data_9AU5
# 
_entry.id   9AU5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9AU5         pdb_00009au5 10.2210/pdb9au5/pdb 
WWPDB D_1000281930 ?            ?                   
EMDB  EMD-43855    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'EM metadata'     1 0 2025-03-05 ? 
3 'Half map'        1 0 2025-03-05 1 
4 'Half map'        1 0 2025-03-05 2 
5 Image             1 0 2025-03-05 ? 
6 'Primary map'     1 0 2025-03-05 ? 
7 'Structure model' 1 1 2025-03-12 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 'Half map'        repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 Image             repository 'Initial release' ? ? 
6 6 'Primary map'     repository 'Initial release' ? ? 
# 
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 7 'Structure model' 'Data collection'     
2 7 '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 7 'Structure model' citation        
2 7 'Structure model' citation_author 
3 7 '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  7 'Structure model' '_citation.country'                 
2  7 'Structure model' '_citation.journal_abbrev'          
3  7 'Structure model' '_citation.journal_id_CSD'          
4  7 'Structure model' '_citation.journal_id_ISSN'         
5  7 'Structure model' '_citation.journal_volume'          
6  7 'Structure model' '_citation.page_first'              
7  7 'Structure model' '_citation.page_last'               
8  7 'Structure model' '_citation.pdbx_database_id_DOI'    
9  7 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 7 'Structure model' '_citation.title'                   
11 7 'Structure model' '_citation.year'                    
12 7 'Structure model' '_citation_author.identifier_ORCID' 
13 7 '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                        9AU5 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-28 
_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 complex of human DNA polymerase theta polymerase domain with a cognate G:C base pair' 
_pdbx_database_related.db_id          EMD-43855 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 3 
_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 
'Li, C.'  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            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                2063 
_citation.page_last                 2063 
_citation.title                     'Structural basis of error-prone DNA synthesis by DNA polymerase theta.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-57269-9 
_citation.pdbx_database_id_PubMed   40021647 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Li, C.'        1 ?                   
primary 'Maksoud, L.M.' 2 ?                   
primary 'Gao, Y.'       3 0000-0002-4037-0431 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'DNA polymerase theta'                                     89585.555 1 2.7.7.7 ? ? ? 
2 polymer     syn 
;DNA (5'-D(*AP*GP*CP*TP*CP*TP*AP*CP*GP*GP*AP*TP*GP*C)-3')
;
8864.712  1 ?       ? ? ? 
3 polymer     syn 
;DNA (5'-D(P*GP*CP*AP*TP*CP*CP*GP*TP*AP*GP*(2DA))-3')
;
6174.001  1 ?       ? ? ? 
4 non-polymer syn "2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE"                        507.181   1 ?       ? ? ? 
5 non-polymer syn 'MAGNESIUM ION'                                            24.305    1 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'DNA polymerase eta' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)'        no no  
;GFKDNSPISDTSFSLQLSQDGLQLTPASSSSESLSIIDVASDQNLFQTFIKEWRCKKRFSISLACEKIRSLTSSKTATIG
SRFKQASSPQEIPIRDDGFPIKGCDDTLVVGLAVCWGGRDAYYFSLQKEQKHSEISASLVPPSLDPSLTLKDRMWYLQSC
LRKESDKECSVVIYDFIQSYKILLLSCGISLEQSYEDPKVACWLLDPDSQEPTLHSIVTSFLPHELPLLEGMETSQGIQS
LGLNAGSEHSGRYRASVESILIFNSMNQLNSLLQKENLQDVFRKVEMPSQYCLALLELNGIGFSTAECESQKHIMQAKLD
AIETQAYQLAGHSFSFTSSDDIAEVLFLELKLPPNREMKNQGSKKTLGSTRRGIDNGRKLRLGRQFSTSKDVLNKLKALH
PLPGLILEWRRITNAITKVVFPLQREKCLNPFLGMERIYPVSQSHTATGRITFTEPNIQNVPRDFEIKMPTLVGESPPSQ
AVGKGLLPMGRGKYKKGFSVNPRCQAQMEERAADRGMPFSISMRHAFVPFPGGSILAADYSQLELRILAHLSHDRRLIQV
LNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGIIYGMGAKSLGEQMGIKENDAACYIDSFKSRYTGINQFMTETV
KNCKRDGFVQTILGRRRYLPGIKDNNPYRKAHAERQAINTIVQGSAADIVKIATVNIQKQLETFHSTFKSHGHREGMLQS
DQTGLSRKRKLQGMFCPIRGGFFILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKLSVKLKVKVKIGASWGELKDFDV
;
;GFKDNSPISDTSFSLQLSQDGLQLTPASSSSESLSIIDVASDQNLFQTFIKEWRCKKRFSISLACEKIRSLTSSKTATIG
SRFKQASSPQEIPIRDDGFPIKGCDDTLVVGLAVCWGGRDAYYFSLQKEQKHSEISASLVPPSLDPSLTLKDRMWYLQSC
LRKESDKECSVVIYDFIQSYKILLLSCGISLEQSYEDPKVACWLLDPDSQEPTLHSIVTSFLPHELPLLEGMETSQGIQS
LGLNAGSEHSGRYRASVESILIFNSMNQLNSLLQKENLQDVFRKVEMPSQYCLALLELNGIGFSTAECESQKHIMQAKLD
AIETQAYQLAGHSFSFTSSDDIAEVLFLELKLPPNREMKNQGSKKTLGSTRRGIDNGRKLRLGRQFSTSKDVLNKLKALH
PLPGLILEWRRITNAITKVVFPLQREKCLNPFLGMERIYPVSQSHTATGRITFTEPNIQNVPRDFEIKMPTLVGESPPSQ
AVGKGLLPMGRGKYKKGFSVNPRCQAQMEERAADRGMPFSISMRHAFVPFPGGSILAADYSQLELRILAHLSHDRRLIQV
LNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGIIYGMGAKSLGEQMGIKENDAACYIDSFKSRYTGINQFMTETV
KNCKRDGFVQTILGRRRYLPGIKDNNPYRKAHAERQAINTIVQGSAADIVKIATVNIQKQLETFHSTFKSHGHREGMLQS
DQTGLSRKRKLQGMFCPIRGGFFILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKLSVKLKVKVKIGASWGELKDFDV
;
A ? 
2 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 ? 
3 polydeoxyribonucleotide no yes 
;(DT)(DG)(DC)(DT)(DG)(DT)(DG)(DA)(DG)(DG)(DC)(DA)(DT)(DC)(DC)(DG)(DT)(DA)(DG)
(2DA)
;
TGCTGTGAGGCATCCGTAGA F ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 "2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE" DGT 
5 'MAGNESIUM ION'                     MG  
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PHE n 
1 3   LYS n 
1 4   ASP n 
1 5   ASN n 
1 6   SER n 
1 7   PRO n 
1 8   ILE n 
1 9   SER n 
1 10  ASP n 
1 11  THR n 
1 12  SER n 
1 13  PHE n 
1 14  SER n 
1 15  LEU n 
1 16  GLN n 
1 17  LEU n 
1 18  SER n 
1 19  GLN n 
1 20  ASP n 
1 21  GLY n 
1 22  LEU n 
1 23  GLN n 
1 24  LEU n 
1 25  THR n 
1 26  PRO n 
1 27  ALA n 
1 28  SER n 
1 29  SER n 
1 30  SER n 
1 31  SER n 
1 32  GLU n 
1 33  SER n 
1 34  LEU n 
1 35  SER n 
1 36  ILE n 
1 37  ILE n 
1 38  ASP n 
1 39  VAL n 
1 40  ALA n 
1 41  SER n 
1 42  ASP n 
1 43  GLN n 
1 44  ASN n 
1 45  LEU n 
1 46  PHE n 
1 47  GLN n 
1 48  THR n 
1 49  PHE n 
1 50  ILE n 
1 51  LYS n 
1 52  GLU n 
1 53  TRP n 
1 54  ARG n 
1 55  CYS n 
1 56  LYS n 
1 57  LYS n 
1 58  ARG n 
1 59  PHE n 
1 60  SER n 
1 61  ILE n 
1 62  SER n 
1 63  LEU n 
1 64  ALA n 
1 65  CYS n 
1 66  GLU n 
1 67  LYS n 
1 68  ILE n 
1 69  ARG n 
1 70  SER n 
1 71  LEU n 
1 72  THR n 
1 73  SER n 
1 74  SER n 
1 75  LYS n 
1 76  THR n 
1 77  ALA n 
1 78  THR n 
1 79  ILE n 
1 80  GLY n 
1 81  SER n 
1 82  ARG n 
1 83  PHE n 
1 84  LYS n 
1 85  GLN n 
1 86  ALA n 
1 87  SER n 
1 88  SER n 
1 89  PRO n 
1 90  GLN n 
1 91  GLU n 
1 92  ILE n 
1 93  PRO n 
1 94  ILE n 
1 95  ARG n 
1 96  ASP n 
1 97  ASP n 
1 98  GLY n 
1 99  PHE n 
1 100 PRO n 
1 101 ILE n 
1 102 LYS n 
1 103 GLY n 
1 104 CYS n 
1 105 ASP n 
1 106 ASP n 
1 107 THR n 
1 108 LEU n 
1 109 VAL n 
1 110 VAL n 
1 111 GLY n 
1 112 LEU n 
1 113 ALA n 
1 114 VAL n 
1 115 CYS n 
1 116 TRP n 
1 117 GLY n 
1 118 GLY n 
1 119 ARG n 
1 120 ASP n 
1 121 ALA n 
1 122 TYR n 
1 123 TYR n 
1 124 PHE n 
1 125 SER n 
1 126 LEU n 
1 127 GLN n 
1 128 LYS n 
1 129 GLU n 
1 130 GLN n 
1 131 LYS n 
1 132 HIS n 
1 133 SER n 
1 134 GLU n 
1 135 ILE n 
1 136 SER n 
1 137 ALA n 
1 138 SER n 
1 139 LEU n 
1 140 VAL n 
1 141 PRO n 
1 142 PRO n 
1 143 SER n 
1 144 LEU n 
1 145 ASP n 
1 146 PRO n 
1 147 SER n 
1 148 LEU n 
1 149 THR n 
1 150 LEU n 
1 151 LYS n 
1 152 ASP n 
1 153 ARG n 
1 154 MET n 
1 155 TRP n 
1 156 TYR n 
1 157 LEU n 
1 158 GLN n 
1 159 SER n 
1 160 CYS n 
1 161 LEU n 
1 162 ARG n 
1 163 LYS n 
1 164 GLU n 
1 165 SER n 
1 166 ASP n 
1 167 LYS n 
1 168 GLU n 
1 169 CYS n 
1 170 SER n 
1 171 VAL n 
1 172 VAL n 
1 173 ILE n 
1 174 TYR n 
1 175 ASP n 
1 176 PHE n 
1 177 ILE n 
1 178 GLN n 
1 179 SER n 
1 180 TYR n 
1 181 LYS n 
1 182 ILE n 
1 183 LEU n 
1 184 LEU n 
1 185 LEU n 
1 186 SER n 
1 187 CYS n 
1 188 GLY n 
1 189 ILE n 
1 190 SER n 
1 191 LEU n 
1 192 GLU n 
1 193 GLN n 
1 194 SER n 
1 195 TYR n 
1 196 GLU n 
1 197 ASP n 
1 198 PRO n 
1 199 LYS n 
1 200 VAL n 
1 201 ALA n 
1 202 CYS n 
1 203 TRP n 
1 204 LEU n 
1 205 LEU n 
1 206 ASP n 
1 207 PRO n 
1 208 ASP n 
1 209 SER n 
1 210 GLN n 
1 211 GLU n 
1 212 PRO n 
1 213 THR n 
1 214 LEU n 
1 215 HIS n 
1 216 SER n 
1 217 ILE n 
1 218 VAL n 
1 219 THR n 
1 220 SER n 
1 221 PHE n 
1 222 LEU n 
1 223 PRO n 
1 224 HIS n 
1 225 GLU n 
1 226 LEU n 
1 227 PRO n 
1 228 LEU n 
1 229 LEU n 
1 230 GLU n 
1 231 GLY n 
1 232 MET n 
1 233 GLU n 
1 234 THR n 
1 235 SER n 
1 236 GLN n 
1 237 GLY n 
1 238 ILE n 
1 239 GLN n 
1 240 SER n 
1 241 LEU n 
1 242 GLY n 
1 243 LEU n 
1 244 ASN n 
1 245 ALA n 
1 246 GLY n 
1 247 SER n 
1 248 GLU n 
1 249 HIS n 
1 250 SER n 
1 251 GLY n 
1 252 ARG n 
1 253 TYR n 
1 254 ARG n 
1 255 ALA n 
1 256 SER n 
1 257 VAL n 
1 258 GLU n 
1 259 SER n 
1 260 ILE n 
1 261 LEU n 
1 262 ILE n 
1 263 PHE n 
1 264 ASN n 
1 265 SER n 
1 266 MET n 
1 267 ASN n 
1 268 GLN n 
1 269 LEU n 
1 270 ASN n 
1 271 SER n 
1 272 LEU n 
1 273 LEU n 
1 274 GLN n 
1 275 LYS n 
1 276 GLU n 
1 277 ASN n 
1 278 LEU n 
1 279 GLN n 
1 280 ASP n 
1 281 VAL n 
1 282 PHE n 
1 283 ARG n 
1 284 LYS n 
1 285 VAL n 
1 286 GLU n 
1 287 MET n 
1 288 PRO n 
1 289 SER n 
1 290 GLN n 
1 291 TYR n 
1 292 CYS n 
1 293 LEU n 
1 294 ALA n 
1 295 LEU n 
1 296 LEU n 
1 297 GLU n 
1 298 LEU n 
1 299 ASN n 
1 300 GLY n 
1 301 ILE n 
1 302 GLY n 
1 303 PHE n 
1 304 SER n 
1 305 THR n 
1 306 ALA n 
1 307 GLU n 
1 308 CYS n 
1 309 GLU n 
1 310 SER n 
1 311 GLN n 
1 312 LYS n 
1 313 HIS n 
1 314 ILE n 
1 315 MET n 
1 316 GLN n 
1 317 ALA n 
1 318 LYS n 
1 319 LEU n 
1 320 ASP n 
1 321 ALA n 
1 322 ILE n 
1 323 GLU n 
1 324 THR n 
1 325 GLN n 
1 326 ALA n 
1 327 TYR n 
1 328 GLN n 
1 329 LEU n 
1 330 ALA n 
1 331 GLY n 
1 332 HIS n 
1 333 SER n 
1 334 PHE n 
1 335 SER n 
1 336 PHE n 
1 337 THR n 
1 338 SER n 
1 339 SER n 
1 340 ASP n 
1 341 ASP n 
1 342 ILE n 
1 343 ALA n 
1 344 GLU n 
1 345 VAL n 
1 346 LEU n 
1 347 PHE n 
1 348 LEU n 
1 349 GLU n 
1 350 LEU n 
1 351 LYS n 
1 352 LEU n 
1 353 PRO n 
1 354 PRO n 
1 355 ASN n 
1 356 ARG n 
1 357 GLU n 
1 358 MET n 
1 359 LYS n 
1 360 ASN n 
1 361 GLN n 
1 362 GLY n 
1 363 SER n 
1 364 LYS n 
1 365 LYS n 
1 366 THR n 
1 367 LEU n 
1 368 GLY n 
1 369 SER n 
1 370 THR n 
1 371 ARG n 
1 372 ARG n 
1 373 GLY n 
1 374 ILE n 
1 375 ASP n 
1 376 ASN n 
1 377 GLY n 
1 378 ARG n 
1 379 LYS n 
1 380 LEU n 
1 381 ARG n 
1 382 LEU n 
1 383 GLY n 
1 384 ARG n 
1 385 GLN n 
1 386 PHE n 
1 387 SER n 
1 388 THR n 
1 389 SER n 
1 390 LYS n 
1 391 ASP n 
1 392 VAL n 
1 393 LEU n 
1 394 ASN n 
1 395 LYS n 
1 396 LEU n 
1 397 LYS n 
1 398 ALA n 
1 399 LEU n 
1 400 HIS n 
1 401 PRO n 
1 402 LEU n 
1 403 PRO n 
1 404 GLY n 
1 405 LEU n 
1 406 ILE n 
1 407 LEU n 
1 408 GLU n 
1 409 TRP n 
1 410 ARG n 
1 411 ARG n 
1 412 ILE n 
1 413 THR n 
1 414 ASN n 
1 415 ALA n 
1 416 ILE n 
1 417 THR n 
1 418 LYS n 
1 419 VAL n 
1 420 VAL n 
1 421 PHE n 
1 422 PRO n 
1 423 LEU n 
1 424 GLN n 
1 425 ARG n 
1 426 GLU n 
1 427 LYS n 
1 428 CYS n 
1 429 LEU n 
1 430 ASN n 
1 431 PRO n 
1 432 PHE n 
1 433 LEU n 
1 434 GLY n 
1 435 MET n 
1 436 GLU n 
1 437 ARG n 
1 438 ILE n 
1 439 TYR n 
1 440 PRO n 
1 441 VAL n 
1 442 SER n 
1 443 GLN n 
1 444 SER n 
1 445 HIS n 
1 446 THR n 
1 447 ALA n 
1 448 THR n 
1 449 GLY n 
1 450 ARG n 
1 451 ILE n 
1 452 THR n 
1 453 PHE n 
1 454 THR n 
1 455 GLU n 
1 456 PRO n 
1 457 ASN n 
1 458 ILE n 
1 459 GLN n 
1 460 ASN n 
1 461 VAL n 
1 462 PRO n 
1 463 ARG n 
1 464 ASP n 
1 465 PHE n 
1 466 GLU n 
1 467 ILE n 
1 468 LYS n 
1 469 MET n 
1 470 PRO n 
1 471 THR n 
1 472 LEU n 
1 473 VAL n 
1 474 GLY n 
1 475 GLU n 
1 476 SER n 
1 477 PRO n 
1 478 PRO n 
1 479 SER n 
1 480 GLN n 
1 481 ALA n 
1 482 VAL n 
1 483 GLY n 
1 484 LYS n 
1 485 GLY n 
1 486 LEU n 
1 487 LEU n 
1 488 PRO n 
1 489 MET n 
1 490 GLY n 
1 491 ARG n 
1 492 GLY n 
1 493 LYS n 
1 494 TYR n 
1 495 LYS n 
1 496 LYS n 
1 497 GLY n 
1 498 PHE n 
1 499 SER n 
1 500 VAL n 
1 501 ASN n 
1 502 PRO n 
1 503 ARG n 
1 504 CYS n 
1 505 GLN n 
1 506 ALA n 
1 507 GLN n 
1 508 MET n 
1 509 GLU n 
1 510 GLU n 
1 511 ARG n 
1 512 ALA n 
1 513 ALA n 
1 514 ASP n 
1 515 ARG n 
1 516 GLY n 
1 517 MET n 
1 518 PRO n 
1 519 PHE n 
1 520 SER n 
1 521 ILE n 
1 522 SER n 
1 523 MET n 
1 524 ARG n 
1 525 HIS n 
1 526 ALA n 
1 527 PHE n 
1 528 VAL n 
1 529 PRO n 
1 530 PHE n 
1 531 PRO n 
1 532 GLY n 
1 533 GLY n 
1 534 SER n 
1 535 ILE n 
1 536 LEU n 
1 537 ALA n 
1 538 ALA n 
1 539 ASP n 
1 540 TYR n 
1 541 SER n 
1 542 GLN n 
1 543 LEU n 
1 544 GLU n 
1 545 LEU n 
1 546 ARG n 
1 547 ILE n 
1 548 LEU n 
1 549 ALA n 
1 550 HIS n 
1 551 LEU n 
1 552 SER n 
1 553 HIS n 
1 554 ASP n 
1 555 ARG n 
1 556 ARG n 
1 557 LEU n 
1 558 ILE n 
1 559 GLN n 
1 560 VAL n 
1 561 LEU n 
1 562 ASN n 
1 563 THR n 
1 564 GLY n 
1 565 ALA n 
1 566 ASP n 
1 567 VAL n 
1 568 PHE n 
1 569 ARG n 
1 570 SER n 
1 571 ILE n 
1 572 ALA n 
1 573 ALA n 
1 574 GLU n 
1 575 TRP n 
1 576 LYS n 
1 577 MET n 
1 578 ILE n 
1 579 GLU n 
1 580 PRO n 
1 581 GLU n 
1 582 SER n 
1 583 VAL n 
1 584 GLY n 
1 585 ASP n 
1 586 ASP n 
1 587 LEU n 
1 588 ARG n 
1 589 GLN n 
1 590 GLN n 
1 591 ALA n 
1 592 LYS n 
1 593 GLN n 
1 594 ILE n 
1 595 CYS n 
1 596 TYR n 
1 597 GLY n 
1 598 ILE n 
1 599 ILE n 
1 600 TYR n 
1 601 GLY n 
1 602 MET n 
1 603 GLY n 
1 604 ALA n 
1 605 LYS n 
1 606 SER n 
1 607 LEU n 
1 608 GLY n 
1 609 GLU n 
1 610 GLN n 
1 611 MET n 
1 612 GLY n 
1 613 ILE n 
1 614 LYS n 
1 615 GLU n 
1 616 ASN n 
1 617 ASP n 
1 618 ALA n 
1 619 ALA n 
1 620 CYS n 
1 621 TYR n 
1 622 ILE n 
1 623 ASP n 
1 624 SER n 
1 625 PHE n 
1 626 LYS n 
1 627 SER n 
1 628 ARG n 
1 629 TYR n 
1 630 THR n 
1 631 GLY n 
1 632 ILE n 
1 633 ASN n 
1 634 GLN n 
1 635 PHE n 
1 636 MET n 
1 637 THR n 
1 638 GLU n 
1 639 THR n 
1 640 VAL n 
1 641 LYS n 
1 642 ASN n 
1 643 CYS n 
1 644 LYS n 
1 645 ARG n 
1 646 ASP n 
1 647 GLY n 
1 648 PHE n 
1 649 VAL n 
1 650 GLN n 
1 651 THR n 
1 652 ILE n 
1 653 LEU n 
1 654 GLY n 
1 655 ARG n 
1 656 ARG n 
1 657 ARG n 
1 658 TYR n 
1 659 LEU n 
1 660 PRO n 
1 661 GLY n 
1 662 ILE n 
1 663 LYS n 
1 664 ASP n 
1 665 ASN n 
1 666 ASN n 
1 667 PRO n 
1 668 TYR n 
1 669 ARG n 
1 670 LYS n 
1 671 ALA n 
1 672 HIS n 
1 673 ALA n 
1 674 GLU n 
1 675 ARG n 
1 676 GLN n 
1 677 ALA n 
1 678 ILE n 
1 679 ASN n 
1 680 THR n 
1 681 ILE n 
1 682 VAL n 
1 683 GLN n 
1 684 GLY n 
1 685 SER n 
1 686 ALA n 
1 687 ALA n 
1 688 ASP n 
1 689 ILE n 
1 690 VAL n 
1 691 LYS n 
1 692 ILE n 
1 693 ALA n 
1 694 THR n 
1 695 VAL n 
1 696 ASN n 
1 697 ILE n 
1 698 GLN n 
1 699 LYS n 
1 700 GLN n 
1 701 LEU n 
1 702 GLU n 
1 703 THR n 
1 704 PHE n 
1 705 HIS n 
1 706 SER n 
1 707 THR n 
1 708 PHE n 
1 709 LYS n 
1 710 SER n 
1 711 HIS n 
1 712 GLY n 
1 713 HIS n 
1 714 ARG n 
1 715 GLU n 
1 716 GLY n 
1 717 MET n 
1 718 LEU n 
1 719 GLN n 
1 720 SER n 
1 721 ASP n 
1 722 GLN n 
1 723 THR n 
1 724 GLY n 
1 725 LEU n 
1 726 SER n 
1 727 ARG n 
1 728 LYS n 
1 729 ARG n 
1 730 LYS n 
1 731 LEU n 
1 732 GLN n 
1 733 GLY n 
1 734 MET n 
1 735 PHE n 
1 736 CYS n 
1 737 PRO n 
1 738 ILE n 
1 739 ARG n 
1 740 GLY n 
1 741 GLY n 
1 742 PHE n 
1 743 PHE n 
1 744 ILE n 
1 745 LEU n 
1 746 GLN n 
1 747 LEU n 
1 748 HIS n 
1 749 ASP n 
1 750 GLU n 
1 751 LEU n 
1 752 LEU n 
1 753 TYR n 
1 754 GLU n 
1 755 VAL n 
1 756 ALA n 
1 757 GLU n 
1 758 GLU n 
1 759 ASP n 
1 760 VAL n 
1 761 VAL n 
1 762 GLN n 
1 763 VAL n 
1 764 ALA n 
1 765 GLN n 
1 766 ILE n 
1 767 VAL n 
1 768 LYS n 
1 769 ASN n 
1 770 GLU n 
1 771 MET n 
1 772 GLU n 
1 773 SER n 
1 774 ALA n 
1 775 VAL n 
1 776 LYS n 
1 777 LEU n 
1 778 SER n 
1 779 VAL n 
1 780 LYS n 
1 781 LEU n 
1 782 LYS n 
1 783 VAL n 
1 784 LYS n 
1 785 VAL n 
1 786 LYS n 
1 787 ILE n 
1 788 GLY n 
1 789 ALA n 
1 790 SER n 
1 791 TRP n 
1 792 GLY n 
1 793 GLU n 
1 794 LEU n 
1 795 LYS n 
1 796 ASP n 
1 797 PHE n 
1 798 ASP n 
1 799 VAL n 
2 1   DG  n 
2 2   DC  n 
2 3   DA  n 
2 4   DG  n 
2 5   DT  n 
2 6   DC  n 
2 7   DA  n 
2 8   DG  n 
2 9   DC  n 
2 10  DT  n 
2 11  DC  n 
2 12  DT  n 
2 13  DA  n 
2 14  DC  n 
2 15  DG  n 
2 16  DG  n 
2 17  DA  n 
2 18  DT  n 
2 19  DG  n 
2 20  DC  n 
2 21  DC  n 
2 22  DT  n 
2 23  DC  n 
2 24  DA  n 
2 25  DC  n 
2 26  DA  n 
2 27  DG  n 
2 28  DC  n 
2 29  DA  n 
3 1   DT  n 
3 2   DG  n 
3 3   DC  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 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   799 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'POLQ, POLH' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
2 1 sample 1 29 'Homo sapiens' ? 9606 ? 
3 1 sample 1 20 'Homo sapiens' ? 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   GLY 1   1792 ?    ?   ?   A . n 
A 1 2   PHE 2   1793 ?    ?   ?   A . n 
A 1 3   LYS 3   1794 ?    ?   ?   A . n 
A 1 4   ASP 4   1795 ?    ?   ?   A . n 
A 1 5   ASN 5   1796 ?    ?   ?   A . n 
A 1 6   SER 6   1797 ?    ?   ?   A . n 
A 1 7   PRO 7   1798 ?    ?   ?   A . n 
A 1 8   ILE 8   1799 ?    ?   ?   A . n 
A 1 9   SER 9   1800 ?    ?   ?   A . n 
A 1 10  ASP 10  1801 ?    ?   ?   A . n 
A 1 11  THR 11  1802 ?    ?   ?   A . n 
A 1 12  SER 12  1803 ?    ?   ?   A . n 
A 1 13  PHE 13  1804 ?    ?   ?   A . n 
A 1 14  SER 14  1805 ?    ?   ?   A . n 
A 1 15  LEU 15  1806 ?    ?   ?   A . n 
A 1 16  GLN 16  1807 ?    ?   ?   A . n 
A 1 17  LEU 17  1808 ?    ?   ?   A . n 
A 1 18  SER 18  1809 ?    ?   ?   A . n 
A 1 19  GLN 19  1810 ?    ?   ?   A . n 
A 1 20  ASP 20  1811 ?    ?   ?   A . n 
A 1 21  GLY 21  1812 ?    ?   ?   A . n 
A 1 22  LEU 22  1813 ?    ?   ?   A . n 
A 1 23  GLN 23  1814 ?    ?   ?   A . n 
A 1 24  LEU 24  1815 ?    ?   ?   A . n 
A 1 25  THR 25  1816 ?    ?   ?   A . n 
A 1 26  PRO 26  1817 ?    ?   ?   A . n 
A 1 27  ALA 27  1818 ?    ?   ?   A . n 
A 1 28  SER 28  1819 ?    ?   ?   A . n 
A 1 29  SER 29  1820 ?    ?   ?   A . n 
A 1 30  SER 30  1821 ?    ?   ?   A . n 
A 1 31  SER 31  1822 ?    ?   ?   A . n 
A 1 32  GLU 32  1823 ?    ?   ?   A . n 
A 1 33  SER 33  1824 1824 SER SER A . n 
A 1 34  LEU 34  1825 1825 LEU LEU A . n 
A 1 35  SER 35  1826 1826 SER SER A . n 
A 1 36  ILE 36  1827 1827 ILE ILE A . n 
A 1 37  ILE 37  1828 1828 ILE ILE A . n 
A 1 38  ASP 38  1829 1829 ASP ASP A . n 
A 1 39  VAL 39  1830 1830 VAL VAL A . n 
A 1 40  ALA 40  1831 1831 ALA ALA A . n 
A 1 41  SER 41  1832 1832 SER SER A . n 
A 1 42  ASP 42  1833 1833 ASP ASP A . n 
A 1 43  GLN 43  1834 1834 GLN GLN A . n 
A 1 44  ASN 44  1835 1835 ASN ASN A . n 
A 1 45  LEU 45  1836 1836 LEU LEU A . n 
A 1 46  PHE 46  1837 1837 PHE PHE A . n 
A 1 47  GLN 47  1838 1838 GLN GLN A . n 
A 1 48  THR 48  1839 1839 THR THR A . n 
A 1 49  PHE 49  1840 1840 PHE PHE A . n 
A 1 50  ILE 50  1841 1841 ILE ILE A . n 
A 1 51  LYS 51  1842 1842 LYS LYS A . n 
A 1 52  GLU 52  1843 1843 GLU GLU A . n 
A 1 53  TRP 53  1844 1844 TRP TRP A . n 
A 1 54  ARG 54  1845 1845 ARG ARG A . n 
A 1 55  CYS 55  1846 1846 CYS CYS A . n 
A 1 56  LYS 56  1847 1847 LYS LYS A . n 
A 1 57  LYS 57  1848 1848 LYS LYS A . n 
A 1 58  ARG 58  1849 1849 ARG ARG A . n 
A 1 59  PHE 59  1850 1850 PHE PHE A . n 
A 1 60  SER 60  1851 1851 SER SER A . n 
A 1 61  ILE 61  1852 1852 ILE ILE A . n 
A 1 62  SER 62  1853 1853 SER SER A . n 
A 1 63  LEU 63  1854 1854 LEU LEU A . n 
A 1 64  ALA 64  1855 1855 ALA ALA A . n 
A 1 65  CYS 65  1856 1856 CYS CYS A . n 
A 1 66  GLU 66  1857 1857 GLU GLU A . n 
A 1 67  LYS 67  1858 1858 LYS LYS A . n 
A 1 68  ILE 68  1859 1859 ILE ILE A . n 
A 1 69  ARG 69  1860 1860 ARG ARG A . n 
A 1 70  SER 70  1861 1861 SER SER A . n 
A 1 71  LEU 71  1862 ?    ?   ?   A . n 
A 1 72  THR 72  1863 ?    ?   ?   A . n 
A 1 73  SER 73  1864 ?    ?   ?   A . n 
A 1 74  SER 74  1865 ?    ?   ?   A . n 
A 1 75  LYS 75  1866 ?    ?   ?   A . n 
A 1 76  THR 76  1867 ?    ?   ?   A . n 
A 1 77  ALA 77  1868 ?    ?   ?   A . n 
A 1 78  THR 78  1869 ?    ?   ?   A . n 
A 1 79  ILE 79  1870 ?    ?   ?   A . n 
A 1 80  GLY 80  1871 ?    ?   ?   A . n 
A 1 81  SER 81  1872 ?    ?   ?   A . n 
A 1 82  ARG 82  1873 ?    ?   ?   A . n 
A 1 83  PHE 83  1874 ?    ?   ?   A . n 
A 1 84  LYS 84  1875 ?    ?   ?   A . n 
A 1 85  GLN 85  1876 ?    ?   ?   A . n 
A 1 86  ALA 86  1877 ?    ?   ?   A . n 
A 1 87  SER 87  1878 ?    ?   ?   A . n 
A 1 88  SER 88  1879 ?    ?   ?   A . n 
A 1 89  PRO 89  1880 ?    ?   ?   A . n 
A 1 90  GLN 90  1881 ?    ?   ?   A . n 
A 1 91  GLU 91  1882 ?    ?   ?   A . n 
A 1 92  ILE 92  1883 ?    ?   ?   A . n 
A 1 93  PRO 93  1884 ?    ?   ?   A . n 
A 1 94  ILE 94  1885 1885 ILE ILE A . n 
A 1 95  ARG 95  1886 1886 ARG ARG A . n 
A 1 96  ASP 96  1887 1887 ASP ASP A . n 
A 1 97  ASP 97  1888 1888 ASP ASP A . n 
A 1 98  GLY 98  1889 1889 GLY GLY A . n 
A 1 99  PHE 99  1890 1890 PHE PHE A . n 
A 1 100 PRO 100 1891 1891 PRO PRO A . n 
A 1 101 ILE 101 1892 1892 ILE ILE A . n 
A 1 102 LYS 102 1893 1893 LYS LYS A . n 
A 1 103 GLY 103 1894 1894 GLY GLY A . n 
A 1 104 CYS 104 1895 1895 CYS CYS A . n 
A 1 105 ASP 105 1896 1896 ASP ASP A . n 
A 1 106 ASP 106 1897 1897 ASP ASP A . n 
A 1 107 THR 107 1898 1898 THR THR A . n 
A 1 108 LEU 108 1899 1899 LEU LEU A . n 
A 1 109 VAL 109 1900 1900 VAL VAL A . n 
A 1 110 VAL 110 1901 1901 VAL VAL A . n 
A 1 111 GLY 111 1902 1902 GLY GLY A . n 
A 1 112 LEU 112 1903 1903 LEU LEU A . n 
A 1 113 ALA 113 1904 1904 ALA ALA A . n 
A 1 114 VAL 114 1905 1905 VAL VAL A . n 
A 1 115 CYS 115 1906 1906 CYS CYS A . n 
A 1 116 TRP 116 1907 1907 TRP TRP A . n 
A 1 117 GLY 117 1908 1908 GLY GLY A . n 
A 1 118 GLY 118 1909 1909 GLY GLY A . n 
A 1 119 ARG 119 1910 1910 ARG ARG A . n 
A 1 120 ASP 120 1911 1911 ASP ASP A . n 
A 1 121 ALA 121 1912 1912 ALA ALA A . n 
A 1 122 TYR 122 1913 1913 TYR TYR A . n 
A 1 123 TYR 123 1914 1914 TYR TYR A . n 
A 1 124 PHE 124 1915 1915 PHE PHE A . n 
A 1 125 SER 125 1916 1916 SER SER A . n 
A 1 126 LEU 126 1917 1917 LEU LEU A . n 
A 1 127 GLN 127 1918 1918 GLN GLN A . n 
A 1 128 LYS 128 1919 1919 LYS LYS A . n 
A 1 129 GLU 129 1920 1920 GLU GLU A . n 
A 1 130 GLN 130 1921 ?    ?   ?   A . n 
A 1 131 LYS 131 1922 ?    ?   ?   A . n 
A 1 132 HIS 132 1923 ?    ?   ?   A . n 
A 1 133 SER 133 1924 ?    ?   ?   A . n 
A 1 134 GLU 134 1925 ?    ?   ?   A . n 
A 1 135 ILE 135 1926 ?    ?   ?   A . n 
A 1 136 SER 136 1927 ?    ?   ?   A . n 
A 1 137 ALA 137 1928 ?    ?   ?   A . n 
A 1 138 SER 138 1929 ?    ?   ?   A . n 
A 1 139 LEU 139 1930 ?    ?   ?   A . n 
A 1 140 VAL 140 1931 ?    ?   ?   A . n 
A 1 141 PRO 141 1932 ?    ?   ?   A . n 
A 1 142 PRO 142 1933 ?    ?   ?   A . n 
A 1 143 SER 143 1934 ?    ?   ?   A . n 
A 1 144 LEU 144 1935 ?    ?   ?   A . n 
A 1 145 ASP 145 1936 1936 ASP ASP A . n 
A 1 146 PRO 146 1937 1937 PRO PRO A . n 
A 1 147 SER 147 1938 1938 SER SER A . n 
A 1 148 LEU 148 1939 1939 LEU LEU A . n 
A 1 149 THR 149 1940 1940 THR THR A . n 
A 1 150 LEU 150 1941 1941 LEU LEU A . n 
A 1 151 LYS 151 1942 1942 LYS LYS A . n 
A 1 152 ASP 152 1943 1943 ASP ASP A . n 
A 1 153 ARG 153 1944 1944 ARG ARG A . n 
A 1 154 MET 154 1945 1945 MET MET A . n 
A 1 155 TRP 155 1946 1946 TRP TRP A . n 
A 1 156 TYR 156 1947 1947 TYR TYR A . n 
A 1 157 LEU 157 1948 1948 LEU LEU A . n 
A 1 158 GLN 158 1949 1949 GLN GLN A . n 
A 1 159 SER 159 1950 1950 SER SER A . n 
A 1 160 CYS 160 1951 1951 CYS CYS A . n 
A 1 161 LEU 161 1952 1952 LEU LEU A . n 
A 1 162 ARG 162 1953 1953 ARG ARG A . n 
A 1 163 LYS 163 1954 1954 LYS LYS A . n 
A 1 164 GLU 164 1955 1955 GLU GLU A . n 
A 1 165 SER 165 1956 1956 SER SER A . n 
A 1 166 ASP 166 1957 1957 ASP ASP A . n 
A 1 167 LYS 167 1958 1958 LYS LYS A . n 
A 1 168 GLU 168 1959 1959 GLU GLU A . n 
A 1 169 CYS 169 1960 1960 CYS CYS A . n 
A 1 170 SER 170 1961 1961 SER SER A . n 
A 1 171 VAL 171 1962 1962 VAL VAL A . n 
A 1 172 VAL 172 1963 1963 VAL VAL A . n 
A 1 173 ILE 173 1964 1964 ILE ILE A . n 
A 1 174 TYR 174 1965 1965 TYR TYR A . n 
A 1 175 ASP 175 1966 1966 ASP ASP A . n 
A 1 176 PHE 176 1967 1967 PHE PHE A . n 
A 1 177 ILE 177 1968 1968 ILE ILE A . n 
A 1 178 GLN 178 1969 1969 GLN GLN A . n 
A 1 179 SER 179 1970 1970 SER SER A . n 
A 1 180 TYR 180 1971 1971 TYR TYR A . n 
A 1 181 LYS 181 1972 1972 LYS LYS A . n 
A 1 182 ILE 182 1973 1973 ILE ILE A . n 
A 1 183 LEU 183 1974 1974 LEU LEU A . n 
A 1 184 LEU 184 1975 1975 LEU LEU A . n 
A 1 185 LEU 185 1976 1976 LEU LEU A . n 
A 1 186 SER 186 1977 1977 SER SER A . n 
A 1 187 CYS 187 1978 1978 CYS CYS A . n 
A 1 188 GLY 188 1979 1979 GLY GLY A . n 
A 1 189 ILE 189 1980 1980 ILE ILE A . n 
A 1 190 SER 190 1981 1981 SER SER A . n 
A 1 191 LEU 191 1982 1982 LEU LEU A . n 
A 1 192 GLU 192 1983 1983 GLU GLU A . n 
A 1 193 GLN 193 1984 1984 GLN GLN A . n 
A 1 194 SER 194 1985 1985 SER SER A . n 
A 1 195 TYR 195 1986 1986 TYR TYR A . n 
A 1 196 GLU 196 1987 1987 GLU GLU A . n 
A 1 197 ASP 197 1988 1988 ASP ASP A . n 
A 1 198 PRO 198 1989 1989 PRO PRO A . n 
A 1 199 LYS 199 1990 1990 LYS LYS A . n 
A 1 200 VAL 200 1991 1991 VAL VAL A . n 
A 1 201 ALA 201 1992 1992 ALA ALA A . n 
A 1 202 CYS 202 1993 1993 CYS CYS A . n 
A 1 203 TRP 203 1994 1994 TRP TRP A . n 
A 1 204 LEU 204 1995 1995 LEU LEU A . n 
A 1 205 LEU 205 1996 1996 LEU LEU A . n 
A 1 206 ASP 206 1997 1997 ASP ASP A . n 
A 1 207 PRO 207 1998 1998 PRO PRO A . n 
A 1 208 ASP 208 1999 1999 ASP ASP A . n 
A 1 209 SER 209 2000 2000 SER SER A . n 
A 1 210 GLN 210 2001 2001 GLN GLN A . n 
A 1 211 GLU 211 2002 2002 GLU GLU A . n 
A 1 212 PRO 212 2003 2003 PRO PRO A . n 
A 1 213 THR 213 2004 2004 THR THR A . n 
A 1 214 LEU 214 2005 2005 LEU LEU A . n 
A 1 215 HIS 215 2006 2006 HIS HIS A . n 
A 1 216 SER 216 2007 2007 SER SER A . n 
A 1 217 ILE 217 2008 2008 ILE ILE A . n 
A 1 218 VAL 218 2009 2009 VAL VAL A . n 
A 1 219 THR 219 2010 2010 THR THR A . n 
A 1 220 SER 220 2011 2011 SER SER A . n 
A 1 221 PHE 221 2012 2012 PHE PHE A . n 
A 1 222 LEU 222 2013 2013 LEU LEU A . n 
A 1 223 PRO 223 2014 2014 PRO PRO A . n 
A 1 224 HIS 224 2015 2015 HIS HIS A . n 
A 1 225 GLU 225 2016 2016 GLU GLU A . n 
A 1 226 LEU 226 2017 2017 LEU LEU A . n 
A 1 227 PRO 227 2018 2018 PRO PRO A . n 
A 1 228 LEU 228 2019 2019 LEU LEU A . n 
A 1 229 LEU 229 2020 2020 LEU LEU A . n 
A 1 230 GLU 230 2021 2021 GLU GLU A . n 
A 1 231 GLY 231 2022 2022 GLY GLY A . n 
A 1 232 MET 232 2023 2023 MET MET A . n 
A 1 233 GLU 233 2024 2024 GLU GLU A . n 
A 1 234 THR 234 2025 2025 THR THR A . n 
A 1 235 SER 235 2026 2026 SER SER A . n 
A 1 236 GLN 236 2027 2027 GLN GLN A . n 
A 1 237 GLY 237 2028 2028 GLY GLY A . n 
A 1 238 ILE 238 2029 2029 ILE ILE A . n 
A 1 239 GLN 239 2030 2030 GLN GLN A . n 
A 1 240 SER 240 2031 2031 SER SER A . n 
A 1 241 LEU 241 2032 2032 LEU LEU A . n 
A 1 242 GLY 242 2033 2033 GLY GLY A . n 
A 1 243 LEU 243 2034 2034 LEU LEU A . n 
A 1 244 ASN 244 2035 2035 ASN ASN A . n 
A 1 245 ALA 245 2036 2036 ALA ALA A . n 
A 1 246 GLY 246 2037 2037 GLY GLY A . n 
A 1 247 SER 247 2038 2038 SER SER A . n 
A 1 248 GLU 248 2039 2039 GLU GLU A . n 
A 1 249 HIS 249 2040 2040 HIS HIS A . n 
A 1 250 SER 250 2041 2041 SER SER A . n 
A 1 251 GLY 251 2042 2042 GLY GLY A . n 
A 1 252 ARG 252 2043 2043 ARG ARG A . n 
A 1 253 TYR 253 2044 2044 TYR TYR A . n 
A 1 254 ARG 254 2045 2045 ARG ARG A . n 
A 1 255 ALA 255 2046 2046 ALA ALA A . n 
A 1 256 SER 256 2047 2047 SER SER A . n 
A 1 257 VAL 257 2048 2048 VAL VAL A . n 
A 1 258 GLU 258 2049 2049 GLU GLU A . n 
A 1 259 SER 259 2050 2050 SER SER A . n 
A 1 260 ILE 260 2051 2051 ILE ILE A . n 
A 1 261 LEU 261 2052 2052 LEU LEU A . n 
A 1 262 ILE 262 2053 2053 ILE ILE A . n 
A 1 263 PHE 263 2054 2054 PHE PHE A . n 
A 1 264 ASN 264 2055 2055 ASN ASN A . n 
A 1 265 SER 265 2056 2056 SER SER A . n 
A 1 266 MET 266 2057 2057 MET MET A . n 
A 1 267 ASN 267 2058 2058 ASN ASN A . n 
A 1 268 GLN 268 2059 2059 GLN GLN A . n 
A 1 269 LEU 269 2060 2060 LEU LEU A . n 
A 1 270 ASN 270 2061 2061 ASN ASN A . n 
A 1 271 SER 271 2062 2062 SER SER A . n 
A 1 272 LEU 272 2063 2063 LEU LEU A . n 
A 1 273 LEU 273 2064 2064 LEU LEU A . n 
A 1 274 GLN 274 2065 2065 GLN GLN A . n 
A 1 275 LYS 275 2066 2066 LYS LYS A . n 
A 1 276 GLU 276 2067 2067 GLU GLU A . n 
A 1 277 ASN 277 2068 2068 ASN ASN A . n 
A 1 278 LEU 278 2069 2069 LEU LEU A . n 
A 1 279 GLN 279 2070 2070 GLN GLN A . n 
A 1 280 ASP 280 2071 2071 ASP ASP A . n 
A 1 281 VAL 281 2072 2072 VAL VAL A . n 
A 1 282 PHE 282 2073 2073 PHE PHE A . n 
A 1 283 ARG 283 2074 2074 ARG ARG A . n 
A 1 284 LYS 284 2075 2075 LYS LYS A . n 
A 1 285 VAL 285 2076 2076 VAL VAL A . n 
A 1 286 GLU 286 2077 2077 GLU GLU A . n 
A 1 287 MET 287 2078 2078 MET MET A . n 
A 1 288 PRO 288 2079 2079 PRO PRO A . n 
A 1 289 SER 289 2080 2080 SER SER A . n 
A 1 290 GLN 290 2081 2081 GLN GLN A . n 
A 1 291 TYR 291 2082 2082 TYR TYR A . n 
A 1 292 CYS 292 2083 2083 CYS CYS A . n 
A 1 293 LEU 293 2084 2084 LEU LEU A . n 
A 1 294 ALA 294 2085 2085 ALA ALA A . n 
A 1 295 LEU 295 2086 2086 LEU LEU A . n 
A 1 296 LEU 296 2087 2087 LEU LEU A . n 
A 1 297 GLU 297 2088 2088 GLU GLU A . n 
A 1 298 LEU 298 2089 2089 LEU LEU A . n 
A 1 299 ASN 299 2090 2090 ASN ASN A . n 
A 1 300 GLY 300 2091 2091 GLY GLY A . n 
A 1 301 ILE 301 2092 2092 ILE ILE A . n 
A 1 302 GLY 302 2093 2093 GLY GLY A . n 
A 1 303 PHE 303 2094 2094 PHE PHE A . n 
A 1 304 SER 304 2095 2095 SER SER A . n 
A 1 305 THR 305 2096 2096 THR THR A . n 
A 1 306 ALA 306 2097 2097 ALA ALA A . n 
A 1 307 GLU 307 2098 2098 GLU GLU A . n 
A 1 308 CYS 308 2099 2099 CYS CYS A . n 
A 1 309 GLU 309 2100 2100 GLU GLU A . n 
A 1 310 SER 310 2101 2101 SER SER A . n 
A 1 311 GLN 311 2102 2102 GLN GLN A . n 
A 1 312 LYS 312 2103 2103 LYS LYS A . n 
A 1 313 HIS 313 2104 2104 HIS HIS A . n 
A 1 314 ILE 314 2105 2105 ILE ILE A . n 
A 1 315 MET 315 2106 2106 MET MET A . n 
A 1 316 GLN 316 2107 2107 GLN GLN A . n 
A 1 317 ALA 317 2108 2108 ALA ALA A . n 
A 1 318 LYS 318 2109 2109 LYS LYS A . n 
A 1 319 LEU 319 2110 2110 LEU LEU A . n 
A 1 320 ASP 320 2111 2111 ASP ASP A . n 
A 1 321 ALA 321 2112 2112 ALA ALA A . n 
A 1 322 ILE 322 2113 2113 ILE ILE A . n 
A 1 323 GLU 323 2114 2114 GLU GLU A . n 
A 1 324 THR 324 2115 2115 THR THR A . n 
A 1 325 GLN 325 2116 2116 GLN GLN A . n 
A 1 326 ALA 326 2117 2117 ALA ALA A . n 
A 1 327 TYR 327 2118 2118 TYR TYR A . n 
A 1 328 GLN 328 2119 2119 GLN GLN A . n 
A 1 329 LEU 329 2120 2120 LEU LEU A . n 
A 1 330 ALA 330 2121 2121 ALA ALA A . n 
A 1 331 GLY 331 2122 2122 GLY GLY A . n 
A 1 332 HIS 332 2123 2123 HIS HIS A . n 
A 1 333 SER 333 2124 2124 SER SER A . n 
A 1 334 PHE 334 2125 2125 PHE PHE A . n 
A 1 335 SER 335 2126 2126 SER SER A . n 
A 1 336 PHE 336 2127 2127 PHE PHE A . n 
A 1 337 THR 337 2128 2128 THR THR A . n 
A 1 338 SER 338 2129 2129 SER SER A . n 
A 1 339 SER 339 2130 2130 SER SER A . n 
A 1 340 ASP 340 2131 2131 ASP ASP A . n 
A 1 341 ASP 341 2132 2132 ASP ASP A . n 
A 1 342 ILE 342 2133 2133 ILE ILE A . n 
A 1 343 ALA 343 2134 2134 ALA ALA A . n 
A 1 344 GLU 344 2135 2135 GLU GLU A . n 
A 1 345 VAL 345 2136 2136 VAL VAL A . n 
A 1 346 LEU 346 2137 2137 LEU LEU A . n 
A 1 347 PHE 347 2138 2138 PHE PHE A . n 
A 1 348 LEU 348 2139 2139 LEU LEU A . n 
A 1 349 GLU 349 2140 2140 GLU GLU A . n 
A 1 350 LEU 350 2141 2141 LEU LEU A . n 
A 1 351 LYS 351 2142 2142 LYS LYS A . n 
A 1 352 LEU 352 2143 2143 LEU LEU A . n 
A 1 353 PRO 353 2144 2144 PRO PRO A . n 
A 1 354 PRO 354 2145 2145 PRO PRO A . n 
A 1 355 ASN 355 2146 2146 ASN ASN A . n 
A 1 356 ARG 356 2147 2147 ARG ARG A . n 
A 1 357 GLU 357 2148 ?    ?   ?   A . n 
A 1 358 MET 358 2149 ?    ?   ?   A . n 
A 1 359 LYS 359 2150 ?    ?   ?   A . n 
A 1 360 ASN 360 2151 ?    ?   ?   A . n 
A 1 361 GLN 361 2152 ?    ?   ?   A . n 
A 1 362 GLY 362 2153 ?    ?   ?   A . n 
A 1 363 SER 363 2154 ?    ?   ?   A . n 
A 1 364 LYS 364 2155 ?    ?   ?   A . n 
A 1 365 LYS 365 2156 ?    ?   ?   A . n 
A 1 366 THR 366 2157 ?    ?   ?   A . n 
A 1 367 LEU 367 2158 ?    ?   ?   A . n 
A 1 368 GLY 368 2159 ?    ?   ?   A . n 
A 1 369 SER 369 2160 ?    ?   ?   A . n 
A 1 370 THR 370 2161 ?    ?   ?   A . n 
A 1 371 ARG 371 2162 ?    ?   ?   A . n 
A 1 372 ARG 372 2163 ?    ?   ?   A . n 
A 1 373 GLY 373 2164 ?    ?   ?   A . n 
A 1 374 ILE 374 2165 ?    ?   ?   A . n 
A 1 375 ASP 375 2166 ?    ?   ?   A . n 
A 1 376 ASN 376 2167 ?    ?   ?   A . n 
A 1 377 GLY 377 2168 ?    ?   ?   A . n 
A 1 378 ARG 378 2169 ?    ?   ?   A . n 
A 1 379 LYS 379 2170 ?    ?   ?   A . n 
A 1 380 LEU 380 2171 ?    ?   ?   A . n 
A 1 381 ARG 381 2172 ?    ?   ?   A . n 
A 1 382 LEU 382 2173 ?    ?   ?   A . n 
A 1 383 GLY 383 2174 2174 GLY GLY A . n 
A 1 384 ARG 384 2175 2175 ARG ARG A . n 
A 1 385 GLN 385 2176 2176 GLN GLN A . n 
A 1 386 PHE 386 2177 2177 PHE PHE A . n 
A 1 387 SER 387 2178 2178 SER SER A . n 
A 1 388 THR 388 2179 2179 THR THR A . n 
A 1 389 SER 389 2180 2180 SER SER A . n 
A 1 390 LYS 390 2181 2181 LYS LYS A . n 
A 1 391 ASP 391 2182 2182 ASP ASP A . n 
A 1 392 VAL 392 2183 2183 VAL VAL A . n 
A 1 393 LEU 393 2184 2184 LEU LEU A . n 
A 1 394 ASN 394 2185 2185 ASN ASN A . n 
A 1 395 LYS 395 2186 2186 LYS LYS A . n 
A 1 396 LEU 396 2187 2187 LEU LEU A . n 
A 1 397 LYS 397 2188 2188 LYS LYS A . n 
A 1 398 ALA 398 2189 2189 ALA ALA A . n 
A 1 399 LEU 399 2190 2190 LEU LEU A . n 
A 1 400 HIS 400 2191 2191 HIS HIS A . n 
A 1 401 PRO 401 2192 2192 PRO PRO A . n 
A 1 402 LEU 402 2193 2193 LEU LEU A . n 
A 1 403 PRO 403 2194 2194 PRO PRO A . n 
A 1 404 GLY 404 2195 2195 GLY GLY A . n 
A 1 405 LEU 405 2196 2196 LEU LEU A . n 
A 1 406 ILE 406 2197 2197 ILE ILE A . n 
A 1 407 LEU 407 2198 2198 LEU LEU A . n 
A 1 408 GLU 408 2199 2199 GLU GLU A . n 
A 1 409 TRP 409 2200 2200 TRP TRP A . n 
A 1 410 ARG 410 2201 2201 ARG ARG A . n 
A 1 411 ARG 411 2202 2202 ARG ARG A . n 
A 1 412 ILE 412 2203 2203 ILE ILE A . n 
A 1 413 THR 413 2204 2204 THR THR A . n 
A 1 414 ASN 414 2205 2205 ASN ASN A . n 
A 1 415 ALA 415 2206 2206 ALA ALA A . n 
A 1 416 ILE 416 2207 2207 ILE ILE A . n 
A 1 417 THR 417 2208 2208 THR THR A . n 
A 1 418 LYS 418 2209 2209 LYS LYS A . n 
A 1 419 VAL 419 2210 2210 VAL VAL A . n 
A 1 420 VAL 420 2211 2211 VAL VAL A . n 
A 1 421 PHE 421 2212 2212 PHE PHE A . n 
A 1 422 PRO 422 2213 2213 PRO PRO A . n 
A 1 423 LEU 423 2214 2214 LEU LEU A . n 
A 1 424 GLN 424 2215 2215 GLN GLN A . n 
A 1 425 ARG 425 2216 2216 ARG ARG A . n 
A 1 426 GLU 426 2217 2217 GLU GLU A . n 
A 1 427 LYS 427 2218 2218 LYS LYS A . n 
A 1 428 CYS 428 2219 2219 CYS CYS A . n 
A 1 429 LEU 429 2220 2220 LEU LEU A . n 
A 1 430 ASN 430 2221 2221 ASN ASN A . n 
A 1 431 PRO 431 2222 2222 PRO PRO A . n 
A 1 432 PHE 432 2223 2223 PHE PHE A . n 
A 1 433 LEU 433 2224 2224 LEU LEU A . n 
A 1 434 GLY 434 2225 2225 GLY GLY A . n 
A 1 435 MET 435 2226 2226 MET MET A . n 
A 1 436 GLU 436 2227 2227 GLU GLU A . n 
A 1 437 ARG 437 2228 2228 ARG ARG A . n 
A 1 438 ILE 438 2229 2229 ILE ILE A . n 
A 1 439 TYR 439 2230 2230 TYR TYR A . n 
A 1 440 PRO 440 2231 2231 PRO PRO A . n 
A 1 441 VAL 441 2232 2232 VAL VAL A . n 
A 1 442 SER 442 2233 2233 SER SER A . n 
A 1 443 GLN 443 2234 2234 GLN GLN A . n 
A 1 444 SER 444 2235 2235 SER SER A . n 
A 1 445 HIS 445 2236 2236 HIS HIS A . n 
A 1 446 THR 446 2237 2237 THR THR A . n 
A 1 447 ALA 447 2238 2238 ALA ALA A . n 
A 1 448 THR 448 2239 2239 THR THR A . n 
A 1 449 GLY 449 2240 2240 GLY GLY A . n 
A 1 450 ARG 450 2241 2241 ARG ARG A . n 
A 1 451 ILE 451 2242 2242 ILE ILE A . n 
A 1 452 THR 452 2243 2243 THR THR A . n 
A 1 453 PHE 453 2244 2244 PHE PHE A . n 
A 1 454 THR 454 2245 2245 THR THR A . n 
A 1 455 GLU 455 2246 2246 GLU GLU A . n 
A 1 456 PRO 456 2247 2247 PRO PRO A . n 
A 1 457 ASN 457 2248 2248 ASN ASN A . n 
A 1 458 ILE 458 2249 2249 ILE ILE A . n 
A 1 459 GLN 459 2250 2250 GLN GLN A . n 
A 1 460 ASN 460 2251 2251 ASN ASN A . n 
A 1 461 VAL 461 2252 2252 VAL VAL A . n 
A 1 462 PRO 462 2253 2253 PRO PRO A . n 
A 1 463 ARG 463 2254 2254 ARG ARG A . n 
A 1 464 ASP 464 2255 2255 ASP ASP A . n 
A 1 465 PHE 465 2256 2256 PHE PHE A . n 
A 1 466 GLU 466 2257 2257 GLU GLU A . n 
A 1 467 ILE 467 2258 2258 ILE ILE A . n 
A 1 468 LYS 468 2259 2259 LYS LYS A . n 
A 1 469 MET 469 2260 2260 MET MET A . n 
A 1 470 PRO 470 2261 2261 PRO PRO A . n 
A 1 471 THR 471 2262 2262 THR THR A . n 
A 1 472 LEU 472 2263 ?    ?   ?   A . n 
A 1 473 VAL 473 2264 ?    ?   ?   A . n 
A 1 474 GLY 474 2265 ?    ?   ?   A . n 
A 1 475 GLU 475 2266 ?    ?   ?   A . n 
A 1 476 SER 476 2267 ?    ?   ?   A . n 
A 1 477 PRO 477 2268 ?    ?   ?   A . n 
A 1 478 PRO 478 2269 ?    ?   ?   A . n 
A 1 479 SER 479 2270 ?    ?   ?   A . n 
A 1 480 GLN 480 2271 ?    ?   ?   A . n 
A 1 481 ALA 481 2272 ?    ?   ?   A . n 
A 1 482 VAL 482 2273 ?    ?   ?   A . n 
A 1 483 GLY 483 2274 ?    ?   ?   A . n 
A 1 484 LYS 484 2275 ?    ?   ?   A . n 
A 1 485 GLY 485 2276 ?    ?   ?   A . n 
A 1 486 LEU 486 2277 ?    ?   ?   A . n 
A 1 487 LEU 487 2278 ?    ?   ?   A . n 
A 1 488 PRO 488 2279 ?    ?   ?   A . n 
A 1 489 MET 489 2280 ?    ?   ?   A . n 
A 1 490 GLY 490 2281 ?    ?   ?   A . n 
A 1 491 ARG 491 2282 ?    ?   ?   A . n 
A 1 492 GLY 492 2283 ?    ?   ?   A . n 
A 1 493 LYS 493 2284 ?    ?   ?   A . n 
A 1 494 TYR 494 2285 ?    ?   ?   A . n 
A 1 495 LYS 495 2286 ?    ?   ?   A . n 
A 1 496 LYS 496 2287 ?    ?   ?   A . n 
A 1 497 GLY 497 2288 ?    ?   ?   A . n 
A 1 498 PHE 498 2289 ?    ?   ?   A . n 
A 1 499 SER 499 2290 ?    ?   ?   A . n 
A 1 500 VAL 500 2291 ?    ?   ?   A . n 
A 1 501 ASN 501 2292 ?    ?   ?   A . n 
A 1 502 PRO 502 2293 ?    ?   ?   A . n 
A 1 503 ARG 503 2294 ?    ?   ?   A . n 
A 1 504 CYS 504 2295 ?    ?   ?   A . n 
A 1 505 GLN 505 2296 ?    ?   ?   A . n 
A 1 506 ALA 506 2297 ?    ?   ?   A . n 
A 1 507 GLN 507 2298 ?    ?   ?   A . n 
A 1 508 MET 508 2299 ?    ?   ?   A . n 
A 1 509 GLU 509 2300 ?    ?   ?   A . n 
A 1 510 GLU 510 2301 ?    ?   ?   A . n 
A 1 511 ARG 511 2302 ?    ?   ?   A . n 
A 1 512 ALA 512 2303 ?    ?   ?   A . n 
A 1 513 ALA 513 2304 ?    ?   ?   A . n 
A 1 514 ASP 514 2305 ?    ?   ?   A . n 
A 1 515 ARG 515 2306 ?    ?   ?   A . n 
A 1 516 GLY 516 2307 ?    ?   ?   A . n 
A 1 517 MET 517 2308 2308 MET MET A . n 
A 1 518 PRO 518 2309 2309 PRO PRO A . n 
A 1 519 PHE 519 2310 2310 PHE PHE A . n 
A 1 520 SER 520 2311 2311 SER SER A . n 
A 1 521 ILE 521 2312 2312 ILE ILE A . n 
A 1 522 SER 522 2313 2313 SER SER A . n 
A 1 523 MET 523 2314 2314 MET MET A . n 
A 1 524 ARG 524 2315 2315 ARG ARG A . n 
A 1 525 HIS 525 2316 2316 HIS HIS A . n 
A 1 526 ALA 526 2317 2317 ALA ALA A . n 
A 1 527 PHE 527 2318 2318 PHE PHE A . n 
A 1 528 VAL 528 2319 2319 VAL VAL A . n 
A 1 529 PRO 529 2320 2320 PRO PRO A . n 
A 1 530 PHE 530 2321 2321 PHE PHE A . n 
A 1 531 PRO 531 2322 2322 PRO PRO A . n 
A 1 532 GLY 532 2323 2323 GLY GLY A . n 
A 1 533 GLY 533 2324 2324 GLY GLY A . n 
A 1 534 SER 534 2325 2325 SER SER A . n 
A 1 535 ILE 535 2326 2326 ILE ILE A . n 
A 1 536 LEU 536 2327 2327 LEU LEU A . n 
A 1 537 ALA 537 2328 2328 ALA ALA A . n 
A 1 538 ALA 538 2329 2329 ALA ALA A . n 
A 1 539 ASP 539 2330 2330 ASP ASP A . n 
A 1 540 TYR 540 2331 2331 TYR TYR A . n 
A 1 541 SER 541 2332 2332 SER SER A . n 
A 1 542 GLN 542 2333 2333 GLN GLN A . n 
A 1 543 LEU 543 2334 2334 LEU LEU A . n 
A 1 544 GLU 544 2335 2335 GLU GLU A . n 
A 1 545 LEU 545 2336 2336 LEU LEU A . n 
A 1 546 ARG 546 2337 2337 ARG ARG A . n 
A 1 547 ILE 547 2338 2338 ILE ILE A . n 
A 1 548 LEU 548 2339 2339 LEU LEU A . n 
A 1 549 ALA 549 2340 2340 ALA ALA A . n 
A 1 550 HIS 550 2341 2341 HIS HIS A . n 
A 1 551 LEU 551 2342 2342 LEU LEU A . n 
A 1 552 SER 552 2343 2343 SER SER A . n 
A 1 553 HIS 553 2344 2344 HIS HIS A . n 
A 1 554 ASP 554 2345 2345 ASP ASP A . n 
A 1 555 ARG 555 2346 2346 ARG ARG A . n 
A 1 556 ARG 556 2347 2347 ARG ARG A . n 
A 1 557 LEU 557 2348 2348 LEU LEU A . n 
A 1 558 ILE 558 2349 2349 ILE ILE A . n 
A 1 559 GLN 559 2350 2350 GLN GLN A . n 
A 1 560 VAL 560 2351 2351 VAL VAL A . n 
A 1 561 LEU 561 2352 2352 LEU LEU A . n 
A 1 562 ASN 562 2353 2353 ASN ASN A . n 
A 1 563 THR 563 2354 2354 THR THR A . n 
A 1 564 GLY 564 2355 2355 GLY GLY A . n 
A 1 565 ALA 565 2356 2356 ALA ALA A . n 
A 1 566 ASP 566 2357 2357 ASP ASP A . n 
A 1 567 VAL 567 2358 2358 VAL VAL A . n 
A 1 568 PHE 568 2359 2359 PHE PHE A . n 
A 1 569 ARG 569 2360 2360 ARG ARG A . n 
A 1 570 SER 570 2361 2361 SER SER A . n 
A 1 571 ILE 571 2362 2362 ILE ILE A . n 
A 1 572 ALA 572 2363 2363 ALA ALA A . n 
A 1 573 ALA 573 2364 2364 ALA ALA A . n 
A 1 574 GLU 574 2365 2365 GLU GLU A . n 
A 1 575 TRP 575 2366 2366 TRP TRP A . n 
A 1 576 LYS 576 2367 2367 LYS LYS A . n 
A 1 577 MET 577 2368 2368 MET MET A . n 
A 1 578 ILE 578 2369 2369 ILE ILE A . n 
A 1 579 GLU 579 2370 2370 GLU GLU A . n 
A 1 580 PRO 580 2371 2371 PRO PRO A . n 
A 1 581 GLU 581 2372 2372 GLU GLU A . n 
A 1 582 SER 582 2373 2373 SER SER A . n 
A 1 583 VAL 583 2374 2374 VAL VAL A . n 
A 1 584 GLY 584 2375 2375 GLY GLY A . n 
A 1 585 ASP 585 2376 2376 ASP ASP A . n 
A 1 586 ASP 586 2377 2377 ASP ASP A . n 
A 1 587 LEU 587 2378 2378 LEU LEU A . n 
A 1 588 ARG 588 2379 2379 ARG ARG A . n 
A 1 589 GLN 589 2380 2380 GLN GLN A . n 
A 1 590 GLN 590 2381 2381 GLN GLN A . n 
A 1 591 ALA 591 2382 2382 ALA ALA A . n 
A 1 592 LYS 592 2383 2383 LYS LYS A . n 
A 1 593 GLN 593 2384 2384 GLN GLN A . n 
A 1 594 ILE 594 2385 2385 ILE ILE A . n 
A 1 595 CYS 595 2386 2386 CYS CYS A . n 
A 1 596 TYR 596 2387 2387 TYR TYR A . n 
A 1 597 GLY 597 2388 2388 GLY GLY A . n 
A 1 598 ILE 598 2389 2389 ILE ILE A . n 
A 1 599 ILE 599 2390 2390 ILE ILE A . n 
A 1 600 TYR 600 2391 2391 TYR TYR A . n 
A 1 601 GLY 601 2392 2392 GLY GLY A . n 
A 1 602 MET 602 2393 2393 MET MET A . n 
A 1 603 GLY 603 2394 2394 GLY GLY A . n 
A 1 604 ALA 604 2395 2395 ALA ALA A . n 
A 1 605 LYS 605 2396 2396 LYS LYS A . n 
A 1 606 SER 606 2397 2397 SER SER A . n 
A 1 607 LEU 607 2398 2398 LEU LEU A . n 
A 1 608 GLY 608 2399 2399 GLY GLY A . n 
A 1 609 GLU 609 2400 2400 GLU GLU A . n 
A 1 610 GLN 610 2401 2401 GLN GLN A . n 
A 1 611 MET 611 2402 2402 MET MET A . n 
A 1 612 GLY 612 2403 2403 GLY GLY A . n 
A 1 613 ILE 613 2404 2404 ILE ILE A . n 
A 1 614 LYS 614 2405 2405 LYS LYS A . n 
A 1 615 GLU 615 2406 2406 GLU GLU A . n 
A 1 616 ASN 616 2407 2407 ASN ASN A . n 
A 1 617 ASP 617 2408 2408 ASP ASP A . n 
A 1 618 ALA 618 2409 2409 ALA ALA A . n 
A 1 619 ALA 619 2410 2410 ALA ALA A . n 
A 1 620 CYS 620 2411 2411 CYS CYS A . n 
A 1 621 TYR 621 2412 2412 TYR TYR A . n 
A 1 622 ILE 622 2413 2413 ILE ILE A . n 
A 1 623 ASP 623 2414 2414 ASP ASP A . n 
A 1 624 SER 624 2415 2415 SER SER A . n 
A 1 625 PHE 625 2416 2416 PHE PHE A . n 
A 1 626 LYS 626 2417 2417 LYS LYS A . n 
A 1 627 SER 627 2418 2418 SER SER A . n 
A 1 628 ARG 628 2419 2419 ARG ARG A . n 
A 1 629 TYR 629 2420 2420 TYR TYR A . n 
A 1 630 THR 630 2421 2421 THR THR A . n 
A 1 631 GLY 631 2422 2422 GLY GLY A . n 
A 1 632 ILE 632 2423 2423 ILE ILE A . n 
A 1 633 ASN 633 2424 2424 ASN ASN A . n 
A 1 634 GLN 634 2425 2425 GLN GLN A . n 
A 1 635 PHE 635 2426 2426 PHE PHE A . n 
A 1 636 MET 636 2427 2427 MET MET A . n 
A 1 637 THR 637 2428 2428 THR THR A . n 
A 1 638 GLU 638 2429 2429 GLU GLU A . n 
A 1 639 THR 639 2430 2430 THR THR A . n 
A 1 640 VAL 640 2431 2431 VAL VAL A . n 
A 1 641 LYS 641 2432 2432 LYS LYS A . n 
A 1 642 ASN 642 2433 2433 ASN ASN A . n 
A 1 643 CYS 643 2434 2434 CYS CYS A . n 
A 1 644 LYS 644 2435 2435 LYS LYS A . n 
A 1 645 ARG 645 2436 2436 ARG ARG A . n 
A 1 646 ASP 646 2437 2437 ASP ASP A . n 
A 1 647 GLY 647 2438 2438 GLY GLY A . n 
A 1 648 PHE 648 2439 2439 PHE PHE A . n 
A 1 649 VAL 649 2440 2440 VAL VAL A . n 
A 1 650 GLN 650 2441 2441 GLN GLN A . n 
A 1 651 THR 651 2442 2442 THR THR A . n 
A 1 652 ILE 652 2443 2443 ILE ILE A . n 
A 1 653 LEU 653 2444 2444 LEU LEU A . n 
A 1 654 GLY 654 2445 2445 GLY GLY A . n 
A 1 655 ARG 655 2446 2446 ARG ARG A . n 
A 1 656 ARG 656 2447 2447 ARG ARG A . n 
A 1 657 ARG 657 2448 2448 ARG ARG A . n 
A 1 658 TYR 658 2449 2449 TYR TYR A . n 
A 1 659 LEU 659 2450 2450 LEU LEU A . n 
A 1 660 PRO 660 2451 2451 PRO PRO A . n 
A 1 661 GLY 661 2452 2452 GLY GLY A . n 
A 1 662 ILE 662 2453 2453 ILE ILE A . n 
A 1 663 LYS 663 2454 2454 LYS LYS A . n 
A 1 664 ASP 664 2455 2455 ASP ASP A . n 
A 1 665 ASN 665 2456 2456 ASN ASN A . n 
A 1 666 ASN 666 2457 2457 ASN ASN A . n 
A 1 667 PRO 667 2458 2458 PRO PRO A . n 
A 1 668 TYR 668 2459 2459 TYR TYR A . n 
A 1 669 ARG 669 2460 2460 ARG ARG A . n 
A 1 670 LYS 670 2461 2461 LYS LYS A . n 
A 1 671 ALA 671 2462 2462 ALA ALA A . n 
A 1 672 HIS 672 2463 2463 HIS HIS A . n 
A 1 673 ALA 673 2464 2464 ALA ALA A . n 
A 1 674 GLU 674 2465 2465 GLU GLU A . n 
A 1 675 ARG 675 2466 2466 ARG ARG A . n 
A 1 676 GLN 676 2467 2467 GLN GLN A . n 
A 1 677 ALA 677 2468 2468 ALA ALA A . n 
A 1 678 ILE 678 2469 2469 ILE ILE A . n 
A 1 679 ASN 679 2470 2470 ASN ASN A . n 
A 1 680 THR 680 2471 2471 THR THR A . n 
A 1 681 ILE 681 2472 2472 ILE ILE A . n 
A 1 682 VAL 682 2473 2473 VAL VAL A . n 
A 1 683 GLN 683 2474 2474 GLN GLN A . n 
A 1 684 GLY 684 2475 2475 GLY GLY A . n 
A 1 685 SER 685 2476 2476 SER SER A . n 
A 1 686 ALA 686 2477 2477 ALA ALA A . n 
A 1 687 ALA 687 2478 2478 ALA ALA A . n 
A 1 688 ASP 688 2479 2479 ASP ASP A . n 
A 1 689 ILE 689 2480 2480 ILE ILE A . n 
A 1 690 VAL 690 2481 2481 VAL VAL A . n 
A 1 691 LYS 691 2482 2482 LYS LYS A . n 
A 1 692 ILE 692 2483 2483 ILE ILE A . n 
A 1 693 ALA 693 2484 2484 ALA ALA A . n 
A 1 694 THR 694 2485 2485 THR THR A . n 
A 1 695 VAL 695 2486 2486 VAL VAL A . n 
A 1 696 ASN 696 2487 2487 ASN ASN A . n 
A 1 697 ILE 697 2488 2488 ILE ILE A . n 
A 1 698 GLN 698 2489 2489 GLN GLN A . n 
A 1 699 LYS 699 2490 2490 LYS LYS A . n 
A 1 700 GLN 700 2491 2491 GLN GLN A . n 
A 1 701 LEU 701 2492 2492 LEU LEU A . n 
A 1 702 GLU 702 2493 2493 GLU GLU A . n 
A 1 703 THR 703 2494 2494 THR THR A . n 
A 1 704 PHE 704 2495 2495 PHE PHE A . n 
A 1 705 HIS 705 2496 2496 HIS HIS A . n 
A 1 706 SER 706 2497 2497 SER SER A . n 
A 1 707 THR 707 2498 2498 THR THR A . n 
A 1 708 PHE 708 2499 2499 PHE PHE A . n 
A 1 709 LYS 709 2500 2500 LYS LYS A . n 
A 1 710 SER 710 2501 2501 SER SER A . n 
A 1 711 HIS 711 2502 2502 HIS HIS A . n 
A 1 712 GLY 712 2503 2503 GLY GLY A . n 
A 1 713 HIS 713 2504 2504 HIS HIS A . n 
A 1 714 ARG 714 2505 2505 ARG ARG A . n 
A 1 715 GLU 715 2506 2506 GLU GLU A . n 
A 1 716 GLY 716 2507 2507 GLY GLY A . n 
A 1 717 MET 717 2508 2508 MET MET A . n 
A 1 718 LEU 718 2509 ?    ?   ?   A . n 
A 1 719 GLN 719 2510 ?    ?   ?   A . n 
A 1 720 SER 720 2511 ?    ?   ?   A . n 
A 1 721 ASP 721 2512 ?    ?   ?   A . n 
A 1 722 GLN 722 2513 ?    ?   ?   A . n 
A 1 723 THR 723 2514 ?    ?   ?   A . n 
A 1 724 GLY 724 2515 ?    ?   ?   A . n 
A 1 725 LEU 725 2516 ?    ?   ?   A . n 
A 1 726 SER 726 2517 ?    ?   ?   A . n 
A 1 727 ARG 727 2518 ?    ?   ?   A . n 
A 1 728 LYS 728 2519 ?    ?   ?   A . n 
A 1 729 ARG 729 2520 ?    ?   ?   A . n 
A 1 730 LYS 730 2521 ?    ?   ?   A . n 
A 1 731 LEU 731 2522 ?    ?   ?   A . n 
A 1 732 GLN 732 2523 ?    ?   ?   A . n 
A 1 733 GLY 733 2524 ?    ?   ?   A . n 
A 1 734 MET 734 2525 ?    ?   ?   A . n 
A 1 735 PHE 735 2526 2526 PHE PHE A . n 
A 1 736 CYS 736 2527 2527 CYS CYS A . n 
A 1 737 PRO 737 2528 2528 PRO PRO A . n 
A 1 738 ILE 738 2529 2529 ILE ILE A . n 
A 1 739 ARG 739 2530 2530 ARG ARG A . n 
A 1 740 GLY 740 2531 2531 GLY GLY A . n 
A 1 741 GLY 741 2532 2532 GLY GLY A . n 
A 1 742 PHE 742 2533 2533 PHE PHE A . n 
A 1 743 PHE 743 2534 2534 PHE PHE A . n 
A 1 744 ILE 744 2535 2535 ILE ILE A . n 
A 1 745 LEU 745 2536 2536 LEU LEU A . n 
A 1 746 GLN 746 2537 2537 GLN GLN A . n 
A 1 747 LEU 747 2538 2538 LEU LEU A . n 
A 1 748 HIS 748 2539 2539 HIS HIS A . n 
A 1 749 ASP 749 2540 2540 ASP ASP A . n 
A 1 750 GLU 750 2541 2541 GLU GLU A . n 
A 1 751 LEU 751 2542 2542 LEU LEU A . n 
A 1 752 LEU 752 2543 2543 LEU LEU A . n 
A 1 753 TYR 753 2544 2544 TYR TYR A . n 
A 1 754 GLU 754 2545 2545 GLU GLU A . n 
A 1 755 VAL 755 2546 2546 VAL VAL A . n 
A 1 756 ALA 756 2547 2547 ALA ALA A . n 
A 1 757 GLU 757 2548 2548 GLU GLU A . n 
A 1 758 GLU 758 2549 2549 GLU GLU A . n 
A 1 759 ASP 759 2550 2550 ASP ASP A . n 
A 1 760 VAL 760 2551 2551 VAL VAL A . n 
A 1 761 VAL 761 2552 2552 VAL VAL A . n 
A 1 762 GLN 762 2553 2553 GLN GLN A . n 
A 1 763 VAL 763 2554 2554 VAL VAL A . n 
A 1 764 ALA 764 2555 2555 ALA ALA A . n 
A 1 765 GLN 765 2556 2556 GLN GLN A . n 
A 1 766 ILE 766 2557 2557 ILE ILE A . n 
A 1 767 VAL 767 2558 2558 VAL VAL A . n 
A 1 768 LYS 768 2559 2559 LYS LYS A . n 
A 1 769 ASN 769 2560 2560 ASN ASN A . n 
A 1 770 GLU 770 2561 2561 GLU GLU A . n 
A 1 771 MET 771 2562 2562 MET MET A . n 
A 1 772 GLU 772 2563 2563 GLU GLU A . n 
A 1 773 SER 773 2564 2564 SER SER A . n 
A 1 774 ALA 774 2565 2565 ALA ALA A . n 
A 1 775 VAL 775 2566 2566 VAL VAL A . n 
A 1 776 LYS 776 2567 2567 LYS LYS A . n 
A 1 777 LEU 777 2568 2568 LEU LEU A . n 
A 1 778 SER 778 2569 2569 SER SER A . n 
A 1 779 VAL 779 2570 2570 VAL VAL A . n 
A 1 780 LYS 780 2571 2571 LYS LYS A . n 
A 1 781 LEU 781 2572 2572 LEU LEU A . n 
A 1 782 LYS 782 2573 2573 LYS LYS A . n 
A 1 783 VAL 783 2574 2574 VAL VAL A . n 
A 1 784 LYS 784 2575 2575 LYS LYS A . n 
A 1 785 VAL 785 2576 2576 VAL VAL A . n 
A 1 786 LYS 786 2577 2577 LYS LYS A . n 
A 1 787 ILE 787 2578 2578 ILE ILE A . n 
A 1 788 GLY 788 2579 2579 GLY GLY A . n 
A 1 789 ALA 789 2580 2580 ALA ALA A . n 
A 1 790 SER 790 2581 2581 SER SER A . n 
A 1 791 TRP 791 2582 2582 TRP TRP A . n 
A 1 792 GLY 792 2583 2583 GLY GLY A . n 
A 1 793 GLU 793 2584 2584 GLU GLU A . n 
A 1 794 LEU 794 2585 2585 LEU LEU A . n 
A 1 795 LYS 795 2586 2586 LYS LYS A . n 
A 1 796 ASP 796 2587 2587 ASP ASP A . n 
A 1 797 PHE 797 2588 2588 PHE PHE A . n 
A 1 798 ASP 798 2589 2589 ASP ASP A . n 
A 1 799 VAL 799 2590 2590 VAL VAL A . n 
B 2 1   DG  1   1    ?    ?   ?   E . n 
B 2 2   DC  2   2    ?    ?   ?   E . n 
B 2 3   DA  3   3    ?    ?   ?   E . n 
B 2 4   DG  4   4    ?    ?   ?   E . n 
B 2 5   DT  5   5    ?    ?   ?   E . n 
B 2 6   DC  6   6    ?    ?   ?   E . n 
B 2 7   DA  7   7    7    DA  DA  E . n 
B 2 8   DG  8   8    8    DG  DG  E . n 
B 2 9   DC  9   9    9    DC  DC  E . n 
B 2 10  DT  10  10   10   DT  DT  E . n 
B 2 11  DC  11  11   11   DC  DC  E . n 
B 2 12  DT  12  12   12   DT  DT  E . n 
B 2 13  DA  13  13   13   DA  DA  E . n 
B 2 14  DC  14  14   14   DC  DC  E . n 
B 2 15  DG  15  15   15   DG  DG  E . n 
B 2 16  DG  16  16   16   DG  DG  E . n 
B 2 17  DA  17  17   17   DA  DA  E . n 
B 2 18  DT  18  18   18   DT  DT  E . n 
B 2 19  DG  19  19   19   DG  DG  E . n 
B 2 20  DC  20  20   20   DC  DC  E . n 
B 2 21  DC  21  21   ?    ?   ?   E . n 
B 2 22  DT  22  22   ?    ?   ?   E . n 
B 2 23  DC  23  23   ?    ?   ?   E . n 
B 2 24  DA  24  24   ?    ?   ?   E . n 
B 2 25  DC  25  25   ?    ?   ?   E . n 
B 2 26  DA  26  26   ?    ?   ?   E . n 
B 2 27  DG  27  27   ?    ?   ?   E . n 
B 2 28  DC  28  28   ?    ?   ?   E . n 
B 2 29  DA  29  29   ?    ?   ?   E . n 
C 3 1   DT  1   1    ?    ?   ?   F . n 
C 3 2   DG  2   2    ?    ?   ?   F . n 
C 3 3   DC  3   3    ?    ?   ?   F . n 
C 3 4   DT  4   4    ?    ?   ?   F . n 
C 3 5   DG  5   5    ?    ?   ?   F . n 
C 3 6   DT  6   6    ?    ?   ?   F . n 
C 3 7   DG  7   7    ?    ?   ?   F . n 
C 3 8   DA  8   8    ?    ?   ?   F . n 
C 3 9   DG  9   9    ?    ?   ?   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_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 DGT 1 2601 1 DGT DGT A . 
E 5 MG  1 2602 1 MG  MG  A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ARG 1860 ? CG    ? A ARG 69  CG    
2  1 Y 1 A ARG 1860 ? CD    ? A ARG 69  CD    
3  1 Y 1 A ARG 1860 ? NE    ? A ARG 69  NE    
4  1 Y 1 A ARG 1860 ? CZ    ? A ARG 69  CZ    
5  1 Y 1 A ARG 1860 ? NH1   ? A ARG 69  NH1   
6  1 Y 1 A ARG 1860 ? NH2   ? A ARG 69  NH2   
7  1 Y 1 A SER 1861 ? OG    ? A SER 70  OG    
8  1 Y 1 A ASP 1896 ? CG    ? A ASP 105 CG    
9  1 Y 1 A ASP 1896 ? OD1   ? A ASP 105 OD1   
10 1 Y 1 A ASP 1896 ? OD2   ? A ASP 105 OD2   
11 1 Y 1 A LYS 1942 ? CG    ? A LYS 151 CG    
12 1 Y 1 A LYS 1942 ? CD    ? A LYS 151 CD    
13 1 Y 1 A LYS 1942 ? CE    ? A LYS 151 CE    
14 1 Y 1 A LYS 1942 ? NZ    ? A LYS 151 NZ    
15 1 Y 1 A THR 2025 ? OG1   ? A THR 234 OG1   
16 1 Y 1 A THR 2025 ? CG2   ? A THR 234 CG2   
17 1 Y 1 A SER 2026 ? OG    ? A SER 235 OG    
18 1 Y 1 A GLN 2027 ? CG    ? A GLN 236 CG    
19 1 Y 1 A GLN 2027 ? CD    ? A GLN 236 CD    
20 1 Y 1 A GLN 2027 ? OE1   ? A GLN 236 OE1   
21 1 Y 1 A GLN 2027 ? NE2   ? A GLN 236 NE2   
22 1 Y 1 A ARG 2147 ? CG    ? A ARG 356 CG    
23 1 Y 1 A ARG 2147 ? CD    ? A ARG 356 CD    
24 1 Y 1 A ARG 2147 ? NE    ? A ARG 356 NE    
25 1 Y 1 A ARG 2147 ? CZ    ? A ARG 356 CZ    
26 1 Y 1 A ARG 2147 ? NH1   ? A ARG 356 NH1   
27 1 Y 1 A ARG 2147 ? NH2   ? A ARG 356 NH2   
28 1 Y 1 A GLU 2257 ? CG    ? A GLU 466 CG    
29 1 Y 1 A GLU 2257 ? CD    ? A GLU 466 CD    
30 1 Y 1 A GLU 2257 ? OE1   ? A GLU 466 OE1   
31 1 Y 1 A GLU 2257 ? OE2   ? A GLU 466 OE2   
32 1 Y 1 A LYS 2259 ? CG    ? A LYS 468 CG    
33 1 Y 1 A LYS 2259 ? CD    ? A LYS 468 CD    
34 1 Y 1 A LYS 2259 ? CE    ? A LYS 468 CE    
35 1 Y 1 A LYS 2259 ? NZ    ? A LYS 468 NZ    
36 1 Y 1 A GLU 2370 ? CG    ? A GLU 579 CG    
37 1 Y 1 A GLU 2370 ? CD    ? A GLU 579 CD    
38 1 Y 1 A GLU 2370 ? OE1   ? A GLU 579 OE1   
39 1 Y 1 A GLU 2370 ? OE2   ? A GLU 579 OE2   
40 1 Y 1 A GLU 2372 ? CG    ? A GLU 581 CG    
41 1 Y 1 A GLU 2372 ? CD    ? A GLU 581 CD    
42 1 Y 1 A GLU 2372 ? OE1   ? A GLU 581 OE1   
43 1 Y 1 A GLU 2372 ? OE2   ? A GLU 581 OE2   
44 1 Y 1 E DA  7    ? P     ? B DA  7   P     
45 1 Y 1 E DA  7    ? OP1   ? B DA  7   OP1   
46 1 Y 1 E DA  7    ? OP2   ? B DA  7   OP2   
47 1 Y 1 E DA  7    ? "O5'" ? B DA  7   "O5'" 
48 1 Y 1 E DA  7    ? "C5'" ? B DA  7   "C5'" 
49 1 Y 1 E DA  7    ? "C4'" ? B DA  7   "C4'" 
50 1 Y 1 E DA  7    ? "O4'" ? B DA  7   "O4'" 
51 1 Y 1 E DA  7    ? "C3'" ? B DA  7   "C3'" 
52 1 Y 1 E DA  7    ? "C2'" ? B DA  7   "C2'" 
53 1 Y 1 E DA  7    ? "C1'" ? B DA  7   "C1'" 
54 1 Y 1 E DA  7    ? N9    ? B DA  7   N9    
55 1 Y 1 E DA  7    ? C8    ? B DA  7   C8    
56 1 Y 1 E DA  7    ? N7    ? B DA  7   N7    
57 1 Y 1 E DA  7    ? C5    ? B DA  7   C5    
58 1 Y 1 E DA  7    ? C6    ? B DA  7   C6    
59 1 Y 1 E DA  7    ? N6    ? B DA  7   N6    
60 1 Y 1 E DA  7    ? N1    ? B DA  7   N1    
61 1 Y 1 E DA  7    ? C2    ? B DA  7   C2    
62 1 Y 1 E DA  7    ? N3    ? B DA  7   N3    
63 1 Y 1 E DA  7    ? C4    ? B DA  7   C4    
# 
_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                     9AU5 
_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                         9AU5 
_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                   9AU5 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9AU5 
_struct.title                        'Ternary complex of human DNA polymerase theta polymerase domain with a cognate C:G base pair' 
_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        9AU5 
_struct_keywords.text            
'DNA translesion synthesis, theta-mediated end joining, A-family DNA polymerase, 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 UNP DPOLQ_HUMAN O75417 ? 1 
;GFKDNSPISDTSFSLQLSQDGLQLTPASSSSESLSIIDVASDQNLFQTFIKEWRCKKRFSISLACEKIRSLTSSKTATIG
SRFKQASSPQEIPIRDDGFPIKGCDDTLVVGLAVCWGGRDAYYFSLQKEQKHSEISASLVPPSLDPSLTLKDRMWYLQSC
LRKESDKECSVVIYDFIQSYKILLLSCGISLEQSYEDPKVACWLLDPDSQEPTLHSIVTSFLPHELPLLEGMETSQGIQS
LGLNAGSEHSGRYRASVESILIFNSMNQLNSLLQKENLQDVFRKVEMPSQYCLALLELNGIGFSTAECESQKHIMQAKLD
AIETQAYQLAGHSFSFTSSDDIAEVLFLELKLPPNREMKNQGSKKTLGSTRRGIDNGRKLRLGRQFSTSKDVLNKLKALH
PLPGLILEWRRITNAITKVVFPLQREKCLNPFLGMERIYPVSQSHTATGRITFTEPNIQNVPRDFEIKMPTLVGESPPSQ
AVGKGLLPMGRGKYKKGFSVNPRCQAQMEERAADRGMPFSISMRHAFVPFPGGSILAADYSQLELRILAHLSHDRRLIQV
LNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGIIYGMGAKSLGEQMGIKENDAACYIDSFKSRYTGINQFMTETV
KNCKRDGFVQTILGRRRYLPGIKDNNPYRKAHAERQAINTIVQGSAADIVKIATVNIQKQLETFHSTFKSHGHREGMLQS
DQTGLSRKRKLQGMFCPIRGGFFILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKLSVKLKVKVKIGASWGELKDFDV
;
1792 
2 PDB 9AU5        9AU5   ? 2 ? 1    
3 PDB 9AU5        9AU5   ? 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 9AU5 A 1 ? 799 ? O75417 1792 ? 2590 ? 1792 2590 
2 2 9AU5 E 1 ? 29  ? 9AU5   1    ? 29   ? 1    29   
3 3 9AU5 F 1 ? 20  ? 9AU5   1    ? 20   ? 1    20   
# 
_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 ASP A 42  ? LYS A 56  ? ASP A 1833 LYS A 1847 1 ? 15 
HELX_P HELX_P2  AA2 THR A 149 ? LEU A 161 ? THR A 1940 LEU A 1952 1 ? 13 
HELX_P HELX_P3  AA3 ASP A 175 ? SER A 186 ? ASP A 1966 SER A 1977 1 ? 12 
HELX_P HELX_P4  AA4 ASP A 197 ? ASP A 206 ? ASP A 1988 ASP A 1997 1 ? 10 
HELX_P HELX_P5  AA5 THR A 213 ? LEU A 222 ? THR A 2004 LEU A 2013 1 ? 10 
HELX_P HELX_P6  AA6 PRO A 223 ? GLU A 230 ? PRO A 2014 GLU A 2021 5 ? 8  
HELX_P HELX_P7  AA7 SER A 250 ? ASN A 277 ? SER A 2041 ASN A 2068 1 ? 28 
HELX_P HELX_P8  AA8 LEU A 278 ? VAL A 285 ? LEU A 2069 VAL A 2076 1 ? 8  
HELX_P HELX_P9  AA9 VAL A 285 ? GLY A 300 ? VAL A 2076 GLY A 2091 1 ? 16 
HELX_P HELX_P10 AB1 THR A 305 ? GLY A 331 ? THR A 2096 GLY A 2122 1 ? 27 
HELX_P HELX_P11 AB2 SER A 338 ? PHE A 347 ? SER A 2129 PHE A 2138 1 ? 10 
HELX_P HELX_P12 AB3 SER A 389 ? LEU A 396 ? SER A 2180 LEU A 2187 1 ? 8  
HELX_P HELX_P13 AB4 PRO A 401 ? LYS A 418 ? PRO A 2192 LYS A 2209 1 ? 18 
HELX_P HELX_P14 AB5 VAL A 419 ? GLU A 426 ? VAL A 2210 GLU A 2217 1 ? 8  
HELX_P HELX_P15 AB6 MET A 523 ? PHE A 527 ? MET A 2314 PHE A 2318 5 ? 5  
HELX_P HELX_P16 AB7 GLN A 542 ? LEU A 551 ? GLN A 2333 LEU A 2342 1 ? 10 
HELX_P HELX_P17 AB8 ASP A 554 ? THR A 563 ? ASP A 2345 THR A 2354 1 ? 10 
HELX_P HELX_P18 AB9 ASP A 566 ? MET A 577 ? ASP A 2357 MET A 2368 1 ? 12 
HELX_P HELX_P19 AC1 GLY A 584 ? TYR A 600 ? GLY A 2375 TYR A 2391 1 ? 17 
HELX_P HELX_P20 AC2 GLY A 603 ? GLY A 612 ? GLY A 2394 GLY A 2403 1 ? 10 
HELX_P HELX_P21 AC3 LYS A 614 ? TYR A 629 ? LYS A 2405 TYR A 2420 1 ? 16 
HELX_P HELX_P22 AC4 TYR A 629 ? GLY A 647 ? TYR A 2420 GLY A 2438 1 ? 19 
HELX_P HELX_P23 AC5 PRO A 660 ? ASP A 664 ? PRO A 2451 ASP A 2455 5 ? 5  
HELX_P HELX_P24 AC6 ASN A 666 ? PHE A 704 ? ASN A 2457 PHE A 2495 1 ? 39 
HELX_P HELX_P25 AC7 SER A 710 ? MET A 717 ? SER A 2501 MET A 2508 1 ? 8  
HELX_P HELX_P26 AC8 ASP A 759 ? SER A 773 ? ASP A 2550 SER A 2564 1 ? 15 
# 
_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 ? ? ? ? ? ? ?            1.594 ? ? 
metalc1  metalc ?    ? A ASP 539 OD1   ? ? ? 1_555 E MG  .  MG ? ? A ASP 2330 A MG  2602 1_555 ? ? ? ? ? ? ?            2.015 ? ? 
metalc2  metalc ?    ? A ASP 539 OD2   ? ? ? 1_555 E MG  .  MG ? ? A ASP 2330 A MG  2602 1_555 ? ? ? ? ? ? ?            2.195 ? ? 
metalc3  metalc ?    ? A TYR 540 O     ? ? ? 1_555 E MG  .  MG ? ? A TYR 2331 A MG  2602 1_555 ? ? ? ? ? ? ?            2.324 ? ? 
metalc4  metalc ?    ? A ASP 749 OD2   ? ? ? 1_555 E MG  .  MG ? ? A ASP 2540 A MG  2602 1_555 ? ? ? ? ? ? ?            2.034 ? ? 
metalc5  metalc ?    ? D DGT .   O1G   ? ? ? 1_555 E MG  .  MG ? ? A DGT 2601 A MG  2602 1_555 ? ? ? ? ? ? ?            2.806 ? ? 
metalc6  metalc ?    ? D DGT .   O2B   ? ? ? 1_555 E MG  .  MG ? ? A DGT 2601 A MG  2602 1_555 ? ? ? ? ? ? ?            2.006 ? ? 
metalc7  metalc ?    ? D DGT .   O2A   ? ? ? 1_555 E MG  .  MG ? ? A DGT 2601 A MG  2602 1_555 ? ? ? ? ? ? ?            2.998 ? ? 
hydrog1  hydrog ?    ? B DT  10  N3    ? ? ? 1_555 C 2DA 20 N1 ? ? E DT  10   F 2DA 20   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog2  hydrog ?    ? B DT  10  O4    ? ? ? 1_555 C 2DA 20 N6 ? ? E DT  10   F 2DA 20   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog3  hydrog ?    ? B DC  11  N3    ? ? ? 1_555 C DG  19 N1 ? ? E DC  11   F DG  19   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog4  hydrog ?    ? B DC  11  N4    ? ? ? 1_555 C DG  19 O6 ? ? E DC  11   F DG  19   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog5  hydrog ?    ? B DC  11  O2    ? ? ? 1_555 C DG  19 N2 ? ? E DC  11   F DG  19   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog6  hydrog ?    ? B DT  12  N3    ? ? ? 1_555 C DA  18 N1 ? ? E DT  12   F DA  18   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog7  hydrog ?    ? B DT  12  O4    ? ? ? 1_555 C DA  18 N6 ? ? E DT  12   F DA  18   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog8  hydrog ?    ? B DA  13  N1    ? ? ? 1_555 C DT  17 N3 ? ? E DA  13   F DT  17   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog9  hydrog ?    ? B DA  13  N6    ? ? ? 1_555 C DT  17 O4 ? ? E DA  13   F DT  17   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog10 hydrog ?    ? B DC  14  N3    ? ? ? 1_555 C DG  16 N1 ? ? E DC  14   F DG  16   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog11 hydrog ?    ? B DC  14  N4    ? ? ? 1_555 C DG  16 O6 ? ? E DC  14   F DG  16   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog12 hydrog ?    ? B DC  14  O2    ? ? ? 1_555 C DG  16 N2 ? ? E DC  14   F DG  16   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog13 hydrog ?    ? B DG  15  N1    ? ? ? 1_555 C DC  15 N3 ? ? E DG  15   F DC  15   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog14 hydrog ?    ? B DG  15  N2    ? ? ? 1_555 C DC  15 O2 ? ? E DG  15   F DC  15   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog15 hydrog ?    ? B DG  15  O6    ? ? ? 1_555 C DC  15 N4 ? ? E DG  15   F DC  15   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog16 hydrog ?    ? B DG  16  N1    ? ? ? 1_555 C DC  14 N3 ? ? E DG  16   F DC  14   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog17 hydrog ?    ? B DG  16  N2    ? ? ? 1_555 C DC  14 O2 ? ? E DG  16   F DC  14   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog18 hydrog ?    ? B DG  16  O6    ? ? ? 1_555 C DC  14 N4 ? ? E DG  16   F DC  14   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog19 hydrog ?    ? B DA  17  N1    ? ? ? 1_555 C DT  13 N3 ? ? E DA  17   F DT  13   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog20 hydrog ?    ? B DA  17  N6    ? ? ? 1_555 C DT  13 O4 ? ? E DA  17   F DT  13   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog21 hydrog ?    ? B DT  18  N3    ? ? ? 1_555 C DA  12 N1 ? ? E DT  18   F DA  12   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog22 hydrog ?    ? B DT  18  O4    ? ? ? 1_555 C DA  12 N6 ? ? E DT  18   F DA  12   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog23 hydrog ?    ? B DG  19  N1    ? ? ? 1_555 C DC  11 N3 ? ? E DG  19   F DC  11   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog24 hydrog ?    ? B DG  19  N2    ? ? ? 1_555 C DC  11 O2 ? ? E DG  19   F DC  11   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog25 hydrog ?    ? B DG  19  O6    ? ? ? 1_555 C DC  11 N4 ? ? E DG  19   F DC  11   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog26 hydrog ?    ? B DC  20  N3    ? ? ? 1_555 C DG  10 N1 ? ? E DC  20   F DG  10   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog27 hydrog ?    ? B DC  20  N4    ? ? ? 1_555 C DG  10 O6 ? ? E DC  20   F DG  10   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog28 hydrog ?    ? B DC  20  O2    ? ? ? 1_555 C DG  10 N2 ? ? E DC  20   F DG  10   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 ? A ASP 539 ? A ASP 2330 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 OD2 ? A ASP 539 ? A ASP 2330 ? 1_555 62.6  ? 
2  OD1 ? A ASP 539 ? A ASP 2330 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 O   ? A TYR 540 ? A TYR 2331 ? 1_555 124.3 ? 
3  OD2 ? A ASP 539 ? A ASP 2330 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 O   ? A TYR 540 ? A TYR 2331 ? 1_555 74.6  ? 
4  OD1 ? A ASP 539 ? A ASP 2330 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 OD2 ? A ASP 749 ? A ASP 2540 ? 1_555 87.6  ? 
5  OD2 ? A ASP 539 ? A ASP 2330 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 OD2 ? A ASP 749 ? A ASP 2540 ? 1_555 137.7 ? 
6  O   ? A TYR 540 ? A TYR 2331 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 OD2 ? A ASP 749 ? A ASP 2540 ? 1_555 103.3 ? 
7  OD1 ? A ASP 539 ? A ASP 2330 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 O1G ? D DGT .   ? A DGT 2601 ? 1_555 96.6  ? 
8  OD2 ? A ASP 539 ? A ASP 2330 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 O1G ? D DGT .   ? A DGT 2601 ? 1_555 64.1  ? 
9  O   ? A TYR 540 ? A TYR 2331 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 O1G ? D DGT .   ? A DGT 2601 ? 1_555 95.0  ? 
10 OD2 ? A ASP 749 ? A ASP 2540 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 O1G ? D DGT .   ? A DGT 2601 ? 1_555 154.6 ? 
11 OD1 ? A ASP 539 ? A ASP 2330 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 O2B ? D DGT .   ? A DGT 2601 ? 1_555 139.7 ? 
12 OD2 ? A ASP 539 ? A ASP 2330 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 O2B ? D DGT .   ? A DGT 2601 ? 1_555 128.8 ? 
13 O   ? A TYR 540 ? A TYR 2331 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 O2B ? D DGT .   ? A DGT 2601 ? 1_555 94.7  ? 
14 OD2 ? A ASP 749 ? A ASP 2540 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 O2B ? D DGT .   ? A DGT 2601 ? 1_555 93.5  ? 
15 O1G ? D DGT .   ? A DGT 2601 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 O2B ? D DGT .   ? A DGT 2601 ? 1_555 67.3  ? 
16 OD1 ? A ASP 539 ? A ASP 2330 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 O2A ? D DGT .   ? A DGT 2601 ? 1_555 76.4  ? 
17 OD2 ? A ASP 539 ? A ASP 2330 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 O2A ? D DGT .   ? A DGT 2601 ? 1_555 113.3 ? 
18 O   ? A TYR 540 ? A TYR 2331 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 O2A ? D DGT .   ? A DGT 2601 ? 1_555 157.4 ? 
19 OD2 ? A ASP 749 ? A ASP 2540 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 O2A ? D DGT .   ? A DGT 2601 ? 1_555 85.0  ? 
20 O1G ? D DGT .   ? A DGT 2601 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 O2A ? D DGT .   ? A DGT 2601 ? 1_555 71.7  ? 
21 O2B ? D DGT .   ? A DGT 2601 ? 1_555 MG ? E MG . ? A MG 2602 ? 1_555 O2A ? D DGT .   ? A DGT 2601 ? 1_555 63.6  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLU 
_struct_mon_prot_cis.label_seq_id           455 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLU 
_struct_mon_prot_cis.auth_seq_id            2246 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    456 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     2247 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -7.03 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 5 ? 
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 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? 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 ARG A 58  ? PHE A 59  ? ARG A 1849 PHE A 1850 
AA1 2 SER A 170 ? VAL A 171 ? SER A 1961 VAL A 1962 
AA1 3 SER A 194 ? TYR A 195 ? SER A 1985 TYR A 1986 
AA2 1 SER A 62  ? LYS A 67  ? SER A 1853 LYS A 1858 
AA2 2 THR A 107 ? ALA A 113 ? THR A 1898 ALA A 1904 
AA2 3 TYR A 123 ? SER A 125 ? TYR A 1914 SER A 1916 
AA3 1 VAL A 441 ? GLN A 443 ? VAL A 2232 GLN A 2234 
AA3 2 THR A 452 ? THR A 454 ? THR A 2243 THR A 2245 
AA4 1 PHE A 743 ? GLN A 746 ? PHE A 2534 GLN A 2537 
AA4 2 LEU A 751 ? ALA A 756 ? LEU A 2542 ALA A 2547 
AA4 3 GLY A 533 ? TYR A 540 ? GLY A 2324 TYR A 2331 
AA4 4 VAL A 783 ? GLY A 788 ? VAL A 2574 GLY A 2579 
AA4 5 LEU A 794 ? ASP A 796 ? LEU A 2585 ASP A 2587 
AA5 1 PHE A 648 ? VAL A 649 ? PHE A 2439 VAL A 2440 
AA5 2 ARG A 657 ? TYR A 658 ? ARG A 2448 TYR A 2449 
# 
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 PHE A 59  ? N PHE A 1850 O SER A 170 ? O SER A 1961 
AA1 2 3 N VAL A 171 ? N VAL A 1962 O SER A 194 ? O SER A 1985 
AA2 1 2 N ALA A 64  ? N ALA A 1855 O GLY A 111 ? O GLY A 1902 
AA2 2 3 N LEU A 112 ? N LEU A 1903 O PHE A 124 ? O PHE A 1915 
AA3 1 2 N VAL A 441 ? N VAL A 2232 O THR A 454 ? O THR A 2245 
AA4 1 2 N LEU A 745 ? N LEU A 2536 O LEU A 752 ? O LEU A 2543 
AA4 2 3 O VAL A 755 ? O VAL A 2546 N SER A 534 ? N SER A 2325 
AA4 3 4 N ALA A 537 ? N ALA A 2328 O LYS A 786 ? O LYS A 2577 
AA4 4 5 N ILE A 787 ? N ILE A 2578 O LYS A 795 ? O LYS A 2586 
AA5 1 2 N VAL A 649 ? N VAL A 2440 O ARG A 657 ? O ARG A 2448 
# 
_pdbx_entry_details.entry_id                   9AU5 
_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_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 ARG A 1886 ? ? 68.23   -6.08   
2  1 TRP A 1907 ? ? -96.06  55.60   
3  1 ILE A 2029 ? ? 70.98   -56.35  
4  1 GLU A 2039 ? ? 53.30   -126.57 
5  1 THR A 2096 ? ? 67.52   -64.32  
6  1 LYS A 2142 ? ? 57.64   -115.70 
7  1 LEU A 2143 ? ? 53.06   75.03   
8  1 GLU A 2217 ? ? -90.56  59.61   
9  1 LEU A 2342 ? ? -93.70  48.99   
10 1 ASP A 2357 ? ? 58.55   70.06   
11 1 MET A 2368 ? ? 58.30   11.27   
12 1 TYR A 2391 ? ? -98.53  37.38   
13 1 CYS A 2527 ? ? 67.48   156.86  
14 1 HIS A 2539 ? ? 72.81   -12.53  
15 1 ASP A 2540 ? ? -144.00 -2.72   
16 1 ALA A 2565 ? ? -69.56  -172.64 
# 
_space_group_symop.id              1 
_space_group_symop.operation_xyz   x,y,z 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9AU5 
_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                    9AU5 
_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                  3.11 
_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               231192 
_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               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 
'Ternary complex of human DNA polymerase theta polymerase domain with a cognate C:G base pair' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       '1, 2, 3' 
# 
_em_imaging.entry_id                        9AU5 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS 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             800 
_em_imaging.nominal_defocus_max             2000 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_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    ? 
_em_sample_support.grid_mesh_size   ? 
_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              9AU5 
_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            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9AU5 
_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 A GLY 1792 ? A GLY 1   
2   1 Y 1 A PHE 1793 ? A PHE 2   
3   1 Y 1 A LYS 1794 ? A LYS 3   
4   1 Y 1 A ASP 1795 ? A ASP 4   
5   1 Y 1 A ASN 1796 ? A ASN 5   
6   1 Y 1 A SER 1797 ? A SER 6   
7   1 Y 1 A PRO 1798 ? A PRO 7   
8   1 Y 1 A ILE 1799 ? A ILE 8   
9   1 Y 1 A SER 1800 ? A SER 9   
10  1 Y 1 A ASP 1801 ? A ASP 10  
11  1 Y 1 A THR 1802 ? A THR 11  
12  1 Y 1 A SER 1803 ? A SER 12  
13  1 Y 1 A PHE 1804 ? A PHE 13  
14  1 Y 1 A SER 1805 ? A SER 14  
15  1 Y 1 A LEU 1806 ? A LEU 15  
16  1 Y 1 A GLN 1807 ? A GLN 16  
17  1 Y 1 A LEU 1808 ? A LEU 17  
18  1 Y 1 A SER 1809 ? A SER 18  
19  1 Y 1 A GLN 1810 ? A GLN 19  
20  1 Y 1 A ASP 1811 ? A ASP 20  
21  1 Y 1 A GLY 1812 ? A GLY 21  
22  1 Y 1 A LEU 1813 ? A LEU 22  
23  1 Y 1 A GLN 1814 ? A GLN 23  
24  1 Y 1 A LEU 1815 ? A LEU 24  
25  1 Y 1 A THR 1816 ? A THR 25  
26  1 Y 1 A PRO 1817 ? A PRO 26  
27  1 Y 1 A ALA 1818 ? A ALA 27  
28  1 Y 1 A SER 1819 ? A SER 28  
29  1 Y 1 A SER 1820 ? A SER 29  
30  1 Y 1 A SER 1821 ? A SER 30  
31  1 Y 1 A SER 1822 ? A SER 31  
32  1 Y 1 A GLU 1823 ? A GLU 32  
33  1 Y 1 A LEU 1862 ? A LEU 71  
34  1 Y 1 A THR 1863 ? A THR 72  
35  1 Y 1 A SER 1864 ? A SER 73  
36  1 Y 1 A SER 1865 ? A SER 74  
37  1 Y 1 A LYS 1866 ? A LYS 75  
38  1 Y 1 A THR 1867 ? A THR 76  
39  1 Y 1 A ALA 1868 ? A ALA 77  
40  1 Y 1 A THR 1869 ? A THR 78  
41  1 Y 1 A ILE 1870 ? A ILE 79  
42  1 Y 1 A GLY 1871 ? A GLY 80  
43  1 Y 1 A SER 1872 ? A SER 81  
44  1 Y 1 A ARG 1873 ? A ARG 82  
45  1 Y 1 A PHE 1874 ? A PHE 83  
46  1 Y 1 A LYS 1875 ? A LYS 84  
47  1 Y 1 A GLN 1876 ? A GLN 85  
48  1 Y 1 A ALA 1877 ? A ALA 86  
49  1 Y 1 A SER 1878 ? A SER 87  
50  1 Y 1 A SER 1879 ? A SER 88  
51  1 Y 1 A PRO 1880 ? A PRO 89  
52  1 Y 1 A GLN 1881 ? A GLN 90  
53  1 Y 1 A GLU 1882 ? A GLU 91  
54  1 Y 1 A ILE 1883 ? A ILE 92  
55  1 Y 1 A PRO 1884 ? A PRO 93  
56  1 Y 1 A GLN 1921 ? A GLN 130 
57  1 Y 1 A LYS 1922 ? A LYS 131 
58  1 Y 1 A HIS 1923 ? A HIS 132 
59  1 Y 1 A SER 1924 ? A SER 133 
60  1 Y 1 A GLU 1925 ? A GLU 134 
61  1 Y 1 A ILE 1926 ? A ILE 135 
62  1 Y 1 A SER 1927 ? A SER 136 
63  1 Y 1 A ALA 1928 ? A ALA 137 
64  1 Y 1 A SER 1929 ? A SER 138 
65  1 Y 1 A LEU 1930 ? A LEU 139 
66  1 Y 1 A VAL 1931 ? A VAL 140 
67  1 Y 1 A PRO 1932 ? A PRO 141 
68  1 Y 1 A PRO 1933 ? A PRO 142 
69  1 Y 1 A SER 1934 ? A SER 143 
70  1 Y 1 A LEU 1935 ? A LEU 144 
71  1 Y 1 A GLU 2148 ? A GLU 357 
72  1 Y 1 A MET 2149 ? A MET 358 
73  1 Y 1 A LYS 2150 ? A LYS 359 
74  1 Y 1 A ASN 2151 ? A ASN 360 
75  1 Y 1 A GLN 2152 ? A GLN 361 
76  1 Y 1 A GLY 2153 ? A GLY 362 
77  1 Y 1 A SER 2154 ? A SER 363 
78  1 Y 1 A LYS 2155 ? A LYS 364 
79  1 Y 1 A LYS 2156 ? A LYS 365 
80  1 Y 1 A THR 2157 ? A THR 366 
81  1 Y 1 A LEU 2158 ? A LEU 367 
82  1 Y 1 A GLY 2159 ? A GLY 368 
83  1 Y 1 A SER 2160 ? A SER 369 
84  1 Y 1 A THR 2161 ? A THR 370 
85  1 Y 1 A ARG 2162 ? A ARG 371 
86  1 Y 1 A ARG 2163 ? A ARG 372 
87  1 Y 1 A GLY 2164 ? A GLY 373 
88  1 Y 1 A ILE 2165 ? A ILE 374 
89  1 Y 1 A ASP 2166 ? A ASP 375 
90  1 Y 1 A ASN 2167 ? A ASN 376 
91  1 Y 1 A GLY 2168 ? A GLY 377 
92  1 Y 1 A ARG 2169 ? A ARG 378 
93  1 Y 1 A LYS 2170 ? A LYS 379 
94  1 Y 1 A LEU 2171 ? A LEU 380 
95  1 Y 1 A ARG 2172 ? A ARG 381 
96  1 Y 1 A LEU 2173 ? A LEU 382 
97  1 Y 1 A LEU 2263 ? A LEU 472 
98  1 Y 1 A VAL 2264 ? A VAL 473 
99  1 Y 1 A GLY 2265 ? A GLY 474 
100 1 Y 1 A GLU 2266 ? A GLU 475 
101 1 Y 1 A SER 2267 ? A SER 476 
102 1 Y 1 A PRO 2268 ? A PRO 477 
103 1 Y 1 A PRO 2269 ? A PRO 478 
104 1 Y 1 A SER 2270 ? A SER 479 
105 1 Y 1 A GLN 2271 ? A GLN 480 
106 1 Y 1 A ALA 2272 ? A ALA 481 
107 1 Y 1 A VAL 2273 ? A VAL 482 
108 1 Y 1 A GLY 2274 ? A GLY 483 
109 1 Y 1 A LYS 2275 ? A LYS 484 
110 1 Y 1 A GLY 2276 ? A GLY 485 
111 1 Y 1 A LEU 2277 ? A LEU 486 
112 1 Y 1 A LEU 2278 ? A LEU 487 
113 1 Y 1 A PRO 2279 ? A PRO 488 
114 1 Y 1 A MET 2280 ? A MET 489 
115 1 Y 1 A GLY 2281 ? A GLY 490 
116 1 Y 1 A ARG 2282 ? A ARG 491 
117 1 Y 1 A GLY 2283 ? A GLY 492 
118 1 Y 1 A LYS 2284 ? A LYS 493 
119 1 Y 1 A TYR 2285 ? A TYR 494 
120 1 Y 1 A LYS 2286 ? A LYS 495 
121 1 Y 1 A LYS 2287 ? A LYS 496 
122 1 Y 1 A GLY 2288 ? A GLY 497 
123 1 Y 1 A PHE 2289 ? A PHE 498 
124 1 Y 1 A SER 2290 ? A SER 499 
125 1 Y 1 A VAL 2291 ? A VAL 500 
126 1 Y 1 A ASN 2292 ? A ASN 501 
127 1 Y 1 A PRO 2293 ? A PRO 502 
128 1 Y 1 A ARG 2294 ? A ARG 503 
129 1 Y 1 A CYS 2295 ? A CYS 504 
130 1 Y 1 A GLN 2296 ? A GLN 505 
131 1 Y 1 A ALA 2297 ? A ALA 506 
132 1 Y 1 A GLN 2298 ? A GLN 507 
133 1 Y 1 A MET 2299 ? A MET 508 
134 1 Y 1 A GLU 2300 ? A GLU 509 
135 1 Y 1 A GLU 2301 ? A GLU 510 
136 1 Y 1 A ARG 2302 ? A ARG 511 
137 1 Y 1 A ALA 2303 ? A ALA 512 
138 1 Y 1 A ALA 2304 ? A ALA 513 
139 1 Y 1 A ASP 2305 ? A ASP 514 
140 1 Y 1 A ARG 2306 ? A ARG 515 
141 1 Y 1 A GLY 2307 ? A GLY 516 
142 1 Y 1 A LEU 2509 ? A LEU 718 
143 1 Y 1 A GLN 2510 ? A GLN 719 
144 1 Y 1 A SER 2511 ? A SER 720 
145 1 Y 1 A ASP 2512 ? A ASP 721 
146 1 Y 1 A GLN 2513 ? A GLN 722 
147 1 Y 1 A THR 2514 ? A THR 723 
148 1 Y 1 A GLY 2515 ? A GLY 724 
149 1 Y 1 A LEU 2516 ? A LEU 725 
150 1 Y 1 A SER 2517 ? A SER 726 
151 1 Y 1 A ARG 2518 ? A ARG 727 
152 1 Y 1 A LYS 2519 ? A LYS 728 
153 1 Y 1 A ARG 2520 ? A ARG 729 
154 1 Y 1 A LYS 2521 ? A LYS 730 
155 1 Y 1 A LEU 2522 ? A LEU 731 
156 1 Y 1 A GLN 2523 ? A GLN 732 
157 1 Y 1 A GLY 2524 ? A GLY 733 
158 1 Y 1 A MET 2525 ? A MET 734 
159 1 Y 1 E DG  1    ? B DG  1   
160 1 Y 1 E DC  2    ? B DC  2   
161 1 Y 1 E DA  3    ? B DA  3   
162 1 Y 1 E DG  4    ? B DG  4   
163 1 Y 1 E DT  5    ? B DT  5   
164 1 Y 1 E DC  6    ? B DC  6   
165 1 Y 1 E DC  21   ? B DC  21  
166 1 Y 1 E DT  22   ? B DT  22  
167 1 Y 1 E DC  23   ? B DC  23  
168 1 Y 1 E DA  24   ? B DA  24  
169 1 Y 1 E DC  25   ? B DC  25  
170 1 Y 1 E DA  26   ? B DA  26  
171 1 Y 1 E DG  27   ? B DG  27  
172 1 Y 1 E DC  28   ? B DC  28  
173 1 Y 1 E DA  29   ? B DA  29  
174 1 Y 1 F DT  1    ? C DT  1   
175 1 Y 1 F DG  2    ? C DG  2   
176 1 Y 1 F DC  3    ? C DC  3   
177 1 Y 1 F DT  4    ? C DT  4   
178 1 Y 1 F DG  5    ? C DG  5   
179 1 Y 1 F DT  6    ? C DT  6   
180 1 Y 1 F DG  7    ? C DG  7   
181 1 Y 1 F DA  8    ? C DA  8   
182 1 Y 1 F DG  9    ? C DG  9   
# 
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    2024-02-28 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9AU5 
_em_admin.last_update        2025-03-12 
_em_admin.map_release_date   2025-03-05 
_em_admin.title              'Ternary complex of human DNA polymerase theta polymerase domain with a cognate C:G base pair' 
# 
_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          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_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               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         1.2 
_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 ? ? ?      ?            
