data_8S84
# 
_entry.id   8S84 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   8S84         pdb_00008s84 10.2210/pdb8s84/pdb 
WWPDB D_1292137004 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-13 
2 'Structure model' 1 1 2024-12-25 
3 'Structure model' 1 2 2025-01-22 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
4 3 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.pdbx_database_id_DOI'    
2 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
3 2 'Structure model' '_citation.title'                   
4 3 'Structure model' '_citation.journal_volume'          
5 3 'Structure model' '_citation.year'                    
6 3 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8S84 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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_contact_author.id                 2 
_pdbx_contact_author.email              andreas.marx@uni-konstanz.de 
_pdbx_contact_author.name_first         Andreas 
_pdbx_contact_author.name_last          Marx 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6471-3689 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Gutfreund, C.' 1 0009-0003-3915-1105 
'Betz, K.'      2 0000-0002-5111-7730 
# 
_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            'Nucleic Acids Res.' 
_citation.journal_id_ASTM           NARHAD 
_citation.journal_id_CSD            0389 
_citation.journal_id_ISSN           1362-4962 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            53 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structural insights into a DNA polymerase reading the xeno nucleic acid HNA.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1093/nar/gkae1156 
_citation.pdbx_database_id_PubMed   39673482 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Gutfreund, C.' 1 ? 
primary 'Betz, K.'      2 ? 
primary 'Abramov, M.'   3 ? 
primary 'Coosemans, F.' 4 ? 
primary 'Holliger, P.'  5 ? 
primary 'Herdewijn, P.' 6 ? 
primary 'Marx, A.'      7 ? 
# 
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'                                                                             89976.500 1  
2.7.7.7 ? ? ? 
2 polymer     syn 
;DNA (5'-D(*GP*AP*CP*CP*AP*CP*GP*GP*CP*CP*AP*CP*A*(XG4))-3')
;
3930.578  1  ?       ? ? ? 
3 polymer     syn 
;DNA (5'-D(P*AP*CP*TP*GP*TP*GP*GP*CP*CP*GP*TP*GP*GP*TP*C)-3')
;
4930.189  1  ?       ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                                                                              24.305    5  ? ? ? 
? 
5 non-polymer syn "2'-deoxy-5'-O-[(R)-hydroxy{[(R)-hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl]guanosine" 506.196   1  ? ? ? 
? 
6 non-polymer syn 'MANGANESE (II) ION'                                                                         54.938    1  ? ? ? 
? 
7 non-polymer syn IMIDAZOLE                                                                                    69.085    1  ? ? ? 
? 
8 non-polymer syn GLYCEROL                                                                                     92.094    2  ? ? ? 
? 
9 water       nat water                                                                                        18.015    14 ? ? ? 
? 
# 
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 
;MILDTDYITEDGKPVIRIFKKENGEFKIEYDRTFEPYFYALLKDDSAIEEVKKITAERHGTVVTVKRVEKVQKKFLGRPV
EVWKLYFTHPQDQPAIRDKIREHPAVIDIYEYDTPFAKRYLIDKGLVPMEGDEELKMLAFAIATLYHEGEEFAEGPILMI
SYADEEGARVITWKNVDLPYVDVVSTEREMIKRFLRVVKEKDPDVLITYNGDNFDFAYLKKRCEKLGINFALGRDGSEPK
IQRMGDRFAVEVKGRIHFDLYPVIRRTINLPTYTLEAVYEAVFGQPKEKVYAEEITTAWETGENLERVARYSMEDAKVTY
ELGKEFLPMEAQLSRLIGQSLWDVSRSSTGNLVEWFLLRKAYERNELAPNKPDEKELARRRQKYEGGYVKEPERGLWENI
VYLDFRSLYPSIIITHNVSPDTLNREGCGEYDVAPQVGHRFCKDLPGFIPSLLGDLLEERQKIKKKMKATIDPIERKLLD
YRQRLIKILANSVYGHMGFENARWYCKECAESVTAWGREYLTMTIKEIEEKYGFKVIYSDTDGFFATIPGADAETVKKKA
MEFLKYINAKLPGALELEYEGFYKRGFFVTKKKYAVIDEEGKITTRGLEIVRRDWSEIAKETQARVLEALLKDGDVEKAV
RIVKEVTEKLSKYEVPPEKLVIHKQITRDLKDYKATGPHVAVAKRLAARGVKIRPGTVISYIVLKGSGRIGDRAIPFDEF
DPTKHRYDAEYYIEKQVLPAVERILRAFGYRKEDLRYQKTRQVGLSAWLKPKGT
;
;MILDTDYITEDGKPVIRIFKKENGEFKIEYDRTFEPYFYALLKDDSAIEEVKKITAERHGTVVTVKRVEKVQKKFLGRPV
EVWKLYFTHPQDQPAIRDKIREHPAVIDIYEYDTPFAKRYLIDKGLVPMEGDEELKMLAFAIATLYHEGEEFAEGPILMI
SYADEEGARVITWKNVDLPYVDVVSTEREMIKRFLRVVKEKDPDVLITYNGDNFDFAYLKKRCEKLGINFALGRDGSEPK
IQRMGDRFAVEVKGRIHFDLYPVIRRTINLPTYTLEAVYEAVFGQPKEKVYAEEITTAWETGENLERVARYSMEDAKVTY
ELGKEFLPMEAQLSRLIGQSLWDVSRSSTGNLVEWFLLRKAYERNELAPNKPDEKELARRRQKYEGGYVKEPERGLWENI
VYLDFRSLYPSIIITHNVSPDTLNREGCGEYDVAPQVGHRFCKDLPGFIPSLLGDLLEERQKIKKKMKATIDPIERKLLD
YRQRLIKILANSVYGHMGFENARWYCKECAESVTAWGREYLTMTIKEIEEKYGFKVIYSDTDGFFATIPGADAETVKKKA
MEFLKYINAKLPGALELEYEGFYKRGFFVTKKKYAVIDEEGKITTRGLEIVRRDWSEIAKETQARVLEALLKDGDVEKAV
RIVKEVTEKLSKYEVPPEKLVIHKQITRDLKDYKATGPHVAVAKRLAARGVKIRPGTVISYIVLKGSGRIGDRAIPFDEF
DPTKHRYDAEYYIEKQVLPAVERILRAFGYRKEDLRYQKTRQVGLSAWLKPKGT
;
A ? 
2 polydeoxyribonucleotide no no '(DG)(DA)(DC)(DC)(DA)(DC)(DG)(DG)(DC)(DC)(DA)(DC)(DA)' GACCACGGCCACA P ? 
3 polydeoxyribonucleotide no no '(DA)(DA)(DC)(DT)(DG)(DT)(DG)(DG)(DC)(DC)(DG)(DT)(DG)(DG)(DT)(DC)' AACTGTGGCCGTGGTC T ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'MAGNESIUM ION'                                                                              MG  
5 "2'-deoxy-5'-O-[(R)-hydroxy{[(R)-hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl]guanosine" XG4 
6 'MANGANESE (II) ION'                                                                         MN  
7 IMIDAZOLE                                                                                    IMD 
8 GLYCEROL                                                                                     GOL 
9 water                                                                                        HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ILE n 
1 3   LEU n 
1 4   ASP n 
1 5   THR n 
1 6   ASP n 
1 7   TYR n 
1 8   ILE n 
1 9   THR n 
1 10  GLU n 
1 11  ASP n 
1 12  GLY n 
1 13  LYS n 
1 14  PRO n 
1 15  VAL n 
1 16  ILE n 
1 17  ARG n 
1 18  ILE n 
1 19  PHE n 
1 20  LYS n 
1 21  LYS n 
1 22  GLU n 
1 23  ASN n 
1 24  GLY n 
1 25  GLU n 
1 26  PHE n 
1 27  LYS n 
1 28  ILE n 
1 29  GLU n 
1 30  TYR n 
1 31  ASP n 
1 32  ARG n 
1 33  THR n 
1 34  PHE n 
1 35  GLU n 
1 36  PRO n 
1 37  TYR n 
1 38  PHE n 
1 39  TYR n 
1 40  ALA n 
1 41  LEU n 
1 42  LEU n 
1 43  LYS n 
1 44  ASP n 
1 45  ASP n 
1 46  SER n 
1 47  ALA n 
1 48  ILE n 
1 49  GLU n 
1 50  GLU n 
1 51  VAL n 
1 52  LYS n 
1 53  LYS n 
1 54  ILE n 
1 55  THR n 
1 56  ALA n 
1 57  GLU n 
1 58  ARG n 
1 59  HIS n 
1 60  GLY n 
1 61  THR n 
1 62  VAL n 
1 63  VAL n 
1 64  THR n 
1 65  VAL n 
1 66  LYS n 
1 67  ARG n 
1 68  VAL n 
1 69  GLU n 
1 70  LYS n 
1 71  VAL n 
1 72  GLN n 
1 73  LYS n 
1 74  LYS n 
1 75  PHE n 
1 76  LEU n 
1 77  GLY n 
1 78  ARG n 
1 79  PRO n 
1 80  VAL n 
1 81  GLU n 
1 82  VAL n 
1 83  TRP n 
1 84  LYS n 
1 85  LEU n 
1 86  TYR n 
1 87  PHE n 
1 88  THR n 
1 89  HIS n 
1 90  PRO n 
1 91  GLN n 
1 92  ASP n 
1 93  GLN n 
1 94  PRO n 
1 95  ALA n 
1 96  ILE n 
1 97  ARG n 
1 98  ASP n 
1 99  LYS n 
1 100 ILE n 
1 101 ARG n 
1 102 GLU n 
1 103 HIS n 
1 104 PRO n 
1 105 ALA n 
1 106 VAL n 
1 107 ILE n 
1 108 ASP n 
1 109 ILE n 
1 110 TYR n 
1 111 GLU n 
1 112 TYR n 
1 113 ASP n 
1 114 THR n 
1 115 PRO n 
1 116 PHE n 
1 117 ALA n 
1 118 LYS n 
1 119 ARG n 
1 120 TYR n 
1 121 LEU n 
1 122 ILE n 
1 123 ASP n 
1 124 LYS n 
1 125 GLY n 
1 126 LEU n 
1 127 VAL n 
1 128 PRO n 
1 129 MET n 
1 130 GLU n 
1 131 GLY n 
1 132 ASP n 
1 133 GLU n 
1 134 GLU n 
1 135 LEU n 
1 136 LYS n 
1 137 MET n 
1 138 LEU n 
1 139 ALA n 
1 140 PHE n 
1 141 ALA n 
1 142 ILE n 
1 143 ALA n 
1 144 THR n 
1 145 LEU n 
1 146 TYR n 
1 147 HIS n 
1 148 GLU n 
1 149 GLY n 
1 150 GLU n 
1 151 GLU n 
1 152 PHE n 
1 153 ALA n 
1 154 GLU n 
1 155 GLY n 
1 156 PRO n 
1 157 ILE n 
1 158 LEU n 
1 159 MET n 
1 160 ILE n 
1 161 SER n 
1 162 TYR n 
1 163 ALA n 
1 164 ASP n 
1 165 GLU n 
1 166 GLU n 
1 167 GLY n 
1 168 ALA n 
1 169 ARG n 
1 170 VAL n 
1 171 ILE n 
1 172 THR n 
1 173 TRP n 
1 174 LYS n 
1 175 ASN n 
1 176 VAL n 
1 177 ASP n 
1 178 LEU n 
1 179 PRO n 
1 180 TYR n 
1 181 VAL n 
1 182 ASP n 
1 183 VAL n 
1 184 VAL n 
1 185 SER n 
1 186 THR n 
1 187 GLU n 
1 188 ARG n 
1 189 GLU n 
1 190 MET n 
1 191 ILE n 
1 192 LYS n 
1 193 ARG n 
1 194 PHE n 
1 195 LEU n 
1 196 ARG n 
1 197 VAL n 
1 198 VAL n 
1 199 LYS n 
1 200 GLU n 
1 201 LYS n 
1 202 ASP n 
1 203 PRO n 
1 204 ASP n 
1 205 VAL n 
1 206 LEU n 
1 207 ILE n 
1 208 THR n 
1 209 TYR n 
1 210 ASN n 
1 211 GLY n 
1 212 ASP n 
1 213 ASN n 
1 214 PHE n 
1 215 ASP n 
1 216 PHE n 
1 217 ALA n 
1 218 TYR n 
1 219 LEU n 
1 220 LYS n 
1 221 LYS n 
1 222 ARG n 
1 223 CYS n 
1 224 GLU n 
1 225 LYS n 
1 226 LEU n 
1 227 GLY n 
1 228 ILE n 
1 229 ASN n 
1 230 PHE n 
1 231 ALA n 
1 232 LEU n 
1 233 GLY n 
1 234 ARG n 
1 235 ASP n 
1 236 GLY n 
1 237 SER n 
1 238 GLU n 
1 239 PRO n 
1 240 LYS n 
1 241 ILE n 
1 242 GLN n 
1 243 ARG n 
1 244 MET n 
1 245 GLY n 
1 246 ASP n 
1 247 ARG n 
1 248 PHE n 
1 249 ALA n 
1 250 VAL n 
1 251 GLU n 
1 252 VAL n 
1 253 LYS n 
1 254 GLY n 
1 255 ARG n 
1 256 ILE n 
1 257 HIS n 
1 258 PHE n 
1 259 ASP n 
1 260 LEU n 
1 261 TYR n 
1 262 PRO n 
1 263 VAL n 
1 264 ILE n 
1 265 ARG n 
1 266 ARG n 
1 267 THR n 
1 268 ILE n 
1 269 ASN n 
1 270 LEU n 
1 271 PRO n 
1 272 THR n 
1 273 TYR n 
1 274 THR n 
1 275 LEU n 
1 276 GLU n 
1 277 ALA n 
1 278 VAL n 
1 279 TYR n 
1 280 GLU n 
1 281 ALA n 
1 282 VAL n 
1 283 PHE n 
1 284 GLY n 
1 285 GLN n 
1 286 PRO n 
1 287 LYS n 
1 288 GLU n 
1 289 LYS n 
1 290 VAL n 
1 291 TYR n 
1 292 ALA n 
1 293 GLU n 
1 294 GLU n 
1 295 ILE n 
1 296 THR n 
1 297 THR n 
1 298 ALA n 
1 299 TRP n 
1 300 GLU n 
1 301 THR n 
1 302 GLY n 
1 303 GLU n 
1 304 ASN n 
1 305 LEU n 
1 306 GLU n 
1 307 ARG n 
1 308 VAL n 
1 309 ALA n 
1 310 ARG n 
1 311 TYR n 
1 312 SER n 
1 313 MET n 
1 314 GLU n 
1 315 ASP n 
1 316 ALA n 
1 317 LYS n 
1 318 VAL n 
1 319 THR n 
1 320 TYR n 
1 321 GLU n 
1 322 LEU n 
1 323 GLY n 
1 324 LYS n 
1 325 GLU n 
1 326 PHE n 
1 327 LEU n 
1 328 PRO n 
1 329 MET n 
1 330 GLU n 
1 331 ALA n 
1 332 GLN n 
1 333 LEU n 
1 334 SER n 
1 335 ARG n 
1 336 LEU n 
1 337 ILE n 
1 338 GLY n 
1 339 GLN n 
1 340 SER n 
1 341 LEU n 
1 342 TRP n 
1 343 ASP n 
1 344 VAL n 
1 345 SER n 
1 346 ARG n 
1 347 SER n 
1 348 SER n 
1 349 THR n 
1 350 GLY n 
1 351 ASN n 
1 352 LEU n 
1 353 VAL n 
1 354 GLU n 
1 355 TRP n 
1 356 PHE n 
1 357 LEU n 
1 358 LEU n 
1 359 ARG n 
1 360 LYS n 
1 361 ALA n 
1 362 TYR n 
1 363 GLU n 
1 364 ARG n 
1 365 ASN n 
1 366 GLU n 
1 367 LEU n 
1 368 ALA n 
1 369 PRO n 
1 370 ASN n 
1 371 LYS n 
1 372 PRO n 
1 373 ASP n 
1 374 GLU n 
1 375 LYS n 
1 376 GLU n 
1 377 LEU n 
1 378 ALA n 
1 379 ARG n 
1 380 ARG n 
1 381 ARG n 
1 382 GLN n 
1 383 LYS n 
1 384 TYR n 
1 385 GLU n 
1 386 GLY n 
1 387 GLY n 
1 388 TYR n 
1 389 VAL n 
1 390 LYS n 
1 391 GLU n 
1 392 PRO n 
1 393 GLU n 
1 394 ARG n 
1 395 GLY n 
1 396 LEU n 
1 397 TRP n 
1 398 GLU n 
1 399 ASN n 
1 400 ILE n 
1 401 VAL n 
1 402 TYR n 
1 403 LEU n 
1 404 ASP n 
1 405 PHE n 
1 406 ARG n 
1 407 SER n 
1 408 LEU n 
1 409 TYR n 
1 410 PRO n 
1 411 SER n 
1 412 ILE n 
1 413 ILE n 
1 414 ILE n 
1 415 THR n 
1 416 HIS n 
1 417 ASN n 
1 418 VAL n 
1 419 SER n 
1 420 PRO n 
1 421 ASP n 
1 422 THR n 
1 423 LEU n 
1 424 ASN n 
1 425 ARG n 
1 426 GLU n 
1 427 GLY n 
1 428 CYS n 
1 429 GLY n 
1 430 GLU n 
1 431 TYR n 
1 432 ASP n 
1 433 VAL n 
1 434 ALA n 
1 435 PRO n 
1 436 GLN n 
1 437 VAL n 
1 438 GLY n 
1 439 HIS n 
1 440 ARG n 
1 441 PHE n 
1 442 CYS n 
1 443 LYS n 
1 444 ASP n 
1 445 LEU n 
1 446 PRO n 
1 447 GLY n 
1 448 PHE n 
1 449 ILE n 
1 450 PRO n 
1 451 SER n 
1 452 LEU n 
1 453 LEU n 
1 454 GLY n 
1 455 ASP n 
1 456 LEU n 
1 457 LEU n 
1 458 GLU n 
1 459 GLU n 
1 460 ARG n 
1 461 GLN n 
1 462 LYS n 
1 463 ILE n 
1 464 LYS n 
1 465 LYS n 
1 466 LYS n 
1 467 MET n 
1 468 LYS n 
1 469 ALA n 
1 470 THR n 
1 471 ILE n 
1 472 ASP n 
1 473 PRO n 
1 474 ILE n 
1 475 GLU n 
1 476 ARG n 
1 477 LYS n 
1 478 LEU n 
1 479 LEU n 
1 480 ASP n 
1 481 TYR n 
1 482 ARG n 
1 483 GLN n 
1 484 ARG n 
1 485 LEU n 
1 486 ILE n 
1 487 LYS n 
1 488 ILE n 
1 489 LEU n 
1 490 ALA n 
1 491 ASN n 
1 492 SER n 
1 493 VAL n 
1 494 TYR n 
1 495 GLY n 
1 496 HIS n 
1 497 MET n 
1 498 GLY n 
1 499 PHE n 
1 500 GLU n 
1 501 ASN n 
1 502 ALA n 
1 503 ARG n 
1 504 TRP n 
1 505 TYR n 
1 506 CYS n 
1 507 LYS n 
1 508 GLU n 
1 509 CYS n 
1 510 ALA n 
1 511 GLU n 
1 512 SER n 
1 513 VAL n 
1 514 THR n 
1 515 ALA n 
1 516 TRP n 
1 517 GLY n 
1 518 ARG n 
1 519 GLU n 
1 520 TYR n 
1 521 LEU n 
1 522 THR n 
1 523 MET n 
1 524 THR n 
1 525 ILE n 
1 526 LYS n 
1 527 GLU n 
1 528 ILE n 
1 529 GLU n 
1 530 GLU n 
1 531 LYS n 
1 532 TYR n 
1 533 GLY n 
1 534 PHE n 
1 535 LYS n 
1 536 VAL n 
1 537 ILE n 
1 538 TYR n 
1 539 SER n 
1 540 ASP n 
1 541 THR n 
1 542 ASP n 
1 543 GLY n 
1 544 PHE n 
1 545 PHE n 
1 546 ALA n 
1 547 THR n 
1 548 ILE n 
1 549 PRO n 
1 550 GLY n 
1 551 ALA n 
1 552 ASP n 
1 553 ALA n 
1 554 GLU n 
1 555 THR n 
1 556 VAL n 
1 557 LYS n 
1 558 LYS n 
1 559 LYS n 
1 560 ALA n 
1 561 MET n 
1 562 GLU n 
1 563 PHE n 
1 564 LEU n 
1 565 LYS n 
1 566 TYR n 
1 567 ILE n 
1 568 ASN n 
1 569 ALA n 
1 570 LYS n 
1 571 LEU n 
1 572 PRO n 
1 573 GLY n 
1 574 ALA n 
1 575 LEU n 
1 576 GLU n 
1 577 LEU n 
1 578 GLU n 
1 579 TYR n 
1 580 GLU n 
1 581 GLY n 
1 582 PHE n 
1 583 TYR n 
1 584 LYS n 
1 585 ARG n 
1 586 GLY n 
1 587 PHE n 
1 588 PHE n 
1 589 VAL n 
1 590 THR n 
1 591 LYS n 
1 592 LYS n 
1 593 LYS n 
1 594 TYR n 
1 595 ALA n 
1 596 VAL n 
1 597 ILE n 
1 598 ASP n 
1 599 GLU n 
1 600 GLU n 
1 601 GLY n 
1 602 LYS n 
1 603 ILE n 
1 604 THR n 
1 605 THR n 
1 606 ARG n 
1 607 GLY n 
1 608 LEU n 
1 609 GLU n 
1 610 ILE n 
1 611 VAL n 
1 612 ARG n 
1 613 ARG n 
1 614 ASP n 
1 615 TRP n 
1 616 SER n 
1 617 GLU n 
1 618 ILE n 
1 619 ALA n 
1 620 LYS n 
1 621 GLU n 
1 622 THR n 
1 623 GLN n 
1 624 ALA n 
1 625 ARG n 
1 626 VAL n 
1 627 LEU n 
1 628 GLU n 
1 629 ALA n 
1 630 LEU n 
1 631 LEU n 
1 632 LYS n 
1 633 ASP n 
1 634 GLY n 
1 635 ASP n 
1 636 VAL n 
1 637 GLU n 
1 638 LYS n 
1 639 ALA n 
1 640 VAL n 
1 641 ARG n 
1 642 ILE n 
1 643 VAL n 
1 644 LYS n 
1 645 GLU n 
1 646 VAL n 
1 647 THR n 
1 648 GLU n 
1 649 LYS n 
1 650 LEU n 
1 651 SER n 
1 652 LYS n 
1 653 TYR n 
1 654 GLU n 
1 655 VAL n 
1 656 PRO n 
1 657 PRO n 
1 658 GLU n 
1 659 LYS n 
1 660 LEU n 
1 661 VAL n 
1 662 ILE n 
1 663 HIS n 
1 664 LYS n 
1 665 GLN n 
1 666 ILE n 
1 667 THR n 
1 668 ARG n 
1 669 ASP n 
1 670 LEU n 
1 671 LYS n 
1 672 ASP n 
1 673 TYR n 
1 674 LYS n 
1 675 ALA n 
1 676 THR n 
1 677 GLY n 
1 678 PRO n 
1 679 HIS n 
1 680 VAL n 
1 681 ALA n 
1 682 VAL n 
1 683 ALA n 
1 684 LYS n 
1 685 ARG n 
1 686 LEU n 
1 687 ALA n 
1 688 ALA n 
1 689 ARG n 
1 690 GLY n 
1 691 VAL n 
1 692 LYS n 
1 693 ILE n 
1 694 ARG n 
1 695 PRO n 
1 696 GLY n 
1 697 THR n 
1 698 VAL n 
1 699 ILE n 
1 700 SER n 
1 701 TYR n 
1 702 ILE n 
1 703 VAL n 
1 704 LEU n 
1 705 LYS n 
1 706 GLY n 
1 707 SER n 
1 708 GLY n 
1 709 ARG n 
1 710 ILE n 
1 711 GLY n 
1 712 ASP n 
1 713 ARG n 
1 714 ALA n 
1 715 ILE n 
1 716 PRO n 
1 717 PHE n 
1 718 ASP n 
1 719 GLU n 
1 720 PHE n 
1 721 ASP n 
1 722 PRO n 
1 723 THR n 
1 724 LYS n 
1 725 HIS n 
1 726 ARG n 
1 727 TYR n 
1 728 ASP n 
1 729 ALA n 
1 730 GLU n 
1 731 TYR n 
1 732 TYR n 
1 733 ILE n 
1 734 GLU n 
1 735 LYS n 
1 736 GLN n 
1 737 VAL n 
1 738 LEU n 
1 739 PRO n 
1 740 ALA n 
1 741 VAL n 
1 742 GLU n 
1 743 ARG n 
1 744 ILE n 
1 745 LEU n 
1 746 ARG n 
1 747 ALA n 
1 748 PHE n 
1 749 GLY n 
1 750 TYR n 
1 751 ARG n 
1 752 LYS n 
1 753 GLU n 
1 754 ASP n 
1 755 LEU n 
1 756 ARG n 
1 757 TYR n 
1 758 GLN n 
1 759 LYS n 
1 760 THR n 
1 761 ARG n 
1 762 GLN n 
1 763 VAL n 
1 764 GLY n 
1 765 LEU n 
1 766 SER n 
1 767 ALA n 
1 768 TRP n 
1 769 LEU n 
1 770 LYS n 
1 771 PRO n 
1 772 LYS n 
1 773 GLY n 
1 774 THR n 
2 1   DG  n 
2 2   DA  n 
2 3   DC  n 
2 4   DC  n 
2 5   DA  n 
2 6   DC  n 
2 7   DG  n 
2 8   DG  n 
2 9   DC  n 
2 10  DC  n 
2 11  DA  n 
2 12  DC  n 
2 13  DA  n 
3 1   DA  n 
3 2   DA  n 
3 3   DC  n 
3 4   DT  n 
3 5   DG  n 
3 6   DT  n 
3 7   DG  n 
3 8   DG  n 
3 9   DC  n 
3 10  DC  n 
3 11  DG  n 
3 12  DT  n 
3 13  DG  n 
3 14  DG  n 
3 15  DT  n 
3 16  DC  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                   774 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Thermococcus kodakarensis KOD1' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     69014 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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 13 'synthetic construct' ? 32630 ? 
3 1 sample 1 16 'synthetic construct' ? 32630 ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                                      ? 
'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                                                                                     ? 
'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                                   ? 
'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                              ? 
'C4 H7 N O4'        133.103 
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 
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  
GOL non-polymer         . GLYCEROL                                                                                     
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'          92.094  
HIS 'L-peptide linking' y HISTIDINE                                                                                    ? 
'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                                                                                        ? 'H2 O' 
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                   ? 
'C6 H13 N O2'       131.173 
IMD non-polymer         . IMIDAZOLE                                                                                    ? 
'C3 H5 N2 1'        69.085  
LEU 'L-peptide linking' y LEUCINE                                                                                      ? 
'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                                                                                       ? 
'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                                                                                   ? 
'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'                                                                              ? 'Mg 2' 
24.305  
MN  non-polymer         . 'MANGANESE (II) ION'                                                                         ? 'Mn 2' 
54.938  
PHE 'L-peptide linking' y PHENYLALANINE                                                                                ? 
'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                                                                                      ? 
'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                                                                                       ? 
'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                                                                                    ? 
'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                   ? 
'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                     ? 
'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                                                                                       ? 
'C5 H11 N O2'       117.146 
XG4 non-polymer         . "2'-deoxy-5'-O-[(R)-hydroxy{[(R)-hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl]guanosine" ? 
'C10 H17 N6 O12 P3' 506.196 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   ILE 2   2   2   ILE ILE A . n 
A 1 3   LEU 3   3   3   LEU LEU A . n 
A 1 4   ASP 4   4   4   ASP ASP A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   ASP 6   6   6   ASP ASP A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   ILE 8   8   8   ILE ILE A . n 
A 1 9   THR 9   9   9   THR THR A . n 
A 1 10  GLU 10  10  10  GLU GLU A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  LYS 13  13  13  LYS LYS A . n 
A 1 14  PRO 14  14  14  PRO PRO A . n 
A 1 15  VAL 15  15  15  VAL VAL A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  ARG 17  17  17  ARG ARG A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  PHE 19  19  19  PHE PHE A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  LYS 21  21  21  LYS LYS A . n 
A 1 22  GLU 22  22  22  GLU GLU A . n 
A 1 23  ASN 23  23  23  ASN ASN A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  LYS 27  27  27  LYS LYS A . n 
A 1 28  ILE 28  28  28  ILE ILE A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  TYR 30  30  30  TYR TYR A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  ARG 32  32  32  ARG ARG A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  PHE 34  34  34  PHE PHE A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  PHE 38  38  38  PHE PHE A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ALA 40  40  40  ALA ALA A . n 
A 1 41  LEU 41  41  41  LEU LEU A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  LYS 43  43  43  LYS LYS A . n 
A 1 44  ASP 44  44  44  ASP ASP A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  ILE 48  48  48  ILE ILE A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  LYS 52  52  52  LYS LYS A . n 
A 1 53  LYS 53  53  53  LYS LYS A . n 
A 1 54  ILE 54  54  54  ILE ILE A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  HIS 59  59  59  HIS HIS A . n 
A 1 60  GLY 60  60  60  GLY GLY A . n 
A 1 61  THR 61  61  61  THR THR A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  LYS 66  66  66  LYS LYS A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  GLN 72  72  72  GLN GLN A . n 
A 1 73  LYS 73  73  73  LYS LYS A . n 
A 1 74  LYS 74  74  74  LYS LYS A . n 
A 1 75  PHE 75  75  75  PHE PHE A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  ARG 78  78  78  ARG ARG A . n 
A 1 79  PRO 79  79  79  PRO PRO A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  GLU 81  81  81  GLU GLU A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  TRP 83  83  83  TRP TRP A . n 
A 1 84  LYS 84  84  84  LYS LYS A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  TYR 86  86  86  TYR TYR A . n 
A 1 87  PHE 87  87  87  PHE PHE A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  HIS 89  89  89  HIS HIS A . n 
A 1 90  PRO 90  90  90  PRO PRO A . n 
A 1 91  GLN 91  91  91  GLN GLN A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLN 93  93  93  GLN GLN A . n 
A 1 94  PRO 94  94  94  PRO PRO A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  ARG 97  97  97  ARG ARG A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 ARG 101 101 101 ARG ARG A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 HIS 103 103 103 HIS HIS A . n 
A 1 104 PRO 104 104 104 PRO PRO A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 ASP 108 108 108 ASP ASP A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 TYR 110 110 110 TYR TYR A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 TYR 112 112 112 TYR TYR A . n 
A 1 113 ASP 113 113 113 ASP ASP A . n 
A 1 114 THR 114 114 114 THR THR A . n 
A 1 115 PRO 115 115 115 PRO PRO A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 ARG 119 119 119 ARG ARG A . n 
A 1 120 TYR 120 120 120 TYR TYR A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 ASP 123 123 123 ASP ASP A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 PRO 128 128 128 PRO PRO A . n 
A 1 129 MET 129 129 129 MET MET A . n 
A 1 130 GLU 130 130 130 GLU GLU A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 ASP 132 132 132 ASP ASP A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 GLU 134 134 134 GLU GLU A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 MET 137 137 137 MET MET A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 ALA 139 139 139 ALA ALA A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 THR 144 144 144 THR THR A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 TYR 146 146 146 TYR TYR A . n 
A 1 147 HIS 147 147 147 HIS HIS A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 GLU 150 150 150 GLU GLU A . n 
A 1 151 GLU 151 151 151 GLU GLU A . n 
A 1 152 PHE 152 152 152 PHE PHE A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 GLU 154 154 154 GLU GLU A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 PRO 156 156 156 PRO PRO A . n 
A 1 157 ILE 157 157 157 ILE ILE A . n 
A 1 158 LEU 158 158 158 LEU LEU A . n 
A 1 159 MET 159 159 159 MET MET A . n 
A 1 160 ILE 160 160 160 ILE ILE A . n 
A 1 161 SER 161 161 161 SER SER A . n 
A 1 162 TYR 162 162 162 TYR TYR A . n 
A 1 163 ALA 163 163 163 ALA ALA A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 GLU 165 165 165 GLU GLU A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 ARG 169 169 169 ARG ARG A . n 
A 1 170 VAL 170 170 170 VAL VAL A . n 
A 1 171 ILE 171 171 171 ILE ILE A . n 
A 1 172 THR 172 172 172 THR THR A . n 
A 1 173 TRP 173 173 173 TRP TRP A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 ASN 175 175 175 ASN ASN A . n 
A 1 176 VAL 176 176 176 VAL VAL A . n 
A 1 177 ASP 177 177 177 ASP ASP A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 PRO 179 179 179 PRO PRO A . n 
A 1 180 TYR 180 180 180 TYR TYR A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 ASP 182 182 182 ASP ASP A . n 
A 1 183 VAL 183 183 183 VAL VAL A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 THR 186 186 186 THR THR A . n 
A 1 187 GLU 187 187 187 GLU GLU A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 MET 190 190 190 MET MET A . n 
A 1 191 ILE 191 191 191 ILE ILE A . n 
A 1 192 LYS 192 192 192 LYS LYS A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 PHE 194 194 194 PHE PHE A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 ARG 196 196 196 ARG ARG A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 VAL 198 198 198 VAL VAL A . n 
A 1 199 LYS 199 199 199 LYS LYS A . n 
A 1 200 GLU 200 200 200 GLU GLU A . n 
A 1 201 LYS 201 201 201 LYS LYS A . n 
A 1 202 ASP 202 202 202 ASP ASP A . n 
A 1 203 PRO 203 203 203 PRO PRO A . n 
A 1 204 ASP 204 204 204 ASP ASP A . n 
A 1 205 VAL 205 205 205 VAL VAL A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 ILE 207 207 207 ILE ILE A . n 
A 1 208 THR 208 208 208 THR THR A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ASN 210 210 210 ASN ASN A . n 
A 1 211 GLY 211 211 211 GLY GLY A . n 
A 1 212 ASP 212 212 212 ASP ASP A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 PHE 214 214 214 PHE PHE A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 PHE 216 216 216 PHE PHE A . n 
A 1 217 ALA 217 217 217 ALA ALA A . n 
A 1 218 TYR 218 218 218 TYR TYR A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 LYS 220 220 220 LYS LYS A . n 
A 1 221 LYS 221 221 221 LYS LYS A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 CYS 223 223 223 CYS CYS A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 LYS 225 225 225 LYS LYS A . n 
A 1 226 LEU 226 226 226 LEU LEU A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 ILE 228 228 228 ILE ILE A . n 
A 1 229 ASN 229 229 229 ASN ASN A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ALA 231 231 231 ALA ALA A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 GLY 233 233 233 GLY GLY A . n 
A 1 234 ARG 234 234 234 ARG ARG A . n 
A 1 235 ASP 235 235 235 ASP ASP A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 SER 237 237 237 SER SER A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 ILE 241 241 241 ILE ILE A . n 
A 1 242 GLN 242 242 242 GLN GLN A . n 
A 1 243 ARG 243 243 243 ARG ARG A . n 
A 1 244 MET 244 244 244 MET MET A . n 
A 1 245 GLY 245 245 245 GLY GLY A . n 
A 1 246 ASP 246 246 246 ASP ASP A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 GLU 251 251 251 GLU GLU A . n 
A 1 252 VAL 252 252 252 VAL VAL A . n 
A 1 253 LYS 253 253 253 LYS LYS A . n 
A 1 254 GLY 254 254 254 GLY GLY A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 ILE 256 256 256 ILE ILE A . n 
A 1 257 HIS 257 257 257 HIS HIS A . n 
A 1 258 PHE 258 258 258 PHE PHE A . n 
A 1 259 ASP 259 259 259 ASP ASP A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 TYR 261 261 261 TYR TYR A . n 
A 1 262 PRO 262 262 262 PRO PRO A . n 
A 1 263 VAL 263 263 263 VAL VAL A . n 
A 1 264 ILE 264 264 264 ILE ILE A . n 
A 1 265 ARG 265 265 265 ARG ARG A . n 
A 1 266 ARG 266 266 266 ARG ARG A . n 
A 1 267 THR 267 267 267 THR THR A . n 
A 1 268 ILE 268 268 268 ILE ILE A . n 
A 1 269 ASN 269 269 269 ASN ASN A . n 
A 1 270 LEU 270 270 270 LEU LEU A . n 
A 1 271 PRO 271 271 271 PRO PRO A . n 
A 1 272 THR 272 272 272 THR THR A . n 
A 1 273 TYR 273 273 273 TYR TYR A . n 
A 1 274 THR 274 274 274 THR THR A . n 
A 1 275 LEU 275 275 275 LEU LEU A . n 
A 1 276 GLU 276 276 276 GLU GLU A . n 
A 1 277 ALA 277 277 277 ALA ALA A . n 
A 1 278 VAL 278 278 278 VAL VAL A . n 
A 1 279 TYR 279 279 279 TYR TYR A . n 
A 1 280 GLU 280 280 280 GLU GLU A . n 
A 1 281 ALA 281 281 281 ALA ALA A . n 
A 1 282 VAL 282 282 282 VAL VAL A . n 
A 1 283 PHE 283 283 283 PHE PHE A . n 
A 1 284 GLY 284 284 284 GLY GLY A . n 
A 1 285 GLN 285 285 285 GLN GLN A . n 
A 1 286 PRO 286 286 286 PRO PRO A . n 
A 1 287 LYS 287 287 287 LYS LYS A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 LYS 289 289 289 LYS LYS A . n 
A 1 290 VAL 290 290 290 VAL VAL A . n 
A 1 291 TYR 291 291 291 TYR TYR A . n 
A 1 292 ALA 292 292 292 ALA ALA A . n 
A 1 293 GLU 293 293 293 GLU GLU A . n 
A 1 294 GLU 294 294 294 GLU GLU A . n 
A 1 295 ILE 295 295 295 ILE ILE A . n 
A 1 296 THR 296 296 296 THR THR A . n 
A 1 297 THR 297 297 297 THR THR A . n 
A 1 298 ALA 298 298 298 ALA ALA A . n 
A 1 299 TRP 299 299 299 TRP TRP A . n 
A 1 300 GLU 300 300 300 GLU GLU A . n 
A 1 301 THR 301 301 301 THR THR A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 GLU 303 303 303 GLU GLU A . n 
A 1 304 ASN 304 304 304 ASN ASN A . n 
A 1 305 LEU 305 305 305 LEU LEU A . n 
A 1 306 GLU 306 306 306 GLU GLU A . n 
A 1 307 ARG 307 307 307 ARG ARG A . n 
A 1 308 VAL 308 308 308 VAL VAL A . n 
A 1 309 ALA 309 309 309 ALA ALA A . n 
A 1 310 ARG 310 310 310 ARG ARG A . n 
A 1 311 TYR 311 311 311 TYR TYR A . n 
A 1 312 SER 312 312 312 SER SER A . n 
A 1 313 MET 313 313 313 MET MET A . n 
A 1 314 GLU 314 314 314 GLU GLU A . n 
A 1 315 ASP 315 315 315 ASP ASP A . n 
A 1 316 ALA 316 316 316 ALA ALA A . n 
A 1 317 LYS 317 317 317 LYS LYS A . n 
A 1 318 VAL 318 318 318 VAL VAL A . n 
A 1 319 THR 319 319 319 THR THR A . n 
A 1 320 TYR 320 320 320 TYR TYR A . n 
A 1 321 GLU 321 321 321 GLU GLU A . n 
A 1 322 LEU 322 322 322 LEU LEU A . n 
A 1 323 GLY 323 323 323 GLY GLY A . n 
A 1 324 LYS 324 324 324 LYS LYS A . n 
A 1 325 GLU 325 325 325 GLU GLU A . n 
A 1 326 PHE 326 326 326 PHE PHE A . n 
A 1 327 LEU 327 327 327 LEU LEU A . n 
A 1 328 PRO 328 328 328 PRO PRO A . n 
A 1 329 MET 329 329 329 MET MET A . n 
A 1 330 GLU 330 330 330 GLU GLU A . n 
A 1 331 ALA 331 331 331 ALA ALA A . n 
A 1 332 GLN 332 332 332 GLN GLN A . n 
A 1 333 LEU 333 333 333 LEU LEU A . n 
A 1 334 SER 334 334 334 SER SER A . n 
A 1 335 ARG 335 335 335 ARG ARG A . n 
A 1 336 LEU 336 336 336 LEU LEU A . n 
A 1 337 ILE 337 337 337 ILE ILE A . n 
A 1 338 GLY 338 338 338 GLY GLY A . n 
A 1 339 GLN 339 339 339 GLN GLN A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 LEU 341 341 341 LEU LEU A . n 
A 1 342 TRP 342 342 342 TRP TRP A . n 
A 1 343 ASP 343 343 343 ASP ASP A . n 
A 1 344 VAL 344 344 344 VAL VAL A . n 
A 1 345 SER 345 345 345 SER SER A . n 
A 1 346 ARG 346 346 346 ARG ARG A . n 
A 1 347 SER 347 347 347 SER SER A . n 
A 1 348 SER 348 348 348 SER SER A . n 
A 1 349 THR 349 349 349 THR THR A . n 
A 1 350 GLY 350 350 350 GLY GLY A . n 
A 1 351 ASN 351 351 351 ASN ASN A . n 
A 1 352 LEU 352 352 352 LEU LEU A . n 
A 1 353 VAL 353 353 353 VAL VAL A . n 
A 1 354 GLU 354 354 354 GLU GLU A . n 
A 1 355 TRP 355 355 355 TRP TRP A . n 
A 1 356 PHE 356 356 356 PHE PHE A . n 
A 1 357 LEU 357 357 357 LEU LEU A . n 
A 1 358 LEU 358 358 358 LEU LEU A . n 
A 1 359 ARG 359 359 359 ARG ARG A . n 
A 1 360 LYS 360 360 360 LYS LYS A . n 
A 1 361 ALA 361 361 361 ALA ALA A . n 
A 1 362 TYR 362 362 362 TYR TYR A . n 
A 1 363 GLU 363 363 363 GLU GLU A . n 
A 1 364 ARG 364 364 364 ARG ARG A . n 
A 1 365 ASN 365 365 365 ASN ASN A . n 
A 1 366 GLU 366 366 366 GLU GLU A . n 
A 1 367 LEU 367 367 367 LEU LEU A . n 
A 1 368 ALA 368 368 368 ALA ALA A . n 
A 1 369 PRO 369 369 369 PRO PRO A . n 
A 1 370 ASN 370 370 370 ASN ASN A . n 
A 1 371 LYS 371 371 371 LYS LYS A . n 
A 1 372 PRO 372 372 372 PRO PRO A . n 
A 1 373 ASP 373 373 373 ASP ASP A . n 
A 1 374 GLU 374 374 374 GLU GLU A . n 
A 1 375 LYS 375 375 375 LYS LYS A . n 
A 1 376 GLU 376 376 376 GLU GLU A . n 
A 1 377 LEU 377 377 377 LEU LEU A . n 
A 1 378 ALA 378 378 378 ALA ALA A . n 
A 1 379 ARG 379 379 379 ARG ARG A . n 
A 1 380 ARG 380 380 380 ARG ARG A . n 
A 1 381 ARG 381 381 381 ARG ARG A . n 
A 1 382 GLN 382 382 382 GLN GLN A . n 
A 1 383 LYS 383 383 383 LYS LYS A . n 
A 1 384 TYR 384 384 384 TYR TYR A . n 
A 1 385 GLU 385 385 385 GLU GLU A . n 
A 1 386 GLY 386 386 386 GLY GLY A . n 
A 1 387 GLY 387 387 387 GLY GLY A . n 
A 1 388 TYR 388 388 388 TYR TYR A . n 
A 1 389 VAL 389 389 389 VAL VAL A . n 
A 1 390 LYS 390 390 390 LYS LYS A . n 
A 1 391 GLU 391 391 391 GLU GLU A . n 
A 1 392 PRO 392 392 392 PRO PRO A . n 
A 1 393 GLU 393 393 393 GLU GLU A . n 
A 1 394 ARG 394 394 394 ARG ARG A . n 
A 1 395 GLY 395 395 395 GLY GLY A . n 
A 1 396 LEU 396 396 396 LEU LEU A . n 
A 1 397 TRP 397 397 397 TRP TRP A . n 
A 1 398 GLU 398 398 398 GLU GLU A . n 
A 1 399 ASN 399 399 399 ASN ASN A . n 
A 1 400 ILE 400 400 400 ILE ILE A . n 
A 1 401 VAL 401 401 401 VAL VAL A . n 
A 1 402 TYR 402 402 402 TYR TYR A . n 
A 1 403 LEU 403 403 403 LEU LEU A . n 
A 1 404 ASP 404 404 404 ASP ASP A . n 
A 1 405 PHE 405 405 405 PHE PHE A . n 
A 1 406 ARG 406 406 406 ARG ARG A . n 
A 1 407 SER 407 407 407 SER SER A . n 
A 1 408 LEU 408 408 408 LEU LEU A . n 
A 1 409 TYR 409 409 409 TYR TYR A . n 
A 1 410 PRO 410 410 410 PRO PRO A . n 
A 1 411 SER 411 411 411 SER SER A . n 
A 1 412 ILE 412 412 412 ILE ILE A . n 
A 1 413 ILE 413 413 413 ILE ILE A . n 
A 1 414 ILE 414 414 414 ILE ILE A . n 
A 1 415 THR 415 415 415 THR THR A . n 
A 1 416 HIS 416 416 416 HIS HIS A . n 
A 1 417 ASN 417 417 417 ASN ASN A . n 
A 1 418 VAL 418 418 418 VAL VAL A . n 
A 1 419 SER 419 419 419 SER SER A . n 
A 1 420 PRO 420 420 420 PRO PRO A . n 
A 1 421 ASP 421 421 421 ASP ASP A . n 
A 1 422 THR 422 422 422 THR THR A . n 
A 1 423 LEU 423 423 423 LEU LEU A . n 
A 1 424 ASN 424 424 424 ASN ASN A . n 
A 1 425 ARG 425 425 425 ARG ARG A . n 
A 1 426 GLU 426 426 426 GLU GLU A . n 
A 1 427 GLY 427 427 427 GLY GLY A . n 
A 1 428 CYS 428 428 428 CYS CYS A . n 
A 1 429 GLY 429 429 429 GLY GLY A . n 
A 1 430 GLU 430 430 430 GLU GLU A . n 
A 1 431 TYR 431 431 431 TYR TYR A . n 
A 1 432 ASP 432 432 432 ASP ASP A . n 
A 1 433 VAL 433 433 433 VAL VAL A . n 
A 1 434 ALA 434 434 434 ALA ALA A . n 
A 1 435 PRO 435 435 435 PRO PRO A . n 
A 1 436 GLN 436 436 436 GLN GLN A . n 
A 1 437 VAL 437 437 437 VAL VAL A . n 
A 1 438 GLY 438 438 438 GLY GLY A . n 
A 1 439 HIS 439 439 439 HIS HIS A . n 
A 1 440 ARG 440 440 440 ARG ARG A . n 
A 1 441 PHE 441 441 441 PHE PHE A . n 
A 1 442 CYS 442 442 442 CYS CYS A . n 
A 1 443 LYS 443 443 443 LYS LYS A . n 
A 1 444 ASP 444 444 444 ASP ASP A . n 
A 1 445 LEU 445 445 445 LEU LEU A . n 
A 1 446 PRO 446 446 446 PRO PRO A . n 
A 1 447 GLY 447 447 447 GLY GLY A . n 
A 1 448 PHE 448 448 448 PHE PHE A . n 
A 1 449 ILE 449 449 449 ILE ILE A . n 
A 1 450 PRO 450 450 450 PRO PRO A . n 
A 1 451 SER 451 451 451 SER SER A . n 
A 1 452 LEU 452 452 452 LEU LEU A . n 
A 1 453 LEU 453 453 453 LEU LEU A . n 
A 1 454 GLY 454 454 454 GLY GLY A . n 
A 1 455 ASP 455 455 455 ASP ASP A . n 
A 1 456 LEU 456 456 456 LEU LEU A . n 
A 1 457 LEU 457 457 457 LEU LEU A . n 
A 1 458 GLU 458 458 458 GLU GLU A . n 
A 1 459 GLU 459 459 459 GLU GLU A . n 
A 1 460 ARG 460 460 460 ARG ARG A . n 
A 1 461 GLN 461 461 461 GLN GLN A . n 
A 1 462 LYS 462 462 462 LYS LYS A . n 
A 1 463 ILE 463 463 463 ILE ILE A . n 
A 1 464 LYS 464 464 464 LYS LYS A . n 
A 1 465 LYS 465 465 465 LYS LYS A . n 
A 1 466 LYS 466 466 466 LYS LYS A . n 
A 1 467 MET 467 467 467 MET MET A . n 
A 1 468 LYS 468 468 468 LYS LYS A . n 
A 1 469 ALA 469 469 469 ALA ALA A . n 
A 1 470 THR 470 470 470 THR THR A . n 
A 1 471 ILE 471 471 471 ILE ILE A . n 
A 1 472 ASP 472 472 472 ASP ASP A . n 
A 1 473 PRO 473 473 473 PRO PRO A . n 
A 1 474 ILE 474 474 474 ILE ILE A . n 
A 1 475 GLU 475 475 475 GLU GLU A . n 
A 1 476 ARG 476 476 476 ARG ARG A . n 
A 1 477 LYS 477 477 477 LYS LYS A . n 
A 1 478 LEU 478 478 478 LEU LEU A . n 
A 1 479 LEU 479 479 479 LEU LEU A . n 
A 1 480 ASP 480 480 480 ASP ASP A . n 
A 1 481 TYR 481 481 481 TYR TYR A . n 
A 1 482 ARG 482 482 482 ARG ARG A . n 
A 1 483 GLN 483 483 483 GLN GLN A . n 
A 1 484 ARG 484 484 484 ARG ARG A . n 
A 1 485 LEU 485 485 485 LEU LEU A . n 
A 1 486 ILE 486 486 486 ILE ILE A . n 
A 1 487 LYS 487 487 487 LYS LYS A . n 
A 1 488 ILE 488 488 488 ILE ILE A . n 
A 1 489 LEU 489 489 489 LEU LEU A . n 
A 1 490 ALA 490 490 490 ALA ALA A . n 
A 1 491 ASN 491 491 491 ASN ASN A . n 
A 1 492 SER 492 492 492 SER SER A . n 
A 1 493 VAL 493 493 493 VAL VAL A . n 
A 1 494 TYR 494 494 494 TYR TYR A . n 
A 1 495 GLY 495 495 495 GLY GLY A . n 
A 1 496 HIS 496 496 496 HIS HIS A . n 
A 1 497 MET 497 497 497 MET MET A . n 
A 1 498 GLY 498 498 498 GLY GLY A . n 
A 1 499 PHE 499 499 499 PHE PHE A . n 
A 1 500 GLU 500 500 500 GLU GLU A . n 
A 1 501 ASN 501 501 501 ASN ASN A . n 
A 1 502 ALA 502 502 502 ALA ALA A . n 
A 1 503 ARG 503 503 503 ARG ARG A . n 
A 1 504 TRP 504 504 504 TRP TRP A . n 
A 1 505 TYR 505 505 505 TYR TYR A . n 
A 1 506 CYS 506 506 506 CYS CYS A . n 
A 1 507 LYS 507 507 507 LYS LYS A . n 
A 1 508 GLU 508 508 508 GLU GLU A . n 
A 1 509 CYS 509 509 509 CYS CYS A . n 
A 1 510 ALA 510 510 510 ALA ALA A . n 
A 1 511 GLU 511 511 511 GLU GLU A . n 
A 1 512 SER 512 512 512 SER SER A . n 
A 1 513 VAL 513 513 513 VAL VAL A . n 
A 1 514 THR 514 514 514 THR THR A . n 
A 1 515 ALA 515 515 515 ALA ALA A . n 
A 1 516 TRP 516 516 516 TRP TRP A . n 
A 1 517 GLY 517 517 517 GLY GLY A . n 
A 1 518 ARG 518 518 518 ARG ARG A . n 
A 1 519 GLU 519 519 519 GLU GLU A . n 
A 1 520 TYR 520 520 520 TYR TYR A . n 
A 1 521 LEU 521 521 521 LEU LEU A . n 
A 1 522 THR 522 522 522 THR THR A . n 
A 1 523 MET 523 523 523 MET MET A . n 
A 1 524 THR 524 524 524 THR THR A . n 
A 1 525 ILE 525 525 525 ILE ILE A . n 
A 1 526 LYS 526 526 526 LYS LYS A . n 
A 1 527 GLU 527 527 527 GLU GLU A . n 
A 1 528 ILE 528 528 528 ILE ILE A . n 
A 1 529 GLU 529 529 529 GLU GLU A . n 
A 1 530 GLU 530 530 530 GLU GLU A . n 
A 1 531 LYS 531 531 531 LYS LYS A . n 
A 1 532 TYR 532 532 532 TYR TYR A . n 
A 1 533 GLY 533 533 533 GLY GLY A . n 
A 1 534 PHE 534 534 534 PHE PHE A . n 
A 1 535 LYS 535 535 535 LYS LYS A . n 
A 1 536 VAL 536 536 536 VAL VAL A . n 
A 1 537 ILE 537 537 537 ILE ILE A . n 
A 1 538 TYR 538 538 538 TYR TYR A . n 
A 1 539 SER 539 539 539 SER SER A . n 
A 1 540 ASP 540 540 540 ASP ASP A . n 
A 1 541 THR 541 541 541 THR THR A . n 
A 1 542 ASP 542 542 542 ASP ASP A . n 
A 1 543 GLY 543 543 543 GLY GLY A . n 
A 1 544 PHE 544 544 544 PHE PHE A . n 
A 1 545 PHE 545 545 545 PHE PHE A . n 
A 1 546 ALA 546 546 546 ALA ALA A . n 
A 1 547 THR 547 547 547 THR THR A . n 
A 1 548 ILE 548 548 548 ILE ILE A . n 
A 1 549 PRO 549 549 549 PRO PRO A . n 
A 1 550 GLY 550 550 550 GLY GLY A . n 
A 1 551 ALA 551 551 551 ALA ALA A . n 
A 1 552 ASP 552 552 552 ASP ASP A . n 
A 1 553 ALA 553 553 553 ALA ALA A . n 
A 1 554 GLU 554 554 554 GLU GLU A . n 
A 1 555 THR 555 555 555 THR THR A . n 
A 1 556 VAL 556 556 556 VAL VAL A . n 
A 1 557 LYS 557 557 557 LYS LYS A . n 
A 1 558 LYS 558 558 558 LYS LYS A . n 
A 1 559 LYS 559 559 559 LYS LYS A . n 
A 1 560 ALA 560 560 560 ALA ALA A . n 
A 1 561 MET 561 561 561 MET MET A . n 
A 1 562 GLU 562 562 562 GLU GLU A . n 
A 1 563 PHE 563 563 563 PHE PHE A . n 
A 1 564 LEU 564 564 564 LEU LEU A . n 
A 1 565 LYS 565 565 565 LYS LYS A . n 
A 1 566 TYR 566 566 566 TYR TYR A . n 
A 1 567 ILE 567 567 567 ILE ILE A . n 
A 1 568 ASN 568 568 568 ASN ASN A . n 
A 1 569 ALA 569 569 569 ALA ALA A . n 
A 1 570 LYS 570 570 570 LYS LYS A . n 
A 1 571 LEU 571 571 571 LEU LEU A . n 
A 1 572 PRO 572 572 572 PRO PRO A . n 
A 1 573 GLY 573 573 573 GLY GLY A . n 
A 1 574 ALA 574 574 574 ALA ALA A . n 
A 1 575 LEU 575 575 575 LEU LEU A . n 
A 1 576 GLU 576 576 576 GLU GLU A . n 
A 1 577 LEU 577 577 577 LEU LEU A . n 
A 1 578 GLU 578 578 578 GLU GLU A . n 
A 1 579 TYR 579 579 579 TYR TYR A . n 
A 1 580 GLU 580 580 580 GLU GLU A . n 
A 1 581 GLY 581 581 581 GLY GLY A . n 
A 1 582 PHE 582 582 582 PHE PHE A . n 
A 1 583 TYR 583 583 583 TYR TYR A . n 
A 1 584 LYS 584 584 584 LYS LYS A . n 
A 1 585 ARG 585 585 585 ARG ARG A . n 
A 1 586 GLY 586 586 586 GLY GLY A . n 
A 1 587 PHE 587 587 587 PHE PHE A . n 
A 1 588 PHE 588 588 588 PHE PHE A . n 
A 1 589 VAL 589 589 589 VAL VAL A . n 
A 1 590 THR 590 590 590 THR THR A . n 
A 1 591 LYS 591 591 591 LYS LYS A . n 
A 1 592 LYS 592 592 592 LYS LYS A . n 
A 1 593 LYS 593 593 593 LYS LYS A . n 
A 1 594 TYR 594 594 594 TYR TYR A . n 
A 1 595 ALA 595 595 595 ALA ALA A . n 
A 1 596 VAL 596 596 596 VAL VAL A . n 
A 1 597 ILE 597 597 597 ILE ILE A . n 
A 1 598 ASP 598 598 598 ASP ASP A . n 
A 1 599 GLU 599 599 599 GLU GLU A . n 
A 1 600 GLU 600 600 600 GLU GLU A . n 
A 1 601 GLY 601 601 601 GLY GLY A . n 
A 1 602 LYS 602 602 602 LYS LYS A . n 
A 1 603 ILE 603 603 603 ILE ILE A . n 
A 1 604 THR 604 604 604 THR THR A . n 
A 1 605 THR 605 605 605 THR THR A . n 
A 1 606 ARG 606 606 606 ARG ARG A . n 
A 1 607 GLY 607 607 607 GLY GLY A . n 
A 1 608 LEU 608 608 608 LEU LEU A . n 
A 1 609 GLU 609 609 609 GLU GLU A . n 
A 1 610 ILE 610 610 610 ILE ILE A . n 
A 1 611 VAL 611 611 611 VAL VAL A . n 
A 1 612 ARG 612 612 612 ARG ARG A . n 
A 1 613 ARG 613 613 613 ARG ARG A . n 
A 1 614 ASP 614 614 614 ASP ASP A . n 
A 1 615 TRP 615 615 615 TRP TRP A . n 
A 1 616 SER 616 616 616 SER SER A . n 
A 1 617 GLU 617 617 617 GLU GLU A . n 
A 1 618 ILE 618 618 618 ILE ILE A . n 
A 1 619 ALA 619 619 619 ALA ALA A . n 
A 1 620 LYS 620 620 620 LYS LYS A . n 
A 1 621 GLU 621 621 621 GLU GLU A . n 
A 1 622 THR 622 622 622 THR THR A . n 
A 1 623 GLN 623 623 623 GLN GLN A . n 
A 1 624 ALA 624 624 624 ALA ALA A . n 
A 1 625 ARG 625 625 625 ARG ARG A . n 
A 1 626 VAL 626 626 626 VAL VAL A . n 
A 1 627 LEU 627 627 627 LEU LEU A . n 
A 1 628 GLU 628 628 628 GLU GLU A . n 
A 1 629 ALA 629 629 629 ALA ALA A . n 
A 1 630 LEU 630 630 630 LEU LEU A . n 
A 1 631 LEU 631 631 631 LEU LEU A . n 
A 1 632 LYS 632 632 632 LYS LYS A . n 
A 1 633 ASP 633 633 633 ASP ASP A . n 
A 1 634 GLY 634 634 634 GLY GLY A . n 
A 1 635 ASP 635 635 635 ASP ASP A . n 
A 1 636 VAL 636 636 636 VAL VAL A . n 
A 1 637 GLU 637 637 637 GLU GLU A . n 
A 1 638 LYS 638 638 638 LYS LYS A . n 
A 1 639 ALA 639 639 639 ALA ALA A . n 
A 1 640 VAL 640 640 640 VAL VAL A . n 
A 1 641 ARG 641 641 641 ARG ARG A . n 
A 1 642 ILE 642 642 642 ILE ILE A . n 
A 1 643 VAL 643 643 643 VAL VAL A . n 
A 1 644 LYS 644 644 644 LYS LYS A . n 
A 1 645 GLU 645 645 645 GLU GLU A . n 
A 1 646 VAL 646 646 646 VAL VAL A . n 
A 1 647 THR 647 647 647 THR THR A . n 
A 1 648 GLU 648 648 648 GLU GLU A . n 
A 1 649 LYS 649 649 649 LYS LYS A . n 
A 1 650 LEU 650 650 650 LEU LEU A . n 
A 1 651 SER 651 651 651 SER SER A . n 
A 1 652 LYS 652 652 652 LYS LYS A . n 
A 1 653 TYR 653 653 653 TYR TYR A . n 
A 1 654 GLU 654 654 654 GLU GLU A . n 
A 1 655 VAL 655 655 655 VAL VAL A . n 
A 1 656 PRO 656 656 656 PRO PRO A . n 
A 1 657 PRO 657 657 657 PRO PRO A . n 
A 1 658 GLU 658 658 658 GLU GLU A . n 
A 1 659 LYS 659 659 659 LYS LYS A . n 
A 1 660 LEU 660 660 660 LEU LEU A . n 
A 1 661 VAL 661 661 661 VAL VAL A . n 
A 1 662 ILE 662 662 662 ILE ILE A . n 
A 1 663 HIS 663 663 663 HIS HIS A . n 
A 1 664 LYS 664 664 664 LYS LYS A . n 
A 1 665 GLN 665 665 665 GLN GLN A . n 
A 1 666 ILE 666 666 666 ILE ILE A . n 
A 1 667 THR 667 667 667 THR THR A . n 
A 1 668 ARG 668 668 668 ARG ARG A . n 
A 1 669 ASP 669 669 669 ASP ASP A . n 
A 1 670 LEU 670 670 670 LEU LEU A . n 
A 1 671 LYS 671 671 671 LYS LYS A . n 
A 1 672 ASP 672 672 672 ASP ASP A . n 
A 1 673 TYR 673 673 673 TYR TYR A . n 
A 1 674 LYS 674 674 674 LYS LYS A . n 
A 1 675 ALA 675 675 675 ALA ALA A . n 
A 1 676 THR 676 676 676 THR THR A . n 
A 1 677 GLY 677 677 677 GLY GLY A . n 
A 1 678 PRO 678 678 678 PRO PRO A . n 
A 1 679 HIS 679 679 679 HIS HIS A . n 
A 1 680 VAL 680 680 680 VAL VAL A . n 
A 1 681 ALA 681 681 681 ALA ALA A . n 
A 1 682 VAL 682 682 682 VAL VAL A . n 
A 1 683 ALA 683 683 683 ALA ALA A . n 
A 1 684 LYS 684 684 684 LYS LYS A . n 
A 1 685 ARG 685 685 685 ARG ARG A . n 
A 1 686 LEU 686 686 686 LEU LEU A . n 
A 1 687 ALA 687 687 687 ALA ALA A . n 
A 1 688 ALA 688 688 688 ALA ALA A . n 
A 1 689 ARG 689 689 689 ARG ARG A . n 
A 1 690 GLY 690 690 690 GLY GLY A . n 
A 1 691 VAL 691 691 691 VAL VAL A . n 
A 1 692 LYS 692 692 692 LYS LYS A . n 
A 1 693 ILE 693 693 693 ILE ILE A . n 
A 1 694 ARG 694 694 694 ARG ARG A . n 
A 1 695 PRO 695 695 695 PRO PRO A . n 
A 1 696 GLY 696 696 696 GLY GLY A . n 
A 1 697 THR 697 697 697 THR THR A . n 
A 1 698 VAL 698 698 698 VAL VAL A . n 
A 1 699 ILE 699 699 699 ILE ILE A . n 
A 1 700 SER 700 700 700 SER SER A . n 
A 1 701 TYR 701 701 701 TYR TYR A . n 
A 1 702 ILE 702 702 702 ILE ILE A . n 
A 1 703 VAL 703 703 703 VAL VAL A . n 
A 1 704 LEU 704 704 704 LEU LEU A . n 
A 1 705 LYS 705 705 705 LYS LYS A . n 
A 1 706 GLY 706 706 706 GLY GLY A . n 
A 1 707 SER 707 707 707 SER SER A . n 
A 1 708 GLY 708 708 708 GLY GLY A . n 
A 1 709 ARG 709 709 709 ARG ARG A . n 
A 1 710 ILE 710 710 710 ILE ILE A . n 
A 1 711 GLY 711 711 711 GLY GLY A . n 
A 1 712 ASP 712 712 712 ASP ASP A . n 
A 1 713 ARG 713 713 713 ARG ARG A . n 
A 1 714 ALA 714 714 714 ALA ALA A . n 
A 1 715 ILE 715 715 715 ILE ILE A . n 
A 1 716 PRO 716 716 716 PRO PRO A . n 
A 1 717 PHE 717 717 717 PHE PHE A . n 
A 1 718 ASP 718 718 718 ASP ASP A . n 
A 1 719 GLU 719 719 719 GLU GLU A . n 
A 1 720 PHE 720 720 720 PHE PHE A . n 
A 1 721 ASP 721 721 721 ASP ASP A . n 
A 1 722 PRO 722 722 722 PRO PRO A . n 
A 1 723 THR 723 723 723 THR THR A . n 
A 1 724 LYS 724 724 724 LYS LYS A . n 
A 1 725 HIS 725 725 725 HIS HIS A . n 
A 1 726 ARG 726 726 726 ARG ARG A . n 
A 1 727 TYR 727 727 727 TYR TYR A . n 
A 1 728 ASP 728 728 728 ASP ASP A . n 
A 1 729 ALA 729 729 729 ALA ALA A . n 
A 1 730 GLU 730 730 730 GLU GLU A . n 
A 1 731 TYR 731 731 731 TYR TYR A . n 
A 1 732 TYR 732 732 732 TYR TYR A . n 
A 1 733 ILE 733 733 733 ILE ILE A . n 
A 1 734 GLU 734 734 734 GLU GLU A . n 
A 1 735 LYS 735 735 735 LYS LYS A . n 
A 1 736 GLN 736 736 736 GLN GLN A . n 
A 1 737 VAL 737 737 737 VAL VAL A . n 
A 1 738 LEU 738 738 738 LEU LEU A . n 
A 1 739 PRO 739 739 739 PRO PRO A . n 
A 1 740 ALA 740 740 740 ALA ALA A . n 
A 1 741 VAL 741 741 741 VAL VAL A . n 
A 1 742 GLU 742 742 742 GLU GLU A . n 
A 1 743 ARG 743 743 743 ARG ARG A . n 
A 1 744 ILE 744 744 744 ILE ILE A . n 
A 1 745 LEU 745 745 745 LEU LEU A . n 
A 1 746 ARG 746 746 746 ARG ARG A . n 
A 1 747 ALA 747 747 747 ALA ALA A . n 
A 1 748 PHE 748 748 748 PHE PHE A . n 
A 1 749 GLY 749 749 749 GLY GLY A . n 
A 1 750 TYR 750 750 750 TYR TYR A . n 
A 1 751 ARG 751 751 751 ARG ARG A . n 
A 1 752 LYS 752 752 752 LYS LYS A . n 
A 1 753 GLU 753 753 753 GLU GLU A . n 
A 1 754 ASP 754 754 754 ASP ASP A . n 
A 1 755 LEU 755 755 755 LEU LEU A . n 
A 1 756 ARG 756 756 756 ARG ARG A . n 
A 1 757 TYR 757 757 ?   ?   ?   A . n 
A 1 758 GLN 758 758 ?   ?   ?   A . n 
A 1 759 LYS 759 759 ?   ?   ?   A . n 
A 1 760 THR 760 760 ?   ?   ?   A . n 
A 1 761 ARG 761 761 ?   ?   ?   A . n 
A 1 762 GLN 762 762 ?   ?   ?   A . n 
A 1 763 VAL 763 763 ?   ?   ?   A . n 
A 1 764 GLY 764 764 ?   ?   ?   A . n 
A 1 765 LEU 765 765 ?   ?   ?   A . n 
A 1 766 SER 766 766 ?   ?   ?   A . n 
A 1 767 ALA 767 767 ?   ?   ?   A . n 
A 1 768 TRP 768 768 ?   ?   ?   A . n 
A 1 769 LEU 769 769 ?   ?   ?   A . n 
A 1 770 LYS 770 770 ?   ?   ?   A . n 
A 1 771 PRO 771 771 ?   ?   ?   A . n 
A 1 772 LYS 772 772 ?   ?   ?   A . n 
A 1 773 GLY 773 773 ?   ?   ?   A . n 
A 1 774 THR 774 774 ?   ?   ?   A . n 
B 2 1   DG  1   1   1   DG  DG  P . n 
B 2 2   DA  2   2   2   DA  DA  P . n 
B 2 3   DC  3   3   3   DC  DC  P . n 
B 2 4   DC  4   4   4   DC  DC  P . n 
B 2 5   DA  5   5   5   DA  DA  P . n 
B 2 6   DC  6   6   6   DC  DC  P . n 
B 2 7   DG  7   7   7   DG  DG  P . n 
B 2 8   DG  8   8   8   DG  DG  P . n 
B 2 9   DC  9   9   9   DC  DC  P . n 
B 2 10  DC  10  10  10  DC  DC  P . n 
B 2 11  DA  11  11  11  DA  DA  P . n 
B 2 12  DC  12  12  12  DC  DC  P . n 
B 2 13  DA  13  13  13  DA  DA  P . n 
C 3 1   DA  1   1   ?   ?   ?   T . n 
C 3 2   DA  2   2   2   DA  DA  T . n 
C 3 3   DC  3   3   3   DC  DC  T . n 
C 3 4   DT  4   4   4   DT  DT  T . n 
C 3 5   DG  5   5   5   DG  DG  T . n 
C 3 6   DT  6   6   6   DT  DT  T . n 
C 3 7   DG  7   7   7   DG  DG  T . n 
C 3 8   DG  8   8   8   DG  DG  T . n 
C 3 9   DC  9   9   9   DC  DC  T . n 
C 3 10  DC  10  10  10  DC  DC  T . n 
C 3 11  DG  11  11  11  DG  DG  T . n 
C 3 12  DT  12  12  12  DT  DT  T . n 
C 3 13  DG  13  13  13  DG  DG  T . n 
C 3 14  DG  14  14  14  DG  DG  T . n 
C 3 15  DT  15  15  15  DT  DT  T . n 
C 3 16  DC  16  16  16  DC  DC  T . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        XG4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   XG4 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 4 MG  1 801 15 MG  MG  A . 
E 4 MG  1 802 16 MG  MG  A . 
F 4 MG  1 803 17 MG  MG  A . 
G 5 XG4 1 804 14 XG4 XG4 A . 
H 4 MG  1 805 1  MG  MG  A . 
I 4 MG  1 806 2  MG  MG  A . 
J 6 MN  1 807 3  MN  MN  A . 
K 7 IMD 1 808 6  IMD IMD A . 
L 8 GOL 1 101 4  GOL GOL P . 
M 8 GOL 1 101 5  GOL GOL T . 
N 9 HOH 1 901 1  HOH HOH A . 
N 9 HOH 2 902 14 HOH HOH A . 
N 9 HOH 3 903 2  HOH HOH A . 
N 9 HOH 4 904 10 HOH HOH A . 
N 9 HOH 5 905 11 HOH HOH A . 
N 9 HOH 6 906 15 HOH HOH A . 
N 9 HOH 7 907 4  HOH HOH A . 
N 9 HOH 8 908 3  HOH HOH A . 
O 9 HOH 1 201 7  HOH HOH T . 
O 9 HOH 2 202 6  HOH HOH T . 
O 9 HOH 3 203 9  HOH HOH T . 
O 9 HOH 4 204 12 HOH HOH T . 
O 9 HOH 5 205 8  HOH HOH T . 
O 9 HOH 6 206 13 HOH HOH T . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(dev_4788: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                 4 
# 
_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                     8S84 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     110.970 
_cell.length_a_esd                 ? 
_cell.length_b                     152.462 
_cell.length_b_esd                 ? 
_cell.length_c                     70.125 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8S84 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_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                   8S84 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.99 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          58.81 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Morpheus II condition A1:  36 % v/v of a 72% mix: 30% w/v PEG 3000, 40% v/v 1, 2, 4-Butanetriol, 2% w/v NDSB 256; 0.03 M Lithium sulfate, 0.03 M Sodium sulfate, 0.03 Potassium sulfate, 0.1 M MOPSO/Bis-Tris pH 6.5
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-10-10 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.976 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8S84 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.35 
_reflns.d_resolution_low                               46.796 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     95588 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          3.75 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.985 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.35 
_reflns_shell.d_res_low                                     2.49 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             15411 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.1 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8S84 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.35 
_refine.ls_d_res_low                             38.58 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     93177 
_refine.ls_number_reflns_R_free                  3647 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.93 
_refine.ls_percent_reflns_R_free                 3.91 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2383 
_refine.ls_R_factor_R_free                       0.2755 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2368 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.07 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 40.64 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.64 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.35 
_refine_hist.d_res_low                        38.58 
_refine_hist.number_atoms_solvent             14 
_refine_hist.number_atoms_total               6838 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        6200 
_refine_hist.pdbx_number_atoms_nucleic_acid   601 
_refine_hist.pdbx_number_atoms_ligand         23 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.003  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.628  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.398 ? 1149 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.043  ? 1033 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 1129 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.35 2.38  . . 95  2438 69.00  . . . . 0.4914 . . . . . . . . . . . 0.5482 
'X-RAY DIFFRACTION' 2.38 2.41  . . 119 2877 81.00  . . . . 0.4702 . . . . . . . . . . . 0.5313 
'X-RAY DIFFRACTION' 2.41 2.44  . . 128 3213 91.00  . . . . 0.4745 . . . . . . . . . . . 0.4652 
'X-RAY DIFFRACTION' 2.44 2.48  . . 136 3433 95.00  . . . . 0.4663 . . . . . . . . . . . 0.4465 
'X-RAY DIFFRACTION' 2.48 2.52  . . 136 3459 98.00  . . . . 0.5044 . . . . . . . . . . . 0.4644 
'X-RAY DIFFRACTION' 2.52 2.56  . . 143 3494 99.00  . . . . 0.4292 . . . . . . . . . . . 0.4819 
'X-RAY DIFFRACTION' 2.56 2.61  . . 148 3546 100.00 . . . . 0.4174 . . . . . . . . . . . 0.4181 
'X-RAY DIFFRACTION' 2.61 2.65  . . 143 3528 100.00 . . . . 0.3718 . . . . . . . . . . . 0.4396 
'X-RAY DIFFRACTION' 2.65 2.70  . . 148 3600 99.00  . . . . 0.3549 . . . . . . . . . . . 0.3841 
'X-RAY DIFFRACTION' 2.70 2.76  . . 143 3506 100.00 . . . . 0.3565 . . . . . . . . . . . 0.3855 
'X-RAY DIFFRACTION' 2.76 2.82  . . 146 3519 99.00  . . . . 0.3381 . . . . . . . . . . . 0.3400 
'X-RAY DIFFRACTION' 2.82 2.88  . . 144 3522 99.00  . . . . 0.3497 . . . . . . . . . . . 0.3753 
'X-RAY DIFFRACTION' 2.88 2.96  . . 144 3525 99.00  . . . . 0.3447 . . . . . . . . . . . 0.4644 
'X-RAY DIFFRACTION' 2.96 3.04  . . 147 3555 99.00  . . . . 0.3504 . . . . . . . . . . . 0.4065 
'X-RAY DIFFRACTION' 3.04 3.13  . . 145 3525 100.00 . . . . 0.3377 . . . . . . . . . . . 0.3274 
'X-RAY DIFFRACTION' 3.13 3.23  . . 139 3538 100.00 . . . . 0.2987 . . . . . . . . . . . 0.3302 
'X-RAY DIFFRACTION' 3.23 3.34  . . 143 3539 99.00  . . . . 0.2699 . . . . . . . . . . . 0.3157 
'X-RAY DIFFRACTION' 3.34 3.48  . . 143 3534 100.00 . . . . 0.2500 . . . . . . . . . . . 0.2947 
'X-RAY DIFFRACTION' 3.48 3.63  . . 147 3524 100.00 . . . . 0.2365 . . . . . . . . . . . 0.2557 
'X-RAY DIFFRACTION' 3.63 3.82  . . 145 3535 99.00  . . . . 0.2241 . . . . . . . . . . . 0.2852 
'X-RAY DIFFRACTION' 3.83 4.06  . . 148 3523 99.00  . . . . 0.1985 . . . . . . . . . . . 0.2354 
'X-RAY DIFFRACTION' 4.06 4.38  . . 144 3522 98.00  . . . . 0.1691 . . . . . . . . . . . 0.2418 
'X-RAY DIFFRACTION' 4.38 4.82  . . 142 3510 100.00 . . . . 0.1622 . . . . . . . . . . . 0.1734 
'X-RAY DIFFRACTION' 4.82 5.51  . . 143 3527 100.00 . . . . 0.1739 . . . . . . . . . . . 0.2395 
'X-RAY DIFFRACTION' 5.51 6.94  . . 145 3566 99.00  . . . . 0.1939 . . . . . . . . . . . 0.2702 
'X-RAY DIFFRACTION' 6.94 38.58 . . 143 3472 98.00  . . . . 0.1548 . . . . . . . . . . . 0.1695 
# 
_struct.entry_id                     8S84 
_struct.title                        
'KOD-H4 DNA polymerase mutant in a ternary complex with DNA/DNA and non-hydrolyzable triphosphate' 
_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        8S84 
_struct_keywords.text            'Polymerase, XNA, modified nucleotides, Reverse transcriptase, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 4 ? 
F N N 4 ? 
G N N 5 ? 
H N N 4 ? 
I N N 4 ? 
J N N 6 ? 
K N N 7 ? 
L N N 8 ? 
M N N 8 ? 
N N N 9 ? 
O N N 9 ? 
# 
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 D0VWU9_THEKO D0VWU9 ? 1 
;MILDTDYITEDGKPVIRIFKKENGEFKIEYDRTFEPYFYALLKDDSAIEEVKKITAERHGTVVTVKRVEKVQKKFLGRPV
EVWKLYFTHPQDVPAIRDKIREHPAVIDIYEYDIPFAKRYLIDKGLVPMEGDEELKMLAFDIETLYEEGEEFAEGPILMI
SYADEEGARVITWKNVDLPYVDVVSTEREMIKRFLRVVKEKDPDVLITYNGDNFDFAYLKKRCEKLGINFALGRDGSEPK
IQRMGDRFAVEVKGRIHFDLYPVIRRTINLPTYTLEAVYEAVFGQPKEKVYAEEITTAWETGENLERVARYSMEDAKVTY
ELGKEFLPMEAQLSRLIGQSLWDVSRSSTGNLVEWFLLRKAYERNELAPNKPDEKELARRRQSYEGGYVKEPERGLWENI
VYLDFRSLYPSIIITHNVSPDTLNREGCKEYDVAPQVGHRFCKDFPGFIPSLLGDLLEERQKIKKKMKATIDPIERKLLD
YRQRAIKILANSYYGYYGYARARWYCKECAESVTAWGREYITMTIKEIEEKYGFKVIYSDTDGFFATIPGADAETVKKKA
MEFLKYINAKLPGALELEYEGFYERGFFVTKKKYAVIDEEGKITTRGLEIVRRDWSEIAKETQARVLEALLKDGDVEKAV
RIVKEVTEKLSKYEVPPEKLVIHEQITRDLKDYKATGPHVAVAKRLAARGVKIRPGTVISYIVLKGSGRIGDRAIPFDEF
DPTKHKYDAEYYIENQVLPAVERILRAFGYRKEDLRYQKTRQVGLSAWLKPKGT
;
1 
2 PDB 8S84         8S84   ? 2 ? 1 
3 PDB 8S84         8S84   ? 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 8S84 A 1 ? 774 ? D0VWU9 1 ? 774 ? 1 774 
2 2 8S84 P 1 ? 13  ? 8S84   1 ? 13  ? 1 13  
3 3 8S84 T 1 ? 16  ? 8S84   1 ? 16  ? 1 16  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8S84 GLN A 93  ? UNP D0VWU9 VAL 93  conflict 93  1  
1 8S84 THR A 114 ? UNP D0VWU9 ILE 114 conflict 114 2  
1 8S84 ALA A 141 ? UNP D0VWU9 ASP 141 conflict 141 3  
1 8S84 ALA A 143 ? UNP D0VWU9 GLU 143 conflict 143 4  
1 8S84 HIS A 147 ? UNP D0VWU9 GLU 147 conflict 147 5  
1 8S84 LYS A 383 ? UNP D0VWU9 SER 383 conflict 383 6  
1 8S84 GLY A 429 ? UNP D0VWU9 LYS 429 conflict 429 7  
1 8S84 LEU A 445 ? UNP D0VWU9 PHE 445 conflict 445 8  
1 8S84 LEU A 485 ? UNP D0VWU9 ALA 485 conflict 485 9  
1 8S84 VAL A 493 ? UNP D0VWU9 TYR 493 conflict 493 10 
1 8S84 HIS A 496 ? UNP D0VWU9 TYR 496 conflict 496 11 
1 8S84 MET A 497 ? UNP D0VWU9 TYR 497 conflict 497 12 
1 8S84 PHE A 499 ? UNP D0VWU9 TYR 499 conflict 499 13 
1 8S84 GLU A 500 ? UNP D0VWU9 ALA 500 conflict 500 14 
1 8S84 ASN A 501 ? UNP D0VWU9 ARG 501 conflict 501 15 
1 8S84 LEU A 521 ? UNP D0VWU9 ILE 521 conflict 521 16 
1 8S84 LYS A 584 ? UNP D0VWU9 GLU 584 conflict 584 17 
1 8S84 LYS A 664 ? UNP D0VWU9 GLU 664 conflict 664 18 
1 8S84 ARG A 726 ? UNP D0VWU9 LYS 726 conflict 726 19 
1 8S84 LYS A 735 ? UNP D0VWU9 ASN 735 conflict 735 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,F,G,H,I,J,K,L,M,N,O 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 ALA A 47  ? LYS A 53  ? ALA A 47  LYS A 53  1 ? 7  
HELX_P HELX_P2  AA2 GLN A 91  ? GLU A 102 ? GLN A 91  GLU A 102 1 ? 12 
HELX_P HELX_P3  AA3 PRO A 115 ? LYS A 124 ? PRO A 115 LYS A 124 1 ? 10 
HELX_P HELX_P4  AA4 THR A 186 ? ASP A 202 ? THR A 186 ASP A 202 1 ? 17 
HELX_P HELX_P5  AA5 PHE A 214 ? GLY A 227 ? PHE A 214 GLY A 227 1 ? 14 
HELX_P HELX_P6  AA6 LEU A 260 ? ILE A 268 ? LEU A 260 ILE A 268 1 ? 9  
HELX_P HELX_P7  AA7 THR A 274 ? GLY A 284 ? THR A 274 GLY A 284 1 ? 11 
HELX_P HELX_P8  AA8 TYR A 291 ? GLY A 302 ? TYR A 291 GLY A 302 1 ? 12 
HELX_P HELX_P9  AA9 ASN A 304 ? GLY A 338 ? ASN A 304 GLY A 338 1 ? 35 
HELX_P HELX_P10 AB1 SER A 340 ? SER A 345 ? SER A 340 SER A 345 1 ? 6  
HELX_P HELX_P11 AB2 SER A 348 ? ARG A 364 ? SER A 348 ARG A 364 1 ? 17 
HELX_P HELX_P12 AB3 ASP A 373 ? ARG A 380 ? ASP A 373 ARG A 380 1 ? 8  
HELX_P HELX_P13 AB4 SER A 407 ? HIS A 416 ? SER A 407 HIS A 416 1 ? 10 
HELX_P HELX_P14 AB5 SER A 419 ? LEU A 423 ? SER A 419 LEU A 423 5 ? 5  
HELX_P HELX_P15 AB6 GLY A 447 ? THR A 470 ? GLY A 447 THR A 470 1 ? 24 
HELX_P HELX_P16 AB7 ASP A 472 ? GLY A 498 ? ASP A 472 GLY A 498 1 ? 27 
HELX_P HELX_P17 AB8 CYS A 506 ? LYS A 531 ? CYS A 506 LYS A 531 1 ? 26 
HELX_P HELX_P18 AB9 ASP A 552 ? LEU A 571 ? ASP A 552 LEU A 571 1 ? 20 
HELX_P HELX_P19 AC1 LEU A 608 ? ARG A 612 ? LEU A 608 ARG A 612 5 ? 5  
HELX_P HELX_P20 AC2 SER A 616 ? LYS A 632 ? SER A 616 LYS A 632 1 ? 17 
HELX_P HELX_P21 AC3 ASP A 635 ? LYS A 652 ? ASP A 635 LYS A 652 1 ? 18 
HELX_P HELX_P22 AC4 PRO A 656 ? VAL A 661 ? PRO A 656 VAL A 661 5 ? 6  
HELX_P HELX_P23 AC5 ASP A 669 ? TYR A 673 ? ASP A 669 TYR A 673 5 ? 5  
HELX_P HELX_P24 AC6 GLY A 677 ? ALA A 688 ? GLY A 677 ALA A 688 1 ? 12 
HELX_P HELX_P25 AC7 ARG A 709 ? ARG A 713 ? ARG A 709 ARG A 713 1 ? 5  
HELX_P HELX_P26 AC8 ASP A 718 ? PHE A 720 ? ASP A 718 PHE A 720 5 ? 3  
HELX_P HELX_P27 AC9 ASP A 728 ? LYS A 735 ? ASP A 728 LYS A 735 1 ? 8  
HELX_P HELX_P28 AD1 GLN A 736 ? ARG A 746 ? GLN A 736 ARG A 746 1 ? 11 
HELX_P HELX_P29 AD2 ALA A 747 ? GLY A 749 ? ALA A 747 GLY A 749 5 ? 3  
HELX_P HELX_P30 AD3 ARG A 751 ? ARG A 756 ? ARG A 751 ARG A 756 5 ? 6  
# 
_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 
disulf1  disulf ? ? A CYS 506 SG  ? ? ? 1_555 A CYS 509 SG    ? ? A CYS 506 A CYS 509 1_555 ? ? ? ? ? ? ?            2.037 ? ? 
metalc1  metalc ? ? A ASP 4   OD1 ? ? ? 1_555 H MG  .   MG    ? ? A ASP 4   A MG  805 1_555 ? ? ? ? ? ? ?            2.767 ? ? 
metalc2  metalc ? ? A ASP 343 OD2 ? ? ? 1_555 H MG  .   MG    ? ? A ASP 343 A MG  805 1_555 ? ? ? ? ? ? ?            2.709 ? ? 
metalc3  metalc ? ? A ASN 370 OD1 ? ? ? 1_555 I MG  .   MG    ? ? A ASN 370 A MG  806 1_555 ? ? ? ? ? ? ?            2.946 ? ? 
metalc4  metalc ? ? A ASP 404 OD2 ? ? ? 1_555 E MG  .   MG    ? ? A ASP 404 A MG  802 1_555 ? ? ? ? ? ? ?            2.733 ? ? 
metalc5  metalc ? ? A ASP 404 OD2 ? ? ? 1_555 F MG  .   MG    ? ? A ASP 404 A MG  803 1_555 ? ? ? ? ? ? ?            2.505 ? ? 
metalc6  metalc ? ? A PHE 405 O   ? ? ? 1_555 E MG  .   MG    ? ? A PHE 405 A MG  802 1_555 ? ? ? ? ? ? ?            2.640 ? ? 
metalc7  metalc ? ? A GLU 500 OE2 ? ? ? 1_555 J MN  .   MN    ? ? A GLU 500 A MN  807 1_555 ? ? ? ? ? ? ?            2.100 ? ? 
metalc8  metalc ? ? A ASP 542 OD2 ? ? ? 1_555 E MG  .   MG    ? ? A ASP 542 A MG  802 1_555 ? ? ? ? ? ? ?            1.911 ? ? 
metalc9  metalc ? ? A ASP 542 OD2 ? ? ? 1_555 F MG  .   MG    ? ? A ASP 542 A MG  803 1_555 ? ? ? ? ? ? ?            2.253 ? ? 
metalc10 metalc ? ? D MG  .   MG  ? ? ? 1_555 G XG4 .   O1B   ? ? A MG  801 A XG4 804 1_555 ? ? ? ? ? ? ?            2.242 ? ? 
metalc11 metalc ? ? D MG  .   MG  ? ? ? 1_555 G XG4 .   O1G   ? ? A MG  801 A XG4 804 1_555 ? ? ? ? ? ? ?            2.790 ? ? 
metalc12 metalc ? ? E MG  .   MG  ? ? ? 1_555 G XG4 .   O3B   ? ? A MG  802 A XG4 804 1_555 ? ? ? ? ? ? ?            2.503 ? ? 
metalc13 metalc ? ? F MG  .   MG  ? ? ? 1_555 G XG4 .   O1A   ? ? A MG  803 A XG4 804 1_555 ? ? ? ? ? ? ?            2.199 ? ? 
metalc14 metalc ? ? F MG  .   MG  ? ? ? 1_555 G XG4 .   O3G   ? ? A MG  803 A XG4 804 1_555 ? ? ? ? ? ? ?            2.805 ? ? 
metalc15 metalc ? ? F MG  .   MG  ? ? ? 1_555 N HOH .   O     ? ? A MG  803 A HOH 904 1_555 ? ? ? ? ? ? ?            2.588 ? ? 
metalc16 metalc ? ? F MG  .   MG  ? ? ? 1_555 B DA  13  "O3'" ? ? A MG  803 P DA  13  1_555 ? ? ? ? ? ? ?            2.991 ? ? 
metalc17 metalc ? ? J MN  .   MN  ? ? ? 1_555 C DT  4   OP1   ? ? A MN  807 T DT  4   1_555 ? ? ? ? ? ? ?            2.101 ? ? 
hydrog1  hydrog ? ? B DG  1   N1  ? ? ? 1_555 C DC  16  N3    ? ? P DG  1   T DC  16  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog2  hydrog ? ? B DG  1   N2  ? ? ? 1_555 C DC  16  O2    ? ? P DG  1   T DC  16  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog3  hydrog ? ? B DG  1   O6  ? ? ? 1_555 C DC  16  N4    ? ? P DG  1   T DC  16  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog4  hydrog ? ? B DA  2   N1  ? ? ? 1_555 C DT  15  N3    ? ? P DA  2   T DT  15  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog5  hydrog ? ? B DA  2   N6  ? ? ? 1_555 C DT  15  O4    ? ? P DA  2   T DT  15  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog6  hydrog ? ? B DC  3   N3  ? ? ? 1_555 C DG  14  N1    ? ? P DC  3   T DG  14  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog7  hydrog ? ? B DC  3   N4  ? ? ? 1_555 C DG  14  O6    ? ? P DC  3   T DG  14  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog8  hydrog ? ? B DC  3   O2  ? ? ? 1_555 C DG  14  N2    ? ? P DC  3   T DG  14  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog9  hydrog ? ? B DC  4   N3  ? ? ? 1_555 C DG  13  N1    ? ? P DC  4   T DG  13  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog10 hydrog ? ? B DC  4   N4  ? ? ? 1_555 C DG  13  O6    ? ? P DC  4   T DG  13  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog11 hydrog ? ? B DC  4   O2  ? ? ? 1_555 C DG  13  N2    ? ? P DC  4   T DG  13  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog12 hydrog ? ? B DA  5   N1  ? ? ? 1_555 C DT  12  N3    ? ? P DA  5   T DT  12  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog13 hydrog ? ? B DA  5   N6  ? ? ? 1_555 C DT  12  O4    ? ? P DA  5   T DT  12  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog14 hydrog ? ? B DC  6   N3  ? ? ? 1_555 C DG  11  N1    ? ? P DC  6   T DG  11  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog15 hydrog ? ? B DC  6   N4  ? ? ? 1_555 C DG  11  O6    ? ? P DC  6   T DG  11  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog16 hydrog ? ? B DC  6   O2  ? ? ? 1_555 C DG  11  N2    ? ? P DC  6   T DG  11  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog17 hydrog ? ? B DG  7   N1  ? ? ? 1_555 C DC  10  N3    ? ? P DG  7   T DC  10  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog18 hydrog ? ? B DG  7   N2  ? ? ? 1_555 C DC  10  O2    ? ? P DG  7   T DC  10  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog19 hydrog ? ? B DG  7   O6  ? ? ? 1_555 C DC  10  N4    ? ? P DG  7   T DC  10  1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog20 hydrog ? ? B DG  8   N1  ? ? ? 1_555 C DC  9   N3    ? ? P DG  8   T DC  9   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog21 hydrog ? ? B DG  8   N2  ? ? ? 1_555 C DC  9   O2    ? ? P DG  8   T DC  9   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog22 hydrog ? ? B DG  8   O6  ? ? ? 1_555 C DC  9   N4    ? ? P DG  8   T DC  9   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog23 hydrog ? ? B DC  9   N3  ? ? ? 1_555 C DG  8   N1    ? ? P DC  9   T DG  8   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog24 hydrog ? ? B DC  9   N4  ? ? ? 1_555 C DG  8   O6    ? ? P DC  9   T DG  8   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog25 hydrog ? ? B DC  9   O2  ? ? ? 1_555 C DG  8   N2    ? ? P DC  9   T DG  8   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog26 hydrog ? ? B DC  10  N3  ? ? ? 1_555 C DG  7   N1    ? ? P DC  10  T DG  7   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog27 hydrog ? ? B DC  10  N4  ? ? ? 1_555 C DG  7   O6    ? ? P DC  10  T DG  7   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog28 hydrog ? ? B DC  10  O2  ? ? ? 1_555 C DG  7   N2    ? ? P DC  10  T DG  7   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog29 hydrog ? ? B DA  11  N1  ? ? ? 1_555 C DT  6   N3    ? ? P DA  11  T DT  6   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog30 hydrog ? ? B DA  11  N6  ? ? ? 1_555 C DT  6   O4    ? ? P DA  11  T DT  6   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog31 hydrog ? ? B DC  12  N3  ? ? ? 1_555 C DG  5   N1    ? ? P DC  12  T DG  5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog32 hydrog ? ? B DC  12  N4  ? ? ? 1_555 C DG  5   O6    ? ? P DC  12  T DG  5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog33 hydrog ? ? B DC  12  O2  ? ? ? 1_555 C DG  5   N2    ? ? P DC  12  T DG  5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog34 hydrog ? ? B DA  13  N1  ? ? ? 1_555 C DT  4   N3    ? ? P DA  13  T DT  4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog35 hydrog ? ? B DA  13  N6  ? ? ? 1_555 C DT  4   O4    ? ? P DA  13  T DT  4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
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 4   ? A ASP 4   ? 1_555 MG ? H MG . ? A MG 805 ? 1_555 OD2   ? A ASP 343 ? A ASP 343 ? 1_555 105.4 ? 
2  OD2 ? A ASP 404 ? A ASP 404 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 O     ? A PHE 405 ? A PHE 405 ? 1_555 70.8  ? 
3  OD2 ? A ASP 404 ? A ASP 404 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 OD2   ? A ASP 542 ? A ASP 542 ? 1_555 66.1  ? 
4  O   ? A PHE 405 ? A PHE 405 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 OD2   ? A ASP 542 ? A ASP 542 ? 1_555 133.6 ? 
5  OD2 ? A ASP 404 ? A ASP 404 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 O3B   ? G XG4 .   ? A XG4 804 ? 1_555 68.9  ? 
6  O   ? A PHE 405 ? A PHE 405 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 O3B   ? G XG4 .   ? A XG4 804 ? 1_555 65.4  ? 
7  OD2 ? A ASP 542 ? A ASP 542 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 O3B   ? G XG4 .   ? A XG4 804 ? 1_555 111.7 ? 
8  OD2 ? A ASP 404 ? A ASP 404 ? 1_555 MG ? F MG . ? A MG 803 ? 1_555 OD2   ? A ASP 542 ? A ASP 542 ? 1_555 66.7  ? 
9  OD2 ? A ASP 404 ? A ASP 404 ? 1_555 MG ? F MG . ? A MG 803 ? 1_555 O1A   ? G XG4 .   ? A XG4 804 ? 1_555 118.4 ? 
10 OD2 ? A ASP 542 ? A ASP 542 ? 1_555 MG ? F MG . ? A MG 803 ? 1_555 O1A   ? G XG4 .   ? A XG4 804 ? 1_555 70.4  ? 
11 OD2 ? A ASP 404 ? A ASP 404 ? 1_555 MG ? F MG . ? A MG 803 ? 1_555 O3G   ? G XG4 .   ? A XG4 804 ? 1_555 64.7  ? 
12 OD2 ? A ASP 542 ? A ASP 542 ? 1_555 MG ? F MG . ? A MG 803 ? 1_555 O3G   ? G XG4 .   ? A XG4 804 ? 1_555 116.9 ? 
13 O1A ? G XG4 .   ? A XG4 804 ? 1_555 MG ? F MG . ? A MG 803 ? 1_555 O3G   ? G XG4 .   ? A XG4 804 ? 1_555 100.8 ? 
14 OD2 ? A ASP 404 ? A ASP 404 ? 1_555 MG ? F MG . ? A MG 803 ? 1_555 O     ? N HOH .   ? A HOH 904 ? 1_555 140.5 ? 
15 OD2 ? A ASP 542 ? A ASP 542 ? 1_555 MG ? F MG . ? A MG 803 ? 1_555 O     ? N HOH .   ? A HOH 904 ? 1_555 133.4 ? 
16 O1A ? G XG4 .   ? A XG4 804 ? 1_555 MG ? F MG . ? A MG 803 ? 1_555 O     ? N HOH .   ? A HOH 904 ? 1_555 63.1  ? 
17 O3G ? G XG4 .   ? A XG4 804 ? 1_555 MG ? F MG . ? A MG 803 ? 1_555 O     ? N HOH .   ? A HOH 904 ? 1_555 76.2  ? 
18 OD2 ? A ASP 404 ? A ASP 404 ? 1_555 MG ? F MG . ? A MG 803 ? 1_555 "O3'" ? B DA  13  ? P DA  13  ? 1_555 135.2 ? 
19 OD2 ? A ASP 542 ? A ASP 542 ? 1_555 MG ? F MG . ? A MG 803 ? 1_555 "O3'" ? B DA  13  ? P DA  13  ? 1_555 82.6  ? 
20 O1A ? G XG4 .   ? A XG4 804 ? 1_555 MG ? F MG . ? A MG 803 ? 1_555 "O3'" ? B DA  13  ? P DA  13  ? 1_555 77.0  ? 
21 O3G ? G XG4 .   ? A XG4 804 ? 1_555 MG ? F MG . ? A MG 803 ? 1_555 "O3'" ? B DA  13  ? P DA  13  ? 1_555 158.8 ? 
22 O   ? N HOH .   ? A HOH 904 ? 1_555 MG ? F MG . ? A MG 803 ? 1_555 "O3'" ? B DA  13  ? P DA  13  ? 1_555 84.3  ? 
23 OE2 ? A GLU 500 ? A GLU 500 ? 1_555 MN ? J MN . ? A MN 807 ? 1_555 OP1   ? C DT  4   ? T DT  4   ? 1_555 80.1  ? 
24 O1B ? G XG4 .   ? A XG4 804 ? 1_555 MG ? D MG . ? A MG 801 ? 1_555 O1G   ? G XG4 .   ? A XG4 804 ? 1_555 66.6  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       506 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      509 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        506 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       509 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 6 ? 
AA5 ? 2 ? 
AA6 ? 6 ? 
AA7 ? 2 ? 
AA8 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? parallel      
AA4 5 6 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 2   ? GLU A 10  ? ILE A 2   GLU A 10  
AA1 2 LYS A 13  ? GLU A 22  ? LYS A 13  GLU A 22  
AA1 3 GLU A 25  ? ASP A 31  ? GLU A 25  ASP A 31  
AA2 1 VAL A 68  ? PHE A 75  ? VAL A 68  PHE A 75  
AA2 2 ARG A 78  ? TYR A 86  ? ARG A 78  TYR A 86  
AA2 3 TYR A 37  ? LEU A 42  ? TYR A 37  LEU A 42  
AA2 4 VAL A 106 ? TYR A 110 ? VAL A 106 TYR A 110 
AA3 1 THR A 55  ? GLU A 57  ? THR A 55  GLU A 57  
AA3 2 VAL A 62  ? THR A 64  ? VAL A 62  THR A 64  
AA4 1 VAL A 181 ? VAL A 183 ? VAL A 181 VAL A 183 
AA4 2 GLY A 167 ? THR A 172 ? GLY A 167 THR A 172 
AA4 3 ILE A 157 ? ASP A 164 ? ILE A 157 ASP A 164 
AA4 4 MET A 137 ? THR A 144 ? MET A 137 THR A 144 
AA4 5 VAL A 205 ? THR A 208 ? VAL A 205 THR A 208 
AA4 6 ILE A 256 ? ASP A 259 ? ILE A 256 ASP A 259 
AA5 1 LYS A 240 ? GLN A 242 ? LYS A 240 GLN A 242 
AA5 2 ALA A 249 ? GLU A 251 ? ALA A 249 GLU A 251 
AA6 1 LYS A 535 ? SER A 539 ? LYS A 535 SER A 539 
AA6 2 GLY A 543 ? THR A 547 ? GLY A 543 THR A 547 
AA6 3 GLY A 395 ? PHE A 405 ? GLY A 395 PHE A 405 
AA6 4 LEU A 577 ? THR A 590 ? LEU A 577 THR A 590 
AA6 5 LYS A 593 ? ASP A 598 ? LYS A 593 ASP A 598 
AA6 6 ILE A 603 ? ARG A 606 ? ILE A 603 ARG A 606 
AA7 1 TYR A 431 ? VAL A 433 ? TYR A 431 VAL A 433 
AA7 2 ARG A 440 ? CYS A 442 ? ARG A 440 CYS A 442 
AA8 1 ILE A 662 ? GLN A 665 ? ILE A 662 GLN A 665 
AA8 2 VAL A 698 ? VAL A 703 ? VAL A 698 VAL A 703 
AA8 3 ALA A 714 ? PRO A 716 ? ALA A 714 PRO A 716 
# 
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 ASP A 6   ? N ASP A 6   O ARG A 17  ? O ARG A 17  
AA1 2 3 N ILE A 18  ? N ILE A 18  O GLU A 29  ? O GLU A 29  
AA2 1 2 N VAL A 71  ? N VAL A 71  O VAL A 82  ? O VAL A 82  
AA2 2 3 O LEU A 85  ? O LEU A 85  N PHE A 38  ? N PHE A 38  
AA2 3 4 N LEU A 41  ? N LEU A 41  O ILE A 107 ? O ILE A 107 
AA3 1 2 N ALA A 56  ? N ALA A 56  O VAL A 63  ? O VAL A 63  
AA4 1 2 O ASP A 182 ? O ASP A 182 N VAL A 170 ? N VAL A 170 
AA4 2 3 O ILE A 171 ? O ILE A 171 N ILE A 160 ? N ILE A 160 
AA4 3 4 O SER A 161 ? O SER A 161 N ALA A 141 ? N ALA A 141 
AA4 4 5 N LEU A 138 ? N LEU A 138 O ILE A 207 ? O ILE A 207 
AA4 5 6 N LEU A 206 ? N LEU A 206 O PHE A 258 ? O PHE A 258 
AA5 1 2 N LYS A 240 ? N LYS A 240 O GLU A 251 ? O GLU A 251 
AA6 1 2 N TYR A 538 ? N TYR A 538 O PHE A 545 ? O PHE A 545 
AA6 2 3 O ALA A 546 ? O ALA A 546 N VAL A 401 ? N VAL A 401 
AA6 3 4 N ASP A 404 ? N ASP A 404 O GLU A 578 ? O GLU A 578 
AA6 4 5 N PHE A 587 ? N PHE A 587 O ALA A 595 ? O ALA A 595 
AA6 5 6 N VAL A 596 ? N VAL A 596 O THR A 604 ? O THR A 604 
AA7 1 2 N ASP A 432 ? N ASP A 432 O PHE A 441 ? O PHE A 441 
AA8 1 2 N LYS A 664 ? N LYS A 664 O ILE A 699 ? O ILE A 699 
AA8 2 3 N ILE A 702 ? N ILE A 702 O ILE A 715 ? O ILE A 715 
# 
_pdbx_entry_details.entry_id                   8S84 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   NZ 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   LYS 
_pdbx_validate_close_contact.auth_seq_id_1    487 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O1B 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   XG4 
_pdbx_validate_close_contact.auth_seq_id_2    804 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.09 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 45  ? ? -88.14  30.82   
2  1 ARG A 58  ? ? -118.23 -79.75  
3  1 LYS A 66  ? ? -65.58  -71.84  
4  1 ASP A 164 ? ? -154.34 -148.35 
5  1 PHE A 214 ? ? -137.55 -69.84  
6  1 ALA A 231 ? ? -85.38  49.97   
7  1 ASP A 373 ? ? -95.22  -157.02 
8  1 ARG A 380 ? ? -47.94  7.47    
9  1 GLN A 382 ? ? -68.63  -176.91 
10 1 GLU A 393 ? ? -67.90  84.96   
11 1 ASN A 399 ? ? 54.99   75.10   
12 1 GLN A 436 ? ? 63.97   -53.23  
13 1 TRP A 504 ? ? -95.28  47.75   
14 1 CYS A 506 ? ? -161.00 95.46   
15 1 ASP A 540 ? ? -102.82 -134.66 
16 1 ALA A 551 ? ? 58.60   -174.19 
17 1 LYS A 592 ? ? 65.07   -0.18   
18 1 ASP A 614 ? ? -96.86  30.01   
19 1 GLN A 736 ? ? -130.18 -57.42  
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         27.8973 
_pdbx_refine_tls.origin_y         21.1681 
_pdbx_refine_tls.origin_z         18.1589 
_pdbx_refine_tls.T[1][1]          0.4336 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0253 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0022 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.4491 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0209 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.4001 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.5542 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.2812 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.0145 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.9699 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.8823 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.9673 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0392 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0537 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.2014 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.1405 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0366 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0068 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0335 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0668 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0861 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
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 TYR 757 ? A TYR 757 
2  1 Y 1 A GLN 758 ? A GLN 758 
3  1 Y 1 A LYS 759 ? A LYS 759 
4  1 Y 1 A THR 760 ? A THR 760 
5  1 Y 1 A ARG 761 ? A ARG 761 
6  1 Y 1 A GLN 762 ? A GLN 762 
7  1 Y 1 A VAL 763 ? A VAL 763 
8  1 Y 1 A GLY 764 ? A GLY 764 
9  1 Y 1 A LEU 765 ? A LEU 765 
10 1 Y 1 A SER 766 ? A SER 766 
11 1 Y 1 A ALA 767 ? A ALA 767 
12 1 Y 1 A TRP 768 ? A TRP 768 
13 1 Y 1 A LEU 769 ? A LEU 769 
14 1 Y 1 A LYS 770 ? A LYS 770 
15 1 Y 1 A PRO 771 ? A PRO 771 
16 1 Y 1 A LYS 772 ? A LYS 772 
17 1 Y 1 A GLY 773 ? A GLY 773 
18 1 Y 1 A THR 774 ? A THR 774 
19 1 Y 1 T DA  1   ? C DA  1   
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
DA  OP3    O  N N 88  
DA  P      P  N N 89  
DA  OP1    O  N N 90  
DA  OP2    O  N N 91  
DA  "O5'"  O  N N 92  
DA  "C5'"  C  N N 93  
DA  "C4'"  C  N R 94  
DA  "O4'"  O  N N 95  
DA  "C3'"  C  N S 96  
DA  "O3'"  O  N N 97  
DA  "C2'"  C  N N 98  
DA  "C1'"  C  N R 99  
DA  N9     N  Y N 100 
DA  C8     C  Y N 101 
DA  N7     N  Y N 102 
DA  C5     C  Y N 103 
DA  C6     C  Y N 104 
DA  N6     N  N N 105 
DA  N1     N  Y N 106 
DA  C2     C  Y N 107 
DA  N3     N  Y N 108 
DA  C4     C  Y N 109 
DA  HOP3   H  N N 110 
DA  HOP2   H  N N 111 
DA  "H5'"  H  N N 112 
DA  "H5''" H  N N 113 
DA  "H4'"  H  N N 114 
DA  "H3'"  H  N N 115 
DA  "HO3'" H  N N 116 
DA  "H2'"  H  N N 117 
DA  "H2''" H  N N 118 
DA  "H1'"  H  N N 119 
DA  H8     H  N N 120 
DA  H61    H  N N 121 
DA  H62    H  N N 122 
DA  H2     H  N N 123 
DC  OP3    O  N N 124 
DC  P      P  N N 125 
DC  OP1    O  N N 126 
DC  OP2    O  N N 127 
DC  "O5'"  O  N N 128 
DC  "C5'"  C  N N 129 
DC  "C4'"  C  N R 130 
DC  "O4'"  O  N N 131 
DC  "C3'"  C  N S 132 
DC  "O3'"  O  N N 133 
DC  "C2'"  C  N N 134 
DC  "C1'"  C  N R 135 
DC  N1     N  N N 136 
DC  C2     C  N N 137 
DC  O2     O  N N 138 
DC  N3     N  N N 139 
DC  C4     C  N N 140 
DC  N4     N  N N 141 
DC  C5     C  N N 142 
DC  C6     C  N N 143 
DC  HOP3   H  N N 144 
DC  HOP2   H  N N 145 
DC  "H5'"  H  N N 146 
DC  "H5''" H  N N 147 
DC  "H4'"  H  N N 148 
DC  "H3'"  H  N N 149 
DC  "HO3'" H  N N 150 
DC  "H2'"  H  N N 151 
DC  "H2''" H  N N 152 
DC  "H1'"  H  N N 153 
DC  H41    H  N N 154 
DC  H42    H  N N 155 
DC  H5     H  N N 156 
DC  H6     H  N N 157 
DG  OP3    O  N N 158 
DG  P      P  N N 159 
DG  OP1    O  N N 160 
DG  OP2    O  N N 161 
DG  "O5'"  O  N N 162 
DG  "C5'"  C  N N 163 
DG  "C4'"  C  N R 164 
DG  "O4'"  O  N N 165 
DG  "C3'"  C  N S 166 
DG  "O3'"  O  N N 167 
DG  "C2'"  C  N N 168 
DG  "C1'"  C  N R 169 
DG  N9     N  Y N 170 
DG  C8     C  Y N 171 
DG  N7     N  Y N 172 
DG  C5     C  Y N 173 
DG  C6     C  N N 174 
DG  O6     O  N N 175 
DG  N1     N  N N 176 
DG  C2     C  N N 177 
DG  N2     N  N N 178 
DG  N3     N  N N 179 
DG  C4     C  Y N 180 
DG  HOP3   H  N N 181 
DG  HOP2   H  N N 182 
DG  "H5'"  H  N N 183 
DG  "H5''" H  N N 184 
DG  "H4'"  H  N N 185 
DG  "H3'"  H  N N 186 
DG  "HO3'" H  N N 187 
DG  "H2'"  H  N N 188 
DG  "H2''" H  N N 189 
DG  "H1'"  H  N N 190 
DG  H8     H  N N 191 
DG  H1     H  N N 192 
DG  H21    H  N N 193 
DG  H22    H  N N 194 
DT  OP3    O  N N 195 
DT  P      P  N N 196 
DT  OP1    O  N N 197 
DT  OP2    O  N N 198 
DT  "O5'"  O  N N 199 
DT  "C5'"  C  N N 200 
DT  "C4'"  C  N R 201 
DT  "O4'"  O  N N 202 
DT  "C3'"  C  N S 203 
DT  "O3'"  O  N N 204 
DT  "C2'"  C  N N 205 
DT  "C1'"  C  N R 206 
DT  N1     N  N N 207 
DT  C2     C  N N 208 
DT  O2     O  N N 209 
DT  N3     N  N N 210 
DT  C4     C  N N 211 
DT  O4     O  N N 212 
DT  C5     C  N N 213 
DT  C7     C  N N 214 
DT  C6     C  N N 215 
DT  HOP3   H  N N 216 
DT  HOP2   H  N N 217 
DT  "H5'"  H  N N 218 
DT  "H5''" H  N N 219 
DT  "H4'"  H  N N 220 
DT  "H3'"  H  N N 221 
DT  "HO3'" H  N N 222 
DT  "H2'"  H  N N 223 
DT  "H2''" H  N N 224 
DT  "H1'"  H  N N 225 
DT  H3     H  N N 226 
DT  H71    H  N N 227 
DT  H72    H  N N 228 
DT  H73    H  N N 229 
DT  H6     H  N N 230 
GLN N      N  N N 231 
GLN CA     C  N S 232 
GLN C      C  N N 233 
GLN O      O  N N 234 
GLN CB     C  N N 235 
GLN CG     C  N N 236 
GLN CD     C  N N 237 
GLN OE1    O  N N 238 
GLN NE2    N  N N 239 
GLN OXT    O  N N 240 
GLN H      H  N N 241 
GLN H2     H  N N 242 
GLN HA     H  N N 243 
GLN HB2    H  N N 244 
GLN HB3    H  N N 245 
GLN HG2    H  N N 246 
GLN HG3    H  N N 247 
GLN HE21   H  N N 248 
GLN HE22   H  N N 249 
GLN HXT    H  N N 250 
GLU N      N  N N 251 
GLU CA     C  N S 252 
GLU C      C  N N 253 
GLU O      O  N N 254 
GLU CB     C  N N 255 
GLU CG     C  N N 256 
GLU CD     C  N N 257 
GLU OE1    O  N N 258 
GLU OE2    O  N N 259 
GLU OXT    O  N N 260 
GLU H      H  N N 261 
GLU H2     H  N N 262 
GLU HA     H  N N 263 
GLU HB2    H  N N 264 
GLU HB3    H  N N 265 
GLU HG2    H  N N 266 
GLU HG3    H  N N 267 
GLU HE2    H  N N 268 
GLU HXT    H  N N 269 
GLY N      N  N N 270 
GLY CA     C  N N 271 
GLY C      C  N N 272 
GLY O      O  N N 273 
GLY OXT    O  N N 274 
GLY H      H  N N 275 
GLY H2     H  N N 276 
GLY HA2    H  N N 277 
GLY HA3    H  N N 278 
GLY HXT    H  N N 279 
GOL C1     C  N N 280 
GOL O1     O  N N 281 
GOL C2     C  N N 282 
GOL O2     O  N N 283 
GOL C3     C  N N 284 
GOL O3     O  N N 285 
GOL H11    H  N N 286 
GOL H12    H  N N 287 
GOL HO1    H  N N 288 
GOL H2     H  N N 289 
GOL HO2    H  N N 290 
GOL H31    H  N N 291 
GOL H32    H  N N 292 
GOL HO3    H  N N 293 
HIS N      N  N N 294 
HIS CA     C  N S 295 
HIS C      C  N N 296 
HIS O      O  N N 297 
HIS CB     C  N N 298 
HIS CG     C  Y N 299 
HIS ND1    N  Y N 300 
HIS CD2    C  Y N 301 
HIS CE1    C  Y N 302 
HIS NE2    N  Y N 303 
HIS OXT    O  N N 304 
HIS H      H  N N 305 
HIS H2     H  N N 306 
HIS HA     H  N N 307 
HIS HB2    H  N N 308 
HIS HB3    H  N N 309 
HIS HD1    H  N N 310 
HIS HD2    H  N N 311 
HIS HE1    H  N N 312 
HIS HE2    H  N N 313 
HIS HXT    H  N N 314 
HOH O      O  N N 315 
HOH H1     H  N N 316 
HOH H2     H  N N 317 
ILE N      N  N N 318 
ILE CA     C  N S 319 
ILE C      C  N N 320 
ILE O      O  N N 321 
ILE CB     C  N S 322 
ILE CG1    C  N N 323 
ILE CG2    C  N N 324 
ILE CD1    C  N N 325 
ILE OXT    O  N N 326 
ILE H      H  N N 327 
ILE H2     H  N N 328 
ILE HA     H  N N 329 
ILE HB     H  N N 330 
ILE HG12   H  N N 331 
ILE HG13   H  N N 332 
ILE HG21   H  N N 333 
ILE HG22   H  N N 334 
ILE HG23   H  N N 335 
ILE HD11   H  N N 336 
ILE HD12   H  N N 337 
ILE HD13   H  N N 338 
ILE HXT    H  N N 339 
IMD N1     N  Y N 340 
IMD C2     C  Y N 341 
IMD N3     N  Y N 342 
IMD C4     C  Y N 343 
IMD C5     C  Y N 344 
IMD HN1    H  N N 345 
IMD H2     H  N N 346 
IMD HN3    H  N N 347 
IMD H4     H  N N 348 
IMD H5     H  N N 349 
LEU N      N  N N 350 
LEU CA     C  N S 351 
LEU C      C  N N 352 
LEU O      O  N N 353 
LEU CB     C  N N 354 
LEU CG     C  N N 355 
LEU CD1    C  N N 356 
LEU CD2    C  N N 357 
LEU OXT    O  N N 358 
LEU H      H  N N 359 
LEU H2     H  N N 360 
LEU HA     H  N N 361 
LEU HB2    H  N N 362 
LEU HB3    H  N N 363 
LEU HG     H  N N 364 
LEU HD11   H  N N 365 
LEU HD12   H  N N 366 
LEU HD13   H  N N 367 
LEU HD21   H  N N 368 
LEU HD22   H  N N 369 
LEU HD23   H  N N 370 
LEU HXT    H  N N 371 
LYS N      N  N N 372 
LYS CA     C  N S 373 
LYS C      C  N N 374 
LYS O      O  N N 375 
LYS CB     C  N N 376 
LYS CG     C  N N 377 
LYS CD     C  N N 378 
LYS CE     C  N N 379 
LYS NZ     N  N N 380 
LYS OXT    O  N N 381 
LYS H      H  N N 382 
LYS H2     H  N N 383 
LYS HA     H  N N 384 
LYS HB2    H  N N 385 
LYS HB3    H  N N 386 
LYS HG2    H  N N 387 
LYS HG3    H  N N 388 
LYS HD2    H  N N 389 
LYS HD3    H  N N 390 
LYS HE2    H  N N 391 
LYS HE3    H  N N 392 
LYS HZ1    H  N N 393 
LYS HZ2    H  N N 394 
LYS HZ3    H  N N 395 
LYS HXT    H  N N 396 
MET N      N  N N 397 
MET CA     C  N S 398 
MET C      C  N N 399 
MET O      O  N N 400 
MET CB     C  N N 401 
MET CG     C  N N 402 
MET SD     S  N N 403 
MET CE     C  N N 404 
MET OXT    O  N N 405 
MET H      H  N N 406 
MET H2     H  N N 407 
MET HA     H  N N 408 
MET HB2    H  N N 409 
MET HB3    H  N N 410 
MET HG2    H  N N 411 
MET HG3    H  N N 412 
MET HE1    H  N N 413 
MET HE2    H  N N 414 
MET HE3    H  N N 415 
MET HXT    H  N N 416 
MG  MG     MG N N 417 
MN  MN     MN N N 418 
PHE N      N  N N 419 
PHE CA     C  N S 420 
PHE C      C  N N 421 
PHE O      O  N N 422 
PHE CB     C  N N 423 
PHE CG     C  Y N 424 
PHE CD1    C  Y N 425 
PHE CD2    C  Y N 426 
PHE CE1    C  Y N 427 
PHE CE2    C  Y N 428 
PHE CZ     C  Y N 429 
PHE OXT    O  N N 430 
PHE H      H  N N 431 
PHE H2     H  N N 432 
PHE HA     H  N N 433 
PHE HB2    H  N N 434 
PHE HB3    H  N N 435 
PHE HD1    H  N N 436 
PHE HD2    H  N N 437 
PHE HE1    H  N N 438 
PHE HE2    H  N N 439 
PHE HZ     H  N N 440 
PHE HXT    H  N N 441 
PRO N      N  N N 442 
PRO CA     C  N S 443 
PRO C      C  N N 444 
PRO O      O  N N 445 
PRO CB     C  N N 446 
PRO CG     C  N N 447 
PRO CD     C  N N 448 
PRO OXT    O  N N 449 
PRO H      H  N N 450 
PRO HA     H  N N 451 
PRO HB2    H  N N 452 
PRO HB3    H  N N 453 
PRO HG2    H  N N 454 
PRO HG3    H  N N 455 
PRO HD2    H  N N 456 
PRO HD3    H  N N 457 
PRO HXT    H  N N 458 
SER N      N  N N 459 
SER CA     C  N S 460 
SER C      C  N N 461 
SER O      O  N N 462 
SER CB     C  N N 463 
SER OG     O  N N 464 
SER OXT    O  N N 465 
SER H      H  N N 466 
SER H2     H  N N 467 
SER HA     H  N N 468 
SER HB2    H  N N 469 
SER HB3    H  N N 470 
SER HG     H  N N 471 
SER HXT    H  N N 472 
THR N      N  N N 473 
THR CA     C  N S 474 
THR C      C  N N 475 
THR O      O  N N 476 
THR CB     C  N R 477 
THR OG1    O  N N 478 
THR CG2    C  N N 479 
THR OXT    O  N N 480 
THR H      H  N N 481 
THR H2     H  N N 482 
THR HA     H  N N 483 
THR HB     H  N N 484 
THR HG1    H  N N 485 
THR HG21   H  N N 486 
THR HG22   H  N N 487 
THR HG23   H  N N 488 
THR HXT    H  N N 489 
TRP N      N  N N 490 
TRP CA     C  N S 491 
TRP C      C  N N 492 
TRP O      O  N N 493 
TRP CB     C  N N 494 
TRP CG     C  Y N 495 
TRP CD1    C  Y N 496 
TRP CD2    C  Y N 497 
TRP NE1    N  Y N 498 
TRP CE2    C  Y N 499 
TRP CE3    C  Y N 500 
TRP CZ2    C  Y N 501 
TRP CZ3    C  Y N 502 
TRP CH2    C  Y N 503 
TRP OXT    O  N N 504 
TRP H      H  N N 505 
TRP H2     H  N N 506 
TRP HA     H  N N 507 
TRP HB2    H  N N 508 
TRP HB3    H  N N 509 
TRP HD1    H  N N 510 
TRP HE1    H  N N 511 
TRP HE3    H  N N 512 
TRP HZ2    H  N N 513 
TRP HZ3    H  N N 514 
TRP HH2    H  N N 515 
TRP HXT    H  N N 516 
TYR N      N  N N 517 
TYR CA     C  N S 518 
TYR C      C  N N 519 
TYR O      O  N N 520 
TYR CB     C  N N 521 
TYR CG     C  Y N 522 
TYR CD1    C  Y N 523 
TYR CD2    C  Y N 524 
TYR CE1    C  Y N 525 
TYR CE2    C  Y N 526 
TYR CZ     C  Y N 527 
TYR OH     O  N N 528 
TYR OXT    O  N N 529 
TYR H      H  N N 530 
TYR H2     H  N N 531 
TYR HA     H  N N 532 
TYR HB2    H  N N 533 
TYR HB3    H  N N 534 
TYR HD1    H  N N 535 
TYR HD2    H  N N 536 
TYR HE1    H  N N 537 
TYR HE2    H  N N 538 
TYR HH     H  N N 539 
TYR HXT    H  N N 540 
VAL N      N  N N 541 
VAL CA     C  N S 542 
VAL C      C  N N 543 
VAL O      O  N N 544 
VAL CB     C  N N 545 
VAL CG1    C  N N 546 
VAL CG2    C  N N 547 
VAL OXT    O  N N 548 
VAL H      H  N N 549 
VAL H2     H  N N 550 
VAL HA     H  N N 551 
VAL HB     H  N N 552 
VAL HG11   H  N N 553 
VAL HG12   H  N N 554 
VAL HG13   H  N N 555 
VAL HG21   H  N N 556 
VAL HG22   H  N N 557 
VAL HG23   H  N N 558 
VAL HXT    H  N N 559 
XG4 N1     N  N N 560 
XG4 C2     C  N N 561 
XG4 N2     N  N N 562 
XG4 N3     N  N N 563 
XG4 C4     C  Y N 564 
XG4 C5     C  Y N 565 
XG4 C6     C  N N 566 
XG4 O6     O  N N 567 
XG4 N7     N  Y N 568 
XG4 C8     C  Y N 569 
XG4 N9     N  Y N 570 
XG4 PA     P  N N 571 
XG4 PB     P  N N 572 
XG4 PG     P  N N 573 
XG4 "C1'"  C  N R 574 
XG4 O1A    O  N N 575 
XG4 O1B    O  N N 576 
XG4 O1G    O  N N 577 
XG4 "C2'"  C  N N 578 
XG4 O2A    O  N N 579 
XG4 O2B    O  N N 580 
XG4 O2G    O  N N 581 
XG4 "C3'"  C  N S 582 
XG4 "O3'"  O  N N 583 
XG4 N3A    N  N N 584 
XG4 O3B    O  N N 585 
XG4 O3G    O  N N 586 
XG4 "C4'"  C  N R 587 
XG4 "O4'"  O  N N 588 
XG4 "C5'"  C  N N 589 
XG4 "O5'"  O  N N 590 
XG4 HN1    H  N N 591 
XG4 HN2    H  N N 592 
XG4 HN2A   H  N N 593 
XG4 H8     H  N N 594 
XG4 "H1'"  H  N N 595 
XG4 "H2'"  H  N N 596 
XG4 "H2'A" H  N N 597 
XG4 HO2A   H  N N 598 
XG4 HO2B   H  N N 599 
XG4 HO2G   H  N N 600 
XG4 "H3'"  H  N N 601 
XG4 "HO3'" H  N N 602 
XG4 HN3A   H  N N 603 
XG4 HO3G   H  N N 604 
XG4 "H4'"  H  N N 605 
XG4 "H5'"  H  N N 606 
XG4 "H5'A" H  N N 607 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
DA  OP3   P      sing N N 83  
DA  OP3   HOP3   sing N N 84  
DA  P     OP1    doub N N 85  
DA  P     OP2    sing N N 86  
DA  P     "O5'"  sing N N 87  
DA  OP2   HOP2   sing N N 88  
DA  "O5'" "C5'"  sing N N 89  
DA  "C5'" "C4'"  sing N N 90  
DA  "C5'" "H5'"  sing N N 91  
DA  "C5'" "H5''" sing N N 92  
DA  "C4'" "O4'"  sing N N 93  
DA  "C4'" "C3'"  sing N N 94  
DA  "C4'" "H4'"  sing N N 95  
DA  "O4'" "C1'"  sing N N 96  
DA  "C3'" "O3'"  sing N N 97  
DA  "C3'" "C2'"  sing N N 98  
DA  "C3'" "H3'"  sing N N 99  
DA  "O3'" "HO3'" sing N N 100 
DA  "C2'" "C1'"  sing N N 101 
DA  "C2'" "H2'"  sing N N 102 
DA  "C2'" "H2''" sing N N 103 
DA  "C1'" N9     sing N N 104 
DA  "C1'" "H1'"  sing N N 105 
DA  N9    C8     sing Y N 106 
DA  N9    C4     sing Y N 107 
DA  C8    N7     doub Y N 108 
DA  C8    H8     sing N N 109 
DA  N7    C5     sing Y N 110 
DA  C5    C6     sing Y N 111 
DA  C5    C4     doub Y N 112 
DA  C6    N6     sing N N 113 
DA  C6    N1     doub Y N 114 
DA  N6    H61    sing N N 115 
DA  N6    H62    sing N N 116 
DA  N1    C2     sing Y N 117 
DA  C2    N3     doub Y N 118 
DA  C2    H2     sing N N 119 
DA  N3    C4     sing Y N 120 
DC  OP3   P      sing N N 121 
DC  OP3   HOP3   sing N N 122 
DC  P     OP1    doub N N 123 
DC  P     OP2    sing N N 124 
DC  P     "O5'"  sing N N 125 
DC  OP2   HOP2   sing N N 126 
DC  "O5'" "C5'"  sing N N 127 
DC  "C5'" "C4'"  sing N N 128 
DC  "C5'" "H5'"  sing N N 129 
DC  "C5'" "H5''" sing N N 130 
DC  "C4'" "O4'"  sing N N 131 
DC  "C4'" "C3'"  sing N N 132 
DC  "C4'" "H4'"  sing N N 133 
DC  "O4'" "C1'"  sing N N 134 
DC  "C3'" "O3'"  sing N N 135 
DC  "C3'" "C2'"  sing N N 136 
DC  "C3'" "H3'"  sing N N 137 
DC  "O3'" "HO3'" sing N N 138 
DC  "C2'" "C1'"  sing N N 139 
DC  "C2'" "H2'"  sing N N 140 
DC  "C2'" "H2''" sing N N 141 
DC  "C1'" N1     sing N N 142 
DC  "C1'" "H1'"  sing N N 143 
DC  N1    C2     sing N N 144 
DC  N1    C6     sing N N 145 
DC  C2    O2     doub N N 146 
DC  C2    N3     sing N N 147 
DC  N3    C4     doub N N 148 
DC  C4    N4     sing N N 149 
DC  C4    C5     sing N N 150 
DC  N4    H41    sing N N 151 
DC  N4    H42    sing N N 152 
DC  C5    C6     doub N N 153 
DC  C5    H5     sing N N 154 
DC  C6    H6     sing N N 155 
DG  OP3   P      sing N N 156 
DG  OP3   HOP3   sing N N 157 
DG  P     OP1    doub N N 158 
DG  P     OP2    sing N N 159 
DG  P     "O5'"  sing N N 160 
DG  OP2   HOP2   sing N N 161 
DG  "O5'" "C5'"  sing N N 162 
DG  "C5'" "C4'"  sing N N 163 
DG  "C5'" "H5'"  sing N N 164 
DG  "C5'" "H5''" sing N N 165 
DG  "C4'" "O4'"  sing N N 166 
DG  "C4'" "C3'"  sing N N 167 
DG  "C4'" "H4'"  sing N N 168 
DG  "O4'" "C1'"  sing N N 169 
DG  "C3'" "O3'"  sing N N 170 
DG  "C3'" "C2'"  sing N N 171 
DG  "C3'" "H3'"  sing N N 172 
DG  "O3'" "HO3'" sing N N 173 
DG  "C2'" "C1'"  sing N N 174 
DG  "C2'" "H2'"  sing N N 175 
DG  "C2'" "H2''" sing N N 176 
DG  "C1'" N9     sing N N 177 
DG  "C1'" "H1'"  sing N N 178 
DG  N9    C8     sing Y N 179 
DG  N9    C4     sing Y N 180 
DG  C8    N7     doub Y N 181 
DG  C8    H8     sing N N 182 
DG  N7    C5     sing Y N 183 
DG  C5    C6     sing N N 184 
DG  C5    C4     doub Y N 185 
DG  C6    O6     doub N N 186 
DG  C6    N1     sing N N 187 
DG  N1    C2     sing N N 188 
DG  N1    H1     sing N N 189 
DG  C2    N2     sing N N 190 
DG  C2    N3     doub N N 191 
DG  N2    H21    sing N N 192 
DG  N2    H22    sing N N 193 
DG  N3    C4     sing N N 194 
DT  OP3   P      sing N N 195 
DT  OP3   HOP3   sing N N 196 
DT  P     OP1    doub N N 197 
DT  P     OP2    sing N N 198 
DT  P     "O5'"  sing N N 199 
DT  OP2   HOP2   sing N N 200 
DT  "O5'" "C5'"  sing N N 201 
DT  "C5'" "C4'"  sing N N 202 
DT  "C5'" "H5'"  sing N N 203 
DT  "C5'" "H5''" sing N N 204 
DT  "C4'" "O4'"  sing N N 205 
DT  "C4'" "C3'"  sing N N 206 
DT  "C4'" "H4'"  sing N N 207 
DT  "O4'" "C1'"  sing N N 208 
DT  "C3'" "O3'"  sing N N 209 
DT  "C3'" "C2'"  sing N N 210 
DT  "C3'" "H3'"  sing N N 211 
DT  "O3'" "HO3'" sing N N 212 
DT  "C2'" "C1'"  sing N N 213 
DT  "C2'" "H2'"  sing N N 214 
DT  "C2'" "H2''" sing N N 215 
DT  "C1'" N1     sing N N 216 
DT  "C1'" "H1'"  sing N N 217 
DT  N1    C2     sing N N 218 
DT  N1    C6     sing N N 219 
DT  C2    O2     doub N N 220 
DT  C2    N3     sing N N 221 
DT  N3    C4     sing N N 222 
DT  N3    H3     sing N N 223 
DT  C4    O4     doub N N 224 
DT  C4    C5     sing N N 225 
DT  C5    C7     sing N N 226 
DT  C5    C6     doub N N 227 
DT  C7    H71    sing N N 228 
DT  C7    H72    sing N N 229 
DT  C7    H73    sing N N 230 
DT  C6    H6     sing N N 231 
GLN N     CA     sing N N 232 
GLN N     H      sing N N 233 
GLN N     H2     sing N N 234 
GLN CA    C      sing N N 235 
GLN CA    CB     sing N N 236 
GLN CA    HA     sing N N 237 
GLN C     O      doub N N 238 
GLN C     OXT    sing N N 239 
GLN CB    CG     sing N N 240 
GLN CB    HB2    sing N N 241 
GLN CB    HB3    sing N N 242 
GLN CG    CD     sing N N 243 
GLN CG    HG2    sing N N 244 
GLN CG    HG3    sing N N 245 
GLN CD    OE1    doub N N 246 
GLN CD    NE2    sing N N 247 
GLN NE2   HE21   sing N N 248 
GLN NE2   HE22   sing N N 249 
GLN OXT   HXT    sing N N 250 
GLU N     CA     sing N N 251 
GLU N     H      sing N N 252 
GLU N     H2     sing N N 253 
GLU CA    C      sing N N 254 
GLU CA    CB     sing N N 255 
GLU CA    HA     sing N N 256 
GLU C     O      doub N N 257 
GLU C     OXT    sing N N 258 
GLU CB    CG     sing N N 259 
GLU CB    HB2    sing N N 260 
GLU CB    HB3    sing N N 261 
GLU CG    CD     sing N N 262 
GLU CG    HG2    sing N N 263 
GLU CG    HG3    sing N N 264 
GLU CD    OE1    doub N N 265 
GLU CD    OE2    sing N N 266 
GLU OE2   HE2    sing N N 267 
GLU OXT   HXT    sing N N 268 
GLY N     CA     sing N N 269 
GLY N     H      sing N N 270 
GLY N     H2     sing N N 271 
GLY CA    C      sing N N 272 
GLY CA    HA2    sing N N 273 
GLY CA    HA3    sing N N 274 
GLY C     O      doub N N 275 
GLY C     OXT    sing N N 276 
GLY OXT   HXT    sing N N 277 
GOL C1    O1     sing N N 278 
GOL C1    C2     sing N N 279 
GOL C1    H11    sing N N 280 
GOL C1    H12    sing N N 281 
GOL O1    HO1    sing N N 282 
GOL C2    O2     sing N N 283 
GOL C2    C3     sing N N 284 
GOL C2    H2     sing N N 285 
GOL O2    HO2    sing N N 286 
GOL C3    O3     sing N N 287 
GOL C3    H31    sing N N 288 
GOL C3    H32    sing N N 289 
GOL O3    HO3    sing N N 290 
HIS N     CA     sing N N 291 
HIS N     H      sing N N 292 
HIS N     H2     sing N N 293 
HIS CA    C      sing N N 294 
HIS CA    CB     sing N N 295 
HIS CA    HA     sing N N 296 
HIS C     O      doub N N 297 
HIS C     OXT    sing N N 298 
HIS CB    CG     sing N N 299 
HIS CB    HB2    sing N N 300 
HIS CB    HB3    sing N N 301 
HIS CG    ND1    sing Y N 302 
HIS CG    CD2    doub Y N 303 
HIS ND1   CE1    doub Y N 304 
HIS ND1   HD1    sing N N 305 
HIS CD2   NE2    sing Y N 306 
HIS CD2   HD2    sing N N 307 
HIS CE1   NE2    sing Y N 308 
HIS CE1   HE1    sing N N 309 
HIS NE2   HE2    sing N N 310 
HIS OXT   HXT    sing N N 311 
HOH O     H1     sing N N 312 
HOH O     H2     sing N N 313 
ILE N     CA     sing N N 314 
ILE N     H      sing N N 315 
ILE N     H2     sing N N 316 
ILE CA    C      sing N N 317 
ILE CA    CB     sing N N 318 
ILE CA    HA     sing N N 319 
ILE C     O      doub N N 320 
ILE C     OXT    sing N N 321 
ILE CB    CG1    sing N N 322 
ILE CB    CG2    sing N N 323 
ILE CB    HB     sing N N 324 
ILE CG1   CD1    sing N N 325 
ILE CG1   HG12   sing N N 326 
ILE CG1   HG13   sing N N 327 
ILE CG2   HG21   sing N N 328 
ILE CG2   HG22   sing N N 329 
ILE CG2   HG23   sing N N 330 
ILE CD1   HD11   sing N N 331 
ILE CD1   HD12   sing N N 332 
ILE CD1   HD13   sing N N 333 
ILE OXT   HXT    sing N N 334 
IMD N1    C2     sing Y N 335 
IMD N1    C5     sing Y N 336 
IMD N1    HN1    sing N N 337 
IMD C2    N3     doub Y N 338 
IMD C2    H2     sing N N 339 
IMD N3    C4     sing Y N 340 
IMD N3    HN3    sing N N 341 
IMD C4    C5     doub Y N 342 
IMD C4    H4     sing N N 343 
IMD C5    H5     sing N N 344 
LEU N     CA     sing N N 345 
LEU N     H      sing N N 346 
LEU N     H2     sing N N 347 
LEU CA    C      sing N N 348 
LEU CA    CB     sing N N 349 
LEU CA    HA     sing N N 350 
LEU C     O      doub N N 351 
LEU C     OXT    sing N N 352 
LEU CB    CG     sing N N 353 
LEU CB    HB2    sing N N 354 
LEU CB    HB3    sing N N 355 
LEU CG    CD1    sing N N 356 
LEU CG    CD2    sing N N 357 
LEU CG    HG     sing N N 358 
LEU CD1   HD11   sing N N 359 
LEU CD1   HD12   sing N N 360 
LEU CD1   HD13   sing N N 361 
LEU CD2   HD21   sing N N 362 
LEU CD2   HD22   sing N N 363 
LEU CD2   HD23   sing N N 364 
LEU OXT   HXT    sing N N 365 
LYS N     CA     sing N N 366 
LYS N     H      sing N N 367 
LYS N     H2     sing N N 368 
LYS CA    C      sing N N 369 
LYS CA    CB     sing N N 370 
LYS CA    HA     sing N N 371 
LYS C     O      doub N N 372 
LYS C     OXT    sing N N 373 
LYS CB    CG     sing N N 374 
LYS CB    HB2    sing N N 375 
LYS CB    HB3    sing N N 376 
LYS CG    CD     sing N N 377 
LYS CG    HG2    sing N N 378 
LYS CG    HG3    sing N N 379 
LYS CD    CE     sing N N 380 
LYS CD    HD2    sing N N 381 
LYS CD    HD3    sing N N 382 
LYS CE    NZ     sing N N 383 
LYS CE    HE2    sing N N 384 
LYS CE    HE3    sing N N 385 
LYS NZ    HZ1    sing N N 386 
LYS NZ    HZ2    sing N N 387 
LYS NZ    HZ3    sing N N 388 
LYS OXT   HXT    sing N N 389 
MET N     CA     sing N N 390 
MET N     H      sing N N 391 
MET N     H2     sing N N 392 
MET CA    C      sing N N 393 
MET CA    CB     sing N N 394 
MET CA    HA     sing N N 395 
MET C     O      doub N N 396 
MET C     OXT    sing N N 397 
MET CB    CG     sing N N 398 
MET CB    HB2    sing N N 399 
MET CB    HB3    sing N N 400 
MET CG    SD     sing N N 401 
MET CG    HG2    sing N N 402 
MET CG    HG3    sing N N 403 
MET SD    CE     sing N N 404 
MET CE    HE1    sing N N 405 
MET CE    HE2    sing N N 406 
MET CE    HE3    sing N N 407 
MET OXT   HXT    sing N N 408 
PHE N     CA     sing N N 409 
PHE N     H      sing N N 410 
PHE N     H2     sing N N 411 
PHE CA    C      sing N N 412 
PHE CA    CB     sing N N 413 
PHE CA    HA     sing N N 414 
PHE C     O      doub N N 415 
PHE C     OXT    sing N N 416 
PHE CB    CG     sing N N 417 
PHE CB    HB2    sing N N 418 
PHE CB    HB3    sing N N 419 
PHE CG    CD1    doub Y N 420 
PHE CG    CD2    sing Y N 421 
PHE CD1   CE1    sing Y N 422 
PHE CD1   HD1    sing N N 423 
PHE CD2   CE2    doub Y N 424 
PHE CD2   HD2    sing N N 425 
PHE CE1   CZ     doub Y N 426 
PHE CE1   HE1    sing N N 427 
PHE CE2   CZ     sing Y N 428 
PHE CE2   HE2    sing N N 429 
PHE CZ    HZ     sing N N 430 
PHE OXT   HXT    sing N N 431 
PRO N     CA     sing N N 432 
PRO N     CD     sing N N 433 
PRO N     H      sing N N 434 
PRO CA    C      sing N N 435 
PRO CA    CB     sing N N 436 
PRO CA    HA     sing N N 437 
PRO C     O      doub N N 438 
PRO C     OXT    sing N N 439 
PRO CB    CG     sing N N 440 
PRO CB    HB2    sing N N 441 
PRO CB    HB3    sing N N 442 
PRO CG    CD     sing N N 443 
PRO CG    HG2    sing N N 444 
PRO CG    HG3    sing N N 445 
PRO CD    HD2    sing N N 446 
PRO CD    HD3    sing N N 447 
PRO OXT   HXT    sing N N 448 
SER N     CA     sing N N 449 
SER N     H      sing N N 450 
SER N     H2     sing N N 451 
SER CA    C      sing N N 452 
SER CA    CB     sing N N 453 
SER CA    HA     sing N N 454 
SER C     O      doub N N 455 
SER C     OXT    sing N N 456 
SER CB    OG     sing N N 457 
SER CB    HB2    sing N N 458 
SER CB    HB3    sing N N 459 
SER OG    HG     sing N N 460 
SER OXT   HXT    sing N N 461 
THR N     CA     sing N N 462 
THR N     H      sing N N 463 
THR N     H2     sing N N 464 
THR CA    C      sing N N 465 
THR CA    CB     sing N N 466 
THR CA    HA     sing N N 467 
THR C     O      doub N N 468 
THR C     OXT    sing N N 469 
THR CB    OG1    sing N N 470 
THR CB    CG2    sing N N 471 
THR CB    HB     sing N N 472 
THR OG1   HG1    sing N N 473 
THR CG2   HG21   sing N N 474 
THR CG2   HG22   sing N N 475 
THR CG2   HG23   sing N N 476 
THR OXT   HXT    sing N N 477 
TRP N     CA     sing N N 478 
TRP N     H      sing N N 479 
TRP N     H2     sing N N 480 
TRP CA    C      sing N N 481 
TRP CA    CB     sing N N 482 
TRP CA    HA     sing N N 483 
TRP C     O      doub N N 484 
TRP C     OXT    sing N N 485 
TRP CB    CG     sing N N 486 
TRP CB    HB2    sing N N 487 
TRP CB    HB3    sing N N 488 
TRP CG    CD1    doub Y N 489 
TRP CG    CD2    sing Y N 490 
TRP CD1   NE1    sing Y N 491 
TRP CD1   HD1    sing N N 492 
TRP CD2   CE2    doub Y N 493 
TRP CD2   CE3    sing Y N 494 
TRP NE1   CE2    sing Y N 495 
TRP NE1   HE1    sing N N 496 
TRP CE2   CZ2    sing Y N 497 
TRP CE3   CZ3    doub Y N 498 
TRP CE3   HE3    sing N N 499 
TRP CZ2   CH2    doub Y N 500 
TRP CZ2   HZ2    sing N N 501 
TRP CZ3   CH2    sing Y N 502 
TRP CZ3   HZ3    sing N N 503 
TRP CH2   HH2    sing N N 504 
TRP OXT   HXT    sing N N 505 
TYR N     CA     sing N N 506 
TYR N     H      sing N N 507 
TYR N     H2     sing N N 508 
TYR CA    C      sing N N 509 
TYR CA    CB     sing N N 510 
TYR CA    HA     sing N N 511 
TYR C     O      doub N N 512 
TYR C     OXT    sing N N 513 
TYR CB    CG     sing N N 514 
TYR CB    HB2    sing N N 515 
TYR CB    HB3    sing N N 516 
TYR CG    CD1    doub Y N 517 
TYR CG    CD2    sing Y N 518 
TYR CD1   CE1    sing Y N 519 
TYR CD1   HD1    sing N N 520 
TYR CD2   CE2    doub Y N 521 
TYR CD2   HD2    sing N N 522 
TYR CE1   CZ     doub Y N 523 
TYR CE1   HE1    sing N N 524 
TYR CE2   CZ     sing Y N 525 
TYR CE2   HE2    sing N N 526 
TYR CZ    OH     sing N N 527 
TYR OH    HH     sing N N 528 
TYR OXT   HXT    sing N N 529 
VAL N     CA     sing N N 530 
VAL N     H      sing N N 531 
VAL N     H2     sing N N 532 
VAL CA    C      sing N N 533 
VAL CA    CB     sing N N 534 
VAL CA    HA     sing N N 535 
VAL C     O      doub N N 536 
VAL C     OXT    sing N N 537 
VAL CB    CG1    sing N N 538 
VAL CB    CG2    sing N N 539 
VAL CB    HB     sing N N 540 
VAL CG1   HG11   sing N N 541 
VAL CG1   HG12   sing N N 542 
VAL CG1   HG13   sing N N 543 
VAL CG2   HG21   sing N N 544 
VAL CG2   HG22   sing N N 545 
VAL CG2   HG23   sing N N 546 
VAL OXT   HXT    sing N N 547 
XG4 C2    N1     sing N N 548 
XG4 N1    C6     sing N N 549 
XG4 N1    HN1    sing N N 550 
XG4 N3    C2     doub N N 551 
XG4 N2    C2     sing N N 552 
XG4 N2    HN2    sing N N 553 
XG4 N2    HN2A   sing N N 554 
XG4 N3    C4     sing N N 555 
XG4 N9    C4     sing Y N 556 
XG4 C4    C5     doub Y N 557 
XG4 C5    N7     sing Y N 558 
XG4 C5    C6     sing N N 559 
XG4 C6    O6     doub N N 560 
XG4 C8    N7     doub Y N 561 
XG4 N9    C8     sing Y N 562 
XG4 C8    H8     sing N N 563 
XG4 "C1'" N9     sing N N 564 
XG4 "O5'" PA     sing N N 565 
XG4 O1A   PA     doub N N 566 
XG4 PA    O2A    sing N N 567 
XG4 PA    N3A    sing N N 568 
XG4 O1B   PB     doub N N 569 
XG4 N3A   PB     sing N N 570 
XG4 PB    O2B    sing N N 571 
XG4 PB    O3B    sing N N 572 
XG4 O1G   PG     doub N N 573 
XG4 PG    O3B    sing N N 574 
XG4 PG    O2G    sing N N 575 
XG4 PG    O3G    sing N N 576 
XG4 "O4'" "C1'"  sing N N 577 
XG4 "C1'" "C2'"  sing N N 578 
XG4 "C1'" "H1'"  sing N N 579 
XG4 "C2'" "C3'"  sing N N 580 
XG4 "C2'" "H2'"  sing N N 581 
XG4 "C2'" "H2'A" sing N N 582 
XG4 O2A   HO2A   sing N N 583 
XG4 O2B   HO2B   sing N N 584 
XG4 O2G   HO2G   sing N N 585 
XG4 "C4'" "C3'"  sing N N 586 
XG4 "C3'" "O3'"  sing N N 587 
XG4 "C3'" "H3'"  sing N N 588 
XG4 "O3'" "HO3'" sing N N 589 
XG4 N3A   HN3A   sing N N 590 
XG4 O3G   HO3G   sing N N 591 
XG4 "O4'" "C4'"  sing N N 592 
XG4 "C4'" "C5'"  sing N N 593 
XG4 "C4'" "H4'"  sing N N 594 
XG4 "C5'" "O5'"  sing N N 595 
XG4 "C5'" "H5'"  sing N N 596 
XG4 "C5'" "H5'A" sing N N 597 
# 
loop_
_ndb_struct_conf_na.entry_id 
_ndb_struct_conf_na.feature 
8S84 'double helix'        
8S84 '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 DG 1  1_555 C DC 16 1_555 -0.893 -0.390 -0.017 -18.017 -9.191  1.733  1  P_DG1:DC16_T P 1  ? T 16 ? 19 1 
1 B DA 2  1_555 C DT 15 1_555 -0.415 -0.392 0.145  -7.647  -15.113 4.857  2  P_DA2:DT15_T P 2  ? T 15 ? 20 1 
1 B DC 3  1_555 C DG 14 1_555 0.531  -0.474 0.924  -12.414 -8.324  -5.249 3  P_DC3:DG14_T P 3  ? T 14 ? 19 1 
1 B DC 4  1_555 C DG 13 1_555 -0.372 -0.320 0.812  -6.400  -5.619  4.038  4  P_DC4:DG13_T P 4  ? T 13 ? 19 1 
1 B DA 5  1_555 C DT 12 1_555 0.477  -0.211 0.149  0.720   -13.505 -4.630 5  P_DA5:DT12_T P 5  ? T 12 ? 20 1 
1 B DC 6  1_555 C DG 11 1_555 0.688  -0.384 0.280  3.042   -11.508 -1.559 6  P_DC6:DG11_T P 6  ? T 11 ? 19 1 
1 B DG 7  1_555 C DC 10 1_555 -0.200 -0.115 0.167  -9.395  -10.185 0.480  7  P_DG7:DC10_T P 7  ? T 10 ? 19 1 
1 B DG 8  1_555 C DC 9  1_555 0.018  0.009  0.239  -1.697  -13.426 8.079  8  P_DG8:DC9_T  P 8  ? T 9  ? 19 1 
1 B DC 9  1_555 C DG 8  1_555 0.068  -0.044 0.221  -3.243  -6.143  -1.823 9  P_DC9:DG8_T  P 9  ? T 8  ? 19 1 
1 B DC 10 1_555 C DG 7  1_555 0.078  0.149  -0.131 18.335  -5.133  5.254  10 P_DC10:DG7_T P 10 ? T 7  ? 19 1 
1 B DA 11 1_555 C DT 6  1_555 0.223  -0.341 -0.389 1.068   -8.778  0.531  11 P_DA11:DT6_T P 11 ? T 6  ? 20 1 
1 B DC 12 1_555 C DG 5  1_555 0.049  -0.295 -0.392 -0.581  0.809   -1.877 12 P_DC12:DG5_T P 12 ? T 5  ? 19 1 
1 B DA 13 1_555 C DT 4  1_555 0.371  -0.245 -0.010 8.575   -4.944  7.583  13 P_DA13:DT4_T P 13 ? T 4  ? 20 1 
# 
loop_
_ndb_struct_na_base_pair_step.model_number 
_ndb_struct_na_base_pair_step.i_label_asym_id_1 
_ndb_struct_na_base_pair_step.i_label_comp_id_1 
_ndb_struct_na_base_pair_step.i_label_seq_id_1 
_ndb_struct_na_base_pair_step.i_symmetry_1 
_ndb_struct_na_base_pair_step.j_label_asym_id_1 
_ndb_struct_na_base_pair_step.j_label_comp_id_1 
_ndb_struct_na_base_pair_step.j_label_seq_id_1 
_ndb_struct_na_base_pair_step.j_symmetry_1 
_ndb_struct_na_base_pair_step.i_label_asym_id_2 
_ndb_struct_na_base_pair_step.i_label_comp_id_2 
_ndb_struct_na_base_pair_step.i_label_seq_id_2 
_ndb_struct_na_base_pair_step.i_symmetry_2 
_ndb_struct_na_base_pair_step.j_label_asym_id_2 
_ndb_struct_na_base_pair_step.j_label_comp_id_2 
_ndb_struct_na_base_pair_step.j_label_seq_id_2 
_ndb_struct_na_base_pair_step.j_symmetry_2 
_ndb_struct_na_base_pair_step.shift 
_ndb_struct_na_base_pair_step.slide 
_ndb_struct_na_base_pair_step.rise 
_ndb_struct_na_base_pair_step.tilt 
_ndb_struct_na_base_pair_step.roll 
_ndb_struct_na_base_pair_step.twist 
_ndb_struct_na_base_pair_step.x_displacement 
_ndb_struct_na_base_pair_step.y_displacement 
_ndb_struct_na_base_pair_step.helical_rise 
_ndb_struct_na_base_pair_step.inclination 
_ndb_struct_na_base_pair_step.tip 
_ndb_struct_na_base_pair_step.helical_twist 
_ndb_struct_na_base_pair_step.step_number 
_ndb_struct_na_base_pair_step.step_name 
_ndb_struct_na_base_pair_step.i_auth_asym_id_1 
_ndb_struct_na_base_pair_step.i_auth_seq_id_1 
_ndb_struct_na_base_pair_step.i_PDB_ins_code_1 
_ndb_struct_na_base_pair_step.j_auth_asym_id_1 
_ndb_struct_na_base_pair_step.j_auth_seq_id_1 
_ndb_struct_na_base_pair_step.j_PDB_ins_code_1 
_ndb_struct_na_base_pair_step.i_auth_asym_id_2 
_ndb_struct_na_base_pair_step.i_auth_seq_id_2 
_ndb_struct_na_base_pair_step.i_PDB_ins_code_2 
_ndb_struct_na_base_pair_step.j_auth_asym_id_2 
_ndb_struct_na_base_pair_step.j_auth_seq_id_2 
_ndb_struct_na_base_pair_step.j_PDB_ins_code_2 
1 B DG 1  1_555 C DC 16 1_555 B DA 2  1_555 C DT 15 1_555 -0.852 1.717  3.133 -6.730 1.978  37.033 2.404  0.452  3.316 3.081  
10.480 37.668 1  PP_DG1DA2:DT15DC16_TT P 1  ? T 16 ? P 2  ? T 15 ? 
1 B DA 2  1_555 C DT 15 1_555 B DC 3  1_555 C DG 14 1_555 -0.208 -0.377 3.463 -7.930 2.823  40.935 -0.843 -0.593 3.411 3.985  
11.196 41.755 2  PP_DA2DC3:DG14DT15_TT P 2  ? T 15 ? P 3  ? T 14 ? 
1 B DC 3  1_555 C DG 14 1_555 B DC 4  1_555 C DG 13 1_555 0.641  -0.619 3.273 1.969  -0.193 27.894 -1.235 -0.855 3.313 -0.400 
-4.077 27.962 3  PP_DC3DC4:DG13DG14_TT P 3  ? T 14 ? P 4  ? T 13 ? 
1 B DC 4  1_555 C DG 13 1_555 B DA 5  1_555 C DT 12 1_555 -0.656 1.408  3.315 3.364  -5.294 43.605 2.368  1.186  3.076 -7.082 
-4.500 44.032 4  PP_DC4DA5:DT12DG13_TT P 4  ? T 13 ? P 5  ? T 12 ? 
1 B DA 5  1_555 C DT 12 1_555 B DC 6  1_555 C DG 11 1_555 0.088  -0.582 3.274 -0.060 6.892  31.851 -2.219 -0.168 3.083 12.378 
0.107  32.569 5  PP_DA5DC6:DG11DT12_TT P 5  ? T 12 ? P 6  ? T 11 ? 
1 B DC 6  1_555 C DG 11 1_555 B DG 7  1_555 C DC 10 1_555 -0.188 1.552  3.709 -1.114 -2.405 39.405 2.615  0.132  3.616 -3.562 
1.650  39.491 6  PP_DC6DG7:DC10DG11_TT P 6  ? T 11 ? P 7  ? T 10 ? 
1 B DG 7  1_555 C DC 10 1_555 B DG 8  1_555 C DC 9  1_555 1.079  0.154  3.253 -0.872 7.635  32.750 -0.978 -2.008 3.179 13.313 
1.520  33.616 7  PP_DG7DG8:DC9DC10_TT  P 7  ? T 10 ? P 8  ? T 9  ? 
1 B DG 8  1_555 C DC 9  1_555 B DC 9  1_555 C DG 8  1_555 -0.554 -0.558 3.372 1.505  7.652  28.982 -2.663 1.382  3.094 14.950 
-2.941 29.992 8  PP_DG8DC9:DG8DC9_TT   P 8  ? T 9  ? P 9  ? T 8  ? 
1 B DC 9  1_555 C DG 8  1_555 B DC 10 1_555 C DG 7  1_555 1.233  0.119  2.877 2.982  2.031  32.041 -0.110 -1.744 2.979 3.665  
-5.381 32.238 9  PP_DC9DC10:DG7DG8_TT  P 9  ? T 8  ? P 10 ? T 7  ? 
1 B DC 10 1_555 C DG 7  1_555 B DA 11 1_555 C DT 6  1_555 -0.724 -1.066 3.770 -1.669 8.431  29.785 -3.811 0.996  3.383 15.987 
3.166  30.973 10 PP_DC10DA11:DT6DG7_TT P 10 ? T 7  ? P 11 ? T 6  ? 
1 B DA 11 1_555 C DT 6  1_555 B DC 12 1_555 C DG 5  1_555 -0.366 -0.958 3.571 -0.471 0.297  35.842 -1.603 0.521  3.568 0.482  
0.765  35.846 11 PP_DA11DC12:DG5DT6_TT P 11 ? T 6  ? P 12 ? T 5  ? 
1 B DC 12 1_555 C DG 5  1_555 B DA 13 1_555 C DT 4  1_555 0.348  -0.445 3.178 -4.185 9.326  32.085 -2.212 -1.250 2.873 16.363 
7.342  33.633 12 PP_DC12DA13:DT4DG5_TT P 12 ? T 5  ? P 13 ? T 4  ? 
# 
_pdbx_audit_support.funding_organization   'German Research Foundation (DFG)' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5OMF 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8S84 
_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]   0.009011 
_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]   0.006559 
_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]   0.014260 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
MN 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . MET A 1 1   ? 22.204  49.333  18.922  1.00 78.56  ? 1   MET A N     1 
ATOM   2    C  CA    . MET A 1 1   ? 22.554  47.924  18.785  1.00 74.56  ? 1   MET A CA    1 
ATOM   3    C  C     . MET A 1 1   ? 21.722  47.260  17.695  1.00 66.89  ? 1   MET A C     1 
ATOM   4    O  O     . MET A 1 1   ? 20.493  47.270  17.748  1.00 74.61  ? 1   MET A O     1 
ATOM   5    C  CB    . MET A 1 1   ? 22.362  47.189  20.112  1.00 68.92  ? 1   MET A CB    1 
ATOM   6    C  CG    . MET A 1 1   ? 22.556  45.684  20.020  1.00 70.46  ? 1   MET A CG    1 
ATOM   7    S  SD    . MET A 1 1   ? 22.141  44.838  21.557  1.00 78.59  ? 1   MET A SD    1 
ATOM   8    C  CE    . MET A 1 1   ? 23.766  44.612  22.270  1.00 64.63  ? 1   MET A CE    1 
ATOM   9    N  N     . ILE A 1 2   ? 22.400  46.685  16.707  1.00 70.19  ? 2   ILE A N     1 
ATOM   10   C  CA    . ILE A 1 2   ? 21.721  46.012  15.607  1.00 67.09  ? 2   ILE A CA    1 
ATOM   11   C  C     . ILE A 1 2   ? 21.223  44.655  16.085  1.00 68.23  ? 2   ILE A C     1 
ATOM   12   O  O     . ILE A 1 2   ? 21.959  43.902  16.733  1.00 65.99  ? 2   ILE A O     1 
ATOM   13   C  CB    . ILE A 1 2   ? 22.656  45.865  14.397  1.00 57.95  ? 2   ILE A CB    1 
ATOM   14   C  CG1   . ILE A 1 2   ? 23.177  47.236  13.957  1.00 49.07  ? 2   ILE A CG1   1 
ATOM   15   C  CG2   . ILE A 1 2   ? 21.942  45.149  13.258  1.00 62.82  ? 2   ILE A CG2   1 
ATOM   16   C  CD1   . ILE A 1 2   ? 23.582  47.310  12.495  1.00 60.45  ? 2   ILE A CD1   1 
ATOM   17   N  N     . LEU A 1 3   ? 19.968  44.343  15.767  1.00 65.28  ? 3   LEU A N     1 
ATOM   18   C  CA    . LEU A 1 3   ? 19.366  43.064  16.123  1.00 58.78  ? 3   LEU A CA    1 
ATOM   19   C  C     . LEU A 1 3   ? 19.319  42.099  14.945  1.00 65.68  ? 3   LEU A C     1 
ATOM   20   O  O     . LEU A 1 3   ? 19.682  40.926  15.085  1.00 68.57  ? 3   LEU A O     1 
ATOM   21   C  CB    . LEU A 1 3   ? 17.950  43.284  16.667  1.00 54.99  ? 3   LEU A CB    1 
ATOM   22   C  CG    . LEU A 1 3   ? 17.790  44.256  17.837  1.00 52.46  ? 3   LEU A CG    1 
ATOM   23   C  CD1   . LEU A 1 3   ? 16.368  44.214  18.373  1.00 60.08  ? 3   LEU A CD1   1 
ATOM   24   C  CD2   . LEU A 1 3   ? 18.786  43.934  18.937  1.00 65.09  ? 3   LEU A CD2   1 
ATOM   25   N  N     . ASP A 1 4   ? 18.886  42.579  13.784  1.00 48.33  ? 4   ASP A N     1 
ATOM   26   C  CA    . ASP A 1 4   ? 18.649  41.737  12.619  1.00 54.42  ? 4   ASP A CA    1 
ATOM   27   C  C     . ASP A 1 4   ? 18.506  42.651  11.410  1.00 54.76  ? 4   ASP A C     1 
ATOM   28   O  O     . ASP A 1 4   ? 18.329  43.864  11.544  1.00 59.32  ? 4   ASP A O     1 
ATOM   29   C  CB    . ASP A 1 4   ? 17.399  40.868  12.813  1.00 60.24  ? 4   ASP A CB    1 
ATOM   30   C  CG    . ASP A 1 4   ? 17.242  39.807  11.739  1.00 73.01  ? 4   ASP A CG    1 
ATOM   31   O  OD1   . ASP A 1 4   ? 18.263  39.219  11.324  1.00 60.85  ? 4   ASP A OD1   1 
ATOM   32   O  OD2   . ASP A 1 4   ? 16.093  39.559  11.311  1.00 90.17  ? 4   ASP A OD2   1 
ATOM   33   N  N     . THR A 1 5   ? 18.602  42.056  10.224  1.00 55.37  ? 5   THR A N     1 
ATOM   34   C  CA    . THR A 1 5   ? 18.337  42.761  8.979   1.00 53.92  ? 5   THR A CA    1 
ATOM   35   C  C     . THR A 1 5   ? 17.513  41.869  8.065   1.00 56.36  ? 5   THR A C     1 
ATOM   36   O  O     . THR A 1 5   ? 17.692  40.648  8.049   1.00 71.60  ? 5   THR A O     1 
ATOM   37   C  CB    . THR A 1 5   ? 19.625  43.172  8.248   1.00 49.26  ? 5   THR A CB    1 
ATOM   38   O  OG1   . THR A 1 5   ? 20.419  42.009  7.979   1.00 49.90  ? 5   THR A OG1   1 
ATOM   39   C  CG2   . THR A 1 5   ? 20.435  44.170  9.070   1.00 44.56  ? 5   THR A CG2   1 
ATOM   40   N  N     . ASP A 1 6   ? 16.602  42.485  7.320   1.00 51.00  ? 6   ASP A N     1 
ATOM   41   C  CA    . ASP A 1 6   ? 15.906  41.824  6.226   1.00 54.68  ? 6   ASP A CA    1 
ATOM   42   C  C     . ASP A 1 6   ? 15.627  42.873  5.156   1.00 55.33  ? 6   ASP A C     1 
ATOM   43   O  O     . ASP A 1 6   ? 16.129  43.998  5.223   1.00 56.19  ? 6   ASP A O     1 
ATOM   44   C  CB    . ASP A 1 6   ? 14.641  41.106  6.725   1.00 58.82  ? 6   ASP A CB    1 
ATOM   45   C  CG    . ASP A 1 6   ? 13.520  42.061  7.114   1.00 62.35  ? 6   ASP A CG    1 
ATOM   46   O  OD1   . ASP A 1 6   ? 13.769  43.272  7.282   1.00 68.96  ? 6   ASP A OD1   1 
ATOM   47   O  OD2   . ASP A 1 6   ? 12.371  41.588  7.248   1.00 65.66  ? 6   ASP A OD2   1 
ATOM   48   N  N     . TYR A 1 7   ? 14.827  42.508  4.159   1.00 54.30  ? 7   TYR A N     1 
ATOM   49   C  CA    . TYR A 1 7   ? 14.458  43.458  3.123   1.00 57.22  ? 7   TYR A CA    1 
ATOM   50   C  C     . TYR A 1 7   ? 13.016  43.232  2.697   1.00 57.95  ? 7   TYR A C     1 
ATOM   51   O  O     . TYR A 1 7   ? 12.492  42.118  2.776   1.00 54.85  ? 7   TYR A O     1 
ATOM   52   C  CB    . TYR A 1 7   ? 15.397  43.372  1.907   1.00 56.80  ? 7   TYR A CB    1 
ATOM   53   C  CG    . TYR A 1 7   ? 15.132  42.215  0.966   1.00 58.08  ? 7   TYR A CG    1 
ATOM   54   C  CD1   . TYR A 1 7   ? 15.683  40.963  1.203   1.00 53.50  ? 7   TYR A CD1   1 
ATOM   55   C  CD2   . TYR A 1 7   ? 14.353  42.383  -0.173  1.00 62.95  ? 7   TYR A CD2   1 
ATOM   56   C  CE1   . TYR A 1 7   ? 15.452  39.906  0.340   1.00 53.46  ? 7   TYR A CE1   1 
ATOM   57   C  CE2   . TYR A 1 7   ? 14.117  41.333  -1.039  1.00 56.66  ? 7   TYR A CE2   1 
ATOM   58   C  CZ    . TYR A 1 7   ? 14.669  40.097  -0.778  1.00 50.62  ? 7   TYR A CZ    1 
ATOM   59   O  OH    . TYR A 1 7   ? 14.437  39.050  -1.639  1.00 66.14  ? 7   TYR A OH    1 
ATOM   60   N  N     . ILE A 1 8   ? 12.379  44.316  2.266   1.00 60.12  ? 8   ILE A N     1 
ATOM   61   C  CA    . ILE A 1 8   ? 11.066  44.275  1.646   1.00 56.12  ? 8   ILE A CA    1 
ATOM   62   C  C     . ILE A 1 8   ? 11.207  44.812  0.227   1.00 60.62  ? 8   ILE A C     1 
ATOM   63   O  O     . ILE A 1 8   ? 12.250  45.339  -0.160  1.00 68.14  ? 8   ILE A O     1 
ATOM   64   C  CB    . ILE A 1 8   ? 10.013  45.077  2.435   1.00 53.33  ? 8   ILE A CB    1 
ATOM   65   C  CG1   . ILE A 1 8   ? 10.406  46.554  2.491   1.00 57.04  ? 8   ILE A CG1   1 
ATOM   66   C  CG2   . ILE A 1 8   ? 9.843   44.504  3.834   1.00 57.01  ? 8   ILE A CG2   1 
ATOM   67   C  CD1   . ILE A 1 8   ? 9.583   47.366  3.460   1.00 61.02  ? 8   ILE A CD1   1 
ATOM   68   N  N     . THR A 1 9   ? 10.139  44.672  -0.551  1.00 62.80  ? 9   THR A N     1 
ATOM   69   C  CA    . THR A 1 9   ? 10.128  45.115  -1.939  1.00 53.28  ? 9   THR A CA    1 
ATOM   70   C  C     . THR A 1 9   ? 9.102   46.229  -2.093  1.00 59.72  ? 9   THR A C     1 
ATOM   71   O  O     . THR A 1 9   ? 7.897   45.999  -1.937  1.00 72.11  ? 9   THR A O     1 
ATOM   72   C  CB    . THR A 1 9   ? 9.830   43.954  -2.886  1.00 59.80  ? 9   THR A CB    1 
ATOM   73   O  OG1   . THR A 1 9   ? 10.666  42.838  -2.549  1.00 56.44  ? 9   THR A OG1   1 
ATOM   74   C  CG2   . THR A 1 9   ? 10.097  44.366  -4.318  1.00 59.68  ? 9   THR A CG2   1 
ATOM   75   N  N     . GLU A 1 10  ? 9.581   47.432  -2.396  1.00 67.36  ? 10  GLU A N     1 
ATOM   76   C  CA    . GLU A 1 10  ? 8.736   48.595  -2.641  1.00 56.09  ? 10  GLU A CA    1 
ATOM   77   C  C     . GLU A 1 10  ? 8.784   48.902  -4.132  1.00 59.69  ? 10  GLU A C     1 
ATOM   78   O  O     . GLU A 1 10  ? 9.796   49.401  -4.636  1.00 61.35  ? 10  GLU A O     1 
ATOM   79   C  CB    . GLU A 1 10  ? 9.196   49.789  -1.807  1.00 56.57  ? 10  GLU A CB    1 
ATOM   80   C  CG    . GLU A 1 10  ? 8.590   51.121  -2.228  1.00 75.32  ? 10  GLU A CG    1 
ATOM   81   C  CD    . GLU A 1 10  ? 8.829   52.218  -1.207  1.00 82.90  ? 10  GLU A CD    1 
ATOM   82   O  OE1   . GLU A 1 10  ? 9.005   51.894  -0.014  1.00 79.77  ? 10  GLU A OE1   1 
ATOM   83   O  OE2   . GLU A 1 10  ? 8.834   53.406  -1.595  1.00 100.94 ? 10  GLU A OE2   1 
ATOM   84   N  N     . ASP A 1 11  ? 7.694   48.587  -4.834  1.00 63.77  ? 11  ASP A N     1 
ATOM   85   C  CA    . ASP A 1 11  ? 7.578   48.832  -6.273  1.00 61.88  ? 11  ASP A CA    1 
ATOM   86   C  C     . ASP A 1 11  ? 8.722   48.173  -7.042  1.00 56.82  ? 11  ASP A C     1 
ATOM   87   O  O     . ASP A 1 11  ? 9.369   48.787  -7.892  1.00 54.25  ? 11  ASP A O     1 
ATOM   88   C  CB    . ASP A 1 11  ? 7.507   50.332  -6.570  1.00 60.55  ? 11  ASP A CB    1 
ATOM   89   C  CG    . ASP A 1 11  ? 6.115   50.896  -6.377  1.00 81.31  ? 11  ASP A CG    1 
ATOM   90   O  OD1   . ASP A 1 11  ? 5.214   50.547  -7.171  1.00 64.10  ? 11  ASP A OD1   1 
ATOM   91   O  OD2   . ASP A 1 11  ? 5.922   51.689  -5.431  1.00 84.42  ? 11  ASP A OD2   1 
ATOM   92   N  N     . GLY A 1 12  ? 8.972   46.903  -6.732  1.00 60.77  ? 12  GLY A N     1 
ATOM   93   C  CA    . GLY A 1 12  ? 9.991   46.136  -7.414  1.00 56.18  ? 12  GLY A CA    1 
ATOM   94   C  C     . GLY A 1 12  ? 11.415  46.435  -7.003  1.00 70.03  ? 12  GLY A C     1 
ATOM   95   O  O     . GLY A 1 12  ? 12.341  45.837  -7.567  1.00 70.06  ? 12  GLY A O     1 
ATOM   96   N  N     . LYS A 1 13  ? 11.625  47.331  -6.036  1.00 70.07  ? 13  LYS A N     1 
ATOM   97   C  CA    . LYS A 1 13  ? 12.959  47.734  -5.627  1.00 55.00  ? 13  LYS A CA    1 
ATOM   98   C  C     . LYS A 1 13  ? 13.248  47.280  -4.200  1.00 62.28  ? 13  LYS A C     1 
ATOM   99   O  O     . LYS A 1 13  ? 12.389  47.415  -3.321  1.00 61.79  ? 13  LYS A O     1 
ATOM   100  C  CB    . LYS A 1 13  ? 13.119  49.257  -5.721  1.00 63.92  ? 13  LYS A CB    1 
ATOM   101  C  CG    . LYS A 1 13  ? 13.328  49.773  -7.142  1.00 61.94  ? 13  LYS A CG    1 
ATOM   102  C  CD    . LYS A 1 13  ? 13.916  51.179  -7.148  1.00 99.54  ? 13  LYS A CD    1 
ATOM   103  C  CE    . LYS A 1 13  ? 15.312  51.204  -6.540  1.00 96.35  ? 13  LYS A CE    1 
ATOM   104  N  NZ    . LYS A 1 13  ? 15.591  52.483  -5.827  1.00 81.82  ? 13  LYS A NZ    1 
ATOM   105  N  N     . PRO A 1 14  ? 14.442  46.748  -3.940  1.00 67.22  ? 14  PRO A N     1 
ATOM   106  C  CA    . PRO A 1 14  ? 14.742  46.221  -2.603  1.00 45.41  ? 14  PRO A CA    1 
ATOM   107  C  C     . PRO A 1 14  ? 14.967  47.341  -1.601  1.00 50.19  ? 14  PRO A C     1 
ATOM   108  O  O     . PRO A 1 14  ? 15.559  48.375  -1.919  1.00 59.09  ? 14  PRO A O     1 
ATOM   109  C  CB    . PRO A 1 14  ? 16.025  45.406  -2.817  1.00 63.16  ? 14  PRO A CB    1 
ATOM   110  C  CG    . PRO A 1 14  ? 16.263  45.400  -4.312  1.00 67.04  ? 14  PRO A CG    1 
ATOM   111  C  CD    . PRO A 1 14  ? 15.585  46.604  -4.851  1.00 68.66  ? 14  PRO A CD    1 
ATOM   112  N  N     . VAL A 1 15  ? 14.486  47.124  -0.378  1.00 52.02  ? 15  VAL A N     1 
ATOM   113  C  CA    . VAL A 1 15  ? 14.608  48.088  0.710   1.00 45.18  ? 15  VAL A CA    1 
ATOM   114  C  C     . VAL A 1 15  ? 15.095  47.337  1.940   1.00 63.22  ? 15  VAL A C     1 
ATOM   115  O  O     . VAL A 1 15  ? 14.339  46.563  2.539   1.00 65.38  ? 15  VAL A O     1 
ATOM   116  C  CB    . VAL A 1 15  ? 13.285  48.808  1.009   1.00 57.89  ? 15  VAL A CB    1 
ATOM   117  C  CG1   . VAL A 1 15  ? 13.525  49.980  1.950   1.00 58.23  ? 15  VAL A CG1   1 
ATOM   118  C  CG2   . VAL A 1 15  ? 12.616  49.277  -0.277  1.00 53.45  ? 15  VAL A CG2   1 
ATOM   119  N  N     . ILE A 1 16  ? 16.350  47.569  2.325   1.00 51.24  ? 16  ILE A N     1 
ATOM   120  C  CA    . ILE A 1 16  ? 16.900  46.935  3.515   1.00 50.76  ? 16  ILE A CA    1 
ATOM   121  C  C     . ILE A 1 16  ? 16.272  47.550  4.760   1.00 52.18  ? 16  ILE A C     1 
ATOM   122  O  O     . ILE A 1 16  ? 16.124  48.775  4.865   1.00 49.11  ? 16  ILE A O     1 
ATOM   123  C  CB    . ILE A 1 16  ? 18.433  47.080  3.535   1.00 58.03  ? 16  ILE A CB    1 
ATOM   124  C  CG1   . ILE A 1 16  ? 19.086  46.069  2.590   1.00 51.94  ? 16  ILE A CG1   1 
ATOM   125  C  CG2   . ILE A 1 16  ? 18.977  46.908  4.944   1.00 45.69  ? 16  ILE A CG2   1 
ATOM   126  C  CD1   . ILE A 1 16  ? 19.128  44.657  3.139   1.00 48.23  ? 16  ILE A CD1   1 
ATOM   127  N  N     . ARG A 1 17  ? 15.886  46.698  5.707   1.00 53.28  ? 17  ARG A N     1 
ATOM   128  C  CA    . ARG A 1 17  ? 15.471  47.125  7.037   1.00 54.16  ? 17  ARG A CA    1 
ATOM   129  C  C     . ARG A 1 17  ? 16.535  46.710  8.042   1.00 57.63  ? 17  ARG A C     1 
ATOM   130  O  O     . ARG A 1 17  ? 16.991  45.562  8.027   1.00 61.44  ? 17  ARG A O     1 
ATOM   131  C  CB    . ARG A 1 17  ? 14.127  46.513  7.437   1.00 61.55  ? 17  ARG A CB    1 
ATOM   132  C  CG    . ARG A 1 17  ? 12.921  47.022  6.677   1.00 57.66  ? 17  ARG A CG    1 
ATOM   133  C  CD    . ARG A 1 17  ? 11.955  45.884  6.428   1.00 55.47  ? 17  ARG A CD    1 
ATOM   134  N  NE    . ARG A 1 17  ? 10.847  45.893  7.373   1.00 64.05  ? 17  ARG A NE    1 
ATOM   135  C  CZ    . ARG A 1 17  ? 10.185  44.810  7.759   1.00 60.20  ? 17  ARG A CZ    1 
ATOM   136  N  NH1   . ARG A 1 17  ? 10.509  43.607  7.315   1.00 63.67  ? 17  ARG A NH1   1 
ATOM   137  N  NH2   . ARG A 1 17  ? 9.176   44.938  8.615   1.00 67.14  ? 17  ARG A NH2   1 
ATOM   138  N  N     . ILE A 1 18  ? 16.925  47.635  8.914   1.00 52.24  ? 18  ILE A N     1 
ATOM   139  C  CA    . ILE A 1 18  ? 17.847  47.348  10.008  1.00 61.57  ? 18  ILE A CA    1 
ATOM   140  C  C     . ILE A 1 18  ? 17.088  47.533  11.314  1.00 63.02  ? 18  ILE A C     1 
ATOM   141  O  O     . ILE A 1 18  ? 16.654  48.647  11.637  1.00 64.07  ? 18  ILE A O     1 
ATOM   142  C  CB    . ILE A 1 18  ? 19.098  48.239  9.958   1.00 65.45  ? 18  ILE A CB    1 
ATOM   143  C  CG1   . ILE A 1 18  ? 19.806  48.101  8.609   1.00 55.69  ? 18  ILE A CG1   1 
ATOM   144  C  CG2   . ILE A 1 18  ? 20.056  47.875  11.083  1.00 52.93  ? 18  ILE A CG2   1 
ATOM   145  C  CD1   . ILE A 1 18  ? 19.544  49.251  7.664   1.00 52.64  ? 18  ILE A CD1   1 
ATOM   146  N  N     . PHE A 1 19  ? 16.922  46.443  12.060  1.00 58.48  ? 19  PHE A N     1 
ATOM   147  C  CA    . PHE A 1 19  ? 16.170  46.457  13.315  1.00 65.55  ? 19  PHE A CA    1 
ATOM   148  C  C     . PHE A 1 19  ? 17.139  46.781  14.444  1.00 55.00  ? 19  PHE A C     1 
ATOM   149  O  O     . PHE A 1 19  ? 17.891  45.918  14.900  1.00 68.80  ? 19  PHE A O     1 
ATOM   150  C  CB    . PHE A 1 19  ? 15.474  45.120  13.541  1.00 54.61  ? 19  PHE A CB    1 
ATOM   151  C  CG    . PHE A 1 19  ? 14.445  44.790  12.500  1.00 54.54  ? 19  PHE A CG    1 
ATOM   152  C  CD1   . PHE A 1 19  ? 13.210  45.417  12.501  1.00 67.66  ? 19  PHE A CD1   1 
ATOM   153  C  CD2   . PHE A 1 19  ? 14.716  43.854  11.516  1.00 52.75  ? 19  PHE A CD2   1 
ATOM   154  C  CE1   . PHE A 1 19  ? 12.263  45.114  11.540  1.00 61.61  ? 19  PHE A CE1   1 
ATOM   155  C  CE2   . PHE A 1 19  ? 13.774  43.547  10.552  1.00 66.48  ? 19  PHE A CE2   1 
ATOM   156  C  CZ    . PHE A 1 19  ? 12.546  44.177  10.564  1.00 58.76  ? 19  PHE A CZ    1 
ATOM   157  N  N     . LYS A 1 20  ? 17.121  48.027  14.899  1.00 66.83  ? 20  LYS A N     1 
ATOM   158  C  CA    . LYS A 1 20  ? 18.045  48.484  15.923  1.00 72.95  ? 20  LYS A CA    1 
ATOM   159  C  C     . LYS A 1 20  ? 17.339  48.641  17.264  1.00 73.03  ? 20  LYS A C     1 
ATOM   160  O  O     . LYS A 1 20  ? 16.109  48.665  17.354  1.00 66.45  ? 20  LYS A O     1 
ATOM   161  C  CB    . LYS A 1 20  ? 18.693  49.812  15.515  1.00 70.14  ? 20  LYS A CB    1 
ATOM   162  C  CG    . LYS A 1 20  ? 19.307  49.805  14.124  1.00 72.16  ? 20  LYS A CG    1 
ATOM   163  C  CD    . LYS A 1 20  ? 20.367  50.886  13.980  1.00 77.17  ? 20  LYS A CD    1 
ATOM   164  C  CE    . LYS A 1 20  ? 19.741  52.235  13.668  1.00 86.74  ? 20  LYS A CE    1 
ATOM   165  N  NZ    . LYS A 1 20  ? 20.716  53.155  13.018  1.00 92.09  ? 20  LYS A NZ    1 
ATOM   166  N  N     . LYS A 1 21  ? 18.148  48.730  18.317  1.00 71.54  ? 21  LYS A N     1 
ATOM   167  C  CA    . LYS A 1 21  ? 17.677  49.082  19.652  1.00 74.07  ? 21  LYS A CA    1 
ATOM   168  C  C     . LYS A 1 21  ? 18.685  50.057  20.240  1.00 85.08  ? 21  LYS A C     1 
ATOM   169  O  O     . LYS A 1 21  ? 19.800  49.660  20.594  1.00 94.23  ? 21  LYS A O     1 
ATOM   170  C  CB    . LYS A 1 21  ? 17.522  47.851  20.543  1.00 74.25  ? 21  LYS A CB    1 
ATOM   171  C  CG    . LYS A 1 21  ? 17.169  48.187  21.984  1.00 88.48  ? 21  LYS A CG    1 
ATOM   172  C  CD    . LYS A 1 21  ? 15.969  47.392  22.460  1.00 88.68  ? 21  LYS A CD    1 
ATOM   173  C  CE    . LYS A 1 21  ? 15.413  47.946  23.759  1.00 78.13  ? 21  LYS A CE    1 
ATOM   174  N  NZ    . LYS A 1 21  ? 13.939  48.132  23.681  1.00 76.32  ? 21  LYS A NZ    1 
ATOM   175  N  N     . GLU A 1 22  ? 18.304  51.328  20.332  1.00 91.96  ? 22  GLU A N     1 
ATOM   176  C  CA    . GLU A 1 22  ? 19.200  52.382  20.786  1.00 91.24  ? 22  GLU A CA    1 
ATOM   177  C  C     . GLU A 1 22  ? 18.501  53.220  21.844  1.00 93.09  ? 22  GLU A C     1 
ATOM   178  O  O     . GLU A 1 22  ? 17.375  53.682  21.630  1.00 89.83  ? 22  GLU A O     1 
ATOM   179  C  CB    . GLU A 1 22  ? 19.648  53.263  19.614  1.00 85.01  ? 22  GLU A CB    1 
ATOM   180  C  CG    . GLU A 1 22  ? 20.490  52.529  18.581  1.00 71.85  ? 22  GLU A CG    1 
ATOM   181  C  CD    . GLU A 1 22  ? 20.665  53.317  17.298  1.00 89.30  ? 22  GLU A CD    1 
ATOM   182  O  OE1   . GLU A 1 22  ? 19.722  54.034  16.904  1.00 90.96  ? 22  GLU A OE1   1 
ATOM   183  O  OE2   . GLU A 1 22  ? 21.745  53.216  16.679  1.00 94.69  ? 22  GLU A OE2   1 
ATOM   184  N  N     . ASN A 1 23  ? 19.173  53.408  22.983  1.00 94.09  ? 23  ASN A N     1 
ATOM   185  C  CA    . ASN A 1 23  ? 18.669  54.231  24.084  1.00 93.65  ? 23  ASN A CA    1 
ATOM   186  C  C     . ASN A 1 23  ? 17.300  53.742  24.557  1.00 93.46  ? 23  ASN A C     1 
ATOM   187  O  O     . ASN A 1 23  ? 16.371  54.525  24.771  1.00 97.37  ? 23  ASN A O     1 
ATOM   188  C  CB    . ASN A 1 23  ? 18.623  55.708  23.686  1.00 96.84  ? 23  ASN A CB    1 
ATOM   189  C  CG    . ASN A 1 23  ? 19.774  56.102  22.779  1.00 104.83 ? 23  ASN A CG    1 
ATOM   190  O  OD1   . ASN A 1 23  ? 20.898  55.626  22.943  1.00 102.52 ? 23  ASN A OD1   1 
ATOM   191  N  ND2   . ASN A 1 23  ? 19.496  56.968  21.812  1.00 99.53  ? 23  ASN A ND2   1 
ATOM   192  N  N     . GLY A 1 24  ? 17.181  52.425  24.717  1.00 91.89  ? 24  GLY A N     1 
ATOM   193  C  CA    . GLY A 1 24  ? 15.942  51.823  25.164  1.00 92.72  ? 24  GLY A CA    1 
ATOM   194  C  C     . GLY A 1 24  ? 14.779  51.947  24.207  1.00 99.10  ? 24  GLY A C     1 
ATOM   195  O  O     . GLY A 1 24  ? 13.642  51.670  24.599  1.00 99.84  ? 24  GLY A O     1 
ATOM   196  N  N     . GLU A 1 25  ? 15.026  52.350  22.963  1.00 97.81  ? 25  GLU A N     1 
ATOM   197  C  CA    . GLU A 1 25  ? 13.981  52.565  21.974  1.00 97.55  ? 25  GLU A CA    1 
ATOM   198  C  C     . GLU A 1 25  ? 14.211  51.658  20.774  1.00 87.14  ? 25  GLU A C     1 
ATOM   199  O  O     . GLU A 1 25  ? 15.340  51.529  20.290  1.00 83.09  ? 25  GLU A O     1 
ATOM   200  C  CB    . GLU A 1 25  ? 13.949  54.030  21.524  1.00 105.80 ? 25  GLU A CB    1 
ATOM   201  C  CG    . GLU A 1 25  ? 12.866  54.354  20.508  1.00 123.12 ? 25  GLU A CG    1 
ATOM   202  C  CD    . GLU A 1 25  ? 13.115  55.669  19.795  1.00 130.36 ? 25  GLU A CD    1 
ATOM   203  O  OE1   . GLU A 1 25  ? 12.491  55.903  18.739  1.00 120.39 ? 25  GLU A OE1   1 
ATOM   204  O  OE2   . GLU A 1 25  ? 13.937  56.469  20.291  1.00 125.79 ? 25  GLU A OE2   1 
ATOM   205  N  N     . PHE A 1 26  ? 13.138  51.032  20.298  1.00 88.95  ? 26  PHE A N     1 
ATOM   206  C  CA    . PHE A 1 26  ? 13.200  50.194  19.109  1.00 73.34  ? 26  PHE A CA    1 
ATOM   207  C  C     . PHE A 1 26  ? 13.031  51.060  17.868  1.00 76.49  ? 26  PHE A C     1 
ATOM   208  O  O     . PHE A 1 26  ? 12.049  51.799  17.747  1.00 79.98  ? 26  PHE A O     1 
ATOM   209  C  CB    . PHE A 1 26  ? 12.126  49.108  19.148  1.00 66.09  ? 26  PHE A CB    1 
ATOM   210  C  CG    . PHE A 1 26  ? 11.989  48.350  17.860  1.00 72.20  ? 26  PHE A CG    1 
ATOM   211  C  CD1   . PHE A 1 26  ? 12.940  47.416  17.488  1.00 65.87  ? 26  PHE A CD1   1 
ATOM   212  C  CD2   . PHE A 1 26  ? 10.911  48.574  17.019  1.00 66.87  ? 26  PHE A CD2   1 
ATOM   213  C  CE1   . PHE A 1 26  ? 12.820  46.717  16.302  1.00 65.94  ? 26  PHE A CE1   1 
ATOM   214  C  CE2   . PHE A 1 26  ? 10.786  47.877  15.833  1.00 66.52  ? 26  PHE A CE2   1 
ATOM   215  C  CZ    . PHE A 1 26  ? 11.741  46.948  15.474  1.00 68.03  ? 26  PHE A CZ    1 
ATOM   216  N  N     . LYS A 1 27  ? 13.989  50.965  16.950  1.00 70.04  ? 27  LYS A N     1 
ATOM   217  C  CA    . LYS A 1 27  ? 14.001  51.776  15.743  1.00 74.53  ? 27  LYS A CA    1 
ATOM   218  C  C     . LYS A 1 27  ? 14.200  50.882  14.529  1.00 72.19  ? 27  LYS A C     1 
ATOM   219  O  O     . LYS A 1 27  ? 14.913  49.877  14.589  1.00 67.35  ? 27  LYS A O     1 
ATOM   220  C  CB    . LYS A 1 27  ? 15.109  52.839  15.799  1.00 72.78  ? 27  LYS A CB    1 
ATOM   221  C  CG    . LYS A 1 27  ? 15.089  53.691  17.061  1.00 89.66  ? 27  LYS A CG    1 
ATOM   222  C  CD    . LYS A 1 27  ? 15.756  55.039  16.842  1.00 106.16 ? 27  LYS A CD    1 
ATOM   223  C  CE    . LYS A 1 27  ? 16.929  55.231  17.791  1.00 97.08  ? 27  LYS A CE    1 
ATOM   224  N  NZ    . LYS A 1 27  ? 16.679  56.308  18.788  1.00 103.03 ? 27  LYS A NZ    1 
ATOM   225  N  N     . ILE A 1 28  ? 13.561  51.257  13.424  1.00 64.19  ? 28  ILE A N     1 
ATOM   226  C  CA    . ILE A 1 28  ? 13.692  50.552  12.153  1.00 62.43  ? 28  ILE A CA    1 
ATOM   227  C  C     . ILE A 1 28  ? 14.279  51.527  11.143  1.00 68.28  ? 28  ILE A C     1 
ATOM   228  O  O     . ILE A 1 28  ? 13.617  52.494  10.744  1.00 68.50  ? 28  ILE A O     1 
ATOM   229  C  CB    . ILE A 1 28  ? 12.354  49.992  11.656  1.00 56.88  ? 28  ILE A CB    1 
ATOM   230  C  CG1   . ILE A 1 28  ? 11.760  49.035  12.687  1.00 68.57  ? 28  ILE A CG1   1 
ATOM   231  C  CG2   . ILE A 1 28  ? 12.538  49.287  10.322  1.00 58.98  ? 28  ILE A CG2   1 
ATOM   232  C  CD1   . ILE A 1 28  ? 10.500  48.346  12.219  1.00 59.71  ? 28  ILE A CD1   1 
ATOM   233  N  N     . GLU A 1 29  ? 15.515  51.274  10.728  1.00 63.95  ? 29  GLU A N     1 
ATOM   234  C  CA    . GLU A 1 29  ? 16.192  52.084  9.728   1.00 59.97  ? 29  GLU A CA    1 
ATOM   235  C  C     . GLU A 1 29  ? 16.041  51.440  8.357   1.00 60.31  ? 29  GLU A C     1 
ATOM   236  O  O     . GLU A 1 29  ? 16.168  50.220  8.216   1.00 68.62  ? 29  GLU A O     1 
ATOM   237  C  CB    . GLU A 1 29  ? 17.674  52.246  10.076  1.00 68.51  ? 29  GLU A CB    1 
ATOM   238  C  CG    . GLU A 1 29  ? 18.569  52.563  8.889   1.00 71.51  ? 29  GLU A CG    1 
ATOM   239  C  CD    . GLU A 1 29  ? 19.989  52.890  9.302   1.00 88.99  ? 29  GLU A CD    1 
ATOM   240  O  OE1   . GLU A 1 29  ? 20.244  53.001  10.520  1.00 98.60  ? 29  GLU A OE1   1 
ATOM   241  O  OE2   . GLU A 1 29  ? 20.852  53.031  8.410   1.00 99.14  ? 29  GLU A OE2   1 
ATOM   242  N  N     . TYR A 1 30  ? 15.764  52.262  7.351   1.00 63.70  ? 30  TYR A N     1 
ATOM   243  C  CA    . TYR A 1 30  ? 15.598  51.796  5.984   1.00 61.84  ? 30  TYR A CA    1 
ATOM   244  C  C     . TYR A 1 30  ? 16.749  52.289  5.117   1.00 52.64  ? 30  TYR A C     1 
ATOM   245  O  O     . TYR A 1 30  ? 17.275  53.387  5.319   1.00 61.25  ? 30  TYR A O     1 
ATOM   246  C  CB    . TYR A 1 30  ? 14.264  52.270  5.396   1.00 48.81  ? 30  TYR A CB    1 
ATOM   247  C  CG    . TYR A 1 30  ? 13.054  51.867  6.208   1.00 63.38  ? 30  TYR A CG    1 
ATOM   248  C  CD1   . TYR A 1 30  ? 12.588  52.669  7.243   1.00 63.11  ? 30  TYR A CD1   1 
ATOM   249  C  CD2   . TYR A 1 30  ? 12.374  50.685  5.939   1.00 60.32  ? 30  TYR A CD2   1 
ATOM   250  C  CE1   . TYR A 1 30  ? 11.482  52.305  7.986   1.00 57.02  ? 30  TYR A CE1   1 
ATOM   251  C  CE2   . TYR A 1 30  ? 11.267  50.314  6.677   1.00 60.65  ? 30  TYR A CE2   1 
ATOM   252  C  CZ    . TYR A 1 30  ? 10.825  51.127  7.699   1.00 62.19  ? 30  TYR A CZ    1 
ATOM   253  O  OH    . TYR A 1 30  ? 9.723   50.760  8.436   1.00 63.18  ? 30  TYR A OH    1 
ATOM   254  N  N     . ASP A 1 31  ? 17.138  51.461  4.149   1.00 50.67  ? 31  ASP A N     1 
ATOM   255  C  CA    . ASP A 1 31  ? 18.194  51.803  3.200   1.00 56.14  ? 31  ASP A CA    1 
ATOM   256  C  C     . ASP A 1 31  ? 17.727  51.381  1.814   1.00 54.05  ? 31  ASP A C     1 
ATOM   257  O  O     . ASP A 1 31  ? 17.649  50.183  1.521   1.00 49.73  ? 31  ASP A O     1 
ATOM   258  C  CB    . ASP A 1 31  ? 19.518  51.126  3.567   1.00 55.42  ? 31  ASP A CB    1 
ATOM   259  C  CG    . ASP A 1 31  ? 20.684  51.615  2.719   1.00 56.62  ? 31  ASP A CG    1 
ATOM   260  O  OD1   . ASP A 1 31  ? 20.455  52.379  1.757   1.00 55.63  ? 31  ASP A OD1   1 
ATOM   261  O  OD2   . ASP A 1 31  ? 21.838  51.238  3.018   1.00 69.61  ? 31  ASP A OD2   1 
ATOM   262  N  N     . ARG A 1 32  ? 17.419  52.361  0.965   1.00 51.50  ? 32  ARG A N     1 
ATOM   263  C  CA    . ARG A 1 32  ? 16.954  52.111  -0.392  1.00 58.43  ? 32  ARG A CA    1 
ATOM   264  C  C     . ARG A 1 32  ? 18.063  52.269  -1.425  1.00 58.32  ? 32  ARG A C     1 
ATOM   265  O  O     . ARG A 1 32  ? 17.775  52.380  -2.622  1.00 76.06  ? 32  ARG A O     1 
ATOM   266  C  CB    . ARG A 1 32  ? 15.791  53.043  -0.732  1.00 57.48  ? 32  ARG A CB    1 
ATOM   267  C  CG    . ARG A 1 32  ? 14.689  53.092  0.312   1.00 50.43  ? 32  ARG A CG    1 
ATOM   268  C  CD    . ARG A 1 32  ? 13.569  54.023  -0.127  1.00 64.20  ? 32  ARG A CD    1 
ATOM   269  N  NE    . ARG A 1 32  ? 12.249  53.489  0.188   1.00 64.41  ? 32  ARG A NE    1 
ATOM   270  C  CZ    . ARG A 1 32  ? 11.669  53.579  1.377   1.00 66.43  ? 32  ARG A CZ    1 
ATOM   271  N  NH1   . ARG A 1 32  ? 12.262  54.184  2.393   1.00 72.05  ? 32  ARG A NH1   1 
ATOM   272  N  NH2   . ARG A 1 32  ? 10.461  53.051  1.551   1.00 89.98  ? 32  ARG A NH2   1 
ATOM   273  N  N     . THR A 1 33  ? 19.324  52.283  -0.991  1.00 66.42  ? 33  THR A N     1 
ATOM   274  C  CA    . THR A 1 33  ? 20.443  52.555  -1.881  1.00 68.47  ? 33  THR A CA    1 
ATOM   275  C  C     . THR A 1 33  ? 21.300  51.334  -2.184  1.00 67.54  ? 33  THR A C     1 
ATOM   276  O  O     . THR A 1 33  ? 22.130  51.397  -3.097  1.00 70.39  ? 33  THR A O     1 
ATOM   277  C  CB    . THR A 1 33  ? 21.339  53.653  -1.287  1.00 64.10  ? 33  THR A CB    1 
ATOM   278  O  OG1   . THR A 1 33  ? 21.954  53.173  -0.085  1.00 66.54  ? 33  THR A OG1   1 
ATOM   279  C  CG2   . THR A 1 33  ? 20.521  54.895  -0.969  1.00 61.74  ? 33  THR A CG2   1 
ATOM   280  N  N     . PHE A 1 34  ? 21.126  50.235  -1.455  1.00 68.50  ? 34  PHE A N     1 
ATOM   281  C  CA    . PHE A 1 34  ? 21.955  49.054  -1.652  1.00 68.72  ? 34  PHE A CA    1 
ATOM   282  C  C     . PHE A 1 34  ? 21.547  48.328  -2.926  1.00 56.71  ? 34  PHE A C     1 
ATOM   283  O  O     . PHE A 1 34  ? 20.357  48.102  -3.169  1.00 67.15  ? 34  PHE A O     1 
ATOM   284  C  CB    . PHE A 1 34  ? 21.841  48.120  -0.449  1.00 61.39  ? 34  PHE A CB    1 
ATOM   285  C  CG    . PHE A 1 34  ? 23.008  47.190  -0.292  1.00 70.52  ? 34  PHE A CG    1 
ATOM   286  C  CD1   . PHE A 1 34  ? 22.880  45.840  -0.573  1.00 75.22  ? 34  PHE A CD1   1 
ATOM   287  C  CD2   . PHE A 1 34  ? 24.234  47.668  0.134   1.00 67.45  ? 34  PHE A CD2   1 
ATOM   288  C  CE1   . PHE A 1 34  ? 23.955  44.982  -0.427  1.00 66.39  ? 34  PHE A CE1   1 
ATOM   289  C  CE2   . PHE A 1 34  ? 25.312  46.816  0.281   1.00 76.32  ? 34  PHE A CE2   1 
ATOM   290  C  CZ    . PHE A 1 34  ? 25.173  45.472  -0.000  1.00 66.43  ? 34  PHE A CZ    1 
ATOM   291  N  N     . GLU A 1 35  ? 22.539  47.954  -3.741  1.00 58.57  ? 35  GLU A N     1 
ATOM   292  C  CA    . GLU A 1 35  ? 22.256  47.277  -4.996  1.00 64.19  ? 35  GLU A CA    1 
ATOM   293  C  C     . GLU A 1 35  ? 22.755  45.838  -4.965  1.00 65.25  ? 35  GLU A C     1 
ATOM   294  O  O     . GLU A 1 35  ? 23.875  45.579  -4.512  1.00 71.85  ? 35  GLU A O     1 
ATOM   295  C  CB    . GLU A 1 35  ? 22.908  48.002  -6.179  1.00 60.65  ? 35  GLU A CB    1 
ATOM   296  C  CG    . GLU A 1 35  ? 22.939  49.509  -6.042  1.00 71.70  ? 35  GLU A CG    1 
ATOM   297  C  CD    . GLU A 1 35  ? 23.777  50.171  -7.116  1.00 84.16  ? 35  GLU A CD    1 
ATOM   298  O  OE1   . GLU A 1 35  ? 23.362  50.144  -8.294  1.00 76.99  ? 35  GLU A OE1   1 
ATOM   299  O  OE2   . GLU A 1 35  ? 24.849  50.722  -6.784  1.00 85.02  ? 35  GLU A OE2   1 
ATOM   300  N  N     . PRO A 1 36  ? 21.952  44.888  -5.435  1.00 70.45  ? 36  PRO A N     1 
ATOM   301  C  CA    . PRO A 1 36  ? 22.408  43.498  -5.507  1.00 63.95  ? 36  PRO A CA    1 
ATOM   302  C  C     . PRO A 1 36  ? 23.361  43.282  -6.670  1.00 63.10  ? 36  PRO A C     1 
ATOM   303  O  O     . PRO A 1 36  ? 23.313  43.978  -7.687  1.00 62.24  ? 36  PRO A O     1 
ATOM   304  C  CB    . PRO A 1 36  ? 21.106  42.714  -5.708  1.00 68.94  ? 36  PRO A CB    1 
ATOM   305  C  CG    . PRO A 1 36  ? 20.215  43.674  -6.414  1.00 58.47  ? 36  PRO A CG    1 
ATOM   306  C  CD    . PRO A 1 36  ? 20.549  45.034  -5.862  1.00 56.17  ? 36  PRO A CD    1 
ATOM   307  N  N     . TYR A 1 37  ? 24.228  42.283  -6.512  1.00 65.17  ? 37  TYR A N     1 
ATOM   308  C  CA    . TYR A 1 37  ? 25.289  42.057  -7.483  1.00 58.95  ? 37  TYR A CA    1 
ATOM   309  C  C     . TYR A 1 37  ? 25.896  40.678  -7.278  1.00 54.54  ? 37  TYR A C     1 
ATOM   310  O  O     . TYR A 1 37  ? 25.740  40.057  -6.223  1.00 56.26  ? 37  TYR A O     1 
ATOM   311  C  CB    . TYR A 1 37  ? 26.384  43.122  -7.365  1.00 58.86  ? 37  TYR A CB    1 
ATOM   312  C  CG    . TYR A 1 37  ? 27.184  43.007  -6.084  1.00 60.85  ? 37  TYR A CG    1 
ATOM   313  C  CD1   . TYR A 1 37  ? 26.739  43.606  -4.912  1.00 50.97  ? 37  TYR A CD1   1 
ATOM   314  C  CD2   . TYR A 1 37  ? 28.378  42.292  -6.043  1.00 61.97  ? 37  TYR A CD2   1 
ATOM   315  C  CE1   . TYR A 1 37  ? 27.460  43.501  -3.737  1.00 59.70  ? 37  TYR A CE1   1 
ATOM   316  C  CE2   . TYR A 1 37  ? 29.105  42.181  -4.873  1.00 42.27  ? 37  TYR A CE2   1 
ATOM   317  C  CZ    . TYR A 1 37  ? 28.641  42.788  -3.723  1.00 53.52  ? 37  TYR A CZ    1 
ATOM   318  O  OH    . TYR A 1 37  ? 29.361  42.681  -2.556  1.00 69.13  ? 37  TYR A OH    1 
ATOM   319  N  N     . PHE A 1 38  ? 26.598  40.216  -8.311  1.00 61.55  ? 38  PHE A N     1 
ATOM   320  C  CA    . PHE A 1 38  ? 27.590  39.160  -8.172  1.00 59.86  ? 38  PHE A CA    1 
ATOM   321  C  C     . PHE A 1 38  ? 28.677  39.406  -9.213  1.00 64.41  ? 38  PHE A C     1 
ATOM   322  O  O     . PHE A 1 38  ? 28.600  40.348  -10.007 1.00 65.03  ? 38  PHE A O     1 
ATOM   323  C  CB    . PHE A 1 38  ? 26.954  37.761  -8.259  1.00 65.12  ? 38  PHE A CB    1 
ATOM   324  C  CG    . PHE A 1 38  ? 26.340  37.415  -9.598  1.00 61.99  ? 38  PHE A CG    1 
ATOM   325  C  CD1   . PHE A 1 38  ? 27.128  37.205  -10.721 1.00 68.50  ? 38  PHE A CD1   1 
ATOM   326  C  CD2   . PHE A 1 38  ? 24.970  37.245  -9.713  1.00 62.50  ? 38  PHE A CD2   1 
ATOM   327  C  CE1   . PHE A 1 38  ? 26.558  36.872  -11.937 1.00 69.35  ? 38  PHE A CE1   1 
ATOM   328  C  CE2   . PHE A 1 38  ? 24.396  36.906  -10.923 1.00 62.34  ? 38  PHE A CE2   1 
ATOM   329  C  CZ    . PHE A 1 38  ? 25.190  36.722  -12.037 1.00 68.12  ? 38  PHE A CZ    1 
ATOM   330  N  N     . TYR A 1 39  ? 29.702  38.560  -9.199  1.00 65.37  ? 39  TYR A N     1 
ATOM   331  C  CA    . TYR A 1 39  ? 30.867  38.748  -10.049 1.00 66.68  ? 39  TYR A CA    1 
ATOM   332  C  C     . TYR A 1 39  ? 30.889  37.732  -11.183 1.00 69.16  ? 39  TYR A C     1 
ATOM   333  O  O     . TYR A 1 39  ? 30.269  36.668  -11.115 1.00 72.01  ? 39  TYR A O     1 
ATOM   334  C  CB    . TYR A 1 39  ? 32.164  38.644  -9.240  1.00 56.29  ? 39  TYR A CB    1 
ATOM   335  C  CG    . TYR A 1 39  ? 32.254  39.631  -8.101  1.00 52.80  ? 39  TYR A CG    1 
ATOM   336  C  CD1   . TYR A 1 39  ? 32.619  40.951  -8.327  1.00 60.37  ? 39  TYR A CD1   1 
ATOM   337  C  CD2   . TYR A 1 39  ? 31.983  39.240  -6.796  1.00 59.27  ? 39  TYR A CD2   1 
ATOM   338  C  CE1   . TYR A 1 39  ? 32.705  41.857  -7.287  1.00 50.00  ? 39  TYR A CE1   1 
ATOM   339  C  CE2   . TYR A 1 39  ? 32.067  40.136  -5.750  1.00 50.99  ? 39  TYR A CE2   1 
ATOM   340  C  CZ    . TYR A 1 39  ? 32.428  41.443  -6.000  1.00 46.33  ? 39  TYR A CZ    1 
ATOM   341  O  OH    . TYR A 1 39  ? 32.510  42.334  -4.954  1.00 45.73  ? 39  TYR A OH    1 
ATOM   342  N  N     . ALA A 1 40  ? 31.623  38.085  -12.236 1.00 81.27  ? 40  ALA A N     1 
ATOM   343  C  CA    . ALA A 1 40  ? 31.850  37.211  -13.375 1.00 85.62  ? 40  ALA A CA    1 
ATOM   344  C  C     . ALA A 1 40  ? 33.258  37.445  -13.899 1.00 86.40  ? 40  ALA A C     1 
ATOM   345  O  O     . ALA A 1 40  ? 33.697  38.591  -14.030 1.00 89.83  ? 40  ALA A O     1 
ATOM   346  C  CB    . ALA A 1 40  ? 30.826  37.454  -14.491 1.00 79.98  ? 40  ALA A CB    1 
ATOM   347  N  N     . LEU A 1 41  ? 33.963  36.356  -14.193 1.00 82.02  ? 41  LEU A N     1 
ATOM   348  C  CA    . LEU A 1 41  ? 35.321  36.410  -14.722 1.00 82.38  ? 41  LEU A CA    1 
ATOM   349  C  C     . LEU A 1 41  ? 35.268  35.919  -16.165 1.00 87.21  ? 41  LEU A C     1 
ATOM   350  O  O     . LEU A 1 41  ? 35.056  34.727  -16.412 1.00 88.95  ? 41  LEU A O     1 
ATOM   351  C  CB    . LEU A 1 41  ? 36.267  35.564  -13.873 1.00 81.19  ? 41  LEU A CB    1 
ATOM   352  C  CG    . LEU A 1 41  ? 37.755  35.921  -13.893 1.00 97.58  ? 41  LEU A CG    1 
ATOM   353  C  CD1   . LEU A 1 41  ? 38.336  35.816  -12.493 1.00 85.45  ? 41  LEU A CD1   1 
ATOM   354  C  CD2   . LEU A 1 41  ? 38.521  35.033  -14.857 1.00 91.37  ? 41  LEU A CD2   1 
ATOM   355  N  N     . LEU A 1 42  ? 35.442  36.836  -17.115 1.00 85.70  ? 42  LEU A N     1 
ATOM   356  C  CA    . LEU A 1 42  ? 35.293  36.506  -18.524 1.00 89.87  ? 42  LEU A CA    1 
ATOM   357  C  C     . LEU A 1 42  ? 36.624  36.105  -19.154 1.00 103.20 ? 42  LEU A C     1 
ATOM   358  O  O     . LEU A 1 42  ? 37.697  36.223  -18.556 1.00 111.04 ? 42  LEU A O     1 
ATOM   359  C  CB    . LEU A 1 42  ? 34.686  37.679  -19.299 1.00 98.17  ? 42  LEU A CB    1 
ATOM   360  C  CG    . LEU A 1 42  ? 33.271  38.135  -18.950 1.00 93.93  ? 42  LEU A CG    1 
ATOM   361  C  CD1   . LEU A 1 42  ? 33.101  39.604  -19.270 1.00 98.37  ? 42  LEU A CD1   1 
ATOM   362  C  CD2   . LEU A 1 42  ? 32.271  37.321  -19.728 1.00 91.99  ? 42  LEU A CD2   1 
ATOM   363  N  N     . LYS A 1 43  ? 36.534  35.614  -20.394 1.00 109.77 ? 43  LYS A N     1 
ATOM   364  C  CA    . LYS A 1 43  ? 37.730  35.235  -21.137 1.00 117.13 ? 43  LYS A CA    1 
ATOM   365  C  C     . LYS A 1 43  ? 38.489  36.468  -21.612 1.00 123.32 ? 43  LYS A C     1 
ATOM   366  O  O     . LYS A 1 43  ? 39.693  36.599  -21.361 1.00 126.76 ? 43  LYS A O     1 
ATOM   367  C  CB    . LYS A 1 43  ? 37.352  34.339  -22.317 1.00 117.71 ? 43  LYS A CB    1 
ATOM   368  C  CG    . LYS A 1 43  ? 36.899  32.946  -21.914 1.00 117.61 ? 43  LYS A CG    1 
ATOM   369  C  CD    . LYS A 1 43  ? 37.879  31.882  -22.380 1.00 130.36 ? 43  LYS A CD    1 
ATOM   370  C  CE    . LYS A 1 43  ? 37.307  30.485  -22.192 1.00 126.63 ? 43  LYS A CE    1 
ATOM   371  N  NZ    . LYS A 1 43  ? 38.179  29.439  -22.795 1.00 110.94 ? 43  LYS A NZ    1 
ATOM   372  N  N     . ASP A 1 44  ? 37.804  37.376  -22.313 1.00 119.68 ? 44  ASP A N     1 
ATOM   373  C  CA    . ASP A 1 44  ? 38.349  38.681  -22.654 1.00 121.97 ? 44  ASP A CA    1 
ATOM   374  C  C     . ASP A 1 44  ? 37.625  39.761  -21.859 1.00 122.06 ? 44  ASP A C     1 
ATOM   375  O  O     . ASP A 1 44  ? 36.495  39.570  -21.397 1.00 116.94 ? 44  ASP A O     1 
ATOM   376  C  CB    . ASP A 1 44  ? 38.339  38.934  -24.196 1.00 124.61 ? 44  ASP A CB    1 
ATOM   377  C  CG    . ASP A 1 44  ? 36.970  39.325  -24.798 1.00 128.73 ? 44  ASP A CG    1 
ATOM   378  O  OD1   . ASP A 1 44  ? 36.971  39.466  -26.051 1.00 134.41 ? 44  ASP A OD1   1 
ATOM   379  O  OD2   . ASP A 1 44  ? 35.940  39.452  -24.094 1.00 135.25 ? 44  ASP A OD2   1 
ATOM   380  N  N     . ASP A 1 45  ? 38.318  40.877  -21.644 1.00 131.80 ? 45  ASP A N     1 
ATOM   381  C  CA    . ASP A 1 45  ? 37.722  41.986  -20.915 1.00 123.88 ? 45  ASP A CA    1 
ATOM   382  C  C     . ASP A 1 45  ? 36.976  42.903  -21.875 1.00 121.18 ? 45  ASP A C     1 
ATOM   383  O  O     . ASP A 1 45  ? 36.874  44.110  -21.639 1.00 117.79 ? 45  ASP A O     1 
ATOM   384  C  CB    . ASP A 1 45  ? 38.789  42.753  -20.129 1.00 128.65 ? 45  ASP A CB    1 
ATOM   385  C  CG    . ASP A 1 45  ? 39.885  43.302  -21.011 1.00 150.02 ? 45  ASP A CG    1 
ATOM   386  O  OD1   . ASP A 1 45  ? 40.638  44.181  -20.543 1.00 134.91 ? 45  ASP A OD1   1 
ATOM   387  O  OD2   . ASP A 1 45  ? 39.999  42.848  -22.168 1.00 154.15 ? 45  ASP A OD2   1 
ATOM   388  N  N     . SER A 1 46  ? 36.437  42.332  -22.952 1.00 119.42 ? 46  SER A N     1 
ATOM   389  C  CA    . SER A 1 46  ? 35.694  43.095  -23.946 1.00 121.41 ? 46  SER A CA    1 
ATOM   390  C  C     . SER A 1 46  ? 34.337  42.508  -24.295 1.00 113.84 ? 46  SER A C     1 
ATOM   391  O  O     . SER A 1 46  ? 33.485  43.248  -24.804 1.00 124.68 ? 46  SER A O     1 
ATOM   392  C  CB    . SER A 1 46  ? 36.511  43.234  -25.240 1.00 123.18 ? 46  SER A CB    1 
ATOM   393  O  OG    . SER A 1 46  ? 37.888  43.416  -24.963 1.00 125.88 ? 46  SER A OG    1 
ATOM   394  N  N     . ALA A 1 47  ? 34.102  41.219  -24.048 1.00 105.99 ? 47  ALA A N     1 
ATOM   395  C  CA    . ALA A 1 47  ? 32.823  40.609  -24.386 1.00 115.68 ? 47  ALA A CA    1 
ATOM   396  C  C     . ALA A 1 47  ? 31.687  41.096  -23.511 1.00 112.92 ? 47  ALA A C     1 
ATOM   397  O  O     . ALA A 1 47  ? 30.554  40.643  -23.713 1.00 103.92 ? 47  ALA A O     1 
ATOM   398  C  CB    . ALA A 1 47  ? 32.912  39.083  -24.292 1.00 110.16 ? 47  ALA A CB    1 
ATOM   399  N  N     . ILE A 1 48  ? 31.936  41.991  -22.550 1.00 104.13 ? 48  ILE A N     1 
ATOM   400  C  CA    . ILE A 1 48  ? 30.858  42.358  -21.639 1.00 101.92 ? 48  ILE A CA    1 
ATOM   401  C  C     . ILE A 1 48  ? 29.678  43.024  -22.306 1.00 107.65 ? 48  ILE A C     1 
ATOM   402  O  O     . ILE A 1 48  ? 28.583  43.018  -21.739 1.00 113.91 ? 48  ILE A O     1 
ATOM   403  C  CB    . ILE A 1 48  ? 31.299  43.245  -20.464 1.00 99.76  ? 48  ILE A CB    1 
ATOM   404  C  CG1   . ILE A 1 48  ? 30.366  42.903  -19.306 1.00 103.80 ? 48  ILE A CG1   1 
ATOM   405  C  CG2   . ILE A 1 48  ? 31.230  44.745  -20.794 1.00 107.82 ? 48  ILE A CG2   1 
ATOM   406  C  CD1   . ILE A 1 48  ? 30.686  43.541  -18.030 1.00 96.28  ? 48  ILE A CD1   1 
ATOM   407  N  N     . GLU A 1 49  ? 29.863  43.635  -23.471 1.00 105.68 ? 49  GLU A N     1 
ATOM   408  C  CA    . GLU A 1 49  ? 28.707  44.155  -24.186 1.00 115.76 ? 49  GLU A CA    1 
ATOM   409  C  C     . GLU A 1 49  ? 27.684  43.047  -24.414 1.00 117.37 ? 49  GLU A C     1 
ATOM   410  O  O     . GLU A 1 49  ? 26.495  43.209  -24.117 1.00 121.73 ? 49  GLU A O     1 
ATOM   411  C  CB    . GLU A 1 49  ? 29.155  44.784  -25.501 1.00 117.18 ? 49  GLU A CB    1 
ATOM   412  C  CG    . GLU A 1 49  ? 30.048  46.008  -25.313 1.00 114.71 ? 49  GLU A CG    1 
ATOM   413  C  CD    . GLU A 1 49  ? 29.459  47.005  -24.329 1.00 118.93 ? 49  GLU A CD    1 
ATOM   414  O  OE1   . GLU A 1 49  ? 28.257  47.329  -24.444 1.00 104.41 ? 49  GLU A OE1   1 
ATOM   415  O  OE2   . GLU A 1 49  ? 30.199  47.455  -23.431 1.00 131.01 ? 49  GLU A OE2   1 
ATOM   416  N  N     . GLU A 1 50  ? 28.142  41.898  -24.913 1.00 117.11 ? 50  GLU A N     1 
ATOM   417  C  CA    . GLU A 1 50  ? 27.281  40.726  -25.004 1.00 122.86 ? 50  GLU A CA    1 
ATOM   418  C  C     . GLU A 1 50  ? 26.783  40.297  -23.626 1.00 119.47 ? 50  GLU A C     1 
ATOM   419  O  O     . GLU A 1 50  ? 25.629  39.871  -23.480 1.00 116.75 ? 50  GLU A O     1 
ATOM   420  C  CB    . GLU A 1 50  ? 28.040  39.585  -25.679 1.00 120.87 ? 50  GLU A CB    1 
ATOM   421  C  CG    . GLU A 1 50  ? 27.207  38.740  -26.616 1.00 125.09 ? 50  GLU A CG    1 
ATOM   422  C  CD    . GLU A 1 50  ? 28.065  37.931  -27.567 1.00 131.23 ? 50  GLU A CD    1 
ATOM   423  O  OE1   . GLU A 1 50  ? 29.266  38.249  -27.703 1.00 129.86 ? 50  GLU A OE1   1 
ATOM   424  O  OE2   . GLU A 1 50  ? 27.538  36.979  -28.179 1.00 138.61 ? 50  GLU A OE2   1 
ATOM   425  N  N     . VAL A 1 51  ? 27.634  40.412  -22.597 1.00 119.29 ? 51  VAL A N     1 
ATOM   426  C  CA    . VAL A 1 51  ? 27.237  39.976  -21.260 1.00 106.38 ? 51  VAL A CA    1 
ATOM   427  C  C     . VAL A 1 51  ? 26.262  40.962  -20.625 1.00 103.26 ? 51  VAL A C     1 
ATOM   428  O  O     . VAL A 1 51  ? 25.449  40.586  -19.775 1.00 106.88 ? 51  VAL A O     1 
ATOM   429  C  CB    . VAL A 1 51  ? 28.466  39.735  -20.367 1.00 95.53  ? 51  VAL A CB    1 
ATOM   430  C  CG1   . VAL A 1 51  ? 28.087  38.838  -19.198 1.00 91.92  ? 51  VAL A CG1   1 
ATOM   431  C  CG2   . VAL A 1 51  ? 29.560  39.075  -21.182 1.00 108.92 ? 51  VAL A CG2   1 
ATOM   432  N  N     . LYS A 1 52  ? 26.322  42.232  -21.013 1.00 99.92  ? 52  LYS A N     1 
ATOM   433  C  CA    . LYS A 1 52  ? 25.287  43.173  -20.604 1.00 103.95 ? 52  LYS A CA    1 
ATOM   434  C  C     . LYS A 1 52  ? 23.921  42.700  -21.099 1.00 115.02 ? 52  LYS A C     1 
ATOM   435  O  O     . LYS A 1 52  ? 22.914  42.840  -20.397 1.00 108.46 ? 52  LYS A O     1 
ATOM   436  C  CB    . LYS A 1 52  ? 25.630  44.569  -21.146 1.00 104.83 ? 52  LYS A CB    1 
ATOM   437  C  CG    . LYS A 1 52  ? 24.663  45.737  -20.884 1.00 123.47 ? 52  LYS A CG    1 
ATOM   438  C  CD    . LYS A 1 52  ? 23.771  45.607  -19.669 1.00 111.52 ? 52  LYS A CD    1 
ATOM   439  C  CE    . LYS A 1 52  ? 23.008  46.896  -19.462 1.00 106.47 ? 52  LYS A CE    1 
ATOM   440  N  NZ    . LYS A 1 52  ? 22.478  47.454  -20.750 1.00 119.22 ? 52  LYS A NZ    1 
ATOM   441  N  N     . LYS A 1 53  ? 23.874  42.075  -22.278 1.00 110.15 ? 53  LYS A N     1 
ATOM   442  C  CA    . LYS A 1 53  ? 22.598  41.860  -22.945 1.00 104.55 ? 53  LYS A CA    1 
ATOM   443  C  C     . LYS A 1 53  ? 21.868  40.579  -22.551 1.00 109.96 ? 53  LYS A C     1 
ATOM   444  O  O     . LYS A 1 53  ? 20.719  40.416  -22.977 1.00 112.45 ? 53  LYS A O     1 
ATOM   445  C  CB    . LYS A 1 53  ? 22.760  41.864  -24.470 1.00 103.37 ? 53  LYS A CB    1 
ATOM   446  C  CG    . LYS A 1 53  ? 23.637  42.958  -25.064 1.00 110.44 ? 53  LYS A CG    1 
ATOM   447  C  CD    . LYS A 1 53  ? 23.162  44.360  -24.694 1.00 111.90 ? 53  LYS A CD    1 
ATOM   448  C  CE    . LYS A 1 53  ? 24.163  45.416  -25.154 1.00 111.95 ? 53  LYS A CE    1 
ATOM   449  N  NZ    . LYS A 1 53  ? 24.759  46.191  -24.034 1.00 113.01 ? 53  LYS A NZ    1 
ATOM   450  N  N     . ILE A 1 54  ? 22.460  39.657  -21.781 1.00 105.71 ? 54  ILE A N     1 
ATOM   451  C  CA    . ILE A 1 54  ? 21.676  38.478  -21.428 1.00 104.40 ? 54  ILE A CA    1 
ATOM   452  C  C     . ILE A 1 54  ? 20.512  38.890  -20.539 1.00 97.74  ? 54  ILE A C     1 
ATOM   453  O  O     . ILE A 1 54  ? 20.647  39.722  -19.631 1.00 100.81 ? 54  ILE A O     1 
ATOM   454  C  CB    . ILE A 1 54  ? 22.476  37.342  -20.757 1.00 83.83  ? 54  ILE A CB    1 
ATOM   455  C  CG1   . ILE A 1 54  ? 23.830  37.060  -21.394 1.00 101.65 ? 54  ILE A CG1   1 
ATOM   456  C  CG2   . ILE A 1 54  ? 21.682  36.073  -20.721 1.00 92.72  ? 54  ILE A CG2   1 
ATOM   457  C  CD1   . ILE A 1 54  ? 24.884  37.721  -20.669 1.00 102.38 ? 54  ILE A CD1   1 
ATOM   458  N  N     . THR A 1 55  ? 19.349  38.317  -20.826 1.00 92.77  ? 55  THR A N     1 
ATOM   459  C  CA    . THR A 1 55  ? 18.131  38.510  -20.073 1.00 94.73  ? 55  THR A CA    1 
ATOM   460  C  C     . THR A 1 55  ? 17.638  37.151  -19.591 1.00 93.58  ? 55  THR A C     1 
ATOM   461  O  O     . THR A 1 55  ? 18.213  36.105  -19.909 1.00 99.48  ? 55  THR A O     1 
ATOM   462  C  CB    . THR A 1 55  ? 17.067  39.209  -20.926 1.00 99.31  ? 55  THR A CB    1 
ATOM   463  O  OG1   . THR A 1 55  ? 16.316  38.229  -21.651 1.00 98.42  ? 55  THR A OG1   1 
ATOM   464  C  CG2   . THR A 1 55  ? 17.710  40.171  -21.914 1.00 106.31 ? 55  THR A CG2   1 
ATOM   465  N  N     . ALA A 1 56  ? 16.559  37.176  -18.816 1.00 98.88  ? 56  ALA A N     1 
ATOM   466  C  CA    . ALA A 1 56  ? 15.895  35.961  -18.363 1.00 96.71  ? 56  ALA A CA    1 
ATOM   467  C  C     . ALA A 1 56  ? 14.506  36.342  -17.874 1.00 100.72 ? 56  ALA A C     1 
ATOM   468  O  O     . ALA A 1 56  ? 14.180  37.522  -17.732 1.00 102.34 ? 56  ALA A O     1 
ATOM   469  C  CB    . ALA A 1 56  ? 16.695  35.254  -17.266 1.00 83.70  ? 56  ALA A CB    1 
ATOM   470  N  N     . GLU A 1 57  ? 13.687  35.328  -17.617 1.00 101.28 ? 57  GLU A N     1 
ATOM   471  C  CA    . GLU A 1 57  ? 12.334  35.531  -17.119 1.00 105.35 ? 57  GLU A CA    1 
ATOM   472  C  C     . GLU A 1 57  ? 12.268  35.155  -15.644 1.00 106.29 ? 57  GLU A C     1 
ATOM   473  O  O     . GLU A 1 57  ? 12.931  34.211  -15.202 1.00 109.68 ? 57  GLU A O     1 
ATOM   474  C  CB    . GLU A 1 57  ? 11.317  34.722  -17.938 1.00 112.75 ? 57  GLU A CB    1 
ATOM   475  C  CG    . GLU A 1 57  ? 11.083  33.290  -17.470 1.00 115.82 ? 57  GLU A CG    1 
ATOM   476  C  CD    . GLU A 1 57  ? 9.929   33.172  -16.494 1.00 120.57 ? 57  GLU A CD    1 
ATOM   477  O  OE1   . GLU A 1 57  ? 9.775   32.095  -15.880 1.00 116.45 ? 57  GLU A OE1   1 
ATOM   478  O  OE2   . GLU A 1 57  ? 9.178   34.158  -16.342 1.00 130.52 ? 57  GLU A OE2   1 
ATOM   479  N  N     . ARG A 1 58  ? 11.486  35.918  -14.881 1.00 105.88 ? 58  ARG A N     1 
ATOM   480  C  CA    . ARG A 1 58  ? 11.264  35.607  -13.474 1.00 111.47 ? 58  ARG A CA    1 
ATOM   481  C  C     . ARG A 1 58  ? 9.789   35.329  -13.220 1.00 116.47 ? 58  ARG A C     1 
ATOM   482  O  O     . ARG A 1 58  ? 9.376   34.167  -13.140 1.00 115.56 ? 58  ARG A O     1 
ATOM   483  C  CB    . ARG A 1 58  ? 11.747  36.747  -12.574 1.00 102.22 ? 58  ARG A CB    1 
ATOM   484  C  CG    . ARG A 1 58  ? 12.200  36.291  -11.196 1.00 84.37  ? 58  ARG A CG    1 
ATOM   485  C  CD    . ARG A 1 58  ? 12.916  37.400  -10.445 1.00 90.97  ? 58  ARG A CD    1 
ATOM   486  N  NE    . ARG A 1 58  ? 12.090  37.957  -9.381  1.00 88.88  ? 58  ARG A NE    1 
ATOM   487  C  CZ    . ARG A 1 58  ? 11.969  39.253  -9.128  1.00 84.51  ? 58  ARG A CZ    1 
ATOM   488  N  NH1   . ARG A 1 58  ? 12.620  40.160  -9.839  1.00 80.13  ? 58  ARG A NH1   1 
ATOM   489  N  NH2   . ARG A 1 58  ? 11.181  39.650  -8.133  1.00 81.60  ? 58  ARG A NH2   1 
ATOM   490  N  N     . HIS A 1 59  ? 8.988   36.391  -13.101 1.00 102.11 ? 59  HIS A N     1 
ATOM   491  C  CA    . HIS A 1 59  ? 7.559   36.283  -12.813 1.00 113.91 ? 59  HIS A CA    1 
ATOM   492  C  C     . HIS A 1 59  ? 6.797   37.138  -13.828 1.00 118.39 ? 59  HIS A C     1 
ATOM   493  O  O     . HIS A 1 59  ? 6.280   38.208  -13.501 1.00 113.38 ? 59  HIS A O     1 
ATOM   494  C  CB    . HIS A 1 59  ? 7.259   36.710  -11.379 1.00 115.56 ? 59  HIS A CB    1 
ATOM   495  C  CG    . HIS A 1 59  ? 7.258   35.575  -10.405 1.00 127.59 ? 59  HIS A CG    1 
ATOM   496  N  ND1   . HIS A 1 59  ? 6.881   34.297  -10.755 1.00 130.36 ? 59  HIS A ND1   1 
ATOM   497  C  CD2   . HIS A 1 59  ? 7.599   35.523  -9.096  1.00 130.53 ? 59  HIS A CD2   1 
ATOM   498  C  CE1   . HIS A 1 59  ? 6.984   33.506  -9.702  1.00 134.19 ? 59  HIS A CE1   1 
ATOM   499  N  NE2   . HIS A 1 59  ? 7.418   34.225  -8.683  1.00 147.68 ? 59  HIS A NE2   1 
ATOM   500  N  N     . GLY A 1 60  ? 6.727   36.651  -15.065 1.00 112.10 ? 60  GLY A N     1 
ATOM   501  C  CA    . GLY A 1 60  ? 6.163   37.446  -16.143 1.00 119.24 ? 60  GLY A CA    1 
ATOM   502  C  C     . GLY A 1 60  ? 6.906   38.739  -16.383 1.00 117.55 ? 60  GLY A C     1 
ATOM   503  O  O     . GLY A 1 60  ? 6.306   39.722  -16.834 1.00 127.00 ? 60  GLY A O     1 
ATOM   504  N  N     . THR A 1 61  ? 8.202   38.766  -16.084 1.00 118.54 ? 61  THR A N     1 
ATOM   505  C  CA    . THR A 1 61  ? 9.007   39.975  -16.167 1.00 115.92 ? 61  THR A CA    1 
ATOM   506  C  C     . THR A 1 61  ? 10.411  39.582  -16.596 1.00 114.08 ? 61  THR A C     1 
ATOM   507  O  O     . THR A 1 61  ? 10.990  38.646  -16.036 1.00 104.28 ? 61  THR A O     1 
ATOM   508  C  CB    . THR A 1 61  ? 9.054   40.705  -14.820 1.00 115.00 ? 61  THR A CB    1 
ATOM   509  O  OG1   . THR A 1 61  ? 9.088   39.744  -13.757 1.00 112.62 ? 61  THR A OG1   1 
ATOM   510  C  CG2   . THR A 1 61  ? 7.836   41.604  -14.647 1.00 97.89  ? 61  THR A CG2   1 
ATOM   511  N  N     . VAL A 1 62  ? 10.952  40.289  -17.581 1.00 103.27 ? 62  VAL A N     1 
ATOM   512  C  CA    . VAL A 1 62  ? 12.306  40.015  -18.044 1.00 94.02  ? 62  VAL A CA    1 
ATOM   513  C  C     . VAL A 1 62  ? 13.297  40.574  -17.029 1.00 96.79  ? 62  VAL A C     1 
ATOM   514  O  O     . VAL A 1 62  ? 13.167  41.717  -16.572 1.00 99.78  ? 62  VAL A O     1 
ATOM   515  C  CB    . VAL A 1 62  ? 12.525  40.581  -19.460 1.00 94.85  ? 62  VAL A CB    1 
ATOM   516  C  CG1   . VAL A 1 62  ? 12.672  42.102  -19.463 1.00 96.13  ? 62  VAL A CG1   1 
ATOM   517  C  CG2   . VAL A 1 62  ? 13.724  39.922  -20.118 1.00 103.03 ? 62  VAL A CG2   1 
ATOM   518  N  N     . VAL A 1 63  ? 14.255  39.745  -16.621 1.00 97.66  ? 63  VAL A N     1 
ATOM   519  C  CA    . VAL A 1 63  ? 15.319  40.170  -15.719 1.00 87.84  ? 63  VAL A CA    1 
ATOM   520  C  C     . VAL A 1 63  ? 16.524  40.536  -16.569 1.00 90.65  ? 63  VAL A C     1 
ATOM   521  O  O     . VAL A 1 63  ? 16.819  39.875  -17.574 1.00 96.93  ? 63  VAL A O     1 
ATOM   522  C  CB    . VAL A 1 63  ? 15.651  39.085  -14.670 1.00 84.27  ? 63  VAL A CB    1 
ATOM   523  C  CG1   . VAL A 1 63  ? 14.413  38.268  -14.353 1.00 87.88  ? 63  VAL A CG1   1 
ATOM   524  C  CG2   . VAL A 1 63  ? 16.789  38.181  -15.119 1.00 95.79  ? 63  VAL A CG2   1 
ATOM   525  N  N     . THR A 1 64  ? 17.175  41.640  -16.217 1.00 92.08  ? 64  THR A N     1 
ATOM   526  C  CA    . THR A 1 64  ? 18.279  42.167  -17.004 1.00 96.92  ? 64  THR A CA    1 
ATOM   527  C  C     . THR A 1 64  ? 19.394  42.614  -16.073 1.00 90.59  ? 64  THR A C     1 
ATOM   528  O  O     . THR A 1 64  ? 19.147  43.058  -14.948 1.00 99.19  ? 64  THR A O     1 
ATOM   529  C  CB    . THR A 1 64  ? 17.859  43.360  -17.888 1.00 86.52  ? 64  THR A CB    1 
ATOM   530  O  OG1   . THR A 1 64  ? 17.776  44.547  -17.090 1.00 76.95  ? 64  THR A OG1   1 
ATOM   531  C  CG2   . THR A 1 64  ? 16.516  43.110  -18.565 1.00 84.88  ? 64  THR A CG2   1 
ATOM   532  N  N     . VAL A 1 65  ? 20.628  42.486  -16.555 1.00 79.09  ? 65  VAL A N     1 
ATOM   533  C  CA    . VAL A 1 65  ? 21.753  43.107  -15.871 1.00 78.53  ? 65  VAL A CA    1 
ATOM   534  C  C     . VAL A 1 65  ? 21.577  44.615  -15.940 1.00 84.43  ? 65  VAL A C     1 
ATOM   535  O  O     . VAL A 1 65  ? 21.546  45.202  -17.029 1.00 88.23  ? 65  VAL A O     1 
ATOM   536  C  CB    . VAL A 1 65  ? 23.078  42.665  -16.498 1.00 89.86  ? 65  VAL A CB    1 
ATOM   537  C  CG1   . VAL A 1 65  ? 24.240  43.414  -15.862 1.00 76.30  ? 65  VAL A CG1   1 
ATOM   538  C  CG2   . VAL A 1 65  ? 23.256  41.162  -16.354 1.00 80.09  ? 65  VAL A CG2   1 
ATOM   539  N  N     . LYS A 1 66  ? 21.442  45.251  -14.777 1.00 67.75  ? 66  LYS A N     1 
ATOM   540  C  CA    . LYS A 1 66  ? 21.269  46.697  -14.740 1.00 62.41  ? 66  LYS A CA    1 
ATOM   541  C  C     . LYS A 1 66  ? 22.527  47.389  -15.251 1.00 78.17  ? 66  LYS A C     1 
ATOM   542  O  O     . LYS A 1 66  ? 22.532  47.935  -16.359 1.00 85.54  ? 66  LYS A O     1 
ATOM   543  C  CB    . LYS A 1 66  ? 20.925  47.169  -13.326 1.00 66.54  ? 66  LYS A CB    1 
ATOM   544  C  CG    . LYS A 1 66  ? 20.899  48.682  -13.174 1.00 72.38  ? 66  LYS A CG    1 
ATOM   545  C  CD    . LYS A 1 66  ? 20.200  49.111  -11.893 1.00 62.34  ? 66  LYS A CD    1 
ATOM   546  C  CE    . LYS A 1 66  ? 20.957  48.638  -10.665 1.00 76.34  ? 66  LYS A CE    1 
ATOM   547  N  NZ    . LYS A 1 66  ? 20.830  49.594  -9.531  1.00 77.49  ? 66  LYS A NZ    1 
ATOM   548  N  N     . ARG A 1 67  ? 23.600  47.358  -14.462 1.00 76.90  ? 67  ARG A N     1 
ATOM   549  C  CA    . ARG A 1 67  ? 24.858  47.990  -14.831 1.00 77.01  ? 67  ARG A CA    1 
ATOM   550  C  C     . ARG A 1 67  ? 26.020  47.049  -14.536 1.00 77.83  ? 67  ARG A C     1 
ATOM   551  O  O     . ARG A 1 67  ? 25.883  46.062  -13.808 1.00 79.30  ? 67  ARG A O     1 
ATOM   552  C  CB    . ARG A 1 67  ? 25.058  49.323  -14.092 1.00 68.07  ? 67  ARG A CB    1 
ATOM   553  C  CG    . ARG A 1 67  ? 24.803  49.246  -12.597 1.00 72.12  ? 67  ARG A CG    1 
ATOM   554  C  CD    . ARG A 1 67  ? 24.905  50.605  -11.931 1.00 73.49  ? 67  ARG A CD    1 
ATOM   555  N  NE    . ARG A 1 67  ? 26.269  50.888  -11.502 1.00 76.99  ? 67  ARG A NE    1 
ATOM   556  C  CZ    . ARG A 1 67  ? 26.630  51.108  -10.245 1.00 80.20  ? 67  ARG A CZ    1 
ATOM   557  N  NH1   . ARG A 1 67  ? 25.750  51.084  -9.259  1.00 73.85  ? 67  ARG A NH1   1 
ATOM   558  N  NH2   . ARG A 1 67  ? 27.907  51.360  -9.972  1.00 83.22  ? 67  ARG A NH2   1 
ATOM   559  N  N     . VAL A 1 68  ? 27.175  47.373  -15.123 1.00 87.08  ? 68  VAL A N     1 
ATOM   560  C  CA    . VAL A 1 68  ? 28.398  46.595  -14.981 1.00 77.57  ? 68  VAL A CA    1 
ATOM   561  C  C     . VAL A 1 68  ? 29.530  47.552  -14.625 1.00 81.02  ? 68  VAL A C     1 
ATOM   562  O  O     . VAL A 1 68  ? 29.441  48.761  -14.849 1.00 89.34  ? 68  VAL A O     1 
ATOM   563  C  CB    . VAL A 1 68  ? 28.735  45.804  -16.265 1.00 75.81  ? 68  VAL A CB    1 
ATOM   564  C  CG1   . VAL A 1 68  ? 27.668  44.760  -16.545 1.00 72.82  ? 68  VAL A CG1   1 
ATOM   565  C  CG2   . VAL A 1 68  ? 28.884  46.743  -17.455 1.00 92.16  ? 68  VAL A CG2   1 
ATOM   566  N  N     . GLU A 1 69  ? 30.607  47.001  -14.066 1.00 84.89  ? 69  GLU A N     1 
ATOM   567  C  CA    . GLU A 1 69  ? 31.714  47.838  -13.614 1.00 82.32  ? 69  GLU A CA    1 
ATOM   568  C  C     . GLU A 1 69  ? 32.980  47.005  -13.478 1.00 84.18  ? 69  GLU A C     1 
ATOM   569  O  O     . GLU A 1 69  ? 32.944  45.901  -12.928 1.00 79.96  ? 69  GLU A O     1 
ATOM   570  C  CB    . GLU A 1 69  ? 31.382  48.515  -12.281 1.00 67.69  ? 69  GLU A CB    1 
ATOM   571  C  CG    . GLU A 1 69  ? 32.583  49.145  -11.607 1.00 83.07  ? 69  GLU A CG    1 
ATOM   572  C  CD    . GLU A 1 69  ? 32.296  49.574  -10.188 1.00 84.62  ? 69  GLU A CD    1 
ATOM   573  O  OE1   . GLU A 1 69  ? 31.662  48.793  -9.447  1.00 77.16  ? 69  GLU A OE1   1 
ATOM   574  O  OE2   . GLU A 1 69  ? 32.705  50.693  -9.814  1.00 94.57  ? 69  GLU A OE2   1 
ATOM   575  N  N     . LYS A 1 70  ? 34.090  47.537  -13.990 1.00 92.02  ? 70  LYS A N     1 
ATOM   576  C  CA    . LYS A 1 70  ? 35.388  46.881  -13.869 1.00 79.34  ? 70  LYS A CA    1 
ATOM   577  C  C     . LYS A 1 70  ? 35.876  46.933  -12.427 1.00 72.56  ? 70  LYS A C     1 
ATOM   578  O  O     . LYS A 1 70  ? 35.969  48.011  -11.831 1.00 80.53  ? 70  LYS A O     1 
ATOM   579  C  CB    . LYS A 1 70  ? 36.395  47.553  -14.800 1.00 96.77  ? 70  LYS A CB    1 
ATOM   580  C  CG    . LYS A 1 70  ? 37.329  46.610  -15.527 1.00 97.86  ? 70  LYS A CG    1 
ATOM   581  C  CD    . LYS A 1 70  ? 36.559  45.491  -16.161 1.00 96.68  ? 70  LYS A CD    1 
ATOM   582  C  CE    . LYS A 1 70  ? 37.465  44.457  -16.810 1.00 111.07 ? 70  LYS A CE    1 
ATOM   583  N  NZ    . LYS A 1 70  ? 38.304  45.059  -17.892 1.00 109.31 ? 70  LYS A NZ    1 
ATOM   584  N  N     . VAL A 1 71  ? 36.190  45.769  -11.867 1.00 72.31  ? 71  VAL A N     1 
ATOM   585  C  CA    . VAL A 1 71  ? 36.730  45.671  -10.519 1.00 72.01  ? 71  VAL A CA    1 
ATOM   586  C  C     . VAL A 1 71  ? 38.010  44.851  -10.568 1.00 77.74  ? 71  VAL A C     1 
ATOM   587  O  O     . VAL A 1 71  ? 38.113  43.881  -11.326 1.00 80.34  ? 71  VAL A O     1 
ATOM   588  C  CB    . VAL A 1 71  ? 35.719  45.044  -9.535  1.00 62.79  ? 71  VAL A CB    1 
ATOM   589  C  CG1   . VAL A 1 71  ? 36.219  45.165  -8.104  1.00 80.20  ? 71  VAL A CG1   1 
ATOM   590  C  CG2   . VAL A 1 71  ? 34.360  45.705  -9.672  1.00 82.55  ? 71  VAL A CG2   1 
ATOM   591  N  N     . GLN A 1 72  ? 38.990  45.253  -9.768  1.00 73.15  ? 72  GLN A N     1 
ATOM   592  C  CA    . GLN A 1 72  ? 40.192  44.465  -9.540  1.00 78.02  ? 72  GLN A CA    1 
ATOM   593  C  C     . GLN A 1 72  ? 40.131  43.919  -8.120  1.00 71.40  ? 72  GLN A C     1 
ATOM   594  O  O     . GLN A 1 72  ? 40.140  44.690  -7.154  1.00 74.18  ? 72  GLN A O     1 
ATOM   595  C  CB    . GLN A 1 72  ? 41.453  45.301  -9.753  1.00 80.16  ? 72  GLN A CB    1 
ATOM   596  C  CG    . GLN A 1 72  ? 42.746  44.521  -9.558  1.00 94.07  ? 72  GLN A CG    1 
ATOM   597  C  CD    . GLN A 1 72  ? 43.931  45.420  -9.265  1.00 102.00 ? 72  GLN A CD    1 
ATOM   598  O  OE1   . GLN A 1 72  ? 44.886  45.014  -8.602  1.00 94.93  ? 72  GLN A OE1   1 
ATOM   599  N  NE2   . GLN A 1 72  ? 43.875  46.650  -9.761  1.00 100.15 ? 72  GLN A NE2   1 
ATOM   600  N  N     . LYS A 1 73  ? 40.046  42.600  -7.998  1.00 76.99  ? 73  LYS A N     1 
ATOM   601  C  CA    . LYS A 1 73  ? 40.011  41.929  -6.710  1.00 80.56  ? 73  LYS A CA    1 
ATOM   602  C  C     . LYS A 1 73  ? 41.169  40.945  -6.615  1.00 83.49  ? 73  LYS A C     1 
ATOM   603  O  O     . LYS A 1 73  ? 41.850  40.649  -7.600  1.00 75.27  ? 73  LYS A O     1 
ATOM   604  C  CB    . LYS A 1 73  ? 38.675  41.205  -6.495  1.00 70.70  ? 73  LYS A CB    1 
ATOM   605  C  CG    . LYS A 1 73  ? 37.453  42.090  -6.667  1.00 72.77  ? 73  LYS A CG    1 
ATOM   606  C  CD    . LYS A 1 73  ? 36.171  41.338  -6.343  1.00 67.27  ? 73  LYS A CD    1 
ATOM   607  C  CE    . LYS A 1 73  ? 35.857  41.388  -4.856  1.00 62.14  ? 73  LYS A CE    1 
ATOM   608  N  NZ    . LYS A 1 73  ? 35.585  42.776  -4.390  1.00 65.61  ? 73  LYS A NZ    1 
ATOM   609  N  N     . LYS A 1 74  ? 41.389  40.436  -5.409  1.00 79.86  ? 74  LYS A N     1 
ATOM   610  C  CA    . LYS A 1 74  ? 42.457  39.483  -5.147  1.00 87.04  ? 74  LYS A CA    1 
ATOM   611  C  C     . LYS A 1 74  ? 41.880  38.073  -5.178  1.00 84.93  ? 74  LYS A C     1 
ATOM   612  O  O     . LYS A 1 74  ? 41.015  37.732  -4.365  1.00 85.43  ? 74  LYS A O     1 
ATOM   613  C  CB    . LYS A 1 74  ? 43.127  39.772  -3.804  1.00 94.51  ? 74  LYS A CB    1 
ATOM   614  C  CG    . LYS A 1 74  ? 43.273  41.258  -3.494  1.00 92.73  ? 74  LYS A CG    1 
ATOM   615  C  CD    . LYS A 1 74  ? 43.926  41.503  -2.138  1.00 102.36 ? 74  LYS A CD    1 
ATOM   616  C  CE    . LYS A 1 74  ? 44.945  40.427  -1.794  1.00 104.11 ? 74  LYS A CE    1 
ATOM   617  N  NZ    . LYS A 1 74  ? 45.142  40.306  -0.323  1.00 108.47 ? 74  LYS A NZ    1 
ATOM   618  N  N     . PHE A 1 75  ? 42.353  37.265  -6.125  1.00 82.89  ? 75  PHE A N     1 
ATOM   619  C  CA    . PHE A 1 75  ? 41.921  35.884  -6.285  1.00 72.01  ? 75  PHE A CA    1 
ATOM   620  C  C     . PHE A 1 75  ? 43.154  35.009  -6.436  1.00 84.49  ? 75  PHE A C     1 
ATOM   621  O  O     . PHE A 1 75  ? 44.029  35.306  -7.256  1.00 94.02  ? 75  PHE A O     1 
ATOM   622  C  CB    . PHE A 1 75  ? 41.002  35.731  -7.501  1.00 78.10  ? 75  PHE A CB    1 
ATOM   623  C  CG    . PHE A 1 75  ? 40.284  34.413  -7.562  1.00 79.91  ? 75  PHE A CG    1 
ATOM   624  C  CD1   . PHE A 1 75  ? 39.338  34.077  -6.608  1.00 79.14  ? 75  PHE A CD1   1 
ATOM   625  C  CD2   . PHE A 1 75  ? 40.550  33.513  -8.580  1.00 74.17  ? 75  PHE A CD2   1 
ATOM   626  C  CE1   . PHE A 1 75  ? 38.672  32.867  -6.667  1.00 64.26  ? 75  PHE A CE1   1 
ATOM   627  C  CE2   . PHE A 1 75  ? 39.889  32.301  -8.644  1.00 75.07  ? 75  PHE A CE2   1 
ATOM   628  C  CZ    . PHE A 1 75  ? 38.949  31.978  -7.686  1.00 69.58  ? 75  PHE A CZ    1 
ATOM   629  N  N     . LEU A 1 76  ? 43.222  33.940  -5.641  1.00 79.63  ? 76  LEU A N     1 
ATOM   630  C  CA    . LEU A 1 76  ? 44.374  33.036  -5.618  1.00 89.65  ? 76  LEU A CA    1 
ATOM   631  C  C     . LEU A 1 76  ? 45.656  33.760  -5.214  1.00 88.06  ? 76  LEU A C     1 
ATOM   632  O  O     . LEU A 1 76  ? 46.752  33.388  -5.641  1.00 90.28  ? 76  LEU A O     1 
ATOM   633  C  CB    . LEU A 1 76  ? 44.568  32.331  -6.966  1.00 90.28  ? 76  LEU A CB    1 
ATOM   634  C  CG    . LEU A 1 76  ? 43.477  31.371  -7.443  1.00 101.60 ? 76  LEU A CG    1 
ATOM   635  C  CD1   . LEU A 1 76  ? 43.981  30.543  -8.617  1.00 74.38  ? 76  LEU A CD1   1 
ATOM   636  C  CD2   . LEU A 1 76  ? 43.011  30.473  -6.307  1.00 97.90  ? 76  LEU A CD2   1 
