   5034 O  OP1   . DA  C 3 18  ? 96.270  101.638 118.183 1.00 60.44  ? 18  DA  F OP1   1 
ATOM   5035 O  OP2   . DA  C 3 18  ? 98.280  100.087 117.984 1.00 58.93  ? 18  DA  F OP2   1 
ATOM   5036 O  "O5'" . DA  C 3 18  ? 98.316  102.391 116.935 1.00 58.22  ? 18  DA  F "O5'" 1 
ATOM   5037 C  "C5'" . DA  C 3 18  ? 97.876  103.767 116.838 1.00 48.75  ? 18  DA  F "C5'" 1 
ATOM   5038 C  "C4'" . DA  C 3 18  ? 98.343  104.347 115.529 1.00 39.58  ? 18  DA  F "C4'" 1 
ATOM   5039 O  "O4'" . DA  C 3 18  ? 99.672  104.868 115.692 1.00 34.58  ? 18  DA  F "O4'" 1 
ATOM   5040 C  "C3'" . DA  C 3 18  ? 98.463  103.337 114.407 1.00 43.53  ? 18  DA  F "C3'" 1 
ATOM   5041 O  "O3'" . DA  C 3 18  ? 97.193  103.184 113.782 1.00 51.67  ? 18  DA  F "O3'" 1 
ATOM   5042 C  "C2'" . DA  C 3 18  ? 99.478  104.019 113.498 1.00 39.33  ? 18  DA  F "C2'" 1 
ATOM   5043 C  "C1'" . DA  C 3 18  ? 100.363 104.799 114.453 1.00 32.10  ? 18  DA  F "C1'" 1 
ATOM   5044 N  N9    . DA  C 3 18  ? 101.646 104.169 114.720 1.00 29.76  ? 18  DA  F N9    1 
ATOM   5045 C  C8    . DA  C 3 18  ? 101.895 103.224 115.678 1.00 33.35  ? 18  DA  F C8    1 
ATOM   5046 N  N7    . DA  C 3 18  ? 103.144 102.842 115.712 1.00 34.27  ? 18  DA  F N7    1 
ATOM   5047 C  C5    . DA  C 3 18  ? 103.762 103.583 114.720 1.00 31.52  ? 18  DA  F C5    1 
ATOM   5048 C  C6    . DA  C 3 18  ? 105.089 103.623 114.260 1.00 31.40  ? 18  DA  F C6    1 
ATOM   5049 N  N6    . DA  C 3 18  ? 106.067 102.881 114.762 1.00 31.12  ? 18  DA  F N6    1 
ATOM   5050 N  N1    . DA  C 3 18  ? 105.373 104.463 113.243 1.00 30.82  ? 18  DA  F N1    1 
ATOM   5051 C  C2    . DA  C 3 18  ? 104.382 105.203 112.739 1.00 33.83  ? 18  DA  F C2    1 
ATOM   5052 N  N3    . DA  C 3 18  ? 103.102 105.252 113.094 1.00 36.36  ? 18  DA  F N3    1 
ATOM   5053 C  C4    . DA  C 3 18  ? 102.849 104.405 114.100 1.00 32.25  ? 18  DA  F C4    1 
ATOM   5054 P  P     . DG  C 3 19  ? 97.053  101.764 113.051 1.00 59.17  ? 19  DG  F P     1 
ATOM   5055 O  OP1   . DG  C 3 19  ? 95.645  101.514 112.591 1.00 60.67  ? 19  DG  F OP1   1 
ATOM   5056 O  OP2   . DG  C 3 19  ? 97.624  100.662 113.896 1.00 49.50  ? 19  DG  F OP2   1 
ATOM   5057 O  "O5'" . DG  C 3 19  ? 97.975  101.919 111.746 1.00 51.59  ? 19  DG  F "O5'" 1 
ATOM   5058 C  "C5'" . DG  C 3 19  ? 97.546  102.799 110.683 1.00 47.69  ? 19  DG  F "C5'" 1 
ATOM   5059 C  "C4'" . DG  C 3 19  ? 98.746  103.183 109.856 1.00 43.85  ? 19  DG  F "C4'" 1 
ATOM   5060 O  "O4'" . DG  C 3 19  ? 99.887  103.327 110.715 1.00 39.05  ? 19  DG  F "O4'" 1 
ATOM   5061 C  "C3'" . DG  C 3 19  ? 99.212  102.125 108.878 1.00 45.93  ? 19  DG  F "C3'" 1 
ATOM   5062 O  "O3'" . DG  C 3 19  ? 98.449  102.089 107.675 1.00 53.89  ? 19  DG  F "O3'" 1 
ATOM   5063 C  "C2'" . DG  C 3 19  ? 100.646 102.573 108.612 1.00 41.35  ? 19  DG  F "C2'" 1 
ATOM   5064 C  "C1'" . DG  C 3 19  ? 101.070 103.183 109.935 1.00 34.22  ? 19  DG  F "C1'" 1 