'MODEL REFINEMENT'         ? 2  ? ? ? PHENIX 1.21.2_5419: 
'IMAGE ACQUISITION'        ? 3  1 ? 1 ?      ?            
MASKING                    ? 4  1 1 1 ?      ?            
'CTF CORRECTION'           ? 5  1 ? ? ?      ?            
'LAYERLINE INDEXING'       ? 6  1 1 1 ?      ?            
'DIFFRACTION INDEXING'     ? 7  1 1 1 ?      ?            
'MODEL FITTING'            ? 8  1 1 1 ?      ?            
OTHER                      ? 9  1 1 1 ?      ?            
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ?      ?            
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? ?      ?            
CLASSIFICATION             ? 12 1 ? ? ?      ?            
RECONSTRUCTION             ? 13 1 ? ? ?      ?            
# 
_em_specimen.concentration           0.7 
_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 
9AU5 'double helix'        
9AU5 'a-form double helix' 
9AU5 'b-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 B DT 10 1_555 C 2DA 20 1_555 -0.109 -0.404 0.641  -6.776 -5.791  -3.443 1  E_DT10:2DA20_F E 10 ? F 20 ? 20 1 
1 B DC 11 1_555 C DG  19 1_555 0.187  -0.177 0.264  -3.889 -0.856  -0.600 2  E_DC11:DG19_F  E 11 ? F 19 ? 19 1 
1 B DT 12 1_555 C DA  18 1_555 -0.111 -0.169 0.482  -1.820 0.136   1.281  3  E_DT12:DA18_F  E 12 ? F 18 ? 20 1 
1 B DA 13 1_555 C DT  17 1_555 0.105  -0.193 0.778  3.722  0.105   -1.923 4  E_DA13:DT17_F  E 13 ? F 17 ? 20 1 
1 B DC 14 1_555 C DG  16 1_555 0.222  -0.262 0.797  4.982  1.392   1.420  5  E_DC14:DG16_F  E 14 ? F 16 ? 19 1 
1 B DG 15 1_555 C DC  15 1_555 -0.161 -0.202 0.725  6.777  -4.035  -2.444 6  E_DG15:DC15_F  E 15 ? F 15 ? 19 1 
1 B DG 16 1_555 C DC  14 1_555 -0.168 -0.197 0.478  1.803  -7.531  -1.736 7  E_DG16:DC14_F  E 16 ? F 14 ? 19 1 
1 B DA 17 1_555 C DT  13 1_555 0.105  -0.069 0.210  -5.254 -7.170  -3.389 8  E_DA17:DT13_F  E 17 ? F 13 ? 20 1 
1 B DT 18 1_555 C DA  12 1_555 -0.138 -0.106 0.248  -4.883 -6.392  -2.578 9  E_DT18:DA12_F  E 18 ? F 12 ? 20 1 
1 B DG 19 1_555 C DC  11 1_555 -0.265 -0.160 -0.135 -5.233 -12.397 1.306  10 E_DG19:DC11_F  E 19 ? F 11 ? 19 1 
1 B DC 20 1_555 C DG  10 1_555 0.217  -0.188 -0.490 -6.597 -7.913  1.329  11 E_DC20:DG10_F  E 20 ? F 10 ? 19 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 B DT 10 1_555 C 2DA 20 1_555 B DC 11 1_555 C DG 19 1_555 -0.416 -1.422 3.224 -1.596 7.521  35.518 -3.274 0.457  2.888 12.153 
2.579  36.315 1  EE_DT10DC11:DG192DA20_FF E 10 ? F 20 ? E 11 ? F 19 ? 
1 B DC 11 1_555 C DG  19 1_555 B DT 12 1_555 C DA 18 1_555 0.294  -1.221 3.377 -0.576 5.328  27.847 -3.719 -0.732 3.088 10.943 
1.182  28.348 2  EE_DC11DT12:DA18DG19_FF  E 11 ? F 19 ? E 12 ? F 18 ? 
1 B DT 12 1_555 C DA  18 1_555 B DA 13 1_555 C DT 17 1_555 -0.326 -0.855 3.062 -0.153 8.538  32.566 -2.739 0.540  2.758 14.908 
0.268  33.637 3  EE_DT12DA13:DT17DA18_FF  E 12 ? F 18 ? E 13 ? F 17 ? 
1 B DA 13 1_555 C DT  17 1_555 B DC 14 1_555 C DG 16 1_555 0.461  -0.915 3.413 1.618  1.305  33.111 -1.831 -0.525 3.394 2.287  
-2.836 33.175 4  EE_DA13DC14:DG16DT17_FF  E 13 ? F 17 ? E 14 ? F 16 ? 
1 B DC 14 1_555 C DG  16 1_555 B DG 15 1_555 C DC 15 1_555 -0.692 0.430  3.201 -1.126 1.835  34.831 0.444  0.985  3.239 3.062  
1.878  34.896 5  EE_DC14DG15:DC15DG16_FF  E 14 ? F 16 ? E 15 ? F 15 ? 
1 B DG 15 1_555 C DC  15 1_555 B DG 16 1_555 C DC 14 1_555 -0.412 -0.331 3.224 0.188  0.337  34.731 -0.606 0.718  3.219 0.565  
-0.315 34.733 6  EE_DG15DG16:DC14DC15_FF  E 15 ? F 15 ? E 16 ? F 14 ? 
1 B DG 16 1_555 C DC  14 1_555 B DA 17 1_555 C DT 13 1_555 -0.144 -0.452 3.285 -0.025 -0.311 43.703 -0.577 0.191  3.288 -0.417 
0.034  43.704 7  EE_DG16DA17:DT13DC14_FF  E 16 ? F 14 ? E 17 ? F 13 ? 
1 B DA 17 1_555 C DT  13 1_555 B DT 18 1_555 C DA 12 1_555 -0.400 -0.402 3.203 -1.077 -0.696 25.391 -0.716 0.603  3.227 -1.582 
2.449  25.423 8  EE_DA17DT18:DA12DT13_FF  E 17 ? F 13 ? E 18 ? F 12 ? 
1 B DT 18 1_555 C DA  12 1_555 B DG 19 1_555 C DC 11 1_555 -0.263 -0.509 3.048 -1.308 10.722 32.789 -2.376 0.259  2.759 18.382 
2.243  34.476 9  EE_DT18DG19:DC11DA12_FF  E 18 ? F 12 ? E 19 ? F 11 ? 
1 B DG 19 1_555 C DC  11 1_555 B DC 20 1_555 C DG 10 1_555 -1.078 3.532  3.248 -2.003 -2.291 42.906 5.037  1.278  3.109 -3.127 
2.735  43.009 10 EE_DG19DC20:DG10DC11_FF  E 19 ? F 11 ? E 20 ? F 10 ? 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'American Cancer Society'                                   'United States' 'RSG-22-082-517 01-DMC' 1 
'Cancer Prevention and Research Institute of Texas (CPRIT)' 'United States' RR190046                2 
# 
_space_group.crystal_system   triclinic 
_space_group.name_H-M_alt     'P 1' 
_space_group.IT_number        1 
_space_group.name_Hall        'P 1' 
_space_group.id               1 
# 
_atom_sites.entry_id                    9AU5 
_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    N  N     . SER A 1 33  ? 90.204  121.462 140.490 1.00 84.51  ? 1824 SER A N     1 
ATOM   2    C  CA    . SER A 1 33  ? 91.026  121.910 139.372 1.00 89.97  ? 1824 SER A CA    1 
ATOM   3    C  C     . SER A 1 33  ? 92.356  121.165 139.340 1.00 89.73  ? 1824 SER A C     1 
ATOM   4    O  O     . SER A 1 33  ? 92.406  119.958 139.571 1.00 87.08  ? 1824 SER A O     1 
ATOM   5    C  CB    . SER A 1 33  ? 91.267  123.419 139.455 1.00 87.64  ? 1824 SER A CB    1 
ATOM   6    O  OG    . SER A 1 33  ? 91.824  123.779 140.707 1.00 84.70  ? 1824 SER A OG    1 
ATOM   7    N  N     . LEU A 1 34  ? 93.429  121.894 139.046 1.00 89.19  ? 1825 LEU A N     1 
ATOM   8    C  CA    . LEU A 1 34  ? 94.757  121.297 139.020 1.00 84.47  ? 1825 LEU A CA    1 
ATOM   9    C  C     . LEU A 1 34  ? 95.171  120.847 140.416 1.00 82.04  ? 1825 LEU A C     1 
ATOM   10   O  O     . LEU A 1 34  ? 94.890  121.517 141.414 1.00 86.26  ? 1825 LEU A O     1 
ATOM   11   C  CB    . LEU A 1 34  ? 95.772  122.292 138.453 1.00 82.36  ? 1825 LEU A CB    1 
ATOM   12   C  CG    . LEU A 1 34  ? 95.997  123.620 139.186 1.00 81.61  ? 1825 LEU A CG    1 
ATOM   13   C  CD1   . LEU A 1 34  ? 97.168  123.540 140.160 1.00 80.72  ? 1825 LEU A CD1   1 
ATOM   14   C  CD2   . LEU A 1 34  ? 96.202  124.752 138.191 1.00 76.33  ? 1825 LEU A CD2   1 
ATOM   15   N  N     . SER A 1 35  ? 95.839  119.695 140.482 1.00 73.93  ? 1826 SER A N     1 
ATOM   16   C  CA    . SER A 1 35  ? 96.304  119.149 141.756 1.00 70.51  ? 1826 SER A CA    1 
ATOM   17   C  C     . SER A 1 35  ? 97.585  118.370 141.477 1.00 66.57  ? 1826 SER A C     1 
ATOM   18   O  O     . SER A 1 35  ? 97.532  117.246 140.968 1.00 67.19  ? 1826 SER A O     1 
ATOM   19   C  CB    . SER A 1 35  ? 95.242  118.269 142.401 1.00 71.20  ? 1826 SER A CB    1 
ATOM   20   O  OG    . SER A 1 35  ? 95.704  117.730 143.627 1.00 72.24  ? 1826 SER A OG    1 
ATOM   21   N  N     . ILE A 1 36  ? 98.724  118.968 141.813 1.00 63.24  ? 1827 ILE A N     1 
ATOM   22   C  CA    . ILE A 1 36  ? 100.035 118.383 141.563 1.00 58.60  ? 1827 ILE A CA    1 
ATOM   23   C  C     . ILE A 1 36  ? 100.696 118.101 142.903 1.00 62.44  ? 1827 ILE A C     1 
ATOM   24   O  O     . ILE A 1 36  ? 100.804 118.996 143.750 1.00 65.55  ? 1827 ILE A O     1 
ATOM   25   C  CB    . ILE A 1 36  ? 100.911 119.309 140.703 1.00 58.98  ? 1827 ILE A CB    1 
ATOM   26   C  CG1   . ILE A 1 36  ? 100.272 119.525 139.330 1.00 55.38  ? 1827 ILE A CG1   1 
ATOM   27   C  CG2   . ILE A 1 36  ? 102.303 118.727 140.550 1.00 59.21  ? 1827 ILE A CG2   1 
ATOM   28   C  CD1   . ILE A 1 36  ? 99.456  120.790 139.215 1.00 64.71  ? 1827 ILE A CD1   1 
ATOM   29   N  N     . ILE A 1 37  ? 101.139 116.862 143.093 1.00 62.28  ? 1828 ILE A N     1 
ATOM   30   C  CA    . ILE A 1 37  ? 101.746 116.419 144.342 1.00 65.91  ? 1828 ILE A CA    1 
ATOM   31   C  C     . ILE A 1 37  ? 103.220 116.146 144.082 1.00 66.63  ? 1828 ILE A C     1 
ATOM   32   O  O     . ILE A 1 37  ? 103.565 115.304 143.244 1.00 62.00  ? 1828 ILE A O     1 
ATOM   33   C  CB    . ILE A 1 37  ? 101.045 115.173 144.903 1.00 60.01  ? 1828 ILE A CB    1 
ATOM   34   C  CG1   . ILE A 1 37  ? 99.702  115.553 145.531 1.00 59.66  ? 1828 ILE A CG1   1 
ATOM   35   C  CG2   . ILE A 1 37  ? 101.930 114.474 145.923 1.00 64.31  ? 1828 ILE A CG2   1 
ATOM   36   C  CD1   . ILE A 1 37  ? 98.545  115.538 144.561 1.00 60.83  ? 1828 ILE A CD1   1 
ATOM   37   N  N     . ASP A 1 38  ? 104.088 116.851 144.801 1.00 74.15  ? 1829 ASP A N     1 
ATOM   38   C  CA    . ASP A 1 38  ? 105.530 116.650 144.686 1.00 72.07  ? 1829 ASP A CA    1 
ATOM   39   C  C     . ASP A 1 38  ? 105.915 115.462 145.555 1.00 77.90  ? 1829 ASP A C     1 
ATOM   40   O  O     . ASP A 1 38  ? 106.059 115.586 146.773 1.00 83.77  ? 1829 ASP A O     1 
ATOM   41   C  CB    . ASP A 1 38  ? 106.284 117.908 145.099 1.00 73.71  ? 1829 ASP A CB    1 
ATOM   42   C  CG    . ASP A 1 38  ? 106.303 118.958 144.010 1.00 73.93  ? 1829 ASP A CG    1 
ATOM   43   O  OD1   . ASP A 1 38  ? 106.435 118.584 142.827 1.00 72.71  ? 1829 ASP A OD1   1 
ATOM   44   O  OD2   . ASP A 1 38  ? 106.184 120.158 144.337 1.00 75.41  ? 1829 ASP A OD2   1 
ATOM   45   N  N     . VAL A 1 39  ? 106.087 114.295 144.925 1.00 72.79  ? 1830 VAL A N     1 
ATOM   46   C  CA    . VAL A 1 39  ? 106.428 113.081 145.664 1.00 79.31  ? 1830 VAL A CA    1 
ATOM   47   C  C     . VAL A 1 39  ? 107.905 112.996 146.006 1.00 87.08  ? 1830 VAL A C     1 
ATOM   48   O  O     . VAL A 1 39  ? 108.317 112.050 146.687 1.00 90.40  ? 1830 VAL A O     1 
ATOM   49   C  CB    . VAL A 1 39  ? 106.017 111.825 144.872 1.00 73.64  ? 1830 VAL A CB    1 
ATOM   50   C  CG1   . VAL A 1 39  ? 104.607 111.983 144.333 1.00 65.80  ? 1830 VAL A CG1   1 
ATOM   51   C  CG2   . VAL A 1 39  ? 106.997 111.567 143.741 1.00 69.70  ? 1830 VAL A CG2   1 
ATOM   52   N  N     . ALA A 1 40  ? 108.714 113.954 145.560 1.00 86.53  ? 1831 ALA A N     1 
ATOM   53   C  CA    . ALA A 1 40  ? 110.143 113.958 145.835 1.00 88.16  ? 1831 ALA A CA    1 
ATOM   54   C  C     . ALA A 1 40  ? 110.527 114.934 146.940 1.00 92.91  ? 1831 ALA A C     1 
ATOM   55   O  O     . ALA A 1 40  ? 111.716 115.217 147.116 1.00 96.87  ? 1831 ALA A O     1 
ATOM   56   C  CB    . ALA A 1 40  ? 110.921 114.280 144.559 1.00 82.68  ? 1831 ALA A CB    1 
ATOM   57   N  N     . SER A 1 41  ? 109.552 115.455 147.684 1.00 91.97  ? 1832 SER A N     1 
ATOM   58   C  CA    . SER A 1 41  ? 109.809 116.431 148.736 1.00 95.01  ? 1832 SER A CA    1 
ATOM   59   C  C     . SER A 1 41  ? 109.809 115.824 150.132 1.00 99.54  ? 1832 SER A C     1 
ATOM   60   O  O     . SER A 1 41  ? 110.619 116.224 150.974 1.00 99.91  ? 1832 SER A O     1 
ATOM   61   C  CB    . SER A 1 41  ? 108.773 117.557 148.674 1.00 93.16  ? 1832 SER A CB    1 
ATOM   62   O  OG    . SER A 1 41  ? 107.459 117.047 148.815 1.00 93.41  ? 1832 SER A OG    1 
ATOM   63   N  N     . ASP A 1 42  ? 108.921 114.872 150.401 1.00 98.00  ? 1833 ASP A N     1 
ATOM   64   C  CA    . ASP A 1 42  ? 108.807 114.244 151.709 1.00 98.34  ? 1833 ASP A CA    1 
ATOM   65   C  C     . ASP A 1 42  ? 109.016 112.742 151.579 1.00 98.69  ? 1833 ASP A C     1 
ATOM   66   O  O     . ASP A 1 42  ? 108.546 112.123 150.620 1.00 95.79  ? 1833 ASP A O     1 
ATOM   67   C  CB    . ASP A 1 42  ? 107.443 114.534 152.345 1.00 96.47  ? 1833 ASP A CB    1 
ATOM   68   C  CG    . ASP A 1 42  ? 107.322 113.972 153.747 1.00 96.88  ? 1833 ASP A CG    1 
ATOM   69   O  OD1   . ASP A 1 42  ? 107.996 114.496 154.659 1.00 98.71  ? 1833 ASP A OD1   1 
ATOM   70   O  OD2   . ASP A 1 42  ? 106.552 113.009 153.938 1.00 95.80  ? 1833 ASP A OD2   1 
ATOM   71   N  N     . GLN A 1 43  ? 109.732 112.164 152.546 1.00 99.93  ? 1834 GLN A N     1 
ATOM   72   C  CA    . GLN A 1 43  ? 110.022 110.734 152.505 1.00 97.08  ? 1834 GLN A CA    1 
ATOM   73   C  C     . GLN A 1 43  ? 108.753 109.905 152.666 1.00 92.23  ? 1834 GLN A C     1 
ATOM   74   O  O     . GLN A 1 43  ? 108.530 108.941 151.924 1.00 89.60  ? 1834 GLN A O     1 
ATOM   75   C  CB    . GLN A 1 43  ? 111.039 110.378 153.589 1.00 98.72  ? 1834 GLN A CB    1 
ATOM   76   C  CG    . GLN A 1 43  ? 111.565 108.955 153.506 1.00 100.40 ? 1834 GLN A CG    1 
ATOM   77   C  CD    . GLN A 1 43  ? 112.724 108.821 152.540 1.00 101.03 ? 1834 GLN A CD    1 
ATOM   78   O  OE1   . GLN A 1 43  ? 113.381 109.804 152.201 1.00 100.78 ? 1834 GLN A OE1   1 
ATOM   79   N  NE2   . GLN A 1 43  ? 112.982 107.598 152.092 1.00 98.79  ? 1834 GLN A NE2   1 
ATOM   80   N  N     . ASN A 1 44  ? 107.911 110.260 153.641 1.00 94.23  ? 1835 ASN A N     1 
ATOM   81   C  CA    . ASN A 1 44  ? 106.663 109.529 153.842 1.00 94.57  ? 1835 ASN A CA    1 
ATOM   82   C  C     . ASN A 1 44  ? 105.743 109.670 152.637 1.00 91.41  ? 1835 ASN A C     1 
ATOM   83   O  O     . ASN A 1 44  ? 105.105 108.697 152.214 1.00 89.85  ? 1835 ASN A O     1 
ATOM   84   C  CB    . ASN A 1 44  ? 105.967 110.017 155.112 1.00 93.47  ? 1835 ASN A CB    1 
ATOM   85   C  CG    . ASN A 1 44  ? 104.566 109.457 155.262 1.00 93.62  ? 1835 ASN A CG    1 
ATOM   86   O  OD1   . ASN A 1 44  ? 103.586 110.092 154.872 1.00 95.04  ? 1835 ASN A OD1   1 
ATOM   87   N  ND2   . ASN A 1 44  ? 104.464 108.260 155.828 1.00 90.58  ? 1835 ASN A ND2   1 
ATOM   88   N  N     . LEU A 1 45  ? 105.662 110.876 152.071 1.00 90.60  ? 1836 LEU A N     1 
ATOM   89   C  CA    . LEU A 1 45  ? 104.868 111.074 150.864 1.00 91.12  ? 1836 LEU A CA    1 
ATOM   90   C  C     . LEU A 1 45  ? 105.421 110.255 149.706 1.00 91.46  ? 1836 LEU A C     1 
ATOM   91   O  O     . LEU A 1 45  ? 104.658 109.689 148.917 1.00 90.62  ? 1836 LEU A O     1 
ATOM   92   C  CB    . LEU A 1 45  ? 104.824 112.558 150.501 1.00 92.00  ? 1836 LEU A CB    1 
ATOM   93   C  CG    . LEU A 1 45  ? 104.019 112.939 149.257 1.00 87.54  ? 1836 LEU A CG    1 
ATOM   94   C  CD1   . LEU A 1 45  ? 102.620 112.343 149.311 1.00 85.33  ? 1836 LEU A CD1   1 
ATOM   95   C  CD2   . LEU A 1 45  ? 103.955 114.451 149.108 1.00 81.97  ? 1836 LEU A CD2   1 
ATOM   96   N  N     . PHE A 1 46  ? 106.749 110.181 149.589 1.00 90.70  ? 1837 PHE A N     1 
ATOM   97   C  CA    . PHE A 1 46  ? 107.355 109.374 148.535 1.00 88.13  ? 1837 PHE A CA    1 
ATOM   98   C  C     . PHE A 1 46  ? 107.014 107.900 148.701 1.00 86.22  ? 1837 PHE A C     1 
ATOM   99   O  O     . PHE A 1 46  ? 106.692 107.216 147.723 1.00 82.54  ? 1837 PHE A O     1 
ATOM   100  C  CB    . PHE A 1 46  ? 108.870 109.570 148.530 1.00 88.84  ? 1837 PHE A CB    1 
ATOM   101  C  CG    . PHE A 1 46  ? 109.573 108.815 147.442 1.00 86.62  ? 1837 PHE A CG    1 
ATOM   102  C  CD1   . PHE A 1 46  ? 109.232 109.012 146.115 1.00 84.89  ? 1837 PHE A CD1   1 
ATOM   103  C  CD2   . PHE A 1 46  ? 110.571 107.907 147.744 1.00 86.92  ? 1837 PHE A CD2   1 
ATOM   104  C  CE1   . PHE A 1 46  ? 109.875 108.318 145.110 1.00 81.83  ? 1837 PHE A CE1   1 
ATOM   105  C  CE2   . PHE A 1 46  ? 111.219 107.210 146.742 1.00 88.98  ? 1837 PHE A CE2   1 
ATOM   106  C  CZ    . PHE A 1 46  ? 110.870 107.416 145.424 1.00 86.40  ? 1837 PHE A CZ    1 
ATOM   107  N  N     . GLN A 1 47  ? 107.084 107.390 149.933 1.00 88.14  ? 1838 GLN A N     1 
ATOM   108  C  CA    . GLN A 1 47  ? 106.755 105.988 150.167 1.00 84.30  ? 1838 GLN A CA    1 
ATOM   109  C  C     . GLN A 1 47  ? 105.284 105.710 149.884 1.00 82.13  ? 1838 GLN A C     1 
ATOM   110  O  O     . GLN A 1 47  ? 104.944 104.669 149.310 1.00 80.66  ? 1838 GLN A O     1 
ATOM   111  C  CB    . GLN A 1 47  ? 107.116 105.594 151.598 1.00 86.94  ? 1838 GLN A CB    1 
ATOM   112  C  CG    . GLN A 1 47  ? 108.601 105.689 151.909 1.00 90.41  ? 1838 GLN A CG    1 
ATOM   113  C  CD    . GLN A 1 47  ? 109.448 104.827 150.992 1.00 88.26  ? 1838 GLN A CD    1 
ATOM   114  O  OE1   . GLN A 1 47  ? 109.049 103.727 150.610 1.00 87.30  ? 1838 GLN A OE1   1 
ATOM   115  N  NE2   . GLN A 1 47  ? 110.626 105.325 150.634 1.00 87.06  ? 1838 GLN A NE2   1 
ATOM   116  N  N     . THR A 1 48  ? 104.397 106.626 150.283 1.00 83.97  ? 1839 THR A N     1 
ATOM   117  C  CA    . THR A 1 48  ? 102.978 106.456 149.983 1.00 83.67  ? 1839 THR A CA    1 
ATOM   118  C  C     . THR A 1 48  ? 102.728 106.471 148.479 1.00 83.27  ? 1839 THR A C     1 
ATOM   119  O  O     . THR A 1 48  ? 101.931 105.675 147.965 1.00 81.81  ? 1839 THR A O     1 
ATOM   120  C  CB    . THR A 1 48  ? 102.160 107.547 150.673 1.00 85.55  ? 1839 THR A CB    1 
ATOM   121  O  OG1   . THR A 1 48  ? 102.478 107.574 152.070 1.00 88.07  ? 1839 THR A OG1   1 
ATOM   122  C  CG2   . THR A 1 48  ? 100.671 107.285 150.504 1.00 85.28  ? 1839 THR A CG2   1 
ATOM   123  N  N     . PHE A 1 49  ? 103.404 107.369 147.759 1.00 81.31  ? 1840 PHE A N     1 
ATOM   124  C  CA    . PHE A 1 49  ? 103.273 107.419 146.307 1.00 75.35  ? 1840 PHE A CA    1 
ATOM   125  C  C     . PHE A 1 49  ? 103.761 106.126 145.667 1.00 76.27  ? 1840 PHE A C     1 
ATOM   126  O  O     . PHE A 1 49  ? 103.124 105.603 144.746 1.00 73.72  ? 1840 PHE A O     1 
ATOM   127  C  CB    . PHE A 1 49  ? 104.044 108.621 145.761 1.00 72.83  ? 1840 PHE A CB    1 
ATOM   128  C  CG    . PHE A 1 49  ? 104.469 108.476 144.327 1.00 74.64  ? 1840 PHE A CG    1 
ATOM   129  C  CD1   . PHE A 1 49  ? 103.556 108.634 143.300 1.00 70.01  ? 1840 PHE A CD1   1 
ATOM   130  C  CD2   . PHE A 1 49  ? 105.787 108.195 144.006 1.00 74.91  ? 1840 PHE A CD2   1 
ATOM   131  C  CE1   . PHE A 1 49  ? 103.943 108.505 141.981 1.00 62.12  ? 1840 PHE A CE1   1 
ATOM   132  C  CE2   . PHE A 1 49  ? 106.181 108.065 142.688 1.00 66.82  ? 1840 PHE A CE2   1 
ATOM   133  C  CZ    . PHE A 1 49  ? 105.257 108.221 141.675 1.00 59.60  ? 1840 PHE A CZ    1 
ATOM   134  N  N     . ILE A 1 50  ? 104.888 105.594 146.145 1.00 77.81  ? 1841 ILE A N     1 
ATOM   135  C  CA    . ILE A 1 50  ? 105.414 104.342 145.606 1.00 74.79  ? 1841 ILE A CA    1 
ATOM   136  C  C     . ILE A 1 50  ? 104.445 103.196 145.871 1.00 74.50  ? 1841 ILE A C     1 
ATOM   137  O  O     . ILE A 1 50  ? 104.199 102.355 144.997 1.00 73.36  ? 1841 ILE A O     1 
ATOM   138  C  CB    . ILE A 1 50  ? 106.809 104.054 146.190 1.00 73.06  ? 1841 ILE A CB    1 
ATOM   139  C  CG1   . ILE A 1 50  ? 107.832 105.051 145.646 1.00 72.99  ? 1841 ILE A CG1   1 
ATOM   140  C  CG2   . ILE A 1 50  ? 107.239 102.631 145.879 1.00 73.94  ? 1841 ILE A CG2   1 
ATOM   141  C  CD1   . ILE A 1 50  ? 108.038 104.959 144.155 1.00 74.67  ? 1841 ILE A CD1   1 
ATOM   142  N  N     . LYS A 1 51  ? 103.889 103.136 147.084 1.00 75.99  ? 1842 LYS A N     1 
ATOM   143  C  CA    . LYS A 1 51  ? 102.943 102.074 147.413 1.00 76.23  ? 1842 LYS A CA    1 
ATOM   144  C  C     . LYS A 1 51  ? 101.694 102.157 146.546 1.00 74.33  ? 1842 LYS A C     1 
ATOM   145  O  O     . LYS A 1 51  ? 101.205 101.136 146.045 1.00 74.44  ? 1842 LYS A O     1 
ATOM   146  C  CB    . LYS A 1 51  ? 102.570 102.145 148.894 1.00 76.14  ? 1842 LYS A CB    1 
ATOM   147  C  CG    . LYS A 1 51  ? 103.648 101.624 149.836 1.00 76.38  ? 1842 LYS A CG    1 
ATOM   148  C  CD    . LYS A 1 51  ? 103.324 101.878 151.311 1.00 83.45  ? 1842 LYS A CD    1 
ATOM   149  C  CE    . LYS A 1 51  ? 101.826 101.866 151.628 1.00 82.41  ? 1842 LYS A CE    1 
ATOM   150  N  NZ    . LYS A 1 51  ? 101.115 100.636 151.164 1.00 81.26  ? 1842 LYS A NZ    1 
ATOM   151  N  N     . GLU A 1 52  ? 101.165 103.368 146.351 1.00 73.46  ? 1843 GLU A N     1 
ATOM   152  C  CA    . GLU A 1 52  ? 99.997  103.533 145.493 1.00 73.48  ? 1843 GLU A CA    1 
ATOM   153  C  C     . GLU A 1 52  ? 100.322 103.171 144.050 1.00 72.51  ? 1843 GLU A C     1 
ATOM   154  O  O     . GLU A 1 52  ? 99.486  102.595 143.343 1.00 72.80  ? 1843 GLU A O     1 
ATOM   155  C  CB    . GLU A 1 52  ? 99.477  104.966 145.587 1.00 75.02  ? 1843 GLU A CB    1 
ATOM   156  C  CG    . GLU A 1 52  ? 98.177  105.109 146.361 1.00 78.32  ? 1843 GLU A CG    1 
ATOM   157  C  CD    . GLU A 1 52  ? 96.964  104.702 145.547 1.00 80.97  ? 1843 GLU A CD    1 
ATOM   158  O  OE1   . GLU A 1 52  ? 97.093  104.564 144.313 1.00 76.92  ? 1843 GLU A OE1   1 
ATOM   159  O  OE2   . GLU A 1 52  ? 95.881  104.522 146.142 1.00 83.63  ? 1843 GLU A OE2   1 
ATOM   160  N  N     . TRP A 1 53  ? 101.530 103.509 143.592 1.00 71.09  ? 1844 TRP A N     1 
ATOM   161  C  CA    . TRP A 1 53  ? 101.943 103.155 142.239 1.00 67.98  ? 1844 TRP A CA    1 
ATOM   162  C  C     . TRP A 1 53  ? 102.004 101.645 142.058 1.00 68.75  ? 1844 TRP A C     1 
ATOM   163  O  O     . TRP A 1 53  ? 101.527 101.112 141.049 1.00 67.76  ? 1844 TRP A O     1 
ATOM   164  C  CB    . TRP A 1 53  ? 103.301 103.784 141.934 1.00 66.73  ? 1844 TRP A CB    1 
ATOM   165  C  CG    . TRP A 1 53  ? 103.478 104.163 140.505 1.00 62.67  ? 1844 TRP A CG    1 
ATOM   166  C  CD1   . TRP A 1 53  ? 102.555 104.055 139.511 1.00 58.39  ? 1844 TRP A CD1   1 
ATOM   167  C  CD2   . TRP A 1 53  ? 104.652 104.717 139.905 1.00 58.29  ? 1844 TRP A CD2   1 
ATOM   168  N  NE1   . TRP A 1 53  ? 103.080 104.506 138.326 1.00 54.83  ? 1844 TRP A NE1   1 
ATOM   169  C  CE2   . TRP A 1 53  ? 104.368 104.919 138.542 1.00 54.58  ? 1844 TRP A CE2   1 
ATOM   170  C  CE3   . TRP A 1 53  ? 105.917 105.064 140.388 1.00 57.66  ? 1844 TRP A CE3   1 
ATOM   171  C  CZ2   . TRP A 1 53  ? 105.299 105.449 137.657 1.00 52.69  ? 1844 TRP A CZ2   1 
ATOM   172  C  CZ3   . TRP A 1 53  ? 106.840 105.589 139.508 1.00 56.48  ? 1844 TRP A CZ3   1 
ATOM   173  C  CH2   . TRP A 1 53  ? 106.526 105.778 138.158 1.00 54.01  ? 1844 TRP A CH2   1 
ATOM   174  N  N     . ARG A 1 54  ? 102.592 100.940 143.027 1.00 68.54  ? 1845 ARG A N     1 
ATOM   175  C  CA    . ARG A 1 54  ? 102.668 99.485  142.941 1.00 67.89  ? 1845 ARG A CA    1 
ATOM   176  C  C     . ARG A 1 54  ? 101.281 98.858  142.990 1.00 68.15  ? 1845 ARG A C     1 
ATOM   177  O  O     . ARG A 1 54  ? 101.002 97.894  142.269 1.00 67.24  ? 1845 ARG A O     1 
ATOM   178  C  CB    . ARG A 1 54  ? 103.546 98.937  144.065 1.00 69.38  ? 1845 ARG A CB    1 
ATOM   179  C  CG    . ARG A 1 54  ? 104.978 99.440  144.038 1.00 70.38  ? 1845 ARG A CG    1 
ATOM   180  C  CD    . ARG A 1 54  ? 105.900 98.466  143.328 1.00 71.17  ? 1845 ARG A CD    1 
ATOM   181  N  NE    . ARG A 1 54  ? 107.291 98.901  143.382 1.00 73.66  ? 1845 ARG A NE    1 
ATOM   182  C  CZ    . ARG A 1 54  ? 108.074 98.778  144.445 1.00 77.48  ? 1845 ARG A CZ    1 
ATOM   183  N  NH1   . ARG A 1 54  ? 107.638 98.229  145.566 1.00 76.33  ? 1845 ARG A NH1   1 
ATOM   184  N  NH2   . ARG A 1 54  ? 109.328 99.218  144.381 1.00 77.64  ? 1845 ARG A NH2   1 
ATOM   185  N  N     . CYS A 1 55  ? 100.400 99.388  143.843 1.00 70.78  ? 1846 CYS A N     1 
ATOM   186  C  CA    . CYS A 1 55  ? 99.048  98.847  143.939 1.00 72.85  ? 1846 CYS A CA    1 
ATOM   187  C  C     . CYS A 1 55  ? 98.271  99.048  142.643 1.00 70.02  ? 1846 CYS A C     1 
ATOM   188  O  O     . CYS A 1 55  ? 97.544  98.149  142.204 1.00 68.68  ? 1846 CYS A O     1 
ATOM   189  C  CB    . CYS A 1 55  ? 98.310  99.491  145.113 1.00 76.93  ? 1846 CYS A CB    1 
ATOM   190  S  SG    . CYS A 1 55  ? 96.617  98.903  145.348 1.00 102.05 ? 1846 CYS A SG    1 
ATOM   191  N  N     . LYS A 1 56  ? 98.407  100.215 142.019 1.00 72.00  ? 1847 LYS A N     1 
ATOM   192  C  CA    . LYS A 1 56  ? 97.658  100.512 140.806 1.00 68.38  ? 1847 LYS A CA    1 
ATOM   193  C  C     . LYS A 1 56  ? 98.174  99.690  139.629 1.00 62.71  ? 1847 LYS A C     1 
ATOM   194  O  O     . LYS A 1 56  ? 99.368  99.405  139.514 1.00 63.34  ? 1847 LYS A O     1 
ATOM   195  C  CB    . LYS A 1 56  ? 97.739  102.002 140.476 1.00 67.00  ? 1847 LYS A CB    1 
ATOM   196  C  CG    . LYS A 1 56  ? 96.949  102.890 141.423 1.00 69.63  ? 1847 LYS A CG    1 
ATOM   197  C  CD    . LYS A 1 56  ? 95.470  102.539 141.409 1.00 73.85  ? 1847 LYS A CD    1 
ATOM   198  C  CE    . LYS A 1 56  ? 94.854  102.788 140.043 1.00 76.20  ? 1847 LYS A CE    1 
ATOM   199  N  NZ    . LYS A 1 56  ? 93.391  102.514 140.039 1.00 86.41  ? 1847 LYS A NZ    1 
ATOM   200  N  N     . LYS A 1 57  ? 97.249  99.311  138.747 1.00 59.86  ? 1848 LYS A N     1 
ATOM   201  C  CA    . LYS A 1 57  ? 97.560  98.499  137.577 1.00 59.77  ? 1848 LYS A CA    1 
ATOM   202  C  C     . LYS A 1 57  ? 97.445  99.285  136.275 1.00 55.95  ? 1848 LYS A C     1 
ATOM   203  O  O     . LYS A 1 57  ? 97.356  98.684  135.201 1.00 56.44  ? 1848 LYS A O     1 
ATOM   204  C  CB    . LYS A 1 57  ? 96.651  97.270  137.530 1.00 61.58  ? 1848 LYS A CB    1 
ATOM   205  C  CG    . LYS A 1 57  ? 96.808  96.331  138.713 1.00 63.47  ? 1848 LYS A CG    1 
ATOM   206  C  CD    . LYS A 1 57  ? 96.078  95.020  138.472 1.00 64.10  ? 1848 LYS A CD    1 
ATOM   207  C  CE    . LYS A 1 57  ? 94.620  95.259  138.115 1.00 65.22  ? 1848 LYS A CE    1 
ATOM   208  N  NZ    . LYS A 1 57  ? 93.913  93.991  137.784 1.00 67.28  ? 1848 LYS A NZ    1 
ATOM   209  N  N     . ARG A 1 58  ? 97.437  100.615 136.348 1.00 52.32  ? 1849 ARG A N     1 
ATOM   210  C  CA    . ARG A 1 58  ? 97.294  101.437 135.148 1.00 44.90  ? 1849 ARG A CA    1 
ATOM   211  C  C     . ARG A 1 58  ? 97.839  102.825 135.456 1.00 43.40  ? 1849 ARG A C     1 
ATOM   212  O  O     . ARG A 1 58  ? 97.266  103.543 136.279 1.00 45.26  ? 1849 ARG A O     1 
ATOM   213  C  CB    . ARG A 1 58  ? 95.837  101.497 134.709 1.00 43.29  ? 1849 ARG A CB    1 
ATOM   214  C  CG    . ARG A 1 58  ? 95.567  102.461 133.574 1.00 45.83  ? 1849 ARG A CG    1 
ATOM   215  C  CD    . ARG A 1 58  ? 94.075  102.644 133.372 1.00 45.96  ? 1849 ARG A CD    1 
ATOM   216  N  NE    . ARG A 1 58  ? 93.467  101.480 132.741 1.00 44.86  ? 1849 ARG A NE    1 
ATOM   217  C  CZ    . ARG A 1 58  ? 93.204  101.388 131.445 1.00 47.62  ? 1849 ARG A CZ    1 
ATOM   218  N  NH1   . ARG A 1 58  ? 93.479  102.378 130.613 1.00 46.14  ? 1849 ARG A NH1   1 
ATOM   219  N  NH2   . ARG A 1 58  ? 92.648  100.275 130.974 1.00 46.16  ? 1849 ARG A NH2   1 
ATOM   220  N  N     . PHE A 1 59  ? 98.935  103.195 134.801 1.00 39.40  ? 1850 PHE A N     1 
ATOM   221  C  CA    . PHE A 1 59  ? 99.595  104.474 135.019 1.00 34.53  ? 1850 PHE A CA    1 
ATOM   222  C  C     . PHE A 1 59  ? 99.390  105.378 133.811 1.00 32.78  ? 1850 PHE A C     1 
ATOM   223  O  O     . PHE A 1 59  ? 98.836  104.976 132.787 1.00 36.28  ? 1850 PHE A O     1 
ATOM   224  C  CB    . PHE A 1 59  ? 101.094 104.287 135.286 1.00 37.29  ? 1850 PHE A CB    1 
ATOM   225  C  CG    . PHE A 1 59  ? 101.433 103.032 136.040 1.00 43.26  ? 1850 PHE A CG    1 
ATOM   226  C  CD1   . PHE A 1 59  ? 100.723 102.665 137.171 1.00 55.29  ? 1850 PHE A CD1   1 
ATOM   227  C  CD2   . PHE A 1 59  ? 102.471 102.222 135.615 1.00 44.60  ? 1850 PHE A CD2   1 
ATOM   228  C  CE1   . PHE A 1 59  ? 101.040 101.509 137.861 1.00 59.91  ? 1850 PHE A CE1   1 
ATOM   229  C  CE2   . PHE A 1 59  ? 102.792 101.066 136.299 1.00 56.71  ? 1850 PHE A CE2   1 
ATOM   230  C  CZ    . PHE A 1 59  ? 102.076 100.709 137.424 1.00 58.23  ? 1850 PHE A CZ    1 
ATOM   231  N  N     . SER A 1 60  ? 99.836  106.623 133.952 1.00 30.76  ? 1851 SER A N     1 
ATOM   232  C  CA    . SER A 1 60  ? 99.768  107.608 132.877 1.00 30.14  ? 1851 SER A CA    1 
ATOM   233  C  C     . SER A 1 60  ? 101.041 108.444 132.844 1.00 29.52  ? 1851 SER A C     1 
ATOM   234  O  O     . SER A 1 60  ? 101.001 109.671 132.762 1.00 34.45  ? 1851 SER A O     1 
ATOM   235  C  CB    . SER A 1 60  ? 98.545  108.501 133.035 1.00 35.21  ? 1851 SER A CB    1 
ATOM   236  O  OG    . SER A 1 60  ? 98.309  109.253 131.861 1.00 36.11  ? 1851 SER A OG    1 
ATOM   237  N  N     . ILE A 1 61  ? 102.197 107.781 132.925 1.00 26.94  ? 1852 ILE A N     1 
ATOM   238  C  CA    . ILE A 1 61  ? 103.444 108.515 133.092 1.00 28.16  ? 1852 ILE A CA    1 
ATOM   239  C  C     . ILE A 1 61  ? 103.705 109.420 131.887 1.00 33.51  ? 1852 ILE A C     1 
ATOM   240  O  O     . ILE A 1 61  ? 103.221 109.187 130.772 1.00 32.93  ? 1852 ILE A O     1 
ATOM   241  C  CB    . ILE A 1 61  ? 104.624 107.561 133.329 1.00 27.27  ? 1852 ILE A CB    1 
ATOM   242  C  CG1   . ILE A 1 61  ? 105.126 106.987 132.009 1.00 26.81  ? 1852 ILE A CG1   1 
ATOM   243  C  CG2   . ILE A 1 61  ? 104.214 106.436 134.260 1.00 37.09  ? 1852 ILE A CG2   1 
ATOM   244  C  CD1   . ILE A 1 61  ? 106.623 106.815 131.966 1.00 34.60  ? 1852 ILE A CD1   1 
ATOM   245  N  N     . SER A 1 62  ? 104.470 110.482 132.133 1.00 39.42  ? 1853 SER A N     1 
ATOM   246  C  CA    . SER A 1 62  ? 104.801 111.471 131.117 1.00 37.89  ? 1853 SER A CA    1 
ATOM   247  C  C     . SER A 1 62  ? 106.155 112.075 131.457 1.00 42.08  ? 1853 SER A C     1 
ATOM   248  O  O     . SER A 1 62  ? 106.633 111.968 132.587 1.00 45.46  ? 1853 SER A O     1 
ATOM   249  C  CB    . SER A 1 62  ? 103.731 112.563 131.022 1.00 35.09  ? 1853 SER A CB    1 
ATOM   250  O  OG    . SER A 1 62  ? 104.167 113.633 130.206 1.00 39.96  ? 1853 SER A OG    1 
ATOM   251  N  N     . LEU A 1 63  ? 106.772 112.710 130.466 1.00 42.51  ? 1854 LEU A N     1 
ATOM   252  C  CA    . LEU A 1 63  ? 108.105 113.280 130.608 1.00 43.96  ? 1854 LEU A CA    1 
ATOM   253  C  C     . LEU A 1 63  ? 108.022 114.799 130.635 1.00 48.03  ? 1854 LEU A C     1 
ATOM   254  O  O     . LEU A 1 63  ? 107.341 115.405 129.801 1.00 50.85  ? 1854 LEU A O     1 
ATOM   255  C  CB    . LEU A 1 63  ? 109.019 112.824 129.469 1.00 42.10  ? 1854 LEU A CB    1 
ATOM   256  C  CG    . LEU A 1 63  ? 109.776 111.511 129.673 1.00 39.76  ? 1854 LEU A CG    1 
ATOM   257  C  CD1   . LEU A 1 63  ? 110.495 111.512 131.010 1.00 41.50  ? 1854 LEU A CD1   1 
ATOM   258  C  CD2   . LEU A 1 63  ? 108.840 110.320 129.561 1.00 34.96  ? 1854 LEU A CD2   1 
ATOM   259  N  N     . ALA A 1 64  ? 108.715 115.407 131.594 1.00 49.33  ? 1855 ALA A N     1 
ATOM   260  C  CA    . ALA A 1 64  ? 108.823 116.856 131.701 1.00 49.67  ? 1855 ALA A CA    1 
ATOM   261  C  C     . ALA A 1 64  ? 110.132 117.294 131.062 1.00 56.07  ? 1855 ALA A C     1 
ATOM   262  O  O     . ALA A 1 64  ? 111.207 116.868 131.491 1.00 59.82  ? 1855 ALA A O     1 
ATOM   263  C  CB    . ALA A 1 64  ? 108.769 117.304 133.160 1.00 53.69  ? 1855 ALA A CB    1 
ATOM   264  N  N     . CYS A 1 65  ? 110.042 118.145 130.044 1.00 57.72  ? 1856 CYS A N     1 
ATOM   265  C  CA    . CYS A 1 65  ? 111.216 118.628 129.331 1.00 62.58  ? 1856 CYS A CA    1 
ATOM   266  C  C     . CYS A 1 65  ? 111.187 120.147 129.285 1.00 68.06  ? 1856 CYS A C     1 
ATOM   267  O  O     . CYS A 1 65  ? 110.190 120.740 128.863 1.00 69.43  ? 1856 CYS A O     1 
ATOM   268  C  CB    . CYS A 1 65  ? 111.278 118.053 127.914 1.00 62.12  ? 1856 CYS A CB    1 
ATOM   269  S  SG    . CYS A 1 65  ? 111.649 116.286 127.835 1.00 61.86  ? 1856 CYS A SG    1 
ATOM   270  N  N     . GLU A 1 66  ? 112.279 120.766 129.713 1.00 71.78  ? 1857 GLU A N     1 
ATOM   271  C  CA    . GLU A 1 66  ? 112.447 122.212 129.698 1.00 74.88  ? 1857 GLU A CA    1 
ATOM   272  C  C     . GLU A 1 66  ? 113.700 122.573 128.907 1.00 81.23  ? 1857 GLU A C     1 
ATOM   273  O  O     . GLU A 1 66  ? 114.376 121.713 128.337 1.00 82.06  ? 1857 GLU A O     1 
ATOM   274  C  CB    . GLU A 1 66  ? 112.534 122.772 131.120 1.00 71.50  ? 1857 GLU A CB    1 
ATOM   275  C  CG    . GLU A 1 66  ? 111.454 122.285 132.064 1.00 69.67  ? 1857 GLU A CG    1 
ATOM   276  C  CD    . GLU A 1 66  ? 111.589 122.887 133.449 1.00 73.82  ? 1857 GLU A CD    1 
ATOM   277  O  OE1   . GLU A 1 66  ? 112.371 123.848 133.604 1.00 78.04  ? 1857 GLU A OE1   1 
ATOM   278  O  OE2   . GLU A 1 66  ? 110.924 122.395 134.385 1.00 74.35  ? 1857 GLU A OE2   1 
ATOM   279  N  N     . LYS A 1 67  ? 114.002 123.867 128.874 1.00 84.35  ? 1858 LYS A N     1 
ATOM   280  C  CA    . LYS A 1 67  ? 115.243 124.337 128.284 1.00 87.05  ? 1858 LYS A CA    1 
ATOM   281  C  C     . LYS A 1 67  ? 116.400 124.131 129.257 1.00 91.17  ? 1858 LYS A C     1 
ATOM   282  O  O     . LYS A 1 67  ? 116.207 123.889 130.452 1.00 92.62  ? 1858 LYS A O     1 
ATOM   283  C  CB    . LYS A 1 67  ? 115.135 125.813 127.901 1.00 89.12  ? 1858 LYS A CB    1 
ATOM   284  C  CG    . LYS A 1 67  ? 114.226 126.085 126.713 1.00 87.34  ? 1858 LYS A CG    1 
ATOM   285  C  CD    . LYS A 1 67  ? 114.763 125.440 125.447 1.00 84.57  ? 1858 LYS A CD    1 
ATOM   286  C  CE    . LYS A 1 67  ? 113.899 125.781 124.245 1.00 81.73  ? 1858 LYS A CE    1 
ATOM   287  N  NZ    . LYS A 1 67  ? 114.356 125.076 123.017 1.00 83.07  ? 1858 LYS A NZ    1 
ATOM   288  N  N     . ILE A 1 68  ? 117.619 124.225 128.725 1.00 92.12  ? 1859 ILE A N     1 
ATOM   289  C  CA    . ILE A 1 68  ? 118.807 124.058 129.559 1.00 96.68  ? 1859 ILE A CA    1 
ATOM   290  C  C     . ILE A 1 68  ? 118.878 125.157 130.611 1.00 101.12 ? 1859 ILE A C     1 
ATOM   291  O  O     . ILE A 1 68  ? 119.179 124.895 131.783 1.00 100.97 ? 1859 ILE A O     1 
ATOM   292  C  CB    . ILE A 1 68  ? 120.074 124.026 128.686 1.00 97.20  ? 1859 ILE A CB    1 
ATOM   293  C  CG1   . ILE A 1 68  ? 119.948 122.954 127.603 1.00 90.16  ? 1859 ILE A CG1   1 
ATOM   294  C  CG2   . ILE A 1 68  ? 121.304 123.772 129.543 1.00 99.68  ? 1859 ILE A CG2   1 
ATOM   295  C  CD1   . ILE A 1 68  ? 119.896 121.545 128.145 1.00 87.33  ? 1859 ILE A CD1   1 
ATOM   296  N  N     . ARG A 1 69  ? 118.600 126.400 130.211 1.00 102.88 ? 1860 ARG A N     1 
ATOM   297  C  CA    . ARG A 1 69  ? 118.631 127.556 131.110 1.00 104.31 ? 1860 ARG A CA    1 
ATOM   298  C  C     . ARG A 1 69  ? 119.993 127.699 131.786 1.00 105.10 ? 1860 ARG A C     1 
ATOM   299  O  O     . ARG A 1 69  ? 120.089 128.031 132.969 1.00 103.23 ? 1860 ARG A O     1 
ATOM   300  C  CB    . ARG A 1 69  ? 117.512 127.480 132.152 1.00 100.54 ? 1860 ARG A CB    1 
ATOM   301  N  N     . SER A 1 70  ? 121.055 127.447 131.027 1.00 106.57 ? 1861 SER A N     1 
ATOM   302  C  CA    . SER A 1 70  ? 122.412 127.551 131.548 1.00 107.31 ? 1861 SER A CA    1 
ATOM   303  C  C     . SER A 1 70  ? 122.927 128.984 131.453 1.00 109.41 ? 1861 SER A C     1 
ATOM   304  O  O     . SER A 1 70  ? 123.984 129.310 131.992 1.00 108.39 ? 1861 SER A O     1 
ATOM   305  C  CB    . SER A 1 70  ? 123.350 126.605 130.796 1.00 102.29 ? 1861 SER A CB    1 
ATOM   306  N  N     . ILE A 1 94  ? 122.908 121.250 133.296 1.00 111.74 ? 1885 ILE A N     1 
ATOM   307  C  CA    . ILE A 1 94  ? 123.676 120.091 132.861 1.00 112.27 ? 1885 ILE A CA    1 
ATOM   308  C  C     . ILE A 1 94  ? 124.194 119.321 134.070 1.00 111.06 ? 1885 ILE A C     1 
ATOM   309  O  O     . ILE A 1 94  ? 124.940 119.862 134.887 1.00 112.64 ? 1885 ILE A O     1 
ATOM   310  C  CB    . ILE A 1 94  ? 124.834 120.507 131.939 1.00 113.47 ? 1885 ILE A CB    1 
ATOM   311  C  CG1   . ILE A 1 94  ? 124.300 121.262 130.720 1.00 108.66 ? 1885 ILE A CG1   1 
ATOM   312  C  CG2   . ILE A 1 94  ? 125.634 119.287 131.506 1.00 112.60 ? 1885 ILE A CG2   1 
ATOM   313  C  CD1   . ILE A 1 94  ? 125.377 121.690 129.746 1.00 105.80 ? 1885 ILE A CD1   1 
ATOM   314  N  N     . ARG A 1 95  ? 123.773 118.060 134.181 1.00 107.80 ? 1886 ARG A N     1 
ATOM   315  C  CA    . ARG A 1 95  ? 124.124 117.114 135.238 1.00 108.57 ? 1886 ARG A CA    1 
ATOM   316  C  C     . ARG A 1 95  ? 123.542 117.494 136.595 1.00 108.09 ? 1886 ARG A C     1 
ATOM   317  O  O     . ARG A 1 95  ? 123.666 116.712 137.546 1.00 107.91 ? 1886 ARG A O     1 
ATOM   318  C  CB    . ARG A 1 95  ? 125.643 116.930 135.382 1.00 107.96 ? 1886 ARG A CB    1 
ATOM   319  C  CG    . ARG A 1 95  ? 126.063 115.534 135.814 1.00 102.31 ? 1886 ARG A CG    1 
ATOM   320  C  CD    . ARG A 1 95  ? 127.571 115.362 135.740 1.00 105.67 ? 1886 ARG A CD    1 
ATOM   321  N  NE    . ARG A 1 95  ? 128.102 115.738 134.435 1.00 113.08 ? 1886 ARG A NE    1 
ATOM   322  C  CZ    . ARG A 1 95  ? 128.123 114.939 133.377 1.00 117.30 ? 1886 ARG A CZ    1 
ATOM   323  N  NH1   . ARG A 1 95  ? 127.644 113.706 133.432 1.00 116.77 ? 1886 ARG A NH1   1 
ATOM   324  N  NH2   . ARG A 1 95  ? 128.637 115.387 132.236 1.00 117.70 ? 1886 ARG A NH2   1 
ATOM   325  N  N     . ASP A 1 96  ? 122.908 118.657 136.720 1.00 107.13 ? 1887 ASP A N     1 
ATOM   326  C  CA    . ASP A 1 96  ? 122.241 119.062 137.951 1.00 106.45 ? 1887 ASP A CA    1 
ATOM   327  C  C     . ASP A 1 96  ? 120.749 119.268 137.752 1.00 102.36 ? 1887 ASP A C     1 
ATOM   328  O  O     . ASP A 1 96  ? 119.947 118.806 138.573 1.00 97.99  ? 1887 ASP A O     1 
ATOM   329  C  CB    . ASP A 1 96  ? 122.878 120.347 138.505 1.00 110.47 ? 1887 ASP A CB    1 
ATOM   330  C  CG    . ASP A 1 96  ? 124.321 120.149 138.929 1.00 111.63 ? 1887 ASP A CG    1 
ATOM   331  O  OD1   . ASP A 1 96  ? 125.190 120.009 138.043 1.00 110.80 ? 1887 ASP A OD1   1 
ATOM   332  O  OD2   . ASP A 1 96  ? 124.585 120.135 140.149 1.00 112.61 ? 1887 ASP A OD2   1 
ATOM   333  N  N     . ASP A 1 97  ? 120.353 119.950 136.676 1.00 101.79 ? 1888 ASP A N     1 
ATOM   334  C  CA    . ASP A 1 97  ? 118.940 120.181 136.409 1.00 96.99  ? 1888 ASP A CA    1 
ATOM   335  C  C     . ASP A 1 97  ? 118.225 118.922 135.935 1.00 92.22  ? 1888 ASP A C     1 
ATOM   336  O  O     . ASP A 1 97  ? 116.994 118.858 136.014 1.00 86.87  ? 1888 ASP A O     1 
ATOM   337  C  CB    . ASP A 1 97  ? 118.784 121.297 135.374 1.00 96.74  ? 1888 ASP A CB    1 
ATOM   338  C  CG    . ASP A 1 97  ? 117.384 121.878 135.344 1.00 95.41  ? 1888 ASP A CG    1 
ATOM   339  O  OD1   . ASP A 1 97  ? 116.645 121.706 136.335 1.00 91.79  ? 1888 ASP A OD1   1 
ATOM   340  O  OD2   . ASP A 1 97  ? 117.023 122.508 134.329 1.00 97.28  ? 1888 ASP A OD2   1 
ATOM   341  N  N     . GLY A 1 98  ? 118.957 117.932 135.445 1.00 91.26  ? 1889 GLY A N     1 
ATOM   342  C  CA    . GLY A 1 98  ? 118.344 116.700 134.998 1.00 80.50  ? 1889 GLY A CA    1 
ATOM   343  C  C     . GLY A 1 98  ? 119.236 115.979 134.006 1.00 79.40  ? 1889 GLY A C     1 
ATOM   344  O  O     . GLY A 1 98  ? 120.402 116.323 133.821 1.00 83.74  ? 1889 GLY A O     1 
ATOM   345  N  N     . PHE A 1 99  ? 118.647 114.965 133.370 1.00 77.37  ? 1890 PHE A N     1 
ATOM   346  C  CA    . PHE A 1 99  ? 119.353 114.124 132.407 1.00 77.05  ? 1890 PHE A CA    1 
ATOM   347  C  C     . PHE A 1 99  ? 119.290 114.747 131.018 1.00 73.97  ? 1890 PHE A C     1 
ATOM   348  O  O     . PHE A 1 99  ? 118.197 115.076 130.544 1.00 72.16  ? 1890 PHE A O     1 
ATOM   349  C  CB    . PHE A 1 99  ? 118.754 112.726 132.369 1.00 70.69  ? 1890 PHE A CB    1 
ATOM   350  C  CG    . PHE A 1 99  ? 118.717 112.047 133.706 1.00 68.74  ? 1890 PHE A CG    1 
ATOM   351  C  CD1   . PHE A 1 99  ? 119.839 111.408 134.203 1.00 71.45  ? 1890 PHE A CD1   1 
ATOM   352  C  CD2   . PHE A 1 99  ? 117.561 112.051 134.466 1.00 68.97  ? 1890 PHE A CD2   1 
ATOM   353  C  CE1   . PHE A 1 99  ? 119.809 110.783 135.433 1.00 75.56  ? 1890 PHE A CE1   1 
ATOM   354  C  CE2   . PHE A 1 99  ? 117.526 111.428 135.696 1.00 74.90  ? 1890 PHE A CE2   1 
ATOM   355  C  CZ    . PHE A 1 99  ? 118.650 110.794 136.180 1.00 77.42  ? 1890 PHE A CZ    1 
ATOM   356  N  N     . PRO A 1 100 ? 120.426 114.927 130.343 1.00 74.07  ? 1891 PRO A N     1 
ATOM   357  C  CA    . PRO A 1 100 ? 120.404 115.500 128.989 1.00 75.45  ? 1891 PRO A CA    1 
ATOM   358  C  C     . PRO A 1 100 ? 119.766 114.531 128.004 1.00 72.56  ? 1891 PRO A C     1 
ATOM   359  O  O     . PRO A 1 100 ? 120.164 113.368 127.911 1.00 70.17  ? 1891 PRO A O     1 
ATOM   360  C  CB    . PRO A 1 100 ? 121.887 115.735 128.678 1.00 79.62  ? 1891 PRO A CB    1 
ATOM   361  C  CG    . PRO A 1 100 ? 122.610 114.755 129.543 1.00 81.05  ? 1891 PRO A CG    1 
ATOM   362  C  CD    . PRO A 1 100 ? 121.793 114.618 130.796 1.00 76.80  ? 1891 PRO A CD    1 
ATOM   363  N  N     . ILE A 1 101 ? 118.773 115.019 127.267 1.00 71.78  ? 1892 ILE A N     1 
ATOM   364  C  CA    . ILE A 1 101 ? 118.071 114.202 126.285 1.00 71.57  ? 1892 ILE A CA    1 
ATOM   365  C  C     . ILE A 1 101 ? 118.935 114.065 125.038 1.00 74.51  ? 1892 ILE A C     1 
ATOM   366  O  O     . ILE A 1 101 ? 119.472 115.055 124.527 1.00 76.24  ? 1892 ILE A O     1 
ATOM   367  C  CB    . ILE A 1 101 ? 116.699 114.811 125.954 1.00 64.98  ? 1892 ILE A CB    1 
ATOM   368  C  CG1   . ILE A 1 101 ? 116.096 114.150 124.715 1.00 62.38  ? 1892 ILE A CG1   1 
ATOM   369  C  CG2   . ILE A 1 101 ? 116.812 116.308 125.756 1.00 69.57  ? 1892 ILE A CG2   1 
ATOM   370  C  CD1   . ILE A 1 101 ? 114.803 114.786 124.260 1.00 61.35  ? 1892 ILE A CD1   1 
ATOM   371  N  N     . LYS A 1 102 ? 119.082 112.833 124.555 1.00 74.38  ? 1893 LYS A N     1 
ATOM   372  C  CA    . LYS A 1 102 ? 119.882 112.584 123.363 1.00 79.12  ? 1893 LYS A CA    1 
ATOM   373  C  C     . LYS A 1 102 ? 119.276 113.289 122.155 1.00 80.03  ? 1893 LYS A C     1 
ATOM   374  O  O     . LYS A 1 102 ? 118.055 113.324 121.981 1.00 82.16  ? 1893 LYS A O     1 
ATOM   375  C  CB    . LYS A 1 102 ? 119.985 111.079 123.104 1.00 75.20  ? 1893 LYS A CB    1 
ATOM   376  C  CG    . LYS A 1 102 ? 120.752 110.703 121.843 1.00 72.45  ? 1893 LYS A CG    1 
ATOM   377  C  CD    . LYS A 1 102 ? 119.817 110.207 120.750 1.00 67.57  ? 1893 LYS A CD    1 
ATOM   378  C  CE    . LYS A 1 102 ? 120.579 109.859 119.481 1.00 69.30  ? 1893 LYS A CE    1 
ATOM   379  N  NZ    . LYS A 1 102 ? 119.670 109.405 118.391 1.00 62.28  ? 1893 LYS A NZ    1 
ATOM   380  N  N     . GLY A 1 103 ? 120.142 113.852 121.317 1.00 77.36  ? 1894 GLY A N     1 
ATOM   381  C  CA    . GLY A 1 103 ? 119.697 114.590 120.153 1.00 80.45  ? 1894 GLY A CA    1 
ATOM   382  C  C     . GLY A 1 103 ? 119.939 116.079 120.287 1.00 88.11  ? 1894 GLY A C     1 
ATOM   383  O  O     . GLY A 1 103 ? 121.087 116.532 120.258 1.00 90.34  ? 1894 GLY A O     1 
ATOM   384  N  N     . CYS A 1 104 ? 118.864 116.850 120.430 1.00 91.73  ? 1895 CYS A N     1 
ATOM   385  C  CA    . CYS A 1 104 ? 118.999 118.285 120.629 1.00 92.08  ? 1895 CYS A CA    1 
ATOM   386  C  C     . CYS A 1 104 ? 119.636 118.578 121.982 1.00 87.58  ? 1895 CYS A C     1 
ATOM   387  O  O     . CYS A 1 104 ? 119.289 117.967 122.997 1.00 83.45  ? 1895 CYS A O     1 
ATOM   388  C  CB    . CYS A 1 104 ? 117.634 118.965 120.527 1.00 91.93  ? 1895 CYS A CB    1 
ATOM   389  S  SG    . CYS A 1 104 ? 116.344 118.216 121.548 1.00 90.16  ? 1895 CYS A SG    1 
ATOM   390  N  N     . ASP A 1 105 ? 120.577 119.518 121.991 1.00 89.86  ? 1896 ASP A N     1 
ATOM   391  C  CA    . ASP A 1 105 ? 121.293 119.889 123.204 1.00 91.02  ? 1896 ASP A CA    1 
ATOM   392  C  C     . ASP A 1 105 ? 120.655 121.060 123.938 1.00 91.18  ? 1896 ASP A C     1 
ATOM   393  O  O     . ASP A 1 105 ? 121.161 121.460 124.992 1.00 87.05  ? 1896 ASP A O     1 
ATOM   394  C  CB    . ASP A 1 105 ? 122.751 120.225 122.872 1.00 87.50  ? 1896 ASP A CB    1 
ATOM   395  N  N     . ASP A 1 106 ? 119.566 121.616 123.414 1.00 91.44  ? 1897 ASP A N     1 
ATOM   396  C  CA    . ASP A 1 106 ? 118.885 122.739 124.044 1.00 90.01  ? 1897 ASP A CA    1 
ATOM   397  C  C     . ASP A 1 106 ? 117.730 122.312 124.942 1.00 90.74  ? 1897 ASP A C     1 
ATOM   398  O  O     . ASP A 1 106 ? 117.074 123.175 125.533 1.00 88.73  ? 1897 ASP A O     1 
ATOM   399  C  CB    . ASP A 1 106 ? 118.377 123.719 122.977 1.00 90.19  ? 1897 ASP A CB    1 
ATOM   400  C  CG    . ASP A 1 106 ? 117.449 123.066 121.961 1.00 92.96  ? 1897 ASP A CG    1 
ATOM   401  O  OD1   . ASP A 1 106 ? 117.151 121.859 122.086 1.00 90.60  ? 1897 ASP A OD1   1 
ATOM   402  O  OD2   . ASP A 1 106 ? 117.014 123.770 121.026 1.00 93.96  ? 1897 ASP A OD2   1 
ATOM   403  N  N     . THR A 1 107 ? 117.472 121.013 125.063 1.00 89.75  ? 1898 THR A N     1 
ATOM   404  C  CA    . THR A 1 107 ? 116.385 120.497 125.880 1.00 83.53  ? 1898 THR A CA    1 
ATOM   405  C  C     . THR A 1 107 ? 116.948 119.598 126.972 1.00 81.45  ? 1898 THR A C     1 
ATOM   406  O  O     . THR A 1 107 ? 118.046 119.048 126.842 1.00 82.31  ? 1898 THR A O     1 
ATOM   407  C  CB    . THR A 1 107 ? 115.369 119.720 125.032 1.00 80.09  ? 1898 THR A CB    1 
ATOM   408  O  OG1   . THR A 1 107 ? 115.261 120.329 123.740 1.00 83.46  ? 1898 THR A OG1   1 
ATOM   409  C  CG2   . THR A 1 107 ? 114.001 119.728 125.695 1.00 75.05  ? 1898 THR A CG2   1 
ATOM   410  N  N     . LEU A 1 108 ? 116.192 119.465 128.060 1.00 80.17  ? 1899 LEU A N     1 
ATOM   411  C  CA    . LEU A 1 108 ? 116.617 118.659 129.193 1.00 76.24  ? 1899 LEU A CA    1 
ATOM   412  C  C     . LEU A 1 108 ? 115.384 118.113 129.899 1.00 69.76  ? 1899 LEU A C     1 
ATOM   413  O  O     . LEU A 1 108 ? 114.313 118.723 129.861 1.00 69.02  ? 1899 LEU A O     1 
ATOM   414  C  CB    . LEU A 1 108 ? 117.480 119.483 130.155 1.00 78.32  ? 1899 LEU A CB    1 
ATOM   415  C  CG    . LEU A 1 108 ? 118.078 118.785 131.372 1.00 76.99  ? 1899 LEU A CG    1 
ATOM   416  C  CD1   . LEU A 1 108 ? 119.594 118.882 131.357 1.00 79.97  ? 1899 LEU A CD1   1 
ATOM   417  C  CD2   . LEU A 1 108 ? 117.509 119.398 132.631 1.00 80.24  ? 1899 LEU A CD2   1 
ATOM   418  N  N     . VAL A 1 109 ? 115.539 116.955 130.542 1.00 69.30  ? 1900 VAL A N     1 
ATOM   419  C  CA    . VAL A 1 109 ? 114.447 116.309 131.264 1.00 67.07  ? 1900 VAL A CA    1 
ATOM   420  C  C     . VAL A 1 109 ? 114.544 116.685 132.737 1.00 70.42  ? 1900 VAL A C     1 
ATOM   421  O  O     . VAL A 1 109 ? 115.644 116.839 133.284 1.00 75.85  ? 1900 VAL A O     1 
ATOM   422  C  CB    . VAL A 1 109 ? 114.460 114.779 131.065 1.00 62.36  ? 1900 VAL A CB    1 
ATOM   423  C  CG1   . VAL A 1 109 ? 115.489 114.113 131.959 1.00 63.04  ? 1900 VAL A CG1   1 
ATOM   424  C  CG2   . VAL A 1 109 ? 113.079 114.199 131.315 1.00 58.26  ? 1900 VAL A CG2   1 
ATOM   425  N  N     . VAL A 1 110 ? 113.389 116.872 133.371 1.00 64.43  ? 1901 VAL A N     1 
ATOM   426  C  CA    . VAL A 1 110 ? 113.333 117.352 134.747 1.00 64.14  ? 1901 VAL A CA    1 
ATOM   427  C  C     . VAL A 1 110 ? 112.684 116.306 135.645 1.00 67.60  ? 1901 VAL A C     1 
ATOM   428  O  O     . VAL A 1 110 ? 113.026 116.190 136.827 1.00 72.47  ? 1901 VAL A O     1 
ATOM   429  C  CB    . VAL A 1 110 ? 112.578 118.692 134.824 1.00 66.13  ? 1901 VAL A CB    1 
ATOM   430  C  CG1   . VAL A 1 110 ? 112.587 119.235 136.240 1.00 69.53  ? 1901 VAL A CG1   1 
ATOM   431  C  CG2   . VAL A 1 110 ? 113.194 119.695 133.867 1.00 71.39  ? 1901 VAL A CG2   1 
ATOM   432  N  N     . GLY A 1 111 ? 111.762 115.530 135.094 1.00 65.51  ? 1902 GLY A N     1 
ATOM   433  C  CA    . GLY A 1 111 ? 111.079 114.528 135.886 1.00 62.31  ? 1902 GLY A CA    1 
ATOM   434  C  C     . GLY A 1 111 ? 109.903 113.945 135.136 1.00 54.02  ? 1902 GLY A C     1 
ATOM   435  O  O     . GLY A 1 111 ? 109.649 114.267 133.974 1.00 54.88  ? 1902 GLY A O     1 
ATOM   436  N  N     . LEU A 1 112 ? 109.187 113.073 135.835 1.00 50.09  ? 1903 LEU A N     1 
ATOM   437  C  CA    . LEU A 1 112 ? 108.020 112.385 135.308 1.00 47.31  ? 1903 LEU A CA    1 
ATOM   438  C  C     . LEU A 1 112 ? 106.758 112.891 135.992 1.00 49.21  ? 1903 LEU A C     1 
ATOM   439  O  O     . LEU A 1 112 ? 106.802 113.501 137.061 1.00 55.23  ? 1903 LEU A O     1 
ATOM   440  C  CB    . LEU A 1 112 ? 108.139 110.867 135.497 1.00 45.56  ? 1903 LEU A CB    1 
ATOM   441  C  CG    . LEU A 1 112 ? 109.122 110.051 134.655 1.00 48.81  ? 1903 LEU A CG    1 
ATOM   442  C  CD1   . LEU A 1 112 ? 110.570 110.354 135.005 1.00 54.97  ? 1903 LEU A CD1   1 
ATOM   443  C  CD2   . LEU A 1 112 ? 108.829 108.572 134.826 1.00 45.66  ? 1903 LEU A CD2   1 
ATOM   444  N  N     . ALA A 1 113 ? 105.618 112.611 135.369 1.00 43.07  ? 1904 ALA A N     1 
ATOM   445  C  CA    . ALA A 1 113 ? 104.321 112.928 135.953 1.00 39.45  ? 1904 ALA A CA    1 
ATOM   446  C  C     . ALA A 1 113 ? 103.406 111.728 135.775 1.00 38.13  ? 1904 ALA A C     1 
ATOM   447  O  O     . ALA A 1 113 ? 103.192 111.275 134.649 1.00 41.23  ? 1904 ALA A O     1 
ATOM   448  C  CB    . ALA A 1 113 ? 103.713 114.176 135.311 1.00 40.88  ? 1904 ALA A CB    1 
ATOM   449  N  N     . VAL A 1 114 ? 102.873 111.217 136.881 1.00 38.47  ? 1905 VAL A N     1 
ATOM   450  C  CA    . VAL A 1 114 ? 102.017 110.038 136.886 1.00 32.23  ? 1905 VAL A CA    1 
ATOM   451  C  C     . VAL A 1 114 ? 100.642 110.437 137.398 1.00 38.52  ? 1905 VAL A C     1 
ATOM   452  O  O     . VAL A 1 114 ? 100.526 111.175 138.382 1.00 49.84  ? 1905 VAL A O     1 
ATOM   453  C  CB    . VAL A 1 114 ? 102.615 108.911 137.750 1.00 32.55  ? 1905 VAL A CB    1 
ATOM   454  C  CG1   . VAL A 1 114 ? 101.926 107.593 137.450 1.00 37.98  ? 1905 VAL A CG1   1 
ATOM   455  C  CG2   . VAL A 1 114 ? 104.111 108.805 137.518 1.00 36.23  ? 1905 VAL A CG2   1 
ATOM   456  N  N     . CYS A 1 115 ? 99.599  109.948 136.730 1.00 34.65  ? 1906 CYS A N     1 
ATOM   457  C  CA    . CYS A 1 115 ? 98.219  110.281 137.086 1.00 42.25  ? 1906 CYS A CA    1 
ATOM   458  C  C     . CYS A 1 115 ? 97.374  109.021 136.934 1.00 48.47  ? 1906 CYS A C     1 
ATOM   459  O  O     . CYS A 1 115 ? 96.972  108.671 135.822 1.00 49.82  ? 1906 CYS A O     1 
ATOM   460  C  CB    . CYS A 1 115 ? 97.689  111.413 136.214 1.00 46.01  ? 1906 CYS A CB    1 
ATOM   461  S  SG    . CYS A 1 115 ? 95.886  111.563 136.175 1.00 64.83  ? 1906 CYS A SG    1 
ATOM   462  N  N     . TRP A 1 116 ? 97.113  108.339 138.045 1.00 53.45  ? 1907 TRP A N     1 
ATOM   463  C  CA    . TRP A 1 116 ? 96.279  107.137 138.025 1.00 53.38  ? 1907 TRP A CA    1 
ATOM   464  C  C     . TRP A 1 116 ? 94.832  107.474 138.385 1.00 57.01  ? 1907 TRP A C     1 
ATOM   465  O  O     . TRP A 1 116 ? 94.234  106.904 139.297 1.00 59.95  ? 1907 TRP A O     1 
ATOM   466  C  CB    . TRP A 1 116 ? 96.853  106.078 138.961 1.00 54.71  ? 1907 TRP A CB    1 
ATOM   467  C  CG    . TRP A 1 116 ? 97.234  106.588 140.314 1.00 57.79  ? 1907 TRP A CG    1 
ATOM   468  C  CD1   . TRP A 1 116 ? 96.398  107.082 141.272 1.00 60.14  ? 1907 TRP A CD1   1 
ATOM   469  C  CD2   . TRP A 1 116 ? 98.551  106.639 140.869 1.00 59.09  ? 1907 TRP A CD2   1 
ATOM   470  N  NE1   . TRP A 1 116 ? 97.113  107.444 142.385 1.00 62.58  ? 1907 TRP A NE1   1 
ATOM   471  C  CE2   . TRP A 1 116 ? 98.439  107.182 142.162 1.00 61.95  ? 1907 TRP A CE2   1 
ATOM   472  C  CE3   . TRP A 1 116 ? 99.816  106.282 140.395 1.00 60.15  ? 1907 TRP A CE3   1 
ATOM   473  C  CZ2   . TRP A 1 116 ? 99.541  107.376 142.986 1.00 64.42  ? 1907 TRP A CZ2   1 
ATOM   474  C  CZ3   . TRP A 1 116 ? 100.908 106.476 141.214 1.00 60.73  ? 1907 TRP A CZ3   1 
ATOM   475  C  CH2   . TRP A 1 116 ? 100.764 107.016 142.496 1.00 62.39  ? 1907 TRP A CH2   1 
ATOM   476  N  N     . GLY A 1 117 ? 94.264  108.402 137.638 1.00 56.17  ? 1908 GLY A N     1 
ATOM   477  C  CA    . GLY A 1 117 ? 92.874  108.753 137.829 1.00 58.01  ? 1908 GLY A CA    1 
ATOM   478  C  C     . GLY A 1 117 ? 92.712  110.111 138.488 1.00 61.97  ? 1908 GLY A C     1 
ATOM   479  O  O     . GLY A 1 117 ? 93.534  110.542 139.308 1.00 60.45  ? 1908 GLY A O     1 
ATOM   480  N  N     . GLY A 1 118 ? 91.632  110.797 138.123 1.00 68.08  ? 1909 GLY A N     1 
ATOM   481  C  CA    . GLY A 1 118 ? 91.326  112.086 138.699 1.00 70.19  ? 1909 GLY A CA    1 
ATOM   482  C  C     . GLY A 1 118 ? 92.288  113.169 138.239 1.00 67.77  ? 1909 GLY A C     1 
ATOM   483  O  O     . GLY A 1 118 ? 93.054  113.016 137.288 1.00 65.15  ? 1909 GLY A O     1 
ATOM   484  N  N     . ARG A 1 119 ? 92.231  114.290 138.953 1.00 68.31  ? 1910 ARG A N     1 
ATOM   485  C  CA    . ARG A 1 119 ? 93.128  115.408 138.697 1.00 66.70  ? 1910 ARG A CA    1 
ATOM   486  C  C     . ARG A 1 119 ? 94.461  115.269 139.416 1.00 64.98  ? 1910 ARG A C     1 
ATOM   487  O  O     . ARG A 1 119 ? 95.316  116.149 139.275 1.00 65.98  ? 1910 ARG A O     1 
ATOM   488  C  CB    . ARG A 1 119 ? 92.458  116.723 139.102 1.00 70.51  ? 1910 ARG A CB    1 
ATOM   489  C  CG    . ARG A 1 119 ? 91.171  117.019 138.351 1.00 71.21  ? 1910 ARG A CG    1 
ATOM   490  C  CD    . ARG A 1 119 ? 91.429  117.201 136.867 1.00 71.46  ? 1910 ARG A CD    1 
ATOM   491  N  NE    . ARG A 1 119 ? 90.218  117.574 136.146 1.00 76.46  ? 1910 ARG A NE    1 
ATOM   492  C  CZ    . ARG A 1 119 ? 89.789  118.819 135.995 1.00 79.78  ? 1910 ARG A CZ    1 
ATOM   493  N  NH1   . ARG A 1 119 ? 90.452  119.845 136.503 1.00 79.48  ? 1910 ARG A NH1   1 
ATOM   494  N  NH2   . ARG A 1 119 ? 88.666  119.041 135.318 1.00 81.90  ? 1910 ARG A NH2   1 
ATOM   495  N  N     . ASP A 1 120 ? 94.653  114.201 140.188 1.00 65.77  ? 1911 ASP A N     1 
ATOM   496  C  CA    . ASP A 1 120 ? 95.925  113.979 140.860 1.00 64.24  ? 1911 ASP A CA    1 
ATOM   497  C  C     . ASP A 1 120 ? 97.015  113.724 139.829 1.00 59.08  ? 1911 ASP A C     1 
ATOM   498  O  O     . ASP A 1 120 ? 96.846  112.907 138.920 1.00 58.20  ? 1911 ASP A O     1 
ATOM   499  C  CB    . ASP A 1 120 ? 95.813  112.800 141.825 1.00 68.25  ? 1911 ASP A CB    1 
ATOM   500  C  CG    . ASP A 1 120 ? 95.207  113.194 143.156 1.00 69.14  ? 1911 ASP A CG    1 
ATOM   501  O  OD1   . ASP A 1 120 ? 95.792  114.052 143.848 1.00 65.40  ? 1911 ASP A OD1   1 
ATOM   502  O  OD2   . ASP A 1 120 ? 94.142  112.647 143.512 1.00 70.64  ? 1911 ASP A OD2   1 
ATOM   503  N  N     . ALA A 1 121 ? 98.136  114.422 139.973 1.00 55.42  ? 1912 ALA A N     1 
ATOM   504  C  CA    . ALA A 1 121 ? 99.207  114.436 138.983 1.00 50.01  ? 1912 ALA A CA    1 
ATOM   505  C  C     . ALA A 1 121 ? 100.559 114.262 139.655 1.00 49.35  ? 1912 ALA A C     1 
ATOM   506  O  O     . ALA A 1 121 ? 101.475 115.066 139.468 1.00 51.39  ? 1912 ALA A O     1 
ATOM   507  C  CB    . ALA A 1 121 ? 99.173  115.720 138.165 1.00 53.06  ? 1912 ALA A CB    1 
ATOM   508  N  N     . TYR A 1 122 ? 100.682 113.219 140.477 1.00 49.77  ? 1913 TYR A N     1 
ATOM   509  C  CA    . TYR A 1 122 ? 101.897 112.964 141.247 1.00 50.33  ? 1913 TYR A CA    1 
ATOM   510  C  C     . TYR A 1 122 ? 103.140 113.120 140.384 1.00 45.94  ? 1913 TYR A C     1 
ATOM   511  O  O     . TYR A 1 122 ? 103.343 112.375 139.423 1.00 48.31  ? 1913 TYR A O     1 
ATOM   512  C  CB    . TYR A 1 122 ? 101.847 111.555 141.842 1.00 50.62  ? 1913 TYR A CB    1 
ATOM   513  C  CG    . TYR A 1 122 ? 100.671 111.307 142.759 1.00 56.82  ? 1913 TYR A CG    1 
ATOM   514  C  CD1   . TYR A 1 122 ? 99.448  110.889 142.254 1.00 58.77  ? 1913 TYR A CD1   1 
ATOM   515  C  CD2   . TYR A 1 122 ? 100.787 111.484 144.130 1.00 63.28  ? 1913 TYR A CD2   1 
ATOM   516  C  CE1   . TYR A 1 122 ? 98.372  110.659 143.087 1.00 63.14  ? 1913 TYR A CE1   1 
ATOM   517  C  CE2   . TYR A 1 122 ? 99.717  111.256 144.972 1.00 63.11  ? 1913 TYR A CE2   1 
ATOM   518  C  CZ    . TYR A 1 122 ? 98.512  110.844 144.445 1.00 62.14  ? 1913 TYR A CZ    1 
ATOM   519  O  OH    . TYR A 1 122 ? 97.443  110.616 145.279 1.00 61.65  ? 1913 TYR A OH    1 
ATOM   520  N  N     . TYR A 1 123 ? 103.972 114.094 140.737 1.00 50.46  ? 1914 TYR A N     1 
ATOM   521  C  CA    . TYR A 1 123 ? 105.136 114.470 139.945 1.00 49.60  ? 1914 TYR A CA    1 
ATOM   522  C  C     . TYR A 1 123 ? 106.379 113.853 140.576 1.00 54.57  ? 1914 TYR A C     1 
ATOM   523  O  O     . TYR A 1 123 ? 106.772 114.223 141.687 1.00 63.14  ? 1914 TYR A O     1 
ATOM   524  C  CB    . TYR A 1 123 ? 105.256 115.990 139.858 1.00 53.67  ? 1914 TYR A CB    1 
ATOM   525  C  CG    . TYR A 1 123 ? 106.451 116.473 139.071 1.00 53.44  ? 1914 TYR A CG    1 
ATOM   526  C  CD1   . TYR A 1 123 ? 106.380 116.633 137.694 1.00 53.39  ? 1914 TYR A CD1   1 
ATOM   527  C  CD2   . TYR A 1 123 ? 107.648 116.775 139.703 1.00 56.58  ? 1914 TYR A CD2   1 
ATOM   528  C  CE1   . TYR A 1 123 ? 107.468 117.075 136.970 1.00 56.36  ? 1914 TYR A CE1   1 
ATOM   529  C  CE2   . TYR A 1 123 ? 108.741 117.217 138.988 1.00 58.99  ? 1914 TYR A CE2   1 
ATOM   530  C  CZ    . TYR A 1 123 ? 108.646 117.365 137.623 1.00 59.32  ? 1914 TYR A CZ    1 
ATOM   531  O  OH    . TYR A 1 123 ? 109.735 117.807 136.910 1.00 63.10  ? 1914 TYR A OH    1 
ATOM   532  N  N     . PHE A 1 124 ? 106.995 112.917 139.861 1.00 52.07  ? 1915 PHE A N     1 
ATOM   533  C  CA    . PHE A 1 124 ? 108.231 112.271 140.293 1.00 58.35  ? 1915 PHE A CA    1 
ATOM   534  C  C     . PHE A 1 124 ? 109.389 113.142 139.822 1.00 61.17  ? 1915 PHE A C     1 
ATOM   535  O  O     . PHE A 1 124 ? 109.777 113.101 138.654 1.00 63.61  ? 1915 PHE A O     1 
ATOM   536  C  CB    . PHE A 1 124 ? 108.314 110.858 139.725 1.00 55.86  ? 1915 PHE A CB    1 
ATOM   537  C  CG    . PHE A 1 124 ? 109.245 109.947 140.472 1.00 56.50  ? 1915 PHE A CG    1 
ATOM   538  C  CD1   . PHE A 1 124 ? 110.150 110.447 141.392 1.00 64.70  ? 1915 PHE A CD1   1 
ATOM   539  C  CD2   . PHE A 1 124 ? 109.212 108.583 140.251 1.00 61.33  ? 1915 PHE A CD2   1 
ATOM   540  C  CE1   . PHE A 1 124 ? 111.003 109.604 142.072 1.00 71.31  ? 1915 PHE A CE1   1 
ATOM   541  C  CE2   . PHE A 1 124 ? 110.062 107.736 140.930 1.00 69.09  ? 1915 PHE A CE2   1 
ATOM   542  C  CZ    . PHE A 1 124 ? 110.959 108.247 141.840 1.00 73.62  ? 1915 PHE A CZ    1 
ATOM   543  N  N     . SER A 1 125 ? 109.943 113.935 140.732 1.00 62.56  ? 1916 SER A N     1 
ATOM   544  C  CA    . SER A 1 125 ? 111.003 114.865 140.371 1.00 65.42  ? 1916 SER A CA    1 
ATOM   545  C  C     . SER A 1 125 ? 112.341 114.144 140.295 1.00 71.39  ? 1916 SER A C     1 
ATOM   546  O  O     . SER A 1 125 ? 112.751 113.472 141.247 1.00 79.39  ? 1916 SER A O     1 
ATOM   547  C  CB    . SER A 1 125 ? 111.076 116.008 141.383 1.00 69.85  ? 1916 SER A CB    1 
ATOM   548  O  OG    . SER A 1 125 ? 112.142 116.890 141.081 1.00 74.69  ? 1916 SER A OG    1 
ATOM   549  N  N     . LEU A 1 126 ? 113.021 114.286 139.159 1.00 68.84  ? 1917 LEU A N     1 
ATOM   550  C  CA    . LEU A 1 126 ? 114.375 113.784 138.983 1.00 71.45  ? 1917 LEU A CA    1 
ATOM   551  C  C     . LEU A 1 126 ? 115.421 114.864 139.213 1.00 77.68  ? 1917 LEU A C     1 
ATOM   552  O  O     . LEU A 1 126 ? 116.596 114.657 138.894 1.00 81.38  ? 1917 LEU A O     1 
ATOM   553  C  CB    . LEU A 1 126 ? 114.544 113.177 137.589 1.00 71.29  ? 1917 LEU A CB    1 
ATOM   554  C  CG    . LEU A 1 126 ? 113.489 112.173 137.120 1.00 70.24  ? 1917 LEU A CG    1 
ATOM   555  C  CD1   . LEU A 1 126 ? 113.964 111.450 135.872 1.00 62.49  ? 1917 LEU A CD1   1 
ATOM   556  C  CD2   . LEU A 1 126 ? 113.164 111.172 138.219 1.00 74.97  ? 1917 LEU A CD2   1 
ATOM   557  N  N     . GLN A 1 127 ? 115.016 116.012 139.750 1.00 82.46  ? 1918 GLN A N     1 
ATOM   558  C  CA    . GLN A 1 127 ? 115.951 117.092 140.027 1.00 88.33  ? 1918 GLN A CA    1 
ATOM   559  C  C     . GLN A 1 127 ? 116.954 116.677 141.095 1.00 94.84  ? 1918 GLN A C     1 
ATOM   560  O  O     . GLN A 1 127 ? 116.620 115.962 142.043 1.00 91.23  ? 1918 GLN A O     1 
ATOM   561  C  CB    . GLN A 1 127 ? 115.192 118.337 140.484 1.00 91.18  ? 1918 GLN A CB    1 
ATOM   562  C  CG    . GLN A 1 127 ? 114.375 119.008 139.397 1.00 87.49  ? 1918 GLN A CG    1 
ATOM   563  C  CD    . GLN A 1 127 ? 115.164 120.064 138.653 1.00 95.10  ? 1918 GLN A CD    1 
ATOM   564  O  OE1   . GLN A 1 127 ? 116.381 119.957 138.507 1.00 97.07  ? 1918 GLN A OE1   1 
ATOM   565  N  NE2   . GLN A 1 127 ? 114.474 121.098 138.184 1.00 96.68  ? 1918 GLN A NE2   1 
ATOM   566  N  N     . LYS A 1 128 ? 118.195 117.134 140.936 1.00 100.19 ? 1919 LYS A N     1 
ATOM   567  C  CA    . LYS A 1 128 ? 119.224 116.904 141.940 1.00 103.84 ? 1919 LYS A CA    1 
ATOM   568  C  C     . LYS A 1 128 ? 119.145 117.885 143.101 1.00 103.71 ? 1919 LYS A C     1 
ATOM   569  O  O     . LYS A 1 128 ? 119.876 117.717 144.083 1.00 101.60 ? 1919 LYS A O     1 
ATOM   570  C  CB    . LYS A 1 128 ? 120.613 116.979 141.300 1.00 105.95 ? 1919 LYS A CB    1 
ATOM   571  C  CG    . LYS A 1 128 ? 120.944 115.801 140.401 1.00 103.12 ? 1919 LYS A CG    1 
ATOM   572  C  CD    . LYS A 1 128 ? 121.011 114.508 141.196 1.00 101.92 ? 1919 LYS A CD    1 
ATOM   573  C  CE    . LYS A 1 128 ? 122.099 114.566 142.255 1.00 102.26 ? 1919 LYS A CE    1 
ATOM   574  N  NZ    . LYS A 1 128 ? 122.114 113.345 143.106 1.00 100.67 ? 1919 LYS A NZ    1 
ATOM   575  N  N     . GLU A 1 129 ? 118.287 118.896 143.015 1.00 101.75 ? 1920 GLU A N     1 
ATOM   576  C  CA    . GLU A 1 129 ? 118.143 119.876 144.083 1.00 102.60 ? 1920 GLU A CA    1 
ATOM   577  C  C     . GLU A 1 129 ? 117.070 119.449 145.079 1.00 105.80 ? 1920 GLU A C     1 
ATOM   578  O  O     . GLU A 1 129 ? 116.762 120.175 146.024 1.00 111.19 ? 1920 GLU A O     1 
ATOM   579  C  CB    . GLU A 1 129 ? 117.808 121.252 143.503 1.00 106.60 ? 1920 GLU A CB    1 
ATOM   580  C  CG    . GLU A 1 129 ? 116.770 121.225 142.392 1.00 104.61 ? 1920 GLU A CG    1 
ATOM   581  C  CD    . GLU A 1 129 ? 115.352 121.345 142.913 1.00 107.14 ? 1920 GLU A CD    1 
ATOM   582  O  OE1   . GLU A 1 129 ? 115.179 121.750 144.082 1.00 110.83 ? 1920 GLU A OE1   1 
ATOM   583  O  OE2   . GLU A 1 129 ? 114.409 121.039 142.154 1.00 102.76 ? 1920 GLU A OE2   1 
ATOM   584  N  N     . ASP A 1 145 ? 114.736 117.432 148.662 1.00 108.03 ? 1936 ASP A N     1 
ATOM   585  C  CA    . ASP A 1 145 ? 114.840 116.536 149.807 1.00 112.56 ? 1936 ASP A CA    1 
ATOM   586  C  C     . ASP A 1 145 ? 116.150 115.754 149.770 1.00 113.71 ? 1936 ASP A C     1 
ATOM   587  O  O     . ASP A 1 145 ? 116.310 114.843 148.958 1.00 110.09 ? 1936 ASP A O     1 
ATOM   588  C  CB    . ASP A 1 145 ? 113.651 115.574 149.844 1.00 108.74 ? 1936 ASP A CB    1 
ATOM   589  C  CG    . ASP A 1 145 ? 113.464 114.929 151.203 1.00 108.35 ? 1936 ASP A CG    1 
ATOM   590  O  OD1   . ASP A 1 145 ? 114.195 115.300 152.146 1.00 109.80 ? 1936 ASP A OD1   1 
ATOM   591  O  OD2   . ASP A 1 145 ? 112.583 114.052 151.330 1.00 105.63 ? 1936 ASP A OD2   1 
ATOM   592  N  N     . PRO A 1 146 ? 117.088 116.116 150.649 1.00 114.65 ? 1937 PRO A N     1 
ATOM   593  C  CA    . PRO A 1 146 ? 118.383 115.415 150.671 1.00 115.49 ? 1937 PRO A CA    1 
ATOM   594  C  C     . PRO A 1 146 ? 118.273 113.940 151.011 1.00 115.94 ? 1937 PRO A C     1 
ATOM   595  O  O     . PRO A 1 146 ? 119.153 113.164 150.617 1.00 115.36 ? 1937 PRO A O     1 
ATOM   596  C  CB    . PRO A 1 146 ? 119.178 116.179 151.739 1.00 112.57 ? 1937 PRO A CB    1 
ATOM   597  C  CG    . PRO A 1 146 ? 118.137 116.810 152.606 1.00 111.75 ? 1937 PRO A CG    1 
ATOM   598  C  CD    . PRO A 1 146 ? 116.998 117.152 151.692 1.00 110.17 ? 1937 PRO A CD    1 
ATOM   599  N  N     . SER A 1 147 ? 117.229 113.527 151.733 1.00 114.70 ? 1938 SER A N     1 
ATOM   600  C  CA    . SER A 1 147 ? 117.079 112.117 152.078 1.00 111.50 ? 1938 SER A CA    1 
ATOM   601  C  C     . SER A 1 147 ? 116.825 111.259 150.846 1.00 109.05 ? 1938 SER A C     1 
ATOM   602  O  O     . SER A 1 147 ? 117.155 110.068 150.843 1.00 104.83 ? 1938 SER A O     1 
ATOM   603  C  CB    . SER A 1 147 ? 115.947 111.941 153.090 1.00 107.55 ? 1938 SER A CB    1 
ATOM   604  O  OG    . SER A 1 147 ? 114.706 112.349 152.541 1.00 103.23 ? 1938 SER A OG    1 
ATOM   605  N  N     . LEU A 1 148 ? 116.244 111.839 149.798 1.00 109.30 ? 1939 LEU A N     1 
ATOM   606  C  CA    . LEU A 1 148 ? 115.974 111.131 148.547 1.00 105.89 ? 1939 LEU A CA    1 
ATOM   607  C  C     . LEU A 1 148 ? 117.047 111.529 147.539 1.00 103.13 ? 1939 LEU A C     1 
ATOM   608  O  O     . LEU A 1 148 ? 116.904 112.508 146.806 1.00 103.01 ? 1939 LEU A O     1 
ATOM   609  C  CB    . LEU A 1 148 ? 114.576 111.450 148.032 1.00 103.43 ? 1939 LEU A CB    1 
ATOM   610  C  CG    . LEU A 1 148 ? 113.405 110.879 148.829 1.00 101.61 ? 1939 LEU A CG    1 
ATOM   611  C  CD1   . LEU A 1 148 ? 112.089 111.246 148.167 1.00 95.41  ? 1939 LEU A CD1   1 
ATOM   612  C  CD2   . LEU A 1 148 ? 113.543 109.372 148.958 1.00 99.53  ? 1939 LEU A CD2   1 
ATOM   613  N  N     . THR A 1 149 ? 118.131 110.760 147.504 1.00 103.08 ? 1940 THR A N     1 
ATOM   614  C  CA    . THR A 1 149 ? 119.181 111.001 146.530 1.00 103.93 ? 1940 THR A CA    1 
ATOM   615  C  C     . THR A 1 149 ? 118.745 110.481 145.162 1.00 99.82  ? 1940 THR A C     1 
ATOM   616  O  O     . THR A 1 149 ? 117.683 109.871 145.007 1.00 98.86  ? 1940 THR A O     1 
ATOM   617  C  CB    . THR A 1 149 ? 120.491 110.352 146.975 1.00 105.56 ? 1940 THR A CB    1 
ATOM   618  O  OG1   . THR A 1 149 ? 120.343 108.927 146.989 1.00 106.24 ? 1940 THR A OG1   1 
ATOM   619  C  CG2   . THR A 1 149 ? 120.877 110.831 148.366 1.00 105.12 ? 1940 THR A CG2   1 
ATOM   620  N  N     . LEU A 1 150 ? 119.575 110.733 144.149 1.00 97.87  ? 1941 LEU A N     1 
ATOM   621  C  CA    . LEU A 1 150 ? 119.242 110.291 142.800 1.00 95.42  ? 1941 LEU A CA    1 
ATOM   622  C  C     . LEU A 1 150 ? 119.214 108.770 142.704 1.00 96.13  ? 1941 LEU A C     1 
ATOM   623  O  O     . LEU A 1 150 ? 118.377 108.206 141.992 1.00 95.75  ? 1941 LEU A O     1 
ATOM   624  C  CB    . LEU A 1 150 ? 120.235 110.872 141.794 1.00 93.76  ? 1941 LEU A CB    1 
ATOM   625  C  CG    . LEU A 1 150 ? 119.856 110.718 140.319 1.00 92.70  ? 1941 LEU A CG    1 
ATOM   626  C  CD1   . LEU A 1 150 ? 118.518 111.385 140.036 1.00 88.15  ? 1941 LEU A CD1   1 
ATOM   627  C  CD2   . LEU A 1 150 ? 120.943 111.278 139.414 1.00 88.81  ? 1941 LEU A CD2   1 
ATOM   628  N  N     . LYS A 1 151 ? 120.118 108.092 143.415 1.00 96.92  ? 1942 LYS A N     1 
ATOM   629  C  CA    . LYS A 1 151 ? 120.240 106.643 143.275 1.00 96.62  ? 1942 LYS A CA    1 
ATOM   630  C  C     . LYS A 1 151 ? 118.966 105.929 143.712 1.00 95.68  ? 1942 LYS A C     1 
ATOM   631  O  O     . LYS A 1 151 ? 118.406 105.122 142.961 1.00 92.96  ? 1942 LYS A O     1 
ATOM   632  C  CB    . LYS A 1 151 ? 121.442 106.141 144.075 1.00 94.67  ? 1942 LYS A CB    1 
ATOM   633  N  N     . ASP A 1 152 ? 118.485 106.218 144.925 1.00 95.16  ? 1943 ASP A N     1 
ATOM   634  C  CA    . ASP A 1 152 ? 117.302 105.522 145.423 1.00 95.76  ? 1943 ASP A CA    1 
ATOM   635  C  C     . ASP A 1 152 ? 116.052 105.934 144.656 1.00 93.39  ? 1943 ASP A C     1 
ATOM   636  O  O     . ASP A 1 152 ? 115.166 105.107 144.412 1.00 89.09  ? 1943 ASP A O     1 
ATOM   637  C  CB    . ASP A 1 152 ? 117.128 105.768 146.925 1.00 93.63  ? 1943 ASP A CB    1 
ATOM   638  C  CG    . ASP A 1 152 ? 117.019 107.240 147.276 1.00 97.82  ? 1943 ASP A CG    1 
ATOM   639  O  OD1   . ASP A 1 152 ? 115.960 107.847 147.010 1.00 97.46  ? 1943 ASP A OD1   1 
ATOM   640  O  OD2   . ASP A 1 152 ? 117.991 107.790 147.833 1.00 101.22 ? 1943 ASP A OD2   1 
ATOM   641  N  N     . ARG A 1 153 ? 115.966 107.205 144.259 1.00 93.48  ? 1944 ARG A N     1 
ATOM   642  C  CA    . ARG A 1 153 ? 114.824 107.662 143.474 1.00 88.78  ? 1944 ARG A CA    1 
ATOM   643  C  C     . ARG A 1 153 ? 114.757 106.930 142.140 1.00 86.65  ? 1944 ARG A C     1 
ATOM   644  O  O     . ARG A 1 153 ? 113.692 106.455 141.728 1.00 85.06  ? 1944 ARG A O     1 
ATOM   645  C  CB    . ARG A 1 153 ? 114.918 109.172 143.254 1.00 86.51  ? 1944 ARG A CB    1 
ATOM   646  C  CG    . ARG A 1 153 ? 114.128 110.006 144.243 1.00 87.71  ? 1944 ARG A CG    1 
ATOM   647  C  CD    . ARG A 1 153 ? 113.639 111.291 143.601 1.00 87.44  ? 1944 ARG A CD    1 
ATOM   648  N  NE    . ARG A 1 153 ? 114.691 112.297 143.531 1.00 88.15  ? 1944 ARG A NE    1 
ATOM   649  C  CZ    . ARG A 1 153 ? 114.827 113.301 144.386 1.00 88.31  ? 1944 ARG A CZ    1 
ATOM   650  N  NH1   . ARG A 1 153 ? 113.998 113.458 145.405 1.00 90.53  ? 1944 ARG A NH1   1 
ATOM   651  N  NH2   . ARG A 1 153 ? 115.823 114.166 144.218 1.00 89.58  ? 1944 ARG A NH2   1 
ATOM   652  N  N     . MET A 1 154 ? 115.898 106.813 141.459 1.00 86.87  ? 1945 MET A N     1 
ATOM   653  C  CA    . MET A 1 154 ? 115.928 106.121 140.176 1.00 84.65  ? 1945 MET A CA    1 
ATOM   654  C  C     . MET A 1 154 ? 115.685 104.628 140.348 1.00 84.42  ? 1945 MET A C     1 
ATOM   655  O  O     . MET A 1 154 ? 115.058 103.995 139.492 1.00 83.42  ? 1945 MET A O     1 
ATOM   656  C  CB    . MET A 1 154 ? 117.258 106.377 139.470 1.00 87.46  ? 1945 MET A CB    1 
ATOM   657  C  CG    . MET A 1 154 ? 117.432 107.812 139.004 1.00 87.70  ? 1945 MET A CG    1 
ATOM   658  S  SD    . MET A 1 154 ? 116.238 108.278 137.739 1.00 80.43  ? 1945 MET A SD    1 
ATOM   659  C  CE    . MET A 1 154 ? 117.024 107.613 136.279 1.00 71.71  ? 1945 MET A CE    1 
ATOM   660  N  N     . TRP A 1 155 ? 116.177 104.043 141.444 1.00 85.58  ? 1946 TRP A N     1 
ATOM   661  C  CA    . TRP A 1 155 ? 115.901 102.634 141.705 1.00 85.59  ? 1946 TRP A CA    1 
ATOM   662  C  C     . TRP A 1 155 ? 114.410 102.394 141.903 1.00 83.01  ? 1946 TRP A C     1 
ATOM   663  O  O     . TRP A 1 155 ? 113.853 101.429 141.368 1.00 78.27  ? 1946 TRP A O     1 
ATOM   664  C  CB    . TRP A 1 155 ? 116.691 102.160 142.925 1.00 85.13  ? 1946 TRP A CB    1 
ATOM   665  C  CG    . TRP A 1 155 ? 116.324 100.778 143.374 1.00 85.82  ? 1946 TRP A CG    1 
ATOM   666  C  CD1   . TRP A 1 155 ? 116.868 99.605  142.940 1.00 84.88  ? 1946 TRP A CD1   1 
ATOM   667  C  CD2   . TRP A 1 155 ? 115.336 100.425 144.349 1.00 88.31  ? 1946 TRP A CD2   1 
ATOM   668  N  NE1   . TRP A 1 155 ? 116.277 98.544  143.581 1.00 88.50  ? 1946 TRP A NE1   1 
ATOM   669  C  CE2   . TRP A 1 155 ? 115.334 99.021  144.451 1.00 87.85  ? 1946 TRP A CE2   1 
ATOM   670  C  CE3   . TRP A 1 155 ? 114.452 101.161 145.144 1.00 86.86  ? 1946 TRP A CE3   1 
ATOM   671  C  CZ2   . TRP A 1 155 ? 114.483 98.337  145.316 1.00 82.71  ? 1946 TRP A CZ2   1 
ATOM   672  C  CZ3   . TRP A 1 155 ? 113.608 100.480 146.001 1.00 83.87  ? 1946 TRP A CZ3   1 
ATOM   673  C  CH2   . TRP A 1 155 ? 113.630 99.083  146.081 1.00 81.86  ? 1946 TRP A CH2   1 
ATOM   674  N  N     . TYR A 1 156 ? 113.746 103.267 142.666 1.00 84.69  ? 1947 TYR A N     1 
ATOM   675  C  CA    . TYR A 1 156 ? 112.303 103.146 142.846 1.00 81.76  ? 1947 TYR A CA    1 
ATOM   676  C  C     . TYR A 1 156 ? 111.570 103.330 141.524 1.00 76.50  ? 1947 TYR A C     1 
ATOM   677  O  O     . TYR A 1 156 ? 110.606 102.611 141.232 1.00 74.86  ? 1947 TYR A O     1 
ATOM   678  C  CB    . TYR A 1 156 ? 111.814 104.166 143.874 1.00 81.99  ? 1947 TYR A CB    1 
ATOM   679  C  CG    . TYR A 1 156 ? 111.783 103.648 145.293 1.00 84.29  ? 1947 TYR A CG    1 
ATOM   680  C  CD1   . TYR A 1 156 ? 110.805 102.754 145.705 1.00 84.55  ? 1947 TYR A CD1   1 
ATOM   681  C  CD2   . TYR A 1 156 ? 112.730 104.056 146.222 1.00 85.84  ? 1947 TYR A CD2   1 
ATOM   682  C  CE1   . TYR A 1 156 ? 110.771 102.279 147.002 1.00 86.87  ? 1947 TYR A CE1   1 
ATOM   683  C  CE2   . TYR A 1 156 ? 112.705 103.587 147.521 1.00 87.22  ? 1947 TYR A CE2   1 
ATOM   684  C  CZ    . TYR A 1 156 ? 111.724 102.699 147.906 1.00 87.72  ? 1947 TYR A CZ    1 
ATOM   685  O  OH    . TYR A 1 156 ? 111.696 102.229 149.199 1.00 85.08  ? 1947 TYR A OH    1 
ATOM   686  N  N     . LEU A 1 157 ? 112.014 104.293 140.713 1.00 76.58  ? 1948 LEU A N     1 
ATOM   687  C  CA    . LEU A 1 157 ? 111.385 104.527 139.418 1.00 73.17  ? 1948 LEU A CA    1 
ATOM   688  C  C     . LEU A 1 157 ? 111.511 103.308 138.514 1.00 73.84  ? 1948 LEU A C     1 
ATOM   689  O  O     . LEU A 1 157 ? 110.547 102.920 137.844 1.00 71.69  ? 1948 LEU A O     1 
ATOM   690  C  CB    . LEU A 1 157 ? 112.008 105.758 138.758 1.00 69.94  ? 1948 LEU A CB    1 
ATOM   691  C  CG    . LEU A 1 157 ? 111.363 106.297 137.482 1.00 62.80  ? 1948 LEU A CG    1 
ATOM   692  C  CD1   . LEU A 1 157 ? 109.856 106.265 137.587 1.00 57.80  ? 1948 LEU A CD1   1 
ATOM   693  C  CD2   . LEU A 1 157 ? 111.844 107.712 137.218 1.00 63.26  ? 1948 LEU A CD2   1 
ATOM   694  N  N     . GLN A 1 158 ? 112.694 102.691 138.481 1.00 76.53  ? 1949 GLN A N     1 
ATOM   695  C  CA    . GLN A 1 158 ? 112.887 101.498 137.663 1.00 72.67  ? 1949 GLN A CA    1 
ATOM   696  C  C     . GLN A 1 158 ? 112.072 100.325 138.193 1.00 73.69  ? 1949 GLN A C     1 
ATOM   697  O  O     . GLN A 1 158 ? 111.479 99.572  137.411 1.00 72.60  ? 1949 GLN A O     1 
ATOM   698  C  CB    . GLN A 1 158 ? 114.373 101.143 137.602 1.00 73.89  ? 1949 GLN A CB    1 
ATOM   699  C  CG    . GLN A 1 158 ? 114.666 99.757  137.050 1.00 75.97  ? 1949 GLN A CG    1 
ATOM   700  C  CD    . GLN A 1 158 ? 114.997 98.753  138.137 1.00 77.93  ? 1949 GLN A CD    1 
ATOM   701  O  OE1   . GLN A 1 158 ? 115.033 99.091  139.320 1.00 81.27  ? 1949 GLN A OE1   1 
ATOM   702  N  NE2   . GLN A 1 158 ? 115.241 97.509  137.741 1.00 73.48  ? 1949 GLN A NE2   1 
ATOM   703  N  N     . SER A 1 159 ? 112.028 100.154 139.517 1.00 75.07  ? 1950 SER A N     1 
ATOM   704  C  CA    . SER A 1 159 ? 111.286 99.039  140.097 1.00 72.34  ? 1950 SER A CA    1 
ATOM   705  C  C     . SER A 1 159 ? 109.792 99.163  139.827 1.00 70.94  ? 1950 SER A C     1 
ATOM   706  O  O     . SER A 1 159 ? 109.128 98.168  139.513 1.00 72.68  ? 1950 SER A O     1 
ATOM   707  C  CB    . SER A 1 159 ? 111.555 98.955  141.598 1.00 74.11  ? 1950 SER A CB    1 
ATOM   708  O  OG    . SER A 1 159 ? 110.826 97.893  142.187 1.00 77.58  ? 1950 SER A OG    1 
ATOM   709  N  N     . CYS A 1 160 ? 109.243 100.373 139.945 1.00 71.21  ? 1951 CYS A N     1 
ATOM   710  C  CA    . CYS A 1 160 ? 107.821 100.569 139.699 1.00 67.30  ? 1951 CYS A CA    1 
ATOM   711  C  C     . CYS A 1 160 ? 107.468 100.537 138.218 1.00 63.91  ? 1951 CYS A C     1 
ATOM   712  O  O     . CYS A 1 160 ? 106.294 100.355 137.880 1.00 58.70  ? 1951 CYS A O     1 
ATOM   713  C  CB    . CYS A 1 160 ? 107.359 101.894 140.307 1.00 67.56  ? 1951 CYS A CB    1 
ATOM   714  S  SG    . CYS A 1 160 ? 107.511 101.982 142.104 1.00 84.56  ? 1951 CYS A SG    1 
ATOM   715  N  N     . LEU A 1 161 ? 108.450 100.708 137.334 1.00 63.07  ? 1952 LEU A N     1 
ATOM   716  C  CA    . LEU A 1 161 ? 108.228 100.682 135.896 1.00 59.42  ? 1952 LEU A CA    1 
ATOM   717  C  C     . LEU A 1 161 ? 108.628 99.356  135.262 1.00 62.49  ? 1952 LEU A C     1 
ATOM   718  O  O     . LEU A 1 161 ? 108.656 99.253  134.032 1.00 59.94  ? 1952 LEU A O     1 
ATOM   719  C  CB    . LEU A 1 161 ? 108.985 101.830 135.225 1.00 54.25  ? 1952 LEU A CB    1 
ATOM   720  C  CG    . LEU A 1 161 ? 108.292 103.192 135.217 1.00 50.90  ? 1952 LEU A CG    1 
ATOM   721  C  CD1   . LEU A 1 161 ? 109.111 104.200 134.432 1.00 48.81  ? 1952 LEU A CD1   1 
ATOM   722  C  CD2   . LEU A 1 161 ? 106.889 103.080 134.647 1.00 47.23  ? 1952 LEU A CD2   1 
ATOM   723  N  N     . ARG A 1 162 ? 108.939 98.345  136.067 1.00 65.12  ? 1953 ARG A N     1 
ATOM   724  C  CA    . ARG A 1 162 ? 109.335 97.033  135.575 1.00 63.31  ? 1953 ARG A CA    1 
ATOM   725  C  C     . ARG A 1 162 ? 108.212 96.038  135.829 1.00 62.18  ? 1953 ARG A C     1 
ATOM   726  O  O     . ARG A 1 162 ? 107.670 95.978  136.937 1.00 64.82  ? 1953 ARG A O     1 
ATOM   727  C  CB    . ARG A 1 162 ? 110.624 96.561  136.250 1.00 67.26  ? 1953 ARG A CB    1 
ATOM   728  C  CG    . ARG A 1 162 ? 111.366 95.483  135.482 1.00 67.76  ? 1953 ARG A CG    1 
ATOM   729  C  CD    . ARG A 1 162 ? 112.869 95.607  135.671 1.00 72.42  ? 1953 ARG A CD    1 
ATOM   730  N  NE    . ARG A 1 162 ? 113.447 96.618  134.795 1.00 74.05  ? 1953 ARG A NE    1 
ATOM   731  C  CZ    . ARG A 1 162 ? 114.746 96.760  134.569 1.00 74.01  ? 1953 ARG A CZ    1 
ATOM   732  N  NH1   . ARG A 1 162 ? 115.638 95.970  135.144 1.00 74.62  ? 1953 ARG A NH1   1 
ATOM   733  N  NH2   . ARG A 1 162 ? 115.161 97.719  133.746 1.00 69.49  ? 1953 ARG A NH2   1 
ATOM   734  N  N     . LYS A 1 163 ? 107.869 95.263  134.805 1.00 61.19  ? 1954 LYS A N     1 
ATOM   735  C  CA    . LYS A 1 163 ? 106.794 94.283  134.886 1.00 66.36  ? 1954 LYS A CA    1 
ATOM   736  C  C     . LYS A 1 163 ? 107.375 92.908  135.183 1.00 71.07  ? 1954 LYS A C     1 
ATOM   737  O  O     . LYS A 1 163 ? 108.295 92.456  134.494 1.00 70.11  ? 1954 LYS A O     1 
ATOM   738  C  CB    . LYS A 1 163 ? 105.991 94.245  133.585 1.00 61.34  ? 1954 LYS A CB    1 
ATOM   739  C  CG    . LYS A 1 163 ? 104.827 93.270  133.605 1.00 62.97  ? 1954 LYS A CG    1 
ATOM   740  C  CD    . LYS A 1 163 ? 104.152 93.186  132.247 1.00 59.16  ? 1954 LYS A CD    1 
ATOM   741  C  CE    . LYS A 1 163 ? 105.063 92.537  131.218 1.00 61.40  ? 1954 LYS A CE    1 
ATOM   742  N  NZ    . LYS A 1 163 ? 104.398 92.403  129.892 1.00 58.81  ? 1954 LYS A NZ    1 
ATOM   743  N  N     . GLU A 1 164 ? 106.834 92.249  136.204 1.00 75.92  ? 1955 GLU A N     1 
ATOM   744  C  CA    . GLU A 1 164 ? 107.282 90.916  136.577 1.00 80.18  ? 1955 GLU A CA    1 
ATOM   745  C  C     . GLU A 1 164 ? 106.167 90.220  137.341 1.00 88.66  ? 1955 GLU A C     1 
ATOM   746  O  O     . GLU A 1 164 ? 105.230 90.860  137.824 1.00 88.25  ? 1955 GLU A O     1 
ATOM   747  C  CB    . GLU A 1 164 ? 108.565 90.964  137.415 1.00 81.04  ? 1955 GLU A CB    1 
ATOM   748  C  CG    . GLU A 1 164 ? 108.335 91.255  138.889 1.00 83.81  ? 1955 GLU A CG    1 
ATOM   749  C  CD    . GLU A 1 164 ? 108.192 92.737  139.177 1.00 81.80  ? 1955 GLU A CD    1 
ATOM   750  O  OE1   . GLU A 1 164 ? 108.538 93.550  138.296 1.00 80.93  ? 1955 GLU A OE1   1 
ATOM   751  O  OE2   . GLU A 1 164 ? 107.733 93.087  140.284 1.00 82.72  ? 1955 GLU A OE2   1 
ATOM   752  N  N     . SER A 1 165 ? 106.284 88.893  137.432 1.00 93.11  ? 1956 SER A N     1 
ATOM   753  C  CA    . SER A 1 165 ? 105.340 88.047  138.169 1.00 96.71  ? 1956 SER A CA    1 
ATOM   754  C  C     . SER A 1 165 ? 103.898 88.289  137.722 1.00 97.05  ? 1956 SER A C     1 