ATOM   637  N  N     . GLY A 1 77  ? 45.534  34.801  -4.393  1.00 85.82  ? 77  GLY A N     1 
ATOM   638  C  CA    . GLY A 1 77  ? 46.689  35.543  -3.933  1.00 95.81  ? 77  GLY A CA    1 
ATOM   639  C  C     . GLY A 1 77  ? 47.277  36.519  -4.928  1.00 97.44  ? 77  GLY A C     1 
ATOM   640  O  O     . GLY A 1 77  ? 48.234  37.224  -4.582  1.00 100.94 ? 77  GLY A O     1 
ATOM   641  N  N     . ARG A 1 78  ? 46.750  36.583  -6.149  1.00 95.49  ? 78  ARG A N     1 
ATOM   642  C  CA    . ARG A 1 78  ? 47.224  37.550  -7.120  1.00 101.88 ? 78  ARG A CA    1 
ATOM   643  C  C     . ARG A 1 78  ? 46.063  38.400  -7.620  1.00 104.38 ? 78  ARG A C     1 
ATOM   644  O  O     . ARG A 1 78  ? 44.944  37.898  -7.764  1.00 100.73 ? 78  ARG A O     1 
ATOM   645  C  CB    . ARG A 1 78  ? 47.911  36.860  -8.308  1.00 102.61 ? 78  ARG A CB    1 
ATOM   646  C  CG    . ARG A 1 78  ? 49.180  36.119  -7.927  1.00 110.25 ? 78  ARG A CG    1 
ATOM   647  C  CD    . ARG A 1 78  ? 50.060  35.837  -9.142  1.00 113.56 ? 78  ARG A CD    1 
ATOM   648  N  NE    . ARG A 1 78  ? 51.257  35.045  -8.858  1.00 122.25 ? 78  ARG A NE    1 
ATOM   649  C  CZ    . ARG A 1 78  ? 52.120  35.253  -7.868  1.00 125.84 ? 78  ARG A CZ    1 
ATOM   650  N  NH1   . ARG A 1 78  ? 52.021  36.298  -7.060  1.00 125.76 ? 78  ARG A NH1   1 
ATOM   651  N  NH2   . ARG A 1 78  ? 53.125  34.399  -7.697  1.00 110.76 ? 78  ARG A NH2   1 
ATOM   652  N  N     . PRO A 1 79  ? 46.292  39.687  -7.886  1.00 99.29  ? 79  PRO A N     1 
ATOM   653  C  CA    . PRO A 1 79  ? 45.189  40.569  -8.300  1.00 85.84  ? 79  PRO A CA    1 
ATOM   654  C  C     . PRO A 1 79  ? 44.677  40.192  -9.682  1.00 89.55  ? 79  PRO A C     1 
ATOM   655  O  O     . PRO A 1 79  ? 45.424  40.204  -10.662 1.00 99.00  ? 79  PRO A O     1 
ATOM   656  C  CB    . PRO A 1 79  ? 45.822  41.967  -8.288  1.00 75.91  ? 79  PRO A CB    1 
ATOM   657  C  CG    . PRO A 1 79  ? 47.146  41.810  -7.584  1.00 87.20  ? 79  PRO A CG    1 
ATOM   658  C  CD    . PRO A 1 79  ? 47.574  40.404  -7.824  1.00 87.32  ? 79  PRO A CD    1 
ATOM   659  N  N     . VAL A 1 80  ? 43.392  39.858  -9.753  1.00 90.88  ? 80  VAL A N     1 
ATOM   660  C  CA    . VAL A 1 80  ? 42.734  39.495  -11.001 1.00 87.80  ? 80  VAL A CA    1 
ATOM   661  C  C     . VAL A 1 80  ? 41.685  40.554  -11.310 1.00 86.93  ? 80  VAL A C     1 
ATOM   662  O  O     . VAL A 1 80  ? 41.121  41.182  -10.406 1.00 76.79  ? 80  VAL A O     1 
ATOM   663  C  CB    . VAL A 1 80  ? 42.106  38.086  -10.915 1.00 91.31  ? 80  VAL A CB    1 
ATOM   664  C  CG1   . VAL A 1 80  ? 41.449  37.689  -12.231 1.00 90.75  ? 80  VAL A CG1   1 
ATOM   665  C  CG2   . VAL A 1 80  ? 43.156  37.061  -10.512 1.00 92.99  ? 80  VAL A CG2   1 
ATOM   666  N  N     . GLU A 1 81  ? 41.442  40.768  -12.601 1.00 102.76 ? 81  GLU A N     1 
ATOM   667  C  CA    . GLU A 1 81  ? 40.440  41.722  -13.056 1.00 94.63  ? 81  GLU A CA    1 
ATOM   668  C  C     . GLU A 1 81  ? 39.104  41.005  -13.217 1.00 86.85  ? 81  GLU A C     1 
ATOM   669  O  O     . GLU A 1 81  ? 38.978  40.092  -14.041 1.00 76.07  ? 81  GLU A O     1 
ATOM   670  C  CB    . GLU A 1 81  ? 40.876  42.370  -14.369 1.00 93.30  ? 81  GLU A CB    1 
ATOM   671  C  CG    . GLU A 1 81  ? 40.639  43.866  -14.426 1.00 96.26  ? 81  GLU A CG    1 
ATOM   672  C  CD    . GLU A 1 81  ? 40.884  44.439  -15.805 1.00 107.93 ? 81  GLU A CD    1 
ATOM   673  O  OE1   . GLU A 1 81  ? 40.720  43.698  -16.798 1.00 111.53 ? 81  GLU A OE1   1 
ATOM   674  O  OE2   . GLU A 1 81  ? 41.249  45.629  -15.896 1.00 114.52 ? 81  GLU A OE2   1 
ATOM   675  N  N     . VAL A 1 82  ? 38.113  41.415  -12.426 1.00 80.14  ? 82  VAL A N     1 
ATOM   676  C  CA    . VAL A 1 82  ? 36.811  40.762  -12.406 1.00 85.74  ? 82  VAL A CA    1 
ATOM   677  C  C     . VAL A 1 82  ? 35.738  41.786  -12.756 1.00 77.76  ? 82  VAL A C     1 
ATOM   678  O  O     . VAL A 1 82  ? 35.919  42.997  -12.607 1.00 84.33  ? 82  VAL A O     1 
ATOM   679  C  CB    . VAL A 1 82  ? 36.512  40.094  -11.045 1.00 76.85  ? 82  VAL A CB    1 
ATOM   680  C  CG1   . VAL A 1 82  ? 36.015  41.121  -10.033 1.00 77.88  ? 82  VAL A CG1   1 
ATOM   681  C  CG2   . VAL A 1 82  ? 35.510  38.953  -11.211 1.00 84.00  ? 82  VAL A CG2   1 
ATOM   682  N  N     . TRP A 1 83  ? 34.607  41.281  -13.234 1.00 81.76  ? 83  TRP A N     1 
ATOM   683  C  CA    . TRP A 1 83  ? 33.505  42.112  -13.698 1.00 81.45  ? 83  TRP A CA    1 
ATOM   684  C  C     . TRP A 1 83  ? 32.361  42.015  -12.699 1.00 78.70  ? 83  TRP A C     1 
ATOM   685  O  O     . TRP A 1 83  ? 31.887  40.914  -12.400 1.00 73.28  ? 83  TRP A O     1 
ATOM   686  C  CB    . TRP A 1 83  ? 33.028  41.664  -15.078 1.00 75.72  ? 83  TRP A CB    1 
ATOM   687  C  CG    . TRP A 1 83  ? 33.607  42.392  -16.258 1.00 95.19  ? 83  TRP A CG    1 
ATOM   688  C  CD1   . TRP A 1 83  ? 34.324  41.839  -17.278 1.00 96.73  ? 83  TRP A CD1   1 
ATOM   689  C  CD2   . TRP A 1 83  ? 33.484  43.786  -16.568 1.00 99.96  ? 83  TRP A CD2   1 
ATOM   690  N  NE1   . TRP A 1 83  ? 34.664  42.799  -18.200 1.00 99.46  ? 83  TRP A NE1   1 
ATOM   691  C  CE2   . TRP A 1 83  ? 34.151  44.002  -17.794 1.00 103.86 ? 83  TRP A CE2   1 
ATOM   692  C  CE3   . TRP A 1 83  ? 32.866  44.869  -15.939 1.00 94.09  ? 83  TRP A CE3   1 
ATOM   693  C  CZ2   . TRP A 1 83  ? 34.228  45.257  -18.392 1.00 97.99  ? 83  TRP A CZ2   1 
ATOM   694  C  CZ3   . TRP A 1 83  ? 32.940  46.112  -16.539 1.00 96.64  ? 83  TRP A CZ3   1 
ATOM   695  C  CH2   . TRP A 1 83  ? 33.623  46.298  -17.746 1.00 97.56  ? 83  TRP A CH2   1 
ATOM   696  N  N     . LYS A 1 84  ? 31.909  43.164  -12.203 1.00 73.75  ? 84  LYS A N     1 
ATOM   697  C  CA    . LYS A 1 84  ? 30.811  43.224  -11.247 1.00 71.24  ? 84  LYS A CA    1 
ATOM   698  C  C     . LYS A 1 84  ? 29.497  43.439  -11.989 1.00 67.32  ? 84  LYS A C     1 
ATOM   699  O  O     . LYS A 1 84  ? 29.373  44.373  -12.788 1.00 74.93  ? 84  LYS A O     1 
ATOM   700  C  CB    . LYS A 1 84  ? 31.046  44.347  -10.238 1.00 72.29  ? 84  LYS A CB    1 
ATOM   701  C  CG    . LYS A 1 84  ? 30.114  44.344  -9.037  1.00 63.55  ? 84  LYS A CG    1 
ATOM   702  C  CD    . LYS A 1 84  ? 30.427  45.523  -8.130  1.00 56.69  ? 84  LYS A CD    1 
ATOM   703  C  CE    . LYS A 1 84  ? 29.852  45.336  -6.739  1.00 60.92  ? 84  LYS A CE    1 
ATOM   704  N  NZ    . LYS A 1 84  ? 30.030  46.550  -5.897  1.00 64.07  ? 84  LYS A NZ    1 
ATOM   705  N  N     . LEU A 1 85  ? 28.520  42.578  -11.722 1.00 69.19  ? 85  LEU A N     1 
ATOM   706  C  CA    . LEU A 1 85  ? 27.240  42.589  -12.425 1.00 69.92  ? 85  LEU A CA    1 
ATOM   707  C  C     . LEU A 1 85  ? 26.154  43.038  -11.456 1.00 72.12  ? 85  LEU A C     1 
ATOM   708  O  O     . LEU A 1 85  ? 25.801  42.302  -10.529 1.00 66.21  ? 85  LEU A O     1 
ATOM   709  C  CB    . LEU A 1 85  ? 26.928  41.209  -12.999 1.00 64.85  ? 85  LEU A CB    1 
ATOM   710  C  CG    . LEU A 1 85  ? 28.006  40.627  -13.914 1.00 64.07  ? 85  LEU A CG    1 
ATOM   711  C  CD1   . LEU A 1 85  ? 27.525  39.351  -14.573 1.00 61.50  ? 85  LEU A CD1   1 
ATOM   712  C  CD2   . LEU A 1 85  ? 28.417  41.643  -14.962 1.00 64.64  ? 85  LEU A CD2   1 
ATOM   713  N  N     . TYR A 1 86  ? 25.622  44.238  -11.676 1.00 66.88  ? 86  TYR A N     1 
ATOM   714  C  CA    . TYR A 1 86  ? 24.579  44.790  -10.822 1.00 69.47  ? 86  TYR A CA    1 
ATOM   715  C  C     . TYR A 1 86  ? 23.203  44.398  -11.341 1.00 67.32  ? 86  TYR A C     1 
ATOM   716  O  O     . TYR A 1 86  ? 22.982  44.310  -12.553 1.00 75.40  ? 86  TYR A O     1 
ATOM   717  C  CB    . TYR A 1 86  ? 24.682  46.312  -10.755 1.00 61.88  ? 86  TYR A CB    1 
ATOM   718  C  CG    . TYR A 1 86  ? 25.823  46.837  -9.917  1.00 65.90  ? 86  TYR A CG    1 
ATOM   719  C  CD1   . TYR A 1 86  ? 25.699  46.960  -8.540  1.00 69.47  ? 86  TYR A CD1   1 
ATOM   720  C  CD2   . TYR A 1 86  ? 27.019  47.227  -10.506 1.00 63.31  ? 86  TYR A CD2   1 
ATOM   721  C  CE1   . TYR A 1 86  ? 26.739  47.448  -7.770  1.00 68.31  ? 86  TYR A CE1   1 
ATOM   722  C  CE2   . TYR A 1 86  ? 28.063  47.716  -9.746  1.00 58.62  ? 86  TYR A CE2   1 
ATOM   723  C  CZ    . TYR A 1 86  ? 27.917  47.826  -8.378  1.00 67.59  ? 86  TYR A CZ    1 
ATOM   724  O  OH    . TYR A 1 86  ? 28.953  48.313  -7.615  1.00 80.49  ? 86  TYR A OH    1 
ATOM   725  N  N     . PHE A 1 87  ? 22.274  44.178  -10.416 1.00 65.16  ? 87  PHE A N     1 
ATOM   726  C  CA    . PHE A 1 87  ? 20.912  43.793  -10.750 1.00 70.20  ? 87  PHE A CA    1 
ATOM   727  C  C     . PHE A 1 87  ? 19.937  44.691  -10.004 1.00 67.74  ? 87  PHE A C     1 
ATOM   728  O  O     . PHE A 1 87  ? 20.308  45.424  -9.084  1.00 69.39  ? 87  PHE A O     1 
ATOM   729  C  CB    . PHE A 1 87  ? 20.652  42.319  -10.418 1.00 60.89  ? 87  PHE A CB    1 
ATOM   730  C  CG    . PHE A 1 87  ? 21.546  41.372  -11.160 1.00 73.99  ? 87  PHE A CG    1 
ATOM   731  C  CD1   . PHE A 1 87  ? 22.779  41.012  -10.640 1.00 64.03  ? 87  PHE A CD1   1 
ATOM   732  C  CD2   . PHE A 1 87  ? 21.163  40.854  -12.385 1.00 76.89  ? 87  PHE A CD2   1 
ATOM   733  C  CE1   . PHE A 1 87  ? 23.608  40.148  -11.324 1.00 63.53  ? 87  PHE A CE1   1 
ATOM   734  C  CE2   . PHE A 1 87  ? 21.989  39.987  -13.074 1.00 82.58  ? 87  PHE A CE2   1 
ATOM   735  C  CZ    . PHE A 1 87  ? 23.213  39.634  -12.543 1.00 70.78  ? 87  PHE A CZ    1 
ATOM   736  N  N     . THR A 1 88  ? 18.672  44.633  -10.420 1.00 70.82  ? 88  THR A N     1 
ATOM   737  C  CA    . THR A 1 88  ? 17.648  45.441  -9.770  1.00 62.22  ? 88  THR A CA    1 
ATOM   738  C  C     . THR A 1 88  ? 17.222  44.829  -8.441  1.00 63.27  ? 88  THR A C     1 
ATOM   739  O  O     . THR A 1 88  ? 17.162  45.523  -7.421  1.00 61.32  ? 88  THR A O     1 
ATOM   740  C  CB    . THR A 1 88  ? 16.440  45.604  -10.695 1.00 62.33  ? 88  THR A CB    1 
ATOM   741  O  OG1   . THR A 1 88  ? 16.851  46.230  -11.915 1.00 64.01  ? 88  THR A OG1   1 
ATOM   742  C  CG2   . THR A 1 88  ? 15.372  46.456  -10.028 1.00 64.04  ? 88  THR A CG2   1 
ATOM   743  N  N     . HIS A 1 89  ? 16.938  43.527  -8.434  1.00 62.04  ? 89  HIS A N     1 
ATOM   744  C  CA    . HIS A 1 89  ? 16.376  42.849  -7.278  1.00 66.45  ? 89  HIS A CA    1 
ATOM   745  C  C     . HIS A 1 89  ? 17.186  41.601  -6.955  1.00 62.93  ? 89  HIS A C     1 
ATOM   746  O  O     . HIS A 1 89  ? 17.707  40.946  -7.865  1.00 68.33  ? 89  HIS A O     1 
ATOM   747  C  CB    . HIS A 1 89  ? 14.909  42.469  -7.543  1.00 75.12  ? 89  HIS A CB    1 
ATOM   748  C  CG    . HIS A 1 89  ? 14.094  42.293  -6.300  1.00 62.13  ? 89  HIS A CG    1 
ATOM   749  N  ND1   . HIS A 1 89  ? 14.050  41.106  -5.601  1.00 58.57  ? 89  HIS A ND1   1 
ATOM   750  C  CD2   . HIS A 1 89  ? 13.301  43.157  -5.625  1.00 65.37  ? 89  HIS A CD2   1 
ATOM   751  C  CE1   . HIS A 1 89  ? 13.261  41.246  -4.551  1.00 68.10  ? 89  HIS A CE1   1 
ATOM   752  N  NE2   . HIS A 1 89  ? 12.794  42.481  -4.542  1.00 72.97  ? 89  HIS A NE2   1 
ATOM   753  N  N     . PRO A 1 90  ? 17.319  41.251  -5.669  1.00 64.46  ? 90  PRO A N     1 
ATOM   754  C  CA    . PRO A 1 90  ? 18.078  40.036  -5.322  1.00 61.49  ? 90  PRO A CA    1 
ATOM   755  C  C     . PRO A 1 90  ? 17.531  38.777  -5.968  1.00 71.75  ? 90  PRO A C     1 
ATOM   756  O  O     . PRO A 1 90  ? 18.310  37.945  -6.448  1.00 74.81  ? 90  PRO A O     1 
ATOM   757  C  CB    . PRO A 1 90  ? 17.968  39.975  -3.791  1.00 62.66  ? 90  PRO A CB    1 
ATOM   758  C  CG    . PRO A 1 90  ? 17.618  41.345  -3.362  1.00 65.01  ? 90  PRO A CG    1 
ATOM   759  C  CD    . PRO A 1 90  ? 16.904  42.017  -4.483  1.00 58.41  ? 90  PRO A CD    1 
ATOM   760  N  N     . GLN A 1 91  ? 16.206  38.614  -5.999  1.00 70.19  ? 91  GLN A N     1 
ATOM   761  C  CA    . GLN A 1 91  ? 15.615  37.424  -6.601  1.00 62.42  ? 91  GLN A CA    1 
ATOM   762  C  C     . GLN A 1 91  ? 15.867  37.332  -8.099  1.00 66.65  ? 91  GLN A C     1 
ATOM   763  O  O     . GLN A 1 91  ? 15.540  36.303  -8.701  1.00 75.11  ? 91  GLN A O     1 
ATOM   764  C  CB    . GLN A 1 91  ? 14.111  37.382  -6.323  1.00 73.66  ? 91  GLN A CB    1 
ATOM   765  C  CG    . GLN A 1 91  ? 13.716  37.924  -4.964  1.00 66.15  ? 91  GLN A CG    1 
ATOM   766  C  CD    . GLN A 1 91  ? 12.631  37.099  -4.302  1.00 85.10  ? 91  GLN A CD    1 
ATOM   767  O  OE1   . GLN A 1 91  ? 12.730  35.875  -4.221  1.00 114.05 ? 91  GLN A OE1   1 
ATOM   768  N  NE2   . GLN A 1 91  ? 11.586  37.767  -3.827  1.00 75.74  ? 91  GLN A NE2   1 
ATOM   769  N  N     . ASP A 1 92  ? 16.429  38.373  -8.716  1.00 66.20  ? 92  ASP A N     1 
ATOM   770  C  CA    . ASP A 1 92  ? 16.852  38.253  -10.105 1.00 76.58  ? 92  ASP A CA    1 
ATOM   771  C  C     . ASP A 1 92  ? 18.009  37.272  -10.238 1.00 79.95  ? 92  ASP A C     1 
ATOM   772  O  O     . ASP A 1 92  ? 18.018  36.438  -11.151 1.00 91.04  ? 92  ASP A O     1 
ATOM   773  C  CB    . ASP A 1 92  ? 17.252  39.622  -10.659 1.00 82.55  ? 92  ASP A CB    1 
ATOM   774  C  CG    . ASP A 1 92  ? 16.076  40.572  -10.782 1.00 89.05  ? 92  ASP A CG    1 
ATOM   775  O  OD1   . ASP A 1 92  ? 14.930  40.092  -10.910 1.00 85.93  ? 92  ASP A OD1   1 
ATOM   776  O  OD2   . ASP A 1 92  ? 16.302  41.801  -10.753 1.00 80.21  ? 92  ASP A OD2   1 
ATOM   777  N  N     . GLN A 1 93  ? 18.973  37.340  -9.317  1.00 66.84  ? 93  GLN A N     1 
ATOM   778  C  CA    . GLN A 1 93  ? 20.218  36.577  -9.427  1.00 65.08  ? 93  GLN A CA    1 
ATOM   779  C  C     . GLN A 1 93  ? 20.018  35.089  -9.695  1.00 74.77  ? 93  GLN A C     1 
ATOM   780  O  O     . GLN A 1 93  ? 20.610  34.582  -10.661 1.00 74.63  ? 93  GLN A O     1 
ATOM   781  C  CB    . GLN A 1 93  ? 21.061  36.801  -8.162  1.00 61.33  ? 93  GLN A CB    1 
ATOM   782  C  CG    . GLN A 1 93  ? 21.267  38.261  -7.792  1.00 58.56  ? 93  GLN A CG    1 
ATOM   783  C  CD    . GLN A 1 93  ? 22.389  38.451  -6.790  1.00 64.76  ? 93  GLN A CD    1 
ATOM   784  O  OE1   . GLN A 1 93  ? 23.300  37.629  -6.698  1.00 74.44  ? 93  GLN A OE1   1 
ATOM   785  N  NE2   . GLN A 1 93  ? 22.327  39.539  -6.029  1.00 60.98  ? 93  GLN A NE2   1 
ATOM   786  N  N     . PRO A 1 94  ? 19.221  34.338  -8.921  1.00 72.14  ? 94  PRO A N     1 
ATOM   787  C  CA    . PRO A 1 94  ? 19.075  32.906  -9.237  1.00 72.99  ? 94  PRO A CA    1 
ATOM   788  C  C     . PRO A 1 94  ? 18.382  32.650  -10.564 1.00 79.08  ? 94  PRO A C     1 
ATOM   789  O  O     . PRO A 1 94  ? 18.645  31.620  -11.197 1.00 82.22  ? 94  PRO A O     1 
ATOM   790  C  CB    . PRO A 1 94  ? 18.258  32.364  -8.056  1.00 64.41  ? 94  PRO A CB    1 
ATOM   791  C  CG    . PRO A 1 94  ? 17.521  33.534  -7.542  1.00 62.17  ? 94  PRO A CG    1 
ATOM   792  C  CD    . PRO A 1 94  ? 18.415  34.718  -7.746  1.00 68.20  ? 94  PRO A CD    1 
ATOM   793  N  N     . ALA A 1 95  ? 17.511  33.557  -11.009 1.00 76.00  ? 95  ALA A N     1 
ATOM   794  C  CA    . ALA A 1 95  ? 16.821  33.402  -12.284 1.00 82.48  ? 95  ALA A CA    1 
ATOM   795  C  C     . ALA A 1 95  ? 17.709  33.690  -13.488 1.00 85.42  ? 95  ALA A C     1 
ATOM   796  O  O     . ALA A 1 95  ? 17.326  33.344  -14.611 1.00 88.63  ? 95  ALA A O     1 
ATOM   797  C  CB    . ALA A 1 95  ? 15.590  34.313  -12.331 1.00 83.66  ? 95  ALA A CB    1 
ATOM   798  N  N     . ILE A 1 96  ? 18.873  34.303  -13.290 1.00 84.05  ? 96  ILE A N     1 
ATOM   799  C  CA    . ILE A 1 96  ? 19.742  34.667  -14.401 1.00 82.51  ? 96  ILE A CA    1 
ATOM   800  C  C     . ILE A 1 96  ? 21.150  34.095  -14.263 1.00 82.12  ? 96  ILE A C     1 
ATOM   801  O  O     . ILE A 1 96  ? 21.857  33.979  -15.279 1.00 83.11  ? 96  ILE A O     1 
ATOM   802  C  CB    . ILE A 1 96  ? 19.795  36.206  -14.567 1.00 78.33  ? 96  ILE A CB    1 
ATOM   803  C  CG1   . ILE A 1 96  ? 20.763  36.643  -15.666 1.00 79.20  ? 96  ILE A CG1   1 
ATOM   804  C  CG2   . ILE A 1 96  ? 20.203  36.868  -13.261 1.00 82.36  ? 96  ILE A CG2   1 
ATOM   805  C  CD1   . ILE A 1 96  ? 20.793  38.141  -15.890 1.00 77.11  ? 96  ILE A CD1   1 
ATOM   806  N  N     . ARG A 1 97  ? 21.569  33.686  -13.060 1.00 77.56  ? 97  ARG A N     1 
ATOM   807  C  CA    . ARG A 1 97  ? 22.954  33.273  -12.837 1.00 80.93  ? 97  ARG A CA    1 
ATOM   808  C  C     . ARG A 1 97  ? 23.378  32.154  -13.783 1.00 88.02  ? 97  ARG A C     1 
ATOM   809  O  O     . ARG A 1 97  ? 24.505  32.161  -14.294 1.00 90.85  ? 97  ARG A O     1 
ATOM   810  C  CB    . ARG A 1 97  ? 23.146  32.842  -11.381 1.00 77.40  ? 97  ARG A CB    1 
ATOM   811  C  CG    . ARG A 1 97  ? 22.315  31.636  -10.967 1.00 79.83  ? 97  ARG A CG    1 
ATOM   812  C  CD    . ARG A 1 97  ? 22.957  30.883  -9.818  1.00 78.77  ? 97  ARG A CD    1 
ATOM   813  N  NE    . ARG A 1 97  ? 22.492  31.371  -8.526  1.00 79.83  ? 97  ARG A NE    1 
ATOM   814  C  CZ    . ARG A 1 97  ? 21.594  30.751  -7.774  1.00 71.73  ? 97  ARG A CZ    1 
ATOM   815  N  NH1   . ARG A 1 97  ? 21.046  29.608  -8.153  1.00 78.03  ? 97  ARG A NH1   1 
ATOM   816  N  NH2   . ARG A 1 97  ? 21.236  31.290  -6.612  1.00 73.30  ? 97  ARG A NH2   1 
ATOM   817  N  N     . ASP A 1 98  ? 22.494  31.185  -14.034 1.00 90.35  ? 98  ASP A N     1 
ATOM   818  C  CA    . ASP A 1 98  ? 22.857  30.072  -14.906 1.00 82.34  ? 98  ASP A CA    1 
ATOM   819  C  C     . ASP A 1 98  ? 23.005  30.530  -16.350 1.00 84.90  ? 98  ASP A C     1 
ATOM   820  O  O     . ASP A 1 98  ? 23.934  30.107  -17.049 1.00 96.83  ? 98  ASP A O     1 
ATOM   821  C  CB    . ASP A 1 98  ? 21.818  28.956  -14.801 1.00 91.80  ? 98  ASP A CB    1 
ATOM   822  C  CG    . ASP A 1 98  ? 21.867  28.238  -13.466 1.00 100.64 ? 98  ASP A CG    1 
ATOM   823  O  OD1   . ASP A 1 98  ? 22.962  28.156  -12.871 1.00 104.83 ? 98  ASP A OD1   1 
ATOM   824  O  OD2   . ASP A 1 98  ? 20.809  27.752  -13.014 1.00 107.03 ? 98  ASP A OD2   1 
ATOM   825  N  N     . LYS A 1 99  ? 22.100  31.397  -16.814 1.00 87.49  ? 99  LYS A N     1 
ATOM   826  C  CA    . LYS A 1 99  ? 22.200  31.926  -18.170 1.00 95.80  ? 99  LYS A CA    1 
ATOM   827  C  C     . LYS A 1 99  ? 23.512  32.664  -18.386 1.00 91.82  ? 99  LYS A C     1 
ATOM   828  O  O     . LYS A 1 99  ? 24.039  32.681  -19.504 1.00 93.83  ? 99  LYS A O     1 
ATOM   829  C  CB    . LYS A 1 99  ? 21.023  32.856  -18.461 1.00 92.31  ? 99  LYS A CB    1 
ATOM   830  C  CG    . LYS A 1 99  ? 19.673  32.169  -18.478 1.00 90.09  ? 99  LYS A CG    1 
ATOM   831  C  CD    . LYS A 1 99  ? 18.887  32.571  -19.712 1.00 91.09  ? 99  LYS A CD    1 
ATOM   832  C  CE    . LYS A 1 99  ? 17.549  31.859  -19.774 1.00 87.69  ? 99  LYS A CE    1 
ATOM   833  N  NZ    . LYS A 1 99  ? 16.659  32.472  -20.796 1.00 94.99  ? 99  LYS A NZ    1 
ATOM   834  N  N     . ILE A 1 100 ? 24.050  33.278  -17.335 1.00 88.68  ? 100 ILE A N     1 
ATOM   835  C  CA    . ILE A 1 100 ? 25.329  33.967  -17.453 1.00 88.60  ? 100 ILE A CA    1 
ATOM   836  C  C     . ILE A 1 100 ? 26.463  32.956  -17.548 1.00 96.19  ? 100 ILE A C     1 
ATOM   837  O  O     . ILE A 1 100 ? 27.230  32.958  -18.513 1.00 102.47 ? 100 ILE A O     1 
ATOM   838  C  CB    . ILE A 1 100 ? 25.526  34.939  -16.279 1.00 87.64  ? 100 ILE A CB    1 
ATOM   839  C  CG1   . ILE A 1 100 ? 24.468  36.043  -16.350 1.00 88.26  ? 100 ILE A CG1   1 
ATOM   840  C  CG2   . ILE A 1 100 ? 26.937  35.512  -16.301 1.00 74.83  ? 100 ILE A CG2   1 
ATOM   841  C  CD1   . ILE A 1 100 ? 24.879  37.347  -15.729 1.00 85.57  ? 100 ILE A CD1   1 
ATOM   842  N  N     . ARG A 1 101 ? 26.563  32.063  -16.557 1.00 92.43  ? 101 ARG A N     1 
ATOM   843  C  CA    . ARG A 1 101 ? 27.604  31.035  -16.556 1.00 85.44  ? 101 ARG A CA    1 
ATOM   844  C  C     . ARG A 1 101 ? 27.688  30.304  -17.892 1.00 96.81  ? 101 ARG A C     1 
ATOM   845  O  O     . ARG A 1 101 ? 28.785  30.068  -18.411 1.00 97.41  ? 101 ARG A O     1 
ATOM   846  C  CB    . ARG A 1 101 ? 27.343  30.035  -15.429 1.00 93.28  ? 101 ARG A CB    1 
ATOM   847  C  CG    . ARG A 1 101 ? 28.566  29.257  -14.973 1.00 87.31  ? 101 ARG A CG    1 
ATOM   848  C  CD    . ARG A 1 101 ? 28.524  29.012  -13.476 1.00 87.22  ? 101 ARG A CD    1 
ATOM   849  N  NE    . ARG A 1 101 ? 27.178  28.704  -13.010 1.00 99.18  ? 101 ARG A NE    1 
ATOM   850  C  CZ    . ARG A 1 101 ? 26.829  28.623  -11.733 1.00 101.19 ? 101 ARG A CZ    1 
ATOM   851  N  NH1   . ARG A 1 101 ? 27.706  28.824  -10.763 1.00 91.58  ? 101 ARG A NH1   1 
ATOM   852  N  NH2   . ARG A 1 101 ? 25.569  28.335  -11.422 1.00 93.71  ? 101 ARG A NH2   1 
ATOM   853  N  N     . GLU A 1 102 ? 26.537  29.950  -18.469 1.00 96.92  ? 102 GLU A N     1 
ATOM   854  C  CA    . GLU A 1 102 ? 26.504  29.207  -19.724 1.00 95.35  ? 102 GLU A CA    1 
ATOM   855  C  C     . GLU A 1 102 ? 27.033  30.005  -20.909 1.00 94.03  ? 102 GLU A C     1 
ATOM   856  O  O     . GLU A 1 102 ? 27.250  29.419  -21.975 1.00 95.96  ? 102 GLU A O     1 
ATOM   857  C  CB    . GLU A 1 102 ? 25.078  28.737  -20.015 1.00 105.29 ? 102 GLU A CB    1 
ATOM   858  C  CG    . GLU A 1 102 ? 24.590  27.628  -19.098 1.00 116.04 ? 102 GLU A CG    1 
ATOM   859  C  CD    . GLU A 1 102 ? 23.093  27.416  -19.193 1.00 128.92 ? 102 GLU A CD    1 
ATOM   860  O  OE1   . GLU A 1 102 ? 22.405  28.286  -19.769 1.00 121.48 ? 102 GLU A OE1   1 
ATOM   861  O  OE2   . GLU A 1 102 ? 22.605  26.382  -18.692 1.00 132.14 ? 102 GLU A OE2   1 
ATOM   862  N  N     . HIS A 1 103 ? 27.234  31.310  -20.759 1.00 97.91  ? 103 HIS A N     1 
ATOM   863  C  CA    . HIS A 1 103 ? 27.833  32.098  -21.829 1.00 105.39 ? 103 HIS A CA    1 
ATOM   864  C  C     . HIS A 1 103 ? 29.274  31.638  -22.022 1.00 106.44 ? 103 HIS A C     1 
ATOM   865  O  O     . HIS A 1 103 ? 29.996  31.450  -21.036 1.00 96.88  ? 103 HIS A O     1 
ATOM   866  C  CB    . HIS A 1 103 ? 27.772  33.592  -21.490 1.00 104.94 ? 103 HIS A CB    1 
ATOM   867  C  CG    . HIS A 1 103 ? 28.193  34.500  -22.608 1.00 109.29 ? 103 HIS A CG    1 
ATOM   868  N  ND1   . HIS A 1 103 ? 29.364  34.329  -23.315 1.00 104.03 ? 103 HIS A ND1   1 
ATOM   869  C  CD2   . HIS A 1 103 ? 27.595  35.596  -23.134 1.00 111.12 ? 103 HIS A CD2   1 
ATOM   870  C  CE1   . HIS A 1 103 ? 29.465  35.272  -24.234 1.00 106.15 ? 103 HIS A CE1   1 
ATOM   871  N  NE2   . HIS A 1 103 ? 28.406  36.057  -24.142 1.00 113.52 ? 103 HIS A NE2   1 
ATOM   872  N  N     . PRO A 1 104 ? 29.717  31.411  -23.260 1.00 108.40 ? 104 PRO A N     1 
ATOM   873  C  CA    . PRO A 1 104 ? 31.089  30.916  -23.469 1.00 103.17 ? 104 PRO A CA    1 
ATOM   874  C  C     . PRO A 1 104 ? 32.176  31.877  -23.013 1.00 105.59 ? 104 PRO A C     1 
ATOM   875  O  O     . PRO A 1 104 ? 33.248  31.425  -22.591 1.00 109.00 ? 104 PRO A O     1 
ATOM   876  C  CB    . PRO A 1 104 ? 31.146  30.679  -24.985 1.00 98.99  ? 104 PRO A CB    1 
ATOM   877  C  CG    . PRO A 1 104 ? 29.718  30.506  -25.399 1.00 92.00  ? 104 PRO A CG    1 
ATOM   878  C  CD    . PRO A 1 104 ? 28.918  31.388  -24.497 1.00 90.66  ? 104 PRO A CD    1 
ATOM   879  N  N     . ALA A 1 105 ? 31.939  33.188  -23.076 1.00 102.07 ? 105 ALA A N     1 
ATOM   880  C  CA    . ALA A 1 105 ? 32.994  34.143  -22.761 1.00 103.82 ? 105 ALA A CA    1 
ATOM   881  C  C     . ALA A 1 105 ? 33.289  34.233  -21.268 1.00 101.34 ? 105 ALA A C     1 
ATOM   882  O  O     . ALA A 1 105 ? 34.360  34.721  -20.896 1.00 105.53 ? 105 ALA A O     1 
ATOM   883  C  CB    . ALA A 1 105 ? 32.632  35.528  -23.299 1.00 104.52 ? 105 ALA A CB    1 
ATOM   884  N  N     . VAL A 1 106 ? 32.379  33.779  -20.409 1.00 95.01  ? 106 VAL A N     1 
ATOM   885  C  CA    . VAL A 1 106 ? 32.573  33.826  -18.963 1.00 91.65  ? 106 VAL A CA    1 
ATOM   886  C  C     . VAL A 1 106 ? 32.989  32.446  -18.476 1.00 92.85  ? 106 VAL A C     1 
ATOM   887  O  O     . VAL A 1 106 ? 32.380  31.433  -18.844 1.00 92.47  ? 106 VAL A O     1 
ATOM   888  C  CB    . VAL A 1 106 ? 31.305  34.313  -18.242 1.00 92.83  ? 106 VAL A CB    1 
ATOM   889  C  CG1   . VAL A 1 106 ? 30.109  33.556  -18.728 1.00 78.43  ? 106 VAL A CG1   1 
ATOM   890  C  CG2   . VAL A 1 106 ? 31.453  34.178  -16.731 1.00 93.09  ? 106 VAL A CG2   1 
ATOM   891  N  N     . ILE A 1 107 ? 34.033  32.407  -17.650 1.00 87.19  ? 107 ILE A N     1 
ATOM   892  C  CA    . ILE A 1 107 ? 34.536  31.143  -17.129 1.00 82.67  ? 107 ILE A CA    1 
ATOM   893  C  C     . ILE A 1 107 ? 33.687  30.665  -15.958 1.00 80.82  ? 107 ILE A C     1 
ATOM   894  O  O     . ILE A 1 107 ? 33.284  29.498  -15.901 1.00 94.36  ? 107 ILE A O     1 
ATOM   895  C  CB    . ILE A 1 107 ? 36.017  31.294  -16.738 1.00 82.99  ? 107 ILE A CB    1 
ATOM   896  C  CG1   . ILE A 1 107 ? 36.813  31.817  -17.936 1.00 88.63  ? 107 ILE A CG1   1 
ATOM   897  C  CG2   . ILE A 1 107 ? 36.577  29.970  -16.244 1.00 85.09  ? 107 ILE A CG2   1 
ATOM   898  C  CD1   . ILE A 1 107 ? 37.706  32.987  -17.619 1.00 89.64  ? 107 ILE A CD1   1 
ATOM   899  N  N     . ASP A 1 108 ? 33.396  31.557  -15.015 1.00 78.24  ? 108 ASP A N     1 
ATOM   900  C  CA    . ASP A 1 108 ? 32.589  31.215  -13.853 1.00 79.24  ? 108 ASP A CA    1 
ATOM   901  C  C     . ASP A 1 108 ? 32.090  32.503  -13.214 1.00 77.49  ? 108 ASP A C     1 
ATOM   902  O  O     . ASP A 1 108 ? 32.564  33.598  -13.523 1.00 77.21  ? 108 ASP A O     1 
ATOM   903  C  CB    . ASP A 1 108 ? 33.386  30.371  -12.850 1.00 83.93  ? 108 ASP A CB    1 
ATOM   904  C  CG    . ASP A 1 108 ? 32.498  29.495  -11.988 1.00 94.49  ? 108 ASP A CG    1 
ATOM   905  O  OD1   . ASP A 1 108 ? 31.260  29.595  -12.113 1.00 87.13  ? 108 ASP A OD1   1 
ATOM   906  O  OD2   . ASP A 1 108 ? 33.040  28.702  -11.191 1.00 94.34  ? 108 ASP A OD2   1 
ATOM   907  N  N     . ILE A 1 109 ? 31.118  32.355  -12.317 1.00 79.98  ? 109 ILE A N     1 
ATOM   908  C  CA    . ILE A 1 109 ? 30.568  33.471  -11.561 1.00 66.71  ? 109 ILE A CA    1 
ATOM   909  C  C     . ILE A 1 109 ? 30.821  33.225  -10.081 1.00 68.61  ? 109 ILE A C     1 
ATOM   910  O  O     . ILE A 1 109 ? 30.963  32.081  -9.639  1.00 77.39  ? 109 ILE A O     1 
ATOM   911  C  CB    . ILE A 1 109 ? 29.061  33.674  -11.839 1.00 79.31  ? 109 ILE A CB    1 
ATOM   912  C  CG1   . ILE A 1 109 ? 28.319  32.340  -11.766 1.00 79.72  ? 109 ILE A CG1   1 
ATOM   913  C  CG2   . ILE A 1 109 ? 28.855  34.324  -13.198 1.00 74.31  ? 109 ILE A CG2   1 
ATOM   914  C  CD1   . ILE A 1 109 ? 26.816  32.482  -11.803 1.00 73.58  ? 109 ILE A CD1   1 
ATOM   915  N  N     . TYR A 1 110 ? 30.878  34.311  -9.313  1.00 67.46  ? 110 TYR A N     1 
ATOM   916  C  CA    . TYR A 1 110 ? 31.293  34.243  -7.920  1.00 63.36  ? 110 TYR A CA    1 
ATOM   917  C  C     . TYR A 1 110 ? 30.391  35.116  -7.059  1.00 60.30  ? 110 TYR A C     1 
ATOM   918  O  O     . TYR A 1 110 ? 29.925  36.174  -7.492  1.00 62.84  ? 110 TYR A O     1 
ATOM   919  C  CB    . TYR A 1 110 ? 32.757  34.682  -7.759  1.00 68.86  ? 110 TYR A CB    1 
ATOM   920  C  CG    . TYR A 1 110 ? 33.713  33.915  -8.645  1.00 66.87  ? 110 TYR A CG    1 
ATOM   921  C  CD1   . TYR A 1 110 ? 34.128  32.634  -8.306  1.00 70.01  ? 110 TYR A CD1   1 
ATOM   922  C  CD2   . TYR A 1 110 ? 34.185  34.464  -9.829  1.00 68.85  ? 110 TYR A CD2   1 
ATOM   923  C  CE1   . TYR A 1 110 ? 34.996  31.925  -9.116  1.00 81.42  ? 110 TYR A CE1   1 
ATOM   924  C  CE2   . TYR A 1 110 ? 35.053  33.762  -10.647 1.00 74.44  ? 110 TYR A CE2   1 
ATOM   925  C  CZ    . TYR A 1 110 ? 35.455  32.493  -10.284 1.00 79.30  ? 110 TYR A CZ    1 
ATOM   926  O  OH    . TYR A 1 110 ? 36.318  31.787  -11.089 1.00 87.19  ? 110 TYR A OH    1 
ATOM   927  N  N     . GLU A 1 111 ? 30.159  34.657  -5.827  1.00 61.56  ? 111 GLU A N     1 
ATOM   928  C  CA    . GLU A 1 111 ? 29.388  35.401  -4.826  1.00 68.19  ? 111 GLU A CA    1 
ATOM   929  C  C     . GLU A 1 111 ? 27.972  35.696  -5.321  1.00 72.23  ? 111 GLU A C     1 
ATOM   930  O  O     . GLU A 1 111 ? 27.448  36.799  -5.151  1.00 68.54  ? 111 GLU A O     1 
ATOM   931  C  CB    . GLU A 1 111 ? 30.112  36.688  -4.422  1.00 59.59  ? 111 GLU A CB    1 
ATOM   932  C  CG    . GLU A 1 111 ? 31.543  36.453  -3.957  1.00 72.54  ? 111 GLU A CG    1 
ATOM   933  C  CD    . GLU A 1 111 ? 32.162  37.668  -3.296  1.00 70.11  ? 111 GLU A CD    1 
ATOM   934  O  OE1   . GLU A 1 111 ? 31.412  38.607  -2.956  1.00 69.47  ? 111 GLU A OE1   1 
ATOM   935  O  OE2   . GLU A 1 111 ? 33.399  37.685  -3.115  1.00 69.69  ? 111 GLU A OE2   1 
ATOM   936  N  N     . TYR A 1 112 ? 27.347  34.693  -5.936  1.00 65.15  ? 112 TYR A N     1 
ATOM   937  C  CA    . TYR A 1 112 ? 26.017  34.816  -6.515  1.00 65.94  ? 112 TYR A CA    1 
ATOM   938  C  C     . TYR A 1 112 ? 24.917  34.288  -5.605  1.00 73.86  ? 112 TYR A C     1 
ATOM   939  O  O     . TYR A 1 112 ? 23.737  34.414  -5.946  1.00 73.90  ? 112 TYR A O     1 
ATOM   940  C  CB    . TYR A 1 112 ? 25.963  34.079  -7.858  1.00 70.82  ? 112 TYR A CB    1 
ATOM   941  C  CG    . TYR A 1 112 ? 26.439  32.645  -7.774  1.00 78.19  ? 112 TYR A CG    1 
ATOM   942  C  CD1   . TYR A 1 112 ? 25.558  31.617  -7.465  1.00 72.73  ? 112 TYR A CD1   1 
ATOM   943  C  CD2   . TYR A 1 112 ? 27.771  32.319  -7.996  1.00 80.07  ? 112 TYR A CD2   1 
ATOM   944  C  CE1   . TYR A 1 112 ? 25.987  30.308  -7.381  1.00 76.68  ? 112 TYR A CE1   1 
ATOM   945  C  CE2   . TYR A 1 112 ? 28.211  31.012  -7.914  1.00 76.91  ? 112 TYR A CE2   1 
ATOM   946  C  CZ    . TYR A 1 112 ? 27.314  30.011  -7.607  1.00 90.38  ? 112 TYR A CZ    1 
ATOM   947  O  OH    . TYR A 1 112 ? 27.746  28.707  -7.524  1.00 98.34  ? 112 TYR A OH    1 
ATOM   948  N  N     . ASP A 1 113 ? 25.270  33.697  -4.464  1.00 78.75  ? 113 ASP A N     1 
ATOM   949  C  CA    . ASP A 1 113 ? 24.300  33.048  -3.591  1.00 59.91  ? 113 ASP A CA    1 
ATOM   950  C  C     . ASP A 1 113 ? 24.274  33.640  -2.188  1.00 59.59  ? 113 ASP A C     1 
ATOM   951  O  O     . ASP A 1 113 ? 23.615  33.081  -1.303  1.00 69.33  ? 113 ASP A O     1 
ATOM   952  C  CB    . ASP A 1 113 ? 24.582  31.544  -3.518  1.00 62.69  ? 113 ASP A CB    1 
ATOM   953  C  CG    . ASP A 1 113 ? 26.004  31.237  -3.081  1.00 87.58  ? 113 ASP A CG    1 
ATOM   954  O  OD1   . ASP A 1 113 ? 26.806  32.185  -2.928  1.00 81.03  ? 113 ASP A OD1   1 
ATOM   955  O  OD2   . ASP A 1 113 ? 26.321  30.045  -2.890  1.00 114.38 ? 113 ASP A OD2   1 
ATOM   956  N  N     . THR A 1 114 ? 24.969  34.746  -1.956  1.00 70.97  ? 114 THR A N     1 
ATOM   957  C  CA    . THR A 1 114 ? 24.970  35.367  -0.638  1.00 60.46  ? 114 THR A CA    1 
ATOM   958  C  C     . THR A 1 114 ? 23.659  36.113  -0.424  1.00 65.47  ? 114 THR A C     1 
ATOM   959  O  O     . THR A 1 114 ? 23.327  36.999  -1.220  1.00 64.51  ? 114 THR A O     1 
ATOM   960  C  CB    . THR A 1 114 ? 26.147  36.322  -0.493  1.00 57.97  ? 114 THR A CB    1 
ATOM   961  O  OG1   . THR A 1 114 ? 27.342  35.682  -0.959  1.00 64.20  ? 114 THR A OG1   1 
ATOM   962  C  CG2   . THR A 1 114 ? 26.326  36.719  0.965   1.00 44.33  ? 114 THR A CG2   1 
ATOM   963  N  N     . PRO A 1 115 ? 22.890  35.790  0.617   1.00 64.64  ? 115 PRO A N     1 
ATOM   964  C  CA    . PRO A 1 115 ? 21.591  36.447  0.810   1.00 52.19  ? 115 PRO A CA    1 
ATOM   965  C  C     . PRO A 1 115 ? 21.730  37.950  1.008   1.00 49.12  ? 115 PRO A C     1 
ATOM   966  O  O     . PRO A 1 115 ? 22.686  38.432  1.618   1.00 55.49  ? 115 PRO A O     1 
ATOM   967  C  CB    . PRO A 1 115 ? 21.032  35.762  2.063   1.00 37.72  ? 115 PRO A CB    1 
ATOM   968  C  CG    . PRO A 1 115 ? 21.729  34.446  2.114   1.00 56.06  ? 115 PRO A CG    1 
ATOM   969  C  CD    . PRO A 1 115 ? 23.111  34.708  1.590   1.00 58.49  ? 115 PRO A CD    1 
ATOM   970  N  N     . PHE A 1 116 ? 20.741  38.680  0.486   1.00 53.53  ? 116 PHE A N     1 
ATOM   971  C  CA    . PHE A 1 116 ? 20.767  40.140  0.466   1.00 48.16  ? 116 PHE A CA    1 
ATOM   972  C  C     . PHE A 1 116 ? 21.014  40.725  1.851   1.00 52.25  ? 116 PHE A C     1 
ATOM   973  O  O     . PHE A 1 116 ? 21.991  41.450  2.071   1.00 59.03  ? 116 PHE A O     1 
ATOM   974  C  CB    . PHE A 1 116 ? 19.447  40.658  -0.109  1.00 52.32  ? 116 PHE A CB    1 
ATOM   975  C  CG    . PHE A 1 116 ? 19.512  42.067  -0.621  1.00 61.77  ? 116 PHE A CG    1 
ATOM   976  C  CD1   . PHE A 1 116 ? 20.413  42.424  -1.612  1.00 62.30  ? 116 PHE A CD1   1 
ATOM   977  C  CD2   . PHE A 1 116 ? 18.657  43.035  -0.119  1.00 53.25  ? 116 PHE A CD2   1 
ATOM   978  C  CE1   . PHE A 1 116 ? 20.463  43.724  -2.087  1.00 54.63  ? 116 PHE A CE1   1 
ATOM   979  C  CE2   . PHE A 1 116 ? 18.703  44.333  -0.587  1.00 59.01  ? 116 PHE A CE2   1 
ATOM   980  C  CZ    . PHE A 1 116 ? 19.607  44.679  -1.572  1.00 60.49  ? 116 PHE A CZ    1 
ATOM   981  N  N     . ALA A 1 117 ? 20.125  40.420  2.801   1.00 54.43  ? 117 ALA A N     1 
ATOM   982  C  CA    . ALA A 1 117 ? 20.209  41.031  4.124   1.00 53.67  ? 117 ALA A CA    1 
ATOM   983  C  C     . ALA A 1 117 ? 21.533  40.724  4.810   1.00 50.25  ? 117 ALA A C     1 
ATOM   984  O  O     . ALA A 1 117 ? 22.020  41.535  5.606   1.00 53.18  ? 117 ALA A O     1 
ATOM   985  C  CB    . ALA A 1 117 ? 19.045  40.561  4.993   1.00 45.89  ? 117 ALA A CB    1 
ATOM   986  N  N     . LYS A 1 118 ? 22.128  39.568  4.517   1.00 52.87  ? 118 LYS A N     1 
ATOM   987  C  CA    . LYS A 1 118 ? 23.401  39.209  5.129   1.00 52.28  ? 118 LYS A CA    1 
ATOM   988  C  C     . LYS A 1 118 ? 24.580  39.847  4.406   1.00 50.25  ? 118 LYS A C     1 
ATOM   989  O  O     . LYS A 1 118 ? 25.575  40.202  5.048   1.00 51.43  ? 118 LYS A O     1 
ATOM   990  C  CB    . LYS A 1 118 ? 23.555  37.689  5.164   1.00 55.11  ? 118 LYS A CB    1 
ATOM   991  C  CG    . LYS A 1 118 ? 22.548  36.999  6.068   1.00 43.71  ? 118 LYS A CG    1 
ATOM   992  C  CD    . LYS A 1 118 ? 23.006  35.606  6.459   1.00 54.40  ? 118 LYS A CD    1 
ATOM   993  C  CE    . LYS A 1 118 ? 21.871  34.819  7.090   1.00 60.88  ? 118 LYS A CE    1 
ATOM   994  N  NZ    . LYS A 1 118 ? 21.529  33.617  6.283   1.00 77.85  ? 118 LYS A NZ    1 
ATOM   995  N  N     . ARG A 1 119 ? 24.489  39.996  3.082   1.00 45.74  ? 119 ARG A N     1 
ATOM   996  C  CA    . ARG A 1 119 ? 25.511  40.738  2.353   1.00 57.55  ? 119 ARG A CA    1 
ATOM   997  C  C     . ARG A 1 119 ? 25.561  42.189  2.809   1.00 61.78  ? 119 ARG A C     1 
ATOM   998  O  O     . ARG A 1 119 ? 26.644  42.779  2.912   1.00 70.77  ? 119 ARG A O     1 
ATOM   999  C  CB    . ARG A 1 119 ? 25.254  40.662  0.849   1.00 52.31  ? 119 ARG A CB    1 
ATOM   1000 C  CG    . ARG A 1 119 ? 26.257  41.463  0.034   1.00 56.75  ? 119 ARG A CG    1 
ATOM   1001 C  CD    . ARG A 1 119 ? 26.597  40.783  -1.284  1.00 62.72  ? 119 ARG A CD    1 
ATOM   1002 N  NE    . ARG A 1 119 ? 27.527  39.667  -1.132  1.00 82.36  ? 119 ARG A NE    1 
ATOM   1003 C  CZ    . ARG A 1 119 ? 28.764  39.752  -0.655  1.00 66.44  ? 119 ARG A CZ    1 
ATOM   1004 N  NH1   . ARG A 1 119 ? 29.297  40.911  -0.302  1.00 70.37  ? 119 ARG A NH1   1 
ATOM   1005 N  NH2   . ARG A 1 119 ? 29.490  38.644  -0.540  1.00 62.48  ? 119 ARG A NH2   1 
ATOM   1006 N  N     . TYR A 1 120 ? 24.394  42.780  3.082   1.00 54.60  ? 120 TYR A N     1 
ATOM   1007 C  CA    . TYR A 1 120 ? 24.342  44.141  3.605   1.00 59.61  ? 120 TYR A CA    1 
ATOM   1008 C  C     . TYR A 1 120 ? 25.196  44.281  4.858   1.00 53.73  ? 120 TYR A C     1 
ATOM   1009 O  O     . TYR A 1 120 ? 26.035  45.182  4.955   1.00 61.17  ? 120 TYR A O     1 
ATOM   1010 C  CB    . TYR A 1 120 ? 22.892  44.535  3.898   1.00 46.31  ? 120 TYR A CB    1 
ATOM   1011 C  CG    . TYR A 1 120 ? 22.724  45.995  4.253   1.00 43.00  ? 120 TYR A CG    1 
ATOM   1012 C  CD1   . TYR A 1 120 ? 22.678  46.969  3.263   1.00 41.53  ? 120 TYR A CD1   1 
ATOM   1013 C  CD2   . TYR A 1 120 ? 22.622  46.403  5.577   1.00 39.25  ? 120 TYR A CD2   1 
ATOM   1014 C  CE1   . TYR A 1 120 ? 22.531  48.305  3.582   1.00 43.22  ? 120 TYR A CE1   1 
ATOM   1015 C  CE2   . TYR A 1 120 ? 22.475  47.739  5.905   1.00 42.29  ? 120 TYR A CE2   1 
ATOM   1016 C  CZ    . TYR A 1 120 ? 22.430  48.686  4.902   1.00 45.82  ? 120 TYR A CZ    1 
ATOM   1017 O  OH    . TYR A 1 120 ? 22.284  50.019  5.215   1.00 47.46  ? 120 TYR A OH    1 
ATOM   1018 N  N     . LEU A 1 121 ? 24.999  43.384  5.827   1.00 47.94  ? 121 LEU A N     1 
ATOM   1019 C  CA    . LEU A 1 121 ? 25.788  43.423  7.054   1.00 55.75  ? 121 LEU A CA    1 
ATOM   1020 C  C     . LEU A 1 121 ? 27.282  43.343  6.759   1.00 57.41  ? 121 LEU A C     1 
ATOM   1021 O  O     . LEU A 1 121 ? 28.088  44.020  7.407   1.00 58.26  ? 121 LEU A O     1 
ATOM   1022 C  CB    . LEU A 1 121 ? 25.364  42.282  7.977   1.00 46.86  ? 121 LEU A CB    1 
ATOM   1023 C  CG    . LEU A 1 121 ? 24.068  42.492  8.760   1.00 47.08  ? 121 LEU A CG    1 
ATOM   1024 C  CD1   . LEU A 1 121 ? 23.746  41.262  9.596   1.00 52.16  ? 121 LEU A CD1   1 
ATOM   1025 C  CD2   . LEU A 1 121 ? 24.166  43.731  9.636   1.00 47.96  ? 121 LEU A CD2   1 
ATOM   1026 N  N     . ILE A 1 122 ? 27.668  42.526  5.778   1.00 57.68  ? 122 ILE A N     1 
ATOM   1027 C  CA    . ILE A 1 122 ? 29.083  42.356  5.459   1.00 58.50  ? 122 ILE A CA    1 
ATOM   1028 C  C     . ILE A 1 122 ? 29.613  43.580  4.721   1.00 63.73  ? 122 ILE A C     1 
ATOM   1029 O  O     . ILE A 1 122 ? 30.577  44.219  5.157   1.00 70.23  ? 122 ILE A O     1 
ATOM   1030 C  CB    . ILE A 1 122 ? 29.301  41.070  4.644   1.00 53.34  ? 122 ILE A CB    1 
ATOM   1031 C  CG1   . ILE A 1 122 ? 29.126  39.841  5.535   1.00 49.48  ? 122 ILE A CG1   1 
ATOM   1032 C  CG2   . ILE A 1 122 ? 30.680  41.066  4.008   1.00 42.15  ? 122 ILE A CG2   1 
ATOM   1033 C  CD1   . ILE A 1 122 ? 29.232  38.533  4.791   1.00 48.32  ? 122 ILE A CD1   1 
ATOM   1034 N  N     . ASP A 1 123 ? 28.988  43.923  3.591   1.00 56.93  ? 123 ASP A N     1 
ATOM   1035 C  CA    . ASP A 1 123 ? 29.473  45.040  2.783   1.00 52.59  ? 123 ASP A CA    1 
ATOM   1036 C  C     . ASP A 1 123 ? 29.426  46.349  3.562   1.00 55.46  ? 123 ASP A C     1 
ATOM   1037 O  O     . ASP A 1 123 ? 30.399  47.111  3.575   1.00 69.23  ? 123 ASP A O     1 
ATOM   1038 C  CB    . ASP A 1 123 ? 28.660  45.151  1.493   1.00 49.13  ? 123 ASP A CB    1 
ATOM   1039 C  CG    . ASP A 1 123 ? 28.869  43.967  0.573   1.00 58.10  ? 123 ASP A CG    1 
ATOM   1040 O  OD1   . ASP A 1 123 ? 29.434  42.952  1.031   1.00 50.37  ? 123 ASP A OD1   1 
ATOM   1041 O  OD2   . ASP A 1 123 ? 28.467  44.053  -0.607  1.00 59.32  ? 123 ASP A OD2   1 
ATOM   1042 N  N     . LYS A 1 124 ? 28.301  46.626  4.223   1.00 64.37  ? 124 LYS A N     1 
ATOM   1043 C  CA    . LYS A 1 124 ? 28.176  47.841  5.021   1.00 56.66  ? 124 LYS A CA    1 
ATOM   1044 C  C     . LYS A 1 124 ? 28.997  47.795  6.305   1.00 63.52  ? 124 LYS A C     1 
ATOM   1045 O  O     . LYS A 1 124 ? 28.983  48.777  7.055   1.00 67.09  ? 124 LYS A O     1 
ATOM   1046 C  CB    . LYS A 1 124 ? 26.706  48.103  5.359   1.00 53.51  ? 124 LYS A CB    1 
ATOM   1047 C  CG    . LYS A 1 124 ? 26.197  49.478  4.960   1.00 69.80  ? 124 LYS A CG    1 
ATOM   1048 C  CD    . LYS A 1 124 ? 25.948  49.587  3.462   1.00 56.29  ? 124 LYS A CD    1 
ATOM   1049 C  CE    . LYS A 1 124 ? 25.575  51.014  3.078   1.00 68.21  ? 124 LYS A CE    1 
ATOM   1050 N  NZ    . LYS A 1 124 ? 24.969  51.101  1.718   1.00 80.40  ? 124 LYS A NZ    1 
ATOM   1051 N  N     . GLY A 1 125 ? 29.694  46.694  6.579   1.00 60.21  ? 125 GLY A N     1 
ATOM   1052 C  CA    . GLY A 1 125 ? 30.578  46.628  7.731   1.00 50.44  ? 125 GLY A CA    1 
ATOM   1053 C  C     . GLY A 1 125 ? 29.885  46.752  9.068   1.00 55.83  ? 125 GLY A C     1 
ATOM   1054 O  O     . GLY A 1 125 ? 30.467  47.294  10.013  1.00 60.87  ? 125 GLY A O     1 
ATOM   1055 N  N     . LEU A 1 126 ? 28.656  46.264  9.179   1.00 62.02  ? 126 LEU A N     1 
ATOM   1056 C  CA    . LEU A 1 126 ? 27.903  46.351  10.420  1.00 56.88  ? 126 LEU A CA    1 
ATOM   1057 C  C     . LEU A 1 126 ? 27.991  45.040  11.189  1.00 54.13  ? 126 LEU A C     1 
ATOM   1058 O  O     . LEU A 1 126 ? 28.106  43.959  10.605  1.00 50.27  ? 126 LEU A O     1 
ATOM   1059 C  CB    . LEU A 1 126 ? 26.440  46.706  10.148  1.00 62.82  ? 126 LEU A CB    1 
ATOM   1060 C  CG    . LEU A 1 126 ? 26.224  48.001  9.365   1.00 60.36  ? 126 LEU A CG    1 
ATOM   1061 C  CD1   . LEU A 1 126 ? 24.889  47.970  8.642   1.00 59.03  ? 126 LEU A CD1   1 
ATOM   1062 C  CD2   . LEU A 1 126 ? 26.313  49.203  10.291  1.00 60.22  ? 126 LEU A CD2   1 
ATOM   1063 N  N     . VAL A 1 127 ? 27.943  45.149  12.517  1.00 47.51  ? 127 VAL A N     1 
ATOM   1064 C  CA    . VAL A 1 127 ? 28.083  44.008  13.407  1.00 54.06  ? 127 VAL A CA    1 
ATOM   1065 C  C     . VAL A 1 127 ? 26.916  44.012  14.385  1.00 60.79  ? 127 VAL A C     1 
ATOM   1066 O  O     . VAL A 1 127 ? 26.788  44.941  15.189  1.00 61.60  ? 127 VAL A O     1 
ATOM   1067 C  CB    . VAL A 1 127 ? 29.417  44.023  14.174  1.00 59.54  ? 127 VAL A CB    1 
ATOM   1068 C  CG1   . VAL A 1 127 ? 29.511  42.816  15.095  1.00 54.20  ? 127 VAL A CG1   1 
ATOM   1069 C  CG2   . VAL A 1 127 ? 30.586  44.059  13.204  1.00 48.58  ? 127 VAL A CG2   1 
ATOM   1070 N  N     . PRO A 1 128 ? 26.043  43.011  14.364  1.00 65.19  ? 128 PRO A N     1 
ATOM   1071 C  CA    . PRO A 1 128 ? 24.934  42.986  15.319  1.00 67.33  ? 128 PRO A CA    1 
ATOM   1072 C  C     . PRO A 1 128 ? 25.414  42.622  16.715  1.00 61.40  ? 128 PRO A C     1 
ATOM   1073 O  O     . PRO A 1 128 ? 26.505  42.082  16.911  1.00 68.44  ? 128 PRO A O     1 
ATOM   1074 C  CB    . PRO A 1 128 ? 24.000  41.909  14.755  1.00 51.23  ? 128 PRO A CB    1 
ATOM   1075 C  CG    . PRO A 1 128 ? 24.889  41.023  13.969  1.00 59.75  ? 128 PRO A CG    1 
ATOM   1076 C  CD    . PRO A 1 128 ? 25.985  41.888  13.413  1.00 65.27  ? 128 PRO A CD    1 
ATOM   1077 N  N     . MET A 1 129 ? 24.572  42.954  17.693  1.00 69.07  ? 129 MET A N     1 
ATOM   1078 C  CA    . MET A 1 129 ? 24.725  42.558  19.089  1.00 62.18  ? 129 MET A CA    1 
ATOM   1079 C  C     . MET A 1 129 ? 25.905  43.225  19.783  1.00 67.93  ? 129 MET A C     1 
ATOM   1080 O  O     . MET A 1 129 ? 26.418  42.692  20.770  1.00 72.92  ? 129 MET A O     1 
ATOM   1081 C  CB    . MET A 1 129 ? 24.843  41.034  19.223  1.00 64.30  ? 129 MET A CB    1 
ATOM   1082 C  CG    . MET A 1 129 ? 23.582  40.290  18.841  1.00 65.09  ? 129 MET A CG    1 
ATOM   1083 S  SD    . MET A 1 129 ? 22.105  41.234  19.237  1.00 67.13  ? 129 MET A SD    1 
ATOM   1084 C  CE    . MET A 1 129 ? 21.814  40.670  20.908  1.00 42.32  ? 129 MET A CE    1 
ATOM   1085 N  N     . GLU A 1 130 ? 26.346  44.387  19.315  1.00 73.41  ? 130 GLU A N     1 
ATOM   1086 C  CA    . GLU A 1 130 ? 27.417  45.121  19.975  1.00 80.78  ? 130 GLU A CA    1 
ATOM   1087 C  C     . GLU A 1 130 ? 26.850  46.363  20.652  1.00 78.57  ? 130 GLU A C     1 
ATOM   1088 O  O     . GLU A 1 130 ? 25.924  46.999  20.137  1.00 88.22  ? 130 GLU A O     1 
ATOM   1089 C  CB    . GLU A 1 130 ? 28.530  45.493  18.985  1.00 81.38  ? 130 GLU A CB    1 
ATOM   1090 C  CG    . GLU A 1 130 ? 28.250  46.688  18.093  1.00 97.88  ? 130 GLU A CG    1 
ATOM   1091 C  CD    . GLU A 1 130 ? 29.314  46.870  17.026  1.00 114.41 ? 130 GLU A CD    1 
ATOM   1092 O  OE1   . GLU A 1 130 ? 30.261  46.055  16.983  1.00 79.31  ? 130 GLU A OE1   1 
ATOM   1093 O  OE2   . GLU A 1 130 ? 29.205  47.829  16.232  1.00 131.43 ? 130 GLU A OE2   1 
ATOM   1094 N  N     . GLY A 1 131 ? 27.395  46.687  21.816  1.00 85.91  ? 131 GLY A N     1 
ATOM   1095 C  CA    . GLY A 1 131 ? 26.915  47.779  22.637  1.00 84.29  ? 131 GLY A CA    1 
ATOM   1096 C  C     . GLY A 1 131 ? 26.543  47.305  24.028  1.00 87.62  ? 131 GLY A C     1 
ATOM   1097 O  O     . GLY A 1 131 ? 26.695  46.137  24.382  1.00 82.89  ? 131 GLY A O     1 
ATOM   1098 N  N     . ASP A 1 132 ? 26.043  48.251  24.823  1.00 92.72  ? 132 ASP A N     1 
ATOM   1099 C  CA    . ASP A 1 132 ? 25.646  47.981  26.200  1.00 94.53  ? 132 ASP A CA    1 
ATOM   1100 C  C     . ASP A 1 132 ? 24.134  47.933  26.376  1.00 93.83  ? 132 ASP A C     1 
ATOM   1101 O  O     . ASP A 1 132 ? 23.650  47.993  27.511  1.00 96.97  ? 132 ASP A O     1 
ATOM   1102 C  CB    . ASP A 1 132 ? 26.243  49.032  27.138  1.00 92.96  ? 132 ASP A CB    1 
ATOM   1103 C  CG    . ASP A 1 132 ? 27.699  49.317  26.840  1.00 119.08 ? 132 ASP A CG    1 
ATOM   1104 O  OD1   . ASP A 1 132 ? 28.003  49.720  25.697  1.00 124.28 ? 132 ASP A OD1   1 
ATOM   1105 O  OD2   . ASP A 1 132 ? 28.539  49.141  27.748  1.00 117.73 ? 132 ASP A OD2   1 
ATOM   1106 N  N     . GLU A 1 133 ? 23.378  47.827  25.286  1.00 86.43  ? 133 GLU A N     1 
ATOM   1107 C  CA    . GLU A 1 133 ? 21.925  47.863  25.375  1.00 81.35  ? 133 GLU A CA    1 
ATOM   1108 C  C     . GLU A 1 133 ? 21.396  46.612  26.063  1.00 76.47  ? 133 GLU A C     1 
ATOM   1109 O  O     . GLU A 1 133 ? 21.744  45.487  25.690  1.00 86.18  ? 133 GLU A O     1 
ATOM   1110 C  CB    . GLU A 1 133 ? 21.312  47.997  23.983  1.00 82.21  ? 133 GLU A CB    1 
ATOM   1111 C  CG    . GLU A 1 133 ? 20.989  49.428  23.594  1.00 89.55  ? 133 GLU A CG    1 
ATOM   1112 C  CD    . GLU A 1 133 ? 19.633  49.875  24.103  1.00 94.88  ? 133 GLU A CD    1 
ATOM   1113 O  OE1   . GLU A 1 133 ? 18.944  49.064  24.757  1.00 98.11  ? 133 GLU A OE1   1 
ATOM   1114 O  OE2   . GLU A 1 133 ? 19.257  51.037  23.850  1.00 96.91  ? 133 GLU A OE2   1 
ATOM   1115 N  N     . GLU A 1 134 ? 20.553  46.811  27.073  1.00 77.74  ? 134 GLU A N     1 
ATOM   1116 C  CA    . GLU A 1 134 ? 19.914  45.712  27.788  1.00 85.61  ? 134 GLU A CA    1 
ATOM   1117 C  C     . GLU A 1 134 ? 18.613  45.366  27.074  1.00 84.78  ? 134 GLU A C     1 
ATOM   1118 O  O     . GLU A 1 134 ? 17.684  46.179  27.030  1.00 89.07  ? 134 GLU A O     1 
ATOM   1119 C  CB    . GLU A 1 134 ? 19.666  46.087  29.246  1.00 91.70  ? 134 GLU A CB    1 
ATOM   1120 C  CG    . GLU A 1 134 ? 20.897  45.965  30.130  1.00 115.08 ? 134 GLU A CG    1 
ATOM   1121 C  CD    . GLU A 1 134 ? 20.720  46.641  31.475  1.00 146.20 ? 134 GLU A CD    1 
ATOM   1122 O  OE1   . GLU A 1 134 ? 19.564  46.926  31.854  1.00 134.21 ? 134 GLU A OE1   1 
ATOM   1123 O  OE2   . GLU A 1 134 ? 21.739  46.887  32.155  1.00 146.64 ? 134 GLU A OE2   1 
ATOM   1124 N  N     . LEU A 1 135 ? 18.549  44.163  26.512  1.00 79.30  ? 135 LEU A N     1 
ATOM   1125 C  CA    . LEU A 1 135 ? 17.380  43.739  25.758  1.00 77.18  ? 135 LEU A CA    1 
ATOM   1126 C  C     . LEU A 1 135 ? 16.309  43.195  26.692  1.00 78.96  ? 135 LEU A C     1 
ATOM   1127 O  O     . LEU A 1 135 ? 16.606  42.483  27.656  1.00 81.74  ? 135 LEU A O     1 
ATOM   1128 C  CB    . LEU A 1 135 ? 17.767  42.671  24.735  1.00 73.60  ? 135 LEU A CB    1 
ATOM   1129 C  CG    . LEU A 1 135 ? 18.886  43.030  23.758  1.00 62.49  ? 135 LEU A CG    1 
ATOM   1130 C  CD1   . LEU A 1 135 ? 19.052  41.925  22.736  1.00 63.48  ? 135 LEU A CD1   1 
ATOM   1131 C  CD2   . LEU A 1 135 ? 18.606  44.357  23.073  1.00 75.37  ? 135 LEU A CD2   1 
ATOM   1132 N  N     . LYS A 1 136 ? 15.055  43.532  26.400  1.00 70.21  ? 136 LYS A N     1 
ATOM   1133 C  CA    . LYS A 1 136 ? 13.929  43.009  27.163  1.00 81.20  ? 136 LYS A CA    1 
ATOM   1134 C  C     . LYS A 1 136 ? 13.563  41.630  26.632  1.00 76.43  ? 136 LYS A C     1 
ATOM   1135 O  O     . LYS A 1 136 ? 13.272  41.472  25.441  1.00 81.01  ? 136 LYS A O     1 
ATOM   1136 C  CB    . LYS A 1 136 ? 12.735  43.957  27.082  1.00 74.01  ? 136 LYS A CB    1 
ATOM   1137 C  CG    . LYS A 1 136 ? 12.762  45.068  28.119  1.00 81.49  ? 136 LYS A CG    1 
ATOM   1138 C  CD    . LYS A 1 136 ? 11.362  45.543  28.466  1.00 105.02 ? 136 LYS A CD    1 
ATOM   1139 C  CE    . LYS A 1 136 ? 10.488  44.388  28.927  1.00 100.67 ? 136 LYS A CE    1 
ATOM   1140 N  NZ    . LYS A 1 136 ? 9.064   44.587  28.543  1.00 96.40  ? 136 LYS A NZ    1 
ATOM   1141 N  N     . MET A 1 137 ? 13.577  40.635  27.512  1.00 69.63  ? 137 MET A N     1 
ATOM   1142 C  CA    . MET A 1 137 ? 13.347  39.251  27.136  1.00 67.31  ? 137 MET A CA    1 
ATOM   1143 C  C     . MET A 1 137 ? 12.038  38.759  27.733  1.00 64.77  ? 137 MET A C     1 
ATOM   1144 O  O     . MET A 1 137 ? 11.579  39.258  28.764  1.00 76.73  ? 137 MET A O     1 
ATOM   1145 C  CB    . MET A 1 137 ? 14.492  38.358  27.609  1.00 61.61  ? 137 MET A CB    1 
ATOM   1146 C  CG    . MET A 1 137 ? 15.849  39.005  27.480  1.00 75.37  ? 137 MET A CG    1 
ATOM   1147 S  SD    . MET A 1 137 ? 17.141  37.878  26.940  1.00 83.44  ? 137 MET A SD    1 
ATOM   1148 C  CE    . MET A 1 137 ? 18.572  38.823  27.450  1.00 93.37  ? 137 MET A CE    1 
ATOM   1149 N  N     . LEU A 1 138 ? 11.447  37.764  27.080  1.00 63.45  ? 138 LEU A N     1 
ATOM   1150 C  CA    . LEU A 1 138 ? 10.206  37.167  27.549  1.00 71.29  ? 138 LEU A CA    1 
ATOM   1151 C  C     . LEU A 1 138 ? 10.143  35.737  27.041  1.00 68.11  ? 138 LEU A C     1 
ATOM   1152 O  O     . LEU A 1 138 ? 10.260  35.501  25.835  1.00 68.94  ? 138 LEU A O     1 
ATOM   1153 C  CB    . LEU A 1 138 ? 8.988   37.968  27.070  1.00 64.53  ? 138 LEU A CB    1 
ATOM   1154 C  CG    . LEU A 1 138 ? 7.613   37.321  27.243  1.00 68.59  ? 138 LEU A CG    1 
ATOM   1155 C  CD1   . LEU A 1 138 ? 7.226   37.281  28.711  1.00 72.09  ? 138 LEU A CD1   1 
ATOM   1156 C  CD2   . LEU A 1 138 ? 6.567   38.072  26.435  1.00 76.88  ? 138 LEU A CD2   1 
ATOM   1157 N  N     . ALA A 1 139 ? 9.983   34.791  27.958  1.00 64.00  ? 139 ALA A N     1 
ATOM   1158 C  CA    . ALA A 1 139 ? 9.830   33.388  27.613  1.00 63.83  ? 139 ALA A CA    1 
ATOM   1159 C  C     . ALA A 1 139 ? 8.355   33.012  27.612  1.00 76.06  ? 139 ALA A C     1 
ATOM   1160 O  O     . ALA A 1 139 ? 7.528   33.658  28.258  1.00 69.30  ? 139 ALA A O     1 
ATOM   1161 C  CB    . ALA A 1 139 ? 10.597  32.499  28.595  1.00 72.78  ? 139 ALA A CB    1 
ATOM   1162 N  N     . PHE A 1 140 ? 8.028   31.958  26.868  1.00 64.57  ? 140 PHE A N     1 
ATOM   1163 C  CA    . PHE A 1 140 ? 6.670   31.439  26.896  1.00 74.77  ? 140 PHE A CA    1 
ATOM   1164 C  C     . PHE A 1 140 ? 6.675   29.957  26.553  1.00 75.00  ? 140 PHE A C     1 
ATOM   1165 O  O     . PHE A 1 140 ? 7.545   29.470  25.826  1.00 68.45  ? 140 PHE A O     1 
ATOM   1166 C  CB    . PHE A 1 140 ? 5.735   32.224  25.958  1.00 79.05  ? 140 PHE A CB    1 
ATOM   1167 C  CG    . PHE A 1 140 ? 5.892   31.893  24.498  1.00 71.78  ? 140 PHE A CG    1 
ATOM   1168 C  CD1   . PHE A 1 140 ? 6.832   32.551  23.723  1.00 64.35  ? 140 PHE A CD1   1 
ATOM   1169 C  CD2   . PHE A 1 140 ? 5.075   30.950  23.893  1.00 70.16  ? 140 PHE A CD2   1 
ATOM   1170 C  CE1   . PHE A 1 140 ? 6.968   32.261  22.377  1.00 68.91  ? 140 PHE A CE1   1 
ATOM   1171 C  CE2   . PHE A 1 140 ? 5.209   30.652  22.550  1.00 67.13  ? 140 PHE A CE2   1 
ATOM   1172 C  CZ    . PHE A 1 140 ? 6.157   31.308  21.791  1.00 70.90  ? 140 PHE A CZ    1 
ATOM   1173 N  N     . ALA A 1 141 ? 5.698   29.246  27.112  1.00 72.89  ? 141 ALA A N     1 
ATOM   1174 C  CA    . ALA A 1 141 ? 5.481   27.836  26.831  1.00 78.67  ? 141 ALA A CA    1 
ATOM   1175 C  C     . ALA A 1 141 ? 3.982   27.580  26.856  1.00 77.25  ? 141 ALA A C     1 
ATOM   1176 O  O     . ALA A 1 141 ? 3.207   28.388  27.375  1.00 84.44  ? 141 ALA A O     1 
ATOM   1177 C  CB    . ALA A 1 141 ? 6.208   26.936  27.837  1.00 81.42  ? 141 ALA A CB    1 
ATOM   1178 N  N     . ILE A 1 142 ? 3.574   26.448  26.285  1.00 70.79  ? 142 ILE A N     1 
ATOM   1179 C  CA    . ILE A 1 142 ? 2.162   26.124  26.145  1.00 83.09  ? 142 ILE A CA    1 
ATOM   1180 C  C     . ILE A 1 142 ? 1.907   24.714  26.666  1.00 89.23  ? 142 ILE A C     1 
ATOM   1181 O  O     . ILE A 1 142 ? 2.828   23.933  26.903  1.00 83.52  ? 142 ILE A O     1 
ATOM   1182 C  CB    . ILE A 1 142 ? 1.672   26.255  24.687  1.00 82.10  ? 142 ILE A CB    1 
ATOM   1183 C  CG1   . ILE A 1 142 ? 2.391   25.251  23.784  1.00 75.44  ? 142 ILE A CG1   1 
ATOM   1184 C  CG2   . ILE A 1 142 ? 1.868   27.676  24.179  1.00 74.29  ? 142 ILE A CG2   1 
ATOM   1185 C  CD1   . ILE A 1 142 ? 1.755   25.096  22.420  1.00 79.16  ? 142 ILE A CD1   1 
ATOM   1186 N  N     . ALA A 1 143 ? 0.623   24.408  26.850  1.00 80.18  ? 143 ALA A N     1 
ATOM   1187 C  CA    . ALA A 1 143 ? 0.155   23.080  27.221  1.00 76.44  ? 143 ALA A CA    1 
ATOM   1188 C  C     . ALA A 1 143 ? -1.029  22.728  26.333  1.00 86.53  ? 143 ALA A C     1 
ATOM   1189 O  O     . ALA A 1 143 ? -1.874  23.583  26.052  1.00 83.43  ? 143 ALA A O     1 
ATOM   1190 C  CB    . ALA A 1 143 ? -0.242  23.014  28.700  1.00 85.81  ? 143 ALA A CB    1 
ATOM   1191 N  N     . THR A 1 144 ? -1.091  21.470  25.897  1.00 91.98  ? 144 THR A N     1 
ATOM   1192 C  CA    . THR A 1 144 ? -1.953  21.075  24.792  1.00 93.43  ? 144 THR A CA    1 
ATOM   1193 C  C     . THR A 1 144 ? -2.756  19.829  25.145  1.00 94.77  ? 144 THR A C     1 
ATOM   1194 O  O     . THR A 1 144 ? -2.305  18.978  25.917  1.00 96.74  ? 144 THR A O     1 
ATOM   1195 C  CB    . THR A 1 144 ? -1.125  20.805  23.527  1.00 88.59  ? 144 THR A CB    1 
ATOM   1196 O  OG1   . THR A 1 144 ? -0.161  19.779  23.799  1.00 84.78  ? 144 THR A OG1   1 
ATOM   1197 C  CG2   . THR A 1 144 ? -0.379  22.058  23.113  1.00 84.60  ? 144 THR A CG2   1 
ATOM   1198 N  N     . LEU A 1 145 ? -3.954  19.728  24.567  1.00 94.08  ? 145 LEU A N     1 
ATOM   1199 C  CA    . LEU A 1 145 ? -4.781  18.532  24.700  1.00 106.75 ? 145 LEU A CA    1 
ATOM   1200 C  C     . LEU A 1 145 ? -4.334  17.519  23.655  1.00 110.16 ? 145 LEU A C     1 
ATOM   1201 O  O     . LEU A 1 145 ? -4.568  17.706  22.456  1.00 119.84 ? 145 LEU A O     1 
ATOM   1202 C  CB    . LEU A 1 145 ? -6.262  18.865  24.536  1.00 91.09  ? 145 LEU A CB    1 
ATOM   1203 C  CG    . LEU A 1 145 ? -7.212  17.675  24.347  1.00 97.56  ? 145 LEU A CG    1 
ATOM   1204 C  CD1   . LEU A 1 145 ? -7.089  16.697  25.502  1.00 100.94 ? 145 LEU A CD1   1 
ATOM   1205 C  CD2   . LEU A 1 145 ? -8.655  18.129  24.197  1.00 85.78  ? 145 LEU A CD2   1 
ATOM   1206 N  N     . TYR A 1 146 ? -3.689  16.448  24.103  1.00 107.56 ? 146 TYR A N     1 
ATOM   1207 C  CA    . TYR A 1 146 ? -3.177  15.417  23.216  1.00 105.09 ? 146 TYR A CA    1 
ATOM   1208 C  C     . TYR A 1 146 ? -3.958  14.124  23.398  1.00 110.00 ? 146 TYR A C     1 
ATOM   1209 O  O     . TYR A 1 146 ? -4.309  13.748  24.520  1.00 112.68 ? 146 TYR A O     1 
ATOM   1210 C  CB    . TYR A 1 146 ? -1.691  15.149  23.473  1.00 100.54 ? 146 TYR A CB    1 
ATOM   1211 C  CG    . TYR A 1 146 ? -1.096  14.118  22.538  1.00 111.94 ? 146 TYR A CG    1 
ATOM   1212 C  CD1   . TYR A 1 146 ? -0.533  12.946  23.029  1.00 110.37 ? 146 TYR A CD1   1 
ATOM   1213 C  CD2   . TYR A 1 146 ? -1.103  14.313  21.163  1.00 110.13 ? 146 TYR A CD2   1 
ATOM   1214 C  CE1   . TYR A 1 146 ? 0.009   11.999  22.176  1.00 112.23 ? 146 TYR A CE1   1 
ATOM   1215 C  CE2   . TYR A 1 146 ? -0.563  13.373  20.303  1.00 111.10 ? 146 TYR A CE2   1 
ATOM   1216 C  CZ    . TYR A 1 146 ? -0.009  12.218  20.815  1.00 111.80 ? 146 TYR A CZ    1 
ATOM   1217 O  OH    . TYR A 1 146 ? 0.528   11.281  19.962  1.00 123.84 ? 146 TYR A OH    1 
ATOM   1218 N  N     . HIS A 1 147 ? -4.237  13.456  22.285  1.00 108.98 ? 147 HIS A N     1 
ATOM   1219 C  CA    . HIS A 1 147 ? -4.656  12.065  22.290  1.00 117.54 ? 147 HIS A CA    1 
ATOM   1220 C  C     . HIS A 1 147 ? -3.838  11.341  21.236  1.00 120.62 ? 147 HIS A C     1 
ATOM   1221 O  O     . HIS A 1 147 ? -3.459  11.929  20.219  1.00 123.60 ? 147 HIS A O     1 
ATOM   1222 C  CB    . HIS A 1 147 ? -6.139  11.888  21.956  1.00 120.24 ? 147 HIS A CB    1 
ATOM   1223 C  CG    . HIS A 1 147 ? -7.078  12.476  22.962  1.00 118.03 ? 147 HIS A CG    1 
ATOM   1224 N  ND1   . HIS A 1 147 ? -7.931  13.511  22.648  1.00 108.89 ? 147 HIS A ND1   1 
ATOM   1225 C  CD2   . HIS A 1 147 ? -7.339  12.150  24.250  1.00 120.38 ? 147 HIS A CD2   1 
ATOM   1226 C  CE1   . HIS A 1 147 ? -8.657  13.818  23.707  1.00 108.33 ? 147 HIS A CE1   1 
ATOM   1227 N  NE2   . HIS A 1 147 ? -8.320  13.005  24.691  1.00 107.92 ? 147 HIS A NE2   1 
ATOM   1228 N  N     . GLU A 1 148 ? -3.563  10.066  21.485  1.00 133.25 ? 148 GLU A N     1 
ATOM   1229 C  CA    . GLU A 1 148 ? -2.858  9.266   20.496  1.00 140.06 ? 148 GLU A CA    1 
ATOM   1230 C  C     . GLU A 1 148 ? -3.684  9.158   19.221  1.00 147.50 ? 148 GLU A C     1 
ATOM   1231 O  O     . GLU A 1 148 ? -4.861  8.789   19.256  1.00 134.63 ? 148 GLU A O     1 
ATOM   1232 C  CB    . GLU A 1 148 ? -2.557  7.876   21.050  1.00 138.36 ? 148 GLU A CB    1 
ATOM   1233 C  CG    . GLU A 1 148 ? -1.558  7.094   20.219  1.00 141.71 ? 148 GLU A CG    1 
ATOM   1234 C  CD    . GLU A 1 148 ? -0.371  6.619   21.031  1.00 152.45 ? 148 GLU A CD    1 
ATOM   1235 O  OE1   . GLU A 1 148 ? -0.556  6.287   22.221  1.00 152.56 ? 148 GLU A OE1   1 
ATOM   1236 O  OE2   . GLU A 1 148 ? 0.748   6.573   20.477  1.00 142.89 ? 148 GLU A OE2   1 
ATOM   1237 N  N     . GLY A 1 149 ? -3.070  9.501   18.092  1.00 155.14 ? 149 GLY A N     1 
ATOM   1238 C  CA    . GLY A 1 149 ? -3.734  9.338   16.816  1.00 146.77 ? 149 GLY A CA    1 
ATOM   1239 C  C     . GLY A 1 149 ? -4.133  10.631  16.138  1.00 143.42 ? 149 GLY A C     1 
ATOM   1240 O  O     . GLY A 1 149 ? -3.829  10.818  14.956  1.00 147.71 ? 149 GLY A O     1 
ATOM   1241 N  N     . GLU A 1 150 ? -4.820  11.523  16.854  1.00 139.36 ? 150 GLU A N     1 
ATOM   1242 C  CA    . GLU A 1 150 ? -5.293  12.747  16.222  1.00 127.76 ? 150 GLU A CA    1 
ATOM   1243 C  C     . GLU A 1 150 ? -4.133  13.566  15.676  1.00 134.09 ? 150 GLU A C     1 
ATOM   1244 O  O     . GLU A 1 150 ? -3.096  13.722  16.326  1.00 124.58 ? 150 GLU A O     1 
ATOM   1245 C  CB    . GLU A 1 150 ? -6.126  13.600  17.183  1.00 116.70 ? 150 GLU A CB    1 
ATOM   1246 C  CG    . GLU A 1 150 ? -5.822  13.513  18.665  1.00 125.34 ? 150 GLU A CG    1 
ATOM   1247 C  CD    . GLU A 1 150 ? -6.866  14.256  19.480  1.00 132.78 ? 150 GLU A CD    1 
ATOM   1248 O  OE1   . GLU A 1 150 ? -6.813  15.509  19.492  1.00 126.71 ? 150 GLU A OE1   1 
ATOM   1249 O  OE2   . GLU A 1 150 ? -7.779  13.597  20.032  1.00 134.05 ? 150 GLU A OE2   1 
ATOM   1250 N  N     . GLU A 1 151 ? -4.331  14.096  14.467  1.00 129.36 ? 151 GLU A N     1 
ATOM   1251 C  CA    . GLU A 1 151 ? -3.316  14.839  13.731  1.00 119.60 ? 151 GLU A CA    1 
ATOM   1252 C  C     . GLU A 1 151 ? -2.757  16.004  14.539  1.00 115.91 ? 151 GLU A C     1 
ATOM   1253 O  O     . GLU A 1 151 ? -3.311  16.368  15.582  1.00 116.24 ? 151 GLU A O     1 
ATOM   1254 C  CB    . GLU A 1 151 ? -3.902  15.350  12.414  1.00 119.87 ? 151 GLU A CB    1 
ATOM   1255 C  CG    . GLU A 1 151 ? -5.011  16.375  12.604  1.00 128.88 ? 151 GLU A CG    1 
ATOM   1256 C  CD    . GLU A 1 151 ? -5.774  16.659  11.326  1.00 137.70 ? 151 GLU A CD    1 
ATOM   1257 O  OE1   . GLU A 1 151 ? -6.213  17.813  11.138  1.00 133.38 ? 151 GLU A OE1   1 
ATOM   1258 O  OE2   . GLU A 1 151 ? -5.937  15.727  10.511  1.00 151.04 ? 151 GLU A OE2   1 
ATOM   1259 N  N     . PHE A 1 152 ? -1.660  16.590  14.065  1.00 103.00 ? 152 PHE A N     1 
ATOM   1260 C  CA    . PHE A 1 152 ? -1.053  17.712  14.768  1.00 94.57  ? 152 PHE A CA    1 
ATOM   1261 C  C     . PHE A 1 152 ? -2.063  18.838  14.941  1.00 97.08  ? 152 PHE A C     1 
ATOM   1262 O  O     . PHE A 1 152 ? -2.755  19.221  13.993  1.00 103.75 ? 152 PHE A O     1 
ATOM   1263 C  CB    . PHE A 1 152 ? 0.175   18.221  14.014  1.00 109.99 ? 152 PHE A CB    1 
ATOM   1264 C  CG    . PHE A 1 152 ? 0.833   19.405  14.665  1.00 96.48  ? 152 PHE A CG    1 
ATOM   1265 C  CD1   . PHE A 1 152 ? 1.694   19.234  15.737  1.00 91.27  ? 152 PHE A CD1   1 
ATOM   1266 C  CD2   . PHE A 1 152 ? 0.579   20.691  14.214  1.00 101.16 ? 152 PHE A CD2   1 
ATOM   1267 C  CE1   . PHE A 1 152 ? 2.296   20.323  16.342  1.00 80.98  ? 152 PHE A CE1   1 
ATOM   1268 C  CE2   . PHE A 1 152 ? 1.176   21.783  14.816  1.00 97.89  ? 152 PHE A CE2   1 
ATOM   1269 C  CZ    . PHE A 1 152 ? 2.036   21.598  15.881  1.00 88.48  ? 152 PHE A CZ    1 
ATOM   1270 N  N     . ALA A 1 153 ? -2.155  19.348  16.168  1.00 88.22  ? 153 ALA A N     1 
ATOM   1271 C  CA    . ALA A 1 153 ? -3.042  20.450  16.532  1.00 98.24  ? 153 ALA A CA    1 
ATOM   1272 C  C     . ALA A 1 153 ? -4.510  20.133  16.278  1.00 95.95  ? 153 ALA A C     1 
ATOM   1273 O  O     . ALA A 1 153 ? -5.322  21.048  16.098  1.00 98.35  ? 153 ALA A O     1 
ATOM   1274 C  CB    . ALA A 1 153 ? -2.644  21.742  15.816  1.00 86.98  ? 153 ALA A CB    1 
ATOM   1275 N  N     . GLU A 1 154 ? -4.870  18.848  16.260  1.00 100.91 ? 154 GLU A N     1 
ATOM   1276 C  CA    . GLU A 1 154 ? -6.281  18.481  16.215  1.00 106.06 ? 154 GLU A CA    1 
ATOM   1277 C  C     . GLU A 1 154 ? -7.013  19.002  17.445  1.00 99.08  ? 154 GLU A C     1 
ATOM   1278 O  O     . GLU A 1 154 ? -8.175  19.416  17.361  1.00 99.76  ? 154 GLU A O     1 
ATOM   1279 C  CB    . GLU A 1 154 ? -6.423  16.964  16.109  1.00 112.05 ? 154 GLU A CB    1 
ATOM   1280 C  CG    . GLU A 1 154 ? -7.838  16.448  16.305  1.00 121.29 ? 154 GLU A CG    1 
ATOM   1281 C  CD    . GLU A 1 154 ? -8.676  16.551  15.050  1.00 135.71 ? 154 GLU A CD    1 
ATOM   1282 O  OE1   . GLU A 1 154 ? -9.246  17.634  14.800  1.00 136.16 ? 154 GLU A OE1   1 
ATOM   1283 O  OE2   . GLU A 1 154 ? -8.762  15.546  14.314  1.00 131.28 ? 154 GLU A OE2   1 
ATOM   1284 N  N     . GLY A 1 155 ? -6.341  18.999  18.594  1.00 101.58 ? 155 GLY A N     1 
ATOM   1285 C  CA    . GLY A 1 155 ? -6.910  19.501  19.821  1.00 95.89  ? 155 GLY A CA    1 
ATOM   1286 C  C     . GLY A 1 155 ? -6.495  20.930  20.108  1.00 94.28  ? 155 GLY A C     1 
ATOM   1287 O  O     . GLY A 1 155 ? -5.781  21.566  19.326  1.00 96.01  ? 155 GLY A O     1 
ATOM   1288 N  N     . PRO A 1 156 ? -6.943  21.462  21.245  1.00 92.48  ? 156 PRO A N     1 
ATOM   1289 C  CA    . PRO A 1 156 ? -6.676  22.870  21.563  1.00 94.93  ? 156 PRO A CA    1 
ATOM   1290 C  C     . PRO A 1 156 ? -5.469  23.095  22.467  1.00 89.21  ? 156 PRO A C     1 
ATOM   1291 O  O     . PRO A 1 156 ? -4.964  22.159  23.094  1.00 95.31  ? 156 PRO A O     1 
ATOM   1292 C  CB    . PRO A 1 156 ? -7.971  23.301  22.260  1.00 100.48 ? 156 PRO A CB    1 
ATOM   1293 C  CG    . PRO A 1 156 ? -8.419  22.061  22.969  1.00 87.77  ? 156 PRO A CG    1 
ATOM   1294 C  CD    . PRO A 1 156 ? -7.974  20.886  22.124  1.00 96.45  ? 156 PRO A CD    1 
ATOM   1295 N  N     . ILE A 1 157 ? -5.003  24.342  22.527  1.00 90.07  ? 157 ILE A N     1 
ATOM   1296 C  CA    . ILE A 1 157 ? -3.994  24.767  23.496  1.00 85.35  ? 157 ILE A CA    1 
ATOM   1297 C  C     . ILE A 1 157 ? -4.708  24.984  24.823  1.00 87.68  ? 157 ILE A C     1 
ATOM   1298 O  O     . ILE A 1 157 ? -5.466  25.944  24.971  1.00 105.17 ? 157 ILE A O     1 
ATOM   1299 C  CB    . ILE A 1 157 ? -3.285  26.052  23.053  1.00 91.10  ? 157 ILE A CB    1 
ATOM   1300 C  CG1   . ILE A 1 157 ? -2.535  25.851  21.744  1.00 81.85  ? 157 ILE A CG1   1 
ATOM   1301 C  CG2   . ILE A 1 157 ? -2.329  26.533  24.140  1.00 87.57  ? 157 ILE A CG2   1 
ATOM   1302 C  CD1   . ILE A 1 157 ? -2.264  27.137  20.996  1.00 71.03  ? 157 ILE A CD1   1 
ATOM   1303 N  N     . LEU A 1 158 ? -4.458  24.111  25.799  1.00 90.30  ? 158 LEU A N     1 
ATOM   1304 C  CA    . LEU A 1 158 ? -5.176  24.230  27.062  1.00 91.55  ? 158 LEU A CA    1 
ATOM   1305 C  C     . LEU A 1 158 ? -4.740  25.472  27.831  1.00 83.02  ? 158 LEU A C     1 
ATOM   1306 O  O     . LEU A 1 158 ? -5.581  26.227  28.332  1.00 97.84  ? 158 LEU A O     1 
ATOM   1307 C  CB    . LEU A 1 158 ? -4.990  22.971  27.909  1.00 96.18  ? 158 LEU A CB    1 
ATOM   1308 C  CG    . LEU A 1 158 ? -5.229  21.647  27.181  1.00 102.55 ? 158 LEU A CG    1 
ATOM   1309 C  CD1   . LEU A 1 158 ? -4.545  20.493  27.905  1.00 102.54 ? 158 LEU A CD1   1 
ATOM   1310 C  CD2   . LEU A 1 158 ? -6.714  21.390  27.011  1.00 89.02  ? 158 LEU A CD2   1 
ATOM   1311 N  N     . MET A 1 159 ? -3.431  25.702  27.945  1.00 82.81  ? 159 MET A N     1 
ATOM   1312 C  CA    . MET A 1 159 ? -2.931  26.858  28.677  1.00 88.82  ? 159 MET A CA    1 
ATOM   1313 C  C     . MET A 1 159 ? -1.693  27.420  27.991  1.00 88.23  ? 159 MET A C     1 
ATOM   1314 O  O     . MET A 1 159 ? -1.005  26.732  27.235  1.00 86.74  ? 159 MET A O     1 
ATOM   1315 C  CB    . MET A 1 159 ? -2.592  26.526  30.141  1.00 96.86  ? 159 MET A CB    1 
ATOM   1316 C  CG    . MET A 1 159 ? -3.457  25.450  30.772  1.00 97.73  ? 159 MET A CG    1 
ATOM   1317 S  SD    . MET A 1 159 ? -2.616  24.588  32.103  1.00 106.59 ? 159 MET A SD    1 
ATOM   1318 C  CE    . MET A 1 159 ? -2.952  25.712  33.451  1.00 103.47 ? 159 MET A CE    1 
ATOM   1319 N  N     . ILE A 1 160 ? -1.422  28.693  28.274  1.00 84.17  ? 160 ILE A N     1 
ATOM   1320 C  CA    . ILE A 1 160 ? -0.229  29.387  27.806  1.00 78.86  ? 160 ILE A CA    1 
ATOM   1321 C  C     . ILE A 1 160 ? 0.437   30.036  29.009  1.00 81.03  ? 160 ILE A C     1 
ATOM   1322 O  O     . ILE A 1 160 ? -0.232  30.693  29.814  1.00 88.67  ? 160 ILE A O     1 
ATOM   1323 C  CB    . ILE A 1 160 ? -0.555  30.447  26.736  1.00 81.35  ? 160 ILE A CB    1 
ATOM   1324 C  CG1   . ILE A 1 160 ? -0.919  29.777  25.410  1.00 91.89  ? 160 ILE A CG1   1 
ATOM   1325 C  CG2   . ILE A 1 160 ? 0.620   31.398  26.546  1.00 74.14  ? 160 ILE A CG2   1 
ATOM   1326 C  CD1   . ILE A 1 160 ? -1.077  30.751  24.262  1.00 84.91  ? 160 ILE A CD1   1 
ATOM   1327 N  N     . SER A 1 161 ? 1.746   29.848  29.135  1.00 85.61  ? 161 SER A N     1 
ATOM   1328 C  CA    . SER A 1 161 ? 2.516   30.422  30.223  1.00 80.47  ? 161 SER A CA    1 
ATOM   1329 C  C     . SER A 1 161 ? 3.575   31.363  29.664  1.00 80.45  ? 161 SER A C     1 
ATOM   1330 O  O     . SER A 1 161 ? 3.961   31.274  28.496  1.00 72.81  ? 161 SER A O     1 
ATOM   1331 C  CB    . SER A 1 161 ? 3.176   29.329  31.072  1.00 73.80  ? 161 SER A CB    1 
ATOM   1332 O  OG    . SER A 1 161 ? 3.691   28.292  30.255  1.00 87.79  ? 161 SER A OG    1 
ATOM   1333 N  N     . TYR A 1 162 ? 4.034   32.278  30.514  1.00 74.64  ? 162 TYR A N     1 
ATOM   1334 C  CA    . TYR A 1 162 ? 5.084   33.212  30.134  1.00 70.20  ? 162 TYR A CA    1 
ATOM   1335 C  C     . TYR A 1 162 ? 5.793   33.685  31.393  1.00 77.67  ? 162 TYR A C     1 
ATOM   1336 O  O     . TYR A 1 162 ? 5.236   33.643  32.492  1.00 83.03  ? 162 TYR A O     1 
ATOM   1337 C  CB    . TYR A 1 162 ? 4.526   34.393  29.327  1.00 71.68  ? 162 TYR A CB    1 
ATOM   1338 C  CG    . TYR A 1 162 ? 3.677   35.375  30.109  1.00 81.70  ? 162 TYR A CG    1 
ATOM   1339 C  CD1   . TYR A 1 162 ? 4.255   36.426  30.816  1.00 71.67  ? 162 TYR A CD1   1 
ATOM   1340 C  CD2   . TYR A 1 162 ? 2.294   35.254  30.132  1.00 85.95  ? 162 TYR A CD2   1 
ATOM   1341 C  CE1   . TYR A 1 162 ? 3.475   37.323  31.526  1.00 81.10  ? 162 TYR A CE1   1 
ATOM   1342 C  CE2   . TYR A 1 162 ? 1.507   36.145  30.838  1.00 84.07  ? 162 TYR A CE2   1 
ATOM   1343 C  CZ    . TYR A 1 162 ? 2.102   37.178  31.533  1.00 87.32  ? 162 TYR A CZ    1 
ATOM   1344 O  OH    . TYR A 1 162 ? 1.322   38.067  32.238  1.00 94.78  ? 162 TYR A OH    1 
ATOM   1345 N  N     . ALA A 1 163 ? 7.032   34.137  31.217  1.00 75.37  ? 163 ALA A N     1 
ATOM   1346 C  CA    . ALA A 1 163 ? 7.854   34.551  32.344  1.00 79.00  ? 163 ALA A CA    1 
ATOM   1347 C  C     . ALA A 1 163 ? 8.864   35.595  31.889  1.00 81.90  ? 163 ALA A C     1 
ATOM   1348 O  O     . ALA A 1 163 ? 9.345   35.564  30.751  1.00 84.16  ? 163 ALA A O     1 
ATOM   1349 C  CB    . ALA A 1 163 ? 8.569   33.352  32.977  1.00 74.10  ? 163 ALA A CB    1 
ATOM   1350 N  N     . ASP A 1 164 ? 9.180   36.520  32.799  1.00 85.53  ? 164 ASP A N     1 
ATOM   1351 C  CA    . ASP A 1 164 ? 10.192  37.547  32.579  1.00 83.06  ? 164 ASP A CA    1 
ATOM   1352 C  C     . ASP A 1 164 ? 10.780  38.026  33.902  1.00 88.86  ? 164 ASP A C     1 
ATOM   1353 O  O     . ASP A 1 164 ? 10.868  37.260  34.865  1.00 89.24  ? 164 ASP A O     1 
ATOM   1354 C  CB    . ASP A 1 164 ? 9.600   38.709  31.779  1.00 87.52  ? 164 ASP A CB    1 
ATOM   1355 C  CG    . ASP A 1 164 ? 8.425   39.381  32.475  1.00 90.92  ? 164 ASP A CG    1 
ATOM   1356 O  OD1   . ASP A 1 164 ? 8.323   39.339  33.720  1.00 99.80  ? 164 ASP A OD1   1 
ATOM   1357 O  OD2   . ASP A 1 164 ? 7.584   39.950  31.756  1.00 87.49  ? 164 ASP A OD2   1 
ATOM   1358 N  N     . GLU A 1 165 ? 11.177  39.298  33.966  1.00 90.45  ? 165 GLU A N     1 
ATOM   1359 C  CA    . GLU A 1 165 ? 11.706  39.834  35.214  1.00 96.20  ? 165 GLU A CA    1 
ATOM   1360 C  C     . GLU A 1 165 ? 10.616  40.155  36.228  1.00 102.75 ? 165 GLU A C     1 
ATOM   1361 O  O     . GLU A 1 165 ? 10.941  40.440  37.384  1.00 93.59  ? 165 GLU A O     1 
ATOM   1362 C  CB    . GLU A 1 165 ? 12.547  41.084  34.941  1.00 92.36  ? 165 GLU A CB    1 
ATOM   1363 C  CG    . GLU A 1 165 ? 13.762  41.228  35.863  1.00 106.07 ? 165 GLU A CG    1 
ATOM   1364 C  CD    . GLU A 1 165 ? 14.933  40.340  35.465  1.00 117.35 ? 165 GLU A CD    1 
ATOM   1365 O  OE1   . GLU A 1 165 ? 14.773  39.493  34.560  1.00 104.01 ? 165 GLU A OE1   1 
ATOM   1366 O  OE2   . GLU A 1 165 ? 16.021  40.499  36.058  1.00 116.79 ? 165 GLU A OE2   1 
ATOM   1367 N  N     . GLU A 1 166 ? 9.346   40.108  35.830  1.00 101.15 ? 166 GLU A N     1 
ATOM   1368 C  CA    . GLU A 1 166 ? 8.230   40.296  36.747  1.00 97.26  ? 166 GLU A CA    1 
ATOM   1369 C  C     . GLU A 1 166 ? 7.669   38.980  37.269  1.00 99.44  ? 166 GLU A C     1 
ATOM   1370 O  O     . GLU A 1 166 ? 6.697   38.994  38.031  1.00 90.06  ? 166 GLU A O     1 
ATOM   1371 C  CB    . GLU A 1 166 ? 7.110   41.093  36.066  1.00 95.62  ? 166 GLU A CB    1 
ATOM   1372 C  CG    . GLU A 1 166 ? 7.195   42.597  36.267  1.00 111.25 ? 166 GLU A CG    1 
ATOM   1373 C  CD    . GLU A 1 166 ? 8.042   43.281  35.211  1.00 122.54 ? 166 GLU A CD    1 
ATOM   1374 O  OE1   . GLU A 1 166 ? 9.172   43.703  35.535  1.00 127.59 ? 166 GLU A OE1   1 
ATOM   1375 O  OE2   . GLU A 1 166 ? 7.578   43.394  34.056  1.00 117.96 ? 166 GLU A OE2   1 
ATOM   1376 N  N     . GLY A 1 167 ? 8.247   37.854  36.877  1.00 98.78  ? 167 GLY A N     1 
ATOM   1377 C  CA    . GLY A 1 167 ? 7.793   36.550  37.312  1.00 95.88  ? 167 GLY A CA    1 
ATOM   1378 C  C     . GLY A 1 167 ? 7.098   35.795  36.194  1.00 85.89  ? 167 GLY A C     1 
ATOM   1379 O  O     . GLY A 1 167 ? 7.134   36.176  35.020  1.00 82.04  ? 167 GLY A O     1 
ATOM   1380 N  N     . ALA A 1 168 ? 6.449   34.702  36.583  1.00 78.26  ? 168 ALA A N     1 
ATOM   1381 C  CA    . ALA A 1 168 ? 5.760   33.822  35.653  1.00 86.88  ? 168 ALA A CA    1 
ATOM   1382 C  C     . ALA A 1 168 ? 4.257   33.855  35.898  1.00 87.48  ? 168 ALA A C     1 
ATOM   1383 O  O     . ALA A 1 168 ? 3.798   34.020  37.032  1.00 96.36  ? 168 ALA A O     1 
ATOM   1384 C  CB    . ALA A 1 168 ? 6.276   32.385  35.773  1.00 80.56  ? 168 ALA A CB    1 
ATOM   1385 N  N     . ARG A 1 169 ? 3.494   33.700  34.817  1.00 68.09  ? 169 ARG A N     1 
ATOM   1386 C  CA    . ARG A 1 169 ? 2.040   33.674  34.881  1.00 82.21  ? 169 ARG A CA    1 
ATOM   1387 C  C     . ARG A 1 169 ? 1.518   32.614  33.921  1.00 88.34  ? 169 ARG A C     1 
ATOM   1388 O  O     . ARG A 1 169 ? 2.227   32.161  33.020  1.00 84.89  ? 169 ARG A O     1 
ATOM   1389 C  CB    . ARG A 1 169 ? 1.427   35.041  34.541  1.00 83.16  ? 169 ARG A CB    1 
ATOM   1390 C  CG    . ARG A 1 169 ? 1.879   36.179  35.446  1.00 85.20  ? 169 ARG A CG    1 
ATOM   1391 C  CD    . ARG A 1 169 ? 1.008   36.293  36.687  1.00 91.07  ? 169 ARG A CD    1 
ATOM   1392 N  NE    . ARG A 1 169 ? -0.115  37.199  36.481  1.00 84.52  ? 169 ARG A NE    1 
ATOM   1393 C  CZ    . ARG A 1 169 ? -1.350  36.969  36.904  1.00 96.60  ? 169 ARG A CZ    1 
ATOM   1394 N  NH1   . ARG A 1 169 ? -1.658  35.870  37.573  1.00 93.98  ? 169 ARG A NH1   1 
ATOM   1395 N  NH2   . ARG A 1 169 ? -2.300  37.864  36.650  1.00 101.37 ? 169 ARG A NH2   1 
ATOM   1396 N  N     . VAL A 1 170 ? 0.261   32.218  34.128  1.00 91.04  ? 170 VAL A N     1 
ATOM   1397 C  CA    . VAL A 1 170 ? -0.402  31.222  33.295  1.00 91.86  ? 170 VAL A CA    1 
ATOM   1398 C  C     . VAL A 1 170 ? -1.749  31.773  32.853  1.00 93.33  ? 170 VAL A C     1 
ATOM   1399 O  O     . VAL A 1 170 ? -2.413  32.506  33.591  1.00 93.37  ? 170 VAL A O     1 
ATOM   1400 C  CB    . VAL A 1 170 ? -0.586  29.873  34.034  1.00 93.35  ? 170 VAL A CB    1 
ATOM   1401 C  CG1   . VAL A 1 170 ? -1.142  28.813  33.094  1.00 93.79  ? 170 VAL A CG1   1 
ATOM   1402 C  CG2   . VAL A 1 170 ? 0.722   29.409  34.641  1.00 94.48  ? 170 VAL A CG2   1 
ATOM   1403 N  N     . ILE A 1 171 ? -2.149  31.423  31.632  1.00 95.55  ? 171 ILE A N     1 
ATOM   1404 C  CA    . ILE A 1 171 ? -3.435  31.827  31.075  1.00 93.32  ? 171 ILE A CA    1 
ATOM   1405 C  C     . ILE A 1 171 ? -4.125  30.585  30.529  1.00 98.98  ? 171 ILE A C     1 
ATOM   1406 O  O     . ILE A 1 171 ? -3.541  29.851  29.726  1.00 92.88  ? 171 ILE A O     1 
ATOM   1407 C  CB    . ILE A 1 171 ? -3.279  32.887  29.968  1.00 88.17  ? 171 ILE A CB    1 
ATOM   1408 C  CG1   . ILE A 1 171 ? -2.319  33.990  30.408  1.00 87.74  ? 171 ILE A CG1   1 
ATOM   1409 C  CG2   . ILE A 1 171 ? -4.630  33.494  29.627  1.00 104.17 ? 171 ILE A CG2   1 
ATOM   1410 C  CD1   . ILE A 1 171 ? -1.864  34.898  29.287  1.00 90.28  ? 171 ILE A CD1   1 
ATOM   1411 N  N     . THR A 1 172 ? -5.358  30.349  30.971  1.00 105.15 ? 172 THR A N     1 
ATOM   1412 C  CA    . THR A 1 172 ? -6.146  29.210  30.520  1.00 108.64 ? 172 THR A CA    1 
ATOM   1413 C  C     . THR A 1 172 ? -7.616  29.606  30.542  1.00 105.72 ? 172 THR A C     1 
ATOM   1414 O  O     . THR A 1 172 ? -7.980  30.671  31.042  1.00 105.09 ? 172 THR A O     1 
ATOM   1415 C  CB    . THR A 1 172 ? -5.900  27.973  31.391  1.00 99.95  ? 172 THR A CB    1 
ATOM   1416 O  OG1   . THR A 1 172 ? -6.825  26.938  31.034  1.00 102.87 ? 172 THR A OG1   1 
ATOM   1417 C  CG2   . THR A 1 172 ? -6.069  28.317  32.863  1.00 101.34 ? 172 THR A CG2   1 
ATOM   1418 N  N     . TRP A 1 173 ? -8.472  28.739  29.993  1.00 110.01 ? 173 TRP A N     1 
ATOM   1419 C  CA    . TRP A 1 173 ? -9.897  29.049  29.967  1.00 115.32 ? 173 TRP A CA    1 
ATOM   1420 C  C     . TRP A 1 173 ? -10.714 28.273  30.993  1.00 120.71 ? 173 TRP A C     1 
ATOM   1421 O  O     . TRP A 1 173 ? -11.787 28.745  31.383  1.00 134.65 ? 173 TRP A O     1 
ATOM   1422 C  CB    . TRP A 1 173 ? -10.480 28.831  28.561  1.00 119.27 ? 173 TRP A CB    1 
ATOM   1423 C  CG    . TRP A 1 173 ? -10.661 27.406  28.119  1.00 124.14 ? 173 TRP A CG    1 
ATOM   1424 C  CD1   . TRP A 1 173 ? -11.597 26.515  28.564  1.00 124.41 ? 173 TRP A CD1   1 
ATOM   1425 C  CD2   . TRP A 1 173 ? -9.919  26.728  27.101  1.00 120.51 ? 173 TRP A CD2   1 
ATOM   1426 N  NE1   . TRP A 1 173 ? -11.464 25.318  27.903  1.00 129.97 ? 173 TRP A NE1   1 
ATOM   1427 C  CE2   . TRP A 1 173 ? -10.443 25.425  26.997  1.00 132.04 ? 173 TRP A CE2   1 
ATOM   1428 C  CE3   . TRP A 1 173 ? -8.854  27.094  26.275  1.00 106.98 ? 173 TRP A CE3   1 
ATOM   1429 C  CZ2   . TRP A 1 173 ? -9.936  24.486  26.102  1.00 127.72 ? 173 TRP A CZ2   1 
ATOM   1430 C  CZ3   . TRP A 1 173 ? -8.358  26.164  25.386  1.00 114.92 ? 173 TRP A CZ3   1 
ATOM   1431 C  CH2   . TRP A 1 173 ? -8.894  24.875  25.307  1.00 125.79 ? 173 TRP A CH2   1 
ATOM   1432 N  N     . LYS A 1 174 ? -10.249 27.110  31.439  1.00 115.80 ? 174 LYS A N     1 
ATOM   1433 C  CA    . LYS A 1 174 ? -10.880 26.445  32.571  1.00 107.88 ? 174 LYS A CA    1 
ATOM   1434 C  C     . LYS A 1 174 ? -10.446 27.118  33.865  1.00 110.47 ? 174 LYS A C     1 
ATOM   1435 O  O     . LYS A 1 174 ? -9.305  27.572  33.994  1.00 109.47 ? 174 LYS A O     1 
ATOM   1436 C  CB    . LYS A 1 174 ? -10.519 24.960  32.606  1.00 100.59 ? 174 LYS A CB    1 
ATOM   1437 C  CG    . LYS A 1 174 ? -11.694 24.038  32.891  1.00 108.09 ? 174 LYS A CG    1 
ATOM   1438 C  CD    . LYS A 1 174 ? -11.506 22.683  32.227  1.00 106.14 ? 174 LYS A CD    1 
ATOM   1439 C  CE    . LYS A 1 174 ? -12.215 22.623  30.886  1.00 111.79 ? 174 LYS A CE    1 
ATOM   1440 N  NZ    . LYS A 1 174 ? -12.402 21.219  30.428  1.00 113.23 ? 174 LYS A NZ    1 
ATOM   1441 N  N     . ASN A 1 175 ? -11.362 27.182  34.827  1.00 123.20 ? 175 ASN A N     1 
ATOM   1442 C  CA    . ASN A 1 175 ? -11.102 27.907  36.066  1.00 124.15 ? 175 ASN A CA    1 
ATOM   1443 C  C     . ASN A 1 175 ? -10.107 27.134  36.921  1.00 119.06 ? 175 ASN A C     1 
ATOM   1444 O  O     . ASN A 1 175 ? -10.450 26.106  37.514  1.00 124.90 ? 175 ASN A O     1 
ATOM   1445 C  CB    . ASN A 1 175 ? -12.399 28.148  36.830  1.00 109.81 ? 175 ASN A CB    1 
ATOM   1446 C  CG    . ASN A 1 175 ? -12.162 28.761  38.199  1.00 128.66 ? 175 ASN A CG    1 
ATOM   1447 O  OD1   . ASN A 1 175 ? -11.177 29.472  38.415  1.00 122.46 ? 175 ASN A OD1   1 
ATOM   1448 N  ND2   . ASN A 1 175 ? -13.062 28.486  39.134  1.00 149.44 ? 175 ASN A ND2   1 
ATOM   1449 N  N     . VAL A 1 176 ? -8.876  27.631  36.988  1.00 115.38 ? 176 VAL A N     1 
ATOM   1450 C  CA    . VAL A 1 176 ? -7.860  27.129  37.904  1.00 115.50 ? 176 VAL A CA    1 
ATOM   1451 C  C     . VAL A 1 176 ? -7.580  28.236  38.911  1.00 107.77 ? 176 VAL A C     1 
ATOM   1452 O  O     . VAL A 1 176 ? -7.233  29.361  38.529  1.00 109.06 ? 176 VAL A O     1 
ATOM   1453 C  CB    . VAL A 1 176 ? -6.585  26.698  37.160  1.00 112.46 ? 176 VAL A CB    1 
ATOM   1454 C  CG1   . VAL A 1 176 ? -5.369  26.845  38.050  1.00 106.75 ? 176 VAL A CG1   1 
ATOM   1455 C  CG2   . VAL A 1 176 ? -6.714  25.259  36.683  1.00 95.29  ? 176 VAL A CG2   1 
ATOM   1456 N  N     . ASP A 1 177 ? -7.757  27.929  40.193  1.00 107.01 ? 177 ASP A N     1 
ATOM   1457 C  CA    . ASP A 1 177 ? -7.639  28.924  41.257  1.00 123.57 ? 177 ASP A CA    1 
ATOM   1458 C  C     . ASP A 1 177 ? -6.208  28.898  41.783  1.00 119.57 ? 177 ASP A C     1 
ATOM   1459 O  O     . ASP A 1 177 ? -5.843  28.035  42.584  1.00 108.98 ? 177 ASP A O     1 
ATOM   1460 C  CB    . ASP A 1 177 ? -8.657  28.651  42.361  1.00 128.91 ? 177 ASP A CB    1 
ATOM   1461 C  CG    . ASP A 1 177 ? -8.319  29.362  43.658  1.00 136.27 ? 177 ASP A CG    1 
ATOM   1462 O  OD1   . ASP A 1 177 ? -7.936  30.551  43.607  1.00 141.88 ? 177 ASP A OD1   1 
ATOM   1463 O  OD2   . ASP A 1 177 ? -8.441  28.730  44.729  1.00 130.98 ? 177 ASP A OD2   1 
ATOM   1464 N  N     . LEU A 1 178 ? -5.396  29.843  41.322  1.00 115.19 ? 178 LEU A N     1 
ATOM   1465 C  CA    . LEU A 1 178 ? -4.016  29.988  41.760  1.00 111.08 ? 178 LEU A CA    1 
ATOM   1466 C  C     . LEU A 1 178 ? -3.607  31.441  41.578  1.00 113.84 ? 178 LEU A C     1 
ATOM   1467 O  O     . LEU A 1 178 ? -4.203  32.160  40.768  1.00 115.89 ? 178 LEU A O     1 
ATOM   1468 C  CB    . LEU A 1 178 ? -3.072  29.057  40.986  1.00 109.02 ? 178 LEU A CB    1 
ATOM   1469 C  CG    . LEU A 1 178 ? -2.926  27.627  41.516  1.00 104.14 ? 178 LEU A CG    1 
ATOM   1470 C  CD1   . LEU A 1 178 ? -2.781  26.621  40.390  1.00 96.40  ? 178 LEU A CD1   1 
ATOM   1471 C  CD2   . LEU A 1 178 ? -1.750  27.529  42.472  1.00 110.66 ? 178 LEU A CD2   1 
ATOM   1472 N  N     . PRO A 1 179 ? -2.596  31.909  42.322  1.00 114.09 ? 179 PRO A N     1 
ATOM   1473 C  CA    . PRO A 1 179 ? -2.227  33.331  42.248  1.00 112.79 ? 179 PRO A CA    1 
ATOM   1474 C  C     . PRO A 1 179 ? -1.504  33.727  40.970  1.00 104.35 ? 179 PRO A C     1 
ATOM   1475 O  O     . PRO A 1 179 ? -1.370  34.931  40.712  1.00 98.50  ? 179 PRO A O     1 
ATOM   1476 C  CB    . PRO A 1 179 ? -1.324  33.519  43.472  1.00 112.13 ? 179 PRO A CB    1 
ATOM   1477 C  CG    . PRO A 1 179 ? -0.723  32.174  43.685  1.00 108.86 ? 179 PRO A CG    1 
ATOM   1478 C  CD    . PRO A 1 179 ? -1.817  31.197  43.349  1.00 109.75 ? 179 PRO A CD    1 
ATOM   1479 N  N     . TYR A 1 180 ? -1.032  32.773  40.165  1.00 102.29 ? 180 TYR A N     1 
ATOM   1480 C  CA    . TYR A 1 180 ? -0.317  33.086  38.932  1.00 96.74  ? 180 TYR A CA    1 
ATOM   1481 C  C     . TYR A 1 180 ? -1.076  32.623  37.693  1.00 99.59  ? 180 TYR A C     1 
ATOM   1482 O  O     . TYR A 1 180 ? -0.483  32.507  36.615  1.00 102.17 ? 180 TYR A O     1 
ATOM   1483 C  CB    . TYR A 1 180 ? 1.086   32.474  38.956  1.00 89.76  ? 180 TYR A CB    1 
ATOM   1484 C  CG    . TYR A 1 180 ? 1.109   30.991  39.260  1.00 97.52  ? 180 TYR A CG    1 
ATOM   1485 C  CD1   . TYR A 1 180 ? 0.847   30.052  38.269  1.00 92.60  ? 180 TYR A CD1   1 
ATOM   1486 C  CD2   . TYR A 1 180 ? 1.393   30.531  40.538  1.00 107.97 ? 180 TYR A CD2   1 
ATOM   1487 C  CE1   . TYR A 1 180 ? 0.865   28.698  38.545  1.00 81.82  ? 180 TYR A CE1   1 
ATOM   1488 C  CE2   . TYR A 1 180 ? 1.415   29.179  40.822  1.00 100.79 ? 180 TYR A CE2   1 
ATOM   1489 C  CZ    . TYR A 1 180 ? 1.151   28.268  39.822  1.00 94.92  ? 180 TYR A CZ    1 
ATOM   1490 O  OH    . TYR A 1 180 ? 1.172   26.922  40.103  1.00 103.69 ? 180 TYR A OH    1 
ATOM   1491 N  N     . VAL A 1 181 ? -2.373  32.358  37.820  1.00 98.00  ? 181 VAL A N     1 
ATOM   1492 C  CA    . VAL A 1 181 ? -3.194  31.870  36.719  1.00 99.99  ? 181 VAL A CA    1 
ATOM   1493 C  C     . VAL A 1 181 ? -4.261  32.907  36.400  1.00 95.96  ? 181 VAL A C     1 
ATOM   1494 O  O     . VAL A 1 181 ? -4.874  33.483  37.305  1.00 105.47 ? 181 VAL A O     1 
ATOM   1495 C  CB    . VAL A 1 181 ? -3.834  30.505  37.046  1.00 105.70 ? 181 VAL A CB    1 
ATOM   1496 C  CG1   . VAL A 1 181 ? -4.632  29.991  35.858  1.00 98.14  ? 181 VAL A CG1   1 
ATOM   1497 C  CG2   . VAL A 1 181 ? -2.762  29.501  37.437  1.00 101.82 ? 181 VAL A CG2   1 
ATOM   1498 N  N     . ASP A 1 182 ? -4.471  33.147  35.108  1.00 96.26  ? 182 ASP A N     1 
ATOM   1499 C  CA    . ASP A 1 182 ? -5.506  34.047  34.616  1.00 96.87  ? 182 ASP A CA    1 
ATOM   1500 C  C     . ASP A 1 182 ? -6.475  33.234  33.771  1.00 101.43 ? 182 ASP A C     1 
ATOM   1501 O  O     . ASP A 1 182 ? -6.081  32.662  32.749  1.00 95.65  ? 182 ASP A O     1 
ATOM   1502 C  CB    . ASP A 1 182 ? -4.901  35.188  33.798  1.00 97.91  ? 182 ASP A CB    1 
ATOM   1503 C  CG    . ASP A 1 182 ? -3.848  35.957  34.566  1.00 102.11 ? 182 ASP A CG    1 
ATOM   1504 O  OD1   . ASP A 1 182 ? -4.068  36.221  35.767  1.00 85.67  ? 182 ASP A OD1   1 
ATOM   1505 O  OD2   . ASP A 1 182 ? -2.800  36.287  33.972  1.00 94.51  ? 182 ASP A OD2   1 
ATOM   1506 N  N     . VAL A 1 183 ? -7.732  33.177  34.196  1.00 108.84 ? 183 VAL A N     1 
ATOM   1507 C  CA    . VAL A 1 183 ? -8.754  32.402  33.503  1.00 111.29 ? 183 VAL A CA    1 
ATOM   1508 C  C     . VAL A 1 183 ? -9.520  33.309  32.551  1.00 101.13 ? 183 VAL A C     1 
ATOM   1509 O  O     . VAL A 1 183 ? -9.763  34.486  32.845  1.00 94.13  ? 183 VAL A O     1 
ATOM   1510 C  CB    . VAL A 1 183 ? -9.709  31.712  34.497  1.00 108.05 ? 183 VAL A CB    1 
ATOM   1511 C  CG1   . VAL A 1 183 ? -10.463 30.599  33.796  1.00 110.73 ? 183 VAL A CG1   1 
ATOM   1512 C  CG2   . VAL A 1 183 ? -8.935  31.163  35.688  1.00 100.59 ? 183 VAL A CG2   1 
ATOM   1513 N  N     . VAL A 1 184 ? -9.892  32.758  31.397  1.00 97.43  ? 184 VAL A N     1 
ATOM   1514 C  CA    . VAL A 1 184 ? -10.659 33.453  30.376  1.00 100.58 ? 184 VAL A CA    1 
ATOM   1515 C  C     . VAL A 1 184 ? -11.801 32.545  29.925  1.00 109.03 ? 184 VAL A C     1 
ATOM   1516 O  O     . VAL A 1 184 ? -11.985 31.443  30.440  1.00 115.72 ? 184 VAL A O     1 
ATOM   1517 C  CB    . VAL A 1 184 ? -9.787  33.885  29.178  1.00 106.39 ? 184 VAL A CB    1 
ATOM   1518 C  CG1   . VAL A 1 184 ? -8.679  34.825  29.635  1.00 87.78  ? 184 VAL A CG1   1 
ATOM   1519 C  CG2   . VAL A 1 184 ? -9.197  32.667  28.480  1.00 99.84  ? 184 VAL A CG2   1 
ATOM   1520 N  N     . SER A 1 185 ? -12.572 33.021  28.945  1.00 114.76 ? 185 SER A N     1 
ATOM   1521 C  CA    . SER A 1 185 ? -13.741 32.272  28.497  1.00 119.85 ? 185 SER A CA    1 
ATOM   1522 C  C     . SER A 1 185 ? -13.351 31.100  27.603  1.00 111.64 ? 185 SER A C     1 
ATOM   1523 O  O     . SER A 1 185 ? -13.764 29.961  27.848  1.00 114.68 ? 185 SER A O     1 
ATOM   1524 C  CB    . SER A 1 185 ? -14.715 33.199  27.770  1.00 110.28 ? 185 SER A CB    1 
ATOM   1525 O  OG    . SER A 1 185 ? -15.019 34.336  28.560  1.00 122.23 ? 185 SER A OG    1 
ATOM   1526 N  N     . THR A 1 186 ? -12.554 31.353  26.565  1.00 108.22 ? 186 THR A N     1 
ATOM   1527 C  CA    . THR A 1 186 ? -12.273 30.342  25.559  1.00 115.16 ? 186 THR A CA    1 
ATOM   1528 C  C     . THR A 1 186 ? -10.801 30.383  25.170  1.00 113.24 ? 186 THR A C     1 
ATOM   1529 O  O     . THR A 1 186 ? -10.022 31.221  25.642  1.00 119.40 ? 186 THR A O     1 
ATOM   1530 C  CB    . THR A 1 186 ? -13.154 30.535  24.320  1.00 128.03 ? 186 THR A CB    1 
ATOM   1531 O  OG1   . THR A 1 186 ? -12.965 29.433  23.420  1.00 139.54 ? 186 THR A OG1   1 
ATOM   1532 C  CG2   . THR A 1 186 ? -12.794 31.831  23.608  1.00 120.87 ? 186 THR A CG2   1 
ATOM   1533 N  N     . GLU A 1 187 ? -10.432 29.447  24.292  1.00 110.48 ? 187 GLU A N     1 
ATOM   1534 C  CA    . GLU A 1 187 ? -9.103  29.434  23.692  1.00 102.87 ? 187 GLU A CA    1 
ATOM   1535 C  C     . GLU A 1 187 ? -8.789  30.754  23.004  1.00 107.03 ? 187 GLU A C     1 
ATOM   1536 O  O     . GLU A 1 187 ? -7.689  31.298  23.151  1.00 104.26 ? 187 GLU A O     1 
ATOM   1537 C  CB    . GLU A 1 187 ? -9.013  28.284  22.691  1.00 92.50  ? 187 GLU A CB    1 
ATOM   1538 C  CG    . GLU A 1 187 ? -7.651  28.114  22.074  1.00 90.20  ? 187 GLU A CG    1 
ATOM   1539 C  CD    . GLU A 1 187 ? -7.382  26.690  21.666  1.00 96.14  ? 187 GLU A CD    1 
ATOM   1540 O  OE1   . GLU A 1 187 ? -7.994  26.225  20.681  1.00 88.44  ? 187 GLU A OE1   1 
ATOM   1541 O  OE2   . GLU A 1 187 ? -6.553  26.040  22.327  1.00 106.08 ? 187 GLU A OE2   1 
ATOM   1542 N  N     . ARG A 1 188 ? -9.741  31.265  22.219  1.00 107.17 ? 188 ARG A N     1 
ATOM   1543 C  CA    . ARG A 1 188 ? -9.539  32.520  21.503  1.00 96.99  ? 188 ARG A CA    1 
ATOM   1544 C  C     . ARG A 1 188 ? -9.105  33.624  22.452  1.00 87.64  ? 188 ARG A C     1 
ATOM   1545 O  O     . ARG A 1 188 ? -8.031  34.214  22.294  1.00 91.91  ? 188 ARG A O     1 
ATOM   1546 C  CB    . ARG A 1 188 ? -10.819 32.932  20.778  1.00 110.67 ? 188 ARG A CB    1 
ATOM   1547 C  CG    . ARG A 1 188 ? -10.790 34.377  20.307  1.00 111.35 ? 188 ARG A CG    1 
ATOM   1548 C  CD    . ARG A 1 188 ? -12.033 34.753  19.522  1.00 117.92 ? 188 ARG A CD    1 
ATOM   1549 N  NE    . ARG A 1 188 ? -11.687 35.485  18.310  1.00 129.12 ? 188 ARG A NE    1 
ATOM   1550 C  CZ    . ARG A 1 188 ? -11.486 34.927  17.124  1.00 117.19 ? 188 ARG A CZ    1 
ATOM   1551 N  NH1   . ARG A 1 188 ? -11.622 33.625  16.941  1.00 113.64 ? 188 ARG A NH1   1 
ATOM   1552 N  NH2   . ARG A 1 188 ? -11.148 35.697  16.094  1.00 111.59 ? 188 ARG A NH2   1 
ATOM   1553 N  N     . GLU A 1 189 ? -9.938  33.907  23.454  1.00 98.51  ? 189 GLU A N     1 
ATOM   1554 C  CA    . GLU A 1 189 ? -9.605  34.938  24.427  1.00 104.53 ? 189 GLU A CA    1 
ATOM   1555 C  C     . GLU A 1 189 ? -8.291  34.654  25.141  1.00 93.70  ? 189 GLU A C     1 
ATOM   1556 O  O     . GLU A 1 189 ? -7.665  35.591  25.639  1.00 93.56  ? 189 GLU A O     1 
ATOM   1557 C  CB    . GLU A 1 189 ? -10.736 35.087  25.450  1.00 106.43 ? 189 GLU A CB    1 
ATOM   1558 C  CG    . GLU A 1 189 ? -12.117 35.413  24.869  1.00 109.54 ? 189 GLU A CG    1 
ATOM   1559 C  CD    . GLU A 1 189 ? -12.065 36.162  23.545  1.00 118.79 ? 189 GLU A CD    1 
ATOM   1560 O  OE1   . GLU A 1 189 ? -11.517 37.284  23.493  1.00 103.91 ? 189 GLU A OE1   1 
ATOM   1561 O  OE2   . GLU A 1 189 ? -12.599 35.626  22.552  1.00 134.30 ? 189 GLU A OE2   1 
ATOM   1562 N  N     . MET A 1 190 ? -7.857  33.392  25.200  1.00 91.94  ? 190 MET A N     1 
ATOM   1563 C  CA    . MET A 1 190 ? -6.550  33.083  25.776  1.00 95.00  ? 190 MET A CA    1 
ATOM   1564 C  C     . MET A 1 190 ? -5.425  33.483  24.828  1.00 93.38  ? 190 MET A C     1 
ATOM   1565 O  O     . MET A 1 190 ? -4.545  34.273  25.187  1.00 87.00  ? 190 MET A O     1 
ATOM   1566 C  CB    . MET A 1 190 ? -6.454  31.593  26.113  1.00 95.64  ? 190 MET A CB    1 
ATOM   1567 C  CG    . MET A 1 190 ? -5.239  31.234  26.960  1.00 87.83  ? 190 MET A CG    1 
ATOM   1568 S  SD    . MET A 1 190 ? -4.761  29.498  26.841  1.00 86.83  ? 190 MET A SD    1 
ATOM   1569 C  CE    . MET A 1 190 ? -5.196  29.132  25.143  1.00 86.99  ? 190 MET A CE    1 
ATOM   1570 N  N     . ILE A 1 191 ? -5.429  32.926  23.612  1.00 87.58  ? 191 ILE A N     1 
ATOM   1571 C  CA    . ILE A 1 191 ? -4.415  33.286  22.624  1.00 79.03  ? 191 ILE A CA    1 
ATOM   1572 C  C     . ILE A 1 191 ? -4.457  34.781  22.340  1.00 85.10  ? 191 ILE A C     1 
ATOM   1573 O  O     . ILE A 1 191 ? -3.414  35.435  22.211  1.00 86.21  ? 191 ILE A O     1 
ATOM   1574 C  CB    . ILE A 1 191 ? -4.598  32.463  21.334  1.00 72.59  ? 191 ILE A CB    1 
ATOM   1575 C  CG1   . ILE A 1 191 ? -4.613  30.966  21.642  1.00 73.86  ? 191 ILE A CG1   1 
ATOM   1576 C  CG2   . ILE A 1 191 ? -3.501  32.786  20.331  1.00 86.20  ? 191 ILE A CG2   1 
ATOM   1577 C  CD1   . ILE A 1 191 ? -5.168  30.127  20.516  1.00 78.23  ? 191 ILE A CD1   1 
ATOM   1578 N  N     . LYS A 1 192 ? -5.663  35.347  22.243  1.00 78.50  ? 192 LYS A N     1 
ATOM   1579 C  CA    . LYS A 1 192 ? -5.792  36.789  22.061  1.00 85.44  ? 192 LYS A CA    1 
ATOM   1580 C  C     . LYS A 1 192 ? -5.222  37.544  23.254  1.00 85.28  ? 192 LYS A C     1 
ATOM   1581 O  O     . LYS A 1 192 ? -4.585  38.592  23.089  1.00 74.59  ? 192 LYS A O     1 
ATOM   1582 C  CB    . LYS A 1 192 ? -7.259  37.162  21.842  1.00 85.39  ? 192 LYS A CB    1 
ATOM   1583 C  CG    . LYS A 1 192 ? -7.492  38.238  20.796  1.00 97.49  ? 192 LYS A CG    1 
ATOM   1584 C  CD    . LYS A 1 192 ? -8.937  38.715  20.821  1.00 102.24 ? 192 LYS A CD    1 
ATOM   1585 C  CE    . LYS A 1 192 ? -9.651  38.389  19.519  1.00 101.63 ? 192 LYS A CE    1 
ATOM   1586 N  NZ    . LYS A 1 192 ? -11.047 38.912  19.506  1.00 95.56  ? 192 LYS A NZ    1 
ATOM   1587 N  N     . ARG A 1 193 ? -5.437  37.025  24.467  1.00 88.76  ? 193 ARG A N     1 
ATOM   1588 C  CA    . ARG A 1 193 ? -4.876  37.666  25.653  1.00 93.23  ? 193 ARG A CA    1 
ATOM   1589 C  C     . ARG A 1 193 ? -3.356  37.611  25.639  1.00 85.18  ? 193 ARG A C     1 
ATOM   1590 O  O     . ARG A 1 193 ? -2.693  38.606  25.951  1.00 87.76  ? 193 ARG A O     1 
ATOM   1591 C  CB    . ARG A 1 193 ? -5.422  37.005  26.919  1.00 90.57  ? 193 ARG A CB    1 
ATOM   1592 C  CG    . ARG A 1 193 ? -4.534  37.126  28.141  1.00 97.46  ? 193 ARG A CG    1 
ATOM   1593 C  CD    . ARG A 1 193 ? -4.605  38.522  28.723  1.00 108.71 ? 193 ARG A CD    1 
ATOM   1594 N  NE    . ARG A 1 193 ? -4.300  38.536  30.147  1.00 118.58 ? 193 ARG A NE    1 
ATOM   1595 C  CZ    . ARG A 1 193 ? -4.203  39.637  30.879  1.00 122.69 ? 193 ARG A CZ    1 
ATOM   1596 N  NH1   . ARG A 1 193 ? -4.378  40.836  30.350  1.00 124.61 ? 193 ARG A NH1   1 
ATOM   1597 N  NH2   . ARG A 1 193 ? -3.928  39.531  32.176  1.00 106.68 ? 193 ARG A NH2   1 
ATOM   1598 N  N     . PHE A 1 194 ? -2.788  36.457  25.280  1.00 80.27  ? 194 PHE A N     1 
ATOM   1599 C  CA    . PHE A 1 194 ? -1.335  36.329  25.238  1.00 86.50  ? 194 PHE A CA    1 
ATOM   1600 C  C     . PHE A 1 194 ? -0.724  37.308  24.245  1.00 82.45  ? 194 PHE A C     1 
ATOM   1601 O  O     . PHE A 1 194 ? 0.340   37.882  24.505  1.00 79.62  ? 194 PHE A O     1 
ATOM   1602 C  CB    . PHE A 1 194 ? -0.947  34.893  24.889  1.00 83.69  ? 194 PHE A CB    1 
ATOM   1603 C  CG    . PHE A 1 194 ? 0.522   34.706  24.635  1.00 81.27  ? 194 PHE A CG    1 
ATOM   1604 C  CD1   . PHE A 1 194 ? 1.442   34.908  25.649  1.00 84.07  ? 194 PHE A CD1   1 
ATOM   1605 C  CD2   . PHE A 1 194 ? 0.981   34.327  23.384  1.00 77.11  ? 194 PHE A CD2   1 
ATOM   1606 C  CE1   . PHE A 1 194 ? 2.793   34.736  25.422  1.00 69.97  ? 194 PHE A CE1   1 
ATOM   1607 C  CE2   . PHE A 1 194 ? 2.333   34.153  23.151  1.00 63.22  ? 194 PHE A CE2   1 
ATOM   1608 C  CZ    . PHE A 1 194 ? 3.239   34.358  24.172  1.00 67.90  ? 194 PHE A CZ    1 
ATOM   1609 N  N     . LEU A 1 195 ? -1.382  37.508  23.099  1.00 82.05  ? 195 LEU A N     1 
ATOM   1610 C  CA    . LEU A 1 195 ? -0.937  38.528  22.152  1.00 79.51  ? 195 LEU A CA    1 
ATOM   1611 C  C     . LEU A 1 195 ? -0.927  39.909  22.785  1.00 83.86  ? 195 LEU A C     1 
ATOM   1612 O  O     . LEU A 1 195 ? 0.011   40.689  22.577  1.00 88.01  ? 195 LEU A O     1 
ATOM   1613 C  CB    . LEU A 1 195 ? -1.830  38.526  20.914  1.00 75.54  ? 195 LEU A CB    1 
ATOM   1614 C  CG    . LEU A 1 195 ? -1.706  37.293  20.034  1.00 80.86  ? 195 LEU A CG    1 
ATOM   1615 C  CD1   . LEU A 1 195 ? -2.884  37.174  19.088  1.00 94.12  ? 195 LEU A CD1   1 
ATOM   1616 C  CD2   . LEU A 1 195 ? -0.412  37.446  19.269  1.00 86.97  ? 195 LEU A CD2   1 
ATOM   1617 N  N     . ARG A 1 196 ? -1.971  40.234  23.550  1.00 90.90  ? 196 ARG A N     1 
ATOM   1618 C  CA    . ARG A 1 196 ? -2.021  41.527  24.222  1.00 92.71  ? 196 ARG A CA    1 
ATOM   1619 C  C     . ARG A 1 196 ? -0.837  41.714  25.160  1.00 81.57  ? 196 ARG A C     1 
ATOM   1620 O  O     . ARG A 1 196 ? -0.354  42.839  25.332  1.00 80.94  ? 196 ARG A O     1 
ATOM   1621 C  CB    . ARG A 1 196 ? -3.335  41.664  24.990  1.00 80.52  ? 196 ARG A CB    1 
ATOM   1622 C  CG    . ARG A 1 196 ? -4.300  42.676  24.401  1.00 86.69  ? 196 ARG A CG    1 
ATOM   1623 C  CD    . ARG A 1 196 ? -5.740  42.286  24.689  1.00 84.59  ? 196 ARG A CD    1 
ATOM   1624 N  NE    . ARG A 1 196 ? -5.967  42.064  26.112  1.00 86.35  ? 196 ARG A NE    1 
ATOM   1625 C  CZ    . ARG A 1 196 ? -6.625  41.027  26.612  1.00 94.32  ? 196 ARG A CZ    1 
ATOM   1626 N  NH1   . ARG A 1 196 ? -7.139  40.092  25.830  1.00 89.09  ? 196 ARG A NH1   1 
ATOM   1627 N  NH2   . ARG A 1 196 ? -6.772  40.926  27.930  1.00 92.00  ? 196 ARG A NH2   1 
ATOM   1628 N  N     . VAL A 1 197 ? -0.352  40.630  25.766  1.00 84.94  ? 197 VAL A N     1 
ATOM   1629 C  CA    . VAL A 1 197 ? 0.796   40.728  26.662  1.00 95.64  ? 197 VAL A CA    1 
ATOM   1630 C  C     . VAL A 1 197 ? 2.055   41.071  25.876  1.00 79.35  ? 197 VAL A C     1 
ATOM   1631 O  O     . VAL A 1 197 ? 2.694   42.100  26.119  1.00 89.00  ? 197 VAL A O     1 
ATOM   1632 C  CB    . VAL A 1 197 ? 0.971   39.429  27.466  1.00 97.37  ? 197 VAL A CB    1 
ATOM   1633 C  CG1   . VAL A 1 197 ? 1.957   39.645  28.602  1.00 88.28  ? 197 VAL A CG1   1 
ATOM   1634 C  CG2   . VAL A 1 197 ? -0.364  38.962  28.013  1.00 81.12  ? 197 VAL A CG2   1 
ATOM   1635 N  N     . VAL A 1 198 ? 2.416   40.220  24.911  1.00 76.66  ? 198 VAL A N     1 
ATOM   1636 C  CA    . VAL A 1 198 ? 3.668   40.399  24.175  1.00 84.14  ? 198 VAL A CA    1 
ATOM   1637 C  C     . VAL A 1 198 ? 3.731   41.788  23.551  1.00 85.66  ? 198 VAL A C     1 
ATOM   1638 O  O     . VAL A 1 198 ? 4.752   42.481  23.638  1.00 83.68  ? 198 VAL A O     1 
ATOM   1639 C  CB    . VAL A 1 198 ? 3.828   39.299  23.111  1.00 80.18  ? 198 VAL A CB    1 
ATOM   1640 C  CG1   . VAL A 1 198 ? 4.994   39.623  22.189  1.00 77.56  ? 198 VAL A CG1   1 
ATOM   1641 C  CG2   . VAL A 1 198 ? 4.020   37.946  23.773  1.00 76.08  ? 198 VAL A CG2   1 
ATOM   1642 N  N     . LYS A 1 199 ? 2.637   42.217  22.918  1.00 83.35  ? 199 LYS A N     1 
ATOM   1643 C  CA    . LYS A 1 199 ? 2.599   43.557  22.341  1.00 84.71  ? 199 LYS A CA    1 
ATOM   1644 C  C     . LYS A 1 199 ? 2.800   44.622  23.412  1.00 82.28  ? 199 LYS A C     1 
ATOM   1645 O  O     . LYS A 1 199 ? 3.423   45.660  23.159  1.00 84.74  ? 199 LYS A O     1 
ATOM   1646 C  CB    . LYS A 1 199 ? 1.274   43.775  21.608  1.00 79.30  ? 199 LYS A CB    1 
ATOM   1647 C  CG    . LYS A 1 199 ? 1.355   43.599  20.098  1.00 100.97 ? 199 LYS A CG    1 
ATOM   1648 C  CD    . LYS A 1 199 ? 1.699   44.908  19.401  1.00 111.16 ? 199 LYS A CD    1 
ATOM   1649 C  CE    . LYS A 1 199 ? 2.178   44.668  17.977  1.00 114.78 ? 199 LYS A CE    1 
ATOM   1650 N  NZ    . LYS A 1 199 ? 3.200   45.665  17.551  1.00 94.18  ? 199 LYS A NZ    1 
ATOM   1651 N  N     . GLU A 1 200 ? 2.292   44.375  24.622  1.00 88.72  ? 200 GLU A N     1 
ATOM   1652 C  CA    . GLU A 1 200 ? 2.396   45.363  25.690  1.00 85.22  ? 200 GLU A CA    1 
ATOM   1653 C  C     . GLU A 1 200 ? 3.811   45.424  26.254  1.00 84.73  ? 200 GLU A C     1 
ATOM   1654 O  O     . GLU A 1 200 ? 4.376   46.512  26.421  1.00 82.70  ? 200 GLU A O     1 
ATOM   1655 C  CB    . GLU A 1 200 ? 1.388   45.046  26.795  1.00 86.32  ? 200 GLU A CB    1 
ATOM   1656 C  CG    . GLU A 1 200 ? 1.469   45.967  28.000  1.00 99.26  ? 200 GLU A CG    1 
ATOM   1657 C  CD    . GLU A 1 200 ? 0.301   46.931  28.077  1.00 119.25 ? 200 GLU A CD    1 
ATOM   1658 O  OE1   . GLU A 1 200 ? -0.797  46.576  27.600  1.00 118.71 ? 200 GLU A OE1   1 
ATOM   1659 O  OE2   . GLU A 1 200 ? 0.481   48.044  28.615  1.00 132.02 ? 200 GLU A OE2   1 
ATOM   1660 N  N     . LYS A 1 201 ? 4.402   44.265  26.558  1.00 89.11  ? 201 LYS A N     1 
ATOM   1661 C  CA    . LYS A 1 201 ? 5.746   44.259  27.129  1.00 86.72  ? 201 LYS A CA    1 
ATOM   1662 C  C     . LYS A 1 201 ? 6.801   44.642  26.100  1.00 91.33  ? 201 LYS A C     1 
ATOM   1663 O  O     . LYS A 1 201 ? 7.865   45.151  26.473  1.00 92.15  ? 201 LYS A O     1 
ATOM   1664 C  CB    . LYS A 1 201 ? 6.070   42.888  27.728  1.00 82.18  ? 201 LYS A CB    1 
ATOM   1665 C  CG    . LYS A 1 201 ? 4.857   42.099  28.186  1.00 94.26  ? 201 LYS A CG    1 
ATOM   1666 C  CD    . LYS A 1 201 ? 5.178   41.182  29.351  1.00 84.62  ? 201 LYS A CD    1 
ATOM   1667 C  CE    . LYS A 1 201 ? 5.450   41.980  30.615  1.00 93.60  ? 201 LYS A CE    1 
ATOM   1668 N  NZ    . LYS A 1 201 ? 5.430   41.113  31.826  1.00 85.30  ? 201 LYS A NZ    1 
ATOM   1669 N  N     . ASP A 1 202 ? 6.529   44.412  24.820  1.00 83.65  ? 202 ASP A N     1 
ATOM   1670 C  CA    . ASP A 1 202 ? 7.457   44.720  23.736  1.00 80.91  ? 202 ASP A CA    1 
ATOM   1671 C  C     . ASP A 1 202 ? 8.841   44.118  23.970  1.00 84.96  ? 202 ASP A C     1 
ATOM   1672 O  O     . ASP A 1 202 ? 9.830   44.858  24.120  1.00 87.84  ? 202 ASP A O     1 
ATOM   1673 C  CB    . ASP A 1 202 ? 7.549   46.224  23.521  1.00 80.69  ? 202 ASP A CB    1 
ATOM   1674 C  CG    . ASP A 1 202 ? 8.074   46.585  22.143  1.00 96.97  ? 202 ASP A CG    1 
ATOM   1675 O  OD1   . ASP A 1 202 ? 8.168   45.681  21.286  1.00 94.09  ? 202 ASP A OD1   1 
ATOM   1676 O  OD2   . ASP A 1 202 ? 8.392   47.773  21.919  1.00 95.26  ? 202 ASP A OD2   1 
ATOM   1677 N  N     . PRO A 1 203 ? 8.964   42.794  24.007  1.00 81.18  ? 203 PRO A N     1 
ATOM   1678 C  CA    . PRO A 1 203 ? 10.273  42.184  24.257  1.00 74.72  ? 203 PRO A CA    1 
ATOM   1679 C  C     . PRO A 1 203 ? 11.113  42.121  22.991  1.00 72.86  ? 203 PRO A C     1 
ATOM   1680 O  O     . PRO A 1 203 ? 10.601  41.913  21.888  1.00 73.02  ? 203 PRO A O     1 
ATOM   1681 C  CB    . PRO A 1 203 ? 9.913   40.780  24.753  1.00 74.95  ? 203 PRO A CB    1 
ATOM   1682 C  CG    . PRO A 1 203 ? 8.644   40.466  24.034  1.00 77.50  ? 203 PRO A CG    1 
ATOM   1683 C  CD    . PRO A 1 203 ? 7.905   41.776  23.866  1.00 84.58  ? 203 PRO A CD    1 
ATOM   1684 N  N     . ASP A 1 204 ? 12.422  42.310  23.162  1.00 75.61  ? 204 ASP A N     1 
ATOM   1685 C  CA    . ASP A 1 204 ? 13.342  42.149  22.043  1.00 62.75  ? 204 ASP A CA    1 
ATOM   1686 C  C     . ASP A 1 204 ? 13.626  40.682  21.757  1.00 57.91  ? 204 ASP A C     1 
ATOM   1687 O  O     . ASP A 1 204 ? 13.862  40.312  20.602  1.00 63.76  ? 204 ASP A O     1 
ATOM   1688 C  CB    . ASP A 1 204 ? 14.651  42.887  22.321  1.00 63.23  ? 204 ASP A CB    1 
ATOM   1689 C  CG    . ASP A 1 204 ? 14.427  44.316  22.764  1.00 74.95  ? 204 ASP A CG    1 
ATOM   1690 O  OD1   . ASP A 1 204 ? 13.849  45.097  21.979  1.00 79.54  ? 204 ASP A OD1   1 
ATOM   1691 O  OD2   . ASP A 1 204 ? 14.825  44.657  23.897  1.00 72.17  ? 204 ASP A OD2   1 
ATOM   1692 N  N     . VAL A 1 205 ? 13.599  39.840  22.785  1.00 62.38  ? 205 VAL A N     1 
ATOM   1693 C  CA    . VAL A 1 205 ? 13.907  38.423  22.659  1.00 61.27  ? 205 VAL A CA    1 
ATOM   1694 C  C     . VAL A 1 205 ? 12.701  37.621  23.125  1.00 61.95  ? 205 VAL A C     1 
ATOM   1695 O  O     . VAL A 1 205 ? 12.173  37.861  24.218  1.00 63.68  ? 205 VAL A O     1 
ATOM   1696 C  CB    . VAL A 1 205 ? 15.160  38.041  23.469  1.00 60.92  ? 205 VAL A CB    1 
ATOM   1697 C  CG1   . VAL A 1 205 ? 15.397  36.542  23.400  1.00 63.22  ? 205 VAL A CG1   1 
ATOM   1698 C  CG2   . VAL A 1 205 ? 16.372  38.808  22.962  1.00 59.04  ? 205 VAL A CG2   1 
ATOM   1699 N  N     . LEU A 1 206 ? 12.265  36.679  22.295  1.00 66.68  ? 206 LEU A N     1 
ATOM   1700 C  CA    . LEU A 1 206 ? 11.235  35.711  22.657  1.00 63.68  ? 206 LEU A CA    1 
ATOM   1701 C  C     . LEU A 1 206 ? 11.924  34.369  22.868  1.00 61.18  ? 206 LEU A C     1 
ATOM   1702 O  O     . LEU A 1 206 ? 12.375  33.738  21.906  1.00 70.53  ? 206 LEU A O     1 
ATOM   1703 C  CB    . LEU A 1 206 ? 10.155  35.618  21.580  1.00 57.60  ? 206 LEU A CB    1 
ATOM   1704 C  CG    . LEU A 1 206 ? 9.116   36.740  21.521  1.00 68.55  ? 206 LEU A CG    1 
ATOM   1705 C  CD1   . LEU A 1 206 ? 8.217   36.574  20.303  1.00 69.63  ? 206 LEU A CD1   1 
ATOM   1706 C  CD2   . LEU A 1 206 ? 8.291   36.777  22.797  1.00 64.33  ? 206 LEU A CD2   1 
ATOM   1707 N  N     . ILE A 1 207 ? 12.013  33.940  24.121  1.00 57.40  ? 207 ILE A N     1 
ATOM   1708 C  CA    . ILE A 1 207 ? 12.722  32.717  24.475  1.00 59.72  ? 207 ILE A CA    1 
ATOM   1709 C  C     . ILE A 1 207 ? 11.740  31.556  24.484  1.00 71.42  ? 207 ILE A C     1 
ATOM   1710 O  O     . ILE A 1 207 ? 10.660  31.645  25.080  1.00 71.46  ? 207 ILE A O     1 
ATOM   1711 C  CB    . ILE A 1 207 ? 13.418  32.858  25.838  1.00 68.67  ? 207 ILE A CB    1 
ATOM   1712 C  CG1   . ILE A 1 207 ? 14.184  34.179  25.915  1.00 58.58  ? 207 ILE A CG1   1 
ATOM   1713 C  CG2   . ILE A 1 207 ? 14.353  31.686  26.077  1.00 68.37  ? 207 ILE A CG2   1 
ATOM   1714 C  CD1   . ILE A 1 207 ? 14.618  34.551  27.316  1.00 67.80  ? 207 ILE A CD1   1 
ATOM   1715 N  N     . THR A 1 208 ? 12.108  30.468  23.810  1.00 68.82  ? 208 THR A N     1 
ATOM   1716 C  CA    . THR A 1 208 ? 11.329  29.238  23.824  1.00 61.75  ? 208 THR A CA    1 
ATOM   1717 C  C     . THR A 1 208 ? 12.270  28.058  24.006  1.00 62.76  ? 208 THR A C     1 
ATOM   1718 O  O     . THR A 1 208 ? 13.494  28.185  23.908  1.00 59.69  ? 208 THR A O     1 
ATOM   1719 C  CB    . THR A 1 208 ? 10.514  29.044  22.536  1.00 72.85  ? 208 THR A CB    1 
ATOM   1720 O  OG1   . THR A 1 208 ? 11.379  28.600  21.483  1.00 62.36  ? 208 THR A OG1   1 
ATOM   1721 C  CG2   . THR A 1 208 ? 9.825   30.331  22.115  1.00 71.24  ? 208 THR A CG2   1 
ATOM   1722 N  N     . TYR A 1 209 ? 11.680  26.897  24.276  1.00 66.79  ? 209 TYR A N     1 
ATOM   1723 C  CA    . TYR A 1 209 ? 12.389  25.621  24.251  1.00 57.07  ? 209 TYR A CA    1 
ATOM   1724 C  C     . TYR A 1 209 ? 11.678  24.737  23.235  1.00 60.11  ? 209 TYR A C     1 
ATOM   1725 O  O     . TYR A 1 209 ? 10.575  24.247  23.501  1.00 71.89  ? 209 TYR A O     1 
ATOM   1726 C  CB    . TYR A 1 209 ? 12.422  24.973  25.634  1.00 65.75  ? 209 TYR A CB    1 
ATOM   1727 C  CG    . TYR A 1 209 ? 13.443  23.863  25.761  1.00 74.12  ? 209 TYR A CG    1 
ATOM   1728 C  CD1   . TYR A 1 209 ? 14.805  24.140  25.731  1.00 66.72  ? 209 TYR A CD1   1 
ATOM   1729 C  CD2   . TYR A 1 209 ? 13.047  22.540  25.914  1.00 61.59  ? 209 TYR A CD2   1 
ATOM   1730 C  CE1   . TYR A 1 209 ? 15.742  23.132  25.848  1.00 66.76  ? 209 TYR A CE1   1 
ATOM   1731 C  CE2   . TYR A 1 209 ? 13.977  21.526  26.032  1.00 72.86  ? 209 TYR A CE2   1 
ATOM   1732 C  CZ    . TYR A 1 209 ? 15.322  21.827  25.998  1.00 72.47  ? 209 TYR A CZ    1 
ATOM   1733 O  OH    . TYR A 1 209 ? 16.249  20.818  26.115  1.00 73.33  ? 209 TYR A OH    1 
ATOM   1734 N  N     . ASN A 1 210 ? 12.308  24.558  22.072  1.00 62.20  ? 210 ASN A N     1 
ATOM   1735 C  CA    . ASN A 1 210 ? 11.753  23.850  20.920  1.00 62.71  ? 210 ASN A CA    1 
ATOM   1736 C  C     . ASN A 1 210 ? 10.577  24.587  20.287  1.00 70.41  ? 210 ASN A C     1 
ATOM   1737 O  O     . ASN A 1 210 ? 9.738   23.967  19.625  1.00 70.47  ? 210 ASN A O     1 
ATOM   1738 C  CB    . ASN A 1 210 ? 11.344  22.414  21.273  1.00 58.10  ? 210 ASN A CB    1 
ATOM   1739 C  CG    . ASN A 1 210 ? 11.249  21.519  20.053  1.00 74.18  ? 210 ASN A CG    1 
ATOM   1740 O  OD1   . ASN A 1 210 ? 12.031  21.652  19.111  1.00 81.89  ? 210 ASN A OD1   1 
ATOM   1741 N  ND2   . ASN A 1 210 ? 10.281  20.610  20.057  1.00 76.61  ? 210 ASN A ND2   1 
ATOM   1742 N  N     . GLY A 1 211 ? 10.493  25.906  20.469  1.00 64.62  ? 211 GLY A N     1 
ATOM   1743 C  CA    . GLY A 1 211 ? 9.464   26.668  19.784  1.00 69.38  ? 211 GLY A CA    1 
ATOM   1744 C  C     . GLY A 1 211 ? 9.618   26.668  18.279  1.00 73.55  ? 211 GLY A C     1 
ATOM   1745 O  O     . GLY A 1 211 ? 8.644   26.923  17.562  1.00 72.62  ? 211 GLY A O     1 
ATOM   1746 N  N     . ASP A 1 212 ? 10.824  26.379  17.783  1.00 69.23  ? 212 ASP A N     1 
ATOM   1747 C  CA    . ASP A 1 212 ? 11.049  26.311  16.344  1.00 66.10  ? 212 ASP A CA    1 
ATOM   1748 C  C     . ASP A 1 212 ? 10.227  25.210  15.694  1.00 70.78  ? 212 ASP A C     1 
ATOM   1749 O  O     . ASP A 1 212 ? 9.877   25.313  14.513  1.00 72.56  ? 212 ASP A O     1 
ATOM   1750 C  CB    . ASP A 1 212 ? 12.529  26.075  16.057  1.00 65.96  ? 212 ASP A CB    1 
ATOM   1751 C  CG    . ASP A 1 212 ? 13.282  27.352  15.801  1.00 69.27  ? 212 ASP A CG    1 
ATOM   1752 O  OD1   . ASP A 1 212 ? 12.640  28.418  15.699  1.00 67.31  ? 212 ASP A OD1   1 
ATOM   1753 O  OD2   . ASP A 1 212 ? 14.525  27.295  15.702  1.00 68.86  ? 212 ASP A OD2   1 
ATOM   1754 N  N     . ASN A 1 213 ? 9.918   24.150  16.439  1.00 69.84  ? 213 ASN A N     1 
ATOM   1755 C  CA    . ASN A 1 213 ? 9.284   22.979  15.861  1.00 75.07  ? 213 ASN A CA    1 
ATOM   1756 C  C     . ASN A 1 213 ? 7.988   22.566  16.545  1.00 70.87  ? 213 ASN A C     1 
ATOM   1757 O  O     . ASN A 1 213 ? 7.357   21.604  16.093  1.00 75.64  ? 213 ASN A O     1 
ATOM   1758 C  CB    . ASN A 1 213 ? 10.263  21.793  15.871  1.00 69.29  ? 213 ASN A CB    1 
ATOM   1759 C  CG    . ASN A 1 213 ? 11.511  22.061  15.051  1.00 62.15  ? 213 ASN A CG    1 
ATOM   1760 O  OD1   . ASN A 1 213 ? 11.452  22.179  13.827  1.00 76.57  ? 213 ASN A OD1   1 
ATOM   1761 N  ND2   . ASN A 1 213 ? 12.651  22.163  15.724  1.00 80.06  ? 213 ASN A ND2   1 
ATOM   1762 N  N     . PHE A 1 214 ? 7.566   23.252  17.610  1.00 73.53  ? 214 PHE A N     1 
ATOM   1763 C  CA    . PHE A 1 214 ? 6.302   22.891  18.245  1.00 75.82  ? 214 PHE A CA    1 
ATOM   1764 C  C     . PHE A 1 214 ? 5.458   24.102  18.630  1.00 76.18  ? 214 PHE A C     1 
ATOM   1765 O  O     . PHE A 1 214 ? 4.408   24.335  18.022  1.00 71.24  ? 214 PHE A O     1 
ATOM   1766 C  CB    . PHE A 1 214 ? 6.540   22.022  19.481  1.00 68.88  ? 214 PHE A CB    1 
ATOM   1767 C  CG    . PHE A 1 214 ? 5.285   21.734  20.259  1.00 87.47  ? 214 PHE A CG    1 
ATOM   1768 C  CD1   . PHE A 1 214 ? 4.280   20.955  19.710  1.00 74.20  ? 214 PHE A CD1   1 
ATOM   1769 C  CD2   . PHE A 1 214 ? 5.103   22.248  21.531  1.00 91.05  ? 214 PHE A CD2   1 
ATOM   1770 C  CE1   . PHE A 1 214 ? 3.122   20.692  20.415  1.00 71.97  ? 214 PHE A CE1   1 
ATOM   1771 C  CE2   . PHE A 1 214 ? 3.947   21.991  22.242  1.00 79.20  ? 214 PHE A CE2   1 
ATOM   1772 C  CZ    . PHE A 1 214 ? 2.955   21.210  21.683  1.00 72.13  ? 214 PHE A CZ    1 
ATOM   1773 N  N     . ASP A 1 215 ? 5.901   24.868  19.637  1.00 74.04  ? 215 ASP A N     1 
ATOM   1774 C  CA    . ASP A 1 215 ? 5.050   25.892  20.246  1.00 71.63  ? 215 ASP A CA    1 
ATOM   1775 C  C     . ASP A 1 215 ? 4.466   26.841  19.204  1.00 75.51  ? 215 ASP A C     1 
ATOM   1776 O  O     . ASP A 1 215 ? 3.253   27.084  19.175  1.00 77.94  ? 215 ASP A O     1 
ATOM   1777 C  CB    . ASP A 1 215 ? 5.831   26.696  21.293  1.00 71.70  ? 215 ASP A CB    1 
ATOM   1778 C  CG    . ASP A 1 215 ? 6.482   25.826  22.355  1.00 95.14  ? 215 ASP A CG    1 
ATOM   1779 O  OD1   . ASP A 1 215 ? 6.821   26.363  23.433  1.00 99.25  ? 215 ASP A OD1   1 
ATOM   1780 O  OD2   . ASP A 1 215 ? 6.684   24.623  22.111  1.00 89.34  ? 215 ASP A OD2   1 
ATOM   1781 N  N     . PHE A 1 216 ? 5.319   27.388  18.337  1.00 70.69  ? 216 PHE A N     1 
ATOM   1782 C  CA    . PHE A 1 216 ? 4.856   28.383  17.374  1.00 70.36  ? 216 PHE A CA    1 
ATOM   1783 C  C     . PHE A 1 216 ? 3.905   27.769  16.352  1.00 62.99  ? 216 PHE A C     1 
ATOM   1784 O  O     . PHE A 1 216 ? 2.904   28.391  15.975  1.00 71.80  ? 216 PHE A O     1 
ATOM   1785 C  CB    . PHE A 1 216 ? 6.054   29.027  16.679  1.00 65.18  ? 216 PHE A CB    1 
ATOM   1786 C  CG    . PHE A 1 216 ? 6.585   30.238  17.390  1.00 68.40  ? 216 PHE A CG    1 
ATOM   1787 C  CD1   . PHE A 1 216 ? 5.919   31.449  17.315  1.00 58.07  ? 216 PHE A CD1   1 
ATOM   1788 C  CD2   . PHE A 1 216 ? 7.751   30.165  18.136  1.00 63.08  ? 216 PHE A CD2   1 
ATOM   1789 C  CE1   . PHE A 1 216 ? 6.406   32.566  17.973  1.00 71.67  ? 216 PHE A CE1   1 
ATOM   1790 C  CE2   . PHE A 1 216 ? 8.243   31.278  18.794  1.00 57.26  ? 216 PHE A CE2   1 
ATOM   1791 C  CZ    . PHE A 1 216 ? 7.570   32.480  18.713  1.00 66.03  ? 216 PHE A CZ    1 
ATOM   1792 N  N     . ALA A 1 217 ? 4.193   26.547  15.899  1.00 70.77  ? 217 ALA A N     1 
ATOM   1793 C  CA    . ALA A 1 217 ? 3.361   25.928  14.872  1.00 67.24  ? 217 ALA A CA    1 
ATOM   1794 C  C     . ALA A 1 217 ? 2.004   25.519  15.433  1.00 78.19  ? 217 ALA A C     1 
ATOM   1795 O  O     . ALA A 1 217 ? 0.989   25.594  14.730  1.00 83.61  ? 217 ALA A O     1 
ATOM   1796 C  CB    . ALA A 1 217 ? 4.080   24.725  14.263  1.00 62.48  ? 217 ALA A CB    1 
ATOM   1797 N  N     . TYR A 1 218 ? 1.969   25.067  16.690  1.00 74.31  ? 218 TYR A N     1 
ATOM   1798 C  CA    . TYR A 1 218 ? 0.690   24.833  17.353  1.00 75.07  ? 218 TYR A CA    1 
ATOM   1799 C  C     . TYR A 1 218 ? -0.119  26.124  17.431  1.00 73.47  ? 218 TYR A C     1 
ATOM   1800 O  O     . TYR A 1 218 ? -1.282  26.169  17.014  1.00 83.00  ? 218 TYR A O     1 
ATOM   1801 C  CB    . TYR A 1 218 ? 0.906   24.264  18.756  1.00 78.52  ? 218 TYR A CB    1 
ATOM   1802 C  CG    . TYR A 1 218 ? -0.097  23.199  19.146  1.00 85.59  ? 218 TYR A CG    1 
ATOM   1803 C  CD1   . TYR A 1 218 ? -0.005  21.902  18.655  1.00 85.11  ? 218 TYR A CD1   1 
ATOM   1804 C  CD2   . TYR A 1 218 ? -1.181  23.513  19.946  1.00 94.86  ? 218 TYR A CD2   1 
ATOM   1805 C  CE1   . TYR A 1 218 ? -0.935  20.938  19.012  1.00 86.01  ? 218 TYR A CE1   1 
ATOM   1806 C  CE2   . TYR A 1 218 ? -2.126  22.565  20.291  1.00 89.26  ? 218 TYR A CE2   1 
ATOM   1807 C  CZ    . TYR A 1 218 ? -2.000  21.278  19.821  1.00 92.10  ? 218 TYR A CZ    1 
ATOM   1808 O  OH    . TYR A 1 218 ? -2.939  20.332  20.170  1.00 81.23  ? 218 TYR A OH    1 
ATOM   1809 N  N     . LEU A 1 219 ? 0.495   27.193  17.949  1.00 77.85  ? 219 LEU A N     1 
ATOM   1810 C  CA    . LEU A 1 219 ? -0.157  28.497  17.977  1.00 74.21  ? 219 LEU A CA    1 
ATOM   1811 C  C     . LEU A 1 219 ? -0.569  28.951  16.586  1.00 77.67  ? 219 LEU A C     1 
ATOM   1812 O  O     . LEU A 1 219 ? -1.522  29.722  16.444  1.00 85.69  ? 219 LEU A O     1 
ATOM   1813 C  CB    . LEU A 1 219 ? 0.766   29.533  18.616  1.00 63.68  ? 219 LEU A CB    1 
ATOM   1814 C  CG    . LEU A 1 219 ? 0.795   29.544  20.144  1.00 71.75  ? 219 LEU A CG    1 
ATOM   1815 C  CD1   . LEU A 1 219 ? 2.139   30.041  20.647  1.00 57.68  ? 219 LEU A CD1   1 
ATOM   1816 C  CD2   . LEU A 1 219 ? -0.340  30.394  20.700  1.00 70.47  ? 219 LEU A CD2   1 
ATOM   1817 N  N     . LYS A 1 220 ? 0.133   28.491  15.550  1.00 70.40  ? 220 LYS A N     1 
ATOM   1818 C  CA    . LYS A 1 220 ? -0.269  28.811  14.184  1.00 74.15  ? 220 LYS A CA    1 
ATOM   1819 C  C     . LYS A 1 220 ? -1.563  28.098  13.814  1.00 79.78  ? 220 LYS A C     1 
ATOM   1820 O  O     . LYS A 1 220 ? -2.548  28.736  13.426  1.00 89.51  ? 220 LYS A O     1 
ATOM   1821 C  CB    . LYS A 1 220 ? 0.847   28.444  13.205  1.00 74.04  ? 220 LYS A CB    1 
ATOM   1822 C  CG    . LYS A 1 220 ? 0.543   28.801  11.759  1.00 83.99  ? 220 LYS A CG    1 
ATOM   1823 C  CD    . LYS A 1 220 ? 1.295   27.899  10.797  1.00 77.17  ? 220 LYS A CD    1 
ATOM   1824 C  CE    . LYS A 1 220 ? 1.783   28.675  9.588   1.00 73.66  ? 220 LYS A CE    1 
ATOM   1825 N  NZ    . LYS A 1 220 ? 2.464   27.787  8.609   1.00 86.47  ? 220 LYS A NZ    1 
ATOM   1826 N  N     . LYS A 1 221 ? -1.579  26.766  13.941  1.00 79.87  ? 221 LYS A N     1 
ATOM   1827 C  CA    . LYS A 1 221 ? -2.714  25.979  13.456  1.00 83.37  ? 221 LYS A CA    1 
ATOM   1828 C  C     . LYS A 1 221 ? -4.011  26.353  14.163  1.00 91.43  ? 221 LYS A C     1 
ATOM   1829 O  O     . LYS A 1 221 ? -5.062  26.458  13.522  1.00 88.11  ? 221 LYS A O     1 
ATOM   1830 C  CB    . LYS A 1 221 ? -2.438  24.489  13.623  1.00 80.94  ? 221 LYS A CB    1 
ATOM   1831 C  CG    . LYS A 1 221 ? -3.504  23.603  12.988  1.00 87.20  ? 221 LYS A CG    1 
ATOM   1832 C  CD    . LYS A 1 221 ? -3.436  23.635  11.474  1.00 99.83  ? 221 LYS A CD    1 
ATOM   1833 C  CE    . LYS A 1 221 ? -2.852  22.342  10.943  1.00 101.11 ? 221 LYS A CE    1 
ATOM   1834 N  NZ    . LYS A 1 221 ? -2.749  22.354  9.462   1.00 95.90  ? 221 LYS A NZ    1 
ATOM   1835 N  N     . ARG A 1 222 ? -3.969  26.532  15.483  1.00 78.95  ? 222 ARG A N     1 
ATOM   1836 C  CA    . ARG A 1 222 ? -5.169  26.978  16.174  1.00 85.85  ? 222 ARG A CA    1 
ATOM   1837 C  C     . ARG A 1 222 ? -5.579  28.368  15.702  1.00 93.20  ? 222 ARG A C     1 
ATOM   1838 O  O     . ARG A 1 222 ? -6.732  28.582  15.318  1.00 100.92 ? 222 ARG A O     1 
ATOM   1839 C  CB    . ARG A 1 222 ? -4.957  26.943  17.687  1.00 84.84  ? 222 ARG A CB    1 
ATOM   1840 C  CG    . ARG A 1 222 ? -4.098  25.781  18.152  1.00 92.78  ? 222 ARG A CG    1 
ATOM   1841 C  CD    . ARG A 1 222 ? -4.926  24.520  18.388  1.00 90.75  ? 222 ARG A CD    1 
ATOM   1842 N  NE    . ARG A 1 222 ? -6.266  24.793  18.897  1.00 89.12  ? 222 ARG A NE    1 
ATOM   1843 C  CZ    . ARG A 1 222 ? -7.382  24.282  18.393  1.00 93.31  ? 222 ARG A CZ    1 
ATOM   1844 N  NH1   . ARG A 1 222 ? -7.362  23.481  17.340  1.00 82.62  ? 222 ARG A NH1   1 
ATOM   1845 N  NH2   . ARG A 1 222 ? -8.548  24.581  18.960  1.00 77.26  ? 222 ARG A NH2   1 
ATOM   1846 N  N     . CYS A 1 223 ? -4.628  29.308  15.664  1.00 84.76  ? 223 CYS A N     1 
ATOM   1847 C  CA    . CYS A 1 223 ? -4.939  30.680  15.267  1.00 89.22  ? 223 CYS A CA    1 
ATOM   1848 C  C     . CYS A 1 223 ? -5.685  30.735  13.935  1.00 89.16  ? 223 CYS A C     1 
ATOM   1849 O  O     . CYS A 1 223 ? -6.555  31.591  13.745  1.00 83.02  ? 223 CYS A O     1 
ATOM   1850 C  CB    . CYS A 1 223 ? -3.660  31.519  15.188  1.00 79.30  ? 223 CYS A CB    1 
ATOM   1851 S  SG    . CYS A 1 223 ? -3.222  32.355  16.732  1.00 76.92  ? 223 CYS A SG    1 
ATOM   1852 N  N     . GLU A 1 224 ? -5.362  29.839  12.997  1.00 85.51  ? 224 GLU A N     1 
ATOM   1853 C  CA    . GLU A 1 224 ? -6.102  29.820  11.736  1.00 94.98  ? 224 GLU A CA    1 
ATOM   1854 C  C     . GLU A 1 224 ? -7.413  29.052  11.882  1.00 92.70  ? 224 GLU A C     1 
ATOM   1855 O  O     . GLU A 1 224 ? -8.487  29.568  11.553  1.00 96.17  ? 224 GLU A O     1 
ATOM   1856 C  CB    . GLU A 1 224 ? -5.256  29.220  10.606  1.00 93.37  ? 224 GLU A CB    1 
ATOM   1857 C  CG    . GLU A 1 224 ? -4.330  28.107  11.032  1.00 97.85  ? 224 GLU A CG    1 
ATOM   1858 C  CD    . GLU A 1 224 ? -3.201  27.869  10.052  1.00 97.83  ? 224 GLU A CD    1 
ATOM   1859 O  OE1   . GLU A 1 224 ? -2.577  28.855  9.609   1.00 84.38  ? 224 GLU A OE1   1 
ATOM   1860 O  OE2   . GLU A 1 224 ? -2.937  26.692  9.727   1.00 113.51 ? 224 GLU A OE2   1 
ATOM   1861 N  N     . LYS A 1 225 ? -7.342  27.822  12.401  1.00 92.94  ? 225 LYS A N     1 
ATOM   1862 C  CA    . LYS A 1 225 ? -8.517  27.003  12.686  1.00 100.07 ? 225 LYS A CA    1 
ATOM   1863 C  C     . LYS A 1 225 ? -9.500  27.736  13.591  1.00 105.44 ? 225 LYS A C     1 
ATOM   1864 O  O     . LYS A 1 225 ? -10.650 27.314  13.746  1.00 102.28 ? 225 LYS A O     1 
ATOM   1865 C  CB    . LYS A 1 225 ? -8.104  25.682  13.344  1.00 103.31 ? 225 LYS A CB    1 
ATOM   1866 C  CG    . LYS A 1 225 ? -8.608  24.417  12.658  1.00 118.06 ? 225 LYS A CG    1 
ATOM   1867 C  CD    . LYS A 1 225 ? -7.840  24.099  11.382  1.00 128.93 ? 225 LYS A CD    1 
ATOM   1868 C  CE    . LYS A 1 225 ? -8.455  22.904  10.665  1.00 139.03 ? 225 LYS A CE    1 
ATOM   1869 N  NZ    . LYS A 1 225 ? -7.657  22.477  9.483   1.00 125.59 ? 225 LYS A NZ    1 
ATOM   1870 N  N     . LEU A 1 226 ? -9.046  28.829  14.199  1.00 97.13  ? 226 LEU A N     1 
ATOM   1871 C  CA    . LEU A 1 226 ? -9.826  29.616  15.139  1.00 101.30 ? 226 LEU A CA    1 
ATOM   1872 C  C     . LEU A 1 226 ? -10.023 31.065  14.710  1.00 89.24  ? 226 LEU A C     1 
ATOM   1873 O  O     . LEU A 1 226 ? -11.010 31.679  15.117  1.00 99.09  ? 226 LEU A O     1 
ATOM   1874 C  CB    . LEU A 1 226 ? -9.155  29.567  16.520  1.00 99.36  ? 226 LEU A CB    1 
ATOM   1875 C  CG    . LEU A 1 226 ? -9.898  29.835  17.813  1.00 100.75 ? 226 LEU A CG    1 
ATOM   1876 C  CD1   . LEU A 1 226 ? -9.248  29.041  18.924  1.00 90.25  ? 226 LEU A CD1   1 
ATOM   1877 C  CD2   . LEU A 1 226 ? -9.766  31.291  18.079  1.00 103.56 ? 226 LEU A CD2   1 
ATOM   1878 N  N     . GLY A 1 227 ? -9.120  31.629  13.908  1.00 98.30  ? 227 GLY A N     1 
ATOM   1879 C  CA    . GLY A 1 227 ? -9.343  32.941  13.324  1.00 101.40 ? 227 GLY A CA    1 
ATOM   1880 C  C     . GLY A 1 227 ? -8.710  34.115  14.046  1.00 94.35  ? 227 GLY A C     1 
ATOM   1881 O  O     . GLY A 1 227 ? -9.324  35.182  14.147  1.00 89.11  ? 227 GLY A O     1 
ATOM   1882 N  N     . ILE A 1 228 ? -7.486  33.947  14.544  1.00 91.70  ? 228 ILE A N     1 
ATOM   1883 C  CA    . ILE A 1 228 ? -6.749  35.029  15.187  1.00 91.45  ? 228 ILE A CA    1 
ATOM   1884 C  C     . ILE A 1 228 ? -5.554  35.394  14.318  1.00 92.95  ? 228 ILE A C     1 
ATOM   1885 O  O     . ILE A 1 228 ? -4.967  34.544  13.638  1.00 84.01  ? 228 ILE A O     1 
ATOM   1886 C  CB    . ILE A 1 228 ? -6.283  34.664  16.614  1.00 91.77  ? 228 ILE A CB    1 
ATOM   1887 C  CG1   . ILE A 1 228 ? -7.364  33.878  17.353  1.00 90.07  ? 228 ILE A CG1   1 
ATOM   1888 C  CG2   . ILE A 1 228 ? -5.929  35.916  17.405  1.00 86.32  ? 228 ILE A CG2   1 
ATOM   1889 C  CD1   . ILE A 1 228 ? -6.972  33.490  18.764  1.00 77.79  ? 228 ILE A CD1   1 
ATOM   1890 N  N     . ASN A 1 229 ? -5.196  36.674  14.344  1.00 88.09  ? 229 ASN A N     1 
ATOM   1891 C  CA    . ASN A 1 229 ? -4.011  37.172  13.657  1.00 88.49  ? 229 ASN A CA    1 
ATOM   1892 C  C     . ASN A 1 229 ? -2.888  37.296  14.680  1.00 97.58  ? 229 ASN A C     1 
ATOM   1893 O  O     . ASN A 1 229 ? -2.905  38.195  15.528  1.00 92.85  ? 229 ASN A O     1 
ATOM   1894 C  CB    . ASN A 1 229 ? -4.292  38.510  12.981  1.00 89.39  ? 229 ASN A CB    1 
ATOM   1895 C  CG    . ASN A 1 229 ? -3.217  38.892  11.988  1.00 97.74  ? 229 ASN A CG    1 
ATOM   1896 O  OD1   . ASN A 1 229 ? -3.098  38.289  10.922  1.00 110.21 ? 229 ASN A OD1   1 
ATOM   1897 N  ND2   . ASN A 1 229 ? -2.420  39.895  12.338  1.00 100.00 ? 229 ASN A ND2   1 
ATOM   1898 N  N     . PHE A 1 230 ? -1.917  36.386  14.599  1.00 88.31  ? 230 PHE A N     1 
ATOM   1899 C  CA    . PHE A 1 230 ? -0.775  36.353  15.514  1.00 77.67  ? 230 PHE A CA    1 
ATOM   1900 C  C     . PHE A 1 230 ? 0.190   37.472  15.128  1.00 75.32  ? 230 PHE A C     1 
ATOM   1901 O  O     . PHE A 1 230 ? 1.204   37.264  14.461  1.00 87.09  ? 230 PHE A O     1 
ATOM   1902 C  CB    . PHE A 1 230 ? -0.096  34.988  15.463  1.00 80.70  ? 230 PHE A CB    1 
ATOM   1903 C  CG    . PHE A 1 230 ? 0.294   34.447  16.809  1.00 78.81  ? 230 PHE A CG    1 
ATOM   1904 C  CD1   . PHE A 1 230 ? -0.624  34.399  17.842  1.00 81.28  ? 230 PHE A CD1   1 
ATOM   1905 C  CD2   . PHE A 1 230 ? 1.582   33.989  17.041  1.00 84.83  ? 230 PHE A CD2   1 
ATOM   1906 C  CE1   . PHE A 1 230 ? -0.268  33.907  19.086  1.00 83.94  ? 230 PHE A CE1   1 
ATOM   1907 C  CE2   . PHE A 1 230 ? 1.945   33.494  18.280  1.00 83.18  ? 230 PHE A CE2   1 
ATOM   1908 C  CZ    . PHE A 1 230 ? 1.019   33.453  19.304  1.00 83.37  ? 230 PHE A CZ    1 
ATOM   1909 N  N     . ALA A 1 231 ? -0.131  38.687  15.563  1.00 75.46  ? 231 ALA A N     1 
ATOM   1910 C  CA    . ALA A 1 231 ? 0.694   39.854  15.239  1.00 70.42  ? 231 ALA A CA    1 
ATOM   1911 C  C     . ALA A 1 231 ? 1.851   40.024  16.223  1.00 80.80  ? 231 ALA A C     1 
ATOM   1912 O  O     . ALA A 1 231 ? 2.085   41.109  16.758  1.00 79.26  ? 231 ALA A O     1 
ATOM   1913 C  CB    . ALA A 1 231 ? -0.170  41.109  15.186  1.00 71.80  ? 231 ALA A CB    1 
ATOM   1914 N  N     . LEU A 1 232 ? 2.599   38.941  16.455  1.00 75.90  ? 232 LEU A N     1 
ATOM   1915 C  CA    . LEU A 1 232 ? 3.747   39.010  17.352  1.00 76.07  ? 232 LEU A CA    1 
ATOM   1916 C  C     . LEU A 1 232 ? 4.851   39.914  16.824  1.00 64.59  ? 232 LEU A C     1 
ATOM   1917 O  O     . LEU A 1 232 ? 5.622   40.454  17.623  1.00 68.31  ? 232 LEU A O     1 
ATOM   1918 C  CB    . LEU A 1 232 ? 4.334   37.621  17.604  1.00 66.46  ? 232 LEU A CB    1 
ATOM   1919 C  CG    . LEU A 1 232 ? 3.645   36.719  18.627  1.00 72.10  ? 232 LEU A CG    1 
ATOM   1920 C  CD1   . LEU A 1 232 ? 4.566   35.555  18.948  1.00 65.00  ? 232 LEU A CD1   1 
ATOM   1921 C  CD2   . LEU A 1 232 ? 3.240   37.477  19.889  1.00 60.30  ? 232 LEU A CD2   1 
ATOM   1922 N  N     . GLY A 1 233 ? 4.956   40.088  15.511  1.00 59.38  ? 233 GLY A N     1 
ATOM   1923 C  CA    . GLY A 1 233 ? 5.987   40.950  14.972  1.00 67.26  ? 233 GLY A CA    1 
ATOM   1924 C  C     . GLY A 1 233 ? 5.788   42.400  15.373  1.00 73.79  ? 233 GLY A C     1 
ATOM   1925 O  O     . GLY A 1 233 ? 4.669   42.869  15.588  1.00 79.11  ? 233 GLY A O     1 
ATOM   1926 N  N     . ARG A 1 234 ? 6.907   43.120  15.471  1.00 70.60  ? 234 ARG A N     1 
ATOM   1927 C  CA    . ARG A 1 234 ? 6.874   44.554  15.730  1.00 68.96  ? 234 ARG A CA    1 
ATOM   1928 C  C     . ARG A 1 234 ? 6.420   45.366  14.521  1.00 75.79  ? 234 ARG A C     1 
ATOM   1929 O  O     . ARG A 1 234 ? 6.038   46.529  14.689  1.00 88.70  ? 234 ARG A O     1 
ATOM   1930 C  CB    . ARG A 1 234 ? 8.250   45.034  16.197  1.00 65.77  ? 234 ARG A CB    1 
ATOM   1931 C  CG    . ARG A 1 234 ? 8.557   44.684  17.643  1.00 63.20  ? 234 ARG A CG    1 
ATOM   1932 C  CD    . ARG A 1 234 ? 9.954   45.122  18.010  1.00 66.13  ? 234 ARG A CD    1 
ATOM   1933 N  NE    . ARG A 1 234 ? 10.128  45.300  19.446  1.00 72.73  ? 234 ARG A NE    1 
ATOM   1934 C  CZ    . ARG A 1 234 ? 11.267  45.078  20.086  1.00 76.87  ? 234 ARG A CZ    1 
ATOM   1935 N  NH1   . ARG A 1 234 ? 12.353  44.683  19.444  1.00 64.68  ? 234 ARG A NH1   1 
ATOM   1936 N  NH2   . ARG A 1 234 ? 11.317  45.259  21.403  1.00 75.97  ? 234 ARG A NH2   1 
ATOM   1937 N  N     . ASP A 1 235 ? 6.444   44.788  13.321  1.00 64.09  ? 235 ASP A N     1 
ATOM   1938 C  CA    . ASP A 1 235 ? 5.839   45.384  12.138  1.00 74.24  ? 235 ASP A CA    1 
ATOM   1939 C  C     . ASP A 1 235 ? 4.381   44.974  11.959  1.00 78.62  ? 235 ASP A C     1 
ATOM   1940 O  O     . ASP A 1 235 ? 3.796   45.245  10.904  1.00 82.87  ? 235 ASP A O     1 
ATOM   1941 C  CB    . ASP A 1 235 ? 6.645   45.008  10.890  1.00 60.26  ? 235 ASP A CB    1 
ATOM   1942 C  CG    . ASP A 1 235 ? 6.586   43.526  10.589  1.00 70.97  ? 235 ASP A CG    1 
ATOM   1943 O  OD1   . ASP A 1 235 ? 6.851   43.121  9.436   1.00 61.23  ? 235 ASP A OD1   1 
ATOM   1944 O  OD2   . ASP A 1 235 ? 6.290   42.760  11.528  1.00 73.29  ? 235 ASP A OD2   1 
ATOM   1945 N  N     . GLY A 1 236 ? 3.788   44.334  12.963  1.00 73.86  ? 236 GLY A N     1 
ATOM   1946 C  CA    . GLY A 1 236 ? 2.453   43.794  12.825  1.00 69.91  ? 236 GLY A CA    1 
ATOM   1947 C  C     . GLY A 1 236 ? 2.365   42.497  12.052  1.00 73.25  ? 236 GLY A C     1 
ATOM   1948 O  O     . GLY A 1 236 ? 1.268   42.123  11.632  1.00 84.72  ? 236 GLY A O     1 
ATOM   1949 N  N     . SER A 1 237 ? 3.480   41.798  11.849  1.00 67.72  ? 237 SER A N     1 
ATOM   1950 C  CA    . SER A 1 237 ? 3.466   40.571  11.070  1.00 68.89  ? 237 SER A CA    1 
ATOM   1951 C  C     . SER A 1 237 ? 3.212   39.367  11.967  1.00 63.33  ? 237 SER A C     1 
ATOM   1952 O  O     . SER A 1 237 ? 3.188   39.458  13.196  1.00 63.01  ? 237 SER A O     1 
ATOM   1953 C  CB    . SER A 1 237 ? 4.790   40.369  10.330  1.00 74.78  ? 237 SER A CB    1 
ATOM   1954 O  OG    . SER A 1 237 ? 5.894   40.610  11.185  1.00 73.08  ? 237 SER A OG    1 
ATOM   1955 N  N     . GLU A 1 238 ? 3.058   38.223  11.333  1.00 60.15  ? 238 GLU A N     1 
ATOM   1956 C  CA    . GLU A 1 238 ? 2.909   36.951  12.004  1.00 65.51  ? 238 GLU A CA    1 
ATOM   1957 C  C     . GLU A 1 238 ? 4.244   36.228  12.060  1.00 76.64  ? 238 GLU A C     1 
ATOM   1958 O  O     . GLU A 1 238 ? 5.147   36.522  11.272  1.00 78.88  ? 238 GLU A O     1 
ATOM   1959 C  CB    . GLU A 1 238 ? 1.867   36.098  11.277  1.00 66.04  ? 238 GLU A CB    1 
ATOM   1960 C  CG    . GLU A 1 238 ? 0.482   36.722  11.294  1.00 78.90  ? 238 GLU A CG    1 
ATOM   1961 C  CD    . GLU A 1 238 ? -0.629  35.701  11.217  1.00 95.35  ? 238 GLU A CD    1 
ATOM   1962 O  OE1   . GLU A 1 238 ? -0.751  35.041  10.165  1.00 97.42  ? 238 GLU A OE1   1 
ATOM   1963 O  OE2   . GLU A 1 238 ? -1.384  35.566  12.204  1.00 93.92  ? 238 GLU A OE2   1 
ATOM   1964 N  N     . PRO A 1 239 ? 4.423   35.311  13.011  1.00 77.25  ? 239 PRO A N     1 
ATOM   1965 C  CA    . PRO A 1 239 ? 5.651   34.512  13.041  1.00 69.19  ? 239 PRO A CA    1 
ATOM   1966 C  C     . PRO A 1 239 ? 5.930   33.888  11.684  1.00 73.89  ? 239 PRO A C     1 
ATOM   1967 O  O     . PRO A 1 239 ? 5.048   33.291  11.062  1.00 79.98  ? 239 PRO A O     1 
ATOM   1968 C  CB    . PRO A 1 239 ? 5.347   33.450  14.104  1.00 72.86  ? 239 PRO A CB    1 
ATOM   1969 C  CG    . PRO A 1 239 ? 4.452   34.165  15.059  1.00 75.59  ? 239 PRO A CG    1 
ATOM   1970 C  CD    . PRO A 1 239 ? 3.598   35.091  14.214  1.00 75.06  ? 239 PRO A CD    1 
ATOM   1971 N  N     . LYS A 1 240 ? 7.160   34.058  11.212  1.00 65.41  ? 240 LYS A N     1 
ATOM   1972 C  CA    . LYS A 1 240 ? 7.562   33.612  9.886   1.00 68.90  ? 240 LYS A CA    1 
ATOM   1973 C  C     . LYS A 1 240 ? 8.340   32.309  9.999   1.00 78.11  ? 240 LYS A C     1 
ATOM   1974 O  O     . LYS A 1 240 ? 9.287   32.211  10.788  1.00 71.39  ? 240 LYS A O     1 
ATOM   1975 C  CB    . LYS A 1 240 ? 8.408   34.678  9.188   1.00 65.06  ? 240 LYS A CB    1 
ATOM   1976 C  CG    . LYS A 1 240 ? 8.813   34.315  7.770   1.00 75.20  ? 240 LYS A CG    1 
ATOM   1977 C  CD    . LYS A 1 240 ? 9.700   35.385  7.157   1.00 84.07  ? 240 LYS A CD    1 
ATOM   1978 C  CE    . LYS A 1 240 ? 9.413   35.549  5.673   1.00 91.96  ? 240 LYS A CE    1 
ATOM   1979 N  NZ    . LYS A 1 240 ? 9.241   36.980  5.297   1.00 96.14  ? 240 LYS A NZ    1 
ATOM   1980 N  N     . ILE A 1 241 ? 7.939   31.313  9.212   1.00 70.58  ? 241 ILE A N     1 
ATOM   1981 C  CA    . ILE A 1 241 ? 8.546   29.987  9.240   1.00 67.93  ? 241 ILE A CA    1 
ATOM   1982 C  C     . ILE A 1 241 ? 9.594   29.893  8.142   1.00 73.58  ? 241 ILE A C     1 
ATOM   1983 O  O     . ILE A 1 241 ? 9.359   30.310  7.000   1.00 79.10  ? 241 ILE A O     1 
ATOM   1984 C  CB    . ILE A 1 241 ? 7.483   28.882  9.086   1.00 73.51  ? 241 ILE A CB    1 
ATOM   1985 C  CG1   . ILE A 1 241 ? 6.150   29.317  9.708   1.00 83.92  ? 241 ILE A CG1   1 
ATOM   1986 C  CG2   . ILE A 1 241 ? 7.971   27.578  9.704   1.00 67.47  ? 241 ILE A CG2   1 
ATOM   1987 C  CD1   . ILE A 1 241 ? 6.147   29.347  11.228  1.00 74.53  ? 241 ILE A CD1   1 
ATOM   1988 N  N     . GLN A 1 242 ? 10.756  29.353  8.488   1.00 80.67  ? 242 GLN A N     1 
ATOM   1989 C  CA    . GLN A 1 242 ? 11.825  29.049  7.549   1.00 85.33  ? 242 GLN A CA    1 
ATOM   1990 C  C     . GLN A 1 242 ? 12.101  27.550  7.590   1.00 85.27  ? 242 GLN A C     1 
ATOM   1991 O  O     . GLN A 1 242 ? 11.460  26.801  8.329   1.00 89.95  ? 242 GLN A O     1 
ATOM   1992 C  CB    . GLN A 1 242 ? 13.084  29.862  7.866   1.00 68.15  ? 242 GLN A CB    1 
ATOM   1993 C  CG    . GLN A 1 242 ? 12.908  31.359  7.666   1.00 79.01  ? 242 GLN A CG    1 
ATOM   1994 C  CD    . GLN A 1 242 ? 13.256  31.803  6.258   1.00 108.48 ? 242 GLN A CD    1 
ATOM   1995 O  OE1   . GLN A 1 242 ? 12.733  32.803  5.762   1.00 128.79 ? 242 GLN A OE1   1 
ATOM   1996 N  NE2   . GLN A 1 242 ? 14.138  31.058  5.604   1.00 103.45 ? 242 GLN A NE2   1 
ATOM   1997 N  N     . ARG A 1 243 ? 13.062  27.109  6.784   1.00 88.26  ? 243 ARG A N     1 
ATOM   1998 C  CA    . ARG A 1 243 ? 13.416  25.694  6.692   1.00 100.84 ? 243 ARG A CA    1 
ATOM   1999 C  C     . ARG A 1 243 ? 14.877  25.527  7.096   1.00 100.89 ? 243 ARG A C     1 
ATOM   2000 O  O     . ARG A 1 243 ? 15.781  25.726  6.278   1.00 115.35 ? 243 ARG A O     1 
ATOM   2001 C  CB    . ARG A 1 243 ? 13.159  25.155  5.286   1.00 108.60 ? 243 ARG A CB    1 
ATOM   2002 C  CG    . ARG A 1 243 ? 11.830  24.433  5.136   1.00 108.45 ? 243 ARG A CG    1 
ATOM   2003 C  CD    . ARG A 1 243 ? 11.768  23.638  3.836   1.00 123.18 ? 243 ARG A CD    1 
ATOM   2004 N  NE    . ARG A 1 243 ? 11.013  22.393  3.952   1.00 132.59 ? 243 ARG A NE    1 
ATOM   2005 C  CZ    . ARG A 1 243 ? 11.311  21.388  4.767   1.00 121.98 ? 243 ARG A CZ    1 
ATOM   2006 N  NH1   . ARG A 1 243 ? 12.402  21.400  5.518   1.00 115.09 ? 243 ARG A NH1   1 
ATOM   2007 N  NH2   . ARG A 1 243 ? 10.497  20.338  4.824   1.00 111.72 ? 243 ARG A NH2   1 
ATOM   2008 N  N     . MET A 1 244 ? 15.105  25.165  8.360   1.00 94.80  ? 244 MET A N     1 
ATOM   2009 C  CA    . MET A 1 244 ? 16.446  24.839  8.847   1.00 106.84 ? 244 MET A CA    1 
ATOM   2010 C  C     . MET A 1 244 ? 16.671  23.344  8.642   1.00 110.95 ? 244 MET A C     1 
ATOM   2011 O  O     . MET A 1 244 ? 16.558  22.526  9.559   1.00 107.09 ? 244 MET A O     1 
ATOM   2012 C  CB    . MET A 1 244 ? 16.608  25.238  10.309  1.00 98.73  ? 244 MET A CB    1 
ATOM   2013 C  CG    . MET A 1 244 ? 16.905  26.712  10.523  1.00 88.28  ? 244 MET A CG    1 
ATOM   2014 S  SD    . MET A 1 244 ? 18.512  27.218  9.883   1.00 120.58 ? 244 MET A SD    1 
ATOM   2015 C  CE    . MET A 1 244 ? 18.011  28.237  8.497   1.00 102.25 ? 244 MET A CE    1 
ATOM   2016 N  N     . GLY A 1 245 ? 16.992  22.987  7.399   1.00 105.83 ? 245 GLY A N     1 
ATOM   2017 C  CA    . GLY A 1 245 ? 17.168  21.590  7.052   1.00 107.41 ? 245 GLY A CA    1 
ATOM   2018 C  C     . GLY A 1 245 ? 15.843  20.847  6.993   1.00 117.78 ? 245 GLY A C     1 
ATOM   2019 O  O     . GLY A 1 245 ? 14.813  21.379  6.565   1.00 125.95 ? 245 GLY A O     1 
ATOM   2020 N  N     . ASP A 1 246 ? 15.879  19.584  7.429   1.00 122.09 ? 246 ASP A N     1 
ATOM   2021 C  CA    . ASP A 1 246 ? 14.660  18.782  7.492   1.00 126.07 ? 246 ASP A CA    1 
ATOM   2022 C  C     . ASP A 1 246 ? 13.622  19.434  8.396   1.00 124.96 ? 246 ASP A C     1 
ATOM   2023 O  O     . ASP A 1 246 ? 12.423  19.423  8.091   1.00 124.50 ? 246 ASP A O     1 
ATOM   2024 C  CB    . ASP A 1 246 ? 14.988  17.370  7.981   1.00 143.56 ? 246 ASP A CB    1 
ATOM   2025 C  CG    . ASP A 1 246 ? 15.509  16.472  6.873   1.00 160.41 ? 246 ASP A CG    1 
ATOM   2026 O  OD1   . ASP A 1 246 ? 15.700  16.968  5.744   1.00 163.56 ? 246 ASP A OD1   1 
ATOM   2027 O  OD2   . ASP A 1 246 ? 15.725  15.268  7.131   1.00 162.10 ? 246 ASP A OD2   1 
ATOM   2028 N  N     . ARG A 1 247 ? 14.064  20.014  9.509   1.00 123.01 ? 247 ARG A N     1 
ATOM   2029 C  CA    . ARG A 1 247 ? 13.183  20.701  10.437  1.00 113.03 ? 247 ARG A CA    1 
ATOM   2030 C  C     . ARG A 1 247 ? 13.117  22.187  10.086  1.00 105.42 ? 247 ARG A C     1 
ATOM   2031 O  O     . ARG A 1 247 ? 13.729  22.652  9.122   1.00 108.08 ? 247 ARG A O     1 
ATOM   2032 C  CB    . ARG A 1 247 ? 13.657  20.479  11.870  1.00 116.70 ? 247 ARG A CB    1 
ATOM   2033 C  CG    . ARG A 1 247 ? 13.816  19.016  12.241  1.00 121.08 ? 247 ARG A CG    1 
ATOM   2034 C  CD    . ARG A 1 247 ? 15.003  18.829  13.168  1.00 133.45 ? 247 ARG A CD    1 
ATOM   2035 N  NE    . ARG A 1 247 ? 16.078  19.760  12.849  1.00 141.88 ? 247 ARG A NE    1 
ATOM   2036 C  CZ    . ARG A 1 247 ? 17.159  19.948  13.594  1.00 150.60 ? 247 ARG A CZ    1 
ATOM   2037 N  NH1   . ARG A 1 247 ? 17.349  19.277  14.718  1.00 152.90 ? 247 ARG A NH1   1 
ATOM   2038 N  NH2   . ARG A 1 247 ? 18.071  20.834  13.203  1.00 144.16 ? 247 ARG A NH2   1 
ATOM   2039 N  N     . PHE A 1 248 ? 12.354  22.945  10.870  1.00 84.44  ? 248 PHE A N     1 
ATOM   2040 C  CA    . PHE A 1 248 ? 12.060  24.340  10.570  1.00 85.51  ? 248 PHE A CA    1 
ATOM   2041 C  C     . PHE A 1 248 ? 12.516  25.238  11.715  1.00 79.64  ? 248 PHE A C     1 
ATOM   2042 O  O     . PHE A 1 248 ? 12.878  24.774  12.799  1.00 76.56  ? 248 PHE A O     1 
ATOM   2043 C  CB    . PHE A 1 248 ? 10.559  24.552  10.314  1.00 89.43  ? 248 PHE A CB    1 
ATOM   2044 C  CG    . PHE A 1 248 ? 9.929   23.511  9.423   1.00 92.01  ? 248 PHE A CG    1 
ATOM   2045 C  CD1   . PHE A 1 248 ? 8.606   23.146  9.607   1.00 87.37  ? 248 PHE A CD1   1 
ATOM   2046 C  CD2   . PHE A 1 248 ? 10.641  22.927  8.386   1.00 106.05 ? 248 PHE A CD2   1 
ATOM   2047 C  CE1   . PHE A 1 248 ? 8.011   22.198  8.796   1.00 94.78  ? 248 PHE A CE1   1 
ATOM   2048 C  CE2   . PHE A 1 248 ? 10.057  21.973  7.578   1.00 112.71 ? 248 PHE A CE2   1 
ATOM   2049 C  CZ    . PHE A 1 248 ? 8.741   21.611  7.776   1.00 95.96  ? 248 PHE A CZ    1 
ATOM   2050 N  N     . ALA A 1 249 ? 12.492  26.545  11.452  1.00 73.41  ? 249 ALA A N     1 
ATOM   2051 C  CA    . ALA A 1 249 ? 12.774  27.566  12.450  1.00 69.23  ? 249 ALA A CA    1 
ATOM   2052 C  C     . ALA A 1 249 ? 11.812  28.727  12.252  1.00 62.67  ? 249 ALA A C     1 
ATOM   2053 O  O     . ALA A 1 249 ? 11.336  28.972  11.141  1.00 64.06  ? 249 ALA A O     1 
ATOM   2054 C  CB    . ALA A 1 249 ? 14.222  28.063  12.371  1.00 57.33  ? 249 ALA A CB    1 
ATOM   2055 N  N     . VAL A 1 250 ? 11.535  29.448  13.337  1.00 57.25  ? 250 VAL A N     1 
ATOM   2056 C  CA    . VAL A 1 250 ? 10.515  30.490  13.353  1.00 62.58  ? 250 VAL A CA    1 
ATOM   2057 C  C     . VAL A 1 250 ? 11.170  31.830  13.657  1.00 61.01  ? 250 VAL A C     1 
ATOM   2058 O  O     . VAL A 1 250 ? 11.875  31.973  14.664  1.00 60.22  ? 250 VAL A O     1 
ATOM   2059 C  CB    . VAL A 1 250 ? 9.408   30.182  14.377  1.00 60.45  ? 250 VAL A CB    1 
ATOM   2060 C  CG1   . VAL A 1 250 ? 8.427   31.338  14.466  1.00 62.68  ? 250 VAL A CG1   1 
ATOM   2061 C  CG2   . VAL A 1 250 ? 8.689   28.896  14.000  1.00 52.61  ? 250 VAL A CG2   1 
ATOM   2062 N  N     . GLU A 1 251 ? 10.923  32.808  12.792  1.00 62.67  ? 251 GLU A N     1 
ATOM   2063 C  CA    . GLU A 1 251 ? 11.376  34.179  12.963  1.00 50.06  ? 251 GLU A CA    1 
ATOM   2064 C  C     . GLU A 1 251 ? 10.210  35.051  13.412  1.00 67.18  ? 251 GLU A C     1 
ATOM   2065 O  O     . GLU A 1 251 ? 9.056   34.805  13.051  1.00 73.16  ? 251 GLU A O     1 
ATOM   2066 C  CB    . GLU A 1 251 ? 11.952  34.718  11.651  1.00 49.24  ? 251 GLU A CB    1 
ATOM   2067 C  CG    . GLU A 1 251 ? 13.286  35.425  11.775  1.00 74.04  ? 251 GLU A CG    1 
ATOM   2068 C  CD    . GLU A 1 251 ? 13.887  35.746  10.419  1.00 81.71  ? 251 GLU A CD    1 
ATOM   2069 O  OE1   . GLU A 1 251 ? 13.260  35.393  9.397   1.00 64.95  ? 251 GLU A OE1   1 
ATOM   2070 O  OE2   . GLU A 1 251 ? 14.983  36.346  10.375  1.00 72.46  ? 251 GLU A OE2   1 
ATOM   2071 N  N     . VAL A 1 252 ? 10.517  36.072  14.208  1.00 64.62  ? 252 VAL A N     1 
ATOM   2072 C  CA    . VAL A 1 252 ? 9.532   37.055  14.656  1.00 43.09  ? 252 VAL A CA    1 
ATOM   2073 C  C     . VAL A 1 252 ? 10.118  38.426  14.340  1.00 49.43  ? 252 VAL A C     1 
ATOM   2074 O  O     . VAL A 1 252 ? 11.007  38.906  15.052  1.00 56.99  ? 252 VAL A O     1 
ATOM   2075 C  CB    . VAL A 1 252 ? 9.196   36.920  16.146  1.00 60.82  ? 252 VAL A CB    1 
ATOM   2076 C  CG1   . VAL A 1 252 ? 8.148   37.947  16.553  1.00 62.81  ? 252 VAL A CG1   1 
ATOM   2077 C  CG2   . VAL A 1 252 ? 8.706   35.513  16.455  1.00 53.37  ? 252 VAL A CG2   1 
ATOM   2078 N  N     . LYS A 1 253 ? 9.620   39.059  13.277  1.00 53.41  ? 253 LYS A N     1 
ATOM   2079 C  CA    . LYS A 1 253 ? 10.223  40.283  12.761  1.00 55.34  ? 253 LYS A CA    1 
ATOM   2080 C  C     . LYS A 1 253 ? 10.260  41.377  13.821  1.00 61.66  ? 253 LYS A C     1 
ATOM   2081 O  O     . LYS A 1 253 ? 9.304   41.571  14.578  1.00 66.23  ? 253 LYS A O     1 
ATOM   2082 C  CB    . LYS A 1 253 ? 9.454   40.771  11.532  1.00 48.75  ? 253 LYS A CB    1 
ATOM   2083 C  CG    . LYS A 1 253 ? 9.601   39.865  10.321  1.00 53.90  ? 253 LYS A CG    1 
ATOM   2084 C  CD    . LYS A 1 253 ? 11.034  39.862  9.820   1.00 65.89  ? 253 LYS A CD    1 
ATOM   2085 C  CE    . LYS A 1 253 ? 11.385  38.540  9.161   1.00 63.80  ? 253 LYS A CE    1 
ATOM   2086 N  NZ    . LYS A 1 253 ? 12.171  38.736  7.912   1.00 62.87  ? 253 LYS A NZ    1 
ATOM   2087 N  N     . GLY A 1 254 ? 11.381  42.101  13.864  1.00 61.63  ? 254 GLY A N     1 
ATOM   2088 C  CA    . GLY A 1 254 ? 11.610  43.114  14.868  1.00 58.04  ? 254 GLY A CA    1 
ATOM   2089 C  C     . GLY A 1 254 ? 12.106  42.589  16.196  1.00 54.48  ? 254 GLY A C     1 
ATOM   2090 O  O     . GLY A 1 254 ? 12.500  43.392  17.052  1.00 61.21  ? 254 GLY A O     1 
ATOM   2091 N  N     . ARG A 1 255 ? 12.094  41.274  16.402  1.00 60.72  ? 255 ARG A N     1 
ATOM   2092 C  CA    . ARG A 1 255 ? 12.561  40.646  17.628  1.00 54.22  ? 255 ARG A CA    1 
ATOM   2093 C  C     . ARG A 1 255 ? 13.455  39.466  17.272  1.00 65.17  ? 255 ARG A C     1 
ATOM   2094 O  O     . ARG A 1 255 ? 13.566  39.067  16.110  1.00 74.11  ? 255 ARG A O     1 
ATOM   2095 C  CB    . ARG A 1 255 ? 11.390  40.178  18.505  1.00 60.38  ? 255 ARG A CB    1 
ATOM   2096 C  CG    . ARG A 1 255 ? 10.042  40.741  18.088  1.00 68.40  ? 255 ARG A CG    1 
ATOM   2097 C  CD    . ARG A 1 255 ? 8.953   40.436  19.100  1.00 65.83  ? 255 ARG A CD    1 
ATOM   2098 N  NE    . ARG A 1 255 ? 8.704   41.570  19.980  1.00 76.23  ? 255 ARG A NE    1 
ATOM   2099 C  CZ    . ARG A 1 255 ? 7.563   42.244  20.027  1.00 70.46  ? 255 ARG A CZ    1 
ATOM   2100 N  NH1   . ARG A 1 255 ? 6.535   41.916  19.261  1.00 63.45  ? 255 ARG A NH1   1 
ATOM   2101 N  NH2   . ARG A 1 255 ? 7.450   43.272  20.861  1.00 79.63  ? 255 ARG A NH2   1 
ATOM   2102 N  N     . ILE A 1 256 ? 14.094  38.901  18.290  1.00 63.08  ? 256 ILE A N     1 
ATOM   2103 C  CA    . ILE A 1 256 ? 14.948  37.731  18.134  1.00 62.22  ? 256 ILE A CA    1 
ATOM   2104 C  C     . ILE A 1 256 ? 14.259  36.571  18.835  1.00 53.78  ? 256 ILE A C     1 
ATOM   2105 O  O     . ILE A 1 256 ? 14.165  36.545  20.069  1.00 52.36  ? 256 ILE A O     1 
ATOM   2106 C  CB    . ILE A 1 256 ? 16.356  37.965  18.697  1.00 61.65  ? 256 ILE A CB    1 
ATOM   2107 C  CG1   . ILE A 1 256 ? 17.120  38.974  17.834  1.00 66.85  ? 256 ILE A CG1   1 
ATOM   2108 C  CG2   . ILE A 1 256 ? 17.125  36.651  18.793  1.00 62.99  ? 256 ILE A CG2   1 
ATOM   2109 C  CD1   . ILE A 1 256 ? 17.872  38.356  16.659  1.00 70.65  ? 256 ILE A CD1   1 
ATOM   2110 N  N     . HIS A 1 257 ? 13.758  35.617  18.057  1.00 59.15  ? 257 HIS A N     1 
ATOM   2111 C  CA    . HIS A 1 257 ? 13.257  34.377  18.631  1.00 58.24  ? 257 HIS A CA    1 
ATOM   2112 C  C     . HIS A 1 257 ? 14.450  33.510  19.004  1.00 56.89  ? 257 HIS A C     1 
ATOM   2113 O  O     . HIS A 1 257 ? 15.232  33.115  18.134  1.00 59.73  ? 257 HIS A O     1 
ATOM   2114 C  CB    . HIS A 1 257 ? 12.343  33.640  17.657  1.00 55.07  ? 257 HIS A CB    1 
ATOM   2115 C  CG    . HIS A 1 257 ? 11.980  32.261  18.112  1.00 52.03  ? 257 HIS A CG    1 
ATOM   2116 N  ND1   . HIS A 1 257 ? 11.740  31.223  17.237  1.00 55.46  ? 257 HIS A ND1   1 
ATOM   2117 C  CD2   . HIS A 1 257 ? 11.823  31.747  19.355  1.00 47.26  ? 257 HIS A CD2   1 
ATOM   2118 C  CE1   . HIS A 1 257 ? 11.449  30.132  17.921  1.00 56.58  ? 257 HIS A CE1   1 
ATOM   2119 N  NE2   . HIS A 1 257 ? 11.494  30.422  19.209  1.00 55.44  ? 257 HIS A NE2   1 
ATOM   2120 N  N     . PHE A 1 258 ? 14.596  33.228  20.291  1.00 60.87  ? 258 PHE A N     1 
ATOM   2121 C  CA    . PHE A 1 258 ? 15.709  32.441  20.808  1.00 55.24  ? 258 PHE A CA    1 
ATOM   2122 C  C     . PHE A 1 258 ? 15.158  31.090  21.260  1.00 63.91  ? 258 PHE A C     1 
ATOM   2123 O  O     . PHE A 1 258 ? 14.681  30.944  22.387  1.00 70.17  ? 258 PHE A O     1 
ATOM   2124 C  CB    . PHE A 1 258 ? 16.409  33.171  21.952  1.00 57.83  ? 258 PHE A CB    1 
ATOM   2125 C  CG    . PHE A 1 258 ? 17.747  32.593  22.312  1.00 64.28  ? 258 PHE A CG    1 
ATOM   2126 C  CD1   . PHE A 1 258 ? 18.663  32.266  21.327  1.00 67.21  ? 258 PHE A CD1   1 
ATOM   2127 C  CD2   . PHE A 1 258 ? 18.081  32.361  23.636  1.00 66.52  ? 258 PHE A CD2   1 
ATOM   2128 C  CE1   . PHE A 1 258 ? 19.893  31.732  21.657  1.00 67.56  ? 258 PHE A CE1   1 
ATOM   2129 C  CE2   . PHE A 1 258 ? 19.309  31.828  23.972  1.00 66.24  ? 258 PHE A CE2   1 
ATOM   2130 C  CZ    . PHE A 1 258 ? 20.214  31.511  22.981  1.00 71.98  ? 258 PHE A CZ    1 
ATOM   2131 N  N     . ASP A 1 259 ? 15.211  30.105  20.365  1.00 59.13  ? 259 ASP A N     1 
ATOM   2132 C  CA    . ASP A 1 259 ? 14.904  28.728  20.735  1.00 47.47  ? 259 ASP A CA    1 
ATOM   2133 C  C     . ASP A 1 259 ? 16.134  28.144  21.414  1.00 69.84  ? 259 ASP A C     1 
ATOM   2134 O  O     . ASP A 1 259 ? 17.184  27.985  20.783  1.00 65.44  ? 259 ASP A O     1 
ATOM   2135 C  CB    . ASP A 1 259 ? 14.505  27.902  19.516  1.00 49.08  ? 259 ASP A CB    1 
ATOM   2136 C  CG    . ASP A 1 259 ? 13.960  26.532  19.893  1.00 65.72  ? 259 ASP A CG    1 
ATOM   2137 O  OD1   . ASP A 1 259 ? 14.089  26.133  21.069  1.00 60.52  ? 259 ASP A OD1   1 
ATOM   2138 O  OD2   . ASP A 1 259 ? 13.400  25.850  19.011  1.00 70.25  ? 259 ASP A OD2   1 
ATOM   2139 N  N     . LEU A 1 260 ? 16.010  27.835  22.705  1.00 66.37  ? 260 LEU A N     1 
ATOM   2140 C  CA    . LEU A 1 260 ? 17.143  27.303  23.449  1.00 69.50  ? 260 LEU A CA    1 
ATOM   2141 C  C     . LEU A 1 260 ? 17.528  25.901  23.001  1.00 70.69  ? 260 LEU A C     1 
ATOM   2142 O  O     . LEU A 1 260 ? 18.679  25.501  23.205  1.00 73.69  ? 260 LEU A O     1 
ATOM   2143 C  CB    . LEU A 1 260 ? 16.833  27.294  24.946  1.00 61.70  ? 260 LEU A CB    1 
ATOM   2144 C  CG    . LEU A 1 260 ? 16.837  28.634  25.681  1.00 53.57  ? 260 LEU A CG    1 
ATOM   2145 C  CD1   . LEU A 1 260 ? 15.947  28.560  26.912  1.00 58.98  ? 260 LEU A CD1   1 
ATOM   2146 C  CD2   . LEU A 1 260 ? 18.252  29.030  26.065  1.00 62.69  ? 260 LEU A CD2   1 
ATOM   2147 N  N     . TYR A 1 261 ? 16.604  25.156  22.391  1.00 64.10  ? 261 TYR A N     1 
ATOM   2148 C  CA    . TYR A 1 261 ? 16.867  23.748  22.097  1.00 67.05  ? 261 TYR A CA    1 
ATOM   2149 C  C     . TYR A 1 261 ? 18.100  23.536  21.228  1.00 70.01  ? 261 TYR A C     1 
ATOM   2150 O  O     . TYR A 1 261 ? 18.957  22.721  21.610  1.00 73.72  ? 261 TYR A O     1 
ATOM   2151 C  CB    . TYR A 1 261 ? 15.622  23.102  21.480  1.00 65.65  ? 261 TYR A CB    1 
ATOM   2152 C  CG    . TYR A 1 261 ? 15.725  21.599  21.396  1.00 67.92  ? 261 TYR A CG    1 
ATOM   2153 C  CD1   . TYR A 1 261 ? 15.358  20.799  22.470  1.00 76.25  ? 261 TYR A CD1   1 
ATOM   2154 C  CD2   . TYR A 1 261 ? 16.194  20.980  20.247  1.00 72.93  ? 261 TYR A CD2   1 
ATOM   2155 C  CE1   . TYR A 1 261 ? 15.456  19.424  22.400  1.00 89.49  ? 261 TYR A CE1   1 
ATOM   2156 C  CE2   . TYR A 1 261 ? 16.292  19.608  20.165  1.00 85.33  ? 261 TYR A CE2   1 
ATOM   2157 C  CZ    . TYR A 1 261 ? 15.924  18.833  21.244  1.00 94.78  ? 261 TYR A CZ    1 
ATOM   2158 O  OH    . TYR A 1 261 ? 16.024  17.464  21.164  1.00 96.59  ? 261 TYR A OH    1 
ATOM   2159 N  N     . PRO A 1 262 ? 18.270  24.206  20.081  1.00 75.24  ? 262 PRO A N     1 
ATOM   2160 C  CA    . PRO A 1 262 ? 19.529  24.027  19.338  1.00 69.10  ? 262 PRO A CA    1 
ATOM   2161 C  C     . PRO A 1 262 ? 20.746  24.495  20.113  1.00 65.61  ? 262 PRO A C     1 
ATOM   2162 O  O     . PRO A 1 262 ? 21.827  23.910  19.970  1.00 72.84  ? 262 PRO A O     1 
ATOM   2163 C  CB    . PRO A 1 262 ? 19.313  24.861  18.067  1.00 53.35  ? 262 PRO A CB    1 
ATOM   2164 C  CG    . PRO A 1 262 ? 18.246  25.830  18.419  1.00 60.12  ? 262 PRO A CG    1 
ATOM   2165 C  CD    . PRO A 1 262 ? 17.347  25.111  19.370  1.00 64.68  ? 262 PRO A CD    1 
ATOM   2166 N  N     . VAL A 1 263 ? 20.598  25.526  20.946  1.00 69.51  ? 263 VAL A N     1 
ATOM   2167 C  CA    . VAL A 1 263 ? 21.741  26.062  21.676  1.00 76.18  ? 263 VAL A CA    1 
ATOM   2168 C  C     . VAL A 1 263 ? 22.210  25.077  22.741  1.00 75.87  ? 263 VAL A C     1 
ATOM   2169 O  O     . VAL A 1 263 ? 23.416  24.873  22.925  1.00 72.80  ? 263 VAL A O     1 
ATOM   2170 C  CB    . VAL A 1 263 ? 21.384  27.431  22.281  1.00 62.84  ? 263 VAL A CB    1 
ATOM   2171 C  CG1   . VAL A 1 263 ? 22.483  27.909  23.218  1.00 67.62  ? 263 VAL A CG1   1 
ATOM   2172 C  CG2   . VAL A 1 263 ? 21.142  28.444  21.176  1.00 64.98  ? 263 VAL A CG2   1 
ATOM   2173 N  N     . ILE A 1 264 ? 21.271  24.440  23.446  1.00 75.24  ? 264 ILE A N     1 
ATOM   2174 C  CA    . ILE A 1 264 ? 21.634  23.556  24.554  1.00 75.18  ? 264 ILE A CA    1 
ATOM   2175 C  C     . ILE A 1 264 ? 22.404  22.345  24.042  1.00 74.28  ? 264 ILE A C     1 
ATOM   2176 O  O     . ILE A 1 264 ? 23.530  22.073  24.477  1.00 81.73  ? 264 ILE A O     1 
ATOM   2177 C  CB    . ILE A 1 264 ? 20.383  23.127  25.338  1.00 79.74  ? 264 ILE A CB    1 
ATOM   2178 C  CG1   . ILE A 1 264 ? 19.699  24.339  25.970  1.00 70.82  ? 264 ILE A CG1   1 
ATOM   2179 C  CG2   . ILE A 1 264 ? 20.755  22.110  26.407  1.00 78.73  ? 264 ILE A CG2   1 
ATOM   2180 C  CD1   . ILE A 1 264 ? 20.643  25.263  26.684  1.00 64.67  ? 264 ILE A CD1   1 
ATOM   2181 N  N     . ARG A 1 265 ? 21.797  21.591  23.119  1.00 74.57  ? 265 ARG A N     1 
ATOM   2182 C  CA    . ARG A 1 265 ? 22.423  20.373  22.607  1.00 78.27  ? 265 ARG A CA    1 
ATOM   2183 C  C     . ARG A 1 265 ? 23.817  20.644  22.063  1.00 83.59  ? 265 ARG A C     1 
ATOM   2184 O  O     . ARG A 1 265 ? 24.756  19.884  22.322  1.00 102.05 ? 265 ARG A O     1 
ATOM   2185 C  CB    . ARG A 1 265 ? 21.554  19.756  21.511  1.00 83.51  ? 265 ARG A CB    1 
ATOM   2186 C  CG    . ARG A 1 265 ? 20.071  19.753  21.803  1.00 85.92  ? 265 ARG A CG    1 
ATOM   2187 C  CD    . ARG A 1 265 ? 19.400  18.603  21.081  1.00 98.26  ? 265 ARG A CD    1 
ATOM   2188 N  NE    . ARG A 1 265 ? 20.240  17.411  21.056  1.00 112.27 ? 265 ARG A NE    1 
ATOM   2189 C  CZ    . ARG A 1 265 ? 20.104  16.418  20.189  1.00 128.11 ? 265 ARG A CZ    1 
ATOM   2190 N  NH1   . ARG A 1 265 ? 19.175  16.445  19.247  1.00 107.03 ? 265 ARG A NH1   1 
ATOM   2191 N  NH2   . ARG A 1 265 ? 20.922  15.372  20.267  1.00 127.36 ? 265 ARG A NH2   1 
ATOM   2192 N  N     . ARG A 1 266 ? 23.968  21.727  21.303  1.00 82.49  ? 266 ARG A N     1 
ATOM   2193 C  CA    . ARG A 1 266 ? 25.256  22.060  20.714  1.00 74.77  ? 266 ARG A CA    1 
ATOM   2194 C  C     . ARG A 1 266 ? 26.280  22.474  21.769  1.00 71.94  ? 266 ARG A C     1 
ATOM   2195 O  O     . ARG A 1 266 ? 27.486  22.390  21.512  1.00 82.88  ? 266 ARG A O     1 
ATOM   2196 C  CB    . ARG A 1 266 ? 25.038  23.154  19.662  1.00 68.04  ? 266 ARG A CB    1 
ATOM   2197 C  CG    . ARG A 1 266 ? 26.139  24.173  19.500  1.00 80.64  ? 266 ARG A CG    1 
ATOM   2198 C  CD    . ARG A 1 266 ? 25.710  25.267  18.542  1.00 90.93  ? 266 ARG A CD    1 
ATOM   2199 N  NE    . ARG A 1 266 ? 25.264  26.433  19.291  1.00 85.90  ? 266 ARG A NE    1 
ATOM   2200 C  CZ    . ARG A 1 266 ? 26.075  27.282  19.904  1.00 102.09 ? 266 ARG A CZ    1 
ATOM   2201 N  NH1   . ARG A 1 266 ? 27.390  27.178  19.807  1.00 102.82 ? 266 ARG A NH1   1 
ATOM   2202 N  NH2   . ARG A 1 266 ? 25.554  28.257  20.636  1.00 90.43  ? 266 ARG A NH2   1 
ATOM   2203 N  N     . THR A 1 267 ? 25.832  22.869  22.961  1.00 78.02  ? 267 THR A N     1 
ATOM   2204 C  CA    . THR A 1 267 ? 26.718  23.358  24.013  1.00 72.26  ? 267 THR A CA    1 
ATOM   2205 C  C     . THR A 1 267 ? 26.978  22.322  25.101  1.00 81.83  ? 267 THR A C     1 
ATOM   2206 O  O     . THR A 1 267 ? 28.132  22.097  25.481  1.00 86.57  ? 267 THR A O     1 
ATOM   2207 C  CB    . THR A 1 267 ? 26.131  24.635  24.633  1.00 75.41  ? 267 THR A CB    1 
ATOM   2208 O  OG1   . THR A 1 267 ? 26.452  25.756  23.801  1.00 90.83  ? 267 THR A OG1   1 
ATOM   2209 C  CG2   . THR A 1 267 ? 26.694  24.874  26.028  1.00 72.68  ? 267 THR A CG2   1 
ATOM   2210 N  N     . ILE A 1 268 ? 25.932  21.679  25.608  1.00 86.39  ? 268 ILE A N     1 
ATOM   2211 C  CA    . ILE A 1 268 ? 26.057  20.735  26.712  1.00 78.89  ? 268 ILE A CA    1 
ATOM   2212 C  C     . ILE A 1 268 ? 25.939  19.313  26.178  1.00 74.47  ? 268 ILE A C     1 
ATOM   2213 O  O     . ILE A 1 268 ? 25.237  19.049  25.195  1.00 87.67  ? 268 ILE A O     1 
ATOM   2214 C  CB    . ILE A 1 268 ? 24.998  21.027  27.800  1.00 75.05  ? 268 ILE A CB    1 
ATOM   2215 C  CG1   . ILE A 1 268 ? 25.359  22.279  28.583  1.00 85.79  ? 268 ILE A CG1   1 
ATOM   2216 C  CG2   . ILE A 1 268 ? 24.914  19.927  28.821  1.00 86.90  ? 268 ILE A CG2   1 
ATOM   2217 C  CD1   . ILE A 1 268 ? 24.297  22.643  29.581  1.00 88.35  ? 268 ILE A CD1   1 
ATOM   2218 N  N     . ASN A 1 269 ? 26.653  18.387  26.819  1.00 79.33  ? 269 ASN A N     1 
ATOM   2219 C  CA    . ASN A 1 269 ? 26.587  16.961  26.505  1.00 78.64  ? 269 ASN A CA    1 
ATOM   2220 C  C     . ASN A 1 269 ? 25.760  16.274  27.590  1.00 79.65  ? 269 ASN A C     1 
ATOM   2221 O  O     . ASN A 1 269 ? 26.258  16.022  28.691  1.00 85.85  ? 269 ASN A O     1 
ATOM   2222 C  CB    . ASN A 1 269 ? 27.988  16.361  26.409  1.00 85.34  ? 269 ASN A CB    1 
ATOM   2223 C  CG    . ASN A 1 269 ? 27.999  15.022  25.699  1.00 92.92  ? 269 ASN A CG    1 
ATOM   2224 O  OD1   . ASN A 1 269 ? 27.712  13.987  26.299  1.00 95.41  ? 269 ASN A OD1   1 
ATOM   2225 N  ND2   . ASN A 1 269 ? 28.327  15.038  24.413  1.00 91.80  ? 269 ASN A ND2   1 
ATOM   2226 N  N     . LEU A 1 270 ? 24.499  15.976  27.279  1.00 84.86  ? 270 LEU A N     1 
ATOM   2227 C  CA    . LEU A 1 270 ? 23.585  15.290  28.181  1.00 71.40  ? 270 LEU A CA    1 
ATOM   2228 C  C     . LEU A 1 270 ? 23.024  14.038  27.524  1.00 74.97  ? 270 LEU A C     1 
ATOM   2229 O  O     . LEU A 1 270 ? 22.822  14.006  26.306  1.00 80.07  ? 270 LEU A O     1 
ATOM   2230 C  CB    . LEU A 1 270 ? 22.415  16.196  28.597  1.00 74.61  ? 270 LEU A CB    1 
ATOM   2231 C  CG    . LEU A 1 270 ? 22.715  17.364  29.538  1.00 75.70  ? 270 LEU A CG    1 
ATOM   2232 C  CD1   . LEU A 1 270 ? 21.431  17.984  30.071  1.00 62.62  ? 270 LEU A CD1   1 
ATOM   2233 C  CD2   . LEU A 1 270 ? 23.625  16.930  30.678  1.00 69.91  ? 270 LEU A CD2   1 
ATOM   2234 N  N     . PRO A 1 271 ? 22.761  12.989  28.309  1.00 71.04  ? 271 PRO A N     1 
ATOM   2235 C  CA    . PRO A 1 271 ? 22.097  11.804  27.739  1.00 69.01  ? 271 PRO A CA    1 
ATOM   2236 C  C     . PRO A 1 271 ? 20.692  12.093  27.240  1.00 75.88  ? 271 PRO A C     1 
ATOM   2237 O  O     . PRO A 1 271 ? 20.264  11.501  26.242  1.00 79.07  ? 271 PRO A O     1 
ATOM   2238 C  CB    . PRO A 1 271 ? 22.094  10.803  28.904  1.00 73.71  ? 271 PRO A CB    1 
ATOM   2239 C  CG    . PRO A 1 271 ? 22.298  11.629  30.133  1.00 75.06  ? 271 PRO A CG    1 
ATOM   2240 C  CD    . PRO A 1 271 ? 23.124  12.804  29.724  1.00 59.96  ? 271 PRO A CD    1 
ATOM   2241 N  N     . THR A 1 272 ? 19.963  12.989  27.902  1.00 71.87  ? 272 THR A N     1 
ATOM   2242 C  CA    . THR A 1 272 ? 18.646  13.419  27.459  1.00 79.07  ? 272 THR A CA    1 
ATOM   2243 C  C     . THR A 1 272 ? 18.573  14.937  27.512  1.00 78.71  ? 272 THR A C     1 
ATOM   2244 O  O     . THR A 1 272 ? 19.190  15.574  28.371  1.00 77.26  ? 272 THR A O     1 
ATOM   2245 C  CB    . THR A 1 272 ? 17.524  12.817  28.318  1.00 60.55  ? 272 THR A CB    1 
ATOM   2246 O  OG1   . THR A 1 272 ? 17.958  12.726  29.681  1.00 88.26  ? 272 THR A OG1   1 
ATOM   2247 C  CG2   . THR A 1 272 ? 17.154  11.432  27.815  1.00 65.31  ? 272 THR A CG2   1 
ATOM   2248 N  N     . TYR A 1 273 ? 17.815  15.514  26.585  1.00 72.81  ? 273 TYR A N     1 
ATOM   2249 C  CA    . TYR A 1 273 ? 17.687  16.960  26.468  1.00 70.02  ? 273 TYR A CA    1 
ATOM   2250 C  C     . TYR A 1 273 ? 16.249  17.411  26.693  1.00 81.53  ? 273 TYR A C     1 
ATOM   2251 O  O     . TYR A 1 273 ? 15.730  18.276  25.985  1.00 84.80  ? 273 TYR A O     1 
ATOM   2252 C  CB    . TYR A 1 273 ? 18.203  17.445  25.116  1.00 76.99  ? 273 TYR A CB    1 
ATOM   2253 C  CG    . TYR A 1 273 ? 19.697  17.286  24.947  1.00 80.73  ? 273 TYR A CG    1 
ATOM   2254 C  CD1   . TYR A 1 273 ? 20.583  18.128  25.606  1.00 79.14  ? 273 TYR A CD1   1 
ATOM   2255 C  CD2   . TYR A 1 273 ? 20.221  16.296  24.128  1.00 84.61  ? 273 TYR A CD2   1 
ATOM   2256 C  CE1   . TYR A 1 273 ? 21.950  17.988  25.454  1.00 78.64  ? 273 TYR A CE1   1 
ATOM   2257 C  CE2   . TYR A 1 273 ? 21.585  16.148  23.970  1.00 84.59  ? 273 TYR A CE2   1 
ATOM   2258 C  CZ    . TYR A 1 273 ? 22.445  16.995  24.634  1.00 77.85  ? 273 TYR A CZ    1 
ATOM   2259 O  OH    . TYR A 1 273 ? 23.803  16.848  24.476  1.00 87.43  ? 273 TYR A OH    1 
ATOM   2260 N  N     . THR A 1 274 ? 15.587  16.824  27.684  1.00 78.43  ? 274 THR A N     1 
ATOM   2261 C  CA    . THR A 1 274 ? 14.296  17.332  28.106  1.00 60.05  ? 274 THR A CA    1 
ATOM   2262 C  C     . THR A 1 274 ? 14.487  18.608  28.919  1.00 72.31  ? 274 THR A C     1 
ATOM   2263 O  O     . THR A 1 274 ? 15.578  18.898  29.418  1.00 78.16  ? 274 THR A O     1 
ATOM   2264 C  CB    . THR A 1 274 ? 13.542  16.292  28.936  1.00 67.75  ? 274 THR A CB    1 
ATOM   2265 O  OG1   . THR A 1 274 ? 14.123  16.209  30.243  1.00 75.62  ? 274 THR A OG1   1 
ATOM   2266 C  CG2   . THR A 1 274 ? 13.611  14.928  28.272  1.00 60.27  ? 274 THR A CG2   1 
ATOM   2267 N  N     . LEU A 1 275 ? 13.406  19.380  29.041  1.00 73.39  ? 275 LEU A N     1 
ATOM   2268 C  CA    . LEU A 1 275 ? 13.464  20.611  29.824  1.00 71.01  ? 275 LEU A CA    1 
ATOM   2269 C  C     . LEU A 1 275 ? 13.854  20.321  31.267  1.00 77.89  ? 275 LEU A C     1 
ATOM   2270 O  O     . LEU A 1 275 ? 14.707  21.005  31.844  1.00 74.20  ? 275 LEU A O     1 
ATOM   2271 C  CB    . LEU A 1 275 ? 12.118  21.333  29.766  1.00 77.78  ? 275 LEU A CB    1 
ATOM   2272 C  CG    . LEU A 1 275 ? 12.085  22.765  30.304  1.00 76.69  ? 275 LEU A CG    1 
ATOM   2273 C  CD1   . LEU A 1 275 ? 13.341  23.539  29.912  1.00 63.58  ? 275 LEU A CD1   1 
ATOM   2274 C  CD2   . LEU A 1 275 ? 10.833  23.480  29.826  1.00 68.17  ? 275 LEU A CD2   1 
ATOM   2275 N  N     . GLU A 1 276 ? 13.241  19.296  31.864  1.00 73.44  ? 276 GLU A N     1 
ATOM   2276 C  CA    . GLU A 1 276 ? 13.552  18.940  33.244  1.00 71.00  ? 276 GLU A CA    1 
ATOM   2277 C  C     . GLU A 1 276 ? 14.999  18.485  33.383  1.00 75.03  ? 276 GLU A C     1 
ATOM   2278 O  O     . GLU A 1 276 ? 15.663  18.795  34.380  1.00 78.40  ? 276 GLU A O     1 
ATOM   2279 C  CB    . GLU A 1 276 ? 12.596  17.849  33.731  1.00 76.58  ? 276 GLU A CB    1 
ATOM   2280 C  CG    . GLU A 1 276 ? 11.124  18.248  33.735  1.00 81.32  ? 276 GLU A CG    1 
ATOM   2281 C  CD    . GLU A 1 276 ? 10.495  18.218  32.352  1.00 85.76  ? 276 GLU A CD    1 
ATOM   2282 O  OE1   . GLU A 1 276 ? 10.936  17.406  31.511  1.00 78.72  ? 276 GLU A OE1   1 
ATOM   2283 O  OE2   . GLU A 1 276 ? 9.561   19.010  32.107  1.00 81.98  ? 276 GLU A OE2   1 
ATOM   2284 N  N     . ALA A 1 277 ? 15.509  17.752  32.390  1.00 76.37  ? 277 ALA A N     1 
ATOM   2285 C  CA    . ALA A 1 277 ? 16.895  17.298  32.445  1.00 80.90  ? 277 ALA A CA    1 
ATOM   2286 C  C     . ALA A 1 277 ? 17.862  18.450  32.212  1.00 77.76  ? 277 ALA A C     1 
ATOM   2287 O  O     . ALA A 1 277 ? 18.878  18.566  32.908  1.00 73.69  ? 277 ALA A O     1 
ATOM   2288 C  CB    . ALA A 1 277 ? 17.129  16.189  31.421  1.00 67.16  ? 277 ALA A CB    1 
ATOM   2289 N  N     . VAL A 1 278 ? 17.567  19.310  31.235  1.00 77.74  ? 278 VAL A N     1 
ATOM   2290 C  CA    . VAL A 1 278 ? 18.446  20.439  30.950  1.00 71.71  ? 278 VAL A CA    1 
ATOM   2291 C  C     . VAL A 1 278 ? 18.464  21.413  32.120  1.00 80.55  ? 278 VAL A C     1 
ATOM   2292 O  O     . VAL A 1 278 ? 19.526  21.905  32.517  1.00 77.33  ? 278 VAL A O     1 
ATOM   2293 C  CB    . VAL A 1 278 ? 18.020  21.127  29.641  1.00 69.46  ? 278 VAL A CB    1 
ATOM   2294 C  CG1   . VAL A 1 278 ? 18.704  22.477  29.502  1.00 75.26  ? 278 VAL A CG1   1 
ATOM   2295 C  CG2   . VAL A 1 278 ? 18.351  20.239  28.456  1.00 76.22  ? 278 VAL A CG2   1 
ATOM   2296 N  N     . TYR A 1 279 ? 17.295  21.700  32.697  1.00 77.41  ? 279 TYR A N     1 
ATOM   2297 C  CA    . TYR A 1 279 ? 17.234  22.604  33.841  1.00 77.92  ? 279 TYR A CA    1 
ATOM   2298 C  C     . TYR A 1 279 ? 18.068  22.081  35.003  1.00 80.39  ? 279 TYR A C     1 
ATOM   2299 O  O     . TYR A 1 279 ? 18.922  22.795  35.542  1.00 84.73  ? 279 TYR A O     1 
ATOM   2300 C  CB    . TYR A 1 279 ? 15.783  22.802  34.277  1.00 80.49  ? 279 TYR A CB    1 
ATOM   2301 C  CG    . TYR A 1 279 ? 15.625  23.734  35.455  1.00 76.08  ? 279 TYR A CG    1 
ATOM   2302 C  CD1   . TYR A 1 279 ? 16.023  25.063  35.373  1.00 75.30  ? 279 TYR A CD1   1 
ATOM   2303 C  CD2   . TYR A 1 279 ? 15.096  23.281  36.656  1.00 82.88  ? 279 TYR A CD2   1 
ATOM   2304 C  CE1   . TYR A 1 279 ? 15.884  25.917  36.452  1.00 78.48  ? 279 TYR A CE1   1 
ATOM   2305 C  CE2   . TYR A 1 279 ? 14.955  24.127  37.740  1.00 95.85  ? 279 TYR A CE2   1 
ATOM   2306 C  CZ    . TYR A 1 279 ? 15.351  25.445  37.632  1.00 91.27  ? 279 TYR A CZ    1 
ATOM   2307 O  OH    . TYR A 1 279 ? 15.213  26.292  38.707  1.00 98.32  ? 279 TYR A OH    1 
ATOM   2308 N  N     . GLU A 1 280 ? 17.838  20.826  35.395  1.00 79.47  ? 280 GLU A N     1 
ATOM   2309 C  CA    . GLU A 1 280 ? 18.528  20.267  36.553  1.00 91.26  ? 280 GLU A CA    1 
ATOM   2310 C  C     . GLU A 1 280 ? 20.028  20.143  36.310  1.00 87.77  ? 280 GLU A C     1 
ATOM   2311 O  O     . GLU A 1 280 ? 20.819  20.232  37.256  1.00 74.60  ? 280 GLU A O     1 
ATOM   2312 C  CB    . GLU A 1 280 ? 17.913  18.910  36.907  1.00 95.51  ? 280 GLU A CB    1 
ATOM   2313 C  CG    . GLU A 1 280 ? 18.709  18.067  37.890  1.00 100.80 ? 280 GLU A CG    1 
ATOM   2314 C  CD    . GLU A 1 280 ? 18.017  16.759  38.219  1.00 105.35 ? 280 GLU A CD    1 
ATOM   2315 O  OE1   . GLU A 1 280 ? 16.776  16.695  38.090  1.00 107.05 ? 280 GLU A OE1   1 
ATOM   2316 O  OE2   . GLU A 1 280 ? 18.712  15.796  38.605  1.00 109.83 ? 280 GLU A OE2   1 
ATOM   2317 N  N     . ALA A 1 281 ? 20.440  19.964  35.055  1.00 89.35  ? 281 ALA A N     1 
ATOM   2318 C  CA    . ALA A 1 281 ? 21.857  19.824  34.745  1.00 84.01  ? 281 ALA A CA    1 
ATOM   2319 C  C     . ALA A 1 281 ? 22.592  21.157  34.704  1.00 80.09  ? 281 ALA A C     1 
ATOM   2320 O  O     . ALA A 1 281 ? 23.826  21.168  34.753  1.00 80.68  ? 281 ALA A O     1 
ATOM   2321 C  CB    . ALA A 1 281 ? 22.035  19.104  33.408  1.00 63.92  ? 281 ALA A CB    1 
ATOM   2322 N  N     . VAL A 1 282 ? 21.870  22.273  34.620  1.00 90.02  ? 282 VAL A N     1 
ATOM   2323 C  CA    . VAL A 1 282 ? 22.496  23.587  34.525  1.00 85.37  ? 282 VAL A CA    1 
ATOM   2324 C  C     . VAL A 1 282 ? 22.418  24.292  35.873  1.00 86.25  ? 282 VAL A C     1 
ATOM   2325 O  O     . VAL A 1 282 ? 23.324  25.047  36.245  1.00 92.00  ? 282 VAL A O     1 
ATOM   2326 C  CB    . VAL A 1 282 ? 21.838  24.434  33.419  1.00 81.22  ? 282 VAL A CB    1 
ATOM   2327 C  CG1   . VAL A 1 282 ? 22.430  25.835  33.388  1.00 84.43  ? 282 VAL A CG1   1 
ATOM   2328 C  CG2   . VAL A 1 282 ? 22.005  23.760  32.073  1.00 67.19  ? 282 VAL A CG2   1 
ATOM   2329 N  N     . PHE A 1 283 ? 21.344  24.043  36.620  1.00 85.52  ? 283 PHE A N     1 
ATOM   2330 C  CA    . PHE A 1 283 ? 21.088  24.759  37.861  1.00 95.62  ? 283 PHE A CA    1 
ATOM   2331 C  C     . PHE A 1 283 ? 21.103  23.872  39.100  1.00 99.66  ? 283 PHE A C     1 
ATOM   2332 O  O     . PHE A 1 283 ? 20.957  24.394  40.212  1.00 89.91  ? 283 PHE A O     1 
ATOM   2333 C  CB    . PHE A 1 283 ? 19.743  25.494  37.772  1.00 94.00  ? 283 PHE A CB    1 
ATOM   2334 C  CG    . PHE A 1 283 ? 19.746  26.629  36.793  1.00 89.88  ? 283 PHE A CG    1 
ATOM   2335 C  CD1   . PHE A 1 283 ? 20.305  27.846  37.136  1.00 86.23  ? 283 PHE A CD1   1 
ATOM   2336 C  CD2   . PHE A 1 283 ? 19.206  26.477  35.527  1.00 87.32  ? 283 PHE A CD2   1 
ATOM   2337 C  CE1   . PHE A 1 283 ? 20.319  28.895  36.241  1.00 81.11  ? 283 PHE A CE1   1 
ATOM   2338 C  CE2   . PHE A 1 283 ? 19.216  27.524  34.626  1.00 84.25  ? 283 PHE A CE2   1 
ATOM   2339 C  CZ    . PHE A 1 283 ? 19.775  28.734  34.984  1.00 81.76  ? 283 PHE A CZ    1 
ATOM   2340 N  N     . GLY A 1 284 ? 21.271  22.562  38.945  1.00 110.27 ? 284 GLY A N     1 
ATOM   2341 C  CA    . GLY A 1 284 ? 21.314  21.617  40.056  1.00 101.32 ? 284 GLY A CA    1 
ATOM   2342 C  C     . GLY A 1 284 ? 19.979  21.217  40.665  1.00 99.25  ? 284 GLY A C     1 
ATOM   2343 O  O     . GLY A 1 284 ? 19.821  20.084  41.126  1.00 113.55 ? 284 GLY A O     1 
ATOM   2344 N  N     . GLN A 1 285 ? 19.018  22.132  40.681  1.00 92.68  ? 285 GLN A N     1 
ATOM   2345 C  CA    . GLN A 1 285 ? 17.726  21.816  41.275  1.00 103.61 ? 285 GLN A CA    1 
ATOM   2346 C  C     . GLN A 1 285 ? 16.846  21.080  40.265  1.00 102.04 ? 285 GLN A C     1 
ATOM   2347 O  O     . GLN A 1 285 ? 16.805  21.451  39.089  1.00 95.67  ? 285 GLN A O     1 
ATOM   2348 C  CB    . GLN A 1 285 ? 17.026  23.086  41.751  1.00 96.48  ? 285 GLN A CB    1 
ATOM   2349 C  CG    . GLN A 1 285 ? 17.662  23.708  42.984  1.00 104.24 ? 285 GLN A CG    1 
ATOM   2350 C  CD    . GLN A 1 285 ? 18.284  22.672  43.903  1.00 116.19 ? 285 GLN A CD    1 
ATOM   2351 O  OE1   . GLN A 1 285 ? 17.581  21.881  44.533  1.00 114.26 ? 285 GLN A OE1   1 
ATOM   2352 N  NE2   . GLN A 1 285 ? 19.610  22.671  43.981  1.00 109.93 ? 285 GLN A NE2   1 
ATOM   2353 N  N     . PRO A 1 286 ? 16.137  20.043  40.698  1.00 99.17  ? 286 PRO A N     1 
ATOM   2354 C  CA    . PRO A 1 286 ? 15.323  19.252  39.772  1.00 100.57 ? 286 PRO A CA    1 
ATOM   2355 C  C     . PRO A 1 286 ? 14.026  19.965  39.408  1.00 103.32 ? 286 PRO A C     1 
ATOM   2356 O  O     . PRO A 1 286 ? 13.678  21.015  39.950  1.00 96.61  ? 286 PRO A O     1 
ATOM   2357 C  CB    . PRO A 1 286 ? 15.049  17.971  40.562  1.00 94.73  ? 286 PRO A CB    1 
ATOM   2358 C  CG    . PRO A 1 286 ? 15.044  18.422  41.984  1.00 99.98  ? 286 PRO A CG    1 
ATOM   2359 C  CD    . PRO A 1 286 ? 16.060  19.534  42.079  1.00 96.26  ? 286 PRO A CD    1 
ATOM   2360 N  N     . LYS A 1 287 ? 13.302  19.356  38.471  1.00 91.39  ? 287 LYS A N     1 
ATOM   2361 C  CA    . LYS A 1 287 ? 12.090  19.953  37.926  1.00 92.10  ? 287 LYS A CA    1 
ATOM   2362 C  C     . LYS A 1 287 ? 11.085  18.852  37.617  1.00 90.66  ? 287 LYS A C     1 
ATOM   2363 O  O     . LYS A 1 287 ? 11.427  17.862  36.965  1.00 91.63  ? 287 LYS A O     1 
ATOM   2364 C  CB    . LYS A 1 287 ? 12.412  20.767  36.667  1.00 90.78  ? 287 LYS A CB    1 
ATOM   2365 C  CG    . LYS A 1 287 ? 11.246  21.552  36.103  1.00 93.33  ? 287 LYS A CG    1 
ATOM   2366 C  CD    . LYS A 1 287 ? 11.382  21.711  34.600  1.00 76.77  ? 287 LYS A CD    1 
ATOM   2367 C  CE    . LYS A 1 287 ? 10.245  22.536  34.032  1.00 84.10  ? 287 LYS A CE    1 
ATOM   2368 N  NZ    . LYS A 1 287 ? 9.072   21.693  33.698  1.00 90.71  ? 287 LYS A NZ    1 
ATOM   2369 N  N     . GLU A 1 288 ? 9.852   19.030  38.087  1.00 92.72  ? 288 GLU A N     1 
ATOM   2370 C  CA    . GLU A 1 288 ? 8.829   18.008  37.920  1.00 84.76  ? 288 GLU A CA    1 
ATOM   2371 C  C     . GLU A 1 288 ? 8.328   17.962  36.482  1.00 83.76  ? 288 GLU A C     1 
ATOM   2372 O  O     . GLU A 1 288 ? 8.235   18.985  35.797  1.00 94.15  ? 288 GLU A O     1 
ATOM   2373 C  CB    . GLU A 1 288 ? 7.656   18.266  38.864  1.00 86.18  ? 288 GLU A CB    1 
ATOM   2374 C  CG    . GLU A 1 288 ? 7.736   17.508  40.176  1.00 98.17  ? 288 GLU A CG    1 
ATOM   2375 C  CD    . GLU A 1 288 ? 7.027   18.227  41.304  1.00 119.43 ? 288 GLU A CD    1 
ATOM   2376 O  OE1   . GLU A 1 288 ? 7.704   18.642  42.269  1.00 122.95 ? 288 GLU A OE1   1 
ATOM   2377 O  OE2   . GLU A 1 288 ? 5.789   18.379  41.223  1.00 120.10 ? 288 GLU A OE2   1 
ATOM   2378 N  N     . LYS A 1 289 ? 7.993   16.756  36.029  1.00 75.78  ? 289 LYS A N     1 
ATOM   2379 C  CA    . LYS A 1 289 ? 7.463   16.533  34.690  1.00 84.65  ? 289 LYS A CA    1 
ATOM   2380 C  C     . LYS A 1 289 ? 6.057   15.962  34.800  1.00 91.69  ? 289 LYS A C     1 
ATOM   2381 O  O     . LYS A 1 289 ? 5.867   14.874  35.354  1.00 100.47 ? 289 LYS A O     1 
ATOM   2382 C  CB    . LYS A 1 289 ? 8.361   15.587  33.888  1.00 79.33  ? 289 LYS A CB    1 
ATOM   2383 C  CG    . LYS A 1 289 ? 7.691   14.977  32.660  1.00 71.06  ? 289 LYS A CG    1 
ATOM   2384 C  CD    . LYS A 1 289 ? 7.238   16.044  31.672  1.00 76.38  ? 289 LYS A CD    1 
ATOM   2385 C  CE    . LYS A 1 289 ? 7.742   15.751  30.270  1.00 80.50  ? 289 LYS A CE    1 
ATOM   2386 N  NZ    . LYS A 1 289 ? 6.851   16.340  29.231  1.00 68.89  ? 289 LYS A NZ    1 
ATOM   2387 N  N     . VAL A 1 290 ? 5.080   16.696  34.279  1.00 80.38  ? 290 VAL A N     1 
ATOM   2388 C  CA    . VAL A 1 290 ? 3.723   16.196  34.104  1.00 87.08  ? 290 VAL A CA    1 
ATOM   2389 C  C     . VAL A 1 290 ? 3.569   15.794  32.645  1.00 85.51  ? 290 VAL A C     1 
ATOM   2390 O  O     . VAL A 1 290 ? 3.927   16.560  31.741  1.00 86.88  ? 290 VAL A O     1 
ATOM   2391 C  CB    . VAL A 1 290 ? 2.678   17.249  34.508  1.00 84.57  ? 290 VAL A CB    1 
ATOM   2392 C  CG1   . VAL A 1 290 ? 1.276   16.687  34.359  1.00 89.34  ? 290 VAL A CG1   1 
ATOM   2393 C  CG2   . VAL A 1 290 ? 2.920   17.715  35.935  1.00 87.17  ? 290 VAL A CG2   1 
ATOM   2394 N  N     . TYR A 1 291 ? 3.050   14.594  32.410  1.00 84.23  ? 291 TYR A N     1 
ATOM   2395 C  CA    . TYR A 1 291 ? 3.055   14.020  31.075  1.00 82.46  ? 291 TYR A CA    1 
ATOM   2396 C  C     . TYR A 1 291 ? 1.751   14.318  30.339  1.00 84.88  ? 291 TYR A C     1 
ATOM   2397 O  O     . TYR A 1 291 ? 0.764   14.780  30.916  1.00 91.33  ? 291 TYR A O     1 
ATOM   2398 C  CB    . TYR A 1 291 ? 3.306   12.514  31.145  1.00 80.99  ? 291 TYR A CB    1 
ATOM   2399 C  CG    . TYR A 1 291 ? 4.663   12.167  31.712  1.00 85.65  ? 291 TYR A CG    1 
ATOM   2400 C  CD1   . TYR A 1 291 ? 4.866   12.081  33.083  1.00 84.71  ? 291 TYR A CD1   1 
ATOM   2401 C  CD2   . TYR A 1 291 ? 5.747   11.944  30.874  1.00 83.62  ? 291 TYR A CD2   1 
ATOM   2402 C  CE1   . TYR A 1 291 ? 6.106   11.771  33.604  1.00 88.06  ? 291 TYR A CE1   1 
ATOM   2403 C  CE2   . TYR A 1 291 ? 6.992   11.634  31.385  1.00 88.76  ? 291 TYR A CE2   1 
ATOM   2404 C  CZ    . TYR A 1 291 ? 7.166   11.549  32.751  1.00 98.27  ? 291 TYR A CZ    1 
ATOM   2405 O  OH    . TYR A 1 291 ? 8.404   11.241  33.265  1.00 98.21  ? 291 TYR A OH    1 
ATOM   2406 N  N     . ALA A 1 292 ? 1.765   14.042  29.031  1.00 79.95  ? 292 ALA A N     1 
ATOM   2407 C  CA    . ALA A 1 292 ? 0.611   14.339  28.190  1.00 85.16  ? 292 ALA A CA    1 
ATOM   2408 C  C     . ALA A 1 292 ? -0.576  13.443  28.516  1.00 104.68 ? 292 ALA A C     1 
ATOM   2409 O  O     . ALA A 1 292 ? -1.724  13.823  28.260  1.00 100.19 ? 292 ALA A O     1 
ATOM   2410 C  CB    . ALA A 1 292 ? 0.984   14.208  26.714  1.00 79.87  ? 292 ALA A CB    1 
ATOM   2411 N  N     . GLU A 1 293 ? -0.327  12.252  29.063  1.00 103.05 ? 293 GLU A N     1 
ATOM   2412 C  CA    . GLU A 1 293 ? -1.437  11.407  29.486  1.00 85.15  ? 293 GLU A CA    1 
ATOM   2413 C  C     . GLU A 1 293 ? -2.152  12.006  30.687  1.00 97.87  ? 293 GLU A C     1 
ATOM   2414 O  O     . GLU A 1 293 ? -3.373  11.864  30.815  1.00 104.07 ? 293 GLU A O     1 
ATOM   2415 C  CB    . GLU A 1 293 ? -0.937  9.997   29.800  1.00 101.57 ? 293 GLU A CB    1 
ATOM   2416 C  CG    . GLU A 1 293 ? -0.417  9.254   28.580  1.00 113.64 ? 293 GLU A CG    1 
ATOM   2417 C  CD    . GLU A 1 293 ? 1.012   9.638   28.228  1.00 116.30 ? 293 GLU A CD    1 
ATOM   2418 O  OE1   . GLU A 1 293 ? 1.784   9.992   29.144  1.00 121.60 ? 293 GLU A OE1   1 
ATOM   2419 O  OE2   . GLU A 1 293 ? 1.363   9.586   27.031  1.00 110.70 ? 293 GLU A OE2   1 
ATOM   2420 N  N     . GLU A 1 294 ? -1.418  12.705  31.554  1.00 97.14  ? 294 GLU A N     1 
ATOM   2421 C  CA    . GLU A 1 294 ? -2.025  13.285  32.746  1.00 90.95  ? 294 GLU A CA    1 
ATOM   2422 C  C     . GLU A 1 294 ? -2.801  14.554  32.422  1.00 96.13  ? 294 GLU A C     1 
ATOM   2423 O  O     . GLU A 1 294 ? -3.912  14.745  32.928  1.00 96.21  ? 294 GLU A O     1 
ATOM   2424 C  CB    . GLU A 1 294 ? -0.952  13.570  33.800  1.00 95.51  ? 294 GLU A CB    1 
ATOM   2425 C  CG    . GLU A 1 294 ? 0.141   12.519  33.881  1.00 97.50  ? 294 GLU A CG    1 
ATOM   2426 C  CD    . GLU A 1 294 ? 1.148   12.814  34.975  1.00 95.98  ? 294 GLU A CD    1 
ATOM   2427 O  OE1   . GLU A 1 294 ? 0.725   13.187  36.089  1.00 100.77 ? 294 GLU A OE1   1 
ATOM   2428 O  OE2   . GLU A 1 294 ? 2.362   12.677  34.722  1.00 98.06  ? 294 GLU A OE2   1 
ATOM   2429 N  N     . ILE A 1 295 ? -2.248  15.423  31.570  1.00 95.90  ? 295 ILE A N     1 
ATOM   2430 C  CA    . ILE A 1 295 ? -2.877  16.723  31.375  1.00 95.65  ? 295 ILE A CA    1 
ATOM   2431 C  C     . ILE A 1 295 ? -4.130  16.595  30.513  1.00 100.20 ? 295 ILE A C     1 
ATOM   2432 O  O     . ILE A 1 295 ? -5.002  17.471  30.549  1.00 103.05 ? 295 ILE A O     1 
ATOM   2433 C  CB    . ILE A 1 295 ? -1.855  17.750  30.823  1.00 103.02 ? 295 ILE A CB    1 
ATOM   2434 C  CG1   . ILE A 1 295 ? -1.048  17.290  29.595  1.00 105.16 ? 295 ILE A CG1   1 
ATOM   2435 C  CG2   . ILE A 1 295 ? -0.839  18.082  31.898  1.00 105.40 ? 295 ILE A CG2   1 
ATOM   2436 C  CD1   . ILE A 1 295 ? -1.844  16.918  28.364  1.00 98.60  ? 295 ILE A CD1   1 
ATOM   2437 N  N     . THR A 1 296 ? -4.245  15.511  29.743  1.00 103.60 ? 296 THR A N     1 
ATOM   2438 C  CA    . THR A 1 296 ? -5.449  15.273  28.958  1.00 96.13  ? 296 THR A CA    1 
ATOM   2439 C  C     . THR A 1 296 ? -6.569  14.737  29.839  1.00 99.20  ? 296 THR A C     1 
ATOM   2440 O  O     . THR A 1 296 ? -7.713  15.196  29.751  1.00 113.20 ? 296 THR A O     1 
ATOM   2441 C  CB    . THR A 1 296 ? -5.145  14.304  27.811  1.00 95.09  ? 296 THR A CB    1 
ATOM   2442 O  OG1   . THR A 1 296 ? -4.548  15.021  26.722  1.00 105.38 ? 296 THR A OG1   1 
ATOM   2443 C  CG2   . THR A 1 296 ? -6.415  13.620  27.325  1.00 98.19  ? 296 THR A CG2   1 
ATOM   2444 N  N     . THR A 1 297 ? -6.251  13.768  30.700  1.00 98.98  ? 297 THR A N     1 
ATOM   2445 C  CA    . THR A 1 297 ? -7.238  13.269  31.651  1.00 97.76  ? 297 THR A CA    1 
ATOM   2446 C  C     . THR A 1 297 ? -7.633  14.351  32.650  1.00 107.35 ? 297 THR A C     1 
ATOM   2447 O  O     . THR A 1 297 ? -8.821  14.519  32.954  1.00 108.40 ? 297 THR A O     1 
ATOM   2448 C  CB    . THR A 1 297 ? -6.690  12.039  32.374  1.00 101.13 ? 297 THR A CB    1 
ATOM   2449 O  OG1   . THR A 1 297 ? -6.840  10.886  31.537  1.00 108.53 ? 297 THR A OG1   1 
ATOM   2450 C  CG2   . THR A 1 297 ? -7.429  11.806  33.685  1.00 97.71  ? 297 THR A CG2   1 
ATOM   2451 N  N     . ALA A 1 298 ? -6.652  15.104  33.156  1.00 113.51 ? 298 ALA A N     1 
ATOM   2452 C  CA    . ALA A 1 298 ? -6.948  16.175  34.103  1.00 109.39 ? 298 ALA A CA    1 
ATOM   2453 C  C     . ALA A 1 298 ? -7.867  17.224  33.494  1.00 103.33 ? 298 ALA A C     1 
ATOM   2454 O  O     . ALA A 1 298 ? -8.621  17.882  34.219  1.00 104.99 ? 298 ALA A O     1 
ATOM   2455 C  CB    . ALA A 1 298 ? -5.653  16.826  34.589  1.00 103.23 ? 298 ALA A CB    1 
ATOM   2456 N  N     . TRP A 1 299 ? -7.822  17.393  32.173  1.00 100.12 ? 299 TRP A N     1 
ATOM   2457 C  CA    . TRP A 1 299 ? -8.686  18.363  31.510  1.00 104.75 ? 299 TRP A CA    1 
ATOM   2458 C  C     . TRP A 1 299 ? -10.102 17.824  31.342  1.00 111.47 ? 299 TRP A C     1 
ATOM   2459 O  O     . TRP A 1 299 ? -11.073 18.442  31.792  1.00 110.20 ? 299 TRP A O     1 
ATOM   2460 C  CB    . TRP A 1 299 ? -8.100  18.747  30.150  1.00 102.56 ? 299 TRP A CB    1 
ATOM   2461 C  CG    . TRP A 1 299 ? -8.695  19.999  29.602  1.00 107.01 ? 299 TRP A CG    1 