ATOM   5065 N  N9    . DG  C 3 19  ? 102.006 102.369 110.698 1.00 28.39  ? 19  DG  F N9    1 
ATOM   5066 C  C8    . DG  C 3 19  ? 101.714 101.601 111.794 1.00 30.61  ? 19  DG  F C8    1 
ATOM   5067 N  N7    . DG  C 3 19  ? 102.760 100.987 112.285 1.00 31.10  ? 19  DG  F N7    1 
ATOM   5068 C  C5    . DG  C 3 19  ? 103.808 101.385 111.466 1.00 29.73  ? 19  DG  F C5    1 
ATOM   5069 C  C6    . DG  C 3 19  ? 105.183 101.043 111.514 1.00 29.61  ? 19  DG  F C6    1 
ATOM   5070 O  O6    . DG  C 3 19  ? 105.769 100.301 112.312 1.00 30.44  ? 19  DG  F O6    1 
ATOM   5071 N  N1    . DG  C 3 19  ? 105.896 101.664 110.495 1.00 27.27  ? 19  DG  F N1    1 
ATOM   5072 C  C2    . DG  C 3 19  ? 105.359 102.501 109.555 1.00 30.82  ? 19  DG  F C2    1 
ATOM   5073 N  N2    . DG  C 3 19  ? 106.210 102.997 108.649 1.00 36.24  ? 19  DG  F N2    1 
ATOM   5074 N  N3    . DG  C 3 19  ? 104.070 102.829 109.507 1.00 29.03  ? 19  DG  F N3    1 
ATOM   5075 C  C4    . DG  C 3 19  ? 103.356 102.236 110.488 1.00 27.60  ? 19  DG  F C4    1 
HETATM 5076 P  P     . 2DA C 3 20  ? 98.359  100.597 107.088 1.00 66.24  ? 20  2DA F P     1 
HETATM 5077 O  OP1   . 2DA C 3 20  ? 96.956  100.124 107.320 1.00 65.22  ? 20  2DA F OP1   1 
HETATM 5078 O  OP2   . 2DA C 3 20  ? 99.505  99.782  107.587 1.00 55.25  ? 20  2DA F OP2   1 
HETATM 5079 O  "O5'" . 2DA C 3 20  ? 98.657  100.820 105.543 1.00 50.02  ? 20  2DA F "O5'" 1 
HETATM 5080 C  "C5'" . 2DA C 3 20  ? 99.498  99.879  104.906 1.00 50.06  ? 20  2DA F "C5'" 1 
HETATM 5081 C  "C4'" . 2DA C 3 20  ? 100.870 100.495 104.790 1.00 41.74  ? 20  2DA F "C4'" 1 
HETATM 5082 O  "O4'" . 2DA C 3 20  ? 101.416 100.682 106.079 1.00 38.24  ? 20  2DA F "O4'" 1 
HETATM 5083 C  "C3'" . 2DA C 3 20  ? 101.821 99.569  104.062 1.00 42.95  ? 20  2DA F "C3'" 1 
HETATM 5084 C  "C2'" . 2DA C 3 20  ? 103.131 99.650  104.817 1.00 37.52  ? 20  2DA F "C2'" 1 
HETATM 5085 C  "C1'" . 2DA C 3 20  ? 102.813 100.408 106.087 1.00 36.38  ? 20  2DA F "C1'" 1 
HETATM 5086 N  N9    . 2DA C 3 20  ? 103.212 99.608  107.260 1.00 34.86  ? 20  2DA F N9    1 
HETATM 5087 C  C8    . 2DA C 3 20  ? 102.427 99.099  108.217 1.00 34.97  ? 20  2DA F C8    1 
HETATM 5088 N  N7    . 2DA C 3 20  ? 103.156 98.427  109.132 1.00 32.06  ? 20  2DA F N7    1 
HETATM 5089 C  C5    . 2DA C 3 20  ? 104.429 98.511  108.748 1.00 30.48  ? 20  2DA F C5    1 
HETATM 5090 C  C6    . 2DA C 3 20  ? 105.712 98.031  109.257 1.00 28.47  ? 20  2DA F C6    1 
HETATM 5091 N  N6    . 2DA C 3 20  ? 105.769 97.310  110.389 1.00 26.54  ? 20  2DA F N6    1 
HETATM 5092 N  N1    . 2DA C 3 20  ? 106.812 98.336  108.559 1.00 31.21  ? 20  2DA F N1    1 
HETATM 5093 C  C2    . 2DA C 3 20  ? 106.749 99.063  107.435 1.00 33.83  ? 20  2DA F C2    1 
HETATM 5094 N  N3    . 2DA C 3 20  ? 105.619 99.538  106.910 1.00 32.03  ? 20  2DA F N3    1 
HETATM 5095 C  C4    . 2DA C 3 20  ? 104.456 99.291  107.519 1.00 32.99  ? 20  2DA F C4    1 
HETATM 5096 MG MG    B MG  D 4 .   ? 99.085  96.262  99.805  0.50 50.48  ? 701 MG  A MG    1 