ATOM   755  O  O     . SER A 1 165 ? 102.972 88.335  138.535 1.00 97.30  ? 1956 SER A O     1 
ATOM   756  C  CB    . SER A 1 165 ? 105.488 88.239  139.682 1.00 96.63  ? 1956 SER A CB    1 
ATOM   757  O  OG    . SER A 1 165 ? 104.956 89.478  140.117 1.00 91.37  ? 1956 SER A OG    1 
ATOM   758  N  N     . ASP A 1 166 ? 103.713 88.435  136.408 1.00 94.77  ? 1957 ASP A N     1 
ATOM   759  C  CA    . ASP A 1 166 ? 102.392 88.614  135.800 1.00 93.09  ? 1957 ASP A CA    1 
ATOM   760  C  C     . ASP A 1 166 ? 101.646 89.799  136.415 1.00 91.20  ? 1957 ASP A C     1 
ATOM   761  O  O     . ASP A 1 166 ? 100.462 89.716  136.745 1.00 90.52  ? 1957 ASP A O     1 
ATOM   762  C  CB    . ASP A 1 166 ? 101.562 87.331  135.904 1.00 96.19  ? 1957 ASP A CB    1 
ATOM   763  C  CG    . ASP A 1 166 ? 102.125 86.202  135.063 1.00 105.03 ? 1957 ASP A CG    1 
ATOM   764  O  OD1   . ASP A 1 166 ? 103.221 85.701  135.393 1.00 107.11 ? 1957 ASP A OD1   1 
ATOM   765  O  OD2   . ASP A 1 166 ? 101.471 85.814  134.072 1.00 109.48 ? 1957 ASP A OD2   1 
ATOM   766  N  N     . LYS A 1 167 ? 102.355 90.914  136.567 1.00 89.00  ? 1958 LYS A N     1 
ATOM   767  C  CA    . LYS A 1 167 ? 101.777 92.151  137.088 1.00 82.95  ? 1958 LYS A CA    1 
ATOM   768  C  C     . LYS A 1 167 ? 101.285 92.971  135.900 1.00 78.87  ? 1958 LYS A C     1 
ATOM   769  O  O     . LYS A 1 167 ? 102.056 93.699  135.272 1.00 76.72  ? 1958 LYS A O     1 
ATOM   770  C  CB    . LYS A 1 167 ? 102.795 92.922  137.921 1.00 79.90  ? 1958 LYS A CB    1 
ATOM   771  C  CG    . LYS A 1 167 ? 102.256 94.210  138.524 1.00 77.77  ? 1958 LYS A CG    1 
ATOM   772  C  CD    . LYS A 1 167 ? 101.016 93.954  139.363 1.00 79.13  ? 1958 LYS A CD    1 
ATOM   773  C  CE    . LYS A 1 167 ? 100.432 95.253  139.893 1.00 76.66  ? 1958 LYS A CE    1 
ATOM   774  N  NZ    . LYS A 1 167 ? 99.209  95.021  140.708 1.00 76.54  ? 1958 LYS A NZ    1 
ATOM   775  N  N     . GLU A 1 168 ? 99.996  92.847  135.594 1.00 77.70  ? 1959 GLU A N     1 
ATOM   776  C  CA    . GLU A 1 168 ? 99.412  93.570  134.473 1.00 73.78  ? 1959 GLU A CA    1 
ATOM   777  C  C     . GLU A 1 168 ? 99.358  95.060  134.786 1.00 72.45  ? 1959 GLU A C     1 
ATOM   778  O  O     . GLU A 1 168 ? 98.636  95.485  135.693 1.00 74.22  ? 1959 GLU A O     1 
ATOM   779  C  CB    . GLU A 1 168 ? 98.015  93.034  134.171 1.00 74.86  ? 1959 GLU A CB    1 
ATOM   780  C  CG    . GLU A 1 168 ? 97.381  93.625  132.923 1.00 80.50  ? 1959 GLU A CG    1 
ATOM   781  C  CD    . GLU A 1 168 ? 95.949  93.169  132.724 1.00 85.53  ? 1959 GLU A CD    1 
ATOM   782  O  OE1   . GLU A 1 168 ? 95.284  92.841  133.728 1.00 78.79  ? 1959 GLU A OE1   1 
ATOM   783  O  OE2   . GLU A 1 168 ? 95.488  93.140  131.564 1.00 92.16  ? 1959 GLU A OE2   1 
ATOM   784  N  N     . CYS A 1 169 ? 100.123 95.852  134.037 1.00 66.94  ? 1960 CYS A N     1 
ATOM   785  C  CA    . CYS A 1 169 ? 100.147 97.301  134.201 1.00 58.80  ? 1960 CYS A CA    1 
ATOM   786  C  C     . CYS A 1 169 ? 100.125 97.942  132.824 1.00 48.32  ? 1960 CYS A C     1 
ATOM   787  O  O     . CYS A 1 169 ? 101.008 97.679  132.004 1.00 48.04  ? 1960 CYS A O     1 
ATOM   788  C  CB    . CYS A 1 169 ? 101.381 97.754  134.986 1.00 56.77  ? 1960 CYS A CB    1 
ATOM   789  S  SG    . CYS A 1 169 ? 101.394 97.241  136.718 1.00 67.40  ? 1960 CYS A SG    1 
ATOM   790  N  N     . SER A 1 170 ? 99.121  98.779  132.573 1.00 45.55  ? 1961 SER A N     1 
ATOM   791  C  CA    . SER A 1 170 ? 98.965  99.460  131.289 1.00 38.85  ? 1961 SER A CA    1 
ATOM   792  C  C     . SER A 1 170 ? 99.445  100.898 131.452 1.00 36.85  ? 1961 SER A C     1 
ATOM   793  O  O     . SER A 1 170 ? 98.701  101.777 131.885 1.00 39.31  ? 1961 SER A O     1 
ATOM   794  C  CB    . SER A 1 170 ? 97.518  99.398  130.815 1.00 39.49  ? 1961 SER A CB    1 
ATOM   795  O  OG    . SER A 1 170 ? 97.103  98.058  130.623 1.00 44.18  ? 1961 SER A OG    1 
ATOM   796  N  N     . VAL A 1 171 ? 100.705 101.135 131.098 1.00 33.93  ? 1962 VAL A N     1 
ATOM   797  C  CA    . VAL A 1 171 ? 101.262 102.482 131.141 1.00 28.82  ? 1962 VAL A CA    1 
ATOM   798  C  C     . VAL A 1 171 ? 100.719 103.271 129.958 1.00 27.99  ? 1962 VAL A C     1 
ATOM   799  O  O     . VAL A 1 171 ? 100.850 102.853 128.803 1.00 36.61  ? 1962 VAL A O     1 
ATOM   800  C  CB    . VAL A 1 171 ? 102.794 102.441 131.118 1.00 27.35  ? 1962 VAL A CB    1 
ATOM   801  C  CG1   . VAL A 1 171 ? 103.364 103.843 131.222 1.00 27.43  ? 1962 VAL A CG1   1 
ATOM   802  C  CG2   . VAL A 1 171 ? 103.317 101.559 132.234 1.00 37.78  ? 1962 VAL A CG2   1 
ATOM   803  N  N     . VAL A 1 172 ? 100.108 104.417 130.238 1.00 24.08  ? 1963 VAL A N     1 
ATOM   804  C  CA    . VAL A 1 172 ? 99.568  105.291 129.204 1.00 24.08  ? 1963 VAL A CA    1 
ATOM   805  C  C     . VAL A 1 172 ? 100.578 106.397 128.941 1.00 28.35  ? 1963 VAL A C     1 
ATOM   806  O  O     . VAL A 1 172 ? 100.903 107.178 129.842 1.00 34.67  ? 1963 VAL A O     1 
ATOM   807  C  CB    . VAL A 1 172 ? 98.210  105.876 129.612 1.00 28.84  ? 1963 VAL A CB    1 
ATOM   808  C  CG1   . VAL A 1 172 ? 97.768  106.901 128.590 1.00 31.07  ? 1963 VAL A CG1   1 
ATOM   809  C  CG2   . VAL A 1 172 ? 97.178  104.774 129.752 1.00 31.45  ? 1963 VAL A CG2   1 
ATOM   810  N  N     . ILE A 1 173 ? 101.073 106.470 127.708 1.00 27.26  ? 1964 ILE A N     1 
ATOM   811  C  CA    . ILE A 1 173 ? 102.087 107.448 127.335 1.00 25.21  ? 1964 ILE A CA    1 
ATOM   812  C  C     . ILE A 1 173 ? 101.698 108.069 126.003 1.00 27.68  ? 1964 ILE A C     1 
ATOM   813  O  O     . ILE A 1 173 ? 101.531 107.354 125.010 1.00 30.28  ? 1964 ILE A O     1 
ATOM   814  C  CB    . ILE A 1 173 ? 103.484 106.818 127.228 1.00 22.79  ? 1964 ILE A CB    1 
ATOM   815  C  CG1   . ILE A 1 173 ? 104.001 106.408 128.600 1.00 24.32  ? 1964 ILE A CG1   1 
ATOM   816  C  CG2   . ILE A 1 173 ? 104.440 107.790 126.591 1.00 25.99  ? 1964 ILE A CG2   1 
ATOM   817  C  CD1   . ILE A 1 173 ? 105.421 105.929 128.571 1.00 21.28  ? 1964 ILE A CD1   1 
ATOM   818  N  N     . TYR A 1 174 ? 101.572 109.392 125.970 1.00 31.20  ? 1965 TYR A N     1 
ATOM   819  C  CA    . TYR A 1 174 ? 101.435 110.099 124.706 1.00 32.08  ? 1965 TYR A CA    1 
ATOM   820  C  C     . TYR A 1 174 ? 102.770 110.085 123.976 1.00 35.32  ? 1965 TYR A C     1 
ATOM   821  O  O     . TYR A 1 174 ? 103.816 110.333 124.583 1.00 35.40  ? 1965 TYR A O     1 
ATOM   822  C  CB    . TYR A 1 174 ? 100.973 111.535 124.933 1.00 34.57  ? 1965 TYR A CB    1 
ATOM   823  C  CG    . TYR A 1 174 ? 100.739 112.300 123.651 1.00 36.95  ? 1965 TYR A CG    1 
ATOM   824  C  CD1   . TYR A 1 174 ? 101.782 112.951 123.009 1.00 39.18  ? 1965 TYR A CD1   1 
ATOM   825  C  CD2   . TYR A 1 174 ? 99.479  112.376 123.086 1.00 35.16  ? 1965 TYR A CD2   1 
ATOM   826  C  CE1   . TYR A 1 174 ? 101.580 113.651 121.841 1.00 43.04  ? 1965 TYR A CE1   1 
ATOM   827  C  CE2   . TYR A 1 174 ? 99.268  113.074 121.923 1.00 36.34  ? 1965 TYR A CE2   1 
ATOM   828  C  CZ    . TYR A 1 174 ? 100.319 113.708 121.303 1.00 42.89  ? 1965 TYR A CZ    1 
ATOM   829  O  OH    . TYR A 1 174 ? 100.103 114.404 120.136 1.00 50.24  ? 1965 TYR A OH    1 
ATOM   830  N  N     . ASP A 1 175 ? 102.731 109.808 122.672 1.00 35.82  ? 1966 ASP A N     1 
ATOM   831  C  CA    . ASP A 1 175 ? 103.938 109.671 121.861 1.00 33.17  ? 1966 ASP A CA    1 
ATOM   832  C  C     . ASP A 1 175 ? 104.873 108.640 122.492 1.00 31.58  ? 1966 ASP A C     1 
ATOM   833  O  O     . ASP A 1 175 ? 105.979 108.946 122.940 1.00 31.00  ? 1966 ASP A O     1 
ATOM   834  C  CB    . ASP A 1 175 ? 104.633 111.024 121.674 1.00 36.10  ? 1966 ASP A CB    1 
ATOM   835  C  CG    . ASP A 1 175 ? 105.570 111.040 120.483 1.00 42.31  ? 1966 ASP A CG    1 
ATOM   836  O  OD1   . ASP A 1 175 ? 105.504 110.106 119.657 1.00 38.96  ? 1966 ASP A OD1   1 
ATOM   837  O  OD2   . ASP A 1 175 ? 106.370 111.993 120.368 1.00 49.61  ? 1966 ASP A OD2   1 
ATOM   838  N  N     . PHE A 1 176 ? 104.383 107.398 122.536 1.00 31.06  ? 1967 PHE A N     1 
ATOM   839  C  CA    . PHE A 1 176 ? 105.064 106.349 123.286 1.00 30.11  ? 1967 PHE A CA    1 
ATOM   840  C  C     . PHE A 1 176 ? 106.469 106.103 122.758 1.00 30.90  ? 1967 PHE A C     1 
ATOM   841  O  O     . PHE A 1 176 ? 107.392 105.846 123.537 1.00 34.55  ? 1967 PHE A O     1 
ATOM   842  C  CB    . PHE A 1 176 ? 104.251 105.056 123.249 1.00 26.33  ? 1967 PHE A CB    1 
ATOM   843  C  CG    . PHE A 1 176 ? 105.080 103.823 123.451 1.00 25.34  ? 1967 PHE A CG    1 
ATOM   844  C  CD1   . PHE A 1 176 ? 105.694 103.576 124.667 1.00 29.11  ? 1967 PHE A CD1   1 
ATOM   845  C  CD2   . PHE A 1 176 ? 105.262 102.922 122.420 1.00 24.81  ? 1967 PHE A CD2   1 
ATOM   846  C  CE1   . PHE A 1 176 ? 106.468 102.452 124.849 1.00 28.16  ? 1967 PHE A CE1   1 
ATOM   847  C  CE2   . PHE A 1 176 ? 106.032 101.795 122.600 1.00 26.78  ? 1967 PHE A CE2   1 
ATOM   848  C  CZ    . PHE A 1 176 ? 106.635 101.559 123.816 1.00 27.77  ? 1967 PHE A CZ    1 
ATOM   849  N  N     . ILE A 1 177 ? 106.653 106.162 121.439 1.00 28.62  ? 1968 ILE A N     1 
ATOM   850  C  CA    . ILE A 1 177 ? 107.967 105.880 120.870 1.00 26.46  ? 1968 ILE A CA    1 
ATOM   851  C  C     . ILE A 1 177 ? 108.997 106.885 121.370 1.00 30.96  ? 1968 ILE A C     1 
ATOM   852  O  O     . ILE A 1 177 ? 110.067 106.508 121.868 1.00 32.91  ? 1968 ILE A O     1 
ATOM   853  C  CB    . ILE A 1 177 ? 107.887 105.871 119.334 1.00 24.54  ? 1968 ILE A CB    1 
ATOM   854  C  CG1   . ILE A 1 177 ? 106.834 104.869 118.861 1.00 22.27  ? 1968 ILE A CG1   1 
ATOM   855  C  CG2   . ILE A 1 177 ? 109.239 105.551 118.742 1.00 27.15  ? 1968 ILE A CG2   1 
ATOM   856  C  CD1   . ILE A 1 177 ? 106.659 104.830 117.364 1.00 20.77  ? 1968 ILE A CD1   1 
ATOM   857  N  N     . GLN A 1 178 ? 108.682 108.177 121.267 1.00 32.02  ? 1969 GLN A N     1 
ATOM   858  C  CA    . GLN A 1 178 ? 109.640 109.205 121.654 1.00 30.82  ? 1969 GLN A CA    1 
ATOM   859  C  C     . GLN A 1 178 ? 109.879 109.213 123.159 1.00 35.32  ? 1969 GLN A C     1 
ATOM   860  O  O     . GLN A 1 178 ? 111.017 109.392 123.604 1.00 38.64  ? 1969 GLN A O     1 
ATOM   861  C  CB    . GLN A 1 178 ? 109.162 110.576 121.181 1.00 31.66  ? 1969 GLN A CB    1 
ATOM   862  C  CG    . GLN A 1 178 ? 110.156 111.693 121.440 1.00 40.00  ? 1969 GLN A CG    1 
ATOM   863  C  CD    . GLN A 1 178 ? 111.426 111.542 120.626 1.00 42.03  ? 1969 GLN A CD    1 
ATOM   864  O  OE1   . GLN A 1 178 ? 111.432 110.900 119.576 1.00 42.62  ? 1969 GLN A OE1   1 
ATOM   865  N  NE2   . GLN A 1 178 ? 112.512 112.132 121.111 1.00 42.09  ? 1969 GLN A NE2   1 
ATOM   866  N  N     . SER A 1 179 ? 108.827 109.020 123.956 1.00 32.58  ? 1970 SER A N     1 
ATOM   867  C  CA    . SER A 1 179 ? 109.005 108.971 125.403 1.00 31.63  ? 1970 SER A CA    1 
ATOM   868  C  C     . SER A 1 179 ? 109.812 107.753 125.830 1.00 33.61  ? 1970 SER A C     1 
ATOM   869  O  O     . SER A 1 179 ? 110.623 107.845 126.754 1.00 35.70  ? 1970 SER A O     1 
ATOM   870  C  CB    . SER A 1 179 ? 107.650 108.978 126.101 1.00 32.60  ? 1970 SER A CB    1 
ATOM   871  O  OG    . SER A 1 179 ? 106.929 110.161 125.805 1.00 39.60  ? 1970 SER A OG    1 
ATOM   872  N  N     . TYR A 1 180 ? 109.595 106.608 125.181 1.00 34.63  ? 1971 TYR A N     1 
ATOM   873  C  CA    . TYR A 1 180 ? 110.401 105.421 125.449 1.00 35.04  ? 1971 TYR A CA    1 
ATOM   874  C  C     . TYR A 1 180 ? 111.866 105.677 125.123 1.00 36.96  ? 1971 TYR A C     1 
ATOM   875  O  O     . TYR A 1 180 ? 112.762 105.327 125.902 1.00 40.10  ? 1971 TYR A O     1 
ATOM   876  C  CB    . TYR A 1 180 ? 109.856 104.244 124.636 1.00 30.73  ? 1971 TYR A CB    1 
ATOM   877  C  CG    . TYR A 1 180 ? 110.501 102.904 124.914 1.00 33.47  ? 1971 TYR A CG    1 
ATOM   878  C  CD1   . TYR A 1 180 ? 111.675 102.529 124.276 1.00 34.15  ? 1971 TYR A CD1   1 
ATOM   879  C  CD2   . TYR A 1 180 ? 109.922 102.004 125.796 1.00 37.49  ? 1971 TYR A CD2   1 
ATOM   880  C  CE1   . TYR A 1 180 ? 112.261 101.304 124.521 1.00 33.02  ? 1971 TYR A CE1   1 
ATOM   881  C  CE2   . TYR A 1 180 ? 110.501 100.777 126.046 1.00 37.54  ? 1971 TYR A CE2   1 
ATOM   882  C  CZ    . TYR A 1 180 ? 111.669 100.433 125.407 1.00 36.04  ? 1971 TYR A CZ    1 
ATOM   883  O  OH    . TYR A 1 180 ? 112.247 99.211  125.655 1.00 35.26  ? 1971 TYR A OH    1 
ATOM   884  N  N     . LYS A 1 181 ? 112.128 106.301 123.971 1.00 34.68  ? 1972 LYS A N     1 
ATOM   885  C  CA    . LYS A 1 181 ? 113.504 106.614 123.603 1.00 33.08  ? 1972 LYS A CA    1 
ATOM   886  C  C     . LYS A 1 181 ? 114.136 107.580 124.598 1.00 37.15  ? 1972 LYS A C     1 
ATOM   887  O  O     . LYS A 1 181 ? 115.306 107.428 124.962 1.00 42.82  ? 1972 LYS A O     1 
ATOM   888  C  CB    . LYS A 1 181 ? 113.556 107.187 122.187 1.00 33.46  ? 1972 LYS A CB    1 
ATOM   889  C  CG    . LYS A 1 181 ? 113.126 106.210 121.106 1.00 31.16  ? 1972 LYS A CG    1 
ATOM   890  C  CD    . LYS A 1 181 ? 112.830 106.917 119.793 1.00 29.46  ? 1972 LYS A CD    1 
ATOM   891  C  CE    . LYS A 1 181 ? 113.838 108.018 119.513 1.00 36.66  ? 1972 LYS A CE    1 
ATOM   892  N  NZ    . LYS A 1 181 ? 115.095 107.486 118.919 1.00 39.45  ? 1972 LYS A NZ    1 
ATOM   893  N  N     . ILE A 1 182 ? 113.379 108.584 125.043 1.00 39.54  ? 1973 ILE A N     1 
ATOM   894  C  CA    . ILE A 1 182 ? 113.905 109.543 126.010 1.00 42.65  ? 1973 ILE A CA    1 
ATOM   895  C  C     . ILE A 1 182 ? 114.195 108.862 127.341 1.00 44.17  ? 1973 ILE A C     1 
ATOM   896  O  O     . ILE A 1 182 ? 115.244 109.090 127.954 1.00 46.93  ? 1973 ILE A O     1 
ATOM   897  C  CB    . ILE A 1 182 ? 112.927 110.719 126.175 1.00 38.97  ? 1973 ILE A CB    1 
ATOM   898  C  CG1   . ILE A 1 182 ? 112.904 111.567 124.904 1.00 39.89  ? 1973 ILE A CG1   1 
ATOM   899  C  CG2   . ILE A 1 182 ? 113.310 111.568 127.373 1.00 39.54  ? 1973 ILE A CG2   1 
ATOM   900  C  CD1   . ILE A 1 182 ? 111.876 112.663 124.926 1.00 43.02  ? 1973 ILE A CD1   1 
ATOM   901  N  N     . LEU A 1 183 ? 113.280 108.009 127.804 1.00 42.50  ? 1974 LEU A N     1 
ATOM   902  C  CA    . LEU A 1 183 ? 113.475 107.317 129.072 1.00 44.55  ? 1974 LEU A CA    1 
ATOM   903  C  C     . LEU A 1 183 ? 114.664 106.369 129.020 1.00 46.61  ? 1974 LEU A C     1 
ATOM   904  O  O     . LEU A 1 183 ? 115.362 106.200 130.025 1.00 49.46  ? 1974 LEU A O     1 
ATOM   905  C  CB    . LEU A 1 183 ? 112.207 106.555 129.453 1.00 41.93  ? 1974 LEU A CB    1 
ATOM   906  C  CG    . LEU A 1 183 ? 111.122 107.360 130.167 1.00 40.73  ? 1974 LEU A CG    1 
ATOM   907  C  CD1   . LEU A 1 183 ? 109.876 106.516 130.363 1.00 35.67  ? 1974 LEU A CD1   1 
ATOM   908  C  CD2   . LEU A 1 183 ? 111.633 107.883 131.500 1.00 38.77  ? 1974 LEU A CD2   1 
ATOM   909  N  N     . LEU A 1 184 ? 114.912 105.741 127.871 1.00 44.60  ? 1975 LEU A N     1 
ATOM   910  C  CA    . LEU A 1 184 ? 116.036 104.816 127.772 1.00 45.48  ? 1975 LEU A CA    1 
ATOM   911  C  C     . LEU A 1 184 ? 117.365 105.546 127.604 1.00 46.37  ? 1975 LEU A C     1 
ATOM   912  O  O     . LEU A 1 184 ? 118.316 105.305 128.354 1.00 50.07  ? 1975 LEU A O     1 
ATOM   913  C  CB    . LEU A 1 184 ? 115.817 103.845 126.613 1.00 36.26  ? 1975 LEU A CB    1 
ATOM   914  C  CG    . LEU A 1 184 ? 116.446 102.474 126.838 1.00 35.08  ? 1975 LEU A CG    1 
ATOM   915  C  CD1   . LEU A 1 184 ? 115.713 101.710 127.915 1.00 43.88  ? 1975 LEU A CD1   1 
ATOM   916  C  CD2   . LEU A 1 184 ? 116.458 101.699 125.548 1.00 38.47  ? 1975 LEU A CD2   1 
ATOM   917  N  N     . LEU A 1 185 ? 117.453 106.430 126.611 1.00 44.42  ? 1976 LEU A N     1 
ATOM   918  C  CA    . LEU A 1 185 ? 118.743 107.005 126.246 1.00 48.40  ? 1976 LEU A CA    1 
ATOM   919  C  C     . LEU A 1 185 ? 119.270 107.947 127.322 1.00 50.34  ? 1976 LEU A C     1 
ATOM   920  O  O     . LEU A 1 185 ? 120.476 107.970 127.593 1.00 52.73  ? 1976 LEU A O     1 
ATOM   921  C  CB    . LEU A 1 185 ? 118.630 107.719 124.901 1.00 54.18  ? 1976 LEU A CB    1 
ATOM   922  C  CG    . LEU A 1 185 ? 118.180 106.812 123.754 1.00 47.92  ? 1976 LEU A CG    1 
ATOM   923  C  CD1   . LEU A 1 185 ? 117.907 107.615 122.496 1.00 52.75  ? 1976 LEU A CD1   1 
ATOM   924  C  CD2   . LEU A 1 185 ? 119.218 105.734 123.493 1.00 44.93  ? 1976 LEU A CD2   1 
ATOM   925  N  N     . SER A 1 186 ? 118.392 108.731 127.947 1.00 50.44  ? 1977 SER A N     1 
ATOM   926  C  CA    . SER A 1 186 ? 118.823 109.693 128.956 1.00 54.58  ? 1977 SER A CA    1 
ATOM   927  C  C     . SER A 1 186 ? 118.642 109.178 130.380 1.00 55.11  ? 1977 SER A C     1 
ATOM   928  O  O     . SER A 1 186 ? 119.596 109.181 131.162 1.00 57.50  ? 1977 SER A O     1 
ATOM   929  C  CB    . SER A 1 186 ? 118.080 111.023 128.774 1.00 61.14  ? 1977 SER A CB    1 
ATOM   930  O  OG    . SER A 1 186 ? 116.742 110.949 129.226 1.00 60.91  ? 1977 SER A OG    1 
ATOM   931  N  N     . CYS A 1 187 ? 117.437 108.731 130.736 1.00 52.88  ? 1978 CYS A N     1 
ATOM   932  C  CA    . CYS A 1 187 ? 117.188 108.251 132.090 1.00 53.24  ? 1978 CYS A CA    1 
ATOM   933  C  C     . CYS A 1 187 ? 117.723 106.845 132.330 1.00 51.75  ? 1978 CYS A C     1 
ATOM   934  O  O     . CYS A 1 187 ? 117.942 106.472 133.487 1.00 50.51  ? 1978 CYS A O     1 
ATOM   935  C  CB    . CYS A 1 187 ? 115.689 108.286 132.395 1.00 53.80  ? 1978 CYS A CB    1 
ATOM   936  S  SG    . CYS A 1 187 ? 114.909 109.897 132.146 1.00 64.74  ? 1978 CYS A SG    1 
ATOM   937  N  N     . GLY A 1 188 ? 117.948 106.066 131.276 1.00 54.49  ? 1979 GLY A N     1 
ATOM   938  C  CA    . GLY A 1 188 ? 118.370 104.689 131.450 1.00 52.55  ? 1979 GLY A CA    1 
ATOM   939  C  C     . GLY A 1 188 ? 117.328 103.800 132.089 1.00 49.48  ? 1979 GLY A C     1 
ATOM   940  O  O     . GLY A 1 188 ? 117.675 102.924 132.886 1.00 53.25  ? 1979 GLY A O     1 
ATOM   941  N  N     . ILE A 1 189 ? 116.056 104.000 131.756 1.00 46.06  ? 1980 ILE A N     1 
ATOM   942  C  CA    . ILE A 1 189 ? 114.950 103.254 132.345 1.00 47.19  ? 1980 ILE A CA    1 
ATOM   943  C  C     . ILE A 1 189 ? 114.301 102.427 131.246 1.00 48.52  ? 1980 ILE A C     1 
ATOM   944  O  O     . ILE A 1 189 ? 113.815 102.977 130.250 1.00 48.53  ? 1980 ILE A O     1 
ATOM   945  C  CB    . ILE A 1 189 ? 113.929 104.190 133.006 1.00 46.35  ? 1980 ILE A CB    1 
ATOM   946  C  CG1   . ILE A 1 189 ? 114.529 104.819 134.262 1.00 52.93  ? 1980 ILE A CG1   1 
ATOM   947  C  CG2   . ILE A 1 189 ? 112.652 103.439 133.337 1.00 44.68  ? 1980 ILE A CG2   1 
ATOM   948  C  CD1   . ILE A 1 189 ? 113.785 106.032 134.739 1.00 56.15  ? 1980 ILE A CD1   1 
ATOM   949  N  N     . SER A 1 190 ? 114.283 101.111 131.430 1.00 51.85  ? 1981 SER A N     1 
ATOM   950  C  CA    . SER A 1 190 ? 113.728 100.194 130.441 1.00 49.63  ? 1981 SER A CA    1 
ATOM   951  C  C     . SER A 1 190 ? 112.263 99.942  130.773 1.00 51.03  ? 1981 SER A C     1 
ATOM   952  O  O     . SER A 1 190 ? 111.947 99.268  131.759 1.00 55.51  ? 1981 SER A O     1 
ATOM   953  C  CB    . SER A 1 190 ? 114.519 98.889  130.412 1.00 53.21  ? 1981 SER A CB    1 
ATOM   954  O  OG    . SER A 1 190 ? 113.978 97.987  129.462 1.00 51.58  ? 1981 SER A OG    1 
ATOM   955  N  N     . LEU A 1 191 ? 111.370 100.486 129.953 1.00 44.73  ? 1982 LEU A N     1 
ATOM   956  C  CA    . LEU A 1 191 ? 109.942 100.264 130.126 1.00 46.90  ? 1982 LEU A CA    1 
ATOM   957  C  C     . LEU A 1 191 ? 109.598 98.856  129.660 1.00 50.47  ? 1982 LEU A C     1 
ATOM   958  O  O     . LEU A 1 191 ? 109.909 98.480  128.524 1.00 52.19  ? 1982 LEU A O     1 
ATOM   959  C  CB    . LEU A 1 191 ? 109.149 101.305 129.342 1.00 40.87  ? 1982 LEU A CB    1 
ATOM   960  C  CG    . LEU A 1 191 ? 108.421 102.370 130.157 1.00 37.55  ? 1982 LEU A CG    1 
ATOM   961  C  CD1   . LEU A 1 191 ? 107.775 103.367 129.226 1.00 32.41  ? 1982 LEU A CD1   1 
ATOM   962  C  CD2   . LEU A 1 191 ? 107.385 101.732 131.061 1.00 42.51  ? 1982 LEU A CD2   1 
ATOM   963  N  N     . GLU A 1 192 ? 108.965 98.072  130.534 1.00 45.91  ? 1983 GLU A N     1 
ATOM   964  C  CA    . GLU A 1 192 ? 108.631 96.693  130.216 1.00 46.38  ? 1983 GLU A CA    1 
ATOM   965  C  C     . GLU A 1 192 ? 107.162 96.354  130.422 1.00 47.90  ? 1983 GLU A C     1 
ATOM   966  O  O     . GLU A 1 192 ? 106.774 95.204  130.191 1.00 54.34  ? 1983 GLU A O     1 
ATOM   967  C  CB    . GLU A 1 192 ? 109.494 95.727  131.043 1.00 52.91  ? 1983 GLU A CB    1 
ATOM   968  C  CG    . GLU A 1 192 ? 110.966 96.107  131.095 1.00 54.82  ? 1983 GLU A CG    1 
ATOM   969  C  CD    . GLU A 1 192 ? 111.867 94.927  131.394 1.00 64.00  ? 1983 GLU A CD    1 
ATOM   970  O  OE1   . GLU A 1 192 ? 111.969 94.023  130.538 1.00 63.98  ? 1983 GLU A OE1   1 
ATOM   971  O  OE2   . GLU A 1 192 ? 112.479 94.905  132.482 1.00 69.75  ? 1983 GLU A OE2   1 
ATOM   972  N  N     . GLN A 1 193 ? 106.337 97.309  130.841 1.00 47.86  ? 1984 GLN A N     1 
ATOM   973  C  CA    . GLN A 1 193 ? 104.918 97.059  131.027 1.00 46.81  ? 1984 GLN A CA    1 
ATOM   974  C  C     . GLN A 1 193 ? 104.180 97.200  129.698 1.00 41.10  ? 1984 GLN A C     1 
ATOM   975  O  O     . GLN A 1 193 ? 104.781 97.394  128.639 1.00 40.77  ? 1984 GLN A O     1 
ATOM   976  C  CB    . GLN A 1 193 ? 104.348 98.009  132.076 1.00 46.46  ? 1984 GLN A CB    1 
ATOM   977  C  CG    . GLN A 1 193 ? 104.775 97.688  133.495 1.00 51.05  ? 1984 GLN A CG    1 
ATOM   978  C  CD    . GLN A 1 193 ? 105.331 98.894  134.221 1.00 53.62  ? 1984 GLN A CD    1 
ATOM   979  O  OE1   . GLN A 1 193 ? 105.833 99.830  133.599 1.00 52.63  ? 1984 GLN A OE1   1 
ATOM   980  N  NE2   . GLN A 1 193 ? 105.243 98.879  135.544 1.00 56.53  ? 1984 GLN A NE2   1 
ATOM   981  N  N     . SER A 1 194 ? 102.857 97.088  129.749 1.00 35.90  ? 1985 SER A N     1 
ATOM   982  C  CA    . SER A 1 194 ? 102.048 97.349  128.571 1.00 31.60  ? 1985 SER A CA    1 
ATOM   983  C  C     . SER A 1 194 ? 101.989 98.849  128.298 1.00 32.81  ? 1985 SER A C     1 
ATOM   984  O  O     . SER A 1 194 ? 102.209 99.677  129.184 1.00 36.70  ? 1985 SER A O     1 
ATOM   985  C  CB    . SER A 1 194 ? 100.638 96.787  128.748 1.00 33.06  ? 1985 SER A CB    1 
ATOM   986  O  OG    . SER A 1 194 ? 100.666 95.377  128.878 1.00 36.65  ? 1985 SER A OG    1 
ATOM   987  N  N     . TYR A 1 195 ? 101.697 99.194  127.048 1.00 31.31  ? 1986 TYR A N     1 
ATOM   988  C  CA    . TYR A 1 195 ? 101.649 100.581 126.611 1.00 28.24  ? 1986 TYR A CA    1 
ATOM   989  C  C     . TYR A 1 195 ? 100.296 100.877 125.984 1.00 30.55  ? 1986 TYR A C     1 
ATOM   990  O  O     . TYR A 1 195 ? 99.709  100.021 125.317 1.00 34.07  ? 1986 TYR A O     1 
ATOM   991  C  CB    . TYR A 1 195 ? 102.771 100.882 125.621 1.00 31.42  ? 1986 TYR A CB    1 
ATOM   992  C  CG    . TYR A 1 195 ? 104.067 100.187 125.956 1.00 33.84  ? 1986 TYR A CG    1 
ATOM   993  C  CD1   . TYR A 1 195 ? 104.815 100.569 127.060 1.00 31.74  ? 1986 TYR A CD1   1 
ATOM   994  C  CD2   . TYR A 1 195 ? 104.543 99.147  125.171 1.00 33.30  ? 1986 TYR A CD2   1 
ATOM   995  C  CE1   . TYR A 1 195 ? 106.002 99.939  127.370 1.00 33.98  ? 1986 TYR A CE1   1 
ATOM   996  C  CE2   . TYR A 1 195 ? 105.727 98.510  125.474 1.00 33.79  ? 1986 TYR A CE2   1 
ATOM   997  C  CZ    . TYR A 1 195 ? 106.452 98.910  126.574 1.00 35.07  ? 1986 TYR A CZ    1 
ATOM   998  O  OH    . TYR A 1 195 ? 107.632 98.276  126.879 1.00 39.72  ? 1986 TYR A OH    1 
ATOM   999  N  N     . GLU A 1 196 ? 99.800  102.089 126.216 1.00 25.94  ? 1987 GLU A N     1 
ATOM   1000 C  CA    . GLU A 1 196 ? 98.465  102.489 125.785 1.00 28.36  ? 1987 GLU A CA    1 
ATOM   1001 C  C     . GLU A 1 196 ? 98.501  103.889 125.178 1.00 28.76  ? 1987 GLU A C     1 
ATOM   1002 O  O     . GLU A 1 196 ? 97.741  104.777 125.565 1.00 34.78  ? 1987 GLU A O     1 
ATOM   1003 C  CB    . GLU A 1 196 ? 97.481  102.408 126.948 1.00 30.40  ? 1987 GLU A CB    1 
ATOM   1004 C  CG    . GLU A 1 196 ? 96.884  101.028 127.142 1.00 35.37  ? 1987 GLU A CG    1 
ATOM   1005 C  CD    . GLU A 1 196 ? 95.770  101.016 128.163 1.00 39.66  ? 1987 GLU A CD    1 
ATOM   1006 O  OE1   . GLU A 1 196 ? 95.869  101.762 129.158 1.00 37.03  ? 1987 GLU A OE1   1 
ATOM   1007 O  OE2   . GLU A 1 196 ? 94.795  100.260 127.971 1.00 45.70  ? 1987 GLU A OE2   1 
ATOM   1008 N  N     . ASP A 1 197 ? 99.417  104.099 124.235 1.00 26.27  ? 1988 ASP A N     1 
ATOM   1009 C  CA    . ASP A 1 197 ? 99.595  105.370 123.548 1.00 24.72  ? 1988 ASP A CA    1 
ATOM   1010 C  C     . ASP A 1 197 ? 98.256  105.934 123.071 1.00 24.81  ? 1988 ASP A C     1 
ATOM   1011 O  O     . ASP A 1 197 ? 97.582  105.299 122.246 1.00 25.44  ? 1988 ASP A O     1 
ATOM   1012 C  CB    . ASP A 1 197 ? 100.532 105.184 122.358 1.00 26.91  ? 1988 ASP A CB    1 
ATOM   1013 C  CG    . ASP A 1 197 ? 101.127 106.489 121.865 1.00 26.08  ? 1988 ASP A CG    1 
ATOM   1014 O  OD1   . ASP A 1 197 ? 100.547 107.559 122.134 1.00 26.48  ? 1988 ASP A OD1   1 
ATOM   1015 O  OD2   . ASP A 1 197 ? 102.168 106.440 121.180 1.00 27.07  ? 1988 ASP A OD2   1 
ATOM   1016 N  N     . PRO A 1 198 ? 97.832  107.101 123.570 1.00 25.47  ? 1989 PRO A N     1 
ATOM   1017 C  CA    . PRO A 1 198 ? 96.586  107.698 123.066 1.00 22.29  ? 1989 PRO A CA    1 
ATOM   1018 C  C     . PRO A 1 198 ? 96.635  108.056 121.593 1.00 24.23  ? 1989 PRO A C     1 
ATOM   1019 O  O     . PRO A 1 198 ? 95.600  107.984 120.920 1.00 28.11  ? 1989 PRO A O     1 
ATOM   1020 C  CB    . PRO A 1 198 ? 96.414  108.944 123.946 1.00 25.84  ? 1989 PRO A CB    1 
ATOM   1021 C  CG    . PRO A 1 198 ? 97.783  109.255 124.433 1.00 25.11  ? 1989 PRO A CG    1 
ATOM   1022 C  CD    . PRO A 1 198 ? 98.461  107.933 124.608 1.00 26.68  ? 1989 PRO A CD    1 
ATOM   1023 N  N     . LYS A 1 199 ? 97.800  108.446 121.071 1.00 25.74  ? 1990 LYS A N     1 
ATOM   1024 C  CA    . LYS A 1 199 ? 97.904  108.762 119.650 1.00 25.21  ? 1990 LYS A CA    1 
ATOM   1025 C  C     . LYS A 1 199 ? 97.605  107.540 118.795 1.00 25.72  ? 1990 LYS A C     1 
ATOM   1026 O  O     . LYS A 1 199 ? 96.933  107.641 117.760 1.00 27.00  ? 1990 LYS A O     1 
ATOM   1027 C  CB    . LYS A 1 199 ? 99.297  109.307 119.336 1.00 26.36  ? 1990 LYS A CB    1 
ATOM   1028 C  CG    . LYS A 1 199 ? 99.372  110.823 119.289 1.00 33.77  ? 1990 LYS A CG    1 
ATOM   1029 C  CD    . LYS A 1 199 ? 100.569 111.308 118.486 1.00 39.93  ? 1990 LYS A CD    1 
ATOM   1030 C  CE    . LYS A 1 199 ? 101.832 110.550 118.856 1.00 41.78  ? 1990 LYS A CE    1 
ATOM   1031 N  NZ    . LYS A 1 199 ? 103.027 111.079 118.141 1.00 43.47  ? 1990 LYS A NZ    1 
ATOM   1032 N  N     . VAL A 1 200 ? 98.095  106.373 119.215 1.00 23.07  ? 1991 VAL A N     1 
ATOM   1033 C  CA    . VAL A 1 200 ? 97.844  105.144 118.473 1.00 19.56  ? 1991 VAL A CA    1 
ATOM   1034 C  C     . VAL A 1 200 ? 96.362  104.797 118.490 1.00 21.83  ? 1991 VAL A C     1 
ATOM   1035 O  O     . VAL A 1 200 ? 95.805  104.363 117.478 1.00 25.71  ? 1991 VAL A O     1 
ATOM   1036 C  CB    . VAL A 1 200 ? 98.704  104.003 119.039 1.00 19.03  ? 1991 VAL A CB    1 
ATOM   1037 C  CG1   . VAL A 1 200 ? 98.348  102.700 118.373 1.00 21.26  ? 1991 VAL A CG1   1 
ATOM   1038 C  CG2   . VAL A 1 200 ? 100.168 104.316 118.843 1.00 18.76  ? 1991 VAL A CG2   1 
ATOM   1039 N  N     . ALA A 1 201 ? 95.699  104.974 119.635 1.00 22.08  ? 1992 ALA A N     1 
ATOM   1040 C  CA    . ALA A 1 201 ? 94.262  104.719 119.698 1.00 21.69  ? 1992 ALA A CA    1 
ATOM   1041 C  C     . ALA A 1 201 ? 93.490  105.688 118.812 1.00 25.56  ? 1992 ALA A C     1 
ATOM   1042 O  O     . ALA A 1 201 ? 92.535  105.295 118.129 1.00 28.08  ? 1992 ALA A O     1 
ATOM   1043 C  CB    . ALA A 1 201 ? 93.776  104.807 121.143 1.00 24.42  ? 1992 ALA A CB    1 
ATOM   1044 N  N     . CYS A 1 202 ? 93.892  106.961 118.810 1.00 28.23  ? 1993 CYS A N     1 
ATOM   1045 C  CA    . CYS A 1 202 ? 93.248  107.941 117.942 1.00 25.84  ? 1993 CYS A CA    1 
ATOM   1046 C  C     . CYS A 1 202 ? 93.405  107.560 116.478 1.00 26.03  ? 1993 CYS A C     1 
ATOM   1047 O  O     . CYS A 1 202 ? 92.458  107.680 115.692 1.00 29.61  ? 1993 CYS A O     1 
ATOM   1048 C  CB    . CYS A 1 202 ? 93.831  109.330 118.193 1.00 28.02  ? 1993 CYS A CB    1 
ATOM   1049 S  SG    . CYS A 1 202 ? 93.457  110.014 119.814 1.00 28.29  ? 1993 CYS A SG    1 
ATOM   1050 N  N     . TRP A 1 203 ? 94.599  107.108 116.089 1.00 26.51  ? 1994 TRP A N     1 
ATOM   1051 C  CA    . TRP A 1 203 ? 94.792  106.634 114.723 1.00 28.48  ? 1994 TRP A CA    1 
ATOM   1052 C  C     . TRP A 1 203 ? 93.932  105.411 114.439 1.00 28.35  ? 1994 TRP A C     1 
ATOM   1053 O  O     . TRP A 1 203 ? 93.335  105.300 113.365 1.00 31.64  ? 1994 TRP A O     1 
ATOM   1054 C  CB    . TRP A 1 203 ? 96.261  106.312 114.467 1.00 26.92  ? 1994 TRP A CB    1 
ATOM   1055 C  CG    . TRP A 1 203 ? 96.456  105.569 113.186 1.00 27.26  ? 1994 TRP A CG    1 
ATOM   1056 C  CD1   . TRP A 1 203 ? 96.417  106.088 111.927 1.00 30.19  ? 1994 TRP A CD1   1 
ATOM   1057 C  CD2   . TRP A 1 203 ? 96.689  104.167 113.035 1.00 28.06  ? 1994 TRP A CD2   1 
ATOM   1058 N  NE1   . TRP A 1 203 ? 96.624  105.098 111.000 1.00 28.36  ? 1994 TRP A NE1   1 
ATOM   1059 C  CE2   . TRP A 1 203 ? 96.793  103.907 111.656 1.00 29.19  ? 1994 TRP A CE2   1 
ATOM   1060 C  CE3   . TRP A 1 203 ? 96.826  103.105 113.932 1.00 28.12  ? 1994 TRP A CE3   1 
ATOM   1061 C  CZ2   . TRP A 1 203 ? 97.028  102.633 111.154 1.00 27.24  ? 1994 TRP A CZ2   1 
ATOM   1062 C  CZ3   . TRP A 1 203 ? 97.058  101.843 113.431 1.00 28.10  ? 1994 TRP A CZ3   1 
ATOM   1063 C  CH2   . TRP A 1 203 ? 97.158  101.617 112.056 1.00 27.05  ? 1994 TRP A CH2   1 
ATOM   1064 N  N     . LEU A 1 204 ? 93.859  104.480 115.391 1.00 26.61  ? 1995 LEU A N     1 
ATOM   1065 C  CA    . LEU A 1 204 ? 93.074  103.267 115.188 1.00 24.90  ? 1995 LEU A CA    1 
ATOM   1066 C  C     . LEU A 1 204 ? 91.605  103.596 114.965 1.00 27.34  ? 1995 LEU A C     1 
ATOM   1067 O  O     . LEU A 1 204 ? 90.920  102.918 114.190 1.00 27.50  ? 1995 LEU A O     1 
ATOM   1068 C  CB    . LEU A 1 204 ? 93.238  102.331 116.383 1.00 26.08  ? 1995 LEU A CB    1 
ATOM   1069 C  CG    . LEU A 1 204 ? 93.242  100.833 116.083 1.00 22.93  ? 1995 LEU A CG    1 
ATOM   1070 C  CD1   . LEU A 1 204 ? 94.595  100.398 115.557 1.00 24.76  ? 1995 LEU A CD1   1 
ATOM   1071 C  CD2   . LEU A 1 204 ? 92.869  100.042 117.321 1.00 26.06  ? 1995 LEU A CD2   1 
ATOM   1072 N  N     . LEU A 1 205 ? 91.100  104.627 115.644 1.00 31.14  ? 1996 LEU A N     1 
ATOM   1073 C  CA    . LEU A 1 205 ? 89.722  105.050 115.414 1.00 33.26  ? 1996 LEU A CA    1 
ATOM   1074 C  C     . LEU A 1 205 ? 89.541  105.601 114.003 1.00 35.06  ? 1996 LEU A C     1 
ATOM   1075 O  O     . LEU A 1 205 ? 88.627  105.194 113.278 1.00 38.73  ? 1996 LEU A O     1 
ATOM   1076 C  CB    . LEU A 1 205 ? 89.311  106.089 116.458 1.00 34.43  ? 1996 LEU A CB    1 
ATOM   1077 C  CG    . LEU A 1 205 ? 89.294  105.624 117.915 1.00 30.71  ? 1996 LEU A CG    1 
ATOM   1078 C  CD1   . LEU A 1 205 ? 88.606  106.653 118.790 1.00 31.03  ? 1996 LEU A CD1   1 
ATOM   1079 C  CD2   . LEU A 1 205 ? 88.599  104.281 118.029 1.00 28.87  ? 1996 LEU A CD2   1 
ATOM   1080 N  N     . ASP A 1 206 ? 90.409  106.528 113.594 1.00 35.33  ? 1997 ASP A N     1 
ATOM   1081 C  CA    . ASP A 1 206 ? 90.313  107.198 112.296 1.00 36.71  ? 1997 ASP A CA    1 
ATOM   1082 C  C     . ASP A 1 206 ? 91.677  107.168 111.618 1.00 36.17  ? 1997 ASP A C     1 
ATOM   1083 O  O     . ASP A 1 206 ? 92.451  108.130 111.713 1.00 36.12  ? 1997 ASP A O     1 
ATOM   1084 C  CB    . ASP A 1 206 ? 89.805  108.631 112.457 1.00 39.09  ? 1997 ASP A CB    1 
ATOM   1085 C  CG    . ASP A 1 206 ? 89.048  109.121 111.242 1.00 44.33  ? 1997 ASP A CG    1 
ATOM   1086 O  OD1   . ASP A 1 206 ? 89.497  108.848 110.111 1.00 45.09  ? 1997 ASP A OD1   1 
ATOM   1087 O  OD2   . ASP A 1 206 ? 88.001  109.779 111.418 1.00 47.02  ? 1997 ASP A OD2   1 
ATOM   1088 N  N     . PRO A 1 207 ? 92.009  106.071 110.932 1.00 35.52  ? 1998 PRO A N     1 
ATOM   1089 C  CA    . PRO A 1 207 ? 93.348  105.960 110.326 1.00 33.76  ? 1998 PRO A CA    1 
ATOM   1090 C  C     . PRO A 1 207 ? 93.644  107.006 109.266 1.00 37.45  ? 1998 PRO A C     1 
ATOM   1091 O  O     . PRO A 1 207 ? 94.799  107.432 109.143 1.00 36.96  ? 1998 PRO A O     1 
ATOM   1092 C  CB    . PRO A 1 207 ? 93.348  104.543 109.737 1.00 33.03  ? 1998 PRO A CB    1 
ATOM   1093 C  CG    . PRO A 1 207 ? 91.913  104.202 109.561 1.00 37.40  ? 1998 PRO A CG    1 
ATOM   1094 C  CD    . PRO A 1 207 ? 91.182  104.882 110.674 1.00 37.70  ? 1998 PRO A CD    1 
ATOM   1095 N  N     . ASP A 1 208 ? 92.648  107.436 108.497 1.00 42.02  ? 1999 ASP A N     1 
ATOM   1096 C  CA    . ASP A 1 208 ? 92.865  108.397 107.424 1.00 43.48  ? 1999 ASP A CA    1 
ATOM   1097 C  C     . ASP A 1 208 ? 92.692  109.841 107.880 1.00 46.86  ? 1999 ASP A C     1 
ATOM   1098 O  O     . ASP A 1 208 ? 92.744  110.752 107.047 1.00 49.56  ? 1999 ASP A O     1 
ATOM   1099 C  CB    . ASP A 1 208 ? 91.933  108.101 106.243 1.00 41.91  ? 1999 ASP A CB    1 
ATOM   1100 C  CG    . ASP A 1 208 ? 90.472  108.332 106.572 1.00 52.08  ? 1999 ASP A CG    1 
ATOM   1101 O  OD1   . ASP A 1 208 ? 89.994  107.801 107.595 1.00 49.86  ? 1999 ASP A OD1   1 
ATOM   1102 O  OD2   . ASP A 1 208 ? 89.796  109.046 105.801 1.00 57.16  ? 1999 ASP A OD2   1 
ATOM   1103 N  N     . SER A 1 209 ? 92.489  110.071 109.174 1.00 44.74  ? 2000 SER A N     1 
ATOM   1104 C  CA    . SER A 1 209 ? 92.429  111.419 109.710 1.00 44.84  ? 2000 SER A CA    1 
ATOM   1105 C  C     . SER A 1 209 ? 93.833  112.009 109.828 1.00 47.75  ? 2000 SER A C     1 
ATOM   1106 O  O     . SER A 1 209 ? 94.844  111.322 109.660 1.00 47.58  ? 2000 SER A O     1 
ATOM   1107 C  CB    . SER A 1 209 ? 91.736  111.425 111.071 1.00 46.62  ? 2000 SER A CB    1 
ATOM   1108 O  OG    . SER A 1 209 ? 92.685  111.443 112.123 1.00 49.72  ? 2000 SER A OG    1 
ATOM   1109 N  N     . GLN A 1 210 ? 93.888  113.305 110.124 1.00 50.42  ? 2001 GLN A N     1 
ATOM   1110 C  CA    . GLN A 1 210 ? 95.165  113.984 110.260 1.00 49.31  ? 2001 GLN A CA    1 
ATOM   1111 C  C     . GLN A 1 210 ? 95.875  113.535 111.536 1.00 46.11  ? 2001 GLN A C     1 
ATOM   1112 O  O     . GLN A 1 210 ? 95.307  112.846 112.389 1.00 45.52  ? 2001 GLN A O     1 
ATOM   1113 C  CB    . GLN A 1 210 ? 94.970  115.500 110.261 1.00 50.04  ? 2001 GLN A CB    1 
ATOM   1114 C  CG    . GLN A 1 210 ? 93.805  115.979 111.108 1.00 53.02  ? 2001 GLN A CG    1 
ATOM   1115 C  CD    . GLN A 1 210 ? 93.736  117.491 111.199 1.00 59.16  ? 2001 GLN A CD    1 
ATOM   1116 O  OE1   . GLN A 1 210 ? 94.659  118.191 110.781 1.00 63.10  ? 2001 GLN A OE1   1 
ATOM   1117 N  NE2   . GLN A 1 210 ? 92.641  118.002 111.748 1.00 58.05  ? 2001 GLN A NE2   1 
ATOM   1118 N  N     . GLU A 1 211 ? 97.137  113.931 111.655 1.00 44.98  ? 2002 GLU A N     1 
ATOM   1119 C  CA    . GLU A 1 211 ? 97.936  113.544 112.809 1.00 41.50  ? 2002 GLU A CA    1 
ATOM   1120 C  C     . GLU A 1 211 ? 97.307  114.094 114.084 1.00 44.17  ? 2002 GLU A C     1 
ATOM   1121 O  O     . GLU A 1 211 ? 97.004  115.293 114.152 1.00 48.07  ? 2002 GLU A O     1 
ATOM   1122 C  CB    . GLU A 1 211 ? 99.367  114.057 112.664 1.00 45.09  ? 2002 GLU A CB    1 
ATOM   1123 C  CG    . GLU A 1 211 ? 100.087 113.549 111.429 1.00 46.22  ? 2002 GLU A CG    1 
ATOM   1124 C  CD    . GLU A 1 211 ? 101.145 112.519 111.762 1.00 49.89  ? 2002 GLU A CD    1 
ATOM   1125 O  OE1   . GLU A 1 211 ? 101.442 112.340 112.961 1.00 47.49  ? 2002 GLU A OE1   1 
ATOM   1126 O  OE2   . GLU A 1 211 ? 101.679 111.890 110.825 1.00 49.87  ? 2002 GLU A OE2   1 
ATOM   1127 N  N     . PRO A 1 212 ? 97.096  113.268 115.106 1.00 42.25  ? 2003 PRO A N     1 
ATOM   1128 C  CA    . PRO A 1 212 ? 96.382  113.721 116.305 1.00 42.06  ? 2003 PRO A CA    1 
ATOM   1129 C  C     . PRO A 1 212 ? 97.297  114.529 117.213 1.00 43.74  ? 2003 PRO A C     1 
ATOM   1130 O  O     . PRO A 1 212 ? 98.179  113.981 117.879 1.00 42.92  ? 2003 PRO A O     1 
ATOM   1131 C  CB    . PRO A 1 212 ? 95.936  112.406 116.963 1.00 35.68  ? 2003 PRO A CB    1 
ATOM   1132 C  CG    . PRO A 1 212 ? 96.587  111.286 116.168 1.00 39.13  ? 2003 PRO A CG    1 
ATOM   1133 C  CD    . PRO A 1 212 ? 97.604  111.900 115.266 1.00 41.53  ? 2003 PRO A CD    1 
ATOM   1134 N  N     . THR A 1 213 ? 97.085  115.840 117.238 1.00 45.52  ? 2004 THR A N     1 
ATOM   1135 C  CA    . THR A 1 213 ? 97.767  116.674 118.211 1.00 44.97  ? 2004 THR A CA    1 
ATOM   1136 C  C     . THR A 1 213 ? 97.164  116.453 119.591 1.00 47.27  ? 2004 THR A C     1 
ATOM   1137 O  O     . THR A 1 213 ? 96.058  115.929 119.736 1.00 47.22  ? 2004 THR A O     1 
ATOM   1138 C  CB    . THR A 1 213 ? 97.665  118.151 117.828 1.00 50.93  ? 2004 THR A CB    1 
ATOM   1139 O  OG1   . THR A 1 213 ? 96.383  118.408 117.244 1.00 56.18  ? 2004 THR A OG1   1 
ATOM   1140 C  CG2   . THR A 1 213 ? 98.747  118.518 116.833 1.00 54.76  ? 2004 THR A CG2   1 
ATOM   1141 N  N     . LEU A 1 214 ? 97.908  116.862 120.617 1.00 48.88  ? 2005 LEU A N     1 
ATOM   1142 C  CA    . LEU A 1 214 ? 97.404  116.735 121.979 1.00 46.29  ? 2005 LEU A CA    1 
ATOM   1143 C  C     . LEU A 1 214 ? 96.112  117.523 122.150 1.00 50.26  ? 2005 LEU A C     1 
ATOM   1144 O  O     . LEU A 1 214 ? 95.133  117.019 122.716 1.00 51.75  ? 2005 LEU A O     1 
ATOM   1145 C  CB    . LEU A 1 214 ? 98.467  117.210 122.966 1.00 42.06  ? 2005 LEU A CB    1 
ATOM   1146 C  CG    . LEU A 1 214 ? 98.616  116.477 124.297 1.00 39.06  ? 2005 LEU A CG    1 
ATOM   1147 C  CD1   . LEU A 1 214 ? 99.839  117.011 125.003 1.00 44.32  ? 2005 LEU A CD1   1 
ATOM   1148 C  CD2   . LEU A 1 214 ? 97.384  116.631 125.169 1.00 33.59  ? 2005 LEU A CD2   1 
ATOM   1149 N  N     . HIS A 1 215 ? 96.083  118.752 121.633 1.00 51.37  ? 2006 HIS A N     1 
ATOM   1150 C  CA    . HIS A 1 215 ? 94.868  119.554 121.700 1.00 52.79  ? 2006 HIS A CA    1 
ATOM   1151 C  C     . HIS A 1 215 ? 93.732  118.893 120.932 1.00 53.76  ? 2006 HIS A C     1 
ATOM   1152 O  O     . HIS A 1 215 ? 92.570  118.981 121.340 1.00 54.50  ? 2006 HIS A O     1 
ATOM   1153 C  CB    . HIS A 1 215 ? 95.137  120.960 121.166 1.00 54.24  ? 2006 HIS A CB    1 
ATOM   1154 C  CG    . HIS A 1 215 ? 93.963  121.882 121.276 1.00 57.56  ? 2006 HIS A CG    1 
ATOM   1155 N  ND1   . HIS A 1 215 ? 92.982  121.954 120.311 1.00 59.66  ? 2006 HIS A ND1   1 
ATOM   1156 C  CD2   . HIS A 1 215 ? 93.612  122.767 122.237 1.00 57.14  ? 2006 HIS A CD2   1 
ATOM   1157 C  CE1   . HIS A 1 215 ? 92.077  122.845 120.673 1.00 59.51  ? 2006 HIS A CE1   1 
ATOM   1158 N  NE2   . HIS A 1 215 ? 92.435  123.353 121.838 1.00 59.31  ? 2006 HIS A NE2   1 
ATOM   1159 N  N     . SER A 1 216 ? 94.044  118.228 119.817 1.00 53.34  ? 2007 SER A N     1 
ATOM   1160 C  CA    . SER A 1 216 ? 92.999  117.563 119.043 1.00 54.73  ? 2007 SER A CA    1 
ATOM   1161 C  C     . SER A 1 216 ? 92.350  116.438 119.838 1.00 53.87  ? 2007 SER A C     1 
ATOM   1162 O  O     . SER A 1 216 ? 91.119  116.318 119.866 1.00 57.53  ? 2007 SER A O     1 
ATOM   1163 C  CB    . SER A 1 216 ? 93.575  117.026 117.734 1.00 52.28  ? 2007 SER A CB    1 
ATOM   1164 O  OG    . SER A 1 216 ? 92.582  116.356 116.976 1.00 53.05  ? 2007 SER A OG    1 
ATOM   1165 N  N     . ILE A 1 217 ? 93.161  115.604 120.494 1.00 51.11  ? 2008 ILE A N     1 
ATOM   1166 C  CA    . ILE A 1 217 ? 92.612  114.535 121.323 1.00 51.99  ? 2008 ILE A CA    1 
ATOM   1167 C  C     . ILE A 1 217 ? 91.812  115.108 122.480 1.00 53.55  ? 2008 ILE A C     1 
ATOM   1168 O  O     . ILE A 1 217 ? 90.729  114.609 122.807 1.00 54.84  ? 2008 ILE A O     1 
ATOM   1169 C  CB    . ILE A 1 217 ? 93.728  113.599 121.820 1.00 48.92  ? 2008 ILE A CB    1 
ATOM   1170 C  CG1   . ILE A 1 217 ? 94.715  113.299 120.695 1.00 51.48  ? 2008 ILE A CG1   1 
ATOM   1171 C  CG2   . ILE A 1 217 ? 93.139  112.342 122.437 1.00 43.17  ? 2008 ILE A CG2   1 
ATOM   1172 C  CD1   . ILE A 1 217 ? 96.043  112.827 121.178 1.00 41.83  ? 2008 ILE A CD1   1 
ATOM   1173 N  N     . VAL A 1 218 ? 92.330  116.154 123.124 1.00 53.36  ? 2009 VAL A N     1 
ATOM   1174 C  CA    . VAL A 1 218 ? 91.612  116.726 124.258 1.00 52.59  ? 2009 VAL A CA    1 
ATOM   1175 C  C     . VAL A 1 218 ? 90.274  117.301 123.808 1.00 57.96  ? 2009 VAL A C     1 
ATOM   1176 O  O     . VAL A 1 218 ? 89.260  117.159 124.498 1.00 63.69  ? 2009 VAL A O     1 
ATOM   1177 C  CB    . VAL A 1 218 ? 92.479  117.776 124.974 1.00 52.68  ? 2009 VAL A CB    1 
ATOM   1178 C  CG1   . VAL A 1 218 ? 91.712  118.391 126.128 1.00 60.47  ? 2009 VAL A CG1   1 
ATOM   1179 C  CG2   . VAL A 1 218 ? 93.748  117.131 125.482 1.00 49.12  ? 2009 VAL A CG2   1 
ATOM   1180 N  N     . THR A 1 219 ? 90.244  117.950 122.643 1.00 55.01  ? 2010 THR A N     1 
ATOM   1181 C  CA    . THR A 1 219 ? 88.990  118.495 122.133 1.00 57.20  ? 2010 THR A CA    1 
ATOM   1182 C  C     . THR A 1 219 ? 88.008  117.391 121.757 1.00 59.26  ? 2010 THR A C     1 
ATOM   1183 O  O     . THR A 1 219 ? 86.813  117.486 122.060 1.00 62.76  ? 2010 THR A O     1 
ATOM   1184 C  CB    . THR A 1 219 ? 89.262  119.396 120.928 1.00 55.61  ? 2010 THR A CB    1 
ATOM   1185 O  OG1   . THR A 1 219 ? 90.142  120.458 121.314 1.00 56.72  ? 2010 THR A OG1   1 
ATOM   1186 C  CG2   . THR A 1 219 ? 87.966  119.989 120.397 1.00 58.85  ? 2010 THR A CG2   1 
ATOM   1187 N  N     . SER A 1 220 ? 88.490  116.334 121.105 1.00 56.02  ? 2011 SER A N     1 
ATOM   1188 C  CA    . SER A 1 220 ? 87.604  115.339 120.516 1.00 56.53  ? 2011 SER A CA    1 
ATOM   1189 C  C     . SER A 1 220 ? 87.205  114.221 121.471 1.00 56.78  ? 2011 SER A C     1 
ATOM   1190 O  O     . SER A 1 220 ? 86.251  113.495 121.175 1.00 57.47  ? 2011 SER A O     1 
ATOM   1191 C  CB    . SER A 1 220 ? 88.259  114.726 119.273 1.00 55.94  ? 2011 SER A CB    1 
ATOM   1192 O  OG    . SER A 1 220 ? 87.358  113.875 118.586 1.00 57.41  ? 2011 SER A OG    1 
ATOM   1193 N  N     . PHE A 1 221 ? 87.891  114.059 122.601 1.00 56.55  ? 2012 PHE A N     1 
ATOM   1194 C  CA    . PHE A 1 221 ? 87.608  112.914 123.458 1.00 55.62  ? 2012 PHE A CA    1 
ATOM   1195 C  C     . PHE A 1 221 ? 87.418  113.312 124.916 1.00 56.27  ? 2012 PHE A C     1 
ATOM   1196 O  O     . PHE A 1 221 ? 86.750  112.600 125.673 1.00 56.48  ? 2012 PHE A O     1 
ATOM   1197 C  CB    . PHE A 1 221 ? 88.727  111.878 123.333 1.00 50.84  ? 2012 PHE A CB    1 
ATOM   1198 C  CG    . PHE A 1 221 ? 88.846  111.285 121.958 1.00 50.96  ? 2012 PHE A CG    1 
ATOM   1199 C  CD1   . PHE A 1 221 ? 87.767  110.654 121.366 1.00 49.41  ? 2012 PHE A CD1   1 
ATOM   1200 C  CD2   . PHE A 1 221 ? 90.033  111.365 121.254 1.00 49.83  ? 2012 PHE A CD2   1 
ATOM   1201 C  CE1   . PHE A 1 221 ? 87.873  110.113 120.099 1.00 46.61  ? 2012 PHE A CE1   1 
ATOM   1202 C  CE2   . PHE A 1 221 ? 90.144  110.826 119.989 1.00 45.95  ? 2012 PHE A CE2   1 
ATOM   1203 C  CZ    . PHE A 1 221 ? 89.063  110.198 119.411 1.00 44.99  ? 2012 PHE A CZ    1 
ATOM   1204 N  N     . LEU A 1 222 ? 88.001  114.435 125.327 1.00 57.85  ? 2013 LEU A N     1 
ATOM   1205 C  CA    . LEU A 1 222 ? 87.904  114.919 126.704 1.00 60.54  ? 2013 LEU A CA    1 
ATOM   1206 C  C     . LEU A 1 222 ? 87.595  116.413 126.712 1.00 61.65  ? 2013 LEU A C     1 
ATOM   1207 O  O     . LEU A 1 222 ? 88.409  117.223 127.172 1.00 61.06  ? 2013 LEU A O     1 
ATOM   1208 C  CB    . LEU A 1 222 ? 89.201  114.620 127.455 1.00 58.55  ? 2013 LEU A CB    1 
ATOM   1209 C  CG    . LEU A 1 222 ? 89.185  114.554 128.977 1.00 57.39  ? 2013 LEU A CG    1 
ATOM   1210 C  CD1   . LEU A 1 222 ? 88.390  113.351 129.444 1.00 57.97  ? 2013 LEU A CD1   1 
ATOM   1211 C  CD2   . LEU A 1 222 ? 90.613  114.481 129.480 1.00 53.11  ? 2013 LEU A CD2   1 
ATOM   1212 N  N     . PRO A 1 223 ? 86.425  116.817 126.200 1.00 63.70  ? 2014 PRO A N     1 
ATOM   1213 C  CA    . PRO A 1 223 ? 86.138  118.260 126.107 1.00 67.68  ? 2014 PRO A CA    1 
ATOM   1214 C  C     . PRO A 1 223 ? 86.115  118.976 127.447 1.00 72.73  ? 2014 PRO A C     1 
ATOM   1215 O  O     . PRO A 1 223 ? 86.574  120.122 127.538 1.00 71.20  ? 2014 PRO A O     1 
ATOM   1216 C  CB    . PRO A 1 223 ? 84.760  118.296 125.430 1.00 70.16  ? 2014 PRO A CB    1 
ATOM   1217 C  CG    . PRO A 1 223 ? 84.660  117.007 124.699 1.00 64.68  ? 2014 PRO A CG    1 
ATOM   1218 C  CD    . PRO A 1 223 ? 85.366  116.011 125.568 1.00 65.89  ? 2014 PRO A CD    1 
ATOM   1219 N  N     . HIS A 1 224 ? 85.602  118.328 128.497 1.00 72.85  ? 2015 HIS A N     1 
ATOM   1220 C  CA    . HIS A 1 224 ? 85.425  119.000 129.780 1.00 71.57  ? 2015 HIS A CA    1 
ATOM   1221 C  C     . HIS A 1 224 ? 86.747  119.408 130.415 1.00 73.15  ? 2015 HIS A C     1 
ATOM   1222 O  O     . HIS A 1 224 ? 86.770  120.341 131.224 1.00 77.71  ? 2015 HIS A O     1 
ATOM   1223 C  CB    . HIS A 1 224 ? 84.647  118.100 130.741 1.00 73.19  ? 2015 HIS A CB    1 
ATOM   1224 C  CG    . HIS A 1 224 ? 85.432  116.927 131.242 1.00 76.45  ? 2015 HIS A CG    1 
ATOM   1225 N  ND1   . HIS A 1 224 ? 86.280  117.006 132.325 1.00 77.58  ? 2015 HIS A ND1   1 
ATOM   1226 C  CD2   . HIS A 1 224 ? 85.494  115.646 130.808 1.00 74.39  ? 2015 HIS A CD2   1 
ATOM   1227 C  CE1   . HIS A 1 224 ? 86.833  115.824 132.536 1.00 75.59  ? 2015 HIS A CE1   1 
ATOM   1228 N  NE2   . HIS A 1 224 ? 86.372  114.982 131.630 1.00 74.31  ? 2015 HIS A NE2   1 
ATOM   1229 N  N     . GLU A 1 225 ? 87.837  118.734 130.068 1.00 71.58  ? 2016 GLU A N     1 
ATOM   1230 C  CA    . GLU A 1 225 ? 89.161  119.043 130.586 1.00 70.03  ? 2016 GLU A CA    1 
ATOM   1231 C  C     . GLU A 1 225 ? 89.891  120.050 129.698 1.00 69.42  ? 2016 GLU A C     1 
ATOM   1232 O  O     . GLU A 1 225 ? 90.995  120.488 130.038 1.00 71.97  ? 2016 GLU A O     1 
ATOM   1233 C  CB    . GLU A 1 225 ? 89.938  117.723 130.745 1.00 70.40  ? 2016 GLU A CB    1 
ATOM   1234 C  CG    . GLU A 1 225 ? 91.448  117.777 130.860 1.00 66.28  ? 2016 GLU A CG    1 
ATOM   1235 C  CD    . GLU A 1 225 ? 91.916  118.002 132.282 1.00 67.27  ? 2016 GLU A CD    1 
ATOM   1236 O  OE1   . GLU A 1 225 ? 92.993  118.605 132.466 1.00 66.88  ? 2016 GLU A OE1   1 
ATOM   1237 O  OE2   . GLU A 1 225 ? 91.210  117.570 133.217 1.00 65.60  ? 2016 GLU A OE2   1 
ATOM   1238 N  N     . LEU A 1 226 ? 89.255  120.476 128.606 1.00 69.05  ? 2017 LEU A N     1 
ATOM   1239 C  CA    . LEU A 1 226 ? 89.841  121.466 127.703 1.00 72.04  ? 2017 LEU A CA    1 
ATOM   1240 C  C     . LEU A 1 226 ? 90.329  122.750 128.370 1.00 73.04  ? 2017 LEU A C     1 
ATOM   1241 O  O     . LEU A 1 226 ? 91.441  123.191 128.034 1.00 70.10  ? 2017 LEU A O     1 
ATOM   1242 C  CB    . LEU A 1 226 ? 88.824  121.811 126.605 1.00 69.70  ? 2017 LEU A CB    1 
ATOM   1243 C  CG    . LEU A 1 226 ? 89.364  122.254 125.242 1.00 64.14  ? 2017 LEU A CG    1 
ATOM   1244 C  CD1   . LEU A 1 226 ? 90.706  121.612 124.935 1.00 61.16  ? 2017 LEU A CD1   1 
ATOM   1245 C  CD2   . LEU A 1 226 ? 88.357  121.947 124.145 1.00 62.95  ? 2017 LEU A CD2   1 
ATOM   1246 N  N     . PRO A 1 227 ? 89.590  123.402 129.278 1.00 75.68  ? 2018 PRO A N     1 
ATOM   1247 C  CA    . PRO A 1 227 ? 90.082  124.681 129.817 1.00 77.33  ? 2018 PRO A CA    1 
ATOM   1248 C  C     . PRO A 1 227 ? 91.379  124.567 130.598 1.00 78.30  ? 2018 PRO A C     1 
ATOM   1249 O  O     . PRO A 1 227 ? 92.029  125.593 130.836 1.00 79.00  ? 2018 PRO A O     1 
ATOM   1250 C  CB    . PRO A 1 227 ? 88.925  125.160 130.702 1.00 75.98  ? 2018 PRO A CB    1 
ATOM   1251 C  CG    . PRO A 1 227 ? 88.232  123.927 131.111 1.00 73.17  ? 2018 PRO A CG    1 
ATOM   1252 C  CD    . PRO A 1 227 ? 88.338  122.990 129.941 1.00 74.52  ? 2018 PRO A CD    1 
ATOM   1253 N  N     . LEU A 1 228 ? 91.779  123.362 131.012 1.00 75.39  ? 2019 LEU A N     1 
ATOM   1254 C  CA    . LEU A 1 228 ? 93.084  123.193 131.642 1.00 72.14  ? 2019 LEU A CA    1 
ATOM   1255 C  C     . LEU A 1 228 ? 94.229  123.482 130.679 1.00 75.51  ? 2019 LEU A C     1 
ATOM   1256 O  O     . LEU A 1 228 ? 95.360  123.696 131.128 1.00 75.94  ? 2019 LEU A O     1 
ATOM   1257 C  CB    . LEU A 1 228 ? 93.223  121.779 132.203 1.00 69.33  ? 2019 LEU A CB    1 
ATOM   1258 C  CG    . LEU A 1 228 ? 93.134  121.643 133.724 1.00 74.92  ? 2019 LEU A CG    1 
ATOM   1259 C  CD1   . LEU A 1 228 ? 94.374  122.222 134.384 1.00 77.17  ? 2019 LEU A CD1   1 
ATOM   1260 C  CD2   . LEU A 1 228 ? 91.876  122.316 134.253 1.00 75.35  ? 2019 LEU A CD2   1 
ATOM   1261 N  N     . LEU A 1 229 ? 93.962  123.487 129.372 1.00 77.37  ? 2020 LEU A N     1 
ATOM   1262 C  CA    . LEU A 1 229 ? 94.948  123.839 128.359 1.00 75.88  ? 2020 LEU A CA    1 
ATOM   1263 C  C     . LEU A 1 229 ? 94.839  125.299 127.932 1.00 78.20  ? 2020 LEU A C     1 
ATOM   1264 O  O     . LEU A 1 229 ? 95.183  125.641 126.795 1.00 78.14  ? 2020 LEU A O     1 
ATOM   1265 C  CB    . LEU A 1 229 ? 94.811  122.923 127.142 1.00 68.86  ? 2020 LEU A CB    1 
ATOM   1266 C  CG    . LEU A 1 229 ? 95.344  121.500 127.289 1.00 60.37  ? 2020 LEU A CG    1 
ATOM   1267 C  CD1   . LEU A 1 229 ? 95.075  120.693 126.031 1.00 52.58  ? 2020 LEU A CD1   1 
ATOM   1268 C  CD2   . LEU A 1 229 ? 96.825  121.536 127.595 1.00 61.70  ? 2020 LEU A CD2   1 
ATOM   1269 N  N     . GLU A 1 230 ? 94.362  126.166 128.822 1.00 80.26  ? 2021 GLU A N     1 
ATOM   1270 C  CA    . GLU A 1 230 ? 94.206  127.574 128.487 1.00 82.84  ? 2021 GLU A CA    1 
ATOM   1271 C  C     . GLU A 1 230 ? 95.571  128.229 128.326 1.00 84.60  ? 2021 GLU A C     1 
ATOM   1272 O  O     . GLU A 1 230 ? 96.443  128.096 129.190 1.00 83.45  ? 2021 GLU A O     1 
ATOM   1273 C  CB    . GLU A 1 230 ? 93.395  128.289 129.566 1.00 85.29  ? 2021 GLU A CB    1 
ATOM   1274 C  CG    . GLU A 1 230 ? 93.049  129.732 129.233 1.00 91.55  ? 2021 GLU A CG    1 
ATOM   1275 C  CD    . GLU A 1 230 ? 92.093  130.347 130.236 1.00 94.67  ? 2021 GLU A CD    1 
ATOM   1276 O  OE1   . GLU A 1 230 ? 91.655  129.630 131.160 1.00 96.81  ? 2021 GLU A OE1   1 
ATOM   1277 O  OE2   . GLU A 1 230 ? 91.780  131.549 130.101 1.00 92.87  ? 2021 GLU A OE2   1 
ATOM   1278 N  N     . GLY A 1 231 ? 95.756  128.935 127.212 1.00 83.86  ? 2022 GLY A N     1 
ATOM   1279 C  CA    . GLY A 1 231 ? 97.023  129.579 126.934 1.00 82.95  ? 2022 GLY A CA    1 
ATOM   1280 C  C     . GLY A 1 231 ? 98.162  128.638 126.624 1.00 81.81  ? 2022 GLY A C     1 
ATOM   1281 O  O     . GLY A 1 231 ? 99.309  129.086 126.531 1.00 80.05  ? 2022 GLY A O     1 
ATOM   1282 N  N     . MET A 1 232 ? 97.884  127.345 126.460 1.00 86.36  ? 2023 MET A N     1 
ATOM   1283 C  CA    . MET A 1 232 ? 98.916  126.347 126.190 1.00 85.69  ? 2023 MET A CA    1 
ATOM   1284 C  C     . MET A 1 232 ? 98.933  126.071 124.689 1.00 83.53  ? 2023 MET A C     1 
ATOM   1285 O  O     . MET A 1 232 ? 98.459  125.041 124.209 1.00 76.96  ? 2023 MET A O     1 
ATOM   1286 C  CB    . MET A 1 232 ? 98.656  125.081 127.001 1.00 80.32  ? 2023 MET A CB    1 
ATOM   1287 C  CG    . MET A 1 232 ? 98.683  125.300 128.505 1.00 81.53  ? 2023 MET A CG    1 
ATOM   1288 S  SD    . MET A 1 232 ? 99.023  123.797 129.438 1.00 84.72  ? 2023 MET A SD    1 
ATOM   1289 C  CE    . MET A 1 232 ? 100.768 124.001 129.771 1.00 71.36  ? 2023 MET A CE    1 
ATOM   1290 N  N     . GLU A 1 233 ? 99.495  127.019 123.939 1.00 84.09  ? 2024 GLU A N     1 
ATOM   1291 C  CA    . GLU A 1 233 ? 99.600  126.873 122.494 1.00 82.01  ? 2024 GLU A CA    1 
ATOM   1292 C  C     . GLU A 1 233 ? 100.720 125.932 122.075 1.00 79.53  ? 2024 GLU A C     1 
ATOM   1293 O  O     . GLU A 1 233 ? 100.799 125.577 120.894 1.00 76.58  ? 2024 GLU A O     1 
ATOM   1294 C  CB    . GLU A 1 233 ? 99.806  128.239 121.833 1.00 83.64  ? 2024 GLU A CB    1 
ATOM   1295 C  CG    . GLU A 1 233 ? 101.213 128.798 121.969 1.00 86.45  ? 2024 GLU A CG    1 
ATOM   1296 C  CD    . GLU A 1 233 ? 101.376 129.678 123.192 1.00 91.31  ? 2024 GLU A CD    1 
ATOM   1297 O  OE1   . GLU A 1 233 ? 100.371 129.919 123.893 1.00 91.34  ? 2024 GLU A OE1   1 
ATOM   1298 O  OE2   . GLU A 1 233 ? 102.509 130.135 123.449 1.00 92.86  ? 2024 GLU A OE2   1 
ATOM   1299 N  N     . THR A 1 234 ? 101.586 125.525 123.007 1.00 78.71  ? 2025 THR A N     1 
ATOM   1300 C  CA    . THR A 1 234 ? 102.645 124.579 122.681 1.00 74.33  ? 2025 THR A CA    1 
ATOM   1301 C  C     . THR A 1 234 ? 102.102 123.200 122.330 1.00 72.21  ? 2025 THR A C     1 
ATOM   1302 O  O     . THR A 1 234 ? 102.795 122.428 121.659 1.00 71.13  ? 2025 THR A O     1 
ATOM   1303 C  CB    . THR A 1 234 ? 103.630 124.463 123.847 1.00 71.16  ? 2025 THR A CB    1 
ATOM   1304 N  N     . SER A 1 235 ? 100.889 122.874 122.767 1.00 70.00  ? 2026 SER A N     1 
ATOM   1305 C  CA    . SER A 1 235 ? 100.267 121.587 122.456 1.00 63.40  ? 2026 SER A CA    1 
ATOM   1306 C  C     . SER A 1 235 ? 99.549  121.625 121.111 1.00 66.52  ? 2026 SER A C     1 
ATOM   1307 O  O     . SER A 1 235 ? 98.380  121.262 120.993 1.00 61.54  ? 2026 SER A O     1 
ATOM   1308 C  CB    . SER A 1 235 ? 99.311  121.193 123.573 1.00 53.28  ? 2026 SER A CB    1 
ATOM   1309 N  N     . GLN A 1 236 ? 100.258 122.075 120.078 1.00 67.86  ? 2027 GLN A N     1 
ATOM   1310 C  CA    . GLN A 1 236 ? 99.712  122.137 118.729 1.00 65.18  ? 2027 GLN A CA    1 
ATOM   1311 C  C     . GLN A 1 236 ? 100.664 121.644 117.651 1.00 66.50  ? 2027 GLN A C     1 
ATOM   1312 O  O     . GLN A 1 236 ? 100.203 121.359 116.539 1.00 68.89  ? 2027 GLN A O     1 
ATOM   1313 C  CB    . GLN A 1 236 ? 99.282  123.572 118.387 1.00 66.66  ? 2027 GLN A CB    1 
ATOM   1314 N  N     . GLY A 1 237 ? 101.962 121.547 117.925 1.00 64.78  ? 2028 GLY A N     1 
ATOM   1315 C  CA    . GLY A 1 237 ? 102.920 121.141 116.916 1.00 66.28  ? 2028 GLY A CA    1 
ATOM   1316 C  C     . GLY A 1 237 ? 103.224 119.657 116.901 1.00 65.45  ? 2028 GLY A C     1 
ATOM   1317 O  O     . GLY A 1 237 ? 104.391 119.270 116.791 1.00 65.49  ? 2028 GLY A O     1 
ATOM   1318 N  N     . ILE A 1 238 ? 102.177 118.830 117.005 1.00 65.93  ? 2029 ILE A N     1 
ATOM   1319 C  CA    . ILE A 1 238 ? 102.245 117.368 116.961 1.00 62.62  ? 2029 ILE A CA    1 
ATOM   1320 C  C     . ILE A 1 238 ? 102.889 116.811 118.226 1.00 62.38  ? 2029 ILE A C     1 
ATOM   1321 O  O     . ILE A 1 238 ? 102.295 115.978 118.919 1.00 59.69  ? 2029 ILE A O     1 
ATOM   1322 C  CB    . ILE A 1 238 ? 102.984 116.865 115.705 1.00 62.14  ? 2029 ILE A CB    1 
ATOM   1323 C  CG1   . ILE A 1 238 ? 102.367 117.466 114.439 1.00 62.12  ? 2029 ILE A CG1   1 
ATOM   1324 C  CG2   . ILE A 1 238 ? 102.956 115.346 115.646 1.00 61.26  ? 2029 ILE A CG2   1 
ATOM   1325 C  CD1   . ILE A 1 238 ? 100.931 117.059 114.204 1.00 57.78  ? 2029 ILE A CD1   1 
ATOM   1326 N  N     . GLN A 1 239 ? 104.106 117.256 118.529 1.00 63.31  ? 2030 GLN A N     1 
ATOM   1327 C  CA    . GLN A 1 239 ? 104.809 116.789 119.715 1.00 63.36  ? 2030 GLN A CA    1 
ATOM   1328 C  C     . GLN A 1 239 ? 104.051 117.184 120.976 1.00 65.82  ? 2030 GLN A C     1 
ATOM   1329 O  O     . GLN A 1 239 ? 103.382 118.220 121.021 1.00 65.88  ? 2030 GLN A O     1 
ATOM   1330 C  CB    . GLN A 1 239 ? 106.225 117.366 119.746 1.00 64.38  ? 2030 GLN A CB    1 
ATOM   1331 C  CG    . GLN A 1 239 ? 107.155 116.707 120.748 1.00 67.00  ? 2030 GLN A CG    1 
ATOM   1332 C  CD    . GLN A 1 239 ? 108.614 116.839 120.360 1.00 73.98  ? 2030 GLN A CD    1 
ATOM   1333 O  OE1   . GLN A 1 239 ? 109.231 117.884 120.568 1.00 73.18  ? 2030 GLN A OE1   1 
ATOM   1334 N  NE2   . GLN A 1 239 ? 109.173 115.778 119.791 1.00 70.97  ? 2030 GLN A NE2   1 
ATOM   1335 N  N     . SER A 1 240 ? 104.149 116.340 122.001 1.00 64.30  ? 2031 SER A N     1 
ATOM   1336 C  CA    . SER A 1 240 ? 103.469 116.611 123.259 1.00 59.31  ? 2031 SER A CA    1 
ATOM   1337 C  C     . SER A 1 240 ? 104.020 117.873 123.906 1.00 59.95  ? 2031 SER A C     1 
ATOM   1338 O  O     . SER A 1 240 ? 105.193 118.222 123.746 1.00 63.67  ? 2031 SER A O     1 
ATOM   1339 C  CB    . SER A 1 240 ? 103.629 115.436 124.221 1.00 57.17  ? 2031 SER A CB    1 
ATOM   1340 O  OG    . SER A 1 240 ? 104.993 115.186 124.497 1.00 55.80  ? 2031 SER A OG    1 
ATOM   1341 N  N     . LEU A 1 241 ? 103.150 118.567 124.643 1.00 57.88  ? 2032 LEU A N     1 
ATOM   1342 C  CA    . LEU A 1 241 ? 103.595 119.733 125.394 1.00 58.30  ? 2032 LEU A CA    1 
ATOM   1343 C  C     . LEU A 1 241 ? 104.614 119.351 126.460 1.00 55.89  ? 2032 LEU A C     1 
ATOM   1344 O  O     . LEU A 1 241 ? 105.479 120.160 126.810 1.00 59.76  ? 2032 LEU A O     1 
ATOM   1345 C  CB    . LEU A 1 241 ? 102.391 120.447 126.011 1.00 56.07  ? 2032 LEU A CB    1 
ATOM   1346 C  CG    . LEU A 1 241 ? 101.524 119.686 127.015 1.00 51.96  ? 2032 LEU A CG    1 
ATOM   1347 C  CD1   . LEU A 1 241 ? 101.990 119.945 128.423 1.00 54.80  ? 2032 LEU A CD1   1 
ATOM   1348 C  CD2   . LEU A 1 241 ? 100.069 120.082 126.873 1.00 49.82  ? 2032 LEU A CD2   1 
ATOM   1349 N  N     . GLY A 1 242 ? 104.539 118.122 126.973 1.00 48.52  ? 2033 GLY A N     1 
ATOM   1350 C  CA    . GLY A 1 242 ? 105.505 117.685 127.965 1.00 49.46  ? 2033 GLY A CA    1 
ATOM   1351 C  C     . GLY A 1 242 ? 106.927 117.644 127.442 1.00 54.26  ? 2033 GLY A C     1 
ATOM   1352 O  O     . GLY A 1 242 ? 107.874 117.881 128.195 1.00 56.03  ? 2033 GLY A O     1 
ATOM   1353 N  N     . LEU A 1 243 ? 107.099 117.343 126.155 1.00 55.86  ? 2034 LEU A N     1 
ATOM   1354 C  CA    . LEU A 1 243 ? 108.432 117.211 125.579 1.00 55.68  ? 2034 LEU A CA    1 
ATOM   1355 C  C     . LEU A 1 243 ? 108.985 118.518 125.025 1.00 61.04  ? 2034 LEU A C     1 
ATOM   1356 O  O     . LEU A 1 243 ? 110.208 118.694 124.994 1.00 64.55  ? 2034 LEU A O     1 
ATOM   1357 C  CB    . LEU A 1 243 ? 108.427 116.149 124.476 1.00 58.39  ? 2034 LEU A CB    1 
ATOM   1358 C  CG    . LEU A 1 243 ? 108.096 114.730 124.943 1.00 54.37  ? 2034 LEU A CG    1 
ATOM   1359 C  CD1   . LEU A 1 243 ? 108.300 113.726 123.822 1.00 46.68  ? 2034 LEU A CD1   1 
ATOM   1360 C  CD2   . LEU A 1 243 ? 108.928 114.360 126.157 1.00 54.41  ? 2034 LEU A CD2   1 
ATOM   1361 N  N     . ASN A 1 244 ? 108.131 119.434 124.577 1.00 64.17  ? 2035 ASN A N     1 
ATOM   1362 C  CA    . ASN A 1 244 ? 108.636 120.714 124.110 1.00 63.92  ? 2035 ASN A CA    1 
ATOM   1363 C  C     . ASN A 1 244 ? 108.904 121.641 125.294 1.00 63.95  ? 2035 ASN A C     1 
ATOM   1364 O  O     . ASN A 1 244 ? 108.428 121.424 126.411 1.00 61.52  ? 2035 ASN A O     1 
ATOM   1365 C  CB    . ASN A 1 244 ? 107.665 121.355 123.113 1.00 64.64  ? 2035 ASN A CB    1 
ATOM   1366 C  CG    . ASN A 1 244 ? 106.266 121.539 123.677 1.00 64.47  ? 2035 ASN A CG    1 
ATOM   1367 O  OD1   . ASN A 1 244 ? 106.086 122.001 124.803 1.00 60.43  ? 2035 ASN A OD1   1 
ATOM   1368 N  ND2   . ASN A 1 244 ? 105.264 121.186 122.881 1.00 65.54  ? 2035 ASN A ND2   1 
ATOM   1369 N  N     . ALA A 1 245 ? 109.686 122.690 125.039 1.00 68.28  ? 2036 ALA A N     1 
ATOM   1370 C  CA    . ALA A 1 245 ? 110.103 123.615 126.086 1.00 71.60  ? 2036 ALA A CA    1 
ATOM   1371 C  C     . ALA A 1 245 ? 109.651 125.047 125.830 1.00 73.09  ? 2036 ALA A C     1 
ATOM   1372 O  O     . ALA A 1 245 ? 110.172 125.971 126.466 1.00 70.79  ? 2036 ALA A O     1 
ATOM   1373 C  CB    . ALA A 1 245 ? 111.624 123.570 126.254 1.00 74.12  ? 2036 ALA A CB    1 
ATOM   1374 N  N     . GLY A 1 246 ? 108.699 125.260 124.922 1.00 73.63  ? 2037 GLY A N     1 
ATOM   1375 C  CA    . GLY A 1 246 ? 108.226 126.592 124.614 1.00 77.39  ? 2037 GLY A CA    1 
ATOM   1376 C  C     . GLY A 1 246 ? 107.036 127.009 125.461 1.00 79.13  ? 2037 GLY A C     1 
ATOM   1377 O  O     . GLY A 1 246 ? 106.551 126.274 126.321 1.00 74.14  ? 2037 GLY A O     1 
ATOM   1378 N  N     . SER A 1 247 ? 106.570 128.233 125.200 1.00 84.49  ? 2038 SER A N     1 
ATOM   1379 C  CA    . SER A 1 247 ? 105.382 128.800 125.842 1.00 88.94  ? 2038 SER A CA    1 
ATOM   1380 C  C     . SER A 1 247 ? 105.523 128.861 127.362 1.00 86.11  ? 2038 SER A C     1 
ATOM   1381 O  O     . SER A 1 247 ? 104.531 128.761 128.089 1.00 85.57  ? 2038 SER A O     1 
ATOM   1382 C  CB    . SER A 1 247 ? 104.120 128.021 125.452 1.00 88.63  ? 2038 SER A CB    1 
ATOM   1383 O  OG    . SER A 1 247 ? 102.944 128.694 125.869 1.00 90.90  ? 2038 SER A OG    1 
ATOM   1384 N  N     . GLU A 1 248 ? 106.753 129.044 127.848 1.00 83.25  ? 2039 GLU A N     1 
ATOM   1385 C  CA    . GLU A 1 248 ? 107.064 129.071 129.285 1.00 82.67  ? 2039 GLU A CA    1 
ATOM   1386 C  C     . GLU A 1 248 ? 106.496 127.789 129.896 1.00 80.69  ? 2039 GLU A C     1 
ATOM   1387 O  O     . GLU A 1 248 ? 106.806 126.701 129.391 1.00 76.85  ? 2039 GLU A O     1 
ATOM   1388 C  CB    . GLU A 1 248 ? 106.558 130.372 129.894 1.00 83.79  ? 2039 GLU A CB    1 
ATOM   1389 C  CG    . GLU A 1 248 ? 107.529 131.016 130.868 1.00 84.00  ? 2039 GLU A CG    1 
ATOM   1390 C  CD    . GLU A 1 248 ? 107.476 130.387 132.247 1.00 82.78  ? 2039 GLU A CD    1 
ATOM   1391 O  OE1   . GLU A 1 248 ? 106.363 130.065 132.713 1.00 80.13  ? 2039 GLU A OE1   1 
ATOM   1392 O  OE2   . GLU A 1 248 ? 108.548 130.214 132.863 1.00 87.08  ? 2039 GLU A OE2   1 
ATOM   1393 N  N     . HIS A 1 249 ? 105.677 127.867 130.948 1.00 79.46  ? 2040 HIS A N     1 
ATOM   1394 C  CA    . HIS A 1 249 ? 104.967 126.711 131.494 1.00 76.31  ? 2040 HIS A CA    1 
ATOM   1395 C  C     . HIS A 1 249 ? 105.951 125.611 131.902 1.00 70.46  ? 2040 HIS A C     1 
ATOM   1396 O  O     . HIS A 1 249 ? 106.054 124.560 131.271 1.00 69.09  ? 2040 HIS A O     1 
ATOM   1397 C  CB    . HIS A 1 249 ? 103.924 126.193 130.497 1.00 77.06  ? 2040 HIS A CB    1 
ATOM   1398 C  CG    . HIS A 1 249 ? 102.710 127.061 130.391 1.00 77.98  ? 2040 HIS A CG    1 
ATOM   1399 N  ND1   . HIS A 1 249 ? 101.948 127.140 129.246 1.00 80.08  ? 2040 HIS A ND1   1 
ATOM   1400 C  CD2   . HIS A 1 249 ? 102.125 127.888 131.290 1.00 76.48  ? 2040 HIS A CD2   1 
ATOM   1401 C  CE1   . HIS A 1 249 ? 100.945 127.977 129.443 1.00 79.63  ? 2040 HIS A CE1   1 
ATOM   1402 N  NE2   . HIS A 1 249 ? 101.030 128.445 130.675 1.00 79.21  ? 2040 HIS A NE2   1 
ATOM   1403 N  N     . SER A 1 250 ? 106.702 125.912 132.965 1.00 71.03  ? 2041 SER A N     1 
ATOM   1404 C  CA    . SER A 1 250 ? 107.763 125.050 133.478 1.00 69.44  ? 2041 SER A CA    1 
ATOM   1405 C  C     . SER A 1 250 ? 107.362 123.580 133.494 1.00 68.49  ? 2041 SER A C     1 
ATOM   1406 O  O     . SER A 1 250 ? 106.194 123.248 133.722 1.00 67.60  ? 2041 SER A O     1 
ATOM   1407 C  CB    . SER A 1 250 ? 108.169 125.492 134.886 1.00 72.44  ? 2041 SER A CB    1 
ATOM   1408 O  OG    . SER A 1 250 ? 109.208 124.674 135.396 1.00 71.79  ? 2041 SER A OG    1 
ATOM   1409 N  N     . GLY A 1 251 ? 108.339 122.698 133.256 1.00 68.77  ? 2042 GLY A N     1 
ATOM   1410 C  CA    . GLY A 1 251 ? 108.041 121.309 132.944 1.00 62.59  ? 2042 GLY A CA    1 
ATOM   1411 C  C     . GLY A 1 251 ? 107.213 120.591 133.992 1.00 58.28  ? 2042 GLY A C     1 
ATOM   1412 O  O     . GLY A 1 251 ? 106.514 119.628 133.674 1.00 59.46  ? 2042 GLY A O     1 
ATOM   1413 N  N     . ARG A 1 252 ? 107.276 121.042 135.245 1.00 59.62  ? 2043 ARG A N     1 
ATOM   1414 C  CA    . ARG A 1 252 ? 106.430 120.470 136.287 1.00 59.10  ? 2043 ARG A CA    1 
ATOM   1415 C  C     . ARG A 1 252 ? 104.958 120.540 135.895 1.00 53.57  ? 2043 ARG A C     1 
ATOM   1416 O  O     . ARG A 1 252 ? 104.290 119.512 135.720 1.00 51.84  ? 2043 ARG A O     1 
ATOM   1417 C  CB    . ARG A 1 252 ? 106.662 121.208 137.606 1.00 62.88  ? 2043 ARG A CB    1 
ATOM   1418 C  CG    . ARG A 1 252 ? 107.533 120.474 138.606 1.00 63.10  ? 2043 ARG A CG    1 
ATOM   1419 C  CD    . ARG A 1 252 ? 107.624 121.238 139.919 1.00 67.88  ? 2043 ARG A CD    1 
ATOM   1420 N  NE    . ARG A 1 252 ? 106.460 122.086 140.149 1.00 74.06  ? 2043 ARG A NE    1 
ATOM   1421 C  CZ    . ARG A 1 252 ? 105.306 121.660 140.645 1.00 69.05  ? 2043 ARG A CZ    1 
ATOM   1422 N  NH1   . ARG A 1 252 ? 105.122 120.393 140.975 1.00 62.84  ? 2043 ARG A NH1   1 
ATOM   1423 N  NH2   . ARG A 1 252 ? 104.311 122.526 140.812 1.00 69.33  ? 2043 ARG A NH2   1 
ATOM   1424 N  N     . TYR A 1 253 ? 104.446 121.763 135.743 1.00 54.94  ? 2044 TYR A N     1 
ATOM   1425 C  CA    . TYR A 1 253 ? 103.037 121.953 135.421 1.00 55.31  ? 2044 TYR A CA    1 
ATOM   1426 C  C     . TYR A 1 253 ? 102.690 121.341 134.073 1.00 55.05  ? 2044 TYR A C     1 
ATOM   1427 O  O     . TYR A 1 253 ? 101.629 120.726 133.918 1.00 56.42  ? 2044 TYR A O     1 
ATOM   1428 C  CB    . TYR A 1 253 ? 102.698 123.443 135.439 1.00 54.83  ? 2044 TYR A CB    1 
ATOM   1429 C  CG    . TYR A 1 253 ? 101.279 123.759 135.027 1.00 57.42  ? 2044 TYR A CG    1 
ATOM   1430 C  CD1   . TYR A 1 253 ? 100.216 123.511 135.882 1.00 59.21  ? 2044 TYR A CD1   1 
ATOM   1431 C  CD2   . TYR A 1 253 ? 101.004 124.312 133.784 1.00 60.81  ? 2044 TYR A CD2   1 
ATOM   1432 C  CE1   . TYR A 1 253 ? 98.918  123.800 135.510 1.00 63.78  ? 2044 TYR A CE1   1 
ATOM   1433 C  CE2   . TYR A 1 253 ? 99.710  124.605 133.403 1.00 63.51  ? 2044 TYR A CE2   1 
ATOM   1434 C  CZ    . TYR A 1 253 ? 98.671  124.347 134.270 1.00 64.76  ? 2044 TYR A CZ    1 
ATOM   1435 O  OH    . TYR A 1 253 ? 97.380  124.638 133.897 1.00 66.29  ? 2044 TYR A OH    1 
ATOM   1436 N  N     . ARG A 1 254 ? 103.573 121.499 133.084 1.00 54.82  ? 2045 ARG A N     1 
ATOM   1437 C  CA    . ARG A 1 254 ? 103.293 120.969 131.754 1.00 51.94  ? 2045 ARG A CA    1 
ATOM   1438 C  C     . ARG A 1 254 ? 103.130 119.455 131.788 1.00 51.56  ? 2045 ARG A C     1 
ATOM   1439 O  O     . ARG A 1 254 ? 102.123 118.920 131.316 1.00 52.70  ? 2045 ARG A O     1 
ATOM   1440 C  CB    . ARG A 1 254 ? 104.404 121.372 130.783 1.00 54.08  ? 2045 ARG A CB    1 
ATOM   1441 C  CG    . ARG A 1 254 ? 104.030 122.527 129.869 1.00 57.90  ? 2045 ARG A CG    1 
ATOM   1442 C  CD    . ARG A 1 254 ? 104.917 122.583 128.638 1.00 57.10  ? 2045 ARG A CD    1 
ATOM   1443 N  NE    . ARG A 1 254 ? 106.252 123.087 128.936 1.00 60.87  ? 2045 ARG A NE    1 
ATOM   1444 C  CZ    . ARG A 1 254 ? 107.313 122.324 129.156 1.00 59.83  ? 2045 ARG A CZ    1 
ATOM   1445 N  NH1   . ARG A 1 254 ? 107.240 121.005 129.108 1.00 58.08  ? 2045 ARG A NH1   1 
ATOM   1446 N  NH2   . ARG A 1 254 ? 108.479 122.901 129.433 1.00 65.78  ? 2045 ARG A NH2   1 
ATOM   1447 N  N     . ALA A 1 255 ? 104.104 118.747 132.364 1.00 51.52  ? 2046 ALA A N     1 
ATOM   1448 C  CA    . ALA A 1 255 ? 104.021 117.293 132.422 1.00 44.83  ? 2046 ALA A CA    1 
ATOM   1449 C  C     . ALA A 1 255 ? 102.834 116.836 133.256 1.00 46.47  ? 2046 ALA A C     1 
ATOM   1450 O  O     . ALA A 1 255 ? 102.155 115.865 132.899 1.00 47.77  ? 2046 ALA A O     1 
ATOM   1451 C  CB    . ALA A 1 255 ? 105.317 116.712 132.979 1.00 44.75  ? 2046 ALA A CB    1 
ATOM   1452 N  N     . SER A 1 256 ? 102.568 117.514 134.375 1.00 47.63  ? 2047 SER A N     1 
ATOM   1453 C  CA    . SER A 1 256 ? 101.464 117.099 135.234 1.00 45.27  ? 2047 SER A CA    1 
ATOM   1454 C  C     . SER A 1 256 ? 100.123 117.245 134.523 1.00 47.59  ? 2047 SER A C     1 
ATOM   1455 O  O     . SER A 1 256 ? 99.303  116.316 134.520 1.00 47.92  ? 2047 SER A O     1 
ATOM   1456 C  CB    . SER A 1 256 ? 101.486 117.909 136.526 1.00 50.29  ? 2047 SER A CB    1 
ATOM   1457 O  OG    . SER A 1 256 ? 102.708 117.722 137.217 1.00 53.06  ? 2047 SER A OG    1 
ATOM   1458 N  N     . VAL A 1 257 ? 99.884  118.405 133.905 1.00 48.25  ? 2048 VAL A N     1 
ATOM   1459 C  CA    . VAL A 1 257 ? 98.627  118.596 133.193 1.00 48.85  ? 2048 VAL A CA    1 
ATOM   1460 C  C     . VAL A 1 257 ? 98.554  117.669 131.989 1.00 50.58  ? 2048 VAL A C     1 
ATOM   1461 O  O     . VAL A 1 257 ? 97.472  117.190 131.638 1.00 52.38  ? 2048 VAL A O     1 
ATOM   1462 C  CB    . VAL A 1 257 ? 98.436  120.075 132.801 1.00 48.90  ? 2048 VAL A CB    1 
ATOM   1463 C  CG1   . VAL A 1 257 ? 99.371  120.476 131.674 1.00 52.65  ? 2048 VAL A CG1   1 
ATOM   1464 C  CG2   . VAL A 1 257 ? 96.991  120.335 132.412 1.00 54.62  ? 2048 VAL A CG2   1 
ATOM   1465 N  N     . GLU A 1 258 ? 99.692  117.375 131.354 1.00 49.68  ? 2049 GLU A N     1 
ATOM   1466 C  CA    . GLU A 1 258 ? 99.701  116.436 130.239 1.00 46.12  ? 2049 GLU A CA    1 
ATOM   1467 C  C     . GLU A 1 258 ? 99.270  115.046 130.686 1.00 45.08  ? 2049 GLU A C     1 
ATOM   1468 O  O     . GLU A 1 258 ? 98.487  114.382 129.999 1.00 45.43  ? 2049 GLU A O     1 
ATOM   1469 C  CB    . GLU A 1 258 ? 101.094 116.403 129.608 1.00 47.59  ? 2049 GLU A CB    1 
ATOM   1470 C  CG    . GLU A 1 258 ? 101.586 115.029 129.183 1.00 45.06  ? 2049 GLU A CG    1 
ATOM   1471 C  CD    . GLU A 1 258 ? 101.051 114.597 127.836 1.00 48.23  ? 2049 GLU A CD    1 
ATOM   1472 O  OE1   . GLU A 1 258 ? 100.005 115.123 127.412 1.00 52.05  ? 2049 GLU A OE1   1 
ATOM   1473 O  OE2   . GLU A 1 258 ? 101.682 113.730 127.198 1.00 48.45  ? 2049 GLU A OE2   1 
ATOM   1474 N  N     . SER A 1 259 ? 99.769  114.592 131.838 1.00 45.65  ? 2050 SER A N     1 
ATOM   1475 C  CA    . SER A 1 259 ? 99.354  113.297 132.367 1.00 40.91  ? 2050 SER A CA    1 
ATOM   1476 C  C     . SER A 1 259 ? 97.873  113.295 132.712 1.00 44.00  ? 2050 SER A C     1 
ATOM   1477 O  O     . SER A 1 259 ? 97.159  112.325 132.422 1.00 44.05  ? 2050 SER A O     1 
ATOM   1478 C  CB    . SER A 1 259 ? 100.187 112.941 133.594 1.00 39.36  ? 2050 SER A CB    1 
ATOM   1479 O  OG    . SER A 1 259 ? 101.565 113.025 133.297 1.00 41.86  ? 2050 SER A OG    1 
ATOM   1480 N  N     . ILE A 1 260 ? 97.394  114.378 133.333 1.00 49.15  ? 2051 ILE A N     1 
ATOM   1481 C  CA    . ILE A 1 260 ? 95.973  114.481 133.656 1.00 49.00  ? 2051 ILE A CA    1 
ATOM   1482 C  C     . ILE A 1 260 ? 95.134  114.368 132.391 1.00 50.77  ? 2051 ILE A C     1 
ATOM   1483 O  O     . ILE A 1 260 ? 94.120  113.660 132.361 1.00 50.40  ? 2051 ILE A O     1 
ATOM   1484 C  CB    . ILE A 1 260 ? 95.681  115.795 134.403 1.00 48.23  ? 2051 ILE A CB    1 
ATOM   1485 C  CG1   . ILE A 1 260 ? 96.423  115.839 135.737 1.00 49.37  ? 2051 ILE A CG1   1 
ATOM   1486 C  CG2   . ILE A 1 260 ? 94.188  115.960 134.624 1.00 54.07  ? 2051 ILE A CG2   1 
ATOM   1487 C  CD1   . ILE A 1 260 ? 96.377  117.197 136.398 1.00 54.31  ? 2051 ILE A CD1   1 
ATOM   1488 N  N     . LEU A 1 261 ? 95.544  115.063 131.329 1.00 50.26  ? 2052 LEU A N     1 
ATOM   1489 C  CA    . LEU A 1 261 ? 94.818  114.987 130.067 1.00 48.99  ? 2052 LEU A CA    1 
ATOM   1490 C  C     . LEU A 1 261 ? 94.841  113.572 129.505 1.00 47.58  ? 2052 LEU A C     1 
ATOM   1491 O  O     . LEU A 1 261 ? 93.790  113.010 129.168 1.00 50.39  ? 2052 LEU A O     1 
ATOM   1492 C  CB    . LEU A 1 261 ? 95.415  115.965 129.052 1.00 49.53  ? 2052 LEU A CB    1 
ATOM   1493 C  CG    . LEU A 1 261 ? 95.467  117.464 129.351 1.00 52.37  ? 2052 LEU A CG    1 
ATOM   1494 C  CD1   . LEU A 1 261 ? 96.705  118.070 128.713 1.00 55.10  ? 2052 LEU A CD1   1 
ATOM   1495 C  CD2   . LEU A 1 261 ? 94.230  118.169 128.850 1.00 56.34  ? 2052 LEU A CD2   1 
ATOM   1496 N  N     . ILE A 1 262 ? 96.034  112.976 129.405 1.00 46.44  ? 2053 ILE A N     1 
ATOM   1497 C  CA    . ILE A 1 262 ? 96.173  111.744 128.636 1.00 43.91  ? 2053 ILE A CA    1 
ATOM   1498 C  C     . ILE A 1 262 ? 95.548  110.560 129.356 1.00 45.35  ? 2053 ILE A C     1 
ATOM   1499 O  O     . ILE A 1 262 ? 95.009  109.668 128.701 1.00 46.51  ? 2053 ILE A O     1 
ATOM   1500 C  CB    . ILE A 1 262 ? 97.642  111.459 128.263 1.00 38.21  ? 2053 ILE A CB    1 
ATOM   1501 C  CG1   . ILE A 1 262 ? 98.515  111.280 129.502 1.00 39.05  ? 2053 ILE A CG1   1 
ATOM   1502 C  CG2   . ILE A 1 262 ? 98.181  112.546 127.353 1.00 40.20  ? 2053 ILE A CG2   1 
ATOM   1503 C  CD1   . ILE A 1 262 ? 99.923  110.829 129.185 1.00 32.94  ? 2053 ILE A CD1   1 
ATOM   1504 N  N     . PHE A 1 263 ? 95.583  110.515 130.691 1.00 43.95  ? 2054 PHE A N     1 
ATOM   1505 C  CA    . PHE A 1 263 ? 94.964  109.380 131.375 1.00 42.33  ? 2054 PHE A CA    1 
ATOM   1506 C  C     . PHE A 1 263 ? 93.466  109.321 131.101 1.00 46.20  ? 2054 PHE A C     1 
ATOM   1507 O  O     . PHE A 1 263 ? 92.929  108.272 130.726 1.00 48.39  ? 2054 PHE A O     1 
ATOM   1508 C  CB    . PHE A 1 263 ? 95.217  109.443 132.879 1.00 44.45  ? 2054 PHE A CB    1 
ATOM   1509 C  CG    . PHE A 1 263 ? 94.754  108.214 133.614 1.00 46.29  ? 2054 PHE A CG    1 
ATOM   1510 C  CD1   . PHE A 1 263 ? 95.540  107.076 133.652 1.00 43.52  ? 2054 PHE A CD1   1 
ATOM   1511 C  CD2   . PHE A 1 263 ? 93.524  108.189 134.246 1.00 49.07  ? 2054 PHE A CD2   1 
ATOM   1512 C  CE1   . PHE A 1 263 ? 95.119  105.947 134.319 1.00 44.44  ? 2054 PHE A CE1   1 
ATOM   1513 C  CE2   . PHE A 1 263 ? 93.096  107.057 134.910 1.00 50.10  ? 2054 PHE A CE2   1 
ATOM   1514 C  CZ    . PHE A 1 263 ? 93.895  105.937 134.948 1.00 48.02  ? 2054 PHE A CZ    1 
ATOM   1515 N  N     . ASN A 1 264 ? 92.772  110.445 131.278 1.00 46.61  ? 2055 ASN A N     1 
ATOM   1516 C  CA    . ASN A 1 264 ? 91.329  110.448 131.073 1.00 47.84  ? 2055 ASN A CA    1 
ATOM   1517 C  C     . ASN A 1 264 ? 90.977  110.308 129.597 1.00 47.47  ? 2055 ASN A C     1 
ATOM   1518 O  O     . ASN A 1 264 ? 90.019  109.603 129.247 1.00 51.64  ? 2055 ASN A O     1 
ATOM   1519 C  CB    . ASN A 1 264 ? 90.720  111.715 131.667 1.00 49.65  ? 2055 ASN A CB    1 
ATOM   1520 C  CG    . ASN A 1 264 ? 90.826  111.757 133.179 1.00 53.35  ? 2055 ASN A CG    1 
ATOM   1521 O  OD1   . ASN A 1 264 ? 89.874  111.432 133.888 1.00 52.37  ? 2055 ASN A OD1   1 
ATOM   1522 N  ND2   . ASN A 1 264 ? 91.989  112.155 133.680 1.00 52.30  ? 2055 ASN A ND2   1 
ATOM   1523 N  N     . SER A 1 265 ? 91.742  110.954 128.709 1.00 44.80  ? 2056 SER A N     1 
ATOM   1524 C  CA    . SER A 1 265 ? 91.469  110.786 127.288 1.00 45.86  ? 2056 SER A CA    1 
ATOM   1525 C  C     . SER A 1 265 ? 91.721  109.353 126.848 1.00 45.08  ? 2056 SER A C     1 
ATOM   1526 O  O     . SER A 1 265 ? 91.033  108.854 125.957 1.00 42.51  ? 2056 SER A O     1 
ATOM   1527 C  CB    . SER A 1 265 ? 92.309  111.752 126.455 1.00 47.11  ? 2056 SER A CB    1 
ATOM   1528 O  OG    . SER A 1 265 ? 93.681  111.651 126.779 1.00 45.79  ? 2056 SER A OG    1 
ATOM   1529 N  N     . MET A 1 266 ? 92.674  108.664 127.478 1.00 45.58  ? 2057 MET A N     1 
ATOM   1530 C  CA    . MET A 1 266 ? 92.950  107.280 127.126 1.00 40.82  ? 2057 MET A CA    1 
ATOM   1531 C  C     . MET A 1 266 ? 91.905  106.342 127.707 1.00 42.84  ? 2057 MET A C     1 
ATOM   1532 O  O     . MET A 1 266 ? 91.617  105.305 127.109 1.00 50.18  ? 2057 MET A O     1 
ATOM   1533 C  CB    . MET A 1 266 ? 94.342  106.884 127.612 1.00 36.19  ? 2057 MET A CB    1 
ATOM   1534 C  CG    . MET A 1 266 ? 94.866  105.596 127.008 1.00 37.59  ? 2057 MET A CG    1 
ATOM   1535 S  SD    . MET A 1 266 ? 94.608  105.573 125.225 1.00 36.62  ? 2057 MET A SD    1 
ATOM   1536 C  CE    . MET A 1 266 ? 94.527  103.820 124.902 1.00 27.65  ? 2057 MET A CE    1 
ATOM   1537 N  N     . ASN A 1 267 ? 91.330  106.679 128.863 1.00 41.65  ? 2058 ASN A N     1 
ATOM   1538 C  CA    . ASN A 1 267 ? 90.168  105.933 129.341 1.00 42.76  ? 2058 ASN A CA    1 
ATOM   1539 C  C     . ASN A 1 267 ? 88.997  106.073 128.374 1.00 43.98  ? 2058 ASN A C     1 
ATOM   1540 O  O     . ASN A 1 267 ? 88.314  105.088 128.058 1.00 47.51  ? 2058 ASN A O     1 
ATOM   1541 C  CB    . ASN A 1 267 ? 89.769  106.411 130.736 1.00 45.61  ? 2058 ASN A CB    1 
ATOM   1542 C  CG    . ASN A 1 267 ? 90.565  105.738 131.831 1.00 48.00  ? 2058 ASN A CG    1 
ATOM   1543 O  OD1   . ASN A 1 267 ? 91.126  104.661 131.634 1.00 51.55  ? 2058 ASN A OD1   1 
ATOM   1544 N  ND2   . ASN A 1 267 ? 90.617  106.369 132.997 1.00 44.54  ? 2058 ASN A ND2   1 
ATOM   1545 N  N     . GLN A 1 268 ? 88.757  107.292 127.886 1.00 41.12  ? 2059 GLN A N     1 
ATOM   1546 C  CA    . GLN A 1 268 ? 87.719  107.490 126.878 1.00 41.17  ? 2059 GLN A CA    1 
ATOM   1547 C  C     . GLN A 1 268 ? 88.048  106.735 125.595 1.00 43.48  ? 2059 GLN A C     1 
ATOM   1548 O  O     . GLN A 1 268 ? 87.160  106.165 124.949 1.00 47.57  ? 2059 GLN A O     1 
ATOM   1549 C  CB    . GLN A 1 268 ? 87.541  108.981 126.598 1.00 46.57  ? 2059 GLN A CB    1 
ATOM   1550 C  CG    . GLN A 1 268 ? 86.094  109.432 126.544 1.00 50.48  ? 2059 GLN A CG    1 
ATOM   1551 C  CD    . GLN A 1 268 ? 85.466  109.197 125.188 1.00 53.25  ? 2059 GLN A CD    1 
ATOM   1552 O  OE1   . GLN A 1 268 ? 86.158  108.906 124.213 1.00 52.88  ? 2059 GLN A OE1   1 
ATOM   1553 N  NE2   . GLN A 1 268 ? 84.146  109.322 125.117 1.00 51.66  ? 2059 GLN A NE2   1 
ATOM   1554 N  N     . LEU A 1 269 ? 89.324  106.722 125.210 1.00 42.36  ? 2060 LEU A N     1 
ATOM   1555 C  CA    . LEU A 1 269 ? 89.742  105.983 124.025 1.00 40.58  ? 2060 LEU A CA    1 
ATOM   1556 C  C     . LEU A 1 269 ? 89.533  104.487 124.208 1.00 39.72  ? 2060 LEU A C     1 
ATOM   1557 O  O     . LEU A 1 269 ? 89.139  103.793 123.269 1.00 38.75  ? 2060 LEU A O     1 
ATOM   1558 C  CB    . LEU A 1 269 ? 91.204  106.293 123.709 1.00 33.57  ? 2060 LEU A CB    1 