ATOM   2462 C  CD1   . TRP A 1 299 ? -9.648  20.100  28.630  1.00 109.39 ? 299 TRP A CD1   1 
ATOM   2463 C  CD2   . TRP A 1 299 ? -8.385  21.337  30.002  1.00 105.96 ? 299 TRP A CD2   1 
ATOM   2464 N  NE1   . TRP A 1 299 ? -9.947  21.421  28.398  1.00 113.00 ? 299 TRP A NE1   1 
ATOM   2465 C  CE2   . TRP A 1 299 ? -9.185  22.200  29.228  1.00 112.64 ? 299 TRP A CE2   1 
ATOM   2466 C  CE3   . TRP A 1 299 ? -7.506  21.889  30.938  1.00 98.47  ? 299 TRP A CE3   1 
ATOM   2467 C  CZ2   . TRP A 1 299 ? -9.131  23.584  29.361  1.00 110.53 ? 299 TRP A CZ2   1 
ATOM   2468 C  CZ3   . TRP A 1 299 ? -7.454  23.263  31.068  1.00 100.38 ? 299 TRP A CZ3   1 
ATOM   2469 C  CH2   . TRP A 1 299 ? -8.259  24.095  30.281  1.00 102.68 ? 299 TRP A CH2   1 
ATOM   2470 N  N     . GLU A 1 300 ? -10.235 16.668  30.687  1.00 111.24 ? 300 GLU A N     1 
ATOM   2471 C  CA    . GLU A 1 300 ? -11.551 16.114  30.389  1.00 116.36 ? 300 GLU A CA    1 
ATOM   2472 C  C     . GLU A 1 300 ? -12.329 15.750  31.646  1.00 107.53 ? 300 GLU A C     1 
ATOM   2473 O  O     . GLU A 1 300 ? -13.563 15.687  31.601  1.00 94.20  ? 300 GLU A O     1 
ATOM   2474 C  CB    . GLU A 1 300 ? -11.396 14.894  29.481  1.00 108.53 ? 300 GLU A CB    1 
ATOM   2475 C  CG    . GLU A 1 300 ? -10.529 15.164  28.261  1.00 105.30 ? 300 GLU A CG    1 
ATOM   2476 C  CD    . GLU A 1 300 ? -10.382 13.957  27.358  1.00 112.22 ? 300 GLU A CD    1 
ATOM   2477 O  OE1   . GLU A 1 300 ? -10.234 12.833  27.883  1.00 109.22 ? 300 GLU A OE1   1 
ATOM   2478 O  OE2   . GLU A 1 300 ? -10.408 14.136  26.122  1.00 101.67 ? 300 GLU A OE2   1 
ATOM   2479 N  N     . THR A 1 301 ? -11.641 15.511  32.762  1.00 104.98 ? 301 THR A N     1 
ATOM   2480 C  CA    . THR A 1 301 ? -12.291 15.250  34.038  1.00 107.08 ? 301 THR A CA    1 
ATOM   2481 C  C     . THR A 1 301 ? -12.326 16.471  34.948  1.00 109.79 ? 301 THR A C     1 
ATOM   2482 O  O     . THR A 1 301 ? -13.083 16.474  35.925  1.00 109.21 ? 301 THR A O     1 
ATOM   2483 C  CB    . THR A 1 301 ? -11.589 14.097  34.771  1.00 100.17 ? 301 THR A CB    1 
ATOM   2484 O  OG1   . THR A 1 301 ? -10.197 14.401  34.925  1.00 108.55 ? 301 THR A OG1   1 
ATOM   2485 C  CG2   . THR A 1 301 ? -11.732 12.799  33.989  1.00 95.83  ? 301 THR A CG2   1 
ATOM   2486 N  N     . GLY A 1 302 ? -11.535 17.503  34.653  1.00 111.07 ? 302 GLY A N     1 
ATOM   2487 C  CA    . GLY A 1 302 ? -11.441 18.667  35.509  1.00 107.45 ? 302 GLY A CA    1 
ATOM   2488 C  C     . GLY A 1 302 ? -10.733 18.439  36.825  1.00 111.96 ? 302 GLY A C     1 
ATOM   2489 O  O     . GLY A 1 302 ? -10.610 19.384  37.613  1.00 104.54 ? 302 GLY A O     1 
ATOM   2490 N  N     . GLU A 1 303 ? -10.256 17.226  37.083  1.00 109.16 ? 303 GLU A N     1 
ATOM   2491 C  CA    . GLU A 1 303 ? -9.660  16.878  38.364  1.00 114.16 ? 303 GLU A CA    1 
ATOM   2492 C  C     . GLU A 1 303 ? -8.165  17.159  38.355  1.00 117.17 ? 303 GLU A C     1 
ATOM   2493 O  O     . GLU A 1 303 ? -7.467  16.848  37.385  1.00 113.69 ? 303 GLU A O     1 
ATOM   2494 C  CB    . GLU A 1 303 ? -9.911  15.404  38.683  1.00 115.63 ? 303 GLU A CB    1 
ATOM   2495 C  CG    . GLU A 1 303 ? -11.347 14.962  38.462  1.00 117.03 ? 303 GLU A CG    1 
ATOM   2496 C  CD    . GLU A 1 303 ? -11.659 13.642  39.135  1.00 117.22 ? 303 GLU A CD    1 
ATOM   2497 O  OE1   . GLU A 1 303 ? -10.707 12.906  39.470  1.00 111.34 ? 303 GLU A OE1   1 
ATOM   2498 O  OE2   . GLU A 1 303 ? -12.856 13.338  39.326  1.00 122.07 ? 303 GLU A OE2   1 
ATOM   2499 N  N     . ASN A 1 304 ? -7.682  17.749  39.451  1.00 129.90 ? 304 ASN A N     1 
ATOM   2500 C  CA    . ASN A 1 304 ? -6.260  18.044  39.641  1.00 128.22 ? 304 ASN A CA    1 
ATOM   2501 C  C     . ASN A 1 304 ? -5.703  18.873  38.487  1.00 111.39 ? 304 ASN A C     1 
ATOM   2502 O  O     . ASN A 1 304 ? -4.616  18.609  37.968  1.00 109.90 ? 304 ASN A O     1 
ATOM   2503 C  CB    . ASN A 1 304 ? -5.452  16.760  39.835  1.00 128.71 ? 304 ASN A CB    1 
ATOM   2504 C  CG    . ASN A 1 304 ? -4.450  16.871  40.969  1.00 143.59 ? 304 ASN A CG    1 
ATOM   2505 O  OD1   . ASN A 1 304 ? -3.833  17.918  41.168  1.00 130.39 ? 304 ASN A OD1   1 
ATOM   2506 N  ND2   . ASN A 1 304 ? -4.287  15.789  41.723  1.00 149.04 ? 304 ASN A ND2   1 
ATOM   2507 N  N     . LEU A 1 305 ? -6.465  19.887  38.076  1.00 118.77 ? 305 LEU A N     1 
ATOM   2508 C  CA    . LEU A 1 305 ? -5.998  20.811  37.053  1.00 113.00 ? 305 LEU A CA    1 
ATOM   2509 C  C     . LEU A 1 305 ? -4.976  21.801  37.592  1.00 103.98 ? 305 LEU A C     1 
ATOM   2510 O  O     . LEU A 1 305 ? -4.220  22.383  36.808  1.00 97.21  ? 305 LEU A O     1 
ATOM   2511 C  CB    . LEU A 1 305 ? -7.186  21.563  36.448  1.00 107.66 ? 305 LEU A CB    1 
ATOM   2512 C  CG    . LEU A 1 305 ? -7.225  21.696  34.924  1.00 104.02 ? 305 LEU A CG    1 
ATOM   2513 C  CD1   . LEU A 1 305 ? -6.664  20.453  34.249  1.00 96.12  ? 305 LEU A CD1   1 
ATOM   2514 C  CD2   . LEU A 1 305 ? -8.647  21.963  34.460  1.00 110.97 ? 305 LEU A CD2   1 
ATOM   2515 N  N     . GLU A 1 306 ? -4.938  21.998  38.912  1.00 106.59 ? 306 GLU A N     1 
ATOM   2516 C  CA    . GLU A 1 306 ? -3.940  22.877  39.509  1.00 97.85  ? 306 GLU A CA    1 
ATOM   2517 C  C     . GLU A 1 306 ? -2.534  22.315  39.351  1.00 108.29 ? 306 GLU A C     1 
ATOM   2518 O  O     . GLU A 1 306 ? -1.566  23.081  39.282  1.00 106.94 ? 306 GLU A O     1 
ATOM   2519 C  CB    . GLU A 1 306 ? -4.267  23.095  40.985  1.00 96.34  ? 306 GLU A CB    1 
ATOM   2520 C  CG    . GLU A 1 306 ? -5.726  22.822  41.323  1.00 113.53 ? 306 GLU A CG    1 
ATOM   2521 C  CD    . GLU A 1 306 ? -6.103  23.266  42.721  1.00 124.24 ? 306 GLU A CD    1 
ATOM   2522 O  OE1   . GLU A 1 306 ? -5.250  23.169  43.628  1.00 133.42 ? 306 GLU A OE1   1 
ATOM   2523 O  OE2   . GLU A 1 306 ? -7.256  23.708  42.914  1.00 107.61 ? 306 GLU A OE2   1 
ATOM   2524 N  N     . ARG A 1 307 ? -2.403  20.987  39.297  1.00 112.67 ? 307 ARG A N     1 
ATOM   2525 C  CA    . ARG A 1 307 ? -1.098  20.378  39.063  1.00 105.27 ? 307 ARG A CA    1 
ATOM   2526 C  C     . ARG A 1 307 ? -0.569  20.734  37.680  1.00 107.92 ? 307 ARG A C     1 
ATOM   2527 O  O     . ARG A 1 307 ? 0.635   20.961  37.504  1.00 102.61 ? 307 ARG A O     1 
ATOM   2528 C  CB    . ARG A 1 307 ? -1.192  18.862  39.230  1.00 101.96 ? 307 ARG A CB    1 
ATOM   2529 C  CG    . ARG A 1 307 ? 0.076   18.122  38.846  1.00 103.26 ? 307 ARG A CG    1 
ATOM   2530 C  CD    . ARG A 1 307 ? 0.384   16.986  39.808  1.00 96.49  ? 307 ARG A CD    1 
ATOM   2531 N  NE    . ARG A 1 307 ? 1.448   16.129  39.298  1.00 101.81 ? 307 ARG A NE    1 
ATOM   2532 C  CZ    . ARG A 1 307 ? 1.318   15.294  38.275  1.00 106.75 ? 307 ARG A CZ    1 
ATOM   2533 N  NH1   . ARG A 1 307 ? 0.163   15.144  37.646  1.00 109.81 ? 307 ARG A NH1   1 
ATOM   2534 N  NH2   . ARG A 1 307 ? 2.372   14.589  37.876  1.00 95.79  ? 307 ARG A NH2   1 
ATOM   2535 N  N     . VAL A 1 308 ? -1.457  20.781  36.684  1.00 108.01 ? 308 VAL A N     1 
ATOM   2536 C  CA    . VAL A 1 308 ? -1.064  21.206  35.345  1.00 102.82 ? 308 VAL A CA    1 
ATOM   2537 C  C     . VAL A 1 308 ? -0.615  22.659  35.348  1.00 99.54  ? 308 VAL A C     1 
ATOM   2538 O  O     . VAL A 1 308 ? 0.303   23.038  34.611  1.00 101.05 ? 308 VAL A O     1 
ATOM   2539 C  CB    . VAL A 1 308 ? -2.227  20.983  34.359  1.00 104.17 ? 308 VAL A CB    1 
ATOM   2540 C  CG1   . VAL A 1 308 ? -1.779  21.269  32.938  1.00 95.45  ? 308 VAL A CG1   1 
ATOM   2541 C  CG2   . VAL A 1 308 ? -2.772  19.568  34.492  1.00 100.82 ? 308 VAL A CG2   1 
ATOM   2542 N  N     . ALA A 1 309 ? -1.250  23.495  36.172  1.00 107.01 ? 309 ALA A N     1 
ATOM   2543 C  CA    . ALA A 1 309 ? -0.904  24.911  36.202  1.00 104.20 ? 309 ALA A CA    1 
ATOM   2544 C  C     . ALA A 1 309 ? 0.499   25.129  36.751  1.00 98.24  ? 309 ALA A C     1 
ATOM   2545 O  O     . ALA A 1 309 ? 1.240   25.984  36.251  1.00 93.28  ? 309 ALA A O     1 
ATOM   2546 C  CB    . ALA A 1 309 ? -1.932  25.683  37.027  1.00 106.89 ? 309 ALA A CB    1 
ATOM   2547 N  N     . ARG A 1 310 ? 0.881   24.369  37.779  1.00 96.26  ? 310 ARG A N     1 
ATOM   2548 C  CA    . ARG A 1 310 ? 2.236   24.474  38.309  1.00 98.17  ? 310 ARG A CA    1 
ATOM   2549 C  C     . ARG A 1 310 ? 3.263   24.113  37.244  1.00 98.47  ? 310 ARG A C     1 
ATOM   2550 O  O     . ARG A 1 310 ? 4.219   24.859  37.009  1.00 98.50  ? 310 ARG A O     1 
ATOM   2551 C  CB    . ARG A 1 310 ? 2.394   23.579  39.538  1.00 99.96  ? 310 ARG A CB    1 
ATOM   2552 C  CG    . ARG A 1 310 ? 3.731   23.736  40.240  1.00 110.61 ? 310 ARG A CG    1 
ATOM   2553 C  CD    . ARG A 1 310 ? 4.060   22.524  41.096  1.00 121.38 ? 310 ARG A CD    1 
ATOM   2554 N  NE    . ARG A 1 310 ? 4.033   21.283  40.329  1.00 131.62 ? 310 ARG A NE    1 
ATOM   2555 C  CZ    . ARG A 1 310 ? 3.373   20.192  40.694  1.00 130.87 ? 310 ARG A CZ    1 
ATOM   2556 N  NH1   . ARG A 1 310 ? 2.681   20.147  41.820  1.00 117.82 ? 310 ARG A NH1   1 
ATOM   2557 N  NH2   . ARG A 1 310 ? 3.414   19.117  39.911  1.00 118.18 ? 310 ARG A NH2   1 
ATOM   2558 N  N     . TYR A 1 311 ? 3.068   22.972  36.576  1.00 100.43 ? 311 TYR A N     1 
ATOM   2559 C  CA    . TYR A 1 311 ? 3.973   22.564  35.506  1.00 94.85  ? 311 TYR A CA    1 
ATOM   2560 C  C     . TYR A 1 311 ? 4.026   23.607  34.396  1.00 89.66  ? 311 TYR A C     1 
ATOM   2561 O  O     . TYR A 1 311 ? 5.108   23.933  33.892  1.00 85.93  ? 311 TYR A O     1 
ATOM   2562 C  CB    . TYR A 1 311 ? 3.535   21.210  34.947  1.00 89.43  ? 311 TYR A CB    1 
ATOM   2563 C  CG    . TYR A 1 311 ? 4.367   20.707  33.789  1.00 81.07  ? 311 TYR A CG    1 
ATOM   2564 C  CD1   . TYR A 1 311 ? 3.769   20.325  32.596  1.00 75.15  ? 311 TYR A CD1   1 
ATOM   2565 C  CD2   . TYR A 1 311 ? 5.747   20.595  33.895  1.00 95.25  ? 311 TYR A CD2   1 
ATOM   2566 C  CE1   . TYR A 1 311 ? 4.523   19.860  31.533  1.00 78.06  ? 311 TYR A CE1   1 
ATOM   2567 C  CE2   . TYR A 1 311 ? 6.508   20.128  32.839  1.00 89.14  ? 311 TYR A CE2   1 
ATOM   2568 C  CZ    . TYR A 1 311 ? 5.893   19.764  31.662  1.00 86.27  ? 311 TYR A CZ    1 
ATOM   2569 O  OH    . TYR A 1 311 ? 6.653   19.301  30.611  1.00 91.19  ? 311 TYR A OH    1 
ATOM   2570 N  N     . SER A 1 312 ? 2.866   24.140  34.004  1.00 94.86  ? 312 SER A N     1 
ATOM   2571 C  CA    . SER A 1 312 ? 2.824   25.173  32.972  1.00 94.43  ? 312 SER A CA    1 
ATOM   2572 C  C     . SER A 1 312 ? 3.652   26.386  33.380  1.00 87.41  ? 312 SER A C     1 
ATOM   2573 O  O     . SER A 1 312 ? 4.480   26.876  32.605  1.00 74.87  ? 312 SER A O     1 
ATOM   2574 C  CB    . SER A 1 312 ? 1.374   25.576  32.694  1.00 95.91  ? 312 SER A CB    1 
ATOM   2575 O  OG    . SER A 1 312 ? 1.266   26.374  31.527  1.00 90.77  ? 312 SER A OG    1 
ATOM   2576 N  N     . MET A 1 313 ? 3.440   26.882  34.601  1.00 95.51  ? 313 MET A N     1 
ATOM   2577 C  CA    . MET A 1 313 ? 4.221   28.017  35.082  1.00 88.52  ? 313 MET A CA    1 
ATOM   2578 C  C     . MET A 1 313 ? 5.697   27.658  35.194  1.00 87.63  ? 313 MET A C     1 
ATOM   2579 O  O     . MET A 1 313 ? 6.568   28.469  34.858  1.00 89.07  ? 313 MET A O     1 
ATOM   2580 C  CB    . MET A 1 313 ? 3.669   28.493  36.428  1.00 85.34  ? 313 MET A CB    1 
ATOM   2581 C  CG    . MET A 1 313 ? 4.528   29.520  37.154  1.00 87.35  ? 313 MET A CG    1 
ATOM   2582 S  SD    . MET A 1 313 ? 5.764   28.796  38.254  1.00 97.94  ? 313 MET A SD    1 
ATOM   2583 C  CE    . MET A 1 313 ? 6.242   30.230  39.213  1.00 104.52 ? 313 MET A CE    1 
ATOM   2584 N  N     . GLU A 1 314 ? 5.995   26.443  35.663  1.00 89.87  ? 314 GLU A N     1 
ATOM   2585 C  CA    . GLU A 1 314 ? 7.385   26.020  35.797  1.00 85.76  ? 314 GLU A CA    1 
ATOM   2586 C  C     . GLU A 1 314 ? 8.095   26.021  34.450  1.00 83.83  ? 314 GLU A C     1 
ATOM   2587 O  O     . GLU A 1 314 ? 9.236   26.482  34.345  1.00 79.57  ? 314 GLU A O     1 
ATOM   2588 C  CB    . GLU A 1 314 ? 7.454   24.634  36.439  1.00 83.45  ? 314 GLU A CB    1 
ATOM   2589 C  CG    . GLU A 1 314 ? 7.178   24.625  37.933  1.00 88.49  ? 314 GLU A CG    1 
ATOM   2590 C  CD    . GLU A 1 314 ? 8.108   23.701  38.691  1.00 109.99 ? 314 GLU A CD    1 
ATOM   2591 O  OE1   . GLU A 1 314 ? 8.546   22.687  38.107  1.00 108.28 ? 314 GLU A OE1   1 
ATOM   2592 O  OE2   . GLU A 1 314 ? 8.395   23.983  39.874  1.00 121.11 ? 314 GLU A OE2   1 
ATOM   2593 N  N     . ASP A 1 315 ? 7.430   25.513  33.408  1.00 85.90  ? 315 ASP A N     1 
ATOM   2594 C  CA    . ASP A 1 315 ? 8.020   25.502  32.073  1.00 74.72  ? 315 ASP A CA    1 
ATOM   2595 C  C     . ASP A 1 315 ? 8.452   26.900  31.648  1.00 85.20  ? 315 ASP A C     1 
ATOM   2596 O  O     . ASP A 1 315 ? 9.597   27.110  31.236  1.00 77.16  ? 315 ASP A O     1 
ATOM   2597 C  CB    . ASP A 1 315 ? 7.027   24.918  31.067  1.00 71.78  ? 315 ASP A CB    1 
ATOM   2598 C  CG    . ASP A 1 315 ? 7.289   23.457  30.769  1.00 78.13  ? 315 ASP A CG    1 
ATOM   2599 O  OD1   . ASP A 1 315 ? 7.795   22.749  31.664  1.00 87.49  ? 315 ASP A OD1   1 
ATOM   2600 O  OD2   . ASP A 1 315 ? 6.988   23.016  29.640  1.00 79.58  ? 315 ASP A OD2   1 
ATOM   2601 N  N     . ALA A 1 316 ? 7.546   27.874  31.755  1.00 89.70  ? 316 ALA A N     1 
ATOM   2602 C  CA    . ALA A 1 316 ? 7.888   29.243  31.377  1.00 81.92  ? 316 ALA A CA    1 
ATOM   2603 C  C     . ALA A 1 316 ? 8.986   29.807  32.269  1.00 80.98  ? 316 ALA A C     1 
ATOM   2604 O  O     . ALA A 1 316 ? 9.916   30.460  31.783  1.00 74.65  ? 316 ALA A O     1 
ATOM   2605 C  CB    . ALA A 1 316 ? 6.646   30.129  31.434  1.00 68.92  ? 316 ALA A CB    1 
ATOM   2606 N  N     . LYS A 1 317 ? 8.898   29.558  33.578  1.00 80.91  ? 317 LYS A N     1 
ATOM   2607 C  CA    . LYS A 1 317 ? 9.883   30.105  34.506  1.00 84.00  ? 317 LYS A CA    1 
ATOM   2608 C  C     . LYS A 1 317 ? 11.284  29.585  34.206  1.00 85.86  ? 317 LYS A C     1 
ATOM   2609 O  O     . LYS A 1 317 ? 12.255  30.350  34.234  1.00 78.39  ? 317 LYS A O     1 
ATOM   2610 C  CB    . LYS A 1 317 ? 9.488   29.774  35.946  1.00 78.71  ? 317 LYS A CB    1 
ATOM   2611 C  CG    . LYS A 1 317 ? 10.427  30.353  36.996  1.00 97.09  ? 317 LYS A CG    1 
ATOM   2612 C  CD    . LYS A 1 317 ? 9.750   30.452  38.354  1.00 98.21  ? 317 LYS A CD    1 
ATOM   2613 C  CE    . LYS A 1 317 ? 10.665  29.962  39.465  1.00 99.57  ? 317 LYS A CE    1 
ATOM   2614 N  NZ    . LYS A 1 317 ? 11.073  31.063  40.378  1.00 88.49  ? 317 LYS A NZ    1 
ATOM   2615 N  N     . VAL A 1 318 ? 11.411  28.290  33.912  1.00 83.31  ? 318 VAL A N     1 
ATOM   2616 C  CA    . VAL A 1 318 ? 12.741  27.709  33.758  1.00 73.39  ? 318 VAL A CA    1 
ATOM   2617 C  C     . VAL A 1 318 ? 13.357  28.086  32.414  1.00 79.22  ? 318 VAL A C     1 
ATOM   2618 O  O     . VAL A 1 318 ? 14.568  28.316  32.324  1.00 78.91  ? 318 VAL A O     1 
ATOM   2619 C  CB    . VAL A 1 318 ? 12.694  26.182  33.960  1.00 73.29  ? 318 VAL A CB    1 
ATOM   2620 C  CG1   . VAL A 1 318 ? 12.179  25.845  35.354  1.00 64.15  ? 318 VAL A CG1   1 
ATOM   2621 C  CG2   . VAL A 1 318 ? 11.847  25.510  32.890  1.00 82.12  ? 318 VAL A CG2   1 
ATOM   2622 N  N     . THR A 1 319 ? 12.549  28.159  31.349  1.00 74.65  ? 319 THR A N     1 
ATOM   2623 C  CA    . THR A 1 319 ? 13.096  28.547  30.051  1.00 74.57  ? 319 THR A CA    1 
ATOM   2624 C  C     . THR A 1 319 ? 13.594  29.984  30.073  1.00 77.78  ? 319 THR A C     1 
ATOM   2625 O  O     . THR A 1 319 ? 14.610  30.304  29.445  1.00 75.45  ? 319 THR A O     1 
ATOM   2626 C  CB    . THR A 1 319 ? 12.059  28.360  28.943  1.00 59.63  ? 319 THR A CB    1 
ATOM   2627 O  OG1   . THR A 1 319 ? 10.958  29.253  29.151  1.00 84.17  ? 319 THR A OG1   1 
ATOM   2628 C  CG2   . THR A 1 319 ? 11.569  26.921  28.892  1.00 68.25  ? 319 THR A CG2   1 
ATOM   2629 N  N     . TYR A 1 320 ? 12.891  30.867  30.785  1.00 79.82  ? 320 TYR A N     1 
ATOM   2630 C  CA    . TYR A 1 320 ? 13.398  32.221  30.974  1.00 72.09  ? 320 TYR A CA    1 
ATOM   2631 C  C     . TYR A 1 320 ? 14.712  32.206  31.743  1.00 76.73  ? 320 TYR A C     1 
ATOM   2632 O  O     . TYR A 1 320 ? 15.701  32.816  31.320  1.00 75.68  ? 320 TYR A O     1 
ATOM   2633 C  CB    . TYR A 1 320 ? 12.371  33.078  31.706  1.00 68.11  ? 320 TYR A CB    1 
ATOM   2634 C  CG    . TYR A 1 320 ? 12.887  34.464  31.988  1.00 78.36  ? 320 TYR A CG    1 
ATOM   2635 C  CD1   . TYR A 1 320 ? 13.142  35.350  30.951  1.00 74.34  ? 320 TYR A CD1   1 
ATOM   2636 C  CD2   . TYR A 1 320 ? 13.154  34.877  33.285  1.00 76.02  ? 320 TYR A CD2   1 
ATOM   2637 C  CE1   . TYR A 1 320 ? 13.627  36.616  31.200  1.00 83.07  ? 320 TYR A CE1   1 
ATOM   2638 C  CE2   . TYR A 1 320 ? 13.640  36.141  33.544  1.00 72.69  ? 320 TYR A CE2   1 
ATOM   2639 C  CZ    . TYR A 1 320 ? 13.873  37.007  32.497  1.00 87.99  ? 320 TYR A CZ    1 
ATOM   2640 O  OH    . TYR A 1 320 ? 14.358  38.270  32.746  1.00 94.18  ? 320 TYR A OH    1 
ATOM   2641 N  N     . GLU A 1 321 ? 14.733  31.513  32.885  1.00 82.67  ? 321 GLU A N     1 
ATOM   2642 C  CA    . GLU A 1 321 ? 15.960  31.396  33.666  1.00 76.05  ? 321 GLU A CA    1 
ATOM   2643 C  C     . GLU A 1 321 ? 17.091  30.817  32.827  1.00 78.84  ? 321 GLU A C     1 
ATOM   2644 O  O     . GLU A 1 321 ? 18.251  31.225  32.966  1.00 81.93  ? 321 GLU A O     1 
ATOM   2645 C  CB    . GLU A 1 321 ? 15.710  30.532  34.902  1.00 75.89  ? 321 GLU A CB    1 
ATOM   2646 C  CG    . GLU A 1 321 ? 16.127  31.174  36.218  1.00 94.13  ? 321 GLU A CG    1 
ATOM   2647 C  CD    . GLU A 1 321 ? 15.219  32.318  36.627  1.00 118.35 ? 321 GLU A CD    1 
ATOM   2648 O  OE1   . GLU A 1 321 ? 15.723  33.449  36.796  1.00 108.20 ? 321 GLU A OE1   1 
ATOM   2649 O  OE2   . GLU A 1 321 ? 14.001  32.086  36.780  1.00 116.58 ? 321 GLU A OE2   1 
ATOM   2650 N  N     . LEU A 1 322 ? 16.771  29.869  31.944  1.00 77.68  ? 322 LEU A N     1 
ATOM   2651 C  CA    . LEU A 1 322 ? 17.787  29.309  31.059  1.00 80.41  ? 322 LEU A CA    1 
ATOM   2652 C  C     . LEU A 1 322 ? 18.169  30.297  29.965  1.00 80.75  ? 322 LEU A C     1 
ATOM   2653 O  O     . LEU A 1 322 ? 19.337  30.365  29.563  1.00 76.78  ? 322 LEU A O     1 
ATOM   2654 C  CB    . LEU A 1 322 ? 17.285  28.002  30.448  1.00 63.77  ? 322 LEU A CB    1 
ATOM   2655 C  CG    . LEU A 1 322 ? 17.335  26.763  31.343  1.00 69.02  ? 322 LEU A CG    1 
ATOM   2656 C  CD1   . LEU A 1 322 ? 16.256  25.767  30.944  1.00 73.71  ? 322 LEU A CD1   1 
ATOM   2657 C  CD2   . LEU A 1 322 ? 18.711  26.120  31.289  1.00 65.39  ? 322 LEU A CD2   1 
ATOM   2658 N  N     . GLY A 1 323 ? 17.198  31.067  29.469  1.00 83.49  ? 323 GLY A N     1 
ATOM   2659 C  CA    . GLY A 1 323 ? 17.491  32.024  28.415  1.00 70.40  ? 323 GLY A CA    1 
ATOM   2660 C  C     . GLY A 1 323 ? 18.444  33.114  28.862  1.00 67.77  ? 323 GLY A C     1 
ATOM   2661 O  O     . GLY A 1 323 ? 19.355  33.497  28.123  1.00 62.04  ? 323 GLY A O     1 
ATOM   2662 N  N     . LYS A 1 324 ? 18.250  33.629  30.081  1.00 75.55  ? 324 LYS A N     1 
ATOM   2663 C  CA    . LYS A 1 324 ? 19.173  34.620  30.624  1.00 75.65  ? 324 LYS A CA    1 
ATOM   2664 C  C     . LYS A 1 324 ? 20.590  34.076  30.711  1.00 76.86  ? 324 LYS A C     1 
ATOM   2665 O  O     . LYS A 1 324 ? 21.556  34.848  30.695  1.00 65.85  ? 324 LYS A O     1 
ATOM   2666 C  CB    . LYS A 1 324 ? 18.705  35.072  32.008  1.00 79.52  ? 324 LYS A CB    1 
ATOM   2667 C  CG    . LYS A 1 324 ? 17.319  35.685  32.039  1.00 76.74  ? 324 LYS A CG    1 
ATOM   2668 C  CD    . LYS A 1 324 ? 17.208  36.713  33.156  1.00 81.92  ? 324 LYS A CD    1 
ATOM   2669 C  CE    . LYS A 1 324 ? 17.722  36.155  34.476  1.00 93.75  ? 324 LYS A CE    1 
ATOM   2670 N  NZ    . LYS A 1 324 ? 17.009  36.734  35.649  1.00 92.92  ? 324 LYS A NZ    1 
ATOM   2671 N  N     . GLU A 1 325 ? 20.733  32.755  30.801  1.00 75.30  ? 325 GLU A N     1 
ATOM   2672 C  CA    . GLU A 1 325 ? 22.047  32.137  30.927  1.00 73.08  ? 325 GLU A CA    1 
ATOM   2673 C  C     . GLU A 1 325 ? 22.746  32.028  29.576  1.00 74.39  ? 325 GLU A C     1 
ATOM   2674 O  O     . GLU A 1 325 ? 23.867  32.518  29.402  1.00 85.39  ? 325 GLU A O     1 
ATOM   2675 C  CB    . GLU A 1 325 ? 21.904  30.756  31.572  1.00 77.40  ? 325 GLU A CB    1 
ATOM   2676 C  CG    . GLU A 1 325 ? 23.180  29.937  31.585  1.00 81.01  ? 325 GLU A CG    1 
ATOM   2677 C  CD    . GLU A 1 325 ? 23.832  29.900  32.951  1.00 92.16  ? 325 GLU A CD    1 
ATOM   2678 O  OE1   . GLU A 1 325 ? 23.314  30.562  33.877  1.00 74.75  ? 325 GLU A OE1   1 
ATOM   2679 O  OE2   . GLU A 1 325 ? 24.860  29.204  33.097  1.00 93.87  ? 325 GLU A OE2   1 
ATOM   2680 N  N     . PHE A 1 326 ? 22.091  31.396  28.605  1.00 70.33  ? 326 PHE A N     1 
ATOM   2681 C  CA    . PHE A 1 326 ? 22.736  31.038  27.350  1.00 71.24  ? 326 PHE A CA    1 
ATOM   2682 C  C     . PHE A 1 326 ? 22.699  32.144  26.302  1.00 81.57  ? 326 PHE A C     1 
ATOM   2683 O  O     . PHE A 1 326 ? 23.429  32.050  25.309  1.00 88.79  ? 326 PHE A O     1 
ATOM   2684 C  CB    . PHE A 1 326 ? 22.097  29.767  26.779  1.00 59.03  ? 326 PHE A CB    1 
ATOM   2685 C  CG    . PHE A 1 326 ? 22.408  28.529  27.572  1.00 67.52  ? 326 PHE A CG    1 
ATOM   2686 C  CD1   . PHE A 1 326 ? 21.640  28.183  28.671  1.00 74.39  ? 326 PHE A CD1   1 
ATOM   2687 C  CD2   . PHE A 1 326 ? 23.478  27.719  27.226  1.00 73.04  ? 326 PHE A CD2   1 
ATOM   2688 C  CE1   . PHE A 1 326 ? 21.927  27.048  29.408  1.00 71.83  ? 326 PHE A CE1   1 
ATOM   2689 C  CE2   . PHE A 1 326 ? 23.771  26.583  27.957  1.00 65.42  ? 326 PHE A CE2   1 
ATOM   2690 C  CZ    . PHE A 1 326 ? 22.995  26.247  29.050  1.00 71.12  ? 326 PHE A CZ    1 
ATOM   2691 N  N     . LEU A 1 327 ? 21.885  33.189  26.490  1.00 74.60  ? 327 LEU A N     1 
ATOM   2692 C  CA    . LEU A 1 327 ? 21.837  34.247  25.480  1.00 77.23  ? 327 LEU A CA    1 
ATOM   2693 C  C     . LEU A 1 327 ? 23.108  35.088  25.441  1.00 75.63  ? 327 LEU A C     1 
ATOM   2694 O  O     . LEU A 1 327 ? 23.622  35.332  24.335  1.00 79.79  ? 327 LEU A O     1 
ATOM   2695 C  CB    . LEU A 1 327 ? 20.607  35.133  25.687  1.00 79.72  ? 327 LEU A CB    1 
ATOM   2696 C  CG    . LEU A 1 327 ? 20.393  36.023  24.456  1.00 84.73  ? 327 LEU A CG    1 
ATOM   2697 C  CD1   . LEU A 1 327 ? 19.161  35.603  23.660  1.00 72.12  ? 327 LEU A CD1   1 
ATOM   2698 C  CD2   . LEU A 1 327 ? 20.354  37.500  24.794  1.00 76.15  ? 327 LEU A CD2   1 
ATOM   2699 N  N     . PRO A 1 328 ? 23.652  35.584  26.564  1.00 71.32  ? 328 PRO A N     1 
ATOM   2700 C  CA    . PRO A 1 328 ? 24.827  36.468  26.463  1.00 82.16  ? 328 PRO A CA    1 
ATOM   2701 C  C     . PRO A 1 328 ? 26.014  35.837  25.757  1.00 83.35  ? 328 PRO A C     1 
ATOM   2702 O  O     . PRO A 1 328 ? 26.775  36.552  25.093  1.00 84.77  ? 328 PRO A O     1 
ATOM   2703 C  CB    . PRO A 1 328 ? 25.153  36.797  27.930  1.00 85.37  ? 328 PRO A CB    1 
ATOM   2704 C  CG    . PRO A 1 328 ? 24.459  35.756  28.732  1.00 97.06  ? 328 PRO A CG    1 
ATOM   2705 C  CD    . PRO A 1 328 ? 23.219  35.438  27.964  1.00 84.95  ? 328 PRO A CD    1 
ATOM   2706 N  N     . MET A 1 329 ? 26.203  34.522  25.879  1.00 84.63  ? 329 MET A N     1 
ATOM   2707 C  CA    . MET A 1 329 ? 27.247  33.865  25.100  1.00 77.55  ? 329 MET A CA    1 
ATOM   2708 C  C     . MET A 1 329 ? 26.901  33.860  23.616  1.00 77.88  ? 329 MET A C     1 
ATOM   2709 O  O     . MET A 1 329 ? 27.763  34.125  22.770  1.00 74.57  ? 329 MET A O     1 
ATOM   2710 C  CB    . MET A 1 329 ? 27.467  32.440  25.607  1.00 86.16  ? 329 MET A CB    1 
ATOM   2711 C  CG    . MET A 1 329 ? 28.306  31.584  24.673  1.00 101.16 ? 329 MET A CG    1 
ATOM   2712 S  SD    . MET A 1 329 ? 29.451  30.491  25.534  1.00 127.82 ? 329 MET A SD    1 
ATOM   2713 C  CE    . MET A 1 329 ? 29.471  29.090  24.418  1.00 67.75  ? 329 MET A CE    1 
ATOM   2714 N  N     . GLU A 1 330 ? 25.638  33.573  23.284  1.00 83.98  ? 330 GLU A N     1 
ATOM   2715 C  CA    . GLU A 1 330 ? 25.204  33.598  21.892  1.00 60.07  ? 330 GLU A CA    1 
ATOM   2716 C  C     . GLU A 1 330 ? 25.351  34.982  21.278  1.00 59.11  ? 330 GLU A C     1 
ATOM   2717 O  O     . GLU A 1 330 ? 25.494  35.106  20.056  1.00 52.40  ? 330 GLU A O     1 
ATOM   2718 C  CB    . GLU A 1 330 ? 23.756  33.130  21.793  1.00 65.49  ? 330 GLU A CB    1 
ATOM   2719 C  CG    . GLU A 1 330 ? 23.581  31.685  22.142  1.00 66.81  ? 330 GLU A CG    1 
ATOM   2720 C  CD    . GLU A 1 330 ? 24.494  30.810  21.331  1.00 77.07  ? 330 GLU A CD    1 
ATOM   2721 O  OE1   . GLU A 1 330 ? 24.384  30.824  20.087  1.00 58.76  ? 330 GLU A OE1   1 
ATOM   2722 O  OE2   . GLU A 1 330 ? 25.341  30.116  21.932  1.00 84.84  ? 330 GLU A OE2   1 
ATOM   2723 N  N     . ALA A 1 331 ? 25.308  36.029  22.102  1.00 62.51  ? 331 ALA A N     1 
ATOM   2724 C  CA    . ALA A 1 331 ? 25.528  37.377  21.594  1.00 64.55  ? 331 ALA A CA    1 
ATOM   2725 C  C     . ALA A 1 331 ? 26.979  37.577  21.175  1.00 70.95  ? 331 ALA A C     1 
ATOM   2726 O  O     . ALA A 1 331 ? 27.254  38.222  20.156  1.00 67.84  ? 331 ALA A O     1 
ATOM   2727 C  CB    . ALA A 1 331 ? 25.124  38.404  22.650  1.00 67.24  ? 331 ALA A CB    1 
ATOM   2728 N  N     . GLN A 1 332 ? 27.920  37.030  21.949  1.00 76.87  ? 332 GLN A N     1 
ATOM   2729 C  CA    . GLN A 1 332 ? 29.331  37.152  21.596  1.00 67.45  ? 332 GLN A CA    1 
ATOM   2730 C  C     . GLN A 1 332 ? 29.634  36.424  20.294  1.00 56.71  ? 332 GLN A C     1 
ATOM   2731 O  O     . GLN A 1 332 ? 30.415  36.911  19.469  1.00 67.58  ? 332 GLN A O     1 
ATOM   2732 C  CB    . GLN A 1 332 ? 30.206  36.617  22.729  1.00 81.28  ? 332 GLN A CB    1 
ATOM   2733 C  CG    . GLN A 1 332 ? 30.030  37.361  24.038  1.00 92.98  ? 332 GLN A CG    1 
ATOM   2734 C  CD    . GLN A 1 332 ? 30.216  38.858  23.881  1.00 98.20  ? 332 GLN A CD    1 
ATOM   2735 O  OE1   . GLN A 1 332 ? 31.325  39.336  23.644  1.00 102.27 ? 332 GLN A OE1   1 
ATOM   2736 N  NE2   . GLN A 1 332 ? 29.125  39.604  24.007  1.00 90.40  ? 332 GLN A NE2   1 
ATOM   2737 N  N     . LEU A 1 333 ? 29.020  35.256  20.092  1.00 52.08  ? 333 LEU A N     1 
ATOM   2738 C  CA    . LEU A 1 333 ? 29.159  34.561  18.817  1.00 49.87  ? 333 LEU A CA    1 
ATOM   2739 C  C     . LEU A 1 333 ? 28.639  35.417  17.669  1.00 55.76  ? 333 LEU A C     1 
ATOM   2740 O  O     . LEU A 1 333 ? 29.195  35.394  16.565  1.00 60.25  ? 333 LEU A O     1 
ATOM   2741 C  CB    . LEU A 1 333 ? 28.422  33.224  18.866  1.00 51.99  ? 333 LEU A CB    1 
ATOM   2742 C  CG    . LEU A 1 333 ? 28.466  32.385  17.587  1.00 55.09  ? 333 LEU A CG    1 
ATOM   2743 C  CD1   . LEU A 1 333 ? 29.884  31.917  17.299  1.00 48.11  ? 333 LEU A CD1   1 
ATOM   2744 C  CD2   . LEU A 1 333 ? 27.513  31.206  17.685  1.00 51.35  ? 333 LEU A CD2   1 
ATOM   2745 N  N     A SER A 1 334 ? 27.574  36.185  17.915  0.66 62.52  ? 334 SER A N     1 
ATOM   2746 N  N     B SER A 1 334 ? 27.571  36.182  17.912  0.34 63.14  ? 334 SER A N     1 
ATOM   2747 C  CA    A SER A 1 334 ? 27.029  37.055  16.879  0.66 59.23  ? 334 SER A CA    1 
ATOM   2748 C  CA    B SER A 1 334 ? 27.030  37.050  16.871  0.34 61.80  ? 334 SER A CA    1 
ATOM   2749 C  C     A SER A 1 334 ? 28.026  38.141  16.496  0.66 59.16  ? 334 SER A C     1 
ATOM   2750 C  C     B SER A 1 334 ? 28.018  38.148  16.496  0.34 58.06  ? 334 SER A C     1 
ATOM   2751 O  O     A SER A 1 334 ? 28.252  38.402  15.309  0.66 62.47  ? 334 SER A O     1 
ATOM   2752 O  O     B SER A 1 334 ? 28.224  38.426  15.309  0.34 64.69  ? 334 SER A O     1 
ATOM   2753 C  CB    A SER A 1 334 ? 25.711  37.671  17.353  0.66 69.03  ? 334 SER A CB    1 
ATOM   2754 C  CB    B SER A 1 334 ? 25.704  37.655  17.331  0.34 67.80  ? 334 SER A CB    1 
ATOM   2755 O  OG    A SER A 1 334 ? 25.143  38.501  16.355  0.66 54.16  ? 334 SER A OG    1 
ATOM   2756 O  OG    B SER A 1 334 ? 24.943  36.712  18.063  0.34 62.26  ? 334 SER A OG    1 
ATOM   2757 N  N     . ARG A 1 335 ? 28.638  38.783  17.493  1.00 56.23  ? 335 ARG A N     1 
ATOM   2758 C  CA    . ARG A 1 335 ? 29.635  39.808  17.204  1.00 60.58  ? 335 ARG A CA    1 
ATOM   2759 C  C     . ARG A 1 335 ? 30.857  39.210  16.521  1.00 62.05  ? 335 ARG A C     1 
ATOM   2760 O  O     . ARG A 1 335 ? 31.423  39.819  15.606  1.00 64.52  ? 335 ARG A O     1 
ATOM   2761 C  CB    . ARG A 1 335 ? 30.045  40.533  18.486  1.00 65.14  ? 335 ARG A CB    1 
ATOM   2762 C  CG    . ARG A 1 335 ? 28.888  41.070  19.303  1.00 71.76  ? 335 ARG A CG    1 
ATOM   2763 C  CD    . ARG A 1 335 ? 29.280  41.323  20.755  1.00 73.40  ? 335 ARG A CD    1 
ATOM   2764 N  NE    . ARG A 1 335 ? 30.176  42.466  20.887  1.00 94.16  ? 335 ARG A NE    1 
ATOM   2765 C  CZ    . ARG A 1 335 ? 31.452  42.387  21.238  1.00 93.45  ? 335 ARG A CZ    1 
ATOM   2766 N  NH1   . ARG A 1 335 ? 32.008  41.235  21.572  1.00 84.27  ? 335 ARG A NH1   1 
ATOM   2767 N  NH2   . ARG A 1 335 ? 32.184  43.497  21.271  1.00 86.36  ? 335 ARG A NH2   1 
ATOM   2768 N  N     . LEU A 1 336 ? 31.276  38.017  16.951  1.00 55.31  ? 336 LEU A N     1 
ATOM   2769 C  CA    . LEU A 1 336 ? 32.459  37.390  16.366  1.00 53.31  ? 336 LEU A CA    1 
ATOM   2770 C  C     . LEU A 1 336 ? 32.227  37.008  14.910  1.00 56.52  ? 336 LEU A C     1 
ATOM   2771 O  O     . LEU A 1 336 ? 33.095  37.230  14.056  1.00 66.24  ? 336 LEU A O     1 
ATOM   2772 C  CB    . LEU A 1 336 ? 32.859  36.163  17.185  1.00 69.82  ? 336 LEU A CB    1 
ATOM   2773 C  CG    . LEU A 1 336 ? 34.222  35.528  16.883  1.00 70.07  ? 336 LEU A CG    1 
ATOM   2774 C  CD1   . LEU A 1 336 ? 35.316  36.575  16.729  1.00 57.24  ? 336 LEU A CD1   1 
ATOM   2775 C  CD2   . LEU A 1 336 ? 34.593  34.529  17.969  1.00 70.24  ? 336 LEU A CD2   1 
ATOM   2776 N  N     . ILE A 1 337 ? 31.066  36.428  14.607  1.00 68.85  ? 337 ILE A N     1 
ATOM   2777 C  CA    . ILE A 1 337 ? 30.780  35.989  13.247  1.00 47.83  ? 337 ILE A CA    1 
ATOM   2778 C  C     . ILE A 1 337 ? 30.228  37.110  12.372  1.00 51.64  ? 337 ILE A C     1 
ATOM   2779 O  O     . ILE A 1 337 ? 30.380  37.058  11.143  1.00 58.78  ? 337 ILE A O     1 
ATOM   2780 C  CB    . ILE A 1 337 ? 29.813  34.791  13.283  1.00 38.17  ? 337 ILE A CB    1 
ATOM   2781 C  CG1   . ILE A 1 337 ? 30.371  33.705  14.199  1.00 50.53  ? 337 ILE A CG1   1 
ATOM   2782 C  CG2   . ILE A 1 337 ? 29.596  34.216  11.895  1.00 50.78  ? 337 ILE A CG2   1 
ATOM   2783 C  CD1   . ILE A 1 337 ? 31.655  33.090  13.694  1.00 56.11  ? 337 ILE A CD1   1 
ATOM   2784 N  N     . GLY A 1 338 ? 29.619  38.133  12.963  1.00 54.78  ? 338 GLY A N     1 
ATOM   2785 C  CA    . GLY A 1 338 ? 29.057  39.211  12.175  1.00 53.86  ? 338 GLY A CA    1 
ATOM   2786 C  C     . GLY A 1 338 ? 27.728  38.890  11.534  1.00 58.87  ? 338 GLY A C     1 
ATOM   2787 O  O     . GLY A 1 338 ? 27.453  39.359  10.425  1.00 57.28  ? 338 GLY A O     1 
ATOM   2788 N  N     . GLN A 1 339 ? 26.897  38.090  12.197  1.00 51.17  ? 339 GLN A N     1 
ATOM   2789 C  CA    . GLN A 1 339 ? 25.569  37.756  11.708  1.00 57.56  ? 339 GLN A CA    1 
ATOM   2790 C  C     . GLN A 1 339 ? 24.598  37.807  12.878  1.00 60.14  ? 339 GLN A C     1 
ATOM   2791 O  O     . GLN A 1 339 ? 24.999  37.831  14.044  1.00 53.08  ? 339 GLN A O     1 
ATOM   2792 C  CB    . GLN A 1 339 ? 25.544  36.380  11.032  1.00 62.91  ? 339 GLN A CB    1 
ATOM   2793 C  CG    . GLN A 1 339 ? 26.316  36.314  9.724   1.00 51.36  ? 339 GLN A CG    1 
ATOM   2794 C  CD    . GLN A 1 339 ? 25.831  37.332  8.711   1.00 58.25  ? 339 GLN A CD    1 
ATOM   2795 O  OE1   . GLN A 1 339 ? 24.628  37.531  8.541   1.00 77.37  ? 339 GLN A OE1   1 
ATOM   2796 N  NE2   . GLN A 1 339 ? 26.768  37.985  8.033   1.00 53.22  ? 339 GLN A NE2   1 
ATOM   2797 N  N     . SER A 1 340 ? 23.307  37.825  12.556  1.00 62.37  ? 340 SER A N     1 
ATOM   2798 C  CA    . SER A 1 340 ? 22.286  37.992  13.581  1.00 48.13  ? 340 SER A CA    1 
ATOM   2799 C  C     . SER A 1 340 ? 22.330  36.846  14.585  1.00 53.61  ? 340 SER A C     1 
ATOM   2800 O  O     . SER A 1 340 ? 22.694  35.713  14.256  1.00 50.77  ? 340 SER A O     1 
ATOM   2801 C  CB    . SER A 1 340 ? 20.900  38.074  12.943  1.00 53.78  ? 340 SER A CB    1 
ATOM   2802 O  OG    . SER A 1 340 ? 20.476  36.801  12.486  1.00 63.87  ? 340 SER A OG    1 
ATOM   2803 N  N     . LEU A 1 341 ? 21.967  37.162  15.831  1.00 48.94  ? 341 LEU A N     1 
ATOM   2804 C  CA    . LEU A 1 341 ? 21.854  36.130  16.857  1.00 52.71  ? 341 LEU A CA    1 
ATOM   2805 C  C     . LEU A 1 341 ? 20.904  35.029  16.410  1.00 63.13  ? 341 LEU A C     1 
ATOM   2806 O  O     . LEU A 1 341 ? 21.175  33.841  16.619  1.00 66.72  ? 341 LEU A O     1 
ATOM   2807 C  CB    . LEU A 1 341 ? 21.386  36.756  18.175  1.00 58.35  ? 341 LEU A CB    1 
ATOM   2808 C  CG    . LEU A 1 341 ? 20.822  35.923  19.337  1.00 65.86  ? 341 LEU A CG    1 
ATOM   2809 C  CD1   . LEU A 1 341 ? 21.588  34.634  19.586  1.00 53.31  ? 341 LEU A CD1   1 
ATOM   2810 C  CD2   . LEU A 1 341 ? 20.781  36.763  20.602  1.00 63.73  ? 341 LEU A CD2   1 
ATOM   2811 N  N     . TRP A 1 342 ? 19.791  35.406  15.776  1.00 59.53  ? 342 TRP A N     1 
ATOM   2812 C  CA    . TRP A 1 342 ? 18.856  34.412  15.261  1.00 60.82  ? 342 TRP A CA    1 
ATOM   2813 C  C     . TRP A 1 342 ? 19.551  33.427  14.330  1.00 53.94  ? 342 TRP A C     1 
ATOM   2814 O  O     . TRP A 1 342 ? 19.252  32.228  14.348  1.00 56.40  ? 342 TRP A O     1 
ATOM   2815 C  CB    . TRP A 1 342 ? 17.700  35.105  14.536  1.00 70.56  ? 342 TRP A CB    1 
ATOM   2816 C  CG    . TRP A 1 342 ? 16.568  34.183  14.208  1.00 55.81  ? 342 TRP A CG    1 
ATOM   2817 C  CD1   . TRP A 1 342 ? 15.434  33.990  14.938  1.00 55.53  ? 342 TRP A CD1   1 
ATOM   2818 C  CD2   . TRP A 1 342 ? 16.463  33.324  13.066  1.00 55.79  ? 342 TRP A CD2   1 
ATOM   2819 N  NE1   . TRP A 1 342 ? 14.627  33.065  14.323  1.00 58.23  ? 342 TRP A NE1   1 
ATOM   2820 C  CE2   . TRP A 1 342 ? 15.236  32.641  13.171  1.00 53.93  ? 342 TRP A CE2   1 
ATOM   2821 C  CE3   . TRP A 1 342 ? 17.285  33.068  11.965  1.00 50.44  ? 342 TRP A CE3   1 
ATOM   2822 C  CZ2   . TRP A 1 342 ? 14.812  31.718  12.219  1.00 50.12  ? 342 TRP A CZ2   1 
ATOM   2823 C  CZ3   . TRP A 1 342 ? 16.863  32.151  11.021  1.00 55.65  ? 342 TRP A CZ3   1 
ATOM   2824 C  CH2   . TRP A 1 342 ? 15.637  31.488  11.154  1.00 52.80  ? 342 TRP A CH2   1 
ATOM   2825 N  N     . ASP A 1 343 ? 20.493  33.911  13.520  1.00 55.49  ? 343 ASP A N     1 
ATOM   2826 C  CA    . ASP A 1 343 ? 21.162  33.041  12.559  1.00 61.56  ? 343 ASP A CA    1 
ATOM   2827 C  C     . ASP A 1 343 ? 22.268  32.219  13.214  1.00 59.15  ? 343 ASP A C     1 
ATOM   2828 O  O     . ASP A 1 343 ? 22.328  30.997  13.038  1.00 58.99  ? 343 ASP A O     1 
ATOM   2829 C  CB    . ASP A 1 343 ? 21.719  33.869  11.399  1.00 63.66  ? 343 ASP A CB    1 
ATOM   2830 C  CG    . ASP A 1 343 ? 20.646  34.268  10.398  1.00 58.05  ? 343 ASP A CG    1 
ATOM   2831 O  OD1   . ASP A 1 343 ? 20.211  33.400  9.612   1.00 59.22  ? 343 ASP A OD1   1 
ATOM   2832 O  OD2   . ASP A 1 343 ? 20.237  35.448  10.398  1.00 64.45  ? 343 ASP A OD2   1 
ATOM   2833 N  N     . VAL A 1 344 ? 23.154  32.867  13.975  1.00 53.42  ? 344 VAL A N     1 
ATOM   2834 C  CA    . VAL A 1 344 ? 24.288  32.145  14.545  1.00 63.72  ? 344 VAL A CA    1 
ATOM   2835 C  C     . VAL A 1 344 ? 23.858  31.161  15.624  1.00 61.38  ? 344 VAL A C     1 
ATOM   2836 O  O     . VAL A 1 344 ? 24.612  30.237  15.948  1.00 60.44  ? 344 VAL A O     1 
ATOM   2837 C  CB    . VAL A 1 344 ? 25.339  33.122  15.106  1.00 52.29  ? 344 VAL A CB    1 
ATOM   2838 C  CG1   . VAL A 1 344 ? 25.861  34.026  14.002  1.00 52.54  ? 344 VAL A CG1   1 
ATOM   2839 C  CG2   . VAL A 1 344 ? 24.760  33.934  16.254  1.00 61.46  ? 344 VAL A CG2   1 
ATOM   2840 N  N     . SER A 1 345 ? 22.662  31.325  16.192  1.00 69.84  ? 345 SER A N     1 
ATOM   2841 C  CA    . SER A 1 345 ? 22.229  30.423  17.252  1.00 64.93  ? 345 SER A CA    1 
ATOM   2842 C  C     . SER A 1 345 ? 21.801  29.063  16.721  1.00 51.84  ? 345 SER A C     1 
ATOM   2843 O  O     . SER A 1 345 ? 21.759  28.098  17.491  1.00 56.28  ? 345 SER A O     1 
ATOM   2844 C  CB    . SER A 1 345 ? 21.087  31.053  18.046  1.00 49.98  ? 345 SER A CB    1 
ATOM   2845 O  OG    . SER A 1 345 ? 20.055  31.476  17.175  1.00 68.72  ? 345 SER A OG    1 
ATOM   2846 N  N     . ARG A 1 346 ? 21.483  28.962  15.430  1.00 54.60  ? 346 ARG A N     1 
ATOM   2847 C  CA    . ARG A 1 346 ? 21.089  27.700  14.822  1.00 57.29  ? 346 ARG A CA    1 
ATOM   2848 C  C     . ARG A 1 346 ? 22.042  27.243  13.728  1.00 65.75  ? 346 ARG A C     1 
ATOM   2849 O  O     . ARG A 1 346 ? 21.771  26.227  13.076  1.00 66.53  ? 346 ARG A O     1 
ATOM   2850 C  CB    . ARG A 1 346 ? 19.673  27.805  14.242  1.00 54.60  ? 346 ARG A CB    1 
ATOM   2851 C  CG    . ARG A 1 346 ? 18.684  28.473  15.169  1.00 57.67  ? 346 ARG A CG    1 
ATOM   2852 C  CD    . ARG A 1 346 ? 17.778  29.421  14.415  1.00 62.37  ? 346 ARG A CD    1 
ATOM   2853 N  NE    . ARG A 1 346 ? 17.314  30.495  15.282  1.00 71.99  ? 346 ARG A NE    1 
ATOM   2854 C  CZ    . ARG A 1 346 ? 16.167  30.474  15.944  1.00 58.46  ? 346 ARG A CZ    1 
ATOM   2855 N  NH1   . ARG A 1 346 ? 15.327  29.462  15.835  1.00 57.98  ? 346 ARG A NH1   1 
ATOM   2856 N  NH2   . ARG A 1 346 ? 15.857  31.494  16.737  1.00 69.36  ? 346 ARG A NH2   1 
ATOM   2857 N  N     . SER A 1 347 ? 23.143  27.954  13.510  1.00 69.61  ? 347 SER A N     1 
ATOM   2858 C  CA    . SER A 1 347 ? 24.048  27.632  12.418  1.00 59.86  ? 347 SER A CA    1 
ATOM   2859 C  C     . SER A 1 347 ? 25.026  26.540  12.826  1.00 65.00  ? 347 SER A C     1 
ATOM   2860 O  O     . SER A 1 347 ? 25.481  26.485  13.972  1.00 58.69  ? 347 SER A O     1 
ATOM   2861 C  CB    . SER A 1 347 ? 24.815  28.880  11.984  1.00 62.79  ? 347 SER A CB    1 
ATOM   2862 O  OG    . SER A 1 347 ? 23.980  29.739  11.229  1.00 78.06  ? 347 SER A OG    1 
ATOM   2863 N  N     . SER A 1 348 ? 25.340  25.663  11.876  1.00 58.44  ? 348 SER A N     1 
ATOM   2864 C  CA    . SER A 1 348 ? 26.384  24.675  12.085  1.00 57.49  ? 348 SER A CA    1 
ATOM   2865 C  C     . SER A 1 348 ? 27.750  25.355  12.134  1.00 60.48  ? 348 SER A C     1 
ATOM   2866 O  O     . SER A 1 348 ? 27.932  26.481  11.661  1.00 69.87  ? 348 SER A O     1 
ATOM   2867 C  CB    . SER A 1 348 ? 26.357  23.624  10.975  1.00 64.61  ? 348 SER A CB    1 
ATOM   2868 O  OG    . SER A 1 348 ? 26.974  24.112  9.796   1.00 72.75  ? 348 SER A OG    1 
ATOM   2869 N  N     . THR A 1 349 ? 28.719  24.652  12.723  1.00 69.76  ? 349 THR A N     1 
ATOM   2870 C  CA    . THR A 1 349 ? 30.066  25.203  12.839  1.00 58.92  ? 349 THR A CA    1 
ATOM   2871 C  C     . THR A 1 349 ? 30.636  25.559  11.470  1.00 60.33  ? 349 THR A C     1 
ATOM   2872 O  O     . THR A 1 349 ? 31.280  26.603  11.309  1.00 61.23  ? 349 THR A O     1 
ATOM   2873 C  CB    . THR A 1 349 ? 30.975  24.212  13.566  1.00 55.60  ? 349 THR A CB    1 
ATOM   2874 O  OG1   . THR A 1 349 ? 30.643  24.198  14.960  1.00 66.99  ? 349 THR A OG1   1 
ATOM   2875 C  CG2   . THR A 1 349 ? 32.437  24.602  13.407  1.00 62.84  ? 349 THR A CG2   1 
ATOM   2876 N  N     . GLY A 1 350 ? 30.388  24.715  10.467  1.00 57.73  ? 350 GLY A N     1 
ATOM   2877 C  CA    . GLY A 1 350 ? 30.877  25.013  9.131   1.00 49.31  ? 350 GLY A CA    1 
ATOM   2878 C  C     . GLY A 1 350 ? 30.322  26.315  8.586   1.00 66.64  ? 350 GLY A C     1 
ATOM   2879 O  O     . GLY A 1 350 ? 31.065  27.155  8.072   1.00 64.39  ? 350 GLY A O     1 
ATOM   2880 N  N     . ASN A 1 351 ? 29.006  26.504  8.703   1.00 68.02  ? 351 ASN A N     1 
ATOM   2881 C  CA    . ASN A 1 351 ? 28.384  27.714  8.175   1.00 62.94  ? 351 ASN A CA    1 
ATOM   2882 C  C     . ASN A 1 351 ? 28.806  28.955  8.951   1.00 58.45  ? 351 ASN A C     1 
ATOM   2883 O  O     . ASN A 1 351 ? 28.884  30.045  8.374   1.00 58.87  ? 351 ASN A O     1 
ATOM   2884 C  CB    . ASN A 1 351 ? 26.863  27.570  8.186   1.00 55.58  ? 351 ASN A CB    1 
ATOM   2885 C  CG    . ASN A 1 351 ? 26.350  26.773  7.006   1.00 65.31  ? 351 ASN A CG    1 
ATOM   2886 O  OD1   . ASN A 1 351 ? 26.984  26.725  5.953   1.00 70.83  ? 351 ASN A OD1   1 
ATOM   2887 N  ND2   . ASN A 1 351 ? 25.196  26.139  7.177   1.00 71.06  ? 351 ASN A ND2   1 
ATOM   2888 N  N     . LEU A 1 352 ? 29.077  28.815  10.251  1.00 56.31  ? 352 LEU A N     1 
ATOM   2889 C  CA    . LEU A 1 352 ? 29.574  29.949  11.022  1.00 55.32  ? 352 LEU A CA    1 
ATOM   2890 C  C     . LEU A 1 352 ? 30.950  30.382  10.534  1.00 61.13  ? 352 LEU A C     1 
ATOM   2891 O  O     . LEU A 1 352 ? 31.267  31.577  10.524  1.00 65.55  ? 352 LEU A O     1 
ATOM   2892 C  CB    . LEU A 1 352 ? 29.624  29.599  12.509  1.00 53.57  ? 352 LEU A CB    1 
ATOM   2893 C  CG    . LEU A 1 352 ? 28.292  29.491  13.250  1.00 56.66  ? 352 LEU A CG    1 
ATOM   2894 C  CD1   . LEU A 1 352 ? 28.354  28.385  14.288  1.00 54.49  ? 352 LEU A CD1   1 
ATOM   2895 C  CD2   . LEU A 1 352 ? 27.936  30.814  13.904  1.00 67.00  ? 352 LEU A CD2   1 
ATOM   2896 N  N     . VAL A 1 353 ? 31.779  29.423  10.120  1.00 63.63  ? 353 VAL A N     1 
ATOM   2897 C  CA    . VAL A 1 353 ? 33.124  29.748  9.654   1.00 60.29  ? 353 VAL A CA    1 
ATOM   2898 C  C     . VAL A 1 353 ? 33.064  30.434  8.296   1.00 59.48  ? 353 VAL A C     1 
ATOM   2899 O  O     . VAL A 1 353 ? 33.744  31.440  8.060   1.00 63.17  ? 353 VAL A O     1 
ATOM   2900 C  CB    . VAL A 1 353 ? 33.992  28.480  9.611   1.00 59.27  ? 353 VAL A CB    1 
ATOM   2901 C  CG1   . VAL A 1 353 ? 35.253  28.720  8.797   1.00 60.17  ? 353 VAL A CG1   1 
ATOM   2902 C  CG2   . VAL A 1 353 ? 34.335  28.045  11.015  1.00 59.89  ? 353 VAL A CG2   1 
ATOM   2903 N  N     . GLU A 1 354 ? 32.251  29.895  7.383   1.00 54.28  ? 354 GLU A N     1 
ATOM   2904 C  CA    . GLU A 1 354 ? 32.103  30.495  6.062   1.00 57.31  ? 354 GLU A CA    1 
ATOM   2905 C  C     . GLU A 1 354 ? 31.689  31.957  6.158   1.00 65.65  ? 354 GLU A C     1 
ATOM   2906 O  O     . GLU A 1 354 ? 32.223  32.811  5.441   1.00 64.23  ? 354 GLU A O     1 
ATOM   2907 C  CB    . GLU A 1 354 ? 31.083  29.703  5.244   1.00 64.19  ? 354 GLU A CB    1 
ATOM   2908 C  CG    . GLU A 1 354 ? 30.930  30.183  3.817   1.00 70.69  ? 354 GLU A CG    1 
ATOM   2909 C  CD    . GLU A 1 354 ? 29.535  29.954  3.277   1.00 75.38  ? 354 GLU A CD    1 
ATOM   2910 O  OE1   . GLU A 1 354 ? 28.572  30.023  4.069   1.00 82.16  ? 354 GLU A OE1   1 
ATOM   2911 O  OE2   . GLU A 1 354 ? 29.397  29.719  2.059   1.00 80.28  ? 354 GLU A OE2   1 
ATOM   2912 N  N     . TRP A 1 355 ? 30.740  32.264  7.045   1.00 58.82  ? 355 TRP A N     1 
ATOM   2913 C  CA    . TRP A 1 355 ? 30.320  33.650  7.222   1.00 64.80  ? 355 TRP A CA    1 
ATOM   2914 C  C     . TRP A 1 355 ? 31.456  34.501  7.773   1.00 56.46  ? 355 TRP A C     1 
ATOM   2915 O  O     . TRP A 1 355 ? 31.658  35.640  7.336   1.00 67.14  ? 355 TRP A O     1 
ATOM   2916 C  CB    . TRP A 1 355 ? 29.103  33.713  8.143   1.00 61.99  ? 355 TRP A CB    1 
ATOM   2917 C  CG    . TRP A 1 355 ? 27.817  33.384  7.452   1.00 64.37  ? 355 TRP A CG    1 
ATOM   2918 C  CD1   . TRP A 1 355 ? 27.556  33.476  6.116   1.00 69.52  ? 355 TRP A CD1   1 
ATOM   2919 C  CD2   . TRP A 1 355 ? 26.614  32.908  8.065   1.00 65.70  ? 355 TRP A CD2   1 
ATOM   2920 N  NE1   . TRP A 1 355 ? 26.263  33.088  5.859   1.00 71.49  ? 355 TRP A NE1   1 
ATOM   2921 C  CE2   . TRP A 1 355 ? 25.664  32.734  7.039   1.00 65.57  ? 355 TRP A CE2   1 
ATOM   2922 C  CE3   . TRP A 1 355 ? 26.248  32.613  9.381   1.00 70.75  ? 355 TRP A CE3   1 
ATOM   2923 C  CZ2   . TRP A 1 355 ? 24.372  32.278  7.289   1.00 73.18  ? 355 TRP A CZ2   1 
ATOM   2924 C  CZ3   . TRP A 1 355 ? 24.966  32.162  9.627   1.00 62.80  ? 355 TRP A CZ3   1 
ATOM   2925 C  CH2   . TRP A 1 355 ? 24.043  31.998  8.587   1.00 64.78  ? 355 TRP A CH2   1 
ATOM   2926 N  N     . PHE A 1 356 ? 32.209  33.966  8.737   1.00 62.33  ? 356 PHE A N     1 
ATOM   2927 C  CA    . PHE A 1 356 ? 33.384  34.672  9.239   1.00 62.76  ? 356 PHE A CA    1 
ATOM   2928 C  C     . PHE A 1 356 ? 34.404  34.895  8.131   1.00 66.04  ? 356 PHE A C     1 
ATOM   2929 O  O     . PHE A 1 356 ? 34.981  35.983  8.014   1.00 58.94  ? 356 PHE A O     1 
ATOM   2930 C  CB    . PHE A 1 356 ? 34.007  33.888  10.395  1.00 56.67  ? 356 PHE A CB    1 
ATOM   2931 C  CG    . PHE A 1 356 ? 35.220  34.543  10.990  1.00 59.71  ? 356 PHE A CG    1 
ATOM   2932 C  CD1   . PHE A 1 356 ? 35.094  35.650  11.813  1.00 59.91  ? 356 PHE A CD1   1 
ATOM   2933 C  CD2   . PHE A 1 356 ? 36.487  34.050  10.727  1.00 58.63  ? 356 PHE A CD2   1 
ATOM   2934 C  CE1   . PHE A 1 356 ? 36.210  36.252  12.362  1.00 61.49  ? 356 PHE A CE1   1 
ATOM   2935 C  CE2   . PHE A 1 356 ? 37.605  34.648  11.271  1.00 54.94  ? 356 PHE A CE2   1 
ATOM   2936 C  CZ    . PHE A 1 356 ? 37.467  35.751  12.090  1.00 60.59  ? 356 PHE A CZ    1 
ATOM   2937 N  N     . LEU A 1 357 ? 34.633  33.875  7.301   1.00 62.51  ? 357 LEU A N     1 
ATOM   2938 C  CA    . LEU A 1 357 ? 35.591  34.003  6.208   1.00 53.44  ? 357 LEU A CA    1 
ATOM   2939 C  C     . LEU A 1 357 ? 35.098  34.984  5.151   1.00 61.59  ? 357 LEU A C     1 
ATOM   2940 O  O     . LEU A 1 357 ? 35.884  35.778  4.621   1.00 60.31  ? 357 LEU A O     1 
ATOM   2941 C  CB    . LEU A 1 357 ? 35.856  32.632  5.588   1.00 56.57  ? 357 LEU A CB    1 
ATOM   2942 C  CG    . LEU A 1 357 ? 36.609  31.627  6.464   1.00 58.78  ? 357 LEU A CG    1 
ATOM   2943 C  CD1   . LEU A 1 357 ? 37.054  30.421  5.650   1.00 62.83  ? 357 LEU A CD1   1 
ATOM   2944 C  CD2   . LEU A 1 357 ? 37.799  32.287  7.142   1.00 59.06  ? 357 LEU A CD2   1 
ATOM   2945 N  N     . LEU A 1 358 ? 33.800  34.942  4.834   1.00 68.44  ? 358 LEU A N     1 
ATOM   2946 C  CA    . LEU A 1 358 ? 33.251  35.836  3.819   1.00 56.79  ? 358 LEU A CA    1 
ATOM   2947 C  C     . LEU A 1 358 ? 33.391  37.295  4.230   1.00 54.35  ? 358 LEU A C     1 
ATOM   2948 O  O     . LEU A 1 358 ? 33.692  38.157  3.396   1.00 52.87  ? 358 LEU A O     1 
ATOM   2949 C  CB    . LEU A 1 358 ? 31.783  35.497  3.557   1.00 64.03  ? 358 LEU A CB    1 
ATOM   2950 C  CG    . LEU A 1 358 ? 31.493  34.319  2.627   1.00 70.23  ? 358 LEU A CG    1 
ATOM   2951 C  CD1   . LEU A 1 358 ? 30.019  34.287  2.257   1.00 67.08  ? 358 LEU A CD1   1 
ATOM   2952 C  CD2   . LEU A 1 358 ? 32.357  34.387  1.383   1.00 66.62  ? 358 LEU A CD2   1 
ATOM   2953 N  N     . ARG A 1 359 ? 33.165  37.595  5.510   1.00 42.69  ? 359 ARG A N     1 
ATOM   2954 C  CA    . ARG A 1 359 ? 33.370  38.956  5.992   1.00 49.74  ? 359 ARG A CA    1 
ATOM   2955 C  C     . ARG A 1 359 ? 34.842  39.333  5.934   1.00 58.53  ? 359 ARG A C     1 
ATOM   2956 O  O     . ARG A 1 359 ? 35.199  40.411  5.445   1.00 60.00  ? 359 ARG A O     1 
ATOM   2957 C  CB    . ARG A 1 359 ? 32.833  39.097  7.415   1.00 53.83  ? 359 ARG A CB    1 
ATOM   2958 C  CG    . ARG A 1 359 ? 32.789  40.530  7.911   1.00 46.53  ? 359 ARG A CG    1 
ATOM   2959 C  CD    . ARG A 1 359 ? 32.217  40.608  9.310   1.00 53.24  ? 359 ARG A CD    1 
ATOM   2960 N  NE    . ARG A 1 359 ? 30.762  40.543  9.290   1.00 55.73  ? 359 ARG A NE    1 
ATOM   2961 C  CZ    . ARG A 1 359 ? 29.966  41.602  9.317   1.00 56.36  ? 359 ARG A CZ    1 
ATOM   2962 N  NH1   . ARG A 1 359 ? 30.453  42.831  9.357   1.00 52.88  ? 359 ARG A NH1   1 
ATOM   2963 N  NH2   . ARG A 1 359 ? 28.648  41.424  9.302   1.00 64.86  ? 359 ARG A NH2   1 
ATOM   2964 N  N     . LYS A 1 360 ? 35.713  38.455  6.439   1.00 63.87  ? 360 LYS A N     1 
ATOM   2965 C  CA    . LYS A 1 360 ? 37.148  38.680  6.312   1.00 61.16  ? 360 LYS A CA    1 
ATOM   2966 C  C     . LYS A 1 360 ? 37.547  38.848  4.852   1.00 66.64  ? 360 LYS A C     1 
ATOM   2967 O  O     . LYS A 1 360 ? 38.342  39.731  4.516   1.00 53.26  ? 360 LYS A O     1 
ATOM   2968 C  CB    . LYS A 1 360 ? 37.918  37.522  6.948   1.00 52.92  ? 360 LYS A CB    1 
ATOM   2969 C  CG    . LYS A 1 360 ? 37.950  37.529  8.472   1.00 50.57  ? 360 LYS A CG    1 
ATOM   2970 C  CD    . LYS A 1 360 ? 38.261  38.906  9.036   1.00 57.21  ? 360 LYS A CD    1 
ATOM   2971 C  CE    . LYS A 1 360 ? 37.709  39.057  10.447  1.00 69.96  ? 360 LYS A CE    1 
ATOM   2972 N  NZ    . LYS A 1 360 ? 37.467  40.481  10.811  1.00 70.66  ? 360 LYS A NZ    1 
ATOM   2973 N  N     . ALA A 1 361 ? 36.987  38.019  3.965   1.00 55.24  ? 361 ALA A N     1 
ATOM   2974 C  CA    . ALA A 1 361 ? 37.314  38.123  2.546   1.00 55.74  ? 361 ALA A CA    1 
ATOM   2975 C  C     . ALA A 1 361 ? 36.894  39.471  1.976   1.00 60.72  ? 361 ALA A C     1 
ATOM   2976 O  O     . ALA A 1 361 ? 37.590  40.038  1.126   1.00 67.49  ? 361 ALA A O     1 
ATOM   2977 C  CB    . ALA A 1 361 ? 36.654  36.985  1.769   1.00 50.55  ? 361 ALA A CB    1 
ATOM   2978 N  N     . TYR A 1 362 ? 35.758  40.004  2.433   1.00 54.63  ? 362 TYR A N     1 
ATOM   2979 C  CA    . TYR A 1 362 ? 35.314  41.304  1.941   1.00 56.33  ? 362 TYR A CA    1 
ATOM   2980 C  C     . TYR A 1 362 ? 36.216  42.423  2.445   1.00 54.72  ? 362 TYR A C     1 
ATOM   2981 O  O     . TYR A 1 362 ? 36.463  43.398  1.726   1.00 49.49  ? 362 TYR A O     1 
ATOM   2982 C  CB    . TYR A 1 362 ? 33.865  41.565  2.353   1.00 54.14  ? 362 TYR A CB    1 
ATOM   2983 C  CG    . TYR A 1 362 ? 33.329  42.876  1.823   1.00 47.94  ? 362 TYR A CG    1 
ATOM   2984 C  CD1   . TYR A 1 362 ? 32.778  42.959  0.551   1.00 49.45  ? 362 TYR A CD1   1 
ATOM   2985 C  CD2   . TYR A 1 362 ? 33.389  44.036  2.588   1.00 39.91  ? 362 TYR A CD2   1 
ATOM   2986 C  CE1   . TYR A 1 362 ? 32.296  44.156  0.057   1.00 51.22  ? 362 TYR A CE1   1 
ATOM   2987 C  CE2   . TYR A 1 362 ? 32.912  45.238  2.100   1.00 45.82  ? 362 TYR A CE2   1 
ATOM   2988 C  CZ    . TYR A 1 362 ? 32.365  45.292  0.835   1.00 48.14  ? 362 TYR A CZ    1 
ATOM   2989 O  OH    . TYR A 1 362 ? 31.885  46.486  0.347   1.00 63.81  ? 362 TYR A OH    1 
ATOM   2990 N  N     . GLU A 1 363 ? 36.706  42.306  3.680   1.00 60.48  ? 363 GLU A N     1 
ATOM   2991 C  CA    . GLU A 1 363 ? 37.560  43.349  4.238   1.00 61.86  ? 363 GLU A CA    1 
ATOM   2992 C  C     . GLU A 1 363 ? 38.878  43.451  3.479   1.00 64.00  ? 363 GLU A C     1 
ATOM   2993 O  O     . GLU A 1 363 ? 39.388  44.555  3.255   1.00 66.00  ? 363 GLU A O     1 
ATOM   2994 C  CB    . GLU A 1 363 ? 37.813  43.083  5.723   1.00 67.07  ? 363 GLU A CB    1 
ATOM   2995 C  CG    . GLU A 1 363 ? 36.555  43.007  6.577   1.00 42.26  ? 363 GLU A CG    1 
ATOM   2996 C  CD    . GLU A 1 363 ? 36.855  42.618  8.014   1.00 66.55  ? 363 GLU A CD    1 
ATOM   2997 O  OE1   . GLU A 1 363 ? 38.018  42.265  8.303   1.00 87.56  ? 363 GLU A OE1   1 
ATOM   2998 O  OE2   . GLU A 1 363 ? 35.930  42.658  8.853   1.00 62.97  ? 363 GLU A OE2   1 
ATOM   2999 N  N     . ARG A 1 364 ? 39.443  42.316  3.071   1.00 68.04  ? 364 ARG A N     1 
ATOM   3000 C  CA    . ARG A 1 364 ? 40.723  42.296  2.374   1.00 66.56  ? 364 ARG A CA    1 
ATOM   3001 C  C     . ARG A 1 364 ? 40.575  42.293  0.855   1.00 70.96  ? 364 ARG A C     1 
ATOM   3002 O  O     . ARG A 1 364 ? 41.565  42.054  0.156   1.00 71.71  ? 364 ARG A O     1 
ATOM   3003 C  CB    . ARG A 1 364 ? 41.553  41.080  2.805   1.00 62.61  ? 364 ARG A CB    1 
ATOM   3004 C  CG    . ARG A 1 364 ? 41.262  40.550  4.202   1.00 77.03  ? 364 ARG A CG    1 
ATOM   3005 C  CD    . ARG A 1 364 ? 41.875  41.408  5.297   1.00 95.96  ? 364 ARG A CD    1 
ATOM   3006 N  NE    . ARG A 1 364 ? 41.476  40.948  6.623   1.00 98.29  ? 364 ARG A NE    1 
ATOM   3007 C  CZ    . ARG A 1 364 ? 42.306  40.426  7.517   1.00 95.25  ? 364 ARG A CZ    1 
ATOM   3008 N  NH1   . ARG A 1 364 ? 43.596  40.280  7.260   1.00 69.21  ? 364 ARG A NH1   1 
ATOM   3009 N  NH2   . ARG A 1 364 ? 41.830  40.042  8.698   1.00 76.69  ? 364 ARG A NH2   1 
ATOM   3010 N  N     . ASN A 1 365 ? 39.372  42.549  0.334   1.00 58.28  ? 365 ASN A N     1 
ATOM   3011 C  CA    . ASN A 1 365 ? 39.114  42.547  -1.110  1.00 53.80  ? 365 ASN A CA    1 
ATOM   3012 C  C     . ASN A 1 365 ? 39.522  41.218  -1.745  1.00 61.00  ? 365 ASN A C     1 
ATOM   3013 O  O     . ASN A 1 365 ? 40.065  41.173  -2.850  1.00 67.60  ? 365 ASN A O     1 
ATOM   3014 C  CB    . ASN A 1 365 ? 39.811  43.722  -1.803  1.00 55.20  ? 365 ASN A CB    1 
ATOM   3015 C  CG    . ASN A 1 365 ? 39.264  43.991  -3.197  1.00 76.44  ? 365 ASN A CG    1 
ATOM   3016 O  OD1   . ASN A 1 365 ? 38.053  43.977  -3.417  1.00 77.02  ? 365 ASN A OD1   1 
ATOM   3017 N  ND2   . ASN A 1 365 ? 40.161  44.236  -4.146  1.00 69.20  ? 365 ASN A ND2   1 
ATOM   3018 N  N     . GLU A 1 366 ? 39.260  40.125  -1.034  1.00 67.39  ? 366 GLU A N     1 
ATOM   3019 C  CA    . GLU A 1 366 ? 39.544  38.780  -1.523  1.00 69.82  ? 366 GLU A CA    1 
ATOM   3020 C  C     . GLU A 1 366 ? 38.284  38.227  -2.177  1.00 66.10  ? 366 GLU A C     1 
ATOM   3021 O  O     . GLU A 1 366 ? 37.275  38.003  -1.500  1.00 71.10  ? 366 GLU A O     1 
ATOM   3022 C  CB    . GLU A 1 366 ? 40.003  37.880  -0.378  1.00 74.00  ? 366 GLU A CB    1 
ATOM   3023 C  CG    . GLU A 1 366 ? 41.216  37.009  -0.681  1.00 85.07  ? 366 GLU A CG    1 
ATOM   3024 C  CD    . GLU A 1 366 ? 42.528  37.740  -0.485  1.00 89.07  ? 366 GLU A CD    1 
ATOM   3025 O  OE1   . GLU A 1 366 ? 42.742  38.300  0.611   1.00 76.73  ? 366 GLU A OE1   1 
ATOM   3026 O  OE2   . GLU A 1 366 ? 43.359  37.727  -1.417  1.00 99.07  ? 366 GLU A OE2   1 
ATOM   3027 N  N     . LEU A 1 367 ? 38.336  38.011  -3.489  1.00 68.06  ? 367 LEU A N     1 
ATOM   3028 C  CA    . LEU A 1 367 ? 37.217  37.386  -4.182  1.00 55.92  ? 367 LEU A CA    1 
ATOM   3029 C  C     . LEU A 1 367 ? 37.003  35.978  -3.645  1.00 73.47  ? 367 LEU A C     1 
ATOM   3030 O  O     . LEU A 1 367 ? 37.915  35.145  -3.677  1.00 71.92  ? 367 LEU A O     1 
ATOM   3031 C  CB    . LEU A 1 367 ? 37.470  37.352  -5.688  1.00 64.35  ? 367 LEU A CB    1 
ATOM   3032 C  CG    . LEU A 1 367 ? 36.382  36.652  -6.509  1.00 62.15  ? 367 LEU A CG    1 
ATOM   3033 C  CD1   . LEU A 1 367 ? 35.117  37.493  -6.549  1.00 68.11  ? 367 LEU A CD1   1 
ATOM   3034 C  CD2   . LEU A 1 367 ? 36.869  36.352  -7.917  1.00 60.59  ? 367 LEU A CD2   1 
ATOM   3035 N  N     . ALA A 1 368 ? 35.802  35.716  -3.146  1.00 71.51  ? 368 ALA A N     1 
ATOM   3036 C  CA    . ALA A 1 368 ? 35.532  34.439  -2.509  1.00 61.44  ? 368 ALA A CA    1 
ATOM   3037 C  C     . ALA A 1 368 ? 35.440  33.330  -3.555  1.00 63.48  ? 368 ALA A C     1 
ATOM   3038 O  O     . ALA A 1 368 ? 34.811  33.513  -4.602  1.00 71.63  ? 368 ALA A O     1 
ATOM   3039 C  CB    . ALA A 1 368 ? 34.236  34.505  -1.706  1.00 55.35  ? 368 ALA A CB    1 
ATOM   3040 N  N     . PRO A 1 369 ? 36.060  32.180  -3.308  1.00 71.16  ? 369 PRO A N     1 
ATOM   3041 C  CA    . PRO A 1 369 ? 35.894  31.042  -4.216  1.00 67.91  ? 369 PRO A CA    1 
ATOM   3042 C  C     . PRO A 1 369 ? 34.554  30.359  -4.003  1.00 68.41  ? 369 PRO A C     1 
ATOM   3043 O  O     . PRO A 1 369 ? 34.002  30.340  -2.901  1.00 70.52  ? 369 PRO A O     1 
ATOM   3044 C  CB    . PRO A 1 369 ? 37.054  30.107  -3.842  1.00 56.18  ? 369 PRO A CB    1 
ATOM   3045 C  CG    . PRO A 1 369 ? 37.853  30.824  -2.776  1.00 59.24  ? 369 PRO A CG    1 
ATOM   3046 C  CD    . PRO A 1 369 ? 36.966  31.870  -2.193  1.00 68.79  ? 369 PRO A CD    1 
ATOM   3047 N  N     . ASN A 1 370 ? 34.033  29.791  -5.087  1.00 72.92  ? 370 ASN A N     1 
ATOM   3048 C  CA    . ASN A 1 370 ? 32.748  29.115  -5.021  1.00 68.51  ? 370 ASN A CA    1 
ATOM   3049 C  C     . ASN A 1 370 ? 32.854  27.843  -4.182  1.00 72.34  ? 370 ASN A C     1 
ATOM   3050 O  O     . ASN A 1 370 ? 33.942  27.370  -3.843  1.00 77.06  ? 370 ASN A O     1 
ATOM   3051 C  CB    . ASN A 1 370 ? 32.249  28.767  -6.421  1.00 63.56  ? 370 ASN A CB    1 
ATOM   3052 C  CG    . ASN A 1 370 ? 32.091  29.983  -7.303  1.00 65.76  ? 370 ASN A CG    1 
ATOM   3053 O  OD1   . ASN A 1 370 ? 31.730  31.061  -6.833  1.00 69.18  ? 370 ASN A OD1   1 
ATOM   3054 N  ND2   . ASN A 1 370 ? 32.363  29.818  -8.592  1.00 64.96  ? 370 ASN A ND2   1 
ATOM   3055 N  N     . LYS A 1 371 ? 31.696  27.292  -3.843  1.00 69.67  ? 371 LYS A N     1 
ATOM   3056 C  CA    . LYS A 1 371 ? 31.637  25.957  -3.282  1.00 59.51  ? 371 LYS A CA    1 
ATOM   3057 C  C     . LYS A 1 371 ? 31.858  24.934  -4.393  1.00 61.85  ? 371 LYS A C     1 
ATOM   3058 O  O     . LYS A 1 371 ? 31.611  25.220  -5.567  1.00 67.63  ? 371 LYS A O     1 
ATOM   3059 C  CB    . LYS A 1 371 ? 30.292  25.736  -2.596  1.00 59.34  ? 371 LYS A CB    1 
ATOM   3060 C  CG    . LYS A 1 371 ? 30.062  26.639  -1.394  1.00 59.72  ? 371 LYS A CG    1 
ATOM   3061 C  CD    . LYS A 1 371 ? 29.460  25.873  -0.232  1.00 55.72  ? 371 LYS A CD    1 
ATOM   3062 C  CE    . LYS A 1 371 ? 29.418  26.726  1.024   1.00 69.59  ? 371 LYS A CE    1 
ATOM   3063 N  NZ    . LYS A 1 371 ? 29.612  25.922  2.263   1.00 85.04  ? 371 LYS A NZ    1 
ATOM   3064 N  N     . PRO A 1 372 ? 32.340  23.739  -4.058  1.00 63.50  ? 372 PRO A N     1 
ATOM   3065 C  CA    . PRO A 1 372 ? 32.600  22.742  -5.102  1.00 70.79  ? 372 PRO A CA    1 
ATOM   3066 C  C     . PRO A 1 372 ? 31.303  22.182  -5.668  1.00 81.39  ? 372 PRO A C     1 
ATOM   3067 O  O     . PRO A 1 372 ? 30.275  22.134  -4.990  1.00 85.69  ? 372 PRO A O     1 
ATOM   3068 C  CB    . PRO A 1 372 ? 33.399  21.662  -4.362  1.00 65.64  ? 372 PRO A CB    1 
ATOM   3069 C  CG    . PRO A 1 372 ? 32.891  21.747  -2.958  1.00 69.61  ? 372 PRO A CG    1 
ATOM   3070 C  CD    . PRO A 1 372 ? 32.625  23.211  -2.710  1.00 67.69  ? 372 PRO A CD    1 
ATOM   3071 N  N     . ASP A 1 373 ? 31.346  21.759  -6.934  1.00 81.78  ? 373 ASP A N     1 
ATOM   3072 C  CA    . ASP A 1 373 ? 30.187  21.078  -7.496  1.00 91.62  ? 373 ASP A CA    1 
ATOM   3073 C  C     . ASP A 1 373 ? 30.412  19.569  -7.348  1.00 93.68  ? 373 ASP A C     1 
ATOM   3074 O  O     . ASP A 1 373 ? 31.179  19.135  -6.485  1.00 95.44  ? 373 ASP A O     1 
ATOM   3075 C  CB    . ASP A 1 373 ? 29.912  21.569  -8.929  1.00 96.19  ? 373 ASP A CB    1 
ATOM   3076 C  CG    . ASP A 1 373 ? 30.925  21.055  -9.960  1.00 105.22 ? 373 ASP A CG    1 
ATOM   3077 O  OD1   . ASP A 1 373 ? 30.890  19.860  -10.297 1.00 116.29 ? 373 ASP A OD1   1 
ATOM   3078 O  OD2   . ASP A 1 373 ? 31.749  21.854  -10.440 1.00 102.99 ? 373 ASP A OD2   1 
ATOM   3079 N  N     . GLU A 1 374 ? 29.753  18.750  -8.171  1.00 101.48 ? 374 GLU A N     1 
ATOM   3080 C  CA    . GLU A 1 374 ? 29.708  17.314  -7.898  1.00 104.07 ? 374 GLU A CA    1 
ATOM   3081 C  C     . GLU A 1 374 ? 31.076  16.663  -8.071  1.00 103.92 ? 374 GLU A C     1 
ATOM   3082 O  O     . GLU A 1 374 ? 31.546  15.942  -7.182  1.00 104.85 ? 374 GLU A O     1 
ATOM   3083 C  CB    . GLU A 1 374 ? 28.677  16.643  -8.802  1.00 121.22 ? 374 GLU A CB    1 
ATOM   3084 C  CG    . GLU A 1 374 ? 27.377  16.286  -8.098  1.00 130.77 ? 374 GLU A CG    1 
ATOM   3085 C  CD    . GLU A 1 374 ? 26.455  15.462  -8.972  1.00 138.21 ? 374 GLU A CD    1 
ATOM   3086 O  OE1   . GLU A 1 374 ? 26.180  15.887  -10.113 1.00 127.89 ? 374 GLU A OE1   1 
ATOM   3087 O  OE2   . GLU A 1 374 ? 26.008  14.388  -8.518  1.00 133.31 ? 374 GLU A OE2   1 
ATOM   3088 N  N     . LYS A 1 375 ? 31.723  16.899  -9.214  1.00 104.93 ? 375 LYS A N     1 
ATOM   3089 C  CA    . LYS A 1 375 ? 33.019  16.281  -9.482  1.00 117.88 ? 375 LYS A CA    1 
ATOM   3090 C  C     . LYS A 1 375 ? 34.056  16.675  -8.433  1.00 117.24 ? 375 LYS A C     1 
ATOM   3091 O  O     . LYS A 1 375 ? 34.852  15.836  -8.000  1.00 119.52 ? 375 LYS A O     1 
ATOM   3092 C  CB    . LYS A 1 375 ? 33.504  16.669  -10.879 1.00 124.52 ? 375 LYS A CB    1 
ATOM   3093 C  CG    . LYS A 1 375 ? 33.423  15.564  -11.915 1.00 131.75 ? 375 LYS A CG    1 
ATOM   3094 C  CD    . LYS A 1 375 ? 34.453  15.771  -13.017 1.00 126.73 ? 375 LYS A CD    1 
ATOM   3095 C  CE    . LYS A 1 375 ? 35.856  15.896  -12.444 1.00 132.67 ? 375 LYS A CE    1 
ATOM   3096 N  NZ    . LYS A 1 375 ? 36.282  14.654  -11.745 1.00 125.96 ? 375 LYS A NZ    1 
ATOM   3097 N  N     . GLU A 1 376 ? 34.067  17.945  -8.014  1.00 107.63 ? 376 GLU A N     1 
ATOM   3098 C  CA    . GLU A 1 376 ? 35.063  18.392  -7.041  1.00 93.43  ? 376 GLU A CA    1 
ATOM   3099 C  C     . GLU A 1 376 ? 34.760  17.810  -5.669  1.00 91.12  ? 376 GLU A C     1 
ATOM   3100 O  O     . GLU A 1 376 ? 35.665  17.339  -4.976  1.00 95.49  ? 376 GLU A O     1 
ATOM   3101 C  CB    . GLU A 1 376 ? 35.127  19.926  -6.969  1.00 91.82  ? 376 GLU A CB    1 
ATOM   3102 C  CG    . GLU A 1 376 ? 35.424  20.700  -8.272  1.00 114.05 ? 376 GLU A CG    1 
ATOM   3103 C  CD    . GLU A 1 376 ? 34.647  20.162  -9.433  1.00 127.87 ? 376 GLU A CD    1 
ATOM   3104 O  OE1   . GLU A 1 376 ? 35.270  19.891  -10.486 1.00 128.04 ? 376 GLU A OE1   1 
ATOM   3105 O  OE2   . GLU A 1 376 ? 33.456  19.821  -9.229  1.00 127.16 ? 376 GLU A OE2   1 
ATOM   3106 N  N     . LEU A 1 377 ? 33.483  17.817  -5.261  1.00 91.34  ? 377 LEU A N     1 
ATOM   3107 C  CA    . LEU A 1 377 ? 33.102  17.149  -4.014  1.00 84.29  ? 377 LEU A CA    1 
ATOM   3108 C  C     . LEU A 1 377 ? 33.483  15.673  -4.034  1.00 94.30  ? 377 LEU A C     1 
ATOM   3109 O  O     . LEU A 1 377 ? 33.792  15.094  -2.985  1.00 92.27  ? 377 LEU A O     1 
ATOM   3110 C  CB    . LEU A 1 377 ? 31.599  17.300  -3.771  1.00 82.35  ? 377 LEU A CB    1 
ATOM   3111 C  CG    . LEU A 1 377 ? 31.147  18.329  -2.734  1.00 88.65  ? 377 LEU A CG    1 
ATOM   3112 C  CD1   . LEU A 1 377 ? 29.685  18.682  -2.940  1.00 82.74  ? 377 LEU A CD1   1 
ATOM   3113 C  CD2   . LEU A 1 377 ? 31.368  17.798  -1.332  1.00 93.08  ? 377 LEU A CD2   1 
ATOM   3114 N  N     . ALA A 1 378 ? 33.465  15.052  -5.216  1.00 98.56  ? 378 ALA A N     1 
ATOM   3115 C  CA    . ALA A 1 378 ? 33.887  13.661  -5.336  1.00 99.12  ? 378 ALA A CA    1 
ATOM   3116 C  C     . ALA A 1 378 ? 35.381  13.523  -5.086  1.00 104.12 ? 378 ALA A C     1 
ATOM   3117 O  O     . ALA A 1 378 ? 35.814  12.638  -4.339  1.00 106.84 ? 378 ALA A O     1 
ATOM   3118 C  CB    . ALA A 1 378 ? 33.519  13.113  -6.715  1.00 92.75  ? 378 ALA A CB    1 
ATOM   3119 N  N     . ARG A 1 379 ? 36.185  14.388  -5.709  1.00 104.79 ? 379 ARG A N     1 
ATOM   3120 C  CA    . ARG A 1 379 ? 37.618  14.408  -5.452  1.00 97.91  ? 379 ARG A CA    1 
ATOM   3121 C  C     . ARG A 1 379 ? 37.840  14.575  -3.954  1.00 102.61 ? 379 ARG A C     1 
ATOM   3122 O  O     . ARG A 1 379 ? 38.183  13.604  -3.273  1.00 106.56 ? 379 ARG A O     1 
ATOM   3123 C  CB    . ARG A 1 379 ? 38.302  15.515  -6.267  1.00 88.80  ? 379 ARG A CB    1 
ATOM   3124 C  CG    . ARG A 1 379 ? 39.663  15.980  -5.752  1.00 99.74  ? 379 ARG A CG    1 
ATOM   3125 C  CD    . ARG A 1 379 ? 40.133  17.242  -6.472  1.00 99.58  ? 379 ARG A CD    1 
ATOM   3126 N  NE    . ARG A 1 379 ? 39.415  18.441  -6.052  1.00 123.65 ? 379 ARG A NE    1 
ATOM   3127 C  CZ    . ARG A 1 379 ? 38.685  19.205  -6.854  1.00 107.74 ? 379 ARG A CZ    1 
ATOM   3128 N  NH1   . ARG A 1 379 ? 38.511  18.904  -8.131  1.00 98.29  ? 379 ARG A NH1   1 
ATOM   3129 N  NH2   . ARG A 1 379 ? 38.120  20.303  -6.362  1.00 75.31  ? 379 ARG A NH2   1 
ATOM   3130 N  N     . ARG A 1 380 ? 37.532  15.759  -3.421  1.00 93.79  ? 380 ARG A N     1 
ATOM   3131 C  CA    . ARG A 1 380 ? 37.792  16.145  -2.033  1.00 85.77  ? 380 ARG A CA    1 
ATOM   3132 C  C     . ARG A 1 380 ? 37.365  15.128  -0.973  1.00 81.60  ? 380 ARG A C     1 
ATOM   3133 O  O     . ARG A 1 380 ? 37.420  15.424  0.225   1.00 76.08  ? 380 ARG A O     1 
ATOM   3134 C  CB    . ARG A 1 380 ? 37.101  17.481  -1.748  1.00 78.24  ? 380 ARG A CB    1 
ATOM   3135 C  CG    . ARG A 1 380 ? 37.453  18.574  -2.742  1.00 71.92  ? 380 ARG A CG    1 
ATOM   3136 C  CD    . ARG A 1 380 ? 36.851  19.909  -2.347  1.00 71.08  ? 380 ARG A CD    1 
ATOM   3137 N  NE    . ARG A 1 380 ? 37.120  20.935  -3.348  1.00 72.34  ? 380 ARG A NE    1 
ATOM   3138 C  CZ    . ARG A 1 380 ? 36.793  22.213  -3.219  1.00 69.59  ? 380 ARG A CZ    1 
ATOM   3139 N  NH1   . ARG A 1 380 ? 36.163  22.661  -2.145  1.00 59.80  ? 380 ARG A NH1   1 
ATOM   3140 N  NH2   . ARG A 1 380 ? 37.101  23.063  -4.194  1.00 75.99  ? 380 ARG A NH2   1 
ATOM   3141 N  N     . ARG A 1 381 ? 36.943  13.935  -1.388  1.00 93.08  ? 381 ARG A N     1 
ATOM   3142 C  CA    . ARG A 1 381 ? 36.585  12.873  -0.460  1.00 104.96 ? 381 ARG A CA    1 
ATOM   3143 C  C     . ARG A 1 381 ? 37.794  12.119  0.081   1.00 108.05 ? 381 ARG A C     1 
ATOM   3144 O  O     . ARG A 1 381 ? 37.602  11.126  0.791   1.00 113.95 ? 381 ARG A O     1 
ATOM   3145 C  CB    . ARG A 1 381 ? 35.628  11.881  -1.132  1.00 106.07 ? 381 ARG A CB    1 
ATOM   3146 C  CG    . ARG A 1 381 ? 34.242  12.428  -1.419  1.00 106.58 ? 381 ARG A CG    1 
ATOM   3147 C  CD    . ARG A 1 381 ? 33.584  13.003  -0.174  1.00 105.77 ? 381 ARG A CD    1 
ATOM   3148 N  NE    . ARG A 1 381 ? 32.331  13.676  -0.498  1.00 115.61 ? 381 ARG A NE    1 
ATOM   3149 C  CZ    . ARG A 1 381 ? 31.296  13.777  0.324   1.00 107.93 ? 381 ARG A CZ    1 
ATOM   3150 N  NH1   . ARG A 1 381 ? 31.330  13.270  1.546   1.00 116.33 ? 381 ARG A NH1   1 
ATOM   3151 N  NH2   . ARG A 1 381 ? 30.198  14.402  -0.090  1.00 89.28  ? 381 ARG A NH2   1 
ATOM   3152 N  N     . GLN A 1 382 ? 39.020  12.543  -0.230  1.00 110.02 ? 382 GLN A N     1 
ATOM   3153 C  CA    . GLN A 1 382 ? 40.182  11.819  0.265   1.00 99.15  ? 382 GLN A CA    1 
ATOM   3154 C  C     . GLN A 1 382 ? 40.298  11.985  1.777   1.00 85.80  ? 382 GLN A C     1 
ATOM   3155 O  O     . GLN A 1 382 ? 39.470  12.621  2.432   1.00 93.16  ? 382 GLN A O     1 
ATOM   3156 C  CB    . GLN A 1 382 ? 41.479  12.297  -0.385  1.00 101.37 ? 382 GLN A CB    1 
ATOM   3157 C  CG    . GLN A 1 382 ? 41.596  13.786  -0.618  1.00 117.71 ? 382 GLN A CG    1 
ATOM   3158 C  CD    . GLN A 1 382 ? 41.565  14.177  -2.090  1.00 113.20 ? 382 GLN A CD    1 
ATOM   3159 O  OE1   . GLN A 1 382 ? 40.537  14.114  -2.751  1.00 111.52 ? 382 GLN A OE1   1 
ATOM   3160 N  NE2   . GLN A 1 382 ? 42.713  14.585  -2.605  1.00 115.41 ? 382 GLN A NE2   1 
ATOM   3161 N  N     . LYS A 1 383 ? 41.365  11.416  2.331   1.00 78.82  ? 383 LYS A N     1 
ATOM   3162 C  CA    . LYS A 1 383 ? 41.697  11.605  3.732   1.00 75.12  ? 383 LYS A CA    1 
ATOM   3163 C  C     . LYS A 1 383 ? 43.196  11.839  3.848   1.00 80.66  ? 383 LYS A C     1 
ATOM   3164 O  O     . LYS A 1 383 ? 43.970  11.493  2.952   1.00 87.47  ? 383 LYS A O     1 
ATOM   3165 C  CB    . LYS A 1 383 ? 41.269  10.405  4.590   1.00 81.17  ? 383 LYS A CB    1 
ATOM   3166 C  CG    . LYS A 1 383 ? 41.045  10.735  6.067   1.00 83.06  ? 383 LYS A CG    1 
ATOM   3167 C  CD    . LYS A 1 383 ? 40.449  9.556   6.832   1.00 96.19  ? 383 LYS A CD    1 
ATOM   3168 C  CE    . LYS A 1 383 ? 39.574  8.681   5.940   1.00 106.92 ? 383 LYS A CE    1 
ATOM   3169 N  NZ    . LYS A 1 383 ? 39.359  7.324   6.521   1.00 94.50  ? 383 LYS A NZ    1 
ATOM   3170 N  N     . TYR A 1 384 ? 43.599  12.444  4.961   1.00 69.84  ? 384 TYR A N     1 
ATOM   3171 C  CA    . TYR A 1 384 ? 45.002  12.732  5.209   1.00 56.69  ? 384 TYR A CA    1 
ATOM   3172 C  C     . TYR A 1 384 ? 45.322  12.424  6.662   1.00 61.58  ? 384 TYR A C     1 
ATOM   3173 O  O     . TYR A 1 384 ? 44.430  12.311  7.505   1.00 64.08  ? 384 TYR A O     1 
ATOM   3174 C  CB    . TYR A 1 384 ? 45.347  14.188  4.872   1.00 60.77  ? 384 TYR A CB    1 
ATOM   3175 C  CG    . TYR A 1 384 ? 44.570  15.213  5.666   1.00 62.61  ? 384 TYR A CG    1 
ATOM   3176 C  CD1   . TYR A 1 384 ? 43.342  15.683  5.218   1.00 53.90  ? 384 TYR A CD1   1 
ATOM   3177 C  CD2   . TYR A 1 384 ? 45.072  15.723  6.856   1.00 58.71  ? 384 TYR A CD2   1 
ATOM   3178 C  CE1   . TYR A 1 384 ? 42.631  16.627  5.939   1.00 59.35  ? 384 TYR A CE1   1 
ATOM   3179 C  CE2   . TYR A 1 384 ? 44.371  16.665  7.583   1.00 61.88  ? 384 TYR A CE2   1 
ATOM   3180 C  CZ    . TYR A 1 384 ? 43.153  17.114  7.121   1.00 62.25  ? 384 TYR A CZ    1 
ATOM   3181 O  OH    . TYR A 1 384 ? 42.457  18.054  7.848   1.00 52.79  ? 384 TYR A OH    1 
ATOM   3182 N  N     . GLU A 1 385 ? 46.614  12.282  6.946   1.00 55.03  ? 385 GLU A N     1 
ATOM   3183 C  CA    . GLU A 1 385 ? 47.042  11.934  8.293   1.00 55.74  ? 385 GLU A CA    1 
ATOM   3184 C  C     . GLU A 1 385 ? 46.847  13.114  9.237   1.00 53.99  ? 385 GLU A C     1 
ATOM   3185 O  O     . GLU A 1 385 ? 47.030  14.274  8.857   1.00 58.52  ? 385 GLU A O     1 
ATOM   3186 C  CB    . GLU A 1 385 ? 48.504  11.491  8.292   1.00 61.69  ? 385 GLU A CB    1 
ATOM   3187 C  CG    . GLU A 1 385 ? 48.922  10.765  9.560   1.00 63.97  ? 385 GLU A CG    1 
ATOM   3188 C  CD    . GLU A 1 385 ? 50.308  10.160  9.465   1.00 69.39  ? 385 GLU A CD    1 
ATOM   3189 O  OE1   . GLU A 1 385 ? 50.877  10.146  8.353   1.00 76.53  ? 385 GLU A OE1   1 
ATOM   3190 O  OE2   . GLU A 1 385 ? 50.826  9.699   10.505  1.00 62.32  ? 385 GLU A OE2   1 
ATOM   3191 N  N     . GLY A 1 386 ? 46.468  12.809  10.475  1.00 54.76  ? 386 GLY A N     1 
ATOM   3192 C  CA    . GLY A 1 386 ? 46.224  13.841  11.462  1.00 57.07  ? 386 GLY A CA    1 
ATOM   3193 C  C     . GLY A 1 386 ? 47.185  13.805  12.632  1.00 59.82  ? 386 GLY A C     1 
ATOM   3194 O  O     . GLY A 1 386 ? 48.385  13.571  12.458  1.00 61.93  ? 386 GLY A O     1 
ATOM   3195 N  N     . GLY A 1 387 ? 46.663  14.039  13.834  1.00 67.48  ? 387 GLY A N     1 
ATOM   3196 C  CA    . GLY A 1 387 ? 47.505  14.068  15.009  1.00 64.17  ? 387 GLY A CA    1 
ATOM   3197 C  C     . GLY A 1 387 ? 48.031  12.696  15.385  1.00 66.85  ? 387 GLY A C     1 
ATOM   3198 O  O     . GLY A 1 387 ? 47.471  11.657  15.036  1.00 71.59  ? 387 GLY A O     1 
ATOM   3199 N  N     . TYR A 1 388 ? 49.141  12.706  16.116  1.00 69.40  ? 388 TYR A N     1 
ATOM   3200 C  CA    . TYR A 1 388 ? 49.786  11.484  16.576  1.00 49.13  ? 388 TYR A CA    1 
ATOM   3201 C  C     . TYR A 1 388 ? 49.287  11.142  17.973  1.00 58.28  ? 388 TYR A C     1 
ATOM   3202 O  O     . TYR A 1 388 ? 49.197  12.018  18.836  1.00 59.74  ? 388 TYR A O     1 
ATOM   3203 C  CB    . TYR A 1 388 ? 51.307  11.653  16.573  1.00 62.65  ? 388 TYR A CB    1 
ATOM   3204 C  CG    . TYR A 1 388 ? 52.057  10.738  17.519  1.00 61.37  ? 388 TYR A CG    1 
ATOM   3205 C  CD1   . TYR A 1 388 ? 52.352  9.429   17.162  1.00 50.73  ? 388 TYR A CD1   1 
ATOM   3206 C  CD2   . TYR A 1 388 ? 52.489  11.191  18.762  1.00 65.06  ? 388 TYR A CD2   1 
ATOM   3207 C  CE1   . TYR A 1 388 ? 53.044  8.591   18.019  1.00 61.85  ? 388 TYR A CE1   1 
ATOM   3208 C  CE2   . TYR A 1 388 ? 53.181  10.360  19.627  1.00 60.58  ? 388 TYR A CE2   1 
ATOM   3209 C  CZ    . TYR A 1 388 ? 53.456  9.062   19.249  1.00 67.26  ? 388 TYR A CZ    1 
ATOM   3210 O  OH    . TYR A 1 388 ? 54.148  8.228   20.096  1.00 76.67  ? 388 TYR A OH    1 
ATOM   3211 N  N     . VAL A 1 389 ? 48.949  9.875   18.187  1.00 58.23  ? 389 VAL A N     1 
ATOM   3212 C  CA    . VAL A 1 389 ? 48.527  9.385   19.495  1.00 63.92  ? 389 VAL A CA    1 
ATOM   3213 C  C     . VAL A 1 389 ? 49.409  8.199   19.852  1.00 64.38  ? 389 VAL A C     1 
ATOM   3214 O  O     . VAL A 1 389 ? 49.484  7.227   19.091  1.00 77.22  ? 389 VAL A O     1 
ATOM   3215 C  CB    . VAL A 1 389 ? 47.042  8.983   19.520  1.00 65.64  ? 389 VAL A CB    1 
ATOM   3216 C  CG1   . VAL A 1 389 ? 46.536  8.928   20.955  1.00 59.33  ? 389 VAL A CG1   1 
ATOM   3217 C  CG2   . VAL A 1 389 ? 46.206  9.951   18.695  1.00 55.49  ? 389 VAL A CG2   1 
ATOM   3218 N  N     . LYS A 1 390 ? 50.075  8.277   20.999  1.00 57.25  ? 390 LYS A N     1 
ATOM   3219 C  CA    . LYS A 1 390 ? 50.915  7.188   21.464  1.00 67.94  ? 390 LYS A CA    1 
ATOM   3220 C  C     . LYS A 1 390 ? 50.098  6.216   22.302  1.00 69.45  ? 390 LYS A C     1 
ATOM   3221 O  O     . LYS A 1 390 ? 49.081  6.581   22.899  1.00 77.52  ? 390 LYS A O     1 
ATOM   3222 C  CB    . LYS A 1 390 ? 52.096  7.713   22.282  1.00 75.80  ? 390 LYS A CB    1 
ATOM   3223 C  CG    . LYS A 1 390 ? 51.777  8.030   23.731  1.00 75.79  ? 390 LYS A CG    1 
ATOM   3224 C  CD    . LYS A 1 390 ? 53.046  8.076   24.570  1.00 74.91  ? 390 LYS A CD    1 
ATOM   3225 C  CE    . LYS A 1 390 ? 53.775  6.741   24.549  1.00 76.29  ? 390 LYS A CE    1 
ATOM   3226 N  NZ    . LYS A 1 390 ? 54.739  6.612   25.679  1.00 77.46  ? 390 LYS A NZ    1 
ATOM   3227 N  N     . GLU A 1 391 ? 50.545  4.973   22.331  1.00 72.95  ? 391 GLU A N     1 
ATOM   3228 C  CA    . GLU A 1 391 ? 49.912  3.982   23.187  1.00 72.25  ? 391 GLU A CA    1 
ATOM   3229 C  C     . GLU A 1 391 ? 50.254  4.290   24.637  1.00 75.01  ? 391 GLU A C     1 
ATOM   3230 O  O     . GLU A 1 391 ? 51.443  4.374   24.978  1.00 75.73  ? 391 GLU A O     1 
ATOM   3231 C  CB    . GLU A 1 391 ? 50.364  2.574   22.813  1.00 63.76  ? 391 GLU A CB    1 
ATOM   3232 C  CG    . GLU A 1 391 ? 49.292  1.765   22.105  1.00 68.03  ? 391 GLU A CG    1 
ATOM   3233 C  CD    . GLU A 1 391 ? 48.027  1.621   22.931  1.00 80.01  ? 391 GLU A CD    1 
ATOM   3234 O  OE1   . GLU A 1 391 ? 48.133  1.465   24.167  1.00 72.68  ? 391 GLU A OE1   1 
ATOM   3235 O  OE2   . GLU A 1 391 ? 46.925  1.681   22.346  1.00 82.19  ? 391 GLU A OE2   1 
ATOM   3236 N  N     . PRO A 1 392 ? 49.268  4.483   25.510  1.00 79.29  ? 392 PRO A N     1 
ATOM   3237 C  CA    . PRO A 1 392 ? 49.577  4.822   26.903  1.00 88.12  ? 392 PRO A CA    1 
ATOM   3238 C  C     . PRO A 1 392 ? 50.360  3.709   27.577  1.00 82.40  ? 392 PRO A C     1 
ATOM   3239 O  O     . PRO A 1 392 ? 50.101  2.524   27.363  1.00 94.70  ? 392 PRO A O     1 
ATOM   3240 C  CB    . PRO A 1 392 ? 48.195  4.997   27.544  1.00 79.91  ? 392 PRO A CB    1 
ATOM   3241 C  CG    . PRO A 1 392 ? 47.258  5.211   26.408  1.00 80.47  ? 392 PRO A CG    1 
ATOM   3242 C  CD    . PRO A 1 392 ? 47.820  4.447   25.253  1.00 75.28  ? 392 PRO A CD    1 
ATOM   3243 N  N     . GLU A 1 393 ? 51.335  4.102   28.393  1.00 68.01  ? 393 GLU A N     1 
ATOM   3244 C  CA    . GLU A 1 393 ? 51.992  3.156   29.290  1.00 84.39  ? 393 GLU A CA    1 
ATOM   3245 C  C     . GLU A 1 393 ? 50.949  2.747   30.327  1.00 83.74  ? 393 GLU A C     1 
ATOM   3246 O  O     . GLU A 1 393 ? 50.854  3.310   31.420  1.00 85.92  ? 393 GLU A O     1 
ATOM   3247 C  CB    . GLU A 1 393 ? 53.235  3.773   29.917  1.00 91.61  ? 393 GLU A CB    1 
ATOM   3248 C  CG    . GLU A 1 393 ? 54.216  4.366   28.910  1.00 83.33  ? 393 GLU A CG    1 
ATOM   3249 C  CD    . GLU A 1 393 ? 55.002  3.307   28.152  1.00 93.10  ? 393 GLU A CD    1 
ATOM   3250 O  OE1   . GLU A 1 393 ? 54.897  2.111   28.502  1.00 98.86  ? 393 GLU A OE1   1 
ATOM   3251 O  OE2   . GLU A 1 393 ? 55.725  3.672   27.200  1.00 95.96  ? 393 GLU A OE2   1 
ATOM   3252 N  N     . ARG A 1 394 ? 50.148  1.748   29.953  1.00 91.82  ? 394 ARG A N     1 
ATOM   3253 C  CA    . ARG A 1 394 ? 48.912  1.432   30.662  1.00 82.16  ? 394 ARG A CA    1 
ATOM   3254 C  C     . ARG A 1 394 ? 49.174  1.080   32.120  1.00 90.36  ? 394 ARG A C     1 
ATOM   3255 O  O     . ARG A 1 394 ? 50.067  0.288   32.430  1.00 96.70  ? 394 ARG A O     1 
ATOM   3256 C  CB    . ARG A 1 394 ? 48.200  0.272   29.964  1.00 82.36  ? 394 ARG A CB    1 
ATOM   3257 C  CG    . ARG A 1 394 ? 46.855  -0.091  30.566  1.00 81.87  ? 394 ARG A CG    1 
ATOM   3258 C  CD    . ARG A 1 394 ? 46.115  -1.074  29.674  1.00 98.24  ? 394 ARG A CD    1 
ATOM   3259 N  NE    . ARG A 1 394 ? 44.703  -1.192  30.021  1.00 98.48  ? 394 ARG A NE    1 
ATOM   3260 C  CZ    . ARG A 1 394 ? 43.793  -1.775  29.252  1.00 96.72  ? 394 ARG A CZ    1 
ATOM   3261 N  NH1   . ARG A 1 394 ? 44.107  -2.278  28.069  1.00 107.85 ? 394 ARG A NH1   1 
ATOM   3262 N  NH2   . ARG A 1 394 ? 42.534  -1.846  29.675  1.00 87.55  ? 394 ARG A NH2   1 
ATOM   3263 N  N     . GLY A 1 395 ? 48.384  1.666   33.016  1.00 79.88  ? 395 GLY A N     1 
ATOM   3264 C  CA    . GLY A 1 395 ? 48.547  1.419   34.436  1.00 91.30  ? 395 GLY A CA    1 
ATOM   3265 C  C     . GLY A 1 395 ? 48.381  2.659   35.293  1.00 96.55  ? 395 GLY A C     1 
ATOM   3266 O  O     . GLY A 1 395 ? 47.746  3.628   34.882  1.00 94.51  ? 395 GLY A O     1 
ATOM   3267 N  N     . LEU A 1 396 ? 48.951  2.628   36.498  1.00 102.06 ? 396 LEU A N     1 
ATOM   3268 C  CA    . LEU A 1 396 ? 48.867  3.741   37.432  1.00 101.04 ? 396 LEU A CA    1 
ATOM   3269 C  C     . LEU A 1 396 ? 50.210  4.456   37.487  1.00 106.33 ? 396 LEU A C     1 
ATOM   3270 O  O     . LEU A 1 396 ? 51.260  3.810   37.596  1.00 100.90 ? 396 LEU A O     1 
ATOM   3271 C  CB    . LEU A 1 396 ? 48.458  3.248   38.825  1.00 109.66 ? 396 LEU A CB    1 
ATOM   3272 C  CG    . LEU A 1 396 ? 48.638  4.187   40.015  1.00 116.59 ? 396 LEU A CG    1 
ATOM   3273 C  CD1   . LEU A 1 396 ? 47.428  4.099   40.925  1.00 102.74 ? 396 LEU A CD1   1 
ATOM   3274 C  CD2   . LEU A 1 396 ? 49.910  3.840   40.775  1.00 104.10 ? 396 LEU A CD2   1 
ATOM   3275 N  N     . TRP A 1 397 ? 50.174  5.783   37.403  1.00 99.62  ? 397 TRP A N     1 
ATOM   3276 C  CA    . TRP A 1 397 ? 51.376  6.602   37.448  1.00 96.20  ? 397 TRP A CA    1 
ATOM   3277 C  C     . TRP A 1 397 ? 51.230  7.671   38.519  1.00 94.62  ? 397 TRP A C     1 
ATOM   3278 O  O     . TRP A 1 397 ? 50.118  8.080   38.864  1.00 94.06  ? 397 TRP A O     1 
ATOM   3279 C  CB    . TRP A 1 397 ? 51.668  7.244   36.085  1.00 85.34  ? 397 TRP A CB    1 
ATOM   3280 C  CG    . TRP A 1 397 ? 52.017  6.235   35.042  1.00 89.14  ? 397 TRP A CG    1 
ATOM   3281 C  CD1   . TRP A 1 397 ? 51.150  5.486   34.301  1.00 89.36  ? 397 TRP A CD1   1 
ATOM   3282 C  CD2   . TRP A 1 397 ? 53.333  5.839   34.642  1.00 79.92  ? 397 TRP A CD2   1 
ATOM   3283 N  NE1   . TRP A 1 397 ? 51.846  4.656   33.455  1.00 90.35  ? 397 TRP A NE1   1 
ATOM   3284 C  CE2   . TRP A 1 397 ? 53.188  4.855   33.647  1.00 87.62  ? 397 TRP A CE2   1 
ATOM   3285 C  CE3   . TRP A 1 397 ? 54.620  6.227   35.026  1.00 91.09  ? 397 TRP A CE3   1 
ATOM   3286 C  CZ2   . TRP A 1 397 ? 54.282  4.251   33.033  1.00 88.60  ? 397 TRP A CZ2   1 
ATOM   3287 C  CZ3   . TRP A 1 397 ? 55.704  5.628   34.413  1.00 87.95  ? 397 TRP A CZ3   1 
ATOM   3288 C  CH2   . TRP A 1 397 ? 55.528  4.652   33.426  1.00 92.00  ? 397 TRP A CH2   1 
ATOM   3289 N  N     . GLU A 1 398 ? 52.367  8.117   39.046  1.00 92.24  ? 398 GLU A N     1 
ATOM   3290 C  CA    . GLU A 1 398 ? 52.393  9.066   40.148  1.00 92.73  ? 398 GLU A CA    1 
ATOM   3291 C  C     . GLU A 1 398 ? 53.298  10.241  39.808  1.00 100.83 ? 398 GLU A C     1 
ATOM   3292 O  O     . GLU A 1 398 ? 54.304  10.091  39.108  1.00 107.07 ? 398 GLU A O     1 
ATOM   3293 C  CB    . GLU A 1 398 ? 52.864  8.395   41.446  1.00 99.35  ? 398 GLU A CB    1 
ATOM   3294 C  CG    . GLU A 1 398 ? 53.991  7.394   41.251  1.00 110.67 ? 398 GLU A CG    1 
ATOM   3295 C  CD    . GLU A 1 398 ? 53.887  6.212   42.195  1.00 118.78 ? 398 GLU A CD    1 
ATOM   3296 O  OE1   . GLU A 1 398 ? 52.753  5.761   42.461  1.00 127.29 ? 398 GLU A OE1   1 
ATOM   3297 O  OE2   . GLU A 1 398 ? 54.938  5.734   42.670  1.00 110.20 ? 398 GLU A OE2   1 
ATOM   3298 N  N     . ASN A 1 399 ? 52.921  11.417  40.317  1.00 97.33  ? 399 ASN A N     1 
ATOM   3299 C  CA    . ASN A 1 399 ? 53.641  12.663  40.075  1.00 86.48  ? 399 ASN A CA    1 
ATOM   3300 C  C     . ASN A 1 399 ? 53.794  12.925  38.582  1.00 94.88  ? 399 ASN A C     1 
ATOM   3301 O  O     . ASN A 1 399 ? 54.882  12.758  38.022  1.00 97.56  ? 399 ASN A O     1 
ATOM   3302 C  CB    . ASN A 1 399 ? 55.007  12.641  40.766  1.00 92.46  ? 399 ASN A CB    1 
ATOM   3303 C  CG    . ASN A 1 399 ? 54.899  12.420  42.265  1.00 98.86  ? 399 ASN A CG    1 
ATOM   3304 O  OD1   . ASN A 1 399 ? 54.032  12.992  42.927  1.00 97.86  ? 399 ASN A OD1   1 
ATOM   3305 N  ND2   . ASN A 1 399 ? 55.783  11.590  42.807  1.00 107.01 ? 399 ASN A ND2   1 
ATOM   3306 N  N     . ILE A 1 400 ? 52.709  13.343  37.935  1.00 87.87  ? 400 ILE A N     1 
ATOM   3307 C  CA    . ILE A 1 400 ? 52.663  13.536  36.491  1.00 87.96  ? 400 ILE A CA    1 
ATOM   3308 C  C     . ILE A 1 400 ? 52.468  15.015  36.194  1.00 88.84  ? 400 ILE A C     1 
ATOM   3309 O  O     . ILE A 1 400 ? 51.772  15.722  36.932  1.00 90.58  ? 400 ILE A O     1 
ATOM   3310 C  CB    . ILE A 1 400 ? 51.535  12.705  35.849  1.00 83.43  ? 400 ILE A CB    1 
ATOM   3311 C  CG1   . ILE A 1 400 ? 51.443  11.328  36.504  1.00 84.25  ? 400 ILE A CG1   1 
ATOM   3312 C  CG2   . ILE A 1 400 ? 51.746  12.573  34.348  1.00 82.87  ? 400 ILE A CG2   1 
ATOM   3313 C  CD1   . ILE A 1 400 ? 50.141  10.621  36.227  1.00 90.64  ? 400 ILE A CD1   1 
ATOM   3314 N  N     . VAL A 1 401 ? 53.084  15.479  35.111  1.00 79.89  ? 401 VAL A N     1 
ATOM   3315 C  CA    . VAL A 1 401 ? 52.832  16.808  34.570  1.00 71.43  ? 401 VAL A CA    1 
ATOM   3316 C  C     . VAL A 1 401 ? 52.241  16.647  33.178  1.00 74.82  ? 401 VAL A C     1 
ATOM   3317 O  O     . VAL A 1 401 ? 52.573  15.708  32.447  1.00 77.46  ? 401 VAL A O     1 
ATOM   3318 C  CB    . VAL A 1 401 ? 54.106  17.681  34.519  1.00 79.70  ? 401 VAL A CB    1 
ATOM   3319 C  CG1   . VAL A 1 401 ? 54.488  18.156  35.912  1.00 74.87  ? 401 VAL A CG1   1 
ATOM   3320 C  CG2   . VAL A 1 401 ? 55.252  16.918  33.871  1.00 77.72  ? 401 VAL A CG2   1 
ATOM   3321 N  N     . TYR A 1 402 ? 51.351  17.565  32.817  1.00 64.78  ? 402 TYR A N     1 
ATOM   3322 C  CA    . TYR A 1 402 ? 50.797  17.636  31.471  1.00 67.33  ? 402 TYR A CA    1 
ATOM   3323 C  C     . TYR A 1 402 ? 51.318  18.908  30.816  1.00 72.84  ? 402 TYR A C     1 
ATOM   3324 O  O     . TYR A 1 402 ? 50.960  20.017  31.227  1.00 75.68  ? 402 TYR A O     1 
ATOM   3325 C  CB    . TYR A 1 402 ? 49.270  17.615  31.484  1.00 73.01  ? 402 TYR A CB    1 
ATOM   3326 C  CG    . TYR A 1 402 ? 48.666  17.597  30.097  1.00 59.50  ? 402 TYR A CG    1 
ATOM   3327 C  CD1   . TYR A 1 402 ? 48.927  16.552  29.220  1.00 68.28  ? 402 TYR A CD1   1 
ATOM   3328 C  CD2   . TYR A 1 402 ? 47.852  18.632  29.657  1.00 73.08  ? 402 TYR A CD2   1 
ATOM   3329 C  CE1   . TYR A 1 402 ? 48.383  16.530  27.950  1.00 65.92  ? 402 TYR A CE1   1 
ATOM   3330 C  CE2   . TYR A 1 402 ? 47.304  18.619  28.387  1.00 82.31  ? 402 TYR A CE2   1 
ATOM   3331 C  CZ    . TYR A 1 402 ? 47.573  17.565  27.538  1.00 77.67  ? 402 TYR A CZ    1 
ATOM   3332 O  OH    . TYR A 1 402 ? 47.033  17.544  26.271  1.00 91.86  ? 402 TYR A OH    1 
ATOM   3333 N  N     . LEU A 1 403 ? 52.169  18.746  29.811  1.00 66.94  ? 403 LEU A N     1 
ATOM   3334 C  CA    . LEU A 1 403 ? 52.668  19.859  29.020  1.00 66.10  ? 403 LEU A CA    1 
ATOM   3335 C  C     . LEU A 1 403 ? 51.910  19.892  27.703  1.00 66.49  ? 403 LEU A C     1 
ATOM   3336 O  O     . LEU A 1 403 ? 51.708  18.847  27.075  1.00 64.07  ? 403 LEU A O     1 
ATOM   3337 C  CB    . LEU A 1 403 ? 54.170  19.725  28.772  1.00 64.30  ? 403 LEU A CB    1 
ATOM   3338 C  CG    . LEU A 1 403 ? 55.013  19.460  30.019  1.00 59.23  ? 403 LEU A CG    1 
ATOM   3339 C  CD1   . LEU A 1 403 ? 56.480  19.340  29.648  1.00 72.04  ? 403 LEU A CD1   1 
ATOM   3340 C  CD2   . LEU A 1 403 ? 54.800  20.555  31.049  1.00 67.26  ? 403 LEU A CD2   1 
ATOM   3341 N  N     . ASP A 1 404 ? 51.487  21.084  27.289  1.00 60.52  ? 404 ASP A N     1 
ATOM   3342 C  CA    . ASP A 1 404 ? 50.648  21.219  26.110  1.00 63.74  ? 404 ASP A CA    1 
ATOM   3343 C  C     . ASP A 1 404 ? 51.026  22.471  25.334  1.00 68.74  ? 404 ASP A C     1 
ATOM   3344 O  O     . ASP A 1 404 ? 51.485  23.465  25.903  1.00 72.95  ? 404 ASP A O     1 
ATOM   3345 C  CB    . ASP A 1 404 ? 49.163  21.274  26.484  1.00 67.69  ? 404 ASP A CB    1 
ATOM   3346 C  CG    . ASP A 1 404 ? 48.268  20.742  25.386  1.00 76.67  ? 404 ASP A CG    1 
ATOM   3347 O  OD1   . ASP A 1 404 ? 48.161  19.506  25.238  1.00 86.56  ? 404 ASP A OD1   1 
ATOM   3348 O  OD2   . ASP A 1 404 ? 47.686  21.564  24.655  1.00 81.58  ? 404 ASP A OD2   1 
ATOM   3349 N  N     . PHE A 1 405 ? 50.816  22.407  24.022  1.00 61.39  ? 405 PHE A N     1 
ATOM   3350 C  CA    . PHE A 1 405 ? 51.095  23.523  23.134  1.00 71.04  ? 405 PHE A CA    1 
ATOM   3351 C  C     . PHE A 1 405 ? 49.951  24.530  23.163  1.00 76.59  ? 405 PHE A C     1 
ATOM   3352 O  O     . PHE A 1 405 ? 48.787  24.176  23.370  1.00 76.01  ? 405 PHE A O     1 
ATOM   3353 C  CB    . PHE A 1 405 ? 51.302  23.023  21.703  1.00 75.79  ? 405 PHE A CB    1 
ATOM   3354 C  CG    . PHE A 1 405 ? 52.705  22.576  21.409  1.00 70.90  ? 405 PHE A CG    1 
ATOM   3355 C  CD1   . PHE A 1 405 ? 53.737  23.493  21.332  1.00 68.07  ? 405 PHE A CD1   1 
ATOM   3356 C  CD2   . PHE A 1 405 ? 52.989  21.236  21.201  1.00 66.62  ? 405 PHE A CD2   1 
ATOM   3357 C  CE1   . PHE A 1 405 ? 55.028  23.082  21.058  1.00 75.69  ? 405 PHE A CE1   1 
ATOM   3358 C  CE2   . PHE A 1 405 ? 54.280  20.819  20.928  1.00 68.14  ? 405 PHE A CE2   1 
ATOM   3359 C  CZ    . PHE A 1 405 ? 55.300  21.743  20.856  1.00 56.98  ? 405 PHE A CZ    1 
ATOM   3360 N  N     . ARG A 1 406 ? 50.293  25.798  22.950  1.00 72.06  ? 406 ARG A N     1 
ATOM   3361 C  CA    . ARG A 1 406 ? 49.295  26.857  22.854  1.00 71.06  ? 406 ARG A CA    1 
ATOM   3362 C  C     . ARG A 1 406 ? 48.765  26.902  21.428  1.00 75.34  ? 406 ARG A C     1 
ATOM   3363 O  O     . ARG A 1 406 ? 49.506  27.247  20.502  1.00 77.72  ? 406 ARG A O     1 
ATOM   3364 C  CB    . ARG A 1 406 ? 49.895  28.204  23.240  1.00 71.34  ? 406 ARG A CB    1 
ATOM   3365 C  CG    . ARG A 1 406 ? 49.038  29.383  22.801  1.00 88.93  ? 406 ARG A CG    1 
ATOM   3366 C  CD    . ARG A 1 406 ? 49.317  30.625  23.630  1.00 97.75  ? 406 ARG A CD    1 
ATOM   3367 N  NE    . ARG A 1 406 ? 50.724  31.016  23.642  1.00 108.98 ? 406 ARG A NE    1 
ATOM   3368 C  CZ    . ARG A 1 406 ? 51.483  31.226  22.571  1.00 112.09 ? 406 ARG A CZ    1 
ATOM   3369 N  NH1   . ARG A 1 406 ? 50.993  31.160  21.342  1.00 97.66  ? 406 ARG A NH1   1 
ATOM   3370 N  NH2   . ARG A 1 406 ? 52.767  31.531  22.739  1.00 94.13  ? 406 ARG A NH2   1 
ATOM   3371 N  N     . SER A 1 407 ? 47.479  26.575  21.257  1.00 73.10  ? 407 SER A N     1 
ATOM   3372 C  CA    . SER A 1 407 ? 46.808  26.595  19.959  1.00 69.62  ? 407 SER A CA    1 
ATOM   3373 C  C     . SER A 1 407 ? 47.702  26.015  18.871  1.00 68.68  ? 407 SER A C     1 
ATOM   3374 O  O     . SER A 1 407 ? 48.124  26.734  17.960  1.00 67.11  ? 407 SER A O     1 
ATOM   3375 C  CB    . SER A 1 407 ? 46.384  28.020  19.598  1.00 67.71  ? 407 SER A CB    1 
ATOM   3376 O  OG    . SER A 1 407 ? 45.405  28.498  20.503  1.00 80.65  ? 407 SER A OG    1 
ATOM   3377 N  N     . LEU A 1 408 ? 47.995  24.716  18.970  1.00 62.23  ? 408 LEU A N     1 
ATOM   3378 C  CA    . LEU A 1 408 ? 49.061  24.121  18.169  1.00 64.28  ? 408 LEU A CA    1 
ATOM   3379 C  C     . LEU A 1 408 ? 48.807  24.301  16.676  1.00 61.52  ? 408 LEU A C     1 
ATOM   3380 O  O     . LEU A 1 408 ? 49.694  24.739  15.935  1.00 74.30  ? 408 LEU A O     1 
ATOM   3381 C  CB    . LEU A 1 408 ? 49.215  22.643  18.535  1.00 62.68  ? 408 LEU A CB    1 
ATOM   3382 C  CG    . LEU A 1 408 ? 50.471  21.890  18.082  1.00 69.23  ? 408 LEU A CG    1 
ATOM   3383 C  CD1   . LEU A 1 408 ? 50.298  21.294  16.698  1.00 70.07  ? 408 LEU A CD1   1 
ATOM   3384 C  CD2   . LEU A 1 408 ? 51.684  22.804  18.109  1.00 67.24  ? 408 LEU A CD2   1 
ATOM   3385 N  N     . TYR A 1 409 ? 47.593  23.985  16.215  1.00 62.48  ? 409 TYR A N     1 
ATOM   3386 C  CA    . TYR A 1 409 ? 47.327  24.065  14.779  1.00 56.14  ? 409 TYR A CA    1 
ATOM   3387 C  C     . TYR A 1 409 ? 47.262  25.504  14.281  1.00 52.24  ? 409 TYR A C     1 
ATOM   3388 O  O     . TYR A 1 409 ? 47.926  25.813  13.276  1.00 62.96  ? 409 TYR A O     1 
ATOM   3389 C  CB    . TYR A 1 409 ? 46.057  23.280  14.434  1.00 52.96  ? 409 TYR A CB    1 
ATOM   3390 C  CG    . TYR A 1 409 ? 46.250  21.780  14.380  1.00 49.07  ? 409 TYR A CG    1 
ATOM   3391 C  CD1   . TYR A 1 409 ? 47.324  21.175  15.014  1.00 49.40  ? 409 TYR A CD1   1 
ATOM   3392 C  CD2   . TYR A 1 409 ? 45.352  20.970  13.701  1.00 55.36  ? 409 TYR A CD2   1 
ATOM   3393 C  CE1   . TYR A 1 409 ? 47.502  19.806  14.973  1.00 57.06  ? 409 TYR A CE1   1 
ATOM   3394 C  CE2   . TYR A 1 409 ? 45.520  19.598  13.653  1.00 59.05  ? 409 TYR A CE2   1 
ATOM   3395 C  CZ    . TYR A 1 409 ? 46.598  19.021  14.291  1.00 57.67  ? 409 TYR A CZ    1 
ATOM   3396 O  OH    . TYR A 1 409 ? 46.773  17.657  14.248  1.00 51.51  ? 409 TYR A OH    1 
ATOM   3397 N  N     . PRO A 1 410 ? 46.508  26.422  14.899  1.00 67.89  ? 410 PRO A N     1 
ATOM   3398 C  CA    . PRO A 1 410 ? 46.536  27.810  14.409  1.00 60.84  ? 410 PRO A CA    1 
ATOM   3399 C  C     . PRO A 1 410 ? 47.908  28.454  14.510  1.00 54.71  ? 410 PRO A C     1 
ATOM   3400 O  O     . PRO A 1 410 ? 48.249  29.295  13.670  1.00 52.67  ? 410 PRO A O     1 
ATOM   3401 C  CB    . PRO A 1 410 ? 45.509  28.518  15.303  1.00 51.98  ? 410 PRO A CB    1 
ATOM   3402 C  CG    . PRO A 1 410 ? 44.613  27.431  15.777  1.00 47.44  ? 410 PRO A CG    1 
ATOM   3403 C  CD    . PRO A 1 410 ? 45.521  26.262  15.983  1.00 63.50  ? 410 PRO A CD    1 
ATOM   3404 N  N     . SER A 1 411 ? 48.711  28.082  15.510  1.00 56.26  ? 411 SER A N     1 
ATOM   3405 C  CA    . SER A 1 411 ? 50.067  28.615  15.593  1.00 63.01  ? 411 SER A CA    1 
ATOM   3406 C  C     . SER A 1 411 ? 50.936  28.112  14.447  1.00 60.17  ? 411 SER A C     1 
ATOM   3407 O  O     . SER A 1 411 ? 51.829  28.832  13.987  1.00 60.91  ? 411 SER A O     1 
ATOM   3408 C  CB    . SER A 1 411 ? 50.697  28.253  16.937  1.00 64.12  ? 411 SER A CB    1 
ATOM   3409 O  OG    . SER A 1 411 ? 49.977  28.835  18.011  1.00 66.81  ? 411 SER A OG    1 
ATOM   3410 N  N     . ILE A 1 412 ? 50.692  26.888  13.973  1.00 57.53  ? 412 ILE A N     1 
ATOM   3411 C  CA    . ILE A 1 412 ? 51.445  26.367  12.835  1.00 51.36  ? 412 ILE A CA    1 
ATOM   3412 C  C     . ILE A 1 412 ? 51.086  27.132  11.568  1.00 57.99  ? 412 ILE A C     1 
ATOM   3413 O  O     . ILE A 1 412 ? 51.964  27.521  10.789  1.00 56.50  ? 412 ILE A O     1 
ATOM   3414 C  CB    . ILE A 1 412 ? 51.194  24.859  12.669  1.00 55.66  ? 412 ILE A CB    1 
ATOM   3415 C  CG1   . ILE A 1 412 ? 51.944  24.072  13.741  1.00 45.52  ? 412 ILE A CG1   1 
ATOM   3416 C  CG2   . ILE A 1 412 ? 51.613  24.394  11.282  1.00 50.03  ? 412 ILE A CG2   1 
ATOM   3417 C  CD1   . ILE A 1 412 ? 51.664  22.598  13.696  1.00 56.26  ? 412 ILE A CD1   1 
ATOM   3418 N  N     . ILE A 1 413 ? 49.788  27.352  11.341  1.00 56.33  ? 413 ILE A N     1 
ATOM   3419 C  CA    . ILE A 1 413 ? 49.348  28.111  10.174  1.00 50.99  ? 413 ILE A CA    1 
ATOM   3420 C  C     . ILE A 1 413 ? 49.964  29.503  10.187  1.00 53.05  ? 413 ILE A C     1 
ATOM   3421 O  O     . ILE A 1 413 ? 50.384  30.025  9.147   1.00 49.83  ? 413 ILE A O     1 
ATOM   3422 C  CB    . ILE A 1 413 ? 47.810  28.174  10.130  1.00 53.00  ? 413 ILE A CB    1 
ATOM   3423 C  CG1   . ILE A 1 413 ? 47.244  26.950  9.421   1.00 55.46  ? 413 ILE A CG1   1 
ATOM   3424 C  CG2   . ILE A 1 413 ? 47.343  29.424  9.412   1.00 45.15  ? 413 ILE A CG2   1 
ATOM   3425 C  CD1   . ILE A 1 413 ? 45.885  26.533  9.937   1.00 61.32  ? 413 ILE A CD1   1 
ATOM   3426 N  N     . ILE A 1 414 ? 50.040  30.117  11.367  1.00 52.81  ? 414 ILE A N     1 
ATOM   3427 C  CA    . ILE A 1 414 ? 50.598  31.461  11.476  1.00 55.01  ? 414 ILE A CA    1 
ATOM   3428 C  C     . ILE A 1 414 ? 52.106  31.433  11.264  1.00 59.96  ? 414 ILE A C     1 
ATOM   3429 O  O     . ILE A 1 414 ? 52.652  32.215  10.477  1.00 59.12  ? 414 ILE A O     1 
ATOM   3430 C  CB    . ILE A 1 414 ? 50.232  32.081  12.835  1.00 59.45  ? 414 ILE A CB    1 
ATOM   3431 C  CG1   . ILE A 1 414 ? 48.723  32.311  12.924  1.00 51.06  ? 414 ILE A CG1   1 
ATOM   3432 C  CG2   . ILE A 1 414 ? 50.992  33.379  13.050  1.00 47.84  ? 414 ILE A CG2   1 
ATOM   3433 C  CD1   . ILE A 1 414 ? 48.238  32.610  14.320  1.00 44.60  ? 414 ILE A CD1   1 
ATOM   3434 N  N     . THR A 1 415 ? 52.801  30.531  11.962  1.00 63.00  ? 415 THR A N     1 
ATOM   3435 C  CA    . THR A 1 415 ? 54.260  30.509  11.909  1.00 64.13  ? 415 THR A CA    1 
ATOM   3436 C  C     . THR A 1 415 ? 54.768  30.227  10.501  1.00 65.08  ? 415 THR A C     1 
ATOM   3437 O  O     . THR A 1 415 ? 55.740  30.844  10.049  1.00 65.37  ? 415 THR A O     1 
ATOM   3438 C  CB    . THR A 1 415 ? 54.806  29.468  12.887  1.00 61.33  ? 415 THR A CB    1 
ATOM   3439 O  OG1   . THR A 1 415 ? 54.225  29.672  14.181  1.00 66.80  ? 415 THR A OG1   1 
ATOM   3440 C  CG2   . THR A 1 415 ? 56.320  29.571  12.989  1.00 55.73  ? 415 THR A CG2   1 
ATOM   3441 N  N     . HIS A 1 416 ? 54.125  29.306  9.790   1.00 57.68  ? 416 HIS A N     1 
ATOM   3442 C  CA    . HIS A 1 416 ? 54.592  28.871  8.482   1.00 56.47  ? 416 HIS A CA    1 
ATOM   3443 C  C     . HIS A 1 416 ? 53.787  29.464  7.333   1.00 57.39  ? 416 HIS A C     1 
ATOM   3444 O  O     . HIS A 1 416 ? 53.978  29.054  6.184   1.00 61.84  ? 416 HIS A O     1 
ATOM   3445 C  CB    . HIS A 1 416 ? 54.575  27.344  8.408   1.00 61.00  ? 416 HIS A CB    1 
ATOM   3446 C  CG    . HIS A 1 416 ? 55.505  26.686  9.379   1.00 60.72  ? 416 HIS A CG    1 
ATOM   3447 N  ND1   . HIS A 1 416 ? 56.834  27.032  9.487   1.00 58.31  ? 416 HIS A ND1   1 
ATOM   3448 C  CD2   . HIS A 1 416 ? 55.293  25.717  10.300  1.00 54.83  ? 416 HIS A CD2   1 
ATOM   3449 C  CE1   . HIS A 1 416 ? 57.404  26.295  10.424  1.00 52.55  ? 416 HIS A CE1   1 
ATOM   3450 N  NE2   . HIS A 1 416 ? 56.491  25.489  10.933  1.00 53.60  ? 416 HIS A NE2   1 
ATOM   3451 N  N     . ASN A 1 417 ? 52.899  30.419  7.617   1.00 66.28  ? 417 ASN A N     1 
ATOM   3452 C  CA    . ASN A 1 417 ? 52.099  31.101  6.598   1.00 63.83  ? 417 ASN A CA    1 
ATOM   3453 C  C     . ASN A 1 417 ? 51.371  30.101  5.700   1.00 58.02  ? 417 ASN A C     1 
ATOM   3454 O  O     . ASN A 1 417 ? 51.408  30.183  4.470   1.00 53.56  ? 417 ASN A O     1 
ATOM   3455 C  CB    . ASN A 1 417 ? 52.962  32.055  5.771   1.00 55.44  ? 417 ASN A CB    1 
ATOM   3456 C  CG    . ASN A 1 417 ? 52.280  33.387  5.524   1.00 56.05  ? 417 ASN A CG    1 
ATOM   3457 O  OD1   . ASN A 1 417 ? 51.710  33.984  6.437   1.00 55.32  ? 417 ASN A OD1   1 
ATOM   3458 N  ND2   . ASN A 1 417 ? 52.336  33.860  4.284   1.00 62.32  ? 417 ASN A ND2   1 
ATOM   3459 N  N     . VAL A 1 418 ? 50.700  29.145  6.333   1.00 50.61  ? 418 VAL A N     1 
ATOM   3460 C  CA    . VAL A 1 418 ? 49.977  28.107  5.607   1.00 56.27  ? 418 VAL A CA    1 
ATOM   3461 C  C     . VAL A 1 418 ? 48.632  28.667  5.164   1.00 60.57  ? 418 VAL A C     1 
ATOM   3462 O  O     . VAL A 1 418 ? 47.805  29.065  5.993   1.00 57.82  ? 418 VAL A O     1 
ATOM   3463 C  CB    . VAL A 1 418 ? 49.799  26.851  6.470   1.00 56.26  ? 418 VAL A CB    1 
ATOM   3464 C  CG1   . VAL A 1 418 ? 49.226  25.719  5.639   1.00 59.65  ? 418 VAL A CG1   1 
ATOM   3465 C  CG2   . VAL A 1 418 ? 51.132  26.445  7.084   1.00 58.12  ? 418 VAL A CG2   1 
ATOM   3466 N  N     . SER A 1 419 ? 48.412  28.697  3.853   1.00 53.13  ? 419 SER A N     1 
ATOM   3467 C  CA    . SER A 1 419 ? 47.193  29.241  3.274   1.00 52.71  ? 419 SER A CA    1 
ATOM   3468 C  C     . SER A 1 419 ? 47.100  28.771  1.832   1.00 63.80  ? 419 SER A C     1 
ATOM   3469 O  O     . SER A 1 419 ? 48.135  28.579  1.182   1.00 63.79  ? 419 SER A O     1 
ATOM   3470 C  CB    . SER A 1 419 ? 47.190  30.774  3.336   1.00 56.00  ? 419 SER A CB    1 
ATOM   3471 O  OG    . SER A 1 419 ? 45.870  31.289  3.321   1.00 64.66  ? 419 SER A OG    1 
ATOM   3472 N  N     . PRO A 1 420 ? 45.891  28.573  1.307   1.00 70.65  ? 420 PRO A N     1 
ATOM   3473 C  CA    . PRO A 1 420 ? 45.768  28.194  -0.109  1.00 66.36  ? 420 PRO A CA    1 
ATOM   3474 C  C     . PRO A 1 420 ? 46.426  29.184  -1.048  1.00 62.29  ? 420 PRO A C     1 
ATOM   3475 O  O     . PRO A 1 420 ? 46.879  28.798  -2.134  1.00 66.79  ? 420 PRO A O     1 
ATOM   3476 C  CB    . PRO A 1 420 ? 44.249  28.142  -0.325  1.00 52.81  ? 420 PRO A CB    1 
ATOM   3477 C  CG    . PRO A 1 420 ? 43.674  27.956  1.040   1.00 55.92  ? 420 PRO A CG    1 
ATOM   3478 C  CD    . PRO A 1 420 ? 44.581  28.691  1.968   1.00 53.84  ? 420 PRO A CD    1 
ATOM   3479 N  N     . ASP A 1 421 ? 46.499  30.454  -0.654  1.00 60.93  ? 421 ASP A N     1 
ATOM   3480 C  CA    . ASP A 1 421 ? 47.080  31.510  -1.470  1.00 68.71  ? 421 ASP A CA    1 
ATOM   3481 C  C     . ASP A 1 421 ? 48.594  31.606  -1.341  1.00 71.48  ? 421 ASP A C     1 
ATOM   3482 O  O     . ASP A 1 421 ? 49.203  32.430  -2.030  1.00 74.79  ? 421 ASP A O     1 
ATOM   3483 C  CB    . ASP A 1 421 ? 46.448  32.853  -1.100  1.00 49.42  ? 421 ASP A CB    1 
ATOM   3484 C  CG    . ASP A 1 421 ? 46.347  33.051  0.399   1.00 56.31  ? 421 ASP A CG    1 
ATOM   3485 O  OD1   . ASP A 1 421 ? 45.524  32.361  1.037   1.00 56.86  ? 421 ASP A OD1   1 
ATOM   3486 O  OD2   . ASP A 1 421 ? 47.096  33.889  0.942   1.00 67.98  ? 421 ASP A OD2   1 
ATOM   3487 N  N     . THR A 1 422 ? 49.217  30.805  -0.477  1.00 57.20  ? 422 THR A N     1 
ATOM   3488 C  CA    . THR A 1 422 ? 50.666  30.792  -0.345  1.00 67.36  ? 422 THR A CA    1 
ATOM   3489 C  C     . THR A 1 422 ? 51.287  29.460  -0.734  1.00 76.92  ? 422 THR A C     1 
ATOM   3490 O  O     . THR A 1 422 ? 52.508  29.307  -0.621  1.00 75.31  ? 422 THR A O     1 
ATOM   3491 C  CB    . THR A 1 422 ? 51.079  31.138  1.092   1.00 63.67  ? 422 THR A CB    1 
ATOM   3492 O  OG1   . THR A 1 422 ? 50.615  30.115  1.982   1.00 63.65  ? 422 THR A OG1   1 
ATOM   3493 C  CG2   . THR A 1 422 ? 50.495  32.475  1.508   1.00 50.92  ? 422 THR A CG2   1 
ATOM   3494 N  N     . LEU A 1 423 ? 50.489  28.500  -1.193  1.00 68.42  ? 423 LEU A N     1 
ATOM   3495 C  CA    . LEU A 1 423 ? 50.985  27.164  -1.497  1.00 65.44  ? 423 LEU A CA    1 
ATOM   3496 C  C     . LEU A 1 423 ? 51.650  27.146  -2.870  1.00 75.36  ? 423 LEU A C     1 
ATOM   3497 O  O     . LEU A 1 423 ? 51.018  27.489  -3.876  1.00 79.44  ? 423 LEU A O     1 
ATOM   3498 C  CB    . LEU A 1 423 ? 49.838  26.159  -1.439  1.00 64.33  ? 423 LEU A CB    1 
ATOM   3499 C  CG    . LEU A 1 423 ? 50.099  24.761  -2.001  1.00 77.65  ? 423 LEU A CG    1 
ATOM   3500 C  CD1   . LEU A 1 423 ? 51.015  23.964  -1.085  1.00 62.68  ? 423 LEU A CD1   1 
ATOM   3501 C  CD2   . LEU A 1 423 ? 48.783  24.032  -2.222  1.00 57.24  ? 423 LEU A CD2   1 
ATOM   3502 N  N     . ASN A 1 424 ? 52.925  26.750  -2.905  1.00 69.65  ? 424 ASN A N     1 
ATOM   3503 C  CA    . ASN A 1 424 ? 53.651  26.500  -4.152  1.00 60.96  ? 424 ASN A CA    1 
ATOM   3504 C  C     . ASN A 1 424 ? 53.650  27.722  -5.068  1.00 64.29  ? 424 ASN A C     1 
ATOM   3505 O  O     . ASN A 1 424 ? 53.487  27.607  -6.284  1.00 75.90  ? 424 ASN A O     1 
ATOM   3506 C  CB    . ASN A 1 424 ? 53.081  25.282  -4.883  1.00 64.78  ? 424 ASN A CB    1 
ATOM   3507 C  CG    . ASN A 1 424 ? 53.210  24.007  -4.079  1.00 77.58  ? 424 ASN A CG    1 
ATOM   3508 O  OD1   . ASN A 1 424 ? 54.040  23.909  -3.175  1.00 79.99  ? 424 ASN A OD1   1 
ATOM   3509 N  ND2   . ASN A 1 424 ? 52.384  23.019  -4.403  1.00 89.71  ? 424 ASN A ND2   1 
ATOM   3510 N  N     . ARG A 1 425 ? 53.840  28.902  -4.484  1.00 71.07  ? 425 ARG A N     1 
ATOM   3511 C  CA    . ARG A 1 425 ? 53.858  30.133  -5.261  1.00 77.97  ? 425 ARG A CA    1 
ATOM   3512 C  C     . ARG A 1 425 ? 55.168  30.262  -6.028  1.00 80.27  ? 425 ARG A C     1 
ATOM   3513 O  O     . ARG A 1 425 ? 56.251  30.074  -5.464  1.00 97.84  ? 425 ARG A O     1 
ATOM   3514 C  CB    . ARG A 1 425 ? 53.659  31.344  -4.352  1.00 83.43  ? 425 ARG A CB    1 
ATOM   3515 C  CG    . ARG A 1 425 ? 52.311  31.386  -3.664  1.00 80.54  ? 425 ARG A CG    1 
ATOM   3516 C  CD    . ARG A 1 425 ? 51.588  32.686  -3.977  1.00 109.67 ? 425 ARG A CD    1 
ATOM   3517 N  NE    . ARG A 1 425 ? 51.052  32.714  -5.334  1.00 108.76 ? 425 ARG A NE    1 
ATOM   3518 C  CZ    . ARG A 1 425 ? 50.007  32.010  -5.749  1.00 104.18 ? 425 ARG A CZ    1 
ATOM   3519 N  NH1   . ARG A 1 425 ? 49.346  31.203  -4.934  1.00 102.93 ? 425 ARG A NH1   1 
ATOM   3520 N  NH2   . ARG A 1 425 ? 49.613  32.120  -7.015  1.00 115.31 ? 425 ARG A NH2   1 
ATOM   3521 N  N     . GLU A 1 426 ? 55.065  30.587  -7.313  1.00 87.43  ? 426 GLU A N     1 
ATOM   3522 C  CA    . GLU A 1 426 ? 56.249  30.774  -8.137  1.00 94.05  ? 426 GLU A CA    1 
ATOM   3523 C  C     . GLU A 1 426 ? 56.950  32.080  -7.780  1.00 88.92  ? 426 GLU A C     1 
ATOM   3524 O  O     . GLU A 1 426 ? 56.330  33.038  -7.310  1.00 88.75  ? 426 GLU A O     1 
ATOM   3525 C  CB    . GLU A 1 426 ? 55.876  30.772  -9.619  1.00 100.86 ? 426 GLU A CB    1 
ATOM   3526 C  CG    . GLU A 1 426 ? 54.864  29.711  -10.013 1.00 105.57 ? 426 GLU A CG    1 
ATOM   3527 C  CD    . GLU A 1 426 ? 55.233  29.013  -11.308 1.00 119.24 ? 426 GLU A CD    1 
ATOM   3528 O  OE1   . GLU A 1 426 ? 56.429  28.712  -11.503 1.00 131.36 ? 426 GLU A OE1   1 
ATOM   3529 O  OE2   . GLU A 1 426 ? 54.327  28.768  -12.132 1.00 111.71 ? 426 GLU A OE2   1 
ATOM   3530 N  N     . GLY A 1 427 ? 58.260  32.110  -8.014  1.00 82.67  ? 427 GLY A N     1 
ATOM   3531 C  CA    . GLY A 1 427 ? 59.042  33.293  -7.715  1.00 81.61  ? 427 GLY A CA    1 
ATOM   3532 C  C     . GLY A 1 427 ? 59.148  33.617  -6.243  1.00 85.15  ? 427 GLY A C     1 
ATOM   3533 O  O     . GLY A 1 427 ? 59.353  34.781  -5.886  1.00 86.15  ? 427 GLY A O     1 
ATOM   3534 N  N     A CYS A 1 428 ? 59.002  32.626  -5.368  0.48 82.57  ? 428 CYS A N     1 
ATOM   3535 N  N     B CYS A 1 428 ? 59.023  32.612  -5.382  0.52 82.88  ? 428 CYS A N     1 
ATOM   3536 C  CA    A CYS A 1 428 ? 59.068  32.880  -3.936  0.48 80.06  ? 428 CYS A CA    1 
ATOM   3537 C  CA    B CYS A 1 428 ? 59.109  32.828  -3.946  0.52 80.60  ? 428 CYS A CA    1 
ATOM   3538 C  C     A CYS A 1 428 ? 60.513  33.083  -3.497  0.48 84.87  ? 428 CYS A C     1 
ATOM   3539 C  C     B CYS A 1 428 ? 60.547  33.105  -3.526  0.52 84.84  ? 428 CYS A C     1 
ATOM   3540 O  O     A CYS A 1 428 ? 61.431  32.431  -4.003  0.48 78.35  ? 428 CYS A O     1 
ATOM   3541 O  O     B CYS A 1 428 ? 61.494  32.526  -4.065  0.52 78.19  ? 428 CYS A O     1 
ATOM   3542 C  CB    A CYS A 1 428 ? 58.431  31.730  -3.155  0.48 74.01  ? 428 CYS A CB    1 
ATOM   3543 C  CB    B CYS A 1 428 ? 58.569  31.606  -3.205  0.52 74.19  ? 428 CYS A CB    1 
ATOM   3544 S  SG    A CYS A 1 428 ? 59.007  30.083  -3.619  0.48 82.77  ? 428 CYS A SG    1 
ATOM   3545 S  SG    B CYS A 1 428 ? 58.702  31.702  -1.418  0.52 74.88  ? 428 CYS A SG    1 
ATOM   3546 N  N     . GLY A 1 429 ? 60.707  34.001  -2.554  1.00 86.87  ? 429 GLY A N     1 
ATOM   3547 C  CA    . GLY A 1 429 ? 62.025  34.311  -2.039  1.00 73.12  ? 429 GLY A CA    1 
ATOM   3548 C  C     . GLY A 1 429 ? 62.324  33.605  -0.734  1.00 66.51  ? 429 GLY A C     1 
ATOM   3549 O  O     . GLY A 1 429 ? 63.467  33.213  -0.476  1.00 75.93  ? 429 GLY A O     1 
ATOM   3550 N  N     . GLU A 1 430 ? 61.301  33.440  0.101   1.00 65.00  ? 430 GLU A N     1 
ATOM   3551 C  CA    . GLU A 1 430 ? 61.429  32.731  1.372   1.00 65.41  ? 430 GLU A CA    1 
ATOM   3552 C  C     . GLU A 1 430 ? 60.233  31.804  1.515   1.00 73.00  ? 430 GLU A C     1 
ATOM   3553 O  O     . GLU A 1 430 ? 59.098  32.274  1.642   1.00 77.92  ? 430 GLU A O     1 
ATOM   3554 C  CB    . GLU A 1 430 ? 61.502  33.702  2.551   1.00 64.47  ? 430 GLU A CB    1 
ATOM   3555 C  CG    . GLU A 1 430 ? 61.644  33.010  3.899   1.00 76.48  ? 430 GLU A CG    1 
ATOM   3556 C  CD    . GLU A 1 430 ? 61.573  33.978  5.065   1.00 93.53  ? 430 GLU A CD    1 
ATOM   3557 O  OE1   . GLU A 1 430 ? 61.246  35.162  4.837   1.00 87.10  ? 430 GLU A OE1   1 
ATOM   3558 O  OE2   . GLU A 1 430 ? 61.829  33.550  6.210   1.00 102.42 ? 430 GLU A OE2   1 
ATOM   3559 N  N     . TYR A 1 431 ? 60.477  30.495  1.496   1.00 64.02  ? 431 TYR A N     1 
ATOM   3560 C  CA    . TYR A 1 431 ? 59.415  29.515  1.657   1.00 68.63  ? 431 TYR A CA    1 
ATOM   3561 C  C     . TYR A 1 431 ? 59.756  28.559  2.791   1.00 68.30  ? 431 TYR A C     1 
ATOM   3562 O  O     . TYR A 1 431 ? 60.918  28.401  3.176   1.00 68.98  ? 431 TYR A O     1 
ATOM   3563 C  CB    . TYR A 1 431 ? 59.154  28.741  0.347   1.00 72.48  ? 431 TYR A CB    1 
ATOM   3564 C  CG    . TYR A 1 431 ? 60.312  27.915  -0.182  1.00 78.25  ? 431 TYR A CG    1 
ATOM   3565 C  CD1   . TYR A 1 431 ? 60.664  26.704  0.406   1.00 71.90  ? 431 TYR A CD1   1 
ATOM   3566 C  CD2   . TYR A 1 431 ? 61.053  28.349  -1.274  1.00 87.32  ? 431 TYR A CD2   1 
ATOM   3567 C  CE1   . TYR A 1 431 ? 61.719  25.953  -0.082  1.00 86.94  ? 431 TYR A CE1   1 
ATOM   3568 C  CE2   . TYR A 1 431 ? 62.113  27.602  -1.765  1.00 87.02  ? 431 TYR A CE2   1 
ATOM   3569 C  CZ    . TYR A 1 431 ? 62.442  26.404  -1.163  1.00 93.49  ? 431 TYR A CZ    1 
ATOM   3570 O  OH    . TYR A 1 431 ? 63.494  25.652  -1.642  1.00 75.38  ? 431 TYR A OH    1 
ATOM   3571 N  N     . ASP A 1 432 ? 58.715  27.931  3.330   1.00 66.34  ? 432 ASP A N     1 
ATOM   3572 C  CA    . ASP A 1 432 ? 58.840  26.898  4.348   1.00 60.93  ? 432 ASP A CA    1 
ATOM   3573 C  C     . ASP A 1 432 ? 58.295  25.591  3.789   1.00 56.36  ? 432 ASP A C     1 
ATOM   3574 O  O     . ASP A 1 432 ? 57.235  25.573  3.155   1.00 71.82  ? 432 ASP A O     1 
ATOM   3575 C  CB    . ASP A 1 432 ? 58.087  27.282  5.629   1.00 59.28  ? 432 ASP A CB    1 
ATOM   3576 C  CG    . ASP A 1 432 ? 58.889  28.209  6.524   1.00 67.31  ? 432 ASP A CG    1 
ATOM   3577 O  OD1   . ASP A 1 432 ? 59.990  28.632  6.113   1.00 81.93  ? 432 ASP A OD1   1 
ATOM   3578 O  OD2   . ASP A 1 432 ? 58.415  28.523  7.639   1.00 59.90  ? 432 ASP A OD2   1 
ATOM   3579 N  N     . VAL A 1 433 ? 59.019  24.500  4.020   1.00 57.39  ? 433 VAL A N     1 
ATOM   3580 C  CA    . VAL A 1 433 ? 58.672  23.195  3.467   1.00 57.45  ? 433 VAL A CA    1 
ATOM   3581 C  C     . VAL A 1 433 ? 58.055  22.340  4.564   1.00 73.09  ? 433 VAL A C     1 
ATOM   3582 O  O     . VAL A 1 433 ? 58.616  22.221  5.661   1.00 68.05  ? 433 VAL A O     1 
ATOM   3583 C  CB    . VAL A 1 433 ? 59.902  22.501  2.858   1.00 60.30  ? 433 VAL A CB    1 
ATOM   3584 C  CG1   . VAL A 1 433 ? 59.530  21.112  2.369   1.00 62.18  ? 433 VAL A CG1   1 
ATOM   3585 C  CG2   . VAL A 1 433 ? 60.465  23.330  1.726   1.00 66.74  ? 433 VAL A CG2   1 
ATOM   3586 N  N     . ALA A 1 434 ? 56.903  21.735  4.265   1.00 67.76  ? 434 ALA A N     1 
ATOM   3587 C  CA    . ALA A 1 434 ? 56.189  20.906  5.226   1.00 70.45  ? 434 ALA A CA    1 
ATOM   3588 C  C     . ALA A 1 434 ? 56.871  19.548  5.374   1.00 60.13  ? 434 ALA A C     1 
ATOM   3589 O  O     . ALA A 1 434 ? 57.305  18.958  4.381   1.00 61.25  ? 434 ALA A O     1 
ATOM   3590 C  CB    . ALA A 1 434 ? 54.739  20.711  4.792   1.00 64.00  ? 434 ALA A CB    1 
ATOM   3591 N  N     . PRO A 1 435 ? 56.983  19.035  6.597   1.00 62.34  ? 435 PRO A N     1 
ATOM   3592 C  CA    . PRO A 1 435 ? 57.545  17.694  6.781   1.00 61.72  ? 435 PRO A CA    1 
ATOM   3593 C  C     . PRO A 1 435 ? 56.652  16.634  6.156   1.00 79.72  ? 435 PRO A C     1 
ATOM   3594 O  O     . PRO A 1 435 ? 55.435  16.804  6.043   1.00 72.78  ? 435 PRO A O     1 
ATOM   3595 C  CB    . PRO A 1 435 ? 57.613  17.537  8.306   1.00 58.99  ? 435 PRO A CB    1 
ATOM   3596 C  CG    . PRO A 1 435 ? 56.710  18.595  8.857   1.00 59.87  ? 435 PRO A CG    1 
ATOM   3597 C  CD    . PRO A 1 435 ? 56.722  19.717  7.875   1.00 62.05  ? 435 PRO A CD    1 
ATOM   3598 N  N     . GLN A 1 436 ? 57.283  15.537  5.730   1.00 78.14  ? 436 GLN A N     1 
ATOM   3599 C  CA    . GLN A 1 436 ? 56.612  14.389  5.124   1.00 65.68  ? 436 GLN A CA    1 
ATOM   3600 C  C     . GLN A 1 436 ? 55.932  14.727  3.800   1.00 62.12  ? 436 GLN A C     1 
ATOM   3601 O  O     . GLN A 1 436 ? 56.167  14.051  2.792   1.00 67.72  ? 436 GLN A O     1 
ATOM   3602 C  CB    . GLN A 1 436 ? 55.583  13.783  6.085   1.00 67.32  ? 436 GLN A CB    1 
ATOM   3603 C  CG    . GLN A 1 436 ? 56.162  13.264  7.389   1.00 80.67  ? 436 GLN A CG    1 
ATOM   3604 C  CD    . GLN A 1 436 ? 55.118  12.583  8.251   1.00 84.47  ? 436 GLN A CD    1 
ATOM   3605 O  OE1   . GLN A 1 436 ? 54.172  11.983  7.740   1.00 76.63  ? 436 GLN A OE1   1 
ATOM   3606 N  NE2   . GLN A 1 436 ? 55.282  12.673  9.566   1.00 100.71 ? 436 GLN A NE2   1 
ATOM   3607 N  N     . VAL A 1 437 ? 55.078  15.756  3.785   1.00 61.24  ? 437 VAL A N     1 
ATOM   3608 C  CA    . VAL A 1 437 ? 54.284  16.052  2.594   1.00 63.34  ? 437 VAL A CA    1 
ATOM   3609 C  C     . VAL A 1 437 ? 54.963  17.036  1.650   1.00 75.66  ? 437 VAL A C     1 
ATOM   3610 O  O     . VAL A 1 437 ? 54.485  17.216  0.520   1.00 68.84  ? 437 VAL A O     1 
ATOM   3611 C  CB    . VAL A 1 437 ? 52.891  16.576  2.994   1.00 62.13  ? 437 VAL A CB    1 
ATOM   3612 C  CG1   . VAL A 1 437 ? 52.011  15.421  3.430   1.00 52.19  ? 437 VAL A CG1   1 
ATOM   3613 C  CG2   . VAL A 1 437 ? 53.012  17.600  4.108   1.00 61.24  ? 437 VAL A CG2   1 
ATOM   3614 N  N     . GLY A 1 438 ? 56.048  17.683  2.076   1.00 71.60  ? 438 GLY A N     1 
ATOM   3615 C  CA    . GLY A 1 438 ? 56.874  18.476  1.185   1.00 58.18  ? 438 GLY A CA    1 
ATOM   3616 C  C     . GLY A 1 438 ? 56.226  19.694  0.563   1.00 65.54  ? 438 GLY A C     1 
ATOM   3617 O  O     . GLY A 1 438 ? 56.789  20.253  -0.379  1.00 66.07  ? 438 GLY A O     1 
ATOM   3618 N  N     . HIS A 1 439 ? 55.069  20.132  1.058   1.00 67.53  ? 439 HIS A N     1 
ATOM   3619 C  CA    . HIS A 1 439 ? 54.421  21.306  0.489   1.00 66.11  ? 439 HIS A CA    1 
ATOM   3620 C  C     . HIS A 1 439 ? 55.177  22.570  0.880   1.00 66.31  ? 439 HIS A C     1 
ATOM   3621 O  O     . HIS A 1 439 ? 55.551  22.747  2.044   1.00 61.10  ? 439 HIS A O     1 
ATOM   3622 C  CB    . HIS A 1 439 ? 52.969  21.388  0.959   1.00 66.18  ? 439 HIS A CB    1 
ATOM   3623 C  CG    . HIS A 1 439 ? 52.136  20.215  0.548   1.00 63.60  ? 439 HIS A CG    1 
ATOM   3624 N  ND1   . HIS A 1 439 ? 51.964  19.850  -0.770  1.00 63.80  ? 439 HIS A ND1   1 
ATOM   3625 C  CD2   . HIS A 1 439 ? 51.434  19.319  1.282   1.00 56.57  ? 439 HIS A CD2   1 
ATOM   3626 C  CE1   . HIS A 1 439 ? 51.190  18.781  -0.830  1.00 63.78  ? 439 HIS A CE1   1 
ATOM   3627 N  NE2   . HIS A 1 439 ? 50.854  18.439  0.401   1.00 61.87  ? 439 HIS A NE2   1 
ATOM   3628 N  N     . ARG A 1 440 ? 55.397  23.450  -0.092  1.00 66.55  ? 440 ARG A N     1 
ATOM   3629 C  CA    . ARG A 1 440 ? 56.136  24.689  0.120   1.00 68.37  ? 440 ARG A CA    1 
ATOM   3630 C  C     . ARG A 1 440 ? 55.160  25.849  0.259   1.00 67.27  ? 440 ARG A C     1 
ATOM   3631 O  O     . ARG A 1 440 ? 54.219  25.972  -0.532  1.00 72.59  ? 440 ARG A O     1 
ATOM   3632 C  CB    . ARG A 1 440 ? 57.106  24.951  -1.033  1.00 66.71  ? 440 ARG A CB    1 
ATOM   3633 C  CG    . ARG A 1 440 ? 57.792  23.705  -1.552  1.00 68.19  ? 440 ARG A CG    1 
ATOM   3634 C  CD    . ARG A 1 440 ? 58.993  24.046  -2.411  1.00 71.49  ? 440 ARG A CD    1 
ATOM   3635 N  NE    . ARG A 1 440 ? 60.120  23.168  -2.122  1.00 92.80  ? 440 ARG A NE    1 
ATOM   3636 C  CZ    . ARG A 1 440 ? 61.098  22.899  -2.975  1.00 88.97  ? 440 ARG A CZ    1 
ATOM   3637 N  NH1   . ARG A 1 440 ? 61.125  23.429  -4.187  1.00 95.39  ? 440 ARG A NH1   1 
ATOM   3638 N  NH2   . ARG A 1 440 ? 62.075  22.078  -2.601  1.00 89.12  ? 440 ARG A NH2   1 
ATOM   3639 N  N     . PHE A 1 441 ? 55.389  26.699  1.257   1.00 59.73  ? 441 PHE A N     1 
ATOM   3640 C  CA    . PHE A 1 441 ? 54.506  27.822  1.544   1.00 62.76  ? 441 PHE A CA    1 
ATOM   3641 C  C     . PHE A 1 441 ? 55.304  29.116  1.527   1.00 70.25  ? 441 PHE A C     1 
ATOM   3642 O  O     . PHE A 1 441 ? 56.238  29.289  2.318   1.00 74.48  ? 441 PHE A O     1 
ATOM   3643 C  CB    . PHE A 1 441 ? 53.795  27.625  2.883   1.00 70.09  ? 441 PHE A CB    1 
ATOM   3644 C  CG    . PHE A 1 441 ? 52.794  26.509  2.865   1.00 61.76  ? 441 PHE A CG    1 
ATOM   3645 C  CD1   . PHE A 1 441 ? 51.550  26.690  2.282   1.00 60.03  ? 441 PHE A CD1   1 
ATOM   3646 C  CD2   . PHE A 1 441 ? 53.104  25.272  3.403   1.00 60.44  ? 441 PHE A CD2   1 
ATOM   3647 C  CE1   . PHE A 1 441 ? 50.627  25.663  2.252   1.00 67.50  ? 441 PHE A CE1   1 
ATOM   3648 C  CE2   . PHE A 1 441 ? 52.185  24.241  3.375   1.00 63.02  ? 441 PHE A CE2   1 
ATOM   3649 C  CZ    . PHE A 1 441 ? 50.945  24.437  2.798   1.00 69.95  ? 441 PHE A CZ    1 
ATOM   3650 N  N     . CYS A 1 442 ? 54.929  30.019  0.625   1.00 73.22  ? 442 CYS A N     1 
ATOM   3651 C  CA    . CYS A 1 442 ? 55.634  31.282  0.459   1.00 73.90  ? 442 CYS A CA    1 
ATOM   3652 C  C     . CYS A 1 442 ? 55.447  32.174  1.680   1.00 74.01  ? 442 CYS A C     1 
ATOM   3653 O  O     . CYS A 1 442 ? 54.331  32.330  2.185   1.00 69.69  ? 442 CYS A O     1 
ATOM   3654 C  CB    . CYS A 1 442 ? 55.130  31.990  -0.798  1.00 82.68  ? 442 CYS A CB    1 
ATOM   3655 S  SG    . CYS A 1 442 ? 55.883  33.593  -1.130  1.00 84.53  ? 442 CYS A SG    1 
ATOM   3656 N  N     . LYS A 1 443 ? 56.545  32.763  2.151   1.00 61.72  ? 443 LYS A N     1 
ATOM   3657 C  CA    . LYS A 1 443 ? 56.512  33.699  3.267   1.00 58.26  ? 443 LYS A CA    1 
ATOM   3658 C  C     . LYS A 1 443 ? 56.771  35.136  2.832   1.00 56.05  ? 443 LYS A C     1 
ATOM   3659 O  O     . LYS A 1 443 ? 56.987  36.001  3.686   1.00 77.92  ? 443 LYS A O     1 
ATOM   3660 C  CB    . LYS A 1 443 ? 57.524  33.287  4.337   1.00 56.18  ? 443 LYS A CB    1 
ATOM   3661 C  CG    . LYS A 1 443 ? 57.574  31.794  4.608   1.00 66.86  ? 443 LYS A CG    1 
ATOM   3662 C  CD    . LYS A 1 443 ? 58.341  31.501  5.885   1.00 77.41  ? 443 LYS A CD    1 
ATOM   3663 C  CE    . LYS A 1 443 ? 57.838  32.340  7.044   1.00 67.21  ? 443 LYS A CE    1 
ATOM   3664 N  NZ    . LYS A 1 443 ? 57.613  31.501  8.250   1.00 65.49  ? 443 LYS A NZ    1 
ATOM   3665 N  N     . ASP A 1 444 ? 56.756  35.412  1.525   1.00 63.74  ? 444 ASP A N     1 
ATOM   3666 C  CA    . ASP A 1 444 ? 56.986  36.775  1.057   1.00 66.36  ? 444 ASP A CA    1 
ATOM   3667 C  C     . ASP A 1 444 ? 55.846  37.697  1.468   1.00 73.04  ? 444 ASP A C     1 
ATOM   3668 O  O     . ASP A 1 444 ? 56.082  38.821  1.926   1.00 82.22  ? 444 ASP A O     1 
ATOM   3669 C  CB    . ASP A 1 444 ? 57.165  36.788  -0.461  1.00 69.03  ? 444 ASP A CB    1 
ATOM   3670 C  CG    . ASP A 1 444 ? 58.427  36.072  -0.908  1.00 79.87  ? 444 ASP A CG    1 
ATOM   3671 O  OD1   . ASP A 1 444 ? 59.367  35.950  -0.092  1.00 73.80  ? 444 ASP A OD1   1 
ATOM   3672 O  OD2   . ASP A 1 444 ? 58.479  35.629  -2.075  1.00 80.59  ? 444 ASP A OD2   1 
ATOM   3673 N  N     . LEU A 1 445 ? 54.606  37.240  1.315   1.00 79.53  ? 445 LEU A N     1 
ATOM   3674 C  CA    . LEU A 1 445 ? 53.445  38.009  1.712   1.00 78.02  ? 445 LEU A CA    1 
ATOM   3675 C  C     . LEU A 1 445 ? 52.606  37.218  2.706   1.00 69.25  ? 445 LEU A C     1 
ATOM   3676 O  O     . LEU A 1 445 ? 52.505  35.992  2.593   1.00 70.96  ? 445 LEU A O     1 
ATOM   3677 C  CB    . LEU A 1 445 ? 52.585  38.378  0.495   1.00 81.11  ? 445 LEU A CB    1 
ATOM   3678 C  CG    . LEU A 1 445 ? 53.067  39.594  -0.297  1.00 88.54  ? 445 LEU A CG    1 
ATOM   3679 C  CD1   . LEU A 1 445 ? 52.580  39.524  -1.735  1.00 95.24  ? 445 LEU A CD1   1 
ATOM   3680 C  CD2   . LEU A 1 445 ? 52.611  40.881  0.372   1.00 90.31  ? 445 LEU A CD2   1 
ATOM   3681 N  N     . PRO A 1 446 ? 52.003  37.883  3.690   1.00 70.76  ? 446 PRO A N     1 
ATOM   3682 C  CA    . PRO A 1 446 ? 51.157  37.164  4.649   1.00 66.36  ? 446 PRO A CA    1 
ATOM   3683 C  C     . PRO A 1 446 ? 49.950  36.552  3.955   1.00 60.60  ? 446 PRO A C     1 
ATOM   3684 O  O     . PRO A 1 446 ? 49.291  37.191  3.133   1.00 66.26  ? 446 PRO A O     1 
ATOM   3685 C  CB    . PRO A 1 446 ? 50.743  38.254  5.644   1.00 66.14  ? 446 PRO A CB    1 
ATOM   3686 C  CG    . PRO A 1 446 ? 50.881  39.532  4.883   1.00 75.88  ? 446 PRO A CG    1 
ATOM   3687 C  CD    . PRO A 1 446 ? 52.054  39.328  3.971   1.00 74.70  ? 446 PRO A CD    1 
ATOM   3688 N  N     . GLY A 1 447 ? 49.671  35.296  4.290   1.00 63.08  ? 447 GLY A N     1 
ATOM   3689 C  CA    . GLY A 1 447 ? 48.544  34.614  3.695   1.00 60.84  ? 447 GLY A CA    1 
ATOM   3690 C  C     . GLY A 1 447 ? 47.217  35.127  4.217   1.00 61.02  ? 447 GLY A C     1 
ATOM   3691 O  O     . GLY A 1 447 ? 47.131  35.798  5.247   1.00 50.63  ? 447 GLY A O     1 
ATOM   3692 N  N     . PHE A 1 448 ? 46.157  34.803  3.474   1.00 64.50  ? 448 PHE A N     1 
ATOM   3693 C  CA    . PHE A 1 448 ? 44.811  35.164  3.902   1.00 53.71  ? 448 PHE A CA    1 
ATOM   3694 C  C     . PHE A 1 448 ? 44.476  34.517  5.240   1.00 60.30  ? 448 PHE A C     1 
ATOM   3695 O  O     . PHE A 1 448 ? 44.184  35.205  6.224   1.00 49.85  ? 448 PHE A O     1 
ATOM   3696 C  CB    . PHE A 1 448 ? 43.794  34.757  2.835   1.00 57.25  ? 448 PHE A CB    1 
ATOM   3697 C  CG    . PHE A 1 448 ? 42.372  35.035  3.222   1.00 73.36  ? 448 PHE A CG    1 
ATOM   3698 C  CD1   . PHE A 1 448 ? 41.978  36.310  3.596   1.00 80.51  ? 448 PHE A CD1   1 
ATOM   3699 C  CD2   . PHE A 1 448 ? 41.429  34.021  3.222   1.00 66.84  ? 448 PHE A CD2   1 
ATOM   3700 C  CE1   . PHE A 1 448 ? 40.669  36.569  3.958   1.00 63.39  ? 448 PHE A CE1   1 
ATOM   3701 C  CE2   . PHE A 1 448 ? 40.119  34.273  3.582   1.00 65.07  ? 448 PHE A CE2   1 
ATOM   3702 C  CZ    . PHE A 1 448 ? 39.739  35.549  3.951   1.00 58.99  ? 448 PHE A CZ    1 
ATOM   3703 N  N     . ILE A 1 449 ? 44.531  33.183  5.294   1.00 56.40  ? 449 ILE A N     1 
ATOM   3704 C  CA    . ILE A 1 449 ? 44.198  32.475  6.532   1.00 51.81  ? 449 ILE A CA    1 
ATOM   3705 C  C     . ILE A 1 449 ? 45.119  32.849  7.686   1.00 56.08  ? 449 ILE A C     1 
ATOM   3706 O  O     . ILE A 1 449 ? 44.611  33.108  8.791   1.00 60.05  ? 449 ILE A O     1 
ATOM   3707 C  CB    . ILE A 1 449 ? 44.162  30.953  6.274   1.00 54.24  ? 449 ILE A CB    1 
ATOM   3708 C  CG1   . ILE A 1 449 ? 43.126  30.620  5.201   1.00 44.71  ? 449 ILE A CG1   1 
ATOM   3709 C  CG2   . ILE A 1 449 ? 43.868  30.199  7.560   1.00 39.96  ? 449 ILE A CG2   1 
ATOM   3710 C  CD1   . ILE A 1 449 ? 41.725  31.048  5.562   1.00 53.69  ? 449 ILE A CD1   1 
ATOM   3711 N  N     . PRO A 1 450 ? 46.449  32.889  7.528   1.00 52.31  ? 450 PRO A N     1 
ATOM   3712 C  CA    . PRO A 1 450 ? 47.293  33.280  8.670   1.00 47.16  ? 450 PRO A CA    1 
ATOM   3713 C  C     . PRO A 1 450 ? 46.995  34.671  9.201   1.00 47.57  ? 450 PRO A C     1 
ATOM   3714 O  O     . PRO A 1 450 ? 47.096  34.895  10.414  1.00 50.32  ? 450 PRO A O     1 
ATOM   3715 C  CB    . PRO A 1 450 ? 48.714  33.190  8.099   1.00 53.25  ? 450 PRO A CB    1 
ATOM   3716 C  CG    . PRO A 1 450 ? 48.612  32.207  7.003   1.00 54.31  ? 450 PRO A CG    1 
ATOM   3717 C  CD    . PRO A 1 450 ? 47.273  32.453  6.385   1.00 54.34  ? 450 PRO A CD    1 
ATOM   3718 N  N     . SER A 1 451 ? 46.626  35.615  8.333   1.00 51.87  ? 451 SER A N     1 
ATOM   3719 C  CA    . SER A 1 451 ? 46.358  36.972  8.798   1.00 57.64  ? 451 SER A CA    1 
ATOM   3720 C  C     . SER A 1 451 ? 45.117  37.036  9.680   1.00 60.12  ? 451 SER A C     1 
ATOM   3721 O  O     . SER A 1 451 ? 45.079  37.826  10.630  1.00 61.20  ? 451 SER A O     1 
ATOM   3722 C  CB    . SER A 1 451 ? 46.213  37.916  7.606   1.00 61.51  ? 451 SER A CB    1 
ATOM   3723 O  OG    . SER A 1 451 ? 44.981  37.703  6.942   1.00 82.99  ? 451 SER A OG    1 
ATOM   3724 N  N     . LEU A 1 452 ? 44.097  36.222  9.389   1.00 54.31  ? 452 LEU A N     1 
ATOM   3725 C  CA    . LEU A 1 452 ? 42.911  36.199  10.242  1.00 57.74  ? 452 LEU A CA    1 
ATOM   3726 C  C     . LEU A 1 452 ? 43.208  35.516  11.570  1.00 65.69  ? 452 LEU A C     1 
ATOM   3727 O  O     . LEU A 1 452 ? 42.887  36.049  12.639  1.00 77.87  ? 452 LEU A O     1 
ATOM   3728 C  CB    . LEU A 1 452 ? 41.755  35.489  9.538   1.00 45.18  ? 452 LEU A CB    1 
ATOM   3729 C  CG    . LEU A 1 452 ? 41.683  35.570  8.018   1.00 57.60  ? 452 LEU A CG    1 
ATOM   3730 C  CD1   . LEU A 1 452 ? 40.659  34.580  7.484   1.00 57.54  ? 452 LEU A CD1   1 
ATOM   3731 C  CD2   . LEU A 1 452 ? 41.379  36.984  7.552   1.00 72.09  ? 452 LEU A CD2   1 
ATOM   3732 N  N     . LEU A 1 453 ? 43.811  34.325  11.517  1.00 50.04  ? 453 LEU A N     1 
ATOM   3733 C  CA    . LEU A 1 453 ? 44.114  33.585  12.738  1.00 50.39  ? 453 LEU A CA    1 
ATOM   3734 C  C     . LEU A 1 453 ? 45.030  34.383  13.654  1.00 61.73  ? 453 LEU A C     1 
ATOM   3735 O  O     . LEU A 1 453 ? 44.884  34.339  14.882  1.00 66.20  ? 453 LEU A O     1 
ATOM   3736 C  CB    . LEU A 1 453 ? 44.747  32.238  12.390  1.00 53.73  ? 453 LEU A CB    1 
ATOM   3737 C  CG    . LEU A 1 453 ? 43.837  31.226  11.692  1.00 60.42  ? 453 LEU A CG    1 
ATOM   3738 C  CD1   . LEU A 1 453 ? 44.523  29.877  11.573  1.00 52.43  ? 453 LEU A CD1   1 
ATOM   3739 C  CD2   . LEU A 1 453 ? 42.520  31.093  12.438  1.00 58.55  ? 453 LEU A CD2   1 
ATOM   3740 N  N     . GLY A 1 454 ? 45.981  35.119  13.077  1.00 66.61  ? 454 GLY A N     1 
ATOM   3741 C  CA    . GLY A 1 454 ? 46.838  35.968  13.888  1.00 60.08  ? 454 GLY A CA    1 
ATOM   3742 C  C     . GLY A 1 454 ? 46.052  37.021  14.644  1.00 74.37  ? 454 GLY A C     1 
ATOM   3743 O  O     . GLY A 1 454 ? 46.272  37.241  15.837  1.00 69.79  ? 454 GLY A O     1 
ATOM   3744 N  N     . ASP A 1 455 ? 45.114  37.681  13.959  1.00 78.65  ? 455 ASP A N     1 
ATOM   3745 C  CA    . ASP A 1 455 ? 44.277  38.677  14.622  1.00 79.44  ? 455 ASP A CA    1 
ATOM   3746 C  C     . ASP A 1 455 ? 43.392  38.035  15.682  1.00 76.66  ? 455 ASP A C     1 
ATOM   3747 O  O     . ASP A 1 455 ? 43.140  38.632  16.736  1.00 82.52  ? 455 ASP A O     1 
ATOM   3748 C  CB    . ASP A 1 455 ? 43.423  39.416  13.592  1.00 72.23  ? 455 ASP A CB    1 
ATOM   3749 C  CG    . ASP A 1 455 ? 44.245  40.302  12.680  1.00 82.84  ? 455 ASP A CG    1 
ATOM   3750 O  OD1   . ASP A 1 455 ? 45.202  40.938  13.171  1.00 82.09  ? 455 ASP A OD1   1 
ATOM   3751 O  OD2   . ASP A 1 455 ? 43.932  40.365  11.472  1.00 82.68  ? 455 ASP A OD2   1 
ATOM   3752 N  N     . LEU A 1 456 ? 42.911  36.816  15.422  1.00 69.75  ? 456 LEU A N     1 
ATOM   3753 C  CA    . LEU A 1 456 ? 42.038  36.141  16.377  1.00 64.74  ? 456 LEU A CA    1 
ATOM   3754 C  C     . LEU A 1 456 ? 42.798  35.750  17.638  1.00 75.60  ? 456 LEU A C     1 
ATOM   3755 O  O     . LEU A 1 456 ? 42.385  36.086  18.754  1.00 85.46  ? 456 LEU A O     1 
ATOM   3756 C  CB    . LEU A 1 456 ? 41.403  34.911  15.729  1.00 62.13  ? 456 LEU A CB    1 
ATOM   3757 C  CG    . LEU A 1 456 ? 40.202  35.146  14.814  1.00 63.38  ? 456 LEU A CG    1 
ATOM   3758 C  CD1   . LEU A 1 456 ? 39.738  33.831  14.212  1.00 55.99  ? 456 LEU A CD1   1 
ATOM   3759 C  CD2   . LEU A 1 456 ? 39.072  35.820  15.575  1.00 71.86  ? 456 LEU A CD2   1 
ATOM   3760 N  N     . LEU A 1 457 ? 43.915  35.033  17.479  1.00 79.43  ? 457 LEU A N     1 
ATOM   3761 C  CA    . LEU A 1 457 ? 44.694  34.613  18.640  1.00 80.13  ? 457 LEU A CA    1 
ATOM   3762 C  C     . LEU A 1 457 ? 45.289  35.804  19.380  1.00 80.41  ? 457 LEU A C     1 
ATOM   3763 O  O     . LEU A 1 457 ? 45.463  35.745  20.603  1.00 75.83  ? 457 LEU A O     1 
ATOM   3764 C  CB    . LEU A 1 457 ? 45.797  33.644  18.213  1.00 72.16  ? 457 LEU A CB    1 
ATOM   3765 C  CG    . LEU A 1 457 ? 45.335  32.229  17.856  1.00 74.58  ? 457 LEU A CG    1 
ATOM   3766 C  CD1   . LEU A 1 457 ? 46.502  31.394  17.357  1.00 65.24  ? 457 LEU A CD1   1 
ATOM   3767 C  CD2   . LEU A 1 457 ? 44.661  31.560  19.046  1.00 73.81  ? 457 LEU A CD2   1 
ATOM   3768 N  N     . GLU A 1 458 ? 45.608  36.885  18.665  1.00 78.38  ? 458 GLU A N     1 
ATOM   3769 C  CA    . GLU A 1 458 ? 46.027  38.110  19.338  1.00 77.66  ? 458 GLU A CA    1 
ATOM   3770 C  C     . GLU A 1 458 ? 44.892  38.682  20.177  1.00 83.75  ? 458 GLU A C     1 
ATOM   3771 O  O     . GLU A 1 458 ? 45.108  39.122  21.313  1.00 83.44  ? 458 GLU A O     1 
ATOM   3772 C  CB    . GLU A 1 458 ? 46.512  39.135  18.311  1.00 83.48  ? 458 GLU A CB    1 
ATOM   3773 C  CG    . GLU A 1 458 ? 46.258  40.586  18.693  1.00 101.36 ? 458 GLU A CG    1 
ATOM   3774 C  CD    . GLU A 1 458 ? 46.846  41.565  17.693  1.00 106.12 ? 458 GLU A CD    1 
ATOM   3775 O  OE1   . GLU A 1 458 ? 47.353  42.623  18.123  1.00 105.77 ? 458 GLU A OE1   1 
ATOM   3776 O  OE2   . GLU A 1 458 ? 46.798  41.279  16.478  1.00 106.12 ? 458 GLU A OE2   1 
ATOM   3777 N  N     . GLU A 1 459 ? 43.669  38.676  19.637  1.00 98.87  ? 459 GLU A N     1 
ATOM   3778 C  CA    . GLU A 1 459 ? 42.523  39.144  20.409  1.00 103.63 ? 459 GLU A CA    1 
ATOM   3779 C  C     . GLU A 1 459 ? 42.167  38.179  21.530  1.00 93.88  ? 459 GLU A C     1 
ATOM   3780 O  O     . GLU A 1 459 ? 41.698  38.611  22.589  1.00 104.07 ? 459 GLU A O     1 
ATOM   3781 C  CB    . GLU A 1 459 ? 41.313  39.357  19.499  1.00 96.17  ? 459 GLU A CB    1 
ATOM   3782 C  CG    . GLU A 1 459 ? 40.200  40.153  20.160  1.00 100.05 ? 459 GLU A CG    1 
ATOM   3783 C  CD    . GLU A 1 459 ? 39.198  40.703  19.168  1.00 120.75 ? 459 GLU A CD    1 
ATOM   3784 O  OE1   . GLU A 1 459 ? 39.158  40.208  18.022  1.00 127.50 ? 459 GLU A OE1   1 
ATOM   3785 O  OE2   . GLU A 1 459 ? 38.447  41.630  19.538  1.00 136.98 ? 459 GLU A OE2   1 
ATOM   3786 N  N     . ARG A 1 460 ? 42.367  36.876  21.317  1.00 72.33  ? 460 ARG A N     1 
ATOM   3787 C  CA    . ARG A 1 460 ? 42.137  35.915  22.390  1.00 85.48  ? 460 ARG A CA    1 
ATOM   3788 C  C     . ARG A 1 460 ? 43.040  36.213  23.578  1.00 104.17 ? 460 ARG A C     1 
ATOM   3789 O  O     . ARG A 1 460 ? 42.567  36.360  24.710  1.00 107.04 ? 460 ARG A O     1 
ATOM   3790 C  CB    . ARG A 1 460 ? 42.360  34.488  21.883  1.00 88.56  ? 460 ARG A CB    1 
ATOM   3791 C  CG    . ARG A 1 460 ? 41.693  33.415  22.743  1.00 92.13  ? 460 ARG A CG    1 
ATOM   3792 C  CD    . ARG A 1 460 ? 42.542  32.154  22.853  1.00 91.32  ? 460 ARG A CD    1 
ATOM   3793 N  NE    . ARG A 1 460 ? 41.987  31.200  23.808  1.00 95.20  ? 460 ARG A NE    1 
ATOM   3794 C  CZ    . ARG A 1 460 ? 42.137  29.884  23.726  1.00 97.70  ? 460 ARG A CZ    1 
ATOM   3795 N  NH1   . ARG A 1 460 ? 42.817  29.326  22.738  1.00 88.47  ? 460 ARG A NH1   1 
ATOM   3796 N  NH2   . ARG A 1 460 ? 41.591  29.109  24.659  1.00 99.68  ? 460 ARG A NH2   1 
ATOM   3797 N  N     . GLN A 1 461 ? 44.347  36.342  23.330  1.00 112.57 ? 461 GLN A N     1 
ATOM   3798 C  CA    . GLN A 1 461 ? 45.289  36.592  24.415  1.00 105.71 ? 461 GLN A CA    1 
ATOM   3799 C  C     . GLN A 1 461 ? 45.085  37.969  25.038  1.00 97.06  ? 461 GLN A C     1 
ATOM   3800 O  O     . GLN A 1 461 ? 45.423  38.170  26.210  1.00 104.35 ? 461 GLN A O     1 
ATOM   3801 C  CB    . GLN A 1 461 ? 46.722  36.439  23.911  1.00 106.01 ? 461 GLN A CB    1 
ATOM   3802 C  CG    . GLN A 1 461 ? 47.231  35.005  23.947  1.00 120.44 ? 461 GLN A CG    1 
ATOM   3803 C  CD    . GLN A 1 461 ? 47.862  34.640  25.277  1.00 146.59 ? 461 GLN A CD    1 
ATOM   3804 O  OE1   . GLN A 1 461 ? 47.506  35.191  26.319  1.00 143.50 ? 461 GLN A OE1   1 
ATOM   3805 N  NE2   . GLN A 1 461 ? 48.799  33.699  25.249  1.00 130.29 ? 461 GLN A NE2   1 
ATOM   3806 N  N     . LYS A 1 462 ? 44.547  38.925  24.277  1.00 98.70  ? 462 LYS A N     1 
ATOM   3807 C  CA    . LYS A 1 462 ? 44.153  40.199  24.871  1.00 102.55 ? 462 LYS A CA    1 
ATOM   3808 C  C     . LYS A 1 462 ? 43.024  40.007  25.873  1.00 112.81 ? 462 LYS A C     1 
ATOM   3809 O  O     . LYS A 1 462 ? 42.979  40.684  26.907  1.00 114.68 ? 462 LYS A O     1 
ATOM   3810 C  CB    . LYS A 1 462 ? 43.730  41.187  23.783  1.00 109.90 ? 462 LYS A CB    1 
ATOM   3811 C  CG    . LYS A 1 462 ? 43.986  42.649  24.122  1.00 109.28 ? 462 LYS A CG    1 
ATOM   3812 C  CD    . LYS A 1 462 ? 43.288  43.563  23.126  1.00 123.83 ? 462 LYS A CD    1 
ATOM   3813 C  CE    . LYS A 1 462 ? 41.780  43.566  23.346  1.00 121.48 ? 462 LYS A CE    1 
ATOM   3814 N  NZ    . LYS A 1 462 ? 41.043  44.196  22.214  1.00 108.23 ? 462 LYS A NZ    1 
ATOM   3815 N  N     . ILE A 1 463 ? 42.104  39.085  25.585  1.00 102.36 ? 463 ILE A N     1 
ATOM   3816 C  CA    . ILE A 1 463 ? 40.946  38.885  26.452  1.00 106.23 ? 463 ILE A CA    1 
ATOM   3817 C  C     . ILE A 1 463 ? 41.343  38.125  27.714  1.00 114.43 ? 463 ILE A C     1 
ATOM   3818 O  O     . ILE A 1 463 ? 40.941  38.497  28.821  1.00 127.10 ? 463 ILE A O     1 
ATOM   3819 C  CB    . ILE A 1 463 ? 39.820  38.173  25.679  1.00 115.44 ? 463 ILE A CB    1 
ATOM   3820 C  CG1   . ILE A 1 463 ? 38.822  39.181  25.099  1.00 112.87 ? 463 ILE A CG1   1 
ATOM   3821 C  CG2   . ILE A 1 463 ? 39.075  37.212  26.583  1.00 107.53 ? 463 ILE A CG2   1 
ATOM   3822 C  CD1   . ILE A 1 463 ? 39.451  40.321  24.322  1.00 104.56 ? 463 ILE A CD1   1 
ATOM   3823 N  N     . LYS A 1 464 ? 42.149  37.066  27.577  1.00 109.54 ? 464 LYS A N     1 
ATOM   3824 C  CA    . LYS A 1 464 ? 42.637  36.328  28.739  1.00 109.82 ? 464 LYS A CA    1 
ATOM   3825 C  C     . LYS A 1 464 ? 43.403  37.212  29.715  1.00 114.99 ? 464 LYS A C     1 
ATOM   3826 O  O     . LYS A 1 464 ? 43.628  36.793  30.857  1.00 115.89 ? 464 LYS A O     1 
ATOM   3827 C  CB    . LYS A 1 464 ? 43.530  35.165  28.295  1.00 103.36 ? 464 LYS A CB    1 
ATOM   3828 C  CG    . LYS A 1 464 ? 43.078  34.492  27.010  1.00 97.85  ? 464 LYS A CG    1 
ATOM   3829 C  CD    . LYS A 1 464 ? 43.544  33.048  26.891  1.00 101.28 ? 464 LYS A CD    1 
ATOM   3830 C  CE    . LYS A 1 464 ? 43.307  32.263  28.168  1.00 95.27  ? 464 LYS A CE    1 
ATOM   3831 N  NZ    . LYS A 1 464 ? 44.021  30.954  28.150  1.00 80.55  ? 464 LYS A NZ    1 
ATOM   3832 N  N     . LYS A 1 465 ? 43.809  38.411  29.294  1.00 112.35 ? 465 LYS A N     1 
ATOM   3833 C  CA    . LYS A 1 465 ? 44.514  39.359  30.149  1.00 121.30 ? 465 LYS A CA    1 
ATOM   3834 C  C     . LYS A 1 465 ? 43.572  40.390  30.766  1.00 126.38 ? 465 LYS A C     1 
ATOM   3835 O  O     . LYS A 1 465 ? 43.472  40.473  31.993  1.00 136.91 ? 465 LYS A O     1 
ATOM   3836 C  CB    . LYS A 1 465 ? 45.629  40.057  29.351  1.00 124.17 ? 465 LYS A CB    1 
ATOM   3837 C  CG    . LYS A 1 465 ? 45.933  41.475  29.817  1.00 132.68 ? 465 LYS A CG    1 
ATOM   3838 C  CD    . LYS A 1 465 ? 47.217  42.012  29.225  1.00 128.73 ? 465 LYS A CD    1 
ATOM   3839 C  CE    . LYS A 1 465 ? 47.946  42.846  30.258  1.00 122.37 ? 465 LYS A CE    1 
ATOM   3840 N  NZ    . LYS A 1 465 ? 47.617  44.287  30.126  1.00 122.23 ? 465 LYS A NZ    1 
ATOM   3841 N  N     . LYS A 1 466 ? 42.874  41.178  29.933  1.00 126.83 ? 466 LYS A N     1 
ATOM   3842 C  CA    . LYS A 1 466 ? 42.028  42.250  30.459  1.00 126.06 ? 466 LYS A CA    1 
ATOM   3843 C  C     . LYS A 1 466 ? 40.989  41.710  31.430  1.00 135.62 ? 466 LYS A C     1 
ATOM   3844 O  O     . LYS A 1 466 ? 40.561  42.424  32.346  1.00 144.09 ? 466 LYS A O     1 
ATOM   3845 C  CB    . LYS A 1 466 ? 41.345  43.001  29.313  1.00 118.14 ? 466 LYS A CB    1 
ATOM   3846 C  CG    . LYS A 1 466 ? 40.300  44.018  29.768  1.00 116.24 ? 466 LYS A CG    1 
ATOM   3847 C  CD    . LYS A 1 466 ? 39.403  44.482  28.632  1.00 110.19 ? 466 LYS A CD    1 
ATOM   3848 C  CE    . LYS A 1 466 ? 40.192  44.761  27.366  1.00 104.46 ? 466 LYS A CE    1 
ATOM   3849 N  NZ    . LYS A 1 466 ? 39.331  45.362  26.310  1.00 88.47  ? 466 LYS A NZ    1 
ATOM   3850 N  N     . MET A 1 467 ? 40.586  40.451  31.249  1.00 131.14 ? 467 MET A N     1 
ATOM   3851 C  CA    . MET A 1 467 ? 39.736  39.727  32.187  1.00 138.29 ? 467 MET A CA    1 
ATOM   3852 C  C     . MET A 1 467 ? 40.218  39.909  33.622  1.00 143.28 ? 467 MET A C     1 
ATOM   3853 O  O     . MET A 1 467 ? 39.410  40.116  34.533  1.00 146.79 ? 467 MET A O     1 
ATOM   3854 C  CB    . MET A 1 467 ? 39.696  38.242  31.806  1.00 134.10 ? 467 MET A CB    1 
ATOM   3855 C  CG    . MET A 1 467 ? 38.384  37.530  32.126  1.00 137.04 ? 467 MET A CG    1 
ATOM   3856 S  SD    . MET A 1 467 ? 38.128  37.317  33.900  1.00 201.18 ? 467 MET A SD    1 
ATOM   3857 C  CE    . MET A 1 467 ? 38.533  35.588  34.111  1.00 142.99 ? 467 MET A CE    1 
ATOM   3858 N  N     . LYS A 1 468 ? 41.535  39.866  33.831  1.00 143.00 ? 468 LYS A N     1 
ATOM   3859 C  CA    . LYS A 1 468 ? 42.065  39.939  35.189  1.00 140.90 ? 468 LYS A CA    1 
ATOM   3860 C  C     . LYS A 1 468 ? 41.846  41.319  35.797  1.00 135.40 ? 468 LYS A C     1 
ATOM   3861 O  O     . LYS A 1 468 ? 41.619  41.441  37.006  1.00 131.08 ? 468 LYS A O     1 
ATOM   3862 C  CB    . LYS A 1 468 ? 43.551  39.577  35.188  1.00 129.65 ? 468 LYS A CB    1 
ATOM   3863 C  CG    . LYS A 1 468 ? 43.916  38.130  34.777  1.00 130.37 ? 468 LYS A CG    1 
ATOM   3864 C  CD    . LYS A 1 468 ? 42.778  37.097  34.852  1.00 139.11 ? 468 LYS A CD    1 
ATOM   3865 C  CE    . LYS A 1 468 ? 42.266  36.851  36.272  1.00 135.63 ? 468 LYS A CE    1 
ATOM   3866 N  NZ    . LYS A 1 468 ? 40.839  36.424  36.264  1.00 136.94 ? 468 LYS A NZ    1 
ATOM   3867 N  N     . ALA A 1 469 ? 41.902  42.371  34.974  1.00 133.55 ? 469 ALA A N     1 
ATOM   3868 C  CA    . ALA A 1 469 ? 41.658  43.717  35.485  1.00 138.77 ? 469 ALA A CA    1 
ATOM   3869 C  C     . ALA A 1 469 ? 40.194  43.910  35.856  1.00 152.53 ? 469 ALA A C     1 
ATOM   3870 O  O     . ALA A 1 469 ? 39.887  44.514  36.887  1.00 149.97 ? 469 ALA A O     1 
ATOM   3871 C  CB    . ALA A 1 469 ? 42.087  44.758  34.453  1.00 134.54 ? 469 ALA A CB    1 
ATOM   3872 N  N     . THR A 1 470 ? 39.281  43.405  35.025  1.00 161.86 ? 470 THR A N     1 
ATOM   3873 C  CA    . THR A 1 470 ? 37.852  43.577  35.263  1.00 149.21 ? 470 THR A CA    1 
ATOM   3874 C  C     . THR A 1 470 ? 37.432  42.879  36.554  1.00 167.54 ? 470 THR A C     1 
ATOM   3875 O  O     . THR A 1 470 ? 38.000  41.856  36.950  1.00 151.80 ? 470 THR A O     1 
ATOM   3876 C  CB    . THR A 1 470 ? 37.038  43.034  34.081  1.00 145.45 ? 470 THR A CB    1 
ATOM   3877 O  OG1   . THR A 1 470 ? 37.063  41.602  34.084  1.00 147.26 ? 470 THR A OG1   1 
ATOM   3878 C  CG2   . THR A 1 470 ? 37.596  43.548  32.754  1.00 137.41 ? 470 THR A CG2   1 
ATOM   3879 N  N     . ILE A 1 471 ? 36.419  43.447  37.215  1.00 146.39 ? 471 ILE A N     1 
ATOM   3880 C  CA    . ILE A 1 471 ? 35.945  42.971  38.510  1.00 136.56 ? 471 ILE A CA    1 
ATOM   3881 C  C     . ILE A 1 471 ? 34.517  42.444  38.424  1.00 138.03 ? 471 ILE A C     1 
ATOM   3882 O  O     . ILE A 1 471 ? 34.195  41.398  38.998  1.00 131.18 ? 471 ILE A O     1 
ATOM   3883 C  CB    . ILE A 1 471 ? 36.059  44.068  39.589  1.00 121.09 ? 471 ILE A CB    1 
ATOM   3884 C  CG1   . ILE A 1 471 ? 37.472  44.649  39.605  1.00 117.54 ? 471 ILE A CG1   1 
ATOM   3885 C  CG2   . ILE A 1 471 ? 35.678  43.515  40.959  1.00 115.88 ? 471 ILE A CG2   1 
ATOM   3886 C  CD1   . ILE A 1 471 ? 37.731  45.594  40.755  1.00 104.93 ? 471 ILE A CD1   1 
ATOM   3887 N  N     . ASP A 1 472 ? 33.639  43.168  37.727  1.00 141.64 ? 472 ASP A N     1 
ATOM   3888 C  CA    . ASP A 1 472 ? 32.255  42.750  37.556  1.00 139.19 ? 472 ASP A CA    1 
ATOM   3889 C  C     . ASP A 1 472 ? 32.218  41.310  37.047  1.00 141.03 ? 472 ASP A C     1 
ATOM   3890 O  O     . ASP A 1 472 ? 32.765  41.028  35.970  1.00 144.05 ? 472 ASP A O     1 
ATOM   3891 C  CB    . ASP A 1 472 ? 31.524  43.676  36.582  1.00 132.37 ? 472 ASP A CB    1 
ATOM   3892 C  CG    . ASP A 1 472 ? 30.008  43.492  36.613  1.00 131.21 ? 472 ASP A CG    1 
ATOM   3893 O  OD1   . ASP A 1 472 ? 29.537  42.382  36.931  1.00 135.85 ? 472 ASP A OD1   1 
ATOM   3894 O  OD2   . ASP A 1 472 ? 29.282  44.463  36.306  1.00 132.54 ? 472 ASP A OD2   1 
ATOM   3895 N  N     . PRO A 1 473 ? 31.617  40.379  37.793  1.00 135.89 ? 473 PRO A N     1 
ATOM   3896 C  CA    . PRO A 1 473 ? 31.621  38.974  37.354  1.00 138.03 ? 473 PRO A CA    1 
ATOM   3897 C  C     . PRO A 1 473 ? 31.039  38.768  35.969  1.00 142.22 ? 473 PRO A C     1 
ATOM   3898 O  O     . PRO A 1 473 ? 31.461  37.841  35.266  1.00 140.13 ? 473 PRO A O     1 
ATOM   3899 C  CB    . PRO A 1 473 ? 30.782  38.266  38.429  1.00 137.37 ? 473 PRO A CB    1 
ATOM   3900 C  CG    . PRO A 1 473 ? 30.037  39.364  39.138  1.00 135.25 ? 473 PRO A CG    1 
ATOM   3901 C  CD    . PRO A 1 473 ? 30.940  40.549  39.088  1.00 127.22 ? 473 PRO A CD    1 
ATOM   3902 N  N     . ILE A 1 474 ? 30.089  39.608  35.550  1.00 150.96 ? 474 ILE A N     1 
ATOM   3903 C  CA    . ILE A 1 474 ? 29.480  39.435  34.233  1.00 150.53 ? 474 ILE A CA    1 
ATOM   3904 C  C     . ILE A 1 474 ? 30.512  39.683  33.136  1.00 147.04 ? 474 ILE A C     1 
ATOM   3905 O  O     . ILE A 1 474 ? 30.663  38.873  32.215  1.00 142.47 ? 474 ILE A O     1 
ATOM   3906 C  CB    . ILE A 1 474 ? 28.230  40.329  34.083  1.00 140.35 ? 474 ILE A CB    1 
ATOM   3907 C  CG1   . ILE A 1 474 ? 28.583  41.813  33.926  1.00 140.66 ? 474 ILE A CG1   1 
ATOM   3908 C  CG2   . ILE A 1 474 ? 27.294  40.139  35.274  1.00 125.09 ? 474 ILE A CG2   1 
ATOM   3909 C  CD1   . ILE A 1 474 ? 27.385  42.734  33.807  1.00 129.04 ? 474 ILE A CD1   1 
ATOM   3910 N  N     . GLU A 1 475 ? 31.274  40.778  33.244  1.00 140.14 ? 475 GLU A N     1 
ATOM   3911 C  CA    . GLU A 1 475 ? 32.273  41.085  32.223  1.00 137.02 ? 475 GLU A CA    1 
ATOM   3912 C  C     . GLU A 1 475 ? 33.327  39.991  32.152  1.00 136.52 ? 475 GLU A C     1 
ATOM   3913 O  O     . GLU A 1 475 ? 33.788  39.631  31.064  1.00 135.57 ? 475 GLU A O     1 
ATOM   3914 C  CB    . GLU A 1 475 ? 32.920  42.441  32.505  1.00 131.20 ? 475 GLU A CB    1 
ATOM   3915 C  CG    . GLU A 1 475 ? 33.629  43.050  31.302  1.00 129.84 ? 475 GLU A CG    1 
ATOM   3916 C  CD    . GLU A 1 475 ? 32.739  43.114  30.072  1.00 133.14 ? 475 GLU A CD    1 
ATOM   3917 O  OE1   . GLU A 1 475 ? 31.551  43.470  30.216  1.00 139.31 ? 475 GLU A OE1   1 
ATOM   3918 O  OE2   . GLU A 1 475 ? 33.222  42.800  28.964  1.00 129.07 ? 475 GLU A OE2   1 
ATOM   3919 N  N     . ARG A 1 476 ? 33.716  39.449  33.308  1.00 135.78 ? 476 ARG A N     1 
ATOM   3920 C  CA    . ARG A 1 476 ? 34.590  38.281  33.335  1.00 139.17 ? 476 ARG A CA    1 
ATOM   3921 C  C     . ARG A 1 476 ? 34.011  37.147  32.502  1.00 139.42 ? 476 ARG A C     1 
ATOM   3922 O  O     . ARG A 1 476 ? 34.689  36.586  31.635  1.00 142.43 ? 476 ARG A O     1 
ATOM   3923 C  CB    . ARG A 1 476 ? 34.798  37.821  34.776  1.00 144.49 ? 476 ARG A CB    1 
ATOM   3924 C  CG    . ARG A 1 476 ? 35.472  38.842  35.662  1.00 149.90 ? 476 ARG A CG    1 
ATOM   3925 C  CD    . ARG A 1 476 ? 35.572  38.330  37.083  1.00 156.15 ? 476 ARG A CD    1 
ATOM   3926 N  NE    . ARG A 1 476 ? 36.425  37.152  37.165  1.00 169.88 ? 476 ARG A NE    1 
ATOM   3927 C  CZ    . ARG A 1 476 ? 36.603  36.431  38.263  1.00 159.66 ? 476 ARG A CZ    1 
ATOM   3928 N  NH1   . ARG A 1 476 ? 36.001  36.741  39.399  1.00 139.18 ? 476 ARG A NH1   1 
ATOM   3929 N  NH2   . ARG A 1 476 ? 37.409  35.374  38.219  1.00 160.61 ? 476 ARG A NH2   1 
ATOM   3930 N  N     . LYS A 1 477 ? 32.751  36.793  32.756  1.00 141.38 ? 477 LYS A N     1 
ATOM   3931 C  CA    . LYS A 1 477 ? 32.123  35.727  31.987  1.00 135.09 ? 477 LYS A CA    1 
ATOM   3932 C  C     . LYS A 1 477 ? 31.988  36.120  30.518  1.00 133.57 ? 477 LYS A C     1 
ATOM   3933 O  O     . LYS A 1 477 ? 32.436  35.386  29.630  1.00 132.04 ? 477 LYS A O     1 
ATOM   3934 C  CB    . LYS A 1 477 ? 30.767  35.380  32.603  1.00 135.83 ? 477 LYS A CB    1 
ATOM   3935 C  CG    . LYS A 1 477 ? 30.720  33.993  33.241  1.00 137.58 ? 477 LYS A CG    1 
ATOM   3936 C  CD    . LYS A 1 477 ? 29.584  33.876  34.245  1.00 128.84 ? 477 LYS A CD    1 
ATOM   3937 C  CE    . LYS A 1 477 ? 29.911  32.869  35.335  1.00 122.08 ? 477 LYS A CE    1 
ATOM   3938 N  NZ    . LYS A 1 477 ? 28.701  32.515  36.122  1.00 111.93 ? 477 LYS A NZ    1 
ATOM   3939 N  N     . LEU A 1 478 ? 31.405  37.295  30.245  1.00 133.62 ? 478 LEU A N     1 
ATOM   3940 C  CA    . LEU A 1 478 ? 31.244  37.754  28.864  1.00 133.09 ? 478 LEU A CA    1 
ATOM   3941 C  C     . LEU A 1 478 ? 32.564  37.716  28.099  1.00 133.17 ? 478 LEU A C     1 
ATOM   3942 O  O     . LEU A 1 478 ? 32.626  37.209  26.972  1.00 129.34 ? 478 LEU A O     1 
ATOM   3943 C  CB    . LEU A 1 478 ? 30.651  39.165  28.829  1.00 131.45 ? 478 LEU A CB    1 
ATOM   3944 C  CG    . LEU A 1 478 ? 29.341  39.479  29.560  1.00 133.55 ? 478 LEU A CG    1 
ATOM   3945 C  CD1   . LEU A 1 478 ? 29.236  40.975  29.840  1.00 126.83 ? 478 LEU A CD1   1 
ATOM   3946 C  CD2   . LEU A 1 478 ? 28.127  38.983  28.780  1.00 117.53 ? 478 LEU A CD2   1 
ATOM   3947 N  N     . LEU A 1 479 ? 33.629  38.256  28.694  1.00 136.49 ? 479 LEU A N     1 
ATOM   3948 C  CA    . LEU A 1 479 ? 34.931  38.252  28.035  1.00 128.04 ? 479 LEU A CA    1 
ATOM   3949 C  C     . LEU A 1 479 ? 35.471  36.835  27.892  1.00 125.89 ? 479 LEU A C     1 
ATOM   3950 O  O     . LEU A 1 479 ? 35.984  36.460  26.831  1.00 120.49 ? 479 LEU A O     1 
ATOM   3951 C  CB    . LEU A 1 479 ? 35.911  39.128  28.818  1.00 117.63 ? 479 LEU A CB    1 
ATOM   3952 C  CG    . LEU A 1 479 ? 35.654  40.634  28.732  1.00 121.24 ? 479 LEU A CG    1 
ATOM   3953 C  CD1   . LEU A 1 479 ? 36.760  41.411  29.427  1.00 121.90 ? 479 LEU A CD1   1 
ATOM   3954 C  CD2   . LEU A 1 479 ? 35.498  41.082  27.284  1.00 120.79 ? 479 LEU A CD2   1 
ATOM   3955 N  N     . ASP A 1 480 ? 35.359  36.029  28.953  1.00 124.97 ? 480 ASP A N     1 
ATOM   3956 C  CA    . ASP A 1 480 ? 35.814  34.644  28.883  1.00 121.29 ? 480 ASP A CA    1 
ATOM   3957 C  C     . ASP A 1 480 ? 35.129  33.890  27.745  1.00 128.98 ? 480 ASP A C     1 
ATOM   3958 O  O     . ASP A 1 480 ? 35.749  33.031  27.108  1.00 130.99 ? 480 ASP A O     1 
ATOM   3959 C  CB    . ASP A 1 480 ? 35.571  33.937  30.220  1.00 119.34 ? 480 ASP A CB    1 
ATOM   3960 C  CG    . ASP A 1 480 ? 35.999  32.478  30.196  1.00 129.49 ? 480 ASP A CG    1 
ATOM   3961 O  OD1   . ASP A 1 480 ? 37.200  32.198  30.396  1.00 123.63 ? 480 ASP A OD1   1 
ATOM   3962 O  OD2   . ASP A 1 480 ? 35.132  31.612  29.961  1.00 131.22 ? 480 ASP A OD2   1 
ATOM   3963 N  N     . TYR A 1 481 ? 33.857  34.207  27.464  1.00 133.59 ? 481 TYR A N     1 
ATOM   3964 C  CA    . TYR A 1 481 ? 33.156  33.553  26.359  1.00 141.27 ? 481 TYR A CA    1 
ATOM   3965 C  C     . TYR A 1 481 ? 33.882  33.792  25.043  1.00 124.32 ? 481 TYR A C     1 
ATOM   3966 O  O     . TYR A 1 481 ? 34.150  32.852  24.285  1.00 113.93 ? 481 TYR A O     1 
ATOM   3967 C  CB    . TYR A 1 481 ? 31.709  34.050  26.243  1.00 130.19 ? 481 TYR A CB    1 
ATOM   3968 C  CG    . TYR A 1 481 ? 30.851  33.821  27.467  1.00 148.07 ? 481 TYR A CG    1 
ATOM   3969 C  CD1   . TYR A 1 481 ? 30.854  32.593  28.126  1.00 154.94 ? 481 TYR A CD1   1 
ATOM   3970 C  CD2   . TYR A 1 481 ? 29.990  34.812  27.929  1.00 132.88 ? 481 TYR A CD2   1 
ATOM   3971 C  CE1   . TYR A 1 481 ? 30.068  32.381  29.249  1.00 152.97 ? 481 TYR A CE1   1 
ATOM   3972 C  CE2   . TYR A 1 481 ? 29.192  34.611  29.041  1.00 132.33 ? 481 TYR A CE2   1 
ATOM   3973 C  CZ    . TYR A 1 481 ? 29.233  33.392  29.698  1.00 142.12 ? 481 TYR A CZ    1 
ATOM   3974 O  OH    . TYR A 1 481 ? 28.439  33.193  30.805  1.00 137.15 ? 481 TYR A OH    1 
ATOM   3975 N  N     . ARG A 1 482 ? 34.210  35.053  24.754  1.00 112.38 ? 482 ARG A N     1 
ATOM   3976 C  CA    . ARG A 1 482 ? 34.920  35.364  23.517  1.00 105.85 ? 482 ARG A CA    1 
ATOM   3977 C  C     . ARG A 1 482 ? 36.245  34.617  23.444  1.00 108.35 ? 482 ARG A C     1 
ATOM   3978 O  O     . ARG A 1 482 ? 36.657  34.175  22.365  1.00 102.24 ? 482 ARG A O     1 
ATOM   3979 C  CB    . ARG A 1 482 ? 35.131  36.875  23.406  1.00 93.73  ? 482 ARG A CB    1 
ATOM   3980 C  CG    . ARG A 1 482 ? 34.149  37.553  22.470  1.00 100.76 ? 482 ARG A CG    1 
ATOM   3981 C  CD    . ARG A 1 482 ? 34.656  38.907  22.005  1.00 106.34 ? 482 ARG A CD    1 
ATOM   3982 N  NE    . ARG A 1 482 ? 34.954  38.941  20.578  1.00 112.48 ? 482 ARG A NE    1 
ATOM   3983 C  CZ    . ARG A 1 482 ? 34.036  39.065  19.629  1.00 129.53 ? 482 ARG A CZ    1 
ATOM   3984 N  NH1   . ARG A 1 482 ? 32.745  39.055  19.913  1.00 106.88 ? 482 ARG A NH1   1 
ATOM   3985 N  NH2   . ARG A 1 482 ? 34.422  39.193  18.364  1.00 118.96 ? 482 ARG A NH2   1 
ATOM   3986 N  N     . GLN A 1 483 ? 36.908  34.433  24.589  1.00 107.16 ? 483 GLN A N     1 
ATOM   3987 C  CA    . GLN A 1 483 ? 38.192  33.741  24.607  1.00 107.44 ? 483 GLN A CA    1 
ATOM   3988 C  C     . GLN A 1 483 ? 38.059  32.302  24.119  1.00 117.35 ? 483 GLN A C     1 
ATOM   3989 O  O     . GLN A 1 483 ? 38.783  31.876  23.211  1.00 109.21 ? 483 GLN A O     1 
ATOM   3990 C  CB    . GLN A 1 483 ? 38.782  33.775  26.013  1.00 106.39 ? 483 GLN A CB    1 
ATOM   3991 C  CG    . GLN A 1 483 ? 39.997  32.893  26.192  1.00 101.72 ? 483 GLN A CG    1 
ATOM   3992 C  CD    . GLN A 1 483 ? 39.968  32.143  27.504  1.00 123.29 ? 483 GLN A CD    1 
ATOM   3993 O  OE1   . GLN A 1 483 ? 40.008  32.745  28.576  1.00 130.99 ? 483 GLN A OE1   1 
ATOM   3994 N  NE2   . GLN A 1 483 ? 39.893  30.819  27.428  1.00 122.00 ? 483 GLN A NE2   1 
ATOM   3995 N  N     . ARG A 1 484 ? 37.145  31.531  24.719  1.00 114.30 ? 484 ARG A N     1 
ATOM   3996 C  CA    . ARG A 1 484 ? 36.947  30.152  24.281  1.00 95.08  ? 484 ARG A CA    1 
ATOM   3997 C  C     . ARG A 1 484 ? 36.412  30.099  22.855  1.00 98.16  ? 484 ARG A C     1 
ATOM   3998 O  O     . ARG A 1 484 ? 36.826  29.243  22.065  1.00 89.00  ? 484 ARG A O     1 
ATOM   3999 C  CB    . ARG A 1 484 ? 36.002  29.412  25.230  1.00 105.25 ? 484 ARG A CB    1 
ATOM   4000 C  CG    . ARG A 1 484 ? 34.863  30.254  25.766  1.00 120.02 ? 484 ARG A CG    1 
ATOM   4001 C  CD    . ARG A 1 484 ? 33.805  29.400  26.448  1.00 130.26 ? 484 ARG A CD    1 
ATOM   4002 N  NE    . ARG A 1 484 ? 33.478  29.889  27.783  1.00 132.49 ? 484 ARG A NE    1 
ATOM   4003 C  CZ    . ARG A 1 484 ? 32.572  29.341  28.582  1.00 128.32 ? 484 ARG A CZ    1 
ATOM   4004 N  NH1   . ARG A 1 484 ? 31.871  28.282  28.209  1.00 107.13 ? 484 ARG A NH1   1 
ATOM   4005 N  NH2   . ARG A 1 484 ? 32.358  29.873  29.781  1.00 126.12 ? 484 ARG A NH2   1 
ATOM   4006 N  N     . LEU A 1 485 ? 35.506  31.017  22.505  1.00 87.56  ? 485 LEU A N     1 
ATOM   4007 C  CA    . LEU A 1 485 ? 34.913  31.030  21.168  1.00 69.54  ? 485 LEU A CA    1 
ATOM   4008 C  C     . LEU A 1 485 ? 35.972  31.208  20.086  1.00 72.30  ? 485 LEU A C     1 
ATOM   4009 O  O     . LEU A 1 485 ? 35.975  30.483  19.084  1.00 67.60  ? 485 LEU A O     1 
ATOM   4010 C  CB    . LEU A 1 485 ? 33.867  32.141  21.071  1.00 83.54  ? 485 LEU A CB    1 
ATOM   4011 C  CG    . LEU A 1 485 ? 32.435  31.783  21.474  1.00 90.53  ? 485 LEU A CG    1 
ATOM   4012 C  CD1   . LEU A 1 485 ? 31.596  33.037  21.685  1.00 74.85  ? 485 LEU A CD1   1 
ATOM   4013 C  CD2   . LEU A 1 485 ? 31.783  30.864  20.445  1.00 64.71  ? 485 LEU A CD2   1 
ATOM   4014 N  N     . ILE A 1 486 ? 36.865  32.189  20.259  1.00 76.30  ? 486 ILE A N     1 
ATOM   4015 C  CA    . ILE A 1 486 ? 37.931  32.433  19.284  1.00 73.04  ? 486 ILE A CA    1 
ATOM   4016 C  C     . ILE A 1 486 ? 38.705  31.152  18.999  1.00 70.81  ? 486 ILE A C     1 
ATOM   4017 O  O     . ILE A 1 486 ? 39.137  30.899  17.867  1.00 67.94  ? 486 ILE A O     1 
ATOM   4018 C  CB    . ILE A 1 486 ? 38.863  33.555  19.787  1.00 79.93  ? 486 ILE A CB    1 
ATOM   4019 C  CG1   . ILE A 1 486 ? 38.132  34.900  19.789  1.00 83.31  ? 486 ILE A CG1   1 
ATOM   4020 C  CG2   . ILE A 1 486 ? 40.151  33.622  18.960  1.00 76.50  ? 486 ILE A CG2   1 
ATOM   4021 C  CD1   . ILE A 1 486 ? 38.878  35.996  20.517  1.00 80.22  ? 486 ILE A CD1   1 
ATOM   4022 N  N     . LYS A 1 487 ? 38.880  30.320  20.021  1.00 69.77  ? 487 LYS A N     1 
ATOM   4023 C  CA    . LYS A 1 487 ? 39.603  29.067  19.862  1.00 74.38  ? 487 LYS A CA    1 
ATOM   4024 C  C     . LYS A 1 487 ? 38.818  28.074  19.011  1.00 65.16  ? 487 LYS A C     1 
ATOM   4025 O  O     . LYS A 1 487 ? 39.353  27.501  18.053  1.00 64.18  ? 487 LYS A O     1 
ATOM   4026 C  CB    . LYS A 1 487 ? 39.884  28.494  21.241  1.00 81.57  ? 487 LYS A CB    1 
ATOM   4027 C  CG    . LYS A 1 487 ? 40.459  27.140  21.231  1.00 77.41  ? 487 LYS A CG    1 
ATOM   4028 C  CD    . LYS A 1 487 ? 40.390  26.625  22.630  1.00 79.78  ? 487 LYS A CD    1 
ATOM   4029 C  CE    . LYS A 1 487 ? 40.674  25.164  22.669  1.00 91.78  ? 487 LYS A CE    1 
ATOM   4030 N  NZ    . LYS A 1 487 ? 41.790  24.946  23.577  1.00 117.88 ? 487 LYS A NZ    1 
ATOM   4031 N  N     . ILE A 1 488 ? 37.548  27.839  19.361  1.00 63.75  ? 488 ILE A N     1 
ATOM   4032 C  CA    . ILE A 1 488 ? 36.717  26.945  18.558  1.00 56.32  ? 488 ILE A CA    1 
ATOM   4033 C  C     . ILE A 1 488 ? 36.650  27.441  17.121  1.00 60.68  ? 488 ILE A C     1 
ATOM   4034 O  O     . ILE A 1 488 ? 36.736  26.654  16.171  1.00 58.47  ? 488 ILE A O     1 
ATOM   4035 C  CB    . ILE A 1 488 ? 35.310  26.807  19.171  1.00 69.20  ? 488 ILE A CB    1 
ATOM   4036 C  CG1   . ILE A 1 488 ? 35.374  26.213  20.581  1.00 68.31  ? 488 ILE A CG1   1 
ATOM   4037 C  CG2   . ILE A 1 488 ? 34.424  25.948  18.281  1.00 57.74  ? 488 ILE A CG2   1 
ATOM   4038 C  CD1   . ILE A 1 488 ? 34.681  27.053  21.630  1.00 63.92  ? 488 ILE A CD1   1 
ATOM   4039 N  N     . LEU A 1 489 ? 36.507  28.755  16.941  1.00 60.86  ? 489 LEU A N     1 
ATOM   4040 C  CA    . LEU A 1 489 ? 36.488  29.325  15.599  1.00 63.78  ? 489 LEU A CA    1 
ATOM   4041 C  C     . LEU A 1 489 ? 37.807  29.071  14.880  1.00 61.12  ? 489 LEU A C     1 
ATOM   4042 O  O     . LEU A 1 489 ? 37.822  28.638  13.722  1.00 58.60  ? 489 LEU A O     1 
ATOM   4043 C  CB    . LEU A 1 489 ? 36.189  30.822  15.677  1.00 55.92  ? 489 LEU A CB    1 
ATOM   4044 C  CG    . LEU A 1 489 ? 36.322  31.630  14.385  1.00 63.38  ? 489 LEU A CG    1 
ATOM   4045 C  CD1   . LEU A 1 489 ? 35.298  31.171  13.360  1.00 50.73  ? 489 LEU A CD1   1 
ATOM   4046 C  CD2   . LEU A 1 489 ? 36.173  33.115  14.672  1.00 60.57  ? 489 LEU A CD2   1 
ATOM   4047 N  N     . ALA A 1 490 ? 38.928  29.321  15.562  1.00 66.12  ? 490 ALA A N     1 
ATOM   4048 C  CA    . ALA A 1 490 ? 40.238  29.149  14.940  1.00 57.24  ? 490 ALA A CA    1 
ATOM   4049 C  C     . ALA A 1 490 ? 40.451  27.708  14.491  1.00 52.16  ? 490 ALA A C     1 
ATOM   4050 O  O     . ALA A 1 490 ? 40.817  27.455  13.337  1.00 49.77  ? 490 ALA A O     1 
ATOM   4051 C  CB    . ALA A 1 490 ? 41.339  29.583  15.907  1.00 52.58  ? 490 ALA A CB    1 
ATOM   4052 N  N     . ASN A 1 491 ? 40.218  26.746  15.391  1.00 51.82  ? 491 ASN A N     1 
ATOM   4053 C  CA    . ASN A 1 491 ? 40.352  25.339  15.023  1.00 51.95  ? 491 ASN A CA    1 
ATOM   4054 C  C     . ASN A 1 491 ? 39.406  24.962  13.891  1.00 55.19  ? 491 ASN A C     1 
ATOM   4055 O  O     . ASN A 1 491 ? 39.751  24.129  13.044  1.00 50.09  ? 491 ASN A O     1 
ATOM   4056 C  CB    . ASN A 1 491 ? 40.097  24.446  16.238  1.00 50.47  ? 491 ASN A CB    1 
ATOM   4057 C  CG    . ASN A 1 491 ? 41.175  24.576  17.294  1.00 60.95  ? 491 ASN A CG    1 
ATOM   4058 O  OD1   . ASN A 1 491 ? 42.313  24.939  16.996  1.00 71.96  ? 491 ASN A OD1   1 
ATOM   4059 N  ND2   . ASN A 1 491 ? 40.823  24.275  18.539  1.00 61.31  ? 491 ASN A ND2   1 
ATOM   4060 N  N     . SER A 1 492 ? 38.215  25.564  13.856  1.00 62.63  ? 492 SER A N     1 
ATOM   4061 C  CA    . SER A 1 492 ? 37.284  25.290  12.768  1.00 60.17  ? 492 SER A CA    1 
ATOM   4062 C  C     . SER A 1 492 ? 37.751  25.912  11.458  1.00 59.27  ? 492 SER A C     1 
ATOM   4063 O  O     . SER A 1 492 ? 37.383  25.430  10.380  1.00 53.51  ? 492 SER A O     1 
ATOM   4064 C  CB    . SER A 1 492 ? 35.891  25.792  13.137  1.00 60.16  ? 492 SER A CB    1 
ATOM   4065 O  OG    . SER A 1 492 ? 35.638  25.620  14.520  1.00 69.98  ? 492 SER A OG    1 
ATOM   4066 N  N     . VAL A 1 493 ? 38.552  26.980  11.525  1.00 63.21  ? 493 VAL A N     1 
ATOM   4067 C  CA    . VAL A 1 493 ? 39.161  27.519  10.312  1.00 60.82  ? 493 VAL A CA    1 
ATOM   4068 C  C     . VAL A 1 493 ? 40.179  26.534  9.750   1.00 56.12  ? 493 VAL A C     1 
ATOM   4069 O  O     . VAL A 1 493 ? 40.286  26.361  8.529   1.00 48.81  ? 493 VAL A O     1 
ATOM   4070 C  CB    . VAL A 1 493 ? 39.789  28.899  10.587  1.00 57.07  ? 493 VAL A CB    1 
ATOM   4071 C  CG1   . VAL A 1 493 ? 40.531  29.402  9.357   1.00 55.22  ? 493 VAL A CG1   1 
ATOM   4072 C  CG2   . VAL A 1 493 ? 38.716  29.896  10.988  1.00 54.85  ? 493 VAL A CG2   1 
ATOM   4073 N  N     . TYR A 1 494 ? 40.937  25.867  10.624  1.00 52.04  ? 494 TYR A N     1 
ATOM   4074 C  CA    . TYR A 1 494 ? 41.776  24.765  10.162  1.00 50.50  ? 494 TYR A CA    1 
ATOM   4075 C  C     . TYR A 1 494 ? 40.924  23.665  9.542   1.00 55.93  ? 494 TYR A C     1 
ATOM   4076 O  O     . TYR A 1 494 ? 41.197  23.204  8.428   1.00 59.64  ? 494 TYR A O     1 
ATOM   4077 C  CB    . TYR A 1 494 ? 42.613  24.196  11.308  1.00 42.61  ? 494 TYR A CB    1 
ATOM   4078 C  CG    . TYR A 1 494 ? 42.924  22.729  11.100  1.00 51.19  ? 494 TYR A CG    1 
ATOM   4079 C  CD1   . TYR A 1 494 ? 43.776  22.316  10.081  1.00 54.20  ? 494 TYR A CD1   1 
ATOM   4080 C  CD2   . TYR A 1 494 ? 42.332  21.754  11.892  1.00 50.53  ? 494 TYR A CD2   1 
ATOM   4081 C  CE1   . TYR A 1 494 ? 44.044  20.978  9.872   1.00 53.22  ? 494 TYR A CE1   1 
ATOM   4082 C  CE2   . TYR A 1 494 ? 42.595  20.413  11.689  1.00 44.49  ? 494 TYR A CE2   1 
ATOM   4083 C  CZ    . TYR A 1 494 ? 43.451  20.031  10.679  1.00 54.31  ? 494 TYR A CZ    1 
ATOM   4084 O  OH    . TYR A 1 494 ? 43.715  18.697  10.475  1.00 62.51  ? 494 TYR A OH    1 
ATOM   4085 N  N     . GLY A 1 495 ? 39.886  23.225  10.259  1.00 50.42  ? 495 GLY A N     1 
ATOM   4086 C  CA    . GLY A 1 495 ? 39.020  22.185  9.732   1.00 52.44  ? 495 GLY A CA    1 
ATOM   4087 C  C     . GLY A 1 495 ? 38.331  22.588  8.444   1.00 55.69  ? 495 GLY A C     1 
ATOM   4088 O  O     . GLY A 1 495 ? 37.994  21.732  7.621   1.00 66.90  ? 495 GLY A O     1 
ATOM   4089 N  N     . HIS A 1 496 ? 38.118  23.891  8.251   1.00 59.64  ? 496 HIS A N     1 
ATOM   4090 C  CA    . HIS A 1 496 ? 37.542  24.377  7.003   1.00 56.90  ? 496 HIS A CA    1 
ATOM   4091 C  C     . HIS A 1 496 ? 38.406  23.989  5.809   1.00 53.64  ? 496 HIS A C     1 
ATOM   4092 O  O     . HIS A 1 496 ? 37.887  23.609  4.755   1.00 60.12  ? 496 HIS A O     1 
ATOM   4093 C  CB    . HIS A 1 496 ? 37.366  25.895  7.083   1.00 52.60  ? 496 HIS A CB    1 
ATOM   4094 C  CG    . HIS A 1 496 ? 36.799  26.513  5.843   1.00 60.45  ? 496 HIS A CG    1 
ATOM   4095 N  ND1   . HIS A 1 496 ? 35.448  26.720  5.665   1.00 56.78  ? 496 HIS A ND1   1 
ATOM   4096 C  CD2   . HIS A 1 496 ? 37.401  26.985  4.725   1.00 64.80  ? 496 HIS A CD2   1 
ATOM   4097 C  CE1   . HIS A 1 496 ? 35.242  27.288  4.490   1.00 63.01  ? 496 HIS A CE1   1 
ATOM   4098 N  NE2   . HIS A 1 496 ? 36.411  27.458  3.899   1.00 63.33  ? 496 HIS A NE2   1 
ATOM   4099 N  N     . MET A 1 497 ? 39.730  24.049  5.964   1.00 62.66  ? 497 MET A N     1 
ATOM   4100 C  CA    . MET A 1 497 ? 40.622  23.816  4.833   1.00 59.32  ? 497 MET A CA    1 
ATOM   4101 C  C     . MET A 1 497 ? 40.585  22.377  4.334   1.00 60.84  ? 497 MET A C     1 
ATOM   4102 O  O     . MET A 1 497 ? 40.948  22.128  3.179   1.00 55.55  ? 497 MET A O     1 
ATOM   4103 C  CB    . MET A 1 497 ? 42.050  24.206  5.208   1.00 67.06  ? 497 MET A CB    1 
ATOM   4104 C  CG    . MET A 1 497 ? 42.266  25.709  5.262   1.00 56.93  ? 497 MET A CG    1 
ATOM   4105 S  SD    . MET A 1 497 ? 43.909  26.167  5.838   1.00 62.38  ? 497 MET A SD    1 
ATOM   4106 C  CE    . MET A 1 497 ? 44.228  24.862  7.022   1.00 66.06  ? 497 MET A CE    1 
ATOM   4107 N  N     . GLY A 1 498 ? 40.161  21.431  5.167   1.00 62.64  ? 498 GLY A N     1 
ATOM   4108 C  CA    . GLY A 1 498 ? 39.975  20.053  4.764   1.00 46.98  ? 498 GLY A CA    1 
ATOM   4109 C  C     . GLY A 1 498 ? 38.533  19.643  4.558   1.00 72.49  ? 498 GLY A C     1 
ATOM   4110 O  O     . GLY A 1 498 ? 38.266  18.452  4.354   1.00 62.32  ? 498 GLY A O     1 
ATOM   4111 N  N     . PHE A 1 499 ? 37.596  20.587  4.600   1.00 67.52  ? 499 PHE A N     1 
ATOM   4112 C  CA    . PHE A 1 499 ? 36.175  20.288  4.480   1.00 58.67  ? 499 PHE A CA    1 
ATOM   4113 C  C     . PHE A 1 499 ? 35.800  20.108  3.014   1.00 57.97  ? 499 PHE A C     1 
ATOM   4114 O  O     . PHE A 1 499 ? 36.172  20.925  2.167   1.00 69.07  ? 499 PHE A O     1 
ATOM   4115 C  CB    . PHE A 1 499 ? 35.358  21.414  5.116   1.00 60.02  ? 499 PHE A CB    1 
ATOM   4116 C  CG    . PHE A 1 499 ? 33.868  21.260  4.971   1.00 74.23  ? 499 PHE A CG    1 
ATOM   4117 C  CD1   . PHE A 1 499 ? 33.267  20.012  5.010   1.00 74.26  ? 499 PHE A CD1   1 
ATOM   4118 C  CD2   . PHE A 1 499 ? 33.065  22.378  4.801   1.00 81.41  ? 499 PHE A CD2   1 
ATOM   4119 C  CE1   . PHE A 1 499 ? 31.895  19.882  4.876   1.00 83.77  ? 499 PHE A CE1   1 
ATOM   4120 C  CE2   . PHE A 1 499 ? 31.695  22.255  4.668   1.00 70.74  ? 499 PHE A CE2   1 
ATOM   4121 C  CZ    . PHE A 1 499 ? 31.109  21.006  4.706   1.00 83.40  ? 499 PHE A CZ    1 
ATOM   4122 N  N     . GLU A 1 500 ? 35.063  19.031  2.724   1.00 59.24  ? 500 GLU A N     1 
ATOM   4123 C  CA    . GLU A 1 500 ? 34.645  18.734  1.356   1.00 68.66  ? 500 GLU A CA    1 
ATOM   4124 C  C     . GLU A 1 500 ? 33.981  19.938  0.697   1.00 74.33  ? 500 GLU A C     1 
ATOM   4125 O  O     . GLU A 1 500 ? 34.340  20.328  -0.420  1.00 66.43  ? 500 GLU A O     1 
ATOM   4126 C  CB    . GLU A 1 500 ? 33.684  17.541  1.345   1.00 72.45  ? 500 GLU A CB    1 
ATOM   4127 C  CG    . GLU A 1 500 ? 34.222  16.245  1.930   1.00 83.04  ? 500 GLU A CG    1 
ATOM   4128 C  CD    . GLU A 1 500 ? 34.154  16.208  3.444   1.00 80.34  ? 500 GLU A CD    1 
ATOM   4129 O  OE1   . GLU A 1 500 ? 33.034  16.106  3.990   1.00 68.96  ? 500 GLU A OE1   1 
ATOM   4130 O  OE2   . GLU A 1 500 ? 35.225  16.264  4.085   1.00 60.94  ? 500 GLU A OE2   1 
ATOM   4131 N  N     . ASN A 1 501 ? 33.008  20.542  1.380   1.00 70.03  ? 501 ASN A N     1 
ATOM   4132 C  CA    . ASN A 1 501 ? 32.177  21.597  0.815   1.00 72.00  ? 501 ASN A CA    1 
ATOM   4133 C  C     . ASN A 1 501 ? 32.601  22.988  1.278   1.00 63.19  ? 501 ASN A C     1 
ATOM   4134 O  O     . ASN A 1 501 ? 31.755  23.873  1.444   1.00 74.32  ? 501 ASN A O     1 
ATOM   4135 C  CB    . ASN A 1 501 ? 30.711  21.344  1.162   1.00 79.02  ? 501 ASN A CB    1 
ATOM   4136 C  CG    . ASN A 1 501 ? 29.756  22.082  0.248   1.00 72.73  ? 501 ASN A CG    1 
ATOM   4137 O  OD1   . ASN A 1 501 ? 29.829  21.962  -0.975  1.00 76.34  ? 501 ASN A OD1   1 
ATOM   4138 N  ND2   . ASN A 1 501 ? 28.848  22.848  0.839   1.00 70.42  ? 501 ASN A ND2   1 
ATOM   4139 N  N     . ALA A 1 502 ? 33.895  23.203  1.484   1.00 73.16  ? 502 ALA A N     1 
ATOM   4140 C  CA    . ALA A 1 502 ? 34.404  24.482  1.955   1.00 55.66  ? 502 ALA A CA    1 
ATOM   4141 C  C     . ALA A 1 502 ? 34.890  25.325  0.785   1.00 58.26  ? 502 ALA A C     1 
ATOM   4142 O  O     . ALA A 1 502 ? 35.431  24.801  -0.193  1.00 63.94  ? 502 ALA A O     1 
ATOM   4143 C  CB    . ALA A 1 502 ? 35.538  24.278  2.954   1.00 58.42  ? 502 ALA A CB    1 
ATOM   4144 N  N     . ARG A 1 503 ? 34.696  26.640  0.896   1.00 58.57  ? 503 ARG A N     1 
ATOM   4145 C  CA    . ARG A 1 503 ? 35.130  27.542  -0.166  1.00 68.82  ? 503 ARG A CA    1 
ATOM   4146 C  C     . ARG A 1 503 ? 36.648  27.658  -0.201  1.00 65.82  ? 503 ARG A C     1 
ATOM   4147 O  O     . ARG A 1 503 ? 37.260  27.607  -1.275  1.00 53.10  ? 503 ARG A O     1 
ATOM   4148 C  CB    . ARG A 1 503 ? 34.486  28.915  0.023   1.00 60.83  ? 503 ARG A CB    1 
ATOM   4149 C  CG    . ARG A 1 503 ? 32.994  28.858  0.286   1.00 66.37  ? 503 ARG A CG    1 
ATOM   4150 C  CD    . ARG A 1 503 ? 32.424  30.234  0.570   1.00 71.09  ? 503 ARG A CD    1 
ATOM   4151 N  NE    . ARG A 1 503 ? 31.974  30.900  -0.646  1.00 75.85  ? 503 ARG A NE    1 
ATOM   4152 C  CZ    . ARG A 1 503 ? 30.761  30.773  -1.164  1.00 65.65  ? 503 ARG A CZ    1 
ATOM   4153 N  NH1   . ARG A 1 503 ? 29.843  30.005  -0.599  1.00 77.95  ? 503 ARG A NH1   1 
ATOM   4154 N  NH2   . ARG A 1 503 ? 30.460  31.434  -2.278  1.00 77.18  ? 503 ARG A NH2   1 
ATOM   4155 N  N     . TRP A 1 504 ? 37.272  27.816  0.960   1.00 60.30  ? 504 TRP A N     1 
ATOM   4156 C  CA    . TRP A 1 504 ? 38.730  27.898  1.060   1.00 67.34  ? 504 TRP A CA    1 
ATOM   4157 C  C     . TRP A 1 504 ? 39.338  26.536  1.382   1.00 63.27  ? 504 TRP A C     1 
ATOM   4158 O  O     . TRP A 1 504 ? 40.175  26.394  2.270   1.00 61.07  ? 504 TRP A O     1 
ATOM   4159 C  CB    . TRP A 1 504 ? 39.125  28.940  2.100   1.00 64.00  ? 504 TRP A CB    1 
ATOM   4160 C  CG    . TRP A 1 504 ? 38.955  30.351  1.616   1.00 68.46  ? 504 TRP A CG    1 
ATOM   4161 C  CD1   . TRP A 1 504 ? 39.901  31.131  1.015   1.00 57.79  ? 504 TRP A CD1   1 
ATOM   4162 C  CD2   . TRP A 1 504 ? 37.765  31.148  1.686   1.00 73.35  ? 504 TRP A CD2   1 
ATOM   4163 N  NE1   . TRP A 1 504 ? 39.375  32.363  0.710   1.00 56.52  ? 504 TRP A NE1   1 
ATOM   4164 C  CE2   . TRP A 1 504 ? 38.066  32.399  1.111   1.00 64.98  ? 504 TRP A CE2   1 
ATOM   4165 C  CE3   . TRP A 1 504 ? 36.476  30.925  2.180   1.00 67.07  ? 504 TRP A CE3   1 
ATOM   4166 C  CZ2   . TRP A 1 504 ? 37.126  33.423  1.018   1.00 62.96  ? 504 TRP A CZ2   1 
ATOM   4167 C  CZ3   . TRP A 1 504 ? 35.544  31.943  2.085   1.00 61.04  ? 504 TRP A CZ3   1 
ATOM   4168 C  CH2   . TRP A 1 504 ? 35.874  33.176  1.509   1.00 64.67  ? 504 TRP A CH2   1 
ATOM   4169 N  N     . TYR A 1 505 ? 38.905  25.515  0.647   1.00 61.10  ? 505 TYR A N     1 
ATOM   4170 C  CA    . TYR A 1 505 ? 39.430  24.171  0.836   1.00 60.99  ? 505 TYR A CA    1 
ATOM   4171 C  C     . TYR A 1 505 ? 40.855  24.079  0.308   1.00 69.25  ? 505 TYR A C     1 
ATOM   4172 O  O     . TYR A 1 505 ? 41.182  24.635  -0.744  1.00 68.38  ? 505 TYR A O     1 
ATOM   4173 C  CB    . TYR A 1 505 ? 38.532  23.155  0.128   1.00 53.62  ? 505 TYR A CB    1 
ATOM   4174 C  CG    . TYR A 1 505 ? 39.107  21.759  -0.000  1.00 58.13  ? 505 TYR A CG    1 
ATOM   4175 C  CD1   . TYR A 1 505 ? 39.003  20.844  1.039   1.00 65.21  ? 505 TYR A CD1   1 
ATOM   4176 C  CD2   . TYR A 1 505 ? 39.737  21.351  -1.169  1.00 55.89  ? 505 TYR A CD2   1 
ATOM   4177 C  CE1   . TYR A 1 505 ? 39.517  19.564  0.921   1.00 67.43  ? 505 TYR A CE1   1 
ATOM   4178 C  CE2   . TYR A 1 505 ? 40.255  20.075  -1.296  1.00 59.30  ? 505 TYR A CE2   1 
ATOM   4179 C  CZ    . TYR A 1 505 ? 40.142  19.185  -0.248  1.00 61.07  ? 505 TYR A CZ    1 
ATOM   4180 O  OH    . TYR A 1 505 ? 40.656  17.914  -0.369  1.00 67.55  ? 505 TYR A OH    1 
ATOM   4181 N  N     . CYS A 1 506 ? 41.707  23.373  1.051   1.00 63.72  ? 506 CYS A N     1 
ATOM   4182 C  CA    . CYS A 1 506 ? 43.102  23.178  0.644   1.00 56.74  ? 506 CYS A CA    1 
ATOM   4183 C  C     . CYS A 1 506 ? 43.626  21.973  1.432   1.00 57.44  ? 506 CYS A C     1 
ATOM   4184 O  O     . CYS A 1 506 ? 44.056  22.114  2.577   1.00 56.55  ? 506 CYS A O     1 
ATOM   4185 C  CB    . CYS A 1 506 ? 43.945  24.413  0.895   1.00 54.75  ? 506 CYS A CB    1 
ATOM   4186 S  SG    . CYS A 1 506 ? 45.714  24.216  0.541   1.00 79.83  ? 506 CYS A SG    1 
ATOM   4187 N  N     . LYS A 1 507 ? 43.570  20.795  0.805   1.00 54.01  ? 507 LYS A N     1 
ATOM   4188 C  CA    . LYS A 1 507 ? 44.047  19.591  1.477   1.00 66.25  ? 507 LYS A CA    1 
ATOM   4189 C  C     . LYS A 1 507 ? 45.532  19.692  1.794   1.00 68.72  ? 507 LYS A C     1 
ATOM   4190 O  O     . LYS A 1 507 ? 45.971  19.285  2.877   1.00 63.72  ? 507 LYS A O     1 
ATOM   4191 C  CB    . LYS A 1 507 ? 43.772  18.354  0.625   1.00 61.43  ? 507 LYS A CB    1 
ATOM   4192 C  CG    . LYS A 1 507 ? 43.764  17.068  1.433   1.00 63.40  ? 507 LYS A CG    1 
ATOM   4193 C  CD    . LYS A 1 507 ? 44.004  15.852  0.561   1.00 73.66  ? 507 LYS A CD    1 
ATOM   4194 C  CE    . LYS A 1 507 ? 45.425  15.798  0.030   1.00 84.54  ? 507 LYS A CE    1 
ATOM   4195 N  NZ    . LYS A 1 507 ? 45.693  14.496  -0.643  1.00 88.24  ? 507 LYS A NZ    1 
ATOM   4196 N  N     . GLU A 1 508 ? 46.319  20.226  0.857   1.00 61.40  ? 508 GLU A N     1 
ATOM   4197 C  CA    . GLU A 1 508 ? 47.745  20.417  1.098   1.00 64.96  ? 508 GLU A CA    1 
ATOM   4198 C  C     . GLU A 1 508 ? 47.977  21.271  2.336   1.00 66.99  ? 508 GLU A C     1 
ATOM   4199 O  O     . GLU A 1 508 ? 48.803  20.934  3.191   1.00 68.34  ? 508 GLU A O     1 
ATOM   4200 C  CB    . GLU A 1 508 ? 48.401  21.055  -0.127  1.00 65.36  ? 508 GLU A CB    1 
ATOM   4201 C  CG    . GLU A 1 508 ? 48.127  20.326  -1.432  1.00 68.34  ? 508 GLU A CG    1 
ATOM   4202 C  CD    . GLU A 1 508 ? 46.901  20.858  -2.150  1.00 70.54  ? 508 GLU A CD    1 
ATOM   4203 O  OE1   . GLU A 1 508 ? 46.078  21.541  -1.503  1.00 77.65  ? 508 GLU A OE1   1 
ATOM   4204 O  OE2   . GLU A 1 508 ? 46.761  20.598  -3.363  1.00 56.34  ? 508 GLU A OE2   1 
ATOM   4205 N  N     . CYS A 1 509 ? 47.244  22.381  2.450   1.00 57.20  ? 509 CYS A N     1 
ATOM   4206 C  CA    . CYS A 1 509 ? 47.331  23.208  3.649   1.00 47.26  ? 509 CYS A CA    1 
ATOM   4207 C  C     . CYS A 1 509 ? 46.929  22.423  4.888   1.00 53.60  ? 509 CYS A C     1 
ATOM   4208 O  O     . CYS A 1 509 ? 47.598  22.499  5.925   1.00 61.46  ? 509 CYS A O     1 
ATOM   4209 C  CB    . CYS A 1 509 ? 46.447  24.446  3.498   1.00 43.91  ? 509 CYS A CB    1 
ATOM   4210 S  SG    . CYS A 1 509 ? 46.657  25.350  1.946   1.00 69.56  ? 509 CYS A SG    1 
ATOM   4211 N  N     . ALA A 1 510 ? 45.844  21.653  4.796   1.00 66.87  ? 510 ALA A N     1 
ATOM   4212 C  CA    . ALA A 1 510 ? 45.347  20.924  5.957   1.00 64.35  ? 510 ALA A CA    1 
ATOM   4213 C  C     . ALA A 1 510 ? 46.339  19.862  6.411   1.00 60.03  ? 510 ALA A C     1 
ATOM   4214 O  O     . ALA A 1 510 ? 46.677  19.777  7.597   1.00 56.54  ? 510 ALA A O     1 
ATOM   4215 C  CB    . ALA A 1 510 ? 43.991  20.295  5.638   1.00 63.37  ? 510 ALA A CB    1 
ATOM   4216 N  N     . GLU A 1 511 ? 46.823  19.040  5.477   1.00 59.23  ? 511 GLU A N     1 
ATOM   4217 C  CA    . GLU A 1 511 ? 47.719  17.951  5.845   1.00 60.51  ? 511 GLU A CA    1 
ATOM   4218 C  C     . GLU A 1 511 ? 49.134  18.426  6.149   1.00 68.04  ? 511 GLU A C     1 
ATOM   4219 O  O     . GLU A 1 511 ? 49.882  17.706  6.820   1.00 62.01  ? 511 GLU A O     1 
ATOM   4220 C  CB    . GLU A 1 511 ? 47.745  16.887  4.744   1.00 52.51  ? 511 GLU A CB    1 
ATOM   4221 C  CG    . GLU A 1 511 ? 48.456  17.295  3.467   1.00 62.01  ? 511 GLU A CG    1 
ATOM   4222 C  CD    . GLU A 1 511 ? 48.498  16.168  2.454   1.00 65.06  ? 511 GLU A CD    1 
ATOM   4223 O  OE1   . GLU A 1 511 ? 48.234  15.010  2.845   1.00 62.25  ? 511 GLU A OE1   1 
ATOM   4224 O  OE2   . GLU A 1 511 ? 48.789  16.439  1.270   1.00 65.67  ? 511 GLU A OE2   1 
ATOM   4225 N  N     . SER A 1 512 ? 49.521  19.612  5.673   1.00 64.16  ? 512 SER A N     1 
ATOM   4226 C  CA    . SER A 1 512 ? 50.792  20.188  6.098   1.00 51.55  ? 512 SER A CA    1 
ATOM   4227 C  C     . SER A 1 512 ? 50.742  20.590  7.565   1.00 61.13  ? 512 SER A C     1 
ATOM   4228 O  O     . SER A 1 512 ? 51.721  20.412  8.299   1.00 61.26  ? 512 SER A O     1 
ATOM   4229 C  CB    . SER A 1 512 ? 51.146  21.395  5.229   1.00 49.04  ? 512 SER A CB    1 
ATOM   4230 O  OG    . SER A 1 512 ? 51.367  21.012  3.884   1.00 63.43  ? 512 SER A OG    1 
ATOM   4231 N  N     . VAL A 1 513 ? 49.603  21.130  8.006   1.00 61.23  ? 513 VAL A N     1 
ATOM   4232 C  CA    . VAL A 1 513 ? 49.459  21.567  9.392   1.00 59.20  ? 513 VAL A CA    1 
ATOM   4233 C  C     . VAL A 1 513 ? 49.640  20.390  10.341  1.00 56.36  ? 513 VAL A C     1 
ATOM   4234 O  O     . VAL A 1 513 ? 50.390  20.468  11.322  1.00 57.86  ? 513 VAL A O     1 
ATOM   4235 C  CB    . VAL A 1 513 ? 48.094  22.249  9.592   1.00 51.84  ? 513 VAL A CB    1 
ATOM   4236 C  CG1   . VAL A 1 513 ? 47.769  22.380  11.072  1.00 56.48  ? 513 VAL A CG1   1 
ATOM   4237 C  CG2   . VAL A 1 513 ? 48.081  23.601  8.912   1.00 47.28  ? 513 VAL A CG2   1 
ATOM   4238 N  N     . THR A 1 514 ? 48.957  19.278  10.059  1.00 56.99  ? 514 THR A N     1 
ATOM   4239 C  CA    . THR A 1 514 ? 49.096  18.094  10.898  1.00 64.71  ? 514 THR A CA    1 
ATOM   4240 C  C     . THR A 1 514 ? 50.501  17.512  10.817  1.00 64.81  ? 514 THR A C     1 
ATOM   4241 O  O     . THR A 1 514 ? 51.011  16.988  11.814  1.00 59.57  ? 514 THR A O     1 
ATOM   4242 C  CB    . THR A 1 514 ? 48.066  17.039  10.495  1.00 60.25  ? 514 THR A CB    1 
ATOM   4243 O  OG1   . THR A 1 514 ? 48.084  16.869  9.073   1.00 64.82  ? 514 THR A OG1   1 
ATOM   4244 C  CG2   . THR A 1 514 ? 46.676  17.472  10.924  1.00 51.02  ? 514 THR A CG2   1 
ATOM   4245 N  N     . ALA A 1 515 ? 51.140  17.596  9.647   1.00 62.59  ? 515 ALA A N     1 
ATOM   4246 C  CA    . ALA A 1 515 ? 52.495  17.075  9.505   1.00 57.03  ? 515 ALA A CA    1 
ATOM   4247 C  C     . ALA A 1 515 ? 53.469  17.831  10.398  1.00 67.22  ? 515 ALA A C     1 
ATOM   4248 O  O     . ALA A 1 515 ? 54.337  17.224  11.038  1.00 67.35  ? 515 ALA A O     1 
ATOM   4249 C  CB    . ALA A 1 515 ? 52.937  17.148  8.044   1.00 49.61  ? 515 ALA A CB    1 
ATOM   4250 N  N     . TRP A 1 516 ? 53.345  19.160  10.453  1.00 61.92  ? 516 TRP A N     1 
ATOM   4251 C  CA    . TRP A 1 516 ? 54.176  19.933  11.370  1.00 58.93  ? 516 TRP A CA    1 
ATOM   4252 C  C     . TRP A 1 516 ? 53.858  19.585  12.818  1.00 61.64  ? 516 TRP A C     1 
ATOM   4253 O  O     . TRP A 1 516 ? 54.767  19.425  13.641  1.00 66.72  ? 516 TRP A O     1 
ATOM   4254 C  CB    . TRP A 1 516 ? 53.989  21.431  11.129  1.00 53.86  ? 516 TRP A CB    1 
ATOM   4255 C  CG    . TRP A 1 516 ? 55.035  22.052  10.250  1.00 63.50  ? 516 TRP A CG    1 
ATOM   4256 C  CD1   . TRP A 1 516 ? 56.358  22.215  10.543  1.00 51.41  ? 516 TRP A CD1   1 
ATOM   4257 C  CD2   . TRP A 1 516 ? 54.837  22.641  8.957   1.00 62.11  ? 516 TRP A CD2   1 
ATOM   4258 N  NE1   . TRP A 1 516 ? 57.001  22.843  9.505   1.00 56.28  ? 516 TRP A NE1   1 
ATOM   4259 C  CE2   . TRP A 1 516 ? 56.090  23.117  8.520   1.00 65.27  ? 516 TRP A CE2   1 
ATOM   4260 C  CE3   . TRP A 1 516 ? 53.727  22.801  8.123   1.00 65.24  ? 516 TRP A CE3   1 
ATOM   4261 C  CZ2   . TRP A 1 516 ? 56.262  23.745  7.286   1.00 55.21  ? 516 TRP A CZ2   1 
ATOM   4262 C  CZ3   . TRP A 1 516 ? 53.900  23.422  6.898   1.00 64.87  ? 516 TRP A CZ3   1 
ATOM   4263 C  CH2   . TRP A 1 516 ? 55.157  23.887  6.492   1.00 65.35  ? 516 TRP A CH2   1 
ATOM   4264 N  N     . GLY A 1 517 ? 52.570  19.455  13.145  1.00 60.33  ? 517 GLY A N     1 
ATOM   4265 C  CA    . GLY A 1 517 ? 52.190  19.133  14.511  1.00 57.96  ? 517 GLY A CA    1 
ATOM   4266 C  C     . GLY A 1 517 ? 52.781  17.822  14.992  1.00 50.14  ? 517 GLY A C     1 
ATOM   4267 O  O     . GLY A 1 517 ? 53.212  17.710  16.142  1.00 59.22  ? 517 GLY A O     1 
ATOM   4268 N  N     . ARG A 1 518 ? 52.811  16.814  14.117  1.00 54.01  ? 518 ARG A N     1 
ATOM   4269 C  CA    . ARG A 1 518 ? 53.465  15.556  14.461  1.00 57.95  ? 518 ARG A CA    1 
ATOM   4270 C  C     . ARG A 1 518 ? 54.946  15.769  14.745  1.00 67.71  ? 518 ARG A C     1 
ATOM   4271 O  O     . ARG A 1 518 ? 55.492  15.199  15.696  1.00 68.01  ? 518 ARG A O     1 
ATOM   4272 C  CB    . ARG A 1 518 ? 53.283  14.542  13.332  1.00 65.23  ? 518 ARG A CB    1 
ATOM   4273 C  CG    . ARG A 1 518 ? 51.906  13.911  13.266  1.00 57.27  ? 518 ARG A CG    1 
ATOM   4274 C  CD    . ARG A 1 518 ? 51.763  13.063  12.015  1.00 48.77  ? 518 ARG A CD    1 
ATOM   4275 N  NE    . ARG A 1 518 ? 50.926  13.713  11.015  1.00 69.63  ? 518 ARG A NE    1 
ATOM   4276 C  CZ    . ARG A 1 518 ? 51.170  13.702  9.712   1.00 71.70  ? 518 ARG A CZ    1 
ATOM   4277 N  NH1   . ARG A 1 518 ? 52.222  13.075  9.211   1.00 50.28  ? 518 ARG A NH1   1 
ATOM   4278 N  NH2   . ARG A 1 518 ? 50.337  14.335  8.890   1.00 60.53  ? 518 ARG A NH2   1 
ATOM   4279 N  N     . GLU A 1 519 ? 55.611  16.592  13.931  1.00 67.80  ? 519 GLU A N     1 
ATOM   4280 C  CA    . GLU A 1 519 ? 57.039  16.822  14.122  1.00 72.18  ? 519 GLU A CA    1 
ATOM   4281 C  C     . GLU A 1 519 ? 57.310  17.536  15.439  1.00 68.45  ? 519 GLU A C     1 
ATOM   4282 O  O     . GLU A 1 519 ? 58.173  17.115  16.217  1.00 73.43  ? 519 GLU A O     1 
ATOM   4283 C  CB    . GLU A 1 519 ? 57.608  17.627  12.953  1.00 67.88  ? 519 GLU A CB    1 
ATOM   4284 C  CG    . GLU A 1 519 ? 58.997  18.190  13.225  1.00 81.57  ? 519 GLU A CG    1 
ATOM   4285 C  CD    . GLU A 1 519 ? 59.472  19.140  12.145  1.00 93.28  ? 519 GLU A CD    1 