HETATM 5097 P  PG    . DGT E 5 .   ? 98.144  92.643  100.940 1.00 48.64  ? 702 DGT A PG    1 
HETATM 5098 O  O1G   . DGT E 5 .   ? 98.102  91.792  99.718  1.00 52.25  ? 702 DGT A O1G   1 
HETATM 5099 O  O2G   . DGT E 5 .   ? 97.130  92.224  101.953 1.00 51.15  ? 702 DGT A O2G   1 
HETATM 5100 O  O3G   . DGT E 5 .   ? 98.072  94.104  100.620 1.00 46.71  ? 702 DGT A O3G   1 
HETATM 5101 O  O3B   . DGT E 5 .   ? 99.567  92.374  101.607 1.00 43.84  ? 702 DGT A O3B   1 
HETATM 5102 P  PB    . DGT E 5 .   ? 100.896 93.241  101.497 1.00 44.48  ? 702 DGT A PB    1 
HETATM 5103 O  O1B   . DGT E 5 .   ? 102.069 92.357  101.675 1.00 41.06  ? 702 DGT A O1B   1 
HETATM 5104 O  O2B   . DGT E 5 .   ? 100.797 94.069  100.273 1.00 50.52  ? 702 DGT A O2B   1 
HETATM 5105 O  O3A   . DGT E 5 .   ? 100.760 94.194  102.778 1.00 46.66  ? 702 DGT A O3A   1 
HETATM 5106 P  PA    . DGT E 5 .   ? 100.304 95.704  103.100 1.00 45.80  ? 702 DGT A PA    1 
HETATM 5107 O  O1A   . DGT E 5 .   ? 100.461 95.986  104.553 1.00 43.27  ? 702 DGT A O1A   1 
HETATM 5108 O  O2A   . DGT E 5 .   ? 98.954  95.968  102.529 1.00 51.79  ? 702 DGT A O2A   1 
HETATM 5109 O  "O5'" . DGT E 5 .   ? 101.396 96.536  102.288 1.00 43.33  ? 702 DGT A "O5'" 1 
HETATM 5110 C  "C5'" . DGT E 5 .   ? 102.666 95.907  102.064 1.00 40.57  ? 702 DGT A "C5'" 1 
HETATM 5111 C  "C4'" . DGT E 5 .   ? 103.624 96.418  103.097 1.00 43.91  ? 702 DGT A "C4'" 1 
HETATM 5112 O  "O4'" . DGT E 5 .   ? 103.241 95.924  104.387 1.00 47.13  ? 702 DGT A "O4'" 1 
HETATM 5113 C  "C3'" . DGT E 5 .   ? 105.051 95.934  102.924 1.00 43.45  ? 702 DGT A "C3'" 1 
HETATM 5114 O  "O3'" . DGT E 5 .   ? 105.805 96.936  102.254 1.00 55.33  ? 702 DGT A "O3'" 1 
HETATM 5115 C  "C2'" . DGT E 5 .   ? 105.545 95.724  104.356 1.00 40.76  ? 702 DGT A "C2'" 1 
HETATM 5116 C  "C1'" . DGT E 5 .   ? 104.370 96.173  105.208 1.00 40.78  ? 702 DGT A "C1'" 1 
HETATM 5117 N  N9    . DGT E 5 .   ? 104.187 95.508  106.497 1.00 34.31  ? 702 DGT A N9    1 
HETATM 5118 C  C8    . DGT E 5 .   ? 102.995 95.369  107.160 1.00 33.15  ? 702 DGT A C8    1 
HETATM 5119 N  N7    . DGT E 5 .   ? 103.116 94.771  108.318 1.00 33.20  ? 702 DGT A N7    1 
HETATM 5120 C  C5    . DGT E 5 .   ? 104.476 94.521  108.431 1.00 35.25  ? 702 DGT A C5    1 
HETATM 5121 C  C6    . DGT E 5 .   ? 105.201 93.897  109.475 1.00 39.12  ? 702 DGT A C6    1 
HETATM 5122 O  O6    . DGT E 5 .   ? 104.767 93.432  110.537 1.00 40.06  ? 702 DGT A O6    1 
HETATM 5123 N  N1    . DGT E 5 .   ? 106.565 93.842  109.186 1.00 37.54  ? 702 DGT A N1    1 
HETATM 5124 C  C2    . DGT E 5 .   ? 107.155 94.331  108.049 1.00 34.81  ? 702 DGT A C2    1 
HETATM 5125 N  N2    . DGT E 5 .   ? 108.483 94.199  107.946 1.00 36.17  ? 702 DGT A N2    1 
HETATM 5126 N  N3    . DGT E 5 .   ? 106.478 94.922  107.072 1.00 32.87  ? 702 DGT A N3    1 
HETATM 5127 C  C4    . DGT E 5 .   ? 105.149 94.977  107.322 1.00 33.54  ? 702 DGT A C4    1 
# 