ATOM   1559 C  CG    . LEU A 1 269 ? 91.439  107.620 122.987 1.00 34.49  ? 2060 LEU A CG    1 
ATOM   1560 C  CD1   . LEU A 1 269 ? 92.918  107.956 122.933 1.00 32.42  ? 2060 LEU A CD1   1 
ATOM   1561 C  CD2   . LEU A 1 269 ? 90.845  107.575 121.592 1.00 38.39  ? 2060 LEU A CD2   1 
ATOM   1562 N  N     . ASN A 1 270 ? 89.806  103.969 125.407 1.00 37.33  ? 2061 ASN A N     1 
ATOM   1563 C  CA    . ASN A 1 270 ? 89.555  102.560 125.690 1.00 36.03  ? 2061 ASN A CA    1 
ATOM   1564 C  C     . ASN A 1 270 ? 88.073  102.235 125.610 1.00 38.85  ? 2061 ASN A C     1 
ATOM   1565 O  O     . ASN A 1 270 ? 87.690  101.183 125.086 1.00 43.47  ? 2061 ASN A O     1 
ATOM   1566 C  CB    . ASN A 1 270 ? 90.105  102.193 127.066 1.00 38.68  ? 2061 ASN A CB    1 
ATOM   1567 C  CG    . ASN A 1 270 ? 91.585  101.907 127.041 1.00 38.91  ? 2061 ASN A CG    1 
ATOM   1568 O  OD1   . ASN A 1 270 ? 92.248  102.115 126.031 1.00 34.59  ? 2061 ASN A OD1   1 
ATOM   1569 N  ND2   . ASN A 1 270 ? 92.114  101.428 128.158 1.00 43.63  ? 2061 ASN A ND2   1 
ATOM   1570 N  N     . SER A 1 271 ? 87.220  103.115 126.139 1.00 37.39  ? 2062 SER A N     1 
ATOM   1571 C  CA    . SER A 1 271 ? 85.784  102.872 126.029 1.00 37.75  ? 2062 SER A CA    1 
ATOM   1572 C  C     . SER A 1 271 ? 85.345  102.876 124.568 1.00 41.63  ? 2062 SER A C     1 
ATOM   1573 O  O     . SER A 1 271 ? 84.539  102.035 124.150 1.00 43.16  ? 2062 SER A O     1 
ATOM   1574 C  CB    . SER A 1 271 ? 85.000  103.906 126.839 1.00 40.10  ? 2062 SER A CB    1 
ATOM   1575 O  OG    . SER A 1 271 ? 85.005  105.176 126.216 1.00 42.17  ? 2062 SER A OG    1 
ATOM   1576 N  N     . LEU A 1 272 ? 85.883  103.802 123.771 1.00 41.77  ? 2063 LEU A N     1 
ATOM   1577 C  CA    . LEU A 1 272 ? 85.554  103.832 122.348 1.00 40.49  ? 2063 LEU A CA    1 
ATOM   1578 C  C     . LEU A 1 272 ? 86.066  102.589 121.626 1.00 42.92  ? 2063 LEU A C     1 
ATOM   1579 O  O     . LEU A 1 272 ? 85.391  102.057 120.737 1.00 43.70  ? 2063 LEU A O     1 
ATOM   1580 C  CB    . LEU A 1 272 ? 86.117  105.098 121.707 1.00 35.93  ? 2063 LEU A CB    1 
ATOM   1581 C  CG    . LEU A 1 272 ? 85.260  106.346 121.915 1.00 42.87  ? 2063 LEU A CG    1 
ATOM   1582 C  CD1   . LEU A 1 272 ? 85.881  107.538 121.220 1.00 46.87  ? 2063 LEU A CD1   1 
ATOM   1583 C  CD2   . LEU A 1 272 ? 83.845  106.109 121.413 1.00 47.68  ? 2063 LEU A CD2   1 
ATOM   1584 N  N     . LEU A 1 273 ? 87.265  102.123 121.983 1.00 42.53  ? 2064 LEU A N     1 
ATOM   1585 C  CA    . LEU A 1 273 ? 87.807  100.909 121.383 1.00 38.12  ? 2064 LEU A CA    1 
ATOM   1586 C  C     . LEU A 1 273 ? 86.951  99.699  121.730 1.00 39.58  ? 2064 LEU A C     1 
ATOM   1587 O  O     . LEU A 1 273 ? 86.712  98.835  120.881 1.00 40.37  ? 2064 LEU A O     1 
ATOM   1588 C  CB    . LEU A 1 273 ? 89.252  100.693 121.838 1.00 35.38  ? 2064 LEU A CB    1 
ATOM   1589 C  CG    . LEU A 1 273 ? 90.326  101.657 121.324 1.00 30.23  ? 2064 LEU A CG    1 
ATOM   1590 C  CD1   . LEU A 1 273 ? 91.686  101.305 121.900 1.00 27.04  ? 2064 LEU A CD1   1 
ATOM   1591 C  CD2   . LEU A 1 273 ? 90.377  101.670 119.812 1.00 33.85  ? 2064 LEU A CD2   1 
ATOM   1592 N  N     . GLN A 1 274 ? 86.484  99.618  122.978 1.00 41.00  ? 2065 GLN A N     1 
ATOM   1593 C  CA    . GLN A 1 274 ? 85.547  98.564  123.349 1.00 43.49  ? 2065 GLN A CA    1 
ATOM   1594 C  C     . GLN A 1 274 ? 84.266  98.661  122.534 1.00 47.63  ? 2065 GLN A C     1 
ATOM   1595 O  O     . GLN A 1 274 ? 83.716  97.642  122.101 1.00 46.56  ? 2065 GLN A O     1 
ATOM   1596 C  CB    . GLN A 1 274 ? 85.231  98.638  124.843 1.00 45.88  ? 2065 GLN A CB    1 
ATOM   1597 C  CG    . GLN A 1 274 ? 86.049  97.700  125.704 1.00 49.26  ? 2065 GLN A CG    1 
ATOM   1598 C  CD    . GLN A 1 274 ? 85.246  96.511  126.191 1.00 52.80  ? 2065 GLN A CD    1 
ATOM   1599 O  OE1   . GLN A 1 274 ? 84.359  96.650  127.033 1.00 55.41  ? 2065 GLN A OE1   1 
ATOM   1600 N  NE2   . GLN A 1 274 ? 85.552  95.332  125.662 1.00 54.93  ? 2065 GLN A NE2   1 
ATOM   1601 N  N     . LYS A 1 275 ? 83.773  99.883  122.322 1.00 47.91  ? 2066 LYS A N     1 
ATOM   1602 C  CA    . LYS A 1 275 ? 82.566  100.064 121.522 1.00 46.96  ? 2066 LYS A CA    1 
ATOM   1603 C  C     . LYS A 1 275 ? 82.777  99.588  120.089 1.00 47.11  ? 2066 LYS A C     1 
ATOM   1604 O  O     . LYS A 1 275 ? 81.886  98.970  119.494 1.00 46.65  ? 2066 LYS A O     1 
ATOM   1605 C  CB    . LYS A 1 275 ? 82.139  101.532 121.551 1.00 46.56  ? 2066 LYS A CB    1 
ATOM   1606 C  CG    . LYS A 1 275 ? 81.604  102.064 120.232 1.00 52.19  ? 2066 LYS A CG    1 
ATOM   1607 C  CD    . LYS A 1 275 ? 81.015  103.453 120.401 1.00 54.11  ? 2066 LYS A CD    1 
ATOM   1608 C  CE    . LYS A 1 275 ? 79.546  103.386 120.781 1.00 53.81  ? 2066 LYS A CE    1 
ATOM   1609 N  NZ    . LYS A 1 275 ? 79.062  104.676 121.347 1.00 51.96  ? 2066 LYS A NZ    1 
ATOM   1610 N  N     . GLU A 1 276 ? 83.951  99.855  119.524 1.00 47.22  ? 2067 GLU A N     1 
ATOM   1611 C  CA    . GLU A 1 276 ? 84.257  99.494  118.146 1.00 45.31  ? 2067 GLU A CA    1 
ATOM   1612 C  C     . GLU A 1 276 ? 84.912  98.125  118.014 1.00 46.85  ? 2067 GLU A C     1 
ATOM   1613 O  O     . GLU A 1 276 ? 85.235  97.720  116.893 1.00 47.77  ? 2067 GLU A O     1 
ATOM   1614 C  CB    . GLU A 1 276 ? 85.162  100.556 117.515 1.00 44.51  ? 2067 GLU A CB    1 
ATOM   1615 C  CG    . GLU A 1 276 ? 84.481  101.897 117.301 1.00 51.37  ? 2067 GLU A CG    1 
ATOM   1616 C  CD    . GLU A 1 276 ? 83.694  101.951 116.008 1.00 56.25  ? 2067 GLU A CD    1 
ATOM   1617 O  OE1   . GLU A 1 276 ? 84.305  101.780 114.933 1.00 55.04  ? 2067 GLU A OE1   1 
ATOM   1618 O  OE2   . GLU A 1 276 ? 82.466  102.166 116.067 1.00 59.90  ? 2067 GLU A OE2   1 
ATOM   1619 N  N     . ASN A 1 277 ? 85.106  97.406  119.123 1.00 47.55  ? 2068 ASN A N     1 
ATOM   1620 C  CA    . ASN A 1 277 ? 85.779  96.105  119.128 1.00 45.78  ? 2068 ASN A CA    1 
ATOM   1621 C  C     . ASN A 1 277 ? 87.178  96.204  118.519 1.00 43.58  ? 2068 ASN A C     1 
ATOM   1622 O  O     . ASN A 1 277 ? 87.570  95.409  117.664 1.00 41.13  ? 2068 ASN A O     1 
ATOM   1623 C  CB    . ASN A 1 277 ? 84.938  95.047  118.409 1.00 47.28  ? 2068 ASN A CB    1 
ATOM   1624 C  CG    . ASN A 1 277 ? 85.239  93.641  118.887 1.00 52.99  ? 2068 ASN A CG    1 
ATOM   1625 O  OD1   . ASN A 1 277 ? 86.317  93.371  119.417 1.00 50.99  ? 2068 ASN A OD1   1 
ATOM   1626 N  ND2   . ASN A 1 277 ? 84.285  92.737  118.703 1.00 55.10  ? 2068 ASN A ND2   1 
ATOM   1627 N  N     . LEU A 1 278 ? 87.938  97.199  118.978 1.00 42.09  ? 2069 LEU A N     1 
ATOM   1628 C  CA    . LEU A 1 278 ? 89.275  97.466  118.463 1.00 37.16  ? 2069 LEU A CA    1 
ATOM   1629 C  C     . LEU A 1 278 ? 90.350  97.383  119.538 1.00 36.61  ? 2069 LEU A C     1 
ATOM   1630 O  O     . LEU A 1 278 ? 91.510  97.702  119.259 1.00 36.24  ? 2069 LEU A O     1 
ATOM   1631 C  CB    . LEU A 1 278 ? 89.323  98.848  117.803 1.00 35.18  ? 2069 LEU A CB    1 
ATOM   1632 C  CG    . LEU A 1 278 ? 89.357  98.906  116.278 1.00 36.68  ? 2069 LEU A CG    1 
ATOM   1633 C  CD1   . LEU A 1 278 ? 88.181  98.139  115.713 1.00 41.73  ? 2069 LEU A CD1   1 
ATOM   1634 C  CD2   . LEU A 1 278 ? 89.342  100.344 115.795 1.00 33.77  ? 2069 LEU A CD2   1 
ATOM   1635 N  N     . GLN A 1 279 ? 90.001  96.985  120.762 1.00 38.75  ? 2070 GLN A N     1 
ATOM   1636 C  CA    . GLN A 1 279 ? 90.997  96.963  121.828 1.00 38.96  ? 2070 GLN A CA    1 
ATOM   1637 C  C     . GLN A 1 279 ? 91.928  95.764  121.710 1.00 39.28  ? 2070 GLN A C     1 
ATOM   1638 O  O     . GLN A 1 279 ? 93.108  95.859  122.064 1.00 40.22  ? 2070 GLN A O     1 
ATOM   1639 C  CB    . GLN A 1 279 ? 90.317  96.969  123.195 1.00 42.27  ? 2070 GLN A CB    1 
ATOM   1640 C  CG    . GLN A 1 279 ? 91.013  97.864  124.206 1.00 41.86  ? 2070 GLN A CG    1 
ATOM   1641 C  CD    . GLN A 1 279 ? 90.291  97.910  125.532 1.00 45.64  ? 2070 GLN A CD    1 
ATOM   1642 O  OE1   . GLN A 1 279 ? 89.136  97.509  125.634 1.00 45.74  ? 2070 GLN A OE1   1 
ATOM   1643 N  NE2   . GLN A 1 279 ? 90.967  98.412  126.556 1.00 44.87  ? 2070 GLN A NE2   1 
ATOM   1644 N  N     . ASP A 1 280 ? 91.417  94.626  121.234 1.00 38.31  ? 2071 ASP A N     1 
ATOM   1645 C  CA    . ASP A 1 280 ? 92.258  93.442  121.093 1.00 39.34  ? 2071 ASP A CA    1 
ATOM   1646 C  C     . ASP A 1 280 ? 93.383  93.685  120.095 1.00 37.92  ? 2071 ASP A C     1 
ATOM   1647 O  O     . ASP A 1 280 ? 94.545  93.362  120.361 1.00 35.81  ? 2071 ASP A O     1 
ATOM   1648 C  CB    . ASP A 1 280 ? 91.410  92.243  120.671 1.00 43.92  ? 2071 ASP A CB    1 
ATOM   1649 C  CG    . ASP A 1 280 ? 90.726  91.573  121.844 1.00 52.54  ? 2071 ASP A CG    1 
ATOM   1650 O  OD1   . ASP A 1 280 ? 91.305  91.577  122.950 1.00 53.21  ? 2071 ASP A OD1   1 
ATOM   1651 O  OD2   . ASP A 1 280 ? 89.609  91.044  121.661 1.00 57.15  ? 2071 ASP A OD2   1 
ATOM   1652 N  N     . VAL A 1 281 ? 93.057  94.270  118.941 1.00 37.15  ? 2072 VAL A N     1 
ATOM   1653 C  CA    . VAL A 1 281 ? 94.093  94.611  117.973 1.00 30.57  ? 2072 VAL A CA    1 
ATOM   1654 C  C     . VAL A 1 281 ? 94.984  95.723  118.516 1.00 29.17  ? 2072 VAL A C     1 
ATOM   1655 O  O     . VAL A 1 281 ? 96.197  95.734  118.281 1.00 29.14  ? 2072 VAL A O     1 
ATOM   1656 C  CB    . VAL A 1 281 ? 93.461  94.986  116.620 1.00 31.28  ? 2072 VAL A CB    1 
ATOM   1657 C  CG1   . VAL A 1 281 ? 92.301  95.939  116.814 1.00 31.03  ? 2072 VAL A CG1   1 
ATOM   1658 C  CG2   . VAL A 1 281 ? 94.497  95.594  115.692 1.00 33.58  ? 2072 VAL A CG2   1 
ATOM   1659 N  N     . PHE A 1 282 ? 94.404  96.665  119.262 1.00 31.58  ? 2073 PHE A N     1 
ATOM   1660 C  CA    . PHE A 1 282 ? 95.190  97.777  119.786 1.00 29.73  ? 2073 PHE A CA    1 
ATOM   1661 C  C     . PHE A 1 282 ? 96.263  97.300  120.756 1.00 29.67  ? 2073 PHE A C     1 
ATOM   1662 O  O     . PHE A 1 282 ? 97.398  97.788  120.722 1.00 30.47  ? 2073 PHE A O     1 
ATOM   1663 C  CB    . PHE A 1 282 ? 94.276  98.795  120.466 1.00 30.54  ? 2073 PHE A CB    1 
ATOM   1664 C  CG    . PHE A 1 282 ? 95.015  99.849  121.237 1.00 29.91  ? 2073 PHE A CG    1 
ATOM   1665 C  CD1   . PHE A 1 282 ? 95.710  100.846 120.579 1.00 24.56  ? 2073 PHE A CD1   1 
ATOM   1666 C  CD2   . PHE A 1 282 ? 95.012  99.844  122.620 1.00 34.40  ? 2073 PHE A CD2   1 
ATOM   1667 C  CE1   . PHE A 1 282 ? 96.389  101.815 121.284 1.00 24.48  ? 2073 PHE A CE1   1 
ATOM   1668 C  CE2   . PHE A 1 282 ? 95.690  100.811 123.329 1.00 31.53  ? 2073 PHE A CE2   1 
ATOM   1669 C  CZ    . PHE A 1 282 ? 96.379  101.797 122.660 1.00 27.01  ? 2073 PHE A CZ    1 
ATOM   1670 N  N     . ARG A 1 283 ? 95.928  96.351  121.628 1.00 29.93  ? 2074 ARG A N     1 
ATOM   1671 C  CA    . ARG A 1 283 ? 96.850  95.926  122.673 1.00 28.28  ? 2074 ARG A CA    1 
ATOM   1672 C  C     . ARG A 1 283 ? 97.646  94.675  122.330 1.00 29.38  ? 2074 ARG A C     1 
ATOM   1673 O  O     . ARG A 1 283 ? 98.666  94.420  122.979 1.00 28.51  ? 2074 ARG A O     1 
ATOM   1674 C  CB    . ARG A 1 283 ? 96.097  95.678  123.985 1.00 36.49  ? 2074 ARG A CB    1 
ATOM   1675 C  CG    . ARG A 1 283 ? 96.312  96.751  125.035 1.00 41.41  ? 2074 ARG A CG    1 
ATOM   1676 C  CD    . ARG A 1 283 ? 95.993  96.220  126.421 1.00 42.82  ? 2074 ARG A CD    1 
ATOM   1677 N  NE    . ARG A 1 283 ? 94.700  95.549  126.465 1.00 44.07  ? 2074 ARG A NE    1 
ATOM   1678 C  CZ    . ARG A 1 283 ? 93.586  96.109  126.914 1.00 47.44  ? 2074 ARG A CZ    1 
ATOM   1679 N  NH1   . ARG A 1 283 ? 93.575  97.346  127.383 1.00 44.98  ? 2074 ARG A NH1   1 
ATOM   1680 N  NH2   . ARG A 1 283 ? 92.455  95.409  126.896 1.00 47.54  ? 2074 ARG A NH2   1 
ATOM   1681 N  N     . LYS A 1 284 ? 97.219  93.892  121.342 1.00 29.35  ? 2075 LYS A N     1 
ATOM   1682 C  CA    . LYS A 1 284 ? 97.888  92.637  121.023 1.00 28.94  ? 2075 LYS A CA    1 
ATOM   1683 C  C     . LYS A 1 284 ? 98.879  92.756  119.875 1.00 29.33  ? 2075 LYS A C     1 
ATOM   1684 O  O     . LYS A 1 284 ? 99.919  92.092  119.893 1.00 32.40  ? 2075 LYS A O     1 
ATOM   1685 C  CB    . LYS A 1 284 ? 96.853  91.558  120.689 1.00 31.39  ? 2075 LYS A CB    1 
ATOM   1686 C  CG    . LYS A 1 284 ? 96.078  91.051  121.894 1.00 34.14  ? 2075 LYS A CG    1 
ATOM   1687 C  CD    . LYS A 1 284 ? 96.898  90.060  122.698 1.00 38.59  ? 2075 LYS A CD    1 
ATOM   1688 C  CE    . LYS A 1 284 ? 97.112  88.772  121.922 1.00 39.81  ? 2075 LYS A CE    1 
ATOM   1689 N  NZ    . LYS A 1 284 ? 95.820  88.149  121.527 1.00 41.49  ? 2075 LYS A NZ    1 
ATOM   1690 N  N     . VAL A 1 285 ? 98.585  93.582  118.872 1.00 26.61  ? 2076 VAL A N     1 
ATOM   1691 C  CA    . VAL A 1 285 ? 99.440  93.745  117.703 1.00 23.02  ? 2076 VAL A CA    1 
ATOM   1692 C  C     . VAL A 1 285 ? 99.865  95.197  117.516 1.00 25.23  ? 2076 VAL A C     1 
ATOM   1693 O  O     . VAL A 1 285 ? 101.037 95.481  117.263 1.00 28.15  ? 2076 VAL A O     1 
ATOM   1694 C  CB    . VAL A 1 285 ? 98.757  93.203  116.424 1.00 25.96  ? 2076 VAL A CB    1 
ATOM   1695 C  CG1   . VAL A 1 285 ? 97.258  93.362  116.512 1.00 30.05  ? 2076 VAL A CG1   1 
ATOM   1696 C  CG2   . VAL A 1 285 ? 99.291  93.906  115.187 1.00 25.68  ? 2076 VAL A CG2   1 
ATOM   1697 N  N     . GLU A 1 286 ? 98.923  96.132  117.646 1.00 26.89  ? 2077 GLU A N     1 
ATOM   1698 C  CA    . GLU A 1 286 ? 99.206  97.524  117.305 1.00 24.74  ? 2077 GLU A CA    1 
ATOM   1699 C  C     . GLU A 1 286 ? 100.218 98.147  118.262 1.00 23.67  ? 2077 GLU A C     1 
ATOM   1700 O  O     . GLU A 1 286 ? 101.214 98.738  117.828 1.00 25.86  ? 2077 GLU A O     1 
ATOM   1701 C  CB    . GLU A 1 286 ? 97.910  98.330  117.296 1.00 25.75  ? 2077 GLU A CB    1 
ATOM   1702 C  CG    . GLU A 1 286 ? 98.041  99.674  116.626 1.00 24.74  ? 2077 GLU A CG    1 
ATOM   1703 C  CD    . GLU A 1 286 ? 98.599  99.564  115.226 1.00 34.30  ? 2077 GLU A CD    1 
ATOM   1704 O  OE1   . GLU A 1 286 ? 98.109  98.710  114.458 1.00 38.79  ? 2077 GLU A OE1   1 
ATOM   1705 O  OE2   . GLU A 1 286 ? 99.527  100.330 114.890 1.00 37.30  ? 2077 GLU A OE2   1 
ATOM   1706 N  N     . MET A 1 287 ? 99.989  98.024  119.564 1.00 23.34  ? 2078 MET A N     1 
ATOM   1707 C  CA    . MET A 1 287 ? 100.893 98.624  120.540 1.00 21.70  ? 2078 MET A CA    1 
ATOM   1708 C  C     . MET A 1 287 ? 102.191 97.831  120.676 1.00 23.66  ? 2078 MET A C     1 
ATOM   1709 O  O     . MET A 1 287 ? 103.259 98.438  120.833 1.00 24.94  ? 2078 MET A O     1 
ATOM   1710 C  CB    . MET A 1 287 ? 100.209 98.767  121.901 1.00 24.09  ? 2078 MET A CB    1 
ATOM   1711 C  CG    . MET A 1 287 ? 99.437  100.065 122.079 1.00 24.20  ? 2078 MET A CG    1 
ATOM   1712 S  SD    . MET A 1 287 ? 100.194 101.486 121.270 1.00 25.98  ? 2078 MET A SD    1 
ATOM   1713 C  CE    . MET A 1 287 ? 101.696 101.680 122.221 1.00 22.57  ? 2078 MET A CE    1 
ATOM   1714 N  N     . PRO A 1 288 ? 102.165 96.494  120.652 1.00 22.97  ? 2079 PRO A N     1 
ATOM   1715 C  CA    . PRO A 1 288 ? 103.440 95.770  120.542 1.00 23.57  ? 2079 PRO A CA    1 
ATOM   1716 C  C     . PRO A 1 288 ? 104.213 96.107  119.279 1.00 26.70  ? 2079 PRO A C     1 
ATOM   1717 O  O     . PRO A 1 288 ? 105.447 96.159  119.317 1.00 28.70  ? 2079 PRO A O     1 
ATOM   1718 C  CB    . PRO A 1 288 ? 103.007 94.300  120.579 1.00 22.82  ? 2079 PRO A CB    1 
ATOM   1719 C  CG    . PRO A 1 288 ? 101.760 94.313  121.363 1.00 24.84  ? 2079 PRO A CG    1 
ATOM   1720 C  CD    . PRO A 1 288 ? 101.056 95.569  120.955 1.00 24.71  ? 2079 PRO A CD    1 
ATOM   1721 N  N     . SER A 1 289 ? 103.530 96.361  118.159 1.00 25.77  ? 2080 SER A N     1 
ATOM   1722 C  CA    . SER A 1 289 ? 104.239 96.804  116.963 1.00 21.53  ? 2080 SER A CA    1 
ATOM   1723 C  C     . SER A 1 289 ? 104.797 98.208  117.138 1.00 22.62  ? 2080 SER A C     1 
ATOM   1724 O  O     . SER A 1 289 ? 105.854 98.521  116.587 1.00 24.42  ? 2080 SER A O     1 
ATOM   1725 C  CB    . SER A 1 289 ? 103.328 96.757  115.739 1.00 21.99  ? 2080 SER A CB    1 
ATOM   1726 O  OG    . SER A 1 289 ? 102.641 97.982  115.567 1.00 23.87  ? 2080 SER A OG    1 
ATOM   1727 N  N     . GLN A 1 290 ? 104.106 99.066  117.891 1.00 22.35  ? 2081 GLN A N     1 
ATOM   1728 C  CA    . GLN A 1 290 ? 104.671 100.370 118.224 1.00 21.42  ? 2081 GLN A CA    1 
ATOM   1729 C  C     . GLN A 1 290 ? 105.926 100.222 119.071 1.00 22.30  ? 2081 GLN A C     1 
ATOM   1730 O  O     . GLN A 1 290 ? 106.894 100.969 118.900 1.00 23.71  ? 2081 GLN A O     1 
ATOM   1731 C  CB    . GLN A 1 290 ? 103.634 101.224 118.947 1.00 19.80  ? 2081 GLN A CB    1 
ATOM   1732 C  CG    . GLN A 1 290 ? 102.676 101.930 118.019 1.00 18.88  ? 2081 GLN A CG    1 
ATOM   1733 C  CD    . GLN A 1 290 ? 103.297 103.144 117.373 1.00 24.92  ? 2081 GLN A CD    1 
ATOM   1734 O  OE1   . GLN A 1 290 ? 103.706 103.102 116.215 1.00 29.71  ? 2081 GLN A OE1   1 
ATOM   1735 N  NE2   . GLN A 1 290 ? 103.375 104.237 118.120 1.00 25.17  ? 2081 GLN A NE2   1 
ATOM   1736 N  N     . TYR A 1 291 ? 105.921 99.270  120.003 1.00 22.46  ? 2082 TYR A N     1 
ATOM   1737 C  CA    . TYR A 1 291 ? 107.121 98.990  120.786 1.00 23.48  ? 2082 TYR A CA    1 
ATOM   1738 C  C     . TYR A 1 291 ? 108.254 98.484  119.898 1.00 27.38  ? 2082 TYR A C     1 
ATOM   1739 O  O     . TYR A 1 291 ? 109.416 98.880  120.063 1.00 32.15  ? 2082 TYR A O     1 
ATOM   1740 C  CB    . TYR A 1 291 ? 106.794 97.978  121.883 1.00 23.00  ? 2082 TYR A CB    1 
ATOM   1741 C  CG    . TYR A 1 291 ? 107.999 97.322  122.506 1.00 24.72  ? 2082 TYR A CG    1 
ATOM   1742 C  CD1   . TYR A 1 291 ? 108.886 98.052  123.281 1.00 28.15  ? 2082 TYR A CD1   1 
ATOM   1743 C  CD2   . TYR A 1 291 ? 108.244 95.970  122.328 1.00 26.53  ? 2082 TYR A CD2   1 
ATOM   1744 C  CE1   . TYR A 1 291 ? 109.986 97.454  123.856 1.00 32.41  ? 2082 TYR A CE1   1 
ATOM   1745 C  CE2   . TYR A 1 291 ? 109.340 95.364  122.899 1.00 29.03  ? 2082 TYR A CE2   1 
ATOM   1746 C  CZ    . TYR A 1 291 ? 110.208 96.110  123.661 1.00 31.73  ? 2082 TYR A CZ    1 
ATOM   1747 O  OH    . TYR A 1 291 ? 111.304 95.509  124.231 1.00 35.19  ? 2082 TYR A OH    1 
ATOM   1748 N  N     . CYS A 1 292 ? 107.929 97.610  118.943 1.00 25.62  ? 2083 CYS A N     1 
ATOM   1749 C  CA    . CYS A 1 292 ? 108.932 97.136  117.994 1.00 22.50  ? 2083 CYS A CA    1 
ATOM   1750 C  C     . CYS A 1 292 ? 109.475 98.280  117.148 1.00 21.65  ? 2083 CYS A C     1 
ATOM   1751 O  O     . CYS A 1 292 ? 110.669 98.323  116.843 1.00 22.21  ? 2083 CYS A O     1 
ATOM   1752 C  CB    . CYS A 1 292 ? 108.341 96.045  117.103 1.00 23.62  ? 2083 CYS A CB    1 
ATOM   1753 S  SG    . CYS A 1 292 ? 107.776 94.575  117.986 1.00 34.78  ? 2083 CYS A SG    1 
ATOM   1754 N  N     . LEU A 1 293 ? 108.609 99.215  116.755 1.00 22.22  ? 2084 LEU A N     1 
ATOM   1755 C  CA    . LEU A 1 293 ? 109.055 100.374 115.987 1.00 20.48  ? 2084 LEU A CA    1 
ATOM   1756 C  C     . LEU A 1 293 ? 109.924 101.296 116.830 1.00 23.82  ? 2084 LEU A C     1 
ATOM   1757 O  O     . LEU A 1 293 ? 110.858 101.918 116.316 1.00 27.82  ? 2084 LEU A O     1 
ATOM   1758 C  CB    . LEU A 1 293 ? 107.854 101.134 115.438 1.00 19.95  ? 2084 LEU A CB    1 
ATOM   1759 C  CG    . LEU A 1 293 ? 107.135 100.466 114.273 1.00 19.42  ? 2084 LEU A CG    1 
ATOM   1760 C  CD1   . LEU A 1 293 ? 105.954 101.309 113.861 1.00 17.33  ? 2084 LEU A CD1   1 
ATOM   1761 C  CD2   . LEU A 1 293 ? 108.087 100.261 113.111 1.00 22.56  ? 2084 LEU A CD2   1 
ATOM   1762 N  N     . ALA A 1 294 ? 109.621 101.414 118.122 1.00 21.91  ? 2085 ALA A N     1 
ATOM   1763 C  CA    . ALA A 1 294 ? 110.499 102.160 119.016 1.00 21.81  ? 2085 ALA A CA    1 
ATOM   1764 C  C     . ALA A 1 294 ? 111.878 101.519 119.067 1.00 27.06  ? 2085 ALA A C     1 
ATOM   1765 O  O     . ALA A 1 294 ? 112.902 102.205 118.958 1.00 30.73  ? 2085 ALA A O     1 
ATOM   1766 C  CB    . ALA A 1 294 ? 109.886 102.239 120.413 1.00 22.01  ? 2085 ALA A CB    1 
ATOM   1767 N  N     . LEU A 1 295 ? 111.920 100.192 119.204 1.00 26.30  ? 2086 LEU A N     1 
ATOM   1768 C  CA    . LEU A 1 295 ? 113.201 99.492  119.169 1.00 26.42  ? 2086 LEU A CA    1 
ATOM   1769 C  C     . LEU A 1 295 ? 113.913 99.723  117.841 1.00 28.95  ? 2086 LEU A C     1 
ATOM   1770 O  O     . LEU A 1 295 ? 115.131 99.931  117.808 1.00 34.28  ? 2086 LEU A O     1 
ATOM   1771 C  CB    . LEU A 1 295 ? 112.996 97.999  119.420 1.00 23.91  ? 2086 LEU A CB    1 
ATOM   1772 C  CG    . LEU A 1 295 ? 112.375 97.618  120.763 1.00 26.09  ? 2086 LEU A CG    1 
ATOM   1773 C  CD1   . LEU A 1 295 ? 112.469 96.121  120.985 1.00 27.25  ? 2086 LEU A CD1   1 
ATOM   1774 C  CD2   . LEU A 1 295 ? 113.048 98.372  121.894 1.00 30.71  ? 2086 LEU A CD2   1 
ATOM   1775 N  N     . LEU A 1 296 ? 113.161 99.702  116.739 1.00 23.69  ? 2087 LEU A N     1 
ATOM   1776 C  CA    . LEU A 1 296 ? 113.725 99.999  115.426 1.00 22.16  ? 2087 LEU A CA    1 
ATOM   1777 C  C     . LEU A 1 296 ? 114.361 101.381 115.407 1.00 26.31  ? 2087 LEU A C     1 
ATOM   1778 O  O     . LEU A 1 296 ? 115.452 101.568 114.860 1.00 30.54  ? 2087 LEU A O     1 
ATOM   1779 C  CB    . LEU A 1 296 ? 112.631 99.900  114.360 1.00 21.07  ? 2087 LEU A CB    1 
ATOM   1780 C  CG    . LEU A 1 296 ? 112.965 100.109 112.879 1.00 18.02  ? 2087 LEU A CG    1 
ATOM   1781 C  CD1   . LEU A 1 296 ? 111.927 99.427  112.018 1.00 18.41  ? 2087 LEU A CD1   1 
ATOM   1782 C  CD2   . LEU A 1 296 ? 113.048 101.577 112.496 1.00 19.64  ? 2087 LEU A CD2   1 
ATOM   1783 N  N     . GLU A 1 297 ? 113.671 102.371 115.973 1.00 24.25  ? 2088 GLU A N     1 
ATOM   1784 C  CA    . GLU A 1 297 ? 114.211 103.724 116.000 1.00 23.68  ? 2088 GLU A CA    1 
ATOM   1785 C  C     . GLU A 1 297 ? 115.463 103.807 116.857 1.00 25.27  ? 2088 GLU A C     1 
ATOM   1786 O  O     . GLU A 1 297 ? 116.363 104.602 116.563 1.00 30.31  ? 2088 GLU A O     1 
ATOM   1787 C  CB    . GLU A 1 297 ? 113.156 104.708 116.503 1.00 24.40  ? 2088 GLU A CB    1 
ATOM   1788 C  CG    . GLU A 1 297 ? 111.972 104.883 115.572 1.00 22.40  ? 2088 GLU A CG    1 
ATOM   1789 C  CD    . GLU A 1 297 ? 111.109 106.067 115.956 1.00 30.80  ? 2088 GLU A CD    1 
ATOM   1790 O  OE1   . GLU A 1 297 ? 111.574 106.906 116.756 1.00 35.42  ? 2088 GLU A OE1   1 
ATOM   1791 O  OE2   . GLU A 1 297 ? 109.964 106.160 115.467 1.00 30.72  ? 2088 GLU A OE2   1 
ATOM   1792 N  N     . LEU A 1 298 ? 115.540 103.011 117.926 1.00 22.39  ? 2089 LEU A N     1 
ATOM   1793 C  CA    . LEU A 1 298 ? 116.757 103.030 118.733 1.00 26.00  ? 2089 LEU A CA    1 
ATOM   1794 C  C     . LEU A 1 298 ? 117.918 102.341 118.019 1.00 26.70  ? 2089 LEU A C     1 
ATOM   1795 O  O     . LEU A 1 298 ? 119.071 102.765 118.160 1.00 33.00  ? 2089 LEU A O     1 
ATOM   1796 C  CB    . LEU A 1 298 ? 116.524 102.410 120.113 1.00 28.33  ? 2089 LEU A CB    1 
ATOM   1797 C  CG    . LEU A 1 298 ? 115.789 103.277 121.148 1.00 32.91  ? 2089 LEU A CG    1 
ATOM   1798 C  CD1   . LEU A 1 298 ? 114.384 102.797 121.444 1.00 31.03  ? 2089 LEU A CD1   1 
ATOM   1799 C  CD2   . LEU A 1 298 ? 116.585 103.403 122.428 1.00 35.43  ? 2089 LEU A CD2   1 
ATOM   1800 N  N     . ASN A 1 299 ? 117.647 101.284 117.247 1.00 27.37  ? 2090 ASN A N     1 
ATOM   1801 C  CA    . ASN A 1 299 ? 118.714 100.669 116.458 1.00 28.09  ? 2090 ASN A CA    1 
ATOM   1802 C  C     . ASN A 1 299 ? 119.074 101.529 115.253 1.00 30.87  ? 2090 ASN A C     1 
ATOM   1803 O  O     . ASN A 1 299 ? 120.226 101.944 115.091 1.00 34.64  ? 2090 ASN A O     1 
ATOM   1804 C  CB    . ASN A 1 299 ? 118.328 99.259  115.998 1.00 26.64  ? 2090 ASN A CB    1 
ATOM   1805 C  CG    . ASN A 1 299 ? 117.682 98.440  117.084 1.00 28.14  ? 2090 ASN A CG    1 
ATOM   1806 O  OD1   . ASN A 1 299 ? 118.228 98.301  118.172 1.00 37.60  ? 2090 ASN A OD1   1 
ATOM   1807 N  ND2   . ASN A 1 299 ? 116.537 97.847  116.778 1.00 23.83  ? 2090 ASN A ND2   1 
ATOM   1808 N  N     . GLY A 1 300 ? 118.104 101.783 114.381 1.00 27.46  ? 2091 GLY A N     1 
ATOM   1809 C  CA    . GLY A 1 300 ? 118.346 102.553 113.180 1.00 23.27  ? 2091 GLY A CA    1 
ATOM   1810 C  C     . GLY A 1 300 ? 118.992 101.725 112.092 1.00 28.62  ? 2091 GLY A C     1 
ATOM   1811 O  O     . GLY A 1 300 ? 119.851 100.886 112.374 1.00 29.11  ? 2091 GLY A O     1 
ATOM   1812 N  N     . ILE A 1 301 ? 118.579 101.943 110.842 1.00 32.32  ? 2092 ILE A N     1 
ATOM   1813 C  CA    . ILE A 1 301 ? 119.184 101.240 109.720 1.00 24.01  ? 2092 ILE A CA    1 
ATOM   1814 C  C     . ILE A 1 301 ? 120.649 101.644 109.598 1.00 26.05  ? 2092 ILE A C     1 
ATOM   1815 O  O     . ILE A 1 301 ? 121.037 102.774 109.919 1.00 34.93  ? 2092 ILE A O     1 
ATOM   1816 C  CB    . ILE A 1 301 ? 118.405 101.529 108.424 1.00 20.39  ? 2092 ILE A CB    1 
ATOM   1817 C  CG1   . ILE A 1 301 ? 118.983 100.741 107.247 1.00 23.58  ? 2092 ILE A CG1   1 
ATOM   1818 C  CG2   . ILE A 1 301 ? 118.397 103.015 108.129 1.00 26.20  ? 2092 ILE A CG2   1 
ATOM   1819 C  CD1   . ILE A 1 301 ? 118.854 99.244  107.388 1.00 27.38  ? 2092 ILE A CD1   1 
ATOM   1820 N  N     . GLY A 1 302 ? 121.477 100.706 109.156 1.00 22.58  ? 2093 GLY A N     1 
ATOM   1821 C  CA    . GLY A 1 302 ? 122.896 100.962 109.047 1.00 28.84  ? 2093 GLY A CA    1 
ATOM   1822 C  C     . GLY A 1 302 ? 123.239 101.882 107.892 1.00 34.22  ? 2093 GLY A C     1 
ATOM   1823 O  O     . GLY A 1 302 ? 122.423 102.190 107.025 1.00 35.31  ? 2093 GLY A O     1 
ATOM   1824 N  N     . PHE A 1 303 ? 124.488 102.342 107.895 1.00 36.16  ? 2094 PHE A N     1 
ATOM   1825 C  CA    . PHE A 1 303 ? 125.004 103.172 106.818 1.00 37.15  ? 2094 PHE A CA    1 
ATOM   1826 C  C     . PHE A 1 303 ? 126.516 103.023 106.769 1.00 43.90  ? 2094 PHE A C     1 
ATOM   1827 O  O     . PHE A 1 303 ? 127.164 102.782 107.791 1.00 48.70  ? 2094 PHE A O     1 
ATOM   1828 C  CB    . PHE A 1 303 ? 124.616 104.642 106.993 1.00 38.85  ? 2094 PHE A CB    1 
ATOM   1829 C  CG    . PHE A 1 303 ? 124.438 105.378 105.699 1.00 42.86  ? 2094 PHE A CG    1 
ATOM   1830 C  CD1   . PHE A 1 303 ? 123.402 105.058 104.844 1.00 41.79  ? 2094 PHE A CD1   1 
ATOM   1831 C  CD2   . PHE A 1 303 ? 125.307 106.391 105.337 1.00 50.78  ? 2094 PHE A CD2   1 
ATOM   1832 C  CE1   . PHE A 1 303 ? 123.236 105.733 103.653 1.00 43.46  ? 2094 PHE A CE1   1 
ATOM   1833 C  CE2   . PHE A 1 303 ? 125.145 107.071 104.148 1.00 48.40  ? 2094 PHE A CE2   1 
ATOM   1834 C  CZ    . PHE A 1 303 ? 124.108 106.741 103.305 1.00 44.74  ? 2094 PHE A CZ    1 
ATOM   1835 N  N     . SER A 1 304 ? 127.074 103.172 105.566 1.00 44.22  ? 2095 SER A N     1 
ATOM   1836 C  CA    . SER A 1 304 ? 128.493 102.942 105.343 1.00 50.29  ? 2095 SER A CA    1 
ATOM   1837 C  C     . SER A 1 304 ? 129.282 104.203 105.030 1.00 55.36  ? 2095 SER A C     1 
ATOM   1838 O  O     . SER A 1 304 ? 130.502 104.199 105.219 1.00 62.42  ? 2095 SER A O     1 
ATOM   1839 C  CB    . SER A 1 304 ? 128.697 101.938 104.200 1.00 51.05  ? 2095 SER A CB    1 
ATOM   1840 O  OG    . SER A 1 304 ? 130.057 101.555 104.095 1.00 56.42  ? 2095 SER A OG    1 
ATOM   1841 N  N     . THR A 1 305 ? 128.618 105.266 104.566 1.00 52.31  ? 2096 THR A N     1 
ATOM   1842 C  CA    . THR A 1 305 ? 129.230 106.545 104.206 1.00 57.99  ? 2096 THR A CA    1 
ATOM   1843 C  C     . THR A 1 305 ? 130.127 106.423 102.978 1.00 60.66  ? 2096 THR A C     1 
ATOM   1844 O  O     . THR A 1 305 ? 129.845 107.036 101.945 1.00 62.06  ? 2096 THR A O     1 
ATOM   1845 C  CB    . THR A 1 305 ? 130.018 107.135 105.381 1.00 58.08  ? 2096 THR A CB    1 
ATOM   1846 O  OG1   . THR A 1 305 ? 129.113 107.496 106.432 1.00 56.73  ? 2096 THR A OG1   1 
ATOM   1847 C  CG2   . THR A 1 305 ? 130.783 108.373 104.940 1.00 58.44  ? 2096 THR A CG2   1 
ATOM   1848 N  N     . ALA A 1 306 ? 131.213 105.652 103.081 1.00 61.21  ? 2097 ALA A N     1 
ATOM   1849 C  CA    . ALA A 1 306 ? 132.141 105.515 101.963 1.00 63.10  ? 2097 ALA A CA    1 
ATOM   1850 C  C     . ALA A 1 306 ? 131.460 104.906 100.743 1.00 64.02  ? 2097 ALA A C     1 
ATOM   1851 O  O     . ALA A 1 306 ? 131.703 105.338 99.609  1.00 65.57  ? 2097 ALA A O     1 
ATOM   1852 C  CB    . ALA A 1 306 ? 133.344 104.671 102.383 1.00 61.55  ? 2097 ALA A CB    1 
ATOM   1853 N  N     . GLU A 1 307 ? 130.615 103.894 100.951 1.00 60.54  ? 2098 GLU A N     1 
ATOM   1854 C  CA    . GLU A 1 307 ? 129.892 103.296 99.832  1.00 59.32  ? 2098 GLU A CA    1 
ATOM   1855 C  C     . GLU A 1 307 ? 128.963 104.308 99.175  1.00 61.32  ? 2098 GLU A C     1 
ATOM   1856 O  O     . GLU A 1 307 ? 128.882 104.384 97.942  1.00 67.57  ? 2098 GLU A O     1 
ATOM   1857 C  CB    . GLU A 1 307 ? 129.106 102.075 100.307 1.00 56.25  ? 2098 GLU A CB    1 
ATOM   1858 C  CG    . GLU A 1 307 ? 129.884 100.774 100.244 1.00 55.35  ? 2098 GLU A CG    1 
ATOM   1859 C  CD    . GLU A 1 307 ? 129.969 100.214 98.838  1.00 60.53  ? 2098 GLU A CD    1 
ATOM   1860 O  OE1   . GLU A 1 307 ? 129.170 100.640 97.978  1.00 56.87  ? 2098 GLU A OE1   1 
ATOM   1861 O  OE2   . GLU A 1 307 ? 130.834 99.347  98.594  1.00 62.83  ? 2098 GLU A OE2   1 
ATOM   1862 N  N     . CYS A 1 308 ? 128.256 105.100 99.985  1.00 56.90  ? 2099 CYS A N     1 
ATOM   1863 C  CA    . CYS A 1 308 ? 127.404 106.144 99.429  1.00 57.04  ? 2099 CYS A CA    1 
ATOM   1864 C  C     . CYS A 1 308 ? 128.224 107.203 98.708  1.00 60.28  ? 2099 CYS A C     1 
ATOM   1865 O  O     . CYS A 1 308 ? 127.782 107.736 97.687  1.00 61.03  ? 2099 CYS A O     1 
ATOM   1866 C  CB    . CYS A 1 308 ? 126.561 106.782 100.532 1.00 58.87  ? 2099 CYS A CB    1 
ATOM   1867 S  SG    . CYS A 1 308 ? 125.335 107.963 99.931  1.00 66.99  ? 2099 CYS A SG    1 
ATOM   1868 N  N     . GLU A 1 309 ? 129.417 107.521 99.218  1.00 61.78  ? 2100 GLU A N     1 
ATOM   1869 C  CA    . GLU A 1 309 ? 130.285 108.474 98.534  1.00 63.15  ? 2100 GLU A CA    1 
ATOM   1870 C  C     . GLU A 1 309 ? 130.721 107.950 97.172  1.00 63.85  ? 2100 GLU A C     1 
ATOM   1871 O  O     . GLU A 1 309 ? 130.726 108.694 96.186  1.00 65.95  ? 2100 GLU A O     1 
ATOM   1872 C  CB    . GLU A 1 309 ? 131.505 108.790 99.399  1.00 64.09  ? 2100 GLU A CB    1 
ATOM   1873 C  CG    . GLU A 1 309 ? 131.212 109.687 100.589 1.00 67.17  ? 2100 GLU A CG    1 
ATOM   1874 C  CD    . GLU A 1 309 ? 131.004 111.134 100.190 1.00 67.64  ? 2100 GLU A CD    1 
ATOM   1875 O  OE1   . GLU A 1 309 ? 131.447 111.517 99.087  1.00 69.85  ? 2100 GLU A OE1   1 
ATOM   1876 O  OE2   . GLU A 1 309 ? 130.399 111.890 100.979 1.00 63.95  ? 2100 GLU A OE2   1 
ATOM   1877 N  N     . SER A 1 310 ? 131.096 106.670 97.098  1.00 61.82  ? 2101 SER A N     1 
ATOM   1878 C  CA    . SER A 1 310 ? 131.486 106.089 95.817  1.00 62.19  ? 2101 SER A CA    1 
ATOM   1879 C  C     . SER A 1 310 ? 130.317 106.072 94.841  1.00 61.82  ? 2101 SER A C     1 
ATOM   1880 O  O     . SER A 1 310 ? 130.477 106.403 93.656  1.00 63.58  ? 2101 SER A O     1 
ATOM   1881 C  CB    . SER A 1 310 ? 132.028 104.676 96.027  1.00 63.71  ? 2101 SER A CB    1 
ATOM   1882 O  OG    . SER A 1 310 ? 132.286 104.041 94.788  1.00 75.03  ? 2101 SER A OG    1 
ATOM   1883 N  N     . GLN A 1 311 ? 129.131 105.692 95.323  1.00 60.31  ? 2102 GLN A N     1 
ATOM   1884 C  CA    . GLN A 1 311 ? 127.951 105.704 94.467  1.00 57.82  ? 2102 GLN A CA    1 
ATOM   1885 C  C     . GLN A 1 311 ? 127.651 107.111 93.971  1.00 63.07  ? 2102 GLN A C     1 
ATOM   1886 O  O     . GLN A 1 311 ? 127.329 107.305 92.795  1.00 64.91  ? 2102 GLN A O     1 
ATOM   1887 C  CB    . GLN A 1 311 ? 126.749 105.130 95.217  1.00 54.46  ? 2102 GLN A CB    1 
ATOM   1888 C  CG    . GLN A 1 311 ? 126.284 103.776 94.711  1.00 53.79  ? 2102 GLN A CG    1 
ATOM   1889 C  CD    . GLN A 1 311 ? 127.326 102.692 94.899  1.00 57.99  ? 2102 GLN A CD    1 
ATOM   1890 O  OE1   . GLN A 1 311 ? 127.485 102.151 95.993  1.00 58.40  ? 2102 GLN A OE1   1 
ATOM   1891 N  NE2   . GLN A 1 311 ? 128.041 102.365 93.829  1.00 58.37  ? 2102 GLN A NE2   1 
ATOM   1892 N  N     . LYS A 1 312 ? 127.762 108.108 94.854  1.00 62.76  ? 2103 LYS A N     1 
ATOM   1893 C  CA    . LYS A 1 312 ? 127.510 109.488 94.458  1.00 62.45  ? 2103 LYS A CA    1 
ATOM   1894 C  C     . LYS A 1 312 ? 128.525 109.961 93.428  1.00 66.08  ? 2103 LYS A C     1 
ATOM   1895 O  O     . LYS A 1 312 ? 128.169 110.659 92.475  1.00 67.44  ? 2103 LYS A O     1 
ATOM   1896 C  CB    . LYS A 1 312 ? 127.532 110.401 95.685  1.00 63.68  ? 2103 LYS A CB    1 
ATOM   1897 C  CG    . LYS A 1 312 ? 127.534 111.886 95.349  1.00 66.45  ? 2103 LYS A CG    1 
ATOM   1898 C  CD    . LYS A 1 312 ? 127.505 112.748 96.600  1.00 67.25  ? 2103 LYS A CD    1 
ATOM   1899 C  CE    . LYS A 1 312 ? 128.802 112.634 97.381  1.00 64.79  ? 2103 LYS A CE    1 
ATOM   1900 N  NZ    . LYS A 1 312 ? 128.809 113.529 98.570  1.00 63.92  ? 2103 LYS A NZ    1 
ATOM   1901 N  N     . HIS A 1 313 ? 129.796 109.601 93.608  1.00 68.05  ? 2104 HIS A N     1 
ATOM   1902 C  CA    . HIS A 1 313 ? 130.821 110.011 92.653  1.00 66.88  ? 2104 HIS A CA    1 
ATOM   1903 C  C     . HIS A 1 313 ? 130.559 109.410 91.278  1.00 66.34  ? 2104 HIS A C     1 
ATOM   1904 O  O     . HIS A 1 313 ? 130.630 110.107 90.258  1.00 67.43  ? 2104 HIS A O     1 
ATOM   1905 C  CB    . HIS A 1 313 ? 132.203 109.610 93.166  1.00 68.35  ? 2104 HIS A CB    1 
ATOM   1906 C  CG    . HIS A 1 313 ? 132.738 110.518 94.229  1.00 70.83  ? 2104 HIS A CG    1 
ATOM   1907 N  ND1   . HIS A 1 313 ? 132.184 111.750 94.502  1.00 68.32  ? 2104 HIS A ND1   1 
ATOM   1908 C  CD2   . HIS A 1 313 ? 133.774 110.372 95.088  1.00 70.24  ? 2104 HIS A CD2   1 
ATOM   1909 C  CE1   . HIS A 1 313 ? 132.856 112.324 95.484  1.00 67.93  ? 2104 HIS A CE1   1 
ATOM   1910 N  NE2   . HIS A 1 313 ? 133.826 111.509 95.857  1.00 69.68  ? 2104 HIS A NE2   1 
ATOM   1911 N  N     . ILE A 1 314 ? 130.235 108.115 91.233  1.00 67.48  ? 2105 ILE A N     1 
ATOM   1912 C  CA    . ILE A 1 314 ? 129.951 107.475 89.949  1.00 67.78  ? 2105 ILE A CA    1 
ATOM   1913 C  C     . ILE A 1 314 ? 128.703 108.079 89.314  1.00 67.91  ? 2105 ILE A C     1 
ATOM   1914 O  O     . ILE A 1 314 ? 128.663 108.335 88.102  1.00 70.76  ? 2105 ILE A O     1 
ATOM   1915 C  CB    . ILE A 1 314 ? 129.820 105.951 90.127  1.00 65.10  ? 2105 ILE A CB    1 
ATOM   1916 C  CG1   . ILE A 1 314 ? 131.156 105.353 90.571  1.00 64.21  ? 2105 ILE A CG1   1 
ATOM   1917 C  CG2   . ILE A 1 314 ? 129.349 105.301 88.838  1.00 64.49  ? 2105 ILE A CG2   1 
ATOM   1918 C  CD1   . ILE A 1 314 ? 131.145 103.846 90.676  1.00 65.58  ? 2105 ILE A CD1   1 
ATOM   1919 N  N     . MET A 1 315 ? 127.668 108.321 90.122  1.00 66.04  ? 2106 MET A N     1 
ATOM   1920 C  CA    . MET A 1 315 ? 126.430 108.888 89.601  1.00 65.27  ? 2106 MET A CA    1 
ATOM   1921 C  C     . MET A 1 315 ? 126.654 110.293 89.058  1.00 70.61  ? 2106 MET A C     1 
ATOM   1922 O  O     . MET A 1 315 ? 126.104 110.655 88.015  1.00 72.47  ? 2106 MET A O     1 
ATOM   1923 C  CB    . MET A 1 315 ? 125.365 108.899 90.696  1.00 64.12  ? 2106 MET A CB    1 
ATOM   1924 C  CG    . MET A 1 315 ? 124.064 108.225 90.309  1.00 59.98  ? 2106 MET A CG    1 
ATOM   1925 S  SD    . MET A 1 315 ? 122.983 107.954 91.724  1.00 61.17  ? 2106 MET A SD    1 
ATOM   1926 C  CE    . MET A 1 315 ? 124.115 107.193 92.881  1.00 62.13  ? 2106 MET A CE    1 
ATOM   1927 N  N     . GLN A 1 316 ? 127.460 111.100 89.752  1.00 70.47  ? 2107 GLN A N     1 
ATOM   1928 C  CA    . GLN A 1 316 ? 127.750 112.451 89.282  1.00 70.68  ? 2107 GLN A CA    1 
ATOM   1929 C  C     . GLN A 1 316 ? 128.594 112.427 88.016  1.00 73.31  ? 2107 GLN A C     1 
ATOM   1930 O  O     . GLN A 1 316 ? 128.399 113.256 87.120  1.00 75.73  ? 2107 GLN A O     1 
ATOM   1931 C  CB    . GLN A 1 316 ? 128.452 113.251 90.379  1.00 70.66  ? 2107 GLN A CB    1 
ATOM   1932 C  CG    . GLN A 1 316 ? 127.525 114.135 91.195  1.00 70.50  ? 2107 GLN A CG    1 
ATOM   1933 C  CD    . GLN A 1 316 ? 128.228 114.788 92.368  1.00 70.64  ? 2107 GLN A CD    1 
ATOM   1934 O  OE1   . GLN A 1 316 ? 129.373 115.223 92.256  1.00 70.13  ? 2107 GLN A OE1   1 
ATOM   1935 N  NE2   . GLN A 1 316 ? 127.543 114.859 93.503  1.00 67.71  ? 2107 GLN A NE2   1 
ATOM   1936 N  N     . ALA A 1 317 ? 129.543 111.493 87.923  1.00 72.35  ? 2108 ALA A N     1 
ATOM   1937 C  CA    . ALA A 1 317 ? 130.322 111.359 86.697  1.00 73.87  ? 2108 ALA A CA    1 
ATOM   1938 C  C     . ALA A 1 317 ? 129.422 111.009 85.519  1.00 74.01  ? 2108 ALA A C     1 
ATOM   1939 O  O     . ALA A 1 317 ? 129.539 111.592 84.434  1.00 78.19  ? 2108 ALA A O     1 
ATOM   1940 C  CB    . ALA A 1 317 ? 131.412 110.303 86.880  1.00 72.96  ? 2108 ALA A CB    1 
ATOM   1941 N  N     . LYS A 1 318 ? 128.501 110.064 85.722  1.00 73.32  ? 2109 LYS A N     1 
ATOM   1942 C  CA    . LYS A 1 318 ? 127.574 109.709 84.652  1.00 75.79  ? 2109 LYS A CA    1 
ATOM   1943 C  C     . LYS A 1 318 ? 126.625 110.855 84.327  1.00 75.64  ? 2109 LYS A C     1 
ATOM   1944 O  O     . LYS A 1 318 ? 126.269 111.048 83.161  1.00 79.63  ? 2109 LYS A O     1 
ATOM   1945 C  CB    . LYS A 1 318 ? 126.786 108.455 85.025  1.00 77.78  ? 2109 LYS A CB    1 
ATOM   1946 C  CG    . LYS A 1 318 ? 125.866 107.965 83.921  1.00 77.85  ? 2109 LYS A CG    1 
ATOM   1947 C  CD    . LYS A 1 318 ? 126.625 107.756 82.623  1.00 82.72  ? 2109 LYS A CD    1 
ATOM   1948 C  CE    . LYS A 1 318 ? 125.676 107.524 81.461  1.00 83.24  ? 2109 LYS A CE    1 
ATOM   1949 N  NZ    . LYS A 1 318 ? 124.847 106.303 81.650  1.00 85.53  ? 2109 LYS A NZ    1 
ATOM   1950 N  N     . LEU A 1 319 ? 126.207 111.621 85.336  1.00 74.30  ? 2110 LEU A N     1 
ATOM   1951 C  CA    . LEU A 1 319 ? 125.362 112.785 85.092  1.00 77.76  ? 2110 LEU A CA    1 
ATOM   1952 C  C     . LEU A 1 319 ? 126.085 113.823 84.246  1.00 84.00  ? 2110 LEU A C     1 
ATOM   1953 O  O     . LEU A 1 319 ? 125.503 114.393 83.317  1.00 86.29  ? 2110 LEU A O     1 
ATOM   1954 C  CB    . LEU A 1 319 ? 124.921 113.394 86.423  1.00 75.81  ? 2110 LEU A CB    1 
ATOM   1955 C  CG    . LEU A 1 319 ? 123.622 114.198 86.426  1.00 74.74  ? 2110 LEU A CG    1 
ATOM   1956 C  CD1   . LEU A 1 319 ? 122.474 113.338 85.953  1.00 70.67  ? 2110 LEU A CD1   1 
ATOM   1957 C  CD2   . LEU A 1 319 ? 123.341 114.754 87.814  1.00 69.29  ? 2110 LEU A CD2   1 
ATOM   1958 N  N     . ASP A 1 320 ? 127.358 114.081 84.555  1.00 83.75  ? 2111 ASP A N     1 
ATOM   1959 C  CA    . ASP A 1 320 ? 128.139 115.023 83.762  1.00 80.32  ? 2111 ASP A CA    1 
ATOM   1960 C  C     . ASP A 1 320 ? 128.328 114.516 82.339  1.00 82.33  ? 2111 ASP A C     1 
ATOM   1961 O  O     . ASP A 1 320 ? 128.243 115.293 81.379  1.00 86.82  ? 2111 ASP A O     1 
ATOM   1962 C  CB    . ASP A 1 320 ? 129.491 115.275 84.429  1.00 81.21  ? 2111 ASP A CB    1 
ATOM   1963 C  CG    . ASP A 1 320 ? 129.365 116.043 85.730  1.00 85.16  ? 2111 ASP A CG    1 
ATOM   1964 O  OD1   . ASP A 1 320 ? 128.235 116.445 86.077  1.00 83.97  ? 2111 ASP A OD1   1 
ATOM   1965 O  OD2   . ASP A 1 320 ? 130.395 116.244 86.406  1.00 89.27  ? 2111 ASP A OD2   1 
ATOM   1966 N  N     . ALA A 1 321 ? 128.584 113.215 82.181  1.00 81.44  ? 2112 ALA A N     1 
ATOM   1967 C  CA    . ALA A 1 321 ? 128.722 112.649 80.843  1.00 83.13  ? 2112 ALA A CA    1 
ATOM   1968 C  C     . ALA A 1 321 ? 127.428 112.786 80.049  1.00 86.63  ? 2112 ALA A C     1 
ATOM   1969 O  O     . ALA A 1 321 ? 127.451 113.145 78.866  1.00 90.93  ? 2112 ALA A O     1 
ATOM   1970 C  CB    . ALA A 1 321 ? 129.144 111.183 80.933  1.00 79.02  ? 2112 ALA A CB    1 
ATOM   1971 N  N     . ILE A 1 322 ? 126.289 112.512 80.687  1.00 85.14  ? 2113 ILE A N     1 
ATOM   1972 C  CA    . ILE A 1 322 ? 125.000 112.626 80.011  1.00 86.65  ? 2113 ILE A CA    1 
ATOM   1973 C  C     . ILE A 1 322 ? 124.729 114.074 79.628  1.00 90.94  ? 2113 ILE A C     1 
ATOM   1974 O  O     . ILE A 1 322 ? 124.251 114.362 78.524  1.00 95.11  ? 2113 ILE A O     1 
ATOM   1975 C  CB    . ILE A 1 322 ? 123.882 112.055 80.902  1.00 86.07  ? 2113 ILE A CB    1 
ATOM   1976 C  CG1   . ILE A 1 322 ? 123.819 110.533 80.768  1.00 87.59  ? 2113 ILE A CG1   1 
ATOM   1977 C  CG2   . ILE A 1 322 ? 122.537 112.667 80.544  1.00 82.42  ? 2113 ILE A CG2   1 
ATOM   1978 C  CD1   . ILE A 1 322 ? 123.665 110.048 79.350  1.00 85.04  ? 2113 ILE A CD1   1 
ATOM   1979 N  N     . GLU A 1 323 ? 125.027 115.007 80.535  1.00 89.74  ? 2114 GLU A N     1 
ATOM   1980 C  CA    . GLU A 1 323 ? 124.813 116.421 80.251  1.00 91.68  ? 2114 GLU A CA    1 
ATOM   1981 C  C     . GLU A 1 323 ? 125.675 116.890 79.085  1.00 97.18  ? 2114 GLU A C     1 
ATOM   1982 O  O     . GLU A 1 323 ? 125.192 117.599 78.194  1.00 99.24  ? 2114 GLU A O     1 
ATOM   1983 C  CB    . GLU A 1 323 ? 125.100 117.248 81.505  1.00 89.37  ? 2114 GLU A CB    1 
ATOM   1984 C  CG    . GLU A 1 323 ? 124.908 118.745 81.336  1.00 97.18  ? 2114 GLU A CG    1 
ATOM   1985 C  CD    . GLU A 1 323 ? 126.223 119.497 81.305  1.00 100.67 ? 2114 GLU A CD    1 
ATOM   1986 O  OE1   . GLU A 1 323 ? 127.253 118.884 80.954  1.00 100.41 ? 2114 GLU A OE1   1 
ATOM   1987 O  OE2   . GLU A 1 323 ? 126.231 120.699 81.645  1.00 99.47  ? 2114 GLU A OE2   1 
ATOM   1988 N  N     . THR A 1 324 ? 126.952 116.498 79.068  1.00 96.40  ? 2115 THR A N     1 
ATOM   1989 C  CA    . THR A 1 324 ? 127.824 116.891 77.966  1.00 95.07  ? 2115 THR A CA    1 
ATOM   1990 C  C     . THR A 1 324 ? 127.370 116.268 76.651  1.00 97.19  ? 2115 THR A C     1 
ATOM   1991 O  O     . THR A 1 324 ? 127.395 116.929 75.607  1.00 102.68 ? 2115 THR A O     1 
ATOM   1992 C  CB    . THR A 1 324 ? 129.274 116.511 78.268  1.00 93.93  ? 2115 THR A CB    1 
ATOM   1993 O  OG1   . THR A 1 324 ? 129.343 115.136 78.661  1.00 95.01  ? 2115 THR A OG1   1 
ATOM   1994 C  CG2   . THR A 1 324 ? 129.831 117.383 79.384  1.00 93.03  ? 2115 THR A CG2   1 
ATOM   1995 N  N     . GLN A 1 325 ? 126.950 115.000 76.679  1.00 95.88  ? 2116 GLN A N     1 
ATOM   1996 C  CA    . GLN A 1 325 ? 126.462 114.358 75.463  1.00 98.98  ? 2116 GLN A CA    1 
ATOM   1997 C  C     . GLN A 1 325 ? 125.214 115.054 74.933  1.00 103.52 ? 2116 GLN A C     1 
ATOM   1998 O  O     . GLN A 1 325 ? 125.088 115.284 73.724  1.00 107.42 ? 2116 GLN A O     1 
ATOM   1999 C  CB    . GLN A 1 325 ? 126.179 112.880 75.730  1.00 96.87  ? 2116 GLN A CB    1 
ATOM   2000 C  CG    . GLN A 1 325 ? 126.207 112.005 74.490  1.00 95.99  ? 2116 GLN A CG    1 
ATOM   2001 C  CD    . GLN A 1 325 ? 126.508 110.555 74.811  1.00 95.38  ? 2116 GLN A CD    1 
ATOM   2002 O  OE1   . GLN A 1 325 ? 127.558 110.235 75.367  1.00 95.04  ? 2116 GLN A OE1   1 
ATOM   2003 N  NE2   . GLN A 1 325 ? 125.583 109.668 74.461  1.00 95.25  ? 2116 GLN A NE2   1 
ATOM   2004 N  N     . ALA A 1 326 ? 124.283 115.402 75.823  1.00 102.18 ? 2117 ALA A N     1 
ATOM   2005 C  CA    . ALA A 1 326 ? 123.067 116.084 75.392  1.00 105.25 ? 2117 ALA A CA    1 
ATOM   2006 C  C     . ALA A 1 326 ? 123.372 117.479 74.860  1.00 107.79 ? 2117 ALA A C     1 
ATOM   2007 O  O     . ALA A 1 326 ? 122.758 117.924 73.883  1.00 110.14 ? 2117 ALA A O     1 
ATOM   2008 C  CB    . ALA A 1 326 ? 122.067 116.154 76.543  1.00 101.21 ? 2117 ALA A CB    1 
ATOM   2009 N  N     . TYR A 1 327 ? 124.310 118.188 75.492  1.00 105.04 ? 2118 TYR A N     1 
ATOM   2010 C  CA    . TYR A 1 327 ? 124.676 119.515 75.010  1.00 108.56 ? 2118 TYR A CA    1 
ATOM   2011 C  C     . TYR A 1 327 ? 125.363 119.435 73.653  1.00 110.85 ? 2118 TYR A C     1 
ATOM   2012 O  O     . TYR A 1 327 ? 125.185 120.319 72.808  1.00 112.68 ? 2118 TYR A O     1 
ATOM   2013 C  CB    . TYR A 1 327 ? 125.571 120.220 76.030  1.00 108.31 ? 2118 TYR A CB    1 
ATOM   2014 C  CG    . TYR A 1 327 ? 124.831 120.747 77.240  1.00 108.62 ? 2118 TYR A CG    1 
ATOM   2015 C  CD1   . TYR A 1 327 ? 123.491 120.446 77.447  1.00 108.18 ? 2118 TYR A CD1   1 
ATOM   2016 C  CD2   . TYR A 1 327 ? 125.472 121.549 78.174  1.00 107.69 ? 2118 TYR A CD2   1 
ATOM   2017 C  CE1   . TYR A 1 327 ? 122.813 120.923 78.549  1.00 106.58 ? 2118 TYR A CE1   1 
ATOM   2018 C  CE2   . TYR A 1 327 ? 124.800 122.034 79.279  1.00 106.70 ? 2118 TYR A CE2   1 
ATOM   2019 C  CZ    . TYR A 1 327 ? 123.471 121.717 79.462  1.00 106.00 ? 2118 TYR A CZ    1 
ATOM   2020 O  OH    . TYR A 1 327 ? 122.798 122.197 80.562  1.00 102.99 ? 2118 TYR A OH    1 
ATOM   2021 N  N     . GLN A 1 328 ? 126.164 118.391 73.434  1.00 109.19 ? 2119 GLN A N     1 
ATOM   2022 C  CA    . GLN A 1 328 ? 126.756 118.175 72.119  1.00 109.21 ? 2119 GLN A CA    1 
ATOM   2023 C  C     . GLN A 1 328 ? 125.687 117.863 71.079  1.00 110.94 ? 2119 GLN A C     1 
ATOM   2024 O  O     . GLN A 1 328 ? 125.748 118.359 69.948  1.00 112.78 ? 2119 GLN A O     1 
ATOM   2025 C  CB    . GLN A 1 328 ? 127.786 117.048 72.192  1.00 107.04 ? 2119 GLN A CB    1 
ATOM   2026 C  CG    . GLN A 1 328 ? 128.089 116.380 70.861  1.00 108.86 ? 2119 GLN A CG    1 
ATOM   2027 C  CD    . GLN A 1 328 ? 128.937 115.133 71.018  1.00 110.40 ? 2119 GLN A CD    1 
ATOM   2028 O  OE1   . GLN A 1 328 ? 129.498 114.880 72.083  1.00 109.23 ? 2119 GLN A OE1   1 
ATOM   2029 N  NE2   . GLN A 1 328 ? 129.034 114.347 69.952  1.00 110.17 ? 2119 GLN A NE2   1 
ATOM   2030 N  N     . LEU A 1 329 ? 124.696 117.047 71.446  1.00 108.97 ? 2120 LEU A N     1 
ATOM   2031 C  CA    . LEU A 1 329 ? 123.669 116.649 70.488  1.00 111.02 ? 2120 LEU A CA    1 
ATOM   2032 C  C     . LEU A 1 329 ? 122.778 117.825 70.105  1.00 113.26 ? 2120 LEU A C     1 
ATOM   2033 O  O     . LEU A 1 329 ? 122.533 118.068 68.918  1.00 114.90 ? 2120 LEU A O     1 
ATOM   2034 C  CB    . LEU A 1 329 ? 122.834 115.505 71.065  1.00 111.09 ? 2120 LEU A CB    1 
ATOM   2035 C  CG    . LEU A 1 329 ? 121.898 114.774 70.100  1.00 114.11 ? 2120 LEU A CG    1 
ATOM   2036 C  CD1   . LEU A 1 329 ? 121.922 113.277 70.365  1.00 110.52 ? 2120 LEU A CD1   1 
ATOM   2037 C  CD2   . LEU A 1 329 ? 120.478 115.312 70.205  1.00 110.97 ? 2120 LEU A CD2   1 
ATOM   2038 N  N     . ALA A 1 330 ? 122.283 118.567 71.094  1.00 113.20 ? 2121 ALA A N     1 
ATOM   2039 C  CA    . ALA A 1 330 ? 121.344 119.651 70.838  1.00 117.60 ? 2121 ALA A CA    1 
ATOM   2040 C  C     . ALA A 1 330 ? 122.017 121.001 70.623  1.00 117.43 ? 2121 ALA A C     1 
ATOM   2041 O  O     . ALA A 1 330 ? 121.328 121.970 70.286  1.00 116.81 ? 2121 ALA A O     1 
ATOM   2042 C  CB    . ALA A 1 330 ? 120.339 119.763 71.988  1.00 116.67 ? 2121 ALA A CB    1 
ATOM   2043 N  N     . GLY A 1 331 ? 123.330 121.092 70.809  1.00 114.85 ? 2122 GLY A N     1 
ATOM   2044 C  CA    . GLY A 1 331 ? 124.044 122.328 70.555  1.00 114.24 ? 2122 GLY A CA    1 
ATOM   2045 C  C     . GLY A 1 331 ? 124.132 123.269 71.740  1.00 117.83 ? 2122 GLY A C     1 
ATOM   2046 O  O     . GLY A 1 331 ? 125.232 123.607 72.186  1.00 120.40 ? 2122 GLY A O     1 
ATOM   2047 N  N     . HIS A 1 332 ? 122.986 123.700 72.260  1.00 119.03 ? 2123 HIS A N     1 
ATOM   2048 C  CA    . HIS A 1 332 ? 122.949 124.709 73.307  1.00 118.35 ? 2123 HIS A CA    1 
ATOM   2049 C  C     . HIS A 1 332 ? 123.025 124.047 74.684  1.00 114.51 ? 2123 HIS A C     1 
ATOM   2050 O  O     . HIS A 1 332 ? 123.333 122.860 74.816  1.00 110.93 ? 2123 HIS A O     1 
ATOM   2051 C  CB    . HIS A 1 332 ? 121.705 125.583 73.159  1.00 118.89 ? 2123 HIS A CB    1 
ATOM   2052 C  CG    . HIS A 1 332 ? 120.441 124.811 72.946  1.00 118.59 ? 2123 HIS A CG    1 
ATOM   2053 N  ND1   . HIS A 1 332 ? 119.575 124.504 73.973  1.00 116.18 ? 2123 HIS A ND1   1 
ATOM   2054 C  CD2   . HIS A 1 332 ? 119.893 124.289 71.823  1.00 118.00 ? 2123 HIS A CD2   1 
ATOM   2055 C  CE1   . HIS A 1 332 ? 118.549 123.825 73.493  1.00 117.60 ? 2123 HIS A CE1   1 
ATOM   2056 N  NE2   . HIS A 1 332 ? 118.718 123.680 72.191  1.00 118.60 ? 2123 HIS A NE2   1 
ATOM   2057 N  N     . SER A 1 333 ? 122.740 124.823 75.730  1.00 114.19 ? 2124 SER A N     1 
ATOM   2058 C  CA    . SER A 1 333 ? 122.904 124.371 77.107  1.00 112.42 ? 2124 SER A CA    1 
ATOM   2059 C  C     . SER A 1 333 ? 121.569 124.353 77.840  1.00 111.57 ? 2124 SER A C     1 
ATOM   2060 O  O     . SER A 1 333 ? 121.456 124.879 78.952  1.00 110.12 ? 2124 SER A O     1 
ATOM   2061 C  CB    . SER A 1 333 ? 123.903 125.264 77.847  1.00 111.46 ? 2124 SER A CB    1 
ATOM   2062 O  OG    . SER A 1 333 ? 125.185 125.203 77.247  1.00 113.00 ? 2124 SER A OG    1 
ATOM   2063 N  N     . PHE A 1 334 ? 120.553 123.766 77.210  1.00 112.02 ? 2125 PHE A N     1 
ATOM   2064 C  CA    . PHE A 1 334 ? 119.231 123.666 77.815  1.00 108.82 ? 2125 PHE A CA    1 
ATOM   2065 C  C     . PHE A 1 334 ? 119.300 122.950 79.160  1.00 106.35 ? 2125 PHE A C     1 
ATOM   2066 O  O     . PHE A 1 334 ? 120.011 121.955 79.319  1.00 105.11 ? 2125 PHE A O     1 
ATOM   2067 C  CB    . PHE A 1 334 ? 118.282 122.922 76.875  1.00 110.11 ? 2125 PHE A CB    1 
ATOM   2068 C  CG    . PHE A 1 334 ? 118.695 121.503 76.596  1.00 110.81 ? 2125 PHE A CG    1 
ATOM   2069 C  CD1   . PHE A 1 334 ? 119.695 121.221 75.680  1.00 112.86 ? 2125 PHE A CD1   1 
ATOM   2070 C  CD2   . PHE A 1 334 ? 118.089 120.451 77.257  1.00 106.80 ? 2125 PHE A CD2   1 
ATOM   2071 C  CE1   . PHE A 1 334 ? 120.078 119.917 75.431  1.00 111.22 ? 2125 PHE A CE1   1 
ATOM   2072 C  CE2   . PHE A 1 334 ? 118.465 119.145 77.010  1.00 103.94 ? 2125 PHE A CE2   1 
ATOM   2073 C  CZ    . PHE A 1 334 ? 119.460 118.878 76.095  1.00 107.03 ? 2125 PHE A CZ    1 
ATOM   2074 N  N     . SER A 1 335 ? 118.551 123.466 80.131  1.00 105.61 ? 2126 SER A N     1 
ATOM   2075 C  CA    . SER A 1 335 ? 118.568 122.915 81.480  1.00 102.32 ? 2126 SER A CA    1 
ATOM   2076 C  C     . SER A 1 335 ? 117.606 121.738 81.587  1.00 101.64 ? 2126 SER A C     1 
ATOM   2077 O  O     . SER A 1 335 ? 116.446 121.833 81.177  1.00 104.36 ? 2126 SER A O     1 
ATOM   2078 C  CB    . SER A 1 335 ? 118.202 123.994 82.498  1.00 98.28  ? 2126 SER A CB    1 
ATOM   2079 O  OG    . SER A 1 335 ? 118.230 123.479 83.818  1.00 96.08  ? 2126 SER A OG    1 
ATOM   2080 N  N     . PHE A 1 336 ? 118.096 120.626 82.142  1.00 97.90  ? 2127 PHE A N     1 
ATOM   2081 C  CA    . PHE A 1 336 ? 117.252 119.450 82.322  1.00 93.70  ? 2127 PHE A CA    1 
ATOM   2082 C  C     . PHE A 1 336 ? 116.155 119.700 83.350  1.00 97.94  ? 2127 PHE A C     1 
ATOM   2083 O  O     . PHE A 1 336 ? 115.029 119.214 83.194  1.00 98.13  ? 2127 PHE A O     1 
ATOM   2084 C  CB    . PHE A 1 336 ? 118.100 118.251 82.741  1.00 87.22  ? 2127 PHE A CB    1 
ATOM   2085 C  CG    . PHE A 1 336 ? 119.021 117.750 81.669  1.00 86.91  ? 2127 PHE A CG    1 
ATOM   2086 C  CD1   . PHE A 1 336 ? 118.548 116.928 80.660  1.00 84.98  ? 2127 PHE A CD1   1 
ATOM   2087 C  CD2   . PHE A 1 336 ? 120.362 118.092 81.675  1.00 86.86  ? 2127 PHE A CD2   1 
ATOM   2088 C  CE1   . PHE A 1 336 ? 119.394 116.462 79.676  1.00 83.64  ? 2127 PHE A CE1   1 
ATOM   2089 C  CE2   . PHE A 1 336 ? 121.211 117.628 80.693  1.00 87.19  ? 2127 PHE A CE2   1 
ATOM   2090 C  CZ    . PHE A 1 336 ? 120.727 116.813 79.693  1.00 84.60  ? 2127 PHE A CZ    1 
ATOM   2091 N  N     . THR A 1 337 ? 116.468 120.447 84.412  1.00 99.05  ? 2128 THR A N     1 
ATOM   2092 C  CA    . THR A 1 337 ? 115.503 120.668 85.484  1.00 98.79  ? 2128 THR A CA    1 
ATOM   2093 C  C     . THR A 1 337 ? 114.276 121.436 85.015  1.00 104.56 ? 2128 THR A C     1 
ATOM   2094 O  O     . THR A 1 337 ? 113.220 121.339 85.650  1.00 109.01 ? 2128 THR A O     1 
ATOM   2095 C  CB    . THR A 1 337 ? 116.162 121.415 86.646  1.00 97.98  ? 2128 THR A CB    1 
ATOM   2096 O  OG1   . THR A 1 337 ? 116.785 122.610 86.158  1.00 100.36 ? 2128 THR A OG1   1 
ATOM   2097 C  CG2   . THR A 1 337 ? 117.210 120.541 87.317  1.00 92.26  ? 2128 THR A CG2   1 
ATOM   2098 N  N     . SER A 1 338 ? 114.385 122.193 83.928  1.00 105.46 ? 2129 SER A N     1 
ATOM   2099 C  CA    . SER A 1 338 ? 113.268 122.973 83.412  1.00 107.97 ? 2129 SER A CA    1 
ATOM   2100 C  C     . SER A 1 338 ? 112.467 122.121 82.435  1.00 109.16 ? 2129 SER A C     1 
ATOM   2101 O  O     . SER A 1 338 ? 112.986 121.707 81.394  1.00 108.78 ? 2129 SER A O     1 
ATOM   2102 C  CB    . SER A 1 338 ? 113.765 124.248 82.733  1.00 108.86 ? 2129 SER A CB    1 
ATOM   2103 O  OG    . SER A 1 338 ? 112.683 125.002 82.214  1.00 111.65 ? 2129 SER A OG    1 
ATOM   2104 N  N     . SER A 1 339 ? 111.203 121.859 82.777  1.00 111.51 ? 2130 SER A N     1 
ATOM   2105 C  CA    . SER A 1 339 ? 110.338 121.095 81.885  1.00 113.09 ? 2130 SER A CA    1 
ATOM   2106 C  C     . SER A 1 339 ? 110.086 121.848 80.586  1.00 115.77 ? 2130 SER A C     1 
ATOM   2107 O  O     . SER A 1 339 ? 110.027 121.243 79.508  1.00 114.56 ? 2130 SER A O     1 
ATOM   2108 C  CB    . SER A 1 339 ? 109.018 120.772 82.584  1.00 113.75 ? 2130 SER A CB    1 
ATOM   2109 O  OG    . SER A 1 339 ? 108.105 120.161 81.690  1.00 116.09 ? 2130 SER A OG    1 
ATOM   2110 N  N     . ASP A 1 340 ? 109.925 123.172 80.671  1.00 118.02 ? 2131 ASP A N     1 
ATOM   2111 C  CA    . ASP A 1 340 ? 109.685 123.970 79.473  1.00 118.45 ? 2131 ASP A CA    1 
ATOM   2112 C  C     . ASP A 1 340 ? 110.863 123.891 78.511  1.00 117.83 ? 2131 ASP A C     1 
ATOM   2113 O  O     . ASP A 1 340 ? 110.673 123.768 77.296  1.00 118.43 ? 2131 ASP A O     1 
ATOM   2114 C  CB    . ASP A 1 340 ? 109.404 125.422 79.858  1.00 118.63 ? 2131 ASP A CB    1 
ATOM   2115 C  CG    . ASP A 1 340 ? 108.060 125.595 80.535  1.00 123.69 ? 2131 ASP A CG    1 
ATOM   2116 O  OD1   . ASP A 1 340 ? 107.347 124.586 80.715  1.00 123.40 ? 2131 ASP A OD1   1 
ATOM   2117 O  OD2   . ASP A 1 340 ? 107.715 126.743 80.888  1.00 124.67 ? 2131 ASP A OD2   1 
ATOM   2118 N  N     . ASP A 1 341 ? 112.090 123.963 79.035  1.00 115.72 ? 2132 ASP A N     1 
ATOM   2119 C  CA    . ASP A 1 341 ? 113.266 123.868 78.176  1.00 113.68 ? 2132 ASP A CA    1 
ATOM   2120 C  C     . ASP A 1 341 ? 113.347 122.508 77.496  1.00 115.26 ? 2132 ASP A C     1 
ATOM   2121 O  O     . ASP A 1 341 ? 113.667 122.419 76.303  1.00 117.87 ? 2132 ASP A O     1 
ATOM   2122 C  CB    . ASP A 1 341 ? 114.533 124.137 78.988  1.00 112.03 ? 2132 ASP A CB    1 
ATOM   2123 C  CG    . ASP A 1 341 ? 114.751 125.613 79.254  1.00 116.45 ? 2132 ASP A CG    1 
ATOM   2124 O  OD1   . ASP A 1 341 ? 113.869 126.243 79.875  1.00 120.25 ? 2132 ASP A OD1   1 
ATOM   2125 O  OD2   . ASP A 1 341 ? 115.804 126.143 78.843  1.00 113.00 ? 2132 ASP A OD2   1 
ATOM   2126 N  N     . ILE A 1 342 ? 113.063 121.435 78.239  1.00 115.63 ? 2133 ILE A N     1 
ATOM   2127 C  CA    . ILE A 1 342 ? 113.104 120.096 77.657  1.00 114.28 ? 2133 ILE A CA    1 
ATOM   2128 C  C     . ILE A 1 342 ? 112.057 119.968 76.559  1.00 116.50 ? 2133 ILE A C     1 
ATOM   2129 O  O     . ILE A 1 342 ? 112.332 119.443 75.472  1.00 117.98 ? 2133 ILE A O     1 
ATOM   2130 C  CB    . ILE A 1 342 ? 112.901 119.030 78.750  1.00 111.81 ? 2133 ILE A CB    1 
ATOM   2131 C  CG1   . ILE A 1 342 ? 114.157 118.872 79.607  1.00 109.32 ? 2133 ILE A CG1   1 
ATOM   2132 C  CG2   . ILE A 1 342 ? 112.591 117.692 78.116  1.00 107.07 ? 2133 ILE A CG2   1 
ATOM   2133 C  CD1   . ILE A 1 342 ? 115.440 119.063 78.860  1.00 104.88 ? 2133 ILE A CD1   1 
ATOM   2134 N  N     . ALA A 1 343 ? 110.841 120.451 76.824  1.00 117.24 ? 2134 ALA A N     1 
ATOM   2135 C  CA    . ALA A 1 343 ? 109.782 120.378 75.823  1.00 119.74 ? 2134 ALA A CA    1 
ATOM   2136 C  C     . ALA A 1 343 ? 110.139 121.186 74.583  1.00 122.06 ? 2134 ALA A C     1 
ATOM   2137 O  O     . ALA A 1 343 ? 109.884 120.750 73.454  1.00 121.66 ? 2134 ALA A O     1 
ATOM   2138 C  CB    . ALA A 1 343 ? 108.461 120.862 76.419  1.00 118.86 ? 2134 ALA A CB    1 
ATOM   2139 N  N     . GLU A 1 344 ? 110.729 122.368 74.772  1.00 123.27 ? 2135 GLU A N     1 
ATOM   2140 C  CA    . GLU A 1 344 ? 111.124 123.191 73.634  1.00 123.13 ? 2135 GLU A CA    1 
ATOM   2141 C  C     . GLU A 1 344 ? 112.201 122.503 72.805  1.00 121.85 ? 2135 GLU A C     1 
ATOM   2142 O  O     . GLU A 1 344 ? 112.132 122.482 71.572  1.00 123.26 ? 2135 GLU A O     1 
ATOM   2143 C  CB    . GLU A 1 344 ? 111.604 124.559 74.118  1.00 120.65 ? 2135 GLU A CB    1 
ATOM   2144 C  CG    . GLU A 1 344 ? 110.485 125.487 74.563  1.00 120.31 ? 2135 GLU A CG    1 
ATOM   2145 C  CD    . GLU A 1 344 ? 111.002 126.789 75.140  1.00 122.76 ? 2135 GLU A CD    1 
ATOM   2146 O  OE1   . GLU A 1 344 ? 112.236 126.980 75.171  1.00 122.65 ? 2135 GLU A OE1   1 
ATOM   2147 O  OE2   . GLU A 1 344 ? 110.174 127.623 75.564  1.00 125.64 ? 2135 GLU A OE2   1 
ATOM   2148 N  N     . VAL A 1 345 ? 113.206 121.923 73.468  1.00 120.10 ? 2136 VAL A N     1 
ATOM   2149 C  CA    . VAL A 1 345 ? 114.293 121.286 72.735  1.00 119.88 ? 2136 VAL A CA    1 
ATOM   2150 C  C     . VAL A 1 345 ? 113.860 119.964 72.113  1.00 120.19 ? 2136 VAL A C     1 
ATOM   2151 O  O     . VAL A 1 345 ? 114.516 119.478 71.184  1.00 120.25 ? 2136 VAL A O     1 
ATOM   2152 C  CB    . VAL A 1 345 ? 115.520 121.089 73.648  1.00 116.80 ? 2136 VAL A CB    1 
ATOM   2153 C  CG1   . VAL A 1 345 ? 115.334 119.884 74.553  1.00 115.66 ? 2136 VAL A CG1   1 
ATOM   2154 C  CG2   . VAL A 1 345 ? 116.787 120.946 72.819  1.00 116.37 ? 2136 VAL A CG2   1 
ATOM   2155 N  N     . LEU A 1 346 ? 112.769 119.367 72.590  1.00 119.47 ? 2137 LEU A N     1 
ATOM   2156 C  CA    . LEU A 1 346 ? 112.324 118.088 72.045  1.00 120.29 ? 2137 LEU A CA    1 
ATOM   2157 C  C     . LEU A 1 346 ? 111.286 118.252 70.937  1.00 123.62 ? 2137 LEU A C     1 
ATOM   2158 O  O     . LEU A 1 346 ? 111.507 117.817 69.803  1.00 125.66 ? 2137 LEU A O     1 
ATOM   2159 C  CB    . LEU A 1 346 ? 111.763 117.208 73.168  1.00 119.62 ? 2137 LEU A CB    1 
ATOM   2160 C  CG    . LEU A 1 346 ? 112.616 116.007 73.574  1.00 113.81 ? 2137 LEU A CG    1 
ATOM   2161 C  CD1   . LEU A 1 346 ? 113.903 116.471 74.227  1.00 112.39 ? 2137 LEU A CD1   1 
ATOM   2162 C  CD2   . LEU A 1 346 ? 111.839 115.092 74.502  1.00 105.79 ? 2137 LEU A CD2   1 
ATOM   2163 N  N     . PHE A 1 347 ? 110.156 118.886 71.248  1.00 124.01 ? 2138 PHE A N     1 
ATOM   2164 C  CA    . PHE A 1 347 ? 108.985 118.813 70.383  1.00 125.88 ? 2138 PHE A CA    1 
ATOM   2165 C  C     . PHE A 1 347 ? 108.941 119.919 69.332  1.00 126.90 ? 2138 PHE A C     1 
ATOM   2166 O  O     . PHE A 1 347 ? 108.753 119.639 68.145  1.00 126.78 ? 2138 PHE A O     1 
ATOM   2167 C  CB    . PHE A 1 347 ? 107.716 118.841 71.239  1.00 125.88 ? 2138 PHE A CB    1 
ATOM   2168 C  CG    . PHE A 1 347 ? 107.733 117.856 72.373  1.00 125.41 ? 2138 PHE A CG    1 
ATOM   2169 C  CD1   . PHE A 1 347 ? 107.594 116.500 72.133  1.00 124.08 ? 2138 PHE A CD1   1 
ATOM   2170 C  CD2   . PHE A 1 347 ? 107.900 118.285 73.679  1.00 122.74 ? 2138 PHE A CD2   1 
ATOM   2171 C  CE1   . PHE A 1 347 ? 107.614 115.590 73.173  1.00 121.59 ? 2138 PHE A CE1   1 
ATOM   2172 C  CE2   . PHE A 1 347 ? 107.922 117.381 74.723  1.00 119.89 ? 2138 PHE A CE2   1 
ATOM   2173 C  CZ    . PHE A 1 347 ? 107.778 116.032 74.470  1.00 119.99 ? 2138 PHE A CZ    1 
ATOM   2174 N  N     . LEU A 1 348 ? 109.101 121.174 69.741  1.00 126.70 ? 2139 LEU A N     1 
ATOM   2175 C  CA    . LEU A 1 348 ? 108.949 122.292 68.818  1.00 127.93 ? 2139 LEU A CA    1 
ATOM   2176 C  C     . LEU A 1 348 ? 110.255 122.713 68.156  1.00 126.65 ? 2139 LEU A C     1 
ATOM   2177 O  O     . LEU A 1 348 ? 110.262 123.704 67.418  1.00 127.98 ? 2139 LEU A O     1 
ATOM   2178 C  CB    . LEU A 1 348 ? 108.323 123.492 69.537  1.00 128.17 ? 2139 LEU A CB    1 
ATOM   2179 C  CG    . LEU A 1 348 ? 109.032 124.028 70.781  1.00 126.29 ? 2139 LEU A CG    1 
ATOM   2180 C  CD1   . LEU A 1 348 ? 109.773 125.318 70.468  1.00 122.40 ? 2139 LEU A CD1   1 
ATOM   2181 C  CD2   . LEU A 1 348 ? 108.035 124.240 71.909  1.00 124.44 ? 2139 LEU A CD2   1 
ATOM   2182 N  N     . GLU A 1 349 ? 111.347 122.002 68.394  1.00 124.27 ? 2140 GLU A N     1 
ATOM   2183 C  CA    . GLU A 1 349 ? 112.615 122.373 67.773  1.00 123.62 ? 2140 GLU A CA    1 
ATOM   2184 C  C     . GLU A 1 349 ? 113.282 121.226 67.029  1.00 124.12 ? 2140 GLU A C     1 
ATOM   2185 O  O     . GLU A 1 349 ? 113.874 121.452 65.970  1.00 125.67 ? 2140 GLU A O     1 
ATOM   2186 C  CB    . GLU A 1 349 ? 113.574 122.937 68.841  1.00 121.03 ? 2140 GLU A CB    1 
ATOM   2187 C  CG    . GLU A 1 349 ? 115.026 122.513 68.685  1.00 121.44 ? 2140 GLU A CG    1 
ATOM   2188 C  CD    . GLU A 1 349 ? 115.931 123.143 69.724  1.00 121.23 ? 2140 GLU A CD    1 
ATOM   2189 O  OE1   . GLU A 1 349 ? 115.531 124.165 70.322  1.00 121.26 ? 2140 GLU A OE1   1 
ATOM   2190 O  OE2   . GLU A 1 349 ? 117.042 122.619 69.944  1.00 121.80 ? 2140 GLU A OE2   1 
ATOM   2191 N  N     . LEU A 1 350 ? 113.188 120.001 67.539  1.00 122.97 ? 2141 LEU A N     1 
ATOM   2192 C  CA    . LEU A 1 350 ? 113.912 118.858 66.988  1.00 123.34 ? 2141 LEU A CA    1 
ATOM   2193 C  C     . LEU A 1 350 ? 112.931 117.723 66.680  1.00 124.38 ? 2141 LEU A C     1 
ATOM   2194 O  O     . LEU A 1 350 ? 113.124 116.563 67.047  1.00 125.14 ? 2141 LEU A O     1 
ATOM   2195 C  CB    . LEU A 1 350 ? 115.039 118.471 67.956  1.00 123.46 ? 2141 LEU A CB    1 
ATOM   2196 C  CG    . LEU A 1 350 ? 115.803 117.142 67.986  1.00 122.91 ? 2141 LEU A CG    1 
ATOM   2197 C  CD1   . LEU A 1 350 ? 116.439 116.855 66.635  1.00 121.83 ? 2141 LEU A CD1   1 
ATOM   2198 C  CD2   . LEU A 1 350 ? 116.852 117.151 69.086  1.00 120.64 ? 2141 LEU A CD2   1 
ATOM   2199 N  N     . LYS A 1 351 ? 111.842 118.071 65.992  1.00 124.32 ? 2142 LYS A N     1 
ATOM   2200 C  CA    . LYS A 1 351 ? 110.808 117.121 65.562  1.00 125.98 ? 2142 LYS A CA    1 
ATOM   2201 C  C     . LYS A 1 351 ? 110.269 116.420 66.803  1.00 127.02 ? 2142 LYS A C     1 
ATOM   2202 O  O     . LYS A 1 351 ? 109.681 117.106 67.657  1.00 126.54 ? 2142 LYS A O     1 
ATOM   2203 C  CB    . LYS A 1 351 ? 111.385 116.211 64.474  1.00 123.79 ? 2142 LYS A CB    1 
ATOM   2204 C  CG    . LYS A 1 351 ? 112.151 116.951 63.386  1.00 124.59 ? 2142 LYS A CG    1 
ATOM   2205 C  CD    . LYS A 1 351 ? 111.286 118.012 62.720  1.00 123.43 ? 2142 LYS A CD    1 
ATOM   2206 C  CE    . LYS A 1 351 ? 110.315 117.393 61.727  1.00 122.27 ? 2142 LYS A CE    1 
ATOM   2207 N  NZ    . LYS A 1 351 ? 111.022 116.789 60.564  1.00 119.98 ? 2142 LYS A NZ    1 
ATOM   2208 N  N     . LEU A 1 352 ? 110.443 115.100 66.959  1.00 127.51 ? 2143 LEU A N     1 
ATOM   2209 C  CA    . LEU A 1 352 ? 109.977 114.364 68.131  1.00 124.99 ? 2143 LEU A CA    1 
ATOM   2210 C  C     . LEU A 1 352 ? 108.496 114.623 68.381  1.00 125.89 ? 2143 LEU A C     1 
ATOM   2211 O  O     . LEU A 1 352 ? 108.148 115.386 69.291  1.00 124.76 ? 2143 LEU A O     1 
ATOM   2212 C  CB    . LEU A 1 352 ? 110.800 114.739 69.367  1.00 122.45 ? 2143 LEU A CB    1 
ATOM   2213 C  CG    . LEU A 1 352 ? 111.996 113.854 69.728  1.00 118.52 ? 2143 LEU A CG    1 
ATOM   2214 C  CD1   . LEU A 1 352 ? 111.531 112.476 70.160  1.00 113.53 ? 2143 LEU A CD1   1 
ATOM   2215 C  CD2   . LEU A 1 352 ? 112.970 113.745 68.568  1.00 115.99 ? 2143 LEU A CD2   1 
ATOM   2216 N  N     . PRO A 1 353 ? 107.605 114.033 67.586  1.00 127.95 ? 2144 PRO A N     1 
ATOM   2217 C  CA    . PRO A 1 353 ? 106.170 114.343 67.699  1.00 129.73 ? 2144 PRO A CA    1 
ATOM   2218 C  C     . PRO A 1 353 ? 105.662 114.103 69.108  1.00 128.22 ? 2144 PRO A C     1 
ATOM   2219 O  O     . PRO A 1 353 ? 106.069 113.137 69.772  1.00 124.78 ? 2144 PRO A O     1 
ATOM   2220 C  CB    . PRO A 1 353 ? 105.520 113.373 66.700  1.00 127.69 ? 2144 PRO A CB    1 
ATOM   2221 C  CG    . PRO A 1 353 ? 106.609 113.036 65.735  1.00 125.68 ? 2144 PRO A CG    1 
ATOM   2222 C  CD    . PRO A 1 353 ? 107.877 113.038 66.535  1.00 124.90 ? 2144 PRO A CD    1 
ATOM   2223 N  N     . PRO A 1 354 ? 104.769 114.964 69.602  1.00 128.27 ? 2145 PRO A N     1 
ATOM   2224 C  CA    . PRO A 1 354 ? 104.374 114.896 71.015  1.00 126.14 ? 2145 PRO A CA    1 
ATOM   2225 C  C     . PRO A 1 354 ? 103.463 113.722 71.335  1.00 123.92 ? 2145 PRO A C     1 
ATOM   2226 O  O     . PRO A 1 354 ? 103.177 112.883 70.475  1.00 121.68 ? 2145 PRO A O     1 
ATOM   2227 C  CB    . PRO A 1 354 ? 103.657 116.232 71.237  1.00 125.50 ? 2145 PRO A CB    1 
ATOM   2228 C  CG    . PRO A 1 354 ? 103.097 116.571 69.897  1.00 124.79 ? 2145 PRO A CG    1 
ATOM   2229 C  CD    . PRO A 1 354 ? 104.089 116.057 68.885  1.00 126.86 ? 2145 PRO A CD    1 
ATOM   2230 N  N     . ASN A 1 355 ? 103.003 113.663 72.581  1.00 123.77 ? 2146 ASN A N     1 
ATOM   2231 C  CA    . ASN A 1 355 ? 102.150 112.581 73.051  1.00 123.08 ? 2146 ASN A CA    1 
ATOM   2232 C  C     . ASN A 1 355 ? 100.707 112.834 72.618  1.00 123.31 ? 2146 ASN A C     1 
ATOM   2233 O  O     . ASN A 1 355 ? 100.418 113.718 71.807  1.00 123.72 ? 2146 ASN A O     1 
ATOM   2234 C  CB    . ASN A 1 355 ? 102.276 112.437 74.565  1.00 118.21 ? 2146 ASN A CB    1 
ATOM   2235 C  CG    . ASN A 1 355 ? 102.276 113.776 75.278  1.00 116.70 ? 2146 ASN A CG    1 
ATOM   2236 O  OD1   . ASN A 1 355 ? 101.499 114.671 74.947  1.00 117.32 ? 2146 ASN A OD1   1 
ATOM   2237 N  ND2   . ASN A 1 355 ? 103.156 113.922 76.262  1.00 112.88 ? 2146 ASN A ND2   1 
ATOM   2238 N  N     . ARG A 1 356 ? 99.780  112.051 73.160  1.00 121.84 ? 2147 ARG A N     1 
ATOM   2239 C  CA    . ARG A 1 356 ? 98.365  112.199 72.842  1.00 119.97 ? 2147 ARG A CA    1 
ATOM   2240 C  C     . ARG A 1 356 ? 97.787  113.454 73.488  1.00 117.41 ? 2147 ARG A C     1 
ATOM   2241 O  O     . ARG A 1 356 ? 97.874  114.548 72.931  1.00 117.29 ? 2147 ARG A O     1 
ATOM   2242 C  CB    . ARG A 1 356 ? 97.582  110.965 73.296  1.00 116.56 ? 2147 ARG A CB    1 
ATOM   2243 N  N     . GLY A 1 383 ? 105.344 127.548 79.202  1.00 120.00 ? 2174 GLY A N     1 
ATOM   2244 C  CA    . GLY A 1 383 ? 104.722 126.812 78.117  1.00 122.26 ? 2174 GLY A CA    1 
ATOM   2245 C  C     . GLY A 1 383 ? 103.832 125.681 78.594  1.00 125.12 ? 2174 GLY A C     1 
ATOM   2246 O  O     . GLY A 1 383 ? 102.616 125.842 78.701  1.00 126.79 ? 2174 GLY A O     1 
ATOM   2247 N  N     . ARG A 1 384 ? 104.448 124.530 78.869  1.00 126.08 ? 2175 ARG A N     1 
ATOM   2248 C  CA    . ARG A 1 384 ? 103.765 123.340 79.377  1.00 125.35 ? 2175 ARG A CA    1 
ATOM   2249 C  C     . ARG A 1 384 ? 102.692 122.829 78.421  1.00 124.65 ? 2175 ARG A C     1 
ATOM   2250 O  O     . ARG A 1 384 ? 101.729 122.186 78.853  1.00 121.89 ? 2175 ARG A O     1 
ATOM   2251 C  CB    . ARG A 1 384 ? 103.156 123.596 80.761  1.00 124.13 ? 2175 ARG A CB    1 
ATOM   2252 C  CG    . ARG A 1 384 ? 104.180 123.746 81.873  1.00 125.59 ? 2175 ARG A CG    1 
ATOM   2253 C  CD    . ARG A 1 384 ? 103.539 124.303 83.133  1.00 132.57 ? 2175 ARG A CD    1 
ATOM   2254 N  NE    . ARG A 1 384 ? 102.473 123.440 83.627  1.00 133.42 ? 2175 ARG A NE    1 
ATOM   2255 C  CZ    . ARG A 1 384 ? 101.983 123.485 84.858  1.00 133.86 ? 2175 ARG A CZ    1 
ATOM   2256 N  NH1   . ARG A 1 384 ? 102.443 124.342 85.755  1.00 138.78 ? 2175 ARG A NH1   1 
ATOM   2257 N  NH2   . ARG A 1 384 ? 101.006 122.649 85.198  1.00 127.00 ? 2175 ARG A NH2   1 
ATOM   2258 N  N     . GLN A 1 385 ? 102.835 123.106 77.123  1.00 125.21 ? 2176 GLN A N     1 
ATOM   2259 C  CA    . GLN A 1 385 ? 101.859 122.618 76.153  1.00 124.68 ? 2176 GLN A CA    1 
ATOM   2260 C  C     . GLN A 1 385 ? 101.913 121.099 76.026  1.00 122.60 ? 2176 GLN A C     1 
ATOM   2261 O  O     . GLN A 1 385 ? 100.871 120.445 75.903  1.00 120.78 ? 2176 GLN A O     1 
ATOM   2262 C  CB    . GLN A 1 385 ? 102.084 123.283 74.794  1.00 125.14 ? 2176 GLN A CB    1 
ATOM   2263 C  CG    . GLN A 1 385 ? 103.536 123.350 74.350  1.00 123.62 ? 2176 GLN A CG    1 
ATOM   2264 C  CD    . GLN A 1 385 ? 104.244 124.594 74.852  1.00 124.53 ? 2176 GLN A CD    1 
ATOM   2265 O  OE1   . GLN A 1 385 ? 103.610 125.524 75.349  1.00 124.45 ? 2176 GLN A OE1   1 
ATOM   2266 N  NE2   . GLN A 1 385 ? 105.566 124.615 74.725  1.00 124.95 ? 2176 GLN A NE2   1 
ATOM   2267 N  N     . PHE A 1 386 ? 103.111 120.522 76.054  1.00 122.15 ? 2177 PHE A N     1 
ATOM   2268 C  CA    . PHE A 1 386 ? 103.293 119.082 75.943  1.00 120.59 ? 2177 PHE A CA    1 
ATOM   2269 C  C     . PHE A 1 386 ? 103.829 118.520 77.252  1.00 118.16 ? 2177 PHE A C     1 
ATOM   2270 O  O     . PHE A 1 386 ? 104.752 119.083 77.850  1.00 117.45 ? 2177 PHE A O     1 
ATOM   2271 C  CB    . PHE A 1 386 ? 104.246 118.728 74.797  1.00 119.67 ? 2177 PHE A CB    1 
ATOM   2272 C  CG    . PHE A 1 386 ? 104.098 119.608 73.588  1.00 121.52 ? 2177 PHE A CG    1 
ATOM   2273 C  CD1   . PHE A 1 386 ? 102.905 119.647 72.885  1.00 121.47 ? 2177 PHE A CD1   1 
ATOM   2274 C  CD2   . PHE A 1 386 ? 105.156 120.384 73.146  1.00 122.14 ? 2177 PHE A CD2   1 
ATOM   2275 C  CE1   . PHE A 1 386 ? 102.767 120.452 71.770  1.00 120.71 ? 2177 PHE A CE1   1 
ATOM   2276 C  CE2   . PHE A 1 386 ? 105.025 121.189 72.030  1.00 122.59 ? 2177 PHE A CE2   1 
ATOM   2277 C  CZ    . PHE A 1 386 ? 103.829 121.224 71.342  1.00 121.02 ? 2177 PHE A CZ    1 
ATOM   2278 N  N     . SER A 1 387 ? 103.243 117.410 77.693  1.00 116.03 ? 2178 SER A N     1 
ATOM   2279 C  CA    . SER A 1 387 ? 103.684 116.759 78.917  1.00 109.94 ? 2178 SER A CA    1 
ATOM   2280 C  C     . SER A 1 387 ? 105.089 116.191 78.749  1.00 108.31 ? 2178 SER A C     1 
ATOM   2281 O  O     . SER A 1 387 ? 105.481 115.750 77.666  1.00 110.79 ? 2178 SER A O     1 
ATOM   2282 C  CB    . SER A 1 387 ? 102.713 115.645 79.309  1.00 107.60 ? 2178 SER A CB    1 
ATOM   2283 O  OG    . SER A 1 387 ? 103.192 114.920 80.428  1.00 102.50 ? 2178 SER A OG    1 
ATOM   2284 N  N     . THR A 1 388 ? 105.850 116.207 79.840  1.00 105.90 ? 2179 THR A N     1 
ATOM   2285 C  CA    . THR A 1 388 ? 107.232 115.745 79.841  1.00 101.33 ? 2179 THR A CA    1 
ATOM   2286 C  C     . THR A 1 388 ? 107.495 114.839 81.037  1.00 94.96  ? 2179 THR A C     1 
ATOM   2287 O  O     . THR A 1 388 ? 108.477 115.002 81.768  1.00 88.55  ? 2179 THR A O     1 
ATOM   2288 C  CB    . THR A 1 388 ? 108.200 116.926 79.826  1.00 98.01  ? 2179 THR A CB    1 
ATOM   2289 O  OG1   . THR A 1 388 ? 107.706 117.933 78.936  1.00 100.46 ? 2179 THR A OG1   1 
ATOM   2290 C  CG2   . THR A 1 388 ? 109.562 116.478 79.334  1.00 95.00  ? 2179 THR A CG2   1 
ATOM   2291 N  N     . SER A 1 389 ? 106.609 113.875 81.266  1.00 93.18  ? 2180 SER A N     1 
ATOM   2292 C  CA    . SER A 1 389 ? 106.804 112.927 82.350  1.00 87.24  ? 2180 SER A CA    1 
ATOM   2293 C  C     . SER A 1 389 ? 107.789 111.840 81.920  1.00 84.59  ? 2180 SER A C     1 
ATOM   2294 O  O     . SER A 1 389 ? 108.295 111.826 80.795  1.00 86.83  ? 2180 SER A O     1 
ATOM   2295 C  CB    . SER A 1 389 ? 105.468 112.321 82.772  1.00 89.49  ? 2180 SER A CB    1 
ATOM   2296 O  OG    . SER A 1 389 ? 104.881 111.590 81.711  1.00 87.37  ? 2180 SER A OG    1 
ATOM   2297 N  N     . LYS A 1 390 ? 108.069 110.917 82.842  1.00 82.76  ? 2181 LYS A N     1 
ATOM   2298 C  CA    . LYS A 1 390 ? 108.949 109.799 82.523  1.00 80.76  ? 2181 LYS A CA    1 
ATOM   2299 C  C     . LYS A 1 390 ? 108.331 108.903 81.458  1.00 86.23  ? 2181 LYS A C     1 
ATOM   2300 O  O     . LYS A 1 390 ? 109.036 108.380 80.587  1.00 87.73  ? 2181 LYS A O     1 
ATOM   2301 C  CB    . LYS A 1 390 ? 109.261 109.000 83.789  1.00 76.83  ? 2181 LYS A CB    1 
ATOM   2302 C  CG    . LYS A 1 390 ? 109.972 107.682 83.542  1.00 79.34  ? 2181 LYS A CG    1 
ATOM   2303 C  CD    . LYS A 1 390 ? 110.810 107.272 84.742  1.00 72.85  ? 2181 LYS A CD    1 
ATOM   2304 C  CE    . LYS A 1 390 ? 112.016 106.452 84.316  1.00 66.62  ? 2181 LYS A CE    1 
ATOM   2305 N  NZ    . LYS A 1 390 ? 112.313 105.356 85.278  1.00 62.13  ? 2181 LYS A NZ    1 
ATOM   2306 N  N     . ASP A 1 391 ? 107.009 108.721 81.508  1.00 88.66  ? 2182 ASP A N     1 
ATOM   2307 C  CA    . ASP A 1 391 ? 106.336 107.866 80.536  1.00 90.94  ? 2182 ASP A CA    1 
ATOM   2308 C  C     . ASP A 1 391 ? 106.444 108.433 79.125  1.00 92.60  ? 2182 ASP A C     1 
ATOM   2309 O  O     . ASP A 1 391 ? 106.560 107.675 78.155  1.00 92.29  ? 2182 ASP A O     1 
ATOM   2310 C  CB    . ASP A 1 391 ? 104.871 107.677 80.934  1.00 90.30  ? 2182 ASP A CB    1 
ATOM   2311 C  CG    . ASP A 1 391 ? 104.023 107.130 79.801  1.00 91.80  ? 2182 ASP A CG    1 
ATOM   2312 O  OD1   . ASP A 1 391 ? 103.450 107.937 79.039  1.00 90.94  ? 2182 ASP A OD1   1 
ATOM   2313 O  OD2   . ASP A 1 391 ? 103.929 105.891 79.671  1.00 88.91  ? 2182 ASP A OD2   1 
ATOM   2314 N  N     . VAL A 1 392 ? 106.412 109.761 78.988  1.00 92.97  ? 2183 VAL A N     1 
ATOM   2315 C  CA    . VAL A 1 392 ? 106.499 110.374 77.664  1.00 91.70  ? 2183 VAL A CA    1 
ATOM   2316 C  C     . VAL A 1 392 ? 107.839 110.051 77.015  1.00 91.79  ? 2183 VAL A C     1 
ATOM   2317 O  O     . VAL A 1 392 ? 107.901 109.584 75.871  1.00 94.97  ? 2183 VAL A O     1 
ATOM   2318 C  CB    . VAL A 1 392 ? 106.272 111.893 77.760  1.00 91.14  ? 2183 VAL A CB    1 
ATOM   2319 C  CG1   . VAL A 1 392 ? 106.324 112.525 76.379  1.00 92.43  ? 2183 VAL A CG1   1 
ATOM   2320 C  CG2   . VAL A 1 392 ? 104.946 112.186 78.442  1.00 96.10  ? 2183 VAL A CG2   1 
ATOM   2321 N  N     . LEU A 1 393 ? 108.933 110.282 77.742  1.00 88.33  ? 2184 LEU A N     1 
ATOM   2322 C  CA    . LEU A 1 393 ? 110.250 109.983 77.192  1.00 87.86  ? 2184 LEU A CA    1 
ATOM   2323 C  C     . LEU A 1 393 ? 110.460 108.485 77.026  1.00 90.63  ? 2184 LEU A C     1 
ATOM   2324 O  O     . LEU A 1 393 ? 111.187 108.060 76.121  1.00 93.39  ? 2184 LEU A O     1 
ATOM   2325 C  CB    . LEU A 1 393 ? 111.339 110.581 78.078  1.00 83.75  ? 2184 LEU A CB    1 
ATOM   2326 C  CG    . LEU A 1 393 ? 111.121 112.019 78.548  1.00 84.40  ? 2184 LEU A CG    1 
ATOM   2327 C  CD1   . LEU A 1 393 ? 112.264 112.455 79.442  1.00 80.03  ? 2184 LEU A CD1   1 
ATOM   2328 C  CD2   . LEU A 1 393 ? 110.978 112.955 77.362  1.00 86.98  ? 2184 LEU A CD2   1 
ATOM   2329 N  N     . ASN A 1 394 ? 109.844 107.671 77.888  1.00 91.37  ? 2185 ASN A N     1 
ATOM   2330 C  CA    . ASN A 1 394 ? 109.931 106.224 77.724  1.00 93.65  ? 2185 ASN A CA    1 
ATOM   2331 C  C     . ASN A 1 394 ? 109.267 105.782 76.427  1.00 93.68  ? 2185 ASN A C     1 
ATOM   2332 O  O     . ASN A 1 394 ? 109.782 104.905 75.723  1.00 94.07  ? 2185 ASN A O     1 
ATOM   2333 C  CB    . ASN A 1 394 ? 109.296 105.523 78.924  1.00 89.97  ? 2185 ASN A CB    1 
ATOM   2334 C  CG    . ASN A 1 394 ? 110.326 104.896 79.843  1.00 91.16  ? 2185 ASN A CG    1 
ATOM   2335 O  OD1   . ASN A 1 394 ? 111.411 104.513 79.408  1.00 95.15  ? 2185 ASN A OD1   1 
ATOM   2336 N  ND2   . ASN A 1 394 ? 109.990 104.791 81.123  1.00 89.07  ? 2185 ASN A ND2   1 
ATOM   2337 N  N     . LYS A 1 395 ? 108.114 106.370 76.100  1.00 92.24  ? 2186 LYS A N     1 
ATOM   2338 C  CA    . LYS A 1 395 ? 107.477 106.091 74.817  1.00 94.80  ? 2186 LYS A CA    1 
ATOM   2339 C  C     . LYS A 1 395 ? 108.332 106.591 73.660  1.00 95.33  ? 2186 LYS A C     1 
ATOM   2340 O  O     . LYS A 1 395 ? 108.466 105.907 72.639  1.00 96.05  ? 2186 LYS A O     1 
ATOM   2341 C  CB    . LYS A 1 395 ? 106.087 106.723 74.767  1.00 95.71  ? 2186 LYS A CB    1 
ATOM   2342 C  CG    . LYS A 1 395 ? 105.040 105.996 75.595  1.00 97.35  ? 2186 LYS A CG    1 
ATOM   2343 C  CD    . LYS A 1 395 ? 103.636 106.504 75.298  1.00 97.29  ? 2186 LYS A CD    1 
ATOM   2344 C  CE    . LYS A 1 395 ? 103.617 108.003 75.042  1.00 97.56  ? 2186 LYS A CE    1 
ATOM   2345 N  NZ    . LYS A 1 395 ? 103.916 108.784 76.272  1.00 96.73  ? 2186 LYS A NZ    1 
ATOM   2346 N  N     . LEU A 1 396 ? 108.917 107.780 73.799  1.00 94.36  ? 2187 LEU A N     1 
ATOM   2347 C  CA    . LEU A 1 396 ? 109.791 108.316 72.761  1.00 93.98  ? 2187 LEU A CA    1 
ATOM   2348 C  C     . LEU A 1 396 ? 111.208 107.775 72.906  1.00 93.99  ? 2187 LEU A C     1 
ATOM   2349 O  O     . LEU A 1 396 ? 112.168 108.548 72.980  1.00 94.28  ? 2187 LEU A O     1 
ATOM   2350 C  CB    . LEU A 1 396 ? 109.808 109.848 72.789  1.00 93.53  ? 2187 LEU A CB    1 
ATOM   2351 C  CG    . LEU A 1 396 ? 108.503 110.631 72.953  1.00 92.46  ? 2187 LEU A CG    1 
ATOM   2352 C  CD1   . LEU A 1 396 ? 108.708 112.079 72.542  1.00 97.75  ? 2187 LEU A CD1   1 
ATOM   2353 C  CD2   . LEU A 1 396 ? 107.377 110.013 72.137  1.00 93.72  ? 2187 LEU A CD2   1 
ATOM   2354 N  N     . LYS A 1 397 ? 111.349 106.451 72.945  1.00 95.50  ? 2188 LYS A N     1 
ATOM   2355 C  CA    . LYS A 1 397 ? 112.653 105.807 73.029  1.00 99.23  ? 2188 LYS A CA    1 
ATOM   2356 C  C     . LYS A 1 397 ? 113.101 105.164 71.727  1.00 103.03 ? 2188 LYS A C     1 
ATOM   2357 O  O     . LYS A 1 397 ? 114.306 105.030 71.504  1.00 102.49 ? 2188 LYS A O     1 
ATOM   2358 C  CB    . LYS A 1 397 ? 112.654 104.743 74.133  1.00 98.14  ? 2188 LYS A CB    1 
ATOM   2359 C  CG    . LYS A 1 397 ? 113.008 105.279 75.510  1.00 95.44  ? 2188 LYS A CG    1 
ATOM   2360 C  CD    . LYS A 1 397 ? 114.499 105.544 75.633  1.00 97.10  ? 2188 LYS A CD    1 
ATOM   2361 C  CE    . LYS A 1 397 ? 115.302 104.278 75.395  1.00 97.06  ? 2188 LYS A CE    1 