ATOM   4286 O  OE1   . GLU A 1 519 ? 59.383  18.780  10.953  1.00 103.67 ? 519 GLU A OE1   1 
ATOM   4287 O  OE2   . GLU A 1 519 ? 59.938  20.247  12.489  1.00 98.73  ? 519 GLU A OE2   1 
ATOM   4288 N  N     . TYR A 1 520 ? 56.575  18.617  15.711  1.00 65.65  ? 520 TYR A N     1 
ATOM   4289 C  CA    . TYR A 1 520 ? 56.834  19.399  16.916  1.00 62.85  ? 520 TYR A CA    1 
ATOM   4290 C  C     . TYR A 1 520 ? 56.557  18.588  18.174  1.00 66.66  ? 520 TYR A C     1 
ATOM   4291 O  O     . TYR A 1 520 ? 57.280  18.708  19.170  1.00 79.36  ? 520 TYR A O     1 
ATOM   4292 C  CB    . TYR A 1 520 ? 55.995  20.677  16.903  1.00 61.76  ? 520 TYR A CB    1 
ATOM   4293 C  CG    . TYR A 1 520 ? 56.434  21.665  15.850  1.00 63.47  ? 520 TYR A CG    1 
ATOM   4294 C  CD1   . TYR A 1 520 ? 57.710  22.211  15.874  1.00 52.71  ? 520 TYR A CD1   1 
ATOM   4295 C  CD2   . TYR A 1 520 ? 55.577  22.048  14.829  1.00 54.74  ? 520 TYR A CD2   1 
ATOM   4296 C  CE1   . TYR A 1 520 ? 58.120  23.112  14.911  1.00 53.18  ? 520 TYR A CE1   1 
ATOM   4297 C  CE2   . TYR A 1 520 ? 55.978  22.945  13.858  1.00 71.05  ? 520 TYR A CE2   1 
ATOM   4298 C  CZ    . TYR A 1 520 ? 57.252  23.473  13.902  1.00 63.59  ? 520 TYR A CZ    1 
ATOM   4299 O  OH    . TYR A 1 520 ? 57.651  24.375  12.942  1.00 67.82  ? 520 TYR A OH    1 
ATOM   4300 N  N     . LEU A 1 521 ? 55.524  17.746  18.148  1.00 63.99  ? 521 LEU A N     1 
ATOM   4301 C  CA    . LEU A 1 521 ? 55.187  16.966  19.332  1.00 64.65  ? 521 LEU A CA    1 
ATOM   4302 C  C     . LEU A 1 521 ? 56.209  15.862  19.573  1.00 63.23  ? 521 LEU A C     1 
ATOM   4303 O  O     . LEU A 1 521 ? 56.691  15.684  20.698  1.00 66.57  ? 521 LEU A O     1 
ATOM   4304 C  CB    . LEU A 1 521 ? 53.783  16.381  19.196  1.00 54.79  ? 521 LEU A CB    1 
ATOM   4305 C  CG    . LEU A 1 521 ? 53.397  15.398  20.300  1.00 52.13  ? 521 LEU A CG    1 
ATOM   4306 C  CD1   . LEU A 1 521 ? 53.089  16.137  21.595  1.00 49.02  ? 521 LEU A CD1   1 
ATOM   4307 C  CD2   . LEU A 1 521 ? 52.220  14.550  19.862  1.00 62.39  ? 521 LEU A CD2   1 
ATOM   4308 N  N     . THR A 1 522 ? 56.554  15.107  18.526  1.00 67.64  ? 522 THR A N     1 
ATOM   4309 C  CA    . THR A 1 522 ? 57.519  14.024  18.688  1.00 67.86  ? 522 THR A CA    1 
ATOM   4310 C  C     . THR A 1 522 ? 58.922  14.554  18.950  1.00 67.85  ? 522 THR A C     1 
ATOM   4311 O  O     . THR A 1 522 ? 59.709  13.901  19.645  1.00 73.53  ? 522 THR A O     1 
ATOM   4312 C  CB    . THR A 1 522 ? 57.514  13.117  17.456  1.00 68.07  ? 522 THR A CB    1 
ATOM   4313 O  OG1   . THR A 1 522 ? 57.861  13.878  16.293  1.00 76.06  ? 522 THR A OG1   1 
ATOM   4314 C  CG2   . THR A 1 522 ? 56.139  12.490  17.263  1.00 61.52  ? 522 THR A CG2   1 
ATOM   4315 N  N     . MET A 1 523 ? 59.256  15.725  18.403  1.00 68.60  ? 523 MET A N     1 
ATOM   4316 C  CA    . MET A 1 523 ? 60.525  16.362  18.739  1.00 68.55  ? 523 MET A CA    1 
ATOM   4317 C  C     . MET A 1 523 ? 60.577  16.707  20.221  1.00 62.90  ? 523 MET A C     1 
ATOM   4318 O  O     . MET A 1 523 ? 61.558  16.407  20.910  1.00 84.13  ? 523 MET A O     1 
ATOM   4319 C  CB    . MET A 1 523 ? 60.720  17.611  17.873  1.00 66.47  ? 523 MET A CB    1 
ATOM   4320 C  CG    . MET A 1 523 ? 61.909  18.501  18.238  1.00 80.99  ? 523 MET A CG    1 
ATOM   4321 S  SD    . MET A 1 523 ? 61.594  19.659  19.588  1.00 92.01  ? 523 MET A SD    1 
ATOM   4322 C  CE    . MET A 1 523 ? 61.023  21.097  18.690  1.00 78.72  ? 523 MET A CE    1 
ATOM   4323 N  N     . THR A 1 524 ? 59.517  17.342  20.725  1.00 72.12  ? 524 THR A N     1 
ATOM   4324 C  CA    . THR A 1 524 ? 59.458  17.710  22.136  1.00 73.67  ? 524 THR A CA    1 
ATOM   4325 C  C     . THR A 1 524 ? 59.553  16.483  23.033  1.00 72.52  ? 524 THR A C     1 
ATOM   4326 O  O     . THR A 1 524 ? 60.268  16.495  24.043  1.00 83.75  ? 524 THR A O     1 
ATOM   4327 C  CB    . THR A 1 524 ? 58.163  18.474  22.410  1.00 77.03  ? 524 THR A CB    1 
ATOM   4328 O  OG1   . THR A 1 524 ? 57.837  19.281  21.273  1.00 72.38  ? 524 THR A OG1   1 
ATOM   4329 C  CG2   . THR A 1 524 ? 58.316  19.369  23.617  1.00 84.06  ? 524 THR A CG2   1 
ATOM   4330 N  N     . ILE A 1 525 ? 58.837  15.414  22.681  1.00 72.91  ? 525 ILE A N     1 
ATOM   4331 C  CA    . ILE A 1 525 ? 58.888  14.186  23.469  1.00 70.91  ? 525 ILE A CA    1 
ATOM   4332 C  C     . ILE A 1 525 ? 60.286  13.581  23.420  1.00 80.77  ? 525 ILE A C     1 
ATOM   4333 O  O     . ILE A 1 525 ? 60.788  13.054  24.421  1.00 81.98  ? 525 ILE A O     1 
ATOM   4334 C  CB    . ILE A 1 525 ? 57.815  13.200  22.973  1.00 72.30  ? 525 ILE A CB    1 
ATOM   4335 C  CG1   . ILE A 1 525 ? 56.437  13.619  23.493  1.00 68.08  ? 525 ILE A CG1   1 
ATOM   4336 C  CG2   . ILE A 1 525 ? 58.152  11.774  23.382  1.00 60.15  ? 525 ILE A CG2   1 
ATOM   4337 C  CD1   . ILE A 1 525 ? 55.293  13.162  22.625  1.00 53.20  ? 525 ILE A CD1   1 
ATOM   4338 N  N     . LYS A 1 526 ? 60.938  13.653  22.258  1.00 79.79  ? 526 LYS A N     1 
ATOM   4339 C  CA    . LYS A 1 526 ? 62.325  13.212  22.153  1.00 83.33  ? 526 LYS A CA    1 
ATOM   4340 C  C     . LYS A 1 526 ? 63.221  13.990  23.108  1.00 78.68  ? 526 LYS A C     1 
ATOM   4341 O  O     . LYS A 1 526 ? 64.018  13.404  23.850  1.00 82.34  ? 526 LYS A O     1 
ATOM   4342 C  CB    . LYS A 1 526 ? 62.813  13.371  20.712  1.00 91.89  ? 526 LYS A CB    1 
ATOM   4343 C  CG    . LYS A 1 526 ? 64.267  12.988  20.495  1.00 91.90  ? 526 LYS A CG    1 
ATOM   4344 C  CD    . LYS A 1 526 ? 64.480  12.369  19.122  1.00 102.91 ? 526 LYS A CD    1 
ATOM   4345 C  CE    . LYS A 1 526 ? 65.613  11.359  19.140  1.00 112.50 ? 526 LYS A CE    1 
ATOM   4346 N  NZ    . LYS A 1 526 ? 65.276  10.178  19.977  1.00 117.23 ? 526 LYS A NZ    1 
ATOM   4347 N  N     . GLU A 1 527 ? 63.097  15.320  23.104  1.00 82.70  ? 527 GLU A N     1 
ATOM   4348 C  CA    . GLU A 1 527 ? 63.964  16.157  23.928  1.00 79.63  ? 527 GLU A CA    1 
ATOM   4349 C  C     . GLU A 1 527 ? 63.750  15.885  25.412  1.00 82.00  ? 527 GLU A C     1 
ATOM   4350 O  O     . GLU A 1 527 ? 64.713  15.740  26.173  1.00 90.64  ? 527 GLU A O     1 
ATOM   4351 C  CB    . GLU A 1 527 ? 63.715  17.633  23.616  1.00 80.39  ? 527 GLU A CB    1 
ATOM   4352 C  CG    . GLU A 1 527 ? 63.986  18.028  22.174  1.00 80.22  ? 527 GLU A CG    1 
ATOM   4353 C  CD    . GLU A 1 527 ? 65.454  17.944  21.813  1.00 102.32 ? 527 GLU A CD    1 
ATOM   4354 O  OE1   . GLU A 1 527 ? 66.298  18.266  22.676  1.00 92.94  ? 527 GLU A OE1   1 
ATOM   4355 O  OE2   . GLU A 1 527 ? 65.764  17.562  20.665  1.00 104.08 ? 527 GLU A OE2   1 
ATOM   4356 N  N     . ILE A 1 528 ? 62.489  15.806  25.841  1.00 84.78  ? 528 ILE A N     1 
ATOM   4357 C  CA    . ILE A 1 528 ? 62.206  15.693  27.268  1.00 82.37  ? 528 ILE A CA    1 
ATOM   4358 C  C     . ILE A 1 528 ? 62.644  14.336  27.810  1.00 80.17  ? 528 ILE A C     1 
ATOM   4359 O  O     . ILE A 1 528 ? 62.990  14.216  28.992  1.00 85.26  ? 528 ILE A O     1 
ATOM   4360 C  CB    . ILE A 1 528 ? 60.713  15.965  27.535  1.00 79.96  ? 528 ILE A CB    1 
ATOM   4361 C  CG1   . ILE A 1 528 ? 60.454  16.092  29.035  1.00 77.80  ? 528 ILE A CG1   1 
ATOM   4362 C  CG2   . ILE A 1 528 ? 59.842  14.872  26.935  1.00 82.38  ? 528 ILE A CG2   1 
ATOM   4363 C  CD1   . ILE A 1 528 ? 59.203  16.851  29.385  1.00 70.95  ? 528 ILE A CD1   1 
ATOM   4364 N  N     . GLU A 1 529 ? 62.657  13.301  26.967  1.00 81.02  ? 529 GLU A N     1 
ATOM   4365 C  CA    . GLU A 1 529 ? 63.061  11.978  27.427  1.00 78.04  ? 529 GLU A CA    1 
ATOM   4366 C  C     . GLU A 1 529 ? 64.572  11.790  27.384  1.00 94.56  ? 529 GLU A C     1 
ATOM   4367 O  O     . GLU A 1 529 ? 65.129  11.100  28.245  1.00 85.81  ? 529 GLU A O     1 
ATOM   4368 C  CB    . GLU A 1 529 ? 62.383  10.892  26.589  1.00 78.52  ? 529 GLU A CB    1 
ATOM   4369 C  CG    . GLU A 1 529 ? 60.920  10.662  26.929  1.00 82.59  ? 529 GLU A CG    1 
ATOM   4370 C  CD    . GLU A 1 529 ? 60.335  9.457   26.215  1.00 89.64  ? 529 GLU A CD    1 
ATOM   4371 O  OE1   . GLU A 1 529 ? 60.533  9.339   24.988  1.00 85.73  ? 529 GLU A OE1   1 
ATOM   4372 O  OE2   . GLU A 1 529 ? 59.678  8.629   26.881  1.00 81.68  ? 529 GLU A OE2   1 
ATOM   4373 N  N     . GLU A 1 530 ? 65.246  12.387  26.403  1.00 88.06  ? 530 GLU A N     1 
ATOM   4374 C  CA    . GLU A 1 530 ? 66.683  12.200  26.250  1.00 92.73  ? 530 GLU A CA    1 
ATOM   4375 C  C     . GLU A 1 530 ? 67.486  13.276  26.973  1.00 99.22  ? 530 GLU A C     1 
ATOM   4376 O  O     . GLU A 1 530 ? 68.452  12.965  27.677  1.00 106.72 ? 530 GLU A O     1 
ATOM   4377 C  CB    . GLU A 1 530 ? 67.051  12.174  24.764  1.00 90.77  ? 530 GLU A CB    1 
ATOM   4378 C  CG    . GLU A 1 530 ? 66.598  10.917  24.046  1.00 101.32 ? 530 GLU A CG    1 
ATOM   4379 C  CD    . GLU A 1 530 ? 66.900  10.951  22.563  1.00 120.14 ? 530 GLU A CD    1 
ATOM   4380 O  OE1   . GLU A 1 530 ? 67.392  11.992  22.077  1.00 97.65  ? 530 GLU A OE1   1 
ATOM   4381 O  OE2   . GLU A 1 530 ? 66.651  9.933   21.885  1.00 122.60 ? 530 GLU A OE2   1 
ATOM   4382 N  N     . LYS A 1 531 ? 67.104  14.540  26.810  1.00 88.65  ? 531 LYS A N     1 
ATOM   4383 C  CA    . LYS A 1 531 ? 67.845  15.641  27.408  1.00 92.06  ? 531 LYS A CA    1 
ATOM   4384 C  C     . LYS A 1 531 ? 67.417  15.951  28.836  1.00 96.93  ? 531 LYS A C     1 
ATOM   4385 O  O     . LYS A 1 531 ? 68.074  16.762  29.498  1.00 97.08  ? 531 LYS A O     1 
ATOM   4386 C  CB    . LYS A 1 531 ? 67.705  16.903  26.548  1.00 91.84  ? 531 LYS A CB    1 
ATOM   4387 C  CG    . LYS A 1 531 ? 68.839  17.111  25.552  1.00 104.82 ? 531 LYS A CG    1 
ATOM   4388 C  CD    . LYS A 1 531 ? 68.787  16.095  24.421  1.00 114.27 ? 531 LYS A CD    1 
ATOM   4389 C  CE    . LYS A 1 531 ? 69.247  16.702  23.104  1.00 116.03 ? 531 LYS A CE    1 
ATOM   4390 N  NZ    . LYS A 1 531 ? 69.369  15.671  22.036  1.00 114.55 ? 531 LYS A NZ    1 
ATOM   4391 N  N     . TYR A 1 532 ? 66.346  15.332  29.332  1.00 103.24 ? 532 TYR A N     1 
ATOM   4392 C  CA    . TYR A 1 532 ? 65.890  15.608  30.689  1.00 91.95  ? 532 TYR A CA    1 
ATOM   4393 C  C     . TYR A 1 532 ? 65.477  14.374  31.476  1.00 90.93  ? 532 TYR A C     1 
ATOM   4394 O  O     . TYR A 1 532 ? 65.197  14.506  32.671  1.00 92.91  ? 532 TYR A O     1 
ATOM   4395 C  CB    . TYR A 1 532 ? 64.723  16.603  30.665  1.00 85.17  ? 532 TYR A CB    1 
ATOM   4396 C  CG    . TYR A 1 532 ? 65.174  18.042  30.579  1.00 83.94  ? 532 TYR A CG    1 
ATOM   4397 C  CD1   . TYR A 1 532 ? 65.498  18.758  31.724  1.00 92.80  ? 532 TYR A CD1   1 
ATOM   4398 C  CD2   . TYR A 1 532 ? 65.295  18.680  29.352  1.00 86.04  ? 532 TYR A CD2   1 
ATOM   4399 C  CE1   . TYR A 1 532 ? 65.917  20.073  31.650  1.00 92.21  ? 532 TYR A CE1   1 
ATOM   4400 C  CE2   . TYR A 1 532 ? 65.714  19.994  29.267  1.00 87.86  ? 532 TYR A CE2   1 
ATOM   4401 C  CZ    . TYR A 1 532 ? 66.024  20.686  30.419  1.00 85.48  ? 532 TYR A CZ    1 
ATOM   4402 O  OH    . TYR A 1 532 ? 66.441  21.995  30.338  1.00 90.67  ? 532 TYR A OH    1 
ATOM   4403 N  N     . GLY A 1 533 ? 65.424  13.193  30.865  1.00 86.54  ? 533 GLY A N     1 
ATOM   4404 C  CA    . GLY A 1 533 ? 65.200  11.972  31.611  1.00 85.47  ? 533 GLY A CA    1 
ATOM   4405 C  C     . GLY A 1 533 ? 63.762  11.650  31.939  1.00 94.15  ? 533 GLY A C     1 
ATOM   4406 O  O     . GLY A 1 533 ? 63.515  10.827  32.827  1.00 94.19  ? 533 GLY A O     1 
ATOM   4407 N  N     . PHE A 1 534 ? 62.801  12.267  31.256  1.00 89.44  ? 534 PHE A N     1 
ATOM   4408 C  CA    . PHE A 1 534 ? 61.400  11.971  31.505  1.00 81.71  ? 534 PHE A CA    1 
ATOM   4409 C  C     . PHE A 1 534 ? 60.996  10.665  30.823  1.00 88.21  ? 534 PHE A C     1 
ATOM   4410 O  O     . PHE A 1 534 ? 61.725  10.105  30.001  1.00 84.81  ? 534 PHE A O     1 
ATOM   4411 C  CB    . PHE A 1 534 ? 60.504  13.108  31.011  1.00 88.07  ? 534 PHE A CB    1 
ATOM   4412 C  CG    . PHE A 1 534 ? 60.454  14.300  31.931  1.00 97.10  ? 534 PHE A CG    1 
ATOM   4413 C  CD1   . PHE A 1 534 ? 61.562  15.114  32.099  1.00 94.14  ? 534 PHE A CD1   1 
ATOM   4414 C  CD2   . PHE A 1 534 ? 59.293  14.607  32.626  1.00 97.17  ? 534 PHE A CD2   1 
ATOM   4415 C  CE1   . PHE A 1 534 ? 61.516  16.209  32.943  1.00 90.30  ? 534 PHE A CE1   1 
ATOM   4416 C  CE2   . PHE A 1 534 ? 59.241  15.702  33.473  1.00 88.02  ? 534 PHE A CE2   1 
ATOM   4417 C  CZ    . PHE A 1 534 ? 60.354  16.503  33.630  1.00 88.31  ? 534 PHE A CZ    1 
ATOM   4418 N  N     . LYS A 1 535 ? 59.811  10.177  31.184  1.00 95.19  ? 535 LYS A N     1 
ATOM   4419 C  CA    . LYS A 1 535 ? 59.170  9.061   30.494  1.00 90.89  ? 535 LYS A CA    1 
ATOM   4420 C  C     . LYS A 1 535 ? 57.759  9.498   30.135  1.00 87.19  ? 535 LYS A C     1 
ATOM   4421 O  O     . LYS A 1 535 ? 56.930  9.724   31.023  1.00 90.05  ? 535 LYS A O     1 
ATOM   4422 C  CB    . LYS A 1 535 ? 59.150  7.795   31.350  1.00 90.38  ? 535 LYS A CB    1 
ATOM   4423 C  CG    . LYS A 1 535 ? 58.481  6.610   30.660  1.00 84.64  ? 535 LYS A CG    1 
ATOM   4424 C  CD    . LYS A 1 535 ? 59.353  6.065   29.535  1.00 105.96 ? 535 LYS A CD    1 
ATOM   4425 C  CE    . LYS A 1 535 ? 58.737  4.830   28.891  1.00 92.60  ? 535 LYS A CE    1 
ATOM   4426 N  NZ    . LYS A 1 535 ? 58.133  5.142   27.564  1.00 90.73  ? 535 LYS A NZ    1 
ATOM   4427 N  N     . VAL A 1 536 ? 57.491  9.628   28.839  1.00 80.34  ? 536 VAL A N     1 
ATOM   4428 C  CA    . VAL A 1 536 ? 56.185  10.088  28.385  1.00 83.53  ? 536 VAL A CA    1 
ATOM   4429 C  C     . VAL A 1 536 ? 55.172  8.965   28.565  1.00 78.94  ? 536 VAL A C     1 
ATOM   4430 O  O     . VAL A 1 536 ? 55.288  7.897   27.952  1.00 81.25  ? 536 VAL A O     1 
ATOM   4431 C  CB    . VAL A 1 536 ? 56.250  10.560  26.929  1.00 74.51  ? 536 VAL A CB    1 
ATOM   4432 C  CG1   . VAL A 1 536 ? 54.857  10.882  26.420  1.00 68.16  ? 536 VAL A CG1   1 
ATOM   4433 C  CG2   . VAL A 1 536 ? 57.159  11.774  26.820  1.00 63.96  ? 536 VAL A CG2   1 
ATOM   4434 N  N     . ILE A 1 537 ? 54.171  9.206   29.412  1.00 72.67  ? 537 ILE A N     1 
ATOM   4435 C  CA    . ILE A 1 537 ? 53.177  8.182   29.713  1.00 75.12  ? 537 ILE A CA    1 
ATOM   4436 C  C     . ILE A 1 537 ? 52.141  8.085   28.602  1.00 74.36  ? 537 ILE A C     1 
ATOM   4437 O  O     . ILE A 1 537 ? 51.790  6.986   28.159  1.00 67.06  ? 537 ILE A O     1 
ATOM   4438 C  CB    . ILE A 1 537 ? 52.521  8.475   31.074  1.00 77.14  ? 537 ILE A CB    1 
ATOM   4439 C  CG1   . ILE A 1 537 ? 53.553  8.368   32.197  1.00 79.39  ? 537 ILE A CG1   1 
ATOM   4440 C  CG2   . ILE A 1 537 ? 51.350  7.535   31.317  1.00 71.54  ? 537 ILE A CG2   1 
ATOM   4441 C  CD1   . ILE A 1 537 ? 53.406  9.437   33.252  1.00 78.16  ? 537 ILE A CD1   1 
ATOM   4442 N  N     . TYR A 1 538 ? 51.633  9.225   28.141  1.00 72.97  ? 538 TYR A N     1 
ATOM   4443 C  CA    . TYR A 1 538 ? 50.614  9.253   27.103  1.00 64.84  ? 538 TYR A CA    1 
ATOM   4444 C  C     . TYR A 1 538 ? 50.674  10.602  26.404  1.00 70.07  ? 538 TYR A C     1 
ATOM   4445 O  O     . TYR A 1 538 ? 51.039  11.612  27.011  1.00 66.32  ? 538 TYR A O     1 
ATOM   4446 C  CB    . TYR A 1 538 ? 49.219  9.003   27.685  1.00 60.69  ? 538 TYR A CB    1 
ATOM   4447 C  CG    . TYR A 1 538 ? 48.095  9.098   26.681  1.00 64.83  ? 538 TYR A CG    1 
ATOM   4448 C  CD1   . TYR A 1 538 ? 48.128  8.369   25.500  1.00 63.58  ? 538 TYR A CD1   1 
ATOM   4449 C  CD2   . TYR A 1 538 ? 46.994  9.908   26.920  1.00 65.44  ? 538 TYR A CD2   1 
ATOM   4450 C  CE1   . TYR A 1 538 ? 47.098  8.448   24.582  1.00 69.50  ? 538 TYR A CE1   1 
ATOM   4451 C  CE2   . TYR A 1 538 ? 45.959  9.995   26.009  1.00 66.02  ? 538 TYR A CE2   1 
ATOM   4452 C  CZ    . TYR A 1 538 ? 46.016  9.263   24.843  1.00 69.37  ? 538 TYR A CZ    1 
ATOM   4453 O  OH    . TYR A 1 538 ? 44.985  9.348   23.935  1.00 70.86  ? 538 TYR A OH    1 
ATOM   4454 N  N     . SER A 1 539 ? 50.312  10.607  25.124  1.00 66.05  ? 539 SER A N     1 
ATOM   4455 C  CA    . SER A 1 539 ? 50.369  11.821  24.322  1.00 64.83  ? 539 SER A CA    1 
ATOM   4456 C  C     . SER A 1 539 ? 49.319  11.756  23.226  1.00 64.84  ? 539 SER A C     1 
ATOM   4457 O  O     . SER A 1 539 ? 49.262  10.776  22.477  1.00 73.87  ? 539 SER A O     1 
ATOM   4458 C  CB    . SER A 1 539 ? 51.758  12.006  23.704  1.00 53.52  ? 539 SER A CB    1 
ATOM   4459 O  OG    . SER A 1 539 ? 51.799  13.168  22.894  1.00 69.04  ? 539 SER A OG    1 
ATOM   4460 N  N     . ASP A 1 540 ? 48.502  12.796  23.129  1.00 56.21  ? 540 ASP A N     1 
ATOM   4461 C  CA    . ASP A 1 540 ? 47.543  12.940  22.046  1.00 69.37  ? 540 ASP A CA    1 
ATOM   4462 C  C     . ASP A 1 540 ? 48.100  13.965  21.039  1.00 61.52  ? 540 ASP A C     1 
ATOM   4463 O  O     . ASP A 1 540 ? 49.290  13.880  20.736  1.00 86.06  ? 540 ASP A O     1 
ATOM   4464 C  CB    . ASP A 1 540 ? 46.163  13.271  22.610  1.00 77.66  ? 540 ASP A CB    1 
ATOM   4465 C  CG    . ASP A 1 540 ? 45.033  12.708  21.758  1.00 71.26  ? 540 ASP A CG    1 
ATOM   4466 O  OD1   . ASP A 1 540 ? 45.078  12.866  20.517  1.00 57.44  ? 540 ASP A OD1   1 
ATOM   4467 O  OD2   . ASP A 1 540 ? 44.097  12.110  22.331  1.00 70.07  ? 540 ASP A OD2   1 
ATOM   4468 N  N     . THR A 1 541 ? 47.318  14.920  20.549  1.00 54.25  ? 541 THR A N     1 
ATOM   4469 C  CA    . THR A 1 541 ? 47.721  15.653  19.354  1.00 66.41  ? 541 THR A CA    1 
ATOM   4470 C  C     . THR A 1 541 ? 48.677  16.800  19.668  1.00 70.95  ? 541 THR A C     1 
ATOM   4471 O  O     . THR A 1 541 ? 49.612  17.055  18.900  1.00 49.48  ? 541 THR A O     1 
ATOM   4472 C  CB    . THR A 1 541 ? 46.477  16.166  18.626  1.00 67.69  ? 541 THR A CB    1 
ATOM   4473 O  OG1   . THR A 1 541 ? 45.665  15.047  18.242  1.00 74.56  ? 541 THR A OG1   1 
ATOM   4474 C  CG2   . THR A 1 541 ? 46.860  16.954  17.386  1.00 55.37  ? 541 THR A CG2   1 
ATOM   4475 N  N     . ASP A 1 542 ? 48.473  17.498  20.783  1.00 77.06  ? 542 ASP A N     1 
ATOM   4476 C  CA    . ASP A 1 542 ? 49.209  18.724  21.054  1.00 57.74  ? 542 ASP A CA    1 
ATOM   4477 C  C     . ASP A 1 542 ? 49.992  18.705  22.359  1.00 58.73  ? 542 ASP A C     1 
ATOM   4478 O  O     . ASP A 1 542 ? 50.644  19.705  22.682  1.00 66.11  ? 542 ASP A O     1 
ATOM   4479 C  CB    . ASP A 1 542 ? 48.249  19.917  21.070  1.00 55.44  ? 542 ASP A CB    1 
ATOM   4480 C  CG    . ASP A 1 542 ? 47.145  19.755  22.092  1.00 72.63  ? 542 ASP A CG    1 
ATOM   4481 O  OD1   . ASP A 1 542 ? 46.914  18.619  22.558  1.00 68.23  ? 542 ASP A OD1   1 
ATOM   4482 O  OD2   . ASP A 1 542 ? 46.521  20.771  22.441  1.00 72.28  ? 542 ASP A OD2   1 
ATOM   4483 N  N     . GLY A 1 543 ? 49.945  17.616  23.120  1.00 61.10  ? 543 GLY A N     1 
ATOM   4484 C  CA    . GLY A 1 543 ? 50.627  17.581  24.397  1.00 57.65  ? 543 GLY A CA    1 
ATOM   4485 C  C     . GLY A 1 543 ? 50.860  16.155  24.842  1.00 57.69  ? 543 GLY A C     1 
ATOM   4486 O  O     . GLY A 1 543 ? 50.549  15.199  24.129  1.00 62.59  ? 543 GLY A O     1 
ATOM   4487 N  N     . PHE A 1 544 ? 51.413  16.021  26.046  1.00 59.28  ? 544 PHE A N     1 
ATOM   4488 C  CA    . PHE A 1 544 ? 51.750  14.704  26.563  1.00 65.79  ? 544 PHE A CA    1 
ATOM   4489 C  C     . PHE A 1 544 ? 51.765  14.734  28.083  1.00 68.41  ? 544 PHE A C     1 
ATOM   4490 O  O     . PHE A 1 544 ? 51.934  15.786  28.705  1.00 66.68  ? 544 PHE A O     1 
ATOM   4491 C  CB    . PHE A 1 544 ? 53.100  14.217  26.020  1.00 70.56  ? 544 PHE A CB    1 
ATOM   4492 C  CG    . PHE A 1 544 ? 54.244  15.153  26.294  1.00 54.14  ? 544 PHE A CG    1 
ATOM   4493 C  CD1   . PHE A 1 544 ? 54.961  15.065  27.474  1.00 60.42  ? 544 PHE A CD1   1 
ATOM   4494 C  CD2   . PHE A 1 544 ? 54.612  16.110  25.362  1.00 62.40  ? 544 PHE A CD2   1 
ATOM   4495 C  CE1   . PHE A 1 544 ? 56.016  15.922  27.727  1.00 77.07  ? 544 PHE A CE1   1 
ATOM   4496 C  CE2   . PHE A 1 544 ? 55.667  16.969  25.608  1.00 65.09  ? 544 PHE A CE2   1 
ATOM   4497 C  CZ    . PHE A 1 544 ? 56.369  16.875  26.792  1.00 66.36  ? 544 PHE A CZ    1 
ATOM   4498 N  N     . PHE A 1 545 ? 51.577  13.552  28.669  1.00 68.34  ? 545 PHE A N     1 
ATOM   4499 C  CA    . PHE A 1 545 ? 51.735  13.332  30.101  1.00 70.66  ? 545 PHE A CA    1 
ATOM   4500 C  C     . PHE A 1 545 ? 53.076  12.647  30.329  1.00 73.74  ? 545 PHE A C     1 
ATOM   4501 O  O     . PHE A 1 545 ? 53.343  11.590  29.746  1.00 75.54  ? 545 PHE A O     1 
ATOM   4502 C  CB    . PHE A 1 545 ? 50.601  12.471  30.658  1.00 66.53  ? 545 PHE A CB    1 
ATOM   4503 C  CG    . PHE A 1 545 ? 49.243  13.110  30.570  1.00 69.78  ? 545 PHE A CG    1 
ATOM   4504 C  CD1   . PHE A 1 545 ? 48.445  12.922  29.454  1.00 65.36  ? 545 PHE A CD1   1 
ATOM   4505 C  CD2   . PHE A 1 545 ? 48.757  13.882  31.613  1.00 71.91  ? 545 PHE A CD2   1 
ATOM   4506 C  CE1   . PHE A 1 545 ? 47.191  13.501  29.373  1.00 60.80  ? 545 PHE A CE1   1 
ATOM   4507 C  CE2   . PHE A 1 545 ? 47.503  14.463  31.538  1.00 71.90  ? 545 PHE A CE2   1 
ATOM   4508 C  CZ    . PHE A 1 545 ? 46.720  14.272  30.416  1.00 59.42  ? 545 PHE A CZ    1 
ATOM   4509 N  N     . ALA A 1 546 ? 53.915  13.241  31.174  1.00 72.61  ? 546 ALA A N     1 
ATOM   4510 C  CA    . ALA A 1 546 ? 55.248  12.712  31.413  1.00 78.38  ? 546 ALA A CA    1 
ATOM   4511 C  C     . ALA A 1 546 ? 55.576  12.787  32.897  1.00 84.64  ? 546 ALA A C     1 
ATOM   4512 O  O     . ALA A 1 546 ? 54.924  13.495  33.668  1.00 84.59  ? 546 ALA A O     1 
ATOM   4513 C  CB    . ALA A 1 546 ? 56.310  13.466  30.600  1.00 77.12  ? 546 ALA A CB    1 
ATOM   4514 N  N     . THR A 1 547 ? 56.605  12.036  33.283  1.00 90.89  ? 547 THR A N     1 
ATOM   4515 C  CA    . THR A 1 547 ? 57.102  12.040  34.650  1.00 89.38  ? 547 THR A CA    1 
ATOM   4516 C  C     . THR A 1 547 ? 58.544  11.561  34.637  1.00 95.75  ? 547 THR A C     1 
ATOM   4517 O  O     . THR A 1 547 ? 59.004  10.943  33.673  1.00 93.24  ? 547 THR A O     1 
ATOM   4518 C  CB    . THR A 1 547 ? 56.256  11.153  35.572  1.00 87.23  ? 547 THR A CB    1 
ATOM   4519 O  OG1   . THR A 1 547 ? 56.593  11.419  36.940  1.00 87.16  ? 547 THR A OG1   1 
ATOM   4520 C  CG2   . THR A 1 547 ? 56.509  9.682   35.275  1.00 86.64  ? 547 THR A CG2   1 
ATOM   4521 N  N     . ILE A 1 548 ? 59.257  11.875  35.716  1.00 103.74 ? 548 ILE A N     1 
ATOM   4522 C  CA    . ILE A 1 548 ? 60.583  11.321  35.972  1.00 107.47 ? 548 ILE A CA    1 
ATOM   4523 C  C     . ILE A 1 548 ? 60.382  9.993   36.698  1.00 106.83 ? 548 ILE A C     1 
ATOM   4524 O  O     . ILE A 1 548 ? 59.865  9.997   37.829  1.00 99.93  ? 548 ILE A O     1 
ATOM   4525 C  CB    . ILE A 1 548 ? 61.443  12.270  36.814  1.00 105.37 ? 548 ILE A CB    1 
ATOM   4526 C  CG1   . ILE A 1 548 ? 61.832  13.517  36.028  1.00 87.98  ? 548 ILE A CG1   1 
ATOM   4527 C  CG2   . ILE A 1 548 ? 62.729  11.571  37.203  1.00 99.41  ? 548 ILE A CG2   1 
ATOM   4528 C  CD1   . ILE A 1 548 ? 62.439  13.192  34.702  1.00 96.31  ? 548 ILE A CD1   1 
ATOM   4529 N  N     . PRO A 1 549 ? 60.757  8.852   36.100  1.00 104.87 ? 549 PRO A N     1 
ATOM   4530 C  CA    . PRO A 1 549 ? 60.520  7.558   36.760  1.00 92.19  ? 549 PRO A CA    1 
ATOM   4531 C  C     . PRO A 1 549 ? 61.062  7.519   38.180  1.00 113.84 ? 549 PRO A C     1 
ATOM   4532 O  O     . PRO A 1 549 ? 62.275  7.584   38.400  1.00 114.04 ? 549 PRO A O     1 
ATOM   4533 C  CB    . PRO A 1 549 ? 61.245  6.562   35.847  1.00 103.66 ? 549 PRO A CB    1 
ATOM   4534 C  CG    . PRO A 1 549 ? 61.265  7.232   34.512  1.00 91.03  ? 549 PRO A CG    1 
ATOM   4535 C  CD    . PRO A 1 549 ? 61.430  8.695   34.799  1.00 112.39 ? 549 PRO A CD    1 
ATOM   4536 N  N     . GLY A 1 550 ? 60.161  7.420   39.147  1.00 131.08 ? 550 GLY A N     1 
ATOM   4537 C  CA    . GLY A 1 550 ? 60.545  7.618   40.533  1.00 127.40 ? 550 GLY A CA    1 
ATOM   4538 C  C     . GLY A 1 550 ? 60.488  9.089   40.869  1.00 148.61 ? 550 GLY A C     1 
ATOM   4539 O  O     . GLY A 1 550 ? 59.497  9.766   40.576  1.00 149.75 ? 550 GLY A O     1 
ATOM   4540 N  N     . ALA A 1 551 ? 61.558  9.593   41.489  1.00 122.75 ? 551 ALA A N     1 
ATOM   4541 C  CA    . ALA A 1 551 ? 61.701  11.008  41.820  1.00 131.01 ? 551 ALA A CA    1 
ATOM   4542 C  C     . ALA A 1 551 ? 60.586  11.530  42.717  1.00 124.49 ? 551 ALA A C     1 
ATOM   4543 O  O     . ALA A 1 551 ? 59.726  10.768  43.173  1.00 136.49 ? 551 ALA A O     1 
ATOM   4544 C  CB    . ALA A 1 551 ? 61.769  11.857  40.551  1.00 118.13 ? 551 ALA A CB    1 
ATOM   4545 N  N     . ASP A 1 552 ? 60.592  12.837  42.957  1.00 125.16 ? 552 ASP A N     1 
ATOM   4546 C  CA    . ASP A 1 552 ? 59.687  13.489  43.886  1.00 126.33 ? 552 ASP A CA    1 
ATOM   4547 C  C     . ASP A 1 552 ? 58.859  14.508  43.108  1.00 117.23 ? 552 ASP A C     1 
ATOM   4548 O  O     . ASP A 1 552 ? 59.139  14.804  41.944  1.00 128.86 ? 552 ASP A O     1 
ATOM   4549 C  CB    . ASP A 1 552 ? 60.490  14.131  45.032  1.00 126.53 ? 552 ASP A CB    1 
ATOM   4550 C  CG    . ASP A 1 552 ? 59.625  14.870  46.035  1.00 133.32 ? 552 ASP A CG    1 
ATOM   4551 O  OD1   . ASP A 1 552 ? 58.381  14.781  45.950  1.00 134.94 ? 552 ASP A OD1   1 
ATOM   4552 O  OD2   . ASP A 1 552 ? 60.199  15.511  46.942  1.00 126.71 ? 552 ASP A OD2   1 
ATOM   4553 N  N     . ALA A 1 553 ? 57.814  15.031  43.757  1.00 110.30 ? 553 ALA A N     1 
ATOM   4554 C  CA    . ALA A 1 553 ? 56.894  15.948  43.090  1.00 112.44 ? 553 ALA A CA    1 
ATOM   4555 C  C     . ALA A 1 553 ? 57.629  17.159  42.528  1.00 117.70 ? 553 ALA A C     1 
ATOM   4556 O  O     . ALA A 1 553 ? 57.670  17.366  41.311  1.00 115.10 ? 553 ALA A O     1 
ATOM   4557 C  CB    . ALA A 1 553 ? 55.793  16.383  44.059  1.00 114.84 ? 553 ALA A CB    1 
ATOM   4558 N  N     . GLU A 1 554 ? 58.231  17.966  43.407  1.00 121.67 ? 554 GLU A N     1 
ATOM   4559 C  CA    . GLU A 1 554 ? 58.890  19.191  42.965  1.00 130.27 ? 554 GLU A CA    1 
ATOM   4560 C  C     . GLU A 1 554 ? 59.990  18.896  41.953  1.00 121.00 ? 554 GLU A C     1 
ATOM   4561 O  O     . GLU A 1 554 ? 60.133  19.619  40.962  1.00 125.65 ? 554 GLU A O     1 
ATOM   4562 C  CB    . GLU A 1 554 ? 59.456  19.970  44.158  1.00 122.17 ? 554 GLU A CB    1 
ATOM   4563 C  CG    . GLU A 1 554 ? 58.588  20.007  45.421  1.00 139.18 ? 554 GLU A CG    1 
ATOM   4564 C  CD    . GLU A 1 554 ? 58.542  18.684  46.158  1.00 151.27 ? 554 GLU A CD    1 
ATOM   4565 O  OE1   . GLU A 1 554 ? 59.343  17.791  45.815  1.00 145.53 ? 554 GLU A OE1   1 
ATOM   4566 O  OE2   . GLU A 1 554 ? 57.703  18.536  47.072  1.00 161.87 ? 554 GLU A OE2   1 
ATOM   4567 N  N     . THR A 1 555 ? 60.768  17.832  42.178  1.00 102.29 ? 555 THR A N     1 
ATOM   4568 C  CA    . THR A 1 555 ? 61.777  17.429  41.200  1.00 104.72 ? 555 THR A CA    1 
ATOM   4569 C  C     . THR A 1 555 ? 61.176  17.304  39.805  1.00 105.37 ? 555 THR A C     1 
ATOM   4570 O  O     . THR A 1 555 ? 61.763  17.767  38.820  1.00 107.22 ? 555 THR A O     1 
ATOM   4571 C  CB    . THR A 1 555 ? 62.415  16.105  41.619  1.00 105.01 ? 555 THR A CB    1 
ATOM   4572 O  OG1   . THR A 1 555 ? 63.051  16.256  42.894  1.00 102.66 ? 555 THR A OG1   1 
ATOM   4573 C  CG2   . THR A 1 555 ? 63.442  15.663  40.590  1.00 99.79  ? 555 THR A CG2   1 
ATOM   4574 N  N     . VAL A 1 556 ? 59.993  16.697  39.708  1.00 112.19 ? 556 VAL A N     1 
ATOM   4575 C  CA    . VAL A 1 556 ? 59.312  16.603  38.422  1.00 99.50  ? 556 VAL A CA    1 
ATOM   4576 C  C     . VAL A 1 556 ? 58.901  17.988  37.934  1.00 92.08  ? 556 VAL A C     1 
ATOM   4577 O  O     . VAL A 1 556 ? 59.062  18.314  36.752  1.00 93.14  ? 556 VAL A O     1 
ATOM   4578 C  CB    . VAL A 1 556 ? 58.108  15.649  38.529  1.00 99.53  ? 556 VAL A CB    1 
ATOM   4579 C  CG1   . VAL A 1 556 ? 57.025  16.025  37.528  1.00 86.52  ? 556 VAL A CG1   1 
ATOM   4580 C  CG2   . VAL A 1 556 ? 58.556  14.209  38.324  1.00 97.24  ? 556 VAL A CG2   1 
ATOM   4581 N  N     . LYS A 1 557 ? 58.382  18.830  38.833  1.00 89.32  ? 557 LYS A N     1 
ATOM   4582 C  CA    . LYS A 1 557 ? 57.938  20.159  38.421  1.00 97.29  ? 557 LYS A CA    1 
ATOM   4583 C  C     . LYS A 1 557 ? 59.115  21.061  38.072  1.00 94.99  ? 557 LYS A C     1 
ATOM   4584 O  O     . LYS A 1 557 ? 59.032  21.851  37.125  1.00 94.41  ? 557 LYS A O     1 
ATOM   4585 C  CB    . LYS A 1 557 ? 57.080  20.802  39.512  1.00 100.08 ? 557 LYS A CB    1 
ATOM   4586 C  CG    . LYS A 1 557 ? 56.192  19.841  40.274  1.00 98.85  ? 557 LYS A CG    1 
ATOM   4587 C  CD    . LYS A 1 557 ? 54.875  20.498  40.664  1.00 102.99 ? 557 LYS A CD    1 
ATOM   4588 C  CE    . LYS A 1 557 ? 54.867  20.894  42.132  1.00 108.08 ? 557 LYS A CE    1 
ATOM   4589 N  NZ    . LYS A 1 557 ? 53.504  21.264  42.606  1.00 101.54 ? 557 LYS A NZ    1 
ATOM   4590 N  N     . LYS A 1 558 ? 60.216  20.963  38.821  1.00 104.87 ? 558 LYS A N     1 
ATOM   4591 C  CA    . LYS A 1 558 ? 61.350  21.844  38.560  1.00 101.25 ? 558 LYS A CA    1 
ATOM   4592 C  C     . LYS A 1 558 ? 62.003  21.516  37.224  1.00 99.56  ? 558 LYS A C     1 
ATOM   4593 O  O     . LYS A 1 558 ? 62.276  22.416  36.423  1.00 98.59  ? 558 LYS A O     1 
ATOM   4594 C  CB    . LYS A 1 558 ? 62.380  21.767  39.693  1.00 91.05  ? 558 LYS A CB    1 
ATOM   4595 C  CG    . LYS A 1 558 ? 61.931  22.051  41.155  1.00 104.96 ? 558 LYS A CG    1 
ATOM   4596 C  CD    . LYS A 1 558 ? 60.941  23.217  41.385  1.00 115.31 ? 558 LYS A CD    1 
ATOM   4597 C  CE    . LYS A 1 558 ? 59.469  22.851  41.158  1.00 112.77 ? 558 LYS A CE    1 
ATOM   4598 N  NZ    . LYS A 1 558 ? 58.552  24.014  41.307  1.00 116.43 ? 558 LYS A NZ    1 
ATOM   4599 N  N     . LYS A 1 559 ? 62.276  20.233  36.972  1.00 95.44  ? 559 LYS A N     1 
ATOM   4600 C  CA    . LYS A 1 559 ? 62.833  19.840  35.681  1.00 94.52  ? 559 LYS A CA    1 
ATOM   4601 C  C     . LYS A 1 559 ? 61.861  20.118  34.540  1.00 91.50  ? 559 LYS A C     1 
ATOM   4602 O  O     . LYS A 1 559 ? 62.288  20.436  33.423  1.00 95.73  ? 559 LYS A O     1 
ATOM   4603 C  CB    . LYS A 1 559 ? 63.217  18.360  35.705  1.00 99.88  ? 559 LYS A CB    1 
ATOM   4604 C  CG    . LYS A 1 559 ? 64.383  18.031  36.631  1.00 100.07 ? 559 LYS A CG    1 
ATOM   4605 C  CD    . LYS A 1 559 ? 65.525  19.025  36.470  1.00 93.03  ? 559 LYS A CD    1 
ATOM   4606 C  CE    . LYS A 1 559 ? 66.451  18.628  35.329  1.00 107.00 ? 559 LYS A CE    1 
ATOM   4607 N  NZ    . LYS A 1 559 ? 67.750  19.353  35.392  1.00 100.43 ? 559 LYS A NZ    1 
ATOM   4608 N  N     . ALA A 1 560 ? 60.555  20.007  34.797  1.00 93.94  ? 560 ALA A N     1 
ATOM   4609 C  CA    . ALA A 1 560 ? 59.574  20.301  33.756  1.00 91.84  ? 560 ALA A CA    1 
ATOM   4610 C  C     . ALA A 1 560 ? 59.616  21.771  33.361  1.00 89.42  ? 560 ALA A C     1 
ATOM   4611 O  O     . ALA A 1 560 ? 59.520  22.105  32.174  1.00 95.11  ? 560 ALA A O     1 
ATOM   4612 C  CB    . ALA A 1 560 ? 58.171  19.914  34.221  1.00 76.88  ? 560 ALA A CB    1 
ATOM   4613 N  N     . MET A 1 561 ? 59.759  22.666  34.341  1.00 87.74  ? 561 MET A N     1 
ATOM   4614 C  CA    . MET A 1 561 ? 59.851  24.087  34.026  1.00 89.42  ? 561 MET A CA    1 
ATOM   4615 C  C     . MET A 1 561 ? 61.179  24.415  33.354  1.00 100.48 ? 561 MET A C     1 
ATOM   4616 O  O     . MET A 1 561 ? 61.237  25.284  32.477  1.00 100.89 ? 561 MET A O     1 
ATOM   4617 C  CB    . MET A 1 561 ? 59.662  24.921  35.292  1.00 91.68  ? 561 MET A CB    1 
ATOM   4618 C  CG    . MET A 1 561 ? 58.318  24.711  35.972  1.00 100.75 ? 561 MET A CG    1 
ATOM   4619 S  SD    . MET A 1 561 ? 57.102  25.979  35.568  1.00 115.94 ? 561 MET A SD    1 
ATOM   4620 C  CE    . MET A 1 561 ? 56.062  25.924  37.026  1.00 112.33 ? 561 MET A CE    1 
ATOM   4621 N  N     . GLU A 1 562 ? 62.255  23.732  33.754  1.00 93.10  ? 562 GLU A N     1 
ATOM   4622 C  CA    . GLU A 1 562 ? 63.529  23.886  33.058  1.00 92.14  ? 562 GLU A CA    1 
ATOM   4623 C  C     . GLU A 1 562 ? 63.402  23.465  31.600  1.00 97.25  ? 562 GLU A C     1 
ATOM   4624 O  O     . GLU A 1 562 ? 63.868  24.167  30.694  1.00 100.81 ? 562 GLU A O     1 
ATOM   4625 C  CB    . GLU A 1 562 ? 64.616  23.068  33.755  1.00 91.65  ? 562 GLU A CB    1 
ATOM   4626 C  CG    . GLU A 1 562 ? 65.005  23.566  35.134  1.00 94.01  ? 562 GLU A CG    1 
ATOM   4627 C  CD    . GLU A 1 562 ? 66.104  22.727  35.760  1.00 107.56 ? 562 GLU A CD    1 
ATOM   4628 O  OE1   . GLU A 1 562 ? 66.733  21.932  35.031  1.00 104.09 ? 562 GLU A OE1   1 
ATOM   4629 O  OE2   . GLU A 1 562 ? 66.338  22.862  36.980  1.00 103.54 ? 562 GLU A OE2   1 
ATOM   4630 N  N     . PHE A 1 563 ? 62.770  22.314  31.358  1.00 94.41  ? 563 PHE A N     1 
ATOM   4631 C  CA    . PHE A 1 563 ? 62.577  21.844  29.990  1.00 85.81  ? 563 PHE A CA    1 
ATOM   4632 C  C     . PHE A 1 563 ? 61.767  22.840  29.171  1.00 88.61  ? 563 PHE A C     1 
ATOM   4633 O  O     . PHE A 1 563 ? 62.023  23.025  27.976  1.00 95.91  ? 563 PHE A O     1 
ATOM   4634 C  CB    . PHE A 1 563 ? 61.892  20.478  30.000  1.00 73.48  ? 563 PHE A CB    1 
ATOM   4635 C  CG    . PHE A 1 563 ? 61.423  20.032  28.649  1.00 77.51  ? 563 PHE A CG    1 
ATOM   4636 C  CD1   . PHE A 1 563 ? 62.324  19.556  27.713  1.00 78.58  ? 563 PHE A CD1   1 
ATOM   4637 C  CD2   . PHE A 1 563 ? 60.081  20.096  28.311  1.00 85.05  ? 563 PHE A CD2   1 
ATOM   4638 C  CE1   . PHE A 1 563 ? 61.897  19.150  26.467  1.00 90.76  ? 563 PHE A CE1   1 
ATOM   4639 C  CE2   . PHE A 1 563 ? 59.649  19.690  27.067  1.00 81.16  ? 563 PHE A CE2   1 
ATOM   4640 C  CZ    . PHE A 1 563 ? 60.559  19.215  26.145  1.00 84.69  ? 563 PHE A CZ    1 
ATOM   4641 N  N     . LEU A 1 564 ? 60.786  23.493  29.799  1.00 94.83  ? 564 LEU A N     1 
ATOM   4642 C  CA    . LEU A 1 564 ? 59.960  24.457  29.080  1.00 88.52  ? 564 LEU A CA    1 
ATOM   4643 C  C     . LEU A 1 564 ? 60.788  25.637  28.590  1.00 88.88  ? 564 LEU A C     1 
ATOM   4644 O  O     . LEU A 1 564 ? 60.628  26.086  27.450  1.00 95.85  ? 564 LEU A O     1 
ATOM   4645 C  CB    . LEU A 1 564 ? 58.815  24.934  29.972  1.00 89.91  ? 564 LEU A CB    1 
ATOM   4646 C  CG    . LEU A 1 564 ? 57.651  23.956  30.140  1.00 81.63  ? 564 LEU A CG    1 
ATOM   4647 C  CD1   . LEU A 1 564 ? 56.538  24.583  30.961  1.00 81.63  ? 564 LEU A CD1   1 
ATOM   4648 C  CD2   . LEU A 1 564 ? 57.130  23.505  28.786  1.00 76.24  ? 564 LEU A CD2   1 
ATOM   4649 N  N     . LYS A 1 565 ? 61.680  26.155  29.439  1.00 97.75  ? 565 LYS A N     1 
ATOM   4650 C  CA    . LYS A 1 565 ? 62.569  27.230  29.010  1.00 93.45  ? 565 LYS A CA    1 
ATOM   4651 C  C     . LYS A 1 565 ? 63.472  26.772  27.871  1.00 93.02  ? 565 LYS A C     1 
ATOM   4652 O  O     . LYS A 1 565 ? 63.716  27.524  26.919  1.00 93.64  ? 565 LYS A O     1 
ATOM   4653 C  CB    . LYS A 1 565 ? 63.403  27.724  30.192  1.00 92.68  ? 565 LYS A CB    1 
ATOM   4654 C  CG    . LYS A 1 565 ? 64.543  28.660  29.810  1.00 114.53 ? 565 LYS A CG    1 
ATOM   4655 C  CD    . LYS A 1 565 ? 64.729  29.764  30.841  1.00 114.94 ? 565 LYS A CD    1 
ATOM   4656 C  CE    . LYS A 1 565 ? 65.513  30.938  30.270  1.00 109.36 ? 565 LYS A CE    1 
ATOM   4657 N  NZ    . LYS A 1 565 ? 65.248  31.145  28.819  1.00 105.08 ? 565 LYS A NZ    1 
ATOM   4658 N  N     . TYR A 1 566 ? 63.969  25.535  27.947  1.00 89.91  ? 566 TYR A N     1 
ATOM   4659 C  CA    . TYR A 1 566 ? 64.843  25.021  26.898  1.00 93.74  ? 566 TYR A CA    1 
ATOM   4660 C  C     . TYR A 1 566 ? 64.085  24.811  25.594  1.00 94.13  ? 566 TYR A C     1 
ATOM   4661 O  O     . TYR A 1 566 ? 64.597  25.131  24.515  1.00 98.25  ? 566 TYR A O     1 
ATOM   4662 C  CB    . TYR A 1 566 ? 65.496  23.713  27.351  1.00 101.48 ? 566 TYR A CB    1 
ATOM   4663 C  CG    . TYR A 1 566 ? 66.009  22.861  26.210  1.00 110.46 ? 566 TYR A CG    1 
ATOM   4664 C  CD1   . TYR A 1 566 ? 67.217  23.152  25.589  1.00 90.77  ? 566 TYR A CD1   1 
ATOM   4665 C  CD2   . TYR A 1 566 ? 65.285  21.765  25.754  1.00 100.66 ? 566 TYR A CD2   1 
ATOM   4666 C  CE1   . TYR A 1 566 ? 67.689  22.377  24.545  1.00 85.67  ? 566 TYR A CE1   1 
ATOM   4667 C  CE2   . TYR A 1 566 ? 65.748  20.986  24.711  1.00 103.96 ? 566 TYR A CE2   1 
ATOM   4668 C  CZ    . TYR A 1 566 ? 66.951  21.296  24.110  1.00 109.87 ? 566 TYR A CZ    1 
ATOM   4669 O  OH    . TYR A 1 566 ? 67.418  20.523  23.071  1.00 117.73 ? 566 TYR A OH    1 
ATOM   4670 N  N     . ILE A 1 567 ? 62.867  24.274  25.668  1.00 91.82  ? 567 ILE A N     1 
ATOM   4671 C  CA    . ILE A 1 567 ? 62.160  23.923  24.443  1.00 79.21  ? 567 ILE A CA    1 
ATOM   4672 C  C     . ILE A 1 567 ? 61.472  25.140  23.827  1.00 88.97  ? 567 ILE A C     1 
ATOM   4673 O  O     . ILE A 1 567 ? 61.356  25.230  22.600  1.00 88.17  ? 567 ILE A O     1 
ATOM   4674 C  CB    . ILE A 1 567 ? 61.168  22.776  24.706  1.00 84.69  ? 567 ILE A CB    1 
ATOM   4675 C  CG1   . ILE A 1 567 ? 60.717  22.155  23.385  1.00 93.73  ? 567 ILE A CG1   1 
ATOM   4676 C  CG2   . ILE A 1 567 ? 59.968  23.255  25.510  1.00 81.82  ? 567 ILE A CG2   1 
ATOM   4677 C  CD1   . ILE A 1 567 ? 61.827  21.436  22.657  1.00 96.44  ? 567 ILE A CD1   1 
ATOM   4678 N  N     . ASN A 1 568 ? 61.022  26.096  24.643  1.00 88.00  ? 568 ASN A N     1 
ATOM   4679 C  CA    . ASN A 1 568 ? 60.383  27.285  24.092  1.00 75.57  ? 568 ASN A CA    1 
ATOM   4680 C  C     . ASN A 1 568 ? 61.387  28.225  23.443  1.00 81.41  ? 568 ASN A C     1 
ATOM   4681 O  O     . ASN A 1 568 ? 61.000  29.035  22.594  1.00 93.66  ? 568 ASN A O     1 
ATOM   4682 C  CB    . ASN A 1 568 ? 59.599  28.020  25.178  1.00 87.92  ? 568 ASN A CB    1 
ATOM   4683 C  CG    . ASN A 1 568 ? 58.201  27.465  25.360  1.00 83.20  ? 568 ASN A CG    1 
ATOM   4684 O  OD1   . ASN A 1 568 ? 57.706  26.711  24.522  1.00 72.26  ? 568 ASN A OD1   1 
ATOM   4685 N  ND2   . ASN A 1 568 ? 57.556  27.834  26.460  1.00 89.41  ? 568 ASN A ND2   1 
ATOM   4686 N  N     . ALA A 1 569 ? 62.663  28.138  23.824  1.00 95.99  ? 569 ALA A N     1 
ATOM   4687 C  CA    . ALA A 1 569 ? 63.700  28.894  23.134  1.00 93.31  ? 569 ALA A CA    1 
ATOM   4688 C  C     . ALA A 1 569 ? 64.096  28.234  21.821  1.00 93.72  ? 569 ALA A C     1 
ATOM   4689 O  O     . ALA A 1 569 ? 64.567  28.917  20.905  1.00 104.81 ? 569 ALA A O     1 
ATOM   4690 C  CB    . ALA A 1 569 ? 64.926  29.055  24.034  1.00 81.55  ? 569 ALA A CB    1 
ATOM   4691 N  N     . LYS A 1 570 ? 63.916  26.919  21.712  1.00 86.39  ? 570 LYS A N     1 
ATOM   4692 C  CA    . LYS A 1 570 ? 64.181  26.183  20.483  1.00 86.09  ? 570 LYS A CA    1 
ATOM   4693 C  C     . LYS A 1 570 ? 62.955  26.067  19.587  1.00 92.59  ? 570 LYS A C     1 
ATOM   4694 O  O     . LYS A 1 570 ? 63.058  25.503  18.492  1.00 91.70  ? 570 LYS A O     1 
ATOM   4695 C  CB    . LYS A 1 570 ? 64.706  24.780  20.807  1.00 75.75  ? 570 LYS A CB    1 
ATOM   4696 C  CG    . LYS A 1 570 ? 66.117  24.746  21.372  1.00 96.67  ? 570 LYS A CG    1 
ATOM   4697 C  CD    . LYS A 1 570 ? 66.744  23.369  21.205  1.00 99.91  ? 570 LYS A CD    1 
ATOM   4698 C  CE    . LYS A 1 570 ? 68.230  23.469  20.895  1.00 99.36  ? 570 LYS A CE    1 
ATOM   4699 N  NZ    . LYS A 1 570 ? 68.505  24.435  19.794  1.00 104.73 ? 570 LYS A NZ    1 
ATOM   4700 N  N     . LEU A 1 571 ? 61.801  26.581  20.019  1.00 85.19  ? 571 LEU A N     1 
ATOM   4701 C  CA    . LEU A 1 571 ? 60.581  26.437  19.235  1.00 80.33  ? 571 LEU A CA    1 
ATOM   4702 C  C     . LEU A 1 571 ? 60.364  27.670  18.376  1.00 83.25  ? 571 LEU A C     1 
ATOM   4703 O  O     . LEU A 1 571 ? 60.405  28.796  18.894  1.00 89.29  ? 571 LEU A O     1 
ATOM   4704 C  CB    . LEU A 1 571 ? 59.380  26.217  20.148  1.00 85.59  ? 571 LEU A CB    1 
ATOM   4705 C  CG    . LEU A 1 571 ? 59.056  24.748  20.424  1.00 71.75  ? 571 LEU A CG    1 
ATOM   4706 C  CD1   . LEU A 1 571 ? 58.111  24.623  21.606  1.00 76.64  ? 571 LEU A CD1   1 
ATOM   4707 C  CD2   . LEU A 1 571 ? 58.477  24.076  19.189  1.00 65.96  ? 571 LEU A CD2   1 
ATOM   4708 N  N     . PRO A 1 572 ? 60.123  27.499  17.076  1.00 72.71  ? 572 PRO A N     1 
ATOM   4709 C  CA    . PRO A 1 572 ? 60.117  28.646  16.154  1.00 69.45  ? 572 PRO A CA    1 
ATOM   4710 C  C     . PRO A 1 572 ? 58.863  29.495  16.307  1.00 84.64  ? 572 PRO A C     1 
ATOM   4711 O  O     . PRO A 1 572 ? 57.740  28.999  16.184  1.00 80.69  ? 572 PRO A O     1 
ATOM   4712 C  CB    . PRO A 1 572 ? 60.183  27.984  14.773  1.00 82.07  ? 572 PRO A CB    1 
ATOM   4713 C  CG    . PRO A 1 572 ? 59.555  26.643  14.980  1.00 78.77  ? 572 PRO A CG    1 
ATOM   4714 C  CD    . PRO A 1 572 ? 59.938  26.218  16.371  1.00 80.24  ? 572 PRO A CD    1 
ATOM   4715 N  N     . GLY A 1 573 ? 59.066  30.780  16.580  1.00 91.64  ? 573 GLY A N     1 
ATOM   4716 C  CA    . GLY A 1 573 ? 57.990  31.751  16.443  1.00 75.49  ? 573 GLY A CA    1 
ATOM   4717 C  C     . GLY A 1 573 ? 56.871  31.543  17.443  1.00 75.40  ? 573 GLY A C     1 
ATOM   4718 O  O     . GLY A 1 573 ? 57.095  31.411  18.652  1.00 82.55  ? 573 GLY A O     1 
ATOM   4719 N  N     . ALA A 1 574 ? 55.641  31.511  16.928  1.00 76.62  ? 574 ALA A N     1 
ATOM   4720 C  CA    . ALA A 1 574 ? 54.433  31.458  17.744  1.00 69.52  ? 574 ALA A CA    1 
ATOM   4721 C  C     . ALA A 1 574 ? 54.226  30.120  18.438  1.00 75.11  ? 574 ALA A C     1 
ATOM   4722 O  O     . ALA A 1 574 ? 53.195  29.945  19.097  1.00 80.48  ? 574 ALA A O     1 
ATOM   4723 C  CB    . ALA A 1 574 ? 53.212  31.777  16.880  1.00 77.28  ? 574 ALA A CB    1 
ATOM   4724 N  N     . LEU A 1 575 ? 55.156  29.181  18.313  1.00 61.94  ? 575 LEU A N     1 
ATOM   4725 C  CA    . LEU A 1 575 ? 55.012  27.867  18.922  1.00 67.78  ? 575 LEU A CA    1 
ATOM   4726 C  C     . LEU A 1 575 ? 55.542  27.895  20.347  1.00 70.74  ? 575 LEU A C     1 
ATOM   4727 O  O     . LEU A 1 575 ? 56.642  28.398  20.597  1.00 83.91  ? 575 LEU A O     1 
ATOM   4728 C  CB    . LEU A 1 575 ? 55.748  26.820  18.095  1.00 73.57  ? 575 LEU A CB    1 
ATOM   4729 C  CG    . LEU A 1 575 ? 55.078  26.591  16.746  1.00 83.66  ? 575 LEU A CG    1 
ATOM   4730 C  CD1   . LEU A 1 575 ? 55.952  25.719  15.900  1.00 75.61  ? 575 LEU A CD1   1 
ATOM   4731 C  CD2   . LEU A 1 575 ? 53.709  25.958  16.935  1.00 76.57  ? 575 LEU A CD2   1 
ATOM   4732 N  N     . GLU A 1 576 ? 54.762  27.349  21.275  1.00 79.47  ? 576 GLU A N     1 
ATOM   4733 C  CA    . GLU A 1 576 ? 55.096  27.452  22.685  1.00 87.12  ? 576 GLU A CA    1 
ATOM   4734 C  C     . GLU A 1 576 ? 54.440  26.309  23.447  1.00 78.63  ? 576 GLU A C     1 
ATOM   4735 O  O     . GLU A 1 576 ? 53.273  25.987  23.212  1.00 72.78  ? 576 GLU A O     1 
ATOM   4736 C  CB    . GLU A 1 576 ? 54.650  28.807  23.247  1.00 89.11  ? 576 GLU A CB    1 
ATOM   4737 C  CG    . GLU A 1 576 ? 54.343  28.813  24.731  1.00 102.61 ? 576 GLU A CG    1 
ATOM   4738 C  CD    . GLU A 1 576 ? 54.564  30.173  25.359  1.00 102.42 ? 576 GLU A CD    1 
ATOM   4739 O  OE1   . GLU A 1 576 ? 55.516  30.869  24.948  1.00 111.80 ? 576 GLU A OE1   1 
ATOM   4740 O  OE2   . GLU A 1 576 ? 53.781  30.548  26.257  1.00 105.38 ? 576 GLU A OE2   1 
ATOM   4741 N  N     . LEU A 1 577 ? 55.205  25.699  24.347  1.00 77.27  ? 577 LEU A N     1 
ATOM   4742 C  CA    . LEU A 1 577 ? 54.710  24.668  25.247  1.00 77.69  ? 577 LEU A CA    1 
ATOM   4743 C  C     . LEU A 1 577 ? 54.435  25.282  26.614  1.00 78.82  ? 577 LEU A C     1 
ATOM   4744 O  O     . LEU A 1 577 ? 55.212  26.109  27.099  1.00 83.00  ? 577 LEU A O     1 
ATOM   4745 C  CB    . LEU A 1 577 ? 55.728  23.533  25.379  1.00 74.89  ? 577 LEU A CB    1 
ATOM   4746 C  CG    . LEU A 1 577 ? 55.212  22.123  25.665  1.00 76.15  ? 577 LEU A CG    1 
ATOM   4747 C  CD1   . LEU A 1 577 ? 54.441  21.574  24.475  1.00 64.54  ? 577 LEU A CD1   1 
ATOM   4748 C  CD2   . LEU A 1 577 ? 56.370  21.209  26.027  1.00 59.03  ? 577 LEU A CD2   1 
ATOM   4749 N  N     . GLU A 1 578 ? 53.328  24.879  27.236  1.00 76.26  ? 578 GLU A N     1 
ATOM   4750 C  CA    . GLU A 1 578 ? 52.934  25.424  28.527  1.00 78.04  ? 578 GLU A CA    1 
ATOM   4751 C  C     . GLU A 1 578 ? 52.761  24.324  29.565  1.00 83.45  ? 578 GLU A C     1 
ATOM   4752 O  O     . GLU A 1 578 ? 52.433  23.178  29.242  1.00 93.31  ? 578 GLU A O     1 
ATOM   4753 C  CB    . GLU A 1 578 ? 51.629  26.226  28.438  1.00 83.52  ? 578 GLU A CB    1 
ATOM   4754 C  CG    . GLU A 1 578 ? 51.366  26.886  27.103  1.00 82.16  ? 578 GLU A CG    1 
ATOM   4755 C  CD    . GLU A 1 578 ? 49.946  27.398  26.996  1.00 91.40  ? 578 GLU A CD    1 
ATOM   4756 O  OE1   . GLU A 1 578 ? 49.031  26.728  27.520  1.00 94.42  ? 578 GLU A OE1   1 
ATOM   4757 O  OE2   . GLU A 1 578 ? 49.746  28.479  26.404  1.00 100.82 ? 578 GLU A OE2   1 
ATOM   4758 N  N     . TYR A 1 579 ? 52.983  24.702  30.822  1.00 78.34  ? 579 TYR A N     1 
ATOM   4759 C  CA    . TYR A 1 579 ? 52.729  23.844  31.975  1.00 79.66  ? 579 TYR A CA    1 
ATOM   4760 C  C     . TYR A 1 579 ? 51.244  23.923  32.305  1.00 80.71  ? 579 TYR A C     1 
ATOM   4761 O  O     . TYR A 1 579 ? 50.758  24.964  32.759  1.00 85.87  ? 579 TYR A O     1 
ATOM   4762 C  CB    . TYR A 1 579 ? 53.599  24.301  33.144  1.00 86.33  ? 579 TYR A CB    1 
ATOM   4763 C  CG    . TYR A 1 579 ? 53.439  23.549  34.448  1.00 92.92  ? 579 TYR A CG    1 
ATOM   4764 C  CD1   . TYR A 1 579 ? 52.374  23.811  35.302  1.00 88.40  ? 579 TYR A CD1   1 
ATOM   4765 C  CD2   . TYR A 1 579 ? 54.381  22.610  34.847  1.00 90.44  ? 579 TYR A CD2   1 
ATOM   4766 C  CE1   . TYR A 1 579 ? 52.237  23.138  36.500  1.00 82.06  ? 579 TYR A CE1   1 
ATOM   4767 C  CE2   . TYR A 1 579 ? 54.253  21.934  36.043  1.00 96.84  ? 579 TYR A CE2   1 
ATOM   4768 C  CZ    . TYR A 1 579 ? 53.179  22.202  36.866  1.00 89.86  ? 579 TYR A CZ    1 
ATOM   4769 O  OH    . TYR A 1 579 ? 53.050  21.531  38.059  1.00 87.24  ? 579 TYR A OH    1 
ATOM   4770 N  N     . GLU A 1 580 ? 50.513  22.831  32.076  1.00 73.82  ? 580 GLU A N     1 
ATOM   4771 C  CA    . GLU A 1 580 ? 49.060  22.839  32.206  1.00 77.18  ? 580 GLU A CA    1 
ATOM   4772 C  C     . GLU A 1 580 ? 48.557  22.038  33.401  1.00 79.38  ? 580 GLU A C     1 
ATOM   4773 O  O     . GLU A 1 580 ? 47.377  21.675  33.443  1.00 94.85  ? 580 GLU A O     1 
ATOM   4774 C  CB    . GLU A 1 580 ? 48.407  22.325  30.926  1.00 83.12  ? 580 GLU A CB    1 
ATOM   4775 C  CG    . GLU A 1 580 ? 47.115  23.034  30.603  1.00 90.75  ? 580 GLU A CG    1 
ATOM   4776 C  CD    . GLU A 1 580 ? 46.951  23.264  29.130  1.00 98.04  ? 580 GLU A CD    1 
ATOM   4777 O  OE1   . GLU A 1 580 ? 46.852  22.263  28.394  1.00 86.26  ? 580 GLU A OE1   1 
ATOM   4778 O  OE2   . GLU A 1 580 ? 46.926  24.441  28.717  1.00 98.35  ? 580 GLU A OE2   1 
ATOM   4779 N  N     . GLY A 1 581 ? 49.415  21.754  34.371  1.00 80.19  ? 581 GLY A N     1 
ATOM   4780 C  CA    . GLY A 1 581 ? 48.960  21.145  35.608  1.00 81.05  ? 581 GLY A CA    1 
ATOM   4781 C  C     . GLY A 1 581 ? 49.761  19.959  36.102  1.00 85.00  ? 581 GLY A C     1 
ATOM   4782 O  O     . GLY A 1 581 ? 50.293  19.164  35.323  1.00 84.60  ? 581 GLY A O     1 
ATOM   4783 N  N     . PHE A 1 582 ? 49.851  19.841  37.421  1.00 74.32  ? 582 PHE A N     1 
ATOM   4784 C  CA    . PHE A 1 582 ? 50.432  18.687  38.085  1.00 79.21  ? 582 PHE A CA    1 
ATOM   4785 C  C     . PHE A 1 582 ? 49.316  17.820  38.650  1.00 83.32  ? 582 PHE A C     1 
ATOM   4786 O  O     . PHE A 1 582 ? 48.256  18.317  39.039  1.00 85.92  ? 582 PHE A O     1 
ATOM   4787 C  CB    . PHE A 1 582 ? 51.378  19.121  39.205  1.00 75.72  ? 582 PHE A CB    1 
ATOM   4788 C  CG    . PHE A 1 582 ? 52.000  17.980  39.951  1.00 90.33  ? 582 PHE A CG    1 
ATOM   4789 C  CD1   . PHE A 1 582 ? 53.072  17.285  39.415  1.00 94.04  ? 582 PHE A CD1   1 
ATOM   4790 C  CD2   . PHE A 1 582 ? 51.514  17.602  41.190  1.00 97.77  ? 582 PHE A CD2   1 
ATOM   4791 C  CE1   . PHE A 1 582 ? 53.647  16.234  40.105  1.00 100.63 ? 582 PHE A CE1   1 
ATOM   4792 C  CE2   . PHE A 1 582 ? 52.083  16.554  41.884  1.00 103.08 ? 582 PHE A CE2   1 
ATOM   4793 C  CZ    . PHE A 1 582 ? 53.151  15.869  41.342  1.00 99.10  ? 582 PHE A CZ    1 
ATOM   4794 N  N     . TYR A 1 583 ? 49.562  16.514  38.691  1.00 78.20  ? 583 TYR A N     1 
ATOM   4795 C  CA    . TYR A 1 583 ? 48.553  15.562  39.137  1.00 83.43  ? 583 TYR A CA    1 
ATOM   4796 C  C     . TYR A 1 583 ? 49.216  14.516  40.018  1.00 92.51  ? 583 TYR A C     1 
ATOM   4797 O  O     . TYR A 1 583 ? 50.180  13.870  39.595  1.00 95.17  ? 583 TYR A O     1 
ATOM   4798 C  CB    . TYR A 1 583 ? 47.852  14.915  37.942  1.00 67.67  ? 583 TYR A CB    1 
ATOM   4799 C  CG    . TYR A 1 583 ? 47.209  15.924  37.012  1.00 75.66  ? 583 TYR A CG    1 
ATOM   4800 C  CD1   . TYR A 1 583 ? 46.075  16.628  37.398  1.00 78.65  ? 583 TYR A CD1   1 
ATOM   4801 C  CD2   . TYR A 1 583 ? 47.746  16.184  35.758  1.00 78.26  ? 583 TYR A CD2   1 
ATOM   4802 C  CE1   . TYR A 1 583 ? 45.489  17.558  36.558  1.00 74.40  ? 583 TYR A CE1   1 
ATOM   4803 C  CE2   . TYR A 1 583 ? 47.166  17.112  34.911  1.00 77.25  ? 583 TYR A CE2   1 
ATOM   4804 C  CZ    . TYR A 1 583 ? 46.038  17.796  35.317  1.00 80.95  ? 583 TYR A CZ    1 
ATOM   4805 O  OH    . TYR A 1 583 ? 45.456  18.719  34.478  1.00 84.11  ? 583 TYR A OH    1 
ATOM   4806 N  N     . LYS A 1 584 ? 48.699  14.364  41.241  1.00 84.42  ? 584 LYS A N     1 
ATOM   4807 C  CA    . LYS A 1 584 ? 49.281  13.433  42.204  1.00 83.66  ? 584 LYS A CA    1 
ATOM   4808 C  C     . LYS A 1 584 ? 49.387  12.030  41.622  1.00 91.99  ? 584 LYS A C     1 
ATOM   4809 O  O     . LYS A 1 584 ? 50.462  11.420  41.626  1.00 85.23  ? 584 LYS A O     1 
ATOM   4810 C  CB    . LYS A 1 584 ? 48.443  13.422  43.484  1.00 88.42  ? 584 LYS A CB    1 
ATOM   4811 C  CG    . LYS A 1 584 ? 49.254  13.487  44.769  1.00 101.87 ? 584 LYS A CG    1 
ATOM   4812 C  CD    . LYS A 1 584 ? 48.348  13.608  45.986  1.00 108.11 ? 584 LYS A CD    1 
ATOM   4813 C  CE    . LYS A 1 584 ? 47.989  12.240  46.548  1.00 107.97 ? 584 LYS A CE    1 
ATOM   4814 N  NZ    . LYS A 1 584 ? 47.246  12.344  47.836  1.00 106.06 ? 584 LYS A NZ    1 
ATOM   4815 N  N     . ARG A 1 585 ? 48.273  11.500  41.121  1.00 87.44  ? 585 ARG A N     1 
ATOM   4816 C  CA    . ARG A 1 585 ? 48.248  10.187  40.497  1.00 74.82  ? 585 ARG A CA    1 
ATOM   4817 C  C     . ARG A 1 585 ? 47.427  10.263  39.218  1.00 87.68  ? 585 ARG A C     1 
ATOM   4818 O  O     . ARG A 1 585 ? 46.709  11.235  38.969  1.00 80.81  ? 585 ARG A O     1 
ATOM   4819 C  CB    . ARG A 1 585 ? 47.674  9.119   41.438  1.00 82.44  ? 585 ARG A CB    1 
ATOM   4820 C  CG    . ARG A 1 585 ? 47.845  9.427   42.914  1.00 93.70  ? 585 ARG A CG    1 
ATOM   4821 C  CD    . ARG A 1 585 ? 47.030  8.485   43.781  1.00 93.24  ? 585 ARG A CD    1 
ATOM   4822 N  NE    . ARG A 1 585 ? 47.793  7.309   44.183  1.00 96.64  ? 585 ARG A NE    1 
ATOM   4823 C  CZ    . ARG A 1 585 ? 48.795  7.323   45.051  1.00 116.03 ? 585 ARG A CZ    1 
ATOM   4824 N  NH1   . ARG A 1 585 ? 49.186  8.441   45.641  1.00 114.35 ? 585 ARG A NH1   1 
ATOM   4825 N  NH2   . ARG A 1 585 ? 49.419  6.184   45.339  1.00 121.30 ? 585 ARG A NH2   1 
ATOM   4826 N  N     . GLY A 1 586 ? 47.540  9.217   38.405  1.00 93.88  ? 586 GLY A N     1 
ATOM   4827 C  CA    . GLY A 1 586 ? 46.789  9.137   37.169  1.00 84.54  ? 586 GLY A CA    1 
ATOM   4828 C  C     . GLY A 1 586 ? 46.746  7.735   36.601  1.00 84.76  ? 586 GLY A C     1 
ATOM   4829 O  O     . GLY A 1 586 ? 47.780  7.066   36.499  1.00 86.79  ? 586 GLY A O     1 
ATOM   4830 N  N     . PHE A 1 587 ? 45.554  7.272   36.237  1.00 82.30  ? 587 PHE A N     1 
ATOM   4831 C  CA    . PHE A 1 587 ? 45.384  5.971   35.605  1.00 75.07  ? 587 PHE A CA    1 
ATOM   4832 C  C     . PHE A 1 587 ? 45.170  6.171   34.111  1.00 77.51  ? 587 PHE A C     1 
ATOM   4833 O  O     . PHE A 1 587 ? 44.323  6.971   33.700  1.00 83.59  ? 587 PHE A O     1 
ATOM   4834 C  CB    . PHE A 1 587 ? 44.210  5.205   36.220  1.00 74.63  ? 587 PHE A CB    1 
ATOM   4835 C  CG    . PHE A 1 587 ? 44.210  3.736   35.897  1.00 76.23  ? 587 PHE A CG    1 
ATOM   4836 C  CD1   . PHE A 1 587 ? 43.919  3.291   34.619  1.00 84.23  ? 587 PHE A CD1   1 
ATOM   4837 C  CD2   . PHE A 1 587 ? 44.516  2.801   36.871  1.00 79.95  ? 587 PHE A CD2   1 
ATOM   4838 C  CE1   . PHE A 1 587 ? 43.925  1.943   34.317  1.00 83.72  ? 587 PHE A CE1   1 
ATOM   4839 C  CE2   . PHE A 1 587 ? 44.523  1.450   36.576  1.00 96.43  ? 587 PHE A CE2   1 
ATOM   4840 C  CZ    . PHE A 1 587 ? 44.228  1.022   35.296  1.00 91.44  ? 587 PHE A CZ    1 
ATOM   4841 N  N     . PHE A 1 588 ? 45.942  5.447   33.306  1.00 75.40  ? 588 PHE A N     1 
ATOM   4842 C  CA    . PHE A 1 588 ? 45.877  5.533   31.850  1.00 78.01  ? 588 PHE A CA    1 
ATOM   4843 C  C     . PHE A 1 588 ? 45.488  4.158   31.317  1.00 80.65  ? 588 PHE A C     1 
ATOM   4844 O  O     . PHE A 1 588 ? 46.334  3.268   31.192  1.00 80.27  ? 588 PHE A O     1 
ATOM   4845 C  CB    . PHE A 1 588 ? 47.205  6.021   31.276  1.00 71.37  ? 588 PHE A CB    1 
ATOM   4846 C  CG    . PHE A 1 588 ? 47.550  7.426   31.681  1.00 74.48  ? 588 PHE A CG    1 
ATOM   4847 C  CD1   . PHE A 1 588 ? 48.148  7.682   32.905  1.00 80.42  ? 588 PHE A CD1   1 
ATOM   4848 C  CD2   . PHE A 1 588 ? 47.255  8.494   30.851  1.00 70.22  ? 588 PHE A CD2   1 
ATOM   4849 C  CE1   . PHE A 1 588 ? 48.456  8.974   33.287  1.00 71.02  ? 588 PHE A CE1   1 
ATOM   4850 C  CE2   . PHE A 1 588 ? 47.561  9.790   31.228  1.00 58.29  ? 588 PHE A CE2   1 
ATOM   4851 C  CZ    . PHE A 1 588 ? 48.162  10.029  32.449  1.00 64.71  ? 588 PHE A CZ    1 
ATOM   4852 N  N     . VAL A 1 589 ? 44.200  3.989   31.013  1.00 84.55  ? 589 VAL A N     1 
ATOM   4853 C  CA    . VAL A 1 589 ? 43.697  2.700   30.548  1.00 87.93  ? 589 VAL A CA    1 
ATOM   4854 C  C     . VAL A 1 589 ? 44.110  2.452   29.104  1.00 78.61  ? 589 VAL A C     1 
ATOM   4855 O  O     . VAL A 1 589 ? 44.773  1.459   28.788  1.00 74.85  ? 589 VAL A O     1 
ATOM   4856 C  CB    . VAL A 1 589 ? 42.167  2.628   30.709  1.00 76.59  ? 589 VAL A CB    1 
ATOM   4857 C  CG1   . VAL A 1 589 ? 41.705  1.180   30.752  1.00 77.89  ? 589 VAL A CG1   1 
ATOM   4858 C  CG2   . VAL A 1 589 ? 41.718  3.376   31.953  1.00 78.81  ? 589 VAL A CG2   1 
ATOM   4859 N  N     . THR A 1 590 ? 43.724  3.349   28.205  1.00 71.84  ? 590 THR A N     1 
ATOM   4860 C  CA    . THR A 1 590 ? 43.999  3.166   26.787  1.00 75.99  ? 590 THR A CA    1 
ATOM   4861 C  C     . THR A 1 590 ? 43.960  4.530   26.112  1.00 78.72  ? 590 THR A C     1 
ATOM   4862 O  O     . THR A 1 590 ? 43.786  5.564   26.764  1.00 76.24  ? 590 THR A O     1 
ATOM   4863 C  CB    . THR A 1 590 ? 42.999  2.189   26.157  1.00 78.04  ? 590 THR A CB    1 
ATOM   4864 O  OG1   . THR A 1 590 ? 43.374  1.915   24.801  1.00 91.21  ? 590 THR A OG1   1 
ATOM   4865 C  CG2   . THR A 1 590 ? 41.601  2.768   26.194  1.00 71.52  ? 590 THR A CG2   1 
ATOM   4866 N  N     . LYS A 1 591 ? 44.143  4.524   24.795  1.00 71.05  ? 591 LYS A N     1 
ATOM   4867 C  CA    . LYS A 1 591 ? 44.097  5.762   24.030  1.00 72.19  ? 591 LYS A CA    1 
ATOM   4868 C  C     . LYS A 1 591 ? 42.751  6.450   24.223  1.00 68.97  ? 591 LYS A C     1 
ATOM   4869 O  O     . LYS A 1 591 ? 41.700  5.802   24.232  1.00 73.61  ? 591 LYS A O     1 
ATOM   4870 C  CB    . LYS A 1 591 ? 44.338  5.474   22.551  1.00 73.03  ? 591 LYS A CB    1 
ATOM   4871 C  CG    . LYS A 1 591 ? 45.784  5.165   22.209  1.00 73.46  ? 591 LYS A CG    1 
ATOM   4872 C  CD    . LYS A 1 591 ? 45.976  5.070   20.708  1.00 66.71  ? 591 LYS A CD    1 
ATOM   4873 C  CE    . LYS A 1 591 ? 47.431  4.853   20.342  1.00 66.83  ? 591 LYS A CE    1 
ATOM   4874 N  NZ    . LYS A 1 591 ? 47.576  4.536   18.896  1.00 65.15  ? 591 LYS A NZ    1 
ATOM   4875 N  N     . LYS A 1 592 ? 42.793  7.770   24.399  1.00 74.79  ? 592 LYS A N     1 
ATOM   4876 C  CA    . LYS A 1 592 ? 41.643  8.647   24.609  1.00 74.78  ? 592 LYS A CA    1 
ATOM   4877 C  C     . LYS A 1 592 ? 40.910  8.370   25.915  1.00 61.94  ? 592 LYS A C     1 
ATOM   4878 O  O     . LYS A 1 592 ? 39.924  9.057   26.210  1.00 69.99  ? 592 LYS A O     1 
ATOM   4879 C  CB    . LYS A 1 592 ? 40.631  8.569   23.457  1.00 63.19  ? 592 LYS A CB    1 
ATOM   4880 C  CG    . LYS A 1 592 ? 41.259  8.662   22.081  1.00 75.68  ? 592 LYS A CG    1 
ATOM   4881 C  CD    . LYS A 1 592 ? 41.518  10.105  21.695  1.00 58.83  ? 592 LYS A CD    1 
ATOM   4882 C  CE    . LYS A 1 592 ? 42.108  10.192  20.301  1.00 58.52  ? 592 LYS A CE    1 
ATOM   4883 N  NZ    . LYS A 1 592 ? 42.702  11.531  20.037  1.00 68.05  ? 592 LYS A NZ    1 
ATOM   4884 N  N     . LYS A 1 593 ? 41.354  7.399   26.713  1.00 65.95  ? 593 LYS A N     1 
ATOM   4885 C  CA    . LYS A 1 593 ? 40.644  6.979   27.917  1.00 71.78  ? 593 LYS A CA    1 
ATOM   4886 C  C     . LYS A 1 593 ? 41.614  6.961   29.092  1.00 80.60  ? 593 LYS A C     1 
ATOM   4887 O  O     . LYS A 1 593 ? 42.485  6.086   29.173  1.00 72.49  ? 593 LYS A O     1 
ATOM   4888 C  CB    . LYS A 1 593 ? 39.995  5.607   27.722  1.00 75.08  ? 593 LYS A CB    1 
ATOM   4889 C  CG    . LYS A 1 593 ? 38.726  5.629   26.880  1.00 75.54  ? 593 LYS A CG    1 
ATOM   4890 C  CD    . LYS A 1 593 ? 38.411  4.260   26.295  1.00 86.79  ? 593 LYS A CD    1 
ATOM   4891 C  CE    . LYS A 1 593 ? 36.916  3.981   26.288  1.00 80.24  ? 593 LYS A CE    1 
ATOM   4892 N  NZ    . LYS A 1 593 ? 36.370  3.961   24.902  1.00 77.73  ? 593 LYS A NZ    1 
ATOM   4893 N  N     . TYR A 1 594 ? 41.451  7.915   30.006  1.00 68.22  ? 594 TYR A N     1 
ATOM   4894 C  CA    . TYR A 1 594 ? 42.316  8.025   31.171  1.00 66.67  ? 594 TYR A CA    1 
ATOM   4895 C  C     . TYR A 1 594 ? 41.624  8.893   32.212  1.00 76.40  ? 594 TYR A C     1 
ATOM   4896 O  O     . TYR A 1 594 ? 40.688  9.637   31.906  1.00 72.60  ? 594 TYR A O     1 
ATOM   4897 C  CB    . TYR A 1 594 ? 43.685  8.608   30.802  1.00 66.51  ? 594 TYR A CB    1 
ATOM   4898 C  CG    . TYR A 1 594 ? 43.640  10.050  30.339  1.00 65.87  ? 594 TYR A CG    1 
ATOM   4899 C  CD1   . TYR A 1 594 ? 43.812  11.096  31.237  1.00 63.15  ? 594 TYR A CD1   1 
ATOM   4900 C  CD2   . TYR A 1 594 ? 43.415  10.363  29.005  1.00 59.80  ? 594 TYR A CD2   1 
ATOM   4901 C  CE1   . TYR A 1 594 ? 43.765  12.413  30.818  1.00 54.24  ? 594 TYR A CE1   1 
ATOM   4902 C  CE2   . TYR A 1 594 ? 43.367  11.678  28.577  1.00 60.91  ? 594 TYR A CE2   1 
ATOM   4903 C  CZ    . TYR A 1 594 ? 43.542  12.699  29.488  1.00 67.18  ? 594 TYR A CZ    1 
ATOM   4904 O  OH    . TYR A 1 594 ? 43.495  14.011  29.069  1.00 67.71  ? 594 TYR A OH    1 
ATOM   4905 N  N     . ALA A 1 595 ? 42.100  8.783   33.450  1.00 69.09  ? 595 ALA A N     1 
ATOM   4906 C  CA    . ALA A 1 595 ? 41.611  9.595   34.553  1.00 76.01  ? 595 ALA A CA    1 
ATOM   4907 C  C     . ALA A 1 595 ? 42.798  10.059  35.380  1.00 76.47  ? 595 ALA A C     1 
ATOM   4908 O  O     . ALA A 1 595 ? 43.790  9.339   35.525  1.00 72.40  ? 595 ALA A O     1 
ATOM   4909 C  CB    . ALA A 1 595 ? 40.618  8.828   35.433  1.00 76.53  ? 595 ALA A CB    1 
ATOM   4910 N  N     . VAL A 1 596 ? 42.691  11.270  35.923  1.00 68.18  ? 596 VAL A N     1 
ATOM   4911 C  CA    . VAL A 1 596 ? 43.815  11.901  36.600  1.00 83.95  ? 596 VAL A CA    1 
ATOM   4912 C  C     . VAL A 1 596 ? 43.277  12.777  37.724  1.00 84.66  ? 596 VAL A C     1 
ATOM   4913 O  O     . VAL A 1 596 ? 42.176  13.326  37.635  1.00 91.44  ? 596 VAL A O     1 
ATOM   4914 C  CB    . VAL A 1 596 ? 44.678  12.699  35.590  1.00 84.25  ? 596 VAL A CB    1 
ATOM   4915 C  CG1   . VAL A 1 596 ? 44.140  14.116  35.383  1.00 69.72  ? 596 VAL A CG1   1 
ATOM   4916 C  CG2   . VAL A 1 596 ? 46.132  12.697  36.003  1.00 88.96  ? 596 VAL A CG2   1 
ATOM   4917 N  N     . ILE A 1 597 ? 44.059  12.887  38.797  1.00 81.37  ? 597 ILE A N     1 
ATOM   4918 C  CA    . ILE A 1 597 ? 43.678  13.628  39.995  1.00 77.72  ? 597 ILE A CA    1 
ATOM   4919 C  C     . ILE A 1 597 ? 44.835  14.543  40.379  1.00 88.75  ? 597 ILE A C     1 
ATOM   4920 O  O     . ILE A 1 597 ? 45.994  14.115  40.382  1.00 88.84  ? 597 ILE A O     1 
ATOM   4921 C  CB    . ILE A 1 597 ? 43.309  12.683  41.158  1.00 86.52  ? 597 ILE A CB    1 
ATOM   4922 C  CG1   . ILE A 1 597 ? 42.814  13.475  42.369  1.00 91.32  ? 597 ILE A CG1   1 
ATOM   4923 C  CG2   . ILE A 1 597 ? 44.481  11.787  41.543  1.00 85.44  ? 597 ILE A CG2   1 
ATOM   4924 C  CD1   . ILE A 1 597 ? 42.187  12.610  43.440  1.00 86.06  ? 597 ILE A CD1   1 
ATOM   4925 N  N     . ASP A 1 598 ? 44.524  15.798  40.693  1.00 90.21  ? 598 ASP A N     1 
ATOM   4926 C  CA    . ASP A 1 598 ? 45.554  16.790  40.963  1.00 89.68  ? 598 ASP A CA    1 
ATOM   4927 C  C     . ASP A 1 598 ? 45.925  16.786  42.448  1.00 106.90 ? 598 ASP A C     1 
ATOM   4928 O  O     . ASP A 1 598 ? 45.596  15.861  43.196  1.00 104.37 ? 598 ASP A O     1 
ATOM   4929 C  CB    . ASP A 1 598 ? 45.104  18.168  40.468  1.00 94.69  ? 598 ASP A CB    1 
ATOM   4930 C  CG    . ASP A 1 598 ? 43.845  18.680  41.160  1.00 97.60  ? 598 ASP A CG    1 
ATOM   4931 O  OD1   . ASP A 1 598 ? 43.584  18.320  42.327  1.00 106.05 ? 598 ASP A OD1   1 
ATOM   4932 O  OD2   . ASP A 1 598 ? 43.110  19.463  40.523  1.00 92.93  ? 598 ASP A OD2   1 
ATOM   4933 N  N     . GLU A 1 599 ? 46.626  17.836  42.885  1.00 120.00 ? 599 GLU A N     1 
ATOM   4934 C  CA    . GLU A 1 599 ? 47.076  17.910  44.272  1.00 120.10 ? 599 GLU A CA    1 
ATOM   4935 C  C     . GLU A 1 599 ? 45.914  18.091  45.238  1.00 122.98 ? 599 GLU A C     1 
ATOM   4936 O  O     . GLU A 1 599 ? 45.979  17.617  46.378  1.00 117.91 ? 599 GLU A O     1 
ATOM   4937 C  CB    . GLU A 1 599 ? 48.073  19.058  44.439  1.00 133.87 ? 599 GLU A CB    1 
ATOM   4938 C  CG    . GLU A 1 599 ? 49.296  18.970  43.542  1.00 126.03 ? 599 GLU A CG    1 
ATOM   4939 C  CD    . GLU A 1 599 ? 50.515  19.629  44.159  1.00 136.62 ? 599 GLU A CD    1 
ATOM   4940 O  OE1   . GLU A 1 599 ? 50.360  20.701  44.782  1.00 147.97 ? 599 GLU A OE1   1 
ATOM   4941 O  OE2   . GLU A 1 599 ? 51.627  19.077  44.022  1.00 143.01 ? 599 GLU A OE2   1 
ATOM   4942 N  N     . GLU A 1 600 ? 44.852  18.768  44.810  1.00 118.26 ? 600 GLU A N     1 
ATOM   4943 C  CA    . GLU A 1 600 ? 43.740  19.108  45.688  1.00 117.86 ? 600 GLU A CA    1 
ATOM   4944 C  C     . GLU A 1 600 ? 42.628  18.067  45.684  1.00 111.42 ? 600 GLU A C     1 
ATOM   4945 O  O     . GLU A 1 600 ? 41.650  18.226  46.423  1.00 108.59 ? 600 GLU A O     1 
ATOM   4946 C  CB    . GLU A 1 600 ? 43.169  20.474  45.299  1.00 109.95 ? 600 GLU A CB    1 
ATOM   4947 C  CG    . GLU A 1 600 ? 42.875  21.377  46.482  1.00 122.56 ? 600 GLU A CG    1 
ATOM   4948 C  CD    . GLU A 1 600 ? 42.998  22.846  46.135  1.00 130.83 ? 600 GLU A CD    1 
ATOM   4949 O  OE1   . GLU A 1 600 ? 43.335  23.156  44.974  1.00 130.09 ? 600 GLU A OE1   1 
ATOM   4950 O  OE2   . GLU A 1 600 ? 42.762  23.691  47.024  1.00 134.29 ? 600 GLU A OE2   1 
ATOM   4951 N  N     . GLY A 1 601 ? 42.747  17.015  44.882  1.00 101.67 ? 601 GLY A N     1 
ATOM   4952 C  CA    . GLY A 1 601 ? 41.756  15.962  44.852  1.00 92.55  ? 601 GLY A CA    1 
ATOM   4953 C  C     . GLY A 1 601 ? 40.706  16.075  43.771  1.00 97.34  ? 601 GLY A C     1 
ATOM   4954 O  O     . GLY A 1 601 ? 39.723  15.326  43.812  1.00 102.45 ? 601 GLY A O     1 
ATOM   4955 N  N     . LYS A 1 602 ? 40.872  16.983  42.812  1.00 92.78  ? 602 LYS A N     1 
ATOM   4956 C  CA    . LYS A 1 602 ? 39.936  17.100  41.701  1.00 87.46  ? 602 LYS A CA    1 
ATOM   4957 C  C     . LYS A 1 602 ? 40.256  16.033  40.662  1.00 96.40  ? 602 LYS A C     1 
ATOM   4958 O  O     . LYS A 1 602 ? 41.340  16.043  40.067  1.00 92.82  ? 602 LYS A O     1 
ATOM   4959 C  CB    . LYS A 1 602 ? 40.008  18.494  41.082  1.00 90.61  ? 602 LYS A CB    1 
ATOM   4960 C  CG    . LYS A 1 602 ? 38.706  18.969  40.452  1.00 82.06  ? 602 LYS A CG    1 
ATOM   4961 C  CD    . LYS A 1 602 ? 38.945  19.569  39.075  1.00 84.26  ? 602 LYS A CD    1 
ATOM   4962 C  CE    . LYS A 1 602 ? 37.640  19.746  38.314  1.00 77.20  ? 602 LYS A CE    1 
ATOM   4963 N  NZ    . LYS A 1 602 ? 36.881  18.468  38.216  1.00 97.85  ? 602 LYS A NZ    1 
ATOM   4964 N  N     . ILE A 1 603 ? 39.319  15.115  40.445  1.00 89.62  ? 603 ILE A N     1 
ATOM   4965 C  CA    . ILE A 1 603 ? 39.510  14.026  39.495  1.00 85.87  ? 603 ILE A CA    1 
ATOM   4966 C  C     . ILE A 1 603 ? 38.955  14.459  38.145  1.00 83.08  ? 603 ILE A C     1 
ATOM   4967 O  O     . ILE A 1 603 ? 37.785  14.842  38.037  1.00 79.89  ? 603 ILE A O     1 
ATOM   4968 C  CB    . ILE A 1 603 ? 38.838  12.727  39.972  1.00 80.17  ? 603 ILE A CB    1 
ATOM   4969 C  CG1   . ILE A 1 603 ? 39.174  12.418  41.435  1.00 82.34  ? 603 ILE A CG1   1 
ATOM   4970 C  CG2   . ILE A 1 603 ? 39.253  11.562  39.088  1.00 77.35  ? 603 ILE A CG2   1 
ATOM   4971 C  CD1   . ILE A 1 603 ? 38.142  12.924  42.430  1.00 95.49  ? 603 ILE A CD1   1 
ATOM   4972 N  N     . THR A 1 604 ? 39.795  14.399  37.116  1.00 85.88  ? 604 THR A N     1 
ATOM   4973 C  CA    . THR A 1 604 ? 39.392  14.666  35.743  1.00 73.83  ? 604 THR A CA    1 
ATOM   4974 C  C     . THR A 1 604 ? 39.401  13.357  34.967  1.00 80.33  ? 604 THR A C     1 
ATOM   4975 O  O     . THR A 1 604 ? 40.407  12.640  34.967  1.00 79.31  ? 604 THR A O     1 
ATOM   4976 C  CB    . THR A 1 604 ? 40.325  15.681  35.079  1.00 77.05  ? 604 THR A CB    1 
ATOM   4977 O  OG1   . THR A 1 604 ? 40.179  16.956  35.716  1.00 70.04  ? 604 THR A OG1   1 
ATOM   4978 C  CG2   . THR A 1 604 ? 39.999  15.817  33.599  1.00 76.42  ? 604 THR A CG2   1 
ATOM   4979 N  N     . THR A 1 605 ? 38.283  13.043  34.319  1.00 86.89  ? 605 THR A N     1 
ATOM   4980 C  CA    . THR A 1 605 ? 38.145  11.811  33.559  1.00 78.97  ? 605 THR A CA    1 
ATOM   4981 C  C     . THR A 1 605 ? 37.889  12.138  32.096  1.00 71.96  ? 605 THR A C     1 
ATOM   4982 O  O     . THR A 1 605 ? 37.148  13.074  31.780  1.00 68.71  ? 605 THR A O     1 
ATOM   4983 C  CB    . THR A 1 605 ? 37.009  10.942  34.097  1.00 75.46  ? 605 THR A CB    1 
ATOM   4984 O  OG1   . THR A 1 605 ? 37.178  10.754  35.506  1.00 82.43  ? 605 THR A OG1   1 
ATOM   4985 C  CG2   . THR A 1 605 ? 37.039  9.588   33.423  1.00 73.90  ? 605 THR A CG2   1 
ATOM   4986 N  N     . ARG A 1 606 ? 38.509  11.365  31.206  1.00 70.21  ? 606 ARG A N     1 
ATOM   4987 C  CA    . ARG A 1 606 ? 38.397  11.588  29.771  1.00 64.96  ? 606 ARG A CA    1 
ATOM   4988 C  C     . ARG A 1 606 ? 38.166  10.264  29.062  1.00 66.62  ? 606 ARG A C     1 
ATOM   4989 O  O     . ARG A 1 606 ? 38.920  9.308   29.268  1.00 58.27  ? 606 ARG A O     1 
ATOM   4990 C  CB    . ARG A 1 606 ? 39.657  12.262  29.214  1.00 72.36  ? 606 ARG A CB    1 
ATOM   4991 C  CG    . ARG A 1 606 ? 40.105  13.485  29.990  1.00 73.53  ? 606 ARG A CG    1 
ATOM   4992 C  CD    . ARG A 1 606 ? 39.924  14.752  29.177  1.00 73.47  ? 606 ARG A CD    1 
ATOM   4993 N  NE    . ARG A 1 606 ? 39.557  15.883  30.020  1.00 84.53  ? 606 ARG A NE    1 
ATOM   4994 C  CZ    . ARG A 1 606 ? 38.507  16.663  29.807  1.00 83.99  ? 606 ARG A CZ    1 
ATOM   4995 N  NH1   . ARG A 1 606 ? 37.699  16.468  28.778  1.00 81.21  ? 606 ARG A NH1   1 
ATOM   4996 N  NH2   . ARG A 1 606 ? 38.259  17.661  30.651  1.00 82.69  ? 606 ARG A NH2   1 
ATOM   4997 N  N     . GLY A 1 607 ? 37.122  10.210  28.238  1.00 68.05  ? 607 GLY A N     1 
ATOM   4998 C  CA    . GLY A 1 607 ? 36.914  9.094   27.335  1.00 64.06  ? 607 GLY A CA    1 
ATOM   4999 C  C     . GLY A 1 607 ? 36.345  7.830   27.946  1.00 59.90  ? 607 GLY A C     1 
ATOM   5000 O  O     . GLY A 1 607 ? 35.712  7.034   27.245  1.00 59.31  ? 607 GLY A O     1 
ATOM   5001 N  N     . LEU A 1 608 ? 36.569  7.624   29.241  1.00 61.68  ? 608 LEU A N     1 
ATOM   5002 C  CA    . LEU A 1 608 ? 36.094  6.421   29.906  1.00 65.59  ? 608 LEU A CA    1 
ATOM   5003 C  C     . LEU A 1 608 ? 34.565  6.358   29.883  1.00 80.20  ? 608 LEU A C     1 
ATOM   5004 O  O     . LEU A 1 608 ? 33.876  7.325   29.551  1.00 73.94  ? 608 LEU A O     1 
ATOM   5005 C  CB    . LEU A 1 608 ? 36.617  6.370   31.341  1.00 67.35  ? 608 LEU A CB    1 
ATOM   5006 C  CG    . LEU A 1 608 ? 38.134  6.244   31.485  1.00 77.26  ? 608 LEU A CG    1 
ATOM   5007 C  CD1   . LEU A 1 608 ? 38.546  6.231   32.937  1.00 74.20  ? 608 LEU A CD1   1 
ATOM   5008 C  CD2   . LEU A 1 608 ? 38.589  4.963   30.822  1.00 74.93  ? 608 LEU A CD2   1 
ATOM   5009 N  N     . GLU A 1 609 ? 34.039  5.184   30.244  1.00 79.98  ? 609 GLU A N     1 
ATOM   5010 C  CA    . GLU A 1 609 ? 32.595  4.970   30.217  1.00 71.97  ? 609 GLU A CA    1 
ATOM   5011 C  C     . GLU A 1 609 ? 31.858  5.976   31.089  1.00 71.91  ? 609 GLU A C     1 
ATOM   5012 O  O     . GLU A 1 609 ? 30.721  6.353   30.780  1.00 71.92  ? 609 GLU A O     1 
ATOM   5013 C  CB    . GLU A 1 609 ? 32.267  3.549   30.674  1.00 68.00  ? 609 GLU A CB    1 
ATOM   5014 C  CG    . GLU A 1 609 ? 32.641  2.462   29.684  1.00 68.62  ? 609 GLU A CG    1 
ATOM   5015 C  CD    . GLU A 1 609 ? 34.123  2.152   29.677  1.00 75.49  ? 609 GLU A CD    1 
ATOM   5016 O  OE1   . GLU A 1 609 ? 34.816  2.535   30.643  1.00 74.71  ? 609 GLU A OE1   1 
ATOM   5017 O  OE2   . GLU A 1 609 ? 34.594  1.523   28.705  1.00 81.70  ? 609 GLU A OE2   1 
ATOM   5018 N  N     . ILE A 1 610 ? 32.491  6.422   32.176  1.00 67.24  ? 610 ILE A N     1 
ATOM   5019 C  CA    . ILE A 1 610 ? 31.854  7.330   33.126  1.00 71.87  ? 610 ILE A CA    1 
ATOM   5020 C  C     . ILE A 1 610 ? 31.407  8.625   32.456  1.00 65.65  ? 610 ILE A C     1 
ATOM   5021 O  O     . ILE A 1 610 ? 30.432  9.252   32.889  1.00 80.05  ? 610 ILE A O     1 
ATOM   5022 C  CB    . ILE A 1 610 ? 32.821  7.578   34.301  1.00 70.07  ? 610 ILE A CB    1 
ATOM   5023 C  CG1   . ILE A 1 610 ? 32.415  8.798   35.130  1.00 76.70  ? 610 ILE A CG1   1 
ATOM   5024 C  CG2   . ILE A 1 610 ? 34.237  7.682   33.801  1.00 84.32  ? 610 ILE A CG2   1 
ATOM   5025 C  CD1   . ILE A 1 610 ? 33.278  8.996   36.350  1.00 93.91  ? 610 ILE A CD1   1 
ATOM   5026 N  N     . VAL A 1 611 ? 32.082  9.037   31.383  1.00 77.88  ? 611 VAL A N     1 
ATOM   5027 C  CA    . VAL A 1 611 ? 31.689  10.249  30.669  1.00 69.75  ? 611 VAL A CA    1 
ATOM   5028 C  C     . VAL A 1 611 ? 30.814  9.963   29.450  1.00 64.01  ? 611 VAL A C     1 
ATOM   5029 O  O     . VAL A 1 611 ? 30.163  10.890  28.943  1.00 73.10  ? 611 VAL A O     1 
ATOM   5030 C  CB    . VAL A 1 611 ? 32.927  11.069  30.247  1.00 59.93  ? 611 VAL A CB    1 
ATOM   5031 C  CG1   . VAL A 1 611 ? 33.941  11.127  31.382  1.00 66.29  ? 611 VAL A CG1   1 
ATOM   5032 C  CG2   . VAL A 1 611 ? 33.545  10.496  28.982  1.00 56.55  ? 611 VAL A CG2   1 
ATOM   5033 N  N     . ARG A 1 612 ? 30.769  8.721   28.973  1.00 70.20  ? 612 ARG A N     1 
ATOM   5034 C  CA    . ARG A 1 612 ? 30.005  8.398   27.775  1.00 64.89  ? 612 ARG A CA    1 
ATOM   5035 C  C     . ARG A 1 612 ? 28.516  8.354   28.094  1.00 71.61  ? 612 ARG A C     1 
ATOM   5036 O  O     . ARG A 1 612 ? 28.098  7.695   29.050  1.00 74.14  ? 612 ARG A O     1 
ATOM   5037 C  CB    . ARG A 1 612 ? 30.458  7.059   27.194  1.00 73.83  ? 612 ARG A CB    1 
ATOM   5038 C  CG    . ARG A 1 612 ? 31.903  7.036   26.730  1.00 64.95  ? 612 ARG A CG    1 
ATOM   5039 C  CD    . ARG A 1 612 ? 32.193  5.781   25.929  1.00 68.10  ? 612 ARG A CD    1 
ATOM   5040 N  NE    . ARG A 1 612 ? 31.247  5.610   24.834  1.00 48.31  ? 612 ARG A NE    1 
ATOM   5041 C  CZ    . ARG A 1 612 ? 31.449  6.040   23.596  1.00 62.32  ? 612 ARG A CZ    1 
ATOM   5042 N  NH1   . ARG A 1 612 ? 32.557  6.679   23.258  1.00 70.37  ? 612 ARG A NH1   1 
ATOM   5043 N  NH2   . ARG A 1 612 ? 30.517  5.822   22.673  1.00 61.85  ? 612 ARG A NH2   1 
ATOM   5044 N  N     . ARG A 1 613 ? 27.716  9.044   27.282  1.00 73.17  ? 613 ARG A N     1 
ATOM   5045 C  CA    . ARG A 1 613 ? 26.280  9.131   27.520  1.00 75.44  ? 613 ARG A CA    1 
ATOM   5046 C  C     . ARG A 1 613 ? 25.527  7.852   27.169  1.00 70.70  ? 613 ARG A C     1 
ATOM   5047 O  O     . ARG A 1 613 ? 24.378  7.696   27.597  1.00 79.35  ? 613 ARG A O     1 
ATOM   5048 C  CB    . ARG A 1 613 ? 25.696  10.311  26.736  1.00 79.21  ? 613 ARG A CB    1 
ATOM   5049 C  CG    . ARG A 1 613 ? 24.974  9.930   25.454  1.00 84.23  ? 613 ARG A CG    1 
ATOM   5050 C  CD    . ARG A 1 613 ? 24.204  11.111  24.893  1.00 95.45  ? 613 ARG A CD    1 
ATOM   5051 N  NE    . ARG A 1 613 ? 25.088  12.195  24.482  1.00 78.99  ? 613 ARG A NE    1 
ATOM   5052 C  CZ    . ARG A 1 613 ? 25.153  12.679  23.249  1.00 86.76  ? 613 ARG A CZ    1 
ATOM   5053 N  NH1   . ARG A 1 613 ? 24.388  12.204  22.280  1.00 92.85  ? 613 ARG A NH1   1 
ATOM   5054 N  NH2   . ARG A 1 613 ? 26.004  13.666  22.984  1.00 80.42  ? 613 ARG A NH2   1 
ATOM   5055 N  N     . ASP A 1 614 ? 26.139  6.931   26.422  1.00 80.79  ? 614 ASP A N     1 
ATOM   5056 C  CA    . ASP A 1 614 ? 25.467  5.716   25.976  1.00 68.06  ? 614 ASP A CA    1 
ATOM   5057 C  C     . ASP A 1 614 ? 25.758  4.518   26.875  1.00 65.01  ? 614 ASP A C     1 
ATOM   5058 O  O     . ASP A 1 614 ? 25.759  3.375   26.406  1.00 72.37  ? 614 ASP A O     1 
ATOM   5059 C  CB    . ASP A 1 614 ? 25.846  5.396   24.529  1.00 68.99  ? 614 ASP A CB    1 
ATOM   5060 C  CG    . ASP A 1 614 ? 27.346  5.363   24.307  1.00 69.46  ? 614 ASP A CG    1 
ATOM   5061 O  OD1   . ASP A 1 614 ? 28.095  5.826   25.192  1.00 69.54  ? 614 ASP A OD1   1 
ATOM   5062 O  OD2   . ASP A 1 614 ? 27.775  4.871   23.241  1.00 58.90  ? 614 ASP A OD2   1 
ATOM   5063 N  N     . TRP A 1 615 ? 26.000  4.755   28.162  1.00 61.55  ? 615 TRP A N     1 
ATOM   5064 C  CA    . TRP A 1 615 ? 26.202  3.686   29.127  1.00 63.84  ? 615 TRP A CA    1 
ATOM   5065 C  C     . TRP A 1 615 ? 25.233  3.864   30.286  1.00 68.12  ? 615 TRP A C     1 
ATOM   5066 O  O     . TRP A 1 615 ? 24.792  4.977   30.581  1.00 84.06  ? 615 TRP A O     1 
ATOM   5067 C  CB    . TRP A 1 615 ? 27.648  3.654   29.647  1.00 67.43  ? 615 TRP A CB    1 
ATOM   5068 C  CG    . TRP A 1 615 ? 28.633  3.171   28.627  1.00 67.51  ? 615 TRP A CG    1 
ATOM   5069 C  CD1   . TRP A 1 615 ? 29.056  3.840   27.514  1.00 69.03  ? 615 TRP A CD1   1 
ATOM   5070 C  CD2   . TRP A 1 615 ? 29.316  1.911   28.621  1.00 69.62  ? 615 TRP A CD2   1 
ATOM   5071 N  NE1   . TRP A 1 615 ? 29.960  3.076   26.817  1.00 64.88  ? 615 TRP A NE1   1 
ATOM   5072 C  CE2   . TRP A 1 615 ? 30.136  1.887   27.475  1.00 68.90  ? 615 TRP A CE2   1 
ATOM   5073 C  CE3   . TRP A 1 615 ? 29.313  0.802   29.473  1.00 69.06  ? 615 TRP A CE3   1 
ATOM   5074 C  CZ2   . TRP A 1 615 ? 30.947  0.797   27.160  1.00 69.02  ? 615 TRP A CZ2   1 
ATOM   5075 C  CZ3   . TRP A 1 615 ? 30.120  -0.279  29.159  1.00 52.66  ? 615 TRP A CZ3   1 
ATOM   5076 C  CH2   . TRP A 1 615 ? 30.925  -0.273  28.013  1.00 59.08  ? 615 TRP A CH2   1 
ATOM   5077 N  N     . SER A 1 616 ? 24.894  2.752   30.931  1.00 67.70  ? 616 SER A N     1 
ATOM   5078 C  CA    . SER A 1 616 ? 23.984  2.802   32.064  1.00 65.86  ? 616 SER A CA    1 
ATOM   5079 C  C     . SER A 1 616 ? 24.624  3.545   33.230  1.00 68.08  ? 616 SER A C     1 
ATOM   5080 O  O     . SER A 1 616 ? 25.845  3.535   33.408  1.00 79.51  ? 616 SER A O     1 
ATOM   5081 C  CB    . SER A 1 616 ? 23.588  1.391   32.496  1.00 65.78  ? 616 SER A CB    1 
ATOM   5082 O  OG    . SER A 1 616 ? 24.671  0.737   33.131  1.00 70.19  ? 616 SER A OG    1 
ATOM   5083 N  N     . GLU A 1 617 ? 23.780  4.204   34.028  1.00 77.68  ? 617 GLU A N     1 
ATOM   5084 C  CA    . GLU A 1 617 ? 24.283  4.965   35.166  1.00 69.60  ? 617 GLU A CA    1 
ATOM   5085 C  C     . GLU A 1 617 ? 24.972  4.058   36.177  1.00 70.55  ? 617 GLU A C     1 
ATOM   5086 O  O     . GLU A 1 617 ? 25.981  4.442   36.779  1.00 82.91  ? 617 GLU A O     1 
ATOM   5087 C  CB    . GLU A 1 617 ? 23.143  5.739   35.829  1.00 74.60  ? 617 GLU A CB    1 
ATOM   5088 C  CG    . GLU A 1 617 ? 23.589  6.640   36.969  1.00 79.13  ? 617 GLU A CG    1 
ATOM   5089 C  CD    . GLU A 1 617 ? 24.559  7.717   36.517  1.00 111.61 ? 617 GLU A CD    1 
ATOM   5090 O  OE1   . GLU A 1 617 ? 25.594  7.908   37.191  1.00 135.06 ? 617 GLU A OE1   1 
ATOM   5091 O  OE2   . GLU A 1 617 ? 24.286  8.372   35.489  1.00 107.71 ? 617 GLU A OE2   1 
ATOM   5092 N  N     . ILE A 1 618 ? 24.447  2.845   36.368  1.00 75.79  ? 618 ILE A N     1 
ATOM   5093 C  CA    . ILE A 1 618 ? 25.055  1.916   37.315  1.00 75.04  ? 618 ILE A CA    1 
ATOM   5094 C  C     . ILE A 1 618 ? 26.457  1.529   36.864  1.00 81.46  ? 618 ILE A C     1 
ATOM   5095 O  O     . ILE A 1 618 ? 27.307  1.173   37.688  1.00 82.56  ? 618 ILE A O     1 
ATOM   5096 C  CB    . ILE A 1 618 ? 24.149  0.681   37.508  1.00 68.55  ? 618 ILE A CB    1 
ATOM   5097 C  CG1   . ILE A 1 618 ? 24.554  -0.100  38.762  1.00 72.70  ? 618 ILE A CG1   1 
ATOM   5098 C  CG2   . ILE A 1 618 ? 24.175  -0.215  36.276  1.00 64.77  ? 618 ILE A CG2   1 
ATOM   5099 C  CD1   . ILE A 1 618 ? 24.863  0.775   39.957  1.00 78.35  ? 618 ILE A CD1   1 
ATOM   5100 N  N     . ALA A 1 619 ? 26.730  1.603   35.561  1.00 74.48  ? 619 ALA A N     1 
ATOM   5101 C  CA    . ALA A 1 619 ? 28.078  1.337   35.076  1.00 68.01  ? 619 ALA A CA    1 
ATOM   5102 C  C     . ALA A 1 619 ? 28.996  2.526   35.334  1.00 82.88  ? 619 ALA A C     1 
ATOM   5103 O  O     . ALA A 1 619 ? 30.123  2.357   35.812  1.00 85.26  ? 619 ALA A O     1 
ATOM   5104 C  CB    . ALA A 1 619 ? 28.042  0.990   33.586  1.00 61.87  ? 619 ALA A CB    1 
ATOM   5105 N  N     . LYS A 1 620 ? 28.524  3.738   35.030  1.00 73.66  ? 620 LYS A N     1 
ATOM   5106 C  CA    . LYS A 1 620 ? 29.317  4.933   35.301  1.00 66.30  ? 620 LYS A CA    1 
ATOM   5107 C  C     . LYS A 1 620 ? 29.552  5.107   36.796  1.00 84.42  ? 620 LYS A C     1 
ATOM   5108 O  O     . LYS A 1 620 ? 30.689  5.308   37.240  1.00 82.23  ? 620 LYS A O     1 
ATOM   5109 C  CB    . LYS A 1 620 ? 28.619  6.174   34.747  1.00 68.21  ? 620 LYS A CB    1 
ATOM   5110 C  CG    . LYS A 1 620 ? 28.120  6.083   33.323  1.00 68.11  ? 620 LYS A CG    1 
ATOM   5111 C  CD    . LYS A 1 620 ? 27.000  7.096   33.140  1.00 78.73  ? 620 LYS A CD    1 
ATOM   5112 C  CE    . LYS A 1 620 ? 26.618  7.274   31.691  1.00 72.56  ? 620 LYS A CE    1 
ATOM   5113 N  NZ    . LYS A 1 620 ? 27.071  8.592   31.165  1.00 83.94  ? 620 LYS A NZ    1 
ATOM   5114 N  N     . GLU A 1 621 ? 28.474  5.044   37.585  1.00 85.04  ? 621 GLU A N     1 
ATOM   5115 C  CA    . GLU A 1 621 ? 28.551  5.341   39.013  1.00 79.85  ? 621 GLU A CA    1 
ATOM   5116 C  C     . GLU A 1 621 ? 29.598  4.485   39.712  1.00 85.68  ? 621 GLU A C     1 
ATOM   5117 O  O     . GLU A 1 621 ? 30.332  4.972   40.580  1.00 93.69  ? 621 GLU A O     1 
ATOM   5118 C  CB    . GLU A 1 621 ? 27.178  5.134   39.657  1.00 81.91  ? 621 GLU A CB    1 
ATOM   5119 C  CG    . GLU A 1 621 ? 27.196  5.038   41.175  1.00 86.12  ? 621 GLU A CG    1 
ATOM   5120 C  CD    . GLU A 1 621 ? 25.803  5.050   41.775  1.00 101.21 ? 621 GLU A CD    1 
ATOM   5121 O  OE1   . GLU A 1 621 ? 24.869  5.542   41.105  1.00 89.31  ? 621 GLU A OE1   1 
ATOM   5122 O  OE2   . GLU A 1 621 ? 25.639  4.558   42.912  1.00 96.10  ? 621 GLU A OE2   1 
ATOM   5123 N  N     . THR A 1 622 ? 29.690  3.208   39.340  1.00 83.16  ? 622 THR A N     1 
ATOM   5124 C  CA    . THR A 1 622 ? 30.613  2.306   40.018  1.00 87.27  ? 622 THR A CA    1 
ATOM   5125 C  C     . THR A 1 622 ? 32.031  2.416   39.475  1.00 82.91  ? 622 THR A C     1 
ATOM   5126 O  O     . THR A 1 622 ? 32.991  2.258   40.238  1.00 84.18  ? 622 THR A O     1 
ATOM   5127 C  CB    . THR A 1 622 ? 30.110  0.868   39.909  1.00 86.24  ? 622 THR A CB    1 
ATOM   5128 O  OG1   . THR A 1 622 ? 30.103  0.463   38.535  1.00 94.72  ? 622 THR A OG1   1 
ATOM   5129 C  CG2   . THR A 1 622 ? 28.704  0.779   40.460  1.00 73.07  ? 622 THR A CG2   1 
ATOM   5130 N  N     . GLN A 1 623 ? 32.190  2.679   38.176  1.00 80.04  ? 623 GLN A N     1 
ATOM   5131 C  CA    . GLN A 1 623 ? 33.522  2.968   37.655  1.00 79.20  ? 623 GLN A CA    1 
ATOM   5132 C  C     . GLN A 1 623 ? 34.072  4.250   38.265  1.00 82.26  ? 623 GLN A C     1 
ATOM   5133 O  O     . GLN A 1 623 ? 35.276  4.359   38.526  1.00 82.95  ? 623 GLN A O     1 
ATOM   5134 C  CB    . GLN A 1 623 ? 33.492  3.069   36.130  1.00 74.56  ? 623 GLN A CB    1 
ATOM   5135 C  CG    . GLN A 1 623 ? 34.863  3.307   35.513  1.00 72.03  ? 623 GLN A CG    1 
ATOM   5136 C  CD    . GLN A 1 623 ? 34.824  3.403   34.003  1.00 73.34  ? 623 GLN A CD    1 
ATOM   5137 O  OE1   . GLN A 1 623 ? 34.194  4.300   33.442  1.00 76.41  ? 623 GLN A OE1   1 
ATOM   5138 N  NE2   . GLN A 1 623 ? 35.504  2.479   33.333  1.00 72.06  ? 623 GLN A NE2   1 
ATOM   5139 N  N     . ALA A 1 624 ? 33.198  5.231   38.502  1.00 81.78  ? 624 ALA A N     1 
ATOM   5140 C  CA    . ALA A 1 624 ? 33.603  6.443   39.206  1.00 85.53  ? 624 ALA A CA    1 
ATOM   5141 C  C     . ALA A 1 624 ? 34.145  6.116   40.591  1.00 90.85  ? 624 ALA A C     1 
ATOM   5142 O  O     . ALA A 1 624 ? 35.207  6.608   40.991  1.00 90.67  ? 624 ALA A O     1 
ATOM   5143 C  CB    . ALA A 1 624 ? 32.419  7.404   39.311  1.00 72.26  ? 624 ALA A CB    1 
ATOM   5144 N  N     . ARG A 1 625 ? 33.424  5.279   41.340  1.00 88.05  ? 625 ARG A N     1 
ATOM   5145 C  CA    . ARG A 1 625 ? 33.842  4.950   42.698  1.00 92.17  ? 625 ARG A CA    1 
ATOM   5146 C  C     . ARG A 1 625 ? 35.113  4.111   42.698  1.00 92.97  ? 625 ARG A C     1 
ATOM   5147 O  O     . ARG A 1 625 ? 35.969  4.273   43.576  1.00 95.38  ? 625 ARG A O     1 
ATOM   5148 C  CB    . ARG A 1 625 ? 32.714  4.225   43.428  1.00 86.28  ? 625 ARG A CB    1 
ATOM   5149 C  CG    . ARG A 1 625 ? 31.535  5.118   43.770  1.00 89.84  ? 625 ARG A CG    1 
ATOM   5150 C  CD    . ARG A 1 625 ? 30.245  4.324   43.836  1.00 91.50  ? 625 ARG A CD    1 
ATOM   5151 N  NE    . ARG A 1 625 ? 30.102  3.627   45.108  1.00 101.01 ? 625 ARG A NE    1 
ATOM   5152 C  CZ    . ARG A 1 625 ? 29.513  2.448   45.252  1.00 100.81 ? 625 ARG A CZ    1 
ATOM   5153 N  NH1   . ARG A 1 625 ? 28.998  1.802   44.219  1.00 99.61  ? 625 ARG A NH1   1 
ATOM   5154 N  NH2   . ARG A 1 625 ? 29.440  1.902   46.463  1.00 101.00 ? 625 ARG A NH2   1 
ATOM   5155 N  N     . VAL A 1 626 ? 35.253  3.208   41.726  1.00 90.76  ? 626 VAL A N     1 
ATOM   5156 C  CA    . VAL A 1 626 ? 36.474  2.415   41.623  1.00 93.35  ? 626 VAL A CA    1 
ATOM   5157 C  C     . VAL A 1 626 ? 37.661  3.313   41.301  1.00 87.96  ? 626 VAL A C     1 
ATOM   5158 O  O     . VAL A 1 626 ? 38.753  3.151   41.861  1.00 87.34  ? 626 VAL A O     1 
ATOM   5159 C  CB    . VAL A 1 626 ? 36.298  1.302   40.574  1.00 89.04  ? 626 VAL A CB    1 
ATOM   5160 C  CG1   . VAL A 1 626 ? 37.646  0.729   40.162  1.00 85.24  ? 626 VAL A CG1   1 
ATOM   5161 C  CG2   . VAL A 1 626 ? 35.398  0.210   41.121  1.00 82.62  ? 626 VAL A CG2   1 
ATOM   5162 N  N     . LEU A 1 627 ? 37.465  4.281   40.405  1.00 77.86  ? 627 LEU A N     1 
ATOM   5163 C  CA    . LEU A 1 627 ? 38.528  5.230   40.094  1.00 85.65  ? 627 LEU A CA    1 
ATOM   5164 C  C     . LEU A 1 627 ? 38.838  6.124   41.287  1.00 96.84  ? 627 LEU A C     1 
ATOM   5165 O  O     . LEU A 1 627 ? 40.002  6.474   41.521  1.00 100.24 ? 627 LEU A O     1 
ATOM   5166 C  CB    . LEU A 1 627 ? 38.133  6.073   38.885  1.00 82.27  ? 627 LEU A CB    1 
ATOM   5167 C  CG    . LEU A 1 627 ? 38.450  5.482   37.514  1.00 80.50  ? 627 LEU A CG    1 
ATOM   5168 C  CD1   . LEU A 1 627 ? 38.091  6.481   36.437  1.00 76.91  ? 627 LEU A CD1   1 
ATOM   5169 C  CD2   . LEU A 1 627 ? 39.918  5.095   37.426  1.00 82.69  ? 627 LEU A CD2   1 
ATOM   5170 N  N     . GLU A 1 628 ? 37.812  6.507   42.051  1.00 90.16  ? 628 GLU A N     1 
ATOM   5171 C  CA    . GLU A 1 628 ? 38.024  7.379   43.201  1.00 91.59  ? 628 GLU A CA    1 
ATOM   5172 C  C     . GLU A 1 628 ? 38.904  6.703   44.244  1.00 97.56  ? 628 GLU A C     1 
ATOM   5173 O  O     . GLU A 1 628 ? 39.971  7.214   44.602  1.00 104.82 ? 628 GLU A O     1 
ATOM   5174 C  CB    . GLU A 1 628 ? 36.682  7.787   43.811  1.00 97.27  ? 628 GLU A CB    1 
ATOM   5175 C  CG    . GLU A 1 628 ? 36.817  8.435   45.182  1.00 106.53 ? 628 GLU A CG    1 
ATOM   5176 C  CD    . GLU A 1 628 ? 35.758  9.486   45.444  1.00 122.88 ? 628 GLU A CD    1 
ATOM   5177 O  OE1   . GLU A 1 628 ? 35.900  10.615  44.929  1.00 130.29 ? 628 GLU A OE1   1 
ATOM   5178 O  OE2   . GLU A 1 628 ? 34.785  9.185   46.169  1.00 123.66 ? 628 GLU A OE2   1 
ATOM   5179 N  N     . ALA A 1 629 ? 38.474  5.538   44.737  1.00 96.59  ? 629 ALA A N     1 
ATOM   5180 C  CA    . ALA A 1 629 ? 39.257  4.808   45.729  1.00 104.31 ? 629 ALA A CA    1 
ATOM   5181 C  C     . ALA A 1 629 ? 40.652  4.467   45.222  1.00 104.62 ? 629 ALA A C     1 
ATOM   5182 O  O     . ALA A 1 629 ? 41.538  4.165   46.030  1.00 110.04 ? 629 ALA A O     1 
ATOM   5183 C  CB    . ALA A 1 629 ? 38.524  3.531   46.141  1.00 101.02 ? 629 ALA A CB    1 
ATOM   5184 N  N     . LEU A 1 630 ? 40.866  4.515   43.908  1.00 98.44  ? 630 LEU A N     1 
ATOM   5185 C  CA    . LEU A 1 630 ? 42.170  4.249   43.320  1.00 97.83  ? 630 LEU A CA    1 
ATOM   5186 C  C     . LEU A 1 630 ? 43.060  5.487   43.298  1.00 94.21  ? 630 LEU A C     1 
ATOM   5187 O  O     . LEU A 1 630 ? 44.268  5.382   43.531  1.00 100.61 ? 630 LEU A O     1 
ATOM   5188 C  CB    . LEU A 1 630 ? 41.998  3.710   41.899  1.00 87.52  ? 630 LEU A CB    1 
ATOM   5189 C  CG    . LEU A 1 630 ? 42.142  2.194   41.800  1.00 83.01  ? 630 LEU A CG    1 
ATOM   5190 C  CD1   . LEU A 1 630 ? 41.490  1.657   40.536  1.00 87.78  ? 630 LEU A CD1   1 
ATOM   5191 C  CD2   . LEU A 1 630 ? 43.602  1.822   41.869  1.00 95.92  ? 630 LEU A CD2   1 
ATOM   5192 N  N     . LEU A 1 631 ? 42.486  6.660   43.027  1.00 95.51  ? 631 LEU A N     1 
ATOM   5193 C  CA    . LEU A 1 631 ? 43.254  7.894   42.930  1.00 96.18  ? 631 LEU A CA    1 
ATOM   5194 C  C     . LEU A 1 631 ? 43.205  8.746   44.191  1.00 106.18 ? 631 LEU A C     1 
ATOM   5195 O  O     . LEU A 1 631 ? 44.082  9.599   44.374  1.00 107.85 ? 631 LEU A O     1 
ATOM   5196 C  CB    . LEU A 1 631 ? 42.758  8.735   41.746  1.00 82.07  ? 631 LEU A CB    1 
ATOM   5197 C  CG    . LEU A 1 631 ? 42.859  8.128   40.347  1.00 76.42  ? 631 LEU A CG    1 
ATOM   5198 C  CD1   . LEU A 1 631 ? 42.096  8.984   39.350  1.00 74.44  ? 631 LEU A CD1   1 
ATOM   5199 C  CD2   . LEU A 1 631 ? 44.311  7.977   39.924  1.00 84.00  ? 631 LEU A CD2   1 
ATOM   5200 N  N     . LYS A 1 632 ? 42.209  8.549   45.054  1.00 106.42 ? 632 LYS A N     1 
ATOM   5201 C  CA    . LYS A 1 632 ? 42.076  9.359   46.260  1.00 112.84 ? 632 LYS A CA    1 
ATOM   5202 C  C     . LYS A 1 632 ? 42.933  8.811   47.398  1.00 123.15 ? 632 LYS A C     1 
ATOM   5203 O  O     . LYS A 1 632 ? 43.672  9.564   48.040  1.00 133.03 ? 632 LYS A O     1 
ATOM   5204 C  CB    . LYS A 1 632 ? 40.604  9.434   46.677  1.00 111.26 ? 632 LYS A CB    1 
ATOM   5205 C  CG    . LYS A 1 632 ? 40.130  10.800  47.167  1.00 114.90 ? 632 LYS A CG    1 
ATOM   5206 C  CD    . LYS A 1 632 ? 41.026  11.377  48.251  1.00 137.13 ? 632 LYS A CD    1 
ATOM   5207 C  CE    . LYS A 1 632 ? 40.522  12.732  48.723  1.00 132.75 ? 632 LYS A CE    1 
ATOM   5208 N  NZ    . LYS A 1 632 ? 41.617  13.548  49.317  1.00 131.45 ? 632 LYS A NZ    1 
ATOM   5209 N  N     . ASP A 1 633 ? 42.849  7.506   47.656  1.00 124.67 ? 633 ASP A N     1 
ATOM   5210 C  CA    . ASP A 1 633 ? 43.670  6.872   48.676  1.00 138.04 ? 633 ASP A CA    1 
ATOM   5211 C  C     . ASP A 1 633 ? 44.437  5.662   48.168  1.00 131.32 ? 633 ASP A C     1 
ATOM   5212 O  O     . ASP A 1 633 ? 45.153  5.033   48.955  1.00 147.26 ? 633 ASP A O     1 
ATOM   5213 C  CB    . ASP A 1 633 ? 42.811  6.448   49.878  1.00 143.06 ? 633 ASP A CB    1 
ATOM   5214 C  CG    . ASP A 1 633 ? 42.066  7.609   50.504  1.00 158.44 ? 633 ASP A CG    1 
ATOM   5215 O  OD1   . ASP A 1 633 ? 42.666  8.695   50.648  1.00 167.42 ? 633 ASP A OD1   1 
ATOM   5216 O  OD2   . ASP A 1 633 ? 40.880  7.434   50.855  1.00 165.26 ? 633 ASP A OD2   1 
ATOM   5217 N  N     . GLY A 1 634 ? 44.319  5.319   46.888  1.00 121.36 ? 634 GLY A N     1 
ATOM   5218 C  CA    . GLY A 1 634 ? 44.928  4.096   46.396  1.00 110.08 ? 634 GLY A CA    1 
ATOM   5219 C  C     . GLY A 1 634 ? 44.394  2.853   47.067  1.00 112.92 ? 634 GLY A C     1 
ATOM   5220 O  O     . GLY A 1 634 ? 45.101  1.843   47.148  1.00 111.53 ? 634 GLY A O     1 
ATOM   5221 N  N     . ASP A 1 635 ? 43.155  2.903   47.556  1.00 117.23 ? 635 ASP A N     1 
ATOM   5222 C  CA    . ASP A 1 635 ? 42.562  1.806   48.317  1.00 125.20 ? 635 ASP A CA    1 
ATOM   5223 C  C     . ASP A 1 635 ? 42.024  0.784   47.318  1.00 117.40 ? 635 ASP A C     1 
ATOM   5224 O  O     . ASP A 1 635 ? 40.849  0.777   46.945  1.00 118.96 ? 635 ASP A O     1 
ATOM   5225 C  CB    . ASP A 1 635 ? 41.478  2.336   49.250  1.00 119.20 ? 635 ASP A CB    1 
ATOM   5226 C  CG    . ASP A 1 635 ? 40.949  1.283   50.203  1.00 127.05 ? 635 ASP A CG    1 
ATOM   5227 O  OD1   . ASP A 1 635 ? 41.106  0.080   49.925  1.00 136.31 ? 635 ASP A OD1   1 
ATOM   5228 O  OD2   . ASP A 1 635 ? 40.375  1.663   51.245  1.00 121.13 ? 635 ASP A OD2   1 
ATOM   5229 N  N     . VAL A 1 636 ? 42.923  -0.099  46.877  1.00 116.67 ? 636 VAL A N     1 
ATOM   5230 C  CA    . VAL A 1 636 ? 42.557  -1.108  45.889  1.00 107.51 ? 636 VAL A CA    1 
ATOM   5231 C  C     . VAL A 1 636 ? 41.555  -2.103  46.467  1.00 111.50 ? 636 VAL A C     1 
ATOM   5232 O  O     . VAL A 1 636 ? 40.661  -2.577  45.754  1.00 103.65 ? 636 VAL A O     1 
ATOM   5233 C  CB    . VAL A 1 636 ? 43.826  -1.810  45.364  1.00 103.30 ? 636 VAL A CB    1 
ATOM   5234 C  CG1   . VAL A 1 636 ? 44.721  -2.235  46.524  1.00 116.06 ? 636 VAL A CG1   1 
ATOM   5235 C  CG2   . VAL A 1 636 ? 43.469  -2.998  44.480  1.00 98.66  ? 636 VAL A CG2   1 
ATOM   5236 N  N     . GLU A 1 637 ? 41.665  -2.425  47.760  1.00 116.49 ? 637 GLU A N     1 
ATOM   5237 C  CA    . GLU A 1 637 ? 40.753  -3.406  48.339  1.00 119.11 ? 637 GLU A CA    1 
ATOM   5238 C  C     . GLU A 1 637 ? 39.340  -2.849  48.458  1.00 120.64 ? 637 GLU A C     1 
ATOM   5239 O  O     . GLU A 1 637 ? 38.366  -3.574  48.234  1.00 121.47 ? 637 GLU A O     1 
ATOM   5240 C  CB    . GLU A 1 637 ? 41.270  -3.890  49.697  1.00 128.39 ? 637 GLU A CB    1 
ATOM   5241 C  CG    . GLU A 1 637 ? 41.556  -2.797  50.708  1.00 137.56 ? 637 GLU A CG    1 
ATOM   5242 C  CD    . GLU A 1 637 ? 40.549  -2.769  51.842  1.00 144.66 ? 637 GLU A CD    1 
ATOM   5243 O  OE1   . GLU A 1 637 ? 40.479  -1.742  52.551  1.00 139.69 ? 637 GLU A OE1   1 
ATOM   5244 O  OE2   . GLU A 1 637 ? 39.829  -3.773  52.024  1.00 149.23 ? 637 GLU A OE2   1 
ATOM   5245 N  N     . LYS A 1 638 ? 39.198  -1.566  48.796  1.00 123.63 ? 638 LYS A N     1 
ATOM   5246 C  CA    . LYS A 1 638 ? 37.861  -0.982  48.821  1.00 120.96 ? 638 LYS A CA    1 
ATOM   5247 C  C     . LYS A 1 638 ? 37.282  -0.871  47.417  1.00 114.36 ? 638 LYS A C     1 
ATOM   5248 O  O     . LYS A 1 638 ? 36.076  -1.060  47.231  1.00 118.04 ? 638 LYS A O     1 
ATOM   5249 C  CB    . LYS A 1 638 ? 37.891  0.382   49.515  1.00 121.07 ? 638 LYS A CB    1 
ATOM   5250 C  CG    . LYS A 1 638 ? 36.970  1.446   48.933  1.00 112.31 ? 638 LYS A CG    1 
ATOM   5251 C  CD    . LYS A 1 638 ? 36.845  2.622   49.895  1.00 101.67 ? 638 LYS A CD    1 
ATOM   5252 C  CE    . LYS A 1 638 ? 36.229  3.842   49.230  1.00 95.84  ? 638 LYS A CE    1 
ATOM   5253 N  NZ    . LYS A 1 638 ? 36.077  4.976   50.187  1.00 94.27  ? 638 LYS A NZ    1 
ATOM   5254 N  N     . ALA A 1 639 ? 38.126  -0.601  46.417  1.00 114.84 ? 639 ALA A N     1 
ATOM   5255 C  CA    . ALA A 1 639 ? 37.643  -0.539  45.041  1.00 113.90 ? 639 ALA A CA    1 
ATOM   5256 C  C     . ALA A 1 639 ? 37.136  -1.897  44.572  1.00 109.03 ? 639 ALA A C     1 
ATOM   5257 O  O     . ALA A 1 639 ? 36.088  -1.985  43.922  1.00 105.35 ? 639 ALA A O     1 
ATOM   5258 C  CB    . ALA A 1 639 ? 38.748  -0.030  44.117  1.00 103.02 ? 639 ALA A CB    1 
ATOM   5259 N  N     . VAL A 1 640 ? 37.864  -2.969  44.895  1.00 110.21 ? 640 VAL A N     1 
ATOM   5260 C  CA    . VAL A 1 640 ? 37.419  -4.299  44.494  1.00 99.35  ? 640 VAL A CA    1 
ATOM   5261 C  C     . VAL A 1 640 ? 36.215  -4.736  45.319  1.00 105.70 ? 640 VAL A C     1 
ATOM   5262 O  O     . VAL A 1 640 ? 35.377  -5.510  44.840  1.00 107.97 ? 640 VAL A O     1 
ATOM   5263 C  CB    . VAL A 1 640 ? 38.579  -5.310  44.588  1.00 102.49 ? 640 VAL A CB    1 
ATOM   5264 C  CG1   . VAL A 1 640 ? 38.910  -5.634  46.030  1.00 115.47 ? 640 VAL A CG1   1 
ATOM   5265 C  CG2   . VAL A 1 640 ? 38.235  -6.581  43.839  1.00 104.10 ? 640 VAL A CG2   1 
ATOM   5266 N  N     . ARG A 1 641 ? 36.096  -4.251  46.558  1.00 107.75 ? 641 ARG A N     1 
ATOM   5267 C  CA    . ARG A 1 641 ? 34.886  -4.513  47.330  1.00 109.31 ? 641 ARG A CA    1 
ATOM   5268 C  C     . ARG A 1 641 ? 33.673  -3.867  46.675  1.00 112.65 ? 641 ARG A C     1 
ATOM   5269 O  O     . ARG A 1 641 ? 32.618  -4.498  46.555  1.00 111.86 ? 641 ARG A O     1 
ATOM   5270 C  CB    . ARG A 1 641 ? 35.041  -4.009  48.766  1.00 111.22 ? 641 ARG A CB    1 
ATOM   5271 C  CG    . ARG A 1 641 ? 36.000  -4.805  49.637  1.00 115.57 ? 641 ARG A CG    1 
ATOM   5272 C  CD    . ARG A 1 641 ? 35.740  -4.571  51.121  1.00 122.80 ? 641 ARG A CD    1 
ATOM   5273 N  NE    . ARG A 1 641 ? 36.243  -3.280  51.574  1.00 119.61 ? 641 ARG A NE    1 
ATOM   5274 C  CZ    . ARG A 1 641 ? 35.523  -2.167  51.627  1.00 126.10 ? 641 ARG A CZ    1 
ATOM   5275 N  NH1   . ARG A 1 641 ? 34.245  -2.151  51.282  1.00 124.86 ? 641 ARG A NH1   1 
ATOM   5276 N  NH2   . ARG A 1 641 ? 36.099  -1.041  52.039  1.00 130.05 ? 641 ARG A NH2   1 
ATOM   5277 N  N     . ILE A 1 642 ? 33.814  -2.614  46.230  1.00 109.09 ? 642 ILE A N     1 
ATOM   5278 C  CA    . ILE A 1 642 ? 32.689  -1.872  45.662  1.00 103.77 ? 642 ILE A CA    1 
ATOM   5279 C  C     . ILE A 1 642 ? 32.067  -2.629  44.495  1.00 100.20 ? 642 ILE A C     1 
ATOM   5280 O  O     . ILE A 1 642 ? 30.838  -2.710  44.372  1.00 101.87 ? 642 ILE A O     1 
ATOM   5281 C  CB    . ILE A 1 642 ? 33.141  -0.459  45.245  1.00 95.57  ? 642 ILE A CB    1 
ATOM   5282 C  CG1   . ILE A 1 642 ? 33.496  0.378   46.477  1.00 100.94 ? 642 ILE A CG1   1 
ATOM   5283 C  CG2   . ILE A 1 642 ? 32.070  0.218   44.404  1.00 86.83  ? 642 ILE A CG2   1 
ATOM   5284 C  CD1   . ILE A 1 642 ? 33.325  1.874   46.287  1.00 95.58  ? 642 ILE A CD1   1 
ATOM   5285 N  N     . VAL A 1 643 ? 32.901  -3.199  43.620  1.00 94.10  ? 643 VAL A N     1 
ATOM   5286 C  CA    . VAL A 1 643 ? 32.376  -3.976  42.501  1.00 86.64  ? 643 VAL A CA    1 
ATOM   5287 C  C     . VAL A 1 643 ? 31.580  -5.174  43.002  1.00 96.30  ? 643 VAL A C     1 
ATOM   5288 O  O     . VAL A 1 643 ? 30.597  -5.585  42.375  1.00 103.02 ? 643 VAL A O     1 
ATOM   5289 C  CB    . VAL A 1 643 ? 33.522  -4.413  41.568  1.00 89.96  ? 643 VAL A CB    1 
ATOM   5290 C  CG1   . VAL A 1 643 ? 32.970  -5.091  40.326  1.00 83.93  ? 643 VAL A CG1   1 
ATOM   5291 C  CG2   . VAL A 1 643 ? 34.381  -3.222  41.187  1.00 91.18  ? 643 VAL A CG2   1 
ATOM   5292 N  N     . LYS A 1 644 ? 31.975  -5.742  44.143  1.00 102.34 ? 644 LYS A N     1 
ATOM   5293 C  CA    . LYS A 1 644 ? 31.270  -6.901  44.676  1.00 101.11 ? 644 LYS A CA    1 
ATOM   5294 C  C     . LYS A 1 644 ? 29.939  -6.527  45.317  1.00 105.21 ? 644 LYS A C     1 
ATOM   5295 O  O     . LYS A 1 644 ? 28.997  -7.327  45.279  1.00 108.89 ? 644 LYS A O     1 
ATOM   5296 C  CB    . LYS A 1 644 ? 32.154  -7.635  45.687  1.00 105.13 ? 644 LYS A CB    1 
ATOM   5297 C  CG    . LYS A 1 644 ? 32.815  -8.888  45.135  1.00 112.40 ? 644 LYS A CG    1 
ATOM   5298 C  CD    . LYS A 1 644 ? 34.049  -9.264  45.937  1.00 109.17 ? 644 LYS A CD    1 
ATOM   5299 C  CE    . LYS A 1 644 ? 34.954  -10.192 45.145  1.00 112.65 ? 644 LYS A CE    1 
ATOM   5300 N  NZ    . LYS A 1 644 ? 36.364  -10.157 45.626  1.00 104.70 ? 644 LYS A NZ    1 
ATOM   5301 N  N     . GLU A 1 645 ? 29.836  -5.335  45.911  1.00 108.26 ? 645 GLU A N     1 
ATOM   5302 C  CA    . GLU A 1 645 ? 28.558  -4.915  46.482  1.00 115.41 ? 645 GLU A CA    1 
ATOM   5303 C  C     . GLU A 1 645 ? 27.542  -4.609  45.390  1.00 101.16 ? 645 GLU A C     1 
ATOM   5304 O  O     . GLU A 1 645 ? 26.371  -4.989  45.498  1.00 99.09  ? 645 GLU A O     1 
ATOM   5305 C  CB    . GLU A 1 645 ? 28.744  -3.692  47.383  1.00 128.91 ? 645 GLU A CB    1 
ATOM   5306 C  CG    . GLU A 1 645 ? 30.149  -3.499  47.916  1.00 138.63 ? 645 GLU A CG    1 
ATOM   5307 C  CD    . GLU A 1 645 ? 30.243  -2.392  48.947  1.00 146.08 ? 645 GLU A CD    1 
ATOM   5308 O  OE1   . GLU A 1 645 ? 29.391  -1.478  48.920  1.00 138.98 ? 645 GLU A OE1   1 
ATOM   5309 O  OE2   . GLU A 1 645 ? 31.173  -2.432  49.780  1.00 141.03 ? 645 GLU A OE2   1 
ATOM   5310 N  N     . VAL A 1 646 ? 27.974  -3.925  44.330  1.00 101.56 ? 646 VAL A N     1 
ATOM   5311 C  CA    . VAL A 1 646 ? 27.046  -3.539  43.274  1.00 96.84  ? 646 VAL A CA    1 
ATOM   5312 C  C     . VAL A 1 646 ? 26.646  -4.745  42.436  1.00 99.76  ? 646 VAL A C     1 
ATOM   5313 O  O     . VAL A 1 646 ? 25.500  -4.839  41.978  1.00 100.47 ? 646 VAL A O     1 
ATOM   5314 C  CB    . VAL A 1 646 ? 27.671  -2.423  42.418  1.00 85.40  ? 646 VAL A CB    1 
ATOM   5315 C  CG1   . VAL A 1 646 ? 26.879  -2.217  41.135  1.00 84.97  ? 646 VAL A CG1   1 
ATOM   5316 C  CG2   . VAL A 1 646 ? 27.746  -1.140  43.226  1.00 96.47  ? 646 VAL A CG2   1 
ATOM   5317 N  N     . THR A 1 647 ? 27.564  -5.693  42.233  1.00 94.11  ? 647 THR A N     1 
ATOM   5318 C  CA    . THR A 1 647 ? 27.219  -6.885  41.467  1.00 91.42  ? 647 THR A CA    1 
ATOM   5319 C  C     . THR A 1 647 ? 26.195  -7.746  42.201  1.00 104.13 ? 647 THR A C     1 
ATOM   5320 O  O     . THR A 1 647 ? 25.394  -8.433  41.559  1.00 99.52  ? 647 THR A O     1 
ATOM   5321 C  CB    . THR A 1 647 ? 28.483  -7.688  41.136  1.00 93.22  ? 647 THR A CB    1 
ATOM   5322 O  OG1   . THR A 1 647 ? 28.249  -8.506  39.983  1.00 103.46 ? 647 THR A OG1   1 
ATOM   5323 C  CG2   . THR A 1 647 ? 28.906  -8.571  42.303  1.00 99.20  ? 647 THR A CG2   1 
ATOM   5324 N  N     . GLU A 1 648 ? 26.180  -7.706  43.536  1.00 98.63  ? 648 GLU A N     1 
ATOM   5325 C  CA    . GLU A 1 648 ? 25.152  -8.431  44.270  1.00 98.75  ? 648 GLU A CA    1 
ATOM   5326 C  C     . GLU A 1 648 ? 23.833  -7.671  44.283  1.00 104.45 ? 648 GLU A C     1 
ATOM   5327 O  O     . GLU A 1 648 ? 22.765  -8.292  44.304  1.00 102.87 ? 648 GLU A O     1 
ATOM   5328 C  CB    . GLU A 1 648 ? 25.614  -8.715  45.700  1.00 102.62 ? 648 GLU A CB    1 
ATOM   5329 C  CG    . GLU A 1 648 ? 26.072  -10.149 45.924  1.00 118.23 ? 648 GLU A CG    1 
ATOM   5330 C  CD    . GLU A 1 648 ? 25.728  -10.662 47.308  1.00 131.02 ? 648 GLU A CD    1 
ATOM   5331 O  OE1   . GLU A 1 648 ? 25.754  -9.858  48.264  1.00 140.39 ? 648 GLU A OE1   1 
ATOM   5332 O  OE2   . GLU A 1 648 ? 25.430  -11.868 47.442  1.00 116.20 ? 648 GLU A OE2   1 
ATOM   5333 N  N     . LYS A 1 649 ? 23.889  -6.338  44.266  1.00 103.63 ? 649 LYS A N     1 
ATOM   5334 C  CA    . LYS A 1 649 ? 22.669  -5.544  44.174  1.00 96.70  ? 649 LYS A CA    1 
ATOM   5335 C  C     . LYS A 1 649 ? 21.933  -5.821  42.868  1.00 98.66  ? 649 LYS A C     1 
ATOM   5336 O  O     . LYS A 1 649 ? 20.699  -5.901  42.846  1.00 103.55 ? 649 LYS A O     1 
ATOM   5337 C  CB    . LYS A 1 649 ? 23.004  -4.058  44.295  1.00 106.08 ? 649 LYS A CB    1 
ATOM   5338 C  CG    . LYS A 1 649 ? 22.339  -3.350  45.464  1.00 107.48 ? 649 LYS A CG    1 
ATOM   5339 C  CD    . LYS A 1 649 ? 23.272  -2.317  46.080  1.00 119.89 ? 649 LYS A CD    1 
ATOM   5340 C  CE    . LYS A 1 649 ? 22.553  -1.466  47.112  1.00 120.15 ? 649 LYS A CE    1 
ATOM   5341 N  NZ    . LYS A 1 649 ? 23.492  -0.568  47.839  1.00 115.14 ? 649 LYS A NZ    1 
ATOM   5342 N  N     . LEU A 1 650 ? 22.676  -5.967  41.768  1.00 103.20 ? 650 LEU A N     1 
ATOM   5343 C  CA    . LEU A 1 650 ? 22.058  -6.269  40.481  1.00 97.44  ? 650 LEU A CA    1 
ATOM   5344 C  C     . LEU A 1 650 ? 21.391  -7.640  40.498  1.00 96.88  ? 650 LEU A C     1 
ATOM   5345 O  O     . LEU A 1 650 ? 20.209  -7.774  40.156  1.00 95.64  ? 650 LEU A O     1 
ATOM   5346 C  CB    . LEU A 1 650 ? 23.108  -6.195  39.370  1.00 86.23  ? 650 LEU A CB    1 
ATOM   5347 C  CG    . LEU A 1 650 ? 23.630  -4.819  38.953  1.00 90.62  ? 650 LEU A CG    1 
ATOM   5348 C  CD1   . LEU A 1 650 ? 24.113  -4.844  37.516  1.00 90.97  ? 650 LEU A CD1   1 
ATOM   5349 C  CD2   . LEU A 1 650 ? 22.543  -3.782  39.105  1.00 71.51  ? 650 LEU A CD2   1 
ATOM   5350 N  N     . SER A 1 651 ? 22.138  -8.672  40.901  1.00 89.53  ? 651 SER A N     1 
ATOM   5351 C  CA    . SER A 1 651 ? 21.619  -10.037 40.858  1.00 99.98  ? 651 SER A CA    1 
ATOM   5352 C  C     . SER A 1 651 ? 20.394  -10.211 41.746  1.00 105.53 ? 651 SER A C     1 
ATOM   5353 O  O     . SER A 1 651 ? 19.565  -11.093 41.492  1.00 102.27 ? 651 SER A O     1 
ATOM   5354 C  CB    . SER A 1 651 ? 22.713  -11.027 41.261  1.00 100.91 ? 651 SER A CB    1 
ATOM   5355 O  OG    . SER A 1 651 ? 23.187  -10.764 42.571  1.00 101.34 ? 651 SER A OG    1 
ATOM   5356 N  N     . LYS A 1 652 ? 20.263  -9.391  42.788  1.00 112.03 ? 652 LYS A N     1 
ATOM   5357 C  CA    . LYS A 1 652 ? 19.091  -9.406  43.651  1.00 104.35 ? 652 LYS A CA    1 
ATOM   5358 C  C     . LYS A 1 652 ? 18.113  -8.289  43.309  1.00 95.10  ? 652 LYS A C     1 
ATOM   5359 O  O     . LYS A 1 652 ? 17.200  -8.008  44.092  1.00 91.28  ? 652 LYS A O     1 
ATOM   5360 C  CB    . LYS A 1 652 ? 19.523  -9.330  45.118  1.00 94.33  ? 652 LYS A CB    1 
ATOM   5361 C  CG    . LYS A 1 652 ? 20.601  -10.360 45.462  1.00 97.76  ? 652 LYS A CG    1 
ATOM   5362 C  CD    . LYS A 1 652 ? 20.907  -10.465 46.953  1.00 97.21  ? 652 LYS A CD    1 
ATOM   5363 C  CE    . LYS A 1 652 ? 20.424  -9.262  47.739  1.00 103.63 ? 652 LYS A CE    1 
ATOM   5364 N  NZ    . LYS A 1 652 ? 20.689  -9.431  49.194  1.00 101.57 ? 652 LYS A NZ    1 
ATOM   5365 N  N     . TYR A 1 653 ? 18.296  -7.650  42.150  1.00 93.55  ? 653 TYR A N     1 
ATOM   5366 C  CA    . TYR A 1 653 ? 17.343  -6.695  41.583  1.00 99.99  ? 653 TYR A CA    1 
ATOM   5367 C  C     . TYR A 1 653 ? 17.073  -5.521  42.520  1.00 95.30  ? 653 TYR A C     1 
ATOM   5368 O  O     . TYR A 1 653 ? 15.994  -4.924  42.492  1.00 97.06  ? 653 TYR A O     1 
ATOM   5369 C  CB    . TYR A 1 653 ? 16.030  -7.378  41.183  1.00 84.45  ? 653 TYR A CB    1 
ATOM   5370 C  CG    . TYR A 1 653 ? 16.224  -8.569  40.269  1.00 98.71  ? 653 TYR A CG    1 
ATOM   5371 C  CD1   . TYR A 1 653 ? 16.019  -8.453  38.902  1.00 97.42  ? 653 TYR A CD1   1 
ATOM   5372 C  CD2   . TYR A 1 653 ? 16.573  -9.818  40.775  1.00 102.43 ? 653 TYR A CD2   1 
ATOM   5373 C  CE1   . TYR A 1 653 ? 16.193  -9.535  38.058  1.00 104.03 ? 653 TYR A CE1   1 
ATOM   5374 C  CE2   . TYR A 1 653 ? 16.741  -10.906 39.941  1.00 107.68 ? 653 TYR A CE2   1 
ATOM   5375 C  CZ    . TYR A 1 653 ? 16.545  -10.762 38.585  1.00 107.14 ? 653 TYR A CZ    1 
ATOM   5376 O  OH    . TYR A 1 653 ? 16.710  -11.842 37.749  1.00 101.41 ? 653 TYR A OH    1 
ATOM   5377 N  N     . GLU A 1 654 ? 18.059  -5.166  43.339  1.00 97.88  ? 654 GLU A N     1 
ATOM   5378 C  CA    . GLU A 1 654 ? 17.921  -4.080  44.298  1.00 87.85  ? 654 GLU A CA    1 
ATOM   5379 C  C     . GLU A 1 654 ? 18.319  -2.727  43.727  1.00 83.71  ? 654 GLU A C     1 
ATOM   5380 O  O     . GLU A 1 654 ? 18.160  -1.713  44.414  1.00 89.90  ? 654 GLU A O     1 
ATOM   5381 C  CB    . GLU A 1 654 ? 18.761  -4.373  45.542  1.00 92.64  ? 654 GLU A CB    1 
ATOM   5382 C  CG    . GLU A 1 654 ? 18.732  -5.823  45.986  1.00 101.78 ? 654 GLU A CG    1 
ATOM   5383 C  CD    . GLU A 1 654 ? 19.162  -5.994  47.428  1.00 110.67 ? 654 GLU A CD    1 
ATOM   5384 O  OE1   . GLU A 1 654 ? 20.383  -6.074  47.679  1.00 108.02 ? 654 GLU A OE1   1 
ATOM   5385 O  OE2   . GLU A 1 654 ? 18.280  -6.048  48.310  1.00 116.22 ? 654 GLU A OE2   1 
ATOM   5386 N  N     . VAL A 1 655 ? 18.832  -2.680  42.502  1.00 81.69  ? 655 VAL A N     1 
ATOM   5387 C  CA    . VAL A 1 655 ? 19.268  -1.420  41.907  1.00 81.97  ? 655 VAL A CA    1 
ATOM   5388 C  C     . VAL A 1 655 ? 18.108  -0.807  41.133  1.00 84.56  ? 655 VAL A C     1 
ATOM   5389 O  O     . VAL A 1 655 ? 17.436  -1.511  40.364  1.00 90.15  ? 655 VAL A O     1 
ATOM   5390 C  CB    . VAL A 1 655 ? 20.505  -1.624  41.018  1.00 85.41  ? 655 VAL A CB    1 
ATOM   5391 C  CG1   . VAL A 1 655 ? 20.619  -0.518  39.978  1.00 76.55  ? 655 VAL A CG1   1 
ATOM   5392 C  CG2   . VAL A 1 655 ? 21.756  -1.670  41.877  1.00 85.01  ? 655 VAL A CG2   1 
ATOM   5393 N  N     . PRO A 1 656 ? 17.829  0.481   41.319  1.00 77.89  ? 656 PRO A N     1 
ATOM   5394 C  CA    . PRO A 1 656 ? 16.702  1.116   40.630  1.00 78.78  ? 656 PRO A CA    1 
ATOM   5395 C  C     . PRO A 1 656 ? 16.814  0.956   39.126  1.00 83.38  ? 656 PRO A C     1 
ATOM   5396 O  O     . PRO A 1 656 ? 17.880  1.212   38.547  1.00 90.88  ? 656 PRO A O     1 
ATOM   5397 C  CB    . PRO A 1 656 ? 16.824  2.591   41.041  1.00 81.40  ? 656 PRO A CB    1 
ATOM   5398 C  CG    . PRO A 1 656 ? 17.557  2.563   42.327  1.00 82.04  ? 656 PRO A CG    1 
ATOM   5399 C  CD    . PRO A 1 656 ? 18.515  1.411   42.233  1.00 83.35  ? 656 PRO A CD    1 
ATOM   5400 N  N     . PRO A 1 657 ? 15.736  0.531   38.463  1.00 81.53  ? 657 PRO A N     1 
ATOM   5401 C  CA    . PRO A 1 657 ? 15.783  0.379   36.998  1.00 78.93  ? 657 PRO A CA    1 
ATOM   5402 C  C     . PRO A 1 657 ? 16.197  1.647   36.264  1.00 82.54  ? 657 PRO A C     1 
ATOM   5403 O  O     . PRO A 1 657 ? 16.667  1.560   35.123  1.00 81.76  ? 657 PRO A O     1 
ATOM   5404 C  CB    . PRO A 1 657 ? 14.347  -0.031  36.644  1.00 76.15  ? 657 PRO A CB    1 
ATOM   5405 C  CG    . PRO A 1 657 ? 13.826  -0.669  37.882  1.00 78.51  ? 657 PRO A CG    1 
ATOM   5406 C  CD    . PRO A 1 657 ? 14.453  0.077   39.026  1.00 78.14  ? 657 PRO A CD    1 
ATOM   5407 N  N     . GLU A 1 658 ? 16.047  2.816   36.893  1.00 84.48  ? 658 GLU A N     1 
ATOM   5408 C  CA    . GLU A 1 658 ? 16.455  4.065   36.260  1.00 84.90  ? 658 GLU A CA    1 
ATOM   5409 C  C     . GLU A 1 658 ? 17.956  4.104   36.011  1.00 81.91  ? 658 GLU A C     1 
ATOM   5410 O  O     . GLU A 1 658 ? 18.408  4.730   35.048  1.00 90.98  ? 658 GLU A O     1 
ATOM   5411 C  CB    . GLU A 1 658 ? 16.034  5.249   37.133  1.00 83.38  ? 658 GLU A CB    1 
ATOM   5412 C  CG    . GLU A 1 658 ? 14.527  5.426   37.286  1.00 86.52  ? 658 GLU A CG    1 
ATOM   5413 C  CD    . GLU A 1 658 ? 13.933  4.554   38.386  1.00 96.54  ? 658 GLU A CD    1 
ATOM   5414 O  OE1   . GLU A 1 658 ? 14.651  3.682   38.922  1.00 99.23  ? 658 GLU A OE1   1 
ATOM   5415 O  OE2   . GLU A 1 658 ? 12.742  4.739   38.715  1.00 84.89  ? 658 GLU A OE2   1 
ATOM   5416 N  N     . LYS A 1 659 ? 18.741  3.450   36.864  1.00 79.45  ? 659 LYS A N     1 
ATOM   5417 C  CA    . LYS A 1 659 ? 20.187  3.440   36.695  1.00 85.94  ? 659 LYS A CA    1 
ATOM   5418 C  C     . LYS A 1 659 ? 20.651  2.461   35.625  1.00 83.05  ? 659 LYS A C     1 
ATOM   5419 O  O     . LYS A 1 659 ? 21.850  2.413   35.333  1.00 78.34  ? 659 LYS A O     1 
ATOM   5420 C  CB    . LYS A 1 659 ? 20.869  3.117   38.027  1.00 71.97  ? 659 LYS A CB    1 
ATOM   5421 C  CG    . LYS A 1 659 ? 20.513  4.082   39.147  1.00 69.91  ? 659 LYS A CG    1 
ATOM   5422 C  CD    . LYS A 1 659 ? 21.127  3.654   40.471  1.00 73.14  ? 659 LYS A CD    1 
ATOM   5423 C  CE    . LYS A 1 659 ? 21.602  4.858   41.271  1.00 79.59  ? 659 LYS A CE    1 
ATOM   5424 N  NZ    . LYS A 1 659 ? 22.417  4.462   42.454  1.00 85.54  ? 659 LYS A NZ    1 
ATOM   5425 N  N     . LEU A 1 660 ? 19.739  1.695   35.028  1.00 75.45  ? 660 LEU A N     1 
ATOM   5426 C  CA    . LEU A 1 660 ? 20.094  0.709   34.017  1.00 72.14  ? 660 LEU A CA    1 
ATOM   5427 C  C     . LEU A 1 660 ? 19.614  1.112   32.626  1.00 72.02  ? 660 LEU A C     1 
ATOM   5428 O  O     . LEU A 1 660 ? 19.569  0.272   31.722  1.00 73.23  ? 660 LEU A O     1 
ATOM   5429 C  CB    . LEU A 1 660 ? 19.531  -0.659  34.400  1.00 63.78  ? 660 LEU A CB    1 
ATOM   5430 C  CG    . LEU A 1 660 ? 19.945  -1.161  35.786  1.00 73.00  ? 660 LEU A CG    1 
ATOM   5431 C  CD1   . LEU A 1 660 ? 18.739  -1.672  36.545  1.00 82.51  ? 660 LEU A CD1   1 
ATOM   5432 C  CD2   . LEU A 1 660 ? 21.008  -2.232  35.703  1.00 81.22  ? 660 LEU A CD2   1 
ATOM   5433 N  N     . VAL A 1 661 ? 19.252  2.377   32.437  1.00 74.87  ? 661 VAL A N     1 
ATOM   5434 C  CA    . VAL A 1 661 ? 18.762  2.863   31.152  1.00 69.78  ? 661 VAL A CA    1 
ATOM   5435 C  C     . VAL A 1 661 ? 19.943  3.260   30.276  1.00 70.71  ? 661 VAL A C     1 
ATOM   5436 O  O     . VAL A 1 661 ? 20.838  3.994   30.712  1.00 62.95  ? 661 VAL A O     1 
ATOM   5437 C  CB    . VAL A 1 661 ? 17.789  4.040   31.337  1.00 66.20  ? 661 VAL A CB    1 
ATOM   5438 C  CG1   . VAL A 1 661 ? 16.983  4.256   30.069  1.00 69.93  ? 661 VAL A CG1   1 
ATOM   5439 C  CG2   . VAL A 1 661 ? 16.856  3.769   32.503  1.00 73.72  ? 661 VAL A CG2   1 
ATOM   5440 N  N     . ILE A 1 662 ? 19.942  2.773   29.039  1.00 72.67  ? 662 ILE A N     1 
ATOM   5441 C  CA    . ILE A 1 662 ? 20.962  3.101   28.051  1.00 64.10  ? 662 ILE A CA    1 
ATOM   5442 C  C     . ILE A 1 662 ? 20.367  4.113   27.082  1.00 65.13  ? 662 ILE A C     1 
ATOM   5443 O  O     . ILE A 1 662 ? 19.325  3.856   26.467  1.00 86.32  ? 662 ILE A O     1 
ATOM   5444 C  CB    . ILE A 1 662 ? 21.448  1.846   27.309  1.00 66.69  ? 662 ILE A CB    1 
ATOM   5445 C  CG1   . ILE A 1 662 ? 22.114  0.872   28.283  1.00 63.40  ? 662 ILE A CG1   1 
ATOM   5446 C  CG2   . ILE A 1 662 ? 22.401  2.226   26.184  1.00 68.14  ? 662 ILE A CG2   1 
ATOM   5447 C  CD1   . ILE A 1 662 ? 22.089  -0.567  27.819  1.00 64.88  ? 662 ILE A CD1   1 
ATOM   5448 N  N     . HIS A 1 663 ? 21.020  5.263   26.947  1.00 68.76  ? 663 HIS A N     1 
ATOM   5449 C  CA    . HIS A 1 663 ? 20.563  6.322   26.056  1.00 73.73  ? 663 HIS A CA    1 
ATOM   5450 C  C     . HIS A 1 663 ? 21.428  6.333   24.802  1.00 72.59  ? 663 HIS A C     1 
ATOM   5451 O  O     . HIS A 1 663 ? 22.638  6.568   24.881  1.00 78.31  ? 663 HIS A O     1 
ATOM   5452 C  CB    . HIS A 1 663 ? 20.613  7.684   26.749  1.00 71.91  ? 663 HIS A CB    1 
ATOM   5453 C  CG    . HIS A 1 663 ? 19.887  7.725   28.058  1.00 69.91  ? 663 HIS A CG    1 
ATOM   5454 N  ND1   . HIS A 1 663 ? 18.517  7.844   28.146  1.00 71.25  ? 663 HIS A ND1   1 
ATOM   5455 C  CD2   . HIS A 1 663 ? 20.342  7.670   29.332  1.00 68.84  ? 663 HIS A CD2   1 
ATOM   5456 C  CE1   . HIS A 1 663 ? 18.158  7.856   29.417  1.00 73.95  ? 663 HIS A CE1   1 
ATOM   5457 N  NE2   . HIS A 1 663 ? 19.247  7.753   30.158  1.00 69.94  ? 663 HIS A NE2   1 
ATOM   5458 N  N     . LYS A 1 664 ? 20.807  6.087   23.650  1.00 72.45  ? 664 LYS A N     1 
ATOM   5459 C  CA    . LYS A 1 664 ? 21.505  6.115   22.372  1.00 65.32  ? 664 LYS A CA    1 
ATOM   5460 C  C     . LYS A 1 664 ? 20.626  6.810   21.345  1.00 70.36  ? 664 LYS A C     1 
ATOM   5461 O  O     . LYS A 1 664 ? 19.427  6.529   21.257  1.00 81.25  ? 664 LYS A O     1 
ATOM   5462 C  CB    . LYS A 1 664 ? 21.869  4.702   21.904  1.00 64.53  ? 664 LYS A CB    1 
ATOM   5463 C  CG    . LYS A 1 664 ? 23.361  4.486   21.710  1.00 73.52  ? 664 LYS A CG    1 
ATOM   5464 C  CD    . LYS A 1 664 ? 23.678  3.035   21.391  1.00 83.07  ? 664 LYS A CD    1 
ATOM   5465 C  CE    . LYS A 1 664 ? 24.327  2.339   22.577  1.00 76.09  ? 664 LYS A CE    1 
ATOM   5466 N  NZ    . LYS A 1 664 ? 24.923  1.028   22.196  1.00 76.29  ? 664 LYS A NZ    1 
ATOM   5467 N  N     . GLN A 1 665 ? 21.225  7.710   20.574  1.00 65.51  ? 665 GLN A N     1 
ATOM   5468 C  CA    . GLN A 1 665 ? 20.496  8.532   19.620  1.00 74.82  ? 665 GLN A CA    1 
ATOM   5469 C  C     . GLN A 1 665 ? 20.534  7.908   18.231  1.00 75.52  ? 665 GLN A C     1 
ATOM   5470 O  O     . GLN A 1 665 ? 21.559  7.367   17.807  1.00 80.79  ? 665 GLN A O     1 
ATOM   5471 C  CB    . GLN A 1 665 ? 21.092  9.943   19.587  1.00 65.75  ? 665 GLN A CB    1 
ATOM   5472 C  CG    . GLN A 1 665 ? 21.106  10.613  18.225  1.00 71.20  ? 665 GLN A CG    1 
ATOM   5473 C  CD    . GLN A 1 665 ? 21.896  11.909  18.223  1.00 86.64  ? 665 GLN A CD    1 
ATOM   5474 O  OE1   . GLN A 1 665 ? 22.254  12.435  19.277  1.00 86.16  ? 665 GLN A OE1   1 
ATOM   5475 N  NE2   . GLN A 1 665 ? 22.173  12.429  17.033  1.00 87.70  ? 665 GLN A NE2   1 
ATOM   5476 N  N     . ILE A 1 666 ? 19.405  7.976   17.529  1.00 79.59  ? 666 ILE A N     1 
ATOM   5477 C  CA    . ILE A 1 666 ? 19.347  7.567   16.131  1.00 79.43  ? 666 ILE A CA    1 
ATOM   5478 C  C     . ILE A 1 666 ? 19.785  8.749   15.278  1.00 81.98  ? 666 ILE A C     1 
ATOM   5479 O  O     . ILE A 1 666 ? 19.509  9.911   15.596  1.00 77.63  ? 666 ILE A O     1 
ATOM   5480 C  CB    . ILE A 1 666 ? 17.942  7.038   15.752  1.00 77.14  ? 666 ILE A CB    1 
ATOM   5481 C  CG1   . ILE A 1 666 ? 16.920  8.157   15.533  1.00 85.73  ? 666 ILE A CG1   1 
ATOM   5482 C  CG2   . ILE A 1 666 ? 17.438  6.057   16.792  1.00 68.73  ? 666 ILE A CG2   1 
ATOM   5483 C  CD1   . ILE A 1 666 ? 16.797  8.602   14.093  1.00 97.69  ? 666 ILE A CD1   1 
ATOM   5484 N  N     . THR A 1 667 ? 20.488  8.455   14.186  1.00 91.48  ? 667 THR A N     1 
ATOM   5485 C  CA    . THR A 1 667 ? 21.185  9.476   13.417  1.00 88.08  ? 667 THR A CA    1 
ATOM   5486 C  C     . THR A 1 667 ? 20.690  9.609   11.985  1.00 86.91  ? 667 THR A C     1 
ATOM   5487 O  O     . THR A 1 667 ? 21.197  10.463  11.248  1.00 97.95  ? 667 THR A O     1 
ATOM   5488 C  CB    . THR A 1 667 ? 22.692  9.181   13.399  1.00 79.70  ? 667 THR A CB    1 
ATOM   5489 O  OG1   . THR A 1 667 ? 22.937  7.999   12.627  1.00 87.59  ? 667 THR A OG1   1 
ATOM   5490 C  CG2   . THR A 1 667 ? 23.207  8.968   14.815  1.00 59.33  ? 667 THR A CG2   1 
ATOM   5491 N  N     . ARG A 1 668 ? 19.721  8.803   11.570  1.00 95.31  ? 668 ARG A N     1 
ATOM   5492 C  CA    . ARG A 1 668 ? 19.291  8.773   10.181  1.00 89.98  ? 668 ARG A CA    1 
ATOM   5493 C  C     . ARG A 1 668 ? 17.899  8.164   10.142  1.00 100.70 ? 668 ARG A C     1 
ATOM   5494 O  O     . ARG A 1 668 ? 17.341  7.778   11.174  1.00 94.62  ? 668 ARG A O     1 
ATOM   5495 C  CB    . ARG A 1 668 ? 20.276  7.972   9.329   1.00 97.63  ? 668 ARG A CB    1 
ATOM   5496 C  CG    . ARG A 1 668 ? 20.721  6.679   9.999   1.00 98.09  ? 668 ARG A CG    1 
ATOM   5497 C  CD    . ARG A 1 668 ? 21.801  5.969   9.208   1.00 103.78 ? 668 ARG A CD    1 
ATOM   5498 N  NE    . ARG A 1 668 ? 23.119  6.211   9.778   1.00 102.58 ? 668 ARG A NE    1 
ATOM   5499 C  CZ    . ARG A 1 668 ? 24.222  5.574   9.412   1.00 109.70 ? 668 ARG A CZ    1 
ATOM   5500 N  NH1   . ARG A 1 668 ? 24.200  4.634   8.481   1.00 106.29 ? 668 ARG A NH1   1 
ATOM   5501 N  NH2   . ARG A 1 668 ? 25.376  5.886   9.995   1.00 110.92 ? 668 ARG A NH2   1 
ATOM   5502 N  N     . ASP A 1 669 ? 17.342  8.057   8.940   1.00 103.11 ? 669 ASP A N     1 
ATOM   5503 C  CA    . ASP A 1 669 ? 16.046  7.417   8.811   1.00 97.72  ? 669 ASP A CA    1 
ATOM   5504 C  C     . ASP A 1 669 ? 16.264  5.908   8.820   1.00 101.80 ? 669 ASP A C     1 
ATOM   5505 O  O     . ASP A 1 669 ? 17.284  5.401   8.337   1.00 104.61 ? 669 ASP A O     1 
ATOM   5506 C  CB    . ASP A 1 669 ? 15.330  7.900   7.545   1.00 102.42 ? 669 ASP A CB    1 
ATOM   5507 C  CG    . ASP A 1 669 ? 14.261  6.940   7.040   1.00 121.60 ? 669 ASP A CG    1 
ATOM   5508 O  OD1   . ASP A 1 669 ? 13.779  6.056   7.788   1.00 137.29 ? 669 ASP A OD1   1 
ATOM   5509 O  OD2   . ASP A 1 669 ? 13.833  7.138   5.887   1.00 124.75 ? 669 ASP A OD2   1 
ATOM   5510 N  N     . LEU A 1 670 ? 15.291  5.196   9.389   1.00 98.61  ? 670 LEU A N     1 
ATOM   5511 C  CA    . LEU A 1 670 ? 15.480  3.802   9.764   1.00 96.04  ? 670 LEU A CA    1 
ATOM   5512 C  C     . LEU A 1 670 ? 15.557  2.881   8.558   1.00 109.98 ? 670 LEU A C     1 
ATOM   5513 O  O     . LEU A 1 670 ? 16.046  1.754   8.693   1.00 111.08 ? 670 LEU A O     1 
ATOM   5514 C  CB    . LEU A 1 670 ? 14.363  3.362   10.716  1.00 92.52  ? 670 LEU A CB    1 
ATOM   5515 C  CG    . LEU A 1 670 ? 14.325  3.956   12.139  1.00 92.72  ? 670 LEU A CG    1 
ATOM   5516 C  CD1   . LEU A 1 670 ? 14.201  5.462   12.145  1.00 98.95  ? 670 LEU A CD1   1 
ATOM   5517 C  CD2   . LEU A 1 670 ? 13.191  3.363   12.957  1.00 91.69  ? 670 LEU A CD2   1 
ATOM   5518 N  N     . LYS A 1 671 ? 15.094  3.326   7.387   1.00 110.24 ? 671 LYS A N     1 
ATOM   5519 C  CA    . LYS A 1 671 ? 15.324  2.533   6.188   1.00 109.38 ? 671 LYS A CA    1 
ATOM   5520 C  C     . LYS A 1 671 ? 16.795  2.560   5.789   1.00 108.41 ? 671 LYS A C     1 
ATOM   5521 O  O     . LYS A 1 671 ? 17.287  1.602   5.183   1.00 117.35 ? 671 LYS A O     1 
ATOM   5522 C  CB    . LYS A 1 671 ? 14.460  3.026   5.021   1.00 105.76 ? 671 LYS A CB    1 
ATOM   5523 C  CG    . LYS A 1 671 ? 15.015  4.256   4.301   1.00 110.47 ? 671 LYS A CG    1 
ATOM   5524 C  CD    . LYS A 1 671 ? 13.936  5.151   3.719   1.00 118.24 ? 671 LYS A CD    1 
ATOM   5525 C  CE    . LYS A 1 671 ? 14.553  6.290   2.924   1.00 118.18 ? 671 LYS A CE    1 
ATOM   5526 N  NZ    . LYS A 1 671 ? 14.614  7.544   3.699   1.00 118.97 ? 671 LYS A NZ    1 
ATOM   5527 N  N     . ASP A 1 672 ? 17.515  3.633   6.131   1.00 103.15 ? 672 ASP A N     1 
ATOM   5528 C  CA    . ASP A 1 672 ? 18.921  3.794   5.771   1.00 112.06 ? 672 ASP A CA    1 
ATOM   5529 C  C     . ASP A 1 672 ? 19.873  3.113   6.749   1.00 107.89 ? 672 ASP A C     1 
ATOM   5530 O  O     . ASP A 1 672 ? 21.074  3.405   6.730   1.00 107.36 ? 672 ASP A O     1 
ATOM   5531 C  CB    . ASP A 1 672 ? 19.275  5.281   5.656   1.00 109.58 ? 672 ASP A CB    1 
ATOM   5532 C  CG    . ASP A 1 672 ? 18.502  5.986   4.558   1.00 112.49 ? 672 ASP A CG    1 
ATOM   5533 O  OD1   . ASP A 1 672 ? 18.493  7.234   4.545   1.00 114.12 ? 672 ASP A OD1   1 
ATOM   5534 O  OD2   . ASP A 1 672 ? 17.916  5.293   3.702   1.00 119.37 ? 672 ASP A OD2   1 
ATOM   5535 N  N     . TYR A 1 673 ? 19.375  2.222   7.600   1.00 98.02  ? 673 TYR A N     1 
ATOM   5536 C  CA    . TYR A 1 673 ? 20.219  1.524   8.558   1.00 94.88  ? 673 TYR A CA    1 
ATOM   5537 C  C     . TYR A 1 673 ? 20.647  0.180   7.984   1.00 96.94  ? 673 TYR A C     1 
ATOM   5538 O  O     . TYR A 1 673 ? 19.819  -0.576  7.468   1.00 105.43 ? 673 TYR A O     1 
ATOM   5539 C  CB    . TYR A 1 673 ? 19.488  1.329   9.885   1.00 96.34  ? 673 TYR A CB    1 
ATOM   5540 C  CG    . TYR A 1 673 ? 19.798  2.397   10.909  1.00 93.42  ? 673 TYR A CG    1 
ATOM   5541 C  CD1   . TYR A 1 673 ? 21.063  2.499   11.472  1.00 97.24  ? 673 TYR A CD1   1 
ATOM   5542 C  CD2   . TYR A 1 673 ? 18.826  3.302   11.313  1.00 87.23  ? 673 TYR A CD2   1 
ATOM   5543 C  CE1   . TYR A 1 673 ? 21.352  3.474   12.407  1.00 90.37  ? 673 TYR A CE1   1 
ATOM   5544 C  CE2   . TYR A 1 673 ? 19.105  4.280   12.248  1.00 87.75  ? 673 TYR A CE2   1 
ATOM   5545 C  CZ    . TYR A 1 673 ? 20.370  4.362   12.791  1.00 82.36  ? 673 TYR A CZ    1 
ATOM   5546 O  OH    . TYR A 1 673 ? 20.651  5.333   13.724  1.00 88.01  ? 673 TYR A OH    1 
ATOM   5547 N  N     . LYS A 1 674 ? 21.945  -0.106  8.070   1.00 100.60 ? 674 LYS A N     1 
ATOM   5548 C  CA    . LYS A 1 674 ? 22.501  -1.366  7.599   1.00 101.45 ? 674 LYS A CA    1 
ATOM   5549 C  C     . LYS A 1 674 ? 22.851  -2.319  8.733   1.00 99.72  ? 674 LYS A C     1 
ATOM   5550 O  O     . LYS A 1 674 ? 23.184  -3.478  8.466   1.00 99.14  ? 674 LYS A O     1 
ATOM   5551 C  CB    . LYS A 1 674 ? 23.750  -1.106  6.749   1.00 99.19  ? 674 LYS A CB    1 
ATOM   5552 C  CG    . LYS A 1 674 ? 23.551  -0.074  5.649   1.00 105.83 ? 674 LYS A CG    1 
ATOM   5553 C  CD    . LYS A 1 674 ? 24.736  -0.053  4.696   1.00 110.65 ? 674 LYS A CD    1 
ATOM   5554 C  CE    . LYS A 1 674 ? 24.289  -0.210  3.251   1.00 107.55 ? 674 LYS A CE    1 
ATOM   5555 N  NZ    . LYS A 1 674 ? 25.429  -0.503  2.337   1.00 110.29 ? 674 LYS A NZ    1 
ATOM   5556 N  N     . ALA A 1 675 ? 22.787  -1.861  9.982   1.00 108.45 ? 675 ALA A N     1 
ATOM   5557 C  CA    . ALA A 1 675 ? 23.079  -2.697  11.143  1.00 101.73 ? 675 ALA A CA    1 
ATOM   5558 C  C     . ALA A 1 675 ? 22.122  -2.297  12.255  1.00 101.71 ? 675 ALA A C     1 
ATOM   5559 O  O     . ALA A 1 675 ? 22.210  -1.182  12.781  1.00 94.09  ? 675 ALA A O     1 
ATOM   5560 C  CB    . ALA A 1 675 ? 24.534  -2.548  11.587  1.00 96.38  ? 675 ALA A CB    1 
ATOM   5561 N  N     . THR A 1 676 ? 21.212  -3.200  12.611  1.00 93.79  ? 676 THR A N     1 
ATOM   5562 C  CA    . THR A 1 676 ? 20.175  -2.914  13.600  1.00 98.50  ? 676 THR A CA    1 
ATOM   5563 C  C     . THR A 1 676 ? 20.673  -3.350  14.974  1.00 94.26  ? 676 THR A C     1 
ATOM   5564 O  O     . THR A 1 676 ? 20.586  -4.525  15.339  1.00 89.98  ? 676 THR A O     1 
ATOM   5565 C  CB    . THR A 1 676 ? 18.870  -3.609  13.229  1.00 87.95  ? 676 THR A CB    1 
ATOM   5566 O  OG1   . THR A 1 676 ? 18.359  -3.044  12.015  1.00 93.50  ? 676 THR A OG1   1 
ATOM   5567 C  CG2   . THR A 1 676 ? 17.836  -3.431  14.328  1.00 86.46  ? 676 THR A CG2   1 
ATOM   5568 N  N     . GLY A 1 677 ? 21.210  -2.399  15.731  1.00 82.38  ? 677 GLY A N     1 
ATOM   5569 C  CA    . GLY A 1 677 ? 21.537  -2.628  17.118  1.00 81.89  ? 677 GLY A CA    1 
ATOM   5570 C  C     . GLY A 1 677 ? 20.324  -2.467  18.003  1.00 82.60  ? 677 GLY A C     1 
ATOM   5571 O  O     . GLY A 1 677 ? 19.230  -2.080  17.561  1.00 89.75  ? 677 GLY A O     1 
ATOM   5572 N  N     . PRO A 1 678 ? 20.505  -2.772  19.293  1.00 77.17  ? 678 PRO A N     1 
ATOM   5573 C  CA    . PRO A 1 678 ? 19.366  -2.721  20.229  1.00 85.13  ? 678 PRO A CA    1 
ATOM   5574 C  C     . PRO A 1 678 ? 18.588  -1.415  20.199  1.00 82.60  ? 678 PRO A C     1 
ATOM   5575 O  O     . PRO A 1 678 ? 17.352  -1.441  20.259  1.00 78.34  ? 678 PRO A O     1 
ATOM   5576 C  CB    . PRO A 1 678 ? 20.032  -2.949  21.592  1.00 72.38  ? 678 PRO A CB    1 
ATOM   5577 C  CG    . PRO A 1 678 ? 21.252  -3.736  21.287  1.00 75.55  ? 678 PRO A CG    1 
ATOM   5578 C  CD    . PRO A 1 678 ? 21.722  -3.312  19.921  1.00 76.68  ? 678 PRO A CD    1 
ATOM   5579 N  N     . HIS A 1 679 ? 19.270  -0.271  20.100  1.00 76.84  ? 679 HIS A N     1 
ATOM   5580 C  CA    . HIS A 1 679 ? 18.557  1.004   20.107  1.00 78.83  ? 679 HIS A CA    1 
ATOM   5581 C  C     . HIS A 1 679 ? 17.800  1.235   18.805  1.00 80.05  ? 679 HIS A C     1 
ATOM   5582 O  O     . HIS A 1 679 ? 16.717  1.829   18.820  1.00 73.27  ? 679 HIS A O     1 
ATOM   5583 C  CB    . HIS A 1 679 ? 19.531  2.155   20.382  1.00 78.93  ? 679 HIS A CB    1 
ATOM   5584 C  CG    . HIS A 1 679 ? 20.336  2.576   19.190  1.00 74.87  ? 679 HIS A CG    1 
ATOM   5585 N  ND1   . HIS A 1 679 ? 21.156  1.710   18.499  1.00 74.07  ? 679 HIS A ND1   1 
ATOM   5586 C  CD2   . HIS A 1 679 ? 20.456  3.777   18.575  1.00 70.93  ? 679 HIS A CD2   1 
ATOM   5587 C  CE1   . HIS A 1 679 ? 21.740  2.356   17.506  1.00 66.51  ? 679 HIS A CE1   1 
ATOM   5588 N  NE2   . HIS A 1 679 ? 21.332  3.612   17.530  1.00 66.62  ? 679 HIS A NE2   1 
ATOM   5589 N  N     . VAL A 1 680 ? 18.341  0.770   17.678  1.00 83.93  ? 680 VAL A N     1 
ATOM   5590 C  CA    . VAL A 1 680 ? 17.639  0.924   16.408  1.00 78.73  ? 680 VAL A CA    1 
ATOM   5591 C  C     . VAL A 1 680 ? 16.440  -0.013  16.351  1.00 85.64  ? 680 VAL A C     1 
ATOM   5592 O  O     . VAL A 1 680 ? 15.367  0.359   15.860  1.00 84.80  ? 680 VAL A O     1 
ATOM   5593 C  CB    . VAL A 1 680 ? 18.610  0.689   15.234  1.00 81.45  ? 680 VAL A CB    1 
ATOM   5594 C  CG1   . VAL A 1 680 ? 17.872  0.179   13.999  1.00 86.77  ? 680 VAL A CG1   1 
ATOM   5595 C  CG2   . VAL A 1 680 ? 19.370  1.960   14.918  1.00 81.38  ? 680 VAL A CG2   1 
ATOM   5596 N  N     . ALA A 1 681 ? 16.600  -1.238  16.862  1.00 83.25  ? 681 ALA A N     1 
ATOM   5597 C  CA    . ALA A 1 681 ? 15.493  -2.190  16.884  1.00 80.31  ? 681 ALA A CA    1 
ATOM   5598 C  C     . ALA A 1 681 ? 14.318  -1.653  17.690  1.00 89.37  ? 681 ALA A C     1 
ATOM   5599 O  O     . ALA A 1 681 ? 13.157  -1.828  17.301  1.00 86.23  ? 681 ALA A O     1 
ATOM   5600 C  CB    . ALA A 1 681 ? 15.963  -3.530  17.451  1.00 82.13  ? 681 ALA A CB    1 
ATOM   5601 N  N     . VAL A 1 682 ? 14.600  -0.997  18.817  1.00 81.46  ? 682 VAL A N     1 
ATOM   5602 C  CA    . VAL A 1 682 ? 13.535  -0.385  19.606  1.00 81.81  ? 682 VAL A CA    1 
ATOM   5603 C  C     . VAL A 1 682 ? 12.870  0.735   18.817  1.00 81.32  ? 682 VAL A C     1 
ATOM   5604 O  O     . VAL A 1 682 ? 11.638  0.835   18.770  1.00 91.72  ? 682 VAL A O     1 
ATOM   5605 C  CB    . VAL A 1 682 ? 14.089  0.117   20.952  1.00 82.33  ? 682 VAL A CB    1 
ATOM   5606 C  CG1   . VAL A 1 682 ? 13.097  1.054   21.623  1.00 77.70  ? 682 VAL A CG1   1 
ATOM   5607 C  CG2   . VAL A 1 682 ? 14.426  -1.056  21.860  1.00 81.45  ? 682 VAL A CG2   1 
ATOM   5608 N  N     . ALA A 1 683 ? 13.672  1.585   18.169  1.00 74.29  ? 683 ALA A N     1 
ATOM   5609 C  CA    . ALA A 1 683 ? 13.124  2.693   17.396  1.00 84.69  ? 683 ALA A CA    1 
ATOM   5610 C  C     . ALA A 1 683 ? 12.308  2.226   16.198  1.00 95.51  ? 683 ALA A C     1 
ATOM   5611 O  O     . ALA A 1 683 ? 11.454  2.980   15.718  1.00 99.95  ? 683 ALA A O     1 
ATOM   5612 C  CB    . ALA A 1 683 ? 14.249  3.617   16.927  1.00 67.48  ? 683 ALA A CB    1 
ATOM   5613 N  N     . LYS A 1 684 ? 12.547  1.010   15.702  1.00 95.09  ? 684 LYS A N     1 
ATOM   5614 C  CA    . LYS A 1 684 ? 11.781  0.512   14.565  1.00 84.61  ? 684 LYS A CA    1 
ATOM   5615 C  C     . LYS A 1 684 ? 10.401  0.025   14.990  1.00 91.13  ? 684 LYS A C     1 
ATOM   5616 O  O     . LYS A 1 684 ? 9.414   0.264   14.285  1.00 97.99  ? 684 LYS A O     1 
ATOM   5617 C  CB    . LYS A 1 684 ? 12.551  -0.602  13.853  1.00 78.36  ? 684 LYS A CB    1 
ATOM   5618 C  CG    . LYS A 1 684 ? 13.696  -0.093  12.990  1.00 75.91  ? 684 LYS A CG    1 
ATOM   5619 C  CD    . LYS A 1 684 ? 14.678  -1.191  12.623  1.00 88.79  ? 684 LYS A CD    1 
ATOM   5620 C  CE    . LYS A 1 684 ? 14.607  -1.511  11.137  1.00 93.32  ? 684 LYS A CE    1 
ATOM   5621 N  NZ    . LYS A 1 684 ? 15.952  -1.461  10.499  1.00 85.78  ? 684 LYS A NZ    1 
ATOM   5622 N  N     . ARG A 1 685 ? 10.311  -0.658  16.134  1.00 90.95  ? 685 ARG A N     1 
ATOM   5623 C  CA    . ARG A 1 685 ? 9.005   -1.041  16.658  1.00 97.90  ? 685 ARG A CA    1 
ATOM   5624 C  C     . ARG A 1 685 ? 8.198   0.166   17.113  1.00 98.86  ? 685 ARG A C     1 
ATOM   5625 O  O     . ARG A 1 685 ? 6.966   0.086   17.172  1.00 108.10 ? 685 ARG A O     1 
ATOM   5626 C  CB    . ARG A 1 685 ? 9.162   -2.029  17.815  1.00 87.46  ? 685 ARG A CB    1 
ATOM   5627 C  CG    . ARG A 1 685 ? 10.213  -3.098  17.584  1.00 85.93  ? 685 ARG A CG    1 
ATOM   5628 C  CD    . ARG A 1 685 ? 9.998   -4.288  18.502  1.00 80.99  ? 685 ARG A CD    1 
ATOM   5629 N  NE    . ARG A 1 685 ? 10.846  -4.224  19.686  1.00 102.31 ? 685 ARG A NE    1 
ATOM   5630 C  CZ    . ARG A 1 685 ? 12.132  -4.546  19.707  1.00 104.59 ? 685 ARG A CZ    1 
ATOM   5631 N  NH1   . ARG A 1 685 ? 12.758  -4.965  18.619  1.00 104.19 ? 685 ARG A NH1   1 
ATOM   5632 N  NH2   . ARG A 1 685 ? 12.807  -4.448  20.849  1.00 87.70  ? 685 ARG A NH2   1 
ATOM   5633 N  N     . LEU A 1 686 ? 8.861   1.278   17.438  1.00 93.94  ? 686 LEU A N     1 
ATOM   5634 C  CA    . LEU A 1 686 ? 8.132   2.503   17.751  1.00 100.60 ? 686 LEU A CA    1 
ATOM   5635 C  C     . LEU A 1 686 ? 7.544   3.123   16.490  1.00 110.53 ? 686 LEU A C     1 
ATOM   5636 O  O     . LEU A 1 686 ? 6.408   3.611   16.503  1.00 111.54 ? 686 LEU A O     1 
ATOM   5637 C  CB    . LEU A 1 686 ? 9.050   3.496   18.465  1.00 91.16  ? 686 LEU A CB    1 
ATOM   5638 C  CG    . LEU A 1 686 ? 9.582   3.074   19.838  1.00 90.21  ? 686 LEU A CG    1 
ATOM   5639 C  CD1   . LEU A 1 686 ? 9.969   4.291   20.667  1.00 72.30  ? 686 LEU A CD1   1 
ATOM   5640 C  CD2   . LEU A 1 686 ? 8.566   2.218   20.578  1.00 80.32  ? 686 LEU A CD2   1 
ATOM   5641 N  N     . ALA A 1 687 ? 8.298   3.104   15.387  1.00 105.35 ? 687 ALA A N     1 
ATOM   5642 C  CA    . ALA A 1 687 ? 7.762   3.564   14.113  1.00 101.96 ? 687 ALA A CA    1 
ATOM   5643 C  C     . ALA A 1 687 ? 6.581   2.721   13.654  1.00 104.78 ? 687 ALA A C     1 
ATOM   5644 O  O     . ALA A 1 687 ? 5.760   3.199   12.863  1.00 98.07  ? 687 ALA A O     1 
ATOM   5645 C  CB    . ALA A 1 687 ? 8.857   3.558   13.046  1.00 92.79  ? 687 ALA A CB    1 
ATOM   5646 N  N     . ALA A 1 688 ? 6.478   1.477   14.129  1.00 106.37 ? 688 ALA A N     1 
ATOM   5647 C  CA    . ALA A 1 688 ? 5.314   0.653   13.829  1.00 105.33 ? 688 ALA A CA    1 
ATOM   5648 C  C     . ALA A 1 688 ? 4.075   1.109   14.588  1.00 116.40 ? 688 ALA A C     1 
ATOM   5649 O  O     . ALA A 1 688 ? 2.958   0.757   14.193  1.00 100.83 ? 688 ALA A O     1 
ATOM   5650 C  CB    . ALA A 1 688 ? 5.611   -0.814  14.141  1.00 87.30  ? 688 ALA A CB    1 
ATOM   5651 N  N     . ARG A 1 689 ? 4.244   1.871   15.667  1.00 118.70 ? 689 ARG A N     1 
ATOM   5652 C  CA    . ARG A 1 689 ? 3.127   2.495   16.364  1.00 120.97 ? 689 ARG A CA    1 
ATOM   5653 C  C     . ARG A 1 689 ? 2.871   3.922   15.900  1.00 110.82 ? 689 ARG A C     1 
ATOM   5654 O  O     . ARG A 1 689 ? 1.996   4.592   16.458  1.00 114.26 ? 689 ARG A O     1 
ATOM   5655 C  CB    . ARG A 1 689 ? 3.364   2.496   17.879  1.00 122.56 ? 689 ARG A CB    1 
ATOM   5656 C  CG    . ARG A 1 689 ? 4.110   1.292   18.417  1.00 115.84 ? 689 ARG A CG    1 
ATOM   5657 C  CD    . ARG A 1 689 ? 3.847   1.130   19.905  1.00 118.95 ? 689 ARG A CD    1 
ATOM   5658 N  NE    . ARG A 1 689 ? 5.038   0.700   20.625  1.00 138.66 ? 689 ARG A NE    1 
ATOM   5659 C  CZ    . ARG A 1 689 ? 5.300   1.004   21.888  1.00 136.38 ? 689 ARG A CZ    1 
ATOM   5660 N  NH1   . ARG A 1 689 ? 4.469   1.740   22.609  1.00 135.68 ? 689 ARG A NH1   1 
ATOM   5661 N  NH2   . ARG A 1 689 ? 6.425   0.563   22.441  1.00 109.23 ? 689 ARG A NH2   1 
ATOM   5662 N  N     . GLY A 1 690 ? 3.613   4.403   14.906  1.00 107.61 ? 690 GLY A N     1 
ATOM   5663 C  CA    . GLY A 1 690 ? 3.429   5.751   14.409  1.00 101.24 ? 690 GLY A CA    1 
ATOM   5664 C  C     . GLY A 1 690 ? 3.898   6.817   15.376  1.00 106.56 ? 690 GLY A C     1 
ATOM   5665 O  O     . GLY A 1 690 ? 3.094   7.612   15.871  1.00 114.07 ? 690 GLY A O     1 
ATOM   5666 N  N     . VAL A 1 691 ? 5.199   6.840   15.659  1.00 106.79 ? 691 VAL A N     1 
ATOM   5667 C  CA    . VAL A 1 691 ? 5.796   7.847   16.524  1.00 107.87 ? 691 VAL A CA    1 
ATOM   5668 C  C     . VAL A 1 691 ? 6.828   8.625   15.716  1.00 108.93 ? 691 VAL A C     1 
ATOM   5669 O  O     . VAL A 1 691 ? 7.326   8.164   14.686  1.00 109.79 ? 691 VAL A O     1 
ATOM   5670 C  CB    . VAL A 1 691 ? 6.433   7.229   17.788  1.00 107.29 ? 691 VAL A CB    1 
ATOM   5671 C  CG1   . VAL A 1 691 ? 6.574   8.273   18.886  1.00 109.91 ? 691 VAL A CG1   1 
ATOM   5672 C  CG2   . VAL A 1 691 ? 5.600   6.063   18.284  1.00 96.79  ? 691 VAL A CG2   1 
ATOM   5673 N  N     . LYS A 1 692 ? 7.136   9.830   16.193  1.00 108.65 ? 692 LYS A N     1 
ATOM   5674 C  CA    . LYS A 1 692 ? 8.082   10.716  15.518  1.00 120.89 ? 692 LYS A CA    1 
ATOM   5675 C  C     . LYS A 1 692 ? 9.496   10.228  15.794  1.00 124.98 ? 692 LYS A C     1 
ATOM   5676 O  O     . LYS A 1 692 ? 10.111  10.566  16.806  1.00 132.16 ? 692 LYS A O     1 
ATOM   5677 C  CB    . LYS A 1 692 ? 7.903   12.158  15.975  1.00 131.47 ? 692 LYS A CB    1 
ATOM   5678 C  CG    . LYS A 1 692 ? 6.472   12.557  16.282  1.00 142.87 ? 692 LYS A CG    1 
ATOM   5679 C  CD    . LYS A 1 692 ? 6.294   14.064  16.164  1.00 143.03 ? 692 LYS A CD    1 
ATOM   5680 C  CE    . LYS A 1 692 ? 5.038   14.536  16.881  1.00 141.32 ? 692 LYS A CE    1 
ATOM   5681 N  NZ    . LYS A 1 692 ? 5.233   15.869  17.521  1.00 118.07 ? 692 LYS A NZ    1 
ATOM   5682 N  N     . ILE A 1 693 ? 10.026  9.421   14.878  1.00 117.44 ? 693 ILE A N     1 
ATOM   5683 C  CA    . ILE A 1 693 ? 11.431  9.046   14.960  1.00 116.01 ? 693 ILE A CA    1 
ATOM   5684 C  C     . ILE A 1 693 ? 12.177  9.775   13.848  1.00 103.26 ? 693 ILE A C     1 
ATOM   5685 O  O     . ILE A 1 693 ? 12.204  9.323   12.696  1.00 95.78  ? 693 ILE A O     1 
ATOM   5686 C  CB    . ILE A 1 693 ? 11.662  7.524   14.867  1.00 108.66 ? 693 ILE A CB    1 
ATOM   5687 C  CG1   . ILE A 1 693 ? 11.147  6.769   16.100  1.00 88.65  ? 693 ILE A CG1   1 
ATOM   5688 C  CG2   . ILE A 1 693 ? 13.140  7.256   14.833  1.00 100.43 ? 693 ILE A CG2   1 
ATOM   5689 C  CD1   . ILE A 1 693 ? 9.658   6.694   16.262  1.00 111.82 ? 693 ILE A CD1   1 
ATOM   5690 N  N     . ARG A 1 694 ? 12.775  10.908  14.182  1.00 103.57 ? 694 ARG A N     1 
ATOM   5691 C  CA    . ARG A 1 694 ? 13.571  11.697  13.261  1.00 100.58 ? 694 ARG A CA    1 
ATOM   5692 C  C     . ARG A 1 694 ? 15.040  11.626  13.650  1.00 93.91  ? 694 ARG A C     1 
ATOM   5693 O  O     . ARG A 1 694 ? 15.374  11.232  14.772  1.00 82.96  ? 694 ARG A O     1 
ATOM   5694 C  CB    . ARG A 1 694 ? 13.107  13.161  13.263  1.00 99.69  ? 694 ARG A CB    1 
ATOM   5695 C  CG    . ARG A 1 694 ? 11.612  13.347  13.477  1.00 118.08 ? 694 ARG A CG    1 
ATOM   5696 C  CD    . ARG A 1 694 ? 11.289  14.767  13.924  1.00 125.98 ? 694 ARG A CD    1 
ATOM   5697 N  NE    . ARG A 1 694 ? 9.928   15.155  13.573  1.00 125.00 ? 694 ARG A NE    1 
ATOM   5698 C  CZ    . ARG A 1 694 ? 9.584   16.349  13.110  1.00 126.19 ? 694 ARG A CZ    1 
ATOM   5699 N  NH1   . ARG A 1 694 ? 10.480  17.305  12.926  1.00 113.56 ? 694 ARG A NH1   1 
ATOM   5700 N  NH2   . ARG A 1 694 ? 8.308   16.590  12.822  1.00 120.75 ? 694 ARG A NH2   1 
ATOM   5701 N  N     . PRO A 1 695 ? 15.950  11.967  12.740  1.00 99.70  ? 695 PRO A N     1 
ATOM   5702 C  CA    . PRO A 1 695 ? 17.361  12.084  13.124  1.00 81.77  ? 695 PRO A CA    1 
ATOM   5703 C  C     . PRO A 1 695 ? 17.535  13.018  14.313  1.00 82.94  ? 695 PRO A C     1 
ATOM   5704 O  O     . PRO A 1 695 ? 17.099  14.171  14.290  1.00 92.83  ? 695 PRO A O     1 
ATOM   5705 C  CB    . PRO A 1 695 ? 18.022  12.643  11.862  1.00 70.02  ? 695 PRO A CB    1 
ATOM   5706 C  CG    . PRO A 1 695 ? 17.180  12.134  10.747  1.00 84.53  ? 695 PRO A CG    1 
ATOM   5707 C  CD    . PRO A 1 695 ? 15.769  12.008  11.278  1.00 93.60  ? 695 PRO A CD    1 
ATOM   5708 N  N     . GLY A 1 696 ? 18.159  12.504  15.372  1.00 77.65  ? 696 GLY A N     1 
ATOM   5709 C  CA    . GLY A 1 696 ? 18.439  13.271  16.566  1.00 77.28  ? 696 GLY A CA    1 
ATOM   5710 C  C     . GLY A 1 696 ? 17.698  12.815  17.808  1.00 86.06  ? 696 GLY A C     1 
ATOM   5711 O  O     . GLY A 1 696 ? 18.094  13.197  18.917  1.00 85.13  ? 696 GLY A O     1 
ATOM   5712 N  N     . THR A 1 697 ? 16.638  12.021  17.667  1.00 76.19  ? 697 THR A N     1 
ATOM   5713 C  CA    . THR A 1 697 ? 15.913  11.554  18.844  1.00 78.94  ? 697 THR A CA    1 
ATOM   5714 C  C     . THR A 1 697 ? 16.700  10.477  19.580  1.00 81.23  ? 697 THR A C     1 
ATOM   5715 O  O     . THR A 1 697 ? 17.339  9.616   18.968  1.00 78.14  ? 697 THR A O     1 
ATOM   5716 C  CB    . THR A 1 697 ? 14.531  11.023  18.466  1.00 94.07  ? 697 THR A CB    1 
ATOM   5717 O  OG1   . THR A 1 697 ? 14.624  9.640   18.100  1.00 91.46  ? 697 THR A OG1   1 
ATOM   5718 C  CG2   . THR A 1 697 ? 13.917  11.841  17.340  1.00 103.55 ? 697 THR A CG2   1 
ATOM   5719 N  N     . VAL A 1 698 ? 16.636  10.528  20.907  1.00 80.65  ? 698 VAL A N     1 
ATOM   5720 C  CA    . VAL A 1 698 ? 17.393  9.640   21.780  1.00 68.56  ? 698 VAL A CA    1 
ATOM   5721 C  C     . VAL A 1 698 ? 16.506  8.474   22.188  1.00 79.82  ? 698 VAL A C     1 
ATOM   5722 O  O     . VAL A 1 698 ? 15.388  8.675   22.679  1.00 77.34  ? 698 VAL A O     1 
ATOM   5723 C  CB    . VAL A 1 698 ? 17.912  10.392  23.017  1.00 63.89  ? 698 VAL A CB    1 
ATOM   5724 C  CG1   . VAL A 1 698 ? 18.521  9.418   24.017  1.00 78.45  ? 698 VAL A CG1   1 
ATOM   5725 C  CG2   . VAL A 1 698 ? 18.920  11.453  22.608  1.00 79.70  ? 698 VAL A CG2   1 
ATOM   5726 N  N     . ILE A 1 699 ? 17.002  7.257   21.988  1.00 79.81  ? 699 ILE A N     1 
ATOM   5727 C  CA    . ILE A 1 699 ? 16.327  6.053   22.457  1.00 68.59  ? 699 ILE A CA    1 
ATOM   5728 C  C     . ILE A 1 699 ? 16.837  5.728   23.854  1.00 74.62  ? 699 ILE A C     1 
ATOM   5729 O  O     . ILE A 1 699 ? 18.051  5.659   24.082  1.00 86.37  ? 699 ILE A O     1 
ATOM   5730 C  CB    . ILE A 1 699 ? 16.561  4.875   21.496  1.00 65.14  ? 699 ILE A CB    1 
ATOM   5731 C  CG1   . ILE A 1 699 ? 16.296  5.293   20.048  1.00 64.57  ? 699 ILE A CG1   1 
ATOM   5732 C  CG2   . ILE A 1 699 ? 15.688  3.691   21.883  1.00 65.81  ? 699 ILE A CG2   1 
ATOM   5733 C  CD1   . ILE A 1 699 ? 14.941  5.929   19.820  1.00 81.27  ? 699 ILE A CD1   1 
ATOM   5734 N  N     . SER A 1 700 ? 15.914  5.535   24.791  1.00 70.82  ? 700 SER A N     1 
ATOM   5735 C  CA    . SER A 1 700 ? 16.243  5.210   26.177  1.00 74.67  ? 700 SER A CA    1 
ATOM   5736 C  C     . SER A 1 700 ? 15.615  3.857   26.490  1.00 77.00  ? 700 SER A C     1 
ATOM   5737 O  O     . SER A 1 700 ? 14.421  3.777   26.796  1.00 82.52  ? 700 SER A O     1 
ATOM   5738 C  CB    . SER A 1 700 ? 15.744  6.294   27.129  1.00 66.43  ? 700 SER A CB    1 
ATOM   5739 O  OG    . SER A 1 700 ? 16.047  7.586   26.633  1.00 74.42  ? 700 SER A OG    1 
ATOM   5740 N  N     . TYR A 1 701 ? 16.412  2.795   26.415  1.00 78.14  ? 701 TYR A N     1 
ATOM   5741 C  CA    . TYR A 1 701 ? 15.901  1.441   26.558  1.00 75.28  ? 701 TYR A CA    1 
ATOM   5742 C  C     . TYR A 1 701 ? 16.528  0.745   27.758  1.00 74.21  ? 701 TYR A C     1 
ATOM   5743 O  O     . TYR A 1 701 ? 17.665  1.030   28.145  1.00 81.99  ? 701 TYR A O     1 
ATOM   5744 C  CB    . TYR A 1 701 ? 16.148  0.613   25.284  1.00 76.96  ? 701 TYR A CB    1 
ATOM   5745 C  CG    . TYR A 1 701 ? 17.604  0.327   24.963  1.00 79.39  ? 701 TYR A CG    1 
ATOM   5746 C  CD1   . TYR A 1 701 ? 18.247  -0.793  25.481  1.00 80.41  ? 701 TYR A CD1   1 
ATOM   5747 C  CD2   . TYR A 1 701 ? 18.327  1.163   24.123  1.00 76.80  ? 701 TYR A CD2   1 
ATOM   5748 C  CE1   . TYR A 1 701 ? 19.570  -1.061  25.183  1.00 73.70  ? 701 TYR A CE1   1 
ATOM   5749 C  CE2   . TYR A 1 701 ? 19.652  0.901   23.818  1.00 75.78  ? 701 TYR A CE2   1 
ATOM   5750 C  CZ    . TYR A 1 701 ? 20.267  -0.212  24.351  1.00 65.80  ? 701 TYR A CZ    1 
ATOM   5751 O  OH    . TYR A 1 701 ? 21.584  -0.475  24.051  1.00 74.65  ? 701 TYR A OH    1 
ATOM   5752 N  N     . ILE A 1 702 ? 15.759  -0.169  28.344  1.00 66.37  ? 702 ILE A N     1 
ATOM   5753 C  CA    . ILE A 1 702 ? 16.233  -1.082  29.374  1.00 68.52  ? 702 ILE A CA    1 
ATOM   5754 C  C     . ILE A 1 702 ? 16.143  -2.496  28.816  1.00 78.81  ? 702 ILE A C     1 
ATOM   5755 O  O     . ILE A 1 702 ? 15.269  -2.804  27.999  1.00 81.20  ? 702 ILE A O     1 
ATOM   5756 C  CB    . ILE A 1 702 ? 15.430  -0.947  30.690  1.00 66.18  ? 702 ILE A CB    1 
ATOM   5757 C  CG1   . ILE A 1 702 ? 16.124  -1.695  31.831  1.00 71.42  ? 702 ILE A CG1   1 
ATOM   5758 C  CG2   . ILE A 1 702 ? 14.002  -1.442  30.513  1.00 66.63  ? 702 ILE A CG2   1 
ATOM   5759 C  CD1   . ILE A 1 702 ? 15.723  -1.216  33.207  1.00 75.73  ? 702 ILE A CD1   1 
ATOM   5760 N  N     . VAL A 1 703 ? 17.067  -3.351  29.242  1.00 76.87  ? 703 VAL A N     1 
ATOM   5761 C  CA    . VAL A 1 703 ? 17.126  -4.735  28.784  1.00 76.41  ? 703 VAL A CA    1 
ATOM   5762 C  C     . VAL A 1 703 ? 16.418  -5.609  29.810  1.00 76.04  ? 703 VAL A C     1 
ATOM   5763 O  O     . VAL A 1 703 ? 16.759  -5.589  31.000  1.00 81.33  ? 703 VAL A O     1 
ATOM   5764 C  CB    . VAL A 1 703 ? 18.577  -5.192  28.565  1.00 82.24  ? 703 VAL A CB    1 
ATOM   5765 C  CG1   . VAL A 1 703 ? 18.617  -6.390  27.629  1.00 84.95  ? 703 VAL A CG1   1 
ATOM   5766 C  CG2   . VAL A 1 703 ? 19.403  -4.051  28.001  1.00 67.95  ? 703 VAL A CG2   1 
ATOM   5767 N  N     . LEU A 1 704 ? 15.436  -6.378  29.352  1.00 77.68  ? 704 LEU A N     1 
ATOM   5768 C  CA    . LEU A 1 704 ? 14.644  -7.218  30.235  1.00 81.81  ? 704 LEU A CA    1 
ATOM   5769 C  C     . LEU A 1 704 ? 15.237  -8.617  30.324  1.00 83.35  ? 704 LEU A C     1 
ATOM   5770 O  O     . LEU A 1 704 ? 15.905  -9.093  29.401  1.00 88.66  ? 704 LEU A O     1 
ATOM   5771 C  CB    . LEU A 1 704 ? 13.196  -7.297  29.751  1.00 84.65  ? 704 LEU A CB    1 
ATOM   5772 C  CG    . LEU A 1 704 ? 12.429  -5.976  29.800  1.00 92.30  ? 704 LEU A CG    1 
ATOM   5773 C  CD1   . LEU A 1 704 ? 11.035  -6.137  29.212  1.00 87.42  ? 704 LEU A CD1   1 
ATOM   5774 C  CD2   . LEU A 1 704 ? 12.362  -5.460  31.225  1.00 89.71  ? 704 LEU A CD2   1 
ATOM   5775 N  N     . LYS A 1 705 ? 14.984  -9.273  31.455  1.00 86.80  ? 705 LYS A N     1 
ATOM   5776 C  CA    . LYS A 1 705 ? 15.493  -10.618 31.680  1.00 80.87  ? 705 LYS A CA    1 
ATOM   5777 C  C     . LYS A 1 705 ? 14.947  -11.575 30.630  1.00 88.43  ? 705 LYS A C     1 
ATOM   5778 O  O     . LYS A 1 705 ? 13.730  -11.699 30.461  1.00 98.97  ? 705 LYS A O     1 
ATOM   5779 C  CB    . LYS A 1 705 ? 15.120  -11.095 33.082  1.00 77.75  ? 705 LYS A CB    1 
ATOM   5780 C  CG    . LYS A 1 705 ? 15.625  -12.492 33.409  1.00 72.09  ? 705 LYS A CG    1 
ATOM   5781 C  CD    . LYS A 1 705 ? 15.440  -12.820 34.880  1.00 73.59  ? 705 LYS A CD    1 
ATOM   5782 C  CE    . LYS A 1 705 ? 15.777  -14.273 35.163  1.00 75.59  ? 705 LYS A CE    1 
ATOM   5783 N  NZ    . LYS A 1 705 ? 15.793  -14.557 36.622  1.00 88.45  ? 705 LYS A NZ    1 
ATOM   5784 N  N     . GLY A 1 706 ? 15.850  -12.246 29.928  1.00 94.51  ? 706 GLY A N     1 
ATOM   5785 C  CA    . GLY A 1 706 ? 15.443  -13.181 28.901  1.00 102.94 ? 706 GLY A CA    1 
ATOM   5786 C  C     . GLY A 1 706 ? 16.646  -13.725 28.168  1.00 109.44 ? 706 GLY A C     1 
ATOM   5787 O  O     . GLY A 1 706 ? 17.778  -13.629 28.646  1.00 95.57  ? 706 GLY A O     1 
ATOM   5788 N  N     . SER A 1 707 ? 16.387  -14.299 26.995  1.00 122.63 ? 707 SER A N     1 
ATOM   5789 C  CA    . SER A 1 707 ? 17.435  -14.860 26.156  1.00 116.04 ? 707 SER A CA    1 
ATOM   5790 C  C     . SER A 1 707 ? 17.215  -14.413 24.718  1.00 111.22 ? 707 SER A C     1 
ATOM   5791 O  O     . SER A 1 707 ? 16.166  -13.866 24.366  1.00 117.81 ? 707 SER A O     1 
ATOM   5792 C  CB    . SER A 1 707 ? 17.479  -16.390 26.260  1.00 112.61 ? 707 SER A CB    1 
ATOM   5793 O  OG    . SER A 1 707 ? 17.927  -16.795 27.543  1.00 105.17 ? 707 SER A OG    1 
ATOM   5794 N  N     . GLY A 1 708 ? 18.220  -14.651 23.886  1.00 108.87 ? 708 GLY A N     1 
ATOM   5795 C  CA    . GLY A 1 708 ? 18.222  -14.168 22.523  1.00 100.95 ? 708 GLY A CA    1 
ATOM   5796 C  C     . GLY A 1 708 ? 19.011  -12.883 22.371  1.00 95.43  ? 708 GLY A C     1 
ATOM   5797 O  O     . GLY A 1 708 ? 19.832  -12.511 23.213  1.00 96.21  ? 708 GLY A O     1 
ATOM   5798 N  N     . ARG A 1 709 ? 18.748  -12.194 21.265  1.00 88.21  ? 709 ARG A N     1 
ATOM   5799 C  CA    . ARG A 1 709 ? 19.421  -10.932 20.999  1.00 89.29  ? 709 ARG A CA    1 
ATOM   5800 C  C     . ARG A 1 709 ? 18.995  -9.873  22.008  1.00 86.97  ? 709 ARG A C     1 
ATOM   5801 O  O     . ARG A 1 709 ? 17.901  -9.926  22.578  1.00 98.16  ? 709 ARG A O     1 
ATOM   5802 C  CB    . ARG A 1 709 ? 19.119  -10.452 19.581  1.00 83.41  ? 709 ARG A CB    1 
ATOM   5803 C  CG    . ARG A 1 709 ? 19.623  -11.384 18.498  1.00 87.00  ? 709 ARG A CG    1 
ATOM   5804 C  CD    . ARG A 1 709 ? 19.322  -10.832 17.119  1.00 85.33  ? 709 ARG A CD    1 
ATOM   5805 N  NE    . ARG A 1 709 ? 17.892  -10.723 16.862  1.00 86.76  ? 709 ARG A NE    1 
ATOM   5806 C  CZ    . ARG A 1 709 ? 17.371  -10.260 15.734  1.00 91.12  ? 709 ARG A CZ    1 
ATOM   5807 N  NH1   . ARG A 1 709 ? 18.138  -9.849  14.737  1.00 87.44  ? 709 ARG A NH1   1 
ATOM   5808 N  NH2   . ARG A 1 709 ? 16.049  -10.206 15.603  1.00 89.24  ? 709 ARG A NH2   1 
ATOM   5809 N  N     . ILE A 1 710 ? 19.884  -8.904  22.233  1.00 88.99  ? 710 ILE A N     1 
ATOM   5810 C  CA    . ILE A 1 710 ? 19.565  -7.806  23.139  1.00 87.02  ? 710 ILE A CA    1 
ATOM   5811 C  C     . ILE A 1 710 ? 18.419  -6.977  22.579  1.00 84.94  ? 710 ILE A C     1 
ATOM   5812 O  O     . ILE A 1 710 ? 17.528  -6.539  23.318  1.00 83.41  ? 710 ILE A O     1 
ATOM   5813 C  CB    . ILE A 1 710 ? 20.817  -6.947  23.398  1.00 84.01  ? 710 ILE A CB    1 
ATOM   5814 C  CG1   . ILE A 1 710 ? 21.902  -7.769  24.096  1.00 80.36  ? 710 ILE A CG1   1 
ATOM   5815 C  CG2   . ILE A 1 710 ? 20.466  -5.727  24.236  1.00 63.98  ? 710 ILE A CG2   1 
ATOM   5816 C  CD1   . ILE A 1 710 ? 21.388  -8.646  25.218  1.00 65.44  ? 710 ILE A CD1   1 
ATOM   5817 N  N     . GLY A 1 711 ? 18.413  -6.764  21.264  1.00 95.47  ? 711 GLY A N     1 
ATOM   5818 C  CA    . GLY A 1 711 ? 17.374  -5.990  20.612  1.00 104.68 ? 711 GLY A CA    1 
ATOM   5819 C  C     . GLY A 1 711 ? 16.003  -6.625  20.601  1.00 101.28 ? 711 GLY A C     1 
ATOM   5820 O  O     . GLY A 1 711 ? 15.064  -6.020  20.074  1.00 102.58 ? 711 GLY A O     1 
ATOM   5821 N  N     . ASP A 1 712 ? 15.856  -7.828  21.157  1.00 89.64  ? 712 ASP A N     1 
ATOM   5822 C  CA    . ASP A 1 712 ? 14.556  -8.477  21.253  1.00 90.62  ? 712 ASP A CA    1 
ATOM   5823 C  C     . ASP A 1 712 ? 13.950  -8.403  22.647  1.00 88.49  ? 712 ASP A C     1 
ATOM   5824 O  O     . ASP A 1 712 ? 12.746  -8.641  22.793  1.00 90.76  ? 712 ASP A O     1 
ATOM   5825 C  CB    . ASP A 1 712 ? 14.661  -9.947  20.827  1.00 84.58  ? 712 ASP A CB    1 
ATOM   5826 C  CG    . ASP A 1 712 ? 15.015  -10.104 19.362  1.00 86.59  ? 712 ASP A CG    1 
ATOM   5827 O  OD1   . ASP A 1 712 ? 14.853  -9.123  18.603  1.00 81.72  ? 712 ASP A OD1   1 
ATOM   5828 O  OD2   . ASP A 1 712 ? 15.452  -11.206 18.970  1.00 77.49  ? 712 ASP A OD2   1 
ATOM   5829 N  N     . ARG A 1 713 ? 14.747  -8.082  23.667  1.00 80.33  ? 713 ARG A N     1 
ATOM   5830 C  CA    . ARG A 1 713 ? 14.246  -7.919  25.026  1.00 76.19  ? 713 ARG A CA    1 
ATOM   5831 C  C     . ARG A 1 713 ? 14.459  -6.507  25.556  1.00 77.18  ? 713 ARG A C     1 
ATOM   5832 O  O     . ARG A 1 713 ? 14.305  -6.278  26.761  1.00 88.83  ? 713 ARG A O     1 
ATOM   5833 C  CB    . ARG A 1 713 ? 14.899  -8.937  25.966  1.00 83.46  ? 713 ARG A CB    1 
ATOM   5834 C  CG    . ARG A 1 713 ? 16.194  -9.531  25.442  1.00 88.15  ? 713 ARG A CG    1 
ATOM   5835 C  CD    . ARG A 1 713 ? 16.802  -10.485 26.454  1.00 92.51  ? 713 ARG A CD    1 
ATOM   5836 N  NE    . ARG A 1 713 ? 18.107  -10.972 26.025  1.00 105.99 ? 713 ARG A NE    1 
ATOM   5837 C  CZ    . ARG A 1 713 ? 19.149  -11.126 26.830  1.00 100.51 ? 713 ARG A CZ    1 
ATOM   5838 N  NH1   . ARG A 1 713 ? 19.074  -10.838 28.119  1.00 94.50  ? 713 ARG A NH1   1 
ATOM   5839 N  NH2   . ARG A 1 713 ? 20.293  -11.582 26.330  1.00 101.90 ? 713 ARG A NH2   1 
ATOM   5840 N  N     . ALA A 1 714 ? 14.810  -5.560  24.690  1.00 86.61  ? 714 ALA A N     1 
ATOM   5841 C  CA    . ALA A 1 714 ? 14.979  -4.169  25.083  1.00 82.15  ? 714 ALA A CA    1 
ATOM   5842 C  C     . ALA A 1 714 ? 13.683  -3.415  24.813  1.00 81.64  ? 714 ALA A C     1 
ATOM   5843 O  O     . ALA A 1 714 ? 13.177  -3.422  23.685  1.00 85.80  ? 714 ALA A O     1 
ATOM   5844 C  CB    . ALA A 1 714 ? 16.145  -3.529  24.330  1.00 76.03  ? 714 ALA A CB    1 
ATOM   5845 N  N     . ILE A 1 715 ? 13.147  -2.773  25.846  1.00 81.22  ? 715 ILE A N     1 
ATOM   5846 C  CA    . ILE A 1 715 ? 11.933  -1.970  25.722  1.00 87.77  ? 715 ILE A CA    1 
ATOM   5847 C  C     . ILE A 1 715 ? 12.272  -0.544  26.137  1.00 82.88  ? 715 ILE A C     1 
ATOM   5848 O  O     . ILE A 1 715 ? 13.222  -0.339  26.906  1.00 90.73  ? 715 ILE A O     1 
ATOM   5849 C  CB    . ILE A 1 715 ? 10.789  -2.542  26.576  1.00 74.97  ? 715 ILE A CB    1 
ATOM   5850 C  CG1   . ILE A 1 715 ? 11.253  -2.750  28.019  1.00 84.05  ? 715 ILE A CG1   1 
ATOM   5851 C  CG2   . ILE A 1 715 ? 10.283  -3.847  25.984  1.00 79.96  ? 715 ILE A CG2   1 
ATOM   5852 C  CD1   . ILE A 1 715 ? 10.272  -2.250  29.056  1.00 84.62  ? 715 ILE A CD1   1 
ATOM   5853 N  N     . PRO A 1 716 ? 11.545  0.464   25.655  1.00 86.64  ? 716 PRO A N     1 
ATOM   5854 C  CA    . PRO A 1 716 ? 11.781  1.828   26.141  1.00 76.84  ? 716 PRO A CA    1 
ATOM   5855 C  C     . PRO A 1 716 ? 11.496  1.917   27.632  1.00 82.86  ? 716 PRO A C     1 
ATOM   5856 O  O     . PRO A 1 716 ? 10.715  1.140   28.184  1.00 87.58  ? 716 PRO A O     1 
ATOM   5857 C  CB    . PRO A 1 716 ? 10.798  2.678   25.325  1.00 81.78  ? 716 PRO A CB    1 
ATOM   5858 C  CG    . PRO A 1 716 ? 10.381  1.811   24.174  1.00 79.94  ? 716 PRO A CG    1 
ATOM   5859 C  CD    . PRO A 1 716 ? 10.455  0.407   24.668  1.00 79.01  ? 716 PRO A CD    1 
ATOM   5860 N  N     . PHE A 1 717 ? 12.152  2.874   28.294  1.00 78.06  ? 717 PHE A N     1 
ATOM   5861 C  CA    . PHE A 1 717 ? 12.050  2.930   29.749  1.00 77.81  ? 717 PHE A CA    1 
ATOM   5862 C  C     . PHE A 1 717 ? 10.676  3.408   30.199  1.00 93.36  ? 717 PHE A C     1 
ATOM   5863 O  O     . PHE A 1 717 ? 10.155  2.935   31.217  1.00 80.16  ? 717 PHE A O     1 
ATOM   5864 C  CB    . PHE A 1 717 ? 13.138  3.821   30.338  1.00 68.78  ? 717 PHE A CB    1 
ATOM   5865 C  CG    . PHE A 1 717 ? 13.217  3.737   31.831  1.00 74.32  ? 717 PHE A CG    1 
ATOM   5866 C  CD1   . PHE A 1 717 ? 13.342  2.507   32.454  1.00 67.68  ? 717 PHE A CD1   1 
ATOM   5867 C  CD2   . PHE A 1 717 ? 13.132  4.875   32.614  1.00 75.62  ? 717 PHE A CD2   1 
ATOM   5868 C  CE1   . PHE A 1 717 ? 13.402  2.411   33.829  1.00 74.67  ? 717 PHE A CE1   1 
ATOM   5869 C  CE2   . PHE A 1 717 ? 13.192  4.787   33.993  1.00 78.23  ? 717 PHE A CE2   1 
ATOM   5870 C  CZ    . PHE A 1 717 ? 13.326  3.552   34.600  1.00 76.41  ? 717 PHE A CZ    1 
ATOM   5871 N  N     . ASP A 1 718 ? 10.068  4.340   29.458  1.00 97.15  ? 718 ASP A N     1 
ATOM   5872 C  CA    . ASP A 1 718 ? 8.713   4.771   29.789  1.00 93.90  ? 718 ASP A CA    1 
ATOM   5873 C  C     . ASP A 1 718 ? 7.706   3.630   29.722  1.00 96.12  ? 718 ASP A C     1 
ATOM   5874 O  O     . ASP A 1 718 ? 6.578   3.785   30.202  1.00 101.24 ? 718 ASP A O     1 
ATOM   5875 C  CB    . ASP A 1 718 ? 8.285   5.926   28.870  1.00 94.49  ? 718 ASP A CB    1 
ATOM   5876 C  CG    . ASP A 1 718 ? 8.156   5.519   27.402  1.00 107.99 ? 718 ASP A CG    1 
ATOM   5877 O  OD1   . ASP A 1 718 ? 8.002   6.431   26.562  1.00 111.78 ? 718 ASP A OD1   1 
ATOM   5878 O  OD2   . ASP A 1 718 ? 8.213   4.315   27.071  1.00 103.74 ? 718 ASP A OD2   1 
ATOM   5879 N  N     . GLU A 1 719 ? 8.094   2.497   29.142  1.00 100.02 ? 719 GLU A N     1 
ATOM   5880 C  CA    . GLU A 1 719 ? 7.258   1.315   29.018  1.00 84.11  ? 719 GLU A CA    1 
ATOM   5881 C  C     . GLU A 1 719 ? 7.548   0.279   30.094  1.00 84.41  ? 719 GLU A C     1 
ATOM   5882 O  O     . GLU A 1 719 ? 6.894   -0.769  30.123  1.00 90.35  ? 719 GLU A O     1 
ATOM   5883 C  CB    . GLU A 1 719 ? 7.463   0.695   27.637  1.00 82.74  ? 719 GLU A CB    1 
ATOM   5884 C  CG    . GLU A 1 719 ? 6.200   0.280   26.931  1.00 104.93 ? 719 GLU A CG    1 
ATOM   5885 C  CD    . GLU A 1 719 ? 6.342   0.380   25.429  1.00 106.65 ? 719 GLU A CD    1 
ATOM   5886 O  OE1   . GLU A 1 719 ? 6.441   -0.673  24.766  1.00 104.84 ? 719 GLU A OE1   1 
ATOM   5887 O  OE2   . GLU A 1 719 ? 6.365   1.516   24.908  1.00 98.94  ? 719 GLU A OE2   1 
ATOM   5888 N  N     . PHE A 1 720 ? 8.514   0.542   30.970  1.00 93.73  ? 720 PHE A N     1 
ATOM   5889 C  CA    . PHE A 1 720 ? 8.925   -0.411  31.992  1.00 93.49  ? 720 PHE A CA    1 
ATOM   5890 C  C     . PHE A 1 720 ? 8.028   -0.260  33.215  1.00 90.80  ? 720 PHE A C     1 
ATOM   5891 O  O     . PHE A 1 720 ? 7.916   0.835   33.779  1.00 103.25 ? 720 PHE A O     1 
ATOM   5892 C  CB    . PHE A 1 720 ? 10.393  -0.197  32.365  1.00 76.21  ? 720 PHE A CB    1 
ATOM   5893 C  CG    . PHE A 1 720 ? 10.912  -1.169  33.394  1.00 73.78  ? 720 PHE A CG    1 
ATOM   5894 C  CD1   . PHE A 1 720 ? 10.816  -0.888  34.748  1.00 83.84  ? 720 PHE A CD1   1 
ATOM   5895 C  CD2   . PHE A 1 720 ? 11.500  -2.360  33.005  1.00 87.92  ? 720 PHE A CD2   1 
ATOM   5896 C  CE1   . PHE A 1 720 ? 11.292  -1.781  35.692  1.00 86.99  ? 720 PHE A CE1   1 
ATOM   5897 C  CE2   . PHE A 1 720 ? 11.980  -3.255  33.946  1.00 88.03  ? 720 PHE A CE2   1 
ATOM   5898 C  CZ    . PHE A 1 720 ? 11.875  -2.964  35.290  1.00 82.09  ? 720 PHE A CZ    1 
ATOM   5899 N  N     . ASP A 1 721 ? 7.394   -1.353  33.618  1.00 91.92  ? 721 ASP A N     1 
ATOM   5900 C  CA    . ASP A 1 721 ? 6.591   -1.395  34.839  1.00 97.75  ? 721 ASP A CA    1 
ATOM   5901 C  C     . ASP A 1 721 ? 7.220   -2.418  35.775  1.00 104.93 ? 721 ASP A C     1 
ATOM   5902 O  O     . ASP A 1 721 ? 7.228   -3.622  35.455  1.00 107.85 ? 721 ASP A O     1 
ATOM   5903 C  CB    . ASP A 1 721 ? 5.138   -1.753  34.526  1.00 101.97 ? 721 ASP A CB    1 
ATOM   5904 C  CG    . ASP A 1 721 ? 4.304   -1.987  35.775  1.00 95.06  ? 721 ASP A CG    1 
ATOM   5905 O  OD1   . ASP A 1 721 ? 4.679   -1.490  36.857  1.00 95.83  ? 721 ASP A OD1   1 
ATOM   5906 O  OD2   . ASP A 1 721 ? 3.253   -2.652  35.668  1.00 114.84 ? 721 ASP A OD2   1 
ATOM   5907 N  N     . PRO A 1 722 ? 7.760   -1.999  36.924  1.00 103.36 ? 722 PRO A N     1 
ATOM   5908 C  CA    . PRO A 1 722 ? 8.509   -2.943  37.773  1.00 102.86 ? 722 PRO A CA    1 
ATOM   5909 C  C     . PRO A 1 722 ? 7.689   -4.122  38.265  1.00 106.85 ? 722 PRO A C     1 
ATOM   5910 O  O     . PRO A 1 722 ? 8.251   -5.205  38.475  1.00 115.32 ? 722 PRO A O     1 
ATOM   5911 C  CB    . PRO A 1 722 ? 8.984   -2.064  38.940  1.00 114.20 ? 722 PRO A CB    1 
ATOM   5912 C  CG    . PRO A 1 722 ? 8.114   -0.841  38.894  1.00 107.84 ? 722 PRO A CG    1 
ATOM   5913 C  CD    . PRO A 1 722 ? 7.796   -0.627  37.453  1.00 96.12  ? 722 PRO A CD    1 
ATOM   5914 N  N     . THR A 1 723 ? 6.380   -3.952  38.462  1.00 109.29 ? 723 THR A N     1 
ATOM   5915 C  CA    . THR A 1 723 ? 5.560   -5.073  38.908  1.00 108.88 ? 723 THR A CA    1 
ATOM   5916 C  C     . THR A 1 723 ? 5.460   -6.157  37.844  1.00 107.70 ? 723 THR A C     1 
ATOM   5917 O  O     . THR A 1 723 ? 5.343   -7.342  38.179  1.00 108.38 ? 723 THR A O     1 
ATOM   5918 C  CB    . THR A 1 723 ? 4.160   -4.594  39.294  1.00 100.05 ? 723 THR A CB    1 
ATOM   5919 O  OG1   . THR A 1 723 ? 3.727   -3.584  38.374  1.00 101.75 ? 723 THR A OG1   1 
ATOM   5920 C  CG2   . THR A 1 723 ? 4.157   -4.028  40.706  1.00 91.50  ? 723 THR A CG2   1 
ATOM   5921 N  N     . LYS A 1 724 ? 5.504   -5.780  36.565  1.00 107.74 ? 724 LYS A N     1 
ATOM   5922 C  CA    . LYS A 1 724 ? 5.304   -6.722  35.473  1.00 106.14 ? 724 LYS A CA    1 
ATOM   5923 C  C     . LYS A 1 724 ? 6.588   -7.101  34.749  1.00 106.76 ? 724 LYS A C     1 
ATOM   5924 O  O     . LYS A 1 724 ? 6.568   -8.045  33.951  1.00 106.75 ? 724 LYS A O     1 
ATOM   5925 C  CB    . LYS A 1 724 ? 4.305   -6.155  34.447  1.00 102.46 ? 724 LYS A CB    1 
ATOM   5926 C  CG    . LYS A 1 724 ? 2.955   -5.682  35.006  1.00 99.08  ? 724 LYS A CG    1 
ATOM   5927 C  CD    . LYS A 1 724 ? 2.501   -6.461  36.237  1.00 104.56 ? 724 LYS A CD    1 
ATOM   5928 C  CE    . LYS A 1 724 ? 0.996   -6.374  36.424  1.00 111.56 ? 724 LYS A CE    1 
ATOM   5929 N  NZ    . LYS A 1 724 ? 0.260   -6.724  35.179  1.00 109.77 ? 724 LYS A NZ    1 
ATOM   5930 N  N     . HIS A 1 725 ? 7.695   -6.403  34.994  1.00 110.68 ? 725 HIS A N     1 
ATOM   5931 C  CA    . HIS A 1 725 ? 8.947   -6.674  34.304  1.00 105.45 ? 725 HIS A CA    1 
ATOM   5932 C  C     . HIS A 1 725 ? 10.083  -6.850  35.300  1.00 86.47  ? 725 HIS A C     1 
ATOM   5933 O  O     . HIS A 1 725 ? 10.047  -6.332  36.419  1.00 89.60  ? 725 HIS A O     1 
ATOM   5934 C  CB    . HIS A 1 725 ? 9.316   -5.557  33.315  1.00 97.35  ? 725 HIS A CB    1 
ATOM   5935 C  CG    . HIS A 1 725 ? 8.232   -5.233  32.336  1.00 106.16 ? 725 HIS A CG    1 
ATOM   5936 N  ND1   . HIS A 1 725 ? 7.679   -3.975  32.227  1.00 106.04 ? 725 HIS A ND1   1 
ATOM   5937 C  CD2   . HIS A 1 725 ? 7.597   -6.004  31.421  1.00 106.84 ? 725 HIS A CD2   1 
ATOM   5938 C  CE1   . HIS A 1 725 ? 6.751   -3.984  31.287  1.00 108.95 ? 725 HIS A CE1   1 
ATOM   5939 N  NE2   . HIS A 1 725 ? 6.681   -5.203  30.783  1.00 111.60 ? 725 HIS A NE2   1 
ATOM   5940 N  N     . ARG A 1 726 ? 11.099  -7.589  34.866  1.00 93.99  ? 726 ARG A N     1 
ATOM   5941 C  CA    . ARG A 1 726 ? 12.327  -7.789  35.622  1.00 93.11  ? 726 ARG A CA    1 
ATOM   5942 C  C     . ARG A 1 726 ? 13.490  -7.534  34.677  1.00 88.97  ? 726 ARG A C     1 
ATOM   5943 O  O     . ARG A 1 726 ? 13.585  -8.179  33.628  1.00 90.07  ? 726 ARG A O     1 
ATOM   5944 C  CB    . ARG A 1 726 ? 12.390  -9.205  36.198  1.00 78.23  ? 726 ARG A CB    1 
ATOM   5945 C  CG    . ARG A 1 726 ? 12.935  -9.276  37.603  1.00 99.43  ? 726 ARG A CG    1 
ATOM   5946 C  CD    . ARG A 1 726 ? 12.141  -10.239 38.454  1.00 109.05 ? 726 ARG A CD    1 
ATOM   5947 N  NE    . ARG A 1 726 ? 12.352  -10.004 39.877  1.00 118.61 ? 726 ARG A NE    1 
ATOM   5948 C  CZ    . ARG A 1 726 ? 11.741  -9.063  40.581  1.00 123.27 ? 726 ARG A CZ    1 
ATOM   5949 N  NH1   . ARG A 1 726 ? 10.856  -8.250  40.027  1.00 106.55 ? 726 ARG A NH1   1 
ATOM   5950 N  NH2   . ARG A 1 726 ? 12.021  -8.937  41.875  1.00 125.59 ? 726 ARG A NH2   1 
ATOM   5951 N  N     . TYR A 1 727 ? 14.357  -6.588  35.028  1.00 80.53  ? 727 TYR A N     1 
ATOM   5952 C  CA    . TYR A 1 727 ? 15.457  -6.269  34.132  1.00 84.33  ? 727 TYR A CA    1 
ATOM   5953 C  C     . TYR A 1 727 ? 16.500  -7.383  34.148  1.00 88.82  ? 727 TYR A C     1 
ATOM   5954 O  O     . TYR A 1 727 ? 16.606  -8.163  35.099  1.00 80.74  ? 727 TYR A O     1 
ATOM   5955 C  CB    . TYR A 1 727 ? 16.091  -4.921  34.492  1.00 72.95  ? 727 TYR A CB    1 
ATOM   5956 C  CG    . TYR A 1 727 ? 16.572  -4.753  35.922  1.00 82.67  ? 727 TYR A CG    1 
ATOM   5957 C  CD1   . TYR A 1 727 ? 17.687  -5.439  36.393  1.00 88.70  ? 727 TYR A CD1   1 
ATOM   5958 C  CD2   . TYR A 1 727 ? 15.930  -3.878  36.788  1.00 79.96  ? 727 TYR A CD2   1 
ATOM   5959 C  CE1   . TYR A 1 727 ? 18.134  -5.272  37.691  1.00 83.02  ? 727 TYR A CE1   1 
ATOM   5960 C  CE2   . TYR A 1 727 ? 16.369  -3.706  38.088  1.00 89.26  ? 727 TYR A CE2   1 
ATOM   5961 C  CZ    . TYR A 1 727 ? 17.472  -4.404  38.533  1.00 87.21  ? 727 TYR A CZ    1 
ATOM   5962 O  OH    . TYR A 1 727 ? 17.912  -4.229  39.824  1.00 82.31  ? 727 TYR A OH    1 
ATOM   5963 N  N     . ASP A 1 728 ? 17.272  -7.456  33.066  1.00 80.93  ? 728 ASP A N     1 
ATOM   5964 C  CA    . ASP A 1 728 ? 18.262  -8.517  32.893  1.00 86.08  ? 728 ASP A CA    1 
ATOM   5965 C  C     . ASP A 1 728 ? 19.482  -8.185  33.741  1.00 86.74  ? 728 ASP A C     1 
ATOM   5966 O  O     . ASP A 1 728 ? 20.407  -7.499  33.302  1.00 76.15  ? 728 ASP A O     1 
ATOM   5967 C  CB    . ASP A 1 728 ? 18.629  -8.680  31.425  1.00 80.42  ? 728 ASP A CB    1 
ATOM   5968 C  CG    . ASP A 1 728 ? 19.287  -10.013 31.137  1.00 88.66  ? 728 ASP A CG    1 
ATOM   5969 O  OD1   . ASP A 1 728 ? 20.427  -10.229 31.600  1.00 89.36  ? 728 ASP A OD1   1 
ATOM   5970 O  OD2   . ASP A 1 728 ? 18.661  -10.847 30.451  1.00 88.23  ? 728 ASP A OD2   1 
ATOM   5971 N  N     . ALA A 1 729 ? 19.479  -8.680  34.981  1.00 88.15  ? 729 ALA A N     1 
ATOM   5972 C  CA    . ALA A 1 729 ? 20.618  -8.460  35.865  1.00 81.01  ? 729 ALA A CA    1 
ATOM   5973 C  C     . ALA A 1 729 ? 21.891  -9.054  35.281  1.00 82.59  ? 729 ALA A C     1 
ATOM   5974 O  O     . ALA A 1 729 ? 22.970  -8.463  35.396  1.00 89.23  ? 729 ALA A O     1 
ATOM   5975 C  CB    . ALA A 1 729 ? 20.334  -9.052  37.244  1.00 82.42  ? 729 ALA A CB    1 
ATOM   5976 N  N     . GLU A 1 730 ? 21.782  -10.220 34.637  1.00 89.71  ? 730 GLU A N     1 
ATOM   5977 C  CA    . GLU A 1 730 ? 22.956  -10.857 34.048  1.00 91.79  ? 730 GLU A CA    1 
ATOM   5978 C  C     . GLU A 1 730 ? 23.585  -9.982  32.971  1.00 87.80  ? 730 GLU A C     1 
ATOM   5979 O  O     . GLU A 1 730 ? 24.815  -9.907  32.864  1.00 80.21  ? 730 GLU A O     1 
ATOM   5980 C  CB    . GLU A 1 730 ? 22.579  -12.224 33.474  1.00 86.96  ? 730 GLU A CB    1 
ATOM   5981 C  CG    . GLU A 1 730 ? 23.613  -13.326 33.706  1.00 105.59 ? 730 GLU A CG    1 
ATOM   5982 C  CD    . GLU A 1 730 ? 24.151  -13.362 35.127  1.00 114.74 ? 730 GLU A CD    1 
ATOM   5983 O  OE1   . GLU A 1 730 ? 23.355  -13.217 36.082  1.00 102.18 ? 730 GLU A OE1   1 
ATOM   5984 O  OE2   . GLU A 1 730 ? 25.378  -13.538 35.289  1.00 103.31 ? 730 GLU A OE2   1 
ATOM   5985 N  N     . TYR A 1 731 ? 22.760  -9.316  32.159  1.00 84.32  ? 731 TYR A N     1 
ATOM   5986 C  CA    . TYR A 1 731 ? 23.295  -8.460  31.105  1.00 74.74  ? 731 TYR A CA    1 
ATOM   5987 C  C     . TYR A 1 731 ? 24.108  -7.312  31.690  1.00 80.04  ? 731 TYR A C     1 
ATOM   5988 O  O     . TYR A 1 731 ? 25.256  -7.084  31.295  1.00 82.30  ? 731 TYR A O     1 
ATOM   5989 C  CB    . TYR A 1 731 ? 22.163  -7.915  30.236  1.00 71.47  ? 731 TYR A CB    1 
ATOM   5990 C  CG    . TYR A 1 731 ? 22.633  -6.895  29.225  1.00 70.32  ? 731 TYR A CG    1 
ATOM   5991 C  CD1   . TYR A 1 731 ? 23.333  -7.287  28.091  1.00 73.59  ? 731 TYR A CD1   1 
ATOM   5992 C  CD2   . TYR A 1 731 ? 22.399  -5.540  29.414  1.00 74.09  ? 731 TYR A CD2   1 
ATOM   5993 C  CE1   . TYR A 1 731 ? 23.773  -6.359  27.166  1.00 79.16  ? 731 TYR A CE1   1 
ATOM   5994 C  CE2   . TYR A 1 731 ? 22.837  -4.603  28.495  1.00 73.82  ? 731 TYR A CE2   1 
ATOM   5995 C  CZ    . TYR A 1 731 ? 23.523  -5.019  27.373  1.00 72.02  ? 731 TYR A CZ    1 
ATOM   5996 O  OH    . TYR A 1 731 ? 23.960  -4.092  26.455  1.00 77.78  ? 731 TYR A OH    1 
ATOM   5997 N  N     . TYR A 1 732 ? 23.526  -6.578  32.638  1.00 83.78  ? 732 TYR A N     1 
ATOM   5998 C  CA    . TYR A 1 732 ? 24.198  -5.406  33.185  1.00 80.17  ? 732 TYR A CA    1 
ATOM   5999 C  C     . TYR A 1 732 ? 25.381  -5.772  34.072  1.00 78.51  ? 732 TYR A C     1 
ATOM   6000 O  O     . TYR A 1 732 ? 26.267  -4.935  34.276  1.00 81.36  ? 732 TYR A O     1 
ATOM   6001 C  CB    . TYR A 1 732 ? 23.196  -4.553  33.961  1.00 86.25  ? 732 TYR A CB    1 
ATOM   6002 C  CG    . TYR A 1 732 ? 22.145  -3.916  33.080  1.00 80.42  ? 732 TYR A CG    1 
ATOM   6003 C  CD1   . TYR A 1 732 ? 22.403  -2.729  32.408  1.00 69.64  ? 732 TYR A CD1   1 
ATOM   6004 C  CD2   . TYR A 1 732 ? 20.893  -4.498  32.924  1.00 77.04  ? 732 TYR A CD2   1 
ATOM   6005 C  CE1   . TYR A 1 732 ? 21.449  -2.143  31.603  1.00 74.79  ? 732 TYR A CE1   1 
ATOM   6006 C  CE2   . TYR A 1 732 ? 19.930  -3.917  32.120  1.00 76.02  ? 732 TYR A CE2   1 
ATOM   6007 C  CZ    . TYR A 1 732 ? 20.214  -2.739  31.462  1.00 79.54  ? 732 TYR A CZ    1 
ATOM   6008 O  OH    . TYR A 1 732 ? 19.264  -2.151  30.660  1.00 74.55  ? 732 TYR A OH    1 
ATOM   6009 N  N     . ILE A 1 733 ? 25.417  -6.995  34.602  1.00 83.34  ? 733 ILE A N     1 
ATOM   6010 C  CA    . ILE A 1 733 ? 26.587  -7.444  35.350  1.00 81.87  ? 733 ILE A CA    1 
ATOM   6011 C  C     . ILE A 1 733 ? 27.732  -7.763  34.398  1.00 75.42  ? 733 ILE A C     1 
ATOM   6012 O  O     . ILE A 1 733 ? 28.839  -7.229  34.527  1.00 82.24  ? 733 ILE A O     1 
ATOM   6013 C  CB    . ILE A 1 733 ? 26.235  -8.663  36.220  1.00 85.00  ? 733 ILE A CB    1 
ATOM   6014 C  CG1   . ILE A 1 733 ? 25.303  -8.265  37.366  1.00 87.51  ? 733 ILE A CG1   1 
ATOM   6015 C  CG2   . ILE A 1 733 ? 27.505  -9.313  36.749  1.00 83.59  ? 733 ILE A CG2   1 
ATOM   6016 C  CD1   . ILE A 1 733 ? 25.384  -9.175  38.562  1.00 75.50  ? 733 ILE A CD1   1 
ATOM   6017 N  N     . GLU A 1 734 ? 27.478  -8.629  33.417  1.00 72.72  ? 734 GLU A N     1 
ATOM   6018 C  CA    . GLU A 1 734 ? 28.536  -9.174  32.578  1.00 84.02  ? 734 GLU A CA    1 
ATOM   6019 C  C     . GLU A 1 734 ? 28.845  -8.327  31.350  1.00 85.67  ? 734 GLU A C     1 
ATOM   6020 O  O     . GLU A 1 734 ? 29.894  -8.532  30.730  1.00 84.92  ? 734 GLU A O     1 
ATOM   6021 C  CB    . GLU A 1 734 ? 28.166  -10.590 32.125  1.00 78.27  ? 734 GLU A CB    1 
ATOM   6022 C  CG    . GLU A 1 734 ? 27.935  -11.568 33.267  1.00 85.93  ? 734 GLU A CG    1 
ATOM   6023 C  CD    . GLU A 1 734 ? 29.222  -11.973 33.959  1.00 97.81  ? 734 GLU A CD    1 
ATOM   6024 O  OE1   . GLU A 1 734 ? 30.266  -12.041 33.277  1.00 101.53 ? 734 GLU A OE1   1 
ATOM   6025 O  OE2   . GLU A 1 734 ? 29.187  -12.229 35.182  1.00 95.06  ? 734 GLU A OE2   1 
ATOM   6026 N  N     . LYS A 1 735 ? 27.971  -7.391  30.979  1.00 83.92  ? 735 LYS A N     1 
ATOM   6027 C  CA    . LYS A 1 735 ? 28.163  -6.610  29.765  1.00 74.46  ? 735 LYS A CA    1 
ATOM   6028 C  C     . LYS A 1 735 ? 28.233  -5.108  30.002  1.00 69.55  ? 735 LYS A C     1 
ATOM   6029 O  O     . LYS A 1 735 ? 28.462  -4.360  29.045  1.00 68.94  ? 735 LYS A O     1 
ATOM   6030 C  CB    . LYS A 1 735 ? 27.044  -6.908  28.755  1.00 65.60  ? 735 LYS A CB    1 
ATOM   6031 C  CG    . LYS A 1 735 ? 26.876  -8.383  28.428  1.00 76.15  ? 735 LYS A CG    1 
ATOM   6032 C  CD    . LYS A 1 735 ? 27.581  -8.741  27.130  1.00 88.74  ? 735 LYS A CD    1 
ATOM   6033 C  CE    . LYS A 1 735 ? 28.448  -9.979  27.292  1.00 75.32  ? 735 LYS A CE    1 
ATOM   6034 N  NZ    . LYS A 1 735 ? 29.263  -10.247 26.074  1.00 83.10  ? 735 LYS A NZ    1 
ATOM   6035 N  N     . GLN A 1 736 ? 28.047  -4.641  31.236  1.00 70.59  ? 736 GLN A N     1 
ATOM   6036 C  CA    . GLN A 1 736 ? 28.074  -3.206  31.491  1.00 80.84  ? 736 GLN A CA    1 
ATOM   6037 C  C     . GLN A 1 736 ? 28.992  -2.858  32.656  1.00 76.55  ? 736 GLN A C     1 
ATOM   6038 O  O     . GLN A 1 736 ? 29.931  -2.072  32.498  1.00 76.31  ? 736 GLN A O     1 
ATOM   6039 C  CB    . GLN A 1 736 ? 26.661  -2.679  31.755  1.00 74.20  ? 736 GLN A CB    1 
ATOM   6040 C  CG    . GLN A 1 736 ? 25.833  -2.474  30.496  1.00 60.09  ? 736 GLN A CG    1 
ATOM   6041 C  CD    . GLN A 1 736 ? 25.823  -1.029  30.039  1.00 66.81  ? 736 GLN A CD    1 
ATOM   6042 O  OE1   . GLN A 1 736 ? 25.888  -0.110  30.854  1.00 65.63  ? 736 GLN A OE1   1 
ATOM   6043 N  NE2   . GLN A 1 736 ? 25.746  -0.821  28.729  1.00 61.11  ? 736 GLN A NE2   1 
ATOM   6044 N  N     . VAL A 1 737 ? 28.733  -3.435  33.828  1.00 78.48  ? 737 VAL A N     1 
ATOM   6045 C  CA    . VAL A 1 737 ? 29.500  -3.079  35.018  1.00 78.75  ? 737 VAL A CA    1 
ATOM   6046 C  C     . VAL A 1 737 ? 30.876  -3.735  34.991  1.00 78.73  ? 737 VAL A C     1 
ATOM   6047 O  O     . VAL A 1 737 ? 31.905  -3.051  34.975  1.00 84.79  ? 737 VAL A O     1 
ATOM   6048 C  CB    . VAL A 1 737 ? 28.723  -3.450  36.294  1.00 71.56  ? 737 VAL A CB    1 
ATOM   6049 C  CG1   . VAL A 1 737 ? 29.601  -3.264  37.519  1.00 69.27  ? 737 VAL A CG1   1 
ATOM   6050 C  CG2   . VAL A 1 737 ? 27.462  -2.607  36.409  1.00 71.90  ? 737 VAL A CG2   1 
ATOM   6051 N  N     . LEU A 1 738 ? 30.910  -5.070  34.983  1.00 86.15  ? 738 LEU A N     1 
ATOM   6052 C  CA    . LEU A 1 738 ? 32.185  -5.786  35.029  1.00 77.37  ? 738 LEU A CA    1 
ATOM   6053 C  C     . LEU A 1 738 ? 33.127  -5.417  33.890  1.00 81.02  ? 738 LEU A C     1 
ATOM   6054 O  O     . LEU A 1 738 ? 34.317  -5.182  34.163  1.00 86.17  ? 738 LEU A O     1 
ATOM   6055 C  CB    . LEU A 1 738 ? 31.932  -7.296  35.060  1.00 70.00  ? 738 LEU A CB    1 
ATOM   6056 C  CG    . LEU A 1 738 ? 31.552  -7.905  36.405  1.00 74.90  ? 738 LEU A CG    1 
ATOM   6057 C  CD1   . LEU A 1 738 ? 31.780  -9.396  36.349  1.00 81.31  ? 738 LEU A CD1   1 
ATOM   6058 C  CD2   . LEU A 1 738 ? 32.360  -7.280  37.527  1.00 80.89  ? 738 LEU A CD2   1 
ATOM   6059 N  N     . PRO A 1 739 ? 32.700  -5.359  32.622  1.00 81.01  ? 739 PRO A N     1 
ATOM   6060 C  CA    . PRO A 1 739 ? 33.641  -4.928  31.574  1.00 78.93  ? 739 PRO A CA    1 
ATOM   6061 C  C     . PRO A 1 739 ? 34.204  -3.539  31.809  1.00 78.68  ? 739 PRO A C     1 
ATOM   6062 O  O     . PRO A 1 739 ? 35.346  -3.272  31.421  1.00 86.75  ? 739 PRO A O     1 
ATOM   6063 C  CB    . PRO A 1 739 ? 32.793  -4.981  30.296  1.00 74.46  ? 739 PRO A CB    1 
ATOM   6064 C  CG    . PRO A 1 739 ? 31.726  -5.956  30.593  1.00 83.04  ? 739 PRO A CG    1 
ATOM   6065 C  CD    . PRO A 1 739 ? 31.407  -5.774  32.044  1.00 81.51  ? 739 PRO A CD    1 
ATOM   6066 N  N     . ALA A 1 740 ? 33.443  -2.648  32.447  1.00 79.40  ? 740 ALA A N     1 
ATOM   6067 C  CA    . ALA A 1 740 ? 33.908  -1.281  32.647  1.00 78.88  ? 740 ALA A CA    1 
ATOM   6068 C  C     . ALA A 1 740 ? 34.938  -1.173  33.764  1.00 80.17  ? 740 ALA A C     1 
ATOM   6069 O  O     . ALA A 1 740 ? 35.847  -0.340  33.679  1.00 78.99  ? 740 ALA A O     1 
ATOM   6070 C  CB    . ALA A 1 740 ? 32.724  -0.358  32.937  1.00 72.49  ? 740 ALA A CB    1 
ATOM   6071 N  N     . VAL A 1 741 ? 34.818  -1.988  34.814  1.00 78.82  ? 741 VAL A N     1 
ATOM   6072 C  CA    . VAL A 1 741 ? 35.780  -1.922  35.909  1.00 81.31  ? 741 VAL A CA    1 
ATOM   6073 C  C     . VAL A 1 741 ? 36.938  -2.895  35.730  1.00 85.21  ? 741 VAL A C     1 
ATOM   6074 O  O     . VAL A 1 741 ? 38.012  -2.676  36.309  1.00 86.52  ? 741 VAL A O     1 
ATOM   6075 C  CB    . VAL A 1 741 ? 35.107  -2.188  37.268  1.00 79.92  ? 741 VAL A CB    1 
ATOM   6076 C  CG1   . VAL A 1 741 ? 34.427  -0.927  37.781  1.00 73.79  ? 741 VAL A CG1   1 
ATOM   6077 C  CG2   . VAL A 1 741 ? 34.128  -3.341  37.166  1.00 76.23  ? 741 VAL A CG2   1 
ATOM   6078 N  N     . GLU A 1 742 ? 36.755  -3.965  34.951  1.00 93.97  ? 742 GLU A N     1 
ATOM   6079 C  CA    . GLU A 1 742 ? 37.846  -4.908  34.734  1.00 87.10  ? 742 GLU A CA    1 
ATOM   6080 C  C     . GLU A 1 742 ? 38.971  -4.272  33.929  1.00 95.12  ? 742 GLU A C     1 
ATOM   6081 O  O     . GLU A 1 742 ? 40.150  -4.527  34.196  1.00 102.38 ? 742 GLU A O     1 
ATOM   6082 C  CB    . GLU A 1 742 ? 37.332  -6.167  34.033  1.00 92.46  ? 742 GLU A CB    1 
ATOM   6083 C  CG    . GLU A 1 742 ? 38.412  -7.202  33.748  1.00 111.28 ? 742 GLU A CG    1 
ATOM   6084 C  CD    . GLU A 1 742 ? 38.754  -7.300  32.274  1.00 107.57 ? 742 GLU A CD    1 
ATOM   6085 O  OE1   . GLU A 1 742 ? 37.911  -6.907  31.440  1.00 105.85 ? 742 GLU A OE1   1 
ATOM   6086 O  OE2   . GLU A 1 742 ? 39.869  -7.761  31.950  1.00 96.21  ? 742 GLU A OE2   1 
ATOM   6087 N  N     . ARG A 1 743 ? 38.625  -3.435  32.947  1.00 88.65  ? 743 ARG A N     1 
ATOM   6088 C  CA    . ARG A 1 743 ? 39.641  -2.773  32.134  1.00 90.09  ? 743 ARG A CA    1 
ATOM   6089 C  C     . ARG A 1 743 ? 40.554  -1.882  32.961  1.00 78.90  ? 743 ARG A C     1 
ATOM   6090 O  O     . ARG A 1 743 ? 41.674  -1.588  32.535  1.00 82.57  ? 743 ARG A O     1 
ATOM   6091 C  CB    . ARG A 1 743 ? 38.973  -1.964  31.021  1.00 84.34  ? 743 ARG A CB    1 
ATOM   6092 C  CG    . ARG A 1 743 ? 38.103  -2.800  30.100  1.00 75.44  ? 743 ARG A CG    1 
ATOM   6093 C  CD    . ARG A 1 743 ? 37.844  -2.097  28.785  1.00 82.57  ? 743 ARG A CD    1 
ATOM   6094 N  NE    . ARG A 1 743 ? 36.507  -2.379  28.280  1.00 83.03  ? 743 ARG A NE    1 
ATOM   6095 C  CZ    . ARG A 1 743 ? 35.406  -1.772  28.702  1.00 83.35  ? 743 ARG A CZ    1 
ATOM   6096 N  NH1   . ARG A 1 743 ? 35.449  -0.831  29.631  1.00 90.64  ? 743 ARG A NH1   1 
ATOM   6097 N  NH2   . ARG A 1 743 ? 34.234  -2.117  28.179  1.00 83.96  ? 743 ARG A NH2   1 
ATOM   6098 N  N     . ILE A 1 744 ? 40.103  -1.455  34.132  1.00 80.91  ? 744 ILE A N     1 
ATOM   6099 C  CA    . ILE A 1 744 ? 40.936  -0.691  35.055  1.00 81.49  ? 744 ILE A CA    1 
ATOM   6100 C  C     . ILE A 1 744 ? 41.654  -1.613  36.035  1.00 85.80  ? 744 ILE A C     1 
ATOM   6101 O  O     . ILE A 1 744 ? 42.880  -1.573  36.154  1.00 99.36  ? 744 ILE A O     1 
ATOM   6102 C  CB    . ILE A 1 744 ? 40.080  0.357   35.790  1.00 83.98  ? 744 ILE A CB    1 
ATOM   6103 C  CG1   . ILE A 1 744 ? 39.520  1.375   34.806  1.00 73.80  ? 744 ILE A CG1   1 
ATOM   6104 C  CG2   . ILE A 1 744 ? 40.903  1.049   36.858  1.00 83.63  ? 744 ILE A CG2   1 
ATOM   6105 C  CD1   . ILE A 1 744 ? 38.559  2.338   35.434  1.00 82.48  ? 744 ILE A CD1   1 
ATOM   6106 N  N     . LEU A 1 745 ? 40.902  -2.467  36.734  1.00 87.41  ? 745 LEU A N     1 
ATOM   6107 C  CA    . LEU A 1 745 ? 41.469  -3.325  37.768  1.00 83.20  ? 745 LEU A CA    1 
ATOM   6108 C  C     . LEU A 1 745 ? 42.296  -4.476  37.209  1.00 87.73  ? 745 LEU A C     1 
ATOM   6109 O  O     . LEU A 1 745 ? 42.919  -5.197  37.994  1.00 87.82  ? 745 LEU A O     1 
ATOM   6110 C  CB    . LEU A 1 745 ? 40.356  -3.875  38.661  1.00 79.08  ? 745 LEU A CB    1 