ATOM   2362 N  NZ    . LYS A 1 397 ? 114.899 103.186 76.323  1.00 99.82  ? 2188 LYS A NZ    1 
ATOM   2363 N  N     . ALA A 1 398 ? 112.164 104.760 70.865  1.00 104.48 ? 2189 ALA A N     1 
ATOM   2364 C  CA    . ALA A 1 398 ? 112.533 104.199 69.571  1.00 105.82 ? 2189 ALA A CA    1 
ATOM   2365 C  C     . ALA A 1 398 ? 113.140 105.243 68.644  1.00 107.12 ? 2189 ALA A C     1 
ATOM   2366 O  O     . ALA A 1 398 ? 113.813 104.878 67.674  1.00 108.29 ? 2189 ALA A O     1 
ATOM   2367 C  CB    . ALA A 1 398 ? 111.314 103.557 68.907  1.00 104.36 ? 2189 ALA A CB    1 
ATOM   2368 N  N     . LEU A 1 399 ? 112.917 106.524 68.919  1.00 104.06 ? 2190 LEU A N     1 
ATOM   2369 C  CA    . LEU A 1 399 ? 113.481 107.605 68.122  1.00 104.22 ? 2190 LEU A CA    1 
ATOM   2370 C  C     . LEU A 1 399 ? 114.912 107.876 68.586  1.00 105.44 ? 2190 LEU A C     1 
ATOM   2371 O  O     . LEU A 1 399 ? 115.515 107.083 69.315  1.00 108.41 ? 2190 LEU A O     1 
ATOM   2372 C  CB    . LEU A 1 399 ? 112.589 108.840 68.209  1.00 104.50 ? 2190 LEU A CB    1 
ATOM   2373 C  CG    . LEU A 1 399 ? 111.107 108.580 67.919  1.00 106.20 ? 2190 LEU A CG    1 
ATOM   2374 C  CD1   . LEU A 1 399 ? 110.303 109.868 67.967  1.00 109.24 ? 2190 LEU A CD1   1 
ATOM   2375 C  CD2   . LEU A 1 399 ? 110.937 107.891 66.573  1.00 107.35 ? 2190 LEU A CD2   1 
ATOM   2376 N  N     . HIS A 1 400 ? 115.479 109.000 68.152  1.00 105.38 ? 2191 HIS A N     1 
ATOM   2377 C  CA    . HIS A 1 400 ? 116.851 109.330 68.503  1.00 105.34 ? 2191 HIS A CA    1 
ATOM   2378 C  C     . HIS A 1 400 ? 116.983 109.482 70.021  1.00 105.41 ? 2191 HIS A C     1 
ATOM   2379 O  O     . HIS A 1 400 ? 116.052 109.941 70.690  1.00 104.76 ? 2191 HIS A O     1 
ATOM   2380 C  CB    . HIS A 1 400 ? 117.292 110.597 67.769  1.00 107.90 ? 2191 HIS A CB    1 
ATOM   2381 C  CG    . HIS A 1 400 ? 117.217 111.845 68.591  1.00 110.94 ? 2191 HIS A CG    1 
ATOM   2382 N  ND1   . HIS A 1 400 ? 116.023 112.399 68.996  1.00 110.72 ? 2191 HIS A ND1   1 
ATOM   2383 C  CD2   . HIS A 1 400 ? 118.190 112.666 69.051  1.00 110.12 ? 2191 HIS A CD2   1 
ATOM   2384 C  CE1   . HIS A 1 400 ? 116.263 113.499 69.688  1.00 109.71 ? 2191 HIS A CE1   1 
ATOM   2385 N  NE2   . HIS A 1 400 ? 117.570 113.685 69.732  1.00 108.26 ? 2191 HIS A NE2   1 
ATOM   2386 N  N     . PRO A 1 401 ? 118.123 109.092 70.590  1.00 106.10 ? 2192 PRO A N     1 
ATOM   2387 C  CA    . PRO A 1 401 ? 118.177 108.726 72.012  1.00 105.04 ? 2192 PRO A CA    1 
ATOM   2388 C  C     . PRO A 1 401 ? 118.268 109.884 72.994  1.00 101.32 ? 2192 PRO A C     1 
ATOM   2389 O  O     . PRO A 1 401 ? 118.631 109.647 74.150  1.00 97.55  ? 2192 PRO A O     1 
ATOM   2390 C  CB    . PRO A 1 401 ? 119.448 107.866 72.081  1.00 105.55 ? 2192 PRO A CB    1 
ATOM   2391 C  CG    . PRO A 1 401 ? 120.327 108.446 71.038  1.00 106.37 ? 2192 PRO A CG    1 
ATOM   2392 C  CD    . PRO A 1 401 ? 119.415 108.863 69.916  1.00 106.51 ? 2192 PRO A CD    1 
ATOM   2393 N  N     . LEU A 1 402 ? 117.975 111.122 72.599  1.00 102.86 ? 2193 LEU A N     1 
ATOM   2394 C  CA    . LEU A 1 402 ? 117.973 112.208 73.576  1.00 98.98  ? 2193 LEU A CA    1 
ATOM   2395 C  C     . LEU A 1 402 ? 116.967 111.999 74.706  1.00 94.94  ? 2193 LEU A C     1 
ATOM   2396 O  O     . LEU A 1 402 ? 117.324 112.276 75.865  1.00 91.69  ? 2193 LEU A O     1 
ATOM   2397 C  CB    . LEU A 1 402 ? 117.735 113.551 72.875  1.00 102.04 ? 2193 LEU A CB    1 
ATOM   2398 C  CG    . LEU A 1 402 ? 117.727 114.790 73.773  1.00 102.51 ? 2193 LEU A CG    1 
ATOM   2399 C  CD1   . LEU A 1 402 ? 119.076 114.967 74.454  1.00 100.66 ? 2193 LEU A CD1   1 
ATOM   2400 C  CD2   . LEU A 1 402 ? 117.363 116.029 72.973  1.00 110.13 ? 2193 LEU A CD2   1 
ATOM   2401 N  N     . PRO A 1 403 ? 115.723 111.558 74.463  1.00 96.06  ? 2194 PRO A N     1 
ATOM   2402 C  CA    . PRO A 1 403 ? 114.838 111.260 75.603  1.00 94.07  ? 2194 PRO A CA    1 
ATOM   2403 C  C     . PRO A 1 403 ? 115.398 110.211 76.549  1.00 88.65  ? 2194 PRO A C     1 
ATOM   2404 O  O     . PRO A 1 403 ? 115.184 110.309 77.762  1.00 87.56  ? 2194 PRO A O     1 
ATOM   2405 C  CB    . PRO A 1 403 ? 113.548 110.786 74.923  1.00 94.41  ? 2194 PRO A CB    1 
ATOM   2406 C  CG    . PRO A 1 403 ? 113.548 111.487 73.623  1.00 95.12  ? 2194 PRO A CG    1 
ATOM   2407 C  CD    . PRO A 1 403 ? 114.984 111.507 73.188  1.00 98.31  ? 2194 PRO A CD    1 
ATOM   2408 N  N     . GLY A 1 404 ? 116.107 109.206 76.034  1.00 89.49  ? 2195 GLY A N     1 
ATOM   2409 C  CA    . GLY A 1 404 ? 116.758 108.254 76.920  1.00 86.70  ? 2195 GLY A CA    1 
ATOM   2410 C  C     . GLY A 1 404 ? 117.828 108.903 77.776  1.00 80.84  ? 2195 GLY A C     1 
ATOM   2411 O  O     . GLY A 1 404 ? 117.964 108.594 78.965  1.00 78.95  ? 2195 GLY A O     1 
ATOM   2412 N  N     . LEU A 1 405 ? 118.602 109.814 77.182  1.00 83.85  ? 2196 LEU A N     1 
ATOM   2413 C  CA    . LEU A 1 405 ? 119.596 110.559 77.946  1.00 84.15  ? 2196 LEU A CA    1 
ATOM   2414 C  C     . LEU A 1 405 ? 118.935 111.387 79.039  1.00 80.70  ? 2196 LEU A C     1 
ATOM   2415 O  O     . LEU A 1 405 ? 119.434 111.455 80.168  1.00 75.59  ? 2196 LEU A O     1 
ATOM   2416 C  CB    . LEU A 1 405 ? 120.408 111.456 77.011  1.00 88.32  ? 2196 LEU A CB    1 
ATOM   2417 C  CG    . LEU A 1 405 ? 121.727 110.921 76.451  1.00 87.53  ? 2196 LEU A CG    1 
ATOM   2418 C  CD1   . LEU A 1 405 ? 121.522 109.616 75.697  1.00 88.93  ? 2196 LEU A CD1   1 
ATOM   2419 C  CD2   . LEU A 1 405 ? 122.383 111.960 75.556  1.00 92.17  ? 2196 LEU A CD2   1 
ATOM   2420 N  N     . ILE A 1 406 ? 117.803 112.019 78.721  1.00 82.29  ? 2197 ILE A N     1 
ATOM   2421 C  CA    . ILE A 1 406 ? 117.101 112.829 79.711  1.00 79.11  ? 2197 ILE A CA    1 
ATOM   2422 C  C     . ILE A 1 406 ? 116.532 111.949 80.818  1.00 75.65  ? 2197 ILE A C     1 
ATOM   2423 O  O     . ILE A 1 406 ? 116.529 112.334 81.990  1.00 74.54  ? 2197 ILE A O     1 
ATOM   2424 C  CB    . ILE A 1 406 ? 116.008 113.675 79.035  1.00 81.34  ? 2197 ILE A CB    1 
ATOM   2425 C  CG1   . ILE A 1 406 ? 116.635 114.649 78.039  1.00 87.73  ? 2197 ILE A CG1   1 
ATOM   2426 C  CG2   . ILE A 1 406 ? 115.211 114.449 80.069  1.00 81.02  ? 2197 ILE A CG2   1 
ATOM   2427 C  CD1   . ILE A 1 406 ? 115.625 115.393 77.204  1.00 95.10  ? 2197 ILE A CD1   1 
ATOM   2428 N  N     . LEU A 1 407 ? 116.039 110.759 80.467  1.00 77.75  ? 2198 LEU A N     1 
ATOM   2429 C  CA    . LEU A 1 407 ? 115.540 109.837 81.483  1.00 71.21  ? 2198 LEU A CA    1 
ATOM   2430 C  C     . LEU A 1 407 ? 116.653 109.390 82.419  1.00 66.91  ? 2198 LEU A C     1 
ATOM   2431 O  O     . LEU A 1 407 ? 116.464 109.337 83.640  1.00 66.33  ? 2198 LEU A O     1 
ATOM   2432 C  CB    . LEU A 1 407 ? 114.887 108.625 80.822  1.00 75.20  ? 2198 LEU A CB    1 
ATOM   2433 C  CG    . LEU A 1 407 ? 113.473 108.832 80.290  1.00 79.71  ? 2198 LEU A CG    1 
ATOM   2434 C  CD1   . LEU A 1 407 ? 112.996 107.602 79.534  1.00 84.52  ? 2198 LEU A CD1   1 
ATOM   2435 C  CD2   . LEU A 1 407 ? 112.526 109.176 81.424  1.00 76.93  ? 2198 LEU A CD2   1 
ATOM   2436 N  N     . GLU A 1 408 ? 117.819 109.051 81.864  1.00 68.94  ? 2199 GLU A N     1 
ATOM   2437 C  CA    . GLU A 1 408 ? 118.952 108.677 82.707  1.00 65.79  ? 2199 GLU A CA    1 
ATOM   2438 C  C     . GLU A 1 408 ? 119.375 109.838 83.597  1.00 68.27  ? 2199 GLU A C     1 
ATOM   2439 O  O     . GLU A 1 408 ? 119.660 109.649 84.788  1.00 68.51  ? 2199 GLU A O     1 
ATOM   2440 C  CB    . GLU A 1 408 ? 120.120 108.210 81.841  1.00 69.98  ? 2199 GLU A CB    1 
ATOM   2441 C  CG    . GLU A 1 408 ? 120.440 106.732 81.970  1.00 72.09  ? 2199 GLU A CG    1 
ATOM   2442 C  CD    . GLU A 1 408 ? 121.647 106.325 81.148  1.00 79.33  ? 2199 GLU A CD    1 
ATOM   2443 O  OE1   . GLU A 1 408 ? 122.226 107.198 80.468  1.00 79.46  ? 2199 GLU A OE1   1 
ATOM   2444 O  OE2   . GLU A 1 408 ? 122.017 105.133 81.181  1.00 81.18  ? 2199 GLU A OE2   1 
ATOM   2445 N  N     . TRP A 1 409 ? 119.416 111.050 83.036  1.00 70.71  ? 2200 TRP A N     1 
ATOM   2446 C  CA    . TRP A 1 409 ? 119.753 112.230 83.823  1.00 67.77  ? 2200 TRP A CA    1 
ATOM   2447 C  C     . TRP A 1 409 ? 118.769 112.424 84.966  1.00 64.35  ? 2200 TRP A C     1 
ATOM   2448 O  O     . TRP A 1 409 ? 119.172 112.685 86.104  1.00 66.03  ? 2200 TRP A O     1 
ATOM   2449 C  CB    . TRP A 1 409 ? 119.772 113.466 82.921  1.00 73.75  ? 2200 TRP A CB    1 
ATOM   2450 C  CG    . TRP A 1 409 ? 120.321 114.702 83.572  1.00 74.08  ? 2200 TRP A CG    1 
ATOM   2451 C  CD1   . TRP A 1 409 ? 121.571 115.223 83.409  1.00 78.19  ? 2200 TRP A CD1   1 
ATOM   2452 C  CD2   . TRP A 1 409 ? 119.637 115.578 84.478  1.00 70.17  ? 2200 TRP A CD2   1 
ATOM   2453 N  NE1   . TRP A 1 409 ? 121.712 116.361 84.164  1.00 76.99  ? 2200 TRP A NE1   1 
ATOM   2454 C  CE2   . TRP A 1 409 ? 120.538 116.602 84.828  1.00 72.57  ? 2200 TRP A CE2   1 
ATOM   2455 C  CE3   . TRP A 1 409 ? 118.352 115.596 85.028  1.00 70.06  ? 2200 TRP A CE3   1 
ATOM   2456 C  CZ2   . TRP A 1 409 ? 120.196 117.630 85.702  1.00 73.81  ? 2200 TRP A CZ2   1 
ATOM   2457 C  CZ3   . TRP A 1 409 ? 118.016 116.615 85.897  1.00 75.05  ? 2200 TRP A CZ3   1 
ATOM   2458 C  CH2   . TRP A 1 409 ? 118.933 117.618 86.225  1.00 75.85  ? 2200 TRP A CH2   1 
ATOM   2459 N  N     . ARG A 1 410 ? 117.473 112.300 84.680  1.00 63.12  ? 2201 ARG A N     1 
ATOM   2460 C  CA    . ARG A 1 410 ? 116.455 112.501 85.703  1.00 61.93  ? 2201 ARG A CA    1 
ATOM   2461 C  C     . ARG A 1 410 ? 116.547 111.442 86.791  1.00 63.00  ? 2201 ARG A C     1 
ATOM   2462 O  O     . ARG A 1 410 ? 116.435 111.760 87.979  1.00 63.09  ? 2201 ARG A O     1 
ATOM   2463 C  CB    . ARG A 1 410 ? 115.066 112.495 85.065  1.00 61.45  ? 2201 ARG A CB    1 
ATOM   2464 C  CG    . ARG A 1 410 ? 114.379 113.846 85.066  1.00 60.11  ? 2201 ARG A CG    1 
ATOM   2465 C  CD    . ARG A 1 410 ? 112.890 113.703 84.814  1.00 60.21  ? 2201 ARG A CD    1 
ATOM   2466 N  NE    . ARG A 1 410 ? 112.559 113.859 83.403  1.00 65.13  ? 2201 ARG A NE    1 
ATOM   2467 C  CZ    . ARG A 1 410 ? 112.339 115.024 82.812  1.00 74.05  ? 2201 ARG A CZ    1 
ATOM   2468 N  NH1   . ARG A 1 410 ? 112.408 116.163 83.481  1.00 76.32  ? 2201 ARG A NH1   1 
ATOM   2469 N  NH2   . ARG A 1 410 ? 112.043 115.048 81.516  1.00 80.46  ? 2201 ARG A NH2   1 
ATOM   2470 N  N     . ARG A 1 411 ? 116.749 110.178 86.409  1.00 61.32  ? 2202 ARG A N     1 
ATOM   2471 C  CA    . ARG A 1 411 ? 116.868 109.120 87.407  1.00 55.39  ? 2202 ARG A CA    1 
ATOM   2472 C  C     . ARG A 1 411 ? 118.084 109.337 88.295  1.00 55.79  ? 2202 ARG A C     1 
ATOM   2473 O  O     . ARG A 1 411 ? 117.996 109.210 89.523  1.00 60.61  ? 2202 ARG A O     1 
ATOM   2474 C  CB    . ARG A 1 411 ? 116.942 107.755 86.725  1.00 55.78  ? 2202 ARG A CB    1 
ATOM   2475 C  CG    . ARG A 1 411 ? 115.637 107.300 86.097  1.00 60.20  ? 2202 ARG A CG    1 
ATOM   2476 C  CD    . ARG A 1 411 ? 115.605 105.788 85.930  1.00 63.50  ? 2202 ARG A CD    1 
ATOM   2477 N  NE    . ARG A 1 411 ? 116.935 105.230 85.720  1.00 62.29  ? 2202 ARG A NE    1 
ATOM   2478 C  CZ    . ARG A 1 411 ? 117.413 104.854 84.542  1.00 64.89  ? 2202 ARG A CZ    1 
ATOM   2479 N  NH1   . ARG A 1 411 ? 116.692 104.960 83.438  1.00 65.36  ? 2202 ARG A NH1   1 
ATOM   2480 N  NH2   . ARG A 1 411 ? 118.645 104.357 84.469  1.00 65.28  ? 2202 ARG A NH2   1 
ATOM   2481 N  N     . ILE A 1 412 ? 119.226 109.684 87.698  1.00 54.40  ? 2203 ILE A N     1 
ATOM   2482 C  CA    . ILE A 1 412 ? 120.432 109.886 88.493  1.00 55.77  ? 2203 ILE A CA    1 
ATOM   2483 C  C     . ILE A 1 412 ? 120.274 111.098 89.405  1.00 59.02  ? 2203 ILE A C     1 
ATOM   2484 O  O     . ILE A 1 412 ? 120.675 111.067 90.573  1.00 59.26  ? 2203 ILE A O     1 
ATOM   2485 C  CB    . ILE A 1 412 ? 121.660 110.011 87.576  1.00 61.46  ? 2203 ILE A CB    1 
ATOM   2486 C  CG1   . ILE A 1 412 ? 122.171 108.625 87.192  1.00 58.85  ? 2203 ILE A CG1   1 
ATOM   2487 C  CG2   . ILE A 1 412 ? 122.771 110.775 88.271  1.00 67.15  ? 2203 ILE A CG2   1 
ATOM   2488 C  CD1   . ILE A 1 412 ? 122.916 108.601 85.885  1.00 65.83  ? 2203 ILE A CD1   1 
ATOM   2489 N  N     . THR A 1 413 ? 119.680 112.181 88.896  1.00 59.73  ? 2204 THR A N     1 
ATOM   2490 C  CA    . THR A 1 413 ? 119.459 113.356 89.730  1.00 56.70  ? 2204 THR A CA    1 
ATOM   2491 C  C     . THR A 1 413 ? 118.520 113.041 90.888  1.00 57.60  ? 2204 THR A C     1 
ATOM   2492 O  O     . THR A 1 413 ? 118.792 113.415 92.033  1.00 60.71  ? 2204 THR A O     1 
ATOM   2493 C  CB    . THR A 1 413 ? 118.904 114.505 88.889  1.00 59.36  ? 2204 THR A CB    1 
ATOM   2494 O  OG1   . THR A 1 413 ? 119.848 114.849 87.868  1.00 67.75  ? 2204 THR A OG1   1 
ATOM   2495 C  CG2   . THR A 1 413 ? 118.645 115.724 89.758  1.00 55.64  ? 2204 THR A CG2   1 
ATOM   2496 N  N     . ASN A 1 414 ? 117.418 112.339 90.613  1.00 54.13  ? 2205 ASN A N     1 
ATOM   2497 C  CA    . ASN A 1 414 ? 116.497 111.955 91.677  1.00 52.62  ? 2205 ASN A CA    1 
ATOM   2498 C  C     . ASN A 1 414 ? 117.197 111.098 92.720  1.00 52.17  ? 2205 ASN A C     1 
ATOM   2499 O  O     . ASN A 1 414 ? 116.958 111.247 93.923  1.00 53.35  ? 2205 ASN A O     1 
ATOM   2500 C  CB    . ASN A 1 414 ? 115.302 111.210 91.086  1.00 49.10  ? 2205 ASN A CB    1 
ATOM   2501 C  CG    . ASN A 1 414 ? 114.394 110.630 92.149  1.00 51.59  ? 2205 ASN A CG    1 
ATOM   2502 O  OD1   . ASN A 1 414 ? 114.210 111.215 93.214  1.00 53.05  ? 2205 ASN A OD1   1 
ATOM   2503 N  ND2   . ASN A 1 414 ? 113.833 109.462 91.870  1.00 52.60  ? 2205 ASN A ND2   1 
ATOM   2504 N  N     . ALA A 1 415 ? 118.070 110.196 92.278  1.00 50.69  ? 2206 ALA A N     1 
ATOM   2505 C  CA    . ALA A 1 415 ? 118.833 109.388 93.216  1.00 49.01  ? 2206 ALA A CA    1 
ATOM   2506 C  C     . ALA A 1 415 ? 119.865 110.203 93.983  1.00 49.80  ? 2206 ALA A C     1 
ATOM   2507 O  O     . ALA A 1 415 ? 120.237 109.814 95.094  1.00 51.40  ? 2206 ALA A O     1 
ATOM   2508 C  CB    . ALA A 1 415 ? 119.521 108.246 92.472  1.00 49.00  ? 2206 ALA A CB    1 
ATOM   2509 N  N     . ILE A 1 416 ? 120.330 111.321 93.427  1.00 51.03  ? 2207 ILE A N     1 
ATOM   2510 C  CA    . ILE A 1 416 ? 121.475 112.025 93.997  1.00 53.20  ? 2207 ILE A CA    1 
ATOM   2511 C  C     . ILE A 1 416 ? 121.059 113.159 94.930  1.00 53.80  ? 2207 ILE A C     1 
ATOM   2512 O  O     . ILE A 1 416 ? 121.796 113.491 95.864  1.00 55.39  ? 2207 ILE A O     1 
ATOM   2513 C  CB    . ILE A 1 416 ? 122.407 112.543 92.883  1.00 55.09  ? 2207 ILE A CB    1 
ATOM   2514 C  CG1   . ILE A 1 416 ? 123.849 112.592 93.384  1.00 56.82  ? 2207 ILE A CG1   1 
ATOM   2515 C  CG2   . ILE A 1 416 ? 121.978 113.916 92.390  1.00 58.09  ? 2207 ILE A CG2   1 
ATOM   2516 C  CD1   . ILE A 1 416 ? 124.526 111.248 93.388  1.00 59.79  ? 2207 ILE A CD1   1 
ATOM   2517 N  N     . THR A 1 417 ? 119.892 113.770 94.702  1.00 52.89  ? 2208 THR A N     1 
ATOM   2518 C  CA    . THR A 1 417 ? 119.459 114.853 95.578  1.00 54.99  ? 2208 THR A CA    1 
ATOM   2519 C  C     . THR A 1 417 ? 118.293 114.477 96.478  1.00 56.59  ? 2208 THR A C     1 
ATOM   2520 O  O     . THR A 1 417 ? 118.139 115.084 97.542  1.00 58.13  ? 2208 THR A O     1 
ATOM   2521 C  CB    . THR A 1 417 ? 119.069 116.108 94.776  1.00 57.45  ? 2208 THR A CB    1 
ATOM   2522 O  OG1   . THR A 1 417 ? 118.434 117.051 95.647  1.00 63.61  ? 2208 THR A OG1   1 
ATOM   2523 C  CG2   . THR A 1 417 ? 118.081 115.769 93.689  1.00 54.17  ? 2208 THR A CG2   1 
ATOM   2524 N  N     . LYS A 1 418 ? 117.477 113.500 96.089  1.00 54.18  ? 2209 LYS A N     1 
ATOM   2525 C  CA    . LYS A 1 418 ? 116.358 113.069 96.912  1.00 51.99  ? 2209 LYS A CA    1 
ATOM   2526 C  C     . LYS A 1 418 ? 116.678 111.856 97.772  1.00 47.69  ? 2209 LYS A C     1 
ATOM   2527 O  O     . LYS A 1 418 ? 115.946 111.590 98.731  1.00 50.52  ? 2209 LYS A O     1 
ATOM   2528 C  CB    . LYS A 1 418 ? 115.138 112.756 96.037  1.00 52.21  ? 2209 LYS A CB    1 
ATOM   2529 C  CG    . LYS A 1 418 ? 114.307 113.972 95.670  1.00 56.63  ? 2209 LYS A CG    1 
ATOM   2530 C  CD    . LYS A 1 418 ? 113.004 113.581 94.992  1.00 58.44  ? 2209 LYS A CD    1 
ATOM   2531 C  CE    . LYS A 1 418 ? 112.273 112.501 95.773  1.00 53.83  ? 2209 LYS A CE    1 
ATOM   2532 N  NZ    . LYS A 1 418 ? 111.986 112.915 97.174  1.00 48.91  ? 2209 LYS A NZ    1 
ATOM   2533 N  N     . VAL A 1 419 ? 117.738 111.113 97.459  1.00 46.22  ? 2210 VAL A N     1 
ATOM   2534 C  CA    . VAL A 1 419 ? 118.020 109.888 98.195  1.00 43.57  ? 2210 VAL A CA    1 
ATOM   2535 C  C     . VAL A 1 419 ? 119.446 109.903 98.733  1.00 43.29  ? 2210 VAL A C     1 
ATOM   2536 O  O     . VAL A 1 419 ? 119.726 109.314 99.780  1.00 43.17  ? 2210 VAL A O     1 
ATOM   2537 C  CB    . VAL A 1 419 ? 117.759 108.657 97.306  1.00 43.82  ? 2210 VAL A CB    1 
ATOM   2538 C  CG1   . VAL A 1 419 ? 118.434 107.417 97.865  1.00 41.41  ? 2210 VAL A CG1   1 
ATOM   2539 C  CG2   . VAL A 1 419 ? 116.264 108.429 97.147  1.00 37.36  ? 2210 VAL A CG2   1 
ATOM   2540 N  N     . VAL A 1 420 ? 120.352 110.607 98.062  1.00 47.38  ? 2211 VAL A N     1 
ATOM   2541 C  CA    . VAL A 1 420 ? 121.746 110.632 98.506  1.00 49.26  ? 2211 VAL A CA    1 
ATOM   2542 C  C     . VAL A 1 420 ? 122.000 111.774 99.479  1.00 51.36  ? 2211 VAL A C     1 
ATOM   2543 O  O     . VAL A 1 420 ? 122.560 111.569 100.559 1.00 52.72  ? 2211 VAL A O     1 
ATOM   2544 C  CB    . VAL A 1 420 ? 122.699 110.700 97.293  1.00 50.28  ? 2211 VAL A CB    1 
ATOM   2545 C  CG1   . VAL A 1 420 ? 124.039 111.286 97.702  1.00 53.10  ? 2211 VAL A CG1   1 
ATOM   2546 C  CG2   . VAL A 1 420 ? 122.904 109.315 96.714  1.00 48.68  ? 2211 VAL A CG2   1 
ATOM   2547 N  N     . PHE A 1 421 ? 121.605 112.993 99.116  1.00 52.42  ? 2212 PHE A N     1 
ATOM   2548 C  CA    . PHE A 1 421 ? 121.776 114.124 100.026 1.00 52.52  ? 2212 PHE A CA    1 
ATOM   2549 C  C     . PHE A 1 421 ? 120.998 113.965 101.328 1.00 52.90  ? 2212 PHE A C     1 
ATOM   2550 O  O     . PHE A 1 421 ? 121.569 114.250 102.395 1.00 55.00  ? 2212 PHE A O     1 
ATOM   2551 C  CB    . PHE A 1 421 ? 121.414 115.427 99.305  1.00 55.58  ? 2212 PHE A CB    1 
ATOM   2552 C  CG    . PHE A 1 421 ? 122.585 116.098 98.643  1.00 63.18  ? 2212 PHE A CG    1 
ATOM   2553 C  CD1   . PHE A 1 421 ? 123.510 116.803 99.394  1.00 67.01  ? 2212 PHE A CD1   1 
ATOM   2554 C  CD2   . PHE A 1 421 ? 122.760 116.025 97.272  1.00 63.92  ? 2212 PHE A CD2   1 
ATOM   2555 C  CE1   . PHE A 1 421 ? 124.587 117.421 98.790  1.00 68.65  ? 2212 PHE A CE1   1 
ATOM   2556 C  CE2   . PHE A 1 421 ? 123.836 116.640 96.662  1.00 67.60  ? 2212 PHE A CE2   1 
ATOM   2557 C  CZ    . PHE A 1 421 ? 124.750 117.340 97.421  1.00 69.24  ? 2212 PHE A CZ    1 
ATOM   2558 N  N     . PRO A 1 422 ? 119.720 113.557 101.332 1.00 50.87  ? 2213 PRO A N     1 
ATOM   2559 C  CA    . PRO A 1 422 ? 119.039 113.364 102.625 1.00 50.50  ? 2213 PRO A CA    1 
ATOM   2560 C  C     . PRO A 1 422 ? 119.709 112.340 103.525 1.00 49.95  ? 2213 PRO A C     1 
ATOM   2561 O  O     . PRO A 1 422 ? 119.745 112.533 104.746 1.00 52.38  ? 2213 PRO A O     1 
ATOM   2562 C  CB    . PRO A 1 422 ? 117.628 112.923 102.211 1.00 49.99  ? 2213 PRO A CB    1 
ATOM   2563 C  CG    . PRO A 1 422 ? 117.439 113.511 100.868 1.00 50.10  ? 2213 PRO A CG    1 
ATOM   2564 C  CD    . PRO A 1 422 ? 118.779 113.407 100.207 1.00 50.86  ? 2213 PRO A CD    1 
ATOM   2565 N  N     . LEU A 1 423 ? 120.242 111.253 102.963 1.00 47.24  ? 2214 LEU A N     1 
ATOM   2566 C  CA    . LEU A 1 423 ? 120.924 110.264 103.792 1.00 45.12  ? 2214 LEU A CA    1 
ATOM   2567 C  C     . LEU A 1 423 ? 122.218 110.822 104.366 1.00 47.82  ? 2214 LEU A C     1 
ATOM   2568 O  O     . LEU A 1 423 ? 122.514 110.621 105.548 1.00 51.38  ? 2214 LEU A O     1 
ATOM   2569 C  CB    . LEU A 1 423 ? 121.203 108.994 102.990 1.00 45.74  ? 2214 LEU A CB    1 
ATOM   2570 C  CG    . LEU A 1 423 ? 120.006 108.161 102.530 1.00 42.94  ? 2214 LEU A CG    1 
ATOM   2571 C  CD1   . LEU A 1 423 ? 120.484 106.890 101.854 1.00 42.50  ? 2214 LEU A CD1   1 
ATOM   2572 C  CD2   . LEU A 1 423 ? 119.070 107.840 103.674 1.00 40.08  ? 2214 LEU A CD2   1 
ATOM   2573 N  N     . GLN A 1 424 ? 123.003 111.524 103.547 1.00 48.07  ? 2215 GLN A N     1 
ATOM   2574 C  CA    . GLN A 1 424 ? 124.242 112.118 104.035 1.00 50.58  ? 2215 GLN A CA    1 
ATOM   2575 C  C     . GLN A 1 424 ? 123.990 113.232 105.041 1.00 50.58  ? 2215 GLN A C     1 
ATOM   2576 O  O     . GLN A 1 424 ? 124.863 113.514 105.867 1.00 51.00  ? 2215 GLN A O     1 
ATOM   2577 C  CB    . GLN A 1 424 ? 125.069 112.652 102.865 1.00 54.56  ? 2215 GLN A CB    1 
ATOM   2578 C  CG    . GLN A 1 424 ? 125.476 111.595 101.852 1.00 57.06  ? 2215 GLN A CG    1 
ATOM   2579 C  CD    . GLN A 1 424 ? 126.649 110.760 102.320 1.00 61.22  ? 2215 GLN A CD    1 
ATOM   2580 O  OE1   . GLN A 1 424 ? 126.508 109.568 102.591 1.00 58.64  ? 2215 GLN A OE1   1 
ATOM   2581 N  NE2   . GLN A 1 424 ? 127.818 111.382 102.416 1.00 65.23  ? 2215 GLN A NE2   1 
ATOM   2582 N  N     . ARG A 1 425 ? 122.820 113.870 104.989 1.00 52.31  ? 2216 ARG A N     1 
ATOM   2583 C  CA    . ARG A 1 425 ? 122.511 114.951 105.919 1.00 52.37  ? 2216 ARG A CA    1 
ATOM   2584 C  C     . ARG A 1 425 ? 122.038 114.408 107.263 1.00 52.97  ? 2216 ARG A C     1 
ATOM   2585 O  O     . ARG A 1 425 ? 122.632 114.698 108.306 1.00 51.81  ? 2216 ARG A O     1 
ATOM   2586 C  CB    . ARG A 1 425 ? 121.456 115.876 105.307 1.00 50.64  ? 2216 ARG A CB    1 
ATOM   2587 C  CG    . ARG A 1 425 ? 120.839 116.854 106.286 1.00 52.98  ? 2216 ARG A CG    1 
ATOM   2588 C  CD    . ARG A 1 425 ? 119.615 117.519 105.684 1.00 57.87  ? 2216 ARG A CD    1 
ATOM   2589 N  NE    . ARG A 1 425 ? 118.584 116.548 105.337 1.00 56.28  ? 2216 ARG A NE    1 
ATOM   2590 C  CZ    . ARG A 1 425 ? 117.484 116.836 104.655 1.00 60.84  ? 2216 ARG A CZ    1 
ATOM   2591 N  NH1   . ARG A 1 425 ? 117.245 118.059 104.213 1.00 68.91  ? 2216 ARG A NH1   1 
ATOM   2592 N  NH2   . ARG A 1 425 ? 116.602 115.872 104.410 1.00 57.79  ? 2216 ARG A NH2   1 
ATOM   2593 N  N     . GLU A 1 426 ? 120.967 113.615 107.253 1.00 52.86  ? 2217 GLU A N     1 
ATOM   2594 C  CA    . GLU A 1 426 ? 120.402 113.055 108.481 1.00 49.21  ? 2217 GLU A CA    1 
ATOM   2595 C  C     . GLU A 1 426 ? 121.034 111.697 108.793 1.00 45.36  ? 2217 GLU A C     1 
ATOM   2596 O  O     . GLU A 1 426 ? 120.372 110.665 108.880 1.00 41.46  ? 2217 GLU A O     1 
ATOM   2597 C  CB    . GLU A 1 426 ? 118.886 112.950 108.364 1.00 46.61  ? 2217 GLU A CB    1 
ATOM   2598 C  CG    . GLU A 1 426 ? 118.191 114.278 108.099 1.00 50.65  ? 2217 GLU A CG    1 
ATOM   2599 C  CD    . GLU A 1 426 ? 117.921 115.066 109.370 1.00 53.32  ? 2217 GLU A CD    1 
ATOM   2600 O  OE1   . GLU A 1 426 ? 118.270 114.576 110.464 1.00 47.62  ? 2217 GLU A OE1   1 
ATOM   2601 O  OE2   . GLU A 1 426 ? 117.361 116.178 109.273 1.00 53.55  ? 2217 GLU A OE2   1 
ATOM   2602 N  N     . LYS A 1 427 ? 122.353 111.722 108.963 1.00 47.29  ? 2218 LYS A N     1 
ATOM   2603 C  CA    . LYS A 1 427 ? 123.138 110.536 109.280 1.00 44.30  ? 2218 LYS A CA    1 
ATOM   2604 C  C     . LYS A 1 427 ? 123.834 110.758 110.614 1.00 46.69  ? 2218 LYS A C     1 
ATOM   2605 O  O     . LYS A 1 427 ? 124.545 111.754 110.787 1.00 49.15  ? 2218 LYS A O     1 
ATOM   2606 C  CB    . LYS A 1 427 ? 124.154 110.246 108.175 1.00 47.76  ? 2218 LYS A CB    1 
ATOM   2607 C  CG    . LYS A 1 427 ? 125.261 109.290 108.563 1.00 46.97  ? 2218 LYS A CG    1 
ATOM   2608 C  CD    . LYS A 1 427 ? 126.186 109.041 107.386 1.00 49.82  ? 2218 LYS A CD    1 
ATOM   2609 C  CE    . LYS A 1 427 ? 126.677 110.344 106.774 1.00 51.98  ? 2218 LYS A CE    1 
ATOM   2610 N  NZ    . LYS A 1 427 ? 127.392 111.197 107.762 1.00 51.97  ? 2218 LYS A NZ    1 
ATOM   2611 N  N     . CYS A 1 428 ? 123.632 109.837 111.547 1.00 46.37  ? 2219 CYS A N     1 
ATOM   2612 C  CA    . CYS A 1 428 ? 124.166 109.957 112.891 1.00 52.00  ? 2219 CYS A CA    1 
ATOM   2613 C  C     . CYS A 1 428 ? 125.400 109.072 113.048 1.00 49.39  ? 2219 CYS A C     1 
ATOM   2614 O  O     . CYS A 1 428 ? 125.897 108.475 112.089 1.00 48.27  ? 2219 CYS A O     1 
ATOM   2615 C  CB    . CYS A 1 428 ? 123.083 109.608 113.914 1.00 53.96  ? 2219 CYS A CB    1 
ATOM   2616 S  SG    . CYS A 1 428 ? 121.561 110.569 113.751 1.00 73.32  ? 2219 CYS A SG    1 
ATOM   2617 N  N     . LEU A 1 429 ? 125.910 108.992 114.274 1.00 53.47  ? 2220 LEU A N     1 
ATOM   2618 C  CA    . LEU A 1 429 ? 127.058 108.158 114.594 1.00 54.56  ? 2220 LEU A CA    1 
ATOM   2619 C  C     . LEU A 1 429 ? 126.788 107.432 115.902 1.00 57.20  ? 2220 LEU A C     1 
ATOM   2620 O  O     . LEU A 1 429 ? 126.270 108.024 116.853 1.00 61.52  ? 2220 LEU A O     1 
ATOM   2621 C  CB    . LEU A 1 429 ? 128.342 108.991 114.707 1.00 60.53  ? 2220 LEU A CB    1 
ATOM   2622 C  CG    . LEU A 1 429 ? 129.675 108.265 114.513 1.00 60.64  ? 2220 LEU A CG    1 
ATOM   2623 C  CD1   . LEU A 1 429 ? 130.690 109.189 113.858 1.00 61.56  ? 2220 LEU A CD1   1 
ATOM   2624 C  CD2   . LEU A 1 429 ? 130.209 107.739 115.835 1.00 60.67  ? 2220 LEU A CD2   1 
ATOM   2625 N  N     . ASN A 1 430 ? 127.142 106.150 115.946 1.00 56.42  ? 2221 ASN A N     1 
ATOM   2626 C  CA    . ASN A 1 430 ? 126.979 105.345 117.152 1.00 59.59  ? 2221 ASN A CA    1 
ATOM   2627 C  C     . ASN A 1 430 ? 128.353 104.941 117.665 1.00 64.62  ? 2221 ASN A C     1 
ATOM   2628 O  O     . ASN A 1 430 ? 128.953 103.987 117.146 1.00 66.82  ? 2221 ASN A O     1 
ATOM   2629 C  CB    . ASN A 1 430 ? 126.123 104.107 116.868 1.00 58.77  ? 2221 ASN A CB    1 
ATOM   2630 C  CG    . ASN A 1 430 ? 125.658 103.417 118.135 1.00 63.89  ? 2221 ASN A CG    1 
ATOM   2631 O  OD1   . ASN A 1 430 ? 126.388 102.623 118.727 1.00 66.68  ? 2221 ASN A OD1   1 
ATOM   2632 N  ND2   . ASN A 1 430 ? 124.436 103.718 118.559 1.00 58.96  ? 2221 ASN A ND2   1 
ATOM   2633 N  N     . PRO A 1 431 ? 128.900 105.635 118.666 1.00 66.04  ? 2222 PRO A N     1 
ATOM   2634 C  CA    . PRO A 1 431 ? 130.247 105.286 119.150 1.00 68.31  ? 2222 PRO A CA    1 
ATOM   2635 C  C     . PRO A 1 431 ? 130.353 103.869 119.683 1.00 68.39  ? 2222 PRO A C     1 
ATOM   2636 O  O     . PRO A 1 431 ? 131.415 103.248 119.554 1.00 71.86  ? 2222 PRO A O     1 
ATOM   2637 C  CB    . PRO A 1 431 ? 130.502 106.324 120.252 1.00 64.11  ? 2222 PRO A CB    1 
ATOM   2638 C  CG    . PRO A 1 431 ? 129.568 107.451 119.944 1.00 64.74  ? 2222 PRO A CG    1 
ATOM   2639 C  CD    . PRO A 1 431 ? 128.350 106.814 119.353 1.00 65.98  ? 2222 PRO A CD    1 
ATOM   2640 N  N     . PHE A 1 432 ? 129.285 103.342 120.285 1.00 64.96  ? 2223 PHE A N     1 
ATOM   2641 C  CA    . PHE A 1 432 ? 129.336 101.990 120.833 1.00 65.91  ? 2223 PHE A CA    1 
ATOM   2642 C  C     . PHE A 1 432 ? 129.533 100.953 119.734 1.00 64.35  ? 2223 PHE A C     1 
ATOM   2643 O  O     . PHE A 1 432 ? 130.322 100.014 119.890 1.00 67.09  ? 2223 PHE A O     1 
ATOM   2644 C  CB    . PHE A 1 432 ? 128.063 101.701 121.627 1.00 68.81  ? 2223 PHE A CB    1 
ATOM   2645 C  CG    . PHE A 1 432 ? 127.746 102.745 122.660 1.00 69.90  ? 2223 PHE A CG    1 
ATOM   2646 C  CD1   . PHE A 1 432 ? 128.334 102.699 123.913 1.00 70.94  ? 2223 PHE A CD1   1 
ATOM   2647 C  CD2   . PHE A 1 432 ? 126.865 103.775 122.376 1.00 67.76  ? 2223 PHE A CD2   1 
ATOM   2648 C  CE1   . PHE A 1 432 ? 128.046 103.659 124.864 1.00 71.51  ? 2223 PHE A CE1   1 
ATOM   2649 C  CE2   . PHE A 1 432 ? 126.575 104.738 123.322 1.00 67.84  ? 2223 PHE A CE2   1 
ATOM   2650 C  CZ    . PHE A 1 432 ? 127.166 104.680 124.568 1.00 69.52  ? 2223 PHE A CZ    1 
ATOM   2651 N  N     . LEU A 1 433 ? 128.827 101.107 118.613 1.00 63.23  ? 2224 LEU A N     1 
ATOM   2652 C  CA    . LEU A 1 433 ? 128.971 100.175 117.502 1.00 64.61  ? 2224 LEU A CA    1 
ATOM   2653 C  C     . LEU A 1 433 ? 130.187 100.474 116.637 1.00 64.89  ? 2224 LEU A C     1 
ATOM   2654 O  O     . LEU A 1 433 ? 130.592 99.618  115.844 1.00 62.83  ? 2224 LEU A O     1 
ATOM   2655 C  CB    . LEU A 1 433 ? 127.712 100.190 116.632 1.00 57.92  ? 2224 LEU A CB    1 
ATOM   2656 C  CG    . LEU A 1 433 ? 126.443 99.631  117.273 1.00 54.58  ? 2224 LEU A CG    1 
ATOM   2657 C  CD1   . LEU A 1 433 ? 125.351 99.459  116.234 1.00 48.46  ? 2224 LEU A CD1   1 
ATOM   2658 C  CD2   . LEU A 1 433 ? 126.732 98.315  117.971 1.00 59.09  ? 2224 LEU A CD2   1 
ATOM   2659 N  N     . GLY A 1 434 ? 130.774 101.661 116.769 1.00 62.92  ? 2225 GLY A N     1 
ATOM   2660 C  CA    . GLY A 1 434 ? 131.922 102.018 115.964 1.00 60.70  ? 2225 GLY A CA    1 
ATOM   2661 C  C     . GLY A 1 434 ? 131.619 102.309 114.514 1.00 60.19  ? 2225 GLY A C     1 
ATOM   2662 O  O     . GLY A 1 434 ? 132.549 102.377 113.705 1.00 65.50  ? 2225 GLY A O     1 
ATOM   2663 N  N     . MET A 1 435 ? 130.349 102.483 114.156 1.00 56.84  ? 2226 MET A N     1 
ATOM   2664 C  CA    . MET A 1 435 ? 129.962 102.713 112.774 1.00 54.30  ? 2226 MET A CA    1 
ATOM   2665 C  C     . MET A 1 435 ? 128.919 103.819 112.719 1.00 51.08  ? 2226 MET A C     1 
ATOM   2666 O  O     . MET A 1 435 ? 128.279 104.149 113.720 1.00 54.06  ? 2226 MET A O     1 
ATOM   2667 C  CB    . MET A 1 435 ? 129.423 101.437 112.120 1.00 54.81  ? 2226 MET A CB    1 
ATOM   2668 C  CG    . MET A 1 435 ? 127.963 101.168 112.403 1.00 50.21  ? 2226 MET A CG    1 
ATOM   2669 S  SD    . MET A 1 435 ? 127.309 99.921  111.286 1.00 55.61  ? 2226 MET A SD    1 
ATOM   2670 C  CE    . MET A 1 435 ? 126.150 100.900 110.348 1.00 45.07  ? 2226 MET A CE    1 
ATOM   2671 N  N     . GLU A 1 436 ? 128.757 104.390 111.529 1.00 50.52  ? 2227 GLU A N     1 
ATOM   2672 C  CA    . GLU A 1 436 ? 127.901 105.557 111.328 1.00 51.30  ? 2227 GLU A CA    1 
ATOM   2673 C  C     . GLU A 1 436 ? 126.512 105.083 110.918 1.00 45.27  ? 2227 GLU A C     1 
ATOM   2674 O  O     . GLU A 1 436 ? 126.246 104.841 109.740 1.00 45.38  ? 2227 GLU A O     1 
ATOM   2675 C  CB    . GLU A 1 436 ? 128.512 106.487 110.285 1.00 53.34  ? 2227 GLU A CB    1 
ATOM   2676 C  CG    . GLU A 1 436 ? 129.469 107.512 110.875 1.00 56.56  ? 2227 GLU A CG    1 
ATOM   2677 C  CD    . GLU A 1 436 ? 129.592 108.762 110.030 1.00 60.77  ? 2227 GLU A CD    1 
ATOM   2678 O  OE1   . GLU A 1 436 ? 130.482 109.590 110.318 1.00 67.15  ? 2227 GLU A OE1   1 
ATOM   2679 O  OE2   . GLU A 1 436 ? 128.807 108.916 109.075 1.00 60.98  ? 2227 GLU A OE2   1 
ATOM   2680 N  N     . ARG A 1 437 ? 125.620 104.957 111.896 1.00 43.51  ? 2228 ARG A N     1 
ATOM   2681 C  CA    . ARG A 1 437 ? 124.248 104.550 111.643 1.00 34.42  ? 2228 ARG A CA    1 
ATOM   2682 C  C     . ARG A 1 437 ? 123.424 105.727 111.130 1.00 34.08  ? 2228 ARG A C     1 
ATOM   2683 O  O     . ARG A 1 437 ? 123.904 106.855 111.004 1.00 45.50  ? 2228 ARG A O     1 
ATOM   2684 C  CB    . ARG A 1 437 ? 123.607 103.994 112.911 1.00 34.39  ? 2228 ARG A CB    1 
ATOM   2685 C  CG    . ARG A 1 437 ? 124.482 103.050 113.702 1.00 43.06  ? 2228 ARG A CG    1 
ATOM   2686 C  CD    . ARG A 1 437 ? 123.623 102.067 114.468 1.00 42.60  ? 2228 ARG A CD    1 
ATOM   2687 N  NE    . ARG A 1 437 ? 122.776 101.300 113.565 1.00 35.27  ? 2228 ARG A NE    1 
ATOM   2688 C  CZ    . ARG A 1 437 ? 123.190 100.260 112.856 1.00 37.07  ? 2228 ARG A CZ    1 
ATOM   2689 N  NH1   . ARG A 1 437 ? 124.428 99.807  112.955 1.00 42.07  ? 2228 ARG A NH1   1 
ATOM   2690 N  NH2   . ARG A 1 437 ? 122.343 99.664  112.025 1.00 35.64  ? 2228 ARG A NH2   1 
ATOM   2691 N  N     . ILE A 1 438 ? 122.160 105.446 110.822 1.00 25.06  ? 2229 ILE A N     1 
ATOM   2692 C  CA    . ILE A 1 438 ? 121.187 106.480 110.493 1.00 28.65  ? 2229 ILE A CA    1 
ATOM   2693 C  C     . ILE A 1 438 ? 119.843 106.060 111.069 1.00 30.68  ? 2229 ILE A C     1 
ATOM   2694 O  O     . ILE A 1 438 ? 119.359 104.960 110.780 1.00 31.04  ? 2229 ILE A O     1 
ATOM   2695 C  CB    . ILE A 1 438 ? 121.082 106.724 108.978 1.00 35.37  ? 2229 ILE A CB    1 
ATOM   2696 C  CG1   . ILE A 1 438 ? 119.769 107.420 108.637 1.00 34.78  ? 2229 ILE A CG1   1 
ATOM   2697 C  CG2   . ILE A 1 438 ? 121.217 105.428 108.207 1.00 37.07  ? 2229 ILE A CG2   1 
ATOM   2698 C  CD1   . ILE A 1 438 ? 119.664 107.771 107.190 1.00 36.49  ? 2229 ILE A CD1   1 
ATOM   2699 N  N     . TYR A 1 439 ? 119.241 106.929 111.883 1.00 35.01  ? 2230 TYR A N     1 
ATOM   2700 C  CA    . TYR A 1 439 ? 118.015 106.593 112.592 1.00 31.98  ? 2230 TYR A CA    1 
ATOM   2701 C  C     . TYR A 1 439 ? 116.837 107.292 111.937 1.00 31.89  ? 2230 TYR A C     1 
ATOM   2702 O  O     . TYR A 1 439 ? 116.698 108.515 112.084 1.00 37.52  ? 2230 TYR A O     1 
ATOM   2703 C  CB    . TYR A 1 439 ? 118.116 106.995 114.062 1.00 28.63  ? 2230 TYR A CB    1 
ATOM   2704 C  CG    . TYR A 1 439 ? 119.353 106.487 114.759 1.00 28.86  ? 2230 TYR A CG    1 
ATOM   2705 C  CD1   . TYR A 1 439 ? 119.354 105.261 115.403 1.00 29.01  ? 2230 TYR A CD1   1 
ATOM   2706 C  CD2   . TYR A 1 439 ? 120.519 107.235 114.777 1.00 34.17  ? 2230 TYR A CD2   1 
ATOM   2707 C  CE1   . TYR A 1 439 ? 120.481 104.794 116.043 1.00 32.33  ? 2230 TYR A CE1   1 
ATOM   2708 C  CE2   . TYR A 1 439 ? 121.653 106.774 115.413 1.00 37.47  ? 2230 TYR A CE2   1 
ATOM   2709 C  CZ    . TYR A 1 439 ? 121.627 105.552 116.043 1.00 37.20  ? 2230 TYR A CZ    1 
ATOM   2710 O  OH    . TYR A 1 439 ? 122.752 105.087 116.680 1.00 44.47  ? 2230 TYR A OH    1 
ATOM   2711 N  N     . PRO A 1 440 ? 115.973 106.583 111.223 1.00 27.40  ? 2231 PRO A N     1 
ATOM   2712 C  CA    . PRO A 1 440 ? 114.762 107.206 110.687 1.00 28.39  ? 2231 PRO A CA    1 
ATOM   2713 C  C     . PRO A 1 440 ? 113.722 107.386 111.784 1.00 28.39  ? 2231 PRO A C     1 
ATOM   2714 O  O     . PRO A 1 440 ? 113.806 106.804 112.865 1.00 30.15  ? 2231 PRO A O     1 
ATOM   2715 C  CB    . PRO A 1 440 ? 114.291 106.204 109.633 1.00 30.09  ? 2231 PRO A CB    1 
ATOM   2716 C  CG    . PRO A 1 440 ? 114.766 104.893 110.148 1.00 32.95  ? 2231 PRO A CG    1 
ATOM   2717 C  CD    . PRO A 1 440 ? 116.067 105.159 110.861 1.00 31.67  ? 2231 PRO A CD    1 
ATOM   2718 N  N     . VAL A 1 441 ? 112.730 108.216 111.485 1.00 29.13  ? 2232 VAL A N     1 
ATOM   2719 C  CA    . VAL A 1 441 ? 111.617 108.466 112.392 1.00 27.66  ? 2232 VAL A CA    1 
ATOM   2720 C  C     . VAL A 1 441 ? 110.425 107.694 111.847 1.00 28.48  ? 2232 VAL A C     1 
ATOM   2721 O  O     . VAL A 1 441 ? 109.930 107.986 110.752 1.00 28.94  ? 2232 VAL A O     1 
ATOM   2722 C  CB    . VAL A 1 441 ? 111.314 109.964 112.530 1.00 25.13  ? 2232 VAL A CB    1 
ATOM   2723 C  CG1   . VAL A 1 441 ? 109.848 110.197 112.874 1.00 25.27  ? 2232 VAL A CG1   1 
ATOM   2724 C  CG2   . VAL A 1 441 ? 112.217 110.589 113.581 1.00 23.79  ? 2232 VAL A CG2   1 
ATOM   2725 N  N     . SER A 1 442 ? 109.979 106.689 112.591 1.00 28.43  ? 2233 SER A N     1 
ATOM   2726 C  CA    . SER A 1 442 ? 108.871 105.867 112.140 1.00 22.59  ? 2233 SER A CA    1 
ATOM   2727 C  C     . SER A 1 442 ? 107.562 106.646 112.216 1.00 24.55  ? 2233 SER A C     1 
ATOM   2728 O  O     . SER A 1 442 ? 107.417 107.604 112.980 1.00 32.09  ? 2233 SER A O     1 
ATOM   2729 C  CB    . SER A 1 442 ? 108.777 104.592 112.976 1.00 24.18  ? 2233 SER A CB    1 
ATOM   2730 O  OG    . SER A 1 442 ? 107.564 103.906 112.729 1.00 32.34  ? 2233 SER A OG    1 
ATOM   2731 N  N     . GLN A 1 443 ? 106.601 106.226 111.399 1.00 19.76  ? 2234 GLN A N     1 
ATOM   2732 C  CA    . GLN A 1 443 ? 105.272 106.820 111.411 1.00 24.15  ? 2234 GLN A CA    1 
ATOM   2733 C  C     . GLN A 1 443 ? 104.271 105.732 111.067 1.00 23.89  ? 2234 GLN A C     1 
ATOM   2734 O  O     . GLN A 1 443 ? 104.366 105.118 109.999 1.00 29.91  ? 2234 GLN A O     1 
ATOM   2735 C  CB    . GLN A 1 443 ? 105.178 107.978 110.418 1.00 23.23  ? 2234 GLN A CB    1 
ATOM   2736 C  CG    . GLN A 1 443 ? 103.769 108.496 110.205 1.00 29.69  ? 2234 GLN A CG    1 
ATOM   2737 C  CD    . GLN A 1 443 ? 103.705 109.581 109.154 1.00 37.60  ? 2234 GLN A CD    1 
ATOM   2738 O  OE1   . GLN A 1 443 ? 104.726 110.153 108.775 1.00 48.77  ? 2234 GLN A OE1   1 
ATOM   2739 N  NE2   . GLN A 1 443 ? 102.501 109.873 108.676 1.00 36.60  ? 2234 GLN A NE2   1 
ATOM   2740 N  N     . SER A 1 444 ? 103.330 105.487 111.975 1.00 22.22  ? 2235 SER A N     1 
ATOM   2741 C  CA    . SER A 1 444 ? 102.291 104.487 111.780 1.00 22.70  ? 2235 SER A CA    1 
ATOM   2742 C  C     . SER A 1 444 ? 100.931 105.108 111.505 1.00 26.47  ? 2235 SER A C     1 
ATOM   2743 O  O     . SER A 1 444 ? 99.922  104.397 111.520 1.00 30.41  ? 2235 SER A O     1 
ATOM   2744 C  CB    . SER A 1 444 ? 102.209 103.569 112.998 1.00 30.32  ? 2235 SER A CB    1 
ATOM   2745 O  OG    . SER A 1 444 ? 103.502 103.191 113.427 1.00 27.69  ? 2235 SER A OG    1 
ATOM   2746 N  N     . HIS A 1 445 ? 100.877 106.416 111.248 1.00 26.44  ? 2236 HIS A N     1 
ATOM   2747 C  CA    . HIS A 1 445 ? 99.621  107.102 110.976 1.00 26.99  ? 2236 HIS A CA    1 
ATOM   2748 C  C     . HIS A 1 445 ? 99.243  107.060 109.502 1.00 30.06  ? 2236 HIS A C     1 
ATOM   2749 O  O     . HIS A 1 445 ? 98.519  107.941 109.021 1.00 32.58  ? 2236 HIS A O     1 
ATOM   2750 C  CB    . HIS A 1 445 ? 99.688  108.547 111.469 1.00 26.30  ? 2236 HIS A CB    1 
ATOM   2751 C  CG    . HIS A 1 445 ? 98.352  109.120 111.822 1.00 30.20  ? 2236 HIS A CG    1 
ATOM   2752 N  ND1   . HIS A 1 445 ? 97.755  108.915 113.046 1.00 29.46  ? 2236 HIS A ND1   1 
ATOM   2753 C  CD2   . HIS A 1 445 ? 97.491  109.880 111.106 1.00 33.70  ? 2236 HIS A CD2   1 
ATOM   2754 C  CE1   . HIS A 1 445 ? 96.585  109.527 113.071 1.00 33.62  ? 2236 HIS A CE1   1 
ATOM   2755 N  NE2   . HIS A 1 445 ? 96.401  110.121 111.906 1.00 36.05  ? 2236 HIS A NE2   1 
ATOM   2756 N  N     . THR A 1 446 ? 99.722  106.060 108.770 1.00 27.12  ? 2237 THR A N     1 
ATOM   2757 C  CA    . THR A 1 446 ? 99.378  105.923 107.367 1.00 25.63  ? 2237 THR A CA    1 
ATOM   2758 C  C     . THR A 1 446 ? 97.919  105.506 107.214 1.00 26.94  ? 2237 THR A C     1 
ATOM   2759 O  O     . THR A 1 446 ? 97.276  105.030 108.152 1.00 26.70  ? 2237 THR A O     1 
ATOM   2760 C  CB    . THR A 1 446 ? 100.289 104.902 106.696 1.00 25.00  ? 2237 THR A CB    1 
ATOM   2761 O  OG1   . THR A 1 446 ? 99.988  103.599 107.204 1.00 26.21  ? 2237 THR A OG1   1 
ATOM   2762 C  CG2   . THR A 1 446 ? 101.744 105.224 106.990 1.00 22.23  ? 2237 THR A CG2   1 
ATOM   2763 N  N     . ALA A 1 447 ? 97.395  105.694 106.003 1.00 28.88  ? 2238 ALA A N     1 
ATOM   2764 C  CA    . ALA A 1 447 ? 95.981  105.432 105.757 1.00 27.44  ? 2238 ALA A CA    1 
ATOM   2765 C  C     . ALA A 1 447 ? 95.672  103.942 105.835 1.00 26.00  ? 2238 ALA A C     1 
ATOM   2766 O  O     . ALA A 1 447 ? 94.852  103.507 106.652 1.00 29.58  ? 2238 ALA A O     1 
ATOM   2767 C  CB    . ALA A 1 447 ? 95.576  105.998 104.396 1.00 29.57  ? 2238 ALA A CB    1 
ATOM   2768 N  N     . THR A 1 448 ? 96.317  103.142 104.984 1.00 25.07  ? 2239 THR A N     1 
ATOM   2769 C  CA    . THR A 1 448 ? 96.030  101.711 104.952 1.00 24.85  ? 2239 THR A CA    1 
ATOM   2770 C  C     . THR A 1 448 ? 96.413  101.037 106.262 1.00 26.02  ? 2239 THR A C     1 
ATOM   2771 O  O     . THR A 1 448 ? 95.660  100.205 106.783 1.00 30.76  ? 2239 THR A O     1 
ATOM   2772 C  CB    . THR A 1 448 ? 96.760  101.056 103.782 1.00 23.02  ? 2239 THR A CB    1 
ATOM   2773 O  OG1   . THR A 1 448 ? 98.052  101.654 103.632 1.00 24.72  ? 2239 THR A OG1   1 
ATOM   2774 C  CG2   . THR A 1 448 ? 95.973  101.242 102.496 1.00 25.18  ? 2239 THR A CG2   1 
ATOM   2775 N  N     . GLY A 1 449 ? 97.569  101.386 106.815 1.00 23.52  ? 2240 GLY A N     1 
ATOM   2776 C  CA    . GLY A 1 449 ? 98.023  100.770 108.045 1.00 24.04  ? 2240 GLY A CA    1 
ATOM   2777 C  C     . GLY A 1 449 ? 99.492  100.412 108.023 1.00 22.83  ? 2240 GLY A C     1 
ATOM   2778 O  O     . GLY A 1 449 ? 100.001 99.795  108.963 1.00 25.60  ? 2240 GLY A O     1 
ATOM   2779 N  N     . ARG A 1 450 ? 100.186 100.796 106.955 1.00 20.94  ? 2241 ARG A N     1 
ATOM   2780 C  CA    . ARG A 1 450 ? 101.607 100.512 106.836 1.00 22.57  ? 2241 ARG A CA    1 
ATOM   2781 C  C     . ARG A 1 450 ? 102.407 101.373 107.809 1.00 26.17  ? 2241 ARG A C     1 
ATOM   2782 O  O     . ARG A 1 450 ? 101.864 102.142 108.606 1.00 30.21  ? 2241 ARG A O     1 
ATOM   2783 C  CB    . ARG A 1 450 ? 102.085 100.746 105.405 1.00 19.90  ? 2241 ARG A CB    1 
ATOM   2784 C  CG    . ARG A 1 450 ? 100.991 100.718 104.362 1.00 20.12  ? 2241 ARG A CG    1 
ATOM   2785 C  CD    . ARG A 1 450 ? 101.577 100.703 102.963 1.00 18.76  ? 2241 ARG A CD    1 
ATOM   2786 N  NE    . ARG A 1 450 ? 101.882 99.354  102.503 1.00 20.09  ? 2241 ARG A NE    1 
ATOM   2787 C  CZ    . ARG A 1 450 ? 102.337 99.064  101.292 1.00 19.95  ? 2241 ARG A CZ    1 
ATOM   2788 N  NH1   . ARG A 1 450 ? 102.561 100.008 100.395 1.00 16.16  ? 2241 ARG A NH1   1 
ATOM   2789 N  NH2   . ARG A 1 450 ? 102.567 97.794  100.972 1.00 20.20  ? 2241 ARG A NH2   1 
ATOM   2790 N  N     . ILE A 1 451 ? 103.725 101.229 107.740 1.00 24.40  ? 2242 ILE A N     1 
ATOM   2791 C  CA    . ILE A 1 451 ? 104.658 102.014 108.535 1.00 22.11  ? 2242 ILE A CA    1 
ATOM   2792 C  C     . ILE A 1 451 ? 105.614 102.689 107.565 1.00 23.48  ? 2242 ILE A C     1 
ATOM   2793 O  O     . ILE A 1 451 ? 106.233 102.014 106.736 1.00 26.97  ? 2242 ILE A O     1 
ATOM   2794 C  CB    . ILE A 1 451 ? 105.427 101.143 109.540 1.00 20.44  ? 2242 ILE A CB    1 
ATOM   2795 C  CG1   . ILE A 1 451 ? 104.455 100.491 110.525 1.00 23.39  ? 2242 ILE A CG1   1 
ATOM   2796 C  CG2   . ILE A 1 451 ? 106.472 101.966 110.266 1.00 21.99  ? 2242 ILE A CG2   1 
ATOM   2797 C  CD1   . ILE A 1 451 ? 104.959 99.194  111.113 1.00 24.38  ? 2242 ILE A CD1   1 
ATOM   2798 N  N     . THR A 1 452 ? 105.724 104.010 107.653 1.00 21.07  ? 2243 THR A N     1 
ATOM   2799 C  CA    . THR A 1 452 ? 106.575 104.781 106.757 1.00 20.44  ? 2243 THR A CA    1 
ATOM   2800 C  C     . THR A 1 452 ? 107.570 105.593 107.568 1.00 22.65  ? 2243 THR A C     1 
ATOM   2801 O  O     . THR A 1 452 ? 107.225 106.148 108.612 1.00 29.82  ? 2243 THR A O     1 
ATOM   2802 C  CB    . THR A 1 452 ? 105.750 105.708 105.868 1.00 25.31  ? 2243 THR A CB    1 
ATOM   2803 O  OG1   . THR A 1 452 ? 104.832 106.451 106.677 1.00 28.13  ? 2243 THR A OG1   1 
ATOM   2804 C  CG2   . THR A 1 452 ? 104.975 104.898 104.847 1.00 25.02  ? 2243 THR A CG2   1 
ATOM   2805 N  N     . PHE A 1 453 ? 108.804 105.665 107.088 1.00 22.04  ? 2244 PHE A N     1 
ATOM   2806 C  CA    . PHE A 1 453 ? 109.883 106.312 107.820 1.00 25.53  ? 2244 PHE A CA    1 
ATOM   2807 C  C     . PHE A 1 453 ? 110.219 107.647 107.173 1.00 28.12  ? 2244 PHE A C     1 
ATOM   2808 O  O     . PHE A 1 453 ? 110.414 107.723 105.957 1.00 30.98  ? 2244 PHE A O     1 
ATOM   2809 C  CB    . PHE A 1 453 ? 111.110 105.403 107.878 1.00 23.88  ? 2244 PHE A CB    1 
ATOM   2810 C  CG    . PHE A 1 453 ? 110.825 104.064 108.487 1.00 21.75  ? 2244 PHE A CG    1 
ATOM   2811 C  CD1   . PHE A 1 453 ? 110.847 103.896 109.858 1.00 24.28  ? 2244 PHE A CD1   1 
ATOM   2812 C  CD2   . PHE A 1 453 ? 110.511 102.979 107.691 1.00 21.10  ? 2244 PHE A CD2   1 
ATOM   2813 C  CE1   . PHE A 1 453 ? 110.571 102.670 110.422 1.00 21.69  ? 2244 PHE A CE1   1 
ATOM   2814 C  CE2   . PHE A 1 453 ? 110.236 101.749 108.252 1.00 22.17  ? 2244 PHE A CE2   1 
ATOM   2815 C  CZ    . PHE A 1 453 ? 110.267 101.595 109.619 1.00 21.50  ? 2244 PHE A CZ    1 
ATOM   2816 N  N     . THR A 1 454 ? 110.267 108.694 107.989 1.00 26.91  ? 2245 THR A N     1 
ATOM   2817 C  CA    . THR A 1 454 ? 110.568 110.044 107.549 1.00 29.04  ? 2245 THR A CA    1 
ATOM   2818 C  C     . THR A 1 454 ? 111.853 110.526 108.208 1.00 33.37  ? 2245 THR A C     1 
ATOM   2819 O  O     . THR A 1 454 ? 112.318 109.960 109.201 1.00 36.79  ? 2245 THR A O     1 
ATOM   2820 C  CB    . THR A 1 454 ? 109.425 111.011 107.885 1.00 33.02  ? 2245 THR A CB    1 
ATOM   2821 O  OG1   . THR A 1 454 ? 109.639 111.568 109.187 1.00 35.20  ? 2245 THR A OG1   1 
ATOM   2822 C  CG2   . THR A 1 454 ? 108.092 110.285 107.872 1.00 29.03  ? 2245 THR A CG2   1 
ATOM   2823 N  N     . GLU A 1 455 ? 112.420 111.584 107.635 1.00 34.55  ? 2246 GLU A N     1 
ATOM   2824 C  CA    . GLU A 1 455 ? 113.625 112.245 108.122 1.00 37.14  ? 2246 GLU A CA    1 
ATOM   2825 C  C     . GLU A 1 455 ? 114.780 111.269 108.328 1.00 37.57  ? 2246 GLU A C     1 
ATOM   2826 O  O     . GLU A 1 455 ? 115.220 111.072 109.467 1.00 36.31  ? 2246 GLU A O     1 
ATOM   2827 C  CB    . GLU A 1 455 ? 113.332 112.982 109.430 1.00 39.12  ? 2246 GLU A CB    1 
ATOM   2828 C  CG    . GLU A 1 455 ? 112.433 114.198 109.276 1.00 43.47  ? 2246 GLU A CG    1 
ATOM   2829 C  CD    . GLU A 1 455 ? 113.207 115.460 108.950 1.00 54.42  ? 2246 GLU A CD    1 
ATOM   2830 O  OE1   . GLU A 1 455 ? 113.732 115.564 107.821 1.00 55.04  ? 2246 GLU A OE1   1 
ATOM   2831 O  OE2   . GLU A 1 455 ? 113.291 116.349 109.823 1.00 54.42  ? 2246 GLU A OE2   1 
ATOM   2832 N  N     . PRO A 1 456 ? 115.302 110.638 107.266 1.00 38.84  ? 2247 PRO A N     1 
ATOM   2833 C  CA    . PRO A 1 456 ? 114.838 110.629 105.876 1.00 38.17  ? 2247 PRO A CA    1 
ATOM   2834 C  C     . PRO A 1 456 ? 113.978 109.404 105.599 1.00 36.89  ? 2247 PRO A C     1 
ATOM   2835 O  O     . PRO A 1 456 ? 113.582 108.708 106.528 1.00 38.04  ? 2247 PRO A O     1 
ATOM   2836 C  CB    . PRO A 1 456 ? 116.148 110.605 105.093 1.00 41.17  ? 2247 PRO A CB    1 
ATOM   2837 C  CG    . PRO A 1 456 ? 117.028 109.729 105.941 1.00 40.30  ? 2247 PRO A CG    1 
ATOM   2838 C  CD    . PRO A 1 456 ? 116.609 109.967 107.383 1.00 38.56  ? 2247 PRO A CD    1 
ATOM   2839 N  N     . ASN A 1 457 ? 113.677 109.103 104.339 1.00 33.63  ? 2248 ASN A N     1 
ATOM   2840 C  CA    . ASN A 1 457 ? 112.893 107.926 103.984 1.00 30.02  ? 2248 ASN A CA    1 
ATOM   2841 C  C     . ASN A 1 457 ? 113.840 106.833 103.504 1.00 29.22  ? 2248 ASN A C     1 
ATOM   2842 O  O     . ASN A 1 457 ? 114.386 106.914 102.400 1.00 31.98  ? 2248 ASN A O     1 
ATOM   2843 C  CB    . ASN A 1 457 ? 111.855 108.259 102.916 1.00 29.29  ? 2248 ASN A CB    1 
ATOM   2844 C  CG    . ASN A 1 457 ? 110.672 107.318 102.950 1.00 27.96  ? 2248 ASN A CG    1 
ATOM   2845 O  OD1   . ASN A 1 457 ? 110.785 106.179 103.399 1.00 27.13  ? 2248 ASN A OD1   1 
ATOM   2846 N  ND2   . ASN A 1 457 ? 109.527 107.789 102.479 1.00 28.97  ? 2248 ASN A ND2   1 
ATOM   2847 N  N     . ILE A 1 458 ? 114.032 105.809 104.338 1.00 26.19  ? 2249 ILE A N     1 
ATOM   2848 C  CA    . ILE A 1 458 ? 114.888 104.692 103.960 1.00 21.88  ? 2249 ILE A CA    1 
ATOM   2849 C  C     . ILE A 1 458 ? 114.165 103.702 103.061 1.00 23.80  ? 2249 ILE A C     1 
ATOM   2850 O  O     . ILE A 1 458 ? 114.816 102.896 102.386 1.00 26.86  ? 2249 ILE A O     1 
ATOM   2851 C  CB    . ILE A 1 458 ? 115.421 103.966 105.206 1.00 21.49  ? 2249 ILE A CB    1 
ATOM   2852 C  CG1   . ILE A 1 458 ? 115.646 104.955 106.348 1.00 29.43  ? 2249 ILE A CG1   1 
ATOM   2853 C  CG2   . ILE A 1 458 ? 116.710 103.238 104.886 1.00 21.57  ? 2249 ILE A CG2   1 
ATOM   2854 C  CD1   . ILE A 1 458 ? 116.791 105.905 106.112 1.00 37.95  ? 2249 ILE A CD1   1 
ATOM   2855 N  N     . GLN A 1 459 ? 112.832 103.733 103.035 1.00 21.71  ? 2250 GLN A N     1 
ATOM   2856 C  CA    . GLN A 1 459 ? 112.090 102.796 102.200 1.00 22.27  ? 2250 GLN A CA    1 
ATOM   2857 C  C     . GLN A 1 459 ? 112.170 103.177 100.730 1.00 25.87  ? 2250 GLN A C     1 
ATOM   2858 O  O     . GLN A 1 459 ? 112.295 102.305 99.864  1.00 31.85  ? 2250 GLN A O     1 
ATOM   2859 C  CB    . GLN A 1 459 ? 110.638 102.732 102.656 1.00 21.70  ? 2250 GLN A CB    1 
ATOM   2860 C  CG    . GLN A 1 459 ? 110.471 102.255 104.075 1.00 19.79  ? 2250 GLN A CG    1 
ATOM   2861 C  CD    . GLN A 1 459 ? 109.061 102.430 104.565 1.00 20.68  ? 2250 GLN A CD    1 
ATOM   2862 O  OE1   . GLN A 1 459 ? 108.338 103.310 104.101 1.00 22.01  ? 2250 GLN A OE1   1 
ATOM   2863 N  NE2   . GLN A 1 459 ? 108.653 101.587 105.498 1.00 21.39  ? 2250 GLN A NE2   1 
ATOM   2864 N  N     . ASN A 1 460 ? 112.095 104.469 100.426 1.00 24.86  ? 2251 ASN A N     1 
ATOM   2865 C  CA    . ASN A 1 460 ? 112.158 104.937 99.043  1.00 23.98  ? 2251 ASN A CA    1 
ATOM   2866 C  C     . ASN A 1 460 ? 113.598 105.108 98.579  1.00 24.44  ? 2251 ASN A C     1 
ATOM   2867 O  O     . ASN A 1 460 ? 113.986 106.150 98.055  1.00 33.65  ? 2251 ASN A O     1 
ATOM   2868 C  CB    . ASN A 1 460 ? 111.379 106.237 98.898  1.00 27.35  ? 2251 ASN A CB    1 
ATOM   2869 C  CG    . ASN A 1 460 ? 109.920 106.085 99.265  1.00 26.43  ? 2251 ASN A CG    1 
ATOM   2870 O  OD1   . ASN A 1 460 ? 109.383 104.979 99.273  1.00 24.67  ? 2251 ASN A OD1   1 
ATOM   2871 N  ND2   . ASN A 1 460 ? 109.269 107.198 99.571  1.00 30.01  ? 2251 ASN A ND2   1 
ATOM   2872 N  N     . VAL A 1 461 ? 114.406 104.070 98.771  1.00 20.48  ? 2252 VAL A N     1 
ATOM   2873 C  CA    . VAL A 1 461 ? 115.773 104.030 98.261  1.00 24.53  ? 2252 VAL A CA    1 
ATOM   2874 C  C     . VAL A 1 461 ? 115.757 103.182 96.990  1.00 27.62  ? 2252 VAL A C     1 
ATOM   2875 O  O     . VAL A 1 461 ? 115.481 101.974 97.071  1.00 31.65  ? 2252 VAL A O     1 
ATOM   2876 C  CB    . VAL A 1 461 ? 116.752 103.465 99.296  1.00 20.49  ? 2252 VAL A CB    1 
ATOM   2877 C  CG1   . VAL A 1 461 ? 118.099 103.211 98.653  1.00 26.00  ? 2252 VAL A CG1   1 
ATOM   2878 C  CG2   . VAL A 1 461 ? 116.899 104.425 100.460 1.00 23.41  ? 2252 VAL A CG2   1 
ATOM   2879 N  N     . PRO A 1 462 ? 116.019 103.761 95.820  1.00 28.04  ? 2253 PRO A N     1 
ATOM   2880 C  CA    . PRO A 1 462 ? 115.925 102.990 94.575  1.00 29.04  ? 2253 PRO A CA    1 
ATOM   2881 C  C     . PRO A 1 462 ? 116.841 101.777 94.583  1.00 28.50  ? 2253 PRO A C     1 
ATOM   2882 O  O     . PRO A 1 462 ? 117.960 101.819 95.096  1.00 29.88  ? 2253 PRO A O     1 
ATOM   2883 C  CB    . PRO A 1 462 ? 116.340 104.004 93.504  1.00 34.33  ? 2253 PRO A CB    1 
ATOM   2884 C  CG    . PRO A 1 462 ? 116.003 105.325 94.102  1.00 34.90  ? 2253 PRO A CG    1 
ATOM   2885 C  CD    . PRO A 1 462 ? 116.259 105.190 95.571  1.00 30.21  ? 2253 PRO A CD    1 
ATOM   2886 N  N     . ARG A 1 463 ? 116.348 100.686 94.002  1.00 28.98  ? 2254 ARG A N     1 
ATOM   2887 C  CA    . ARG A 1 463 ? 117.096 99.442  93.964  1.00 30.80  ? 2254 ARG A CA    1 
ATOM   2888 C  C     . ARG A 1 463 ? 118.254 99.552  92.977  1.00 38.95  ? 2254 ARG A C     1 
ATOM   2889 O  O     . ARG A 1 463 ? 118.536 100.613 92.413  1.00 41.14  ? 2254 ARG A O     1 
ATOM   2890 C  CB    . ARG A 1 463 ? 116.181 98.279  93.589  1.00 32.47  ? 2254 ARG A CB    1 
ATOM   2891 C  CG    . ARG A 1 463 ? 114.887 98.692  92.918  1.00 30.95  ? 2254 ARG A CG    1 
ATOM   2892 C  CD    . ARG A 1 463 ? 114.065 97.479  92.537  1.00 32.30  ? 2254 ARG A CD    1 
ATOM   2893 N  NE    . ARG A 1 463 ? 113.601 96.734  93.699  1.00 38.80  ? 2254 ARG A NE    1 
ATOM   2894 C  CZ    . ARG A 1 463 ? 113.047 95.531  93.640  1.00 41.65  ? 2254 ARG A CZ    1 
ATOM   2895 N  NH1   . ARG A 1 463 ? 112.890 94.900  92.488  1.00 44.13  ? 2254 ARG A NH1   1 
ATOM   2896 N  NH2   . ARG A 1 463 ? 112.646 94.945  94.764  1.00 38.08  ? 2254 ARG A NH2   1 
ATOM   2897 N  N     . ASP A 1 464 ? 118.940 98.431  92.776  1.00 43.98  ? 2255 ASP A N     1 
ATOM   2898 C  CA    . ASP A 1 464 ? 120.051 98.396  91.838  1.00 48.52  ? 2255 ASP A CA    1 
ATOM   2899 C  C     . ASP A 1 464 ? 119.551 98.665  90.425  1.00 49.00  ? 2255 ASP A C     1 
ATOM   2900 O  O     . ASP A 1 464 ? 118.600 98.031  89.959  1.00 47.28  ? 2255 ASP A O     1 
ATOM   2901 C  CB    . ASP A 1 464 ? 120.755 97.038  91.899  1.00 51.76  ? 2255 ASP A CB    1 
ATOM   2902 C  CG    . ASP A 1 464 ? 121.292 96.711  93.283  1.00 51.50  ? 2255 ASP A CG    1 
ATOM   2903 O  OD1   . ASP A 1 464 ? 121.029 97.473  94.236  1.00 44.69  ? 2255 ASP A OD1   1 
ATOM   2904 O  OD2   . ASP A 1 464 ? 121.984 95.680  93.418  1.00 51.76  ? 2255 ASP A OD2   1 
ATOM   2905 N  N     . PHE A 1 465 ? 120.190 99.614  89.747  1.00 52.21  ? 2256 PHE A N     1 
ATOM   2906 C  CA    . PHE A 1 465 ? 119.882 99.922  88.358  1.00 53.40  ? 2256 PHE A CA    1 
ATOM   2907 C  C     . PHE A 1 465 ? 121.179 100.083 87.581  1.00 57.76  ? 2256 PHE A C     1 
ATOM   2908 O  O     . PHE A 1 465 ? 122.123 100.725 88.051  1.00 58.77  ? 2256 PHE A O     1 
ATOM   2909 C  CB    . PHE A 1 465 ? 119.005 101.187 88.225  1.00 55.81  ? 2256 PHE A CB    1 
ATOM   2910 C  CG    . PHE A 1 465 ? 119.714 102.479 88.550  1.00 59.31  ? 2256 PHE A CG    1 
ATOM   2911 C  CD1   . PHE A 1 465 ? 119.650 103.549 87.672  1.00 58.30  ? 2256 PHE A CD1   1 
ATOM   2912 C  CD2   . PHE A 1 465 ? 120.403 102.643 89.740  1.00 57.22  ? 2256 PHE A CD2   1 
ATOM   2913 C  CE1   . PHE A 1 465 ? 120.283 104.741 87.961  1.00 56.35  ? 2256 PHE A CE1   1 
ATOM   2914 C  CE2   . PHE A 1 465 ? 121.038 103.836 90.033  1.00 52.21  ? 2256 PHE A CE2   1 
ATOM   2915 C  CZ    . PHE A 1 465 ? 120.977 104.885 89.143  1.00 52.67  ? 2256 PHE A CZ    1 
ATOM   2916 N  N     . GLU A 1 466 ? 121.225 99.478  86.398  1.00 62.42  ? 2257 GLU A N     1 
ATOM   2917 C  CA    . GLU A 1 466 ? 122.419 99.516  85.570  1.00 67.31  ? 2257 GLU A CA    1 
ATOM   2918 C  C     . GLU A 1 466 ? 122.586 100.887 84.929  1.00 73.03  ? 2257 GLU A C     1 
ATOM   2919 O  O     . GLU A 1 466 ? 121.611 101.585 84.637  1.00 71.91  ? 2257 GLU A O     1 
ATOM   2920 C  CB    . GLU A 1 466 ? 122.354 98.440  84.486  1.00 69.00  ? 2257 GLU A CB    1 
ATOM   2921 N  N     . ILE A 1 467 ? 123.842 101.268 84.709  1.00 77.80  ? 2258 ILE A N     1 
ATOM   2922 C  CA    . ILE A 1 467 ? 124.173 102.537 84.079  1.00 77.34  ? 2258 ILE A CA    1 
ATOM   2923 C  C     . ILE A 1 467 ? 125.125 102.268 82.923  1.00 83.84  ? 2258 ILE A C     1 
ATOM   2924 O  O     . ILE A 1 467 ? 125.911 101.316 82.947  1.00 87.65  ? 2258 ILE A O     1 
ATOM   2925 C  CB    . ILE A 1 467 ? 124.777 103.539 85.092  1.00 74.71  ? 2258 ILE A CB    1 
ATOM   2926 C  CG1   . ILE A 1 467 ? 124.186 104.931 84.873  1.00 73.02  ? 2258 ILE A CG1   1 
ATOM   2927 C  CG2   . ILE A 1 467 ? 126.297 103.579 85.001  1.00 78.42  ? 2258 ILE A CG2   1 
ATOM   2928 C  CD1   . ILE A 1 467 ? 122.716 105.017 85.204  1.00 67.95  ? 2258 ILE A CD1   1 
ATOM   2929 N  N     . LYS A 1 468 ? 125.027 103.100 81.885  1.00 85.25  ? 2259 LYS A N     1 
ATOM   2930 C  CA    . LYS A 1 468 ? 125.826 102.932 80.672  1.00 87.83  ? 2259 LYS A CA    1 
ATOM   2931 C  C     . LYS A 1 468 ? 127.009 103.895 80.729  1.00 94.56  ? 2259 LYS A C     1 
ATOM   2932 O  O     . LYS A 1 468 ? 127.014 104.961 80.115  1.00 94.79  ? 2259 LYS A O     1 
ATOM   2933 C  CB    . LYS A 1 468 ? 124.969 103.157 79.430  1.00 85.07  ? 2259 LYS A CB    1 
ATOM   2934 N  N     . MET A 1 469 ? 128.036 103.496 81.476  1.00 97.16  ? 2260 MET A N     1 
ATOM   2935 C  CA    . MET A 1 469 ? 129.221 104.324 81.631  1.00 99.64  ? 2260 MET A CA    1 
ATOM   2936 C  C     . MET A 1 469 ? 130.318 103.751 80.746  1.00 108.50 ? 2260 MET A C     1 
ATOM   2937 O  O     . MET A 1 469 ? 130.866 102.686 81.071  1.00 109.22 ? 2260 MET A O     1 
ATOM   2938 C  CB    . MET A 1 469 ? 129.667 104.354 83.092  1.00 95.22  ? 2260 MET A CB    1 
ATOM   2939 C  CG    . MET A 1 469 ? 131.006 105.026 83.353  1.00 98.65  ? 2260 MET A CG    1 
ATOM   2940 S  SD    . MET A 1 469 ? 131.059 106.713 82.717  1.00 113.36 ? 2260 MET A SD    1 
ATOM   2941 C  CE    . MET A 1 469 ? 132.742 106.813 82.117  1.00 113.08 ? 2260 MET A CE    1 
ATOM   2942 N  N     . PRO A 1 470 ? 130.660 104.392 79.630  1.00 109.37 ? 2261 PRO A N     1 
ATOM   2943 C  CA    . PRO A 1 470 ? 131.621 103.792 78.697  1.00 108.99 ? 2261 PRO A CA    1 
ATOM   2944 C  C     . PRO A 1 470 ? 133.017 103.694 79.290  1.00 112.65 ? 2261 PRO A C     1 
ATOM   2945 O  O     . PRO A 1 470 ? 133.438 104.524 80.099  1.00 112.50 ? 2261 PRO A O     1 
ATOM   2946 C  CB    . PRO A 1 470 ? 131.594 104.747 77.498  1.00 107.43 ? 2261 PRO A CB    1 
ATOM   2947 C  CG    . PRO A 1 470 ? 131.125 106.046 78.061  1.00 104.76 ? 2261 PRO A CG    1 
ATOM   2948 C  CD    . PRO A 1 470 ? 130.160 105.693 79.153  1.00 103.92 ? 2261 PRO A CD    1 
ATOM   2949 N  N     . THR A 1 471 ? 133.742 102.665 78.865  1.00 116.12 ? 2262 THR A N     1 
ATOM   2950 C  CA    . THR A 1 471 ? 135.107 102.444 79.331  1.00 117.52 ? 2262 THR A CA    1 
ATOM   2951 C  C     . THR A 1 471 ? 135.956 101.790 78.246  1.00 117.48 ? 2262 THR A C     1 
ATOM   2952 O  O     . THR A 1 471 ? 135.431 101.154 77.332  1.00 116.95 ? 2262 THR A O     1 
ATOM   2953 C  CB    . THR A 1 471 ? 135.139 101.565 80.595  1.00 115.44 ? 2262 THR A CB    1 
ATOM   2954 O  OG1   . THR A 1 471 ? 134.533 102.270 81.686  1.00 113.73 ? 2262 THR A OG1   1 
ATOM   2955 C  CG2   . THR A 1 471 ? 136.572 101.209 80.960  1.00 110.29 ? 2262 THR A CG2   1 
ATOM   2956 N  N     . MET A 1 517 ? 129.703 95.300  81.641  1.00 96.30  ? 2308 MET A N     1 
ATOM   2957 C  CA    . MET A 1 517 ? 129.971 96.684  81.256  1.00 95.57  ? 2308 MET A CA    1 
ATOM   2958 C  C     . MET A 1 517 ? 129.205 97.710  82.115  1.00 93.27  ? 2308 MET A C     1 
ATOM   2959 O  O     . MET A 1 517 ? 129.799 98.702  82.539  1.00 92.34  ? 2308 MET A O     1 
ATOM   2960 C  CB    . MET A 1 517 ? 129.665 96.890  79.764  1.00 97.56  ? 2308 MET A CB    1 
ATOM   2961 C  CG    . MET A 1 517 ? 128.999 98.216  79.420  1.00 101.28 ? 2308 MET A CG    1 
ATOM   2962 S  SD    . MET A 1 517 ? 128.757 98.437  77.648  1.00 113.25 ? 2308 MET A SD    1 
ATOM   2963 C  CE    . MET A 1 517 ? 127.942 100.032 77.615  1.00 107.41 ? 2308 MET A CE    1 
ATOM   2964 N  N     . PRO A 1 518 ? 127.906 97.500  82.374  1.00 92.15  ? 2309 PRO A N     1 
ATOM   2965 C  CA    . PRO A 1 518 ? 127.200 98.421  83.272  1.00 90.48  ? 2309 PRO A CA    1 
ATOM   2966 C  C     . PRO A 1 518 ? 127.781 98.385  84.678  1.00 89.69  ? 2309 PRO A C     1 
ATOM   2967 O  O     . PRO A 1 518 ? 128.220 97.342  85.168  1.00 89.98  ? 2309 PRO A O     1 
ATOM   2968 C  CB    . PRO A 1 518 ? 125.756 97.907  83.250  1.00 88.15  ? 2309 PRO A CB    1 
ATOM   2969 C  CG    . PRO A 1 518 ? 125.641 97.173  81.973  1.00 86.94  ? 2309 PRO A CG    1 
ATOM   2970 C  CD    . PRO A 1 518 ? 126.970 96.517  81.795  1.00 92.00  ? 2309 PRO A CD    1 
ATOM   2971 N  N     . PHE A 1 519 ? 127.777 99.549  85.328  1.00 85.22  ? 2310 PHE A N     1 
ATOM   2972 C  CA    . PHE A 1 519 ? 128.317 99.665  86.676  1.00 82.73  ? 2310 PHE A CA    1 
ATOM   2973 C  C     . PHE A 1 519 ? 127.348 99.198  87.752  1.00 79.30  ? 2310 PHE A C     1 
ATOM   2974 O  O     . PHE A 1 519 ? 127.781 98.989  88.890  1.00 83.14  ? 2310 PHE A O     1 
ATOM   2975 C  CB    . PHE A 1 519 ? 128.732 101.110 86.956  1.00 81.77  ? 2310 PHE A CB    1 
ATOM   2976 C  CG    . PHE A 1 519 ? 130.145 101.422 86.555  1.00 89.98  ? 2310 PHE A CG    1 
ATOM   2977 C  CD1   . PHE A 1 519 ? 131.007 100.410 86.164  1.00 93.38  ? 2310 PHE A CD1   1 
ATOM   2978 C  CD2   . PHE A 1 519 ? 130.612 102.724 86.568  1.00 90.84  ? 2310 PHE A CD2   1 
ATOM   2979 C  CE1   . PHE A 1 519 ? 132.307 100.692 85.795  1.00 93.50  ? 2310 PHE A CE1   1 
ATOM   2980 C  CE2   . PHE A 1 519 ? 131.911 103.013 86.200  1.00 95.29  ? 2310 PHE A CE2   1 
ATOM   2981 C  CZ    . PHE A 1 519 ? 132.760 101.995 85.812  1.00 95.01  ? 2310 PHE A CZ    1 
ATOM   2982 N  N     . SER A 1 520 ? 126.068 99.027  87.420  1.00 74.56  ? 2311 SER A N     1 
ATOM   2983 C  CA    . SER A 1 520 ? 125.040 98.556  88.350  1.00 72.59  ? 2311 SER A CA    1 
ATOM   2984 C  C     . SER A 1 520 ? 125.101 99.330  89.670  1.00 66.66  ? 2311 SER A C     1 
ATOM   2985 O  O     . SER A 1 520 ? 125.412 98.795  90.734  1.00 63.16  ? 2311 SER A O     1 
ATOM   2986 C  CB    . SER A 1 520 ? 125.160 97.045  88.581  1.00 73.43  ? 2311 SER A CB    1 
ATOM   2987 O  OG    . SER A 1 520 ? 126.361 96.704  89.251  1.00 78.43  ? 2311 SER A OG    1 
ATOM   2988 N  N     . ILE A 1 521 ? 124.807 100.625 89.558  1.00 65.21  ? 2312 ILE A N     1 
ATOM   2989 C  CA    . ILE A 1 521 ? 124.872 101.532 90.698  1.00 61.48  ? 2312 ILE A CA    1 
ATOM   2990 C  C     . ILE A 1 521 ? 123.912 101.049 91.775  1.00 59.38  ? 2312 ILE A C     1 
ATOM   2991 O  O     . ILE A 1 521 ? 122.692 101.046 91.583  1.00 59.12  ? 2312 ILE A O     1 
ATOM   2992 C  CB    . ILE A 1 521 ? 124.556 102.980 90.284  1.00 54.88  ? 2312 ILE A CB    1 
ATOM   2993 C  CG1   . ILE A 1 521 ? 125.713 103.566 89.474  1.00 58.34  ? 2312 ILE A CG1   1 
ATOM   2994 C  CG2   . ILE A 1 521 ? 124.284 103.831 91.509  1.00 54.20  ? 2312 ILE A CG2   1 
ATOM   2995 C  CD1   . ILE A 1 521 ? 125.529 105.020 89.105  1.00 60.76  ? 2312 ILE A CD1   1 
ATOM   2996 N  N     . SER A 1 522 ? 124.463 100.639 92.913  1.00 55.76  ? 2313 SER A N     1 
ATOM   2997 C  CA    . SER A 1 522 ? 123.697 100.060 94.014  1.00 50.30  ? 2313 SER A CA    1 
ATOM   2998 C  C     . SER A 1 522 ? 123.997 100.870 95.270  1.00 48.39  ? 2313 SER A C     1 
ATOM   2999 O  O     . SER A 1 522 ? 125.034 100.673 95.909  1.00 51.82  ? 2313 SER A O     1 
ATOM   3000 C  CB    . SER A 1 522 ? 124.048 98.587  94.203  1.00 53.55  ? 2313 SER A CB    1 
ATOM   3001 O  OG    . SER A 1 522 ? 123.540 98.091  95.428  1.00 48.67  ? 2313 SER A OG    1 
ATOM   3002 N  N     . MET A 1 523 ? 123.099 101.790 95.615  1.00 44.18  ? 2314 MET A N     1 
ATOM   3003 C  CA    . MET A 1 523 ? 123.263 102.562 96.839  1.00 44.82  ? 2314 MET A CA    1 
ATOM   3004 C  C     . MET A 1 523 ? 122.591 101.912 98.040  1.00 43.16  ? 2314 MET A C     1 
ATOM   3005 O  O     . MET A 1 523 ? 122.849 102.328 99.174  1.00 44.54  ? 2314 MET A O     1 
ATOM   3006 C  CB    . MET A 1 523 ? 122.746 103.982 96.624  1.00 44.67  ? 2314 MET A CB    1 
ATOM   3007 C  CG    . MET A 1 523 ? 121.484 104.047 95.809  1.00 46.48  ? 2314 MET A CG    1 
ATOM   3008 S  SD    . MET A 1 523 ? 121.341 105.638 94.988  1.00 63.88  ? 2314 MET A SD    1 
ATOM   3009 C  CE    . MET A 1 523 ? 119.569 105.777 94.916  1.00 40.34  ? 2314 MET A CE    1 
ATOM   3010 N  N     . ARG A 1 524 ? 121.758 100.891 97.823  1.00 40.24  ? 2315 ARG A N     1 
ATOM   3011 C  CA    . ARG A 1 524 ? 121.360 100.032 98.931  1.00 32.19  ? 2315 ARG A CA    1 
ATOM   3012 C  C     . ARG A 1 524 ? 122.552 99.272  99.490  1.00 35.42  ? 2315 ARG A C     1 
ATOM   3013 O  O     . ARG A 1 524 ? 122.487 98.776  100.619 1.00 35.76  ? 2315 ARG A O     1 
ATOM   3014 C  CB    . ARG A 1 524 ? 120.274 99.056  98.487  1.00 26.71  ? 2315 ARG A CB    1 
ATOM   3015 C  CG    . ARG A 1 524 ? 118.951 99.714  98.179  1.00 23.28  ? 2315 ARG A CG    1 
ATOM   3016 C  CD    . ARG A 1 524 ? 117.883 98.681  97.897  1.00 21.79  ? 2315 ARG A CD    1 
ATOM   3017 N  NE    . ARG A 1 524 ? 116.549 99.263  97.958  1.00 22.21  ? 2315 ARG A NE    1 
ATOM   3018 C  CZ    . ARG A 1 524 ? 115.427 98.580  97.788  1.00 22.77  ? 2315 ARG A CZ    1 
ATOM   3019 N  NH1   . ARG A 1 524 ? 115.439 97.282  97.540  1.00 24.27  ? 2315 ARG A NH1   1 
ATOM   3020 N  NH2   . ARG A 1 524 ? 114.263 99.216  97.870  1.00 22.02  ? 2315 ARG A NH2   1 
ATOM   3021 N  N     . HIS A 1 525 ? 123.635 99.171  98.716  1.00 40.41  ? 2316 HIS A N     1 
ATOM   3022 C  CA    . HIS A 1 525 ? 124.903 98.684  99.246  1.00 42.59  ? 2316 HIS A CA    1 
ATOM   3023 C  C     . HIS A 1 525 ? 125.373 99.525  100.423 1.00 41.29  ? 2316 HIS A C     1 
ATOM   3024 O  O     . HIS A 1 525 ? 126.113 99.033  101.283 1.00 42.18  ? 2316 HIS A O     1 
ATOM   3025 C  CB    . HIS A 1 525 ? 125.958 98.696  98.140  1.00 47.79  ? 2316 HIS A CB    1 
ATOM   3026 C  CG    . HIS A 1 525 ? 126.980 97.611  98.256  1.00 52.79  ? 2316 HIS A CG    1 
ATOM   3027 N  ND1   . HIS A 1 525 ? 127.667 97.357  99.423  1.00 53.43  ? 2316 HIS A ND1   1 
ATOM   3028 C  CD2   . HIS A 1 525 ? 127.457 96.736  97.340  1.00 53.46  ? 2316 HIS A CD2   1 
ATOM   3029 C  CE1   . HIS A 1 525 ? 128.512 96.361  99.226  1.00 54.64  ? 2316 HIS A CE1   1 
ATOM   3030 N  NE2   . HIS A 1 525 ? 128.405 95.967  97.970  1.00 56.48  ? 2316 HIS A NE2   1 
ATOM   3031 N  N     . ALA A 1 526 ? 124.957 100.791 100.481 1.00 37.98  ? 2317 ALA A N     1 
ATOM   3032 C  CA    . ALA A 1 526 ? 125.408 101.685 101.538 1.00 36.17  ? 2317 ALA A CA    1 
ATOM   3033 C  C     . ALA A 1 526 ? 124.812 101.352 102.898 1.00 40.16  ? 2317 ALA A C     1 
ATOM   3034 O  O     . ALA A 1 526 ? 125.281 101.895 103.901 1.00 44.86  ? 2317 ALA A O     1 
ATOM   3035 C  CB    . ALA A 1 526 ? 125.075 103.133 101.177 1.00 40.29  ? 2317 ALA A CB    1 
ATOM   3036 N  N     . PHE A 1 527 ? 123.806 100.483 102.964 1.00 38.38  ? 2318 PHE A N     1 
ATOM   3037 C  CA    . PHE A 1 527 ? 123.142 100.168 104.230 1.00 30.73  ? 2318 PHE A CA    1 
ATOM   3038 C  C     . PHE A 1 527 ? 123.753 98.907  104.840 1.00 29.94  ? 2318 PHE A C     1 
ATOM   3039 O  O     . PHE A 1 527 ? 123.109 97.873  105.007 1.00 29.61  ? 2318 PHE A O     1 
ATOM   3040 C  CB    . PHE A 1 527 ? 121.640 100.023 104.015 1.00 25.34  ? 2318 PHE A CB    1 
ATOM   3041 C  CG    . PHE A 1 527 ? 120.967 101.297 103.600 1.00 27.40  ? 2318 PHE A CG    1 
ATOM   3042 C  CD1   . PHE A 1 527 ? 120.749 102.308 104.517 1.00 29.01  ? 2318 PHE A CD1   1 
ATOM   3043 C  CD2   . PHE A 1 527 ? 120.560 101.487 102.295 1.00 30.42  ? 2318 PHE A CD2   1 
ATOM   3044 C  CE1   . PHE A 1 527 ? 120.136 103.480 104.142 1.00 28.56  ? 2318 PHE A CE1   1 
ATOM   3045 C  CE2   . PHE A 1 527 ? 119.941 102.657 101.914 1.00 31.96  ? 2318 PHE A CE2   1 
ATOM   3046 C  CZ    . PHE A 1 527 ? 119.729 103.654 102.840 1.00 29.66  ? 2318 PHE A CZ    1 
ATOM   3047 N  N     . VAL A 1 528 ? 125.031 99.025  105.182 1.00 32.13  ? 2319 VAL A N     1 
ATOM   3048 C  CA    . VAL A 1 528 ? 125.794 97.933  105.780 1.00 34.87  ? 2319 VAL A CA    1 
ATOM   3049 C  C     . VAL A 1 528 ? 125.374 97.778  107.239 1.00 36.85  ? 2319 VAL A C     1 
ATOM   3050 O  O     . VAL A 1 528 ? 125.040 98.775  107.896 1.00 38.68  ? 2319 VAL A O     1 
ATOM   3051 C  CB    . VAL A 1 528 ? 127.308 98.182  105.637 1.00 38.13  ? 2319 VAL A CB    1 
ATOM   3052 C  CG1   . VAL A 1 528 ? 127.795 99.220  106.640 1.00 38.39  ? 2319 VAL A CG1   1 
ATOM   3053 C  CG2   . VAL A 1 528 ? 128.096 96.885  105.764 1.00 38.89  ? 2319 VAL A CG2   1 
ATOM   3054 N  N     . PRO A 1 529 ? 125.333 96.563  107.775 1.00 36.40  ? 2320 PRO A N     1 
ATOM   3055 C  CA    . PRO A 1 529 ? 125.077 96.375  109.206 1.00 37.40  ? 2320 PRO A CA    1 
ATOM   3056 C  C     . PRO A 1 529 ? 126.347 96.616  110.016 1.00 40.60  ? 2320 PRO A C     1 
ATOM   3057 O  O     . PRO A 1 529 ? 127.385 97.012  109.490 1.00 42.55  ? 2320 PRO A O     1 
ATOM   3058 C  CB    . PRO A 1 529 ? 124.628 94.916  109.288 1.00 36.84  ? 2320 PRO A CB    1 
ATOM   3059 C  CG    . PRO A 1 529 ? 125.297 94.266  108.139 1.00 35.46  ? 2320 PRO A CG    1 
ATOM   3060 C  CD    . PRO A 1 529 ? 125.294 95.286  107.043 1.00 34.81  ? 2320 PRO A CD    1 
ATOM   3061 N  N     . PHE A 1 530 ? 126.246 96.371  111.321 1.00 40.63  ? 2321 PHE A N     1 
ATOM   3062 C  CA    . PHE A 1 530 ? 127.398 96.544  112.188 1.00 43.06  ? 2321 PHE A CA    1 
ATOM   3063 C  C     . PHE A 1 530 ? 128.446 95.475  111.885 1.00 47.93  ? 2321 PHE A C     1 
ATOM   3064 O  O     . PHE A 1 530 ? 128.113 94.391  111.398 1.00 47.68  ? 2321 PHE A O     1 
ATOM   3065 C  CB    . PHE A 1 530 ? 126.990 96.485  113.660 1.00 44.98  ? 2321 PHE A CB    1 
ATOM   3066 C  CG    . PHE A 1 530 ? 126.343 95.191  114.071 1.00 44.06  ? 2321 PHE A CG    1 
ATOM   3067 C  CD1   . PHE A 1 530 ? 124.969 95.050  114.041 1.00 41.59  ? 2321 PHE A CD1   1 
ATOM   3068 C  CD2   . PHE A 1 530 ? 127.107 94.125  114.513 1.00 49.16  ? 2321 PHE A CD2   1 
ATOM   3069 C  CE1   . PHE A 1 530 ? 124.370 93.869  114.426 1.00 42.95  ? 2321 PHE A CE1   1 
ATOM   3070 C  CE2   . PHE A 1 530 ? 126.513 92.940  114.898 1.00 50.44  ? 2321 PHE A CE2   1 
ATOM   3071 C  CZ    . PHE A 1 530 ? 125.143 92.813  114.854 1.00 46.18  ? 2321 PHE A CZ    1 
ATOM   3072 N  N     . PRO A 1 531 ? 129.723 95.766  112.138 1.00 52.45  ? 2322 PRO A N     1 
ATOM   3073 C  CA    . PRO A 1 531 ? 130.764 94.760  111.898 1.00 53.01  ? 2322 PRO A CA    1 
ATOM   3074 C  C     . PRO A 1 531 ? 130.497 93.493  112.694 1.00 51.47  ? 2322 PRO A C     1 
ATOM   3075 O  O     . PRO A 1 531 ? 130.126 93.539  113.869 1.00 49.44  ? 2322 PRO A O     1 
ATOM   3076 C  CB    . PRO A 1 531 ? 132.046 95.461  112.360 1.00 55.58  ? 2322 PRO A CB    1 
ATOM   3077 C  CG    . PRO A 1 531 ? 131.745 96.915  112.223 1.00 56.31  ? 2322 PRO A CG    1 
ATOM   3078 C  CD    . PRO A 1 531 ? 130.289 97.061  112.552 1.00 51.70  ? 2322 PRO A CD    1 
ATOM   3079 N  N     . GLY A 1 532 ? 130.697 92.351  112.041 1.00 51.80  ? 2323 GLY A N     1 
ATOM   3080 C  CA    . GLY A 1 532 ? 130.342 91.077  112.622 1.00 53.42  ? 2323 GLY A CA    1 
ATOM   3081 C  C     . GLY A 1 532 ? 128.881 90.709  112.501 1.00 49.84  ? 2323 GLY A C     1 
ATOM   3082 O  O     . GLY A 1 532 ? 128.479 89.665  113.029 1.00 50.66  ? 2323 GLY A O     1 
ATOM   3083 N  N     . GLY A 1 533 ? 128.073 91.533  111.835 1.00 45.10  ? 2324 GLY A N     1 
ATOM   3084 C  CA    . GLY A 1 533 ? 126.674 91.254  111.616 1.00 42.02  ? 2324 GLY A CA    1 
ATOM   3085 C  C     . GLY A 1 533 ? 126.351 91.078  110.141 1.00 39.91  ? 2324 GLY A C     1 
ATOM   3086 O  O     . GLY A 1 533 ? 127.218 91.095  109.271 1.00 49.38  ? 2324 GLY A O     1 
ATOM   3087 N  N     . SER A 1 534 ? 125.059 90.908  109.875 1.00 34.31  ? 2325 SER A N     1 
ATOM   3088 C  CA    . SER A 1 534 ? 124.597 90.689  108.513 1.00 36.22  ? 2325 SER A CA    1 
ATOM   3089 C  C     . SER A 1 534 ? 123.113 91.011  108.429 1.00 29.56  ? 2325 SER A C     1 
ATOM   3090 O  O     . SER A 1 534 ? 122.348 90.675  109.335 1.00 29.01  ? 2325 SER A O     1 
ATOM   3091 C  CB    . SER A 1 534 ? 124.853 89.246  108.064 1.00 40.79  ? 2325 SER A CB    1 
ATOM   3092 O  OG    . SER A 1 534 ? 123.678 88.462  108.163 1.00 41.21  ? 2325 SER A OG    1 
ATOM   3093 N  N     . ILE A 1 535 ? 122.719 91.668  107.337 1.00 29.67  ? 2326 ILE A N     1 
ATOM   3094 C  CA    . ILE A 1 535 ? 121.308 91.913  107.084 1.00 25.29  ? 2326 ILE A CA    1 
ATOM   3095 C  C     . ILE A 1 535 ? 120.614 90.590  106.803 1.00 24.12  ? 2326 ILE A C     1 
ATOM   3096 O  O     . ILE A 1 535 ? 121.118 89.749  106.046 1.00 32.76  ? 2326 ILE A O     1 
ATOM   3097 C  CB    . ILE A 1 535 ? 121.127 92.897  105.916 1.00 26.50  ? 2326 ILE A CB    1 
ATOM   3098 C  CG1   . ILE A 1 535 ? 122.011 94.128  106.111 1.00 24.92  ? 2326 ILE A CG1   1 
ATOM   3099 C  CG2   . ILE A 1 535 ? 119.668 93.301  105.783 1.00 21.92  ? 2326 ILE A CG2   1 
ATOM   3100 C  CD1   . ILE A 1 535 ? 121.532 95.058  107.192 1.00 21.85  ? 2326 ILE A CD1   1 
ATOM   3101 N  N     . LEU A 1 536 ? 119.445 90.403  107.412 1.00 19.49  ? 2327 LEU A N     1 
ATOM   3102 C  CA    . LEU A 1 536 ? 118.707 89.145  107.366 1.00 24.74  ? 2327 LEU A CA    1 
ATOM   3103 C  C     . LEU A 1 536 ? 117.288 89.437  106.877 1.00 24.49  ? 2327 LEU A C     1 
ATOM   3104 O  O     . LEU A 1 536 ? 116.287 89.120  107.516 1.00 26.43  ? 2327 LEU A O     1 
ATOM   3105 C  CB    . LEU A 1 536 ? 118.767 88.438  108.726 1.00 28.47  ? 2327 LEU A CB    1 
ATOM   3106 C  CG    . LEU A 1 536 ? 118.207 87.024  108.928 1.00 31.67  ? 2327 LEU A CG    1 
ATOM   3107 C  CD1   . LEU A 1 536 ? 119.105 86.289  109.892 1.00 34.67  ? 2327 LEU A CD1   1 
ATOM   3108 C  CD2   . LEU A 1 536 ? 116.800 87.021  109.493 1.00 33.63  ? 2327 LEU A CD2   1 
ATOM   3109 N  N     . ALA A 1 537 ? 117.212 90.107  105.731 1.00 23.39  ? 2328 ALA A N     1 
ATOM   3110 C  CA    . ALA A 1 537 ? 115.926 90.579  105.240 1.00 20.94  ? 2328 ALA A CA    1 
ATOM   3111 C  C     . ALA A 1 537 ? 114.985 89.406  105.009 1.00 20.62  ? 2328 ALA A C     1 
ATOM   3112 O  O     . ALA A 1 537 ? 115.409 88.299  104.682 1.00 29.03  ? 2328 ALA A O     1 
ATOM   3113 C  CB    . ALA A 1 537 ? 116.107 91.372  103.949 1.00 23.30  ? 2328 ALA A CB    1 
ATOM   3114 N  N     . ALA A 1 538 ? 113.694 89.641  105.218 1.00 20.17  ? 2329 ALA A N     1 
ATOM   3115 C  CA    . ALA A 1 538 ? 112.701 88.571  105.097 1.00 24.47  ? 2329 ALA A CA    1 
ATOM   3116 C  C     . ALA A 1 538 ? 111.504 89.125  104.331 1.00 24.56  ? 2329 ALA A C     1 
ATOM   3117 O  O     . ALA A 1 538 ? 110.565 89.664  104.922 1.00 24.24  ? 2329 ALA A O     1 
ATOM   3118 C  CB    . ALA A 1 538 ? 112.308 88.034  106.462 1.00 22.46  ? 2329 ALA A CB    1 
ATOM   3119 N  N     . ASP A 1 539 ? 111.542 88.973  103.014 1.00 23.59  ? 2330 ASP A N     1 
ATOM   3120 C  CA    . ASP A 1 539 ? 110.505 89.478  102.130 1.00 24.88  ? 2330 ASP A CA    1 
ATOM   3121 C  C     . ASP A 1 539 ? 109.471 88.391  101.887 1.00 25.20  ? 2330 ASP A C     1 
ATOM   3122 O  O     . ASP A 1 539 ? 109.820 87.276  101.488 1.00 32.18  ? 2330 ASP A O     1 
ATOM   3123 C  CB    . ASP A 1 539 ? 111.111 89.941  100.804 1.00 27.89  ? 2330 ASP A CB    1 
ATOM   3124 C  CG    . ASP A 1 539 ? 110.062 90.266  99.763  1.00 30.29  ? 2330 ASP A CG    1 
ATOM   3125 O  OD1   . ASP A 1 539 ? 109.592 91.421  99.722  1.00 29.49  ? 2330 ASP A OD1   1 
ATOM   3126 O  OD2   . ASP A 1 539 ? 109.712 89.359  98.983  1.00 33.25  ? 2330 ASP A OD2   1 
ATOM   3127 N  N     . TYR A 1 540 ? 108.206 88.712  102.134 1.00 23.21  ? 2331 TYR A N     1 
ATOM   3128 C  CA    . TYR A 1 540 ? 107.136 87.778  101.824 1.00 24.03  ? 2331 TYR A CA    1 
ATOM   3129 C  C     . TYR A 1 540 ? 107.088 87.512  100.326 1.00 30.96  ? 2331 TYR A C     1 
ATOM   3130 O  O     . TYR A 1 540 ? 107.188 88.435  99.513  1.00 30.49  ? 2331 TYR A O     1 
ATOM   3131 C  CB    . TYR A 1 540 ? 105.788 88.338  102.280 1.00 21.77  ? 2331 TYR A CB    1 
ATOM   3132 C  CG    . TYR A 1 540 ? 105.393 88.018  103.702 1.00 24.34  ? 2331 TYR A CG    1 
ATOM   3133 C  CD1   . TYR A 1 540 ? 104.971 86.745  104.058 1.00 25.31  ? 2331 TYR A CD1   1 
ATOM   3134 C  CD2   . TYR A 1 540 ? 105.406 89.000  104.682 1.00 24.57  ? 2331 TYR A CD2   1 
ATOM   3135 C  CE1   . TYR A 1 540 ? 104.597 86.455  105.355 1.00 25.01  ? 2331 TYR A CE1   1 
ATOM   3136 C  CE2   . TYR A 1 540 ? 105.027 88.721  105.977 1.00 22.49  ? 2331 TYR A CE2   1 
ATOM   3137 C  CZ    . TYR A 1 540 ? 104.629 87.448  106.309 1.00 25.09  ? 2331 TYR A CZ    1 
ATOM   3138 O  OH    . TYR A 1 540 ? 104.256 87.172  107.603 1.00 30.37  ? 2331 TYR A OH    1 
ATOM   3139 N  N     . SER A 1 541 ? 106.930 86.240  99.958  1.00 30.40  ? 2332 SER A N     1 
ATOM   3140 C  CA    . SER A 1 541 ? 106.495 85.915  98.606  1.00 25.58  ? 2332 SER A CA    1 
ATOM   3141 C  C     . SER A 1 541 ? 105.161 86.616  98.411  1.00 26.72  ? 2332 SER A C     1 
ATOM   3142 O  O     . SER A 1 541 ? 104.472 86.880  99.401  1.00 29.49  ? 2332 SER A O     1 
ATOM   3143 C  CB    . SER A 1 541 ? 106.379 84.404  98.404  1.00 32.59  ? 2332 SER A CB    1 
ATOM   3144 O  OG    . SER A 1 541 ? 105.342 84.086  97.493  1.00 31.39  ? 2332 SER A OG    1 
ATOM   3145 N  N     . GLN A 1 542 ? 104.763 86.871  97.161  1.00 27.41  ? 2333 GLN A N     1 
ATOM   3146 C  CA    . GLN A 1 542 ? 103.864 87.980  96.851  1.00 25.70  ? 2333 GLN A CA    1 
ATOM   3147 C  C     . GLN A 1 542 ? 102.714 88.065  97.843  1.00 22.79  ? 2333 GLN A C     1 
ATOM   3148 O  O     . GLN A 1 542 ? 101.804 87.234  97.826  1.00 22.69  ? 2333 GLN A O     1 
ATOM   3149 C  CB    . GLN A 1 542 ? 103.319 87.826  95.431  1.00 25.95  ? 2333 GLN A CB    1 
ATOM   3150 C  CG    . GLN A 1 542 ? 103.001 86.388  95.044  1.00 28.34  ? 2333 GLN A CG    1 
ATOM   3151 C  CD    . GLN A 1 542 ? 104.144 85.700  94.328  1.00 32.28  ? 2333 GLN A CD    1 
ATOM   3152 O  OE1   . GLN A 1 542 ? 105.277 86.180  94.336  1.00 32.95  ? 2333 GLN A OE1   1 
ATOM   3153 N  NE2   . GLN A 1 542 ? 103.854 84.563  93.708  1.00 34.44  ? 2333 GLN A NE2   1 
ATOM   3154 N  N     . LEU A 1 543 ? 102.725 89.109  98.673  1.00 21.79  ? 2334 LEU A N     1 
ATOM   3155 C  CA    . LEU A 1 543 ? 101.958 89.081  99.914  1.00 19.30  ? 2334 LEU A CA    1 
ATOM   3156 C  C     . LEU A 1 543 ? 100.507 89.467  99.684  1.00 21.22  ? 2334 LEU A C     1 
ATOM   3157 O  O     . LEU A 1 543 ? 99.592  88.798  100.180 1.00 27.43  ? 2334 LEU A O     1 
ATOM   3158 C  CB    . LEU A 1 543 ? 102.599 90.007  100.946 1.00 17.39  ? 2334 LEU A CB    1 
ATOM   3159 C  CG    . LEU A 1 543 ? 101.950 90.015  102.330 1.00 19.43  ? 2334 LEU A CG    1 
ATOM   3160 C  CD1   . LEU A 1 543 ? 101.744 88.599  102.839 1.00 18.10  ? 2334 LEU A CD1   1 
ATOM   3161 C  CD2   . LEU A 1 543 ? 102.790 90.819  103.303 1.00 24.64  ? 2334 LEU A CD2   1 
ATOM   3162 N  N     . GLU A 1 544 ? 100.277 90.552  98.947  1.00 19.76  ? 2335 GLU A N     1 
ATOM   3163 C  CA    . GLU A 1 544 ? 98.908  90.929  98.634  1.00 19.92  ? 2335 GLU A CA    1 
ATOM   3164 C  C     . GLU A 1 544 ? 98.222  89.854  97.807  1.00 23.43  ? 2335 GLU A C     1 
ATOM   3165 O  O     . GLU A 1 544 ? 97.006  89.683  97.909  1.00 26.36  ? 2335 GLU A O     1 