ATOM   6111 C  CG    . LEU A 1 745 ? 39.507  -2.825  39.384  1.00 83.83  ? 745 LEU A CG    1 
ATOM   6112 C  CD1   . LEU A 1 745 ? 38.132  -3.378  39.734  1.00 82.66  ? 745 LEU A CD1   1 
ATOM   6113 C  CD2   . LEU A 1 745 ? 40.219  -2.324  40.632  1.00 85.55  ? 745 LEU A CD2   1 
ATOM   6114 N  N     . ARG A 1 746 ? 42.312  -4.673  35.887  1.00 88.17  ? 746 ARG A N     1 
ATOM   6115 C  CA    . ARG A 1 746 ? 43.160  -5.717  35.319  1.00 78.14  ? 746 ARG A CA    1 
ATOM   6116 C  C     . ARG A 1 746 ? 44.633  -5.427  35.569  1.00 91.45  ? 746 ARG A C     1 
ATOM   6117 O  O     . ARG A 1 746 ? 45.447  -6.356  35.637  1.00 94.94  ? 746 ARG A O     1 
ATOM   6118 C  CB    . ARG A 1 746 ? 42.903  -5.870  33.818  1.00 79.04  ? 746 ARG A CB    1 
ATOM   6119 C  CG    . ARG A 1 746 ? 43.855  -5.071  32.938  1.00 93.57  ? 746 ARG A CG    1 
ATOM   6120 C  CD    . ARG A 1 746 ? 43.439  -5.087  31.480  1.00 95.56  ? 746 ARG A CD    1 
ATOM   6121 N  NE    . ARG A 1 746 ? 41.992  -5.103  31.314  1.00 99.31  ? 746 ARG A NE    1 
ATOM   6122 C  CZ    . ARG A 1 746 ? 41.377  -5.370  30.171  1.00 103.60 ? 746 ARG A CZ    1 
ATOM   6123 N  NH1   . ARG A 1 746 ? 42.057  -5.629  29.066  1.00 102.61 ? 746 ARG A NH1   1 
ATOM   6124 N  NH2   . ARG A 1 746 ? 40.049  -5.381  30.135  1.00 105.78 ? 746 ARG A NH2   1 
ATOM   6125 N  N     . ALA A 1 747 ? 44.994  -4.150  35.715  1.00 92.96  ? 747 ALA A N     1 
ATOM   6126 C  CA    . ALA A 1 747 ? 46.369  -3.781  36.022  1.00 95.19  ? 747 ALA A CA    1 
ATOM   6127 C  C     . ALA A 1 747 ? 46.792  -4.220  37.415  1.00 95.01  ? 747 ALA A C     1 
ATOM   6128 O  O     . ALA A 1 747 ? 47.990  -4.193  37.717  1.00 100.36 ? 747 ALA A O     1 
ATOM   6129 C  CB    . ALA A 1 747 ? 46.550  -2.268  35.877  1.00 81.82  ? 747 ALA A CB    1 
ATOM   6130 N  N     . PHE A 1 748 ? 45.844  -4.624  38.260  1.00 92.59  ? 748 PHE A N     1 
ATOM   6131 C  CA    . PHE A 1 748 ? 46.122  -5.039  39.628  1.00 92.96  ? 748 PHE A CA    1 
ATOM   6132 C  C     . PHE A 1 748 ? 45.929  -6.539  39.816  1.00 93.35  ? 748 PHE A C     1 
ATOM   6133 O  O     . PHE A 1 748 ? 45.813  -7.012  40.951  1.00 91.51  ? 748 PHE A O     1 
ATOM   6134 C  CB    . PHE A 1 748 ? 45.251  -4.254  40.614  1.00 98.35  ? 748 PHE A CB    1 
ATOM   6135 C  CG    . PHE A 1 748 ? 45.540  -2.772  40.646  1.00 101.09 ? 748 PHE A CG    1 
ATOM   6136 C  CD1   . PHE A 1 748 ? 45.432  -1.995  39.500  1.00 107.63 ? 748 PHE A CD1   1 
ATOM   6137 C  CD2   . PHE A 1 748 ? 45.937  -2.159  41.823  1.00 96.49  ? 748 PHE A CD2   1 
ATOM   6138 C  CE1   . PHE A 1 748 ? 45.706  -0.643  39.528  1.00 100.66 ? 748 PHE A CE1   1 
ATOM   6139 C  CE2   . PHE A 1 748 ? 46.213  -0.805  41.856  1.00 103.17 ? 748 PHE A CE2   1 
ATOM   6140 C  CZ    . PHE A 1 748 ? 46.101  -0.049  40.705  1.00 99.94  ? 748 PHE A CZ    1 
ATOM   6141 N  N     . GLY A 1 749 ? 45.894  -7.298  38.719  1.00 97.66  ? 749 GLY A N     1 
ATOM   6142 C  CA    . GLY A 1 749 ? 45.754  -8.733  38.766  1.00 109.82 ? 749 GLY A CA    1 
ATOM   6143 C  C     . GLY A 1 749 ? 44.329  -9.238  38.835  1.00 102.44 ? 749 GLY A C     1 
ATOM   6144 O  O     . GLY A 1 749 ? 44.083  -10.400 38.492  1.00 108.91 ? 749 GLY A O     1 
ATOM   6145 N  N     . TYR A 1 750 ? 43.386  -8.403  39.262  1.00 102.69 ? 750 TYR A N     1 
ATOM   6146 C  CA    . TYR A 1 750 ? 42.008  -8.843  39.417  1.00 103.25 ? 750 TYR A CA    1 
ATOM   6147 C  C     . TYR A 1 750 ? 41.377  -9.143  38.064  1.00 99.00  ? 750 TYR A C     1 
ATOM   6148 O  O     . TYR A 1 750 ? 41.575  -8.414  37.088  1.00 96.67  ? 750 TYR A O     1 
ATOM   6149 C  CB    . TYR A 1 750 ? 41.188  -7.779  40.144  1.00 96.54  ? 750 TYR A CB    1 
ATOM   6150 C  CG    . TYR A 1 750 ? 41.552  -7.606  41.600  1.00 104.37 ? 750 TYR A CG    1 
ATOM   6151 C  CD1   . TYR A 1 750 ? 41.944  -8.690  42.374  1.00 110.69 ? 750 TYR A CD1   1 
ATOM   6152 C  CD2   . TYR A 1 750 ? 41.505  -6.356  42.201  1.00 106.68 ? 750 TYR A CD2   1 
ATOM   6153 C  CE1   . TYR A 1 750 ? 42.279  -8.532  43.708  1.00 112.88 ? 750 TYR A CE1   1 
ATOM   6154 C  CE2   . TYR A 1 750 ? 41.838  -6.188  43.530  1.00 106.27 ? 750 TYR A CE2   1 
ATOM   6155 C  CZ    . TYR A 1 750 ? 42.223  -7.278  44.280  1.00 112.94 ? 750 TYR A CZ    1 
ATOM   6156 O  OH    . TYR A 1 750 ? 42.555  -7.112  45.605  1.00 114.50 ? 750 TYR A OH    1 
ATOM   6157 N  N     . ARG A 1 751 ? 40.609  -10.224 38.013  1.00 106.32 ? 751 ARG A N     1 
ATOM   6158 C  CA    . ARG A 1 751 ? 39.839  -10.602 36.841  1.00 115.65 ? 751 ARG A CA    1 
ATOM   6159 C  C     . ARG A 1 751 ? 38.365  -10.678 37.228  1.00 113.56 ? 751 ARG A C     1 
ATOM   6160 O  O     . ARG A 1 751 ? 38.014  -10.674 38.410  1.00 108.84 ? 751 ARG A O     1 
ATOM   6161 C  CB    . ARG A 1 751 ? 40.343  -11.931 36.263  1.00 117.34 ? 751 ARG A CB    1 
ATOM   6162 C  CG    . ARG A 1 751 ? 40.103  -12.105 34.768  1.00 130.28 ? 751 ARG A CG    1 
ATOM   6163 C  CD    . ARG A 1 751 ? 41.316  -12.694 34.069  1.00 127.02 ? 751 ARG A CD    1 
ATOM   6164 N  NE    . ARG A 1 751 ? 41.484  -14.112 34.361  1.00 136.00 ? 751 ARG A NE    1 
ATOM   6165 C  CZ    . ARG A 1 751 ? 41.680  -15.048 33.443  1.00 127.98 ? 751 ARG A CZ    1 
ATOM   6166 N  NH1   . ARG A 1 751 ? 41.727  -14.755 32.153  1.00 111.81 ? 751 ARG A NH1   1 
ATOM   6167 N  NH2   . ARG A 1 751 ? 41.836  -16.312 33.828  1.00 130.16 ? 751 ARG A NH2   1 
ATOM   6168 N  N     . LYS A 1 752 ? 37.499  -10.743 36.210  1.00 106.67 ? 752 LYS A N     1 
ATOM   6169 C  CA    . LYS A 1 752 ? 36.057  -10.627 36.430  1.00 107.24 ? 752 LYS A CA    1 
ATOM   6170 C  C     . LYS A 1 752 ? 35.560  -11.640 37.454  1.00 109.89 ? 752 LYS A C     1 
ATOM   6171 O  O     . LYS A 1 752 ? 34.775  -11.306 38.349  1.00 111.75 ? 752 LYS A O     1 
ATOM   6172 C  CB    . LYS A 1 752 ? 35.313  -10.795 35.104  1.00 96.37  ? 752 LYS A CB    1 
ATOM   6173 C  CG    . LYS A 1 752 ? 35.448  -9.610  34.162  1.00 92.15  ? 752 LYS A CG    1 
ATOM   6174 C  CD    . LYS A 1 752 ? 34.292  -9.566  33.178  1.00 92.12  ? 752 LYS A CD    1 
ATOM   6175 C  CE    . LYS A 1 752 ? 34.728  -10.039 31.802  1.00 82.19  ? 752 LYS A CE    1 
ATOM   6176 N  NZ    . LYS A 1 752 ? 34.693  -8.939  30.802  1.00 88.59  ? 752 LYS A NZ    1 
ATOM   6177 N  N     . GLU A 1 753 ? 36.022  -12.883 37.338  1.00 104.44 ? 753 GLU A N     1 
ATOM   6178 C  CA    . GLU A 1 753 ? 35.654  -13.928 38.288  1.00 104.84 ? 753 GLU A CA    1 
ATOM   6179 C  C     . GLU A 1 753 ? 35.950  -13.510 39.724  1.00 104.36 ? 753 GLU A C     1 
ATOM   6180 O  O     . GLU A 1 753 ? 35.212  -13.870 40.648  1.00 107.49 ? 753 GLU A O     1 
ATOM   6181 C  CB    . GLU A 1 753 ? 36.397  -15.222 37.946  1.00 108.87 ? 753 GLU A CB    1 
ATOM   6182 C  CG    . GLU A 1 753 ? 36.514  -15.557 36.449  1.00 111.77 ? 753 GLU A CG    1 
ATOM   6183 C  CD    . GLU A 1 753 ? 37.492  -14.679 35.674  1.00 122.31 ? 753 GLU A CD    1 
ATOM   6184 O  OE1   . GLU A 1 753 ? 37.736  -13.528 36.090  1.00 125.95 ? 753 GLU A OE1   1 
ATOM   6185 O  OE2   . GLU A 1 753 ? 38.018  -15.153 34.646  1.00 126.97 ? 753 GLU A OE2   1 
ATOM   6186 N  N     . ASP A 1 754 ? 37.023  -12.744 39.928  1.00 113.08 ? 754 ASP A N     1 
ATOM   6187 C  CA    . ASP A 1 754 ? 37.396  -12.226 41.239  1.00 118.94 ? 754 ASP A CA    1 
ATOM   6188 C  C     . ASP A 1 754 ? 36.578  -11.002 41.648  1.00 118.69 ? 754 ASP A C     1 
ATOM   6189 O  O     . ASP A 1 754 ? 36.880  -10.391 42.678  1.00 125.00 ? 754 ASP A O     1 
ATOM   6190 C  CB    . ASP A 1 754 ? 38.886  -11.867 41.264  1.00 115.12 ? 754 ASP A CB    1 
ATOM   6191 C  CG    . ASP A 1 754 ? 39.762  -12.970 40.699  1.00 124.69 ? 754 ASP A CG    1 
ATOM   6192 O  OD1   . ASP A 1 754 ? 39.339  -13.626 39.726  1.00 142.88 ? 754 ASP A OD1   1 
ATOM   6193 O  OD2   . ASP A 1 754 ? 40.878  -13.178 41.222  1.00 128.00 ? 754 ASP A OD2   1 
ATOM   6194 N  N     . LEU A 1 755 ? 35.560  -10.636 40.867  1.00 117.20 ? 755 LEU A N     1 
ATOM   6195 C  CA    . LEU A 1 755 ? 34.762  -9.445  41.130  1.00 112.65 ? 755 LEU A CA    1 
ATOM   6196 C  C     . LEU A 1 755 ? 33.263  -9.711  41.200  1.00 111.05 ? 755 LEU A C     1 
ATOM   6197 O  O     . LEU A 1 755 ? 32.508  -8.789  41.533  1.00 100.53 ? 755 LEU A O     1 
ATOM   6198 C  CB    . LEU A 1 755 ? 35.024  -8.384  40.050  1.00 104.09 ? 755 LEU A CB    1 
ATOM   6199 C  CG    . LEU A 1 755 ? 36.464  -7.870  39.936  1.00 102.27 ? 755 LEU A CG    1 
ATOM   6200 C  CD1   . LEU A 1 755 ? 36.852  -7.645  38.484  1.00 99.42  ? 755 LEU A CD1   1 
ATOM   6201 C  CD2   . LEU A 1 755 ? 36.624  -6.586  40.717  1.00 92.37  ? 755 LEU A CD2   1 
ATOM   6202 N  N     . ARG A 1 756 ? 32.810  -10.930 40.907  1.00 116.24 ? 756 ARG A N     1 
ATOM   6203 C  CA    . ARG A 1 756 ? 31.386  -11.246 40.831  1.00 105.98 ? 756 ARG A CA    1 
ATOM   6204 C  C     . ARG A 1 756 ? 30.790  -11.535 42.207  1.00 105.06 ? 756 ARG A C     1 
ATOM   6205 O  O     . ARG A 1 756 ? 31.089  -10.842 43.179  1.00 112.48 ? 756 ARG A O     1 
ATOM   6206 C  CB    . ARG A 1 756 ? 31.174  -12.453 39.910  1.00 97.72  ? 756 ARG A CB    1 
ATOM   6207 C  CG    . ARG A 1 756 ? 31.143  -12.092 38.438  1.00 104.31 ? 756 ARG A CG    1 
ATOM   6208 C  CD    . ARG A 1 756 ? 32.140  -12.919 37.634  1.00 103.25 ? 756 ARG A CD    1 
ATOM   6209 N  NE    . ARG A 1 756 ? 31.762  -13.026 36.229  1.00 105.56 ? 756 ARG A NE    1 
ATOM   6210 C  CZ    . ARG A 1 756 ? 32.360  -13.814 35.346  1.00 103.60 ? 756 ARG A CZ    1 
ATOM   6211 N  NH1   . ARG A 1 756 ? 33.393  -14.570 35.680  1.00 117.12 ? 756 ARG A NH1   1 
ATOM   6212 N  NH2   . ARG A 1 756 ? 31.916  -13.837 34.092  1.00 95.66  ? 756 ARG A NH2   1 
ATOM   6213 O  "O5'" . DG  B 2 1   ? 25.859  -25.939 18.946  1.00 123.36 ? 1   DG  P "O5'" 1 
ATOM   6214 C  "C5'" . DG  B 2 1   ? 26.433  -25.125 17.928  1.00 127.01 ? 1   DG  P "C5'" 1 
ATOM   6215 C  "C4'" . DG  B 2 1   ? 27.883  -24.801 18.247  1.00 129.37 ? 1   DG  P "C4'" 1 
ATOM   6216 O  "O4'" . DG  B 2 1   ? 28.585  -24.491 17.019  1.00 115.94 ? 1   DG  P "O4'" 1 
ATOM   6217 C  "C3'" . DG  B 2 1   ? 28.095  -23.582 19.127  1.00 125.52 ? 1   DG  P "C3'" 1 
ATOM   6218 O  "O3'" . DG  B 2 1   ? 29.372  -23.659 19.753  1.00 128.80 ? 1   DG  P "O3'" 1 
ATOM   6219 C  "C2'" . DG  B 2 1   ? 28.047  -22.456 18.101  1.00 112.34 ? 1   DG  P "C2'" 1 
ATOM   6220 C  "C1'" . DG  B 2 1   ? 28.780  -23.089 16.920  1.00 112.72 ? 1   DG  P "C1'" 1 
ATOM   6221 N  N9    . DG  B 2 1   ? 28.280  -22.653 15.622  1.00 119.58 ? 1   DG  P N9    1 
ATOM   6222 C  C8    . DG  B 2 1   ? 26.975  -22.385 15.284  1.00 111.34 ? 1   DG  P C8    1 
ATOM   6223 N  N7    . DG  B 2 1   ? 26.826  -22.020 14.041  1.00 103.99 ? 1   DG  P N7    1 
ATOM   6224 C  C5    . DG  B 2 1   ? 28.114  -22.050 13.521  1.00 116.97 ? 1   DG  P C5    1 
ATOM   6225 C  C6    . DG  B 2 1   ? 28.578  -21.752 12.218  1.00 109.64 ? 1   DG  P C6    1 
ATOM   6226 O  O6    . DG  B 2 1   ? 27.919  -21.392 11.233  1.00 97.24  ? 1   DG  P O6    1 
ATOM   6227 N  N1    . DG  B 2 1   ? 29.958  -21.911 12.114  1.00 97.67  ? 1   DG  P N1    1 
ATOM   6228 C  C2    . DG  B 2 1   ? 30.784  -22.308 13.139  1.00 99.42  ? 1   DG  P C2    1 
ATOM   6229 N  N2    . DG  B 2 1   ? 32.089  -22.405 12.848  1.00 103.15 ? 1   DG  P N2    1 
ATOM   6230 N  N3    . DG  B 2 1   ? 30.361  -22.591 14.364  1.00 104.37 ? 1   DG  P N3    1 
ATOM   6231 C  C4    . DG  B 2 1   ? 29.019  -22.440 14.482  1.00 116.54 ? 1   DG  P C4    1 
ATOM   6232 P  P     . DA  B 2 2   ? 29.762  -22.661 20.953  1.00 129.24 ? 2   DA  P P     1 
ATOM   6233 O  OP1   . DA  B 2 2   ? 29.968  -23.495 22.157  1.00 111.13 ? 2   DA  P OP1   1 
ATOM   6234 O  OP2   . DA  B 2 2   ? 28.788  -21.546 20.983  1.00 102.12 ? 2   DA  P OP2   1 
ATOM   6235 O  "O5'" . DA  B 2 2   ? 31.192  -22.088 20.522  1.00 117.30 ? 2   DA  P "O5'" 1 
ATOM   6236 C  "C5'" . DA  B 2 2   ? 32.314  -22.961 20.459  1.00 117.99 ? 2   DA  P "C5'" 1 
ATOM   6237 C  "C4'" . DA  B 2 2   ? 33.429  -22.356 19.624  1.00 114.10 ? 2   DA  P "C4'" 1 
ATOM   6238 O  "O4'" . DA  B 2 2   ? 32.921  -22.024 18.306  1.00 115.55 ? 2   DA  P "O4'" 1 
ATOM   6239 C  "C3'" . DA  B 2 2   ? 34.036  -21.073 20.180  1.00 104.99 ? 2   DA  P "C3'" 1 
ATOM   6240 O  "O3'" . DA  B 2 2   ? 35.433  -21.046 19.915  1.00 113.63 ? 2   DA  P "O3'" 1 
ATOM   6241 C  "C2'" . DA  B 2 2   ? 33.293  -19.979 19.418  1.00 107.84 ? 2   DA  P "C2'" 1 
ATOM   6242 C  "C1'" . DA  B 2 2   ? 33.052  -20.637 18.066  1.00 106.23 ? 2   DA  P "C1'" 1 
ATOM   6243 N  N9    . DA  B 2 2   ? 31.835  -20.173 17.407  1.00 112.06 ? 2   DA  P N9    1 
ATOM   6244 C  C8    . DA  B 2 2   ? 30.597  -20.033 17.968  1.00 111.30 ? 2   DA  P C8    1 
ATOM   6245 N  N7    . DA  B 2 2   ? 29.683  -19.596 17.134  1.00 108.97 ? 2   DA  P N7    1 
ATOM   6246 C  C5    . DA  B 2 2   ? 30.370  -19.441 15.942  1.00 105.05 ? 2   DA  P C5    1 
ATOM   6247 C  C6    . DA  B 2 2   ? 29.968  -19.007 14.664  1.00 103.01 ? 2   DA  P C6    1 
ATOM   6248 N  N6    . DA  B 2 2   ? 28.716  -18.635 14.372  1.00 92.90  ? 2   DA  P N6    1 
ATOM   6249 N  N1    . DA  B 2 2   ? 30.904  -18.969 13.694  1.00 107.45 ? 2   DA  P N1    1 
ATOM   6250 C  C2    . DA  B 2 2   ? 32.156  -19.341 13.990  1.00 102.35 ? 2   DA  P C2    1 
ATOM   6251 N  N3    . DA  B 2 2   ? 32.652  -19.766 15.150  1.00 100.56 ? 2   DA  P N3    1 
ATOM   6252 C  C4    . DA  B 2 2   ? 31.698  -19.793 16.093  1.00 105.10 ? 2   DA  P C4    1 
ATOM   6253 P  P     . DC  B 2 3   ? 36.345  -19.840 20.458  1.00 115.50 ? 3   DC  P P     1 
ATOM   6254 O  OP1   . DC  B 2 3   ? 37.648  -20.414 20.863  1.00 85.85  ? 3   DC  P OP1   1 
ATOM   6255 O  OP2   . DC  B 2 3   ? 35.554  -19.055 21.431  1.00 116.87 ? 3   DC  P OP2   1 
ATOM   6256 O  "O5'" . DC  B 2 3   ? 36.564  -18.925 19.169  1.00 97.37  ? 3   DC  P "O5'" 1 
ATOM   6257 C  "C5'" . DC  B 2 3   ? 36.942  -19.522 17.938  1.00 102.12 ? 3   DC  P "C5'" 1 
ATOM   6258 C  "C4'" . DC  B 2 3   ? 36.909  -18.503 16.818  1.00 98.89  ? 3   DC  P "C4'" 1 
ATOM   6259 O  "O4'" . DC  B 2 3   ? 35.545  -18.315 16.373  1.00 110.18 ? 3   DC  P "O4'" 1 
ATOM   6260 C  "C3'" . DC  B 2 3   ? 37.437  -17.119 17.201  1.00 96.50  ? 3   DC  P "C3'" 1 
ATOM   6261 O  "O3'" . DC  B 2 3   ? 38.479  -16.738 16.317  1.00 88.86  ? 3   DC  P "O3'" 1 
ATOM   6262 C  "C2'" . DC  B 2 3   ? 36.216  -16.198 17.081  1.00 101.73 ? 3   DC  P "C2'" 1 
ATOM   6263 C  "C1'" . DC  B 2 3   ? 35.327  -16.955 16.108  1.00 98.14  ? 3   DC  P "C1'" 1 
ATOM   6264 N  N1    . DC  B 2 3   ? 33.878  -16.673 16.292  1.00 103.96 ? 3   DC  P N1    1 
ATOM   6265 C  C2    . DC  B 2 3   ? 33.150  -16.084 15.254  1.00 100.40 ? 3   DC  P C2    1 
ATOM   6266 O  O2    . DC  B 2 3   ? 33.726  -15.808 14.194  1.00 98.21  ? 3   DC  P O2    1 
ATOM   6267 N  N3    . DC  B 2 3   ? 31.829  -15.834 15.438  1.00 89.91  ? 3   DC  P N3    1 
ATOM   6268 C  C4    . DC  B 2 3   ? 31.245  -16.148 16.596  1.00 97.08  ? 3   DC  P C4    1 
ATOM   6269 N  N4    . DC  B 2 3   ? 29.941  -15.882 16.731  1.00 99.11  ? 3   DC  P N4    1 
ATOM   6270 C  C5    . DC  B 2 3   ? 31.971  -16.748 17.667  1.00 98.22  ? 3   DC  P C5    1 
ATOM   6271 C  C6    . DC  B 2 3   ? 33.272  -16.990 17.473  1.00 104.63 ? 3   DC  P C6    1 
ATOM   6272 P  P     . DC  B 2 4   ? 39.282  -15.368 16.558  1.00 102.18 ? 4   DC  P P     1 
ATOM   6273 O  OP1   . DC  B 2 4   ? 40.670  -15.572 16.086  1.00 115.13 ? 4   DC  P OP1   1 
ATOM   6274 O  OP2   . DC  B 2 4   ? 39.036  -14.933 17.950  1.00 109.04 ? 4   DC  P OP2   1 
ATOM   6275 O  "O5'" . DC  B 2 4   ? 38.549  -14.332 15.589  1.00 94.56  ? 4   DC  P "O5'" 1 
ATOM   6276 C  "C5'" . DC  B 2 4   ? 38.126  -14.753 14.301  1.00 102.89 ? 4   DC  P "C5'" 1 
ATOM   6277 C  "C4'" . DC  B 2 4   ? 37.434  -13.623 13.569  1.00 108.37 ? 4   DC  P "C4'" 1 
ATOM   6278 O  "O4'" . DC  B 2 4   ? 36.010  -13.656 13.848  1.00 111.38 ? 4   DC  P "O4'" 1 
ATOM   6279 C  "C3'" . DC  B 2 4   ? 37.911  -12.221 13.958  1.00 105.13 ? 4   DC  P "C3'" 1 
ATOM   6280 O  "O3'" . DC  B 2 4   ? 38.062  -11.428 12.795  1.00 108.43 ? 4   DC  P "O3'" 1 
ATOM   6281 C  "C2'" . DC  B 2 4   ? 36.778  -11.702 14.840  1.00 98.61  ? 4   DC  P "C2'" 1 
ATOM   6282 C  "C1'" . DC  B 2 4   ? 35.580  -12.359 14.182  1.00 101.68 ? 4   DC  P "C1'" 1 
ATOM   6283 N  N1    . DC  B 2 4   ? 34.390  -12.459 15.065  1.00 101.65 ? 4   DC  P N1    1 
ATOM   6284 C  C2    . DC  B 2 4   ? 33.133  -12.120 14.561  1.00 95.07  ? 4   DC  P C2    1 
ATOM   6285 O  O2    . DC  B 2 4   ? 33.037  -11.749 13.384  1.00 92.25  ? 4   DC  P O2    1 
ATOM   6286 N  N3    . DC  B 2 4   ? 32.053  -12.212 15.374  1.00 94.65  ? 4   DC  P N3    1 
ATOM   6287 C  C4    . DC  B 2 4   ? 32.199  -12.617 16.636  1.00 95.23  ? 4   DC  P C4    1 
ATOM   6288 N  N4    . DC  B 2 4   ? 31.104  -12.691 17.399  1.00 101.97 ? 4   DC  P N4    1 
ATOM   6289 C  C5    . DC  B 2 4   ? 33.475  -12.966 17.171  1.00 88.66  ? 4   DC  P C5    1 
ATOM   6290 C  C6    . DC  B 2 4   ? 34.533  -12.872 16.358  1.00 102.35 ? 4   DC  P C6    1 
ATOM   6291 P  P     . DA  B 2 5   ? 39.208  -10.307 12.722  1.00 105.62 ? 5   DA  P P     1 
ATOM   6292 O  OP1   . DA  B 2 5   ? 40.394  -10.924 12.087  1.00 116.49 ? 5   DA  P OP1   1 
ATOM   6293 O  OP2   . DA  B 2 5   ? 39.322  -9.687  14.061  1.00 94.48  ? 5   DA  P OP2   1 
ATOM   6294 O  "O5'" . DA  B 2 5   ? 38.603  -9.218  11.723  1.00 89.12  ? 5   DA  P "O5'" 1 
ATOM   6295 C  "C5'" . DA  B 2 5   ? 38.255  -9.596  10.402  1.00 84.39  ? 5   DA  P "C5'" 1 
ATOM   6296 C  "C4'" . DA  B 2 5   ? 36.912  -9.012  10.005  1.00 92.91  ? 5   DA  P "C4'" 1 
ATOM   6297 O  "O4'" . DA  B 2 5   ? 35.912  -9.355  11.001  1.00 104.42 ? 5   DA  P "O4'" 1 
ATOM   6298 C  "C3'" . DA  B 2 5   ? 36.873  -7.491  9.877   1.00 87.91  ? 5   DA  P "C3'" 1 
ATOM   6299 O  "O3'" . DA  B 2 5   ? 36.034  -7.141  8.792   1.00 91.88  ? 5   DA  P "O3'" 1 
ATOM   6300 C  "C2'" . DA  B 2 5   ? 36.272  -7.055  11.212  1.00 87.24  ? 5   DA  P "C2'" 1 
ATOM   6301 C  "C1'" . DA  B 2 5   ? 35.282  -8.179  11.466  1.00 99.19  ? 5   DA  P "C1'" 1 
ATOM   6302 N  N9    . DA  B 2 5   ? 34.943  -8.368  12.873  1.00 100.44 ? 5   DA  P N9    1 
ATOM   6303 C  C8    . DA  B 2 5   ? 35.810  -8.468  13.926  1.00 93.12  ? 5   DA  P C8    1 
ATOM   6304 N  N7    . DA  B 2 5   ? 35.218  -8.648  15.084  1.00 91.93  ? 5   DA  P N7    1 
ATOM   6305 C  C5    . DA  B 2 5   ? 33.870  -8.673  14.767  1.00 94.03  ? 5   DA  P C5    1 
ATOM   6306 C  C6    . DA  B 2 5   ? 32.711  -8.833  15.555  1.00 95.55  ? 5   DA  P C6    1 
ATOM   6307 N  N6    . DA  B 2 5   ? 32.740  -9.004  16.881  1.00 99.46  ? 5   DA  P N6    1 
ATOM   6308 N  N1    . DA  B 2 5   ? 31.518  -8.809  14.923  1.00 78.27  ? 5   DA  P N1    1 
ATOM   6309 C  C2    . DA  B 2 5   ? 31.493  -8.637  13.596  1.00 78.94  ? 5   DA  P C2    1 
ATOM   6310 N  N3    . DA  B 2 5   ? 32.512  -8.476  12.753  1.00 86.81  ? 5   DA  P N3    1 
ATOM   6311 C  C4    . DA  B 2 5   ? 33.683  -8.504  13.409  1.00 96.72  ? 5   DA  P C4    1 
ATOM   6312 P  P     . DC  B 2 6   ? 36.124  -5.685  8.122   1.00 97.07  ? 6   DC  P P     1 
ATOM   6313 O  OP1   . DC  B 2 6   ? 36.451  -5.876  6.692   1.00 101.25 ? 6   DC  P OP1   1 
ATOM   6314 O  OP2   . DC  B 2 6   ? 36.983  -4.834  8.976   1.00 107.19 ? 6   DC  P OP2   1 
ATOM   6315 O  "O5'" . DC  B 2 6   ? 34.628  -5.138  8.233   1.00 106.90 ? 6   DC  P "O5'" 1 
ATOM   6316 C  "C5'" . DC  B 2 6   ? 33.652  -5.901  8.930   1.00 100.63 ? 6   DC  P "C5'" 1 
ATOM   6317 C  "C4'" . DC  B 2 6   ? 32.500  -5.023  9.366   1.00 87.39  ? 6   DC  P "C4'" 1 
ATOM   6318 O  "O4'" . DC  B 2 6   ? 32.139  -5.344  10.737  1.00 96.54  ? 6   DC  P "O4'" 1 
ATOM   6319 C  "C3'" . DC  B 2 6   ? 32.801  -3.528  9.360   1.00 81.11  ? 6   DC  P "C3'" 1 
ATOM   6320 O  "O3'" . DC  B 2 6   ? 31.623  -2.807  9.054   1.00 94.53  ? 6   DC  P "O3'" 1 
ATOM   6321 C  "C2'" . DC  B 2 6   ? 33.234  -3.283  10.798  1.00 92.30  ? 6   DC  P "C2'" 1 
ATOM   6322 C  "C1'" . DC  B 2 6   ? 32.262  -4.187  11.537  1.00 88.55  ? 6   DC  P "C1'" 1 
ATOM   6323 N  N1    . DC  B 2 6   ? 32.729  -4.590  12.892  1.00 88.73  ? 6   DC  P N1    1 
ATOM   6324 C  C2    . DC  B 2 6   ? 31.790  -4.899  13.883  1.00 88.44  ? 6   DC  P C2    1 
ATOM   6325 O  O2    . DC  B 2 6   ? 30.583  -4.835  13.614  1.00 79.68  ? 6   DC  P O2    1 
ATOM   6326 N  N3    . DC  B 2 6   ? 32.231  -5.264  15.112  1.00 87.65  ? 6   DC  P N3    1 
ATOM   6327 C  C4    . DC  B 2 6   ? 33.541  -5.322  15.363  1.00 83.79  ? 6   DC  P C4    1 
ATOM   6328 N  N4    . DC  B 2 6   ? 33.927  -5.686  16.590  1.00 76.94  ? 6   DC  P N4    1 
ATOM   6329 C  C5    . DC  B 2 6   ? 34.512  -5.009  14.366  1.00 91.86  ? 6   DC  P C5    1 
ATOM   6330 C  C6    . DC  B 2 6   ? 34.066  -4.650  13.157  1.00 91.29  ? 6   DC  P C6    1 
ATOM   6331 P  P     . DG  B 2 7   ? 31.497  -2.009  7.667   1.00 97.65  ? 7   DG  P P     1 
ATOM   6332 O  OP1   . DG  B 2 7   ? 31.678  -2.982  6.567   1.00 106.99 ? 7   DG  P OP1   1 
ATOM   6333 O  OP2   . DG  B 2 7   ? 32.369  -0.816  7.755   1.00 91.33  ? 7   DG  P OP2   1 
ATOM   6334 O  "O5'" . DG  B 2 7   ? 29.976  -1.524  7.653   1.00 95.15  ? 7   DG  P "O5'" 1 
ATOM   6335 C  "C5'" . DG  B 2 7   ? 29.560  -0.513  8.551   1.00 99.33  ? 7   DG  P "C5'" 1 
ATOM   6336 C  "C4'" . DG  B 2 7   ? 28.219  -0.848  9.175   1.00 82.82  ? 7   DG  P "C4'" 1 
ATOM   6337 O  "O4'" . DG  B 2 7   ? 28.430  -1.660  10.355  1.00 72.49  ? 7   DG  P "O4'" 1 
ATOM   6338 C  "C3'" . DG  B 2 7   ? 27.455  0.361   9.671   1.00 88.27  ? 7   DG  P "C3'" 1 
ATOM   6339 O  "O3'" . DG  B 2 7   ? 26.066  0.085   9.737   1.00 91.43  ? 7   DG  P "O3'" 1 
ATOM   6340 C  "C2'" . DG  B 2 7   ? 28.055  0.576   11.055  1.00 82.81  ? 7   DG  P "C2'" 1 
ATOM   6341 C  "C1'" . DG  B 2 7   ? 28.351  -0.850  11.518  1.00 71.88  ? 7   DG  P "C1'" 1 
ATOM   6342 N  N9    . DG  B 2 7   ? 29.612  -0.960  12.245  1.00 76.21  ? 7   DG  P N9    1 
ATOM   6343 C  C8    . DG  B 2 7   ? 30.874  -0.778  11.733  1.00 83.01  ? 7   DG  P C8    1 
ATOM   6344 N  N7    . DG  B 2 7   ? 31.821  -0.933  12.615  1.00 86.43  ? 7   DG  P N7    1 
ATOM   6345 C  C5    . DG  B 2 7   ? 31.147  -1.235  13.790  1.00 78.82  ? 7   DG  P C5    1 
ATOM   6346 C  C6    . DG  B 2 7   ? 31.653  -1.507  15.083  1.00 78.22  ? 7   DG  P C6    1 
ATOM   6347 O  O6    . DG  B 2 7   ? 32.835  -1.534  15.455  1.00 76.55  ? 7   DG  P O6    1 
ATOM   6348 N  N1    . DG  B 2 7   ? 30.630  -1.764  15.992  1.00 76.31  ? 7   DG  P N1    1 
ATOM   6349 C  C2    . DG  B 2 7   ? 29.289  -1.759  15.689  1.00 70.61  ? 7   DG  P C2    1 
ATOM   6350 N  N2    . DG  B 2 7   ? 28.452  -2.031  16.701  1.00 62.54  ? 7   DG  P N2    1 
ATOM   6351 N  N3    . DG  B 2 7   ? 28.800  -1.506  14.480  1.00 75.27  ? 7   DG  P N3    1 
ATOM   6352 C  C4    . DG  B 2 7   ? 29.785  -1.253  13.582  1.00 73.91  ? 7   DG  P C4    1 
ATOM   6353 P  P     . DG  B 2 8   ? 25.021  1.305   9.765   1.00 90.41  ? 8   DG  P P     1 
ATOM   6354 O  OP1   . DG  B 2 8   ? 23.656  0.753   9.629   1.00 101.47 ? 8   DG  P OP1   1 
ATOM   6355 O  OP2   . DG  B 2 8   ? 25.507  2.321   8.805   1.00 93.45  ? 8   DG  P OP2   1 
ATOM   6356 O  "O5'" . DG  B 2 8   ? 25.179  1.909   11.237  1.00 85.54  ? 8   DG  P "O5'" 1 
ATOM   6357 C  "C5'" . DG  B 2 8   ? 24.816  1.126   12.369  1.00 85.83  ? 8   DG  P "C5'" 1 
ATOM   6358 C  "C4'" . DG  B 2 8   ? 25.336  1.754   13.649  1.00 84.41  ? 8   DG  P "C4'" 1 
ATOM   6359 O  "O4'" . DG  B 2 8   ? 26.717  1.404   13.841  1.00 71.84  ? 8   DG  P "O4'" 1 
ATOM   6360 C  "C3'" . DG  B 2 8   ? 25.292  3.282   13.683  1.00 86.96  ? 8   DG  P "C3'" 1 
ATOM   6361 O  "O3'" . DG  B 2 8   ? 24.214  3.711   14.504  1.00 83.07  ? 8   DG  P "O3'" 1 
ATOM   6362 C  "C2'" . DG  B 2 8   ? 26.659  3.702   14.264  1.00 76.91  ? 8   DG  P "C2'" 1 
ATOM   6363 C  "C1'" . DG  B 2 8   ? 27.301  2.376   14.665  1.00 72.50  ? 8   DG  P "C1'" 1 
ATOM   6364 N  N9    . DG  B 2 8   ? 28.751  2.339   14.471  1.00 73.53  ? 8   DG  P N9    1 
ATOM   6365 C  C8    . DG  B 2 8   ? 29.441  2.639   13.321  1.00 76.28  ? 8   DG  P C8    1 
ATOM   6366 N  N7    . DG  B 2 8   ? 30.734  2.512   13.441  1.00 75.29  ? 8   DG  P N7    1 
ATOM   6367 C  C5    . DG  B 2 8   ? 30.915  2.103   14.756  1.00 72.07  ? 8   DG  P C5    1 
ATOM   6368 C  C6    . DG  B 2 8   ? 32.106  1.806   15.464  1.00 74.42  ? 8   DG  P C6    1 
ATOM   6369 O  O6    . DG  B 2 8   ? 33.274  1.850   15.055  1.00 84.45  ? 8   DG  P O6    1 
ATOM   6370 N  N1    . DG  B 2 8   ? 31.843  1.427   16.777  1.00 68.68  ? 8   DG  P N1    1 
ATOM   6371 C  C2    . DG  B 2 8   ? 30.591  1.345   17.337  1.00 66.54  ? 8   DG  P C2    1 
ATOM   6372 N  N2    . DG  B 2 8   ? 30.539  0.961   18.621  1.00 65.96  ? 8   DG  P N2    1 
ATOM   6373 N  N3    . DG  B 2 8   ? 29.466  1.620   16.686  1.00 69.10  ? 8   DG  P N3    1 
ATOM   6374 C  C4    . DG  B 2 8   ? 29.704  1.990   15.404  1.00 67.94  ? 8   DG  P C4    1 
ATOM   6375 P  P     . DC  B 2 9   ? 23.952  5.276   14.755  1.00 79.62  ? 9   DC  P P     1 
ATOM   6376 O  OP1   . DC  B 2 9   ? 22.526  5.429   15.122  1.00 81.21  ? 9   DC  P OP1   1 
ATOM   6377 O  OP2   . DC  B 2 9   ? 24.511  6.028   13.609  1.00 80.21  ? 9   DC  P OP2   1 
ATOM   6378 O  "O5'" . DC  B 2 9   ? 24.807  5.595   16.065  1.00 67.16  ? 9   DC  P "O5'" 1 
ATOM   6379 C  "C5'" . DC  B 2 9   ? 24.609  4.818   17.238  1.00 70.37  ? 9   DC  P "C5'" 1 
ATOM   6380 C  "C4'" . DC  B 2 9   ? 25.572  5.239   18.331  1.00 75.91  ? 9   DC  P "C4'" 1 
ATOM   6381 O  "O4'" . DC  B 2 9   ? 26.897  4.767   18.016  1.00 78.72  ? 9   DC  P "O4'" 1 
ATOM   6382 C  "C3'" . DC  B 2 9   ? 25.692  6.752   18.535  1.00 66.06  ? 9   DC  P "C3'" 1 
ATOM   6383 O  "O3'" . DC  B 2 9   ? 25.182  7.107   19.813  1.00 77.52  ? 9   DC  P "O3'" 1 
ATOM   6384 C  "C2'" . DC  B 2 9   ? 27.198  7.048   18.415  1.00 62.11  ? 9   DC  P "C2'" 1 
ATOM   6385 C  "C1'" . DC  B 2 9   ? 27.835  5.668   18.535  1.00 68.55  ? 9   DC  P "C1'" 1 
ATOM   6386 N  N1    . DC  B 2 9   ? 29.095  5.525   17.750  1.00 65.05  ? 9   DC  P N1    1 
ATOM   6387 C  C2    . DC  B 2 9   ? 30.278  5.139   18.394  1.00 71.62  ? 9   DC  P C2    1 
ATOM   6388 O  O2    . DC  B 2 9   ? 30.262  4.924   19.613  1.00 65.15  ? 9   DC  P O2    1 
ATOM   6389 N  N3    . DC  B 2 9   ? 31.413  5.012   17.660  1.00 61.69  ? 9   DC  P N3    1 
ATOM   6390 C  C4    . DC  B 2 9   ? 31.390  5.253   16.348  1.00 59.23  ? 9   DC  P C4    1 
ATOM   6391 N  N4    . DC  B 2 9   ? 32.531  5.115   15.666  1.00 62.52  ? 9   DC  P N4    1 
ATOM   6392 C  C5    . DC  B 2 9   ? 30.195  5.644   15.676  1.00 63.51  ? 9   DC  P C5    1 
ATOM   6393 C  C6    . DC  B 2 9   ? 29.083  5.766   16.408  1.00 58.56  ? 9   DC  P C6    1 
ATOM   6394 P  P     . DC  B 2 10  ? 25.019  8.652   20.220  1.00 67.31  ? 10  DC  P P     1 
ATOM   6395 O  OP1   . DC  B 2 10  ? 23.939  8.738   21.230  1.00 63.65  ? 10  DC  P OP1   1 
ATOM   6396 O  OP2   . DC  B 2 10  ? 24.939  9.448   18.976  1.00 70.12  ? 10  DC  P OP2   1 
ATOM   6397 O  "O5'" . DC  B 2 10  ? 26.401  8.996   20.937  1.00 65.28  ? 10  DC  P "O5'" 1 
ATOM   6398 C  "C5'" . DC  B 2 10  ? 26.828  8.211   22.034  1.00 71.04  ? 10  DC  P "C5'" 1 
ATOM   6399 C  "C4'" . DC  B 2 10  ? 28.280  8.488   22.362  1.00 71.44  ? 10  DC  P "C4'" 1 
ATOM   6400 O  "O4'" . DC  B 2 10  ? 29.122  8.025   21.280  1.00 64.49  ? 10  DC  P "O4'" 1 
ATOM   6401 C  "C3'" . DC  B 2 10  ? 28.626  9.965   22.581  1.00 63.15  ? 10  DC  P "C3'" 1 
ATOM   6402 O  "O3'" . DC  B 2 10  ? 29.200  10.125  23.870  1.00 65.96  ? 10  DC  P "O3'" 1 
ATOM   6403 C  "C2'" . DC  B 2 10  ? 29.627  10.287  21.460  1.00 62.76  ? 10  DC  P "C2'" 1 
ATOM   6404 C  "C1'" . DC  B 2 10  ? 30.194  8.917   21.130  1.00 67.98  ? 10  DC  P "C1'" 1 
ATOM   6405 N  N1    . DC  B 2 10  ? 30.712  8.802   19.736  1.00 61.79  ? 10  DC  P N1    1 
ATOM   6406 C  C2    . DC  B 2 10  ? 31.941  8.175   19.507  1.00 60.87  ? 10  DC  P C2    1 
ATOM   6407 O  O2    . DC  B 2 10  ? 32.576  7.725   20.469  1.00 56.46  ? 10  DC  P O2    1 
ATOM   6408 N  N3    . DC  B 2 10  ? 32.401  8.077   18.235  1.00 53.11  ? 10  DC  P N3    1 
ATOM   6409 C  C4    . DC  B 2 10  ? 31.685  8.574   17.225  1.00 60.09  ? 10  DC  P C4    1 
ATOM   6410 N  N4    . DC  B 2 10  ? 32.181  8.453   15.989  1.00 55.96  ? 10  DC  P N4    1 
ATOM   6411 C  C5    . DC  B 2 10  ? 30.430  9.218   17.439  1.00 57.45  ? 10  DC  P C5    1 
ATOM   6412 C  C6    . DC  B 2 10  ? 29.986  9.309   18.698  1.00 60.32  ? 10  DC  P C6    1 
ATOM   6413 P  P     . DA  B 2 11  ? 29.577  11.581  24.434  1.00 65.60  ? 11  DA  P P     1 
ATOM   6414 O  OP1   . DA  B 2 11  ? 29.120  11.638  25.841  1.00 66.48  ? 11  DA  P OP1   1 
ATOM   6415 O  OP2   . DA  B 2 11  ? 29.134  12.604  23.460  1.00 64.68  ? 11  DA  P OP2   1 
ATOM   6416 O  "O5'" . DA  B 2 11  ? 31.172  11.570  24.443  1.00 71.98  ? 11  DA  P "O5'" 1 
ATOM   6417 C  "C5'" . DA  B 2 11  ? 31.859  10.525  25.111  1.00 62.60  ? 11  DA  P "C5'" 1 
ATOM   6418 C  "C4'" . DA  B 2 11  ? 33.314  10.491  24.694  1.00 59.67  ? 11  DA  P "C4'" 1 
ATOM   6419 O  "O4'" . DA  B 2 11  ? 33.405  10.125  23.302  1.00 60.80  ? 11  DA  P "O4'" 1 
ATOM   6420 C  "C3'" . DA  B 2 11  ? 34.049  11.827  24.830  1.00 55.14  ? 11  DA  P "C3'" 1 
ATOM   6421 O  "O3'" . DA  B 2 11  ? 35.054  11.728  25.828  1.00 66.05  ? 11  DA  P "O3'" 1 
ATOM   6422 C  "C2'" . DA  B 2 11  ? 34.651  12.087  23.439  1.00 55.48  ? 11  DA  P "C2'" 1 
ATOM   6423 C  "C1'" . DA  B 2 11  ? 34.543  10.731  22.758  1.00 49.87  ? 11  DA  P "C1'" 1 
ATOM   6424 N  N9    . DA  B 2 11  ? 34.369  10.825  21.314  1.00 55.73  ? 11  DA  P N9    1 
ATOM   6425 C  C8    . DA  B 2 11  ? 33.234  11.182  20.644  1.00 52.71  ? 11  DA  P C8    1 
ATOM   6426 N  N7    . DA  B 2 11  ? 33.369  11.185  19.338  1.00 57.30  ? 11  DA  P N7    1 
ATOM   6427 C  C5    . DA  B 2 11  ? 34.686  10.805  19.140  1.00 60.56  ? 11  DA  P C5    1 
ATOM   6428 C  C6    . DA  B 2 11  ? 35.456  10.617  17.975  1.00 59.81  ? 11  DA  P C6    1 
ATOM   6429 N  N6    . DA  B 2 11  ? 34.977  10.797  16.740  1.00 52.10  ? 11  DA  P N6    1 
ATOM   6430 N  N1    . DA  B 2 11  ? 36.741  10.234  18.129  1.00 60.17  ? 11  DA  P N1    1 
ATOM   6431 C  C2    . DA  B 2 11  ? 37.216  10.055  19.366  1.00 56.87  ? 11  DA  P C2    1 
ATOM   6432 N  N3    . DA  B 2 11  ? 36.591  10.200  20.534  1.00 57.92  ? 11  DA  P N3    1 
ATOM   6433 C  C4    . DA  B 2 11  ? 35.317  10.580  20.348  1.00 62.40  ? 11  DA  P C4    1 
ATOM   6434 P  P     . DC  B 2 12  ? 35.940  13.011  26.210  1.00 62.82  ? 12  DC  P P     1 
ATOM   6435 O  OP1   . DC  B 2 12  ? 36.468  12.807  27.576  1.00 64.77  ? 12  DC  P OP1   1 
ATOM   6436 O  OP2   . DC  B 2 12  ? 35.151  14.224  25.904  1.00 61.54  ? 12  DC  P OP2   1 
ATOM   6437 O  "O5'" . DC  B 2 12  ? 37.152  12.955  25.175  1.00 73.63  ? 12  DC  P "O5'" 1 
ATOM   6438 C  "C5'" . DC  B 2 12  ? 38.089  11.893  25.236  1.00 56.61  ? 12  DC  P "C5'" 1 
ATOM   6439 C  "C4'" . DC  B 2 12  ? 39.360  12.276  24.508  1.00 60.56  ? 12  DC  P "C4'" 1 
ATOM   6440 O  "O4'" . DC  B 2 12  ? 39.147  12.157  23.079  1.00 69.70  ? 12  DC  P "O4'" 1 
ATOM   6441 C  "C3'" . DC  B 2 12  ? 39.823  13.711  24.756  1.00 61.25  ? 12  DC  P "C3'" 1 
ATOM   6442 O  "O3'" . DC  B 2 12  ? 41.234  13.755  24.913  1.00 78.05  ? 12  DC  P "O3'" 1 
ATOM   6443 C  "C2'" . DC  B 2 12  ? 39.367  14.455  23.503  1.00 59.10  ? 12  DC  P "C2'" 1 
ATOM   6444 C  "C1'" . DC  B 2 12  ? 39.465  13.373  22.439  1.00 54.71  ? 12  DC  P "C1'" 1 
ATOM   6445 N  N1    . DC  B 2 12  ? 38.515  13.566  21.313  1.00 58.05  ? 12  DC  P N1    1 
ATOM   6446 C  C2    . DC  B 2 12  ? 38.973  13.457  19.997  1.00 59.29  ? 12  DC  P C2    1 
ATOM   6447 O  O2    . DC  B 2 12  ? 40.165  13.200  19.793  1.00 61.33  ? 12  DC  P O2    1 
ATOM   6448 N  N3    . DC  B 2 12  ? 38.093  13.634  18.980  1.00 64.46  ? 12  DC  P N3    1 
ATOM   6449 C  C4    . DC  B 2 12  ? 36.814  13.909  19.243  1.00 59.63  ? 12  DC  P C4    1 
ATOM   6450 N  N4    . DC  B 2 12  ? 35.984  14.076  18.208  1.00 56.35  ? 12  DC  P N4    1 
ATOM   6451 C  C5    . DC  B 2 12  ? 36.329  14.025  20.580  1.00 55.09  ? 12  DC  P C5    1 
ATOM   6452 C  C6    . DC  B 2 12  ? 37.206  13.848  21.574  1.00 60.01  ? 12  DC  P C6    1 
ATOM   6453 P  P     . DA  B 2 13  ? 41.928  15.032  25.600  1.00 80.07  ? 13  DA  P P     1 
ATOM   6454 O  OP1   . DA  B 2 13  ? 43.025  14.540  26.465  1.00 67.34  ? 13  DA  P OP1   1 
ATOM   6455 O  OP2   . DA  B 2 13  ? 40.856  15.880  26.170  1.00 72.52  ? 13  DA  P OP2   1 
ATOM   6456 O  "O5'" . DA  B 2 13  ? 42.551  15.827  24.366  1.00 65.61  ? 13  DA  P "O5'" 1 
ATOM   6457 C  "C5'" . DA  B 2 13  ? 43.259  15.118  23.370  1.00 62.81  ? 13  DA  P "C5'" 1 
ATOM   6458 C  "C4'" . DA  B 2 13  ? 43.572  16.008  22.184  1.00 59.37  ? 13  DA  P "C4'" 1 
ATOM   6459 O  "O4'" . DA  B 2 13  ? 42.775  15.601  21.053  1.00 61.38  ? 13  DA  P "O4'" 1 
ATOM   6460 C  "C3'" . DA  B 2 13  ? 43.238  17.474  22.371  1.00 72.98  ? 13  DA  P "C3'" 1 
ATOM   6461 O  "O3'" . DA  B 2 13  ? 44.297  18.131  23.051  1.00 92.50  ? 13  DA  P "O3'" 1 
ATOM   6462 C  "C2'" . DA  B 2 13  ? 43.121  17.951  20.927  1.00 69.73  ? 13  DA  P "C2'" 1 
ATOM   6463 C  "C1'" . DA  B 2 13  ? 42.549  16.718  20.213  1.00 69.90  ? 13  DA  P "C1'" 1 
ATOM   6464 N  N9    . DA  B 2 13  ? 41.119  16.817  19.934  1.00 63.68  ? 13  DA  P N9    1 
ATOM   6465 C  C8    . DA  B 2 13  ? 40.102  16.905  20.845  1.00 58.82  ? 13  DA  P C8    1 
ATOM   6466 N  N7    . DA  B 2 13  ? 38.910  16.989  20.301  1.00 56.50  ? 13  DA  P N7    1 
ATOM   6467 C  C5    . DA  B 2 13  ? 39.163  16.955  18.939  1.00 50.69  ? 13  DA  P C5    1 
ATOM   6468 C  C6    . DA  B 2 13  ? 38.315  17.006  17.813  1.00 54.03  ? 13  DA  P C6    1 
ATOM   6469 N  N6    . DA  B 2 13  ? 36.984  17.107  17.897  1.00 67.04  ? 13  DA  P N6    1 
ATOM   6470 N  N1    . DA  B 2 13  ? 38.892  16.950  16.594  1.00 62.21  ? 13  DA  P N1    1 
ATOM   6471 C  C2    . DA  B 2 13  ? 40.224  16.849  16.513  1.00 53.05  ? 13  DA  P C2    1 
ATOM   6472 N  N3    . DA  B 2 13  ? 41.121  16.791  17.497  1.00 53.21  ? 13  DA  P N3    1 
ATOM   6473 C  C4    . DA  B 2 13  ? 40.519  16.850  18.695  1.00 57.55  ? 13  DA  P C4    1 
ATOM   6474 P  P     . DA  C 3 2   ? 24.945  20.023  11.071  1.00 174.14 ? 2   DA  T P     1 
ATOM   6475 O  OP1   . DA  C 3 2   ? 23.877  20.819  10.426  1.00 113.69 ? 2   DA  T OP1   1 
ATOM   6476 O  OP2   . DA  C 3 2   ? 25.537  20.477  12.350  1.00 120.65 ? 2   DA  T OP2   1 
ATOM   6477 O  "O5'" . DA  C 3 2   ? 26.143  19.812  10.033  1.00 142.54 ? 2   DA  T "O5'" 1 
ATOM   6478 C  "C5'" . DA  C 3 2   ? 26.015  18.869  8.979   1.00 125.69 ? 2   DA  T "C5'" 1 
ATOM   6479 C  "C4'" . DA  C 3 2   ? 27.368  18.286  8.613   1.00 124.88 ? 2   DA  T "C4'" 1 
ATOM   6480 O  "O4'" . DA  C 3 2   ? 27.271  17.635  7.322   1.00 127.94 ? 2   DA  T "O4'" 1 
ATOM   6481 C  "C3'" . DA  C 3 2   ? 28.493  19.307  8.478   1.00 127.48 ? 2   DA  T "C3'" 1 
ATOM   6482 O  "O3'" . DA  C 3 2   ? 29.167  19.460  9.728   1.00 111.13 ? 2   DA  T "O3'" 1 
ATOM   6483 C  "C2'" . DA  C 3 2   ? 29.400  18.669  7.430   1.00 125.46 ? 2   DA  T "C2'" 1 
ATOM   6484 C  "C1'" . DA  C 3 2   ? 28.400  17.948  6.528   1.00 132.36 ? 2   DA  T "C1'" 1 
ATOM   6485 N  N9    . DA  C 3 2   ? 27.958  18.738  5.378   1.00 139.12 ? 2   DA  T N9    1 
ATOM   6486 C  C8    . DA  C 3 2   ? 27.238  19.902  5.398   1.00 117.00 ? 2   DA  T C8    1 
ATOM   6487 N  N7    . DA  C 3 2   ? 26.980  20.387  4.206   1.00 109.62 ? 2   DA  T N7    1 
ATOM   6488 C  C5    . DA  C 3 2   ? 27.568  19.477  3.343   1.00 124.15 ? 2   DA  T C5    1 
ATOM   6489 C  C6    . DA  C 3 2   ? 27.651  19.417  1.937   1.00 131.00 ? 2   DA  T C6    1 
ATOM   6490 N  N6    . DA  C 3 2   ? 27.112  20.336  1.129   1.00 127.54 ? 2   DA  T N6    1 
ATOM   6491 N  N1    . DA  C 3 2   ? 28.312  18.373  1.392   1.00 126.53 ? 2   DA  T N1    1 
ATOM   6492 C  C2    . DA  C 3 2   ? 28.850  17.455  2.205   1.00 119.54 ? 2   DA  T C2    1 
ATOM   6493 N  N3    . DA  C 3 2   ? 28.837  17.404  3.536   1.00 128.33 ? 2   DA  T N3    1 
ATOM   6494 C  C4    . DA  C 3 2   ? 28.174  18.454  4.048   1.00 137.21 ? 2   DA  T C4    1 
ATOM   6495 P  P     . DC  C 3 3   ? 29.748  20.893  10.171  1.00 70.17  ? 3   DC  T P     1 
ATOM   6496 O  OP1   . DC  C 3 3   ? 29.514  21.042  11.625  1.00 63.75  ? 3   DC  T OP1   1 
ATOM   6497 O  OP2   . DC  C 3 3   ? 29.217  21.908  9.234   1.00 65.90  ? 3   DC  T OP2   1 
ATOM   6498 O  "O5'" . DC  C 3 3   ? 31.325  20.771  9.918   1.00 77.82  ? 3   DC  T "O5'" 1 
ATOM   6499 C  "C5'" . DC  C 3 3   ? 31.861  21.042  8.630   1.00 56.82  ? 3   DC  T "C5'" 1 
ATOM   6500 C  "C4'" . DC  C 3 3   ? 33.360  21.280  8.704   1.00 73.97  ? 3   DC  T "C4'" 1 
ATOM   6501 O  "O4'" . DC  C 3 3   ? 33.656  22.193  9.788   1.00 60.86  ? 3   DC  T "O4'" 1 
ATOM   6502 C  "C3'" . DC  C 3 3   ? 34.197  20.056  9.017   1.00 59.62  ? 3   DC  T "C3'" 1 
ATOM   6503 O  "O3'" . DC  C 3 3   ? 34.430  19.302  7.842   1.00 55.39  ? 3   DC  T "O3'" 1 
ATOM   6504 C  "C2'" . DC  C 3 3   ? 35.476  20.698  9.529   1.00 53.96  ? 3   DC  T "C2'" 1 
ATOM   6505 C  "C1'" . DC  C 3 3   ? 34.926  21.873  10.338  1.00 53.07  ? 3   DC  T "C1'" 1 
ATOM   6506 N  N1    . DC  C 3 3   ? 34.754  21.559  11.780  1.00 62.21  ? 3   DC  T N1    1 
ATOM   6507 C  C2    . DC  C 3 3   ? 35.881  21.456  12.601  1.00 55.95  ? 3   DC  T C2    1 
ATOM   6508 O  O2    . DC  C 3 3   ? 36.999  21.633  12.111  1.00 59.41  ? 3   DC  T O2    1 
ATOM   6509 N  N3    . DC  C 3 3   ? 35.714  21.168  13.913  1.00 59.11  ? 3   DC  T N3    1 
ATOM   6510 C  C4    . DC  C 3 3   ? 34.490  20.985  14.404  1.00 49.64  ? 3   DC  T C4    1 
ATOM   6511 N  N4    . DC  C 3 3   ? 34.375  20.702  15.705  1.00 56.24  ? 3   DC  T N4    1 
ATOM   6512 C  C5    . DC  C 3 3   ? 33.328  21.083  13.583  1.00 54.31  ? 3   DC  T C5    1 
ATOM   6513 C  C6    . DC  C 3 3   ? 33.505  21.368  12.289  1.00 57.75  ? 3   DC  T C6    1 
ATOM   6514 P  P     . DT  C 3 4   ? 34.754  17.733  7.953   1.00 56.50  ? 4   DT  T P     1 
ATOM   6515 O  OP1   . DT  C 3 4   ? 34.741  17.176  6.584   1.00 49.31  ? 4   DT  T OP1   1 
ATOM   6516 O  OP2   . DT  C 3 4   ? 33.869  17.163  8.993   1.00 63.45  ? 4   DT  T OP2   1 
ATOM   6517 O  "O5'" . DT  C 3 4   ? 36.249  17.683  8.520   1.00 66.08  ? 4   DT  T "O5'" 1 
ATOM   6518 C  "C5'" . DT  C 3 4   ? 37.332  18.156  7.725   1.00 56.55  ? 4   DT  T "C5'" 1 
ATOM   6519 C  "C4'" . DT  C 3 4   ? 38.651  17.931  8.438   1.00 52.30  ? 4   DT  T "C4'" 1 
ATOM   6520 O  "O4'" . DT  C 3 4   ? 38.630  18.634  9.698   1.00 60.83  ? 4   DT  T "O4'" 1 
ATOM   6521 C  "C3'" . DT  C 3 4   ? 38.941  16.481  8.785   1.00 49.58  ? 4   DT  T "C3'" 1 
ATOM   6522 O  "O3'" . DT  C 3 4   ? 39.665  15.876  7.722   1.00 54.29  ? 4   DT  T "O3'" 1 
ATOM   6523 C  "C2'" . DT  C 3 4   ? 39.793  16.585  10.050  1.00 52.56  ? 4   DT  T "C2'" 1 
ATOM   6524 C  "C1'" . DT  C 3 4   ? 39.328  17.899  10.683  1.00 51.20  ? 4   DT  T "C1'" 1 
ATOM   6525 N  N1    . DT  C 3 4   ? 38.434  17.732  11.870  1.00 55.31  ? 4   DT  T N1    1 
ATOM   6526 C  C2    . DT  C 3 4   ? 38.994  17.511  13.106  1.00 58.35  ? 4   DT  T C2    1 
ATOM   6527 O  O2    . DT  C 3 4   ? 40.195  17.423  13.290  1.00 64.27  ? 4   DT  T O2    1 
ATOM   6528 N  N3    . DT  C 3 4   ? 38.091  17.387  14.130  1.00 57.61  ? 4   DT  T N3    1 
ATOM   6529 C  C4    . DT  C 3 4   ? 36.714  17.467  14.044  1.00 53.23  ? 4   DT  T C4    1 
ATOM   6530 O  O4    . DT  C 3 4   ? 35.988  17.342  15.025  1.00 60.39  ? 4   DT  T O4    1 
ATOM   6531 C  C5    . DT  C 3 4   ? 36.191  17.707  12.720  1.00 53.74  ? 4   DT  T C5    1 
ATOM   6532 C  C7    . DT  C 3 4   ? 34.710  17.812  12.503  1.00 53.56  ? 4   DT  T C7    1 
ATOM   6533 C  C6    . DT  C 3 4   ? 37.066  17.830  11.709  1.00 52.27  ? 4   DT  T C6    1 
ATOM   6534 P  P     . DG  C 3 5   ? 39.561  14.295  7.464   1.00 58.79  ? 5   DG  T P     1 
ATOM   6535 O  OP1   . DG  C 3 5   ? 40.107  14.032  6.113   1.00 54.93  ? 5   DG  T OP1   1 
ATOM   6536 O  OP2   . DG  C 3 5   ? 38.183  13.872  7.800   1.00 66.46  ? 5   DG  T OP2   1 
ATOM   6537 O  "O5'" . DG  C 3 5   ? 40.535  13.661  8.563   1.00 67.62  ? 5   DG  T "O5'" 1 
ATOM   6538 C  "C5'" . DG  C 3 5   ? 41.894  14.079  8.638   1.00 67.20  ? 5   DG  T "C5'" 1 
ATOM   6539 C  "C4'" . DG  C 3 5   ? 42.535  13.603  9.930   1.00 55.87  ? 5   DG  T "C4'" 1 
ATOM   6540 O  "O4'" . DG  C 3 5   ? 41.818  14.162  11.064  1.00 55.44  ? 5   DG  T "O4'" 1 
ATOM   6541 C  "C3'" . DG  C 3 5   ? 42.538  12.086  10.126  1.00 57.04  ? 5   DG  T "C3'" 1 
ATOM   6542 O  "O3'" . DG  C 3 5   ? 43.811  11.653  10.582  1.00 68.52  ? 5   DG  T "O3'" 1 
ATOM   6543 C  "C2'" . DG  C 3 5   ? 41.456  11.853  11.177  1.00 59.86  ? 5   DG  T "C2'" 1 
ATOM   6544 C  "C1'" . DG  C 3 5   ? 41.511  13.140  11.984  1.00 57.40  ? 5   DG  T "C1'" 1 
ATOM   6545 N  N9    . DG  C 3 5   ? 40.240  13.456  12.630  1.00 58.15  ? 5   DG  T N9    1 
ATOM   6546 C  C8    . DG  C 3 5   ? 39.041  13.716  12.010  1.00 55.78  ? 5   DG  T C8    1 
ATOM   6547 N  N7    . DG  C 3 5   ? 38.067  13.956  12.843  1.00 51.88  ? 5   DG  T N7    1 
ATOM   6548 C  C5    . DG  C 3 5   ? 38.654  13.842  14.097  1.00 50.30  ? 5   DG  T C5    1 
ATOM   6549 C  C6    . DG  C 3 5   ? 38.089  13.994  15.385  1.00 47.13  ? 5   DG  T C6    1 
ATOM   6550 O  O6    . DG  C 3 5   ? 36.918  14.269  15.681  1.00 57.87  ? 5   DG  T O6    1 
ATOM   6551 N  N1    . DG  C 3 5   ? 39.033  13.795  16.389  1.00 58.04  ? 5   DG  T N1    1 
ATOM   6552 C  C2    . DG  C 3 5   ? 40.355  13.487  16.175  1.00 54.42  ? 5   DG  T C2    1 
ATOM   6553 N  N2    . DG  C 3 5   ? 41.114  13.332  17.270  1.00 58.78  ? 5   DG  T N2    1 
ATOM   6554 N  N3    . DG  C 3 5   ? 40.897  13.341  14.973  1.00 51.24  ? 5   DG  T N3    1 
ATOM   6555 C  C4    . DG  C 3 5   ? 39.991  13.532  13.984  1.00 52.56  ? 5   DG  T C4    1 
ATOM   6556 P  P     . DT  C 3 6   ? 44.087  10.090  10.834  1.00 64.60  ? 6   DT  T P     1 
ATOM   6557 O  OP1   . DT  C 3 6   ? 45.527  9.845   10.601  1.00 69.42  ? 6   DT  T OP1   1 
ATOM   6558 O  OP2   . DT  C 3 6   ? 43.084  9.321   10.065  1.00 64.11  ? 6   DT  T OP2   1 
ATOM   6559 O  "O5'" . DT  C 3 6   ? 43.780  9.892   12.392  1.00 52.18  ? 6   DT  T "O5'" 1 
ATOM   6560 C  "C5'" . DT  C 3 6   ? 44.644  10.470  13.367  1.00 61.57  ? 6   DT  T "C5'" 1 
ATOM   6561 C  "C4'" . DT  C 3 6   ? 44.241  10.037  14.765  1.00 59.07  ? 6   DT  T "C4'" 1 
ATOM   6562 O  "O4'" . DT  C 3 6   ? 42.934  10.578  15.076  1.00 65.70  ? 6   DT  T "O4'" 1 
ATOM   6563 C  "C3'" . DT  C 3 6   ? 44.141  8.520   14.963  1.00 63.43  ? 6   DT  T "C3'" 1 
ATOM   6564 O  "O3'" . DT  C 3 6   ? 44.977  8.101   16.033  1.00 57.30  ? 6   DT  T "O3'" 1 
ATOM   6565 C  "C2'" . DT  C 3 6   ? 42.662  8.269   15.271  1.00 61.45  ? 6   DT  T "C2'" 1 
ATOM   6566 C  "C1'" . DT  C 3 6   ? 42.191  9.621   15.783  1.00 57.41  ? 6   DT  T "C1'" 1 
ATOM   6567 N  N1    . DT  C 3 6   ? 40.746  9.861   15.524  1.00 60.98  ? 6   DT  T N1    1 
ATOM   6568 C  C2    . DT  C 3 6   ? 39.897  10.071  16.585  1.00 63.57  ? 6   DT  T C2    1 
ATOM   6569 O  O2    . DT  C 3 6   ? 40.267  10.087  17.743  1.00 67.85  ? 6   DT  T O2    1 
ATOM   6570 N  N3    . DT  C 3 6   ? 38.587  10.270  16.238  1.00 55.84  ? 6   DT  T N3    1 
ATOM   6571 C  C4    . DT  C 3 6   ? 38.052  10.274  14.964  1.00 53.44  ? 6   DT  T C4    1 
ATOM   6572 O  O4    . DT  C 3 6   ? 36.858  10.463  14.754  1.00 60.56  ? 6   DT  T O4    1 
ATOM   6573 C  C5    . DT  C 3 6   ? 38.996  10.042  13.897  1.00 54.27  ? 6   DT  T C5    1 
ATOM   6574 C  C7    . DT  C 3 6   ? 38.533  10.025  12.471  1.00 61.21  ? 6   DT  T C7    1 
ATOM   6575 C  C6    . DT  C 3 6   ? 40.282  9.846   14.225  1.00 54.35  ? 6   DT  T C6    1 
ATOM   6576 P  P     . DG  C 3 7   ? 45.263  6.535   16.260  1.00 61.54  ? 7   DG  T P     1 
ATOM   6577 O  OP1   . DG  C 3 7   ? 46.496  6.421   17.073  1.00 73.06  ? 7   DG  T OP1   1 
ATOM   6578 O  OP2   . DG  C 3 7   ? 45.188  5.870   14.939  1.00 55.34  ? 7   DG  T OP2   1 
ATOM   6579 O  "O5'" . DG  C 3 7   ? 44.016  6.040   17.136  1.00 58.53  ? 7   DG  T "O5'" 1 
ATOM   6580 C  "C5'" . DG  C 3 7   ? 43.784  6.622   18.412  1.00 71.51  ? 7   DG  T "C5'" 1 
ATOM   6581 C  "C4'" . DG  C 3 7   ? 42.446  6.195   18.997  1.00 77.81  ? 7   DG  T "C4'" 1 
ATOM   6582 O  "O4'" . DG  C 3 7   ? 41.371  6.885   18.343  1.00 71.42  ? 7   DG  T "O4'" 1 
ATOM   6583 C  "C3'" . DG  C 3 7   ? 42.088  4.723   18.843  1.00 70.88  ? 7   DG  T "C3'" 1 
ATOM   6584 O  "O3'" . DG  C 3 7   ? 42.599  3.981   19.946  1.00 74.87  ? 7   DG  T "O3'" 1 
ATOM   6585 C  "C2'" . DG  C 3 7   ? 40.546  4.732   18.834  1.00 68.75  ? 7   DG  T "C2'" 1 
ATOM   6586 C  "C1'" . DG  C 3 7   ? 40.185  6.217   18.690  1.00 66.34  ? 7   DG  T "C1'" 1 
ATOM   6587 N  N9    . DG  C 3 7   ? 39.167  6.477   17.675  1.00 60.05  ? 7   DG  T N9    1 
ATOM   6588 C  C8    . DG  C 3 7   ? 39.349  6.571   16.316  1.00 59.71  ? 7   DG  T C8    1 
ATOM   6589 N  N7    . DG  C 3 7   ? 38.244  6.806   15.660  1.00 50.15  ? 7   DG  T N7    1 
ATOM   6590 C  C5    . DG  C 3 7   ? 37.268  6.867   16.649  1.00 60.99  ? 7   DG  T C5    1 
ATOM   6591 C  C6    . DG  C 3 7   ? 35.874  7.096   16.544  1.00 56.51  ? 7   DG  T C6    1 
ATOM   6592 O  O6    . DG  C 3 7   ? 35.201  7.296   15.522  1.00 54.16  ? 7   DG  T O6    1 
ATOM   6593 N  N1    . DG  C 3 7   ? 35.255  7.078   17.792  1.00 49.81  ? 7   DG  T N1    1 
ATOM   6594 C  C2    . DG  C 3 7   ? 35.900  6.865   18.987  1.00 58.17  ? 7   DG  T C2    1 
ATOM   6595 N  N2    . DG  C 3 7   ? 35.134  6.884   20.088  1.00 56.24  ? 7   DG  T N2    1 
ATOM   6596 N  N3    . DG  C 3 7   ? 37.204  6.650   19.098  1.00 68.25  ? 7   DG  T N3    1 
ATOM   6597 C  C4    . DG  C 3 7   ? 37.822  6.665   17.893  1.00 60.79  ? 7   DG  T C4    1 
ATOM   6598 P  P     . DG  C 3 8   ? 42.230  2.425   20.125  1.00 71.40  ? 8   DG  T P     1 
ATOM   6599 O  OP1   . DG  C 3 8   ? 43.341  1.794   20.873  1.00 71.15  ? 8   DG  T OP1   1 
ATOM   6600 O  OP2   . DG  C 3 8   ? 41.838  1.883   18.805  1.00 63.48  ? 8   DG  T OP2   1 
ATOM   6601 O  "O5'" . DG  C 3 8   ? 40.949  2.445   21.081  1.00 59.12  ? 8   DG  T "O5'" 1 
ATOM   6602 C  "C5'" . DG  C 3 8   ? 40.985  3.184   22.294  1.00 63.24  ? 8   DG  T "C5'" 1 
ATOM   6603 C  "C4'" . DG  C 3 8   ? 39.721  2.971   23.110  1.00 68.53  ? 8   DG  T "C4'" 1 
ATOM   6604 O  "O4'" . DG  C 3 8   ? 38.584  3.546   22.420  1.00 76.41  ? 8   DG  T "O4'" 1 
ATOM   6605 C  "C3'" . DG  C 3 8   ? 39.352  1.519   23.384  1.00 65.13  ? 8   DG  T "C3'" 1 
ATOM   6606 O  "O3'" . DG  C 3 8   ? 38.735  1.422   24.657  1.00 55.18  ? 8   DG  T "O3'" 1 
ATOM   6607 C  "C2'" . DG  C 3 8   ? 38.373  1.198   22.258  1.00 64.51  ? 8   DG  T "C2'" 1 
ATOM   6608 C  "C1'" . DG  C 3 8   ? 37.663  2.534   22.062  1.00 65.35  ? 8   DG  T "C1'" 1 
ATOM   6609 N  N9    . DG  C 3 8   ? 37.251  2.780   20.686  1.00 63.09  ? 8   DG  T N9    1 
ATOM   6610 C  C8    . DG  C 3 8   ? 38.021  2.642   19.557  1.00 63.55  ? 8   DG  T C8    1 
ATOM   6611 N  N7    . DG  C 3 8   ? 37.392  2.949   18.458  1.00 57.45  ? 8   DG  T N7    1 
ATOM   6612 C  C5    . DG  C 3 8   ? 36.124  3.318   18.884  1.00 62.15  ? 8   DG  T C5    1 
ATOM   6613 C  C6    . DG  C 3 8   ? 35.003  3.748   18.137  1.00 66.27  ? 8   DG  T C6    1 
ATOM   6614 O  O6    . DG  C 3 8   ? 34.908  3.893   16.909  1.00 67.34  ? 8   DG  T O6    1 
ATOM   6615 N  N1    . DG  C 3 8   ? 33.913  4.023   18.958  1.00 72.55  ? 8   DG  T N1    1 
ATOM   6616 C  C2    . DG  C 3 8   ? 33.907  3.898   20.328  1.00 69.00  ? 8   DG  T C2    1 
ATOM   6617 N  N2    . DG  C 3 8   ? 32.759  4.210   20.949  1.00 71.85  ? 8   DG  T N2    1 
ATOM   6618 N  N3    . DG  C 3 8   ? 34.951  3.495   21.041  1.00 64.29  ? 8   DG  T N3    1 
ATOM   6619 C  C4    . DG  C 3 8   ? 36.021  3.223   20.254  1.00 65.51  ? 8   DG  T C4    1 
ATOM   6620 P  P     . DC  C 3 9   ? 38.538  -0.007  25.361  1.00 72.80  ? 9   DC  T P     1 
ATOM   6621 O  OP1   . DC  C 3 9   ? 38.610  0.223   26.822  1.00 78.78  ? 9   DC  T OP1   1 
ATOM   6622 O  OP2   . DC  C 3 9   ? 39.452  -0.975  24.716  1.00 74.54  ? 9   DC  T OP2   1 
ATOM   6623 O  "O5'" . DC  C 3 9   ? 37.042  -0.414  24.978  1.00 77.50  ? 9   DC  T "O5'" 1 
ATOM   6624 C  "C5'" . DC  C 3 9   ? 35.966  0.433   25.349  1.00 67.75  ? 9   DC  T "C5'" 1 
ATOM   6625 C  "C4'" . DC  C 3 9   ? 34.709  0.081   24.575  1.00 76.90  ? 9   DC  T "C4'" 1 
ATOM   6626 O  "O4'" . DC  C 3 9   ? 34.809  0.577   23.231  1.00 77.74  ? 9   DC  T "O4'" 1 
ATOM   6627 C  "C3'" . DC  C 3 9   ? 34.435  -1.414  24.429  1.00 74.82  ? 9   DC  T "C3'" 1 
ATOM   6628 O  "O3'" . DC  C 3 9   ? 33.451  -1.818  25.372  1.00 63.10  ? 9   DC  T "O3'" 1 
ATOM   6629 C  "C2'" . DC  C 3 9   ? 33.938  -1.577  22.976  1.00 70.88  ? 9   DC  T "C2'" 1 
ATOM   6630 C  "C1'" . DC  C 3 9   ? 33.904  -0.144  22.444  1.00 60.27  ? 9   DC  T "C1'" 1 
ATOM   6631 N  N1    . DC  C 3 9   ? 34.313  -0.020  21.015  1.00 59.24  ? 9   DC  T N1    1 
ATOM   6632 C  C2    . DC  C 3 9   ? 33.377  0.399   20.063  1.00 72.08  ? 9   DC  T C2    1 
ATOM   6633 O  O2    . DC  C 3 9   ? 32.223  0.657   20.425  1.00 76.94  ? 9   DC  T O2    1 
ATOM   6634 N  N3    . DC  C 3 9   ? 33.763  0.510   18.767  1.00 65.78  ? 9   DC  T N3    1 
ATOM   6635 C  C4    . DC  C 3 9   ? 35.017  0.221   18.417  1.00 64.17  ? 9   DC  T C4    1 
ATOM   6636 N  N4    . DC  C 3 9   ? 35.351  0.346   17.128  1.00 69.79  ? 9   DC  T N4    1 
ATOM   6637 C  C5    . DC  C 3 9   ? 35.985  -0.207  19.374  1.00 64.76  ? 9   DC  T C5    1 
ATOM   6638 C  C6    . DC  C 3 9   ? 35.593  -0.312  20.648  1.00 67.86  ? 9   DC  T C6    1 
ATOM   6639 P  P     . DC  C 3 10  ? 32.996  -3.357  25.462  1.00 68.95  ? 10  DC  T P     1 
ATOM   6640 O  OP1   . DC  C 3 10  ? 32.563  -3.614  26.853  1.00 71.10  ? 10  DC  T OP1   1 
ATOM   6641 O  OP2   . DC  C 3 10  ? 34.057  -4.191  24.855  1.00 79.37  ? 10  DC  T OP2   1 
ATOM   6642 O  "O5'" . DC  C 3 10  ? 31.714  -3.426  24.515  1.00 76.03  ? 10  DC  T "O5'" 1 
ATOM   6643 C  "C5'" . DC  C 3 10  ? 30.577  -2.624  24.805  1.00 75.75  ? 10  DC  T "C5'" 1 
ATOM   6644 C  "C4'" . DC  C 3 10  ? 29.387  -3.032  23.954  1.00 81.58  ? 10  DC  T "C4'" 1 
ATOM   6645 O  "O4'" . DC  C 3 10  ? 29.600  -2.619  22.580  1.00 73.17  ? 10  DC  T "O4'" 1 
ATOM   6646 C  "C3'" . DC  C 3 10  ? 29.112  -4.529  23.893  1.00 81.10  ? 10  DC  T "C3'" 1 
ATOM   6647 O  "O3'" . DC  C 3 10  ? 27.728  -4.744  23.720  1.00 84.36  ? 10  DC  T "O3'" 1 
ATOM   6648 C  "C2'" . DC  C 3 10  ? 29.890  -4.951  22.653  1.00 69.06  ? 10  DC  T "C2'" 1 
ATOM   6649 C  "C1'" . DC  C 3 10  ? 29.652  -3.755  21.740  1.00 73.16  ? 10  DC  T "C1'" 1 
ATOM   6650 N  N1    . DC  C 3 10  ? 30.730  -3.543  20.738  1.00 83.20  ? 10  DC  T N1    1 
ATOM   6651 C  C2    . DC  C 3 10  ? 30.411  -3.007  19.486  1.00 80.37  ? 10  DC  T C2    1 
ATOM   6652 O  O2    . DC  C 3 10  ? 29.233  -2.723  19.236  1.00 80.65  ? 10  DC  T O2    1 
ATOM   6653 N  N3    . DC  C 3 10  ? 31.403  -2.814  18.583  1.00 77.39  ? 10  DC  T N3    1 
ATOM   6654 C  C4    . DC  C 3 10  ? 32.661  -3.134  18.894  1.00 74.53  ? 10  DC  T C4    1 
ATOM   6655 N  N4    . DC  C 3 10  ? 33.605  -2.926  17.969  1.00 74.15  ? 10  DC  T N4    1 
ATOM   6656 C  C5    . DC  C 3 10  ? 33.006  -3.680  20.165  1.00 65.45  ? 10  DC  T C5    1 
ATOM   6657 C  C6    . DC  C 3 10  ? 32.019  -3.866  21.048  1.00 77.94  ? 10  DC  T C6    1 
ATOM   6658 P  P     . DG  C 3 11  ? 27.023  -6.045  24.340  1.00 75.55  ? 11  DG  T P     1 
ATOM   6659 O  OP1   . DG  C 3 11  ? 26.491  -5.653  25.664  1.00 85.58  ? 11  DG  T OP1   1 
ATOM   6660 O  OP2   . DG  C 3 11  ? 27.965  -7.182  24.228  1.00 80.07  ? 11  DG  T OP2   1 
ATOM   6661 O  "O5'" . DG  C 3 11  ? 25.804  -6.316  23.342  1.00 92.37  ? 11  DG  T "O5'" 1 
ATOM   6662 C  "C5'" . DG  C 3 11  ? 24.950  -5.244  22.962  1.00 75.22  ? 11  DG  T "C5'" 1 
ATOM   6663 C  "C4'" . DG  C 3 11  ? 24.578  -5.338  21.492  1.00 74.65  ? 11  DG  T "C4'" 1 
ATOM   6664 O  "O4'" . DG  C 3 11  ? 25.754  -5.108  20.672  1.00 78.27  ? 11  DG  T "O4'" 1 
ATOM   6665 C  "C3'" . DG  C 3 11  ? 24.006  -6.683  21.051  1.00 86.54  ? 11  DG  T "C3'" 1 
ATOM   6666 O  "O3'" . DG  C 3 11  ? 22.930  -6.475  20.150  1.00 76.62  ? 11  DG  T "O3'" 1 
ATOM   6667 C  "C2'" . DG  C 3 11  ? 25.192  -7.361  20.365  1.00 87.28  ? 11  DG  T "C2'" 1 
ATOM   6668 C  "C1'" . DG  C 3 11  ? 25.922  -6.172  19.761  1.00 82.47  ? 11  DG  T "C1'" 1 
ATOM   6669 N  N9    . DG  C 3 11  ? 27.353  -6.399  19.587  1.00 86.86  ? 11  DG  T N9    1 
ATOM   6670 C  C8    . DG  C 3 11  ? 28.223  -6.919  20.513  1.00 79.90  ? 11  DG  T C8    1 
ATOM   6671 N  N7    . DG  C 3 11  ? 29.451  -7.002  20.085  1.00 89.51  ? 11  DG  T N7    1 
ATOM   6672 C  C5    . DG  C 3 11  ? 29.395  -6.504  18.789  1.00 89.51  ? 11  DG  T C5    1 
ATOM   6673 C  C6    . DG  C 3 11  ? 30.421  -6.347  17.828  1.00 83.24  ? 11  DG  T C6    1 
ATOM   6674 O  O6    . DG  C 3 11  ? 31.623  -6.627  17.936  1.00 88.99  ? 11  DG  T O6    1 
ATOM   6675 N  N1    . DG  C 3 11  ? 29.936  -5.805  16.640  1.00 78.65  ? 11  DG  T N1    1 
ATOM   6676 C  C2    . DG  C 3 11  ? 28.626  -5.459  16.411  1.00 81.06  ? 11  DG  T C2    1 
ATOM   6677 N  N2    . DG  C 3 11  ? 28.350  -4.950  15.202  1.00 76.48  ? 11  DG  T N2    1 
ATOM   6678 N  N3    . DG  C 3 11  ? 27.653  -5.600  17.304  1.00 89.00  ? 11  DG  T N3    1 
ATOM   6679 C  C4    . DG  C 3 11  ? 28.109  -6.127  18.467  1.00 86.25  ? 11  DG  T C4    1 
ATOM   6680 P  P     . DT  C 3 12  ? 22.005  -7.705  19.692  1.00 79.04  ? 12  DT  T P     1 
ATOM   6681 O  OP1   . DT  C 3 12  ? 20.601  -7.235  19.683  1.00 85.31  ? 12  DT  T OP1   1 
ATOM   6682 O  OP2   . DT  C 3 12  ? 22.373  -8.879  20.515  1.00 77.49  ? 12  DT  T OP2   1 
ATOM   6683 O  "O5'" . DT  C 3 12  ? 22.478  -7.987  18.190  1.00 82.55  ? 12  DT  T "O5'" 1 
ATOM   6684 C  "C5'" . DT  C 3 12  ? 22.981  -6.919  17.389  1.00 86.83  ? 12  DT  T "C5'" 1 
ATOM   6685 C  "C4'" . DT  C 3 12  ? 23.460  -7.437  16.045  1.00 87.71  ? 12  DT  T "C4'" 1 
ATOM   6686 O  "O4'" . DT  C 3 12  ? 24.913  -7.445  16.014  1.00 80.31  ? 12  DT  T "O4'" 1 
ATOM   6687 C  "C3'" . DT  C 3 12  ? 23.019  -8.866  15.719  1.00 86.03  ? 12  DT  T "C3'" 1 
ATOM   6688 O  "O3'" . DT  C 3 12  ? 22.581  -8.955  14.368  1.00 91.98  ? 12  DT  T "O3'" 1 
ATOM   6689 C  "C2'" . DT  C 3 12  ? 24.286  -9.685  15.950  1.00 89.08  ? 12  DT  T "C2'" 1 
ATOM   6690 C  "C1'" . DT  C 3 12  ? 25.359  -8.692  15.542  1.00 84.83  ? 12  DT  T "C1'" 1 
ATOM   6691 N  N1    . DT  C 3 12  ? 26.691  -8.983  16.138  1.00 87.95  ? 12  DT  T N1    1 
ATOM   6692 C  C2    . DT  C 3 12  ? 27.823  -8.794  15.381  1.00 85.84  ? 12  DT  T C2    1 
ATOM   6693 O  O2    . DT  C 3 12  ? 27.798  -8.386  14.233  1.00 74.23  ? 12  DT  T O2    1 
ATOM   6694 N  N3    . DT  C 3 12  ? 28.995  -9.094  16.020  1.00 82.48  ? 12  DT  T N3    1 
ATOM   6695 C  C4    . DT  C 3 12  ? 29.146  -9.560  17.314  1.00 87.88  ? 12  DT  T C4    1 
ATOM   6696 O  O4    . DT  C 3 12  ? 30.247  -9.803  17.800  1.00 93.95  ? 12  DT  T O4    1 
ATOM   6697 C  C5    . DT  C 3 12  ? 27.918  -9.742  18.052  1.00 87.53  ? 12  DT  T C5    1 
ATOM   6698 C  C7    . DT  C 3 12  ? 27.955  -10.243 19.465  1.00 83.84  ? 12  DT  T C7    1 
ATOM   6699 C  C6    . DT  C 3 12  ? 26.763  -9.449  17.435  1.00 84.00  ? 12  DT  T C6    1 
ATOM   6700 P  P     . DG  C 3 13  ? 21.546  -10.108 13.935  1.00 107.00 ? 13  DG  T P     1 
ATOM   6701 O  OP1   . DG  C 3 13  ? 20.284  -9.456  13.519  1.00 103.96 ? 13  DG  T OP1   1 
ATOM   6702 O  OP2   . DG  C 3 13  ? 21.552  -11.139 14.996  1.00 87.98  ? 13  DG  T OP2   1 
ATOM   6703 O  "O5'" . DG  C 3 13  ? 22.226  -10.784 12.659  1.00 97.03  ? 13  DG  T "O5'" 1 
ATOM   6704 C  "C5'" . DG  C 3 13  ? 22.337  -10.064 11.442  1.00 86.62  ? 13  DG  T "C5'" 1 
ATOM   6705 C  "C4'" . DG  C 3 13  ? 23.576  -10.503 10.689  1.00 91.97  ? 13  DG  T "C4'" 1 
ATOM   6706 O  "O4'" . DG  C 3 13  ? 24.730  -10.241 11.514  1.00 91.67  ? 13  DG  T "O4'" 1 
ATOM   6707 C  "C3'" . DG  C 3 13  ? 23.625  -11.991 10.364  1.00 98.24  ? 13  DG  T "C3'" 1 
ATOM   6708 O  "O3'" . DG  C 3 13  ? 23.090  -12.241 9.039   1.00 113.99 ? 13  DG  T "O3'" 1 
ATOM   6709 C  "C2'" . DG  C 3 13  ? 25.106  -12.343 10.458  1.00 97.93  ? 13  DG  T "C2'" 1 
ATOM   6710 C  "C1'" . DG  C 3 13  ? 25.689  -11.266 11.370  1.00 94.52  ? 13  DG  T "C1'" 1 
ATOM   6711 N  N9    . DG  C 3 13  ? 26.054  -11.756 12.695  1.00 90.03  ? 13  DG  T N9    1 
ATOM   6712 C  C8    . DG  C 3 13  ? 25.205  -12.128 13.709  1.00 91.23  ? 13  DG  T C8    1 
ATOM   6713 N  N7    . DG  C 3 13  ? 25.826  -12.525 14.786  1.00 88.53  ? 13  DG  T N7    1 
ATOM   6714 C  C5    . DG  C 3 13  ? 27.173  -12.408 14.464  1.00 94.65  ? 13  DG  T C5    1 
ATOM   6715 C  C6    . DG  C 3 13  ? 28.324  -12.693 15.235  1.00 94.32  ? 13  DG  T C6    1 
ATOM   6716 O  O6    . DG  C 3 13  ? 28.386  -13.120 16.396  1.00 91.21  ? 13  DG  T O6    1 
ATOM   6717 N  N1    . DG  C 3 13  ? 29.495  -12.433 14.524  1.00 84.18  ? 13  DG  T N1    1 
ATOM   6718 C  C2    . DG  C 3 13  ? 29.544  -11.959 13.234  1.00 85.60  ? 13  DG  T C2    1 
ATOM   6719 N  N2    . DG  C 3 13  ? 30.763  -11.770 12.712  1.00 84.51  ? 13  DG  T N2    1 
ATOM   6720 N  N3    . DG  C 3 13  ? 28.473  -11.689 12.504  1.00 82.06  ? 13  DG  T N3    1 
ATOM   6721 C  C4    . DG  C 3 13  ? 27.327  -11.936 13.180  1.00 91.23  ? 13  DG  T C4    1 
ATOM   6722 P  P     . DG  C 3 14  ? 23.959  -11.987 7.701   1.00 101.08 ? 14  DG  T P     1 
ATOM   6723 O  OP1   . DG  C 3 14  ? 24.727  -10.729 7.822   1.00 105.20 ? 14  DG  T OP1   1 
ATOM   6724 O  OP2   . DG  C 3 14  ? 23.024  -12.129 6.566   1.00 115.82 ? 14  DG  T OP2   1 
ATOM   6725 O  "O5'" . DG  C 3 14  ? 24.963  -13.232 7.624   1.00 100.82 ? 14  DG  T "O5'" 1 
ATOM   6726 C  "C5'" . DG  C 3 14  ? 25.731  -13.454 6.447   1.00 104.82 ? 14  DG  T "C5'" 1 
ATOM   6727 C  "C4'" . DG  C 3 14  ? 27.220  -13.362 6.734   1.00 96.71  ? 14  DG  T "C4'" 1 
ATOM   6728 O  "O4'" . DG  C 3 14  ? 27.446  -13.297 8.167   1.00 88.00  ? 14  DG  T "O4'" 1 
ATOM   6729 C  "C3'" . DG  C 3 14  ? 28.039  -14.547 6.221   1.00 107.25 ? 14  DG  T "C3'" 1 
ATOM   6730 O  "O3'" . DG  C 3 14  ? 29.143  -14.093 5.460   1.00 103.83 ? 14  DG  T "O3'" 1 
ATOM   6731 C  "C2'" . DG  C 3 14  ? 28.487  -15.270 7.490   1.00 104.44 ? 14  DG  T "C2'" 1 
ATOM   6732 C  "C1'" . DG  C 3 14  ? 28.513  -14.149 8.511   1.00 82.97  ? 14  DG  T "C1'" 1 
ATOM   6733 N  N9    . DG  C 3 14  ? 28.313  -14.609 9.885   1.00 85.94  ? 14  DG  T N9    1 
ATOM   6734 C  C8    . DG  C 3 14  ? 27.113  -14.856 10.505  1.00 93.46  ? 14  DG  T C8    1 
ATOM   6735 N  N7    . DG  C 3 14  ? 27.234  -15.251 11.740  1.00 98.93  ? 14  DG  T N7    1 
ATOM   6736 C  C5    . DG  C 3 14  ? 28.604  -15.279 11.955  1.00 91.57  ? 14  DG  T C5    1 
ATOM   6737 C  C6    . DG  C 3 14  ? 29.336  -15.635 13.112  1.00 96.58  ? 14  DG  T C6    1 
ATOM   6738 O  O6    . DG  C 3 14  ? 28.901  -16.009 14.211  1.00 101.77 ? 14  DG  T O6    1 
ATOM   6739 N  N1    . DG  C 3 14  ? 30.708  -15.525 12.907  1.00 100.46 ? 14  DG  T N1    1 
ATOM   6740 C  C2    . DG  C 3 14  ? 31.299  -15.122 11.732  1.00 97.52  ? 14  DG  T C2    1 
ATOM   6741 N  N2    . DG  C 3 14  ? 32.639  -15.078 11.726  1.00 103.47 ? 14  DG  T N2    1 
ATOM   6742 N  N3    . DG  C 3 14  ? 30.624  -14.785 10.639  1.00 90.60  ? 14  DG  T N3    1 
ATOM   6743 C  C4    . DG  C 3 14  ? 29.285  -14.887 10.823  1.00 92.61  ? 14  DG  T C4    1 
ATOM   6744 P  P     . DT  C 3 15  ? 29.644  -14.951 4.198   1.00 114.49 ? 15  DT  T P     1 
ATOM   6745 O  OP1   . DT  C 3 15  ? 30.322  -14.026 3.264   1.00 117.07 ? 15  DT  T OP1   1 
ATOM   6746 O  OP2   . DT  C 3 15  ? 28.504  -15.776 3.739   1.00 99.70  ? 15  DT  T OP2   1 
ATOM   6747 O  "O5'" . DT  C 3 15  ? 30.710  -15.965 4.821   1.00 100.41 ? 15  DT  T "O5'" 1 
ATOM   6748 C  "C5'" . DT  C 3 15  ? 31.647  -15.515 5.786   1.00 95.59  ? 15  DT  T "C5'" 1 
ATOM   6749 C  "C4'" . DT  C 3 15  ? 32.392  -16.691 6.385   1.00 89.39  ? 15  DT  T "C4'" 1 
ATOM   6750 O  "O4'" . DT  C 3 15  ? 32.228  -16.683 7.820   1.00 100.62 ? 15  DT  T "O4'" 1 
ATOM   6751 C  "C3'" . DT  C 3 15  ? 31.885  -18.051 5.947   1.00 95.91  ? 15  DT  T "C3'" 1 
ATOM   6752 O  "O3'" . DT  C 3 15  ? 32.481  -18.441 4.686   1.00 115.89 ? 15  DT  T "O3'" 1 
ATOM   6753 C  "C2'" . DT  C 3 15  ? 32.297  -18.957 7.108   1.00 102.14 ? 15  DT  T "C2'" 1 
ATOM   6754 C  "C1'" . DT  C 3 15  ? 32.241  -18.010 8.314   1.00 95.11  ? 15  DT  T "C1'" 1 
ATOM   6755 N  N1    . DT  C 3 15  ? 31.043  -18.203 9.198   1.00 100.80 ? 15  DT  T N1    1 
ATOM   6756 C  C2    . DT  C 3 15  ? 31.231  -18.381 10.548  1.00 103.51 ? 15  DT  T C2    1 
ATOM   6757 O  O2    . DT  C 3 15  ? 32.331  -18.400 11.070  1.00 120.87 ? 15  DT  T O2    1 
ATOM   6758 N  N3    . DT  C 3 15  ? 30.079  -18.539 11.272  1.00 102.35 ? 15  DT  T N3    1 
ATOM   6759 C  C4    . DT  C 3 15  ? 28.783  -18.533 10.793  1.00 97.18  ? 15  DT  T C4    1 
ATOM   6760 O  O4    . DT  C 3 15  ? 27.810  -18.683 11.526  1.00 94.26  ? 15  DT  T O4    1 
ATOM   6761 C  C5    . DT  C 3 15  ? 28.653  -18.340 9.369   1.00 99.22  ? 15  DT  T C5    1 
ATOM   6762 C  C7    . DT  C 3 15  ? 27.294  -18.320 8.735   1.00 100.70 ? 15  DT  T C7    1 
ATOM   6763 C  C6    . DT  C 3 15  ? 29.776  -18.186 8.648   1.00 96.57  ? 15  DT  T C6    1 
ATOM   6764 P  P     . DC  C 3 16  ? 34.012  -18.934 4.566   1.00 90.80  ? 16  DC  T P     1 
ATOM   6765 O  OP1   . DC  C 3 16  ? 34.902  -18.124 5.426   1.00 98.87  ? 16  DC  T OP1   1 
ATOM   6766 O  OP2   . DC  C 3 16  ? 34.295  -19.002 3.117   1.00 88.36  ? 16  DC  T OP2   1 
ATOM   6767 O  "O5'" . DC  C 3 16  ? 33.989  -20.440 5.100   1.00 87.33  ? 16  DC  T "O5'" 1 
ATOM   6768 C  "C5'" . DC  C 3 16  ? 35.186  -21.203 5.111   1.00 95.26  ? 16  DC  T "C5'" 1 
ATOM   6769 C  "C4'" . DC  C 3 16  ? 35.436  -21.795 6.486   1.00 100.81 ? 16  DC  T "C4'" 1 
ATOM   6770 O  "O4'" . DC  C 3 16  ? 34.357  -21.417 7.384   1.00 92.35  ? 16  DC  T "O4'" 1 
ATOM   6771 C  "C3'" . DC  C 3 16  ? 35.499  -23.318 6.524   1.00 97.87  ? 16  DC  T "C3'" 1 
ATOM   6772 O  "O3'" . DC  C 3 16  ? 36.455  -23.744 7.485   1.00 111.89 ? 16  DC  T "O3'" 1 
ATOM   6773 C  "C2'" . DC  C 3 16  ? 34.083  -23.700 6.938   1.00 92.14  ? 16  DC  T "C2'" 1 
ATOM   6774 C  "C1'" . DC  C 3 16  ? 33.735  -22.575 7.899   1.00 98.54  ? 16  DC  T "C1'" 1 
ATOM   6775 N  N1    . DC  C 3 16  ? 32.268  -22.316 8.008   1.00 103.89 ? 16  DC  T N1    1 
ATOM   6776 C  C2    . DC  C 3 16  ? 31.691  -22.112 9.267   1.00 104.55 ? 16  DC  T C2    1 
ATOM   6777 O  O2    . DC  C 3 16  ? 32.411  -22.150 10.272  1.00 114.92 ? 16  DC  T O2    1 
ATOM   6778 N  N3    . DC  C 3 16  ? 30.358  -21.877 9.349   1.00 102.78 ? 16  DC  T N3    1 
ATOM   6779 C  C4    . DC  C 3 16  ? 29.616  -21.843 8.241   1.00 98.67  ? 16  DC  T C4    1 
ATOM   6780 N  N4    . DC  C 3 16  ? 28.306  -21.607 8.372   1.00 86.77  ? 16  DC  T N4    1 
ATOM   6781 C  C5    . DC  C 3 16  ? 30.184  -22.049 6.949   1.00 103.84 ? 16  DC  T C5    1 
ATOM   6782 C  C6    . DC  C 3 16  ? 31.500  -22.283 6.880   1.00 101.79 ? 16  DC  T C6    1 
HETATM 6783 MG MG    . MG  D 4 .   ? 42.980  26.125  25.742  1.00 83.14  ? 801 MG  A MG    1 
HETATM 6784 MG MG    . MG  E 4 .   ? 46.993  22.611  22.228  1.00 60.91  ? 802 MG  A MG    1 
HETATM 6785 MG MG    . MG  F 4 .   ? 45.404  20.567  24.387  1.00 73.52  ? 803 MG  A MG    1 
HETATM 6786 N  N1    . XG4 G 5 .   ? 37.853  20.798  15.244  1.00 52.50  ? 804 XG4 A N1    1 
HETATM 6787 C  C2    . XG4 G 5 .   ? 39.005  20.752  14.376  1.00 50.18  ? 804 XG4 A C2    1 
HETATM 6788 N  N2    . XG4 G 5 .   ? 38.904  20.870  12.930  1.00 59.14  ? 804 XG4 A N2    1 
HETATM 6789 N  N3    . XG4 G 5 .   ? 40.322  20.580  14.962  1.00 52.27  ? 804 XG4 A N3    1 
HETATM 6790 C  C4    . XG4 G 5 .   ? 40.486  20.453  16.433  1.00 51.98  ? 804 XG4 A C4    1 
HETATM 6791 C  C5    . XG4 G 5 .   ? 39.419  20.494  17.274  1.00 51.57  ? 804 XG4 A C5    1 
HETATM 6792 C  C6    . XG4 G 5 .   ? 38.017  20.675  16.667  1.00 51.27  ? 804 XG4 A C6    1 
HETATM 6793 O  O6    . XG4 G 5 .   ? 37.064  20.715  17.371  1.00 63.53  ? 804 XG4 A O6    1 
HETATM 6794 N  N7    . XG4 G 5 .   ? 39.885  20.355  18.520  1.00 53.28  ? 804 XG4 A N7    1 
HETATM 6795 C  C8    . XG4 G 5 .   ? 41.234  20.226  18.465  1.00 58.12  ? 804 XG4 A C8    1 
HETATM 6796 N  N9    . XG4 G 5 .   ? 41.569  20.287  17.158  1.00 60.59  ? 804 XG4 A N9    1 
HETATM 6797 P  PA    . XG4 G 5 .   ? 43.481  22.434  21.920  1.00 94.22  ? 804 XG4 A PA    1 
HETATM 6798 P  PB    . XG4 G 5 .   ? 44.753  24.669  23.441  1.00 88.99  ? 804 XG4 A PB    1 
HETATM 6799 P  PG    . XG4 G 5 .   ? 46.249  23.991  25.740  1.00 104.73 ? 804 XG4 A PG    1 
HETATM 6800 C  "C1'" . XG4 G 5 .   ? 43.011  20.153  17.195  1.00 56.83  ? 804 XG4 A "C1'" 1 
HETATM 6801 O  O1A   . XG4 G 5 .   ? 44.069  21.408  22.856  1.00 88.91  ? 804 XG4 A O1A   1 
HETATM 6802 O  O1B   . XG4 G 5 .   ? 43.637  24.439  24.419  1.00 96.93  ? 804 XG4 A O1B   1 
HETATM 6803 O  O1G   . XG4 G 5 .   ? 45.530  25.170  26.349  1.00 109.62 ? 804 XG4 A O1G   1 
HETATM 6804 C  "C2'" . XG4 G 5 .   ? 43.628  21.592  16.780  1.00 48.86  ? 804 XG4 A "C2'" 1 
HETATM 6805 O  O2A   . XG4 G 5 .   ? 42.026  22.550  22.305  1.00 75.75  ? 804 XG4 A O2A   1 
HETATM 6806 O  O2B   . XG4 G 5 .   ? 44.917  26.161  23.241  1.00 82.35  ? 804 XG4 A O2B   1 
HETATM 6807 O  O2G   . XG4 G 5 .   ? 47.698  24.019  26.160  1.00 79.31  ? 804 XG4 A O2G   1 
HETATM 6808 C  "C3'" . XG4 G 5 .   ? 44.015  22.119  17.884  1.00 52.68  ? 804 XG4 A "C3'" 1 
HETATM 6809 O  "O3'" . XG4 G 5 .   ? 45.070  23.160  17.621  1.00 52.79  ? 804 XG4 A "O3'" 1 
HETATM 6810 N  N3A   . XG4 G 5 .   ? 44.343  23.908  21.973  1.00 67.97  ? 804 XG4 A N3A   1 
HETATM 6811 O  O3B   . XG4 G 5 .   ? 46.108  24.016  24.101  1.00 97.15  ? 804 XG4 A O3B   1 
HETATM 6812 O  O3G   . XG4 G 5 .   ? 45.571  22.718  26.179  1.00 87.90  ? 804 XG4 A O3G   1 
HETATM 6813 C  "C4'" . XG4 G 5 .   ? 44.566  20.888  18.626  1.00 57.04  ? 804 XG4 A "C4'" 1 
HETATM 6814 O  "O4'" . XG4 G 5 .   ? 43.480  19.847  18.364  1.00 56.60  ? 804 XG4 A "O4'" 1 
HETATM 6815 C  "C5'" . XG4 G 5 .   ? 44.634  21.126  20.006  1.00 65.02  ? 804 XG4 A "C5'" 1 
HETATM 6816 O  "O5'" . XG4 G 5 .   ? 43.570  21.949  20.358  1.00 70.69  ? 804 XG4 A "O5'" 1 
HETATM 6817 MG MG    . MG  H 4 .   ? 17.933  36.814  9.996   1.00 70.82  ? 805 MG  A MG    1 
HETATM 6818 MG MG    . MG  I 4 .   ? 31.870  32.594  -4.321  1.00 72.33  ? 806 MG  A MG    1 
HETATM 6819 MN MN    . MN  J 6 .   ? 35.184  15.234  5.915   1.00 75.56  ? 807 MN  A MN    1 
HETATM 6820 N  N1    . IMD K 7 .   ? 43.973  17.260  31.770  1.00 90.75  ? 808 IMD A N1    1 
HETATM 6821 C  C2    . IMD K 7 .   ? 43.015  16.556  31.194  1.00 96.08  ? 808 IMD A C2    1 
HETATM 6822 N  N3    . IMD K 7 .   ? 43.191  16.642  29.887  1.00 89.19  ? 808 IMD A N3    1 
HETATM 6823 C  C4    . IMD K 7 .   ? 44.287  17.417  29.615  1.00 87.21  ? 808 IMD A C4    1 
HETATM 6824 C  C5    . IMD K 7 .   ? 44.784  17.810  30.813  1.00 81.86  ? 808 IMD A C5    1 
HETATM 6825 C  C1    . GOL L 8 .   ? 34.467  2.438   11.823  1.00 99.29  ? 101 GOL P C1    1 
HETATM 6826 O  O1    . GOL L 8 .   ? 33.217  2.006   12.309  1.00 92.52  ? 101 GOL P O1    1 
HETATM 6827 C  C2    . GOL L 8 .   ? 35.573  1.854   12.677  1.00 97.38  ? 101 GOL P C2    1 
HETATM 6828 O  O2    . GOL L 8 .   ? 35.683  2.618   13.859  1.00 79.15  ? 101 GOL P O2    1 
HETATM 6829 C  C3    . GOL L 8 .   ? 35.281  0.393   12.985  1.00 81.38  ? 101 GOL P C3    1 
HETATM 6830 O  O3    . GOL L 8 .   ? 34.826  -0.216  11.795  1.00 81.40  ? 101 GOL P O3    1 
HETATM 6831 C  C1    . GOL M 8 .   ? 25.402  -13.959 18.014  1.00 92.52  ? 101 GOL T C1    1 
HETATM 6832 O  O1    . GOL M 8 .   ? 25.853  -12.783 17.384  1.00 94.25  ? 101 GOL T O1    1 
HETATM 6833 C  C2    . GOL M 8 .   ? 24.939  -14.948 16.964  1.00 92.26  ? 101 GOL T C2    1 
HETATM 6834 O  O2    . GOL M 8 .   ? 25.872  -14.955 15.907  1.00 102.56 ? 101 GOL T O2    1 
HETATM 6835 C  C3    . GOL M 8 .   ? 23.547  -14.587 16.471  1.00 98.40  ? 101 GOL T C3    1 
HETATM 6836 O  O3    . GOL M 8 .   ? 23.567  -13.230 16.086  1.00 104.56 ? 101 GOL T O3    1 
HETATM 6837 O  O     . HOH N 9 .   ? 44.123  24.789  19.870  1.00 66.70  ? 901 HOH A O     1 
HETATM 6838 O  O     . HOH N 9 .   ? 8.520   27.155  24.964  1.00 69.77  ? 902 HOH A O     1 
HETATM 6839 O  O     . HOH N 9 .   ? 21.117  39.826  16.707  1.00 57.45  ? 903 HOH A O     1 
HETATM 6840 O  O     . HOH N 9 .   ? 42.946  20.989  25.078  1.00 88.51  ? 904 HOH A O     1 
HETATM 6841 O  O     . HOH N 9 .   ? 40.968  -1.900  27.630  1.00 70.94  ? 905 HOH A O     1 
HETATM 6842 O  O     . HOH N 9 .   ? 50.066  15.803  16.664  1.00 48.22  ? 906 HOH A O     1 
HETATM 6843 O  O     . HOH N 9 .   ? 43.615  12.121  24.970  1.00 67.22  ? 907 HOH A O     1 
HETATM 6844 O  O     . HOH N 9 .   ? 34.984  6.849   24.627  1.00 55.70  ? 908 HOH A O     1 
HETATM 6845 O  O     . HOH O 9 .   ? 37.621  6.303   13.095  1.00 66.41  ? 201 HOH T O     1 
HETATM 6846 O  O     . HOH O 9 .   ? 34.722  14.446  9.642   1.00 60.00  ? 202 HOH T O     1 
HETATM 6847 O  O     . HOH O 9 .   ? 32.140  -12.839 8.730   1.00 82.22  ? 203 HOH T O     1 
HETATM 6848 O  O     . HOH O 9 .   ? 36.622  -4.027  18.167  1.00 53.58  ? 204 HOH T O     1 
HETATM 6849 O  O     . HOH O 9 .   ? 32.649  2.660   24.525  1.00 67.45  ? 205 HOH T O     1 
HETATM 6850 O  O     . HOH O 9 .   ? 35.207  8.131   11.963  1.00 67.58  ? 206 HOH T O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N     . MET A 1   ? 1.0810 0.9046 0.9992 0.0528  -0.0045 -0.0576 1   MET A N     
2    C  CA    . MET A 1   ? 1.0234 0.8692 0.9402 0.0459  -0.0070 -0.0548 1   MET A CA    
3    C  C     . MET A 1   ? 0.9083 0.7872 0.8461 0.0482  0.0002  -0.0441 1   MET A C     
4    O  O     . MET A 1   ? 1.0027 0.8883 0.9437 0.0569  0.0116  -0.0426 1   MET A O     
5    C  CB    . MET A 1   ? 0.9652 0.7999 0.8535 0.0478  -0.0032 -0.0648 1   MET A CB    
6    C  CG    . MET A 1   ? 0.9773 0.8347 0.8653 0.0420  -0.0039 -0.0615 1   MET A CG    
7    S  SD    . MET A 1   ? 1.0945 0.9409 0.9508 0.0458  0.0030  -0.0705 1   MET A SD    
8    C  CE    . MET A 1   ? 0.9295 0.7589 0.7674 0.0348  -0.0141 -0.0765 1   MET A CE    
9    N  N     . ILE A 2   ? 0.9386 0.8378 0.8905 0.0404  -0.0066 -0.0363 2   ILE A N     
10   C  CA    . ILE A 2   ? 0.8837 0.8129 0.8527 0.0412  -0.0021 -0.0270 2   ILE A CA    
11   C  C     . ILE A 2   ? 0.8974 0.8383 0.8569 0.0407  0.0028  -0.0301 2   ILE A C     
12   O  O     . ILE A 2   ? 0.8755 0.8110 0.8210 0.0352  -0.0014 -0.0353 2   ILE A O     
13   C  CB    . ILE A 2   ? 0.7579 0.7023 0.7417 0.0339  -0.0103 -0.0184 2   ILE A CB    
14   C  CG1   . ILE A 2   ? 0.6455 0.5780 0.6408 0.0341  -0.0149 -0.0137 2   ILE A CG1   
15   C  CG2   . ILE A 2   ? 0.8055 0.7787 0.8025 0.0348  -0.0068 -0.0102 2   ILE A CG2   
16   C  CD1   . ILE A 2   ? 0.7765 0.7293 0.7909 0.0312  -0.0181 -0.0012 2   ILE A CD1   
17   N  N     . LEU A 3   ? 0.8513 0.8088 0.8204 0.0463  0.0114  -0.0259 3   LEU A N     
18   C  CA    . LEU A 3   ? 0.7660 0.7366 0.7309 0.0457  0.0165  -0.0269 3   LEU A CA    
19   C  C     . LEU A 3   ? 0.8398 0.8367 0.8191 0.0400  0.0127  -0.0202 3   LEU A C     
20   O  O     . LEU A 3   ? 0.8763 0.8795 0.8496 0.0344  0.0106  -0.0223 3   LEU A O     
21   C  CB    . LEU A 3   ? 0.7169 0.6883 0.6843 0.0555  0.0289  -0.0264 3   LEU A CB    
22   C  CG    . LEU A 3   ? 0.6995 0.6435 0.6504 0.0636  0.0353  -0.0338 3   LEU A CG    
23   C  CD1   . LEU A 3   ? 0.7933 0.7420 0.7475 0.0738  0.0499  -0.0319 3   LEU A CD1   
24   C  CD2   . LEU A 3   ? 0.8752 0.7984 0.7993 0.0591  0.0305  -0.0437 3   LEU A CD2   
25   N  N     . ASP A 4   ? 0.6094 0.6206 0.6062 0.0417  0.0116  -0.0121 4   ASP A N     
26   C  CA    . ASP A 4   ? 0.6748 0.7101 0.6829 0.0375  0.0081  -0.0061 4   ASP A CA    
27   C  C     . ASP A 4   ? 0.6710 0.7156 0.6940 0.0396  0.0051  0.0029  4   ASP A C     
28   O  O     . ASP A 4   ? 0.7306 0.7648 0.7585 0.0454  0.0075  0.0051  4   ASP A O     
29   C  CB    . ASP A 4   ? 0.7416 0.7914 0.7559 0.0391  0.0138  -0.0050 4   ASP A CB    
30   C  CG    . ASP A 4   ? 0.8936 0.9648 0.9156 0.0331  0.0083  -0.0014 4   ASP A CG    
31   O  OD1   . ASP A 4   ? 0.7422 0.8131 0.7566 0.0268  0.0023  -0.0038 4   ASP A OD1   
32   O  OD2   . ASP A 4   ? 1.1008 1.1885 1.1367 0.0347  0.0098  0.0038  4   ASP A OD2   
33   N  N     . THR A 5   ? 0.6707 0.7337 0.6994 0.0353  -0.0002 0.0079  5   THR A N     
34   C  CA    . THR A 5   ? 0.6439 0.7194 0.6854 0.0375  -0.0033 0.0178  5   THR A CA    
35   C  C     . THR A 5   ? 0.6650 0.7635 0.7129 0.0353  -0.0062 0.0218  5   THR A C     
36   O  O     . THR A 5   ? 0.8589 0.9625 0.8992 0.0297  -0.0084 0.0168  5   THR A O     
37   C  CB    . THR A 5   ? 0.5868 0.6589 0.6257 0.0341  -0.0086 0.0212  5   THR A CB    
38   O  OG1   . THR A 5   ? 0.5968 0.6737 0.6256 0.0276  -0.0120 0.0174  5   THR A OG1   
39   C  CG2   . THR A 5   ? 0.5360 0.5852 0.5719 0.0353  -0.0080 0.0183  5   THR A CG2   
40   N  N     . ASP A 6   ? 0.5880 0.6995 0.6503 0.0396  -0.0070 0.0310  6   ASP A N     
41   C  CA    . ASP A 6   ? 0.6252 0.7588 0.6935 0.0369  -0.0129 0.0363  6   ASP A CA    
42   C  C     . ASP A 6   ? 0.6265 0.7699 0.7058 0.0411  -0.0162 0.0482  6   ASP A C     
43   O  O     . ASP A 6   ? 0.6402 0.7725 0.7221 0.0452  -0.0138 0.0520  6   ASP A O     
44   C  CB    . ASP A 6   ? 0.6711 0.8148 0.7490 0.0370  -0.0105 0.0352  6   ASP A CB    
45   C  CG    . ASP A 6   ? 0.7087 0.8551 0.8050 0.0454  -0.0043 0.0424  6   ASP A CG    
46   O  OD1   . ASP A 6   ? 0.7955 0.9305 0.8943 0.0515  -0.0005 0.0454  6   ASP A OD1   
47   O  OD2   . ASP A 6   ? 0.7417 0.9017 0.8515 0.0461  -0.0030 0.0455  6   ASP A OD2   
48   N  N     . TYR A 7   ? 0.6044 0.7681 0.6905 0.0398  -0.0226 0.0547  7   TYR A N     
49   C  CA    . TYR A 7   ? 0.6341 0.8091 0.7309 0.0440  -0.0264 0.0676  7   TYR A CA    
50   C  C     . TYR A 7   ? 0.6310 0.8267 0.7440 0.0449  -0.0309 0.0747  7   TYR A C     
51   O  O     . TYR A 7   ? 0.5891 0.7935 0.7014 0.0397  -0.0344 0.0698  7   TYR A O     
52   C  CB    . TYR A 7   ? 0.6320 0.8114 0.7149 0.0408  -0.0328 0.0709  7   TYR A CB    
53   C  CG    . TYR A 7   ? 0.6466 0.8412 0.7191 0.0349  -0.0416 0.0690  7   TYR A CG    
54   C  CD1   . TYR A 7   ? 0.5956 0.7848 0.6523 0.0286  -0.0423 0.0572  7   TYR A CD1   
55   C  CD2   . TYR A 7   ? 0.7003 0.9135 0.7779 0.0357  -0.0498 0.0791  7   TYR A CD2   
56   C  CE1   . TYR A 7   ? 0.5951 0.7950 0.6409 0.0233  -0.0505 0.0542  7   TYR A CE1   
57   C  CE2   . TYR A 7   ? 0.6210 0.8457 0.6862 0.0300  -0.0593 0.0761  7   TYR A CE2   
58   C  CZ    . TYR A 7   ? 0.5525 0.7694 0.6015 0.0238  -0.0594 0.0630  7   TYR A CZ    
59   O  OH    . TYR A 7   ? 0.7508 0.9760 0.7861 0.0181  -0.0690 0.0588  7   TYR A OH    
60   N  N     . ILE A 8   ? 0.6502 0.8538 0.7802 0.0515  -0.0310 0.0873  8   ILE A N     
61   C  CA    . ILE A 8   ? 0.5860 0.8121 0.7343 0.0527  -0.0373 0.0976  8   ILE A CA    
62   C  C     . ILE A 8   ? 0.6396 0.8779 0.7859 0.0533  -0.0463 0.1094  8   ILE A C     
63   O  O     . ILE A 8   ? 0.7420 0.9708 0.8762 0.0541  -0.0452 0.1106  8   ILE A O     
64   C  CB    . ILE A 8   ? 0.5419 0.7688 0.7157 0.0614  -0.0286 0.1043  8   ILE A CB    
65   C  CG1   . ILE A 8   ? 0.5912 0.8052 0.7708 0.0699  -0.0223 0.1110  8   ILE A CG1   
66   C  CG2   . ILE A 8   ? 0.5926 0.8079 0.7656 0.0615  -0.0188 0.0933  8   ILE A CG2   
67   C  CD1   . ILE A 8   ? 0.6371 0.8444 0.8369 0.0797  -0.0108 0.1142  8   ILE A CD1   
68   N  N     . THR A 9   ? 0.6555 0.9159 0.8146 0.0526  -0.0556 0.1191  9   THR A N     
69   C  CA    . THR A 9   ? 0.5314 0.8058 0.6873 0.0532  -0.0655 0.1314  9   THR A CA    
70   C  C     . THR A 9   ? 0.5992 0.8858 0.7840 0.0614  -0.0651 0.1481  9   THR A C     
71   O  O     . THR A 9   ? 0.7440 1.0458 0.9498 0.0618  -0.0683 0.1531  9   THR A O     
72   C  CB    . THR A 9   ? 0.6135 0.9031 0.7556 0.0447  -0.0799 0.1287  9   THR A CB    
73   O  OG1   . THR A 9   ? 0.5829 0.8596 0.7019 0.0379  -0.0784 0.1122  9   THR A OG1   
74   C  CG2   . THR A 9   ? 0.6129 0.9127 0.7421 0.0455  -0.0893 0.1393  9   THR A CG2   
75   N  N     . GLU A 10  ? 0.6971 0.9773 0.8850 0.0681  -0.0610 0.1577  10  GLU A N     
76   C  CA    . GLU A 10  ? 0.5420 0.8322 0.7570 0.0769  -0.0602 0.1750  10  GLU A CA    
77   C  C     . GLU A 10  ? 0.5842 0.8909 0.7929 0.0764  -0.0720 0.1893  10  GLU A C     
78   O  O     . GLU A 10  ? 0.6129 0.9109 0.8071 0.0774  -0.0704 0.1921  10  GLU A O     
79   C  CB    . GLU A 10  ? 0.5522 0.8204 0.7770 0.0853  -0.0463 0.1756  10  GLU A CB    
80   C  CG    . GLU A 10  ? 0.7790 1.0539 1.0291 0.0950  -0.0450 0.1945  10  GLU A CG    
81   C  CD    . GLU A 10  ? 0.8791 1.1296 1.1413 0.1036  -0.0307 0.1927  10  GLU A CD    
82   O  OE1   . GLU A 10  ? 0.8472 1.0801 1.1037 0.1033  -0.0217 0.1777  10  GLU A OE1   
83   O  OE2   . GLU A 10  ? 1.1035 1.3515 1.3802 0.1108  -0.0286 0.2062  10  GLU A OE2   
84   N  N     . ASP A 11  ? 0.6241 0.9550 0.8439 0.0747  -0.0841 0.1989  11  ASP A N     
85   C  CA    . ASP A 11  ? 0.5966 0.9454 0.8093 0.0744  -0.0973 0.2134  11  ASP A CA    
86   C  C     . ASP A 11  ? 0.5473 0.8901 0.7216 0.0680  -0.1021 0.2049  11  ASP A C     
87   O  O     . ASP A 11  ? 0.5188 0.8617 0.6810 0.0710  -0.1029 0.2146  11  ASP A O     
88   C  CB    . ASP A 11  ? 0.5729 0.9227 0.8052 0.0846  -0.0925 0.2322  11  ASP A CB    
89   C  CG    . ASP A 11  ? 0.8178 1.1837 1.0878 0.0911  -0.0936 0.2465  11  ASP A CG    
90   O  OD1   . ASP A 11  ? 0.5894 0.9799 0.8664 0.0882  -0.1083 0.2565  11  ASP A OD1   
91   O  OD2   . ASP A 11  ? 0.8537 1.2074 1.1463 0.0992  -0.0800 0.2478  11  ASP A OD2   
92   N  N     . GLY A 12  ? 0.6054 0.9427 0.7611 0.0597  -0.1043 0.1874  12  GLY A N     
93   C  CA    . GLY A 12  ? 0.5614 0.8925 0.6808 0.0541  -0.1081 0.1779  12  GLY A CA    
94   C  C     . GLY A 12  ? 0.7486 1.0582 0.8541 0.0561  -0.0948 0.1713  12  GLY A C     
95   O  O     . GLY A 12  ? 0.7603 1.0647 0.8370 0.0527  -0.0958 0.1646  12  GLY A O     
96   N  N     . LYS A 13  ? 0.7469 1.0433 0.8722 0.0616  -0.0826 0.1729  13  LYS A N     
97   C  CA    . LYS A 13  ? 0.5658 0.8420 0.6819 0.0630  -0.0716 0.1682  13  LYS A CA    
98   C  C     . LYS A 13  ? 0.6633 0.9212 0.7819 0.0605  -0.0628 0.1516  13  LYS A C     
99   O  O     . LYS A 13  ? 0.6509 0.9079 0.7891 0.0628  -0.0595 0.1498  13  LYS A O     
100  C  CB    . LYS A 13  ? 0.6739 0.9462 0.8087 0.0711  -0.0657 0.1840  13  LYS A CB    
101  C  CG    . LYS A 13  ? 0.6471 0.9328 0.7737 0.0738  -0.0717 0.2010  13  LYS A CG    
102  C  CD    . LYS A 13  ? 1.1215 1.3976 1.2632 0.0805  -0.0636 0.2145  13  LYS A CD    
103  C  CE    . LYS A 13  ? 1.0912 1.3456 1.2240 0.0781  -0.0541 0.2049  13  LYS A CE    
104  N  NZ    . LYS A 13  ? 0.9050 1.1425 1.0613 0.0832  -0.0456 0.2106  13  LYS A NZ    
105  N  N     . PRO A 14  ? 0.7370 0.9807 0.8362 0.0565  -0.0583 0.1403  14  PRO A N     
106  C  CA    . PRO A 14  ? 0.4665 0.6935 0.5653 0.0537  -0.0513 0.1248  14  PRO A CA    
107  C  C     . PRO A 14  ? 0.5272 0.7371 0.6427 0.0590  -0.0418 0.1262  14  PRO A C     
108  O  O     . PRO A 14  ? 0.6402 0.8443 0.7607 0.0628  -0.0391 0.1357  14  PRO A O     
109  C  CB    . PRO A 14  ? 0.7023 0.9212 0.7764 0.0484  -0.0504 0.1153  14  PRO A CB    
110  C  CG    . PRO A 14  ? 0.7518 0.9842 0.8113 0.0488  -0.0567 0.1251  14  PRO A CG    
111  C  CD    . PRO A 14  ? 0.7629 1.0056 0.8401 0.0551  -0.0589 0.1424  14  PRO A CD    
112  N  N     . VAL A 15  ? 0.5508 0.7515 0.6741 0.0594  -0.0366 0.1166  15  VAL A N     
113  C  CA    . VAL A 15  ? 0.4667 0.6479 0.6019 0.0647  -0.0275 0.1149  15  VAL A CA    
114  C  C     . VAL A 15  ? 0.7047 0.8694 0.8280 0.0606  -0.0226 0.0982  15  VAL A C     
115  O  O     . VAL A 15  ? 0.7303 0.8991 0.8548 0.0594  -0.0215 0.0913  15  VAL A O     
116  C  CB    . VAL A 15  ? 0.6179 0.8049 0.7768 0.0724  -0.0244 0.1228  15  VAL A CB    
117  C  CG1   . VAL A 15  ? 0.6268 0.7906 0.7953 0.0790  -0.0150 0.1218  15  VAL A CG1   
118  C  CG2   . VAL A 15  ? 0.5503 0.7592 0.7212 0.0754  -0.0317 0.1400  15  VAL A CG2   
119  N  N     . ILE A 16  ? 0.5624 0.7089 0.6757 0.0584  -0.0200 0.0928  16  ILE A N     
120  C  CA    . ILE A 16  ? 0.5658 0.6956 0.6673 0.0546  -0.0163 0.0780  16  ILE A CA    
121  C  C     . ILE A 16  ? 0.5860 0.7007 0.6961 0.0604  -0.0089 0.0735  16  ILE A C     
122  O  O     . ILE A 16  ? 0.5461 0.6514 0.6682 0.0667  -0.0057 0.0796  16  ILE A O     
123  C  CB    . ILE A 16  ? 0.6658 0.7820 0.7571 0.0505  -0.0169 0.0754  16  ILE A CB    
124  C  CG1   . ILE A 16  ? 0.5890 0.7180 0.6666 0.0447  -0.0216 0.0754  16  ILE A CG1   
125  C  CG2   . ILE A 16  ? 0.5195 0.6138 0.6027 0.0484  -0.0132 0.0623  16  ILE A CG2   
126  C  CD1   . ILE A 16  ? 0.5465 0.6754 0.6106 0.0394  -0.0220 0.0626  16  ILE A CD1   
127  N  N     . ARG A 17  ? 0.6031 0.7146 0.7066 0.0589  -0.0055 0.0630  17  ARG A N     
128  C  CA    . ARG A 17  ? 0.6197 0.7135 0.7245 0.0644  0.0030  0.0562  17  ARG A CA    
129  C  C     . ARG A 17  ? 0.6769 0.7502 0.7625 0.0597  0.0039  0.0432  17  ARG A C     
130  O  O     . ARG A 17  ? 0.7273 0.8060 0.8013 0.0527  0.0005  0.0376  17  ARG A O     
131  C  CB    . ARG A 17  ? 0.7063 0.8128 0.8195 0.0675  0.0076  0.0561  17  ARG A CB    
132  C  CG    . ARG A 17  ? 0.6429 0.7689 0.7789 0.0735  0.0074  0.0695  17  ARG A CG    
133  C  CD    . ARG A 17  ? 0.6053 0.7541 0.7482 0.0700  0.0045  0.0712  17  ARG A CD    
134  N  NE    . ARG A 17  ? 0.7096 0.8590 0.8651 0.0767  0.0144  0.0713  17  ARG A NE    
135  C  CZ    . ARG A 17  ? 0.6561 0.8166 0.8145 0.0735  0.0156  0.0687  17  ARG A CZ    
136  N  NH1   . ARG A 17  ? 0.7001 0.8702 0.8489 0.0635  0.0070  0.0644  17  ARG A NH1   
137  N  NH2   . ARG A 17  ? 0.7393 0.9007 0.9112 0.0810  0.0265  0.0709  17  ARG A NH2   
138  N  N     . ILE A 18  ? 0.6180 0.6669 0.7000 0.0633  0.0077  0.0385  18  ILE A N     
139  C  CA    . ILE A 18  ? 0.7493 0.7770 0.8129 0.0593  0.0077  0.0262  18  ILE A CA    
140  C  C     . ILE A 18  ? 0.7749 0.7872 0.8324 0.0661  0.0168  0.0184  18  ILE A C     
141  O  O     . ILE A 18  ? 0.7907 0.7894 0.8542 0.0741  0.0220  0.0196  18  ILE A O     
142  C  CB    . ILE A 18  ? 0.8052 0.8147 0.8668 0.0563  0.0025  0.0263  18  ILE A CB    
143  C  CG1   . ILE A 18  ? 0.6736 0.7000 0.7424 0.0511  -0.0043 0.0362  18  ILE A CG1   
144  C  CG2   . ILE A 18  ? 0.6597 0.6489 0.7026 0.0512  0.0003  0.0141  18  ILE A CG2   
145  C  CD1   . ILE A 18  ? 0.6275 0.6590 0.7138 0.0558  -0.0046 0.0493  18  ILE A CD1   
146  N  N     . PHE A 19  ? 0.7210 0.7349 0.7662 0.0638  0.0195  0.0109  19  PHE A N     
147  C  CA    . PHE A 19  ? 0.8174 0.8189 0.8545 0.0707  0.0297  0.0042  19  PHE A CA    
148  C  C     . PHE A 19  ? 0.7013 0.6729 0.7157 0.0693  0.0285  -0.0075 19  PHE A C     
149  O  O     . PHE A 19  ? 0.8822 0.8506 0.8814 0.0623  0.0242  -0.0140 19  PHE A O     
150  C  CB    . PHE A 19  ? 0.6731 0.6922 0.7097 0.0688  0.0332  0.0037  19  PHE A CB    
151  C  CG    . PHE A 19  ? 0.6552 0.7028 0.7143 0.0695  0.0327  0.0147  19  PHE A CG    
152  C  CD1   . PHE A 19  ? 0.8132 0.8677 0.8899 0.0789  0.0408  0.0219  19  PHE A CD1   
153  C  CD2   . PHE A 19  ? 0.6249 0.6920 0.6874 0.0609  0.0238  0.0179  19  PHE A CD2   
154  C  CE1   . PHE A 19  ? 0.7200 0.8019 0.8189 0.0788  0.0384  0.0329  19  PHE A CE1   
155  C  CE2   . PHE A 19  ? 0.7842 0.8763 0.8653 0.0607  0.0213  0.0273  19  PHE A CE2   
156  C  CZ    . PHE A 19  ? 0.6774 0.7777 0.7775 0.0691  0.0278  0.0353  19  PHE A CZ    
157  N  N     . LYS A 20  ? 0.8593 0.8083 0.8716 0.0760  0.0317  -0.0103 20  LYS A N     
158  C  CA    . LYS A 20  ? 0.9545 0.8724 0.9448 0.0742  0.0284  -0.0217 20  LYS A CA    
159  C  C     . LYS A 20  ? 0.9681 0.8665 0.9403 0.0834  0.0397  -0.0310 20  LYS A C     
160  O  O     . LYS A 20  ? 0.8788 0.7862 0.8598 0.0928  0.0516  -0.0270 20  LYS A O     
161  C  CB    . LYS A 20  ? 0.9219 0.8232 0.9201 0.0740  0.0223  -0.0197 20  LYS A CB    
162  C  CG    . LYS A 20  ? 0.9344 0.8555 0.9519 0.0670  0.0135  -0.0083 20  LYS A CG    
163  C  CD    . LYS A 20  ? 1.0034 0.9046 1.0242 0.0632  0.0051  -0.0078 20  LYS A CD    
164  C  CE    . LYS A 20  ? 1.1225 1.0142 1.1589 0.0719  0.0098  -0.0021 20  LYS A CE    
165  N  NZ    . LYS A 20  ? 1.1886 1.0723 1.2382 0.0669  0.0010  0.0045  20  LYS A NZ    
166  N  N     . LYS A 21  ? 0.9667 0.8385 0.9131 0.0808  0.0358  -0.0429 21  LYS A N     
167  C  CA    . LYS A 21  ? 1.0153 0.8613 0.9377 0.0899  0.0455  -0.0535 21  LYS A CA    
168  C  C     . LYS A 21  ? 1.1725 0.9833 1.0769 0.0873  0.0363  -0.0639 21  LYS A C     
169  O  O     . LYS A 21  ? 1.2960 1.0986 1.1858 0.0774  0.0245  -0.0695 21  LYS A O     
170  C  CB    . LYS A 21  ? 1.0226 0.8735 0.9253 0.0889  0.0501  -0.0582 21  LYS A CB    
171  C  CG    . LYS A 21  ? 1.2224 1.0446 1.0948 0.0983  0.0599  -0.0696 21  LYS A CG    
172  C  CD    . LYS A 21  ? 1.2200 1.0577 1.0919 0.1065  0.0760  -0.0659 21  LYS A CD    
173  C  CE    . LYS A 21  ? 1.1050 0.9146 0.9491 0.1195  0.0898  -0.0754 21  LYS A CE    
174  N  NZ    . LYS A 21  ? 1.0716 0.8944 0.9337 0.1331  0.1087  -0.0673 21  LYS A NZ    
175  N  N     . GLU A 22  ? 1.2657 1.0557 1.1727 0.0959  0.0412  -0.0661 22  GLU A N     
176  C  CA    . GLU A 22  ? 1.2728 1.0276 1.1662 0.0932  0.0315  -0.0757 22  GLU A CA    
177  C  C     . GLU A 22  ? 1.3144 1.0365 1.1862 0.1065  0.0431  -0.0870 22  GLU A C     
178  O  O     . GLU A 22  ? 1.2671 0.9938 1.1524 0.1188  0.0575  -0.0818 22  GLU A O     
179  C  CB    . GLU A 22  ? 1.1828 0.9419 1.1053 0.0890  0.0232  -0.0660 22  GLU A CB    
180  C  CG    . GLU A 22  ? 1.0006 0.7880 0.9412 0.0763  0.0118  -0.0556 22  GLU A CG    
181  C  CD    . GLU A 22  ? 1.2078 1.0060 1.1791 0.0747  0.0077  -0.0426 22  GLU A CD    
182  O  OE1   . GLU A 22  ? 1.2232 1.0233 1.2096 0.0846  0.0169  -0.0367 22  GLU A OE1   
183  O  OE2   . GLU A 22  ? 1.2704 1.0759 1.2516 0.0641  -0.0042 -0.0372 22  GLU A OE2   
184  N  N     . ASN A 23  ? 1.3495 1.0384 1.1870 0.1043  0.0368  -0.1021 23  ASN A N     
185  C  CA    . ASN A 23  ? 1.3658 1.0172 1.1751 0.1166  0.0466  -0.1157 23  ASN A CA    
186  C  C     . ASN A 23  ? 1.3618 1.0245 1.1648 0.1311  0.0686  -0.1139 23  ASN A C     
187  O  O     . ASN A 23  ? 1.4155 1.0647 1.2193 0.1456  0.0836  -0.1154 23  ASN A O     
188  C  CB    . ASN A 23  ? 1.4090 1.0375 1.2328 0.1214  0.0458  -0.1163 23  ASN A CB    
189  C  CG    . ASN A 23  ? 1.5015 1.1335 1.3482 0.1072  0.0266  -0.1100 23  ASN A CG    
190  O  OD1   . ASN A 23  ? 1.4757 1.1066 1.3131 0.0938  0.0108  -0.1132 23  ASN A OD1   
191  N  ND2   . ASN A 23  ? 1.4221 1.0594 1.3005 0.1103  0.0285  -0.0997 23  ASN A ND2   
192  N  N     . GLY A 24  ? 1.3349 1.0230 1.1336 0.1274  0.0709  -0.1098 24  GLY A N     
193  C  CA    . GLY A 24  ? 1.3417 1.0440 1.1374 0.1394  0.0910  -0.1061 24  GLY A CA    
194  C  C     . GLY A 24  ? 1.3998 1.1311 1.2345 0.1474  0.1035  -0.0911 24  GLY A C     
195  O  O     . GLY A 24  ? 1.4056 1.1462 1.2416 0.1594  0.1218  -0.0872 24  GLY A O     
196  N  N     . GLU A 25  ? 1.3674 1.1142 1.2346 0.1413  0.0941  -0.0813 25  GLU A N     
197  C  CA    . GLU A 25  ? 1.3425 1.1165 1.2474 0.1481  0.1031  -0.0662 25  GLU A CA    
198  C  C     . GLU A 25  ? 1.1887 1.0017 1.1205 0.1359  0.0925  -0.0533 25  GLU A C     
199  O  O     . GLU A 25  ? 1.1372 0.9508 1.0689 0.1231  0.0763  -0.0541 25  GLU A O     
200  C  CB    . GLU A 25  ? 1.4487 1.2036 1.3678 0.1542  0.1028  -0.0653 25  GLU A CB    
201  C  CG    . GLU A 25  ? 1.6458 1.4278 1.6045 0.1620  0.1115  -0.0486 25  GLU A CG    
202  C  CD    . GLU A 25  ? 1.7358 1.5043 1.7131 0.1636  0.1061  -0.0446 25  GLU A CD    
203  O  OE1   . GLU A 25  ? 1.5895 1.3834 1.6013 0.1664  0.1079  -0.0290 25  GLU A OE1   
204  O  OE2   . GLU A 25  ? 1.6964 1.4287 1.6543 0.1617  0.0993  -0.0567 25  GLU A OE2   
205  N  N     . PHE A 26  ? 1.1932 1.0383 1.1482 0.1400  0.1018  -0.0412 26  PHE A N     
206  C  CA    . PHE A 26  ? 0.9750 0.8564 0.9550 0.1297  0.0924  -0.0293 26  PHE A CA    
207  C  C     . PHE A 26  ? 1.0012 0.8937 1.0113 0.1306  0.0879  -0.0179 26  PHE A C     
208  O  O     . PHE A 26  ? 1.0393 0.9331 1.0665 0.1424  0.0987  -0.0114 26  PHE A O     
209  C  CB    . PHE A 26  ? 0.8696 0.7800 0.8616 0.1324  0.1023  -0.0214 26  PHE A CB    
210  C  CG    . PHE A 26  ? 0.9259 0.8724 0.9449 0.1232  0.0931  -0.0091 26  PHE A CG    
211  C  CD1   . PHE A 26  ? 0.8452 0.8006 0.8570 0.1095  0.0798  -0.0113 26  PHE A CD1   
212  C  CD2   . PHE A 26  ? 0.8397 0.8104 0.8908 0.1286  0.0974  0.0047  26  PHE A CD2   
213  C  CE1   . PHE A 26  ? 0.8289 0.8146 0.8618 0.1017  0.0716  -0.0015 26  PHE A CE1   
214  C  CE2   . PHE A 26  ? 0.8176 0.8197 0.8900 0.1199  0.0875  0.0150  26  PHE A CE2   
215  C  CZ    . PHE A 26  ? 0.8382 0.8466 0.8999 0.1066  0.0749  0.0112  26  PHE A CZ    
216  N  N     . LYS A 27  ? 0.9145 0.8154 0.9313 0.1188  0.0727  -0.0146 27  LYS A N     
217  C  CA    . LYS A 27  ? 0.9596 0.8702 1.0020 0.1187  0.0671  -0.0032 27  LYS A CA    
218  C  C     . LYS A 27  ? 0.9137 0.8579 0.9714 0.1084  0.0571  0.0071  27  LYS A C     
219  O  O     . LYS A 27  ? 0.8547 0.8047 0.8994 0.0985  0.0499  0.0024  27  LYS A O     
220  C  CB    . LYS A 27  ? 0.9499 0.8312 0.9842 0.1154  0.0586  -0.0090 27  LYS A CB    
221  C  CG    . LYS A 27  ? 1.1839 1.0262 1.1967 0.1240  0.0660  -0.0224 27  LYS A CG    
222  C  CD    . LYS A 27  ? 1.3998 1.2162 1.4174 0.1239  0.0594  -0.0235 27  LYS A CD    
223  C  CE    . LYS A 27  ? 1.3060 1.0883 1.2943 0.1170  0.0503  -0.0393 27  LYS A CE    
224  N  NZ    . LYS A 27  ? 1.4004 1.1426 1.3718 0.1273  0.0575  -0.0514 27  LYS A NZ    
225  N  N     . ILE A 28  ? 0.7964 0.7618 0.8808 0.1114  0.0565  0.0211  28  ILE A N     
226  C  CA    . ILE A 28  ? 0.7596 0.7554 0.8571 0.1028  0.0467  0.0312  28  ILE A CA    
227  C  C     . ILE A 28  ? 0.8300 0.8245 0.9399 0.1013  0.0391  0.0400  28  ILE A C     
228  O  O     . ILE A 28  ? 0.8260 0.8218 0.9549 0.1096  0.0431  0.0494  28  ILE A O     
229  C  CB    . ILE A 28  ? 0.6724 0.6984 0.7903 0.1066  0.0510  0.0418  28  ILE A CB    
230  C  CG1   . ILE A 28  ? 0.8232 0.8508 0.9314 0.1082  0.0596  0.0347  28  ILE A CG1   
231  C  CG2   . ILE A 28  ? 0.6866 0.7407 0.8136 0.0974  0.0392  0.0506  28  ILE A CG2   
232  C  CD1   . ILE A 28  ? 0.6932 0.7519 0.8236 0.1098  0.0622  0.0455  28  ILE A CD1   
233  N  N     . GLU A 29  ? 0.7787 0.7714 0.8796 0.0911  0.0288  0.0381  29  GLU A N     
234  C  CA    . GLU A 29  ? 0.7242 0.7177 0.8366 0.0886  0.0216  0.0477  29  GLU A CA    
235  C  C     . GLU A 29  ? 0.7142 0.7402 0.8371 0.0841  0.0154  0.0597  29  GLU A C     
236  O  O     . GLU A 29  ? 0.8179 0.8584 0.9311 0.0776  0.0121  0.0562  29  GLU A O     
237  C  CB    . GLU A 29  ? 0.8441 0.8165 0.9424 0.0805  0.0145  0.0401  29  GLU A CB    
238  C  CG    . GLU A 29  ? 0.8754 0.8575 0.9843 0.0746  0.0062  0.0513  29  GLU A CG    
239  C  CD    . GLU A 29  ? 1.1068 1.0670 1.2073 0.0673  -0.0004 0.0455  29  GLU A CD    
240  O  OE1   . GLU A 29  ? 1.2418 1.1770 1.3276 0.0670  0.0003  0.0322  29  GLU A OE1   
241  O  OE2   . GLU A 29  ? 1.2299 1.1985 1.3386 0.0618  -0.0065 0.0547  29  GLU A OE2   
242  N  N     . TYR A 30  ? 0.7476 0.7837 0.8890 0.0878  0.0137  0.0740  30  TYR A N     
243  C  CA    . TYR A 30  ? 0.7117 0.7771 0.8609 0.0845  0.0071  0.0862  30  TYR A CA    
244  C  C     . TYR A 30  ? 0.5955 0.6595 0.7452 0.0798  0.0007  0.0938  30  TYR A C     
245  O  O     . TYR A 30  ? 0.7088 0.7533 0.8650 0.0820  0.0017  0.0959  30  TYR A O     
246  C  CB    . TYR A 30  ? 0.5334 0.6167 0.7044 0.0928  0.0096  0.0995  30  TYR A CB    
247  C  CG    . TYR A 30  ? 0.7151 0.8021 0.8909 0.0985  0.0173  0.0949  30  TYR A CG    
248  C  CD1   . TYR A 30  ? 0.7171 0.7832 0.8977 0.1079  0.0278  0.0905  30  TYR A CD1   
249  C  CD2   . TYR A 30  ? 0.6684 0.7793 0.8443 0.0947  0.0144  0.0953  30  TYR A CD2   
250  C  CE1   . TYR A 30  ? 0.6368 0.7072 0.8224 0.1142  0.0368  0.0878  30  TYR A CE1   
251  C  CE2   . TYR A 30  ? 0.6683 0.7841 0.8519 0.0998  0.0221  0.0931  30  TYR A CE2   
252  C  CZ    . TYR A 30  ? 0.6926 0.7890 0.8812 0.1099  0.0340  0.0899  30  TYR A CZ    
253  O  OH    . TYR A 30  ? 0.7004 0.8028 0.8974 0.1160  0.0434  0.0890  30  TYR A OH    
254  N  N     . ASP A 31  ? 0.5659 0.6501 0.7091 0.0736  -0.0055 0.0981  31  ASP A N     
255  C  CA    . ASP A 31  ? 0.6342 0.7214 0.7776 0.0698  -0.0102 0.1073  31  ASP A CA    
256  C  C     . ASP A 31  ? 0.5976 0.7134 0.7425 0.0698  -0.0149 0.1194  31  ASP A C     
257  O  O     . ASP A 31  ? 0.5428 0.6723 0.6743 0.0652  -0.0181 0.1142  31  ASP A O     
258  C  CB    . ASP A 31  ? 0.6336 0.7111 0.7609 0.0615  -0.0125 0.0976  31  ASP A CB    
259  C  CG    . ASP A 31  ? 0.6473 0.7257 0.7783 0.0584  -0.0154 0.1082  31  ASP A CG    
260  O  OD1   . ASP A 31  ? 0.6272 0.7156 0.7708 0.0625  -0.0159 0.1234  31  ASP A OD1   
261  O  OD2   . ASP A 31  ? 0.8174 0.8873 0.9401 0.0522  -0.0170 0.1026  31  ASP A OD2   
262  N  N     . ARG A 32  ? 0.5576 0.6811 0.7179 0.0751  -0.0157 0.1354  32  ARG A N     
263  C  CA    . ARG A 32  ? 0.6366 0.7864 0.7972 0.0757  -0.0211 0.1485  32  ARG A CA    
264  C  C     . ARG A 32  ? 0.6358 0.7905 0.7895 0.0729  -0.0236 0.1583  32  ARG A C     
265  O  O     . ARG A 32  ? 0.8540 1.0278 1.0080 0.0750  -0.0276 0.1721  32  ARG A O     
266  C  CB    . ARG A 32  ? 0.6144 0.7729 0.7968 0.0841  -0.0207 0.1623  32  ARG A CB    
267  C  CG    . ARG A 32  ? 0.5233 0.6760 0.7169 0.0891  -0.0156 0.1551  32  ARG A CG    
268  C  CD    . ARG A 32  ? 0.6859 0.8494 0.9040 0.0981  -0.0148 0.1710  32  ARG A CD    
269  N  NE    . ARG A 32  ? 0.6810 0.8585 0.9080 0.1010  -0.0142 0.1694  32  ARG A NE    
270  C  CZ    . ARG A 32  ? 0.7085 0.8729 0.9425 0.1058  -0.0056 0.1605  32  ARG A CZ    
271  N  NH1   . ARG A 32  ? 0.7907 0.9260 1.0210 0.1082  0.0023  0.1508  32  ARG A NH1   
272  N  NH2   . ARG A 32  ? 0.9977 1.1786 1.2426 0.1082  -0.0049 0.1618  32  ARG A NH2   
273  N  N     . THR A 33  ? 0.7458 0.8845 0.8935 0.0684  -0.0214 0.1524  33  THR A N     
274  C  CA    . THR A 33  ? 0.7712 0.9136 0.9168 0.0665  -0.0218 0.1635  33  THR A CA    
275  C  C     . THR A 33  ? 0.7645 0.9132 0.8886 0.0605  -0.0226 0.1562  33  THR A C     
276  O  O     . THR A 33  ? 0.7994 0.9557 0.9193 0.0600  -0.0219 0.1666  33  THR A O     
277  C  CB    . THR A 33  ? 0.7184 0.8384 0.8789 0.0660  -0.0188 0.1662  33  THR A CB    
278  O  OG1   . THR A 33  ? 0.7579 0.8594 0.9108 0.0606  -0.0181 0.1491  33  THR A OG1   
279  C  CG2   . THR A 33  ? 0.6848 0.7949 0.8663 0.0728  -0.0171 0.1727  33  THR A CG2   
280  N  N     . PHE A 34  ? 0.7818 0.9277 0.8930 0.0565  -0.0233 0.1396  34  PHE A N     
281  C  CA    . PHE A 34  ? 0.7899 0.9394 0.8820 0.0513  -0.0235 0.1319  34  PHE A CA    
282  C  C     . PHE A 34  ? 0.6357 0.8065 0.7124 0.0521  -0.0268 0.1368  34  PHE A C     
283  O  O     . PHE A 34  ? 0.7644 0.9464 0.8407 0.0538  -0.0311 0.1367  34  PHE A O     
284  C  CB    . PHE A 34  ? 0.7031 0.8422 0.7872 0.0470  -0.0232 0.1135  34  PHE A CB    
285  C  CG    . PHE A 34  ? 0.8246 0.9595 0.8953 0.0417  -0.0220 0.1057  34  PHE A CG    
286  C  CD1   . PHE A 34  ? 0.8869 1.0309 0.9400 0.0390  -0.0234 0.0973  34  PHE A CD1   
287  C  CD2   . PHE A 34  ? 0.7879 0.9096 0.8653 0.0393  -0.0200 0.1074  34  PHE A CD2   
288  C  CE1   . PHE A 34  ? 0.7801 0.9199 0.8225 0.0350  -0.0215 0.0908  34  PHE A CE1   
289  C  CE2   . PHE A 34  ? 0.9041 1.0235 0.9722 0.0348  -0.0188 0.1018  34  PHE A CE2   
290  C  CZ    . PHE A 34  ? 0.7817 0.9102 0.8323 0.0332  -0.0188 0.0936  34  PHE A CZ    
291  N  N     . GLU A 35  ? 0.6617 0.8379 0.7257 0.0511  -0.0250 0.1413  35  GLU A N     
292  C  CA    . GLU A 35  ? 0.7336 0.9273 0.7782 0.0524  -0.0280 0.1451  35  GLU A CA    
293  C  C     . GLU A 35  ? 0.7545 0.9473 0.7774 0.0482  -0.0274 0.1310  35  GLU A C     
294  O  O     . GLU A 35  ? 0.8417 1.0246 0.8638 0.0458  -0.0222 0.1268  35  GLU A O     
295  C  CB    . GLU A 35  ? 0.6861 0.8885 0.7299 0.0567  -0.0250 0.1635  35  GLU A CB    
296  C  CG    . GLU A 35  ? 0.8191 1.0167 0.8885 0.0601  -0.0231 0.1782  35  GLU A CG    
297  C  CD    . GLU A 35  ? 0.9741 1.1791 1.0444 0.0637  -0.0186 0.1972  35  GLU A CD    
298  O  OE1   . GLU A 35  ? 0.8822 1.1033 0.9396 0.0677  -0.0208 0.2076  35  GLU A OE1   
299  O  OE2   . GLU A 35  ? 0.9838 1.1787 1.0679 0.0625  -0.0132 0.2023  35  GLU A OE2   
300  N  N     . PRO A 36  ? 0.8227 1.0250 0.8289 0.0469  -0.0332 0.1241  36  PRO A N     
301  C  CA    . PRO A 36  ? 0.7483 0.9484 0.7329 0.0434  -0.0327 0.1108  36  PRO A CA    
302  C  C     . PRO A 36  ? 0.7423 0.9475 0.7077 0.0464  -0.0283 0.1176  36  PRO A C     
303  O  O     . PRO A 36  ? 0.7291 0.9444 0.6913 0.0511  -0.0285 0.1320  36  PRO A O     
304  C  CB    . PRO A 36  ? 0.8116 1.0201 0.7875 0.0409  -0.0419 0.1030  36  PRO A CB    
305  C  CG    . PRO A 36  ? 0.6718 0.8933 0.6564 0.0449  -0.0473 0.1173  36  PRO A CG    
306  C  CD    . PRO A 36  ? 0.6368 0.8517 0.6456 0.0483  -0.0414 0.1279  36  PRO A CD    
307  N  N     . TYR A 37  ? 0.7752 0.9735 0.7274 0.0444  -0.0235 0.1075  37  TYR A N     
308  C  CA    . TYR A 37  ? 0.7012 0.9024 0.6365 0.0485  -0.0162 0.1137  37  TYR A CA    
309  C  C     . TYR A 37  ? 0.6533 0.8468 0.5720 0.0462  -0.0127 0.0990  37  TYR A C     
310  O  O     . TYR A 37  ? 0.6759 0.8604 0.6012 0.0412  -0.0147 0.0861  37  TYR A O     
311  C  CB    . TYR A 37  ? 0.6942 0.8933 0.6490 0.0511  -0.0079 0.1283  37  TYR A CB    
312  C  CG    . TYR A 37  ? 0.7180 0.9038 0.6901 0.0466  -0.0044 0.1213  37  TYR A CG    
313  C  CD1   . TYR A 37  ? 0.5888 0.7658 0.5819 0.0430  -0.0086 0.1177  37  TYR A CD1   
314  C  CD2   . TYR A 37  ? 0.7355 0.9172 0.7020 0.0466  0.0032  0.1183  37  TYR A CD2   
315  C  CE1   . TYR A 37  ? 0.6996 0.8637 0.7052 0.0388  -0.0068 0.1110  37  TYR A CE1   
316  C  CE2   . TYR A 37  ? 0.4843 0.6549 0.4669 0.0422  0.0048  0.1128  37  TYR A CE2   
317  C  CZ    . TYR A 37  ? 0.6237 0.7853 0.6246 0.0380  -0.0009 0.1090  37  TYR A CZ    
318  O  OH    . TYR A 37  ? 0.8210 0.9707 0.8348 0.0334  -0.0006 0.1033  37  TYR A OH    
319  N  N     . PHE A 38  ? 0.7485 0.9451 0.6451 0.0508  -0.0065 0.1018  38  PHE A N     
320  C  CA    . PHE A 38  ? 0.7335 0.9219 0.6192 0.0511  0.0013  0.0927  38  PHE A CA    
321  C  C     . PHE A 38  ? 0.7929 0.9866 0.6680 0.0588  0.0128  0.1057  38  PHE A C     
322  O  O     . PHE A 38  ? 0.7974 1.0009 0.6725 0.0632  0.0138  0.1211  38  PHE A O     
323  C  CB    . PHE A 38  ? 0.8095 0.9928 0.6720 0.0481  -0.0045 0.0744  38  PHE A CB    
324  C  CG    . PHE A 38  ? 0.7781 0.9677 0.6095 0.0514  -0.0094 0.0736  38  PHE A CG    
325  C  CD1   . PHE A 38  ? 0.8683 1.0594 0.6750 0.0588  -0.0006 0.0785  38  PHE A CD1   
326  C  CD2   . PHE A 38  ? 0.7849 0.9786 0.6111 0.0470  -0.0231 0.0676  38  PHE A CD2   
327  C  CE1   . PHE A 38  ? 0.8887 1.0837 0.6625 0.0618  -0.0060 0.0767  38  PHE A CE1   
328  C  CE2   . PHE A 38  ? 0.7910 0.9899 0.5878 0.0490  -0.0299 0.0663  38  PHE A CE2   
329  C  CZ    . PHE A 38  ? 0.8737 1.0723 0.6422 0.0564  -0.0218 0.0702  38  PHE A CZ    
330  N  N     . TYR A 39  ? 0.8095 0.9973 0.6768 0.0609  0.0223  0.1007  39  TYR A N     
331  C  CA    . TYR A 39  ? 0.8266 1.0193 0.6877 0.0688  0.0359  0.1138  39  TYR A CA    
332  C  C     . TYR A 39  ? 0.8716 1.0632 0.6931 0.0751  0.0405  0.1066  39  TYR A C     
333  O  O     . TYR A 39  ? 0.9168 1.1005 0.7189 0.0721  0.0339  0.0888  39  TYR A O     
334  C  CB    . TYR A 39  ? 0.6888 0.8766 0.5735 0.0680  0.0453  0.1167  39  TYR A CB    
335  C  CG    . TYR A 39  ? 0.6330 0.8190 0.5541 0.0616  0.0402  0.1228  39  TYR A CG    
336  C  CD1   . TYR A 39  ? 0.7197 0.9128 0.6614 0.0633  0.0428  0.1419  39  TYR A CD1   
337  C  CD2   . TYR A 39  ? 0.7141 0.8900 0.6478 0.0541  0.0330  0.1095  39  TYR A CD2   
338  C  CE1   . TYR A 39  ? 0.5795 0.7678 0.5526 0.0572  0.0374  0.1461  39  TYR A CE1   
339  C  CE2   . TYR A 39  ? 0.6010 0.7728 0.5637 0.0487  0.0282  0.1137  39  TYR A CE2   
340  C  CZ    . TYR A 39  ? 0.5338 0.7109 0.5157 0.0501  0.0300  0.1313  39  TYR A CZ    
341  O  OH    . TYR A 39  ? 0.5196 0.6896 0.5285 0.0446  0.0244  0.1340  39  TYR A OH    
342  N  N     . ALA A 40  ? 1.0265 1.2253 0.8361 0.0840  0.0521  0.1209  40  ALA A N     
343  C  CA    . ALA A 40  ? 1.0957 1.2922 0.8652 0.0921  0.0596  0.1156  40  ALA A CA    
344  C  C     . ALA A 40  ? 1.1028 1.3042 0.8757 0.1016  0.0790  0.1315  40  ALA A C     
345  O  O     . ALA A 40  ? 1.1353 1.3476 0.9304 0.1037  0.0840  0.1520  40  ALA A O     
346  C  CB    . ALA A 40  ? 1.0324 1.2351 0.7712 0.0946  0.0507  0.1173  40  ALA A CB    
347  N  N     . LEU A 41  ? 1.0567 1.2500 0.8095 0.1076  0.0903  0.1228  41  LEU A N     
348  C  CA    . LEU A 41  ? 1.0591 1.2572 0.8139 0.1181  0.1109  0.1373  41  LEU A CA    
349  C  C     . LEU A 41  ? 1.1372 1.3339 0.8427 0.1294  0.1192  0.1355  41  LEU A C     
350  O  O     . LEU A 41  ? 1.1743 1.3575 0.8477 0.1314  0.1189  0.1162  41  LEU A O     
351  C  CB    . LEU A 41  ? 1.0407 1.2304 0.8138 0.1174  0.1193  0.1301  41  LEU A CB    
352  C  CG    . LEU A 41  ? 1.2367 1.4349 1.0361 0.1243  0.1379  0.1497  41  LEU A CG    
353  C  CD1   . LEU A 41  ? 1.0702 1.2654 0.9111 0.1160  0.1349  0.1480  41  LEU A CD1   
354  C  CD2   . LEU A 41  ? 1.1693 1.3640 0.9383 0.1379  0.1571  0.1487  41  LEU A CD2   
355  N  N     . LEU A 42  ? 1.1162 1.3256 0.8144 0.1367  0.1262  0.1555  42  LEU A N     
356  C  CA    . LEU A 42  ? 1.1862 1.3947 0.8337 0.1476  0.1327  0.1551  42  LEU A CA    
357  C  C     . LEU A 42  ? 1.3589 1.5674 0.9950 0.1615  0.1580  0.1639  42  LEU A C     
358  O  O     . LEU A 42  ? 1.4447 1.6572 1.1170 0.1627  0.1705  0.1741  42  LEU A O     
359  C  CB    . LEU A 42  ? 1.2887 1.5114 0.9298 0.1491  0.1267  0.1727  42  LEU A CB    
360  C  CG    . LEU A 42  ? 1.2324 1.4571 0.8792 0.1379  0.1028  0.1666  42  LEU A CG    
361  C  CD1   . LEU A 42  ? 1.2764 1.5178 0.9434 0.1387  0.1012  0.1915  42  LEU A CD1   
362  C  CD2   . LEU A 42  ? 1.2274 1.4438 0.8239 0.1384  0.0909  0.1487  42  LEU A CD2   
363  N  N     . LYS A 43  ? 1.4610 1.6647 1.0449 0.1725  0.1653  0.1598  43  LYS A N     
364  C  CA    . LYS A 43  ? 1.5601 1.7634 1.1269 0.1881  0.1913  0.1685  43  LYS A CA    
365  C  C     . LYS A 43  ? 1.6241 1.8479 1.2134 0.1953  0.2061  0.2008  43  LYS A C     
366  O  O     . LYS A 43  ? 1.6550 1.8857 1.2755 0.2006  0.2246  0.2157  43  LYS A O     
367  C  CB    . LYS A 43  ? 1.5946 1.7838 1.0941 0.1980  0.1940  0.1528  43  LYS A CB    
368  C  CG    . LYS A 43  ? 1.6081 1.7744 1.0860 0.1931  0.1846  0.1214  43  LYS A CG    
369  C  CD    . LYS A 43  ? 1.7834 1.9354 1.2342 0.2074  0.2074  0.1137  43  LYS A CD    
370  C  CE    . LYS A 43  ? 1.7547 1.8811 1.1755 0.2033  0.1969  0.0817  43  LYS A CE    
371  N  NZ    . LYS A 43  ? 1.5728 1.6825 0.9600 0.2189  0.2194  0.0728  43  LYS A NZ    
372  N  N     . ASP A 44  ? 1.5792 1.8134 1.1547 0.1955  0.1983  0.2131  44  ASP A N     
373  C  CA    . ASP A 44  ? 1.5924 1.8465 1.1954 0.1997  0.2085  0.2448  44  ASP A CA    
374  C  C     . ASP A 44  ? 1.5768 1.8392 1.2215 0.1856  0.1886  0.2519  44  ASP A C     
375  O  O     . ASP A 44  ? 1.5163 1.7713 1.1554 0.1751  0.1669  0.2340  44  ASP A O     
376  C  CB    . ASP A 44  ? 1.6399 1.9005 1.1941 0.2142  0.2202  0.2583  44  ASP A CB    
377  C  CG    . ASP A 44  ? 1.7027 1.9645 1.2241 0.2101  0.1992  0.2544  44  ASP A CG    
378  O  OD1   . ASP A 44  ? 1.7876 2.0538 1.2656 0.2222  0.2080  0.2646  44  ASP A OD1   
379  O  OD2   . ASP A 44  ? 1.7813 2.0401 1.3175 0.1964  0.1755  0.2421  44  ASP A OD2   
380  N  N     . ASP A 45  ? 1.6804 1.9575 1.3698 0.1853  0.1966  0.2782  45  ASP A N     
381  C  CA    . ASP A 45  ? 1.5645 1.8479 1.2945 0.1731  0.1797  0.2864  45  ASP A CA    
382  C  C     . ASP A 45  ? 1.5330 1.8271 1.2443 0.1766  0.1742  0.3019  45  ASP A C     
383  O  O     . ASP A 45  ? 1.4747 1.7787 1.2221 0.1720  0.1694  0.3208  45  ASP A O     
384  C  CB    . ASP A 45  ? 1.6023 1.8936 1.3920 0.1693  0.1881  0.3056  45  ASP A CB    
385  C  CG    . ASP A 45  ? 1.8659 2.1719 1.6623 0.1814  0.2112  0.3347  45  ASP A CG    
386  O  OD1   . ASP A 45  ? 1.6547 1.9698 1.5014 0.1778  0.2160  0.3553  45  ASP A OD1   
387  O  OD2   . ASP A 45  ? 1.9327 2.2405 1.6838 0.1946  0.2246  0.3370  45  ASP A OD2   
388  N  N     . SER A 46  ? 1.5306 1.8218 1.1850 0.1846  0.1739  0.2939  46  SER A N     
389  C  CA    . SER A 46  ? 1.5604 1.8618 1.1909 0.1886  0.1677  0.3082  46  SER A CA    
390  C  C     . SER A 46  ? 1.4818 1.7751 1.0683 0.1849  0.1469  0.2866  46  SER A C     
391  O  O     . SER A 46  ? 1.6189 1.9212 1.1973 0.1839  0.1349  0.2969  46  SER A O     
392  C  CB    . SER A 46  ? 1.5896 1.9002 1.1903 0.2052  0.1907  0.3289  46  SER A CB    
393  O  OG    . SER A 46  ? 1.6100 1.9265 1.2463 0.2100  0.2126  0.3452  46  SER A OG    
394  N  N     . ALA A 47  ? 1.3968 1.6737 0.9565 0.1825  0.1418  0.2581  47  ALA A N     
395  C  CA    . ALA A 47  ? 1.5358 1.8045 1.0552 0.1779  0.1210  0.2375  47  ALA A CA    
396  C  C     . ALA A 47  ? 1.4891 1.7604 1.0410 0.1636  0.0973  0.2322  47  ALA A C     
397  O  O     . ALA A 47  ? 1.3855 1.6520 0.9110 0.1584  0.0782  0.2166  47  ALA A O     
398  C  CB    . ALA A 47  ? 1.4836 1.7323 0.9698 0.1784  0.1219  0.2084  47  ALA A CB    
399  N  N     . ILE A 48  ? 1.3568 1.6349 0.9648 0.1572  0.0977  0.2446  48  ILE A N     
400  C  CA    . ILE A 48  ? 1.3190 1.5970 0.9563 0.1445  0.0768  0.2371  48  ILE A CA    
401  C  C     . ILE A 48  ? 1.3926 1.6809 1.0166 0.1437  0.0608  0.2458  48  ILE A C     
402  O  O     . ILE A 48  ? 1.4684 1.7555 1.1043 0.1343  0.0420  0.2350  48  ILE A O     
403  C  CB    . ILE A 48  ? 1.2707 1.5515 0.9682 0.1380  0.0793  0.2477  48  ILE A CB    
404  C  CG1   . ILE A 48  ? 1.3186 1.5906 1.0348 0.1256  0.0613  0.2272  48  ILE A CG1   
405  C  CG2   . ILE A 48  ? 1.3595 1.6550 1.0823 0.1401  0.0799  0.2759  48  ILE A CG2   
406  C  CD1   . ILE A 48  ? 1.2069 1.4768 0.9746 0.1182  0.0613  0.2307  48  ILE A CD1   
407  N  N     . GLU A 49  ? 1.3711 1.6709 0.9735 0.1535  0.0680  0.2666  49  GLU A N     
408  C  CA    . GLU A 49  ? 1.5012 1.8110 1.0861 0.1532  0.0513  0.2743  49  GLU A CA    
409  C  C     . GLU A 49  ? 1.5380 1.8386 1.0829 0.1483  0.0329  0.2487  49  GLU A C     
410  O  O     . GLU A 49  ? 1.5886 1.8927 1.1440 0.1399  0.0124  0.2435  49  GLU A O     
411  C  CB    . GLU A 49  ? 1.5239 1.8458 1.0825 0.1658  0.0633  0.2994  49  GLU A CB    
412  C  CG    . GLU A 49  ? 1.4742 1.8069 1.0775 0.1695  0.0794  0.3279  49  GLU A CG    
413  C  CD    . GLU A 49  ? 1.5078 1.8447 1.1661 0.1596  0.0672  0.3348  49  GLU A CD    
414  O  OE1   . GLU A 49  ? 1.3229 1.6650 0.9791 0.1555  0.0486  0.3346  49  GLU A OE1   
415  O  OE2   . GLU A 49  ? 1.6465 1.9808 1.3503 0.1561  0.0761  0.3403  49  GLU A OE2   
416  N  N     . GLU A 50  ? 1.5536 1.8418 1.0543 0.1535  0.0403  0.2324  50  GLU A N     
417  C  CA    . GLU A 50  ? 1.6422 1.9178 1.1080 0.1475  0.0231  0.2053  50  GLU A CA    
418  C  C     . GLU A 50  ? 1.5893 1.8571 1.0928 0.1343  0.0117  0.1868  50  GLU A C     
419  O  O     . GLU A 50  ? 1.5578 1.8233 1.0549 0.1256  -0.0093 0.1725  50  GLU A O     
420  C  CB    . GLU A 50  ? 1.6389 1.8991 1.0543 0.1563  0.0364  0.1908  50  GLU A CB    
421  C  CG    . GLU A 50  ? 1.7151 1.9664 1.0714 0.1564  0.0203  0.1738  50  GLU A CG    
422  C  CD    . GLU A 50  ? 1.8159 2.0536 1.1165 0.1693  0.0374  0.1665  50  GLU A CD    
423  O  OE1   . GLU A 50  ? 1.7951 2.0362 1.1029 0.1801  0.0628  0.1814  50  GLU A OE1   
424  O  OE2   . GLU A 50  ? 1.9310 2.1544 1.1812 0.1688  0.0256  0.1461  50  GLU A OE2   
425  N  N     . VAL A 51  ? 1.5748 1.8390 1.1186 0.1327  0.0251  0.1877  51  VAL A N     
426  C  CA    . VAL A 51  ? 1.4031 1.6590 0.9800 0.1210  0.0160  0.1704  51  VAL A CA    
427  C  C     . VAL A 51  ? 1.3467 1.6137 0.9632 0.1131  0.0014  0.1796  51  VAL A C     
428  O  O     . VAL A 51  ? 1.3884 1.6508 1.0219 0.1033  -0.0122 0.1649  51  VAL A O     
429  C  CB    . VAL A 51  ? 1.2592 1.5070 0.8634 0.1218  0.0338  0.1680  51  VAL A CB    
430  C  CG1   . VAL A 51  ? 1.2125 1.4476 0.8325 0.1113  0.0248  0.1447  51  VAL A CG1   
431  C  CG2   . VAL A 51  ? 1.4427 1.6841 1.0117 0.1331  0.0526  0.1673  51  VAL A CG2   
432  N  N     . LYS A 52  ? 1.2942 1.5754 0.9269 0.1176  0.0047  0.2044  52  LYS A N     
433  C  CA    . LYS A 52  ? 1.3312 1.6226 0.9959 0.1118  -0.0097 0.2138  52  LYS A CA    
434  C  C     . LYS A 52  ? 1.4787 1.7735 1.1179 0.1073  -0.0313 0.2038  52  LYS A C     
435  O  O     . LYS A 52  ? 1.3863 1.6837 1.0512 0.0992  -0.0457 0.1988  52  LYS A O     
436  C  CB    . LYS A 52  ? 1.3323 1.6377 1.0132 0.1189  -0.0018 0.2435  52  LYS A CB    
437  C  CG    . LYS A 52  ? 1.5532 1.8700 1.2679 0.1156  -0.0139 0.2583  52  LYS A CG    
438  C  CD    . LYS A 52  ? 1.3933 1.7050 1.1390 0.1054  -0.0266 0.2436  52  LYS A CD    
439  C  CE    . LYS A 52  ? 1.3140 1.6364 1.0951 0.1048  -0.0340 0.2615  52  LYS A CE    
440  N  NZ    . LYS A 52  ? 1.4773 1.8153 1.2373 0.1110  -0.0407 0.2805  52  LYS A NZ    
441  N  N     . LYS A 53  ? 1.4345 1.7282 1.0225 0.1124  -0.0340 0.1998  53  LYS A N     
442  C  CA    . LYS A 53  ? 1.3697 1.6697 0.9332 0.1087  -0.0561 0.1959  53  LYS A CA    
443  C  C     . LYS A 53  ? 1.4465 1.7346 0.9969 0.0990  -0.0713 0.1683  53  LYS A C     
444  O  O     . LYS A 53  ? 1.4804 1.7745 1.0177 0.0940  -0.0922 0.1652  53  LYS A O     
445  C  CB    . LYS A 53  ? 1.3706 1.6752 0.8816 0.1182  -0.0552 0.2053  53  LYS A CB    
446  C  CG    . LYS A 53  ? 1.4553 1.7707 0.9702 0.1295  -0.0373 0.2330  53  LYS A CG    
447  C  CD    . LYS A 53  ? 1.4525 1.7840 1.0151 0.1279  -0.0415 0.2561  53  LYS A CD    
448  C  CE    . LYS A 53  ? 1.4469 1.7871 1.0196 0.1382  -0.0219 0.2835  53  LYS A CE    
449  N  NZ    . LYS A 53  ? 1.4416 1.7809 1.0713 0.1356  -0.0104 0.2920  53  LYS A NZ    
450  N  N     . ILE A 54  ? 1.3969 1.6687 0.9509 0.0960  -0.0628 0.1492  54  ILE A N     
451  C  CA    . ILE A 54  ? 1.3873 1.6483 0.9313 0.0863  -0.0785 0.1248  54  ILE A CA    
452  C  C     . ILE A 54  ? 1.2853 1.5560 0.8724 0.0764  -0.0940 0.1262  54  ILE A C     
453  O  O     . ILE A 54  ? 1.3075 1.5838 0.9389 0.0757  -0.0869 0.1367  54  ILE A O     
454  C  CB    . ILE A 54  ? 1.1345 1.3758 0.6747 0.0848  -0.0670 0.1039  54  ILE A CB    
455  C  CG1   . ILE A 54  ? 1.3735 1.6057 0.8830 0.0962  -0.0459 0.1052  54  ILE A CG1   
456  C  CG2   . ILE A 54  ? 1.2580 1.4871 0.7778 0.0760  -0.0837 0.0799  54  ILE A CG2   
457  C  CD1   . ILE A 54  ? 1.3697 1.6048 0.9156 0.1001  -0.0264 0.1177  54  ILE A CD1   
458  N  N     . THR A 55  ? 1.2262 1.4987 0.8001 0.0689  -0.1156 0.1162  55  THR A N     
459  C  CA    . THR A 55  ? 1.2354 1.5173 0.8467 0.0594  -0.1316 0.1161  55  THR A CA    
460  C  C     . THR A 55  ? 1.2272 1.4958 0.8326 0.0493  -0.1424 0.0913  55  THR A C     
461  O  O     . THR A 55  ? 1.3191 1.5708 0.8899 0.0500  -0.1385 0.0745  55  THR A O     
462  C  CB    . THR A 55  ? 1.2884 1.5892 0.8957 0.0593  -0.1498 0.1318  55  THR A CB    
463  O  OG1   . THR A 55  ? 1.2903 1.5874 0.8620 0.0532  -0.1700 0.1177  55  THR A OG1   
464  C  CG2   . THR A 55  ? 1.3804 1.6898 0.9690 0.0707  -0.1399 0.1530  55  THR A CG2   
465  N  N     . ALA A 56  ? 1.2799 1.5563 0.9208 0.0404  -0.1554 0.0899  56  ALA A N     
466  C  CA    . ALA A 56  ? 1.2554 1.5225 0.8966 0.0297  -0.1681 0.0695  56  ALA A CA    
467  C  C     . ALA A 56  ? 1.2877 1.5716 0.9675 0.0220  -0.1847 0.0768  56  ALA A C     
468  O  O     . ALA A 56  ? 1.2934 1.5935 1.0017 0.0257  -0.1832 0.0960  56  ALA A O     
469  C  CB    . ALA A 56  ? 1.0921 1.3419 0.7461 0.0282  -0.1527 0.0547  56  ALA A CB    
470  N  N     . GLU A 57  ? 1.2954 1.5752 0.9778 0.0114  -0.2000 0.0619  57  GLU A N     
471  C  CA    . GLU A 57  ? 1.3286 1.6246 1.0497 0.0035  -0.2156 0.0681  57  GLU A CA    
472  C  C     . GLU A 57  ? 1.3298 1.6197 1.0890 -0.0014 -0.2066 0.0598  57  GLU A C     
473  O  O     . GLU A 57  ? 1.3829 1.6540 1.1304 -0.0036 -0.1983 0.0428  57  GLU A O     
474  C  CB    . GLU A 57  ? 1.4282 1.7272 1.1287 -0.0059 -0.2421 0.0602  57  GLU A CB    
475  C  CG    . GLU A 57  ? 1.4733 1.7563 1.1710 -0.0167 -0.2494 0.0377  57  GLU A CG    
476  C  CD    . GLU A 57  ? 1.5129 1.8081 1.2603 -0.0261 -0.2588 0.0402  57  GLU A CD    
477  O  OE1   . GLU A 57  ? 1.4624 1.7454 1.2166 -0.0345 -0.2613 0.0243  57  GLU A OE1   
478  O  OE2   . GLU A 57  ? 1.6206 1.9375 1.4011 -0.0245 -0.2628 0.0589  57  GLU A OE2   
479  N  N     . ARG A 58  ? 1.3045 1.6098 1.1086 -0.0022 -0.2072 0.0725  58  ARG A N     
480  C  CA    . ARG A 58  ? 1.3647 1.6659 1.2049 -0.0065 -0.1996 0.0662  58  ARG A CA    
481  C  C     . ARG A 58  ? 1.4132 1.7292 1.2829 -0.0155 -0.2174 0.0687  58  ARG A C     
482  O  O     . ARG A 58  ? 1.4054 1.7150 1.2705 -0.0251 -0.2282 0.0547  58  ARG A O     
483  C  CB    . ARG A 58  ? 1.2371 1.5403 1.1066 0.0016  -0.1805 0.0779  58  ARG A CB    
484  C  CG    . ARG A 58  ? 1.0095 1.2989 0.8973 -0.0002 -0.1663 0.0668  58  ARG A CG    
485  C  CD    . ARG A 58  ? 1.0876 1.3743 0.9944 0.0081  -0.1478 0.0763  58  ARG A CD    
486  N  NE    . ARG A 58  ? 1.0449 1.3396 0.9926 0.0080  -0.1454 0.0831  58  ARG A NE    
487  C  CZ    . ARG A 58  ? 0.9795 1.2815 0.9499 0.0150  -0.1388 0.0983  58  ARG A CZ    
488  N  NH1   . ARG A 58  ? 0.9273 1.2308 0.8864 0.0220  -0.1343 0.1095  58  ARG A NH1   
489  N  NH2   . ARG A 58  ? 0.9293 1.2365 0.9346 0.0153  -0.1358 0.1027  58  ARG A NH2   
490  N  N     . HIS A 59  ? 1.2138 1.5498 1.1160 -0.0124 -0.2203 0.0873  59  HIS A N     
491  C  CA    . HIS A 59  ? 1.3457 1.6993 1.2831 -0.0195 -0.2353 0.0936  59  HIS A CA    
492  C  C     . HIS A 59  ? 1.3942 1.7696 1.3346 -0.0171 -0.2505 0.1125  59  HIS A C     
493  O  O     . HIS A 59  ? 1.3142 1.7051 1.2886 -0.0114 -0.2464 0.1302  59  HIS A O     
494  C  CB    . HIS A 59  ? 1.3506 1.7072 1.3330 -0.0171 -0.2206 0.0984  59  HIS A CB    
495  C  CG    . HIS A 59  ? 1.5044 1.8485 1.4950 -0.0246 -0.2166 0.0822  59  HIS A CG    
496  N  ND1   . HIS A 59  ? 1.5454 1.8851 1.5227 -0.0356 -0.2323 0.0691  59  HIS A ND1   
497  C  CD2   . HIS A 59  ? 1.5384 1.8727 1.5484 -0.0225 -0.1991 0.0773  59  HIS A CD2   
498  C  CE1   . HIS A 59  ? 1.5933 1.9218 1.5836 -0.0399 -0.2239 0.0578  59  HIS A CE1   
499  N  NE2   . HIS A 59  ? 1.7588 2.0843 1.7679 -0.0320 -0.2037 0.0627  59  HIS A NE2   
500  N  N     . GLY A 60  ? 1.3267 1.7023 1.2302 -0.0212 -0.2684 0.1086  60  GLY A N     
501  C  CA    . GLY A 60  ? 1.4124 1.8073 1.3109 -0.0183 -0.2831 0.1265  60  GLY A CA    
502  C  C     . GLY A 60  ? 1.3914 1.7887 1.2861 -0.0053 -0.2672 0.1421  60  GLY A C     
503  O  O     . GLY A 60  ? 1.4992 1.9160 1.4103 -0.0008 -0.2739 0.1625  60  GLY A O     
504  N  N     . THR A 61  ? 1.4167 1.7950 1.2923 0.0009  -0.2465 0.1338  61  THR A N     
505  C  CA    . THR A 61  ? 1.3831 1.7616 1.2597 0.0126  -0.2294 0.1482  61  THR A CA    
506  C  C     . THR A 61  ? 1.3808 1.7398 1.2138 0.0166  -0.2170 0.1370  61  THR A C     
507  O  O     . THR A 61  ? 1.2660 1.6073 1.0888 0.0129  -0.2094 0.1183  61  THR A O     
508  C  CB    . THR A 61  ? 1.3569 1.7344 1.2781 0.0168  -0.2117 0.1535  61  THR A CB    
509  O  OG1   . THR A 61  ? 1.3276 1.6924 1.2589 0.0102  -0.2066 0.1354  61  THR A OG1   
510  C  CG2   . THR A 61  ? 1.1189 1.5183 1.0822 0.0185  -0.2193 0.1726  61  THR A CG2   
511  N  N     . VAL A 62  ? 1.2507 1.6135 1.0594 0.0246  -0.2142 0.1497  62  VAL A N     
512  C  CA    . VAL A 62  ? 1.1523 1.4987 0.9215 0.0301  -0.2004 0.1423  62  VAL A CA    
513  C  C     . VAL A 62  ? 1.1829 1.5193 0.9755 0.0357  -0.1765 0.1439  62  VAL A C     
514  O  O     . VAL A 62  ? 1.2065 1.5515 1.0330 0.0404  -0.1696 0.1599  62  VAL A O     
515  C  CB    . VAL A 62  ? 1.1714 1.5263 0.9063 0.0372  -0.2049 0.1569  62  VAL A CB    
516  C  CG1   . VAL A 62  ? 1.1745 1.5422 0.9360 0.0463  -0.1949 0.1821  62  VAL A CG1   
517  C  CG2   . VAL A 62  ? 1.2972 1.6348 0.9827 0.0415  -0.1947 0.1454  62  VAL A CG2   
518  N  N     . VAL A 63  ? 1.2056 1.5231 0.9820 0.0348  -0.1647 0.1268  63  VAL A N     
519  C  CA    . VAL A 63  ? 1.0788 1.3857 0.8730 0.0394  -0.1434 0.1273  63  VAL A CA    
520  C  C     . VAL A 63  ? 1.1254 1.4282 0.8908 0.0482  -0.1309 0.1349  63  VAL A C     
521  O  O     . VAL A 63  ? 1.2203 1.5190 0.9436 0.0496  -0.1345 0.1288  63  VAL A O     
522  C  CB    . VAL A 63  ? 1.0376 1.3278 0.8364 0.0333  -0.1375 0.1063  63  VAL A CB    
523  C  CG1   . VAL A 63  ? 1.0787 1.3727 0.8876 0.0236  -0.1544 0.0958  63  VAL A CG1   
524  C  CG2   . VAL A 63  ? 1.2017 1.4757 0.9623 0.0353  -0.1290 0.0931  63  VAL A CG2   
525  N  N     . THR A 64  ? 1.1354 1.4397 0.9234 0.0545  -0.1167 0.1496  64  THR A N     
526  C  CA    . THR A 64  ? 1.2035 1.5073 0.9718 0.0633  -0.1039 0.1615  64  THR A CA    
527  C  C     . THR A 64  ? 1.1187 1.4123 0.9111 0.0659  -0.0851 0.1632  64  THR A C     
528  O  O     . THR A 64  ? 1.2161 1.5075 1.0452 0.0629  -0.0831 0.1631  64  THR A O     
529  C  CB    . THR A 64  ? 1.0650 1.3859 0.8364 0.0693  -0.1088 0.1857  64  THR A CB    
530  O  OG1   . THR A 64  ? 0.9277 1.2525 0.7437 0.0711  -0.1024 0.1995  64  THR A OG1   
531  C  CG2   . THR A 64  ? 1.0436 1.3776 0.8038 0.0653  -0.1308 0.1865  64  THR A CG2   
532  N  N     . VAL A 65  ? 0.9822 1.2694 0.7534 0.0716  -0.0714 0.1651  65  VAL A N     
533  C  CA    . VAL A 65  ? 0.9693 1.2500 0.7646 0.0746  -0.0545 0.1720  65  VAL A CA    
534  C  C     . VAL A 65  ? 1.0310 1.3223 0.8547 0.0787  -0.0531 0.1950  65  VAL A C     
535  O  O     . VAL A 65  ? 1.0800 1.3826 0.8896 0.0847  -0.0539 0.2118  65  VAL A O     
536  C  CB    . VAL A 65  ? 1.1240 1.3985 0.8919 0.0807  -0.0400 0.1719  65  VAL A CB    
537  C  CG1   . VAL A 65  ? 0.9439 1.2143 0.7409 0.0834  -0.0240 0.1824  65  VAL A CG1   
538  C  CG2   . VAL A 65  ? 1.0131 1.2747 0.7553 0.0771  -0.0407 0.1483  65  VAL A CG2   
539  N  N     . LYS A 66  ? 0.8081 1.0951 0.6709 0.0757  -0.0512 0.1959  66  LYS A N     
540  C  CA    . LYS A 66  ? 0.7283 1.0222 0.6208 0.0794  -0.0496 0.2165  66  LYS A CA    
541  C  C     . LYS A 66  ? 0.9279 1.2217 0.8205 0.0857  -0.0355 0.2331  66  LYS A C     
542  O  O     . LYS A 66  ? 1.0216 1.3270 0.9016 0.0918  -0.0352 0.2508  66  LYS A O     
543  C  CB    . LYS A 66  ? 0.7707 1.0560 0.7017 0.0753  -0.0494 0.2114  66  LYS A CB    
544  C  CG    . LYS A 66  ? 0.8331 1.1206 0.7964 0.0794  -0.0459 0.2311  66  LYS A CG    
545  C  CD    . LYS A 66  ? 0.6977 0.9773 0.6938 0.0763  -0.0483 0.2249  66  LYS A CD    
546  C  CE    . LYS A 66  ? 0.8785 1.1401 0.8819 0.0715  -0.0412 0.2082  66  LYS A CE    
547  N  NZ    . LYS A 66  ? 0.8857 1.1358 0.9228 0.0713  -0.0382 0.2097  66  LYS A NZ    
548  N  N     . ARG A 67  ? 0.9111 1.1927 0.8182 0.0842  -0.0241 0.2284  67  ARG A N     
549  C  CA    . ARG A 67  ? 0.9105 1.1920 0.8236 0.0892  -0.0103 0.2445  67  ARG A CA    
550  C  C     . ARG A 67  ? 0.9280 1.1998 0.8296 0.0880  0.0001  0.2323  67  ARG A C     
551  O  O     . ARG A 67  ? 0.9515 1.2141 0.8476 0.0827  -0.0032 0.2115  67  ARG A O     
552  C  CB    . ARG A 67  ? 0.7845 1.0617 0.7403 0.0885  -0.0071 0.2576  67  ARG A CB    
553  C  CG    . ARG A 67  ? 0.8323 1.0951 0.8127 0.0815  -0.0106 0.2415  67  ARG A CG    
554  C  CD    . ARG A 67  ? 0.8391 1.0952 0.8579 0.0814  -0.0087 0.2535  67  ARG A CD    
555  N  NE    . ARG A 67  ? 0.8814 1.1279 0.9159 0.0799  0.0013  0.2575  67  ARG A NE    
556  C  CZ    . ARG A 67  ? 0.9197 1.1502 0.9774 0.0745  0.0017  0.2485  67  ARG A CZ    
557  N  NH1   . ARG A 67  ? 0.8393 1.0608 0.9060 0.0710  -0.0055 0.2347  67  ARG A NH1   
558  N  NH2   . ARG A 67  ? 0.9553 1.1791 1.0275 0.0727  0.0093  0.2541  67  ARG A NH2   
559  N  N     . VAL A 68  ? 1.0446 1.3194 0.9445 0.0935  0.0133  0.2470  68  VAL A N     
560  C  CA    . VAL A 68  ? 0.9291 1.1972 0.8211 0.0943  0.0253  0.2402  68  VAL A CA    
561  C  C     . VAL A 68  ? 0.9617 1.2285 0.8881 0.0949  0.0363  0.2573  68  VAL A C     
562  O  O     . VAL A 68  ? 1.0581 1.3307 1.0058 0.0968  0.0363  0.2766  68  VAL A O     
563  C  CB    . VAL A 68  ? 0.9193 1.1934 0.7677 0.1019  0.0321  0.2409  68  VAL A CB    
564  C  CG1   . VAL A 68  ? 0.8934 1.1657 0.7078 0.0996  0.0195  0.2215  68  VAL A CG1   
565  C  CG2   . VAL A 68  ? 1.1239 1.4118 0.9658 0.1102  0.0377  0.2665  68  VAL A CG2   
566  N  N     . GLU A 69  ? 1.0108 1.2701 0.9446 0.0931  0.0451  0.2508  69  GLU A N     
567  C  CA    . GLU A 69  ? 0.9668 1.2243 0.9368 0.0920  0.0536  0.2658  69  GLU A CA    
568  C  C     . GLU A 69  ? 0.9920 1.2467 0.9596 0.0931  0.0655  0.2619  69  GLU A C     
569  O  O     . GLU A 69  ? 0.9458 1.1921 0.9004 0.0899  0.0632  0.2414  69  GLU A O     
570  C  CB    . GLU A 69  ? 0.7736 1.0195 0.7787 0.0834  0.0440  0.2602  69  GLU A CB    
571  C  CG    . GLU A 69  ? 0.9583 1.1983 0.9995 0.0799  0.0500  0.2701  69  GLU A CG    
572  C  CD    . GLU A 69  ? 0.9743 1.1987 1.0423 0.0711  0.0400  0.2591  69  GLU A CD    
573  O  OE1   . GLU A 69  ? 0.8863 1.1027 0.9426 0.0671  0.0328  0.2378  69  GLU A OE1   
574  O  OE2   . GLU A 69  ? 1.0912 1.3107 1.1914 0.0684  0.0395  0.2719  69  GLU A OE2   
575  N  N     . LYS A 70  ? 1.0841 1.3464 1.0659 0.0979  0.0786  0.2830  70  LYS A N     
576  C  CA    . LYS A 70  ? 0.9220 1.1837 0.9087 0.0996  0.0915  0.2835  70  LYS A CA    
577  C  C     . LYS A 70  ? 0.8283 1.0784 0.8500 0.0898  0.0859  0.2751  70  LYS A C     
578  O  O     . LYS A 70  ? 0.9189 1.1657 0.9752 0.0841  0.0805  0.2847  70  LYS A O     
579  C  CB    . LYS A 70  ? 1.1349 1.4098 1.1322 0.1074  0.1072  0.3113  70  LYS A CB    
580  C  CG    . LYS A 70  ? 1.1543 1.4349 1.1291 0.1165  0.1243  0.3133  70  LYS A CG    
581  C  CD    . LYS A 70  ? 1.1576 1.4352 1.0807 0.1217  0.1225  0.2944  70  LYS A CD    
582  C  CE    . LYS A 70  ? 1.3476 1.6270 1.2454 0.1314  0.1400  0.2929  70  LYS A CE    
583  N  NZ    . LYS A 70  ? 1.3203 1.6141 1.2188 0.1422  0.1582  0.3205  70  LYS A NZ    
584  N  N     . VAL A 71  ? 0.8308 1.0738 0.8428 0.0877  0.0868  0.2572  71  VAL A N     
585  C  CA    . VAL A 71  ? 0.8209 1.0532 0.8620 0.0789  0.0817  0.2490  71  VAL A CA    
586  C  C     . VAL A 71  ? 0.8914 1.1267 0.9356 0.0822  0.0946  0.2513  71  VAL A C     
587  O  O     . VAL A 71  ? 0.9335 1.1723 0.9468 0.0900  0.1041  0.2461  71  VAL A O     
588  C  CB    . VAL A 71  ? 0.7121 0.9314 0.7421 0.0719  0.0679  0.2236  71  VAL A CB    
589  C  CG1   . VAL A 71  ? 0.9264 1.1342 0.9866 0.0626  0.0613  0.2172  71  VAL A CG1   
590  C  CG2   . VAL A 71  ? 0.9649 1.1839 0.9878 0.0708  0.0572  0.2216  71  VAL A CG2   
591  N  N     . GLN A 72  ? 0.8214 1.0546 0.9032 0.0764  0.0947  0.2594  72  GLN A N     
592  C  CA    . GLN A 72  ? 0.8791 1.1144 0.9711 0.0779  0.1044  0.2606  72  GLN A CA    
593  C  C     . GLN A 72  ? 0.7965 1.0180 0.8985 0.0682  0.0923  0.2415  72  GLN A C     
594  O  O     . GLN A 72  ? 0.8251 1.0390 0.9545 0.0589  0.0807  0.2421  72  GLN A O     
595  C  CB    . GLN A 72  ? 0.8899 1.1359 1.0201 0.0786  0.1137  0.2871  72  GLN A CB    
596  C  CG    . GLN A 72  ? 1.0595 1.3101 1.2047 0.0808  0.1246  0.2914  72  GLN A CG    
597  C  CD    . GLN A 72  ? 1.1408 1.3989 1.3357 0.0763  0.1268  0.3148  72  GLN A CD    
598  O  OE1   . GLN A 72  ? 1.0428 1.3015 1.2624 0.0726  0.1275  0.3165  72  GLN A OE1   
599  N  NE2   . GLN A 72  ? 1.1098 1.3739 1.3214 0.0761  0.1271  0.3339  72  GLN A NE2   
600  N  N     . LYS A 73  ? 0.8767 1.0938 0.9548 0.0705  0.0948  0.2244  73  LYS A N     
601  C  CA    . LYS A 73  ? 0.9239 1.1289 1.0082 0.0625  0.0849  0.2068  73  LYS A CA    
602  C  C     . LYS A 73  ? 0.9578 1.1657 1.0487 0.0659  0.0955  0.2082  73  LYS A C     
603  O  O     . LYS A 73  ? 0.8523 1.0705 0.9370 0.0756  0.1115  0.2196  73  LYS A O     
604  C  CB    . LYS A 73  ? 0.8130 1.0083 0.8648 0.0610  0.0760  0.1836  73  LYS A CB    
605  C  CG    . LYS A 73  ? 0.8421 1.0362 0.8867 0.0590  0.0665  0.1826  73  LYS A CG    
606  C  CD    . LYS A 73  ? 0.7840 0.9698 0.8023 0.0566  0.0573  0.1608  73  LYS A CD    
607  C  CE    . LYS A 73  ? 0.7181 0.8912 0.7518 0.0471  0.0452  0.1486  73  LYS A CE    
608  N  NZ    . LYS A 73  ? 0.7555 0.9255 0.8120 0.0425  0.0373  0.1568  73  LYS A NZ    
609  N  N     . LYS A 74  ? 0.9107 1.1095 1.0140 0.0585  0.0870  0.1970  74  LYS A N     
610  C  CA    . LYS A 74  ? 0.9977 1.1985 1.1110 0.0608  0.0951  0.1979  74  LYS A CA    
611  C  C     . LYS A 74  ? 0.9850 1.1777 1.0644 0.0645  0.0972  0.1770  74  LYS A C     
612  O  O     . LYS A 74  ? 0.9987 1.1799 1.0673 0.0579  0.0847  0.1593  74  LYS A O     
613  C  CB    . LYS A 74  ? 1.0821 1.2782 1.2307 0.0503  0.0838  0.2000  74  LYS A CB    
614  C  CG    . LYS A 74  ? 1.0495 1.2463 1.2275 0.0429  0.0746  0.2137  74  LYS A CG    
615  C  CD    . LYS A 74  ? 1.1634 1.3532 1.3727 0.0318  0.0612  0.2139  74  LYS A CD    
616  C  CE    . LYS A 74  ? 1.1804 1.3746 1.4006 0.0334  0.0669  0.2150  74  LYS A CE    
617  N  NZ    . LYS A 74  ? 1.2345 1.4176 1.4692 0.0224  0.0505  0.2062  74  LYS A NZ    
618  N  N     . PHE A 75  ? 0.9630 1.1610 1.0256 0.0754  0.1134  0.1794  75  PHE A N     
619  C  CA    . PHE A 75  ? 0.8390 1.0279 0.8693 0.0799  0.1169  0.1603  75  PHE A CA    
620  C  C     . PHE A 75  ? 0.9927 1.1852 1.0325 0.0876  0.1322  0.1664  75  PHE A C     
621  O  O     . PHE A 75  ? 1.1065 1.3106 1.1551 0.0962  0.1475  0.1843  75  PHE A O     
622  C  CB    . PHE A 75  ? 0.9299 1.1182 0.9194 0.0871  0.1210  0.1537  75  PHE A CB    
623  C  CG    . PHE A 75  ? 0.9683 1.1440 0.9239 0.0887  0.1194  0.1311  75  PHE A CG    
624  C  CD1   . PHE A 75  ? 0.9631 1.1282 0.9156 0.0791  0.1038  0.1139  75  PHE A CD1   
625  C  CD2   . PHE A 75  ? 0.9059 1.0795 0.8327 0.1000  0.1338  0.1273  75  PHE A CD2   
626  C  CE1   . PHE A 75  ? 0.7879 0.9414 0.7121 0.0798  0.1017  0.0942  75  PHE A CE1   
627  C  CE2   . PHE A 75  ? 0.9321 1.0920 0.8283 0.1008  0.1312  0.1060  75  PHE A CE2   
628  C  CZ    . PHE A 75  ? 0.8656 1.0159 0.7621 0.0902  0.1148  0.0899  75  PHE A CZ    
629  N  N     . LEU A 76  ? 0.9345 1.1173 0.9736 0.0851  0.1290  0.1527  76  LEU A N     
630  C  CA    . LEU A 76  ? 1.0566 1.2416 1.1081 0.0920  0.1425  0.1577  76  LEU A CA    
631  C  C     . LEU A 76  ? 1.0165 1.2150 1.1144 0.0899  0.1452  0.1806  76  LEU A C     
632  O  O     . LEU A 76  ? 1.0370 1.2442 1.1490 0.0989  0.1615  0.1937  76  LEU A O     
633  C  CB    . LEU A 76  ? 1.0746 1.2600 1.0958 0.1069  0.1623  0.1572  76  LEU A CB    
634  C  CG    . LEU A 76  ? 1.2384 1.4088 1.2130 0.1100  0.1607  0.1339  76  LEU A CG    
635  C  CD1   . LEU A 76  ? 0.9032 1.0715 0.8514 0.1255  0.1817  0.1337  76  LEU A CD1   
636  C  CD2   . LEU A 76  ? 1.1958 1.3527 1.1712 0.1015  0.1482  0.1155  76  LEU A CD2   
637  N  N     . GLY A 77  ? 0.9795 1.1793 1.1020 0.0782  0.1294  0.1860  77  GLY A N     
638  C  CA    . GLY A 77  ? 1.0870 1.2982 1.2551 0.0739  0.1283  0.2069  77  GLY A CA    
639  C  C     . GLY A 77  ? 1.0975 1.3238 1.2810 0.0796  0.1400  0.2300  77  GLY A C     
640  O  O     . GLY A 77  ? 1.1246 1.3611 1.3496 0.0751  0.1383  0.2491  77  GLY A O     
641  N  N     . ARG A 78  ? 1.0825 1.3111 1.2348 0.0891  0.1514  0.2297  78  ARG A N     
642  C  CA    . ARG A 78  ? 1.1544 1.3975 1.3190 0.0949  0.1629  0.2525  78  ARG A CA    
643  C  C     . ARG A 78  ? 1.1951 1.4349 1.3361 0.0929  0.1553  0.2485  78  ARG A C     
644  O  O     . ARG A 78  ? 1.1651 1.3941 1.2679 0.0934  0.1499  0.2283  78  ARG A O     
645  C  CB    . ARG A 78  ? 1.1654 1.4175 1.3156 0.1116  0.1883  0.2617  78  ARG A CB    
646  C  CG    . ARG A 78  ? 1.2504 1.5087 1.4299 0.1155  0.1987  0.2705  78  ARG A CG    
647  C  CD    . ARG A 78  ? 1.2890 1.5602 1.4656 0.1325  0.2263  0.2877  78  ARG A CD    
648  N  NE    . ARG A 78  ? 1.3876 1.6654 1.5918 0.1383  0.2387  0.2966  78  ARG A NE    
649  C  CZ    . ARG A 78  ? 1.4139 1.6995 1.6678 0.1295  0.2303  0.3087  78  ARG A CZ    
650  N  NH1   . ARG A 78  ? 1.4025 1.6898 1.6859 0.1141  0.2099  0.3144  78  ARG A NH1   
651  N  NH2   . ARG A 78  ? 1.2140 1.5054 1.4889 0.1365  0.2427  0.3157  78  ARG A NH2   
652  N  N     . PRO A 79  ? 1.1194 1.3688 1.2844 0.0903  0.1544  0.2681  79  PRO A N     
653  C  CA    . PRO A 79  ? 0.9562 1.2027 1.1029 0.0881  0.1463  0.2659  79  PRO A CA    
654  C  C     . PRO A 79  ? 1.0164 1.2663 1.1199 0.1010  0.1601  0.2642  79  PRO A C     
655  O  O     . PRO A 79  ? 1.1321 1.3943 1.2353 0.1121  0.1789  0.2814  79  PRO A O     
656  C  CB    . PRO A 79  ? 0.8130 1.0697 1.0016 0.0833  0.1447  0.2908  79  PRO A CB    
657  C  CG    . PRO A 79  ? 0.9400 1.2025 1.1709 0.0794  0.1464  0.3024  79  PRO A CG    
658  C  CD    . PRO A 79  ? 0.9472 1.2108 1.1600 0.0890  0.1603  0.2945  79  PRO A CD    
659  N  N     . VAL A 80  ? 1.0491 1.2883 1.1157 0.0997  0.1504  0.2437  80  VAL A N     
660  C  CA    . VAL A 80  ? 1.0249 1.2649 1.0463 0.1101  0.1589  0.2390  80  VAL A CA    
661  C  C     . VAL A 80  ? 1.0160 1.2573 1.0298 0.1064  0.1478  0.2420  80  VAL A C     
662  O  O     . VAL A 80  ? 0.8835 1.1189 0.9155 0.0954  0.1313  0.2371  80  VAL A O     
663  C  CB    . VAL A 80  ? 1.0864 1.3128 1.0704 0.1119  0.1566  0.2125  80  VAL A CB    
664  C  CG1   . VAL A 80  ? 1.0958 1.3214 1.0308 0.1222  0.1638  0.2067  80  VAL A CG1   
665  C  CG2   . VAL A 80  ? 1.1044 1.3286 1.1001 0.1154  0.1671  0.2102  80  VAL A CG2   
666  N  N     . GLU A 81  ? 1.2231 1.4719 1.2094 0.1163  0.1575  0.2508  81  GLU A N     
667  C  CA    . GLU A 81  ? 1.1225 1.3742 1.0989 0.1145  0.1482  0.2554  81  GLU A CA    
668  C  C     . GLU A 81  ? 1.0412 1.2829 0.9757 0.1136  0.1371  0.2317  81  GLU A C     
669  O  O     . GLU A 81  ? 0.9185 1.1579 0.8137 0.1221  0.1448  0.2229  81  GLU A O     
670  C  CB    . GLU A 81  ? 1.1032 1.3694 1.0724 0.1256  0.1637  0.2795  81  GLU A CB    
671  C  CG    . GLU A 81  ? 1.1292 1.4031 1.1250 0.1213  0.1574  0.2989  81  GLU A CG    
672  C  CD    . GLU A 81  ? 1.2769 1.5650 1.2591 0.1328  0.1721  0.3220  81  GLU A CD    
673  O  OE1   . GLU A 81  ? 1.3368 1.6261 1.2747 0.1435  0.1819  0.3170  81  GLU A OE1   
674  O  OE2   . GLU A 81  ? 1.3463 1.6436 1.3614 0.1312  0.1738  0.3454  81  GLU A OE2   
675  N  N     . VAL A 82  ? 0.9556 1.1907 0.8987 0.1034  0.1189  0.2216  82  VAL A N     
676  C  CA    . VAL A 82  ? 1.0400 1.2665 0.9512 0.1006  0.1064  0.1998  82  VAL A CA    
677  C  C     . VAL A 82  ? 0.9380 1.1696 0.8469 0.0986  0.0956  0.2063  82  VAL A C     
678  O  O     . VAL A 82  ? 1.0095 1.2469 0.9477 0.0964  0.0944  0.2234  82  VAL A O     
679  C  CB    . VAL A 82  ? 0.9279 1.1415 0.8506 0.0907  0.0951  0.1795  82  VAL A CB    
680  C  CG1   . VAL A 82  ? 0.9314 1.1426 0.8851 0.0809  0.0814  0.1816  82  VAL A CG1   
681  C  CG2   . VAL A 82  ? 1.0336 1.2385 0.9194 0.0904  0.0880  0.1568  82  VAL A CG2   
682  N  N     . TRP A 83  ? 1.0009 1.2300 0.8756 0.0992  0.0871  0.1927  83  TRP A N     
683  C  CA    . TRP A 83  ? 0.9971 1.2323 0.8655 0.0984  0.0766  0.1986  83  TRP A CA    
684  C  C     . TRP A 83  ? 0.9621 1.1893 0.8388 0.0886  0.0595  0.1820  83  TRP A C     
685  O  O     . TRP A 83  ? 0.9024 1.1213 0.7607 0.0856  0.0540  0.1618  83  TRP A O     
686  C  CB    . TRP A 83  ? 0.9381 1.1781 0.7609 0.1066  0.0786  0.1978  83  TRP A CB    
687  C  CG    . TRP A 83  ? 1.1831 1.4356 0.9981 0.1166  0.0912  0.2214  83  TRP A CG    
688  C  CD1   . TRP A 83  ? 1.2118 1.4669 0.9966 0.1274  0.1066  0.2258  83  TRP A CD1   
689  C  CD2   . TRP A 83  ? 1.2327 1.4965 1.0687 0.1176  0.0903  0.2442  83  TRP A CD2   
690  N  NE1   . TRP A 83  ? 1.2418 1.5102 1.0272 0.1351  0.1157  0.2507  83  TRP A NE1   
691  C  CE2   . TRP A 83  ? 1.2850 1.5591 1.1023 0.1289  0.1055  0.2626  83  TRP A CE2   
692  C  CE3   . TRP A 83  ? 1.1472 1.4125 1.0153 0.1106  0.0789  0.2511  83  TRP A CE3   
693  C  CZ2   . TRP A 83  ? 1.2017 1.4883 1.0333 0.1327  0.1090  0.2886  83  TRP A CZ2   
694  C  CZ3   . TRP A 83  ? 1.1709 1.4475 1.0534 0.1145  0.0821  0.2758  83  TRP A CZ3   
695  C  CH2   . TRP A 83  ? 1.1847 1.4722 1.0500 0.1251  0.0968  0.2948  83  TRP A CH2   
696  N  N     . LYS A 84  ? 0.8895 1.1188 0.7940 0.0841  0.0519  0.1910  84  LYS A N     
697  C  CA    . LYS A 84  ? 0.8563 1.0790 0.7713 0.0762  0.0374  0.1777  84  LYS A CA    
698  C  C     . LYS A 84  ? 0.8106 1.0406 0.7067 0.0777  0.0274  0.1782  84  LYS A C     
699  O  O     . LYS A 84  ? 0.9032 1.1433 0.8006 0.0823  0.0286  0.1961  84  LYS A O     
700  C  CB    . LYS A 84  ? 0.8578 1.0762 0.8129 0.0710  0.0350  0.1860  84  LYS A CB    
701  C  CG    . LYS A 84  ? 0.7462 0.9549 0.7135 0.0635  0.0231  0.1713  84  LYS A CG    
702  C  CD    . LYS A 84  ? 0.6496 0.8516 0.6528 0.0595  0.0214  0.1797  84  LYS A CD    
703  C  CE    . LYS A 84  ? 0.7040 0.8930 0.7177 0.0526  0.0129  0.1631  84  LYS A CE    
704  N  NZ    . LYS A 84  ? 0.7367 0.9166 0.7810 0.0492  0.0102  0.1699  84  LYS A NZ    
705  N  N     . LEU A 85  ? 0.8410 1.0666 0.7213 0.0735  0.0172  0.1599  85  LEU A N     
706  C  CA    . LEU A 85  ? 0.8540 1.0872 0.7155 0.0739  0.0059  0.1587  85  LEU A CA    
707  C  C     . LEU A 85  ? 0.8743 1.1057 0.7601 0.0675  -0.0057 0.1539  85  LEU A C     
708  O  O     . LEU A 85  ? 0.8011 1.0239 0.6908 0.0616  -0.0103 0.1372  85  LEU A O     
709  C  CB    . LEU A 85  ? 0.8034 1.0334 0.6272 0.0742  0.0025  0.1421  85  LEU A CB    
710  C  CG    . LEU A 85  ? 0.8032 1.0321 0.5993 0.0817  0.0156  0.1441  85  LEU A CG    
711  C  CD1   . LEU A 85  ? 0.7859 1.0094 0.5413 0.0821  0.0101  0.1270  85  LEU A CD1   
712  C  CD2   . LEU A 85  ? 0.8076 1.0485 0.5998 0.0899  0.0231  0.1672  85  LEU A CD2   
713  N  N     . TYR A 86  ? 0.7998 1.0393 0.7020 0.0694  -0.0094 0.1693  86  TYR A N     
714  C  CA    . TYR A 86  ? 0.8250 1.0633 0.7513 0.0652  -0.0185 0.1671  86  TYR A CA    
715  C  C     . TYR A 86  ? 0.7997 1.0472 0.7108 0.0642  -0.0313 0.1624  86  TYR A C     
716  O  O     . TYR A 86  ? 0.9067 1.1644 0.7938 0.0681  -0.0344 0.1694  86  TYR A O     
717  C  CB    . TYR A 86  ? 0.7186 0.9594 0.6732 0.0681  -0.0159 0.1862  86  TYR A CB    
718  C  CG    . TYR A 86  ? 0.7652 0.9948 0.7441 0.0666  -0.0071 0.1894  86  TYR A CG    
719  C  CD1   . TYR A 86  ? 0.8075 1.0240 0.8078 0.0613  -0.0093 0.1788  86  TYR A CD1   
720  C  CD2   . TYR A 86  ? 0.7308 0.9631 0.7114 0.0704  0.0031  0.2038  86  TYR A CD2   
721  C  CE1   . TYR A 86  ? 0.7896 0.9949 0.8109 0.0590  -0.0035 0.1813  86  TYR A CE1   
722  C  CE2   . TYR A 86  ? 0.6664 0.8891 0.6719 0.0679  0.0094  0.2076  86  TYR A CE2   
723  C  CZ    . TYR A 86  ? 0.7780 0.9868 0.8032 0.0618  0.0050  0.1958  86  TYR A CZ    
724  O  OH    . TYR A 86  ? 0.9370 1.1353 0.9858 0.0585  0.0091  0.1991  86  TYR A OH    
725  N  N     . PHE A 87  ? 0.7688 1.0129 0.6942 0.0590  -0.0389 0.1515  87  PHE A N     
726  C  CA    . PHE A 87  ? 0.8320 1.0854 0.7498 0.0567  -0.0520 0.1474  87  PHE A CA    
727  C  C     . PHE A 87  ? 0.7892 1.0454 0.7391 0.0562  -0.0564 0.1531  87  PHE A C     
728  O  O     . PHE A 87  ? 0.8051 1.0522 0.7793 0.0567  -0.0496 0.1555  87  PHE A O     
729  C  CB    . PHE A 87  ? 0.7218 0.9688 0.6228 0.0507  -0.0567 0.1265  87  PHE A CB    
730  C  CG    . PHE A 87  ? 0.9003 1.1426 0.7684 0.0521  -0.0520 0.1194  87  PHE A CG    
731  C  CD1   . PHE A 87  ? 0.7780 1.0084 0.6464 0.0524  -0.0400 0.1138  87  PHE A CD1   
732  C  CD2   . PHE A 87  ? 0.9453 1.1945 0.7818 0.0534  -0.0596 0.1187  87  PHE A CD2   
733  C  CE1   . PHE A 87  ? 0.7828 1.0088 0.6224 0.0550  -0.0339 0.1079  87  PHE A CE1   
734  C  CE2   . PHE A 87  ? 1.0304 1.2731 0.8342 0.0560  -0.0538 0.1114  87  PHE A CE2   
735  C  CZ    . PHE A 87  ? 0.8840 1.1152 0.6902 0.0572  -0.0401 0.1063  87  PHE A CZ    
736  N  N     . THR A 88  ? 0.8242 1.0928 0.7739 0.0554  -0.0683 0.1554  88  THR A N     
737  C  CA    . THR A 88  ? 0.7035 0.9764 0.6843 0.0560  -0.0719 0.1616  88  THR A CA    
738  C  C     . THR A 88  ? 0.7153 0.9788 0.7099 0.0508  -0.0714 0.1456  88  THR A C     
739  O  O     . THR A 88  ? 0.6850 0.9403 0.7043 0.0523  -0.0655 0.1465  88  THR A O     
740  C  CB    . THR A 88  ? 0.6992 0.9908 0.6783 0.0571  -0.0851 0.1718  88  THR A CB    
741  O  OG1   . THR A 88  ? 0.7223 1.0226 0.6873 0.0626  -0.0850 0.1882  88  THR A OG1   
742  C  CG2   . THR A 88  ? 0.7074 1.0043 0.7215 0.0590  -0.0874 0.1797  88  THR A CG2   
743  N  N     . HIS A 89  ? 0.7053 0.9687 0.6833 0.0450  -0.0773 0.1309  89  HIS A N     
744  C  CA    . HIS A 89  ? 0.7590 1.0163 0.7495 0.0400  -0.0780 0.1173  89  HIS A CA    
745  C  C     . HIS A 89  ? 0.7252 0.9700 0.6959 0.0351  -0.0745 0.1004  89  HIS A C     
746  O  O     . HIS A 89  ? 0.8025 1.0476 0.7462 0.0345  -0.0764 0.0971  89  HIS A O     
747  C  CB    . HIS A 89  ? 0.8615 1.1338 0.8590 0.0368  -0.0911 0.1180  89  HIS A CB    
748  C  CG    . HIS A 89  ? 0.6894 0.9596 0.7117 0.0343  -0.0898 0.1119  89  HIS A CG    
749  N  ND1   . HIS A 89  ? 0.6484 0.9111 0.6660 0.0280  -0.0898 0.0961  89  HIS A ND1   
750  C  CD2   . HIS A 89  ? 0.7193 0.9933 0.7710 0.0382  -0.0871 0.1200  89  HIS A CD2   
751  C  CE1   . HIS A 89  ? 0.7606 1.0237 0.8032 0.0280  -0.0871 0.0954  89  HIS A CE1   
752  N  NE2   . HIS A 89  ? 0.8133 1.0829 0.8764 0.0344  -0.0850 0.1093  89  HIS A NE2   
753  N  N     . PRO A 90  ? 0.7445 0.9776 0.7271 0.0323  -0.0687 0.0899  90  PRO A N     
754  C  CA    . PRO A 90  ? 0.7164 0.9378 0.6822 0.0278  -0.0654 0.0747  90  PRO A CA    
755  C  C     . PRO A 90  ? 0.8510 1.0771 0.7979 0.0227  -0.0753 0.0652  90  PRO A C     
756  O  O     . PRO A 90  ? 0.9000 1.1193 0.8230 0.0216  -0.0737 0.0573  90  PRO A O     
757  C  CB    . PRO A 90  ? 0.7284 0.9393 0.7131 0.0258  -0.0598 0.0673  90  PRO A CB    
758  C  CG    . PRO A 90  ? 0.7501 0.9623 0.7576 0.0307  -0.0565 0.0785  90  PRO A CG    
759  C  CD    . PRO A 90  ? 0.6604 0.8887 0.6702 0.0341  -0.0636 0.0920  90  PRO A CD    
760  N  N     . GLN A 91  ? 0.8240 1.0612 0.7818 0.0195  -0.0856 0.0661  91  GLN A N     
761  C  CA    . GLN A 91  ? 0.7297 0.9705 0.6714 0.0132  -0.0973 0.0569  91  GLN A CA    
762  C  C     . GLN A 91  ? 0.7915 1.0372 0.7038 0.0150  -0.1041 0.0600  91  GLN A C     
763  O  O     . GLN A 91  ? 0.9054 1.1505 0.7981 0.0099  -0.1142 0.0505  91  GLN A O     
764  C  CB    . GLN A 91  ? 0.8601 1.1139 0.8248 0.0092  -0.1077 0.0599  91  GLN A CB    
765  C  CG    . GLN A 91  ? 0.7551 1.0075 0.7510 0.0109  -0.0993 0.0626  91  GLN A CG    
766  C  CD    . GLN A 91  ? 0.9879 1.2450 1.0007 0.0045  -0.1049 0.0569  91  GLN A CD    
767  O  OE1   . GLN A 91  ? 1.3606 1.6110 1.3619 -0.0020 -0.1084 0.0445  91  GLN A OE1   
768  N  NE2   . GLN A 91  ? 0.8558 1.1244 0.8976 0.0068  -0.1053 0.0666  91  GLN A NE2   
769  N  N     . ASP A 92  ? 0.7859 1.0356 0.6938 0.0220  -0.0990 0.0730  92  ASP A N     
770  C  CA    . ASP A 92  ? 0.9272 1.1796 0.8028 0.0249  -0.1026 0.0759  92  ASP A CA    
771  C  C     . ASP A 92  ? 0.9840 1.2210 0.8327 0.0250  -0.0946 0.0628  92  ASP A C     
772  O  O     . ASP A 92  ? 1.1356 1.3701 0.9535 0.0237  -0.1011 0.0550  92  ASP A O     
773  C  CB    . ASP A 92  ? 0.9988 1.2591 0.8787 0.0330  -0.0970 0.0947  92  ASP A CB    
774  C  CG    . ASP A 92  ? 1.0681 1.3445 0.9711 0.0341  -0.1059 0.1091  92  ASP A CG    
775  O  OD1   . ASP A 92  ? 1.0243 1.3097 0.9309 0.0289  -0.1196 0.1060  92  ASP A OD1   
776  O  OD2   . ASP A 92  ? 0.9492 1.2295 0.8687 0.0401  -0.0994 0.1242  92  ASP A OD2   
777  N  N     . GLN A 93  ? 0.8178 1.0438 0.6778 0.0265  -0.0810 0.0600  93  GLN A N     
778  C  CA    . GLN A 93  ? 0.8069 1.0196 0.6460 0.0282  -0.0710 0.0510  93  GLN A CA    
779  C  C     . GLN A 93  ? 0.9405 1.1445 0.7561 0.0232  -0.0774 0.0337  93  GLN A C     
780  O  O     . GLN A 93  ? 0.9508 1.1497 0.7350 0.0266  -0.0753 0.0298  93  GLN A O     
781  C  CB    . GLN A 93  ? 0.7553 0.9584 0.6165 0.0284  -0.0588 0.0500  93  GLN A CB    
782  C  CG    . GLN A 93  ? 0.7104 0.9185 0.5960 0.0325  -0.0533 0.0654  93  GLN A CG    
783  C  CD    . GLN A 93  ? 0.7880 0.9848 0.6879 0.0331  -0.0417 0.0645  93  GLN A CD    
784  O  OE1   . GLN A 93  ? 0.9174 1.1053 0.8056 0.0328  -0.0354 0.0565  93  GLN A OE1   
785  N  NE2   . GLN A 93  ? 0.7317 0.9283 0.6571 0.0339  -0.0393 0.0726  93  GLN A NE2   
786  N  N     . PRO A 94  ? 0.9038 1.1048 0.7321 0.0156  -0.0846 0.0230  94  PRO A N     
787  C  CA    . PRO A 94  ? 0.9254 1.1163 0.7315 0.0105  -0.0911 0.0065  94  PRO A CA    
788  C  C     . PRO A 94  ? 1.0097 1.2061 0.7889 0.0092  -0.1055 0.0053  94  PRO A C     
789  O  O     . PRO A 94  ? 1.0634 1.2481 0.8126 0.0082  -0.1082 -0.0075 94  PRO A O     
790  C  CB    . PRO A 94  ? 0.8085 0.9979 0.6407 0.0024  -0.0960 -0.0007 94  PRO A CB    
791  C  CG    . PRO A 94  ? 0.7655 0.9690 0.6276 0.0032  -0.0975 0.0128  94  PRO A CG    
792  C  CD    . PRO A 94  ? 0.8410 1.0469 0.7036 0.0116  -0.0867 0.0255  94  PRO A CD    
793  N  N     . ALA A 95  ? 0.9622 1.1751 0.7505 0.0096  -0.1151 0.0181  95  ALA A N     
794  C  CA    . ALA A 95  ? 1.0505 1.2703 0.8132 0.0082  -0.1307 0.0187  95  ALA A CA    
795  C  C     . ALA A 95  ? 1.1005 1.3180 0.8269 0.0169  -0.1245 0.0234  95  ALA A C     
796  O  O     . ALA A 95  ? 1.1514 1.3697 0.8463 0.0163  -0.1366 0.0204  95  ALA A O     
797  C  CB    . ALA A 95  ? 1.0502 1.2903 0.8380 0.0062  -0.1429 0.0331  95  ALA A CB    
798  N  N     . ILE A 96  ? 1.0831 1.2977 0.8126 0.0249  -0.1065 0.0312  96  ILE A N     
799  C  CA    . ILE A 96  ? 1.0739 1.2885 0.7728 0.0342  -0.0983 0.0387  96  ILE A CA    
800  C  C     . ILE A 96  ? 1.0787 1.2777 0.7636 0.0395  -0.0804 0.0313  96  ILE A C     
801  O  O     . ILE A 96  ? 1.1038 1.2990 0.7551 0.0471  -0.0736 0.0327  96  ILE A O     
802  C  CB    . ILE A 96  ? 1.0093 1.2398 0.7271 0.0403  -0.0938 0.0614  96  ILE A CB    
803  C  CG1   . ILE A 96  ? 1.0295 1.2610 0.7188 0.0505  -0.0831 0.0720  96  ILE A CG1   
804  C  CG2   . ILE A 96  ? 1.0470 1.2768 0.8054 0.0401  -0.0826 0.0670  96  ILE A CG2   
805  C  CD1   . ILE A 96  ? 0.9915 1.2383 0.6999 0.0561  -0.0793 0.0955  96  ILE A CD1   
806  N  N     . ARG A 97  ? 1.0161 1.2062 0.7246 0.0362  -0.0726 0.0237  97  ARG A N     
807  C  CA    . ARG A 97  ? 1.0650 1.2428 0.7672 0.0417  -0.0551 0.0199  97  ARG A CA    
808  C  C     . ARG A 97  ? 1.1736 1.3379 0.8330 0.0452  -0.0531 0.0067  97  ARG A C     
809  O  O     . ARG A 97  ? 1.2166 1.3764 0.8589 0.0542  -0.0381 0.0105  97  ARG A O     
810  C  CB    . ARG A 97  ? 1.0130 1.1829 0.7450 0.0361  -0.0509 0.0121  97  ARG A CB    
811  C  CG    . ARG A 97  ? 1.0474 1.2084 0.7772 0.0272  -0.0623 -0.0055 97  ARG A CG    
812  C  CD    . ARG A 97  ? 1.0331 1.1814 0.7784 0.0248  -0.0535 -0.0149 97  ARG A CD    
813  N  NE    . ARG A 97  ? 1.0324 1.1861 0.8145 0.0196  -0.0551 -0.0107 97  ARG A NE    
814  C  CZ    . ARG A 97  ? 0.9260 1.0776 0.7219 0.0114  -0.0639 -0.0193 97  ARG A CZ    
815  N  NH1   . ARG A 97  ? 1.0138 1.1578 0.7931 0.0063  -0.0732 -0.0327 97  ARG A NH1   
816  N  NH2   . ARG A 97  ? 0.9338 1.0903 0.7609 0.0085  -0.0631 -0.0143 97  ARG A NH2   
817  N  N     . ASP A 98  ? 1.2114 1.3683 0.8534 0.0384  -0.0679 -0.0087 98  ASP A N     
818  C  CA    . ASP A 98  ? 1.1296 1.2700 0.7289 0.0415  -0.0669 -0.0236 98  ASP A CA    
819  C  C     . ASP A 98  ? 1.1733 1.3183 0.7343 0.0500  -0.0666 -0.0159 98  ASP A C     
820  O  O     . ASP A 98  ? 1.3388 1.4727 0.8676 0.0590  -0.0539 -0.0197 98  ASP A O     
821  C  CB    . ASP A 98  ? 1.2552 1.3855 0.8472 0.0308  -0.0848 -0.0419 98  ASP A CB    
822  C  CG    . ASP A 98  ? 1.3601 1.4816 0.9823 0.0240  -0.0819 -0.0514 98  ASP A CG    
823  O  OD1   . ASP A 98  ? 1.4117 1.5270 1.0445 0.0291  -0.0647 -0.0503 98  ASP A OD1   
824  O  OD2   . ASP A 98  ? 1.4362 1.5578 1.0725 0.0136  -0.0970 -0.0590 98  ASP A OD2   
825  N  N     . LYS A 99  ? 1.1996 1.3612 0.7633 0.0479  -0.0799 -0.0040 99  LYS A N     
826  C  CA    . LYS A 99  ? 1.3147 1.4827 0.8427 0.0561  -0.0803 0.0059  99  LYS A CA    
827  C  C     . LYS A 99  ? 1.2629 1.4348 0.7911 0.0683  -0.0574 0.0214  99  LYS A C     
828  O  O     . LYS A 99  ? 1.3019 1.4715 0.7917 0.0779  -0.0501 0.0250  99  LYS A O     
829  C  CB    . LYS A 99  ? 1.2597 1.4476 0.8001 0.0517  -0.0979 0.0193  99  LYS A CB    
830  C  CG    . LYS A 99  ? 1.2328 1.4196 0.7704 0.0400  -0.1223 0.0066  99  LYS A CG    
831  C  CD    . LYS A 99  ? 1.2513 1.4490 0.7605 0.0406  -0.1392 0.0142  99  LYS A CD    
832  C  CE    . LYS A 99  ? 1.2089 1.4062 0.7166 0.0280  -0.1654 0.0021  99  LYS A CE    
833  N  NZ    . LYS A 99  ? 1.3015 1.5147 0.7931 0.0274  -0.1841 0.0139  99  LYS A NZ    
834  N  N     . ILE A 100 ? 1.2070 1.3846 0.7779 0.0681  -0.0461 0.0310  100 ILE A N     
835  C  CA    . ILE A 100 ? 1.2025 1.3842 0.7797 0.0783  -0.0251 0.0465  100 ILE A CA    
836  C  C     . ILE A 100 ? 1.3111 1.4759 0.8676 0.0846  -0.0089 0.0351  100 ILE A C     
837  O  O     . ILE A 100 ? 1.4014 1.5644 0.9276 0.0955  0.0040  0.0405  100 ILE A O     
838  C  CB    . ILE A 100 ? 1.1699 1.3612 0.7990 0.0750  -0.0204 0.0594  100 ILE A CB    
839  C  CG1   . ILE A 100 ? 1.1663 1.3741 0.8132 0.0715  -0.0339 0.0729  100 ILE A CG1   
840  C  CG2   . ILE A 100 ? 1.0035 1.1971 0.6428 0.0841  0.0007  0.0740  100 ILE A CG2   
841  C  CD1   . ILE A 100 ? 1.1155 1.3335 0.8021 0.0732  -0.0257 0.0919  100 ILE A CD1   
842  N  N     . ARG A 101 ? 1.2623 1.4147 0.8348 0.0785  -0.0087 0.0198  101 ARG A N     
843  C  CA    . ARG A 101 ? 1.1846 1.3203 0.7414 0.0844  0.0064  0.0086  101 ARG A CA    
844  C  C     . ARG A 101 ? 1.3510 1.4747 0.8525 0.0921  0.0081  -0.0013 101 ARG A C     
845  O  O     . ARG A 101 ? 1.3671 1.4846 0.8495 0.1035  0.0270  0.0011  101 ARG A O     
846  C  CB    . ARG A 101 ? 1.2819 1.4048 0.8576 0.0750  0.0006  -0.0089 101 ARG A CB    
847  C  CG    . ARG A 101 ? 1.2092 1.3191 0.7892 0.0803  0.0184  -0.0147 101 ARG A CG    
848  C  CD    . ARG A 101 ? 1.1951 1.3030 0.8158 0.0714  0.0158  -0.0189 101 ARG A CD    
849  N  NE    . ARG A 101 ? 1.3445 1.4514 0.9724 0.0595  -0.0040 -0.0295 101 ARG A NE    
850  C  CZ    . ARG A 101 ? 1.3584 1.4660 1.0205 0.0508  -0.0092 -0.0320 101 ARG A CZ    
851  N  NH1   . ARG A 101 ? 1.2268 1.3352 0.9176 0.0519  0.0021  -0.0258 101 ARG A NH1   
852  N  NH2   . ARG A 101 ? 1.2617 1.3696 0.9292 0.0408  -0.0263 -0.0403 101 ARG A NH2   
853  N  N     . GLU A 102 ? 1.3624 1.4827 0.8375 0.0862  -0.0116 -0.0121 102 GLU A N     
854  C  CA    . GLU A 102 ? 1.3663 1.4723 0.7845 0.0923  -0.0133 -0.0242 102 GLU A CA    
855  C  C     . GLU A 102 ? 1.3561 1.4716 0.7451 0.1052  -0.0022 -0.0075 102 GLU A C     
856  O  O     . GLU A 102 ? 1.4020 1.5041 0.7398 0.1133  0.0015  -0.0163 102 GLU A O     
857  C  CB    . GLU A 102 ? 1.4992 1.6011 0.9001 0.0811  -0.0403 -0.0381 102 GLU A CB    
858  C  CG    . GLU A 102 ? 1.6349 1.7220 1.0523 0.0697  -0.0504 -0.0582 102 GLU A CG    
859  C  CD    . GLU A 102 ? 1.7975 1.8872 1.2134 0.0566  -0.0783 -0.0663 102 GLU A CD    
860  O  OE1   . GLU A 102 ? 1.6991 1.8057 1.1109 0.0557  -0.0901 -0.0538 102 GLU A OE1   
861  O  OE2   . GLU A 102 ? 1.8415 1.9169 1.2623 0.0473  -0.0886 -0.0841 102 GLU A OE2   
862  N  N     . HIS A 103 ? 1.3883 1.5251 0.8069 0.1075  0.0034  0.0162  103 HIS A N     
863  C  CA    . HIS A 103 ? 1.4874 1.6342 0.8826 0.1202  0.0163  0.0349  103 HIS A CA    
864  C  C     . HIS A 103 ? 1.5081 1.6449 0.8912 0.1330  0.0431  0.0352  103 HIS A C     
865  O  O     . HIS A 103 ? 1.3759 1.5102 0.7949 0.1318  0.0543  0.0349  103 HIS A O     
866  C  CB    . HIS A 103 ? 1.4599 1.6305 0.8968 0.1190  0.0168  0.0606  103 HIS A CB    
867  C  CG    . HIS A 103 ? 1.5178 1.7012 0.9335 0.1307  0.0271  0.0823  103 HIS A CG    
868  N  ND1   . HIS A 103 ? 1.4613 1.6402 0.8513 0.1447  0.0500  0.0881  103 HIS A ND1   
869  C  CD2   . HIS A 103 ? 1.5343 1.7354 0.9523 0.1309  0.0183  0.1008  103 HIS A CD2   
870  C  CE1   . HIS A 103 ? 1.4879 1.6812 0.8639 0.1529  0.0550  0.1095  103 HIS A CE1   
871  N  NE2   . HIS A 103 ? 1.5712 1.7780 0.9639 0.1446  0.0355  0.1176  103 HIS A NE2   
872  N  N     . PRO A 104 ? 1.5520 1.6823 0.8846 0.1458  0.0538  0.0358  104 PRO A N     
873  C  CA    . PRO A 104 ? 1.4929 1.6133 0.8139 0.1593  0.0810  0.0363  104 PRO A CA    
874  C  C     . PRO A 104 ? 1.5026 1.6409 0.8684 0.1650  0.1013  0.0617  104 PRO A C     
875  O  O     . PRO A 104 ? 1.5427 1.6749 0.9238 0.1709  0.1204  0.0612  104 PRO A O     
876  C  CB    . PRO A 104 ? 1.4647 1.5771 0.7193 0.1720  0.0864  0.0341  104 PRO A CB    
877  C  CG    . PRO A 104 ? 1.3869 1.4954 0.6134 0.1618  0.0572  0.0211  104 PRO A CG    
878  C  CD    . PRO A 104 ? 1.3456 1.4737 0.6252 0.1479  0.0400  0.0320  104 PRO A CD    
879  N  N     . ALA A 105 ? 1.4430 1.6028 0.8323 0.1632  0.0974  0.0844  105 ALA A N     
880  C  CA    . ALA A 105 ? 1.4463 1.6223 0.8763 0.1687  0.1162  0.1096  105 ALA A CA    
881  C  C     . ALA A 105 ? 1.3947 1.5725 0.8834 0.1586  0.1150  0.1090  105 ALA A C     
882  O  O     . ALA A 105 ? 1.4337 1.6201 0.9560 0.1629  0.1318  0.1256  105 ALA A O     
883  C  CB    . ALA A 105 ? 1.4457 1.6425 0.8830 0.1697  0.1119  0.1342  105 ALA A CB    
884  N  N     . VAL A 106 ? 1.3126 1.4829 0.8144 0.1454  0.0956  0.0912  106 VAL A N     
885  C  CA    . VAL A 106 ? 1.2528 1.4235 0.8059 0.1358  0.0931  0.0894  106 VAL A CA    
886  C  C     . VAL A 106 ? 1.2766 1.4283 0.8228 0.1356  0.0983  0.0685  106 VAL A C     
887  O  O     . VAL A 106 ? 1.2890 1.4253 0.7992 0.1343  0.0898  0.0478  106 VAL A O     
888  C  CB    . VAL A 106 ? 1.2581 1.4344 0.8346 0.1220  0.0700  0.0860  106 VAL A CB    
889  C  CG1   . VAL A 106 ? 1.0912 1.2581 0.6308 0.1172  0.0519  0.0669  106 VAL A CG1   
890  C  CG2   . VAL A 106 ? 1.2476 1.4205 0.8691 0.1124  0.0672  0.0804  106 VAL A CG2   
891  N  N     . ILE A 107 ? 1.1929 1.3455 0.7744 0.1366  0.1117  0.0745  107 ILE A N     
892  C  CA    . ILE A 107 ? 1.1417 1.2775 0.7220 0.1372  0.1182  0.0576  107 ILE A CA    
893  C  C     . ILE A 107 ? 1.1139 1.2422 0.7148 0.1228  0.0997  0.0412  107 ILE A C     
894  O  O     . ILE A 107 ? 1.2981 1.4093 0.8780 0.1203  0.0939  0.0202  107 ILE A O     
895  C  CB    . ILE A 107 ? 1.1334 1.2750 0.7448 0.1444  0.1395  0.0725  107 ILE A CB    
896  C  CG1   . ILE A 107 ? 1.2081 1.3591 0.8004 0.1592  0.1589  0.0911  107 ILE A CG1   
897  C  CG2   . ILE A 107 ? 1.1660 1.2907 0.7765 0.1463  0.1472  0.0565  107 ILE A CG2   
898  C  CD1   . ILE A 107 ? 1.1996 1.3699 0.8364 0.1606  0.1693  0.1181  107 ILE A CD1   
899  N  N     . ASP A 108 ? 1.0637 1.2036 0.7054 0.1135  0.0906  0.0507  108 ASP A N     
900  C  CA    . ASP A 108 ? 1.0711 1.2056 0.7342 0.1006  0.0745  0.0376  108 ASP A CA    
901  C  C     . ASP A 108 ? 1.0328 1.1818 0.7299 0.0931  0.0645  0.0510  108 ASP A C     
902  O  O     . ASP A 108 ? 1.0205 1.1824 0.7306 0.0974  0.0713  0.0705  108 ASP A O     
903  C  CB    . ASP A 108 ? 1.1268 1.2512 0.8110 0.0993  0.0822  0.0302  108 ASP A CB    
904  C  CG    . ASP A 108 ? 1.2632 1.3760 0.9511 0.0885  0.0675  0.0109  108 ASP A CG    
905  O  OD1   . ASP A 108 ? 1.1730 1.2866 0.8509 0.0816  0.0512  0.0040  108 ASP A OD1   
906  O  OD2   . ASP A 108 ? 1.2596 1.3630 0.9617 0.0872  0.0724  0.0039  108 ASP A OD2   
907  N  N     . ILE A 109 ? 1.0603 1.2064 0.7722 0.0821  0.0489  0.0406  109 ILE A N     
908  C  CA    . ILE A 109 ? 0.8780 1.0346 0.6223 0.0750  0.0395  0.0503  109 ILE A CA    
909  C  C     . ILE A 109 ? 0.8931 1.0439 0.6698 0.0679  0.0384  0.0450  109 ILE A C     
910  O  O     . ILE A 109 ? 1.0099 1.1489 0.7815 0.0659  0.0393  0.0308  109 ILE A O     
911  C  CB    . ILE A 109 ? 1.0397 1.2003 0.7732 0.0692  0.0219  0.0452  109 ILE A CB    
912  C  CG1   . ILE A 109 ? 1.0558 1.2038 0.7693 0.0639  0.0123  0.0237  109 ILE A CG1   
913  C  CG2   . ILE A 109 ? 0.9815 1.1519 0.6903 0.0760  0.0220  0.0566  109 ILE A CG2   
914  C  CD1   . ILE A 109 ? 0.9769 1.1298 0.6888 0.0563  -0.0064 0.0190  109 ILE A CD1   
915  N  N     . TYR A 110 ? 0.8654 1.0235 0.6744 0.0641  0.0361  0.0566  110 TYR A N     
916  C  CA    . TYR A 110 ? 0.8053 0.9581 0.6441 0.0583  0.0360  0.0542  110 TYR A CA    
917  C  C     . TYR A 110 ? 0.7581 0.9141 0.6191 0.0509  0.0243  0.0560  110 TYR A C     
918  O  O     . TYR A 110 ? 0.7859 0.9509 0.6508 0.0519  0.0208  0.0668  110 TYR A O     
919  C  CB    . TYR A 110 ? 0.8672 1.0231 0.7260 0.0627  0.0490  0.0681  110 TYR A CB    
920  C  CG    . TYR A 110 ? 0.8491 1.0033 0.6883 0.0719  0.0633  0.0689  110 TYR A CG    
921  C  CD1   . TYR A 110 ? 0.8948 1.0379 0.7273 0.0725  0.0678  0.0561  110 TYR A CD1   
922  C  CD2   . TYR A 110 ? 0.8753 1.0385 0.7023 0.0808  0.0732  0.0828  110 TYR A CD2   
923  C  CE1   . TYR A 110 ? 1.0464 1.1865 0.8606 0.0822  0.0823  0.0564  110 TYR A CE1   
924  C  CE2   . TYR A 110 ? 0.9534 1.1143 0.7607 0.0906  0.0882  0.0837  110 TYR A CE2   
925  C  CZ    . TYR A 110 ? 1.0210 1.1699 0.8220 0.0915  0.0929  0.0700  110 TYR A CZ    
926  O  OH    . TYR A 110 ? 1.1288 1.2741 0.9101 0.1025  0.1092  0.0704  110 TYR A OH    
927  N  N     . GLU A 111 ? 0.7719 0.9200 0.6470 0.0442  0.0193  0.0459  111 GLU A N     
928  C  CA    . GLU A 111 ? 0.8488 0.9973 0.7449 0.0379  0.0103  0.0464  111 GLU A CA    
929  C  C     . GLU A 111 ? 0.9008 1.0557 0.7878 0.0365  0.0003  0.0448  111 GLU A C     
930  O  O     . GLU A 111 ? 0.8474 1.0079 0.7489 0.0358  -0.0040 0.0533  111 GLU A O     
931  C  CB    . GLU A 111 ? 0.7304 0.8820 0.6515 0.0386  0.0136  0.0612  111 GLU A CB    
932  C  CG    . GLU A 111 ? 0.8916 1.0390 0.8254 0.0394  0.0221  0.0650  111 GLU A CG    
933  C  CD    . GLU A 111 ? 0.8514 0.9992 0.8132 0.0372  0.0219  0.0772  111 GLU A CD    
934  O  OE1   . GLU A 111 ? 0.8401 0.9879 0.8115 0.0346  0.0149  0.0797  111 GLU A OE1   
935  O  OE2   . GLU A 111 ? 0.8418 0.9893 0.8169 0.0382  0.0284  0.0846  111 GLU A OE2   
936  N  N     . TYR A 112 ? 0.8194 0.9728 0.6831 0.0360  -0.0040 0.0339  112 TYR A N     
937  C  CA    . TYR A 112 ? 0.8305 0.9908 0.6843 0.0342  -0.0150 0.0322  112 TYR A CA    
938  C  C     . TYR A 112 ? 0.9286 1.0857 0.7921 0.0267  -0.0245 0.0212  112 TYR A C     
939  O  O     . TYR A 112 ? 0.9273 1.0916 0.7887 0.0243  -0.0345 0.0208  112 TYR A O     
940  C  CB    . TYR A 112 ? 0.9034 1.0638 0.7236 0.0378  -0.0157 0.0274  112 TYR A CB    
941  C  CG    . TYR A 112 ? 1.0064 1.1536 0.8109 0.0372  -0.0119 0.0125  112 TYR A CG    
942  C  CD1   . TYR A 112 ? 0.9413 1.0818 0.7402 0.0306  -0.0214 -0.0024 112 TYR A CD1   
943  C  CD2   . TYR A 112 ? 1.0343 1.1759 0.8320 0.0433  0.0017  0.0143  112 TYR A CD2   
944  C  CE1   . TYR A 112 ? 1.0002 1.1271 0.7861 0.0300  -0.0178 -0.0158 112 TYR A CE1   
945  C  CE2   . TYR A 112 ? 1.0029 1.1316 0.7876 0.0436  0.0060  0.0011  112 TYR A CE2   
946  C  CZ    . TYR A 112 ? 1.1784 1.2989 0.9567 0.0369  -0.0039 -0.0143 112 TYR A CZ    
947  O  OH    . TYR A 112 ? 1.2879 1.3942 1.0544 0.0372  0.0004  -0.0272 112 TYR A OH    
948  N  N     . ASP A 113 ? 0.9898 1.1375 0.8650 0.0231  -0.0215 0.0135  113 ASP A N     
949  C  CA    . ASP A 113 ? 0.7495 0.8937 0.6329 0.0165  -0.0286 0.0034  113 ASP A CA    
950  C  C     . ASP A 113 ? 0.7381 0.8797 0.6464 0.0141  -0.0270 0.0059  113 ASP A C     
951  O  O     . ASP A 113 ? 0.8601 0.9980 0.7762 0.0093  -0.0304 -0.0015 113 ASP A O     
952  C  CB    . ASP A 113 ? 0.7929 0.9262 0.6630 0.0140  -0.0274 -0.0102 113 ASP A CB    
953  C  CG    . ASP A 113 ? 1.1101 1.2348 0.9826 0.0169  -0.0164 -0.0100 113 ASP A CG    
954  O  OD1   . ASP A 113 ? 1.0226 1.1503 0.9061 0.0204  -0.0104 0.0008  113 ASP A OD1   
955  O  OD2   . ASP A 113 ? 1.4553 1.5702 1.3204 0.0155  -0.0142 -0.0201 113 ASP A OD2   
956  N  N     . THR A 114 ? 0.8779 1.0203 0.7981 0.0173  -0.0220 0.0163  114 THR A N     
957  C  CA    . THR A 114 ? 0.7398 0.8771 0.6801 0.0153  -0.0212 0.0177  114 THR A CA    
958  C  C     . THR A 114 ? 0.7977 0.9413 0.7487 0.0147  -0.0270 0.0207  114 THR A C     
959  O  O     . THR A 114 ? 0.7822 0.9344 0.7343 0.0180  -0.0290 0.0301  114 THR A O     
960  C  CB    . THR A 114 ? 0.7059 0.8406 0.6562 0.0181  -0.0154 0.0276  114 THR A CB    
961  O  OG1   . THR A 114 ? 0.7884 0.9209 0.7298 0.0201  -0.0091 0.0277  114 THR A OG1   
962  C  CG2   . THR A 114 ? 0.5311 0.6561 0.4973 0.0153  -0.0153 0.0258  114 THR A CG2   
963  N  N     . PRO A 115 ? 0.7854 0.9254 0.7450 0.0113  -0.0292 0.0142  115 PRO A N     
964  C  CA    . PRO A 115 ? 0.6215 0.7685 0.5930 0.0117  -0.0334 0.0178  115 PRO A CA    
965  C  C     . PRO A 115 ? 0.5785 0.7247 0.5629 0.0159  -0.0310 0.0280  115 PRO A C     
966  O  O     . PRO A 115 ? 0.6612 0.7974 0.6499 0.0166  -0.0265 0.0293  115 PRO A O     
967  C  CB    . PRO A 115 ? 0.4380 0.5789 0.4163 0.0080  -0.0330 0.0093  115 PRO A CB    
968  C  CG    . PRO A 115 ? 0.6764 0.8108 0.6427 0.0045  -0.0317 0.0004  115 PRO A CG    
969  C  CD    . PRO A 115 ? 0.7110 0.8416 0.6696 0.0073  -0.0275 0.0041  115 PRO A CD    
970  N  N     . PHE A 116 ? 0.6285 0.7851 0.6203 0.0185  -0.0348 0.0354  116 PHE A N     
971  C  CA    . PHE A 116 ? 0.5563 0.7128 0.5609 0.0232  -0.0329 0.0463  116 PHE A CA    
972  C  C     . PHE A 116 ? 0.6091 0.7510 0.6250 0.0236  -0.0282 0.0435  116 PHE A C     
973  O  O     . PHE A 116 ? 0.6970 0.8296 0.7162 0.0247  -0.0252 0.0471  116 PHE A O     
974  C  CB    . PHE A 116 ? 0.6013 0.7716 0.6149 0.0258  -0.0380 0.0538  116 PHE A CB    
975  C  CG    . PHE A 116 ? 0.7166 0.8900 0.7403 0.0311  -0.0371 0.0675  116 PHE A CG    
976  C  CD1   . PHE A 116 ? 0.7251 0.9013 0.7407 0.0330  -0.0362 0.0756  116 PHE A CD1   
977  C  CD2   . PHE A 116 ? 0.6026 0.7759 0.6448 0.0350  -0.0362 0.0730  116 PHE A CD2   
978  C  CE1   . PHE A 116 ? 0.6232 0.8024 0.6499 0.0378  -0.0352 0.0896  116 PHE A CE1   
979  C  CE2   . PHE A 116 ? 0.6713 0.8464 0.7245 0.0401  -0.0353 0.0861  116 PHE A CE2   
980  C  CZ    . PHE A 116 ? 0.6914 0.8695 0.7373 0.0412  -0.0352 0.0947  116 PHE A CZ    
981  N  N     . ALA A 117 ? 0.6359 0.7751 0.6573 0.0228  -0.0277 0.0372  117 ALA A N     
982  C  CA    . ALA A 117 ? 0.6287 0.7530 0.6573 0.0244  -0.0231 0.0340  117 ALA A CA    
983  C  C     . ALA A 117 ? 0.5929 0.7028 0.6135 0.0212  -0.0211 0.0280  117 ALA A C     
984  O  O     . ALA A 117 ? 0.6334 0.7293 0.6580 0.0223  -0.0192 0.0278  117 ALA A O     
985  C  CB    . ALA A 117 ? 0.5283 0.6536 0.5617 0.0246  -0.0215 0.0285  117 ALA A CB    
986  N  N     . LYS A 118 ? 0.6288 0.7413 0.6386 0.0172  -0.0221 0.0232  118 LYS A N     
987  C  CA    . LYS A 118 ? 0.6270 0.7279 0.6315 0.0142  -0.0205 0.0189  118 LYS A CA    
988  C  C     . LYS A 118 ? 0.6006 0.7015 0.6073 0.0150  -0.0202 0.0271  118 LYS A C     
989  O  O     . LYS A 118 ? 0.6180 0.7078 0.6281 0.0134  -0.0198 0.0274  118 LYS A O     
990  C  CB    . LYS A 118 ? 0.6656 0.7686 0.6599 0.0104  -0.0206 0.0110  118 LYS A CB    
991  C  CG    . LYS A 118 ? 0.5217 0.6232 0.5161 0.0088  -0.0202 0.0037  118 LYS A CG    
992  C  CD    . LYS A 118 ? 0.6609 0.7587 0.6472 0.0046  -0.0196 -0.0040 118 LYS A CD    
993  C  CE    . LYS A 118 ? 0.7418 0.8417 0.7298 0.0028  -0.0193 -0.0092 118 LYS A CE    
994  N  NZ    . LYS A 118 ? 0.9555 1.0636 0.9390 -0.0006 -0.0223 -0.0127 118 LYS A NZ    
995  N  N     . ARG A 119 ? 0.5399 0.6533 0.5447 0.0173  -0.0207 0.0346  119 ARG A N     
996  C  CA    . ARG A 119 ? 0.6875 0.8025 0.6965 0.0191  -0.0190 0.0451  119 ARG A CA    
997  C  C     . ARG A 119 ? 0.7389 0.8456 0.7628 0.0208  -0.0195 0.0518  119 ARG A C     
998  O  O     . ARG A 119 ? 0.8523 0.9526 0.8840 0.0198  -0.0187 0.0575  119 ARG A O     
999  C  CB    . ARG A 119 ? 0.6187 0.7488 0.6201 0.0222  -0.0192 0.0523  119 ARG A CB    
1000 C  CG    . ARG A 119 ? 0.6722 0.8055 0.6784 0.0250  -0.0160 0.0653  119 ARG A CG    
1001 C  CD    . ARG A 119 ? 0.7495 0.8939 0.7397 0.0274  -0.0134 0.0686  119 ARG A CD    
1002 N  NE    . ARG A 119 ? 1.0026 1.1429 0.9838 0.0256  -0.0095 0.0616  119 ARG A NE    
1003 C  CZ    . ARG A 119 ? 0.8000 0.9340 0.7906 0.0245  -0.0055 0.0645  119 ARG A CZ    
1004 N  NH1   . ARG A 119 ? 0.8451 0.9750 0.8538 0.0241  -0.0055 0.0739  119 ARG A NH1   
1005 N  NH2   . ARG A 119 ? 0.7532 0.8845 0.7361 0.0235  -0.0019 0.0582  119 ARG A NH2   
1006 N  N     . TYR A 120 ? 0.6461 0.7526 0.6757 0.0233  -0.0207 0.0517  120 TYR A N     
1007 C  CA    . TYR A 120 ? 0.7089 0.8043 0.7518 0.0256  -0.0207 0.0563  120 TYR A CA    
1008 C  C     . TYR A 120 ? 0.6404 0.7168 0.6843 0.0220  -0.0212 0.0495  120 TYR A C     
1009 O  O     . TYR A 120 ? 0.7345 0.8017 0.7879 0.0211  -0.0224 0.0553  120 TYR A O     
1010 C  CB    . TYR A 120 ? 0.5382 0.6352 0.5862 0.0296  -0.0204 0.0551  120 TYR A CB    
1011 C  CG    . TYR A 120 ? 0.4955 0.5810 0.5573 0.0336  -0.0195 0.0607  120 TYR A CG    
1012 C  CD1   . TYR A 120 ? 0.4708 0.5635 0.5436 0.0372  -0.0199 0.0743  120 TYR A CD1   
1013 C  CD2   . TYR A 120 ? 0.4543 0.5204 0.5168 0.0340  -0.0181 0.0524  120 TYR A CD2   
1014 C  CE1   . TYR A 120 ? 0.4917 0.5722 0.5785 0.0409  -0.0189 0.0796  120 TYR A CE1   
1015 C  CE2   . TYR A 120 ? 0.4936 0.5460 0.5672 0.0380  -0.0172 0.0562  120 TYR A CE2   
1016 C  CZ    . TYR A 120 ? 0.5315 0.5910 0.6186 0.0413  -0.0176 0.0699  120 TYR A CZ    
1017 O  OH    . TYR A 120 ? 0.5531 0.5975 0.6528 0.0454  -0.0166 0.0739  120 TYR A OH    
1018 N  N     . LEU A 121 ? 0.5722 0.6426 0.6066 0.0196  -0.0211 0.0379  121 LEU A N     
1019 C  CA    . LEU A 121 ? 0.6779 0.7303 0.7099 0.0160  -0.0228 0.0311  121 LEU A CA    
1020 C  C     . LEU A 121 ? 0.6978 0.7498 0.7338 0.0119  -0.0249 0.0362  121 LEU A C     
1021 O  O     . LEU A 121 ? 0.7112 0.7491 0.7534 0.0091  -0.0285 0.0368  121 LEU A O     
1022 C  CB    . LEU A 121 ? 0.5703 0.6199 0.5901 0.0142  -0.0218 0.0196  121 LEU A CB    
1023 C  CG    . LEU A 121 ? 0.5756 0.6200 0.5931 0.0180  -0.0190 0.0140  121 LEU A CG    
1024 C  CD1   . LEU A 121 ? 0.6439 0.6875 0.6504 0.0159  -0.0173 0.0047  121 LEU A CD1   
1025 C  CD2   . LEU A 121 ? 0.5927 0.6171 0.6126 0.0201  -0.0196 0.0124  121 LEU A CD2   
1026 N  N     . ILE A 122 ? 0.6973 0.7641 0.7302 0.0116  -0.0228 0.0401  122 ILE A N     
1027 C  CA    . ILE A 122 ? 0.7053 0.7738 0.7435 0.0088  -0.0228 0.0461  122 ILE A CA    
1028 C  C     . ILE A 122 ? 0.7659 0.8364 0.8191 0.0103  -0.0227 0.0598  122 ILE A C     
1029 O  O     . ILE A 122 ? 0.8473 0.9084 0.9126 0.0069  -0.0259 0.0641  122 ILE A O     
1030 C  CB    . ILE A 122 ? 0.6388 0.7208 0.6671 0.0095  -0.0188 0.0453  122 ILE A CB    
1031 C  CG1   . ILE A 122 ? 0.5952 0.6722 0.6127 0.0067  -0.0194 0.0331  122 ILE A CG1   
1032 C  CG2   . ILE A 122 ? 0.4928 0.5799 0.5289 0.0091  -0.0162 0.0552  122 ILE A CG2   
1033 C  CD1   . ILE A 122 ? 0.5806 0.6678 0.5877 0.0074  -0.0157 0.0305  122 ILE A CD1   
1034 N  N     . ASP A 123 ? 0.6756 0.7585 0.7288 0.0149  -0.0198 0.0674  123 ASP A N     
1035 C  CA    . ASP A 123 ? 0.6146 0.7013 0.6822 0.0169  -0.0188 0.0825  123 ASP A CA    
1036 C  C     . ASP A 123 ? 0.6517 0.7219 0.7336 0.0156  -0.0230 0.0839  123 ASP A C     
1037 O  O     . ASP A 123 ? 0.8228 0.8873 0.9203 0.0130  -0.0248 0.0927  123 ASP A O     
1038 C  CB    . ASP A 123 ? 0.5672 0.6699 0.6296 0.0224  -0.0158 0.0901  123 ASP A CB    
1039 C  CG    . ASP A 123 ? 0.6814 0.7982 0.7280 0.0239  -0.0119 0.0895  123 ASP A CG    
1040 O  OD1   . ASP A 123 ? 0.5867 0.7005 0.6264 0.0210  -0.0110 0.0812  123 ASP A OD1   
1041 O  OD2   . ASP A 123 ? 0.6947 0.8246 0.7348 0.0282  -0.0099 0.0972  123 ASP A OD2   
1042 N  N     . LYS A 124 ? 0.7688 0.8306 0.8465 0.0176  -0.0245 0.0756  124 LYS A N     
1043 C  CA    . LYS A 124 ? 0.6740 0.7168 0.7620 0.0174  -0.0278 0.0748  124 LYS A CA    
1044 C  C     . LYS A 124 ? 0.7678 0.7912 0.8544 0.0114  -0.0331 0.0657  124 LYS A C     
1045 O  O     . LYS A 124 ? 0.8176 0.8215 0.9099 0.0107  -0.0369 0.0630  124 LYS A O     
1046 C  CB    . LYS A 124 ? 0.6367 0.6764 0.7199 0.0227  -0.0260 0.0687  124 LYS A CB    
1047 C  CG    . LYS A 124 ? 0.8394 0.8752 0.9374 0.0276  -0.0253 0.0784  124 LYS A CG    
1048 C  CD    . LYS A 124 ? 0.6592 0.7170 0.7628 0.0313  -0.0228 0.0930  124 LYS A CD    
1049 C  CE    . LYS A 124 ? 0.8057 0.8591 0.9267 0.0360  -0.0224 0.1048  124 LYS A CE    
1050 N  NZ    . LYS A 124 ? 0.9519 1.0275 1.0756 0.0411  -0.0203 0.1183  124 LYS A NZ    
1051 N  N     . GLY A 125 ? 0.7273 0.7545 0.8061 0.0073  -0.0339 0.0608  125 GLY A N     
1052 C  CA    . GLY A 125 ? 0.6090 0.6199 0.6874 0.0011  -0.0403 0.0542  125 GLY A CA    
1053 C  C     . GLY A 125 ? 0.6883 0.6796 0.7534 0.0012  -0.0431 0.0400  125 GLY A C     
1054 O  O     . GLY A 125 ? 0.7584 0.7301 0.8244 -0.0031 -0.0502 0.0357  125 GLY A O     
1055 N  N     . LEU A 126 ? 0.7693 0.7652 0.8219 0.0062  -0.0379 0.0330  126 LEU A N     
1056 C  CA    . LEU A 126 ? 0.7145 0.6931 0.7535 0.0080  -0.0380 0.0206  126 LEU A CA    
1057 C  C     . LEU A 126 ? 0.6846 0.6642 0.7079 0.0052  -0.0380 0.0113  126 LEU A C     
1058 O  O     . LEU A 126 ? 0.6304 0.6272 0.6524 0.0042  -0.0354 0.0133  126 LEU A O     
1059 C  CB    . LEU A 126 ? 0.7883 0.7716 0.8271 0.0157  -0.0313 0.0204  126 LEU A CB    
1060 C  CG    . LEU A 126 ? 0.7517 0.7347 0.8068 0.0195  -0.0306 0.0308  126 LEU A CG    
1061 C  CD1   . LEU A 126 ? 0.7285 0.7276 0.7867 0.0265  -0.0243 0.0350  126 LEU A CD1   
1062 C  CD2   . LEU A 126 ? 0.7588 0.7144 0.8150 0.0202  -0.0338 0.0259  126 LEU A CD2   
1063 N  N     . VAL A 127 ? 0.6118 0.5715 0.6220 0.0043  -0.0409 0.0010  127 VAL A N     
1064 C  CA    . VAL A 127 ? 0.7005 0.6584 0.6953 0.0017  -0.0416 -0.0071 127 VAL A CA    
1065 C  C     . VAL A 127 ? 0.7947 0.7417 0.7734 0.0071  -0.0363 -0.0168 127 VAL A C     
1066 O  O     . VAL A 127 ? 0.8146 0.7401 0.7860 0.0090  -0.0382 -0.0224 127 VAL A O     
1067 C  CB    . VAL A 127 ? 0.7750 0.7195 0.7676 -0.0056 -0.0515 -0.0089 127 VAL A CB    
1068 C  CG1   . VAL A 127 ? 0.7131 0.6566 0.6895 -0.0077 -0.0521 -0.0161 127 VAL A CG1   
1069 C  CG2   . VAL A 127 ? 0.6256 0.5823 0.6377 -0.0102 -0.0553 0.0026  127 VAL A CG2   
1070 N  N     . PRO A 128 ? 0.8480 0.8080 0.8210 0.0098  -0.0294 -0.0189 128 PRO A N     
1071 C  CA    . PRO A 128 ? 0.8825 0.8336 0.8421 0.0155  -0.0229 -0.0264 128 PRO A CA    
1072 C  C     . PRO A 128 ? 0.8200 0.7533 0.7595 0.0130  -0.0262 -0.0352 128 PRO A C     
1073 O  O     . PRO A 128 ? 0.9103 0.8427 0.8474 0.0064  -0.0335 -0.0350 128 PRO A O     
1074 C  CB    . PRO A 128 ? 0.6699 0.6431 0.6337 0.0174  -0.0160 -0.0239 128 PRO A CB    
1075 C  CG    . PRO A 128 ? 0.7710 0.7583 0.7408 0.0113  -0.0203 -0.0196 128 PRO A CG    
1076 C  CD    . PRO A 128 ? 0.8391 0.8222 0.8185 0.0083  -0.0268 -0.0142 128 PRO A CD    
1077 N  N     . MET A 129 ? 0.9269 0.8458 0.8516 0.0191  -0.0204 -0.0421 129 MET A N     
1078 C  CA    . MET A 129 ? 0.8531 0.7555 0.7539 0.0188  -0.0212 -0.0506 129 MET A CA    
1079 C  C     . MET A 129 ? 0.9374 0.8166 0.8272 0.0135  -0.0333 -0.0556 129 MET A C     
1080 O  O     . MET A 129 ? 1.0099 0.8792 0.8815 0.0103  -0.0381 -0.0606 129 MET A O     
1081 C  CB    . MET A 129 ? 0.8759 0.7935 0.7738 0.0151  -0.0200 -0.0492 129 MET A CB    
1082 C  CG    . MET A 129 ? 0.8772 0.8137 0.7824 0.0197  -0.0089 -0.0462 129 MET A CG    
1083 S  SD    . MET A 129 ? 0.9066 0.8353 0.8087 0.0309  0.0029  -0.0485 129 MET A SD    
1084 C  CE    . MET A 129 ? 0.6069 0.5203 0.4807 0.0344  0.0089  -0.0560 129 MET A CE    
1085 N  N     . GLU A 130 ? 1.0062 0.8762 0.9070 0.0123  -0.0391 -0.0537 130 GLU A N     
1086 C  CA    . GLU A 130 ? 1.1102 0.9565 1.0026 0.0065  -0.0520 -0.0584 130 GLU A CA    
1087 C  C     . GLU A 130 ? 1.0961 0.9146 0.9745 0.0129  -0.0500 -0.0671 130 GLU A C     
1088 O  O     . GLU A 130 ? 1.2144 1.0353 1.1024 0.0204  -0.0407 -0.0650 130 GLU A O     
1089 C  CB    . GLU A 130 ? 1.1065 0.9614 1.0240 -0.0010 -0.0615 -0.0489 130 GLU A CB    
1090 C  CG    . GLU A 130 ? 1.3097 1.1634 1.2460 0.0020  -0.0594 -0.0435 130 GLU A CG    
1091 C  CD    . GLU A 130 ? 1.5059 1.3730 1.4681 -0.0049 -0.0664 -0.0315 130 GLU A CD    
1092 O  OE1   . GLU A 130 ? 1.0566 0.9340 1.0227 -0.0115 -0.0722 -0.0279 130 GLU A OE1   
1093 O  OE2   . GLU A 130 ? 1.7156 1.5833 1.6950 -0.0030 -0.0653 -0.0249 130 GLU A OE2   
1094 N  N     . GLY A 131 ? 1.2057 0.9975 1.0608 0.0102  -0.0590 -0.0769 131 GLY A N     
1095 C  CA    . GLY A 131 ? 1.2024 0.9628 1.0374 0.0165  -0.0574 -0.0879 131 GLY A CA    
1096 C  C     . GLY A 131 ? 1.2624 1.0063 1.0606 0.0208  -0.0539 -0.0990 131 GLY A C     
1097 O  O     . GLY A 131 ? 1.2010 0.9579 0.9907 0.0183  -0.0536 -0.0974 131 GLY A O     
1098 N  N     . ASP A 132 ? 1.3446 1.0583 1.1202 0.0282  -0.0506 -0.1102 132 ASP A N     
1099 C  CA    . ASP A 132 ? 1.3875 1.0809 1.1234 0.0342  -0.0460 -0.1216 132 ASP A CA    
1100 C  C     . ASP A 132 ? 1.3797 1.0769 1.1087 0.0488  -0.0241 -0.1226 132 ASP A C     
1101 O  O     . ASP A 132 ? 1.4378 1.1139 1.1328 0.0568  -0.0170 -0.1325 132 ASP A O     
1102 C  CB    . ASP A 132 ? 1.3905 1.0427 1.0989 0.0322  -0.0587 -0.1353 132 ASP A CB    
1103 C  CG    . ASP A 132 ? 1.7177 1.3659 1.4408 0.0174  -0.0812 -0.1327 132 ASP A CG    
1104 O  OD1   . ASP A 132 ? 1.7670 1.4296 1.5256 0.0131  -0.0840 -0.1229 132 ASP A OD1   
1105 O  OD2   . ASP A 132 ? 1.7141 1.3454 1.4137 0.0102  -0.0960 -0.1395 132 ASP A OD2   
1106 N  N     . GLU A 133 ? 1.2666 0.9905 1.0269 0.0528  -0.0132 -0.1119 133 GLU A N     
1107 C  CA    . GLU A 133 ? 1.2005 0.9300 0.9604 0.0665  0.0071  -0.1109 133 GLU A CA    
1108 C  C     . GLU A 133 ? 1.1396 0.8822 0.8838 0.0697  0.0169  -0.1099 133 GLU A C     
1109 O  O     . GLU A 133 ? 1.2504 1.0175 1.0063 0.0620  0.0129  -0.1025 133 GLU A O     
1110 C  CB    . GLU A 133 ? 1.1890 0.9463 0.9883 0.0684  0.0133  -0.0983 133 GLU A CB    
1111 C  CG    . GLU A 133 ? 1.2838 1.0247 1.0940 0.0747  0.0157  -0.0994 133 GLU A CG    
1112 C  CD    . GLU A 133 ? 1.3571 1.0890 1.1590 0.0905  0.0347  -0.1024 133 GLU A CD    
1113 O  OE1   . GLU A 133 ? 1.4002 1.1395 1.1880 0.0963  0.0463  -0.1030 133 GLU A OE1   
1114 O  OE2   . GLU A 133 ? 1.3847 1.1020 1.1954 0.0975  0.0387  -0.1032 133 GLU A OE2   
1115 N  N     . GLU A 134 ? 1.1702 0.8956 0.8880 0.0816  0.0307  -0.1169 134 GLU A N     
1116 C  CA    . GLU A 134 ? 1.2710 1.0078 0.9742 0.0865  0.0428  -0.1147 134 GLU A CA    
1117 C  C     . GLU A 134 ? 1.2408 1.0068 0.9738 0.0941  0.0599  -0.1033 134 GLU A C     
1118 O  O     . GLU A 134 ? 1.2954 1.0551 1.0336 0.1056  0.0728  -0.1035 134 GLU A O     
1119 C  CB    . GLU A 134 ? 1.3740 1.0780 1.0324 0.0962  0.0501  -0.1271 134 GLU A CB    
1120 C  CG    . GLU A 134 ? 1.6890 1.3698 1.3138 0.0873  0.0326  -0.1367 134 GLU A CG    
1121 C  CD    . GLU A 134 ? 2.1121 1.7538 1.6891 0.0970  0.0372  -0.1514 134 GLU A CD    
1122 O  OE1   . GLU A 134 ? 1.9651 1.6012 1.5328 0.1120  0.0579  -0.1527 134 GLU A OE1   
1123 O  OE2   . GLU A 134 ? 2.1356 1.7518 1.6841 0.0899  0.0201  -0.1614 134 GLU A OE2   
1124 N  N     . LEU A 135 ? 1.1540 0.9514 0.9076 0.0876  0.0594  -0.0931 135 LEU A N     
1125 C  CA    . LEU A 135 ? 1.1070 0.9340 0.8913 0.0923  0.0722  -0.0816 135 LEU A CA    
1126 C  C     . LEU A 135 ? 1.1329 0.9625 0.9045 0.1029  0.0907  -0.0798 135 LEU A C     
1127 O  O     . LEU A 135 ? 1.1792 1.0016 0.9251 0.1017  0.0912  -0.0831 135 LEU A O     
1128 C  CB    . LEU A 135 ? 1.0427 0.9001 0.8535 0.0806  0.0631  -0.0724 135 LEU A CB    
1129 C  CG    . LEU A 135 ? 0.8970 0.7559 0.7216 0.0700  0.0460  -0.0720 135 LEU A CG    
1130 C  CD1   . LEU A 135 ? 0.8912 0.7805 0.7404 0.0611  0.0409  -0.0629 135 LEU A CD1   
1131 C  CD2   . LEU A 135 ? 1.0572 0.9097 0.8968 0.0749  0.0466  -0.0714 135 LEU A CD2   
1132 N  N     . LYS A 136 ? 1.0117 0.8528 0.8030 0.1133  0.1061  -0.0732 136 LYS A N     
1133 C  CA    . LYS A 136 ? 1.1501 0.9985 0.9368 0.1239  0.1256  -0.0683 136 LYS A CA    
1134 C  C     . LYS A 136 ? 1.0692 0.9523 0.8824 0.1165  0.1259  -0.0561 136 LYS A C     
1135 O  O     . LYS A 136 ? 1.1074 1.0150 0.9556 0.1115  0.1213  -0.0477 136 LYS A O     
1136 C  CB    . LYS A 136 ? 1.0550 0.9020 0.8551 0.1387  0.1425  -0.0650 136 LYS A CB    
1137 C  CG    . LYS A 136 ? 1.1745 0.9831 0.9386 0.1508  0.1505  -0.0778 136 LYS A CG    
1138 C  CD    . LYS A 136 ? 1.4696 1.2794 1.2412 0.1687  0.1746  -0.0726 136 LYS A CD    
1139 C  CE    . LYS A 136 ? 1.4043 1.2379 1.1827 0.1726  0.1899  -0.0616 136 LYS A CE    
1140 N  NZ    . LYS A 136 ? 1.3312 1.1867 1.1449 0.1843  0.2084  -0.0483 136 LYS A NZ    
1141 N  N     . MET A 137 ? 0.9885 0.8728 0.7843 0.1159  0.1307  -0.0552 137 MET A N     
1142 C  CA    . MET A 137 ? 0.9422 0.8552 0.7600 0.1079  0.1298  -0.0447 137 MET A CA    
1143 C  C     . MET A 137 ? 0.9031 0.8293 0.7287 0.1180  0.1505  -0.0352 137 MET A C     
1144 O  O     . MET A 137 ? 1.0683 0.9770 0.8700 0.1307  0.1655  -0.0383 137 MET A O     
1145 C  CB    . MET A 137 ? 0.8793 0.7859 0.6758 0.0977  0.1178  -0.0488 137 MET A CB    
1146 C  CG    . MET A 137 ? 1.0663 0.9522 0.8454 0.0906  0.0999  -0.0595 137 MET A CG    
1147 S  SD    . MET A 137 ? 1.1622 1.0597 0.9486 0.0739  0.0807  -0.0579 137 MET A SD    
1148 C  CE    . MET A 137 ? 1.3092 1.1743 1.0641 0.0702  0.0649  -0.0707 137 MET A CE    
1149 N  N     . LEU A 138 ? 0.8651 0.8215 0.7242 0.1122  0.1513  -0.0233 138 LEU A N     
1150 C  CA    . LEU A 138 ? 0.9539 0.9272 0.8277 0.1197  0.1697  -0.0116 138 LEU A CA    
1151 C  C     . LEU A 138 ? 0.8965 0.8957 0.7957 0.1076  0.1631  -0.0023 138 LEU A C     
1152 O  O     . LEU A 138 ? 0.8924 0.9082 0.8186 0.0979  0.1502  0.0001  138 LEU A O     
1153 C  CB    . LEU A 138 ? 0.8548 0.8401 0.7571 0.1300  0.1818  -0.0041 138 LEU A CB    
1154 C  CG    . LEU A 138 ? 0.8879 0.8987 0.8194 0.1359  0.1989  0.0116  138 LEU A CG    
1155 C  CD1   . LEU A 138 ? 0.9466 0.9429 0.8495 0.1489  0.2196  0.0121  138 LEU A CD1   
1156 C  CD2   . LEU A 138 ? 0.9753 1.0028 0.9431 0.1425  0.2048  0.0201  138 LEU A CD2   
1157 N  N     . ALA A 139 ? 0.8472 0.8482 0.7361 0.1085  0.1719  0.0027  139 ALA A N     
1158 C  CA    . ALA A 139 ? 0.8295 0.8530 0.7427 0.0979  0.1677  0.0121  139 ALA A CA    
1159 C  C     . ALA A 139 ? 0.9652 1.0128 0.9121 0.1035  0.1836  0.0273  139 ALA A C     
1160 O  O     . ALA A 139 ? 0.8819 0.9262 0.8250 0.1174  0.2018  0.0312  139 ALA A O     
1161 C  CB    . ALA A 139 ? 0.9561 0.9682 0.8410 0.0944  0.1666  0.0103  139 ALA A CB    
1162 N  N     . PHE A 140 ? 0.8004 0.8719 0.7812 0.0926  0.1767  0.0361  140 PHE A N     
1163 C  CA    . PHE A 140 ? 0.9096 1.0055 0.9258 0.0957  0.1899  0.0521  140 PHE A CA    
1164 C  C     . PHE A 140 ? 0.8993 1.0120 0.9382 0.0821  0.1815  0.0593  140 PHE A C     
1165 O  O     . PHE A 140 ? 0.8173 0.9282 0.8552 0.0699  0.1634  0.0522  140 PHE A O     
1166 C  CB    . PHE A 140 ? 0.9469 1.0596 0.9969 0.0992  0.1907  0.0576  140 PHE A CB    
1167 C  CG    . PHE A 140 ? 0.8404 0.9689 0.9178 0.0854  0.1703  0.0570  140 PHE A CG    
1168 C  CD1   . PHE A 140 ? 0.7551 0.8718 0.8183 0.0810  0.1547  0.0449  140 PHE A CD1   
1169 C  CD2   . PHE A 140 ? 0.7979 0.9528 0.9151 0.0770  0.1667  0.0690  140 PHE A CD2   
1170 C  CE1   . PHE A 140 ? 0.8008 0.9315 0.8859 0.0695  0.1372  0.0446  140 PHE A CE1   
1171 C  CE2   . PHE A 140 ? 0.7483 0.9157 0.8864 0.0647  0.1475  0.0674  140 PHE A CE2   
1172 C  CZ    . PHE A 140 ? 0.8060 0.9612 0.9266 0.0614  0.1333  0.0551  140 PHE A CZ    
1173 N  N     . ALA A 141 ? 0.8606 0.9888 0.9202 0.0850  0.1959  0.0739  141 ALA A N     
1174 C  CA    . ALA A 141 ? 0.9188 1.0642 1.0060 0.0728  0.1900  0.0830  141 ALA A CA    
1175 C  C     . ALA A 141 ? 0.8782 1.0493 1.0077 0.0764  0.2036  0.1012  141 ALA A C     
1176 O  O     . ALA A 141 ? 0.9680 1.1413 1.0990 0.0903  0.2213  0.1073  141 ALA A O     
1177 C  CB    . ALA A 141 ? 0.9669 1.0991 1.0275 0.0707  0.1929  0.0826  141 ALA A CB    
1178 N  N     . ILE A 142 ? 0.7781 0.9683 0.9434 0.0638  0.1952  0.1101  142 ILE A N     
1179 C  CA    . ILE A 142 ? 0.9090 1.1265 1.1216 0.0642  0.2041  0.1284  142 ILE A CA    
1180 C  C     . ILE A 142 ? 0.9780 1.2044 1.2080 0.0569  0.2082  0.1405  142 ILE A C     
1181 O  O     . ILE A 142 ? 0.9172 1.1300 1.1263 0.0497  0.2007  0.1340  142 ILE A O     
1182 C  CB    . ILE A 142 ? 0.8779 1.1140 1.1274 0.0547  0.1867  0.1290  142 ILE A CB    
1183 C  CG1   . ILE A 142 ? 0.7929 1.0273 1.0460 0.0369  0.1635  0.1208  142 ILE A CG1   
1184 C  CG2   . ILE A 142 ? 0.7864 1.0149 1.0214 0.0627  0.1838  0.1193  142 ILE A CG2   
1185 C  CD1   . ILE A 142 ? 0.8204 1.0751 1.1122 0.0260  0.1464  0.1240  142 ILE A CD1   
1186 N  N     . ALA A 143 ? 0.8417 1.0918 1.1128 0.0593  0.2207  0.1596  143 ALA A N     
1187 C  CA    . ALA A 143 ? 0.7807 1.0439 1.0798 0.0514  0.2245  0.1747  143 ALA A CA    
1188 C  C     . ALA A 143 ? 0.8790 1.1716 1.2372 0.0426  0.2175  0.1885  143 ALA A C     
1189 O  O     . ALA A 143 ? 0.8277 1.1349 1.2072 0.0502  0.2237  0.1952  143 ALA A O     
1190 C  CB    . ALA A 143 ? 0.9039 1.1656 1.1909 0.0655  0.2521  0.1880  143 ALA A CB    
1191 N  N     . THR A 144 ? 0.9362 1.2369 1.3216 0.0265  0.2041  0.1931  144 THR A N     
1192 C  CA    . THR A 144 ? 0.9298 1.2537 1.3663 0.0136  0.1885  0.2007  144 THR A CA    
1193 C  C     . THR A 144 ? 0.9266 1.2679 1.4064 0.0051  0.1931  0.2203  144 THR A C     
1194 O  O     . THR A 144 ? 0.9594 1.2902 1.4261 0.0034  0.1996  0.2227  144 THR A O     
1195 C  CB    . THR A 144 ? 0.8754 1.1887 1.3018 -0.0012 0.1599  0.1821  144 THR A CB    
1196 O  OG1   . THR A 144 ? 0.8404 1.1356 1.2452 -0.0093 0.1538  0.1742  144 THR A OG1   
1197 C  CG2   . THR A 144 ? 0.8424 1.1410 1.2312 0.0066  0.1552  0.1649  144 THR A CG2   
1198 N  N     . LEU A 145 ? 0.8909 1.2594 1.4241 -0.0005 0.1889  0.2352  145 LEU A N     
1199 C  CA    . LEU A 145 ? 1.0287 1.4159 1.6112 -0.0115 0.1890  0.2543  145 LEU A CA    
1200 C  C     . LEU A 145 ? 1.0711 1.4515 1.6629 -0.0327 0.1598  0.2430  145 LEU A C     
1201 O  O     . LEU A 145 ? 1.1855 1.5736 1.7943 -0.0422 0.1385  0.2365  145 LEU A O     
1202 C  CB    . LEU A 145 ? 0.8008 1.2208 1.4395 -0.0089 0.1962  0.2762  145 LEU A CB    
1203 C  CG    . LEU A 145 ? 0.8547 1.2975 1.5545 -0.0242 0.1893  0.2959  145 LEU A CG    
1204 C  CD1   . LEU A 145 ? 0.8998 1.3372 1.5983 -0.0232 0.2065  0.3077  145 LEU A CD1   
1205 C  CD2   . LEU A 145 ? 0.6753 1.1523 1.4317 -0.0203 0.1969  0.3186  145 LEU A CD2   
1206 N  N     . TYR A 146 ? 1.0473 1.4126 1.6270 -0.0396 0.1589  0.2406  146 TYR A N     
1207 C  CA    . TYR A 146 ? 1.0181 1.3725 1.6024 -0.0583 0.1335  0.2289  146 TYR A CA    
1208 C  C     . TYR A 146 ? 1.0592 1.4271 1.6934 -0.0710 0.1322  0.2471  146 TYR A C     
1209 O  O     . TYR A 146 ? 1.0873 1.4614 1.7327 -0.0646 0.1534  0.2649  146 TYR A O     
1210 C  CB    . TYR A 146 ? 0.9884 1.3120 1.5197 -0.0573 0.1308  0.2101  146 TYR A CB    
1211 C  CG    . TYR A 146 ? 1.1368 1.4467 1.6697 -0.0749 0.1062  0.1965  146 TYR A CG    
1212 C  CD1   . TYR A 146 ? 1.1232 1.4186 1.6517 -0.0811 0.1068  0.1972  146 TYR A CD1   
1213 C  CD2   . TYR A 146 ? 1.1120 1.4226 1.6498 -0.0846 0.0827  0.1833  146 TYR A CD2   
1214 C  CE1   . TYR A 146 ? 1.1513 1.4320 1.6809 -0.0961 0.0854  0.1843  146 TYR A CE1   
1215 C  CE2   . TYR A 146 ? 1.1297 1.4257 1.6658 -0.0996 0.0611  0.1699  146 TYR A CE2   
1216 C  CZ    . TYR A 146 ? 1.1450 1.4255 1.6773 -0.1051 0.0629  0.1701  146 TYR A CZ    
1217 O  OH    . TYR A 146 ? 1.3038 1.5676 1.8338 -0.1190 0.0425  0.1562  146 TYR A OH    
1218 N  N     . HIS A 147 ? 1.0352 1.4070 1.6986 -0.0890 0.1070  0.2428  147 HIS A N     
1219 C  CA    . HIS A 147 ? 1.1291 1.5044 1.8325 -0.1046 0.0993  0.2537  147 HIS A CA    
1220 C  C     . HIS A 147 ? 1.1810 1.5338 1.8680 -0.1201 0.0719  0.2316  147 HIS A C     
1221 O  O     . HIS A 147 ? 1.2280 1.5744 1.8937 -0.1220 0.0551  0.2136  147 HIS A O     
1222 C  CB    . HIS A 147 ? 1.1309 1.5377 1.9001 -0.1131 0.0947  0.2749  147 HIS A CB    
1223 C  CG    . HIS A 147 ? 1.0864 1.5179 1.8802 -0.0983 0.1228  0.2998  147 HIS A CG    
1224 N  ND1   . HIS A 147 ? 0.9558 1.4106 1.7709 -0.0910 0.1259  0.3080  147 HIS A ND1   
1225 C  CD2   . HIS A 147 ? 1.1114 1.5487 1.9139 -0.0892 0.1493  0.3193  147 HIS A CD2   
1226 C  CE1   . HIS A 147 ? 0.9361 1.4090 1.7707 -0.0772 0.1542  0.3308  147 HIS A CE1   
1227 N  NE2   . HIS A 147 ? 0.9370 1.3999 1.7635 -0.0758 0.1690  0.3380  147 HIS A NE2   
1228 N  N     . GLU A 148 ? 1.3419 1.6824 2.0387 -0.1305 0.0683  0.2335  148 GLU A N     
1229 C  CA    . GLU A 148 ? 1.4395 1.7576 2.1244 -0.1452 0.0433  0.2133  148 GLU A CA    
1230 C  C     . GLU A 148 ? 1.5182 1.8485 2.2378 -0.1604 0.0178  0.2108  148 GLU A C     
1231 O  O     . GLU A 148 ? 1.3298 1.6824 2.1031 -0.1686 0.0159  0.2300  148 GLU A O     
1232 C  CB    . GLU A 148 ? 1.4190 1.7228 2.1152 -0.1535 0.0453  0.2188  148 GLU A CB    
1233 C  CG    . GLU A 148 ? 1.4793 1.7536 2.1513 -0.1644 0.0246  0.1957  148 GLU A CG    
1234 C  CD    . GLU A 148 ? 1.6350 1.8859 2.2713 -0.1575 0.0368  0.1907  148 GLU A CD    
1235 O  OE1   . GLU A 148 ? 1.6307 1.8875 2.2783 -0.1517 0.0567  0.2095  148 GLU A OE1   
1236 O  OE2   . GLU A 148 ? 1.5348 1.7620 2.1323 -0.1576 0.0266  0.1689  148 GLU A OE2   
1237 N  N     . GLY A 149 ? 1.6297 1.9460 2.3188 -0.1640 -0.0019 0.1878  149 GLY A N     
1238 C  CA    . GLY A 149 ? 1.5126 1.8365 2.2274 -0.1791 -0.0288 0.1828  149 GLY A CA    
1239 C  C     . GLY A 149 ? 1.4662 1.8072 2.1761 -0.1728 -0.0342 0.1806  149 GLY A C     
1240 O  O     . GLY A 149 ? 1.5298 1.8619 2.2206 -0.1791 -0.0558 0.1629  149 GLY A O     
1241 N  N     . GLU A 150 ? 1.4010 1.7661 2.1279 -0.1600 -0.0144 0.1988  150 GLU A N     
1242 C  CA    . GLU A 150 ? 1.2478 1.6306 1.9759 -0.1538 -0.0191 0.1991  150 GLU A CA    
1243 C  C     . GLU A 150 ? 1.3543 1.7168 2.0238 -0.1455 -0.0232 0.1757  150 GLU A C     
1244 O  O     . GLU A 150 ? 1.2540 1.5971 1.8823 -0.1351 -0.0086 0.1667  150 GLU A O     
1245 C  CB    . GLU A 150 ? 1.0911 1.4998 1.8431 -0.1387 0.0065  0.2219  150 GLU A CB    
1246 C  CG    . GLU A 150 ? 1.2064 1.6100 1.9462 -0.1254 0.0367  0.2319  150 GLU A CG    
1247 C  CD    . GLU A 150 ? 1.2808 1.7124 2.0519 -0.1120 0.0603  0.2561  150 GLU A CD    
1248 O  OE1   . GLU A 150 ? 1.2096 1.6451 1.9598 -0.0975 0.0696  0.2532  150 GLU A OE1   
1249 O  OE2   . GLU A 150 ? 1.2747 1.7248 2.0937 -0.1163 0.0687  0.2785  150 GLU A OE2   
1250 N  N     . GLU A 151 ? 1.2932 1.6613 1.9607 -0.1504 -0.0437 0.1671  151 GLU A N     
1251 C  CA    . GLU A 151 ? 1.1923 1.5431 1.8090 -0.1447 -0.0511 0.1458  151 GLU A CA    
1252 C  C     . GLU A 151 ? 1.1569 1.5051 1.7420 -0.1247 -0.0271 0.1460  151 GLU A C     
1253 O  O     . GLU A 151 ? 1.1502 1.5126 1.7536 -0.1144 -0.0054 0.1630  151 GLU A O     
1254 C  CB    . GLU A 151 ? 1.1873 1.5518 1.8153 -0.1516 -0.0743 0.1431  151 GLU A CB    
1255 C  CG    . GLU A 151 ? 1.2796 1.6756 1.9418 -0.1432 -0.0657 0.1630  151 GLU A CG    
1256 C  CD    . GLU A 151 ? 1.3783 1.7914 2.0622 -0.1530 -0.0914 0.1643  151 GLU A CD    
1257 O  OE1   . GLU A 151 ? 1.3156 1.7465 2.0057 -0.1432 -0.0876 0.1722  151 GLU A OE1   
1258 O  OE2   . GLU A 151 ? 1.5456 1.9533 2.2398 -0.1704 -0.1159 0.1575  151 GLU A OE2   
1259 N  N     . PHE A 152 ? 1.0156 1.3450 1.5530 -0.1190 -0.0308 0.1272  152 PHE A N     
1260 C  CA    . PHE A 152 ? 0.9212 1.2453 1.4268 -0.1012 -0.0108 0.1254  152 PHE A CA    
1261 C  C     . PHE A 152 ? 0.9364 1.2855 1.4666 -0.0912 -0.0010 0.1409  152 PHE A C     
1262 O  O     . PHE A 152 ? 1.0086 1.3739 1.5595 -0.0960 -0.0160 0.1441  152 PHE A O     
1263 C  CB    . PHE A 152 ? 1.1394 1.4428 1.5968 -0.0986 -0.0198 0.1042  152 PHE A CB    
1264 C  CG    . PHE A 152 ? 0.9814 1.2777 1.4065 -0.0817 -0.0020 0.1014  152 PHE A CG    
1265 C  CD1   . PHE A 152 ? 0.9300 1.2091 1.3288 -0.0744 0.0141  0.0981  152 PHE A CD1   
1266 C  CD2   . PHE A 152 ? 1.0384 1.3449 1.4604 -0.0735 -0.0021 0.1026  152 PHE A CD2   
1267 C  CE1   . PHE A 152 ? 0.8124 1.0834 1.1810 -0.0599 0.0286  0.0948  152 PHE A CE1   
1268 C  CE2   . PHE A 152 ? 1.0095 1.3074 1.4026 -0.0586 0.0135  0.0995  152 PHE A CE2   
1269 C  CZ    . PHE A 152 ? 0.9055 1.1850 1.2713 -0.0521 0.0283  0.0951  152 PHE A CZ    
1270 N  N     . ALA A 153 ? 0.8243 1.1759 1.3517 -0.0769 0.0244  0.1510  153 ALA A N     
1271 C  CA    . ALA A 153 ? 0.9377 1.3099 1.4851 -0.0641 0.0390  0.1659  153 ALA A CA    
1272 C  C     . ALA A 153 ? 0.8787 1.2813 1.4858 -0.0715 0.0338  0.1861  153 ALA A C     
1273 O  O     . ALA A 153 ? 0.8947 1.3177 1.5243 -0.0642 0.0375  0.1974  153 ALA A O     
1274 C  CB    . ALA A 153 ? 0.8049 1.1735 1.3265 -0.0562 0.0337  0.1555  153 ALA A CB    
1275 N  N     . GLU A 154 ? 0.9308 1.3372 1.5662 -0.0860 0.0248  0.1918  154 GLU A N     
1276 C  CA    . GLU A 154 ? 0.9656 1.4018 1.6622 -0.0931 0.0222  0.2139  154 GLU A CA    
1277 C  C     . GLU A 154 ? 0.8643 1.3175 1.5827 -0.0772 0.0524  0.2351  154 GLU A C     
1278 O  O     . GLU A 154 ? 0.8486 1.3300 1.6118 -0.0748 0.0554  0.2540  154 GLU A O     
1279 C  CB    . GLU A 154 ? 1.0347 1.4676 1.7553 -0.1114 0.0088  0.2156  154 GLU A CB    
1280 C  CG    . GLU A 154 ? 1.1195 1.5824 1.9067 -0.1190 0.0092  0.2410  154 GLU A CG    
1281 C  CD    . GLU A 154 ? 1.2839 1.7666 2.1059 -0.1316 -0.0178 0.2445  154 GLU A CD    
1282 O  OE1   . GLU A 154 ? 1.2790 1.7811 2.1133 -0.1225 -0.0149 0.2528  154 GLU A OE1   
1283 O  OE2   . GLU A 154 ? 1.2246 1.7026 2.0611 -0.1507 -0.0426 0.2387  154 GLU A OE2   
1284 N  N     . GLY A 155 ? 0.9123 1.3485 1.5987 -0.0657 0.0751  0.2326  155 GLY A N     
1285 C  CA    . GLY A 155 ? 0.8329 1.2804 1.5300 -0.0488 0.1056  0.2504  155 GLY A CA    
1286 C  C     . GLY A 155 ? 0.8282 1.2666 1.4875 -0.0297 0.1204  0.2426  155 GLY A C     
1287 O  O     . GLY A 155 ? 0.8650 1.2900 1.4927 -0.0298 0.1066  0.2247  155 GLY A O     
1288 N  N     . PRO A 156 ? 0.8025 1.2471 1.4643 -0.0125 0.1494  0.2563  156 PRO A N     
1289 C  CA    . PRO A 156 ? 0.8474 1.2830 1.4766 0.0066  0.1647  0.2500  156 PRO A CA    
1290 C  C     . PRO A 156 ? 0.8058 1.2097 1.3741 0.0168  0.1780  0.2343  156 PRO A C     
1291 O  O     . PRO A 156 ? 0.8918 1.2837 1.4458 0.0122  0.1814  0.2327  156 PRO A O     
1292 C  CB    . PRO A 156 ? 0.8954 1.3568 1.5656 0.0200  0.1890  0.2750  156 PRO A CB    
1293 C  CG    . PRO A 156 ? 0.7215 1.1928 1.4203 0.0132  0.1976  0.2912  156 PRO A CG    
1294 C  CD    . PRO A 156 ? 0.8312 1.2970 1.5365 -0.0098 0.1686  0.2815  156 PRO A CD    
1295 N  N     . ILE A 157 ? 0.8330 1.2231 1.3662 0.0305  0.1846  0.2231  157 ILE A N     
1296 C  CA    . ILE A 157 ? 0.8015 1.1628 1.2787 0.0426  0.1994  0.2103  157 ILE A CA    
1297 C  C     . ILE A 157 ? 0.8271 1.1945 1.3097 0.0594  0.2309  0.2267  157 ILE A C     
1298 O  O     . ILE A 157 ? 1.0404 1.4185 1.5369 0.0732  0.2455  0.2357  157 ILE A O     
1299 C  CB    . ILE A 157 ? 0.8922 1.2362 1.3331 0.0504  0.1942  0.1930  157 ILE A CB    
1300 C  CG1   . ILE A 157 ? 0.7798 1.1176 1.2125 0.0350  0.1648  0.1773  157 ILE A CG1   
1301 C  CG2   . ILE A 157 ? 0.8757 1.1904 1.2611 0.0631  0.2096  0.1809  157 ILE A CG2   
1302 C  CD1   . ILE A 157 ? 0.6495 0.9819 1.0674 0.0410  0.1575  0.1673  157 ILE A CD1   
1303 N  N     . LEU A 158 ? 0.8669 1.2267 1.3373 0.0591  0.2422  0.2312  158 LEU A N     
1304 C  CA    . LEU A 158 ? 0.8787 1.2454 1.3542 0.0752  0.2732  0.2485  158 LEU A CA    
1305 C  C     . LEU A 158 ? 0.7947 1.1390 1.2207 0.0955  0.2915  0.2380  158 LEU A C     
1306 O  O     . LEU A 158 ? 0.9755 1.3291 1.4129 0.1120  0.3139  0.2497  158 LEU A O     
1307 C  CB    . LEU A 158 ? 0.9392 1.3030 1.4124 0.0699  0.2805  0.2567  158 LEU A CB    
1308 C  CG    . LEU A 158 ? 1.0004 1.3796 1.5166 0.0483  0.2602  0.2638  158 LEU A CG    
1309 C  CD1   . LEU A 158 ? 1.0113 1.3764 1.5082 0.0420  0.2619  0.2635  158 LEU A CD1   
1310 C  CD2   . LEU A 158 ? 0.7950 1.2093 1.3780 0.0465  0.2669  0.2894  158 LEU A CD2   
1311 N  N     . MET A 159 ? 0.8203 1.1344 1.1918 0.0948  0.2826  0.2162  159 MET A N     
1312 C  CA    . MET A 159 ? 0.9212 1.2105 1.2429 0.1124  0.2972  0.2044  159 MET A CA    
1313 C  C     . MET A 159 ? 0.9342 1.1999 1.2184 0.1064  0.2755  0.1801  159 MET A C     
1314 O  O     . MET A 159 ? 0.9157 1.1793 1.2009 0.0899  0.2526  0.1715  159 MET A O     
1315 C  CB    . MET A 159 ? 1.0415 1.3140 1.3249 0.1226  0.3179  0.2064  159 MET A CB    
1316 C  CG    . MET A 159 ? 1.0338 1.3278 1.3516 0.1216  0.3333  0.2299  159 MET A CG    
1317 S  SD    . MET A 159 ? 1.1686 1.4414 1.4400 0.1235  0.3433  0.2287  159 MET A SD    
1318 C  CE    . MET A 159 ? 1.1477 1.4056 1.3783 0.1511  0.3772  0.2308  159 MET A CE    
1319 N  N     . ILE A 160 ? 0.8997 1.1470 1.1514 0.1206  0.2839  0.1695  160 ILE A N     
1320 C  CA    . ILE A 160 ? 0.8536 1.0762 1.0666 0.1176  0.2670  0.1474  160 ILE A CA    
1321 C  C     . ILE A 160 ? 0.9098 1.1018 1.0671 0.1318  0.2817  0.1366  160 ILE A C     
1322 O  O     . ILE A 160 ? 1.0096 1.1989 1.1604 0.1491  0.3051  0.1430  160 ILE A O     
1323 C  CB    . ILE A 160 ? 0.8762 1.1061 1.1085 0.1193  0.2581  0.1444  160 ILE A CB    
1324 C  CG1   . ILE A 160 ? 0.9862 1.2414 1.2637 0.1023  0.2367  0.1504  160 ILE A CG1   
1325 C  CG2   . ILE A 160 ? 0.8094 1.0104 0.9974 0.1212  0.2476  0.1232  160 ILE A CG2   
1326 C  CD1   . ILE A 160 ? 0.8908 1.1522 1.1831 0.1020  0.2242  0.1466  160 ILE A CD1   
1327 N  N     . SER A 161 ? 0.9890 1.1578 1.1061 0.1248  0.2679  0.1205  161 SER A N     
1328 C  CA    . SER A 161 ? 0.9528 1.0906 1.0142 0.1357  0.2769  0.1085  161 SER A CA    
1329 C  C     . SER A 161 ? 0.9693 1.0849 1.0024 0.1330  0.2596  0.0886  161 SER A C     
1330 O  O     . SER A 161 ? 0.8640 0.9871 0.9153 0.1203  0.2390  0.0837  161 SER A O     
1331 C  CB    . SER A 161 ? 0.8794 1.0085 0.9162 0.1303  0.2769  0.1092  161 SER A CB    
1332 O  OG    . SER A 161 ? 1.0466 1.1857 1.1033 0.1118  0.2558  0.1085  161 SER A OG    
1333 N  N     . TYR A 162 ? 0.9200 1.0076 0.9081 0.1453  0.2684  0.0775  162 TYR A N     
1334 C  CA    . TYR A 162 ? 0.8814 0.9452 0.8407 0.1432  0.2529  0.0590  162 TYR A CA    
1335 C  C     . TYR A 162 ? 1.0059 1.0366 0.9085 0.1528  0.2603  0.0473  162 TYR A C     
1336 O  O     . TYR A 162 ? 1.0811 1.1067 0.9669 0.1656  0.2815  0.0533  162 TYR A O     
1337 C  CB    . TYR A 162 ? 0.8916 0.9598 0.8721 0.1495  0.2535  0.0580  162 TYR A CB    
1338 C  CG    . TYR A 162 ? 1.0248 1.0838 0.9959 0.1698  0.2780  0.0609  162 TYR A CG    
1339 C  CD1   . TYR A 162 ? 0.9245 0.9493 0.8492 0.1805  0.2826  0.0458  162 TYR A CD1   
1340 C  CD2   . TYR A 162 ? 1.0574 1.1414 1.0669 0.1784  0.2964  0.0788  162 TYR A CD2   
1341 C  CE1   . TYR A 162 ? 1.0511 1.0650 0.9653 0.2001  0.3059  0.0474  162 TYR A CE1   
1342 C  CE2   . TYR A 162 ? 1.0389 1.1146 1.0409 0.1983  0.3207  0.0821  162 TYR A CE2   
1343 C  CZ    . TYR A 162 ? 1.1084 1.1480 1.0612 0.2096  0.3258  0.0657  162 TYR A CZ    
1344 O  OH    . TYR A 162 ? 1.2098 1.2386 1.1529 0.2304  0.3509  0.0679  162 TYR A OH    
1345 N  N     . ALA A 163 ? 0.9942 1.0024 0.8673 0.1465  0.2423  0.0309  163 ALA A N     
1346 C  CA    . ALA A 163 ? 1.0694 1.0449 0.8875 0.1528  0.2440  0.0184  163 ALA A CA    
1347 C  C     . ALA A 163 ? 1.1204 1.0729 0.9184 0.1492  0.2266  0.0013  163 ALA A C     
1348 O  O     . ALA A 163 ? 1.1381 1.1004 0.9593 0.1371  0.2084  -0.0010 163 ALA A O     
1349 C  CB    . ALA A 163 ? 1.0140 0.9879 0.8134 0.1442  0.2380  0.0203  163 ALA A CB    
1350 N  N     . ASP A 164 ? 1.1916 1.1126 0.9456 0.1600  0.2325  -0.0106 164 ASP A N     
1351 C  CA    . ASP A 164 ? 1.1771 1.0715 0.9073 0.1570  0.2163  -0.0273 164 ASP A CA    
1352 C  C     . ASP A 164 ? 1.2819 1.1402 0.9541 0.1649  0.2193  -0.0400 164 ASP A C     
1353 O  O     . ASP A 164 ? 1.2960 1.1512 0.9436 0.1666  0.2254  -0.0368 164 ASP A O     
1354 C  CB    . ASP A 164 ? 1.2253 1.1209 0.9790 0.1636  0.2198  -0.0285 164 ASP A CB    
1355 C  CG    . ASP A 164 ? 1.2726 1.1617 1.0204 0.1833  0.2461  -0.0250 164 ASP A CG    
1356 O  OD1   . ASP A 164 ? 1.4038 1.2747 1.1135 0.1938  0.2602  -0.0280 164 ASP A OD1   
1357 O  OD2   . ASP A 164 ? 1.2131 1.1161 0.9951 0.1889  0.2531  -0.0186 164 ASP A OD2   
1358 N  N     . GLU A 165 ? 1.3192 1.1491 0.9685 0.1698  0.2146  -0.0543 165 GLU A N     
1359 C  CA    . GLU A 165 ? 1.4237 1.2161 1.0154 0.1774  0.2161  -0.0681 165 GLU A CA    
1360 C  C     . GLU A 165 ? 1.5175 1.2995 1.0871 0.1976  0.2445  -0.0659 165 GLU A C     
1361 O  O     . GLU A 165 ? 1.4290 1.1805 0.9463 0.2053  0.2485  -0.0763 165 GLU A O     
1362 C  CB    . GLU A 165 ? 1.3904 1.1536 0.9654 0.1746  0.1998  -0.0849 165 GLU A CB    
1363 C  CG    . GLU A 165 ? 1.5924 1.3225 1.1154 0.1698  0.1843  -0.0994 165 GLU A CG    
1364 C  CD    . GLU A 165 ? 1.7280 1.4706 1.2601 0.1509  0.1604  -0.0972 165 GLU A CD    
1365 O  OE1   . GLU A 165 ? 1.5337 1.3096 1.1085 0.1422  0.1578  -0.0848 165 GLU A OE1   
1366 O  OE2   . GLU A 165 ? 1.7409 1.4592 1.2374 0.1448  0.1439  -0.1081 165 GLU A OE2   
1367 N  N     . GLU A 166 ? 1.4763 1.2828 1.0839 0.2066  0.2641  -0.0523 166 GLU A N     
1368 C  CA    . GLU A 166 ? 1.4335 1.2354 1.0266 0.2266  0.2938  -0.0468 166 GLU A CA    
1369 C  C     . GLU A 166 ? 1.4498 1.2766 1.0517 0.2273  0.3076  -0.0297 166 GLU A C     
1370 O  O     . GLU A 166 ? 1.3334 1.1611 0.9273 0.2440  0.3343  -0.0218 166 GLU A O     
1371 C  CB    . GLU A 166 ? 1.3957 1.2099 1.0277 0.2377  0.3090  -0.0401 166 GLU A CB    
1372 C  CG    . GLU A 166 ? 1.6146 1.3927 1.2197 0.2497  0.3123  -0.0563 166 GLU A CG    
1373 C  CD    . GLU A 166 ? 1.7548 1.5263 1.3749 0.2366  0.2868  -0.0661 166 GLU A CD    
1374 O  OE1   . GLU A 166 ? 1.8417 1.5824 1.4237 0.2302  0.2693  -0.0828 166 GLU A OE1   
1375 O  OE2   . GLU A 166 ? 1.6712 1.4689 1.3417 0.2325  0.2839  -0.0563 166 GLU A OE2   
1376 N  N     . GLY A 167 ? 1.4290 1.2758 1.0483 0.2104  0.2911  -0.0233 167 GLY A N     
1377 C  CA    . GLY A 167 ? 1.3806 1.2508 1.0116 0.2091  0.3018  -0.0066 167 GLY A CA    
1378 C  C     . GLY A 167 ? 1.2187 1.1299 0.9148 0.1999  0.3006  0.0102  167 GLY A C     
1379 O  O     . GLY A 167 ? 1.1551 1.0771 0.8849 0.1922  0.2877  0.0083  167 GLY A O     
1380 N  N     . ALA A 168 ? 1.1089 1.0425 0.8220 0.2007  0.3140  0.0273  168 ALA A N     
1381 C  CA    . ALA A 168 ? 1.1854 1.1571 0.9587 0.1911  0.3126  0.0442  168 ALA A CA    
1382 C  C     . ALA A 168 ? 1.1766 1.1684 0.9790 0.2055  0.3404  0.0615  168 ALA A C     
1383 O  O     . ALA A 168 ? 1.3024 1.2829 1.0761 0.2215  0.3635  0.0650  168 ALA A O     
1384 C  CB    . ALA A 168 ? 1.0994 1.0836 0.8777 0.1772  0.3024  0.0518  168 ALA A CB    
1385 N  N     . ARG A 169 ? 0.9018 0.9238 0.7616 0.1998  0.3380  0.0728  169 ARG A N     
1386 C  CA    . ARG A 169 ? 1.0595 1.1061 0.9581 0.2113  0.3619  0.0918  169 ARG A CA    
1387 C  C     . ARG A 169 ? 1.1044 1.1887 1.0634 0.1961  0.3522  0.1079  169 ARG A C     
1388 O  O     . ARG A 169 ? 1.0549 1.1442 1.0263 0.1785  0.3271  0.1019  169 ARG A O     
1389 C  CB    . ARG A 169 ? 1.0704 1.1116 0.9777 0.2249  0.3715  0.0880  169 ARG A CB    
1390 C  CG    . ARG A 169 ? 1.1293 1.1303 0.9776 0.2405  0.3810  0.0707  169 ARG A CG    
1391 C  CD    . ARG A 169 ? 1.2118 1.2075 1.0408 0.2618  0.4144  0.0799  169 ARG A CD    
1392 N  NE    . ARG A 169 ? 1.1171 1.1207 0.9736 0.2781  0.4345  0.0874  169 ARG A NE    
1393 C  CZ    . ARG A 169 ? 1.2539 1.2789 1.1376 0.2918  0.4623  0.1074  169 ARG A CZ    
1394 N  NH1   . ARG A 169 ? 1.2145 1.2549 1.1014 0.2912  0.4741  0.1225  169 ARG A NH1   
1395 N  NH2   . ARG A 169 ? 1.3033 1.3349 1.2136 0.3066  0.4790  0.1138  169 ARG A NH2   
1396 N  N     . VAL A 170 ? 1.1174 1.2276 1.1141 0.2034  0.3727  0.1289  170 VAL A N     
1397 C  CA    . VAL A 170 ? 1.0955 1.2420 1.1527 0.1898  0.3652  0.1460  170 VAL A CA    
1398 C  C     . VAL A 170 ? 1.0898 1.2608 1.1953 0.1993  0.3795  0.1610  170 VAL A C     
1399 O  O     . VAL A 170 ? 1.0955 1.2609 1.1911 0.2190  0.4050  0.1659  170 VAL A O     
1400 C  CB    . VAL A 170 ? 1.1084 1.2669 1.1716 0.1857  0.3741  0.1611  170 VAL A CB    
1401 C  CG1   . VAL A 170 ? 1.0821 1.2744 1.2069 0.1689  0.3618  0.1762  170 VAL A CG1   
1402 C  CG2   . VAL A 170 ? 1.1484 1.2811 1.1602 0.1794  0.3629  0.1476  170 VAL A CG2   
1403 N  N     . ILE A 171 ? 1.0916 1.2896 1.2492 0.1854  0.3627  0.1685  171 ILE A N     
1404 C  CA    . ILE A 171 ? 1.0361 1.2622 1.2474 0.1915  0.3720  0.1849  171 ILE A CA    
1405 C  C     . ILE A 171 ? 1.0771 1.3383 1.3452 0.1765  0.3643  0.2040  171 ILE A C     
1406 O  O     . ILE A 171 ? 0.9957 1.2609 1.2726 0.1570  0.3387  0.1980  171 ILE A O     
1407 C  CB    . ILE A 171 ? 0.9690 1.1922 1.1886 0.1898  0.3560  0.1741  171 ILE A CB    
1408 C  CG1   . ILE A 171 ? 0.9964 1.1806 1.1569 0.1997  0.3567  0.1519  171 ILE A CG1   
1409 C  CG2   . ILE A 171 ? 1.1469 1.3955 1.4156 0.2008  0.3703  0.1917  171 ILE A CG2   
1410 C  CD1   . ILE A 171 ? 1.0298 1.2075 1.1929 0.1945  0.3365  0.1393  171 ILE A CD1   
1411 N  N     . THR A 172 ? 1.1343 1.4200 1.4409 0.1856  0.3867  0.2270  172 THR A N     
1412 C  CA    . THR A 172 ? 1.1473 1.4675 1.5129 0.1720  0.3809  0.2475  172 THR A CA    
1413 C  C     . THR A 172 ? 1.0831 1.4327 1.5010 0.1844  0.4016  0.2709  172 THR A C     
1414 O  O     . THR A 172 ? 1.0826 1.4238 1.4864 0.2048  0.4232  0.2712  172 THR A O     
1415 C  CB    . THR A 172 ? 1.0416 1.3600 1.3961 0.1668  0.3877  0.2546  172 THR A CB    
1416 O  OG1   . THR A 172 ? 1.0464 1.3990 1.4633 0.1554  0.3854  0.2771  172 THR A OG1   
1417 C  CG2   . THR A 172 ? 1.0762 1.3800 1.3941 0.1886  0.4207  0.2595  172 THR A CG2   
1418 N  N     . TRP A 173 ? 1.1053 1.4893 1.5853 0.1720  0.3947  0.2910  173 TRP A N     
1419 C  CA    . TRP A 173 ? 1.1430 1.5589 1.6799 0.1824  0.4128  0.3158  173 TRP A CA    
1420 C  C     . TRP A 173 ? 1.2043 1.6274 1.7547 0.1868  0.4310  0.3358  173 TRP A C     
1421 O  O     . TRP A 173 ? 1.3733 1.8018 1.9410 0.1998  0.4457  0.3496  173 TRP A O     
1422 C  CB    . TRP A 173 ? 1.1627 1.6087 1.7603 0.1652  0.3868  0.3242  173 TRP A CB    
1423 C  CG    . TRP A 173 ? 1.2044 1.6710 1.8413 0.1427  0.3682  0.3346  173 TRP A CG    
1424 C  CD1   . TRP A 173 ? 1.1884 1.6743 1.8645 0.1394  0.3763  0.3571  173 TRP A CD1   
1425 C  CD2   . TRP A 173 ? 1.1611 1.6226 1.7951 0.1194  0.3333  0.3200  173 TRP A CD2   
1426 N  NE1   . TRP A 173 ? 1.2433 1.7441 1.9510 0.1162  0.3536  0.3604  173 TRP A NE1   
1427 C  CE2   . TRP A 173 ? 1.2846 1.7683 1.9639 0.1037  0.3261  0.3365  173 TRP A CE2   
1428 C  CE3   . TRP A 173 ? 1.0092 1.4488 1.6065 0.1107  0.3083  0.2948  173 TRP A CE3   
1429 C  CZ2   . TRP A 173 ? 1.2279 1.7105 1.9144 0.0801  0.2947  0.3271  173 TRP A CZ2   
1430 C  CZ3   . TRP A 173 ? 1.1072 1.5474 1.7118 0.0881  0.2785  0.2865  173 TRP A CZ3   
1431 C  CH2   . TRP A 173 ? 1.2238 1.6842 1.8712 0.0732  0.2718  0.3018  173 TRP A CH2   
1432 N  N     . LYS A 174 ? 1.1457 1.5669 1.6873 0.1765  0.4292  0.3378  174 LYS A N     
1433 C  CA    . LYS A 174 ? 1.0454 1.4661 1.5873 0.1829  0.4471  0.3543  174 LYS A CA    
1434 C  C     . LYS A 174 ? 1.1112 1.4996 1.5867 0.2043  0.4714  0.3442  174 LYS A C     
1435 O  O     . LYS A 174 ? 1.1242 1.4879 1.5473 0.2076  0.4702  0.3230  174 LYS A O     
1436 C  CB    . LYS A 174 ? 0.9461 1.3745 1.5016 0.1644  0.4361  0.3603  174 LYS A CB    
1437 C  CG    . LYS A 174 ? 1.0174 1.4671 1.6223 0.1597  0.4396  0.3859  174 LYS A CG    
1438 C  CD    . LYS A 174 ? 0.9752 1.4404 1.6173 0.1347  0.4168  0.3910  174 LYS A CD    
1439 C  CE    . LYS A 174 ? 1.0178 1.5093 1.7205 0.1195  0.3932  0.3974  174 LYS A CE    
1440 N  NZ    . LYS A 174 ? 1.0168 1.5232 1.7621 0.0968  0.3737  0.4073  174 LYS A NZ    
1441 N  N     . ASN A 175 ? 1.2721 1.6599 1.7492 0.2188  0.4927  0.3594  175 ASN A N     
1442 C  CA    . ASN A 175 ? 1.3151 1.6718 1.7301 0.2403  0.5157  0.3504  175 ASN A CA    
1443 C  C     . ASN A 175 ? 1.2732 1.6108 1.6399 0.2375  0.5181  0.3427  175 ASN A C     
1444 O  O     . ASN A 175 ? 1.3395 1.6862 1.7199 0.2338  0.5236  0.3588  175 ASN A O     
1445 C  CB    . ASN A 175 ? 1.1255 1.4885 1.5585 0.2566  0.5380  0.3703  175 ASN A CB    
1446 C  CG    . ASN A 175 ? 1.3968 1.7272 1.7646 0.2781  0.5617  0.3619  175 ASN A CG    
1447 O  OD1   . ASN A 175 ? 1.3470 1.6481 1.6577 0.2842  0.5612  0.3386  175 ASN A OD1   
1448 N  ND2   . ASN A 175 ? 1.6559 1.9906 2.0316 0.2896  0.5818  0.3808  175 ASN A ND2   
1449 N  N     . VAL A 176 ? 1.2543 1.5648 1.5648 0.2393  0.5133  0.3188  176 VAL A N     
1450 C  CA    . VAL A 176 ? 1.2828 1.5693 1.5363 0.2397  0.5163  0.3093  176 VAL A CA    
1451 C  C     . VAL A 176 ? 1.2187 1.4700 1.4061 0.2610  0.5328  0.2942  176 VAL A C     
1452 O  O     . VAL A 176 ? 1.2475 1.4828 1.4133 0.2675  0.5298  0.2768  176 VAL A O     
1453 C  CB    . VAL A 176 ? 1.2496 1.5322 1.4910 0.2225  0.4949  0.2941  176 VAL A CB    
1454 C  CG1   . VAL A 176 ? 1.2145 1.4617 1.3797 0.2287  0.4978  0.2759  176 VAL A CG1   
1455 C  CG2   . VAL A 176 ? 1.0068 1.3160 1.2976 0.2020  0.4822  0.3099  176 VAL A CG2   
1456 N  N     . ASP A 177 ? 1.2236 1.4625 1.3798 0.2718  0.5496  0.3011  177 ASP A N     
1457 C  CA    . ASP A 177 ? 1.4649 1.6705 1.5597 0.2924  0.5661  0.2887  177 ASP A CA    
1458 C  C     . ASP A 177 ? 1.4481 1.6219 1.4733 0.2903  0.5578  0.2672  177 ASP A C     
1459 O  O     . ASP A 177 ? 1.3234 1.4922 1.3250 0.2880  0.5602  0.2724  177 ASP A O     
1460 C  CB    . ASP A 177 ? 1.5297 1.7397 1.6287 0.3062  0.5891  0.3085  177 ASP A CB    
1461 C  CG    . ASP A 177 ? 1.6596 1.8326 1.6855 0.3250  0.6045  0.2954  177 ASP A CG    
1462 O  OD1   . ASP A 177 ? 1.7513 1.8988 1.7406 0.3339  0.6039  0.2750  177 ASP A OD1   
1463 O  OD2   . ASP A 177 ? 1.6008 1.7697 1.6060 0.3307  0.6166  0.3055  177 ASP A OD2   
1464 N  N     . LEU A 178 ? 1.4105 1.5625 1.4035 0.2910  0.5472  0.2438  178 LEU A N     
1465 C  CA    . LEU A 178 ? 1.3920 1.5110 1.3175 0.2894  0.5372  0.2215  178 LEU A CA    
1466 C  C     . LEU A 178 ? 1.4487 1.5388 1.3378 0.2991  0.5344  0.1981  178 LEU A C     
1467 O  O     . LEU A 178 ? 1.4589 1.5602 1.3843 0.3019  0.5350  0.1989  178 LEU A O     
1468 C  CB    . LEU A 178 ? 1.3582 1.4883 1.2958 0.2689  0.5165  0.2192  178 LEU A CB    
1469 C  CG    . LEU A 178 ? 1.2905 1.4326 1.2337 0.2595  0.5164  0.2347  178 LEU A CG    
1470 C  CD1   . LEU A 178 ? 1.1644 1.3361 1.1623 0.2387  0.5007  0.2443  178 LEU A CD1   
1471 C  CD2   . LEU A 178 ? 1.4082 1.5175 1.2787 0.2615  0.5122  0.2202  178 LEU A CD2   
1472 N  N     . PRO A 179 ? 1.4882 1.5403 1.3066 0.3040  0.5301  0.1771  179 PRO A N     
1473 C  CA    . PRO A 179 ? 1.4943 1.5151 1.2762 0.3135  0.5273  0.1543  179 PRO A CA    
1474 C  C     . PRO A 179 ? 1.3825 1.4042 1.1779 0.3025  0.5077  0.1405  179 PRO A C     
1475 O  O     . PRO A 179 ? 1.3208 1.3217 1.1000 0.3100  0.5057  0.1246  179 PRO A O     
1476 C  CB    . PRO A 179 ? 1.5250 1.5065 1.2288 0.3191  0.5255  0.1376  179 PRO A CB    
1477 C  CG    . PRO A 179 ? 1.4809 1.4738 1.1814 0.3059  0.5170  0.1461  179 PRO A CG    
1478 C  CD    . PRO A 179 ? 1.4555 1.4905 1.2239 0.3018  0.5278  0.1743  179 PRO A CD    
1479 N  N     . TYR A 180 ? 1.3394 1.3832 1.1640 0.2849  0.4926  0.1459  180 TYR A N     
1480 C  CA    . TYR A 180 ? 1.2639 1.3063 1.1054 0.2677  0.4608  0.1311  180 TYR A CA    
1481 C  C     . TYR A 180 ? 1.2613 1.3436 1.1790 0.2556  0.4526  0.1469  180 TYR A C     
1482 O  O     . TYR A 180 ? 1.2858 1.3732 1.2228 0.2379  0.4247  0.1385  180 TYR A O     
1483 C  CB    . TYR A 180 ? 1.1920 1.2181 1.0002 0.2504  0.4337  0.1173  180 TYR A CB    
1484 C  CG    . TYR A 180 ? 1.2788 1.3245 1.1020 0.2399  0.4330  0.1335  180 TYR A CG    
1485 C  CD1   . TYR A 180 ? 1.1859 1.2639 1.0686 0.2226  0.4193  0.1460  180 TYR A CD1   
1486 C  CD2   . TYR A 180 ? 1.4316 1.4623 1.2087 0.2475  0.4456  0.1363  180 TYR A CD2   
1487 C  CE1   . TYR A 180 ? 1.0390 1.1329 0.9369 0.2129  0.4185  0.1607  180 TYR A CE1   
1488 C  CE2   . TYR A 180 ? 1.3296 1.3779 1.1219 0.2382  0.4453  0.1523  180 TYR A CE2   
1489 C  CZ    . TYR A 180 ? 1.2245 1.3039 1.0782 0.2209  0.4319  0.1644  180 TYR A CZ    
1490 O  OH    . TYR A 180 ? 1.3249 1.4199 1.1950 0.2115  0.4314  0.1802  180 TYR A OH    
1491 N  N     . VAL A 181 ? 1.2172 1.3279 1.1785 0.2648  0.4760  0.1700  181 VAL A N     
1492 C  CA    . VAL A 181 ? 1.2045 1.3546 1.2399 0.2533  0.4685  0.1871  181 VAL A CA    
1493 C  C     . VAL A 181 ? 1.1395 1.3005 1.2058 0.2687  0.4854  0.1943  181 VAL A C     
1494 O  O     . VAL A 181 ? 1.2702 1.4197 1.3177 0.2878  0.5092  0.1980  181 VAL A O     
1495 C  CB    . VAL A 181 ? 1.2550 1.4345 1.3267 0.2476  0.4784  0.2117  181 VAL A CB    
1496 C  CG1   . VAL A 181 ? 1.1209 1.3392 1.2689 0.2336  0.4666  0.2278  181 VAL A CG1   
1497 C  CG2   . VAL A 181 ? 1.2210 1.3876 1.2602 0.2340  0.4632  0.2050  181 VAL A CG2   
1498 N  N     . ASP A 182 ? 1.1221 1.3015 1.2340 0.2577  0.4665  0.1947  182 ASP A N     
1499 C  CA    . ASP A 182 ? 1.1114 1.3065 1.2628 0.2696  0.4785  0.2041  182 ASP A CA    
1500 C  C     . ASP A 182 ? 1.1287 1.3689 1.3561 0.2575  0.4727  0.2277  182 ASP A C     
1501 O  O     . ASP A 182 ? 1.0436 1.2961 1.2947 0.2362  0.4438  0.2246  182 ASP A O     
1502 C  CB    . ASP A 182 ? 1.1358 1.3115 1.2729 0.2678  0.4599  0.1838  182 ASP A CB    
1503 C  CG    . ASP A 182 ? 1.2289 1.3586 1.2921 0.2766  0.4610  0.1592  182 ASP A CG    
1504 O  OD1   . ASP A 182 ? 1.0387 1.1505 1.0657 0.2951  0.4872  0.1594  182 ASP A OD1   
1505 O  OD2   . ASP A 182 ? 1.1462 1.2574 1.1874 0.2648  0.4354  0.1399  182 ASP A OD2   
1506 N  N     . VAL A 183 ? 1.2049 1.4643 1.4663 0.2680  0.4930  0.2491  183 VAL A N     
1507 C  CA    . VAL A 183 ? 1.1982 1.4985 1.5319 0.2562  0.4862  0.2727  183 VAL A CA    
1508 C  C     . VAL A 183 ? 1.0499 1.3663 1.4264 0.2595  0.4814  0.2782  183 VAL A C     
1509 O  O     . VAL A 183 ? 0.9741 1.2719 1.3305 0.2766  0.4938  0.2721  183 VAL A O     
1510 C  CB    . VAL A 183 ? 1.1500 1.4590 1.4966 0.2618  0.5037  0.2933  183 VAL A CB    
1511 C  CG1   . VAL A 183 ? 1.1479 1.4960 1.5634 0.2443  0.4914  0.3151  183 VAL A CG1   
1512 C  CG2   . VAL A 183 ? 1.0829 1.3670 1.3722 0.2650  0.5130  0.2855  183 VAL A CG2   
1513 N  N     . VAL A 184 ? 0.9720 1.3223 1.4074 0.2426  0.4622  0.2895  184 VAL A N     
1514 C  CA    . VAL A 184 ? 0.9894 1.3601 1.4720 0.2425  0.4534  0.2976  184 VAL A CA    
1515 C  C     . VAL A 184 ? 1.0617 1.4698 1.6112 0.2300  0.4453  0.3227  184 VAL A C     
1516 O  O     . VAL A 184 ? 1.1411 1.5570 1.6989 0.2227  0.4480  0.3332  184 VAL A O     
1517 C  CB    . VAL A 184 ? 1.0646 1.4332 1.5443 0.2318  0.4286  0.2808  184 VAL A CB    
1518 C  CG1   . VAL A 184 ? 0.8675 1.1915 1.2762 0.2417  0.4306  0.2540  184 VAL A CG1   
1519 C  CG2   . VAL A 184 ? 0.9762 1.3529 1.4643 0.2051  0.3981  0.2764  184 VAL A CG2   
1520 N  N     . SER A 185 ? 1.1110 1.5413 1.7081 0.2272  0.4341  0.3327  185 SER A N     
1521 C  CA    . SER A 185 ? 1.1431 1.6070 1.8035 0.2159  0.4251  0.3568  185 SER A CA    
1522 C  C     . SER A 185 ? 1.0228 1.5072 1.7116 0.1902  0.3975  0.3570  185 SER A C     
1523 O  O     . SER A 185 ? 1.0488 1.5465 1.7619 0.1795  0.3951  0.3702  185 SER A O     
1524 C  CB    . SER A 185 ? 1.0037 1.4832 1.7034 0.2217  0.4217  0.3679  185 SER A CB    
1525 O  OG    . SER A 185 ? 1.1713 1.6293 1.8435 0.2454  0.4469  0.3663  185 SER A OG    
1526 N  N     . THR A 186 ? 0.9800 1.4659 1.6659 0.1802  0.3764  0.3425  186 THR A N     
1527 C  CA    . THR A 186 ? 1.0509 1.5572 1.7674 0.1555  0.3476  0.3427  186 THR A CA    
1528 C  C     . THR A 186 ? 1.0574 1.5303 1.7148 0.1456  0.3261  0.3128  186 THR A C     
1529 O  O     . THR A 186 ? 1.1638 1.6057 1.7673 0.1583  0.3355  0.2951  186 THR A O     
1530 C  CB    . THR A 186 ? 1.1865 1.7206 1.9575 0.1456  0.3254  0.3545  186 THR A CB    
1531 O  OG1   . THR A 186 ? 1.3173 1.8686 2.1161 0.1205  0.2965  0.3548  186 THR A OG1   
1532 C  CG2   . THR A 186 ? 1.1023 1.6300 1.8604 0.1538  0.3197  0.3430  186 THR A CG2   
1533 N  N     . GLU A 187 ? 1.0169 1.4956 1.6853 0.1224  0.2961  0.3073  187 GLU A N     
1534 C  CA    . GLU A 187 ? 0.9456 1.3969 1.5661 0.1109  0.2721  0.2807  187 GLU A CA    
1535 C  C     . GLU A 187 ? 1.0078 1.4485 1.6103 0.1183  0.2647  0.2686  187 GLU A C     
1536 O  O     . GLU A 187 ? 1.0012 1.4105 1.5497 0.1223  0.2628  0.2474  187 GLU A O     
1537 C  CB    . GLU A 187 ? 0.8015 1.2657 1.4472 0.0859  0.2415  0.2800  187 GLU A CB    
1538 C  CG    . GLU A 187 ? 0.7970 1.2344 1.3959 0.0738  0.2179  0.2542  187 GLU A CG    
1539 C  CD    . GLU A 187 ? 0.8676 1.3081 1.4773 0.0525  0.1976  0.2521  187 GLU A CD    
1540 O  OE1   . GLU A 187 ? 0.7486 1.2113 1.4004 0.0381  0.1772  0.2599  187 GLU A OE1   
1541 O  OE2   . GLU A 187 ? 1.0117 1.4314 1.5873 0.0501  0.2014  0.2425  187 GLU A OE2   
1542 N  N     . ARG A 188 ? 0.9850 1.4524 1.6348 0.1193  0.2592  0.2828  188 ARG A N     
1543 C  CA    . ARG A 188 ? 0.8620 1.3222 1.5008 0.1262  0.2519  0.2743  188 ARG A CA    
1544 C  C     . ARG A 188 ? 0.7681 1.1995 1.3623 0.1481  0.2769  0.2642  188 ARG A C     
1545 O  O     . ARG A 188 ? 0.8477 1.2500 1.3943 0.1488  0.2690  0.2430  188 ARG A O     
1546 C  CB    . ARG A 188 ? 1.0026 1.4986 1.7036 0.1281  0.2488  0.2963  188 ARG A CB    
1547 C  CG    . ARG A 188 ? 1.0162 1.5054 1.7093 0.1410  0.2499  0.2921  188 ARG A CG    
1548 C  CD    . ARG A 188 ? 1.0660 1.5920 1.8224 0.1420  0.2443  0.3148  188 ARG A CD    
1549 N  NE    . ARG A 188 ? 1.2102 1.7345 1.9613 0.1369  0.2209  0.3067  188 ARG A NE    
1550 C  CZ    . ARG A 188 ? 1.0525 1.5874 1.8128 0.1164  0.1884  0.3030  188 ARG A CZ    
1551 N  NH1   . ARG A 188 ? 0.9973 1.5452 1.7752 0.0983  0.1739  0.3063  188 ARG A NH1   
1552 N  NH2   . ARG A 188 ? 0.9857 1.5174 1.7369 0.1145  0.1703  0.2962  188 ARG A NH2   
1553 N  N     . GLU A 189 ? 0.8984 1.3368 1.5075 0.1662  0.3076  0.2794  189 GLU A N     
1554 C  CA    . GLU A 189 ? 0.9990 1.4083 1.5645 0.1882  0.3330  0.2697  189 GLU A CA    
1555 C  C     . GLU A 189 ? 0.8961 1.2684 1.3956 0.1859  0.3326  0.2469  189 GLU A C     
1556 O  O     . GLU A 189 ? 0.9201 1.2613 1.3735 0.1990  0.3425  0.2315  189 GLU A O     
1557 C  CB    . GLU A 189 ? 1.0095 1.4332 1.6012 0.2078  0.3677  0.2907  189 GLU A CB    
1558 C  CG    . GLU A 189 ? 1.0128 1.4750 1.6742 0.2126  0.3716  0.3163  189 GLU A CG    
1559 C  CD    . GLU A 189 ? 1.1222 1.5913 1.7999 0.2063  0.3473  0.3124  189 GLU A CD    
1560 O  OE1   . GLU A 189 ? 0.9540 1.3973 1.5970 0.2172  0.3498  0.2975  189 GLU A OE1   
1561 O  OE2   . GLU A 189 ? 1.2922 1.7923 2.0182 0.1903  0.3253  0.3249  189 GLU A OE2   
1562 N  N     . MET A 190 ? 0.8748 1.2489 1.3695 0.1694  0.3206  0.2447  190 MET A N     
1563 C  CA    . MET A 190 ? 0.9447 1.2854 1.3793 0.1656  0.3168  0.2238  190 MET A CA    
1564 C  C     . MET A 190 ? 0.9400 1.2620 1.3459 0.1547  0.2899  0.2024  190 MET A C     
1565 O  O     . MET A 190 ? 0.8856 1.1765 1.2434 0.1625  0.2926  0.1848  190 MET A O     
1566 C  CB    . MET A 190 ? 0.9477 1.2968 1.3895 0.1519  0.3128  0.2296  190 MET A CB    
1567 C  CG    . MET A 190 ? 0.8795 1.1962 1.2617 0.1512  0.3144  0.2123  190 MET A CG    
1568 S  SD    . MET A 190 ? 0.8624 1.1854 1.2514 0.1288  0.2969  0.2132  190 MET A SD    
1569 C  CE    . MET A 190 ? 0.8375 1.1883 1.2794 0.1091  0.2666  0.2179  190 MET A CE    
1570 N  N     . ILE A 191 ? 0.8510 1.1913 1.2856 0.1363  0.2635  0.2039  191 ILE A N     
1571 C  CA    . ILE A 191 ? 0.7556 1.0811 1.1661 0.1262  0.2387  0.1857  191 ILE A CA    
1572 C  C     . ILE A 191 ? 0.8380 1.1544 1.2412 0.1397  0.2432  0.1816  191 ILE A C     
1573 O  O     . ILE A 191 ? 0.8743 1.1641 1.2371 0.1406  0.2358  0.1636  191 ILE A O     
1574 C  CB    . ILE A 191 ? 0.6546 1.0034 1.0999 0.1059  0.2113  0.1900  191 ILE A CB    
1575 C  CG1   . ILE A 191 ? 0.6647 1.0212 1.1202 0.0928  0.2076  0.1946  191 ILE A CG1   
1576 C  CG2   . ILE A 191 ? 0.8417 1.1746 1.2588 0.0963  0.1874  0.1715  191 ILE A CG2   
1577 C  CD1   . ILE A 191 ? 0.6965 1.0796 1.1961 0.0747  0.1848  0.2033  191 ILE A CD1   
1578 N  N     . LYS A 192 ? 0.7332 1.0718 1.1777 0.1505  0.2554  0.1993  192 LYS A N     
1579 C  CA    . LYS A 192 ? 0.8255 1.1550 1.2659 0.1654  0.2626  0.1972  192 LYS A CA    
1580 C  C     . LYS A 192 ? 0.8519 1.1459 1.2424 0.1824  0.2842  0.1841  192 LYS A C     
1581 O  O     . LYS A 192 ? 0.7339 1.0042 1.0961 0.1885  0.2814  0.1705  192 LYS A O     
1582 C  CB    . LYS A 192 ? 0.7950 1.1567 1.2927 0.1749  0.2741  0.2210  192 LYS A CB    
1583 C  CG    . LYS A 192 ? 0.9395 1.3084 1.4564 0.1779  0.2632  0.2236  192 LYS A CG    
1584 C  CD    . LYS A 192 ? 0.9720 1.3697 1.5429 0.1914  0.2798  0.2478  192 LYS A CD    
1585 C  CE    . LYS A 192 ? 0.9341 1.3688 1.5586 0.1774  0.2563  0.2634  192 LYS A CE    
1586 N  NZ    . LYS A 192 ? 0.8285 1.2930 1.5092 0.1907  0.2713  0.2886  192 LYS A NZ    
1587 N  N     . ARG A 193 ? 0.9018 1.1908 1.2800 0.1901  0.3055  0.1880  193 ARG A N     
1588 C  CA    . ARG A 193 ? 0.9877 1.2411 1.3134 0.2058  0.3250  0.1745  193 ARG A CA    
1589 C  C     . ARG A 193 ? 0.9139 1.1358 1.1866 0.1955  0.3072  0.1507  193 ARG A C     
1590 O  O     . ARG A 193 ? 0.9698 1.1609 1.2036 0.2045  0.3103  0.1354  193 ARG A O     
1591 C  CB    . ARG A 193 ? 0.9539 1.2106 1.2767 0.2152  0.3506  0.1851  193 ARG A CB    
1592 C  CG    . ARG A 193 ? 1.0750 1.2940 1.3339 0.2235  0.3627  0.1683  193 ARG A CG    
1593 C  CD    . ARG A 193 ? 1.2357 1.4282 1.4666 0.2453  0.3820  0.1603  193 ARG A CD    
1594 N  NE    . ARG A 193 ? 1.3869 1.5513 1.5672 0.2584  0.4032  0.1524  193 ARG A NE    
1595 C  CZ    . ARG A 193 ? 1.4619 1.5953 1.6045 0.2774  0.4207  0.1416  193 ARG A CZ    
1596 N  NH1   . ARG A 193 ? 1.4859 1.6114 1.6371 0.2859  0.4205  0.1376  193 ARG A NH1   
1597 N  NH2   . ARG A 193 ? 1.2835 1.3920 1.3778 0.2882  0.4385  0.1347  193 ARG A NH2   
1598 N  N     . PHE A 194 ? 0.8496 1.0785 1.1217 0.1767  0.2884  0.1478  194 PHE A N     
1599 C  CA    . PHE A 194 ? 0.9529 1.1547 1.1791 0.1666  0.2713  0.1271  194 PHE A CA    
1600 C  C     . PHE A 194 ? 0.9074 1.0987 1.1266 0.1636  0.2540  0.1158  194 PHE A C     
1601 O  O     . PHE A 194 ? 0.8959 1.0569 1.0723 0.1650  0.2495  0.0985  194 PHE A O     
1602 C  CB    . PHE A 194 ? 0.9103 1.1247 1.1448 0.1472  0.2543  0.1281  194 PHE A CB    
1603 C  CG    . PHE A 194 ? 0.9003 1.0918 1.0958 0.1356  0.2346  0.1089  194 PHE A CG    
1604 C  CD1   . PHE A 194 ? 0.9629 1.1233 1.1082 0.1412  0.2411  0.0954  194 PHE A CD1   
1605 C  CD2   . PHE A 194 ? 0.8399 1.0409 1.0489 0.1193  0.2097  0.1050  194 PHE A CD2   
1606 C  CE1   . PHE A 194 ? 0.8012 0.9425 0.9147 0.1305  0.2229  0.0795  194 PHE A CE1   
1607 C  CE2   . PHE A 194 ? 0.6818 0.8630 0.8573 0.1097  0.1933  0.0888  194 PHE A CE2   
1608 C  CZ    . PHE A 194 ? 0.7659 0.9181 0.8957 0.1151  0.1999  0.0766  194 PHE A CZ    
1609 N  N     . LEU A 195 ? 0.8797 1.0963 1.1414 0.1591  0.2435  0.1262  195 LEU A N     
1610 C  CA    . LEU A 195 ? 0.8512 1.0600 1.1097 0.1584  0.2295  0.1186  195 LEU A CA    
1611 C  C     . LEU A 195 ? 0.9220 1.1058 1.1585 0.1771  0.2465  0.1126  195 LEU A C     
1612 O  O     . LEU A 195 ? 0.9926 1.1517 1.1998 0.1769  0.2376  0.0980  195 LEU A O     
1613 C  CB    . LEU A 195 ? 0.7727 1.0152 1.0824 0.1526  0.2179  0.1338  195 LEU A CB    
1614 C  CG    . LEU A 195 ? 0.8270 1.0901 1.1550 0.1323  0.1957  0.1364  195 LEU A CG    
1615 C  CD1   . LEU A 195 ? 0.9649 1.2639 1.3471 0.1284  0.1882  0.1549  195 LEU A CD1   
1616 C  CD2   . LEU A 195 ? 0.9204 1.1660 1.2182 0.1216  0.1744  0.1197  195 LEU A CD2   
1617 N  N     . ARG A 196 ? 1.0044 1.1937 1.2556 0.1937  0.2714  0.1240  196 ARG A N     
1618 C  CA    . ARG A 196 ? 1.0436 1.2065 1.2724 0.2131  0.2897  0.1176  196 ARG A CA    
1619 C  C     . ARG A 196 ? 0.9363 1.0588 1.1043 0.2150  0.2914  0.0965  196 ARG A C     
1620 O  O     . ARG A 196 ? 0.9469 1.0404 1.0880 0.2237  0.2935  0.0842  196 ARG A O     
1621 C  CB    . ARG A 196 ? 0.8769 1.0528 1.1298 0.2312  0.3187  0.1340  196 ARG A CB    
1622 C  CG    . ARG A 196 ? 0.9368 1.1275 1.2296 0.2432  0.3260  0.1469  196 ARG A CG    
1623 C  CD    . ARG A 196 ? 0.8836 1.1069 1.2236 0.2526  0.3461  0.1708  196 ARG A CD    
1624 N  NE    . ARG A 196 ? 0.9191 1.1282 1.2338 0.2667  0.3736  0.1705  196 ARG A NE    
1625 C  CZ    . ARG A 196 ? 1.0054 1.2373 1.3409 0.2653  0.3848  0.1853  196 ARG A CZ    
1626 N  NH1   . ARG A 196 ? 0.9108 1.1800 1.2942 0.2499  0.3703  0.2009  196 ARG A NH1   
1627 N  NH2   . ARG A 196 ? 0.9908 1.2069 1.2979 0.2798  0.4111  0.1846  196 ARG A NH2   
1628 N  N     . VAL A 197 ? 0.9871 1.1067 1.1335 0.2066  0.2895  0.0926  197 VAL A N     
1629 C  CA    . VAL A 197 ? 1.1539 1.2368 1.2431 0.2071  0.2888  0.0736  197 VAL A CA    
1630 C  C     . VAL A 197 ? 0.9588 1.0262 1.0298 0.1941  0.2633  0.0585  197 VAL A C     
1631 O  O     . VAL A 197 ? 1.1015 1.1384 1.1418 0.2003  0.2626  0.0447  197 VAL A O     
1632 C  CB    . VAL A 197 ? 1.1795 1.2661 1.2540 0.2011  0.2926  0.0756  197 VAL A CB    
1633 C  CG1   . VAL A 197 ? 1.0972 1.1457 1.1115 0.2058  0.2964  0.0582  197 VAL A CG1   
1634 C  CG2   . VAL A 197 ? 0.9558 1.0661 1.0602 0.2115  0.3161  0.0949  197 VAL A CG2   
1635 N  N     . VAL A 198 ? 0.9115 0.9992 1.0020 0.1761  0.2423  0.0612  198 VAL A N     
1636 C  CA    . VAL A 198 ? 1.0163 1.0911 1.0895 0.1633  0.2190  0.0481  198 VAL A CA    
1637 C  C     . VAL A 198 ? 1.0378 1.1019 1.1151 0.1697  0.2157  0.0446  198 VAL A C     
1638 O  O     . VAL A 198 ? 1.0322 1.0685 1.0788 0.1688  0.2078  0.0304  198 VAL A O     
1639 C  CB    . VAL A 198 ? 0.9487 1.0500 1.0476 0.1451  0.1995  0.0538  198 VAL A CB    
1640 C  CG1   . VAL A 198 ? 0.9231 1.0143 1.0097 0.1341  0.1775  0.0429  198 VAL A CG1   
1641 C  CG2   . VAL A 198 ? 0.8987 1.0041 0.9880 0.1377  0.2008  0.0546  198 VAL A CG2   
1642 N  N     . LYS A 199 ? 0.9877 1.0741 1.1050 0.1761  0.2214  0.0586  199 LYS A N     
1643 C  CA    . LYS A 199 ? 1.0056 1.0828 1.1301 0.1835  0.2199  0.0574  199 LYS A CA    
1644 C  C     . LYS A 199 ? 0.9986 1.0390 1.0885 0.1994  0.2360  0.0460  199 LYS A C     
1645 O  O     . LYS A 199 ? 1.0420 1.0599 1.1177 0.2014  0.2294  0.0366  199 LYS A O     
1646 C  CB    . LYS A 199 ? 0.9095 1.0188 1.0848 0.1890  0.2252  0.0766  199 LYS A CB    
1647 C  CG    . LYS A 199 ? 1.1661 1.2998 1.3704 0.1752  0.2026  0.0834  199 LYS A CG    
1648 C  CD    . LYS A 199 ? 1.2995 1.4205 1.5038 0.1794  0.1959  0.0804  199 LYS A CD    
1649 C  CE    . LYS A 199 ? 1.3351 1.4731 1.5530 0.1639  0.1713  0.0827  199 LYS A CE    
1650 N  NZ    . LYS A 199 ? 1.0889 1.2032 1.2864 0.1630  0.1615  0.0726  199 LYS A NZ    
1651 N  N     . GLU A 200 ? 1.0878 1.1206 1.1627 0.2109  0.2570  0.0466  200 GLU A N     
1652 C  CA    . GLU A 200 ? 1.0676 1.0637 1.1065 0.2274  0.2738  0.0351  200 GLU A CA    
1653 C  C     . GLU A 200 ? 1.0903 1.0513 1.0776 0.2203  0.2618  0.0147  200 GLU A C     
1654 O  O     . GLU A 200 ? 1.0834 1.0126 1.0464 0.2255  0.2597  0.0018  200 GLU A O     
1655 C  CB    . GLU A 200 ? 1.0809 1.0807 1.1183 0.2428  0.3012  0.0432  200 GLU A CB    
1656 C  CG    . GLU A 200 ? 1.2726 1.2323 1.2667 0.2610  0.3202  0.0302  200 GLU A CG    
1657 C  CD    . GLU A 200 ? 1.5173 1.4786 1.5350 0.2817  0.3431  0.0397  200 GLU A CD    
1658 O  OE1   . GLU A 200 ? 1.4819 1.4800 1.5485 0.2843  0.3512  0.0599  200 GLU A OE1   
1659 O  OE2   . GLU A 200 ? 1.7007 1.6262 1.6892 0.2952  0.3526  0.0272  200 GLU A OE2   
1660 N  N     . LYS A 201 ? 1.1496 1.1154 1.1210 0.2081  0.2533  0.0119  201 LYS A N     
1661 C  CA    . LYS A 201 ? 1.1453 1.0800 1.0697 0.2010  0.2413  -0.0059 201 LYS A CA    
1662 C  C     . LYS A 201 ? 1.2041 1.1343 1.1318 0.1873  0.2167  -0.0128 201 LYS A C     
1663 O  O     . LYS A 201 ? 1.2363 1.1356 1.1293 0.1845  0.2072  -0.0278 201 LYS A O     
1664 C  CB    . LYS A 201 ? 1.0901 1.0328 0.9995 0.1923  0.2394  -0.0050 201 LYS A CB    
1665 C  CG    . LYS A 201 ? 1.2280 1.1951 1.1583 0.1998  0.2594  0.0105  201 LYS A CG    
1666 C  CD    . LYS A 201 ? 1.1201 1.0781 1.0169 0.1993  0.2658  0.0076  201 LYS A CD    
1667 C  CE    . LYS A 201 ? 1.2640 1.1828 1.1094 0.2136  0.2788  -0.0061 201 LYS A CE    
1668 N  NZ    . LYS A 201 ? 1.1704 1.0842 0.9863 0.2172  0.2908  -0.0047 201 LYS A NZ    
1669 N  N     . ASP A 202 ? 1.0834 1.0435 1.0515 0.1787  0.2060  -0.0017 202 ASP A N     
1670 C  CA    . ASP A 202 ? 1.0466 1.0065 1.0210 0.1662  0.1841  -0.0057 202 ASP A CA    
1671 C  C     . ASP A 202 ? 1.1126 1.0586 1.0567 0.1527  0.1680  -0.0173 202 ASP A C     
1672 O  O     . ASP A 202 ? 1.1664 1.0850 1.0861 0.1508  0.1589  -0.0294 202 ASP A O     
1673 C  CB    . ASP A 202 ? 1.0518 0.9899 1.0242 0.1749  0.1850  -0.0107 202 ASP A CB    
1674 C  CG    . ASP A 202 ? 1.2470 1.1961 1.2413 0.1644  0.1662  -0.0074 202 ASP A CG    
1675 O  OD1   . ASP A 202 ? 1.1949 1.1713 1.2087 0.1522  0.1544  -0.0001 202 ASP A OD1   
1676 O  OD2   . ASP A 202 ? 1.2330 1.1624 1.2242 0.1688  0.1636  -0.0120 202 ASP A OD2   
1677 N  N     . PRO A 203 ? 1.0581 1.0217 1.0047 0.1430  0.1637  -0.0136 203 PRO A N     
1678 C  CA    . PRO A 203 ? 0.9893 0.9407 0.9092 0.1310  0.1492  -0.0233 203 PRO A CA    
1679 C  C     . PRO A 203 ? 0.9574 0.9188 0.8922 0.1174  0.1289  -0.0233 203 PRO A C     
1680 O  O     . PRO A 203 ? 0.9398 0.9272 0.9074 0.1135  0.1247  -0.0134 203 PRO A O     
1681 C  CB    . PRO A 203 ? 0.9859 0.9543 0.9076 0.1274  0.1549  -0.0171 203 PRO A CB    
1682 C  CG    . PRO A 203 ? 0.9936 0.9939 0.9573 0.1296  0.1619  -0.0021 203 PRO A CG    
1683 C  CD    . PRO A 203 ? 1.0810 1.0762 1.0564 0.1427  0.1720  0.0003  203 PRO A CD    
1684 N  N     . ASP A 204 ? 1.0074 0.9481 0.9175 0.1104  0.1161  -0.0340 204 ASP A N     
1685 C  CA    . ASP A 204 ? 0.8377 0.7874 0.7593 0.0977  0.0980  -0.0336 204 ASP A CA    
1686 C  C     . ASP A 204 ? 0.7675 0.7371 0.6956 0.0866  0.0912  -0.0299 204 ASP A C     
1687 O  O     . ASP A 204 ? 0.8290 0.8167 0.7770 0.0780  0.0807  -0.0252 204 ASP A O     
1688 C  CB    . ASP A 204 ? 0.8613 0.7829 0.7583 0.0939  0.0868  -0.0448 204 ASP A CB    
1689 C  CG    . ASP A 204 ? 1.0218 0.9180 0.9081 0.1049  0.0933  -0.0506 204 ASP A CG    
1690 O  OD1   . ASP A 204 ? 1.0697 0.9733 0.9792 0.1097  0.0960  -0.0446 204 ASP A OD1   
1691 O  OD2   . ASP A 204 ? 1.0068 0.8746 0.8607 0.1088  0.0956  -0.0612 204 ASP A OD2   
1692 N  N     . VAL A 205 ? 0.8312 0.7968 0.7422 0.0870  0.0973  -0.0316 205 VAL A N     
1693 C  CA    . VAL A 205 ? 0.8106 0.7914 0.7260 0.0770  0.0916  -0.0285 205 VAL A CA    
1694 C  C     . VAL A 205 ? 0.8098 0.8068 0.7373 0.0817  0.1057  -0.0199 205 VAL A C     
1695 O  O     . VAL A 205 ? 0.8405 0.8264 0.7525 0.0918  0.1199  -0.0205 205 VAL A O     
1696 C  CB    . VAL A 205 ? 0.8227 0.7843 0.7076 0.0715  0.0839  -0.0370 205 VAL A CB    
1697 C  CG1   . VAL A 205 ? 0.8447 0.8216 0.7357 0.0625  0.0800  -0.0328 205 VAL A CG1   
1698 C  CG2   . VAL A 205 ? 0.8059 0.7538 0.6838 0.0659  0.0693  -0.0437 205 VAL A CG2   
1699 N  N     . LEU A 206 ? 0.8520 0.8746 0.8069 0.0744  0.1019  -0.0118 206 LEU A N     
1700 C  CA    . LEU A 206 ? 0.8029 0.8431 0.7738 0.0757  0.1125  -0.0024 206 LEU A CA    
1701 C  C     . LEU A 206 ? 0.7730 0.8151 0.7366 0.0655  0.1056  -0.0034 206 LEU A C     
1702 O  O     . LEU A 206 ? 0.8835 0.9364 0.8599 0.0550  0.0928  -0.0034 206 LEU A O     
1703 C  CB    . LEU A 206 ? 0.7039 0.7710 0.7134 0.0744  0.1120  0.0081  206 LEU A CB    
1704 C  CG    . LEU A 206 ? 0.8365 0.9073 0.8607 0.0864  0.1231  0.0136  206 LEU A CG    
1705 C  CD1   . LEU A 206 ? 0.8278 0.9269 0.8911 0.0825  0.1178  0.0243  206 LEU A CD1   
1706 C  CD2   . LEU A 206 ? 0.7869 0.8529 0.8045 0.0984  0.1435  0.0178  206 LEU A CD2   
1707 N  N     . ILE A 207 ? 0.7359 0.7669 0.6780 0.0692  0.1145  -0.0041 207 ILE A N     
1708 C  CA    . ILE A 207 ? 0.7685 0.7989 0.7016 0.0607  0.1088  -0.0045 207 ILE A CA    
1709 C  C     . ILE A 207 ? 0.9011 0.9529 0.8597 0.0583  0.1161  0.0070  207 ILE A C     
1710 O  O     . ILE A 207 ? 0.8969 0.9551 0.8632 0.0668  0.1316  0.0148  207 ILE A O     
1711 C  CB    . ILE A 207 ? 0.9027 0.9092 0.7972 0.0654  0.1128  -0.0106 207 ILE A CB    
1712 C  CG1   . ILE A 207 ? 0.7903 0.7741 0.6614 0.0690  0.1068  -0.0216 207 ILE A CG1   
1713 C  CG2   . ILE A 207 ? 0.9022 0.9073 0.7881 0.0559  0.1040  -0.0110 207 ILE A CG2   
1714 C  CD1   . ILE A 207 ? 0.9289 0.8871 0.7601 0.0757  0.1118  -0.0283 207 ILE A CD1   
1715 N  N     . THR A 208 ? 0.8598 0.9223 0.8328 0.0468  0.1053  0.0084  208 THR A N     
1716 C  CA    . THR A 208 ? 0.7563 0.8366 0.7534 0.0423  0.1096  0.0185  208 THR A CA    
1717 C  C     . THR A 208 ? 0.7738 0.8489 0.7620 0.0333  0.1017  0.0165  208 THR A C     
1718 O  O     . THR A 208 ? 0.7462 0.8075 0.7144 0.0298  0.0915  0.0078  208 THR A O     
1719 C  CB    . THR A 208 ? 0.8773 0.9797 0.9110 0.0365  0.1033  0.0238  208 THR A CB    
1720 O  OG1   . THR A 208 ? 0.7438 0.8463 0.7792 0.0259  0.0866  0.0172  208 THR A OG1   
1721 C  CG2   . THR A 208 ? 0.8524 0.9594 0.8952 0.0445  0.1072  0.0250  208 THR A CG2   
1722 N  N     . TYR A 209 ? 0.8152 0.9017 0.8207 0.0296  0.1067  0.0256  209 TYR A N     
1723 C  CA    . TYR A 209 ? 0.6925 0.7775 0.6985 0.0201  0.0990  0.0255  209 TYR A CA    
1724 C  C     . TYR A 209 ? 0.7128 0.8163 0.7546 0.0111  0.0931  0.0307  209 TYR A C     
1725 O  O     . TYR A 209 ? 0.8498 0.9671 0.9146 0.0115  0.1018  0.0416  209 TYR A O     
1726 C  CB    . TYR A 209 ? 0.8096 0.8879 0.8008 0.0238  0.1099  0.0320  209 TYR A CB    
1727 C  CG    . TYR A 209 ? 0.9202 0.9916 0.9045 0.0158  0.1015  0.0306  209 TYR A CG    
1728 C  CD1   . TYR A 209 ? 0.8396 0.8956 0.7997 0.0140  0.0910  0.0210  209 TYR A CD1   
1729 C  CD2   . TYR A 209 ? 0.7519 0.8322 0.7561 0.0101  0.1042  0.0400  209 TYR A CD2   
1730 C  CE1   . TYR A 209 ? 0.8433 0.8938 0.7994 0.0075  0.0839  0.0209  209 TYR A CE1   
1731 C  CE2   . TYR A 209 ? 0.8987 0.9718 0.8979 0.0036  0.0971  0.0392  209 TYR A CE2   
1732 C  CZ    . TYR A 209 ? 0.9066 0.9652 0.8817 0.0027  0.0873  0.0298  209 TYR A CZ    
1733 O  OH    . TYR A 209 ? 0.9205 0.9729 0.8930 -0.0030 0.0808  0.0303  209 TYR A OH    
1734 N  N     . ASN A 210 ? 0.7378 0.8414 0.7840 0.0031  0.0783  0.0231  210 ASN A N     
1735 C  CA    . ASN A 210 ? 0.7299 0.8479 0.8050 -0.0061 0.0694  0.0248  210 ASN A CA    
1736 C  C     . ASN A 210 ? 0.8147 0.9489 0.9119 -0.0036 0.0705  0.0295  210 ASN A C     
1737 O  O     . ASN A 210 ? 0.8009 0.9502 0.9266 -0.0102 0.0658  0.0348  210 ASN A O     
1738 C  CB    . ASN A 210 ? 0.6635 0.7870 0.7568 -0.0126 0.0716  0.0325  210 ASN A CB    
1739 C  CG    . ASN A 210 ? 0.8582 0.9883 0.9722 -0.0240 0.0581  0.0296  210 ASN A CG    
1740 O  OD1   . ASN A 210 ? 0.9610 1.0851 1.0653 -0.0276 0.0467  0.0196  210 ASN A OD1   
1741 N  ND2   . ASN A 210 ? 0.8755 1.0174 1.0181 -0.0298 0.0594  0.0386  210 ASN A ND2   
1742 N  N     . GLY A 211 ? 0.7461 0.8772 0.8320 0.0058  0.0759  0.0280  211 GLY A N     
1743 C  CA    . GLY A 211 ? 0.7941 0.9404 0.9016 0.0086  0.0761  0.0327  211 GLY A CA    
1744 C  C     . GLY A 211 ? 0.8411 0.9945 0.9588 0.0007  0.0597  0.0277  211 GLY A C     
1745 O  O     . GLY A 211 ? 0.8157 0.9858 0.9578 -0.0003 0.0565  0.0336  211 GLY A O     
1746 N  N     . ASP A 212 ? 0.7966 0.9380 0.8958 -0.0047 0.0493  0.0177  212 ASP A N     
1747 C  CA    . ASP A 212 ? 0.7535 0.9000 0.8580 -0.0117 0.0346  0.0126  212 ASP A CA    
1748 C  C     . ASP A 212 ? 0.7996 0.9598 0.9300 -0.0212 0.0271  0.0166  212 ASP A C     
1749 O  O     . ASP A 212 ? 0.8153 0.9852 0.9564 -0.0257 0.0159  0.0155  212 ASP A O     
1750 C  CB    . ASP A 212 ? 0.7651 0.8957 0.8455 -0.0148 0.0275  0.0022  212 ASP A CB    
1751 C  CG    . ASP A 212 ? 0.8156 0.9381 0.8780 -0.0089 0.0262  -0.0027 212 ASP A CG    
1752 O  OD1   . ASP A 212 ? 0.7868 0.9154 0.8553 -0.0029 0.0294  0.0010  212 ASP A OD1   
1753 O  OD2   . ASP A 212 ? 0.8208 0.9307 0.8647 -0.0103 0.0220  -0.0095 212 ASP A OD2   
1754 N  N     . ASN A 213 ? 0.7840 0.9449 0.9246 -0.0247 0.0323  0.0214  213 ASN A N     
1755 C  CA    . ASN A 213 ? 0.8392 1.0095 1.0037 -0.0353 0.0238  0.0241  213 ASN A CA    
1756 C  C     . ASN A 213 ? 0.7710 0.9562 0.9656 -0.0356 0.0324  0.0378  213 ASN A C     
1757 O  O     . ASN A 213 ? 0.8204 1.0144 1.0392 -0.0453 0.0245  0.0413  213 ASN A O     
1758 C  CB    . ASN A 213 ? 0.7750 0.9305 0.9273 -0.0421 0.0189  0.0166  213 ASN A CB    
1759 C  CG    . ASN A 213 ? 0.6972 0.8400 0.8242 -0.0425 0.0101  0.0042  213 ASN A CG    
1760 O  OD1   . ASN A 213 ? 0.8779 1.0248 1.0066 -0.0466 -0.0013 -0.0008 213 ASN A OD1   
1761 N  ND2   . ASN A 213 ? 0.9368 1.0648 1.0406 -0.0382 0.0155  0.0001  213 ASN A ND2   
1762 N  N     . PHE A 214 ? 0.8038 0.9918 0.9980 -0.0253 0.0483  0.0458  214 PHE A N     
1763 C  CA    . PHE A 214 ? 0.8173 1.0214 1.0421 -0.0244 0.0583  0.0607  214 PHE A CA    
1764 C  C     . PHE A 214 ? 0.8155 1.0305 1.0487 -0.0127 0.0707  0.0693  214 PHE A C     
1765 O  O     . PHE A 214 ? 0.7364 0.9706 0.9998 -0.0143 0.0671  0.0775  214 PHE A O     
1766 C  CB    . PHE A 214 ? 0.7341 0.9300 0.9531 -0.0236 0.0700  0.0654  214 PHE A CB    
1767 C  CG    . PHE A 214 ? 0.9541 1.1664 1.2030 -0.0208 0.0837  0.0825  214 PHE A CG    
1768 C  CD1   . PHE A 214 ? 0.7668 0.9969 1.0556 -0.0307 0.0766  0.0916  214 PHE A CD1   
1769 C  CD2   . PHE A 214 ? 1.0041 1.2138 1.2413 -0.0083 0.1035  0.0896  214 PHE A CD2   
1770 C  CE1   . PHE A 214 ? 0.7224 0.9694 1.0426 -0.0283 0.0897  0.1092  214 PHE A CE1   
1771 C  CE2   . PHE A 214 ? 0.8394 1.0651 1.1046 -0.0046 0.1181  0.1066  214 PHE A CE2   
1772 C  CZ    . PHE A 214 ? 0.7289 0.9743 1.0375 -0.0147 0.1114  0.1172  214 PHE A CZ    
1773 N  N     . ASP A 215 ? 0.8014 1.0036 1.0083 -0.0008 0.0850  0.0676  215 ASP A N     
1774 C  CA    . ASP A 215 ? 0.7659 0.9757 0.9799 0.0120  0.1008  0.0764  215 ASP A CA    
1775 C  C     . ASP A 215 ? 0.8051 1.0278 1.0362 0.0135  0.0935  0.0778  215 ASP A C     
1776 O  O     . ASP A 215 ? 0.8187 1.0610 1.0816 0.0170  0.0998  0.0907  215 ASP A O     
1777 C  CB    . ASP A 215 ? 0.7869 0.9754 0.9620 0.0238  0.1131  0.0697  215 ASP A CB    
1778 C  CG    . ASP A 215 ? 1.0952 1.2702 1.2497 0.0229  0.1194  0.0687  215 ASP A CG    
1779 O  OD1   . ASP A 215 ? 1.1614 1.3218 1.2878 0.0333  0.1321  0.0669  215 ASP A OD1   
1780 O  OD2   . ASP A 215 ? 1.0174 1.1949 1.1821 0.0120  0.1112  0.0695  215 ASP A OD2   
1781 N  N     . PHE A 216 ? 0.7536 0.9667 0.9655 0.0112  0.0805  0.0658  216 PHE A N     
1782 C  CA    . PHE A 216 ? 0.7416 0.9655 0.9663 0.0138  0.0740  0.0675  216 PHE A CA    
1783 C  C     . PHE A 216 ? 0.6282 0.8752 0.8897 0.0035  0.0610  0.0754  216 PHE A C     
1784 O  O     . PHE A 216 ? 0.7251 0.9900 1.0129 0.0073  0.0617  0.0855  216 PHE A O     
1785 C  CB    . PHE A 216 ? 0.6910 0.8992 0.8864 0.0131  0.0632  0.0539  216 PHE A CB    
1786 C  CG    . PHE A 216 ? 0.7460 0.9372 0.9156 0.0254  0.0743  0.0492  216 PHE A CG    
1787 C  CD1   . PHE A 216 ? 0.6100 0.8069 0.7894 0.0354  0.0810  0.0547  216 PHE A CD1   
1788 C  CD2   . PHE A 216 ? 0.6972 0.8661 0.8334 0.0267  0.0772  0.0394  216 PHE A CD2   
1789 C  CE1   . PHE A 216 ? 0.7965 0.9749 0.9515 0.0465  0.0907  0.0493  216 PHE A CE1   
1790 C  CE2   . PHE A 216 ? 0.6374 0.7889 0.7492 0.0370  0.0855  0.0343  216 PHE A CE2   
1791 C  CZ    . PHE A 216 ? 0.7444 0.8996 0.8649 0.0469  0.0923  0.0386  216 PHE A CZ    
1792 N  N     . ALA A 217 ? 0.7261 0.9724 0.9905 -0.0094 0.0484  0.0712  217 ALA A N     
1793 C  CA    . ALA A 217 ? 0.6645 0.9297 0.9606 -0.0206 0.0330  0.0767  217 ALA A CA    
1794 C  C     . ALA A 217 ? 0.7827 1.0688 1.1193 -0.0207 0.0417  0.0939  217 ALA A C     
1795 O  O     . ALA A 217 ? 0.8333 1.1406 1.2030 -0.0248 0.0331  0.1035  217 ALA A O     
1796 C  CB    . ALA A 217 ? 0.6111 0.8663 0.8967 -0.0340 0.0177  0.0660  217 ALA A CB    
1797 N  N     . TYR A 218 ? 0.7357 1.0167 1.0710 -0.0163 0.0584  0.0991  218 TYR A N     
1798 C  CA    . TYR A 218 ? 0.7260 1.0272 1.0992 -0.0134 0.0711  0.1175  218 TYR A CA    
1799 C  C     . TYR A 218 ? 0.6965 1.0110 1.0841 -0.0005 0.0819  0.1272  218 TYR A C     
1800 O  O     . TYR A 218 ? 0.7953 1.1343 1.2239 -0.0025 0.0790  0.1412  218 TYR A O     
1801 C  CB    . TYR A 218 ? 0.7767 1.0678 1.1390 -0.0084 0.0896  0.1213  218 TYR A CB    
1802 C  CG    . TYR A 218 ? 0.8468 1.1558 1.2496 -0.0150 0.0939  0.1375  218 TYR A CG    
1803 C  CD1   . TYR A 218 ? 0.8360 1.1451 1.2526 -0.0309 0.0784  0.1356  218 TYR A CD1   
1804 C  CD2   . TYR A 218 ? 0.9496 1.2755 1.3792 -0.0051 0.1133  0.1556  218 TYR A CD2   
1805 C  CE1   . TYR A 218 ? 0.8288 1.1539 1.2853 -0.0377 0.0818  0.1514  218 TYR A CE1   
1806 C  CE2   . TYR A 218 ? 0.8589 1.2030 1.3294 -0.0112 0.1178  0.1725  218 TYR A CE2   
1807 C  CZ    . TYR A 218 ? 0.8903 1.2340 1.3750 -0.0280 0.1014  0.1706  218 TYR A CZ    
1808 O  OH    . TYR A 218 ? 0.7324 1.0937 1.2603 -0.0348 0.1053  0.1882  218 TYR A OH    
1809 N  N     . LEU A 219 ? 0.7682 1.0665 1.1234 0.0128  0.0938  0.1202  219 LEU A N     
1810 C  CA    . LEU A 219 ? 0.7160 1.0227 1.0811 0.0261  0.1040  0.1274  219 LEU A CA    
1811 C  C     . LEU A 219 ? 0.7474 1.0700 1.1335 0.0205  0.0856  0.1292  219 LEU A C     
1812 O  O     . LEU A 219 ? 0.8342 1.1740 1.2474 0.0282  0.0912  0.1415  219 LEU A O     
1813 C  CB    . LEU A 219 ? 0.6054 0.8868 0.9273 0.0389  0.1153  0.1157  219 LEU A CB    
1814 C  CG    . LEU A 219 ? 0.7176 0.9868 1.0219 0.0505  0.1388  0.1182  219 LEU A CG    
1815 C  CD1   . LEU A 219 ? 0.5664 0.8050 0.8201 0.0553  0.1405  0.1014  219 LEU A CD1   
1816 C  CD2   . LEU A 219 ? 0.6901 0.9716 1.0159 0.0658  0.1589  0.1322  219 LEU A CD2   
1817 N  N     . LYS A 220 ? 0.6616 0.9784 1.0348 0.0078  0.0640  0.1177  220 LYS A N     
1818 C  CA    . LYS A 220 ? 0.6981 1.0301 1.0891 0.0015  0.0450  0.1198  220 LYS A CA    
1819 C  C     . LYS A 220 ? 0.7440 1.1037 1.1834 -0.0074 0.0371  0.1352  220 LYS A C     
1820 O  O     . LYS A 220 ? 0.8497 1.2308 1.3206 -0.0036 0.0361  0.1484  220 LYS A O     
1821 C  CB    . LYS A 220 ? 0.7117 1.0288 1.0728 -0.0089 0.0254  0.1032  220 LYS A CB    
1822 C  CG    . LYS A 220 ? 0.8296 1.1600 1.2015 -0.0149 0.0053  0.1041  220 LYS A CG    
1823 C  CD    . LYS A 220 ? 0.7528 1.0737 1.1058 -0.0288 -0.0150 0.0908  220 LYS A CD    
1824 C  CE    . LYS A 220 ? 0.7152 1.0340 1.0497 -0.0286 -0.0286 0.0844  220 LYS A CE    
1825 N  NZ    . LYS A 220 ? 0.8870 1.1964 1.2019 -0.0410 -0.0473 0.0717  220 LYS A NZ    
1826 N  N     . LYS A 221 ? 0.7422 1.1019 1.1903 -0.0196 0.0310  0.1345  221 LYS A N     
1827 C  CA    . LYS A 221 ? 0.7632 1.1473 1.2573 -0.0313 0.0188  0.1476  221 LYS A CA    
1828 C  C     . LYS A 221 ? 0.8429 1.2511 1.3800 -0.0223 0.0357  0.1694  221 LYS A C     
1829 O  O     . LYS A 221 ? 0.7788 1.2124 1.3565 -0.0266 0.0257  0.1829  221 LYS A O     
1830 C  CB    . LYS A 221 ? 0.7349 1.1109 1.2296 -0.0450 0.0118  0.1428  221 LYS A CB    
1831 C  CG    . LYS A 221 ? 0.7915 1.1895 1.3320 -0.0599 -0.0053 0.1538  221 LYS A CG    
1832 C  CD    . LYS A 221 ? 0.9521 1.3526 1.4885 -0.0708 -0.0331 0.1452  221 LYS A CD    
1833 C  CE    . LYS A 221 ? 0.9782 1.3628 1.5006 -0.0868 -0.0511 0.1313  221 LYS A CE    
1834 N  NZ    . LYS A 221 ? 0.9154 1.3001 1.4281 -0.0967 -0.0777 0.1216  221 LYS A NZ    
1835 N  N     . ARG A 222 ? 0.6899 1.0908 1.2191 -0.0098 0.0613  0.1738  222 ARG A N     
1836 C  CA    . ARG A 222 ? 0.7573 1.1800 1.3247 0.0013  0.0805  0.1947  222 ARG A CA    
1837 C  C     . ARG A 222 ? 0.8447 1.2770 1.4194 0.0128  0.0824  0.1995  222 ARG A C     
1838 O  O     . ARG A 222 ? 0.9179 1.3780 1.5386 0.0128  0.0797  0.2169  222 ARG A O     
1839 C  CB    . ARG A 222 ? 0.7547 1.1645 1.3044 0.0140  0.1086  0.1968  222 ARG A CB    
1840 C  CG    . ARG A 222 ? 0.8699 1.2608 1.3946 0.0048  0.1064  0.1865  222 ARG A CG    
1841 C  CD    . ARG A 222 ? 0.8240 1.2330 1.3911 -0.0061 0.1055  0.2017  222 ARG A CD    
1842 N  NE    . ARG A 222 ? 0.7789 1.2149 1.3922 0.0023  0.1223  0.2253  222 ARG A NE    
1843 C  CZ    . ARG A 222 ? 0.8043 1.2686 1.4724 -0.0077 0.1124  0.2422  222 ARG A CZ    
1844 N  NH1   . ARG A 222 ? 0.6628 1.1312 1.3450 -0.0269 0.0844  0.2371  222 ARG A NH1   
1845 N  NH2   . ARG A 222 ? 0.5790 1.0677 1.2888 0.0020  0.1309  0.2649  222 ARG A NH2   
1846 N  N     . CYS A 223 ? 0.7596 1.1696 1.2914 0.0217  0.0854  0.1847  223 CYS A N     
1847 C  CA    . CYS A 223 ? 0.8124 1.2283 1.3490 0.0336  0.0885  0.1889  223 CYS A CA    
1848 C  C     . CYS A 223 ? 0.7913 1.2327 1.3635 0.0239  0.0657  0.1981  223 CYS A C     
1849 O  O     . CYS A 223 ? 0.6974 1.1574 1.2994 0.0329  0.0706  0.2124  223 CYS A O     
1850 C  CB    . CYS A 223 ? 0.7138 1.1005 1.1987 0.0399  0.0884  0.1698  223 CYS A CB    
1851 S  SG    . CYS A 223 ? 0.7030 1.0649 1.1548 0.0602  0.1195  0.1650  223 CYS A SG    
1852 N  N     . GLU A 224 ? 0.7461 1.1879 1.3151 0.0061  0.0405  0.1901  224 GLU A N     
1853 C  CA    . GLU A 224 ? 0.8474 1.3130 1.4483 -0.0041 0.0170  0.1987  224 GLU A CA    
1854 C  C     . GLU A 224 ? 0.7900 1.2848 1.4472 -0.0114 0.0151  0.2187  224 GLU A C     
1855 O  O     . GLU A 224 ? 0.8110 1.3326 1.5103 -0.0081 0.0133  0.2367  224 GLU A O     
1856 C  CB    . GLU A 224 ? 0.8407 1.2938 1.4130 -0.0196 -0.0098 0.1815  224 GLU A CB    
1857 C  CG    . GLU A 224 ? 0.9150 1.3453 1.4577 -0.0281 -0.0100 0.1662  224 GLU A CG    
1858 C  CD    . GLU A 224 ? 0.9347 1.3455 1.4367 -0.0370 -0.0293 0.1464  224 GLU A CD    
1859 O  OE1   . GLU A 224 ? 0.7764 1.1778 1.2517 -0.0295 -0.0299 0.1394  224 GLU A OE1   
1860 O  OE2   . GLU A 224 ? 1.1371 1.5414 1.6345 -0.0511 -0.0431 0.1383  224 GLU A OE2   
1861 N  N     . LYS A 225 ? 0.7933 1.2837 1.4543 -0.0212 0.0159  0.2170  225 LYS A N     
1862 C  CA    . LYS A 225 ? 0.8570 1.3731 1.5720 -0.0285 0.0161  0.2364  225 LYS A CA    
1863 C  C     . LYS A 225 ? 0.9069 1.4425 1.6569 -0.0116 0.0427  0.2579  225 LYS A C     
1864 O  O     . LYS A 225 ? 0.8397 1.4030 1.6434 -0.0152 0.0443  0.2788  225 LYS A O     
1865 C  CB    . LYS A 225 ? 0.9055 1.4079 1.6119 -0.0381 0.0190  0.2304  225 LYS A CB    
1866 C  CG    . LYS A 225 ? 1.0776 1.5922 1.8160 -0.0596 -0.0057 0.2340  225 LYS A CG    
1867 C  CD    . LYS A 225 ? 1.2307 1.7300 1.9379 -0.0734 -0.0352 0.2139  225 LYS A CD    
1868 C  CE    . LYS A 225 ? 1.3437 1.8547 2.0841 -0.0947 -0.0611 0.2175  225 LYS A CE    
1869 N  NZ    . LYS A 225 ? 1.1917 1.6837 1.8964 -0.1077 -0.0883 0.1961  225 LYS A NZ    
1870 N  N     . LEU A 226 ? 0.8167 1.3372 1.5368 0.0072  0.0641  0.2529  226 LEU A N     
1871 C  CA    . LEU A 226 ? 0.8578 1.3901 1.6009 0.0263  0.0929  0.2699  226 LEU A CA    
1872 C  C     . LEU A 226 ? 0.7035 1.2400 1.4472 0.0402  0.0962  0.2731  226 LEU A C     
1873 O  O     . LEU A 226 ? 0.8095 1.3657 1.5897 0.0534  0.1136  0.2923  226 LEU A O     
1874 C  CB    . LEU A 226 ? 0.8543 1.3612 1.5597 0.0383  0.1201  0.2617  226 LEU A CB    
1875 C  CG    . LEU A 226 ? 0.8628 1.3779 1.5872 0.0557  0.1532  0.2784  226 LEU A CG    
1876 C  CD1   . LEU A 226 ? 0.7473 1.2415 1.4404 0.0561  0.1678  0.2707  226 LEU A CD1   
1877 C  CD2   . LEU A 226 ? 0.9093 1.4129 1.6126 0.0760  0.1701  0.2751  226 LEU A CD2   
1878 N  N     . GLY A 227 ? 0.8368 1.3555 1.5426 0.0382  0.0810  0.2559  227 GLY A N     
1879 C  CA    . GLY A 227 ? 0.8724 1.3970 1.5832 0.0490  0.0801  0.2603  227 GLY A CA    
1880 C  C     . GLY A 227 ? 0.8041 1.3031 1.4775 0.0686  0.1029  0.2511  227 GLY A C     
1881 O  O     . GLY A 227 ? 0.7283 1.2364 1.4211 0.0838  0.1160  0.2627  227 GLY A O     
1882 N  N     . ILE A 228 ? 0.7989 1.2656 1.4198 0.0685  0.1073  0.2304  228 ILE A N     
1883 C  CA    . ILE A 228 ? 0.8184 1.2571 1.3992 0.0849  0.1252  0.2189  228 ILE A CA    
1884 C  C     . ILE A 228 ? 0.8576 1.2759 1.3983 0.0783  0.1063  0.2002  228 ILE A C     
1885 O  O     . ILE A 228 ? 0.7497 1.1653 1.2772 0.0620  0.0854  0.1904  228 ILE A O     
1886 C  CB    . ILE A 228 ? 0.8397 1.2564 1.3909 0.0922  0.1480  0.2113  228 ILE A CB    
1887 C  CG1   . ILE A 228 ? 0.7974 1.2364 1.3883 0.0933  0.1624  0.2298  228 ILE A CG1   
1888 C  CG2   . ILE A 228 ? 0.7886 1.1812 1.3100 0.1122  0.1700  0.2047  228 ILE A CG2   
1889 C  CD1   . ILE A 228 ? 0.6582 1.0772 1.2201 0.1011  0.1853  0.2244  228 ILE A CD1   
1890 N  N     . ASN A 229 ? 0.8074 1.2105 1.3292 0.0915  0.1144  0.1955  229 ASN A N     
1891 C  CA    . ASN A 229 ? 0.8325 1.2142 1.3155 0.0878  0.1005  0.1789  229 ASN A CA    
1892 C  C     . ASN A 229 ? 0.9753 1.3223 1.4100 0.0937  0.1141  0.1613  229 ASN A C     
1893 O  O     . ASN A 229 ? 0.9242 1.2560 1.3477 0.1096  0.1343  0.1604  229 ASN A O     
1894 C  CB    . ASN A 229 ? 0.8384 1.2250 1.3330 0.0975  0.0989  0.1858  229 ASN A CB    
1895 C  CG    . ASN A 229 ? 0.9590 1.3315 1.4231 0.0906  0.0802  0.1729  229 ASN A CG    
1896 O  OD1   . ASN A 229 ? 1.1119 1.4963 1.5793 0.0763  0.0576  0.1721  229 ASN A OD1   
1897 N  ND2   . ASN A 229 ? 1.0067 1.3527 1.4400 0.1008  0.0897  0.1626  229 ASN A ND2   
1898 N  N     . PHE A 230 ? 0.8717 1.2056 1.2780 0.0809  0.1026  0.1473  230 PHE A N     
1899 C  CA    . PHE A 230 ? 0.7625 1.0650 1.1235 0.0839  0.1119  0.1309  230 PHE A CA    
1900 C  C     . PHE A 230 ? 0.7500 1.0309 1.0810 0.0885  0.1075  0.1194  230 PHE A C     
1901 O  O     . PHE A 230 ? 0.9101 1.1808 1.2181 0.0787  0.0916  0.1080  230 PHE A O     
1902 C  CB    . PHE A 230 ? 0.8074 1.1056 1.1532 0.0685  0.1001  0.1218  230 PHE A CB    
1903 C  CG    . PHE A 230 ? 0.7968 1.0779 1.1200 0.0721  0.1159  0.1162  230 PHE A CG    
1904 C  CD1   . PHE A 230 ? 0.8196 1.1083 1.1603 0.0822  0.1368  0.1278  230 PHE A CD1   
1905 C  CD2   . PHE A 230 ? 0.8935 1.1516 1.1781 0.0658  0.1102  0.1004  230 PHE A CD2   
1906 C  CE1   . PHE A 230 ? 0.8664 1.1394 1.1837 0.0860  0.1515  0.1234  230 PHE A CE1   
1907 C  CE2   . PHE A 230 ? 0.8848 1.1278 1.1480 0.0690  0.1237  0.0962  230 PHE A CE2   
1908 C  CZ    . PHE A 230 ? 0.8798 1.1298 1.1579 0.0791  0.1442  0.1076  230 PHE A CZ    
1909 N  N     . ALA A 231 ? 0.7538 1.0270 1.0862 0.1041  0.1225  0.1228  231 ALA A N     
1910 C  CA    . ALA A 231 ? 0.7049 0.9573 1.0133 0.1094  0.1194  0.1136  231 ALA A CA    
1911 C  C     . ALA A 231 ? 0.8629 1.0809 1.1261 0.1127  0.1273  0.0967  231 ALA A C     
1912 O  O     . ALA A 231 ? 0.8559 1.0528 1.1028 0.1248  0.1385  0.0918  231 ALA A O     
1913 C  CB    . ALA A 231 ? 0.7125 0.9708 1.0446 0.1244  0.1306  0.1251  231 ALA A CB    
1914 N  N     . LEU A 232 ? 0.8099 1.0214 1.0526 0.1016  0.1205  0.0875  232 LEU A N     
1915 C  CA    . LEU A 232 ? 0.8364 1.0170 1.0369 0.1031  0.1252  0.0722  232 LEU A CA    
1916 C  C     . LEU A 232 ? 0.7051 0.8663 0.8827 0.1021  0.1151  0.0617  232 LEU A C     
1917 O  O     . LEU A 232 ? 0.7717 0.9053 0.9185 0.1075  0.1213  0.0508  232 LEU A O     
1918 C  CB    . LEU A 232 ? 0.7194 0.8994 0.9065 0.0908  0.1185  0.0662  232 LEU A CB    
1919 C  CG    . LEU A 232 ? 0.7858 0.9728 0.9806 0.0929  0.1325  0.0725  232 LEU A CG    
1920 C  CD1   . LEU A 232 ? 0.7066 0.8843 0.8790 0.0818  0.1254  0.0637  232 LEU A CD1   
1921 C  CD2   . LEU A 232 ? 0.6452 0.8176 0.8283 0.1097  0.1554  0.0735  232 LEU A CD2   
1922 N  N     . GLY A 233 ? 0.6301 0.8044 0.8215 0.0952  0.0993  0.0651  233 GLY A N     
1923 C  CA    . GLY A 233 ? 0.7418 0.8993 0.9144 0.0944  0.0905  0.0574  233 GLY A CA    
1924 C  C     . GLY A 233 ? 0.8303 0.9721 1.0014 0.1086  0.1020  0.0581  233 GLY A C     
1925 O  O     . GLY A 233 ? 0.8867 1.0384 1.0807 0.1191  0.1138  0.0682  233 GLY A O     
1926 N  N     . ARG A 234 ? 0.8071 0.9234 0.9520 0.1089  0.0984  0.0474  234 ARG A N     
1927 C  CA    . ARG A 234 ? 0.7935 0.8911 0.9356 0.1210  0.1066  0.0465  234 ARG A CA    
1928 C  C     . ARG A 234 ? 0.8658 0.9790 1.0350 0.1231  0.1001  0.0582  234 ARG A C     
1929 O  O     . ARG A 234 ? 1.0302 1.1333 1.2067 0.1350  0.1091  0.0614  234 ARG A O     
1930 C  CB    . ARG A 234 ? 0.7753 0.8408 0.8829 0.1189  0.1027  0.0319  234 ARG A CB    
1931 C  CG    . ARG A 234 ? 0.7599 0.8032 0.8382 0.1221  0.1129  0.0207  234 ARG A CG    
1932 C  CD    . ARG A 234 ? 0.8175 0.8310 0.8641 0.1181  0.1054  0.0070  234 ARG A CD    
1933 N  NE    . ARG A 234 ? 0.9202 0.9062 0.9372 0.1253  0.1165  -0.0036 234 ARG A NE    
1934 C  CZ    . ARG A 234 ? 0.9901 0.9546 0.9761 0.1193  0.1100  -0.0156 234 ARG A CZ    
1935 N  NH1   . ARG A 234 ? 0.8359 0.8032 0.8185 0.1064  0.0937  -0.0182 234 ARG A NH1   
1936 N  NH2   . ARG A 234 ? 0.9964 0.9361 0.9538 0.1266  0.1201  -0.0249 234 ARG A NH2   
1937 N  N     . ASP A 235 ? 0.7052 0.8418 0.8884 0.1124  0.0848  0.0645  235 ASP A N     
1938 C  CA    . ASP A 235 ? 0.8177 0.9744 1.0285 0.1139  0.0778  0.0780  235 ASP A CA    
1939 C  C     . ASP A 235 ? 0.8519 1.0380 1.0972 0.1169  0.0815  0.0924  235 ASP A C     
1940 O  O     . ASP A 235 ? 0.8902 1.0980 1.1605 0.1161  0.0729  0.1050  235 ASP A O     
1941 C  CB    . ASP A 235 ? 0.6397 0.8054 0.8443 0.1013  0.0587  0.0775  235 ASP A CB    
1942 C  CG    . ASP A 235 ? 0.7697 0.9528 0.9741 0.0892  0.0496  0.0760  235 ASP A CG    
1943 O  OD1   . ASP A 235 ? 0.6414 0.8382 0.8470 0.0801  0.0347  0.0785  235 ASP A OD1   
1944 O  OD2   . ASP A 235 ? 0.8005 0.9821 1.0020 0.0891  0.0578  0.0721  235 ASP A OD2   
1945 N  N     . GLY A 236 ? 0.7901 0.9780 1.0381 0.1201  0.0939  0.0918  236 GLY A N     
1946 C  CA    . GLY A 236 ? 0.7185 0.9360 1.0017 0.1210  0.0968  0.1062  236 GLY A CA    
1947 C  C     . GLY A 236 ? 0.7502 0.9906 1.0424 0.1056  0.0803  0.1087  236 GLY A C     
1948 O  O     . GLY A 236 ? 0.8750 1.1430 1.2008 0.1040  0.0773  0.1223  236 GLY A O     
1949 N  N     . SER A 237 ? 0.6931 0.9226 0.9575 0.0941  0.0692  0.0961  237 SER A N     
1950 C  CA    . SER A 237 ? 0.7001 0.9477 0.9698 0.0796  0.0532  0.0967  237 SER A CA    
1951 C  C     . SER A 237 ? 0.6290 0.8784 0.8988 0.0753  0.0597  0.0939  237 SER A C     
1952 O  O     . SER A 237 ? 0.6327 0.8682 0.8933 0.0833  0.0764  0.0906  237 SER A O     
1953 C  CB    . SER A 237 ? 0.7882 1.0239 1.0293 0.0699  0.0388  0.0855  237 SER A CB    
1954 O  OG    . SER A 237 ? 0.7865 0.9938 0.9965 0.0726  0.0464  0.0725  237 SER A OG    
1955 N  N     . GLU A 238 ? 0.5806 0.8459 0.8590 0.0625  0.0461  0.0949  238 GLU A N     
1956 C  CA    . GLU A 238 ? 0.6474 0.9150 0.9268 0.0559  0.0490  0.0926  238 GLU A CA    
1957 C  C     . GLU A 238 ? 0.8063 1.0545 1.0511 0.0471  0.0423  0.0771  238 GLU A C     
1958 O  O     . GLU A 238 ? 0.8437 1.0836 1.0699 0.0434  0.0314  0.0701  238 GLU A O     
1959 C  CB    . GLU A 238 ? 0.6333 0.9295 0.9466 0.0466  0.0372  0.1035  238 GLU A CB    
1960 C  CG    . GLU A 238 ? 0.7756 1.0939 1.1284 0.0551  0.0443  0.1212  238 GLU A CG    
1961 C  CD    . GLU A 238 ? 0.9633 1.3073 1.3523 0.0473  0.0397  0.1328  238 GLU A CD    
1962 O  OE1   . GLU A 238 ? 0.9822 1.3396 1.3799 0.0343  0.0192  0.1335  238 GLU A OE1   
1963 O  OE2   . GLU A 238 ? 0.9366 1.2869 1.3451 0.0541  0.0565  0.1415  238 GLU A OE2   
1964 N  N     . PRO A 239 ? 0.8195 1.0600 1.0556 0.0445  0.0496  0.0725  239 PRO A N     
1965 C  CA    . PRO A 239 ? 0.7326 0.9568 0.9396 0.0358  0.0427  0.0592  239 PRO A CA    
1966 C  C     . PRO A 239 ? 0.7886 1.0220 0.9968 0.0237  0.0230  0.0566  239 PRO A C     
1967 O  O     . PRO A 239 ? 0.8508 1.1043 1.0838 0.0172  0.0142  0.0639  239 PRO A O     
1968 C  CB    . PRO A 239 ? 0.7779 1.0019 0.9885 0.0339  0.0521  0.0603  239 PRO A CB    
1969 C  CG    . PRO A 239 ? 0.8072 1.0340 1.0309 0.0469  0.0705  0.0693  239 PRO A CG    
1970 C  CD    . PRO A 239 ? 0.7861 1.0300 1.0357 0.0516  0.0672  0.0795  239 PRO A CD    
1971 N  N     . LYS A 240 ? 0.6952 0.9137 0.8764 0.0211  0.0159  0.0464  240 LYS A N     
1972 C  CA    . LYS A 240 ? 0.7393 0.9633 0.9154 0.0117  -0.0011 0.0428  240 LYS A CA    
1973 C  C     . LYS A 240 ? 0.8647 1.0787 1.0245 0.0025  -0.0056 0.0328  240 LYS A C     
1974 O  O     . LYS A 240 ? 0.7925 0.9884 0.9316 0.0044  0.0015  0.0253  240 LYS A O     
1975 C  CB    . LYS A 240 ? 0.6992 0.9147 0.8582 0.0156  -0.0050 0.0400  240 LYS A CB    
1976 C  CG    . LYS A 240 ? 0.8284 1.0496 0.9793 0.0077  -0.0212 0.0373  240 LYS A CG    
1977 C  CD    . LYS A 240 ? 0.9488 1.1617 1.0836 0.0123  -0.0229 0.0362  240 LYS A CD    
1978 C  CE    . LYS A 240 ? 1.0426 1.2703 1.1810 0.0090  -0.0368 0.0414  240 LYS A CE    
1979 N  NZ    . LYS A 240 ? 1.0919 1.3235 1.2374 0.0174  -0.0351 0.0504  240 LYS A NZ    
1980 N  N     . ILE A 241 ? 0.7622 0.9874 0.9319 -0.0074 -0.0180 0.0328  241 ILE A N     
1981 C  CA    . ILE A 241 ? 0.7356 0.9517 0.8935 -0.0163 -0.0227 0.0239  241 ILE A CA    
1982 C  C     . ILE A 241 ? 0.8179 1.0256 0.9521 -0.0203 -0.0336 0.0148  241 ILE A C     
1983 O  O     . ILE A 241 ? 0.8843 1.1014 1.0198 -0.0214 -0.0440 0.0171  241 ILE A O     
1984 C  CB    . ILE A 241 ? 0.7933 1.0237 0.9762 -0.0253 -0.0297 0.0285  241 ILE A CB    
1985 C  CG1   . ILE A 241 ? 0.9089 1.1564 1.1234 -0.0202 -0.0213 0.0423  241 ILE A CG1   
1986 C  CG2   . ILE A 241 ? 0.7231 0.9416 0.8987 -0.0316 -0.0275 0.0217  241 ILE A CG2   
1987 C  CD1   . ILE A 241 ? 0.7927 1.0322 1.0071 -0.0130 -0.0026 0.0447  241 ILE A CD1   
1988 N  N     . GLN A 242 ? 0.9207 1.1111 1.0333 -0.0217 -0.0307 0.0054  242 GLN A N     
1989 C  CA    . GLN A 242 ? 0.9902 1.1715 1.0805 -0.0252 -0.0388 -0.0033 242 GLN A CA    
1990 C  C     . GLN A 242 ? 0.9933 1.1672 1.0794 -0.0334 -0.0425 -0.0108 242 GLN A C     
1991 O  O     . GLN A 242 ? 1.0465 1.2231 1.1480 -0.0369 -0.0395 -0.0084 242 GLN A O     
1992 C  CB    . GLN A 242 ? 0.7840 0.9511 0.8542 -0.0186 -0.0317 -0.0066 242 GLN A CB    
1993 C  CG    . GLN A 242 ? 0.9190 1.0909 0.9923 -0.0109 -0.0293 0.0001  242 GLN A CG    
1994 C  CD    . GLN A 242 ? 1.2937 1.4702 1.3579 -0.0114 -0.0386 0.0005  242 GLN A CD    
1995 O  OE1   . GLN A 242 ? 1.5448 1.7311 1.6175 -0.0071 -0.0405 0.0081  242 GLN A OE1   
1996 N  NE2   . GLN A 242 ? 1.2381 1.4075 1.2849 -0.0157 -0.0437 -0.0070 242 GLN A NE2   
1997 N  N     . ARG A 243 ? 1.0411 1.2055 1.1070 -0.0361 -0.0484 -0.0193 243 ARG A N     
1998 C  CA    . ARG A 243 ? 1.2055 1.3604 1.2656 -0.0433 -0.0521 -0.0274 243 ARG A CA    
1999 C  C     . ARG A 243 ? 1.2185 1.3565 1.2585 -0.0400 -0.0449 -0.0336 243 ARG A C     
2000 O  O     . ARG A 243 ? 1.4096 1.5418 1.4315 -0.0381 -0.0472 -0.0382 243 ARG A O     
2001 C  CB    . ARG A 243 ? 1.3048 1.4625 1.3588 -0.0495 -0.0663 -0.0326 243 ARG A CB    
2002 C  CG    . ARG A 243 ? 1.2919 1.4606 1.3682 -0.0579 -0.0757 -0.0299 243 ARG A CG    
2003 C  CD    . ARG A 243 ? 1.4834 1.6486 1.5481 -0.0654 -0.0908 -0.0385 243 ARG A CD    
2004 N  NE    . ARG A 243 ? 1.5974 1.7620 1.6785 -0.0755 -0.0985 -0.0409 243 ARG A NE    
2005 C  CZ    . ARG A 243 ? 1.4654 1.6184 1.5508 -0.0786 -0.0925 -0.0444 243 ARG A CZ    
2006 N  NH1   . ARG A 243 ? 1.3865 1.5271 1.4592 -0.0725 -0.0795 -0.0468 243 ARG A NH1   
2007 N  NH2   . ARG A 243 ? 1.3289 1.4829 1.4332 -0.0884 -0.1004 -0.0448 243 ARG A NH2   
2008 N  N     . MET A 244 ? 1.1424 1.2734 1.1862 -0.0391 -0.0359 -0.0326 244 MET A N     
2009 C  CA    . MET A 244 ? 1.3051 1.4209 1.3333 -0.0371 -0.0302 -0.0374 244 MET A CA    
2010 C  C     . MET A 244 ? 1.3604 1.4680 1.3873 -0.0436 -0.0337 -0.0440 244 MET A C     
2011 O  O     . MET A 244 ? 1.3104 1.4134 1.3452 -0.0461 -0.0295 -0.0430 244 MET A O     
2012 C  CB    . MET A 244 ? 1.2031 1.3148 1.2334 -0.0326 -0.0199 -0.0329 244 MET A CB    
2013 C  CG    . MET A 244 ? 1.0728 1.1847 1.0969 -0.0254 -0.0160 -0.0294 244 MET A CG    
2014 S  SD    . MET A 244 ? 1.4915 1.5937 1.4964 -0.0226 -0.0176 -0.0336 244 MET A SD    
2015 C  CE    . MET A 244 ? 1.2548 1.3690 1.2612 -0.0206 -0.0239 -0.0308 244 MET A CE    
2016 N  N     . GLY A 245 ? 1.3003 1.4049 1.3160 -0.0459 -0.0413 -0.0507 245 GLY A N     
2017 C  CA    . GLY A 245 ? 1.3247 1.4190 1.3375 -0.0517 -0.0453 -0.0585 245 GLY A CA    
2018 C  C     . GLY A 245 ? 1.4476 1.5485 1.4790 -0.0598 -0.0528 -0.0577 245 GLY A C     
2019 O  O     . GLY A 245 ? 1.5430 1.6578 1.5849 -0.0617 -0.0593 -0.0534 245 GLY A O     
2020 N  N     . ASP A 246 ? 1.5033 1.5944 1.5410 -0.0650 -0.0523 -0.0609 246 ASP A N     
2021 C  CA    . ASP A 246 ? 1.5448 1.6413 1.6040 -0.0737 -0.0591 -0.0590 246 ASP A CA    
2022 C  C     . ASP A 246 ? 1.5177 1.6308 1.5996 -0.0726 -0.0543 -0.0467 246 ASP A C     
2023 O  O     . ASP A 246 ? 1.5011 1.6272 1.6022 -0.0779 -0.0619 -0.0422 246 ASP A O     
2024 C  CB    . ASP A 246 ? 1.7697 1.8515 1.8333 -0.0784 -0.0571 -0.0630 246 ASP A CB    
2025 C  CG    . ASP A 246 ? 1.9938 2.0597 2.0413 -0.0821 -0.0653 -0.0760 246 ASP A CG    
2026 O  OD1   . ASP A 246 ? 2.0395 2.1059 2.0693 -0.0802 -0.0716 -0.0820 246 ASP A OD1   
2027 O  OD2   . ASP A 246 ? 2.0183 2.0705 2.0701 -0.0863 -0.0648 -0.0802 246 ASP A OD2   
2028 N  N     . ARG A 247 ? 1.4937 1.6064 1.5737 -0.0655 -0.0419 -0.0408 247 ARG A N     
2029 C  CA    . ARG A 247 ? 1.3573 1.4831 1.4543 -0.0622 -0.0346 -0.0297 247 ARG A CA    
2030 C  C     . ARG A 247 ? 1.2600 1.3948 1.3507 -0.0552 -0.0339 -0.0269 247 ARG A C     
2031 O  O     . ARG A 247 ? 1.3001 1.4320 1.3744 -0.0535 -0.0394 -0.0326 247 ARG A O     
2032 C  CB    . ARG A 247 ? 1.4067 1.5252 1.5021 -0.0583 -0.0219 -0.0255 247 ARG A CB    
2033 C  CG    . ARG A 247 ? 1.4633 1.5721 1.5652 -0.0646 -0.0219 -0.0271 247 ARG A CG    
2034 C  CD    . ARG A 247 ? 1.6296 1.7249 1.7159 -0.0598 -0.0131 -0.0278 247 ARG A CD    
2035 N  NE    . ARG A 247 ? 1.7456 1.8355 1.8097 -0.0534 -0.0126 -0.0327 247 ARG A NE    
2036 C  CZ    . ARG A 247 ? 1.8640 1.9445 1.9138 -0.0484 -0.0063 -0.0326 247 ARG A CZ    
2037 N  NH1   . ARG A 247 ? 1.8942 1.9689 1.9463 -0.0484 0.0001  -0.0281 247 ARG A NH1   
2038 N  NH2   . ARG A 247 ? 1.7890 1.8660 1.8223 -0.0436 -0.0071 -0.0363 247 ARG A NH2   
2039 N  N     . PHE A 248 ? 0.9863 1.1317 1.0903 -0.0504 -0.0263 -0.0174 248 PHE A N     
2040 C  CA    . PHE A 248 ? 0.9970 1.1516 1.1004 -0.0439 -0.0255 -0.0133 248 PHE A CA    
2041 C  C     . PHE A 248 ? 0.9278 1.0763 1.0218 -0.0346 -0.0124 -0.0103 248 PHE A C     
2042 O  O     . PHE A 248 ? 0.8933 1.0329 0.9829 -0.0334 -0.0042 -0.0099 248 PHE A O     
2043 C  CB    . PHE A 248 ? 1.0310 1.2051 1.1618 -0.0459 -0.0292 -0.0042 248 PHE A CB    
2044 C  CG    . PHE A 248 ? 1.0573 1.2374 1.2014 -0.0568 -0.0430 -0.0062 248 PHE A CG    
2045 C  CD1   . PHE A 248 ? 0.9831 1.1787 1.1581 -0.0615 -0.0452 0.0031  248 PHE A CD1   
2046 C  CD2   . PHE A 248 ? 1.2446 1.4144 1.3706 -0.0620 -0.0539 -0.0172 248 PHE A CD2   
2047 C  CE1   . PHE A 248 ? 1.0710 1.2711 1.2592 -0.0727 -0.0598 0.0010  248 PHE A CE1   
2048 C  CE2   . PHE A 248 ? 1.3249 1.4973 1.4604 -0.0722 -0.0675 -0.0205 248 PHE A CE2   
2049 C  CZ    . PHE A 248 ? 1.0973 1.2846 1.2642 -0.0782 -0.0716 -0.0117 248 PHE A CZ    
2050 N  N     . ALA A 249 ? 0.8490 1.0012 0.9390 -0.0280 -0.0112 -0.0081 249 ALA A N     
2051 C  CA    . ALA A 249 ? 0.8011 0.9467 0.8826 -0.0190 -0.0002 -0.0057 249 ALA A CA    
2052 C  C     . ALA A 249 ? 0.7094 0.8673 0.8044 -0.0131 0.0020  0.0017  249 ALA A C     
2053 O  O     . ALA A 249 ? 0.7200 0.8896 0.8245 -0.0154 -0.0070 0.0037  249 ALA A O     
2054 C  CB    . ALA A 249 ? 0.6635 0.7940 0.7206 -0.0163 -0.0008 -0.0126 249 ALA A CB    
2055 N  N     . VAL A 250 ? 0.6420 0.7964 0.7369 -0.0049 0.0140  0.0058  250 VAL A N     
2056 C  CA    . VAL A 250 ? 0.7007 0.8660 0.8113 0.0023  0.0191  0.0139  250 VAL A CA    
2057 C  C     . VAL A 250 ? 0.6909 0.8430 0.7843 0.0110  0.0243  0.0112  250 VAL A C     
2058 O  O     . VAL A 250 ? 0.6926 0.8282 0.7673 0.0146  0.0314  0.0066  250 VAL A O     
2059 C  CB    . VAL A 250 ? 0.6650 0.8382 0.7936 0.0056  0.0309  0.0224  250 VAL A CB    
2060 C  CG1   . VAL A 250 ? 0.6847 0.8677 0.8291 0.0150  0.0384  0.0310  250 VAL A CG1   
2061 C  CG2   . VAL A 250 ? 0.5536 0.7410 0.7042 -0.0041 0.0243  0.0264  250 VAL A CG2   
2062 N  N     . GLU A 251 ? 0.7074 0.8664 0.8075 0.0140  0.0199  0.0144  251 GLU A N     
2063 C  CA    . GLU A 251 ? 0.5551 0.7028 0.6442 0.0223  0.0241  0.0133  251 GLU A CA    
2064 C  C     . GLU A 251 ? 0.7640 0.9185 0.8702 0.0318  0.0343  0.0217  251 GLU A C     
2065 O  O     . GLU A 251 ? 0.8248 0.9988 0.9560 0.0311  0.0337  0.0304  251 GLU A O     
2066 C  CB    . GLU A 251 ? 0.5451 0.6952 0.6306 0.0199  0.0130  0.0125  251 GLU A CB    
2067 C  CG    . GLU A 251 ? 0.8726 1.0041 0.9366 0.0219  0.0127  0.0062  251 GLU A CG    
2068 C  CD    . GLU A 251 ? 0.9691 1.1051 1.0303 0.0189  0.0024  0.0067  251 GLU A CD    
2069 O  OE1   . GLU A 251 ? 0.7476 0.9000 0.8202 0.0153  -0.0051 0.0109  251 GLU A OE1   
2070 O  OE2   . GLU A 251 ? 0.8608 0.9839 0.9083 0.0199  0.0014  0.0035  251 GLU A OE2   
2071 N  N     . VAL A 252 ? 0.7413 0.8794 0.8346 0.0407  0.0434  0.0192  252 VAL A N     
2072 C  CA    . VAL A 252 ? 0.4636 0.6039 0.5699 0.0518  0.0548  0.0261  252 VAL A CA    
2073 C  C     . VAL A 252 ? 0.5514 0.6785 0.6483 0.0574  0.0532  0.0236  252 VAL A C     
2074 O  O     . VAL A 252 ? 0.6625 0.7668 0.7362 0.0601  0.0563  0.0154  252 VAL A O     
2075 C  CB    . VAL A 252 ? 0.6943 0.8241 0.7923 0.0589  0.0705  0.0251  252 VAL A CB    
2076 C  CG1   . VAL A 252 ? 0.7142 0.8461 0.8261 0.0719  0.0838  0.0324  252 VAL A CG1   
2077 C  CG2   . VAL A 252 ? 0.5924 0.7349 0.7006 0.0526  0.0718  0.0286  252 VAL A CG2   
2078 N  N     . LYS A 253 ? 0.5909 0.7320 0.7064 0.0587  0.0477  0.0314  253 LYS A N     
2079 C  CA    . LYS A 253 ? 0.6207 0.7515 0.7303 0.0624  0.0442  0.0307  253 LYS A CA    
2080 C  C     . LYS A 253 ? 0.7115 0.8203 0.8111 0.0735  0.0566  0.0273  253 LYS A C     
2081 O  O     . LYS A 253 ? 0.7661 0.8759 0.8745 0.0821  0.0693  0.0310  253 LYS A O     
2082 C  CB    . LYS A 253 ? 0.5221 0.6738 0.6562 0.0634  0.0377  0.0421  253 LYS A CB    
2083 C  CG    . LYS A 253 ? 0.5804 0.7495 0.7181 0.0523  0.0230  0.0437  253 LYS A CG    
2084 C  CD    . LYS A 253 ? 0.7440 0.9005 0.8590 0.0466  0.0148  0.0360  253 LYS A CD    
2085 C  CE    . LYS A 253 ? 0.7167 0.8821 0.8254 0.0357  0.0045  0.0321  253 LYS A CE    
2086 N  NZ    . LYS A 253 ? 0.7070 0.8748 0.8071 0.0318  -0.0061 0.0324  253 LYS A NZ    
2087 N  N     . GLY A 254 ? 0.7242 0.8123 0.8052 0.0733  0.0529  0.0203  254 GLY A N     
2088 C  CA    . GLY A 254 ? 0.6921 0.7544 0.7586 0.0822  0.0620  0.0143  254 GLY A CA    
2089 C  C     . GLY A 254 ? 0.6620 0.7054 0.7028 0.0819  0.0676  0.0039  254 GLY A C     
2090 O  O     . GLY A 254 ? 0.7618 0.7798 0.7842 0.0878  0.0727  -0.0034 254 GLY A O     
2091 N  N     . ARG A 255 ? 0.7382 0.7922 0.7765 0.0751  0.0664  0.0032  255 ARG A N     
2092 C  CA    . ARG A 255 ? 0.6690 0.7077 0.6835 0.0742  0.0710  -0.0050 255 ARG A CA    
2093 C  C     . ARG A 255 ? 0.8078 0.8524 0.8160 0.0620  0.0598  -0.0080 255 ARG A C     
2094 O  O     . ARG A 255 ? 0.9109 0.9720 0.9329 0.0550  0.0503  -0.0041 255 ARG A O     
2095 C  CB    . ARG A 255 ? 0.7428 0.7883 0.7631 0.0813  0.0857  -0.0006 255 ARG A CB    
2096 C  CG    . ARG A 255 ? 0.8295 0.8915 0.8780 0.0897  0.0939  0.0102  255 ARG A CG    
2097 C  CD    . ARG A 255 ? 0.7939 0.8599 0.8473 0.0986  0.1111  0.0150  255 ARG A CD    
2098 N  NE    . ARG A 255 ? 0.9374 0.9818 0.9773 0.1126  0.1249  0.0114  255 ARG A NE    
2099 C  CZ    . ARG A 255 ? 0.8552 0.9068 0.9150 0.1244  0.1378  0.0199  255 ARG A CZ    
2100 N  NH1   . ARG A 255 ? 0.7444 0.8260 0.8406 0.1236  0.1378  0.0335  255 ARG A NH1   
2101 N  NH2   . ARG A 255 ? 0.9850 1.0125 1.0282 0.1376  0.1506  0.0146  255 ARG A NH2   
2102 N  N     . ILE A 256 ? 0.7935 0.8237 0.7794 0.0600  0.0613  -0.0149 256 ILE A N     
2103 C  CA    . ILE A 256 ? 0.7835 0.8175 0.7631 0.0496  0.0526  -0.0176 256 ILE A CA    
2104 C  C     . ILE A 256 ? 0.6730 0.7155 0.6548 0.0492  0.0603  -0.0148 256 ILE A C     
2105 O  O     . ILE A 256 ? 0.6649 0.6945 0.6300 0.0544  0.0693  -0.0174 256 ILE A O     
2106 C  CB    . ILE A 256 ? 0.7920 0.8037 0.7468 0.0464  0.0461  -0.0262 256 ILE A CB    
2107 C  CG1   . ILE A 256 ? 0.8587 0.8650 0.8164 0.0447  0.0371  -0.0270 256 ILE A CG1   
2108 C  CG2   . ILE A 256 ? 0.8099 0.8250 0.7584 0.0376  0.0401  -0.0279 256 ILE A CG2   
2109 C  CD1   . ILE A 256 ? 0.8993 0.9188 0.8662 0.0356  0.0262  -0.0248 256 ILE A CD1   
2110 N  N     . HIS A 257 ? 0.7272 0.7911 0.7292 0.0431  0.0567  -0.0091 257 HIS A N     
2111 C  CA    . HIS A 257 ? 0.7114 0.7835 0.7179 0.0405  0.0619  -0.0059 257 HIS A CA    
2112 C  C     . HIS A 257 ? 0.7039 0.7655 0.6920 0.0333  0.0557  -0.0120 257 HIS A C     
2113 O  O     . HIS A 257 ? 0.7385 0.8030 0.7281 0.0257  0.0447  -0.0145 257 HIS A O     
2114 C  CB    . HIS A 257 ? 0.6535 0.7501 0.6886 0.0352  0.0582  0.0016  257 HIS A CB    
2115 C  CG    . HIS A 257 ? 0.6102 0.7145 0.6521 0.0302  0.0611  0.0048  257 HIS A CG    
2116 N  ND1   . HIS A 257 ? 0.6427 0.7622 0.7023 0.0208  0.0524  0.0073  257 HIS A ND1   
2117 C  CD2   . HIS A 257 ? 0.5549 0.6530 0.5880 0.0332  0.0715  0.0062  257 HIS A CD2   
2118 C  CE1   . HIS A 257 ? 0.6546 0.7768 0.7184 0.0179  0.0573  0.0103  257 HIS A CE1   
2119 N  NE2   . HIS A 257 ? 0.6494 0.7596 0.6975 0.0255  0.0692  0.0105  257 HIS A NE2   
2120 N  N     . PHE A 258 ? 0.7645 0.8137 0.7348 0.0365  0.0632  -0.0137 258 PHE A N     
2121 C  CA    . PHE A 258 ? 0.7025 0.7413 0.6551 0.0307  0.0579  -0.0181 258 PHE A CA    
2122 C  C     . PHE A 258 ? 0.8062 0.8550 0.7673 0.0278  0.0633  -0.0124 258 PHE A C     
2123 O  O     . PHE A 258 ? 0.8899 0.9342 0.8421 0.0334  0.0743  -0.0095 258 PHE A O     
2124 C  CB    . PHE A 258 ? 0.7530 0.7683 0.6760 0.0359  0.0601  -0.0243 258 PHE A CB    
2125 C  CG    . PHE A 258 ? 0.8438 0.8483 0.7500 0.0295  0.0511  -0.0286 258 PHE A CG    
2126 C  CD1   . PHE A 258 ? 0.8767 0.8860 0.7911 0.0215  0.0393  -0.0299 258 PHE A CD1   
2127 C  CD2   . PHE A 258 ? 0.8851 0.8752 0.7672 0.0319  0.0547  -0.0304 258 PHE A CD2   
2128 C  CE1   . PHE A 258 ? 0.8880 0.8888 0.7903 0.0162  0.0316  -0.0324 258 PHE A CE1   
2129 C  CE2   . PHE A 258 ? 0.8889 0.8703 0.7577 0.0259  0.0455  -0.0329 258 PHE A CE2   
2130 C  CZ    . PHE A 258 ? 0.9556 0.9429 0.8362 0.0181  0.0341  -0.0336 258 PHE A CZ    
2131 N  N     . ASP A 259 ? 0.7356 0.7973 0.7138 0.0192  0.0559  -0.0106 259 ASP A N     
2132 C  CA    . ASP A 259 ? 0.5827 0.6515 0.5695 0.0146  0.0587  -0.0058 259 ASP A CA    
2133 C  C     . ASP A 259 ? 0.8777 0.9321 0.8437 0.0116  0.0551  -0.0097 259 ASP A C     
2134 O  O     . ASP A 259 ? 0.8247 0.8751 0.7867 0.0063  0.0448  -0.0146 259 ASP A O     
2135 C  CB    . ASP A 259 ? 0.5894 0.6744 0.6009 0.0064  0.0511  -0.0037 259 ASP A CB    
2136 C  CG    . ASP A 259 ? 0.7930 0.8856 0.8184 0.0017  0.0546  0.0024  259 ASP A CG    
2137 O  OD1   . ASP A 259 ? 0.7334 0.8185 0.7475 0.0043  0.0625  0.0051  259 ASP A OD1   
2138 O  OD2   . ASP A 259 ? 0.8388 0.9444 0.8861 -0.0049 0.0490  0.0046  259 ASP A OD2   
2139 N  N     . LEU A 260 ? 0.8405 0.8878 0.7933 0.0155  0.0639  -0.0066 260 LEU A N     
2140 C  CA    . LEU A 260 ? 0.8913 0.9255 0.8240 0.0131  0.0601  -0.0088 260 LEU A CA    
2141 C  C     . LEU A 260 ? 0.8996 0.9404 0.8459 0.0044  0.0544  -0.0065 260 LEU A C     
2142 O  O     . LEU A 260 ? 0.9445 0.9762 0.8792 0.0011  0.0478  -0.0090 260 LEU A O     
2143 C  CB    . LEU A 260 ? 0.8019 0.8273 0.7152 0.0200  0.0714  -0.0051 260 LEU A CB    
2144 C  CG    . LEU A 260 ? 0.7123 0.7225 0.6006 0.0291  0.0761  -0.0101 260 LEU A CG    
2145 C  CD1   . LEU A 260 ? 0.7853 0.7932 0.6623 0.0377  0.0919  -0.0042 260 LEU A CD1   
2146 C  CD2   . LEU A 260 ? 0.8427 0.8344 0.7050 0.0271  0.0652  -0.0176 260 LEU A CD2   
2147 N  N     . TYR A 261 ? 0.8028 0.8584 0.7743 0.0007  0.0562  -0.0017 261 TYR A N     
2148 C  CA    . TYR A 261 ? 0.8348 0.8939 0.8188 -0.0071 0.0520  0.0004  261 TYR A CA    
2149 C  C     . TYR A 261 ? 0.8754 0.9290 0.8557 -0.0124 0.0403  -0.0067 261 TYR A C     
2150 O  O     . TYR A 261 ? 0.9268 0.9732 0.9012 -0.0151 0.0379  -0.0062 261 TYR A O     
2151 C  CB    . TYR A 261 ? 0.8021 0.8772 0.8150 -0.0111 0.0539  0.0057  261 TYR A CB    
2152 C  CG    . TYR A 261 ? 0.8260 0.9024 0.8522 -0.0187 0.0513  0.0087  261 TYR A CG    
2153 C  CD1   . TYR A 261 ? 0.9304 1.0069 0.9598 -0.0181 0.0601  0.0177  261 TYR A CD1   
2154 C  CD2   . TYR A 261 ? 0.8866 0.9631 0.9214 -0.0260 0.0407  0.0028  261 TYR A CD2   
2155 C  CE1   . TYR A 261 ? 1.0935 1.1700 1.1368 -0.0251 0.0577  0.0210  261 TYR A CE1   
2156 C  CE2   . TYR A 261 ? 1.0402 1.1152 1.0869 -0.0326 0.0385  0.0046  261 TYR A CE2   
2157 C  CZ    . TYR A 261 ? 1.1580 1.2329 1.2102 -0.0324 0.0467  0.0139  261 TYR A CZ    
2158 O  OH    . TYR A 261 ? 1.1773 1.2497 1.2431 -0.0391 0.0444  0.0163  261 TYR A OH    
2159 N  N     . PRO A 262 ? 0.9394 0.9962 0.9233 -0.0134 0.0335  -0.0123 262 PRO A N     
2160 C  CA    . PRO A 262 ? 0.8652 0.9163 0.8439 -0.0170 0.0244  -0.0179 262 PRO A CA    
2161 C  C     . PRO A 262 ? 0.8321 0.8702 0.7906 -0.0144 0.0226  -0.0194 262 PRO A C     
2162 O  O     . PRO A 262 ? 0.9262 0.9592 0.8823 -0.0174 0.0175  -0.0206 262 PRO A O     
2163 C  CB    . PRO A 262 ? 0.6615 0.7194 0.6461 -0.0169 0.0194  -0.0218 262 PRO A CB    
2164 C  CG    . PRO A 262 ? 0.7448 0.8078 0.7318 -0.0115 0.0254  -0.0188 262 PRO A CG    
2165 C  CD    . PRO A 262 ? 0.7990 0.8656 0.7929 -0.0110 0.0340  -0.0125 262 PRO A CD    
2166 N  N     . VAL A 263 ? 0.8883 0.9202 0.8326 -0.0088 0.0262  -0.0193 263 VAL A N     
2167 C  CA    . VAL A 263 ? 0.9840 1.0024 0.9083 -0.0072 0.0221  -0.0214 263 VAL A CA    
2168 C  C     . VAL A 263 ? 0.9849 0.9973 0.9007 -0.0084 0.0233  -0.0173 263 VAL A C     
2169 O  O     . VAL A 263 ? 0.9505 0.9560 0.8594 -0.0107 0.0165  -0.0176 263 VAL A O     
2170 C  CB    . VAL A 263 ? 0.8225 0.8332 0.7319 -0.0008 0.0254  -0.0237 263 VAL A CB    
2171 C  CG1   . VAL A 263 ? 0.8961 0.8906 0.7827 0.0001  0.0200  -0.0261 263 VAL A CG1   
2172 C  CG2   . VAL A 263 ? 0.8449 0.8605 0.7635 0.0002  0.0227  -0.0270 263 VAL A CG2   
2173 N  N     . ILE A 264 ? 0.9748 0.9908 0.8931 -0.0068 0.0321  -0.0119 264 ILE A N     
2174 C  CA    . ILE A 264 ? 0.9790 0.9894 0.8880 -0.0071 0.0343  -0.0063 264 ILE A CA    
2175 C  C     . ILE A 264 ? 0.9625 0.9750 0.8847 -0.0133 0.0287  -0.0045 264 ILE A C     
2176 O  O     . ILE A 264 ? 1.0624 1.0675 0.9755 -0.0145 0.0230  -0.0033 264 ILE A O     
2177 C  CB    . ILE A 264 ? 1.0343 1.0497 0.9459 -0.0038 0.0465  0.0008  264 ILE A CB    
2178 C  CG1   . ILE A 264 ? 0.9281 0.9391 0.8235 0.0042  0.0538  -0.0008 264 ILE A CG1   
2179 C  CG2   . ILE A 264 ? 1.0258 1.0365 0.9292 -0.0043 0.0489  0.0083  264 ILE A CG2   
2180 C  CD1   . ILE A 264 ? 0.8656 0.8601 0.7317 0.0074  0.0484  -0.0062 264 ILE A CD1   
2181 N  N     . ARG A 265 ? 0.9556 0.9777 0.8999 -0.0171 0.0300  -0.0042 265 ARG A N     
2182 C  CA    . ARG A 265 ? 0.9982 1.0203 0.9552 -0.0223 0.0260  -0.0034 265 ARG A CA    
2183 C  C     . ARG A 265 ? 1.0692 1.0859 1.0210 -0.0232 0.0175  -0.0079 265 ARG A C     
2184 O  O     . ARG A 265 ? 1.3044 1.3163 1.2566 -0.0247 0.0148  -0.0049 265 ARG A O     
2185 C  CB    . ARG A 265 ? 1.0545 1.0855 1.0332 -0.0265 0.0265  -0.0053 265 ARG A CB    
2186 C  CG    . ARG A 265 ? 1.0787 1.1185 1.0676 -0.0258 0.0339  -0.0007 265 ARG A CG    
2187 C  CD    . ARG A 265 ? 1.2251 1.2710 1.2374 -0.0322 0.0331  0.0003  265 ARG A CD    
2188 N  NE    . ARG A 265 ? 1.4038 1.4421 1.4198 -0.0359 0.0302  0.0007  265 ARG A NE    
2189 C  CZ    . ARG A 265 ? 1.5992 1.6372 1.6313 -0.0416 0.0264  -0.0022 265 ARG A CZ    
2190 N  NH1   . ARG A 265 ? 1.3251 1.3707 1.3707 -0.0454 0.0235  -0.0059 265 ARG A NH1   
2191 N  NH2   . ARG A 265 ? 1.5918 1.6209 1.6263 -0.0437 0.0251  -0.0014 265 ARG A NH2   
2192 N  N     . ARG A 266 ? 1.0557 1.0738 1.0046 -0.0220 0.0138  -0.0137 266 ARG A N     
2193 C  CA    . ARG A 266 ? 0.9597 0.9745 0.9066 -0.0226 0.0066  -0.0166 266 ARG A CA    
2194 C  C     . ARG A 266 ? 0.9319 0.9378 0.8638 -0.0212 0.0023  -0.0136 266 ARG A C     
2195 O  O     . ARG A 266 ? 1.0704 1.0741 1.0045 -0.0225 -0.0035 -0.0128 266 ARG A O     
2196 C  CB    . ARG A 266 ? 0.8725 0.8918 0.8210 -0.0215 0.0044  -0.0219 266 ARG A CB    
2197 C  CG    . ARG A 266 ? 1.0359 1.0508 0.9771 -0.0204 -0.0017 -0.0233 266 ARG A CG    
2198 C  CD    . ARG A 266 ? 1.1639 1.1837 1.1074 -0.0189 -0.0024 -0.0271 266 ARG A CD    
2199 N  NE    . ARG A 266 ? 1.1056 1.1204 1.0378 -0.0156 -0.0016 -0.0278 266 ARG A NE    
2200 C  CZ    . ARG A 266 ? 1.3175 1.3229 1.2384 -0.0147 -0.0064 -0.0280 266 ARG A CZ    
2201 N  NH1   . ARG A 266 ? 1.3273 1.3298 1.2495 -0.0171 -0.0129 -0.0263 266 ARG A NH1   
2202 N  NH2   . ARG A 266 ? 1.1764 1.1747 1.0849 -0.0112 -0.0048 -0.0298 266 ARG A NH2   
2203 N  N     . THR A 267 ? 1.0156 1.0165 0.9323 -0.0186 0.0050  -0.0115 267 THR A N     
2204 C  CA    . THR A 267 ? 0.9521 0.9429 0.8505 -0.0176 -0.0007 -0.0098 267 THR A CA    
2205 C  C     . THR A 267 ? 1.0764 1.0638 0.9692 -0.0180 0.0003  -0.0024 267 THR A C     
2206 O  O     . THR A 267 ? 1.1388 1.1219 1.0284 -0.0197 -0.0072 0.0011  267 THR A O     
2207 C  CB    . THR A 267 ? 1.0004 0.9846 0.8802 -0.0134 0.0009  -0.0137 267 THR A CB    
2208 O  OG1   . THR A 267 ? 1.1950 1.1787 1.0775 -0.0136 -0.0042 -0.0192 267 THR A OG1   
2209 C  CG2   . THR A 267 ? 0.9781 0.9498 0.8338 -0.0120 -0.0033 -0.0117 267 THR A CG2   
2210 N  N     . ILE A 268 ? 1.1330 1.1232 1.0263 -0.0165 0.0094  0.0015  268 ILE A N     
2211 C  CA    . ILE A 268 ? 1.0411 1.0283 0.9281 -0.0162 0.0117  0.0100  268 ILE A CA    
2212 C  C     . ILE A 268 ? 0.9752 0.9688 0.8857 -0.0197 0.0150  0.0146  268 ILE A C     
2213 O  O     . ILE A 268 ? 1.1341 1.1346 1.0622 -0.0215 0.0187  0.0112  268 ILE A O     
2214 C  CB    . ILE A 268 ? 0.9992 0.9837 0.8687 -0.0114 0.0208  0.0128  268 ILE A CB    
2215 C  CG1   . ILE A 268 ? 1.1488 1.1217 0.9892 -0.0077 0.0162  0.0082  268 ILE A CG1   
2216 C  CG2   . ILE A 268 ? 1.1507 1.1345 1.0166 -0.0109 0.0255  0.0233  268 ILE A CG2   
2217 C  CD1   . ILE A 268 ? 1.1890 1.1579 1.0099 -0.0013 0.0269  0.0098  268 ILE A CD1   
2218 N  N     . ASN A 269 ? 1.0376 1.0281 0.9484 -0.0207 0.0129  0.0225  269 ASN A N     
2219 C  CA    . ASN A 269 ? 1.0207 1.0144 0.9528 -0.0235 0.0164  0.0279  269 ASN A CA    
2220 C  C     . ASN A 269 ? 1.0345 1.0286 0.9631 -0.0221 0.0248  0.0375  269 ASN A C     
2221 O  O     . ASN A 269 ? 1.1191 1.1087 1.0341 -0.0204 0.0235  0.0456  269 ASN A O     
2222 C  CB    . ASN A 269 ? 1.1044 1.0950 1.0432 -0.0249 0.0092  0.0315  269 ASN A CB    
2223 C  CG    . ASN A 269 ? 1.1918 1.1836 1.1549 -0.0274 0.0125  0.0335  269 ASN A CG    
2224 O  OD1   . ASN A 269 ? 1.2215 1.2122 1.1913 -0.0280 0.0170  0.0419  269 ASN A OD1   
2225 N  ND2   . ASN A 269 ? 1.1732 1.1661 1.1486 -0.0287 0.0105  0.0256  269 ASN A ND2   
2226 N  N     . LEU A 270 ? 1.0941 1.0945 1.0358 -0.0229 0.0332  0.0376  270 LEU A N     
2227 C  CA    . LEU A 270 ? 0.9221 0.9250 0.8660 -0.0217 0.0430  0.0481  270 LEU A CA    
2228 C  C     . LEU A 270 ? 0.9558 0.9631 0.9295 -0.0268 0.0464  0.0512  270 LEU A C     
2229 O  O     . LEU A 270 ? 1.0142 1.0243 1.0039 -0.0304 0.0434  0.0428  270 LEU A O     
2230 C  CB    . LEU A 270 ? 0.9650 0.9720 0.8978 -0.0174 0.0513  0.0474  270 LEU A CB    
2231 C  CG    . LEU A 270 ? 0.9924 0.9920 0.8918 -0.0113 0.0505  0.0454  270 LEU A CG    
2232 C  CD1   . LEU A 270 ? 0.8284 0.8316 0.7193 -0.0056 0.0625  0.0472  270 LEU A CD1   
2233 C  CD2   . LEU A 270 ? 0.9280 0.9197 0.8086 -0.0099 0.0469  0.0534  270 LEU A CD2   
2234 N  N     . PRO A 271 ? 0.9035 0.9108 0.8848 -0.0273 0.0524  0.0634  271 PRO A N     
2235 C  CA    . PRO A 271 ? 0.8668 0.8770 0.8782 -0.0328 0.0557  0.0667  271 PRO A CA    
2236 C  C     . PRO A 271 ? 0.9460 0.9656 0.9714 -0.0347 0.0609  0.0643  271 PRO A C     
2237 O  O     . PRO A 271 ? 0.9780 0.9994 1.0268 -0.0406 0.0584  0.0599  271 PRO A O     
2238 C  CB    . PRO A 271 ? 0.9263 0.9347 0.9398 -0.0319 0.0618  0.0826  271 PRO A CB    
2239 C  CG    . PRO A 271 ? 0.9542 0.9615 0.9362 -0.0251 0.0645  0.0876  271 PRO A CG    
2240 C  CD    . PRO A 271 ? 0.7708 0.7742 0.7332 -0.0232 0.0553  0.0751  271 PRO A CD    
2241 N  N     . THR A 272 ? 0.8981 0.9233 0.9096 -0.0296 0.0680  0.0670  272 THR A N     
2242 C  CA    . THR A 272 ? 0.9810 1.0169 1.0063 -0.0302 0.0732  0.0657  272 THR A CA    
2243 C  C     . THR A 272 ? 0.9837 1.0205 0.9865 -0.0240 0.0736  0.0582  272 THR A C     
2244 O  O     . THR A 272 ? 0.9770 1.0067 0.9517 -0.0182 0.0742  0.0584  272 THR A O     
2245 C  CB    . THR A 272 ? 0.7394 0.7831 0.7781 -0.0294 0.0857  0.0808  272 THR A CB    
2246 O  OG1   . THR A 272 ? 1.0997 1.1381 1.1158 -0.0234 0.0919  0.0908  272 THR A OG1   
2247 C  CG2   . THR A 272 ? 0.7879 0.8335 0.8603 -0.0379 0.0843  0.0860  272 THR A CG2   
2248 N  N     . TYR A 273 ? 0.9022 0.9469 0.9176 -0.0255 0.0724  0.0517  273 TYR A N     
2249 C  CA    . TYR A 273 ? 0.8722 0.9177 0.8707 -0.0199 0.0725  0.0443  273 TYR A CA    
2250 C  C     . TYR A 273 ? 1.0106 1.0676 1.0194 -0.0162 0.0834  0.0501  273 TYR A C     
2251 O  O     . TYR A 273 ? 1.0482 1.1114 1.0622 -0.0151 0.0821  0.0443  273 TYR A O     
2252 C  CB    . TYR A 273 ? 0.9596 1.0042 0.9614 -0.0235 0.0611  0.0315  273 TYR A CB    
2253 C  CG    . TYR A 273 ? 1.0148 1.0485 1.0039 -0.0249 0.0519  0.0260  273 TYR A CG    
2254 C  CD1   . TYR A 273 ? 1.0064 1.0315 0.9690 -0.0200 0.0495  0.0237  273 TYR A CD1   
2255 C  CD2   . TYR A 273 ? 1.0597 1.0912 1.0639 -0.0310 0.0455  0.0233  273 TYR A CD2   
2256 C  CE1   . TYR A 273 ? 1.0054 1.0225 0.9602 -0.0216 0.0408  0.0204  273 TYR A CE1   
2257 C  CE2   . TYR A 273 ? 1.0654 1.0882 1.0606 -0.0313 0.0385  0.0197  273 TYR A CE2   
2258 C  CZ    . TYR A 273 ? 0.9896 1.0064 0.9617 -0.0268 0.0360  0.0190  273 TYR A CZ    
2259 O  OH    . TYR A 273 ? 1.1149 1.1250 1.0819 -0.0274 0.0287  0.0171  273 TYR A OH    
2260 N  N     . THR A 274 ? 0.9685 1.0296 0.9821 -0.0138 0.0950  0.0631  274 THR A N     
2261 C  CA    . THR A 274 ? 0.7296 0.8015 0.7503 -0.0080 0.1080  0.0706  274 THR A CA    
2262 C  C     . THR A 274 ? 0.8993 0.9629 0.8852 0.0028  0.1142  0.0669  274 THR A C     
2263 O  O     . THR A 274 ? 0.9880 1.0375 0.9441 0.0051  0.1091  0.0615  274 THR A O     
2264 C  CB    . THR A 274 ? 0.8192 0.8984 0.8565 -0.0082 0.1199  0.0872  274 THR A CB    
2265 O  OG1   . THR A 274 ? 0.9322 1.0013 0.9398 -0.0017 0.1266  0.0931  274 THR A OG1   
2266 C  CG2   . THR A 274 ? 0.7136 0.7954 0.7810 -0.0194 0.1121  0.0900  274 THR A CG2   
2267 N  N     . LEU A 275 ? 0.9087 0.9807 0.8993 0.0094  0.1249  0.0699  275 LEU A N     
2268 C  CA    . LEU A 275 ? 0.8928 0.9550 0.8502 0.0206  0.1323  0.0658  275 LEU A CA    
2269 C  C     . LEU A 275 ? 0.9937 1.0449 0.9209 0.0267  0.1406  0.0725  275 LEU A C     
2270 O  O     . LEU A 275 ? 0.9646 0.9995 0.8554 0.0313  0.1367  0.0648  275 LEU A O     
2271 C  CB    . LEU A 275 ? 0.9698 1.0439 0.9417 0.0277  0.1452  0.0705  275 LEU A CB    
2272 C  CG    . LEU A 275 ? 0.9699 1.0329 0.9110 0.0396  0.1522  0.0636  275 LEU A CG    
2273 C  CD1   . LEU A 275 ? 0.8178 0.8642 0.7337 0.0376  0.1368  0.0479  275 LEU A CD1   
2274 C  CD2   . LEU A 275 ? 0.8496 0.9265 0.8141 0.0449  0.1613  0.0669  275 LEU A CD2   
2275 N  N     . GLU A 276 ? 0.9294 0.9894 0.8715 0.0264  0.1512  0.0875  276 GLU A N     
2276 C  CA    . GLU A 276 ? 0.9110 0.9620 0.8246 0.0325  0.1597  0.0960  276 GLU A CA    
2277 C  C     . GLU A 276 ? 0.9729 1.0104 0.8673 0.0270  0.1450  0.0909  276 GLU A C     
2278 O  O     . GLU A 276 ? 1.0328 1.0565 0.8894 0.0327  0.1452  0.0899  276 GLU A O     
2279 C  CB    . GLU A 276 ? 0.9685 1.0335 0.9079 0.0322  0.1738  0.1150  276 GLU A CB    
2280 C  CG    . GLU A 276 ? 1.0162 1.0966 0.9771 0.0385  0.1904  0.1234  276 GLU A CG    
2281 C  CD    . GLU A 276 ? 1.0532 1.1486 1.0569 0.0300  0.1826  0.1202  276 GLU A CD    
2282 O  OE1   . GLU A 276 ? 0.9562 1.0534 0.9814 0.0181  0.1683  0.1171  276 GLU A OE1   
2283 O  OE2   . GLU A 276 ? 0.9982 1.1031 1.0134 0.0357  0.1908  0.1209  276 GLU A OE2   
2284 N  N     . ALA A 277 ? 0.9803 1.0214 0.9001 0.0162  0.1318  0.0876  277 ALA A N     
2285 C  CA    . ALA A 277 ? 1.0458 1.0757 0.9522 0.0113  0.1184  0.0837  277 ALA A CA    
2286 C  C     . ALA A 277 ? 1.0192 1.0366 0.8988 0.0129  0.1067  0.0687  277 ALA A C     
2287 O  O     . ALA A 277 ? 0.9812 0.9862 0.8326 0.0144  0.1001  0.0672  277 ALA A O     
2288 C  CB    . ALA A 277 ? 0.8582 0.8942 0.7995 0.0005  0.1094  0.0842  277 ALA A CB    
2289 N  N     . VAL A 278 ? 1.0146 1.0354 0.9039 0.0123  0.1032  0.0584  278 VAL A N     
2290 C  CA    . VAL A 278 ? 0.9492 0.9586 0.8167 0.0133  0.0924  0.0450  278 VAL A CA    
2291 C  C     . VAL A 278 ? 1.0786 1.0749 0.9072 0.0229  0.0981  0.0430  278 VAL A C     
2292 O  O     . VAL A 278 ? 1.0516 1.0337 0.8531 0.0231  0.0880  0.0366  278 VAL A O     
2293 C  CB    . VAL A 278 ? 0.9115 0.9285 0.7994 0.0110  0.0887  0.0363  278 VAL A CB    
2294 C  CG1   . VAL A 278 ? 0.9966 1.0017 0.8614 0.0140  0.0809  0.0243  278 VAL A CG1   
2295 C  CG2   . VAL A 278 ? 0.9848 1.0094 0.9019 0.0013  0.0792  0.0349  278 VAL A CG2   
2296 N  N     . TYR A 279 ? 1.0386 1.0389 0.8637 0.0310  0.1143  0.0487  279 TYR A N     
2297 C  CA    . TYR A 279 ? 1.0634 1.0490 0.8483 0.0415  0.1217  0.0461  279 TYR A CA    
2298 C  C     . TYR A 279 ? 1.1088 1.0827 0.8631 0.0423  0.1185  0.0510  279 TYR A C     
2299 O  O     . TYR A 279 ? 1.1811 1.1376 0.9005 0.0444  0.1096  0.0427  279 TYR A O     
2300 C  CB    . TYR A 279 ? 1.0915 1.0854 0.8816 0.0509  0.1425  0.0541  279 TYR A CB    
2301 C  CG    . TYR A 279 ? 1.0557 1.0329 0.8022 0.0634  0.1527  0.0509  279 TYR A CG    
2302 C  CD1   . TYR A 279 ? 1.0594 1.0203 0.7814 0.0673  0.1463  0.0361  279 TYR A CD1   
2303 C  CD2   . TYR A 279 ? 1.1480 1.1245 0.8766 0.0716  0.1687  0.0627  279 TYR A CD2   
2304 C  CE1   . TYR A 279 ? 1.1200 1.0624 0.7995 0.0790  0.1552  0.0316  279 TYR A CE1   
2305 C  CE2   . TYR A 279 ? 1.3328 1.2919 1.0172 0.0840  0.1786  0.0589  279 TYR A CE2   
2306 C  CZ    . TYR A 279 ? 1.2891 1.2302 0.9483 0.0875  0.1714  0.0425  279 TYR A CZ    
2307 O  OH    . TYR A 279 ? 1.4007 1.3214 1.0135 0.1000  0.1809  0.0371  279 TYR A OH    
2308 N  N     . GLU A 280 ? 1.0895 1.0727 0.8574 0.0402  0.1247  0.0651  280 GLU A N     
2309 C  CA    . GLU A 280 ? 1.2514 1.2252 0.9909 0.0417  0.1229  0.0725  280 GLU A CA    
2310 C  C     . GLU A 280 ? 1.2124 1.1775 0.9450 0.0339  0.1021  0.0662  280 GLU A C     
2311 O  O     . GLU A 280 ? 1.0612 1.0133 0.7599 0.0359  0.0956  0.0668  280 GLU A O     
2312 C  CB    . GLU A 280 ? 1.2934 1.2804 1.0552 0.0407  0.1344  0.0905  280 GLU A CB    
2313 C  CG    . GLU A 280 ? 1.3690 1.3497 1.1112 0.0400  0.1305  0.1007  280 GLU A CG    
2314 C  CD    . GLU A 280 ? 1.4138 1.4078 1.1810 0.0392  0.1432  0.1197  280 GLU A CD    
2315 O  OE1   . GLU A 280 ? 1.4244 1.4303 1.2126 0.0424  0.1588  0.1262  280 GLU A OE1   
2316 O  OE2   . GLU A 280 ? 1.4708 1.4636 1.2388 0.0352  0.1373  0.1290  280 GLU A OE2   
2317 N  N     . ALA A 281 ? 1.2197 1.1918 0.9834 0.0253  0.0914  0.0604  281 ALA A N     
2318 C  CA    . ALA A 281 ? 1.1546 1.1206 0.9167 0.0183  0.0731  0.0558  281 ALA A CA    
2319 C  C     . ALA A 281 ? 1.1180 1.0702 0.8549 0.0193  0.0615  0.0421  281 ALA A C     
2320 O  O     . ALA A 281 ? 1.1304 1.0757 0.8593 0.0148  0.0463  0.0397  281 ALA A O     
2321 C  CB    . ALA A 281 ? 0.8825 0.8602 0.6858 0.0098  0.0675  0.0550  281 ALA A CB    
2322 N  N     . VAL A 282 ? 1.2487 1.1967 0.9750 0.0251  0.0681  0.0337  282 VAL A N     
2323 C  CA    . VAL A 282 ? 1.2016 1.1354 0.9067 0.0258  0.0573  0.0204  282 VAL A CA    
2324 C  C     . VAL A 282 ? 1.2342 1.1498 0.8930 0.0342  0.0609  0.0178  282 VAL A C     
2325 O  O     . VAL A 282 ? 1.3214 1.2206 0.9536 0.0331  0.0474  0.0095  282 VAL A O     
2326 C  CB    . VAL A 282 ? 1.1405 1.0799 0.8656 0.0265  0.0607  0.0119  282 VAL A CB    
2327 C  CG1   . VAL A 282 ? 1.1938 1.1169 0.8971 0.0277  0.0506  -0.0010 282 VAL A CG1   
2328 C  CG2   . VAL A 282 ? 0.9441 0.8992 0.7096 0.0182  0.0555  0.0133  282 VAL A CG2   
2329 N  N     . PHE A 283 ? 1.2277 1.1455 0.8763 0.0425  0.0790  0.0252  283 PHE A N     
2330 C  CA    . PHE A 283 ? 1.3770 1.2767 0.9792 0.0526  0.0859  0.0220  283 PHE A CA    
2331 C  C     . PHE A 283 ? 1.4367 1.3345 1.0154 0.0563  0.0919  0.0346  283 PHE A C     
2332 O  O     . PHE A 283 ? 1.3334 1.2147 0.8681 0.0651  0.0974  0.0323  283 PHE A O     
2333 C  CB    . PHE A 283 ? 1.3555 1.2568 0.9593 0.0626  0.1048  0.0193  283 PHE A CB    
2334 C  CG    . PHE A 283 ? 1.3005 1.1984 0.9162 0.0613  0.0988  0.0060  283 PHE A CG    
2335 C  CD1   . PHE A 283 ? 1.2731 1.1480 0.8552 0.0640  0.0898  -0.0077 283 PHE A CD1   
2336 C  CD2   . PHE A 283 ? 1.2469 1.1638 0.9070 0.0570  0.1013  0.0075  283 PHE A CD2   
2337 C  CE1   . PHE A 283 ? 1.2053 1.0767 0.7998 0.0628  0.0844  -0.0187 283 PHE A CE1   
2338 C  CE2   . PHE A 283 ? 1.2055 1.1197 0.8760 0.0561  0.0958  -0.0033 283 PHE A CE2   
2339 C  CZ    . PHE A 283 ? 1.1921 1.0838 0.8308 0.0592  0.0879  -0.0159 283 PHE A CZ    
2340 N  N     . GLY A 284 ? 1.5573 1.4701 1.1623 0.0503  0.0914  0.0477  284 GLY A N     
2341 C  CA    . GLY A 284 ? 1.4497 1.3627 1.0372 0.0531  0.0969  0.0621  284 GLY A CA    
2342 C  C     . GLY A 284 ? 1.4210 1.3421 1.0079 0.0625  0.1213  0.0743  284 GLY A C     
2343 O  O     . GLY A 284 ? 1.5960 1.5265 1.1920 0.0621  0.1281  0.0903  284 GLY A O     
2344 N  N     . GLN A 285 ? 1.3418 1.2597 0.9200 0.0715  0.1354  0.0680  285 GLN A N     
2345 C  CA    . GLN A 285 ? 1.4770 1.4036 1.0562 0.0815  0.1602  0.0806  285 GLN A CA    
2346 C  C     . GLN A 285 ? 1.4295 1.3809 1.0667 0.0763  0.1689  0.0899  285 GLN A C     
2347 O  O     . GLN A 285 ? 1.3368 1.2946 1.0036 0.0703  0.1616  0.0808  285 GLN A O     
2348 C  CB    . GLN A 285 ? 1.4022 1.3149 0.9488 0.0946  0.1734  0.0711  285 GLN A CB    
2349 C  CG    . GLN A 285 ? 1.5303 1.4166 1.0136 0.1018  0.1689  0.0639  285 GLN A CG    
2350 C  CD    . GLN A 285 ? 1.6884 1.5740 1.1524 0.0997  0.1643  0.0770  285 GLN A CD    
2351 O  OE1   . GLN A 285 ? 1.6599 1.5558 1.1256 0.1056  0.1821  0.0939  285 GLN A OE1   
2352 N  NE2   . GLN A 285 ? 1.6182 1.4927 1.0658 0.0912  0.1404  0.0706  285 GLN A NE2   
2353 N  N     . PRO A 286 ? 1.3829 1.3482 1.0370 0.0783  0.1838  0.1083  286 PRO A N     
2354 C  CA    . PRO A 286 ? 1.3743 1.3623 1.0846 0.0719  0.1900  0.1177  286 PRO A CA    
2355 C  C     . PRO A 286 ? 1.4003 1.3978 1.1277 0.0790  0.2062  0.1169  286 PRO A C     
2356 O  O     . PRO A 286 ? 1.3295 1.3159 1.0252 0.0905  0.2160  0.1104  286 PRO A O     
2357 C  CB    . PRO A 286 ? 1.2949 1.2918 1.0125 0.0724  0.2008  0.1388  286 PRO A CB    
2358 C  CG    . PRO A 286 ? 1.3841 1.3666 1.0479 0.0853  0.2118  0.1420  286 PRO A CG    
2359 C  CD    . PRO A 286 ? 1.3585 1.3187 0.9800 0.0862  0.1953  0.1220  286 PRO A CD    
2360 N  N     . LYS A 287 ? 1.2252 1.2430 1.0044 0.0720  0.2087  0.1238  287 LYS A N     
2361 C  CA    . LYS A 287 ? 1.2213 1.2517 1.0262 0.0766  0.2210  0.1241  287 LYS A CA    
2362 C  C     . LYS A 287 ? 1.1787 1.2325 1.0336 0.0717  0.2310  0.1422  287 LYS A C     
2363 O  O     . LYS A 287 ? 1.1785 1.2396 1.0635 0.0593  0.2191  0.1451  287 LYS A O     
2364 C  CB    . LYS A 287 ? 1.2009 1.2296 1.0187 0.0705  0.2053  0.1067  287 LYS A CB    
2365 C  CG    . LYS A 287 ? 1.2218 1.2620 1.0625 0.0760  0.2161  0.1060  287 LYS A CG    
2366 C  CD    . LYS A 287 ? 0.9982 1.0466 0.8721 0.0652  0.1998  0.0963  287 LYS A CD    
2367 C  CE    . LYS A 287 ? 1.0795 1.1398 0.9763 0.0708  0.2092  0.0964  287 LYS A CE    
2368 N  NZ    . LYS A 287 ? 1.1391 1.2240 1.0836 0.0673  0.2185  0.1127  287 LYS A NZ    
2369 N  N     . GLU A 288 ? 1.1978 1.2629 1.0623 0.0817  0.2530  0.1544  288 GLU A N     
2370 C  CA    . GLU A 288 ? 1.0732 1.1612 0.9863 0.0774  0.2637  0.1740  288 GLU A CA    
2371 C  C     . GLU A 288 ? 1.0385 1.1423 1.0018 0.0667  0.2533  0.1699  288 GLU A C     
2372 O  O     . GLU A 288 ? 1.1709 1.2731 1.1333 0.0685  0.2481  0.1566  288 GLU A O     
2373 C  CB    . GLU A 288 ? 1.0895 1.1860 0.9991 0.0922  0.2916  0.1896  288 GLU A CB    
2374 C  CG    . GLU A 288 ? 1.2501 1.3433 1.1367 0.0984  0.3053  0.2061  288 GLU A CG    
2375 C  CD    . GLU A 288 ? 1.5315 1.6209 1.3854 0.1174  0.3313  0.2132  288 GLU A CD    
2376 O  OE1   . GLU A 288 ? 1.6021 1.6704 1.3989 0.1264  0.3331  0.2070  288 GLU A OE1   
2377 O  OE2   . GLU A 288 ? 1.5237 1.6310 1.4088 0.1237  0.3497  0.2252  288 GLU A OE2   
2378 N  N     . LYS A 289 ? 0.9179 1.0366 0.9249 0.0554  0.2498  0.1817  289 LYS A N     
2379 C  CA    . LYS A 289 ? 1.0089 1.1428 1.0645 0.0440  0.2389  0.1793  289 LYS A CA    
2380 C  C     . LYS A 289 ? 1.0751 1.2323 1.1763 0.0441  0.2546  0.2005  289 LYS A C     
2381 O  O     . LYS A 289 ? 1.1793 1.3421 1.2960 0.0411  0.2615  0.2170  289 LYS A O     
2382 C  CB    . LYS A 289 ? 0.9387 1.0674 1.0082 0.0287  0.2175  0.1722  289 LYS A CB    
2383 C  CG    . LYS A 289 ? 0.8111 0.9557 0.9333 0.0158  0.2078  0.1741  289 LYS A CG    
2384 C  CD    . LYS A 289 ? 0.8729 1.0242 1.0048 0.0164  0.2020  0.1628  289 LYS A CD    
2385 C  CE    . LYS A 289 ? 0.9201 1.0695 1.0692 0.0028  0.1792  0.1489  289 LYS A CE    
2386 N  NZ    . LYS A 289 ? 0.7584 0.9227 0.9364 0.0002  0.1747  0.1460  289 LYS A NZ    
2387 N  N     . VAL A 290 ? 0.9195 1.0907 1.0440 0.0476  0.2601  0.2012  290 VAL A N     
2388 C  CA    . VAL A 290 ? 0.9782 1.1747 1.1557 0.0451  0.2708  0.2205  290 VAL A CA    
2389 C  C     . VAL A 290 ? 0.9409 1.1472 1.1608 0.0287  0.2494  0.2140  290 VAL A C     
2390 O  O     . VAL A 290 ? 0.9629 1.1639 1.1745 0.0264  0.2351  0.1966  290 VAL A O     
2391 C  CB    . VAL A 290 ? 0.9425 1.1497 1.1211 0.0604  0.2918  0.2278  290 VAL A CB    
2392 C  CG1   . VAL A 290 ? 0.9737 1.2094 1.2115 0.0576  0.3030  0.2503  290 VAL A CG1   
2393 C  CG2   . VAL A 290 ? 0.9970 1.1900 1.1253 0.0776  0.3123  0.2310  290 VAL A CG2   
2394 N  N     . TYR A 291 ? 0.9057 1.1252 1.1696 0.0172  0.2466  0.2280  291 TYR A N     
2395 C  CA    . TYR A 291 ? 0.8701 1.0942 1.1687 0.0002  0.2240  0.2203  291 TYR A CA    
2396 C  C     . TYR A 291 ? 0.8771 1.1251 1.2229 -0.0029 0.2241  0.2284  291 TYR A C     
2397 O  O     . TYR A 291 ? 0.9489 1.2127 1.3087 0.0075  0.2435  0.2436  291 TYR A O     
2398 C  CB    . TYR A 291 ? 0.8455 1.0668 1.1651 -0.0121 0.2176  0.2287  291 TYR A CB    
2399 C  CG    . TYR A 291 ? 0.9263 1.1247 1.2032 -0.0106 0.2140  0.2203  291 TYR A CG    
2400 C  CD1   . TYR A 291 ? 0.9254 1.1185 1.1747 0.0005  0.2320  0.2320  291 TYR A CD1   
2401 C  CD2   . TYR A 291 ? 0.9104 1.0927 1.1740 -0.0196 0.1928  0.2014  291 TYR A CD2   
2402 C  CE1   . TYR A 291 ? 0.9871 1.1603 1.1984 0.0016  0.2272  0.2255  291 TYR A CE1   
2403 C  CE2   . TYR A 291 ? 0.9938 1.1568 1.2218 -0.0180 0.1893  0.1953  291 TYR A CE2   
2404 C  CZ    . TYR A 291 ? 1.1240 1.2829 1.3267 -0.0078 0.2057  0.2075  291 TYR A CZ    
2405 O  OH    . TYR A 291 ? 1.1408 1.2815 1.3092 -0.0066 0.2008  0.2025  291 TYR A OH    
2406 N  N     . ALA A 292 ? 0.8056 1.0562 1.1758 -0.0171 0.2017  0.2181  292 ALA A N     
2407 C  CA    . ALA A 292 ? 0.8494 1.1223 1.2638 -0.0218 0.1970  0.2240  292 ALA A CA    
2408 C  C     . ALA A 292 ? 1.0716 1.3664 1.5393 -0.0272 0.2063  0.2489  292 ALA A C     
2409 O  O     . ALA A 292 ? 0.9947 1.3123 1.4998 -0.0260 0.2111  0.2609  292 ALA A O     
2410 C  CB    . ALA A 292 ? 0.7813 1.0494 1.2038 -0.0361 0.1694  0.2063  292 ALA A CB    
2411 N  N     . GLU A 293 ? 1.0505 1.3396 1.5254 -0.0334 0.2086  0.2580  293 GLU A N     
2412 C  CA    . GLU A 293 ? 0.7998 1.1096 1.3259 -0.0379 0.2194  0.2839  293 GLU A CA    
2413 C  C     . GLU A 293 ? 0.9574 1.2807 1.4805 -0.0200 0.2497  0.3033  293 GLU A C     
2414 O  O     . GLU A 293 ? 1.0116 1.3599 1.5825 -0.0200 0.2606  0.3247  293 GLU A O     
2415 C  CB    . GLU A 293 ? 1.0093 1.3076 1.5423 -0.0483 0.2149  0.2891  293 GLU A CB    
2416 C  CG    . GLU A 293 ? 1.1625 1.4485 1.7068 -0.0666 0.1863  0.2724  293 GLU A CG    
2417 C  CD    . GLU A 293 ? 1.2228 1.4828 1.7133 -0.0644 0.1741  0.2464  293 GLU A CD    
2418 O  OE1   . GLU A 293 ? 1.3086 1.5560 1.7557 -0.0522 0.1866  0.2442  293 GLU A OE1   
2419 O  OE2   . GLU A 293 ? 1.1540 1.4062 1.6457 -0.0749 0.1519  0.2285  293 GLU A OE2   
2420 N  N     . GLU A 294 ? 0.9720 1.2792 1.4397 -0.0044 0.2634  0.2960  294 GLU A N     
2421 C  CA    . GLU A 294 ? 0.8942 1.2102 1.3511 0.0142  0.2933  0.3126  294 GLU A CA    
2422 C  C     . GLU A 294 ? 0.9527 1.2824 1.4175 0.0245  0.3007  0.3116  294 GLU A C     
2423 O  O     . GLU A 294 ? 0.9370 1.2879 1.4308 0.0336  0.3218  0.3326  294 GLU A O     
2424 C  CB    . GLU A 294 ? 0.9819 1.2735 1.3737 0.0268  0.3037  0.3042  294 GLU A CB    
2425 C  CG    . GLU A 294 ? 1.0188 1.2918 1.3939 0.0162  0.2900  0.2979  294 GLU A CG    
2426 C  CD    . GLU A 294 ? 1.0277 1.2787 1.3403 0.0287  0.2997  0.2919  294 GLU A CD    
2427 O  OE1   . GLU A 294 ? 1.0932 1.3477 1.3877 0.0443  0.3243  0.3052  294 GLU A OE1   
2428 O  OE2   . GLU A 294 ? 1.0714 1.3018 1.3527 0.0233  0.2827  0.2742  294 GLU A OE2   
2429 N  N     . ILE A 295 ? 0.9612 1.2799 1.4028 0.0237  0.2841  0.2886  295 ILE A N     
2430 C  CA    . ILE A 295 ? 0.9545 1.2827 1.3969 0.0358  0.2928  0.2871  295 ILE A CA    
2431 C  C     . ILE A 295 ? 0.9802 1.3382 1.4885 0.0272  0.2868  0.3010  295 ILE A C     
2432 O  O     . ILE A 295 ? 1.0055 1.3796 1.5304 0.0384  0.3002  0.3096  295 ILE A O     
2433 C  CB    . ILE A 295 ? 1.0710 1.3772 1.4661 0.0387  0.2785  0.2596  295 ILE A CB    
2434 C  CG1   . ILE A 295 ? 1.1010 1.3974 1.4973 0.0207  0.2474  0.2412  295 ILE A CG1   
2435 C  CG2   . ILE A 295 ? 1.1307 1.4109 1.4630 0.0509  0.2895  0.2501  295 ILE A CG2   
2436 C  CD1   . ILE A 295 ? 0.9928 1.3099 1.4436 0.0059  0.2298  0.2454  295 ILE A CD1   
2437 N  N     . THR A 296 ? 1.0081 1.3733 1.5548 0.0075  0.2666  0.3035  296 THR A N     
2438 C  CA    . THR A 296 ? 0.8824 1.2761 1.4940 -0.0026 0.2586  0.3179  296 THR A CA    
2439 C  C     . THR A 296 ? 0.8987 1.3161 1.5541 0.0018  0.2820  0.3489  296 THR A C     
2440 O  O     . THR A 296 ? 1.0538 1.4972 1.7503 0.0069  0.2920  0.3655  296 THR A O     
2441 C  CB    . THR A 296 ? 0.8631 1.2529 1.4969 -0.0256 0.2273  0.3078  296 THR A CB    
2442 O  OG1   . THR A 296 ? 1.0052 1.3837 1.6149 -0.0291 0.2061  0.2838  296 THR A OG1   
2443 C  CG2   . THR A 296 ? 0.8690 1.2874 1.5745 -0.0387 0.2208  0.3284  296 THR A CG2   
2444 N  N     . THR A 297 ? 0.9009 1.3106 1.5495 0.0004  0.2916  0.3583  297 THR A N     
2445 C  CA    . THR A 297 ? 0.8658 1.2969 1.5516 0.0063  0.3169  0.3891  297 THR A CA    
2446 C  C     . THR A 297 ? 0.9939 1.4296 1.6553 0.0312  0.3490  0.3980  297 THR A C     
2447 O  O     . THR A 297 ? 0.9920 1.4437 1.6829 0.0393  0.3601  0.4149  297 THR A O     
2448 C  CB    . THR A 297 ? 0.9154 1.3342 1.5928 0.0003  0.3201  0.3962  297 THR A CB    
2449 O  OG1   . THR A 297 ? 0.9922 1.4159 1.7158 -0.0226 0.2962  0.3984  297 THR A OG1   
2450 C  CG2   . THR A 297 ? 0.8671 1.2950 1.5505 0.0146  0.3488  0.4213  297 THR A CG2   
2451 N  N     . ALA A 298 ? 1.1035 1.5129 1.6965 0.0445  0.3551  0.3789  298 ALA A N     
2452 C  CA    . ALA A 298 ? 1.0618 1.4703 1.6243 0.0687  0.3847  0.3839  298 ALA A CA    
2453 C  C     . ALA A 298 ? 0.9691 1.3964 1.5604 0.0756  0.3875  0.3863  298 ALA A C     
2454 O  O     . ALA A 298 ? 0.9925 1.4208 1.5759 0.0940  0.4075  0.3948  298 ALA A O     
2455 C  CB    . ALA A 298 ? 1.0215 1.3955 1.5051 0.0788  0.3845  0.3593  298 ALA A CB    
2456 N  N     . TRP A 299 ? 0.9198 1.3514 1.5331 0.0614  0.3599  0.3733  299 TRP A N     
2457 C  CA    . TRP A 299 ? 0.9617 1.4126 1.6057 0.0668  0.3602  0.3766  299 TRP A CA    
2458 C  C     . TRP A 299 ? 1.0166 1.4937 1.7249 0.0612  0.3587  0.4002  299 TRP A C     
2459 O  O     . TRP A 299 ? 0.9948 1.4796 1.7127 0.0765  0.3748  0.4122  299 TRP A O     
2460 C  CB    . TRP A 299 ? 0.9396 1.3812 1.5759 0.0539  0.3275  0.3523  299 TRP A CB    
2461 C  CG    . TRP A 299 ? 0.9881 1.4413 1.6363 0.0635  0.3294  0.3509  299 TRP A CG    
2462 C  CD1   . TRP A 299 ? 0.9900 1.4707 1.6957 0.0552  0.3168  0.3613  299 TRP A CD1   
2463 C  CD2   . TRP A 299 ? 0.9954 1.4326 1.5978 0.0835  0.3443  0.3390  299 TRP A CD2   
2464 N  NE1   . TRP A 299 ? 1.0368 1.5206 1.7361 0.0693  0.3237  0.3575  299 TRP A NE1   
2465 C  CE2   . TRP A 299 ? 1.0624 1.5188 1.6988 0.0869  0.3409  0.3435  299 TRP A CE2   
2466 C  CE3   . TRP A 299 ? 0.9326 1.3403 1.4687 0.0986  0.3592  0.3250  299 TRP A CE3   
2467 C  CZ2   . TRP A 299 ? 1.0487 1.4949 1.6559 0.1051  0.3530  0.3344  299 TRP A CZ2   
2468 C  CZ3   . TRP A 299 ? 0.9705 1.3671 1.4765 0.1159  0.3701  0.3150  299 TRP A CZ3   
2469 C  CH2   . TRP A 299 ? 0.9813 1.3967 1.5232 0.1192  0.3675  0.3197  299 TRP A CH2   
2470 N  N     . GLU A 300 ? 0.9967 1.4835 1.7463 0.0394  0.3369  0.4053  300 GLU A N     
2471 C  CA    . GLU A 300 ? 1.0348 1.5425 1.8437 0.0317  0.3290  0.4248  300 GLU A CA    
2472 C  C     . GLU A 300 ? 0.9208 1.4304 1.7344 0.0450  0.3531  0.4464  300 GLU A C     
2473 O  O     . GLU A 300 ? 0.7314 1.2589 1.5887 0.0465  0.3546  0.4647  300 GLU A O     
2474 C  CB    . GLU A 300 ? 0.9225 1.4341 1.7670 0.0051  0.2996  0.4229  300 GLU A CB    
2475 C  CG    . GLU A 300 ? 0.8857 1.3934 1.7221 -0.0086 0.2751  0.4008  300 GLU A CG    
2476 C  CD    . GLU A 300 ? 0.9627 1.4704 1.8306 -0.0346 0.2452  0.3969  300 GLU A CD    
2477 O  OE1   . GLU A 300 ? 0.9259 1.4254 1.7984 -0.0416 0.2466  0.4039  300 GLU A OE1   
2478 O  OE2   . GLU A 300 ? 0.8207 1.3352 1.7071 -0.0477 0.2199  0.3865  300 GLU A OE2   
2479 N  N     . THR A 301 ? 0.9092 1.4010 1.6786 0.0550  0.3717  0.4454  301 THR A N     
2480 C  CA    . THR A 301 ? 0.9368 1.4287 1.7030 0.0700  0.3964  0.4648  301 THR A CA    
2481 C  C     . THR A 301 ? 0.9902 1.4713 1.7100 0.0962  0.4236  0.4619  301 THR A C     
2482 O  O     . THR A 301 ? 0.9815 1.4652 1.7026 0.1111  0.4450  0.4790  301 THR A O     
2483 C  CB    . THR A 301 ? 0.8598 1.3385 1.6076 0.0642  0.3991  0.4678  301 THR A CB    
2484 O  OG1   . THR A 301 ? 0.9926 1.4492 1.6827 0.0662  0.3997  0.4471  301 THR A OG1   
2485 C  CG2   . THR A 301 ? 0.7851 1.2729 1.5830 0.0394  0.3740  0.4734  301 THR A CG2   
2486 N  N     . GLY A 302 ? 1.0244 1.4924 1.7032 0.1025  0.4231  0.4408  302 GLY A N     
2487 C  CA    . GLY A 302 ? 1.0006 1.4530 1.6292 0.1268  0.4470  0.4345  302 GLY A CA    
2488 C  C     . GLY A 302 ? 1.0843 1.5139 1.6558 0.1385  0.4653  0.4321  302 GLY A C     
2489 O  O     . GLY A 302 ? 1.0118 1.4246 1.5356 0.1588  0.4845  0.4253  302 GLY A O     
2490 N  N     . GLU A 303 ? 1.0490 1.4761 1.6226 0.1263  0.4590  0.4372  303 GLU A N     
2491 C  CA    . GLU A 303 ? 1.1354 1.5431 1.6589 0.1366  0.4752  0.4383  303 GLU A CA    
2492 C  C     . GLU A 303 ? 1.2013 1.5848 1.6660 0.1350  0.4690  0.4150  303 GLU A C     
2493 O  O     . GLU A 303 ? 1.1529 1.5377 1.6291 0.1177  0.4481  0.4040  303 GLU A O     
2494 C  CB    . GLU A 303 ? 1.1399 1.5569 1.6965 0.1248  0.4719  0.4573  303 GLU A CB    
2495 C  CG    . GLU A 303 ? 1.1267 1.5694 1.7506 0.1215  0.4722  0.4807  303 GLU A CG    
2496 C  CD    . GLU A 303 ? 1.1196 1.5677 1.7664 0.1164  0.4761  0.5013  303 GLU A CD    
2497 O  OE1   . GLU A 303 ? 1.0585 1.4927 1.6791 0.1097  0.4719  0.4965  303 GLU A OE1   
2498 O  OE2   . GLU A 303 ? 1.1601 1.6261 1.8519 0.1194  0.4832  0.5231  303 GLU A OE2   
2499 N  N     . ASN A 304 ? 1.3913 1.7519 1.7924 0.1533  0.4867  0.4075  304 ASN A N     
2500 C  CA    . ASN A 304 ? 1.3996 1.7342 1.7379 0.1542  0.4823  0.3863  304 ASN A CA    
2501 C  C     . ASN A 304 ? 1.1881 1.5205 1.5238 0.1481  0.4671  0.3660  304 ASN A C     
2502 O  O     . ASN A 304 ? 1.1789 1.4999 1.4971 0.1356  0.4487  0.3510  304 ASN A O     
2503 C  CB    . ASN A 304 ? 1.4088 1.7388 1.7430 0.1400  0.4727  0.3904  304 ASN A CB    
2504 C  CG    . ASN A 304 ? 1.6309 1.9329 1.8919 0.1512  0.4819  0.3817  304 ASN A CG    
2505 O  OD1   . ASN A 304 ? 1.4885 1.7699 1.6960 0.1623  0.4850  0.3629  304 ASN A OD1   
2506 N  ND2   . ASN A 304 ? 1.7016 2.0019 1.9595 0.1481  0.4850  0.3952  304 ASN A ND2   
2507 N  N     . LEU A 305 ? 1.2733 1.6138 1.6256 0.1569  0.4715  0.3641  305 LEU A N     
2508 C  CA    . LEU A 305 ? 1.2027 1.5406 1.5503 0.1541  0.4593  0.3453  305 LEU A CA    
2509 C  C     . LEU A 305 ? 1.1253 1.4288 1.3967 0.1673  0.4627  0.3216  305 LEU A C     
2510 O  O     . LEU A 305 ? 1.0512 1.3391 1.3032 0.1605  0.4398  0.2982  305 LEU A O     
2511 C  CB    . LEU A 305 ? 1.1139 1.4711 1.5057 0.1592  0.4613  0.3520  305 LEU A CB    
2512 C  CG    . LEU A 305 ? 1.0468 1.4222 1.4833 0.1434  0.4384  0.3463  305 LEU A CG    
2513 C  CD1   . LEU A 305 ? 0.9400 1.3166 1.3955 0.1187  0.4101  0.3428  305 LEU A CD1   
2514 C  CD2   . LEU A 305 ? 1.1069 1.5080 1.6014 0.1451  0.4396  0.3625  305 LEU A CD2   
2515 N  N     . GLU A 306 ? 1.1797 1.4658 1.4043 0.1843  0.4839  0.3241  306 GLU A N     
2516 C  CA    . GLU A 306 ? 1.1051 1.3576 1.2552 0.1965  0.4877  0.3025  306 GLU A CA    
2517 C  C     . GLU A 306 ? 1.2556 1.4874 1.3716 0.1814  0.4618  0.2853  306 GLU A C     
2518 O  O     . GLU A 306 ? 1.2639 1.4683 1.3311 0.1829  0.4488  0.2610  306 GLU A O     
2519 C  CB    . GLU A 306 ? 1.1060 1.3411 1.2135 0.2154  0.5087  0.3072  306 GLU A CB    
2520 C  CG    . GLU A 306 ? 1.3006 1.5580 1.4550 0.2220  0.5242  0.3310  306 GLU A CG    
2521 C  CD    . GLU A 306 ? 1.4569 1.6961 1.5676 0.2432  0.5467  0.3340  306 GLU A CD    
2522 O  OE1   . GLU A 306 ? 1.6011 1.8158 1.6524 0.2480  0.5488  0.3250  306 GLU A OE1   
2523 O  OE2   . GLU A 306 ? 1.2344 1.4840 1.3704 0.2550  0.5617  0.3458  306 GLU A OE2   
2524 N  N     . ARG A 307 ? 1.2983 1.5418 1.4407 0.1665  0.4531  0.2976  307 ARG A N     
2525 C  CA    . ARG A 307 ? 1.2192 1.4444 1.3361 0.1513  0.4269  0.2822  307 ARG A CA    
2526 C  C     . ARG A 307 ? 1.2492 1.4713 1.3801 0.1367  0.3970  0.2618  307 ARG A C     
2527 O  O     . ARG A 307 ? 1.2031 1.4017 1.2940 0.1315  0.3780  0.2407  307 ARG A O     
2528 C  CB    . ARG A 307 ? 1.1615 1.4013 1.3112 0.1387  0.4251  0.3015  307 ARG A CB    
2529 C  CG    . ARG A 307 ? 1.1884 1.4126 1.3224 0.1219  0.3976  0.2877  307 ARG A CG    
2530 C  CD    . ARG A 307 ? 1.1072 1.3288 1.2300 0.1206  0.4052  0.3030  307 ARG A CD    
2531 N  NE    . ARG A 307 ? 1.1782 1.3896 1.3005 0.1031  0.3789  0.2932  307 ARG A NE    
2532 C  CZ    . ARG A 307 ? 1.2193 1.4439 1.3928 0.0851  0.3612  0.2955  307 ARG A CZ    
2533 N  NH1   . ARG A 307 ? 1.2303 1.4801 1.4619 0.0804  0.3648  0.3082  307 ARG A NH1   
2534 N  NH2   . ARG A 307 ? 1.0873 1.2990 1.2535 0.0715  0.3390  0.2849  307 ARG A NH2   
2535 N  N     . VAL A 308 ? 1.2232 1.4696 1.4111 0.1301  0.3922  0.2686  308 VAL A N     
2536 C  CA    . VAL A 308 ? 1.1538 1.3985 1.3544 0.1180  0.3656  0.2504  308 VAL A CA    
2537 C  C     . VAL A 308 ? 1.1340 1.3576 1.2905 0.1302  0.3660  0.2304  308 VAL A C     
2538 O  O     . VAL A 308 ? 1.1642 1.3729 1.3022 0.1220  0.3434  0.2098  308 VAL A O     
2539 C  CB    . VAL A 308 ? 1.1369 1.4134 1.4075 0.1096  0.3617  0.2643  308 VAL A CB    
2540 C  CG1   . VAL A 308 ? 1.0231 1.2980 1.3056 0.0956  0.3324  0.2463  308 VAL A CG1   
2541 C  CG2   . VAL A 308 ? 1.0728 1.3695 1.3885 0.0985  0.3639  0.2862  308 VAL A CG2   
2542 N  N     . ALA A 309 ? 1.2351 1.4564 1.3746 0.1502  0.3921  0.2362  309 ALA A N     
2543 C  CA    . ALA A 309 ? 1.2201 1.4197 1.3194 0.1627  0.3937  0.2175  309 ALA A CA    
2544 C  C     . ALA A 309 ? 1.1780 1.3434 1.2112 0.1629  0.3832  0.1970  309 ALA A C     
2545 O  O     . ALA A 309 ? 1.1296 1.2765 1.1381 0.1614  0.3677  0.1764  309 ALA A O     
2546 C  CB    . ALA A 309 ? 1.2542 1.4576 1.3497 0.1852  0.4262  0.2291  309 ALA A CB    
2547 N  N     . ARG A 310 ? 1.1650 1.3220 1.1703 0.1647  0.3912  0.2035  310 ARG A N     
2548 C  CA    . ARG A 310 ? 1.2194 1.3457 1.1648 0.1635  0.3790  0.1859  310 ARG A CA    
2549 C  C     . ARG A 310 ? 1.2215 1.3441 1.1758 0.1438  0.3468  0.1716  310 ARG A C     
2550 O  O     . ARG A 310 ? 1.2406 1.3412 1.1606 0.1425  0.3315  0.1511  310 ARG A O     
2551 C  CB    . ARG A 310 ? 1.2519 1.3740 1.1722 0.1676  0.3922  0.1988  310 ARG A CB    
2552 C  CG    . ARG A 310 ? 1.4190 1.5095 1.2743 0.1683  0.3813  0.1825  310 ARG A CG    
2553 C  CD    . ARG A 310 ? 1.5589 1.6504 1.4026 0.1650  0.3849  0.1964  310 ARG A CD    
2554 N  NE    . ARG A 310 ? 1.6638 1.7768 1.5602 0.1470  0.3714  0.2073  310 ARG A NE    
2555 C  CZ    . ARG A 310 ? 1.6373 1.7699 1.5654 0.1451  0.3843  0.2306  310 ARG A CZ    
2556 N  NH1   . ARG A 310 ? 1.4757 1.6115 1.3894 0.1604  0.4120  0.2473  310 ARG A NH1   
2557 N  NH2   . ARG A 310 ? 1.4556 1.6040 1.4307 0.1276  0.3692  0.2375  310 ARG A NH2   
2558 N  N     . TYR A 311 ? 1.2237 1.3673 1.2248 0.1284  0.3364  0.1824  311 TYR A N     
2559 C  CA    . TYR A 311 ? 1.1503 1.2913 1.1624 0.1104  0.3075  0.1696  311 TYR A CA    
2560 C  C     . TYR A 311 ? 1.0822 1.2219 1.1026 0.1084  0.2943  0.1544  311 TYR A C     
2561 O  O     . TYR A 311 ? 1.0478 1.1712 1.0459 0.1016  0.2746  0.1365  311 TYR A O     
2562 C  CB    . TYR A 311 ? 1.0565 1.2204 1.1211 0.0956  0.3011  0.1845  311 TYR A CB    
2563 C  CG    . TYR A 311 ? 0.9468 1.1085 1.0252 0.0776  0.2729  0.1721  311 TYR A CG    
2564 C  CD1   . TYR A 311 ? 0.8482 1.0297 0.9775 0.0657  0.2615  0.1755  311 TYR A CD1   
2565 C  CD2   . TYR A 311 ? 1.1463 1.2861 1.1866 0.0729  0.2579  0.1576  311 TYR A CD2   
2566 C  CE1   . TYR A 311 ? 0.8831 1.0610 1.0216 0.0504  0.2370  0.1635  311 TYR A CE1   
2567 C  CE2   . TYR A 311 ? 1.0654 1.2033 1.1184 0.0579  0.2343  0.1469  311 TYR A CE2   
2568 C  CZ    . TYR A 311 ? 1.0072 1.1633 1.1075 0.0471  0.2245  0.1494  311 TYR A CZ    
2569 O  OH    . TYR A 311 ? 1.0679 1.2201 1.1769 0.0333  0.2022  0.1381  311 TYR A OH    
2570 N  N     . SER A 312 ? 1.1307 1.2885 1.1850 0.1145  0.3052  0.1627  312 SER A N     
2571 C  CA    . SER A 312 ? 1.1221 1.2799 1.1858 0.1138  0.2942  0.1505  312 SER A CA    
2572 C  C     . SER A 312 ? 1.0611 1.1895 1.0708 0.1239  0.2935  0.1316  312 SER A C     
2573 O  O     . SER A 312 ? 0.9095 1.0267 0.9085 0.1169  0.2737  0.1153  312 SER A O     
2574 C  CB    . SER A 312 ? 1.1181 1.3004 1.2256 0.1214  0.3094  0.1653  312 SER A CB    
2575 O  OG    . SER A 312 ? 1.0451 1.2324 1.1712 0.1179  0.2958  0.1565  312 SER A OG    
2576 N  N     . MET A 313 ? 1.1799 1.2947 1.1545 0.1406  0.3150  0.1337  313 MET A N     
2577 C  CA    . MET A 313 ? 1.1197 1.2035 1.0403 0.1501  0.3140  0.1151  313 MET A CA    
2578 C  C     . MET A 313 ? 1.1272 1.1904 1.0119 0.1395  0.2932  0.1013  313 MET A C     
2579 O  O     . MET A 313 ? 1.1602 1.2040 1.0199 0.1375  0.2783  0.0835  313 MET A O     
2580 C  CB    . MET A 313 ? 1.0943 1.1663 0.9817 0.1703  0.3419  0.1205  313 MET A CB    
2581 C  CG    . MET A 313 ? 1.1533 1.1888 0.9770 0.1800  0.3410  0.1011  313 MET A CG    
2582 S  SD    . MET A 313 ? 1.3132 1.3259 1.0819 0.1761  0.3332  0.0956  313 MET A SD    
2583 C  CE    . MET A 313 ? 1.4334 1.4055 1.1323 0.1927  0.3398  0.0761  313 MET A CE    
2584 N  N     . GLU A 314 ? 1.1543 1.2220 1.0383 0.1326  0.2919  0.1103  314 GLU A N     
2585 C  CA    . GLU A 314 ? 1.1182 1.1686 0.9718 0.1227  0.2727  0.0995  314 GLU A CA    
2586 C  C     . GLU A 314 ? 1.0857 1.1390 0.9604 0.1076  0.2472  0.0882  314 GLU A C     
2587 O  O     . GLU A 314 ? 1.0482 1.0819 0.8933 0.1039  0.2314  0.0727  314 GLU A O     
2588 C  CB    . GLU A 314 ? 1.0848 1.1431 0.9427 0.1178  0.2766  0.1140  314 GLU A CB    
2589 C  CG    . GLU A 314 ? 1.1646 1.2128 0.9850 0.1325  0.2985  0.1225  314 GLU A CG    
2590 C  CD    . GLU A 314 ? 1.4494 1.4875 1.2423 0.1273  0.2916  0.1253  314 GLU A CD    
2591 O  OE1   . GLU A 314 ? 1.4152 1.4635 1.2354 0.1127  0.2767  0.1291  314 GLU A OE1   
2592 O  OE2   . GLU A 314 ? 1.6130 1.6324 1.3564 0.1382  0.3010  0.1239  314 GLU A OE2   
2593 N  N     . ASP A 315 ? 1.0868 1.1644 1.0125 0.0988  0.2428  0.0961  315 ASP A N     
2594 C  CA    . ASP A 315 ? 0.9376 1.0187 0.8828 0.0853  0.2200  0.0859  315 ASP A CA    
2595 C  C     . ASP A 315 ? 1.0820 1.1481 1.0070 0.0899  0.2129  0.0700  315 ASP A C     
2596 O  O     . ASP A 315 ? 0.9907 1.0431 0.8981 0.0829  0.1952  0.0569  315 ASP A O     
2597 C  CB    . ASP A 315 ? 0.8726 0.9815 0.8733 0.0774  0.2184  0.0969  315 ASP A CB    
2598 C  CG    . ASP A 315 ? 0.9424 1.0606 0.9655 0.0634  0.2083  0.1034  315 ASP A CG    
2599 O  OD1   . ASP A 315 ? 1.0707 1.1801 1.0735 0.0634  0.2119  0.1073  315 ASP A OD1   
2600 O  OD2   . ASP A 315 ? 0.9433 1.0767 1.0035 0.0524  0.1966  0.1046  315 ASP A OD2   
2601 N  N     . ALA A 316 ? 1.1369 1.2053 1.0658 0.1020  0.2273  0.0719  316 ALA A N     
2602 C  CA    . ALA A 316 ? 1.0492 1.1024 0.9608 0.1071  0.2218  0.0578  316 ALA A CA    
2603 C  C     . ALA A 316 ? 1.0660 1.0879 0.9231 0.1118  0.2184  0.0441  316 ALA A C     
2604 O  O     . ALA A 316 ? 0.9956 1.0030 0.8379 0.1072  0.2023  0.0302  316 ALA A O     
2605 C  CB    . ALA A 316 ? 0.8770 0.9379 0.8038 0.1209  0.2402  0.0641  316 ALA A CB    
2606 N  N     . LYS A 317 ? 1.0787 1.0901 0.9055 0.1207  0.2329  0.0483  317 LYS A N     
2607 C  CA    . LYS A 317 ? 1.1462 1.1270 0.9184 0.1254  0.2292  0.0354  317 LYS A CA    
2608 C  C     . LYS A 317 ? 1.1758 1.1488 0.9375 0.1110  0.2054  0.0275  317 LYS A C     
2609 O  O     . LYS A 317 ? 1.0980 1.0494 0.8310 0.1097  0.1923  0.0131  317 LYS A O     
2610 C  CB    . LYS A 317 ? 1.0919 1.0650 0.8336 0.1372  0.2492  0.0434  317 LYS A CB    
2611 C  CG    . LYS A 317 ? 1.3560 1.2959 1.0370 0.1429  0.2453  0.0301  317 LYS A CG    
2612 C  CD    . LYS A 317 ? 1.3848 1.3147 1.0322 0.1597  0.2700  0.0362  317 LYS A CD    
2613 C  CE    . LYS A 317 ? 1.4243 1.3354 1.0236 0.1589  0.2645  0.0339  317 LYS A CE    
2614 N  NZ    . LYS A 317 ? 1.3153 1.1914 0.8553 0.1702  0.2663  0.0182  317 LYS A NZ    
2615 N  N     . VAL A 318 ? 1.1295 1.1197 0.9159 0.1002  0.1996  0.0371  318 VAL A N     
2616 C  CA    . VAL A 318 ? 1.0100 0.9927 0.7857 0.0882  0.1795  0.0313  318 VAL A CA    
2617 C  C     . VAL A 318 ? 1.0762 1.0617 0.8720 0.0781  0.1606  0.0217  318 VAL A C     
2618 O  O     . VAL A 318 ? 1.0835 1.0546 0.8600 0.0723  0.1444  0.0116  318 VAL A O     
2619 C  CB    . VAL A 318 ? 0.9978 0.9953 0.7915 0.0811  0.1809  0.0450  318 VAL A CB    
2620 C  CG1   . VAL A 318 ? 0.8913 0.8849 0.6613 0.0917  0.1998  0.0555  318 VAL A CG1   
2621 C  CG2   . VAL A 318 ? 1.0833 1.1072 0.9297 0.0740  0.1817  0.0542  318 VAL A CG2   
2622 N  N     . THR A 319 ? 0.9989 1.0036 0.8339 0.0758  0.1620  0.0253  319 THR A N     
2623 C  CA    . THR A 319 ? 0.9913 0.9989 0.8432 0.0672  0.1451  0.0169  319 THR A CA    
2624 C  C     . THR A 319 ? 1.0471 1.0346 0.8735 0.0727  0.1405  0.0040  319 THR A C     
2625 O  O     . THR A 319 ? 1.0214 1.0015 0.8440 0.0655  0.1241  -0.0049 319 THR A O     
2626 C  CB    . THR A 319 ? 0.7792 0.8111 0.6756 0.0641  0.1471  0.0240  319 THR A CB    
2627 O  OG1   . THR A 319 ? 1.0873 1.1223 0.9886 0.0759  0.1624  0.0273  319 THR A OG1   
2628 C  CG2   . THR A 319 ? 0.8730 0.9233 0.7968 0.0573  0.1500  0.0364  319 THR A CG2   
2629 N  N     . TYR A 320 ? 1.0817 1.0596 0.8914 0.0858  0.1555  0.0031  320 TYR A N     
2630 C  CA    . TYR A 320 ? 1.0013 0.9553 0.7825 0.0915  0.1515  -0.0100 320 TYR A CA    
2631 C  C     . TYR A 320 ? 1.0808 1.0117 0.8227 0.0880  0.1396  -0.0189 320 TYR A C     
2632 O  O     . TYR A 320 ? 1.0745 0.9931 0.8081 0.0823  0.1235  -0.0289 320 TYR A O     
2633 C  CB    . TYR A 320 ? 0.9581 0.9037 0.7261 0.1076  0.1718  -0.0093 320 TYR A CB    
2634 C  CG    . TYR A 320 ? 1.1080 1.0251 0.8441 0.1138  0.1679  -0.0238 320 TYR A CG    
2635 C  CD1   . TYR A 320 ? 1.0522 0.9682 0.8043 0.1104  0.1571  -0.0303 320 TYR A CD1   
2636 C  CD2   . TYR A 320 ? 1.1030 0.9933 0.7921 0.1227  0.1742  -0.0310 320 TYR A CD2   
2637 C  CE1   . TYR A 320 ? 1.1807 1.0695 0.9061 0.1154  0.1528  -0.0432 320 TYR A CE1   
2638 C  CE2   . TYR A 320 ? 1.0803 0.9419 0.7398 0.1277  0.1691  -0.0454 320 TYR A CE2   
2639 C  CZ    . TYR A 320 ? 1.2676 1.1286 0.9470 0.1237  0.1585  -0.0513 320 TYR A CZ    
2640 O  OH    . TYR A 320 ? 1.3650 1.1963 1.0173 0.1280  0.1530  -0.0651 320 TYR A OH    
2641 N  N     . GLU A 321 ? 1.1657 1.0913 0.8840 0.0912  0.1469  -0.0142 321 GLU A N     
2642 C  CA    . GLU A 321 ? 1.1009 1.0063 0.7823 0.0874  0.1345  -0.0208 321 GLU A CA    
2643 C  C     . GLU A 321 ? 1.1279 1.0405 0.8270 0.0727  0.1138  -0.0221 321 GLU A C     
2644 O  O     . GLU A 321 ? 1.1796 1.0755 0.8579 0.0679  0.0981  -0.0309 321 GLU A O     
2645 C  CB    . GLU A 321 ? 1.1067 1.0107 0.7660 0.0924  0.1462  -0.0120 321 GLU A CB    
2646 C  CG    . GLU A 321 ? 1.3657 1.2404 0.9703 0.1009  0.1477  -0.0205 321 GLU A CG    
2647 C  CD    . GLU A 321 ? 1.6830 1.5440 1.2696 0.1158  0.1646  -0.0261 321 GLU A CD    
2648 O  OE1   . GLU A 321 ? 1.5720 1.4080 1.1310 0.1185  0.1568  -0.0405 321 GLU A OE1   
2649 O  OE2   . GLU A 321 ? 1.6509 1.5260 1.2526 0.1250  0.1858  -0.0158 321 GLU A OE2   
2650 N  N     . LEU A 322 ? 1.0923 1.0291 0.8303 0.0655  0.1134  -0.0132 322 LEU A N     
2651 C  CA    . LEU A 322 ? 1.1186 1.0623 0.8745 0.0529  0.0958  -0.0144 322 LEU A CA    
2652 C  C     . LEU A 322 ? 1.1196 1.0614 0.8873 0.0496  0.0851  -0.0232 322 LEU A C     
2653 O  O     . LEU A 322 ? 1.0717 1.0080 0.8375 0.0420  0.0693  -0.0282 322 LEU A O     
2654 C  CB    . LEU A 322 ? 0.8881 0.8554 0.6795 0.0467  0.0990  -0.0035 322 LEU A CB    
2655 C  CG    . LEU A 322 ? 0.9558 0.9257 0.7408 0.0457  0.1039  0.0062  322 LEU A CG    
2656 C  CD1   . LEU A 322 ? 0.9961 0.9881 0.8165 0.0439  0.1141  0.0180  322 LEU A CD1   
2657 C  CD2   . LEU A 322 ? 0.9133 0.8781 0.6930 0.0366  0.0877  0.0046  322 LEU A CD2   
2658 N  N     . GLY A 323 ? 1.1478 1.0951 0.9294 0.0557  0.0939  -0.0237 323 GLY A N     
2659 C  CA    . GLY A 323 ? 0.9782 0.9246 0.7721 0.0532  0.0846  -0.0304 323 GLY A CA    
2660 C  C     . GLY A 323 ? 0.9633 0.8843 0.7274 0.0544  0.0752  -0.0413 323 GLY A C     
2661 O  O     . GLY A 323 ? 0.8893 0.8078 0.6600 0.0475  0.0610  -0.0459 323 GLY A O     
2662 N  N     . LYS A 324 ? 1.0795 0.9808 0.8101 0.0633  0.0829  -0.0456 324 LYS A N     
2663 C  CA    . LYS A 324 ? 1.1005 0.9745 0.7994 0.0637  0.0723  -0.0569 324 LYS A CA    
2664 C  C     . LYS A 324 ? 1.1196 0.9896 0.8112 0.0527  0.0541  -0.0581 324 LYS A C     
2665 O  O     . LYS A 324 ? 0.9896 0.8432 0.6692 0.0486  0.0399  -0.0660 324 LYS A O     
2666 C  CB    . LYS A 324 ? 1.1698 1.0223 0.8295 0.0753  0.0842  -0.0614 324 LYS A CB    
2667 C  CG    . LYS A 324 ? 1.1320 0.9865 0.7974 0.0882  0.1041  -0.0599 324 LYS A CG    
2668 C  CD    . LYS A 324 ? 1.2223 1.0456 0.8447 0.0996  0.1108  -0.0704 324 LYS A CD    
2669 C  CE    . LYS A 324 ? 1.3910 1.1989 0.9722 0.1004  0.1094  -0.0719 324 LYS A CE    
2670 N  NZ    . LYS A 324 ? 1.4006 1.1868 0.9431 0.1158  0.1266  -0.0768 324 LYS A NZ    
2671 N  N     . GLU A 325 ? 1.0918 0.9766 0.7926 0.0477  0.0541  -0.0495 325 GLU A N     
2672 C  CA    . GLU A 325 ? 1.0660 0.9486 0.7621 0.0382  0.0381  -0.0487 325 GLU A CA    
2673 C  C     . GLU A 325 ? 1.0674 0.9634 0.7956 0.0289  0.0264  -0.0478 325 GLU A C     
2674 O  O     . GLU A 325 ? 1.2111 1.0978 0.9355 0.0231  0.0115  -0.0523 325 GLU A O     
2675 C  CB    . GLU A 325 ? 1.1181 1.0104 0.8123 0.0375  0.0439  -0.0391 325 GLU A CB    
2676 C  CG    . GLU A 325 ? 1.1623 1.0567 0.8590 0.0279  0.0288  -0.0357 325 GLU A CG    
2677 C  CD    . GLU A 325 ? 1.3223 1.1984 0.9808 0.0291  0.0227  -0.0368 325 GLU A CD    
2678 O  OE1   . GLU A 325 ? 1.1180 0.9776 0.7446 0.0375  0.0300  -0.0417 325 GLU A OE1   
2679 O  OE2   . GLU A 325 ? 1.3430 1.2210 1.0029 0.0220  0.0105  -0.0324 325 GLU A OE2   
2680 N  N     . PHE A 326 ? 0.9983 0.9160 0.7581 0.0273  0.0330  -0.0417 326 PHE A N     
2681 C  CA    . PHE A 326 ? 0.9960 0.9273 0.7835 0.0190  0.0235  -0.0399 326 PHE A CA    
2682 C  C     . PHE A 326 ? 1.1220 1.0542 0.9232 0.0191  0.0201  -0.0444 326 PHE A C     
2683 O  O     . PHE A 326 ? 1.2049 1.1448 1.0238 0.0127  0.0111  -0.0437 326 PHE A O     
2684 C  CB    . PHE A 326 ? 0.8259 0.7781 0.6388 0.0166  0.0304  -0.0320 326 PHE A CB    
2685 C  CG    . PHE A 326 ? 0.9353 0.8885 0.7416 0.0142  0.0310  -0.0259 326 PHE A CG    
2686 C  CD1   . PHE A 326 ? 1.0283 0.9787 0.8195 0.0201  0.0425  -0.0217 326 PHE A CD1   
2687 C  CD2   . PHE A 326 ? 1.0008 0.9578 0.8165 0.0068  0.0209  -0.0234 326 PHE A CD2   
2688 C  CE1   . PHE A 326 ? 0.9974 0.9489 0.7829 0.0181  0.0432  -0.0147 326 PHE A CE1   
2689 C  CE2   . PHE A 326 ? 0.9055 0.8633 0.7167 0.0050  0.0214  -0.0168 326 PHE A CE2   
2690 C  CZ    . PHE A 326 ? 0.9837 0.9388 0.7798 0.0103  0.0322  -0.0122 326 PHE A CZ    
2691 N  N     . LEU A 327 ? 1.0390 0.9632 0.8324 0.0267  0.0277  -0.0484 327 LEU A N     
2692 C  CA    . LEU A 327 ? 1.0671 0.9923 0.8750 0.0270  0.0245  -0.0513 327 LEU A CA    
2693 C  C     . LEU A 327 ? 1.0551 0.9647 0.8538 0.0225  0.0100  -0.0569 327 LEU A C     
2694 O  O     . LEU A 327 ? 1.0983 1.0162 0.9170 0.0176  0.0028  -0.0553 327 LEU A O     
2695 C  CB    . LEU A 327 ? 1.1011 1.0221 0.9059 0.0371  0.0372  -0.0530 327 LEU A CB    
2696 C  CG    . LEU A 327 ? 1.1549 1.0829 0.9817 0.0373  0.0349  -0.0530 327 LEU A CG    
2697 C  CD1   . LEU A 327 ? 0.9785 0.9296 0.8320 0.0397  0.0446  -0.0457 327 LEU A CD1   
2698 C  CD2   . LEU A 327 ? 1.0580 0.9649 0.8705 0.0436  0.0354  -0.0599 327 LEU A CD2   
2699 N  N     . PRO A 328 ? 1.0177 0.9048 0.7874 0.0236  0.0048  -0.0629 328 PRO A N     
2700 C  CA    . PRO A 328 ? 1.1614 1.0338 0.9266 0.0183  -0.0104 -0.0677 328 PRO A CA    
2701 C  C     . PRO A 328 ? 1.1661 1.0507 0.9503 0.0085  -0.0224 -0.0623 328 PRO A C     
2702 O  O     . PRO A 328 ? 1.1808 1.0631 0.9768 0.0041  -0.0320 -0.0627 328 PRO A O     
2703 C  CB    . PRO A 328 ? 1.2230 1.0699 0.9508 0.0205  -0.0146 -0.0747 328 PRO A CB    
2704 C  CG    . PRO A 328 ? 1.3734 1.2260 1.0883 0.0250  -0.0032 -0.0711 328 PRO A CG    
2705 C  CD    . PRO A 328 ? 1.2053 1.0781 0.9441 0.0299  0.0120  -0.0657 328 PRO A CD    
2706 N  N     . MET A 329 ? 1.1767 1.0738 0.9652 0.0054  -0.0215 -0.0566 329 MET A N     
2707 C  CA    . MET A 329 ? 1.0758 0.9858 0.8850 -0.0024 -0.0303 -0.0509 329 MET A CA    
2708 C  C     . MET A 329 ? 1.0646 0.9926 0.9018 -0.0028 -0.0259 -0.0477 329 MET A C     
2709 O  O     . MET A 329 ? 1.0160 0.9487 0.8688 -0.0073 -0.0335 -0.0453 329 MET A O     
2710 C  CB    . MET A 329 ? 1.1829 1.1005 0.9903 -0.0047 -0.0292 -0.0456 329 MET A CB    
2711 C  CG    . MET A 329 ? 1.3595 1.2926 1.1914 -0.0107 -0.0339 -0.0392 329 MET A CG    
2712 S  SD    . MET A 329 ? 1.6997 1.6313 1.5257 -0.0156 -0.0427 -0.0335 329 MET A SD    
2713 C  CE    . MET A 329 ? 0.9223 0.8750 0.7768 -0.0176 -0.0365 -0.0268 329 MET A CE    
2714 N  N     . GLU A 330 ? 1.1361 1.0746 0.9801 0.0020  -0.0138 -0.0468 330 GLU A N     
2715 C  CA    . GLU A 330 ? 0.8199 0.7749 0.6876 0.0018  -0.0106 -0.0440 330 GLU A CA    
2716 C  C     . GLU A 330 ? 0.8079 0.7574 0.6805 0.0030  -0.0144 -0.0460 330 GLU A C     
2717 O  O     . GLU A 330 ? 0.7129 0.6743 0.6039 0.0012  -0.0159 -0.0427 330 GLU A O     
2718 C  CB    . GLU A 330 ? 0.8828 0.8489 0.7565 0.0064  0.0015  -0.0423 330 GLU A CB    
2719 C  CG    . GLU A 330 ? 0.8962 0.8705 0.7716 0.0042  0.0052  -0.0388 330 GLU A CG    
2720 C  CD    . GLU A 330 ? 1.0185 1.0020 0.9076 -0.0023 -0.0013 -0.0360 330 GLU A CD    
2721 O  OE1   . GLU A 330 ? 0.7774 0.7722 0.6830 -0.0038 -0.0020 -0.0351 330 GLU A OE1   
2722 O  OE2   . GLU A 330 ? 1.1206 1.0996 1.0032 -0.0055 -0.0057 -0.0345 330 GLU A OE2   
2723 N  N     . ALA A 331 ? 0.8631 0.7936 0.7186 0.0064  -0.0157 -0.0513 331 ALA A N     
2724 C  CA    . ALA A 331 ? 0.8897 0.8122 0.7506 0.0071  -0.0201 -0.0530 331 ALA A CA    
2725 C  C     . ALA A 331 ? 0.9686 0.8894 0.8379 -0.0004 -0.0330 -0.0505 331 ALA A C     
2726 O  O     . ALA A 331 ? 0.9216 0.8481 0.8078 -0.0016 -0.0356 -0.0471 331 ALA A O     
2727 C  CB    . ALA A 331 ? 0.9390 0.8382 0.7776 0.0129  -0.0182 -0.0604 331 ALA A CB    
2728 N  N     . GLN A 332 ? 1.0492 0.9634 0.9083 -0.0052 -0.0410 -0.0508 332 GLN A N     
2729 C  CA    . GLN A 332 ? 0.9259 0.8406 0.7965 -0.0125 -0.0532 -0.0467 332 GLN A CA    
2730 C  C     . GLN A 332 ? 0.7743 0.7113 0.6691 -0.0147 -0.0505 -0.0391 332 GLN A C     
2731 O  O     . GLN A 332 ? 0.9049 0.8465 0.8161 -0.0177 -0.0556 -0.0343 332 GLN A O     
2732 C  CB    . GLN A 332 ? 1.1093 1.0141 0.9648 -0.0170 -0.0625 -0.0475 332 GLN A CB    
2733 C  CG    . GLN A 332 ? 1.2753 1.1553 1.1021 -0.0151 -0.0668 -0.0560 332 GLN A CG    
2734 C  CD    . GLN A 332 ? 1.3465 1.2106 1.1739 -0.0155 -0.0731 -0.0602 332 GLN A CD    
2735 O  OE1   . GLN A 332 ? 1.3953 1.2560 1.2343 -0.0222 -0.0858 -0.0573 332 GLN A OE1   
2736 N  NE2   . GLN A 332 ? 1.2545 1.1089 1.0716 -0.0080 -0.0641 -0.0663 332 GLN A NE2   
2737 N  N     . LEU A 333 ? 0.7106 0.6609 0.6074 -0.0129 -0.0422 -0.0378 333 LEU A N     
2738 C  CA    . LEU A 333 ? 0.6699 0.6389 0.5859 -0.0140 -0.0389 -0.0324 333 LEU A CA    
2739 C  C     . LEU A 333 ? 0.7384 0.7143 0.6660 -0.0113 -0.0355 -0.0310 333 LEU A C     
2740 O  O     . LEU A 333 ? 0.7868 0.7734 0.7290 -0.0128 -0.0364 -0.0258 333 LEU A O     
2741 C  CB    . LEU A 333 ? 0.6938 0.6727 0.6087 -0.0128 -0.0311 -0.0326 333 LEU A CB    
2742 C  CG    . LEU A 333 ? 0.7224 0.7178 0.6531 -0.0137 -0.0276 -0.0291 333 LEU A CG    
2743 C  CD1   . LEU A 333 ? 0.6302 0.6282 0.5696 -0.0174 -0.0330 -0.0244 333 LEU A CD1   
2744 C  CD2   . LEU A 333 ? 0.6729 0.6753 0.6027 -0.0127 -0.0205 -0.0305 333 LEU A CD2   
2745 N  N     A SER A 334 ? 0.8281 0.7982 0.7492 -0.0066 -0.0310 -0.0347 334 SER A N     
2746 N  N     B SER A 334 ? 0.8359 0.8061 0.7571 -0.0066 -0.0309 -0.0347 334 SER A N     
2747 C  CA    A SER A 334 ? 0.7804 0.7569 0.7130 -0.0035 -0.0282 -0.0323 334 SER A CA    
2748 C  CA    B SER A 334 ? 0.8129 0.7895 0.7456 -0.0035 -0.0281 -0.0323 334 SER A CA    
2749 C  C     A SER A 334 ? 0.7791 0.7491 0.7197 -0.0060 -0.0357 -0.0290 334 SER A C     
2750 C  C     B SER A 334 ? 0.7652 0.7352 0.7058 -0.0059 -0.0357 -0.0290 334 SER A C     
2751 O  O     A SER A 334 ? 0.8123 0.7936 0.7676 -0.0062 -0.0355 -0.0230 334 SER A O     
2752 O  O     B SER A 334 ? 0.8405 0.8217 0.7957 -0.0060 -0.0354 -0.0230 334 SER A O     
2753 C  CB    A SER A 334 ? 0.9089 0.8795 0.8343 0.0028  -0.0213 -0.0362 334 SER A CB    
2754 C  CB    B SER A 334 ? 0.8932 0.8641 0.8188 0.0028  -0.0212 -0.0361 334 SER A CB    
2755 O  OG    A SER A 334 ? 0.7141 0.6918 0.6521 0.0061  -0.0188 -0.0327 334 SER A OG    
2756 O  OG    B SER A 334 ? 0.8254 0.7984 0.7419 0.0046  -0.0149 -0.0388 334 SER A OG    
2757 N  N     . ARG A 335 ? 0.7515 0.7028 0.6823 -0.0081 -0.0429 -0.0325 335 ARG A N     
2758 C  CA    . ARG A 335 ? 0.8056 0.7497 0.7465 -0.0117 -0.0515 -0.0288 335 ARG A CA    
2759 C  C     . ARG A 335 ? 0.8149 0.7717 0.7712 -0.0169 -0.0558 -0.0207 335 ARG A C     
2760 O  O     . ARG A 335 ? 0.8385 0.8013 0.8116 -0.0182 -0.0577 -0.0135 335 ARG A O     
2761 C  CB    . ARG A 335 ? 0.8766 0.7962 0.8020 -0.0138 -0.0602 -0.0353 335 ARG A CB    
2762 C  CG    . ARG A 335 ? 0.9720 0.8761 0.8782 -0.0074 -0.0544 -0.0441 335 ARG A CG    
2763 C  CD    . ARG A 335 ? 1.0090 0.8888 0.8913 -0.0092 -0.0623 -0.0524 335 ARG A CD    
2764 N  NE    . ARG A 335 ? 1.2765 1.1390 1.1622 -0.0141 -0.0746 -0.0532 335 ARG A NE    
2765 C  CZ    . ARG A 335 ? 1.2684 1.1257 1.1565 -0.0224 -0.0883 -0.0511 335 ARG A CZ    
2766 N  NH1   . ARG A 335 ? 1.1497 1.0167 1.0353 -0.0261 -0.0912 -0.0483 335 ARG A NH1   
2767 N  NH2   . ARG A 335 ? 1.1815 1.0235 1.0763 -0.0273 -0.0998 -0.0511 335 ARG A NH2   
2768 N  N     . LEU A 336 ? 0.7294 0.6909 0.6813 -0.0194 -0.0565 -0.0210 336 LEU A N     
2769 C  CA    . LEU A 336 ? 0.6951 0.6682 0.6623 -0.0232 -0.0594 -0.0130 336 LEU A CA    
2770 C  C     . LEU A 336 ? 0.7253 0.7171 0.7052 -0.0202 -0.0509 -0.0077 336 LEU A C     
2771 O  O     . LEU A 336 ? 0.8404 0.8404 0.8360 -0.0214 -0.0519 0.0005  336 LEU A O     
2772 C  CB    . LEU A 336 ? 0.9067 0.8799 0.8663 -0.0256 -0.0612 -0.0143 336 LEU A CB    
2773 C  CG    . LEU A 336 ? 0.9016 0.8837 0.8770 -0.0294 -0.0653 -0.0059 336 LEU A CG    
2774 C  CD1   . LEU A 336 ? 0.7353 0.7138 0.7259 -0.0338 -0.0747 0.0008  336 LEU A CD1   
2775 C  CD2   . LEU A 336 ? 0.9082 0.8862 0.8744 -0.0318 -0.0693 -0.0072 336 LEU A CD2   
2776 N  N     . ILE A 337 ? 0.8816 0.8802 0.8543 -0.0162 -0.0428 -0.0119 337 ILE A N     
2777 C  CA    . ILE A 337 ? 0.6073 0.6222 0.5880 -0.0136 -0.0362 -0.0083 337 ILE A CA    
2778 C  C     . ILE A 337 ? 0.6523 0.6707 0.6389 -0.0105 -0.0344 -0.0051 337 ILE A C     
2779 O  O     . ILE A 337 ? 0.7361 0.7669 0.7304 -0.0088 -0.0311 0.0005  337 ILE A O     
2780 C  CB    . ILE A 337 ? 0.4857 0.5066 0.4580 -0.0119 -0.0302 -0.0137 337 ILE A CB    
2781 C  CG1   . ILE A 337 ? 0.6452 0.6619 0.6126 -0.0148 -0.0319 -0.0156 337 ILE A CG1   
2782 C  CG2   . ILE A 337 ? 0.6388 0.6743 0.6163 -0.0100 -0.0252 -0.0113 337 ILE A CG2   
2783 C  CD1   . ILE A 337 ? 0.7105 0.7332 0.6882 -0.0166 -0.0329 -0.0097 337 ILE A CD1   
2784 N  N     . GLY A 338 ? 0.6972 0.7044 0.6796 -0.0090 -0.0361 -0.0082 338 GLY A N     
2785 C  CA    . GLY A 338 ? 0.6823 0.6924 0.6718 -0.0055 -0.0342 -0.0044 338 GLY A CA    
2786 C  C     . GLY A 338 ? 0.7425 0.7642 0.7300 -0.0012 -0.0278 -0.0056 338 GLY A C     
2787 O  O     . GLY A 338 ? 0.7164 0.7482 0.7117 0.0013  -0.0260 0.0003  338 GLY A O     
2788 N  N     . GLN A 339 ? 0.6483 0.6696 0.6264 -0.0004 -0.0247 -0.0122 339 GLN A N     
2789 C  CA    . GLN A 339 ? 0.7253 0.7578 0.7040 0.0028  -0.0197 -0.0130 339 GLN A CA    
2790 C  C     . GLN A 339 ? 0.7634 0.7872 0.7346 0.0054  -0.0163 -0.0187 339 GLN A C     
2791 O  O     . GLN A 339 ? 0.6820 0.6915 0.6435 0.0044  -0.0176 -0.0232 339 GLN A O     
2792 C  CB    . GLN A 339 ? 0.7889 0.8344 0.7669 0.0007  -0.0183 -0.0136 339 GLN A CB    
2793 C  CG    . GLN A 339 ? 0.6378 0.6929 0.6209 0.0001  -0.0194 -0.0079 339 GLN A CG    
2794 C  CD    . GLN A 339 ? 0.7203 0.7830 0.7100 0.0035  -0.0193 -0.0017 339 GLN A CD    
2795 O  OE1   . GLN A 339 ? 0.9601 1.0284 0.9513 0.0060  -0.0181 -0.0020 339 GLN A OE1   
2796 N  NE2   . GLN A 339 ? 0.6542 0.7182 0.6496 0.0038  -0.0204 0.0054  339 GLN A NE2   
2797 N  N     . SER A 340 ? 0.7870 0.8201 0.7628 0.0091  -0.0118 -0.0179 340 SER A N     
2798 C  CA    . SER A 340 ? 0.6103 0.6369 0.5815 0.0132  -0.0064 -0.0214 340 SER A CA    
2799 C  C     . SER A 340 ? 0.6844 0.7071 0.6453 0.0108  -0.0044 -0.0263 340 SER A C     
2800 O  O     . SER A 340 ? 0.6456 0.6761 0.6073 0.0064  -0.0061 -0.0264 340 SER A O     
2801 C  CB    . SER A 340 ? 0.6731 0.7144 0.6558 0.0171  -0.0022 -0.0175 340 SER A CB    
2802 O  OG    . SER A 340 ? 0.7949 0.8506 0.7811 0.0136  -0.0023 -0.0174 340 SER A OG    
2803 N  N     . LEU A 341 ? 0.6334 0.6427 0.5835 0.0143  -0.0002 -0.0302 341 LEU A N     
2804 C  CA    . LEU A 341 ? 0.6857 0.6917 0.6254 0.0132  0.0030  -0.0334 341 LEU A CA    
2805 C  C     . LEU A 341 ? 0.8082 0.8319 0.7587 0.0121  0.0073  -0.0306 341 LEU A C     
2806 O  O     . LEU A 341 ? 0.8533 0.8800 0.8018 0.0079  0.0067  -0.0312 341 LEU A O     
2807 C  CB    . LEU A 341 ? 0.7675 0.7572 0.6924 0.0190  0.0087  -0.0374 341 LEU A CB    
2808 C  CG    . LEU A 341 ? 0.8674 0.8542 0.7809 0.0210  0.0160  -0.0390 341 LEU A CG    
2809 C  CD1   . LEU A 341 ? 0.7089 0.6983 0.6182 0.0145  0.0118  -0.0389 341 LEU A CD1   
2810 C  CD2   . LEU A 341 ? 0.8548 0.8198 0.7470 0.0269  0.0196  -0.0443 341 LEU A CD2   
2811 N  N     . TRP A 342 ? 0.7544 0.7896 0.7179 0.0156  0.0108  -0.0270 342 TRP A N     
2812 C  CA    . TRP A 342 ? 0.7606 0.8132 0.7370 0.0135  0.0127  -0.0239 342 TRP A CA    
2813 C  C     . TRP A 342 ? 0.6701 0.7303 0.6491 0.0066  0.0058  -0.0245 342 TRP A C     
2814 O  O     . TRP A 342 ? 0.6979 0.7646 0.6805 0.0028  0.0062  -0.0248 342 TRP A O     
2815 C  CB    . TRP A 342 ? 0.8745 0.9396 0.8667 0.0177  0.0147  -0.0186 342 TRP A CB    
2816 C  CG    . TRP A 342 ? 0.6770 0.7592 0.6842 0.0156  0.0163  -0.0148 342 TRP A CG    
2817 C  CD1   . TRP A 342 ? 0.6691 0.7563 0.6845 0.0192  0.0247  -0.0115 342 TRP A CD1   
2818 C  CD2   . TRP A 342 ? 0.6691 0.7653 0.6854 0.0092  0.0091  -0.0138 342 TRP A CD2   
2819 N  NE1   . TRP A 342 ? 0.6920 0.7964 0.7241 0.0146  0.0221  -0.0077 342 TRP A NE1   
2820 C  CE2   . TRP A 342 ? 0.6362 0.7453 0.6676 0.0082  0.0119  -0.0099 342 TRP A CE2   
2821 C  CE3   . TRP A 342 ? 0.6018 0.7004 0.6143 0.0046  0.0008  -0.0157 342 TRP A CE3   
2822 C  CZ2   . TRP A 342 ? 0.5799 0.7024 0.6221 0.0016  0.0047  -0.0089 342 TRP A CZ2   
2823 C  CZ3   . TRP A 342 ? 0.6612 0.7722 0.6811 -0.0007 -0.0049 -0.0154 342 TRP A CZ3   
2824 C  CH2   . TRP A 342 ? 0.6166 0.7388 0.6510 -0.0027 -0.0039 -0.0125 342 TRP A CH2   
2825 N  N     . ASP A 343 ? 0.6907 0.7495 0.6682 0.0052  0.0000  -0.0243 343 ASP A N     
2826 C  CA    . ASP A 343 ? 0.7651 0.8304 0.7435 0.0002  -0.0049 -0.0248 343 ASP A CA    
2827 C  C     . ASP A 343 ? 0.7406 0.7965 0.7102 -0.0032 -0.0059 -0.0279 343 ASP A C     
2828 O  O     . ASP A 343 ? 0.7371 0.7967 0.7076 -0.0068 -0.0062 -0.0295 343 ASP A O     
2829 C  CB    . ASP A 343 ? 0.7896 0.8586 0.7704 0.0010  -0.0091 -0.0217 343 ASP A CB    
2830 C  CG    . ASP A 343 ? 0.7108 0.7934 0.7013 0.0030  -0.0101 -0.0177 343 ASP A CG    
2831 O  OD1   . ASP A 343 ? 0.7212 0.8145 0.7146 -0.0001 -0.0128 -0.0181 343 ASP A OD1   
2832 O  OD2   . ASP A 343 ? 0.7904 0.8726 0.7858 0.0075  -0.0089 -0.0139 343 ASP A OD2   
2833 N  N     . VAL A 344 ? 0.6750 0.7181 0.6366 -0.0023 -0.0070 -0.0286 344 VAL A N     
2834 C  CA    . VAL A 344 ? 0.8102 0.8457 0.7653 -0.0056 -0.0093 -0.0300 344 VAL A CA    
2835 C  C     . VAL A 344 ? 0.7834 0.8157 0.7333 -0.0065 -0.0056 -0.0318 344 VAL A C     
2836 O  O     . VAL A 344 ? 0.7732 0.8026 0.7205 -0.0096 -0.0071 -0.0320 344 VAL A O     
2837 C  CB    . VAL A 344 ? 0.6717 0.6945 0.6207 -0.0054 -0.0136 -0.0296 344 VAL A CB    
2838 C  CG1   . VAL A 344 ? 0.6708 0.6977 0.6278 -0.0050 -0.0167 -0.0260 344 VAL A CG1   
2839 C  CG2   . VAL A 344 ? 0.7949 0.8059 0.7343 -0.0019 -0.0114 -0.0322 344 VAL A CG2   
2840 N  N     . SER A 345 ? 0.8902 0.9236 0.8398 -0.0035 -0.0002 -0.0319 345 SER A N     
2841 C  CA    . SER A 345 ? 0.8304 0.8613 0.7754 -0.0037 0.0046  -0.0319 345 SER A CA    
2842 C  C     . SER A 345 ? 0.6574 0.6991 0.6133 -0.0078 0.0054  -0.0309 345 SER A C     
2843 O  O     . SER A 345 ? 0.7151 0.7544 0.6690 -0.0094 0.0082  -0.0300 345 SER A O     
2844 C  CB    . SER A 345 ? 0.6428 0.6716 0.5847 0.0019  0.0119  -0.0313 345 SER A CB    
2845 O  OG    . SER A 345 ? 0.8714 0.9123 0.8274 0.0039  0.0139  -0.0291 345 SER A OG    
2846 N  N     . ARG A 346 ? 0.6852 0.7376 0.6518 -0.0095 0.0027  -0.0310 346 ARG A N     
2847 C  CA    . ARG A 346 ? 0.7136 0.7739 0.6894 -0.0139 0.0017  -0.0315 346 ARG A CA    
2848 C  C     . ARG A 346 ? 0.8208 0.8815 0.7958 -0.0168 -0.0034 -0.0341 346 ARG A C     
2849 O  O     . ARG A 346 ? 0.8275 0.8924 0.8079 -0.0203 -0.0050 -0.0361 346 ARG A O     
2850 C  CB    . ARG A 346 ? 0.6710 0.7440 0.6597 -0.0139 0.0025  -0.0295 346 ARG A CB    
2851 C  CG    . ARG A 346 ? 0.7085 0.7828 0.7000 -0.0092 0.0092  -0.0258 346 ARG A CG    
2852 C  CD    . ARG A 346 ? 0.7612 0.8459 0.7628 -0.0063 0.0085  -0.0231 346 ARG A CD    
2853 N  NE    . ARG A 346 ? 0.8854 0.9656 0.8841 0.0008  0.0155  -0.0207 346 ARG A NE    
2854 C  CZ    . ARG A 346 ? 0.7094 0.7950 0.7169 0.0041  0.0233  -0.0164 346 ARG A CZ    
2855 N  NH1   . ARG A 346 ? 0.6944 0.7916 0.7171 0.0002  0.0241  -0.0129 346 ARG A NH1   
2856 N  NH2   . ARG A 346 ? 0.8516 0.9304 0.8532 0.0118  0.0307  -0.0153 346 ARG A NH2   
2857 N  N     . SER A 347 ? 0.8735 0.9292 0.8422 -0.0151 -0.0057 -0.0339 347 SER A N     
2858 C  CA    . SER A 347 ? 0.7497 0.8067 0.7178 -0.0162 -0.0087 -0.0351 347 SER A CA    
2859 C  C     . SER A 347 ? 0.8177 0.8679 0.7840 -0.0182 -0.0081 -0.0359 347 SER A C     
2860 O  O     . SER A 347 ? 0.7413 0.7843 0.7044 -0.0182 -0.0073 -0.0341 347 SER A O     
2861 C  CB    . SER A 347 ? 0.7879 0.8442 0.7538 -0.0134 -0.0106 -0.0325 347 SER A CB    
2862 O  OG    . SER A 347 ? 0.9776 1.0417 0.9467 -0.0114 -0.0115 -0.0312 347 SER A OG    
2863 N  N     . SER A 348 ? 0.7337 0.7855 0.7012 -0.0195 -0.0085 -0.0385 348 SER A N     
2864 C  CA    . SER A 348 ? 0.7239 0.7692 0.6913 -0.0202 -0.0072 -0.0386 348 SER A CA    
2865 C  C     . SER A 348 ? 0.7630 0.8057 0.7293 -0.0178 -0.0078 -0.0344 348 SER A C     
2866 O  O     . SER A 348 ? 0.8810 0.9272 0.8466 -0.0159 -0.0093 -0.0323 348 SER A O     
2867 C  CB    . SER A 348 ? 0.8140 0.8595 0.7813 -0.0212 -0.0067 -0.0434 348 SER A CB    
2868 O  OG    . SER A 348 ? 0.9177 0.9661 0.8806 -0.0182 -0.0067 -0.0436 348 SER A OG    
2869 N  N     . THR A 349 ? 0.8817 0.9189 0.8501 -0.0182 -0.0071 -0.0321 349 THR A N     
2870 C  CA    . THR A 349 ? 0.7438 0.7797 0.7151 -0.0167 -0.0087 -0.0267 349 THR A CA    
2871 C  C     . THR A 349 ? 0.7592 0.8005 0.7324 -0.0138 -0.0068 -0.0256 349 THR A C     
2872 O  O     . THR A 349 ? 0.7688 0.8125 0.7451 -0.0126 -0.0086 -0.0207 349 THR A O     
2873 C  CB    . THR A 349 ? 0.7020 0.7328 0.6777 -0.0174 -0.0082 -0.0234 349 THR A CB    
2874 O  OG1   . THR A 349 ? 0.8493 0.8751 0.8211 -0.0196 -0.0108 -0.0222 349 THR A OG1   
2875 C  CG2   . THR A 349 ? 0.7908 0.8228 0.7740 -0.0158 -0.0096 -0.0167 349 THR A CG2   
2876 N  N     . GLY A 350 ? 0.7268 0.7694 0.6975 -0.0125 -0.0031 -0.0301 350 GLY A N     
2877 C  CA    . GLY A 350 ? 0.6192 0.6665 0.5879 -0.0088 -0.0002 -0.0292 350 GLY A CA    
2878 C  C     . GLY A 350 ? 0.8375 0.8913 0.8032 -0.0081 -0.0027 -0.0277 350 GLY A C     
2879 O  O     . GLY A 350 ? 0.8066 0.8645 0.7754 -0.0055 -0.0017 -0.0216 350 GLY A O     
2880 N  N     . ASN A 351 ? 0.8555 0.9112 0.8177 -0.0103 -0.0056 -0.0318 351 ASN A N     
2881 C  CA    . ASN A 351 ? 0.7894 0.8517 0.7503 -0.0092 -0.0079 -0.0297 351 ASN A CA    
2882 C  C     . ASN A 351 ? 0.7312 0.7918 0.6977 -0.0090 -0.0100 -0.0239 351 ASN A C     
2883 O  O     . ASN A 351 ? 0.7346 0.7995 0.7027 -0.0070 -0.0108 -0.0194 351 ASN A O     
2884 C  CB    . ASN A 351 ? 0.6957 0.7612 0.6549 -0.0115 -0.0105 -0.0344 351 ASN A CB    
2885 C  CG    . ASN A 351 ? 0.8201 0.8887 0.7726 -0.0119 -0.0112 -0.0397 351 ASN A CG    
2886 O  OD1   . ASN A 351 ? 0.8919 0.9616 0.8377 -0.0089 -0.0093 -0.0394 351 ASN A OD1   
2887 N  ND2   . ASN A 351 ? 0.8921 0.9617 0.8462 -0.0155 -0.0139 -0.0442 351 ASN A ND2   
2888 N  N     . LEU A 352 ? 0.7058 0.7593 0.6744 -0.0111 -0.0114 -0.0237 352 LEU A N     
2889 C  CA    . LEU A 352 ? 0.6938 0.7427 0.6654 -0.0114 -0.0149 -0.0194 352 LEU A CA    
2890 C  C     . LEU A 352 ? 0.7643 0.8149 0.7434 -0.0105 -0.0152 -0.0125 352 LEU A C     
2891 O  O     . LEU A 352 ? 0.8190 0.8690 0.8027 -0.0103 -0.0181 -0.0078 352 LEU A O     
2892 C  CB    . LEU A 352 ? 0.6756 0.7156 0.6443 -0.0138 -0.0170 -0.0210 352 LEU A CB    
2893 C  CG    . LEU A 352 ? 0.7175 0.7552 0.6800 -0.0141 -0.0158 -0.0256 352 LEU A CG    
2894 C  CD1   . LEU A 352 ? 0.6928 0.7253 0.6522 -0.0161 -0.0150 -0.0269 352 LEU A CD1   
2895 C  CD2   . LEU A 352 ? 0.8517 0.8836 0.8104 -0.0129 -0.0181 -0.0254 352 LEU A CD2   
2896 N  N     . VAL A 353 ? 0.7943 0.8469 0.7764 -0.0096 -0.0119 -0.0110 353 VAL A N     
2897 C  CA    . VAL A 353 ? 0.7475 0.8034 0.7397 -0.0080 -0.0107 -0.0027 353 VAL A CA    
2898 C  C     . VAL A 353 ? 0.7347 0.7986 0.7268 -0.0044 -0.0072 0.0009  353 VAL A C     
2899 O  O     . VAL A 353 ? 0.7772 0.8441 0.7787 -0.0039 -0.0083 0.0091  353 VAL A O     
2900 C  CB    . VAL A 353 ? 0.7333 0.7890 0.7296 -0.0067 -0.0064 -0.0016 353 VAL A CB    
2901 C  CG1   . VAL A 353 ? 0.7388 0.8010 0.7464 -0.0033 -0.0021 0.0077  353 VAL A CG1   
2902 C  CG2   . VAL A 353 ? 0.7425 0.7912 0.7419 -0.0104 -0.0113 -0.0013 353 VAL A CG2   
2903 N  N     . GLU A 354 ? 0.6711 0.7386 0.6527 -0.0021 -0.0035 -0.0046 354 GLU A N     
2904 C  CA    . GLU A 354 ? 0.7081 0.7835 0.6860 0.0017  -0.0006 -0.0012 354 GLU A CA    
2905 C  C     . GLU A 354 ? 0.8114 0.8887 0.7941 0.0009  -0.0049 0.0035  354 GLU A C     
2906 O  O     . GLU A 354 ? 0.7898 0.8725 0.7781 0.0034  -0.0031 0.0120  354 GLU A O     
2907 C  CB    . GLU A 354 ? 0.7995 0.8766 0.7630 0.0028  0.0009  -0.0095 354 GLU A CB    
2908 C  CG    . GLU A 354 ? 0.8818 0.9668 0.8373 0.0070  0.0034  -0.0063 354 GLU A CG    
2909 C  CD    . GLU A 354 ? 0.9443 1.0318 0.8879 0.0060  -0.0005 -0.0135 354 GLU A CD    
2910 O  OE1   . GLU A 354 ? 1.0295 1.1155 0.9766 0.0021  -0.0055 -0.0174 354 GLU A OE1   
2911 O  OE2   . GLU A 354 ? 1.0095 1.1007 0.9402 0.0092  0.0014  -0.0147 354 GLU A OE2   
2912 N  N     . TRP A 355 ? 0.7271 0.7996 0.7082 -0.0019 -0.0096 -0.0014 355 TRP A N     
2913 C  CA    . TRP A 355 ? 0.8015 0.8733 0.7872 -0.0019 -0.0131 0.0023  355 TRP A CA    
2914 C  C     . TRP A 355 ? 0.6937 0.7604 0.6910 -0.0035 -0.0160 0.0094  355 TRP A C     
2915 O  O     . TRP A 355 ? 0.8259 0.8945 0.8307 -0.0024 -0.0169 0.0166  355 TRP A O     
2916 C  CB    . TRP A 355 ? 0.7690 0.8357 0.7504 -0.0036 -0.0159 -0.0045 355 TRP A CB    
2917 C  CG    . TRP A 355 ? 0.7987 0.8729 0.7742 -0.0023 -0.0150 -0.0083 355 TRP A CG    
2918 C  CD1   . TRP A 355 ? 0.8617 0.9455 0.8341 0.0002  -0.0140 -0.0056 355 TRP A CD1   
2919 C  CD2   . TRP A 355 ? 0.8169 0.8902 0.7894 -0.0036 -0.0156 -0.0145 355 TRP A CD2   
2920 N  NE1   . TRP A 355 ? 0.8864 0.9753 0.8546 -0.0002 -0.0156 -0.0102 355 TRP A NE1   
2921 C  CE2   . TRP A 355 ? 0.8127 0.8959 0.7828 -0.0026 -0.0162 -0.0152 355 TRP A CE2   
2922 C  CE3   . TRP A 355 ? 0.8837 0.9493 0.8553 -0.0055 -0.0157 -0.0187 355 TRP A CE3   
2923 C  CZ2   . TRP A 355 ? 0.9078 0.9943 0.8785 -0.0040 -0.0173 -0.0194 355 TRP A CZ2   
2924 C  CZ3   . TRP A 355 ? 0.7820 0.8510 0.7532 -0.0060 -0.0149 -0.0225 355 TRP A CZ3   
2925 C  CH2   . TRP A 355 ? 0.8031 0.8828 0.7756 -0.0056 -0.0159 -0.0225 355 TRP A CH2   
2926 N  N     . PHE A 356 ? 0.7693 0.8294 0.7695 -0.0065 -0.0182 0.0083  356 PHE A N     
2927 C  CA    . PHE A 356 ? 0.7721 0.8278 0.7848 -0.0091 -0.0228 0.0155  356 PHE A CA    
2928 C  C     . PHE A 356 ? 0.8063 0.8718 0.8311 -0.0067 -0.0184 0.0263  356 PHE A C     
2929 O  O     . PHE A 356 ? 0.7122 0.7777 0.7497 -0.0078 -0.0213 0.0347  356 PHE A O     
2930 C  CB    . PHE A 356 ? 0.6971 0.7459 0.7101 -0.0126 -0.0265 0.0131  356 PHE A CB    
2931 C  CG    . PHE A 356 ? 0.7326 0.7770 0.7593 -0.0165 -0.0336 0.0205  356 PHE A CG    
2932 C  CD1   . PHE A 356 ? 0.7390 0.7721 0.7652 -0.0199 -0.0418 0.0192  356 PHE A CD1   
2933 C  CD2   . PHE A 356 ? 0.7121 0.7630 0.7528 -0.0167 -0.0322 0.0289  356 PHE A CD2   
2934 C  CE1   . PHE A 356 ? 0.7565 0.7843 0.7955 -0.0246 -0.0505 0.0256  356 PHE A CE1   
2935 C  CE2   . PHE A 356 ? 0.6610 0.7092 0.7175 -0.0211 -0.0402 0.0369  356 PHE A CE2   
2936 C  CZ    . PHE A 356 ? 0.7368 0.7731 0.7922 -0.0257 -0.0503 0.0350  356 PHE A CZ    
2937 N  N     . LEU A 357 ? 0.7602 0.8334 0.7813 -0.0031 -0.0110 0.0264  357 LEU A N     
2938 C  CA    . LEU A 357 ? 0.6390 0.7219 0.6694 0.0008  -0.0044 0.0370  357 LEU A CA    
2939 C  C     . LEU A 357 ? 0.7409 0.8302 0.7693 0.0040  -0.0020 0.0420  357 LEU A C     
2940 O  O     . LEU A 357 ? 0.7182 0.8131 0.7601 0.0053  0.0000  0.0541  357 LEU A O     
2941 C  CB    . LEU A 357 ? 0.6801 0.7668 0.7027 0.0051  0.0040  0.0340  357 LEU A CB    
2942 C  CG    . LEU A 357 ? 0.7073 0.7896 0.7363 0.0032  0.0035  0.0327  357 LEU A CG    
2943 C  CD1   . LEU A 357 ? 0.7591 0.8449 0.7834 0.0090  0.0137  0.0320  357 LEU A CD1   
2944 C  CD2   . LEU A 357 ? 0.7036 0.7863 0.7542 -0.0003 -0.0017 0.0436  357 LEU A CD2   
2945 N  N     . LEU A 358 ? 0.8325 0.9219 0.8459 0.0052  -0.0025 0.0343  358 LEU A N     
2946 C  CA    . LEU A 358 ? 0.6835 0.7799 0.6945 0.0085  -0.0011 0.0397  358 LEU A CA    
2947 C  C     . LEU A 358 ? 0.6488 0.7416 0.6745 0.0062  -0.0062 0.0472  358 LEU A C     
2948 O  O     . LEU A 358 ? 0.6253 0.7247 0.6587 0.0088  -0.0037 0.0582  358 LEU A O     
2949 C  CB    . LEU A 358 ? 0.7801 0.8775 0.7750 0.0092  -0.0027 0.0302  358 LEU A CB    
2950 C  CG    . LEU A 358 ? 0.8626 0.9647 0.8409 0.0123  0.0020  0.0244  358 LEU A CG    
2951 C  CD1   . LEU A 358 ? 0.8257 0.9308 0.7924 0.0122  -0.0020 0.0181  358 LEU A CD1   
2952 C  CD2   . LEU A 358 ? 0.8151 0.9251 0.7911 0.0179  0.0096  0.0335  358 LEU A CD2   
2953 N  N     . ARG A 359 ? 0.5039 0.5853 0.5328 0.0016  -0.0133 0.0415  359 ARG A N     
2954 C  CA    . ARG A 359 ? 0.5912 0.6654 0.6332 -0.0009 -0.0190 0.0471  359 ARG A CA    
2955 C  C     . ARG A 359 ? 0.6957 0.7715 0.7566 -0.0031 -0.0196 0.0587  359 ARG A C     
2956 O  O     . ARG A 359 ? 0.7091 0.7870 0.7837 -0.0028 -0.0200 0.0694  359 ARG A O     
2957 C  CB    . ARG A 359 ? 0.6497 0.7091 0.6865 -0.0048 -0.0259 0.0369  359 ARG A CB    
2958 C  CG    . ARG A 359 ? 0.5580 0.6062 0.6037 -0.0066 -0.0319 0.0396  359 ARG A CG    
2959 C  CD    . ARG A 359 ? 0.6517 0.6837 0.6874 -0.0090 -0.0373 0.0284  359 ARG A CD    
2960 N  NE    . ARG A 359 ? 0.6869 0.7197 0.7108 -0.0050 -0.0337 0.0214  359 ARG A NE    
2961 C  CZ    . ARG A 359 ? 0.6964 0.7233 0.7216 -0.0023 -0.0340 0.0214  359 ARG A CZ    
2962 N  NH1   . ARG A 359 ? 0.6516 0.6696 0.6882 -0.0034 -0.0380 0.0271  359 ARG A NH1   
2963 N  NH2   . ARG A 359 ? 0.8058 0.8359 0.8229 0.0016  -0.0302 0.0162  359 ARG A NH2   
2964 N  N     . LYS A 360 ? 0.7625 0.8377 0.8267 -0.0054 -0.0200 0.0578  360 LYS A N     
2965 C  CA    . LYS A 360 ? 0.7195 0.7994 0.8049 -0.0072 -0.0200 0.0705  360 LYS A CA    
2966 C  C     . LYS A 360 ? 0.7820 0.8764 0.8736 -0.0012 -0.0098 0.0829  360 LYS A C     
2967 O  O     . LYS A 360 ? 0.6044 0.7030 0.7163 -0.0021 -0.0099 0.0965  360 LYS A O     
2968 C  CB    . LYS A 360 ? 0.6147 0.6943 0.7020 -0.0090 -0.0204 0.0682  360 LYS A CB    
2969 C  CG    . LYS A 360 ? 0.5899 0.6555 0.6760 -0.0157 -0.0319 0.0607  360 LYS A CG    
2970 C  CD    . LYS A 360 ? 0.6730 0.7289 0.7720 -0.0213 -0.0424 0.0651  360 LYS A CD    
2971 C  CE    . LYS A 360 ? 0.8448 0.8831 0.9302 -0.0259 -0.0526 0.0529  360 LYS A CE    
2972 N  NZ    . LYS A 360 ? 0.8569 0.8820 0.9457 -0.0291 -0.0605 0.0526  360 LYS A NZ    
2973 N  N     . ALA A 361 ? 0.6410 0.7429 0.7148 0.0048  -0.0012 0.0784  361 ALA A N     
2974 C  CA    . ALA A 361 ? 0.6430 0.7578 0.7169 0.0115  0.0092  0.0893  361 ALA A CA    
2975 C  C     . ALA A 361 ? 0.7034 0.8208 0.7829 0.0123  0.0079  0.0979  361 ALA A C     
2976 O  O     . ALA A 361 ? 0.7819 0.9087 0.8737 0.0156  0.0140  0.1129  361 ALA A O     
2977 C  CB    . ALA A 361 ? 0.5843 0.7030 0.6332 0.0172  0.0165  0.0801  361 ALA A CB    
2978 N  N     . TYR A 362 ? 0.6315 0.7410 0.7033 0.0101  0.0008  0.0897  362 TYR A N     
2979 C  CA    . TYR A 362 ? 0.6503 0.7612 0.7289 0.0112  -0.0007 0.0981  362 TYR A CA    
2980 C  C     . TYR A 362 ? 0.6230 0.7282 0.7279 0.0064  -0.0059 0.1090  362 TYR A C     
2981 O  O     . TYR A 362 ? 0.5505 0.6612 0.6687 0.0082  -0.0035 0.1229  362 TYR A O     
2982 C  CB    . TYR A 362 ? 0.6291 0.7329 0.6950 0.0108  -0.0062 0.0870  362 TYR A CB    
2983 C  CG    . TYR A 362 ? 0.5477 0.6529 0.6211 0.0129  -0.0073 0.0959  362 TYR A CG    
2984 C  CD1   . TYR A 362 ? 0.5658 0.6836 0.6297 0.0188  -0.0021 0.1023  362 TYR A CD1   
2985 C  CD2   . TYR A 362 ? 0.4448 0.5376 0.5339 0.0091  -0.0140 0.0983  362 TYR A CD2   
2986 C  CE1   . TYR A 362 ? 0.5848 0.7046 0.6568 0.0211  -0.0031 0.1120  362 TYR A CE1   
2987 C  CE2   . TYR A 362 ? 0.5166 0.6098 0.6144 0.0115  -0.0145 0.1071  362 TYR A CE2   
2988 C  CZ    . TYR A 362 ? 0.5438 0.6513 0.6339 0.0176  -0.0088 0.1147  362 TYR A CZ    
2989 O  OH    . TYR A 362 ? 0.7388 0.8472 0.8386 0.0203  -0.0094 0.1249  362 TYR A OH    
2990 N  N     . GLU A 363 ? 0.6972 0.7910 0.8099 -0.0001 -0.0138 0.1032  363 GLU A N     
2991 C  CA    . GLU A 363 ? 0.7089 0.7951 0.8464 -0.0061 -0.0214 0.1121  363 GLU A CA    
2992 C  C     . GLU A 363 ? 0.7240 0.8236 0.8841 -0.0053 -0.0153 0.1303  363 GLU A C     
2993 O  O     . GLU A 363 ? 0.7419 0.8415 0.9242 -0.0076 -0.0176 0.1437  363 GLU A O     
2994 C  CB    . GLU A 363 ? 0.7800 0.8512 0.9173 -0.0133 -0.0322 0.1013  363 GLU A CB    
2995 C  CG    . GLU A 363 ? 0.4776 0.5349 0.5930 -0.0137 -0.0370 0.0842  363 GLU A CG    
2996 C  CD    . GLU A 363 ? 0.7914 0.8346 0.9026 -0.0198 -0.0465 0.0741  363 GLU A CD    
2997 O  OE1   . GLU A 363 ? 1.0522 1.0980 1.1769 -0.0239 -0.0499 0.0800  363 GLU A OE1   
2998 O  OE2   . GLU A 363 ? 0.7560 0.7862 0.8505 -0.0202 -0.0504 0.0612  363 GLU A OE2   
2999 N  N     . ARG A 364 ? 0.7728 0.8835 0.9288 -0.0016 -0.0069 0.1318  364 ARG A N     
3000 C  CA    . ARG A 364 ? 0.7421 0.8667 0.9200 0.0006  0.0011  0.1496  364 ARG A CA    
3001 C  C     . ARG A 364 ? 0.7958 0.9352 0.9653 0.0101  0.0154  0.1596  364 ARG A C     
3002 O  O     . ARG A 364 ? 0.7967 0.9490 0.9789 0.0144  0.0257  0.1736  364 ARG A O     
3003 C  CB    . ARG A 364 ? 0.6902 0.8181 0.8708 0.0003  0.0033  0.1473  364 ARG A CB    
3004 C  CG    . ARG A 364 ? 0.8805 0.9941 1.0523 -0.0062 -0.0084 0.1313  364 ARG A CG    
3005 C  CD    . ARG A 364 ? 1.1164 1.2193 1.3103 -0.0161 -0.0233 0.1348  364 ARG A CD    
3006 N  NE    . ARG A 364 ? 1.1556 1.2437 1.3354 -0.0214 -0.0342 0.1189  364 ARG A NE    
3007 C  CZ    . ARG A 364 ? 1.1144 1.2002 1.3043 -0.0266 -0.0416 0.1191  364 ARG A CZ    
3008 N  NH1   . ARG A 364 ? 0.7717 0.8694 0.9887 -0.0275 -0.0395 0.1345  364 ARG A NH1   
3009 N  NH2   . ARG A 364 ? 0.8896 0.9614 1.0627 -0.0307 -0.0510 0.1047  364 ARG A NH2   
3010 N  N     . ASN A 365 ? 0.6427 0.7809 0.7910 0.0138  0.0163  0.1534  365 ASN A N     
3011 C  CA    . ASN A 365 ? 0.5858 0.7373 0.7211 0.0228  0.0282  0.1618  365 ASN A CA    
3012 C  C     . ASN A 365 ? 0.6796 0.8394 0.7986 0.0297  0.0400  0.1593  365 ASN A C     
3013 O  O     . ASN A 365 ? 0.7594 0.9315 0.8777 0.0372  0.0525  0.1721  365 ASN A O     
3014 C  CB    . ASN A 365 ? 0.5924 0.7525 0.7525 0.0240  0.0325  0.1840  365 ASN A CB    
3015 C  CG    . ASN A 365 ? 0.8631 1.0345 1.0067 0.0328  0.0420  0.1924  365 ASN A CG    
3016 O  OD1   . ASN A 365 ? 0.8791 1.0475 0.9999 0.0346  0.0388  0.1823  365 ASN A OD1   
3017 N  ND2   . ASN A 365 ? 0.7629 0.9479 0.9184 0.0383  0.0539  0.2118  365 ASN A ND2   
3018 N  N     . GLU A 366 ? 0.7677 0.9200 0.8731 0.0277  0.0367  0.1428  366 GLU A N     
3019 C  CA    . GLU A 366 ? 0.8027 0.9591 0.8912 0.0340  0.0470  0.1374  366 GLU A CA    
3020 C  C     . GLU A 366 ? 0.7675 0.9223 0.8217 0.0382  0.0481  0.1241  366 GLU A C     
3021 O  O     . GLU A 366 ? 0.8376 0.9834 0.8805 0.0336  0.0386  0.1094  366 GLU A O     
3022 C  CB    . GLU A 366 ? 0.8559 1.0047 0.9511 0.0292  0.0424  0.1282  366 GLU A CB    
3023 C  CG    . GLU A 366 ? 0.9908 1.1468 1.0949 0.0345  0.0539  0.1356  366 GLU A CG    
3024 C  CD    . GLU A 366 ? 1.0265 1.1903 1.1674 0.0321  0.0546  0.1550  366 GLU A CD    
3025 O  OE1   . GLU A 366 ? 0.8657 1.0231 1.0265 0.0227  0.0415  0.1555  366 GLU A OE1   
3026 O  OE2   . GLU A 366 ? 1.1461 1.3222 1.2959 0.0395  0.0683  0.1699  366 GLU A OE2   
3027 N  N     . LEU A 367 ? 0.7950 0.9586 0.8324 0.0470  0.0593  0.1298  367 LEU A N     
3028 C  CA    . LEU A 367 ? 0.6531 0.8150 0.6566 0.0507  0.0592  0.1170  367 LEU A CA    
3029 C  C     . LEU A 367 ? 0.8833 1.0358 0.8724 0.0493  0.0579  0.0992  367 LEU A C     
3030 O  O     . LEU A 367 ? 0.8631 1.0153 0.8542 0.0529  0.0667  0.0997  367 LEU A O     
3031 C  CB    . LEU A 367 ? 0.7626 0.9342 0.7480 0.0608  0.0719  0.1265  367 LEU A CB    
3032 C  CG    . LEU A 367 ? 0.7482 0.9174 0.6957 0.0646  0.0708  0.1132  367 LEU A CG    
3033 C  CD1   . LEU A 367 ? 0.8247 0.9952 0.7680 0.0606  0.0590  0.1119  367 LEU A CD1   
3034 C  CD2   . LEU A 367 ? 0.7337 0.9096 0.6589 0.0758  0.0851  0.1205  367 LEU A CD2   
3035 N  N     . ALA A 368 ? 0.8650 1.0103 0.8419 0.0443  0.0475  0.0846  368 ALA A N     
3036 C  CA    . ALA A 368 ? 0.7439 0.8798 0.7108 0.0417  0.0451  0.0685  368 ALA A CA    
3037 C  C     . ALA A 368 ? 0.7795 0.9142 0.7183 0.0486  0.0530  0.0609  368 ALA A C     
3038 O  O     . ALA A 368 ? 0.8882 1.0270 0.8064 0.0524  0.0536  0.0608  368 ALA A O     