ATOM   3166 C  CB    . GLU A 1 544 ? 98.885  92.279  97.919  1.00 19.20  ? 2335 GLU A CB    1 
ATOM   3167 C  CG    . GLU A 1 544 ? 99.052  93.457  98.867  1.00 18.29  ? 2335 GLU A CG    1 
ATOM   3168 C  CD    . GLU A 1 544 ? 99.162  94.786  98.151  1.00 22.31  ? 2335 GLU A CD    1 
ATOM   3169 O  OE1   . GLU A 1 544 ? 99.248  94.790  96.906  1.00 23.17  ? 2335 GLU A OE1   1 
ATOM   3170 O  OE2   . GLU A 1 544 ? 99.171  95.830  98.832  1.00 24.11  ? 2335 GLU A OE2   1 
ATOM   3171 N  N     . LEU A 1 545 ? 98.986  89.080  97.033  1.00 22.12  ? 2336 LEU A N     1 
ATOM   3172 C  CA    . LEU A 1 545 ? 98.401  87.962  96.298  1.00 22.57  ? 2336 LEU A CA    1 
ATOM   3173 C  C     . LEU A 1 545 ? 97.927  86.859  97.241  1.00 26.15  ? 2336 LEU A C     1 
ATOM   3174 O  O     . LEU A 1 545 ? 96.821  86.329  97.081  1.00 31.86  ? 2336 LEU A O     1 
ATOM   3175 C  CB    . LEU A 1 545 ? 99.408  87.412  95.289  1.00 23.87  ? 2336 LEU A CB    1 
ATOM   3176 C  CG    . LEU A 1 545 ? 99.222  87.868  93.842  1.00 25.97  ? 2336 LEU A CG    1 
ATOM   3177 C  CD1   . LEU A 1 545 ? 100.122 87.073  92.917  1.00 30.24  ? 2336 LEU A CD1   1 
ATOM   3178 C  CD2   . LEU A 1 545 ? 97.768  87.741  93.418  1.00 29.07  ? 2336 LEU A CD2   1 
ATOM   3179 N  N     . ARG A 1 546 ? 98.753  86.489  98.226  1.00 25.24  ? 2337 ARG A N     1 
ATOM   3180 C  CA    . ARG A 1 546 ? 98.338  85.461  99.178  1.00 24.03  ? 2337 ARG A CA    1 
ATOM   3181 C  C     . ARG A 1 546 ? 97.145  85.926  100.001 1.00 27.20  ? 2337 ARG A C     1 
ATOM   3182 O  O     . ARG A 1 546 ? 96.214  85.153  100.251 1.00 31.61  ? 2337 ARG A O     1 
ATOM   3183 C  CB    . ARG A 1 546 ? 99.496  85.075  100.100 1.00 22.80  ? 2337 ARG A CB    1 
ATOM   3184 C  CG    . ARG A 1 546 ? 100.835 84.927  99.413  1.00 23.46  ? 2337 ARG A CG    1 
ATOM   3185 C  CD    . ARG A 1 546 ? 101.427 83.541  99.568  1.00 26.39  ? 2337 ARG A CD    1 
ATOM   3186 N  NE    . ARG A 1 546 ? 102.239 83.186  98.411  1.00 30.97  ? 2337 ARG A NE    1 
ATOM   3187 C  CZ    . ARG A 1 546 ? 102.846 82.019  98.246  1.00 38.21  ? 2337 ARG A CZ    1 
ATOM   3188 N  NH1   . ARG A 1 546 ? 102.748 81.056  99.146  1.00 36.88  ? 2337 ARG A NH1   1 
ATOM   3189 N  NH2   . ARG A 1 546 ? 103.567 81.812  97.149  1.00 42.05  ? 2337 ARG A NH2   1 
ATOM   3190 N  N     . ILE A 1 547 ? 97.153  87.188  100.430 1.00 23.66  ? 2338 ILE A N     1 
ATOM   3191 C  CA    . ILE A 1 547 ? 96.037  87.708  101.215 1.00 22.84  ? 2338 ILE A CA    1 
ATOM   3192 C  C     . ILE A 1 547 ? 94.777  87.796  100.363 1.00 28.47  ? 2338 ILE A C     1 
ATOM   3193 O  O     . ILE A 1 547 ? 93.662  87.559  100.847 1.00 35.73  ? 2338 ILE A O     1 
ATOM   3194 C  CB    . ILE A 1 547 ? 96.419  89.062  101.832 1.00 17.69  ? 2338 ILE A CB    1 
ATOM   3195 C  CG1   . ILE A 1 547 ? 97.633  88.878  102.735 1.00 16.52  ? 2338 ILE A CG1   1 
ATOM   3196 C  CG2   . ILE A 1 547 ? 95.264  89.642  102.616 1.00 18.99  ? 2338 ILE A CG2   1 
ATOM   3197 C  CD1   . ILE A 1 547 ? 97.888  90.033  103.630 1.00 18.69  ? 2338 ILE A CD1   1 
ATOM   3198 N  N     . LEU A 1 548 ? 94.930  88.132  99.081  1.00 24.99  ? 2339 LEU A N     1 
ATOM   3199 C  CA    . LEU A 1 548 ? 93.801  88.106  98.165  1.00 24.53  ? 2339 LEU A CA    1 
ATOM   3200 C  C     . LEU A 1 548 ? 93.216  86.708  98.074  1.00 28.42  ? 2339 LEU A C     1 
ATOM   3201 O  O     . LEU A 1 548 ? 92.015  86.514  98.279  1.00 32.75  ? 2339 LEU A O     1 
ATOM   3202 C  CB    . LEU A 1 548 ? 94.250  88.581  96.789  1.00 23.35  ? 2339 LEU A CB    1 
ATOM   3203 C  CG    . LEU A 1 548 ? 93.978  90.027  96.404  1.00 23.60  ? 2339 LEU A CG    1 
ATOM   3204 C  CD1   . LEU A 1 548 ? 94.444  90.219  94.989  1.00 31.31  ? 2339 LEU A CD1   1 
ATOM   3205 C  CD2   . LEU A 1 548 ? 92.507  90.346  96.533  1.00 22.32  ? 2339 LEU A CD2   1 
ATOM   3206 N  N     . ALA A 1 549 ? 94.064  85.716  97.791  1.00 28.07  ? 2340 ALA A N     1 
ATOM   3207 C  CA    . ALA A 1 549 ? 93.600  84.338  97.697  1.00 31.76  ? 2340 ALA A CA    1 
ATOM   3208 C  C     . ALA A 1 549 ? 92.968  83.872  99.000  1.00 38.11  ? 2340 ALA A C     1 
ATOM   3209 O  O     . ALA A 1 549 ? 92.067  83.027  98.985  1.00 44.09  ? 2340 ALA A O     1 
ATOM   3210 C  CB    . ALA A 1 549 ? 94.756  83.419  97.309  1.00 33.87  ? 2340 ALA A CB    1 
ATOM   3211 N  N     . HIS A 1 550 ? 93.429  84.405  100.131 1.00 33.80  ? 2341 HIS A N     1 
ATOM   3212 C  CA    . HIS A 1 550 ? 92.767  84.134  101.401 1.00 32.15  ? 2341 HIS A CA    1 
ATOM   3213 C  C     . HIS A 1 550 ? 91.345  84.680  101.397 1.00 34.51  ? 2341 HIS A C     1 
ATOM   3214 O  O     . HIS A 1 550 ? 90.377  83.931  101.569 1.00 41.60  ? 2341 HIS A O     1 
ATOM   3215 C  CB    . HIS A 1 550 ? 93.569  84.737  102.553 1.00 29.85  ? 2341 HIS A CB    1 
ATOM   3216 C  CG    . HIS A 1 550 ? 92.870  84.665  103.875 1.00 31.46  ? 2341 HIS A CG    1 
ATOM   3217 N  ND1   . HIS A 1 550 ? 92.375  83.488  104.392 1.00 32.77  ? 2341 HIS A ND1   1 
ATOM   3218 C  CD2   . HIS A 1 550 ? 92.582  85.625  104.785 1.00 33.81  ? 2341 HIS A CD2   1 
ATOM   3219 C  CE1   . HIS A 1 550 ? 91.814  83.725  105.563 1.00 31.31  ? 2341 HIS A CE1   1 
ATOM   3220 N  NE2   . HIS A 1 550 ? 91.926  85.014  105.825 1.00 34.37  ? 2341 HIS A NE2   1 
ATOM   3221 N  N     . LEU A 1 551 ? 91.200  85.988  101.209 1.00 29.97  ? 2342 LEU A N     1 
ATOM   3222 C  CA    . LEU A 1 551 ? 89.862  86.583  101.179 1.00 32.46  ? 2342 LEU A CA    1 
ATOM   3223 C  C     . LEU A 1 551 ? 89.304  86.696  99.763  1.00 37.58  ? 2342 LEU A C     1 
ATOM   3224 O  O     . LEU A 1 551 ? 88.817  87.748  99.360  1.00 40.61  ? 2342 LEU A O     1 
ATOM   3225 C  CB    . LEU A 1 551 ? 89.874  87.946  101.862 1.00 33.63  ? 2342 LEU A CB    1 
ATOM   3226 C  CG    . LEU A 1 551 ? 90.576  88.092  103.211 1.00 33.75  ? 2342 LEU A CG    1 
ATOM   3227 C  CD1   . LEU A 1 551 ? 91.835  88.917  103.067 1.00 25.87  ? 2342 LEU A CD1   1 
ATOM   3228 C  CD2   . LEU A 1 551 ? 89.640  88.709  104.239 1.00 32.68  ? 2342 LEU A CD2   1 
ATOM   3229 N  N     . SER A 1 552 ? 89.365  85.614  98.987  1.00 39.65  ? 2343 SER A N     1 
ATOM   3230 C  CA    . SER A 1 552 ? 88.555  85.523  97.774  1.00 44.15  ? 2343 SER A CA    1 
ATOM   3231 C  C     . SER A 1 552 ? 87.904  84.168  97.577  1.00 52.25  ? 2343 SER A C     1 
ATOM   3232 O  O     . SER A 1 552 ? 86.922  84.088  96.830  1.00 57.79  ? 2343 SER A O     1 
ATOM   3233 C  CB    . SER A 1 552 ? 89.380  85.836  96.520  1.00 45.33  ? 2343 SER A CB    1 
ATOM   3234 O  OG    . SER A 1 552 ? 90.661  85.246  96.574  1.00 43.83  ? 2343 SER A OG    1 
ATOM   3235 N  N     . HIS A 1 553 ? 88.413  83.103  98.199  1.00 49.71  ? 2344 HIS A N     1 
ATOM   3236 C  CA    . HIS A 1 553 ? 88.006  81.730  97.905  1.00 52.59  ? 2344 HIS A CA    1 
ATOM   3237 C  C     . HIS A 1 553 ? 88.252  81.385  96.438  1.00 58.02  ? 2344 HIS A C     1 
ATOM   3238 O  O     . HIS A 1 553 ? 87.526  80.585  95.843  1.00 65.14  ? 2344 HIS A O     1 
ATOM   3239 C  CB    . HIS A 1 553 ? 86.546  81.484  98.293  1.00 56.66  ? 2344 HIS A CB    1 
ATOM   3240 C  CG    . HIS A 1 553 ? 86.155  82.120  99.591  1.00 61.62  ? 2344 HIS A CG    1 
ATOM   3241 N  ND1   . HIS A 1 553 ? 86.883  81.951  100.750 1.00 63.27  ? 2344 HIS A ND1   1 
ATOM   3242 C  CD2   . HIS A 1 553 ? 85.118  82.929  99.913  1.00 60.06  ? 2344 HIS A CD2   1 
ATOM   3243 C  CE1   . HIS A 1 553 ? 86.310  82.628  101.729 1.00 58.70  ? 2344 HIS A CE1   1 
ATOM   3244 N  NE2   . HIS A 1 553 ? 85.237  83.229  101.248 1.00 59.60  ? 2344 HIS A NE2   1 
ATOM   3245 N  N     . ASP A 1 554 ? 89.282  81.996  95.851  1.00 54.19  ? 2345 ASP A N     1 
ATOM   3246 C  CA    . ASP A 1 554 ? 89.723  81.675  94.499  1.00 55.53  ? 2345 ASP A CA    1 
ATOM   3247 C  C     . ASP A 1 554 ? 90.434  80.333  94.461  1.00 57.68  ? 2345 ASP A C     1 
ATOM   3248 O  O     . ASP A 1 554 ? 91.641  80.268  94.707  1.00 58.17  ? 2345 ASP A O     1 
ATOM   3249 C  CB    . ASP A 1 554 ? 90.662  82.757  93.964  1.00 52.50  ? 2345 ASP A CB    1 
ATOM   3250 C  CG    . ASP A 1 554 ? 90.407  83.085  92.509  1.00 56.57  ? 2345 ASP A CG    1 
ATOM   3251 O  OD1   . ASP A 1 554 ? 90.774  82.262  91.643  1.00 63.46  ? 2345 ASP A OD1   1 
ATOM   3252 O  OD2   . ASP A 1 554 ? 89.873  84.171  92.223  1.00 54.87  ? 2345 ASP A OD2   1 
ATOM   3253 N  N     . ARG A 1 555 ? 89.704  79.264  94.133  1.00 58.05  ? 2346 ARG A N     1 
ATOM   3254 C  CA    . ARG A 1 555 ? 90.309  77.936  94.099  1.00 61.15  ? 2346 ARG A CA    1 
ATOM   3255 C  C     . ARG A 1 555 ? 91.529  77.909  93.188  1.00 62.75  ? 2346 ARG A C     1 
ATOM   3256 O  O     . ARG A 1 555 ? 92.553  77.301  93.524  1.00 63.22  ? 2346 ARG A O     1 
ATOM   3257 C  CB    . ARG A 1 555 ? 89.277  76.902  93.645  1.00 64.29  ? 2346 ARG A CB    1 
ATOM   3258 C  CG    . ARG A 1 555 ? 87.838  77.265  93.982  1.00 66.86  ? 2346 ARG A CG    1 
ATOM   3259 C  CD    . ARG A 1 555 ? 87.577  77.202  95.480  1.00 70.16  ? 2346 ARG A CD    1 
ATOM   3260 N  NE    . ARG A 1 555 ? 87.691  75.845  96.000  1.00 76.77  ? 2346 ARG A NE    1 
ATOM   3261 C  CZ    . ARG A 1 555 ? 87.463  75.506  97.262  1.00 75.57  ? 2346 ARG A CZ    1 
ATOM   3262 N  NH1   . ARG A 1 555 ? 87.105  76.404  98.165  1.00 75.89  ? 2346 ARG A NH1   1 
ATOM   3263 N  NH2   . ARG A 1 555 ? 87.598  74.234  97.627  1.00 76.26  ? 2346 ARG A NH2   1 
ATOM   3264 N  N     . ARG A 1 556 ? 91.446  78.583  92.038  1.00 59.45  ? 2347 ARG A N     1 
ATOM   3265 C  CA    . ARG A 1 556 ? 92.585  78.645  91.129  1.00 58.14  ? 2347 ARG A CA    1 
ATOM   3266 C  C     . ARG A 1 556 ? 93.771  79.353  91.770  1.00 55.58  ? 2347 ARG A C     1 
ATOM   3267 O  O     . ARG A 1 556 ? 94.903  78.860  91.710  1.00 56.01  ? 2347 ARG A O     1 
ATOM   3268 C  CB    . ARG A 1 556 ? 92.180  79.349  89.834  1.00 60.14  ? 2347 ARG A CB    1 
ATOM   3269 C  CG    . ARG A 1 556 ? 93.263  79.360  88.771  1.00 65.07  ? 2347 ARG A CG    1 
ATOM   3270 C  CD    . ARG A 1 556 ? 92.993  78.313  87.706  1.00 68.99  ? 2347 ARG A CD    1 
ATOM   3271 N  NE    . ARG A 1 556 ? 91.865  78.677  86.858  1.00 69.46  ? 2347 ARG A NE    1 
ATOM   3272 C  CZ    . ARG A 1 556 ? 91.978  79.186  85.639  1.00 70.54  ? 2347 ARG A CZ    1 
ATOM   3273 N  NH1   . ARG A 1 556 ? 93.161  79.402  85.088  1.00 71.54  ? 2347 ARG A NH1   1 
ATOM   3274 N  NH2   . ARG A 1 556 ? 90.877  79.484  84.955  1.00 69.35  ? 2347 ARG A NH2   1 
ATOM   3275 N  N     . LEU A 1 557 ? 93.533  80.508  92.396  1.00 54.68  ? 2348 LEU A N     1 
ATOM   3276 C  CA    . LEU A 1 557 ? 94.634  81.266  92.982  1.00 52.46  ? 2348 LEU A CA    1 
ATOM   3277 C  C     . LEU A 1 557 ? 95.231  80.543  94.183  1.00 54.26  ? 2348 LEU A C     1 
ATOM   3278 O  O     . LEU A 1 557 ? 96.454  80.536  94.359  1.00 54.22  ? 2348 LEU A O     1 
ATOM   3279 C  CB    . LEU A 1 557 ? 94.165  82.667  93.371  1.00 49.04  ? 2348 LEU A CB    1 
ATOM   3280 C  CG    . LEU A 1 557 ? 95.265  83.698  93.629  1.00 42.14  ? 2348 LEU A CG    1 
ATOM   3281 C  CD1   . LEU A 1 557 ? 96.384  83.562  92.612  1.00 40.93  ? 2348 LEU A CD1   1 
ATOM   3282 C  CD2   . LEU A 1 557 ? 94.693  85.106  93.607  1.00 35.62  ? 2348 LEU A CD2   1 
ATOM   3283 N  N     . ILE A 1 558 ? 94.390  79.934  95.023  1.00 55.83  ? 2349 ILE A N     1 
ATOM   3284 C  CA    . ILE A 1 558 ? 94.904  79.164  96.152  1.00 55.19  ? 2349 ILE A CA    1 
ATOM   3285 C  C     . ILE A 1 558 ? 95.731  77.984  95.657  1.00 57.43  ? 2349 ILE A C     1 
ATOM   3286 O  O     . ILE A 1 558 ? 96.807  77.694  96.193  1.00 57.32  ? 2349 ILE A O     1 
ATOM   3287 C  CB    . ILE A 1 558 ? 93.757  78.704  97.074  1.00 53.36  ? 2349 ILE A CB    1 
ATOM   3288 C  CG1   . ILE A 1 558 ? 93.190  79.880  97.875  1.00 47.98  ? 2349 ILE A CG1   1 
ATOM   3289 C  CG2   . ILE A 1 558 ? 94.230  77.612  98.019  1.00 52.75  ? 2349 ILE A CG2   1 
ATOM   3290 C  CD1   . ILE A 1 558 ? 91.701  80.075  97.736  1.00 53.03  ? 2349 ILE A CD1   1 
ATOM   3291 N  N     . GLN A 1 559 ? 95.247  77.290  94.624  1.00 55.97  ? 2350 GLN A N     1 
ATOM   3292 C  CA    . GLN A 1 559 ? 95.994  76.164  94.074  1.00 57.95  ? 2350 GLN A CA    1 
ATOM   3293 C  C     . GLN A 1 559 ? 97.334  76.612  93.504  1.00 59.47  ? 2350 GLN A C     1 
ATOM   3294 O  O     . GLN A 1 559 ? 98.354  75.939  93.693  1.00 62.77  ? 2350 GLN A O     1 
ATOM   3295 C  CB    . GLN A 1 559 ? 95.160  75.463  93.002  1.00 60.65  ? 2350 GLN A CB    1 
ATOM   3296 C  CG    . GLN A 1 559 ? 95.947  74.531  92.100  1.00 62.27  ? 2350 GLN A CG    1 
ATOM   3297 C  CD    . GLN A 1 559 ? 95.186  74.165  90.842  1.00 69.98  ? 2350 GLN A CD    1 
ATOM   3298 O  OE1   . GLN A 1 559 ? 93.956  74.185  90.820  1.00 72.56  ? 2350 GLN A OE1   1 
ATOM   3299 N  NE2   . GLN A 1 559 ? 95.916  73.831  89.785  1.00 76.08  ? 2350 GLN A NE2   1 
ATOM   3300 N  N     . VAL A 1 560 ? 97.353  77.748  92.805  1.00 58.42  ? 2351 VAL A N     1 
ATOM   3301 C  CA    . VAL A 1 560 ? 98.593  78.232  92.206  1.00 57.40  ? 2351 VAL A CA    1 
ATOM   3302 C  C     . VAL A 1 560 ? 99.577  78.681  93.281  1.00 57.50  ? 2351 VAL A C     1 
ATOM   3303 O  O     . VAL A 1 560 ? 100.781 78.418  93.187  1.00 60.31  ? 2351 VAL A O     1 
ATOM   3304 C  CB    . VAL A 1 560 ? 98.293  79.362  91.203  1.00 54.16  ? 2351 VAL A CB    1 
ATOM   3305 C  CG1   . VAL A 1 560 ? 99.575  80.057  90.785  1.00 48.65  ? 2351 VAL A CG1   1 
ATOM   3306 C  CG2   . VAL A 1 560 ? 97.571  78.809  89.985  1.00 54.05  ? 2351 VAL A CG2   1 
ATOM   3307 N  N     . LEU A 1 561 ? 99.087  79.362  94.318  1.00 54.93  ? 2352 LEU A N     1 
ATOM   3308 C  CA    . LEU A 1 561 ? 99.979  79.914  95.332  1.00 52.03  ? 2352 LEU A CA    1 
ATOM   3309 C  C     . LEU A 1 561 ? 100.491 78.845  96.290  1.00 56.39  ? 2352 LEU A C     1 
ATOM   3310 O  O     . LEU A 1 561 ? 101.635 78.924  96.752  1.00 54.06  ? 2352 LEU A O     1 
ATOM   3311 C  CB    . LEU A 1 561 ? 99.265  81.025  96.100  1.00 43.33  ? 2352 LEU A CB    1 
ATOM   3312 C  CG    . LEU A 1 561 ? 99.104  82.343  95.340  1.00 36.75  ? 2352 LEU A CG    1 
ATOM   3313 C  CD1   . LEU A 1 561 ? 98.305  83.340  96.153  1.00 33.13  ? 2352 LEU A CD1   1 
ATOM   3314 C  CD2   . LEU A 1 561 ? 100.463 82.915  94.977  1.00 36.19  ? 2352 LEU A CD2   1 
ATOM   3315 N  N     . ASN A 1 562 ? 99.664  77.847  96.610  1.00 60.59  ? 2353 ASN A N     1 
ATOM   3316 C  CA    . ASN A 1 562 ? 100.086 76.807  97.545  1.00 61.06  ? 2353 ASN A CA    1 
ATOM   3317 C  C     . ASN A 1 562 ? 101.229 75.981  96.968  1.00 61.40  ? 2353 ASN A C     1 
ATOM   3318 O  O     . ASN A 1 562 ? 102.235 75.733  97.643  1.00 63.18  ? 2353 ASN A O     1 
ATOM   3319 C  CB    . ASN A 1 562 ? 98.900  75.913  97.905  1.00 56.18  ? 2353 ASN A CB    1 
ATOM   3320 C  CG    . ASN A 1 562 ? 98.221  76.338  99.190  1.00 56.22  ? 2353 ASN A CG    1 
ATOM   3321 O  OD1   . ASN A 1 562 ? 97.339  77.194  99.184  1.00 54.09  ? 2353 ASN A OD1   1 
ATOM   3322 N  ND2   . ASN A 1 562 ? 98.633  75.743  100.303 1.00 57.85  ? 2353 ASN A ND2   1 
ATOM   3323 N  N     . THR A 1 563 ? 101.092 75.546  95.717  1.00 58.70  ? 2354 THR A N     1 
ATOM   3324 C  CA    . THR A 1 563 ? 102.161 74.852  94.999  1.00 61.56  ? 2354 THR A CA    1 
ATOM   3325 C  C     . THR A 1 563 ? 102.870 75.904  94.153  1.00 62.63  ? 2354 THR A C     1 
ATOM   3326 O  O     . THR A 1 563 ? 102.416 76.256  93.064  1.00 63.93  ? 2354 THR A O     1 
ATOM   3327 C  CB    . THR A 1 563 ? 101.610 73.711  94.151  1.00 65.32  ? 2354 THR A CB    1 
ATOM   3328 O  OG1   . THR A 1 563 ? 100.566 74.201  93.301  1.00 68.00  ? 2354 THR A OG1   1 
ATOM   3329 C  CG2   . THR A 1 563 ? 101.053 72.609  95.039  1.00 65.42  ? 2354 THR A CG2   1 
ATOM   3330 N  N     . GLY A 1 564 ? 104.000 76.395  94.662  1.00 64.69  ? 2355 GLY A N     1 
ATOM   3331 C  CA    . GLY A 1 564 ? 104.665 77.571  94.130  1.00 66.17  ? 2355 GLY A CA    1 
ATOM   3332 C  C     . GLY A 1 564 ? 104.793 77.637  92.623  1.00 64.56  ? 2355 GLY A C     1 
ATOM   3333 O  O     . GLY A 1 564 ? 105.504 76.835  92.011  1.00 60.51  ? 2355 GLY A O     1 
ATOM   3334 N  N     . ALA A 1 565 ? 104.100 78.599  92.017  1.00 62.69  ? 2356 ALA A N     1 
ATOM   3335 C  CA    . ALA A 1 565 ? 104.107 78.784  90.574  1.00 60.45  ? 2356 ALA A CA    1 
ATOM   3336 C  C     . ALA A 1 565 ? 104.505 80.192  90.160  1.00 57.14  ? 2356 ALA A C     1 
ATOM   3337 O  O     . ALA A 1 565 ? 104.730 80.429  88.967  1.00 53.94  ? 2356 ALA A O     1 
ATOM   3338 C  CB    . ALA A 1 565 ? 102.732 78.443  89.989  1.00 59.68  ? 2356 ALA A CB    1 
ATOM   3339 N  N     . ASP A 1 566 ? 104.597 81.129  91.107  1.00 56.81  ? 2357 ASP A N     1 
ATOM   3340 C  CA    . ASP A 1 566 ? 105.066 82.490  90.849  1.00 51.39  ? 2357 ASP A CA    1 
ATOM   3341 C  C     . ASP A 1 566 ? 104.195 83.184  89.797  1.00 48.41  ? 2357 ASP A C     1 
ATOM   3342 O  O     . ASP A 1 566 ? 104.595 83.396  88.654  1.00 50.00  ? 2357 ASP A O     1 
ATOM   3343 C  CB    . ASP A 1 566 ? 106.541 82.493  90.436  1.00 52.78  ? 2357 ASP A CB    1 
ATOM   3344 C  CG    . ASP A 1 566 ? 107.297 83.653  91.033  1.00 52.18  ? 2357 ASP A CG    1 
ATOM   3345 O  OD1   . ASP A 1 566 ? 106.662 84.701  91.269  1.00 45.71  ? 2357 ASP A OD1   1 
ATOM   3346 O  OD2   . ASP A 1 566 ? 108.517 83.522  91.263  1.00 58.92  ? 2357 ASP A OD2   1 
ATOM   3347 N  N     . VAL A 1 567 ? 102.964 83.484  90.216  1.00 44.72  ? 2358 VAL A N     1 
ATOM   3348 C  CA    . VAL A 1 567 ? 101.935 84.096  89.376  1.00 41.95  ? 2358 VAL A CA    1 
ATOM   3349 C  C     . VAL A 1 567 ? 102.479 85.237  88.522  1.00 42.57  ? 2358 VAL A C     1 
ATOM   3350 O  O     . VAL A 1 567 ? 102.066 85.408  87.370  1.00 47.26  ? 2358 VAL A O     1 
ATOM   3351 C  CB    . VAL A 1 567 ? 100.763 84.598  90.236  1.00 39.04  ? 2358 VAL A CB    1 
ATOM   3352 C  CG1   . VAL A 1 567 ? 99.578  84.959  89.359  1.00 38.69  ? 2358 VAL A CG1   1 
ATOM   3353 C  CG2   . VAL A 1 567 ? 100.375 83.554  91.264  1.00 46.04  ? 2358 VAL A CG2   1 
ATOM   3354 N  N     . PHE A 1 568 ? 103.393 86.036  89.076  1.00 38.78  ? 2359 PHE A N     1 
ATOM   3355 C  CA    . PHE A 1 568 ? 103.959 87.143  88.308  1.00 36.75  ? 2359 PHE A CA    1 
ATOM   3356 C  C     . PHE A 1 568 ? 104.818 86.641  87.154  1.00 44.43  ? 2359 PHE A C     1 
ATOM   3357 O  O     . PHE A 1 568 ? 104.742 87.170  86.038  1.00 48.20  ? 2359 PHE A O     1 
ATOM   3358 C  CB    . PHE A 1 568 ? 104.768 88.057  89.225  1.00 34.22  ? 2359 PHE A CB    1 
ATOM   3359 C  CG    . PHE A 1 568 ? 103.948 88.712  90.293  1.00 29.42  ? 2359 PHE A CG    1 
ATOM   3360 C  CD1   . PHE A 1 568 ? 102.616 89.010  90.072  1.00 29.87  ? 2359 PHE A CD1   1 
ATOM   3361 C  CD2   . PHE A 1 568 ? 104.505 89.025  91.516  1.00 26.88  ? 2359 PHE A CD2   1 
ATOM   3362 C  CE1   . PHE A 1 568 ? 101.857 89.610  91.049  1.00 24.00  ? 2359 PHE A CE1   1 
ATOM   3363 C  CE2   . PHE A 1 568 ? 103.751 89.626  92.497  1.00 27.10  ? 2359 PHE A CE2   1 
ATOM   3364 C  CZ    . PHE A 1 568 ? 102.425 89.917  92.264  1.00 24.89  ? 2359 PHE A CZ    1 
ATOM   3365 N  N     . ARG A 1 569 ? 105.646 85.626  87.405  1.00 47.80  ? 2360 ARG A N     1 
ATOM   3366 C  CA    . ARG A 1 569 ? 106.435 85.031  86.333  1.00 46.34  ? 2360 ARG A CA    1 
ATOM   3367 C  C     . ARG A 1 569 ? 105.536 84.401  85.278  1.00 47.24  ? 2360 ARG A C     1 
ATOM   3368 O  O     . ARG A 1 569 ? 105.818 84.488  84.078  1.00 51.87  ? 2360 ARG A O     1 
ATOM   3369 C  CB    . ARG A 1 569 ? 107.402 83.996  86.907  1.00 47.97  ? 2360 ARG A CB    1 
ATOM   3370 C  CG    . ARG A 1 569 ? 108.827 84.495  87.039  1.00 49.09  ? 2360 ARG A CG    1 
ATOM   3371 C  CD    . ARG A 1 569 ? 109.746 83.419  87.586  1.00 50.30  ? 2360 ARG A CD    1 
ATOM   3372 N  NE    . ARG A 1 569 ? 111.132 83.643  87.194  1.00 58.65  ? 2360 ARG A NE    1 
ATOM   3373 C  CZ    . ARG A 1 569 ? 111.987 84.405  87.863  1.00 62.00  ? 2360 ARG A CZ    1 
ATOM   3374 N  NH1   . ARG A 1 569 ? 111.631 85.036  88.969  1.00 57.45  ? 2360 ARG A NH1   1 
ATOM   3375 N  NH2   . ARG A 1 569 ? 113.231 84.537  87.410  1.00 63.62  ? 2360 ARG A NH2   1 
ATOM   3376 N  N     . SER A 1 570 ? 104.447 83.759  85.708  1.00 44.09  ? 2361 SER A N     1 
ATOM   3377 C  CA    . SER A 1 570 ? 103.493 83.196  84.758  1.00 47.00  ? 2361 SER A CA    1 
ATOM   3378 C  C     . SER A 1 570 ? 102.854 84.285  83.906  1.00 48.52  ? 2361 SER A C     1 
ATOM   3379 O  O     . SER A 1 570 ? 102.663 84.107  82.698  1.00 52.19  ? 2361 SER A O     1 
ATOM   3380 C  CB    . SER A 1 570 ? 102.421 82.401  85.503  1.00 51.89  ? 2361 SER A CB    1 
ATOM   3381 O  OG    . SER A 1 570 ? 101.386 81.996  84.627  1.00 58.03  ? 2361 SER A OG    1 
ATOM   3382 N  N     . ILE A 1 571 ? 102.511 85.418  84.522  1.00 47.70  ? 2362 ILE A N     1 
ATOM   3383 C  CA    . ILE A 1 571 ? 101.929 86.532  83.778  1.00 46.62  ? 2362 ILE A CA    1 
ATOM   3384 C  C     . ILE A 1 571 ? 102.924 87.070  82.760  1.00 50.42  ? 2362 ILE A C     1 
ATOM   3385 O  O     . ILE A 1 571 ? 102.569 87.352  81.609  1.00 56.53  ? 2362 ILE A O     1 
ATOM   3386 C  CB    . ILE A 1 571 ? 101.460 87.630  84.749  1.00 42.83  ? 2362 ILE A CB    1 
ATOM   3387 C  CG1   . ILE A 1 571 ? 100.102 87.261  85.345  1.00 45.06  ? 2362 ILE A CG1   1 
ATOM   3388 C  CG2   . ILE A 1 571 ? 101.392 88.979  84.050  1.00 46.31  ? 2362 ILE A CG2   1 
ATOM   3389 C  CD1   . ILE A 1 571 ? 99.415  88.407  86.034  1.00 38.98  ? 2362 ILE A CD1   1 
ATOM   3390 N  N     . ALA A 1 572 ? 104.186 87.224  83.168  1.00 48.33  ? 2363 ALA A N     1 
ATOM   3391 C  CA    . ALA A 1 572 ? 105.208 87.700  82.241  1.00 50.31  ? 2363 ALA A CA    1 
ATOM   3392 C  C     . ALA A 1 572 ? 105.395 86.730  81.082  1.00 55.54  ? 2363 ALA A C     1 
ATOM   3393 O  O     . ALA A 1 572 ? 105.518 87.148  79.924  1.00 59.36  ? 2363 ALA A O     1 
ATOM   3394 C  CB    . ALA A 1 572 ? 106.529 87.913  82.979  1.00 50.39  ? 2363 ALA A CB    1 
ATOM   3395 N  N     . ALA A 1 573 ? 105.417 85.428  81.374  1.00 53.35  ? 2364 ALA A N     1 
ATOM   3396 C  CA    . ALA A 1 573 ? 105.564 84.429  80.321  1.00 55.54  ? 2364 ALA A CA    1 
ATOM   3397 C  C     . ALA A 1 573 ? 104.386 84.460  79.358  1.00 56.38  ? 2364 ALA A C     1 
ATOM   3398 O  O     . ALA A 1 573 ? 104.569 84.363  78.139  1.00 61.87  ? 2364 ALA A O     1 
ATOM   3399 C  CB    . ALA A 1 573 ? 105.712 83.040  80.938  1.00 58.23  ? 2364 ALA A CB    1 
ATOM   3400 N  N     . GLU A 1 574 ? 103.166 84.580  79.884  1.00 55.02  ? 2365 GLU A N     1 
ATOM   3401 C  CA    . GLU A 1 574 ? 101.990 84.620  79.022  1.00 58.97  ? 2365 GLU A CA    1 
ATOM   3402 C  C     . GLU A 1 574 ? 101.974 85.876  78.161  1.00 60.59  ? 2365 GLU A C     1 
ATOM   3403 O  O     . GLU A 1 574 ? 101.612 85.822  76.980  1.00 62.30  ? 2365 GLU A O     1 
ATOM   3404 C  CB    . GLU A 1 574 ? 100.720 84.529  79.867  1.00 62.48  ? 2365 GLU A CB    1 
ATOM   3405 C  CG    . GLU A 1 574 ? 99.448  84.310  79.064  1.00 66.13  ? 2365 GLU A CG    1 
ATOM   3406 C  CD    . GLU A 1 574 ? 98.631  85.577  78.911  1.00 65.12  ? 2365 GLU A CD    1 
ATOM   3407 O  OE1   . GLU A 1 574 ? 99.122  86.655  79.307  1.00 64.95  ? 2365 GLU A OE1   1 
ATOM   3408 O  OE2   . GLU A 1 574 ? 97.496  85.496  78.398  1.00 67.42  ? 2365 GLU A OE2   1 
ATOM   3409 N  N     . TRP A 1 575 ? 102.362 87.017  78.733  1.00 59.08  ? 2366 TRP A N     1 
ATOM   3410 C  CA    . TRP A 1 575 ? 102.309 88.275  77.995  1.00 59.13  ? 2366 TRP A CA    1 
ATOM   3411 C  C     . TRP A 1 575 ? 103.397 88.337  76.929  1.00 63.92  ? 2366 TRP A C     1 
ATOM   3412 O  O     . TRP A 1 575 ? 103.135 88.721  75.783  1.00 71.18  ? 2366 TRP A O     1 
ATOM   3413 C  CB    . TRP A 1 575 ? 102.416 89.447  78.976  1.00 59.14  ? 2366 TRP A CB    1 
ATOM   3414 C  CG    . TRP A 1 575 ? 102.864 90.756  78.388  1.00 61.42  ? 2366 TRP A CG    1 
ATOM   3415 C  CD1   . TRP A 1 575 ? 102.510 91.287  77.180  1.00 62.06  ? 2366 TRP A CD1   1 
ATOM   3416 C  CD2   . TRP A 1 575 ? 103.734 91.712  79.004  1.00 63.10  ? 2366 TRP A CD2   1 
ATOM   3417 N  NE1   . TRP A 1 575 ? 103.120 92.504  77.001  1.00 63.20  ? 2366 TRP A NE1   1 
ATOM   3418 C  CE2   . TRP A 1 575 ? 103.876 92.788  78.107  1.00 63.65  ? 2366 TRP A CE2   1 
ATOM   3419 C  CE3   . TRP A 1 575 ? 104.413 91.759  80.225  1.00 59.24  ? 2366 TRP A CE3   1 
ATOM   3420 C  CZ2   . TRP A 1 575 ? 104.665 93.899  78.394  1.00 64.05  ? 2366 TRP A CZ2   1 
ATOM   3421 C  CZ3   . TRP A 1 575 ? 105.195 92.861  80.508  1.00 54.98  ? 2366 TRP A CZ3   1 
ATOM   3422 C  CH2   . TRP A 1 575 ? 105.316 93.916  79.596  1.00 59.72  ? 2366 TRP A CH2   1 
ATOM   3423 N  N     . LYS A 1 576 ? 104.621 87.948  77.277  1.00 62.23  ? 2367 LYS A N     1 
ATOM   3424 C  CA    . LYS A 1 576 ? 105.748 88.050  76.360  1.00 63.30  ? 2367 LYS A CA    1 
ATOM   3425 C  C     . LYS A 1 576 ? 105.971 86.779  75.548  1.00 66.19  ? 2367 LYS A C     1 
ATOM   3426 O  O     . LYS A 1 576 ? 106.951 86.701  74.800  1.00 64.98  ? 2367 LYS A O     1 
ATOM   3427 C  CB    . LYS A 1 576 ? 107.020 88.410  77.131  1.00 60.15  ? 2367 LYS A CB    1 
ATOM   3428 C  CG    . LYS A 1 576 ? 107.105 89.878  77.516  1.00 58.70  ? 2367 LYS A CG    1 
ATOM   3429 C  CD    . LYS A 1 576 ? 107.121 90.772  76.288  1.00 57.14  ? 2367 LYS A CD    1 
ATOM   3430 C  CE    . LYS A 1 576 ? 107.429 92.213  76.658  1.00 57.20  ? 2367 LYS A CE    1 
ATOM   3431 N  NZ    . LYS A 1 576 ? 108.768 92.350  77.293  1.00 55.92  ? 2367 LYS A NZ    1 
ATOM   3432 N  N     . MET A 1 577 ? 105.087 85.789  75.677  1.00 66.10  ? 2368 MET A N     1 
ATOM   3433 C  CA    . MET A 1 577 ? 105.120 84.520  74.950  1.00 65.11  ? 2368 MET A CA    1 
ATOM   3434 C  C     . MET A 1 577 ? 106.409 83.732  75.168  1.00 66.50  ? 2368 MET A C     1 
ATOM   3435 O  O     . MET A 1 577 ? 106.654 82.750  74.457  1.00 68.95  ? 2368 MET A O     1 
ATOM   3436 C  CB    . MET A 1 577 ? 104.880 84.712  73.443  1.00 67.76  ? 2368 MET A CB    1 
ATOM   3437 C  CG    . MET A 1 577 ? 104.091 85.958  73.061  1.00 74.97  ? 2368 MET A CG    1 
ATOM   3438 S  SD    . MET A 1 577 ? 103.318 85.825  71.438  1.00 111.11 ? 2368 MET A SD    1 
ATOM   3439 C  CE    . MET A 1 577 ? 103.048 87.552  71.049  1.00 86.30  ? 2368 MET A CE    1 
ATOM   3440 N  N     . ILE A 1 578 ? 107.238 84.127  76.128  1.00 67.62  ? 2369 ILE A N     1 
ATOM   3441 C  CA    . ILE A 1 578 ? 108.473 83.415  76.420  1.00 66.63  ? 2369 ILE A CA    1 
ATOM   3442 C  C     . ILE A 1 578 ? 108.204 82.358  77.484  1.00 65.72  ? 2369 ILE A C     1 
ATOM   3443 O  O     . ILE A 1 578 ? 107.161 82.350  78.141  1.00 65.87  ? 2369 ILE A O     1 
ATOM   3444 C  CB    . ILE A 1 578 ? 109.596 84.372  76.861  1.00 65.77  ? 2369 ILE A CB    1 
ATOM   3445 C  CG1   . ILE A 1 578 ? 109.058 85.413  77.841  1.00 62.16  ? 2369 ILE A CG1   1 
ATOM   3446 C  CG2   . ILE A 1 578 ? 110.226 85.045  75.652  1.00 64.58  ? 2369 ILE A CG2   1 
ATOM   3447 C  CD1   . ILE A 1 578 ? 110.044 86.511  78.158  1.00 62.71  ? 2369 ILE A CD1   1 
ATOM   3448 N  N     . GLU A 1 579 ? 109.154 81.441  77.639  1.00 66.92  ? 2370 GLU A N     1 
ATOM   3449 C  CA    . GLU A 1 579 ? 109.044 80.426  78.673  1.00 65.58  ? 2370 GLU A CA    1 
ATOM   3450 C  C     . GLU A 1 579 ? 109.125 81.068  80.058  1.00 68.79  ? 2370 GLU A C     1 
ATOM   3451 O  O     . GLU A 1 579 ? 109.838 82.057  80.252  1.00 69.20  ? 2370 GLU A O     1 
ATOM   3452 C  CB    . GLU A 1 579 ? 110.146 79.382  78.517  1.00 64.44  ? 2370 GLU A CB    1 
ATOM   3453 N  N     . PRO A 1 580 ? 108.398 80.526  81.038  1.00 70.06  ? 2371 PRO A N     1 
ATOM   3454 C  CA    . PRO A 1 580 ? 108.403 81.131  82.381  1.00 66.25  ? 2371 PRO A CA    1 
ATOM   3455 C  C     . PRO A 1 580 ? 109.759 81.111  83.063  1.00 68.49  ? 2371 PRO A C     1 
ATOM   3456 O  O     . PRO A 1 580 ? 109.964 81.874  84.015  1.00 66.54  ? 2371 PRO A O     1 
ATOM   3457 C  CB    . PRO A 1 580 ? 107.379 80.285  83.152  1.00 63.15  ? 2371 PRO A CB    1 
ATOM   3458 C  CG    . PRO A 1 580 ? 106.535 79.641  82.099  1.00 66.27  ? 2371 PRO A CG    1 
ATOM   3459 C  CD    . PRO A 1 580 ? 107.451 79.402  80.941  1.00 69.36  ? 2371 PRO A CD    1 
ATOM   3460 N  N     . GLU A 1 581 ? 110.685 80.267  82.623  1.00 71.88  ? 2372 GLU A N     1 
ATOM   3461 C  CA    . GLU A 1 581 ? 112.001 80.173  83.239  1.00 71.88  ? 2372 GLU A CA    1 
ATOM   3462 C  C     . GLU A 1 581 ? 113.023 81.111  82.608  1.00 70.39  ? 2372 GLU A C     1 
ATOM   3463 O  O     . GLU A 1 581 ? 114.195 81.076  82.997  1.00 70.97  ? 2372 GLU A O     1 
ATOM   3464 C  CB    . GLU A 1 581 ? 112.514 78.731  83.167  1.00 68.86  ? 2372 GLU A CB    1 
ATOM   3465 N  N     . SER A 1 582 ? 112.615 81.944  81.655  1.00 67.82  ? 2373 SER A N     1 
ATOM   3466 C  CA    . SER A 1 582 ? 113.519 82.824  80.922  1.00 68.47  ? 2373 SER A CA    1 
ATOM   3467 C  C     . SER A 1 582 ? 112.986 84.251  80.912  1.00 69.99  ? 2373 SER A C     1 
ATOM   3468 O  O     . SER A 1 582 ? 112.939 84.920  79.878  1.00 69.13  ? 2373 SER A O     1 
ATOM   3469 C  CB    . SER A 1 582 ? 113.729 82.316  79.499  1.00 69.56  ? 2373 SER A CB    1 
ATOM   3470 O  OG    . SER A 1 582 ? 112.489 82.079  78.856  1.00 66.76  ? 2373 SER A OG    1 
ATOM   3471 N  N     . VAL A 1 583 ? 112.574 84.737  82.080  1.00 69.84  ? 2374 VAL A N     1 
ATOM   3472 C  CA    . VAL A 1 583 ? 112.024 86.078  82.236  1.00 67.35  ? 2374 VAL A CA    1 
ATOM   3473 C  C     . VAL A 1 583 ? 112.947 86.877  83.146  1.00 64.58  ? 2374 VAL A C     1 
ATOM   3474 O  O     . VAL A 1 583 ? 113.321 86.408  84.228  1.00 61.34  ? 2374 VAL A O     1 
ATOM   3475 C  CB    . VAL A 1 583 ? 110.589 86.040  82.795  1.00 63.63  ? 2374 VAL A CB    1 
ATOM   3476 C  CG1   . VAL A 1 583 ? 110.487 85.024  83.912  1.00 61.66  ? 2374 VAL A CG1   1 
ATOM   3477 C  CG2   . VAL A 1 583 ? 110.171 87.414  83.285  1.00 57.88  ? 2374 VAL A CG2   1 
ATOM   3478 N  N     . GLY A 1 584 ? 113.315 88.077  82.706  1.00 62.68  ? 2375 GLY A N     1 
ATOM   3479 C  CA    . GLY A 1 584 ? 114.225 88.907  83.464  1.00 62.28  ? 2375 GLY A CA    1 
ATOM   3480 C  C     . GLY A 1 584 ? 113.579 89.516  84.694  1.00 60.82  ? 2375 GLY A C     1 
ATOM   3481 O  O     . GLY A 1 584 ? 112.374 89.418  84.928  1.00 57.82  ? 2375 GLY A O     1 
ATOM   3482 N  N     . ASP A 1 585 ? 114.422 90.156  85.508  1.00 61.53  ? 2376 ASP A N     1 
ATOM   3483 C  CA    . ASP A 1 585 ? 113.938 90.778  86.737  1.00 57.29  ? 2376 ASP A CA    1 
ATOM   3484 C  C     . ASP A 1 585 ? 113.035 91.970  86.441  1.00 55.37  ? 2376 ASP A C     1 
ATOM   3485 O  O     . ASP A 1 585 ? 111.978 92.122  87.065  1.00 57.66  ? 2376 ASP A O     1 
ATOM   3486 C  CB    . ASP A 1 585 ? 115.119 91.203  87.609  1.00 61.58  ? 2376 ASP A CB    1 
ATOM   3487 C  CG    . ASP A 1 585 ? 114.780 91.205  89.087  1.00 68.77  ? 2376 ASP A CG    1 
ATOM   3488 O  OD1   . ASP A 1 585 ? 113.591 91.386  89.426  1.00 66.86  ? 2376 ASP A OD1   1 
ATOM   3489 O  OD2   . ASP A 1 585 ? 115.702 91.023  89.910  1.00 71.19  ? 2376 ASP A OD2   1 
ATOM   3490 N  N     . ASP A 1 586 ? 113.434 92.832  85.502  1.00 53.76  ? 2377 ASP A N     1 
ATOM   3491 C  CA    . ASP A 1 586 ? 112.608 93.989  85.174  1.00 50.94  ? 2377 ASP A CA    1 
ATOM   3492 C  C     . ASP A 1 586 ? 111.297 93.576  84.519  1.00 49.12  ? 2377 ASP A C     1 
ATOM   3493 O  O     . ASP A 1 586 ? 110.257 94.194  84.773  1.00 49.34  ? 2377 ASP A O     1 
ATOM   3494 C  CB    . ASP A 1 586 ? 113.388 94.967  84.289  1.00 54.74  ? 2377 ASP A CB    1 
ATOM   3495 C  CG    . ASP A 1 586 ? 113.496 94.507  82.844  1.00 60.55  ? 2377 ASP A CG    1 
ATOM   3496 O  OD1   . ASP A 1 586 ? 113.742 93.305  82.609  1.00 60.30  ? 2377 ASP A OD1   1 
ATOM   3497 O  OD2   . ASP A 1 586 ? 113.338 95.354  81.940  1.00 62.62  ? 2377 ASP A OD2   1 
ATOM   3498 N  N     . LEU A 1 587 ? 111.317 92.527  83.695  1.00 51.16  ? 2378 LEU A N     1 
ATOM   3499 C  CA    . LEU A 1 587 ? 110.074 91.998  83.146  1.00 51.61  ? 2378 LEU A CA    1 
ATOM   3500 C  C     . LEU A 1 587 ? 109.187 91.441  84.249  1.00 48.76  ? 2378 LEU A C     1 
ATOM   3501 O  O     . LEU A 1 587 ? 107.963 91.605  84.214  1.00 48.93  ? 2378 LEU A O     1 
ATOM   3502 C  CB    . LEU A 1 587 ? 110.375 90.924  82.103  1.00 54.06  ? 2378 LEU A CB    1 
ATOM   3503 C  CG    . LEU A 1 587 ? 109.181 90.405  81.304  1.00 52.19  ? 2378 LEU A CG    1 
ATOM   3504 C  CD1   . LEU A 1 587 ? 108.392 91.565  80.736  1.00 53.06  ? 2378 LEU A CD1   1 
ATOM   3505 C  CD2   . LEU A 1 587 ? 109.650 89.485  80.193  1.00 53.07  ? 2378 LEU A CD2   1 
ATOM   3506 N  N     . ARG A 1 588 ? 109.792 90.783  85.241  1.00 50.37  ? 2379 ARG A N     1 
ATOM   3507 C  CA    . ARG A 1 588 ? 109.026 90.275  86.373  1.00 47.35  ? 2379 ARG A CA    1 
ATOM   3508 C  C     . ARG A 1 588 ? 108.376 91.411  87.151  1.00 43.67  ? 2379 ARG A C     1 
ATOM   3509 O  O     . ARG A 1 588 ? 107.212 91.311  87.553  1.00 38.87  ? 2379 ARG A O     1 
ATOM   3510 C  CB    . ARG A 1 588 ? 109.931 89.464  87.294  1.00 48.64  ? 2379 ARG A CB    1 
ATOM   3511 C  CG    . ARG A 1 588 ? 109.197 88.817  88.442  1.00 43.95  ? 2379 ARG A CG    1 
ATOM   3512 C  CD    . ARG A 1 588 ? 110.073 88.697  89.670  1.00 44.08  ? 2379 ARG A CD    1 
ATOM   3513 N  NE    . ARG A 1 588 ? 109.260 88.744  90.877  1.00 38.01  ? 2379 ARG A NE    1 
ATOM   3514 C  CZ    . ARG A 1 588 ? 108.596 87.702  91.354  1.00 36.51  ? 2379 ARG A CZ    1 
ATOM   3515 N  NH1   . ARG A 1 588 ? 108.682 86.513  90.784  1.00 42.45  ? 2379 ARG A NH1   1 
ATOM   3516 N  NH2   . ARG A 1 588 ? 107.827 87.856  92.426  1.00 33.57  ? 2379 ARG A NH2   1 
ATOM   3517 N  N     . GLN A 1 589 ? 109.119 92.495  87.383  1.00 44.81  ? 2380 GLN A N     1 
ATOM   3518 C  CA    . GLN A 1 589 ? 108.559 93.641  88.093  1.00 38.22  ? 2380 GLN A CA    1 
ATOM   3519 C  C     . GLN A 1 589 ? 107.439 94.294  87.296  1.00 39.23  ? 2380 GLN A C     1 
ATOM   3520 O  O     . GLN A 1 589 ? 106.426 94.711  87.868  1.00 41.09  ? 2380 GLN A O     1 
ATOM   3521 C  CB    . GLN A 1 589 ? 109.656 94.657  88.403  1.00 37.76  ? 2380 GLN A CB    1 
ATOM   3522 C  CG    . GLN A 1 589 ? 110.609 94.209  89.488  1.00 41.82  ? 2380 GLN A CG    1 
ATOM   3523 C  CD    . GLN A 1 589 ? 110.045 94.436  90.872  1.00 50.41  ? 2380 GLN A CD    1 
ATOM   3524 O  OE1   . GLN A 1 589 ? 110.390 93.730  91.818  1.00 55.51  ? 2380 GLN A OE1   1 
ATOM   3525 N  NE2   . GLN A 1 589 ? 109.169 95.425  90.999  1.00 46.87  ? 2380 GLN A NE2   1 
ATOM   3526 N  N     . GLN A 1 590 ? 107.607 94.404  85.978  1.00 40.35  ? 2381 GLN A N     1 
ATOM   3527 C  CA    . GLN A 1 590 ? 106.542 94.954  85.149  1.00 39.92  ? 2381 GLN A CA    1 
ATOM   3528 C  C     . GLN A 1 590 ? 105.299 94.075  85.201  1.00 39.27  ? 2381 GLN A C     1 
ATOM   3529 O  O     . GLN A 1 590 ? 104.174 94.581  85.274  1.00 37.59  ? 2381 GLN A O     1 
ATOM   3530 C  CB    . GLN A 1 590 ? 107.028 95.121  83.710  1.00 46.15  ? 2381 GLN A CB    1 
ATOM   3531 C  CG    . GLN A 1 590 ? 106.105 95.958  82.845  1.00 53.07  ? 2381 GLN A CG    1 
ATOM   3532 C  CD    . GLN A 1 590 ? 106.741 96.347  81.528  1.00 61.80  ? 2381 GLN A CD    1 
ATOM   3533 O  OE1   . GLN A 1 590 ? 107.916 96.069  81.286  1.00 62.68  ? 2381 GLN A OE1   1 
ATOM   3534 N  NE2   . GLN A 1 590 ? 105.968 96.998  80.667  1.00 65.35  ? 2381 GLN A NE2   1 
ATOM   3535 N  N     . ALA A 1 591 ? 105.484 92.753  85.173  1.00 40.16  ? 2382 ALA A N     1 
ATOM   3536 C  CA    . ALA A 1 591 ? 104.348 91.843  85.278  1.00 35.14  ? 2382 ALA A CA    1 
ATOM   3537 C  C     . ALA A 1 591 ? 103.667 91.963  86.634  1.00 35.82  ? 2382 ALA A C     1 
ATOM   3538 O  O     . ALA A 1 591 ? 102.436 91.913  86.724  1.00 38.29  ? 2382 ALA A O     1 
ATOM   3539 C  CB    . ALA A 1 591 ? 104.803 90.405  85.035  1.00 38.31  ? 2382 ALA A CB    1 
ATOM   3540 N  N     . LYS A 1 592 ? 104.452 92.111  87.703  1.00 34.53  ? 2383 LYS A N     1 
ATOM   3541 C  CA    . LYS A 1 592 ? 103.875 92.281  89.033  1.00 30.65  ? 2383 LYS A CA    1 
ATOM   3542 C  C     . LYS A 1 592 ? 103.072 93.571  89.124  1.00 28.66  ? 2383 LYS A C     1 
ATOM   3543 O  O     . LYS A 1 592 ? 101.967 93.586  89.681  1.00 30.58  ? 2383 LYS A O     1 
ATOM   3544 C  CB    . LYS A 1 592 ? 104.981 92.265  90.088  1.00 30.35  ? 2383 LYS A CB    1 
ATOM   3545 C  CG    . LYS A 1 592 ? 104.720 93.162  91.285  1.00 23.04  ? 2383 LYS A CG    1 
ATOM   3546 C  CD    . LYS A 1 592 ? 105.669 92.842  92.421  1.00 22.62  ? 2383 LYS A CD    1 
ATOM   3547 C  CE    . LYS A 1 592 ? 107.107 92.845  91.947  1.00 25.90  ? 2383 LYS A CE    1 
ATOM   3548 N  NZ    . LYS A 1 592 ? 108.056 92.598  93.062  1.00 24.16  ? 2383 LYS A NZ    1 
ATOM   3549 N  N     . GLN A 1 593 ? 103.540 94.669  88.583  1.00 29.89  ? 2384 GLN A N     1 
ATOM   3550 C  CA    . GLN A 1 593 ? 102.816 95.952  88.613  1.00 29.40  ? 2384 GLN A CA    1 
ATOM   3551 C  C     . GLN A 1 593 ? 101.640 95.917  87.665  1.00 29.71  ? 2384 GLN A C     1 
ATOM   3552 O  O     . GLN A 1 593 ? 100.747 96.687  87.864  1.00 27.88  ? 2384 GLN A O     1 
ATOM   3553 C  CB    . GLN A 1 593 ? 103.785 97.080  88.314  1.00 31.46  ? 2384 GLN A CB    1 
ATOM   3554 C  CG    . GLN A 1 593 ? 105.073 96.963  89.092  1.00 31.29  ? 2384 GLN A CG    1 
ATOM   3555 C  CD    . GLN A 1 593 ? 105.702 98.316  89.292  1.00 43.23  ? 2384 GLN A CD    1 
ATOM   3556 O  OE1   . GLN A 1 593 ? 106.858 98.546  88.948  1.00 45.11  ? 2384 GLN A OE1   1 
ATOM   3557 N  NE2   . GLN A 1 593 ? 104.930 99.231  89.847  1.00 45.21  ? 2384 GLN A NE2   1 
ATOM   3558 N  N     . ILE A 1 594 ? 101.665 95.107  86.627  1.00 32.96  ? 2385 ILE A N     1 
ATOM   3559 C  CA    . ILE A 1 594 ? 100.481 94.926  85.792  1.00 32.58  ? 2385 ILE A CA    1 
ATOM   3560 C  C     . ILE A 1 594 ? 99.421  94.131  86.547  1.00 29.91  ? 2385 ILE A C     1 
ATOM   3561 O  O     . ILE A 1 594 ? 98.235  94.485  86.550  1.00 30.48  ? 2385 ILE A O     1 
ATOM   3562 C  CB    . ILE A 1 594 ? 100.868 94.239  84.469  1.00 34.44  ? 2385 ILE A CB    1 
ATOM   3563 C  CG1   . ILE A 1 594 ? 101.323 95.276  83.441  1.00 41.64  ? 2385 ILE A CG1   1 
ATOM   3564 C  CG2   . ILE A 1 594 ? 99.702  93.433  83.917  1.00 37.40  ? 2385 ILE A CG2   1 
ATOM   3565 C  CD1   . ILE A 1 594 ? 100.209 96.062  82.819  1.00 46.39  ? 2385 ILE A CD1   1 
ATOM   3566 N  N     . CYS A 1 595 ? 99.839  93.048  87.208  1.00 29.69  ? 2386 CYS A N     1 
ATOM   3567 C  CA    . CYS A 1 595 ? 98.902  92.214  87.953  1.00 28.35  ? 2386 CYS A CA    1 
ATOM   3568 C  C     . CYS A 1 595 ? 98.259  92.987  89.094  1.00 29.87  ? 2386 CYS A C     1 
ATOM   3569 O  O     . CYS A 1 595 ? 97.043  92.909  89.299  1.00 34.49  ? 2386 CYS A O     1 
ATOM   3570 C  CB    . CYS A 1 595 ? 99.617  90.976  88.491  1.00 27.74  ? 2386 CYS A CB    1 
ATOM   3571 S  SG    . CYS A 1 595 ? 98.612  89.953  89.585  1.00 44.47  ? 2386 CYS A SG    1 
ATOM   3572 N  N     . TYR A 1 596 ? 99.058  93.747  89.845  1.00 27.42  ? 2387 TYR A N     1 
ATOM   3573 C  CA    . TYR A 1 596 ? 98.507  94.529  90.945  1.00 20.83  ? 2387 TYR A CA    1 
ATOM   3574 C  C     . TYR A 1 596 ? 97.582  95.625  90.432  1.00 22.63  ? 2387 TYR A C     1 
ATOM   3575 O  O     . TYR A 1 596 ? 96.569  95.937  91.069  1.00 23.83  ? 2387 TYR A O     1 
ATOM   3576 C  CB    . TYR A 1 596 ? 99.636  95.114  91.785  1.00 19.10  ? 2387 TYR A CB    1 
ATOM   3577 C  CG    . TYR A 1 596 ? 100.224 94.117  92.751  1.00 16.73  ? 2387 TYR A CG    1 
ATOM   3578 C  CD1   . TYR A 1 596 ? 99.407  93.266  93.478  1.00 17.38  ? 2387 TYR A CD1   1 
ATOM   3579 C  CD2   . TYR A 1 596 ? 101.595 94.016  92.926  1.00 17.54  ? 2387 TYR A CD2   1 
ATOM   3580 C  CE1   . TYR A 1 596 ? 99.938  92.350  94.358  1.00 15.41  ? 2387 TYR A CE1   1 
ATOM   3581 C  CE2   . TYR A 1 596 ? 102.134 93.102  93.804  1.00 15.57  ? 2387 TYR A CE2   1 
ATOM   3582 C  CZ    . TYR A 1 596 ? 101.302 92.273  94.516  1.00 14.86  ? 2387 TYR A CZ    1 
ATOM   3583 O  OH    . TYR A 1 596 ? 101.836 91.362  95.391  1.00 17.68  ? 2387 TYR A OH    1 
ATOM   3584 N  N     . GLY A 1 597 ? 97.909  96.220  89.284  1.00 22.82  ? 2388 GLY A N     1 
ATOM   3585 C  CA    . GLY A 1 597 ? 97.006  97.189  88.691  1.00 25.68  ? 2388 GLY A CA    1 
ATOM   3586 C  C     . GLY A 1 597 ? 95.667  96.580  88.332  1.00 29.66  ? 2388 GLY A C     1 
ATOM   3587 O  O     . GLY A 1 597 ? 94.615  97.130  88.660  1.00 34.28  ? 2388 GLY A O     1 
ATOM   3588 N  N     . ILE A 1 598 ? 95.688  95.420  87.669  1.00 26.97  ? 2389 ILE A N     1 
ATOM   3589 C  CA    . ILE A 1 598 ? 94.434  94.746  87.329  1.00 25.03  ? 2389 ILE A CA    1 
ATOM   3590 C  C     . ILE A 1 598 ? 93.661  94.392  88.590  1.00 24.66  ? 2389 ILE A C     1 
ATOM   3591 O  O     . ILE A 1 598 ? 92.426  94.462  88.621  1.00 24.52  ? 2389 ILE A O     1 
ATOM   3592 C  CB    . ILE A 1 598 ? 94.695  93.503  86.460  1.00 31.62  ? 2389 ILE A CB    1 
ATOM   3593 C  CG1   . ILE A 1 598 ? 95.592  93.850  85.276  1.00 32.05  ? 2389 ILE A CG1   1 
ATOM   3594 C  CG2   . ILE A 1 598 ? 93.385  92.902  85.983  1.00 42.03  ? 2389 ILE A CG2   1 
ATOM   3595 C  CD1   . ILE A 1 598 ? 95.981  92.657  84.445  1.00 39.61  ? 2389 ILE A CD1   1 
ATOM   3596 N  N     . ILE A 1 599 ? 94.373  94.003  89.648  1.00 26.64  ? 2390 ILE A N     1 
ATOM   3597 C  CA    . ILE A 1 599 ? 93.719  93.718  90.921  1.00 26.82  ? 2390 ILE A CA    1 
ATOM   3598 C  C     . ILE A 1 599 ? 93.015  94.961  91.451  1.00 28.38  ? 2390 ILE A C     1 
ATOM   3599 O  O     . ILE A 1 599 ? 91.864  94.898  91.901  1.00 30.41  ? 2390 ILE A O     1 
ATOM   3600 C  CB    . ILE A 1 599 ? 94.743  93.179  91.936  1.00 27.47  ? 2390 ILE A CB    1 
ATOM   3601 C  CG1   . ILE A 1 599 ? 95.174  91.758  91.566  1.00 27.32  ? 2390 ILE A CG1   1 
ATOM   3602 C  CG2   . ILE A 1 599 ? 94.175  93.238  93.332  1.00 27.37  ? 2390 ILE A CG2   1 
ATOM   3603 C  CD1   . ILE A 1 599 ? 94.037  90.784  91.443  1.00 29.61  ? 2390 ILE A CD1   1 
ATOM   3604 N  N     . TYR A 1 600 ? 93.683  96.111  91.387  1.00 27.22  ? 2391 TYR A N     1 
ATOM   3605 C  CA    . TYR A 1 600 ? 93.188  97.355  91.974  1.00 23.06  ? 2391 TYR A CA    1 
ATOM   3606 C  C     . TYR A 1 600 ? 92.519  98.254  90.944  1.00 28.00  ? 2391 TYR A C     1 
ATOM   3607 O  O     . TYR A 1 600 ? 92.660  99.478  90.991  1.00 30.49  ? 2391 TYR A O     1 
ATOM   3608 C  CB    . TYR A 1 600 ? 94.324  98.087  92.677  1.00 24.34  ? 2391 TYR A CB    1 
ATOM   3609 C  CG    . TYR A 1 600 ? 94.914  97.286  93.810  1.00 26.97  ? 2391 TYR A CG    1 
ATOM   3610 C  CD1   . TYR A 1 600 ? 94.102  96.528  94.636  1.00 29.71  ? 2391 TYR A CD1   1 
ATOM   3611 C  CD2   . TYR A 1 600 ? 96.279  97.269  94.042  1.00 24.90  ? 2391 TYR A CD2   1 
ATOM   3612 C  CE1   . TYR A 1 600 ? 94.628  95.786  95.668  1.00 27.58  ? 2391 TYR A CE1   1 
ATOM   3613 C  CE2   . TYR A 1 600 ? 96.816  96.528  95.075  1.00 22.35  ? 2391 TYR A CE2   1 
ATOM   3614 C  CZ    . TYR A 1 600 ? 95.984  95.788  95.883  1.00 23.86  ? 2391 TYR A CZ    1 
ATOM   3615 O  OH    . TYR A 1 600 ? 96.500  95.045  96.913  1.00 25.88  ? 2391 TYR A OH    1 
ATOM   3616 N  N     . GLY A 1 601 ? 91.795  97.667  89.998  1.00 33.61  ? 2392 GLY A N     1 
ATOM   3617 C  CA    . GLY A 1 601 ? 90.965  98.432  89.081  1.00 31.41  ? 2392 GLY A CA    1 
ATOM   3618 C  C     . GLY A 1 601 ? 91.697  99.330  88.108  1.00 28.02  ? 2392 GLY A C     1 
ATOM   3619 O  O     . GLY A 1 601 ? 91.289  100.481 87.910  1.00 30.73  ? 2392 GLY A O     1 
ATOM   3620 N  N     . MET A 1 602 ? 92.766  98.836  87.494  1.00 28.85  ? 2393 MET A N     1 
ATOM   3621 C  CA    . MET A 1 602 ? 93.436  99.590  86.445  1.00 33.93  ? 2393 MET A CA    1 
ATOM   3622 C  C     . MET A 1 602 ? 92.529  99.730  85.232  1.00 40.41  ? 2393 MET A C     1 
ATOM   3623 O  O     . MET A 1 602 ? 91.865  98.776  84.817  1.00 45.87  ? 2393 MET A O     1 
ATOM   3624 C  CB    . MET A 1 602 ? 94.735  98.902  86.034  1.00 30.86  ? 2393 MET A CB    1 
ATOM   3625 C  CG    . MET A 1 602 ? 95.910  99.837  85.853  1.00 31.54  ? 2393 MET A CG    1 
ATOM   3626 S  SD    . MET A 1 602 ? 97.353  98.964  85.225  1.00 38.00  ? 2393 MET A SD    1 
ATOM   3627 C  CE    . MET A 1 602 ? 98.672  99.905  85.973  1.00 32.96  ? 2393 MET A CE    1 
ATOM   3628 N  N     . GLY A 1 603 ? 92.502  100.930 84.662  1.00 41.09  ? 2394 GLY A N     1 
ATOM   3629 C  CA    . GLY A 1 603 ? 91.752  101.142 83.446  1.00 47.43  ? 2394 GLY A CA    1 
ATOM   3630 C  C     . GLY A 1 603 ? 92.411  100.487 82.250  1.00 52.23  ? 2394 GLY A C     1 
ATOM   3631 O  O     . GLY A 1 603 ? 93.589  100.130 82.265  1.00 52.11  ? 2394 GLY A O     1 
ATOM   3632 N  N     . ALA A 1 604 ? 91.620  100.317 81.190  1.00 52.28  ? 2395 ALA A N     1 
ATOM   3633 C  CA    . ALA A 1 604 ? 92.158  99.751  79.958  1.00 52.94  ? 2395 ALA A CA    1 
ATOM   3634 C  C     . ALA A 1 604 ? 93.203  100.671 79.340  1.00 55.97  ? 2395 ALA A C     1 
ATOM   3635 O  O     . ALA A 1 604 ? 94.218  100.200 78.813  1.00 57.41  ? 2395 ALA A O     1 
ATOM   3636 C  CB    . ALA A 1 604 ? 91.028  99.476  78.969  1.00 59.37  ? 2395 ALA A CB    1 
ATOM   3637 N  N     . LYS A 1 605 ? 92.974  101.985 79.397  1.00 58.19  ? 2396 LYS A N     1 
ATOM   3638 C  CA    . LYS A 1 605 ? 93.901  102.932 78.784  1.00 57.03  ? 2396 LYS A CA    1 
ATOM   3639 C  C     . LYS A 1 605 ? 95.275  102.866 79.441  1.00 55.41  ? 2396 LYS A C     1 
ATOM   3640 O  O     . LYS A 1 605 ? 96.298  102.751 78.756  1.00 56.99  ? 2396 LYS A O     1 
ATOM   3641 C  CB    . LYS A 1 605 ? 93.329  104.347 78.868  1.00 59.91  ? 2396 LYS A CB    1 
ATOM   3642 C  CG    . LYS A 1 605 ? 94.366  105.453 78.707  1.00 62.91  ? 2396 LYS A CG    1 
ATOM   3643 C  CD    . LYS A 1 605 ? 93.758  106.862 78.707  1.00 63.90  ? 2396 LYS A CD    1 
ATOM   3644 C  CE    . LYS A 1 605 ? 92.351  106.957 78.104  1.00 64.94  ? 2396 LYS A CE    1 
ATOM   3645 N  NZ    . LYS A 1 605 ? 92.166  106.250 76.800  1.00 64.21  ? 2396 LYS A NZ    1 
ATOM   3646 N  N     . SER A 1 606 ? 95.317  102.928 80.773  1.00 54.68  ? 2397 SER A N     1 
ATOM   3647 C  CA    . SER A 1 606 ? 96.598  102.873 81.471  1.00 51.61  ? 2397 SER A CA    1 
ATOM   3648 C  C     . SER A 1 606 ? 97.246  101.501 81.348  1.00 53.56  ? 2397 SER A C     1 
ATOM   3649 O  O     . SER A 1 606 ? 98.476  101.404 81.258  1.00 57.88  ? 2397 SER A O     1 
ATOM   3650 C  CB    . SER A 1 606 ? 96.415  103.245 82.941  1.00 49.59  ? 2397 SER A CB    1 
ATOM   3651 O  OG    . SER A 1 606 ? 97.655  103.236 83.624  1.00 51.51  ? 2397 SER A OG    1 
ATOM   3652 N  N     . LEU A 1 607 ? 96.442  100.436 81.341  1.00 50.57  ? 2398 LEU A N     1 
ATOM   3653 C  CA    . LEU A 1 607 ? 96.990  99.097  81.154  1.00 52.05  ? 2398 LEU A CA    1 
ATOM   3654 C  C     . LEU A 1 607 ? 97.680  98.978  79.802  1.00 58.58  ? 2398 LEU A C     1 
ATOM   3655 O  O     . LEU A 1 607 ? 98.795  98.455  79.704  1.00 62.48  ? 2398 LEU A O     1 
ATOM   3656 C  CB    . LEU A 1 607 ? 95.883  98.052  81.276  1.00 53.11  ? 2398 LEU A CB    1 
ATOM   3657 C  CG    . LEU A 1 607 ? 96.369  96.611  81.434  1.00 54.20  ? 2398 LEU A CG    1 
ATOM   3658 C  CD1   . LEU A 1 607 ? 96.712  96.327  82.881  1.00 46.58  ? 2398 LEU A CD1   1 
ATOM   3659 C  CD2   . LEU A 1 607 ? 95.352  95.620  80.912  1.00 60.31  ? 2398 LEU A CD2   1 
ATOM   3660 N  N     . GLY A 1 608 ? 97.026  99.464  78.744  1.00 59.64  ? 2399 GLY A N     1 
ATOM   3661 C  CA    . GLY A 1 608 ? 97.644  99.450  77.431  1.00 60.58  ? 2399 GLY A CA    1 
ATOM   3662 C  C     . GLY A 1 608 ? 98.848  100.362 77.330  1.00 60.54  ? 2399 GLY A C     1 
ATOM   3663 O  O     . GLY A 1 608 ? 99.812  100.046 76.627  1.00 63.24  ? 2399 GLY A O     1 
ATOM   3664 N  N     . GLU A 1 609 ? 98.810  101.505 78.018  1.00 59.61  ? 2400 GLU A N     1 
ATOM   3665 C  CA    . GLU A 1 609 ? 99.953  102.412 78.008  1.00 60.62  ? 2400 GLU A CA    1 
ATOM   3666 C  C     . GLU A 1 609 ? 101.172 101.769 78.657  1.00 61.52  ? 2400 GLU A C     1 
ATOM   3667 O  O     . GLU A 1 609 ? 102.293 101.898 78.151  1.00 63.25  ? 2400 GLU A O     1 
ATOM   3668 C  CB    . GLU A 1 609 ? 99.589  103.715 78.718  1.00 64.91  ? 2400 GLU A CB    1 
ATOM   3669 C  CG    . GLU A 1 609 ? 100.700 104.748 78.739  1.00 74.65  ? 2400 GLU A CG    1 
ATOM   3670 C  CD    . GLU A 1 609 ? 100.202 106.126 79.130  1.00 80.94  ? 2400 GLU A CD    1 
ATOM   3671 O  OE1   . GLU A 1 609 ? 99.105  106.513 78.676  1.00 80.95  ? 2400 GLU A OE1   1 
ATOM   3672 O  OE2   . GLU A 1 609 ? 100.906 106.821 79.891  1.00 87.55  ? 2400 GLU A OE2   1 
ATOM   3673 N  N     . GLN A 1 610 ? 100.975 101.076 79.780  1.00 61.42  ? 2401 GLN A N     1 
ATOM   3674 C  CA    . GLN A 1 610 ? 102.104 100.447 80.457  1.00 61.37  ? 2401 GLN A CA    1 
ATOM   3675 C  C     . GLN A 1 610 ? 102.572 99.189  79.735  1.00 61.46  ? 2401 GLN A C     1 
ATOM   3676 O  O     . GLN A 1 610 ? 103.778 98.932  79.653  1.00 64.13  ? 2401 GLN A O     1 
ATOM   3677 C  CB    . GLN A 1 610 ? 101.743 100.121 81.905  1.00 59.09  ? 2401 GLN A CB    1 
ATOM   3678 C  CG    . GLN A 1 610 ? 102.898 99.519  82.690  1.00 59.24  ? 2401 GLN A CG    1 
ATOM   3679 C  CD    . GLN A 1 610 ? 102.540 99.218  84.127  1.00 56.65  ? 2401 GLN A CD    1 
ATOM   3680 O  OE1   . GLN A 1 610 ? 101.368 99.216  84.499  1.00 50.78  ? 2401 GLN A OE1   1 
ATOM   3681 N  NE2   . GLN A 1 610 ? 103.551 98.958  84.947  1.00 54.76  ? 2401 GLN A NE2   1 
ATOM   3682 N  N     . MET A 1 611 ? 101.643 98.396  79.208  1.00 61.60  ? 2402 MET A N     1 
ATOM   3683 C  CA    . MET A 1 611 ? 101.976 97.136  78.558  1.00 61.63  ? 2402 MET A CA    1 
ATOM   3684 C  C     . MET A 1 611 ? 102.379 97.308  77.099  1.00 63.95  ? 2402 MET A C     1 
ATOM   3685 O  O     . MET A 1 611 ? 102.802 96.335  76.468  1.00 62.71  ? 2402 MET A O     1 
ATOM   3686 C  CB    . MET A 1 611 ? 100.791 96.169  78.664  1.00 62.89  ? 2402 MET A CB    1 
ATOM   3687 C  CG    . MET A 1 611 ? 101.169 94.701  78.571  1.00 64.25  ? 2402 MET A CG    1 
ATOM   3688 S  SD    . MET A 1 611 ? 99.971  93.579  79.314  1.00 76.08  ? 2402 MET A SD    1 
ATOM   3689 C  CE    . MET A 1 611 ? 98.485  94.570  79.247  1.00 62.52  ? 2402 MET A CE    1 
ATOM   3690 N  N     . GLY A 1 612 ? 102.274 98.517  76.554  1.00 67.05  ? 2403 GLY A N     1 
ATOM   3691 C  CA    . GLY A 1 612 ? 102.650 98.740  75.173  1.00 67.11  ? 2403 GLY A CA    1 
ATOM   3692 C  C     . GLY A 1 612 ? 101.693 98.176  74.152  1.00 65.77  ? 2403 GLY A C     1 
ATOM   3693 O  O     . GLY A 1 612 ? 102.091 97.943  73.008  1.00 69.61  ? 2403 GLY A O     1 
ATOM   3694 N  N     . ILE A 1 613 ? 100.436 97.945  74.528  1.00 65.49  ? 2404 ILE A N     1 
ATOM   3695 C  CA    . ILE A 1 613 ? 99.455  97.386  73.606  1.00 68.47  ? 2404 ILE A CA    1 
ATOM   3696 C  C     . ILE A 1 613 ? 98.291  98.356  73.446  1.00 72.35  ? 2404 ILE A C     1 
ATOM   3697 O  O     . ILE A 1 613 ? 98.247  99.405  74.096  1.00 70.42  ? 2404 ILE A O     1 
ATOM   3698 C  CB    . ILE A 1 613 ? 98.964  96.006  74.079  1.00 67.32  ? 2404 ILE A CB    1 
ATOM   3699 C  CG1   . ILE A 1 613 ? 98.086  96.144  75.323  1.00 67.79  ? 2404 ILE A CG1   1 
ATOM   3700 C  CG2   . ILE A 1 613 ? 100.142 95.089  74.363  1.00 67.40  ? 2404 ILE A CG2   1 
ATOM   3701 C  CD1   . ILE A 1 613 ? 97.527  94.829  75.810  1.00 67.85  ? 2404 ILE A CD1   1 
ATOM   3702 N  N     . LYS A 1 614 ? 97.345  98.008  72.578  1.00 75.36  ? 2405 LYS A N     1 
ATOM   3703 C  CA    . LYS A 1 614 ? 96.217  98.872  72.273  1.00 76.36  ? 2405 LYS A CA    1 
ATOM   3704 C  C     . LYS A 1 614 ? 95.199  98.862  73.412  1.00 74.63  ? 2405 LYS A C     1 
ATOM   3705 O  O     . LYS A 1 614 ? 95.267  98.055  74.342  1.00 71.87  ? 2405 LYS A O     1 
ATOM   3706 C  CB    . LYS A 1 614 ? 95.554  98.441  70.965  1.00 75.89  ? 2405 LYS A CB    1 
ATOM   3707 C  CG    . LYS A 1 614 ? 95.992  99.241  69.750  1.00 76.86  ? 2405 LYS A CG    1 
ATOM   3708 C  CD    . LYS A 1 614 ? 95.160  100.504 69.593  1.00 80.24  ? 2405 LYS A CD    1 
ATOM   3709 C  CE    . LYS A 1 614 ? 95.931  101.587 68.855  1.00 82.40  ? 2405 LYS A CE    1 
ATOM   3710 N  NZ    . LYS A 1 614 ? 95.110  102.812 68.647  1.00 80.07  ? 2405 LYS A NZ    1 
ATOM   3711 N  N     . GLU A 1 615 ? 94.245  99.792  73.327  1.00 74.83  ? 2406 GLU A N     1 
ATOM   3712 C  CA    . GLU A 1 615 ? 93.179  99.868  74.322  1.00 71.19  ? 2406 GLU A CA    1 
ATOM   3713 C  C     . GLU A 1 615 ? 92.304  98.620  74.293  1.00 69.03  ? 2406 GLU A C     1 
ATOM   3714 O  O     . GLU A 1 615 ? 91.956  98.068  75.344  1.00 68.38  ? 2406 GLU A O     1 
ATOM   3715 C  CB    . GLU A 1 615 ? 92.338  101.122 74.083  1.00 71.94  ? 2406 GLU A CB    1 
ATOM   3716 C  CG    . GLU A 1 615 ? 90.903  101.021 74.574  1.00 72.62  ? 2406 GLU A CG    1 
ATOM   3717 C  CD    . GLU A 1 615 ? 90.755  101.418 76.026  1.00 72.98  ? 2406 GLU A CD    1 
ATOM   3718 O  OE1   . GLU A 1 615 ? 91.778  101.751 76.657  1.00 70.92  ? 2406 GLU A OE1   1 
ATOM   3719 O  OE2   . GLU A 1 615 ? 89.615  101.398 76.536  1.00 78.33  ? 2406 GLU A OE2   1 
ATOM   3720 N  N     . ASN A 1 616 ? 91.933  98.163  73.095  1.00 71.16  ? 2407 ASN A N     1 
ATOM   3721 C  CA    . ASN A 1 616 ? 91.093  96.975  72.984  1.00 71.97  ? 2407 ASN A CA    1 
ATOM   3722 C  C     . ASN A 1 616 ? 91.814  95.741  73.509  1.00 71.04  ? 2407 ASN A C     1 
ATOM   3723 O  O     . ASN A 1 616 ? 91.219  94.917  74.215  1.00 71.21  ? 2407 ASN A O     1 
ATOM   3724 C  CB    . ASN A 1 616 ? 90.663  96.768  71.531  1.00 74.40  ? 2407 ASN A CB    1 
ATOM   3725 C  CG    . ASN A 1 616 ? 89.724  97.855  71.037  1.00 77.94  ? 2407 ASN A CG    1 
ATOM   3726 O  OD1   . ASN A 1 616 ? 89.622  98.926  71.635  1.00 78.97  ? 2407 ASN A OD1   1 
ATOM   3727 N  ND2   . ASN A 1 616 ? 89.033  97.581  69.937  1.00 79.08  ? 2407 ASN A ND2   1 
ATOM   3728 N  N     . ASP A 1 617 ? 93.098  95.596  73.176  1.00 70.54  ? 2408 ASP A N     1 
ATOM   3729 C  CA    . ASP A 1 617 ? 93.868  94.461  73.672  1.00 70.63  ? 2408 ASP A CA    1 
ATOM   3730 C  C     . ASP A 1 617 ? 94.011  94.514  75.188  1.00 69.33  ? 2408 ASP A C     1 
ATOM   3731 O  O     . ASP A 1 617 ? 93.939  93.481  75.863  1.00 68.22  ? 2408 ASP A O     1 
ATOM   3732 C  CB    . ASP A 1 617 ? 95.239  94.423  72.999  1.00 72.66  ? 2408 ASP A CB    1 
ATOM   3733 C  CG    . ASP A 1 617 ? 95.145  94.270  71.493  1.00 78.36  ? 2408 ASP A CG    1 
ATOM   3734 O  OD1   . ASP A 1 617 ? 94.166  93.659  71.016  1.00 79.70  ? 2408 ASP A OD1   1 
ATOM   3735 O  OD2   . ASP A 1 617 ? 96.049  94.762  70.785  1.00 79.15  ? 2408 ASP A OD2   1 
ATOM   3736 N  N     . ALA A 1 618 ? 94.214  95.712  75.743  1.00 69.68  ? 2409 ALA A N     1 
ATOM   3737 C  CA    . ALA A 1 618 ? 94.306  95.849  77.193  1.00 63.66  ? 2409 ALA A CA    1 
ATOM   3738 C  C     . ALA A 1 618 ? 92.989  95.490  77.870  1.00 61.61  ? 2409 ALA A C     1 
ATOM   3739 O  O     . ALA A 1 618 ? 92.983  94.828  78.912  1.00 62.31  ? 2409 ALA A O     1 
ATOM   3740 C  CB    . ALA A 1 618 ? 94.730  97.268  77.561  1.00 63.08  ? 2409 ALA A CB    1 
ATOM   3741 N  N     . ALA A 1 619 ? 91.862  95.918  77.297  1.00 62.74  ? 2410 ALA A N     1 
ATOM   3742 C  CA    . ALA A 1 619 ? 90.569  95.539  77.858  1.00 60.51  ? 2410 ALA A CA    1 
ATOM   3743 C  C     . ALA A 1 619 ? 90.360  94.031  77.788  1.00 64.36  ? 2410 ALA A C     1 
ATOM   3744 O  O     . ALA A 1 619 ? 89.867  93.418  78.744  1.00 66.02  ? 2410 ALA A O     1 
ATOM   3745 C  CB    . ALA A 1 619 ? 89.444  96.274  77.131  1.00 64.50  ? 2410 ALA A CB    1 
ATOM   3746 N  N     . CYS A 1 620 ? 90.730  93.416  76.662  1.00 65.20  ? 2411 CYS A N     1 
ATOM   3747 C  CA    . CYS A 1 620 ? 90.616  91.967  76.541  1.00 66.03  ? 2411 CYS A CA    1 
ATOM   3748 C  C     . CYS A 1 620 ? 91.477  91.265  77.582  1.00 63.90  ? 2411 CYS A C     1 
ATOM   3749 O  O     . CYS A 1 620 ? 91.063  90.255  78.161  1.00 64.16  ? 2411 CYS A O     1 
ATOM   3750 C  CB    . CYS A 1 620 ? 91.003  91.523  75.131  1.00 68.37  ? 2411 CYS A CB    1 
ATOM   3751 S  SG    . CYS A 1 620 ? 89.832  92.014  73.844  1.00 79.79  ? 2411 CYS A SG    1 
ATOM   3752 N  N     . TYR A 1 621 ? 92.677  91.790  77.837  1.00 61.01  ? 2412 TYR A N     1 
ATOM   3753 C  CA    . TYR A 1 621 ? 93.521  91.238  78.892  1.00 61.03  ? 2412 TYR A CA    1 
ATOM   3754 C  C     . TYR A 1 621 ? 92.879  91.416  80.263  1.00 60.95  ? 2412 TYR A C     1 
ATOM   3755 O  O     . TYR A 1 621 ? 93.007  90.547  81.132  1.00 62.67  ? 2412 TYR A O     1 
ATOM   3756 C  CB    . TYR A 1 621 ? 94.900  91.895  78.855  1.00 60.88  ? 2412 TYR A CB    1 
ATOM   3757 C  CG    . TYR A 1 621 ? 95.941  91.176  79.678  1.00 56.40  ? 2412 TYR A CG    1 
ATOM   3758 C  CD1   . TYR A 1 621 ? 96.450  89.952  79.271  1.00 59.18  ? 2412 TYR A CD1   1 
ATOM   3759 C  CD2   . TYR A 1 621 ? 96.415  91.721  80.862  1.00 50.45  ? 2412 TYR A CD2   1 
ATOM   3760 C  CE1   . TYR A 1 621 ? 97.402  89.291  80.020  1.00 61.98  ? 2412 TYR A CE1   1 
ATOM   3761 C  CE2   . TYR A 1 621 ? 97.367  91.067  81.617  1.00 50.86  ? 2412 TYR A CE2   1 
ATOM   3762 C  CZ    . TYR A 1 621 ? 97.857  89.853  81.192  1.00 57.37  ? 2412 TYR A CZ    1 
ATOM   3763 O  OH    . TYR A 1 621 ? 98.805  89.199  81.943  1.00 57.55  ? 2412 TYR A OH    1 
ATOM   3764 N  N     . ILE A 1 622 ? 92.195  92.542  80.476  1.00 60.09  ? 2413 ILE A N     1 
ATOM   3765 C  CA    . ILE A 1 622 ? 91.495  92.768  81.739  1.00 56.37  ? 2413 ILE A CA    1 
ATOM   3766 C  C     . ILE A 1 622 ? 90.440  91.691  81.958  1.00 58.06  ? 2413 ILE A C     1 
ATOM   3767 O  O     . ILE A 1 622 ? 90.363  91.080  83.032  1.00 59.01  ? 2413 ILE A O     1 
ATOM   3768 C  CB    . ILE A 1 622 ? 90.870  94.175  81.765  1.00 58.64  ? 2413 ILE A CB    1 
ATOM   3769 C  CG1   . ILE A 1 622 ? 91.939  95.246  81.977  1.00 54.56  ? 2413 ILE A CG1   1 
ATOM   3770 C  CG2   . ILE A 1 622 ? 89.807  94.269  82.847  1.00 60.45  ? 2413 ILE A CG2   1 
ATOM   3771 C  CD1   . ILE A 1 622 ? 92.679  95.120  83.279  1.00 47.12  ? 2413 ILE A CD1   1 
ATOM   3772 N  N     . ASP A 1 623 ? 89.609  91.443  80.942  1.00 59.99  ? 2414 ASP A N     1 
ATOM   3773 C  CA    . ASP A 1 623 ? 88.589  90.404  81.085  1.00 61.71  ? 2414 ASP A CA    1 
ATOM   3774 C  C     . ASP A 1 623 ? 89.210  89.017  81.202  1.00 58.80  ? 2414 ASP A C     1 
ATOM   3775 O  O     . ASP A 1 623 ? 88.678  88.155  81.909  1.00 57.14  ? 2414 ASP A O     1 
ATOM   3776 C  CB    . ASP A 1 623 ? 87.574  90.438  79.938  1.00 67.30  ? 2414 ASP A CB    1 
ATOM   3777 C  CG    . ASP A 1 623 ? 86.969  91.811  79.719  1.00 72.29  ? 2414 ASP A CG    1 
ATOM   3778 O  OD1   . ASP A 1 623 ? 87.482  92.579  78.887  1.00 72.59  ? 2414 ASP A OD1   1 
ATOM   3779 O  OD2   . ASP A 1 623 ? 85.965  92.124  80.393  1.00 76.29  ? 2414 ASP A OD2   1 
ATOM   3780 N  N     . SER A 1 624 ? 90.327  88.774  80.513  1.00 58.47  ? 2415 SER A N     1 
ATOM   3781 C  CA    . SER A 1 624 ? 90.994  87.481  80.633  1.00 58.07  ? 2415 SER A CA    1 
ATOM   3782 C  C     . SER A 1 624 ? 91.496  87.249  82.052  1.00 56.00  ? 2415 SER A C     1 
ATOM   3783 O  O     . SER A 1 624 ? 91.362  86.146  82.594  1.00 60.11  ? 2415 SER A O     1 
ATOM   3784 C  CB    . SER A 1 624 ? 92.147  87.388  79.634  1.00 61.78  ? 2415 SER A CB    1 
ATOM   3785 O  OG    . SER A 1 624 ? 91.675  87.438  78.299  1.00 64.63  ? 2415 SER A OG    1 
ATOM   3786 N  N     . PHE A 1 625 ? 92.083  88.277  82.666  1.00 54.04  ? 2416 PHE A N     1 
ATOM   3787 C  CA    . PHE A 1 625 ? 92.543  88.155  84.046  1.00 52.62  ? 2416 PHE A CA    1 
ATOM   3788 C  C     . PHE A 1 625 ? 91.373  87.990  85.007  1.00 51.73  ? 2416 PHE A C     1 
ATOM   3789 O  O     . PHE A 1 625 ? 91.432  87.167  85.928  1.00 50.99  ? 2416 PHE A O     1 
ATOM   3790 C  CB    . PHE A 1 625 ? 93.383  89.374  84.426  1.00 49.65  ? 2416 PHE A CB    1 
ATOM   3791 C  CG    . PHE A 1 625 ? 94.097  89.237  85.741  1.00 42.25  ? 2416 PHE A CG    1 
ATOM   3792 C  CD1   . PHE A 1 625 ? 93.458  89.544  86.930  1.00 40.97  ? 2416 PHE A CD1   1 
ATOM   3793 C  CD2   . PHE A 1 625 ? 95.412  88.812  85.786  1.00 39.39  ? 2416 PHE A CD2   1 
ATOM   3794 C  CE1   . PHE A 1 625 ? 94.113  89.423  88.137  1.00 37.65  ? 2416 PHE A CE1   1 
ATOM   3795 C  CE2   . PHE A 1 625 ? 96.071  88.689  86.991  1.00 41.42  ? 2416 PHE A CE2   1 
ATOM   3796 C  CZ    . PHE A 1 625 ? 95.422  88.996  88.168  1.00 39.14  ? 2416 PHE A CZ    1 
ATOM   3797 N  N     . LYS A 1 626 ? 90.303  88.766  84.816  1.00 53.05  ? 2417 LYS A N     1 
ATOM   3798 C  CA    . LYS A 1 626 ? 89.166  88.692  85.728  1.00 51.44  ? 2417 LYS A CA    1 
ATOM   3799 C  C     . LYS A 1 626 ? 88.467  87.341  85.640  1.00 54.70  ? 2417 LYS A C     1 
ATOM   3800 O  O     . LYS A 1 626 ? 88.068  86.775  86.664  1.00 57.34  ? 2417 LYS A O     1 
ATOM   3801 C  CB    . LYS A 1 626 ? 88.184  89.825  85.434  1.00 56.52  ? 2417 LYS A CB    1 
ATOM   3802 C  CG    . LYS A 1 626 ? 88.585  91.163  86.035  1.00 60.14  ? 2417 LYS A CG    1 
ATOM   3803 C  CD    . LYS A 1 626 ? 87.432  92.152  86.003  1.00 60.40  ? 2417 LYS A CD    1 
ATOM   3804 C  CE    . LYS A 1 626 ? 87.936  93.585  85.989  1.00 54.89  ? 2417 LYS A CE    1 
ATOM   3805 N  NZ    . LYS A 1 626 ? 89.203  93.735  86.756  1.00 54.24  ? 2417 LYS A NZ    1 
ATOM   3806 N  N     . SER A 1 627 ? 88.304  86.809  84.427  1.00 56.01  ? 2418 SER A N     1 
ATOM   3807 C  CA    . SER A 1 627 ? 87.651  85.515  84.266  1.00 53.32  ? 2418 SER A CA    1 
ATOM   3808 C  C     . SER A 1 627 ? 88.523  84.378  84.778  1.00 51.57  ? 2418 SER A C     1 
ATOM   3809 O  O     . SER A 1 627 ? 88.000  83.377  85.280  1.00 53.18  ? 2418 SER A O     1 
ATOM   3810 C  CB    . SER A 1 627 ? 87.291  85.287  82.798  1.00 53.74  ? 2418 SER A CB    1 
ATOM   3811 O  OG    . SER A 1 627 ? 86.243  86.148  82.390  1.00 53.94  ? 2418 SER A OG    1 
ATOM   3812 N  N     . ARG A 1 628 ? 89.845  84.507  84.652  1.00 51.83  ? 2419 ARG A N     1 
ATOM   3813 C  CA    . ARG A 1 628 ? 90.740  83.466  85.147  1.00 53.53  ? 2419 ARG A CA    1 
ATOM   3814 C  C     . ARG A 1 628 ? 90.629  83.318  86.659  1.00 56.74  ? 2419 ARG A C     1 
ATOM   3815 O  O     . ARG A 1 628 ? 90.625  82.196  87.179  1.00 60.39  ? 2419 ARG A O     1 
ATOM   3816 C  CB    . ARG A 1 628 ? 92.179  83.777  84.736  1.00 54.97  ? 2419 ARG A CB    1 
ATOM   3817 C  CG    . ARG A 1 628 ? 93.212  82.822  85.302  1.00 58.89  ? 2419 ARG A CG    1 
ATOM   3818 C  CD    . ARG A 1 628 ? 94.288  82.508  84.276  1.00 65.54  ? 2419 ARG A CD    1 
ATOM   3819 N  NE    . ARG A 1 628 ? 95.292  83.561  84.196  1.00 69.78  ? 2419 ARG A NE    1 
ATOM   3820 C  CZ    . ARG A 1 628 ? 96.504  83.403  83.682  1.00 75.15  ? 2419 ARG A CZ    1 
ATOM   3821 N  NH1   . ARG A 1 628 ? 96.899  82.241  83.187  1.00 76.29  ? 2419 ARG A NH1   1 
ATOM   3822 N  NH2   . ARG A 1 628 ? 97.341  84.436  83.663  1.00 75.05  ? 2419 ARG A NH2   1 
ATOM   3823 N  N     . TYR A 1 629 ? 90.532  84.433  87.377  1.00 55.72  ? 2420 TYR A N     1 
ATOM   3824 C  CA    . TYR A 1 629 ? 90.353  84.441  88.828  1.00 48.43  ? 2420 TYR A CA    1 
ATOM   3825 C  C     . TYR A 1 629 ? 88.965  85.011  89.115  1.00 50.01  ? 2420 TYR A C     1 
ATOM   3826 O  O     . TYR A 1 629 ? 88.810  86.207  89.363  1.00 48.68  ? 2420 TYR A O     1 
ATOM   3827 C  CB    . TYR A 1 629 ? 91.445  85.259  89.510  1.00 41.11  ? 2420 TYR A CB    1 
ATOM   3828 C  CG    . TYR A 1 629 ? 92.848  84.861  89.122  1.00 43.27  ? 2420 TYR A CG    1 
ATOM   3829 C  CD1   . TYR A 1 629 ? 93.189  83.529  88.942  1.00 49.47  ? 2420 TYR A CD1   1 
ATOM   3830 C  CD2   . TYR A 1 629 ? 93.832  85.819  88.931  1.00 43.50  ? 2420 TYR A CD2   1 
ATOM   3831 C  CE1   . TYR A 1 629 ? 94.472  83.163  88.586  1.00 52.39  ? 2420 TYR A CE1   1 
ATOM   3832 C  CE2   . TYR A 1 629 ? 95.117  85.462  88.575  1.00 46.71  ? 2420 TYR A CE2   1 
ATOM   3833 C  CZ    . TYR A 1 629 ? 95.431  84.134  88.403  1.00 51.76  ? 2420 TYR A CZ    1 
ATOM   3834 O  OH    . TYR A 1 629 ? 96.710  83.774  88.048  1.00 55.45  ? 2420 TYR A OH    1 
ATOM   3835 N  N     . THR A 1 630 ? 87.953  84.141  89.081  1.00 53.15  ? 2421 THR A N     1 
ATOM   3836 C  CA    . THR A 1 630 ? 86.586  84.589  89.328  1.00 54.55  ? 2421 THR A CA    1 
ATOM   3837 C  C     . THR A 1 630 ? 86.405  85.041  90.771  1.00 53.75  ? 2421 THR A C     1 
ATOM   3838 O  O     . THR A 1 630 ? 85.680  86.008  91.041  1.00 55.48  ? 2421 THR A O     1 
ATOM   3839 C  CB    . THR A 1 630 ? 85.597  83.475  88.990  1.00 58.60  ? 2421 THR A CB    1 
ATOM   3840 O  OG1   . THR A 1 630 ? 86.085  82.721  87.873  1.00 58.90  ? 2421 THR A OG1   1 
ATOM   3841 C  CG2   . THR A 1 630 ? 84.236  84.060  88.643  1.00 59.26  ? 2421 THR A CG2   1 
ATOM   3842 N  N     . GLY A 1 631 ? 87.052  84.349  91.710  1.00 51.56  ? 2422 GLY A N     1 
ATOM   3843 C  CA    . GLY A 1 631 ? 86.957  84.738  93.104  1.00 51.36  ? 2422 GLY A CA    1 
ATOM   3844 C  C     . GLY A 1 631 ? 87.498  86.127  93.371  1.00 52.06  ? 2422 GLY A C     1 
ATOM   3845 O  O     . GLY A 1 631 ? 87.002  86.827  94.254  1.00 52.56  ? 2422 GLY A O     1 
ATOM   3846 N  N     . ILE A 1 632 ? 88.516  86.547  92.618  1.00 50.43  ? 2423 ILE A N     1 
ATOM   3847 C  CA    . ILE A 1 632 ? 89.050  87.898  92.775  1.00 43.26  ? 2423 ILE A CA    1 
ATOM   3848 C  C     . ILE A 1 632 ? 87.989  88.931  92.414  1.00 43.78  ? 2423 ILE A C     1 
ATOM   3849 O  O     . ILE A 1 632 ? 87.775  89.907  93.141  1.00 47.57  ? 2423 ILE A O     1 
ATOM   3850 C  CB    . ILE A 1 632 ? 90.322  88.077  91.928  1.00 44.32  ? 2423 ILE A CB    1 
ATOM   3851 C  CG1   . ILE A 1 632 ? 91.506  87.366  92.584  1.00 43.39  ? 2423 ILE A CG1   1 
ATOM   3852 C  CG2   . ILE A 1 632 ? 90.628  89.550  91.732  1.00 36.62  ? 2423 ILE A CG2   1 
ATOM   3853 C  CD1   . ILE A 1 632 ? 91.747  87.777  94.010  1.00 37.10  ? 2423 ILE A CD1   1 
ATOM   3854 N  N     . ASN A 1 633 ? 87.304  88.727  91.287  1.00 46.60  ? 2424 ASN A N     1 
ATOM   3855 C  CA    . ASN A 1 633 ? 86.239  89.645  90.893  1.00 50.18  ? 2424 ASN A CA    1 
ATOM   3856 C  C     . ASN A 1 633 ? 85.093  89.625  91.898  1.00 51.56  ? 2424 ASN A C     1 
ATOM   3857 O  O     . ASN A 1 633 ? 84.522  90.675  92.225  1.00 50.67  ? 2424 ASN A O     1 
ATOM   3858 C  CB    . ASN A 1 633 ? 85.738  89.292  89.493  1.00 54.50  ? 2424 ASN A CB    1 
ATOM   3859 C  CG    . ASN A 1 633 ? 84.779  90.326  88.939  1.00 59.39  ? 2424 ASN A CG    1 
ATOM   3860 O  OD1   . ASN A 1 633 ? 84.739  91.465  89.403  1.00 62.34  ? 2424 ASN A OD1   1 
ATOM   3861 N  ND2   . ASN A 1 633 ? 84.001  89.934  87.937  1.00 55.76  ? 2424 ASN A ND2   1 
ATOM   3862 N  N     . GLN A 1 634 ? 84.736  88.437  92.392  1.00 51.99  ? 2425 GLN A N     1 
ATOM   3863 C  CA    . GLN A 1 634 ? 83.690  88.348  93.407  1.00 51.20  ? 2425 GLN A CA    1 
ATOM   3864 C  C     . GLN A 1 634 ? 84.084  89.112  94.664  1.00 51.23  ? 2425 GLN A C     1 
ATOM   3865 O  O     . GLN A 1 634 ? 83.258  89.816  95.258  1.00 54.09  ? 2425 GLN A O     1 
ATOM   3866 C  CB    . GLN A 1 634 ? 83.399  86.884  93.735  1.00 50.93  ? 2425 GLN A CB    1 
ATOM   3867 C  CG    . GLN A 1 634 ? 82.823  86.093  92.574  1.00 53.31  ? 2425 GLN A CG    1 
ATOM   3868 C  CD    . GLN A 1 634 ? 82.792  84.602  92.844  1.00 62.50  ? 2425 GLN A CD    1 
ATOM   3869 O  OE1   . GLN A 1 634 ? 82.997  84.160  93.974  1.00 62.75  ? 2425 GLN A OE1   1 
ATOM   3870 N  NE2   . GLN A 1 634 ? 82.535  83.818  91.804  1.00 66.17  ? 2425 GLN A NE2   1 
ATOM   3871 N  N     . PHE A 1 635 ? 85.347  88.993  95.077  1.00 49.36  ? 2426 PHE A N     1 
ATOM   3872 C  CA    . PHE A 1 635 ? 85.832  89.742  96.229  1.00 50.98  ? 2426 PHE A CA    1 
ATOM   3873 C  C     . PHE A 1 635 ? 85.810  91.240  95.959  1.00 50.12  ? 2426 PHE A C     1 
ATOM   3874 O  O     . PHE A 1 635 ? 85.547  92.034  96.864  1.00 49.61  ? 2426 PHE A O     1 
ATOM   3875 C  CB    . PHE A 1 635 ? 87.242  89.282  96.593  1.00 44.83  ? 2426 PHE A CB    1 
ATOM   3876 C  CG    . PHE A 1 635 ? 87.899  90.115  97.655  1.00 41.06  ? 2426 PHE A CG    1 
ATOM   3877 C  CD1   . PHE A 1 635 ? 87.291  90.304  98.883  1.00 43.44  ? 2426 PHE A CD1   1 
ATOM   3878 C  CD2   . PHE A 1 635 ? 89.128  90.706  97.425  1.00 36.51  ? 2426 PHE A CD2   1 
ATOM   3879 C  CE1   . PHE A 1 635 ? 87.897  91.066  99.861  1.00 42.25  ? 2426 PHE A CE1   1 
ATOM   3880 C  CE2   . PHE A 1 635 ? 89.737  91.471  98.398  1.00 36.94  ? 2426 PHE A CE2   1 
ATOM   3881 C  CZ    . PHE A 1 635 ? 89.122  91.651  99.616  1.00 40.37  ? 2426 PHE A CZ    1 
ATOM   3882 N  N     . MET A 1 636 ? 86.096  91.644  94.721  1.00 48.33  ? 2427 MET A N     1 
ATOM   3883 C  CA    . MET A 1 636 ? 86.058  93.064  94.383  1.00 43.24  ? 2427 MET A CA    1 
ATOM   3884 C  C     . MET A 1 636 ? 84.648  93.618  94.537  1.00 46.72  ? 2427 MET A C     1 
ATOM   3885 O  O     . MET A 1 636 ? 84.442  94.680  95.143  1.00 47.35  ? 2427 MET A O     1 
ATOM   3886 C  CB    . MET A 1 636 ? 86.556  93.276  92.954  1.00 46.95  ? 2427 MET A CB    1 
ATOM   3887 C  CG    . MET A 1 636 ? 88.030  92.993  92.771  1.00 47.45  ? 2427 MET A CG    1 
ATOM   3888 S  SD    . MET A 1 636 ? 88.985  93.442  94.223  1.00 46.59  ? 2427 MET A SD    1 
ATOM   3889 C  CE    . MET A 1 636 ? 90.552  92.661  93.852  1.00 35.66  ? 2427 MET A CE    1 
ATOM   3890 N  N     . THR A 1 637 ? 83.660  92.905  93.991  1.00 52.02  ? 2428 THR A N     1 
ATOM   3891 C  CA    . THR A 1 637 ? 82.274  93.345  94.134  1.00 53.96  ? 2428 THR A CA    1 
ATOM   3892 C  C     . THR A 1 637 ? 81.835  93.331  95.594  1.00 52.93  ? 2428 THR A C     1 
ATOM   3893 O  O     . THR A 1 637 ? 81.122  94.237  96.041  1.00 54.57  ? 2428 THR A O     1 
ATOM   3894 C  CB    . THR A 1 637 ? 81.337  92.485  93.281  1.00 59.40  ? 2428 THR A CB    1 
ATOM   3895 O  OG1   . THR A 1 637 ? 81.082  91.237  93.940  1.00 60.79  ? 2428 THR A OG1   1 
ATOM   3896 C  CG2   . THR A 1 637 ? 81.920  92.243  91.900  1.00 55.03  ? 2428 THR A CG2   1 
ATOM   3897 N  N     . GLU A 1 638 ? 82.245  92.310  96.351  1.00 51.98  ? 2429 GLU A N     1 
ATOM   3898 C  CA    . GLU A 1 638 ? 81.896  92.255  97.768  1.00 53.84  ? 2429 GLU A CA    1 
ATOM   3899 C  C     . GLU A 1 638 ? 82.507  93.423  98.531  1.00 52.51  ? 2429 GLU A C     1 
ATOM   3900 O  O     . GLU A 1 638 ? 81.854  94.016  99.395  1.00 55.19  ? 2429 GLU A O     1 
ATOM   3901 C  CB    . GLU A 1 638 ? 82.347  90.925  98.369  1.00 55.63  ? 2429 GLU A CB    1 
ATOM   3902 C  CG    . GLU A 1 638 ? 81.469  89.745  97.986  1.00 60.66  ? 2429 GLU A CG    1 
ATOM   3903 C  CD    . GLU A 1 638 ? 80.137  89.746  98.711  1.00 69.22  ? 2429 GLU A CD    1 
ATOM   3904 O  OE1   . GLU A 1 638 ? 80.022  90.431  99.749  1.00 62.14  ? 2429 GLU A OE1   1 
ATOM   3905 O  OE2   . GLU A 1 638 ? 79.203  89.063  98.241  1.00 76.01  ? 2429 GLU A OE2   1 
ATOM   3906 N  N     . THR A 1 639 ? 83.760  93.765  98.226  1.00 47.79  ? 2430 THR A N     1 
ATOM   3907 C  CA    . THR A 1 639 ? 84.403  94.923  98.838  1.00 45.52  ? 2430 THR A CA    1 
ATOM   3908 C  C     . THR A 1 639 ? 83.651  96.207  98.530  1.00 47.64  ? 2430 THR A C     1 
ATOM   3909 O  O     . THR A 1 639 ? 83.393  97.018  99.426  1.00 47.23  ? 2430 THR A O     1 
ATOM   3910 C  CB    . THR A 1 639 ? 85.846  95.032  98.349  1.00 44.90  ? 2430 THR A CB    1 
ATOM   3911 O  OG1   . THR A 1 639 ? 86.618  93.929  98.841  1.00 42.08  ? 2430 THR A OG1   1 
ATOM   3912 C  CG2   . THR A 1 639 ? 86.457  96.363  98.752  1.00 40.32  ? 2430 THR A CG2   1 
ATOM   3913 N  N     . VAL A 1 640 ? 83.305  96.418  97.259  1.00 51.77  ? 2431 VAL A N     1 
ATOM   3914 C  CA    . VAL A 1 640 ? 82.607  97.647  96.892  1.00 50.81  ? 2431 VAL A CA    1 
ATOM   3915 C  C     . VAL A 1 640 ? 81.261  97.722  97.601  1.00 55.41  ? 2431 VAL A C     1 
ATOM   3916 O  O     . VAL A 1 640 ? 80.893  98.764  98.162  1.00 60.13  ? 2431 VAL A O     1 
ATOM   3917 C  CB    . VAL A 1 640 ? 82.455  97.740  95.363  1.00 50.81  ? 2431 VAL A CB    1 
ATOM   3918 C  CG1   . VAL A 1 640 ? 81.520  98.879  94.988  1.00 52.73  ? 2431 VAL A CG1   1 
ATOM   3919 C  CG2   . VAL A 1 640 ? 83.814  97.927  94.709  1.00 48.15  ? 2431 VAL A CG2   1 
ATOM   3920 N  N     . LYS A 1 641 ? 80.519  96.612  97.612  1.00 54.26  ? 2432 LYS A N     1 
ATOM   3921 C  CA    . LYS A 1 641 ? 79.212  96.593  98.261  1.00 54.77  ? 2432 LYS A CA    1 
ATOM   3922 C  C     . LYS A 1 641 ? 79.329  96.841  99.760  1.00 56.41  ? 2432 LYS A C     1 
ATOM   3923 O  O     . LYS A 1 641 ? 78.545  97.606  100.330 1.00 59.13  ? 2432 LYS A O     1 
ATOM   3924 C  CB    . LYS A 1 641 ? 78.518  95.259  97.989  1.00 55.34  ? 2432 LYS A CB    1 
ATOM   3925 C  CG    . LYS A 1 641 ? 77.096  95.171  98.515  1.00 61.31  ? 2432 LYS A CG    1 
ATOM   3926 C  CD    . LYS A 1 641 ? 76.585  93.740  98.474  1.00 64.73  ? 2432 LYS A CD    1 
ATOM   3927 C  CE    . LYS A 1 641 ? 76.848  93.096  97.121  1.00 61.22  ? 2432 LYS A CE    1 
ATOM   3928 N  NZ    . LYS A 1 641 ? 76.108  91.814  96.957  1.00 56.94  ? 2432 LYS A NZ    1 
ATOM   3929 N  N     . ASN A 1 642 ? 80.305  96.207  100.415 1.00 56.16  ? 2433 ASN A N     1 
ATOM   3930 C  CA    . ASN A 1 642 ? 80.465  96.375  101.855 1.00 57.30  ? 2433 ASN A CA    1 
ATOM   3931 C  C     . ASN A 1 642 ? 80.886  97.795  102.206 1.00 57.13  ? 2433 ASN A C     1 
ATOM   3932 O  O     . ASN A 1 642 ? 80.404  98.364  103.192 1.00 58.38  ? 2433 ASN A O     1 
ATOM   3933 C  CB    . ASN A 1 642 ? 81.479  95.365  102.392 1.00 54.91  ? 2433 ASN A CB    1 
ATOM   3934 C  CG    . ASN A 1 642 ? 80.945  93.946  102.394 1.00 55.49  ? 2433 ASN A CG    1 
ATOM   3935 O  OD1   . ASN A 1 642 ? 79.965  93.638  101.715 1.00 56.95  ? 2433 ASN A OD1   1 
ATOM   3936 N  ND2   . ASN A 1 642 ? 81.590  93.073  103.158 1.00 55.06  ? 2433 ASN A ND2   1 
ATOM   3937 N  N     . CYS A 1 643 ? 81.791  98.383  101.420 1.00 55.52  ? 2434 CYS A N     1 
ATOM   3938 C  CA    . CYS A 1 643 ? 82.204  99.757  101.679 1.00 53.00  ? 2434 CYS A CA    1 
ATOM   3939 C  C     . CYS A 1 643 ? 81.049  100.727 101.470 1.00 55.25  ? 2434 CYS A C     1 
ATOM   3940 O  O     . CYS A 1 643 ? 80.903  101.694 102.226 1.00 55.86  ? 2434 CYS A O     1 
ATOM   3941 C  CB    . CYS A 1 643 ? 83.388  100.129 100.788 1.00 50.86  ? 2434 CYS A CB    1 
ATOM   3942 S  SG    . CYS A 1 643 ? 84.297  101.589 101.339 1.00 52.04  ? 2434 CYS A SG    1 
ATOM   3943 N  N     . LYS A 1 644 ? 80.224  100.496 100.446 1.00 56.84  ? 2435 LYS A N     1 
ATOM   3944 C  CA    . LYS A 1 644 ? 79.056  101.347 100.246 1.00 59.42  ? 2435 LYS A CA    1 
ATOM   3945 C  C     . LYS A 1 644 ? 78.051  101.189 101.382 1.00 62.83  ? 2435 LYS A C     1 
ATOM   3946 O  O     . LYS A 1 644 ? 77.455  102.174 101.833 1.00 64.69  ? 2435 LYS A O     1 
ATOM   3947 C  CB    . LYS A 1 644 ? 78.400  101.035 98.902  1.00 58.67  ? 2435 LYS A CB    1 
ATOM   3948 C  CG    . LYS A 1 644 ? 79.205  101.494 97.698  1.00 60.70  ? 2435 LYS A CG    1 
ATOM   3949 C  CD    . LYS A 1 644 ? 78.297  101.923 96.558  1.00 63.04  ? 2435 LYS A CD    1 
ATOM   3950 C  CE    . LYS A 1 644 ? 77.567  103.214 96.892  1.00 64.61  ? 2435 LYS A CE    1 
ATOM   3951 N  NZ    . LYS A 1 644 ? 76.332  103.383 96.079  1.00 66.23  ? 2435 LYS A NZ    1 
ATOM   3952 N  N     . ARG A 1 645 ? 77.849  99.957  101.857 1.00 62.49  ? 2436 ARG A N     1 
ATOM   3953 C  CA    . ARG A 1 645 ? 76.830  99.710  102.871 1.00 62.03  ? 2436 ARG A CA    1 
ATOM   3954 C  C     . ARG A 1 645 ? 77.250  100.239 104.238 1.00 61.46  ? 2436 ARG A C     1 
ATOM   3955 O  O     . ARG A 1 645 ? 76.452  100.881 104.931 1.00 62.34  ? 2436 ARG A O     1 
ATOM   3956 C  CB    . ARG A 1 645 ? 76.528  98.213  102.947 1.00 59.95  ? 2436 ARG A CB    1 
ATOM   3957 C  CG    . ARG A 1 645 ? 75.561  97.822  104.050 1.00 60.03  ? 2436 ARG A CG    1 
ATOM   3958 C  CD    . ARG A 1 645 ? 75.235  96.340  103.988 1.00 64.97  ? 2436 ARG A CD    1 
ATOM   3959 N  NE    . ARG A 1 645 ? 76.439  95.520  103.910 1.00 68.33  ? 2436 ARG A NE    1 
ATOM   3960 C  CZ    . ARG A 1 645 ? 77.060  94.999  104.959 1.00 68.65  ? 2436 ARG A CZ    1 
ATOM   3961 N  NH1   . ARG A 1 645 ? 76.613  95.186  106.190 1.00 68.96  ? 2436 ARG A NH1   1 
ATOM   3962 N  NH2   . ARG A 1 645 ? 78.156  94.271  104.768 1.00 64.55  ? 2436 ARG A NH2   1 
ATOM   3963 N  N     . ASP A 1 646 ? 78.495  99.986  104.642 1.00 60.11  ? 2437 ASP A N     1 
ATOM   3964 C  CA    . ASP A 1 646 ? 78.945  100.314 105.988 1.00 58.30  ? 2437 ASP A CA    1 
ATOM   3965 C  C     . ASP A 1 646 ? 79.673  101.647 106.082 1.00 59.74  ? 2437 ASP A C     1 
ATOM   3966 O  O     . ASP A 1 646 ? 79.758  102.210 107.179 1.00 59.17  ? 2437 ASP A O     1 
ATOM   3967 C  CB    . ASP A 1 646 ? 79.866  99.210  106.522 1.00 57.16  ? 2437 ASP A CB    1 
ATOM   3968 C  CG    . ASP A 1 646 ? 79.140  97.897  106.737 1.00 65.40  ? 2437 ASP A CG    1 
ATOM   3969 O  OD1   . ASP A 1 646 ? 77.913  97.850  106.512 1.00 67.70  ? 2437 ASP A OD1   1 