3039 C  CB    . ALA A 368 ? 0.6700 0.7995 0.6333 0.0347  0.0326  0.0566  368 ALA A CB    
3040 N  N     . PRO A 369 ? 0.8795 1.0080 0.8162 0.0504  0.0589  0.0546  369 PRO A N     
3041 C  CA    . PRO A 369 ? 0.8497 0.9730 0.7577 0.0566  0.0657  0.0443  369 PRO A CA    
3042 C  C     . PRO A 369 ? 0.8649 0.9795 0.7548 0.0511  0.0548  0.0269  369 PRO A C     
3043 O  O     . PRO A 369 ? 0.8889 0.9997 0.7911 0.0432  0.0452  0.0212  369 PRO A O     
3044 C  CB    . PRO A 369 ? 0.6994 0.8180 0.6174 0.0601  0.0754  0.0446  369 PRO A CB    
3045 C  CG    . PRO A 369 ? 0.7247 0.8484 0.6779 0.0552  0.0726  0.0566  369 PRO A CG    
3046 C  CD    . PRO A 369 ? 0.8426 0.9678 0.8033 0.0471  0.0593  0.0568  369 PRO A CD    
3047 N  N     . ASN A 370 ? 0.9331 1.0446 0.7930 0.0555  0.0564  0.0188  370 ASN A N     
3048 C  CA    . ASN A 370 ? 0.8853 0.9893 0.7287 0.0499  0.0453  0.0030  370 ASN A CA    
3049 C  C     . ASN A 370 ? 0.9366 1.0281 0.7838 0.0465  0.0450  -0.0091 370 ASN A C     
3050 O  O     . ASN A 370 ? 0.9941 1.0821 0.8517 0.0501  0.0544  -0.0062 370 ASN A O     
3051 C  CB    . ASN A 370 ? 0.8347 0.9368 0.6434 0.0550  0.0458  -0.0031 370 ASN A CB    
3052 C  CG    . ASN A 370 ? 0.8601 0.9751 0.6632 0.0587  0.0459  0.0099  370 ASN A CG    
3053 O  OD1   . ASN A 370 ? 0.8939 1.0179 0.7168 0.0544  0.0395  0.0189  370 ASN A OD1   
3054 N  ND2   . ASN A 370 ? 0.8595 0.9744 0.6345 0.0672  0.0534  0.0110  370 ASN A ND2   
3055 N  N     . LYS A 371 ? 0.9069 0.9924 0.7476 0.0396  0.0341  -0.0216 371 LYS A N     
3056 C  CA    . LYS A 371 ? 0.7831 0.8555 0.6225 0.0367  0.0335  -0.0341 371 LYS A CA    
3057 C  C     . LYS A 371 ? 0.8259 0.8873 0.6368 0.0432  0.0400  -0.0438 371 LYS A C     
3058 O  O     . LYS A 371 ? 0.9060 0.9699 0.6937 0.0476  0.0403  -0.0440 371 LYS A O     
3059 C  CB    . LYS A 371 ? 0.7802 0.8507 0.6238 0.0271  0.0201  -0.0427 371 LYS A CB    
3060 C  CG    . LYS A 371 ? 0.7740 0.8521 0.6431 0.0217  0.0151  -0.0349 371 LYS A CG    
3061 C  CD    . LYS A 371 ? 0.7221 0.7933 0.6018 0.0144  0.0093  -0.0428 371 LYS A CD    
3062 C  CE    . LYS A 371 ? 0.8888 0.9650 0.7905 0.0106  0.0063  -0.0354 371 LYS A CE    
3063 N  NZ    . LYS A 371 ? 1.0832 1.1515 0.9964 0.0068  0.0065  -0.0389 371 LYS A NZ    
3064 N  N     . PRO A 372 ? 0.8512 0.8996 0.6621 0.0445  0.0454  -0.0518 372 PRO A N     
3065 C  CA    . PRO A 372 ? 0.9575 0.9922 0.7399 0.0517  0.0526  -0.0622 372 PRO A CA    
3066 C  C     . PRO A 372 ? 1.1028 1.1287 0.8611 0.0462  0.0401  -0.0774 372 PRO A C     
3067 O  O     . PRO A 372 ? 1.1530 1.1803 0.9224 0.0361  0.0271  -0.0817 372 PRO A O     
3068 C  CB    . PRO A 372 ? 0.8917 0.9148 0.6874 0.0534  0.0605  -0.0657 372 PRO A CB    
3069 C  CG    . PRO A 372 ? 0.9319 0.9586 0.7542 0.0430  0.0504  -0.0643 372 PRO A CG    
3070 C  CD    . PRO A 372 ? 0.8974 0.9415 0.7329 0.0397  0.0448  -0.0522 372 PRO A CD    
3071 N  N     . ASP A 373 ? 1.1220 1.1385 0.8466 0.0528  0.0438  -0.0853 373 ASP A N     
3072 C  CA    . ASP A 373 ? 1.2585 1.2638 0.9588 0.0471  0.0305  -0.1012 373 ASP A CA    
3073 C  C     . ASP A 373 ? 1.2947 1.2771 0.9876 0.0475  0.0339  -0.1163 373 ASP A C     
3074 O  O     . ASP A 373 ? 1.3108 1.2898 1.0256 0.0491  0.0427  -0.1131 373 ASP A O     
3075 C  CB    . ASP A 373 ? 1.3271 1.3350 0.9928 0.0524  0.0287  -0.1016 373 ASP A CB    
3076 C  CG    . ASP A 373 ? 1.4559 1.4510 1.0909 0.0658  0.0448  -0.1054 373 ASP A CG    
3077 O  OD1   . ASP A 373 ? 1.6105 1.5840 1.2241 0.0673  0.0454  -0.1218 373 ASP A OD1   
3078 O  OD2   . ASP A 373 ? 1.4247 1.4308 1.0575 0.0753  0.0574  -0.0918 373 ASP A OD2   
3079 N  N     . GLU A 374 ? 1.4092 1.3751 1.0716 0.0459  0.0262  -0.1326 374 GLU A N     
3080 C  CA    . GLU A 374 ? 1.4507 1.3935 1.1101 0.0435  0.0257  -0.1480 374 GLU A CA    
3081 C  C     . GLU A 374 ? 1.4553 1.3847 1.1085 0.0562  0.0458  -0.1488 374 GLU A C     
3082 O  O     . GLU A 374 ? 1.4622 1.3840 1.1376 0.0557  0.0515  -0.1492 374 GLU A O     
3083 C  CB    . GLU A 374 ? 1.6840 1.6108 1.3111 0.0382  0.0112  -0.1657 374 GLU A CB    
3084 C  CG    . GLU A 374 ? 1.7984 1.7257 1.4444 0.0228  -0.0080 -0.1714 374 GLU A CG    
3085 C  CD    . GLU A 374 ? 1.9088 1.8174 1.5250 0.0168  -0.0231 -0.1898 374 GLU A CD    
3086 O  OE1   . GLU A 374 ? 1.7885 1.6982 1.3726 0.0197  -0.0285 -0.1927 374 GLU A OE1   
3087 O  OE2   . GLU A 374 ? 1.8493 1.7418 1.4742 0.0090  -0.0302 -0.2010 374 GLU A OE2   
3088 N  N     . LYS A 375 ? 1.4788 1.4055 1.1023 0.0684  0.0574  -0.1481 375 LYS A N     
3089 C  CA    . LYS A 375 ? 1.6494 1.5635 1.2660 0.0823  0.0783  -0.1483 375 LYS A CA    
3090 C  C     . LYS A 375 ? 1.6225 1.5518 1.2803 0.0852  0.0902  -0.1306 375 LYS A C     
3091 O  O     . LYS A 375 ? 1.6511 1.5692 1.3210 0.0905  0.1016  -0.1318 375 LYS A O     
3092 C  CB    . LYS A 375 ? 1.7466 1.6595 1.3252 0.0955  0.0897  -0.1473 375 LYS A CB    
3093 C  CG    . LYS A 375 ? 1.8630 1.7463 1.3965 0.1021  0.0925  -0.1680 375 LYS A CG    
3094 C  CD    . LYS A 375 ? 1.8102 1.6909 1.3141 0.1202  0.1138  -0.1633 375 LYS A CD    
3095 C  CE    . LYS A 375 ? 1.8712 1.7620 1.4077 0.1306  0.1360  -0.1466 375 LYS A CE    
3096 N  NZ    . LYS A 375 ? 1.7874 1.6588 1.3399 0.1316  0.1421  -0.1556 375 LYS A NZ    
3097 N  N     . GLU A 376 ? 1.4851 1.4392 1.1652 0.0817  0.0872  -0.1137 376 GLU A N     
3098 C  CA    . GLU A 376 ? 1.2878 1.2561 1.0060 0.0837  0.0964  -0.0968 376 GLU A CA    
3099 C  C     . GLU A 376 ? 1.2501 1.2149 0.9974 0.0735  0.0879  -0.0994 376 GLU A C     
3100 O  O     . GLU A 376 ? 1.2988 1.2615 1.0680 0.0771  0.0973  -0.0939 376 GLU A O     
3101 C  CB    . GLU A 376 ? 1.2542 1.2473 0.9874 0.0821  0.0943  -0.0791 376 GLU A CB    
3102 C  CG    . GLU A 376 ? 1.5415 1.5423 1.2498 0.0918  0.1027  -0.0722 376 GLU A CG    
3103 C  CD    . GLU A 376 ? 1.7363 1.7219 1.4003 0.0937  0.0977  -0.0887 376 GLU A CD    
3104 O  OE1   . GLU A 376 ? 1.7506 1.7281 1.3862 0.1063  0.1118  -0.0906 376 GLU A OE1   
3105 O  OE2   . GLU A 376 ? 1.7316 1.7106 1.3893 0.0827  0.0803  -0.1012 376 GLU A OE2   
3106 N  N     . LEU A 377 ? 1.2523 1.2172 1.0009 0.0610  0.0703  -0.1068 377 LEU A N     
3107 C  CA    . LEU A 377 ? 1.1566 1.1165 0.9293 0.0518  0.0629  -0.1100 377 LEU A CA    
3108 C  C     . LEU A 377 ? 1.2931 1.2299 1.0598 0.0557  0.0698  -0.1217 377 LEU A C     
3109 O  O     . LEU A 377 ? 1.2604 1.1939 1.0516 0.0531  0.0713  -0.1189 377 LEU A O     
3110 C  CB    . LEU A 377 ? 1.1314 1.0941 0.9033 0.0390  0.0443  -0.1167 377 LEU A CB    
3111 C  CG    . LEU A 377 ? 1.1958 1.1779 0.9946 0.0310  0.0361  -0.1048 377 LEU A CG    
3112 C  CD1   . LEU A 377 ? 1.1216 1.1088 0.9135 0.0217  0.0202  -0.1100 377 LEU A CD1   
3113 C  CD2   . LEU A 377 ? 1.2434 1.2233 1.0700 0.0264  0.0364  -0.1016 377 LEU A CD2   
3114 N  N     . ALA A 378 ? 1.3641 1.2835 1.0971 0.0623  0.0740  -0.1348 378 ALA A N     
3115 C  CA    . ALA A 378 ? 1.3823 1.2767 1.1073 0.0676  0.0821  -0.1467 378 ALA A CA    
3116 C  C     . ALA A 378 ? 1.4394 1.3358 1.1810 0.0798  0.1018  -0.1352 378 ALA A C     
3117 O  O     . ALA A 378 ? 1.4707 1.3573 1.2316 0.0804  0.1064  -0.1355 378 ALA A O     
3118 C  CB    . ALA A 378 ? 1.3232 1.1969 1.0041 0.0723  0.0817  -0.1643 378 ALA A CB    
3119 N  N     . ARG A 379 ? 1.4451 1.3550 1.1814 0.0898  0.1136  -0.1236 379 ARG A N     
3120 C  CA    . ARG A 379 ? 1.3487 1.2651 1.1062 0.1010  0.1318  -0.1093 379 ARG A CA    
3121 C  C     . ARG A 379 ? 1.3897 1.3192 1.1897 0.0928  0.1261  -0.0969 379 ARG A C     
3122 O  O     . ARG A 379 ? 1.4381 1.3566 1.2541 0.0932  0.1293  -0.0987 379 ARG A O     
3123 C  CB    . ARG A 379 ? 1.2301 1.1637 0.9804 0.1105  0.1428  -0.0958 379 ARG A CB    
3124 C  CG    . ARG A 379 ? 1.3514 1.3021 1.1361 0.1176  0.1566  -0.0747 379 ARG A CG    
3125 C  CD    . ARG A 379 ? 1.3438 1.3142 1.1254 0.1238  0.1640  -0.0597 379 ARG A CD    
3126 N  NE    . ARG A 379 ? 1.6391 1.6275 1.4314 0.1119  0.1480  -0.0527 379 ARG A NE    
3127 C  CZ    . ARG A 379 ? 1.4439 1.4376 1.2122 0.1102  0.1416  -0.0548 379 ARG A CZ    
3128 N  NH1   . ARG A 379 ? 1.3411 1.3234 1.0700 0.1187  0.1482  -0.0645 379 ARG A NH1   
3129 N  NH2   . ARG A 379 ? 1.0227 1.0328 0.8061 0.1002  0.1283  -0.0468 379 ARG A NH2   
3130 N  N     . ARG A 380 ? 1.2655 1.2164 1.0817 0.0847  0.1162  -0.0855 380 ARG A N     
3131 C  CA    . ARG A 380 ? 1.1471 1.1119 1.0001 0.0775  0.1104  -0.0726 380 ARG A CA    
3132 C  C     . ARG A 380 ? 1.0935 1.0466 0.9603 0.0698  0.1030  -0.0793 380 ARG A C     
3133 O  O     . ARG A 380 ? 1.0115 0.9748 0.9045 0.0628  0.0963  -0.0699 380 ARG A O     
3134 C  CB    . ARG A 380 ? 1.0439 1.0269 0.9021 0.0684  0.0977  -0.0658 380 ARG A CB    
3135 C  CG    . ARG A 380 ? 0.9633 0.9590 0.8103 0.0750  0.1039  -0.0573 380 ARG A CG    
3136 C  CD    . ARG A 380 ? 0.9436 0.9565 0.8005 0.0664  0.0918  -0.0492 380 ARG A CD    
3137 N  NE    . ARG A 380 ? 0.9594 0.9838 0.8054 0.0725  0.0973  -0.0407 380 ARG A NE    
3138 C  CZ    . ARG A 380 ? 0.9168 0.9563 0.7712 0.0676  0.0899  -0.0314 380 ARG A CZ    
3139 N  NH1   . ARG A 380 ? 0.7853 0.8298 0.6570 0.0570  0.0769  -0.0303 380 ARG A NH1   
3140 N  NH2   . ARG A 380 ? 0.9979 1.0471 0.8425 0.0741  0.0964  -0.0227 380 ARG A NH2   
3141 N  N     . ARG A 381 ? 1.2523 1.1833 1.1012 0.0708  0.1038  -0.0952 381 ARG A N     
3142 C  CA    . ARG A 381 ? 1.4023 1.3207 1.2651 0.0644  0.0982  -0.1008 381 ARG A CA    
3143 C  C     . ARG A 381 ? 1.4357 1.3493 1.3203 0.0723  0.1109  -0.0927 381 ARG A C     
3144 O  O     . ARG A 381 ? 1.5108 1.4121 1.4068 0.0685  0.1081  -0.0968 381 ARG A O     
3145 C  CB    . ARG A 381 ? 1.4328 1.3279 1.2696 0.0614  0.0928  -0.1211 381 ARG A CB    
3146 C  CG    . ARG A 381 ? 1.4427 1.3424 1.2643 0.0507  0.0765  -0.1289 381 ARG A CG    
3147 C  CD    . ARG A 381 ? 1.4187 1.3347 1.2656 0.0389  0.0643  -0.1200 381 ARG A CD    
3148 N  NE    . ARG A 381 ? 1.5446 1.4683 1.3797 0.0302  0.0505  -0.1247 381 ARG A NE    
3149 C  CZ    . ARG A 381 ? 1.4408 1.3704 1.2896 0.0188  0.0380  -0.1242 381 ARG A CZ    
3150 N  NH1   . ARG A 381 ? 1.5396 1.4682 1.4121 0.0143  0.0372  -0.1193 381 ARG A NH1   
3151 N  NH2   . ARG A 381 ? 1.2054 1.1428 1.0441 0.0123  0.0265  -0.1277 381 ARG A NH2   
3152 N  N     . GLN A 382 ? 1.4547 1.3781 1.3475 0.0832  0.1246  -0.0804 382 GLN A N     
3153 C  CA    . GLN A 382 ? 1.3102 1.2305 1.2267 0.0913  0.1366  -0.0713 382 GLN A CA    
3154 C  C     . GLN A 382 ? 1.1259 1.0588 1.0755 0.0823  0.1270  -0.0585 382 GLN A C     
3155 O  O     . GLN A 382 ? 1.2150 1.1572 1.1674 0.0707  0.1124  -0.0579 382 GLN A O     
3156 C  CB    . GLN A 382 ? 1.3328 1.2639 1.2549 0.1049  0.1535  -0.0584 382 GLN A CB    
3157 C  CG    . GLN A 382 ? 1.5314 1.4856 1.4556 0.1030  0.1506  -0.0467 382 GLN A CG    
3158 C  CD    . GLN A 382 ? 1.4856 1.4375 1.3780 0.1119  0.1601  -0.0522 382 GLN A CD    
3159 O  OE1   . GLN A 382 ? 1.4783 1.4195 1.3395 0.1084  0.1531  -0.0676 382 GLN A OE1   
3160 N  NE2   . GLN A 382 ? 1.5072 1.4698 1.4082 0.1237  0.1760  -0.0385 382 GLN A NE2   
3161 N  N     . LYS A 383 ? 1.0290 0.9622 1.0036 0.0886  0.1358  -0.0476 383 LYS A N     
3162 C  CA    . LYS A 383 ? 0.9675 0.9138 0.9731 0.0818  0.1275  -0.0332 383 LYS A CA    
3163 C  C     . LYS A 383 ? 1.0243 0.9841 1.0562 0.0912  0.1386  -0.0146 383 LYS A C     
3164 O  O     . LYS A 383 ? 1.1131 1.0682 1.1421 0.1041  0.1550  -0.0137 383 LYS A O     
3165 C  CB    . LYS A 383 ? 1.0464 0.9776 1.0601 0.0770  0.1227  -0.0384 383 LYS A CB    
3166 C  CG    . LYS A 383 ? 1.0595 1.0027 1.0938 0.0659  0.1089  -0.0281 383 LYS A CG    
3167 C  CD    . LYS A 383 ? 1.2292 1.1571 1.2683 0.0607  0.1043  -0.0336 383 LYS A CD    
3168 C  CE    . LYS A 383 ? 1.3806 1.2858 1.3961 0.0612  0.1067  -0.0533 383 LYS A CE    
3169 N  NZ    . LYS A 383 ? 1.2259 1.1134 1.2514 0.0597  0.1069  -0.0566 383 LYS A NZ    
3170 N  N     . TYR A 384 ? 0.8730 0.8498 0.9308 0.0846  0.1293  0.0006  384 TYR A N     
3171 C  CA    . TYR A 384 ? 0.6913 0.6835 0.7791 0.0912  0.1363  0.0203  384 TYR A CA    
3172 C  C     . TYR A 384 ? 0.7425 0.7399 0.8573 0.0847  0.1262  0.0316  384 TYR A C     
3173 O  O     . TYR A 384 ? 0.7778 0.7705 0.8866 0.0742  0.1129  0.0256  384 TYR A O     
3174 C  CB    . TYR A 384 ? 0.7352 0.7472 0.8267 0.0899  0.1343  0.0304  384 TYR A CB    
3175 C  CG    . TYR A 384 ? 0.7563 0.7773 0.8454 0.0759  0.1155  0.0304  384 TYR A CG    
3176 C  CD1   . TYR A 384 ? 0.6568 0.6729 0.7180 0.0701  0.1089  0.0163  384 TYR A CD1   
3177 C  CD2   . TYR A 384 ? 0.6941 0.7280 0.8086 0.0688  0.1041  0.0445  384 TYR A CD2   
3178 C  CE1   . TYR A 384 ? 0.7239 0.7475 0.7836 0.0586  0.0934  0.0165  384 TYR A CE1   
3179 C  CE2   . TYR A 384 ? 0.7339 0.7735 0.8436 0.0571  0.0880  0.0435  384 TYR A CE2   
3180 C  CZ    . TYR A 384 ? 0.7494 0.7837 0.8323 0.0525  0.0836  0.0296  384 TYR A CZ    
3181 O  OH    . TYR A 384 ? 0.6292 0.6685 0.7082 0.0421  0.0690  0.0288  384 TYR A OH    
3182 N  N     . GLU A 385 ? 0.6461 0.6538 0.7910 0.0914  0.1328  0.0490  385 GLU A N     
3183 C  CA    . GLU A 385 ? 0.6446 0.6577 0.8157 0.0863  0.1232  0.0614  385 GLU A CA    
3184 C  C     . GLU A 385 ? 0.6155 0.6438 0.7920 0.0735  0.1045  0.0688  385 GLU A C     
3185 O  O     . GLU A 385 ? 0.6688 0.7098 0.8451 0.0718  0.1023  0.0731  385 GLU A O     
3186 C  CB    . GLU A 385 ? 0.7060 0.7276 0.9102 0.0972  0.1348  0.0794  385 GLU A CB    
3187 C  CG    . GLU A 385 ? 0.7261 0.7490 0.9555 0.0943  0.1272  0.0909  385 GLU A CG    
3188 C  CD    . GLU A 385 ? 0.7812 0.8109 1.0442 0.1065  0.1404  0.1081  385 GLU A CD    
3189 O  OE1   . GLU A 385 ? 0.8711 0.9014 1.1353 0.1188  0.1582  0.1090  385 GLU A OE1   
3190 O  OE2   . GLU A 385 ? 0.6816 0.7164 0.9699 0.1045  0.1334  0.1215  385 GLU A OE2   
3191 N  N     . GLY A 386 ? 0.6247 0.6507 0.8052 0.0649  0.0914  0.0702  386 GLY A N     
3192 C  CA    . GLY A 386 ? 0.6501 0.6867 0.8316 0.0532  0.0736  0.0754  386 GLY A CA    
3193 C  C     . GLY A 386 ? 0.6719 0.7193 0.8817 0.0504  0.0643  0.0937  386 GLY A C     
3194 O  O     . GLY A 386 ? 0.6867 0.7431 0.9234 0.0578  0.0714  0.1080  386 GLY A O     
3195 N  N     . GLY A 387 ? 0.7711 0.8181 0.9748 0.0401  0.0484  0.0938  387 GLY A N     
3196 C  CA    . GLY A 387 ? 0.7184 0.7751 0.9446 0.0363  0.0366  0.1106  387 GLY A CA    
3197 C  C     . GLY A 387 ? 0.7478 0.8000 0.9920 0.0425  0.0427  0.1187  387 GLY A C     
3198 O  O     . GLY A 387 ? 0.8159 0.8536 1.0505 0.0472  0.0530  0.1088  387 GLY A O     
3199 N  N     . TYR A 388 ? 0.7666 0.8313 1.0388 0.0422  0.0354  0.1376  388 TYR A N     
3200 C  CA    . TYR A 388 ? 0.5030 0.5662 0.7975 0.0482  0.0397  0.1491  388 TYR A CA    
3201 C  C     . TYR A 388 ? 0.6233 0.6819 0.9093 0.0398  0.0249  0.1513  388 TYR A C     
3202 O  O     . TYR A 388 ? 0.6419 0.7071 0.9207 0.0301  0.0077  0.1546  388 TYR A O     
3203 C  CB    . TYR A 388 ? 0.6554 0.7366 0.9883 0.0531  0.0401  0.1707  388 TYR A CB    
3204 C  CG    . TYR A 388 ? 0.6290 0.7143 0.9883 0.0551  0.0355  0.1880  388 TYR A CG    
3205 C  CD1   . TYR A 388 ? 0.4923 0.5694 0.8658 0.0665  0.0516  0.1906  388 TYR A CD1   
3206 C  CD2   . TYR A 388 ? 0.6686 0.7651 1.0381 0.0458  0.0145  0.2019  388 TYR A CD2   
3207 C  CE1   . TYR A 388 ? 0.6231 0.7044 1.0226 0.0689  0.0476  0.2078  388 TYR A CE1   
3208 C  CE2   . TYR A 388 ? 0.6022 0.7035 0.9959 0.0476  0.0093  0.2190  388 TYR A CE2   
3209 C  CZ    . TYR A 388 ? 0.6838 0.7782 1.0936 0.0593  0.0262  0.2225  388 TYR A CZ    
3210 O  OH    . TYR A 388 ? 0.7926 0.8921 1.2282 0.0617  0.0213  0.2408  388 TYR A OH    
3211 N  N     . VAL A 389 ? 0.6268 0.6730 0.9126 0.0437  0.0318  0.1493  389 VAL A N     
3212 C  CA    . VAL A 389 ? 0.7023 0.7443 0.9822 0.0374  0.0202  0.1537  389 VAL A CA    
3213 C  C     . VAL A 389 ? 0.6980 0.7409 1.0074 0.0448  0.0251  0.1698  389 VAL A C     
3214 O  O     . VAL A 389 ? 0.8610 0.8937 1.1791 0.0544  0.0417  0.1662  389 VAL A O     
3215 C  CB    . VAL A 389 ? 0.7396 0.7647 0.9897 0.0336  0.0229  0.1360  389 VAL A CB    
3216 C  CG1   . VAL A 389 ? 0.6637 0.6881 0.9026 0.0252  0.0086  0.1411  389 VAL A CG1   
3217 C  CG2   . VAL A 389 ? 0.6201 0.6429 0.8456 0.0302  0.0246  0.1186  389 VAL A CG2   
3218 N  N     . LYS A 390 ? 0.5990 0.6531 0.9231 0.0406  0.0103  0.1876  390 LYS A N     
3219 C  CA    . LYS A 390 ? 0.7236 0.7803 1.0774 0.0471  0.0129  0.2053  390 LYS A CA    
3220 C  C     . LYS A 390 ? 0.7515 0.7949 1.0925 0.0447  0.0112  0.2037  390 LYS A C     
3221 O  O     . LYS A 390 ? 0.8653 0.9029 1.1772 0.0360  0.0023  0.1944  390 LYS A O     
3222 C  CB    . LYS A 390 ? 0.8083 0.8851 1.1868 0.0437  -0.0035 0.2274  390 LYS A CB    
3223 C  CG    . LYS A 390 ? 0.8129 0.8918 1.1748 0.0326  -0.0251 0.2330  390 LYS A CG    
3224 C  CD    . LYS A 390 ? 0.7859 0.8823 1.1779 0.0313  -0.0402 0.2577  390 LYS A CD    
3225 C  CE    . LYS A 390 ? 0.7916 0.8894 1.2177 0.0419  -0.0294 0.2737  390 LYS A CE    
3226 N  NZ    . LYS A 390 ? 0.7936 0.9064 1.2431 0.0390  -0.0474 0.2983  390 LYS A NZ    
3227 N  N     . GLU A 391 ? 0.7899 0.8281 1.1540 0.0531  0.0207  0.2135  391 GLU A N     
3228 C  CA    . GLU A 391 ? 0.7868 0.8136 1.1447 0.0513  0.0190  0.2161  391 GLU A CA    
3229 C  C     . GLU A 391 ? 0.8173 0.8568 1.1761 0.0438  -0.0014 0.2336  391 GLU A C     
3230 O  O     . GLU A 391 ? 0.8122 0.8670 1.1984 0.0460  -0.0086 0.2527  391 GLU A O     
3231 C  CB    . GLU A 391 ? 0.6737 0.6906 1.0584 0.0628  0.0348  0.2228  391 GLU A CB    
3232 C  CG    . GLU A 391 ? 0.7410 0.7343 1.1097 0.0654  0.0496  0.2034  391 GLU A CG    
3233 C  CD    . GLU A 391 ? 0.9042 0.8886 1.2473 0.0556  0.0415  0.1968  391 GLU A CD    
3234 O  OE1   . GLU A 391 ? 0.8080 0.7993 1.1542 0.0512  0.0296  0.2123  391 GLU A OE1   
3235 O  OE2   . GLU A 391 ? 0.9439 0.9152 1.2636 0.0523  0.0469  0.1769  391 GLU A OE2   
3236 N  N     . PRO A 392 ? 0.8830 0.9171 1.2126 0.0350  -0.0112 0.2283  392 PRO A N     
3237 C  CA    . PRO A 392 ? 0.9930 1.0375 1.3177 0.0281  -0.0311 0.2439  392 PRO A CA    
3238 C  C     . PRO A 392 ? 0.9098 0.9580 1.2630 0.0335  -0.0322 0.2663  392 PRO A C     
3239 O  O     . PRO A 392 ? 1.0658 1.1023 1.4302 0.0399  -0.0186 0.2669  392 PRO A O     
3240 C  CB    . PRO A 392 ? 0.9052 0.9391 1.1918 0.0205  -0.0349 0.2319  392 PRO A CB    
3241 C  CG    . PRO A 392 ? 0.9211 0.9439 1.1927 0.0211  -0.0213 0.2091  392 PRO A CG    
3242 C  CD    . PRO A 392 ? 0.8475 0.8662 1.1467 0.0311  -0.0047 0.2081  392 PRO A CD    
3243 N  N     . GLU A 393 ? 0.7178 0.7822 1.0839 0.0306  -0.0494 0.2851  393 GLU A N     
3244 C  CA    . GLU A 393 ? 0.9160 0.9857 1.3047 0.0338  -0.0551 0.3085  393 GLU A CA    
3245 C  C     . GLU A 393 ? 0.9213 0.9805 1.2801 0.0287  -0.0598 0.3074  393 GLU A C     
3246 O  O     . GLU A 393 ? 0.9545 1.0190 1.2909 0.0209  -0.0779 0.3134  393 GLU A O     
3247 C  CB    . GLU A 393 ? 0.9943 1.0845 1.4019 0.0305  -0.0750 0.3284  393 GLU A CB    
3248 C  CG    . GLU A 393 ? 0.8756 0.9784 1.3123 0.0343  -0.0711 0.3298  393 GLU A CG    
3249 C  CD    . GLU A 393 ? 0.9845 1.0889 1.4641 0.0478  -0.0526 0.3408  393 GLU A CD    
3250 O  OE1   . GLU A 393 ? 1.0566 1.1532 1.5465 0.0536  -0.0455 0.3494  393 GLU A OE1   
3251 O  OE2   . GLU A 393 ? 1.0099 1.1230 1.5132 0.0531  -0.0444 0.3412  393 GLU A OE2   
3252 N  N     . ARG A 394 ? 1.0292 1.0723 1.3872 0.0333  -0.0426 0.2995  394 ARG A N     
3253 C  CA    . ARG A 394 ? 0.9207 0.9521 1.2490 0.0284  -0.0424 0.2940  394 ARG A CA    
3254 C  C     . ARG A 394 ? 1.0233 1.0613 1.3485 0.0259  -0.0569 0.3159  394 ARG A C     
3255 O  O     . ARG A 394 ? 1.0914 1.1354 1.4472 0.0314  -0.0582 0.3364  394 ARG A O     
3256 C  CB    . ARG A 394 ? 0.9260 0.9395 1.2636 0.0342  -0.0221 0.2852  394 ARG A CB    
3257 C  CG    . ARG A 394 ? 0.9324 0.9341 1.2440 0.0291  -0.0198 0.2794  394 ARG A CG    
3258 C  CD    . ARG A 394 ? 1.1428 1.1259 1.4639 0.0332  -0.0009 0.2669  394 ARG A CD    
3259 N  NE    . ARG A 394 ? 1.1576 1.1306 1.4536 0.0270  0.0019  0.2575  394 ARG A NE    
3260 C  CZ    . ARG A 394 ? 1.1405 1.0974 1.4371 0.0272  0.0152  0.2425  394 ARG A CZ    
3261 N  NH1   . ARG A 394 ? 1.2784 1.2251 1.5944 0.0335  0.0271  0.2329  394 ARG A NH1   
3262 N  NH2   . ARG A 394 ? 1.0329 0.9837 1.3098 0.0211  0.0164  0.2370  394 ARG A NH2   
3263 N  N     . GLY A 395 ? 0.9037 0.9403 1.1912 0.0181  -0.0672 0.3120  395 GLY A N     
3264 C  CA    . GLY A 395 ? 1.0500 1.0919 1.3270 0.0156  -0.0815 0.3316  395 GLY A CA    
3265 C  C     . GLY A 395 ? 1.1278 1.1748 1.3660 0.0070  -0.1004 0.3281  395 GLY A C     
3266 O  O     . GLY A 395 ? 1.1115 1.1542 1.3251 0.0026  -0.0996 0.3081  395 GLY A O     
3267 N  N     . LEU A 396 ? 1.1969 1.2521 1.4287 0.0048  -0.1180 0.3476  396 LEU A N     
3268 C  CA    . LEU A 396 ? 1.1963 1.2541 1.3887 -0.0031 -0.1379 0.3453  396 LEU A CA    
3269 C  C     . LEU A 396 ? 1.2529 1.3251 1.4621 -0.0063 -0.1579 0.3546  396 LEU A C     
3270 O  O     . LEU A 396 ? 1.1685 1.2518 1.4135 -0.0027 -0.1630 0.3753  396 LEU A O     
3271 C  CB    . LEU A 396 ? 1.3152 1.3703 1.4811 -0.0039 -0.1448 0.3598  396 LEU A CB    
3272 C  CG    . LEU A 396 ? 1.4154 1.4732 1.5414 -0.0108 -0.1685 0.3635  396 LEU A CG    
3273 C  CD1   . LEU A 396 ? 1.2585 1.3054 1.3398 -0.0114 -0.1638 0.3604  396 LEU A CD1   
3274 C  CD2   . LEU A 396 ? 1.2464 1.3175 1.3916 -0.0110 -0.1881 0.3895  396 LEU A CD2   
3275 N  N     . TRP A 397 ? 1.1756 1.2478 1.3616 -0.0132 -0.1691 0.3402  397 TRP A N     
3276 C  CA    . TRP A 397 ? 1.1231 1.2081 1.3239 -0.0180 -0.1896 0.3475  397 TRP A CA    
3277 C  C     . TRP A 397 ? 1.1194 1.2007 1.2749 -0.0271 -0.2125 0.3434  397 TRP A C     
3278 O  O     . TRP A 397 ? 1.1311 1.1990 1.2436 -0.0291 -0.2084 0.3281  397 TRP A O     
3279 C  CB    . TRP A 397 ? 0.9766 1.0651 1.2009 -0.0174 -0.1810 0.3339  397 TRP A CB    
3280 C  CG    . TRP A 397 ? 1.0087 1.1008 1.2774 -0.0079 -0.1604 0.3390  397 TRP A CG    
3281 C  CD1   . TRP A 397 ? 1.0148 1.0953 1.2852 -0.0015 -0.1363 0.3276  397 TRP A CD1   
3282 C  CD2   . TRP A 397 ? 0.8705 0.9778 1.1883 -0.0032 -0.1620 0.3572  397 TRP A CD2   
3283 N  NE1   . TRP A 397 ? 1.0110 1.0965 1.3255 0.0071  -0.1228 0.3359  397 TRP A NE1   
3284 C  CE2   . TRP A 397 ? 0.9606 1.0631 1.3054 0.0069  -0.1371 0.3546  397 TRP A CE2   
3285 C  CE3   . TRP A 397 ? 0.9979 1.1226 1.3404 -0.0066 -0.1824 0.3757  397 TRP A CE3   
3286 C  CZ2   . TRP A 397 ? 0.9530 1.0666 1.3469 0.0149  -0.1300 0.3697  397 TRP A CZ2   
3287 C  CZ3   . TRP A 397 ? 0.9362 1.0743 1.3310 0.0009  -0.1757 0.3921  397 TRP A CZ3   
3288 C  CH2   . TRP A 397 ? 0.9812 1.1136 1.4007 0.0122  -0.1488 0.3889  397 TRP A CH2   
3289 N  N     . GLU A 398 ? 1.0819 1.1748 1.2481 -0.0324 -0.2368 0.3576  398 GLU A N     
3290 C  CA    . GLU A 398 ? 1.1038 1.1920 1.2276 -0.0413 -0.2620 0.3556  398 GLU A CA    
3291 C  C     . GLU A 398 ? 1.1993 1.2950 1.3366 -0.0491 -0.2808 0.3524  398 GLU A C     
3292 O  O     . GLU A 398 ? 1.2568 1.3679 1.4435 -0.0478 -0.2813 0.3636  398 GLU A O     
3293 C  CB    . GLU A 398 ? 1.1884 1.2818 1.3046 -0.0417 -0.2790 0.3791  398 GLU A CB    
3294 C  CG    . GLU A 398 ? 1.3072 1.4185 1.4793 -0.0368 -0.2799 0.4048  398 GLU A CG    
3295 C  CD    . GLU A 398 ? 1.4111 1.5233 1.5789 -0.0319 -0.2794 0.4251  398 GLU A CD    
3296 O  OE1   . GLU A 398 ? 1.5332 1.6322 1.6712 -0.0282 -0.2637 0.4176  398 GLU A OE1   
3297 O  OE2   . GLU A 398 ? 1.2881 1.4148 1.4840 -0.0318 -0.2947 0.4498  398 GLU A OE2   
3298 N  N     . ASN A 399 ? 1.1735 1.2576 1.2669 -0.0571 -0.2957 0.3373  399 ASN A N     
3299 C  CA    . ASN A 399 ? 1.0328 1.1202 1.1329 -0.0660 -0.3150 0.3317  399 ASN A CA    
3300 C  C     . ASN A 399 ? 1.1239 1.2181 1.2630 -0.0631 -0.2975 0.3231  399 ASN A C     
3301 O  O     . ASN A 399 ? 1.1356 1.2470 1.3242 -0.0626 -0.3006 0.3377  399 ASN A O     
3302 C  CB    . ASN A 399 ? 1.0957 1.1981 1.2191 -0.0721 -0.3438 0.3550  399 ASN A CB    
3303 C  CG    . ASN A 399 ? 1.1931 1.2886 1.2745 -0.0751 -0.3631 0.3640  399 ASN A CG    
3304 O  OD1   . ASN A 399 ? 1.2054 1.2823 1.2306 -0.0778 -0.3668 0.3482  399 ASN A OD1   
3305 N  ND2   . ASN A 399 ? 1.2824 1.3929 1.3904 -0.0741 -0.3752 0.3902  399 ASN A ND2   
3306 N  N     . ILE A 400 ? 1.0469 1.1281 1.1638 -0.0609 -0.2790 0.3005  400 ILE A N     
3307 C  CA    . ILE A 400 ? 1.0366 1.1221 1.1835 -0.0571 -0.2598 0.2907  400 ILE A CA    
3308 C  C     . ILE A 400 ? 1.0567 1.1343 1.1843 -0.0645 -0.2682 0.2727  400 ILE A C     
3309 O  O     . ILE A 400 ? 1.0997 1.1618 1.1803 -0.0693 -0.2775 0.2597  400 ILE A O     
3310 C  CB    . ILE A 400 ? 0.9837 1.0612 1.1252 -0.0479 -0.2300 0.2800  400 ILE A CB    
3311 C  CG1   . ILE A 400 ? 0.9924 1.0712 1.1376 -0.0420 -0.2243 0.2955  400 ILE A CG1   
3312 C  CG2   . ILE A 400 ? 0.9613 1.0461 1.1414 -0.0422 -0.2104 0.2756  400 ILE A CG2   
3313 C  CD1   . ILE A 400 ? 1.0829 1.1499 1.2110 -0.0356 -0.2001 0.2839  400 ILE A CD1   
3314 N  N     . VAL A 401 ? 0.9279 1.0157 1.0919 -0.0648 -0.2642 0.2724  401 VAL A N     
3315 C  CA    . VAL A 401 ? 0.8270 0.9078 0.9792 -0.0703 -0.2669 0.2553  401 VAL A CA    
3316 C  C     . VAL A 401 ? 0.8649 0.9461 1.0316 -0.0625 -0.2388 0.2435  401 VAL A C     
3317 O  O     . VAL A 401 ? 0.8833 0.9751 1.0847 -0.0545 -0.2223 0.2527  401 VAL A O     
3318 C  CB    . VAL A 401 ? 0.9181 1.0105 1.0998 -0.0789 -0.2894 0.2658  401 VAL A CB    
3319 C  CG1   . VAL A 401 ? 0.8677 0.9541 1.0229 -0.0890 -0.3207 0.2711  401 VAL A CG1   
3320 C  CG2   . VAL A 401 ? 0.8656 0.9807 1.1066 -0.0740 -0.2837 0.2874  401 VAL A CG2   
3321 N  N     . TYR A 402 ? 0.7514 0.8199 0.8901 -0.0645 -0.2334 0.2231  402 TYR A N     
3322 C  CA    . TYR A 402 ? 0.7801 0.8487 0.9295 -0.0586 -0.2101 0.2109  402 TYR A CA    
3323 C  C     . TYR A 402 ? 0.8439 0.9163 1.0074 -0.0642 -0.2179 0.2070  402 TYR A C     
3324 O  O     . TYR A 402 ? 0.8931 0.9540 1.0283 -0.0712 -0.2305 0.1955  402 TYR A O     
3325 C  CB    . TYR A 402 ? 0.8708 0.9232 0.9801 -0.0555 -0.1956 0.1917  402 TYR A CB    
3326 C  CG    . TYR A 402 ? 0.6961 0.7488 0.8158 -0.0496 -0.1727 0.1797  402 TYR A CG    
3327 C  CD1   . TYR A 402 ? 0.7940 0.8554 0.9449 -0.0416 -0.1551 0.1863  402 TYR A CD1   
3328 C  CD2   . TYR A 402 ? 0.8786 0.9221 0.9761 -0.0516 -0.1691 0.1620  402 TYR A CD2   
3329 C  CE1   . TYR A 402 ? 0.7624 0.8229 0.9193 -0.0362 -0.1354 0.1748  402 TYR A CE1   
3330 C  CE2   . TYR A 402 ? 0.9924 1.0367 1.0983 -0.0464 -0.1495 0.1519  402 TYR A CE2   
3331 C  CZ    . TYR A 402 ? 0.9215 0.9740 1.0557 -0.0389 -0.1332 0.1580  402 TYR A CZ    
3332 O  OH    . TYR A 402 ? 1.0997 1.1518 1.2387 -0.0338 -0.1149 0.1473  402 TYR A OH    
3333 N  N     . LEU A 403 ? 0.7493 0.8374 0.9569 -0.0606 -0.2098 0.2172  403 LEU A N     
3334 C  CA    . LEU A 403 ? 0.7304 0.8242 0.9570 -0.0646 -0.2132 0.2156  403 LEU A CA    
3335 C  C     . LEU A 403 ? 0.7363 0.8278 0.9622 -0.0571 -0.1880 0.2020  403 LEU A C     
3336 O  O     . LEU A 403 ? 0.7008 0.7957 0.9380 -0.0477 -0.1678 0.2031  403 LEU A O     
3337 C  CB    . LEU A 403 ? 0.6836 0.7982 0.9615 -0.0653 -0.2209 0.2380  403 LEU A CB    
3338 C  CG    . LEU A 403 ? 0.6150 0.7354 0.9002 -0.0717 -0.2455 0.2551  403 LEU A CG    
3339 C  CD1   . LEU A 403 ? 0.7507 0.8940 1.0924 -0.0719 -0.2513 0.2785  403 LEU A CD1   
3340 C  CD2   . LEU A 403 ? 0.7333 0.8395 0.9827 -0.0838 -0.2715 0.2463  403 LEU A CD2   
3341 N  N     . ASP A 404 ? 0.6677 0.7523 0.8795 -0.0614 -0.1897 0.1891  404 ASP A N     
3342 C  CA    . ASP A 404 ? 0.7118 0.7928 0.9171 -0.0551 -0.1680 0.1751  404 ASP A CA    
3343 C  C     . ASP A 404 ? 0.7689 0.8543 0.9887 -0.0590 -0.1709 0.1738  404 ASP A C     
3344 O  O     . ASP A 404 ? 0.8231 0.9064 1.0423 -0.0683 -0.1913 0.1762  404 ASP A O     
3345 C  CB    . ASP A 404 ? 0.7830 0.8462 0.9428 -0.0547 -0.1625 0.1560  404 ASP A CB    
3346 C  CG    . ASP A 404 ? 0.8984 0.9599 1.0547 -0.0461 -0.1379 0.1452  404 ASP A CG    
3347 O  OD1   . ASP A 404 ? 1.0205 1.0842 1.1842 -0.0395 -0.1255 0.1488  404 ASP A OD1   
3348 O  OD2   . ASP A 404 ? 0.9651 1.0227 1.1118 -0.0462 -0.1318 0.1335  404 ASP A OD2   
3349 N  N     . PHE A 405 ? 0.6700 0.7606 0.9018 -0.0517 -0.1505 0.1699  405 PHE A N     
3350 C  CA    . PHE A 405 ? 0.7858 0.8814 1.0318 -0.0537 -0.1494 0.1694  405 PHE A CA    
3351 C  C     . PHE A 405 ? 0.8735 0.9531 1.0835 -0.0575 -0.1513 0.1505  405 PHE A C     
3352 O  O     . PHE A 405 ? 0.8808 0.9484 1.0587 -0.0547 -0.1437 0.1364  405 PHE A O     
3353 C  CB    . PHE A 405 ? 0.8344 0.9412 1.1039 -0.0433 -0.1258 0.1730  405 PHE A CB    
3354 C  CG    . PHE A 405 ? 0.7511 0.8767 1.0662 -0.0400 -0.1244 0.1944  405 PHE A CG    
3355 C  CD1   . PHE A 405 ? 0.7012 0.8387 1.0466 -0.0462 -0.1367 0.2080  405 PHE A CD1   
3356 C  CD2   . PHE A 405 ? 0.6901 0.8215 1.0198 -0.0306 -0.1106 0.2016  405 PHE A CD2   
3357 C  CE1   . PHE A 405 ? 0.7762 0.9329 1.1669 -0.0428 -0.1346 0.2294  405 PHE A CE1   
3358 C  CE2   . PHE A 405 ? 0.6889 0.8380 1.0622 -0.0264 -0.1078 0.2222  405 PHE A CE2   
3359 C  CZ    . PHE A 405 ? 0.5326 0.6954 0.9372 -0.0324 -0.1196 0.2366  405 PHE A CZ    
3360 N  N     . ARG A 406 ? 0.8133 0.8931 1.0314 -0.0639 -0.1613 0.1511  406 ARG A N     
3361 C  CA    . ARG A 406 ? 0.8152 0.8805 1.0043 -0.0668 -0.1621 0.1346  406 ARG A CA    
3362 C  C     . ARG A 406 ? 0.8664 0.9366 1.0595 -0.0589 -0.1401 0.1290  406 ARG A C     
3363 O  O     . ARG A 406 ? 0.8823 0.9653 1.1052 -0.0572 -0.1348 0.1391  406 ARG A O     
3364 C  CB    . ARG A 406 ? 0.8175 0.8790 1.0142 -0.0773 -0.1829 0.1378  406 ARG A CB    
3365 C  CG    . ARG A 406 ? 1.0508 1.1002 1.2280 -0.0787 -0.1802 0.1236  406 ARG A CG    
3366 C  CD    . ARG A 406 ? 1.1695 1.2057 1.3391 -0.0899 -0.2040 0.1212  406 ARG A CD    
3367 N  NE    . ARG A 406 ? 1.2947 1.3428 1.5035 -0.0973 -0.2192 0.1387  406 ARG A NE    
3368 C  CZ    . ARG A 406 ? 1.3149 1.3806 1.5634 -0.0956 -0.2112 0.1521  406 ARG A CZ    
3369 N  NH1   . ARG A 406 ? 1.1287 1.2011 1.3809 -0.0867 -0.1886 0.1493  406 ARG A NH1   
3370 N  NH2   . ARG A 406 ? 1.0713 1.1484 1.3569 -0.1030 -0.2267 0.1694  406 ARG A NH2   
3371 N  N     . SER A 407 ? 0.8513 0.9117 1.0143 -0.0540 -0.1279 0.1138  407 SER A N     
3372 C  CA    . SER A 407 ? 0.8072 0.8702 0.9678 -0.0469 -0.1087 0.1065  407 SER A CA    
3373 C  C     . SER A 407 ? 0.7790 0.8584 0.9722 -0.0400 -0.0953 0.1189  407 SER A C     
3374 O  O     . SER A 407 ? 0.7506 0.8381 0.9612 -0.0391 -0.0909 0.1242  407 SER A O     
3375 C  CB    . SER A 407 ? 0.7878 0.8449 0.9401 -0.0507 -0.1126 0.0995  407 SER A CB    
3376 O  OG    . SER A 407 ? 0.9683 1.0086 1.0875 -0.0547 -0.1210 0.0861  407 SER A OG    
3377 N  N     . LEU A 408 ? 0.6931 0.7769 0.8946 -0.0347 -0.0880 0.1242  408 LEU A N     
3378 C  CA    . LEU A 408 ? 0.7028 0.8017 0.9380 -0.0279 -0.0770 0.1385  408 LEU A CA    
3379 C  C     . LEU A 408 ? 0.6658 0.7691 0.9027 -0.0203 -0.0583 0.1346  408 LEU A C     
3380 O  O     . LEU A 408 ? 0.8145 0.9304 1.0782 -0.0180 -0.0538 0.1467  408 LEU A O     
3381 C  CB    . LEU A 408 ? 0.6810 0.7803 0.9202 -0.0225 -0.0708 0.1422  408 LEU A CB    
3382 C  CG    . LEU A 408 ? 0.7466 0.8605 1.0233 -0.0156 -0.0624 0.1597  408 LEU A CG    
3383 C  CD1   . LEU A 408 ? 0.7559 0.8717 1.0346 -0.0040 -0.0384 0.1556  408 LEU A CD1   
3384 C  CD2   . LEU A 408 ? 0.7057 0.8337 1.0153 -0.0206 -0.0736 0.1765  408 LEU A CD2   
3385 N  N     . TYR A 409 ? 0.6906 0.7841 0.8992 -0.0163 -0.0475 0.1187  409 TYR A N     
3386 C  CA    . TYR A 409 ? 0.6098 0.7067 0.8166 -0.0087 -0.0302 0.1146  409 TYR A CA    
3387 C  C     . TYR A 409 ? 0.5591 0.6590 0.7666 -0.0124 -0.0341 0.1150  409 TYR A C     
3388 O  O     . TYR A 409 ? 0.6850 0.7959 0.9114 -0.0076 -0.0246 0.1242  409 TYR A O     
3389 C  CB    . TYR A 409 ? 0.5829 0.6687 0.7608 -0.0043 -0.0196 0.0980  409 TYR A CB    
3390 C  CG    . TYR A 409 ? 0.5326 0.6166 0.7152 0.0025  -0.0092 0.0989  409 TYR A CG    
3391 C  CD1   . TYR A 409 ? 0.5266 0.6168 0.7337 0.0032  -0.0129 0.1128  409 TYR A CD1   
3392 C  CD2   . TYR A 409 ? 0.6214 0.6969 0.7850 0.0081  0.0034  0.0860  409 TYR A CD2   
3393 C  CE1   . TYR A 409 ? 0.6226 0.7101 0.8354 0.0100  -0.0029 0.1141  409 TYR A CE1   
3394 C  CE2   . TYR A 409 ? 0.6680 0.7393 0.8362 0.0142  0.0127  0.0861  409 TYR A CE2   
3395 C  CZ    . TYR A 409 ? 0.6405 0.7175 0.8334 0.0156  0.0101  0.1003  409 TYR A CZ    
3396 O  OH    . TYR A 409 ? 0.5621 0.6340 0.7609 0.0222  0.0199  0.1010  409 TYR A OH    
3397 N  N     . PRO A 410 ? 0.7669 0.8573 0.9554 -0.0201 -0.0466 0.1061  410 PRO A N     
3398 C  CA    . PRO A 410 ? 0.6754 0.7681 0.8683 -0.0234 -0.0502 0.1080  410 PRO A CA    
3399 C  C     . PRO A 410 ? 0.5824 0.6864 0.8100 -0.0276 -0.0588 0.1258  410 PRO A C     
3400 O  O     . PRO A 410 ? 0.5492 0.6607 0.7911 -0.0267 -0.0547 0.1328  410 PRO A O     
3401 C  CB    . PRO A 410 ? 0.5770 0.6548 0.7430 -0.0306 -0.0629 0.0949  410 PRO A CB    
3402 C  CG    . PRO A 410 ? 0.5302 0.5996 0.6729 -0.0280 -0.0587 0.0837  410 PRO A CG    
3403 C  CD    . PRO A 410 ? 0.7251 0.8016 0.8862 -0.0249 -0.0557 0.0937  410 PRO A CD    
3404 N  N     . SER A 411 ? 0.5963 0.7024 0.8391 -0.0322 -0.0711 0.1346  411 SER A N     
3405 C  CA    . SER A 411 ? 0.6651 0.7837 0.9452 -0.0366 -0.0801 0.1534  411 SER A CA    
3406 C  C     . SER A 411 ? 0.6135 0.7497 0.9232 -0.0270 -0.0619 0.1677  411 SER A C     
3407 O  O     . SER A 411 ? 0.6086 0.7571 0.9487 -0.0284 -0.0627 0.1827  411 SER A O     
3408 C  CB    . SER A 411 ? 0.6767 0.7941 0.9655 -0.0438 -0.0984 0.1598  411 SER A CB    
3409 O  OG    . SER A 411 ? 0.7260 0.8264 0.9862 -0.0525 -0.1154 0.1473  411 SER A OG    
3410 N  N     . ILE A 412 ? 0.5826 0.7193 0.8840 -0.0169 -0.0450 0.1635  412 ILE A N     
3411 C  CA    . ILE A 412 ? 0.4922 0.6428 0.8164 -0.0058 -0.0252 0.1751  412 ILE A CA    
3412 C  C     . ILE A 412 ? 0.5777 0.7309 0.8949 -0.0012 -0.0125 0.1727  412 ILE A C     
3413 O  O     . ILE A 412 ? 0.5447 0.7124 0.8894 0.0029  -0.0040 0.1882  412 ILE A O     
3414 C  CB    . ILE A 412 ? 0.5519 0.6981 0.8649 0.0039  -0.0108 0.1689  412 ILE A CB    
3415 C  CG1   . ILE A 412 ? 0.4158 0.5652 0.7484 0.0016  -0.0205 0.1789  412 ILE A CG1   
3416 C  CG2   . ILE A 412 ? 0.4743 0.6291 0.7974 0.0173  0.0131  0.1744  412 ILE A CG2   
3417 C  CD1   . ILE A 412 ? 0.5575 0.7004 0.8798 0.0102  -0.0078 0.1728  412 ILE A CD1   
3418 N  N     . ILE A 413 ? 0.5729 0.7132 0.8542 -0.0016 -0.0109 0.1544  413 ILE A N     
3419 C  CA    . ILE A 413 ? 0.5077 0.6501 0.7796 0.0024  -0.0005 0.1519  413 ILE A CA    
3420 C  C     . ILE A 413 ? 0.5233 0.6735 0.8190 -0.0048 -0.0106 0.1648  413 ILE A C     
3421 O  O     . ILE A 413 ? 0.4742 0.6351 0.7841 0.0002  0.0005  0.1752  413 ILE A O     
3422 C  CB    . ILE A 413 ? 0.5515 0.6789 0.7832 0.0013  -0.0011 0.1309  413 ILE A CB    
3423 C  CG1   . ILE A 413 ? 0.5910 0.7140 0.8021 0.0112  0.0153  0.1204  413 ILE A CG1   
3424 C  CG2   . ILE A 413 ? 0.4540 0.5822 0.6791 0.0000  -0.0006 0.1299  413 ILE A CG2   
3425 C  CD1   . ILE A 413 ? 0.6810 0.7890 0.8597 0.0080  0.0103  0.1014  413 ILE A CD1   
3426 N  N     . ILE A 414 ? 0.5209 0.6648 0.8210 -0.0165 -0.0318 0.1646  414 ILE A N     
3427 C  CA    . ILE A 414 ? 0.5397 0.6878 0.8625 -0.0249 -0.0441 0.1756  414 ILE A CA    
3428 C  C     . ILE A 414 ? 0.5808 0.7479 0.9494 -0.0241 -0.0424 0.1992  414 ILE A C     
3429 O  O     . ILE A 414 ? 0.5586 0.7370 0.9506 -0.0231 -0.0368 0.2127  414 ILE A O     
3430 C  CB    . ILE A 414 ? 0.6051 0.7380 0.9157 -0.0374 -0.0680 0.1668  414 ILE A CB    
3431 C  CG1   . ILE A 414 ? 0.5184 0.6342 0.7873 -0.0373 -0.0675 0.1457  414 ILE A CG1   
3432 C  CG2   . ILE A 414 ? 0.4478 0.5837 0.7862 -0.0472 -0.0831 0.1793  414 ILE A CG2   
3433 C  CD1   . ILE A 414 ? 0.4488 0.5476 0.6982 -0.0467 -0.0871 0.1345  414 ILE A CD1   
3434 N  N     . THR A 415 ? 0.6127 0.7844 0.9965 -0.0243 -0.0468 0.2058  415 THR A N     
3435 C  CA    . THR A 415 ? 0.6048 0.7956 1.0362 -0.0245 -0.0476 0.2297  415 THR A CA    
3436 C  C     . THR A 415 ? 0.6056 0.8124 1.0547 -0.0111 -0.0218 0.2420  415 THR A C     
3437 O  O     . THR A 415 ? 0.5912 0.8143 1.0782 -0.0115 -0.0196 0.2622  415 THR A O     
3438 C  CB    . THR A 415 ? 0.5652 0.7579 1.0072 -0.0256 -0.0557 0.2341  415 THR A CB    
3439 O  OG1   . THR A 415 ? 0.6478 0.8239 1.0662 -0.0368 -0.0781 0.2211  415 THR A OG1   
3440 C  CG2   . THR A 415 ? 0.4697 0.6829 0.9647 -0.0279 -0.0608 0.2602  415 THR A CG2   
3441 N  N     . HIS A 416 ? 0.5226 0.7246 0.9445 0.0010  -0.0020 0.2304  416 HIS A N     
3442 C  CA    . HIS A 416 ? 0.4995 0.7140 0.9320 0.0154  0.0239  0.2401  416 HIS A CA    
3443 C  C     . HIS A 416 ? 0.5211 0.7318 0.9275 0.0207  0.0368  0.2317  416 HIS A C     
3444 O  O     . HIS A 416 ? 0.5758 0.7935 0.9803 0.0338  0.0594  0.2360  416 HIS A O     
3445 C  CB    . HIS A 416 ? 0.5616 0.7727 0.9835 0.0263  0.0379  0.2342  416 HIS A CB    
3446 C  CG    . HIS A 416 ? 0.5455 0.7637 0.9980 0.0235  0.0286  0.2465  416 HIS A CG    
3447 N  ND1   . HIS A 416 ? 0.4922 0.7299 0.9936 0.0218  0.0253  0.2713  416 HIS A ND1   
3448 C  CD2   . HIS A 416 ? 0.4773 0.6863 0.9197 0.0220  0.0211  0.2386  416 HIS A CD2   
3449 C  CE1   . HIS A 416 ? 0.4120 0.6526 0.9319 0.0193  0.0156  0.2780  416 HIS A CE1   
3450 N  NE2   . HIS A 416 ? 0.4431 0.6662 0.9271 0.0196  0.0132  0.2585  416 HIS A NE2   
3451 N  N     . ASN A 417 ? 0.6444 0.8440 1.0301 0.0114  0.0231  0.2202  417 ASN A N     
3452 C  CA    . ASN A 417 ? 0.6221 0.8185 0.9846 0.0152  0.0326  0.2135  417 ASN A CA    
3453 C  C     . ASN A 417 ? 0.5619 0.7524 0.8903 0.0279  0.0521  0.1998  417 ASN A C     
3454 O  O     . ASN A 417 ? 0.5050 0.7020 0.8278 0.0379  0.0700  0.2042  417 ASN A O     
3455 C  CB    . ASN A 417 ? 0.4995 0.7128 0.8943 0.0171  0.0399  0.2350  417 ASN A CB    
3456 C  CG    . ASN A 417 ? 0.5125 0.7204 0.8969 0.0107  0.0323  0.2317  417 ASN A CG    
3457 O  OD1   . ASN A 417 ? 0.5108 0.7057 0.8856 -0.0007 0.0127  0.2214  417 ASN A OD1   
3458 N  ND2   . ASN A 417 ? 0.5885 0.8056 0.9739 0.0186  0.0485  0.2407  417 ASN A ND2   
3459 N  N     . VAL A 418 ? 0.4804 0.6577 0.7850 0.0273  0.0480  0.1831  418 VAL A N     
3460 C  CA    . VAL A 418 ? 0.5656 0.7345 0.8379 0.0376  0.0636  0.1685  418 VAL A CA    
3461 C  C     . VAL A 418 ? 0.6352 0.7939 0.8721 0.0356  0.0614  0.1525  418 VAL A C     
3462 O  O     . VAL A 418 ? 0.6083 0.7568 0.8316 0.0261  0.0456  0.1414  418 VAL A O     
3463 C  CB    . VAL A 418 ? 0.5714 0.7303 0.8358 0.0372  0.0598  0.1585  418 VAL A CB    
3464 C  CG1   . VAL A 418 ? 0.6268 0.7768 0.8630 0.0483  0.0768  0.1452  418 VAL A CG1   
3465 C  CG2   . VAL A 418 ? 0.5784 0.7484 0.8815 0.0372  0.0579  0.1762  418 VAL A CG2   
3466 N  N     . SER A 419 ? 0.5452 0.7068 0.7668 0.0453  0.0776  0.1519  419 SER A N     
3467 C  CA    . SER A 419 ? 0.5526 0.7072 0.7428 0.0445  0.0765  0.1393  419 SER A CA    
3468 C  C     . SER A 419 ? 0.6992 0.8556 0.8692 0.0576  0.0966  0.1376  419 SER A C     
3469 O  O     . SER A 419 ? 0.6899 0.8569 0.8770 0.0667  0.1117  0.1519  419 SER A O     
3470 C  CB    . SER A 419 ? 0.5878 0.7482 0.7916 0.0370  0.0665  0.1486  419 SER A CB    
3471 O  OG    . SER A 419 ? 0.7101 0.8606 0.8862 0.0326  0.0587  0.1343  419 SER A OG    
3472 N  N     . PRO A 420 ? 0.8015 0.9477 0.9351 0.0591  0.0974  0.1209  420 PRO A N     
3473 C  CA    . PRO A 420 ? 0.7550 0.9015 0.8649 0.0713  0.1150  0.1185  420 PRO A CA    
3474 C  C     . PRO A 420 ? 0.6943 0.8555 0.8168 0.0769  0.1251  0.1367  420 PRO A C     
3475 O  O     . PRO A 420 ? 0.7531 0.9182 0.8665 0.0893  0.1436  0.1416  420 PRO A O     
3476 C  CB    . PRO A 420 ? 0.5996 0.7343 0.6728 0.0679  0.1074  0.0990  420 PRO A CB    
3477 C  CG    . PRO A 420 ? 0.6405 0.7665 0.7175 0.0567  0.0905  0.0890  420 PRO A CG    
3478 C  CD    . PRO A 420 ? 0.5995 0.7339 0.7121 0.0501  0.0822  0.1041  420 PRO A CD    
3479 N  N     . ASP A 421 ? 0.6678 0.8365 0.8107 0.0683  0.1139  0.1472  421 ASP A N     
3480 C  CA    . ASP A 421 ? 0.7565 0.9393 0.9150 0.0720  0.1219  0.1662  421 ASP A CA    
3481 C  C     . ASP A 421 ? 0.7726 0.9700 0.9732 0.0746  0.1295  0.1884  421 ASP A C     
3482 O  O     . ASP A 421 ? 0.8042 1.0151 1.0226 0.0782  0.1379  0.2069  421 ASP A O     
3483 C  CB    . ASP A 421 ? 0.5107 0.6932 0.6740 0.0613  0.1059  0.1674  421 ASP A CB    
3484 C  CG    . ASP A 421 ? 0.5949 0.7702 0.7745 0.0481  0.0859  0.1622  421 ASP A CG    
3485 O  OD1   . ASP A 421 ? 0.6131 0.7756 0.7719 0.0446  0.0781  0.1440  421 ASP A OD1   
3486 O  OD2   . ASP A 421 ? 0.7294 0.9112 0.9422 0.0413  0.0780  0.1765  421 ASP A OD2   
3487 N  N     . THR A 422 ? 0.5860 0.7822 0.8052 0.0728  0.1265  0.1885  422 THR A N     
3488 C  CA    . THR A 422 ? 0.6955 0.9067 0.9572 0.0756  0.1336  0.2104  422 THR A CA    
3489 C  C     . THR A 422 ? 0.8170 1.0287 1.0770 0.0887  0.1522  0.2107  422 THR A C     
3490 O  O     . THR A 422 ? 0.7798 1.0048 1.0768 0.0925  0.1596  0.2294  422 THR A O     
3491 C  CB    . THR A 422 ? 0.6379 0.8498 0.9317 0.0616  0.1124  0.2152  422 THR A CB    
3492 O  OG1   . THR A 422 ? 0.6472 0.8456 0.9256 0.0584  0.1040  0.1980  422 THR A OG1   
3493 C  CG2   . THR A 422 ? 0.4769 0.6856 0.7721 0.0491  0.0943  0.2141  422 THR A CG2   
3494 N  N     . LEU A 423 ? 0.7276 0.9249 0.9473 0.0958  0.1597  0.1911  423 LEU A N     
3495 C  CA    . LEU A 423 ? 0.6928 0.8859 0.9076 0.1081  0.1765  0.1883  423 LEU A CA    
3496 C  C     . LEU A 423 ? 0.8164 1.0189 1.0282 0.1244  0.2022  0.2007  423 LEU A C     
3497 O  O     . LEU A 423 ? 0.8798 1.0791 1.0593 0.1295  0.2092  0.1950  423 LEU A O     
3498 C  CB    . LEU A 423 ? 0.6999 0.8716 0.8727 0.1083  0.1731  0.1616  423 LEU A CB    
3499 C  CG    . LEU A 423 ? 0.8774 1.0392 1.0338 0.1223  0.1918  0.1539  423 LEU A CG    
3500 C  CD1   . LEU A 423 ? 0.6758 0.8401 0.8657 0.1226  0.1919  0.1617  423 LEU A CD1   
3501 C  CD2   . LEU A 423 ? 0.6414 0.7819 0.7517 0.1215  0.1876  0.1274  423 LEU A CD2   
3502 N  N     . ASN A 424 ? 0.7288 0.9433 0.9742 0.1329  0.2164  0.2187  424 ASN A N     
3503 C  CA    . ASN A 424 ? 0.6171 0.8394 0.8598 0.1511  0.2445  0.2306  424 ASN A CA    
3504 C  C     . ASN A 424 ? 0.6556 0.8906 0.8965 0.1530  0.2507  0.2442  424 ASN A C     
3505 O  O     . ASN A 424 ? 0.8139 1.0465 1.0233 0.1661  0.2694  0.2422  424 ASN A O     
3506 C  CB    . ASN A 424 ? 0.6881 0.8902 0.8832 0.1637  0.2589  0.2092  424 ASN A CB    
3507 C  CG    . ASN A 424 ? 0.8525 1.0423 1.0529 0.1640  0.2565  0.1986  424 ASN A CG    
3508 O  OD1   . ASN A 424 ? 0.8652 1.0654 1.1085 0.1598  0.2511  0.2123  424 ASN A OD1   
3509 N  ND2   . ASN A 424 ? 1.0280 1.1954 1.1853 0.1687  0.2596  0.1746  424 ASN A ND2   
3510 N  N     . ARG A 425 ? 0.7263 0.9740 1.0001 0.1398  0.2346  0.2582  425 ARG A N     
3511 C  CA    . ARG A 425 ? 0.8083 1.0684 1.0858 0.1402  0.2388  0.2730  425 ARG A CA    
3512 C  C     . ARG A 425 ? 0.8201 1.1006 1.1292 0.1535  0.2632  0.3007  425 ARG A C     
3513 O  O     . ARG A 425 ? 1.0230 1.3162 1.3781 0.1531  0.2649  0.3175  425 ARG A O     
3514 C  CB    . ARG A 425 ? 0.8671 1.1317 1.1712 0.1217  0.2136  0.2787  425 ARG A CB    
3515 C  CG    . ARG A 425 ? 0.8472 1.0930 1.1199 0.1094  0.1913  0.2532  425 ARG A CG    
3516 C  CD    . ARG A 425 ? 1.2190 1.4656 1.4824 0.1024  0.1818  0.2547  425 ARG A CD    
3517 N  NE    . ARG A 425 ? 1.2204 1.4660 1.4460 0.1142  0.1978  0.2514  425 ARG A NE    
3518 C  CZ    . ARG A 425 ? 1.1837 1.4137 1.3609 0.1185  0.1991  0.2287  425 ARG A CZ    
3519 N  NH1   . ARG A 425 ? 1.1783 1.3927 1.3399 0.1123  0.1866  0.2073  425 ARG A NH1   
3520 N  NH2   . ARG A 425 ? 1.3357 1.5660 1.4798 0.1290  0.2127  0.2281  425 ARG A NH2   
3521 N  N     . GLU A 426 ? 0.9174 1.2020 1.2024 0.1656  0.2819  0.3064  426 GLU A N     
3522 C  CA    . GLU A 426 ? 0.9855 1.2903 1.2979 0.1796  0.3075  0.3340  426 GLU A CA    
3523 C  C     . GLU A 426 ? 0.8950 1.2213 1.2623 0.1688  0.2985  0.3615  426 GLU A C     
3524 O  O     . GLU A 426 ? 0.8928 1.2165 1.2628 0.1535  0.2764  0.3582  426 GLU A O     
3525 C  CB    . GLU A 426 ? 1.0883 1.3899 1.3541 0.1957  0.3298  0.3318  426 GLU A CB    
3526 C  CG    . GLU A 426 ? 1.1772 1.4535 1.3803 0.2024  0.3321  0.3005  426 GLU A CG    
3527 C  CD    . GLU A 426 ? 1.3620 1.6356 1.5329 0.2252  0.3637  0.3020  426 GLU A CD    
3528 O  OE1   . GLU A 426 ? 1.5005 1.7876 1.7030 0.2373  0.3851  0.3219  426 GLU A OE1   
3529 O  OE2   . GLU A 426 ? 1.2909 1.5489 1.4048 0.2313  0.3672  0.2836  426 GLU A OE2   
3530 N  N     . GLY A 427 ? 0.7938 1.1411 1.2062 0.1772  0.3160  0.3893  427 GLY A N     
3531 C  CA    . GLY A 427 ? 0.7541 1.1230 1.2239 0.1672  0.3084  0.4178  427 GLY A CA    
3532 C  C     . GLY A 427 ? 0.7868 1.1546 1.2939 0.1464  0.2775  0.4163  427 GLY A C     
3533 O  O     . GLY A 427 ? 0.7849 1.1622 1.3263 0.1331  0.2622  0.4311  427 GLY A O     
3534 N  N     A CYS A 428 ? 0.7606 1.1159 1.2607 0.1431  0.2672  0.3986  428 CYS A N     
3535 N  N     B CYS A 428 ? 0.7644 1.1199 1.2648 0.1435  0.2677  0.3990  428 CYS A N     
3536 C  CA    A CYS A 428 ? 0.7198 1.0725 1.2498 0.1238  0.2372  0.3959  428 CYS A CA    
3537 C  CA    B CYS A 428 ? 0.7262 1.0793 1.2568 0.1245  0.2382  0.3963  428 CYS A CA    
3538 C  C     A CYS A 428 ? 0.7501 1.1263 1.3484 0.1211  0.2373  0.4261  428 CYS A C     
3539 C  C     B CYS A 428 ? 0.7490 1.1260 1.3486 0.1213  0.2380  0.4272  428 CYS A C     
3540 O  O     A CYS A 428 ? 0.6560 1.0461 1.2748 0.1359  0.2608  0.4422  428 CYS A O     
3541 O  O     B CYS A 428 ? 0.6522 1.0442 1.2742 0.1361  0.2618  0.4448  428 CYS A O     
3542 C  CB    A CYS A 428 ? 0.6601 0.9924 1.1596 0.1218  0.2269  0.3685  428 CYS A CB    
3543 C  CB    B CYS A 428 ? 0.6609 0.9948 1.1632 0.1238  0.2299  0.3704  428 CYS A CB    
3544 S  SG    A CYS A 428 ? 0.7743 1.1056 1.2650 0.1425  0.2545  0.3665  428 CYS A SG    
3545 S  SG    B CYS A 428 ? 0.6605 0.9903 1.1943 0.1025  0.1953  0.3666  428 CYS A SG    
3546 N  N     . GLY A 429 ? 0.7624 1.1423 1.3961 0.1021  0.2107  0.4339  429 GLY A N     
3547 C  CA    . GLY A 429 ? 0.5584 0.9603 1.2596 0.0960  0.2052  0.4625  429 GLY A CA    
3548 C  C     . GLY A 429 ? 0.4702 0.8677 1.1891 0.0867  0.1853  0.4560  429 GLY A C     
3549 O  O     . GLY A 429 ? 0.5676 0.9832 1.3342 0.0894  0.1898  0.4771  429 GLY A O     
3550 N  N     . GLU A 430 ? 0.4713 0.8455 1.1526 0.0760  0.1635  0.4280  430 GLU A N     
3551 C  CA    . GLU A 430 ? 0.4762 0.8434 1.1656 0.0674  0.1440  0.4191  430 GLU A CA    
3552 C  C     . GLU A 430 ? 0.6007 0.9432 1.2297 0.0715  0.1443  0.3865  430 GLU A C     
3553 O  O     . GLU A 430 ? 0.6818 1.0067 1.2722 0.0641  0.1322  0.3660  430 GLU A O     
3554 C  CB    . GLU A 430 ? 0.4569 0.8213 1.1714 0.0452  0.1097  0.4214  430 GLU A CB    
3555 C  CG    . GLU A 430 ? 0.6092 0.9665 1.3300 0.0359  0.0881  0.4131  430 GLU A CG    
3556 C  CD    . GLU A 430 ? 0.8231 1.1728 1.5578 0.0141  0.0534  0.4110  430 GLU A CD    
3557 O  OE1   . GLU A 430 ? 0.7432 1.0893 1.4770 0.0062  0.0458  0.4119  430 GLU A OE1   
3558 O  OE2   . GLU A 430 ? 0.9336 1.2797 1.6783 0.0052  0.0335  0.4082  430 GLU A OE2   
3559 N  N     . TYR A 431 ? 0.4895 0.8307 1.1123 0.0834  0.1582  0.3824  431 TYR A N     
3560 C  CA    . TYR A 431 ? 0.5731 0.8912 1.1434 0.0871  0.1586  0.3530  431 TYR A CA    
3561 C  C     . TYR A 431 ? 0.5652 0.8800 1.1499 0.0832  0.1466  0.3502  431 TYR A C     
3562 O  O     . TYR A 431 ? 0.5517 0.8840 1.1852 0.0831  0.1458  0.3722  431 TYR A O     
3563 C  CB    . TYR A 431 ? 0.6348 0.9484 1.1709 0.1075  0.1898  0.3459  431 TYR A CB    
3564 C  CG    . TYR A 431 ? 0.6929 1.0216 1.2584 0.1243  0.2153  0.3648  431 TYR A CG    
3565 C  CD1   . TYR A 431 ? 0.6113 0.9360 1.1848 0.1290  0.2170  0.3615  431 TYR A CD1   
3566 C  CD2   . TYR A 431 ? 0.7950 1.1421 1.3808 0.1364  0.2387  0.3869  431 TYR A CD2   
3567 C  CE1   . TYR A 431 ? 0.7880 1.1259 1.3895 0.1455  0.2415  0.3792  431 TYR A CE1   
3568 C  CE2   . TYR A 431 ? 0.7775 1.1385 1.3905 0.1531  0.2640  0.4049  431 TYR A CE2   
3569 C  CZ    . TYR A 431 ? 0.8583 1.2144 1.4795 0.1578  0.2653  0.4007  431 TYR A CZ    
3570 O  OH    . TYR A 431 ? 0.6151 0.9845 1.2647 0.1755  0.2914  0.4188  431 TYR A OH    
3571 N  N     . ASP A 432 ? 0.5617 0.8546 1.1044 0.0798  0.1370  0.3239  432 ASP A N     
3572 C  CA    . ASP A 432 ? 0.4939 0.7804 1.0408 0.0775  0.1275  0.3181  432 ASP A CA    
3573 C  C     . ASP A 432 ? 0.4534 0.7251 0.9630 0.0922  0.1474  0.3005  432 ASP A C     
3574 O  O     . ASP A 432 ? 0.6695 0.9259 1.1333 0.0956  0.1538  0.2807  432 ASP A O     
3575 C  CB    . ASP A 432 ? 0.4829 0.7552 1.0144 0.0593  0.0967  0.3030  432 ASP A CB    
3576 C  CG    . ASP A 432 ? 0.5657 0.8509 1.1409 0.0444  0.0735  0.3212  432 ASP A CG    
3577 O  OD1   . ASP A 432 ? 0.7290 1.0352 1.3488 0.0470  0.0806  0.3463  432 ASP A OD1   
3578 O  OD2   . ASP A 432 ? 0.4792 0.7529 1.0437 0.0300  0.0481  0.3106  432 ASP A OD2   
3579 N  N     . VAL A 433 ? 0.4582 0.7339 0.9883 0.1008  0.1566  0.3081  433 VAL A N     
3580 C  CA    . VAL A 433 ? 0.4739 0.7350 0.9741 0.1159  0.1771  0.2936  433 VAL A CA    
3581 C  C     . VAL A 433 ? 0.6833 0.9273 1.1665 0.1086  0.1610  0.2767  433 VAL A C     
3582 O  O     . VAL A 433 ? 0.6067 0.8580 1.1210 0.1003  0.1446  0.2874  433 VAL A O     
3583 C  CB    . VAL A 433 ? 0.4938 0.7695 1.0280 0.1333  0.2025  0.3140  433 VAL A CB    
3584 C  CG1   . VAL A 433 ? 0.5346 0.7913 1.0365 0.1486  0.2223  0.2970  433 VAL A CG1   
3585 C  CG2   . VAL A 433 ? 0.5649 0.8575 1.1135 0.1416  0.2208  0.3313  433 VAL A CG2   
3586 N  N     . ALA A 434 ? 0.6395 0.8613 1.0739 0.1117  0.1652  0.2511  434 ALA A N     
3587 C  CA    . ALA A 434 ? 0.6857 0.8902 1.1008 0.1052  0.1517  0.2342  434 ALA A CA    
3588 C  C     . ALA A 434 ? 0.5498 0.7525 0.9823 0.1167  0.1646  0.2399  434 ALA A C     
3589 O  O     . ALA A 434 ? 0.5641 0.7667 0.9966 0.1332  0.1897  0.2429  434 ALA A O     
3590 C  CB    . ALA A 434 ? 0.6295 0.8119 0.9905 0.1047  0.1525  0.2066  434 ALA A CB    
3591 N  N     . PRO A 435 ? 0.5736 0.7745 1.0206 0.1089  0.1484  0.2418  435 PRO A N     
3592 C  CA    . PRO A 435 ? 0.5616 0.7591 1.0244 0.1198  0.1601  0.2465  435 PRO A CA    
3593 C  C     . PRO A 435 ? 0.8119 0.9845 1.2325 0.1295  0.1752  0.2230  435 PRO A C     
3594 O  O     . PRO A 435 ? 0.7431 0.8997 1.1226 0.1231  0.1683  0.2015  435 PRO A O     
3595 C  CB    . PRO A 435 ? 0.5210 0.7201 1.0004 0.1064  0.1349  0.2512  435 PRO A CB    
3596 C  CG    . PRO A 435 ? 0.5414 0.7360 0.9974 0.0895  0.1120  0.2398  435 PRO A CG    
3597 C  CD    . PRO A 435 ? 0.5673 0.7704 1.0199 0.0905  0.1190  0.2423  435 PRO A CD    
3598 N  N     . GLN A 436 ? 0.7890 0.9581 1.2217 0.1452  0.1960  0.2279  436 GLN A N     
3599 C  CA    . GLN A 436 ? 0.6515 0.7953 1.0487 0.1559  0.2117  0.2069  436 GLN A CA    
3600 C  C     . GLN A 436 ? 0.6237 0.7568 0.9797 0.1624  0.2256  0.1908  436 GLN A C     
3601 O  O     . GLN A 436 ? 0.7019 0.8254 1.0459 0.1790  0.2497  0.1866  436 GLN A O     
3602 C  CB    . GLN A 436 ? 0.6859 0.8111 1.0608 0.1447  0.1938  0.1894  436 GLN A CB    
3603 C  CG    . GLN A 436 ? 0.8412 0.9734 1.2506 0.1395  0.1807  0.2036  436 GLN A CG    
3604 C  CD    . GLN A 436 ? 0.9039 1.0167 1.2890 0.1303  0.1664  0.1867  436 GLN A CD    
3605 O  OE1   . GLN A 436 ? 0.8239 0.9147 1.1730 0.1333  0.1736  0.1653  436 GLN A OE1   
3606 N  NE2   . GLN A 436 ? 1.1004 1.2213 1.5049 0.1189  0.1458  0.1967  436 GLN A NE2   
3607 N  N     . VAL A 437 ? 0.6201 0.7539 0.9529 0.1500  0.2109  0.1815  437 VAL A N     
3608 C  CA    . VAL A 437 ? 0.6645 0.7872 0.9549 0.1547  0.2210  0.1650  437 VAL A CA    
3609 C  C     . VAL A 437 ? 0.8108 0.9519 1.1122 0.1617  0.2339  0.1804  437 VAL A C     
3610 O  O     . VAL A 437 ? 0.7383 0.8715 1.0056 0.1688  0.2462  0.1697  437 VAL A O     
3611 C  CB    . VAL A 437 ? 0.6636 0.7760 0.9209 0.1390  0.1997  0.1460  437 VAL A CB    
3612 C  CG1   . VAL A 437 ? 0.5535 0.6424 0.7871 0.1367  0.1949  0.1261  437 VAL A CG1   
3613 C  CG2   . VAL A 437 ? 0.6386 0.7672 0.9210 0.1230  0.1765  0.1580  437 VAL A CG2   
3614 N  N     . GLY A 438 ? 0.7356 0.9011 1.0837 0.1594  0.2308  0.2059  438 GLY A N     
3615 C  CA    . GLY A 438 ? 0.5531 0.7378 0.9199 0.1678  0.2463  0.2246  438 GLY A CA    
3616 C  C     . GLY A 438 ? 0.6530 0.8411 0.9963 0.1617  0.2415  0.2202  438 GLY A C     
3617 O  O     . GLY A 438 ? 0.6529 0.8539 1.0037 0.1710  0.2580  0.2336  438 GLY A O     
3618 N  N     . HIS A 439 ? 0.6907 0.8682 1.0071 0.1469  0.2201  0.2030  439 HIS A N     
3619 C  CA    . HIS A 439 ? 0.6786 0.8591 0.9740 0.1412  0.2150  0.1993  439 HIS A CA    
3620 C  C     . HIS A 439 ? 0.6596 0.8635 0.9965 0.1324  0.2047  0.2226  439 HIS A C     
3621 O  O     . HIS A 439 ? 0.5810 0.7920 0.9486 0.1210  0.1866  0.2312  439 HIS A O     
3622 C  CB    . HIS A 439 ? 0.6978 0.8607 0.9560 0.1285  0.1955  0.1753  439 HIS A CB    
3623 C  CG    . HIS A 439 ? 0.6863 0.8259 0.9042 0.1352  0.2033  0.1521  439 HIS A CG    
3624 N  ND1   . HIS A 439 ? 0.7023 0.8328 0.8891 0.1490  0.2234  0.1438  439 HIS A ND1   
3625 C  CD2   . HIS A 439 ? 0.6078 0.7302 0.8114 0.1297  0.1931  0.1357  439 HIS A CD2   
3626 C  CE1   . HIS A 439 ? 0.7200 0.8279 0.8755 0.1511  0.2241  0.1223  439 HIS A CE1   
3627 N  NE2   . HIS A 439 ? 0.6936 0.7969 0.8603 0.1394  0.2063  0.1176  439 HIS A NE2   
3628 N  N     . ARG A 440 ? 0.6588 0.8740 0.9960 0.1374  0.2158  0.2330  440 ARG A N     
3629 C  CA    . ARG A 440 ? 0.6610 0.8982 1.0387 0.1297  0.2079  0.2563  440 ARG A CA    
3630 C  C     . ARG A 440 ? 0.6550 0.8879 1.0129 0.1160  0.1893  0.2471  440 ARG A C     
3631 O  O     . ARG A 440 ? 0.7398 0.9619 1.0563 0.1194  0.1946  0.2320  440 ARG A O     
3632 C  CB    . ARG A 440 ? 0.6278 0.8822 1.0246 0.1447  0.2337  0.2776  440 ARG A CB    
3633 C  CG    . ARG A 440 ? 0.6461 0.8989 1.0457 0.1634  0.2592  0.2808  440 ARG A CG    
3634 C  CD    . ARG A 440 ? 0.6695 0.9445 1.1024 0.1769  0.2830  0.3082  440 ARG A CD    
3635 N  NE    . ARG A 440 ? 0.9233 1.2077 1.3950 0.1867  0.2954  0.3237  440 ARG A NE    
3636 C  CZ    . ARG A 440 ? 0.8639 1.1612 1.3553 0.2050  0.3241  0.3423  440 ARG A CZ    
3637 N  NH1   . ARG A 440 ? 0.9491 1.2517 1.4237 0.2158  0.3441  0.3482  440 ARG A NH1   
3638 N  NH2   . ARG A 440 ? 0.8505 1.1560 1.3796 0.2132  0.3336  0.3562  440 ARG A NH2   
3639 N  N     . PHE A 441 ? 0.5471 0.7880 0.9345 0.1006  0.1671  0.2563  441 PHE A N     
3640 C  CA    . PHE A 441 ? 0.5923 0.8278 0.9645 0.0871  0.1481  0.2480  441 PHE A CA    
3641 C  C     . PHE A 441 ? 0.6675 0.9216 1.0800 0.0807  0.1426  0.2715  441 PHE A C     
3642 O  O     . PHE A 441 ? 0.7031 0.9685 1.1582 0.0738  0.1321  0.2877  441 PHE A O     
3643 C  CB    . PHE A 441 ? 0.6935 0.9147 1.0548 0.0733  0.1238  0.2318  441 PHE A CB    
3644 C  CG    . PHE A 441 ? 0.6084 0.8103 0.9279 0.0777  0.1274  0.2077  441 PHE A CG    
3645 C  CD1   . PHE A 441 ? 0.6048 0.7941 0.8819 0.0779  0.1282  0.1892  441 PHE A CD1   
3646 C  CD2   . PHE A 441 ? 0.5916 0.7883 0.9164 0.0814  0.1300  0.2046  441 PHE A CD2   
3647 C  CE1   . PHE A 441 ? 0.7171 0.8889 0.9585 0.0810  0.1304  0.1677  441 PHE A CE1   
3648 C  CE2   . PHE A 441 ? 0.6426 0.8208 0.9312 0.0849  0.1331  0.1831  441 PHE A CE2   
3649 C  CZ    . PHE A 441 ? 0.7483 0.9140 0.9955 0.0843  0.1330  0.1645  441 PHE A CZ    
3650 N  N     . CYS A 442 ? 0.7086 0.9654 1.1080 0.0826  0.1489  0.2737  442 CYS A N     
3651 C  CA    . CYS A 442 ? 0.6991 0.9727 1.1359 0.0773  0.1457  0.2967  442 CYS A CA    
3652 C  C     . CYS A 442 ? 0.6966 0.9657 1.1496 0.0581  0.1160  0.2950  442 CYS A C     
3653 O  O     . CYS A 442 ? 0.6586 0.9103 1.0792 0.0501  0.1012  0.2740  442 CYS A O     
3654 C  CB    . CYS A 442 ? 0.8174 1.0928 1.2311 0.0842  0.1592  0.2977  442 CYS A CB    
3655 S  SG    . CYS A 442 ? 0.8197 1.1146 1.2773 0.0782  0.1568  0.3263  442 CYS A SG    
3656 N  N     . LYS A 443 ? 0.5192 0.8035 1.0225 0.0508  0.1074  0.3174  443 LYS A N     
3657 C  CA    . LYS A 443 ? 0.4711 0.7506 0.9921 0.0324  0.0789  0.3177  443 LYS A CA    
3658 C  C     . LYS A 443 ? 0.4321 0.7204 0.9772 0.0265  0.0754  0.3339  443 LYS A C     
3659 O  O     . LYS A 443 ? 0.7022 0.9881 1.2704 0.0114  0.0525  0.3384  443 LYS A O     
3660 C  CB    . LYS A 443 ? 0.4290 0.7162 0.9892 0.0254  0.0654  0.3292  443 LYS A CB    
3661 C  CG    . LYS A 443 ? 0.5697 0.8533 1.1174 0.0341  0.0737  0.3205  443 LYS A CG    
3662 C  CD    . LYS A 443 ? 0.6911 0.9788 1.2714 0.0241  0.0539  0.3286  443 LYS A CD    
3663 C  CE    . LYS A 443 ? 0.5691 0.8429 1.1419 0.0057  0.0231  0.3180  443 LYS A CE    
3664 N  NZ    . LYS A 443 ? 0.5556 0.8178 1.1150 0.0003  0.0078  0.3053  443 LYS A NZ    
3665 N  N     . ASP A 444 ? 0.5284 0.8258 1.0677 0.0380  0.0974  0.3429  444 ASP A N     
3666 C  CA    . ASP A 444 ? 0.5508 0.8569 1.1137 0.0330  0.0955  0.3599  444 ASP A CA    
3667 C  C     . ASP A 444 ? 0.6508 0.9378 1.1868 0.0215  0.0763  0.3423  444 ASP A C     
3668 O  O     . ASP A 444 ? 0.7582 1.0447 1.3211 0.0087  0.0592  0.3514  444 ASP A O     
3669 C  CB    . ASP A 444 ? 0.5819 0.9016 1.1394 0.0494  0.1249  0.3731  444 ASP A CB    
3670 C  CG    . ASP A 444 ? 0.7009 1.0414 1.2924 0.0614  0.1456  0.3949  444 ASP A CG    
3671 O  OD1   . ASP A 444 ? 0.6064 0.9564 1.2414 0.0542  0.1349  0.4080  444 ASP A OD1   
3672 O  OD2   . ASP A 444 ? 0.7136 1.0608 1.2878 0.0783  0.1728  0.3993  444 ASP A OD2   
3673 N  N     . LEU A 445 ? 0.7556 1.0263 1.2400 0.0259  0.0787  0.3176  445 LEU A N     
3674 C  CA    . LEU A 445 ? 0.7516 1.0041 1.2088 0.0167  0.0623  0.3001  445 LEU A CA    
3675 C  C     . LEU A 445 ? 0.6576 0.8915 1.0821 0.0123  0.0494  0.2742  445 LEU A C     
3676 O  O     . LEU A 445 ? 0.6859 0.9188 1.0915 0.0209  0.0601  0.2652  445 LEU A O     
3677 C  CB    . LEU A 445 ? 0.8015 1.0531 1.2273 0.0258  0.0770  0.2963  445 LEU A CB    
3678 C  CG    . LEU A 445 ? 0.8819 1.1465 1.3356 0.0260  0.0830  0.3194  445 LEU A CG    
3679 C  CD1   . LEU A 445 ? 0.9746 1.2450 1.3992 0.0404  0.1055  0.3211  445 LEU A CD1   
3680 C  CD2   . LEU A 445 ? 0.9056 1.1581 1.3678 0.0115  0.0609  0.3166  445 LEU A CD2   
3681 N  N     . PRO A 446 ? 0.6843 0.9024 1.1016 -0.0005 0.0273  0.2622  446 PRO A N     
3682 C  CA    . PRO A 446 ? 0.6451 0.8458 1.0304 -0.0041 0.0162  0.2385  446 PRO A CA    
3683 C  C     . PRO A 446 ? 0.5898 0.7831 0.9297 0.0055  0.0290  0.2205  446 PRO A C     
3684 O  O     . PRO A 446 ? 0.6667 0.8594 0.9913 0.0089  0.0352  0.2193  446 PRO A O     
3685 C  CB    . PRO A 446 ? 0.6470 0.8325 1.0334 -0.0183 -0.0074 0.2317  446 PRO A CB    
3686 C  CG    . PRO A 446 ? 0.7625 0.9538 1.1669 -0.0194 -0.0048 0.2457  446 PRO A CG    
3687 C  CD    . PRO A 446 ? 0.7289 0.9431 1.1663 -0.0116 0.0122  0.2697  446 PRO A CD    
3688 N  N     . GLY A 447 ? 0.6298 0.8175 0.9495 0.0094  0.0321  0.2073  447 GLY A N     
3689 C  CA    . GLY A 447 ? 0.6179 0.7978 0.8961 0.0173  0.0423  0.1896  447 GLY A CA    
3690 C  C     . GLY A 447 ? 0.6347 0.7986 0.8853 0.0104  0.0290  0.1716  447 GLY A C     
3691 O  O     . GLY A 447 ? 0.5033 0.6587 0.7619 -0.0003 0.0114  0.1691  447 GLY A O     
3692 N  N     . PHE A 448 ? 0.6914 0.8509 0.9086 0.0169  0.0377  0.1590  448 PHE A N     
3693 C  CA    . PHE A 448 ? 0.5680 0.7138 0.7590 0.0119  0.0272  0.1421  448 PHE A CA    
3694 C  C     . PHE A 448 ? 0.6582 0.7917 0.8411 0.0053  0.0149  0.1286  448 PHE A C     
3695 O  O     . PHE A 448 ? 0.5284 0.6523 0.7133 -0.0036 -0.0002 0.1242  448 PHE A O     
3696 C  CB    . PHE A 448 ? 0.6238 0.7689 0.7823 0.0202  0.0385  0.1320  448 PHE A CB    
3697 C  CG    . PHE A 448 ? 0.8401 0.9734 0.9740 0.0159  0.0289  0.1158  448 PHE A CG    
3698 C  CD1   . PHE A 448 ? 0.9299 1.0587 1.0702 0.0094  0.0182  0.1176  448 PHE A CD1   
3699 C  CD2   . PHE A 448 ? 0.7691 0.8953 0.8753 0.0183  0.0308  0.0993  448 PHE A CD2   
3700 C  CE1   . PHE A 448 ? 0.7235 0.8420 0.8429 0.0066  0.0109  0.1036  448 PHE A CE1   
3701 C  CE2   . PHE A 448 ? 0.7561 0.8733 0.8431 0.0145  0.0227  0.0861  448 PHE A CE2   
3702 C  CZ    . PHE A 448 ? 0.6780 0.7918 0.7717 0.0092  0.0133  0.0885  448 PHE A CZ    
3703 N  N     . ILE A 449 ? 0.6124 0.7451 0.7854 0.0100  0.0217  0.1220  449 ILE A N     
3704 C  CA    . ILE A 449 ? 0.5607 0.6825 0.7253 0.0045  0.0114  0.1103  449 ILE A CA    
3705 C  C     . ILE A 449 ? 0.6064 0.7278 0.7967 -0.0040 -0.0026 0.1191  449 ILE A C     
3706 O  O     . ILE A 449 ? 0.6636 0.7731 0.8448 -0.0117 -0.0168 0.1101  449 ILE A O     
3707 C  CB    . ILE A 449 ? 0.5958 0.7169 0.7480 0.0118  0.0224  0.1035  449 ILE A CB    
3708 C  CG1   . ILE A 449 ? 0.4856 0.6042 0.6088 0.0185  0.0328  0.0924  449 ILE A CG1   
3709 C  CG2   . ILE A 449 ? 0.4206 0.5314 0.5664 0.0063  0.0124  0.0937  449 ILE A CG2   
3710 C  CD1   . ILE A 449 ? 0.6101 0.7189 0.7110 0.0134  0.0236  0.0785  449 ILE A CD1   
3711 N  N     . PRO A 450 ? 0.5440 0.6775 0.7659 -0.0032 0.0000  0.1365  450 PRO A N     
3712 C  CA    . PRO A 450 ? 0.4708 0.6036 0.7174 -0.0128 -0.0165 0.1448  450 PRO A CA    
3713 C  C     . PRO A 450 ? 0.4783 0.6023 0.7267 -0.0224 -0.0322 0.1435  450 PRO A C     
3714 O  O     . PRO A 450 ? 0.5159 0.6301 0.7657 -0.0314 -0.0493 0.1400  450 PRO A O     
3715 C  CB    . PRO A 450 ? 0.5298 0.6804 0.8132 -0.0089 -0.0081 0.1661  450 PRO A CB    
3716 C  CG    . PRO A 450 ? 0.5451 0.7020 0.8165 0.0041  0.0134  0.1646  450 PRO A CG    
3717 C  CD    . PRO A 450 ? 0.5601 0.7082 0.7965 0.0069  0.0180  0.1495  450 PRO A CD    
3718 N  N     . SER A 451 ? 0.5326 0.6586 0.7796 -0.0205 -0.0270 0.1462  451 SER A N     
3719 C  CA    . SER A 451 ? 0.6080 0.7240 0.8582 -0.0291 -0.0412 0.1453  451 SER A CA    
3720 C  C     . SER A 451 ? 0.6563 0.7535 0.8744 -0.0328 -0.0507 0.1253  451 SER A C     
3721 O  O     . SER A 451 ? 0.6739 0.7582 0.8930 -0.0414 -0.0667 0.1218  451 SER A O     
3722 C  CB    . SER A 451 ? 0.6525 0.7756 0.9091 -0.0252 -0.0321 0.1540  451 SER A CB    
3723 O  OG    . SER A 451 ? 0.9360 1.0559 1.1613 -0.0183 -0.0222 0.1416  451 SER A OG    
3724 N  N     . LEU A 452 ? 0.5930 0.6879 0.7827 -0.0263 -0.0411 0.1122  452 LEU A N     
3725 C  CA    . LEU A 452 ? 0.6512 0.7301 0.8127 -0.0290 -0.0484 0.0948  452 LEU A CA    
3726 C  C     . LEU A 452 ? 0.7556 0.8267 0.9138 -0.0342 -0.0591 0.0899  452 LEU A C     
3727 O  O     . LEU A 452 ? 0.9178 0.9745 1.0663 -0.0407 -0.0724 0.0825  452 LEU A O     
3728 C  CB    . LEU A 452 ? 0.5002 0.5804 0.6360 -0.0214 -0.0359 0.0837  452 LEU A CB    
3729 C  CG    . LEU A 452 ? 0.6531 0.7456 0.7901 -0.0136 -0.0216 0.0901  452 LEU A CG    
3730 C  CD1   . LEU A 452 ? 0.6610 0.7534 0.7720 -0.0073 -0.0120 0.0780  452 LEU A CD1   
3731 C  CD2   . LEU A 452 ? 0.8352 0.9269 0.9772 -0.0149 -0.0240 0.0949  452 LEU A CD2   
3732 N  N     . LEU A 453 ? 0.5522 0.6320 0.7172 -0.0308 -0.0530 0.0941  453 LEU A N     
3733 C  CA    . LEU A 453 ? 0.5594 0.6333 0.7220 -0.0351 -0.0626 0.0912  453 LEU A CA    
3734 C  C     . LEU A 453 ? 0.6982 0.7679 0.8794 -0.0446 -0.0804 0.0992  453 LEU A C     
3735 O  O     . LEU A 453 ? 0.7631 0.8205 0.9318 -0.0504 -0.0937 0.0923  453 LEU A O     
3736 C  CB    . LEU A 453 ? 0.5946 0.6797 0.7671 -0.0290 -0.0519 0.0972  453 LEU A CB    
3737 C  CG    . LEU A 453 ? 0.6865 0.7718 0.8374 -0.0208 -0.0368 0.0869  453 LEU A CG    
3738 C  CD1   . LEU A 453 ? 0.5797 0.6720 0.7405 -0.0155 -0.0283 0.0919  453 LEU A CD1   
3739 C  CD2   . LEU A 453 ? 0.6773 0.7487 0.7988 -0.0231 -0.0417 0.0706  453 LEU A CD2   
3740 N  N     . GLY A 454 ? 0.7468 0.8265 0.9576 -0.0464 -0.0814 0.1141  454 GLY A N     
3741 C  CA    . GLY A 454 ? 0.6590 0.7341 0.8897 -0.0567 -0.1002 0.1219  454 GLY A CA    
3742 C  C     . GLY A 454 ? 0.8539 0.9083 1.0636 -0.0632 -0.1135 0.1092  454 GLY A C     
3743 O  O     . GLY A 454 ? 0.8019 0.8435 1.0062 -0.0712 -0.1310 0.1053  454 GLY A O     
3744 N  N     . ASP A 455 ? 0.9140 0.9640 1.1104 -0.0593 -0.1054 0.1026  455 ASP A N     
3745 C  CA    . ASP A 455 ? 0.9377 0.9671 1.1136 -0.0636 -0.1155 0.0901  455 ASP A CA    
3746 C  C     . ASP A 455 ? 0.9184 0.9339 1.0604 -0.0630 -0.1187 0.0737  455 ASP A C     
3747 O  O     . ASP A 455 ? 1.0041 1.0007 1.1306 -0.0686 -0.1322 0.0649  455 ASP A O     
3748 C  CB    . ASP A 455 ? 0.8479 0.8781 1.0186 -0.0581 -0.1043 0.0880  455 ASP A CB    
3749 C  CG    . ASP A 455 ? 0.9681 1.0086 1.1710 -0.0596 -0.1030 0.1045  455 ASP A CG    
3750 O  OD1   . ASP A 455 ? 0.9522 0.9892 1.1777 -0.0682 -0.1172 0.1131  455 ASP A OD1   
3751 O  OD2   . ASP A 455 ? 0.9612 1.0135 1.1669 -0.0524 -0.0883 0.1095  455 ASP A OD2   
3752 N  N     . LEU A 456 ? 0.8323 0.8560 0.9619 -0.0561 -0.1060 0.0697  456 LEU A N     
3753 C  CA    . LEU A 456 ? 0.7826 0.7950 0.8822 -0.0551 -0.1072 0.0560  456 LEU A CA    
3754 C  C     . LEU A 456 ? 0.9222 0.9285 1.0218 -0.0615 -0.1220 0.0578  456 LEU A C     
3755 O  O     . LEU A 456 ? 1.0604 1.0491 1.1377 -0.0653 -0.1328 0.0481  456 LEU A O     
3756 C  CB    . LEU A 456 ? 0.7491 0.7721 0.8396 -0.0470 -0.0908 0.0527  456 LEU A CB    
3757 C  CG    . LEU A 456 ? 0.7687 0.7931 0.8463 -0.0408 -0.0784 0.0455  456 LEU A CG    
3758 C  CD1   . LEU A 456 ? 0.6743 0.7083 0.7448 -0.0343 -0.0649 0.0426  456 LEU A CD1   
3759 C  CD2   . LEU A 456 ? 0.8897 0.8974 0.9434 -0.0419 -0.0831 0.0329  456 LEU A CD2   
3760 N  N     . LEU A 457 ? 0.9579 0.9784 1.0815 -0.0623 -0.1224 0.0705  457 LEU A N     
3761 C  CA    . LEU A 457 ? 0.9673 0.9841 1.0933 -0.0684 -0.1374 0.0742  457 LEU A CA    
3762 C  C     . LEU A 457 ? 0.9730 0.9774 1.1048 -0.0785 -0.1580 0.0759  457 LEU A C     
3763 O  O     . LEU A 457 ? 0.9238 0.9160 1.0414 -0.0842 -0.1734 0.0720  457 LEU A O     
3764 C  CB    . LEU A 457 ? 0.8500 0.8863 1.0054 -0.0663 -0.1325 0.0894  457 LEU A CB    
3765 C  CG    . LEU A 457 ? 0.8810 0.9250 1.0275 -0.0576 -0.1161 0.0865  457 LEU A CG    
3766 C  CD1   . LEU A 457 ? 0.7462 0.8083 0.9242 -0.0546 -0.1102 0.1023  457 LEU A CD1   
3767 C  CD2   . LEU A 457 ? 0.8851 0.9167 1.0027 -0.0586 -0.1213 0.0760  457 LEU A CD2   
3768 N  N     . GLU A 458 ? 0.9400 0.9463 1.0918 -0.0810 -0.1592 0.0819  458 GLU A N     
3769 C  CA    . GLU A 458 ? 0.9349 0.9255 1.0902 -0.0909 -0.1792 0.0814  458 GLU A CA    
3770 C  C     . GLU A 458 ? 1.0338 0.9989 1.1495 -0.0913 -0.1842 0.0624  458 GLU A C     
3771 O  O     . GLU A 458 ? 1.0405 0.9874 1.1423 -0.0987 -0.2027 0.0567  458 GLU A O     
3772 C  CB    . GLU A 458 ? 0.9958 0.9939 1.1822 -0.0927 -0.1772 0.0924  458 GLU A CB    
3773 C  CG    . GLU A 458 ? 1.2318 1.2081 1.4113 -0.0995 -0.1905 0.0853  458 GLU A CG    
3774 C  CD    . GLU A 458 ? 1.2775 1.2624 1.4923 -0.1020 -0.1892 0.0990  458 GLU A CD    
3775 O  OE1   . GLU A 458 ? 1.2734 1.2450 1.5003 -0.1117 -0.2067 0.1011  458 GLU A OE1   
3776 O  OE2   . GLU A 458 ? 1.2661 1.2703 1.4958 -0.0942 -0.1707 0.1079  458 GLU A OE2   
3777 N  N     . GLU A 459 ? 1.2322 1.1955 1.3288 -0.0829 -0.1680 0.0527  459 GLU A N     
3778 C  CA    . GLU A 459 ? 1.3123 1.2530 1.3723 -0.0814 -0.1697 0.0356  459 GLU A CA    
3779 C  C     . GLU A 459 ? 1.2005 1.1345 1.2321 -0.0802 -0.1721 0.0276  459 GLU A C     
3780 O  O     . GLU A 459 ? 1.3465 1.2587 1.3490 -0.0820 -0.1810 0.0159  459 GLU A O     
3781 C  CB    . GLU A 459 ? 1.2197 1.1632 1.2710 -0.0727 -0.1517 0.0295  459 GLU A CB    
3782 C  CG    . GLU A 459 ? 1.2868 1.2070 1.3076 -0.0708 -0.1531 0.0141  459 GLU A CG    
3783 C  CD    . GLU A 459 ? 1.5478 1.4710 1.5690 -0.0638 -0.1388 0.0115  459 GLU A CD    
3784 O  OE1   . GLU A 459 ? 1.6211 1.5649 1.6584 -0.0593 -0.1261 0.0193  459 GLU A OE1   
3785 O  OE2   . GLU A 459 ? 1.7652 1.6697 1.7698 -0.0624 -0.1403 0.0018  459 GLU A OE2   
3786 N  N     . ARG A 460 ? 0.9195 0.8707 0.9580 -0.0766 -0.1635 0.0338  460 ARG A N     
3787 C  CA    . ARG A 460 ? 1.0957 1.0417 1.1107 -0.0758 -0.1661 0.0288  460 ARG A CA    
3788 C  C     . ARG A 460 ? 1.3376 1.2716 1.3487 -0.0850 -0.1887 0.0308  460 ARG A C     
3789 O  O     . ARG A 460 ? 1.3914 1.3062 1.3695 -0.0861 -0.1966 0.0202  460 ARG A O     
3790 C  CB    . ARG A 460 ? 1.1231 1.0896 1.1520 -0.0710 -0.1540 0.0371  460 ARG A CB    
3791 C  CG    . ARG A 460 ? 1.1786 1.1408 1.1813 -0.0675 -0.1500 0.0307  460 ARG A CG    
3792 C  CD    . ARG A 460 ? 1.1579 1.1344 1.1774 -0.0675 -0.1502 0.0421  460 ARG A CD    
3793 N  NE    . ARG A 460 ? 1.2170 1.1879 1.2121 -0.0652 -0.1486 0.0376  460 ARG A NE    
3794 C  CZ    . ARG A 460 ? 1.2422 1.2244 1.2455 -0.0616 -0.1407 0.0437  460 ARG A CZ    
3795 N  NH1   . ARG A 460 ? 1.1097 1.1086 1.1431 -0.0591 -0.1330 0.0537  460 ARG A NH1   
3796 N  NH2   . ARG A 460 ? 1.2769 1.2528 1.2576 -0.0599 -0.1399 0.0402  460 ARG A NH2   
3797 N  N     . GLN A 461 ? 1.4294 1.3742 1.4736 -0.0915 -0.1995 0.0447  461 GLN A N     
3798 C  CA    . GLN A 461 ? 1.3458 1.2810 1.3899 -0.1014 -0.2233 0.0482  461 GLN A CA    
3799 C  C     . GLN A 461 ? 1.2513 1.1602 1.2764 -0.1076 -0.2386 0.0371  461 GLN A C     
3800 O  O     . GLN A 461 ? 1.3555 1.2478 1.3616 -0.1144 -0.2580 0.0328  461 GLN A O     
3801 C  CB    . GLN A 461 ? 1.3276 1.2830 1.4175 -0.1068 -0.2305 0.0676  461 GLN A CB    
3802 C  CG    . GLN A 461 ? 1.4996 1.4741 1.6025 -0.1033 -0.2249 0.0786  461 GLN A CG    
3803 C  CD    . GLN A 461 ? 1.8363 1.8041 1.9294 -0.1103 -0.2457 0.0814  461 GLN A CD    
3804 O  OE1   . GLN A 461 ? 1.8154 1.7608 1.8759 -0.1149 -0.2600 0.0698  461 GLN A OE1   
3805 N  NE2   . GLN A 461 ? 1.6143 1.6012 1.7348 -0.1104 -0.2471 0.0971  461 GLN A NE2   
3806 N  N     . LYS A 462 ? 1.2726 1.1762 1.3015 -0.1054 -0.2307 0.0323  462 LYS A N     
3807 C  CA    . LYS A 462 ? 1.3382 1.2135 1.3448 -0.1094 -0.2422 0.0193  462 LYS A CA    
3808 C  C     . LYS A 462 ? 1.4913 1.3463 1.4489 -0.1037 -0.2387 0.0022  462 LYS A C     
3809 O  O     . LYS A 462 ? 1.5328 1.3616 1.4629 -0.1082 -0.2540 -0.0085 462 LYS A O     
3810 C  CB    . LYS A 462 ? 1.4260 1.3014 1.4482 -0.1066 -0.2319 0.0190  462 LYS A CB    
3811 C  CG    . LYS A 462 ? 1.4263 1.2774 1.4483 -0.1146 -0.2490 0.0138  462 LYS A CG    
3812 C  CD    . LYS A 462 ? 1.6084 1.4575 1.6392 -0.1095 -0.2358 0.0118  462 LYS A CD    
3813 C  CE    . LYS A 462 ? 1.5955 1.4316 1.5886 -0.0990 -0.2208 -0.0044 462 LYS A CE    
3814 N  NZ    . LYS A 462 ? 1.4219 1.2633 1.4270 -0.0923 -0.2048 -0.0034 462 LYS A NZ    
3815 N  N     . ILE A 463 ? 1.3590 1.2252 1.3049 -0.0938 -0.2185 -0.0004 463 ILE A N     
3816 C  CA    . ILE A 463 ? 1.4279 1.2775 1.3306 -0.0873 -0.2118 -0.0148 463 ILE A CA    
3817 C  C     . ILE A 463 ? 1.5411 1.3849 1.4217 -0.0904 -0.2239 -0.0149 463 ILE A C     
3818 O  O     . ILE A 463 ? 1.7223 1.5420 1.5650 -0.0904 -0.2316 -0.0267 463 ILE A O     
3819 C  CB    . ILE A 463 ? 1.5399 1.4046 1.4418 -0.0766 -0.1870 -0.0161 463 ILE A CB    
3820 C  CG1   . ILE A 463 ? 1.5121 1.3677 1.4088 -0.0713 -0.1765 -0.0247 463 ILE A CG1   
3821 C  CG2   . ILE A 463 ? 1.4514 1.3125 1.3217 -0.0712 -0.1803 -0.0221 463 ILE A CG2   
3822 C  CD1   . ILE A 463 ? 1.3980 1.2526 1.3222 -0.0765 -0.1837 -0.0196 463 ILE A CD1   
3823 N  N     . LYS A 464 ? 1.4649 1.3296 1.3676 -0.0926 -0.2256 -0.0015 464 LYS A N     
3824 C  CA    . LYS A 464 ? 1.4753 1.3366 1.3609 -0.0960 -0.2385 0.0011  464 LYS A CA    
3825 C  C     . LYS A 464 ? 1.5522 1.3921 1.4248 -0.1062 -0.2652 -0.0023 464 LYS A C     
3826 O  O     . LYS A 464 ? 1.5751 1.4058 1.4223 -0.1087 -0.2777 -0.0035 464 LYS A O     
3827 C  CB    . LYS A 464 ? 1.3731 1.2613 1.2928 -0.0970 -0.2368 0.0182  464 LYS A CB    
3828 C  CG    . LYS A 464 ? 1.2884 1.1983 1.2313 -0.0890 -0.2131 0.0230  464 LYS A CG    
3829 C  CD    . LYS A 464 ? 1.3192 1.2496 1.2795 -0.0864 -0.2069 0.0352  464 LYS A CD    
3830 C  CE    . LYS A 464 ? 1.2559 1.1781 1.1860 -0.0857 -0.2120 0.0329  464 LYS A CE    
3831 N  NZ    . LYS A 464 ? 1.0561 0.9968 1.0078 -0.0848 -0.2105 0.0472  464 LYS A NZ    
3832 N  N     . LYS A 465 ? 1.5162 1.3474 1.4053 -0.1124 -0.2750 -0.0035 465 LYS A N     
3833 C  CA    . LYS A 465 ? 1.6408 1.4491 1.5190 -0.1232 -0.3019 -0.0080 465 LYS A CA    
3834 C  C     . LYS A 465 ? 1.7307 1.5053 1.5660 -0.1204 -0.3027 -0.0281 465 LYS A C     
3835 O  O     . LYS A 465 ? 1.8852 1.6370 1.6798 -0.1220 -0.3154 -0.0382 465 LYS A O     
3836 C  CB    . LYS A 465 ? 1.6578 1.4763 1.5839 -0.1328 -0.3137 0.0044  465 LYS A CB    
3837 C  CG    . LYS A 465 ? 1.7780 1.5678 1.6955 -0.1423 -0.3353 -0.0046 465 LYS A CG    
3838 C  CD    . LYS A 465 ? 1.7072 1.5090 1.6751 -0.1538 -0.3510 0.0110  465 LYS A CD    
3839 C  CE    . LYS A 465 ? 1.6394 1.4151 1.5952 -0.1673 -0.3832 0.0057  465 LYS A CE    
3840 N  NZ    . LYS A 465 ? 1.6488 1.3972 1.5982 -0.1705 -0.3886 -0.0065 465 LYS A NZ    
3841 N  N     . LYS A 466 ? 1.7352 1.5058 1.5780 -0.1155 -0.2888 -0.0339 466 LYS A N     
3842 C  CA    . LYS A 466 ? 1.7487 1.4864 1.5548 -0.1123 -0.2892 -0.0523 466 LYS A CA    
3843 C  C     . LYS A 466 ? 1.8907 1.6153 1.6470 -0.1027 -0.2789 -0.0645 466 LYS A C     
3844 O  O     . LYS A 466 ? 2.0222 1.7149 1.7378 -0.1015 -0.2856 -0.0799 466 LYS A O     
3845 C  CB    . LYS A 466 ? 1.6409 1.3816 1.4664 -0.1066 -0.2722 -0.0540 466 LYS A CB    
3846 C  CG    . LYS A 466 ? 1.6395 1.3481 1.4288 -0.1004 -0.2675 -0.0725 466 LYS A CG    
3847 C  CD    . LYS A 466 ? 1.5544 1.2712 1.3611 -0.0919 -0.2462 -0.0725 466 LYS A CD    
3848 C  CE    . LYS A 466 ? 1.4574 1.1959 1.3156 -0.0979 -0.2478 -0.0571 466 LYS A CE    
3849 N  NZ    . LYS A 466 ? 1.2488 0.9920 1.1208 -0.0900 -0.2295 -0.0575 466 LYS A NZ    
3850 N  N     . MET A 467 ? 1.8254 1.5732 1.5842 -0.0957 -0.2623 -0.0574 467 MET A N     
3851 C  CA    . MET A 467 ? 1.9323 1.6728 1.6493 -0.0875 -0.2527 -0.0646 467 MET A CA    
3852 C  C     . MET A 467 ? 2.0170 1.7322 1.6949 -0.0930 -0.2746 -0.0716 467 MET A C     
3853 O  O     . MET A 467 ? 2.0847 1.7767 1.7160 -0.0863 -0.2704 -0.0849 467 MET A O     
3854 C  CB    . MET A 467 ? 1.8627 1.6342 1.5982 -0.0835 -0.2391 -0.0516 467 MET A CB    
3855 C  CG    . MET A 467 ? 1.9088 1.6813 1.6168 -0.0717 -0.2172 -0.0570 467 MET A CG    
3856 S  SD    . MET A 467 ? 2.7491 2.4964 2.3986 -0.0694 -0.2256 -0.0659 467 MET A SD    
3857 C  CE    . MET A 467 ? 1.9993 1.7732 1.6606 -0.0695 -0.2228 -0.0498 467 MET A CE    
3858 N  N     . LYS A 468 ? 2.0060 1.7253 1.7022 -0.1051 -0.2985 -0.0625 468 LYS A N     
3859 C  CA    . LYS A 468 ? 1.9989 1.6963 1.6584 -0.1113 -0.3219 -0.0677 468 LYS A CA    
3860 C  C     . LYS A 468 ? 1.9538 1.6120 1.5788 -0.1136 -0.3344 -0.0862 468 LYS A C     
3861 O  O     . LYS A 468 ? 1.9248 1.5566 1.4989 -0.1122 -0.3433 -0.0979 468 LYS A O     
3862 C  CB    . LYS A 468 ? 1.8397 1.5534 1.5330 -0.1242 -0.3454 -0.0517 468 LYS A CB    
3863 C  CG    . LYS A 468 ? 1.8266 1.5761 1.5507 -0.1221 -0.3357 -0.0330 468 LYS A CG    
3864 C  CD    . LYS A 468 ? 1.9410 1.6999 1.6446 -0.1088 -0.3093 -0.0345 468 LYS A CD    
3865 C  CE    . LYS A 468 ? 1.9233 1.6605 1.5694 -0.1048 -0.3133 -0.0440 468 LYS A CE    
3866 N  NZ    . LYS A 468 ? 1.9480 1.6850 1.5701 -0.0910 -0.2851 -0.0511 468 LYS A NZ    
3867 N  N     . ALA A 469 ? 1.9237 1.5761 1.5744 -0.1166 -0.3348 -0.0891 469 ALA A N     
3868 C  CA    . ALA A 469 ? 2.0132 1.6263 1.6333 -0.1183 -0.3455 -0.1072 469 ALA A CA    
3869 C  C     . ALA A 469 ? 2.2084 1.8024 1.7846 -0.1031 -0.3226 -0.1231 469 ALA A C     
3870 O  O     . ALA A 469 ? 2.2043 1.7627 1.7311 -0.1011 -0.3305 -0.1398 469 ALA A O     
3871 C  CB    . ALA A 469 ? 1.9450 1.5587 1.6084 -0.1251 -0.3504 -0.1041 469 ALA A CB    
3872 N  N     . THR A 470 ? 2.3132 1.9301 1.9065 -0.0921 -0.2943 -0.1181 470 THR A N     
3873 C  CA    . THR A 470 ? 2.1688 1.7721 1.7283 -0.0773 -0.2708 -0.1306 470 THR A CA    
3874 C  C     . THR A 470 ? 2.4221 2.0138 1.9300 -0.0710 -0.2686 -0.1366 470 THR A C     
3875 O  O     . THR A 470 ? 2.2173 1.8250 1.7255 -0.0751 -0.2761 -0.1263 470 THR A O     
3876 C  CB    . THR A 470 ? 2.0995 1.7342 1.6926 -0.0685 -0.2434 -0.1214 470 THR A CB    
3877 O  OG1   . THR A 470 ? 2.1105 1.7736 1.7113 -0.0667 -0.2353 -0.1092 470 THR A OG1   
3878 C  CG2   . THR A 470 ? 1.9747 1.6258 1.6206 -0.0752 -0.2461 -0.1120 470 THR A CG2   
3879 N  N     . ILE A 471 ? 2.1785 1.7419 1.6417 -0.0601 -0.2571 -0.1526 471 ILE A N     
3880 C  CA    . ILE A 471 ? 2.0779 1.6250 1.4856 -0.0525 -0.2537 -0.1599 471 ILE A CA    
3881 C  C     . ILE A 471 ? 2.0965 1.6545 1.4936 -0.0362 -0.2209 -0.1598 471 ILE A C     
3882 O  O     . ILE A 471 ? 2.0119 1.5815 1.3907 -0.0309 -0.2117 -0.1538 471 ILE A O     
3883 C  CB    . ILE A 471 ? 1.9152 1.4151 1.2707 -0.0534 -0.2703 -0.1796 471 ILE A CB    
3884 C  CG1   . ILE A 471 ? 1.8684 1.3578 1.2398 -0.0712 -0.3046 -0.1791 471 ILE A CG1   
3885 C  CG2   . ILE A 471 ? 1.8746 1.3584 1.1697 -0.0458 -0.2679 -0.1858 471 ILE A CG2   
3886 C  CD1   . ILE A 471 ? 1.7424 1.1844 1.0600 -0.0744 -0.3259 -0.1983 471 ILE A CD1   
3887 N  N     . ASP A 472 ? 2.1391 1.6939 1.5488 -0.0281 -0.2032 -0.1655 472 ASP A N     
3888 C  CA    . ASP A 472 ? 2.1053 1.6720 1.5112 -0.0131 -0.1724 -0.1643 472 ASP A CA    
3889 C  C     . ASP A 472 ? 2.1048 1.7121 1.5417 -0.0138 -0.1622 -0.1466 472 ASP A C     
3890 O  O     . ASP A 472 ? 2.1185 1.7515 1.6032 -0.0216 -0.1662 -0.1354 472 ASP A O     
3891 C  CB    . ASP A 472 ? 2.0110 1.5766 1.4420 -0.0072 -0.1583 -0.1682 472 ASP A CB    
3892 C  CG    . ASP A 472 ? 1.9984 1.5687 1.4181 0.0094  -0.1279 -0.1698 472 ASP A CG    
3893 O  OD1   . ASP A 472 ? 2.0533 1.6421 1.4663 0.0147  -0.1150 -0.1618 472 ASP A OD1   
3894 O  OD2   . ASP A 472 ? 2.0199 1.5759 1.4401 0.0173  -0.1169 -0.1778 472 ASP A OD2   
3895 N  N     . PRO A 473 ? 2.0465 1.6593 1.4574 -0.0058 -0.1492 -0.1434 473 PRO A N     
3896 C  CA    . PRO A 473 ? 2.0516 1.7007 1.4920 -0.0072 -0.1408 -0.1267 473 PRO A CA    
3897 C  C     . PRO A 473 ? 2.0793 1.7566 1.5680 -0.0049 -0.1240 -0.1189 473 PRO A C     
3898 O  O     . PRO A 473 ? 2.0314 1.7371 1.5557 -0.0106 -0.1247 -0.1060 473 PRO A O     
3899 C  CB    . PRO A 473 ? 2.0581 1.7029 1.4585 0.0037  -0.1254 -0.1266 473 PRO A CB    
3900 C  CG    . PRO A 473 ? 2.0572 1.6678 1.4139 0.0140  -0.1181 -0.1432 473 PRO A CG    
3901 C  CD    . PRO A 473 ? 1.9651 1.5507 1.3180 0.0048  -0.1416 -0.1542 473 PRO A CD    
3902 N  N     . ILE A 474 ? 2.1920 1.8614 1.6823 0.0034  -0.1094 -0.1263 474 ILE A N     
3903 C  CA    . ILE A 474 ? 2.1631 1.8592 1.6973 0.0057  -0.0943 -0.1188 474 ILE A CA    
3904 C  C     . ILE A 474 ? 2.1010 1.8098 1.6762 -0.0059 -0.1094 -0.1130 474 ILE A C     
3905 O  O     . ILE A 474 ? 2.0214 1.7593 1.6325 -0.0093 -0.1054 -0.1015 474 ILE A O     
3906 C  CB    . ILE A 474 ? 2.0404 1.7249 1.5672 0.0177  -0.0760 -0.1270 474 ILE A CB    
3907 C  CG1   . ILE A 474 ? 2.0544 1.7126 1.5775 0.0155  -0.0873 -0.1383 474 ILE A CG1   
3908 C  CG2   . ILE A 474 ? 1.8666 1.5363 1.3501 0.0299  -0.0610 -0.1325 474 ILE A CG2   
3909 C  CD1   . ILE A 474 ? 1.9138 1.5590 1.4302 0.0281  -0.0693 -0.1461 474 ILE A CD1   
3910 N  N     . GLU A 475 ? 2.0228 1.7093 1.5925 -0.0122 -0.1271 -0.1207 475 GLU A N     
3911 C  CA    . GLU A 475 ? 1.9659 1.6644 1.5758 -0.0229 -0.1407 -0.1139 475 GLU A CA    
3912 C  C     . GLU A 475 ? 1.9464 1.6661 1.5747 -0.0322 -0.1522 -0.1015 475 GLU A C     
3913 O  O     . GLU A 475 ? 1.9127 1.6569 1.5815 -0.0369 -0.1520 -0.0908 475 GLU A O     
3914 C  CB    . GLU A 475 ? 1.9056 1.5741 1.5051 -0.0288 -0.1590 -0.1239 475 GLU A CB    
3915 C  CG    . GLU A 475 ? 1.8702 1.5495 1.5139 -0.0370 -0.1674 -0.1172 475 GLU A CG    
3916 C  CD    . GLU A 475 ? 1.8952 1.5949 1.5685 -0.0298 -0.1473 -0.1120 475 GLU A CD    
3917 O  OE1   . GLU A 475 ? 1.9820 1.6725 1.6386 -0.0188 -0.1309 -0.1194 475 GLU A OE1   
3918 O  OE2   . GLU A 475 ? 1.8220 1.5472 1.5347 -0.0348 -0.1476 -0.1002 475 GLU A OE2   
3919 N  N     . ARG A 476 ? 1.9502 1.6604 1.5484 -0.0341 -0.1617 -0.1024 476 ARG A N     
3920 C  CA    . ARG A 476 ? 1.9808 1.7119 1.5952 -0.0409 -0.1701 -0.0895 476 ARG A CA    
3921 C  C     . ARG A 476 ? 1.9643 1.7265 1.6065 -0.0362 -0.1506 -0.0790 476 ARG A C     
3922 O  O     . ARG A 476 ? 1.9825 1.7674 1.6616 -0.0417 -0.1533 -0.0680 476 ARG A O     
3923 C  CB    . ARG A 476 ? 2.0672 1.7832 1.6396 -0.0409 -0.1792 -0.0921 476 ARG A CB    
3924 C  CG    . ARG A 476 ? 2.1565 1.8405 1.6984 -0.0469 -0.2018 -0.1029 476 ARG A CG    
3925 C  CD    . ARG A 476 ? 2.2558 1.9254 1.7518 -0.0457 -0.2094 -0.1052 476 ARG A CD    
3926 N  NE    . ARG A 476 ? 2.4160 2.1083 1.9302 -0.0523 -0.2185 -0.0899 476 ARG A NE    
3927 C  CZ    . ARG A 476 ? 2.2985 1.9866 1.7814 -0.0517 -0.2247 -0.0867 476 ARG A CZ    
3928 N  NH1   . ARG A 476 ? 2.0659 1.7277 1.4947 -0.0448 -0.2225 -0.0980 476 ARG A NH1   
3929 N  NH2   . ARG A 476 ? 2.2953 2.0058 1.8013 -0.0576 -0.2326 -0.0714 476 ARG A NH2   
3930 N  N     . LYS A 477 ? 1.9947 1.7577 1.6195 -0.0257 -0.1307 -0.0821 477 LYS A N     
3931 C  CA    . LYS A 477 ? 1.8972 1.6878 1.5478 -0.0218 -0.1132 -0.0729 477 LYS A CA    
3932 C  C     . LYS A 477 ? 1.8602 1.6660 1.5489 -0.0226 -0.1073 -0.0705 477 LYS A C     
3933 O  O     . LYS A 477 ? 1.8225 1.6509 1.5434 -0.0266 -0.1067 -0.0608 477 LYS A O     
3934 C  CB    . LYS A 477 ? 1.9160 1.7034 1.5416 -0.0108 -0.0938 -0.0761 477 LYS A CB    
3935 C  CG    . LYS A 477 ? 1.9369 1.7358 1.5549 -0.0098 -0.0893 -0.0673 477 LYS A CG    
3936 C  CD    . LYS A 477 ? 1.8416 1.6296 1.4242 0.0007  -0.0741 -0.0712 477 LYS A CD    
3937 C  CE    . LYS A 477 ? 1.7636 1.5512 1.3237 0.0002  -0.0776 -0.0644 477 LYS A CE    
3938 N  NZ    . LYS A 477 ? 1.6450 1.4291 1.1789 0.0112  -0.0583 -0.0643 477 LYS A NZ    
3939 N  N     . LEU A 478 ? 1.8664 1.6593 1.5511 -0.0186 -0.1031 -0.0790 478 LEU A N     
3940 C  CA    . LEU A 478 ? 1.8438 1.6504 1.5626 -0.0189 -0.0978 -0.0761 478 LEU A CA    
3941 C  C     . LEU A 478 ? 1.8308 1.6490 1.5802 -0.0289 -0.1120 -0.0679 478 LEU A C     
3942 O  O     . LEU A 478 ? 1.7643 1.6054 1.5445 -0.0297 -0.1057 -0.0598 478 LEU A O     
3943 C  CB    . LEU A 478 ? 1.8331 1.6197 1.5418 -0.0141 -0.0952 -0.0860 478 LEU A CB    
3944 C  CG    . LEU A 478 ? 1.8744 1.6464 1.5536 -0.0028 -0.0802 -0.0947 478 LEU A CG    
3945 C  CD1   . LEU A 478 ? 1.8042 1.5475 1.4672 -0.0002 -0.0847 -0.1060 478 LEU A CD1   
3946 C  CD2   . LEU A 478 ? 1.6578 1.4518 1.3559 0.0047  -0.0600 -0.0895 478 LEU A CD2   
3947 N  N     . LEU A 479 ? 1.8807 1.6832 1.6221 -0.0363 -0.1311 -0.0698 479 LEU A N     
3948 C  CA    . LEU A 479 ? 1.7593 1.5734 1.5322 -0.0458 -0.1447 -0.0604 479 LEU A CA    
3949 C  C     . LEU A 479 ? 1.7194 1.5560 1.5079 -0.0481 -0.1437 -0.0491 479 LEU A C     
3950 O  O     . LEU A 479 ? 1.6329 1.4901 1.4550 -0.0506 -0.1415 -0.0395 479 LEU A O     
3951 C  CB    . LEU A 479 ? 1.6391 1.4304 1.3997 -0.0540 -0.1670 -0.0646 479 LEU A CB    
3952 C  CG    . LEU A 479 ? 1.6945 1.4632 1.4489 -0.0536 -0.1707 -0.0744 479 LEU A CG    
3953 C  CD1   . LEU A 479 ? 1.7125 1.4597 1.4596 -0.0638 -0.1954 -0.0775 479 LEU A CD1   
3954 C  CD2   . LEU A 479 ? 1.6714 1.4561 1.4621 -0.0525 -0.1615 -0.0683 479 LEU A CD2   
3955 N  N     . ASP A 480 ? 1.7174 1.5497 1.4813 -0.0468 -0.1445 -0.0496 480 ASP A N     
3956 C  CA    . ASP A 480 ? 1.6592 1.5115 1.4377 -0.0482 -0.1428 -0.0387 480 ASP A CA    
3957 C  C     . ASP A 480 ? 1.7414 1.6158 1.5435 -0.0431 -0.1241 -0.0341 480 ASP A C     
3958 O  O     . ASP A 480 ? 1.7521 1.6449 1.5801 -0.0455 -0.1233 -0.0244 480 ASP A O     
3959 C  CB    . ASP A 480 ? 1.6485 1.4917 1.3940 -0.0460 -0.1439 -0.0400 480 ASP A CB    
3960 C  CG    . ASP A 480 ? 1.7655 1.6281 1.5264 -0.0470 -0.1416 -0.0280 480 ASP A CG    
3961 O  OD1   . ASP A 480 ? 1.6860 1.5527 1.4589 -0.0539 -0.1566 -0.0199 480 ASP A OD1   
3962 O  OD2   . ASP A 480 ? 1.7830 1.6566 1.5461 -0.0411 -0.1249 -0.0263 480 ASP A OD2   
3963 N  N     . TYR A 481 ? 1.8032 1.6755 1.5969 -0.0360 -0.1094 -0.0410 481 TYR A N     
3964 C  CA    . TYR A 481 ? 1.8867 1.7790 1.7019 -0.0320 -0.0937 -0.0374 481 TYR A CA    
3965 C  C     . TYR A 481 ? 1.6565 1.5625 1.5045 -0.0357 -0.0962 -0.0315 481 TYR A C     
3966 O  O     . TYR A 481 ? 1.5121 1.4358 1.3809 -0.0360 -0.0911 -0.0244 481 TYR A O     
3967 C  CB    . TYR A 481 ? 1.7516 1.6396 1.5554 -0.0244 -0.0797 -0.0449 481 TYR A CB    
3968 C  CG    . TYR A 481 ? 1.9926 1.8686 1.7649 -0.0189 -0.0733 -0.0498 481 TYR A CG    
3969 C  CD1   . TYR A 481 ? 2.0801 1.9619 1.8450 -0.0187 -0.0707 -0.0447 481 TYR A CD1   
3970 C  CD2   . TYR A 481 ? 1.8128 1.6723 1.5638 -0.0129 -0.0681 -0.0588 481 TYR A CD2   
3971 C  CE1   . TYR A 481 ? 2.0682 1.9398 1.8039 -0.0130 -0.0636 -0.0477 481 TYR A CE1   
3972 C  CE2   . TYR A 481 ? 1.8193 1.6680 1.5406 -0.0065 -0.0601 -0.0626 481 TYR A CE2   
3973 C  CZ    . TYR A 481 ? 1.9437 1.7990 1.6571 -0.0067 -0.0578 -0.0567 481 TYR A CZ    
3974 O  OH    . TYR A 481 ? 1.8940 1.7394 1.5776 0.0002  -0.0487 -0.0591 481 TYR A OH    
3975 N  N     . ARG A 482 ? 1.5069 1.4038 1.3593 -0.0380 -0.1036 -0.0341 482 ARG A N     
3976 C  CA    . ARG A 482 ? 1.4096 1.3193 1.2929 -0.0411 -0.1054 -0.0271 482 ARG A CA    
3977 C  C     . ARG A 482 ? 1.4312 1.3520 1.3334 -0.0467 -0.1139 -0.0167 482 ARG A C     
3978 O  O     . ARG A 482 ? 1.3397 1.2779 1.2672 -0.0465 -0.1085 -0.0090 482 ARG A O     
3979 C  CB    . ARG A 482 ? 1.2603 1.1560 1.1449 -0.0435 -0.1136 -0.0307 482 ARG A CB    
3980 C  CG    . ARG A 482 ? 1.3463 1.2451 1.2370 -0.0379 -0.1019 -0.0336 482 ARG A CG    
3981 C  CD    . ARG A 482 ? 1.4152 1.3060 1.3192 -0.0412 -0.1099 -0.0324 482 ARG A CD    
3982 N  NE    . ARG A 482 ? 1.4768 1.3869 1.4102 -0.0412 -0.1045 -0.0231 482 ARG A NE    
3983 C  CZ    . ARG A 482 ? 1.6875 1.6074 1.6266 -0.0353 -0.0920 -0.0231 482 ARG A CZ    
3984 N  NH1   . ARG A 482 ? 1.4080 1.3231 1.3297 -0.0290 -0.0827 -0.0309 482 ARG A NH1   
3985 N  NH2   . ARG A 482 ? 1.5404 1.4760 1.5036 -0.0354 -0.0886 -0.0142 482 ARG A NH2   
3986 N  N     . GLN A 483 ? 1.4238 1.3347 1.3131 -0.0511 -0.1267 -0.0160 483 GLN A N     
3987 C  CA    . GLN A 483 ? 1.4170 1.3389 1.3262 -0.0564 -0.1357 -0.0048 483 GLN A CA    
3988 C  C     . GLN A 483 ? 1.5327 1.4726 1.4536 -0.0524 -0.1232 0.0012  483 GLN A C     
3989 O  O     . GLN A 483 ? 1.4151 1.3707 1.3638 -0.0529 -0.1205 0.0102  483 GLN A O     
3990 C  CB    . GLN A 483 ? 1.4152 1.3225 1.3047 -0.0616 -0.1525 -0.0055 483 GLN A CB    
3991 C  CG    . GLN A 483 ? 1.3455 1.2651 1.2542 -0.0662 -0.1615 0.0072  483 GLN A CG    
3992 C  CD    . GLN A 483 ? 1.6296 1.5417 1.5130 -0.0664 -0.1676 0.0069  483 GLN A CD    
3993 O  OE1   . GLN A 483 ? 1.7425 1.6357 1.5990 -0.0696 -0.1807 0.0008  483 GLN A OE1   
3994 N  NE2   . GLN A 483 ? 1.6064 1.5321 1.4969 -0.0629 -0.1580 0.0135  483 GLN A NE2   
3995 N  N     . ARG A 484 ? 1.5017 1.4389 1.4021 -0.0481 -0.1149 -0.0034 484 ARG A N     
3996 C  CA    . ARG A 484 ? 1.2498 1.2016 1.1612 -0.0446 -0.1033 0.0016  484 ARG A CA    
3997 C  C     . ARG A 484 ? 1.2792 1.2432 1.2074 -0.0408 -0.0900 0.0005  484 ARG A C     
3998 O  O     . ARG A 484 ? 1.1521 1.1295 1.1000 -0.0397 -0.0841 0.0066  484 ARG A O     
3999 C  CB    . ARG A 484 ? 1.3887 1.3346 1.2758 -0.0412 -0.0971 -0.0024 484 ARG A CB    
4000 C  CG    . ARG A 484 ? 1.5894 1.5212 1.4498 -0.0379 -0.0936 -0.0129 484 ARG A CG    
4001 C  CD    . ARG A 484 ? 1.7254 1.6561 1.5679 -0.0332 -0.0828 -0.0148 484 ARG A CD    
4002 N  NE    . ARG A 484 ? 1.7706 1.6835 1.5800 -0.0319 -0.0874 -0.0200 484 ARG A NE    
4003 C  CZ    . ARG A 484 ? 1.7257 1.6351 1.5150 -0.0272 -0.0784 -0.0212 484 ARG A CZ    
4004 N  NH1   . ARG A 484 ? 1.4491 1.3714 1.2499 -0.0243 -0.0654 -0.0173 484 ARG A NH1   
4005 N  NH2   . ARG A 484 ? 1.7147 1.6063 1.4710 -0.0254 -0.0826 -0.0263 484 ARG A NH2   
4006 N  N     . LEU A 485 ? 1.1494 1.1082 1.0693 -0.0383 -0.0853 -0.0071 485 LEU A N     
4007 C  CA    . LEU A 485 ? 0.9130 0.8831 0.8460 -0.0347 -0.0738 -0.0081 485 LEU A CA    
4008 C  C     . LEU A 485 ? 0.9358 0.9169 0.8944 -0.0364 -0.0756 -0.0003 485 LEU A C     
4009 O  O     . LEU A 485 ? 0.8677 0.8613 0.8394 -0.0337 -0.0667 0.0026  485 LEU A O     
4010 C  CB    . LEU A 485 ? 1.0969 1.0591 1.0181 -0.0320 -0.0705 -0.0160 485 LEU A CB    
4011 C  CG    . LEU A 485 ? 1.1918 1.1515 1.0962 -0.0273 -0.0605 -0.0225 485 LEU A CG    
4012 C  CD1   . LEU A 485 ? 1.0014 0.9497 0.8928 -0.0243 -0.0594 -0.0294 485 LEU A CD1   
4013 C  CD2   . LEU A 485 ? 0.8557 0.8306 0.7723 -0.0246 -0.0493 -0.0213 485 LEU A CD2   
4014 N  N     . ILE A 486 ? 0.9859 0.9617 0.9515 -0.0408 -0.0870 0.0032  486 ILE A N     
4015 C  CA    . ILE A 486 ? 0.9320 0.9191 0.9243 -0.0424 -0.0884 0.0128  486 ILE A CA    
4016 C  C     . ILE A 486 ? 0.8942 0.8940 0.9021 -0.0414 -0.0845 0.0210  486 ILE A C     
4017 O  O     . ILE A 486 ? 0.8475 0.8599 0.8741 -0.0387 -0.0769 0.0271  486 ILE A O     
4018 C  CB    . ILE A 486 ? 1.0199 0.9982 1.0188 -0.0489 -0.1038 0.0166  486 ILE A CB    
4019 C  CG1   . ILE A 486 ? 1.0708 1.0363 1.0583 -0.0488 -0.1056 0.0088  486 ILE A CG1   
4020 C  CG2   . ILE A 486 ? 0.9613 0.9534 0.9921 -0.0511 -0.1058 0.0298  486 ILE A CG2   
4021 C  CD1   . ILE A 486 ? 1.0363 0.9874 1.0244 -0.0558 -0.1225 0.0094  486 ILE A CD1   
4022 N  N     . LYS A 487 ? 0.8851 0.8811 0.8848 -0.0429 -0.0889 0.0217  487 LYS A N     
4023 C  CA    . LYS A 487 ? 0.9349 0.9414 0.9498 -0.0415 -0.0852 0.0298  487 LYS A CA    
4024 C  C     . LYS A 487 ? 0.8163 0.8295 0.8302 -0.0354 -0.0695 0.0259  487 LYS A C     
4025 O  O     . LYS A 487 ? 0.7945 0.8182 0.8259 -0.0323 -0.0619 0.0313  487 LYS A O     
4026 C  CB    . LYS A 487 ? 1.0318 1.0314 1.0361 -0.0445 -0.0946 0.0318  487 LYS A CB    
4027 C  CG    . LYS A 487 ? 0.9716 0.9801 0.9895 -0.0424 -0.0904 0.0397  487 LYS A CG    
4028 C  CD    . LYS A 487 ? 1.0099 1.0101 1.0110 -0.0447 -0.0984 0.0401  487 LYS A CD    
4029 C  CE    . LYS A 487 ? 1.1560 1.1633 1.1677 -0.0417 -0.0920 0.0469  487 LYS A CE    
4030 N  NZ    . LYS A 487 ? 1.4835 1.4919 1.5034 -0.0456 -0.1056 0.0578  487 LYS A NZ    
4031 N  N     . ILE A 488 ? 0.8073 0.8142 0.8008 -0.0337 -0.0646 0.0166  488 ILE A N     
4032 C  CA    . ILE A 488 ? 0.7116 0.7239 0.7045 -0.0293 -0.0517 0.0121  488 ILE A CA    
4033 C  C     . ILE A 488 ? 0.7612 0.7811 0.7634 -0.0266 -0.0451 0.0115  488 ILE A C     
4034 O  O     . ILE A 488 ? 0.7281 0.7551 0.7384 -0.0231 -0.0364 0.0122  488 ILE A O     
4035 C  CB    . ILE A 488 ? 0.8838 0.8891 0.8562 -0.0286 -0.0482 0.0035  488 ILE A CB    
4036 C  CG1   . ILE A 488 ? 0.8787 0.8768 0.8400 -0.0304 -0.0531 0.0054  488 ILE A CG1   
4037 C  CG2   . ILE A 488 ? 0.7363 0.7473 0.7104 -0.0253 -0.0369 -0.0009 488 ILE A CG2   
4038 C  CD1   . ILE A 488 ? 0.8343 0.8210 0.7734 -0.0313 -0.0579 0.0000  488 ILE A CD1   
4039 N  N     . LEU A 489 ? 0.7649 0.7826 0.7650 -0.0278 -0.0492 0.0101  489 LEU A N     
4040 C  CA    . LEU A 489 ? 0.7964 0.8218 0.8051 -0.0251 -0.0435 0.0112  489 LEU A CA    
4041 C  C     . LEU A 489 ? 0.7526 0.7875 0.7822 -0.0240 -0.0416 0.0214  489 LEU A C     
4042 O  O     . LEU A 489 ? 0.7163 0.7591 0.7509 -0.0194 -0.0319 0.0223  489 LEU A O     
4043 C  CB    . LEU A 489 ? 0.7000 0.7200 0.7049 -0.0269 -0.0492 0.0096  489 LEU A CB    
4044 C  CG    . LEU A 489 ? 0.7882 0.8161 0.8038 -0.0247 -0.0451 0.0135  489 LEU A CG    
4045 C  CD1   . LEU A 489 ? 0.6282 0.6625 0.6368 -0.0200 -0.0348 0.0082  489 LEU A CD1   
4046 C  CD2   . LEU A 489 ? 0.7557 0.7757 0.7699 -0.0272 -0.0524 0.0129  489 LEU A CD2   
4047 N  N     . ALA A 490 ? 0.8121 0.8463 0.8539 -0.0278 -0.0508 0.0296  490 ALA A N     
4048 C  CA    . ALA A 490 ? 0.6881 0.7328 0.7538 -0.0265 -0.0488 0.0415  490 ALA A CA    
4049 C  C     . ALA A 490 ? 0.6204 0.6707 0.6906 -0.0213 -0.0383 0.0427  490 ALA A C     
4050 O  O     . ALA A 490 ? 0.5842 0.6429 0.6640 -0.0160 -0.0280 0.0465  490 ALA A O     
4051 C  CB    . ALA A 490 ? 0.6253 0.6682 0.7043 -0.0326 -0.0627 0.0503  490 ALA A CB    
4052 N  N     . ASN A 491 ? 0.6206 0.6654 0.6831 -0.0222 -0.0401 0.0397  491 ASN A N     
4053 C  CA    . ASN A 491 ? 0.6199 0.6674 0.6865 -0.0173 -0.0303 0.0401  491 ASN A CA    
4054 C  C     . ASN A 491 ? 0.6647 0.7123 0.7200 -0.0125 -0.0185 0.0308  491 ASN A C     
4055 O  O     . ASN A 491 ? 0.5969 0.6479 0.6583 -0.0070 -0.0084 0.0319  491 ASN A O     
4056 C  CB    . ASN A 491 ? 0.6061 0.6465 0.6649 -0.0196 -0.0347 0.0384  491 ASN A CB    
4057 C  CG    . ASN A 491 ? 0.7346 0.7758 0.8053 -0.0238 -0.0466 0.0489  491 ASN A CG    
4058 O  OD1   . ASN A 491 ? 0.8644 0.9136 0.9561 -0.0239 -0.0493 0.0594  491 ASN A OD1   
4059 N  ND2   . ASN A 491 ? 0.7462 0.7796 0.8038 -0.0272 -0.0541 0.0470  491 ASN A ND2   
4060 N  N     . SER A 492 ? 0.7660 0.8094 0.8044 -0.0143 -0.0199 0.0217  492 SER A N     
4061 C  CA    . SER A 492 ? 0.7379 0.7823 0.7659 -0.0106 -0.0111 0.0134  492 SER A CA    
4062 C  C     . SER A 492 ? 0.7217 0.7740 0.7561 -0.0066 -0.0054 0.0175  492 SER A C     
4063 O  O     . SER A 492 ? 0.6505 0.7044 0.6782 -0.0022 0.0030  0.0128  492 SER A O     
4064 C  CB    . SER A 492 ? 0.7448 0.7844 0.7566 -0.0135 -0.0145 0.0046  492 SER A CB    
4065 O  OG    . SER A 492 ? 0.8732 0.9060 0.8795 -0.0173 -0.0208 0.0037  492 SER A OG    
4066 N  N     . VAL A 493 ? 0.7661 0.8229 0.8127 -0.0082 -0.0103 0.0263  493 VAL A N     
4067 C  CA    . VAL A 493 ? 0.7298 0.7955 0.7857 -0.0039 -0.0038 0.0333  493 VAL A CA    
4068 C  C     . VAL A 493 ? 0.6645 0.7352 0.7325 0.0020  0.0059  0.0397  493 VAL A C     
4069 O  O     . VAL A 493 ? 0.5713 0.6466 0.6367 0.0084  0.0166  0.0401  493 VAL A O     
4070 C  CB    . VAL A 493 ? 0.6766 0.7454 0.7462 -0.0079 -0.0119 0.0424  493 VAL A CB    
4071 C  CG1   . VAL A 493 ? 0.6453 0.7248 0.7280 -0.0031 -0.0040 0.0524  493 VAL A CG1   
4072 C  CG2   . VAL A 493 ? 0.6554 0.7174 0.7113 -0.0119 -0.0192 0.0351  493 VAL A CG2   
4073 N  N     . TYR A 494 ? 0.6090 0.6787 0.6895 0.0005  0.0027  0.0450  494 TYR A N     
4074 C  CA    . TYR A 494 ? 0.5848 0.6576 0.6763 0.0071  0.0131  0.0500  494 TYR A CA    
4075 C  C     . TYR A 494 ? 0.6623 0.7277 0.7350 0.0117  0.0223  0.0376  494 TYR A C     
4076 O  O     . TYR A 494 ? 0.7094 0.7765 0.7803 0.0193  0.0343  0.0372  494 TYR A O     
4077 C  CB    . TYR A 494 ? 0.4795 0.5521 0.5875 0.0044  0.0067  0.0579  494 TYR A CB    
4078 C  CG    . TYR A 494 ? 0.5878 0.6578 0.6993 0.0108  0.0169  0.0574  494 TYR A CG    
4079 C  CD1   . TYR A 494 ? 0.6199 0.6959 0.7436 0.0196  0.0303  0.0640  494 TYR A CD1   
4080 C  CD2   . TYR A 494 ? 0.5858 0.6463 0.6880 0.0087  0.0143  0.0504  494 TYR A CD2   
4081 C  CE1   . TYR A 494 ? 0.6083 0.6795 0.7343 0.0263  0.0405  0.0626  494 TYR A CE1   
4082 C  CE2   . TYR A 494 ? 0.5092 0.5656 0.6155 0.0146  0.0236  0.0498  494 TYR A CE2   
4083 C  CZ    . TYR A 494 ? 0.6283 0.6891 0.7461 0.0235  0.0366  0.0553  494 TYR A CZ    
4084 O  OH    . TYR A 494 ? 0.7332 0.7875 0.8546 0.0301  0.0466  0.0540  494 TYR A OH    
4085 N  N     . GLY A 495 ? 0.6002 0.6569 0.6588 0.0072  0.0168  0.0275  495 GLY A N     
4086 C  CA    . GLY A 495 ? 0.6336 0.6824 0.6765 0.0099  0.0234  0.0157  495 GLY A CA    
4087 C  C     . GLY A 495 ? 0.6795 0.7296 0.7069 0.0129  0.0285  0.0086  495 GLY A C     
4088 O  O     . GLY A 495 ? 0.8271 0.8716 0.8431 0.0172  0.0359  0.0007  495 GLY A O     
4089 N  N     . HIS A 496 ? 0.7279 0.7843 0.7538 0.0107  0.0240  0.0114  496 HIS A N     
4090 C  CA    . HIS A 496 ? 0.6968 0.7562 0.7091 0.0139  0.0283  0.0071  496 HIS A CA    
4091 C  C     . HIS A 496 ? 0.6542 0.7166 0.6672 0.0227  0.0407  0.0111  496 HIS A C     
4092 O  O     . HIS A 496 ? 0.7433 0.8026 0.7385 0.0269  0.0465  0.0032  496 HIS A O     
4093 C  CB    . HIS A 496 ? 0.6391 0.7050 0.6545 0.0105  0.0217  0.0124  496 HIS A CB    
4094 C  CG    . HIS A 496 ? 0.7411 0.8115 0.7440 0.0138  0.0252  0.0103  496 HIS A CG    
4095 N  ND1   . HIS A 496 ? 0.7006 0.7688 0.6881 0.0111  0.0207  0.0012  496 HIS A ND1   
4096 C  CD2   . HIS A 496 ? 0.7934 0.8712 0.7975 0.0196  0.0327  0.0175  496 HIS A CD2   
4097 C  CE1   . HIS A 496 ? 0.7803 0.8543 0.7594 0.0149  0.0243  0.0026  496 HIS A CE1   
4098 N  NE2   . HIS A 496 ? 0.7798 0.8592 0.7673 0.0203  0.0319  0.0124  496 HIS A NE2   
4099 N  N     . MET A 497 ? 0.7597 0.8280 0.7929 0.0258  0.0448  0.0235  497 MET A N     
4100 C  CA    . MET A 497 ? 0.7150 0.7879 0.7510 0.0354  0.0585  0.0297  497 MET A CA    
4101 C  C     . MET A 497 ? 0.7417 0.8043 0.7658 0.0418  0.0684  0.0205  497 MET A C     
4102 O  O     . MET A 497 ? 0.6777 0.7402 0.6928 0.0508  0.0808  0.0206  497 MET A O     
4103 C  CB    . MET A 497 ? 0.7999 0.8830 0.8652 0.0367  0.0603  0.0469  497 MET A CB    
4104 C  CG    . MET A 497 ? 0.6644 0.7575 0.7413 0.0324  0.0535  0.0571  497 MET A CG    
4105 S  SD    . MET A 497 ? 0.7165 0.8216 0.8320 0.0315  0.0520  0.0778  497 MET A SD    
4106 C  CE    . MET A 497 ? 0.7627 0.8607 0.8866 0.0296  0.0480  0.0755  497 MET A CE    
4107 N  N     . GLY A 498 ? 0.7681 0.8208 0.7911 0.0379  0.0637  0.0130  498 GLY A N     
4108 C  CA    . GLY A 498 ? 0.5779 0.6178 0.5893 0.0428  0.0714  0.0027  498 GLY A CA    
4109 C  C     . GLY A 498 ? 0.9122 0.9417 0.9003 0.0381  0.0657  -0.0135 498 GLY A C     
4110 O  O     . GLY A 498 ? 0.7908 0.8072 0.7699 0.0403  0.0696  -0.0232 498 GLY A O     
4111 N  N     . PHE A 499 ? 0.8504 0.8850 0.8302 0.0319  0.0565  -0.0162 499 PHE A N     
4112 C  CA    . PHE A 499 ? 0.7466 0.7740 0.7086 0.0266  0.0497  -0.0295 499 PHE A CA    
4113 C  C     . PHE A 499 ? 0.7469 0.7700 0.6857 0.0318  0.0550  -0.0382 499 PHE A C     
4114 O  O     . PHE A 499 ? 0.8866 0.9178 0.8201 0.0366  0.0595  -0.0328 499 PHE A O     
4115 C  CB    . PHE A 499 ? 0.7603 0.7956 0.7245 0.0190  0.0387  -0.0275 499 PHE A CB    
4116 C  CG    . PHE A 499 ? 0.9463 0.9778 0.8962 0.0136  0.0317  -0.0387 499 PHE A CG    
4117 C  CD1   . PHE A 499 ? 0.9526 0.9727 0.8963 0.0116  0.0312  -0.0489 499 PHE A CD1   
4118 C  CD2   . PHE A 499 ? 1.0361 1.0756 0.9813 0.0105  0.0254  -0.0381 499 PHE A CD2   
4119 C  CE1   . PHE A 499 ? 1.0769 1.0949 1.0110 0.0059  0.0239  -0.0578 499 PHE A CE1   
4120 C  CE2   . PHE A 499 ? 0.9048 0.9427 0.8402 0.0057  0.0188  -0.0467 499 PHE A CE2   
4121 C  CZ    . PHE A 499 ? 1.0702 1.0981 1.0007 0.0031  0.0177  -0.0563 499 PHE A CZ    
4122 N  N     . GLU A 500 ? 0.7721 0.7820 0.6968 0.0305  0.0540  -0.0515 500 GLU A N     
4123 C  CA    . GLU A 500 ? 0.9023 0.9051 0.8013 0.0348  0.0570  -0.0619 500 GLU A CA    
4124 C  C     . GLU A 500 ? 0.9743 0.9883 0.8618 0.0330  0.0513  -0.0603 500 GLU A C     
4125 O  O     . GLU A 500 ? 0.8782 0.8949 0.7509 0.0401  0.0578  -0.0588 500 GLU A O     
4126 C  CB    . GLU A 500 ? 0.9593 0.9463 0.8473 0.0299  0.0516  -0.0769 500 GLU A CB    
4127 C  CG    . GLU A 500 ? 1.0944 1.0678 0.9929 0.0316  0.0571  -0.0793 500 GLU A CG    
4128 C  CD    . GLU A 500 ? 1.0506 1.0287 0.9733 0.0247  0.0514  -0.0720 500 GLU A CD    
4129 O  OE1   . GLU A 500 ? 0.9063 0.8837 0.8301 0.0159  0.0414  -0.0766 500 GLU A OE1   
4130 O  OE2   . GLU A 500 ? 0.7974 0.7801 0.7378 0.0282  0.0568  -0.0610 500 GLU A OE2   
4131 N  N     . ASN A 501 ? 0.9153 0.9360 0.8096 0.0244  0.0399  -0.0599 501 ASN A N     
4132 C  CA    . ASN A 501 ? 0.9401 0.9705 0.8250 0.0221  0.0332  -0.0591 501 ASN A CA    
4133 C  C     . ASN A 501 ? 0.8186 0.8631 0.7192 0.0219  0.0326  -0.0454 501 ASN A C     
4134 O  O     . ASN A 501 ? 0.9565 1.0085 0.8588 0.0174  0.0246  -0.0436 501 ASN A O     
4135 C  CB    . ASN A 501 ? 1.0304 1.0588 0.9131 0.0132  0.0214  -0.0677 501 ASN A CB    
4136 C  CG    . ASN A 501 ? 0.9531 0.9888 0.8213 0.0119  0.0144  -0.0695 501 ASN A CG    
4137 O  OD1   . ASN A 501 ? 1.0068 1.0397 0.8540 0.0167  0.0168  -0.0737 501 ASN A OD1   
4138 N  ND2   . ASN A 501 ? 0.9173 0.9623 0.7961 0.0060  0.0061  -0.0660 501 ASN A ND2   
4139 N  N     . ALA A 502 ? 0.9395 0.9872 0.8531 0.0268  0.0406  -0.0353 502 ALA A N     
4140 C  CA    . ALA A 502 ? 0.7084 0.7675 0.6389 0.0259  0.0391  -0.0223 502 ALA A CA    
4141 C  C     . ALA A 502 ? 0.7406 0.8083 0.6647 0.0325  0.0455  -0.0143 502 ALA A C     
4142 O  O     . ALA A 502 ? 0.8175 0.8825 0.7294 0.0402  0.0555  -0.0152 502 ALA A O     
4143 C  CB    . ALA A 502 ? 0.7362 0.7951 0.6884 0.0260  0.0419  -0.0141 502 ALA A CB    
4144 N  N     . ARG A 503 ? 0.7386 0.8158 0.6708 0.0300  0.0406  -0.0060 503 ARG A N     
4145 C  CA    . ARG A 503 ? 0.8667 0.9531 0.7952 0.0358  0.0464  0.0038  503 ARG A CA    
4146 C  C     . ARG A 503 ? 0.8213 0.9126 0.7669 0.0414  0.0566  0.0167  503 ARG A C     
4147 O  O     . ARG A 503 ? 0.6619 0.7566 0.5992 0.0498  0.0677  0.0218  503 ARG A O     
4148 C  CB    . ARG A 503 ? 0.7606 0.8548 0.6959 0.0314  0.0380  0.0097  503 ARG A CB    
4149 C  CG    . ARG A 503 ? 0.8350 0.9262 0.7604 0.0256  0.0276  -0.0009 503 ARG A CG    
4150 C  CD    . ARG A 503 ? 0.8894 0.9873 0.8242 0.0223  0.0206  0.0057  503 ARG A CD    
4151 N  NE    . ARG A 503 ? 0.9512 1.0568 0.8738 0.0260  0.0211  0.0097  503 ARG A NE    
4152 C  CZ    . ARG A 503 ? 0.8267 0.9335 0.7342 0.0247  0.0151  0.0027  503 ARG A CZ    
4153 N  NH1   . ARG A 503 ? 0.9855 1.0866 0.8898 0.0195  0.0086  -0.0086 503 ARG A NH1   
4154 N  NH2   . ARG A 503 ? 0.9737 1.0884 0.8703 0.0285  0.0152  0.0084  503 ARG A NH2   
4155 N  N     . TRP A 504 ? 0.7434 0.8352 0.7128 0.0370  0.0531  0.0227  504 TRP A N     
4156 C  CA    . TRP A 504 ? 0.8233 0.9209 0.8143 0.0410  0.0609  0.0362  504 TRP A CA    
4157 C  C     . TRP A 504 ? 0.7732 0.8637 0.7670 0.0441  0.0672  0.0321  504 TRP A C     
4158 O  O     . TRP A 504 ? 0.7375 0.8293 0.7537 0.0421  0.0659  0.0393  504 TRP A O     
4159 C  CB    . TRP A 504 ? 0.7711 0.8735 0.7872 0.0339  0.0517  0.0462  504 TRP A CB    
4160 C  CG    . TRP A 504 ? 0.8236 0.9340 0.8434 0.0332  0.0493  0.0550  504 TRP A CG    
4161 C  CD1   . TRP A 504 ? 0.6800 0.8007 0.7152 0.0371  0.0559  0.0708  504 TRP A CD1   
4162 C  CD2   . TRP A 504 ? 0.8894 0.9982 0.8992 0.0286  0.0402  0.0496  504 TRP A CD2   
4163 N  NE1   . TRP A 504 ? 0.6626 0.7874 0.6976 0.0349  0.0511  0.0754  504 TRP A NE1   
4164 C  CE2   . TRP A 504 ? 0.7774 0.8949 0.7968 0.0300  0.0415  0.0624  504 TRP A CE2   
4165 C  CE3   . TRP A 504 ? 0.8170 0.9186 0.8129 0.0238  0.0318  0.0363  504 TRP A CE3   
4166 C  CZ2   . TRP A 504 ? 0.7530 0.8712 0.7679 0.0271  0.0345  0.0619  504 TRP A CZ2   
4167 C  CZ3   . TRP A 504 ? 0.7413 0.8447 0.7333 0.0212  0.0252  0.0361  504 TRP A CZ3   
4168 C  CH2   . TRP A 504 ? 0.7816 0.8928 0.7828 0.0230  0.0265  0.0485  504 TRP A CH2   
4169 N  N     . TYR A 505 ? 0.7563 0.8382 0.7270 0.0491  0.0734  0.0204  505 TYR A N     
4170 C  CA    . TYR A 505 ? 0.7575 0.8304 0.7294 0.0532  0.0805  0.0157  505 TYR A CA    
4171 C  C     . TYR A 505 ? 0.8554 0.9348 0.8410 0.0630  0.0954  0.0288  505 TYR A C     
4172 O  O     . TYR A 505 ? 0.8443 0.9308 0.8231 0.0699  0.1044  0.0356  505 TYR A O     
4173 C  CB    . TYR A 505 ? 0.6785 0.7380 0.6207 0.0555  0.0823  -0.0014 505 TYR A CB    
4174 C  CG    . TYR A 505 ? 0.7405 0.7883 0.6798 0.0621  0.0925  -0.0070 505 TYR A CG    
4175 C  CD1   . TYR A 505 ? 0.8297 0.8686 0.7793 0.0574  0.0878  -0.0122 505 TYR A CD1   
4176 C  CD2   . TYR A 505 ? 0.7180 0.7625 0.6433 0.0738  0.1077  -0.0068 505 TYR A CD2   
4177 C  CE1   . TYR A 505 ? 0.8622 0.8892 0.8105 0.0638  0.0974  -0.0169 505 TYR A CE1   
4178 C  CE2   . TYR A 505 ? 0.7664 0.7982 0.6887 0.0809  0.1180  -0.0125 505 TYR A CE2   
4179 C  CZ    . TYR A 505 ? 0.7875 0.8104 0.7224 0.0757  0.1125  -0.0175 505 TYR A CZ    
4180 O  OH    . TYR A 505 ? 0.8746 0.8837 0.8082 0.0830  0.1230  -0.0227 505 TYR A OH    
4181 N  N     . CYS A 506 ? 0.7792 0.8569 0.7851 0.0640  0.0983  0.0335  506 CYS A N     
4182 C  CA    . CYS A 506 ? 0.6824 0.7672 0.7062 0.0739  0.1131  0.0472  506 CYS A CA    
4183 C  C     . CYS A 506 ? 0.6892 0.7665 0.7269 0.0750  0.1152  0.0459  506 CYS A C     
4184 O  O     . CYS A 506 ? 0.6678 0.7500 0.7308 0.0685  0.1063  0.0539  506 CYS A O     
4185 C  CB    . CYS A 506 ? 0.6420 0.7438 0.6946 0.0715  0.1110  0.0666  506 CYS A CB    
4186 S  SG    . CYS A 506 ? 0.9453 1.0593 1.0287 0.0826  0.1284  0.0871  506 CYS A SG    
4187 N  N     . LYS A 507 ? 0.6561 0.7203 0.6759 0.0833  0.1264  0.0354  507 LYS A N     
4188 C  CA    . LYS A 507 ? 0.8095 0.8652 0.8424 0.0854  0.1296  0.0342  507 LYS A CA    
4189 C  C     . LYS A 507 ? 0.8246 0.8935 0.8931 0.0909  0.1375  0.0543  507 LYS A C     
4190 O  O     . LYS A 507 ? 0.7530 0.8231 0.8451 0.0868  0.1315  0.0603  507 LYS A O     
4191 C  CB    . LYS A 507 ? 0.7633 0.8005 0.7701 0.0945  0.1413  0.0193  507 LYS A CB    
4192 C  CG    . LYS A 507 ? 0.7903 0.8139 0.8048 0.0932  0.1399  0.0129  507 LYS A CG    
4193 C  CD    . LYS A 507 ? 0.9316 0.9378 0.9294 0.1055  0.1560  0.0032  507 LYS A CD    
4194 C  CE    . LYS A 507 ? 1.0610 1.0751 1.0759 0.1196  0.1752  0.0181  507 LYS A CE    
4195 N  NZ    . LYS A 507 ? 1.1195 1.1136 1.1197 0.1322  0.1915  0.0080  507 LYS A NZ    
4196 N  N     . GLU A 508 ? 0.7265 0.8062 0.8002 0.1001  0.1511  0.0660  508 GLU A N     
4197 C  CA    . GLU A 508 ? 0.7538 0.8490 0.8655 0.1051  0.1587  0.0875  508 GLU A CA    
4198 C  C     . GLU A 508 ? 0.7655 0.8730 0.9067 0.0921  0.1404  0.0991  508 GLU A C     
4199 O  O     . GLU A 508 ? 0.7707 0.8838 0.9421 0.0907  0.1375  0.1103  508 GLU A O     
4200 C  CB    . GLU A 508 ? 0.7550 0.8616 0.8668 0.1159  0.1753  0.0993  508 GLU A CB    
4201 C  CG    . GLU A 508 ? 0.8091 0.9022 0.8851 0.1292  0.1932  0.0868  508 GLU A CG    
4202 C  CD    . GLU A 508 ? 0.8521 0.9386 0.8894 0.1254  0.1868  0.0724  508 GLU A CD    
4203 O  OE1   . GLU A 508 ? 0.9417 1.0303 0.9783 0.1121  0.1681  0.0683  508 GLU A OE1   
4204 O  OE2   . GLU A 508 ? 0.6848 0.7639 0.6919 0.1361  0.2007  0.0656  508 GLU A OE2   
4205 N  N     . CYS A 509 ? 0.6435 0.7544 0.7756 0.0826  0.1274  0.0965  509 CYS A N     
4206 C  CA    . CYS A 509 ? 0.5077 0.6260 0.6618 0.0698  0.1088  0.1042  509 CYS A CA    
4207 C  C     . CYS A 509 ? 0.5917 0.6996 0.7455 0.0626  0.0967  0.0956  509 CYS A C     
4208 O  O     . CYS A 509 ? 0.6804 0.7944 0.8605 0.0570  0.0872  0.1063  509 CYS A O     
4209 C  CB    . CYS A 509 ? 0.4698 0.5896 0.6092 0.0621  0.0984  0.0997  509 CYS A CB    
4210 S  SG    . CYS A 509 ? 0.7934 0.9236 0.9259 0.0707  0.1125  0.1081  509 CYS A SG    
4211 N  N     . ALA A 510 ? 0.7745 0.8670 0.8992 0.0623  0.0965  0.0771  510 ALA A N     
4212 C  CA    . ALA A 510 ? 0.7465 0.8291 0.8695 0.0553  0.0856  0.0693  510 ALA A CA    
4213 C  C     . ALA A 510 ? 0.6844 0.7668 0.8298 0.0607  0.0917  0.0778  510 ALA A C     
4214 O  O     . ALA A 510 ? 0.6332 0.7183 0.7968 0.0542  0.0805  0.0848  510 ALA A O     
4215 C  CB    . ALA A 510 ? 0.7503 0.8173 0.8404 0.0543  0.0853  0.0491  510 ALA A CB    
4216 N  N     . GLU A 511 ? 0.6761 0.7548 0.8196 0.0730  0.1097  0.0775  511 GLU A N     
4217 C  CA    . GLU A 511 ? 0.6856 0.7628 0.8505 0.0796  0.1172  0.0852  511 GLU A CA    
4218 C  C     . GLU A 511 ? 0.7616 0.8577 0.9659 0.0816  0.1185  0.1083  511 GLU A C     
4219 O  O     . GLU A 511 ? 0.6765 0.7747 0.9050 0.0836  0.1188  0.1180  511 GLU A O     
4220 C  CB    . GLU A 511 ? 0.5942 0.6584 0.7426 0.0930  0.1369  0.0760  511 GLU A CB    
4221 C  CG    . GLU A 511 ? 0.7117 0.7841 0.8604 0.1049  0.1546  0.0836  511 GLU A CG    
4222 C  CD    . GLU A 511 ? 0.7622 0.8185 0.8913 0.1190  0.1741  0.0732  511 GLU A CD    
4223 O  OE1   . GLU A 511 ? 0.7334 0.7737 0.8581 0.1199  0.1744  0.0636  511 GLU A OE1   
4224 O  OE2   . GLU A 511 ? 0.7733 0.8318 0.8902 0.1294  0.1894  0.0744  511 GLU A OE2   
4225 N  N     . SER A 512 ? 0.7047 0.8150 0.9180 0.0809  0.1187  0.1186  512 SER A N     
4226 C  CA    . SER A 512 ? 0.5250 0.6544 0.7792 0.0798  0.1157  0.1414  512 SER A CA    
4227 C  C     . SER A 512 ? 0.6410 0.7729 0.9086 0.0655  0.0924  0.1453  512 SER A C     
4228 O  O     . SER A 512 ? 0.6285 0.7702 0.9287 0.0641  0.0872  0.1610  512 SER A O     
4229 C  CB    . SER A 512 ? 0.4866 0.6296 0.7472 0.0815  0.1210  0.1515  512 SER A CB    
4230 O  OG    . SER A 512 ? 0.6728 0.8148 0.9223 0.0962  0.1441  0.1508  512 SER A OG    
4231 N  N     . VAL A 513 ? 0.6537 0.7768 0.8959 0.0552  0.0783  0.1314  513 VAL A N     
4232 C  CA    . VAL A 513 ? 0.6259 0.7488 0.8744 0.0422  0.0566  0.1331  513 VAL A CA    
4233 C  C     . VAL A 513 ? 0.5895 0.7067 0.8451 0.0421  0.0530  0.1337  513 VAL A C     
4234 O  O     . VAL A 513 ? 0.5980 0.7227 0.8779 0.0367  0.0409  0.1467  513 VAL A O     
4235 C  CB    . VAL A 513 ? 0.5468 0.6594 0.7635 0.0337  0.0458  0.1165  513 VAL A CB    
4236 C  CG1   . VAL A 513 ? 0.6080 0.7154 0.8227 0.0224  0.0262  0.1144  513 VAL A CG1   
4237 C  CG2   . VAL A 513 ? 0.4862 0.6067 0.7034 0.0319  0.0452  0.1203  513 VAL A CG2   
4238 N  N     . THR A 514 ? 0.6092 0.7125 0.8439 0.0477  0.0626  0.1201  514 THR A N     
4239 C  CA    . THR A 514 ? 0.7067 0.8035 0.9485 0.0484  0.0607  0.1212  514 THR A CA    
4240 C  C     . THR A 514 ? 0.6925 0.8000 0.9699 0.0570  0.0700  0.1395  514 THR A C     
4241 O  O     . THR A 514 ? 0.6190 0.7291 0.9154 0.0545  0.0618  0.1492  514 THR A O     
4242 C  CB    . THR A 514 ? 0.6656 0.7442 0.8793 0.0526  0.0698  0.1028  514 THR A CB    
4243 O  OG1   . THR A 514 ? 0.7279 0.8036 0.9315 0.0632  0.0879  0.0972  514 THR A OG1   
4244 C  CG2   . THR A 514 ? 0.5616 0.6309 0.7461 0.0426  0.0578  0.0874  514 THR A CG2   
4245 N  N     . ALA A 515 ? 0.6588 0.7733 0.9460 0.0677  0.0873  0.1455  515 ALA A N     
4246 C  CA    . ALA A 515 ? 0.5724 0.6986 0.8960 0.0774  0.0984  0.1644  515 ALA A CA    
4247 C  C     . ALA A 515 ? 0.6830 0.8281 1.0430 0.0692  0.0824  0.1853  515 ALA A C     
4248 O  O     . ALA A 515 ? 0.6723 0.8246 1.0621 0.0711  0.0802  0.1999  515 ALA A O     
4249 C  CB    . ALA A 515 ? 0.4767 0.6071 0.8010 0.0909  0.1211  0.1670  515 ALA A CB    
4250 N  N     . TRP A 516 ? 0.6138 0.7664 0.9725 0.0598  0.0704  0.1871  516 TRP A N     
4251 C  CA    . TRP A 516 ? 0.5604 0.7279 0.9506 0.0498  0.0517  0.2047  516 TRP A CA    
4252 C  C     . TRP A 516 ? 0.5992 0.7594 0.9836 0.0397  0.0314  0.2016  516 TRP A C     
4253 O  O     . TRP A 516 ? 0.6499 0.8205 1.0645 0.0364  0.0206  0.2181  516 TRP A O     
4254 C  CB    . TRP A 516 ? 0.4955 0.6687 0.8823 0.0415  0.0425  0.2049  516 TRP A CB    
4255 C  CG    . TRP A 516 ? 0.6006 0.7923 1.0196 0.0472  0.0533  0.2235  516 TRP A CG    
4256 C  CD1   . TRP A 516 ? 0.4258 0.6364 0.8912 0.0466  0.0495  0.2474  516 TRP A CD1   
4257 C  CD2   . TRP A 516 ? 0.5856 0.7798 0.9943 0.0539  0.0691  0.2211  516 TRP A CD2   
4258 N  NE1   . TRP A 516 ? 0.4758 0.7008 0.9618 0.0530  0.0633  0.2605  516 TRP A NE1   
4259 C  CE2   . TRP A 516 ? 0.6049 0.8199 1.0554 0.0578  0.0758  0.2448  516 TRP A CE2   
4260 C  CE3   . TRP A 516 ? 0.6428 0.8245 1.0116 0.0571  0.0779  0.2024  516 TRP A CE3   
4261 C  CZ2   . TRP A 516 ? 0.4741 0.6973 0.9262 0.0652  0.0921  0.2504  516 TRP A CZ2   
4262 C  CZ3   . TRP A 516 ? 0.6354 0.8249 1.0044 0.0642  0.0929  0.2075  516 TRP A CZ3   
4263 C  CH2   . TRP A 516 ? 0.6212 0.8310 1.0308 0.0685  0.1004  0.2313  516 TRP A CH2   
4264 N  N     . GLY A 517 ? 0.6012 0.7441 0.9471 0.0348  0.0261  0.1815  517 GLY A N     
4265 C  CA    . GLY A 517 ? 0.5768 0.7121 0.9134 0.0259  0.0085  0.1783  517 GLY A CA    
4266 C  C     . GLY A 517 ? 0.4713 0.6073 0.8265 0.0318  0.0125  0.1877  517 GLY A C     
4267 O  O     . GLY A 517 ? 0.5807 0.7206 0.9489 0.0253  -0.0036 0.1979  517 GLY A O     
4268 N  N     . ARG A 518 ? 0.5218 0.6529 0.8775 0.0445  0.0339  0.1845  518 ARG A N     
4269 C  CA    . ARG A 518 ? 0.5641 0.6959 0.9417 0.0519  0.0401  0.1949  518 ARG A CA    
4270 C  C     . ARG A 518 ? 0.6654 0.8182 1.0890 0.0530  0.0356  0.2204  518 ARG A C     
4271 O  O     . ARG A 518 ? 0.6610 0.8184 1.1048 0.0512  0.0260  0.2330  518 ARG A O     
4272 C  CB    . ARG A 518 ? 0.6626 0.7836 1.0322 0.0662  0.0652  0.1860  518 ARG A CB    
4273 C  CG    . ARG A 518 ? 0.5821 0.6812 0.9129 0.0652  0.0681  0.1632  518 ARG A CG    
4274 C  CD    . ARG A 518 ? 0.4817 0.5689 0.8025 0.0788  0.0916  0.1531  518 ARG A CD    
4275 N  NE    . ARG A 518 ? 0.7582 0.8391 1.0485 0.0786  0.0972  0.1368  518 ARG A NE    
4276 C  CZ    . ARG A 518 ? 0.7861 0.8662 1.0719 0.0897  0.1157  0.1339  518 ARG A CZ    
4277 N  NH1   . ARG A 518 ? 0.5054 0.5897 0.8152 0.1028  0.1324  0.1455  518 ARG A NH1   
4278 N  NH2   . ARG A 518 ? 0.6564 0.7311 0.9124 0.0882  0.1179  0.1195  518 ARG A NH2   
4279 N  N     . GLU A 519 ? 0.6556 0.8224 1.0981 0.0559  0.0421  0.2297  519 GLU A N     
4280 C  CA    . GLU A 519 ? 0.6876 0.8764 1.1784 0.0569  0.0386  0.2556  519 GLU A CA    
4281 C  C     . GLU A 519 ? 0.6343 0.8306 1.1359 0.0412  0.0091  0.2649  519 GLU A C     
4282 O  O     . GLU A 519 ? 0.6835 0.8906 1.2160 0.0399  -0.0006 0.2826  519 GLU A O     
4283 C  CB    . GLU A 519 ? 0.6231 0.8254 1.1308 0.0627  0.0521  0.2637  519 GLU A CB    
4284 C  CG    . GLU A 519 ? 0.7710 0.9981 1.3302 0.0599  0.0437  0.2913  519 GLU A CG    
4285 C  CD    . GLU A 519 ? 0.9094 1.1502 1.4846 0.0636  0.0552  0.3000  519 GLU A CD    
4286 O  OE1   . GLU A 519 ? 1.0451 1.2828 1.6111 0.0777  0.0811  0.2952  519 GLU A OE1   
4287 O  OE2   . GLU A 519 ? 0.9670 1.2208 1.5634 0.0524  0.0382  0.3118  519 GLU A OE2   
4288 N  N     . TYR A 520 ? 0.6097 0.7996 1.0852 0.0294  -0.0059 0.2529  520 TYR A N     
4289 C  CA    . TYR A 520 ? 0.5705 0.7649 1.0525 0.0144  -0.0344 0.2600  520 TYR A CA    
4290 C  C     . TYR A 520 ? 0.6258 0.8115 1.0957 0.0101  -0.0478 0.2582  520 TYR A C     
4291 O  O     . TYR A 520 ? 0.7767 0.9713 1.2672 0.0025  -0.0677 0.2730  520 TYR A O     
4292 C  CB    . TYR A 520 ? 0.5695 0.7550 1.0219 0.0042  -0.0452 0.2452  520 TYR A CB    
4293 C  CG    . TYR A 520 ? 0.5815 0.7784 1.0518 0.0058  -0.0371 0.2516  520 TYR A CG    
4294 C  CD1   . TYR A 520 ? 0.4233 0.6402 0.9391 0.0028  -0.0445 0.2746  520 TYR A CD1   
4295 C  CD2   . TYR A 520 ? 0.4826 0.6712 0.9259 0.0103  -0.0225 0.2362  520 TYR A CD2   
4296 C  CE1   . TYR A 520 ? 0.4194 0.6475 0.9536 0.0045  -0.0362 0.2823  520 TYR A CE1   
4297 C  CE2   . TYR A 520 ? 0.6804 0.8797 1.1396 0.0123  -0.0144 0.2435  520 TYR A CE2   
4298 C  CZ    . TYR A 520 ? 0.5641 0.7831 1.0690 0.0095  -0.0207 0.2668  520 TYR A CZ    
4299 O  OH    . TYR A 520 ? 0.6080 0.8384 1.1305 0.0115  -0.0121 0.2757  520 TYR A OH    
4300 N  N     . LEU A 521 ? 0.6086 0.7771 1.0457 0.0148  -0.0376 0.2412  521 LEU A N     
4301 C  CA    . LEU A 521 ? 0.6242 0.7840 1.0483 0.0111  -0.0489 0.2400  521 LEU A CA    
4302 C  C     . LEU A 521 ? 0.5906 0.7609 1.0512 0.0188  -0.0443 0.2595  521 LEU A C     
4303 O  O     . LEU A 521 ? 0.6270 0.8027 1.0996 0.0126  -0.0625 0.2721  521 LEU A O     
4304 C  CB    . LEU A 521 ? 0.5199 0.6593 0.9026 0.0137  -0.0387 0.2176  521 LEU A CB    
4305 C  CG    . LEU A 521 ? 0.4933 0.6234 0.8641 0.0120  -0.0458 0.2174  521 LEU A CG    
4306 C  CD1   . LEU A 521 ? 0.4616 0.5886 0.8126 -0.0013 -0.0708 0.2161  521 LEU A CD1   
4307 C  CD2   . LEU A 521 ? 0.6385 0.7511 0.9808 0.0178  -0.0296 0.1991  521 LEU A CD2   
4308 N  N     . THR A 522 ? 0.6399 0.8126 1.1177 0.0328  -0.0200 0.2624  522 THR A N     
4309 C  CA    . THR A 522 ? 0.6276 0.8093 1.1417 0.0419  -0.0130 0.2811  522 THR A CA    
4310 C  C     . THR A 522 ? 0.6034 0.8096 1.1649 0.0391  -0.0245 0.3071  522 THR A C     
4311 O  O     . THR A 522 ? 0.6623 0.8783 1.2533 0.0405  -0.0314 0.3256  522 THR A O     
4312 C  CB    . THR A 522 ? 0.6309 0.8064 1.1489 0.0585  0.0172  0.2761  522 THR A CB    
4313 O  OG1   . THR A 522 ? 0.7261 0.9105 1.2531 0.0634  0.0300  0.2769  522 THR A OG1   
4314 C  CG2   . THR A 522 ? 0.5708 0.7217 1.0448 0.0602  0.0261  0.2513  522 THR A CG2   
4315 N  N     . MET A 523 ? 0.6061 0.8230 1.1776 0.0349  -0.0270 0.3101  523 MET A N     
4316 C  CA    . MET A 523 ? 0.5825 0.8227 1.1995 0.0293  -0.0418 0.3348  523 MET A CA    
4317 C  C     . MET A 523 ? 0.5125 0.7529 1.1246 0.0139  -0.0742 0.3396  523 MET A C     
4318 O  O     . MET A 523 ? 0.7643 1.0198 1.4123 0.0119  -0.0870 0.3614  523 MET A O     
4319 C  CB    . MET A 523 ? 0.5507 0.7995 1.1754 0.0267  -0.0387 0.3352  523 MET A CB    
4320 C  CG    . MET A 523 ? 0.7120 0.9836 1.3818 0.0175  -0.0575 0.3590  523 MET A CG    
4321 S  SD    . MET A 523 ? 0.8604 1.1256 1.5098 -0.0051 -0.0971 0.3535  523 MET A SD    
4322 C  CE    . MET A 523 ? 0.7004 0.9601 1.3306 -0.0100 -0.0933 0.3395  523 MET A CE    
4323 N  N     . THR A 524 ? 0.6499 0.8733 1.2169 0.0032  -0.0878 0.3197  524 THR A N     
4324 C  CA    . THR A 524 ? 0.6751 0.8951 1.2290 -0.0110 -0.1180 0.3213  524 THR A CA    
4325 C  C     . THR A 524 ? 0.6607 0.8788 1.2162 -0.0079 -0.1219 0.3290  524 THR A C     
4326 O  O     . THR A 524 ? 0.7937 1.0214 1.3672 -0.0153 -0.1443 0.3454  524 THR A O     
4327 C  CB    . THR A 524 ? 0.7422 0.9415 1.2432 -0.0196 -0.1259 0.2962  524 THR A CB    
4328 O  OG1   . THR A 524 ? 0.6855 0.8836 1.1811 -0.0175 -0.1125 0.2860  524 THR A OG1   
4329 C  CG2   . THR A 524 ? 0.8349 1.0325 1.3263 -0.0354 -0.1580 0.2985  524 THR A CG2   
4330 N  N     . ILE A 525 ? 0.6759 0.8813 1.2129 0.0028  -0.1011 0.3179  525 ILE A N     
4331 C  CA    . ILE A 525 ? 0.6507 0.8531 1.1905 0.0067  -0.1025 0.3258  525 ILE A CA    
4332 C  C     . ILE A 525 ? 0.7499 0.9736 1.3454 0.0138  -0.1001 0.3534  525 ILE A C     
4333 O  O     . ILE A 525 ? 0.7581 0.9883 1.3683 0.0112  -0.1152 0.3693  525 ILE A O     
4334 C  CB    . ILE A 525 ? 0.6843 0.8675 1.1954 0.0165  -0.0796 0.3075  525 ILE A CB    
4335 C  CG1   . ILE A 525 ? 0.6550 0.8188 1.1130 0.0076  -0.0880 0.2849  525 ILE A CG1   
4336 C  CG2   . ILE A 525 ? 0.5243 0.7076 1.0538 0.0251  -0.0728 0.3201  525 ILE A CG2   
4337 C  CD1   . ILE A 525 ? 0.4818 0.6283 0.9114 0.0149  -0.0656 0.2633  525 ILE A CD1   
4338 N  N     . LYS A 526 ? 0.7230 0.9584 1.3504 0.0235  -0.0808 0.3607  526 LYS A N     
4339 C  CA    . LYS A 526 ? 0.7409 0.9991 1.4259 0.0307  -0.0776 0.3888  526 LYS A CA    
4340 C  C     . LYS A 526 ? 0.6671 0.9437 1.3788 0.0169  -0.1090 0.4086  526 LYS A C     
4341 O  O     . LYS A 526 ? 0.6989 0.9883 1.4416 0.0170  -0.1204 0.4300  526 LYS A O     
4342 C  CB    . LYS A 526 ? 0.8378 1.1053 1.5484 0.0429  -0.0514 0.3921  526 LYS A CB    
4343 C  CG    . LYS A 526 ? 0.8086 1.1014 1.5820 0.0517  -0.0450 0.4223  526 LYS A CG    
4344 C  CD    . LYS A 526 ? 0.9432 1.2358 1.7310 0.0713  -0.0087 0.4218  526 LYS A CD    
4345 C  CE    . LYS A 526 ? 1.0418 1.3504 1.8821 0.0845  0.0025  0.4478  526 LYS A CE    
4346 N  NZ    . LYS A 526 ? 1.1097 1.4055 1.9390 0.0868  -0.0013 0.4465  526 LYS A NZ    
4347 N  N     . GLU A 527 ? 0.7216 0.9990 1.4217 0.0045  -0.1242 0.4019  527 GLU A N     
4348 C  CA    . GLU A 527 ? 0.6688 0.9622 1.3947 -0.0097 -0.1552 0.4195  527 GLU A CA    
4349 C  C     . GLU A 527 ? 0.7088 0.9946 1.4122 -0.0199 -0.1824 0.4204  527 GLU A C     
4350 O  O     . GLU A 527 ? 0.8015 1.1038 1.5385 -0.0249 -0.2023 0.4433  527 GLU A O     
4351 C  CB    . GLU A 527 ? 0.6840 0.9744 1.3959 -0.0210 -0.1653 0.4085  527 GLU A CB    
4352 C  CG    . GLU A 527 ? 0.6712 0.9709 1.4060 -0.0119 -0.1404 0.4101  527 GLU A CG    
4353 C  CD    . GLU A 527 ? 0.9188 1.2478 1.7211 -0.0071 -0.1372 0.4411  527 GLU A CD    
4354 O  OE1   . GLU A 527 ? 0.7850 1.1287 1.6176 -0.0181 -0.1642 0.4603  527 GLU A OE1   
4355 O  OE2   . GLU A 527 ? 0.9309 1.2681 1.7557 0.0080  -0.1077 0.4465  527 GLU A OE2   
4356 N  N     . ILE A 528 ? 0.7710 1.0326 1.4176 -0.0229 -0.1834 0.3965  528 ILE A N     
4357 C  CA    . ILE A 528 ? 0.7527 1.0057 1.3713 -0.0330 -0.2094 0.3960  528 ILE A CA    
4358 C  C     . ILE A 528 ? 0.7157 0.9755 1.3549 -0.0250 -0.2069 0.4136  528 ILE A C     
4359 O  O     . ILE A 528 ? 0.7792 1.0427 1.4176 -0.0330 -0.2320 0.4256  528 ILE A O     
4360 C  CB    . ILE A 528 ? 0.7527 0.9788 1.3068 -0.0368 -0.2081 0.3668  528 ILE A CB    
4361 C  CG1   . ILE A 528 ? 0.7391 0.9560 1.2608 -0.0483 -0.2366 0.3659  528 ILE A CG1   
4362 C  CG2   . ILE A 528 ? 0.7934 1.0068 1.3298 -0.0233 -0.1786 0.3541  528 ILE A CG2   
4363 C  CD1   . ILE A 528 ? 0.6798 0.8734 1.1427 -0.0556 -0.2422 0.3397  528 ILE A CD1   
4364 N  N     . GLU A 529 ? 0.7199 0.9809 1.3776 -0.0091 -0.1773 0.4158  529 GLU A N     
4365 C  CA    . GLU A 529 ? 0.6733 0.9394 1.3526 -0.0004 -0.1729 0.4326  529 GLU A CA    
4366 C  C     . GLU A 529 ? 0.8514 1.1456 1.5957 0.0029  -0.1780 0.4642  529 GLU A C     
4367 O  O     . GLU A 529 ? 0.7310 1.0343 1.4953 0.0030  -0.1909 0.4839  529 GLU A O     
4368 C  CB    . GLU A 529 ? 0.6874 0.9391 1.3567 0.0152  -0.1395 0.4202  529 GLU A CB    
4369 C  CG    . GLU A 529 ? 0.7671 0.9927 1.3781 0.0127  -0.1363 0.3950  529 GLU A CG    
4370 C  CD    . GLU A 529 ? 0.8628 1.0744 1.4688 0.0272  -0.1065 0.3855  529 GLU A CD    
4371 O  OE1   . GLU A 529 ? 0.8069 1.0199 1.4305 0.0378  -0.0830 0.3820  529 GLU A OE1   
4372 O  OE2   . GLU A 529 ? 0.7738 0.9720 1.3577 0.0280  -0.1066 0.3816  529 GLU A OE2   
4373 N  N     . GLU A 530 ? 0.7525 1.0615 1.5318 0.0060  -0.1680 0.4710  530 GLU A N     
4374 C  CA    . GLU A 530 ? 0.7826 1.1174 1.6234 0.0093  -0.1675 0.4995  530 GLU A CA    
4375 C  C     . GLU A 530 ? 0.8588 1.2031 1.7078 -0.0110 -0.1970 0.5080  530 GLU A C     
4376 O  O     . GLU A 530 ? 0.9430 1.2969 1.8150 -0.0175 -0.2083 0.5254  530 GLU A O     
4377 C  CB    . GLU A 530 ? 0.7452 1.0879 1.6157 0.0236  -0.1351 0.5012  530 GLU A CB    
4378 C  CG    . GLU A 530 ? 0.8833 1.2151 1.7515 0.0440  -0.1027 0.4952  530 GLU A CG    
4379 C  CD    . GLU A 530 ? 1.1126 1.4495 2.0025 0.0585  -0.0705 0.4944  530 GLU A CD    
4380 O  OE1   . GLU A 530 ? 0.8179 1.1679 1.7245 0.0527  -0.0733 0.4990  530 GLU A OE1   
4381 O  OE2   . GLU A 530 ? 1.1487 1.4741 2.0354 0.0749  -0.0418 0.4880  530 GLU A OE2   
4382 N  N     . LYS A 531 ? 0.7324 1.0729 1.5631 -0.0211 -0.2098 0.4959  531 LYS A N     
4383 C  CA    . LYS A 531 ? 0.7715 1.1171 1.6092 -0.0404 -0.2370 0.5021  531 LYS A CA    
4384 C  C     . LYS A 531 ? 0.8514 1.1835 1.6481 -0.0556 -0.2705 0.4944  531 LYS A C     
4385 O  O     . LYS A 531 ? 0.8518 1.1850 1.6517 -0.0719 -0.2953 0.4995  531 LYS A O     
4386 C  CB    . LYS A 531 ? 0.7682 1.1144 1.6070 -0.0446 -0.2346 0.4932  531 LYS A CB    
4387 C  CG    . LYS A 531 ? 0.9099 1.2735 1.7991 -0.0403 -0.2159 0.5103  531 LYS A CG    
4388 C  CD    . LYS A 531 ? 1.0214 1.3909 1.9295 -0.0182 -0.1778 0.5132  531 LYS A CD    
4389 C  CE    . LYS A 531 ? 1.0313 1.4109 1.9665 -0.0121 -0.1558 0.5179  531 LYS A CE    
4390 N  NZ    . LYS A 531 ? 1.0049 1.3890 1.9584 0.0098  -0.1181 0.5221  531 LYS A NZ    
4391 N  N     . TYR A 532 ? 0.9490 1.2671 1.7064 -0.0505 -0.2716 0.4824  532 TYR A N     
4392 C  CA    . TYR A 532 ? 0.8256 1.1294 1.5388 -0.0638 -0.3014 0.4745  532 TYR A CA    
4393 C  C     . TYR A 532 ? 0.8210 1.1186 1.5155 -0.0571 -0.3004 0.4779  532 TYR A C     
4394 O  O     . TYR A 532 ? 0.8618 1.1485 1.5198 -0.0674 -0.3242 0.4738  532 TYR A O     
4395 C  CB    . TYR A 532 ? 0.7611 1.0477 1.4273 -0.0696 -0.3112 0.4509  532 TYR A CB    
4396 C  CG    . TYR A 532 ? 0.7441 1.0306 1.4145 -0.0845 -0.3280 0.4468  532 TYR A CG    
4397 C  CD1   . TYR A 532 ? 0.8667 1.1437 1.5154 -0.1018 -0.3591 0.4449  532 TYR A CD1   
4398 C  CD2   . TYR A 532 ? 0.7597 1.0542 1.4554 -0.0808 -0.3120 0.4450  532 TYR A CD2   
4399 C  CE1   . TYR A 532 ? 0.8590 1.1327 1.5118 -0.1153 -0.3743 0.4410  532 TYR A CE1   
4400 C  CE2   . TYR A 532 ? 0.7813 1.0745 1.4824 -0.0944 -0.3267 0.4424  532 TYR A CE2   
4401 C  CZ    . TYR A 532 ? 0.7620 1.0439 1.4422 -0.1117 -0.3580 0.4403  532 TYR A CZ    
4402 O  OH    . TYR A 532 ? 0.8273 1.1048 1.5130 -0.1250 -0.3726 0.4376  532 TYR A OH    
4403 N  N     . GLY A 533 ? 0.7565 1.0589 1.4728 -0.0401 -0.2734 0.4849  533 GLY A N     
4404 C  CA    . GLY A 533 ? 0.7480 1.0454 1.4541 -0.0341 -0.2717 0.4915  533 GLY A CA    
4405 C  C     . GLY A 533 ? 0.8849 1.1582 1.5343 -0.0314 -0.2667 0.4708  533 GLY A C     
4406 O  O     . GLY A 533 ? 0.8925 1.1603 1.5259 -0.0300 -0.2726 0.4767  533 GLY A O     
4407 N  N     . PHE A 534 ? 0.8424 1.0989 1.4569 -0.0318 -0.2527 0.4441  534 PHE A N     
4408 C  CA    . PHE A 534 ? 0.7718 1.0032 1.3297 -0.0305 -0.2429 0.4205  534 PHE A CA    
4409 C  C     . PHE A 534 ? 0.8532 1.0786 1.4199 -0.0147 -0.2110 0.4184  534 PHE A C     
4410 O  O     . PHE A 534 ? 0.7907 1.0287 1.4028 -0.0039 -0.1935 0.4311  534 PHE A O     
4411 C  CB    . PHE A 534 ? 0.8702 1.0864 1.3898 -0.0366 -0.2398 0.3936  534 PHE A CB    
4412 C  CG    . PHE A 534 ? 0.9960 1.2071 1.4862 -0.0524 -0.2710 0.3881  534 PHE A CG    
4413 C  CD1   . PHE A 534 ? 0.9425 1.1699 1.4646 -0.0619 -0.2941 0.4033  534 PHE A CD1   
4414 C  CD2   . PHE A 534 ? 1.0241 1.2131 1.4549 -0.0578 -0.2770 0.3678  534 PHE A CD2   
4415 C  CE1   . PHE A 534 ? 0.9060 1.1255 1.3994 -0.0768 -0.3238 0.3969  534 PHE A CE1   
4416 C  CE2   . PHE A 534 ? 0.9208 1.1021 1.3215 -0.0715 -0.3049 0.3614  534 PHE A CE2   
4417 C  CZ    . PHE A 534 ? 0.9096 1.1051 1.3406 -0.0812 -0.3289 0.3752  534 PHE A CZ    
4418 N  N     . LYS A 535 ? 0.9631 1.1681 1.4856 -0.0133 -0.2034 0.4022  535 LYS A N     
4419 C  CA    . LYS A 535 ? 0.9128 1.1063 1.4344 -0.0003 -0.1737 0.3940  535 LYS A CA    
4420 C  C     . LYS A 535 ? 0.8895 1.0618 1.3616 -0.0027 -0.1630 0.3644  535 LYS A C     
4421 O  O     . LYS A 535 ? 0.9439 1.1040 1.3735 -0.0100 -0.1748 0.3548  535 LYS A O     
4422 C  CB    . LYS A 535 ? 0.9061 1.0973 1.4306 0.0044  -0.1744 0.4082  535 LYS A CB    
4423 C  CG    . LYS A 535 ? 0.8380 1.0150 1.3628 0.0172  -0.1446 0.3996  535 LYS A CG    
4424 C  CD    . LYS A 535 ? 1.0882 1.2753 1.6627 0.0301  -0.1238 0.4095  535 LYS A CD    
4425 C  CE    . LYS A 535 ? 0.9246 1.0948 1.4988 0.0428  -0.0957 0.4007  535 LYS A CE    
4426 N  NZ    . LYS A 535 ? 0.9093 1.0680 1.4702 0.0474  -0.0740 0.3771  535 LYS A NZ    
4427 N  N     . VAL A 536 ? 0.8023 0.9707 1.2798 0.0039  -0.1408 0.3507  536 VAL A N     
4428 C  CA    . VAL A 536 ? 0.8629 1.0132 1.2975 0.0018  -0.1308 0.3235  536 VAL A CA    
4429 C  C     . VAL A 536 ? 0.8177 0.9511 1.2305 0.0074  -0.1165 0.3149  536 VAL A C     
4430 O  O     . VAL A 536 ? 0.8406 0.9715 1.2752 0.0183  -0.0969 0.3183  536 VAL A O     
4431 C  CB    . VAL A 536 ? 0.7439 0.8960 1.1911 0.0073  -0.1124 0.3130  536 VAL A CB    
4432 C  CG1   . VAL A 536 ? 0.6837 0.8173 1.0887 0.0062  -0.1010 0.2860  536 VAL A CG1   
4433 C  CG2   . VAL A 536 ? 0.5982 0.7664 1.0655 0.0002  -0.1278 0.3215  536 VAL A CG2   
4434 N  N     . ILE A 537 ? 0.7567 0.8777 1.1267 0.0000  -0.1261 0.3040  537 ILE A N     
4435 C  CA    . ILE A 537 ? 0.7994 0.9055 1.1494 0.0039  -0.1145 0.2978  537 ILE A CA    
4436 C  C     . ILE A 537 ? 0.7996 0.8917 1.1343 0.0082  -0.0924 0.2752  537 ILE A C     
4437 O  O     . ILE A 537 ? 0.7072 0.7905 1.0502 0.0161  -0.0746 0.2730  537 ILE A O     
4438 C  CB    . ILE A 537 ? 0.8403 0.9397 1.1509 -0.0049 -0.1322 0.2967  537 ILE A CB    
4439 C  CG1   . ILE A 537 ? 0.8597 0.9719 1.1849 -0.0085 -0.1543 0.3205  537 ILE A CG1   
4440 C  CG2   . ILE A 537 ? 0.7819 0.8660 1.0705 -0.0016 -0.1187 0.2891  537 ILE A CG2   
4441 C  CD1   . ILE A 537 ? 0.8565 0.9671 1.1461 -0.0200 -0.1791 0.3176  537 ILE A CD1   
4442 N  N     . TYR A 538 ? 0.7902 0.8795 1.1028 0.0030  -0.0941 0.2583  538 TYR A N     
4443 C  CA    . TYR A 538 ? 0.6969 0.7739 0.9928 0.0060  -0.0758 0.2369  538 TYR A CA    
4444 C  C     . TYR A 538 ? 0.7638 0.8453 1.0533 0.0019  -0.0789 0.2262  538 TYR A C     
4445 O  O     . TYR A 538 ? 0.7162 0.8044 0.9991 -0.0061 -0.0975 0.2301  538 TYR A O     
4446 C  CB    . TYR A 538 ? 0.6617 0.7237 0.9206 0.0025  -0.0742 0.2244  538 TYR A CB    
4447 C  CG    . TYR A 538 ? 0.7240 0.7742 0.9651 0.0042  -0.0582 0.2025  538 TYR A CG    
4448 C  CD1   . TYR A 538 ? 0.7036 0.7494 0.9627 0.0125  -0.0392 0.1972  538 TYR A CD1   
4449 C  CD2   . TYR A 538 ? 0.7458 0.7890 0.9516 -0.0023 -0.0622 0.1874  538 TYR A CD2   
4450 C  CE1   . TYR A 538 ? 0.7880 0.8229 1.0296 0.0134  -0.0266 0.1774  538 TYR A CE1   
4451 C  CE2   . TYR A 538 ? 0.7610 0.7949 0.9524 -0.0012 -0.0489 0.1688  538 TYR A CE2   
4452 C  CZ    . TYR A 538 ? 0.7989 0.8289 1.0081 0.0062  -0.0321 0.1639  538 TYR A CZ    
4453 O  OH    . TYR A 538 ? 0.8259 0.8467 1.0197 0.0067  -0.0208 0.1455  538 TYR A OH    
4454 N  N     . SER A 539 ? 0.7140 0.7909 1.0049 0.0074  -0.0611 0.2129  539 SER A N     
4455 C  CA    . SER A 539 ? 0.6982 0.7796 0.9854 0.0049  -0.0614 0.2038  539 SER A CA    
4456 C  C     . SER A 539 ? 0.7084 0.7781 0.9773 0.0087  -0.0437 0.1835  539 SER A C     
4457 O  O     . SER A 539 ? 0.8210 0.8850 1.1005 0.0173  -0.0266 0.1810  539 SER A O     
4458 C  CB    . SER A 539 ? 0.5364 0.6340 0.8632 0.0095  -0.0597 0.2188  539 SER A CB    
4459 O  OG    . SER A 539 ? 0.7323 0.8343 1.0566 0.0072  -0.0589 0.2111  539 SER A OG    
4460 N  N     . ASP A 540 ? 0.6097 0.6750 0.8511 0.0024  -0.0484 0.1691  540 ASP A N     
4461 C  CA    . ASP A 540 ? 0.7848 0.8414 1.0093 0.0050  -0.0343 0.1507  540 ASP A CA    
4462 C  C     . ASP A 540 ? 0.6789 0.7447 0.9138 0.0061  -0.0319 0.1495  540 ASP A C     
4463 O  O     . ASP A 540 ? 0.9758 1.0530 1.2410 0.0104  -0.0302 0.1635  540 ASP A O     
4464 C  CB    . ASP A 540 ? 0.9053 0.9511 1.0943 -0.0014 -0.0390 0.1367  540 ASP A CB    
4465 C  CG    . ASP A 540 ? 0.8326 0.8670 1.0079 0.0021  -0.0235 0.1207  540 ASP A CG    
4466 O  OD1   . ASP A 540 ? 0.6559 0.6906 0.8358 0.0067  -0.0126 0.1134  540 ASP A OD1   
4467 O  OD2   . ASP A 540 ? 0.8258 0.8509 0.9857 0.0002  -0.0225 0.1160  540 ASP A OD2   
4468 N  N     . THR A 541 ? 0.5953 0.6575 0.8085 0.0026  -0.0317 0.1354  541 THR A N     
4469 C  CA    . THR A 541 ? 0.7438 0.8129 0.9667 0.0059  -0.0243 0.1336  541 THR A CA    
4470 C  C     . THR A 541 ? 0.7917 0.8736 1.0305 0.0003  -0.0385 0.1454  541 THR A C     
4471 O  O     . THR A 541 ? 0.5076 0.6007 0.7718 0.0047  -0.0328 0.1546  541 THR A O     
4472 C  CB    . THR A 541 ? 0.7722 0.8326 0.9671 0.0048  -0.0180 0.1146  541 THR A CB    
4473 O  OG1   . THR A 541 ? 0.8667 0.9156 1.0507 0.0096  -0.0053 0.1045  541 THR A OG1   
4474 C  CG2   . THR A 541 ? 0.6112 0.6789 0.8139 0.0084  -0.0103 0.1136  541 THR A CG2   
4475 N  N     . ASP A 542 ? 0.8744 0.9543 1.0991 -0.0091 -0.0570 0.1455  542 ASP A N     
4476 C  CA    . ASP A 542 ? 0.6234 0.7118 0.8586 -0.0161 -0.0724 0.1533  542 ASP A CA    
4477 C  C     . ASP A 542 ? 0.6311 0.7240 0.8764 -0.0225 -0.0922 0.1675  542 ASP A C     
4478 O  O     . ASP A 542 ? 0.7194 0.8183 0.9742 -0.0296 -0.1079 0.1743  542 ASP A O     
4479 C  CB    . ASP A 542 ? 0.6071 0.6867 0.8128 -0.0224 -0.0784 0.1383  542 ASP A CB    
4480 C  CG    . ASP A 542 ? 0.8407 0.9066 1.0125 -0.0265 -0.0847 0.1276  542 ASP A CG    
4481 O  OD1   . ASP A 542 ? 0.7871 0.8494 0.9558 -0.0235 -0.0805 0.1294  542 ASP A OD1   
4482 O  OD2   . ASP A 542 ? 0.8462 0.9049 0.9953 -0.0324 -0.0933 0.1182  542 ASP A OD2   
4483 N  N     . GLY A 543 ? 0.6628 0.7526 0.9063 -0.0206 -0.0929 0.1724  543 GLY A N     
4484 C  CA    . GLY A 543 ? 0.6158 0.7094 0.8651 -0.0268 -0.1128 0.1859  543 GLY A CA    
4485 C  C     . GLY A 543 ? 0.6121 0.7068 0.8730 -0.0211 -0.1077 0.1963  543 GLY A C     
4486 O  O     . GLY A 543 ? 0.6734 0.7651 0.9399 -0.0124 -0.0884 0.1927  543 GLY A O     
4487 N  N     . PHE A 544 ? 0.6301 0.7282 0.8940 -0.0262 -0.1259 0.2092  544 PHE A N     
4488 C  CA    . PHE A 544 ? 0.7070 0.8076 0.9852 -0.0211 -0.1231 0.2223  544 PHE A CA    
4489 C  C     . PHE A 544 ? 0.7474 0.8450 1.0068 -0.0287 -0.1446 0.2292  544 PHE A C     
4490 O  O     . PHE A 544 ? 0.7304 0.8274 0.9759 -0.0378 -0.1643 0.2283  544 PHE A O     
4491 C  CB    . PHE A 544 ? 0.7455 0.8630 1.0723 -0.0149 -0.1184 0.2416  544 PHE A CB    
4492 C  CG    . PHE A 544 ? 0.5247 0.6569 0.8753 -0.0220 -0.1377 0.2557  544 PHE A CG    
4493 C  CD1   . PHE A 544 ? 0.5990 0.7382 0.9584 -0.0281 -0.1597 0.2721  544 PHE A CD1   
4494 C  CD2   . PHE A 544 ? 0.6220 0.7615 0.9874 -0.0229 -0.1346 0.2536  544 PHE A CD2   
4495 C  CE1   . PHE A 544 ? 0.7975 0.9501 1.1807 -0.0358 -0.1794 0.2854  544 PHE A CE1   
4496 C  CE2   . PHE A 544 ? 0.6431 0.7962 1.0337 -0.0303 -0.1530 0.2676  544 PHE A CE2   
4497 C  CZ    . PHE A 544 ? 0.6539 0.8135 1.0540 -0.0371 -0.1760 0.2832  544 PHE A CZ    
4498 N  N     . PHE A 545 ? 0.7481 0.8426 1.0061 -0.0245 -0.1406 0.2361  545 PHE A N     
4499 C  CA    . PHE A 545 ? 0.7823 0.8759 1.0266 -0.0296 -0.1593 0.2470  545 PHE A CA    
4500 C  C     . PHE A 545 ? 0.8020 0.9116 1.0883 -0.0269 -0.1660 0.2716  545 PHE A C     
4501 O  O     . PHE A 545 ? 0.8141 0.9277 1.1283 -0.0175 -0.1491 0.2790  545 PHE A O     
4502 C  CB    . PHE A 545 ? 0.7441 0.8243 0.9594 -0.0268 -0.1502 0.2406  545 PHE A CB    
4503 C  CG    . PHE A 545 ? 0.8036 0.8693 0.9784 -0.0294 -0.1444 0.2185  545 PHE A CG    
4504 C  CD1   . PHE A 545 ? 0.7497 0.8096 0.9240 -0.0243 -0.1235 0.2038  545 PHE A CD1   
4505 C  CD2   . PHE A 545 ? 0.8460 0.9033 0.9828 -0.0366 -0.1598 0.2128  545 PHE A CD2   
4506 C  CE1   . PHE A 545 ? 0.7072 0.7555 0.8476 -0.0266 -0.1185 0.1851  545 PHE A CE1   
4507 C  CE2   . PHE A 545 ? 0.8618 0.9064 0.9637 -0.0379 -0.1531 0.1936  545 PHE A CE2   
4508 C  CZ    . PHE A 545 ? 0.7037 0.7448 0.8092 -0.0331 -0.1325 0.1805  545 PHE A CZ    
4509 N  N     . ALA A 546 ? 0.7832 0.9013 1.0745 -0.0349 -0.1909 0.2842  546 ALA A N     
4510 C  CA    . ALA A 546 ? 0.8359 0.9717 1.1704 -0.0333 -0.2000 0.3093  546 ALA A CA    
4511 C  C     . ALA A 546 ? 0.9201 1.0569 1.2387 -0.0415 -0.2272 0.3215  546 ALA A C     
4512 O  O     . ALA A 546 ? 0.9383 1.0624 1.2131 -0.0492 -0.2408 0.3097  546 ALA A O     
4513 C  CB    . ALA A 546 ? 0.8017 0.9533 1.1752 -0.0348 -0.2033 0.3169  546 ALA A CB    
4514 N  N     . THR A 547 ? 0.9825 1.1341 1.3367 -0.0390 -0.2347 0.3457  547 THR A N     
4515 C  CA    . THR A 547 ? 0.9652 1.1209 1.3101 -0.0464 -0.2623 0.3610  547 THR A CA    
4516 C  C     . THR A 547 ? 1.0195 1.1981 1.4206 -0.0443 -0.2708 0.3890  547 THR A C     
4517 O  O     . THR A 547 ? 0.9701 1.1589 1.4136 -0.0344 -0.2508 0.3967  547 THR A O     
4518 C  CB    . THR A 547 ? 0.9537 1.0969 1.2639 -0.0435 -0.2593 0.3605  547 THR A CB    
4519 O  OG1   . THR A 547 ? 0.9598 1.1037 1.2482 -0.0521 -0.2882 0.3712  547 THR A OG1   
4520 C  CG2   . THR A 547 ? 0.9322 1.0823 1.2774 -0.0318 -0.2407 0.3759  547 THR A CG2   
4521 N  N     . ILE A 548 ? 1.1182 1.3045 1.5189 -0.0534 -0.3011 0.4042  548 ILE A N     
4522 C  CA    . ILE A 548 ? 1.1409 1.3498 1.5927 -0.0521 -0.3130 0.4340  548 ILE A CA    
4523 C  C     . ILE A 548 ? 1.1349 1.3420 1.5822 -0.0449 -0.3083 0.4470  548 ILE A C     
4524 O  O     . ILE A 548 ? 1.0658 1.2619 1.4692 -0.0504 -0.3236 0.4447  548 ILE A O     
4525 C  CB    . ILE A 548 ? 1.1105 1.3287 1.5644 -0.0664 -0.3503 0.4450  548 ILE A CB    
4526 C  CG1   . ILE A 548 ? 0.8830 1.1060 1.3537 -0.0733 -0.3549 0.4368  548 ILE A CG1   
4527 C  CG2   . ILE A 548 ? 1.0123 1.2514 1.5134 -0.0658 -0.3588 0.4726  548 ILE A CG2   
4528 C  CD1   . ILE A 548 ? 0.9643 1.2037 1.4915 -0.0632 -0.3308 0.4455  548 ILE A CD1   
4529 N  N     . PRO A 549 ? 1.0928 1.3092 1.5827 -0.0323 -0.2870 0.4607  549 PRO A N     
4530 C  CA    . PRO A 549 ? 0.9343 1.1473 1.4213 -0.0250 -0.2811 0.4732  549 PRO A CA    
4531 C  C     . PRO A 549 ? 1.2087 1.4296 1.6871 -0.0329 -0.3128 0.4935  549 PRO A C     
4532 O  O     . PRO A 549 ? 1.1938 1.4322 1.7071 -0.0374 -0.3249 0.5088  549 PRO A O     
4533 C  CB    . PRO A 549 ? 1.0554 1.2813 1.6019 -0.0114 -0.2587 0.4889  549 PRO A CB    
4534 C  CG    . PRO A 549 ? 0.8903 1.1168 1.4515 -0.0090 -0.2418 0.4735  549 PRO A CG    
4535 C  CD    . PRO A 549 ? 1.1662 1.3955 1.7086 -0.0234 -0.2668 0.4659  549 PRO A CD    
4536 N  N     . GLY A 550 ? 1.4502 1.6551 1.8752 -0.0364 -0.3195 0.4855  550 GLY A N     
4537 C  CA    . GLY A 550 ? 1.4107 1.6182 1.8119 -0.0460 -0.3491 0.4963  550 GLY A CA    
4538 C  C     . GLY A 550 ? 1.6936 1.8940 2.0591 -0.0598 -0.3725 0.4804  550 GLY A C     
4539 O  O     . GLY A 550 ? 1.7261 1.9100 2.0536 -0.0614 -0.3664 0.4577  550 GLY A O     
4540 N  N     . ALA A 551 ? 1.3594 1.5694 1.7351 -0.0706 -0.3950 0.4871  551 ALA A N     
4541 C  CA    . ALA A 551 ? 1.4758 1.6784 1.8237 -0.0847 -0.4185 0.4726  551 ALA A CA    
4542 C  C     . ALA A 551 ? 1.4255 1.6046 1.6998 -0.0892 -0.4299 0.4551  551 ALA A C     
4543 O  O     . ALA A 551 ? 1.5906 1.7605 1.8349 -0.0821 -0.4204 0.4562  551 ALA A O     
4544 C  CB    . ALA A 551 ? 1.3030 1.5090 1.6764 -0.0854 -0.4103 0.4622  551 ALA A CB    
4545 N  N     . ASP A 552 ? 1.4473 1.6155 1.6927 -0.1009 -0.4488 0.4388  552 ASP A N     
4546 C  CA    . ASP A 552 ? 1.4939 1.6382 1.6678 -0.1062 -0.4615 0.4208  552 ASP A CA    
4547 C  C     . ASP A 552 ? 1.3901 1.5209 1.5432 -0.1079 -0.4560 0.3983  552 ASP A C     
4548 O  O     . ASP A 552 ? 1.5201 1.6611 1.7149 -0.1067 -0.4464 0.3977  552 ASP A O     
4549 C  CB    . ASP A 552 ? 1.5044 1.6447 1.6586 -0.1186 -0.4908 0.4209  552 ASP A CB    
4550 C  CG    . ASP A 552 ? 1.6246 1.7384 1.7027 -0.1234 -0.5038 0.4008  552 ASP A CG    
4551 O  OD1   . ASP A 552 ? 1.6630 1.7624 1.7019 -0.1168 -0.4896 0.3888  552 ASP A OD1   
4552 O  OD2   . ASP A 552 ? 1.5503 1.6569 1.6071 -0.1334 -0.5278 0.3976  552 ASP A OD2   
4553 N  N     . ALA A 553 ? 1.3319 1.4394 1.4194 -0.1099 -0.4607 0.3801  553 ALA A N     
4554 C  CA    . ALA A 553 ? 1.3731 1.4638 1.4353 -0.1104 -0.4479 0.3535  553 ALA A CA    
4555 C  C     . ALA A 553 ? 1.4304 1.5246 1.5170 -0.1207 -0.4645 0.3481  553 ALA A C     
4556 O  O     . ALA A 553 ? 1.3828 1.4845 1.5059 -0.1177 -0.4461 0.3429  553 ALA A O     
4557 C  CB    . ALA A 553 ? 1.4376 1.5017 1.4240 -0.1114 -0.4513 0.3347  553 ALA A CB    
4558 N  N     . GLU A 554 ? 1.4902 1.5759 1.5567 -0.1322 -0.4908 0.3442  554 GLU A N     
4559 C  CA    . GLU A 554 ? 1.5929 1.6774 1.6792 -0.1428 -0.5036 0.3357  554 GLU A CA    
4560 C  C     . GLU A 554 ? 1.4408 1.5528 1.6039 -0.1421 -0.4970 0.3545  554 GLU A C     
4561 O  O     . GLU A 554 ? 1.4894 1.6052 1.6796 -0.1445 -0.4923 0.3488  554 GLU A O     
4562 C  CB    . GLU A 554 ? 1.5056 1.5756 1.5608 -0.1547 -0.5312 0.3297  554 GLU A CB    
4563 C  CG    . GLU A 554 ? 1.7541 1.7997 1.7343 -0.1536 -0.5380 0.3164  554 GLU A CG    
4564 C  CD    . GLU A 554 ? 1.9066 1.9613 1.8797 -0.1458 -0.5334 0.3337  554 GLU A CD    
4565 O  OE1   . GLU A 554 ? 1.8076 1.8868 1.8351 -0.1428 -0.5288 0.3562  554 GLU A OE1   
4566 O  OE2   . GLU A 554 ? 2.0664 2.1036 1.9802 -0.1420 -0.5331 0.3251  554 GLU A OE2   
4567 N  N     . THR A 555 ? 1.1856 1.3167 1.3844 -0.1382 -0.4952 0.3773  555 THR A N     
4568 C  CA    . THR A 555 ? 1.1834 1.3406 1.4550 -0.1353 -0.4846 0.3960  555 THR A CA    
4569 C  C     . THR A 555 ? 1.1817 1.3452 1.4768 -0.1251 -0.4589 0.3916  555 THR A C     
4570 O  O     . THR A 555 ? 1.1862 1.3620 1.5256 -0.1263 -0.4531 0.3947  555 THR A O     
4571 C  CB    . THR A 555 ? 1.1717 1.3461 1.4720 -0.1291 -0.4806 0.4197  555 THR A CB    
4572 O  OG1   . THR A 555 ? 1.1498 1.3200 1.4309 -0.1389 -0.5059 0.4248  555 THR A OG1   
4573 C  CG2   . THR A 555 ? 1.0723 1.2724 1.4469 -0.1246 -0.4668 0.4386  555 THR A CG2   
4574 N  N     . VAL A 556 ? 1.2811 1.4357 1.5461 -0.1150 -0.4428 0.3846  556 VAL A N     
4575 C  CA    . VAL A 556 ? 1.1175 1.2697 1.3936 -0.1054 -0.4082 0.3701  556 VAL A CA    
4576 C  C     . VAL A 556 ? 1.0345 1.1732 1.2910 -0.1125 -0.4103 0.3476  556 VAL A C     
4577 O  O     . VAL A 556 ? 1.0343 1.1808 1.3239 -0.1097 -0.3944 0.3444  556 VAL A O     
4578 C  CB    . VAL A 556 ? 1.1335 1.2727 1.3756 -0.0944 -0.3827 0.3603  556 VAL A CB    
4579 C  CG1   . VAL A 556 ? 0.9787 1.1047 1.2039 -0.0892 -0.3555 0.3354  556 VAL A CG1   
4580 C  CG2   . VAL A 556 ? 1.0852 1.2411 1.3685 -0.0837 -0.3677 0.3819  556 VAL A CG2   
4581 N  N     . LYS A 557 ? 1.0248 1.1423 1.2268 -0.1213 -0.4297 0.3322  557 LYS A N     
4582 C  CA    . LYS A 557 ? 1.1377 1.2397 1.3191 -0.1276 -0.4317 0.3102  557 LYS A CA    
4583 C  C     . LYS A 557 ? 1.0900 1.2048 1.3143 -0.1384 -0.4529 0.3201  557 LYS A C     
4584 O  O     . LYS A 557 ? 1.0779 1.1919 1.3175 -0.1396 -0.4434 0.3102  557 LYS A O     
4585 C  CB    . LYS A 557 ? 1.2059 1.2800 1.3166 -0.1330 -0.4460 0.2909  557 LYS A CB    
4586 C  CG    . LYS A 557 ? 1.2073 1.2719 1.2765 -0.1247 -0.4345 0.2889  557 LYS A CG    
4587 C  CD    . LYS A 557 ? 1.2907 1.3272 1.2951 -0.1238 -0.4279 0.2625  557 LYS A CD    
4588 C  CE    . LYS A 557 ? 1.3789 1.3978 1.3297 -0.1312 -0.4561 0.2598  557 LYS A CE    
4589 N  NZ    . LYS A 557 ? 1.3264 1.3189 1.2126 -0.1269 -0.4447 0.2367  557 LYS A NZ    
4590 N  N     . LYS A 558 ? 1.2053 1.3301 1.4491 -0.1462 -0.4771 0.3379  558 LYS A N     
4591 C  CA    . LYS A 558 ? 1.1446 1.2763 1.4263 -0.1569 -0.4897 0.3433  558 LYS A CA    
4592 C  C     . LYS A 558 ? 1.0915 1.2497 1.4414 -0.1503 -0.4704 0.3592  558 LYS A C     
4593 O  O     . LYS A 558 ? 1.0705 1.2312 1.4442 -0.1546 -0.4687 0.3556  558 LYS A O     
4594 C  CB    . LYS A 558 ? 1.0143 1.1468 1.2983 -0.1662 -0.5125 0.3553  558 LYS A CB    
4595 C  CG    . LYS A 558 ? 1.2213 1.3283 1.4384 -0.1725 -0.5333 0.3418  558 LYS A CG    
4596 C  CD    . LYS A 558 ? 1.3819 1.4586 1.5409 -0.1772 -0.5397 0.3135  558 LYS A CD    
4597 C  CE    . LYS A 558 ? 1.3670 1.4330 1.4849 -0.1663 -0.5208 0.2992  558 LYS A CE    
4598 N  NZ    . LYS A 558 ? 1.4404 1.4776 1.5061 -0.1704 -0.5251 0.2722  558 LYS A NZ    
4599 N  N     . LYS A 559 ? 1.0224 1.1997 1.4042 -0.1392 -0.4544 0.3773  559 LYS A N     
4600 C  CA    . LYS A 559 ? 0.9824 1.1833 1.4256 -0.1303 -0.4322 0.3914  559 LYS A CA    
4601 C  C     . LYS A 559 ? 0.9487 1.1440 1.3837 -0.1221 -0.4082 0.3747  559 LYS A C     
4602 O  O     . LYS A 559 ? 0.9843 1.1927 1.4602 -0.1191 -0.3942 0.3790  559 LYS A O     
4603 C  CB    . LYS A 559 ? 1.0349 1.2525 1.5075 -0.1187 -0.4178 0.4114  559 LYS A CB    
4604 C  CG    . LYS A 559 ? 1.0281 1.2542 1.5197 -0.1261 -0.4348 0.4294  559 LYS A CG    
4605 C  CD    . LYS A 559 ? 0.9256 1.1585 1.4507 -0.1386 -0.4488 0.4361  559 LYS A CD    
4606 C  CE    . LYS A 559 ? 1.0716 1.3294 1.6647 -0.1310 -0.4277 0.4553  559 LYS A CE    
4607 N  NZ    . LYS A 559 ? 0.9731 1.2396 1.6032 -0.1434 -0.4428 0.4686  559 LYS A NZ    
4608 N  N     . ALA A 560 ? 1.0066 1.1785 1.3841 -0.1181 -0.3962 0.3518  560 ALA A N     
4609 C  CA    . ALA A 560 ? 0.9891 1.1499 1.3506 -0.1110 -0.3680 0.3306  560 ALA A CA    
4610 C  C     . ALA A 560 ? 0.9614 1.1154 1.3209 -0.1208 -0.3783 0.3191  560 ALA A C     
4611 O  O     . ALA A 560 ? 1.0249 1.1838 1.4051 -0.1161 -0.3584 0.3143  560 ALA A O     
4612 C  CB    . ALA A 560 ? 0.8269 0.9651 1.1290 -0.1058 -0.3557 0.3102  560 ALA A CB    
4613 N  N     . MET A 561 ? 0.9528 1.0944 1.2864 -0.1343 -0.4096 0.3145  561 MET A N     
4614 C  CA    . MET A 561 ? 0.9769 1.1103 1.3104 -0.1445 -0.4217 0.3043  561 MET A CA    
4615 C  C     . MET A 561 ? 1.0860 1.2447 1.4869 -0.1491 -0.4290 0.3263  561 MET A C     
4616 O  O     . MET A 561 ? 1.0848 1.2446 1.5038 -0.1513 -0.4224 0.3216  561 MET A O     
4617 C  CB    . MET A 561 ? 1.0291 1.1396 1.3149 -0.1576 -0.4539 0.2928  561 MET A CB    
4618 C  CG    . MET A 561 ? 1.1753 1.2600 1.3926 -0.1525 -0.4457 0.2710  561 MET A CG    
4619 S  SD    . MET A 561 ? 1.3918 1.4486 1.5649 -0.1536 -0.4357 0.2398  561 MET A SD    
4620 C  CE    . MET A 561 ? 1.3823 1.4095 1.4763 -0.1538 -0.4458 0.2220  561 MET A CE    
4621 N  N     . GLU A 562 ? 0.9739 1.1517 1.4119 -0.1502 -0.4394 0.3502  562 GLU A N     
4622 C  CA    . GLU A 562 ? 0.9340 1.1327 1.4343 -0.1519 -0.4345 0.3698  562 GLU A CA    
4623 C  C     . GLU A 562 ? 0.9791 1.1977 1.5184 -0.1379 -0.4042 0.3761  562 GLU A C     
4624 O  O     . GLU A 562 ? 1.0100 1.2375 1.5829 -0.1394 -0.3968 0.3802  562 GLU A O     
4625 C  CB    . GLU A 562 ? 0.9149 1.1262 1.4412 -0.1533 -0.4423 0.3913  562 GLU A CB    
4626 C  CG    . GLU A 562 ? 0.9603 1.1549 1.4568 -0.1681 -0.4735 0.3884  562 GLU A CG    
4627 C  CD    . GLU A 562 ? 1.1169 1.3265 1.6432 -0.1693 -0.4807 0.4113  562 GLU A CD    
4628 O  OE1   . GLU A 562 ? 1.0482 1.2815 1.6253 -0.1602 -0.4616 0.4305  562 GLU A OE1   
4629 O  OE2   . GLU A 562 ? 1.0795 1.2768 1.5777 -0.1790 -0.5048 0.4099  562 GLU A OE2   
4630 N  N     . PHE A 563 ? 0.9468 1.1660 1.4743 -0.1235 -0.3799 0.3733  563 PHE A N     
4631 C  CA    . PHE A 563 ? 0.8274 1.0555 1.3777 -0.1089 -0.3433 0.3725  563 PHE A CA    
4632 C  C     . PHE A 563 ? 0.8754 1.0891 1.4021 -0.1095 -0.3306 0.3506  563 PHE A C     
4633 O  O     . PHE A 563 ? 0.9535 1.1790 1.5118 -0.1031 -0.3104 0.3548  563 PHE A O     
4634 C  CB    . PHE A 563 ? 0.6795 0.9025 1.2099 -0.0950 -0.3202 0.3680  563 PHE A CB    
4635 C  CG    . PHE A 563 ? 0.7275 0.9518 1.2658 -0.0805 -0.2832 0.3603  563 PHE A CG    
4636 C  CD1   . PHE A 563 ? 0.7154 0.9620 1.3084 -0.0709 -0.2657 0.3792  563 PHE A CD1   
4637 C  CD2   . PHE A 563 ? 0.8459 1.0491 1.3364 -0.0761 -0.2661 0.3344  563 PHE A CD2   
4638 C  CE1   . PHE A 563 ? 0.8689 1.1147 1.4648 -0.0573 -0.2322 0.3711  563 PHE A CE1   
4639 C  CE2   . PHE A 563 ? 0.7948 0.9984 1.2906 -0.0635 -0.2342 0.3269  563 PHE A CE2   
4640 C  CZ    . PHE A 563 ? 0.8158 1.0398 1.3624 -0.0540 -0.2174 0.3446  563 PHE A CZ    
4641 N  N     . LEU A 564 ? 0.9814 1.1696 1.4523 -0.1165 -0.3416 0.3278  564 LEU A N     
4642 C  CA    . LEU A 564 ? 0.9141 1.0878 1.3615 -0.1170 -0.3304 0.3071  564 LEU A CA    
4643 C  C     . LEU A 564 ? 0.9030 1.0863 1.3875 -0.1264 -0.3426 0.3161  564 LEU A C     
4644 O  O     . LEU A 564 ? 0.9855 1.1725 1.4838 -0.1216 -0.3232 0.3123  564 LEU A O     
4645 C  CB    . LEU A 564 ? 0.9630 1.1076 1.3453 -0.1226 -0.3414 0.2829  564 LEU A CB    
4646 C  CG    . LEU A 564 ? 0.8760 1.0083 1.2172 -0.1119 -0.3213 0.2690  564 LEU A CG    
4647 C  CD1   . LEU A 564 ? 0.9058 1.0104 1.1855 -0.1171 -0.3310 0.2459  564 LEU A CD1   
4648 C  CD2   . LEU A 564 ? 0.8024 0.9400 1.1545 -0.0988 -0.2868 0.2633  564 LEU A CD2   
4649 N  N     . LYS A 565 ? 1.0083 1.1959 1.5099 -0.1401 -0.3753 0.3286  565 LYS A N     
4650 C  CA    . LYS A 565 ? 0.9361 1.1347 1.4800 -0.1501 -0.3888 0.3403  565 LYS A CA    
4651 C  C     . LYS A 565 ? 0.8992 1.1282 1.5070 -0.1408 -0.3676 0.3635  565 LYS A C     
4652 O  O     . LYS A 565 ? 0.8954 1.1319 1.5304 -0.1411 -0.3583 0.3668  565 LYS A O     
4653 C  CB    . LYS A 565 ? 0.9287 1.1201 1.4727 -0.1659 -0.4230 0.3474  565 LYS A CB    
4654 C  CG    . LYS A 565 ? 1.1893 1.3865 1.7759 -0.1751 -0.4294 0.3608  565 LYS A CG    
4655 C  CD    . LYS A 565 ? 1.2129 1.3838 1.7705 -0.1918 -0.4601 0.3505  565 LYS A CD    
4656 C  CE    . LYS A 565 ? 1.1302 1.3017 1.7233 -0.2004 -0.4647 0.3586  565 LYS A CE    
4657 N  NZ    . LYS A 565 ? 1.0613 1.2481 1.6833 -0.1913 -0.4386 0.3611  565 LYS A NZ    
4658 N  N     . TYR A 566 ? 0.8459 1.0922 1.4781 -0.1316 -0.3586 0.3801  566 TYR A N     
4659 C  CA    . TYR A 566 ? 0.8658 1.1393 1.5565 -0.1208 -0.3358 0.4020  566 TYR A CA    
4660 C  C     . TYR A 566 ? 0.8751 1.1459 1.5555 -0.1059 -0.2984 0.3895  566 TYR A C     
4661 O  O     . TYR A 566 ? 0.9091 1.1959 1.6282 -0.1009 -0.2822 0.4005  566 TYR A O     
4662 C  CB    . TYR A 566 ? 0.9537 1.2386 1.6634 -0.1139 -0.3312 0.4190  566 TYR A CB    
4663 C  CG    . TYR A 566 ? 1.0450 1.3521 1.8000 -0.0970 -0.2988 0.4352  566 TYR A CG    
4664 C  CD1   . TYR A 566 ? 0.7741 1.0966 1.5779 -0.0977 -0.2902 0.4549  566 TYR A CD1   
4665 C  CD2   . TYR A 566 ? 0.9262 1.2317 1.6666 -0.0803 -0.2728 0.4279  566 TYR A CD2   
4666 C  CE1   . TYR A 566 ? 0.6912 1.0317 1.5323 -0.0814 -0.2588 0.4689  566 TYR A CE1   
4667 C  CE2   . TYR A 566 ? 0.9499 1.2721 1.7278 -0.0640 -0.2423 0.4409  566 TYR A CE2   
4668 C  CZ    . TYR A 566 ? 1.0008 1.3427 1.8310 -0.0640 -0.2360 0.4623  566 TYR A CZ    
4669 O  OH    . TYR A 566 ? 1.0845 1.4407 1.9479 -0.0469 -0.2038 0.4743  566 TYR A OH    
4670 N  N     . ILE A 567 ? 0.8704 1.1206 1.4979 -0.0985 -0.2839 0.3668  567 ILE A N     
4671 C  CA    . ILE A 567 ? 0.7152 0.9624 1.3319 -0.0840 -0.2486 0.3551  567 ILE A CA    
4672 C  C     . ILE A 567 ? 0.8507 1.0850 1.4449 -0.0884 -0.2453 0.3378  567 ILE A C     
4673 O  O     . ILE A 567 ? 0.8349 1.0751 1.4403 -0.0790 -0.2203 0.3368  567 ILE A O     
4674 C  CB    . ILE A 567 ? 0.8034 1.0357 1.3788 -0.0743 -0.2338 0.3400  567 ILE A CB    
4675 C  CG1   . ILE A 567 ? 0.9173 1.1509 1.4932 -0.0580 -0.1974 0.3335  567 ILE A CG1   
4676 C  CG2   . ILE A 567 ? 0.7962 1.0017 1.3109 -0.0822 -0.2467 0.3152  567 ILE A CG2   
4677 C  CD1   . ILE A 567 ? 0.9254 1.1830 1.5559 -0.0469 -0.1806 0.3571  567 ILE A CD1   
4678 N  N     . ASN A 568 ? 0.8552 1.0713 1.4173 -0.1020 -0.2697 0.3244  568 ASN A N     
4679 C  CA    . ASN A 568 ? 0.7085 0.9116 1.2512 -0.1061 -0.2672 0.3088  568 ASN A CA    
4680 C  C     . ASN A 568 ? 0.7601 0.9803 1.3529 -0.1119 -0.2723 0.3265  568 ASN A C     
4681 O  O     . ASN A 568 ? 0.9178 1.1339 1.5070 -0.1109 -0.2611 0.3189  568 ASN A O     
4682 C  CB    . ASN A 568 ? 0.8904 1.0669 1.3831 -0.1178 -0.2908 0.2888  568 ASN A CB    
4683 C  CG    . ASN A 568 ? 0.8561 1.0124 1.2929 -0.1101 -0.2763 0.2655  568 ASN A CG    
4684 O  OD1   . ASN A 568 ? 0.7173 0.8774 1.1509 -0.0972 -0.2486 0.2614  568 ASN A OD1   
4685 N  ND2   . ASN A 568 ? 0.9568 1.0912 1.3492 -0.1181 -0.2951 0.2502  568 ASN A ND2   
4686 N  N     . ALA A 569 ? 0.9220 1.1622 1.5632 -0.1180 -0.2891 0.3511  569 ALA A N     
4687 C  CA    . ALA A 569 ? 0.8625 1.1232 1.5597 -0.1222 -0.2909 0.3719  569 ALA A CA    
4688 C  C     . ALA A 569 ? 0.8484 1.1312 1.5813 -0.1054 -0.2563 0.3861  569 ALA A C     
4689 O  O     . ALA A 569 ? 0.9732 1.2691 1.7399 -0.1047 -0.2469 0.3974  569 ALA A O     
4690 C  CB    . ALA A 569 ? 0.6969 0.9694 1.4321 -0.1353 -0.3213 0.3932  569 ALA A CB    
4691 N  N     . LYS A 570 ? 0.7570 1.0432 1.4823 -0.0916 -0.2369 0.3858  570 LYS A N     
4692 C  CA    . LYS A 570 ? 0.7394 1.0418 1.4899 -0.0739 -0.2022 0.3957  570 LYS A CA    
4693 C  C     . LYS A 570 ? 0.8423 1.1281 1.5478 -0.0629 -0.1751 0.3718  570 LYS A C     
4694 O  O     . LYS A 570 ? 0.8235 1.1188 1.5418 -0.0477 -0.1454 0.3765  570 LYS A O     
4695 C  CB    . LYS A 570 ? 0.5980 0.9123 1.3679 -0.0642 -0.1952 0.4091  570 LYS A CB    
4696 C  CG    . LYS A 570 ? 0.8351 1.1740 1.6639 -0.0710 -0.2150 0.4393  570 LYS A CG    
4697 C  CD    . LYS A 570 ? 0.8609 1.2157 1.7196 -0.0561 -0.1966 0.4563  570 LYS A CD    
4698 C  CE    . LYS A 570 ? 0.8330 1.2021 1.7400 -0.0574 -0.1904 0.4820  570 LYS A CE    
4699 N  NZ    . LYS A 570 ? 0.8925 1.2681 1.8187 -0.0565 -0.1766 0.4871  570 LYS A NZ    
4700 N  N     . LEU A 571 ? 0.7745 1.0352 1.4272 -0.0698 -0.1846 0.3467  571 LEU A N     
4701 C  CA    . LEU A 571 ? 0.7324 0.9776 1.3423 -0.0601 -0.1611 0.3243  571 LEU A CA    
4702 C  C     . LEU A 571 ? 0.7696 1.0136 1.3801 -0.0628 -0.1562 0.3205  571 LEU A C     
4703 O  O     . LEU A 571 ? 0.8486 1.0859 1.4582 -0.0768 -0.1791 0.3188  571 LEU A O     
4704 C  CB    . LEU A 571 ? 0.8262 1.0462 1.3797 -0.0642 -0.1711 0.3001  571 LEU A CB    
4705 C  CG    . LEU A 571 ? 0.6570 0.8738 1.1955 -0.0542 -0.1592 0.2964  571 LEU A CG    
4706 C  CD1   . LEU A 571 ? 0.7419 0.9371 1.2327 -0.0611 -0.1753 0.2785  571 LEU A CD1   
4707 C  CD2   . LEU A 571 ? 0.5878 0.8033 1.1152 -0.0385 -0.1263 0.2876  571 LEU A CD2   
4708 N  N     . PRO A 572 ? 0.6344 0.8834 1.2450 -0.0498 -0.1273 0.3188  572 PRO A N     
4709 C  CA    . PRO A 572 ? 0.5886 0.8413 1.2087 -0.0512 -0.1210 0.3210  572 PRO A CA    
4710 C  C     . PRO A 572 ? 0.8049 1.0339 1.3772 -0.0579 -0.1285 0.2966  572 PRO A C     
4711 O  O     . PRO A 572 ? 0.7744 0.9881 1.3032 -0.0515 -0.1173 0.2762  572 PRO A O     
4712 C  CB    . PRO A 572 ? 0.7422 1.0060 1.3701 -0.0332 -0.0865 0.3256  572 PRO A CB    
4713 C  CG    . PRO A 572 ? 0.7141 0.9672 1.3114 -0.0238 -0.0753 0.3119  572 PRO A CG    
4714 C  CD    . PRO A 572 ? 0.7307 0.9827 1.3353 -0.0328 -0.0992 0.3168  572 PRO A CD    
4715 N  N     . GLY A 573 ? 0.8909 1.1170 1.4738 -0.0708 -0.1479 0.2995  573 GLY A N     
4716 C  CA    . GLY A 573 ? 0.7052 0.9117 1.2513 -0.0752 -0.1506 0.2800  573 GLY A CA    
4717 C  C     . GLY A 573 ? 0.7296 0.9115 1.2239 -0.0793 -0.1622 0.2560  573 GLY A C     
4718 O  O     . GLY A 573 ? 0.8239 0.9991 1.3136 -0.0882 -0.1844 0.2554  573 GLY A O     
4719 N  N     . ALA A 574 ? 0.7626 0.9314 1.2172 -0.0724 -0.1469 0.2366  574 ALA A N     
4720 C  CA    . ALA A 574 ? 0.6969 0.8425 1.1020 -0.0753 -0.1548 0.2135  574 ALA A CA    
4721 C  C     . ALA A 574 ? 0.7743 0.9172 1.1625 -0.0708 -0.1531 0.2089  574 ALA A C     
4722 O  O     . ALA A 574 ? 0.8618 0.9868 1.2092 -0.0719 -0.1570 0.1909  574 ALA A O     
4723 C  CB    . ALA A 574 ? 0.8090 0.9447 1.1826 -0.0685 -0.1375 0.1970  574 ALA A CB    
4724 N  N     . LEU A 575 ? 0.5913 0.7514 1.0107 -0.0655 -0.1468 0.2254  575 LEU A N     
4725 C  CA    . LEU A 575 ? 0.6700 0.8281 1.0771 -0.0606 -0.1441 0.2229  575 LEU A CA    
4726 C  C     . LEU A 575 ? 0.7073 0.8624 1.1181 -0.0718 -0.1715 0.2288  575 LEU A C     
4727 O  O     . LEU A 575 ? 0.8582 1.0249 1.3049 -0.0794 -0.1872 0.2459  575 LEU A O     
4728 C  CB    . LEU A 575 ? 0.7267 0.9033 1.1653 -0.0483 -0.1232 0.2377  575 LEU A CB    
4729 C  CG    . LEU A 575 ? 0.8593 1.0352 1.2842 -0.0361 -0.0956 0.2285  575 LEU A CG    
4730 C  CD1   . LEU A 575 ? 0.7405 0.9340 1.1985 -0.0239 -0.0754 0.2444  575 LEU A CD1   
4731 C  CD2   . LEU A 575 ? 0.7913 0.9487 1.1693 -0.0325 -0.0889 0.2061  575 LEU A CD2   
4732 N  N     . GLU A 576 ? 0.8355 0.9751 1.2090 -0.0727 -0.1776 0.2154  576 GLU A N     
4733 C  CA    . GLU A 576 ? 0.9368 1.0699 1.3035 -0.0834 -0.2045 0.2181  576 GLU A CA    
4734 C  C     . GLU A 576 ? 0.8425 0.9664 1.1787 -0.0790 -0.2016 0.2100  576 GLU A C     
4735 O  O     . GLU A 576 ? 0.7835 0.8956 1.0862 -0.0728 -0.1867 0.1933  576 GLU A O     
4736 C  CB    . GLU A 576 ? 0.9764 1.0913 1.3181 -0.0949 -0.2240 0.2055  576 GLU A CB    
4737 C  CG    . GLU A 576 ? 1.1645 1.2621 1.4721 -0.1030 -0.2464 0.1971  576 GLU A CG    
4738 C  CD    . GLU A 576 ? 1.1686 1.2531 1.4698 -0.1165 -0.2722 0.1934  576 GLU A CD    
4739 O  OE1   . GLU A 576 ? 1.2705 1.3665 1.6108 -0.1226 -0.2808 0.2070  576 GLU A OE1   
4740 O  OE2   . GLU A 576 ? 1.2282 1.2903 1.4854 -0.1208 -0.2834 0.1768  576 GLU A OE2   
4741 N  N     . LEU A 577 ? 0.8183 0.9489 1.1687 -0.0822 -0.2162 0.2234  577 LEU A N     
4742 C  CA    . LEU A 577 ? 0.8352 0.9576 1.1590 -0.0795 -0.2173 0.2190  577 LEU A CA    
4743 C  C     . LEU A 577 ? 0.8665 0.9720 1.1564 -0.0908 -0.2436 0.2111  577 LEU A C     
4744 O  O     . LEU A 577 ? 0.9143 1.0214 1.2180 -0.1015 -0.2669 0.2188  577 LEU A O     
4745 C  CB    . LEU A 577 ? 0.7815 0.9219 1.1420 -0.0748 -0.2158 0.2401  577 LEU A CB    
4746 C  CG    . LEU A 577 ? 0.8037 0.9406 1.1490 -0.0658 -0.2027 0.2379  577 LEU A CG    
4747 C  CD1   . LEU A 577 ? 0.6597 0.7942 0.9985 -0.0538 -0.1726 0.2269  577 LEU A CD1   
4748 C  CD2   . LEU A 577 ? 0.5683 0.7225 0.9522 -0.0635 -0.2079 0.2612  577 LEU A CD2   
4749 N  N     . GLU A 578 ? 0.8543 0.9432 1.0998 -0.0883 -0.2399 0.1960  578 GLU A N     
4750 C  CA    . GLU A 578 ? 0.8962 0.9666 1.1023 -0.0970 -0.2617 0.1865  578 GLU A CA    
4751 C  C     . GLU A 578 ? 0.9722 1.0397 1.1590 -0.0946 -0.2653 0.1902  578 GLU A C     
4752 O  O     . GLU A 578 ? 1.0937 1.1670 1.2847 -0.0851 -0.2461 0.1925  578 GLU A O     
4753 C  CB    . GLU A 578 ? 0.9866 1.0364 1.1505 -0.0967 -0.2550 0.1635  578 GLU A CB    
4754 C  CG    . GLU A 578 ? 0.9632 1.0167 1.1418 -0.0934 -0.2389 0.1577  578 GLU A CG    
4755 C  CD    . GLU A 578 ? 1.1000 1.1352 1.2377 -0.0907 -0.2286 0.1361  578 GLU A CD    
4756 O  OE1   . GLU A 578 ? 1.1518 1.1778 1.2580 -0.0861 -0.2212 0.1272  578 GLU A OE1   
4757 O  OE2   . GLU A 578 ? 1.2206 1.2510 1.3592 -0.0930 -0.2279 0.1292  578 GLU A OE2   
4758 N  N     . TYR A 579 ? 0.9183 0.9756 1.0828 -0.1035 -0.2907 0.1907  579 TYR A N     
4759 C  CA    . TYR A 579 ? 0.9461 0.9974 1.0833 -0.1023 -0.2971 0.1930  579 TYR A CA    
4760 C  C     . TYR A 579 ? 0.9838 1.0143 1.0687 -0.0982 -0.2855 0.1721  579 TYR A C     
4761 O  O     . TYR A 579 ? 1.0663 1.0786 1.1177 -0.1036 -0.2961 0.1578  579 TYR A O     
4762 C  CB    . TYR A 579 ? 1.0330 1.0814 1.1657 -0.1137 -0.3302 0.2020  579 TYR A CB    
4763 C  CG    . TYR A 579 ? 1.1291 1.1708 1.2307 -0.1137 -0.3409 0.2059  579 TYR A CG    
4764 C  CD1   . TYR A 579 ? 1.0988 1.1175 1.1427 -0.1136 -0.3427 0.1888  579 TYR A CD1   
4765 C  CD2   . TYR A 579 ? 1.0825 1.1412 1.2127 -0.1135 -0.3496 0.2278  579 TYR A CD2   
4766 C  CE1   . TYR A 579 ? 1.0304 1.0433 1.0444 -0.1131 -0.3519 0.1936  579 TYR A CE1   
4767 C  CE2   . TYR A 579 ? 1.1749 1.2281 1.2766 -0.1134 -0.3600 0.2329  579 TYR A CE2   
4768 C  CZ    . TYR A 579 ? 1.1139 1.1441 1.1565 -0.1132 -0.3610 0.2158  579 TYR A CZ    
4769 O  OH    . TYR A 579 ? 1.0925 1.1173 1.1050 -0.1125 -0.3704 0.2219  579 TYR A OH    
4770 N  N     . GLU A 580 ? 0.8977 0.9303 0.9768 -0.0885 -0.2637 0.1706  580 GLU A N     
4771 C  CA    . GLU A 580 ? 0.9596 0.9760 0.9967 -0.0837 -0.2491 0.1524  580 GLU A CA    
4772 C  C     . GLU A 580 ? 1.0012 1.0095 1.0055 -0.0815 -0.2514 0.1540  580 GLU A C     
4773 O  O     . GLU A 580 ? 1.2086 1.2083 1.1870 -0.0755 -0.2348 0.1435  580 GLU A O     
4774 C  CB    . GLU A 580 ? 1.0274 1.0504 1.0804 -0.0747 -0.2212 0.1469  580 GLU A CB    
4775 C  CG    . GLU A 580 ? 1.1391 1.1479 1.1613 -0.0728 -0.2097 0.1268  580 GLU A CG    
4776 C  CD    . GLU A 580 ? 1.2210 1.2374 1.2668 -0.0688 -0.1926 0.1221  580 GLU A CD    
4777 O  OE1   . GLU A 580 ? 1.0622 1.0882 1.1271 -0.0617 -0.1751 0.1260  580 GLU A OE1   
4778 O  OE2   . GLU A 580 ? 1.2268 1.2388 1.2713 -0.0725 -0.1970 0.1145  580 GLU A OE2   
4779 N  N     . GLY A 581 ? 1.0097 1.0214 1.0156 -0.0862 -0.2717 0.1679  581 GLY A N     
4780 C  CA    . GLY A 581 ? 1.0357 1.0383 1.0055 -0.0848 -0.2763 0.1697  581 GLY A CA    
4781 C  C     . GLY A 581 ? 1.0737 1.0902 1.0656 -0.0833 -0.2820 0.1913  581 GLY A C     
4782 O  O     . GLY A 581 ? 1.0487 1.0819 1.0838 -0.0788 -0.2709 0.2032  581 GLY A O     
4783 N  N     . PHE A 582 ? 0.9515 0.9603 0.9122 -0.0866 -0.2995 0.1964  582 PHE A N     
4784 C  CA    . PHE A 582 ? 1.0056 1.0254 0.9789 -0.0845 -0.3051 0.2169  582 PHE A CA    
4785 C  C     . PHE A 582 ? 1.0713 1.0825 1.0120 -0.0769 -0.2888 0.2142  582 PHE A C     
4786 O  O     . PHE A 582 ? 1.1246 1.1188 1.0209 -0.0759 -0.2833 0.1981  582 PHE A O     
4787 C  CB    . PHE A 582 ? 0.9656 0.9841 0.9272 -0.0939 -0.3382 0.2271  582 PHE A CB    
4788 C  CG    . PHE A 582 ? 1.1427 1.1729 1.1164 -0.0921 -0.3462 0.2497  582 PHE A CG    
4789 C  CD1   . PHE A 582 ? 1.1633 1.2158 1.1938 -0.0908 -0.3465 0.2700  582 PHE A CD1   
4790 C  CD2   . PHE A 582 ? 1.2557 1.2749 1.1842 -0.0909 -0.3525 0.2516  582 PHE A CD2   
4791 C  CE1   . PHE A 582 ? 1.2388 1.3024 1.2824 -0.0887 -0.3539 0.2919  582 PHE A CE1   
4792 C  CE2   . PHE A 582 ? 1.3154 1.3458 1.2552 -0.0891 -0.3602 0.2737  582 PHE A CE2   
4793 C  CZ    . PHE A 582 ? 1.2382 1.2907 1.2364 -0.0881 -0.3613 0.2940  582 PHE A CZ    
4794 N  N     . TYR A 583 ? 0.9944 1.0176 0.9593 -0.0713 -0.2802 0.2310  583 TYR A N     
4795 C  CA    . TYR A 583 ? 1.0701 1.0873 1.0124 -0.0640 -0.2631 0.2314  583 TYR A CA    
4796 C  C     . TYR A 583 ? 1.1792 1.2053 1.1304 -0.0628 -0.2730 0.2545  583 TYR A C     
4797 O  O     . TYR A 583 ? 1.1921 1.2343 1.1895 -0.0616 -0.2745 0.2709  583 TYR A O     
4798 C  CB    . TYR A 583 ? 0.8611 0.8820 0.8282 -0.0564 -0.2339 0.2249  583 TYR A CB    
4799 C  CG    . TYR A 583 ? 0.9667 0.9806 0.9273 -0.0573 -0.2242 0.2036  583 TYR A CG    
4800 C  CD1   . TYR A 583 ? 1.0250 1.0227 0.9407 -0.0575 -0.2203 0.1865  583 TYR A CD1   
4801 C  CD2   . TYR A 583 ? 0.9835 1.0071 0.9829 -0.0573 -0.2186 0.2017  583 TYR A CD2   
4802 C  CE1   . TYR A 583 ? 0.9746 0.9663 0.8859 -0.0580 -0.2119 0.1683  583 TYR A CE1   
4803 C  CE2   . TYR A 583 ? 0.9748 0.9925 0.9680 -0.0580 -0.2103 0.1836  583 TYR A CE2   
4804 C  CZ    . TYR A 583 ? 1.0413 1.0432 0.9913 -0.0585 -0.2074 0.1671  583 TYR A CZ    
4805 O  OH    . TYR A 583 ? 1.0846 1.0811 1.0300 -0.0589 -0.1993 0.1503  583 TYR A OH    
4806 N  N     . LYS A 584 ? 1.0951 1.1107 1.0016 -0.0624 -0.2792 0.2563  584 LYS A N     
4807 C  CA    . LYS A 584 ? 1.0823 1.1053 0.9911 -0.0615 -0.2904 0.2790  584 LYS A CA    
4808 C  C     . LYS A 584 ? 1.1685 1.2046 1.1220 -0.0538 -0.2712 0.2939  584 LYS A C     
4809 O  O     . LYS A 584 ? 1.0654 1.1163 1.0567 -0.0538 -0.2803 0.3138  584 LYS A O     
4810 C  CB    . LYS A 584 ? 1.1672 1.1753 1.0172 -0.0601 -0.2930 0.2768  584 LYS A CB    
4811 C  CG    . LYS A 584 ? 1.3451 1.3533 1.1723 -0.0652 -0.3220 0.2917  584 LYS A CG    
4812 C  CD    . LYS A 584 ? 1.4514 1.4424 1.2138 -0.0629 -0.3227 0.2867  584 LYS A CD    
4813 C  CE    . LYS A 584 ? 1.4476 1.4443 1.2104 -0.0552 -0.3097 0.3055  584 LYS A CE    
4814 N  NZ    . LYS A 584 ? 1.4498 1.4314 1.1487 -0.0527 -0.3121 0.3043  584 LYS A NZ    
4815 N  N     . ARG A 585 ? 1.1138 1.1441 1.0643 -0.0472 -0.2448 0.2846  585 ARG A N     
4816 C  CA    . ARG A 585 ? 0.9380 0.9766 0.9284 -0.0399 -0.2250 0.2954  585 ARG A CA    
4817 C  C     . ARG A 585 ? 1.0981 1.1324 1.1009 -0.0365 -0.2012 0.2768  585 ARG A C     
4818 O  O     . ARG A 585 ? 1.0231 1.0480 0.9994 -0.0389 -0.1983 0.2571  585 ARG A O     
4819 C  CB    . ARG A 585 ? 1.0413 1.0765 1.0144 -0.0351 -0.2182 0.3085  585 ARG A CB    
4820 C  CG    . ARG A 585 ? 1.1995 1.2306 1.1300 -0.0387 -0.2396 0.3175  585 ARG A CG    
4821 C  CD    . ARG A 585 ? 1.2031 1.2292 1.1105 -0.0332 -0.2286 0.3278  585 ARG A CD    
4822 N  NE    . ARG A 585 ? 1.2325 1.2700 1.1694 -0.0302 -0.2329 0.3542  585 ARG A NE    
4823 C  CZ    . ARG A 585 ? 1.4768 1.5216 1.4105 -0.0335 -0.2573 0.3719  585 ARG A CZ    
4824 N  NH1   . ARG A 585 ? 1.4679 1.5085 1.3686 -0.0407 -0.2812 0.3655  585 ARG A NH1   
4825 N  NH2   . ARG A 585 ? 1.5295 1.5853 1.4941 -0.0297 -0.2586 0.3967  585 ARG A NH2   
4826 N  N     . GLY A 586 ? 1.1611 1.2017 1.2040 -0.0305 -0.1843 0.2832  586 GLY A N     
4827 C  CA    . GLY A 586 ? 1.0402 1.0764 1.0957 -0.0270 -0.1622 0.2667  586 GLY A CA    
4828 C  C     . GLY A 586 ? 1.0306 1.0690 1.1210 -0.0199 -0.1438 0.2754  586 GLY A C     
4829 O  O     . GLY A 586 ? 1.0412 1.0893 1.1671 -0.0170 -0.1471 0.2920  586 GLY A O     
4830 N  N     . PHE A 587 ? 1.0053 1.0344 1.0874 -0.0170 -0.1247 0.2646  587 PHE A N     
4831 C  CA    . PHE A 587 ? 0.9039 0.9313 1.0173 -0.0108 -0.1067 0.2694  587 PHE A CA    
4832 C  C     . PHE A 587 ? 0.9296 0.9545 1.0607 -0.0090 -0.0926 0.2518  587 PHE A C     
4833 O  O     . PHE A 587 ? 1.0159 1.0352 1.1250 -0.0117 -0.0884 0.2334  587 PHE A O     
4834 C  CB    . PHE A 587 ? 0.9073 0.9257 1.0025 -0.0094 -0.0956 0.2712  587 PHE A CB    
4835 C  CG    . PHE A 587 ? 0.9173 0.9333 1.0456 -0.0037 -0.0814 0.2817  587 PHE A CG    
4836 C  CD1   . PHE A 587 ? 1.0127 1.0230 1.1647 -0.0006 -0.0651 0.2696  587 PHE A CD1   
4837 C  CD2   . PHE A 587 ? 0.9616 0.9797 1.0963 -0.0013 -0.0850 0.3037  587 PHE A CD2   
4838 C  CE1   . PHE A 587 ? 0.9981 1.0032 1.1796 0.0046  -0.0525 0.2779  587 PHE A CE1   
4839 C  CE2   . PHE A 587 ? 1.1610 1.1753 1.3276 0.0040  -0.0719 0.3135  587 PHE A CE2   
4840 C  CZ    . PHE A 587 ? 1.0925 1.0993 1.2825 0.0069  -0.0556 0.3000  587 PHE A CZ    
4841 N  N     . PHE A 588 ? 0.8888 0.9175 1.0587 -0.0037 -0.0852 0.2581  588 PHE A N     
4842 C  CA    . PHE A 588 ? 0.9168 0.9429 1.1042 -0.0006 -0.0715 0.2431  588 PHE A CA    
4843 C  C     . PHE A 588 ? 0.9463 0.9632 1.1547 0.0055  -0.0534 0.2438  588 PHE A C     
4844 O  O     . PHE A 588 ? 0.9300 0.9496 1.1701 0.0114  -0.0500 0.2577  588 PHE A O     
4845 C  CB    . PHE A 588 ? 0.8200 0.8580 1.0337 0.0009  -0.0781 0.2486  588 PHE A CB    
4846 C  CG    . PHE A 588 ? 0.8634 0.9085 1.0582 -0.0062 -0.0963 0.2459  588 PHE A CG    
4847 C  CD1   . PHE A 588 ? 0.9391 0.9909 1.1254 -0.0106 -0.1162 0.2609  588 PHE A CD1   
4848 C  CD2   . PHE A 588 ? 0.8132 0.8572 0.9977 -0.0088 -0.0942 0.2283  588 PHE A CD2   
4849 C  CE1   . PHE A 588 ? 0.8250 0.8806 0.9928 -0.0178 -0.1341 0.2572  588 PHE A CE1   
4850 C  CE2   . PHE A 588 ? 0.6660 0.7146 0.8341 -0.0157 -0.1111 0.2256  588 PHE A CE2   
4851 C  CZ    . PHE A 588 ? 0.7486 0.8020 0.9081 -0.0203 -0.1313 0.2395  588 PHE A CZ    
4852 N  N     . VAL A 589 ? 1.0050 1.0106 1.1968 0.0041  -0.0422 0.2292  589 VAL A N     
4853 C  CA    . VAL A 589 ? 1.0457 1.0400 1.2551 0.0085  -0.0263 0.2283  589 VAL A CA    
4854 C  C     . VAL A 589 ? 0.9213 0.9115 1.1543 0.0139  -0.0147 0.2180  589 VAL A C     
4855 O  O     . VAL A 589 ? 0.8649 0.8520 1.1270 0.0206  -0.0074 0.2270  589 VAL A O     
4856 C  CB    . VAL A 589 ? 0.9131 0.8978 1.0990 0.0043  -0.0195 0.2170  589 VAL A CB    
4857 C  CG1   . VAL A 589 ? 0.9272 0.9011 1.1311 0.0071  -0.0079 0.2235  589 VAL A CG1   
4858 C  CG2   . VAL A 589 ? 0.9505 0.9402 1.1038 -0.0009 -0.0308 0.2215  589 VAL A CG2   
4859 N  N     . THR A 590 ? 0.8400 0.8296 1.0599 0.0118  -0.0122 0.1994  590 THR A N     
4860 C  CA    . THR A 590 ? 0.8889 0.8733 1.1251 0.0173  -0.0002 0.1879  590 THR A CA    
4861 C  C     . THR A 590 ? 0.9265 0.9174 1.1471 0.0143  -0.0039 0.1740  590 THR A C     
4862 O  O     . THR A 590 ? 0.8996 0.8979 1.0994 0.0082  -0.0159 0.1738  590 THR A O     
4863 C  CB    . THR A 590 ? 0.9201 0.8874 1.1576 0.0186  0.0138  0.1762  590 THR A CB    
4864 O  OG1   . THR A 590 ? 1.0844 1.0448 1.3362 0.0250  0.0254  0.1657  590 THR A OG1   
4865 C  CG2   . THR A 590 ? 0.8483 0.8118 1.0572 0.0112  0.0130  0.1614  590 THR A CG2   
4866 N  N     . LYS A 591 ? 0.8276 0.8146 1.0575 0.0191  0.0067  0.1627  591 LYS A N     
4867 C  CA    . LYS A 591 ? 0.8444 0.8371 1.0614 0.0170  0.0050  0.1501  591 LYS A CA    
4868 C  C     . LYS A 591 ? 0.8152 0.8041 1.0014 0.0095  0.0015  0.1362  591 LYS A C     
4869 O  O     . LYS A 591 ? 0.8800 0.8583 1.0584 0.0078  0.0077  0.1292  591 LYS A O     
4870 C  CB    . LYS A 591 ? 0.8533 0.8398 1.0817 0.0242  0.0193  0.1395  591 LYS A CB    
4871 C  CG    . LYS A 591 ? 0.8463 0.8400 1.1047 0.0327  0.0234  0.1527  591 LYS A CG    
4872 C  CD    . LYS A 591 ? 0.7612 0.7487 1.0246 0.0404  0.0384  0.1407  591 LYS A CD    
4873 C  CE    . LYS A 591 ? 0.7495 0.7459 1.0438 0.0499  0.0443  0.1548  591 LYS A CE    
4874 N  NZ    . LYS A 591 ? 0.7305 0.7174 1.0276 0.0594  0.0619  0.1431  591 LYS A NZ    
4875 N  N     . LYS A 592 ? 0.8910 0.8889 1.0617 0.0049  -0.0084 0.1332  592 LYS A N     
4876 C  CA    . LYS A 592 ? 0.9012 0.8972 1.0431 -0.0015 -0.0123 0.1212  592 LYS A CA    
4877 C  C     . LYS A 592 ? 0.7447 0.7378 0.8709 -0.0056 -0.0174 0.1270  592 LYS A C     
4878 O  O     . LYS A 592 ? 0.8551 0.8467 0.9576 -0.0100 -0.0196 0.1185  592 LYS A O     
4879 C  CB    . LYS A 592 ? 0.7595 0.7473 0.8942 -0.0011 -0.0012 0.1032  592 LYS A CB    
4880 C  CG    . LYS A 592 ? 0.9133 0.9016 1.0607 0.0044  0.0066  0.0968  592 LYS A CG    
4881 C  CD    . LYS A 592 ? 0.6998 0.6975 0.8380 0.0023  0.0005  0.0922  592 LYS A CD    
4882 C  CE    . LYS A 592 ? 0.6917 0.6905 0.8413 0.0084  0.0098  0.0869  592 LYS A CE    
4883 N  NZ    . LYS A 592 ? 0.8089 0.8191 0.9575 0.0070  0.0034  0.0883  592 LYS A NZ    
4884 N  N     . LYS A 593 ? 0.7915 0.7841 0.9302 -0.0037 -0.0187 0.1422  593 LYS A N     
4885 C  CA    . LYS A 593 ? 0.8711 0.8605 0.9957 -0.0066 -0.0212 0.1495  593 LYS A CA    
4886 C  C     . LYS A 593 ? 0.9796 0.9763 1.1064 -0.0067 -0.0339 0.1682  593 LYS A C     
4887 O  O     . LYS A 593 ? 0.8681 0.8667 1.0196 -0.0026 -0.0331 0.1817  593 LYS A O     
4888 C  CB    . LYS A 593 ? 0.9119 0.8911 1.0496 -0.0044 -0.0090 0.1501  593 LYS A CB    
4889 C  CG    . LYS A 593 ? 0.9231 0.8945 1.0525 -0.0066 0.0004  0.1324  593 LYS A CG    
4890 C  CD    . LYS A 593 ? 1.0628 1.0225 1.2122 -0.0041 0.0119  0.1309  593 LYS A CD    
4891 C  CE    . LYS A 593 ? 0.9854 0.9381 1.1254 -0.0087 0.0175  0.1225  593 LYS A CE    
4892 N  NZ    . LYS A 593 ? 0.9553 0.9004 1.0977 -0.0091 0.0242  0.1043  593 LYS A NZ    
4893 N  N     . TYR A 594 ? 0.8306 0.8306 0.9309 -0.0112 -0.0457 0.1689  594 TYR A N     
4894 C  CA    . TYR A 594 ? 0.8101 0.8164 0.9068 -0.0125 -0.0605 0.1854  594 TYR A CA    
4895 C  C     . TYR A 594 ? 0.9471 0.9507 1.0052 -0.0170 -0.0693 0.1820  594 TYR A C     
4896 O  O     . TYR A 594 ? 0.9069 0.9062 0.9452 -0.0190 -0.0650 0.1666  594 TYR A O     
4897 C  CB    . TYR A 594 ? 0.7987 0.8146 0.9138 -0.0124 -0.0708 0.1905  594 TYR A CB    
4898 C  CG    . TYR A 594 ? 0.7949 0.8127 0.8952 -0.0164 -0.0770 0.1768  594 TYR A CG    
4899 C  CD1   . TYR A 594 ? 0.7681 0.7871 0.8441 -0.0218 -0.0936 0.1776  594 TYR A CD1   
4900 C  CD2   . TYR A 594 ? 0.7153 0.7322 0.8247 -0.0146 -0.0663 0.1629  594 TYR A CD2   
4901 C  CE1   . TYR A 594 ? 0.6593 0.6783 0.7233 -0.0255 -0.0991 0.1653  594 TYR A CE1   
4902 C  CE2   . TYR A 594 ? 0.7328 0.7515 0.8301 -0.0181 -0.0716 0.1517  594 TYR A CE2   
4903 C  CZ    . TYR A 594 ? 0.8191 0.8386 0.8950 -0.0235 -0.0878 0.1530  594 TYR A CZ    
4904 O  OH    . TYR A 594 ? 0.8293 0.8489 0.8946 -0.0270 -0.0931 0.1421  594 TYR A OH    
4905 N  N     . ALA A 595 ? 0.8572 0.8632 0.9045 -0.0181 -0.0815 0.1968  595 ALA A N     
4906 C  CA    . ALA A 595 ? 0.9595 0.9616 0.9670 -0.0215 -0.0912 0.1949  595 ALA A CA    
4907 C  C     . ALA A 595 ? 0.9652 0.9728 0.9677 -0.0244 -0.1122 0.2068  595 ALA A C     
4908 O  O     . ALA A 595 ? 0.9026 0.9175 0.9308 -0.0229 -0.1177 0.2231  595 ALA A O     
4909 C  CB    . ALA A 595 ? 0.9736 0.9703 0.9637 -0.0197 -0.0828 0.2013  595 ALA A CB    
4910 N  N     . VAL A 596 ? 0.8724 0.8758 0.8422 -0.0286 -0.1245 0.1988  596 VAL A N     
4911 C  CA    . VAL A 596 ? 1.0728 1.0800 1.0369 -0.0330 -0.1471 0.2071  596 VAL A CA    
4912 C  C     . VAL A 596 ? 1.1020 1.0985 1.0164 -0.0360 -0.1576 0.2009  596 VAL A C     
4913 O  O     . VAL A 596 ? 1.1992 1.1867 1.0882 -0.0352 -0.1478 0.1857  596 VAL A O     
4914 C  CB    . VAL A 596 ? 1.0661 1.0798 1.0552 -0.0360 -0.1535 0.2011  596 VAL A CB    
4915 C  CG1   . VAL A 596 ? 0.8938 0.8993 0.8559 -0.0398 -0.1569 0.1821  596 VAL A CG1   
4916 C  CG2   . VAL A 596 ? 1.1157 1.1395 1.1247 -0.0391 -0.1732 0.2179  596 VAL A CG2   
4917 N  N     . ILE A 597 ? 1.0648 1.0621 0.9648 -0.0391 -0.1776 0.2131  597 ILE A N     
4918 C  CA    . ILE A 597 ? 1.0396 1.0249 0.8885 -0.0413 -0.1894 0.2087  597 ILE A CA    
4919 C  C     . ILE A 597 ? 1.1808 1.1666 1.0249 -0.0486 -0.2164 0.2107  597 ILE A C     
4920 O  O     . ILE A 597 ? 1.1677 1.1654 1.0424 -0.0508 -0.2289 0.2266  597 ILE A O     
4921 C  CB    . ILE A 597 ? 1.1587 1.1422 0.9863 -0.0374 -0.1869 0.2234  597 ILE A CB    
4922 C  CG1   . ILE A 597 ? 1.2437 1.2129 1.0130 -0.0383 -0.1964 0.2172  597 ILE A CG1   
4923 C  CG2   . ILE A 597 ? 1.1322 1.1275 0.9868 -0.0380 -0.1994 0.2465  597 ILE A CG2   
4924 C  CD1   . ILE A 597 ? 1.1867 1.1530 0.9302 -0.0331 -0.1888 0.2299  597 ILE A CD1   
4925 N  N     . ASP A 598 ? 1.2159 1.1884 1.0234 -0.0523 -0.2255 0.1951  598 ASP A N     
4926 C  CA    . ASP A 598 ? 1.2111 1.1816 1.0145 -0.0604 -0.2518 0.1943  598 ASP A CA    
4927 C  C     . ASP A 598 ? 1.4442 1.4077 1.2097 -0.0631 -0.2730 0.2039  598 ASP A C     
4928 O  O     . ASP A 598 ? 1.4167 1.3809 1.1679 -0.0583 -0.2674 0.2156  598 ASP A O     
4929 C  CB    . ASP A 598 ? 1.2843 1.2427 1.0709 -0.0634 -0.2519 0.1723  598 ASP A CB    
4930 C  CG    . ASP A 598 ? 1.3456 1.2849 1.0780 -0.0597 -0.2437 0.1575  598 ASP A CG    
4931 O  OD1   . ASP A 598 ? 1.4670 1.3991 1.1633 -0.0574 -0.2475 0.1636  598 ASP A OD1   
4932 O  OD2   . ASP A 598 ? 1.2912 1.2229 1.0169 -0.0585 -0.2327 0.1402  598 ASP A OD2   
4933 N  N     . GLU A 599 ? 1.6184 1.5742 1.3668 -0.0712 -0.2985 0.1992  599 GLU A N     
4934 C  CA    . GLU A 599 ? 1.6349 1.5829 1.3455 -0.0749 -0.3223 0.2076  599 GLU A CA    
4935 C  C     . GLU A 599 ? 1.6989 1.6271 1.3466 -0.0695 -0.3142 0.1972  599 GLU A C     
4936 O  O     . GLU A 599 ? 1.6462 1.5709 1.2628 -0.0681 -0.3232 0.2085  599 GLU A O     
4937 C  CB    . GLU A 599 ? 1.8120 1.7546 1.5199 -0.0858 -0.3526 0.2031  599 GLU A CB    
4938 C  CG    . GLU A 599 ? 1.6848 1.6480 1.4557 -0.0914 -0.3619 0.2151  599 GLU A CG    
4939 C  CD    . GLU A 599 ? 1.8191 1.7820 1.5898 -0.1028 -0.3978 0.2222  599 GLU A CD    
4940 O  OE1   . GLU A 599 ? 1.9845 1.9266 1.7110 -0.1085 -0.4145 0.2075  599 GLU A OE1   
4941 O  OE2   . GLU A 599 ? 1.8785 1.8614 1.6939 -0.1060 -0.4096 0.2427  599 GLU A OE2   
4942 N  N     . GLU A 600 ? 1.6496 1.5654 1.2783 -0.0659 -0.2969 0.1770  600 GLU A N     
4943 C  CA    . GLU A 600 ? 1.6711 1.5671 1.2400 -0.0601 -0.2883 0.1657  600 GLU A CA    
4944 C  C     . GLU A 600 ? 1.5878 1.4894 1.1564 -0.0501 -0.2592 0.1715  600 GLU A C     