ATOM   3970 O  OD2   . ASP A 1 646 ? 79.797  96.911  107.131 1.00 68.86  ? 2437 ASP A OD2   1 
ATOM   3971 N  N     . GLY A 1 647 ? 80.195  102.163 104.973 1.00 62.32  ? 2438 GLY A N     1 
ATOM   3972 C  CA    . GLY A 1 647 ? 80.972  103.382 104.991 1.00 59.31  ? 2438 GLY A CA    1 
ATOM   3973 C  C     . GLY A 1 647 ? 82.437  103.196 105.311 1.00 57.11  ? 2438 GLY A C     1 
ATOM   3974 O  O     . GLY A 1 647 ? 83.193  104.174 105.264 1.00 55.65  ? 2438 GLY A O     1 
ATOM   3975 N  N     . PHE A 1 648 ? 82.862  101.977 105.634 1.00 53.91  ? 2439 PHE A N     1 
ATOM   3976 C  CA    . PHE A 1 648 ? 84.256  101.692 105.939 1.00 46.84  ? 2439 PHE A CA    1 
ATOM   3977 C  C     . PHE A 1 648 ? 84.580  100.288 105.446 1.00 47.57  ? 2439 PHE A C     1 
ATOM   3978 O  O     . PHE A 1 648 ? 83.698  99.537  105.023 1.00 53.29  ? 2439 PHE A O     1 
ATOM   3979 C  CB    . PHE A 1 648 ? 84.537  101.843 107.437 1.00 46.75  ? 2439 PHE A CB    1 
ATOM   3980 C  CG    . PHE A 1 648 ? 83.729  100.921 108.307 1.00 50.56  ? 2439 PHE A CG    1 
ATOM   3981 C  CD1   . PHE A 1 648 ? 82.475  101.294 108.758 1.00 53.97  ? 2439 PHE A CD1   1 
ATOM   3982 C  CD2   . PHE A 1 648 ? 84.228  99.685  108.683 1.00 47.67  ? 2439 PHE A CD2   1 
ATOM   3983 C  CE1   . PHE A 1 648 ? 81.733  100.450 109.561 1.00 56.60  ? 2439 PHE A CE1   1 
ATOM   3984 C  CE2   . PHE A 1 648 ? 83.490  98.838  109.485 1.00 47.17  ? 2439 PHE A CE2   1 
ATOM   3985 C  CZ    . PHE A 1 648 ? 82.242  99.220  109.924 1.00 51.31  ? 2439 PHE A CZ    1 
ATOM   3986 N  N     . VAL A 1 649 ? 85.862  99.938  105.501 1.00 43.43  ? 2440 VAL A N     1 
ATOM   3987 C  CA    . VAL A 1 649 ? 86.338  98.619  105.106 1.00 37.58  ? 2440 VAL A CA    1 
ATOM   3988 C  C     . VAL A 1 649 ? 87.170  98.046  106.241 1.00 38.92  ? 2440 VAL A C     1 
ATOM   3989 O  O     . VAL A 1 649 ? 88.034  98.730  106.800 1.00 40.13  ? 2440 VAL A O     1 
ATOM   3990 C  CB    . VAL A 1 649 ? 87.153  98.669  103.799 1.00 31.54  ? 2440 VAL A CB    1 
ATOM   3991 C  CG1   . VAL A 1 649 ? 86.221  98.738  102.608 1.00 35.94  ? 2440 VAL A CG1   1 
ATOM   3992 C  CG2   . VAL A 1 649 ? 88.099  99.855  103.807 1.00 35.82  ? 2440 VAL A CG2   1 
ATOM   3993 N  N     . GLN A 1 650 ? 86.910  96.788  106.580 1.00 36.97  ? 2441 GLN A N     1 
ATOM   3994 C  CA    . GLN A 1 650 ? 87.514  96.145  107.737 1.00 33.29  ? 2441 GLN A CA    1 
ATOM   3995 C  C     . GLN A 1 650 ? 88.736  95.344  107.310 1.00 31.48  ? 2441 GLN A C     1 
ATOM   3996 O  O     . GLN A 1 650 ? 88.661  94.531  106.383 1.00 30.51  ? 2441 GLN A O     1 
ATOM   3997 C  CB    . GLN A 1 650 ? 86.503  95.238  108.437 1.00 35.26  ? 2441 GLN A CB    1 
ATOM   3998 C  CG    . GLN A 1 650 ? 86.718  95.098  109.930 1.00 38.91  ? 2441 GLN A CG    1 
ATOM   3999 C  CD    . GLN A 1 650 ? 85.618  94.301  110.597 1.00 45.80  ? 2441 GLN A CD    1 
ATOM   4000 O  OE1   . GLN A 1 650 ? 84.605  94.855  111.023 1.00 43.77  ? 2441 GLN A OE1   1 
ATOM   4001 N  NE2   . GLN A 1 650 ? 85.809  92.990  110.689 1.00 50.86  ? 2441 GLN A NE2   1 
ATOM   4002 N  N     . THR A 1 651 ? 89.852  95.572  107.996 1.00 29.02  ? 2442 THR A N     1 
ATOM   4003 C  CA    . THR A 1 651 ? 91.084  94.844  107.742 1.00 26.80  ? 2442 THR A CA    1 
ATOM   4004 C  C     . THR A 1 651 ? 90.955  93.421  108.300 1.00 34.89  ? 2442 THR A C     1 
ATOM   4005 O  O     . THR A 1 651 ? 89.945  93.053  108.907 1.00 42.07  ? 2442 THR A O     1 
ATOM   4006 C  CB    . THR A 1 651 ? 92.255  95.618  108.347 1.00 24.20  ? 2442 THR A CB    1 
ATOM   4007 O  OG1   . THR A 1 651 ? 92.141  96.994  107.970 1.00 26.29  ? 2442 THR A OG1   1 
ATOM   4008 C  CG2   . THR A 1 651 ? 93.586  95.121  107.834 1.00 23.66  ? 2442 THR A CG2   1 
ATOM   4009 N  N     . ILE A 1 652 ? 91.990  92.602  108.087 1.00 30.72  ? 2443 ILE A N     1 
ATOM   4010 C  CA    . ILE A 1 652 ? 91.929  91.193  108.471 1.00 29.60  ? 2443 ILE A CA    1 
ATOM   4011 C  C     . ILE A 1 652 ? 91.750  91.036  109.976 1.00 31.96  ? 2443 ILE A C     1 
ATOM   4012 O  O     . ILE A 1 652 ? 91.214  90.022  110.441 1.00 32.51  ? 2443 ILE A O     1 
ATOM   4013 C  CB    . ILE A 1 652 ? 93.182  90.448  107.966 1.00 29.36  ? 2443 ILE A CB    1 
ATOM   4014 C  CG1   . ILE A 1 652 ? 92.914  88.945  107.881 1.00 32.28  ? 2443 ILE A CG1   1 
ATOM   4015 C  CG2   . ILE A 1 652 ? 94.380  90.720  108.863 1.00 28.75  ? 2443 ILE A CG2   1 
ATOM   4016 C  CD1   . ILE A 1 652 ? 94.112  88.143  107.433 1.00 27.58  ? 2443 ILE A CD1   1 
ATOM   4017 N  N     . LEU A 1 653 ? 92.186  92.021  110.760 1.00 31.95  ? 2444 LEU A N     1 
ATOM   4018 C  CA    . LEU A 1 653 ? 92.005  91.989  112.205 1.00 34.55  ? 2444 LEU A CA    1 
ATOM   4019 C  C     . LEU A 1 653 ? 90.933  92.941  112.705 1.00 32.35  ? 2444 LEU A C     1 
ATOM   4020 O  O     . LEU A 1 653 ? 90.383  92.716  113.784 1.00 38.30  ? 2444 LEU A O     1 
ATOM   4021 C  CB    . LEU A 1 653 ? 93.322  92.310  112.919 1.00 34.90  ? 2444 LEU A CB    1 
ATOM   4022 C  CG    . LEU A 1 653 ? 94.392  91.217  112.896 1.00 34.08  ? 2444 LEU A CG    1 
ATOM   4023 C  CD1   . LEU A 1 653 ? 95.344  91.404  114.060 1.00 32.13  ? 2444 LEU A CD1   1 
ATOM   4024 C  CD2   . LEU A 1 653 ? 93.767  89.830  112.925 1.00 33.74  ? 2444 LEU A CD2   1 
ATOM   4025 N  N     . GLY A 1 654 ? 90.626  93.995  111.956 1.00 28.08  ? 2445 GLY A N     1 
ATOM   4026 C  CA    . GLY A 1 654 ? 89.550  94.883  112.341 1.00 33.88  ? 2445 GLY A CA    1 
ATOM   4027 C  C     . GLY A 1 654 ? 89.933  96.345  112.416 1.00 36.64  ? 2445 GLY A C     1 
ATOM   4028 O  O     . GLY A 1 654 ? 89.168  97.154  112.944 1.00 42.21  ? 2445 GLY A O     1 
ATOM   4029 N  N     . ARG A 1 655 ? 91.107  96.704  111.894 1.00 30.93  ? 2446 ARG A N     1 
ATOM   4030 C  CA    . ARG A 1 655 ? 91.528  98.105  111.847 1.00 27.13  ? 2446 ARG A CA    1 
ATOM   4031 C  C     . ARG A 1 655 ? 90.786  98.806  110.710 1.00 28.74  ? 2446 ARG A C     1 
ATOM   4032 O  O     . ARG A 1 655 ? 91.322  99.069  109.632 1.00 33.77  ? 2446 ARG A O     1 
ATOM   4033 C  CB    . ARG A 1 655 ? 93.035  98.215  111.676 1.00 27.65  ? 2446 ARG A CB    1 
ATOM   4034 C  CG    . ARG A 1 655 ? 93.843  97.314  112.581 1.00 30.83  ? 2446 ARG A CG    1 
ATOM   4035 C  CD    . ARG A 1 655 ? 95.332  97.598  112.452 1.00 30.87  ? 2446 ARG A CD    1 
ATOM   4036 N  NE    . ARG A 1 655 ? 95.851  97.283  111.126 1.00 29.04  ? 2446 ARG A NE    1 
ATOM   4037 C  CZ    . ARG A 1 655 ? 96.022  98.171  110.155 1.00 26.22  ? 2446 ARG A CZ    1 
ATOM   4038 N  NH1   . ARG A 1 655 ? 95.701  99.443  110.317 1.00 26.30  ? 2446 ARG A NH1   1 
ATOM   4039 N  NH2   . ARG A 1 655 ? 96.521  97.770  108.991 1.00 26.40  ? 2446 ARG A NH2   1 
ATOM   4040 N  N     . ARG A 1 656 ? 89.521  99.114  110.977 1.00 32.25  ? 2447 ARG A N     1 
ATOM   4041 C  CA    . ARG A 1 656 ? 88.652  99.672  109.953 1.00 34.22  ? 2447 ARG A CA    1 
ATOM   4042 C  C     . ARG A 1 656 ? 89.178  101.016 109.468 1.00 36.26  ? 2447 ARG A C     1 
ATOM   4043 O  O     . ARG A 1 656 ? 89.695  101.821 110.247 1.00 39.68  ? 2447 ARG A O     1 
ATOM   4044 C  CB    . ARG A 1 656 ? 87.231  99.823  110.495 1.00 37.58  ? 2447 ARG A CB    1 
ATOM   4045 C  CG    . ARG A 1 656 ? 87.121  100.722 111.712 1.00 40.96  ? 2447 ARG A CG    1 
ATOM   4046 C  CD    . ARG A 1 656 ? 86.000  100.272 112.630 1.00 43.61  ? 2447 ARG A CD    1 
ATOM   4047 N  NE    . ARG A 1 656 ? 85.947  98.820  112.753 1.00 43.90  ? 2447 ARG A NE    1 
ATOM   4048 C  CZ    . ARG A 1 656 ? 84.882  98.142  113.157 1.00 48.19  ? 2447 ARG A CZ    1 
ATOM   4049 N  NH1   . ARG A 1 656 ? 83.756  98.755  113.484 1.00 48.83  ? 2447 ARG A NH1   1 
ATOM   4050 N  NH2   . ARG A 1 656 ? 84.948  96.817  113.235 1.00 48.63  ? 2447 ARG A NH2   1 
ATOM   4051 N  N     . ARG A 1 657 ? 89.063  101.243 108.163 1.00 34.85  ? 2448 ARG A N     1 
ATOM   4052 C  CA    . ARG A 1 657 ? 89.407  102.515 107.544 1.00 35.18  ? 2448 ARG A CA    1 
ATOM   4053 C  C     . ARG A 1 657 ? 88.136  103.122 106.972 1.00 38.77  ? 2448 ARG A C     1 
ATOM   4054 O  O     . ARG A 1 657 ? 87.449  102.485 106.167 1.00 38.84  ? 2448 ARG A O     1 
ATOM   4055 C  CB    . ARG A 1 657 ? 90.460  102.334 106.454 1.00 32.27  ? 2448 ARG A CB    1 
ATOM   4056 C  CG    . ARG A 1 657 ? 90.812  103.613 105.721 1.00 37.25  ? 2448 ARG A CG    1 
ATOM   4057 C  CD    . ARG A 1 657 ? 92.103  103.457 104.943 1.00 34.94  ? 2448 ARG A CD    1 
ATOM   4058 N  NE    . ARG A 1 657 ? 92.512  104.701 104.302 1.00 35.83  ? 2448 ARG A NE    1 
ATOM   4059 C  CZ    . ARG A 1 657 ? 92.428  104.935 103.001 1.00 29.95  ? 2448 ARG A CZ    1 
ATOM   4060 N  NH1   . ARG A 1 657 ? 91.946  104.030 102.167 1.00 30.10  ? 2448 ARG A NH1   1 
ATOM   4061 N  NH2   . ARG A 1 657 ? 92.839  106.105 102.524 1.00 32.31  ? 2448 ARG A NH2   1 
ATOM   4062 N  N     . TYR A 1 658 ? 87.826  104.346 107.385 1.00 42.50  ? 2449 TYR A N     1 
ATOM   4063 C  CA    . TYR A 1 658 ? 86.590  105.002 106.987 1.00 43.86  ? 2449 TYR A CA    1 
ATOM   4064 C  C     . TYR A 1 658 ? 86.798  105.733 105.670 1.00 45.69  ? 2449 TYR A C     1 
ATOM   4065 O  O     . TYR A 1 658 ? 87.714  106.552 105.542 1.00 47.82  ? 2449 TYR A O     1 
ATOM   4066 C  CB    . TYR A 1 658 ? 86.122  105.968 108.073 1.00 45.63  ? 2449 TYR A CB    1 
ATOM   4067 C  CG    . TYR A 1 658 ? 85.556  105.269 109.286 1.00 46.87  ? 2449 TYR A CG    1 
ATOM   4068 C  CD1   . TYR A 1 658 ? 86.391  104.787 110.285 1.00 44.42  ? 2449 TYR A CD1   1 
ATOM   4069 C  CD2   . TYR A 1 658 ? 84.189  105.078 109.426 1.00 50.36  ? 2449 TYR A CD2   1 
ATOM   4070 C  CE1   . TYR A 1 658 ? 85.879  104.142 111.392 1.00 49.58  ? 2449 TYR A CE1   1 
ATOM   4071 C  CE2   . TYR A 1 658 ? 83.668  104.435 110.529 1.00 54.10  ? 2449 TYR A CE2   1 
ATOM   4072 C  CZ    . TYR A 1 658 ? 84.518  103.969 111.509 1.00 55.33  ? 2449 TYR A CZ    1 
ATOM   4073 O  OH    . TYR A 1 658 ? 84.003  103.328 112.610 1.00 55.74  ? 2449 TYR A OH    1 
ATOM   4074 N  N     . LEU A 1 659 ? 85.947  105.432 104.693 1.00 47.08  ? 2450 LEU A N     1 
ATOM   4075 C  CA    . LEU A 1 659 ? 86.034  106.003 103.351 1.00 47.93  ? 2450 LEU A CA    1 
ATOM   4076 C  C     . LEU A 1 659 ? 84.678  106.587 102.984 1.00 53.20  ? 2450 LEU A C     1 
ATOM   4077 O  O     . LEU A 1 659 ? 83.868  105.935 102.311 1.00 57.31  ? 2450 LEU A O     1 
ATOM   4078 C  CB    . LEU A 1 659 ? 86.480  104.953 102.334 1.00 42.12  ? 2450 LEU A CB    1 
ATOM   4079 C  CG    . LEU A 1 659 ? 87.863  104.354 102.579 1.00 33.45  ? 2450 LEU A CG    1 
ATOM   4080 C  CD1   . LEU A 1 659 ? 88.147  103.256 101.583 1.00 30.27  ? 2450 LEU A CD1   1 
ATOM   4081 C  CD2   . LEU A 1 659 ? 88.927  105.433 102.503 1.00 35.40  ? 2450 LEU A CD2   1 
ATOM   4082 N  N     . PRO A 1 660 ? 84.392  107.817 103.419 1.00 52.43  ? 2451 PRO A N     1 
ATOM   4083 C  CA    . PRO A 1 660 ? 83.128  108.454 103.016 1.00 56.15  ? 2451 PRO A CA    1 
ATOM   4084 C  C     . PRO A 1 660 ? 83.045  108.726 101.526 1.00 61.67  ? 2451 PRO A C     1 
ATOM   4085 O  O     . PRO A 1 660 ? 81.933  108.877 101.001 1.00 65.17  ? 2451 PRO A O     1 
ATOM   4086 C  CB    . PRO A 1 660 ? 83.102  109.757 103.827 1.00 56.49  ? 2451 PRO A CB    1 
ATOM   4087 C  CG    . PRO A 1 660 ? 84.485  109.964 104.338 1.00 53.77  ? 2451 PRO A CG    1 
ATOM   4088 C  CD    . PRO A 1 660 ? 85.309  108.739 104.108 1.00 52.30  ? 2451 PRO A CD    1 
ATOM   4089 N  N     . GLY A 1 661 ? 84.179  108.767 100.825 1.00 59.34  ? 2452 GLY A N     1 
ATOM   4090 C  CA    . GLY A 1 661 ? 84.180  108.983 99.390  1.00 60.05  ? 2452 GLY A CA    1 
ATOM   4091 C  C     . GLY A 1 661 ? 83.473  107.903 98.602  1.00 60.81  ? 2452 GLY A C     1 
ATOM   4092 O  O     . GLY A 1 661 ? 83.181  108.113 97.419  1.00 65.93  ? 2452 GLY A O     1 
ATOM   4093 N  N     . ILE A 1 662 ? 83.198  106.752 99.221  1.00 56.05  ? 2453 ILE A N     1 
ATOM   4094 C  CA    . ILE A 1 662 ? 82.403  105.722 98.569  1.00 58.15  ? 2453 ILE A CA    1 
ATOM   4095 C  C     . ILE A 1 662 ? 80.982  106.201 98.310  1.00 67.56  ? 2453 ILE A C     1 
ATOM   4096 O  O     . ILE A 1 662 ? 80.272  105.611 97.490  1.00 71.76  ? 2453 ILE A O     1 
ATOM   4097 C  CB    . ILE A 1 662 ? 82.410  104.428 99.410  1.00 57.45  ? 2453 ILE A CB    1 
ATOM   4098 C  CG1   . ILE A 1 662 ? 82.423  103.200 98.500  1.00 54.69  ? 2453 ILE A CG1   1 
ATOM   4099 C  CG2   . ILE A 1 662 ? 81.219  104.389 100.357 1.00 60.95  ? 2453 ILE A CG2   1 
ATOM   4100 C  CD1   . ILE A 1 662 ? 83.789  102.853 97.969  1.00 48.80  ? 2453 ILE A CD1   1 
ATOM   4101 N  N     . LYS A 1 663 ? 80.544  107.258 98.995  1.00 70.87  ? 2454 LYS A N     1 
ATOM   4102 C  CA    . LYS A 1 663 ? 79.233  107.846 98.764  1.00 74.30  ? 2454 LYS A CA    1 
ATOM   4103 C  C     . LYS A 1 663 ? 79.310  109.125 97.938  1.00 74.98  ? 2454 LYS A C     1 
ATOM   4104 O  O     . LYS A 1 663 ? 78.320  109.860 97.850  1.00 78.55  ? 2454 LYS A O     1 
ATOM   4105 C  CB    . LYS A 1 663 ? 78.529  108.111 100.095 1.00 73.33  ? 2454 LYS A CB    1 
ATOM   4106 C  CG    . LYS A 1 663 ? 77.886  106.877 100.703 1.00 75.61  ? 2454 LYS A CG    1 
ATOM   4107 C  CD    . LYS A 1 663 ? 76.967  107.241 101.856 1.00 85.32  ? 2454 LYS A CD    1 
ATOM   4108 C  CE    . LYS A 1 663 ? 76.174  106.033 102.326 1.00 88.05  ? 2454 LYS A CE    1 
ATOM   4109 N  NZ    . LYS A 1 663 ? 77.067  104.935 102.790 1.00 78.36  ? 2454 LYS A NZ    1 
ATOM   4110 N  N     . ASP A 1 664 ? 80.462  109.404 97.336  1.00 72.21  ? 2455 ASP A N     1 
ATOM   4111 C  CA    . ASP A 1 664 ? 80.618  110.591 96.512  1.00 77.30  ? 2455 ASP A CA    1 
ATOM   4112 C  C     . ASP A 1 664 ? 79.791  110.472 95.235  1.00 80.25  ? 2455 ASP A C     1 
ATOM   4113 O  O     . ASP A 1 664 ? 79.532  109.378 94.726  1.00 78.24  ? 2455 ASP A O     1 
ATOM   4114 C  CB    . ASP A 1 664 ? 82.090  110.811 96.163  1.00 75.01  ? 2455 ASP A CB    1 
ATOM   4115 C  CG    . ASP A 1 664 ? 82.489  112.272 96.203  1.00 78.46  ? 2455 ASP A CG    1 
ATOM   4116 O  OD1   . ASP A 1 664 ? 81.722  113.114 95.691  1.00 78.06  ? 2455 ASP A OD1   1 
ATOM   4117 O  OD2   . ASP A 1 664 ? 83.568  112.578 96.749  1.00 79.31  ? 2455 ASP A OD2   1 
ATOM   4118 N  N     . ASN A 1 665 ? 79.374  111.626 94.717  1.00 80.32  ? 2456 ASN A N     1 
ATOM   4119 C  CA    . ASN A 1 665 ? 78.617  111.686 93.474  1.00 80.33  ? 2456 ASN A CA    1 
ATOM   4120 C  C     . ASN A 1 665 ? 79.500  111.833 92.245  1.00 78.60  ? 2456 ASN A C     1 
ATOM   4121 O  O     . ASN A 1 665 ? 79.097  111.417 91.154  1.00 77.89  ? 2456 ASN A O     1 
ATOM   4122 C  CB    . ASN A 1 665 ? 77.618  112.846 93.515  1.00 84.58  ? 2456 ASN A CB    1 
ATOM   4123 C  CG    . ASN A 1 665 ? 76.641  112.732 94.668  1.00 85.02  ? 2456 ASN A CG    1 
ATOM   4124 O  OD1   . ASN A 1 665 ? 76.257  111.631 95.064  1.00 82.13  ? 2456 ASN A OD1   1 
ATOM   4125 N  ND2   . ASN A 1 665 ? 76.233  113.872 95.214  1.00 86.38  ? 2456 ASN A ND2   1 
ATOM   4126 N  N     . ASN A 1 666 ? 80.684  112.412 92.394  1.00 77.84  ? 2457 ASN A N     1 
ATOM   4127 C  CA    . ASN A 1 666 ? 81.606  112.525 91.273  1.00 77.31  ? 2457 ASN A CA    1 
ATOM   4128 C  C     . ASN A 1 666 ? 82.104  111.137 90.884  1.00 76.16  ? 2457 ASN A C     1 
ATOM   4129 O  O     . ASN A 1 666 ? 82.589  110.396 91.748  1.00 74.64  ? 2457 ASN A O     1 
ATOM   4130 C  CB    . ASN A 1 666 ? 82.776  113.434 91.641  1.00 75.40  ? 2457 ASN A CB    1 
ATOM   4131 C  CG    . ASN A 1 666 ? 83.833  113.492 90.559  1.00 73.60  ? 2457 ASN A CG    1 
ATOM   4132 O  OD1   . ASN A 1 666 ? 84.804  112.738 90.584  1.00 74.63  ? 2457 ASN A OD1   1 
ATOM   4133 N  ND2   . ASN A 1 666 ? 83.651  114.393 89.602  1.00 74.21  ? 2457 ASN A ND2   1 
ATOM   4134 N  N     . PRO A 1 667 ? 81.985  110.741 89.613  1.00 77.15  ? 2458 PRO A N     1 
ATOM   4135 C  CA    . PRO A 1 667 ? 82.388  109.373 89.237  1.00 75.92  ? 2458 PRO A CA    1 
ATOM   4136 C  C     . PRO A 1 667 ? 83.843  109.057 89.534  1.00 71.77  ? 2458 PRO A C     1 
ATOM   4137 O  O     . PRO A 1 667 ? 84.150  107.940 89.971  1.00 70.01  ? 2458 PRO A O     1 
ATOM   4138 C  CB    . PRO A 1 667 ? 82.091  109.327 87.730  1.00 76.82  ? 2458 PRO A CB    1 
ATOM   4139 C  CG    . PRO A 1 667 ? 81.077  110.403 87.505  1.00 76.12  ? 2458 PRO A CG    1 
ATOM   4140 C  CD    . PRO A 1 667 ? 81.423  111.488 88.477  1.00 76.26  ? 2458 PRO A CD    1 
ATOM   4141 N  N     . TYR A 1 668 ? 84.753  110.011 89.316  1.00 71.96  ? 2459 TYR A N     1 
ATOM   4142 C  CA    . TYR A 1 668 ? 86.161  109.749 89.593  1.00 70.04  ? 2459 TYR A CA    1 
ATOM   4143 C  C     . TYR A 1 668 ? 86.404  109.534 91.079  1.00 67.46  ? 2459 TYR A C     1 
ATOM   4144 O  O     . TYR A 1 668 ? 87.161  108.638 91.464  1.00 67.07  ? 2459 TYR A O     1 
ATOM   4145 C  CB    . TYR A 1 668 ? 87.035  110.890 89.077  1.00 73.73  ? 2459 TYR A CB    1 
ATOM   4146 C  CG    . TYR A 1 668 ? 88.469  110.787 89.550  1.00 76.88  ? 2459 TYR A CG    1 
ATOM   4147 C  CD1   . TYR A 1 668 ? 89.313  109.802 89.057  1.00 75.78  ? 2459 TYR A CD1   1 
ATOM   4148 C  CD2   . TYR A 1 668 ? 88.973  111.666 90.498  1.00 79.69  ? 2459 TYR A CD2   1 
ATOM   4149 C  CE1   . TYR A 1 668 ? 90.621  109.699 89.489  1.00 75.67  ? 2459 TYR A CE1   1 
ATOM   4150 C  CE2   . TYR A 1 668 ? 90.280  111.571 90.936  1.00 79.05  ? 2459 TYR A CE2   1 
ATOM   4151 C  CZ    . TYR A 1 668 ? 91.099  110.586 90.428  1.00 76.90  ? 2459 TYR A CZ    1 
ATOM   4152 O  OH    . TYR A 1 668 ? 92.402  110.487 90.861  1.00 72.80  ? 2459 TYR A OH    1 
ATOM   4153 N  N     . ARG A 1 669 ? 85.782  110.354 91.930  1.00 68.44  ? 2460 ARG A N     1 
ATOM   4154 C  CA    . ARG A 1 669 ? 85.961  110.194 93.369  1.00 68.41  ? 2460 ARG A CA    1 
ATOM   4155 C  C     . ARG A 1 669 ? 85.396  108.863 93.849  1.00 62.29  ? 2460 ARG A C     1 
ATOM   4156 O  O     . ARG A 1 669 ? 86.009  108.183 94.678  1.00 57.25  ? 2460 ARG A O     1 
ATOM   4157 C  CB    . ARG A 1 669 ? 85.307  111.358 94.112  1.00 72.33  ? 2460 ARG A CB    1 
ATOM   4158 C  CG    . ARG A 1 669 ? 85.829  112.724 93.700  1.00 75.74  ? 2460 ARG A CG    1 
ATOM   4159 C  CD    . ARG A 1 669 ? 86.027  113.628 94.907  1.00 79.12  ? 2460 ARG A CD    1 
ATOM   4160 N  NE    . ARG A 1 669 ? 86.735  114.856 94.567  1.00 87.69  ? 2460 ARG A NE    1 
ATOM   4161 C  CZ    . ARG A 1 669 ? 88.035  114.929 94.313  1.00 94.43  ? 2460 ARG A CZ    1 
ATOM   4162 N  NH1   . ARG A 1 669 ? 88.810  113.858 94.362  1.00 93.31  ? 2460 ARG A NH1   1 
ATOM   4163 N  NH2   . ARG A 1 669 ? 88.571  116.107 94.008  1.00 93.36  ? 2460 ARG A NH2   1 
ATOM   4164 N  N     . LYS A 1 670 ? 84.229  108.472 93.332  1.00 63.45  ? 2461 LYS A N     1 
ATOM   4165 C  CA    . LYS A 1 670 ? 83.646  107.186 93.698  1.00 60.71  ? 2461 LYS A CA    1 
ATOM   4166 C  C     . LYS A 1 670 ? 84.536  106.029 93.262  1.00 55.86  ? 2461 LYS A C     1 
ATOM   4167 O  O     . LYS A 1 670 ? 84.752  105.077 94.023  1.00 53.87  ? 2461 LYS A O     1 
ATOM   4168 C  CB    . LYS A 1 670 ? 82.255  107.056 93.078  1.00 67.20  ? 2461 LYS A CB    1 
ATOM   4169 C  CG    . LYS A 1 670 ? 81.655  105.666 93.160  1.00 62.57  ? 2461 LYS A CG    1 
ATOM   4170 C  CD    . LYS A 1 670 ? 80.729  105.534 94.351  1.00 61.16  ? 2461 LYS A CD    1 
ATOM   4171 C  CE    . LYS A 1 670 ? 79.788  104.354 94.185  1.00 65.16  ? 2461 LYS A CE    1 
ATOM   4172 N  NZ    . LYS A 1 670 ? 78.681  104.657 93.236  1.00 67.54  ? 2461 LYS A NZ    1 
ATOM   4173 N  N     . ALA A 1 671 ? 85.063  106.092 92.036  1.00 59.05  ? 2462 ALA A N     1 
ATOM   4174 C  CA    . ALA A 1 671 ? 85.941  105.030 91.557  1.00 57.40  ? 2462 ALA A CA    1 
ATOM   4175 C  C     . ALA A 1 671 ? 87.221  104.963 92.379  1.00 50.12  ? 2462 ALA A C     1 
ATOM   4176 O  O     . ALA A 1 671 ? 87.699  103.871 92.708  1.00 50.26  ? 2462 ALA A O     1 
ATOM   4177 C  CB    . ALA A 1 671 ? 86.261  105.241 90.078  1.00 62.28  ? 2462 ALA A CB    1 
ATOM   4178 N  N     . HIS A 1 672 ? 87.792  106.121 92.716  1.00 48.42  ? 2463 HIS A N     1 
ATOM   4179 C  CA    . HIS A 1 672 ? 88.987  106.142 93.549  1.00 42.52  ? 2463 HIS A CA    1 
ATOM   4180 C  C     . HIS A 1 672 ? 88.702  105.569 94.928  1.00 43.37  ? 2463 HIS A C     1 
ATOM   4181 O  O     . HIS A 1 672 ? 89.539  104.863 95.495  1.00 43.83  ? 2463 HIS A O     1 
ATOM   4182 C  CB    . HIS A 1 672 ? 89.529  107.565 93.661  1.00 46.71  ? 2463 HIS A CB    1 
ATOM   4183 C  CG    . HIS A 1 672 ? 90.744  107.680 94.526  1.00 39.78  ? 2463 HIS A CG    1 
ATOM   4184 N  ND1   . HIS A 1 672 ? 91.754  106.743 94.517  1.00 34.68  ? 2463 HIS A ND1   1 
ATOM   4185 C  CD2   . HIS A 1 672 ? 91.115  108.623 95.423  1.00 39.64  ? 2463 HIS A CD2   1 
ATOM   4186 C  CE1   . HIS A 1 672 ? 92.694  107.103 95.372  1.00 34.23  ? 2463 HIS A CE1   1 
ATOM   4187 N  NE2   . HIS A 1 672 ? 92.331  108.240 95.936  1.00 36.00  ? 2463 HIS A NE2   1 
ATOM   4188 N  N     . ALA A 1 673 ? 87.526  105.867 95.485  1.00 47.21  ? 2464 ALA A N     1 
ATOM   4189 C  CA    . ALA A 1 673 ? 87.161  105.306 96.781  1.00 46.06  ? 2464 ALA A CA    1 
ATOM   4190 C  C     . ALA A 1 673 ? 87.025  103.792 96.710  1.00 45.27  ? 2464 ALA A C     1 
ATOM   4191 O  O     . ALA A 1 673 ? 87.481  103.079 97.610  1.00 44.72  ? 2464 ALA A O     1 
ATOM   4192 C  CB    . ALA A 1 673 ? 85.865  105.937 97.282  1.00 51.11  ? 2464 ALA A CB    1 
ATOM   4193 N  N     . GLU A 1 674 ? 86.402  103.280 95.647  1.00 45.02  ? 2465 GLU A N     1 
ATOM   4194 C  CA    . GLU A 1 674 ? 86.294  101.832 95.487  1.00 39.63  ? 2465 GLU A CA    1 
ATOM   4195 C  C     . GLU A 1 674 ? 87.672  101.189 95.386  1.00 36.43  ? 2465 GLU A C     1 
ATOM   4196 O  O     . GLU A 1 674 ? 87.962  100.195 96.066  1.00 38.78  ? 2465 GLU A O     1 
ATOM   4197 C  CB    . GLU A 1 674 ? 85.457  101.499 94.253  1.00 46.44  ? 2465 GLU A CB    1 
ATOM   4198 C  CG    . GLU A 1 674 ? 84.008  101.942 94.334  1.00 58.06  ? 2465 GLU A CG    1 
ATOM   4199 C  CD    . GLU A 1 674 ? 83.322  101.914 92.983  1.00 67.48  ? 2465 GLU A CD    1 
ATOM   4200 O  OE1   . GLU A 1 674 ? 83.863  101.277 92.055  1.00 60.59  ? 2465 GLU A OE1   1 
ATOM   4201 O  OE2   . GLU A 1 674 ? 82.240  102.523 92.849  1.00 74.27  ? 2465 GLU A OE2   1 
ATOM   4202 N  N     . ARG A 1 675 ? 88.539  101.755 94.542  1.00 35.96  ? 2466 ARG A N     1 
ATOM   4203 C  CA    . ARG A 1 675 ? 89.872  101.193 94.360  1.00 31.89  ? 2466 ARG A CA    1 
ATOM   4204 C  C     . ARG A 1 675 ? 90.682  101.258 95.647  1.00 29.59  ? 2466 ARG A C     1 
ATOM   4205 O  O     . ARG A 1 675 ? 91.409  100.315 95.975  1.00 30.87  ? 2466 ARG A O     1 
ATOM   4206 C  CB    . ARG A 1 675 ? 90.597  101.912 93.222  1.00 33.96  ? 2466 ARG A CB    1 
ATOM   4207 C  CG    . ARG A 1 675 ? 89.897  101.783 91.878  1.00 33.92  ? 2466 ARG A CG    1 
ATOM   4208 C  CD    . ARG A 1 675 ? 90.843  102.051 90.717  1.00 33.00  ? 2466 ARG A CD    1 
ATOM   4209 N  NE    . ARG A 1 675 ? 91.492  103.354 90.794  1.00 32.96  ? 2466 ARG A NE    1 
ATOM   4210 C  CZ    . ARG A 1 675 ? 90.868  104.514 90.647  1.00 40.64  ? 2466 ARG A CZ    1 
ATOM   4211 N  NH1   . ARG A 1 675 ? 89.572  104.576 90.393  1.00 47.58  ? 2466 ARG A NH1   1 
ATOM   4212 N  NH2   . ARG A 1 675 ? 91.565  105.642 90.742  1.00 44.17  ? 2466 ARG A NH2   1 
ATOM   4213 N  N     . GLN A 1 676 ? 90.558  102.351 96.402  1.00 29.74  ? 2467 GLN A N     1 
ATOM   4214 C  CA    . GLN A 1 676 ? 91.321  102.462 97.637  1.00 28.35  ? 2467 GLN A CA    1 
ATOM   4215 C  C     . GLN A 1 676 ? 90.747  101.575 98.733  1.00 29.91  ? 2467 GLN A C     1 
ATOM   4216 O  O     . GLN A 1 676 ? 91.489  101.141 99.611  1.00 31.01  ? 2467 GLN A O     1 
ATOM   4217 C  CB    . GLN A 1 676 ? 91.398  103.920 98.094  1.00 29.52  ? 2467 GLN A CB    1 
ATOM   4218 C  CG    . GLN A 1 676 ? 90.110  104.506 98.620  1.00 32.31  ? 2467 GLN A CG    1 
ATOM   4219 C  CD    . GLN A 1 676 ? 90.240  105.980 98.944  1.00 37.19  ? 2467 GLN A CD    1 
ATOM   4220 O  OE1   . GLN A 1 676 ? 89.329  106.767 98.691  1.00 40.82  ? 2467 GLN A OE1   1 
ATOM   4221 N  NE2   . GLN A 1 676 ? 91.380  106.364 99.503  1.00 35.47  ? 2467 GLN A NE2   1 
ATOM   4222 N  N     . ALA A 1 677 ? 89.452  101.257 98.689  1.00 30.37  ? 2468 ALA A N     1 
ATOM   4223 C  CA    . ALA A 1 677 ? 88.906  100.281 99.630  1.00 27.68  ? 2468 ALA A CA    1 
ATOM   4224 C  C     . ALA A 1 677 ? 89.422  98.878  99.328  1.00 28.34  ? 2468 ALA A C     1 
ATOM   4225 O  O     . ALA A 1 677 ? 89.833  98.136  100.239 1.00 30.06  ? 2468 ALA A O     1 
ATOM   4226 C  CB    . ALA A 1 677 ? 87.379  100.312 99.586  1.00 31.99  ? 2468 ALA A CB    1 
ATOM   4227 N  N     . ILE A 1 678 ? 89.387  98.492  98.048  1.00 31.69  ? 2469 ILE A N     1 
ATOM   4228 C  CA    . ILE A 1 678 ? 89.970  97.216  97.640  1.00 28.96  ? 2469 ILE A CA    1 
ATOM   4229 C  C     . ILE A 1 678 ? 91.428  97.140  98.065  1.00 27.64  ? 2469 ILE A C     1 
ATOM   4230 O  O     . ILE A 1 678 ? 91.881  96.134  98.623  1.00 23.73  ? 2469 ILE A O     1 
ATOM   4231 C  CB    . ILE A 1 678 ? 89.825  97.004  96.122  1.00 27.49  ? 2469 ILE A CB    1 
ATOM   4232 C  CG1   . ILE A 1 678 ? 88.371  96.715  95.738  1.00 33.39  ? 2469 ILE A CG1   1 
ATOM   4233 C  CG2   . ILE A 1 678 ? 90.779  95.928  95.649  1.00 26.44  ? 2469 ILE A CG2   1 
ATOM   4234 C  CD1   . ILE A 1 678 ? 87.869  97.504  94.551  1.00 34.71  ? 2469 ILE A CD1   1 
ATOM   4235 N  N     . ASN A 1 679 ? 92.186  98.207  97.815  1.00 29.15  ? 2470 ASN A N     1 
ATOM   4236 C  CA    . ASN A 1 679 ? 93.586  98.198  98.205  1.00 24.29  ? 2470 ASN A CA    1 
ATOM   4237 C  C     . ASN A 1 679 ? 93.751  98.228  99.714  1.00 23.61  ? 2470 ASN A C     1 
ATOM   4238 O  O     . ASN A 1 679 ? 94.742  97.713  100.224 1.00 24.69  ? 2470 ASN A O     1 
ATOM   4239 C  CB    . ASN A 1 679 ? 94.332  99.374  97.585  1.00 26.67  ? 2470 ASN A CB    1 
ATOM   4240 C  CG    . ASN A 1 679 ? 95.771  99.448  98.049  1.00 27.15  ? 2470 ASN A CG    1 
ATOM   4241 O  OD1   . ASN A 1 679 ? 96.654  98.821  97.468  1.00 29.40  ? 2470 ASN A OD1   1 
ATOM   4242 N  ND2   . ASN A 1 679 ? 96.013  100.209 99.108  1.00 28.11  ? 2470 ASN A ND2   1 
ATOM   4243 N  N     . THR A 1 680 ? 92.818  98.837  100.445 1.00 23.82  ? 2471 THR A N     1 
ATOM   4244 C  CA    . THR A 1 680 ? 92.959  98.907  101.892 1.00 23.40  ? 2471 THR A CA    1 
ATOM   4245 C  C     . THR A 1 680 ? 92.838  97.529  102.518 1.00 24.92  ? 2471 THR A C     1 
ATOM   4246 O  O     . THR A 1 680 ? 93.729  97.100  103.256 1.00 24.07  ? 2471 THR A O     1 
ATOM   4247 C  CB    . THR A 1 680 ? 91.923  99.861  102.484 1.00 23.06  ? 2471 THR A CB    1 
ATOM   4248 O  OG1   . THR A 1 680 ? 92.346  101.211 102.269 1.00 28.13  ? 2471 THR A OG1   1 
ATOM   4249 C  CG2   . THR A 1 680 ? 91.776  99.622  103.978 1.00 23.34  ? 2471 THR A CG2   1 
ATOM   4250 N  N     . ILE A 1 681 ? 91.776  96.791  102.182 1.00 24.89  ? 2472 ILE A N     1 
ATOM   4251 C  CA    . ILE A 1 681 ? 91.572  95.507  102.855 1.00 16.65  ? 2472 ILE A CA    1 
ATOM   4252 C  C     . ILE A 1 681 ? 92.697  94.517  102.575 1.00 17.67  ? 2472 ILE A C     1 
ATOM   4253 O  O     . ILE A 1 681 ? 92.857  93.543  103.315 1.00 18.56  ? 2472 ILE A O     1 
ATOM   4254 C  CB    . ILE A 1 681 ? 90.206  94.892  102.498 1.00 14.72  ? 2472 ILE A CB    1 
ATOM   4255 C  CG1   . ILE A 1 681 ? 89.124  95.957  102.530 1.00 24.27  ? 2472 ILE A CG1   1 
ATOM   4256 C  CG2   . ILE A 1 681 ? 89.838  93.778  103.461 1.00 18.81  ? 2472 ILE A CG2   1 
ATOM   4257 C  CD1   . ILE A 1 681 ? 87.978  95.636  101.657 1.00 27.45  ? 2472 ILE A CD1   1 
ATOM   4258 N  N     . VAL A 1 682 ? 93.497  94.747  101.541 1.00 21.55  ? 2473 VAL A N     1 
ATOM   4259 C  CA    . VAL A 1 682 ? 94.607  93.860  101.205 1.00 18.97  ? 2473 VAL A CA    1 
ATOM   4260 C  C     . VAL A 1 682 ? 95.940  94.413  101.697 1.00 18.96  ? 2473 VAL A C     1 
ATOM   4261 O  O     . VAL A 1 682 ? 96.722  93.702  102.323 1.00 20.64  ? 2473 VAL A O     1 
ATOM   4262 C  CB    . VAL A 1 682 ? 94.634  93.591  99.685  1.00 17.44  ? 2473 VAL A CB    1 
ATOM   4263 C  CG1   . VAL A 1 682 ? 95.611  92.484  99.370  1.00 20.49  ? 2473 VAL A CG1   1 
ATOM   4264 C  CG2   . VAL A 1 682 ? 93.245  93.232  99.189  1.00 19.15  ? 2473 VAL A CG2   1 
ATOM   4265 N  N     . GLN A 1 683 ? 96.211  95.693  101.437 1.00 19.46  ? 2474 GLN A N     1 
ATOM   4266 C  CA    . GLN A 1 683 ? 97.481  96.304  101.809 1.00 19.39  ? 2474 GLN A CA    1 
ATOM   4267 C  C     . GLN A 1 683 ? 97.577  96.542  103.310 1.00 18.33  ? 2474 GLN A C     1 
ATOM   4268 O  O     . GLN A 1 683 ? 98.622  96.284  103.916 1.00 18.95  ? 2474 GLN A O     1 
ATOM   4269 C  CB    . GLN A 1 683 ? 97.651  97.616  101.048 1.00 21.40  ? 2474 GLN A CB    1 
ATOM   4270 C  CG    . GLN A 1 683 ? 99.002  98.266  101.205 1.00 22.56  ? 2474 GLN A CG    1 
ATOM   4271 C  CD    . GLN A 1 683 ? 99.291  99.255  100.097 1.00 19.32  ? 2474 GLN A CD    1 
ATOM   4272 O  OE1   . GLN A 1 683 ? 99.605  100.414 100.353 1.00 20.98  ? 2474 GLN A OE1   1 
ATOM   4273 N  NE2   . GLN A 1 683 ? 99.188  98.799  98.856  1.00 18.43  ? 2474 GLN A NE2   1 
ATOM   4274 N  N     . GLY A 1 684 ? 96.516  97.068  103.928 1.00 19.51  ? 2475 GLY A N     1 
ATOM   4275 C  CA    . GLY A 1 684 ? 96.507  97.175  105.372 1.00 20.03  ? 2475 GLY A CA    1 
ATOM   4276 C  C     . GLY A 1 684 ? 96.562  95.823  106.045 1.00 20.57  ? 2475 GLY A C     1 
ATOM   4277 O  O     . GLY A 1 684 ? 97.178  95.678  107.099 1.00 23.20  ? 2475 GLY A O     1 
ATOM   4278 N  N     . SER A 1 685 ? 95.933  94.811  105.442 1.00 19.86  ? 2476 SER A N     1 
ATOM   4279 C  CA    . SER A 1 685 ? 96.054  93.454  105.963 1.00 18.14  ? 2476 SER A CA    1 
ATOM   4280 C  C     . SER A 1 685 ? 97.485  92.948  105.859 1.00 18.64  ? 2476 SER A C     1 
ATOM   4281 O  O     . SER A 1 685 ? 97.973  92.274  106.769 1.00 21.69  ? 2476 SER A O     1 
ATOM   4282 C  CB    . SER A 1 685 ? 95.103  92.519  105.225 1.00 18.00  ? 2476 SER A CB    1 
ATOM   4283 O  OG    . SER A 1 685 ? 95.313  91.178  105.622 1.00 23.69  ? 2476 SER A OG    1 
ATOM   4284 N  N     . ALA A 1 686 ? 98.168  93.251  104.755 1.00 18.41  ? 2477 ALA A N     1 
ATOM   4285 C  CA    . ALA A 1 686 ? 99.571  92.873  104.627 1.00 18.08  ? 2477 ALA A CA    1 
ATOM   4286 C  C     . ALA A 1 686 ? 100.425 93.570  105.673 1.00 20.30  ? 2477 ALA A C     1 
ATOM   4287 O  O     . ALA A 1 686 ? 101.287 92.945  106.298 1.00 22.60  ? 2477 ALA A O     1 
ATOM   4288 C  CB    . ALA A 1 686 ? 100.073 93.194  103.220 1.00 17.65  ? 2477 ALA A CB    1 
ATOM   4289 N  N     . ALA A 1 687 ? 100.186 94.863  105.889 1.00 20.35  ? 2478 ALA A N     1 
ATOM   4290 C  CA    . ALA A 1 687 ? 100.926 95.601  106.906 1.00 20.52  ? 2478 ALA A CA    1 
ATOM   4291 C  C     . ALA A 1 687 ? 100.622 95.084  108.305 1.00 22.26  ? 2478 ALA A C     1 
ATOM   4292 O  O     . ALA A 1 687 ? 101.508 95.054  109.164 1.00 25.63  ? 2478 ALA A O     1 
ATOM   4293 C  CB    . ALA A 1 687 ? 100.605 97.090  106.813 1.00 25.05  ? 2478 ALA A CB    1 
ATOM   4294 N  N     . ASP A 1 688 ? 99.386  94.652  108.546 1.00 23.93  ? 2479 ASP A N     1 
ATOM   4295 C  CA    . ASP A 1 688 ? 99.004  94.161  109.863 1.00 22.70  ? 2479 ASP A CA    1 
ATOM   4296 C  C     . ASP A 1 688 ? 99.599  92.776  110.104 1.00 21.58  ? 2479 ASP A C     1 
ATOM   4297 O  O     . ASP A 1 688 ? 100.057 92.475  111.211 1.00 24.63  ? 2479 ASP A O     1 
ATOM   4298 C  CB    . ASP A 1 688 ? 97.469  94.206  109.947 1.00 24.53  ? 2479 ASP A CB    1 
ATOM   4299 C  CG    . ASP A 1 688 ? 96.859  93.381  111.081 1.00 34.10  ? 2479 ASP A CG    1 
ATOM   4300 O  OD1   . ASP A 1 688 ? 97.491  92.513  111.708 1.00 37.58  ? 2479 ASP A OD1   1 
ATOM   4301 O  OD2   . ASP A 1 688 ? 95.677  93.647  111.359 1.00 39.13  ? 2479 ASP A OD2   1 
ATOM   4302 N  N     . ILE A 1 689 ? 99.631  91.933  109.070 1.00 20.10  ? 2480 ILE A N     1 
ATOM   4303 C  CA    . ILE A 1 689 ? 100.337 90.657  109.154 1.00 19.89  ? 2480 ILE A CA    1 
ATOM   4304 C  C     . ILE A 1 689 ? 101.820 90.893  109.404 1.00 22.23  ? 2480 ILE A C     1 
ATOM   4305 O  O     . ILE A 1 689 ? 102.458 90.174  110.181 1.00 24.12  ? 2480 ILE A O     1 
ATOM   4306 C  CB    . ILE A 1 689 ? 100.105 89.832  107.873 1.00 18.04  ? 2480 ILE A CB    1 
ATOM   4307 C  CG1   . ILE A 1 689 ? 98.649  89.373  107.783 1.00 19.55  ? 2480 ILE A CG1   1 
ATOM   4308 C  CG2   . ILE A 1 689 ? 101.043 88.638  107.820 1.00 17.49  ? 2480 ILE A CG2   1 
ATOM   4309 C  CD1   . ILE A 1 689 ? 98.430  88.220  106.831 1.00 22.06  ? 2480 ILE A CD1   1 
ATOM   4310 N  N     . VAL A 1 690 ? 102.392 91.902  108.747 1.00 22.75  ? 2481 VAL A N     1 
ATOM   4311 C  CA    . VAL A 1 690 ? 103.796 92.238  108.958 1.00 20.56  ? 2481 VAL A CA    1 
ATOM   4312 C  C     . VAL A 1 690 ? 104.024 92.693  110.394 1.00 22.61  ? 2481 VAL A C     1 
ATOM   4313 O  O     . VAL A 1 690 ? 105.028 92.339  111.018 1.00 27.89  ? 2481 VAL A O     1 
ATOM   4314 C  CB    . VAL A 1 690 ? 104.243 93.301  107.938 1.00 18.68  ? 2481 VAL A CB    1 
ATOM   4315 C  CG1   . VAL A 1 690 ? 105.497 94.003  108.407 1.00 18.50  ? 2481 VAL A CG1   1 
ATOM   4316 C  CG2   . VAL A 1 690 ? 104.474 92.661  106.584 1.00 19.32  ? 2481 VAL A CG2   1 
ATOM   4317 N  N     . LYS A 1 691 ? 103.100 93.485  110.940 1.00 21.64  ? 2482 LYS A N     1 
ATOM   4318 C  CA    . LYS A 1 691 ? 103.221 93.922  112.329 1.00 21.92  ? 2482 LYS A CA    1 
ATOM   4319 C  C     . LYS A 1 691 ? 103.113 92.747  113.295 1.00 24.78  ? 2482 LYS A C     1 
ATOM   4320 O  O     . LYS A 1 691 ? 103.848 92.686  114.286 1.00 26.07  ? 2482 LYS A O     1 
ATOM   4321 C  CB    . LYS A 1 691 ? 102.166 94.982  112.643 1.00 23.27  ? 2482 LYS A CB    1 
ATOM   4322 C  CG    . LYS A 1 691 ? 102.547 96.378  112.174 1.00 26.65  ? 2482 LYS A CG    1 
ATOM   4323 C  CD    . LYS A 1 691 ? 101.455 97.393  112.462 1.00 28.81  ? 2482 LYS A CD    1 
ATOM   4324 C  CE    . LYS A 1 691 ? 100.224 97.128  111.623 1.00 30.62  ? 2482 LYS A CE    1 
ATOM   4325 N  NZ    . LYS A 1 691 ? 99.208  98.201  111.777 1.00 26.29  ? 2482 LYS A NZ    1 
ATOM   4326 N  N     . ILE A 1 692 ? 102.204 91.806  113.026 1.00 24.48  ? 2483 ILE A N     1 
ATOM   4327 C  CA    . ILE A 1 692 ? 102.107 90.608  113.859 1.00 21.77  ? 2483 ILE A CA    1 
ATOM   4328 C  C     . ILE A 1 692 ? 103.398 89.805  113.787 1.00 24.88  ? 2483 ILE A C     1 
ATOM   4329 O  O     . ILE A 1 692 ? 103.894 89.303  114.803 1.00 28.49  ? 2483 ILE A O     1 
ATOM   4330 C  CB    . ILE A 1 692 ? 100.898 89.750  113.444 1.00 19.85  ? 2483 ILE A CB    1 
ATOM   4331 C  CG1   . ILE A 1 692 ? 99.589  90.477  113.728 1.00 20.31  ? 2483 ILE A CG1   1 
ATOM   4332 C  CG2   . ILE A 1 692 ? 100.917 88.419  114.171 1.00 23.94  ? 2483 ILE A CG2   1 
ATOM   4333 C  CD1   . ILE A 1 692 ? 98.419  89.886  112.994 1.00 22.15  ? 2483 ILE A CD1   1 
ATOM   4334 N  N     . ALA A 1 693 ? 103.953 89.659  112.583 1.00 23.23  ? 2484 ALA A N     1 
ATOM   4335 C  CA    . ALA A 1 693 ? 105.212 88.942  112.428 1.00 21.83  ? 2484 ALA A CA    1 
ATOM   4336 C  C     . ALA A 1 693 ? 106.333 89.640  113.181 1.00 22.14  ? 2484 ALA A C     1 
ATOM   4337 O  O     . ALA A 1 693 ? 107.167 88.984  113.810 1.00 26.15  ? 2484 ALA A O     1 
ATOM   4338 C  CB    . ALA A 1 693 ? 105.559 88.806  110.948 1.00 23.57  ? 2484 ALA A CB    1 
ATOM   4339 N  N     . THR A 1 694 ? 106.367 90.973  113.130 1.00 22.14  ? 2485 THR A N     1 
ATOM   4340 C  CA    . THR A 1 694 ? 107.376 91.724  113.870 1.00 22.62  ? 2485 THR A CA    1 
ATOM   4341 C  C     . THR A 1 694 ? 107.228 91.516  115.370 1.00 29.04  ? 2485 THR A C     1 
ATOM   4342 O  O     . THR A 1 694 ? 108.223 91.342  116.080 1.00 33.00  ? 2485 THR A O     1 
ATOM   4343 C  CB    . THR A 1 694 ? 107.282 93.212  113.543 1.00 22.00  ? 2485 THR A CB    1 
ATOM   4344 O  OG1   . THR A 1 694 ? 107.265 93.400  112.124 1.00 23.82  ? 2485 THR A OG1   1 
ATOM   4345 C  CG2   . THR A 1 694 ? 108.464 93.945  114.132 1.00 25.07  ? 2485 THR A CG2   1 
ATOM   4346 N  N     . VAL A 1 695 ? 105.991 91.540  115.869 1.00 27.46  ? 2486 VAL A N     1 
ATOM   4347 C  CA    . VAL A 1 695 ? 105.757 91.332  117.295 1.00 25.97  ? 2486 VAL A CA    1 
ATOM   4348 C  C     . VAL A 1 695 ? 106.210 89.937  117.707 1.00 31.13  ? 2486 VAL A C     1 
ATOM   4349 O  O     . VAL A 1 695 ? 106.874 89.756  118.735 1.00 37.13  ? 2486 VAL A O     1 
ATOM   4350 C  CB    . VAL A 1 695 ? 104.274 91.565  117.632 1.00 24.50  ? 2486 VAL A CB    1 
ATOM   4351 C  CG1   . VAL A 1 695 ? 103.988 91.166  119.064 1.00 30.35  ? 2486 VAL A CG1   1 
ATOM   4352 C  CG2   . VAL A 1 695 ? 103.904 93.014  117.395 1.00 24.40  ? 2486 VAL A CG2   1 
ATOM   4353 N  N     . ASN A 1 696 ? 105.860 88.930  116.905 1.00 27.69  ? 2487 ASN A N     1 
ATOM   4354 C  CA    . ASN A 1 696 ? 106.239 87.558  117.226 1.00 28.25  ? 2487 ASN A CA    1 
ATOM   4355 C  C     . ASN A 1 696 ? 107.751 87.377  117.190 1.00 33.15  ? 2487 ASN A C     1 
ATOM   4356 O  O     . ASN A 1 696 ? 108.326 86.709  118.058 1.00 39.95  ? 2487 ASN A O     1 
ATOM   4357 C  CB    . ASN A 1 696 ? 105.555 86.591  116.261 1.00 28.92  ? 2487 ASN A CB    1 
ATOM   4358 C  CG    . ASN A 1 696 ? 104.049 86.563  116.432 1.00 28.62  ? 2487 ASN A CG    1 
ATOM   4359 O  OD1   . ASN A 1 696 ? 103.481 87.366  117.170 1.00 25.78  ? 2487 ASN A OD1   1 
ATOM   4360 N  ND2   . ASN A 1 696 ? 103.394 85.637  115.742 1.00 32.15  ? 2487 ASN A ND2   1 
ATOM   4361 N  N     . ILE A 1 697 ? 108.415 87.967  116.194 1.00 30.38  ? 2488 ILE A N     1 
ATOM   4362 C  CA    . ILE A 1 697 ? 109.866 87.863  116.098 1.00 28.95  ? 2488 ILE A CA    1 
ATOM   4363 C  C     . ILE A 1 697 ? 110.532 88.568  117.270 1.00 33.47  ? 2488 ILE A C     1 
ATOM   4364 O  O     . ILE A 1 697 ? 111.523 88.078  117.821 1.00 42.57  ? 2488 ILE A O     1 
ATOM   4365 C  CB    . ILE A 1 697 ? 110.355 88.423  114.751 1.00 24.94  ? 2488 ILE A CB    1 
ATOM   4366 C  CG1   . ILE A 1 697 ? 109.890 87.530  113.604 1.00 27.49  ? 2488 ILE A CG1   1 
ATOM   4367 C  CG2   . ILE A 1 697 ? 111.868 88.539  114.745 1.00 25.04  ? 2488 ILE A CG2   1 
ATOM   4368 C  CD1   . ILE A 1 697 ? 110.001 88.181  112.254 1.00 26.19  ? 2488 ILE A CD1   1 
ATOM   4369 N  N     . GLN A 1 698 ? 110.012 89.733  117.661 1.00 32.42  ? 2489 GLN A N     1 
ATOM   4370 C  CA    . GLN A 1 698 ? 110.566 90.433  118.813 1.00 36.98  ? 2489 GLN A CA    1 
ATOM   4371 C  C     . GLN A 1 698 ? 110.401 89.610  120.082 1.00 40.10  ? 2489 GLN A C     1 
ATOM   4372 O  O     . GLN A 1 698 ? 111.329 89.513  120.891 1.00 45.24  ? 2489 GLN A O     1 
ATOM   4373 C  CB    . GLN A 1 698 ? 109.906 91.801  118.969 1.00 33.91  ? 2489 GLN A CB    1 
ATOM   4374 C  CG    . GLN A 1 698 ? 110.724 92.774  119.792 1.00 33.01  ? 2489 GLN A CG    1 
ATOM   4375 C  CD    . GLN A 1 698 ? 112.109 92.989  119.222 1.00 38.83  ? 2489 GLN A CD    1 
ATOM   4376 O  OE1   . GLN A 1 698 ? 113.110 92.848  119.923 1.00 42.84  ? 2489 GLN A OE1   1 
ATOM   4377 N  NE2   . GLN A 1 698 ? 112.175 93.336  117.943 1.00 35.25  ? 2489 GLN A NE2   1 
ATOM   4378 N  N     . LYS A 1 699 ? 109.233 88.992  120.263 1.00 39.55  ? 2490 LYS A N     1 
ATOM   4379 C  CA    . LYS A 1 699 ? 109.033 88.119  121.414 1.00 40.35  ? 2490 LYS A CA    1 
ATOM   4380 C  C     . LYS A 1 699 ? 110.040 86.976  121.411 1.00 43.97  ? 2490 LYS A C     1 
ATOM   4381 O  O     . LYS A 1 699 ? 110.694 86.705  122.426 1.00 48.99  ? 2490 LYS A O     1 
ATOM   4382 C  CB    . LYS A 1 699 ? 107.605 87.575  121.415 1.00 36.26  ? 2490 LYS A CB    1 
ATOM   4383 C  CG    . LYS A 1 699 ? 106.544 88.602  121.758 1.00 38.43  ? 2490 LYS A CG    1 
ATOM   4384 C  CD    . LYS A 1 699 ? 105.149 88.036  121.558 1.00 38.48  ? 2490 LYS A CD    1 
ATOM   4385 C  CE    . LYS A 1 699 ? 104.082 89.038  121.963 1.00 42.92  ? 2490 LYS A CE    1 
ATOM   4386 N  NZ    . LYS A 1 699 ? 102.717 88.579  121.586 1.00 43.36  ? 2490 LYS A NZ    1 
ATOM   4387 N  N     . GLN A 1 700 ? 110.199 86.312  120.264 1.00 42.40  ? 2491 GLN A N     1 
ATOM   4388 C  CA    . GLN A 1 700 ? 111.063 85.138  120.206 1.00 45.96  ? 2491 GLN A CA    1 
ATOM   4389 C  C     . GLN A 1 700 ? 112.533 85.498  120.378 1.00 49.08  ? 2491 GLN A C     1 
ATOM   4390 O  O     . GLN A 1 700 ? 113.289 84.724  120.977 1.00 55.71  ? 2491 GLN A O     1 
ATOM   4391 C  CB    . GLN A 1 700 ? 110.845 84.389  118.894 1.00 44.08  ? 2491 GLN A CB    1 
ATOM   4392 C  CG    . GLN A 1 700 ? 109.587 83.540  118.886 1.00 39.84  ? 2491 GLN A CG    1 
ATOM   4393 C  CD    . GLN A 1 700 ? 109.846 82.121  118.427 1.00 43.98  ? 2491 GLN A CD    1 
ATOM   4394 O  OE1   . GLN A 1 700 ? 110.760 81.866  117.644 1.00 50.75  ? 2491 GLN A OE1   1 
ATOM   4395 N  NE2   . GLN A 1 700 ? 109.041 81.185  118.916 1.00 43.67  ? 2491 GLN A NE2   1 
ATOM   4396 N  N     . LEU A 1 701 ? 112.962 86.651  119.867 1.00 42.16  ? 2492 LEU A N     1 
ATOM   4397 C  CA    . LEU A 1 701 ? 114.336 87.087  120.073 1.00 44.13  ? 2492 LEU A CA    1 
ATOM   4398 C  C     . LEU A 1 701 ? 114.534 87.766  121.421 1.00 50.83  ? 2492 LEU A C     1 
ATOM   4399 O  O     . LEU A 1 701 ? 115.676 88.064  121.785 1.00 58.03  ? 2492 LEU A O     1 
ATOM   4400 C  CB    . LEU A 1 701 ? 114.775 88.004  118.920 1.00 44.48  ? 2492 LEU A CB    1 
ATOM   4401 C  CG    . LEU A 1 701 ? 114.482 89.509  118.844 1.00 48.63  ? 2492 LEU A CG    1 
ATOM   4402 C  CD1   . LEU A 1 701 ? 115.454 90.363  119.657 1.00 46.67  ? 2492 LEU A CD1   1 
ATOM   4403 C  CD2   . LEU A 1 701 ? 114.473 89.956  117.390 1.00 41.31  ? 2492 LEU A CD2   1 
ATOM   4404 N  N     . GLU A 1 702 ? 113.454 88.025  122.161 1.00 51.53  ? 2493 GLU A N     1 
ATOM   4405 C  CA    . GLU A 1 702 ? 113.595 88.449  123.548 1.00 51.10  ? 2493 GLU A CA    1 
ATOM   4406 C  C     . GLU A 1 702 ? 113.744 87.253  124.480 1.00 52.53  ? 2493 GLU A C     1 
ATOM   4407 O  O     . GLU A 1 702 ? 114.609 87.260  125.364 1.00 55.83  ? 2493 GLU A O     1 
ATOM   4408 C  CB    . GLU A 1 702 ? 112.398 89.303  123.963 1.00 48.61  ? 2493 GLU A CB    1 
ATOM   4409 C  CG    . GLU A 1 702 ? 112.518 90.768  123.579 1.00 44.08  ? 2493 GLU A CG    1 
ATOM   4410 C  CD    . GLU A 1 702 ? 111.238 91.540  123.831 1.00 45.69  ? 2493 GLU A CD    1 
ATOM   4411 O  OE1   . GLU A 1 702 ? 110.276 90.945  124.359 1.00 46.12  ? 2493 GLU A OE1   1 
ATOM   4412 O  OE2   . GLU A 1 702 ? 111.194 92.742  123.498 1.00 46.03  ? 2493 GLU A OE2   1 
ATOM   4413 N  N     . THR A 1 703 ? 112.912 86.220  124.306 1.00 51.44  ? 2494 THR A N     1 
ATOM   4414 C  CA    . THR A 1 703 ? 113.087 85.009  125.105 1.00 58.02  ? 2494 THR A CA    1 
ATOM   4415 C  C     . THR A 1 703 ? 114.422 84.338  124.806 1.00 59.66  ? 2494 THR A C     1 
ATOM   4416 O  O     . THR A 1 703 ? 115.118 83.887  125.723 1.00 62.76  ? 2494 THR A O     1 
ATOM   4417 C  CB    . THR A 1 703 ? 111.929 84.032  124.878 1.00 57.78  ? 2494 THR A CB    1 
ATOM   4418 O  OG1   . THR A 1 703 ? 112.173 83.245  123.704 1.00 55.18  ? 2494 THR A OG1   1 
ATOM   4419 C  CG2   . THR A 1 703 ? 110.602 84.764  124.758 1.00 55.35  ? 2494 THR A CG2   1 
ATOM   4420 N  N     . PHE A 1 704 ? 114.798 84.267  123.535 1.00 58.06  ? 2495 PHE A N     1 
ATOM   4421 C  CA    . PHE A 1 704 ? 116.097 83.746  123.143 1.00 61.39  ? 2495 PHE A CA    1 
ATOM   4422 C  C     . PHE A 1 704 ? 117.113 84.883  123.075 1.00 62.19  ? 2495 PHE A C     1 
ATOM   4423 O  O     . PHE A 1 704 ? 116.775 86.057  123.229 1.00 63.16  ? 2495 PHE A O     1 
ATOM   4424 C  CB    . PHE A 1 704 ? 116.000 83.027  121.797 1.00 62.57  ? 2495 PHE A CB    1 
ATOM   4425 C  CG    . PHE A 1 704 ? 115.864 81.537  121.912 1.00 67.68  ? 2495 PHE A CG    1 
ATOM   4426 C  CD1   . PHE A 1 704 ? 116.663 80.819  122.786 1.00 71.70  ? 2495 PHE A CD1   1 
ATOM   4427 C  CD2   . PHE A 1 704 ? 114.935 80.853  121.145 1.00 70.67  ? 2495 PHE A CD2   1 
ATOM   4428 C  CE1   . PHE A 1 704 ? 116.539 79.446  122.893 1.00 72.58  ? 2495 PHE A CE1   1 
ATOM   4429 C  CE2   . PHE A 1 704 ? 114.806 79.481  121.247 1.00 73.80  ? 2495 PHE A CE2   1 
ATOM   4430 C  CZ    . PHE A 1 704 ? 115.609 78.777  122.122 1.00 72.95  ? 2495 PHE A CZ    1 
ATOM   4431 N  N     . HIS A 1 705 ? 118.373 84.517  122.845 1.00 64.78  ? 2496 HIS A N     1 
ATOM   4432 C  CA    . HIS A 1 705 ? 119.472 85.470  122.682 1.00 68.94  ? 2496 HIS A CA    1 
ATOM   4433 C  C     . HIS A 1 705 ? 119.474 86.507  123.809 1.00 71.02  ? 2496 HIS A C     1 
ATOM   4434 O  O     . HIS A 1 705 ? 119.237 87.697  123.604 1.00 67.28  ? 2496 HIS A O     1 
ATOM   4435 C  CB    . HIS A 1 705 ? 119.410 86.158  121.314 1.00 63.22  ? 2496 HIS A CB    1 
ATOM   4436 C  CG    . HIS A 1 705 ? 118.769 85.332  120.243 1.00 64.80  ? 2496 HIS A CG    1 
ATOM   4437 N  ND1   . HIS A 1 705 ? 117.420 85.386  119.968 1.00 62.56  ? 2496 HIS A ND1   1 
ATOM   4438 C  CD2   . HIS A 1 705 ? 119.293 84.433  119.377 1.00 65.77  ? 2496 HIS A CD2   1 
ATOM   4439 C  CE1   . HIS A 1 705 ? 117.140 84.558  118.978 1.00 61.70  ? 2496 HIS A CE1   1 
ATOM   4440 N  NE2   . HIS A 1 705 ? 118.258 83.964  118.604 1.00 62.24  ? 2496 HIS A NE2   1 
ATOM   4441 N  N     . SER A 1 706 ? 119.735 86.011  125.019 1.00 72.09  ? 2497 SER A N     1 
ATOM   4442 C  CA    . SER A 1 706 ? 119.681 86.853  126.209 1.00 75.54  ? 2497 SER A CA    1 
ATOM   4443 C  C     . SER A 1 706 ? 120.714 87.970  126.135 1.00 75.37  ? 2497 SER A C     1 
ATOM   4444 O  O     . SER A 1 706 ? 121.915 87.731  126.299 1.00 77.78  ? 2497 SER A O     1 
ATOM   4445 C  CB    . SER A 1 706 ? 119.895 86.009  127.467 1.00 77.37  ? 2497 SER A CB    1 
ATOM   4446 O  OG    . SER A 1 706 ? 121.062 85.214  127.355 1.00 75.98  ? 2497 SER A OG    1 
ATOM   4447 N  N     . THR A 1 707 ? 120.248 89.190  125.899 1.00 70.25  ? 2498 THR A N     1 
ATOM   4448 C  CA    . THR A 1 707 ? 121.097 90.361  125.694 1.00 67.18  ? 2498 THR A CA    1 
ATOM   4449 C  C     . THR A 1 707 ? 120.194 91.591  125.735 1.00 67.78  ? 2498 THR A C     1 
ATOM   4450 O  O     . THR A 1 707 ? 119.000 91.493  126.045 1.00 65.89  ? 2498 THR A O     1 
ATOM   4451 C  CB    . THR A 1 707 ? 121.867 90.261  124.375 1.00 66.23  ? 2498 THR A CB    1 
ATOM   4452 O  OG1   . THR A 1 707 ? 122.890 91.264  124.331 1.00 66.80  ? 2498 THR A OG1   1 
ATOM   4453 C  CG2   . THR A 1 707 ? 120.922 90.454  123.200 1.00 61.43  ? 2498 THR A CG2   1 
ATOM   4454 N  N     . PHE A 1 708 ? 120.763 92.755  125.428 1.00 66.25  ? 2499 PHE A N     1 
ATOM   4455 C  CA    . PHE A 1 708 ? 119.967 93.967  125.298 1.00 56.98  ? 2499 PHE A CA    1 
ATOM   4456 C  C     . PHE A 1 708 ? 119.026 93.856  124.105 1.00 49.44  ? 2499 PHE A C     1 
ATOM   4457 O  O     . PHE A 1 708 ? 119.404 93.366  123.037 1.00 53.14  ? 2499 PHE A O     1 
ATOM   4458 C  CB    . PHE A 1 708 ? 120.875 95.185  125.138 1.00 53.41  ? 2499 PHE A CB    1 
ATOM   4459 C  CG    . PHE A 1 708 ? 122.090 95.155  126.016 1.00 59.76  ? 2499 PHE A CG    1 
ATOM   4460 C  CD1   . PHE A 1 708 ? 121.967 95.192  127.394 1.00 65.91  ? 2499 PHE A CD1   1 
ATOM   4461 C  CD2   . PHE A 1 708 ? 123.358 95.092  125.464 1.00 59.85  ? 2499 PHE A CD2   1 
ATOM   4462 C  CE1   . PHE A 1 708 ? 123.085 95.167  128.205 1.00 70.31  ? 2499 PHE A CE1   1 
ATOM   4463 C  CE2   . PHE A 1 708 ? 124.480 95.066  126.269 1.00 62.84  ? 2499 PHE A CE2   1 
ATOM   4464 C  CZ    . PHE A 1 708 ? 124.343 95.103  127.641 1.00 70.12  ? 2499 PHE A CZ    1 
ATOM   4465 N  N     . LYS A 1 709 ? 117.791 94.321  124.290 1.00 42.76  ? 2500 LYS A N     1 
ATOM   4466 C  CA    . LYS A 1 709 ? 116.777 94.220  123.247 1.00 37.82  ? 2500 LYS A CA    1 
ATOM   4467 C  C     . LYS A 1 709 ? 117.031 95.158  122.076 1.00 36.49  ? 2500 LYS A C     1 
ATOM   4468 O  O     . LYS A 1 709 ? 116.363 95.025  121.046 1.00 40.12  ? 2500 LYS A O     1 
ATOM   4469 C  CB    . LYS A 1 709 ? 115.395 94.506  123.834 1.00 36.24  ? 2500 LYS A CB    1 
ATOM   4470 C  CG    . LYS A 1 709 ? 115.210 94.005  125.254 1.00 42.39  ? 2500 LYS A CG    1 
ATOM   4471 C  CD    . LYS A 1 709 ? 113.804 94.280  125.754 1.00 41.04  ? 2500 LYS A CD    1 
ATOM   4472 C  CE    . LYS A 1 709 ? 113.711 94.117  127.261 1.00 44.93  ? 2500 LYS A CE    1 
ATOM   4473 N  NZ    . LYS A 1 709 ? 114.512 95.146  127.979 1.00 48.71  ? 2500 LYS A NZ    1 
ATOM   4474 N  N     . SER A 1 710 ? 117.965 96.096  122.206 1.00 35.94  ? 2501 SER A N     1 
ATOM   4475 C  CA    . SER A 1 710 ? 118.195 97.097  121.175 1.00 33.34  ? 2501 SER A CA    1 
ATOM   4476 C  C     . SER A 1 710 ? 119.579 97.699  121.369 1.00 39.82  ? 2501 SER A C     1 
ATOM   4477 O  O     . SER A 1 710 ? 120.184 97.574  122.436 1.00 47.84  ? 2501 SER A O     1 
ATOM   4478 C  CB    . SER A 1 710 ? 117.112 98.182  121.213 1.00 31.09  ? 2501 SER A CB    1 
ATOM   4479 O  OG    . SER A 1 710 ? 117.512 99.355  120.530 1.00 33.43  ? 2501 SER A OG    1 
ATOM   4480 N  N     . HIS A 1 711 ? 120.077 98.347  120.314 1.00 38.53  ? 2502 HIS A N     1 
ATOM   4481 C  CA    . HIS A 1 711 ? 121.326 99.094  120.431 1.00 39.49  ? 2502 HIS A CA    1 
ATOM   4482 C  C     . HIS A 1 711 ? 121.180 100.245 121.416 1.00 44.26  ? 2502 HIS A C     1 
ATOM   4483 O  O     . HIS A 1 711 ? 122.126 100.579 122.139 1.00 51.55  ? 2502 HIS A O     1 
ATOM   4484 C  CB    . HIS A 1 711 ? 121.763 99.613  119.062 1.00 36.74  ? 2502 HIS A CB    1 
ATOM   4485 C  CG    . HIS A 1 711 ? 122.087 98.531  118.081 1.00 38.63  ? 2502 HIS A CG    1 
ATOM   4486 N  ND1   . HIS A 1 711 ? 121.427 98.394  116.879 1.00 36.52  ? 2502 HIS A ND1   1 
ATOM   4487 C  CD2   . HIS A 1 711 ? 123.002 97.534  118.123 1.00 44.31  ? 2502 HIS A CD2   1 
ATOM   4488 C  CE1   . HIS A 1 711 ? 121.921 97.360  116.223 1.00 41.30  ? 2502 HIS A CE1   1 
ATOM   4489 N  NE2   . HIS A 1 711 ? 122.878 96.821  116.956 1.00 45.57  ? 2502 HIS A NE2   1 
ATOM   4490 N  N     . GLY A 1 712 ? 120.003 100.869 121.453 1.00 39.60  ? 2503 GLY A N     1 
ATOM   4491 C  CA    . GLY A 1 712 ? 119.755 101.891 122.454 1.00 40.56  ? 2503 GLY A CA    1 
ATOM   4492 C  C     . GLY A 1 712 ? 119.766 101.334 123.863 1.00 42.93  ? 2503 GLY A C     1 
ATOM   4493 O  O     . GLY A 1 712 ? 120.200 102.005 124.803 1.00 47.38  ? 2503 GLY A O     1 
ATOM   4494 N  N     . HIS A 1 713 ? 119.281 100.102 124.032 1.00 38.03  ? 2504 HIS A N     1 
ATOM   4495 C  CA    . HIS A 1 713 ? 119.389 99.441  125.328 1.00 40.24  ? 2504 HIS A CA    1 
ATOM   4496 C  C     . HIS A 1 713 ? 120.847 99.233  125.711 1.00 47.88  ? 2504 HIS A C     1 
ATOM   4497 O  O     . HIS A 1 713 ? 121.217 99.378  126.881 1.00 57.23  ? 2504 HIS A O     1 
ATOM   4498 C  CB    . HIS A 1 713 ? 118.646 98.106  125.309 1.00 39.12  ? 2504 HIS A CB    1 
ATOM   4499 C  CG    . HIS A 1 713 ? 117.156 98.238  125.366 1.00 34.52  ? 2504 HIS A CG    1 
ATOM   4500 N  ND1   . HIS A 1 713 ? 116.408 98.710  124.310 1.00 34.45  ? 2504 HIS A ND1   1 
ATOM   4501 C  CD2   . HIS A 1 713 ? 116.274 97.955  126.353 1.00 34.04  ? 2504 HIS A CD2   1 
ATOM   4502 C  CE1   . HIS A 1 713 ? 115.130 98.712  124.643 1.00 34.78  ? 2504 HIS A CE1   1 
ATOM   4503 N  NE2   . HIS A 1 713 ? 115.022 98.260  125.879 1.00 33.59  ? 2504 HIS A NE2   1 
ATOM   4504 N  N     . ARG A 1 714 ? 121.690 98.881  124.737 1.00 45.74  ? 2505 ARG A N     1 
ATOM   4505 C  CA    . ARG A 1 714 ? 123.120 98.762  125.003 1.00 51.60  ? 2505 ARG A CA    1 
ATOM   4506 C  C     . ARG A 1 714 ? 123.718 100.105 125.401 1.00 51.93  ? 2505 ARG A C     1 
ATOM   4507 O  O     . ARG A 1 714 ? 124.554 100.178 126.309 1.00 55.96  ? 2505 ARG A O     1 
ATOM   4508 C  CB    . ARG A 1 714 ? 123.833 98.198  123.775 1.00 53.95  ? 2505 ARG A CB    1 
ATOM   4509 C  CG    . ARG A 1 714 ? 125.348 98.167  123.888 1.00 56.56  ? 2505 ARG A CG    1 
ATOM   4510 C  CD    . ARG A 1 714 ? 125.968 97.373  122.749 1.00 56.23  ? 2505 ARG A CD    1 
ATOM   4511 N  NE    . ARG A 1 714 ? 125.603 95.963  122.804 1.00 56.13  ? 2505 ARG A NE    1 
ATOM   4512 C  CZ    . ARG A 1 714 ? 124.681 95.397  122.038 1.00 58.38  ? 2505 ARG A CZ    1 
ATOM   4513 N  NH1   . ARG A 1 714 ? 124.008 96.094  121.139 1.00 52.31  ? 2505 ARG A NH1   1 
ATOM   4514 N  NH2   . ARG A 1 714 ? 124.427 94.099  122.180 1.00 64.28  ? 2505 ARG A NH2   1 
ATOM   4515 N  N     . GLU A 1 715 ? 123.303 101.180 124.727 1.00 51.67  ? 2506 GLU A N     1 
ATOM   4516 C  CA    . GLU A 1 715 ? 123.810 102.508 125.059 1.00 55.92  ? 2506 GLU A CA    1 
ATOM   4517 C  C     . GLU A 1 715 ? 123.397 102.922 126.466 1.00 57.74  ? 2506 GLU A C     1 
ATOM   4518 O  O     . GLU A 1 715 ? 124.197 103.500 127.212 1.00 59.25  ? 2506 GLU A O     1 
ATOM   4519 C  CB    . GLU A 1 715 ? 123.319 103.526 124.028 1.00 54.79  ? 2506 GLU A CB    1 
ATOM   4520 C  CG    . GLU A 1 715 ? 122.999 104.901 124.596 1.00 59.08  ? 2506 GLU A CG    1 
ATOM   4521 C  CD    . GLU A 1 715 ? 123.005 105.986 123.536 1.00 64.31  ? 2506 GLU A CD    1 
ATOM   4522 O  OE1   . GLU A 1 715 ? 123.013 105.647 122.335 1.00 65.73  ? 2506 GLU A OE1   1 
ATOM   4523 O  OE2   . GLU A 1 715 ? 123.000 107.180 123.906 1.00 60.34  ? 2506 GLU A OE2   1 
ATOM   4524 N  N     . GLY A 1 716 ? 122.154 102.629 126.851 1.00 56.08  ? 2507 GLY A N     1 
ATOM   4525 C  CA    . GLY A 1 716 ? 121.689 103.025 128.170 1.00 57.51  ? 2507 GLY A CA    1 
ATOM   4526 C  C     . GLY A 1 716 ? 122.278 102.170 129.277 1.00 58.21  ? 2507 GLY A C     1 
ATOM   4527 O  O     . GLY A 1 716 ? 122.891 102.684 130.216 1.00 60.89  ? 2507 GLY A O     1 
ATOM   4528 N  N     . MET A 1 717 ? 122.100 100.857 129.181 1.00 56.27  ? 2508 MET A N     1 
ATOM   4529 C  CA    . MET A 1 717 ? 122.628 99.937  130.181 1.00 62.30  ? 2508 MET A CA    1 
ATOM   4530 C  C     . MET A 1 717 ? 123.602 98.949  129.548 1.00 60.23  ? 2508 MET A C     1 
ATOM   4531 O  O     . MET A 1 717 ? 124.621 98.600  130.143 1.00 65.27  ? 2508 MET A O     1 
ATOM   4532 C  CB    . MET A 1 717 ? 121.494 99.180  130.879 1.00 69.50  ? 2508 MET A CB    1 
ATOM   4533 C  CG    . MET A 1 717 ? 120.426 98.627  129.945 1.00 62.97  ? 2508 MET A CG    1 
ATOM   4534 S  SD    . MET A 1 717 ? 119.122 99.811  129.559 1.00 66.95  ? 2508 MET A SD    1 
ATOM   4535 C  CE    . MET A 1 717 ? 118.093 99.663  131.016 1.00 56.97  ? 2508 MET A CE    1 
ATOM   4536 N  N     . PHE A 1 735 ? 129.833 95.017  126.620 1.00 100.70 ? 2526 PHE A N     1 
ATOM   4537 C  CA    . PHE A 1 735 ? 130.654 93.822  126.776 1.00 103.21 ? 2526 PHE A CA    1 
ATOM   4538 C  C     . PHE A 1 735 ? 130.089 92.667  125.956 1.00 104.58 ? 2526 PHE A C     1 
ATOM   4539 O  O     . PHE A 1 735 ? 128.900 92.653  125.634 1.00 106.99 ? 2526 PHE A O     1 
ATOM   4540 C  CB    . PHE A 1 735 ? 130.755 93.425  128.252 1.00 100.11 ? 2526 PHE A CB    1 
ATOM   4541 C  CG    . PHE A 1 735 ? 129.450 92.981  128.854 1.00 101.16 ? 2526 PHE A CG    1 
ATOM   4542 C  CD1   . PHE A 1 735 ? 128.538 93.909  129.330 1.00 98.72  ? 2526 PHE A CD1   1 
ATOM   4543 C  CD2   . PHE A 1 735 ? 129.140 91.634  128.953 1.00 104.03 ? 2526 PHE A CD2   1 
ATOM   4544 C  CE1   . PHE A 1 735 ? 127.339 93.502  129.885 1.00 96.01  ? 2526 PHE A CE1   1 
ATOM   4545 C  CE2   . PHE A 1 735 ? 127.943 91.221  129.507 1.00 103.18 ? 2526 PHE A CE2   1 
ATOM   4546 C  CZ    . PHE A 1 735 ? 127.042 92.156  129.973 1.00 97.90  ? 2526 PHE A CZ    1 
ATOM   4547 N  N     . CYS A 1 736 ? 130.962 91.711  125.614 1.00 102.49 ? 2527 CYS A N     1 
ATOM   4548 C  CA    . CYS A 1 736 ? 130.637 90.492  124.876 1.00 98.45  ? 2527 CYS A CA    1 
ATOM   4549 C  C     . CYS A 1 736 ? 130.229 90.803  123.438 1.00 96.96  ? 2527 CYS A C     1 
ATOM   4550 O  O     . CYS A 1 736 ? 129.809 91.928  123.137 1.00 94.18  ? 2527 CYS A O     1 
ATOM   4551 C  CB    . CYS A 1 736 ? 129.532 89.707  125.591 1.00 98.20  ? 2527 CYS A CB    1 
ATOM   4552 S  SG    . CYS A 1 736 ? 130.087 88.817  127.064 1.00 110.21 ? 2527 CYS A SG    1 
ATOM   4553 N  N     . PRO A 1 737 ? 130.354 89.845  122.521 1.00 96.98  ? 2528 PRO A N     1 
ATOM   4554 C  CA    . PRO A 1 737 ? 129.937 90.096  121.138 1.00 92.54  ? 2528 PRO A CA    1 
ATOM   4555 C  C     . PRO A 1 737 ? 128.434 90.292  121.025 1.00 86.55  ? 2528 PRO A C     1 
ATOM   4556 O  O     . PRO A 1 737 ? 127.649 89.780  121.827 1.00 84.47  ? 2528 PRO A O     1 
ATOM   4557 C  CB    . PRO A 1 737 ? 130.391 88.835  120.393 1.00 89.88  ? 2528 PRO A CB    1 
ATOM   4558 C  CG    . PRO A 1 737 ? 130.543 87.795  121.453 1.00 91.41  ? 2528 PRO A CG    1 
ATOM   4559 C  CD    . PRO A 1 737 ? 131.004 88.532  122.669 1.00 94.72  ? 2528 PRO A CD    1 
ATOM   4560 N  N     . ILE A 1 738 ? 128.042 91.058  120.007 1.00 80.35  ? 2529 ILE A N     1 
ATOM   4561 C  CA    . ILE A 1 738 ? 126.633 91.333  119.760 1.00 69.13  ? 2529 ILE A CA    1 
ATOM   4562 C  C     . ILE A 1 738 ? 125.939 90.067  119.277 1.00 68.06  ? 2529 ILE A C     1 
ATOM   4563 O  O     . ILE A 1 738 ? 126.474 89.324  118.443 1.00 69.40  ? 2529 ILE A O     1 
ATOM   4564 C  CB    . ILE A 1 738 ? 126.493 92.469  118.735 1.00 61.82  ? 2529 ILE A CB    1 
ATOM   4565 C  CG1   . ILE A 1 738 ? 127.569 93.529  118.973 1.00 63.78  ? 2529 ILE A CG1   1 
ATOM   4566 C  CG2   . ILE A 1 738 ? 125.121 93.090  118.823 1.00 51.95  ? 2529 ILE A CG2   1 
ATOM   4567 C  CD1   . ILE A 1 738 ? 127.409 94.762  118.118 1.00 53.94  ? 2529 ILE A CD1   1 
ATOM   4568 N  N     . ARG A 1 739 ? 124.738 89.811  119.803 1.00 64.57  ? 2530 ARG A N     1 
ATOM   4569 C  CA    . ARG A 1 739 ? 123.983 88.604  119.461 1.00 66.04  ? 2530 ARG A CA    1 
ATOM   4570 C  C     . ARG A 1 739 ? 122.497 88.921  119.609 1.00 56.08  ? 2530 ARG A C     1 
ATOM   4571 O  O     . ARG A 1 739 ? 121.977 88.926  120.727 1.00 62.80  ? 2530 ARG A O     1 
ATOM   4572 C  CB    . ARG A 1 739 ? 124.387 87.433  120.351 1.00 68.21  ? 2530 ARG A CB    1 
ATOM   4573 C  CG    . ARG A 1 739 ? 125.674 86.731  119.947 1.00 71.01  ? 2530 ARG A CG    1 
ATOM   4574 C  CD    . ARG A 1 739 ? 126.122 85.740  121.008 1.00 71.83  ? 2530 ARG A CD    1 
ATOM   4575 N  NE    . ARG A 1 739 ? 125.870 84.360  120.613 1.00 74.79  ? 2530 ARG A NE    1 
ATOM   4576 C  CZ    . ARG A 1 739 ? 124.792 83.668  120.956 1.00 78.18  ? 2530 ARG A CZ    1 
ATOM   4577 N  NH1   . ARG A 1 739 ? 123.837 84.200  121.699 1.00 78.38  ? 2530 ARG A NH1   1 
ATOM   4578 N  NH2   . ARG A 1 739 ? 124.671 82.409  120.543 1.00 75.09  ? 2530 ARG A NH2   1 
ATOM   4579 N  N     . GLY A 1 740 ? 121.821 89.162  118.492 1.00 46.11  ? 2531 GLY A N     1 
ATOM   4580 C  CA    . GLY A 1 740 ? 120.399 89.454  118.551 1.00 40.62  ? 2531 GLY A CA    1 
ATOM   4581 C  C     . GLY A 1 740 ? 119.826 89.662  117.168 1.00 35.36  ? 2531 GLY A C     1 
ATOM   4582 O  O     . GLY A 1 740 ? 120.522 89.545  116.154 1.00 38.28  ? 2531 GLY A O     1 
ATOM   4583 N  N     . GLY A 1 741 ? 118.530 89.971  117.142 1.00 35.61  ? 2532 GLY A N     1 
ATOM   4584 C  CA    . GLY A 1 741 ? 117.820 90.219  115.901 1.00 32.50  ? 2532 GLY A CA    1 
ATOM   4585 C  C     . GLY A 1 741 ? 117.920 91.656  115.429 1.00 32.26  ? 2532 GLY A C     1 
ATOM   4586 O  O     . GLY A 1 741 ? 118.372 91.914  114.310 1.00 37.09  ? 2532 GLY A O     1 
ATOM   4587 N  N     . PHE A 1 742 ? 117.498 92.598  116.274 1.00 31.85  ? 2533 PHE A N     1 
ATOM   4588 C  CA    . PHE A 1 742 ? 117.679 94.033  116.045 1.00 28.63  ? 2533 PHE A CA    1 
ATOM   4589 C  C     . PHE A 1 742 ? 116.997 94.491  114.752 1.00 24.82  ? 2533 PHE A C     1 
ATOM   4590 O  O     . PHE A 1 742 ? 117.637 94.848  113.763 1.00 28.06  ? 2533 PHE A O     1 
ATOM   4591 C  CB    . PHE A 1 742 ? 119.167 94.392  116.051 1.00 29.40  ? 2533 PHE A CB    1 
ATOM   4592 C  CG    . PHE A 1 742 ? 119.839 94.119  117.357 1.00 32.92  ? 2533 PHE A CG    1 
ATOM   4593 C  CD1   . PHE A 1 742 ? 121.168 93.750  117.405 1.00 37.46  ? 2533 PHE A CD1   1 
ATOM   4594 C  CD2   . PHE A 1 742 ? 119.135 94.227  118.542 1.00 36.53  ? 2533 PHE A CD2   1 
ATOM   4595 C  CE1   . PHE A 1 742 ? 121.780 93.496  118.611 1.00 43.29  ? 2533 PHE A CE1   1 
ATOM   4596 C  CE2   . PHE A 1 742 ? 119.744 93.975  119.750 1.00 42.06  ? 2533 PHE A CE2   1 
ATOM   4597 C  CZ    . PHE A 1 742 ? 121.069 93.609  119.785 1.00 44.50  ? 2533 PHE A CZ    1 
ATOM   4598 N  N     . PHE A 1 743 ? 115.667 94.437  114.788 1.00 21.61  ? 2534 PHE A N     1 
ATOM   4599 C  CA    . PHE A 1 743 ? 114.812 95.037  113.771 1.00 17.79  ? 2534 PHE A CA    1 
ATOM   4600 C  C     . PHE A 1 743 ? 115.299 96.431  113.398 1.00 19.41  ? 2534 PHE A C     1 
ATOM   4601 O  O     . PHE A 1 743 ? 115.386 97.318  114.252 1.00 26.34  ? 2534 PHE A O     1 
ATOM   4602 C  CB    . PHE A 1 743 ? 113.379 95.108  114.302 1.00 17.42  ? 2534 PHE A CB    1 
ATOM   4603 C  CG    . PHE A 1 743 ? 112.357 95.467  113.267 1.00 15.49  ? 2534 PHE A CG    1 
ATOM   4604 C  CD1   . PHE A 1 743 ? 112.527 95.100  111.948 1.00 18.13  ? 2534 PHE A CD1   1 
ATOM   4605 C  CD2   . PHE A 1 743 ? 111.218 96.167  113.619 1.00 14.29  ? 2534 PHE A CD2   1 
ATOM   4606 C  CE1   . PHE A 1 743 ? 111.583 95.425  111.002 1.00 18.58  ? 2534 PHE A CE1   1 
ATOM   4607 C  CE2   . PHE A 1 743 ? 110.272 96.495  112.676 1.00 15.35  ? 2534 PHE A CE2   1 
ATOM   4608 C  CZ    . PHE A 1 743 ? 110.455 96.125  111.366 1.00 16.91  ? 2534 PHE A CZ    1 
ATOM   4609 N  N     . ILE A 1 744 ? 115.617 96.631  112.117 1.00 18.77  ? 2535 ILE A N     1 
ATOM   4610 C  CA    . ILE A 1 744 ? 116.204 97.876  111.645 1.00 19.52  ? 2535 ILE A CA    1 
ATOM   4611 C  C     . ILE A 1 744 ? 115.306 98.597  110.649 1.00 19.31  ? 2535 ILE A C     1 
ATOM   4612 O  O     . ILE A 1 744 ? 115.230 99.830  110.661 1.00 25.06  ? 2535 ILE A O     1 
ATOM   4613 C  CB    . ILE A 1 744 ? 117.602 97.645  111.038 1.00 19.08  ? 2535 ILE A CB    1 
ATOM   4614 C  CG1   . ILE A 1 744 ? 117.606 96.404  110.150 1.00 20.91  ? 2535 ILE A CG1   1 
ATOM   4615 C  CG2   . ILE A 1 744 ? 118.640 97.531  112.135 1.00 21.51  ? 2535 ILE A CG2   1 
ATOM   4616 C  CD1   . ILE A 1 744 ? 118.953 96.109  109.537 1.00 21.90  ? 2535 ILE A CD1   1 
ATOM   4617 N  N     . LEU A 1 745 ? 114.634 97.864  109.765 1.00 15.11  ? 2536 LEU A N     1 
ATOM   4618 C  CA    . LEU A 1 745 ? 113.850 98.511  108.725 1.00 15.73  ? 2536 LEU A CA    1 
ATOM   4619 C  C     . LEU A 1 745 ? 112.708 97.604  108.293 1.00 16.99  ? 2536 LEU A C     1 
ATOM   4620 O  O     . LEU A 1 745 ? 112.808 96.378  108.363 1.00 19.01  ? 2536 LEU A O     1 
ATOM   4621 C  CB    . LEU A 1 745 ? 114.728 98.871  107.520 1.00 17.85  ? 2536 LEU A CB    1 
ATOM   4622 C  CG    . LEU A 1 745 ? 114.121 99.766  106.441 1.00 17.36  ? 2536 LEU A CG    1 
ATOM   4623 C  CD1   . LEU A 1 745 ? 113.785 101.130 107.012 1.00 20.25  ? 2536 LEU A CD1   1 
ATOM   4624 C  CD2   . LEU A 1 745 ? 115.073 99.892  105.271 1.00 17.75  ? 2536 LEU A CD2   1 
ATOM   4625 N  N     . GLN A 1 746 ? 111.623 98.227  107.841 1.00 15.57  ? 2537 GLN A N     1 
ATOM   4626 C  CA    . GLN A 1 746 ? 110.473 97.528  107.289 1.00 16.28  ? 2537 GLN A CA    1 
ATOM   4627 C  C     . GLN A 1 746 ? 110.152 98.112  105.922 1.00 20.49  ? 2537 GLN A C     1 
ATOM   4628 O  O     . GLN A 1 746 ? 110.270 99.322  105.716 1.00 23.03  ? 2537 GLN A O     1 
ATOM   4629 C  CB    . GLN A 1 746 ? 109.258 97.638  108.220 1.00 15.66  ? 2537 GLN A CB    1 
ATOM   4630 C  CG    . GLN A 1 746 ? 107.925 97.370  107.546 1.00 18.00  ? 2537 GLN A CG    1 
ATOM   4631 C  CD    . GLN A 1 746 ? 106.780 97.292  108.527 1.00 20.25  ? 2537 GLN A CD    1 
ATOM   4632 O  OE1   . GLN A 1 746 ? 106.974 96.979  109.700 1.00 23.29  ? 2537 GLN A OE1   1 
ATOM   4633 N  NE2   . GLN A 1 746 ? 105.573 97.574  108.051 1.00 20.94  ? 2537 GLN A NE2   1 
ATOM   4634 N  N     . LEU A 1 747 ? 109.763 97.248  104.982 1.00 17.65  ? 2538 LEU A N     1 
ATOM   4635 C  CA    . LEU A 1 747 ? 109.423 97.659  103.625 1.00 17.15  ? 2538 LEU A CA    1 
ATOM   4636 C  C     . LEU A 1 747 ? 107.976 97.322  103.281 1.00 17.73  ? 2538 LEU A C     1 
ATOM   4637 O  O     . LEU A 1 747 ? 107.657 97.039  102.126 1.00 20.68  ? 2538 LEU A O     1 
ATOM   4638 C  CB    . LEU A 1 747 ? 110.371 97.021  102.614 1.00 19.05  ? 2538 LEU A CB    1 
ATOM   4639 C  CG    . LEU A 1 747 ? 111.853 97.343  102.785 1.00 18.07  ? 2538 LEU A CG    1 
ATOM   4640 C  CD1   . LEU A 1 747 ? 112.681 96.344  102.008 1.00 22.11  ? 2538 LEU A CD1   1 
ATOM   4641 C  CD2   . LEU A 1 747 ? 112.140 98.757  102.322 1.00 20.49  ? 2538 LEU A CD2   1 
ATOM   4642 N  N     . HIS A 1 748 ? 107.107 97.310  104.292 1.00 17.94  ? 2539 HIS A N     1 
ATOM   4643 C  CA    . HIS A 1 748 ? 105.664 97.108  104.170 1.00 18.83  ? 2539 HIS A CA    1 
ATOM   4644 C  C     . HIS A 1 748 ? 105.310 95.663  103.843 1.00 21.31  ? 2539 HIS A C     1 
ATOM   4645 O  O     . HIS A 1 748 ? 104.142 95.273  103.926 1.00 25.62  ? 2539 HIS A O     1 
ATOM   4646 C  CB    . HIS A 1 748 ? 105.071 98.030  103.100 1.00 20.03  ? 2539 HIS A CB    1 
ATOM   4647 C  CG    . HIS A 1 748 ? 105.527 99.452  103.197 1.00 19.78  ? 2539 HIS A CG    1 
ATOM   4648 N  ND1   . HIS A 1 748 ? 105.611 100.280 102.099 1.00 17.26  ? 2539 HIS A ND1   1 
ATOM   4649 C  CD2   . HIS A 1 748 ? 105.906 100.199 104.260 1.00 22.50  ? 2539 HIS A CD2   1 
ATOM   4650 C  CE1   . HIS A 1 748 ? 106.033 101.472 102.480 1.00 20.55  ? 2539 HIS A CE1   1 
ATOM   4651 N  NE2   . HIS A 1 748 ? 106.217 101.450 103.787 1.00 21.96  ? 2539 HIS A NE2   1 
ATOM   4652 N  N     . ASP A 1 749 ? 106.305 94.863  103.464 1.00 20.71  ? 2540 ASP A N     1 
ATOM   4653 C  CA    . ASP A 1 749 ? 106.166 93.415  103.435 1.00 19.48  ? 2540 ASP A CA    1 
ATOM   4654 C  C     . ASP A 1 749 ? 107.447 92.703  103.837 1.00 20.75  ? 2540 ASP A C     1 
ATOM   4655 O  O     . ASP A 1 749 ? 107.452 91.471  103.907 1.00 23.07  ? 2540 ASP A O     1 
ATOM   4656 C  CB    . ASP A 1 749 ? 105.720 92.934  102.045 1.00 17.49  ? 2540 ASP A CB    1 
ATOM   4657 C  CG    . ASP A 1 749 ? 106.879 92.746  101.092 1.00 25.26  ? 2540 ASP A CG    1 
ATOM   4658 O  OD1   . ASP A 1 749 ? 107.786 93.604  101.070 1.00 27.97  ? 2540 ASP A OD1   1 
ATOM   4659 O  OD2   . ASP A 1 749 ? 106.880 91.739  100.354 1.00 29.76  ? 2540 ASP A OD2   1 
ATOM   4660 N  N     . GLU A 1 750 ? 108.523 93.436  104.104 1.00 20.84  ? 2541 GLU A N     1 
ATOM   4661 C  CA    . GLU A 1 750 ? 109.850 92.872  104.296 1.00 20.81  ? 2541 GLU A CA    1 
ATOM   4662 C  C     . GLU A 1 750 ? 110.401 93.356  105.625 1.00 20.74  ? 2541 GLU A C     1 
ATOM   4663 O  O     . GLU A 1 750 ? 110.351 94.553  105.921 1.00 23.28  ? 2541 GLU A O     1 
ATOM   4664 C  CB    . GLU A 1 750 ? 110.777 93.278  103.147 1.00 19.96  ? 2541 GLU A CB    1 
ATOM   4665 C  CG    . GLU A 1 750 ? 112.139 92.617  103.157 1.00 22.90  ? 2541 GLU A CG    1 
ATOM   4666 C  CD    . GLU A 1 750 ? 112.850 92.755  101.826 1.00 27.30  ? 2541 GLU A CD    1 
ATOM   4667 O  OE1   . GLU A 1 750 ? 112.238 93.297  100.882 1.00 28.55  ? 2541 GLU A OE1   1 
ATOM   4668 O  OE2   . GLU A 1 750 ? 114.015 92.324  101.720 1.00 30.48  ? 2541 GLU A OE2   1 
ATOM   4669 N  N     . LEU A 1 751 ? 110.922 92.433  106.418 1.00 18.27  ? 2542 LEU A N     1 
ATOM   4670 C  CA    . LEU A 1 751 ? 111.444 92.733  107.746 1.00 17.77  ? 2542 LEU A CA    1 
ATOM   4671 C  C     . LEU A 1 751 ? 112.960 92.590  107.712 1.00 17.80  ? 2542 LEU A C     1 
ATOM   4672 O  O     . LEU A 1 751 ? 113.490 91.483  107.827 1.00 21.88  ? 2542 LEU A O     1 
ATOM   4673 C  CB    . LEU A 1 751 ? 110.830 91.810  108.792 1.00 21.90  ? 2542 LEU A CB    1 
ATOM   4674 C  CG    . LEU A 1 751 ? 109.471 92.184  109.378 1.00 21.62  ? 2542 LEU A CG    1 
ATOM   4675 C  CD1   . LEU A 1 751 ? 108.366 91.920  108.383 1.00 24.29  ? 2542 LEU A CD1   1 
ATOM   4676 C  CD2   . LEU A 1 751 ? 109.240 91.395  110.645 1.00 21.89  ? 2542 LEU A CD2   1 
ATOM   4677 N  N     . LEU A 1 752 ? 113.655 93.711  107.552 1.00 15.36  ? 2543 LEU A N     1 
ATOM   4678 C  CA    . LEU A 1 752 ? 115.107 93.701  107.638 1.00 17.01  ? 2543 LEU A CA    1 
ATOM   4679 C  C     . LEU A 1 752 ? 115.536 93.592  109.094 1.00 17.69  ? 2543 LEU A C     1 
ATOM   4680 O  O     . LEU A 1 752 ? 115.000 94.285  109.962 1.00 21.39  ? 2543 LEU A O     1 
ATOM   4681 C  CB    . LEU A 1 752 ? 115.690 94.962  107.007 1.00 18.87  ? 2543 LEU A CB    1 
ATOM   4682 C  CG    . LEU A 1 752 ? 116.057 94.869  105.529 1.00 16.97  ? 2543 LEU A CG    1 
ATOM   4683 C  CD1   . LEU A 1 752 ? 114.820 95.023  104.666 1.00 17.15  ? 2543 LEU A CD1   1 
ATOM   4684 C  CD2   . LEU A 1 752 ? 117.093 95.917  105.182 1.00 21.34  ? 2543 LEU A CD2   1 
ATOM   4685 N  N     . TYR A 1 753 ? 116.502 92.720  109.363 1.00 18.30  ? 2544 TYR A N     1 
ATOM   4686 C  CA    . TYR A 1 753 ? 117.004 92.503  110.712 1.00 19.40  ? 2544 TYR A CA    1 
ATOM   4687 C  C     . TYR A 1 753 ? 118.521 92.553  110.697 1.00 20.63  ? 2544 TYR A C     1 
ATOM   4688 O  O     . TYR A 1 753 ? 119.155 91.991  109.799 1.00 25.66  ? 2544 TYR A O     1 
ATOM   4689 C  CB    . TYR A 1 753 ? 116.519 91.163  111.271 1.00 22.30  ? 2544 TYR A CB    1 
ATOM   4690 C  CG    . TYR A 1 753 ? 115.109 91.209  111.806 1.00 21.64  ? 2544 TYR A CG    1 
ATOM   4691 C  CD1   . TYR A 1 753 ? 114.858 91.579  113.117 1.00 21.74  ? 2544 TYR A CD1   1 
ATOM   4692 C  CD2   . TYR A 1 753 ? 114.029 90.896  110.997 1.00 20.15  ? 2544 TYR A CD2   1 
ATOM   4693 C  CE1   . TYR A 1 753 ? 113.572 91.628  113.610 1.00 21.98  ? 2544 TYR A CE1   1 
ATOM   4694 C  CE2   . TYR A 1 753 ? 112.740 90.942  111.482 1.00 18.54  ? 2544 TYR A CE2   1 
ATOM   4695 C  CZ    . TYR A 1 753 ? 112.517 91.310  112.786 1.00 19.68  ? 2544 TYR A CZ    1 
ATOM   4696 O  OH    . TYR A 1 753 ? 111.233 91.359  113.273 1.00 25.06  ? 2544 TYR A OH    1 
ATOM   4697 N  N     . GLU A 1 754 ? 119.100 93.223  111.688 1.00 23.55  ? 2545 GLU A N     1 
ATOM   4698 C  CA    . GLU A 1 754 ? 120.553 93.334  111.807 1.00 27.98  ? 2545 GLU A CA    1 
ATOM   4699 C  C     . GLU A 1 754 ? 121.105 92.190  112.657 1.00 34.09  ? 2545 GLU A C     1 
ATOM   4700 O  O     . GLU A 1 754 ? 121.706 92.383  113.713 1.00 37.32  ? 2545 GLU A O     1 
ATOM   4701 C  CB    . GLU A 1 754 ? 120.930 94.686  112.392 1.00 27.99  ? 2545 GLU A CB    1 
ATOM   4702 C  CG    . GLU A 1 754 ? 122.251 95.208  111.900 1.00 30.85  ? 2545 GLU A CG    1 
ATOM   4703 C  CD    . GLU A 1 754 ? 122.544 96.592  112.418 1.00 40.46  ? 2545 GLU A CD    1 
ATOM   4704 O  OE1   . GLU A 1 754 ? 121.702 97.139  113.159 1.00 38.64  ? 2545 GLU A OE1   1 
ATOM   4705 O  OE2   . GLU A 1 754 ? 123.618 97.134  112.087 1.00 45.35  ? 2545 GLU A OE2   1 
ATOM   4706 N  N     . VAL A 1 755 ? 120.891 90.973  112.160 1.00 28.40  ? 2546 VAL A N     1 
ATOM   4707 C  CA    . VAL A 1 755 ? 121.231 89.777  112.918 1.00 28.04  ? 2546 VAL A CA    1 
ATOM   4708 C  C     . VAL A 1 755 ? 122.738 89.564  112.919 1.00 35.30  ? 2546 VAL A C     1 
ATOM   4709 O  O     . VAL A 1 755 ? 123.410 89.728  111.892 1.00 43.37  ? 2546 VAL A O     1 
ATOM   4710 C  CB    . VAL A 1 755 ? 120.495 88.564  112.332 1.00 30.74  ? 2546 VAL A CB    1 
ATOM   4711 C  CG1   . VAL A 1 755 ? 120.879 87.303  113.074 1.00 41.14  ? 2546 VAL A CG1   1 
ATOM   4712 C  CG2   . VAL A 1 755 ? 119.002 88.796  112.390 1.00 28.95  ? 2546 VAL A CG2   1 
ATOM   4713 N  N     . ALA A 1 756 ? 123.275 89.195  114.077 1.00 34.06  ? 2547 ALA A N     1 
ATOM   4714 C  CA    . ALA A 1 756 ? 124.700 88.937  114.202 1.00 45.19  ? 2547 ALA A CA    1 
ATOM   4715 C  C     . ALA A 1 756 ? 125.088 87.659  113.463 1.00 52.72  ? 2547 ALA A C     1 
ATOM   4716 O  O     . ALA A 1 756 ? 124.261 86.783  113.198 1.00 52.56  ? 2547 ALA A O     1 
ATOM   4717 C  CB    . ALA A 1 756 ? 125.097 88.830  115.672 1.00 49.30  ? 2547 ALA A CB    1 
ATOM   4718 N  N     . GLU A 1 757 ? 126.380 87.562  113.137 1.00 54.89  ? 2548 GLU A N     1 
ATOM   4719 C  CA    . GLU A 1 757 ? 126.874 86.427  112.361 1.00 56.65  ? 2548 GLU A CA    1 
ATOM   4720 C  C     . GLU A 1 757 ? 126.700 85.119  113.124 1.00 59.38  ? 2548 GLU A C     1 
ATOM   4721 O  O     . GLU A 1 757 ? 126.371 84.085  112.529 1.00 61.38  ? 2548 GLU A O     1 
ATOM   4722 C  CB    . GLU A 1 757 ? 128.344 86.656  111.991 1.00 58.50  ? 2548 GLU A CB    1 
ATOM   4723 C  CG    . GLU A 1 757 ? 129.220 85.409  111.800 1.00 63.63  ? 2548 GLU A CG    1 
ATOM   4724 C  CD    . GLU A 1 757 ? 128.699 84.416  110.764 1.00 61.74  ? 2548 GLU A CD    1 
ATOM   4725 O  OE1   . GLU A 1 757 ? 129.257 83.300  110.693 1.00 55.19  ? 2548 GLU A OE1   1 
ATOM   4726 O  OE2   . GLU A 1 757 ? 127.769 84.749  110.000 1.00 61.73  ? 2548 GLU A OE2   1 
ATOM   4727 N  N     . GLU A 1 758 ? 126.902 85.146  114.444 1.00 60.65  ? 2549 GLU A N     1 
ATOM   4728 C  CA    . GLU A 1 758 ? 126.808 83.923  115.235 1.00 62.77  ? 2549 GLU A CA    1 
ATOM   4729 C  C     . GLU A 1 758 ? 125.415 83.310  115.153 1.00 59.68  ? 2549 GLU A C     1 
ATOM   4730 O  O     . GLU A 1 758 ? 125.274 82.086  115.040 1.00 56.44  ? 2549 GLU A O     1 
ATOM   4731 C  CB    . GLU A 1 758 ? 127.181 84.210  116.690 1.00 65.97  ? 2549 GLU A CB    1 
ATOM   4732 C  CG    . GLU A 1 758 ? 128.583 84.767  116.874 1.00 71.83  ? 2549 GLU A CG    1 
ATOM   4733 C  CD    . GLU A 1 758 ? 128.583 86.250  117.183 1.00 79.85  ? 2549 GLU A CD    1 
ATOM   4734 O  OE1   . GLU A 1 758 ? 127.487 86.843  117.249 1.00 75.75  ? 2549 GLU A OE1   1 
ATOM   4735 O  OE2   . GLU A 1 758 ? 129.679 86.825  117.360 1.00 86.54  ? 2549 GLU A OE2   1 
ATOM   4736 N  N     . ASP A 1 759 ? 124.374 84.140  115.203 1.00 59.60  ? 2550 ASP A N     1 
ATOM   4737 C  CA    . ASP A 1 759 ? 122.996 83.668  115.182 1.00 57.37  ? 2550 ASP A CA    1 
ATOM   4738 C  C     . ASP A 1 759 ? 122.305 83.952  113.852 1.00 52.88  ? 2550 ASP A C     1 
ATOM   4739 O  O     . ASP A 1 759 ? 121.091 84.154  113.814 1.00 50.87  ? 2550 ASP A O     1 
ATOM   4740 C  CB    . ASP A 1 759 ? 122.197 84.287  116.328 1.00 59.75  ? 2550 ASP A CB    1 
ATOM   4741 C  CG    . ASP A 1 759 ? 123.018 84.460  117.586 1.00 66.37  ? 2550 ASP A CG    1 
ATOM   4742 O  OD1   . ASP A 1 759 ? 123.663 83.482  118.017 1.00 68.49  ? 2550 ASP A OD1   1 
ATOM   4743 O  OD2   . ASP A 1 759 ? 123.011 85.574  118.149 1.00 65.00  ? 2550 ASP A OD2   1 
ATOM   4744 N  N     . VAL A 1 760 ? 123.060 83.974  112.752 1.00 52.02  ? 2551 VAL A N     1 
ATOM   4745 C  CA    . VAL A 1 760 ? 122.444 84.193  111.445 1.00 49.05  ? 2551 VAL A CA    1 
ATOM   4746 C  C     . VAL A 1 760 ? 121.456 83.076  111.133 1.00 49.52  ? 2551 VAL A C     1 
ATOM   4747 O  O     . VAL A 1 760 ? 120.300 83.328  110.774 1.00 45.81  ? 2551 VAL A O     1 
ATOM   4748 C  CB    . VAL A 1 760 ? 123.522 84.318  110.352 1.00 51.81  ? 2551 VAL A CB    1 
ATOM   4749 C  CG1   . VAL A 1 760 ? 122.984 83.843  109.010 1.00 51.98  ? 2551 VAL A CG1   1 
ATOM   4750 C  CG2   . VAL A 1 760 ? 123.992 85.754  110.237 1.00 46.89  ? 2551 VAL A CG2   1 
ATOM   4751 N  N     . VAL A 1 761 ? 121.885 81.823  111.301 1.00 53.07  ? 2552 VAL A N     1 
ATOM   4752 C  CA    . VAL A 1 761 ? 121.025 80.692  110.967 1.00 51.66  ? 2552 VAL A CA    1 
ATOM   4753 C  C     . VAL A 1 761 ? 119.864 80.584  111.949 1.00 48.14  ? 2552 VAL A C     1 
ATOM   4754 O  O     . VAL A 1 761 ? 118.710 80.393  111.546 1.00 47.06  ? 2552 VAL A O     1 
ATOM   4755 C  CB    . VAL A 1 761 ? 121.851 79.393  110.912 1.00 51.50  ? 2552 VAL A CB    1 
ATOM   4756 C  CG1   . VAL A 1 761 ? 122.798 79.307  112.101 1.00 49.90  ? 2552 VAL A CG1   1 
ATOM   4757 C  CG2   . VAL A 1 761 ? 120.935 78.182  110.867 1.00 49.86  ? 2552 VAL A CG2   1 
ATOM   4758 N  N     . GLN A 1 762 ? 120.142 80.720  113.248 1.00 49.72  ? 2553 GLN A N     1 
ATOM   4759 C  CA    . GLN A 1 762 ? 119.098 80.543  114.254 1.00 51.00  ? 2553 GLN A CA    1 
ATOM   4760 C  C     . GLN A 1 762 ? 118.040 81.634  114.152 1.00 49.28  ? 2553 GLN A C     1 
ATOM   4761 O  O     . GLN A 1 762 ? 116.838 81.346  114.131 1.00 46.77  ? 2553 GLN A O     1 
ATOM   4762 C  CB    . GLN A 1 762 ? 119.714 80.519  115.652 1.00 53.93  ? 2553 GLN A CB    1 
ATOM   4763 C  CG    . GLN A 1 762 ? 118.724 80.184  116.754 1.00 55.26  ? 2553 GLN A CG    1 
ATOM   4764 C  CD    . GLN A 1 762 ? 119.061 80.863  118.065 1.00 60.67  ? 2553 GLN A CD    1 
ATOM   4765 O  OE1   . GLN A 1 762 ? 120.007 81.645  118.146 1.00 60.98  ? 2553 GLN A OE1   1 
ATOM   4766 N  NE2   . GLN A 1 762 ? 118.285 80.567  119.101 1.00 65.97  ? 2553 GLN A NE2   1 
ATOM   4767 N  N     . VAL A 1 763 ? 118.466 82.897  114.085 1.00 51.24  ? 2554 VAL A N     1 
ATOM   4768 C  CA    . VAL A 1 763 ? 117.495 83.980  113.980 1.00 44.56  ? 2554 VAL A CA    1 
ATOM   4769 C  C     . VAL A 1 763 ? 116.826 83.975  112.613 1.00 44.04  ? 2554 VAL A C     1 
ATOM   4770 O  O     . VAL A 1 763 ? 115.665 84.370  112.490 1.00 40.42  ? 2554 VAL A O     1 
ATOM   4771 C  CB    . VAL A 1 763 ? 118.147 85.339  114.288 1.00 38.06  ? 2554 VAL A CB    1 
ATOM   4772 C  CG1   . VAL A 1 763 ? 117.108 86.443  114.244 1.00 36.57  ? 2554 VAL A CG1   1 
ATOM   4773 C  CG2   . VAL A 1 763 ? 118.807 85.306  115.649 1.00 44.13  ? 2554 VAL A CG2   1 