4945 O  O     . GLU A 600 ? 1.5721 1.4597 1.0940 -0.0439 -0.2487 0.1650  600 GLU A O     
4946 C  CB    . GLU A 600 ? 1.5839 1.4624 1.1313 -0.0612 -0.2858 0.1412  600 GLU A CB    
4947 C  CG    . GLU A 600 ? 1.7746 1.6271 1.2551 -0.0612 -0.2987 0.1290  600 GLU A CG    
4948 C  CD    . GLU A 600 ? 1.8885 1.7242 1.3583 -0.0670 -0.3103 0.1085  600 GLU A CD    
4949 O  OE1   . GLU A 600 ? 1.8603 1.7065 1.3761 -0.0712 -0.3085 0.1053  600 GLU A OE1   
4950 O  OE2   . GLU A 600 ? 1.9588 1.7699 1.3735 -0.0671 -0.3210 0.0957  600 GLU A OE2   
4951 N  N     . GLY A 601 ? 1.4411 1.3617 1.0604 -0.0481 -0.2456 0.1836  601 GLY A N     
4952 C  CA    . GLY A 601 ? 1.3221 1.2481 0.9464 -0.0398 -0.2198 0.1904  601 GLY A CA    
4953 C  C     . GLY A 601 ? 1.3764 1.3033 1.0186 -0.0359 -0.1947 0.1765  601 GLY A C     
4954 O  O     . GLY A 601 ? 1.4407 1.3697 1.0823 -0.0295 -0.1734 0.1802  601 GLY A O     
4955 N  N     . LYS A 602 ? 1.3136 1.2393 0.9724 -0.0399 -0.1972 0.1616  602 LYS A N     
4956 C  CA    . LYS A 602 ? 1.2390 1.1669 0.9172 -0.0366 -0.1752 0.1491  602 LYS A CA    
4957 C  C     . LYS A 602 ? 1.3283 1.2735 1.0612 -0.0362 -0.1650 0.1589  602 LYS A C     
4958 O  O     . LYS A 602 ? 1.2689 1.2231 1.0348 -0.0407 -0.1762 0.1635  602 LYS A O     
4959 C  CB    . LYS A 602 ? 1.2830 1.2027 0.9570 -0.0406 -0.1820 0.1305  602 LYS A CB    
4960 C  CG    . LYS A 602 ? 1.1786 1.0930 0.8463 -0.0360 -0.1610 0.1146  602 LYS A CG    
4961 C  CD    . LYS A 602 ? 1.1931 1.1133 0.8952 -0.0393 -0.1597 0.1046  602 LYS A CD    
4962 C  CE    . LYS A 602 ? 1.1030 1.0226 0.8079 -0.0344 -0.1373 0.0926  602 LYS A CE    
4963 N  NZ    . LYS A 602 ? 1.3566 1.2854 1.0760 -0.0294 -0.1182 0.1016  602 LYS A NZ    
4964 N  N     . ILE A 603 ? 1.2376 1.1869 0.9805 -0.0308 -0.1435 0.1624  603 ILE A N     
4965 C  CA    . ILE A 603 ? 1.1698 1.1320 0.9609 -0.0297 -0.1325 0.1704  603 ILE A CA    
4966 C  C     . ILE A 603 ? 1.1272 1.0908 0.9388 -0.0297 -0.1197 0.1544  603 ILE A C     
4967 O  O     . ILE A 603 ? 1.0946 1.0522 0.8887 -0.0271 -0.1067 0.1430  603 ILE A O     
4968 C  CB    . ILE A 603 ? 1.0958 1.0607 0.8896 -0.0248 -0.1177 0.1837  603 ILE A CB    
4969 C  CG1   . ILE A 603 ? 1.1343 1.0962 0.8981 -0.0238 -0.1290 0.1989  603 ILE A CG1   
4970 C  CG2   . ILE A 603 ? 1.0400 1.0157 0.8833 -0.0240 -0.1098 0.1930  603 ILE A CG2   
4971 C  CD1   . ILE A 603 ? 1.3217 1.2718 1.0347 -0.0202 -0.1234 0.1935  603 ILE A CD1   
4972 N  N     . THR A 604 ? 1.1475 1.1195 0.9962 -0.0321 -0.1230 0.1546  604 THR A N     
4973 C  CA    . THR A 604 ? 0.9864 0.9612 0.8575 -0.0317 -0.1111 0.1416  604 THR A CA    
4974 C  C     . THR A 604 ? 1.0537 1.0363 0.9622 -0.0288 -0.0977 0.1489  604 THR A C     
4975 O  O     . THR A 604 ? 1.0303 1.0197 0.9635 -0.0287 -0.1034 0.1622  604 THR A O     
4976 C  CB    . THR A 604 ? 1.0224 0.9996 0.9056 -0.0360 -0.1238 0.1353  604 THR A CB    
4977 O  OG1   . THR A 604 ? 0.9489 0.9157 0.7966 -0.0389 -0.1352 0.1257  604 THR A OG1   
4978 C  CG2   . THR A 604 ? 1.0046 0.9861 0.9129 -0.0349 -0.1108 0.1243  604 THR A CG2   
4979 N  N     . THR A 605 ? 1.1357 1.1168 1.0490 -0.0264 -0.0804 0.1403  605 THR A N     
4980 C  CA    . THR A 605 ? 1.0233 1.0084 0.9690 -0.0240 -0.0674 0.1446  605 THR A CA    
4981 C  C     . THR A 605 ? 0.9280 0.9146 0.8916 -0.0241 -0.0592 0.1303  605 THR A C     
4982 O  O     . THR A 605 ? 0.8932 0.8769 0.8407 -0.0251 -0.0566 0.1168  605 THR A O     
4983 C  CB    . THR A 605 ? 0.9824 0.9642 0.9206 -0.0217 -0.0546 0.1492  605 THR A CB    
4984 O  OG1   . THR A 605 ? 1.0787 1.0588 0.9945 -0.0211 -0.0618 0.1625  605 THR A OG1   
4985 C  CG2   . THR A 605 ? 0.9505 0.9342 0.9234 -0.0199 -0.0440 0.1553  605 THR A CG2   
4986 N  N     . ARG A 606 ? 0.8937 0.8842 0.8898 -0.0225 -0.0547 0.1335  606 ARG A N     
4987 C  CA    . ARG A 606 ? 0.8214 0.8131 0.8338 -0.0219 -0.0472 0.1209  606 ARG A CA    
4988 C  C     . ARG A 606 ? 0.8347 0.8244 0.8721 -0.0190 -0.0343 0.1224  606 ARG A C     
4989 O  O     . ARG A 606 ? 0.7223 0.7129 0.7789 -0.0166 -0.0345 0.1349  606 ARG A O     
4990 C  CB    . ARG A 606 ? 0.9085 0.9063 0.9346 -0.0224 -0.0563 0.1216  606 ARG A CB    
4991 C  CG    . ARG A 606 ? 0.9301 0.9286 0.9353 -0.0262 -0.0721 0.1222  606 ARG A CG    
4992 C  CD    . ARG A 606 ? 0.9314 0.9299 0.9304 -0.0280 -0.0731 0.1081  606 ARG A CD    
4993 N  NE    . ARG A 606 ? 1.0839 1.0765 1.0513 -0.0314 -0.0828 0.1027  606 ARG A NE    
4994 C  CZ    . ARG A 606 ? 1.0853 1.0726 1.0334 -0.0316 -0.0775 0.0894  606 ARG A CZ    
4995 N  NH1   . ARG A 606 ? 1.0467 1.0350 1.0039 -0.0295 -0.0640 0.0804  606 ARG A NH1   
4996 N  NH2   . ARG A 606 ? 1.0811 1.0611 0.9996 -0.0337 -0.0863 0.0850  606 ARG A NH2   
4997 N  N     . GLY A 607 ? 0.8541 0.8401 0.8912 -0.0192 -0.0238 0.1097  607 GLY A N     
4998 C  CA    . GLY A 607 ? 0.7976 0.7793 0.8573 -0.0171 -0.0128 0.1071  607 GLY A CA    
4999 C  C     . GLY A 607 ? 0.7442 0.7207 0.8110 -0.0169 -0.0063 0.1160  607 GLY A C     
5000 O  O     . GLY A 607 ? 0.7346 0.7049 0.8142 -0.0168 0.0031  0.1103  607 GLY A O     
5001 N  N     . LEU A 608 ? 0.7690 0.7472 0.8274 -0.0169 -0.0117 0.1303  608 LEU A N     
5002 C  CA    . LEU A 608 ? 0.8173 0.7914 0.8834 -0.0164 -0.0056 0.1416  608 LEU A CA    
5003 C  C     . LEU A 608 ? 1.0064 0.9772 1.0637 -0.0191 0.0033  0.1343  608 LEU A C     
5004 O  O     . LEU A 608 ? 0.9317 0.9043 0.9733 -0.0209 0.0036  0.1219  608 LEU A O     
5005 C  CB    . LEU A 608 ? 0.8424 0.8200 0.8964 -0.0157 -0.0140 0.1588  608 LEU A CB    
5006 C  CG    . LEU A 608 ? 0.9618 0.9440 1.0297 -0.0134 -0.0237 0.1700  608 LEU A CG    
5007 C  CD1   . LEU A 608 ? 0.9270 0.9127 0.9794 -0.0135 -0.0339 0.1868  608 LEU A CD1   
5008 C  CD2   . LEU A 608 ? 0.9222 0.9006 1.0241 -0.0099 -0.0157 0.1753  608 LEU A CD2   
5009 N  N     . GLU A 609 ? 1.0008 0.9671 1.0709 -0.0192 0.0106  0.1434  609 GLU A N     
5010 C  CA    . GLU A 609 ? 0.9006 0.8649 0.9689 -0.0221 0.0193  0.1391  609 GLU A CA    
5011 C  C     . GLU A 609 ? 0.9078 0.8777 0.9466 -0.0227 0.0182  0.1391  609 GLU A C     
5012 O  O     . GLU A 609 ? 0.9092 0.8802 0.9431 -0.0248 0.0240  0.1303  609 GLU A O     
5013 C  CB    . GLU A 609 ? 0.8456 0.8047 0.9334 -0.0223 0.0263  0.1527  609 GLU A CB    
5014 C  CG    . GLU A 609 ? 0.8465 0.7962 0.9643 -0.0219 0.0303  0.1495  609 GLU A CG    
5015 C  CD    . GLU A 609 ? 0.9302 0.8792 1.0589 -0.0173 0.0252  0.1571  609 GLU A CD    
5016 O  OE1   . GLU A 609 ? 0.9220 0.8781 1.0384 -0.0153 0.0179  0.1691  609 GLU A OE1   
5017 O  OE2   . GLU A 609 ? 1.0045 0.9456 1.1541 -0.0154 0.0285  0.1512  609 GLU A OE2   
5018 N  N     . ILE A 610 ? 0.8546 0.8274 0.8730 -0.0206 0.0107  0.1489  610 ILE A N     
5019 C  CA    . ILE A 610 ? 0.9231 0.8984 0.9094 -0.0200 0.0101  0.1494  610 ILE A CA    
5020 C  C     . ILE A 610 ? 0.8484 0.8251 0.8209 -0.0210 0.0090  0.1317  610 ILE A C     
5021 O  O     . ILE A 610 ? 1.0370 1.0146 0.9900 -0.0204 0.0138  0.1285  610 ILE A O     
5022 C  CB    . ILE A 610 ? 0.9067 0.8829 0.8726 -0.0178 -0.0007 0.1615  610 ILE A CB    
5023 C  CG1   . ILE A 610 ? 1.0039 0.9795 0.9308 -0.0167 -0.0042 0.1573  610 ILE A CG1   
5024 C  CG2   . ILE A 610 ? 1.0825 1.0598 1.0614 -0.0181 -0.0118 0.1610  610 ILE A CG2   
5025 C  CD1   . ILE A 610 ? 1.2301 1.2048 1.1331 -0.0152 -0.0160 0.1690  610 ILE A CD1   
5026 N  N     . VAL A 611 ? 0.9996 0.9765 0.9828 -0.0221 0.0038  0.1209  611 VAL A N     
5027 C  CA    . VAL A 611 ? 0.8999 0.8781 0.8723 -0.0230 0.0027  0.1051  611 VAL A CA    
5028 C  C     . VAL A 611 ? 0.8209 0.7993 0.8118 -0.0250 0.0111  0.0942  611 VAL A C     
5029 O  O     . VAL A 611 ? 0.9383 0.9188 0.9205 -0.0257 0.0122  0.0828  611 VAL A O     
5030 C  CB    . VAL A 611 ? 0.7759 0.7552 0.7462 -0.0230 -0.0086 0.1001  611 VAL A CB    
5031 C  CG1   . VAL A 611 ? 0.8606 0.8397 0.8185 -0.0221 -0.0192 0.1124  611 VAL A CG1   
5032 C  CG2   . VAL A 611 ? 0.7236 0.7032 0.7219 -0.0231 -0.0071 0.0960  611 VAL A CG2   
5033 N  N     . ARG A 612 ? 0.8920 0.8675 0.9078 -0.0260 0.0162  0.0975  612 ARG A N     
5034 C  CA    . ARG A 612 ? 0.8198 0.7937 0.8522 -0.0287 0.0219  0.0865  612 ARG A CA    
5035 C  C     . ARG A 612 ? 0.9047 0.8812 0.9352 -0.0309 0.0294  0.0871  612 ARG A C     
5036 O  O     . ARG A 612 ? 0.9362 0.9128 0.9681 -0.0307 0.0342  0.0997  612 ARG A O     
5037 C  CB    . ARG A 612 ? 0.9267 0.8936 0.9851 -0.0290 0.0246  0.0891  612 ARG A CB    
5038 C  CG    . ARG A 612 ? 0.8126 0.7776 0.8776 -0.0258 0.0194  0.0888  612 ARG A CG    
5039 C  CD    . ARG A 612 ? 0.8472 0.8031 0.9370 -0.0252 0.0241  0.0877  612 ARG A CD    
5040 N  NE    . ARG A 612 ? 0.5961 0.5473 0.6920 -0.0285 0.0284  0.0738  612 ARG A NE    
5041 C  CZ    . ARG A 612 ? 0.7743 0.7239 0.8695 -0.0278 0.0276  0.0598  612 ARG A CZ    
5042 N  NH1   . ARG A 612 ? 0.8767 0.8296 0.9673 -0.0238 0.0241  0.0582  612 ARG A NH1   
5043 N  NH2   . ARG A 612 ? 0.7686 0.7135 0.8679 -0.0314 0.0302  0.0480  612 ARG A NH2   
5044 N  N     . ARG A 613 ? 0.9239 0.9036 0.9528 -0.0327 0.0307  0.0747  613 ARG A N     
5045 C  CA    . ARG A 613 ? 0.9507 0.9352 0.9803 -0.0345 0.0376  0.0756  613 ARG A CA    
5046 C  C     . ARG A 613 ? 0.8828 0.8647 0.9388 -0.0389 0.0430  0.0789  613 ARG A C     
5047 O  O     . ARG A 613 ? 0.9890 0.9759 1.0503 -0.0406 0.0496  0.0846  613 ARG A O     
5048 C  CB    . ARG A 613 ? 0.9996 0.9891 1.0211 -0.0349 0.0363  0.0622  613 ARG A CB    
5049 C  CG    . ARG A 613 ? 1.0564 1.0463 1.0978 -0.0395 0.0370  0.0526  613 ARG A CG    
5050 C  CD    . ARG A 613 ? 1.1987 1.1957 1.2321 -0.0396 0.0365  0.0430  613 ARG A CD    
5051 N  NE    . ARG A 613 ? 0.9957 0.9923 1.0131 -0.0366 0.0303  0.0349  613 ARG A NE    
5052 C  CZ    . ARG A 613 ? 1.0930 1.0906 1.1127 -0.0377 0.0264  0.0234  613 ARG A CZ    
5053 N  NH1   . ARG A 613 ? 1.1648 1.1633 1.1996 -0.0417 0.0269  0.0173  613 ARG A NH1   
5054 N  NH2   . ARG A 613 ? 1.0172 1.0147 1.0237 -0.0348 0.0214  0.0183  613 ARG A NH2   
5055 N  N     . ASP A 614 ? 1.0073 0.9811 1.0810 -0.0407 0.0408  0.0759  614 ASP A N     
5056 C  CA    . ASP A 614 ? 0.8395 0.8077 0.9386 -0.0456 0.0444  0.0769  614 ASP A CA    
5057 C  C     . ASP A 614 ? 0.7986 0.7614 0.9103 -0.0452 0.0482  0.0929  614 ASP A C     
5058 O  O     . ASP A 614 ? 0.8876 0.8408 1.0214 -0.0482 0.0493  0.0930  614 ASP A O     
5059 C  CB    . ASP A 614 ? 0.8508 0.8102 0.9602 -0.0476 0.0403  0.0622  614 ASP A CB    
5060 C  CG    . ASP A 614 ? 0.8602 0.8138 0.9650 -0.0426 0.0370  0.0609  614 ASP A CG    
5061 O  OD1   . ASP A 614 ? 0.8641 0.8222 0.9560 -0.0385 0.0354  0.0696  614 ASP A OD1   
5062 O  OD2   . ASP A 614 ? 0.7266 0.6709 0.8406 -0.0427 0.0359  0.0513  614 ASP A OD2   
5063 N  N     . TRP A 615 ? 0.7580 0.7258 0.8550 -0.0413 0.0501  0.1064  615 TRP A N     
5064 C  CA    . TRP A 615 ? 0.7846 0.7491 0.8917 -0.0405 0.0540  0.1240  615 TRP A CA    
5065 C  C     . TRP A 615 ? 0.8391 0.8121 0.9372 -0.0397 0.0612  0.1370  615 TRP A C     
5066 O  O     . TRP A 615 ? 1.0456 1.0262 1.1221 -0.0376 0.0621  0.1332  615 TRP A O     
5067 C  CB    . TRP A 615 ? 0.8342 0.7961 0.9316 -0.0355 0.0486  0.1310  615 TRP A CB    
5068 C  CG    . TRP A 615 ? 0.8332 0.7863 0.9456 -0.0350 0.0445  0.1228  615 TRP A CG    
5069 C  CD1   . TRP A 615 ? 0.8542 0.8062 0.9624 -0.0346 0.0400  0.1066  615 TRP A CD1   
5070 C  CD2   . TRP A 615 ? 0.8559 0.7995 0.9898 -0.0339 0.0457  0.1312  615 TRP A CD2   
5071 N  NE1   . TRP A 615 ? 0.7993 0.7419 0.9238 -0.0329 0.0393  0.1042  615 TRP A NE1   
5072 C  CE2   . TRP A 615 ? 0.8467 0.7835 0.9877 -0.0323 0.0427  0.1187  615 TRP A CE2   
5073 C  CE3   . TRP A 615 ? 0.8453 0.7853 0.9935 -0.0336 0.0499  0.1489  615 TRP A CE3   
5074 C  CZ2   . TRP A 615 ? 0.8451 0.7708 1.0066 -0.0298 0.0442  0.1225  615 TRP A CZ2   
5075 C  CZ3   . TRP A 615 ? 0.6339 0.5629 0.8039 -0.0317 0.0504  0.1530  615 TRP A CZ3   
5076 C  CH2   . TRP A 615 ? 0.7155 0.6372 0.8920 -0.0296 0.0478  0.1394  615 TRP A CH2   
5077 N  N     . SER A 616 ? 0.8287 0.7998 0.9439 -0.0410 0.0674  0.1527  616 SER A N     
5078 C  CA    . SER A 616 ? 0.8050 0.7844 0.9131 -0.0395 0.0763  0.1675  616 SER A CA    
5079 C  C     . SER A 616 ? 0.8434 0.8264 0.9169 -0.0325 0.0748  0.1753  616 SER A C     
5080 O  O     . SER A 616 ? 0.9929 0.9713 1.0568 -0.0299 0.0671  0.1765  616 SER A O     
5081 C  CB    . SER A 616 ? 0.7958 0.7719 0.9317 -0.0424 0.0830  0.1845  616 SER A CB    
5082 O  OG    . SER A 616 ? 0.8542 0.8245 0.9884 -0.0389 0.0805  0.1966  616 SER A OG    
5083 N  N     . GLU A 617 ? 0.9688 0.9595 1.0232 -0.0294 0.0822  0.1806  617 GLU A N     
5084 C  CA    . GLU A 617 ? 0.8787 0.8707 0.8953 -0.0227 0.0807  0.1865  617 GLU A CA    
5085 C  C     . GLU A 617 ? 0.8923 0.8813 0.9070 -0.0203 0.0804  0.2057  617 GLU A C     
5086 O  O     . GLU A 617 ? 1.0580 1.0444 1.0478 -0.0166 0.0720  0.2081  617 GLU A O     
5087 C  CB    . GLU A 617 ? 0.9460 0.9453 0.9431 -0.0188 0.0913  0.1890  617 GLU A CB    
5088 C  CG    . GLU A 617 ? 1.0188 1.0164 0.9714 -0.0115 0.0895  0.1920  617 GLU A CG    
5089 C  CD    . GLU A 617 ? 1.4388 1.4312 1.3705 -0.0111 0.0758  0.1751  617 GLU A CD    
5090 O  OE1   . GLU A 617 ? 1.7452 1.7327 1.6537 -0.0086 0.0667  0.1787  617 GLU A OE1   
5091 O  OE2   . GLU A 617 ? 1.3863 1.3801 1.3260 -0.0136 0.0736  0.1590  617 GLU A OE2   
5092 N  N     . ILE A 618 ? 0.9494 0.9388 0.9915 -0.0227 0.0886  0.2203  618 ILE A N     
5093 C  CA    . ILE A 618 ? 0.9403 0.9273 0.9836 -0.0202 0.0890  0.2406  618 ILE A CA    
5094 C  C     . ILE A 618 ? 1.0212 1.0007 1.0733 -0.0210 0.0768  0.2374  618 ILE A C     
5095 O  O     . ILE A 618 ? 1.0387 1.0170 1.0812 -0.0175 0.0724  0.2514  618 ILE A O     
5096 C  CB    . ILE A 618 ? 0.8468 0.8352 0.9226 -0.0233 0.1007  0.2570  618 ILE A CB    
5097 C  CG1   . ILE A 618 ? 0.9013 0.8897 0.9712 -0.0191 0.1039  0.2816  618 ILE A CG1   
5098 C  CG2   . ILE A 618 ? 0.7877 0.7685 0.9048 -0.0305 0.0979  0.2488  618 ILE A CG2   
5099 C  CD1   . ILE A 618 ? 0.9873 0.9795 1.0101 -0.0116 0.1028  0.2878  618 ILE A CD1   
5100 N  N     . ALA A 619 ? 0.9283 0.9033 0.9983 -0.0249 0.0713  0.2197  619 ALA A N     
5101 C  CA    . ALA A 619 ? 0.8458 0.8146 0.9239 -0.0243 0.0612  0.2161  619 ALA A CA    
5102 C  C     . ALA A 619 ? 1.0437 1.0153 1.0899 -0.0208 0.0505  0.2093  619 ALA A C     
5103 O  O     . ALA A 619 ? 1.0759 1.0465 1.1171 -0.0181 0.0425  0.2182  619 ALA A O     
5104 C  CB    . ALA A 619 ? 0.7610 0.7230 0.8670 -0.0288 0.0604  0.1997  619 ALA A CB    
5105 N  N     . LYS A 620 ? 0.9325 0.9075 0.9585 -0.0210 0.0496  0.1944  620 LYS A N     
5106 C  CA    . LYS A 620 ? 0.8491 0.8254 0.8447 -0.0184 0.0391  0.1875  620 LYS A CA    
5107 C  C     . LYS A 620 ? 1.0882 1.0660 1.0535 -0.0143 0.0368  0.2026  620 LYS A C     
5108 O  O     . LYS A 620 ? 1.0649 1.0418 1.0177 -0.0127 0.0252  0.2071  620 LYS A O     
5109 C  CB    . LYS A 620 ? 0.8775 0.8561 0.8579 -0.0192 0.0401  0.1697  620 LYS A CB    
5110 C  CG    . LYS A 620 ? 0.8680 0.8461 0.8737 -0.0233 0.0431  0.1550  620 LYS A CG    
5111 C  CD    . LYS A 620 ? 1.0056 0.9882 0.9976 -0.0234 0.0483  0.1444  620 LYS A CD    
5112 C  CE    . LYS A 620 ? 0.9210 0.9039 0.9321 -0.0274 0.0480  0.1282  620 LYS A CE    
5113 N  NZ    . LYS A 620 ? 1.0709 1.0544 1.0641 -0.0263 0.0404  0.1136  620 LYS A NZ    
5114 N  N     . GLU A 621 ? 1.0993 1.0797 1.0522 -0.0122 0.0478  0.2110  621 GLU A N     
5115 C  CA    . GLU A 621 ? 1.0454 1.0262 0.9623 -0.0073 0.0472  0.2237  621 GLU A CA    
5116 C  C     . GLU A 621 ? 1.1185 1.0981 1.0387 -0.0061 0.0397  0.2416  621 GLU A C     
5117 O  O     . GLU A 621 ? 1.2306 1.2091 1.1199 -0.0034 0.0294  0.2466  621 GLU A O     
5118 C  CB    . GLU A 621 ? 1.0721 1.0567 0.9832 -0.0046 0.0637  0.2330  621 GLU A CB    
5119 C  CG    . GLU A 621 ? 1.1364 1.1209 1.0148 0.0012  0.0664  0.2511  621 GLU A CG    
5120 C  CD    . GLU A 621 ? 1.3289 1.3180 1.1984 0.0052  0.0845  0.2589  621 GLU A CD    
5121 O  OE1   . GLU A 621 ? 1.1741 1.1662 1.0530 0.0040  0.0924  0.2469  621 GLU A OE1   
5122 O  OE2   . GLU A 621 ? 1.2689 1.2594 1.1230 0.0098  0.0911  0.2782  621 GLU A OE2   
5123 N  N     . THR A 622 ? 1.0743 1.0536 1.0320 -0.0082 0.0439  0.2515  622 THR A N     
5124 C  CA    . THR A 622 ? 1.1241 1.1029 1.0888 -0.0065 0.0382  0.2708  622 THR A CA    
5125 C  C     . THR A 622 ? 1.0660 1.0433 1.0409 -0.0075 0.0234  0.2657  622 THR A C     
5126 O  O     . THR A 622 ? 1.0849 1.0635 1.0501 -0.0053 0.0132  0.2790  622 THR A O     
5127 C  CB    . THR A 622 ? 1.0991 1.0767 1.1008 -0.0078 0.0497  0.2850  622 THR A CB    
5128 O  OG1   . THR A 622 ? 1.1960 1.1692 1.2338 -0.0122 0.0510  0.2715  622 THR A OG1   
5129 C  CG2   . THR A 622 ? 0.9334 0.9146 0.9282 -0.0070 0.0648  0.2920  622 THR A CG2   
5130 N  N     . GLN A 623 ? 1.0237 0.9990 1.0185 -0.0105 0.0219  0.2477  623 GLN A N     
5131 C  CA    . GLN A 623 ? 1.0105 0.9859 1.0128 -0.0107 0.0088  0.2424  623 GLN A CA    
5132 C  C     . GLN A 623 ? 1.0609 1.0387 1.0258 -0.0100 -0.0044 0.2380  623 GLN A C     
5133 O  O     . GLN A 623 ? 1.0693 1.0491 1.0333 -0.0095 -0.0178 0.2442  623 GLN A O     
5134 C  CB    . GLN A 623 ? 0.9446 0.9171 0.9714 -0.0133 0.0115  0.2236  623 GLN A CB    
5135 C  CG    . GLN A 623 ? 0.9083 0.8818 0.9468 -0.0127 0.0005  0.2194  623 GLN A CG    
5136 C  CD    . GLN A 623 ? 0.9191 0.8893 0.9785 -0.0142 0.0045  0.2013  623 GLN A CD    
5137 O  OE1   . GLN A 623 ? 0.9619 0.9326 1.0087 -0.0163 0.0060  0.1850  623 GLN A OE1   
5138 N  NE2   . GLN A 623 ? 0.8937 0.8600 0.9842 -0.0126 0.0065  0.2042  623 GLN A NE2   
5139 N  N     . ALA A 624 ? 1.0650 1.0422 1.0002 -0.0100 -0.0010 0.2274  624 ALA A N     
5140 C  CA    . ALA A 624 ? 1.1260 1.1023 1.0216 -0.0091 -0.0131 0.2229  624 ALA A CA    
5141 C  C     . ALA A 624 ? 1.2006 1.1772 1.0742 -0.0065 -0.0209 0.2423  624 ALA A C     
5142 O  O     . ALA A 624 ? 1.2031 1.1798 1.0623 -0.0073 -0.0377 0.2443  624 ALA A O     
5143 C  CB    . ALA A 624 ? 0.9679 0.9418 0.8359 -0.0081 -0.0048 0.2101  624 ALA A CB    
5144 N  N     . ARG A 625 ? 1.1656 1.1428 1.0369 -0.0037 -0.0095 0.2576  625 ARG A N     
5145 C  CA    . ARG A 625 ? 1.2258 1.2034 1.0728 -0.0006 -0.0159 0.2772  625 ARG A CA    
5146 C  C     . ARG A 625 ? 1.2259 1.2070 1.0996 -0.0015 -0.0272 0.2920  625 ARG A C     
5147 O  O     . ARG A 625 ? 1.2630 1.2452 1.1158 -0.0007 -0.0421 0.3028  625 ARG A O     
5148 C  CB    . ARG A 625 ? 1.1529 1.1312 0.9942 0.0030  0.0012  0.2914  625 ARG A CB    
5149 C  CG    . ARG A 625 ? 1.2102 1.1859 1.0174 0.0058  0.0119  0.2813  625 ARG A CG    
5150 C  CD    . ARG A 625 ? 1.2246 1.2035 1.0485 0.0076  0.0330  0.2907  625 ARG A CD    
5151 N  NE    . ARG A 625 ? 1.3501 1.3306 1.1574 0.0123  0.0382  0.3145  625 ARG A NE    
5152 C  CZ    . ARG A 625 ? 1.3369 1.3214 1.1719 0.0128  0.0519  0.3320  625 ARG A CZ    
5153 N  NH1   . ARG A 625 ? 1.3061 1.2922 1.1865 0.0084  0.0609  0.3277  625 ARG A NH1   
5154 N  NH2   . ARG A 625 ? 1.3451 1.3313 1.1612 0.0176  0.0561  0.3546  625 ARG A NH2   
5155 N  N     . VAL A 626 ? 1.1821 1.1645 1.1018 -0.0029 -0.0207 0.2927  626 VAL A N     
5156 C  CA    . VAL A 626 ? 1.2041 1.1896 1.1531 -0.0026 -0.0298 0.3061  626 VAL A CA    
5157 C  C     . VAL A 626 ? 1.1362 1.1244 1.0813 -0.0047 -0.0479 0.2975  626 VAL A C     
5158 O  O     . VAL A 626 ? 1.1266 1.1190 1.0727 -0.0042 -0.0622 0.3116  626 VAL A O     
5159 C  CB    . VAL A 626 ? 1.1342 1.1175 1.1314 -0.0029 -0.0174 0.3059  626 VAL A CB    
5160 C  CG1   . VAL A 626 ? 1.0746 1.0602 1.1041 -0.0019 -0.0262 0.3139  626 VAL A CG1   
5161 C  CG2   . VAL A 626 ? 1.0505 1.0319 1.0567 -0.0013 -0.0031 0.3217  626 VAL A CG2   
5162 N  N     . LEU A 627 ? 1.0101 0.9964 0.9519 -0.0073 -0.0478 0.2754  627 LEU A N     
5163 C  CA    . LEU A 627 ? 1.1090 1.0979 1.0473 -0.0098 -0.0645 0.2672  627 LEU A CA    
5164 C  C     . LEU A 627 ? 1.2659 1.2538 1.1599 -0.0106 -0.0804 0.2705  627 LEU A C     
5165 O  O     . LEU A 627 ? 1.3076 1.2993 1.2016 -0.0127 -0.0987 0.2757  627 LEU A O     
5166 C  CB    . LEU A 627 ? 1.0652 1.0520 1.0085 -0.0121 -0.0595 0.2436  627 LEU A CB    
5167 C  CG    . LEU A 627 ? 1.0279 1.0160 1.0148 -0.0119 -0.0521 0.2380  627 LEU A CG    
5168 C  CD1   . LEU A 627 ? 0.9837 0.9703 0.9682 -0.0142 -0.0495 0.2155  627 LEU A CD1   
5169 C  CD2   . LEU A 627 ? 1.0450 1.0391 1.0576 -0.0110 -0.0634 0.2503  627 LEU A CD2   
5170 N  N     . GLU A 628 ? 1.1958 1.1782 1.0517 -0.0090 -0.0740 0.2676  628 GLU A N     
5171 C  CA    . GLU A 628 ? 1.2314 1.2094 1.0393 -0.0092 -0.0883 0.2686  628 GLU A CA    
5172 C  C     . GLU A 628 ? 1.3072 1.2892 1.1105 -0.0082 -0.1014 0.2919  628 GLU A C     
5173 O  O     . GLU A 628 ? 1.4018 1.3852 1.1955 -0.0112 -0.1226 0.2946  628 GLU A O     
5174 C  CB    . GLU A 628 ? 1.3187 1.2894 1.0877 -0.0057 -0.0750 0.2625  628 GLU A CB    
5175 C  CG    . GLU A 628 ? 1.4564 1.4203 1.1712 -0.0040 -0.0871 0.2667  628 GLU A CG    
5176 C  CD    . GLU A 628 ? 1.6806 1.6345 1.3540 -0.0013 -0.0786 0.2501  628 GLU A CD    
5177 O  OE1   . GLU A 628 ? 1.7791 1.7277 1.4437 -0.0043 -0.0860 0.2311  628 GLU A OE1   
5178 O  OE2   . GLU A 628 ? 1.6988 1.6503 1.3494 0.0042  -0.0639 0.2571  628 GLU A OE2   
5179 N  N     . ALA A 629 ? 1.2912 1.2755 1.1034 -0.0043 -0.0897 0.3099  629 ALA A N     
5180 C  CA    . ALA A 629 ? 1.3882 1.3771 1.1979 -0.0028 -0.1011 0.3342  629 ALA A CA    
5181 C  C     . ALA A 629 ? 1.3763 1.3734 1.2255 -0.0054 -0.1156 0.3421  629 ALA A C     
5182 O  O     . ALA A 629 ? 1.4446 1.4466 1.2896 -0.0053 -0.1314 0.3606  629 ALA A O     
5183 C  CB    . ALA A 629 ? 1.3420 1.3324 1.1639 0.0018  -0.0834 0.3526  629 ALA A CB    
5184 N  N     . LEU A 630 ? 1.2847 1.2838 1.1717 -0.0072 -0.1105 0.3293  630 LEU A N     
5185 C  CA    . LEU A 630 ? 1.2610 1.2683 1.1877 -0.0086 -0.1217 0.3359  630 LEU A CA    
5186 C  C     . LEU A 630 ? 1.2192 1.2286 1.1318 -0.0136 -0.1431 0.3267  630 LEU A C     
5187 O  O     . LEU A 630 ? 1.2922 1.3098 1.2208 -0.0151 -0.1603 0.3402  630 LEU A O     
5188 C  CB    . LEU A 630 ? 1.1153 1.1227 1.0873 -0.0073 -0.1052 0.3265  630 LEU A CB    
5189 C  CG    . LEU A 630 ? 1.0446 1.0541 1.0553 -0.0030 -0.0945 0.3448  630 LEU A CG    
5190 C  CD1   . LEU A 630 ? 1.0964 1.1004 1.1385 -0.0017 -0.0746 0.3319  630 LEU A CD1   
5191 C  CD2   . LEU A 630 ? 1.1954 1.2142 1.2349 -0.0020 -0.1089 0.3616  630 LEU A CD2   
5192 N  N     . LEU A 631 ? 1.2473 1.2495 1.1323 -0.0163 -0.1427 0.3048  631 LEU A N     
5193 C  CA    . LEU A 631 ? 1.2597 1.2620 1.1328 -0.0218 -0.1623 0.2943  631 LEU A CA    
5194 C  C     . LEU A 631 ? 1.4073 1.4017 1.2254 -0.0241 -0.1790 0.2934  631 LEU A C     
5195 O  O     . LEU A 631 ? 1.4312 1.4259 1.2405 -0.0295 -0.2007 0.2907  631 LEU A O     
5196 C  CB    . LEU A 631 ? 1.0801 1.0785 0.9597 -0.0235 -0.1528 0.2702  631 LEU A CB    
5197 C  CG    . LEU A 631 ? 0.9902 0.9943 0.9192 -0.0216 -0.1381 0.2665  631 LEU A CG    
5198 C  CD1   . LEU A 631 ? 0.9684 0.9672 0.8929 -0.0228 -0.1277 0.2428  631 LEU A CD1   
5199 C  CD2   . LEU A 631 ? 1.0699 1.0850 1.0366 -0.0230 -0.1510 0.2770  631 LEU A CD2   
5200 N  N     . LYS A 632 ? 1.4253 1.4120 1.2061 -0.0202 -0.1693 0.2955  632 LYS A N     
5201 C  CA    . LYS A 632 ? 1.5295 1.5059 1.2522 -0.0211 -0.1829 0.2931  632 LYS A CA    
5202 C  C     . LYS A 632 ? 1.6622 1.6432 1.3736 -0.0214 -0.2014 0.3163  632 LYS A C     
5203 O  O     . LYS A 632 ? 1.7977 1.7750 1.4820 -0.0261 -0.2257 0.3158  632 LYS A O     
5204 C  CB    . LYS A 632 ? 1.5249 1.4913 1.2112 -0.0156 -0.1626 0.2854  632 LYS A CB    
5205 C  CG    . LYS A 632 ? 1.5941 1.5454 1.2260 -0.0162 -0.1684 0.2665  632 LYS A CG    
5206 C  CD    . LYS A 632 ? 1.8908 1.8358 1.4838 -0.0197 -0.1961 0.2713  632 LYS A CD    
5207 C  CE    . LYS A 632 ? 1.8600 1.7864 1.3972 -0.0198 -0.2011 0.2506  632 LYS A CE    
5208 N  NZ    . LYS A 632 ? 1.8543 1.7737 1.3664 -0.0268 -0.2326 0.2486  632 LYS A NZ    
5209 N  N     . ASP A 633 ? 1.6719 1.6605 1.4044 -0.0168 -0.1911 0.3371  633 ASP A N     
5210 C  CA    . ASP A 633 ? 1.8409 1.8358 1.5682 -0.0165 -0.2076 0.3619  633 ASP A CA    
5211 C  C     . ASP A 633 ? 1.7310 1.7403 1.5181 -0.0151 -0.2054 0.3818  633 ASP A C     
5212 O  O     . ASP A 633 ? 1.9297 1.9461 1.7194 -0.0144 -0.2185 0.4049  633 ASP A O     
5213 C  CB    . ASP A 633 ? 1.9215 1.9099 1.6041 -0.0107 -0.1989 0.3730  633 ASP A CB    
5214 C  CG    . ASP A 633 ? 2.1427 2.1154 1.7618 -0.0103 -0.2002 0.3548  633 ASP A CG    
5215 O  OD1   . ASP A 633 ? 2.2665 2.2328 1.8619 -0.0158 -0.2217 0.3426  633 ASP A OD1   
5216 O  OD2   . ASP A 633 ? 2.2395 2.2059 1.8335 -0.0042 -0.1796 0.3532  633 ASP A OD2   
5217 N  N     . GLY A 634 ? 1.5880 1.6011 1.4220 -0.0143 -0.1894 0.3737  634 GLY A N     
5218 C  CA    . GLY A 634 ? 1.4232 1.4469 1.3124 -0.0114 -0.1835 0.3915  634 GLY A CA    
5219 C  C     . GLY A 634 ? 1.4586 1.4824 1.3492 -0.0056 -0.1705 0.4119  634 GLY A C     
5220 O  O     . GLY A 634 ? 1.4265 1.4588 1.3524 -0.0031 -0.1727 0.4335  634 GLY A O     
5221 N  N     . ASP A 635 ? 1.5282 1.5431 1.3828 -0.0031 -0.1562 0.4066  635 ASP A N     
5222 C  CA    . ASP A 635 ? 1.6304 1.6453 1.4815 0.0022  -0.1436 0.4272  635 ASP A CA    
5223 C  C     . ASP A 635 ? 1.5152 1.5300 1.4155 0.0048  -0.1202 0.4269  635 ASP A C     
5224 O  O     . ASP A 635 ? 1.5385 1.5469 1.4345 0.0058  -0.1008 0.4147  635 ASP A O     
5225 C  CB    . ASP A 635 ? 1.5768 1.5828 1.3694 0.0042  -0.1375 0.4222  635 ASP A CB    
5226 C  CG    . ASP A 635 ? 1.6788 1.6859 1.4626 0.0098  -0.1265 0.4465  635 ASP A CG    
5227 O  OD1   . ASP A 635 ? 1.7793 1.7919 1.6078 0.0120  -0.1176 0.4633  635 ASP A OD1   
5228 O  OD2   . ASP A 635 ? 1.6231 1.6248 1.3544 0.0124  -0.1264 0.4491  635 ASP A OD2   
5229 N  N     . VAL A 636 ? 1.4874 1.5093 1.4363 0.0061  -0.1226 0.4409  636 VAL A N     
5230 C  CA    . VAL A 636 ? 1.3563 1.3756 1.3532 0.0086  -0.1022 0.4402  636 VAL A CA    
5231 C  C     . VAL A 636 ? 1.4088 1.4240 1.4037 0.0123  -0.0850 0.4547  636 VAL A C     
5232 O  O     . VAL A 636 ? 1.3047 1.3135 1.3200 0.0127  -0.0654 0.4459  636 VAL A O     
5233 C  CB    . VAL A 636 ? 1.2836 1.3103 1.3310 0.0104  -0.1089 0.4530  636 VAL A CB    
5234 C  CG1   . VAL A 636 ? 1.4437 1.4794 1.4867 0.0123  -0.1260 0.4815  636 VAL A CG1   
5235 C  CG2   . VAL A 636 ? 1.2111 1.2321 1.3055 0.0141  -0.0880 0.4544  636 VAL A CG2   
5236 N  N     . GLU A 637 ? 1.4790 1.4978 1.4492 0.0147  -0.0921 0.4775  637 GLU A N     
5237 C  CA    . GLU A 637 ? 1.5130 1.5290 1.4838 0.0185  -0.0751 0.4944  637 GLU A CA    
5238 C  C     . GLU A 637 ? 1.5460 1.5554 1.4824 0.0180  -0.0601 0.4794  637 GLU A C     
5239 O  O     . GLU A 637 ? 1.5517 1.5573 1.5063 0.0192  -0.0401 0.4822  637 GLU A O     
5240 C  CB    . GLU A 637 ? 1.6347 1.6569 1.5867 0.0218  -0.0866 0.5243  637 GLU A CB    
5241 C  CG    . GLU A 637 ? 1.7700 1.7939 1.6627 0.0205  -0.1060 0.5227  637 GLU A CG    
5242 C  CD    . GLU A 637 ? 1.8775 1.8977 1.7214 0.0240  -0.0970 0.5317  637 GLU A CD    
5243 O  OE1   . GLU A 637 ? 1.8341 1.8511 1.6225 0.0233  -0.1082 0.5234  637 GLU A OE1   
5244 O  OE2   . GLU A 637 ? 1.9298 1.9495 1.7908 0.0277  -0.0784 0.5472  637 GLU A OE2   
5245 N  N     . LYS A 638 ? 1.6006 1.6080 1.4889 0.0161  -0.0693 0.4636  638 LYS A N     
5246 C  CA    . LYS A 638 ? 1.5786 1.5800 1.4373 0.0165  -0.0539 0.4483  638 LYS A CA    
5247 C  C     . LYS A 638 ? 1.4853 1.4831 1.3770 0.0134  -0.0406 0.4256  638 LYS A C     
5248 O  O     . LYS A 638 ? 1.5322 1.5268 1.4259 0.0141  -0.0218 0.4209  638 LYS A O     
5249 C  CB    . LYS A 638 ? 1.6010 1.5990 1.3999 0.0160  -0.0671 0.4361  638 LYS A CB    
5250 C  CG    . LYS A 638 ? 1.4987 1.4902 1.2783 0.0145  -0.0578 0.4084  638 LYS A CG    
5251 C  CD    . LYS A 638 ? 1.3876 1.3729 1.1024 0.0160  -0.0676 0.4007  638 LYS A CD    
5252 C  CE    . LYS A 638 ? 1.3216 1.3001 1.0199 0.0140  -0.0634 0.3716  638 LYS A CE    
5253 N  NZ    . LYS A 638 ? 1.3262 1.2956 0.9600 0.0162  -0.0720 0.3634  638 LYS A NZ    
5254 N  N     . ALA A 639 ? 1.4820 1.4807 1.4008 0.0102  -0.0500 0.4125  639 ALA A N     
5255 C  CA    . ALA A 639 ? 1.4611 1.4560 1.4104 0.0075  -0.0382 0.3915  639 ALA A CA    
5256 C  C     . ALA A 639 ? 1.3858 1.3780 1.3788 0.0087  -0.0211 0.4012  639 ALA A C     
5257 O  O     . ALA A 639 ? 1.3370 1.3248 1.3408 0.0070  -0.0059 0.3890  639 ALA A O     
5258 C  CB    . ALA A 639 ? 1.3161 1.3130 1.2852 0.0048  -0.0514 0.3785  639 ALA A CB    
5259 N  N     . VAL A 640 ? 1.3911 1.3857 1.4108 0.0112  -0.0240 0.4236  640 VAL A N     
5260 C  CA    . VAL A 640 ? 1.2411 1.2308 1.3031 0.0122  -0.0083 0.4336  640 VAL A CA    
5261 C  C     . VAL A 640 ? 1.3266 1.3155 1.3739 0.0134  0.0058  0.4466  640 VAL A C     
5262 O  O     . VAL A 640 ? 1.3477 1.3311 1.4236 0.0121  0.0215  0.4466  640 VAL A O     
5263 C  CB    . VAL A 640 ? 1.2684 1.2602 1.3654 0.0155  -0.0150 0.4543  640 VAL A CB    
5264 C  CG1   . VAL A 640 ? 1.4378 1.4363 1.5133 0.0188  -0.0228 0.4825  640 VAL A CG1   
5265 C  CG2   . VAL A 640 ? 1.2755 1.2584 1.4212 0.0160  0.0005  0.4578  640 VAL A CG2   
5266 N  N     . ARG A 641 ? 1.3660 1.3598 1.3684 0.0158  0.0006  0.4578  641 ARG A N     
5267 C  CA    . ARG A 641 ? 1.3917 1.3856 1.3759 0.0178  0.0159  0.4690  641 ARG A CA    
5268 C  C     . ARG A 641 ? 1.4372 1.4279 1.4150 0.0150  0.0289  0.4464  641 ARG A C     
5269 O  O     . ARG A 641 ? 1.4213 1.4106 1.4184 0.0143  0.0460  0.4513  641 ARG A O     
5270 C  CB    . ARG A 641 ? 1.4322 1.4307 1.3631 0.0220  0.0075  0.4833  641 ARG A CB    
5271 C  CG    . ARG A 641 ? 1.4843 1.4874 1.4195 0.0253  -0.0032 0.5120  641 ARG A CG    
5272 C  CD    . ARG A 641 ? 1.5924 1.5987 1.4749 0.0301  -0.0049 0.5297  641 ARG A CD    
5273 N  NE    . ARG A 641 ? 1.5694 1.5752 1.4001 0.0298  -0.0228 0.5166  641 ARG A NE    
5274 C  CZ    . ARG A 641 ? 1.6665 1.6679 1.4569 0.0298  -0.0189 0.4963  641 ARG A CZ    
5275 N  NH1   . ARG A 641 ? 1.6500 1.6490 1.4451 0.0304  0.0024  0.4877  641 ARG A NH1   
5276 N  NH2   . ARG A 641 ? 1.7323 1.7311 1.4778 0.0291  -0.0373 0.4848  641 ARG A NH2   
5277 N  N     . ILE A 642 ? 1.4004 1.3904 1.3540 0.0130  0.0205  0.4223  642 ILE A N     
5278 C  CA    . ILE A 642 ? 1.3368 1.3249 1.2811 0.0110  0.0315  0.4012  642 ILE A CA    
5279 C  C     . ILE A 642 ? 1.2765 1.2609 1.2697 0.0069  0.0441  0.3937  642 ILE A C     
5280 O  O     . ILE A 642 ? 1.2961 1.2806 1.2939 0.0058  0.0591  0.3912  642 ILE A O     
5281 C  CB    . ILE A 642 ? 1.2425 1.2293 1.1595 0.0093  0.0184  0.3770  642 ILE A CB    
5282 C  CG1   . ILE A 642 ? 1.3285 1.3161 1.1907 0.0128  0.0070  0.3822  642 ILE A CG1   
5283 C  CG2   . ILE A 642 ? 1.1322 1.1171 1.0500 0.0068  0.0294  0.3544  642 ILE A CG2   
5284 C  CD1   . ILE A 642 ? 1.2738 1.2580 1.1000 0.0118  0.0012  0.3581  642 ILE A CD1   
5285 N  N     . VAL A 643 ? 1.1881 1.1689 1.2185 0.0048  0.0382  0.3903  643 VAL A N     
5286 C  CA    . VAL A 643 ? 1.0809 1.0554 1.1557 0.0010  0.0488  0.3824  643 VAL A CA    
5287 C  C     . VAL A 643 ? 1.1964 1.1695 1.2933 0.0012  0.0628  0.4036  643 VAL A C     
5288 O  O     . VAL A 643 ? 1.2745 1.2437 1.3961 -0.0028 0.0745  0.3974  643 VAL A O     
5289 C  CB    . VAL A 643 ? 1.1138 1.0831 1.2212 0.0005  0.0406  0.3765  643 VAL A CB    
5290 C  CG1   . VAL A 643 ? 1.0274 0.9873 1.1743 -0.0034 0.0505  0.3639  643 VAL A CG1   
5291 C  CG2   . VAL A 643 ? 1.1352 1.1077 1.2215 0.0005  0.0265  0.3594  643 VAL A CG2   
5292 N  N     . LYS A 644 ? 1.2743 1.2509 1.3634 0.0055  0.0613  0.4296  644 LYS A N     
5293 C  CA    . LYS A 644 ? 1.2515 1.2273 1.3629 0.0059  0.0747  0.4526  644 LYS A CA    
5294 C  C     . LYS A 644 ? 1.3093 1.2910 1.3971 0.0064  0.0881  0.4568  644 LYS A C     
5295 O  O     . LYS A 644 ? 1.3472 1.3277 1.4626 0.0041  0.1022  0.4668  644 LYS A O     
5296 C  CB    . LYS A 644 ? 1.3017 1.2802 1.4127 0.0109  0.0687  0.4809  644 LYS A CB    
5297 C  CG    . LYS A 644 ? 1.3796 1.3502 1.5410 0.0104  0.0684  0.4901  644 LYS A CG    
5298 C  CD    . LYS A 644 ? 1.3385 1.3133 1.4962 0.0156  0.0565  0.5123  644 LYS A CD    
5299 C  CE    . LYS A 644 ? 1.3694 1.3359 1.5748 0.0161  0.0535  0.5140  644 LYS A CE    
5300 N  NZ    . LYS A 644 ? 1.2684 1.2411 1.4686 0.0208  0.0377  0.5272  644 LYS A NZ    
5301 N  N     . GLU A 645 ? 1.3626 1.3499 1.4010 0.0096  0.0843  0.4497  645 GLU A N     
5302 C  CA    . GLU A 645 ? 1.4591 1.4517 1.4744 0.0114  0.0988  0.4526  645 GLU A CA    
5303 C  C     . GLU A 645 ? 1.2718 1.2632 1.3086 0.0060  0.1077  0.4315  645 GLU A C     
5304 O  O     . GLU A 645 ? 1.2394 1.2342 1.2912 0.0048  0.1233  0.4397  645 GLU A O     
5305 C  CB    . GLU A 645 ? 1.6491 1.6452 1.6036 0.0170  0.0924  0.4488  645 GLU A CB    
5306 C  CG    . GLU A 645 ? 1.7803 1.7755 1.7115 0.0195  0.0731  0.4541  645 GLU A CG    
5307 C  CD    . GLU A 645 ? 1.8952 1.8916 1.7635 0.0248  0.0668  0.4525  645 GLU A CD    
5308 O  OE1   . GLU A 645 ? 1.8139 1.8100 1.6565 0.0261  0.0748  0.4377  645 GLU A OE1   
5309 O  OE2   . GLU A 645 ? 1.8390 1.8361 1.6835 0.0278  0.0534  0.4658  645 GLU A OE2   
5310 N  N     . VAL A 646 ? 1.2773 1.2647 1.3169 0.0024  0.0976  0.4055  646 VAL A N     
5311 C  CA    . VAL A 646 ? 1.2122 1.1989 1.2684 -0.0026 0.1041  0.3848  646 VAL A CA    
5312 C  C     . VAL A 646 ? 1.2331 1.2140 1.3432 -0.0088 0.1104  0.3873  646 VAL A C     
5313 O  O     . VAL A 646 ? 1.2353 1.2178 1.3644 -0.0131 0.1206  0.3825  646 VAL A O     
5314 C  CB    . VAL A 646 ? 1.0734 1.0574 1.1141 -0.0041 0.0912  0.3575  646 VAL A CB    
5315 C  CG1   . VAL A 646 ? 1.0604 1.0426 1.1255 -0.0100 0.0957  0.3366  646 VAL A CG1   
5316 C  CG2   . VAL A 646 ? 1.2300 1.2182 1.2174 0.0011  0.0870  0.3529  646 VAL A CG2   
5317 N  N     . THR A 647 ? 1.1553 1.1289 1.2916 -0.0094 0.1042  0.3952  647 THR A N     
5318 C  CA    . THR A 647 ? 1.1076 1.0722 1.2938 -0.0151 0.1099  0.3971  647 THR A CA    
5319 C  C     . THR A 647 ? 1.2614 1.2295 1.4655 -0.0160 0.1243  0.4210  647 THR A C     
5320 O  O     . THR A 647 ? 1.1922 1.1552 1.4338 -0.0225 0.1312  0.4192  647 THR A O     
5321 C  CB    . THR A 647 ? 1.1261 1.0810 1.3350 -0.0139 0.1011  0.4008  647 THR A CB    
5322 O  OG1   . THR A 647 ? 1.2458 1.1879 1.4973 -0.0198 0.1036  0.3903  647 THR A OG1   
5323 C  CG2   . THR A 647 ? 1.2000 1.1568 1.4124 -0.0093 0.1031  0.4318  647 THR A CG2   
5324 N  N     . GLU A 648 ? 1.1977 1.1744 1.3753 -0.0098 0.1288  0.4437  648 GLU A N     
5325 C  CA    . GLU A 648 ? 1.1925 1.1744 1.3852 -0.0099 0.1443  0.4677  648 GLU A CA    
5326 C  C     . GLU A 648 ? 1.2656 1.2569 1.4462 -0.0110 0.1556  0.4607  648 GLU A C     
5327 O  O     . GLU A 648 ? 1.2346 1.2290 1.4451 -0.0148 0.1684  0.4725  648 GLU A O     
5328 C  CB    . GLU A 648 ? 1.2478 1.2355 1.4156 -0.0021 0.1460  0.4962  648 GLU A CB    
5329 C  CG    . GLU A 648 ? 1.4352 1.4163 1.6406 -0.0027 0.1470  0.5196  648 GLU A CG    
5330 C  CD    . GLU A 648 ? 1.5981 1.5877 1.7924 0.0030  0.1579  0.5534  648 GLU A CD    
5331 O  OE1   . GLU A 648 ? 1.7303 1.7288 1.8750 0.0099  0.1583  0.5591  648 GLU A OE1   
5332 O  OE2   . GLU A 648 ? 1.3983 1.3844 1.6324 0.0006  0.1661  0.5744  648 GLU A OE2   
5333 N  N     . LYS A 649 ? 1.2673 1.2632 1.4068 -0.0077 0.1510  0.4426  649 LYS A N     
5334 C  CA    . LYS A 649 ? 1.1801 1.1845 1.3097 -0.0080 0.1616  0.4340  649 LYS A CA    
5335 C  C     . LYS A 649 ? 1.1913 1.1926 1.3647 -0.0176 0.1627  0.4182  649 LYS A C     
5336 O  O     . LYS A 649 ? 1.2448 1.2535 1.4362 -0.0204 0.1751  0.4235  649 LYS A O     
5337 C  CB    . LYS A 649 ? 1.3150 1.3218 1.3938 -0.0028 0.1545  0.4151  649 LYS A CB    
5338 C  CG    . LYS A 649 ? 1.3437 1.3595 1.3805 0.0056  0.1665  0.4260  649 LYS A CG    
5339 C  CD    . LYS A 649 ? 1.5205 1.5334 1.5014 0.0124  0.1549  0.4179  649 LYS A CD    
5340 C  CE    . LYS A 649 ? 1.5373 1.5560 1.4719 0.0213  0.1671  0.4233  649 LYS A CE    
5341 N  NZ    . LYS A 649 ? 1.4946 1.5078 1.3726 0.0276  0.1546  0.4174  649 LYS A NZ    
5342 N  N     . LEU A 650 ? 1.2467 1.2370 1.4374 -0.0226 0.1497  0.3991  650 LEU A N     
5343 C  CA    . LEU A 650 ? 1.1628 1.1476 1.3920 -0.0319 0.1488  0.3828  650 LEU A CA    
5344 C  C     . LEU A 650 ? 1.1411 1.1223 1.4177 -0.0380 0.1572  0.4012  650 LEU A C     
5345 O  O     . LEU A 650 ? 1.1155 1.1014 1.4171 -0.0440 0.1646  0.4012  650 LEU A O     
5346 C  CB    . LEU A 650 ? 1.0233 0.9957 1.2572 -0.0344 0.1340  0.3601  650 LEU A CB    
5347 C  CG    . LEU A 650 ? 1.0902 1.0651 1.2877 -0.0313 0.1247  0.3370  650 LEU A CG    
5348 C  CD1   . LEU A 650 ? 1.0924 1.0563 1.3078 -0.0364 0.1146  0.3131  650 LEU A CD1   
5349 C  CD2   . LEU A 650 ? 0.8509 0.8376 1.0287 -0.0305 0.1319  0.3310  650 LEU A CD2   
5350 N  N     . SER A 651 ? 1.0457 1.0187 1.3372 -0.0366 0.1557  0.4179  651 SER A N     
5351 C  CA    . SER A 651 ? 1.1643 1.1306 1.5038 -0.0428 0.1623  0.4348  651 SER A CA    
5352 C  C     . SER A 651 ? 1.2274 1.2076 1.5746 -0.0426 0.1783  0.4585  651 SER A C     
5353 O  O     . SER A 651 ? 1.1724 1.1501 1.5634 -0.0504 0.1845  0.4679  651 SER A O     
5354 C  CB    . SER A 651 ? 1.1761 1.1318 1.5264 -0.0394 0.1585  0.4507  651 SER A CB    
5355 O  OG    . SER A 651 ? 1.1896 1.1554 1.5053 -0.0300 0.1613  0.4712  651 SER A OG    
5356 N  N     . LYS A 652 ? 1.3189 1.3133 1.6245 -0.0339 0.1854  0.4685  652 LYS A N     
5357 C  CA    . LYS A 652 ? 1.2162 1.2252 1.5236 -0.0317 0.2027  0.4904  652 LYS A CA    
5358 C  C     . LYS A 652 ? 1.0996 1.1200 1.3937 -0.0321 0.2077  0.4747  652 LYS A C     
5359 O  O     . LYS A 652 ? 1.0494 1.0840 1.3347 -0.0276 0.2231  0.4908  652 LYS A O     
5360 C  CB    . LYS A 652 ? 1.0996 1.1158 1.3687 -0.0205 0.2094  0.5146  652 LYS A CB    
5361 C  CG    . LYS A 652 ? 1.1429 1.1486 1.4230 -0.0193 0.2027  0.5302  652 LYS A CG    
5362 C  CD    . LYS A 652 ? 1.1443 1.1578 1.3916 -0.0090 0.2099  0.5588  652 LYS A CD    
5363 C  CE    . LYS A 652 ? 1.2388 1.2651 1.4337 -0.0005 0.2182  0.5581  652 LYS A CE    
5364 N  NZ    . LYS A 652 ? 1.2220 1.2543 1.3828 0.0096  0.2253  0.5865  652 LYS A NZ    
5365 N  N     . TYR A 653 ? 1.0823 1.0970 1.3752 -0.0368 0.1957  0.4447  653 TYR A N     
5366 C  CA    . TYR A 653 ? 1.1617 1.1858 1.4517 -0.0390 0.1986  0.4283  653 TYR A CA    
5367 C  C     . TYR A 653 ? 1.1142 1.1512 1.3557 -0.0280 0.2081  0.4317  653 TYR A C     
5368 O  O     . TYR A 653 ? 1.1318 1.1808 1.3750 -0.0273 0.2181  0.4306  653 TYR A O     
5369 C  CB    . TYR A 653 ? 0.9457 0.9757 1.2872 -0.0484 0.2070  0.4374  653 TYR A CB    
5370 C  CG    . TYR A 653 ? 1.1157 1.1300 1.5047 -0.0598 0.1974  0.4333  653 TYR A CG    
5371 C  CD1   . TYR A 653 ? 1.0951 1.1018 1.5046 -0.0692 0.1859  0.4080  653 TYR A CD1   
5372 C  CD2   . TYR A 653 ? 1.1575 1.1637 1.5705 -0.0609 0.2002  0.4552  653 TYR A CD2   
5373 C  CE1   . TYR A 653 ? 1.1713 1.1608 1.6205 -0.0791 0.1771  0.4025  653 TYR A CE1   
5374 C  CE2   . TYR A 653 ? 1.2154 1.2046 1.6712 -0.0708 0.1919  0.4505  653 TYR A CE2   
5375 C  CZ    . TYR A 653 ? 1.2061 1.1861 1.6788 -0.0799 0.1803  0.4234  653 TYR A CZ    
5376 O  OH    . TYR A 653 ? 1.1270 1.0873 1.6388 -0.0894 0.1719  0.4172  653 TYR A OH    
5377 N  N     . GLU A 654 ? 1.1626 1.1964 1.3601 -0.0190 0.2045  0.4353  654 GLU A N     
5378 C  CA    . GLU A 654 ? 1.0501 1.0921 1.1957 -0.0079 0.2123  0.4377  654 GLU A CA    
5379 C  C     . GLU A 654 ? 1.0101 1.0490 1.1214 -0.0059 0.2014  0.4085  654 GLU A C     
5380 O  O     . GLU A 654 ? 1.1017 1.1451 1.1692 0.0030  0.2071  0.4065  654 GLU A O     
5381 C  CB    . GLU A 654 ? 1.1226 1.1621 1.2351 0.0004  0.2126  0.4574  654 GLU A CB    
5382 C  CG    . GLU A 654 ? 1.2266 1.2656 1.3748 -0.0022 0.2188  0.4854  654 GLU A CG    
5383 C  CD    . GLU A 654 ? 1.3506 1.3922 1.4623 0.0079  0.2247  0.5102  654 GLU A CD    
5384 O  OE1   . GLU A 654 ? 1.3268 1.3603 1.4174 0.0103  0.2111  0.5095  654 GLU A OE1   
5385 O  OE2   . GLU A 654 ? 1.4198 1.4720 1.5240 0.0137  0.2431  0.5311  654 GLU A OE2   
5386 N  N     . VAL A 655 ? 0.9814 1.0120 1.1107 -0.0135 0.1865  0.3861  655 VAL A N     
5387 C  CA    . VAL A 655 ? 0.9958 1.0233 1.0954 -0.0120 0.1757  0.3592  655 VAL A CA    
5388 C  C     . VAL A 655 ? 1.0206 1.0560 1.1362 -0.0156 0.1814  0.3463  655 VAL A C     
5389 O  O     . VAL A 655 ? 1.0757 1.1127 1.2368 -0.0243 0.1828  0.3467  655 VAL A O     
5390 C  CB    . VAL A 655 ? 1.0409 1.0561 1.1482 -0.0170 0.1574  0.3429  655 VAL A CB    
5391 C  CG1   . VAL A 655 ? 0.9329 0.9463 1.0293 -0.0190 0.1479  0.3144  655 VAL A CG1   
5392 C  CG2   . VAL A 655 ? 1.0480 1.0579 1.1241 -0.0108 0.1496  0.3515  655 VAL A CG2   
5393 N  N     . PRO A 656 ? 0.9463 0.9863 1.0268 -0.0091 0.1843  0.3351  656 PRO A N     
5394 C  CA    . PRO A 656 ? 0.9495 0.9984 1.0454 -0.0115 0.1902  0.3245  656 PRO A CA    
5395 C  C     . PRO A 656 ? 0.9984 1.0425 1.1270 -0.0222 0.1767  0.3046  656 PRO A C     
5396 O  O     . PRO A 656 ? 1.1010 1.1348 1.2171 -0.0237 0.1619  0.2878  656 PRO A O     
5397 C  CB    . PRO A 656 ? 0.9995 1.0486 1.0449 -0.0020 0.1911  0.3121  656 PRO A CB    
5398 C  CG    . PRO A 656 ? 1.0228 1.0668 1.0275 0.0066  0.1928  0.3251  656 PRO A CG    
5399 C  CD    . PRO A 656 ? 1.0354 1.0719 1.0597 0.0009  0.1823  0.3329  656 PRO A CD    
5400 N  N     . PRO A 657 ? 0.9586 1.0100 1.1293 -0.0297 0.1813  0.3063  657 PRO A N     
5401 C  CA    . PRO A 657 ? 0.9180 0.9639 1.1172 -0.0400 0.1678  0.2866  657 PRO A CA    
5402 C  C     . PRO A 657 ? 0.9735 1.0170 1.1456 -0.0379 0.1578  0.2614  657 PRO A C     
5403 O  O     . PRO A 657 ? 0.9625 0.9977 1.1463 -0.0445 0.1446  0.2438  657 PRO A O     
5404 C  CB    . PRO A 657 ? 0.8645 0.9220 1.1067 -0.0469 0.1760  0.2950  657 PRO A CB    
5405 C  CG    . PRO A 657 ? 0.8894 0.9549 1.1387 -0.0426 0.1925  0.3236  657 PRO A CG    
5406 C  CD    . PRO A 657 ? 0.9025 0.9675 1.0989 -0.0296 0.1984  0.3281  657 PRO A CD    
5407 N  N     . GLU A 658 ? 1.0084 1.0578 1.1438 -0.0287 0.1641  0.2594  658 GLU A N     
5408 C  CA    . GLU A 658 ? 1.0233 1.0697 1.1327 -0.0264 0.1549  0.2367  658 GLU A CA    
5409 C  C     . GLU A 658 ? 0.9966 1.0295 1.0862 -0.0266 0.1400  0.2251  658 GLU A C     
5410 O  O     . GLU A 658 ? 1.1144 1.1430 1.1993 -0.0289 0.1288  0.2053  658 GLU A O     
5411 C  CB    . GLU A 658 ? 1.0143 1.0669 1.0867 -0.0156 0.1656  0.2384  658 GLU A CB    
5412 C  CG    . GLU A 658 ? 1.0426 1.1103 1.1343 -0.0139 0.1815  0.2483  658 GLU A CG    
5413 C  CD    . GLU A 658 ? 1.1636 1.2384 1.2662 -0.0108 0.1976  0.2751  658 GLU A CD    
5414 O  OE1   . GLU A 658 ? 1.2008 1.2684 1.3010 -0.0115 0.1954  0.2861  658 GLU A OE1   
5415 O  OE2   . GLU A 658 ? 1.0073 1.0955 1.1224 -0.0073 0.2132  0.2864  658 GLU A OE2   
5416 N  N     . LYS A 659 ? 0.9710 0.9980 1.0499 -0.0237 0.1397  0.2383  659 LYS A N     
5417 C  CA    . LYS A 659 ? 1.0620 1.0779 1.1255 -0.0235 0.1258  0.2302  659 LYS A CA    
5418 C  C     . LYS A 659 ? 1.0163 1.0244 1.1150 -0.0318 0.1169  0.2241  659 LYS A C     
5419 O  O     . LYS A 659 ? 0.9620 0.9614 1.0532 -0.0316 0.1061  0.2169  659 LYS A O     
5420 C  CB    . LYS A 659 ? 0.8943 0.9074 0.9330 -0.0172 0.1278  0.2477  659 LYS A CB    
5421 C  CG    . LYS A 659 ? 0.8806 0.8981 0.8776 -0.0080 0.1362  0.2527  659 LYS A CG    
5422 C  CD    . LYS A 659 ? 0.9307 0.9453 0.9028 -0.0021 0.1378  0.2715  659 LYS A CD    
5423 C  CE    . LYS A 659 ? 1.0317 1.0423 0.9500 0.0060  0.1340  0.2653  659 LYS A CE    
5424 N  NZ    . LYS A 659 ? 1.1174 1.1237 1.0089 0.0107  0.1307  0.2815  659 LYS A NZ    
5425 N  N     . LEU A 660 ? 0.9066 0.9169 1.0434 -0.0389 0.1212  0.2266  660 LEU A N     
5426 C  CA    . LEU A 660 ? 0.8574 0.8573 1.0264 -0.0467 0.1134  0.2200  660 LEU A CA    
5427 C  C     . LEU A 660 ? 0.8513 0.8510 1.0344 -0.0530 0.1069  0.1993  660 LEU A C     
5428 O  O     . LEU A 660 ? 0.8597 0.8509 1.0717 -0.0603 0.1019  0.1933  660 LEU A O     
5429 C  CB    . LEU A 660 ? 0.7403 0.7391 0.9438 -0.0512 0.1209  0.2393  660 LEU A CB    
5430 C  CG    . LEU A 660 ? 0.8608 0.8605 1.0525 -0.0450 0.1279  0.2625  660 LEU A CG    
5431 C  CD1   . LEU A 660 ? 0.9716 0.9814 1.1820 -0.0457 0.1424  0.2839  660 LEU A CD1   
5432 C  CD2   . LEU A 660 ? 0.9645 0.9510 1.1705 -0.0463 0.1215  0.2674  660 LEU A CD2   
5433 N  N     . VAL A 661 ? 0.8916 0.8994 1.0538 -0.0500 0.1068  0.1884  661 VAL A N     
5434 C  CA    . VAL A 661 ? 0.8229 0.8323 0.9961 -0.0554 0.1005  0.1700  661 VAL A CA    
5435 C  C     . VAL A 661 ? 0.8429 0.8424 1.0014 -0.0547 0.0885  0.1515  661 VAL A C     
5436 O  O     . VAL A 661 ? 0.7549 0.7532 0.8836 -0.0483 0.0858  0.1491  661 VAL A O     
5437 C  CB    . VAL A 661 ? 0.7772 0.8005 0.9377 -0.0519 0.1068  0.1682  661 VAL A CB    
5438 C  CG1   . VAL A 661 ? 0.8159 0.8433 0.9980 -0.0591 0.1014  0.1547  661 VAL A CG1   
5439 C  CG2   . VAL A 661 ? 0.8670 0.9006 1.0334 -0.0489 0.1215  0.1895  661 VAL A CG2   
5440 N  N     . ILE A 662 ? 0.8633 0.8552 1.0425 -0.0615 0.0812  0.1388  662 ILE A N     
5441 C  CA    . ILE A 662 ? 0.7614 0.7442 0.9297 -0.0609 0.0712  0.1212  662 ILE A CA    
5442 C  C     . ILE A 662 ? 0.7741 0.7635 0.9371 -0.0628 0.0669  0.1053  662 ILE A C     
5443 O  O     . ILE A 662 ? 1.0343 1.0269 1.2185 -0.0694 0.0664  0.1023  662 ILE A O     
5444 C  CB    . ILE A 662 ? 0.7917 0.7591 0.9829 -0.0657 0.0667  0.1172  662 ILE A CB    
5445 C  CG1   . ILE A 662 ? 0.7502 0.7112 0.9475 -0.0629 0.0708  0.1342  662 ILE A CG1   
5446 C  CG2   . ILE A 662 ? 0.8166 0.7756 0.9967 -0.0642 0.0582  0.0986  662 ILE A CG2   
5447 C  CD1   . ILE A 662 ? 0.7633 0.7099 0.9917 -0.0687 0.0701  0.1359  662 ILE A CD1   
5448 N  N     . HIS A 663 ? 0.8283 0.8198 0.9644 -0.0575 0.0632  0.0960  663 HIS A N     
5449 C  CA    . HIS A 663 ? 0.8915 0.8893 1.0205 -0.0582 0.0592  0.0818  663 HIS A CA    
5450 C  C     . HIS A 663 ? 0.8809 0.8693 1.0077 -0.0595 0.0501  0.0657  663 HIS A C     
5451 O  O     . HIS A 663 ? 0.9604 0.9434 1.0718 -0.0548 0.0472  0.0634  663 HIS A O     
5452 C  CB    . HIS A 663 ? 0.8750 0.8812 0.9759 -0.0512 0.0619  0.0826  663 HIS A CB    
5453 C  CG    . HIS A 663 ? 0.8485 0.8625 0.9454 -0.0478 0.0724  0.0983  663 HIS A CG    
5454 N  ND1   . HIS A 663 ? 0.8571 0.8820 0.9682 -0.0496 0.0796  0.1035  663 HIS A ND1   
5455 C  CD2   . HIS A 663 ? 0.8412 0.8537 0.9206 -0.0423 0.0774  0.1106  663 HIS A CD2   
5456 C  CE1   . HIS A 663 ? 0.8925 0.9223 0.9949 -0.0446 0.0900  0.1185  663 HIS A CE1   
5457 N  NE2   . HIS A 663 ? 0.8514 0.8732 0.9327 -0.0401 0.0886  0.1226  663 HIS A NE2   
5458 N  N     . LYS A 664 ? 0.8748 0.8614 1.0167 -0.0656 0.0455  0.0552  664 LYS A N     
5459 C  CA    . LYS A 664 ? 0.7890 0.7664 0.9265 -0.0663 0.0379  0.0392  664 LYS A CA    
5460 C  C     . LYS A 664 ? 0.8502 0.8345 0.9885 -0.0700 0.0329  0.0278  664 LYS A C     
5461 O  O     . LYS A 664 ? 0.9802 0.9704 1.1366 -0.0760 0.0329  0.0306  664 LYS A O     
5462 C  CB    . LYS A 664 ? 0.7784 0.7397 0.9337 -0.0701 0.0361  0.0372  664 LYS A CB    
5463 C  CG    . LYS A 664 ? 0.8994 0.8496 1.0445 -0.0644 0.0351  0.0336  664 LYS A CG    
5464 C  CD    . LYS A 664 ? 1.0199 0.9529 1.1837 -0.0670 0.0353  0.0332  664 LYS A CD    
5465 C  CE    . LYS A 664 ? 0.9304 0.8605 1.1003 -0.0634 0.0407  0.0497  664 LYS A CE    
5466 N  NZ    . LYS A 664 ? 0.9337 0.8451 1.1198 -0.0637 0.0413  0.0485  664 LYS A NZ    
5467 N  N     . GLN A 665 ? 0.7947 0.7793 0.9151 -0.0666 0.0284  0.0162  665 GLN A N     
5468 C  CA    . GLN A 665 ? 0.9109 0.9033 1.0287 -0.0688 0.0233  0.0064  665 GLN A CA    
5469 C  C     . GLN A 665 ? 0.9215 0.9031 1.0449 -0.0737 0.0158  -0.0072 665 GLN A C     
5470 O  O     . GLN A 665 ? 0.9945 0.9627 1.1126 -0.0715 0.0149  -0.0129 665 GLN A O     
5471 C  CB    . GLN A 665 ? 0.8016 0.8005 0.8961 -0.0621 0.0229  0.0025  665 GLN A CB    
5472 C  CG    . GLN A 665 ? 0.8729 0.8728 0.9596 -0.0626 0.0162  -0.0110 665 GLN A CG    
5473 C  CD    . GLN A 665 ? 1.0740 1.0782 1.1399 -0.0559 0.0160  -0.0135 665 GLN A CD    
5474 O  OE1   . GLN A 665 ? 1.0700 1.0771 1.1266 -0.0515 0.0200  -0.0059 665 GLN A OE1   
5475 N  NE2   . GLN A 665 ? 1.0903 1.0939 1.1480 -0.0552 0.0110  -0.0241 665 GLN A NE2   
5476 N  N     . ILE A 666 ? 0.9677 0.9548 1.1015 -0.0801 0.0103  -0.0119 666 ILE A N     
5477 C  CA    . ILE A 666 ? 0.9691 0.9463 1.1028 -0.0847 0.0014  -0.0264 666 ILE A CA    
5478 C  C     . ILE A 666 ? 1.0070 0.9891 1.1187 -0.0797 -0.0019 -0.0361 666 ILE A C     
5479 O  O     . ILE A 666 ? 0.9494 0.9459 1.0541 -0.0764 -0.0001 -0.0320 666 ILE A O     
5480 C  CB    . ILE A 666 ? 0.9313 0.9119 1.0876 -0.0949 -0.0052 -0.0265 666 ILE A CB    
5481 C  CG1   . ILE A 666 ? 1.0333 1.0333 1.1909 -0.0961 -0.0083 -0.0251 666 ILE A CG1   
5482 C  CG2   . ILE A 666 ? 0.8170 0.7968 0.9976 -0.0993 0.0001  -0.0130 666 ILE A CG2   
5483 C  CD1   . ILE A 666 ? 1.1889 1.1877 1.3351 -0.0982 -0.0190 -0.0395 666 ILE A CD1   
5484 N  N     . THR A 667 ? 1.1356 1.1046 1.2357 -0.0787 -0.0061 -0.0487 667 THR A N     
5485 C  CA    . THR A 667 ? 1.0988 1.0707 1.1772 -0.0726 -0.0073 -0.0563 667 THR A CA    
5486 C  C     . THR A 667 ? 1.0872 1.0570 1.1581 -0.0762 -0.0164 -0.0692 667 THR A C     
5487 O  O     . THR A 667 ? 1.2320 1.2048 1.2849 -0.0712 -0.0174 -0.0749 667 THR A O     
5488 C  CB    . THR A 667 ? 1.0003 0.9602 1.0676 -0.0654 -0.0020 -0.0582 667 THR A CB    
5489 O  OG1   . THR A 667 ? 1.1059 1.0471 1.1750 -0.0675 -0.0040 -0.0677 667 THR A OG1   
5490 C  CG2   . THR A 667 ? 0.7395 0.7010 0.8138 -0.0624 0.0052  -0.0449 667 THR A CG2   
5491 N  N     . ARG A 668 ? 1.1907 1.1557 1.2750 -0.0850 -0.0237 -0.0733 668 ARG A N     
5492 C  CA    . ARG A 668 ? 1.1280 1.0879 1.2031 -0.0891 -0.0343 -0.0865 668 ARG A CA    
5493 C  C     . ARG A 668 ? 1.2553 1.2179 1.3529 -0.1005 -0.0434 -0.0853 668 ARG A C     
5494 O  O     . ARG A 668 ? 1.1687 1.1372 1.2891 -0.1043 -0.0397 -0.0736 668 ARG A O     
5495 C  CB    . ARG A 668 ? 1.2377 1.1750 1.2968 -0.0861 -0.0342 -0.0994 668 ARG A CB    
5496 C  CG    . ARG A 668 ? 1.2445 1.1654 1.3170 -0.0869 -0.0287 -0.0968 668 ARG A CG    
5497 C  CD    . ARG A 668 ? 1.3296 1.2278 1.3859 -0.0815 -0.0260 -0.1088 668 ARG A CD    
5498 N  NE    . ARG A 668 ? 1.3161 1.2149 1.3667 -0.0711 -0.0145 -0.1020 668 ARG A NE    
5499 C  CZ    . ARG A 668 ? 1.4149 1.2963 1.4571 -0.0644 -0.0083 -0.1077 668 ARG A CZ    
5500 N  NH1   . ARG A 668 ? 1.3812 1.2406 1.4166 -0.0661 -0.0117 -0.1216 668 ARG A NH1   
5501 N  NH2   . ARG A 668 ? 1.4294 1.3150 1.4701 -0.0556 0.0012  -0.0992 668 ARG A NH2   
5502 N  N     . ASP A 669 ? 1.2893 1.2476 1.3807 -0.1063 -0.0556 -0.0967 669 ASP A N     
5503 C  CA    . ASP A 669 ? 1.2128 1.1727 1.3275 -0.1184 -0.0666 -0.0960 669 ASP A CA    
5504 C  C     . ASP A 669 ? 1.2696 1.2053 1.3929 -0.1237 -0.0681 -0.1019 669 ASP A C     
5505 O  O     . ASP A 669 ? 1.3184 1.2336 1.4226 -0.1187 -0.0653 -0.1127 669 ASP A O     
5506 C  CB    . ASP A 669 ? 1.2739 1.2388 1.3788 -0.1233 -0.0812 -0.1054 669 ASP A CB    
5507 C  CG    . ASP A 669 ? 1.5133 1.4708 1.6363 -0.1370 -0.0965 -0.1105 669 ASP A CG    
5508 O  OD1   . ASP A 669 ? 1.7038 1.6582 1.8546 -0.1439 -0.0957 -0.1031 669 ASP A OD1   
5509 O  OD2   . ASP A 669 ? 1.5578 1.5140 1.6681 -0.1413 -0.1104 -0.1207 669 ASP A OD2   
5510 N  N     . LEU A 670 ? 1.2181 1.1565 1.3722 -0.1335 -0.0718 -0.0937 670 LEU A N     
5511 C  CA    . LEU A 670 ? 1.1873 1.1052 1.3565 -0.1380 -0.0703 -0.0941 670 LEU A CA    
5512 C  C     . LEU A 670 ? 1.3765 1.2677 1.5345 -0.1439 -0.0824 -0.1131 670 LEU A C     
5513 O  O     . LEU A 670 ? 1.3966 1.2649 1.5590 -0.1447 -0.0797 -0.1171 670 LEU A O     
5514 C  CB    . LEU A 670 ? 1.1258 1.0560 1.3334 -0.1471 -0.0704 -0.0780 670 LEU A CB    
5515 C  CG    . LEU A 670 ? 1.1173 1.0686 1.3371 -0.1408 -0.0557 -0.0581 670 LEU A CG    
5516 C  CD1   . LEU A 670 ? 1.1933 1.1671 1.3992 -0.1339 -0.0528 -0.0546 670 LEU A CD1   
5517 C  CD2   . LEU A 670 ? 1.0881 1.0493 1.3464 -0.1499 -0.0554 -0.0425 670 LEU A CD2   
5518 N  N     . LYS A 671 ? 1.3846 1.2770 1.5270 -0.1476 -0.0958 -0.1249 671 LYS A N     
5519 C  CA    . LYS A 671 ? 1.3897 1.2538 1.5123 -0.1511 -0.1065 -0.1452 671 LYS A CA    
5520 C  C     . LYS A 671 ? 1.3942 1.2413 1.4836 -0.1377 -0.0954 -0.1554 671 LYS A C     
5521 O  O     . LYS A 671 ? 1.5215 1.3395 1.5979 -0.1375 -0.0973 -0.1698 671 LYS A O     
5522 C  CB    . LYS A 671 ? 1.3456 1.2157 1.4570 -0.1583 -0.1246 -0.1548 671 LYS A CB    
5523 C  CG    . LYS A 671 ? 1.4131 1.2936 1.4905 -0.1478 -0.1221 -0.1597 671 LYS A CG    
5524 C  CD    . LYS A 671 ? 1.5035 1.4059 1.5831 -0.1540 -0.1362 -0.1574 671 LYS A CD    
5525 C  CE    . LYS A 671 ? 1.5120 1.4216 1.5566 -0.1434 -0.1336 -0.1627 671 LYS A CE    
5526 N  NZ    . LYS A 671 ? 1.5100 1.4476 1.5628 -0.1358 -0.1222 -0.1465 671 LYS A NZ    
5527 N  N     . ASP A 672 ? 1.3263 1.1903 1.4027 -0.1262 -0.0834 -0.1479 672 ASP A N     
5528 C  CA    . ASP A 672 ? 1.4523 1.3047 1.5006 -0.1131 -0.0723 -0.1549 672 ASP A CA    
5529 C  C     . ASP A 672 ? 1.3991 1.2417 1.4584 -0.1068 -0.0579 -0.1473 672 ASP A C     
5530 O  O     . ASP A 672 ? 1.3990 1.2386 1.4417 -0.0951 -0.0467 -0.1476 672 ASP A O     
5531 C  CB    . ASP A 672 ? 1.4190 1.2939 1.4505 -0.1045 -0.0674 -0.1496 672 ASP A CB    
5532 C  CG    . ASP A 672 ? 1.4580 1.3414 1.4746 -0.1087 -0.0808 -0.1573 672 ASP A CG    
5533 O  OD1   . ASP A 672 ? 1.4738 1.3785 1.4836 -0.1039 -0.0787 -0.1506 672 ASP A OD1   
5534 O  OD2   . ASP A 672 ? 1.5520 1.4200 1.5633 -0.1168 -0.0941 -0.1700 672 ASP A OD2   
5535 N  N     . TYR A 673 ? 1.2659 1.1043 1.3542 -0.1142 -0.0582 -0.1392 673 TYR A N     
5536 C  CA    . TYR A 673 ? 1.2250 1.0544 1.3254 -0.1086 -0.0455 -0.1304 673 TYR A CA    
5537 C  C     . TYR A 673 ? 1.2634 1.0592 1.3606 -0.1093 -0.0465 -0.1438 673 TYR A C     
5538 O  O     . TYR A 673 ? 1.3733 1.1544 1.4781 -0.1200 -0.0586 -0.1531 673 TYR A O     
5539 C  CB    . TYR A 673 ? 1.2275 1.0719 1.3610 -0.1150 -0.0432 -0.1118 673 TYR A CB    
5540 C  CG    . TYR A 673 ? 1.1820 1.0516 1.3159 -0.1077 -0.0332 -0.0958 673 TYR A CG    
5541 C  CD1   . TYR A 673 ? 1.2338 1.1015 1.3592 -0.0969 -0.0212 -0.0902 673 TYR A CD1   
5542 C  CD2   . TYR A 673 ? 1.0923 0.9867 1.2353 -0.1116 -0.0360 -0.0864 673 TYR A CD2   
5543 C  CE1   . TYR A 673 ? 1.1404 1.0290 1.2643 -0.0910 -0.0138 -0.0768 673 TYR A CE1   
5544 C  CE2   . TYR A 673 ? 1.0930 1.0074 1.2336 -0.1047 -0.0270 -0.0734 673 TYR A CE2   
5545 C  CZ    . TYR A 673 ? 1.0296 0.9402 1.1596 -0.0948 -0.0166 -0.0692 673 TYR A CZ    
5546 O  OH    . TYR A 673 ? 1.0965 1.0249 1.2224 -0.0886 -0.0094 -0.0572 673 TYR A OH    
5547 N  N     . LYS A 674 ? 1.3174 1.1007 1.4041 -0.0978 -0.0342 -0.1448 674 LYS A N     
5548 C  CA    . LYS A 674 ? 1.3404 1.0906 1.4238 -0.0957 -0.0320 -0.1567 674 LYS A CA    
5549 C  C     . LYS A 674 ? 1.3117 1.0543 1.4228 -0.0952 -0.0234 -0.1434 674 LYS A C     
5550 O  O     . LYS A 674 ? 1.3129 1.0267 1.4273 -0.0946 -0.0219 -0.1517 674 LYS A O     
5551 C  CB    . LYS A 674 ? 1.3259 1.0649 1.3780 -0.0819 -0.0232 -0.1676 674 LYS A CB    
5552 C  CG    . LYS A 674 ? 1.4169 1.1650 1.4393 -0.0804 -0.0297 -0.1785 674 LYS A CG    
5553 C  CD    . LYS A 674 ? 1.4934 1.2256 1.4853 -0.0669 -0.0203 -0.1905 674 LYS A CD    
5554 C  CE    . LYS A 674 ? 1.4703 1.1837 1.4325 -0.0697 -0.0310 -0.2120 674 LYS A CE    
5555 N  NZ    . LYS A 674 ? 1.5222 1.2131 1.4551 -0.0560 -0.0201 -0.2249 674 LYS A NZ    
5556 N  N     . ALA A 675 ? 1.4081 1.1747 1.5378 -0.0948 -0.0177 -0.1233 675 ALA A N     
5557 C  CA    . ALA A 675 ? 1.3158 1.0783 1.4714 -0.0943 -0.0097 -0.1081 675 ALA A CA    
5558 C  C     . ALA A 675 ? 1.2996 1.0875 1.4776 -0.1018 -0.0115 -0.0899 675 ALA A C     
5559 O  O     . ALA A 675 ? 1.1970 1.0098 1.3681 -0.0976 -0.0078 -0.0803 675 ALA A O     
5560 C  CB    . ALA A 675 ? 1.2500 1.0137 1.3983 -0.0803 0.0038  -0.1007 675 ALA A CB    
5561 N  N     . THR A 676 ? 1.1927 0.9734 1.3974 -0.1126 -0.0165 -0.0851 676 THR A N     
5562 C  CA    . THR A 676 ? 1.2369 1.0408 1.4650 -0.1201 -0.0175 -0.0676 676 THR A CA    
5563 C  C     . THR A 676 ? 1.1761 0.9842 1.4213 -0.1154 -0.0057 -0.0474 676 THR A C     
5564 O  O     . THR A 676 ? 1.1197 0.9118 1.3875 -0.1195 -0.0044 -0.0420 676 THR A O     
5565 C  CB    . THR A 676 ? 1.0982 0.8947 1.3487 -0.1349 -0.0298 -0.0715 676 THR A CB    
5566 O  OG1   . THR A 676 ? 1.1743 0.9711 1.4070 -0.1393 -0.0421 -0.0885 676 THR A OG1   
5567 C  CG2   . THR A 676 ? 1.0618 0.8823 1.3408 -0.1416 -0.0281 -0.0507 676 THR A CG2   
5568 N  N     . GLY A 677 ? 1.0225 0.8513 1.2563 -0.1068 0.0023  -0.0362 677 GLY A N     
5569 C  CA    . GLY A 677 ? 1.0091 0.8463 1.2562 -0.1030 0.0120  -0.0155 677 GLY A CA    
5570 C  C     . GLY A 677 ? 1.0050 0.8613 1.2720 -0.1103 0.0122  0.0002  677 GLY A C     
5571 O  O     . GLY A 677 ? 1.0908 0.9564 1.3630 -0.1182 0.0049  -0.0042 677 GLY A O     
5572 N  N     . PRO A 678 ? 0.9301 0.7931 1.2090 -0.1074 0.0211  0.0201  678 PRO A N     
5573 C  CA    . PRO A 678 ? 1.0183 0.8989 1.3173 -0.1132 0.0239  0.0374  678 PRO A CA    
5574 C  C     . PRO A 678 ? 0.9820 0.8863 1.2701 -0.1137 0.0223  0.0368  678 PRO A C     
5575 O  O     . PRO A 678 ? 0.9179 0.8325 1.2260 -0.1219 0.0198  0.0423  678 PRO A O     
5576 C  CB    . PRO A 678 ? 0.8549 0.7402 1.1551 -0.1059 0.0348  0.0573  678 PRO A CB    
5577 C  CG    . PRO A 678 ? 0.9033 0.7667 1.2006 -0.1008 0.0356  0.0517  678 PRO A CG    
5578 C  CD    . PRO A 678 ? 0.9277 0.7811 1.2048 -0.0989 0.0288  0.0284  678 PRO A CD    
5579 N  N     . HIS A 679 ? 0.9158 0.8289 1.1750 -0.1051 0.0236  0.0311  679 HIS A N     
5580 C  CA    . HIS A 679 ? 0.9372 0.8716 1.1863 -0.1046 0.0228  0.0310  679 HIS A CA    
5581 C  C     . HIS A 679 ? 0.9522 0.8859 1.2034 -0.1120 0.0116  0.0152  679 HIS A C     
5582 O  O     . HIS A 679 ? 0.8580 0.8084 1.1175 -0.1161 0.0097  0.0188  679 HIS A O     
5583 C  CB    . HIS A 679 ? 0.9460 0.8884 1.1647 -0.0939 0.0266  0.0294  679 HIS A CB    
5584 C  CG    . HIS A 679 ? 0.9043 0.8377 1.1028 -0.0907 0.0205  0.0110  679 HIS A CG    
5585 N  ND1   . HIS A 679 ? 0.9010 0.8138 1.0993 -0.0900 0.0183  0.0014  679 HIS A ND1   
5586 C  CD2   . HIS A 679 ? 0.8582 0.8005 1.0361 -0.0872 0.0172  0.0014  679 HIS A CD2   
5587 C  CE1   . HIS A 679 ? 0.8132 0.7232 0.9908 -0.0860 0.0145  -0.0131 679 HIS A CE1   
5588 N  NE2   . HIS A 679 ? 0.8125 0.7406 0.9780 -0.0846 0.0134  -0.0130 679 HIS A NE2   
5589 N  N     . VAL A 680 ? 1.0105 0.9248 1.2538 -0.1133 0.0044  -0.0019 680 VAL A N     
5590 C  CA    . VAL A 680 ? 0.9458 0.8575 1.1882 -0.1206 -0.0077 -0.0173 680 VAL A CA    
5591 C  C     . VAL A 680 ? 1.0236 0.9319 1.2985 -0.1334 -0.0143 -0.0134 680 VAL A C     
5592 O  O     . VAL A 680 ? 1.0061 0.9255 1.2904 -0.1409 -0.0229 -0.0158 680 VAL A O     
5593 C  CB    . VAL A 680 ? 0.9945 0.8849 1.2152 -0.1171 -0.0124 -0.0369 680 VAL A CB    
5594 C  CG1   . VAL A 680 ? 1.0648 0.9420 1.2901 -0.1272 -0.0260 -0.0525 680 VAL A CG1   
5595 C  CG2   . VAL A 680 ? 1.0003 0.9007 1.1911 -0.1073 -0.0100 -0.0426 680 VAL A CG2   
5596 N  N     . ALA A 681 ? 0.9917 0.8850 1.2863 -0.1363 -0.0109 -0.0062 681 ALA A N     
5597 C  CA    . ALA A 681 ? 0.9443 0.8334 1.2735 -0.1492 -0.0171 -0.0007 681 ALA A CA    
5598 C  C     . ALA A 681 ? 1.0428 0.9597 1.3932 -0.1528 -0.0134 0.0175  681 ALA A C     
5599 O  O     . ALA A 681 ? 0.9932 0.9161 1.3671 -0.1639 -0.0226 0.0182  681 ALA A O     
5600 C  CB    . ALA A 681 ? 0.9681 0.8373 1.3153 -0.1501 -0.0118 0.0069  681 ALA A CB    
5601 N  N     . VAL A 682 ? 0.9397 0.8735 1.2818 -0.1434 -0.0001 0.0326  682 VAL A N     
5602 C  CA    . VAL A 682 ? 0.9302 0.8902 1.2879 -0.1443 0.0060  0.0496  682 VAL A CA    
5603 C  C     . VAL A 682 ? 0.9217 0.8971 1.2709 -0.1457 -0.0017 0.0403  682 VAL A C     
5604 O  O     . VAL A 682 ? 1.0400 1.0305 1.4145 -0.1533 -0.0053 0.0476  682 VAL A O     
5605 C  CB    . VAL A 682 ? 0.9379 0.9091 1.2812 -0.1327 0.0216  0.0652  682 VAL A CB    
5606 C  CG1   . VAL A 682 ? 0.8685 0.8662 1.2175 -0.1305 0.0289  0.0787  682 VAL A CG1   
5607 C  CG2   . VAL A 682 ? 0.9248 0.8853 1.2847 -0.1329 0.0293  0.0798  682 VAL A CG2   
5608 N  N     . ALA A 683 ? 0.8448 0.8173 1.1605 -0.1385 -0.0045 0.0253  683 ALA A N     
5609 C  CA    . ALA A 683 ? 0.9751 0.9618 1.2810 -0.1388 -0.0117 0.0170  683 ALA A CA    
5610 C  C     . ALA A 683 ? 1.1088 1.0896 1.4305 -0.1513 -0.0282 0.0058  683 ALA A C     
5611 O  O     . ALA A 683 ? 1.1580 1.1552 1.4844 -0.1544 -0.0348 0.0048  683 ALA A O     
5612 C  CB    . ALA A 683 ? 0.7712 0.7539 1.0387 -0.1287 -0.0111 0.0039  683 ALA A CB    
5613 N  N     . LYS A 684 ? 1.1086 1.0658 1.4385 -0.1585 -0.0357 -0.0027 684 LYS A N     
5614 C  CA    . LYS A 684 ? 0.9745 0.9231 1.3174 -0.1712 -0.0533 -0.0146 684 LYS A CA    
5615 C  C     . LYS A 684 ? 1.0380 0.9999 1.4248 -0.1831 -0.0569 0.0009  684 LYS A C     
5616 O  O     . LYS A 684 ? 1.1170 1.0887 1.5174 -0.1921 -0.0702 -0.0021 684 LYS A O     
5617 C  CB    . LYS A 684 ? 0.9096 0.8249 1.2430 -0.1740 -0.0600 -0.0310 684 LYS A CB    
5618 C  CG    . LYS A 684 ? 0.8967 0.7993 1.1883 -0.1645 -0.0607 -0.0498 684 LYS A CG    
5619 C  CD    . LYS A 684 ? 1.0740 0.9441 1.3556 -0.1629 -0.0605 -0.0619 684 LYS A CD    
5620 C  CE    . LYS A 684 ? 1.1438 0.9929 1.4090 -0.1688 -0.0762 -0.0850 684 LYS A CE    
5621 N  NZ    . LYS A 684 ? 1.0668 0.8967 1.2958 -0.1575 -0.0713 -0.1004 684 LYS A NZ    
5622 N  N     . ARG A 685 ? 1.0273 0.9906 1.4379 -0.1832 -0.0455 0.0188  685 ARG A N     
5623 C  CA    . ARG A 685 ? 1.0953 1.0748 1.5498 -0.1932 -0.0460 0.0371  685 ARG A CA    
5624 C  C     . ARG A 685 ? 1.0946 1.1069 1.5548 -0.1886 -0.0391 0.0504  685 ARG A C     
5625 O  O     . ARG A 685 ? 1.1940 1.2233 1.6902 -0.1976 -0.0432 0.0624  685 ARG A O     
5626 C  CB    . ARG A 685 ? 0.9576 0.9312 1.4342 -0.1931 -0.0334 0.0548  685 ARG A CB    
5627 C  CG    . ARG A 685 ? 0.9526 0.8937 1.4187 -0.1930 -0.0353 0.0436  685 ARG A CG    
5628 C  CD    . ARG A 685 ? 0.8807 0.8154 1.3813 -0.1981 -0.0282 0.0618  685 ARG A CD    
5629 N  NE    . ARG A 685 ? 1.1542 1.0917 1.6414 -0.1854 -0.0099 0.0755  685 ARG A NE    
5630 C  CZ    . ARG A 685 ? 1.1981 1.1153 1.6608 -0.1773 -0.0060 0.0672  685 ARG A CZ    
5631 N  NH1   . ARG A 685 ? 1.2065 1.0981 1.6541 -0.1793 -0.0169 0.0451  685 ARG A NH1   
5632 N  NH2   . ARG A 685 ? 0.9855 0.9084 1.4383 -0.1665 0.0093  0.0820  685 ARG A NH2   
5633 N  N     . LEU A 686 ? 1.0403 1.0615 1.4675 -0.1748 -0.0285 0.0490  686 LEU A N     
5634 C  CA    . LEU A 686 ? 1.1147 1.1640 1.5437 -0.1695 -0.0224 0.0587  686 LEU A CA    
5635 C  C     . LEU A 686 ? 1.2387 1.2948 1.6662 -0.1753 -0.0390 0.0460  686 LEU A C     
5636 O  O     . LEU A 686 ? 1.2356 1.3147 1.6876 -0.1788 -0.0407 0.0565  686 LEU A O     
5637 C  CB    . LEU A 686 ? 1.0057 1.0592 1.3988 -0.1535 -0.0076 0.0598  686 LEU A CB    
5638 C  CG    . LEU A 686 ? 0.9953 1.0459 1.3865 -0.1463 0.0093  0.0747  686 LEU A CG    
5639 C  CD1   . LEU A 686 ? 0.7736 0.8366 1.1371 -0.1321 0.0233  0.0802  686 LEU A CD1   
5640 C  CD2   . LEU A 686 ? 0.8529 0.9126 1.2864 -0.1537 0.0149  0.0952  686 LEU A CD2   
5641 N  N     . ALA A 687 ? 1.1888 1.2260 1.5882 -0.1760 -0.0511 0.0243  687 ALA A N     
5642 C  CA    . ALA A 687 ? 1.1456 1.1868 1.5417 -0.1824 -0.0687 0.0117  687 ALA A CA    
5643 C  C     . ALA A 687 ? 1.1676 1.2104 1.6033 -0.1990 -0.0843 0.0150  687 ALA A C     
5644 O  O     . ALA A 687 ? 1.0753 1.1310 1.5198 -0.2053 -0.0981 0.0123  687 ALA A O     
5645 C  CB    . ALA A 687 ? 1.0504 1.0681 1.4070 -0.1795 -0.0772 -0.0118 687 ALA A CB    
5646 N  N     . ALA A 688 ? 1.1835 1.2136 1.6446 -0.2067 -0.0834 0.0216  688 ALA A N     
5647 C  CA    . ALA A 688 ? 1.1551 1.1877 1.6594 -0.2234 -0.0978 0.0275  688 ALA A CA    
5648 C  C     . ALA A 688 ? 1.2708 1.3370 1.8149 -0.2250 -0.0905 0.0520  688 ALA A C     
5649 O  O     . ALA A 688 ? 1.0578 1.1338 1.6395 -0.2387 -0.1046 0.0580  688 ALA A O     
5650 C  CB    . ALA A 688 ? 0.9294 0.9370 1.4504 -0.2308 -0.0981 0.0280  688 ALA A CB    
5651 N  N     . ARG A 689 ? 1.2964 1.3800 1.8336 -0.2113 -0.0690 0.0666  689 ARG A N     
5652 C  CA    . ARG A 689 ? 1.3039 1.4200 1.8726 -0.2095 -0.0592 0.0890  689 ARG A CA    
5653 C  C     . ARG A 689 ? 1.1745 1.3099 1.7262 -0.2019 -0.0606 0.0852  689 ARG A C     
5654 O  O     . ARG A 689 ? 1.2016 1.3640 1.7758 -0.1978 -0.0507 0.1029  689 ARG A O     
5655 C  CB    . ARG A 689 ? 1.3209 1.4443 1.8915 -0.1982 -0.0338 0.1082  689 ARG A CB    
5656 C  CG    . ARG A 689 ? 1.2437 1.3438 1.8138 -0.2001 -0.0287 0.1091  689 ARG A CG    
5657 C  CD    . ARG A 689 ? 1.2726 1.3864 1.8607 -0.1933 -0.0064 0.1346  689 ARG A CD    
5658 N  NE    . ARG A 689 ? 1.5375 1.6323 2.0986 -0.1848 0.0051  0.1333  689 ARG A NE    
5659 C  CZ    . ARG A 689 ? 1.5094 1.6128 2.0597 -0.1726 0.0259  0.1488  689 ARG A CZ    
5660 N  NH1   . ARG A 689 ? 1.4879 1.6172 2.0503 -0.1662 0.0396  0.1664  689 ARG A NH1   
5661 N  NH2   . ARG A 689 ? 1.1797 1.2648 1.7057 -0.1662 0.0332  0.1468  689 ARG A NH2   
5662 N  N     . GLY A 690 ? 1.1512 1.2732 1.6644 -0.1992 -0.0714 0.0634  690 GLY A N     
5663 C  CA    . GLY A 690 ? 1.0706 1.2091 1.5669 -0.1921 -0.0733 0.0597  690 GLY A CA    
5664 C  C     . GLY A 690 ? 1.1419 1.2910 1.6159 -0.1748 -0.0512 0.0674  690 GLY A C     
5665 O  O     . GLY A 690 ? 1.2231 1.3968 1.7143 -0.1694 -0.0418 0.0824  690 GLY A O     
5666 N  N     . VAL A 691 ? 1.1638 1.2938 1.5998 -0.1658 -0.0430 0.0573  691 VAL A N     
5667 C  CA    . VAL A 691 ? 1.1846 1.3202 1.5939 -0.1500 -0.0246 0.0616  691 VAL A CA    
5668 C  C     . VAL A 691 ? 1.2161 1.3402 1.5828 -0.1434 -0.0303 0.0425  691 VAL A C     
5669 O  O     . VAL A 691 ? 1.2370 1.3442 1.5904 -0.1494 -0.0447 0.0261  691 VAL A O     
5670 C  CB    . VAL A 691 ? 1.1820 1.3080 1.5865 -0.1444 -0.0081 0.0708  691 VAL A CB    
5671 C  CG1   . VAL A 691 ? 1.2167 1.3547 1.6045 -0.1296 0.0113  0.0811  691 VAL A CG1   
5672 C  CG2   . VAL A 691 ? 1.0336 1.1633 1.4806 -0.1544 -0.0070 0.0862  691 VAL A CG2   
5673 N  N     . LYS A 692 ? 1.2166 1.3495 1.5620 -0.1306 -0.0186 0.0449  692 LYS A N     
5674 C  CA    . LYS A 692 ? 1.3869 1.5117 1.6945 -0.1236 -0.0223 0.0296  692 LYS A CA    
5675 C  C     . LYS A 692 ? 1.4556 1.5579 1.7353 -0.1193 -0.0178 0.0209  692 LYS A C     
5676 O  O     . LYS A 692 ? 1.5521 1.6527 1.8166 -0.1099 -0.0040 0.0264  692 LYS A O     
5677 C  CB    . LYS A 692 ? 1.5193 1.6598 1.8164 -0.1119 -0.0115 0.0358  692 LYS A CB    
5678 C  CG    . LYS A 692 ? 1.6442 1.8092 1.9749 -0.1127 -0.0076 0.0516  692 LYS A CG    
5679 C  CD    . LYS A 692 ? 1.6462 1.8240 1.9644 -0.1027 -0.0033 0.0521  692 LYS A CD    
5680 C  CE    . LYS A 692 ? 1.6069 1.8078 1.9550 -0.0988 0.0081  0.0706  692 LYS A CE    
5681 N  NZ    . LYS A 692 ? 1.3179 1.5231 1.6450 -0.0840 0.0227  0.0731  692 LYS A NZ    
5682 N  N     . ILE A 693 ? 1.3686 1.4528 1.6409 -0.1261 -0.0300 0.0070  693 ILE A N     
5683 C  CA    . ILE A 693 ? 1.3663 1.4297 1.6118 -0.1211 -0.0264 -0.0022 693 ILE A CA    
5684 C  C     . ILE A 693 ? 1.2170 1.2741 1.4323 -0.1171 -0.0339 -0.0181 693 ILE A C     
5685 O  O     . ILE A 693 ? 1.1272 1.1739 1.3382 -0.1235 -0.0469 -0.0308 693 ILE A O     
5686 C  CB    . ILE A 693 ? 1.2756 1.3198 1.5331 -0.1294 -0.0309 -0.0056 693 ILE A CB    
5687 C  CG1   . ILE A 693 ? 1.0114 1.0601 1.2967 -0.1318 -0.0210 0.0120  693 ILE A CG1   
5688 C  CG2   . ILE A 693 ? 1.1873 1.2114 1.4171 -0.1228 -0.0272 -0.0152 693 ILE A CG2   
5689 C  CD1   . ILE A 693 ? 1.2865 1.3541 1.6082 -0.1396 -0.0232 0.0248  693 ILE A CD1   
5690 N  N     . ARG A 694 ? 1.2263 1.2890 1.4201 -0.1066 -0.0258 -0.0173 694 ARG A N     
5691 C  CA    . ARG A 694 ? 1.1992 1.2573 1.3649 -0.1015 -0.0305 -0.0296 694 ARG A CA    
5692 C  C     . ARG A 694 ? 1.1272 1.1709 1.2699 -0.0939 -0.0229 -0.0334 694 ARG A C     
5693 O  O     . ARG A 694 ? 0.9884 1.0289 1.1348 -0.0913 -0.0134 -0.0249 694 ARG A O     
5694 C  CB    . ARG A 694 ? 1.1833 1.2596 1.3448 -0.0956 -0.0282 -0.0251 694 ARG A CB    
5695 C  CG    . ARG A 694 ? 1.4002 1.4957 1.5907 -0.1001 -0.0294 -0.0140 694 ARG A CG    
5696 C  CD    . ARG A 694 ? 1.4963 1.6076 1.6829 -0.0912 -0.0214 -0.0066 694 ARG A CD    
5697 N  NE    . ARG A 694 ? 1.4692 1.5997 1.6805 -0.0951 -0.0266 0.0005  694 ARG A NE    
5698 C  CZ    . ARG A 694 ? 1.4816 1.6243 1.6889 -0.0904 -0.0284 0.0010  694 ARG A CZ    
5699 N  NH1   . ARG A 694 ? 1.3326 1.4699 1.5122 -0.0821 -0.0257 -0.0054 694 ARG A NH1   
5700 N  NH2   . ARG A 694 ? 1.3976 1.5588 1.6316 -0.0943 -0.0334 0.0092  694 ARG A NH2   
5701 N  N     . PRO A 695 ? 1.2112 1.2463 1.3306 -0.0903 -0.0269 -0.0451 695 PRO A N     
5702 C  CA    . PRO A 695 ? 0.9940 1.0188 1.0939 -0.0824 -0.0194 -0.0467 695 PRO A CA    
5703 C  C     . PRO A 695 ? 1.0070 1.0417 1.1027 -0.0752 -0.0096 -0.0361 695 PRO A C     
5704 O  O     . PRO A 695 ? 1.1293 1.1766 1.2213 -0.0720 -0.0092 -0.0338 695 PRO A O     
5705 C  CB    . PRO A 695 ? 0.8539 0.8744 0.9322 -0.0792 -0.0250 -0.0586 695 PRO A CB    
5706 C  CG    . PRO A 695 ? 1.0363 1.0548 1.1207 -0.0873 -0.0367 -0.0667 695 PRO A CG    
5707 C  CD    . PRO A 695 ? 1.1378 1.1697 1.2488 -0.0942 -0.0390 -0.0573 695 PRO A CD    
5708 N  N     . GLY A 696 ? 0.9421 0.9703 1.0379 -0.0726 -0.0020 -0.0296 696 GLY A N     
5709 C  CA    . GLY A 696 ? 0.9382 0.9721 1.0259 -0.0659 0.0065  -0.0205 696 GLY A CA    
5710 C  C     . GLY A 696 ? 1.0428 1.0818 1.1454 -0.0671 0.0140  -0.0077 696 GLY A C     
5711 O  O     . GLY A 696 ? 1.0341 1.0737 1.1267 -0.0613 0.0214  -0.0003 696 GLY A O     
5712 N  N     . THR A 697 ? 0.9087 0.9515 1.0347 -0.0744 0.0120  -0.0042 697 THR A N     
5713 C  CA    . THR A 697 ? 0.9361 0.9848 1.0785 -0.0752 0.0205  0.0099  697 THR A CA    
5714 C  C     . THR A 697 ? 0.9692 1.0053 1.1119 -0.0751 0.0247  0.0149  697 THR A C     
5715 O  O     . THR A 697 ? 0.9340 0.9567 1.0781 -0.0785 0.0193  0.0077  697 THR A O     
5716 C  CB    . THR A 697 ? 1.1148 1.1727 1.2866 -0.0838 0.0167  0.0139  697 THR A CB    
5717 O  OG1   . THR A 697 ? 1.0811 1.1266 1.2676 -0.0918 0.0112  0.0113  697 THR A OG1   
5718 C  CG2   . THR A 697 ? 1.2315 1.2988 1.4040 -0.0858 0.0079  0.0060  697 THR A CG2   
5719 N  N     . VAL A 698 ? 0.9612 1.0012 1.1020 -0.0706 0.0348  0.0278  698 VAL A N     
5720 C  CA    . VAL A 698 ? 0.8119 0.8419 0.9510 -0.0692 0.0395  0.0352  698 VAL A CA    
5721 C  C     . VAL A 698 ? 0.9445 0.9760 1.1121 -0.0757 0.0430  0.0465  698 VAL A C     
5722 O  O     . VAL A 698 ? 0.9041 0.9489 1.0854 -0.0763 0.0490  0.0565  698 VAL A O     
5723 C  CB    . VAL A 698 ? 0.7596 0.7918 0.8761 -0.0604 0.0475  0.0429  698 VAL A CB    
5724 C  CG1   . VAL A 698 ? 0.9465 0.9707 1.0636 -0.0593 0.0523  0.0537  698 VAL A CG1   
5725 C  CG2   . VAL A 698 ? 0.9696 0.9982 1.0606 -0.0551 0.0426  0.0322  698 VAL A CG2   
5726 N  N     . ILE A 699 ? 0.9453 0.9634 1.1236 -0.0801 0.0400  0.0456  699 ILE A N     
5727 C  CA    . ILE A 699 ? 0.7944 0.8113 1.0006 -0.0864 0.0434  0.0575  699 ILE A CA    
5728 C  C     . ILE A 699 ? 0.8733 0.8888 1.0729 -0.0805 0.0536  0.0726  699 ILE A C     
5729 O  O     . ILE A 699 ? 1.0315 1.0370 1.2133 -0.0756 0.0531  0.0704  699 ILE A O     
5730 C  CB    . ILE A 699 ? 0.7509 0.7515 0.9726 -0.0943 0.0344  0.0482  699 ILE A CB    
5731 C  CG1   . ILE A 699 ? 0.7450 0.7445 0.9639 -0.0987 0.0229  0.0309  699 ILE A CG1   
5732 C  CG2   . ILE A 699 ? 0.7485 0.7483 1.0036 -0.1024 0.0365  0.0603  699 ILE A CG2   
5733 C  CD1   . ILE A 699 ? 0.9459 0.9633 1.1786 -0.1028 0.0209  0.0336  699 ILE A CD1   
5734 N  N     . SER A 700 ? 0.8168 0.8430 1.0309 -0.0808 0.0629  0.0889  700 SER A N     
5735 C  CA    . SER A 700 ? 0.8680 0.8942 1.0751 -0.0751 0.0733  0.1053  700 SER A CA    
5736 C  C     . SER A 700 ? 0.8868 0.9112 1.1274 -0.0821 0.0769  0.1190  700 SER A C     
5737 O  O     . SER A 700 ? 0.9454 0.9825 1.2075 -0.0851 0.0831  0.1303  700 SER A O     
5738 C  CB    . SER A 700 ? 0.7649 0.8049 0.9543 -0.0670 0.0836  0.1137  700 SER A CB    
5739 O  OG    . SER A 700 ? 0.8734 0.9156 1.0387 -0.0625 0.0791  0.0999  700 SER A OG    
5740 N  N     . TYR A 701 ? 0.9043 0.9132 1.1516 -0.0846 0.0735  0.1191  701 TYR A N     
5741 C  CA    . TYR A 701 ? 0.8584 0.8621 1.1397 -0.0923 0.0751  0.1304  701 TYR A CA    
5742 C  C     . TYR A 701 ? 0.8475 0.8463 1.1259 -0.0874 0.0835  0.1476  701 TYR A C     
5743 O  O     . TYR A 701 ? 0.9567 0.9500 1.2088 -0.0799 0.0834  0.1460  701 TYR A O     
5744 C  CB    . TYR A 701 ? 0.8802 0.8667 1.1775 -0.1008 0.0630  0.1150  701 TYR A CB    
5745 C  CG    . TYR A 701 ? 0.9228 0.8915 1.2021 -0.0964 0.0586  0.1049  701 TYR A CG    
5746 C  CD1   . TYR A 701 ? 0.9366 0.8923 1.2263 -0.0958 0.0617  0.1146  701 TYR A CD1   
5747 C  CD2   . TYR A 701 ? 0.8994 0.8649 1.1537 -0.0925 0.0519  0.0869  701 TYR A CD2   
5748 C  CE1   . TYR A 701 ? 0.8611 0.8017 1.1374 -0.0911 0.0585  0.1067  701 TYR A CE1   
5749 C  CE2   . TYR A 701 ? 0.8958 0.8466 1.1367 -0.0880 0.0491  0.0791  701 TYR A CE2   
5750 C  CZ    . TYR A 701 ? 0.7697 0.7084 1.0221 -0.0871 0.0525  0.0890  701 TYR A CZ    
5751 O  OH    . TYR A 701 ? 0.8898 0.8151 1.1316 -0.0818 0.0504  0.0826  701 TYR A OH    
5752 N  N     . ILE A 702 ? 0.7374 0.7394 1.0449 -0.0920 0.0903  0.1653  702 ILE A N     
5753 C  CA    . ILE A 702 ? 0.7649 0.7611 1.0774 -0.0892 0.0976  0.1836  702 ILE A CA    
5754 C  C     . ILE A 702 ? 0.8885 0.8694 1.2367 -0.0990 0.0923  0.1842  702 ILE A C     
5755 O  O     . ILE A 702 ? 0.9101 0.8904 1.2849 -0.1088 0.0865  0.1779  702 ILE A O     
5756 C  CB    . ILE A 702 ? 0.7291 0.7420 1.0435 -0.0848 0.1124  0.2070  702 ILE A CB    
5757 C  CG1   . ILE A 702 ? 0.7990 0.8063 1.1083 -0.0797 0.1196  0.2257  702 ILE A CG1   
5758 C  CG2   . ILE A 702 ? 0.7181 0.7407 1.0729 -0.0938 0.1160  0.2167  702 ILE A CG2   
5759 C  CD1   . ILE A 702 ? 0.8546 0.8767 1.1460 -0.0710 0.1341  0.2453  702 ILE A CD1   
5760 N  N     . VAL A 703 ? 0.8681 0.8356 1.2172 -0.0964 0.0935  0.1914  703 VAL A N     
5761 C  CA    . VAL A 703 ? 0.8576 0.8068 1.2388 -0.1043 0.0892  0.1921  703 VAL A CA    
5762 C  C     . VAL A 703 ? 0.8415 0.7964 1.2513 -0.1071 0.0995  0.2186  703 VAL A C     
5763 O  O     . VAL A 703 ? 0.9104 0.8724 1.3074 -0.0992 0.1092  0.2370  703 VAL A O     
5764 C  CB    . VAL A 703 ? 0.9419 0.8722 1.3106 -0.0993 0.0849  0.1847  703 VAL A CB    
5765 C  CG1   . VAL A 703 ? 0.9744 0.8819 1.3715 -0.1076 0.0777  0.1754  703 VAL A CG1   
5766 C  CG2   . VAL A 703 ? 0.7724 0.7041 1.1054 -0.0927 0.0791  0.1657  703 VAL A CG2   
5767 N  N     . LEU A 704 ? 0.8505 0.8022 1.2988 -0.1185 0.0968  0.2210  704 LEU A N     
5768 C  CA    . LEU A 704 ? 0.8897 0.8478 1.3709 -0.1225 0.1065  0.2470  704 LEU A CA    
5769 C  C     . LEU A 704 ? 0.9089 0.8454 1.4127 -0.1255 0.1053  0.2544  704 LEU A C     
5770 O  O     . LEU A 704 ? 0.9830 0.8976 1.4881 -0.1285 0.0950  0.2363  704 LEU A O     
5771 C  CB    . LEU A 704 ? 0.9107 0.8788 1.4267 -0.1340 0.1040  0.2484  704 LEU A CB    
5772 C  CG    . LEU A 704 ? 1.0047 0.9969 1.5053 -0.1306 0.1078  0.2463  704 LEU A CG    
5773 C  CD1   . LEU A 704 ? 0.9266 0.9285 1.4667 -0.1429 0.1033  0.2478  704 LEU A CD1   
5774 C  CD2   . LEU A 704 ? 0.9722 0.9825 1.4540 -0.1191 0.1250  0.2683  704 LEU A CD2   
5775 N  N     . LYS A 705 ? 0.9447 0.8872 1.4660 -0.1241 0.1169  0.2819  705 LYS A N     
5776 C  CA    . LYS A 705 ? 0.8680 0.7913 1.4135 -0.1264 0.1174  0.2930  705 LYS A CA    
5777 C  C     . LYS A 705 ? 0.9568 0.8611 1.5421 -0.1405 0.1069  0.2823  705 LYS A C     
5778 O  O     . LYS A 705 ? 1.0772 0.9906 1.6926 -0.1505 0.1063  0.2877  705 LYS A O     
5779 C  CB    . LYS A 705 ? 0.8196 0.7556 1.3789 -0.1230 0.1323  0.3267  705 LYS A CB    
5780 C  CG    . LYS A 705 ? 0.7452 0.6624 1.3314 -0.1248 0.1338  0.3415  705 LYS A CG    
5781 C  CD    . LYS A 705 ? 0.7580 0.6894 1.3487 -0.1188 0.1493  0.3758  705 LYS A CD    
5782 C  CE    . LYS A 705 ? 0.7781 0.6912 1.4028 -0.1220 0.1509  0.3927  705 LYS A CE    
5783 N  NZ    . LYS A 705 ? 0.9373 0.8637 1.5599 -0.1143 0.1657  0.4264  705 LYS A NZ    
5784 N  N     . GLY A 706 ? 1.0425 0.9203 1.6283 -0.1412 0.0986  0.2673  706 GLY A N     
5785 C  CA    . GLY A 706 ? 1.1459 1.0007 1.7646 -0.1540 0.0877  0.2544  706 GLY A CA    
5786 C  C     . GLY A 706 ? 1.2418 1.0670 1.8496 -0.1505 0.0808  0.2357  706 GLY A C     
5787 O  O     . GLY A 706 ? 1.0743 0.8974 1.6594 -0.1388 0.0861  0.2397  706 GLY A O     
5788 N  N     . SER A 707 ? 1.4111 1.2130 2.0354 -0.1606 0.0687  0.2153  707 SER A N     
5789 C  CA    . SER A 707 ? 1.3411 1.1119 1.9559 -0.1574 0.0626  0.1951  707 SER A CA    
5790 C  C     . SER A 707 ? 1.2886 1.0487 1.8885 -0.1633 0.0489  0.1634  707 SER A C     
5791 O  O     . SER A 707 ? 1.3656 1.1403 1.9705 -0.1719 0.0425  0.1587  707 SER A O     
5792 C  CB    . SER A 707 ? 1.2940 1.0377 1.9471 -0.1632 0.0630  0.2045  707 SER A CB    
5793 O  OG    . SER A 707 ? 1.1943 0.9460 1.8558 -0.1554 0.0758  0.2332  707 SER A OG    
5794 N  N     . GLY A 708 ? 1.2733 1.0083 1.8550 -0.1578 0.0447  0.1424  708 GLY A N     
5795 C  CA    . GLY A 708 ? 1.1841 0.9081 1.7435 -0.1604 0.0330  0.1119  708 GLY A CA    
5796 C  C     . GLY A 708 ? 1.1230 0.8635 1.6394 -0.1482 0.0357  0.1021  708 GLY A C     
5797 O  O     . GLY A 708 ? 1.1336 0.8868 1.6353 -0.1367 0.0456  0.1154  708 GLY A O     
5798 N  N     . ARG A 709 ? 1.0386 0.7784 1.5347 -0.1513 0.0258  0.0787  709 ARG A N     
5799 C  CA    . ARG A 709 ? 1.0603 0.8151 1.5171 -0.1410 0.0272  0.0683  709 ARG A CA    
5800 C  C     . ARG A 709 ? 1.0214 0.8118 1.4714 -0.1380 0.0337  0.0863  709 ARG A C     
5801 O  O     . ARG A 709 ? 1.1504 0.9557 1.6233 -0.1459 0.0346  0.1012  709 ARG A O     
5802 C  CB    . ARG A 709 ? 0.9947 0.7415 1.4330 -0.1457 0.0149  0.0408  709 ARG A CB    
5803 C  CG    . ARG A 709 ? 1.0533 0.7629 1.4896 -0.1467 0.0089  0.0196  709 ARG A CG    
5804 C  CD    . ARG A 709 ? 1.0421 0.7452 1.4550 -0.1507 -0.0033 -0.0069 709 ARG A CD    
5805 N  NE    . ARG A 709 ? 1.0509 0.7636 1.4817 -0.1656 -0.0151 -0.0076 709 ARG A NE    
5806 C  CZ    . ARG A 709 ? 1.1121 0.8224 1.5275 -0.1717 -0.0282 -0.0277 709 ARG A CZ    
5807 N  NH1   . ARG A 709 ? 1.0814 0.7796 1.4612 -0.1640 -0.0304 -0.0492 709 ARG A NH1   
5808 N  NH2   . ARG A 709 ? 1.0775 0.7988 1.5146 -0.1857 -0.0392 -0.0249 709 ARG A NH2   
5809 N  N     . ILE A 710 ? 1.0532 0.8564 1.4715 -0.1262 0.0386  0.0850  710 ILE A N     
5810 C  CA    . ILE A 710 ? 1.0222 0.8561 1.4280 -0.1222 0.0444  0.0990  710 ILE A CA    
5811 C  C     . ILE A 710 ? 0.9914 0.8405 1.3954 -0.1297 0.0376  0.0902  710 ILE A C     
5812 O  O     . ILE A 710 ? 0.9617 0.8327 1.3747 -0.1321 0.0419  0.1053  710 ILE A O     
5813 C  CB    . ILE A 710 ? 0.9929 0.8340 1.3651 -0.1090 0.0488  0.0972  710 ILE A CB    
5814 C  CG1   . ILE A 710 ? 0.9486 0.7783 1.3264 -0.1016 0.0556  0.1101  710 ILE A CG1   
5815 C  CG2   . ILE A 710 ? 0.7354 0.6051 1.0904 -0.1050 0.0534  0.1081  710 ILE A CG2   
5816 C  CD1   . ILE A 710 ? 0.7494 0.5816 1.1553 -0.1050 0.0622  0.1349  710 ILE A CD1   
5817 N  N     . GLY A 711 ? 1.1323 0.9702 1.5248 -0.1330 0.0272  0.0665  711 GLY A N     
5818 C  CA    . GLY A 711 ? 1.2451 1.0965 1.6358 -0.1401 0.0189  0.0573  711 GLY A CA    
5819 C  C     . GLY A 711 ? 1.1892 1.0426 1.6164 -0.1539 0.0134  0.0645  711 GLY A C     
5820 O  O     . GLY A 711 ? 1.2004 1.0667 1.6304 -0.1605 0.0057  0.0587  711 GLY A O     
5821 N  N     . ASP A 712 ? 1.0356 0.8771 1.4931 -0.1588 0.0167  0.0779  712 ASP A N     
5822 C  CA    . ASP A 712 ? 1.0338 0.8783 1.5310 -0.1726 0.0121  0.0881  712 ASP A CA    
5823 C  C     . ASP A 712 ? 0.9920 0.8608 1.5095 -0.1713 0.0250  0.1175  712 ASP A C     
5824 O  O     . ASP A 712 ? 1.0062 0.8860 1.5564 -0.1817 0.0228  0.1287  712 ASP A O     
5825 C  CB    . ASP A 712 ? 0.9599 0.7722 1.4817 -0.1808 0.0057  0.0829  712 ASP A CB    
5826 C  CG    . ASP A 712 ? 1.0000 0.7862 1.5037 -0.1838 -0.0081 0.0529  712 ASP A CG    
5827 O  OD1   . ASP A 712 ? 0.9431 0.7392 1.4228 -0.1831 -0.0151 0.0378  712 ASP A OD1   
5828 O  OD2   . ASP A 712 ? 0.8923 0.6474 1.4047 -0.1864 -0.0115 0.0446  712 ASP A OD2   
5829 N  N     . ARG A 713 ? 0.8919 0.7695 1.3908 -0.1588 0.0382  0.1307  713 ARG A N     
5830 C  CA    . ARG A 713 ? 0.8281 0.7285 1.3384 -0.1555 0.0517  0.1582  713 ARG A CA    
5831 C  C     . ARG A 713 ? 0.8445 0.7680 1.3200 -0.1442 0.0592  0.1603  713 ARG A C     
5832 O  O     . ARG A 713 ? 0.9870 0.9271 1.4610 -0.1381 0.0719  0.1815  713 ARG A O     
5833 C  CB    . ARG A 713 ? 0.9200 0.8092 1.4418 -0.1515 0.0610  0.1764  713 ARG A CB    
5834 C  CG    . ARG A 713 ? 0.9930 0.8547 1.5016 -0.1470 0.0568  0.1621  713 ARG A CG    
5835 C  CD    . ARG A 713 ? 1.0466 0.9001 1.5683 -0.1423 0.0664  0.1830  713 ARG A CD    
5836 N  NE    . ARG A 713 ? 1.2295 1.0590 1.7384 -0.1360 0.0641  0.1711  713 ARG A NE    
5837 C  CZ    . ARG A 713 ? 1.1643 0.9931 1.6617 -0.1253 0.0720  0.1836  713 ARG A CZ    
5838 N  NH1   . ARG A 713 ? 1.0828 0.9319 1.5760 -0.1198 0.0821  0.2074  713 ARG A NH1   
5839 N  NH2   . ARG A 713 ? 1.1917 0.9988 1.6812 -0.1197 0.0697  0.1723  713 ARG A NH2   
5840 N  N     . ALA A 714 ? 0.9733 0.8974 1.4200 -0.1410 0.0518  0.1390  714 ALA A N     
5841 C  CA    . ALA A 714 ? 0.9209 0.8649 1.3354 -0.1312 0.0574  0.1389  714 ALA A CA    
5842 C  C     . ALA A 714 ? 0.9042 0.8685 1.3293 -0.1365 0.0553  0.1390  714 ALA A C     
5843 O  O     . ALA A 714 ? 0.9551 0.9150 1.3900 -0.1451 0.0430  0.1238  714 ALA A O     
5844 C  CB    . ALA A 714 ? 0.8586 0.7926 1.2375 -0.1241 0.0513  0.1176  714 ALA A CB    
5845 N  N     . ILE A 715 ? 0.8923 0.8786 1.3150 -0.1308 0.0674  0.1565  715 ILE A N     
5846 C  CA    . ILE A 715 ? 0.9646 0.9726 1.3976 -0.1335 0.0682  0.1594  715 ILE A CA    
5847 C  C     . ILE A 715 ? 0.9109 0.9324 1.3057 -0.1212 0.0751  0.1566  715 ILE A C     
5848 O  O     . ILE A 715 ? 1.0207 1.0385 1.3881 -0.1113 0.0821  0.1605  715 ILE A O     
5849 C  CB    . ILE A 715 ? 0.7853 0.8076 1.2558 -0.1382 0.0783  0.1846  715 ILE A CB    
5850 C  CG1   . ILE A 715 ? 0.9029 0.9283 1.3624 -0.1284 0.0946  0.2055  715 ILE A CG1   
5851 C  CG2   . ILE A 715 ? 0.8388 0.8481 1.3514 -0.1528 0.0685  0.1853  715 ILE A CG2   
5852 C  CD1   . ILE A 715 ? 0.8994 0.9493 1.3666 -0.1234 0.1104  0.2274  715 ILE A CD1   
5853 N  N     . PRO A 716 ? 0.9544 0.9910 1.3464 -0.1214 0.0725  0.1501  716 PRO A N     
5854 C  CA    . PRO A 716 ? 0.8377 0.8863 1.1955 -0.1094 0.0801  0.1490  716 PRO A CA    
5855 C  C     . PRO A 716 ? 0.9109 0.9715 1.2658 -0.1013 0.0978  0.1716  716 PRO A C     
5856 O  O     . PRO A 716 ? 0.9581 1.0254 1.3442 -0.1056 0.1052  0.1901  716 PRO A O     
5857 C  CB    . PRO A 716 ? 0.8924 0.9557 1.2593 -0.1129 0.0743  0.1413  716 PRO A CB    
5858 C  CG    . PRO A 716 ? 0.8622 0.9166 1.2586 -0.1268 0.0593  0.1321  716 PRO A CG    
5859 C  CD    . PRO A 716 ? 0.8459 0.8890 1.2670 -0.1326 0.0619  0.1443  716 PRO A CD    
5860 N  N     . PHE A 717 ? 0.8624 0.9250 1.1787 -0.0894 0.1046  0.1703  717 PHE A N     
5861 C  CA    . PHE A 717 ? 0.8602 0.9304 1.1657 -0.0805 0.1210  0.1904  717 PHE A CA    
5862 C  C     . PHE A 717 ? 1.0447 1.1359 1.3669 -0.0785 0.1333  0.2043  717 PHE A C     
5863 O  O     . PHE A 717 ? 0.8706 0.9698 1.2051 -0.0759 0.1473  0.2259  717 PHE A O     
5864 C  CB    . PHE A 717 ? 0.7636 0.8282 1.0215 -0.0690 0.1231  0.1843  717 PHE A CB    
5865 C  CG    . PHE A 717 ? 0.8381 0.9062 1.0797 -0.0601 0.1378  0.2038  717 PHE A CG    
5866 C  CD1   . PHE A 717 ? 0.7497 0.8131 1.0087 -0.0627 0.1424  0.2206  717 PHE A CD1   
5867 C  CD2   . PHE A 717 ? 0.8633 0.9384 1.0716 -0.0489 0.1474  0.2057  717 PHE A CD2   
5868 C  CE1   . PHE A 717 ? 0.8426 0.9096 1.0849 -0.0543 0.1559  0.2396  717 PHE A CE1   
5869 C  CE2   . PHE A 717 ? 0.9020 0.9790 1.0913 -0.0404 0.1608  0.2232  717 PHE A CE2   
5870 C  CZ    . PHE A 717 ? 0.8745 0.9482 1.0805 -0.0430 0.1651  0.2407  717 PHE A CZ    
5871 N  N     . ASP A 718 ? 1.0887 1.1899 1.4126 -0.0790 0.1292  0.1937  718 ASP A N     
5872 C  CA    . ASP A 718 ? 1.0334 1.1557 1.3786 -0.0771 0.1408  0.2074  718 ASP A CA    
5873 C  C     . ASP A 718 ? 1.0416 1.1722 1.4385 -0.0881 0.1420  0.2237  718 ASP A C     
5874 O  O     . ASP A 718 ? 1.0924 1.2421 1.5124 -0.0862 0.1546  0.2408  718 ASP A O     
5875 C  CB    . ASP A 718 ? 1.0393 1.1702 1.3805 -0.0766 0.1338  0.1926  718 ASP A CB    
5876 C  CG    . ASP A 718 ? 1.2037 1.3302 1.5690 -0.0900 0.1143  0.1778  718 ASP A CG    
5877 O  OD1   . ASP A 718 ? 1.2528 1.3837 1.6105 -0.0897 0.1063  0.1641  718 ASP A OD1   
5878 O  OD2   . ASP A 718 ? 1.1447 1.2621 1.5348 -0.1005 0.1065  0.1793  718 ASP A OD2   
5879 N  N     . GLU A 719 ? 1.0892 1.2055 1.5055 -0.0992 0.1297  0.2191  719 GLU A N     
5880 C  CA    . GLU A 719 ? 0.8699 0.9897 1.3360 -0.1114 0.1280  0.2330  719 GLU A CA    
5881 C  C     . GLU A 719 ? 0.8733 0.9872 1.3467 -0.1099 0.1391  0.2527  719 GLU A C     
5882 O  O     . GLU A 719 ? 0.9335 1.0495 1.4499 -0.1198 0.1392  0.2669  719 GLU A O     
5883 C  CB    . GLU A 719 ? 0.8521 0.9567 1.3348 -0.1251 0.1064  0.2140  719 GLU A CB    
5884 C  CG    . GLU A 719 ? 1.1133 1.2289 1.6445 -0.1386 0.0980  0.2185  719 GLU A CG    
5885 C  CD    . GLU A 719 ? 1.1391 1.2440 1.6691 -0.1479 0.0761  0.1937  719 GLU A CD    
5886 O  OE1   . GLU A 719 ? 1.1150 1.2033 1.6652 -0.1599 0.0628  0.1870  719 GLU A OE1   
5887 O  OE2   . GLU A 719 ? 1.0467 1.1586 1.5540 -0.1428 0.0723  0.1807  719 GLU A OE2   
5888 N  N     . PHE A 720 ? 1.0071 1.1136 1.4406 -0.0983 0.1475  0.2546  720 PHE A N     
5889 C  CA    . PHE A 720 ? 1.0055 1.1055 1.4412 -0.0960 0.1569  0.2731  720 PHE A CA    
5890 C  C     . PHE A 720 ? 0.9625 1.0820 1.4054 -0.0883 0.1784  0.2995  720 PHE A C     
5891 O  O     . PHE A 720 ? 1.1273 1.2566 1.5390 -0.0763 0.1892  0.3001  720 PHE A O     
5892 C  CB    . PHE A 720 ? 0.8074 0.8913 1.1970 -0.0872 0.1546  0.2637  720 PHE A CB    
5893 C  CG    . PHE A 720 ? 0.7790 0.8556 1.1687 -0.0845 0.1627  0.2828  720 PHE A CG    
5894 C  CD1   . PHE A 720 ? 0.9103 0.9965 1.2789 -0.0732 0.1799  0.3022  720 PHE A CD1   
5895 C  CD2   . PHE A 720 ? 0.9572 1.0165 1.3669 -0.0926 0.1533  0.2814  720 PHE A CD2   
5896 C  CE1   . PHE A 720 ? 0.9524 1.0326 1.3202 -0.0705 0.1869  0.3209  720 PHE A CE1   
5897 C  CE2   . PHE A 720 ? 0.9600 1.0131 1.3715 -0.0897 0.1606  0.3001  720 PHE A CE2   
5898 C  CZ    . PHE A 720 ? 0.8881 0.9523 1.2787 -0.0789 0.1771  0.3204  720 PHE A CZ    
5899 N  N     . ASP A 721 ? 0.9616 1.0858 1.4452 -0.0948 0.1851  0.3213  721 ASP A N     
5900 C  CA    . ASP A 721 ? 1.0263 1.1685 1.5193 -0.0873 0.2074  0.3498  721 ASP A CA    
5901 C  C     . ASP A 721 ? 1.1216 1.2536 1.6117 -0.0852 0.2143  0.3675  721 ASP A C     
5902 O  O     . ASP A 721 ? 1.1493 1.2722 1.6764 -0.0967 0.2070  0.3733  721 ASP A O     
5903 C  CB    . ASP A 721 ? 1.0544 1.2154 1.6046 -0.0969 0.2108  0.3645  721 ASP A CB    
5904 C  CG    . ASP A 721 ? 0.9551 1.1348 1.5219 -0.0898 0.2351  0.3972  721 ASP A CG    
5905 O  OD1   . ASP A 721 ? 0.9781 1.1595 1.5036 -0.0747 0.2511  0.4055  721 ASP A OD1   
5906 O  OD2   . ASP A 721 ? 1.1831 1.3761 1.8042 -0.0993 0.2383  0.4149  721 ASP A OD2   
5907 N  N     . PRO A 722 ? 1.1160 1.2482 1.5631 -0.0709 0.2276  0.3765  722 PRO A N     
5908 C  CA    . PRO A 722 ? 1.1156 1.2370 1.5556 -0.0685 0.2319  0.3922  722 PRO A CA    
5909 C  C     . PRO A 722 ? 1.1471 1.2768 1.6361 -0.0747 0.2429  0.4214  722 PRO A C     
5910 O  O     . PRO A 722 ? 1.2542 1.3711 1.7561 -0.0790 0.2395  0.4306  722 PRO A O     
5911 C  CB    . PRO A 722 ? 1.2774 1.4015 1.6604 -0.0515 0.2450  0.3971  722 PRO A CB    
5912 C  CG    . PRO A 722 ? 1.1949 1.3350 1.5674 -0.0448 0.2541  0.3921  722 PRO A CG    
5913 C  CD    . PRO A 722 ? 1.0374 1.1772 1.4374 -0.0564 0.2374  0.3708  722 PRO A CD    
5914 N  N     . THR A 723 ? 1.1607 1.3118 1.6798 -0.0751 0.2563  0.4375  723 THR A N     
5915 C  CA    . THR A 723 ? 1.1353 1.2957 1.7059 -0.0817 0.2669  0.4670  723 THR A CA    
5916 C  C     . THR A 723 ? 1.1072 1.2557 1.7293 -0.1005 0.2483  0.4604  723 THR A C     
5917 O  O     . THR A 723 ? 1.1058 1.2502 1.7621 -0.1068 0.2509  0.4797  723 THR A O     
5918 C  CB    . THR A 723 ? 1.0064 1.1941 1.6008 -0.0778 0.2856  0.4859  723 THR A CB    
5919 O  OG1   . THR A 723 ? 1.0260 1.2208 1.6191 -0.0796 0.2769  0.4643  723 THR A OG1   
5920 C  CG2   . THR A 723 ? 0.9099 1.1068 1.4599 -0.0581 0.3083  0.5016  723 THR A CG2   
5921 N  N     . LYS A 724 ? 1.1085 1.2501 1.7349 -0.1092 0.2290  0.4327  724 LYS A N     
5922 C  CA    . LYS A 724 ? 1.0769 1.2063 1.7497 -0.1273 0.2104  0.4239  724 LYS A CA    
5923 C  C     . LYS A 724 ? 1.1015 1.2020 1.7528 -0.1310 0.1916  0.3991  724 LYS A C     
5924 O  O     . LYS A 724 ? 1.0950 1.1802 1.7809 -0.1449 0.1772  0.3924  724 LYS A O     
5925 C  CB    . LYS A 724 ? 1.0173 1.1595 1.7164 -0.1361 0.2007  0.4117  724 LYS A CB    
5926 C  CG    . LYS A 724 ? 0.9554 1.1284 1.6806 -0.1325 0.2185  0.4349  724 LYS A CG    
5927 C  CD    . LYS A 724 ? 1.0167 1.1984 1.7577 -0.1261 0.2360  0.4649  724 LYS A CD    
5928 C  CE    . LYS A 724 ? 1.0853 1.2920 1.8616 -0.1245 0.2429  0.4792  724 LYS A CE    
5929 N  NZ    . LYS A 724 ? 1.0470 1.2540 1.8699 -0.1418 0.2218  0.4677  724 LYS A NZ    
5930 N  N     . HIS A 725 ? 1.1722 1.2644 1.7686 -0.1190 0.1914  0.3855  725 HIS A N     
5931 C  CA    . HIS A 725 ? 1.1214 1.1883 1.6971 -0.1210 0.1751  0.3627  725 HIS A CA    
5932 C  C     . HIS A 725 ? 0.8956 0.9537 1.4361 -0.1096 0.1824  0.3717  725 HIS A C     
5933 O  O     . HIS A 725 ? 0.9397 1.0109 1.4540 -0.0977 0.1979  0.3875  725 HIS A O     
5934 C  CB    . HIS A 725 ? 1.0302 1.0943 1.5745 -0.1194 0.1622  0.3319  725 HIS A CB    
5935 C  CG    . HIS A 725 ? 1.1287 1.2030 1.7020 -0.1294 0.1540  0.3224  725 HIS A CG    
5936 N  ND1   . HIS A 725 ? 1.1266 1.2189 1.6835 -0.1238 0.1577  0.3164  725 HIS A ND1   
5937 C  CD2   . HIS A 725 ? 1.1243 1.1929 1.7422 -0.1450 0.1414  0.3182  725 HIS A CD2   
5938 C  CE1   . HIS A 725 ? 1.1497 1.2488 1.7409 -0.1352 0.1477  0.3100  725 HIS A CE1   
5939 N  NE2   . HIS A 725 ? 1.1759 1.2606 1.8036 -0.1486 0.1370  0.3106  725 HIS A NE2   
5940 N  N     . ARG A 726 ? 0.9986 1.0339 1.5385 -0.1130 0.1708  0.3613  726 ARG A N     
5941 C  CA    . ARG A 726 ? 1.0015 1.0264 1.5098 -0.1033 0.1736  0.3669  726 ARG A CA    
5942 C  C     . ARG A 726 ? 0.9634 0.9697 1.4475 -0.1031 0.1574  0.3383  726 ARG A C     
5943 O  O     . ARG A 726 ? 0.9745 0.9644 1.4831 -0.1130 0.1450  0.3237  726 ARG A O     
5944 C  CB    . ARG A 726 ? 0.8048 0.8211 1.3464 -0.1071 0.1787  0.3906  726 ARG A CB    
5945 C  CG    . ARG A 726 ? 1.0803 1.1018 1.5957 -0.0949 0.1920  0.4140  726 ARG A CG    
5946 C  CD    . ARG A 726 ? 1.1869 1.2166 1.7398 -0.0976 0.2061  0.4470  726 ARG A CD    
5947 N  NE    . ARG A 726 ? 1.3144 1.3559 1.8361 -0.0844 0.2219  0.4707  726 ARG A NE    
5948 C  CZ    . ARG A 726 ? 1.3753 1.4367 1.8716 -0.0755 0.2355  0.4788  726 ARG A CZ    
5949 N  NH1   . ARG A 726 ? 1.1578 1.2315 1.6592 -0.0780 0.2362  0.4669  726 ARG A NH1   
5950 N  NH2   . ARG A 726 ? 1.4130 1.4815 1.8773 -0.0632 0.2489  0.4997  726 ARG A NH2   
5951 N  N     . TYR A 727 ? 0.8718 0.8799 1.3081 -0.0919 0.1574  0.3300  727 TYR A N     
5952 C  CA    . TYR A 727 ? 0.9323 0.9251 1.3467 -0.0911 0.1432  0.3042  727 TYR A CA    
5953 C  C     . TYR A 727 ? 0.9926 0.9655 1.4168 -0.0916 0.1385  0.3078  727 TYR A C     
5954 O  O     . TYR A 727 ? 0.8869 0.8595 1.3215 -0.0891 0.1468  0.3314  727 TYR A O     
5955 C  CB    . TYR A 727 ? 0.8026 0.8031 1.1662 -0.0799 0.1436  0.2949  727 TYR A CB    
5956 C  CG    . TYR A 727 ? 0.9333 0.9401 1.2675 -0.0688 0.1537  0.3146  727 TYR A CG    
5957 C  CD1   . TYR A 727 ? 1.0158 1.0111 1.3433 -0.0652 0.1512  0.3230  727 TYR A CD1   
5958 C  CD2   . TYR A 727 ? 0.9010 0.9248 1.2121 -0.0614 0.1656  0.3244  727 TYR A CD2   
5959 C  CE1   . TYR A 727 ? 0.9515 0.9527 1.2500 -0.0554 0.1586  0.3410  727 TYR A CE1   
5960 C  CE2   . TYR A 727 ? 1.0280 1.0559 1.3075 -0.0511 0.1741  0.3412  727 TYR A CE2   
5961 C  CZ    . TYR A 727 ? 1.0080 1.0248 1.2808 -0.0485 0.1698  0.3495  727 TYR A CZ    
5962 O  OH    . TYR A 727 ? 0.9556 0.9766 1.1951 -0.0386 0.1766  0.3664  727 TYR A OH    
5963 N  N     . ASP A 728 ? 0.8993 0.8554 1.3204 -0.0941 0.1257  0.2848  728 ASP A N     
5964 C  CA    . ASP A 728 ? 0.9675 0.9027 1.4006 -0.0943 0.1211  0.2853  728 ASP A CA    
5965 C  C     . ASP A 728 ? 0.9866 0.9234 1.3858 -0.0825 0.1231  0.2928  728 ASP A C     
5966 O  O     . ASP A 728 ? 0.8628 0.7960 1.2344 -0.0775 0.1158  0.2758  728 ASP A O     
5967 C  CB    . ASP A 728 ? 0.8998 0.8162 1.3394 -0.1001 0.1082  0.2578  728 ASP A CB    
5968 C  CG    . ASP A 728 ? 1.0040 0.8963 1.4683 -0.1025 0.1052  0.2593  728 ASP A CG    
5969 O  OD1   . ASP A 728 ? 1.0192 0.9055 1.4704 -0.0942 0.1065  0.2656  728 ASP A OD1   
5970 O  OD2   . ASP A 728 ? 0.9919 0.8708 1.4896 -0.1129 0.1010  0.2545  728 ASP A OD2   
5971 N  N     . ALA A 729 ? 1.0015 0.9444 1.4034 -0.0782 0.1328  0.3197  729 ALA A N     
5972 C  CA    . ALA A 729 ? 0.9207 0.8653 1.2919 -0.0677 0.1334  0.3294  729 ALA A CA    
5973 C  C     . ALA A 729 ? 0.9453 0.8710 1.3219 -0.0663 0.1243  0.3201  729 ALA A C     
5974 O  O     . ALA A 729 ? 1.0390 0.9651 1.3863 -0.0590 0.1189  0.3141  729 ALA A O     
5975 C  CB    . ALA A 729 ? 0.9341 0.8870 1.3106 -0.0640 0.1452  0.3615  729 ALA A CB    
5976 N  N     . GLU A 730 ? 1.0285 0.9368 1.4432 -0.0732 0.1226  0.3188  730 GLU A N     
5977 C  CA    . GLU A 730 ? 1.0588 0.9475 1.4811 -0.0710 0.1159  0.3102  730 GLU A CA    
5978 C  C     . GLU A 730 ? 1.0173 0.9019 1.4167 -0.0691 0.1065  0.2814  730 GLU A C     
5979 O  O     . GLU A 730 ? 0.9275 0.8062 1.3140 -0.0622 0.1023  0.2771  730 GLU A O     
5980 C  CB    . GLU A 730 ? 0.9897 0.8578 1.4565 -0.0793 0.1160  0.3113  730 GLU A CB    
5981 C  CG    . GLU A 730 ? 1.2257 1.0768 1.7095 -0.0746 0.1166  0.3229  730 GLU A CG    
5982 C  CD    . GLU A 730 ? 1.3415 1.2058 1.8122 -0.0660 0.1225  0.3510  730 GLU A CD    
5983 O  OE1   . GLU A 730 ? 1.1779 1.0585 1.6461 -0.0666 0.1302  0.3704  730 GLU A OE1   
5984 O  OE2   . GLU A 730 ? 1.2013 1.0599 1.6642 -0.0581 0.1196  0.3542  730 GLU A OE2   
5985 N  N     . TYR A 731 ? 0.9731 0.8616 1.3690 -0.0751 0.1034  0.2628  731 TYR A N     
5986 C  CA    . TYR A 731 ? 0.8600 0.7454 1.2342 -0.0735 0.0950  0.2364  731 TYR A CA    
5987 C  C     . TYR A 731 ? 0.9353 0.8349 1.2709 -0.0642 0.0938  0.2371  731 TYR A C     
5988 O  O     . TYR A 731 ? 0.9703 0.8639 1.2930 -0.0587 0.0884  0.2275  731 TYR A O     
5989 C  CB    . TYR A 731 ? 0.8162 0.7059 1.1934 -0.0816 0.0918  0.2194  731 TYR A CB    
5990 C  CG    . TYR A 731 ? 0.8103 0.6997 1.1619 -0.0794 0.0840  0.1941  731 TYR A CG    
5991 C  CD1   . TYR A 731 ? 0.8567 0.7268 1.2124 -0.0796 0.0778  0.1756  731 TYR A CD1   
5992 C  CD2   . TYR A 731 ? 0.8615 0.7692 1.1844 -0.0763 0.0838  0.1893  731 TYR A CD2   
5993 C  CE1   . TYR A 731 ? 0.9349 0.8056 1.2673 -0.0770 0.0717  0.1541  731 TYR A CE1   
5994 C  CE2   . TYR A 731 ? 0.8652 0.7730 1.1664 -0.0742 0.0769  0.1677  731 TYR A CE2   
5995 C  CZ    . TYR A 731 ? 0.8467 0.7368 1.1530 -0.0747 0.0710  0.1508  731 TYR A CZ    
5996 O  OH    . TYR A 731 ? 0.9266 0.8174 1.2114 -0.0722 0.0651  0.1308  731 TYR A OH    
5997 N  N     . TYR A 732 ? 0.9826 0.9007 1.2998 -0.0621 0.0988  0.2487  732 TYR A N     
5998 C  CA    . TYR A 732 ? 0.9460 0.8760 1.2242 -0.0542 0.0964  0.2475  732 TYR A CA    
5999 C  C     . TYR A 732 ? 0.9285 0.8568 1.1979 -0.0469 0.0954  0.2638  732 TYR A C     
6000 O  O     . TYR A 732 ? 0.9723 0.9057 1.2134 -0.0411 0.0896  0.2594  732 TYR A O     
6001 C  CB    . TYR A 732 ? 1.0233 0.9709 1.2829 -0.0534 0.1030  0.2548  732 TYR A CB    
6002 C  CG    . TYR A 732 ? 0.9465 0.8989 1.2101 -0.0593 0.1024  0.2379  732 TYR A CG    
6003 C  CD1   . TYR A 732 ? 0.8170 0.7728 1.0563 -0.0575 0.0958  0.2174  732 TYR A CD1   
6004 C  CD2   . TYR A 732 ? 0.8930 0.8474 1.1868 -0.0668 0.1080  0.2436  732 TYR A CD2   
6005 C  CE1   . TYR A 732 ? 0.8791 0.8400 1.1226 -0.0625 0.0948  0.2032  732 TYR A CE1   
6006 C  CE2   . TYR A 732 ? 0.8763 0.8365 1.1756 -0.0724 0.1062  0.2293  732 TYR A CE2   
6007 C  CZ    . TYR A 732 ? 0.9284 0.8919 1.2018 -0.0700 0.0997  0.2092  732 TYR A CZ    
6008 O  OH    . TYR A 732 ? 0.8611 0.8312 1.1404 -0.0752 0.0975  0.1961  732 TYR A OH    
6009 N  N     . ILE A 733 ? 0.9834 0.9051 1.2779 -0.0474 0.1003  0.2831  733 ILE A N     
6010 C  CA    . ILE A 733 ? 0.9669 0.8863 1.2574 -0.0405 0.0983  0.2992  733 ILE A CA    
6011 C  C     . ILE A 733 ? 0.8863 0.7917 1.1875 -0.0386 0.0912  0.2857  733 ILE A C     
6012 O  O     . ILE A 733 ? 0.9780 0.8869 1.2601 -0.0325 0.0847  0.2840  733 ILE A O     
6013 C  CB    . ILE A 733 ? 0.9990 0.9159 1.3146 -0.0412 0.1065  0.3259  733 ILE A CB    
6014 C  CG1   . ILE A 733 ? 1.0310 0.9642 1.3297 -0.0403 0.1149  0.3432  733 ILE A CG1   
6015 C  CG2   . ILE A 733 ? 0.9817 0.8932 1.3011 -0.0347 0.1033  0.3413  733 ILE A CG2   
6016 C  CD1   . ILE A 733 ? 0.8751 0.8102 1.1832 -0.0370 0.1216  0.3739  733 ILE A CD1   
6017 N  N     . GLU A 734 ? 0.8475 0.7363 1.1794 -0.0436 0.0923  0.2758  734 GLU A N     
6018 C  CA    . GLU A 734 ? 0.9915 0.8639 1.3372 -0.0406 0.0885  0.2658  734 GLU A CA    
6019 C  C     . GLU A 734 ? 1.0182 0.8879 1.3491 -0.0405 0.0826  0.2382  734 GLU A C     
6020 O  O     . GLU A 734 ? 1.0105 0.8702 1.3457 -0.0356 0.0799  0.2305  734 GLU A O     
6021 C  CB    . GLU A 734 ? 0.9125 0.7644 1.2971 -0.0453 0.0928  0.2682  734 GLU A CB    
6022 C  CG    . GLU A 734 ? 1.0026 0.8551 1.4072 -0.0452 0.0992  0.2971  734 GLU A CG    
6023 C  CD    . GLU A 734 ? 1.1529 1.0052 1.5581 -0.0361 0.0984  0.3147  734 GLU A CD    
6024 O  OE1   . GLU A 734 ? 1.2026 1.0452 1.6100 -0.0311 0.0946  0.3038  734 GLU A OE1   
6025 O  OE2   . GLU A 734 ? 1.1152 0.9776 1.5191 -0.0336 0.1018  0.3403  734 GLU A OE2   
6026 N  N     . LYS A 735 ? 0.9984 0.8771 1.3131 -0.0452 0.0811  0.2243  735 LYS A N     
6027 C  CA    . LYS A 735 ? 0.8838 0.7598 1.1854 -0.0456 0.0758  0.1988  735 LYS A CA    
6028 C  C     . LYS A 735 ? 0.8269 0.7211 1.0946 -0.0430 0.0719  0.1930  735 LYS A C     
6029 O  O     . LYS A 735 ? 0.8234 0.7171 1.0788 -0.0427 0.0674  0.1735  735 LYS A O     
6030 C  CB    . LYS A 735 ? 0.7698 0.6360 1.0867 -0.0544 0.0759  0.1829  735 LYS A CB    
6031 C  CG    . LYS A 735 ? 0.8992 0.7442 1.2501 -0.0583 0.0787  0.1859  735 LYS A CG    
6032 C  CD    . LYS A 735 ? 1.0640 0.8885 1.4193 -0.0563 0.0757  0.1654  735 LYS A CD    
6033 C  CE    . LYS A 735 ? 0.8924 0.6990 1.2703 -0.0513 0.0795  0.1757  735 LYS A CE    
6034 N  NZ    . LYS A 735 ? 0.9974 0.7843 1.3759 -0.0468 0.0785  0.1562  735 LYS A NZ    
6035 N  N     . GLN A 736 ? 0.8408 0.7496 1.0917 -0.0410 0.0735  0.2092  736 GLN A N     
6036 C  CA    . GLN A 736 ? 0.9769 0.9002 1.1945 -0.0386 0.0696  0.2028  736 GLN A CA    
6037 C  C     . GLN A 736 ? 0.9266 0.8583 1.1237 -0.0321 0.0664  0.2185  736 GLN A C     
6038 O  O     . GLN A 736 ? 0.9283 0.8633 1.1079 -0.0283 0.0591  0.2115  736 GLN A O     
6039 C  CB    . GLN A 736 ? 0.8919 0.8251 1.1023 -0.0430 0.0745  0.2023  736 GLN A CB    
6040 C  CG    . GLN A 736 ? 0.7111 0.6406 0.9315 -0.0493 0.0735  0.1822  736 GLN A CG    
6041 C  CD    . GLN A 736 ? 0.8022 0.7407 0.9957 -0.0479 0.0688  0.1659  736 GLN A CD    
6042 O  OE1   . GLN A 736 ? 0.7921 0.7417 0.9598 -0.0439 0.0688  0.1711  736 GLN A OE1   
6043 N  NE2   . GLN A 736 ? 0.7304 0.6630 0.9287 -0.0510 0.0646  0.1461  736 GLN A NE2   
6044 N  N     . VAL A 737 ? 0.9492 0.8844 1.1484 -0.0309 0.0712  0.2404  737 VAL A N     
6045 C  CA    . VAL A 737 ? 0.9578 0.9011 1.1333 -0.0252 0.0671  0.2560  737 VAL A CA    
6046 C  C     . VAL A 737 ? 0.9549 0.8922 1.1443 -0.0211 0.0614  0.2637  737 VAL A C     
6047 O  O     . VAL A 737 ? 1.0354 0.9766 1.2095 -0.0175 0.0525  0.2597  737 VAL A O     
6048 C  CB    . VAL A 737 ? 0.8665 0.8161 1.0365 -0.0246 0.0750  0.2777  737 VAL A CB    
6049 C  CG1   . VAL A 737 ? 0.8434 0.7991 0.9893 -0.0185 0.0696  0.2951  737 VAL A CG1   
6050 C  CG2   . VAL A 737 ? 0.8738 0.8318 1.0263 -0.0268 0.0810  0.2709  737 VAL A CG2   
6051 N  N     . LEU A 738 ? 1.0416 0.9692 1.2626 -0.0214 0.0666  0.2755  738 LEU A N     
6052 C  CA    . LEU A 738 ? 0.9267 0.8486 1.1643 -0.0165 0.0627  0.2856  738 LEU A CA    
6053 C  C     . LEU A 738 ? 0.9732 0.8903 1.2149 -0.0143 0.0571  0.2673  738 LEU A C     
6054 O  O     . LEU A 738 ? 1.0383 0.9604 1.2752 -0.0093 0.0499  0.2738  738 LEU A O     
6055 C  CB    . LEU A 738 ? 0.8256 0.7350 1.0991 -0.0175 0.0705  0.2989  738 LEU A CB    
6056 C  CG    . LEU A 738 ? 0.8855 0.8004 1.1601 -0.0167 0.0752  0.3262  738 LEU A CG    
6057 C  CD1   . LEU A 738 ? 0.9583 0.8594 1.2717 -0.0160 0.0804  0.3400  738 LEU A CD1   
6058 C  CD2   . LEU A 738 ? 0.9666 0.8950 1.2119 -0.0111 0.0675  0.3409  738 LEU A CD2   
6059 N  N     . PRO A 739 ? 0.9731 0.8811 1.2239 -0.0177 0.0598  0.2456  739 PRO A N     
6060 C  CA    . PRO A 739 ? 0.9478 0.8524 1.1989 -0.0145 0.0555  0.2293  739 PRO A CA    
6061 C  C     . PRO A 739 ? 0.9495 0.8688 1.1712 -0.0126 0.0467  0.2249  739 PRO A C     
6062 O  O     . PRO A 739 ? 1.0504 0.9712 1.2745 -0.0081 0.0417  0.2224  739 PRO A O     
6063 C  CB    . PRO A 739 ? 0.8923 0.7860 1.1507 -0.0194 0.0597  0.2069  739 PRO A CB    
6064 C  CG    . PRO A 739 ? 0.9976 0.8836 1.2741 -0.0246 0.0663  0.2148  739 PRO A CG    
6065 C  CD    . PRO A 739 ? 0.9780 0.8777 1.2415 -0.0244 0.0666  0.2359  739 PRO A CD    
6066 N  N     . ALA A 740 ? 0.9640 0.8937 1.1590 -0.0156 0.0448  0.2245  740 ALA A N     
6067 C  CA    . ALA A 740 ? 0.9633 0.9043 1.1294 -0.0144 0.0360  0.2185  740 ALA A CA    
6068 C  C     . ALA A 740 ? 0.9804 0.9292 1.1364 -0.0104 0.0275  0.2370  740 ALA A C     
6069 O  O     . ALA A 740 ? 0.9673 0.9222 1.1119 -0.0087 0.0180  0.2331  740 ALA A O     
6070 C  CB    . ALA A 740 ? 0.8888 0.8361 1.0292 -0.0182 0.0377  0.2110  740 ALA A CB    
6071 N  N     . VAL A 741 ? 0.9619 0.9109 1.1221 -0.0092 0.0298  0.2578  741 VAL A N     
6072 C  CA    . VAL A 741 ? 0.9945 0.9512 1.1438 -0.0056 0.0204  0.2766  741 VAL A CA    
6073 C  C     . VAL A 741 ? 1.0345 0.9878 1.2154 -0.0013 0.0186  0.2888  741 VAL A C     
6074 O  O     . VAL A 741 ? 1.0501 1.0110 1.2264 0.0016  0.0079  0.3007  741 VAL A O     
6075 C  CB    . VAL A 741 ? 0.9813 0.9418 1.1134 -0.0056 0.0231  0.2951  741 VAL A CB    
6076 C  CG1   . VAL A 741 ? 0.9151 0.8819 1.0066 -0.0072 0.0206  0.2867  741 VAL A CG1   
6077 C  CG2   . VAL A 741 ? 0.9290 0.8817 1.0856 -0.0073 0.0366  0.3013  741 VAL A CG2   
6078 N  N     . GLU A 742 ? 1.1387 1.0800 1.3518 -0.0008 0.0284  0.2862  742 GLU A N     
6079 C  CA    . GLU A 742 ? 1.0429 0.9793 1.2873 0.0046  0.0285  0.2973  742 GLU A CA    
6080 C  C     . GLU A 742 ? 1.1419 1.0820 1.3903 0.0078  0.0222  0.2868  742 GLU A C     
6081 O  O     . GLU A 742 ? 1.2273 1.1724 1.4901 0.0128  0.0165  0.3008  742 GLU A O     
6082 C  CB    . GLU A 742 ? 1.1058 1.0253 1.3818 0.0045  0.0409  0.2944  742 GLU A CB    
6083 C  CG    . GLU A 742 ? 1.3356 1.2471 1.6456 0.0112  0.0432  0.3049  742 GLU A CG    
6084 C  CD    . GLU A 742 ? 1.2873 1.1867 1.6132 0.0137  0.0485  0.2841  742 GLU A CD    
6085 O  OE1   . GLU A 742 ? 1.2709 1.1641 1.5867 0.0090  0.0522  0.2626  742 GLU A OE1   
6086 O  OE2   . GLU A 742 ? 1.1370 1.0335 1.4850 0.0208  0.0493  0.2899  742 GLU A OE2   
6087 N  N     . ARG A 743 ? 1.0641 1.0030 1.3013 0.0052  0.0233  0.2636  743 ARG A N     
6088 C  CA    . ARG A 743 ? 1.0797 1.0228 1.3205 0.0083  0.0185  0.2539  743 ARG A CA    
6089 C  C     . ARG A 743 ? 0.9380 0.8968 1.1631 0.0088  0.0041  0.2648  743 ARG A C     
6090 O  O     . ARG A 743 ? 0.9785 0.9429 1.2158 0.0123  -0.0009 0.2655  743 ARG A O     
6091 C  CB    . ARG A 743 ? 1.0124 0.9522 1.2401 0.0048  0.0220  0.2282  743 ARG A CB    
6092 C  CG    . ARG A 743 ? 0.9002 0.8238 1.1426 0.0035  0.0340  0.2156  743 ARG A CG    
6093 C  CD    . ARG A 743 ? 0.9941 0.9143 1.2289 0.0022  0.0363  0.1913  743 ARG A CD    
6094 N  NE    . ARG A 743 ? 1.0040 0.9141 1.2365 -0.0032 0.0429  0.1780  743 ARG A NE    
6095 C  CZ    . ARG A 743 ? 1.0128 0.9287 1.2256 -0.0093 0.0413  0.1745  743 ARG A CZ    
6096 N  NH1   . ARG A 743 ? 1.1080 1.0378 1.2980 -0.0102 0.0342  0.1815  743 ARG A NH1   
6097 N  NH2   . ARG A 743 ? 1.0222 0.9295 1.2385 -0.0143 0.0469  0.1638  743 ARG A NH2   
6098 N  N     . ILE A 744 ? 0.9701 0.9355 1.1685 0.0054  -0.0028 0.2736  744 ILE A N     
6099 C  CA    . ILE A 744 ? 0.9792 0.9572 1.1599 0.0052  -0.0184 0.2850  744 ILE A CA    
6100 C  C     . ILE A 744 ? 1.0277 1.0093 1.2231 0.0088  -0.0231 0.3115  744 ILE A C     
6101 O  O     . ILE A 744 ? 1.1920 1.1817 1.4015 0.0116  -0.0329 0.3226  744 ILE A O     
6102 C  CB    . ILE A 744 ? 1.0236 1.0050 1.1623 0.0003  -0.0237 0.2786  744 ILE A CB    
6103 C  CG1   . ILE A 744 ? 0.8995 0.8789 1.0256 -0.0028 -0.0208 0.2537  744 ILE A CG1   
6104 C  CG2   . ILE A 744 ? 1.0230 1.0143 1.1403 -0.0003 -0.0412 0.2908  744 ILE A CG2   
6105 C  CD1   . ILE A 744 ? 1.0219 1.0026 1.1096 -0.0065 -0.0229 0.2463  744 ILE A CD1   
6106 N  N     . LEU A 745 ? 1.0500 1.0266 1.2447 0.0088  -0.0161 0.3233  745 LEU A N     
6107 C  CA    . LEU A 745 ? 0.9918 0.9722 1.1972 0.0122  -0.0206 0.3503  745 LEU A CA    
6108 C  C     . LEU A 745 ? 1.0357 1.0114 1.2861 0.0181  -0.0148 0.3602  745 LEU A C     
6109 O  O     . LEU A 745 ? 1.0310 1.0108 1.2952 0.0216  -0.0192 0.3840  745 LEU A O     
6110 C  CB    . LEU A 745 ? 0.9457 0.9221 1.1370 0.0107  -0.0132 0.3606  745 LEU A CB    
6111 C  CG    . LEU A 745 ? 1.0197 1.0003 1.1650 0.0066  -0.0170 0.3540  745 LEU A CG    
6112 C  CD1   . LEU A 745 ? 1.0088 0.9834 1.1487 0.0052  -0.0029 0.3569  745 LEU A CD1   
6113 C  CD2   . LEU A 745 ? 1.0473 1.0379 1.1651 0.0073  -0.0336 0.3701  745 LEU A CD2   
6114 N  N     . ARG A 746 ? 1.0370 1.0036 1.3094 0.0198  -0.0048 0.3431  746 ARG A N     
6115 C  CA    . ARG A 746 ? 0.8982 0.8587 1.2118 0.0267  0.0017  0.3514  746 ARG A CA    
6116 C  C     . ARG A 746 ? 1.0580 1.0326 1.3843 0.0310  -0.0107 0.3657  746 ARG A C     
6117 O  O     . ARG A 746 ? 1.0914 1.0655 1.4505 0.0376  -0.0085 0.3829  746 ARG A O     
6118 C  CB    . ARG A 746 ? 0.9093 0.8561 1.2378 0.0282  0.0144  0.3280  746 ARG A CB    
6119 C  CG    . ARG A 746 ? 1.0895 1.0432 1.4227 0.0311  0.0107  0.3170  746 ARG A CG    
6120 C  CD    . ARG A 746 ? 1.1174 1.0573 1.4560 0.0320  0.0231  0.2920  746 ARG A CD    
6121 N  NE    . ARG A 746 ? 1.1745 1.1039 1.4950 0.0255  0.0292  0.2771  746 ARG A NE    
6122 C  CZ    . ARG A 746 ? 1.2324 1.1467 1.5572 0.0250  0.0397  0.2570  746 ARG A CZ    
6123 N  NH1   . ARG A 746 ? 1.2165 1.1227 1.5594 0.0314  0.0467  0.2477  746 ARG A NH1   
6124 N  NH2   . ARG A 746 ? 1.2672 1.1743 1.5777 0.0182  0.0433  0.2463  746 ARG A NH2   
6125 N  N     . ALA A 747 ? 1.0807 1.0680 1.3835 0.0273  -0.0240 0.3595  747 ALA A N     
6126 C  CA    . ALA A 747 ? 1.0998 1.1023 1.4145 0.0297  -0.0383 0.3739  747 ALA A CA    
6127 C  C     . ALA A 747 ? 1.0953 1.1065 1.4082 0.0302  -0.0503 0.4018  747 ALA A C     
6128 O  O     . ALA A 747 ? 1.1528 1.1766 1.4839 0.0328  -0.0622 0.4185  747 ALA A O     
6129 C  CB    . ALA A 747 ? 0.9362 0.9482 1.2245 0.0241  -0.0507 0.3598  747 ALA A CB    
6130 N  N     . PHE A 748 ? 1.0733 1.0791 1.3658 0.0278  -0.0475 0.4082  748 PHE A N     
6131 C  CA    . PHE A 748 ? 1.0778 1.0911 1.3631 0.0283  -0.0582 0.4349  748 PHE A CA    
6132 C  C     . PHE A 748 ? 1.0758 1.0805 1.3907 0.0337  -0.0455 0.4524  748 PHE A C     
6133 O  O     . PHE A 748 ? 1.0543 1.0624 1.3601 0.0340  -0.0502 0.4739  748 PHE A O     
6134 C  CB    . PHE A 748 ? 1.1624 1.1775 1.3969 0.0221  -0.0657 0.4318  748 PHE A CB    
6135 C  CG    . PHE A 748 ? 1.2048 1.2277 1.4084 0.0169  -0.0811 0.4179  748 PHE A CG    
6136 C  CD1   . PHE A 748 ? 1.2882 1.3082 1.4932 0.0148  -0.0767 0.3931  748 PHE A CD1   
6137 C  CD2   . PHE A 748 ? 1.1539 1.1858 1.3265 0.0139  -0.1007 0.4299  748 PHE A CD2   
6138 C  CE1   . PHE A 748 ? 1.2064 1.2326 1.3855 0.0099  -0.0908 0.3812  748 PHE A CE1   
6139 C  CE2   . PHE A 748 ? 1.2461 1.2828 1.3911 0.0086  -0.1157 0.4167  748 PHE A CE2   
6140 C  CZ    . PHE A 748 ? 1.2045 1.2385 1.3544 0.0065  -0.1105 0.3927  748 PHE A CZ    
6141 N  N     . GLY A 749 ? 1.1230 1.1153 1.4722 0.0381  -0.0295 0.4436  749 GLY A N     
6142 C  CA    . GLY A 749 ? 1.2702 1.2513 1.6513 0.0433  -0.0170 0.4582  749 GLY A CA    
6143 C  C     . GLY A 749 ? 1.1850 1.1519 1.5554 0.0395  -0.0038 0.4515  749 GLY A C     
6144 O  O     . GLY A 749 ? 1.2617 1.2143 1.6622 0.0429  0.0094  0.4558  749 GLY A O     
6145 N  N     . TYR A 750 ? 1.2006 1.1706 1.5306 0.0327  -0.0068 0.4413  750 TYR A N     
6146 C  CA    . TYR A 750 ? 1.2141 1.1735 1.5354 0.0290  0.0053  0.4377  750 TYR A CA    
6147 C  C     . TYR A 750 ? 1.1596 1.1025 1.4993 0.0277  0.0196  0.4136  750 TYR A C     
6148 O  O     . TYR A 750 ? 1.1317 1.0739 1.4674 0.0269  0.0188  0.3916  750 TYR A O     
6149 C  CB    . TYR A 750 ? 1.1424 1.1098 1.4158 0.0231  -0.0005 0.4317  750 TYR A CB    
6150 C  CG    . TYR A 750 ? 1.2456 1.2257 1.4945 0.0240  -0.0131 0.4556  750 TYR A CG    
6151 C  CD1   . TYR A 750 ? 1.3185 1.2997 1.5873 0.0284  -0.0130 0.4841  750 TYR A CD1   
6152 C  CD2   . TYR A 750 ? 1.2865 1.2761 1.4909 0.0207  -0.0256 0.4495  750 TYR A CD2   
6153 C  CE1   . TYR A 750 ? 1.3509 1.3437 1.5945 0.0293  -0.0255 0.5065  750 TYR A CE1   
6154 C  CE2   . TYR A 750 ? 1.2869 1.2862 1.4645 0.0215  -0.0382 0.4701  750 TYR A CE2   
6155 C  CZ    . TYR A 750 ? 1.3644 1.3657 1.5609 0.0257  -0.0383 0.4988  750 TYR A CZ    
6156 O  OH    . TYR A 750 ? 1.3908 1.4017 1.5580 0.0266  -0.0517 0.5198  750 TYR A OH    
6157 N  N     . ARG A 751 ? 1.2504 1.1794 1.6098 0.0272  0.0321  0.4184  751 ARG A N     
6158 C  CA    . ARG A 751 ? 1.3695 1.2808 1.7441 0.0246  0.0445  0.3965  751 ARG A CA    
6159 C  C     . ARG A 751 ? 1.3488 1.2569 1.7092 0.0176  0.0511  0.3949  751 ARG A C     
6160 O  O     . ARG A 751 ? 1.2912 1.2087 1.6355 0.0165  0.0488  0.4138  751 ARG A O     
6161 C  CB    . ARG A 751 ? 1.3819 1.2762 1.8002 0.0304  0.0535  0.4024  751 ARG A CB    
6162 C  CG    . ARG A 751 ? 1.5473 1.4231 1.9796 0.0301  0.0626  0.3752  751 ARG A CG    
6163 C  CD    . ARG A 751 ? 1.4986 1.3658 1.9617 0.0396  0.0660  0.3763  751 ARG A CD    
6164 N  NE    . ARG A 751 ? 1.6054 1.4586 2.1034 0.0443  0.0735  0.3951  751 ARG A NE    
6165 C  CZ    . ARG A 751 ? 1.5017 1.3319 2.0292 0.0492  0.0842  0.3867  751 ARG A CZ    
6166 N  NH1   . ARG A 751 ? 1.3016 1.1202 1.8264 0.0504  0.0890  0.3597  751 ARG A NH1   
6167 N  NH2   . ARG A 751 ? 1.5229 1.3405 2.0822 0.0535  0.0904  0.4059  751 ARG A NH2   
6168 N  N     . LYS A 752 ? 1.2639 1.1589 1.6302 0.0130  0.0593  0.3726  752 LYS A N     
6169 C  CA    . LYS A 752 ? 1.2756 1.1699 1.6290 0.0056  0.0649  0.3682  752 LYS A CA    
6170 C  C     . LYS A 752 ? 1.3051 1.1978 1.6726 0.0052  0.0708  0.3944  752 LYS A C     
6171 O  O     . LYS A 752 ? 1.3323 1.2353 1.6782 0.0023  0.0719  0.4043  752 LYS A O     
6172 C  CB    . LYS A 752 ? 1.1389 1.0172 1.5053 0.0008  0.0719  0.3426  752 LYS A CB    
6173 C  CG    . LYS A 752 ? 1.0913 0.9736 1.4364 -0.0003 0.0671  0.3162  752 LYS A CG    
6174 C  CD    . LYS A 752 ? 1.0939 0.9654 1.4409 -0.0074 0.0725  0.2937  752 LYS A CD    
6175 C  CE    . LYS A 752 ? 0.9676 0.8206 1.3345 -0.0053 0.0756  0.2749  752 LYS A CE    
6176 N  NZ    . LYS A 752 ? 1.0546 0.9108 1.4006 -0.0067 0.0720  0.2495  752 LYS A NZ    
6177 N  N     . GLU A 753 ? 1.2283 1.1078 1.6321 0.0089  0.0756  0.4068  753 GLU A N     
6178 C  CA    . GLU A 753 ? 1.2282 1.1053 1.6498 0.0090  0.0813  0.4340  753 GLU A CA    
6179 C  C     . GLU A 753 ? 1.2244 1.1215 1.6193 0.0121  0.0746  0.4586  753 GLU A C     
6180 O  O     . GLU A 753 ? 1.2639 1.1652 1.6550 0.0103  0.0797  0.4776  753 GLU A O     
6181 C  CB    . GLU A 753 ? 1.2708 1.1310 1.7348 0.0144  0.0856  0.4440  753 GLU A CB    
6182 C  CG    . GLU A 753 ? 1.3074 1.1461 1.7933 0.0143  0.0902  0.4178  753 GLU A CG    
6183 C  CD    . GLU A 753 ? 1.4437 1.2875 1.9162 0.0190  0.0838  0.3992  753 GLU A CD    
6184 O  OE1   . GLU A 753 ? 1.4938 1.3574 1.9344 0.0188  0.0750  0.3979  753 GLU A OE1   
6185 O  OE2   . GLU A 753 ? 1.5011 1.3280 1.9952 0.0231  0.0880  0.3861  753 GLU A OE2   
6186 N  N     . ASP A 754 ? 1.3371 1.2464 1.7128 0.0166  0.0630  0.4588  754 ASP A N     
6187 C  CA    . ASP A 754 ? 1.4156 1.3429 1.7608 0.0191  0.0535  0.4792  754 ASP A CA    
6188 C  C     . ASP A 754 ? 1.4241 1.3623 1.7235 0.0147  0.0511  0.4682  754 ASP A C     
6189 O  O     . ASP A 754 ? 1.5105 1.4620 1.7770 0.0167  0.0421  0.4804  754 ASP A O     
6190 C  CB    . ASP A 754 ? 1.3645 1.3001 1.7093 0.0247  0.0401  0.4833  754 ASP A CB    
6191 C  CG    . ASP A 754 ? 1.4740 1.3985 1.8651 0.0304  0.0436  0.4910  754 ASP A CG    
6192 O  OD1   . ASP A 754 ? 1.7011 1.6080 2.1196 0.0293  0.0548  0.4775  754 ASP A OD1   
6193 O  OD2   . ASP A 754 ? 1.5101 1.4431 1.9102 0.0362  0.0349  0.5105  754 ASP A OD2   
6194 N  N     . LEU A 755 ? 1.4082 1.3404 1.7046 0.0091  0.0586  0.4455  755 LEU A N     
6195 C  CA    . LEU A 755 ? 1.3609 1.3024 1.6170 0.0057  0.0576  0.4332  755 LEU A CA    
6196 C  C     . LEU A 755 ? 1.3405 1.2792 1.5996 0.0008  0.0709  0.4328  755 LEU A C     
6197 O  O     . LEU A 755 ? 1.2154 1.1623 1.4421 -0.0011 0.0723  0.4258  755 LEU A O     
6198 C  CB    . LEU A 755 ? 1.2563 1.1976 1.5011 0.0037  0.0515  0.4034  755 LEU A CB    
6199 C  CG    . LEU A 755 ? 1.2331 1.1800 1.4726 0.0078  0.0378  0.4017  755 LEU A CG    
6200 C  CD1   . LEU A 755 ? 1.1938 1.1330 1.4509 0.0071  0.0378  0.3772  755 LEU A CD1   
6201 C  CD2   . LEU A 755 ? 1.1186 1.0787 1.3123 0.0077  0.0266  0.4005  755 LEU A CD2   
6202 N  N     . ARG A 756 ? 1.3972 1.3243 1.6951 -0.0013 0.0807  0.4407  756 ARG A N     
6203 C  CA    . ARG A 756 ? 1.2648 1.1887 1.5733 -0.0072 0.0928  0.4400  756 ARG A CA    
6204 C  C     . ARG A 756 ? 1.2537 1.1875 1.5504 -0.0054 0.0998  0.4682  756 ARG A C     
6205 O  O     . ARG A 756 ? 1.3562 1.3025 1.6150 -0.0009 0.0948  0.4780  756 ARG A O     
6206 C  CB    . ARG A 756 ? 1.1504 1.0556 1.5070 -0.0110 0.0991  0.4360  756 ARG A CB    
6207 C  CG    . ARG A 756 ? 1.2348 1.1294 1.5990 -0.0149 0.0965  0.4040  756 ARG A CG    
6208 C  CD    . ARG A 756 ? 1.2168 1.0945 1.6117 -0.0117 0.0945  0.3993  756 ARG A CD    
6209 N  NE    . ARG A 756 ? 1.2461 1.1079 1.6569 -0.0167 0.0961  0.3723  756 ARG A NE    
6210 C  CZ    . ARG A 756 ? 1.2185 1.0610 1.6568 -0.0147 0.0970  0.3638  756 ARG A CZ    
6211 N  NH1   . ARG A 756 ? 1.3854 1.2226 1.8419 -0.0075 0.0969  0.3804  756 ARG A NH1   
6212 N  NH2   . ARG A 756 ? 1.1201 0.9478 1.5668 -0.0195 0.0980  0.3381  756 ARG A NH2   
6213 O  "O5'" . DG  B 1   ? 1.5614 0.9023 2.2234 -0.1076 0.0646  0.0406  1   DG  P "O5'" 
6214 C  "C5'" . DG  B 1   ? 1.6226 0.9532 2.2498 -0.0999 0.0653  0.0146  1   DG  P "C5'" 
6215 C  "C4'" . DG  B 1   ? 1.6530 0.9940 2.2686 -0.0791 0.0809  0.0244  1   DG  P "C4'" 
6216 O  "O4'" . DG  B 1   ? 1.5016 0.8232 2.0804 -0.0684 0.0831  -0.0054 1   DG  P "O4'" 
6217 C  "C3'" . DG  B 1   ? 1.5910 0.9839 2.1944 -0.0749 0.0841  0.0453  1   DG  P "C3'" 
6218 O  "O3'" . DG  B 1   ? 1.6281 1.0295 2.2361 -0.0579 0.0975  0.0635  1   DG  P "O3'" 
6219 C  "C2'" . DG  B 1   ? 1.4353 0.8375 1.9956 -0.0741 0.0781  0.0189  1   DG  P "C2'" 
6220 C  "C1'" . DG  B 1   ? 1.4594 0.8182 2.0052 -0.0643 0.0824  -0.0079 1   DG  P "C1'" 
6221 N  N9    . DG  B 1   ? 1.5620 0.9067 2.0748 -0.0700 0.0722  -0.0406 1   DG  P N9    
6222 C  C8    . DG  B 1   ? 1.4574 0.8058 1.9674 -0.0880 0.0563  -0.0511 1   DG  P C8    
6223 N  N7    . DG  B 1   ? 1.3807 0.7137 1.8567 -0.0891 0.0490  -0.0811 1   DG  P N7    
6224 C  C5    . DG  B 1   ? 1.5575 0.8752 2.0119 -0.0700 0.0622  -0.0911 1   DG  P C5    
6225 C  C6    . DG  B 1   ? 1.4849 0.7824 1.8987 -0.0614 0.0632  -0.1206 1   DG  P C6    
6226 O  O6    . DG  B 1   ? 1.3400 0.6284 1.7264 -0.0695 0.0510  -0.1449 1   DG  P O6    
6227 N  N1    . DG  B 1   ? 1.3387 0.6272 1.7451 -0.0408 0.0807  -0.1192 1   DG  P N1    
6228 C  C2    . DG  B 1   ? 1.3479 0.6461 1.7836 -0.0305 0.0939  -0.0925 1   DG  P C2    
6229 N  N2    . DG  B 1   ? 1.4014 0.6902 1.8277 -0.0107 0.1098  -0.0942 1   DG  P N2    
6230 N  N3    . DG  B 1   ? 1.3923 0.7090 1.8642 -0.0388 0.0919  -0.0650 1   DG  P N3    
6231 C  C4    . DG  B 1   ? 1.5414 0.8665 2.0199 -0.0583 0.0765  -0.0662 1   DG  P C4    
6232 P  P     . DA  B 2   ? 1.6188 1.0700 2.2216 -0.0524 0.1017  0.0918  2   DA  P P     
6233 O  OP1   . DA  B 2   ? 1.3766 0.8303 2.0156 -0.0504 0.1082  0.1237  2   DA  P OP1   
6234 O  OP2   . DA  B 2   ? 1.2717 0.7531 1.8552 -0.0638 0.0919  0.0878  2   DA  P OP2   
6235 O  "O5'" . DA  B 2   ? 1.4744 0.9305 2.0519 -0.0338 0.1103  0.0844  2   DA  P "O5'" 
6236 C  "C5'" . DA  B 2   ? 1.4859 0.9183 2.0788 -0.0194 0.1216  0.0888  2   DA  P "C5'" 
6237 C  "C4'" . DA  B 2   ? 1.4462 0.8782 2.0108 -0.0041 0.1283  0.0725  2   DA  P "C4'" 
6238 O  "O4'" . DA  B 2   ? 1.4804 0.8944 2.0155 -0.0090 0.1223  0.0387  2   DA  P "O4'" 
6239 C  "C3'" . DA  B 2   ? 1.3222 0.7984 1.8685 0.0022  0.1289  0.0862  2   DA  P "C3'" 
6240 O  "O3'" . DA  B 2   ? 1.4333 0.9075 1.9766 0.0201  0.1398  0.0874  2   DA  P "O3'" 
6241 C  "C2'" . DA  B 2   ? 1.3658 0.8541 1.8777 -0.0066 0.1195  0.0635  2   DA  P "C2'" 
6242 C  "C1'" . DA  B 2   ? 1.3626 0.8082 1.8653 -0.0074 0.1192  0.0325  2   DA  P "C1'" 
6243 N  N9    . DA  B 2   ? 1.4433 0.8878 1.9267 -0.0223 0.1065  0.0119  2   DA  P N9    
6244 C  C8    . DA  B 2   ? 1.4251 0.8844 1.9193 -0.0388 0.0959  0.0201  2   DA  P C8    
6245 N  N7    . DA  B 2   ? 1.4035 0.8590 1.8779 -0.0496 0.0851  -0.0019 2   DA  P N7    
6246 C  C5    . DA  B 2   ? 1.3699 0.8057 1.8159 -0.0394 0.0887  -0.0267 2   DA  P C5    
6247 C  C6    . DA  B 2   ? 1.3590 0.7820 1.7728 -0.0430 0.0813  -0.0565 2   DA  P C6    
6248 N  N6    . DA  B 2   ? 1.2312 0.6603 1.6383 -0.0591 0.0668  -0.0663 2   DA  P N6    
6249 N  N1    . DA  B 2   ? 1.4298 0.8341 1.8187 -0.0289 0.0895  -0.0749 2   DA  P N1    
6250 C  C2    . DA  B 2   ? 1.3633 0.7631 1.7623 -0.0124 0.1044  -0.0636 2   DA  P C2    
6251 N  N3    . DA  B 2   ? 1.3263 0.7376 1.7568 -0.0079 0.1115  -0.0357 2   DA  P N3    
6252 C  C4    . DA  B 2   ? 1.3710 0.7999 1.8226 -0.0222 0.1028  -0.0185 2   DA  P C4    
6253 P  P     . DC  B 3   ? 1.4477 0.9639 1.9770 0.0288  0.1412  0.1028  3   DC  P P     
6254 O  OP1   . DC  B 3   ? 1.0654 0.5792 1.6175 0.0445  0.1521  0.1215  3   DC  P OP1   
6255 O  OP2   . DC  B 3   ? 1.4554 1.0058 1.9795 0.0168  0.1312  0.1179  3   DC  P OP2   
6256 O  "O5'" . DC  B 3   ? 1.2305 0.7458 1.7232 0.0330  0.1413  0.0743  3   DC  P "O5'" 
6257 C  "C5'" . DC  B 3   ? 1.3053 0.7842 1.7908 0.0416  0.1493  0.0505  3   DC  P "C5'" 
6258 C  "C4'" . DC  B 3   ? 1.2756 0.7593 1.7226 0.0426  0.1473  0.0254  3   DC  P "C4'" 
6259 O  "O4'" . DC  B 3   ? 1.4263 0.9028 1.8571 0.0263  0.1349  0.0070  3   DC  P "O4'" 
6260 C  "C3'" . DC  B 3   ? 1.2361 0.7626 1.6679 0.0459  0.1453  0.0366  3   DC  P "C3'" 
6261 O  "O3'" . DC  B 3   ? 1.1455 0.6694 1.5616 0.0606  0.1553  0.0259  3   DC  P "O3'" 
6262 C  "C2'" . DC  B 3   ? 1.3046 0.8475 1.7130 0.0302  0.1318  0.0256  3   DC  P "C2'" 
6263 C  "C1'" . DC  B 3   ? 1.2739 0.7793 1.6756 0.0228  0.1284  0.0001  3   DC  P "C1'" 
6264 N  N1    . DC  B 3   ? 1.3464 0.8596 1.7440 0.0043  0.1144  -0.0041 3   DC  P N1    
6265 C  C2    . DC  B 3   ? 1.3127 0.8213 1.6810 -0.0028 0.1063  -0.0293 3   DC  P C2    
6266 O  O2    . DC  B 3   ? 1.2969 0.7941 1.6407 0.0065  0.1113  -0.0480 3   DC  P O2    
6267 N  N3    . DC  B 3   ? 1.1768 0.6942 1.5451 -0.0194 0.0935  -0.0313 3   DC  P N3    
6268 C  C4    . DC  B 3   ? 1.2544 0.7846 1.6496 -0.0282 0.0902  -0.0095 3   DC  P C4    
6269 N  N4    . DC  B 3   ? 1.2765 0.8163 1.6730 -0.0439 0.0788  -0.0112 3   DC  P N4    
6270 C  C5    . DC  B 3   ? 1.2583 0.7927 1.6808 -0.0210 0.0987  0.0160  3   DC  P C5    
6271 C  C6    . DC  B 3   ? 1.3423 0.8681 1.7653 -0.0051 0.1099  0.0178  3   DC  P C6    
6272 P  P     . DC  B 4   ? 1.3048 0.8691 1.7083 0.0666  0.1552  0.0369  4   DC  P P     
6273 O  OP1   . DC  B 4   ? 1.4686 1.0267 1.8790 0.0853  0.1699  0.0393  4   DC  P OP1   
6274 O  OP2   . DC  B 4   ? 1.3767 0.9732 1.7931 0.0583  0.1460  0.0623  4   DC  P OP2   
6275 O  "O5'" . DC  B 4   ? 1.2193 0.7887 1.5847 0.0592  0.1479  0.0122  4   DC  P "O5'" 
6276 C  "C5'" . DC  B 4   ? 1.3426 0.8785 1.6882 0.0594  0.1501  -0.0164 4   DC  P "C5'" 
6277 C  "C4'" . DC  B 4   ? 1.4193 0.9678 1.7303 0.0515  0.1412  -0.0346 4   DC  P "C4'" 
6278 O  "O4'" . DC  B 4   ? 1.4580 1.0062 1.7678 0.0335  0.1270  -0.0391 4   DC  P "O4'" 
6279 C  "C3'" . DC  B 4   ? 1.3678 0.9574 1.6692 0.0534  0.1389  -0.0221 4   DC  P "C3'" 
6280 O  "O3'" . DC  B 4   ? 1.4198 1.0100 1.6901 0.0579  0.1410  -0.0411 4   DC  P "O3'" 
6281 C  "C2'" . DC  B 4   ? 1.2775 0.8890 1.5803 0.0368  0.1244  -0.0135 4   DC  P "C2'" 
6282 C  "C1'" . DC  B 4   ? 1.3283 0.9114 1.6237 0.0260  0.1179  -0.0342 4   DC  P "C1'" 
6283 N  N1    . DC  B 4   ? 1.3202 0.9129 1.6290 0.0102  0.1065  -0.0247 4   DC  P N1    
6284 C  C2    . DC  B 4   ? 1.2427 0.8337 1.5358 -0.0032 0.0951  -0.0406 4   DC  P C2    
6285 O  O2    . DC  B 4   ? 1.2192 0.8001 1.4858 -0.0018 0.0937  -0.0627 4   DC  P O2    
6286 N  N3    . DC  B 4   ? 1.2291 0.8302 1.5371 -0.0169 0.0862  -0.0302 4   DC  P N3    
6287 C  C4    . DC  B 4   ? 1.2240 0.8358 1.5583 -0.0172 0.0887  -0.0056 4   DC  P C4    
6288 N  N4    . DC  B 4   ? 1.3015 0.9235 1.6493 -0.0301 0.0813  0.0048  4   DC  P N4    
6289 C  C5    . DC  B 4   ? 1.1357 0.7489 1.4842 -0.0041 0.0991  0.0106  4   DC  P C5    
6290 C  C6    . DC  B 4   ? 1.3162 0.9201 1.6526 0.0091  0.1075  0.0005  4   DC  P C6    
6291 P  P     . DA  B 5   ? 1.3768 0.9961 1.6403 0.0691  0.1474  -0.0312 5   DA  P P     
6292 O  OP1   . DA  B 5   ? 1.5184 1.1194 1.7881 0.0869  0.1643  -0.0332 5   DA  P OP1   
6293 O  OP2   . DA  B 5   ? 1.2187 0.8721 1.4990 0.0637  0.1399  -0.0063 5   DA  P OP2   
6294 O  "O5'" . DA  B 5   ? 1.1776 0.8040 1.4045 0.0640  0.1412  -0.0514 5   DA  P "O5'" 
6295 C  "C5'" . DA  B 5   ? 1.1360 0.7324 1.3380 0.0662  0.1442  -0.0777 5   DA  P "C5'" 
6296 C  "C4'" . DA  B 5   ? 1.2509 0.8502 1.4292 0.0511  0.1293  -0.0932 5   DA  P "C4'" 
6297 O  "O4'" . DA  B 5   ? 1.3887 0.9925 1.5862 0.0363  0.1175  -0.0841 5   DA  P "O4'" 
6298 C  "C3'" . DA  B 5   ? 1.1828 0.8150 1.3425 0.0489  0.1240  -0.0910 5   DA  P "C3'" 
6299 O  "O3'" . DA  B 5   ? 1.2467 0.8689 1.3754 0.0431  0.1171  -0.1136 5   DA  P "O3'" 
6300 C  "C2'" . DA  B 5   ? 1.1593 0.8183 1.3370 0.0367  0.1128  -0.0725 5   DA  P "C2'" 
6301 C  "C1'" . DA  B 5   ? 1.3142 0.9499 1.5045 0.0263  0.1066  -0.0775 5   DA  P "C1'" 
6302 N  N9    . DA  B 5   ? 1.3162 0.9671 1.5328 0.0186  0.1014  -0.0563 5   DA  P N9    
6303 C  C8    . DA  B 5   ? 1.2112 0.8767 1.4504 0.0248  0.1068  -0.0332 5   DA  P C8    
6304 N  N7    . DA  B 5   ? 1.1866 0.8630 1.4435 0.0157  0.1004  -0.0174 5   DA  P N7    
6305 C  C5    . DA  B 5   ? 1.2183 0.8877 1.4666 0.0026  0.0909  -0.0305 5   DA  P C5    
6306 C  C6    . DA  B 5   ? 1.2313 0.9073 1.4917 -0.0107 0.0821  -0.0228 5   DA  P C6    
6307 N  N6    . DA  B 5   ? 1.2691 0.9597 1.5501 -0.0127 0.0822  0.0003  5   DA  P N6    
6308 N  N1    . DA  B 5   ? 1.0186 0.6861 1.2691 -0.0218 0.0733  -0.0389 5   DA  P N1    
6309 C  C2    . DA  B 5   ? 1.0399 0.6925 1.2670 -0.0198 0.0724  -0.0619 5   DA  P C2    
6310 N  N3    . DA  B 5   ? 1.1479 0.7920 1.3585 -0.0072 0.0807  -0.0717 5   DA  P N3    
6311 C  C4    . DA  B 5   ? 1.2658 0.9195 1.4897 0.0038  0.0904  -0.0546 5   DA  P C4    
6312 P  P     . DC  B 6   ? 1.3136 0.9595 1.4151 0.0449  0.1153  -0.1182 6   DC  P P     
6313 O  OP1   . DC  B 6   ? 1.3840 1.0062 1.4567 0.0548  0.1236  -0.1389 6   DC  P OP1   
6314 O  OP2   . DC  B 6   ? 1.4257 1.1042 1.5429 0.0496  0.1189  -0.0957 6   DC  P OP2   
6315 O  "O5'" . DC  B 6   ? 1.4377 1.0940 1.5298 0.0272  0.0975  -0.1244 6   DC  P "O5'" 
6316 C  "C5'" . DC  B 6   ? 1.3551 1.0027 1.4658 0.0147  0.0882  -0.1222 6   DC  P "C5'" 
6317 C  "C4'" . DC  B 6   ? 1.1799 0.8516 1.2887 0.0005  0.0740  -0.1186 6   DC  P "C4'" 
6318 O  "O4'" . DC  B 6   ? 1.2825 0.9653 1.4202 -0.0069 0.0706  -0.0999 6   DC  P "O4'" 
6319 C  "C3'" . DC  B 6   ? 1.0946 0.7976 1.1897 0.0033  0.0735  -0.1123 6   DC  P "C3'" 
6320 O  "O3'" . DC  B 6   ? 1.2656 0.9791 1.3469 -0.0080 0.0609  -0.1202 6   DC  P "O3'" 
6321 C  "C2'" . DC  B 6   ? 1.2205 0.9463 1.3401 0.0034  0.0752  -0.0882 6   DC  P "C2'" 
6322 C  "C1'" . DC  B 6   ? 1.1696 0.8859 1.3091 -0.0077 0.0686  -0.0842 6   DC  P "C1'" 
6323 N  N1    . DC  B 6   ? 1.1600 0.8852 1.3262 -0.0063 0.0724  -0.0621 6   DC  P N1    
6324 C  C2    . DC  B 6   ? 1.1485 0.8796 1.3321 -0.0172 0.0657  -0.0516 6   DC  P C2    
6325 O  O2    . DC  B 6   ? 1.0396 0.7690 1.2188 -0.0281 0.0569  -0.0605 6   DC  P O2    
6326 N  N3    . DC  B 6   ? 1.1287 0.8677 1.3338 -0.0153 0.0693  -0.0308 6   DC  P N3    
6327 C  C4    . DC  B 6   ? 1.0769 0.8187 1.2882 -0.0037 0.0776  -0.0206 6   DC  P C4    
6328 N  N4    . DC  B 6   ? 0.9805 0.7306 1.2124 -0.0025 0.0795  0.0005  6   DC  P N4    
6329 C  C5    . DC  B 6   ? 1.1854 0.9224 1.3826 0.0073  0.0846  -0.0306 6   DC  P C5    
6330 C  C6    . DC  B 6   ? 1.1887 0.9172 1.3628 0.0059  0.0824  -0.0511 6   DC  P C6    
6331 P  P     . DG  B 7   ? 1.3166 1.0296 1.3641 -0.0054 0.0586  -0.1378 7   DG  P P     
6332 O  OP1   . DG  B 7   ? 1.4515 1.1303 1.4835 -0.0003 0.0626  -0.1569 7   DG  P OP1   
6333 O  OP2   . DG  B 7   ? 1.2303 0.9685 1.2715 0.0030  0.0648  -0.1274 7   DG  P OP2   
6334 O  "O5'" . DG  B 7   ? 1.2827 1.0063 1.3265 -0.0207 0.0425  -0.1425 7   DG  P "O5'" 
6335 C  "C5'" . DG  B 7   ? 1.3222 1.0764 1.3755 -0.0263 0.0377  -0.1278 7   DG  P "C5'" 
6336 C  "C4'" . DG  B 7   ? 1.1064 0.8633 1.1769 -0.0405 0.0268  -0.1246 7   DG  P "C4'" 
6337 O  "O4'" . DG  B 7   ? 0.9675 0.7218 1.0652 -0.0413 0.0314  -0.1098 7   DG  P "O4'" 
6338 C  "C3'" . DG  B 7   ? 1.1656 0.9519 1.2365 -0.0470 0.0198  -0.1159 7   DG  P "C3'" 
6339 O  "O3'" . DG  B 7   ? 1.2023 0.9883 1.2833 -0.0600 0.0088  -0.1187 7   DG  P "O3'" 
6340 C  "C2'" . DG  B 7   ? 1.0851 0.8878 1.1736 -0.0433 0.0267  -0.0954 7   DG  P "C2'" 
6341 C  "C1'" . DG  B 7   ? 0.9469 0.7288 1.0553 -0.0428 0.0314  -0.0917 7   DG  P "C1'" 
6342 N  N9    . DG  B 7   ? 0.9977 0.7832 1.1149 -0.0329 0.0416  -0.0780 7   DG  P N9    
6343 C  C8    . DG  B 7   ? 1.0883 0.8705 1.1954 -0.0209 0.0501  -0.0801 7   DG  P C8    
6344 N  N7    . DG  B 7   ? 1.1246 0.9129 1.2462 -0.0144 0.0569  -0.0644 7   DG  P N7    
6345 C  C5    . DG  B 7   ? 1.0200 0.8153 1.1596 -0.0224 0.0528  -0.0515 7   DG  P C5    
6346 C  C6    . DG  B 7   ? 1.0035 0.8071 1.1615 -0.0204 0.0560  -0.0317 7   DG  P C6    
6347 O  O6    . DG  B 7   ? 0.9790 0.7862 1.1433 -0.0115 0.0621  -0.0213 7   DG  P O6    
6348 N  N1    . DG  B 7   ? 0.9734 0.7823 1.1439 -0.0299 0.0512  -0.0229 7   DG  P N1    
6349 C  C2    . DG  B 7   ? 0.9021 0.7096 1.0711 -0.0402 0.0441  -0.0315 7   DG  P C2    
6350 N  N2    . DG  B 7   ? 0.7924 0.6069 0.9769 -0.0478 0.0418  -0.0191 7   DG  P N2    
6351 N  N3    . DG  B 7   ? 0.9687 0.7689 1.1223 -0.0429 0.0396  -0.0499 7   DG  P N3    
6352 C  C4    . DG  B 7   ? 0.9588 0.7527 1.0967 -0.0335 0.0442  -0.0593 7   DG  P C4    
6353 P  P     . DG  B 8   ? 1.1821 0.9940 1.2590 -0.0671 -0.0002 -0.1160 8   DG  P P     
6354 O  OP1   . DG  B 8   ? 1.3196 1.1264 1.4096 -0.0802 -0.0116 -0.1204 8   DG  P OP1   
6355 O  OP2   . DG  B 8   ? 1.2276 1.0459 1.2773 -0.0601 0.0004  -0.1244 8   DG  P OP2   
6356 O  "O5'" . DG  B 8   ? 1.1077 0.9429 1.1997 -0.0654 0.0055  -0.0950 8   DG  P "O5'" 
6357 C  "C5'" . DG  B 8   ? 1.1032 0.9376 1.2205 -0.0703 0.0072  -0.0822 8   DG  P "C5'" 
6358 C  "C4'" . DG  B 8   ? 1.0770 0.9306 1.1994 -0.0653 0.0141  -0.0640 8   DG  P "C4'" 
6359 O  "O4'" . DG  B 8   ? 0.9212 0.7664 1.0421 -0.0555 0.0225  -0.0602 8   DG  P "O4'" 
6360 C  "C3'" . DG  B 8   ? 1.1070 0.9833 1.2139 -0.0627 0.0128  -0.0618 8   DG  P "C3'" 
6361 O  "O3'" . DG  B 8   ? 1.0488 0.9416 1.1660 -0.0691 0.0101  -0.0520 8   DG  P "O3'" 
6362 C  "C2'" . DG  B 8   ? 0.9797 0.8615 1.0809 -0.0526 0.0204  -0.0528 8   DG  P "C2'" 
6363 C  "C1'" . DG  B 8   ? 0.9246 0.7893 1.0409 -0.0502 0.0259  -0.0479 8   DG  P "C1'" 
6364 N  N9    . DG  B 8   ? 0.9412 0.8005 1.0519 -0.0399 0.0326  -0.0470 8   DG  P N9    
6365 C  C8    . DG  B 8   ? 0.9834 0.8367 1.0783 -0.0334 0.0347  -0.0588 8   DG  P C8    
6366 N  N7    . DG  B 8   ? 0.9708 0.8219 1.0678 -0.0241 0.0420  -0.0530 8   DG  P N7    
6367 C  C5    . DG  B 8   ? 0.9227 0.7785 1.0372 -0.0249 0.0435  -0.0367 8   DG  P C5    
6368 C  C6    . DG  B 8   ? 0.9483 0.8054 1.0738 -0.0176 0.0492  -0.0233 8   DG  P C6    
6369 O  O6    . DG  B 8   ? 1.0764 0.9314 1.2009 -0.0086 0.0549  -0.0228 8   DG  P O6    
6370 N  N1    . DG  B 8   ? 0.8691 0.7314 1.0090 -0.0214 0.0480  -0.0081 8   DG  P N1    
6371 C  C2    . DG  B 8   ? 0.8396 0.7056 0.9832 -0.0304 0.0436  -0.0057 8   DG  P C2    
6372 N  N2    . DG  B 8   ? 0.8263 0.6973 0.9826 -0.0319 0.0444  0.0108  8   DG  P N2    
6373 N  N3    . DG  B 8   ? 0.8744 0.7402 1.0109 -0.0373 0.0388  -0.0176 8   DG  P N3    
6374 C  C4    . DG  B 8   ? 0.8664 0.7269 0.9881 -0.0343 0.0383  -0.0329 8   DG  P C4    
6375 P  P     . DC  B 9   ? 1.0015 0.9174 1.1062 -0.0671 0.0091  -0.0480 9   DC  P P     
6376 O  OP1   . DC  B 9   ? 1.0137 0.9410 1.1309 -0.0752 0.0052  -0.0433 9   DC  P OP1   
6377 O  OP2   . DC  B 9   ? 1.0161 0.9316 1.1000 -0.0623 0.0070  -0.0600 9   DC  P OP2   
6378 O  "O5'" . DC  B 9   ? 0.8411 0.7651 0.9456 -0.0608 0.0162  -0.0329 9   DC  P "O5'" 
6379 C  "C5'" . DC  B 9   ? 0.8765 0.7995 0.9975 -0.0628 0.0200  -0.0195 9   DC  P "C5'" 
6380 C  "C4'" . DC  B 9   ? 0.9464 0.8765 1.0614 -0.0560 0.0248  -0.0070 9   DC  P "C4'" 
6381 O  "O4'" . DC  B 9   ? 0.9863 0.9052 1.0997 -0.0499 0.0273  -0.0088 9   DC  P "O4'" 
6382 C  "C3'" . DC  B 9   ? 0.8225 0.7682 0.9195 -0.0525 0.0236  -0.0063 9   DC  P "C3'" 
6383 O  "O3'" . DC  B 9   ? 0.9639 0.9203 1.0612 -0.0531 0.0260  0.0063  9   DC  P "O3'" 
6384 C  "C2'" . DC  B 9   ? 0.7765 0.7197 0.8639 -0.0450 0.0247  -0.0062 9   DC  P "C2'" 
6385 C  "C1'" . DC  B 9   ? 0.8581 0.7868 0.9598 -0.0437 0.0282  -0.0024 9   DC  P "C1'" 
6386 N  N1    . DC  B 9   ? 0.8175 0.7380 0.9159 -0.0372 0.0300  -0.0080 9   DC  P N1    
6387 C  C2    . DC  B 9   ? 0.8994 0.8178 1.0040 -0.0315 0.0332  0.0027  9   DC  P C2    
6388 O  O2    . DC  B 9   ? 0.8140 0.7369 0.9246 -0.0323 0.0335  0.0163  9   DC  P O2    
6389 N  N3    . DC  B 9   ? 0.7758 0.6881 0.8802 -0.0248 0.0361  -0.0012 9   DC  P N3    
6390 C  C4    . DC  B 9   ? 0.7494 0.6567 0.8445 -0.0234 0.0365  -0.0156 9   DC  P C4    
6391 N  N4    . DC  B 9   ? 0.7929 0.6946 0.8878 -0.0157 0.0413  -0.0180 9   DC  P N4    
6392 C  C5    . DC  B 9   ? 0.8062 0.7148 0.8921 -0.0294 0.0322  -0.0271 9   DC  P C5    
6393 C  C6    . DC  B 9   ? 0.7399 0.6556 0.8294 -0.0363 0.0288  -0.0226 9   DC  P C6    
6394 P  P     . DC  B 10  ? 0.8356 0.8066 0.9152 -0.0503 0.0251  0.0075  10  DC  P P     
6395 O  OP1   . DC  B 10  ? 0.7851 0.7645 0.8688 -0.0526 0.0287  0.0173  10  DC  P OP1   
6396 O  OP2   . DC  B 10  ? 0.8733 0.8467 0.9443 -0.0502 0.0208  -0.0056 10  DC  P OP2   
6397 O  "O5'" . DC  B 10  ? 0.8138 0.7844 0.8822 -0.0440 0.0254  0.0144  10  DC  P "O5'" 
6398 C  "C5'" . DC  B 10  ? 0.8860 0.8530 0.9602 -0.0428 0.0282  0.0273  10  DC  P "C5'" 
6399 C  "C4'" . DC  B 10  ? 0.8940 0.8601 0.9604 -0.0374 0.0260  0.0316  10  DC  P "C4'" 
6400 O  "O4'" . DC  B 10  ? 0.8062 0.7643 0.8800 -0.0354 0.0255  0.0242  10  DC  P "O4'" 
6401 C  "C3'" . DC  B 10  ? 0.7926 0.7672 0.8395 -0.0347 0.0219  0.0299  10  DC  P "C3'" 
6402 O  "O3'" . DC  B 10  ? 0.8305 0.8070 0.8687 -0.0324 0.0203  0.0417  10  DC  P "O3'" 
6403 C  "C2'" . DC  B 10  ? 0.7883 0.7609 0.8353 -0.0320 0.0191  0.0215  10  DC  P "C2'" 
6404 C  "C1'" . DC  B 10  ? 0.8523 0.8148 0.9160 -0.0311 0.0223  0.0235  10  DC  P "C1'" 
6405 N  N1    . DC  B 10  ? 0.7745 0.7316 0.8416 -0.0288 0.0232  0.0126  10  DC  P N1    
6406 C  C2    . DC  B 10  ? 0.7619 0.7128 0.8382 -0.0239 0.0254  0.0159  10  DC  P C2    
6407 O  O2    . DC  B 10  ? 0.7037 0.6547 0.7870 -0.0222 0.0253  0.0284  10  DC  P O2    
6408 N  N3    . DC  B 10  ? 0.6650 0.6105 0.7423 -0.0206 0.0279  0.0061  10  DC  P N3    
6409 C  C4    . DC  B 10  ? 0.7566 0.7024 0.8243 -0.0227 0.0271  -0.0066 10  DC  P C4    
6410 N  N4    . DC  B 10  ? 0.7070 0.6466 0.7727 -0.0186 0.0302  -0.0158 10  DC  P N4    
6411 C  C5    . DC  B 10  ? 0.7233 0.6763 0.7833 -0.0283 0.0235  -0.0096 10  DC  P C5    
6412 C  C6    . DC  B 10  ? 0.7577 0.7160 0.8184 -0.0309 0.0223  0.0002  10  DC  P C6    
6413 P  P     . DA  B 11  ? 0.8313 0.8136 0.8477 -0.0302 0.0149  0.0417  11  DA  P P     
6414 O  OP1   . DA  B 11  ? 0.8460 0.8297 0.8501 -0.0297 0.0163  0.0517  11  DA  P OP1   
6415 O  OP2   . DA  B 11  ? 0.8202 0.8064 0.8310 -0.0308 0.0138  0.0295  11  DA  P OP2   
6416 O  "O5'" . DA  B 11  ? 0.9116 0.8925 0.9306 -0.0274 0.0091  0.0462  11  DA  P "O5'" 
6417 C  "C5'" . DA  B 11  ? 0.7907 0.7680 0.8196 -0.0262 0.0092  0.0580  11  DA  P "C5'" 
6418 C  "C4'" . DA  B 11  ? 0.7505 0.7279 0.7888 -0.0234 0.0049  0.0604  11  DA  P "C4'" 
6419 O  "O4'" . DA  B 11  ? 0.7615 0.7356 0.8131 -0.0224 0.0095  0.0507  11  DA  P "O4'" 
6420 C  "C3'" . DA  B 11  ? 0.6956 0.6786 0.7209 -0.0229 -0.0036 0.0593  11  DA  P "C3'" 
6421 O  "O3'" . DA  B 11  ? 0.8336 0.8179 0.8583 -0.0219 -0.0107 0.0720  11  DA  P "O3'" 
6422 C  "C2'" . DA  B 11  ? 0.6958 0.6800 0.7319 -0.0210 -0.0024 0.0511  11  DA  P "C2'" 
6423 C  "C1'" . DA  B 11  ? 0.6211 0.5987 0.6751 -0.0196 0.0058  0.0498  11  DA  P "C1'" 
6424 N  N9    . DA  B 11  ? 0.6947 0.6704 0.7523 -0.0185 0.0103  0.0373  11  DA  P N9    
6425 C  C8    . DA  B 11  ? 0.6593 0.6346 0.7089 -0.0212 0.0125  0.0257  11  DA  P C8    
6426 N  N7    . DA  B 11  ? 0.7173 0.6903 0.7697 -0.0193 0.0156  0.0162  11  DA  P N7    
6427 C  C5    . DA  B 11  ? 0.7551 0.7269 0.8189 -0.0144 0.0171  0.0219  11  DA  P C5    
6428 C  C6    . DA  B 11  ? 0.7443 0.7134 0.8148 -0.0093 0.0220  0.0174  11  DA  P C6    
6429 N  N6    . DA  B 11  ? 0.6499 0.6161 0.7135 -0.0087 0.0254  0.0048  11  DA  P N6    
6430 N  N1    . DA  B 11  ? 0.7440 0.7138 0.8285 -0.0043 0.0236  0.0271  11  DA  P N1    
6431 C  C2    . DA  B 11  ? 0.6990 0.6722 0.7897 -0.0052 0.0188  0.0403  11  DA  P C2    
6432 N  N3    . DA  B 11  ? 0.7145 0.6896 0.7968 -0.0100 0.0131  0.0453  11  DA  P N3    
6433 C  C4    . DA  B 11  ? 0.7760 0.7501 0.8449 -0.0141 0.0134  0.0353  11  DA  P C4    
6434 P  P     . DC  B 12  ? 0.7951 0.7839 0.8078 -0.0226 -0.0224 0.0735  12  DC  P P     
6435 O  OP1   . DC  B 12  ? 0.8225 0.8111 0.8273 -0.0229 -0.0303 0.0867  12  DC  P OP1   
6436 O  OP2   . DC  B 12  ? 0.7845 0.7736 0.7800 -0.0242 -0.0228 0.0617  12  DC  P OP2   
6437 O  "O5'" . DC  B 12  ? 0.9236 0.9162 0.9580 -0.0202 -0.0232 0.0740  12  DC  P "O5'" 
6438 C  "C5'" . DC  B 12  ? 0.7009 0.6938 0.7562 -0.0174 -0.0221 0.0851  12  DC  P "C5'" 
6439 C  "C4'" . DC  B 12  ? 0.7433 0.7424 0.8152 -0.0150 -0.0251 0.0876  12  DC  P "C4'" 
6440 O  "O4'" . DC  B 12  ? 0.8569 0.8543 0.9372 -0.0121 -0.0149 0.0767  12  DC  P "O4'" 
6441 C  "C3'" . DC  B 12  ? 0.7538 0.7585 0.8149 -0.0182 -0.0366 0.0871  12  DC  P "C3'" 
6442 O  "O3'" . DC  B 12  ? 0.9582 0.9700 1.0374 -0.0172 -0.0443 0.0993  12  DC  P "O3'" 
6443 C  "C2'" . DC  B 12  ? 0.7273 0.7326 0.7857 -0.0177 -0.0307 0.0734  12  DC  P "C2'" 
6444 C  "C1'" . DC  B 12  ? 0.6663 0.6694 0.7430 -0.0127 -0.0184 0.0713  12  DC  P "C1'" 
6445 N  N1    . DC  B 12  ? 0.7122 0.7120 0.7814 -0.0123 -0.0100 0.0566  12  DC  P N1    
6446 C  C2    . DC  B 12  ? 0.7239 0.7246 0.8044 -0.0078 -0.0025 0.0521  12  DC  P C2    
6447 O  O2    . DC  B 12  ? 0.7424 0.7471 0.8408 -0.0038 -0.0015 0.0609  12  DC  P O2    
6448 N  N3    . DC  B 12  ? 0.7934 0.7909 0.8648 -0.0077 0.0037  0.0389  12  DC  P N3    
6449 C  C4    . DC  B 12  ? 0.7385 0.7333 0.7940 -0.0120 0.0024  0.0312  12  DC  P C4    
6450 N  N4    . DC  B 12  ? 0.7000 0.6928 0.7484 -0.0120 0.0071  0.0193  12  DC  P N4    
6451 C  C5    . DC  B 12  ? 0.6844 0.6788 0.7301 -0.0159 -0.0037 0.0361  12  DC  P C5    
6452 C  C6    . DC  B 12  ? 0.7442 0.7405 0.7955 -0.0158 -0.0096 0.0483  12  DC  P C6    
6453 P  P     . DA  B 13  ? 0.9850 1.0016 1.0558 -0.0221 -0.0610 0.1038  13  DA  P P     
6454 O  OP1   . DA  B 13  ? 0.8176 0.8391 0.9020 -0.0224 -0.0710 0.1206  13  DA  P OP1   
6455 O  OP2   . DA  B 13  ? 0.9020 0.9117 0.9416 -0.0259 -0.0647 0.0937  13  DA  P OP2   
6456 O  "O5'" . DA  B 13  ? 0.7945 0.8178 0.8807 -0.0209 -0.0590 0.1000  13  DA  P "O5'" 
6457 C  "C5'" . DA  B 13  ? 0.7485 0.7768 0.8614 -0.0151 -0.0489 0.1043  13  DA  P "C5'" 
6458 C  "C4'" . DA  B 13  ? 0.7004 0.7342 0.8210 -0.0138 -0.0453 0.0990  13  DA  P "C4'" 
6459 O  "O4'" . DA  B 13  ? 0.7290 0.7578 0.8453 -0.0095 -0.0302 0.0868  13  DA  P "O4'" 
6460 C  "C3'" . DA  B 13  ? 0.8788 0.9123 0.9817 -0.0197 -0.0552 0.0923  13  DA  P "C3'" 
6461 O  "O3'" . DA  B 13  ? 1.1208 1.1605 1.2332 -0.0239 -0.0705 0.1036  13  DA  P "O3'" 
6462 C  "C2'" . DA  B 13  ? 0.8350 0.8715 0.9431 -0.0163 -0.0449 0.0844  13  DA  P "C2'" 
6463 C  "C1'" . DA  B 13  ? 0.8382 0.8696 0.9478 -0.0104 -0.0293 0.0784  13  DA  P "C1'" 
6464 N  N9    . DA  B 13  ? 0.7696 0.7933 0.8568 -0.0117 -0.0242 0.0637  13  DA  P N9    
6465 C  C8    . DA  B 13  ? 0.7169 0.7342 0.7837 -0.0159 -0.0287 0.0589  13  DA  P C8    
6466 N  N7    . DA  B 13  ? 0.6936 0.7066 0.7468 -0.0161 -0.0222 0.0468  13  DA  P N7    
6467 C  C5    . DA  B 13  ? 0.6159 0.6316 0.6786 -0.0119 -0.0138 0.0426  13  DA  P C5    
6468 C  C6    . DA  B 13  ? 0.6615 0.6749 0.7165 -0.0103 -0.0058 0.0308  13  DA  P C6    
6469 N  N6    . DA  B 13  ? 0.8329 0.8421 0.8722 -0.0132 -0.0052 0.0216  13  DA  P N6    
6470 N  N1    . DA  B 13  ? 0.7611 0.7774 0.8254 -0.0053 0.0016  0.0298  13  DA  P N1    
6471 C  C2    . DA  B 13  ? 0.6370 0.6590 0.7198 -0.0018 0.0022  0.0405  13  DA  P C2    
6472 N  N3    . DA  B 13  ? 0.6336 0.6594 0.7288 -0.0032 -0.0053 0.0530  13  DA  P N3    
6473 C  C4    . DA  B 13  ? 0.6939 0.7158 0.7768 -0.0087 -0.0139 0.0529  13  DA  P C4    
6474 P  P     . DA  C 2   ? 2.2013 2.2351 2.1801 -0.0309 -0.0060 -0.0538 2   DA  T P     
6475 O  OP1   . DA  C 2   ? 1.4327 1.4760 1.4109 -0.0320 -0.0100 -0.0552 2   DA  T OP1   
6476 O  OP2   . DA  C 2   ? 1.5239 1.5566 1.5037 -0.0290 -0.0034 -0.0469 2   DA  T OP2   
6477 O  "O5'" . DA  C 2   ? 1.8054 1.8340 1.7764 -0.0271 -0.0044 -0.0572 2   DA  T "O5'" 
6478 C  "C5'" . DA  C 2   ? 1.5956 1.6180 1.5621 -0.0281 -0.0053 -0.0652 2   DA  T "C5'" 
6479 C  "C4'" . DA  C 2   ? 1.5896 1.6031 1.5521 -0.0233 0.0001  -0.0662 2   DA  T "C4'" 
6480 O  "O4'" . DA  C 2   ? 1.6342 1.6408 1.5863 -0.0225 -0.0003 -0.0755 2   DA  T "O4'" 
6481 C  "C3'" . DA  C 2   ? 1.6217 1.6405 1.5814 -0.0176 0.0034  -0.0600 2   DA  T "C3'" 
6482 O  "O3'" . DA  C 2   ? 1.4115 1.4305 1.3804 -0.0172 0.0048  -0.0519 2   DA  T "O3'" 
6483 C  "C2'" . DA  C 2   ? 1.6009 1.6125 1.5534 -0.0124 0.0087  -0.0640 2   DA  T "C2'" 
6484 C  "C1'" . DA  C 2   ? 1.6935 1.6991 1.6364 -0.0155 0.0051  -0.0749 2   DA  T "C1'" 
6485 N  N9    . DA  C 2   ? 1.7814 1.7935 1.7112 -0.0143 0.0018  -0.0781 2   DA  T N9    
6486 C  C8    . DA  C 2   ? 1.4967 1.5212 1.4274 -0.0162 -0.0032 -0.0741 2   DA  T C8    
6487 N  N7    . DA  C 2   ? 1.4064 1.4348 1.3237 -0.0143 -0.0056 -0.0770 2   DA  T N7    
6488 C  C5    . DA  C 2   ? 1.5985 1.6155 1.5030 -0.0107 -0.0015 -0.0843 2   DA  T C5    
6489 C  C6    . DA  C 2   ? 1.6933 1.7070 1.5771 -0.0067 -0.0011 -0.0905 2   DA  T C6    
6490 N  N6    . DA  C 2   ? 1.6495 1.6730 1.5232 -0.0063 -0.0060 -0.0892 2   DA  T N6    
6491 N  N1    . DA  C 2   ? 1.6453 1.6443 1.5179 -0.0026 0.0048  -0.0980 2   DA  T N1    
6492 C  C2    . DA  C 2   ? 1.5560 1.5455 1.4406 -0.0026 0.0097  -0.0981 2   DA  T C2    
6493 N  N3    . DA  C 2   ? 1.6594 1.6521 1.5645 -0.0065 0.0092  -0.0916 2   DA  T N3    
6494 C  C4    . DA  C 2   ? 1.7647 1.7712 1.6775 -0.0104 0.0034  -0.0852 2   DA  T C4    
6495 P  P     . DC  C 3   ? 0.8897 0.9166 0.8600 -0.0153 0.0035  -0.0439 3   DC  T P     
6496 O  OP1   . DC  C 3   ? 0.8069 0.8333 0.7820 -0.0182 0.0012  -0.0394 3   DC  T OP1   
6497 O  OP2   . DC  C 3   ? 0.8355 0.8697 0.7988 -0.0144 0.0015  -0.0458 3   DC  T OP2   
6498 O  "O5'" . DC  C 3   ? 0.9858 1.0111 0.9602 -0.0103 0.0082  -0.0387 3   DC  T "O5'" 
6499 C  "C5'" . DC  C 3   ? 0.7206 0.7484 0.6898 -0.0055 0.0121  -0.0396 3   DC  T "C5'" 
6500 C  "C4'" . DC  C 3   ? 0.9340 0.9640 0.9124 -0.0010 0.0162  -0.0306 3   DC  T "C4'" 
6501 O  "O4'" . DC  C 3   ? 0.7638 0.7981 0.7504 -0.0039 0.0107  -0.0228 3   DC  T "O4'" 
6502 C  "C3'" . DC  C 3   ? 0.7518 0.7748 0.7384 0.0014  0.0212  -0.0289 3   DC  T "C3'" 
6503 O  "O3'" . DC  C 3   ? 0.7025 0.7201 0.6820 0.0068  0.0288  -0.0345 3   DC  T "O3'" 
6504 C  "C2'" . DC  C 3   ? 0.6736 0.7028 0.6740 0.0032  0.0210  -0.0168 3   DC  T "C2'" 
6505 C  "C1'" . DC  C 3   ? 0.6612 0.6949 0.6604 -0.0022 0.0122  -0.0146 3   DC  T "C1'" 
6506 N  N1    . DC  C 3   ? 0.7771 0.8067 0.7799 -0.0067 0.0067  -0.0126 3   DC  T N1    
6507 C  C2    . DC  C 3   ? 0.6935 0.7237 0.7085 -0.0066 0.0044  -0.0033 3   DC  T C2    
6508 O  O2    . DC  C 3   ? 0.7322 0.7671 0.7579 -0.0030 0.0074  0.0036  3   DC  T O2    
6509 N  N3    . DC  C 3   ? 0.7349 0.7610 0.7500 -0.0104 -0.0010 -0.0012 3   DC  T N3    
6510 C  C4    . DC  C 3   ? 0.6197 0.6419 0.6244 -0.0136 -0.0025 -0.0075 3   DC  T C4    
6511 N  N4    . DC  C 3   ? 0.7050 0.7234 0.7083 -0.0165 -0.0066 -0.0043 3   DC  T N4    
6512 C  C5    . DC  C 3   ? 0.6817 0.7043 0.6773 -0.0138 0.0002  -0.0164 3   DC  T C5    
6513 C  C6    . DC  C 3   ? 0.7244 0.7507 0.7189 -0.0106 0.0039  -0.0189 3   DC  T C6    
6514 P  P     . DT  C 4   ? 0.7193 0.7247 0.7026 0.0091  0.0343  -0.0382 4   DT  T P     
6515 O  OP1   . DT  C 4   ? 0.6354 0.6334 0.6048 0.0146  0.0412  -0.0470 4   DT  T OP1   
6516 O  OP2   . DT  C 4   ? 0.8079 0.8084 0.7943 0.0022  0.0283  -0.0409 4   DT  T OP2   
6517 O  "O5'" . DT  C 4   ? 0.8334 0.8424 0.8349 0.0134  0.0386  -0.0255 4   DT  T "O5'" 
6518 C  "C5'" . DT  C 4   ? 0.7093 0.7246 0.7148 0.0205  0.0459  -0.0189 4   DT  T "C5'" 
6519 C  "C4'" . DT  C 4   ? 0.6468 0.6659 0.6743 0.0234  0.0484  -0.0059 4   DT  T "C4'" 
6520 O  "O4'" . DT  C 4   ? 0.7498 0.7751 0.7863 0.0163  0.0375  0.0013  4   DT  T "O4'" 
6521 C  "C3'" . DT  C 4   ? 0.6137 0.6220 0.6482 0.0261  0.0534  -0.0072 4   DT  T "C3'" 
6522 O  "O3'" . DT  C 4   ? 0.6750 0.6786 0.7089 0.0359  0.0663  -0.0082 4   DT  T "O3'" 
6523 C  "C2'" . DT  C 4   ? 0.6420 0.6570 0.6979 0.0237  0.0480  0.0067  4   DT  T "C2'" 
6524 C  "C1'" . DT  C 4   ? 0.6231 0.6467 0.6755 0.0161  0.0364  0.0090  4   DT  T "C1'" 
6525 N  N1    . DT  C 4   ? 0.6785 0.6976 0.7257 0.0085  0.0272  0.0060  4   DT  T N1    
6526 C  C2    . DT  C 4   ? 0.7125 0.7328 0.7719 0.0060  0.0214  0.0155  4   DT  T C2    
6527 O  O2    . DT  C 4   ? 0.7801 0.8054 0.8567 0.0091  0.0224  0.0266  4   DT  T O2    
6528 N  N3    . DT  C 4   ? 0.7073 0.7233 0.7585 -0.0001 0.0145  0.0126  4   DT  T N3    
6529 C  C4    . DT  C 4   ? 0.6583 0.6702 0.6940 -0.0038 0.0132  0.0021  4   DT  T C4    
6530 O  O4    . DT  C 4   ? 0.7517 0.7608 0.7822 -0.0083 0.0084  0.0015  4   DT  T O4    
6531 C  C5    . DT  C 4   ? 0.6680 0.6798 0.6941 -0.0015 0.0181  -0.0072 4   DT  T C5    
6532 C  C7    . DT  C 4   ? 0.6712 0.6804 0.6833 -0.0056 0.0161  -0.0176 4   DT  T C7    
6533 C  C6    . DT  C 4   ? 0.6468 0.6617 0.6774 0.0045  0.0246  -0.0051 4   DT  T C6    
6534 P  P     . DG  C 5   ? 0.7391 0.7251 0.7694 0.0403  0.0741  -0.0171 5   DG  T P     
6535 O  OP1   . DG  C 5   ? 0.6952 0.6760 0.7160 0.0510  0.0877  -0.0210 5   DG  T OP1   
6536 O  OP2   . DG  C 5   ? 0.8436 0.8202 0.8613 0.0320  0.0658  -0.0288 5   DG  T OP2   
6537 O  "O5'" . DG  C 5   ? 0.8419 0.8293 0.8982 0.0417  0.0748  -0.0040 5   DG  T "O5'" 
6538 C  "C5'" . DG  C 5   ? 0.8256 0.8253 0.9025 0.0473  0.0794  0.0114  5   DG  T "C5'" 
6539 C  "C4'" . DG  C 5   ? 0.6732 0.6759 0.7737 0.0452  0.0745  0.0239  5   DG  T "C4'" 
6540 O  "O4'" . DG  C 5   ? 0.6675 0.6742 0.7646 0.0342  0.0595  0.0246  5   DG  T "O4'" 
6541 C  "C3'" . DG  C 5   ? 0.6915 0.6790 0.7968 0.0490  0.0807  0.0207  5   DG  T "C3'" 
6542 O  "O3'" . DG  C 5   ? 0.8260 0.8192 0.9583 0.0548  0.0852  0.0362  5   DG  T "O3'" 
6543 C  "C2'" . DG  C 5   ? 0.7311 0.7135 0.8297 0.0386  0.0688  0.0161  5   DG  T "C2'" 
6544 C  "C1'" . DG  C 5   ? 0.6938 0.6918 0.7954 0.0313  0.0565  0.0247  5   DG  T "C1'" 
6545 N  N9    . DG  C 5   ? 0.7092 0.7048 0.7955 0.0219  0.0462  0.0173  5   DG  T N9    
6546 C  C8    . DG  C 5   ? 0.6876 0.6784 0.7535 0.0186  0.0454  0.0035  5   DG  T C8    
6547 N  N7    . DG  C 5   ? 0.6406 0.6314 0.6991 0.0107  0.0366  0.0011  5   DG  T N7    
6548 C  C5    . DG  C 5   ? 0.6149 0.6096 0.6865 0.0088  0.0312  0.0132  5   DG  T C5    
6549 C  C6    . DG  C 5   ? 0.5756 0.5713 0.6439 0.0021  0.0222  0.0167  5   DG  T C6    
6550 O  O6    . DG  C 5   ? 0.7165 0.7106 0.7716 -0.0032 0.0182  0.0100  5   DG  T O6    
6551 N  N1    . DG  C 5   ? 0.7078 0.7073 0.7901 0.0024  0.0180  0.0301  5   DG  T N1    
6552 C  C2    . DG  C 5   ? 0.6545 0.6578 0.7555 0.0082  0.0218  0.0400  5   DG  T C2    
6553 N  N2    . DG  C 5   ? 0.7039 0.7117 0.8177 0.0070  0.0152  0.0535  5   DG  T N2    
6554 N  N3    . DG  C 5   ? 0.6124 0.6154 0.7189 0.0151  0.0318  0.0375  5   DG  T N3    
6555 C  C4    . DG  C 5   ? 0.6366 0.6346 0.7260 0.0151  0.0361  0.0235  5   DG  T C4    
6556 P  P     . DT  C 6   ? 0.7773 0.7560 0.9213 0.0606  0.0930  0.0369  6   DT  T P     
6557 O  OP1   . DT  C 6   ? 0.8276 0.8134 0.9967 0.0714  0.1039  0.0513  6   DT  T OP1   
6558 O  OP2   . DT  C 6   ? 0.7854 0.7440 0.9065 0.0615  0.0985  0.0179  6   DT  T OP2   
6559 O  "O5'" . DT  C 6   ? 0.6161 0.5973 0.7693 0.0511  0.0791  0.0446  6   DT  T "O5'" 
6560 C  "C5'" . DT  C 6   ? 0.7228 0.7203 0.8962 0.0484  0.0701  0.0623  6   DT  T "C5'" 
6561 C  "C4'" . DT  C 6   ? 0.6908 0.6863 0.8671 0.0408  0.0588  0.0675  6   DT  T "C4'" 
6562 O  "O4'" . DT  C 6   ? 0.7837 0.7763 0.9362 0.0313  0.0498  0.0563  6   DT  T "O4'" 
6563 C  "C3'" . DT  C 6   ? 0.7485 0.7290 0.9326 0.0449  0.0659  0.0669  6   DT  T "C3'" 
6564 O  "O3'" . DT  C 6   ? 0.6609 0.6481 0.8682 0.0454  0.0610  0.0848  6   DT  T "O3'" 
6565 C  "C2'" . DT  C 6   ? 0.7343 0.7035 0.8970 0.0366  0.0606  0.0538  6   DT  T "C2'" 
6566 C  "C1'" . DT  C 6   ? 0.6835 0.6651 0.8328 0.0279  0.0480  0.0537  6   DT  T "C1'" 
6567 N  N1    . DT  C 6   ? 0.7389 0.7136 0.8646 0.0215  0.0455  0.0382  6   DT  T N1    
6568 C  C2    . DT  C 6   ? 0.7742 0.7501 0.8911 0.0133  0.0359  0.0390  6   DT  T C2    
6569 O  O2    . DT  C 6   ? 0.8241 0.8055 0.9483 0.0108  0.0287  0.0511  6   DT  T O2    
6570 N  N3    . DT  C 6   ? 0.6840 0.6548 0.7828 0.0084  0.0350  0.0256  6   DT  T N3    
6571 C  C4    . DT  C 6   ? 0.6594 0.6239 0.7472 0.0101  0.0408  0.0115  6   DT  T C4    
6572 O  O4    . DT  C 6   ? 0.7552 0.7167 0.8290 0.0049  0.0381  0.0013  6   DT  T O4    
6573 C  C5    . DT  C 6   ? 0.6688 0.6308 0.7626 0.0189  0.0503  0.0105  6   DT  T C5    
6574 C  C7    . DT  C 6   ? 0.7644 0.7184 0.8430 0.0219  0.0569  -0.0045 6   DT  T C7    
6575 C  C6    . DT  C 6   ? 0.6617 0.6289 0.7745 0.0245  0.0531  0.0239  6   DT  T C6    
6576 P  P     . DG  C 7   ? 0.7131 0.6874 0.9375 0.0519  0.0695  0.0898  7   DG  T P     
6577 O  OP1   . DG  C 7   ? 0.8452 0.8326 1.0981 0.0547  0.0654  0.1115  7   DG  T OP1   
6578 O  OP2   . DG  C 7   ? 0.6415 0.6004 0.8609 0.0608  0.0857  0.0767  7   DG  T OP2   
6579 O  "O5'" . DG  C 7   ? 0.6832 0.6473 0.8933 0.0429  0.0618  0.0842  7   DG  T "O5'" 
6580 C  "C5'" . DG  C 7   ? 0.8455 0.8201 1.0515 0.0340  0.0470  0.0930  7   DG  T "C5'" 
6581 C  "C4'" . DG  C 7   ? 0.9342 0.8985 1.1239 0.0267  0.0433  0.0855  7   DG  T "C4'" 
6582 O  "O4'" . DG  C 7   ? 0.8619 0.8234 1.0282 0.0220  0.0429  0.0686  7   DG  T "O4'" 
6583 C  "C3'" . DG  C 7   ? 0.8495 0.7961 1.0474 0.0300  0.0525  0.0824  7   DG  T "C3'" 
6584 O  "O3'" . DG  C 7   ? 0.8936 0.8418 1.1094 0.0309  0.0495  0.0996  7   DG  T "O3'" 
6585 C  "C2'" . DG  C 7   ? 0.8324 0.7704 1.0093 0.0219  0.0502  0.0683  7   DG  T "C2'" 
6586 C  "C1'" . DG  C 7   ? 0.8042 0.7547 0.9618 0.0168  0.0427  0.0621  7   DG  T "C1'" 
6587 N  N9    . DG  C 7   ? 0.7327 0.6762 0.8729 0.0144  0.0459  0.0438  7   DG  T N9    
6588 C  C8    . DG  C 7   ? 0.7316 0.6700 0.8671 0.0196  0.0535  0.0324  7   DG  T C8    
6589 N  N7    . DG  C 7   ? 0.6181 0.5512 0.7362 0.0153  0.0530  0.0174  7   DG  T N7    
6590 C  C5    . DG  C 7   ? 0.7562 0.6915 0.8695 0.0070  0.0454  0.0196  7   DG  T C5    
6591 C  C6    . DG  C 7   ? 0.7047 0.6380 0.8042 -0.0003 0.0417  0.0092  7   DG  T C6    
6592 O  O6    . DG  C 7   ? 0.6804 0.6092 0.7681 -0.0015 0.0428  -0.0046 7   DG  T O6    
6593 N  N1    . DG  C 7   ? 0.6182 0.5559 0.7183 -0.0061 0.0362  0.0173  7   DG  T N1    
6594 C  C2    . DG  C 7   ? 0.7195 0.6618 0.8290 -0.0053 0.0336  0.0329  7   DG  T C2    
6595 N  N2    . DG  C 7   ? 0.6953 0.6409 0.8006 -0.0107 0.0293  0.0390  7   DG  T N2    
6596 N  N3    . DG  C 7   ? 0.8420 0.7865 0.9646 0.0007  0.0353  0.0427  7   DG  T N3    
6597 C  C4    . DG  C 7   ? 0.7478 0.6889 0.8729 0.0067  0.0416  0.0355  7   DG  T C4    
6598 P  P     . DG  C 8   ? 0.8517 0.7819 1.0794 0.0331  0.0569  0.1008  8   DG  T P     
6599 O  OP1   . DG  C 8   ? 0.8383 0.7735 1.0916 0.0386  0.0566  0.1212  8   DG  T OP1   
6600 O  OP2   . DG  C 8   ? 0.7587 0.6714 0.9819 0.0372  0.0685  0.0830  8   DG  T OP2   
6601 O  "O5'" . DG  C 8   ? 0.7015 0.6307 0.9139 0.0229  0.0489  0.0999  8   DG  T "O5'" 
6602 C  "C5'" . DG  C 8   ? 0.7514 0.6953 0.9562 0.0175  0.0370  0.1118  8   DG  T "C5'" 
6603 C  "C4'" . DG  C 8   ? 0.8241 0.7641 1.0157 0.0100  0.0336  0.1110  8   DG  T "C4'" 
6604 O  "O4'" . DG  C 8   ? 0.9313 0.8681 1.1040 0.0051  0.0348  0.0931  8   DG  T "O4'" 
6605 C  "C3'" . DG  C 8   ? 0.7806 0.7067 0.9874 0.0108  0.0401  0.1161  8   DG  T "C3'" 
6606 O  "O3'" . DG  C 8   ? 0.6554 0.5856 0.8556 0.0055  0.0346  0.1271  8   DG  T "O3'" 
6607 C  "C2'" . DG  C 8   ? 0.7794 0.6910 0.9806 0.0089  0.0474  0.0964  8   DG  T "C2'" 
6608 C  "C1'" . DG  C 8   ? 0.7948 0.7165 0.9718 0.0032  0.0415  0.0855  8   DG  T "C1'" 
6609 N  N9    . DG  C 8   ? 0.7712 0.6858 0.9400 0.0035  0.0460  0.0663  8   DG  T N9    
6610 C  C8    . DG  C 8   ? 0.7772 0.6858 0.9514 0.0106  0.0526  0.0590  8   DG  T C8    
6611 N  N7    . DG  C 8   ? 0.7065 0.6092 0.8673 0.0092  0.0548  0.0417  8   DG  T N7    
6612 C  C5    . DG  C 8   ? 0.7689 0.6751 0.9176 0.0004  0.0489  0.0377  8   DG  T C5    
6613 C  C6    . DG  C 8   ? 0.8269 0.7307 0.9604 -0.0049 0.0473  0.0222  8   DG  T C6    
6614 O  O6    . DG  C 8   ? 0.8453 0.7428 0.9704 -0.0031 0.0500  0.0079  8   DG  T O6    
6615 N  N1    . DG  C 8   ? 0.9061 0.8164 1.0342 -0.0126 0.0420  0.0251  8   DG  T N1    
6616 C  C2    . DG  C 8   ? 0.8573 0.7742 0.9904 -0.0145 0.0394  0.0406  8   DG  T C2    
6617 N  N2    . DG  C 8   ? 0.8939 0.8163 1.0195 -0.0210 0.0363  0.0416  8   DG  T N2    
6618 N  N3    . DG  C 8   ? 0.7934 0.7118 0.9378 -0.0099 0.0399  0.0548  8   DG  T N3    
6619 C  C4    . DG  C 8   ? 0.8075 0.7208 0.9607 -0.0028 0.0444  0.0527  8   DG  T C4    
6620 P  P     . DC  C 9   ? 0.8759 0.7959 1.0941 0.0061  0.0389  0.1402  9   DC  T P     
6621 O  OP1   . DC  C 9   ? 0.9504 0.8819 1.1611 0.0037  0.0307  0.1580  9   DC  T OP1   
6622 O  OP2   . DC  C 9   ? 0.8932 0.8028 1.1363 0.0140  0.0467  0.1426  9   DC  T OP2   
6623 O  "O5'" . DC  C 9   ? 0.9413 0.8496 1.1539 -0.0001 0.0440  0.1272  9   DC  T "O5'" 
6624 C  "C5'" . DC  C 9   ? 0.8223 0.7385 1.0134 -0.0070 0.0398  0.1220  9   DC  T "C5'" 
6625 C  "C4'" . DC  C 9   ? 0.9418 0.8471 1.1329 -0.0121 0.0446  0.1069  9   DC  T "C4'" 
6626 O  "O4'" . DC  C 9   ? 0.9558 0.8574 1.1406 -0.0108 0.0458  0.0885  9   DC  T "O4'" 
6627 C  "C3'" . DC  C 9   ? 0.9138 0.8017 1.1275 -0.0123 0.0513  0.1095  9   DC  T "C3'" 
6628 O  "O3'" . DC  C 9   ? 0.7640 0.6533 0.9802 -0.0180 0.0516  0.1197  9   DC  T "O3'" 
6629 C  "C2'" . DC  C 9   ? 0.8684 0.7426 1.0819 -0.0139 0.0546  0.0878  9   DC  T "C2'" 
6630 C  "C1'" . DC  C 9   ? 0.7374 0.6243 0.9282 -0.0145 0.0501  0.0761  9   DC  T "C1'" 
6631 N  N1    . DC  C 9   ? 0.7284 0.6067 0.9159 -0.0106 0.0529  0.0591  9   DC  T N1    
6632 C  C2    . DC  C 9   ? 0.8962 0.7713 1.0712 -0.0154 0.0516  0.0414  9   DC  T C2    
6633 O  O2    . DC  C 9   ? 0.9577 0.8380 1.1275 -0.0228 0.0481  0.0406  9   DC  T O2    
6634 N  N3    . DC  C 9   ? 0.8212 0.6881 0.9900 -0.0112 0.0544  0.0265  9   DC  T N3    
6635 C  C4    . DC  C 9   ? 0.8001 0.6622 0.9760 -0.0021 0.0598  0.0290  9   DC  T C4    
6636 N  N4    . DC  C 9   ? 0.8768 0.7307 1.0443 0.0027  0.0640  0.0144  9   DC  T N4    
6637 C  C5    . DC  C 9   ? 0.8007 0.6670 0.9929 0.0029  0.0614  0.0475  9   DC  T C5    
6638 C  C6    . DC  C 9   ? 0.8359 0.7100 1.0327 -0.0019 0.0572  0.0620  9   DC  T C6    
6639 P  P     . DC  C 10  ? 0.8353 0.7077 1.0769 -0.0200 0.0576  0.1258  10  DC  T P     
6640 O  OP1   . DC  C 10  ? 0.8590 0.7396 1.1028 -0.0224 0.0575  0.1459  10  DC  T OP1   
6641 O  OP2   . DC  C 10  ? 0.9662 0.8243 1.2254 -0.0129 0.0617  0.1249  10  DC  T OP2   
6642 O  "O5'" . DC  C 10  ? 0.9281 0.7914 1.1691 -0.0276 0.0584  0.1074  10  DC  T "O5'" 
6643 C  "C5'" . DC  C 10  ? 0.9251 0.8009 1.1522 -0.0341 0.0556  0.1050  10  DC  T "C5'" 
6644 C  "C4'" . DC  C 10  ? 0.9996 0.8649 1.2350 -0.0418 0.0559  0.0912  10  DC  T "C4'" 
6645 O  "O4'" . DC  C 10  ? 0.8988 0.7572 1.1243 -0.0407 0.0537  0.0700  10  DC  T "O4'" 
6646 C  "C3'" . DC  C 10  ? 0.9910 0.8371 1.2534 -0.0448 0.0596  0.0952  10  DC  T "C3'" 
6647 O  "O3'" . DC  C 10  ? 1.0301 0.8745 1.3009 -0.0544 0.0583  0.0909  10  DC  T "O3'" 
6648 C  "C2'" . DC  C 10  ? 0.8440 0.6713 1.1085 -0.0403 0.0604  0.0789  10  DC  T "C2'" 
6649 C  "C1'" . DC  C 10  ? 0.9010 0.7365 1.1421 -0.0413 0.0559  0.0608  10  DC  T "C1'" 
6650 N  N1    . DC  C 10  ? 1.0339 0.8618 1.2655 -0.0334 0.0573  0.0483  10  DC  T N1    
6651 C  C2    . DC  C 10  ? 1.0044 0.8284 1.2208 -0.0349 0.0544  0.0277  10  DC  T C2    
6652 O  O2    . DC  C 10  ? 1.0082 0.8354 1.2206 -0.0433 0.0497  0.0203  10  DC  T O2    
6653 N  N3    . DC  C 10  ? 0.9720 0.7895 1.1790 -0.0269 0.0573  0.0176  10  DC  T N3    
6654 C  C4    . DC  C 10  ? 0.9336 0.7495 1.1488 -0.0177 0.0627  0.0276  10  DC  T C4    
6655 N  N4    . DC  C 10  ? 0.9331 0.7438 1.1405 -0.0092 0.0668  0.0183  10  DC  T N4    
6656 C  C5    . DC  C 10  ? 0.8114 0.6318 1.0437 -0.0164 0.0644  0.0487  10  DC  T C5    
6657 C  C6    . DC  C 10  ? 0.9657 0.7916 1.2042 -0.0244 0.0616  0.0581  10  DC  T C6    
6658 P  P     . DG  C 11  ? 0.9120 0.7466 1.2119 -0.0603 0.0618  0.1050  11  DG  T P     
6659 O  OP1   . DG  C 11  ? 1.0333 0.8877 1.3305 -0.0614 0.0644  0.1248  11  DG  T OP1   
6660 O  OP2   . DG  C 11  ? 0.9703 0.7851 1.2870 -0.0552 0.0652  0.1086  11  DG  T OP2   
6661 O  "O5'" . DG  C 11  ? 1.1251 0.9496 1.4348 -0.0707 0.0573  0.0888  11  DG  T "O5'" 
6662 C  "C5'" . DG  C 11  ? 0.9080 0.7474 1.2027 -0.0753 0.0528  0.0789  11  DG  T "C5'" 
6663 C  "C4'" . DG  C 11  ? 0.9063 0.7309 1.1992 -0.0804 0.0462  0.0553  11  DG  T "C4'" 
6664 O  "O4'" . DG  C 11  ? 0.9613 0.7761 1.2366 -0.0720 0.0461  0.0416  11  DG  T "O4'" 
6665 C  "C3'" . DG  C 11  ? 1.0558 0.8573 1.3751 -0.0885 0.0439  0.0514  11  DG  T "C3'" 
6666 O  "O3'" . DG  C 11  ? 0.9304 0.7304 1.2502 -0.0981 0.0355  0.0364  11  DG  T "O3'" 
6667 C  "C2'" . DG  C 11  ? 1.0741 0.8515 1.3905 -0.0811 0.0460  0.0409  11  DG  T "C2'" 
6668 C  "C1'" . DG  C 11  ? 1.0201 0.8075 1.3058 -0.0733 0.0451  0.0288  11  DG  T "C1'" 
6669 N  N9    . DG  C 11  ? 1.0811 0.8584 1.3607 -0.0619 0.0507  0.0277  11  DG  T N9    
6670 C  C8    . DG  C 11  ? 0.9891 0.7663 1.2806 -0.0551 0.0572  0.0456  11  DG  T C8    
6671 N  N7    . DG  C 11  ? 1.1156 0.8843 1.4010 -0.0450 0.0614  0.0412  11  DG  T N7    
6672 C  C5    . DG  C 11  ? 1.1243 0.8863 1.3906 -0.0448 0.0582  0.0188  11  DG  T C5    
6673 C  C6    . DG  C 11  ? 1.0526 0.8049 1.3050 -0.0352 0.0619  0.0058  11  DG  T C6    
6674 O  O6    . DG  C 11  ? 1.1254 0.8735 1.3822 -0.0248 0.0688  0.0121  11  DG  T O6    
6675 N  N1    . DG  C 11  ? 1.0025 0.7509 1.2349 -0.0382 0.0570  -0.0152 11  DG  T N1    
6676 C  C2    . DG  C 11  ? 1.0327 0.7865 1.2609 -0.0495 0.0485  -0.0225 11  DG  T C2    
6677 N  N2    . DG  C 11  ? 0.9830 0.7323 1.1905 -0.0507 0.0438  -0.0424 11  DG  T N2    
6678 N  N3    . DG  C 11  ? 1.1246 0.8884 1.3687 -0.0585 0.0452  -0.0101 11  DG  T N3    
6679 C  C4    . DG  C 11  ? 1.0827 0.8498 1.3445 -0.0553 0.0509  0.0101  11  DG  T C4    
6680 P  P     . DT  C 12  ? 0.9587 0.7377 1.3069 -0.1100 0.0298  0.0318  12  DT  T P     
6681 O  OP1   . DT  C 12  ? 1.0294 0.8251 1.3868 -0.1207 0.0236  0.0334  12  DT  T OP1   
6682 O  OP2   . DT  C 12  ? 0.9350 0.7015 1.3077 -0.1087 0.0366  0.0483  12  DT  T OP2   
6683 O  "O5'" . DT  C 12  ? 1.0170 0.7696 1.3501 -0.1090 0.0235  0.0049  12  DT  T "O5'" 
6684 C  "C5'" . DT  C 12  ? 1.0796 0.8389 1.3806 -0.1025 0.0216  -0.0104 12  DT  T "C5'" 
6685 C  "C4'" . DT  C 12  ? 1.1047 0.8351 1.3929 -0.1006 0.0178  -0.0338 12  DT  T "C4'" 
6686 O  "O4'" . DT  C 12  ? 1.0178 0.7411 1.2925 -0.0867 0.0271  -0.0343 12  DT  T "O4'" 
6687 C  "C3'" . DT  C 12  ? 1.0858 0.7859 1.3969 -0.1088 0.0135  -0.0396 12  DT  T "C3'" 
6688 O  "O3'" . DT  C 12  ? 1.1720 0.8537 1.4690 -0.1146 0.0028  -0.0639 12  DT  T "O3'" 
6689 C  "C2'" . DT  C 12  ? 1.1298 0.8103 1.4447 -0.0977 0.0240  -0.0358 12  DT  T "C2'" 
6690 C  "C1'" . DT  C 12  ? 1.0828 0.7735 1.3668 -0.0849 0.0292  -0.0426 12  DT  T "C1'" 
6691 N  N1    . DT  C 12  ? 1.1219 0.8104 1.4093 -0.0720 0.0410  -0.0306 12  DT  T N1    
6692 C  C2    . DT  C 12  ? 1.1052 0.7840 1.3725 -0.0601 0.0466  -0.0421 12  DT  T C2    
6693 O  O2    . DT  C 12  ? 0.9683 0.6396 1.2123 -0.0591 0.0430  -0.0621 12  DT  T O2    
6694 N  N3    . DT  C 12  ? 1.0595 0.7387 1.3354 -0.0489 0.0568  -0.0282 12  DT  T N3    
6695 C  C4    . DT  C 12  ? 1.1173 0.8046 1.4171 -0.0487 0.0610  -0.0046 12  DT  T C4    
6696 O  O4    . DT  C 12  ? 1.1917 0.8796 1.4984 -0.0383 0.0691  0.0075  12  DT  T O4    
6697 C  C5    . DT  C 12  ? 1.1041 0.8004 1.4213 -0.0611 0.0554  0.0062  12  DT  T C5    
6698 C  C7    . DT  C 12  ? 1.0461 0.7519 1.3875 -0.0614 0.0601  0.0327  12  DT  T C7    
6699 C  C6    . DT  C 12  ? 1.0612 0.7579 1.3725 -0.0720 0.0462  -0.0070 12  DT  T C6    
6700 P  P     . DG  C 13  ? 1.3628 1.0195 1.6833 -0.1293 -0.0085 -0.0720 13  DG  T P     
6701 O  OP1   . DG  C 13  ? 1.3191 0.9919 1.6392 -0.1414 -0.0217 -0.0771 13  DG  T OP1   
6702 O  OP2   . DG  C 13  ? 1.1127 0.7627 1.4675 -0.1313 -0.0020 -0.0526 13  DG  T OP2   
6703 O  "O5'" . DG  C 13  ? 1.2563 0.8744 1.5560 -0.1245 -0.0105 -0.0978 13  DG  T "O5'" 
6704 C  "C5'" . DG  C 13  ? 1.1373 0.7525 1.4014 -0.1217 -0.0165 -0.1196 13  DG  T "C5'" 
6705 C  "C4'" . DG  C 13  ? 1.2222 0.8088 1.4633 -0.1083 -0.0081 -0.1351 13  DG  T "C4'" 
6706 O  "O4'" . DG  C 13  ? 1.2131 0.8137 1.4563 -0.0943 0.0077  -0.1185 13  DG  T "O4'" 
6707 C  "C3'" . DG  C 13  ? 1.3111 0.8559 1.5656 -0.1112 -0.0094 -0.1453 13  DG  T "C3'" 
6708 O  "O3'" . DG  C 13  ? 1.5265 1.0450 1.7597 -0.1181 -0.0228 -0.1722 13  DG  T "O3'" 
6709 C  "C2'" . DG  C 13  ? 1.3142 0.8453 1.5615 -0.0935 0.0077  -0.1436 13  DG  T "C2'" 
6710 C  "C1'" . DG  C 13  ? 1.2581 0.8285 1.5048 -0.0849 0.0173  -0.1226 13  DG  T "C1'" 
6711 N  N9    . DG  C 13  ? 1.1881 0.7669 1.4656 -0.0822 0.0265  -0.0977 13  DG  T N9    
6712 C  C8    . DG  C 13  ? 1.1892 0.7787 1.4984 -0.0932 0.0228  -0.0795 13  DG  T C8    
6713 N  N7    . DG  C 13  ? 1.1463 0.7416 1.4759 -0.0869 0.0332  -0.0582 13  DG  T N7    
6714 C  C5    . DG  C 13  ? 1.2318 0.8204 1.5442 -0.0712 0.0436  -0.0626 13  DG  T C5    
6715 C  C6    . DG  C 13  ? 1.2228 0.8145 1.5465 -0.0589 0.0561  -0.0454 13  DG  T C6    
6716 O  O6    . DG  C 13  ? 1.1719 0.7723 1.5213 -0.0594 0.0602  -0.0225 13  DG  T O6    
6717 N  N1    . DG  C 13  ? 1.1039 0.6882 1.4063 -0.0447 0.0642  -0.0559 13  DG  T N1    
6718 C  C2    . DG  C 13  ? 1.1354 0.7100 1.4069 -0.0421 0.0615  -0.0800 13  DG  T C2    
6719 N  N2    . DG  C 13  ? 1.1287 0.6981 1.3842 -0.0269 0.0721  -0.0854 13  DG  T N2    
6720 N  N3    . DG  C 13  ? 1.0963 0.6673 1.3542 -0.0535 0.0493  -0.0965 13  DG  T N3    
6721 C  C4    . DG  C 13  ? 1.2023 0.7810 1.4831 -0.0679 0.0404  -0.0866 13  DG  T C4    
6722 P  P     . DG  C 14  ? 1.3851 0.8828 1.5725 -0.1054 -0.0192 -0.1973 14  DG  T P     
6723 O  OP1   . DG  C 14  ? 1.4336 0.9626 1.6010 -0.0928 -0.0088 -0.1893 14  DG  T OP1   
6724 O  OP2   . DG  C 14  ? 1.5842 1.0625 1.7537 -0.1173 -0.0376 -0.2205 14  DG  T OP2   
6725 O  "O5'" . DG  C 14  ? 1.3934 0.8521 1.5852 -0.0945 -0.0067 -0.2029 14  DG  T "O5'" 
6726 C  "C5'" . DG  C 14  ? 1.4662 0.8944 1.6223 -0.0828 -0.0015 -0.2264 14  DG  T "C5'" 
6727 C  "C4'" . DG  C 14  ? 1.3638 0.7952 1.5156 -0.0625 0.0201  -0.2172 14  DG  T "C4'" 
6728 O  "O4'" . DG  C 14  ? 1.2324 0.6911 1.4200 -0.0619 0.0276  -0.1879 14  DG  T "O4'" 
6729 C  "C3'" . DG  C 14  ? 1.5139 0.9004 1.6608 -0.0514 0.0307  -0.2309 14  DG  T "C3'" 
6730 O  "O3'" . DG  C 14  ? 1.4828 0.8657 1.5968 -0.0333 0.0444  -0.2405 14  DG  T "O3'" 
6731 C  "C2'" . DG  C 14  ? 1.4632 0.8525 1.6524 -0.0484 0.0411  -0.2066 14  DG  T "C2'" 
6732 C  "C1'" . DG  C 14  ? 1.1705 0.6102 1.3720 -0.0491 0.0430  -0.1813 14  DG  T "C1'" 
6733 N  N9    . DG  C 14  ? 1.1898 0.6427 1.4329 -0.0547 0.0446  -0.1555 14  DG  T N9    
6734 C  C8    . DG  C 14  ? 1.2739 0.7344 1.5428 -0.0718 0.0323  -0.1463 14  DG  T C8    
6735 N  N7    . DG  C 14  ? 1.3280 0.8003 1.6305 -0.0721 0.0383  -0.1214 14  DG  T N7    
6736 C  C5    . DG  C 14  ? 1.2358 0.7082 1.5353 -0.0546 0.0542  -0.1138 14  DG  T C5    
6737 C  C6    . DG  C 14  ? 1.2867 0.7695 1.6132 -0.0471 0.0654  -0.0883 14  DG  T C6    
6738 O  O6    . DG  C 14  ? 1.3386 0.8324 1.6957 -0.0542 0.0641  -0.0670 14  DG  T O6    
6739 N  N1    . DG  C 14  ? 1.3403 0.8209 1.6560 -0.0291 0.0793  -0.0878 14  DG  T N1    
6740 C  C2    . DG  C 14  ? 1.3177 0.7873 1.6004 -0.0191 0.0835  -0.1088 14  DG  T C2    
6741 N  N2    . DG  C 14  ? 1.3934 0.8642 1.6739 -0.0017 0.0984  -0.1027 14  DG  T N2    
6742 N  N3    . DG  C 14  ? 1.2430 0.7019 1.4974 -0.0255 0.0739  -0.1330 14  DG  T N3    
6743 C  C4    . DG  C 14  ? 1.2644 0.7253 1.5291 -0.0436 0.0587  -0.1342 14  DG  T C4    
6744 P  P     . DT  C 15  ? 1.6448 0.9772 1.7282 -0.0229 0.0503  -0.2688 15  DT  T P     
6745 O  OP1   . DT  C 15  ? 1.6884 1.0294 1.7303 -0.0094 0.0584  -0.2794 15  DT  T OP1   
6746 O  OP2   . DT  C 15  ? 1.4684 0.7683 1.5516 -0.0396 0.0317  -0.2873 15  DT  T OP2   
6747 O  "O5'" . DT  C 15  ? 1.4637 0.7772 1.5743 -0.0093 0.0690  -0.2571 15  DT  T "O5'" 
6748 C  "C5'" . DT  C 15  ? 1.3844 0.7304 1.5171 0.0017  0.0836  -0.2304 15  DT  T "C5'" 
6749 C  "C4'" . DT  C 15  ? 1.3031 0.6265 1.4668 0.0109  0.0971  -0.2198 15  DT  T "C4'" 
6750 O  "O4'" . DT  C 15  ? 1.4219 0.7743 1.6269 0.0039  0.0954  -0.1904 15  DT  T "O4'" 
6751 C  "C3'" . DT  C 15  ? 1.4010 0.6739 1.5691 0.0048  0.0916  -0.2382 15  DT  T "C3'" 
6752 O  "O3'" . DT  C 15  ? 1.6790 0.9130 1.8111 0.0186  0.1008  -0.2647 15  DT  T "O3'" 
6753 C  "C2'" . DT  C 15  ? 1.4655 0.7352 1.6801 0.0075  0.1003  -0.2149 15  DT  T "C2'" 
6754 C  "C1'" . DT  C 15  ? 1.3512 0.6747 1.5879 0.0028  0.0985  -0.1849 15  DT  T "C1'" 
6755 N  N1    . DT  C 15  ? 1.4094 0.7452 1.6754 -0.0173 0.0833  -0.1718 15  DT  T N1    
6756 C  C2    . DT  C 15  ? 1.4237 0.7817 1.7274 -0.0178 0.0878  -0.1420 15  DT  T C2    
6757 O  O2    . DT  C 15  ? 1.6366 1.0045 1.9516 -0.0035 0.1022  -0.1256 15  DT  T O2    
6758 N  N3    . DT  C 15  ? 1.3974 0.7662 1.7254 -0.0358 0.0748  -0.1309 15  DT  T N3    
6759 C  C4    . DT  C 15  ? 1.3364 0.6975 1.6585 -0.0534 0.0575  -0.1457 15  DT  T C4    
6760 O  O4    . DT  C 15  ? 1.2864 0.6600 1.6351 -0.0684 0.0478  -0.1322 15  DT  T O4    
6761 C  C5    . DT  C 15  ? 1.3831 0.7211 1.6658 -0.0526 0.0516  -0.1771 15  DT  T C5    
6762 C  C7    . DT  C 15  ? 1.4079 0.7365 1.6817 -0.0714 0.0310  -0.1947 15  DT  T C7    
6763 C  C6    . DT  C 15  ? 1.3626 0.6887 1.6178 -0.0345 0.0650  -0.1888 15  DT  T C6    
6764 P  P     . DC  C 16  ? 1.3664 0.5834 1.5002 0.0437  0.1268  -0.2611 16  DC  T P     
6765 O  OP1   . DC  C 16  ? 1.4470 0.7097 1.6001 0.0536  0.1388  -0.2323 16  DC  T OP1   
6766 O  OP2   . DC  C 16  ? 1.3628 0.5459 1.4486 0.0546  0.1324  -0.2915 16  DC  T OP2   
6767 O  "O5'" . DC  C 16  ? 1.3227 0.5028 1.4926 0.0422  0.1295  -0.2574 16  DC  T "O5'" 
6768 C  "C5'" . DC  C 16  ? 1.4269 0.5842 1.6082 0.0625  0.1512  -0.2534 16  DC  T "C5'" 
6769 C  "C4'" . DC  C 16  ? 1.4753 0.6451 1.7100 0.0615  0.1556  -0.2229 16  DC  T "C4'" 
6770 O  "O4'" . DC  C 16  ? 1.3507 0.5512 1.6070 0.0401  0.1370  -0.2075 16  DC  T "O4'" 
6771 C  "C3'" . DC  C 16  ? 1.4470 0.5673 1.7043 0.0640  0.1607  -0.2286 16  DC  T "C3'" 
6772 O  "O3'" . DC  C 16  ? 1.6077 0.7390 1.9045 0.0765  0.1763  -0.2007 16  DC  T "O3'" 
6773 C  "C2'" . DC  C 16  ? 1.3704 0.4851 1.6456 0.0389  0.1382  -0.2295 16  DC  T "C2'" 
6774 C  "C1'" . DC  C 16  ? 1.4271 0.6011 1.7161 0.0290  0.1301  -0.2038 16  DC  T "C1'" 
6775 N  N1    . DC  C 16  ? 1.4911 0.6749 1.7812 0.0048  0.1070  -0.2081 16  DC  T N1    
6776 C  C2    . DC  C 16  ? 1.4760 0.6947 1.8019 -0.0080 0.0995  -0.1803 16  DC  T C2    
6777 O  O2    . DC  C 16  ? 1.5910 0.8311 1.9444 0.0005  0.1109  -0.1532 16  DC  T O2    
6778 N  N3    . DC  C 16  ? 1.4493 0.6777 1.7782 -0.0291 0.0800  -0.1832 16  DC  T N3    
6779 C  C4    . DC  C 16  ? 1.4148 0.6202 1.7140 -0.0382 0.0664  -0.2121 16  DC  T C4    
6780 N  N4    . DC  C 16  ? 1.2572 0.4752 1.5643 -0.0591 0.0469  -0.2123 16  DC  T N4    
6781 C  C5    . DC  C 16  ? 1.5056 0.6743 1.7653 -0.0259 0.0724  -0.2415 16  DC  T C5    
6782 C  C6    . DC  C 16  ? 1.4842 0.6430 1.7403 -0.0043 0.0936  -0.2385 16  DC  T C6    
6783 MG MG    . MG  D .   ? 1.0539 1.0483 1.0568 -0.0580 -0.1421 0.0646  801 MG  A MG    
6784 MG MG    . MG  E .   ? 0.6999 0.7611 0.8534 -0.0398 -0.1070 0.1182  802 MG  A MG    
6785 MG MG    . MG  F .   ? 0.8824 0.9238 0.9870 -0.0384 -0.1070 0.1107  803 MG  A MG    
6786 N  N1    . XG4 G .   ? 0.6426 0.6710 0.6811 -0.0104 -0.0072 0.0173  804 XG4 A N1    
6787 C  C2    . XG4 G .   ? 0.6061 0.6406 0.6601 -0.0056 -0.0019 0.0240  804 XG4 A C2    
6788 N  N2    . XG4 G .   ? 0.7194 0.7566 0.7709 -0.0007 0.0073  0.0193  804 XG4 A N2    
6789 N  N3    . XG4 G .   ? 0.6247 0.6637 0.6977 -0.0051 -0.0055 0.0368  804 XG4 A N3    
6790 C  C4    . XG4 G .   ? 0.6219 0.6581 0.6952 -0.0101 -0.0161 0.0422  804 XG4 A C4    
6791 C  C5    . XG4 G .   ? 0.6250 0.6542 0.6802 -0.0143 -0.0209 0.0355  804 XG4 A C5    
6792 C  C6    . XG4 G .   ? 0.6282 0.6536 0.6663 -0.0143 -0.0156 0.0226  804 XG4 A C6    
6793 O  O6    . XG4 G .   ? 0.7897 0.8101 0.8141 -0.0173 -0.0183 0.0178  804 XG4 A O6    
6794 N  N7    . XG4 G .   ? 0.6465 0.6742 0.7036 -0.0175 -0.0300 0.0430  804 XG4 A N7    
6795 C  C8    . XG4 G .   ? 0.6984 0.7330 0.7769 -0.0160 -0.0321 0.0548  804 XG4 A C8    
6796 N  N9    . XG4 G .   ? 0.7244 0.7643 0.8134 -0.0111 -0.0225 0.0542  804 XG4 A N9    
6797 P  PA    . XG4 G .   ? 1.1540 1.1894 1.2367 -0.0349 -0.0843 0.0798  804 XG4 A PA    
6798 P  PB    . XG4 G .   ? 1.0903 1.1204 1.1705 -0.0500 -0.1222 0.0877  804 XG4 A PB    
6799 P  PG    . XG4 G .   ? 1.2886 1.3184 1.3721 -0.0586 -0.1531 0.1078  804 XG4 A PG    
6800 C  "C1'" . XG4 G .   ? 0.6656 0.7140 0.7799 -0.0092 -0.0244 0.0684  804 XG4 A "C1'" 
6801 O  O1A   . XG4 G .   ? 1.0840 1.1207 1.1736 -0.0350 -0.0897 0.0904  804 XG4 A O1A   
6802 O  O1B   . XG4 G .   ? 1.2070 1.2236 1.2523 -0.0502 -0.1229 0.0776  804 XG4 A O1B   
6803 O  O1G   . XG4 G .   ? 1.3668 1.3806 1.4176 -0.0637 -0.1630 0.0947  804 XG4 A O1G   
6804 C  "C2'" . XG4 G .   ? 0.5588 0.6154 0.6822 -0.0116 -0.0302 0.0734  804 XG4 A "C2'" 
6805 O  O2A   . XG4 G .   ? 0.9342 0.9583 0.9858 -0.0352 -0.0810 0.0661  804 XG4 A O2A   
6806 O  O2B   . XG4 G .   ? 1.0074 1.0339 1.0875 -0.0553 -0.1316 0.0845  804 XG4 A O2B   
6807 O  O2G   . XG4 G .   ? 0.9542 0.9939 1.0652 -0.0637 -0.1697 0.1247  804 XG4 A O2G   
6808 C  "C3'" . XG4 G .   ? 0.6068 0.6631 0.7317 -0.0181 -0.0451 0.0793  804 XG4 A "C3'" 
6809 O  "O3'" . XG4 G .   ? 0.5982 0.6639 0.7437 -0.0205 -0.0519 0.0898  804 XG4 A "O3'" 
6810 N  N3A   . XG4 G .   ? 0.8172 0.8555 0.9099 -0.0412 -0.0992 0.0848  804 XG4 A N3A   
6811 O  O3B   . XG4 G .   ? 1.1826 1.2217 1.2867 -0.0523 -0.1337 0.1051  804 XG4 A O3B   
6812 O  O3G   . XG4 G .   ? 1.0811 1.1081 1.1506 -0.0534 -0.1431 0.1066  804 XG4 A O3G   
6813 C  "C4'" . XG4 G .   ? 0.6582 0.7149 0.7940 -0.0166 -0.0460 0.0878  804 XG4 A "C4'" 
6814 O  "O4'" . XG4 G .   ? 0.6610 0.7091 0.7806 -0.0125 -0.0342 0.0767  804 XG4 A "O4'" 
6815 C  "C5'" . XG4 G .   ? 0.7634 0.8161 0.8911 -0.0233 -0.0618 0.0912  804 XG4 A "C5'" 
6816 O  "O5'" . XG4 G .   ? 0.8473 0.8908 0.9479 -0.0276 -0.0666 0.0792  804 XG4 A "O5'" 
6817 MG MG    . MG  H .   ? 0.8583 0.9566 0.8760 0.0160  -0.0053 -0.0043 805 MG  A MG    
6818 MG MG    . MG  I .   ? 0.9111 1.0398 0.7972 0.0422  0.0306  0.0309  806 MG  A MG    
6819 MN MN    . MN  J .   ? 0.9764 0.9531 0.9413 0.0214  0.0520  -0.0567 807 MN  A MN    
6820 N  N1    . IMD K .   ? 1.1501 1.1571 1.1410 -0.0445 -0.1454 0.1378  808 IMD A N1    
6821 C  C2    . IMD K .   ? 1.2175 1.2230 1.2101 -0.0394 -0.1261 0.1316  808 IMD A C2    
6822 N  N3    . IMD K .   ? 1.1200 1.1314 1.1373 -0.0374 -0.1166 0.1269  808 IMD A N3    
6823 C  C4    . IMD K .   ? 1.0873 1.1052 1.1210 -0.0409 -0.1288 0.1312  808 IMD A C4    
6824 C  C5    . IMD K .   ? 1.0257 1.0408 1.0440 -0.0460 -0.1478 0.1381  808 IMD A C5    
6825 C  C1    . GOL L .   ? 1.2819 1.1201 1.3705 0.0078  0.0663  -0.0543 101 GOL P C1    
6826 O  O1    . GOL L .   ? 1.1960 1.0302 1.2892 -0.0030 0.0587  -0.0563 101 GOL P O1    
6827 C  C2    . GOL L .   ? 1.2503 1.0890 1.3605 0.0145  0.0727  -0.0383 101 GOL P C2    
6828 O  O2    . GOL L .   ? 1.0099 0.8701 1.1273 0.0109  0.0670  -0.0226 101 GOL P O2    
6829 C  C3    . GOL L .   ? 1.0498 0.8674 1.1749 0.0128  0.0750  -0.0388 101 GOL P C3    
6830 O  O3    . GOL L .   ? 1.0617 0.8569 1.1742 0.0131  0.0770  -0.0580 101 GOL P O3    
6831 C  C1    . GOL M .   ? 1.1633 0.7795 1.5724 -0.0936 0.0447  0.0062  101 GOL T C1    
6832 O  O1    . GOL M .   ? 1.1920 0.8223 1.5669 -0.0868 0.0441  -0.0070 101 GOL T O1    
6833 C  C2    . GOL M .   ? 1.1702 0.7488 1.5863 -0.1013 0.0373  -0.0150 101 GOL T C2    
6834 O  O2    . GOL M .   ? 1.3165 0.8736 1.7069 -0.0907 0.0404  -0.0364 101 GOL T O2    
6835 C  C3    . GOL M .   ? 1.2460 0.8310 1.6618 -0.1169 0.0234  -0.0253 101 GOL T C3    
6836 O  O3    . GOL M .   ? 1.3261 0.9357 1.7108 -0.1137 0.0209  -0.0333 101 GOL T O3    
6837 O  O     . HOH N .   ? 0.7940 0.8404 0.9001 -0.0360 -0.0825 0.0793  901 HOH A O     
6838 O  O     . HOH N .   ? 0.8250 0.9455 0.8806 0.0444  0.1391  0.0518  902 HOH A O     
6839 O  O     . HOH N .   ? 0.7520 0.7347 0.6961 0.0271  0.0060  -0.0330 903 HOH A O     
6840 O  O     . HOH N .   ? 1.0996 1.1192 1.1442 -0.0395 -0.1013 0.0857  904 HOH A O     
6841 O  O     . HOH N .   ? 0.8332 0.7610 1.1012 0.0182  0.0340  0.1971  905 HOH A O     
6842 O  O     . HOH N .   ? 0.4845 0.5786 0.7691 0.0255  0.0054  0.1530  906 HOH A O     
6843 O  O     . HOH N .   ? 0.7992 0.8218 0.9329 -0.0095 -0.0445 0.1281  907 HOH A O     
6844 O  O     . HOH N .   ? 0.6869 0.6479 0.7814 -0.0168 0.0151  0.0821  908 HOH A O     
6845 O  O     . HOH O .   ? 0.8388 0.7491 0.9353 0.0212  0.0653  -0.0123 201 HOH T O     
6846 O  O     . HOH O .   ? 0.7661 0.7445 0.7693 0.0061  0.0376  -0.0409 202 HOH T O     
6847 O  O     . HOH O .   ? 1.1560 0.6317 1.3363 -0.0006 0.0869  -0.1580 203 HOH T O     
6848 O  O     . HOH O .   ? 0.6656 0.4667 0.9035 0.0152  0.0832  0.0394  204 HOH T O     
6849 O  O     . HOH O .   ? 0.8306 0.7577 0.9743 -0.0231 0.0366  0.0870  205 HOH T O     
6850 O  O     . HOH O .   ? 0.8645 0.7842 0.9192 0.0074  0.0519  -0.0365 206 HOH T O     
# 