ATOM   4774 N  N     . ALA A 1 764 ? 117.526 83.534  111.566 1.00 47.38  ? 2555 ALA A N     1 
ATOM   4775 C  CA    . ALA A 1 764 ? 116.882 83.397  110.263 1.00 42.04  ? 2555 ALA A CA    1 
ATOM   4776 C  C     . ALA A 1 764 ? 115.744 82.389  110.326 1.00 44.21  ? 2555 ALA A C     1 
ATOM   4777 O  O     . ALA A 1 764 ? 114.644 82.640  109.820 1.00 43.00  ? 2555 ALA A O     1 
ATOM   4778 C  CB    . ALA A 1 764 ? 117.909 82.984  109.209 1.00 42.03  ? 2555 ALA A CB    1 
ATOM   4779 N  N     . GLN A 1 765 ? 115.991 81.240  110.960 1.00 46.45  ? 2556 GLN A N     1 
ATOM   4780 C  CA    . GLN A 1 765 ? 114.940 80.244  111.126 1.00 45.25  ? 2556 GLN A CA    1 
ATOM   4781 C  C     . GLN A 1 765 ? 113.808 80.780  111.991 1.00 46.75  ? 2556 GLN A C     1 
ATOM   4782 O  O     . GLN A 1 765 ? 112.631 80.546  111.696 1.00 45.96  ? 2556 GLN A O     1 
ATOM   4783 C  CB    . GLN A 1 765 ? 115.519 78.966  111.729 1.00 49.00  ? 2556 GLN A CB    1 
ATOM   4784 C  CG    . GLN A 1 765 ? 114.685 77.727  111.470 1.00 52.86  ? 2556 GLN A CG    1 
ATOM   4785 C  CD    . GLN A 1 765 ? 114.939 76.635  112.488 1.00 62.54  ? 2556 GLN A CD    1 
ATOM   4786 O  OE1   . GLN A 1 765 ? 115.759 76.793  113.392 1.00 66.82  ? 2556 GLN A OE1   1 
ATOM   4787 N  NE2   . GLN A 1 765 ? 114.234 75.518  112.347 1.00 61.94  ? 2556 GLN A NE2   1 
ATOM   4788 N  N     . ILE A 1 766 ? 114.144 81.506  113.060 1.00 48.00  ? 2557 ILE A N     1 
ATOM   4789 C  CA    . ILE A 1 766 ? 113.117 82.067  113.936 1.00 46.33  ? 2557 ILE A CA    1 
ATOM   4790 C  C     . ILE A 1 766 ? 112.251 83.062  113.174 1.00 42.89  ? 2557 ILE A C     1 
ATOM   4791 O  O     . ILE A 1 766 ? 111.020 83.049  113.287 1.00 40.35  ? 2557 ILE A O     1 
ATOM   4792 C  CB    . ILE A 1 766 ? 113.766 82.712  115.176 1.00 44.78  ? 2557 ILE A CB    1 
ATOM   4793 C  CG1   . ILE A 1 766 ? 113.963 81.671  116.278 1.00 50.09  ? 2557 ILE A CG1   1 
ATOM   4794 C  CG2   . ILE A 1 766 ? 112.922 83.866  115.693 1.00 35.17  ? 2557 ILE A CG2   1 
ATOM   4795 C  CD1   . ILE A 1 766 ? 114.846 82.145  117.410 1.00 55.01  ? 2557 ILE A CD1   1 
ATOM   4796 N  N     . VAL A 1 767 ? 112.878 83.933  112.383 1.00 41.73  ? 2558 VAL A N     1 
ATOM   4797 C  CA    . VAL A 1 767 ? 112.140 84.937  111.623 1.00 34.80  ? 2558 VAL A CA    1 
ATOM   4798 C  C     . VAL A 1 767 ? 111.249 84.266  110.587 1.00 34.98  ? 2558 VAL A C     1 
ATOM   4799 O  O     . VAL A 1 767 ? 110.069 84.605  110.447 1.00 34.23  ? 2558 VAL A O     1 
ATOM   4800 C  CB    . VAL A 1 767 ? 113.113 85.934  110.970 1.00 31.51  ? 2558 VAL A CB    1 
ATOM   4801 C  CG1   . VAL A 1 767 ? 112.422 86.704  109.862 1.00 28.68  ? 2558 VAL A CG1   1 
ATOM   4802 C  CG2   . VAL A 1 767 ? 113.677 86.884  112.010 1.00 28.76  ? 2558 VAL A CG2   1 
ATOM   4803 N  N     . LYS A 1 768 ? 111.798 83.298  109.849 1.00 35.91  ? 2559 LYS A N     1 
ATOM   4804 C  CA    . LYS A 1 768 ? 111.004 82.609  108.838 1.00 36.89  ? 2559 LYS A CA    1 
ATOM   4805 C  C     . LYS A 1 768 ? 109.826 81.878  109.469 1.00 42.10  ? 2559 LYS A C     1 
ATOM   4806 O  O     . LYS A 1 768 ? 108.706 81.925  108.947 1.00 44.22  ? 2559 LYS A O     1 
ATOM   4807 C  CB    . LYS A 1 768 ? 111.884 81.640  108.050 1.00 36.75  ? 2559 LYS A CB    1 
ATOM   4808 C  CG    . LYS A 1 768 ? 111.124 80.776  107.057 1.00 38.41  ? 2559 LYS A CG    1 
ATOM   4809 C  CD    . LYS A 1 768 ? 112.017 80.342  105.906 1.00 43.84  ? 2559 LYS A CD    1 
ATOM   4810 C  CE    . LYS A 1 768 ? 113.252 79.613  106.406 1.00 51.56  ? 2559 LYS A CE    1 
ATOM   4811 N  NZ    . LYS A 1 768 ? 114.213 79.331  105.305 1.00 51.70  ? 2559 LYS A NZ    1 
ATOM   4812 N  N     . ASN A 1 769 ? 110.056 81.209  110.602 1.00 41.42  ? 2560 ASN A N     1 
ATOM   4813 C  CA    . ASN A 1 769 ? 108.977 80.494  111.272 1.00 36.50  ? 2560 ASN A CA    1 
ATOM   4814 C  C     . ASN A 1 769 ? 107.911 81.450  111.791 1.00 36.22  ? 2560 ASN A C     1 
ATOM   4815 O  O     . ASN A 1 769 ? 106.717 81.208  111.604 1.00 32.09  ? 2560 ASN A O     1 
ATOM   4816 C  CB    . ASN A 1 769 ? 109.540 79.647  112.412 1.00 40.27  ? 2560 ASN A CB    1 
ATOM   4817 C  CG    . ASN A 1 769 ? 110.221 78.386  111.917 1.00 52.60  ? 2560 ASN A CG    1 
ATOM   4818 O  OD1   . ASN A 1 769 ? 109.937 77.903  110.821 1.00 50.95  ? 2560 ASN A OD1   1 
ATOM   4819 N  ND2   . ASN A 1 769 ? 111.125 77.845  112.726 1.00 60.37  ? 2560 ASN A ND2   1 
ATOM   4820 N  N     . GLU A 1 770 ? 108.317 82.549  112.433 1.00 39.37  ? 2561 GLU A N     1 
ATOM   4821 C  CA    . GLU A 1 770 ? 107.345 83.475  113.000 1.00 35.29  ? 2561 GLU A CA    1 
ATOM   4822 C  C     . GLU A 1 770 ? 106.616 84.276  111.932 1.00 35.32  ? 2561 GLU A C     1 
ATOM   4823 O  O     . GLU A 1 770 ? 105.531 84.800  112.203 1.00 34.85  ? 2561 GLU A O     1 
ATOM   4824 C  CB    . GLU A 1 770 ? 108.029 84.422  113.985 1.00 28.92  ? 2561 GLU A CB    1 
ATOM   4825 C  CG    . GLU A 1 770 ? 108.584 83.734  115.220 1.00 36.62  ? 2561 GLU A CG    1 
ATOM   4826 C  CD    . GLU A 1 770 ? 107.541 82.910  115.948 1.00 42.94  ? 2561 GLU A CD    1 
ATOM   4827 O  OE1   . GLU A 1 770 ? 106.494 83.473  116.327 1.00 41.00  ? 2561 GLU A OE1   1 
ATOM   4828 O  OE2   . GLU A 1 770 ? 107.769 81.698  116.142 1.00 46.81  ? 2561 GLU A OE2   1 
ATOM   4829 N  N     . MET A 1 771 ? 107.186 84.387  110.732 1.00 34.12  ? 2562 MET A N     1 
ATOM   4830 C  CA    . MET A 1 771 ? 106.495 85.069  109.646 1.00 31.91  ? 2562 MET A CA    1 
ATOM   4831 C  C     . MET A 1 771 ? 105.554 84.127  108.905 1.00 37.72  ? 2562 MET A C     1 
ATOM   4832 O  O     . MET A 1 771 ? 104.462 84.535  108.494 1.00 39.56  ? 2562 MET A O     1 
ATOM   4833 C  CB    . MET A 1 771 ? 107.520 85.682  108.694 1.00 28.83  ? 2562 MET A CB    1 
ATOM   4834 C  CG    . MET A 1 771 ? 108.266 86.855  109.302 1.00 30.48  ? 2562 MET A CG    1 
ATOM   4835 S  SD    . MET A 1 771 ? 109.358 87.709  108.159 1.00 39.31  ? 2562 MET A SD    1 
ATOM   4836 C  CE    . MET A 1 771 ? 108.192 88.545  107.100 1.00 27.27  ? 2562 MET A CE    1 
ATOM   4837 N  N     . GLU A 1 772 ? 105.954 82.866  108.728 1.00 38.31  ? 2563 GLU A N     1 
ATOM   4838 C  CA    . GLU A 1 772 ? 105.060 81.896  108.105 1.00 38.16  ? 2563 GLU A CA    1 
ATOM   4839 C  C     . GLU A 1 772 ? 103.957 81.464  109.065 1.00 39.05  ? 2563 GLU A C     1 
ATOM   4840 O  O     . GLU A 1 772 ? 102.797 81.322  108.663 1.00 38.51  ? 2563 GLU A O     1 
ATOM   4841 C  CB    . GLU A 1 772 ? 105.857 80.685  107.621 1.00 40.35  ? 2563 GLU A CB    1 
ATOM   4842 C  CG    . GLU A 1 772 ? 106.808 80.982  106.475 1.00 39.44  ? 2563 GLU A CG    1 
ATOM   4843 C  CD    . GLU A 1 772 ? 107.588 79.760  106.034 1.00 54.25  ? 2563 GLU A CD    1 
ATOM   4844 O  OE1   . GLU A 1 772 ? 107.338 78.666  106.582 1.00 58.88  ? 2563 GLU A OE1   1 
ATOM   4845 O  OE2   . GLU A 1 772 ? 108.450 79.892  105.140 1.00 55.61  ? 2563 GLU A OE2   1 
ATOM   4846 N  N     . SER A 1 773 ? 104.298 81.259  110.336 1.00 36.62  ? 2564 SER A N     1 
ATOM   4847 C  CA    . SER A 1 773 ? 103.354 80.828  111.359 1.00 36.53  ? 2564 SER A CA    1 
ATOM   4848 C  C     . SER A 1 773 ? 102.614 82.004  111.992 1.00 38.12  ? 2564 SER A C     1 
ATOM   4849 O  O     . SER A 1 773 ? 101.917 81.826  112.996 1.00 39.04  ? 2564 SER A O     1 
ATOM   4850 C  CB    . SER A 1 773 ? 104.089 79.985  112.416 1.00 39.68  ? 2564 SER A CB    1 
ATOM   4851 O  OG    . SER A 1 773 ? 103.484 80.006  113.696 1.00 41.84  ? 2564 SER A OG    1 
ATOM   4852 N  N     . ALA A 1 774 ? 102.699 83.185  111.391 1.00 39.26  ? 2565 ALA A N     1 
ATOM   4853 C  CA    . ALA A 1 774 ? 101.875 84.313  111.803 1.00 36.82  ? 2565 ALA A CA    1 
ATOM   4854 C  C     . ALA A 1 774 ? 100.432 84.004  111.408 1.00 38.71  ? 2565 ALA A C     1 
ATOM   4855 O  O     . ALA A 1 774 ? 100.108 82.890  110.985 1.00 41.44  ? 2565 ALA A O     1 
ATOM   4856 C  CB    . ALA A 1 774 ? 102.388 85.608  111.183 1.00 28.93  ? 2565 ALA A CB    1 
ATOM   4857 N  N     . VAL A 1 775 ? 99.539  84.983  111.564 1.00 32.90  ? 2566 VAL A N     1 
ATOM   4858 C  CA    . VAL A 1 775 ? 98.112  84.753  111.353 1.00 34.45  ? 2566 VAL A CA    1 
ATOM   4859 C  C     . VAL A 1 775 ? 97.903  84.052  110.018 1.00 35.95  ? 2566 VAL A C     1 
ATOM   4860 O  O     . VAL A 1 775 ? 98.266  84.572  108.957 1.00 34.17  ? 2566 VAL A O     1 
ATOM   4861 C  CB    . VAL A 1 775 ? 97.312  86.065  111.439 1.00 31.21  ? 2566 VAL A CB    1 
ATOM   4862 C  CG1   . VAL A 1 775 ? 97.207  86.512  112.886 1.00 35.16  ? 2566 VAL A CG1   1 
ATOM   4863 C  CG2   . VAL A 1 775 ? 97.968  87.149  110.604 1.00 26.45  ? 2566 VAL A CG2   1 
ATOM   4864 N  N     . LYS A 1 776 ? 97.336  82.852  110.073 1.00 37.28  ? 2567 LYS A N     1 
ATOM   4865 C  CA    . LYS A 1 776 ? 97.358  81.923  108.957 1.00 35.75  ? 2567 LYS A CA    1 
ATOM   4866 C  C     . LYS A 1 776 ? 96.107  82.068  108.103 1.00 37.73  ? 2567 LYS A C     1 
ATOM   4867 O  O     . LYS A 1 776 ? 95.032  82.431  108.589 1.00 36.39  ? 2567 LYS A O     1 
ATOM   4868 C  CB    . LYS A 1 776 ? 97.495  80.481  109.451 1.00 37.28  ? 2567 LYS A CB    1 
ATOM   4869 C  CG    . LYS A 1 776 ? 96.260  79.925  110.135 1.00 38.09  ? 2567 LYS A CG    1 
ATOM   4870 C  CD    . LYS A 1 776 ? 96.504  78.512  110.637 1.00 41.93  ? 2567 LYS A CD    1 
ATOM   4871 C  CE    . LYS A 1 776 ? 97.144  77.646  109.563 1.00 36.38  ? 2567 LYS A CE    1 
ATOM   4872 N  NZ    . LYS A 1 776 ? 96.128  76.999  108.689 1.00 34.25  ? 2567 LYS A NZ    1 
ATOM   4873 N  N     . LEU A 1 777 ? 96.267  81.784  106.819 1.00 36.63  ? 2568 LEU A N     1 
ATOM   4874 C  CA    . LEU A 1 777 ? 95.231  81.955  105.817 1.00 35.09  ? 2568 LEU A CA    1 
ATOM   4875 C  C     . LEU A 1 777 ? 94.938  80.617  105.147 1.00 39.10  ? 2568 LEU A C     1 
ATOM   4876 O  O     . LEU A 1 777 ? 95.542  79.588  105.463 1.00 41.62  ? 2568 LEU A O     1 
ATOM   4877 C  CB    . LEU A 1 777 ? 95.664  83.001  104.787 1.00 34.97  ? 2568 LEU A CB    1 
ATOM   4878 C  CG    . LEU A 1 777 ? 96.503  84.180  105.285 1.00 30.19  ? 2568 LEU A CG    1 
ATOM   4879 C  CD1   . LEU A 1 777 ? 96.978  85.022  104.117 1.00 24.37  ? 2568 LEU A CD1   1 
ATOM   4880 C  CD2   . LEU A 1 777 ? 95.714  85.030  106.264 1.00 31.56  ? 2568 LEU A CD2   1 
ATOM   4881 N  N     . SER A 1 778 ? 93.989  80.637  104.208 1.00 39.41  ? 2569 SER A N     1 
ATOM   4882 C  CA    . SER A 1 778 ? 93.763  79.468  103.369 1.00 40.07  ? 2569 SER A CA    1 
ATOM   4883 C  C     . SER A 1 778 ? 94.941  79.200  102.444 1.00 41.22  ? 2569 SER A C     1 
ATOM   4884 O  O     . SER A 1 778 ? 95.068  78.086  101.926 1.00 41.81  ? 2569 SER A O     1 
ATOM   4885 C  CB    . SER A 1 778 ? 92.482  79.641  102.553 1.00 37.91  ? 2569 SER A CB    1 
ATOM   4886 O  OG    . SER A 1 778 ? 92.509  80.843  101.806 1.00 35.22  ? 2569 SER A OG    1 
ATOM   4887 N  N     . VAL A 1 779 ? 95.798  80.195  102.229 1.00 40.19  ? 2570 VAL A N     1 
ATOM   4888 C  CA    . VAL A 1 779 ? 97.011  80.052  101.434 1.00 38.27  ? 2570 VAL A CA    1 
ATOM   4889 C  C     . VAL A 1 779 ? 98.206  80.128  102.370 1.00 38.10  ? 2570 VAL A C     1 
ATOM   4890 O  O     . VAL A 1 779 ? 98.285  81.027  103.215 1.00 39.50  ? 2570 VAL A O     1 
ATOM   4891 C  CB    . VAL A 1 779 ? 97.096  81.136  100.346 1.00 36.42  ? 2570 VAL A CB    1 
ATOM   4892 C  CG1   . VAL A 1 779 ? 98.540  81.444  100.013 1.00 35.21  ? 2570 VAL A CG1   1 
ATOM   4893 C  CG2   . VAL A 1 779 ? 96.372  80.685  99.105  1.00 44.40  ? 2570 VAL A CG2   1 
ATOM   4894 N  N     . LYS A 1 780 ? 99.126  79.177  102.233 1.00 39.91  ? 2571 LYS A N     1 
ATOM   4895 C  CA    . LYS A 1 780 ? 100.348 79.205  103.024 1.00 41.95  ? 2571 LYS A CA    1 
ATOM   4896 C  C     . LYS A 1 780 ? 101.125 80.483  102.739 1.00 36.77  ? 2571 LYS A C     1 
ATOM   4897 O  O     . LYS A 1 780 ? 101.339 80.848  101.581 1.00 37.88  ? 2571 LYS A O     1 
ATOM   4898 C  CB    . LYS A 1 780 ? 101.205 77.979  102.709 1.00 43.54  ? 2571 LYS A CB    1 
ATOM   4899 C  CG    . LYS A 1 780 ? 102.568 77.982  103.378 1.00 46.00  ? 2571 LYS A CG    1 
ATOM   4900 C  CD    . LYS A 1 780 ? 103.512 76.996  102.709 1.00 47.33  ? 2571 LYS A CD    1 
ATOM   4901 C  CE    . LYS A 1 780 ? 102.910 75.602  102.659 1.00 51.11  ? 2571 LYS A CE    1 
ATOM   4902 N  NZ    . LYS A 1 780 ? 102.617 75.074  104.020 1.00 51.09  ? 2571 LYS A NZ    1 
ATOM   4903 N  N     . LEU A 1 781 ? 101.541 81.167  103.800 1.00 33.66  ? 2572 LEU A N     1 
ATOM   4904 C  CA    . LEU A 1 781 ? 102.312 82.398  103.676 1.00 33.49  ? 2572 LEU A CA    1 
ATOM   4905 C  C     . LEU A 1 781 ? 103.785 82.028  103.562 1.00 36.53  ? 2572 LEU A C     1 
ATOM   4906 O  O     . LEU A 1 781 ? 104.370 81.484  104.503 1.00 42.77  ? 2572 LEU A O     1 
ATOM   4907 C  CB    . LEU A 1 781 ? 102.065 83.317  104.869 1.00 32.50  ? 2572 LEU A CB    1 
ATOM   4908 C  CG    . LEU A 1 781 ? 100.770 84.131  104.866 1.00 26.59  ? 2572 LEU A CG    1 
ATOM   4909 C  CD1   . LEU A 1 781 ? 100.688 84.996  106.108 1.00 27.27  ? 2572 LEU A CD1   1 
ATOM   4910 C  CD2   . LEU A 1 781 ? 100.675 84.984  103.617 1.00 27.29  ? 2572 LEU A CD2   1 
ATOM   4911 N  N     . LYS A 1 782 ? 104.381 82.315  102.412 1.00 35.45  ? 2573 LYS A N     1 
ATOM   4912 C  CA    . LYS A 1 782 ? 105.778 82.002  102.161 1.00 34.37  ? 2573 LYS A CA    1 
ATOM   4913 C  C     . LYS A 1 782 ? 106.628 83.261  102.253 1.00 30.32  ? 2573 LYS A C     1 
ATOM   4914 O  O     . LYS A 1 782 ? 106.186 84.359  101.910 1.00 31.27  ? 2573 LYS A O     1 
ATOM   4915 C  CB    . LYS A 1 782 ? 105.958 81.354  100.787 1.00 35.96  ? 2573 LYS A CB    1 
ATOM   4916 C  CG    . LYS A 1 782 ? 105.789 79.845  100.787 1.00 38.76  ? 2573 LYS A CG    1 
ATOM   4917 C  CD    . LYS A 1 782 ? 106.292 79.236  99.490  1.00 43.61  ? 2573 LYS A CD    1 
ATOM   4918 C  CE    . LYS A 1 782 ? 107.803 79.072  99.508  1.00 47.69  ? 2573 LYS A CE    1 
ATOM   4919 N  NZ    . LYS A 1 782 ? 108.210 77.720  99.981  1.00 54.54  ? 2573 LYS A NZ    1 
ATOM   4920 N  N     . VAL A 1 783 ? 107.857 83.090  102.739 1.00 30.69  ? 2574 VAL A N     1 
ATOM   4921 C  CA    . VAL A 1 783 ? 108.836 84.164  102.802 1.00 31.50  ? 2574 VAL A CA    1 
ATOM   4922 C  C     . VAL A 1 783 ? 110.115 83.677  102.138 1.00 32.21  ? 2574 VAL A C     1 
ATOM   4923 O  O     . VAL A 1 783 ? 110.338 82.477  101.968 1.00 35.85  ? 2574 VAL A O     1 
ATOM   4924 C  CB    . VAL A 1 783 ? 109.125 84.629  104.248 1.00 32.29  ? 2574 VAL A CB    1 
ATOM   4925 C  CG1   . VAL A 1 783 ? 107.833 84.864  105.004 1.00 33.30  ? 2574 VAL A CG1   1 
ATOM   4926 C  CG2   . VAL A 1 783 ? 109.992 83.618  104.971 1.00 35.71  ? 2574 VAL A CG2   1 
ATOM   4927 N  N     . LYS A 1 784 ? 110.956 84.631  101.752 1.00 29.18  ? 2575 LYS A N     1 
ATOM   4928 C  CA    . LYS A 1 784 ? 112.263 84.349  101.166 1.00 33.60  ? 2575 LYS A CA    1 
ATOM   4929 C  C     . LYS A 1 784 ? 113.300 85.073  102.015 1.00 29.27  ? 2575 LYS A C     1 
ATOM   4930 O  O     . LYS A 1 784 ? 113.592 86.249  101.790 1.00 28.15  ? 2575 LYS A O     1 
ATOM   4931 C  CB    . LYS A 1 784 ? 112.326 84.779  99.702  1.00 40.38  ? 2575 LYS A CB    1 
ATOM   4932 C  CG    . LYS A 1 784 ? 111.913 83.693  98.721  1.00 40.35  ? 2575 LYS A CG    1 
ATOM   4933 C  CD    . LYS A 1 784 ? 111.244 84.281  97.493  1.00 46.58  ? 2575 LYS A CD    1 
ATOM   4934 C  CE    . LYS A 1 784 ? 109.974 85.027  97.862  1.00 42.11  ? 2575 LYS A CE    1 
ATOM   4935 N  NZ    . LYS A 1 784 ? 109.231 85.486  96.657  1.00 43.57  ? 2575 LYS A NZ    1 
ATOM   4936 N  N     . VAL A 1 785 ? 113.850 84.365  103.000 1.00 30.43  ? 2576 VAL A N     1 
ATOM   4937 C  CA    . VAL A 1 785 ? 114.879 84.944  103.851 1.00 32.80  ? 2576 VAL A CA    1 
ATOM   4938 C  C     . VAL A 1 785 ? 116.151 85.133  103.038 1.00 35.65  ? 2576 VAL A C     1 
ATOM   4939 O  O     . VAL A 1 785 ? 116.649 84.193  102.406 1.00 43.24  ? 2576 VAL A O     1 
ATOM   4940 C  CB    . VAL A 1 785 ? 115.123 84.056  105.079 1.00 35.34  ? 2576 VAL A CB    1 
ATOM   4941 C  CG1   . VAL A 1 785 ? 116.331 84.546  105.857 1.00 37.15  ? 2576 VAL A CG1   1 
ATOM   4942 C  CG2   . VAL A 1 785 ? 113.891 84.032  105.963 1.00 34.12  ? 2576 VAL A CG2   1 
ATOM   4943 N  N     . LYS A 1 786 ? 116.679 86.353  103.048 1.00 28.60  ? 2577 LYS A N     1 
ATOM   4944 C  CA    . LYS A 1 786 ? 117.857 86.722  102.282 1.00 28.23  ? 2577 LYS A CA    1 
ATOM   4945 C  C     . LYS A 1 786 ? 118.924 87.254  103.226 1.00 27.66  ? 2577 LYS A C     1 
ATOM   4946 O  O     . LYS A 1 786 ? 118.679 88.201  103.986 1.00 29.72  ? 2577 LYS A O     1 
ATOM   4947 C  CB    . LYS A 1 786 ? 117.510 87.765  101.219 1.00 30.84  ? 2577 LYS A CB    1 
ATOM   4948 C  CG    . LYS A 1 786 ? 116.267 87.424  100.415 1.00 33.35  ? 2577 LYS A CG    1 
ATOM   4949 C  CD    . LYS A 1 786 ? 115.864 88.558  99.491  1.00 33.87  ? 2577 LYS A CD    1 
ATOM   4950 C  CE    . LYS A 1 786 ? 116.820 88.674  98.320  1.00 31.49  ? 2577 LYS A CE    1 
ATOM   4951 N  NZ    . LYS A 1 786 ? 116.891 87.410  97.538  1.00 30.20  ? 2577 LYS A NZ    1 
ATOM   4952 N  N     . ILE A 1 787 ? 120.107 86.649  103.157 1.00 33.67  ? 2578 ILE A N     1 
ATOM   4953 C  CA    . ILE A 1 787 ? 121.252 87.007  103.985 1.00 35.54  ? 2578 ILE A CA    1 
ATOM   4954 C  C     . ILE A 1 787 ? 122.187 87.861  103.145 1.00 35.78  ? 2578 ILE A C     1 
ATOM   4955 O  O     . ILE A 1 787 ? 122.449 87.542  101.980 1.00 39.24  ? 2578 ILE A O     1 
ATOM   4956 C  CB    . ILE A 1 787 ? 121.974 85.750  104.503 1.00 40.77  ? 2578 ILE A CB    1 
ATOM   4957 C  CG1   . ILE A 1 787 ? 121.228 85.153  105.692 1.00 40.80  ? 2578 ILE A CG1   1 
ATOM   4958 C  CG2   . ILE A 1 787 ? 123.407 86.070  104.898 1.00 40.23  ? 2578 ILE A CG2   1 
ATOM   4959 C  CD1   . ILE A 1 787 ? 120.816 86.174  106.702 1.00 35.97  ? 2578 ILE A CD1   1 
ATOM   4960 N  N     . GLY A 1 788 ? 122.675 88.951  103.714 1.00 31.05  ? 2579 GLY A N     1 
ATOM   4961 C  CA    . GLY A 1 788 ? 123.584 89.813  102.981 1.00 34.36  ? 2579 GLY A CA    1 
ATOM   4962 C  C     . GLY A 1 788 ? 124.569 90.500  103.892 1.00 36.43  ? 2579 GLY A C     1 
ATOM   4963 O  O     . GLY A 1 788 ? 124.269 90.799  105.052 1.00 35.22  ? 2579 GLY A O     1 
ATOM   4964 N  N     . ALA A 1 789 ? 125.765 90.751  103.358 1.00 38.82  ? 2580 ALA A N     1 
ATOM   4965 C  CA    . ALA A 1 789 ? 126.701 91.649  104.017 1.00 38.51  ? 2580 ALA A CA    1 
ATOM   4966 C  C     . ALA A 1 789 ? 126.227 93.091  103.973 1.00 36.84  ? 2580 ALA A C     1 
ATOM   4967 O  O     . ALA A 1 789 ? 126.814 93.943  104.647 1.00 40.68  ? 2580 ALA A O     1 
ATOM   4968 C  CB    . ALA A 1 789 ? 128.085 91.535  103.376 1.00 40.51  ? 2580 ALA A CB    1 
ATOM   4969 N  N     . SER A 1 790 ? 125.194 93.375  103.188 1.00 32.97  ? 2581 SER A N     1 
ATOM   4970 C  CA    . SER A 1 790 ? 124.579 94.692  103.109 1.00 32.53  ? 2581 SER A CA    1 
ATOM   4971 C  C     . SER A 1 790 ? 123.155 94.502  102.607 1.00 26.56  ? 2581 SER A C     1 
ATOM   4972 O  O     . SER A 1 790 ? 122.689 93.376  102.416 1.00 29.53  ? 2581 SER A O     1 
ATOM   4973 C  CB    . SER A 1 790 ? 125.378 95.626  102.198 1.00 37.13  ? 2581 SER A CB    1 
ATOM   4974 O  OG    . SER A 1 790 ? 126.289 96.414  102.943 1.00 39.72  ? 2581 SER A OG    1 
ATOM   4975 N  N     . TRP A 1 791 ? 122.461 95.616  102.399 1.00 22.53  ? 2582 TRP A N     1 
ATOM   4976 C  CA    . TRP A 1 791 ? 121.135 95.573  101.800 1.00 21.78  ? 2582 TRP A CA    1 
ATOM   4977 C  C     . TRP A 1 791 ? 121.188 95.407  100.288 1.00 28.37  ? 2582 TRP A C     1 
ATOM   4978 O  O     . TRP A 1 791 ? 120.142 95.208  99.662  1.00 30.13  ? 2582 TRP A O     1 
ATOM   4979 C  CB    . TRP A 1 791 ? 120.362 96.841  102.170 1.00 22.44  ? 2582 TRP A CB    1 
ATOM   4980 C  CG    . TRP A 1 791 ? 118.885 96.767  101.939 1.00 18.82  ? 2582 TRP A CG    1 
ATOM   4981 C  CD1   . TRP A 1 791 ? 118.144 95.651  101.691 1.00 16.29  ? 2582 TRP A CD1   1 
ATOM   4982 C  CD2   . TRP A 1 791 ? 117.968 97.865  101.933 1.00 20.31  ? 2582 TRP A CD2   1 
ATOM   4983 N  NE1   . TRP A 1 791 ? 116.823 95.987  101.528 1.00 14.99  ? 2582 TRP A NE1   1 
ATOM   4984 C  CE2   . TRP A 1 791 ? 116.690 97.342  101.674 1.00 17.55  ? 2582 TRP A CE2   1 
ATOM   4985 C  CE3   . TRP A 1 791 ? 118.106 99.242  102.124 1.00 21.07  ? 2582 TRP A CE3   1 
ATOM   4986 C  CZ2   . TRP A 1 791 ? 115.559 98.146  101.598 1.00 18.93  ? 2582 TRP A CZ2   1 
ATOM   4987 C  CZ3   . TRP A 1 791 ? 116.982 100.038 102.048 1.00 19.40  ? 2582 TRP A CZ3   1 
ATOM   4988 C  CH2   . TRP A 1 791 ? 115.725 99.489  101.787 1.00 19.08  ? 2582 TRP A CH2   1 
ATOM   4989 N  N     . GLY A 1 792 ? 122.374 95.476  99.689  1.00 32.25  ? 2583 GLY A N     1 
ATOM   4990 C  CA    . GLY A 1 792 ? 122.509 95.293  98.259  1.00 33.50  ? 2583 GLY A CA    1 
ATOM   4991 C  C     . GLY A 1 792 ? 122.670 93.844  97.846  1.00 32.94  ? 2583 GLY A C     1 
ATOM   4992 O  O     . GLY A 1 792 ? 121.893 93.338  97.032  1.00 36.85  ? 2583 GLY A O     1 
ATOM   4993 N  N     . GLU A 1 793 ? 123.674 93.164  98.402  1.00 31.70  ? 2584 GLU A N     1 
ATOM   4994 C  CA    . GLU A 1 793 ? 123.976 91.782  98.028  1.00 34.39  ? 2584 GLU A CA    1 
ATOM   4995 C  C     . GLU A 1 793 ? 123.205 90.839  98.946  1.00 34.98  ? 2584 GLU A C     1 
ATOM   4996 O  O     . GLU A 1 793 ? 123.765 90.116  99.772  1.00 38.43  ? 2584 GLU A O     1 
ATOM   4997 C  CB    . GLU A 1 793 ? 125.477 91.523  98.078  1.00 38.24  ? 2584 GLU A CB    1 
ATOM   4998 C  CG    . GLU A 1 793 ? 126.162 91.963  99.362  1.00 42.04  ? 2584 GLU A CG    1 
ATOM   4999 C  CD    . GLU A 1 793 ? 126.817 93.318  99.237  1.00 49.28  ? 2584 GLU A CD    1 
ATOM   5000 O  OE1   . GLU A 1 793 ? 126.325 94.144  98.443  1.00 47.41  ? 2584 GLU A OE1   1 
ATOM   5001 O  OE2   . GLU A 1 793 ? 127.826 93.554  99.933  1.00 53.08  ? 2584 GLU A OE2   1 
ATOM   5002 N  N     . LEU A 1 794 ? 121.884 90.837  98.779  1.00 31.11  ? 2585 LEU A N     1 
ATOM   5003 C  CA    . LEU A 1 794 ? 121.011 89.974  99.571  1.00 31.69  ? 2585 LEU A CA    1 
ATOM   5004 C  C     . LEU A 1 794 ? 120.907 88.621  98.872  1.00 35.29  ? 2585 LEU A C     1 
ATOM   5005 O  O     . LEU A 1 794 ? 119.992 88.351  98.091  1.00 36.23  ? 2585 LEU A O     1 
ATOM   5006 C  CB    . LEU A 1 794 ? 119.647 90.622  99.763  1.00 29.53  ? 2585 LEU A CB    1 
ATOM   5007 C  CG    . LEU A 1 794 ? 119.517 91.597  100.933 1.00 27.49  ? 2585 LEU A CG    1 
ATOM   5008 C  CD1   . LEU A 1 794 ? 118.095 92.116  101.031 1.00 25.48  ? 2585 LEU A CD1   1 
ATOM   5009 C  CD2   . LEU A 1 794 ? 119.942 90.943  102.235 1.00 27.05  ? 2585 LEU A CD2   1 
ATOM   5010 N  N     . LYS A 1 795 ? 121.877 87.757  99.158  1.00 35.67  ? 2586 LYS A N     1 
ATOM   5011 C  CA    . LYS A 1 795 ? 121.869 86.421  98.587  1.00 36.28  ? 2586 LYS A CA    1 
ATOM   5012 C  C     . LYS A 1 795 ? 120.791 85.570  99.247  1.00 40.69  ? 2586 LYS A C     1 
ATOM   5013 O  O     . LYS A 1 795 ? 120.535 85.673  100.450 1.00 41.31  ? 2586 LYS A O     1 
ATOM   5014 C  CB    . LYS A 1 795 ? 123.236 85.760  98.757  1.00 38.59  ? 2586 LYS A CB    1 
ATOM   5015 C  CG    . LYS A 1 795 ? 124.364 86.465  98.022  1.00 39.39  ? 2586 LYS A CG    1 
ATOM   5016 C  CD    . LYS A 1 795 ? 124.185 86.371  96.519  1.00 42.25  ? 2586 LYS A CD    1 
ATOM   5017 C  CE    . LYS A 1 795 ? 125.220 87.208  95.787  1.00 45.69  ? 2586 LYS A CE    1 
ATOM   5018 N  NZ    . LYS A 1 795 ? 125.044 88.663  96.045  1.00 40.36  ? 2586 LYS A NZ    1 
ATOM   5019 N  N     . ASP A 1 796 ? 120.164 84.713  98.447  1.00 44.52  ? 2587 ASP A N     1 
ATOM   5020 C  CA    . ASP A 1 796 ? 119.081 83.881  98.951  1.00 45.92  ? 2587 ASP A CA    1 
ATOM   5021 C  C     . ASP A 1 796 ? 119.592 82.934  100.030 1.00 47.77  ? 2587 ASP A C     1 
ATOM   5022 O  O     . ASP A 1 796 ? 120.722 82.443  99.968  1.00 51.32  ? 2587 ASP A O     1 
ATOM   5023 C  CB    . ASP A 1 796 ? 118.446 83.088  97.809  1.00 49.29  ? 2587 ASP A CB    1 
ATOM   5024 C  CG    . ASP A 1 796 ? 116.961 82.863  98.012  1.00 55.43  ? 2587 ASP A CG    1 
ATOM   5025 O  OD1   . ASP A 1 796 ? 116.527 82.741  99.176  1.00 49.86  ? 2587 ASP A OD1   1 
ATOM   5026 O  OD2   . ASP A 1 796 ? 116.226 82.810  97.004  1.00 63.63  ? 2587 ASP A OD2   1 
ATOM   5027 N  N     . PHE A 1 797 ? 118.747 82.685  101.029 1.00 46.44  ? 2588 PHE A N     1 
ATOM   5028 C  CA    . PHE A 1 797 ? 119.101 81.848  102.175 1.00 48.44  ? 2588 PHE A CA    1 
ATOM   5029 C  C     . PHE A 1 797 ? 117.920 80.921  102.446 1.00 52.24  ? 2588 PHE A C     1 
ATOM   5030 O  O     . PHE A 1 797 ? 116.938 81.326  103.075 1.00 50.97  ? 2588 PHE A O     1 
ATOM   5031 C  CB    . PHE A 1 797 ? 119.435 82.702  103.392 1.00 46.37  ? 2588 PHE A CB    1 
ATOM   5032 C  CG    . PHE A 1 797 ? 119.905 81.916  104.579 1.00 50.55  ? 2588 PHE A CG    1 
ATOM   5033 C  CD1   . PHE A 1 797 ? 121.216 81.480  104.662 1.00 55.06  ? 2588 PHE A CD1   1 
ATOM   5034 C  CD2   . PHE A 1 797 ? 119.039 81.621  105.617 1.00 50.09  ? 2588 PHE A CD2   1 
ATOM   5035 C  CE1   . PHE A 1 797 ? 121.652 80.761  105.756 1.00 57.59  ? 2588 PHE A CE1   1 
ATOM   5036 C  CE2   . PHE A 1 797 ? 119.471 80.902  106.712 1.00 52.40  ? 2588 PHE A CE2   1 
ATOM   5037 C  CZ    . PHE A 1 797 ? 120.779 80.472  106.782 1.00 54.43  ? 2588 PHE A CZ    1 
ATOM   5038 N  N     . ASP A 1 798 ? 118.017 79.683  101.967 1.00 53.56  ? 2589 ASP A N     1 
ATOM   5039 C  CA    . ASP A 1 798 ? 116.943 78.707  102.092 1.00 54.73  ? 2589 ASP A CA    1 
ATOM   5040 C  C     . ASP A 1 798 ? 117.094 77.802  103.306 1.00 57.39  ? 2589 ASP A C     1 
ATOM   5041 O  O     . ASP A 1 798 ? 116.271 76.901  103.494 1.00 57.75  ? 2589 ASP A O     1 
ATOM   5042 C  CB    . ASP A 1 798 ? 116.859 77.854  100.822 1.00 52.94  ? 2589 ASP A CB    1 
ATOM   5043 C  CG    . ASP A 1 798 ? 116.472 78.663  99.600  1.00 52.48  ? 2589 ASP A CG    1 
ATOM   5044 O  OD1   . ASP A 1 798 ? 115.680 79.618  99.745  1.00 53.08  ? 2589 ASP A OD1   1 
ATOM   5045 O  OD2   . ASP A 1 798 ? 116.961 78.346  98.496  1.00 53.79  ? 2589 ASP A OD2   1 
ATOM   5046 N  N     . VAL A 1 799 ? 118.115 78.014  104.130 1.00 58.62  ? 2590 VAL A N     1 
ATOM   5047 C  CA    . VAL A 1 799 ? 118.324 77.187  105.312 1.00 61.89  ? 2590 VAL A CA    1 
ATOM   5048 C  C     . VAL A 1 799 ? 117.447 77.679  106.460 1.00 59.95  ? 2590 VAL A C     1 
ATOM   5049 O  O     . VAL A 1 799 ? 117.101 78.858  106.535 1.00 56.60  ? 2590 VAL A O     1 
ATOM   5050 C  CB    . VAL A 1 799 ? 119.808 77.172  105.721 1.00 61.84  ? 2590 VAL A CB    1 
ATOM   5051 C  CG1   . VAL A 1 799 ? 120.076 76.058  106.722 1.00 59.42  ? 2590 VAL A CG1   1 
ATOM   5052 C  CG2   . VAL A 1 799 ? 120.692 77.019  104.494 1.00 62.83  ? 2590 VAL A CG2   1 
ATOM   5053 O  OXT   . VAL A 1 799 ? 117.057 76.912  107.340 1.00 58.19  ? 2590 VAL A OXT   1 
ATOM   5054 O  "O3'" . DA  B 2 7   ? 92.333  109.882 83.260  1.00 102.03 ? 7    DA  E "O3'" 1 
ATOM   5055 P  P     . DG  B 2 8   ? 93.268  110.324 84.490  1.00 113.35 ? 8    DG  E P     1 
ATOM   5056 O  OP1   . DG  B 2 8   ? 92.634  111.494 85.136  1.00 105.36 ? 8    DG  E OP1   1 
ATOM   5057 O  OP2   . DG  B 2 8   ? 94.656  110.422 83.990  1.00 105.27 ? 8    DG  E OP2   1 
ATOM   5058 O  "O5'" . DG  B 2 8   ? 93.195  109.081 85.493  1.00 92.99  ? 8    DG  E "O5'" 1 
ATOM   5059 C  "C5'" . DG  B 2 8   ? 91.955  108.719 86.087  1.00 80.48  ? 8    DG  E "C5'" 1 
ATOM   5060 C  "C4'" . DG  B 2 8   ? 92.069  107.389 86.806  1.00 70.32  ? 8    DG  E "C4'" 1 
ATOM   5061 O  "O4'" . DG  B 2 8   ? 90.799  107.070 87.425  1.00 71.18  ? 8    DG  E "O4'" 1 
ATOM   5062 C  "C3'" . DG  B 2 8   ? 92.386  106.204 85.910  1.00 67.06  ? 8    DG  E "C3'" 1 
ATOM   5063 O  "O3'" . DG  B 2 8   ? 93.057  105.197 86.650  1.00 57.51  ? 8    DG  E "O3'" 1 
ATOM   5064 C  "C2'" . DG  B 2 8   ? 91.001  105.747 85.475  1.00 71.89  ? 8    DG  E "C2'" 1 
ATOM   5065 C  "C1'" . DG  B 2 8   ? 90.173  106.008 86.731  1.00 69.47  ? 8    DG  E "C1'" 1 
ATOM   5066 N  N9    . DG  B 2 8   ? 88.796  106.397 86.442  1.00 73.38  ? 8    DG  E N9    1 
ATOM   5067 C  C8    . DG  B 2 8   ? 88.356  107.628 86.021  1.00 75.40  ? 8    DG  E C8    1 
ATOM   5068 N  N7    . DG  B 2 8   ? 87.067  107.685 85.838  1.00 78.68  ? 8    DG  E N7    1 
ATOM   5069 C  C5    . DG  B 2 8   ? 86.622  106.408 86.158  1.00 80.25  ? 8    DG  E C5    1 
ATOM   5070 C  C6    . DG  B 2 8   ? 85.314  105.870 86.149  1.00 80.83  ? 8    DG  E C6    1 
ATOM   5071 O  O6    . DG  B 2 8   ? 84.254  106.434 85.847  1.00 79.31  ? 8    DG  E O6    1 
ATOM   5072 N  N1    . DG  B 2 8   ? 85.304  104.534 86.542  1.00 82.30  ? 8    DG  E N1    1 
ATOM   5073 C  C2    . DG  B 2 8   ? 86.418  103.811 86.898  1.00 82.35  ? 8    DG  E C2    1 
ATOM   5074 N  N2    . DG  B 2 8   ? 86.211  102.534 87.249  1.00 82.47  ? 8    DG  E N2    1 
ATOM   5075 N  N3    . DG  B 2 8   ? 87.650  104.304 86.911  1.00 80.50  ? 8    DG  E N3    1 
ATOM   5076 C  C4    . DG  B 2 8   ? 87.676  105.604 86.531  1.00 77.34  ? 8    DG  E C4    1 
ATOM   5077 P  P     . DC  B 2 9   ? 94.253  104.365 85.973  1.00 58.13  ? 9    DC  E P     1 
ATOM   5078 O  OP1   . DC  B 2 9   ? 95.394  105.285 85.786  1.00 64.00  ? 9    DC  E OP1   1 
ATOM   5079 O  OP2   . DC  B 2 9   ? 93.694  103.632 84.818  1.00 52.10  ? 9    DC  E OP2   1 
ATOM   5080 O  "O5'" . DC  B 2 9   ? 94.652  103.297 87.087  1.00 41.69  ? 9    DC  E "O5'" 1 
ATOM   5081 C  "C5'" . DC  B 2 9   ? 95.119  103.737 88.346  1.00 36.33  ? 9    DC  E "C5'" 1 
ATOM   5082 C  "C4'" . DC  B 2 9   ? 94.800  102.717 89.420  1.00 30.90  ? 9    DC  E "C4'" 1 
ATOM   5083 O  "O4'" . DC  B 2 9   ? 95.440  101.463 89.091  1.00 30.77  ? 9    DC  E "O4'" 1 
ATOM   5084 C  "C3'" . DC  B 2 9   ? 95.312  103.068 90.803  1.00 29.81  ? 9    DC  E "C3'" 1 
ATOM   5085 O  "O3'" . DC  B 2 9   ? 94.357  103.871 91.484  1.00 32.57  ? 9    DC  E "O3'" 1 
ATOM   5086 C  "C2'" . DC  B 2 9   ? 95.450  101.698 91.448  1.00 28.06  ? 9    DC  E "C2'" 1 
ATOM   5087 C  "C1'" . DC  B 2 9   ? 95.908  100.837 90.270  1.00 28.29  ? 9    DC  E "C1'" 1 
ATOM   5088 N  N1    . DC  B 2 9   ? 97.386  100.688 90.172  1.00 27.64  ? 9    DC  E N1    1 
ATOM   5089 C  C2    . DC  B 2 9   ? 98.061  99.900  91.103  1.00 25.29  ? 9    DC  E C2    1 
ATOM   5090 O  O2    . DC  B 2 9   ? 97.416  99.343  91.996  1.00 26.26  ? 9    DC  E O2    1 
ATOM   5091 N  N3    . DC  B 2 9   ? 99.404  99.767  91.002  1.00 21.58  ? 9    DC  E N3    1 
ATOM   5092 C  C4    . DC  B 2 9   ? 100.063 100.381 90.023  1.00 22.64  ? 9    DC  E C4    1 
ATOM   5093 N  N4    . DC  B 2 9   ? 101.387 100.222 89.965  1.00 23.74  ? 9    DC  E N4    1 
ATOM   5094 C  C5    . DC  B 2 9   ? 99.393  101.189 89.061  1.00 28.49  ? 9    DC  E C5    1 
ATOM   5095 C  C6    . DC  B 2 9   ? 98.067  101.310 89.170  1.00 30.47  ? 9    DC  E C6    1 
ATOM   5096 P  P     . DT  B 2 10  ? 94.843  105.119 92.370  1.00 44.05  ? 10   DT  E P     1 
ATOM   5097 O  OP1   . DT  B 2 10  ? 93.696  106.032 92.537  1.00 45.40  ? 10   DT  E OP1   1 
ATOM   5098 O  OP2   . DT  B 2 10  ? 96.109  105.623 91.794  1.00 37.70  ? 10   DT  E OP2   1 
ATOM   5099 O  "O5'" . DT  B 2 10  ? 95.185  104.473 93.786  1.00 31.34  ? 10   DT  E "O5'" 1 
ATOM   5100 C  "C5'" . DT  B 2 10  ? 94.170  103.835 94.537  1.00 28.11  ? 10   DT  E "C5'" 1 
ATOM   5101 C  "C4'" . DT  B 2 10  ? 94.778  103.049 95.678  1.00 27.29  ? 10   DT  E "C4'" 1 
ATOM   5102 O  "O4'" . DT  B 2 10  ? 95.667  102.051 95.137  1.00 23.07  ? 10   DT  E "O4'" 1 
ATOM   5103 C  "C3'" . DT  B 2 10  ? 95.642  103.868 96.618  1.00 28.20  ? 10   DT  E "C3'" 1 
ATOM   5104 O  "O3'" . DT  B 2 10  ? 94.842  104.439 97.644  1.00 31.85  ? 10   DT  E "O3'" 1 
ATOM   5105 C  "C2'" . DT  B 2 10  ? 96.597  102.825 97.180  1.00 26.01  ? 10   DT  E "C2'" 1 
ATOM   5106 C  "C1'" . DT  B 2 10  ? 96.754  101.847 96.017  1.00 22.11  ? 10   DT  E "C1'" 1 
ATOM   5107 N  N1    . DT  B 2 10  ? 98.021  102.006 95.260  1.00 22.58  ? 10   DT  E N1    1 
ATOM   5108 C  C2    . DT  B 2 10  ? 99.204  101.623 95.844  1.00 20.98  ? 10   DT  E C2    1 
ATOM   5109 O  O2    . DT  B 2 10  ? 99.278  101.177 96.973  1.00 21.03  ? 10   DT  E O2    1 
ATOM   5110 N  N3    . DT  B 2 10  ? 100.311 101.805 95.063  1.00 19.85  ? 10   DT  E N3    1 
ATOM   5111 C  C4    . DT  B 2 10  ? 100.352 102.307 93.779  1.00 22.07  ? 10   DT  E C4    1 
ATOM   5112 O  O4    . DT  B 2 10  ? 101.400 102.427 93.155  1.00 22.03  ? 10   DT  E O4    1 
ATOM   5113 C  C5    . DT  B 2 10  ? 99.076  102.678 93.222  1.00 23.48  ? 10   DT  E C5    1 
ATOM   5114 C  C7    . DT  B 2 10  ? 98.994  103.237 91.837  1.00 24.21  ? 10   DT  E C7    1 
ATOM   5115 C  C6    . DT  B 2 10  ? 97.985  102.509 93.980  1.00 24.58  ? 10   DT  E C6    1 
ATOM   5116 P  P     . DC  B 2 11  ? 95.328  105.771 98.398  1.00 32.10  ? 11   DC  E P     1 
ATOM   5117 O  OP1   . DC  B 2 11  ? 94.253  106.170 99.330  1.00 29.90  ? 11   DC  E OP1   1 
ATOM   5118 O  OP2   . DC  B 2 11  ? 95.809  106.724 97.375  1.00 30.91  ? 11   DC  E OP2   1 
ATOM   5119 O  "O5'" . DC  B 2 11  ? 96.593  105.296 99.251  1.00 27.58  ? 11   DC  E "O5'" 1 
ATOM   5120 C  "C5'" . DC  B 2 11  ? 96.410  104.467 100.387 1.00 28.16  ? 11   DC  E "C5'" 1 
ATOM   5121 C  "C4'" . DC  B 2 11  ? 97.733  104.207 101.083 1.00 24.79  ? 11   DC  E "C4'" 1 
ATOM   5122 O  "O4'" . DC  B 2 11  ? 98.523  103.296 100.290 1.00 21.47  ? 11   DC  E "O4'" 1 
ATOM   5123 C  "C3'" . DC  B 2 11  ? 98.613  105.428 101.257 1.00 25.09  ? 11   DC  E "C3'" 1 
ATOM   5124 O  "O3'" . DC  B 2 11  ? 98.263  106.114 102.448 1.00 26.73  ? 11   DC  E "O3'" 1 
ATOM   5125 C  "C2'" . DC  B 2 11  ? 100.000 104.809 101.361 1.00 23.15  ? 11   DC  E "C2'" 1 
ATOM   5126 C  "C1'" . DC  B 2 11  ? 99.897  103.616 100.417 1.00 21.21  ? 11   DC  E "C1'" 1 
ATOM   5127 N  N1    . DC  B 2 11  ? 100.447 103.873 99.062  1.00 22.17  ? 11   DC  E N1    1 
ATOM   5128 C  C2    . DC  B 2 11  ? 101.818 103.738 98.835  1.00 21.86  ? 11   DC  E C2    1 
ATOM   5129 O  O2    . DC  B 2 11  ? 102.553 103.417 99.776  1.00 20.99  ? 11   DC  E O2    1 
ATOM   5130 N  N3    . DC  B 2 11  ? 102.301 103.968 97.589  1.00 20.21  ? 11   DC  E N3    1 
ATOM   5131 C  C4    . DC  B 2 11  ? 101.468 104.312 96.606  1.00 20.95  ? 11   DC  E C4    1 
ATOM   5132 N  N4    . DC  B 2 11  ? 101.982 104.530 95.394  1.00 23.50  ? 11   DC  E N4    1 
ATOM   5133 C  C5    . DC  B 2 11  ? 100.070 104.454 96.823  1.00 22.49  ? 11   DC  E C5    1 
ATOM   5134 C  C6    . DC  B 2 11  ? 99.608  104.220 98.051  1.00 23.47  ? 11   DC  E C6    1 
ATOM   5135 P  P     . DT  B 2 12  ? 98.584  107.680 102.598 1.00 39.09  ? 12   DT  E P     1 
ATOM   5136 O  OP1   . DT  B 2 12  ? 97.986  108.141 103.869 1.00 29.25  ? 12   DT  E OP1   1 
ATOM   5137 O  OP2   . DT  B 2 12  ? 98.212  108.340 101.328 1.00 37.14  ? 12   DT  E OP2   1 
ATOM   5138 O  "O5'" . DT  B 2 12  ? 100.174 107.730 102.734 1.00 32.63  ? 12   DT  E "O5'" 1 
ATOM   5139 C  "C5'" . DT  B 2 12  ? 100.805 107.123 103.848 1.00 27.76  ? 12   DT  E "C5'" 1 
ATOM   5140 C  "C4'" . DT  B 2 12  ? 102.304 107.031 103.637 1.00 27.62  ? 12   DT  E "C4'" 1 
ATOM   5141 O  "O4'" . DT  B 2 12  ? 102.583 106.251 102.457 1.00 24.84  ? 12   DT  E "O4'" 1 
ATOM   5142 C  "C3'" . DT  B 2 12  ? 102.997 108.352 103.387 1.00 27.23  ? 12   DT  E "C3'" 1 
ATOM   5143 O  "O3'" . DT  B 2 12  ? 103.299 108.976 104.622 1.00 30.44  ? 12   DT  E "O3'" 1 
ATOM   5144 C  "C2'" . DT  B 2 12  ? 104.265 107.914 102.662 1.00 26.51  ? 12   DT  E "C2'" 1 
ATOM   5145 C  "C1'" . DT  B 2 12  ? 103.801 106.686 101.880 1.00 23.13  ? 12   DT  E "C1'" 1 
ATOM   5146 N  N1    . DT  B 2 12  ? 103.580 106.942 100.429 1.00 20.64  ? 12   DT  E N1    1 
ATOM   5147 C  C2    . DT  B 2 12  ? 104.657 106.965 99.579  1.00 21.17  ? 12   DT  E C2    1 
ATOM   5148 O  O2    . DT  B 2 12  ? 105.804 106.800 99.951  1.00 20.29  ? 12   DT  E O2    1 
ATOM   5149 N  N3    . DT  B 2 12  ? 104.344 107.195 98.267  1.00 23.50  ? 12   DT  E N3    1 
ATOM   5150 C  C4    . DT  B 2 12  ? 103.088 107.395 97.731  1.00 24.65  ? 12   DT  E C4    1 
ATOM   5151 O  O4    . DT  B 2 12  ? 102.909 107.594 96.535  1.00 28.83  ? 12   DT  E O4    1 
ATOM   5152 C  C5    . DT  B 2 12  ? 102.002 107.355 98.676  1.00 22.66  ? 12   DT  E C5    1 
ATOM   5153 C  C7    . DT  B 2 12  ? 100.592 107.561 98.213  1.00 23.63  ? 12   DT  E C7    1 
ATOM   5154 C  C6    . DT  B 2 12  ? 102.297 107.131 99.964  1.00 22.89  ? 12   DT  E C6    1 
ATOM   5155 P  P     . DA  B 2 13  ? 103.591 110.553 104.678 1.00 42.86  ? 13   DA  E P     1 
ATOM   5156 O  OP1   . DA  B 2 13  ? 103.484 110.981 106.090 1.00 44.60  ? 13   DA  E OP1   1 
ATOM   5157 O  OP2   . DA  B 2 13  ? 102.751 111.194 103.642 1.00 38.83  ? 13   DA  E OP2   1 
ATOM   5158 O  "O5'" . DA  B 2 13  ? 105.115 110.674 104.220 1.00 38.02  ? 13   DA  E "O5'" 1 
ATOM   5159 C  "C5'" . DA  B 2 13  ? 106.111 109.898 104.866 1.00 31.97  ? 13   DA  E "C5'" 1 
ATOM   5160 C  "C4'" . DA  B 2 13  ? 107.400 109.904 104.066 1.00 36.67  ? 13   DA  E "C4'" 1 
ATOM   5161 O  "O4'" . DA  B 2 13  ? 107.134 109.443 102.716 1.00 36.65  ? 13   DA  E "O4'" 1 
ATOM   5162 C  "C3'" . DA  B 2 13  ? 108.064 111.270 103.931 1.00 35.42  ? 13   DA  E "C3'" 1 
ATOM   5163 O  "O3'" . DA  B 2 13  ? 109.464 111.143 104.091 1.00 37.50  ? 13   DA  E "O3'" 1 
ATOM   5164 C  "C2'" . DA  B 2 13  ? 107.694 111.711 102.517 1.00 32.95  ? 13   DA  E "C2'" 1 
ATOM   5165 C  "C1'" . DA  B 2 13  ? 107.604 110.385 101.778 1.00 30.40  ? 13   DA  E "C1'" 1 
ATOM   5166 N  N9    . DA  B 2 13  ? 106.670 110.413 100.656 1.00 27.63  ? 13   DA  E N9    1 
ATOM   5167 C  C8    . DA  B 2 13  ? 105.308 110.385 100.727 1.00 29.77  ? 13   DA  E C8    1 
ATOM   5168 N  N7    . DA  B 2 13  ? 104.715 110.415 99.562  1.00 30.58  ? 13   DA  E N7    1 
ATOM   5169 C  C5    . DA  B 2 13  ? 105.759 110.471 98.659  1.00 29.81  ? 13   DA  E C5    1 
ATOM   5170 C  C6    . DA  B 2 13  ? 105.789 110.525 97.256  1.00 34.40  ? 13   DA  E C6    1 
ATOM   5171 N  N6    . DA  B 2 13  ? 104.689 110.531 96.500  1.00 37.24  ? 13   DA  E N6    1 
ATOM   5172 N  N1    . DA  B 2 13  ? 106.996 110.573 96.658  1.00 35.61  ? 13   DA  E N1    1 
ATOM   5173 C  C2    . DA  B 2 13  ? 108.094 110.565 97.422  1.00 34.54  ? 13   DA  E C2    1 
ATOM   5174 N  N3    . DA  B 2 13  ? 108.190 110.516 98.751  1.00 33.46  ? 13   DA  E N3    1 
ATOM   5175 C  C4    . DA  B 2 13  ? 106.973 110.470 99.314  1.00 29.95  ? 13   DA  E C4    1 
ATOM   5176 P  P     . DC  B 2 14  ? 110.350 112.428 104.462 1.00 39.78  ? 14   DC  E P     1 
ATOM   5177 O  OP1   . DC  B 2 14  ? 111.647 111.954 104.985 1.00 39.03  ? 14   DC  E OP1   1 
ATOM   5178 O  OP2   . DC  B 2 14  ? 109.512 113.349 105.259 1.00 37.28  ? 14   DC  E OP2   1 
ATOM   5179 O  "O5'" . DC  B 2 14  ? 110.619 113.114 103.053 1.00 44.95  ? 14   DC  E "O5'" 1 
ATOM   5180 C  "C5'" . DC  B 2 14  ? 111.303 112.397 102.040 1.00 44.72  ? 14   DC  E "C5'" 1 
ATOM   5181 C  "C4'" . DC  B 2 14  ? 111.508 113.280 100.832 1.00 45.06  ? 14   DC  E "C4'" 1 
ATOM   5182 O  "O4'" . DC  B 2 14  ? 110.418 113.080 99.893  1.00 43.21  ? 14   DC  E "O4'" 1 
ATOM   5183 C  "C3'" . DC  B 2 14  ? 111.525 114.777 101.148 1.00 49.58  ? 14   DC  E "C3'" 1 
ATOM   5184 O  "O3'" . DC  B 2 14  ? 112.550 115.418 100.411 1.00 59.73  ? 14   DC  E "O3'" 1 
ATOM   5185 C  "C2'" . DC  B 2 14  ? 110.143 115.235 100.697 1.00 45.40  ? 14   DC  E "C2'" 1 
ATOM   5186 C  "C1'" . DC  B 2 14  ? 109.932 114.335 99.497  1.00 43.26  ? 14   DC  E "C1'" 1 
ATOM   5187 N  N1    . DC  B 2 14  ? 108.510 114.210 99.084  1.00 41.39  ? 14   DC  E N1    1 
ATOM   5188 C  C2    . DC  B 2 14  ? 108.193 114.202 97.726  1.00 48.80  ? 14   DC  E C2    1 
ATOM   5189 O  O2    . DC  B 2 14  ? 109.108 114.278 96.898  1.00 54.47  ? 14   DC  E O2    1 
ATOM   5190 N  N3    . DC  B 2 14  ? 106.894 114.100 97.353  1.00 48.97  ? 14   DC  E N3    1 
ATOM   5191 C  C4    . DC  B 2 14  ? 105.941 114.020 98.282  1.00 45.66  ? 14   DC  E C4    1 
ATOM   5192 N  N4    . DC  B 2 14  ? 104.673 113.923 97.870  1.00 47.37  ? 14   DC  E N4    1 
ATOM   5193 C  C5    . DC  B 2 14  ? 106.245 114.034 99.674  1.00 39.95  ? 14   DC  E C5    1 
ATOM   5194 C  C6    . DC  B 2 14  ? 107.531 114.135 100.026 1.00 39.85  ? 14   DC  E C6    1 
ATOM   5195 P  P     . DG  B 2 15  ? 113.349 116.658 101.048 1.00 62.16  ? 15   DG  E P     1 
ATOM   5196 O  OP1   . DG  B 2 15  ? 114.445 116.111 101.878 1.00 62.09  ? 15   DG  E OP1   1 
ATOM   5197 O  OP2   . DG  B 2 15  ? 112.356 117.574 101.651 1.00 54.13  ? 15   DG  E OP2   1 
ATOM   5198 O  "O5'" . DG  B 2 15  ? 113.980 117.389 99.778  1.00 60.19  ? 15   DG  E "O5'" 1 
ATOM   5199 C  "C5'" . DG  B 2 15  ? 114.694 116.634 98.814  1.00 58.05  ? 15   DG  E "C5'" 1 
ATOM   5200 C  "C4'" . DG  B 2 15  ? 114.333 117.077 97.409  1.00 62.16  ? 15   DG  E "C4'" 1 
ATOM   5201 O  "O4'" . DG  B 2 15  ? 112.974 116.664 97.101  1.00 60.23  ? 15   DG  E "O4'" 1 
ATOM   5202 C  "C3'" . DG  B 2 15  ? 114.388 118.585 97.176  1.00 73.20  ? 15   DG  E "C3'" 1 
ATOM   5203 O  "O3'" . DG  B 2 15  ? 114.993 118.860 95.923  1.00 80.53  ? 15   DG  E "O3'" 1 
ATOM   5204 C  "C2'" . DG  B 2 15  ? 112.919 118.995 97.192  1.00 74.97  ? 15   DG  E "C2'" 1 
ATOM   5205 C  "C1'" . DG  B 2 15  ? 112.241 117.763 96.612  1.00 69.56  ? 15   DG  E "C1'" 1 
ATOM   5206 N  N9    . DG  B 2 15  ? 110.852 117.620 97.041  1.00 65.86  ? 15   DG  E N9    1 
ATOM   5207 C  C8    . DG  B 2 15  ? 110.399 117.562 98.332  1.00 63.38  ? 15   DG  E C8    1 
ATOM   5208 N  N7    . DG  B 2 15  ? 109.107 117.438 98.427  1.00 62.86  ? 15   DG  E N7    1 
ATOM   5209 C  C5    . DG  B 2 15  ? 108.668 117.419 97.112  1.00 68.29  ? 15   DG  E C5    1 
ATOM   5210 C  C6    . DG  B 2 15  ? 107.358 117.304 96.596  1.00 72.13  ? 15   DG  E C6    1 
ATOM   5211 O  O6    . DG  B 2 15  ? 106.297 117.197 97.224  1.00 71.34  ? 15   DG  E O6    1 
ATOM   5212 N  N1    . DG  B 2 15  ? 107.347 117.326 95.205  1.00 76.77  ? 15   DG  E N1    1 
ATOM   5213 C  C2    . DG  B 2 15  ? 108.464 117.443 94.414  1.00 76.12  ? 15   DG  E C2    1 
ATOM   5214 N  N2    . DG  B 2 15  ? 108.255 117.448 93.088  1.00 77.67  ? 15   DG  E N2    1 
ATOM   5215 N  N3    . DG  B 2 15  ? 109.703 117.551 94.887  1.00 73.92  ? 15   DG  E N3    1 
ATOM   5216 C  C4    . DG  B 2 15  ? 109.729 117.531 96.242  1.00 69.85  ? 15   DG  E C4    1 
ATOM   5217 P  P     . DG  B 2 16  ? 115.584 120.321 95.613  1.00 86.98  ? 16   DG  E P     1 
ATOM   5218 O  OP1   . DG  B 2 16  ? 116.998 120.151 95.211  1.00 80.66  ? 16   DG  E OP1   1 
ATOM   5219 O  OP2   . DG  B 2 16  ? 115.247 121.203 96.752  1.00 83.58  ? 16   DG  E OP2   1 
ATOM   5220 O  "O5'" . DG  B 2 16  ? 114.743 120.807 94.344  1.00 89.64  ? 16   DG  E "O5'" 1 
ATOM   5221 C  "C5'" . DG  B 2 16  ? 114.826 120.083 93.127  1.00 91.61  ? 16   DG  E "C5'" 1 
ATOM   5222 C  "C4'" . DG  B 2 16  ? 113.602 120.323 92.263  1.00 101.38 ? 16   DG  E "C4'" 1 
ATOM   5223 O  "O4'" . DG  B 2 16  ? 112.413 119.874 92.962  1.00 94.39  ? 16   DG  E "O4'" 1 
ATOM   5224 C  "C3'" . DG  B 2 16  ? 113.349 121.784 91.878  1.00 106.83 ? 16   DG  E "C3'" 1 
ATOM   5225 O  "O3'" . DG  B 2 16  ? 113.085 121.872 90.482  1.00 112.18 ? 16   DG  E "O3'" 1 
ATOM   5226 C  "C2'" . DG  B 2 16  ? 112.125 122.169 92.712  1.00 103.25 ? 16   DG  E "C2'" 1 
ATOM   5227 C  "C1'" . DG  B 2 16  ? 111.401 120.840 92.824  1.00 98.41  ? 16   DG  E "C1'" 1 
ATOM   5228 N  N9    . DG  B 2 16  ? 110.523 120.750 93.985  1.00 93.21  ? 16   DG  E N9    1 
ATOM   5229 C  C8    . DG  B 2 16  ? 110.899 120.759 95.303  1.00 87.28  ? 16   DG  E C8    1 
ATOM   5230 N  N7    . DG  B 2 16  ? 109.898 120.657 96.131  1.00 86.76  ? 16   DG  E N7    1 
ATOM   5231 C  C5    . DG  B 2 16  ? 108.784 120.579 95.308  1.00 93.00  ? 16   DG  E C5    1 
ATOM   5232 C  C6    . DG  B 2 16  ? 107.416 120.457 95.640  1.00 95.87  ? 16   DG  E C6    1 
ATOM   5233 O  O6    . DG  B 2 16  ? 106.905 120.394 96.765  1.00 93.57  ? 16   DG  E O6    1 
ATOM   5234 N  N1    . DG  B 2 16  ? 106.612 120.410 94.504  1.00 100.37 ? 16   DG  E N1    1 
ATOM   5235 C  C2    . DG  B 2 16  ? 107.075 120.468 93.212  1.00 103.71 ? 16   DG  E C2    1 
ATOM   5236 N  N2    . DG  B 2 16  ? 106.149 120.412 92.244  1.00 105.04 ? 16   DG  E N2    1 
ATOM   5237 N  N3    . DG  B 2 16  ? 108.356 120.586 92.887  1.00 104.33 ? 16   DG  E N3    1 
ATOM   5238 C  C4    . DG  B 2 16  ? 109.151 120.632 93.983  1.00 98.14  ? 16   DG  E C4    1 
ATOM   5239 P  P     . DA  B 2 17  ? 112.821 123.296 89.786  1.00 123.71 ? 17   DA  E P     1 
ATOM   5240 O  OP1   . DA  B 2 17  ? 113.458 123.260 88.452  1.00 118.48 ? 17   DA  E OP1   1 
ATOM   5241 O  OP2   . DA  B 2 17  ? 113.198 124.360 90.742  1.00 120.38 ? 17   DA  E OP2   1 
ATOM   5242 O  "O5'" . DA  B 2 17  ? 111.233 123.335 89.593  1.00 124.75 ? 17   DA  E "O5'" 1 
ATOM   5243 C  "C5'" . DA  B 2 17  ? 110.575 122.282 88.890  1.00 123.80 ? 17   DA  E "C5'" 1 
ATOM   5244 C  "C4'" . DA  B 2 17  ? 109.132 122.648 88.573  1.00 131.47 ? 17   DA  E "C4'" 1 
ATOM   5245 O  "O4'" . DA  B 2 17  ? 108.297 122.407 89.734  1.00 125.43 ? 17   DA  E "O4'" 1 
ATOM   5246 C  "C3'" . DA  B 2 17  ? 108.902 124.101 88.183  1.00 137.95 ? 17   DA  E "C3'" 1 
ATOM   5247 O  "O3'" . DA  B 2 17  ? 107.863 124.188 87.215  1.00 144.56 ? 17   DA  E "O3'" 1 
ATOM   5248 C  "C2'" . DA  B 2 17  ? 108.495 124.748 89.503  1.00 133.84 ? 17   DA  E "C2'" 1 
ATOM   5249 C  "C1'" . DA  B 2 17  ? 107.740 123.621 90.201  1.00 129.10 ? 17   DA  E "C1'" 1 
ATOM   5250 N  N9    . DA  B 2 17  ? 107.871 123.643 91.656  1.00 123.55 ? 17   DA  E N9    1 
ATOM   5251 C  C8    . DA  B 2 17  ? 109.032 123.728 92.371  1.00 118.13 ? 17   DA  E C8    1 
ATOM   5252 N  N7    . DA  B 2 17  ? 108.858 123.717 93.670  1.00 116.99 ? 17   DA  E N7    1 
ATOM   5253 C  C5    . DA  B 2 17  ? 107.487 123.607 93.822  1.00 118.22 ? 17   DA  E C5    1 
ATOM   5254 C  C6    . DA  B 2 17  ? 106.664 123.540 94.963  1.00 120.08 ? 17   DA  E C6    1 
ATOM   5255 N  N6    . DA  B 2 17  ? 107.139 123.577 96.211  1.00 119.34 ? 17   DA  E N6    1 
ATOM   5256 N  N1    . DA  B 2 17  ? 105.332 123.431 94.771  1.00 122.34 ? 17   DA  E N1    1 
ATOM   5257 C  C2    . DA  B 2 17  ? 104.863 123.393 93.517  1.00 123.24 ? 17   DA  E C2    1 
ATOM   5258 N  N3    . DA  B 2 17  ? 105.539 123.449 92.366  1.00 123.95 ? 17   DA  E N3    1 
ATOM   5259 C  C4    . DA  B 2 17  ? 106.859 123.558 92.591  1.00 122.55 ? 17   DA  E C4    1 
ATOM   5260 P  P     . DT  B 2 18  ? 108.001 125.200 85.974  1.00 156.89 ? 18   DT  E P     1 
ATOM   5261 O  OP1   . DT  B 2 18  ? 107.921 124.399 84.733  1.00 146.73 ? 18   DT  E OP1   1 
ATOM   5262 O  OP2   . DT  B 2 18  ? 109.182 126.056 86.222  1.00 149.91 ? 18   DT  E OP2   1 
ATOM   5263 O  "O5'" . DT  B 2 18  ? 106.697 126.120 86.081  1.00 151.70 ? 18   DT  E "O5'" 1 
ATOM   5264 C  "C5'" . DT  B 2 18  ? 106.323 126.681 87.334  1.00 148.92 ? 18   DT  E "C5'" 1 
ATOM   5265 C  "C4'" . DT  B 2 18  ? 104.947 126.195 87.751  1.00 150.23 ? 18   DT  E "C4'" 1 
ATOM   5266 O  "O4'" . DT  B 2 18  ? 105.007 125.666 89.103  1.00 146.27 ? 18   DT  E "O4'" 1 
ATOM   5267 C  "C3'" . DT  B 2 18  ? 103.878 127.272 87.806  1.00 156.00 ? 18   DT  E "C3'" 1 
ATOM   5268 O  "O3'" . DT  B 2 18  ? 102.599 126.663 87.677  1.00 158.49 ? 18   DT  E "O3'" 1 
ATOM   5269 C  "C2'" . DT  B 2 18  ? 104.088 127.817 89.211  1.00 155.18 ? 18   DT  E "C2'" 1 
ATOM   5270 C  "C1'" . DT  B 2 18  ? 104.275 126.514 89.973  1.00 148.90 ? 18   DT  E "C1'" 1 
ATOM   5271 N  N1    . DT  B 2 18  ? 105.031 126.634 91.258  1.00 143.69 ? 18   DT  E N1    1 
ATOM   5272 C  C2    . DT  B 2 18  ? 104.351 126.555 92.453  1.00 144.10 ? 18   DT  E C2    1 
ATOM   5273 O  O2    . DT  B 2 18  ? 103.142 126.429 92.528  1.00 146.34 ? 18   DT  E O2    1 
ATOM   5274 N  N3    . DT  B 2 18  ? 105.144 126.652 93.568  1.00 142.58 ? 18   DT  E N3    1 
ATOM   5275 C  C4    . DT  B 2 18  ? 106.519 126.800 93.605  1.00 138.85 ? 18   DT  E C4    1 
ATOM   5276 O  O4    . DT  B 2 18  ? 107.145 126.876 94.657  1.00 137.98 ? 18   DT  E O4    1 
ATOM   5277 C  C5    . DT  B 2 18  ? 107.167 126.861 92.320  1.00 136.68 ? 18   DT  E C5    1 
ATOM   5278 C  C7    . DT  B 2 18  ? 108.656 127.025 92.237  1.00 129.24 ? 18   DT  E C7    1 
ATOM   5279 C  C6    . DT  B 2 18  ? 106.402 126.773 91.222  1.00 139.51 ? 18   DT  E C6    1 
ATOM   5280 P  P     . DG  B 2 19  ? 101.303 127.542 87.319  1.00 165.37 ? 19   DG  E P     1 
ATOM   5281 O  OP1   . DG  B 2 19  ? 100.851 127.128 85.972  1.00 158.98 ? 19   DG  E OP1   1 
ATOM   5282 O  OP2   . DG  B 2 19  ? 101.621 128.963 87.577  1.00 164.21 ? 19   DG  E OP2   1 
ATOM   5283 O  "O5'" . DG  B 2 19  ? 100.213 127.065 88.391  1.00 164.86 ? 19   DG  E "O5'" 1 
ATOM   5284 C  "C5'" . DG  B 2 19  ? 100.539 127.042 89.781  1.00 162.69 ? 19   DG  E "C5'" 1 
ATOM   5285 C  "C4'" . DG  B 2 19  ? 99.596  127.932 90.568  1.00 166.30 ? 19   DG  E "C4'" 1 
ATOM   5286 O  "O4'" . DG  B 2 19  ? 100.175 128.218 91.869  1.00 165.25 ? 19   DG  E "O4'" 1 
ATOM   5287 C  "C3'" . DG  B 2 19  ? 99.362  129.297 89.954  1.00 170.41 ? 19   DG  E "C3'" 1 
ATOM   5288 O  "O3'" . DG  B 2 19  ? 98.173  129.864 90.491  1.00 173.79 ? 19   DG  E "O3'" 1 
ATOM   5289 C  "C2'" . DG  B 2 19  ? 100.594 130.040 90.446  1.00 167.67 ? 19   DG  E "C2'" 1 
ATOM   5290 C  "C1'" . DG  B 2 19  ? 100.649 129.556 91.891  1.00 166.11 ? 19   DG  E "C1'" 1 
ATOM   5291 N  N9    . DG  B 2 19  ? 101.990 129.553 92.465  1.00 162.03 ? 19   DG  E N9    1 
ATOM   5292 C  C8    . DG  B 2 19  ? 103.181 129.567 91.785  1.00 157.91 ? 19   DG  E C8    1 
ATOM   5293 N  N7    . DG  B 2 19  ? 104.226 129.545 92.564  1.00 155.62 ? 19   DG  E N7    1 
ATOM   5294 C  C5    . DG  B 2 19  ? 103.693 129.512 93.845  1.00 157.07 ? 19   DG  E C5    1 
ATOM   5295 C  C6    . DG  B 2 19  ? 104.342 129.479 95.100  1.00 155.62 ? 19   DG  E C6    1 
ATOM   5296 O  O6    . DG  B 2 19  ? 105.558 129.470 95.336  1.00 153.37 ? 19   DG  E O6    1 
ATOM   5297 N  N1    . DG  B 2 19  ? 103.428 129.456 96.150  1.00 156.60 ? 19   DG  E N1    1 
ATOM   5298 C  C2    . DG  B 2 19  ? 102.061 129.466 96.004  1.00 157.15 ? 19   DG  E C2    1 
ATOM   5299 N  N2    . DG  B 2 19  ? 101.342 129.438 97.135  1.00 154.94 ? 19   DG  E N2    1 
ATOM   5300 N  N3    . DG  B 2 19  ? 101.441 129.494 94.833  1.00 159.03 ? 19   DG  E N3    1 
ATOM   5301 C  C4    . DG  B 2 19  ? 102.317 129.517 93.801  1.00 159.99 ? 19   DG  E C4    1 
ATOM   5302 P  P     . DC  B 2 20  ? 96.764  129.666 89.744  1.00 178.04 ? 20   DC  E P     1 
ATOM   5303 O  OP1   . DC  B 2 20  ? 96.707  128.282 89.223  1.00 172.51 ? 20   DC  E OP1   1 
ATOM   5304 O  OP2   . DC  B 2 20  ? 96.589  130.806 88.819  1.00 174.27 ? 20   DC  E OP2   1 
ATOM   5305 O  "O5'" . DC  B 2 20  ? 95.685  129.818 90.918  1.00 179.70 ? 20   DC  E "O5'" 1 
ATOM   5306 C  "C5'" . DC  B 2 20  ? 94.777  130.913 90.909  1.00 179.20 ? 20   DC  E "C5'" 1 
ATOM   5307 C  "C4'" . DC  B 2 20  ? 94.434  131.349 92.323  1.00 179.57 ? 20   DC  E "C4'" 1 
ATOM   5308 O  "O4'" . DC  B 2 20  ? 95.647  131.421 93.110  1.00 177.74 ? 20   DC  E "O4'" 1 
ATOM   5309 C  "C3'" . DC  B 2 20  ? 93.845  132.739 92.427  1.00 182.94 ? 20   DC  E "C3'" 1 
ATOM   5310 O  "O3'" . DC  B 2 20  ? 93.195  132.893 93.685  1.00 186.30 ? 20   DC  E "O3'" 1 
ATOM   5311 C  "C2'" . DC  B 2 20  ? 95.103  133.589 92.347  1.00 180.85 ? 20   DC  E "C2'" 1 
ATOM   5312 C  "C1'" . DC  B 2 20  ? 96.068  132.774 93.211  1.00 179.15 ? 20   DC  E "C1'" 1 
ATOM   5313 N  N1    . DC  B 2 20  ? 97.484  132.847 92.761  1.00 178.51 ? 20   DC  E N1    1 
ATOM   5314 C  C2    . DC  B 2 20  ? 98.519  132.805 93.705  1.00 176.75 ? 20   DC  E C2    1 
ATOM   5315 O  O2    . DC  B 2 20  ? 98.241  132.727 94.909  1.00 175.56 ? 20   DC  E O2    1 
ATOM   5316 N  N3    . DC  B 2 20  ? 99.805  132.861 93.273  1.00 174.89 ? 20   DC  E N3    1 
ATOM   5317 C  C4    . DC  B 2 20  ? 100.065 132.951 91.968  1.00 172.50 ? 20   DC  E C4    1 
ATOM   5318 N  N4    . DC  B 2 20  ? 101.346 133.000 91.587  1.00 168.95 ? 20   DC  E N4    1 
ATOM   5319 C  C5    . DC  B 2 20  ? 99.024  132.990 90.994  1.00 174.49 ? 20   DC  E C5    1 
ATOM   5320 C  C6    . DC  B 2 20  ? 97.764  132.933 91.430  1.00 177.43 ? 20   DC  E C6    1 
ATOM   5321 P  P     . DG  C 3 10  ? 108.805 135.327 100.124 1.00 176.15 ? 10   DG  F P     1 
ATOM   5322 O  OP1   . DG  C 3 10  ? 109.161 136.656 100.671 1.00 172.94 ? 10   DG  F OP1   1 
ATOM   5323 O  OP2   . DG  C 3 10  ? 109.122 134.135 100.940 1.00 172.44 ? 10   DG  F OP2   1 
ATOM   5324 O  "O5'" . DG  C 3 10  ? 107.241 135.259 99.788  1.00 172.45 ? 10   DG  F "O5'" 1 
ATOM   5325 C  "C5'" . DG  C 3 10  ? 106.278 135.593 100.784 1.00 169.79 ? 10   DG  F "C5'" 1 
ATOM   5326 C  "C4'" . DG  C 3 10  ? 105.383 134.405 101.099 1.00 167.51 ? 10   DG  F "C4'" 1 
ATOM   5327 O  "O4'" . DG  C 3 10  ? 104.503 134.145 99.975  1.00 166.29 ? 10   DG  F "O4'" 1 
ATOM   5328 C  "C3'" . DG  C 3 10  ? 106.121 133.101 101.385 1.00 166.90 ? 10   DG  F "C3'" 1 
ATOM   5329 O  "O3'" . DG  C 3 10  ? 105.524 132.424 102.485 1.00 166.92 ? 10   DG  F "O3'" 1 
ATOM   5330 C  "C2'" . DG  C 3 10  ? 105.982 132.313 100.084 1.00 165.29 ? 10   DG  F "C2'" 1 
ATOM   5331 C  "C1'" . DG  C 3 10  ? 104.659 132.817 99.520  1.00 165.62 ? 10   DG  F "C1'" 1 
ATOM   5332 N  N9    . DG  C 3 10  ? 104.634 132.836 98.061  1.00 166.75 ? 10   DG  F N9    1 
ATOM   5333 C  C8    . DG  C 3 10  ? 105.709 132.688 97.220  1.00 166.96 ? 10   DG  F C8    1 
ATOM   5334 N  N7    . DG  C 3 10  ? 105.397 132.756 95.958  1.00 167.08 ? 10   DG  F N7    1 
ATOM   5335 C  C5    . DG  C 3 10  ? 104.026 132.967 95.956  1.00 168.60 ? 10   DG  F C5    1 
ATOM   5336 C  C6    . DG  C 3 10  ? 103.132 133.121 94.872  1.00 169.31 ? 10   DG  F C6    1 
ATOM   5337 O  O6    . DG  C 3 10  ? 103.388 133.102 93.660  1.00 167.70 ? 10   DG  F O6    1 
ATOM   5338 N  N1    . DG  C 3 10  ? 101.823 133.313 95.305  1.00 171.31 ? 10   DG  F N1    1 
ATOM   5339 C  C2    . DG  C 3 10  ? 101.431 133.355 96.621  1.00 169.69 ? 10   DG  F C2    1 
ATOM   5340 N  N2    . DG  C 3 10  ? 100.122 133.544 96.837  1.00 170.08 ? 10   DG  F N2    1 
ATOM   5341 N  N3    . DG  C 3 10  ? 102.258 133.209 97.651  1.00 167.61 ? 10   DG  F N3    1 
ATOM   5342 C  C4    . DG  C 3 10  ? 103.537 133.020 97.244  1.00 167.95 ? 10   DG  F C4    1 
ATOM   5343 P  P     . DC  C 3 11  ? 106.417 132.029 103.762 1.00 171.82 ? 11   DC  F P     1 
ATOM   5344 O  OP1   . DC  C 3 11  ? 107.188 133.230 104.153 1.00 169.00 ? 11   DC  F OP1   1 
ATOM   5345 O  OP2   . DC  C 3 11  ? 107.128 130.773 103.438 1.00 168.32 ? 11   DC  F OP2   1 
ATOM   5346 O  "O5'" . DC  C 3 11  ? 105.349 131.706 104.909 1.00 166.81 ? 11   DC  F "O5'" 1 
ATOM   5347 C  "C5'" . DC  C 3 11  ? 104.788 130.400 105.019 1.00 163.04 ? 11   DC  F "C5'" 1 
ATOM   5348 C  "C4'" . DC  C 3 11  ? 103.404 130.353 104.398 1.00 160.63 ? 11   DC  F "C4'" 1 
ATOM   5349 O  "O4'" . DC  C 3 11  ? 103.505 130.628 102.976 1.00 161.63 ? 11   DC  F "O4'" 1 
ATOM   5350 C  "C3'" . DC  C 3 11  ? 102.701 129.007 104.494 1.00 158.66 ? 11   DC  F "C3'" 1 
ATOM   5351 O  "O3'" . DC  C 3 11  ? 101.290 129.207 104.465 1.00 158.15 ? 11   DC  F "O3'" 1 
ATOM   5352 C  "C2'" . DC  C 3 11  ? 103.192 128.314 103.231 1.00 155.50 ? 11   DC  F "C2'" 1 
ATOM   5353 C  "C1'" . DC  C 3 11  ? 103.159 129.469 102.241 1.00 158.07 ? 11   DC  F "C1'" 1 
ATOM   5354 N  N1    . DC  C 3 11  ? 104.118 129.319 101.114 1.00 157.51 ? 11   DC  F N1    1 
ATOM   5355 C  C2    . DC  C 3 11  ? 103.675 129.515 99.804  1.00 155.59 ? 11   DC  F C2    1 
ATOM   5356 O  O2    . DC  C 3 11  ? 102.490 129.812 99.608  1.00 155.48 ? 11   DC  F O2    1 
ATOM   5357 N  N3    . DC  C 3 11  ? 104.556 129.378 98.785  1.00 155.28 ? 11   DC  F N3    1 
ATOM   5358 C  C4    . DC  C 3 11  ? 105.826 129.057 99.040  1.00 155.02 ? 11   DC  F C4    1 
ATOM   5359 N  N4    . DC  C 3 11  ? 106.659 128.935 98.002  1.00 153.58 ? 11   DC  F N4    1 
ATOM   5360 C  C5    . DC  C 3 11  ? 106.297 128.851 100.370 1.00 156.30 ? 11   DC  F C5    1 
ATOM   5361 C  C6    . DC  C 3 11  ? 105.417 128.991 101.367 1.00 157.75 ? 11   DC  F C6    1 
ATOM   5362 P  P     . DA  C 3 12  ? 100.275 127.998 104.778 1.00 159.96 ? 12   DA  F P     1 
ATOM   5363 O  OP1   . DA  C 3 12  ? 99.544  128.345 106.016 1.00 159.49 ? 12   DA  F OP1   1 
ATOM   5364 O  OP2   . DA  C 3 12  ? 101.015 126.719 104.706 1.00 157.63 ? 12   DA  F OP2   1 
ATOM   5365 O  "O5'" . DA  C 3 12  ? 99.251  128.044 103.550 1.00 155.60 ? 12   DA  F "O5'" 1 
ATOM   5366 C  "C5'" . DA  C 3 12  ? 99.743  128.221 102.225 1.00 152.85 ? 12   DA  F "C5'" 1 
ATOM   5367 C  "C4'" . DA  C 3 12  ? 99.194  127.157 101.295 1.00 149.30 ? 12   DA  F "C4'" 1 
ATOM   5368 O  "O4'" . DA  C 3 12  ? 100.058 127.043 100.133 1.00 147.51 ? 12   DA  F "O4'" 1 
ATOM   5369 C  "C3'" . DA  C 3 12  ? 99.119  125.760 101.900 1.00 149.79 ? 12   DA  F "C3'" 1 
ATOM   5370 O  "O3'" . DA  C 3 12  ? 97.980  125.073 101.400 1.00 150.98 ? 12   DA  F "O3'" 1 
ATOM   5371 C  "C2'" . DA  C 3 12  ? 100.417 125.114 101.429 1.00 146.65 ? 12   DA  F "C2'" 1 
ATOM   5372 C  "C1'" . DA  C 3 12  ? 100.591 125.737 100.051 1.00 144.66 ? 12   DA  F "C1'" 1 
ATOM   5373 N  N9    . DA  C 3 12  ? 101.986 125.831 99.631  1.00 143.24 ? 12   DA  F N9    1 
ATOM   5374 C  C8    . DA  C 3 12  ? 103.090 125.774 100.434 1.00 144.94 ? 12   DA  F C8    1 
ATOM   5375 N  N7    . DA  C 3 12  ? 104.223 125.887 99.786  1.00 145.53 ? 12   DA  F N7    1 
ATOM   5376 C  C5    . DA  C 3 12  ? 103.838 126.028 98.464  1.00 143.08 ? 12   DA  F C5    1 
ATOM   5377 C  C6    . DA  C 3 12  ? 104.575 126.190 97.276  1.00 141.22 ? 12   DA  F C6    1 
ATOM   5378 N  N6    . DA  C 3 12  ? 105.909 126.235 97.242  1.00 138.93 ? 12   DA  F N6    1 
ATOM   5379 N  N1    . DA  C 3 12  ? 103.886 126.301 96.121  1.00 141.91 ? 12   DA  F N1    1 
ATOM   5380 C  C2    . DA  C 3 12  ? 102.548 126.250 96.161  1.00 142.21 ? 12   DA  F C2    1 
ATOM   5381 N  N3    . DA  C 3 12  ? 101.746 126.103 97.217  1.00 142.08 ? 12   DA  F N3    1 
ATOM   5382 C  C4    . DA  C 3 12  ? 102.462 125.995 98.348  1.00 142.32 ? 12   DA  F C4    1 
ATOM   5383 P  P     . DT  C 3 13  ? 97.264  123.944 102.292 1.00 156.57 ? 13   DT  F P     1 
ATOM   5384 O  OP1   . DT  C 3 13  ? 95.898  124.418 102.607 1.00 155.39 ? 13   DT  F OP1   1 
ATOM   5385 O  OP2   . DT  C 3 13  ? 98.191  123.584 103.387 1.00 153.30 ? 13   DT  F OP2   1 
ATOM   5386 O  "O5'" . DT  C 3 13  ? 97.162  122.690 101.307 1.00 150.76 ? 13   DT  F "O5'" 1 
ATOM   5387 C  "C5'" . DT  C 3 13  ? 98.279  122.327 100.507 1.00 142.69 ? 13   DT  F "C5'" 1 
ATOM   5388 C  "C4'" . DT  C 3 13  ? 98.045  122.696 99.054  1.00 137.04 ? 13   DT  F "C4'" 1 
ATOM   5389 O  "O4'" . DT  C 3 13  ? 99.218  123.378 98.532  1.00 136.40 ? 13   DT  F "O4'" 1 
ATOM   5390 C  "C3'" . DT  C 3 13  ? 97.829  121.512 98.127  1.00 135.98 ? 13   DT  F "C3'" 1 
ATOM   5391 O  "O3'" . DT  C 3 13  ? 97.056  121.912 96.999  1.00 136.29 ? 13   DT  F "O3'" 1 
ATOM   5392 C  "C2'" . DT  C 3 13  ? 99.258  121.175 97.733  1.00 132.78 ? 13   DT  F "C2'" 1 
ATOM   5393 C  "C1'" . DT  C 3 13  ? 99.842  122.571 97.552  1.00 133.19 ? 13   DT  F "C1'" 1 
ATOM   5394 N  N1    . DT  C 3 13  ? 101.324 122.633 97.752  1.00 131.99 ? 13   DT  F N1    1 
ATOM   5395 C  C2    . DT  C 3 13  ? 102.148 122.852 96.666  1.00 128.59 ? 13   DT  F C2    1 
ATOM   5396 O  O2    . DT  C 3 13  ? 101.732 123.004 95.531  1.00 126.71 ? 13   DT  F O2    1 
ATOM   5397 N  N3    . DT  C 3 13  ? 103.487 122.887 96.963  1.00 128.37 ? 13   DT  F N3    1 
ATOM   5398 C  C4    . DT  C 3 13  ? 104.070 122.728 98.208  1.00 130.36 ? 13   DT  F C4    1 
ATOM   5399 O  O4    . DT  C 3 13  ? 105.284 122.775 98.378  1.00 129.57 ? 13   DT  F O4    1 
ATOM   5400 C  C5    . DT  C 3 13  ? 103.151 122.502 99.297  1.00 132.23 ? 13   DT  F C5    1 
ATOM   5401 C  C7    . DT  C 3 13  ? 103.669 122.315 100.693 1.00 131.15 ? 13   DT  F C7    1 
ATOM   5402 C  C6    . DT  C 3 13  ? 101.840 122.465 99.019  1.00 133.69 ? 13   DT  F C6    1 
ATOM   5403 P  P     . DC  C 3 14  ? 96.292  120.816 96.105  1.00 134.57 ? 14   DC  F P     1 
ATOM   5404 O  OP1   . DC  C 3 14  ? 94.850  121.147 96.132  1.00 132.64 ? 14   DC  F OP1   1 
ATOM   5405 O  OP2   . DC  C 3 14  ? 96.743  119.477 96.543  1.00 132.24 ? 14   DC  F OP2   1 
ATOM   5406 O  "O5'" . DC  C 3 14  ? 96.853  121.069 94.628  1.00 132.03 ? 14   DC  F "O5'" 1 
ATOM   5407 C  "C5'" . DC  C 3 14  ? 98.217  121.423 94.445  1.00 128.44 ? 14   DC  F "C5'" 1 
ATOM   5408 C  "C4'" . DC  C 3 14  ? 98.678  121.133 93.031  1.00 125.10 ? 14   DC  F "C4'" 1 
ATOM   5409 O  "O4'" . DC  C 3 14  ? 100.122 121.220 92.978  1.00 121.52 ? 14   DC  F "O4'" 1 
ATOM   5410 C  "C3'" . DC  C 3 14  ? 98.352  119.742 92.521  1.00 124.65 ? 14   DC  F "C3'" 1 
ATOM   5411 O  "O3'" . DC  C 3 14  ? 98.304  119.750 91.098  1.00 125.92 ? 14   DC  F "O3'" 1 
ATOM   5412 C  "C2'" . DC  C 3 14  ? 99.528  118.923 93.043  1.00 117.09 ? 14   DC  F "C2'" 1 
ATOM   5413 C  "C1'" . DC  C 3 14  ? 100.686 119.920 92.969  1.00 116.78 ? 14   DC  F "C1'" 1 
ATOM   5414 N  N1    . DC  C 3 14  ? 101.627 119.804 94.119  1.00 113.49 ? 14   DC  F N1    1 
ATOM   5415 C  C2    . DC  C 3 14  ? 103.007 119.906 93.905  1.00 109.21 ? 14   DC  F C2    1 
ATOM   5416 O  O2    . DC  C 3 14  ? 103.426 120.099 92.757  1.00 107.43 ? 14   DC  F O2    1 
ATOM   5417 N  N3    . DC  C 3 14  ? 103.844 119.792 94.967  1.00 106.53 ? 14   DC  F N3    1 
ATOM   5418 C  C4    . DC  C 3 14  ? 103.347 119.584 96.188  1.00 107.15 ? 14   DC  F C4    1 
ATOM   5419 N  N4    . DC  C 3 14  ? 104.207 119.477 97.205  1.00 104.78 ? 14   DC  F N4    1 
ATOM   5420 C  C5    . DC  C 3 14  ? 101.948 119.473 96.420  1.00 109.63 ? 14   DC  F C5    1 
ATOM   5421 C  C6    . DC  C 3 14  ? 101.134 119.586 95.368  1.00 111.60 ? 14   DC  F C6    1 
ATOM   5422 P  P     . DC  C 3 15  ? 98.201  118.374 90.273  1.00 131.33 ? 15   DC  F P     1 
ATOM   5423 O  OP1   . DC  C 3 15  ? 97.540  118.685 88.987  1.00 131.73 ? 15   DC  F OP1   1 
ATOM   5424 O  OP2   . DC  C 3 15  ? 97.622  117.337 91.156  1.00 126.21 ? 15   DC  F OP2   1 
ATOM   5425 O  "O5'" . DC  C 3 15  ? 99.728  117.995 89.983  1.00 117.29 ? 15   DC  F "O5'" 1 
ATOM   5426 C  "C5'" . DC  C 3 15  ? 100.602 118.972 89.428  1.00 112.31 ? 15   DC  F "C5'" 1 
ATOM   5427 C  "C4'" . DC  C 3 15  ? 101.975 118.385 89.151  1.00 104.01 ? 15   DC  F "C4'" 1 
ATOM   5428 O  "O4'" . DC  C 3 15  ? 102.770 118.390 90.366  1.00 100.52 ? 15   DC  F "O4'" 1 
ATOM   5429 C  "C3'" . DC  C 3 15  ? 101.975 116.943 88.647  1.00 98.91  ? 15   DC  F "C3'" 1 
ATOM   5430 O  "O3'" . DC  C 3 15  ? 102.927 116.808 87.607  1.00 98.19  ? 15   DC  F "O3'" 1 
ATOM   5431 C  "C2'" . DC  C 3 15  ? 102.374 116.143 89.886  1.00 92.40  ? 15   DC  F "C2'" 1 
ATOM   5432 C  "C1'" . DC  C 3 15  ? 103.323 117.109 90.574  1.00 93.10  ? 15   DC  F "C1'" 1 
ATOM   5433 N  N1    . DC  C 3 15  ? 103.444 116.893 92.043  1.00 90.72  ? 15   DC  F N1    1 
ATOM   5434 C  C2    . DC  C 3 15  ? 104.711 116.855 92.639  1.00 85.14  ? 15   DC  F C2    1 
ATOM   5435 O  O2    . DC  C 3 15  ? 105.717 116.992 91.932  1.00 84.74  ? 15   DC  F O2    1 
ATOM   5436 N  N3    . DC  C 3 15  ? 104.799 116.667 93.979  1.00 82.00  ? 15   DC  F N3    1 
ATOM   5437 C  C4    . DC  C 3 15  ? 103.689 116.524 94.706  1.00 82.35  ? 15   DC  F C4    1 
ATOM   5438 N  N4    . DC  C 3 15  ? 103.823 116.341 96.022  1.00 78.86  ? 15   DC  F N4    1 
ATOM   5439 C  C5    . DC  C 3 15  ? 102.393 116.562 94.116  1.00 89.65  ? 15   DC  F C5    1 
ATOM   5440 C  C6    . DC  C 3 15  ? 102.319 116.748 92.796  1.00 92.22  ? 15   DC  F C6    1 
ATOM   5441 P  P     . DG  C 3 16  ? 102.852 115.569 86.588  1.00 103.70 ? 16   DG  F P     1 
ATOM   5442 O  OP1   . DG  C 3 16  ? 102.785 116.122 85.217  1.00 99.17  ? 16   DG  F OP1   1 
ATOM   5443 O  OP2   . DG  C 3 16  ? 101.795 114.649 87.063  1.00 101.57 ? 16   DG  F OP2   1 
ATOM   5444 O  "O5'" . DG  C 3 16  ? 104.262 114.846 86.781  1.00 95.47  ? 16   DG  F "O5'" 1 
ATOM   5445 C  "C5'" . DG  C 3 16  ? 105.455 115.620 86.787  1.00 91.35  ? 16   DG  F "C5'" 1 
ATOM   5446 C  "C4'" . DG  C 3 16  ? 106.561 114.895 87.527  1.00 84.11  ? 16   DG  F "C4'" 1 
ATOM   5447 O  "O4'" . DG  C 3 16  ? 106.327 114.981 88.958  1.00 81.58  ? 16   DG  F "O4'" 1 
ATOM   5448 C  "C3'" . DG  C 3 16  ? 106.678 113.403 87.201  1.00 76.67  ? 16   DG  F "C3'" 1 
ATOM   5449 O  "O3'" . DG  C 3 16  ? 108.033 113.053 86.975  1.00 75.08  ? 16   DG  F "O3'" 1 
ATOM   5450 C  "C2'" . DG  C 3 16  ? 106.126 112.723 88.449  1.00 73.04  ? 16   DG  F "C2'" 1 
ATOM   5451 C  "C1'" . DG  C 3 16  ? 106.517 113.712 89.531  1.00 71.04  ? 16   DG  F "C1'" 1 
ATOM   5452 N  N9    . DG  C 3 16  ? 105.696 113.606 90.733  1.00 66.26  ? 16   DG  F N9    1 
ATOM   5453 C  C8    . DG  C 3 16  ? 104.325 113.563 90.797  1.00 70.92  ? 16   DG  F C8    1 
ATOM   5454 N  N7    . DG  C 3 16  ? 103.865 113.455 92.013  1.00 69.25  ? 16   DG  F N7    1 
ATOM   5455 C  C5    . DG  C 3 16  ? 105.004 113.420 92.805  1.00 64.27  ? 16   DG  F C5    1 
ATOM   5456 C  C6    . DG  C 3 16  ? 105.135 113.311 94.209  1.00 61.63  ? 16   DG  F C6    1 
ATOM   5457 O  O6    . DG  C 3 16  ? 104.239 113.223 95.059  1.00 64.18  ? 16   DG  F O6    1 
ATOM   5458 N  N1    . DG  C 3 16  ? 106.470 113.315 94.604  1.00 56.92  ? 16   DG  F N1    1 
ATOM   5459 C  C2    . DG  C 3 16  ? 107.539 113.403 93.748  1.00 55.13  ? 16   DG  F C2    1 
ATOM   5460 N  N2    . DG  C 3 16  ? 108.750 113.391 94.316  1.00 53.02  ? 16   DG  F N2    1 
ATOM   5461 N  N3    . DG  C 3 16  ? 107.431 113.508 92.431  1.00 58.35  ? 16   DG  F N3    1 
ATOM   5462 C  C4    . DG  C 3 16  ? 106.139 113.509 92.031  1.00 62.37  ? 16   DG  F C4    1 
ATOM   5463 P  P     . DT  C 3 17  ? 108.400 111.608 86.376  1.00 77.94  ? 17   DT  F P     1 
ATOM   5464 O  OP1   . DT  C 3 17  ? 109.434 111.818 85.340  1.00 78.78  ? 17   DT  F OP1   1 
ATOM   5465 O  OP2   . DT  C 3 17  ? 107.138 110.917 86.032  1.00 76.99  ? 17   DT  F OP2   1 
ATOM   5466 O  "O5'" . DT  C 3 17  ? 109.072 110.839 87.606  1.00 68.74  ? 17   DT  F "O5'" 1 
ATOM   5467 C  "C5'" . DT  C 3 17  ? 110.463 110.976 87.838  1.00 62.77  ? 17   DT  F "C5'" 1 
ATOM   5468 C  "C4'" . DT  C 3 17  ? 110.842 110.516 89.234  1.00 57.26  ? 17   DT  F "C4'" 1 
ATOM   5469 O  "O4'" . DT  C 3 17  ? 110.000 111.156 90.214  1.00 58.77  ? 17   DT  F "O4'" 1 
ATOM   5470 C  "C3'" . DT  C 3 17  ? 110.636 109.046 89.521  1.00 50.44  ? 17   DT  F "C3'" 1 
ATOM   5471 O  "O3'" . DT  C 3 17  ? 111.698 108.271 88.985  1.00 52.61  ? 17   DT  F "O3'" 1 
ATOM   5472 C  "C2'" . DT  C 3 17  ? 110.666 109.037 91.044  1.00 48.94  ? 17   DT  F "C2'" 1 
ATOM   5473 C  "C1'" . DT  C 3 17  ? 110.065 110.395 91.408  1.00 50.23  ? 17   DT  F "C1'" 1 
ATOM   5474 N  N1    . DT  C 3 17  ? 108.711 110.293 92.018  1.00 48.06  ? 17   DT  F N1    1 
ATOM   5475 C  C2    . DT  C 3 17  ? 108.610 110.145 93.379  1.00 45.63  ? 17   DT  F C2    1 
ATOM   5476 O  O2    . DT  C 3 17  ? 109.578 110.098 94.117  1.00 43.70  ? 17   DT  F O2    1 
ATOM   5477 N  N3    . DT  C 3 17  ? 107.331 110.058 93.854  1.00 45.85  ? 17   DT  F N3    1 
ATOM   5478 C  C4    . DT  C 3 17  ? 106.165 110.096 93.114  1.00 47.84  ? 17   DT  F C4    1 
ATOM   5479 O  O4    . DT  C 3 17  ? 105.057 110.009 93.630  1.00 47.36  ? 17   DT  F O4    1 
ATOM   5480 C  C5    . DT  C 3 17  ? 106.339 110.246 91.692  1.00 52.53  ? 17   DT  F C5    1 
ATOM   5481 C  C7    . DT  C 3 17  ? 105.141 110.298 90.794  1.00 55.56  ? 17   DT  F C7    1 
ATOM   5482 C  C6    . DT  C 3 17  ? 107.591 110.334 91.215  1.00 52.40  ? 17   DT  F C6    1 
ATOM   5483 P  P     . DA  C 3 18  ? 111.547 106.673 88.886  1.00 62.84  ? 18   DA  F P     1 
ATOM   5484 O  OP1   . DA  C 3 18  ? 112.698 106.150 88.119  1.00 65.67  ? 18   DA  F OP1   1 
ATOM   5485 O  OP2   . DA  C 3 18  ? 110.169 106.395 88.429  1.00 59.86  ? 18   DA  F OP2   1 
ATOM   5486 O  "O5'" . DA  C 3 18  ? 111.665 106.169 90.402  1.00 50.52  ? 18   DA  F "O5'" 1 
ATOM   5487 C  "C5'" . DA  C 3 18  ? 112.871 106.376 91.133  1.00 44.25  ? 18   DA  F "C5'" 1 
ATOM   5488 C  "C4'" . DA  C 3 18  ? 112.674 106.081 92.613  1.00 39.64  ? 18   DA  F "C4'" 1 
ATOM   5489 O  "O4'" . DA  C 3 18  ? 111.819 107.081 93.214  1.00 38.39  ? 18   DA  F "O4'" 1 
ATOM   5490 C  "C3'" . DA  C 3 18  ? 111.979 104.776 92.926  1.00 33.60  ? 18   DA  F "C3'" 1 
ATOM   5491 O  "O3'" . DA  C 3 18  ? 112.897 103.705 92.864  1.00 28.82  ? 18   DA  F "O3'" 1 
ATOM   5492 C  "C2'" . DA  C 3 18  ? 111.508 105.026 94.351  1.00 30.92  ? 18   DA  F "C2'" 1 
ATOM   5493 C  "C1'" . DA  C 3 18  ? 111.100 106.497 94.291  1.00 29.66  ? 18   DA  F "C1'" 1 
ATOM   5494 N  N9    . DA  C 3 18  ? 109.669 106.693 94.067  1.00 29.50  ? 18   DA  F N9    1 
ATOM   5495 C  C8    . DA  C 3 18  ? 109.045 106.916 92.875  1.00 36.19  ? 18   DA  F C8    1 
ATOM   5496 N  N7    . DA  C 3 18  ? 107.746 107.063 92.974  1.00 34.62  ? 18   DA  F N7    1 
ATOM   5497 C  C5    . DA  C 3 18  ? 107.499 106.915 94.325  1.00 29.53  ? 18   DA  F C5    1 
ATOM   5498 C  C6    . DA  C 3 18  ? 106.314 106.959 95.082  1.00 28.56  ? 18   DA  F C6    1 
ATOM   5499 N  N6    . DA  C 3 18  ? 105.108 107.174 94.548  1.00 27.79  ? 18   DA  F N6    1 
ATOM   5500 N  N1    . DA  C 3 18  ? 106.416 106.773 96.412  1.00 29.33  ? 18   DA  F N1    1 
ATOM   5501 C  C2    . DA  C 3 18  ? 107.624 106.560 96.940  1.00 28.92  ? 18   DA  F C2    1 
ATOM   5502 N  N3    . DA  C 3 18  ? 108.806 106.498 96.333  1.00 26.89  ? 18   DA  F N3    1 
ATOM   5503 C  C4    . DA  C 3 18  ? 108.673 106.685 95.014  1.00 28.03  ? 18   DA  F C4    1 
ATOM   5504 P  P     . DG  C 3 19  ? 112.368 102.221 92.563  1.00 36.51  ? 19   DG  F P     1 
ATOM   5505 O  OP1   . DG  C 3 19  ? 113.539 101.414 92.167  1.00 39.20  ? 19   DG  F OP1   1 
ATOM   5506 O  OP2   . DG  C 3 19  ? 111.205 102.331 91.656  1.00 35.24  ? 19   DG  F OP2   1 
ATOM   5507 O  "O5'" . DG  C 3 19  ? 111.830 101.711 93.978  1.00 30.89  ? 19   DG  F "O5'" 1 
ATOM   5508 C  "C5'" . DG  C 3 19  ? 112.737 101.520 95.050  1.00 26.55  ? 19   DG  F "C5'" 1 
ATOM   5509 C  "C4'" . DG  C 3 19  ? 112.008 101.464 96.379  1.00 22.44  ? 19   DG  F "C4'" 1 
ATOM   5510 O  "O4'" . DG  C 3 19  ? 111.245 102.678 96.563  1.00 22.33  ? 19   DG  F "O4'" 1 
ATOM   5511 C  "C3'" . DG  C 3 19  ? 110.987 100.353 96.508  1.00 21.21  ? 19   DG  F "C3'" 1 
ATOM   5512 O  "O3'" . DG  C 3 19  ? 111.622 99.150  96.913  1.00 22.87  ? 19   DG  F "O3'" 1 
ATOM   5513 C  "C2'" . DG  C 3 19  ? 110.084 100.899 97.603  1.00 23.44  ? 19   DG  F "C2'" 1 
ATOM   5514 C  "C1'" . DG  C 3 19  ? 110.054 102.388 97.272  1.00 19.14  ? 19   DG  F "C1'" 1 
ATOM   5515 N  N9    . DG  C 3 19  ? 108.917 102.775 96.450  1.00 16.47  ? 19   DG  F N9    1 
ATOM   5516 C  C8    . DG  C 3 19  ? 108.922 103.042 95.107  1.00 21.16  ? 19   DG  F C8    1 
ATOM   5517 N  N7    . DG  C 3 19  ? 107.752 103.369 94.639  1.00 22.39  ? 19   DG  F N7    1 
ATOM   5518 C  C5    . DG  C 3 19  ? 106.917 103.313 95.743  1.00 18.81  ? 19   DG  F C5    1 
ATOM   5519 C  C6    . DG  C 3 19  ? 105.534 103.567 95.848  1.00 19.58  ? 19   DG  F C6    1 
ATOM   5520 O  O6    . DG  C 3 19  ? 104.751 103.904 94.952  1.00 21.14  ? 19   DG  F O6    1 
ATOM   5521 N  N1    . DG  C 3 19  ? 105.074 103.395 97.150  1.00 18.66  ? 19   DG  F N1    1 
ATOM   5522 C  C2    . DG  C 3 19  ? 105.858 103.025 98.215  1.00 18.50  ? 19   DG  F C2    1 
ATOM   5523 N  N2    . DG  C 3 19  ? 105.242 102.908 99.398  1.00 17.16  ? 19   DG  F N2    1 
ATOM   5524 N  N3    . DG  C 3 19  ? 107.159 102.785 98.128  1.00 19.77  ? 19   DG  F N3    1 
ATOM   5525 C  C4    . DG  C 3 19  ? 107.618 102.948 96.866  1.00 18.04  ? 19   DG  F C4    1 
HETATM 5526 P  P     . 2DA C 3 20  ? 110.921 97.845  96.324  1.00 25.45  ? 20   2DA F P     1 
HETATM 5527 O  OP1   . 2DA C 3 20  ? 111.842 96.736  96.671  1.00 27.75  ? 20   2DA F OP1   1 
HETATM 5528 O  OP2   . 2DA C 3 20  ? 110.424 98.073  94.938  1.00 22.86  ? 20   2DA F OP2   1 
HETATM 5529 O  "O5'" . 2DA C 3 20  ? 109.633 97.769  97.235  1.00 24.25  ? 20   2DA F "O5'" 1 
HETATM 5530 C  "C5'" . 2DA C 3 20  ? 109.746 97.469  98.608  1.00 21.05  ? 20   2DA F "C5'" 1 
HETATM 5531 C  "C4'" . 2DA C 3 20  ? 108.403 97.765  99.205  1.00 16.65  ? 20   2DA F "C4'" 1 
HETATM 5532 O  "O4'" . 2DA C 3 20  ? 107.772 98.676  98.364  1.00 13.87  ? 20   2DA F "O4'" 1 
HETATM 5533 C  "C3'" . 2DA C 3 20  ? 107.540 96.554  99.124  1.00 16.88  ? 20   2DA F "C3'" 1 
HETATM 5534 C  "C2'" . 2DA C 3 20  ? 106.253 97.100  98.581  1.00 17.44  ? 20   2DA F "C2'" 1 
HETATM 5535 C  "C1'" . 2DA C 3 20  ? 106.418 98.569  98.540  1.00 13.79  ? 20   2DA F "C1'" 1 
HETATM 5536 N  N9    . 2DA C 3 20  ? 105.926 99.108  97.312  1.00 13.99  ? 20   2DA F N9    1 
HETATM 5537 C  C8    . 2DA C 3 20  ? 106.683 99.249  96.257  1.00 16.49  ? 20   2DA F C8    1 
HETATM 5538 N  N7    . 2DA C 3 20  ? 105.979 99.783  95.254  1.00 17.33  ? 20   2DA F N7    1 
HETATM 5539 C  C5    . 2DA C 3 20  ? 104.759 99.984  95.688  1.00 16.60  ? 20   2DA F C5    1 
HETATM 5540 C  C6    . 2DA C 3 20  ? 103.547 100.510 95.114  1.00 17.58  ? 20   2DA F C6    1 
HETATM 5541 N  N6    . 2DA C 3 20  ? 103.526 100.953 93.853  1.00 18.28  ? 20   2DA F N6    1 
HETATM 5542 N  N1    . 2DA C 3 20  ? 102.473 100.541 95.889  1.00 18.30  ? 20   2DA F N1    1 
HETATM 5543 C  C2    . 2DA C 3 20  ? 102.509 100.109 97.144  1.00 19.12  ? 20   2DA F C2    1 
HETATM 5544 N  N3    . 2DA C 3 20  ? 103.599 99.628  97.725  1.00 18.63  ? 20   2DA F N3    1 
HETATM 5545 C  C4    . 2DA C 3 20  ? 104.731 99.537  97.049  1.00 15.67  ? 20   2DA F C4    1 
HETATM 5546 P  PG    . DGT D 4 .   ? 108.205 89.411  95.242  1.00 33.84  ? 2601 DGT A PG    1 
HETATM 5547 O  O1G   . DGT D 4 .   ? 108.889 89.944  96.473  1.00 34.07  ? 2601 DGT A O1G   1 
HETATM 5548 O  O2G   . DGT D 4 .   ? 108.287 87.906  95.237  1.00 32.37  ? 2601 DGT A O2G   1 
HETATM 5549 O  O3G   . DGT D 4 .   ? 108.899 89.968  94.024  1.00 30.25  ? 2601 DGT A O3G   1 
HETATM 5550 O  O3B   . DGT D 4 .   ? 106.627 89.879  95.238  1.00 28.21  ? 2601 DGT A O3B   1 
HETATM 5551 P  PB    . DGT D 4 .   ? 106.068 91.059  96.141  1.00 27.49  ? 2601 DGT A PB    1 
HETATM 5552 O  O1B   . DGT D 4 .   ? 104.481 91.037  96.124  1.00 21.32  ? 2601 DGT A O1B   1 
HETATM 5553 O  O2B   . DGT D 4 .   ? 106.544 90.876  97.561  1.00 26.13  ? 2601 DGT A O2B   1 
HETATM 5554 O  O3A   . DGT D 4 .   ? 106.581 92.445  95.554  1.00 34.50  ? 2601 DGT A O3A   1 
HETATM 5555 P  PA    . DGT D 4 .   ? 107.182 93.646  96.405  1.00 27.93  ? 2601 DGT A PA    1 
HETATM 5556 O  O1A   . DGT D 4 .   ? 107.901 94.604  95.488  1.00 21.29  ? 2601 DGT A O1A   1 
HETATM 5557 O  O2A   . DGT D 4 .   ? 108.154 93.125  97.434  1.00 25.68  ? 2601 DGT A O2A   1 
HETATM 5558 O  "O5'" . DGT D 4 .   ? 105.954 94.426  97.167  1.00 20.71  ? 2601 DGT A "O5'" 1 
HETATM 5559 C  "C5'" . DGT D 4 .   ? 105.412 93.801  98.291  1.00 20.59  ? 2601 DGT A "C5'" 1 
HETATM 5560 C  "C4'" . DGT D 4 .   ? 104.163 94.523  98.730  1.00 21.10  ? 2601 DGT A "C4'" 1 
HETATM 5561 O  "O4'" . DGT D 4 .   ? 103.949 95.689  97.892  1.00 18.96  ? 2601 DGT A "O4'" 1 
HETATM 5562 C  "C3'" . DGT D 4 .   ? 102.969 93.599  98.524  1.00 22.23  ? 2601 DGT A "C3'" 1 
HETATM 5563 O  "O3'" . DGT D 4 .   ? 102.063 93.742  99.634  1.00 26.64  ? 2601 DGT A "O3'" 1 
HETATM 5564 C  "C2'" . DGT D 4 .   ? 102.345 94.126  97.253  1.00 18.13  ? 2601 DGT A "C2'" 1 
HETATM 5565 C  "C1'" . DGT D 4 .   ? 102.644 95.607  97.343  1.00 16.29  ? 2601 DGT A "C1'" 1 
HETATM 5566 N  N9    . DGT D 4 .   ? 102.624 96.210  96.033  1.00 17.66  ? 2601 DGT A N9    1 
HETATM 5567 C  C8    . DGT D 4 .   ? 103.836 95.915  95.522  1.00 19.08  ? 2601 DGT A C8    1 
HETATM 5568 N  N7    . DGT D 4 .   ? 103.975 96.419  94.280  1.00 15.73  ? 2601 DGT A N7    1 
HETATM 5569 C  C5    . DGT D 4 .   ? 102.830 97.040  94.009  1.00 15.90  ? 2601 DGT A C5    1 
HETATM 5570 C  C6    . DGT D 4 .   ? 102.351 97.780  92.839  1.00 15.65  ? 2601 DGT A C6    1 
HETATM 5571 O  O6    . DGT D 4 .   ? 103.035 97.941  91.832  1.00 17.78  ? 2601 DGT A O6    1 
HETATM 5572 N  N1    . DGT D 4 .   ? 101.085 98.279  92.956  1.00 16.56  ? 2601 DGT A N1    1 
HETATM 5573 C  C2    . DGT D 4 .   ? 100.288 98.125  94.058  1.00 19.33  ? 2601 DGT A C2    1 
HETATM 5574 N  N2    . DGT D 4 .   ? 99.063  98.654  94.076  1.00 20.21  ? 2601 DGT A N2    1 
HETATM 5575 N  N3    . DGT D 4 .   ? 100.717 97.457  95.120  1.00 18.98  ? 2601 DGT A N3    1 
HETATM 5576 C  C4    . DGT D 4 .   ? 101.967 96.908  95.129  1.00 18.07  ? 2601 DGT A C4    1 
HETATM 5577 MG MG    . MG  E 5 .   ? 107.896 90.592  99.016  1.00 27.25  ? 2602 MG  A MG    1 
# 
